HEADER LYASE 27-JUL-99 1C3C TITLE T. MARITIMA ADENYLOSUCCINATE LYASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENYLOSUCCINATE LYASE; COMPND 3 CHAIN: A, B; COMPND 4 EC: 4.3.2.2; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA; SOURCE 3 ORGANISM_COMMON: BACTERIA; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PT7-7 KEYWDS PURINE BIOSYNTHESIS, LYASE EXPDTA X-RAY DIFFRACTION AUTHOR E.A.TOTH,T.O.YEATES REVDAT 1 09-FEB-00 1C3C 0 JRNL AUTH E.A.TOTH,T.O.YEATES JRNL TITL THE STRUCTURE OF ADENYLOSUCCINATE LYASE, AN ENZYME JRNL TITL 2 WITH DUAL ACTIVITY IN THE DE NOVO PURINE JRNL TITL 3 BIOSYNTHETIC PATHWAY JRNL REF STRUCTURE (LONDON) V. 8 163 2000 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 3 NUMBER OF REFLECTIONS : 117163 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.179 REMARK 3 FREE R VALUE : 0.207 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 5858 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6734 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 693 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 16.33 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.015 ; NULL REMARK 3 ANGLE DISTANCE (A) : 2.640 ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1C3C COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 7 REMARK 7 WATERS 1 TO 374 ARE ASSOCIATED WITH CHAIN A. REMARK 7 WATERS 401 TO 774 ARE ASSOCIATED WITH CHAIN B. REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-1999. REMARK 100 THE RCSB ID CODE IS RCSB009412. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-FEB-1999 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X8C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC Q-4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117163 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 49.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : 0.05900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.6700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 84.1 REMARK 200 DATA REDUNDANCY IN SHELL : 1.80 REMARK 200 R MERGE FOR SHELL (I) : 0.29500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NAACETATE, 0.5% PEG REMARK 280 4000, 6% GLYCEROL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 -X,Y,1/2-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 1/2+X,1/2+Y,Z REMARK 290 6555 1/2-X,1/2-Y,1/2+Z REMARK 290 7555 1/2-X,1/2+Y,1/2-Z REMARK 290 8555 1/2+X,1/2-Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.50000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.50000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.40450 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.37650 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 60.40450 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.37650 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.50000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.40450 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.37650 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.50000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 60.40450 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.37650 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 258 REMARK 465 GLN A 259 REMARK 465 ARG A 260 REMARK 465 GLY A 261 REMARK 465 SER A 262 REMARK 465 GLY B 258 REMARK 465 GLN B 259 REMARK 465 ARG B 260 REMARK 465 GLY B 261 REMARK 465 SER B 262 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 3 CG CD OE1 OE2 REMARK 470 GLU A 17 OE1 OE2 REMARK 470 LYS A 42 CG CD CE NZ REMARK 470 GLU A 46 CD OE1 OE2 REMARK 470 GLU A 57 CG CD OE1 OE2 REMARK 470 LYS A 61 CG CD CE NZ REMARK 470 GLU A 64 CG CD OE1 OE2 REMARK 470 LYS A 65 CG CD CE NZ REMARK 470 ASN A 67 CG OD1 ND2 REMARK 470 GLU A 115 CG CD OE1 OE2 REMARK 470 ARG A 256 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 257 CG CD CE NZ REMARK 470 LYS A 335 CG CD CE NZ REMARK 470 LYS A 343 NZ REMARK 470 ARG A 368 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 369 CG CD CE NZ REMARK 470 ARG A 377 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 387 CG CD CE NZ REMARK 470 GLU A 391 CG CD OE1 OE2 REMARK 470 GLU A 397 CG CD OE1 OE2 REMARK 470 GLU A 398 CG CD OE1 OE2 REMARK 470 LYS A 400 CG CD CE NZ REMARK 470 LYS A 401 CG CD CE NZ REMARK 470 GLU A 406 CG CD OE1 OE2 REMARK 470 GLU B 3 CG CD OE1 OE2 REMARK 470 GLU B 17 OE1 OE2 REMARK 470 LYS B 42 CG CD CE NZ REMARK 470 GLU B 46 CD OE1 OE2 REMARK 470 GLU B 57 CG CD OE1 OE2 REMARK 470 LYS B 61 CG CD CE NZ REMARK 470 GLU B 64 CG CD OE1 OE2 REMARK 470 LYS B 65 CG CD CE NZ REMARK 470 ASN B 67 CG OD1 ND2 REMARK 470 GLU B 115 CG CD OE1 OE2 REMARK 470 ARG B 256 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 257 CG CD CE NZ REMARK 470 LYS B 335 CG CD CE NZ REMARK 470 LYS B 343 NZ REMARK 470 ARG B 368 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 369 CG CD CE NZ REMARK 470 ARG B 377 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 387 CG CD CE NZ REMARK 470 GLU B 391 CG CD OE1 OE2 REMARK 470 GLU B 397 CG CD OE1 OE2 REMARK 470 GLU B 398 CG CD OE1 OE2 REMARK 470 LYS B 400 CG CD CE NZ REMARK 470 LYS B 401 CG CD CE NZ REMARK 470 GLU B 406 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OE2 GLU B 36 OE1 GLU A 410 5545 1.90 REMARK 500 OE2 GLU B 36 OE2 GLU A 410 5545 2.19 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 161 SD MET A 161 CG 0.104 REMARK 500 MET A 284 SD MET A 284 CG 0.095 REMARK 500 MET B 39 CE MET B 39 SD -0.251 REMARK 500 MET B 284 SD MET B 284 CG 0.103 REMARK 500 MET B 341 SD MET B 341 CG 0.100 REMARK 500 MET B 341 CE MET B 341 SD 0.097 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO A 9 N - CA - C ANGL. DEV. = 16.5 DEGREES REMARK 500 ARG A 21 CD - NE - CZ ANGL. DEV. = 27.0 DEGREES REMARK 500 ARG A 310 CD - NE - CZ ANGL. DEV. = 20.3 DEGREES REMARK 500 LEU A 408 CD1 - CG - CD2 ANGL. DEV. =-16.1 DEGREES REMARK 500 ASP A 422 CB - CG - OD2 ANGL. DEV. = 17.0 DEGREES REMARK 500 GLU A 429 CA - C - N ANGL. DEV. = 15.7 DEGREES REMARK 500 GLU A 429 O - C - N ANGL. DEV. =-16.5 DEGREES REMARK 500 LYS A 430 C - N - CA ANGL. DEV. = 34.8 DEGREES REMARK 500 ARG B 21 CD - NE - CZ ANGL. DEV. = 22.6 DEGREES REMARK 500 ARG B 310 CD - NE - CZ ANGL. DEV. = 22.7 DEGREES REMARK 500 GLU B 386 OE1 - CD - OE2 ANGL. DEV. = 15.4 DEGREES REMARK 500 LEU B 408 CD1 - CG - CD2 ANGL. DEV. =-15.6 DEGREES REMARK 500 LYS B 430 C - N - CA ANGL. DEV. = 22.6 DEGREES REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER A 8 PRO A 9 -67.34 REMARK 500 GLU A 429 LYS A 430 141.08 REMARK 500 SER B 8 PRO B 9 -88.17 DBREF 1C3C A 2 430 GB 4981640 AAD36171 2 430 DBREF 1C3C B 2 430 GB 4981640 AAD36171 2 430 SEQRES 1 A 429 VAL GLU ARG TYR SER LEU SER PRO MET LYS ASP LEU TRP SEQRES 2 A 429 THR GLU GLU ALA LYS TYR ARG ARG TRP LEU GLU VAL GLU SEQRES 3 A 429 LEU ALA VAL THR ARG ALA TYR GLU GLU LEU GLY MET ILE SEQRES 4 A 429 PRO LYS GLY VAL THR GLU ARG ILE ARG ASN ASN ALA LYS SEQRES 5 A 429 ILE ASP VAL GLU LEU PHE LYS LYS ILE GLU GLU LYS THR SEQRES 6 A 429 ASN HIS ASP VAL VAL ALA PHE VAL GLU GLY ILE GLY SER SEQRES 7 A 429 MET ILE GLY GLU ASP SER ARG PHE PHE HIS TYR GLY LEU SEQRES 8 A 429 THR SER SER ASP VAL LEU ASP THR ALA ASN SER LEU ALA SEQRES 9 A 429 LEU VAL GLU ALA GLY LYS ILE LEU LEU GLU SER LEU LYS SEQRES 10 A 429 GLU PHE CYS ASP VAL LEU TRP GLU VAL ALA ASN ARG TYR SEQRES 11 A 429 LYS HIS THR PRO THR ILE GLY ARG THR HIS GLY VAL HIS SEQRES 12 A 429 ALA GLU PRO THR SER PHE GLY LEU LYS VAL LEU GLY TRP SEQRES 13 A 429 TYR SER GLU MET LYS ARG ASN VAL GLN ARG LEU GLU ARG SEQRES 14 A 429 ALA ILE GLU GLU VAL SER TYR GLY LYS ILE SER GLY ALA SEQRES 15 A 429 VAL GLY ASN TYR ALA ASN VAL PRO PRO GLU VAL GLU GLU SEQRES 16 A 429 LYS ALA LEU SER TYR LEU GLY LEU LYS PRO GLU PRO VAL SEQRES 17 A 429 SER THR GLN VAL VAL PRO ARG ASP ARG HIS ALA PHE TYR SEQRES 18 A 429 LEU SER THR LEU ALA ILE VAL ALA ALA GLY ILE GLU ARG SEQRES 19 A 429 ILE ALA VAL GLU ILE ARG HIS LEU GLN ARG THR GLU VAL SEQRES 20 A 429 LEU GLU VAL GLU GLU PRO PHE ARG LYS GLY GLN ARG GLY SEQRES 21 A 429 SER SER ALA MET PRO HIS LYS LYS ASN PRO ILE THR CYS SEQRES 22 A 429 GLU ARG LEU THR GLY LEU SER ARG MET MET ARG ALA TYR SEQRES 23 A 429 VAL ASP PRO SER LEU GLU ASN ILE ALA LEU TRP HIS GLU SEQRES 24 A 429 ARG ASP ILE SER HIS SER SER VAL GLU ARG TYR VAL PHE SEQRES 25 A 429 PRO ASP ALA THR GLN THR LEU TYR TYR MET ILE VAL THR SEQRES 26 A 429 ALA THR ASN VAL VAL ARG ASN MET LYS VAL ASN GLU GLU SEQRES 27 A 429 ARG MET LYS LYS ASN ILE ASP LEU THR LYS GLY LEU VAL SEQRES 28 A 429 PHE SER GLN ARG VAL LEU LEU LYS LEU ILE GLU LYS GLY SEQRES 29 A 429 LEU THR ARG LYS GLU ALA TYR ASP ILE VAL GLN ARG ASN SEQRES 30 A 429 ALA LEU LYS THR TRP ASN SER GLU LYS HIS PHE LEU GLU SEQRES 31 A 429 TYR LEU LEU GLU ASP GLU GLU VAL LYS LYS LEU VAL THR SEQRES 32 A 429 LYS GLU GLU LEU GLU GLU LEU PHE ASP ILE SER TYR TYR SEQRES 33 A 429 LEU LYS HIS VAL ASP HIS ILE PHE GLU ARG PHE GLU LYS SEQRES 1 B 429 VAL GLU ARG TYR SER LEU SER PRO MET LYS ASP LEU TRP SEQRES 2 B 429 THR GLU GLU ALA LYS TYR ARG ARG TRP LEU GLU VAL GLU SEQRES 3 B 429 LEU ALA VAL THR ARG ALA TYR GLU GLU LEU GLY MET ILE SEQRES 4 B 429 PRO LYS GLY VAL THR GLU ARG ILE ARG ASN ASN ALA LYS SEQRES 5 B 429 ILE ASP VAL GLU LEU PHE LYS LYS ILE GLU GLU LYS THR SEQRES 6 B 429 ASN HIS ASP VAL VAL ALA PHE VAL GLU GLY ILE GLY SER SEQRES 7 B 429 MET ILE GLY GLU ASP SER ARG PHE PHE HIS TYR GLY LEU SEQRES 8 B 429 THR SER SER ASP VAL LEU ASP THR ALA ASN SER LEU ALA SEQRES 9 B 429 LEU VAL GLU ALA GLY LYS ILE LEU LEU GLU SER LEU LYS SEQRES 10 B 429 GLU PHE CYS ASP VAL LEU TRP GLU VAL ALA ASN ARG TYR SEQRES 11 B 429 LYS HIS THR PRO THR ILE GLY ARG THR HIS GLY VAL HIS SEQRES 12 B 429 ALA GLU PRO THR SER PHE GLY LEU LYS VAL LEU GLY TRP SEQRES 13 B 429 TYR SER GLU MET LYS ARG ASN VAL GLN ARG LEU GLU ARG SEQRES 14 B 429 ALA ILE GLU GLU VAL SER TYR GLY LYS ILE SER GLY ALA SEQRES 15 B 429 VAL GLY ASN TYR ALA ASN VAL PRO PRO GLU VAL GLU GLU SEQRES 16 B 429 LYS ALA LEU SER TYR LEU GLY LEU LYS PRO GLU PRO VAL SEQRES 17 B 429 SER THR GLN VAL VAL PRO ARG ASP ARG HIS ALA PHE TYR SEQRES 18 B 429 LEU SER THR LEU ALA ILE VAL ALA ALA GLY ILE GLU ARG SEQRES 19 B 429 ILE ALA VAL GLU ILE ARG HIS LEU GLN ARG THR GLU VAL SEQRES 20 B 429 LEU GLU VAL GLU GLU PRO PHE ARG LYS GLY GLN ARG GLY SEQRES 21 B 429 SER SER ALA MET PRO HIS LYS LYS ASN PRO ILE THR CYS SEQRES 22 B 429 GLU ARG LEU THR GLY LEU SER ARG MET MET ARG ALA TYR SEQRES 23 B 429 VAL ASP PRO SER LEU GLU ASN ILE ALA LEU TRP HIS GLU SEQRES 24 B 429 ARG ASP ILE SER HIS SER SER VAL GLU ARG TYR VAL PHE SEQRES 25 B 429 PRO ASP ALA THR GLN THR LEU TYR TYR MET ILE VAL THR SEQRES 26 B 429 ALA THR ASN VAL VAL ARG ASN MET LYS VAL ASN GLU GLU SEQRES 27 B 429 ARG MET LYS LYS ASN ILE ASP LEU THR LYS GLY LEU VAL SEQRES 28 B 429 PHE SER GLN ARG VAL LEU LEU LYS LEU ILE GLU LYS GLY SEQRES 29 B 429 LEU THR ARG LYS GLU ALA TYR ASP ILE VAL GLN ARG ASN SEQRES 30 B 429 ALA LEU LYS THR TRP ASN SER GLU LYS HIS PHE LEU GLU SEQRES 31 B 429 TYR LEU LEU GLU ASP GLU GLU VAL LYS LYS LEU VAL THR SEQRES 32 B 429 LYS GLU GLU LEU GLU GLU LEU PHE ASP ILE SER TYR TYR SEQRES 33 B 429 LEU LYS HIS VAL ASP HIS ILE PHE GLU ARG PHE GLU LYS FORMUL 3 HOH *693(H2 O1) HELIX 1 1 VAL A 2 SER A 6 5 5 HELIX 2 2 PRO A 9 TRP A 14 1 6 HELIX 3 3 THR A 15 LEU A 37 1 23 HELIX 4 4 GLY A 43 ALA A 52 1 10 HELIX 5 5 ASP A 55 ASN A 67 1 13 HELIX 6 6 HIS A 68 GLY A 82 1 15 HELIX 7 7 GLU A 83 PHE A 88 5 6 HELIX 8 8 THR A 93 TYR A 131 1 39 HELIX 9 9 PHE A 150 VAL A 175 1 26 HELIX 10 10 PRO A 191 LEU A 202 1 12 HELIX 11 11 ARG A 216 GLN A 244 1 29 HELIX 12 12 PRO A 271 TYR A 287 1 17 HELIX 13 13 TYR A 287 ASN A 294 1 8 HELIX 14 14 ILE A 303 MET A 334 1 32 HELIX 15 15 ASN A 337 ASP A 346 1 10 HELIX 16 16 GLY A 350 VAL A 352 5 3 HELIX 17 17 PHE A 353 LYS A 364 1 12 HELIX 18 18 THR A 367 ASN A 384 1 18 HELIX 19 19 HIS A 388 GLU A 395 1 8 HELIX 20 20 ASP A 396 LYS A 401 1 6 HELIX 21 21 THR A 404 LEU A 411 1 8 HELIX 22 22 ILE A 414 LYS A 419 1 6 HELIX 23 23 HIS A 420 ARG A 427 1 8 HELIX 24 24 VAL B 2 SER B 6 5 5 HELIX 25 25 PRO B 9 TRP B 14 1 6 HELIX 26 26 THR B 15 LEU B 37 1 23 HELIX 27 27 GLY B 43 ALA B 52 1 10 HELIX 28 28 ASP B 55 ASN B 67 1 13 HELIX 29 29 HIS B 68 GLY B 82 1 15 HELIX 30 30 GLU B 83 PHE B 88 5 6 HELIX 31 31 THR B 93 TYR B 131 1 39 HELIX 32 32 PHE B 150 VAL B 175 1 26 HELIX 33 33 PRO B 191 LEU B 202 1 12 HELIX 34 34 ARG B 216 GLN B 244 1 29 HELIX 35 35 PRO B 271 TYR B 287 1 17 HELIX 36 36 TYR B 287 ASN B 294 1 8 HELIX 37 37 ILE B 303 MET B 334 1 32 HELIX 38 38 ASN B 337 ASP B 346 1 10 HELIX 39 39 GLY B 350 VAL B 352 5 3 HELIX 40 40 PHE B 353 LYS B 364 1 12 HELIX 41 41 THR B 367 ASN B 384 1 18 HELIX 42 42 HIS B 388 GLU B 395 1 8 HELIX 43 43 ASP B 396 LYS B 401 1 6 HELIX 44 44 THR B 404 LEU B 411 1 8 HELIX 45 45 ILE B 414 LYS B 419 1 6 HELIX 46 46 HIS B 420 ARG B 427 1 8 SHEET 1 A 2 PRO A 135 THR A 140 0 SHEET 2 A 2 VAL A 143 SER A 149 -1 O VAL A 143 N THR A 140 SHEET 1 B 2 TYR A 177 GLY A 178 0 SHEET 2 B 2 LYS A 205 PRO A 206 1 O LYS A 205 N GLY A 178 SHEET 1 C 2 VAL A 251 GLU A 252 0 SHEET 2 C 2 LYS A 335 VAL A 336 -1 N LYS A 335 O GLU A 252 SHEET 1 D 2 PRO B 135 THR B 140 0 SHEET 2 D 2 VAL B 143 SER B 149 -1 O VAL B 143 N THR B 140 SHEET 1 E 2 TYR B 177 GLY B 178 0 SHEET 2 E 2 LYS B 205 PRO B 206 1 O LYS B 205 N GLY B 178 SHEET 1 F 2 VAL B 251 GLU B 252 0 SHEET 2 F 2 LYS B 335 VAL B 336 -1 N LYS B 335 O GLU B 252 CRYST1 120.809 126.753 169.000 90.00 90.00 90.00 C 2 2 21 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008280 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007890 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005920 0.00000 ATOM 1 N VAL A 2 22.440 5.934 19.298 1.00 35.11 N ANISOU 1 N VAL A 2 4392 4435 4512 -59 40 -92 N ATOM 2 CA VAL A 2 23.177 7.187 19.668 1.00 34.60 C ANISOU 2 CA VAL A 2 4430 4332 4385 -15 31 -10 C ATOM 3 C VAL A 2 22.291 8.027 20.578 1.00 35.24 C ANISOU 3 C VAL A 2 4469 4479 4441 24 41 -18 C ATOM 4 O VAL A 2 21.432 8.778 20.121 1.00 36.28 O ANISOU 4 O VAL A 2 4626 4535 4622 49 -35 87 O ATOM 5 CB VAL A 2 23.681 7.954 18.445 1.00 34.01 C ANISOU 5 CB VAL A 2 4315 4257 4349 -8 41 -84 C ATOM 6 CG1 VAL A 2 24.221 9.336 18.789 1.00 33.79 C ANISOU 6 CG1 VAL A 2 4244 4274 4319 -71 38 -74 C ATOM 7 CG2 VAL A 2 24.787 7.171 17.735 1.00 34.25 C ANISOU 7 CG2 VAL A 2 4302 4294 4417 11 65 -52 C ATOM 8 N GLU A 3 22.532 7.963 21.898 1.00 35.66 N ANISOU 8 N GLU A 3 4525 4588 4436 -21 39 -22 N ATOM 9 CA GLU A 3 21.621 8.455 22.919 1.00 35.76 C ANISOU 9 CA GLU A 3 4569 4559 4458 66 0 -32 C ATOM 10 C GLU A 3 21.234 9.897 22.639 1.00 35.77 C ANISOU 10 C GLU A 3 4507 4551 4533 -2 52 32 C ATOM 11 O GLU A 3 20.107 10.398 22.776 1.00 36.39 O ANISOU 11 O GLU A 3 4501 4691 4633 92 -33 111 O ATOM 12 CB GLU A 3 22.254 8.397 24.313 1.00 36.67 C ANISOU 12 CB GLU A 3 4637 4806 4489 21 -43 11 C ATOM 13 N ARG A 4 22.246 10.637 22.161 1.00 35.76 N ANISOU 13 N ARG A 4 4513 4519 4553 -37 12 30 N ATOM 14 CA ARG A 4 22.024 12.027 21.770 1.00 35.53 C ANISOU 14 CA ARG A 4 4432 4531 4536 -39 -23 57 C ATOM 15 C ARG A 4 20.867 12.201 20.800 1.00 35.30 C ANISOU 15 C ARG A 4 4460 4500 4451 -40 -23 -10 C ATOM 16 O ARG A 4 20.303 13.334 20.875 1.00 36.51 O ANISOU 16 O ARG A 4 4651 4601 4622 62 -3 -7 O ATOM 17 CB ARG A 4 23.292 12.748 21.320 1.00 36.27 C ANISOU 17 CB ARG A 4 4504 4653 4623 -86 37 47 C ATOM 18 CG ARG A 4 23.551 13.029 19.866 1.00 36.90 C ANISOU 18 CG ARG A 4 4628 4754 4641 -84 53 29 C ATOM 19 CD ARG A 4 24.865 13.728 19.577 1.00 37.36 C ANISOU 19 CD ARG A 4 4751 4674 4769 -187 8 -37 C ATOM 20 NE ARG A 4 25.471 14.539 20.616 1.00 38.73 N ANISOU 20 NE ARG A 4 5132 4722 4862 -131 -102 -74 N ATOM 21 CZ ARG A 4 25.647 15.861 20.461 1.00 39.40 C ANISOU 21 CZ ARG A 4 5307 4780 4883 -136 -148 -22 C ATOM 22 NH1 ARG A 4 25.252 16.439 19.311 1.00 40.66 N ANISOU 22 NH1 ARG A 4 5396 5153 4900 -6 -126 70 N ATOM 23 NH2 ARG A 4 26.210 16.622 21.403 1.00 39.91 N ANISOU 23 NH2 ARG A 4 5239 5001 4922 -175 -159 -119 N ATOM 24 N TYR A 5 20.418 11.306 19.942 1.00 34.15 N ANISOU 24 N TYR A 5 4253 4307 4417 -64 23 35 N ATOM 25 CA TYR A 5 19.209 11.554 19.141 1.00 34.36 C ANISOU 25 CA TYR A 5 4308 4374 4374 1 -1 57 C ATOM 26 C TYR A 5 17.979 10.865 19.719 1.00 34.89 C ANISOU 26 C TYR A 5 4331 4387 4537 -44 -14 68 C ATOM 27 O TYR A 5 16.933 10.822 19.087 1.00 35.37 O ANISOU 27 O TYR A 5 4466 4405 4569 -75 -114 153 O ATOM 28 CB TYR A 5 19.443 11.147 17.669 1.00 33.72 C ANISOU 28 CB TYR A 5 4185 4281 4346 -10 -22 73 C ATOM 29 CG TYR A 5 20.730 11.755 17.133 1.00 33.39 C ANISOU 29 CG TYR A 5 4174 4220 4293 -3 -17 36 C ATOM 30 CD1 TYR A 5 21.754 10.973 16.628 1.00 33.50 C ANISOU 30 CD1 TYR A 5 4245 4275 4207 -34 64 -10 C ATOM 31 CD2 TYR A 5 20.932 13.135 17.213 1.00 33.09 C ANISOU 31 CD2 TYR A 5 4112 4179 4282 16 -4 105 C ATOM 32 CE1 TYR A 5 22.951 11.551 16.201 1.00 32.87 C ANISOU 32 CE1 TYR A 5 4280 4108 4100 -71 42 -44 C ATOM 33 CE2 TYR A 5 22.109 13.708 16.773 1.00 32.58 C ANISOU 33 CE2 TYR A 5 4154 4042 4183 35 42 124 C ATOM 34 CZ TYR A 5 23.110 12.915 16.257 1.00 32.30 C ANISOU 34 CZ TYR A 5 4155 4067 4052 -18 82 50 C ATOM 35 OH TYR A 5 24.294 13.504 15.838 1.00 30.89 O ANISOU 35 OH TYR A 5 4176 3733 3830 59 111 -36 O ATOM 36 N SER A 6 18.023 10.334 20.938 1.00 35.57 N ANISOU 36 N SER A 6 4504 4496 4516 11 53 14 N ATOM 37 CA SER A 6 16.870 9.593 21.465 1.00 36.67 C ANISOU 37 CA SER A 6 4491 4717 4723 -21 78 -3 C ATOM 38 C SER A 6 15.923 10.546 22.187 1.00 35.92 C ANISOU 38 C SER A 6 4393 4630 4626 -68 7 -30 C ATOM 39 O SER A 6 16.353 11.445 22.899 1.00 36.60 O ANISOU 39 O SER A 6 4476 4738 4690 -131 10 -104 O ATOM 40 CB SER A 6 17.329 8.504 22.443 1.00 38.50 C ANISOU 40 CB SER A 6 4840 4912 4875 -9 9 112 C ATOM 41 OG SER A 6 17.878 9.213 23.565 1.00 40.60 O ANISOU 41 OG SER A 6 5223 5221 4982 -58 -16 -29 O ATOM 42 N LEU A 7 14.614 10.363 22.002 1.00 33.74 N ANISOU 42 N LEU A 7 4274 4235 4309 24 90 -45 N ATOM 43 CA LEU A 7 13.559 11.216 22.487 1.00 31.04 C ANISOU 43 CA LEU A 7 3968 3895 3933 -158 37 75 C ATOM 44 C LEU A 7 12.419 10.312 22.995 1.00 29.33 C ANISOU 44 C LEU A 7 3835 3610 3698 -65 -30 -87 C ATOM 45 O LEU A 7 11.993 9.382 22.332 1.00 25.60 O ANISOU 45 O LEU A 7 3463 3174 3089 -119 48 176 O ATOM 46 CB LEU A 7 12.913 12.090 21.414 1.00 30.90 C ANISOU 46 CB LEU A 7 3890 3892 3960 -121 -22 24 C ATOM 47 CG LEU A 7 13.773 13.083 20.630 1.00 31.05 C ANISOU 47 CG LEU A 7 3929 3954 3916 -107 -20 94 C ATOM 48 CD1 LEU A 7 12.988 13.773 19.521 1.00 29.76 C ANISOU 48 CD1 LEU A 7 3760 3824 3725 -97 71 9 C ATOM 49 CD2 LEU A 7 14.319 14.120 21.625 1.00 31.51 C ANISOU 49 CD2 LEU A 7 4039 3978 3954 -91 -18 40 C ATOM 50 N SER A 8 11.934 10.681 24.188 1.00 30.44 N ANISOU 50 N SER A 8 3998 3826 3741 44 37 -43 N ATOM 51 CA SER A 8 10.670 10.068 24.659 1.00 31.57 C ANISOU 51 CA SER A 8 4067 3996 3932 -34 93 -22 C ATOM 52 C SER A 8 9.582 10.164 23.624 1.00 33.11 C ANISOU 52 C SER A 8 4225 4295 4059 -68 19 -47 C ATOM 53 O SER A 8 9.747 11.191 23.012 1.00 36.18 O ANISOU 53 O SER A 8 4757 4493 4495 -34 -18 150 O ATOM 54 CB SER A 8 10.395 10.523 26.089 1.00 32.08 C ANISOU 54 CB SER A 8 4236 4045 3910 -10 -8 -60 C ATOM 55 OG SER A 8 11.394 9.842 26.889 1.00 31.94 O ANISOU 55 OG SER A 8 4259 4090 3787 -47 -62 -229 O ATOM 56 N PRO A 9 8.499 9.428 23.855 1.00 32.30 N ANISOU 56 N PRO A 9 4107 4057 4109 22 34 -137 N ATOM 57 CA PRO A 9 8.168 8.048 23.904 1.00 29.84 C ANISOU 57 CA PRO A 9 3777 3836 3726 152 31 -100 C ATOM 58 C PRO A 9 8.889 6.885 23.249 1.00 25.85 C ANISOU 58 C PRO A 9 3278 3428 3115 -29 60 103 C ATOM 59 O PRO A 9 8.899 5.773 23.741 1.00 25.37 O ANISOU 59 O PRO A 9 3323 3365 2953 3 204 17 O ATOM 60 CB PRO A 9 6.669 7.840 23.601 1.00 31.64 C ANISOU 60 CB PRO A 9 3839 4073 4110 77 3 -32 C ATOM 61 CG PRO A 9 6.400 8.997 22.683 1.00 32.91 C ANISOU 61 CG PRO A 9 4210 4092 4203 112 -39 -8 C ATOM 62 CD PRO A 9 7.148 9.994 23.560 1.00 33.71 C ANISOU 62 CD PRO A 9 4196 4260 4351 84 -81 -63 C ATOM 63 N MET A 10 9.514 7.344 22.174 1.00 21.95 N ANISOU 63 N MET A 10 2890 2675 2777 89 -104 -86 N ATOM 64 CA MET A 10 10.163 6.364 21.317 1.00 19.15 C ANISOU 64 CA MET A 10 2538 2462 2279 -120 31 75 C ATOM 65 C MET A 10 11.292 5.723 22.104 1.00 20.23 C ANISOU 65 C MET A 10 2748 2477 2460 -55 -50 73 C ATOM 66 O MET A 10 11.452 4.494 22.024 1.00 20.21 O ANISOU 66 O MET A 10 2779 2494 2407 -7 31 3 O ATOM 67 CB MET A 10 10.663 7.023 20.019 1.00 15.62 C ANISOU 67 CB MET A 10 2231 1595 2110 -190 -56 -196 C ATOM 68 CG MET A 10 11.157 5.911 19.069 1.00 12.64 C ANISOU 68 CG MET A 10 1558 1410 1835 -101 85 150 C ATOM 69 SD MET A 10 9.864 4.727 18.523 1.00 6.98 S ANISOU 69 SD MET A 10 765 494 1391 43 229 514 S ATOM 70 CE MET A 10 9.238 5.728 17.126 1.00 10.65 C ANISOU 70 CE MET A 10 1249 869 1929 110 89 129 C ATOM 71 N LYS A 11 12.102 6.490 22.858 1.00 21.05 N ANISOU 71 N LYS A 11 2859 2584 2553 -178 -57 80 N ATOM 72 CA LYS A 11 13.233 5.785 23.487 1.00 22.56 C ANISOU 72 CA LYS A 11 2960 2802 2809 -19 -3 126 C ATOM 73 C LYS A 11 12.729 4.820 24.567 1.00 21.08 C ANISOU 73 C LYS A 11 2766 2604 2638 -118 -106 -30 C ATOM 74 O LYS A 11 13.365 3.768 24.747 1.00 20.64 O ANISOU 74 O LYS A 11 2778 2485 2580 -268 -154 139 O ATOM 75 CB LYS A 11 14.280 6.729 24.036 1.00 26.32 C ANISOU 75 CB LYS A 11 3270 3224 3507 -229 -126 32 C ATOM 76 CG LYS A 11 13.861 7.446 25.317 1.00 31.16 C ANISOU 76 CG LYS A 11 4126 3962 3750 23 60 -113 C ATOM 77 CD LYS A 11 15.057 8.362 25.658 1.00 35.39 C ANISOU 77 CD LYS A 11 4392 4496 4559 -231 -65 -48 C ATOM 78 CE LYS A 11 14.612 9.463 26.603 1.00 38.42 C ANISOU 78 CE LYS A 11 4905 4809 4885 19 54 -141 C ATOM 79 NZ LYS A 11 14.235 8.879 27.917 1.00 41.18 N ANISOU 79 NZ LYS A 11 5336 5241 5071 -15 59 79 N ATOM 80 N ASP A 12 11.611 5.110 25.196 1.00 19.79 N ANISOU 80 N ASP A 12 2801 2310 2407 -157 -103 -124 N ATOM 81 CA ASP A 12 11.055 4.214 26.218 1.00 21.61 C ANISOU 81 CA ASP A 12 3160 2469 2583 -244 -74 -47 C ATOM 82 C ASP A 12 10.650 2.840 25.674 1.00 19.50 C ANISOU 82 C ASP A 12 2847 2352 2209 -76 -54 14 C ATOM 83 O ASP A 12 10.628 1.845 26.384 1.00 18.19 O ANISOU 83 O ASP A 12 2881 2256 1774 -124 -47 -137 O ATOM 84 CB ASP A 12 9.836 4.888 26.839 1.00 25.75 C ANISOU 84 CB ASP A 12 3369 3190 3225 59 44 16 C ATOM 85 CG ASP A 12 10.320 6.241 27.385 1.00 31.01 C ANISOU 85 CG ASP A 12 4272 3564 3947 -97 -119 -202 C ATOM 86 OD1 ASP A 12 10.152 7.277 26.702 1.00 33.27 O ANISOU 86 OD1 ASP A 12 4610 3728 4305 55 -70 -48 O ATOM 87 OD2 ASP A 12 10.949 6.181 28.456 1.00 33.08 O ANISOU 87 OD2 ASP A 12 4701 3946 3920 -39 -185 -168 O ATOM 88 N LEU A 13 10.347 2.764 24.374 1.00 17.21 N ANISOU 88 N LEU A 13 2343 2075 2120 -134 -12 -75 N ATOM 89 CA LEU A 13 9.980 1.503 23.753 1.00 16.03 C ANISOU 89 CA LEU A 13 2134 2032 1925 -103 -54 -18 C ATOM 90 C LEU A 13 11.129 0.533 23.687 1.00 14.84 C ANISOU 90 C LEU A 13 2023 1905 1709 -197 -53 75 C ATOM 91 O LEU A 13 10.890 -0.686 23.595 1.00 14.60 O ANISOU 91 O LEU A 13 1954 1865 1729 -159 -2 120 O ATOM 92 CB LEU A 13 9.594 1.855 22.312 1.00 18.13 C ANISOU 92 CB LEU A 13 2550 2317 2022 -139 -75 102 C ATOM 93 CG LEU A 13 8.849 0.852 21.462 1.00 19.65 C ANISOU 93 CG LEU A 13 2637 2574 2254 -210 -140 78 C ATOM 94 CD1 LEU A 13 7.635 0.316 22.238 1.00 20.35 C ANISOU 94 CD1 LEU A 13 2685 2649 2398 -249 -67 178 C ATOM 95 CD2 LEU A 13 8.354 1.552 20.180 1.00 19.58 C ANISOU 95 CD2 LEU A 13 2742 2597 2101 -206 -176 38 C ATOM 96 N TRP A 14 12.381 0.999 23.579 1.00 13.74 N ANISOU 96 N TRP A 14 1950 1770 1500 -182 -101 79 N ATOM 97 CA TRP A 14 13.501 0.158 23.252 1.00 15.04 C ANISOU 97 CA TRP A 14 1977 2043 1693 -115 39 138 C ATOM 98 C TRP A 14 14.407 -0.103 24.460 1.00 16.64 C ANISOU 98 C TRP A 14 2164 2333 1825 -90 -51 81 C ATOM 99 O TRP A 14 15.544 -0.528 24.250 1.00 19.56 O ANISOU 99 O TRP A 14 2320 3014 2096 159 -34 180 O ATOM 100 CB TRP A 14 14.317 0.763 22.064 1.00 14.35 C ANISOU 100 CB TRP A 14 1928 2012 1514 -102 -20 84 C ATOM 101 CG TRP A 14 13.453 0.829 20.821 1.00 13.64 C ANISOU 101 CG TRP A 14 1835 1829 1518 -70 24 80 C ATOM 102 CD1 TRP A 14 12.984 1.975 20.226 1.00 13.39 C ANISOU 102 CD1 TRP A 14 1766 1865 1456 -66 45 68 C ATOM 103 CD2 TRP A 14 12.949 -0.267 20.062 1.00 13.24 C ANISOU 103 CD2 TRP A 14 1716 1813 1503 -81 76 72 C ATOM 104 NE1 TRP A 14 12.223 1.623 19.117 1.00 12.92 N ANISOU 104 NE1 TRP A 14 1668 1736 1505 -118 63 17 N ATOM 105 CE2 TRP A 14 12.192 0.265 19.004 1.00 13.15 C ANISOU 105 CE2 TRP A 14 1718 1717 1560 -16 55 31 C ATOM 106 CE3 TRP A 14 13.097 -1.662 20.138 1.00 13.30 C ANISOU 106 CE3 TRP A 14 1618 1803 1632 -73 92 15 C ATOM 107 CZ2 TRP A 14 11.559 -0.551 18.053 1.00 12.92 C ANISOU 107 CZ2 TRP A 14 1605 1660 1645 -144 40 95 C ATOM 108 CZ3 TRP A 14 12.459 -2.481 19.207 1.00 12.88 C ANISOU 108 CZ3 TRP A 14 1581 1817 1494 -24 116 27 C ATOM 109 CH2 TRP A 14 11.709 -1.914 18.157 1.00 12.30 C ANISOU 109 CH2 TRP A 14 1308 1715 1648 39 151 26 C ATOM 110 N THR A 15 13.937 -0.028 25.694 1.00 15.16 N ANISOU 110 N THR A 15 1918 2018 1823 -250 26 104 N ATOM 111 CA THR A 15 14.758 -0.476 26.824 1.00 16.42 C ANISOU 111 CA THR A 15 2049 2188 2004 -156 -56 47 C ATOM 112 C THR A 15 14.649 -1.970 27.052 1.00 17.28 C ANISOU 112 C THR A 15 2216 2197 2153 -107 -85 74 C ATOM 113 O THR A 15 13.724 -2.660 26.556 1.00 16.49 O ANISOU 113 O THR A 15 2234 2112 1921 -131 -150 181 O ATOM 114 CB THR A 15 14.251 0.248 28.105 1.00 16.80 C ANISOU 114 CB THR A 15 2081 2268 2034 -123 -15 -7 C ATOM 115 OG1 THR A 15 12.861 -0.173 28.290 1.00 15.75 O ANISOU 115 OG1 THR A 15 2096 2256 1634 -252 -67 -45 O ATOM 116 CG2 THR A 15 14.309 1.761 27.935 1.00 18.19 C ANISOU 116 CG2 THR A 15 2408 2341 2161 -175 -124 42 C ATOM 117 N GLU A 16 15.567 -2.527 27.851 1.00 18.09 N ANISOU 117 N GLU A 16 2228 2412 2233 -78 -110 92 N ATOM 118 CA GLU A 16 15.454 -3.943 28.220 1.00 19.70 C ANISOU 118 CA GLU A 16 2589 2441 2455 -63 -30 106 C ATOM 119 C GLU A 16 14.177 -4.221 28.985 1.00 18.19 C ANISOU 119 C GLU A 16 2458 2284 2171 -41 -161 84 C ATOM 120 O GLU A 16 13.509 -5.248 28.746 1.00 16.27 O ANISOU 120 O GLU A 16 2339 2228 1614 -37 -122 114 O ATOM 121 CB GLU A 16 16.684 -4.336 29.080 1.00 23.53 C ANISOU 121 CB GLU A 16 2927 2965 3049 -9 -354 113 C ATOM 122 CG GLU A 16 17.938 -4.232 28.221 1.00 29.50 C ANISOU 122 CG GLU A 16 3473 4008 3729 -60 55 152 C ATOM 123 CD GLU A 16 18.297 -5.516 27.527 1.00 34.89 C ANISOU 123 CD GLU A 16 4471 4279 4506 30 23 -81 C ATOM 124 OE1 GLU A 16 17.481 -6.355 27.097 1.00 36.14 O ANISOU 124 OE1 GLU A 16 4363 4669 4701 -40 -98 -48 O ATOM 125 OE2 GLU A 16 19.533 -5.759 27.429 1.00 38.89 O ANISOU 125 OE2 GLU A 16 4615 4997 5166 70 62 15 O ATOM 126 N GLU A 17 13.792 -3.292 29.875 1.00 17.76 N ANISOU 126 N GLU A 17 2347 2257 2143 -69 -123 82 N ATOM 127 CA GLU A 17 12.555 -3.473 30.631 1.00 19.24 C ANISOU 127 CA GLU A 17 2369 2582 2360 -84 -115 179 C ATOM 128 C GLU A 17 11.369 -3.591 29.672 1.00 17.33 C ANISOU 128 C GLU A 17 2387 2193 2006 -166 -28 116 C ATOM 129 O GLU A 17 10.470 -4.431 29.829 1.00 15.95 O ANISOU 129 O GLU A 17 2330 2155 1574 -187 -136 96 O ATOM 130 CB GLU A 17 12.347 -2.303 31.592 1.00 22.94 C ANISOU 130 CB GLU A 17 3107 2855 2752 -71 -19 -61 C ATOM 131 CG GLU A 17 11.058 -2.356 32.406 1.00 28.00 C ANISOU 131 CG GLU A 17 3330 3735 3573 -49 150 -48 C ATOM 132 CD GLU A 17 10.900 -1.111 33.312 1.00 30.82 C ANISOU 132 CD GLU A 17 4019 3840 3851 22 56 -169 C ATOM 133 N ALA A 18 11.339 -2.711 28.660 1.00 14.51 N ANISOU 133 N ALA A 18 1891 1859 1762 -115 -16 -6 N ATOM 134 CA ALA A 18 10.232 -2.708 27.711 1.00 14.62 C ANISOU 134 CA ALA A 18 2131 1732 1692 -151 -82 61 C ATOM 135 C ALA A 18 10.195 -4.016 26.939 1.00 13.47 C ANISOU 135 C ALA A 18 1829 1703 1585 -73 -7 90 C ATOM 136 O ALA A 18 9.112 -4.554 26.652 1.00 13.49 O ANISOU 136 O ALA A 18 1867 1773 1488 -109 -60 32 O ATOM 137 CB ALA A 18 10.341 -1.534 26.708 1.00 14.34 C ANISOU 137 CB ALA A 18 2027 1604 1819 -109 -26 44 C ATOM 138 N LYS A 19 11.355 -4.531 26.559 1.00 12.85 N ANISOU 138 N LYS A 19 1718 1667 1500 -132 -97 52 N ATOM 139 CA LYS A 19 11.385 -5.794 25.820 1.00 13.31 C ANISOU 139 CA LYS A 19 1875 1557 1626 -114 -58 106 C ATOM 140 C LYS A 19 10.783 -6.929 26.650 1.00 13.20 C ANISOU 140 C LYS A 19 1769 1666 1579 -178 -98 85 C ATOM 141 O LYS A 19 9.938 -7.699 26.173 1.00 12.20 O ANISOU 141 O LYS A 19 1789 1531 1315 -255 -112 59 O ATOM 142 CB LYS A 19 12.833 -6.142 25.487 1.00 15.36 C ANISOU 142 CB LYS A 19 1920 1973 1944 -115 31 102 C ATOM 143 CG LYS A 19 12.981 -7.434 24.717 1.00 18.28 C ANISOU 143 CG LYS A 19 2603 2127 2216 -117 -43 -66 C ATOM 144 CD LYS A 19 14.388 -7.909 24.502 1.00 22.62 C ANISOU 144 CD LYS A 19 2873 2729 2991 32 128 -99 C ATOM 145 CE LYS A 19 15.245 -7.791 25.708 1.00 26.43 C ANISOU 145 CE LYS A 19 3458 3316 3269 21 -130 -152 C ATOM 146 NZ LYS A 19 16.205 -8.835 26.084 1.00 29.19 N ANISOU 146 NZ LYS A 19 3962 3404 3724 170 -96 -64 N ATOM 147 N TYR A 20 11.272 -7.042 27.910 1.00 12.85 N ANISOU 147 N TYR A 20 1962 1542 1378 -148 -22 40 N ATOM 148 CA TYR A 20 10.711 -8.152 28.715 1.00 13.78 C ANISOU 148 CA TYR A 20 1936 1766 1533 -142 6 167 C ATOM 149 C TYR A 20 9.249 -7.939 29.007 1.00 13.86 C ANISOU 149 C TYR A 20 1911 1766 1588 -119 -118 95 C ATOM 150 O TYR A 20 8.505 -8.942 29.117 1.00 14.09 O ANISOU 150 O TYR A 20 1972 1787 1594 -208 30 35 O ATOM 151 CB TYR A 20 11.500 -8.210 30.053 1.00 15.68 C ANISOU 151 CB TYR A 20 2193 2048 1718 -139 -201 115 C ATOM 152 CG TYR A 20 12.906 -8.709 29.903 1.00 17.63 C ANISOU 152 CG TYR A 20 2345 2372 1983 -19 -77 174 C ATOM 153 CD1 TYR A 20 13.983 -7.931 30.331 1.00 20.02 C ANISOU 153 CD1 TYR A 20 2566 2601 2439 -160 -86 94 C ATOM 154 CD2 TYR A 20 13.185 -9.964 29.424 1.00 19.15 C ANISOU 154 CD2 TYR A 20 2575 2556 2146 -72 -99 -41 C ATOM 155 CE1 TYR A 20 15.298 -8.385 30.224 1.00 21.96 C ANISOU 155 CE1 TYR A 20 2745 2807 2792 42 -24 59 C ATOM 156 CE2 TYR A 20 14.462 -10.450 29.311 1.00 21.31 C ANISOU 156 CE2 TYR A 20 2688 2916 2492 58 -61 9 C ATOM 157 CZ TYR A 20 15.511 -9.643 29.704 1.00 23.13 C ANISOU 157 CZ TYR A 20 2932 2898 2958 -66 5 -25 C ATOM 158 OH TYR A 20 16.808 -10.117 29.631 1.00 25.90 O ANISOU 158 OH TYR A 20 3024 3345 3471 48 -10 55 O ATOM 159 N ARG A 21 8.769 -6.696 29.148 1.00 13.72 N ANISOU 159 N ARG A 21 1936 1719 1559 -135 -75 -27 N ATOM 160 CA ARG A 21 7.332 -6.476 29.313 1.00 14.86 C ANISOU 160 CA ARG A 21 1907 2045 1696 -122 -41 30 C ATOM 161 C ARG A 21 6.576 -6.949 28.072 1.00 13.42 C ANISOU 161 C ARG A 21 1717 1718 1663 -126 107 9 C ATOM 162 O ARG A 21 5.491 -7.546 28.234 1.00 12.69 O ANISOU 162 O ARG A 21 1692 1661 1469 -220 70 -39 O ATOM 163 CB ARG A 21 6.947 -5.027 29.640 1.00 18.96 C ANISOU 163 CB ARG A 21 2515 2193 2496 -36 104 -14 C ATOM 164 CG ARG A 21 7.424 -4.567 31.025 1.00 23.73 C ANISOU 164 CG ARG A 21 3027 3222 2768 -162 -73 -107 C ATOM 165 CD ARG A 21 6.875 -3.183 31.411 1.00 28.81 C ANISOU 165 CD ARG A 21 3687 3471 3789 114 62 -152 C ATOM 166 NE ARG A 21 7.029 -2.200 30.396 1.00 32.86 N ANISOU 166 NE ARG A 21 4358 4025 4100 68 52 106 N ATOM 167 CZ ARG A 21 7.654 -1.172 29.879 1.00 34.38 C ANISOU 167 CZ ARG A 21 4376 4260 4426 -46 84 60 C ATOM 168 NH1 ARG A 21 7.185 -0.712 28.687 1.00 35.06 N ANISOU 168 NH1 ARG A 21 4585 4370 4365 61 140 95 N ATOM 169 NH2 ARG A 21 8.681 -0.551 30.450 1.00 34.79 N ANISOU 169 NH2 ARG A 21 4367 4392 4462 16 32 -166 N ATOM 170 N ARG A 22 7.111 -6.755 26.870 1.00 11.48 N ANISOU 170 N ARG A 22 1566 1402 1394 -156 -54 20 N ATOM 171 CA ARG A 22 6.455 -7.300 25.677 1.00 11.14 C ANISOU 171 CA ARG A 22 1601 1301 1332 -136 30 69 C ATOM 172 C ARG A 22 6.508 -8.832 25.644 1.00 11.06 C ANISOU 172 C ARG A 22 1522 1315 1365 -107 12 63 C ATOM 173 O ARG A 22 5.497 -9.456 25.273 1.00 11.15 O ANISOU 173 O ARG A 22 1562 1402 1271 -233 40 74 O ATOM 174 CB ARG A 22 7.123 -6.799 24.377 1.00 9.76 C ANISOU 174 CB ARG A 22 1192 1268 1250 -109 -38 87 C ATOM 175 CG ARG A 22 6.757 -5.340 24.110 1.00 10.73 C ANISOU 175 CG ARG A 22 1542 1308 1226 -57 106 170 C ATOM 176 CD ARG A 22 7.301 -4.913 22.734 1.00 10.79 C ANISOU 176 CD ARG A 22 1445 1448 1209 -13 146 101 C ATOM 177 NE ARG A 22 8.776 -4.955 22.650 1.00 11.49 N ANISOU 177 NE ARG A 22 1479 1529 1357 -140 -56 116 N ATOM 178 CZ ARG A 22 9.519 -3.878 22.962 1.00 11.88 C ANISOU 178 CZ ARG A 22 1532 1596 1385 -121 -36 96 C ATOM 179 NH1 ARG A 22 8.925 -2.757 23.367 1.00 12.87 N ANISOU 179 NH1 ARG A 22 1846 1653 1392 -220 123 -104 N ATOM 180 NH2 ARG A 22 10.827 -3.955 22.814 1.00 11.87 N ANISOU 180 NH2 ARG A 22 1486 1856 1170 -230 -43 176 N ATOM 181 N TRP A 23 7.627 -9.423 26.052 1.00 10.22 N ANISOU 181 N TRP A 23 1407 1248 1227 -95 209 48 N ATOM 182 CA TRP A 23 7.654 -10.904 26.100 1.00 9.96 C ANISOU 182 CA TRP A 23 1396 1246 1141 -10 173 47 C ATOM 183 C TRP A 23 6.577 -11.420 27.057 1.00 10.89 C ANISOU 183 C TRP A 23 1449 1380 1311 -166 120 53 C ATOM 184 O TRP A 23 5.907 -12.411 26.751 1.00 10.02 O ANISOU 184 O TRP A 23 1497 1346 963 -143 -13 61 O ATOM 185 CB TRP A 23 9.014 -11.410 26.531 1.00 10.59 C ANISOU 185 CB TRP A 23 1361 1310 1352 -88 95 78 C ATOM 186 CG TRP A 23 10.139 -11.138 25.565 1.00 11.56 C ANISOU 186 CG TRP A 23 1428 1598 1368 38 65 79 C ATOM 187 CD1 TRP A 23 10.047 -10.513 24.336 1.00 11.05 C ANISOU 187 CD1 TRP A 23 1448 1369 1384 -167 165 64 C ATOM 188 CD2 TRP A 23 11.490 -11.547 25.724 1.00 12.26 C ANISOU 188 CD2 TRP A 23 1385 1666 1605 -38 42 27 C ATOM 189 NE1 TRP A 23 11.278 -10.520 23.734 1.00 11.50 N ANISOU 189 NE1 TRP A 23 1382 1499 1487 -52 68 -83 N ATOM 190 CE2 TRP A 23 12.184 -11.120 24.574 1.00 12.31 C ANISOU 190 CE2 TRP A 23 1586 1521 1573 -1 5 92 C ATOM 191 CE3 TRP A 23 12.182 -12.238 26.735 1.00 13.60 C ANISOU 191 CE3 TRP A 23 1606 1865 1696 -47 -37 116 C ATOM 192 CZ2 TRP A 23 13.545 -11.348 24.401 1.00 13.60 C ANISOU 192 CZ2 TRP A 23 1596 1810 1762 -4 57 89 C ATOM 193 CZ3 TRP A 23 13.544 -12.473 26.548 1.00 14.26 C ANISOU 193 CZ3 TRP A 23 1691 1983 1744 93 -33 101 C ATOM 194 CH2 TRP A 23 14.229 -12.026 25.396 1.00 14.85 C ANISOU 194 CH2 TRP A 23 1770 2048 1825 -33 -34 104 C ATOM 195 N LEU A 24 6.456 -10.783 28.216 1.00 12.10 N ANISOU 195 N LEU A 24 1773 1607 1215 -83 147 69 N ATOM 196 CA LEU A 24 5.404 -11.202 29.171 1.00 13.71 C ANISOU 196 CA LEU A 24 1659 1904 1647 -175 175 32 C ATOM 197 C LEU A 24 4.010 -11.024 28.594 1.00 13.51 C ANISOU 197 C LEU A 24 1752 1759 1624 -108 62 26 C ATOM 198 O LEU A 24 3.110 -11.869 28.764 1.00 12.43 O ANISOU 198 O LEU A 24 1711 1636 1377 -125 16 81 O ATOM 199 CB LEU A 24 5.565 -10.433 30.489 1.00 15.64 C ANISOU 199 CB LEU A 24 2191 2029 1721 -106 94 -54 C ATOM 200 CG LEU A 24 4.543 -10.754 31.570 1.00 17.55 C ANISOU 200 CG LEU A 24 2385 2331 1953 -174 133 32 C ATOM 201 CD1 LEU A 24 4.537 -12.209 31.944 1.00 17.16 C ANISOU 201 CD1 LEU A 24 2171 2243 2107 -256 188 7 C ATOM 202 CD2 LEU A 24 4.870 -10.169 32.931 1.00 17.48 C ANISOU 202 CD2 LEU A 24 2343 2342 1958 -284 80 -47 C ATOM 203 N GLU A 25 3.774 -9.909 27.905 1.00 13.44 N ANISOU 203 N GLU A 25 1796 1723 1587 -138 100 31 N ATOM 204 CA GLU A 25 2.463 -9.684 27.278 1.00 15.00 C ANISOU 204 CA GLU A 25 1965 1950 1785 -44 -43 -74 C ATOM 205 C GLU A 25 2.115 -10.818 26.306 1.00 12.99 C ANISOU 205 C GLU A 25 1656 1672 1608 -25 30 87 C ATOM 206 O GLU A 25 0.966 -11.272 26.254 1.00 11.79 O ANISOU 206 O GLU A 25 1591 1628 1260 -29 -4 129 O ATOM 207 CB GLU A 25 2.472 -8.428 26.420 1.00 18.66 C ANISOU 207 CB GLU A 25 2501 2238 2350 -162 75 248 C ATOM 208 CG GLU A 25 2.175 -7.094 27.045 1.00 24.21 C ANISOU 208 CG GLU A 25 3211 2785 3204 97 205 -13 C ATOM 209 CD GLU A 25 1.970 -6.133 25.838 1.00 27.24 C ANISOU 209 CD GLU A 25 3556 3261 3535 6 109 290 C ATOM 210 OE1 GLU A 25 2.980 -5.579 25.389 1.00 27.45 O ANISOU 210 OE1 GLU A 25 3565 3228 3634 -73 127 228 O ATOM 211 OE2 GLU A 25 0.852 -5.983 25.261 1.00 28.86 O ANISOU 211 OE2 GLU A 25 3750 3471 3745 70 -5 202 O ATOM 212 N VAL A 26 3.097 -11.192 25.475 1.00 10.50 N ANISOU 212 N VAL A 26 1495 1262 1232 -112 -26 99 N ATOM 213 CA VAL A 26 2.828 -12.326 24.566 1.00 10.60 C ANISOU 213 CA VAL A 26 1512 1240 1277 -26 71 95 C ATOM 214 C VAL A 26 2.519 -13.615 25.336 1.00 10.82 C ANISOU 214 C VAL A 26 1356 1383 1373 -173 48 104 C ATOM 215 O VAL A 26 1.517 -14.290 25.034 1.00 10.08 O ANISOU 215 O VAL A 26 1392 1280 1156 -228 -43 28 O ATOM 216 CB VAL A 26 4.050 -12.567 23.657 1.00 10.59 C ANISOU 216 CB VAL A 26 1539 1227 1257 -69 78 73 C ATOM 217 CG1 VAL A 26 3.830 -13.835 22.809 1.00 11.36 C ANISOU 217 CG1 VAL A 26 1541 1407 1370 -155 110 -78 C ATOM 218 CG2 VAL A 26 4.284 -11.362 22.752 1.00 10.90 C ANISOU 218 CG2 VAL A 26 1635 1320 1186 -212 137 97 C ATOM 219 N GLU A 27 3.366 -13.938 26.320 1.00 10.20 N ANISOU 219 N GLU A 27 1325 1254 1296 -53 64 84 N ATOM 220 CA GLU A 27 3.048 -15.155 27.094 1.00 11.76 C ANISOU 220 CA GLU A 27 1550 1454 1463 -85 71 198 C ATOM 221 C GLU A 27 1.667 -15.151 27.744 1.00 11.79 C ANISOU 221 C GLU A 27 1436 1471 1572 -71 -55 69 C ATOM 222 O GLU A 27 1.016 -16.211 27.807 1.00 11.61 O ANISOU 222 O GLU A 27 1730 1349 1331 -123 -89 63 O ATOM 223 CB GLU A 27 4.111 -15.303 28.178 1.00 12.35 C ANISOU 223 CB GLU A 27 1487 1577 1629 -192 -34 147 C ATOM 224 CG GLU A 27 5.530 -15.522 27.714 1.00 14.21 C ANISOU 224 CG GLU A 27 1650 1897 1853 -62 101 123 C ATOM 225 CD GLU A 27 5.861 -16.887 27.202 1.00 16.90 C ANISOU 225 CD GLU A 27 2052 2160 2207 -26 88 -11 C ATOM 226 OE1 GLU A 27 5.000 -17.779 27.053 1.00 18.42 O ANISOU 226 OE1 GLU A 27 2186 2339 2475 -124 51 -150 O ATOM 227 OE2 GLU A 27 7.067 -17.076 26.943 1.00 17.63 O ANISOU 227 OE2 GLU A 27 2133 2274 2290 74 240 43 O ATOM 228 N LEU A 28 1.264 -14.004 28.318 1.00 11.21 N ANISOU 228 N LEU A 28 1465 1490 1306 -67 -50 62 N ATOM 229 CA LEU A 28 -0.049 -13.913 28.969 1.00 12.33 C ANISOU 229 CA LEU A 28 1619 1628 1438 -85 54 52 C ATOM 230 C LEU A 28 -1.191 -13.976 27.965 1.00 12.38 C ANISOU 230 C LEU A 28 1637 1656 1411 -160 56 41 C ATOM 231 O LEU A 28 -2.294 -14.424 28.270 1.00 13.03 O ANISOU 231 O LEU A 28 1757 1719 1476 -331 119 -95 O ATOM 232 CB LEU A 28 -0.177 -12.642 29.819 1.00 12.84 C ANISOU 232 CB LEU A 28 1872 1606 1402 -69 167 49 C ATOM 233 CG LEU A 28 0.662 -12.703 31.121 1.00 15.00 C ANISOU 233 CG LEU A 28 2043 1953 1704 -82 -15 3 C ATOM 234 CD1 LEU A 28 0.763 -11.330 31.758 1.00 15.77 C ANISOU 234 CD1 LEU A 28 2170 2006 1815 -109 46 -90 C ATOM 235 CD2 LEU A 28 0.028 -13.730 32.065 1.00 16.93 C ANISOU 235 CD2 LEU A 28 2551 2079 1804 -122 40 105 C ATOM 236 N ALA A 29 -0.983 -13.471 26.739 1.00 11.67 N ANISOU 236 N ALA A 29 1563 1523 1347 -108 42 56 N ATOM 237 CA ALA A 29 -2.000 -13.636 25.699 1.00 11.18 C ANISOU 237 CA ALA A 29 1639 1361 1247 -98 10 153 C ATOM 238 C ALA A 29 -2.169 -15.117 25.375 1.00 11.05 C ANISOU 238 C ALA A 29 1554 1368 1276 -83 36 138 C ATOM 239 O ALA A 29 -3.282 -15.603 25.125 1.00 11.08 O ANISOU 239 O ALA A 29 1518 1361 1331 -46 20 163 O ATOM 240 CB ALA A 29 -1.638 -12.826 24.437 1.00 10.84 C ANISOU 240 CB ALA A 29 1546 1294 1278 -178 6 175 C ATOM 241 N VAL A 30 -1.054 -15.861 25.357 1.00 9.78 N ANISOU 241 N VAL A 30 1553 1111 1052 -108 45 251 N ATOM 242 CA VAL A 30 -1.139 -17.292 25.029 1.00 10.53 C ANISOU 242 CA VAL A 30 1578 1212 1211 -52 116 113 C ATOM 243 C VAL A 30 -1.832 -18.038 26.175 1.00 11.11 C ANISOU 243 C VAL A 30 1480 1436 1306 -175 117 101 C ATOM 244 O VAL A 30 -2.678 -18.920 25.898 1.00 10.37 O ANISOU 244 O VAL A 30 1473 1391 1078 -226 75 143 O ATOM 245 CB VAL A 30 0.271 -17.861 24.766 1.00 10.70 C ANISOU 245 CB VAL A 30 1446 1312 1310 -110 108 125 C ATOM 246 CG1 VAL A 30 0.283 -19.394 24.640 1.00 11.29 C ANISOU 246 CG1 VAL A 30 1492 1356 1443 -29 133 98 C ATOM 247 CG2 VAL A 30 0.846 -17.260 23.465 1.00 10.22 C ANISOU 247 CG2 VAL A 30 1207 1480 1196 -40 112 43 C ATOM 248 N THR A 31 -1.451 -17.740 27.430 1.00 10.95 N ANISOU 248 N THR A 31 1434 1409 1318 -17 49 -15 N ATOM 249 CA THR A 31 -2.136 -18.485 28.519 1.00 12.78 C ANISOU 249 CA THR A 31 1726 1664 1466 -93 40 89 C ATOM 250 C THR A 31 -3.615 -18.135 28.516 1.00 12.92 C ANISOU 250 C THR A 31 1735 1630 1543 -170 101 -29 C ATOM 251 O THR A 31 -4.476 -18.988 28.758 1.00 12.42 O ANISOU 251 O THR A 31 1749 1673 1297 -299 72 32 O ATOM 252 CB THR A 31 -1.546 -18.251 29.931 1.00 14.61 C ANISOU 252 CB THR A 31 1882 1958 1709 -6 -107 -68 C ATOM 253 OG1 THR A 31 -1.645 -16.886 30.290 1.00 16.06 O ANISOU 253 OG1 THR A 31 2285 2038 1780 -136 70 -96 O ATOM 254 CG2 THR A 31 -0.077 -18.687 29.986 1.00 13.89 C ANISOU 254 CG2 THR A 31 1760 1929 1589 -106 -89 -135 C ATOM 255 N ARG A 32 -3.966 -16.865 28.254 1.00 12.15 N ANISOU 255 N ARG A 32 1683 1620 1313 -110 107 105 N ATOM 256 CA ARG A 32 -5.368 -16.479 28.189 1.00 12.72 C ANISOU 256 CA ARG A 32 1722 1681 1431 -103 73 -3 C ATOM 257 C ARG A 32 -6.107 -17.291 27.126 1.00 12.76 C ANISOU 257 C ARG A 32 1679 1677 1494 -137 114 -35 C ATOM 258 O ARG A 32 -7.232 -17.773 27.361 1.00 13.47 O ANISOU 258 O ARG A 32 1664 1868 1585 -182 315 -154 O ATOM 259 CB ARG A 32 -5.536 -14.976 27.946 1.00 13.36 C ANISOU 259 CB ARG A 32 1849 1684 1543 -49 115 -30 C ATOM 260 CG ARG A 32 -6.994 -14.553 27.890 1.00 16.11 C ANISOU 260 CG ARG A 32 1928 2141 2050 26 35 -25 C ATOM 261 CD ARG A 32 -7.085 -13.020 27.723 1.00 19.87 C ANISOU 261 CD ARG A 32 2649 2263 2637 21 38 38 C ATOM 262 NE ARG A 32 -8.477 -12.682 27.407 1.00 23.23 N ANISOU 262 NE ARG A 32 2738 2950 3137 50 -63 -93 N ATOM 263 CZ ARG A 32 -8.856 -11.485 26.974 1.00 26.26 C ANISOU 263 CZ ARG A 32 3318 3124 3537 79 -21 65 C ATOM 264 NH1 ARG A 32 -7.974 -10.500 26.850 1.00 26.24 N ANISOU 264 NH1 ARG A 32 3441 3082 3448 43 12 17 N ATOM 265 NH2 ARG A 32 -10.138 -11.262 26.671 1.00 28.52 N ANISOU 265 NH2 ARG A 32 3397 3616 3825 86 -111 -37 N ATOM 266 N ALA A 33 -5.507 -17.451 25.956 1.00 11.99 N ANISOU 266 N ALA A 33 1656 1524 1375 -129 90 36 N ATOM 267 CA ALA A 33 -6.147 -18.215 24.876 1.00 11.86 C ANISOU 267 CA ALA A 33 1685 1553 1269 -75 173 -21 C ATOM 268 C ALA A 33 -6.298 -19.680 25.202 1.00 11.46 C ANISOU 268 C ALA A 33 1602 1605 1146 -54 156 3 C ATOM 269 O ALA A 33 -7.368 -20.271 25.001 1.00 12.36 O ANISOU 269 O ALA A 33 1695 1567 1432 -141 29 92 O ATOM 270 CB ALA A 33 -5.274 -18.130 23.593 1.00 11.76 C ANISOU 270 CB ALA A 33 1639 1634 1194 -29 108 81 C ATOM 271 N TYR A 34 -5.249 -20.309 25.763 1.00 11.56 N ANISOU 271 N TYR A 34 1552 1624 1218 30 316 21 N ATOM 272 CA TYR A 34 -5.434 -21.711 26.182 1.00 12.83 C ANISOU 272 CA TYR A 34 1650 1616 1610 -11 217 -26 C ATOM 273 C TYR A 34 -6.573 -21.806 27.213 1.00 13.70 C ANISOU 273 C TYR A 34 1695 1816 1696 -133 231 -101 C ATOM 274 O TYR A 34 -7.396 -22.714 27.193 1.00 14.69 O ANISOU 274 O TYR A 34 1915 1876 1792 -232 344 -136 O ATOM 275 CB TYR A 34 -4.147 -22.200 26.834 1.00 12.15 C ANISOU 275 CB TYR A 34 1562 1566 1489 -53 174 -32 C ATOM 276 CG TYR A 34 -3.056 -22.809 25.960 1.00 12.76 C ANISOU 276 CG TYR A 34 1537 1620 1693 -41 177 -34 C ATOM 277 CD1 TYR A 34 -1.777 -22.260 25.929 1.00 12.35 C ANISOU 277 CD1 TYR A 34 1554 1517 1621 -34 86 58 C ATOM 278 CD2 TYR A 34 -3.264 -23.969 25.235 1.00 13.67 C ANISOU 278 CD2 TYR A 34 1753 1778 1663 -57 224 -87 C ATOM 279 CE1 TYR A 34 -0.764 -22.824 25.192 1.00 12.28 C ANISOU 279 CE1 TYR A 34 1517 1543 1605 -67 115 67 C ATOM 280 CE2 TYR A 34 -2.239 -24.598 24.500 1.00 13.33 C ANISOU 280 CE2 TYR A 34 1563 1734 1768 13 116 -37 C ATOM 281 CZ TYR A 34 -1.008 -23.992 24.478 1.00 12.83 C ANISOU 281 CZ TYR A 34 1632 1631 1614 -64 176 -3 C ATOM 282 OH TYR A 34 0.029 -24.587 23.789 1.00 12.30 O ANISOU 282 OH TYR A 34 1538 1427 1707 -61 214 139 O ATOM 283 N GLU A 35 -6.607 -20.884 28.158 1.00 14.05 N ANISOU 283 N GLU A 35 1818 1835 1684 -142 126 -151 N ATOM 284 CA GLU A 35 -7.635 -20.893 29.206 1.00 15.91 C ANISOU 284 CA GLU A 35 1965 2161 1919 -119 190 -163 C ATOM 285 C GLU A 35 -9.026 -20.693 28.632 1.00 15.95 C ANISOU 285 C GLU A 35 2017 2079 1962 -223 91 -131 C ATOM 286 O GLU A 35 -9.974 -21.449 29.010 1.00 16.83 O ANISOU 286 O GLU A 35 2133 2310 1951 -378 224 -55 O ATOM 287 CB GLU A 35 -7.272 -19.790 30.225 1.00 17.70 C ANISOU 287 CB GLU A 35 2349 2273 2105 -187 89 -237 C ATOM 288 CG GLU A 35 -8.149 -19.827 31.484 1.00 19.46 C ANISOU 288 CG GLU A 35 2598 2573 2223 -137 175 -117 C ATOM 289 CD GLU A 35 -7.613 -18.894 32.551 1.00 21.15 C ANISOU 289 CD GLU A 35 2769 2851 2414 -113 -18 -163 C ATOM 290 OE1 GLU A 35 -6.403 -18.597 32.588 1.00 20.80 O ANISOU 290 OE1 GLU A 35 2804 2798 2298 -158 -62 -214 O ATOM 291 OE2 GLU A 35 -8.413 -18.420 33.388 1.00 22.38 O ANISOU 291 OE2 GLU A 35 2797 3012 2693 25 -5 -219 O ATOM 292 N GLU A 36 -9.218 -19.787 27.692 1.00 15.48 N ANISOU 292 N GLU A 36 2031 1897 1954 -256 158 -137 N ATOM 293 CA GLU A 36 -10.521 -19.527 27.103 1.00 19.62 C ANISOU 293 CA GLU A 36 2283 2596 2575 -66 -20 -162 C ATOM 294 C GLU A 36 -10.990 -20.686 26.258 1.00 19.20 C ANISOU 294 C GLU A 36 2332 2403 2561 -59 72 -22 C ATOM 295 O GLU A 36 -12.213 -20.928 26.126 1.00 20.45 O ANISOU 295 O GLU A 36 2354 2665 2751 -163 104 -73 O ATOM 296 CB GLU A 36 -10.529 -18.196 26.313 1.00 24.14 C ANISOU 296 CB GLU A 36 3026 2995 3150 -12 48 198 C ATOM 297 CG GLU A 36 -10.353 -17.062 27.342 1.00 29.81 C ANISOU 297 CG GLU A 36 3904 3660 3764 -93 -48 -209 C ATOM 298 CD GLU A 36 -10.669 -15.656 26.879 1.00 33.05 C ANISOU 298 CD GLU A 36 4266 3931 4359 39 -16 -8 C ATOM 299 OE1 GLU A 36 -10.591 -14.703 27.694 1.00 32.52 O ANISOU 299 OE1 GLU A 36 4056 4038 4261 -1 12 -66 O ATOM 300 OE2 GLU A 36 -10.984 -15.548 25.667 1.00 36.01 O ANISOU 300 OE2 GLU A 36 4700 4543 4439 -35 -101 13 O ATOM 301 N LEU A 37 -10.058 -21.478 25.744 1.00 17.80 N ANISOU 301 N LEU A 37 2252 2237 2272 -189 190 34 N ATOM 302 CA LEU A 37 -10.398 -22.688 25.000 1.00 19.30 C ANISOU 302 CA LEU A 37 2504 2407 2421 -181 66 -39 C ATOM 303 C LEU A 37 -10.548 -23.903 25.909 1.00 18.92 C ANISOU 303 C LEU A 37 2430 2365 2396 -164 97 -80 C ATOM 304 O LEU A 37 -10.681 -25.058 25.486 1.00 18.71 O ANISOU 304 O LEU A 37 2346 2419 2342 -335 112 -84 O ATOM 305 CB LEU A 37 -9.276 -22.952 23.998 1.00 20.69 C ANISOU 305 CB LEU A 37 2556 2703 2602 -105 109 -183 C ATOM 306 CG LEU A 37 -9.374 -22.493 22.554 1.00 23.91 C ANISOU 306 CG LEU A 37 3031 3222 2834 15 107 78 C ATOM 307 CD1 LEU A 37 -10.671 -21.934 22.031 1.00 23.75 C ANISOU 307 CD1 LEU A 37 3063 3137 2823 -1 67 116 C ATOM 308 CD2 LEU A 37 -8.161 -21.683 22.134 1.00 24.94 C ANISOU 308 CD2 LEU A 37 3251 3112 3114 -253 -110 -46 C ATOM 309 N GLY A 38 -10.442 -23.748 27.224 1.00 18.87 N ANISOU 309 N GLY A 38 2367 2431 2372 -244 -42 -20 N ATOM 310 CA GLY A 38 -10.543 -24.838 28.175 1.00 18.61 C ANISOU 310 CA GLY A 38 2307 2427 2335 -181 34 -56 C ATOM 311 C GLY A 38 -9.373 -25.781 28.187 1.00 19.51 C ANISOU 311 C GLY A 38 2469 2437 2507 -145 80 -52 C ATOM 312 O GLY A 38 -9.558 -26.901 28.728 1.00 21.16 O ANISOU 312 O GLY A 38 2709 2658 2673 -389 209 97 O ATOM 313 N MET A 39 -8.181 -25.414 27.782 1.00 18.12 N ANISOU 313 N MET A 39 2340 2302 2242 -274 34 -75 N ATOM 314 CA MET A 39 -7.074 -26.329 27.648 1.00 19.09 C ANISOU 314 CA MET A 39 2564 2315 2373 -125 39 -79 C ATOM 315 C MET A 39 -6.193 -26.293 28.892 1.00 19.46 C ANISOU 315 C MET A 39 2599 2409 2385 -81 41 -9 C ATOM 316 O MET A 39 -5.274 -27.077 29.057 1.00 20.23 O ANISOU 316 O MET A 39 2860 2349 2479 -10 -53 -110 O ATOM 317 CB MET A 39 -6.208 -26.036 26.418 1.00 19.53 C ANISOU 317 CB MET A 39 2613 2513 2295 -101 69 17 C ATOM 318 CG MET A 39 -7.026 -25.603 25.196 1.00 19.17 C ANISOU 318 CG MET A 39 2704 2721 1859 -77 403 -15 C ATOM 319 SD MET A 39 -6.241 -25.979 23.627 1.00 15.08 S ANISOU 319 SD MET A 39 2082 2093 1556 -552 425 24 S ATOM 320 CE MET A 39 -7.451 -26.034 22.344 1.00 19.82 C ANISOU 320 CE MET A 39 2518 2635 2376 -237 69 -10 C ATOM 321 N ILE A 40 -6.335 -25.202 29.675 1.00 19.03 N ANISOU 321 N ILE A 40 2549 2276 2404 -199 -14 9 N ATOM 322 CA ILE A 40 -5.662 -25.072 30.962 1.00 18.91 C ANISOU 322 CA ILE A 40 2490 2205 2488 -231 -44 69 C ATOM 323 C ILE A 40 -6.746 -24.578 31.920 1.00 20.79 C ANISOU 323 C ILE A 40 2661 2449 2790 -231 93 -30 C ATOM 324 O ILE A 40 -7.762 -23.987 31.554 1.00 20.35 O ANISOU 324 O ILE A 40 2654 2605 2473 -256 110 17 O ATOM 325 CB ILE A 40 -4.433 -24.123 30.995 1.00 17.52 C ANISOU 325 CB ILE A 40 2212 2134 2311 -24 19 71 C ATOM 326 CG1 ILE A 40 -4.817 -22.672 30.683 1.00 16.25 C ANISOU 326 CG1 ILE A 40 2038 1959 2179 -198 -4 11 C ATOM 327 CG2 ILE A 40 -3.352 -24.605 30.009 1.00 17.76 C ANISOU 327 CG2 ILE A 40 2227 2150 2372 -96 88 27 C ATOM 328 CD1 ILE A 40 -3.641 -21.693 30.864 1.00 14.78 C ANISOU 328 CD1 ILE A 40 1893 1797 1925 -37 -45 84 C ATOM 329 N PRO A 41 -6.517 -24.775 33.203 1.00 23.69 N ANISOU 329 N PRO A 41 3209 2861 2931 -205 42 35 N ATOM 330 CA PRO A 41 -7.540 -24.555 34.223 1.00 25.37 C ANISOU 330 CA PRO A 41 3341 3208 3091 -124 82 20 C ATOM 331 C PRO A 41 -7.907 -23.086 34.357 1.00 24.64 C ANISOU 331 C PRO A 41 3167 3232 2965 -116 30 -9 C ATOM 332 O PRO A 41 -7.087 -22.187 34.166 1.00 23.19 O ANISOU 332 O PRO A 41 3072 3055 2683 -126 127 -60 O ATOM 333 CB PRO A 41 -6.888 -25.099 35.485 1.00 26.60 C ANISOU 333 CB PRO A 41 3471 3392 3245 -94 14 129 C ATOM 334 CG PRO A 41 -5.756 -25.959 35.058 1.00 27.50 C ANISOU 334 CG PRO A 41 3575 3479 3396 -72 108 96 C ATOM 335 CD PRO A 41 -5.289 -25.390 33.742 1.00 26.01 C ANISOU 335 CD PRO A 41 3316 3345 3222 -51 18 25 C ATOM 336 N LYS A 42 -9.160 -22.814 34.681 1.00 24.82 N ANISOU 336 N LYS A 42 3116 3284 3030 -138 20 77 N ATOM 337 CA LYS A 42 -9.650 -21.472 34.943 1.00 25.88 C ANISOU 337 CA LYS A 42 3268 3392 3175 -66 0 -23 C ATOM 338 C LYS A 42 -8.856 -20.815 36.077 1.00 25.42 C ANISOU 338 C LYS A 42 3260 3268 3130 -66 30 -18 C ATOM 339 O LYS A 42 -8.577 -21.475 37.069 1.00 26.90 O ANISOU 339 O LYS A 42 3605 3469 3148 -82 -19 24 O ATOM 340 CB LYS A 42 -11.129 -21.522 35.340 1.00 27.07 C ANISOU 340 CB LYS A 42 3284 3576 3424 -73 57 64 C ATOM 341 N GLY A 43 -8.457 -19.567 35.904 1.00 23.15 N ANISOU 341 N GLY A 43 2973 3171 2654 -3 81 -92 N ATOM 342 CA GLY A 43 -7.718 -18.816 36.890 1.00 22.71 C ANISOU 342 CA GLY A 43 2820 3110 2699 -36 83 1 C ATOM 343 C GLY A 43 -6.224 -18.735 36.675 1.00 21.59 C ANISOU 343 C GLY A 43 2810 2844 2548 -28 120 -112 C ATOM 344 O GLY A 43 -5.599 -17.860 37.305 1.00 21.96 O ANISOU 344 O GLY A 43 3055 2859 2430 -41 191 -231 O ATOM 345 N VAL A 44 -5.649 -19.569 35.789 1.00 19.36 N ANISOU 345 N VAL A 44 2560 2442 2353 -102 22 -67 N ATOM 346 CA VAL A 44 -4.202 -19.540 35.626 1.00 18.25 C ANISOU 346 CA VAL A 44 2497 2218 2218 -2 61 -70 C ATOM 347 C VAL A 44 -3.688 -18.179 35.196 1.00 17.48 C ANISOU 347 C VAL A 44 2318 2167 2158 70 43 -110 C ATOM 348 O VAL A 44 -2.695 -17.662 35.698 1.00 16.89 O ANISOU 348 O VAL A 44 2216 2121 2083 44 80 6 O ATOM 349 CB VAL A 44 -3.733 -20.623 34.607 1.00 18.53 C ANISOU 349 CB VAL A 44 2501 2208 2332 24 69 -91 C ATOM 350 CG1 VAL A 44 -2.298 -20.391 34.168 1.00 18.47 C ANISOU 350 CG1 VAL A 44 2508 2364 2146 29 18 -83 C ATOM 351 CG2 VAL A 44 -3.911 -21.990 35.296 1.00 19.19 C ANISOU 351 CG2 VAL A 44 2724 2263 2305 40 53 -41 C ATOM 352 N THR A 45 -4.345 -17.563 34.199 1.00 16.69 N ANISOU 352 N THR A 45 2296 2064 1981 18 106 -154 N ATOM 353 CA THR A 45 -3.808 -16.350 33.578 1.00 17.26 C ANISOU 353 CA THR A 45 2455 2082 2022 15 57 -115 C ATOM 354 C THR A 45 -3.758 -15.223 34.613 1.00 17.33 C ANISOU 354 C THR A 45 2402 2180 2003 -71 -38 -90 C ATOM 355 O THR A 45 -2.765 -14.535 34.743 1.00 15.56 O ANISOU 355 O THR A 45 2460 1892 1559 -27 87 -23 O ATOM 356 CB THR A 45 -4.659 -15.939 32.369 1.00 17.85 C ANISOU 356 CB THR A 45 2534 2123 2127 -70 -18 -99 C ATOM 357 OG1 THR A 45 -4.535 -16.982 31.354 1.00 18.77 O ANISOU 357 OG1 THR A 45 2734 2484 1915 -63 -1 -161 O ATOM 358 CG2 THR A 45 -4.138 -14.653 31.724 1.00 18.19 C ANISOU 358 CG2 THR A 45 2676 2261 1973 -1 15 10 C ATOM 359 N GLU A 46 -4.838 -15.127 35.398 1.00 18.69 N ANISOU 359 N GLU A 46 2562 2389 2149 34 112 -98 N ATOM 360 CA GLU A 46 -4.864 -14.053 36.411 1.00 20.70 C ANISOU 360 CA GLU A 46 2811 2644 2411 22 30 -221 C ATOM 361 C GLU A 46 -3.761 -14.258 37.433 1.00 20.00 C ANISOU 361 C GLU A 46 2781 2571 2247 14 125 -51 C ATOM 362 O GLU A 46 -3.127 -13.263 37.858 1.00 20.02 O ANISOU 362 O GLU A 46 2789 2625 2192 -38 22 -13 O ATOM 363 CB GLU A 46 -6.277 -14.026 37.004 1.00 23.14 C ANISOU 363 CB GLU A 46 2914 3018 2862 82 149 -146 C ATOM 364 CG GLU A 46 -6.414 -12.935 38.089 1.00 25.61 C ANISOU 364 CG GLU A 46 3476 3201 3056 93 -3 -285 C ATOM 365 N ARG A 47 -3.525 -15.515 37.847 1.00 18.15 N ANISOU 365 N ARG A 47 2557 2424 1915 87 131 -133 N ATOM 366 CA ARG A 47 -2.470 -15.736 38.853 1.00 17.96 C ANISOU 366 CA ARG A 47 2316 2418 2090 -19 156 -65 C ATOM 367 C ARG A 47 -1.093 -15.398 38.323 1.00 16.70 C ANISOU 367 C ARG A 47 2284 2242 1818 -63 114 -98 C ATOM 368 O ARG A 47 -0.223 -14.810 38.994 1.00 15.95 O ANISOU 368 O ARG A 47 2251 2483 1326 -23 248 -125 O ATOM 369 CB ARG A 47 -2.488 -17.215 39.328 1.00 18.96 C ANISOU 369 CB ARG A 47 2486 2402 2316 -32 95 60 C ATOM 370 CG ARG A 47 -3.769 -17.510 40.146 1.00 20.16 C ANISOU 370 CG ARG A 47 2559 2634 2465 4 146 28 C ATOM 371 CD ARG A 47 -3.602 -18.847 40.859 1.00 21.65 C ANISOU 371 CD ARG A 47 2907 2637 2684 -116 170 102 C ATOM 372 NE ARG A 47 -3.365 -19.969 39.963 1.00 22.18 N ANISOU 372 NE ARG A 47 3085 2761 2580 -114 169 40 N ATOM 373 CZ ARG A 47 -4.302 -20.827 39.556 1.00 23.09 C ANISOU 373 CZ ARG A 47 3004 2954 2815 -73 66 -36 C ATOM 374 NH1 ARG A 47 -3.950 -21.846 38.753 1.00 22.71 N ANISOU 374 NH1 ARG A 47 3045 2860 2724 -133 103 0 N ATOM 375 NH2 ARG A 47 -5.551 -20.667 39.956 1.00 22.86 N ANISOU 375 NH2 ARG A 47 2962 2875 2850 -104 67 -19 N ATOM 376 N ILE A 48 -0.824 -15.843 37.068 1.00 15.84 N ANISOU 376 N ILE A 48 2150 2176 1694 -79 75 -53 N ATOM 377 CA ILE A 48 0.478 -15.518 36.489 1.00 16.37 C ANISOU 377 CA ILE A 48 2231 2248 1741 -10 184 -94 C ATOM 378 C ILE A 48 0.661 -14.012 36.348 1.00 16.73 C ANISOU 378 C ILE A 48 2346 2302 1708 -53 199 -144 C ATOM 379 O ILE A 48 1.675 -13.391 36.696 1.00 16.29 O ANISOU 379 O ILE A 48 2391 2337 1461 -71 209 -31 O ATOM 380 CB ILE A 48 0.656 -16.232 35.131 1.00 16.10 C ANISOU 380 CB ILE A 48 2188 2089 1839 -53 114 -158 C ATOM 381 CG1 ILE A 48 0.694 -17.761 35.352 1.00 16.34 C ANISOU 381 CG1 ILE A 48 2297 2087 1823 -9 145 -75 C ATOM 382 CG2 ILE A 48 1.947 -15.744 34.457 1.00 16.30 C ANISOU 382 CG2 ILE A 48 2305 2020 1870 3 195 -13 C ATOM 383 CD1 ILE A 48 0.851 -18.526 34.037 1.00 15.97 C ANISOU 383 CD1 ILE A 48 2213 2060 1793 -68 127 -30 C ATOM 384 N ARG A 49 -0.397 -13.326 35.896 1.00 17.25 N ANISOU 384 N ARG A 49 2532 2443 1580 8 112 -79 N ATOM 385 CA ARG A 49 -0.410 -11.869 35.820 1.00 20.64 C ANISOU 385 CA ARG A 49 2961 2584 2299 -68 122 -57 C ATOM 386 C ARG A 49 -0.083 -11.208 37.166 1.00 21.10 C ANISOU 386 C ARG A 49 2940 2702 2374 -113 65 -86 C ATOM 387 O ARG A 49 0.721 -10.246 37.210 1.00 19.90 O ANISOU 387 O ARG A 49 3222 2483 1856 -166 184 -70 O ATOM 388 CB ARG A 49 -1.769 -11.367 35.304 1.00 23.22 C ANISOU 388 CB ARG A 49 3105 3110 2608 67 0 2 C ATOM 389 CG ARG A 49 -1.709 -9.838 35.116 1.00 27.42 C ANISOU 389 CG ARG A 49 3732 3251 3436 -24 46 -73 C ATOM 390 CD ARG A 49 -2.938 -9.298 34.408 1.00 31.44 C ANISOU 390 CD ARG A 49 4007 3854 4085 175 -112 107 C ATOM 391 NE ARG A 49 -2.995 -9.726 33.010 1.00 34.87 N ANISOU 391 NE ARG A 49 4561 4340 4348 187 -110 -81 N ATOM 392 CZ ARG A 49 -3.903 -10.576 32.529 1.00 36.06 C ANISOU 392 CZ ARG A 49 4622 4452 4626 92 -92 -50 C ATOM 393 NH1 ARG A 49 -4.843 -11.101 33.314 1.00 37.50 N ANISOU 393 NH1 ARG A 49 4798 4729 4720 155 50 58 N ATOM 394 NH2 ARG A 49 -3.857 -10.875 31.238 1.00 36.28 N ANISOU 394 NH2 ARG A 49 4674 4558 4553 203 0 20 N ATOM 395 N ASN A 50 -0.616 -11.775 38.251 1.00 21.19 N ANISOU 395 N ASN A 50 2972 2708 2371 -15 134 28 N ATOM 396 CA ASN A 50 -0.371 -11.224 39.591 1.00 22.08 C ANISOU 396 CA ASN A 50 3052 2769 2569 -12 -43 -45 C ATOM 397 C ASN A 50 1.065 -11.446 40.015 1.00 21.73 C ANISOU 397 C ASN A 50 2970 2737 2549 -74 90 7 C ATOM 398 O ASN A 50 1.606 -10.625 40.770 1.00 22.65 O ANISOU 398 O ASN A 50 3145 2648 2813 -118 55 -52 O ATOM 399 CB ASN A 50 -1.336 -11.859 40.611 1.00 23.98 C ANISOU 399 CB ASN A 50 3281 3133 2699 -77 97 -46 C ATOM 400 CG ASN A 50 -2.767 -11.366 40.484 1.00 26.40 C ANISOU 400 CG ASN A 50 3461 3460 3110 38 72 -100 C ATOM 401 OD1 ASN A 50 -2.974 -10.236 40.014 1.00 27.89 O ANISOU 401 OD1 ASN A 50 3744 3553 3300 221 67 -36 O ATOM 402 ND2 ASN A 50 -3.746 -12.158 40.875 1.00 27.03 N ANISOU 402 ND2 ASN A 50 3556 3583 3131 -92 92 -128 N ATOM 403 N ASN A 51 1.692 -12.553 39.632 1.00 19.77 N ANISOU 403 N ASN A 51 2744 2569 2198 -139 186 76 N ATOM 404 CA ASN A 51 2.956 -13.001 40.190 1.00 21.19 C ANISOU 404 CA ASN A 51 2812 2823 2414 -84 102 33 C ATOM 405 C ASN A 51 4.151 -12.635 39.299 1.00 21.16 C ANISOU 405 C ASN A 51 2762 2684 2592 -97 56 59 C ATOM 406 O ASN A 51 5.303 -12.532 39.717 1.00 20.57 O ANISOU 406 O ASN A 51 2741 2654 2422 -77 77 165 O ATOM 407 CB ASN A 51 2.919 -14.536 40.332 1.00 22.17 C ANISOU 407 CB ASN A 51 3029 2812 2584 -30 47 20 C ATOM 408 CG ASN A 51 2.084 -15.016 41.520 1.00 24.71 C ANISOU 408 CG ASN A 51 3459 3209 2720 -148 98 105 C ATOM 409 OD1 ASN A 51 2.309 -14.439 42.573 1.00 24.24 O ANISOU 409 OD1 ASN A 51 3664 2959 2586 -20 405 73 O ATOM 410 ND2 ASN A 51 1.291 -16.081 41.311 1.00 26.45 N ANISOU 410 ND2 ASN A 51 3516 3557 2979 -286 13 174 N ATOM 411 N ALA A 52 3.888 -12.465 38.000 1.00 21.04 N ANISOU 411 N ALA A 52 2850 2619 2525 -60 86 -64 N ATOM 412 CA ALA A 52 5.000 -12.346 37.061 1.00 22.17 C ANISOU 412 CA ALA A 52 2838 2891 2697 -96 100 -37 C ATOM 413 C ALA A 52 5.491 -10.896 37.055 1.00 24.18 C ANISOU 413 C ALA A 52 3192 2975 3021 -73 96 16 C ATOM 414 O ALA A 52 4.800 -9.984 36.596 1.00 24.69 O ANISOU 414 O ALA A 52 3403 2810 3167 -130 108 132 O ATOM 415 CB ALA A 52 4.617 -12.784 35.657 1.00 21.94 C ANISOU 415 CB ALA A 52 2766 2918 2654 -88 89 34 C ATOM 416 N LYS A 53 6.661 -10.696 37.621 1.00 25.59 N ANISOU 416 N LYS A 53 3293 3351 3077 -143 56 16 N ATOM 417 CA LYS A 53 7.248 -9.363 37.692 1.00 27.53 C ANISOU 417 CA LYS A 53 3602 3393 3465 -118 104 14 C ATOM 418 C LYS A 53 8.473 -9.280 36.782 1.00 26.12 C ANISOU 418 C LYS A 53 3391 3239 3295 -118 -56 10 C ATOM 419 O LYS A 53 9.212 -10.256 36.641 1.00 25.56 O ANISOU 419 O LYS A 53 3250 3265 3196 -127 -16 93 O ATOM 420 CB LYS A 53 7.730 -9.079 39.111 1.00 30.95 C ANISOU 420 CB LYS A 53 4102 3964 3693 -99 -105 -86 C ATOM 421 CG LYS A 53 6.761 -9.433 40.229 1.00 33.64 C ANISOU 421 CG LYS A 53 4267 4349 4166 -140 117 -1 C ATOM 422 CD LYS A 53 5.495 -8.595 40.161 1.00 35.07 C ANISOU 422 CD LYS A 53 4412 4430 4482 -9 -19 -36 C ATOM 423 CE LYS A 53 4.649 -8.798 41.416 1.00 36.78 C ANISOU 423 CE LYS A 53 4670 4704 4603 -16 72 58 C ATOM 424 NZ LYS A 53 3.228 -8.424 41.121 1.00 38.00 N ANISOU 424 NZ LYS A 53 4701 4899 4838 2 70 -31 N ATOM 425 N ILE A 54 8.682 -8.108 36.185 1.00 24.94 N ANISOU 425 N ILE A 54 3257 3227 2991 -83 -98 5 N ATOM 426 CA ILE A 54 9.885 -7.947 35.371 1.00 25.23 C ANISOU 426 CA ILE A 54 3295 3179 3111 -39 -16 8 C ATOM 427 C ILE A 54 11.063 -7.642 36.277 1.00 26.87 C ANISOU 427 C ILE A 54 3501 3488 3219 -57 -65 -16 C ATOM 428 O ILE A 54 11.043 -6.606 36.943 1.00 28.47 O ANISOU 428 O ILE A 54 3856 3560 3403 -85 -191 -154 O ATOM 429 CB ILE A 54 9.668 -6.830 34.318 1.00 24.72 C ANISOU 429 CB ILE A 54 3173 3161 3058 -96 -20 -22 C ATOM 430 CG1 ILE A 54 8.481 -7.210 33.404 1.00 24.04 C ANISOU 430 CG1 ILE A 54 3087 3026 3023 -49 6 75 C ATOM 431 CG2 ILE A 54 10.937 -6.635 33.508 1.00 24.88 C ANISOU 431 CG2 ILE A 54 3239 3091 3122 -133 17 16 C ATOM 432 CD1 ILE A 54 8.612 -8.585 32.762 1.00 22.81 C ANISOU 432 CD1 ILE A 54 2817 3080 2771 -148 -46 18 C ATOM 433 N ASP A 55 12.040 -8.520 36.333 1.00 27.54 N ANISOU 433 N ASP A 55 3555 3590 3321 1 -30 78 N ATOM 434 CA ASP A 55 13.265 -8.328 37.104 1.00 29.36 C ANISOU 434 CA ASP A 55 3639 3917 3599 -75 -77 -53 C ATOM 435 C ASP A 55 14.458 -8.508 36.163 1.00 28.11 C ANISOU 435 C ASP A 55 3539 3710 3430 -38 -172 -15 C ATOM 436 O ASP A 55 14.939 -9.614 35.905 1.00 26.78 O ANISOU 436 O ASP A 55 3264 3704 3207 -64 -290 83 O ATOM 437 CB ASP A 55 13.293 -9.335 38.253 1.00 31.48 C ANISOU 437 CB ASP A 55 4080 4041 3840 16 -48 74 C ATOM 438 CG ASP A 55 14.495 -9.231 39.167 1.00 34.07 C ANISOU 438 CG ASP A 55 4253 4507 4187 -83 -160 -3 C ATOM 439 OD1 ASP A 55 15.453 -8.489 38.860 1.00 34.53 O ANISOU 439 OD1 ASP A 55 4344 4609 4169 -157 -136 -29 O ATOM 440 OD2 ASP A 55 14.479 -9.929 40.212 1.00 35.63 O ANISOU 440 OD2 ASP A 55 4558 4726 4255 -76 -113 86 O ATOM 441 N VAL A 56 14.869 -7.395 35.556 1.00 28.09 N ANISOU 441 N VAL A 56 3536 3645 3492 -90 -187 -83 N ATOM 442 CA VAL A 56 15.884 -7.437 34.508 1.00 29.35 C ANISOU 442 CA VAL A 56 3711 3763 3679 -75 -60 -19 C ATOM 443 C VAL A 56 17.168 -8.081 35.011 1.00 30.44 C ANISOU 443 C VAL A 56 3807 3870 3888 -28 -88 27 C ATOM 444 O VAL A 56 17.780 -8.903 34.318 1.00 30.72 O ANISOU 444 O VAL A 56 3911 3947 3815 -95 -104 -41 O ATOM 445 CB VAL A 56 16.195 -6.045 33.919 1.00 29.41 C ANISOU 445 CB VAL A 56 3674 3787 3714 -33 -73 5 C ATOM 446 CG1 VAL A 56 17.300 -6.171 32.886 1.00 28.98 C ANISOU 446 CG1 VAL A 56 3645 3717 3651 -67 -76 23 C ATOM 447 CG2 VAL A 56 14.946 -5.422 33.291 1.00 29.23 C ANISOU 447 CG2 VAL A 56 3739 3710 3658 -13 -63 2 C ATOM 448 N GLU A 57 17.618 -7.711 36.210 1.00 31.60 N ANISOU 448 N GLU A 57 4040 4033 3936 -48 -96 -35 N ATOM 449 CA GLU A 57 18.840 -8.279 36.776 1.00 32.20 C ANISOU 449 CA GLU A 57 4038 4104 4092 -27 -105 -25 C ATOM 450 C GLU A 57 18.767 -9.784 36.953 1.00 31.80 C ANISOU 450 C GLU A 57 3975 4109 3998 -50 -74 -28 C ATOM 451 O GLU A 57 19.748 -10.471 36.635 1.00 32.09 O ANISOU 451 O GLU A 57 3912 4240 4040 -52 -184 -104 O ATOM 452 CB GLU A 57 19.185 -7.603 38.106 1.00 33.71 C ANISOU 452 CB GLU A 57 4337 4390 4080 -41 -87 -56 C ATOM 453 N LEU A 58 17.652 -10.324 37.421 1.00 30.83 N ANISOU 453 N LEU A 58 3946 3903 3867 -36 -64 -7 N ATOM 454 CA LEU A 58 17.498 -11.779 37.470 1.00 29.76 C ANISOU 454 CA LEU A 58 3763 3855 3689 8 -77 0 C ATOM 455 C LEU A 58 17.567 -12.443 36.111 1.00 28.30 C ANISOU 455 C LEU A 58 3530 3641 3583 7 -50 95 C ATOM 456 O LEU A 58 18.261 -13.450 35.939 1.00 27.43 O ANISOU 456 O LEU A 58 3506 3615 3303 -14 -146 107 O ATOM 457 CB LEU A 58 16.180 -12.141 38.166 1.00 30.35 C ANISOU 457 CB LEU A 58 3782 3908 3840 -10 -2 4 C ATOM 458 CG LEU A 58 15.806 -13.623 38.190 1.00 31.22 C ANISOU 458 CG LEU A 58 3959 3900 4005 12 6 12 C ATOM 459 CD1 LEU A 58 16.814 -14.384 39.059 1.00 32.06 C ANISOU 459 CD1 LEU A 58 4122 4070 3988 -8 -74 44 C ATOM 460 CD2 LEU A 58 14.404 -13.824 38.731 1.00 31.29 C ANISOU 460 CD2 LEU A 58 3952 3921 4016 -49 -45 27 C ATOM 461 N PHE A 59 16.819 -11.928 35.112 1.00 27.02 N ANISOU 461 N PHE A 59 3373 3506 3387 -79 -5 -12 N ATOM 462 CA PHE A 59 16.828 -12.585 33.806 1.00 26.25 C ANISOU 462 CA PHE A 59 3319 3359 3295 -24 -78 107 C ATOM 463 C PHE A 59 18.240 -12.568 33.244 1.00 27.35 C ANISOU 463 C PHE A 59 3382 3582 3430 58 -46 75 C ATOM 464 O PHE A 59 18.723 -13.569 32.716 1.00 27.27 O ANISOU 464 O PHE A 59 3426 3432 3504 -118 -42 36 O ATOM 465 CB PHE A 59 15.841 -11.930 32.853 1.00 24.59 C ANISOU 465 CB PHE A 59 3033 3230 3079 -52 24 -18 C ATOM 466 CG PHE A 59 14.424 -11.814 33.337 1.00 23.06 C ANISOU 466 CG PHE A 59 2948 2973 2841 -87 -51 -5 C ATOM 467 CD1 PHE A 59 13.656 -10.732 32.959 1.00 22.12 C ANISOU 467 CD1 PHE A 59 2780 2871 2752 -122 11 -80 C ATOM 468 CD2 PHE A 59 13.854 -12.791 34.160 1.00 23.11 C ANISOU 468 CD2 PHE A 59 2868 3040 2871 -79 -5 25 C ATOM 469 CE1 PHE A 59 12.342 -10.596 33.383 1.00 21.69 C ANISOU 469 CE1 PHE A 59 2740 2867 2634 -117 -85 -79 C ATOM 470 CE2 PHE A 59 12.545 -12.635 34.590 1.00 22.50 C ANISOU 470 CE2 PHE A 59 2830 2899 2820 -52 -47 -37 C ATOM 471 CZ PHE A 59 11.788 -11.548 34.199 1.00 21.47 C ANISOU 471 CZ PHE A 59 2692 2800 2666 -119 -66 -80 C ATOM 472 N LYS A 60 18.924 -11.424 33.362 1.00 29.10 N ANISOU 472 N LYS A 60 3658 3703 3696 -70 -176 79 N ATOM 473 CA LYS A 60 20.311 -11.358 32.862 1.00 31.86 C ANISOU 473 CA LYS A 60 3881 4181 4044 16 18 58 C ATOM 474 C LYS A 60 21.244 -12.349 33.551 1.00 32.10 C ANISOU 474 C LYS A 60 3967 4117 4113 -13 -56 30 C ATOM 475 O LYS A 60 22.102 -12.970 32.891 1.00 31.94 O ANISOU 475 O LYS A 60 3896 4123 4117 -89 -22 28 O ATOM 476 CB LYS A 60 20.852 -9.936 33.014 1.00 34.04 C ANISOU 476 CB LYS A 60 4241 4284 4407 -88 14 -43 C ATOM 477 CG LYS A 60 20.201 -8.930 32.053 1.00 36.91 C ANISOU 477 CG LYS A 60 4645 4672 4706 45 -58 112 C ATOM 478 CD LYS A 60 20.542 -9.284 30.616 1.00 39.21 C ANISOU 478 CD LYS A 60 5020 5022 4857 -15 38 -20 C ATOM 479 CE LYS A 60 19.595 -8.641 29.616 1.00 40.71 C ANISOU 479 CE LYS A 60 5140 5158 5169 35 -60 31 C ATOM 480 NZ LYS A 60 19.629 -7.163 29.662 1.00 41.42 N ANISOU 480 NZ LYS A 60 5283 5165 5289 -5 -3 3 N ATOM 481 N LYS A 61 21.056 -12.543 34.861 1.00 32.16 N ANISOU 481 N LYS A 61 3980 4164 4075 -23 -57 4 N ATOM 482 CA LYS A 61 21.900 -13.477 35.609 1.00 32.41 C ANISOU 482 CA LYS A 61 3979 4193 4142 6 -50 18 C ATOM 483 C LYS A 61 21.665 -14.917 35.177 1.00 32.38 C ANISOU 483 C LYS A 61 3915 4211 4178 1 -48 -2 C ATOM 484 O LYS A 61 22.571 -15.743 35.023 1.00 31.90 O ANISOU 484 O LYS A 61 3691 4333 4096 -15 -168 -33 O ATOM 485 CB LYS A 61 21.665 -13.330 37.106 1.00 33.10 C ANISOU 485 CB LYS A 61 4037 4360 4179 -37 5 -5 C ATOM 486 N ILE A 62 20.401 -15.275 34.930 1.00 32.01 N ANISOU 486 N ILE A 62 3904 4177 4081 -20 -94 24 N ATOM 487 CA ILE A 62 20.093 -16.612 34.436 1.00 31.50 C ANISOU 487 CA ILE A 62 3820 4097 4050 -1 -72 42 C ATOM 488 C ILE A 62 20.654 -16.784 33.033 1.00 31.90 C ANISOU 488 C ILE A 62 3795 4167 4159 -23 -17 -33 C ATOM 489 O ILE A 62 21.189 -17.832 32.688 1.00 31.44 O ANISOU 489 O ILE A 62 3721 4071 4155 13 -65 91 O ATOM 490 CB ILE A 62 18.565 -16.831 34.450 1.00 31.07 C ANISOU 490 CB ILE A 62 3821 4010 3976 2 -22 36 C ATOM 491 CG1 ILE A 62 18.093 -16.798 35.906 1.00 31.39 C ANISOU 491 CG1 ILE A 62 3848 4103 3976 48 -4 16 C ATOM 492 CG2 ILE A 62 18.205 -18.138 33.753 1.00 30.61 C ANISOU 492 CG2 ILE A 62 3771 3973 3887 39 -64 55 C ATOM 493 CD1 ILE A 62 16.596 -16.731 36.101 1.00 31.32 C ANISOU 493 CD1 ILE A 62 3849 4047 4004 -16 3 98 C ATOM 494 N GLU A 63 20.592 -15.721 32.215 1.00 32.98 N ANISOU 494 N GLU A 63 3889 4248 4394 -30 -83 65 N ATOM 495 CA GLU A 63 21.061 -15.820 30.843 1.00 35.83 C ANISOU 495 CA GLU A 63 4459 4662 4493 -23 12 1 C ATOM 496 C GLU A 63 22.573 -16.044 30.762 1.00 37.84 C ANISOU 496 C GLU A 63 4562 4915 4902 70 41 20 C ATOM 497 O GLU A 63 23.062 -16.669 29.816 1.00 36.88 O ANISOU 497 O GLU A 63 4391 4875 4746 54 -74 53 O ATOM 498 CB GLU A 63 20.668 -14.575 30.054 1.00 36.31 C ANISOU 498 CB GLU A 63 4451 4602 4744 -8 -24 18 C ATOM 499 CG GLU A 63 20.888 -14.696 28.558 1.00 38.12 C ANISOU 499 CG GLU A 63 4780 4905 4798 -19 16 -29 C ATOM 500 CD GLU A 63 20.589 -13.378 27.850 1.00 40.25 C ANISOU 500 CD GLU A 63 5118 5051 5123 48 -24 63 C ATOM 501 OE1 GLU A 63 21.237 -13.096 26.817 1.00 41.17 O ANISOU 501 OE1 GLU A 63 5219 5273 5150 48 20 35 O ATOM 502 OE2 GLU A 63 19.708 -12.608 28.302 1.00 40.98 O ANISOU 502 OE2 GLU A 63 5239 5149 5181 87 24 -19 O ATOM 503 N GLU A 64 23.326 -15.607 31.768 1.00 40.59 N ANISOU 503 N GLU A 64 5060 5259 5103 -78 -100 -43 N ATOM 504 CA GLU A 64 24.746 -15.968 31.853 1.00 43.24 C ANISOU 504 CA GLU A 64 5212 5691 5525 39 -44 -30 C ATOM 505 C GLU A 64 24.920 -17.477 31.902 1.00 45.15 C ANISOU 505 C GLU A 64 5654 5751 5751 46 -81 -21 C ATOM 506 O GLU A 64 25.809 -18.007 31.228 1.00 45.96 O ANISOU 506 O GLU A 64 5653 5966 5842 42 -53 -38 O ATOM 507 CB GLU A 64 25.408 -15.283 33.035 1.00 43.57 C ANISOU 507 CB GLU A 64 5365 5669 5520 -5 -52 -32 C ATOM 508 N LYS A 65 24.087 -18.194 32.647 1.00 46.60 N ANISOU 508 N LYS A 65 5786 6016 5905 -12 1 35 N ATOM 509 CA LYS A 65 24.117 -19.650 32.643 1.00 48.11 C ANISOU 509 CA LYS A 65 6027 6062 6189 32 5 21 C ATOM 510 C LYS A 65 23.540 -20.214 31.352 1.00 49.51 C ANISOU 510 C LYS A 65 6226 6323 6260 9 -37 -18 C ATOM 511 O LYS A 65 24.168 -21.011 30.651 1.00 50.76 O ANISOU 511 O LYS A 65 6367 6439 6479 70 55 -47 O ATOM 512 CB LYS A 65 23.392 -20.190 33.869 1.00 47.95 C ANISOU 512 CB LYS A 65 6027 6070 6122 35 -17 4 C ATOM 513 N THR A 66 22.334 -19.793 30.989 1.00 49.71 N ANISOU 513 N THR A 66 6256 6345 6287 27 -59 6 N ATOM 514 CA THR A 66 21.612 -20.308 29.835 1.00 49.33 C ANISOU 514 CA THR A 66 6229 6303 6211 26 8 16 C ATOM 515 C THR A 66 22.316 -20.028 28.512 1.00 48.53 C ANISOU 515 C THR A 66 6123 6121 6194 30 -6 0 C ATOM 516 O THR A 66 22.308 -20.841 27.591 1.00 49.38 O ANISOU 516 O THR A 66 6279 6270 6214 74 -26 -52 O ATOM 517 CB THR A 66 20.219 -19.621 29.778 1.00 49.84 C ANISOU 517 CB THR A 66 6205 6417 6316 5 -10 -20 C ATOM 518 OG1 THR A 66 19.438 -20.026 30.916 1.00 50.63 O ANISOU 518 OG1 THR A 66 6340 6531 6367 15 26 28 O ATOM 519 CG2 THR A 66 19.451 -20.027 28.545 1.00 50.39 C ANISOU 519 CG2 THR A 66 6349 6492 6306 0 -32 -1 C ATOM 520 N ASN A 67 22.787 -18.798 28.340 1.00 46.95 N ANISOU 520 N ASN A 67 5849 6088 5902 49 12 36 N ATOM 521 CA ASN A 67 23.166 -18.224 27.061 1.00 45.41 C ANISOU 521 CA ASN A 67 5596 5887 5772 50 -62 -25 C ATOM 522 C ASN A 67 22.015 -18.119 26.073 1.00 43.87 C ANISOU 522 C ASN A 67 5365 5706 5596 38 105 -7 C ATOM 523 O ASN A 67 22.252 -18.019 24.859 1.00 45.04 O ANISOU 523 O ASN A 67 5604 5885 5623 60 59 30 O ATOM 524 CB ASN A 67 24.307 -19.022 26.443 1.00 46.05 C ANISOU 524 CB ASN A 67 5775 5906 5816 85 -10 -28 C ATOM 525 N HIS A 68 20.757 -18.143 26.500 1.00 40.63 N ANISOU 525 N HIS A 68 5135 5242 5060 53 -74 23 N ATOM 526 CA HIS A 68 19.605 -18.062 25.636 1.00 37.61 C ANISOU 526 CA HIS A 68 4720 4833 4736 189 205 -42 C ATOM 527 C HIS A 68 18.589 -17.143 26.337 1.00 32.82 C ANISOU 527 C HIS A 68 4132 4162 4176 -41 -75 132 C ATOM 528 O HIS A 68 18.126 -17.504 27.419 1.00 30.96 O ANISOU 528 O HIS A 68 3660 3964 4138 148 -23 -24 O ATOM 529 CB HIS A 68 18.878 -19.364 25.362 1.00 41.22 C ANISOU 529 CB HIS A 68 5213 5197 5253 -113 -23 5 C ATOM 530 CG HIS A 68 19.685 -20.481 24.794 1.00 44.63 C ANISOU 530 CG HIS A 68 5639 5576 5743 104 46 -90 C ATOM 531 ND1 HIS A 68 19.934 -21.642 25.505 1.00 46.15 N ANISOU 531 ND1 HIS A 68 5894 5749 5892 59 11 41 N ATOM 532 CD2 HIS A 68 20.312 -20.607 23.596 1.00 45.77 C ANISOU 532 CD2 HIS A 68 5829 5811 5748 30 63 -30 C ATOM 533 CE1 HIS A 68 20.676 -22.448 24.757 1.00 46.85 C ANISOU 533 CE1 HIS A 68 5991 5870 5940 75 45 -17 C ATOM 534 NE2 HIS A 68 20.918 -21.848 23.603 1.00 46.85 N ANISOU 534 NE2 HIS A 68 5983 5867 5951 86 63 -15 N ATOM 535 N ASP A 69 18.303 -16.033 25.711 1.00 28.43 N ANISOU 535 N ASP A 69 3371 3867 3564 -6 96 -145 N ATOM 536 CA ASP A 69 17.606 -14.943 26.385 1.00 26.94 C ANISOU 536 CA ASP A 69 3126 3594 3517 -47 28 8 C ATOM 537 C ASP A 69 16.174 -15.336 26.733 1.00 23.72 C ANISOU 537 C ASP A 69 2980 3062 2970 22 -39 -82 C ATOM 538 O ASP A 69 15.731 -15.074 27.861 1.00 21.50 O ANISOU 538 O ASP A 69 2443 2889 2838 -69 -109 22 O ATOM 539 CB ASP A 69 17.714 -13.674 25.555 1.00 28.74 C ANISOU 539 CB ASP A 69 3507 3622 3791 17 93 81 C ATOM 540 CG ASP A 69 17.311 -13.785 24.104 1.00 31.26 C ANISOU 540 CG ASP A 69 3837 4091 3948 14 -4 -3 C ATOM 541 OD1 ASP A 69 17.340 -12.754 23.359 1.00 32.75 O ANISOU 541 OD1 ASP A 69 4017 4265 4161 38 -26 131 O ATOM 542 OD2 ASP A 69 16.959 -14.887 23.620 1.00 32.15 O ANISOU 542 OD2 ASP A 69 3965 4117 4135 16 43 -23 O ATOM 543 N VAL A 70 15.454 -15.953 25.794 1.00 21.82 N ANISOU 543 N VAL A 70 2683 2844 2763 40 61 25 N ATOM 544 CA VAL A 70 14.040 -16.243 26.103 1.00 20.74 C ANISOU 544 CA VAL A 70 2644 2611 2624 1 -50 41 C ATOM 545 C VAL A 70 13.926 -17.350 27.143 1.00 20.53 C ANISOU 545 C VAL A 70 2600 2717 2483 1 -24 18 C ATOM 546 O VAL A 70 13.085 -17.288 28.044 1.00 18.66 O ANISOU 546 O VAL A 70 2320 2458 2311 45 -117 76 O ATOM 547 CB VAL A 70 13.236 -16.617 24.848 1.00 21.12 C ANISOU 547 CB VAL A 70 2811 2657 2558 -5 -29 25 C ATOM 548 CG1 VAL A 70 11.798 -16.976 25.188 1.00 20.81 C ANISOU 548 CG1 VAL A 70 2754 2672 2482 -12 -165 -6 C ATOM 549 CG2 VAL A 70 13.272 -15.419 23.889 1.00 21.34 C ANISOU 549 CG2 VAL A 70 2903 2601 2604 -95 -125 -18 C ATOM 550 N VAL A 71 14.791 -18.367 26.996 1.00 21.44 N ANISOU 550 N VAL A 71 2753 2684 2710 57 8 9 N ATOM 551 CA VAL A 71 14.798 -19.441 28.007 1.00 23.47 C ANISOU 551 CA VAL A 71 3168 2900 2849 44 -52 99 C ATOM 552 C VAL A 71 15.063 -18.896 29.401 1.00 21.07 C ANISOU 552 C VAL A 71 2653 2543 2809 67 -8 91 C ATOM 553 O VAL A 71 14.429 -19.312 30.370 1.00 20.42 O ANISOU 553 O VAL A 71 2664 2393 2700 105 -53 22 O ATOM 554 CB VAL A 71 15.844 -20.526 27.649 1.00 26.21 C ANISOU 554 CB VAL A 71 3445 3185 3330 170 27 6 C ATOM 555 CG1 VAL A 71 15.974 -21.548 28.786 1.00 27.86 C ANISOU 555 CG1 VAL A 71 3785 3323 3479 91 -26 106 C ATOM 556 CG2 VAL A 71 15.402 -21.238 26.376 1.00 27.83 C ANISOU 556 CG2 VAL A 71 3741 3449 3387 16 38 -55 C ATOM 557 N ALA A 72 15.992 -17.966 29.552 1.00 20.31 N ANISOU 557 N ALA A 72 2576 2500 2641 103 -71 73 N ATOM 558 CA ALA A 72 16.295 -17.392 30.856 1.00 20.58 C ANISOU 558 CA ALA A 72 2549 2602 2669 -15 -18 27 C ATOM 559 C ALA A 72 15.095 -16.616 31.398 1.00 19.77 C ANISOU 559 C ALA A 72 2386 2600 2528 -56 -89 87 C ATOM 560 O ALA A 72 14.829 -16.689 32.607 1.00 20.29 O ANISOU 560 O ALA A 72 2378 2785 2545 -33 -51 103 O ATOM 561 CB ALA A 72 17.488 -16.441 30.725 1.00 21.23 C ANISOU 561 CB ALA A 72 2600 2751 2717 -108 -80 49 C ATOM 562 N PHE A 73 14.440 -15.849 30.532 1.00 17.83 N ANISOU 562 N PHE A 73 2155 2262 2356 -130 -12 37 N ATOM 563 CA PHE A 73 13.195 -15.192 30.954 1.00 17.06 C ANISOU 563 CA PHE A 73 2229 2166 2086 -70 -85 131 C ATOM 564 C PHE A 73 12.141 -16.184 31.417 1.00 16.69 C ANISOU 564 C PHE A 73 2171 2143 2029 -6 -25 103 C ATOM 565 O PHE A 73 11.506 -15.976 32.461 1.00 15.98 O ANISOU 565 O PHE A 73 2110 1984 1978 -254 67 0 O ATOM 566 CB PHE A 73 12.683 -14.330 29.807 1.00 16.98 C ANISOU 566 CB PHE A 73 2278 2154 2019 -33 -55 114 C ATOM 567 CG PHE A 73 11.278 -13.857 29.879 1.00 16.16 C ANISOU 567 CG PHE A 73 2241 2033 1866 -54 12 227 C ATOM 568 CD1 PHE A 73 10.946 -12.703 30.567 1.00 16.43 C ANISOU 568 CD1 PHE A 73 2242 2122 1877 7 48 240 C ATOM 569 CD2 PHE A 73 10.274 -14.576 29.219 1.00 16.35 C ANISOU 569 CD2 PHE A 73 2166 2099 1945 -38 18 267 C ATOM 570 CE1 PHE A 73 9.632 -12.272 30.615 1.00 16.64 C ANISOU 570 CE1 PHE A 73 2200 2145 1976 -21 16 221 C ATOM 571 CE2 PHE A 73 8.959 -14.144 29.286 1.00 16.42 C ANISOU 571 CE2 PHE A 73 2218 2106 1915 -26 50 231 C ATOM 572 CZ PHE A 73 8.644 -13.006 29.980 1.00 16.35 C ANISOU 572 CZ PHE A 73 2312 2043 1856 -21 1 259 C ATOM 573 N VAL A 74 11.933 -17.253 30.644 1.00 16.87 N ANISOU 573 N VAL A 74 2268 2120 2023 -31 -163 153 N ATOM 574 CA VAL A 74 10.938 -18.250 31.031 1.00 18.35 C ANISOU 574 CA VAL A 74 2409 2265 2299 -101 -23 129 C ATOM 575 C VAL A 74 11.295 -18.897 32.368 1.00 18.74 C ANISOU 575 C VAL A 74 2536 2338 2247 -23 -23 78 C ATOM 576 O VAL A 74 10.407 -19.125 33.205 1.00 17.24 O ANISOU 576 O VAL A 74 2401 1982 2169 -33 -78 183 O ATOM 577 CB VAL A 74 10.785 -19.334 29.941 1.00 19.50 C ANISOU 577 CB VAL A 74 2578 2468 2363 -102 -77 52 C ATOM 578 CG1 VAL A 74 9.912 -20.494 30.432 1.00 20.25 C ANISOU 578 CG1 VAL A 74 2704 2451 2540 -169 -83 -7 C ATOM 579 CG2 VAL A 74 10.227 -18.693 28.672 1.00 19.75 C ANISOU 579 CG2 VAL A 74 2531 2618 2357 -126 -81 80 C ATOM 580 N GLU A 75 12.562 -19.214 32.569 1.00 20.58 N ANISOU 580 N GLU A 75 2581 2615 2624 -27 -51 10 N ATOM 581 CA GLU A 75 12.981 -19.780 33.863 1.00 22.92 C ANISOU 581 CA GLU A 75 3063 2902 2745 16 -90 81 C ATOM 582 C GLU A 75 12.791 -18.795 35.015 1.00 21.53 C ANISOU 582 C GLU A 75 2704 2816 2662 -55 -50 114 C ATOM 583 O GLU A 75 12.334 -19.114 36.101 1.00 21.25 O ANISOU 583 O GLU A 75 2745 2753 2577 -66 -105 152 O ATOM 584 CB GLU A 75 14.455 -20.215 33.763 1.00 26.53 C ANISOU 584 CB GLU A 75 3105 3484 3493 59 -6 142 C ATOM 585 CG GLU A 75 14.618 -21.353 32.776 1.00 31.15 C ANISOU 585 CG GLU A 75 4075 3907 3854 -3 -28 -115 C ATOM 586 CD GLU A 75 15.984 -22.015 32.775 1.00 35.10 C ANISOU 586 CD GLU A 75 4285 4483 4570 153 -6 -30 C ATOM 587 OE1 GLU A 75 16.901 -21.572 33.506 1.00 36.84 O ANISOU 587 OE1 GLU A 75 4420 4690 4887 53 -126 -66 O ATOM 588 OE2 GLU A 75 16.119 -23.021 32.037 1.00 36.83 O ANISOU 588 OE2 GLU A 75 4735 4639 4620 125 20 -121 O ATOM 589 N GLY A 76 13.126 -17.527 34.779 1.00 20.55 N ANISOU 589 N GLY A 76 2653 2646 2510 76 -162 -15 N ATOM 590 CA GLY A 76 12.987 -16.477 35.799 1.00 19.39 C ANISOU 590 CA GLY A 76 2462 2586 2320 56 -81 72 C ATOM 591 C GLY A 76 11.528 -16.273 36.183 1.00 19.30 C ANISOU 591 C GLY A 76 2488 2559 2286 -35 -64 71 C ATOM 592 O GLY A 76 11.200 -16.192 37.376 1.00 19.49 O ANISOU 592 O GLY A 76 2573 2636 2196 14 -131 71 O ATOM 593 N ILE A 77 10.634 -16.145 35.194 1.00 17.73 N ANISOU 593 N ILE A 77 2305 2280 2152 -47 5 156 N ATOM 594 CA ILE A 77 9.210 -16.052 35.494 1.00 18.12 C ANISOU 594 CA ILE A 77 2314 2336 2234 -23 -39 161 C ATOM 595 C ILE A 77 8.751 -17.337 36.197 1.00 19.33 C ANISOU 595 C ILE A 77 2528 2439 2379 -88 -3 158 C ATOM 596 O ILE A 77 8.006 -17.261 37.181 1.00 19.73 O ANISOU 596 O ILE A 77 2538 2576 2382 -74 37 147 O ATOM 597 CB ILE A 77 8.357 -15.812 34.245 1.00 17.20 C ANISOU 597 CB ILE A 77 2167 2244 2125 -52 36 145 C ATOM 598 CG1 ILE A 77 8.726 -14.457 33.580 1.00 16.84 C ANISOU 598 CG1 ILE A 77 2163 2161 2075 -92 7 78 C ATOM 599 CG2 ILE A 77 6.876 -15.813 34.572 1.00 16.38 C ANISOU 599 CG2 ILE A 77 2146 2293 1783 -169 10 282 C ATOM 600 CD1 ILE A 77 8.420 -13.201 34.379 1.00 17.71 C ANISOU 600 CD1 ILE A 77 2158 2241 2330 -35 167 65 C ATOM 601 N GLY A 78 9.216 -18.480 35.728 1.00 20.75 N ANISOU 601 N GLY A 78 2735 2574 2575 87 -85 74 N ATOM 602 CA GLY A 78 8.833 -19.766 36.329 1.00 22.93 C ANISOU 602 CA GLY A 78 3032 2768 2912 -58 64 129 C ATOM 603 C GLY A 78 9.095 -19.778 37.822 1.00 24.30 C ANISOU 603 C GLY A 78 3192 3053 2990 43 16 97 C ATOM 604 O GLY A 78 8.255 -20.301 38.566 1.00 25.79 O ANISOU 604 O GLY A 78 3524 3252 3021 -30 141 162 O ATOM 605 N SER A 79 10.131 -19.156 38.309 1.00 24.95 N ANISOU 605 N SER A 79 3184 3161 3133 1 -3 59 N ATOM 606 CA SER A 79 10.519 -19.097 39.698 1.00 26.17 C ANISOU 606 CA SER A 79 3429 3370 3143 27 36 51 C ATOM 607 C SER A 79 9.583 -18.222 40.523 1.00 25.61 C ANISOU 607 C SER A 79 3323 3324 3083 82 -71 97 C ATOM 608 O SER A 79 9.656 -18.221 41.762 1.00 27.18 O ANISOU 608 O SER A 79 3541 3753 3033 66 -31 238 O ATOM 609 CB SER A 79 11.970 -18.611 39.845 1.00 27.04 C ANISOU 609 CB SER A 79 3465 3527 3280 11 -74 51 C ATOM 610 OG SER A 79 12.068 -17.197 39.723 1.00 27.83 O ANISOU 610 OG SER A 79 3634 3627 3315 -123 -91 45 O ATOM 611 N MET A 80 8.719 -17.439 39.896 1.00 22.84 N ANISOU 611 N MET A 80 2969 3094 2614 -47 -4 54 N ATOM 612 CA MET A 80 7.773 -16.578 40.566 1.00 21.46 C ANISOU 612 CA MET A 80 2919 2690 2544 -94 -119 134 C ATOM 613 C MET A 80 6.336 -17.100 40.552 1.00 20.66 C ANISOU 613 C MET A 80 2851 2603 2394 -46 5 67 C ATOM 614 O MET A 80 5.477 -16.553 41.253 1.00 19.75 O ANISOU 614 O MET A 80 2965 2461 2076 -78 -25 40 O ATOM 615 CB MET A 80 7.753 -15.207 39.860 1.00 21.05 C ANISOU 615 CB MET A 80 2714 2522 2764 -182 -7 91 C ATOM 616 CG MET A 80 9.085 -14.463 39.801 1.00 18.49 C ANISOU 616 CG MET A 80 2641 1911 2473 -3 -125 427 C ATOM 617 SD MET A 80 8.936 -12.896 38.764 1.00 12.57 S ANISOU 617 SD MET A 80 1701 1219 1856 -313 -111 455 S ATOM 618 CE MET A 80 10.653 -12.832 38.277 1.00 18.67 C ANISOU 618 CE MET A 80 2091 2505 2497 30 6 25 C ATOM 619 N ILE A 81 6.038 -18.087 39.685 1.00 19.81 N ANISOU 619 N ILE A 81 2778 2551 2197 -102 35 81 N ATOM 620 CA ILE A 81 4.628 -18.414 39.461 1.00 19.66 C ANISOU 620 CA ILE A 81 2781 2550 2140 -21 -25 -27 C ATOM 621 C ILE A 81 4.240 -19.795 39.966 1.00 20.63 C ANISOU 621 C ILE A 81 2889 2655 2293 -134 49 -29 C ATOM 622 O ILE A 81 3.083 -20.181 39.722 1.00 19.83 O ANISOU 622 O ILE A 81 2836 2748 1951 -191 168 14 O ATOM 623 CB ILE A 81 4.230 -18.262 37.959 1.00 19.23 C ANISOU 623 CB ILE A 81 2731 2405 2173 25 13 0 C ATOM 624 CG1 ILE A 81 5.056 -19.202 37.056 1.00 18.73 C ANISOU 624 CG1 ILE A 81 2584 2378 2153 -31 -56 -115 C ATOM 625 CG2 ILE A 81 4.446 -16.798 37.539 1.00 18.36 C ANISOU 625 CG2 ILE A 81 2739 2319 1919 -11 -12 -132 C ATOM 626 CD1 ILE A 81 4.537 -19.191 35.607 1.00 18.52 C ANISOU 626 CD1 ILE A 81 2582 2329 2124 -62 36 32 C ATOM 627 N GLY A 82 5.115 -20.496 40.662 1.00 22.11 N ANISOU 627 N GLY A 82 3044 2702 2655 -9 -33 -34 N ATOM 628 CA GLY A 82 4.684 -21.742 41.331 1.00 24.07 C ANISOU 628 CA GLY A 82 3322 2965 2859 -91 41 116 C ATOM 629 C GLY A 82 4.249 -22.818 40.331 1.00 24.92 C ANISOU 629 C GLY A 82 3347 3138 2983 -16 -50 -2 C ATOM 630 O GLY A 82 4.846 -22.960 39.258 1.00 24.14 O ANISOU 630 O GLY A 82 3267 3022 2883 -38 -63 59 O ATOM 631 N GLU A 83 3.186 -23.553 40.641 1.00 25.57 N ANISOU 631 N GLU A 83 3407 3325 2984 -52 -12 91 N ATOM 632 CA GLU A 83 2.769 -24.695 39.813 1.00 28.19 C ANISOU 632 CA GLU A 83 3851 3544 3317 25 -178 -64 C ATOM 633 C GLU A 83 2.154 -24.256 38.487 1.00 25.20 C ANISOU 633 C GLU A 83 3423 2994 3157 -14 37 18 C ATOM 634 O GLU A 83 1.979 -25.052 37.557 1.00 24.43 O ANISOU 634 O GLU A 83 3479 2885 2920 8 40 159 O ATOM 635 CB GLU A 83 1.719 -25.558 40.521 1.00 33.28 C ANISOU 635 CB GLU A 83 4254 4057 4335 -207 148 -13 C ATOM 636 CG GLU A 83 2.141 -26.051 41.889 1.00 39.55 C ANISOU 636 CG GLU A 83 5258 5102 4669 -96 -95 129 C ATOM 637 CD GLU A 83 3.027 -27.269 41.896 1.00 44.09 C ANISOU 637 CD GLU A 83 5620 5485 5650 140 -16 23 C ATOM 638 OE1 GLU A 83 3.760 -27.539 40.920 1.00 45.84 O ANISOU 638 OE1 GLU A 83 5912 5838 5666 70 101 80 O ATOM 639 OE2 GLU A 83 3.000 -28.014 42.917 1.00 46.55 O ANISOU 639 OE2 GLU A 83 6027 5853 5806 3 46 154 O ATOM 640 N ASP A 84 1.824 -22.956 38.369 1.00 21.51 N ANISOU 640 N ASP A 84 2920 2858 2396 -16 51 -37 N ATOM 641 CA ASP A 84 1.377 -22.451 37.083 1.00 20.74 C ANISOU 641 CA ASP A 84 2764 2649 2467 -9 90 14 C ATOM 642 C ASP A 84 2.489 -22.452 36.021 1.00 19.35 C ANISOU 642 C ASP A 84 2562 2475 2314 27 -12 -1 C ATOM 643 O ASP A 84 2.169 -22.229 34.845 1.00 18.48 O ANISOU 643 O ASP A 84 2453 2404 2163 64 127 -26 O ATOM 644 CB ASP A 84 0.788 -21.050 37.216 1.00 21.53 C ANISOU 644 CB ASP A 84 2902 2677 2600 53 30 51 C ATOM 645 CG ASP A 84 -0.566 -21.075 37.912 1.00 23.43 C ANISOU 645 CG ASP A 84 3010 2969 2923 -3 84 44 C ATOM 646 OD1 ASP A 84 -1.299 -22.070 37.805 1.00 25.33 O ANISOU 646 OD1 ASP A 84 3391 2972 3263 -123 79 55 O ATOM 647 OD2 ASP A 84 -0.924 -20.066 38.559 1.00 23.70 O ANISOU 647 OD2 ASP A 84 3163 2947 2893 -52 143 3 O ATOM 648 N SER A 85 3.739 -22.705 36.351 1.00 18.51 N ANISOU 648 N SER A 85 2531 2328 2173 -36 -95 20 N ATOM 649 CA SER A 85 4.795 -22.822 35.369 1.00 20.20 C ANISOU 649 CA SER A 85 2592 2532 2551 -80 57 28 C ATOM 650 C SER A 85 4.537 -23.953 34.366 1.00 20.94 C ANISOU 650 C SER A 85 2697 2637 2625 -148 42 -4 C ATOM 651 O SER A 85 4.976 -23.795 33.219 1.00 20.06 O ANISOU 651 O SER A 85 2395 2608 2617 -288 37 49 O ATOM 652 CB SER A 85 6.176 -23.005 35.987 1.00 22.09 C ANISOU 652 CB SER A 85 2738 2846 2807 -4 -48 49 C ATOM 653 OG SER A 85 6.210 -24.258 36.633 1.00 24.53 O ANISOU 653 OG SER A 85 3161 2969 3192 124 -71 110 O ATOM 654 N ARG A 86 3.730 -24.958 34.731 1.00 20.44 N ANISOU 654 N ARG A 86 2650 2503 2615 -112 34 125 N ATOM 655 CA ARG A 86 3.363 -26.012 33.790 1.00 22.51 C ANISOU 655 CA ARG A 86 2956 2856 2742 -50 -86 -35 C ATOM 656 C ARG A 86 2.619 -25.463 32.585 1.00 20.53 C ANISOU 656 C ARG A 86 2758 2453 2589 -45 115 9 C ATOM 657 O ARG A 86 2.588 -26.128 31.534 1.00 21.21 O ANISOU 657 O ARG A 86 2989 2435 2633 -16 46 -92 O ATOM 658 CB ARG A 86 2.398 -27.020 34.464 1.00 26.84 C ANISOU 658 CB ARG A 86 3480 3166 3551 -287 118 79 C ATOM 659 CG ARG A 86 2.887 -27.621 35.764 1.00 32.34 C ANISOU 659 CG ARG A 86 4256 4109 3924 15 -134 153 C ATOM 660 CD ARG A 86 1.794 -28.453 36.468 1.00 36.48 C ANISOU 660 CD ARG A 86 4664 4545 4653 -168 135 231 C ATOM 661 NE ARG A 86 0.933 -27.641 37.323 1.00 39.36 N ANISOU 661 NE ARG A 86 5057 4929 4969 50 112 6 N ATOM 662 CZ ARG A 86 -0.229 -27.955 37.878 1.00 40.82 C ANISOU 662 CZ ARG A 86 5169 5206 5136 -43 129 51 C ATOM 663 NH1 ARG A 86 -0.764 -29.161 37.693 1.00 41.97 N ANISOU 663 NH1 ARG A 86 5417 5277 5252 -91 72 -19 N ATOM 664 NH2 ARG A 86 -0.906 -27.092 38.621 1.00 41.09 N ANISOU 664 NH2 ARG A 86 5290 5196 5127 -12 89 8 N ATOM 665 N PHE A 87 1.914 -24.340 32.729 1.00 17.72 N ANISOU 665 N PHE A 87 2453 2200 2081 -177 55 14 N ATOM 666 CA PHE A 87 1.044 -23.808 31.694 1.00 17.61 C ANISOU 666 CA PHE A 87 2375 2106 2208 -173 58 85 C ATOM 667 C PHE A 87 1.668 -22.614 30.945 1.00 16.42 C ANISOU 667 C PHE A 87 2208 1990 2043 -54 74 -4 C ATOM 668 O PHE A 87 0.997 -22.051 30.085 1.00 16.55 O ANISOU 668 O PHE A 87 2340 1934 2015 -205 87 181 O ATOM 669 CB PHE A 87 -0.270 -23.341 32.344 1.00 19.23 C ANISOU 669 CB PHE A 87 2443 2435 2430 -23 4 30 C ATOM 670 CG PHE A 87 -0.911 -24.474 33.122 1.00 22.25 C ANISOU 670 CG PHE A 87 2755 2811 2889 -175 63 224 C ATOM 671 CD1 PHE A 87 -1.160 -24.296 34.474 1.00 23.97 C ANISOU 671 CD1 PHE A 87 3072 3072 2964 -77 17 118 C ATOM 672 CD2 PHE A 87 -1.225 -25.668 32.505 1.00 23.47 C ANISOU 672 CD2 PHE A 87 3052 2916 2951 -48 -13 92 C ATOM 673 CE1 PHE A 87 -1.766 -25.346 35.188 1.00 25.52 C ANISOU 673 CE1 PHE A 87 3305 3201 3191 -147 56 132 C ATOM 674 CE2 PHE A 87 -1.839 -26.694 33.206 1.00 24.86 C ANISOU 674 CE2 PHE A 87 3197 3076 3174 -155 25 133 C ATOM 675 CZ PHE A 87 -2.084 -26.526 34.552 1.00 24.91 C ANISOU 675 CZ PHE A 87 3209 3073 3182 -105 86 186 C ATOM 676 N PHE A 88 2.859 -22.248 31.344 1.00 15.67 N ANISOU 676 N PHE A 88 2206 1903 1843 -165 169 17 N ATOM 677 CA PHE A 88 3.465 -20.993 30.843 1.00 15.30 C ANISOU 677 CA PHE A 88 2108 1905 1798 -156 109 -6 C ATOM 678 C PHE A 88 4.445 -21.367 29.731 1.00 14.52 C ANISOU 678 C PHE A 88 1961 1764 1793 -111 80 21 C ATOM 679 O PHE A 88 5.185 -22.353 29.883 1.00 14.27 O ANISOU 679 O PHE A 88 1928 1777 1718 -106 225 163 O ATOM 680 CB PHE A 88 4.202 -20.290 31.973 1.00 15.60 C ANISOU 680 CB PHE A 88 2081 2023 1824 -56 10 -22 C ATOM 681 CG PHE A 88 4.793 -18.934 31.653 1.00 15.76 C ANISOU 681 CG PHE A 88 2121 2078 1788 -98 -14 11 C ATOM 682 CD1 PHE A 88 4.005 -17.812 31.619 1.00 15.62 C ANISOU 682 CD1 PHE A 88 2264 1995 1675 -105 50 -29 C ATOM 683 CD2 PHE A 88 6.148 -18.825 31.362 1.00 16.57 C ANISOU 683 CD2 PHE A 88 2174 2281 1839 -171 -56 45 C ATOM 684 CE1 PHE A 88 4.554 -16.549 31.366 1.00 16.08 C ANISOU 684 CE1 PHE A 88 2240 2172 1698 -193 -14 86 C ATOM 685 CE2 PHE A 88 6.701 -17.580 31.089 1.00 16.62 C ANISOU 685 CE2 PHE A 88 2221 2204 1891 -96 -81 21 C ATOM 686 CZ PHE A 88 5.911 -16.451 31.075 1.00 15.97 C ANISOU 686 CZ PHE A 88 2185 2142 1740 -112 -99 6 C ATOM 687 N HIS A 89 4.440 -20.628 28.633 1.00 13.52 N ANISOU 687 N HIS A 89 1837 1566 1734 -173 7 -74 N ATOM 688 CA HIS A 89 5.311 -20.931 27.495 1.00 14.42 C ANISOU 688 CA HIS A 89 1814 1749 1914 -158 109 -47 C ATOM 689 C HIS A 89 5.027 -22.341 26.966 1.00 14.74 C ANISOU 689 C HIS A 89 1817 1749 2034 -79 27 -56 C ATOM 690 O HIS A 89 5.942 -23.039 26.555 1.00 15.51 O ANISOU 690 O HIS A 89 1928 1759 2207 -209 208 -179 O ATOM 691 CB HIS A 89 6.786 -20.746 27.854 1.00 15.17 C ANISOU 691 CB HIS A 89 1834 1953 1978 -27 28 12 C ATOM 692 CG HIS A 89 7.674 -20.459 26.660 1.00 16.40 C ANISOU 692 CG HIS A 89 1976 2183 2072 -31 68 77 C ATOM 693 ND1 HIS A 89 8.537 -21.423 26.139 1.00 18.32 N ANISOU 693 ND1 HIS A 89 2334 2415 2210 23 159 -96 N ATOM 694 CD2 HIS A 89 7.844 -19.379 25.896 1.00 15.32 C ANISOU 694 CD2 HIS A 89 1835 1970 2014 20 -55 20 C ATOM 695 CE1 HIS A 89 9.198 -20.918 25.100 1.00 16.45 C ANISOU 695 CE1 HIS A 89 1934 2127 2190 -13 -44 16 C ATOM 696 NE2 HIS A 89 8.794 -19.672 24.958 1.00 17.44 N ANISOU 696 NE2 HIS A 89 2158 2311 2159 27 7 44 N ATOM 697 N TYR A 90 3.777 -22.759 26.939 1.00 13.89 N ANISOU 697 N TYR A 90 1883 1668 1727 -288 79 107 N ATOM 698 CA TYR A 90 3.497 -24.183 26.727 1.00 15.55 C ANISOU 698 CA TYR A 90 2133 1793 1981 -226 16 -110 C ATOM 699 C TYR A 90 3.436 -24.477 25.230 1.00 14.31 C ANISOU 699 C TYR A 90 1800 1787 1849 -192 143 54 C ATOM 700 O TYR A 90 2.559 -23.941 24.543 1.00 14.58 O ANISOU 700 O TYR A 90 1788 1887 1864 -168 180 127 O ATOM 701 CB TYR A 90 2.137 -24.510 27.403 1.00 18.34 C ANISOU 701 CB TYR A 90 2249 2472 2248 -98 191 -42 C ATOM 702 CG TYR A 90 1.915 -26.024 27.342 1.00 23.66 C ANISOU 702 CG TYR A 90 3190 2694 3106 -264 141 53 C ATOM 703 CD1 TYR A 90 0.974 -26.571 26.489 1.00 26.94 C ANISOU 703 CD1 TYR A 90 3440 3403 3395 -200 -114 2 C ATOM 704 CD2 TYR A 90 2.660 -26.887 28.122 1.00 26.62 C ANISOU 704 CD2 TYR A 90 3420 3214 3479 -21 -44 52 C ATOM 705 CE1 TYR A 90 0.767 -27.934 26.431 1.00 29.53 C ANISOU 705 CE1 TYR A 90 3885 3422 3911 -146 -78 31 C ATOM 706 CE2 TYR A 90 2.462 -28.264 28.084 1.00 29.25 C ANISOU 706 CE2 TYR A 90 3905 3353 3854 -126 -35 46 C ATOM 707 CZ TYR A 90 1.511 -28.774 27.225 1.00 30.63 C ANISOU 707 CZ TYR A 90 3941 3712 3984 -99 -124 49 C ATOM 708 OH TYR A 90 1.313 -30.152 27.151 1.00 32.15 O ANISOU 708 OH TYR A 90 4295 3765 4155 -169 -108 80 O ATOM 709 N GLY A 91 4.365 -25.267 24.718 1.00 12.74 N ANISOU 709 N GLY A 91 1753 1503 1586 -243 20 69 N ATOM 710 CA GLY A 91 4.382 -25.600 23.288 1.00 13.24 C ANISOU 710 CA GLY A 91 1806 1592 1631 -174 28 12 C ATOM 711 C GLY A 91 5.063 -24.564 22.397 1.00 13.12 C ANISOU 711 C GLY A 91 1740 1657 1586 -106 14 27 C ATOM 712 O GLY A 91 5.221 -24.750 21.172 1.00 13.82 O ANISOU 712 O GLY A 91 1944 1746 1562 -90 85 -79 O ATOM 713 N LEU A 92 5.510 -23.455 22.975 1.00 13.00 N ANISOU 713 N LEU A 92 1752 1492 1697 -45 -37 53 N ATOM 714 CA LEU A 92 6.069 -22.345 22.213 1.00 13.46 C ANISOU 714 CA LEU A 92 1676 1583 1856 -71 111 52 C ATOM 715 C LEU A 92 7.531 -22.567 21.865 1.00 13.58 C ANISOU 715 C LEU A 92 1667 1627 1868 16 4 93 C ATOM 716 O LEU A 92 8.275 -23.243 22.596 1.00 13.94 O ANISOU 716 O LEU A 92 1545 1795 1957 -131 23 335 O ATOM 717 CB LEU A 92 5.964 -21.025 23.024 1.00 15.18 C ANISOU 717 CB LEU A 92 1918 1741 2108 32 70 -102 C ATOM 718 CG LEU A 92 4.557 -20.562 23.450 1.00 16.26 C ANISOU 718 CG LEU A 92 1992 1934 2251 78 66 -204 C ATOM 719 CD1 LEU A 92 4.566 -19.075 23.823 1.00 15.98 C ANISOU 719 CD1 LEU A 92 1909 1862 2303 165 45 -156 C ATOM 720 CD2 LEU A 92 3.501 -20.812 22.397 1.00 16.62 C ANISOU 720 CD2 LEU A 92 2155 2138 2023 209 -14 -110 C ATOM 721 N THR A 93 7.961 -21.959 20.763 1.00 13.54 N ANISOU 721 N THR A 93 1644 1684 1818 -55 75 8 N ATOM 722 CA THR A 93 9.389 -21.817 20.446 1.00 13.78 C ANISOU 722 CA THR A 93 1634 1731 1870 -136 40 -43 C ATOM 723 C THR A 93 9.798 -20.390 20.785 1.00 13.30 C ANISOU 723 C THR A 93 1529 1650 1874 -94 -5 98 C ATOM 724 O THR A 93 8.991 -19.462 20.877 1.00 12.38 O ANISOU 724 O THR A 93 1527 1437 1740 -191 111 134 O ATOM 725 CB THR A 93 9.656 -22.179 18.959 1.00 14.64 C ANISOU 725 CB THR A 93 1873 1836 1855 -41 -10 12 C ATOM 726 OG1 THR A 93 11.074 -22.362 18.738 1.00 15.55 O ANISOU 726 OG1 THR A 93 1955 1962 1992 58 82 -151 O ATOM 727 CG2 THR A 93 9.132 -21.118 18.003 1.00 13.45 C ANISOU 727 CG2 THR A 93 1754 1685 1670 -99 -16 -78 C ATOM 728 N SER A 94 11.111 -20.190 20.968 1.00 12.69 N ANISOU 728 N SER A 94 1552 1527 1743 -168 -115 162 N ATOM 729 CA SER A 94 11.547 -18.839 21.406 1.00 12.30 C ANISOU 729 CA SER A 94 1546 1487 1639 -61 -145 74 C ATOM 730 C SER A 94 11.104 -17.739 20.451 1.00 11.60 C ANISOU 730 C SER A 94 1478 1466 1463 -62 -31 -8 C ATOM 731 O SER A 94 10.695 -16.684 20.937 1.00 10.95 O ANISOU 731 O SER A 94 1567 1314 1281 -115 -76 35 O ATOM 732 CB SER A 94 13.081 -18.726 21.579 1.00 14.74 C ANISOU 732 CB SER A 94 1578 1945 2079 -30 -94 136 C ATOM 733 OG SER A 94 13.428 -19.611 22.656 1.00 16.61 O ANISOU 733 OG SER A 94 1887 2102 2323 110 -211 172 O ATOM 734 N SER A 95 11.159 -17.998 19.119 1.00 10.97 N ANISOU 734 N SER A 95 1403 1433 1331 -116 -53 19 N ATOM 735 CA SER A 95 10.773 -16.917 18.208 1.00 11.27 C ANISOU 735 CA SER A 95 1341 1474 1468 -106 7 58 C ATOM 736 C SER A 95 9.277 -16.658 18.177 1.00 11.63 C ANISOU 736 C SER A 95 1426 1473 1521 -68 16 59 C ATOM 737 O SER A 95 8.881 -15.595 17.662 1.00 11.20 O ANISOU 737 O SER A 95 1501 1308 1448 -48 -5 -54 O ATOM 738 CB SER A 95 11.336 -17.217 16.795 1.00 13.20 C ANISOU 738 CB SER A 95 1623 1802 1591 -81 18 -6 C ATOM 739 OG SER A 95 12.754 -17.045 16.842 1.00 14.98 O ANISOU 739 OG SER A 95 1610 2063 2020 74 254 12 O ATOM 740 N ASP A 96 8.405 -17.548 18.671 1.00 10.48 N ANISOU 740 N ASP A 96 1412 1345 1225 -97 78 47 N ATOM 741 CA ASP A 96 7.008 -17.146 18.876 1.00 11.01 C ANISOU 741 CA ASP A 96 1395 1351 1438 -111 44 48 C ATOM 742 C ASP A 96 6.945 -15.914 19.794 1.00 11.43 C ANISOU 742 C ASP A 96 1468 1422 1453 -110 -71 28 C ATOM 743 O ASP A 96 6.189 -14.978 19.545 1.00 12.21 O ANISOU 743 O ASP A 96 1650 1387 1602 37 -45 -133 O ATOM 744 CB ASP A 96 6.217 -18.260 19.639 1.00 11.64 C ANISOU 744 CB ASP A 96 1338 1388 1698 -137 25 89 C ATOM 745 CG ASP A 96 5.937 -19.448 18.727 1.00 12.12 C ANISOU 745 CG ASP A 96 1323 1566 1716 -33 43 21 C ATOM 746 OD1 ASP A 96 5.768 -19.267 17.510 1.00 12.93 O ANISOU 746 OD1 ASP A 96 1441 1757 1714 -94 24 85 O ATOM 747 OD2 ASP A 96 5.929 -20.599 19.220 1.00 13.36 O ANISOU 747 OD2 ASP A 96 1692 1448 1939 -155 173 -47 O ATOM 748 N VAL A 97 7.735 -15.917 20.878 1.00 9.94 N ANISOU 748 N VAL A 97 1253 1370 1153 -224 82 135 N ATOM 749 CA VAL A 97 7.778 -14.733 21.740 1.00 10.94 C ANISOU 749 CA VAL A 97 1423 1423 1311 -138 41 60 C ATOM 750 C VAL A 97 8.561 -13.593 21.102 1.00 11.12 C ANISOU 750 C VAL A 97 1482 1359 1382 -68 -5 59 C ATOM 751 O VAL A 97 8.099 -12.452 21.035 1.00 11.03 O ANISOU 751 O VAL A 97 1613 1321 1256 -73 -119 3 O ATOM 752 CB VAL A 97 8.412 -15.167 23.095 1.00 12.24 C ANISOU 752 CB VAL A 97 1697 1588 1365 -94 -36 71 C ATOM 753 CG1 VAL A 97 8.602 -13.962 24.013 1.00 14.69 C ANISOU 753 CG1 VAL A 97 2196 1798 1586 -143 -24 -77 C ATOM 754 CG2 VAL A 97 7.555 -16.232 23.769 1.00 13.51 C ANISOU 754 CG2 VAL A 97 1804 1726 1602 -132 22 144 C ATOM 755 N LEU A 98 9.778 -13.860 20.635 1.00 11.92 N ANISOU 755 N LEU A 98 1469 1563 1499 -30 24 11 N ATOM 756 CA LEU A 98 10.659 -12.790 20.129 1.00 12.33 C ANISOU 756 CA LEU A 98 1410 1611 1666 -94 41 12 C ATOM 757 C LEU A 98 10.031 -12.052 18.948 1.00 12.24 C ANISOU 757 C LEU A 98 1314 1760 1578 -55 102 -32 C ATOM 758 O LEU A 98 10.027 -10.811 18.904 1.00 13.28 O ANISOU 758 O LEU A 98 1525 1823 1696 -161 114 -54 O ATOM 759 CB LEU A 98 11.989 -13.353 19.622 1.00 13.71 C ANISOU 759 CB LEU A 98 1624 1759 1825 7 35 -118 C ATOM 760 CG LEU A 98 12.960 -13.967 20.617 1.00 15.38 C ANISOU 760 CG LEU A 98 1948 1901 1993 13 -48 11 C ATOM 761 CD1 LEU A 98 13.997 -14.858 19.939 1.00 16.01 C ANISOU 761 CD1 LEU A 98 2030 2050 2005 -3 95 -2 C ATOM 762 CD2 LEU A 98 13.687 -12.827 21.327 1.00 17.23 C ANISOU 762 CD2 LEU A 98 2257 2174 2116 -94 -128 -172 C ATOM 763 N ASP A 99 9.495 -12.815 17.993 1.00 11.34 N ANISOU 763 N ASP A 99 1155 1695 1459 -76 149 -40 N ATOM 764 CA ASP A 99 9.006 -12.154 16.759 1.00 12.03 C ANISOU 764 CA ASP A 99 1409 1632 1529 6 72 -76 C ATOM 765 C ASP A 99 7.647 -11.484 16.991 1.00 11.14 C ANISOU 765 C ASP A 99 1358 1521 1354 -95 79 -8 C ATOM 766 O ASP A 99 7.371 -10.426 16.457 1.00 11.51 O ANISOU 766 O ASP A 99 1564 1706 1104 -85 224 132 O ATOM 767 CB ASP A 99 8.840 -13.103 15.566 1.00 12.53 C ANISOU 767 CB ASP A 99 1554 1659 1550 -95 17 -65 C ATOM 768 CG ASP A 99 10.155 -13.475 14.906 1.00 13.99 C ANISOU 768 CG ASP A 99 1742 1803 1771 -11 90 -82 C ATOM 769 OD1 ASP A 99 11.211 -12.946 15.351 1.00 16.28 O ANISOU 769 OD1 ASP A 99 1952 2106 2128 -285 71 -37 O ATOM 770 OD2 ASP A 99 10.169 -14.307 13.958 1.00 13.73 O ANISOU 770 OD2 ASP A 99 1685 1789 1743 -70 129 -89 O ATOM 771 N THR A 100 6.794 -12.114 17.819 1.00 10.26 N ANISOU 771 N THR A 100 1266 1405 1227 -59 66 66 N ATOM 772 CA THR A 100 5.525 -11.452 18.135 1.00 9.88 C ANISOU 772 CA THR A 100 1208 1336 1208 -80 50 38 C ATOM 773 C THR A 100 5.813 -10.162 18.910 1.00 10.11 C ANISOU 773 C THR A 100 1202 1292 1347 -96 11 103 C ATOM 774 O THR A 100 5.174 -9.123 18.657 1.00 9.81 O ANISOU 774 O THR A 100 1122 1161 1444 -187 89 59 O ATOM 775 CB THR A 100 4.599 -12.427 18.906 1.00 9.74 C ANISOU 775 CB THR A 100 1137 1204 1361 -65 14 0 C ATOM 776 OG1 THR A 100 4.339 -13.546 18.021 1.00 10.56 O ANISOU 776 OG1 THR A 100 1470 1278 1262 -138 -4 46 O ATOM 777 CG2 THR A 100 3.277 -11.736 19.209 1.00 9.61 C ANISOU 777 CG2 THR A 100 1155 1237 1258 -92 133 -63 C ATOM 778 N ALA A 101 6.754 -10.203 19.846 1.00 9.63 N ANISOU 778 N ALA A 101 1167 1359 1133 -235 19 -23 N ATOM 779 CA ALA A 101 7.077 -8.986 20.604 1.00 10.13 C ANISOU 779 CA ALA A 101 1392 1214 1243 -200 -63 110 C ATOM 780 C ALA A 101 7.716 -7.945 19.681 1.00 10.39 C ANISOU 780 C ALA A 101 1368 1236 1342 -133 -35 153 C ATOM 781 O ALA A 101 7.432 -6.758 19.848 1.00 10.01 O ANISOU 781 O ALA A 101 1315 1220 1269 -126 -40 203 O ATOM 782 CB ALA A 101 8.082 -9.357 21.722 1.00 10.15 C ANISOU 782 CB ALA A 101 1360 1133 1362 -71 -90 66 C ATOM 783 N ASN A 102 8.544 -8.353 18.714 1.00 10.57 N ANISOU 783 N ASN A 102 1435 1394 1188 -214 -81 111 N ATOM 784 CA ASN A 102 9.028 -7.294 17.794 1.00 12.06 C ANISOU 784 CA ASN A 102 1612 1504 1467 -157 -81 235 C ATOM 785 C ASN A 102 7.906 -6.739 16.918 1.00 11.34 C ANISOU 785 C ASN A 102 1495 1365 1448 -124 -19 158 C ATOM 786 O ASN A 102 7.930 -5.555 16.572 1.00 11.17 O ANISOU 786 O ASN A 102 1410 1269 1565 -140 -1 60 O ATOM 787 CB ASN A 102 10.209 -7.801 16.997 1.00 15.50 C ANISOU 787 CB ASN A 102 1967 1952 1972 -36 149 218 C ATOM 788 CG ASN A 102 11.484 -7.510 17.830 1.00 18.93 C ANISOU 788 CG ASN A 102 2118 2535 2540 -53 -16 160 C ATOM 789 OD1 ASN A 102 11.672 -6.535 18.597 1.00 21.85 O ANISOU 789 OD1 ASN A 102 2609 2900 2793 -177 5 33 O ATOM 790 ND2 ASN A 102 12.339 -8.452 17.629 1.00 18.98 N ANISOU 790 ND2 ASN A 102 2187 2436 2590 -46 207 334 N ATOM 791 N SER A 103 6.903 -7.558 16.558 1.00 10.84 N ANISOU 791 N SER A 103 1384 1451 1284 -158 -27 168 N ATOM 792 CA SER A 103 5.745 -6.994 15.856 1.00 11.04 C ANISOU 792 CA SER A 103 1298 1501 1396 -101 38 90 C ATOM 793 C SER A 103 5.033 -5.979 16.728 1.00 11.29 C ANISOU 793 C SER A 103 1491 1420 1378 -183 -10 25 C ATOM 794 O SER A 103 4.732 -4.878 16.257 1.00 11.81 O ANISOU 794 O SER A 103 1572 1558 1357 0 -45 82 O ATOM 795 CB SER A 103 4.788 -8.117 15.441 1.00 13.97 C ANISOU 795 CB SER A 103 2034 1577 1696 -267 -133 -89 C ATOM 796 OG SER A 103 5.549 -8.824 14.426 1.00 18.62 O ANISOU 796 OG SER A 103 2122 2480 2473 19 162 -90 O ATOM 797 N LEU A 104 4.778 -6.314 18.007 1.00 10.89 N ANISOU 797 N LEU A 104 1442 1468 1228 -67 -4 28 N ATOM 798 CA LEU A 104 4.251 -5.289 18.923 1.00 11.01 C ANISOU 798 CA LEU A 104 1483 1300 1401 -122 -27 19 C ATOM 799 C LEU A 104 5.061 -3.984 18.907 1.00 10.88 C ANISOU 799 C LEU A 104 1369 1346 1419 -113 20 118 C ATOM 800 O LEU A 104 4.494 -2.884 18.858 1.00 10.15 O ANISOU 800 O LEU A 104 1326 1169 1360 -262 10 -157 O ATOM 801 CB LEU A 104 4.215 -5.834 20.370 1.00 12.31 C ANISOU 801 CB LEU A 104 1626 1594 1458 -156 84 162 C ATOM 802 CG LEU A 104 3.176 -6.969 20.616 1.00 13.44 C ANISOU 802 CG LEU A 104 1607 1742 1757 -162 -27 208 C ATOM 803 CD1 LEU A 104 3.355 -7.500 22.055 1.00 13.52 C ANISOU 803 CD1 LEU A 104 1739 1733 1665 -111 149 194 C ATOM 804 CD2 LEU A 104 1.746 -6.474 20.398 1.00 15.22 C ANISOU 804 CD2 LEU A 104 1726 1993 2063 -41 3 191 C ATOM 805 N ALA A 105 6.370 -4.148 19.004 1.00 10.23 N ANISOU 805 N ALA A 105 1267 1316 1303 -214 -8 148 N ATOM 806 CA ALA A 105 7.275 -2.988 19.056 1.00 10.99 C ANISOU 806 CA ALA A 105 1278 1340 1558 -188 -13 244 C ATOM 807 C ALA A 105 7.176 -2.197 17.743 1.00 10.71 C ANISOU 807 C ALA A 105 1284 1444 1340 -60 20 87 C ATOM 808 O ALA A 105 7.121 -0.957 17.811 1.00 11.06 O ANISOU 808 O ALA A 105 1382 1437 1382 -68 121 257 O ATOM 809 CB ALA A 105 8.714 -3.433 19.297 1.00 10.63 C ANISOU 809 CB ALA A 105 1361 1215 1463 -119 -90 148 C ATOM 810 N LEU A 106 7.268 -2.867 16.607 1.00 9.98 N ANISOU 810 N LEU A 106 1115 1351 1328 -184 -21 86 N ATOM 811 CA LEU A 106 7.278 -2.088 15.346 1.00 9.89 C ANISOU 811 CA LEU A 106 1213 1388 1158 -4 14 -40 C ATOM 812 C LEU A 106 5.921 -1.461 15.059 1.00 10.37 C ANISOU 812 C LEU A 106 1232 1357 1352 -46 51 16 C ATOM 813 O LEU A 106 5.861 -0.393 14.437 1.00 10.30 O ANISOU 813 O LEU A 106 1201 1394 1320 65 33 143 O ATOM 814 CB LEU A 106 7.748 -3.008 14.212 1.00 10.17 C ANISOU 814 CB LEU A 106 1284 1277 1302 -31 134 -75 C ATOM 815 CG LEU A 106 9.222 -3.470 14.340 1.00 10.81 C ANISOU 815 CG LEU A 106 1289 1390 1429 -54 102 -177 C ATOM 816 CD1 LEU A 106 9.518 -4.382 13.127 1.00 12.19 C ANISOU 816 CD1 LEU A 106 1467 1526 1640 -7 164 -264 C ATOM 817 CD2 LEU A 106 10.167 -2.275 14.336 1.00 12.32 C ANISOU 817 CD2 LEU A 106 1401 1611 1669 -133 131 -53 C ATOM 818 N VAL A 107 4.849 -2.135 15.483 1.00 9.98 N ANISOU 818 N VAL A 107 1153 1321 1317 -122 -68 36 N ATOM 819 CA VAL A 107 3.514 -1.497 15.397 1.00 10.40 C ANISOU 819 CA VAL A 107 1132 1268 1553 -122 116 -12 C ATOM 820 C VAL A 107 3.470 -0.261 16.284 1.00 10.23 C ANISOU 820 C VAL A 107 1189 1263 1435 -79 114 36 C ATOM 821 O VAL A 107 3.018 0.802 15.836 1.00 10.37 O ANISOU 821 O VAL A 107 1099 1237 1603 -93 196 29 O ATOM 822 CB VAL A 107 2.402 -2.516 15.764 1.00 9.90 C ANISOU 822 CB VAL A 107 1074 1230 1457 -89 121 -127 C ATOM 823 CG1 VAL A 107 1.059 -1.791 15.878 1.00 11.34 C ANISOU 823 CG1 VAL A 107 1190 1514 1605 57 149 57 C ATOM 824 CG2 VAL A 107 2.309 -3.551 14.651 1.00 9.41 C ANISOU 824 CG2 VAL A 107 1038 1201 1338 -196 48 -51 C ATOM 825 N GLU A 108 3.896 -0.357 17.528 1.00 10.55 N ANISOU 825 N GLU A 108 1143 1485 1381 -120 83 -73 N ATOM 826 CA GLU A 108 3.835 0.818 18.435 1.00 12.66 C ANISOU 826 CA GLU A 108 1560 1449 1800 -159 166 -92 C ATOM 827 C GLU A 108 4.780 1.920 17.957 1.00 11.46 C ANISOU 827 C GLU A 108 1373 1427 1554 -35 49 52 C ATOM 828 O GLU A 108 4.383 3.087 17.992 1.00 11.95 O ANISOU 828 O GLU A 108 1468 1413 1658 -68 109 11 O ATOM 829 CB GLU A 108 4.152 0.382 19.869 1.00 17.02 C ANISOU 829 CB GLU A 108 2206 2248 2013 -61 12 125 C ATOM 830 CG GLU A 108 4.087 1.548 20.881 1.00 23.45 C ANISOU 830 CG GLU A 108 3327 2811 2769 -102 43 -257 C ATOM 831 CD GLU A 108 2.746 2.266 20.869 1.00 29.15 C ANISOU 831 CD GLU A 108 3602 3683 3790 154 118 -84 C ATOM 832 OE1 GLU A 108 1.667 1.663 20.611 1.00 30.89 O ANISOU 832 OE1 GLU A 108 3984 3856 3897 -139 127 -61 O ATOM 833 OE2 GLU A 108 2.738 3.504 21.089 1.00 32.75 O ANISOU 833 OE2 GLU A 108 4111 3735 4598 -19 144 -72 O ATOM 834 N ALA A 109 5.984 1.586 17.518 1.00 10.30 N ANISOU 834 N ALA A 109 1228 1327 1359 -186 139 134 N ATOM 835 CA ALA A 109 6.899 2.633 16.992 1.00 9.55 C ANISOU 835 CA ALA A 109 1066 1179 1385 -7 221 104 C ATOM 836 C ALA A 109 6.244 3.269 15.775 1.00 9.79 C ANISOU 836 C ALA A 109 989 1345 1387 -33 38 13 C ATOM 837 O ALA A 109 6.349 4.489 15.546 1.00 9.94 O ANISOU 837 O ALA A 109 935 1421 1420 -101 -42 6 O ATOM 838 CB ALA A 109 8.239 2.006 16.588 1.00 9.78 C ANISOU 838 CB ALA A 109 1098 1228 1389 3 190 36 C ATOM 839 N GLY A 110 5.633 2.442 14.906 1.00 9.69 N ANISOU 839 N GLY A 110 1147 1322 1212 14 99 52 N ATOM 840 CA GLY A 110 4.947 2.960 13.714 1.00 10.31 C ANISOU 840 CA GLY A 110 1286 1290 1341 -22 9 60 C ATOM 841 C GLY A 110 3.877 3.981 14.072 1.00 10.84 C ANISOU 841 C GLY A 110 1308 1328 1483 -45 9 34 C ATOM 842 O GLY A 110 3.747 5.029 13.408 1.00 11.18 O ANISOU 842 O GLY A 110 1349 1341 1560 -14 -74 49 O ATOM 843 N LYS A 111 3.033 3.666 15.062 1.00 11.40 N ANISOU 843 N LYS A 111 1410 1446 1477 -143 75 -70 N ATOM 844 CA LYS A 111 1.989 4.584 15.486 1.00 12.39 C ANISOU 844 CA LYS A 111 1518 1501 1688 -58 55 28 C ATOM 845 C LYS A 111 2.565 5.865 16.073 1.00 11.81 C ANISOU 845 C LYS A 111 1495 1431 1563 -42 92 98 C ATOM 846 O LYS A 111 1.995 6.948 15.839 1.00 12.71 O ANISOU 846 O LYS A 111 1541 1455 1832 33 174 31 O ATOM 847 CB LYS A 111 1.109 3.872 16.550 1.00 14.66 C ANISOU 847 CB LYS A 111 1779 1804 1988 -122 210 172 C ATOM 848 CG LYS A 111 0.250 2.758 15.896 1.00 17.92 C ANISOU 848 CG LYS A 111 2201 2185 2423 -209 -27 5 C ATOM 849 CD LYS A 111 -0.537 2.089 17.036 1.00 20.58 C ANISOU 849 CD LYS A 111 2560 2568 2689 -210 145 167 C ATOM 850 CE LYS A 111 -1.394 0.914 16.540 1.00 23.41 C ANISOU 850 CE LYS A 111 2974 2726 3194 -210 28 -35 C ATOM 851 NZ LYS A 111 -2.036 0.315 17.792 1.00 25.84 N ANISOU 851 NZ LYS A 111 3315 3065 3436 -196 198 99 N ATOM 852 N ILE A 112 3.675 5.788 16.806 1.00 11.86 N ANISOU 852 N ILE A 112 1534 1446 1527 -56 57 86 N ATOM 853 CA ILE A 112 4.338 7.002 17.308 1.00 12.26 C ANISOU 853 CA ILE A 112 1636 1504 1521 -50 27 42 C ATOM 854 C ILE A 112 4.833 7.853 16.143 1.00 11.93 C ANISOU 854 C ILE A 112 1605 1410 1519 18 129 -1 C ATOM 855 O ILE A 112 4.643 9.080 16.068 1.00 11.90 O ANISOU 855 O ILE A 112 1720 1489 1311 57 52 101 O ATOM 856 CB ILE A 112 5.495 6.638 18.272 1.00 12.47 C ANISOU 856 CB ILE A 112 1621 1481 1635 -48 -26 19 C ATOM 857 CG1 ILE A 112 4.903 6.082 19.570 1.00 13.33 C ANISOU 857 CG1 ILE A 112 1766 1602 1697 -24 -25 119 C ATOM 858 CG2 ILE A 112 6.357 7.889 18.550 1.00 12.39 C ANISOU 858 CG2 ILE A 112 1602 1448 1658 -18 -59 -3 C ATOM 859 CD1 ILE A 112 5.881 5.358 20.494 1.00 14.14 C ANISOU 859 CD1 ILE A 112 1789 1820 1762 -4 -50 129 C ATOM 860 N LEU A 113 5.492 7.164 15.200 1.00 10.83 N ANISOU 860 N LEU A 113 1348 1452 1316 -86 75 -5 N ATOM 861 CA LEU A 113 5.964 7.846 13.993 1.00 10.70 C ANISOU 861 CA LEU A 113 1400 1174 1492 50 56 30 C ATOM 862 C LEU A 113 4.820 8.485 13.218 1.00 11.15 C ANISOU 862 C LEU A 113 1248 1359 1629 -25 14 -28 C ATOM 863 O LEU A 113 4.925 9.605 12.698 1.00 12.04 O ANISOU 863 O LEU A 113 1404 1443 1728 61 72 66 O ATOM 864 CB LEU A 113 6.688 6.785 13.176 1.00 10.95 C ANISOU 864 CB LEU A 113 1331 1309 1520 -99 260 -25 C ATOM 865 CG LEU A 113 8.160 6.515 13.141 1.00 12.13 C ANISOU 865 CG LEU A 113 1423 1261 1926 7 -79 -135 C ATOM 866 CD1 LEU A 113 9.175 7.465 13.722 1.00 11.89 C ANISOU 866 CD1 LEU A 113 1443 1545 1528 25 -158 -210 C ATOM 867 CD2 LEU A 113 8.577 5.095 12.900 1.00 10.60 C ANISOU 867 CD2 LEU A 113 1251 1062 1716 -69 -66 240 C ATOM 868 N LEU A 114 3.715 7.759 13.065 1.00 10.85 N ANISOU 868 N LEU A 114 1281 1249 1594 -50 2 7 N ATOM 869 CA LEU A 114 2.590 8.199 12.235 1.00 10.89 C ANISOU 869 CA LEU A 114 1137 1326 1675 -146 4 -57 C ATOM 870 C LEU A 114 1.986 9.425 12.881 1.00 11.66 C ANISOU 870 C LEU A 114 1404 1386 1639 -42 3 -12 C ATOM 871 O LEU A 114 1.686 10.402 12.188 1.00 12.73 O ANISOU 871 O LEU A 114 1510 1509 1819 -71 45 129 O ATOM 872 CB LEU A 114 1.563 7.038 12.151 1.00 10.88 C ANISOU 872 CB LEU A 114 1234 1304 1595 -231 -6 21 C ATOM 873 CG LEU A 114 0.271 7.393 11.362 1.00 12.30 C ANISOU 873 CG LEU A 114 1375 1688 1610 -229 -24 88 C ATOM 874 CD1 LEU A 114 0.574 7.721 9.900 1.00 12.63 C ANISOU 874 CD1 LEU A 114 1370 1843 1586 -112 -145 85 C ATOM 875 CD2 LEU A 114 -0.690 6.185 11.437 1.00 13.46 C ANISOU 875 CD2 LEU A 114 1523 1734 1857 -284 -46 -20 C ATOM 876 N GLU A 115 1.800 9.424 14.201 1.00 11.80 N ANISOU 876 N GLU A 115 1526 1353 1606 -30 48 68 N ATOM 877 CA GLU A 115 1.242 10.653 14.816 1.00 13.20 C ANISOU 877 CA GLU A 115 1707 1547 1763 7 105 -39 C ATOM 878 C GLU A 115 2.186 11.834 14.648 1.00 13.33 C ANISOU 878 C GLU A 115 1669 1626 1770 -2 55 61 C ATOM 879 O GLU A 115 1.709 12.941 14.389 1.00 13.63 O ANISOU 879 O GLU A 115 1703 1615 1860 -4 142 54 O ATOM 880 CB GLU A 115 1.014 10.407 16.315 1.00 16.31 C ANISOU 880 CB GLU A 115 2149 2196 1852 25 83 107 C ATOM 881 N SER A 116 3.497 11.665 14.820 1.00 13.01 N ANISOU 881 N SER A 116 1625 1647 1672 -53 -27 -39 N ATOM 882 CA SER A 116 4.410 12.783 14.592 1.00 13.63 C ANISOU 882 CA SER A 116 1738 1714 1725 -98 -25 149 C ATOM 883 C SER A 116 4.386 13.223 13.126 1.00 12.20 C ANISOU 883 C SER A 116 1484 1528 1622 -62 29 -114 C ATOM 884 O SER A 116 4.555 14.435 12.862 1.00 11.26 O ANISOU 884 O SER A 116 1491 1443 1346 74 110 -17 O ATOM 885 CB SER A 116 5.823 12.488 15.060 1.00 16.92 C ANISOU 885 CB SER A 116 1868 2137 2423 -31 -114 55 C ATOM 886 OG SER A 116 6.465 11.505 14.262 1.00 21.45 O ANISOU 886 OG SER A 116 2814 2583 2752 48 76 -58 O ATOM 887 N LEU A 117 4.237 12.278 12.177 1.00 10.24 N ANISOU 887 N LEU A 117 1015 1419 1458 -4 39 -98 N ATOM 888 CA LEU A 117 4.263 12.695 10.781 1.00 11.17 C ANISOU 888 CA LEU A 117 1273 1431 1540 33 51 -49 C ATOM 889 C LEU A 117 2.982 13.444 10.429 1.00 11.11 C ANISOU 889 C LEU A 117 1276 1362 1583 28 73 17 C ATOM 890 O LEU A 117 3.018 14.416 9.659 1.00 10.97 O ANISOU 890 O LEU A 117 1228 1414 1528 -2 164 -1 O ATOM 891 CB LEU A 117 4.424 11.400 9.933 1.00 13.14 C ANISOU 891 CB LEU A 117 1745 1463 1783 -131 120 -168 C ATOM 892 CG LEU A 117 4.622 11.614 8.437 1.00 16.30 C ANISOU 892 CG LEU A 117 2202 2032 1957 -152 138 -111 C ATOM 893 CD1 LEU A 117 5.922 12.421 8.192 1.00 16.20 C ANISOU 893 CD1 LEU A 117 2226 2065 1863 -182 230 3 C ATOM 894 CD2 LEU A 117 4.692 10.241 7.761 1.00 17.06 C ANISOU 894 CD2 LEU A 117 2277 2122 2082 -113 97 -223 C ATOM 895 N LYS A 118 1.834 12.983 10.977 1.00 10.27 N ANISOU 895 N LYS A 118 1129 1341 1433 168 126 8 N ATOM 896 CA LYS A 118 0.621 13.797 10.739 1.00 11.57 C ANISOU 896 CA LYS A 118 1225 1536 1635 94 37 62 C ATOM 897 C LYS A 118 0.771 15.209 11.297 1.00 11.83 C ANISOU 897 C LYS A 118 1329 1544 1621 28 66 29 C ATOM 898 O LYS A 118 0.295 16.175 10.671 1.00 12.34 O ANISOU 898 O LYS A 118 1621 1546 1522 -51 40 85 O ATOM 899 CB LYS A 118 -0.587 13.106 11.395 1.00 12.18 C ANISOU 899 CB LYS A 118 1327 1588 1714 -23 44 100 C ATOM 900 CG LYS A 118 -0.992 11.839 10.659 1.00 14.10 C ANISOU 900 CG LYS A 118 1682 1682 1994 -55 -73 -8 C ATOM 901 CD LYS A 118 -2.177 11.207 11.422 1.00 16.95 C ANISOU 901 CD LYS A 118 2045 2115 2282 -115 186 55 C ATOM 902 CE LYS A 118 -2.589 9.936 10.659 1.00 20.28 C ANISOU 902 CE LYS A 118 2538 2449 2720 -204 93 -159 C ATOM 903 NZ LYS A 118 -3.598 9.161 11.443 1.00 22.19 N ANISOU 903 NZ LYS A 118 2600 2692 3141 -285 200 -166 N ATOM 904 N GLU A 119 1.387 15.376 12.465 1.00 12.01 N ANISOU 904 N GLU A 119 1368 1676 1521 88 130 63 N ATOM 905 CA GLU A 119 1.648 16.704 13.005 1.00 13.58 C ANISOU 905 CA GLU A 119 1592 1738 1830 -14 149 -9 C ATOM 906 C GLU A 119 2.563 17.521 12.113 1.00 11.85 C ANISOU 906 C GLU A 119 1496 1574 1434 175 35 17 C ATOM 907 O GLU A 119 2.380 18.742 11.975 1.00 11.93 O ANISOU 907 O GLU A 119 1476 1492 1563 115 283 -98 O ATOM 908 CB GLU A 119 2.282 16.664 14.422 1.00 18.27 C ANISOU 908 CB GLU A 119 2264 2555 2121 203 -130 52 C ATOM 909 CG GLU A 119 1.238 16.093 15.399 1.00 25.13 C ANISOU 909 CG GLU A 119 3104 3271 3174 -128 316 181 C ATOM 910 CD GLU A 119 1.767 16.012 16.824 1.00 31.09 C ANISOU 910 CD GLU A 119 4090 4208 3513 -74 -69 30 C ATOM 911 OE1 GLU A 119 2.764 16.705 17.138 1.00 33.45 O ANISOU 911 OE1 GLU A 119 4125 4549 4036 -189 -6 -32 O ATOM 912 OE2 GLU A 119 1.174 15.253 17.637 1.00 33.80 O ANISOU 912 OE2 GLU A 119 4492 4382 3970 -137 119 172 O ATOM 913 N PHE A 120 3.590 16.890 11.566 1.00 11.06 N ANISOU 913 N PHE A 120 1354 1445 1403 68 88 -14 N ATOM 914 CA PHE A 120 4.453 17.546 10.599 1.00 10.74 C ANISOU 914 CA PHE A 120 1287 1370 1423 167 101 58 C ATOM 915 C PHE A 120 3.638 18.013 9.372 1.00 10.97 C ANISOU 915 C PHE A 120 1382 1356 1430 85 0 -6 C ATOM 916 O PHE A 120 3.804 19.148 8.923 1.00 10.82 O ANISOU 916 O PHE A 120 1383 1287 1441 33 112 43 O ATOM 917 CB PHE A 120 5.601 16.619 10.152 1.00 10.06 C ANISOU 917 CB PHE A 120 1212 1225 1384 110 83 -18 C ATOM 918 CG PHE A 120 6.705 17.259 9.331 1.00 11.00 C ANISOU 918 CG PHE A 120 1387 1436 1356 42 80 17 C ATOM 919 CD1 PHE A 120 7.041 18.597 9.424 1.00 11.39 C ANISOU 919 CD1 PHE A 120 1377 1555 1394 -128 -38 14 C ATOM 920 CD2 PHE A 120 7.405 16.466 8.427 1.00 11.44 C ANISOU 920 CD2 PHE A 120 1324 1539 1485 94 96 29 C ATOM 921 CE1 PHE A 120 8.041 19.153 8.653 1.00 11.14 C ANISOU 921 CE1 PHE A 120 1340 1687 1203 -14 -43 -4 C ATOM 922 CE2 PHE A 120 8.440 16.999 7.658 1.00 12.15 C ANISOU 922 CE2 PHE A 120 1415 1574 1627 49 97 121 C ATOM 923 CZ PHE A 120 8.767 18.346 7.780 1.00 11.81 C ANISOU 923 CZ PHE A 120 1450 1587 1448 54 -81 -58 C ATOM 924 N CYS A 121 2.755 17.169 8.814 1.00 9.92 N ANISOU 924 N CYS A 121 1116 1225 1429 154 119 -48 N ATOM 925 CA CYS A 121 1.883 17.591 7.728 1.00 11.14 C ANISOU 925 CA CYS A 121 1379 1406 1446 87 -19 -111 C ATOM 926 C CYS A 121 1.065 18.819 8.103 1.00 11.72 C ANISOU 926 C CYS A 121 1497 1398 1557 104 41 -29 C ATOM 927 O CYS A 121 0.869 19.749 7.298 1.00 10.87 O ANISOU 927 O CYS A 121 1324 1456 1351 173 100 -130 O ATOM 928 CB CYS A 121 0.922 16.403 7.390 1.00 11.71 C ANISOU 928 CB CYS A 121 1412 1460 1576 25 26 -122 C ATOM 929 SG CYS A 121 1.758 15.091 6.470 1.00 12.60 S ANISOU 929 SG CYS A 121 1677 1536 1575 153 -56 -126 S ATOM 930 N ASP A 122 0.521 18.823 9.342 1.00 12.16 N ANISOU 930 N ASP A 122 1554 1515 1550 34 57 -33 N ATOM 931 CA ASP A 122 -0.293 19.968 9.766 1.00 13.67 C ANISOU 931 CA ASP A 122 1733 1523 1937 68 44 -53 C ATOM 932 C ASP A 122 0.541 21.257 9.721 1.00 12.94 C ANISOU 932 C ASP A 122 1576 1642 1698 32 58 15 C ATOM 933 O ASP A 122 0.070 22.306 9.272 1.00 13.54 O ANISOU 933 O ASP A 122 1563 1668 1914 175 52 -7 O ATOM 934 CB ASP A 122 -0.858 19.757 11.169 1.00 16.34 C ANISOU 934 CB ASP A 122 2063 2075 2073 87 116 -4 C ATOM 935 CG ASP A 122 -1.926 18.676 11.260 1.00 19.88 C ANISOU 935 CG ASP A 122 2456 2448 2651 -123 85 21 C ATOM 936 OD1 ASP A 122 -2.563 18.287 10.257 1.00 20.24 O ANISOU 936 OD1 ASP A 122 2343 2586 2761 -161 35 -25 O ATOM 937 OD2 ASP A 122 -2.113 18.175 12.397 1.00 21.77 O ANISOU 937 OD2 ASP A 122 2758 2759 2755 -24 281 94 O ATOM 938 N VAL A 123 1.771 21.181 10.207 1.00 11.34 N ANISOU 938 N VAL A 123 1481 1391 1437 55 107 -29 N ATOM 939 CA VAL A 123 2.680 22.331 10.190 1.00 11.94 C ANISOU 939 CA VAL A 123 1539 1484 1515 1 61 52 C ATOM 940 C VAL A 123 2.992 22.764 8.767 1.00 11.29 C ANISOU 940 C VAL A 123 1411 1438 1442 72 22 -21 C ATOM 941 O VAL A 123 2.997 23.967 8.447 1.00 12.34 O ANISOU 941 O VAL A 123 1707 1528 1455 -9 138 36 O ATOM 942 CB VAL A 123 3.959 22.007 10.969 1.00 12.41 C ANISOU 942 CB VAL A 123 1633 1592 1490 -31 -13 40 C ATOM 943 CG1 VAL A 123 5.073 23.007 10.674 1.00 13.55 C ANISOU 943 CG1 VAL A 123 1709 1739 1699 -70 -10 152 C ATOM 944 CG2 VAL A 123 3.651 21.997 12.484 1.00 13.52 C ANISOU 944 CG2 VAL A 123 1906 1661 1569 73 68 62 C ATOM 945 N LEU A 124 3.280 21.790 7.901 1.00 10.91 N ANISOU 945 N LEU A 124 1403 1421 1321 41 -55 -13 N ATOM 946 CA LEU A 124 3.554 22.116 6.497 1.00 10.70 C ANISOU 946 CA LEU A 124 1402 1311 1354 165 -18 -19 C ATOM 947 C LEU A 124 2.353 22.766 5.810 1.00 11.12 C ANISOU 947 C LEU A 124 1353 1403 1469 63 -77 65 C ATOM 948 O LEU A 124 2.585 23.728 5.056 1.00 10.94 O ANISOU 948 O LEU A 124 1356 1470 1330 244 -65 105 O ATOM 949 CB LEU A 124 3.973 20.843 5.756 1.00 9.48 C ANISOU 949 CB LEU A 124 1249 1205 1150 150 -87 -15 C ATOM 950 CG LEU A 124 5.370 20.312 6.163 1.00 8.50 C ANISOU 950 CG LEU A 124 1146 902 1182 94 -53 -47 C ATOM 951 CD1 LEU A 124 5.547 18.853 5.747 1.00 9.26 C ANISOU 951 CD1 LEU A 124 1409 817 1294 116 -112 -43 C ATOM 952 CD2 LEU A 124 6.465 21.110 5.464 1.00 9.92 C ANISOU 952 CD2 LEU A 124 1232 1104 1433 -25 -83 81 C ATOM 953 N TRP A 125 1.133 22.270 6.087 1.00 11.39 N ANISOU 953 N TRP A 125 1308 1571 1450 139 1 -30 N ATOM 954 CA TRP A 125 -0.035 22.915 5.477 1.00 11.65 C ANISOU 954 CA TRP A 125 1271 1487 1669 127 24 12 C ATOM 955 C TRP A 125 -0.164 24.358 5.960 1.00 11.88 C ANISOU 955 C TRP A 125 1404 1494 1614 38 70 -25 C ATOM 956 O TRP A 125 -0.458 25.266 5.139 1.00 11.88 O ANISOU 956 O TRP A 125 1377 1517 1619 204 232 -10 O ATOM 957 CB TRP A 125 -1.282 22.142 5.876 1.00 12.37 C ANISOU 957 CB TRP A 125 1469 1466 1764 -31 40 -3 C ATOM 958 CG TRP A 125 -2.575 22.677 5.316 1.00 14.03 C ANISOU 958 CG TRP A 125 1631 1774 1927 35 -39 93 C ATOM 959 CD1 TRP A 125 -3.583 23.258 6.043 1.00 15.61 C ANISOU 959 CD1 TRP A 125 1879 2051 2001 151 7 49 C ATOM 960 CD2 TRP A 125 -3.004 22.696 3.955 1.00 14.46 C ANISOU 960 CD2 TRP A 125 1748 1874 1872 55 -29 16 C ATOM 961 NE1 TRP A 125 -4.624 23.630 5.202 1.00 15.38 N ANISOU 961 NE1 TRP A 125 1713 2189 1942 139 -8 -33 N ATOM 962 CE2 TRP A 125 -4.278 23.283 3.908 1.00 15.06 C ANISOU 962 CE2 TRP A 125 1787 2014 1919 53 16 -21 C ATOM 963 CE3 TRP A 125 -2.408 22.278 2.756 1.00 14.39 C ANISOU 963 CE3 TRP A 125 1781 1792 1896 39 -68 -27 C ATOM 964 CZ2 TRP A 125 -4.970 23.466 2.710 1.00 14.91 C ANISOU 964 CZ2 TRP A 125 1775 1944 1944 39 -30 -86 C ATOM 965 CZ3 TRP A 125 -3.089 22.447 1.566 1.00 14.77 C ANISOU 965 CZ3 TRP A 125 1805 1922 1886 14 -78 -76 C ATOM 966 CH2 TRP A 125 -4.368 23.061 1.532 1.00 14.53 C ANISOU 966 CH2 TRP A 125 1714 1892 1913 -18 -30 -82 C ATOM 967 N GLU A 126 0.001 24.583 7.269 1.00 12.88 N ANISOU 967 N GLU A 126 1441 1805 1646 41 85 -14 N ATOM 968 CA GLU A 126 -0.069 25.948 7.827 1.00 15.26 C ANISOU 968 CA GLU A 126 1879 1760 2158 -34 115 -27 C ATOM 969 C GLU A 126 0.954 26.865 7.151 1.00 13.42 C ANISOU 969 C GLU A 126 1589 1700 1810 154 12 -22 C ATOM 970 O GLU A 126 0.624 27.988 6.783 1.00 13.23 O ANISOU 970 O GLU A 126 1657 1676 1694 204 51 5 O ATOM 971 CB GLU A 126 0.168 25.927 9.345 1.00 20.89 C ANISOU 971 CB GLU A 126 2691 2866 2382 43 -86 120 C ATOM 972 CG GLU A 126 -0.065 27.212 10.105 1.00 28.84 C ANISOU 972 CG GLU A 126 3926 3289 3744 34 46 -261 C ATOM 973 CD GLU A 126 0.348 27.169 11.571 1.00 35.50 C ANISOU 973 CD GLU A 126 4844 4619 4025 -3 -79 -61 C ATOM 974 OE1 GLU A 126 0.330 28.222 12.273 1.00 38.42 O ANISOU 974 OE1 GLU A 126 5235 4752 4609 15 -5 -267 O ATOM 975 OE2 GLU A 126 0.736 26.077 12.076 1.00 38.27 O ANISOU 975 OE2 GLU A 126 5182 4766 4592 104 -21 45 O ATOM 976 N VAL A 127 2.203 26.407 7.011 1.00 11.37 N ANISOU 976 N VAL A 127 1394 1491 1435 86 75 -63 N ATOM 977 CA VAL A 127 3.254 27.265 6.468 1.00 10.35 C ANISOU 977 CA VAL A 127 1223 1278 1432 156 8 -76 C ATOM 978 C VAL A 127 3.026 27.451 4.985 1.00 10.42 C ANISOU 978 C VAL A 127 1139 1322 1500 164 0 -39 C ATOM 979 O VAL A 127 3.144 28.579 4.485 1.00 11.44 O ANISOU 979 O VAL A 127 1406 1309 1632 103 14 -33 O ATOM 980 CB VAL A 127 4.652 26.676 6.772 1.00 10.20 C ANISOU 980 CB VAL A 127 1164 1362 1349 56 -8 -12 C ATOM 981 CG1 VAL A 127 5.779 27.376 5.976 1.00 11.97 C ANISOU 981 CG1 VAL A 127 1352 1620 1577 -27 123 -41 C ATOM 982 CG2 VAL A 127 4.940 26.765 8.275 1.00 11.62 C ANISOU 982 CG2 VAL A 127 1455 1531 1429 134 -41 -77 C ATOM 983 N ALA A 128 2.613 26.408 4.254 1.00 10.30 N ANISOU 983 N ALA A 128 1105 1256 1553 229 32 -94 N ATOM 984 CA ALA A 128 2.369 26.616 2.811 1.00 10.65 C ANISOU 984 CA ALA A 128 1236 1268 1542 133 -3 -38 C ATOM 985 C ALA A 128 1.253 27.655 2.637 1.00 11.52 C ANISOU 985 C ALA A 128 1483 1229 1667 162 24 39 C ATOM 986 O ALA A 128 1.393 28.508 1.744 1.00 11.00 O ANISOU 986 O ALA A 128 1481 1189 1508 333 84 73 O ATOM 987 CB ALA A 128 1.953 25.333 2.108 1.00 11.51 C ANISOU 987 CB ALA A 128 1413 1383 1576 43 56 -113 C ATOM 988 N ASN A 129 0.179 27.552 3.438 1.00 11.50 N ANISOU 988 N ASN A 129 1438 1305 1627 139 39 -11 N ATOM 989 CA ASN A 129 -0.867 28.595 3.253 1.00 12.77 C ANISOU 989 CA ASN A 129 1601 1404 1847 226 10 12 C ATOM 990 C ASN A 129 -0.424 29.979 3.666 1.00 12.52 C ANISOU 990 C ASN A 129 1585 1491 1680 91 83 63 C ATOM 991 O ASN A 129 -0.868 31.012 3.079 1.00 13.58 O ANISOU 991 O ASN A 129 1678 1355 2125 262 13 -67 O ATOM 992 CB ASN A 129 -2.132 28.156 4.013 1.00 13.79 C ANISOU 992 CB ASN A 129 1675 1574 1990 112 -25 99 C ATOM 993 CG ASN A 129 -2.869 27.162 3.138 1.00 15.12 C ANISOU 993 CG ASN A 129 1864 1766 2117 28 -117 80 C ATOM 994 OD1 ASN A 129 -3.714 27.510 2.313 1.00 15.54 O ANISOU 994 OD1 ASN A 129 1791 1796 2316 131 -109 182 O ATOM 995 ND2 ASN A 129 -2.553 25.886 3.291 1.00 14.62 N ANISOU 995 ND2 ASN A 129 1783 1656 2115 -26 -30 92 N ATOM 996 N ARG A 130 0.356 30.079 4.745 1.00 12.84 N ANISOU 996 N ARG A 130 1523 1485 1870 98 18 -20 N ATOM 997 CA ARG A 130 0.883 31.376 5.177 1.00 14.13 C ANISOU 997 CA ARG A 130 1801 1593 1974 -72 71 -25 C ATOM 998 C ARG A 130 1.580 32.085 4.024 1.00 13.97 C ANISOU 998 C ARG A 130 1835 1514 1960 90 131 -11 C ATOM 999 O ARG A 130 1.492 33.348 3.978 1.00 14.58 O ANISOU 999 O ARG A 130 1909 1465 2165 201 218 71 O ATOM 1000 CB ARG A 130 1.821 31.189 6.387 1.00 15.52 C ANISOU 1000 CB ARG A 130 1997 1797 2101 61 15 21 C ATOM 1001 CG ARG A 130 2.386 32.528 6.902 1.00 18.88 C ANISOU 1001 CG ARG A 130 2437 2123 2613 -218 -25 -46 C ATOM 1002 CD ARG A 130 3.132 32.327 8.201 1.00 23.24 C ANISOU 1002 CD ARG A 130 3051 2889 2889 0 -203 -8 C ATOM 1003 NE ARG A 130 2.196 31.809 9.216 1.00 26.66 N ANISOU 1003 NE ARG A 130 3350 3361 3418 -17 108 36 N ATOM 1004 CZ ARG A 130 2.475 30.793 10.026 1.00 28.40 C ANISOU 1004 CZ ARG A 130 3655 3527 3606 25 38 136 C ATOM 1005 NH1 ARG A 130 1.489 30.446 10.852 1.00 29.93 N ANISOU 1005 NH1 ARG A 130 3618 3908 3847 92 203 -24 N ATOM 1006 NH2 ARG A 130 3.637 30.138 9.975 1.00 28.20 N ANISOU 1006 NH2 ARG A 130 3587 3474 3653 10 103 83 N ATOM 1007 N TYR A 131 2.408 31.387 3.229 1.00 11.67 N ANISOU 1007 N TYR A 131 1434 1353 1646 35 -9 -17 N ATOM 1008 CA TYR A 131 3.156 32.022 2.142 1.00 11.19 C ANISOU 1008 CA TYR A 131 1268 1416 1566 84 -45 -48 C ATOM 1009 C TYR A 131 2.591 31.669 0.785 1.00 10.99 C ANISOU 1009 C TYR A 131 1339 1242 1595 112 -30 35 C ATOM 1010 O TYR A 131 3.288 31.658 -0.258 1.00 11.49 O ANISOU 1010 O TYR A 131 1507 1384 1473 134 -71 -89 O ATOM 1011 CB TYR A 131 4.654 31.537 2.234 1.00 11.70 C ANISOU 1011 CB TYR A 131 1359 1568 1519 185 -54 16 C ATOM 1012 CG TYR A 131 5.204 31.946 3.605 1.00 12.71 C ANISOU 1012 CG TYR A 131 1614 1607 1610 102 -87 -80 C ATOM 1013 CD1 TYR A 131 5.387 30.998 4.598 1.00 12.94 C ANISOU 1013 CD1 TYR A 131 1642 1695 1578 64 -108 -32 C ATOM 1014 CD2 TYR A 131 5.439 33.288 3.896 1.00 13.37 C ANISOU 1014 CD2 TYR A 131 1660 1645 1775 -28 -132 -36 C ATOM 1015 CE1 TYR A 131 5.839 31.364 5.865 1.00 12.81 C ANISOU 1015 CE1 TYR A 131 1542 1705 1620 52 -48 -84 C ATOM 1016 CE2 TYR A 131 5.889 33.664 5.160 1.00 13.09 C ANISOU 1016 CE2 TYR A 131 1620 1711 1644 57 17 -51 C ATOM 1017 CZ TYR A 131 6.083 32.693 6.122 1.00 13.76 C ANISOU 1017 CZ TYR A 131 1750 1719 1760 4 -89 -29 C ATOM 1018 OH TYR A 131 6.525 33.051 7.392 1.00 14.46 O ANISOU 1018 OH TYR A 131 2049 1668 1777 10 -101 -34 O ATOM 1019 N LYS A 132 1.273 31.437 0.722 1.00 11.63 N ANISOU 1019 N LYS A 132 1337 1362 1719 85 -57 -60 N ATOM 1020 CA LYS A 132 0.648 30.918 -0.495 1.00 13.13 C ANISOU 1020 CA LYS A 132 1488 1769 1732 88 -132 -10 C ATOM 1021 C LYS A 132 0.934 31.763 -1.736 1.00 14.27 C ANISOU 1021 C LYS A 132 1626 1921 1874 36 -51 19 C ATOM 1022 O LYS A 132 1.159 31.188 -2.821 1.00 15.74 O ANISOU 1022 O LYS A 132 1711 2382 1889 119 -69 -117 O ATOM 1023 CB LYS A 132 -0.878 30.940 -0.248 1.00 14.40 C ANISOU 1023 CB LYS A 132 1609 1924 1940 -92 32 95 C ATOM 1024 CG LYS A 132 -1.594 30.363 -1.480 1.00 16.95 C ANISOU 1024 CG LYS A 132 2071 2202 2166 -7 -58 -95 C ATOM 1025 CD LYS A 132 -3.038 30.308 -0.948 1.00 21.88 C ANISOU 1025 CD LYS A 132 2356 2911 3047 69 190 -28 C ATOM 1026 CE LYS A 132 -4.007 29.657 -1.866 1.00 25.65 C ANISOU 1026 CE LYS A 132 3217 3226 3302 35 -190 -61 C ATOM 1027 NZ LYS A 132 -5.239 29.146 -1.154 1.00 28.28 N ANISOU 1027 NZ LYS A 132 3616 3195 3935 -57 54 152 N ATOM 1028 N HIS A 133 0.934 33.081 -1.584 1.00 14.01 N ANISOU 1028 N HIS A 133 1473 1767 2083 91 -89 34 N ATOM 1029 CA HIS A 133 1.144 33.976 -2.703 1.00 16.39 C ANISOU 1029 CA HIS A 133 1870 2211 2147 -80 -33 150 C ATOM 1030 C HIS A 133 2.486 34.707 -2.624 1.00 16.25 C ANISOU 1030 C HIS A 133 1774 2093 2308 39 -98 226 C ATOM 1031 O HIS A 133 2.695 35.704 -3.318 1.00 17.07 O ANISOU 1031 O HIS A 133 1595 2238 2654 102 -116 427 O ATOM 1032 CB HIS A 133 -0.012 34.985 -2.813 1.00 19.72 C ANISOU 1032 CB HIS A 133 2331 2433 2729 208 -56 169 C ATOM 1033 CG HIS A 133 -1.353 34.319 -3.009 1.00 22.83 C ANISOU 1033 CG HIS A 133 2681 2886 3109 -100 -73 135 C ATOM 1034 ND1 HIS A 133 -1.539 33.397 -4.029 1.00 25.33 N ANISOU 1034 ND1 HIS A 133 3035 3279 3311 28 -62 -52 N ATOM 1035 CD2 HIS A 133 -2.553 34.431 -2.433 1.00 23.29 C ANISOU 1035 CD2 HIS A 133 2834 2972 3044 119 40 33 C ATOM 1036 CE1 HIS A 133 -2.795 32.953 -4.038 1.00 25.01 C ANISOU 1036 CE1 HIS A 133 3100 3025 3378 -34 62 22 C ATOM 1037 NE2 HIS A 133 -3.415 33.551 -3.058 1.00 24.89 N ANISOU 1037 NE2 HIS A 133 2771 3295 3390 -11 40 57 N ATOM 1038 N THR A 134 3.392 34.279 -1.756 1.00 13.36 N ANISOU 1038 N THR A 134 1474 1543 2060 52 59 100 N ATOM 1039 CA THR A 134 4.701 34.939 -1.618 1.00 12.30 C ANISOU 1039 CA THR A 134 1475 1414 1784 78 -40 74 C ATOM 1040 C THR A 134 5.601 34.643 -2.798 1.00 12.63 C ANISOU 1040 C THR A 134 1589 1414 1795 27 -9 34 C ATOM 1041 O THR A 134 5.980 33.467 -2.993 1.00 12.31 O ANISOU 1041 O THR A 134 1416 1252 2011 64 24 83 O ATOM 1042 CB THR A 134 5.365 34.353 -0.344 1.00 13.37 C ANISOU 1042 CB THR A 134 1652 1699 1729 11 -32 69 C ATOM 1043 OG1 THR A 134 4.465 34.648 0.740 1.00 13.17 O ANISOU 1043 OG1 THR A 134 1503 1698 1802 126 15 181 O ATOM 1044 CG2 THR A 134 6.751 34.905 -0.099 1.00 13.34 C ANISOU 1044 CG2 THR A 134 1640 1676 1753 7 -89 20 C ATOM 1045 N PRO A 135 6.010 35.652 -3.556 1.00 12.57 N ANISOU 1045 N PRO A 135 1621 1440 1715 60 1 75 N ATOM 1046 CA PRO A 135 6.789 35.412 -4.775 1.00 11.94 C ANISOU 1046 CA PRO A 135 1461 1364 1711 174 -20 65 C ATOM 1047 C PRO A 135 8.207 34.987 -4.402 1.00 11.57 C ANISOU 1047 C PRO A 135 1361 1400 1635 54 28 -83 C ATOM 1048 O PRO A 135 8.800 35.547 -3.478 1.00 11.70 O ANISOU 1048 O PRO A 135 1118 1608 1720 170 -185 56 O ATOM 1049 CB PRO A 135 6.798 36.739 -5.555 1.00 13.34 C ANISOU 1049 CB PRO A 135 1726 1465 1879 124 -5 109 C ATOM 1050 CG PRO A 135 5.772 37.578 -4.897 1.00 14.81 C ANISOU 1050 CG PRO A 135 1997 1738 1890 181 175 94 C ATOM 1051 CD PRO A 135 5.466 37.034 -3.507 1.00 13.34 C ANISOU 1051 CD PRO A 135 1738 1501 1829 91 11 91 C ATOM 1052 N THR A 136 8.747 34.040 -5.151 1.00 10.54 N ANISOU 1052 N THR A 136 1255 1065 1684 78 -103 6 N ATOM 1053 CA THR A 136 10.147 33.630 -5.022 1.00 10.95 C ANISOU 1053 CA THR A 136 1233 1381 1547 66 -28 -4 C ATOM 1054 C THR A 136 10.612 33.142 -6.394 1.00 11.19 C ANISOU 1054 C THR A 136 1235 1465 1551 32 10 39 C ATOM 1055 O THR A 136 9.805 32.895 -7.299 1.00 11.89 O ANISOU 1055 O THR A 136 1164 1916 1438 94 104 -116 O ATOM 1056 CB THR A 136 10.254 32.533 -3.939 1.00 12.23 C ANISOU 1056 CB THR A 136 1468 1405 1775 27 -109 87 C ATOM 1057 OG1 THR A 136 11.623 32.270 -3.595 1.00 14.74 O ANISOU 1057 OG1 THR A 136 1627 1807 2166 220 -150 -29 O ATOM 1058 CG2 THR A 136 9.688 31.206 -4.438 1.00 11.44 C ANISOU 1058 CG2 THR A 136 1475 1390 1481 16 -61 108 C ATOM 1059 N ILE A 137 11.912 33.000 -6.590 1.00 10.44 N ANISOU 1059 N ILE A 137 1172 1254 1540 107 10 115 N ATOM 1060 CA ILE A 137 12.429 32.581 -7.876 1.00 10.70 C ANISOU 1060 CA ILE A 137 1320 1283 1464 -7 -3 50 C ATOM 1061 C ILE A 137 12.577 31.056 -7.860 1.00 11.00 C ANISOU 1061 C ILE A 137 1378 1321 1481 44 -102 83 C ATOM 1062 O ILE A 137 13.171 30.513 -6.936 1.00 10.97 O ANISOU 1062 O ILE A 137 1631 893 1643 106 -146 204 O ATOM 1063 CB ILE A 137 13.768 33.274 -8.238 1.00 11.17 C ANISOU 1063 CB ILE A 137 1292 1443 1510 -34 -36 27 C ATOM 1064 CG1 ILE A 137 14.159 32.937 -9.689 1.00 11.62 C ANISOU 1064 CG1 ILE A 137 1302 1675 1438 -36 -55 67 C ATOM 1065 CG2 ILE A 137 14.915 32.923 -7.302 1.00 11.29 C ANISOU 1065 CG2 ILE A 137 1296 1520 1474 -36 -6 27 C ATOM 1066 CD1 ILE A 137 13.159 33.449 -10.732 1.00 12.80 C ANISOU 1066 CD1 ILE A 137 1456 1712 1697 70 -89 184 C ATOM 1067 N GLY A 138 11.969 30.374 -8.815 1.00 11.24 N ANISOU 1067 N GLY A 138 1345 1359 1566 45 -159 21 N ATOM 1068 CA GLY A 138 12.151 28.933 -9.011 1.00 11.01 C ANISOU 1068 CA GLY A 138 1272 1364 1546 34 -68 -57 C ATOM 1069 C GLY A 138 13.553 28.736 -9.592 1.00 11.89 C ANISOU 1069 C GLY A 138 1432 1384 1702 62 57 17 C ATOM 1070 O GLY A 138 14.087 29.561 -10.305 1.00 11.95 O ANISOU 1070 O GLY A 138 1678 1252 1609 154 93 54 O ATOM 1071 N ARG A 139 14.200 27.642 -9.157 1.00 11.67 N ANISOU 1071 N ARG A 139 1306 1393 1735 51 -98 1 N ATOM 1072 CA ARG A 139 15.622 27.458 -9.513 1.00 10.94 C ANISOU 1072 CA ARG A 139 1379 1288 1491 88 33 -138 C ATOM 1073 C ARG A 139 15.802 26.039 -10.059 1.00 10.83 C ANISOU 1073 C ARG A 139 1354 1245 1516 44 -3 -68 C ATOM 1074 O ARG A 139 15.359 25.087 -9.401 1.00 10.32 O ANISOU 1074 O ARG A 139 1248 1174 1497 -20 -62 -153 O ATOM 1075 CB ARG A 139 16.478 27.586 -8.272 1.00 11.79 C ANISOU 1075 CB ARG A 139 1387 1453 1639 0 -22 -181 C ATOM 1076 CG ARG A 139 16.527 29.037 -7.731 1.00 11.52 C ANISOU 1076 CG ARG A 139 1572 1284 1520 121 -89 -93 C ATOM 1077 CD ARG A 139 17.245 29.001 -6.366 1.00 12.79 C ANISOU 1077 CD ARG A 139 1798 1488 1572 -29 -137 -48 C ATOM 1078 NE ARG A 139 17.487 30.332 -5.818 1.00 12.93 N ANISOU 1078 NE ARG A 139 1708 1515 1690 25 -51 -95 N ATOM 1079 CZ ARG A 139 16.763 30.963 -4.894 1.00 12.64 C ANISOU 1079 CZ ARG A 139 1693 1384 1725 14 26 -3 C ATOM 1080 NH1 ARG A 139 15.654 30.444 -4.339 1.00 12.53 N ANISOU 1080 NH1 ARG A 139 1536 1467 1759 178 -36 135 N ATOM 1081 NH2 ARG A 139 17.200 32.149 -4.523 1.00 11.94 N ANISOU 1081 NH2 ARG A 139 1659 1377 1501 77 -140 24 N ATOM 1082 N THR A 140 16.388 25.945 -11.224 1.00 10.47 N ANISOU 1082 N THR A 140 1217 1297 1464 -40 -47 -71 N ATOM 1083 CA THR A 140 16.652 24.599 -11.790 1.00 10.89 C ANISOU 1083 CA THR A 140 1320 1332 1485 66 53 -17 C ATOM 1084 C THR A 140 18.142 24.561 -12.050 1.00 11.26 C ANISOU 1084 C THR A 140 1326 1366 1587 23 27 42 C ATOM 1085 O THR A 140 18.754 25.512 -12.575 1.00 10.95 O ANISOU 1085 O THR A 140 1315 1233 1612 140 34 139 O ATOM 1086 CB THR A 140 15.845 24.314 -13.052 1.00 12.21 C ANISOU 1086 CB THR A 140 1351 1645 1642 14 -27 12 C ATOM 1087 OG1 THR A 140 16.206 25.328 -13.998 1.00 13.62 O ANISOU 1087 OG1 THR A 140 1626 1802 1749 -116 -10 41 O ATOM 1088 CG2 THR A 140 14.336 24.337 -12.747 1.00 11.59 C ANISOU 1088 CG2 THR A 140 1315 1573 1517 109 -86 -44 C ATOM 1089 N HIS A 141 18.801 23.458 -11.688 1.00 10.76 N ANISOU 1089 N HIS A 141 1368 1291 1430 35 51 34 N ATOM 1090 CA HIS A 141 20.266 23.359 -11.797 1.00 12.03 C ANISOU 1090 CA HIS A 141 1452 1509 1610 -9 26 -53 C ATOM 1091 C HIS A 141 20.962 24.419 -10.938 1.00 12.54 C ANISOU 1091 C HIS A 141 1587 1564 1615 -37 -21 -29 C ATOM 1092 O HIS A 141 22.087 24.850 -11.246 1.00 12.83 O ANISOU 1092 O HIS A 141 1704 1504 1667 -52 85 1 O ATOM 1093 CB HIS A 141 20.750 23.493 -13.247 1.00 11.25 C ANISOU 1093 CB HIS A 141 1390 1326 1559 29 -1 66 C ATOM 1094 CG HIS A 141 19.949 22.685 -14.224 1.00 12.49 C ANISOU 1094 CG HIS A 141 1583 1580 1584 3 -52 -29 C ATOM 1095 ND1 HIS A 141 19.962 21.318 -14.292 1.00 13.05 N ANISOU 1095 ND1 HIS A 141 1656 1549 1753 67 -136 49 N ATOM 1096 CD2 HIS A 141 19.040 23.133 -15.158 1.00 13.13 C ANISOU 1096 CD2 HIS A 141 1656 1624 1709 72 -94 16 C ATOM 1097 CE1 HIS A 141 19.130 20.916 -15.246 1.00 13.91 C ANISOU 1097 CE1 HIS A 141 1777 1741 1767 48 -130 -44 C ATOM 1098 NE2 HIS A 141 18.542 21.996 -15.783 1.00 13.56 N ANISOU 1098 NE2 HIS A 141 1807 1680 1665 7 -94 -37 N ATOM 1099 N GLY A 142 20.280 24.914 -9.914 1.00 11.87 N ANISOU 1099 N GLY A 142 1562 1282 1667 37 28 9 N ATOM 1100 CA GLY A 142 20.824 25.955 -9.044 1.00 12.76 C ANISOU 1100 CA GLY A 142 1602 1513 1732 -7 -99 2 C ATOM 1101 C GLY A 142 20.782 27.317 -9.745 1.00 12.62 C ANISOU 1101 C GLY A 142 1524 1470 1800 107 -35 39 C ATOM 1102 O GLY A 142 21.369 28.289 -9.236 1.00 13.78 O ANISOU 1102 O GLY A 142 1496 1627 2111 61 -144 33 O ATOM 1103 N VAL A 143 20.113 27.452 -10.868 1.00 11.98 N ANISOU 1103 N VAL A 143 1567 1289 1697 -4 1 88 N ATOM 1104 CA VAL A 143 20.115 28.681 -11.692 1.00 11.24 C ANISOU 1104 CA VAL A 143 1418 1345 1507 104 21 113 C ATOM 1105 C VAL A 143 18.704 29.249 -11.744 1.00 11.02 C ANISOU 1105 C VAL A 143 1403 1222 1563 43 38 -1 C ATOM 1106 O VAL A 143 17.724 28.489 -11.810 1.00 11.27 O ANISOU 1106 O VAL A 143 1406 1315 1562 11 0 -22 O ATOM 1107 CB VAL A 143 20.583 28.344 -13.130 1.00 11.19 C ANISOU 1107 CB VAL A 143 1349 1380 1525 92 23 110 C ATOM 1108 CG1 VAL A 143 20.443 29.526 -14.083 1.00 11.72 C ANISOU 1108 CG1 VAL A 143 1429 1605 1420 209 41 157 C ATOM 1109 CG2 VAL A 143 22.065 27.920 -13.067 1.00 12.57 C ANISOU 1109 CG2 VAL A 143 1346 1673 1757 55 132 169 C ATOM 1110 N HIS A 144 18.573 30.585 -11.667 1.00 11.47 N ANISOU 1110 N HIS A 144 1532 1234 1592 172 60 -18 N ATOM 1111 CA HIS A 144 17.218 31.161 -11.658 1.00 11.75 C ANISOU 1111 CA HIS A 144 1441 1233 1792 42 -57 -43 C ATOM 1112 C HIS A 144 16.461 30.828 -12.936 1.00 12.73 C ANISOU 1112 C HIS A 144 1531 1577 1730 -11 -12 -12 C ATOM 1113 O HIS A 144 17.008 30.913 -14.056 1.00 12.06 O ANISOU 1113 O HIS A 144 1203 1578 1804 -7 43 60 O ATOM 1114 CB HIS A 144 17.360 32.702 -11.585 1.00 11.55 C ANISOU 1114 CB HIS A 144 1496 1183 1709 65 30 -82 C ATOM 1115 CG HIS A 144 17.762 33.208 -10.244 1.00 11.47 C ANISOU 1115 CG HIS A 144 1381 1342 1635 42 27 0 C ATOM 1116 ND1 HIS A 144 18.250 32.513 -9.154 1.00 12.78 N ANISOU 1116 ND1 HIS A 144 1475 1697 1684 59 -55 -17 N ATOM 1117 CD2 HIS A 144 17.708 34.509 -9.856 1.00 10.07 C ANISOU 1117 CD2 HIS A 144 1080 1203 1544 53 1 28 C ATOM 1118 CE1 HIS A 144 18.473 33.352 -8.143 1.00 10.97 C ANISOU 1118 CE1 HIS A 144 1223 1381 1564 31 23 7 C ATOM 1119 NE2 HIS A 144 18.127 34.585 -8.575 1.00 12.65 N ANISOU 1119 NE2 HIS A 144 1462 1608 1738 -28 -63 46 N ATOM 1120 N ALA A 145 15.224 30.373 -12.751 1.00 12.30 N ANISOU 1120 N ALA A 145 1369 1383 1922 157 57 0 N ATOM 1121 CA ALA A 145 14.437 29.879 -13.898 1.00 13.27 C ANISOU 1121 CA ALA A 145 1618 1514 1909 55 -43 81 C ATOM 1122 C ALA A 145 13.251 30.812 -14.043 1.00 14.82 C ANISOU 1122 C ALA A 145 1638 1843 2151 169 -18 67 C ATOM 1123 O ALA A 145 13.440 31.872 -14.690 1.00 16.33 O ANISOU 1123 O ALA A 145 1732 1991 2483 254 30 208 O ATOM 1124 CB ALA A 145 14.012 28.405 -13.673 1.00 13.26 C ANISOU 1124 CB ALA A 145 1611 1422 2004 84 -102 -84 C ATOM 1125 N GLU A 146 12.121 30.561 -13.413 1.00 14.45 N ANISOU 1125 N GLU A 146 1736 1764 1990 76 -38 120 N ATOM 1126 CA GLU A 146 10.937 31.411 -13.547 1.00 14.75 C ANISOU 1126 CA GLU A 146 1755 1828 2023 181 97 -65 C ATOM 1127 C GLU A 146 10.383 31.635 -12.138 1.00 13.21 C ANISOU 1127 C GLU A 146 1663 1551 1806 121 -85 12 C ATOM 1128 O GLU A 146 10.624 30.809 -11.260 1.00 12.91 O ANISOU 1128 O GLU A 146 1487 1292 2126 225 -53 44 O ATOM 1129 CB GLU A 146 9.753 30.724 -14.303 1.00 16.86 C ANISOU 1129 CB GLU A 146 2047 2187 2171 155 -122 -104 C ATOM 1130 CG GLU A 146 10.098 30.567 -15.775 1.00 19.78 C ANISOU 1130 CG GLU A 146 2572 2598 2344 149 2 -19 C ATOM 1131 CD GLU A 146 9.046 29.927 -16.630 1.00 20.29 C ANISOU 1131 CD GLU A 146 2636 2473 2599 88 -37 -53 C ATOM 1132 OE1 GLU A 146 8.063 29.374 -16.105 1.00 20.55 O ANISOU 1132 OE1 GLU A 146 2741 2552 2517 147 73 21 O ATOM 1133 OE2 GLU A 146 9.240 30.021 -17.881 1.00 22.24 O ANISOU 1133 OE2 GLU A 146 3021 2741 2689 122 53 -8 O ATOM 1134 N PRO A 147 9.709 32.754 -11.917 1.00 12.30 N ANISOU 1134 N PRO A 147 1527 1503 1644 111 -3 37 N ATOM 1135 CA PRO A 147 9.069 33.009 -10.646 1.00 11.69 C ANISOU 1135 CA PRO A 147 1520 1303 1617 86 4 44 C ATOM 1136 C PRO A 147 8.065 31.922 -10.268 1.00 10.82 C ANISOU 1136 C PRO A 147 1385 1272 1453 110 -90 23 C ATOM 1137 O PRO A 147 7.389 31.322 -11.099 1.00 11.09 O ANISOU 1137 O PRO A 147 1470 1330 1413 37 -63 -29 O ATOM 1138 CB PRO A 147 8.399 34.384 -10.827 1.00 11.81 C ANISOU 1138 CB PRO A 147 1447 1389 1650 121 1 197 C ATOM 1139 CG PRO A 147 9.174 35.035 -11.955 1.00 11.96 C ANISOU 1139 CG PRO A 147 1576 1387 1581 13 63 52 C ATOM 1140 CD PRO A 147 9.516 33.870 -12.868 1.00 12.41 C ANISOU 1140 CD PRO A 147 1566 1515 1635 129 70 18 C ATOM 1141 N THR A 148 7.903 31.733 -8.957 1.00 10.51 N ANISOU 1141 N THR A 148 1215 1314 1463 126 -1 47 N ATOM 1142 CA THR A 148 6.840 30.854 -8.445 1.00 11.11 C ANISOU 1142 CA THR A 148 1423 1326 1471 29 4 26 C ATOM 1143 C THR A 148 6.487 31.348 -7.040 1.00 11.69 C ANISOU 1143 C THR A 148 1505 1423 1515 10 -25 5 C ATOM 1144 O THR A 148 6.848 32.512 -6.739 1.00 11.85 O ANISOU 1144 O THR A 148 1502 1425 1577 138 91 -148 O ATOM 1145 CB THR A 148 7.275 29.373 -8.490 1.00 12.01 C ANISOU 1145 CB THR A 148 1615 1377 1572 4 -64 65 C ATOM 1146 OG1 THR A 148 6.119 28.573 -8.178 1.00 12.28 O ANISOU 1146 OG1 THR A 148 1537 1441 1686 1 -39 31 O ATOM 1147 CG2 THR A 148 8.396 29.097 -7.476 1.00 13.31 C ANISOU 1147 CG2 THR A 148 1551 1707 1800 113 -76 45 C ATOM 1148 N SER A 149 5.740 30.567 -6.268 1.00 11.47 N ANISOU 1148 N SER A 149 1377 1542 1439 120 47 20 N ATOM 1149 CA SER A 149 5.446 31.019 -4.911 1.00 11.62 C ANISOU 1149 CA SER A 149 1411 1540 1465 60 -90 89 C ATOM 1150 C SER A 149 6.154 30.175 -3.871 1.00 10.94 C ANISOU 1150 C SER A 149 1273 1407 1477 70 -51 -12 C ATOM 1151 O SER A 149 6.226 28.970 -4.096 1.00 10.64 O ANISOU 1151 O SER A 149 1383 1258 1400 43 -23 102 O ATOM 1152 CB SER A 149 3.925 30.894 -4.800 1.00 13.08 C ANISOU 1152 CB SER A 149 1371 1901 1699 201 2 153 C ATOM 1153 OG SER A 149 3.483 30.215 -3.727 1.00 13.89 O ANISOU 1153 OG SER A 149 1599 1690 1989 252 -34 294 O ATOM 1154 N PHE A 150 6.569 30.807 -2.762 1.00 10.77 N ANISOU 1154 N PHE A 150 1265 1410 1417 108 -102 26 N ATOM 1155 CA PHE A 150 7.215 29.993 -1.715 1.00 10.57 C ANISOU 1155 CA PHE A 150 1241 1338 1437 82 -33 50 C ATOM 1156 C PHE A 150 6.221 29.028 -1.080 1.00 11.29 C ANISOU 1156 C PHE A 150 1370 1338 1583 37 -38 61 C ATOM 1157 O PHE A 150 6.582 27.894 -0.708 1.00 11.00 O ANISOU 1157 O PHE A 150 1331 1297 1551 124 -71 6 O ATOM 1158 CB PHE A 150 7.813 30.956 -0.687 1.00 12.51 C ANISOU 1158 CB PHE A 150 1608 1633 1510 -35 -181 -5 C ATOM 1159 CG PHE A 150 8.551 30.168 0.389 1.00 12.65 C ANISOU 1159 CG PHE A 150 1540 1658 1609 45 -144 3 C ATOM 1160 CD1 PHE A 150 9.678 29.429 0.038 1.00 12.58 C ANISOU 1160 CD1 PHE A 150 1520 1662 1599 8 -145 -23 C ATOM 1161 CD2 PHE A 150 8.086 30.160 1.687 1.00 12.92 C ANISOU 1161 CD2 PHE A 150 1644 1671 1596 -56 -136 -1 C ATOM 1162 CE1 PHE A 150 10.327 28.674 1.000 1.00 12.73 C ANISOU 1162 CE1 PHE A 150 1525 1700 1614 58 -150 -23 C ATOM 1163 CE2 PHE A 150 8.770 29.430 2.661 1.00 12.69 C ANISOU 1163 CE2 PHE A 150 1589 1506 1726 24 -105 -52 C ATOM 1164 CZ PHE A 150 9.885 28.687 2.319 1.00 12.56 C ANISOU 1164 CZ PHE A 150 1353 1731 1689 -96 -91 -36 C ATOM 1165 N GLY A 151 4.942 29.436 -0.982 1.00 11.00 N ANISOU 1165 N GLY A 151 1266 1416 1498 -21 97 108 N ATOM 1166 CA GLY A 151 3.926 28.507 -0.497 1.00 11.29 C ANISOU 1166 CA GLY A 151 1268 1347 1673 -57 0 75 C ATOM 1167 C GLY A 151 3.782 27.254 -1.353 1.00 11.49 C ANISOU 1167 C GLY A 151 1352 1450 1563 52 10 84 C ATOM 1168 O GLY A 151 3.551 26.135 -0.835 1.00 10.68 O ANISOU 1168 O GLY A 151 1152 1219 1689 -4 -1 -50 O ATOM 1169 N LEU A 152 3.902 27.364 -2.667 1.00 12.14 N ANISOU 1169 N LEU A 152 1341 1724 1548 130 -25 34 N ATOM 1170 CA LEU A 152 3.908 26.205 -3.520 1.00 12.80 C ANISOU 1170 CA LEU A 152 1510 1617 1738 -36 -69 20 C ATOM 1171 C LEU A 152 5.114 25.301 -3.259 1.00 11.93 C ANISOU 1171 C LEU A 152 1379 1576 1579 -119 -46 15 C ATOM 1172 O LEU A 152 4.989 24.071 -3.330 1.00 11.84 O ANISOU 1172 O LEU A 152 1328 1519 1654 -30 -78 49 O ATOM 1173 CB LEU A 152 4.000 26.531 -5.023 1.00 15.71 C ANISOU 1173 CB LEU A 152 2029 2123 1817 -180 -5 185 C ATOM 1174 CG LEU A 152 2.724 26.732 -5.761 1.00 17.80 C ANISOU 1174 CG LEU A 152 2227 2490 2048 -294 -116 48 C ATOM 1175 CD1 LEU A 152 2.911 26.850 -7.266 1.00 17.30 C ANISOU 1175 CD1 LEU A 152 2175 2439 1961 -313 37 13 C ATOM 1176 CD2 LEU A 152 1.720 25.605 -5.675 1.00 18.35 C ANISOU 1176 CD2 LEU A 152 2277 2592 2104 -374 17 96 C ATOM 1177 N LYS A 153 6.246 25.921 -2.962 1.00 10.81 N ANISOU 1177 N LYS A 153 1175 1565 1367 -102 26 42 N ATOM 1178 CA LYS A 153 7.405 25.076 -2.649 1.00 12.06 C ANISOU 1178 CA LYS A 153 1389 1478 1714 -83 19 87 C ATOM 1179 C LYS A 153 7.131 24.224 -1.413 1.00 11.35 C ANISOU 1179 C LYS A 153 1411 1391 1510 34 9 -35 C ATOM 1180 O LYS A 153 7.359 23.005 -1.357 1.00 10.47 O ANISOU 1180 O LYS A 153 1242 1299 1439 70 106 -261 O ATOM 1181 CB LYS A 153 8.609 25.977 -2.395 1.00 12.94 C ANISOU 1181 CB LYS A 153 1540 1481 1894 -169 -115 -47 C ATOM 1182 CG LYS A 153 9.887 25.244 -2.065 1.00 15.29 C ANISOU 1182 CG LYS A 153 1760 1866 2183 26 -32 132 C ATOM 1183 CD LYS A 153 11.071 26.199 -1.818 1.00 17.71 C ANISOU 1183 CD LYS A 153 2076 2223 2430 -157 -173 123 C ATOM 1184 CE LYS A 153 11.443 26.921 -3.114 1.00 17.82 C ANISOU 1184 CE LYS A 153 2147 2222 2401 -169 4 128 C ATOM 1185 NZ LYS A 153 12.775 27.616 -2.977 1.00 17.12 N ANISOU 1185 NZ LYS A 153 2118 2300 2087 -97 -165 116 N ATOM 1186 N VAL A 154 6.643 24.894 -0.364 1.00 9.89 N ANISOU 1186 N VAL A 154 1236 1252 1271 84 -79 -1 N ATOM 1187 CA VAL A 154 6.297 24.190 0.862 1.00 10.22 C ANISOU 1187 CA VAL A 154 1298 1202 1384 -96 42 -64 C ATOM 1188 C VAL A 154 5.143 23.213 0.656 1.00 9.34 C ANISOU 1188 C VAL A 154 1055 1223 1271 42 26 -43 C ATOM 1189 O VAL A 154 5.159 22.136 1.253 1.00 9.91 O ANISOU 1189 O VAL A 154 1315 1156 1295 -13 -35 -33 O ATOM 1190 CB VAL A 154 5.958 25.177 2.007 1.00 10.16 C ANISOU 1190 CB VAL A 154 1381 1181 1298 -51 56 -14 C ATOM 1191 CG1 VAL A 154 5.694 24.401 3.308 1.00 10.68 C ANISOU 1191 CG1 VAL A 154 1359 1306 1393 35 196 34 C ATOM 1192 CG2 VAL A 154 7.118 26.149 2.189 1.00 10.65 C ANISOU 1192 CG2 VAL A 154 1221 1270 1555 31 44 60 C ATOM 1193 N LEU A 155 4.188 23.507 -0.198 1.00 8.63 N ANISOU 1193 N LEU A 155 1038 1201 1041 53 2 -104 N ATOM 1194 CA LEU A 155 3.112 22.548 -0.481 1.00 9.51 C ANISOU 1194 CA LEU A 155 1142 1240 1233 23 -129 -31 C ATOM 1195 C LEU A 155 3.676 21.292 -1.127 1.00 8.81 C ANISOU 1195 C LEU A 155 1045 1215 1089 46 -135 41 C ATOM 1196 O LEU A 155 3.113 20.221 -0.936 1.00 9.88 O ANISOU 1196 O LEU A 155 1159 1315 1280 10 -71 36 O ATOM 1197 CB LEU A 155 2.144 23.267 -1.458 1.00 10.62 C ANISOU 1197 CB LEU A 155 1296 1518 1221 131 -92 95 C ATOM 1198 CG LEU A 155 0.899 22.450 -1.761 1.00 13.32 C ANISOU 1198 CG LEU A 155 1513 1917 1632 -92 -62 35 C ATOM 1199 CD1 LEU A 155 -0.014 22.318 -0.544 1.00 12.39 C ANISOU 1199 CD1 LEU A 155 1527 1654 1525 -6 -77 -125 C ATOM 1200 CD2 LEU A 155 -0.073 23.035 -2.734 1.00 13.36 C ANISOU 1200 CD2 LEU A 155 1697 1675 1704 -11 -116 69 C ATOM 1201 N GLY A 156 4.758 21.394 -1.910 1.00 9.12 N ANISOU 1201 N GLY A 156 1071 1206 1188 90 -45 -59 N ATOM 1202 CA GLY A 156 5.392 20.172 -2.463 1.00 9.05 C ANISOU 1202 CA GLY A 156 1075 1158 1204 178 -78 44 C ATOM 1203 C GLY A 156 5.897 19.278 -1.315 1.00 9.79 C ANISOU 1203 C GLY A 156 1248 1241 1230 73 -4 84 C ATOM 1204 O GLY A 156 5.844 18.035 -1.368 1.00 9.95 O ANISOU 1204 O GLY A 156 1240 1233 1307 -103 17 49 O ATOM 1205 N TRP A 157 6.463 19.917 -0.300 1.00 9.50 N ANISOU 1205 N TRP A 157 1002 1419 1190 140 -52 27 N ATOM 1206 CA TRP A 157 6.879 19.124 0.879 1.00 10.83 C ANISOU 1206 CA TRP A 157 1342 1477 1298 13 -73 113 C ATOM 1207 C TRP A 157 5.690 18.519 1.581 1.00 10.42 C ANISOU 1207 C TRP A 157 1329 1197 1434 102 -43 52 C ATOM 1208 O TRP A 157 5.739 17.355 1.991 1.00 10.38 O ANISOU 1208 O TRP A 157 1410 1184 1351 204 -117 149 O ATOM 1209 CB TRP A 157 7.605 20.036 1.873 1.00 11.36 C ANISOU 1209 CB TRP A 157 1380 1420 1515 24 -112 2 C ATOM 1210 CG TRP A 157 8.783 20.805 1.329 1.00 11.62 C ANISOU 1210 CG TRP A 157 1348 1560 1507 96 -103 184 C ATOM 1211 CD1 TRP A 157 9.491 20.617 0.172 1.00 12.96 C ANISOU 1211 CD1 TRP A 157 1461 1860 1603 27 -69 118 C ATOM 1212 CD2 TRP A 157 9.374 21.927 1.983 1.00 12.79 C ANISOU 1212 CD2 TRP A 157 1484 1703 1671 5 -135 88 C ATOM 1213 NE1 TRP A 157 10.497 21.566 0.093 1.00 14.07 N ANISOU 1213 NE1 TRP A 157 1646 1948 1751 -85 20 75 N ATOM 1214 CE2 TRP A 157 10.450 22.373 1.182 1.00 14.14 C ANISOU 1214 CE2 TRP A 157 1684 1886 1803 -61 -36 62 C ATOM 1215 CE3 TRP A 157 9.127 22.569 3.202 1.00 12.72 C ANISOU 1215 CE3 TRP A 157 1442 1512 1878 166 -93 -43 C ATOM 1216 CZ2 TRP A 157 11.257 23.455 1.554 1.00 14.60 C ANISOU 1216 CZ2 TRP A 157 1856 1766 1926 -39 6 76 C ATOM 1217 CZ3 TRP A 157 9.934 23.647 3.556 1.00 13.93 C ANISOU 1217 CZ3 TRP A 157 1617 1506 2170 51 -57 180 C ATOM 1218 CH2 TRP A 157 10.970 24.086 2.725 1.00 14.43 C ANISOU 1218 CH2 TRP A 157 1759 1722 2002 51 12 62 C ATOM 1219 N TYR A 158 4.627 19.315 1.801 1.00 10.16 N ANISOU 1219 N TYR A 158 1126 1269 1467 118 -28 55 N ATOM 1220 CA TYR A 158 3.372 18.771 2.315 1.00 9.95 C ANISOU 1220 CA TYR A 158 1164 1155 1463 112 -8 -7 C ATOM 1221 C TYR A 158 2.870 17.569 1.529 1.00 9.95 C ANISOU 1221 C TYR A 158 1206 1243 1330 57 25 -11 C ATOM 1222 O TYR A 158 2.531 16.520 2.097 1.00 10.41 O ANISOU 1222 O TYR A 158 1226 1276 1452 124 42 59 O ATOM 1223 CB TYR A 158 2.290 19.872 2.234 1.00 9.25 C ANISOU 1223 CB TYR A 158 993 1148 1374 56 -125 -46 C ATOM 1224 CG TYR A 158 0.925 19.358 2.684 1.00 10.32 C ANISOU 1224 CG TYR A 158 1230 1162 1528 27 42 25 C ATOM 1225 CD1 TYR A 158 0.609 19.173 4.022 1.00 11.29 C ANISOU 1225 CD1 TYR A 158 1431 1303 1556 11 95 -24 C ATOM 1226 CD2 TYR A 158 -0.040 19.107 1.707 1.00 11.10 C ANISOU 1226 CD2 TYR A 158 1311 1206 1702 56 -85 19 C ATOM 1227 CE1 TYR A 158 -0.651 18.719 4.390 1.00 12.07 C ANISOU 1227 CE1 TYR A 158 1355 1443 1790 36 57 -59 C ATOM 1228 CE2 TYR A 158 -1.310 18.674 2.062 1.00 12.01 C ANISOU 1228 CE2 TYR A 158 1361 1468 1735 12 16 76 C ATOM 1229 CZ TYR A 158 -1.584 18.491 3.405 1.00 13.29 C ANISOU 1229 CZ TYR A 158 1507 1709 1834 0 2 61 C ATOM 1230 OH TYR A 158 -2.844 18.034 3.740 1.00 15.62 O ANISOU 1230 OH TYR A 158 1433 2246 2255 26 37 295 O ATOM 1231 N SER A 159 2.831 17.700 0.206 1.00 8.82 N ANISOU 1231 N SER A 159 911 1163 1275 84 -142 7 N ATOM 1232 CA SER A 159 2.375 16.585 -0.636 1.00 9.45 C ANISOU 1232 CA SER A 159 1279 1118 1192 164 -89 -22 C ATOM 1233 C SER A 159 3.204 15.315 -0.424 1.00 9.37 C ANISOU 1233 C SER A 159 1236 1077 1248 75 -34 63 C ATOM 1234 O SER A 159 2.634 14.218 -0.336 1.00 9.19 O ANISOU 1234 O SER A 159 1343 1048 1102 86 26 24 O ATOM 1235 CB SER A 159 2.432 17.074 -2.113 1.00 10.05 C ANISOU 1235 CB SER A 159 1397 1263 1159 45 -118 -9 C ATOM 1236 OG SER A 159 1.774 16.092 -2.924 1.00 11.68 O ANISOU 1236 OG SER A 159 1765 1259 1414 -39 -127 -74 O ATOM 1237 N GLU A 160 4.517 15.463 -0.358 1.00 9.25 N ANISOU 1237 N GLU A 160 1142 1160 1213 208 -7 59 N ATOM 1238 CA GLU A 160 5.402 14.309 -0.094 1.00 10.11 C ANISOU 1238 CA GLU A 160 1204 1245 1392 192 -39 125 C ATOM 1239 C GLU A 160 5.133 13.673 1.268 1.00 10.33 C ANISOU 1239 C GLU A 160 1229 1254 1442 27 11 100 C ATOM 1240 O GLU A 160 5.011 12.430 1.350 1.00 10.24 O ANISOU 1240 O GLU A 160 1150 1256 1483 45 -19 288 O ATOM 1241 CB GLU A 160 6.864 14.769 -0.152 1.00 10.58 C ANISOU 1241 CB GLU A 160 1225 1391 1406 103 5 134 C ATOM 1242 CG GLU A 160 7.831 13.572 -0.062 1.00 12.46 C ANISOU 1242 CG GLU A 160 1514 1422 1798 240 -19 30 C ATOM 1243 CD GLU A 160 9.237 13.872 -0.549 1.00 16.80 C ANISOU 1243 CD GLU A 160 1702 2175 2506 79 37 17 C ATOM 1244 OE1 GLU A 160 9.540 15.061 -0.803 1.00 19.13 O ANISOU 1244 OE1 GLU A 160 2093 2275 2902 92 70 73 O ATOM 1245 OE2 GLU A 160 10.094 12.924 -0.724 1.00 17.02 O ANISOU 1245 OE2 GLU A 160 1992 2115 2360 168 -45 -232 O ATOM 1246 N MET A 161 5.008 14.499 2.322 1.00 10.31 N ANISOU 1246 N MET A 161 1210 1213 1494 47 39 116 N ATOM 1247 CA MET A 161 4.760 13.970 3.652 1.00 9.34 C ANISOU 1247 CA MET A 161 992 1322 1236 51 -44 -42 C ATOM 1248 C MET A 161 3.370 13.339 3.719 1.00 9.46 C ANISOU 1248 C MET A 161 1051 1252 1292 69 50 -63 C ATOM 1249 O MET A 161 3.230 12.330 4.452 1.00 10.72 O ANISOU 1249 O MET A 161 1295 1292 1488 178 74 -22 O ATOM 1250 CB MET A 161 5.016 14.979 4.796 1.00 8.16 C ANISOU 1250 CB MET A 161 536 1138 1425 180 -37 -95 C ATOM 1251 CG MET A 161 6.503 15.406 4.880 1.00 9.14 C ANISOU 1251 CG MET A 161 766 1318 1391 120 -148 -6 C ATOM 1252 SD MET A 161 7.632 13.921 5.274 1.00 5.57 S ANISOU 1252 SD MET A 161 646 1210 261 162 -53 -33 S ATOM 1253 CE MET A 161 8.747 14.209 3.938 1.00 8.37 C ANISOU 1253 CE MET A 161 1546 1365 271 52 -131 -67 C ATOM 1254 N LYS A 162 2.369 13.826 2.999 1.00 9.36 N ANISOU 1254 N LYS A 162 1135 1309 1111 24 7 -14 N ATOM 1255 CA LYS A 162 1.080 13.134 2.939 1.00 11.08 C ANISOU 1255 CA LYS A 162 1295 1342 1574 -76 -32 -33 C ATOM 1256 C LYS A 162 1.201 11.788 2.226 1.00 10.21 C ANISOU 1256 C LYS A 162 1199 1315 1364 -1 -49 42 C ATOM 1257 O LYS A 162 0.579 10.823 2.707 1.00 10.40 O ANISOU 1257 O LYS A 162 1193 1275 1482 -49 19 -67 O ATOM 1258 CB LYS A 162 0.005 13.981 2.192 1.00 14.32 C ANISOU 1258 CB LYS A 162 1665 1862 1913 125 -45 254 C ATOM 1259 CG LYS A 162 -0.291 15.225 3.034 1.00 19.16 C ANISOU 1259 CG LYS A 162 2402 2315 2564 72 15 -122 C ATOM 1260 CD LYS A 162 -1.273 14.893 4.190 1.00 23.71 C ANISOU 1260 CD LYS A 162 2934 3101 2974 -13 259 47 C ATOM 1261 CE LYS A 162 -2.686 14.829 3.581 1.00 26.79 C ANISOU 1261 CE LYS A 162 3144 3497 3539 -38 25 -23 C ATOM 1262 NZ LYS A 162 -3.666 14.543 4.672 1.00 29.32 N ANISOU 1262 NZ LYS A 162 3555 3840 3745 -22 220 31 N ATOM 1263 N ARG A 163 1.991 11.664 1.168 1.00 9.92 N ANISOU 1263 N ARG A 163 1299 1265 1205 41 -147 -14 N ATOM 1264 CA ARG A 163 2.260 10.330 0.599 1.00 9.98 C ANISOU 1264 CA ARG A 163 1337 1262 1191 123 32 34 C ATOM 1265 C ARG A 163 2.913 9.432 1.648 1.00 10.31 C ANISOU 1265 C ARG A 163 1255 1318 1344 70 34 82 C ATOM 1266 O ARG A 163 2.541 8.242 1.735 1.00 10.91 O ANISOU 1266 O ARG A 163 1292 1319 1533 1 -49 -26 O ATOM 1267 CB ARG A 163 3.185 10.409 -0.621 1.00 10.30 C ANISOU 1267 CB ARG A 163 1420 1296 1198 52 43 120 C ATOM 1268 CG ARG A 163 2.533 11.108 -1.828 1.00 11.49 C ANISOU 1268 CG ARG A 163 1429 1696 1241 140 -73 59 C ATOM 1269 CD ARG A 163 3.412 10.975 -3.084 1.00 12.18 C ANISOU 1269 CD ARG A 163 1498 1723 1405 -25 22 44 C ATOM 1270 NE ARG A 163 4.696 11.682 -3.087 1.00 11.08 N ANISOU 1270 NE ARG A 163 1414 1399 1398 73 120 49 N ATOM 1271 CZ ARG A 163 4.837 12.981 -3.365 1.00 12.21 C ANISOU 1271 CZ ARG A 163 1522 1492 1624 71 -12 110 C ATOM 1272 NH1 ARG A 163 6.043 13.544 -3.402 1.00 11.36 N ANISOU 1272 NH1 ARG A 163 1567 1501 1249 43 19 62 N ATOM 1273 NH2 ARG A 163 3.776 13.761 -3.575 1.00 11.29 N ANISOU 1273 NH2 ARG A 163 1519 1358 1411 80 -69 143 N ATOM 1274 N ASN A 164 3.817 9.998 2.443 1.00 9.93 N ANISOU 1274 N ASN A 164 1207 1333 1233 93 75 69 N ATOM 1275 CA ASN A 164 4.520 9.195 3.465 1.00 10.25 C ANISOU 1275 CA ASN A 164 1251 1347 1297 -16 -24 75 C ATOM 1276 C ASN A 164 3.584 8.792 4.597 1.00 10.24 C ANISOU 1276 C ASN A 164 1212 1202 1477 69 42 32 C ATOM 1277 O ASN A 164 3.731 7.691 5.141 1.00 10.35 O ANISOU 1277 O ASN A 164 1407 1261 1264 53 58 154 O ATOM 1278 CB ASN A 164 5.725 9.994 3.979 1.00 9.79 C ANISOU 1278 CB ASN A 164 1100 1259 1361 81 6 87 C ATOM 1279 CG ASN A 164 6.874 9.940 2.966 1.00 10.62 C ANISOU 1279 CG ASN A 164 1181 1450 1404 10 12 64 C ATOM 1280 OD1 ASN A 164 7.007 8.892 2.302 1.00 11.52 O ANISOU 1280 OD1 ASN A 164 1245 1683 1448 79 56 15 O ATOM 1281 ND2 ASN A 164 7.655 11.009 2.938 1.00 10.00 N ANISOU 1281 ND2 ASN A 164 940 1402 1456 118 99 229 N ATOM 1282 N VAL A 165 2.542 9.591 4.907 1.00 10.01 N ANISOU 1282 N VAL A 165 1073 1143 1586 69 79 -120 N ATOM 1283 CA VAL A 165 1.528 9.133 5.860 1.00 10.39 C ANISOU 1283 CA VAL A 165 1213 1168 1567 78 101 27 C ATOM 1284 C VAL A 165 0.856 7.868 5.372 1.00 10.54 C ANISOU 1284 C VAL A 165 1187 1314 1503 81 59 13 C ATOM 1285 O VAL A 165 0.709 6.890 6.133 1.00 10.90 O ANISOU 1285 O VAL A 165 1196 1281 1663 33 -60 131 O ATOM 1286 CB VAL A 165 0.449 10.224 6.125 1.00 10.73 C ANISOU 1286 CB VAL A 165 1093 1286 1697 3 199 -117 C ATOM 1287 CG1 VAL A 165 -0.779 9.655 6.860 1.00 11.54 C ANISOU 1287 CG1 VAL A 165 1225 1329 1833 -28 223 118 C ATOM 1288 CG2 VAL A 165 1.083 11.349 6.971 1.00 11.43 C ANISOU 1288 CG2 VAL A 165 1540 1198 1603 -33 115 -61 C ATOM 1289 N GLN A 166 0.432 7.857 4.116 1.00 10.61 N ANISOU 1289 N GLN A 166 1200 1385 1447 166 56 39 N ATOM 1290 CA GLN A 166 -0.193 6.636 3.582 1.00 12.99 C ANISOU 1290 CA GLN A 166 1540 1446 1949 72 33 -42 C ATOM 1291 C GLN A 166 0.780 5.453 3.562 1.00 11.64 C ANISOU 1291 C GLN A 166 1353 1437 1631 63 29 67 C ATOM 1292 O GLN A 166 0.420 4.306 3.877 1.00 11.72 O ANISOU 1292 O GLN A 166 1150 1511 1790 24 34 -48 O ATOM 1293 CB GLN A 166 -0.721 6.892 2.165 1.00 16.91 C ANISOU 1293 CB GLN A 166 2206 2139 2080 -64 -147 79 C ATOM 1294 CG GLN A 166 -1.818 7.956 2.166 1.00 22.90 C ANISOU 1294 CG GLN A 166 2781 2775 3144 287 -132 -29 C ATOM 1295 CD GLN A 166 -2.980 7.648 3.088 1.00 26.87 C ANISOU 1295 CD GLN A 166 3203 3471 3535 31 61 64 C ATOM 1296 OE1 GLN A 166 -3.252 8.408 4.027 1.00 29.63 O ANISOU 1296 OE1 GLN A 166 3697 3790 3772 84 54 -118 O ATOM 1297 NE2 GLN A 166 -3.673 6.533 2.859 1.00 28.60 N ANISOU 1297 NE2 GLN A 166 3464 3573 3831 -76 -18 17 N ATOM 1298 N ARG A 167 2.029 5.710 3.184 1.00 10.15 N ANISOU 1298 N ARG A 167 1221 1170 1464 134 -50 56 N ATOM 1299 CA ARG A 167 3.020 4.624 3.135 1.00 10.12 C ANISOU 1299 CA ARG A 167 1068 1318 1461 88 93 111 C ATOM 1300 C ARG A 167 3.284 4.067 4.531 1.00 10.04 C ANISOU 1300 C ARG A 167 1105 1283 1428 51 31 51 C ATOM 1301 O ARG A 167 3.454 2.849 4.701 1.00 9.56 O ANISOU 1301 O ARG A 167 1146 1197 1291 18 76 -10 O ATOM 1302 CB ARG A 167 4.355 5.119 2.535 1.00 9.34 C ANISOU 1302 CB ARG A 167 1105 1149 1295 27 116 82 C ATOM 1303 CG ARG A 167 4.264 5.396 1.035 1.00 9.51 C ANISOU 1303 CG ARG A 167 1073 1248 1292 43 28 50 C ATOM 1304 CD ARG A 167 5.457 6.291 0.615 1.00 10.50 C ANISOU 1304 CD ARG A 167 1282 1421 1286 -80 40 108 C ATOM 1305 NE ARG A 167 5.315 6.627 -0.831 1.00 12.06 N ANISOU 1305 NE ARG A 167 1609 1659 1314 -46 140 72 N ATOM 1306 CZ ARG A 167 5.945 7.707 -1.316 1.00 11.86 C ANISOU 1306 CZ ARG A 167 1599 1425 1485 17 73 24 C ATOM 1307 NH1 ARG A 167 6.712 8.482 -0.534 1.00 11.42 N ANISOU 1307 NH1 ARG A 167 1324 1435 1582 -58 68 154 N ATOM 1308 NH2 ARG A 167 5.756 7.921 -2.618 1.00 12.54 N ANISOU 1308 NH2 ARG A 167 1721 1533 1510 70 68 2 N ATOM 1309 N LEU A 168 3.307 4.953 5.520 1.00 9.94 N ANISOU 1309 N LEU A 168 1031 1354 1390 67 -56 -12 N ATOM 1310 CA LEU A 168 3.593 4.469 6.891 1.00 11.78 C ANISOU 1310 CA LEU A 168 1378 1578 1519 -9 13 118 C ATOM 1311 C LEU A 168 2.377 3.689 7.394 1.00 11.03 C ANISOU 1311 C LEU A 168 1272 1391 1527 11 -19 3 C ATOM 1312 O LEU A 168 2.565 2.678 8.063 1.00 11.18 O ANISOU 1312 O LEU A 168 1279 1499 1471 25 53 47 O ATOM 1313 CB LEU A 168 3.844 5.657 7.813 1.00 14.30 C ANISOU 1313 CB LEU A 168 1736 1714 1982 80 -61 -168 C ATOM 1314 CG LEU A 168 4.218 5.411 9.265 1.00 17.82 C ANISOU 1314 CG LEU A 168 2344 2221 2207 116 -140 -45 C ATOM 1315 CD1 LEU A 168 5.371 4.396 9.358 1.00 18.75 C ANISOU 1315 CD1 LEU A 168 2349 2381 2395 170 -185 -123 C ATOM 1316 CD2 LEU A 168 4.653 6.753 9.900 1.00 19.01 C ANISOU 1316 CD2 LEU A 168 2375 2290 2556 99 -97 -204 C ATOM 1317 N GLU A 169 1.165 4.111 7.095 1.00 10.25 N ANISOU 1317 N GLU A 169 1164 1381 1350 31 45 -21 N ATOM 1318 CA GLU A 169 0.002 3.270 7.419 1.00 11.32 C ANISOU 1318 CA GLU A 169 1408 1317 1574 -69 55 -30 C ATOM 1319 C GLU A 169 0.112 1.864 6.827 1.00 11.63 C ANISOU 1319 C GLU A 169 1507 1420 1492 4 13 -14 C ATOM 1320 O GLU A 169 -0.168 0.892 7.546 1.00 12.20 O ANISOU 1320 O GLU A 169 1525 1612 1500 -13 69 135 O ATOM 1321 CB GLU A 169 -1.305 3.948 6.976 1.00 13.75 C ANISOU 1321 CB GLU A 169 1513 1662 2050 44 14 14 C ATOM 1322 CG GLU A 169 -1.502 5.213 7.845 1.00 16.94 C ANISOU 1322 CG GLU A 169 2173 2079 2183 59 77 -250 C ATOM 1323 CD GLU A 169 -2.615 6.122 7.359 1.00 21.47 C ANISOU 1323 CD GLU A 169 2573 2693 2892 226 -76 -52 C ATOM 1324 OE1 GLU A 169 -3.100 5.948 6.240 1.00 23.01 O ANISOU 1324 OE1 GLU A 169 2612 3076 3056 290 -258 13 O ATOM 1325 OE2 GLU A 169 -3.008 7.060 8.108 1.00 23.37 O ANISOU 1325 OE2 GLU A 169 2698 2890 3293 351 145 -146 O ATOM 1326 N ARG A 170 0.530 1.733 5.576 1.00 10.26 N ANISOU 1326 N ARG A 170 1141 1401 1356 55 -26 19 N ATOM 1327 CA ARG A 170 0.684 0.427 4.963 1.00 11.45 C ANISOU 1327 CA ARG A 170 1362 1434 1555 1 -77 -14 C ATOM 1328 C ARG A 170 1.812 -0.376 5.612 1.00 10.49 C ANISOU 1328 C ARG A 170 1275 1360 1352 18 80 -16 C ATOM 1329 O ARG A 170 1.681 -1.592 5.784 1.00 10.78 O ANISOU 1329 O ARG A 170 1183 1420 1495 -34 29 66 O ATOM 1330 CB ARG A 170 0.880 0.562 3.433 1.00 14.14 C ANISOU 1330 CB ARG A 170 1911 1814 1646 -185 196 -67 C ATOM 1331 CG ARG A 170 -0.499 0.924 2.870 1.00 21.09 C ANISOU 1331 CG ARG A 170 2469 2666 2877 185 -109 65 C ATOM 1332 CD ARG A 170 -0.623 0.921 1.374 1.00 26.52 C ANISOU 1332 CD ARG A 170 3507 3482 3086 114 -57 -33 C ATOM 1333 NE ARG A 170 0.038 2.092 0.800 1.00 30.40 N ANISOU 1333 NE ARG A 170 3926 3670 3954 -79 46 72 N ATOM 1334 CZ ARG A 170 -0.588 3.274 0.577 1.00 31.91 C ANISOU 1334 CZ ARG A 170 4083 3903 4138 80 -1 105 C ATOM 1335 NH1 ARG A 170 -1.883 3.423 0.860 1.00 31.15 N ANISOU 1335 NH1 ARG A 170 4046 3813 3976 107 8 44 N ATOM 1336 NH2 ARG A 170 0.150 4.273 0.072 1.00 32.19 N ANISOU 1336 NH2 ARG A 170 4229 3824 4178 16 4 86 N ATOM 1337 N ALA A 171 2.906 0.280 5.955 1.00 10.22 N ANISOU 1337 N ALA A 171 1214 1417 1253 75 -44 65 N ATOM 1338 CA ALA A 171 4.014 -0.414 6.639 1.00 10.23 C ANISOU 1338 CA ALA A 171 1216 1263 1407 13 -18 71 C ATOM 1339 C ALA A 171 3.581 -0.917 8.009 1.00 9.55 C ANISOU 1339 C ALA A 171 1203 1098 1326 -39 13 36 C ATOM 1340 O ALA A 171 3.975 -2.014 8.406 1.00 8.94 O ANISOU 1340 O ALA A 171 1072 1213 1112 -31 39 67 O ATOM 1341 CB ALA A 171 5.185 0.567 6.759 1.00 10.59 C ANISOU 1341 CB ALA A 171 1174 1206 1642 36 -87 116 C ATOM 1342 N ILE A 172 2.784 -0.127 8.746 1.00 9.34 N ANISOU 1342 N ILE A 172 1235 1195 1117 -135 80 21 N ATOM 1343 CA ILE A 172 2.260 -0.656 10.035 1.00 9.55 C ANISOU 1343 CA ILE A 172 1336 1132 1162 -145 110 2 C ATOM 1344 C ILE A 172 1.446 -1.906 9.795 1.00 9.94 C ANISOU 1344 C ILE A 172 1307 1161 1309 -32 76 -79 C ATOM 1345 O ILE A 172 1.605 -2.895 10.533 1.00 10.76 O ANISOU 1345 O ILE A 172 1424 1429 1235 48 -34 8 O ATOM 1346 CB ILE A 172 1.437 0.427 10.757 1.00 10.42 C ANISOU 1346 CB ILE A 172 1432 1265 1262 -131 131 -44 C ATOM 1347 CG1 ILE A 172 2.374 1.562 11.271 1.00 10.81 C ANISOU 1347 CG1 ILE A 172 1477 1281 1351 -87 33 -113 C ATOM 1348 CG2 ILE A 172 0.646 -0.159 11.914 1.00 11.07 C ANISOU 1348 CG2 ILE A 172 1628 1415 1164 -174 153 -89 C ATOM 1349 CD1 ILE A 172 1.612 2.875 11.570 1.00 12.55 C ANISOU 1349 CD1 ILE A 172 1853 1353 1561 65 -5 -35 C ATOM 1350 N GLU A 173 0.562 -1.898 8.803 1.00 10.76 N ANISOU 1350 N GLU A 173 1369 1307 1411 108 -21 -146 N ATOM 1351 CA GLU A 173 -0.246 -3.098 8.515 1.00 13.06 C ANISOU 1351 CA GLU A 173 1649 1498 1814 -95 136 -104 C ATOM 1352 C GLU A 173 0.671 -4.271 8.204 1.00 11.65 C ANISOU 1352 C GLU A 173 1581 1383 1461 -56 -26 -4 C ATOM 1353 O GLU A 173 0.453 -5.410 8.660 1.00 11.16 O ANISOU 1353 O GLU A 173 1399 1331 1509 -103 190 -126 O ATOM 1354 CB GLU A 173 -1.168 -2.822 7.306 1.00 18.31 C ANISOU 1354 CB GLU A 173 2294 2493 2170 -145 -162 95 C ATOM 1355 CG GLU A 173 -2.261 -1.828 7.671 1.00 25.78 C ANISOU 1355 CG GLU A 173 3132 3139 3525 172 159 -139 C ATOM 1356 CD GLU A 173 -3.074 -1.280 6.528 1.00 31.97 C ANISOU 1356 CD GLU A 173 3972 4202 3971 126 -186 101 C ATOM 1357 OE1 GLU A 173 -2.820 -1.461 5.320 1.00 34.28 O ANISOU 1357 OE1 GLU A 173 4236 4631 4158 45 78 9 O ATOM 1358 OE2 GLU A 173 -4.074 -0.564 6.831 1.00 36.09 O ANISOU 1358 OE2 GLU A 173 4259 4813 4639 296 50 -41 O ATOM 1359 N GLU A 174 1.733 -4.047 7.414 1.00 11.87 N ANISOU 1359 N GLU A 174 1561 1390 1559 36 13 -110 N ATOM 1360 CA GLU A 174 2.626 -5.141 7.036 1.00 12.04 C ANISOU 1360 CA GLU A 174 1490 1515 1572 137 27 16 C ATOM 1361 C GLU A 174 3.284 -5.816 8.252 1.00 10.95 C ANISOU 1361 C GLU A 174 1378 1325 1457 -35 108 50 C ATOM 1362 O GLU A 174 3.587 -7.019 8.162 1.00 10.85 O ANISOU 1362 O GLU A 174 1296 1282 1543 -12 91 127 O ATOM 1363 CB GLU A 174 3.767 -4.636 6.117 1.00 14.54 C ANISOU 1363 CB GLU A 174 1818 1847 1859 -29 155 58 C ATOM 1364 CG GLU A 174 3.289 -4.330 4.711 1.00 18.37 C ANISOU 1364 CG GLU A 174 2588 2348 2045 193 70 53 C ATOM 1365 CD GLU A 174 3.737 -5.385 3.696 1.00 21.71 C ANISOU 1365 CD GLU A 174 3259 2586 2405 208 62 -138 C ATOM 1366 OE1 GLU A 174 4.245 -6.410 4.193 1.00 26.29 O ANISOU 1366 OE1 GLU A 174 3801 2984 3203 492 -3 149 O ATOM 1367 OE2 GLU A 174 3.610 -5.180 2.480 1.00 19.71 O ANISOU 1367 OE2 GLU A 174 2927 2277 2287 208 32 -155 O ATOM 1368 N VAL A 175 3.577 -5.051 9.298 1.00 10.39 N ANISOU 1368 N VAL A 175 1274 1331 1341 -125 144 114 N ATOM 1369 CA VAL A 175 4.257 -5.657 10.477 1.00 11.72 C ANISOU 1369 CA VAL A 175 1500 1556 1397 -46 90 23 C ATOM 1370 C VAL A 175 3.262 -6.052 11.552 1.00 11.87 C ANISOU 1370 C VAL A 175 1505 1575 1431 -147 13 170 C ATOM 1371 O VAL A 175 3.696 -6.464 12.658 1.00 11.97 O ANISOU 1371 O VAL A 175 1563 1532 1453 -262 32 375 O ATOM 1372 CB VAL A 175 5.355 -4.761 11.075 1.00 11.92 C ANISOU 1372 CB VAL A 175 1502 1545 1484 -36 98 -60 C ATOM 1373 CG1 VAL A 175 6.479 -4.654 10.036 1.00 12.81 C ANISOU 1373 CG1 VAL A 175 1618 1571 1679 -164 168 -88 C ATOM 1374 CG2 VAL A 175 4.903 -3.371 11.520 1.00 11.48 C ANISOU 1374 CG2 VAL A 175 1596 1339 1425 -9 -41 147 C ATOM 1375 N SER A 176 1.948 -5.979 11.281 1.00 11.39 N ANISOU 1375 N SER A 176 1463 1433 1432 -15 7 147 N ATOM 1376 CA SER A 176 0.925 -6.275 12.273 1.00 11.92 C ANISOU 1376 CA SER A 176 1509 1441 1579 -65 90 141 C ATOM 1377 C SER A 176 0.637 -7.774 12.386 1.00 12.95 C ANISOU 1377 C SER A 176 1720 1395 1807 9 77 -43 C ATOM 1378 O SER A 176 -0.531 -8.179 12.547 1.00 14.52 O ANISOU 1378 O SER A 176 1956 1380 2180 -19 325 -7 O ATOM 1379 CB SER A 176 -0.419 -5.566 11.948 1.00 13.65 C ANISOU 1379 CB SER A 176 1545 1654 1985 79 271 189 C ATOM 1380 OG SER A 176 -0.187 -4.174 12.232 1.00 16.68 O ANISOU 1380 OG SER A 176 2017 2035 2284 -38 -9 -97 O ATOM 1381 N TYR A 177 1.619 -8.611 12.121 1.00 12.22 N ANISOU 1381 N TYR A 177 1658 1300 1687 44 -3 170 N ATOM 1382 CA TYR A 177 1.500 -10.055 12.055 1.00 12.05 C ANISOU 1382 CA TYR A 177 1685 1362 1529 -35 -84 34 C ATOM 1383 C TYR A 177 2.428 -10.659 13.123 1.00 12.31 C ANISOU 1383 C TYR A 177 1616 1338 1723 -23 -78 193 C ATOM 1384 O TYR A 177 3.613 -10.293 13.161 1.00 14.22 O ANISOU 1384 O TYR A 177 1777 1581 2047 -254 -147 330 O ATOM 1385 CB TYR A 177 1.899 -10.617 10.671 1.00 12.18 C ANISOU 1385 CB TYR A 177 1688 1367 1573 -3 -19 53 C ATOM 1386 CG TYR A 177 0.798 -10.293 9.671 1.00 12.37 C ANISOU 1386 CG TYR A 177 1666 1582 1453 -26 4 -45 C ATOM 1387 CD1 TYR A 177 0.729 -9.026 9.096 1.00 13.54 C ANISOU 1387 CD1 TYR A 177 1788 1678 1680 -68 -16 80 C ATOM 1388 CD2 TYR A 177 -0.150 -11.250 9.322 1.00 12.83 C ANISOU 1388 CD2 TYR A 177 1576 1623 1677 -46 107 27 C ATOM 1389 CE1 TYR A 177 -0.259 -8.700 8.173 1.00 14.36 C ANISOU 1389 CE1 TYR A 177 1678 1944 1834 -94 11 152 C ATOM 1390 CE2 TYR A 177 -1.175 -10.935 8.440 1.00 14.05 C ANISOU 1390 CE2 TYR A 177 1752 1930 1656 -96 29 80 C ATOM 1391 CZ TYR A 177 -1.187 -9.683 7.860 1.00 15.07 C ANISOU 1391 CZ TYR A 177 1875 1905 1946 -10 -63 8 C ATOM 1392 OH TYR A 177 -2.185 -9.349 6.965 1.00 17.17 O ANISOU 1392 OH TYR A 177 1914 2541 2067 -211 -207 212 O ATOM 1393 N GLY A 178 1.944 -11.650 13.836 1.00 10.26 N ANISOU 1393 N GLY A 178 1273 1320 1305 -91 -138 72 N ATOM 1394 CA GLY A 178 2.742 -12.328 14.866 1.00 9.31 C ANISOU 1394 CA GLY A 178 1112 978 1445 -96 -159 24 C ATOM 1395 C GLY A 178 2.731 -13.820 14.570 1.00 9.75 C ANISOU 1395 C GLY A 178 1174 1115 1416 -16 -50 -21 C ATOM 1396 O GLY A 178 2.188 -14.247 13.525 1.00 10.01 O ANISOU 1396 O GLY A 178 1425 1169 1207 -36 -35 31 O ATOM 1397 N LYS A 179 3.352 -14.615 15.440 1.00 10.31 N ANISOU 1397 N LYS A 179 1285 1294 1341 77 81 74 N ATOM 1398 CA LYS A 179 3.297 -16.051 15.180 1.00 11.29 C ANISOU 1398 CA LYS A 179 1430 1340 1520 -163 53 68 C ATOM 1399 C LYS A 179 3.293 -16.743 16.554 1.00 11.71 C ANISOU 1399 C LYS A 179 1515 1424 1510 -113 -14 47 C ATOM 1400 O LYS A 179 4.002 -16.309 17.437 1.00 11.82 O ANISOU 1400 O LYS A 179 1616 1356 1519 -236 -48 145 O ATOM 1401 CB LYS A 179 4.445 -16.615 14.331 1.00 13.19 C ANISOU 1401 CB LYS A 179 1553 1773 1686 89 2 -19 C ATOM 1402 CG LYS A 179 5.802 -16.544 15.040 1.00 14.44 C ANISOU 1402 CG LYS A 179 1506 1915 2063 -53 -4 -48 C ATOM 1403 CD LYS A 179 6.952 -17.225 14.300 1.00 15.30 C ANISOU 1403 CD LYS A 179 1821 1873 2119 10 96 -98 C ATOM 1404 CE LYS A 179 6.700 -18.676 13.972 1.00 15.48 C ANISOU 1404 CE LYS A 179 2002 1826 2054 43 -54 65 C ATOM 1405 NZ LYS A 179 7.133 -19.667 15.022 1.00 14.24 N ANISOU 1405 NZ LYS A 179 1709 1838 1863 33 93 118 N ATOM 1406 N ILE A 180 2.397 -17.711 16.691 1.00 10.53 N ANISOU 1406 N ILE A 180 1352 1227 1421 -33 198 35 N ATOM 1407 CA ILE A 180 2.396 -18.563 17.882 1.00 11.54 C ANISOU 1407 CA ILE A 180 1645 1285 1455 13 32 23 C ATOM 1408 C ILE A 180 2.219 -19.983 17.291 1.00 12.24 C ANISOU 1408 C ILE A 180 1708 1428 1514 -36 31 -57 C ATOM 1409 O ILE A 180 1.124 -20.552 17.413 1.00 13.52 O ANISOU 1409 O ILE A 180 1695 1630 1814 -29 59 -79 O ATOM 1410 CB ILE A 180 1.243 -18.240 18.848 1.00 12.63 C ANISOU 1410 CB ILE A 180 1756 1491 1553 -34 71 12 C ATOM 1411 CG1 ILE A 180 1.118 -16.763 19.244 1.00 13.67 C ANISOU 1411 CG1 ILE A 180 1850 1542 1802 22 2 30 C ATOM 1412 CG2 ILE A 180 1.408 -19.104 20.118 1.00 13.48 C ANISOU 1412 CG2 ILE A 180 2020 1596 1506 -32 85 36 C ATOM 1413 CD1 ILE A 180 2.203 -16.198 20.104 1.00 14.88 C ANISOU 1413 CD1 ILE A 180 1961 1772 1922 -182 -2 46 C ATOM 1414 N SER A 181 3.273 -20.507 16.667 1.00 11.04 N ANISOU 1414 N SER A 181 1600 1231 1363 -68 12 -42 N ATOM 1415 CA SER A 181 3.065 -21.713 15.820 1.00 11.13 C ANISOU 1415 CA SER A 181 1603 1374 1253 -39 -62 5 C ATOM 1416 C SER A 181 4.108 -22.779 16.150 1.00 11.36 C ANISOU 1416 C SER A 181 1508 1399 1408 -35 80 30 C ATOM 1417 O SER A 181 4.100 -23.858 15.573 1.00 11.97 O ANISOU 1417 O SER A 181 1551 1355 1641 -72 -19 49 O ATOM 1418 CB SER A 181 3.121 -21.343 14.331 1.00 10.59 C ANISOU 1418 CB SER A 181 1443 1338 1244 -153 0 43 C ATOM 1419 OG SER A 181 4.338 -20.718 14.023 1.00 11.17 O ANISOU 1419 OG SER A 181 1498 1497 1250 -173 -47 87 O ATOM 1420 N GLY A 182 4.987 -22.466 17.094 1.00 11.23 N ANISOU 1420 N GLY A 182 1348 1331 1587 -56 3 173 N ATOM 1421 CA GLY A 182 5.955 -23.465 17.588 1.00 11.89 C ANISOU 1421 CA GLY A 182 1357 1353 1808 16 63 84 C ATOM 1422 C GLY A 182 7.106 -23.716 16.638 1.00 11.65 C ANISOU 1422 C GLY A 182 1404 1448 1575 11 -27 5 C ATOM 1423 O GLY A 182 7.361 -22.979 15.678 1.00 12.30 O ANISOU 1423 O GLY A 182 1382 1628 1665 -58 17 69 O ATOM 1424 N ALA A 183 7.884 -24.733 16.970 1.00 12.23 N ANISOU 1424 N ALA A 183 1489 1517 1642 94 -8 15 N ATOM 1425 CA ALA A 183 9.253 -24.900 16.461 1.00 12.53 C ANISOU 1425 CA ALA A 183 1531 1510 1719 59 50 50 C ATOM 1426 C ALA A 183 9.434 -24.722 14.963 1.00 13.80 C ANISOU 1426 C ALA A 183 1806 1661 1777 31 -41 61 C ATOM 1427 O ALA A 183 10.440 -24.051 14.634 1.00 15.52 O ANISOU 1427 O ALA A 183 1793 1913 2191 -134 -117 132 O ATOM 1428 CB ALA A 183 9.712 -26.313 16.804 1.00 12.42 C ANISOU 1428 CB ALA A 183 1666 1581 1473 215 42 77 C ATOM 1429 N VAL A 184 8.674 -25.369 14.072 1.00 12.86 N ANISOU 1429 N VAL A 184 1464 1515 1909 73 -115 -18 N ATOM 1430 CA VAL A 184 8.881 -25.150 12.630 1.00 14.80 C ANISOU 1430 CA VAL A 184 1694 1887 2041 -27 -35 219 C ATOM 1431 C VAL A 184 7.619 -24.558 12.009 1.00 12.90 C ANISOU 1431 C VAL A 184 1639 1568 1692 -113 64 54 C ATOM 1432 O VAL A 184 7.430 -24.573 10.793 1.00 12.20 O ANISOU 1432 O VAL A 184 1575 1420 1641 -20 51 84 O ATOM 1433 CB VAL A 184 9.337 -26.415 11.879 1.00 19.25 C ANISOU 1433 CB VAL A 184 2465 2490 2359 131 85 -87 C ATOM 1434 CG1 VAL A 184 10.766 -26.772 12.358 1.00 19.87 C ANISOU 1434 CG1 VAL A 184 2512 2380 2659 100 39 -21 C ATOM 1435 CG2 VAL A 184 8.414 -27.606 12.081 1.00 20.35 C ANISOU 1435 CG2 VAL A 184 2617 2486 2630 62 -29 -70 C ATOM 1436 N GLY A 185 6.736 -23.959 12.816 1.00 11.11 N ANISOU 1436 N GLY A 185 1236 1189 1798 -95 30 185 N ATOM 1437 CA GLY A 185 5.651 -23.117 12.270 1.00 11.39 C ANISOU 1437 CA GLY A 185 1232 1453 1642 -142 -69 129 C ATOM 1438 C GLY A 185 4.406 -23.908 11.864 1.00 11.72 C ANISOU 1438 C GLY A 185 1390 1394 1671 -154 -66 37 C ATOM 1439 O GLY A 185 3.513 -23.344 11.247 1.00 12.09 O ANISOU 1439 O GLY A 185 1429 1555 1608 -220 -98 156 O ATOM 1440 N ASN A 186 4.332 -25.174 12.243 1.00 11.04 N ANISOU 1440 N ASN A 186 1309 1360 1526 -237 25 52 N ATOM 1441 CA ASN A 186 3.217 -26.006 11.764 1.00 10.81 C ANISOU 1441 CA ASN A 186 1363 1352 1394 -229 51 -65 C ATOM 1442 C ASN A 186 2.274 -26.437 12.875 1.00 10.52 C ANISOU 1442 C ASN A 186 1281 1211 1504 -275 38 -64 C ATOM 1443 O ASN A 186 1.417 -27.318 12.639 1.00 9.86 O ANISOU 1443 O ASN A 186 1157 1054 1537 -264 -90 -106 O ATOM 1444 CB ASN A 186 3.706 -27.228 11.005 1.00 11.33 C ANISOU 1444 CB ASN A 186 1350 1298 1657 -34 52 20 C ATOM 1445 CG ASN A 186 4.635 -28.104 11.796 1.00 11.69 C ANISOU 1445 CG ASN A 186 1432 1342 1670 -71 21 14 C ATOM 1446 OD1 ASN A 186 4.714 -28.021 13.036 1.00 11.36 O ANISOU 1446 OD1 ASN A 186 1367 1229 1720 -201 183 32 O ATOM 1447 ND2 ASN A 186 5.347 -28.990 11.095 1.00 12.04 N ANISOU 1447 ND2 ASN A 186 1306 1450 1819 -109 207 5 N ATOM 1448 N TYR A 187 2.319 -25.849 14.057 1.00 9.88 N ANISOU 1448 N TYR A 187 1209 1253 1292 -58 88 54 N ATOM 1449 CA TYR A 187 1.297 -26.100 15.100 1.00 10.52 C ANISOU 1449 CA TYR A 187 1208 1306 1481 -43 141 158 C ATOM 1450 C TYR A 187 1.390 -27.516 15.636 1.00 10.24 C ANISOU 1450 C TYR A 187 1232 1301 1358 -32 99 55 C ATOM 1451 O TYR A 187 0.409 -27.945 16.278 1.00 11.37 O ANISOU 1451 O TYR A 187 1374 1179 1768 -189 189 220 O ATOM 1452 CB TYR A 187 -0.148 -25.714 14.726 1.00 10.60 C ANISOU 1452 CB TYR A 187 1282 1375 1370 -51 24 179 C ATOM 1453 CG TYR A 187 -0.223 -24.303 14.151 1.00 10.46 C ANISOU 1453 CG TYR A 187 1308 1283 1382 -96 11 100 C ATOM 1454 CD1 TYR A 187 -0.302 -24.192 12.745 1.00 11.53 C ANISOU 1454 CD1 TYR A 187 1436 1486 1460 -65 8 153 C ATOM 1455 CD2 TYR A 187 -0.157 -23.161 14.927 1.00 9.89 C ANISOU 1455 CD2 TYR A 187 1154 1300 1305 0 14 99 C ATOM 1456 CE1 TYR A 187 -0.303 -22.922 12.154 1.00 11.44 C ANISOU 1456 CE1 TYR A 187 1519 1446 1383 -11 45 111 C ATOM 1457 CE2 TYR A 187 -0.195 -21.896 14.350 1.00 10.01 C ANISOU 1457 CE2 TYR A 187 1132 1275 1396 -170 -34 62 C ATOM 1458 CZ TYR A 187 -0.242 -21.811 12.958 1.00 11.15 C ANISOU 1458 CZ TYR A 187 1356 1427 1452 -63 -56 99 C ATOM 1459 OH TYR A 187 -0.269 -20.605 12.345 1.00 12.82 O ANISOU 1459 OH TYR A 187 1599 1607 1665 -160 32 248 O ATOM 1460 N ALA A 188 2.546 -28.185 15.513 1.00 10.83 N ANISOU 1460 N ALA A 188 1387 1262 1466 95 -15 18 N ATOM 1461 CA ALA A 188 2.637 -29.549 16.062 1.00 11.15 C ANISOU 1461 CA ALA A 188 1433 1320 1484 63 50 42 C ATOM 1462 C ALA A 188 2.507 -29.467 17.594 1.00 12.83 C ANISOU 1462 C ALA A 188 1686 1623 1565 -4 48 -31 C ATOM 1463 O ALA A 188 1.911 -30.357 18.213 1.00 13.33 O ANISOU 1463 O ALA A 188 1803 1628 1634 -217 -10 -57 O ATOM 1464 CB ALA A 188 4.008 -30.133 15.722 1.00 10.97 C ANISOU 1464 CB ALA A 188 1437 1234 1497 73 50 31 C ATOM 1465 N ASN A 189 3.011 -28.387 18.192 1.00 12.13 N ANISOU 1465 N ASN A 189 1255 1606 1748 -3 -19 -38 N ATOM 1466 CA ASN A 189 3.104 -28.284 19.645 1.00 12.85 C ANISOU 1466 CA ASN A 189 1587 1594 1701 8 41 8 C ATOM 1467 C ASN A 189 2.226 -27.203 20.253 1.00 12.01 C ANISOU 1467 C ASN A 189 1470 1566 1527 -93 12 45 C ATOM 1468 O ASN A 189 2.121 -27.179 21.498 1.00 12.13 O ANISOU 1468 O ASN A 189 1707 1484 1418 -20 -49 162 O ATOM 1469 CB ASN A 189 4.556 -28.024 20.101 1.00 13.72 C ANISOU 1469 CB ASN A 189 1629 1653 1931 -10 33 -49 C ATOM 1470 CG ASN A 189 5.532 -28.990 19.418 1.00 15.54 C ANISOU 1470 CG ASN A 189 1906 1795 2203 51 111 -101 C ATOM 1471 OD1 ASN A 189 5.333 -30.208 19.434 1.00 15.80 O ANISOU 1471 OD1 ASN A 189 1953 1779 2269 86 -15 -42 O ATOM 1472 ND2 ASN A 189 6.567 -28.436 18.812 1.00 16.29 N ANISOU 1472 ND2 ASN A 189 1927 1986 2278 -4 71 -66 N ATOM 1473 N VAL A 190 1.603 -26.337 19.478 1.00 11.81 N ANISOU 1473 N VAL A 190 1320 1498 1670 -85 30 77 N ATOM 1474 CA VAL A 190 0.688 -25.328 20.052 1.00 12.88 C ANISOU 1474 CA VAL A 190 1502 1630 1761 -46 3 -57 C ATOM 1475 C VAL A 190 -0.416 -25.161 19.009 1.00 13.05 C ANISOU 1475 C VAL A 190 1595 1671 1694 20 -1 44 C ATOM 1476 O VAL A 190 -0.060 -25.078 17.846 1.00 12.65 O ANISOU 1476 O VAL A 190 1487 1584 1737 40 105 -50 O ATOM 1477 CB VAL A 190 1.432 -24.023 20.358 1.00 12.79 C ANISOU 1477 CB VAL A 190 1646 1525 1688 -37 122 3 C ATOM 1478 CG1 VAL A 190 2.268 -23.498 19.187 1.00 12.49 C ANISOU 1478 CG1 VAL A 190 1538 1449 1760 -56 105 21 C ATOM 1479 CG2 VAL A 190 0.409 -22.933 20.750 1.00 12.55 C ANISOU 1479 CG2 VAL A 190 1472 1539 1755 -63 131 -12 C ATOM 1480 N PRO A 191 -1.702 -25.115 19.361 1.00 13.80 N ANISOU 1480 N PRO A 191 1576 1870 1798 -131 -4 72 N ATOM 1481 CA PRO A 191 -2.748 -25.209 18.329 1.00 14.07 C ANISOU 1481 CA PRO A 191 1637 1900 1808 -60 -25 136 C ATOM 1482 C PRO A 191 -2.947 -23.882 17.613 1.00 12.74 C ANISOU 1482 C PRO A 191 1466 1735 1640 -72 75 49 C ATOM 1483 O PRO A 191 -2.790 -22.824 18.228 1.00 11.43 O ANISOU 1483 O PRO A 191 1316 1807 1218 -73 109 9 O ATOM 1484 CB PRO A 191 -4.035 -25.556 19.097 1.00 15.31 C ANISOU 1484 CB PRO A 191 1671 2161 1985 -68 26 148 C ATOM 1485 CG PRO A 191 -3.611 -25.897 20.478 1.00 16.13 C ANISOU 1485 CG PRO A 191 1816 2384 1928 -179 31 61 C ATOM 1486 CD PRO A 191 -2.195 -25.422 20.722 1.00 14.12 C ANISOU 1486 CD PRO A 191 1653 1951 1760 -82 24 52 C ATOM 1487 N PRO A 192 -3.416 -23.896 16.370 1.00 12.90 N ANISOU 1487 N PRO A 192 1525 1662 1716 -85 60 5 N ATOM 1488 CA PRO A 192 -3.678 -22.681 15.622 1.00 12.76 C ANISOU 1488 CA PRO A 192 1526 1637 1684 -42 -11 14 C ATOM 1489 C PRO A 192 -4.798 -21.865 16.227 1.00 13.18 C ANISOU 1489 C PRO A 192 1696 1684 1629 -55 83 -13 C ATOM 1490 O PRO A 192 -4.794 -20.642 16.163 1.00 12.31 O ANISOU 1490 O PRO A 192 1522 1678 1475 -167 121 53 O ATOM 1491 CB PRO A 192 -3.966 -23.134 14.198 1.00 14.03 C ANISOU 1491 CB PRO A 192 1827 1701 1801 -31 -33 -31 C ATOM 1492 CG PRO A 192 -4.441 -24.552 14.371 1.00 14.29 C ANISOU 1492 CG PRO A 192 1859 1749 1821 -51 -5 121 C ATOM 1493 CD PRO A 192 -3.705 -25.119 15.566 1.00 13.56 C ANISOU 1493 CD PRO A 192 1690 1747 1715 -29 -62 -44 C ATOM 1494 N GLU A 193 -5.810 -22.506 16.846 1.00 14.57 N ANISOU 1494 N GLU A 193 1661 2056 1817 -185 94 -79 N ATOM 1495 CA GLU A 193 -6.830 -21.742 17.573 1.00 16.27 C ANISOU 1495 CA GLU A 193 1878 2264 2040 -39 120 -91 C ATOM 1496 C GLU A 193 -6.236 -20.938 18.728 1.00 16.05 C ANISOU 1496 C GLU A 193 1790 2352 1957 -128 144 -19 C ATOM 1497 O GLU A 193 -6.794 -19.870 18.993 1.00 16.68 O ANISOU 1497 O GLU A 193 1952 2302 2085 -62 128 -9 O ATOM 1498 CB GLU A 193 -7.883 -22.713 18.160 1.00 18.60 C ANISOU 1498 CB GLU A 193 2028 2652 2386 -142 235 -4 C ATOM 1499 CG GLU A 193 -8.579 -23.461 17.016 1.00 22.23 C ANISOU 1499 CG GLU A 193 2624 2972 2848 -132 -4 -166 C ATOM 1500 CD GLU A 193 -7.856 -24.748 16.625 1.00 24.04 C ANISOU 1500 CD GLU A 193 2832 3101 3200 50 11 -96 C ATOM 1501 OE1 GLU A 193 -6.787 -25.193 17.089 1.00 22.26 O ANISOU 1501 OE1 GLU A 193 2667 2769 3023 -113 -23 -24 O ATOM 1502 OE2 GLU A 193 -8.431 -25.394 15.695 1.00 27.28 O ANISOU 1502 OE2 GLU A 193 3267 3588 3512 -94 -143 -233 O ATOM 1503 N VAL A 194 -5.217 -21.435 19.408 1.00 13.36 N ANISOU 1503 N VAL A 194 1684 1828 1564 -152 248 -18 N ATOM 1504 CA VAL A 194 -4.534 -20.639 20.434 1.00 13.67 C ANISOU 1504 CA VAL A 194 1687 1806 1702 -102 64 64 C ATOM 1505 C VAL A 194 -3.831 -19.454 19.797 1.00 12.66 C ANISOU 1505 C VAL A 194 1559 1699 1554 5 15 38 C ATOM 1506 O VAL A 194 -3.952 -18.334 20.312 1.00 14.20 O ANISOU 1506 O VAL A 194 1846 1749 1801 -88 170 -9 O ATOM 1507 CB VAL A 194 -3.534 -21.538 21.198 1.00 14.31 C ANISOU 1507 CB VAL A 194 1852 1834 1752 -78 8 117 C ATOM 1508 CG1 VAL A 194 -2.618 -20.737 22.125 1.00 14.60 C ANISOU 1508 CG1 VAL A 194 1900 1854 1794 -11 -22 -19 C ATOM 1509 CG2 VAL A 194 -4.338 -22.570 22.020 1.00 14.67 C ANISOU 1509 CG2 VAL A 194 1904 1945 1726 -19 179 53 C ATOM 1510 N GLU A 195 -3.106 -19.674 18.683 1.00 11.08 N ANISOU 1510 N GLU A 195 1363 1445 1402 -80 -41 120 N ATOM 1511 CA GLU A 195 -2.431 -18.534 18.065 1.00 11.06 C ANISOU 1511 CA GLU A 195 1297 1564 1340 -34 146 118 C ATOM 1512 C GLU A 195 -3.448 -17.458 17.679 1.00 11.64 C ANISOU 1512 C GLU A 195 1461 1533 1427 10 140 25 C ATOM 1513 O GLU A 195 -3.208 -16.264 17.897 1.00 11.75 O ANISOU 1513 O GLU A 195 1374 1566 1525 100 210 -2 O ATOM 1514 CB GLU A 195 -1.716 -19.020 16.780 1.00 11.08 C ANISOU 1514 CB GLU A 195 1445 1346 1420 -98 180 1 C ATOM 1515 CG GLU A 195 -1.178 -17.831 15.947 1.00 10.77 C ANISOU 1515 CG GLU A 195 1438 1248 1406 -52 58 70 C ATOM 1516 CD GLU A 195 -0.513 -18.344 14.679 1.00 12.75 C ANISOU 1516 CD GLU A 195 1658 1600 1585 -3 39 -64 C ATOM 1517 OE1 GLU A 195 -1.284 -18.874 13.809 1.00 13.24 O ANISOU 1517 OE1 GLU A 195 1555 1749 1725 -6 -136 22 O ATOM 1518 OE2 GLU A 195 0.733 -18.256 14.556 1.00 13.97 O ANISOU 1518 OE2 GLU A 195 1693 1595 2021 -79 -6 -52 O ATOM 1519 N GLU A 196 -4.555 -17.896 17.056 1.00 11.74 N ANISOU 1519 N GLU A 196 1365 1743 1353 26 173 -41 N ATOM 1520 CA GLU A 196 -5.500 -16.905 16.514 1.00 13.50 C ANISOU 1520 CA GLU A 196 1711 1798 1620 110 82 -44 C ATOM 1521 C GLU A 196 -6.071 -16.077 17.659 1.00 13.72 C ANISOU 1521 C GLU A 196 1834 1742 1636 69 87 -62 C ATOM 1522 O GLU A 196 -6.191 -14.848 17.529 1.00 13.12 O ANISOU 1522 O GLU A 196 1958 1672 1353 14 214 -81 O ATOM 1523 CB GLU A 196 -6.575 -17.621 15.687 1.00 16.52 C ANISOU 1523 CB GLU A 196 1961 2279 2037 -100 -106 -36 C ATOM 1524 CG GLU A 196 -5.986 -18.258 14.436 1.00 19.49 C ANISOU 1524 CG GLU A 196 2383 2728 2294 -9 65 -103 C ATOM 1525 CD GLU A 196 -6.700 -19.391 13.741 1.00 23.36 C ANISOU 1525 CD GLU A 196 2812 3104 2958 -207 15 -251 C ATOM 1526 OE1 GLU A 196 -7.859 -19.694 14.119 1.00 24.90 O ANISOU 1526 OE1 GLU A 196 2684 3517 3258 -232 0 -349 O ATOM 1527 OE2 GLU A 196 -6.170 -20.056 12.784 1.00 24.29 O ANISOU 1527 OE2 GLU A 196 2893 3420 2917 -75 -31 -269 O ATOM 1528 N LYS A 197 -6.497 -16.719 18.743 1.00 13.93 N ANISOU 1528 N LYS A 197 1800 1835 1658 13 22 35 N ATOM 1529 CA LYS A 197 -7.024 -16.000 19.895 1.00 15.37 C ANISOU 1529 CA LYS A 197 1916 2025 1897 -34 4 -185 C ATOM 1530 C LYS A 197 -5.958 -15.117 20.561 1.00 13.13 C ANISOU 1530 C LYS A 197 1665 1689 1633 -16 68 95 C ATOM 1531 O LYS A 197 -6.216 -13.942 20.816 1.00 13.24 O ANISOU 1531 O LYS A 197 1408 1844 1780 117 90 -97 O ATOM 1532 CB LYS A 197 -7.520 -16.949 21.006 1.00 20.37 C ANISOU 1532 CB LYS A 197 2726 2499 2515 -89 100 244 C ATOM 1533 CG LYS A 197 -8.903 -17.532 20.735 1.00 26.76 C ANISOU 1533 CG LYS A 197 3084 3487 3597 -233 -108 33 C ATOM 1534 CD LYS A 197 -9.368 -18.203 22.063 1.00 31.06 C ANISOU 1534 CD LYS A 197 3996 3968 3836 -104 94 231 C ATOM 1535 CE LYS A 197 -10.862 -18.449 22.010 1.00 34.07 C ANISOU 1535 CE LYS A 197 4071 4393 4481 -92 24 81 C ATOM 1536 NZ LYS A 197 -11.588 -17.210 21.602 1.00 36.57 N ANISOU 1536 NZ LYS A 197 4519 4573 4802 75 22 138 N ATOM 1537 N ALA A 198 -4.792 -15.683 20.865 1.00 11.26 N ANISOU 1537 N ALA A 198 1409 1554 1317 -153 131 -16 N ATOM 1538 CA ALA A 198 -3.751 -14.906 21.548 1.00 11.08 C ANISOU 1538 CA ALA A 198 1315 1490 1407 -39 27 87 C ATOM 1539 C ALA A 198 -3.362 -13.648 20.753 1.00 11.66 C ANISOU 1539 C ALA A 198 1521 1489 1419 -30 62 93 C ATOM 1540 O ALA A 198 -3.267 -12.555 21.334 1.00 12.20 O ANISOU 1540 O ALA A 198 1503 1566 1566 -17 99 88 O ATOM 1541 CB ALA A 198 -2.459 -15.725 21.741 1.00 9.81 C ANISOU 1541 CB ALA A 198 1258 1232 1237 -88 99 258 C ATOM 1542 N LEU A 199 -3.154 -13.808 19.455 1.00 10.97 N ANISOU 1542 N LEU A 199 1200 1555 1411 47 181 143 N ATOM 1543 CA LEU A 199 -2.731 -12.616 18.675 1.00 11.66 C ANISOU 1543 CA LEU A 199 1569 1423 1439 35 109 31 C ATOM 1544 C LEU A 199 -3.850 -11.600 18.565 1.00 12.65 C ANISOU 1544 C LEU A 199 1616 1582 1609 91 128 -33 C ATOM 1545 O LEU A 199 -3.569 -10.392 18.579 1.00 12.59 O ANISOU 1545 O LEU A 199 1627 1579 1577 13 232 -94 O ATOM 1546 CB LEU A 199 -2.250 -13.034 17.275 1.00 11.25 C ANISOU 1546 CB LEU A 199 1405 1413 1456 13 152 60 C ATOM 1547 CG LEU A 199 -0.977 -13.892 17.307 1.00 10.20 C ANISOU 1547 CG LEU A 199 1230 1402 1243 -27 92 -170 C ATOM 1548 CD1 LEU A 199 -0.637 -14.341 15.871 1.00 11.19 C ANISOU 1548 CD1 LEU A 199 1541 1624 1087 -71 115 -39 C ATOM 1549 CD2 LEU A 199 0.245 -13.154 17.872 1.00 11.08 C ANISOU 1549 CD2 LEU A 199 1309 1608 1293 -142 37 -153 C ATOM 1550 N SER A 200 -5.101 -12.054 18.481 1.00 13.83 N ANISOU 1550 N SER A 200 1706 1900 1650 -38 -10 -37 N ATOM 1551 CA SER A 200 -6.193 -11.087 18.516 1.00 15.83 C ANISOU 1551 CA SER A 200 1973 1976 2066 108 -18 -11 C ATOM 1552 C SER A 200 -6.196 -10.256 19.802 1.00 15.12 C ANISOU 1552 C SER A 200 1775 1945 2022 16 -32 36 C ATOM 1553 O SER A 200 -6.485 -9.041 19.695 1.00 14.78 O ANISOU 1553 O SER A 200 1674 1888 2053 -87 32 66 O ATOM 1554 CB SER A 200 -7.566 -11.735 18.299 1.00 19.91 C ANISOU 1554 CB SER A 200 2339 2533 2694 -212 -171 -29 C ATOM 1555 OG SER A 200 -7.946 -12.404 19.520 1.00 25.56 O ANISOU 1555 OG SER A 200 3157 3382 3172 -89 121 176 O ATOM 1556 N TYR A 201 -5.875 -10.801 20.979 1.00 14.12 N ANISOU 1556 N TYR A 201 1633 1827 1904 -118 111 31 N ATOM 1557 CA TYR A 201 -5.817 -10.002 22.191 1.00 14.70 C ANISOU 1557 CA TYR A 201 1770 1948 1868 -114 92 20 C ATOM 1558 C TYR A 201 -4.724 -8.928 22.078 1.00 14.93 C ANISOU 1558 C TYR A 201 1866 1838 1971 -111 163 -13 C ATOM 1559 O TYR A 201 -4.848 -7.888 22.704 1.00 16.38 O ANISOU 1559 O TYR A 201 2052 2045 2125 -126 388 -180 O ATOM 1560 CB TYR A 201 -5.440 -10.821 23.454 1.00 15.32 C ANISOU 1560 CB TYR A 201 1944 1995 1881 -18 116 47 C ATOM 1561 CG TYR A 201 -6.314 -12.020 23.715 1.00 17.03 C ANISOU 1561 CG TYR A 201 2262 2117 2091 -121 125 25 C ATOM 1562 CD1 TYR A 201 -5.734 -13.235 24.107 1.00 18.23 C ANISOU 1562 CD1 TYR A 201 2440 2245 2242 -13 74 21 C ATOM 1563 CD2 TYR A 201 -7.684 -11.948 23.566 1.00 19.29 C ANISOU 1563 CD2 TYR A 201 2322 2533 2473 -94 47 38 C ATOM 1564 CE1 TYR A 201 -6.545 -14.340 24.335 1.00 19.96 C ANISOU 1564 CE1 TYR A 201 2565 2429 2592 -168 67 34 C ATOM 1565 CE2 TYR A 201 -8.510 -13.056 23.809 1.00 20.97 C ANISOU 1565 CE2 TYR A 201 2631 2493 2842 -129 41 36 C ATOM 1566 CZ TYR A 201 -7.920 -14.220 24.198 1.00 21.46 C ANISOU 1566 CZ TYR A 201 2652 2632 2870 -65 -4 84 C ATOM 1567 OH TYR A 201 -8.673 -15.358 24.431 1.00 23.08 O ANISOU 1567 OH TYR A 201 2717 2917 3137 -223 11 71 O ATOM 1568 N LEU A 202 -3.659 -9.209 21.331 1.00 13.81 N ANISOU 1568 N LEU A 202 1694 1787 1766 -101 48 -24 N ATOM 1569 CA LEU A 202 -2.558 -8.261 21.160 1.00 13.51 C ANISOU 1569 CA LEU A 202 1649 1772 1711 -38 38 59 C ATOM 1570 C LEU A 202 -2.729 -7.254 20.021 1.00 14.16 C ANISOU 1570 C LEU A 202 1763 1779 1838 -31 -12 86 C ATOM 1571 O LEU A 202 -1.838 -6.402 19.785 1.00 14.44 O ANISOU 1571 O LEU A 202 1834 1753 1899 -124 -78 132 O ATOM 1572 CB LEU A 202 -1.299 -9.097 20.918 1.00 13.10 C ANISOU 1572 CB LEU A 202 1627 1687 1662 -26 5 8 C ATOM 1573 CG LEU A 202 -0.838 -10.034 22.051 1.00 13.86 C ANISOU 1573 CG LEU A 202 1772 1753 1742 45 4 4 C ATOM 1574 CD1 LEU A 202 0.350 -10.862 21.521 1.00 13.62 C ANISOU 1574 CD1 LEU A 202 1599 1813 1764 34 -22 -9 C ATOM 1575 CD2 LEU A 202 -0.456 -9.241 23.302 1.00 14.17 C ANISOU 1575 CD2 LEU A 202 1866 1827 1692 -103 4 45 C ATOM 1576 N GLY A 203 -3.822 -7.392 19.286 1.00 13.46 N ANISOU 1576 N GLY A 203 1737 1680 1697 20 49 17 N ATOM 1577 CA GLY A 203 -4.084 -6.443 18.168 1.00 13.88 C ANISOU 1577 CA GLY A 203 1889 1749 1636 -21 -16 19 C ATOM 1578 C GLY A 203 -3.330 -6.870 16.910 1.00 13.62 C ANISOU 1578 C GLY A 203 1664 1711 1799 48 69 97 C ATOM 1579 O GLY A 203 -3.187 -6.058 15.968 1.00 14.73 O ANISOU 1579 O GLY A 203 1917 1658 2023 -4 99 153 O ATOM 1580 N LEU A 204 -2.892 -8.129 16.797 1.00 12.53 N ANISOU 1580 N LEU A 204 1465 1659 1637 -22 67 69 N ATOM 1581 CA LEU A 204 -2.093 -8.618 15.701 1.00 12.21 C ANISOU 1581 CA LEU A 204 1461 1675 1503 37 -43 85 C ATOM 1582 C LEU A 204 -2.844 -9.723 14.950 1.00 12.84 C ANISOU 1582 C LEU A 204 1631 1638 1612 -22 25 82 C ATOM 1583 O LEU A 204 -3.775 -10.352 15.460 1.00 14.50 O ANISOU 1583 O LEU A 204 1623 1999 1886 -283 87 -41 O ATOM 1584 CB LEU A 204 -0.752 -9.217 16.183 1.00 11.31 C ANISOU 1584 CB LEU A 204 1307 1591 1398 -40 41 149 C ATOM 1585 CG LEU A 204 0.135 -8.221 16.961 1.00 12.28 C ANISOU 1585 CG LEU A 204 1470 1562 1631 -70 -18 194 C ATOM 1586 CD1 LEU A 204 1.359 -8.982 17.496 1.00 12.16 C ANISOU 1586 CD1 LEU A 204 1395 1676 1549 -101 -80 203 C ATOM 1587 CD2 LEU A 204 0.583 -7.044 16.083 1.00 12.94 C ANISOU 1587 CD2 LEU A 204 1580 1567 1771 -178 -35 185 C ATOM 1588 N LYS A 205 -2.431 -9.990 13.712 1.00 12.49 N ANISOU 1588 N LYS A 205 1547 1593 1606 106 17 -3 N ATOM 1589 CA LYS A 205 -2.998 -11.104 12.947 1.00 12.86 C ANISOU 1589 CA LYS A 205 1601 1533 1753 51 11 38 C ATOM 1590 C LYS A 205 -1.986 -12.253 12.890 1.00 12.01 C ANISOU 1590 C LYS A 205 1447 1525 1592 -27 51 81 C ATOM 1591 O LYS A 205 -0.776 -12.031 12.889 1.00 11.79 O ANISOU 1591 O LYS A 205 1395 1230 1853 -234 -30 199 O ATOM 1592 CB LYS A 205 -3.213 -10.627 11.499 1.00 15.85 C ANISOU 1592 CB LYS A 205 2083 2085 1855 33 -126 78 C ATOM 1593 CG LYS A 205 -4.327 -9.560 11.474 1.00 20.57 C ANISOU 1593 CG LYS A 205 2550 2548 2718 326 -65 79 C ATOM 1594 CD LYS A 205 -4.525 -9.151 9.998 1.00 23.79 C ANISOU 1594 CD LYS A 205 3112 3132 2796 164 -11 148 C ATOM 1595 CE LYS A 205 -3.431 -8.125 9.765 1.00 27.19 C ANISOU 1595 CE LYS A 205 3402 3459 3469 -41 97 143 C ATOM 1596 NZ LYS A 205 -3.386 -7.107 10.862 1.00 29.75 N ANISOU 1596 NZ LYS A 205 3730 3997 3575 -116 83 -67 N ATOM 1597 N PRO A 206 -2.438 -13.479 12.686 1.00 11.91 N ANISOU 1597 N PRO A 206 1458 1487 1582 -43 65 1 N ATOM 1598 CA PRO A 206 -1.526 -14.597 12.533 1.00 11.46 C ANISOU 1598 CA PRO A 206 1429 1470 1456 -77 157 -2 C ATOM 1599 C PRO A 206 -0.842 -14.560 11.171 1.00 10.34 C ANISOU 1599 C PRO A 206 1228 1331 1371 -95 47 74 C ATOM 1600 O PRO A 206 -1.477 -14.385 10.130 1.00 9.93 O ANISOU 1600 O PRO A 206 1035 1437 1299 -116 180 148 O ATOM 1601 CB PRO A 206 -2.410 -15.844 12.597 1.00 13.21 C ANISOU 1601 CB PRO A 206 1573 1710 1737 -226 17 96 C ATOM 1602 CG PRO A 206 -3.797 -15.333 12.454 1.00 15.63 C ANISOU 1602 CG PRO A 206 1777 1896 2264 -48 124 -37 C ATOM 1603 CD PRO A 206 -3.872 -13.875 12.749 1.00 13.68 C ANISOU 1603 CD PRO A 206 1629 1785 1783 -179 188 -70 C ATOM 1604 N GLU A 207 0.470 -14.782 11.146 1.00 10.20 N ANISOU 1604 N GLU A 207 1283 1230 1364 -27 145 -75 N ATOM 1605 CA GLU A 207 1.136 -15.001 9.852 1.00 10.23 C ANISOU 1605 CA GLU A 207 1215 1348 1325 -8 108 -44 C ATOM 1606 C GLU A 207 0.427 -16.171 9.185 1.00 10.77 C ANISOU 1606 C GLU A 207 1302 1349 1443 -9 23 -28 C ATOM 1607 O GLU A 207 0.381 -17.249 9.809 1.00 11.23 O ANISOU 1607 O GLU A 207 1333 1354 1577 -41 83 -56 O ATOM 1608 CB GLU A 207 2.605 -15.333 10.165 1.00 11.30 C ANISOU 1608 CB GLU A 207 1374 1442 1476 179 115 -24 C ATOM 1609 CG GLU A 207 3.425 -15.504 8.868 1.00 11.78 C ANISOU 1609 CG GLU A 207 1626 1469 1381 -19 198 62 C ATOM 1610 CD GLU A 207 3.486 -14.165 8.107 1.00 12.74 C ANISOU 1610 CD GLU A 207 1711 1494 1637 38 29 63 C ATOM 1611 OE1 GLU A 207 3.160 -14.135 6.907 1.00 13.60 O ANISOU 1611 OE1 GLU A 207 1793 1783 1590 -74 36 93 O ATOM 1612 OE2 GLU A 207 3.865 -13.184 8.776 1.00 13.49 O ANISOU 1612 OE2 GLU A 207 1840 1499 1787 30 39 -70 O ATOM 1613 N PRO A 208 0.014 -16.065 7.928 1.00 11.07 N ANISOU 1613 N PRO A 208 1331 1294 1580 -67 -38 24 N ATOM 1614 CA PRO A 208 -0.844 -17.148 7.394 1.00 11.54 C ANISOU 1614 CA PRO A 208 1538 1360 1488 4 -101 -116 C ATOM 1615 C PRO A 208 -0.041 -18.427 7.305 1.00 11.65 C ANISOU 1615 C PRO A 208 1522 1305 1600 -31 -62 -1 C ATOM 1616 O PRO A 208 -0.586 -19.514 7.576 1.00 11.66 O ANISOU 1616 O PRO A 208 1333 1482 1617 -206 -53 9 O ATOM 1617 CB PRO A 208 -1.228 -16.640 6.013 1.00 13.47 C ANISOU 1617 CB PRO A 208 1860 1540 1719 115 -184 75 C ATOM 1618 CG PRO A 208 -0.948 -15.202 6.004 1.00 14.20 C ANISOU 1618 CG PRO A 208 1994 1640 1760 -158 -215 66 C ATOM 1619 CD PRO A 208 -0.182 -14.772 7.223 1.00 12.40 C ANISOU 1619 CD PRO A 208 1679 1540 1494 15 -126 134 C ATOM 1620 N VAL A 209 1.246 -18.368 6.944 1.00 11.02 N ANISOU 1620 N VAL A 209 1494 1244 1450 -24 20 -180 N ATOM 1621 CA VAL A 209 2.098 -19.564 7.091 1.00 12.30 C ANISOU 1621 CA VAL A 209 1395 1649 1631 144 -87 84 C ATOM 1622 C VAL A 209 3.458 -19.030 7.629 1.00 11.94 C ANISOU 1622 C VAL A 209 1523 1589 1425 52 -24 -56 C ATOM 1623 O VAL A 209 4.120 -18.265 6.883 1.00 12.02 O ANISOU 1623 O VAL A 209 1410 1679 1476 117 -66 111 O ATOM 1624 CB VAL A 209 2.679 -20.213 5.816 1.00 17.10 C ANISOU 1624 CB VAL A 209 2378 2076 2043 219 -103 -269 C ATOM 1625 CG1 VAL A 209 2.980 -21.694 6.023 1.00 18.72 C ANISOU 1625 CG1 VAL A 209 2727 2067 2319 177 -61 -204 C ATOM 1626 CG2 VAL A 209 2.190 -19.794 4.498 1.00 18.33 C ANISOU 1626 CG2 VAL A 209 2460 2427 2079 290 -107 -205 C ATOM 1627 N SER A 210 3.855 -19.466 8.809 1.00 11.58 N ANISOU 1627 N SER A 210 1458 1432 1508 -32 -40 127 N ATOM 1628 CA SER A 210 5.159 -19.065 9.343 1.00 11.88 C ANISOU 1628 CA SER A 210 1445 1488 1579 74 -65 -85 C ATOM 1629 C SER A 210 6.106 -20.258 9.317 1.00 12.33 C ANISOU 1629 C SER A 210 1441 1433 1809 -11 -75 9 C ATOM 1630 O SER A 210 5.671 -21.401 9.158 1.00 12.58 O ANISOU 1630 O SER A 210 1532 1419 1828 -58 -112 -37 O ATOM 1631 CB SER A 210 5.082 -18.528 10.784 1.00 12.61 C ANISOU 1631 CB SER A 210 1672 1627 1491 56 -47 -40 C ATOM 1632 OG SER A 210 4.284 -19.385 11.612 1.00 14.44 O ANISOU 1632 OG SER A 210 1938 1844 1704 -78 -9 -73 O ATOM 1633 N THR A 211 7.408 -19.982 9.439 1.00 11.17 N ANISOU 1633 N THR A 211 1232 1313 1700 68 -3 63 N ATOM 1634 CA THR A 211 8.344 -21.105 9.690 1.00 10.37 C ANISOU 1634 CA THR A 211 1251 1185 1506 -15 -27 21 C ATOM 1635 C THR A 211 8.663 -21.059 11.174 1.00 9.80 C ANISOU 1635 C THR A 211 1072 1220 1431 16 23 134 C ATOM 1636 O THR A 211 7.745 -20.794 11.965 1.00 10.29 O ANISOU 1636 O THR A 211 1145 1339 1426 89 -35 -77 O ATOM 1637 CB THR A 211 9.607 -20.954 8.820 1.00 11.03 C ANISOU 1637 CB THR A 211 1361 1283 1546 1 52 -65 C ATOM 1638 OG1 THR A 211 10.193 -19.660 9.072 1.00 11.01 O ANISOU 1638 OG1 THR A 211 1385 1206 1592 16 -5 146 O ATOM 1639 CG2 THR A 211 9.243 -21.044 7.328 1.00 13.25 C ANISOU 1639 CG2 THR A 211 1915 1482 1635 58 0 -19 C ATOM 1640 N GLN A 212 9.945 -21.267 11.608 1.00 8.87 N ANISOU 1640 N GLN A 212 1079 1073 1218 -11 -58 145 N ATOM 1641 CA GLN A 212 10.197 -20.886 13.003 1.00 10.05 C ANISOU 1641 CA GLN A 212 1247 1256 1317 48 -110 70 C ATOM 1642 C GLN A 212 10.018 -19.392 13.256 1.00 11.02 C ANISOU 1642 C GLN A 212 1433 1310 1443 55 13 47 C ATOM 1643 O GLN A 212 9.826 -18.968 14.410 1.00 9.94 O ANISOU 1643 O GLN A 212 1198 1206 1372 64 11 130 O ATOM 1644 CB GLN A 212 11.600 -21.355 13.411 1.00 10.00 C ANISOU 1644 CB GLN A 212 1185 1377 1237 25 -81 9 C ATOM 1645 CG GLN A 212 11.900 -21.107 14.885 1.00 10.84 C ANISOU 1645 CG GLN A 212 1435 1409 1275 59 -116 22 C ATOM 1646 CD GLN A 212 13.118 -21.923 15.317 1.00 11.39 C ANISOU 1646 CD GLN A 212 1391 1390 1548 74 -26 53 C ATOM 1647 OE1 GLN A 212 14.257 -21.457 15.303 1.00 11.60 O ANISOU 1647 OE1 GLN A 212 1562 1481 1364 -72 97 108 O ATOM 1648 NE2 GLN A 212 12.911 -23.149 15.806 1.00 11.97 N ANISOU 1648 NE2 GLN A 212 1548 1396 1604 -34 -12 86 N ATOM 1649 N VAL A 213 10.124 -18.554 12.192 1.00 10.37 N ANISOU 1649 N VAL A 213 1144 1224 1570 -11 10 135 N ATOM 1650 CA VAL A 213 10.054 -17.114 12.366 1.00 11.09 C ANISOU 1650 CA VAL A 213 1266 1266 1681 -49 -11 84 C ATOM 1651 C VAL A 213 8.966 -16.500 11.479 1.00 10.39 C ANISOU 1651 C VAL A 213 1177 1293 1477 -82 33 23 C ATOM 1652 O VAL A 213 8.438 -17.154 10.584 1.00 11.41 O ANISOU 1652 O VAL A 213 1411 1308 1617 -94 -6 -82 O ATOM 1653 CB VAL A 213 11.405 -16.442 11.949 1.00 10.97 C ANISOU 1653 CB VAL A 213 1232 1475 1460 -136 34 15 C ATOM 1654 CG1 VAL A 213 12.533 -16.923 12.873 1.00 11.83 C ANISOU 1654 CG1 VAL A 213 1359 1620 1518 -74 -8 161 C ATOM 1655 CG2 VAL A 213 11.792 -16.744 10.493 1.00 11.36 C ANISOU 1655 CG2 VAL A 213 1480 1358 1479 -167 15 115 C ATOM 1656 N VAL A 214 8.665 -15.225 11.724 1.00 10.29 N ANISOU 1656 N VAL A 214 1143 1305 1461 57 136 119 N ATOM 1657 CA VAL A 214 7.833 -14.405 10.838 1.00 9.95 C ANISOU 1657 CA VAL A 214 1251 1276 1251 12 79 74 C ATOM 1658 C VAL A 214 8.733 -14.030 9.646 1.00 9.69 C ANISOU 1658 C VAL A 214 1201 1270 1209 -40 39 68 C ATOM 1659 O VAL A 214 9.895 -13.632 9.854 1.00 10.50 O ANISOU 1659 O VAL A 214 1150 1429 1411 -76 110 231 O ATOM 1660 CB VAL A 214 7.416 -13.121 11.611 1.00 9.95 C ANISOU 1660 CB VAL A 214 1306 1314 1161 109 101 106 C ATOM 1661 CG1 VAL A 214 6.849 -12.067 10.635 1.00 10.66 C ANISOU 1661 CG1 VAL A 214 1370 1256 1425 137 31 59 C ATOM 1662 CG2 VAL A 214 6.427 -13.435 12.732 1.00 11.27 C ANISOU 1662 CG2 VAL A 214 1361 1527 1393 92 182 -6 C ATOM 1663 N PRO A 215 8.269 -14.160 8.419 1.00 9.72 N ANISOU 1663 N PRO A 215 1094 1339 1259 -120 35 12 N ATOM 1664 CA PRO A 215 9.085 -13.878 7.234 1.00 8.97 C ANISOU 1664 CA PRO A 215 1079 1203 1127 -147 -68 23 C ATOM 1665 C PRO A 215 9.566 -12.423 7.199 1.00 9.57 C ANISOU 1665 C PRO A 215 1096 1167 1373 -31 44 28 C ATOM 1666 O PRO A 215 8.845 -11.469 7.514 1.00 9.22 O ANISOU 1666 O PRO A 215 1104 1054 1345 -63 146 -4 O ATOM 1667 CB PRO A 215 8.192 -14.216 6.040 1.00 9.49 C ANISOU 1667 CB PRO A 215 1076 1384 1145 -109 -58 -34 C ATOM 1668 CG PRO A 215 6.809 -14.056 6.597 1.00 9.66 C ANISOU 1668 CG PRO A 215 1116 1404 1151 28 75 73 C ATOM 1669 CD PRO A 215 6.887 -14.520 8.046 1.00 9.47 C ANISOU 1669 CD PRO A 215 1055 1417 1127 -2 -112 44 C ATOM 1670 N ARG A 216 10.856 -12.273 6.844 1.00 8.79 N ANISOU 1670 N ARG A 216 993 1089 1258 -77 -28 17 N ATOM 1671 CA ARG A 216 11.549 -10.993 7.019 1.00 8.92 C ANISOU 1671 CA ARG A 216 966 1189 1236 -91 -38 64 C ATOM 1672 C ARG A 216 11.335 -10.027 5.878 1.00 8.37 C ANISOU 1672 C ARG A 216 897 1090 1191 -64 41 -12 C ATOM 1673 O ARG A 216 11.797 -8.886 5.973 1.00 8.52 O ANISOU 1673 O ARG A 216 1004 927 1305 -48 126 40 O ATOM 1674 CB ARG A 216 13.073 -11.268 7.229 1.00 8.96 C ANISOU 1674 CB ARG A 216 982 1367 1054 -44 25 87 C ATOM 1675 CG ARG A 216 13.451 -10.859 8.665 1.00 9.75 C ANISOU 1675 CG ARG A 216 1252 1321 1134 -255 10 112 C ATOM 1676 CD ARG A 216 12.706 -11.760 9.680 1.00 9.92 C ANISOU 1676 CD ARG A 216 1283 1338 1148 -138 157 180 C ATOM 1677 NE ARG A 216 12.999 -11.288 11.047 1.00 11.43 N ANISOU 1677 NE ARG A 216 1430 1580 1332 -65 32 55 N ATOM 1678 CZ ARG A 216 12.432 -11.818 12.134 1.00 12.27 C ANISOU 1678 CZ ARG A 216 1547 1664 1451 -128 131 -24 C ATOM 1679 NH1 ARG A 216 12.831 -11.296 13.327 1.00 12.52 N ANISOU 1679 NH1 ARG A 216 1415 1792 1549 -59 -34 -92 N ATOM 1680 NH2 ARG A 216 11.522 -12.822 12.067 1.00 11.89 N ANISOU 1680 NH2 ARG A 216 1273 1697 1548 -103 134 -7 N ATOM 1681 N ASP A 217 10.548 -10.400 4.841 1.00 7.82 N ANISOU 1681 N ASP A 217 830 1160 981 19 95 5 N ATOM 1682 CA ASP A 217 10.205 -9.356 3.850 1.00 9.09 C ANISOU 1682 CA ASP A 217 1125 1162 1166 63 8 25 C ATOM 1683 C ASP A 217 9.282 -8.325 4.497 1.00 9.00 C ANISOU 1683 C ASP A 217 1138 1109 1174 17 35 37 C ATOM 1684 O ASP A 217 9.271 -7.191 4.018 1.00 9.17 O ANISOU 1684 O ASP A 217 991 1097 1395 60 121 25 O ATOM 1685 CB ASP A 217 9.545 -9.994 2.621 1.00 8.89 C ANISOU 1685 CB ASP A 217 1280 1053 1045 -42 -4 68 C ATOM 1686 CG ASP A 217 8.300 -10.799 2.964 1.00 11.05 C ANISOU 1686 CG ASP A 217 1304 1411 1483 -62 -35 32 C ATOM 1687 OD1 ASP A 217 7.152 -10.464 2.570 1.00 12.01 O ANISOU 1687 OD1 ASP A 217 1428 1621 1512 -97 -221 89 O ATOM 1688 OD2 ASP A 217 8.406 -11.830 3.678 1.00 12.37 O ANISOU 1688 OD2 ASP A 217 1486 1645 1569 -237 -46 249 O ATOM 1689 N ARG A 218 8.486 -8.684 5.535 1.00 8.80 N ANISOU 1689 N ARG A 218 981 1045 1317 -75 107 -15 N ATOM 1690 CA ARG A 218 7.671 -7.653 6.172 1.00 9.10 C ANISOU 1690 CA ARG A 218 1073 1153 1232 -134 62 -109 C ATOM 1691 C ARG A 218 8.547 -6.567 6.796 1.00 8.64 C ANISOU 1691 C ARG A 218 998 992 1294 -84 28 17 C ATOM 1692 O ARG A 218 8.247 -5.373 6.664 1.00 8.89 O ANISOU 1692 O ARG A 218 1161 961 1257 -28 -65 -45 O ATOM 1693 CB ARG A 218 6.855 -8.322 7.312 1.00 9.02 C ANISOU 1693 CB ARG A 218 1018 1123 1287 -113 23 98 C ATOM 1694 CG ARG A 218 5.886 -9.397 6.761 1.00 9.78 C ANISOU 1694 CG ARG A 218 1134 1332 1250 -158 10 -44 C ATOM 1695 CD ARG A 218 4.998 -9.931 7.930 1.00 11.04 C ANISOU 1695 CD ARG A 218 1253 1551 1391 -149 -19 115 C ATOM 1696 NE ARG A 218 4.004 -10.887 7.420 1.00 11.59 N ANISOU 1696 NE ARG A 218 1367 1467 1569 -158 21 -58 N ATOM 1697 CZ ARG A 218 2.930 -10.530 6.700 1.00 11.77 C ANISOU 1697 CZ ARG A 218 1419 1551 1501 -62 33 -15 C ATOM 1698 NH1 ARG A 218 2.644 -9.248 6.408 1.00 10.38 N ANISOU 1698 NH1 ARG A 218 1201 1533 1208 -9 72 -76 N ATOM 1699 NH2 ARG A 218 2.065 -11.474 6.257 1.00 11.66 N ANISOU 1699 NH2 ARG A 218 1355 1775 1300 -70 113 -165 N ATOM 1700 N HIS A 219 9.567 -7.005 7.554 1.00 8.36 N ANISOU 1700 N HIS A 219 1172 1061 943 -100 -78 -23 N ATOM 1701 CA HIS A 219 10.433 -6.002 8.216 1.00 8.13 C ANISOU 1701 CA HIS A 219 1047 946 1096 -151 -28 81 C ATOM 1702 C HIS A 219 11.190 -5.179 7.177 1.00 9.03 C ANISOU 1702 C HIS A 219 1275 1095 1059 -107 57 46 C ATOM 1703 O HIS A 219 11.414 -3.972 7.444 1.00 8.83 O ANISOU 1703 O HIS A 219 1142 963 1250 -52 45 157 O ATOM 1704 CB HIS A 219 11.425 -6.729 9.164 1.00 9.08 C ANISOU 1704 CB HIS A 219 1235 1190 1027 -36 -22 94 C ATOM 1705 CG HIS A 219 10.691 -7.746 9.997 1.00 10.50 C ANISOU 1705 CG HIS A 219 1234 1377 1379 -145 47 86 C ATOM 1706 ND1 HIS A 219 10.321 -8.978 9.505 1.00 11.72 N ANISOU 1706 ND1 HIS A 219 1467 1473 1514 -73 188 -69 N ATOM 1707 CD2 HIS A 219 10.265 -7.706 11.298 1.00 11.52 C ANISOU 1707 CD2 HIS A 219 1471 1482 1422 -171 65 23 C ATOM 1708 CE1 HIS A 219 9.693 -9.664 10.473 1.00 12.28 C ANISOU 1708 CE1 HIS A 219 1643 1517 1506 -103 138 -23 C ATOM 1709 NE2 HIS A 219 9.649 -8.918 11.569 1.00 11.38 N ANISOU 1709 NE2 HIS A 219 1700 1342 1283 -183 99 47 N ATOM 1710 N ALA A 220 11.600 -5.794 6.068 1.00 8.09 N ANISOU 1710 N ALA A 220 1010 994 1070 26 34 65 N ATOM 1711 CA ALA A 220 12.330 -5.029 5.034 1.00 8.73 C ANISOU 1711 CA ALA A 220 1145 1066 1108 55 148 39 C ATOM 1712 C ALA A 220 11.402 -4.006 4.382 1.00 8.30 C ANISOU 1712 C ALA A 220 933 1020 1199 -60 49 19 C ATOM 1713 O ALA A 220 11.801 -2.889 4.066 1.00 9.13 O ANISOU 1713 O ALA A 220 1142 995 1332 -65 149 6 O ATOM 1714 CB ALA A 220 12.827 -5.966 3.913 1.00 9.85 C ANISOU 1714 CB ALA A 220 1375 1222 1146 70 135 -71 C ATOM 1715 N PHE A 221 10.137 -4.354 4.146 1.00 8.09 N ANISOU 1715 N PHE A 221 778 1193 1101 25 -24 -14 N ATOM 1716 CA PHE A 221 9.177 -3.359 3.630 1.00 8.68 C ANISOU 1716 CA PHE A 221 913 1053 1331 30 -25 -33 C ATOM 1717 C PHE A 221 9.017 -2.183 4.584 1.00 9.31 C ANISOU 1717 C PHE A 221 1104 1213 1221 -11 -43 -20 C ATOM 1718 O PHE A 221 9.021 -1.002 4.155 1.00 9.16 O ANISOU 1718 O PHE A 221 1075 1131 1275 103 95 -14 O ATOM 1719 CB PHE A 221 7.823 -4.096 3.415 1.00 9.87 C ANISOU 1719 CB PHE A 221 978 1347 1425 -97 -151 -18 C ATOM 1720 CG PHE A 221 6.819 -3.130 2.831 1.00 12.92 C ANISOU 1720 CG PHE A 221 1331 1654 1925 11 -195 130 C ATOM 1721 CD1 PHE A 221 6.776 -3.010 1.448 1.00 15.32 C ANISOU 1721 CD1 PHE A 221 1835 2000 1986 -14 -241 84 C ATOM 1722 CD2 PHE A 221 6.003 -2.387 3.650 1.00 15.31 C ANISOU 1722 CD2 PHE A 221 1827 1920 2069 43 -93 -29 C ATOM 1723 CE1 PHE A 221 5.831 -2.113 0.884 1.00 17.54 C ANISOU 1723 CE1 PHE A 221 2058 2284 2324 229 -196 91 C ATOM 1724 CE2 PHE A 221 5.093 -1.486 3.091 1.00 17.03 C ANISOU 1724 CE2 PHE A 221 2152 2086 2234 123 -144 49 C ATOM 1725 CZ PHE A 221 5.043 -1.369 1.715 1.00 17.45 C ANISOU 1725 CZ PHE A 221 2192 2223 2215 138 -159 43 C ATOM 1726 N TYR A 222 8.882 -2.482 5.869 1.00 9.00 N ANISOU 1726 N TYR A 222 1052 1231 1137 32 105 -80 N ATOM 1727 CA TYR A 222 8.756 -1.400 6.891 1.00 8.34 C ANISOU 1727 CA TYR A 222 1134 1100 934 -75 59 29 C ATOM 1728 C TYR A 222 9.980 -0.513 6.877 1.00 7.73 C ANISOU 1728 C TYR A 222 1063 971 903 19 -41 29 C ATOM 1729 O TYR A 222 9.892 0.726 6.887 1.00 8.28 O ANISOU 1729 O TYR A 222 1086 904 1157 94 46 -61 O ATOM 1730 CB TYR A 222 8.604 -2.069 8.250 1.00 7.92 C ANISOU 1730 CB TYR A 222 1044 1030 937 -69 229 -77 C ATOM 1731 CG TYR A 222 8.396 -1.228 9.493 1.00 7.89 C ANISOU 1731 CG TYR A 222 1102 1049 847 -22 63 -25 C ATOM 1732 CD1 TYR A 222 7.102 -1.046 10.003 1.00 7.83 C ANISOU 1732 CD1 TYR A 222 1188 864 921 68 175 -28 C ATOM 1733 CD2 TYR A 222 9.499 -0.737 10.181 1.00 8.73 C ANISOU 1733 CD2 TYR A 222 1207 1010 1100 -34 -58 -55 C ATOM 1734 CE1 TYR A 222 6.955 -0.288 11.181 1.00 8.39 C ANISOU 1734 CE1 TYR A 222 1298 1040 850 36 66 -43 C ATOM 1735 CE2 TYR A 222 9.349 -0.042 11.388 1.00 9.00 C ANISOU 1735 CE2 TYR A 222 1176 1066 1178 -74 99 -46 C ATOM 1736 CZ TYR A 222 8.067 0.180 11.851 1.00 9.83 C ANISOU 1736 CZ TYR A 222 1243 1200 1290 20 76 -131 C ATOM 1737 OH TYR A 222 7.944 0.830 13.040 1.00 10.68 O ANISOU 1737 OH TYR A 222 1387 1345 1328 -102 73 -163 O ATOM 1738 N LEU A 223 11.180 -1.104 6.875 1.00 7.71 N ANISOU 1738 N LEU A 223 972 1052 903 37 128 38 N ATOM 1739 CA LEU A 223 12.396 -0.270 6.978 1.00 8.97 C ANISOU 1739 CA LEU A 223 1155 1206 1050 -90 -94 -8 C ATOM 1740 C LEU A 223 12.661 0.483 5.680 1.00 9.05 C ANISOU 1740 C LEU A 223 1153 1149 1137 -15 -58 17 C ATOM 1741 O LEU A 223 13.154 1.610 5.671 1.00 8.84 O ANISOU 1741 O LEU A 223 1377 971 1010 76 57 12 O ATOM 1742 CB LEU A 223 13.619 -1.151 7.369 1.00 11.01 C ANISOU 1742 CB LEU A 223 1519 1223 1441 190 25 -60 C ATOM 1743 CG LEU A 223 13.510 -1.672 8.828 1.00 13.51 C ANISOU 1743 CG LEU A 223 2055 1617 1463 95 -58 -81 C ATOM 1744 CD1 LEU A 223 14.397 -2.866 9.073 1.00 14.81 C ANISOU 1744 CD1 LEU A 223 2186 1739 1703 131 -58 5 C ATOM 1745 CD2 LEU A 223 13.744 -0.541 9.843 1.00 13.63 C ANISOU 1745 CD2 LEU A 223 1955 1680 1542 17 -149 -151 C ATOM 1746 N SER A 224 12.308 -0.103 4.526 1.00 9.07 N ANISOU 1746 N SER A 224 1105 1265 1075 67 -61 -118 N ATOM 1747 CA SER A 224 12.412 0.594 3.243 1.00 10.22 C ANISOU 1747 CA SER A 224 1257 1312 1314 69 -100 43 C ATOM 1748 C SER A 224 11.516 1.834 3.239 1.00 10.26 C ANISOU 1748 C SER A 224 1309 1207 1384 -8 74 0 C ATOM 1749 O SER A 224 11.903 2.917 2.783 1.00 10.04 O ANISOU 1749 O SER A 224 1090 1357 1367 -177 68 134 O ATOM 1750 CB SER A 224 11.932 -0.314 2.069 1.00 12.21 C ANISOU 1750 CB SER A 224 1789 1628 1222 98 -43 -163 C ATOM 1751 OG SER A 224 12.936 -1.324 1.904 1.00 16.96 O ANISOU 1751 OG SER A 224 1889 2324 2231 168 -94 -137 O ATOM 1752 N THR A 225 10.303 1.642 3.769 1.00 9.50 N ANISOU 1752 N THR A 225 1009 1240 1362 16 -57 -2 N ATOM 1753 CA THR A 225 9.383 2.747 3.937 1.00 10.04 C ANISOU 1753 CA THR A 225 1170 1220 1425 0 41 -41 C ATOM 1754 C THR A 225 9.946 3.876 4.795 1.00 8.78 C ANISOU 1754 C THR A 225 1105 1125 1106 46 72 59 C ATOM 1755 O THR A 225 9.873 5.054 4.425 1.00 7.69 O ANISOU 1755 O THR A 225 1097 917 907 -89 -101 0 O ATOM 1756 CB THR A 225 8.047 2.240 4.572 1.00 11.04 C ANISOU 1756 CB THR A 225 1093 1456 1644 68 33 -56 C ATOM 1757 OG1 THR A 225 7.487 1.351 3.591 1.00 12.41 O ANISOU 1757 OG1 THR A 225 1274 1774 1669 -143 178 -191 O ATOM 1758 CG2 THR A 225 7.108 3.424 4.758 1.00 10.90 C ANISOU 1758 CG2 THR A 225 1137 1407 1597 109 102 -27 C ATOM 1759 N LEU A 226 10.513 3.531 5.953 1.00 7.39 N ANISOU 1759 N LEU A 226 727 1089 994 97 98 -28 N ATOM 1760 CA LEU A 226 11.147 4.524 6.826 1.00 9.01 C ANISOU 1760 CA LEU A 226 1093 1030 1302 -74 42 74 C ATOM 1761 C LEU A 226 12.249 5.291 6.102 1.00 8.17 C ANISOU 1761 C LEU A 226 982 1038 1084 38 87 56 C ATOM 1762 O LEU A 226 12.380 6.494 6.350 1.00 8.55 O ANISOU 1762 O LEU A 226 1051 1130 1066 -21 48 4 O ATOM 1763 CB LEU A 226 11.708 3.844 8.079 1.00 9.30 C ANISOU 1763 CB LEU A 226 1193 1282 1060 130 -72 -119 C ATOM 1764 CG LEU A 226 10.787 3.670 9.273 1.00 12.97 C ANISOU 1764 CG LEU A 226 1521 1835 1571 60 90 311 C ATOM 1765 CD1 LEU A 226 9.303 3.622 9.003 1.00 11.05 C ANISOU 1765 CD1 LEU A 226 1535 1455 1210 -544 -33 88 C ATOM 1766 CD2 LEU A 226 11.266 2.933 10.487 1.00 10.95 C ANISOU 1766 CD2 LEU A 226 1595 1127 1439 -59 128 207 C ATOM 1767 N ALA A 227 13.048 4.590 5.302 1.00 7.94 N ANISOU 1767 N ALA A 227 813 1174 1028 117 -29 142 N ATOM 1768 CA ALA A 227 14.156 5.285 4.623 1.00 9.09 C ANISOU 1768 CA ALA A 227 1089 1160 1205 103 138 137 C ATOM 1769 C ALA A 227 13.638 6.298 3.594 1.00 8.90 C ANISOU 1769 C ALA A 227 1021 1046 1314 61 -40 94 C ATOM 1770 O ALA A 227 14.254 7.369 3.369 1.00 8.59 O ANISOU 1770 O ALA A 227 1041 981 1244 15 2 150 O ATOM 1771 CB ALA A 227 15.046 4.245 3.948 1.00 8.97 C ANISOU 1771 CB ALA A 227 1022 1021 1365 131 55 10 C ATOM 1772 N ILE A 228 12.528 5.967 2.943 1.00 8.33 N ANISOU 1772 N ILE A 228 949 1112 1104 78 -2 110 N ATOM 1773 CA ILE A 228 11.897 6.915 2.000 1.00 9.30 C ANISOU 1773 CA ILE A 228 1200 1016 1317 117 -58 90 C ATOM 1774 C ILE A 228 11.365 8.121 2.755 1.00 9.08 C ANISOU 1774 C ILE A 228 1212 1088 1151 -6 -35 35 C ATOM 1775 O ILE A 228 11.483 9.257 2.239 1.00 8.61 O ANISOU 1775 O ILE A 228 1206 1071 995 4 0 114 O ATOM 1776 CB ILE A 228 10.782 6.202 1.182 1.00 10.41 C ANISOU 1776 CB ILE A 228 1416 1287 1253 169 -204 7 C ATOM 1777 CG1 ILE A 228 11.489 5.160 0.269 1.00 11.55 C ANISOU 1777 CG1 ILE A 228 1545 1381 1462 75 -6 -64 C ATOM 1778 CG2 ILE A 228 9.974 7.200 0.342 1.00 10.47 C ANISOU 1778 CG2 ILE A 228 1304 1398 1276 179 -155 56 C ATOM 1779 CD1 ILE A 228 10.490 4.197 -0.396 1.00 13.39 C ANISOU 1779 CD1 ILE A 228 1686 1838 1563 41 -204 -145 C ATOM 1780 N VAL A 229 10.743 7.929 3.914 1.00 8.58 N ANISOU 1780 N VAL A 229 1047 1140 1072 -13 -9 -2 N ATOM 1781 CA VAL A 229 10.319 9.104 4.697 1.00 9.32 C ANISOU 1781 CA VAL A 229 1167 1120 1254 -63 5 -33 C ATOM 1782 C VAL A 229 11.511 10.009 5.021 1.00 9.47 C ANISOU 1782 C VAL A 229 1149 1193 1256 -36 -52 53 C ATOM 1783 O VAL A 229 11.466 11.242 4.851 1.00 8.98 O ANISOU 1783 O VAL A 229 1166 1125 1120 1 69 -10 O ATOM 1784 CB VAL A 229 9.590 8.688 5.983 1.00 9.94 C ANISOU 1784 CB VAL A 229 1307 1190 1282 -128 64 -118 C ATOM 1785 CG1 VAL A 229 9.039 9.940 6.708 1.00 10.56 C ANISOU 1785 CG1 VAL A 229 1302 1316 1393 73 85 -114 C ATOM 1786 CG2 VAL A 229 8.414 7.739 5.676 1.00 9.62 C ANISOU 1786 CG2 VAL A 229 1152 1402 1101 -141 -67 46 C ATOM 1787 N ALA A 230 12.601 9.386 5.500 1.00 9.24 N ANISOU 1787 N ALA A 230 1080 1048 1381 -44 -26 -23 N ATOM 1788 CA ALA A 230 13.815 10.112 5.796 1.00 8.87 C ANISOU 1788 CA ALA A 230 878 1102 1390 55 -9 89 C ATOM 1789 C ALA A 230 14.328 10.897 4.599 1.00 8.84 C ANISOU 1789 C ALA A 230 1130 1028 1199 53 -161 83 C ATOM 1790 O ALA A 230 14.851 12.011 4.801 1.00 9.31 O ANISOU 1790 O ALA A 230 1472 949 1118 105 -180 20 O ATOM 1791 CB ALA A 230 14.882 9.110 6.276 1.00 8.38 C ANISOU 1791 CB ALA A 230 1035 854 1293 10 -187 40 C ATOM 1792 N ALA A 231 14.356 10.330 3.392 1.00 8.21 N ANISOU 1792 N ALA A 231 972 1066 1083 14 56 146 N ATOM 1793 CA ALA A 231 14.908 11.032 2.226 1.00 8.83 C ANISOU 1793 CA ALA A 231 1428 904 1024 119 -9 90 C ATOM 1794 C ALA A 231 14.028 12.242 1.893 1.00 8.84 C ANISOU 1794 C ALA A 231 1171 948 1241 79 -57 51 C ATOM 1795 O ALA A 231 14.521 13.237 1.343 1.00 10.04 O ANISOU 1795 O ALA A 231 1459 1139 1217 -132 -92 134 O ATOM 1796 CB ALA A 231 14.958 10.078 1.020 1.00 8.36 C ANISOU 1796 CB ALA A 231 1320 933 921 14 -33 70 C ATOM 1797 N GLY A 232 12.739 12.120 2.131 1.00 8.45 N ANISOU 1797 N GLY A 232 1149 998 1064 27 -23 -51 N ATOM 1798 CA GLY A 232 11.851 13.311 1.979 1.00 9.35 C ANISOU 1798 CA GLY A 232 1185 982 1384 46 -94 -22 C ATOM 1799 C GLY A 232 12.254 14.423 2.950 1.00 10.01 C ANISOU 1799 C GLY A 232 1349 1172 1281 53 -32 4 C ATOM 1800 O GLY A 232 12.217 15.596 2.550 1.00 10.94 O ANISOU 1800 O GLY A 232 1481 1079 1597 76 -67 -11 O ATOM 1801 N ILE A 233 12.564 14.101 4.199 1.00 9.58 N ANISOU 1801 N ILE A 233 1107 1278 1253 119 -51 28 N ATOM 1802 CA ILE A 233 13.016 15.095 5.158 1.00 9.90 C ANISOU 1802 CA ILE A 233 1225 1207 1330 -15 46 41 C ATOM 1803 C ILE A 233 14.370 15.622 4.673 1.00 10.00 C ANISOU 1803 C ILE A 233 1242 1138 1419 -11 44 23 C ATOM 1804 O ILE A 233 14.597 16.840 4.767 1.00 9.80 O ANISOU 1804 O ILE A 233 1313 1065 1344 -8 34 151 O ATOM 1805 CB ILE A 233 13.116 14.521 6.581 1.00 10.52 C ANISOU 1805 CB ILE A 233 1345 1281 1372 -59 -33 40 C ATOM 1806 CG1 ILE A 233 11.685 14.160 7.043 1.00 11.64 C ANISOU 1806 CG1 ILE A 233 1392 1473 1556 -1 72 176 C ATOM 1807 CG2 ILE A 233 13.767 15.528 7.547 1.00 11.36 C ANISOU 1807 CG2 ILE A 233 1491 1359 1466 -81 -105 18 C ATOM 1808 CD1 ILE A 233 11.590 13.324 8.323 1.00 12.56 C ANISOU 1808 CD1 ILE A 233 1570 1639 1562 -47 59 189 C ATOM 1809 N GLU A 234 15.247 14.749 4.146 1.00 8.81 N ANISOU 1809 N GLU A 234 1114 1163 1069 6 -55 48 N ATOM 1810 CA GLU A 234 16.528 15.237 3.616 1.00 9.48 C ANISOU 1810 CA GLU A 234 1185 1226 1190 93 39 100 C ATOM 1811 C GLU A 234 16.326 16.268 2.509 1.00 9.30 C ANISOU 1811 C GLU A 234 1241 1094 1200 0 -10 46 C ATOM 1812 O GLU A 234 17.087 17.250 2.428 1.00 9.24 O ANISOU 1812 O GLU A 234 1152 1079 1279 25 -18 131 O ATOM 1813 CB GLU A 234 17.303 13.993 3.113 1.00 11.30 C ANISOU 1813 CB GLU A 234 1428 1305 1558 126 51 -61 C ATOM 1814 CG GLU A 234 18.697 14.268 2.544 1.00 13.46 C ANISOU 1814 CG GLU A 234 1557 1712 1846 -105 65 15 C ATOM 1815 CD GLU A 234 19.225 13.008 1.850 1.00 17.29 C ANISOU 1815 CD GLU A 234 2218 2105 2247 118 105 -151 C ATOM 1816 OE1 GLU A 234 18.583 11.901 1.885 1.00 17.92 O ANISOU 1816 OE1 GLU A 234 2327 2164 2317 28 128 -195 O ATOM 1817 OE2 GLU A 234 20.310 13.127 1.247 1.00 18.96 O ANISOU 1817 OE2 GLU A 234 2336 2503 2365 100 126 -81 O ATOM 1818 N ARG A 235 15.323 16.005 1.650 1.00 8.69 N ANISOU 1818 N ARG A 235 1069 1144 1088 151 11 167 N ATOM 1819 CA ARG A 235 15.050 16.964 0.553 1.00 9.94 C ANISOU 1819 CA ARG A 235 1382 1160 1236 88 -210 116 C ATOM 1820 C ARG A 235 14.726 18.347 1.118 1.00 9.89 C ANISOU 1820 C ARG A 235 1227 1187 1345 34 -44 73 C ATOM 1821 O ARG A 235 15.171 19.381 0.595 1.00 10.00 O ANISOU 1821 O ARG A 235 1246 1149 1405 -17 9 61 O ATOM 1822 CB ARG A 235 13.866 16.439 -0.298 1.00 10.50 C ANISOU 1822 CB ARG A 235 1343 1303 1343 -68 -164 95 C ATOM 1823 CG ARG A 235 13.646 17.402 -1.513 1.00 11.45 C ANISOU 1823 CG ARG A 235 1489 1483 1377 -31 -168 104 C ATOM 1824 CD ARG A 235 12.766 16.692 -2.549 1.00 13.52 C ANISOU 1824 CD ARG A 235 1530 1791 1817 -182 -194 -98 C ATOM 1825 NE ARG A 235 11.336 16.668 -2.175 1.00 15.94 N ANISOU 1825 NE ARG A 235 1782 2127 2148 -1 54 -108 N ATOM 1826 CZ ARG A 235 10.485 17.621 -2.566 1.00 17.61 C ANISOU 1826 CZ ARG A 235 2013 2374 2305 66 -7 58 C ATOM 1827 NH1 ARG A 235 10.949 18.659 -3.271 1.00 19.01 N ANISOU 1827 NH1 ARG A 235 2302 2283 2637 7 -20 101 N ATOM 1828 NH2 ARG A 235 9.186 17.543 -2.259 1.00 17.87 N ANISOU 1828 NH2 ARG A 235 1925 2467 2398 26 -66 82 N ATOM 1829 N ILE A 236 13.905 18.403 2.155 1.00 8.33 N ANISOU 1829 N ILE A 236 1009 1047 1108 -9 -182 34 N ATOM 1830 CA ILE A 236 13.543 19.650 2.813 1.00 8.85 C ANISOU 1830 CA ILE A 236 1056 1096 1211 -23 11 -13 C ATOM 1831 C ILE A 236 14.770 20.299 3.478 1.00 9.55 C ANISOU 1831 C ILE A 236 1204 1133 1292 -1 -118 40 C ATOM 1832 O ILE A 236 15.022 21.512 3.345 1.00 10.23 O ANISOU 1832 O ILE A 236 1258 1139 1488 -27 -92 76 O ATOM 1833 CB ILE A 236 12.444 19.428 3.882 1.00 9.39 C ANISOU 1833 CB ILE A 236 1087 1211 1268 -71 6 -46 C ATOM 1834 CG1 ILE A 236 11.177 18.845 3.223 1.00 9.51 C ANISOU 1834 CG1 ILE A 236 1027 1277 1307 -150 34 56 C ATOM 1835 CG2 ILE A 236 12.177 20.753 4.615 1.00 9.40 C ANISOU 1835 CG2 ILE A 236 1118 1136 1319 -39 36 -46 C ATOM 1836 CD1 ILE A 236 10.106 18.355 4.225 1.00 9.83 C ANISOU 1836 CD1 ILE A 236 1182 1308 1243 -43 46 239 C ATOM 1837 N ALA A 237 15.541 19.497 4.217 1.00 9.17 N ANISOU 1837 N ALA A 237 1135 1158 1193 47 -122 52 N ATOM 1838 CA ALA A 237 16.747 20.006 4.863 1.00 9.64 C ANISOU 1838 CA ALA A 237 1140 1158 1366 12 -87 137 C ATOM 1839 C ALA A 237 17.730 20.565 3.834 1.00 10.11 C ANISOU 1839 C ALA A 237 1366 1125 1352 -5 -21 129 C ATOM 1840 O ALA A 237 18.295 21.598 4.142 1.00 8.87 O ANISOU 1840 O ALA A 237 1182 1095 1091 -51 -79 161 O ATOM 1841 CB ALA A 237 17.443 18.901 5.672 1.00 8.60 C ANISOU 1841 CB ALA A 237 1047 1123 1098 11 -49 83 C ATOM 1842 N VAL A 238 17.929 19.926 2.661 1.00 10.08 N ANISOU 1842 N VAL A 238 1347 1121 1362 30 -22 150 N ATOM 1843 CA VAL A 238 18.881 20.433 1.681 1.00 10.63 C ANISOU 1843 CA VAL A 238 1388 1263 1389 107 28 147 C ATOM 1844 C VAL A 238 18.375 21.765 1.115 1.00 10.95 C ANISOU 1844 C VAL A 238 1267 1235 1657 23 -69 166 C ATOM 1845 O VAL A 238 19.127 22.725 0.939 1.00 10.14 O ANISOU 1845 O VAL A 238 1144 1175 1535 65 -132 109 O ATOM 1846 CB VAL A 238 19.100 19.387 0.572 1.00 11.57 C ANISOU 1846 CB VAL A 238 1639 1285 1474 115 30 126 C ATOM 1847 CG1 VAL A 238 19.848 19.972 -0.633 1.00 12.76 C ANISOU 1847 CG1 VAL A 238 1754 1597 1499 -98 52 101 C ATOM 1848 CG2 VAL A 238 20.000 18.275 1.185 1.00 11.64 C ANISOU 1848 CG2 VAL A 238 1424 1357 1640 115 -28 130 C ATOM 1849 N GLU A 239 17.047 21.855 0.944 1.00 10.13 N ANISOU 1849 N GLU A 239 1247 1186 1414 105 -152 -1 N ATOM 1850 CA GLU A 239 16.477 23.129 0.467 1.00 10.39 C ANISOU 1850 CA GLU A 239 1362 1147 1440 89 -82 11 C ATOM 1851 C GLU A 239 16.780 24.225 1.487 1.00 10.19 C ANISOU 1851 C GLU A 239 1273 1222 1377 51 -93 12 C ATOM 1852 O GLU A 239 17.204 25.310 1.074 1.00 10.95 O ANISOU 1852 O GLU A 239 1341 1386 1433 1 10 97 O ATOM 1853 CB GLU A 239 14.953 23.008 0.295 1.00 11.33 C ANISOU 1853 CB GLU A 239 1355 1315 1636 50 -88 32 C ATOM 1854 CG GLU A 239 14.345 24.351 -0.200 1.00 14.08 C ANISOU 1854 CG GLU A 239 1746 1501 2103 137 -55 86 C ATOM 1855 CD GLU A 239 14.525 24.553 -1.691 1.00 17.21 C ANISOU 1855 CD GLU A 239 2127 2202 2209 92 1 33 C ATOM 1856 OE1 GLU A 239 14.535 25.716 -2.182 1.00 19.60 O ANISOU 1856 OE1 GLU A 239 2425 2365 2659 41 126 251 O ATOM 1857 OE2 GLU A 239 14.670 23.511 -2.357 1.00 19.37 O ANISOU 1857 OE2 GLU A 239 2612 2481 2267 26 -113 -216 O ATOM 1858 N ILE A 240 16.545 23.988 2.769 1.00 9.50 N ANISOU 1858 N ILE A 240 1098 1208 1304 112 -27 -84 N ATOM 1859 CA ILE A 240 16.779 25.060 3.778 1.00 10.35 C ANISOU 1859 CA ILE A 240 1352 1234 1349 42 -24 -26 C ATOM 1860 C ILE A 240 18.249 25.413 3.838 1.00 10.81 C ANISOU 1860 C ILE A 240 1385 1328 1394 40 31 4 C ATOM 1861 O ILE A 240 18.636 26.597 3.939 1.00 12.08 O ANISOU 1861 O ILE A 240 1661 1406 1522 10 75 -131 O ATOM 1862 CB ILE A 240 16.230 24.593 5.139 1.00 11.27 C ANISOU 1862 CB ILE A 240 1494 1389 1401 43 89 -83 C ATOM 1863 CG1 ILE A 240 14.687 24.554 4.957 1.00 12.84 C ANISOU 1863 CG1 ILE A 240 1527 1583 1767 -86 84 -28 C ATOM 1864 CG2 ILE A 240 16.609 25.542 6.291 1.00 12.65 C ANISOU 1864 CG2 ILE A 240 1628 1674 1506 -123 -1 -75 C ATOM 1865 CD1 ILE A 240 13.970 23.948 6.155 1.00 15.66 C ANISOU 1865 CD1 ILE A 240 2127 2112 1712 -37 138 35 C ATOM 1866 N ARG A 241 19.147 24.421 3.709 1.00 10.39 N ANISOU 1866 N ARG A 241 1307 1450 1192 95 32 26 N ATOM 1867 CA ARG A 241 20.581 24.734 3.656 1.00 9.85 C ANISOU 1867 CA ARG A 241 1294 1202 1247 25 25 115 C ATOM 1868 C ARG A 241 20.930 25.669 2.509 1.00 10.21 C ANISOU 1868 C ARG A 241 1371 1201 1308 -27 10 53 C ATOM 1869 O ARG A 241 21.730 26.593 2.677 1.00 11.37 O ANISOU 1869 O ARG A 241 1461 1271 1588 -121 55 1 O ATOM 1870 CB ARG A 241 21.342 23.398 3.452 1.00 9.96 C ANISOU 1870 CB ARG A 241 1287 1250 1248 69 -21 44 C ATOM 1871 CG ARG A 241 21.370 22.631 4.793 1.00 10.30 C ANISOU 1871 CG ARG A 241 1420 1163 1330 100 -43 97 C ATOM 1872 CD ARG A 241 21.851 21.194 4.554 1.00 11.25 C ANISOU 1872 CD ARG A 241 1423 1287 1563 107 20 18 C ATOM 1873 NE ARG A 241 23.247 21.185 4.107 1.00 12.03 N ANISOU 1873 NE ARG A 241 1371 1558 1641 115 -14 103 N ATOM 1874 CZ ARG A 241 23.872 20.125 3.629 1.00 13.06 C ANISOU 1874 CZ ARG A 241 1478 1573 1910 -14 49 8 C ATOM 1875 NH1 ARG A 241 25.154 20.322 3.270 1.00 12.84 N ANISOU 1875 NH1 ARG A 241 1449 1545 1883 28 176 156 N ATOM 1876 NH2 ARG A 241 23.287 18.906 3.540 1.00 13.35 N ANISOU 1876 NH2 ARG A 241 1800 1368 1903 70 -33 110 N ATOM 1877 N HIS A 242 20.404 25.397 1.317 1.00 9.70 N ANISOU 1877 N HIS A 242 1199 1254 1232 36 -1 70 N ATOM 1878 CA HIS A 242 20.671 26.298 0.198 1.00 9.58 C ANISOU 1878 CA HIS A 242 1254 1172 1215 71 44 31 C ATOM 1879 C HIS A 242 20.100 27.702 0.468 1.00 10.16 C ANISOU 1879 C HIS A 242 1271 1159 1430 23 -34 32 C ATOM 1880 O HIS A 242 20.740 28.703 0.136 1.00 10.42 O ANISOU 1880 O HIS A 242 1375 1003 1584 9 -79 121 O ATOM 1881 CB HIS A 242 19.963 25.793 -1.064 1.00 9.78 C ANISOU 1881 CB HIS A 242 1104 1311 1304 21 91 -154 C ATOM 1882 CG HIS A 242 20.569 24.584 -1.707 1.00 10.17 C ANISOU 1882 CG HIS A 242 1123 1307 1435 59 90 -91 C ATOM 1883 ND1 HIS A 242 21.896 24.606 -2.144 1.00 10.98 N ANISOU 1883 ND1 HIS A 242 1146 1397 1630 -118 90 -10 N ATOM 1884 CD2 HIS A 242 20.080 23.381 -2.043 1.00 9.83 C ANISOU 1884 CD2 HIS A 242 1133 1198 1402 73 23 102 C ATOM 1885 CE1 HIS A 242 22.197 23.463 -2.712 1.00 10.96 C ANISOU 1885 CE1 HIS A 242 1221 1400 1543 -22 54 -65 C ATOM 1886 NE2 HIS A 242 21.098 22.691 -2.667 1.00 10.47 N ANISOU 1886 NE2 HIS A 242 1089 1495 1394 10 91 -1 N ATOM 1887 N LEU A 243 18.871 27.722 1.001 1.00 9.35 N ANISOU 1887 N LEU A 243 1229 1132 1190 37 -1 -65 N ATOM 1888 CA LEU A 243 18.216 29.055 1.161 1.00 10.02 C ANISOU 1888 CA LEU A 243 1231 1157 1418 50 -114 -26 C ATOM 1889 C LEU A 243 18.809 29.872 2.291 1.00 10.95 C ANISOU 1889 C LEU A 243 1383 1325 1454 12 -74 -42 C ATOM 1890 O LEU A 243 18.567 31.097 2.367 1.00 11.72 O ANISOU 1890 O LEU A 243 1523 1297 1631 -35 -210 -70 O ATOM 1891 CB LEU A 243 16.702 28.855 1.419 1.00 10.59 C ANISOU 1891 CB LEU A 243 1364 1332 1329 -89 18 -21 C ATOM 1892 CG LEU A 243 15.961 28.210 0.209 1.00 10.39 C ANISOU 1892 CG LEU A 243 1258 1329 1363 -133 -81 69 C ATOM 1893 CD1 LEU A 243 14.451 28.126 0.529 1.00 11.22 C ANISOU 1893 CD1 LEU A 243 1311 1354 1598 -48 35 8 C ATOM 1894 CD2 LEU A 243 16.181 29.002 -1.055 1.00 12.00 C ANISOU 1894 CD2 LEU A 243 1772 1449 1338 -117 -31 18 C ATOM 1895 N GLN A 244 19.499 29.204 3.227 1.00 10.06 N ANISOU 1895 N GLN A 244 1056 1308 1459 10 57 21 N ATOM 1896 CA GLN A 244 20.158 29.917 4.317 1.00 11.80 C ANISOU 1896 CA GLN A 244 1421 1542 1521 -20 -71 -32 C ATOM 1897 C GLN A 244 21.556 30.392 3.906 1.00 12.72 C ANISOU 1897 C GLN A 244 1559 1641 1632 -83 41 11 C ATOM 1898 O GLN A 244 22.207 31.115 4.701 1.00 12.56 O ANISOU 1898 O GLN A 244 1696 1469 1608 -123 128 -106 O ATOM 1899 CB GLN A 244 20.186 29.048 5.574 1.00 12.20 C ANISOU 1899 CB GLN A 244 1621 1467 1546 -98 55 -42 C ATOM 1900 CG GLN A 244 20.631 29.782 6.829 1.00 14.06 C ANISOU 1900 CG GLN A 244 1945 1826 1572 -45 -61 -35 C ATOM 1901 CD GLN A 244 20.189 29.137 8.127 1.00 14.30 C ANISOU 1901 CD GLN A 244 1940 1795 1699 11 67 -10 C ATOM 1902 OE1 GLN A 244 19.248 28.377 8.169 1.00 15.08 O ANISOU 1902 OE1 GLN A 244 2064 1927 1737 -68 -31 -96 O ATOM 1903 NE2 GLN A 244 20.900 29.432 9.220 1.00 15.24 N ANISOU 1903 NE2 GLN A 244 2083 1984 1725 -6 19 13 N ATOM 1904 N ARG A 245 22.057 29.984 2.720 1.00 11.96 N ANISOU 1904 N ARG A 245 1446 1511 1588 -41 22 -22 N ATOM 1905 CA ARG A 245 23.466 30.369 2.412 1.00 13.13 C ANISOU 1905 CA ARG A 245 1518 1497 1972 -55 73 -32 C ATOM 1906 C ARG A 245 23.634 31.880 2.321 1.00 12.55 C ANISOU 1906 C ARG A 245 1373 1508 1886 -94 -56 74 C ATOM 1907 O ARG A 245 22.658 32.599 2.023 1.00 12.53 O ANISOU 1907 O ARG A 245 1371 1425 1966 -43 40 23 O ATOM 1908 CB ARG A 245 23.934 29.645 1.144 1.00 14.43 C ANISOU 1908 CB ARG A 245 1674 2048 1759 -117 71 -35 C ATOM 1909 CG ARG A 245 23.438 30.127 -0.204 1.00 15.37 C ANISOU 1909 CG ARG A 245 1929 2019 1891 93 -16 -78 C ATOM 1910 CD ARG A 245 24.039 29.207 -1.344 1.00 15.84 C ANISOU 1910 CD ARG A 245 1718 2237 2065 -28 97 -237 C ATOM 1911 NE ARG A 245 25.485 29.515 -1.402 1.00 14.64 N ANISOU 1911 NE ARG A 245 1654 2073 1837 16 43 -94 N ATOM 1912 CZ ARG A 245 26.469 28.646 -1.536 1.00 14.61 C ANISOU 1912 CZ ARG A 245 1705 1790 2057 -41 5 -16 C ATOM 1913 NH1 ARG A 245 26.254 27.333 -1.649 1.00 13.34 N ANISOU 1913 NH1 ARG A 245 1489 1832 1746 -214 -196 -142 N ATOM 1914 NH2 ARG A 245 27.736 29.061 -1.518 1.00 14.36 N ANISOU 1914 NH2 ARG A 245 1616 1845 1996 -27 -22 53 N ATOM 1915 N THR A 246 24.852 32.409 2.522 1.00 10.68 N ANISOU 1915 N THR A 246 1281 1077 1701 -32 -101 106 N ATOM 1916 CA THR A 246 25.011 33.870 2.616 1.00 11.25 C ANISOU 1916 CA THR A 246 1335 1195 1746 -118 -104 39 C ATOM 1917 C THR A 246 24.546 34.612 1.369 1.00 11.72 C ANISOU 1917 C THR A 246 1383 1331 1740 -51 -17 70 C ATOM 1918 O THR A 246 24.131 35.794 1.464 1.00 13.33 O ANISOU 1918 O THR A 246 1480 1463 2121 67 7 50 O ATOM 1919 CB THR A 246 26.508 34.172 2.858 1.00 11.20 C ANISOU 1919 CB THR A 246 1364 1174 1718 -161 -94 16 C ATOM 1920 OG1 THR A 246 26.876 33.507 4.082 1.00 10.23 O ANISOU 1920 OG1 THR A 246 1329 1011 1547 -190 -52 -149 O ATOM 1921 CG2 THR A 246 26.782 35.675 3.011 1.00 12.21 C ANISOU 1921 CG2 THR A 246 1659 1151 1827 -110 -25 18 C ATOM 1922 N GLU A 247 24.672 34.021 0.181 1.00 11.62 N ANISOU 1922 N GLU A 247 1365 1382 1668 -127 -56 68 N ATOM 1923 CA GLU A 247 24.335 34.687 -1.063 1.00 11.55 C ANISOU 1923 CA GLU A 247 1284 1529 1573 -21 33 54 C ATOM 1924 C GLU A 247 22.836 34.673 -1.307 1.00 11.19 C ANISOU 1924 C GLU A 247 1314 1414 1523 -55 -12 47 C ATOM 1925 O GLU A 247 22.416 35.345 -2.271 1.00 11.95 O ANISOU 1925 O GLU A 247 1391 1415 1734 -70 -41 215 O ATOM 1926 CB GLU A 247 25.069 34.103 -2.290 1.00 11.92 C ANISOU 1926 CB GLU A 247 1385 1534 1612 -34 -35 -107 C ATOM 1927 CG GLU A 247 26.598 34.166 -2.203 1.00 12.95 C ANISOU 1927 CG GLU A 247 1415 1807 1699 6 50 74 C ATOM 1928 CD GLU A 247 27.204 32.996 -1.452 1.00 14.43 C ANISOU 1928 CD GLU A 247 1681 1754 2048 19 72 96 C ATOM 1929 OE1 GLU A 247 28.456 32.907 -1.410 1.00 13.92 O ANISOU 1929 OE1 GLU A 247 1616 1726 1948 -152 66 124 O ATOM 1930 OE2 GLU A 247 26.537 32.104 -0.854 1.00 14.10 O ANISOU 1930 OE2 GLU A 247 1468 1748 2142 -128 -4 71 O ATOM 1931 N VAL A 248 22.073 33.896 -0.514 1.00 10.32 N ANISOU 1931 N VAL A 248 1247 1165 1511 24 -50 30 N ATOM 1932 CA VAL A 248 20.644 33.712 -0.814 1.00 10.52 C ANISOU 1932 CA VAL A 248 1196 1237 1563 6 -1 -17 C ATOM 1933 C VAL A 248 19.825 34.347 0.295 1.00 10.95 C ANISOU 1933 C VAL A 248 1289 1356 1514 -25 -9 -48 C ATOM 1934 O VAL A 248 19.038 35.303 0.082 1.00 12.36 O ANISOU 1934 O VAL A 248 1541 1518 1637 104 25 68 O ATOM 1935 CB VAL A 248 20.293 32.224 -1.026 1.00 10.66 C ANISOU 1935 CB VAL A 248 1212 1365 1474 -29 115 -183 C ATOM 1936 CG1 VAL A 248 18.782 32.037 -1.227 1.00 10.23 C ANISOU 1936 CG1 VAL A 248 1226 1288 1373 -55 -17 -32 C ATOM 1937 CG2 VAL A 248 21.092 31.625 -2.226 1.00 9.41 C ANISOU 1937 CG2 VAL A 248 1243 1022 1312 42 41 -113 C ATOM 1938 N LEU A 249 20.044 33.957 1.560 1.00 11.42 N ANISOU 1938 N LEU A 249 1316 1339 1683 -68 -90 43 N ATOM 1939 CA LEU A 249 19.410 34.539 2.722 1.00 13.20 C ANISOU 1939 CA LEU A 249 1539 1651 1824 -76 -30 -94 C ATOM 1940 C LEU A 249 17.888 34.598 2.662 1.00 13.21 C ANISOU 1940 C LEU A 249 1549 1529 1940 -26 -106 -123 C ATOM 1941 O LEU A 249 17.332 35.620 3.095 1.00 13.52 O ANISOU 1941 O LEU A 249 1572 1589 1977 -126 -147 -323 O ATOM 1942 CB LEU A 249 19.939 35.977 3.001 1.00 15.77 C ANISOU 1942 CB LEU A 249 1955 1783 2256 -168 -86 -92 C ATOM 1943 CG LEU A 249 21.468 35.998 3.237 1.00 17.29 C ANISOU 1943 CG LEU A 249 2019 2096 2453 -77 -47 2 C ATOM 1944 CD1 LEU A 249 21.937 37.457 3.410 1.00 18.73 C ANISOU 1944 CD1 LEU A 249 2378 2240 2498 -169 8 -200 C ATOM 1945 CD2 LEU A 249 21.854 35.181 4.444 1.00 18.21 C ANISOU 1945 CD2 LEU A 249 2278 2253 2389 -20 -82 -37 C ATOM 1946 N GLU A 250 17.206 33.552 2.196 1.00 11.79 N ANISOU 1946 N GLU A 250 1455 1306 1718 27 -61 -74 N ATOM 1947 CA GLU A 250 15.739 33.569 2.100 1.00 11.84 C ANISOU 1947 CA GLU A 250 1504 1514 1482 34 -78 15 C ATOM 1948 C GLU A 250 15.055 32.945 3.296 1.00 12.79 C ANISOU 1948 C GLU A 250 1624 1559 1678 2 -10 34 C ATOM 1949 O GLU A 250 13.896 33.267 3.603 1.00 13.58 O ANISOU 1949 O GLU A 250 1556 1635 1968 41 -121 118 O ATOM 1950 CB GLU A 250 15.253 32.842 0.801 1.00 11.21 C ANISOU 1950 CB GLU A 250 1421 1329 1510 19 20 -40 C ATOM 1951 CG GLU A 250 15.565 33.754 -0.403 1.00 11.27 C ANISOU 1951 CG GLU A 250 1421 1379 1483 129 -37 71 C ATOM 1952 CD GLU A 250 15.320 33.190 -1.782 1.00 13.00 C ANISOU 1952 CD GLU A 250 1661 1662 1615 98 46 -16 C ATOM 1953 OE1 GLU A 250 14.819 32.046 -1.893 1.00 14.60 O ANISOU 1953 OE1 GLU A 250 1852 1709 1988 63 20 -1 O ATOM 1954 OE2 GLU A 250 15.618 33.870 -2.812 1.00 13.86 O ANISOU 1954 OE2 GLU A 250 1874 1503 1887 318 77 219 O ATOM 1955 N VAL A 251 15.735 32.031 3.998 1.00 12.36 N ANISOU 1955 N VAL A 251 1551 1435 1712 -29 -98 0 N ATOM 1956 CA VAL A 251 15.140 31.427 5.205 1.00 14.72 C ANISOU 1956 CA VAL A 251 1860 1976 1757 -38 -6 57 C ATOM 1957 C VAL A 251 16.255 31.290 6.240 1.00 15.40 C ANISOU 1957 C VAL A 251 1812 2091 1947 -3 1 87 C ATOM 1958 O VAL A 251 17.439 31.213 5.873 1.00 16.12 O ANISOU 1958 O VAL A 251 1711 2323 2091 -50 -5 252 O ATOM 1959 CB VAL A 251 14.617 30.013 4.849 1.00 17.26 C ANISOU 1959 CB VAL A 251 2239 2179 2141 -263 -62 9 C ATOM 1960 CG1 VAL A 251 14.202 29.214 6.069 1.00 20.24 C ANISOU 1960 CG1 VAL A 251 2728 2671 2290 -205 24 98 C ATOM 1961 CG2 VAL A 251 13.407 30.030 3.898 1.00 17.05 C ANISOU 1961 CG2 VAL A 251 2157 2117 2206 -46 -20 -7 C ATOM 1962 N GLU A 252 15.922 31.145 7.503 1.00 15.60 N ANISOU 1962 N GLU A 252 1893 2110 1923 41 45 -34 N ATOM 1963 CA GLU A 252 16.901 30.835 8.536 1.00 17.21 C ANISOU 1963 CA GLU A 252 2194 2197 2150 67 -84 148 C ATOM 1964 C GLU A 252 16.278 29.851 9.520 1.00 16.47 C ANISOU 1964 C GLU A 252 2093 1982 2182 95 -49 84 C ATOM 1965 O GLU A 252 15.186 30.128 10.064 1.00 15.72 O ANISOU 1965 O GLU A 252 2078 1924 1970 90 -117 204 O ATOM 1966 CB GLU A 252 17.260 32.163 9.228 1.00 21.01 C ANISOU 1966 CB GLU A 252 2818 2481 2683 -56 69 -150 C ATOM 1967 CG GLU A 252 18.291 32.079 10.345 1.00 26.00 C ANISOU 1967 CG GLU A 252 3326 3401 3154 13 -179 -23 C ATOM 1968 CD GLU A 252 18.377 33.512 10.926 1.00 30.27 C ANISOU 1968 CD GLU A 252 4075 3597 3830 -111 -66 -188 C ATOM 1969 OE1 GLU A 252 17.917 33.716 12.067 1.00 32.14 O ANISOU 1969 OE1 GLU A 252 4315 3992 3906 -127 67 -155 O ATOM 1970 OE2 GLU A 252 18.865 34.383 10.163 1.00 31.98 O ANISOU 1970 OE2 GLU A 252 4299 3933 3921 -156 -37 -38 O ATOM 1971 N GLU A 253 16.970 28.710 9.755 1.00 15.74 N ANISOU 1971 N GLU A 253 2005 1879 2095 43 -46 107 N ATOM 1972 CA GLU A 253 16.376 27.745 10.678 1.00 15.49 C ANISOU 1972 CA GLU A 253 1972 1832 2081 63 62 78 C ATOM 1973 C GLU A 253 16.397 28.326 12.074 1.00 16.10 C ANISOU 1973 C GLU A 253 2018 1926 2173 -23 59 -28 C ATOM 1974 O GLU A 253 17.117 29.293 12.372 1.00 15.86 O ANISOU 1974 O GLU A 253 1775 2119 2134 -64 168 46 O ATOM 1975 CB GLU A 253 17.130 26.389 10.605 1.00 16.34 C ANISOU 1975 CB GLU A 253 2027 1890 2291 57 51 97 C ATOM 1976 CG GLU A 253 18.525 26.498 11.114 1.00 16.92 C ANISOU 1976 CG GLU A 253 2062 2091 2275 129 18 17 C ATOM 1977 CD GLU A 253 19.242 25.146 11.199 1.00 17.13 C ANISOU 1977 CD GLU A 253 2150 1951 2408 34 68 31 C ATOM 1978 OE1 GLU A 253 20.019 24.996 12.164 1.00 18.25 O ANISOU 1978 OE1 GLU A 253 2477 2169 2289 106 85 -37 O ATOM 1979 OE2 GLU A 253 19.077 24.278 10.315 1.00 17.17 O ANISOU 1979 OE2 GLU A 253 2053 2061 2409 82 61 -4 O ATOM 1980 N PRO A 254 15.512 27.877 12.964 1.00 16.67 N ANISOU 1980 N PRO A 254 2102 2020 2212 11 97 82 N ATOM 1981 CA PRO A 254 15.478 28.380 14.326 1.00 20.22 C ANISOU 1981 CA PRO A 254 2655 2617 2409 -99 103 -87 C ATOM 1982 C PRO A 254 16.782 28.082 15.059 1.00 23.40 C ANISOU 1982 C PRO A 254 2881 3015 2993 141 -10 57 C ATOM 1983 O PRO A 254 17.504 27.148 14.709 1.00 20.87 O ANISOU 1983 O PRO A 254 2918 2637 2374 -21 -35 -12 O ATOM 1984 CB PRO A 254 14.324 27.627 14.990 1.00 20.39 C ANISOU 1984 CB PRO A 254 2582 2726 2440 -128 98 -159 C ATOM 1985 CG PRO A 254 13.799 26.669 14.009 1.00 19.01 C ANISOU 1985 CG PRO A 254 2359 2466 2398 -163 201 -76 C ATOM 1986 CD PRO A 254 14.622 26.716 12.743 1.00 17.09 C ANISOU 1986 CD PRO A 254 2051 2195 2247 -62 97 19 C ATOM 1987 N PHE A 255 17.138 28.902 16.051 1.00 28.26 N ANISOU 1987 N PHE A 255 3903 3519 3317 -73 102 -252 N ATOM 1988 CA PHE A 255 18.392 28.629 16.760 1.00 35.00 C ANISOU 1988 CA PHE A 255 4307 4575 4418 126 -190 -44 C ATOM 1989 C PHE A 255 18.322 28.955 18.250 1.00 38.41 C ANISOU 1989 C PHE A 255 5007 5024 4562 41 44 -114 C ATOM 1990 O PHE A 255 17.326 29.462 18.730 1.00 38.24 O ANISOU 1990 O PHE A 255 4947 5053 4528 24 7 -120 O ATOM 1991 CB PHE A 255 19.546 29.452 16.177 1.00 37.38 C ANISOU 1991 CB PHE A 255 4673 4885 4645 -49 -12 5 C ATOM 1992 CG PHE A 255 19.278 30.928 16.268 1.00 39.83 C ANISOU 1992 CG PHE A 255 5057 4970 5106 19 -12 -45 C ATOM 1993 CD1 PHE A 255 18.657 31.574 15.215 1.00 40.71 C ANISOU 1993 CD1 PHE A 255 5190 5196 5083 -9 -12 -1 C ATOM 1994 CD2 PHE A 255 19.634 31.663 17.390 1.00 40.82 C ANISOU 1994 CD2 PHE A 255 5208 5213 5089 10 -19 -58 C ATOM 1995 CE1 PHE A 255 18.384 32.934 15.262 1.00 41.71 C ANISOU 1995 CE1 PHE A 255 5367 5221 5261 -28 20 -7 C ATOM 1996 CE2 PHE A 255 19.383 33.020 17.445 1.00 41.41 C ANISOU 1996 CE2 PHE A 255 5284 5220 5231 -35 13 -21 C ATOM 1997 CZ PHE A 255 18.754 33.655 16.386 1.00 41.81 C ANISOU 1997 CZ PHE A 255 5366 5250 5271 -56 -13 -1 C ATOM 1998 N ARG A 256 19.481 28.794 18.871 1.00 41.64 N ANISOU 1998 N ARG A 256 5169 5435 5219 34 -123 -35 N ATOM 1999 CA ARG A 256 19.771 28.987 20.274 1.00 43.46 C ANISOU 1999 CA ARG A 256 5558 5649 5307 -9 -55 -72 C ATOM 2000 C ARG A 256 18.735 29.764 21.066 1.00 44.09 C ANISOU 2000 C ARG A 256 5656 5562 5533 3 18 -56 C ATOM 2001 O ARG A 256 17.856 29.148 21.675 1.00 46.83 O ANISOU 2001 O ARG A 256 5887 5999 5907 -182 89 84 O ATOM 2002 CB ARG A 256 21.131 29.696 20.425 1.00 44.39 C ANISOU 2002 CB ARG A 256 5619 5709 5536 -60 -73 -45 C ATOM 2003 N LYS A 257 18.852 31.078 21.085 1.00 43.22 N ANISOU 2003 N LYS A 257 5488 5513 5420 -11 40 -102 N ATOM 2004 CA LYS A 257 17.967 31.984 21.793 1.00 42.18 C ANISOU 2004 CA LYS A 257 5214 5488 5325 -125 13 -94 C ATOM 2005 C LYS A 257 18.801 32.814 22.785 1.00 42.44 C ANISOU 2005 C LYS A 257 5223 5501 5403 -153 1 -131 C ATOM 2006 O LYS A 257 19.966 33.100 22.370 1.00 43.71 O ANISOU 2006 O LYS A 257 5286 5754 5568 -126 101 -83 O ATOM 2007 CB LYS A 257 16.826 31.323 22.542 1.00 42.37 C ANISOU 2007 CB LYS A 257 5276 5455 5369 -115 53 -14 C ATOM 2008 N SER A 263 23.173 39.022 21.973 1.00 49.40 N ANISOU 2008 N SER A 263 6289 6316 6163 -34 3 -88 N ATOM 2009 CA SER A 263 22.422 38.307 20.899 1.00 48.41 C ANISOU 2009 CA SER A 263 6119 6200 6074 -16 103 -96 C ATOM 2010 C SER A 263 23.380 37.723 19.863 1.00 46.49 C ANISOU 2010 C SER A 263 5921 5926 5818 -116 -40 -115 C ATOM 2011 O SER A 263 24.572 38.058 19.835 1.00 46.78 O ANISOU 2011 O SER A 263 5872 6091 5810 -53 53 -134 O ATOM 2012 CB SER A 263 21.371 39.213 20.270 1.00 49.97 C ANISOU 2012 CB SER A 263 6334 6368 6285 35 -12 -15 C ATOM 2013 OG SER A 263 21.888 40.497 19.979 1.00 51.65 O ANISOU 2013 OG SER A 263 6624 6447 6554 -38 17 -14 O ATOM 2014 N ALA A 264 22.870 36.830 19.024 1.00 43.35 N ANISOU 2014 N ALA A 264 5442 5612 5418 21 158 -26 N ATOM 2015 CA ALA A 264 23.693 36.109 18.063 1.00 40.35 C ANISOU 2015 CA ALA A 264 5156 5106 5071 -120 21 92 C ATOM 2016 C ALA A 264 24.215 37.034 16.967 1.00 37.18 C ANISOU 2016 C ALA A 264 4589 4807 4732 57 41 -104 C ATOM 2017 O ALA A 264 23.598 38.070 16.705 1.00 36.35 O ANISOU 2017 O ALA A 264 4585 4682 4546 -41 47 -98 O ATOM 2018 CB ALA A 264 22.840 35.001 17.445 1.00 41.09 C ANISOU 2018 CB ALA A 264 5207 5211 5195 -93 38 -59 C ATOM 2019 N MET A 265 25.341 36.665 16.344 1.00 33.78 N ANISOU 2019 N MET A 265 4406 4265 4165 -70 -44 61 N ATOM 2020 CA MET A 265 25.857 37.448 15.227 1.00 30.22 C ANISOU 2020 CA MET A 265 3736 3835 3910 11 -113 -140 C ATOM 2021 C MET A 265 24.992 37.182 13.997 1.00 28.91 C ANISOU 2021 C MET A 265 3686 3604 3693 29 -24 -1 C ATOM 2022 O MET A 265 24.778 36.023 13.631 1.00 29.07 O ANISOU 2022 O MET A 265 3634 3647 3764 -102 -114 70 O ATOM 2023 CB MET A 265 27.315 37.126 14.866 1.00 27.96 C ANISOU 2023 CB MET A 265 3633 3442 3550 -139 -157 -216 C ATOM 2024 CG MET A 265 28.302 37.519 15.960 1.00 25.72 C ANISOU 2024 CG MET A 265 3559 2723 3492 -185 -55 -190 C ATOM 2025 SD MET A 265 28.564 39.352 16.050 1.00 19.73 S ANISOU 2025 SD MET A 265 2617 2445 2435 -355 -129 -808 S ATOM 2026 CE MET A 265 29.735 39.254 17.409 1.00 24.65 C ANISOU 2026 CE MET A 265 3183 3323 2859 -104 -302 -202 C ATOM 2027 N PRO A 266 24.611 38.247 13.302 1.00 26.94 N ANISOU 2027 N PRO A 266 3318 3444 3472 -11 55 -80 N ATOM 2028 CA PRO A 266 23.702 38.166 12.188 1.00 26.11 C ANISOU 2028 CA PRO A 266 3297 3281 3344 6 116 -37 C ATOM 2029 C PRO A 266 24.253 37.453 10.971 1.00 24.88 C ANISOU 2029 C PRO A 266 3022 3137 3295 -57 61 -33 C ATOM 2030 O PRO A 266 23.484 36.848 10.200 1.00 24.03 O ANISOU 2030 O PRO A 266 2777 3113 3240 -124 132 75 O ATOM 2031 CB PRO A 266 23.390 39.635 11.885 1.00 26.80 C ANISOU 2031 CB PRO A 266 3386 3324 3471 3 57 4 C ATOM 2032 CG PRO A 266 24.659 40.355 12.267 1.00 27.44 C ANISOU 2032 CG PRO A 266 3450 3461 3516 -17 -9 -49 C ATOM 2033 CD PRO A 266 25.147 39.624 13.501 1.00 27.51 C ANISOU 2033 CD PRO A 266 3482 3441 3528 28 35 -32 C ATOM 2034 N HIS A 267 25.582 37.518 10.807 1.00 23.40 N ANISOU 2034 N HIS A 267 2937 2843 3111 -124 47 -117 N ATOM 2035 CA HIS A 267 26.214 36.938 9.628 1.00 23.56 C ANISOU 2035 CA HIS A 267 2913 2918 3121 -102 110 -31 C ATOM 2036 C HIS A 267 26.649 35.496 9.857 1.00 23.98 C ANISOU 2036 C HIS A 267 3013 2941 3155 -84 69 -75 C ATOM 2037 O HIS A 267 27.124 34.900 8.881 1.00 26.18 O ANISOU 2037 O HIS A 267 3386 3092 3471 24 192 -259 O ATOM 2038 CB HIS A 267 27.432 37.760 9.171 1.00 23.11 C ANISOU 2038 CB HIS A 267 2929 2853 3000 -103 130 -38 C ATOM 2039 CG HIS A 267 28.466 37.979 10.222 1.00 23.84 C ANISOU 2039 CG HIS A 267 2998 2992 3069 -63 45 61 C ATOM 2040 ND1 HIS A 267 28.148 38.604 11.428 1.00 24.50 N ANISOU 2040 ND1 HIS A 267 3092 3043 3176 -127 78 18 N ATOM 2041 CD2 HIS A 267 29.799 37.754 10.270 1.00 23.85 C ANISOU 2041 CD2 HIS A 267 3010 2961 3091 -35 97 14 C ATOM 2042 CE1 HIS A 267 29.238 38.697 12.175 1.00 24.70 C ANISOU 2042 CE1 HIS A 267 3129 3094 3162 -42 21 -14 C ATOM 2043 NE2 HIS A 267 30.257 38.180 11.492 1.00 24.55 N ANISOU 2043 NE2 HIS A 267 3024 3124 3180 -115 71 -8 N ATOM 2044 N LYS A 268 26.486 34.914 11.023 1.00 23.02 N ANISOU 2044 N LYS A 268 2910 2788 3049 -137 -59 -119 N ATOM 2045 CA LYS A 268 27.054 33.602 11.303 1.00 24.50 C ANISOU 2045 CA LYS A 268 3050 2921 3337 -61 58 -24 C ATOM 2046 C LYS A 268 25.958 32.606 11.675 1.00 21.82 C ANISOU 2046 C LYS A 268 2801 2703 2788 22 -101 -60 C ATOM 2047 O LYS A 268 26.162 31.775 12.571 1.00 22.01 O ANISOU 2047 O LYS A 268 2769 2586 3009 50 -211 -47 O ATOM 2048 CB LYS A 268 28.096 33.723 12.429 1.00 28.51 C ANISOU 2048 CB LYS A 268 3604 3624 3603 72 -197 -83 C ATOM 2049 CG LYS A 268 29.347 34.466 11.931 1.00 33.14 C ANISOU 2049 CG LYS A 268 4046 4137 4410 -97 129 79 C ATOM 2050 CD LYS A 268 30.181 34.968 13.078 1.00 37.35 C ANISOU 2050 CD LYS A 268 4721 4800 4672 -115 -84 -125 C ATOM 2051 CE LYS A 268 31.160 33.977 13.665 1.00 40.38 C ANISOU 2051 CE LYS A 268 5029 5117 5195 103 -61 28 C ATOM 2052 NZ LYS A 268 32.580 34.413 13.422 1.00 42.45 N ANISOU 2052 NZ LYS A 268 5218 5438 5474 -115 64 -4 N ATOM 2053 N LYS A 269 24.780 32.751 11.085 1.00 18.38 N ANISOU 2053 N LYS A 269 2482 2115 2388 -21 131 -116 N ATOM 2054 CA LYS A 269 23.694 31.793 11.353 1.00 17.90 C ANISOU 2054 CA LYS A 269 2499 2007 2297 -26 25 -224 C ATOM 2055 C LYS A 269 23.835 30.569 10.432 1.00 15.92 C ANISOU 2055 C LYS A 269 2172 1812 2066 43 17 -61 C ATOM 2056 O LYS A 269 23.561 30.699 9.259 1.00 16.14 O ANISOU 2056 O LYS A 269 2256 1797 2078 62 6 -196 O ATOM 2057 CB LYS A 269 22.325 32.421 11.092 1.00 20.15 C ANISOU 2057 CB LYS A 269 2510 2385 2761 9 12 -50 C ATOM 2058 CG LYS A 269 22.019 33.697 11.875 1.00 24.08 C ANISOU 2058 CG LYS A 269 3244 2714 3190 -1 62 -275 C ATOM 2059 CD LYS A 269 21.812 33.494 13.344 1.00 27.00 C ANISOU 2059 CD LYS A 269 3612 3324 3321 -19 34 -47 C ATOM 2060 CE LYS A 269 21.392 34.825 14.002 1.00 29.28 C ANISOU 2060 CE LYS A 269 3881 3534 3709 90 46 -214 C ATOM 2061 NZ LYS A 269 20.223 35.476 13.341 1.00 31.03 N ANISOU 2061 NZ LYS A 269 4059 3884 3845 90 -48 -49 N ATOM 2062 N ASN A 270 24.173 29.420 10.964 1.00 14.18 N ANISOU 2062 N ASN A 270 1880 1650 1858 -23 16 -216 N ATOM 2063 CA ASN A 270 24.486 28.242 10.136 1.00 13.15 C ANISOU 2063 CA ASN A 270 1641 1522 1835 -118 -19 -165 C ATOM 2064 C ASN A 270 23.315 27.266 10.214 1.00 12.85 C ANISOU 2064 C ASN A 270 1719 1441 1724 -130 18 -98 C ATOM 2065 O ASN A 270 22.784 27.068 11.325 1.00 12.61 O ANISOU 2065 O ASN A 270 1752 1275 1763 -157 98 -219 O ATOM 2066 CB ASN A 270 25.693 27.545 10.740 1.00 13.07 C ANISOU 2066 CB ASN A 270 1598 1580 1789 -108 -84 -136 C ATOM 2067 CG ASN A 270 26.928 28.459 10.660 1.00 14.29 C ANISOU 2067 CG ASN A 270 1794 1777 1860 -173 -42 16 C ATOM 2068 OD1 ASN A 270 27.196 28.983 9.613 1.00 14.33 O ANISOU 2068 OD1 ASN A 270 1882 1631 1931 -213 7 44 O ATOM 2069 ND2 ASN A 270 27.662 28.608 11.762 1.00 15.45 N ANISOU 2069 ND2 ASN A 270 1796 2000 2074 -225 -183 -269 N ATOM 2070 N PRO A 271 23.038 26.573 9.118 1.00 11.91 N ANISOU 2070 N PRO A 271 1597 1333 1595 -148 -66 -10 N ATOM 2071 CA PRO A 271 21.916 25.635 9.107 1.00 11.54 C ANISOU 2071 CA PRO A 271 1479 1368 1537 -114 -89 72 C ATOM 2072 C PRO A 271 22.345 24.269 9.634 1.00 12.09 C ANISOU 2072 C PRO A 271 1510 1421 1662 -37 -109 45 C ATOM 2073 O PRO A 271 22.181 23.210 8.998 1.00 11.87 O ANISOU 2073 O PRO A 271 1474 1475 1561 33 -263 -12 O ATOM 2074 CB PRO A 271 21.526 25.554 7.638 1.00 11.44 C ANISOU 2074 CB PRO A 271 1446 1426 1475 -176 29 -37 C ATOM 2075 CG PRO A 271 22.790 25.832 6.891 1.00 11.36 C ANISOU 2075 CG PRO A 271 1366 1393 1560 -106 14 -110 C ATOM 2076 CD PRO A 271 23.513 26.882 7.754 1.00 12.29 C ANISOU 2076 CD PRO A 271 1582 1511 1577 -190 -5 -181 C ATOM 2077 N ILE A 272 22.849 24.265 10.874 1.00 11.44 N ANISOU 2077 N ILE A 272 1377 1472 1498 -216 30 127 N ATOM 2078 CA ILE A 272 23.400 23.055 11.471 1.00 13.05 C ANISOU 2078 CA ILE A 272 1554 1470 1936 -74 43 103 C ATOM 2079 C ILE A 272 22.350 21.966 11.684 1.00 11.88 C ANISOU 2079 C ILE A 272 1396 1406 1711 -37 78 20 C ATOM 2080 O ILE A 272 22.629 20.768 11.525 1.00 12.78 O ANISOU 2080 O ILE A 272 1512 1448 1897 -21 71 -25 O ATOM 2081 CB ILE A 272 23.902 23.461 12.882 1.00 17.37 C ANISOU 2081 CB ILE A 272 2225 2172 2205 -180 -259 82 C ATOM 2082 CG1 ILE A 272 25.028 24.506 12.741 1.00 20.00 C ANISOU 2082 CG1 ILE A 272 2397 2500 2700 -208 -29 162 C ATOM 2083 CG2 ILE A 272 24.424 22.246 13.649 1.00 18.91 C ANISOU 2083 CG2 ILE A 272 2391 2139 2653 -56 -170 99 C ATOM 2084 CD1 ILE A 272 26.164 23.978 11.929 1.00 20.81 C ANISOU 2084 CD1 ILE A 272 2524 2530 2852 -27 58 93 C ATOM 2085 N THR A 273 21.126 22.344 12.103 1.00 11.11 N ANISOU 2085 N THR A 273 1365 1233 1623 -69 62 -13 N ATOM 2086 CA THR A 273 20.105 21.297 12.300 1.00 11.00 C ANISOU 2086 CA THR A 273 1261 1317 1600 -68 89 -63 C ATOM 2087 C THR A 273 19.819 20.569 11.001 1.00 10.95 C ANISOU 2087 C THR A 273 1366 1258 1538 4 20 40 C ATOM 2088 O THR A 273 19.722 19.342 10.955 1.00 10.45 O ANISOU 2088 O THR A 273 1257 1188 1525 44 -59 206 O ATOM 2089 CB THR A 273 18.770 21.900 12.806 1.00 12.68 C ANISOU 2089 CB THR A 273 1378 1631 1807 -109 173 -127 C ATOM 2090 OG1 THR A 273 19.121 22.670 13.960 1.00 13.22 O ANISOU 2090 OG1 THR A 273 1576 1811 1637 66 71 -88 O ATOM 2091 CG2 THR A 273 17.762 20.814 13.177 1.00 12.60 C ANISOU 2091 CG2 THR A 273 1363 1687 1738 -148 110 -66 C ATOM 2092 N CYS A 274 19.693 21.326 9.902 1.00 10.30 N ANISOU 2092 N CYS A 274 1195 1332 1387 59 11 8 N ATOM 2093 CA CYS A 274 19.387 20.698 8.612 1.00 10.52 C ANISOU 2093 CA CYS A 274 1234 1371 1391 135 21 -30 C ATOM 2094 C CYS A 274 20.576 19.898 8.111 1.00 9.74 C ANISOU 2094 C CYS A 274 1037 1296 1370 -20 -37 -33 C ATOM 2095 O CYS A 274 20.364 18.877 7.470 1.00 9.69 O ANISOU 2095 O CYS A 274 1043 1326 1313 -51 -2 -66 O ATOM 2096 CB CYS A 274 18.949 21.778 7.615 1.00 10.73 C ANISOU 2096 CB CYS A 274 1208 1478 1392 149 63 20 C ATOM 2097 SG CYS A 274 17.305 22.450 8.067 1.00 12.83 S ANISOU 2097 SG CYS A 274 1319 1754 1800 432 -10 15 S ATOM 2098 N GLU A 275 21.813 20.277 8.389 1.00 8.89 N ANISOU 2098 N GLU A 275 971 1191 1214 -52 -60 -42 N ATOM 2099 CA GLU A 275 22.961 19.431 8.020 1.00 9.81 C ANISOU 2099 CA GLU A 275 1107 1166 1453 -58 6 68 C ATOM 2100 C GLU A 275 22.898 18.132 8.814 1.00 9.37 C ANISOU 2100 C GLU A 275 1150 1138 1274 -75 -4 15 C ATOM 2101 O GLU A 275 23.122 17.034 8.280 1.00 9.04 O ANISOU 2101 O GLU A 275 862 1227 1344 0 16 -31 O ATOM 2102 CB GLU A 275 24.251 20.231 8.326 1.00 10.12 C ANISOU 2102 CB GLU A 275 1136 1285 1424 -153 -62 102 C ATOM 2103 CG GLU A 275 24.456 21.323 7.280 1.00 11.34 C ANISOU 2103 CG GLU A 275 1406 1268 1636 -201 -35 145 C ATOM 2104 CD GLU A 275 25.613 22.262 7.604 1.00 13.22 C ANISOU 2104 CD GLU A 275 1542 1544 1935 -240 -199 86 C ATOM 2105 OE1 GLU A 275 26.483 21.917 8.436 1.00 12.85 O ANISOU 2105 OE1 GLU A 275 1703 1530 1651 -224 -104 59 O ATOM 2106 OE2 GLU A 275 25.671 23.342 6.959 1.00 14.65 O ANISOU 2106 OE2 GLU A 275 1741 1598 2226 -301 -79 167 O ATOM 2107 N ARG A 276 22.547 18.236 10.100 1.00 9.26 N ANISOU 2107 N ARG A 276 1093 1153 1274 -12 114 -41 N ATOM 2108 CA ARG A 276 22.423 17.003 10.920 1.00 10.76 C ANISOU 2108 CA ARG A 276 1332 1348 1409 -115 37 46 C ATOM 2109 C ARG A 276 21.336 16.107 10.309 1.00 10.79 C ANISOU 2109 C ARG A 276 1249 1321 1529 -33 20 -28 C ATOM 2110 O ARG A 276 21.519 14.887 10.246 1.00 10.59 O ANISOU 2110 O ARG A 276 1284 1331 1408 -33 36 -5 O ATOM 2111 CB ARG A 276 22.111 17.356 12.396 1.00 12.12 C ANISOU 2111 CB ARG A 276 1592 1547 1464 -17 53 -14 C ATOM 2112 CG ARG A 276 21.845 16.131 13.275 1.00 15.33 C ANISOU 2112 CG ARG A 276 2081 1753 1990 -48 15 217 C ATOM 2113 CD ARG A 276 21.387 16.535 14.696 1.00 20.05 C ANISOU 2113 CD ARG A 276 2792 2528 2297 5 213 6 C ATOM 2114 NE ARG A 276 22.358 17.501 15.243 1.00 23.57 N ANISOU 2114 NE ARG A 276 3104 3053 2797 -155 -57 -53 N ATOM 2115 CZ ARG A 276 21.908 18.697 15.682 1.00 26.91 C ANISOU 2115 CZ ARG A 276 3599 3345 3281 21 4 -173 C ATOM 2116 NH1 ARG A 276 20.607 19.023 15.702 1.00 28.93 N ANISOU 2116 NH1 ARG A 276 3688 3708 3596 80 23 -71 N ATOM 2117 NH2 ARG A 276 22.784 19.593 16.108 1.00 28.15 N ANISOU 2117 NH2 ARG A 276 3755 3436 3506 -160 30 -126 N ATOM 2118 N LEU A 277 20.175 16.658 9.958 1.00 9.97 N ANISOU 2118 N LEU A 277 1106 1429 1252 -148 -9 71 N ATOM 2119 CA LEU A 277 19.118 15.852 9.326 1.00 9.51 C ANISOU 2119 CA LEU A 277 1080 1198 1336 42 -20 -73 C ATOM 2120 C LEU A 277 19.588 15.191 8.038 1.00 9.44 C ANISOU 2120 C LEU A 277 1103 1248 1236 29 -28 15 C ATOM 2121 O LEU A 277 19.205 14.024 7.814 1.00 9.32 O ANISOU 2121 O LEU A 277 913 1327 1301 -61 8 -35 O ATOM 2122 CB LEU A 277 17.874 16.726 8.992 1.00 10.68 C ANISOU 2122 CB LEU A 277 1166 1299 1594 156 7 -90 C ATOM 2123 CG LEU A 277 17.148 17.246 10.257 1.00 12.04 C ANISOU 2123 CG LEU A 277 1511 1536 1527 152 127 49 C ATOM 2124 CD1 LEU A 277 16.027 18.206 9.846 1.00 13.10 C ANISOU 2124 CD1 LEU A 277 1439 1757 1781 226 141 43 C ATOM 2125 CD2 LEU A 277 16.523 16.147 11.073 1.00 13.26 C ANISOU 2125 CD2 LEU A 277 1728 1685 1624 62 172 89 C ATOM 2126 N THR A 278 20.410 15.877 7.241 1.00 9.54 N ANISOU 2126 N THR A 278 1054 1301 1269 -51 8 -66 N ATOM 2127 CA THR A 278 20.927 15.235 6.016 1.00 10.05 C ANISOU 2127 CA THR A 278 1255 1355 1207 20 21 -11 C ATOM 2128 C THR A 278 21.754 13.997 6.362 1.00 10.31 C ANISOU 2128 C THR A 278 1261 1240 1417 -61 -15 -20 C ATOM 2129 O THR A 278 21.600 12.927 5.769 1.00 9.69 O ANISOU 2129 O THR A 278 1199 1196 1287 111 -46 -67 O ATOM 2130 CB THR A 278 21.772 16.252 5.236 1.00 11.07 C ANISOU 2130 CB THR A 278 1483 1364 1361 -92 71 -38 C ATOM 2131 OG1 THR A 278 20.978 17.437 5.002 1.00 12.60 O ANISOU 2131 OG1 THR A 278 1574 1639 1574 45 74 59 O ATOM 2132 CG2 THR A 278 22.240 15.690 3.889 1.00 11.47 C ANISOU 2132 CG2 THR A 278 1599 1452 1307 -55 102 74 C ATOM 2133 N GLY A 279 22.643 14.123 7.356 1.00 9.78 N ANISOU 2133 N GLY A 279 1159 1179 1377 -89 4 132 N ATOM 2134 CA GLY A 279 23.460 12.989 7.820 1.00 10.37 C ANISOU 2134 CA GLY A 279 1061 1208 1672 -86 85 90 C ATOM 2135 C GLY A 279 22.609 11.844 8.351 1.00 9.61 C ANISOU 2135 C GLY A 279 1154 1033 1467 38 58 67 C ATOM 2136 O GLY A 279 22.875 10.678 8.032 1.00 9.60 O ANISOU 2136 O GLY A 279 918 1055 1675 15 68 -140 O ATOM 2137 N LEU A 280 21.592 12.151 9.145 1.00 8.34 N ANISOU 2137 N LEU A 280 892 1024 1253 -146 58 69 N ATOM 2138 CA LEU A 280 20.737 11.060 9.706 1.00 8.38 C ANISOU 2138 CA LEU A 280 1098 982 1104 -168 36 22 C ATOM 2139 C LEU A 280 19.982 10.351 8.599 1.00 8.11 C ANISOU 2139 C LEU A 280 991 1014 1078 -115 12 73 C ATOM 2140 O LEU A 280 19.807 9.140 8.669 1.00 8.26 O ANISOU 2140 O LEU A 280 1116 964 1059 -153 -81 107 O ATOM 2141 CB LEU A 280 19.793 11.673 10.730 1.00 8.74 C ANISOU 2141 CB LEU A 280 1174 1113 1032 -139 43 15 C ATOM 2142 CG LEU A 280 20.511 12.102 12.036 1.00 8.98 C ANISOU 2142 CG LEU A 280 1133 1148 1131 46 -64 -72 C ATOM 2143 CD1 LEU A 280 19.478 12.658 13.010 1.00 9.60 C ANISOU 2143 CD1 LEU A 280 1299 1398 951 18 25 -83 C ATOM 2144 CD2 LEU A 280 21.260 10.936 12.711 1.00 9.62 C ANISOU 2144 CD2 LEU A 280 1229 1323 1104 49 -133 16 C ATOM 2145 N SER A 281 19.600 11.048 7.518 1.00 8.29 N ANISOU 2145 N SER A 281 974 1071 1103 -104 -69 133 N ATOM 2146 CA SER A 281 18.990 10.337 6.385 1.00 9.57 C ANISOU 2146 CA SER A 281 1379 1126 1133 64 -63 -11 C ATOM 2147 C SER A 281 19.948 9.346 5.745 1.00 9.09 C ANISOU 2147 C SER A 281 1130 1108 1218 -1 -39 133 C ATOM 2148 O SER A 281 19.504 8.287 5.271 1.00 10.23 O ANISOU 2148 O SER A 281 1373 1098 1418 20 19 -34 O ATOM 2149 CB SER A 281 18.568 11.358 5.309 1.00 11.40 C ANISOU 2149 CB SER A 281 1643 1203 1484 249 -227 119 C ATOM 2150 OG SER A 281 17.893 10.642 4.270 1.00 16.31 O ANISOU 2150 OG SER A 281 2018 2103 2077 -87 -233 -54 O ATOM 2151 N ARG A 282 21.247 9.644 5.687 1.00 9.00 N ANISOU 2151 N ARG A 282 1017 1126 1275 45 -44 176 N ATOM 2152 CA ARG A 282 22.193 8.627 5.205 1.00 9.12 C ANISOU 2152 CA ARG A 282 1009 1081 1376 -83 -34 -41 C ATOM 2153 C ARG A 282 22.176 7.374 6.054 1.00 9.15 C ANISOU 2153 C ARG A 282 1004 1242 1229 -85 -45 26 C ATOM 2154 O ARG A 282 22.335 6.272 5.501 1.00 9.55 O ANISOU 2154 O ARG A 282 1159 1176 1295 45 -135 96 O ATOM 2155 CB ARG A 282 23.644 9.178 5.201 1.00 10.01 C ANISOU 2155 CB ARG A 282 940 1286 1577 -103 55 74 C ATOM 2156 CG ARG A 282 23.772 10.411 4.262 1.00 10.66 C ANISOU 2156 CG ARG A 282 924 1435 1689 -182 -69 123 C ATOM 2157 CD ARG A 282 25.236 10.974 4.343 1.00 9.67 C ANISOU 2157 CD ARG A 282 947 1236 1490 -213 -65 -63 C ATOM 2158 NE ARG A 282 25.185 12.190 3.529 1.00 11.75 N ANISOU 2158 NE ARG A 282 1353 1370 1741 -73 26 31 N ATOM 2159 CZ ARG A 282 25.919 13.288 3.799 1.00 12.85 C ANISOU 2159 CZ ARG A 282 1612 1442 1828 -126 -44 76 C ATOM 2160 NH1 ARG A 282 26.815 13.316 4.761 1.00 11.72 N ANISOU 2160 NH1 ARG A 282 1309 1252 1893 -170 14 -41 N ATOM 2161 NH2 ARG A 282 25.689 14.369 3.037 1.00 13.39 N ANISOU 2161 NH2 ARG A 282 1691 1549 1846 -73 60 138 N ATOM 2162 N MET A 283 22.040 7.480 7.391 1.00 9.55 N ANISOU 2162 N MET A 283 1077 1293 1260 -51 -14 10 N ATOM 2163 CA MET A 283 21.971 6.286 8.215 1.00 9.86 C ANISOU 2163 CA MET A 283 1172 1311 1262 -153 -39 -6 C ATOM 2164 C MET A 283 20.672 5.512 7.953 1.00 9.80 C ANISOU 2164 C MET A 283 1071 1271 1381 -23 -28 -37 C ATOM 2165 O MET A 283 20.671 4.253 7.926 1.00 10.37 O ANISOU 2165 O MET A 283 1158 1173 1610 -15 -50 8 O ATOM 2166 CB MET A 283 22.085 6.628 9.708 1.00 9.84 C ANISOU 2166 CB MET A 283 1095 1393 1253 2 -43 -82 C ATOM 2167 CG MET A 283 23.437 7.143 10.189 1.00 10.08 C ANISOU 2167 CG MET A 283 1256 981 1594 29 -155 -158 C ATOM 2168 SD MET A 283 24.794 5.943 9.887 1.00 3.98 S ANISOU 2168 SD MET A 283 505 339 667 -60 -159 87 S ATOM 2169 CE MET A 283 24.183 4.421 10.647 1.00 9.64 C ANISOU 2169 CE MET A 283 1387 293 1982 46 -220 241 C ATOM 2170 N MET A 284 19.552 6.206 7.778 1.00 9.40 N ANISOU 2170 N MET A 284 1158 1229 1186 24 -85 5 N ATOM 2171 CA MET A 284 18.267 5.554 7.561 1.00 8.56 C ANISOU 2171 CA MET A 284 959 1132 1162 102 78 -6 C ATOM 2172 C MET A 284 18.320 4.740 6.279 1.00 9.84 C ANISOU 2172 C MET A 284 1253 1199 1289 37 -40 -5 C ATOM 2173 O MET A 284 17.892 3.564 6.208 1.00 11.45 O ANISOU 2173 O MET A 284 1363 1284 1703 -99 14 6 O ATOM 2174 CB MET A 284 17.185 6.636 7.429 1.00 7.96 C ANISOU 2174 CB MET A 284 957 1104 962 70 -8 75 C ATOM 2175 CG MET A 284 16.872 7.381 8.714 1.00 8.20 C ANISOU 2175 CG MET A 284 1097 1239 781 -54 252 273 C ATOM 2176 SD MET A 284 16.236 6.214 10.069 1.00 3.24 S ANISOU 2176 SD MET A 284 254 684 293 -10 -2 39 S ATOM 2177 CE MET A 284 14.758 5.506 9.175 1.00 5.69 C ANISOU 2177 CE MET A 284 307 901 954 51 -189 -50 C ATOM 2178 N ARG A 285 18.916 5.316 5.234 1.00 10.15 N ANISOU 2178 N ARG A 285 1220 1192 1446 -33 33 56 N ATOM 2179 CA ARG A 285 19.019 4.494 3.998 1.00 11.90 C ANISOU 2179 CA ARG A 285 1539 1502 1481 35 79 -8 C ATOM 2180 C ARG A 285 20.053 3.422 4.162 1.00 10.37 C ANISOU 2180 C ARG A 285 1364 1380 1194 -90 117 21 C ATOM 2181 O ARG A 285 19.895 2.319 3.572 1.00 10.56 O ANISOU 2181 O ARG A 285 1393 1149 1470 -127 151 86 O ATOM 2182 CB ARG A 285 19.159 5.370 2.783 1.00 15.95 C ANISOU 2182 CB ARG A 285 2136 2103 1821 -58 44 229 C ATOM 2183 CG ARG A 285 20.493 5.961 2.532 1.00 17.70 C ANISOU 2183 CG ARG A 285 2217 2331 2175 -138 101 252 C ATOM 2184 CD ARG A 285 20.492 6.546 1.071 1.00 17.66 C ANISOU 2184 CD ARG A 285 2282 2286 2144 -67 -137 203 C ATOM 2185 NE ARG A 285 21.157 7.835 1.132 1.00 15.37 N ANISOU 2185 NE ARG A 285 1896 2210 1735 -64 -23 165 N ATOM 2186 CZ ARG A 285 20.556 9.002 1.305 1.00 16.16 C ANISOU 2186 CZ ARG A 285 1969 2232 1940 -82 -62 31 C ATOM 2187 NH1 ARG A 285 19.241 9.172 1.465 1.00 16.60 N ANISOU 2187 NH1 ARG A 285 1959 2329 2018 -62 -92 61 N ATOM 2188 NH2 ARG A 285 21.331 10.091 1.297 1.00 16.69 N ANISOU 2188 NH2 ARG A 285 2005 2313 2024 -177 -87 80 N ATOM 2189 N ALA A 286 21.071 3.596 5.001 1.00 9.60 N ANISOU 2189 N ALA A 286 1157 1139 1352 -122 123 136 N ATOM 2190 CA ALA A 286 22.071 2.513 5.158 1.00 10.10 C ANISOU 2190 CA ALA A 286 1086 1297 1456 -108 42 190 C ATOM 2191 C ALA A 286 21.418 1.262 5.764 1.00 11.14 C ANISOU 2191 C ALA A 286 1370 1189 1674 -102 53 64 C ATOM 2192 O ALA A 286 21.932 0.179 5.480 1.00 11.09 O ANISOU 2192 O ALA A 286 1234 1229 1749 -55 -64 -9 O ATOM 2193 CB ALA A 286 23.186 3.029 6.078 1.00 10.30 C ANISOU 2193 CB ALA A 286 1035 1433 1444 31 44 77 C ATOM 2194 N TYR A 287 20.364 1.419 6.577 1.00 10.20 N ANISOU 2194 N TYR A 287 1126 1297 1454 -136 -36 91 N ATOM 2195 CA TYR A 287 19.719 0.224 7.174 1.00 11.24 C ANISOU 2195 CA TYR A 287 1427 1291 1552 -166 6 72 C ATOM 2196 C TYR A 287 18.918 -0.618 6.180 1.00 12.46 C ANISOU 2196 C TYR A 287 1666 1485 1583 -94 -110 34 C ATOM 2197 O TYR A 287 18.535 -1.784 6.523 1.00 13.71 O ANISOU 2197 O TYR A 287 1740 1569 1901 -21 -128 114 O ATOM 2198 CB TYR A 287 18.745 0.702 8.267 1.00 11.95 C ANISOU 2198 CB TYR A 287 1621 1446 1474 -117 -35 50 C ATOM 2199 CG TYR A 287 19.421 1.455 9.410 1.00 12.00 C ANISOU 2199 CG TYR A 287 1634 1520 1404 -102 -12 52 C ATOM 2200 CD1 TYR A 287 18.849 2.580 9.947 1.00 11.56 C ANISOU 2200 CD1 TYR A 287 1528 1483 1380 -64 81 176 C ATOM 2201 CD2 TYR A 287 20.645 1.003 9.922 1.00 12.00 C ANISOU 2201 CD2 TYR A 287 1480 1478 1603 -104 30 77 C ATOM 2202 CE1 TYR A 287 19.439 3.267 11.007 1.00 12.78 C ANISOU 2202 CE1 TYR A 287 1646 1600 1611 -165 116 24 C ATOM 2203 CE2 TYR A 287 21.241 1.671 10.989 1.00 13.35 C ANISOU 2203 CE2 TYR A 287 1761 1644 1668 -76 -13 32 C ATOM 2204 CZ TYR A 287 20.622 2.796 11.517 1.00 13.86 C ANISOU 2204 CZ TYR A 287 1827 1803 1637 -48 47 29 C ATOM 2205 OH TYR A 287 21.272 3.466 12.515 1.00 16.58 O ANISOU 2205 OH TYR A 287 2292 2050 1957 -175 -26 -162 O ATOM 2206 N VAL A 288 18.609 -0.121 4.981 1.00 11.11 N ANISOU 2206 N VAL A 288 1502 1143 1578 54 -107 -6 N ATOM 2207 CA VAL A 288 17.775 -0.877 4.045 1.00 11.88 C ANISOU 2207 CA VAL A 288 1581 1414 1518 55 -89 -62 C ATOM 2208 C VAL A 288 18.500 -2.126 3.549 1.00 12.71 C ANISOU 2208 C VAL A 288 1619 1486 1723 132 -90 39 C ATOM 2209 O VAL A 288 17.927 -3.235 3.586 1.00 12.34 O ANISOU 2209 O VAL A 288 1557 1453 1678 215 -57 222 O ATOM 2210 CB VAL A 288 17.367 0.017 2.853 1.00 12.69 C ANISOU 2210 CB VAL A 288 1803 1433 1586 143 -183 -115 C ATOM 2211 CG1 VAL A 288 16.553 -0.818 1.848 1.00 13.74 C ANISOU 2211 CG1 VAL A 288 1880 1664 1678 -27 -206 -83 C ATOM 2212 CG2 VAL A 288 16.567 1.224 3.345 1.00 12.70 C ANISOU 2212 CG2 VAL A 288 1594 1451 1782 75 -74 -109 C ATOM 2213 N ASP A 289 19.772 -1.968 3.133 1.00 13.36 N ANISOU 2213 N ASP A 289 1731 1590 1756 26 33 170 N ATOM 2214 CA ASP A 289 20.458 -3.148 2.556 1.00 14.67 C ANISOU 2214 CA ASP A 289 1979 1703 1892 203 -84 123 C ATOM 2215 C ASP A 289 20.505 -4.367 3.478 1.00 12.64 C ANISOU 2215 C ASP A 289 1581 1636 1588 -18 23 34 C ATOM 2216 O ASP A 289 20.164 -5.484 3.085 1.00 11.79 O ANISOU 2216 O ASP A 289 1271 1590 1618 138 -113 111 O ATOM 2217 CB ASP A 289 21.846 -2.754 2.059 1.00 18.81 C ANISOU 2217 CB ASP A 289 2239 2341 2568 -51 84 -9 C ATOM 2218 CG ASP A 289 21.742 -1.935 0.780 1.00 24.28 C ANISOU 2218 CG ASP A 289 3262 3084 2878 52 7 144 C ATOM 2219 OD1 ASP A 289 20.706 -1.915 0.058 1.00 27.02 O ANISOU 2219 OD1 ASP A 289 3355 3617 3295 21 -123 152 O ATOM 2220 OD2 ASP A 289 22.745 -1.272 0.436 1.00 27.67 O ANISOU 2220 OD2 ASP A 289 3425 3444 3644 -83 70 127 O ATOM 2221 N PRO A 290 20.885 -4.208 4.743 1.00 11.44 N ANISOU 2221 N PRO A 290 1441 1344 1560 -92 -100 127 N ATOM 2222 CA PRO A 290 21.049 -5.355 5.643 1.00 10.54 C ANISOU 2222 CA PRO A 290 1309 1327 1368 -135 -89 70 C ATOM 2223 C PRO A 290 19.657 -5.921 5.886 1.00 10.14 C ANISOU 2223 C PRO A 290 1165 1381 1305 -10 -49 16 C ATOM 2224 O PRO A 290 19.534 -7.146 5.986 1.00 10.69 O ANISOU 2224 O PRO A 290 1227 1436 1400 25 -63 63 O ATOM 2225 CB PRO A 290 21.696 -4.815 6.915 1.00 10.85 C ANISOU 2225 CB PRO A 290 1415 1330 1376 3 -52 -39 C ATOM 2226 CG PRO A 290 21.519 -3.318 6.820 1.00 11.77 C ANISOU 2226 CG PRO A 290 1665 1336 1472 -55 -64 -43 C ATOM 2227 CD PRO A 290 21.513 -2.995 5.345 1.00 11.85 C ANISOU 2227 CD PRO A 290 1646 1316 1542 -96 -91 130 C ATOM 2228 N SER A 291 18.624 -5.065 5.915 1.00 9.33 N ANISOU 2228 N SER A 291 1232 1310 1002 23 8 -23 N ATOM 2229 CA SER A 291 17.259 -5.585 6.121 1.00 10.32 C ANISOU 2229 CA SER A 291 1216 1380 1324 1 -130 -67 C ATOM 2230 C SER A 291 16.821 -6.433 4.930 1.00 9.29 C ANISOU 2230 C SER A 291 1145 1169 1215 100 52 -77 C ATOM 2231 O SER A 291 16.138 -7.458 5.106 1.00 10.81 O ANISOU 2231 O SER A 291 1317 1445 1347 33 -34 190 O ATOM 2232 CB SER A 291 16.296 -4.384 6.277 1.00 12.52 C ANISOU 2232 CB SER A 291 1489 1462 1807 54 333 -269 C ATOM 2233 OG SER A 291 16.878 -3.653 7.438 1.00 17.20 O ANISOU 2233 OG SER A 291 2302 2093 2140 -40 -18 -200 O ATOM 2234 N LEU A 292 17.225 -6.058 3.696 1.00 7.58 N ANISOU 2234 N LEU A 292 649 1053 1177 121 -67 42 N ATOM 2235 CA LEU A 292 16.876 -6.883 2.542 1.00 8.94 C ANISOU 2235 CA LEU A 292 1083 1043 1270 107 23 2 C ATOM 2236 C LEU A 292 17.687 -8.188 2.527 1.00 10.46 C ANISOU 2236 C LEU A 292 1208 1162 1605 101 -13 78 C ATOM 2237 O LEU A 292 17.181 -9.236 2.111 1.00 9.93 O ANISOU 2237 O LEU A 292 1072 1205 1497 159 -110 -131 O ATOM 2238 CB LEU A 292 17.208 -6.134 1.217 1.00 9.79 C ANISOU 2238 CB LEU A 292 1151 1244 1325 133 40 47 C ATOM 2239 CG LEU A 292 16.202 -4.958 0.972 1.00 11.81 C ANISOU 2239 CG LEU A 292 1485 1339 1663 101 -224 284 C ATOM 2240 CD1 LEU A 292 16.856 -4.050 -0.071 1.00 14.84 C ANISOU 2240 CD1 LEU A 292 1966 1741 1931 -104 135 217 C ATOM 2241 CD2 LEU A 292 14.934 -5.575 0.425 1.00 13.36 C ANISOU 2241 CD2 LEU A 292 1462 1706 1908 3 -156 190 C ATOM 2242 N GLU A 293 18.938 -8.102 2.973 1.00 11.18 N ANISOU 2242 N GLU A 293 1223 1436 1587 81 -65 80 N ATOM 2243 CA GLU A 293 19.763 -9.321 3.058 1.00 10.90 C ANISOU 2243 CA GLU A 293 1354 1282 1505 30 109 146 C ATOM 2244 C GLU A 293 19.232 -10.313 4.077 1.00 10.86 C ANISOU 2244 C GLU A 293 1324 1289 1511 -32 92 103 C ATOM 2245 O GLU A 293 19.450 -11.532 3.928 1.00 12.50 O ANISOU 2245 O GLU A 293 1525 1382 1842 142 447 83 O ATOM 2246 CB GLU A 293 21.194 -8.956 3.458 1.00 13.09 C ANISOU 2246 CB GLU A 293 1495 1792 1688 -33 -54 39 C ATOM 2247 CG GLU A 293 21.959 -8.256 2.317 1.00 16.00 C ANISOU 2247 CG GLU A 293 1897 2038 2142 -162 165 172 C ATOM 2248 CD GLU A 293 23.439 -8.233 2.705 1.00 20.10 C ANISOU 2248 CD GLU A 293 2193 2743 2702 -102 -65 39 C ATOM 2249 OE1 GLU A 293 24.022 -7.151 2.825 1.00 21.39 O ANISOU 2249 OE1 GLU A 293 2334 2764 3030 -231 -56 80 O ATOM 2250 OE2 GLU A 293 24.046 -9.307 2.917 1.00 22.26 O ANISOU 2250 OE2 GLU A 293 2589 2929 2939 40 -64 105 O ATOM 2251 N ASN A 294 18.491 -9.845 5.066 1.00 10.20 N ANISOU 2251 N ASN A 294 1184 1350 1341 -43 -4 200 N ATOM 2252 CA ASN A 294 17.958 -10.756 6.110 1.00 10.04 C ANISOU 2252 CA ASN A 294 1171 1290 1355 -128 -34 137 C ATOM 2253 C ASN A 294 16.791 -11.599 5.575 1.00 10.80 C ANISOU 2253 C ASN A 294 1325 1348 1432 -122 -97 41 C ATOM 2254 O ASN A 294 16.334 -12.474 6.328 1.00 12.10 O ANISOU 2254 O ASN A 294 1480 1278 1840 -143 -157 118 O ATOM 2255 CB ASN A 294 17.404 -9.902 7.250 1.00 10.43 C ANISOU 2255 CB ASN A 294 1322 1347 1292 -151 -48 88 C ATOM 2256 CG ASN A 294 18.437 -9.334 8.197 1.00 10.62 C ANISOU 2256 CG ASN A 294 1249 1369 1417 -73 -55 82 C ATOM 2257 OD1 ASN A 294 19.600 -9.720 8.236 1.00 11.68 O ANISOU 2257 OD1 ASN A 294 1330 1416 1692 102 -166 239 O ATOM 2258 ND2 ASN A 294 18.014 -8.384 9.015 1.00 11.30 N ANISOU 2258 ND2 ASN A 294 1394 1293 1607 63 -111 37 N ATOM 2259 N ILE A 295 16.241 -11.287 4.394 1.00 9.35 N ANISOU 2259 N ILE A 295 1117 1088 1347 -90 -103 14 N ATOM 2260 CA ILE A 295 15.092 -12.050 3.902 1.00 8.70 C ANISOU 2260 CA ILE A 295 1061 1066 1178 8 -64 -43 C ATOM 2261 C ILE A 295 15.441 -13.496 3.595 1.00 9.75 C ANISOU 2261 C ILE A 295 1160 1105 1440 -52 85 3 C ATOM 2262 O ILE A 295 14.656 -14.407 3.903 1.00 9.93 O ANISOU 2262 O ILE A 295 1430 852 1492 -110 -153 87 O ATOM 2263 CB ILE A 295 14.497 -11.352 2.642 1.00 8.44 C ANISOU 2263 CB ILE A 295 1082 929 1196 16 -113 -119 C ATOM 2264 CG1 ILE A 295 13.893 -10.005 3.150 1.00 7.91 C ANISOU 2264 CG1 ILE A 295 1055 1024 927 184 89 -20 C ATOM 2265 CG2 ILE A 295 13.398 -12.156 1.966 1.00 8.41 C ANISOU 2265 CG2 ILE A 295 1124 1004 1067 -90 -76 -169 C ATOM 2266 CD1 ILE A 295 13.553 -9.051 2.005 1.00 8.91 C ANISOU 2266 CD1 ILE A 295 1251 1114 1020 231 -3 35 C ATOM 2267 N ALA A 296 16.613 -13.757 3.005 1.00 9.84 N ANISOU 2267 N ALA A 296 1149 1291 1297 -71 79 -75 N ATOM 2268 CA ALA A 296 16.962 -15.080 2.529 1.00 11.09 C ANISOU 2268 CA ALA A 296 1459 1278 1479 -23 202 51 C ATOM 2269 C ALA A 296 17.597 -15.919 3.643 1.00 12.52 C ANISOU 2269 C ALA A 296 1505 1649 1602 30 87 122 C ATOM 2270 O ALA A 296 18.742 -16.385 3.588 1.00 13.77 O ANISOU 2270 O ALA A 296 1596 1715 1919 64 279 196 O ATOM 2271 CB ALA A 296 17.856 -14.952 1.287 1.00 11.35 C ANISOU 2271 CB ALA A 296 1508 1267 1537 49 275 -85 C ATOM 2272 N LEU A 297 16.795 -16.189 4.685 1.00 11.85 N ANISOU 2272 N LEU A 297 1665 1426 1413 7 107 45 N ATOM 2273 CA LEU A 297 17.175 -17.085 5.764 1.00 11.73 C ANISOU 2273 CA LEU A 297 1596 1335 1525 59 17 -24 C ATOM 2274 C LEU A 297 17.174 -18.537 5.275 1.00 11.13 C ANISOU 2274 C LEU A 297 1459 1319 1450 19 -34 -19 C ATOM 2275 O LEU A 297 16.362 -18.902 4.400 1.00 11.81 O ANISOU 2275 O LEU A 297 1636 1407 1443 -52 -86 -36 O ATOM 2276 CB LEU A 297 16.121 -16.929 6.877 1.00 12.99 C ANISOU 2276 CB LEU A 297 1727 1578 1631 -12 112 -1 C ATOM 2277 CG LEU A 297 16.067 -15.546 7.532 1.00 13.98 C ANISOU 2277 CG LEU A 297 1772 1731 1810 50 72 -123 C ATOM 2278 CD1 LEU A 297 15.037 -15.601 8.673 1.00 16.51 C ANISOU 2278 CD1 LEU A 297 1891 2282 2099 -78 221 -121 C ATOM 2279 CD2 LEU A 297 17.416 -15.125 8.109 1.00 14.56 C ANISOU 2279 CD2 LEU A 297 1860 1666 2004 18 2 -161 C ATOM 2280 N TRP A 298 18.026 -19.347 5.864 1.00 10.23 N ANISOU 2280 N TRP A 298 1221 1228 1440 -2 58 -78 N ATOM 2281 CA TRP A 298 18.143 -20.755 5.496 1.00 10.39 C ANISOU 2281 CA TRP A 298 1221 1180 1548 -21 -23 -73 C ATOM 2282 C TRP A 298 16.988 -21.565 6.077 1.00 10.15 C ANISOU 2282 C TRP A 298 1199 1236 1421 90 -36 4 C ATOM 2283 O TRP A 298 16.752 -21.603 7.292 1.00 10.87 O ANISOU 2283 O TRP A 298 1294 1417 1421 19 -43 -164 O ATOM 2284 CB TRP A 298 19.480 -21.324 5.979 1.00 10.97 C ANISOU 2284 CB TRP A 298 1219 1385 1565 -16 59 -82 C ATOM 2285 CG TRP A 298 20.696 -20.752 5.275 1.00 11.64 C ANISOU 2285 CG TRP A 298 1355 1516 1552 -126 83 -103 C ATOM 2286 CD1 TRP A 298 20.797 -19.690 4.439 1.00 12.28 C ANISOU 2286 CD1 TRP A 298 1501 1580 1587 33 46 -91 C ATOM 2287 CD2 TRP A 298 22.017 -21.300 5.396 1.00 11.96 C ANISOU 2287 CD2 TRP A 298 1464 1510 1572 22 47 -167 C ATOM 2288 NE1 TRP A 298 22.129 -19.512 4.025 1.00 11.64 N ANISOU 2288 NE1 TRP A 298 1465 1501 1457 -111 -42 -71 N ATOM 2289 CE2 TRP A 298 22.874 -20.494 4.609 1.00 12.24 C ANISOU 2289 CE2 TRP A 298 1461 1510 1679 14 17 -150 C ATOM 2290 CE3 TRP A 298 22.571 -22.369 6.117 1.00 12.77 C ANISOU 2290 CE3 TRP A 298 1556 1706 1589 2 -25 -118 C ATOM 2291 CZ2 TRP A 298 24.254 -20.736 4.482 1.00 13.19 C ANISOU 2291 CZ2 TRP A 298 1467 1629 1916 -23 -110 -95 C ATOM 2292 CZ3 TRP A 298 23.937 -22.633 5.990 1.00 12.73 C ANISOU 2292 CZ3 TRP A 298 1518 1682 1636 -127 -40 -101 C ATOM 2293 CH2 TRP A 298 24.744 -21.803 5.207 1.00 13.09 C ANISOU 2293 CH2 TRP A 298 1552 1775 1645 -103 -62 28 C ATOM 2294 N HIS A 299 16.303 -22.269 5.174 1.00 9.47 N ANISOU 2294 N HIS A 299 1097 1051 1449 8 -21 -29 N ATOM 2295 CA HIS A 299 15.261 -23.227 5.511 1.00 10.55 C ANISOU 2295 CA HIS A 299 1333 1255 1419 -24 188 148 C ATOM 2296 C HIS A 299 14.224 -22.594 6.464 1.00 10.74 C ANISOU 2296 C HIS A 299 1332 1343 1406 6 97 15 C ATOM 2297 O HIS A 299 13.723 -21.510 6.171 1.00 11.17 O ANISOU 2297 O HIS A 299 1388 1380 1477 -17 163 81 O ATOM 2298 CB HIS A 299 15.865 -24.486 6.109 1.00 10.70 C ANISOU 2298 CB HIS A 299 1308 1235 1522 69 52 -13 C ATOM 2299 CG HIS A 299 16.838 -25.231 5.225 1.00 11.54 C ANISOU 2299 CG HIS A 299 1434 1376 1573 34 133 -16 C ATOM 2300 ND1 HIS A 299 16.528 -25.748 3.997 1.00 12.24 N ANISOU 2300 ND1 HIS A 299 1487 1565 1598 15 130 -33 N ATOM 2301 CD2 HIS A 299 18.136 -25.528 5.452 1.00 11.11 C ANISOU 2301 CD2 HIS A 299 1481 1239 1501 61 136 115 C ATOM 2302 CE1 HIS A 299 17.595 -26.402 3.503 1.00 12.19 C ANISOU 2302 CE1 HIS A 299 1502 1475 1655 -30 130 19 C ATOM 2303 NE2 HIS A 299 18.586 -26.258 4.349 1.00 11.78 N ANISOU 2303 NE2 HIS A 299 1590 1416 1470 148 134 90 N ATOM 2304 N GLU A 300 13.924 -23.254 7.584 1.00 10.85 N ANISOU 2304 N GLU A 300 1281 1402 1441 -106 124 47 N ATOM 2305 CA GLU A 300 12.921 -22.748 8.535 1.00 10.89 C ANISOU 2305 CA GLU A 300 1378 1286 1475 -97 77 -46 C ATOM 2306 C GLU A 300 13.475 -21.719 9.497 1.00 11.37 C ANISOU 2306 C GLU A 300 1411 1427 1481 -65 20 -44 C ATOM 2307 O GLU A 300 12.705 -21.231 10.348 1.00 11.45 O ANISOU 2307 O GLU A 300 1455 1457 1440 -191 90 -139 O ATOM 2308 CB GLU A 300 12.271 -23.950 9.263 1.00 12.24 C ANISOU 2308 CB GLU A 300 1597 1503 1550 -87 122 137 C ATOM 2309 CG GLU A 300 11.285 -24.718 8.353 1.00 13.82 C ANISOU 2309 CG GLU A 300 1685 1617 1949 -136 -36 109 C ATOM 2310 CD GLU A 300 11.885 -25.369 7.134 1.00 17.09 C ANISOU 2310 CD GLU A 300 2151 2099 2243 180 36 -14 C ATOM 2311 OE1 GLU A 300 12.879 -26.160 7.196 1.00 15.60 O ANISOU 2311 OE1 GLU A 300 1817 1809 2301 -12 -9 86 O ATOM 2312 OE2 GLU A 300 11.492 -25.131 5.931 1.00 19.99 O ANISOU 2312 OE2 GLU A 300 2617 2459 2520 217 -255 55 O ATOM 2313 N ARG A 301 14.745 -21.337 9.378 1.00 10.53 N ANISOU 2313 N ARG A 301 1336 1318 1347 -31 22 69 N ATOM 2314 CA ARG A 301 15.332 -20.095 9.844 1.00 10.61 C ANISOU 2314 CA ARG A 301 1336 1399 1297 14 -26 -58 C ATOM 2315 C ARG A 301 16.822 -20.279 10.154 1.00 10.97 C ANISOU 2315 C ARG A 301 1317 1391 1462 -70 24 -7 C ATOM 2316 O ARG A 301 17.271 -21.396 10.486 1.00 11.19 O ANISOU 2316 O ARG A 301 1346 1193 1713 -189 -30 -82 O ATOM 2317 CB ARG A 301 14.717 -19.409 11.072 1.00 10.10 C ANISOU 2317 CB ARG A 301 1123 1435 1279 63 41 2 C ATOM 2318 CG ARG A 301 14.921 -20.137 12.410 1.00 11.12 C ANISOU 2318 CG ARG A 301 1313 1553 1358 38 -49 78 C ATOM 2319 CD ARG A 301 16.153 -19.700 13.181 1.00 11.78 C ANISOU 2319 CD ARG A 301 1447 1511 1519 -82 -79 -11 C ATOM 2320 NE ARG A 301 16.035 -18.256 13.547 1.00 12.29 N ANISOU 2320 NE ARG A 301 1614 1456 1601 2 -22 92 N ATOM 2321 CZ ARG A 301 15.331 -17.784 14.553 1.00 13.17 C ANISOU 2321 CZ ARG A 301 1702 1542 1758 -49 131 63 C ATOM 2322 NH1 ARG A 301 14.626 -18.542 15.407 1.00 12.30 N ANISOU 2322 NH1 ARG A 301 1550 1572 1553 -69 56 113 N ATOM 2323 NH2 ARG A 301 15.254 -16.449 14.740 1.00 13.41 N ANISOU 2323 NH2 ARG A 301 1675 1519 1901 -227 60 117 N ATOM 2324 N ASP A 302 17.594 -19.179 10.034 1.00 11.09 N ANISOU 2324 N ASP A 302 1420 1305 1490 -68 6 -4 N ATOM 2325 CA ASP A 302 18.864 -19.135 10.767 1.00 10.98 C ANISOU 2325 CA ASP A 302 1292 1329 1552 -42 46 3 C ATOM 2326 C ASP A 302 18.791 -17.851 11.613 1.00 11.46 C ANISOU 2326 C ASP A 302 1432 1389 1534 -27 53 42 C ATOM 2327 O ASP A 302 17.814 -17.122 11.426 1.00 12.28 O ANISOU 2327 O ASP A 302 1525 1339 1799 20 28 183 O ATOM 2328 CB ASP A 302 20.029 -19.156 9.767 1.00 11.22 C ANISOU 2328 CB ASP A 302 1344 1381 1537 -35 41 16 C ATOM 2329 CG ASP A 302 20.125 -17.922 8.879 1.00 12.89 C ANISOU 2329 CG ASP A 302 1637 1576 1686 -63 3 76 C ATOM 2330 OD1 ASP A 302 20.416 -16.847 9.427 1.00 13.35 O ANISOU 2330 OD1 ASP A 302 1856 1380 1837 -29 -13 114 O ATOM 2331 OD2 ASP A 302 19.932 -18.050 7.642 1.00 12.95 O ANISOU 2331 OD2 ASP A 302 1584 1652 1684 -10 21 -20 O ATOM 2332 N ILE A 303 19.695 -17.588 12.533 1.00 11.41 N ANISOU 2332 N ILE A 303 1468 1392 1474 -98 26 139 N ATOM 2333 CA ILE A 303 19.556 -16.426 13.408 1.00 13.48 C ANISOU 2333 CA ILE A 303 1761 1561 1801 -5 72 2 C ATOM 2334 C ILE A 303 20.447 -15.269 12.989 1.00 11.71 C ANISOU 2334 C ILE A 303 1434 1539 1476 63 -60 -18 C ATOM 2335 O ILE A 303 20.567 -14.258 13.724 1.00 11.96 O ANISOU 2335 O ILE A 303 1526 1354 1665 50 -34 84 O ATOM 2336 CB ILE A 303 19.735 -16.905 14.863 1.00 17.77 C ANISOU 2336 CB ILE A 303 2357 2409 1985 37 -129 59 C ATOM 2337 CG1 ILE A 303 19.030 -15.880 15.745 1.00 22.19 C ANISOU 2337 CG1 ILE A 303 2975 2781 2674 178 116 -91 C ATOM 2338 CG2 ILE A 303 21.222 -17.081 15.178 1.00 17.56 C ANISOU 2338 CG2 ILE A 303 2307 2173 2194 124 25 24 C ATOM 2339 CD1 ILE A 303 18.220 -16.350 16.929 1.00 25.40 C ANISOU 2339 CD1 ILE A 303 3223 3358 3070 -90 225 153 C ATOM 2340 N SER A 304 20.926 -15.239 11.746 1.00 10.05 N ANISOU 2340 N SER A 304 1185 1192 1440 -22 -75 80 N ATOM 2341 CA SER A 304 21.774 -14.127 11.283 1.00 9.92 C ANISOU 2341 CA SER A 304 1208 1219 1345 24 -43 65 C ATOM 2342 C SER A 304 21.049 -12.784 11.375 1.00 10.37 C ANISOU 2342 C SER A 304 1229 1288 1424 60 5 -48 C ATOM 2343 O SER A 304 21.692 -11.781 11.694 1.00 10.89 O ANISOU 2343 O SER A 304 1196 1425 1517 -7 31 -19 O ATOM 2344 CB SER A 304 22.262 -14.349 9.842 1.00 10.78 C ANISOU 2344 CB SER A 304 1284 1388 1423 -70 81 17 C ATOM 2345 OG SER A 304 21.128 -14.423 8.980 1.00 11.34 O ANISOU 2345 OG SER A 304 1545 1526 1239 -136 79 139 O ATOM 2346 N HIS A 305 19.741 -12.771 11.106 1.00 10.10 N ANISOU 2346 N HIS A 305 1196 1278 1365 134 -26 23 N ATOM 2347 CA HIS A 305 18.967 -11.518 11.197 1.00 9.89 C ANISOU 2347 CA HIS A 305 1156 1289 1313 39 -53 55 C ATOM 2348 C HIS A 305 18.943 -10.919 12.591 1.00 9.82 C ANISOU 2348 C HIS A 305 1086 1302 1341 -50 -10 12 C ATOM 2349 O HIS A 305 18.746 -9.715 12.712 1.00 10.51 O ANISOU 2349 O HIS A 305 1138 1365 1490 75 -149 31 O ATOM 2350 CB HIS A 305 17.524 -11.826 10.680 1.00 9.12 C ANISOU 2350 CB HIS A 305 1012 1249 1203 -4 77 48 C ATOM 2351 CG HIS A 305 16.806 -12.709 11.675 1.00 10.45 C ANISOU 2351 CG HIS A 305 1405 1089 1475 -70 29 211 C ATOM 2352 ND1 HIS A 305 16.838 -14.077 11.694 1.00 12.28 N ANISOU 2352 ND1 HIS A 305 1627 1248 1790 -105 82 175 N ATOM 2353 CD2 HIS A 305 16.008 -12.338 12.732 1.00 9.30 C ANISOU 2353 CD2 HIS A 305 1415 600 1517 -93 11 109 C ATOM 2354 CE1 HIS A 305 16.131 -14.547 12.735 1.00 10.17 C ANISOU 2354 CE1 HIS A 305 1310 807 1748 -76 67 264 C ATOM 2355 NE2 HIS A 305 15.637 -13.520 13.381 1.00 12.04 N ANISOU 2355 NE2 HIS A 305 1683 1080 1811 -230 186 247 N ATOM 2356 N SER A 306 19.112 -11.703 13.662 1.00 9.89 N ANISOU 2356 N SER A 306 1145 1306 1305 -5 -52 60 N ATOM 2357 CA SER A 306 18.838 -11.212 15.024 1.00 12.18 C ANISOU 2357 CA SER A 306 1568 1603 1455 14 -76 -57 C ATOM 2358 C SER A 306 19.877 -10.158 15.382 1.00 12.49 C ANISOU 2358 C SER A 306 1638 1528 1579 2 -51 55 C ATOM 2359 O SER A 306 19.528 -9.104 15.889 1.00 13.04 O ANISOU 2359 O SER A 306 1690 1702 1564 35 -211 -14 O ATOM 2360 CB SER A 306 18.901 -12.387 16.016 1.00 15.82 C ANISOU 2360 CB SER A 306 2290 2011 1709 164 -6 180 C ATOM 2361 OG SER A 306 18.896 -11.852 17.354 1.00 19.83 O ANISOU 2361 OG SER A 306 2764 2544 2228 -42 -76 -214 O ATOM 2362 N SER A 307 21.155 -10.399 15.093 1.00 12.49 N ANISOU 2362 N SER A 307 1550 1432 1764 27 -171 117 N ATOM 2363 CA SER A 307 22.154 -9.376 15.369 1.00 14.69 C ANISOU 2363 CA SER A 307 1770 1674 2138 -99 -127 96 C ATOM 2364 C SER A 307 21.912 -8.091 14.552 1.00 15.19 C ANISOU 2364 C SER A 307 1995 1897 1878 86 -177 109 C ATOM 2365 O SER A 307 22.046 -7.005 15.120 1.00 16.78 O ANISOU 2365 O SER A 307 2358 1896 2121 -18 -367 162 O ATOM 2366 CB SER A 307 23.545 -9.925 15.121 1.00 15.18 C ANISOU 2366 CB SER A 307 1790 1997 1980 -103 13 50 C ATOM 2367 OG SER A 307 23.713 -10.333 13.787 1.00 15.74 O ANISOU 2367 OG SER A 307 1793 2228 1958 -205 -161 -78 O ATOM 2368 N VAL A 308 21.519 -8.198 13.275 1.00 12.91 N ANISOU 2368 N VAL A 308 1561 1603 1739 123 -3 28 N ATOM 2369 CA VAL A 308 21.230 -6.995 12.495 1.00 11.16 C ANISOU 2369 CA VAL A 308 1223 1595 1421 170 18 -13 C ATOM 2370 C VAL A 308 20.067 -6.257 13.160 1.00 10.18 C ANISOU 2370 C VAL A 308 1203 1367 1297 28 52 -5 C ATOM 2371 O VAL A 308 20.113 -5.029 13.334 1.00 10.36 O ANISOU 2371 O VAL A 308 1227 1415 1293 -170 -19 -60 O ATOM 2372 CB VAL A 308 20.879 -7.361 11.043 1.00 11.20 C ANISOU 2372 CB VAL A 308 1374 1418 1464 220 23 -38 C ATOM 2373 CG1 VAL A 308 20.407 -6.114 10.241 1.00 10.78 C ANISOU 2373 CG1 VAL A 308 1369 1396 1329 38 -6 63 C ATOM 2374 CG2 VAL A 308 22.094 -8.031 10.358 1.00 12.29 C ANISOU 2374 CG2 VAL A 308 1227 1853 1589 77 65 -167 C ATOM 2375 N GLU A 309 18.986 -6.962 13.529 1.00 9.45 N ANISOU 2375 N GLU A 309 1120 1315 1156 84 46 0 N ATOM 2376 CA GLU A 309 17.773 -6.260 13.987 1.00 9.23 C ANISOU 2376 CA GLU A 309 1082 1204 1221 -22 -1 -74 C ATOM 2377 C GLU A 309 18.003 -5.623 15.355 1.00 9.52 C ANISOU 2377 C GLU A 309 1258 1132 1228 63 -62 -56 C ATOM 2378 O GLU A 309 17.320 -4.653 15.723 1.00 8.19 O ANISOU 2378 O GLU A 309 1131 875 1106 -20 -40 42 O ATOM 2379 CB GLU A 309 16.630 -7.311 14.038 1.00 9.37 C ANISOU 2379 CB GLU A 309 1080 1221 1261 -44 51 -42 C ATOM 2380 CG GLU A 309 16.250 -7.685 12.598 1.00 9.98 C ANISOU 2380 CG GLU A 309 1267 1270 1255 -170 -32 17 C ATOM 2381 CD GLU A 309 15.355 -8.917 12.508 1.00 11.61 C ANISOU 2381 CD GLU A 309 1466 1427 1518 -176 -13 -19 C ATOM 2382 OE1 GLU A 309 15.187 -9.640 13.508 1.00 11.83 O ANISOU 2382 OE1 GLU A 309 1582 1477 1438 -83 21 -60 O ATOM 2383 OE2 GLU A 309 14.828 -9.131 11.390 1.00 12.76 O ANISOU 2383 OE2 GLU A 309 1503 1644 1702 -201 -88 -214 O ATOM 2384 N ARG A 310 19.011 -6.096 16.120 1.00 10.43 N ANISOU 2384 N ARG A 310 1220 1273 1470 146 -110 89 N ATOM 2385 CA ARG A 310 19.352 -5.438 17.379 1.00 12.33 C ANISOU 2385 CA ARG A 310 1578 1569 1537 98 -104 -38 C ATOM 2386 C ARG A 310 19.856 -4.020 17.124 1.00 12.15 C ANISOU 2386 C ARG A 310 1529 1608 1480 104 -92 -24 C ATOM 2387 O ARG A 310 19.645 -3.145 17.989 1.00 13.21 O ANISOU 2387 O ARG A 310 1851 1941 1226 229 -183 -136 O ATOM 2388 CB ARG A 310 20.438 -6.153 18.201 1.00 15.37 C ANISOU 2388 CB ARG A 310 1856 2051 1932 260 -175 176 C ATOM 2389 CG ARG A 310 19.935 -7.474 18.786 1.00 20.03 C ANISOU 2389 CG ARG A 310 2485 2351 2775 -57 6 144 C ATOM 2390 CD ARG A 310 21.097 -8.068 19.640 1.00 25.32 C ANISOU 2390 CD ARG A 310 3044 3465 3111 237 -269 152 C ATOM 2391 NE ARG A 310 20.596 -9.288 20.195 1.00 29.41 N ANISOU 2391 NE ARG A 310 3603 3767 3807 37 -152 234 N ATOM 2392 CZ ARG A 310 20.467 -10.559 19.997 1.00 33.30 C ANISOU 2392 CZ ARG A 310 4265 4040 4347 -8 -124 12 C ATOM 2393 NH1 ARG A 310 20.925 -11.237 18.922 1.00 34.32 N ANISOU 2393 NH1 ARG A 310 4288 4561 4191 71 -81 61 N ATOM 2394 NH2 ARG A 310 19.825 -11.198 21.006 1.00 35.84 N ANISOU 2394 NH2 ARG A 310 4502 4637 4476 -62 40 147 N ATOM 2395 N TYR A 311 20.525 -3.764 16.021 1.00 12.46 N ANISOU 2395 N TYR A 311 1616 1663 1454 -12 -36 -64 N ATOM 2396 CA TYR A 311 20.873 -2.377 15.671 1.00 13.60 C ANISOU 2396 CA TYR A 311 1839 1572 1755 26 -97 -83 C ATOM 2397 C TYR A 311 19.671 -1.705 15.021 1.00 13.12 C ANISOU 2397 C TYR A 311 1804 1604 1578 7 -7 -85 C ATOM 2398 O TYR A 311 19.245 -0.631 15.461 1.00 15.35 O ANISOU 2398 O TYR A 311 2187 1645 2002 69 -33 -180 O ATOM 2399 CB TYR A 311 22.017 -2.344 14.656 1.00 16.33 C ANISOU 2399 CB TYR A 311 2056 2068 2081 -175 81 -15 C ATOM 2400 CG TYR A 311 23.334 -2.853 15.200 1.00 20.51 C ANISOU 2400 CG TYR A 311 2402 2697 2694 -3 -68 121 C ATOM 2401 CD1 TYR A 311 23.656 -4.177 15.271 1.00 21.55 C ANISOU 2401 CD1 TYR A 311 2634 2695 2859 -1 95 -53 C ATOM 2402 CD2 TYR A 311 24.278 -1.911 15.649 1.00 23.36 C ANISOU 2402 CD2 TYR A 311 2839 2884 3153 -198 -111 49 C ATOM 2403 CE1 TYR A 311 24.861 -4.603 15.794 1.00 23.99 C ANISOU 2403 CE1 TYR A 311 2907 3080 3129 83 -79 18 C ATOM 2404 CE2 TYR A 311 25.506 -2.336 16.157 1.00 25.26 C ANISOU 2404 CE2 TYR A 311 2973 3163 3460 -115 -129 169 C ATOM 2405 CZ TYR A 311 25.781 -3.682 16.226 1.00 25.93 C ANISOU 2405 CZ TYR A 311 3111 3198 3545 -51 -41 48 C ATOM 2406 OH TYR A 311 26.988 -4.107 16.744 1.00 29.05 O ANISOU 2406 OH TYR A 311 3266 3751 4022 -65 -106 345 O ATOM 2407 N VAL A 312 19.131 -2.325 13.971 1.00 10.56 N ANISOU 2407 N VAL A 312 1211 1373 1428 -76 95 98 N ATOM 2408 CA VAL A 312 18.261 -1.598 13.051 1.00 11.12 C ANISOU 2408 CA VAL A 312 1303 1484 1439 -20 40 53 C ATOM 2409 C VAL A 312 16.915 -1.254 13.668 1.00 11.25 C ANISOU 2409 C VAL A 312 1369 1452 1454 -24 49 42 C ATOM 2410 O VAL A 312 16.449 -0.116 13.457 1.00 12.10 O ANISOU 2410 O VAL A 312 1474 1510 1613 63 54 -3 O ATOM 2411 CB VAL A 312 18.118 -2.424 11.757 1.00 12.41 C ANISOU 2411 CB VAL A 312 1446 1829 1442 79 135 -11 C ATOM 2412 CG1 VAL A 312 17.110 -1.832 10.787 1.00 13.28 C ANISOU 2412 CG1 VAL A 312 1675 1773 1598 37 6 19 C ATOM 2413 CG2 VAL A 312 19.465 -2.486 11.010 1.00 12.24 C ANISOU 2413 CG2 VAL A 312 1329 1837 1484 -4 68 -28 C ATOM 2414 N PHE A 313 16.275 -2.187 14.370 1.00 10.95 N ANISOU 2414 N PHE A 313 1301 1443 1415 -51 105 57 N ATOM 2415 CA PHE A 313 14.900 -1.884 14.850 1.00 11.45 C ANISOU 2415 CA PHE A 313 1399 1358 1594 -6 98 -40 C ATOM 2416 C PHE A 313 14.877 -0.644 15.751 1.00 11.03 C ANISOU 2416 C PHE A 313 1439 1307 1446 14 60 33 C ATOM 2417 O PHE A 313 14.123 0.315 15.497 1.00 11.23 O ANISOU 2417 O PHE A 313 1494 1320 1453 6 -91 127 O ATOM 2418 CB PHE A 313 14.231 -3.100 15.475 1.00 11.10 C ANISOU 2418 CB PHE A 313 1393 1435 1390 -39 124 -32 C ATOM 2419 CG PHE A 313 13.825 -4.238 14.571 1.00 11.79 C ANISOU 2419 CG PHE A 313 1429 1482 1571 21 27 -74 C ATOM 2420 CD1 PHE A 313 13.323 -5.417 15.098 1.00 11.62 C ANISOU 2420 CD1 PHE A 313 1330 1520 1563 36 40 -31 C ATOM 2421 CD2 PHE A 313 13.952 -4.139 13.183 1.00 11.89 C ANISOU 2421 CD2 PHE A 313 1464 1537 1515 42 -7 -73 C ATOM 2422 CE1 PHE A 313 12.947 -6.472 14.278 1.00 12.10 C ANISOU 2422 CE1 PHE A 313 1323 1660 1616 -7 -4 -37 C ATOM 2423 CE2 PHE A 313 13.566 -5.195 12.341 1.00 11.69 C ANISOU 2423 CE2 PHE A 313 1320 1512 1611 16 -41 -48 C ATOM 2424 CZ PHE A 313 13.077 -6.361 12.892 1.00 11.31 C ANISOU 2424 CZ PHE A 313 1205 1510 1583 84 -48 -70 C ATOM 2425 N PRO A 314 15.640 -0.586 16.841 1.00 10.83 N ANISOU 2425 N PRO A 314 1393 1224 1498 -153 10 -22 N ATOM 2426 CA PRO A 314 15.642 0.560 17.726 1.00 11.27 C ANISOU 2426 CA PRO A 314 1544 1297 1442 -57 7 -42 C ATOM 2427 C PRO A 314 16.265 1.761 17.023 1.00 11.25 C ANISOU 2427 C PRO A 314 1432 1311 1533 -85 -41 -2 C ATOM 2428 O PRO A 314 15.772 2.889 17.226 1.00 11.48 O ANISOU 2428 O PRO A 314 1430 1349 1580 -74 41 -141 O ATOM 2429 CB PRO A 314 16.459 0.166 18.953 1.00 12.42 C ANISOU 2429 CB PRO A 314 1727 1419 1575 -16 -110 25 C ATOM 2430 CG PRO A 314 17.008 -1.201 18.680 1.00 14.19 C ANISOU 2430 CG PRO A 314 1968 1704 1720 120 -129 -213 C ATOM 2431 CD PRO A 314 16.467 -1.694 17.373 1.00 12.22 C ANISOU 2431 CD PRO A 314 1634 1399 1611 -37 -123 -35 C ATOM 2432 N ASP A 315 17.325 1.538 16.218 1.00 11.44 N ANISOU 2432 N ASP A 315 1543 1395 1410 -114 -20 -94 N ATOM 2433 CA ASP A 315 18.009 2.720 15.660 1.00 12.15 C ANISOU 2433 CA ASP A 315 1608 1528 1481 -68 -62 150 C ATOM 2434 C ASP A 315 17.236 3.388 14.524 1.00 11.25 C ANISOU 2434 C ASP A 315 1370 1503 1402 -72 -31 11 C ATOM 2435 O ASP A 315 17.175 4.622 14.502 1.00 12.39 O ANISOU 2435 O ASP A 315 1515 1597 1594 71 -164 122 O ATOM 2436 CB ASP A 315 19.449 2.429 15.226 1.00 14.66 C ANISOU 2436 CB ASP A 315 1728 1857 1986 -33 72 57 C ATOM 2437 CG ASP A 315 20.357 2.080 16.376 1.00 19.35 C ANISOU 2437 CG ASP A 315 2264 2677 2411 36 -163 113 C ATOM 2438 OD1 ASP A 315 19.989 2.160 17.564 1.00 23.20 O ANISOU 2438 OD1 ASP A 315 2925 3425 2465 129 -218 41 O ATOM 2439 OD2 ASP A 315 21.515 1.674 16.178 1.00 22.69 O ANISOU 2439 OD2 ASP A 315 2340 3193 3089 145 -237 129 O ATOM 2440 N ALA A 316 16.557 2.671 13.656 1.00 10.22 N ANISOU 2440 N ALA A 316 1269 1303 1312 -152 110 90 N ATOM 2441 CA ALA A 316 15.843 3.229 12.515 1.00 10.69 C ANISOU 2441 CA ALA A 316 1312 1329 1419 -5 -35 -139 C ATOM 2442 C ALA A 316 14.636 4.002 13.070 1.00 10.26 C ANISOU 2442 C ALA A 316 1399 1100 1398 19 34 -8 C ATOM 2443 O ALA A 316 14.365 5.129 12.623 1.00 8.42 O ANISOU 2443 O ALA A 316 1191 888 1120 -227 322 164 O ATOM 2444 CB ALA A 316 15.416 2.122 11.524 1.00 9.00 C ANISOU 2444 CB ALA A 316 1172 1055 1194 -154 135 89 C ATOM 2445 N THR A 317 13.969 3.382 14.048 1.00 9.85 N ANISOU 2445 N THR A 317 1347 1251 1144 -33 -16 -81 N ATOM 2446 CA THR A 317 12.708 4.004 14.518 1.00 10.56 C ANISOU 2446 CA THR A 317 1336 1308 1369 -67 -31 -41 C ATOM 2447 C THR A 317 13.057 5.236 15.355 1.00 10.64 C ANISOU 2447 C THR A 317 1424 1229 1389 -45 -42 -8 C ATOM 2448 O THR A 317 12.354 6.243 15.251 1.00 10.26 O ANISOU 2448 O THR A 317 1199 1340 1357 -94 -108 19 O ATOM 2449 CB THR A 317 11.817 3.058 15.330 1.00 11.45 C ANISOU 2449 CB THR A 317 1426 1458 1469 -166 -116 25 C ATOM 2450 OG1 THR A 317 12.537 2.455 16.439 1.00 11.56 O ANISOU 2450 OG1 THR A 317 1563 1249 1580 -111 -89 158 O ATOM 2451 CG2 THR A 317 11.263 1.941 14.430 1.00 11.34 C ANISOU 2451 CG2 THR A 317 1339 1383 1587 -160 35 -63 C ATOM 2452 N GLN A 318 14.109 5.153 16.184 1.00 10.44 N ANISOU 2452 N GLN A 318 1424 1223 1320 -99 -44 -15 N ATOM 2453 CA GLN A 318 14.435 6.329 17.026 1.00 10.59 C ANISOU 2453 CA GLN A 318 1501 1171 1352 -136 -19 70 C ATOM 2454 C GLN A 318 14.982 7.476 16.160 1.00 10.10 C ANISOU 2454 C GLN A 318 1328 1192 1317 -43 38 73 C ATOM 2455 O GLN A 318 14.679 8.645 16.385 1.00 10.18 O ANISOU 2455 O GLN A 318 1463 1176 1230 -97 -147 66 O ATOM 2456 CB GLN A 318 15.465 5.934 18.098 1.00 12.12 C ANISOU 2456 CB GLN A 318 1608 1553 1443 -15 -126 -19 C ATOM 2457 CG GLN A 318 14.765 5.061 19.168 1.00 14.66 C ANISOU 2457 CG GLN A 318 2010 1700 1859 -45 34 82 C ATOM 2458 CD GLN A 318 15.732 4.729 20.285 1.00 17.57 C ANISOU 2458 CD GLN A 318 2292 2260 2125 -11 -143 73 C ATOM 2459 OE1 GLN A 318 15.968 5.557 21.157 1.00 20.97 O ANISOU 2459 OE1 GLN A 318 2922 2759 2287 31 -123 -146 O ATOM 2460 NE2 GLN A 318 16.343 3.560 20.238 1.00 18.64 N ANISOU 2460 NE2 GLN A 318 2359 2478 2243 173 -171 100 N ATOM 2461 N THR A 319 15.802 7.105 15.179 1.00 9.27 N ANISOU 2461 N THR A 319 1324 1171 1028 -2 -43 166 N ATOM 2462 CA THR A 319 16.408 8.138 14.312 1.00 9.59 C ANISOU 2462 CA THR A 319 1278 1162 1206 -74 -17 172 C ATOM 2463 C THR A 319 15.298 8.855 13.556 1.00 9.65 C ANISOU 2463 C THR A 319 1188 1073 1404 -57 -75 41 C ATOM 2464 O THR A 319 15.258 10.096 13.428 1.00 9.52 O ANISOU 2464 O THR A 319 1221 1050 1346 -60 -99 17 O ATOM 2465 CB THR A 319 17.423 7.505 13.345 1.00 10.14 C ANISOU 2465 CB THR A 319 1363 1169 1320 3 46 229 C ATOM 2466 OG1 THR A 319 18.531 7.115 14.217 1.00 11.79 O ANISOU 2466 OG1 THR A 319 1367 1467 1646 16 -127 72 O ATOM 2467 CG2 THR A 319 18.052 8.541 12.412 1.00 11.08 C ANISOU 2467 CG2 THR A 319 1507 1379 1324 -138 211 144 C ATOM 2468 N LEU A 320 14.383 8.067 12.940 1.00 9.21 N ANISOU 2468 N LEU A 320 974 1282 1244 -180 -43 167 N ATOM 2469 CA LEU A 320 13.345 8.758 12.150 1.00 10.01 C ANISOU 2469 CA LEU A 320 1056 1368 1381 -108 -167 -9 C ATOM 2470 C LEU A 320 12.453 9.623 13.033 1.00 9.82 C ANISOU 2470 C LEU A 320 1325 1214 1193 -151 -124 -20 C ATOM 2471 O LEU A 320 12.035 10.694 12.605 1.00 8.21 O ANISOU 2471 O LEU A 320 967 1181 972 -75 79 4 O ATOM 2472 CB LEU A 320 12.482 7.733 11.413 1.00 11.05 C ANISOU 2472 CB LEU A 320 1452 1423 1324 -275 -196 -47 C ATOM 2473 CG LEU A 320 11.797 8.104 10.110 1.00 13.03 C ANISOU 2473 CG LEU A 320 1564 1633 1754 -363 -409 112 C ATOM 2474 CD1 LEU A 320 10.492 7.380 9.786 1.00 9.31 C ANISOU 2474 CD1 LEU A 320 844 1391 1304 1 -146 201 C ATOM 2475 CD2 LEU A 320 11.934 9.438 9.472 1.00 12.92 C ANISOU 2475 CD2 LEU A 320 1543 1468 1898 15 -508 52 C ATOM 2476 N TYR A 321 12.129 9.145 14.247 1.00 9.60 N ANISOU 2476 N TYR A 321 1167 1168 1314 -175 189 -18 N ATOM 2477 CA TYR A 321 11.290 9.969 15.142 1.00 10.01 C ANISOU 2477 CA TYR A 321 1328 1134 1342 -87 87 -30 C ATOM 2478 C TYR A 321 12.032 11.264 15.470 1.00 10.04 C ANISOU 2478 C TYR A 321 1246 1123 1447 -71 13 48 C ATOM 2479 O TYR A 321 11.421 12.339 15.375 1.00 10.26 O ANISOU 2479 O TYR A 321 1194 1132 1571 -94 49 -12 O ATOM 2480 CB TYR A 321 11.016 9.154 16.414 1.00 10.24 C ANISOU 2480 CB TYR A 321 1351 1176 1363 -61 110 -28 C ATOM 2481 CG TYR A 321 10.172 9.929 17.415 1.00 12.09 C ANISOU 2481 CG TYR A 321 1691 1390 1511 69 191 -52 C ATOM 2482 CD1 TYR A 321 8.861 10.208 17.060 1.00 13.14 C ANISOU 2482 CD1 TYR A 321 1639 1636 1717 -5 272 -1 C ATOM 2483 CD2 TYR A 321 10.740 10.352 18.616 1.00 13.04 C ANISOU 2483 CD2 TYR A 321 1926 1473 1554 21 71 22 C ATOM 2484 CE1 TYR A 321 8.069 10.951 17.978 1.00 14.26 C ANISOU 2484 CE1 TYR A 321 1867 1640 1909 13 246 -128 C ATOM 2485 CE2 TYR A 321 9.929 11.061 19.511 1.00 15.36 C ANISOU 2485 CE2 TYR A 321 2062 1902 1872 92 196 -40 C ATOM 2486 CZ TYR A 321 8.627 11.337 19.162 1.00 15.82 C ANISOU 2486 CZ TYR A 321 2097 1995 1918 49 154 -24 C ATOM 2487 OH TYR A 321 7.813 12.077 20.022 1.00 18.36 O ANISOU 2487 OH TYR A 321 2444 2309 2222 117 233 -272 O ATOM 2488 N TYR A 322 13.344 11.181 15.776 1.00 9.81 N ANISOU 2488 N TYR A 322 1258 1179 1290 -186 28 113 N ATOM 2489 CA TYR A 322 14.104 12.429 15.972 1.00 9.87 C ANISOU 2489 CA TYR A 322 1189 1187 1373 -130 20 94 C ATOM 2490 C TYR A 322 14.023 13.315 14.723 1.00 9.42 C ANISOU 2490 C TYR A 322 1107 1187 1286 -80 -36 41 C ATOM 2491 O TYR A 322 13.855 14.551 14.879 1.00 10.12 O ANISOU 2491 O TYR A 322 1447 1179 1221 14 49 141 O ATOM 2492 CB TYR A 322 15.568 12.105 16.323 1.00 10.54 C ANISOU 2492 CB TYR A 322 1270 1266 1468 -82 -104 2 C ATOM 2493 CG TYR A 322 16.417 13.372 16.451 1.00 11.84 C ANISOU 2493 CG TYR A 322 1469 1287 1742 -111 -54 33 C ATOM 2494 CD1 TYR A 322 16.509 13.983 17.701 1.00 13.82 C ANISOU 2494 CD1 TYR A 322 1738 1658 1855 -104 -28 -124 C ATOM 2495 CD2 TYR A 322 17.104 13.853 15.345 1.00 11.77 C ANISOU 2495 CD2 TYR A 322 1357 1391 1724 -23 -31 23 C ATOM 2496 CE1 TYR A 322 17.277 15.164 17.821 1.00 14.94 C ANISOU 2496 CE1 TYR A 322 1852 1722 2104 -148 51 -89 C ATOM 2497 CE2 TYR A 322 17.861 15.032 15.465 1.00 13.61 C ANISOU 2497 CE2 TYR A 322 1615 1535 2020 -182 -45 -21 C ATOM 2498 CZ TYR A 322 17.919 15.647 16.703 1.00 15.25 C ANISOU 2498 CZ TYR A 322 1899 1815 2080 -136 87 -92 C ATOM 2499 OH TYR A 322 18.678 16.802 16.824 1.00 17.95 O ANISOU 2499 OH TYR A 322 2182 2034 2603 -264 119 -280 O ATOM 2500 N MET A 323 14.142 12.747 13.527 1.00 8.97 N ANISOU 2500 N MET A 323 928 1262 1219 -117 69 129 N ATOM 2501 CA MET A 323 14.133 13.561 12.296 1.00 9.31 C ANISOU 2501 CA MET A 323 1125 1281 1133 -59 15 -6 C ATOM 2502 C MET A 323 12.796 14.264 12.136 1.00 9.07 C ANISOU 2502 C MET A 323 1183 1057 1206 -85 15 -1 C ATOM 2503 O MET A 323 12.730 15.427 11.723 1.00 9.46 O ANISOU 2503 O MET A 323 1160 1075 1361 24 29 182 O ATOM 2504 CB MET A 323 14.411 12.702 11.050 1.00 8.81 C ANISOU 2504 CB MET A 323 913 1351 1082 144 157 -20 C ATOM 2505 CG MET A 323 15.859 12.186 10.905 1.00 6.49 C ANISOU 2505 CG MET A 323 810 1346 311 77 156 -42 C ATOM 2506 SD MET A 323 16.103 11.078 9.472 1.00 2.36 S ANISOU 2506 SD MET A 323 381 259 256 -25 18 -4 S ATOM 2507 CE MET A 323 16.047 12.322 8.167 1.00 7.77 C ANISOU 2507 CE MET A 323 1316 1014 623 47 -243 121 C ATOM 2508 N ILE A 324 11.701 13.515 12.359 1.00 9.38 N ANISOU 2508 N ILE A 324 1082 1264 1218 -107 145 62 N ATOM 2509 CA ILE A 324 10.367 14.103 12.104 1.00 9.35 C ANISOU 2509 CA ILE A 324 1087 1200 1265 -115 65 -36 C ATOM 2510 C ILE A 324 10.092 15.220 13.096 1.00 10.20 C ANISOU 2510 C ILE A 324 1159 1226 1489 -100 80 -72 C ATOM 2511 O ILE A 324 9.687 16.321 12.702 1.00 10.96 O ANISOU 2511 O ILE A 324 1227 1260 1679 -51 73 2 O ATOM 2512 CB ILE A 324 9.273 13.021 12.238 1.00 9.49 C ANISOU 2512 CB ILE A 324 1089 1095 1422 -103 56 -147 C ATOM 2513 CG1 ILE A 324 9.386 12.024 11.050 1.00 9.12 C ANISOU 2513 CG1 ILE A 324 1026 1068 1373 -141 33 -128 C ATOM 2514 CG2 ILE A 324 7.891 13.698 12.254 1.00 10.23 C ANISOU 2514 CG2 ILE A 324 1088 1276 1522 -28 33 -126 C ATOM 2515 CD1 ILE A 324 8.557 10.741 11.287 1.00 10.47 C ANISOU 2515 CD1 ILE A 324 1227 1210 1540 -185 230 -38 C ATOM 2516 N VAL A 325 10.323 14.942 14.387 1.00 11.02 N ANISOU 2516 N VAL A 325 1280 1396 1513 -110 121 -2 N ATOM 2517 CA VAL A 325 10.072 15.979 15.411 1.00 12.44 C ANISOU 2517 CA VAL A 325 1643 1448 1636 -121 70 -83 C ATOM 2518 C VAL A 325 10.927 17.221 15.173 1.00 11.50 C ANISOU 2518 C VAL A 325 1441 1439 1489 -34 13 67 C ATOM 2519 O VAL A 325 10.464 18.365 15.261 1.00 11.82 O ANISOU 2519 O VAL A 325 1487 1514 1492 33 118 35 O ATOM 2520 CB VAL A 325 10.344 15.412 16.821 1.00 13.88 C ANISOU 2520 CB VAL A 325 1925 1598 1749 -154 116 14 C ATOM 2521 CG1 VAL A 325 10.291 16.501 17.884 1.00 15.73 C ANISOU 2521 CG1 VAL A 325 2235 1799 1944 -87 105 -77 C ATOM 2522 CG2 VAL A 325 9.278 14.337 17.098 1.00 14.59 C ANISOU 2522 CG2 VAL A 325 1746 1827 1971 -89 354 -76 C ATOM 2523 N THR A 326 12.198 17.006 14.828 1.00 10.74 N ANISOU 2523 N THR A 326 1407 1349 1324 -44 -13 149 N ATOM 2524 CA THR A 326 13.141 18.098 14.606 1.00 11.01 C ANISOU 2524 CA THR A 326 1373 1297 1512 -28 26 75 C ATOM 2525 C THR A 326 12.779 18.902 13.366 1.00 11.02 C ANISOU 2525 C THR A 326 1410 1314 1461 10 -29 -1 C ATOM 2526 O THR A 326 12.733 20.139 13.413 1.00 10.94 O ANISOU 2526 O THR A 326 1426 1248 1482 -36 -5 54 O ATOM 2527 CB THR A 326 14.564 17.527 14.461 1.00 11.14 C ANISOU 2527 CB THR A 326 1333 1345 1556 -88 43 102 C ATOM 2528 OG1 THR A 326 14.923 16.897 15.709 1.00 11.59 O ANISOU 2528 OG1 THR A 326 1433 1386 1583 -8 -143 -29 O ATOM 2529 CG2 THR A 326 15.599 18.630 14.216 1.00 12.27 C ANISOU 2529 CG2 THR A 326 1546 1329 1789 -175 167 35 C ATOM 2530 N ALA A 327 12.480 18.208 12.242 1.00 11.04 N ANISOU 2530 N ALA A 327 1355 1472 1369 18 32 -25 N ATOM 2531 CA ALA A 327 12.053 18.908 11.037 1.00 10.57 C ANISOU 2531 CA ALA A 327 1313 1364 1341 53 56 -47 C ATOM 2532 C ALA A 327 10.779 19.709 11.288 1.00 10.46 C ANISOU 2532 C ALA A 327 1293 1296 1385 -11 13 -54 C ATOM 2533 O ALA A 327 10.601 20.781 10.694 1.00 10.93 O ANISOU 2533 O ALA A 327 1321 1295 1535 57 -16 15 O ATOM 2534 CB ALA A 327 11.794 17.942 9.849 1.00 11.94 C ANISOU 2534 CB ALA A 327 1522 1602 1414 -8 -61 -136 C ATOM 2535 N THR A 328 9.867 19.135 12.076 1.00 10.75 N ANISOU 2535 N THR A 328 1374 1370 1340 28 118 -127 N ATOM 2536 CA THR A 328 8.625 19.870 12.366 1.00 11.08 C ANISOU 2536 CA THR A 328 1315 1382 1514 38 56 -81 C ATOM 2537 C THR A 328 8.969 21.207 13.041 1.00 11.73 C ANISOU 2537 C THR A 328 1536 1332 1591 0 42 1 C ATOM 2538 O THR A 328 8.412 22.258 12.701 1.00 12.27 O ANISOU 2538 O THR A 328 1475 1531 1656 230 -20 -85 O ATOM 2539 CB THR A 328 7.731 19.023 13.283 1.00 11.37 C ANISOU 2539 CB THR A 328 1302 1315 1702 68 105 -51 C ATOM 2540 OG1 THR A 328 7.398 17.768 12.652 1.00 11.30 O ANISOU 2540 OG1 THR A 328 1342 1344 1608 40 29 -6 O ATOM 2541 CG2 THR A 328 6.411 19.736 13.581 1.00 11.78 C ANISOU 2541 CG2 THR A 328 1262 1374 1840 89 195 -22 C ATOM 2542 N ASN A 329 9.856 21.179 14.036 1.00 12.28 N ANISOU 2542 N ASN A 329 1637 1469 1559 -76 -24 -34 N ATOM 2543 CA ASN A 329 10.218 22.447 14.721 1.00 14.31 C ANISOU 2543 CA ASN A 329 1933 1570 1935 -158 74 -66 C ATOM 2544 C ASN A 329 10.958 23.373 13.766 1.00 13.24 C ANISOU 2544 C ASN A 329 1591 1702 1739 -26 5 4 C ATOM 2545 O ASN A 329 10.721 24.586 13.807 1.00 13.36 O ANISOU 2545 O ASN A 329 1545 1645 1885 -135 177 -109 O ATOM 2546 CB ASN A 329 11.095 22.171 15.956 1.00 18.29 C ANISOU 2546 CB ASN A 329 2425 2393 2130 -20 -66 78 C ATOM 2547 CG ASN A 329 11.446 23.501 16.624 1.00 23.04 C ANISOU 2547 CG ASN A 329 3119 2811 2825 -120 -54 -187 C ATOM 2548 OD1 ASN A 329 12.552 24.068 16.603 1.00 26.49 O ANISOU 2548 OD1 ASN A 329 3133 3653 3279 -210 -106 -42 O ATOM 2549 ND2 ASN A 329 10.399 24.098 17.185 1.00 25.57 N ANISOU 2549 ND2 ASN A 329 3214 3355 3146 -2 113 -207 N ATOM 2550 N VAL A 330 11.860 22.850 12.923 1.00 12.28 N ANISOU 2550 N VAL A 330 1648 1495 1522 35 -71 21 N ATOM 2551 CA VAL A 330 12.495 23.727 11.930 1.00 12.16 C ANISOU 2551 CA VAL A 330 1418 1591 1610 50 40 7 C ATOM 2552 C VAL A 330 11.455 24.468 11.087 1.00 12.37 C ANISOU 2552 C VAL A 330 1545 1473 1683 51 -41 11 C ATOM 2553 O VAL A 330 11.504 25.708 10.955 1.00 13.39 O ANISOU 2553 O VAL A 330 1610 1507 1970 -46 28 50 O ATOM 2554 CB VAL A 330 13.444 22.895 11.034 1.00 12.22 C ANISOU 2554 CB VAL A 330 1538 1562 1543 90 51 80 C ATOM 2555 CG1 VAL A 330 13.977 23.700 9.834 1.00 12.71 C ANISOU 2555 CG1 VAL A 330 1784 1544 1501 112 134 42 C ATOM 2556 CG2 VAL A 330 14.607 22.449 11.929 1.00 11.02 C ANISOU 2556 CG2 VAL A 330 1296 1412 1477 72 95 8 C ATOM 2557 N VAL A 331 10.492 23.756 10.501 1.00 11.53 N ANISOU 2557 N VAL A 331 1261 1536 1583 159 62 -6 N ATOM 2558 CA VAL A 331 9.584 24.387 9.532 1.00 12.30 C ANISOU 2558 CA VAL A 331 1475 1629 1570 90 -63 -24 C ATOM 2559 C VAL A 331 8.601 25.290 10.299 1.00 12.84 C ANISOU 2559 C VAL A 331 1653 1557 1668 39 -26 -104 C ATOM 2560 O VAL A 331 8.283 26.394 9.850 1.00 13.72 O ANISOU 2560 O VAL A 331 1649 1688 1878 140 -27 -28 O ATOM 2561 CB VAL A 331 8.800 23.321 8.746 1.00 12.73 C ANISOU 2561 CB VAL A 331 1679 1530 1628 75 -29 -79 C ATOM 2562 CG1 VAL A 331 7.728 23.988 7.860 1.00 14.01 C ANISOU 2562 CG1 VAL A 331 1843 1601 1877 73 -171 -77 C ATOM 2563 CG2 VAL A 331 9.765 22.539 7.862 1.00 13.12 C ANISOU 2563 CG2 VAL A 331 1806 1505 1675 56 89 13 C ATOM 2564 N ARG A 332 8.177 24.845 11.475 1.00 12.65 N ANISOU 2564 N ARG A 332 1648 1499 1660 -117 5 -194 N ATOM 2565 CA ARG A 332 7.298 25.659 12.308 1.00 14.35 C ANISOU 2565 CA ARG A 332 1771 1742 1938 33 114 -129 C ATOM 2566 C ARG A 332 7.911 27.020 12.647 1.00 14.49 C ANISOU 2566 C ARG A 332 1806 1726 1974 0 54 -24 C ATOM 2567 O ARG A 332 7.177 28.035 12.629 1.00 15.22 O ANISOU 2567 O ARG A 332 1860 1687 2235 -16 153 -87 O ATOM 2568 CB ARG A 332 6.951 24.937 13.627 1.00 16.10 C ANISOU 2568 CB ARG A 332 2099 1989 2028 33 144 1 C ATOM 2569 CG ARG A 332 5.779 25.679 14.334 1.00 19.19 C ANISOU 2569 CG ARG A 332 2352 2393 2547 158 234 -108 C ATOM 2570 CD ARG A 332 5.668 25.134 15.736 1.00 23.08 C ANISOU 2570 CD ARG A 332 3057 3102 2612 106 165 -33 C ATOM 2571 NE ARG A 332 5.450 23.702 15.919 1.00 25.48 N ANISOU 2571 NE ARG A 332 3466 3213 3003 55 234 -99 N ATOM 2572 CZ ARG A 332 4.289 23.069 15.843 1.00 27.42 C ANISOU 2572 CZ ARG A 332 3639 3488 3291 -46 134 -146 C ATOM 2573 NH1 ARG A 332 3.175 23.741 15.532 1.00 29.53 N ANISOU 2573 NH1 ARG A 332 3685 3959 3574 37 53 -140 N ATOM 2574 NH2 ARG A 332 4.156 21.763 16.068 1.00 28.24 N ANISOU 2574 NH2 ARG A 332 3960 3491 3277 54 312 -46 N ATOM 2575 N ASN A 333 9.184 27.050 13.021 1.00 14.46 N ANISOU 2575 N ASN A 333 1800 1792 1902 -12 57 -87 N ATOM 2576 CA ASN A 333 9.779 28.256 13.615 1.00 15.27 C ANISOU 2576 CA ASN A 333 2017 1886 1900 -130 70 -50 C ATOM 2577 C ASN A 333 10.824 28.911 12.734 1.00 14.71 C ANISOU 2577 C ASN A 333 1997 1703 1891 -123 7 -137 C ATOM 2578 O ASN A 333 11.406 29.945 13.132 1.00 14.45 O ANISOU 2578 O ASN A 333 1979 1566 1945 -256 6 -46 O ATOM 2579 CB ASN A 333 10.410 27.877 14.976 1.00 16.90 C ANISOU 2579 CB ASN A 333 2129 2178 2113 1 -79 -55 C ATOM 2580 CG ASN A 333 9.291 27.509 15.960 1.00 19.36 C ANISOU 2580 CG ASN A 333 2430 2517 2408 -12 98 39 C ATOM 2581 OD1 ASN A 333 8.320 28.252 16.102 1.00 20.05 O ANISOU 2581 OD1 ASN A 333 2403 2663 2550 -19 208 -107 O ATOM 2582 ND2 ASN A 333 9.395 26.347 16.587 1.00 20.25 N ANISOU 2582 ND2 ASN A 333 2721 2615 2357 -145 62 91 N ATOM 2583 N MET A 334 11.050 28.396 11.533 1.00 13.38 N ANISOU 2583 N MET A 334 1830 1569 1685 60 -8 -15 N ATOM 2584 CA MET A 334 12.049 29.048 10.674 1.00 14.11 C ANISOU 2584 CA MET A 334 2108 1553 1700 -14 119 -55 C ATOM 2585 C MET A 334 11.580 30.478 10.342 1.00 14.61 C ANISOU 2585 C MET A 334 2039 1648 1864 44 44 -64 C ATOM 2586 O MET A 334 10.383 30.772 10.179 1.00 14.94 O ANISOU 2586 O MET A 334 1972 1676 2027 -39 95 -28 O ATOM 2587 CB MET A 334 12.307 28.263 9.386 1.00 13.99 C ANISOU 2587 CB MET A 334 2125 1528 1665 47 -49 -162 C ATOM 2588 CG MET A 334 11.164 28.112 8.420 1.00 11.94 C ANISOU 2588 CG MET A 334 1843 1266 1429 155 122 -299 C ATOM 2589 SD MET A 334 11.514 27.001 6.950 1.00 7.98 S ANISOU 2589 SD MET A 334 1224 649 1160 146 285 -325 S ATOM 2590 CE MET A 334 9.871 27.147 6.211 1.00 15.09 C ANISOU 2590 CE MET A 334 1814 2028 1893 0 -76 -6 C ATOM 2591 N LYS A 335 12.567 31.378 10.225 1.00 14.54 N ANISOU 2591 N LYS A 335 2137 1599 1787 -32 44 -86 N ATOM 2592 CA LYS A 335 12.268 32.704 9.681 1.00 15.84 C ANISOU 2592 CA LYS A 335 2309 1696 2012 -58 -131 -21 C ATOM 2593 C LYS A 335 12.205 32.678 8.160 1.00 15.93 C ANISOU 2593 C LYS A 335 2110 1912 2031 9 -71 17 C ATOM 2594 O LYS A 335 13.068 32.049 7.529 1.00 17.72 O ANISOU 2594 O LYS A 335 2335 2208 2191 217 -1 -46 O ATOM 2595 CB LYS A 335 13.377 33.677 10.104 1.00 17.52 C ANISOU 2595 CB LYS A 335 2061 1967 2627 -160 -103 49 C ATOM 2596 N VAL A 336 11.233 33.338 7.582 1.00 14.43 N ANISOU 2596 N VAL A 336 1997 1505 1980 -4 30 54 N ATOM 2597 CA VAL A 336 11.044 33.366 6.132 1.00 14.87 C ANISOU 2597 CA VAL A 336 1973 1699 1978 -31 87 18 C ATOM 2598 C VAL A 336 11.186 34.838 5.707 1.00 14.79 C ANISOU 2598 C VAL A 336 1958 1754 1907 70 106 73 C ATOM 2599 O VAL A 336 10.410 35.672 6.183 1.00 14.59 O ANISOU 2599 O VAL A 336 1958 1643 1941 119 133 103 O ATOM 2600 CB VAL A 336 9.675 32.808 5.719 1.00 15.30 C ANISOU 2600 CB VAL A 336 2023 1736 2056 0 8 33 C ATOM 2601 CG1 VAL A 336 9.418 32.963 4.241 1.00 15.97 C ANISOU 2601 CG1 VAL A 336 2168 1865 2033 82 75 100 C ATOM 2602 CG2 VAL A 336 9.639 31.298 6.083 1.00 14.57 C ANISOU 2602 CG2 VAL A 336 1768 1702 2065 -38 60 69 C ATOM 2603 N ASN A 337 12.174 35.128 4.881 1.00 14.69 N ANISOU 2603 N ASN A 337 1847 1846 1890 13 63 36 N ATOM 2604 CA ASN A 337 12.493 36.519 4.548 1.00 15.89 C ANISOU 2604 CA ASN A 337 2090 1931 2018 12 -32 73 C ATOM 2605 C ASN A 337 11.784 36.884 3.226 1.00 14.93 C ANISOU 2605 C ASN A 337 1804 1895 1974 46 7 21 C ATOM 2606 O ASN A 337 12.370 36.794 2.140 1.00 13.01 O ANISOU 2606 O ASN A 337 1565 1528 1849 121 -100 78 O ATOM 2607 CB ASN A 337 14.015 36.647 4.452 1.00 17.92 C ANISOU 2607 CB ASN A 337 2132 2366 2309 -2 9 -63 C ATOM 2608 CG ASN A 337 14.688 36.368 5.802 1.00 20.79 C ANISOU 2608 CG ASN A 337 2631 2750 2517 82 -103 9 C ATOM 2609 OD1 ASN A 337 14.119 36.711 6.863 1.00 21.70 O ANISOU 2609 OD1 ASN A 337 2724 2898 2622 86 -81 -106 O ATOM 2610 ND2 ASN A 337 15.876 35.752 5.818 1.00 21.59 N ANISOU 2610 ND2 ASN A 337 2619 2888 2695 84 -119 -166 N ATOM 2611 N GLU A 338 10.526 37.332 3.338 1.00 14.06 N ANISOU 2611 N GLU A 338 1743 1593 2006 53 -13 -2 N ATOM 2612 CA GLU A 338 9.729 37.469 2.109 1.00 15.00 C ANISOU 2612 CA GLU A 338 1873 1911 1916 23 22 -51 C ATOM 2613 C GLU A 338 10.301 38.565 1.223 1.00 14.65 C ANISOU 2613 C GLU A 338 1781 1822 1965 54 15 -92 C ATOM 2614 O GLU A 338 10.317 38.520 -0.033 1.00 13.98 O ANISOU 2614 O GLU A 338 1701 1695 1914 64 49 -187 O ATOM 2615 CB GLU A 338 8.274 37.807 2.467 1.00 17.02 C ANISOU 2615 CB GLU A 338 1931 2276 2258 94 7 -77 C ATOM 2616 CG GLU A 338 7.552 36.633 3.169 1.00 19.89 C ANISOU 2616 CG GLU A 338 2480 2455 2623 -60 124 19 C ATOM 2617 CD GLU A 338 6.067 36.988 3.284 1.00 23.83 C ANISOU 2617 CD GLU A 338 2737 3061 3257 135 133 -47 C ATOM 2618 OE1 GLU A 338 5.262 36.860 2.342 1.00 26.10 O ANISOU 2618 OE1 GLU A 338 3042 3304 3569 52 -34 -126 O ATOM 2619 OE2 GLU A 338 5.706 37.421 4.381 1.00 25.36 O ANISOU 2619 OE2 GLU A 338 2992 3262 3380 196 273 -101 O ATOM 2620 N GLU A 339 10.770 39.660 1.868 1.00 15.36 N ANISOU 2620 N GLU A 339 1966 1913 1959 55 -21 -232 N ATOM 2621 CA GLU A 339 11.260 40.756 1.024 1.00 18.02 C ANISOU 2621 CA GLU A 339 2231 2229 2387 42 131 3 C ATOM 2622 C GLU A 339 12.505 40.331 0.237 1.00 16.18 C ANISOU 2622 C GLU A 339 2182 1909 2055 98 -58 -29 C ATOM 2623 O GLU A 339 12.713 40.650 -0.943 1.00 15.01 O ANISOU 2623 O GLU A 339 2115 1436 2154 159 42 84 O ATOM 2624 CB GLU A 339 11.545 42.029 1.835 1.00 22.91 C ANISOU 2624 CB GLU A 339 2991 2720 2993 -112 -66 -342 C ATOM 2625 CG GLU A 339 11.951 43.162 0.882 1.00 29.59 C ANISOU 2625 CG GLU A 339 4008 3451 3782 -100 185 137 C ATOM 2626 CD GLU A 339 11.126 43.309 -0.387 1.00 34.17 C ANISOU 2626 CD GLU A 339 4447 4379 4159 43 -74 36 C ATOM 2627 OE1 GLU A 339 11.692 43.162 -1.520 1.00 33.81 O ANISOU 2627 OE1 GLU A 339 4418 4123 4305 141 141 64 O ATOM 2628 OE2 GLU A 339 9.883 43.570 -0.277 1.00 37.63 O ANISOU 2628 OE2 GLU A 339 4611 4755 4931 163 156 -43 O ATOM 2629 N ARG A 340 13.386 39.583 0.910 1.00 14.41 N ANISOU 2629 N ARG A 340 1933 1528 2014 43 -11 -20 N ATOM 2630 CA ARG A 340 14.554 39.066 0.201 1.00 15.03 C ANISOU 2630 CA ARG A 340 2002 1805 1904 57 68 -4 C ATOM 2631 C ARG A 340 14.191 38.126 -0.920 1.00 13.87 C ANISOU 2631 C ARG A 340 1705 1650 1915 22 -1 99 C ATOM 2632 O ARG A 340 14.778 38.153 -2.019 1.00 13.58 O ANISOU 2632 O ARG A 340 1822 1495 1844 70 15 1 O ATOM 2633 CB ARG A 340 15.498 38.384 1.233 1.00 17.54 C ANISOU 2633 CB ARG A 340 2271 2235 2158 62 -108 125 C ATOM 2634 CG ARG A 340 16.750 37.838 0.571 1.00 20.87 C ANISOU 2634 CG ARG A 340 2573 2717 2638 220 -14 -10 C ATOM 2635 CD ARG A 340 17.678 39.020 0.196 1.00 27.03 C ANISOU 2635 CD ARG A 340 3364 3294 3614 -269 -1 193 C ATOM 2636 NE ARG A 340 18.851 38.371 -0.363 1.00 32.90 N ANISOU 2636 NE ARG A 340 4036 4101 4365 52 146 -77 N ATOM 2637 CZ ARG A 340 20.122 38.716 -0.199 1.00 35.55 C ANISOU 2637 CZ ARG A 340 4197 4554 4757 -113 27 2 C ATOM 2638 NH1 ARG A 340 20.433 39.795 0.507 1.00 37.38 N ANISOU 2638 NH1 ARG A 340 4563 4781 4861 -168 -66 -139 N ATOM 2639 NH2 ARG A 340 21.020 37.963 -0.807 1.00 37.18 N ANISOU 2639 NH2 ARG A 340 4558 4539 5029 66 96 42 N ATOM 2640 N MET A 341 13.208 37.248 -0.718 1.00 13.25 N ANISOU 2640 N MET A 341 1741 1398 1896 58 -35 -11 N ATOM 2641 CA MET A 341 12.740 36.369 -1.788 1.00 12.08 C ANISOU 2641 CA MET A 341 1575 1310 1704 35 0 35 C ATOM 2642 C MET A 341 12.286 37.169 -3.014 1.00 14.07 C ANISOU 2642 C MET A 341 1990 1650 1705 134 76 46 C ATOM 2643 O MET A 341 12.589 36.807 -4.157 1.00 13.88 O ANISOU 2643 O MET A 341 1855 1833 1587 155 -52 38 O ATOM 2644 CB MET A 341 11.578 35.492 -1.304 1.00 11.61 C ANISOU 2644 CB MET A 341 1474 1378 1558 66 129 54 C ATOM 2645 CG MET A 341 11.959 34.429 -0.272 1.00 10.50 C ANISOU 2645 CG MET A 341 1274 1037 1680 -91 165 56 C ATOM 2646 SD MET A 341 10.472 33.446 0.346 1.00 7.01 S ANISOU 2646 SD MET A 341 554 281 1829 9 -13 -206 S ATOM 2647 CE MET A 341 11.412 32.155 1.219 1.00 12.48 C ANISOU 2647 CE MET A 341 1387 1457 1898 72 -94 144 C ATOM 2648 N LYS A 342 11.528 38.253 -2.749 1.00 13.92 N ANISOU 2648 N LYS A 342 1766 1636 1886 156 74 28 N ATOM 2649 CA LYS A 342 11.040 39.060 -3.858 1.00 15.94 C ANISOU 2649 CA LYS A 342 2075 1918 2061 119 -14 149 C ATOM 2650 C LYS A 342 12.196 39.739 -4.575 1.00 15.55 C ANISOU 2650 C LYS A 342 2013 1749 2146 228 44 32 C ATOM 2651 O LYS A 342 12.284 39.812 -5.802 1.00 16.01 O ANISOU 2651 O LYS A 342 2076 1869 2138 321 47 67 O ATOM 2652 CB LYS A 342 10.030 40.098 -3.318 1.00 18.66 C ANISOU 2652 CB LYS A 342 2372 2199 2520 139 116 -105 C ATOM 2653 CG LYS A 342 9.373 40.834 -4.483 1.00 23.50 C ANISOU 2653 CG LYS A 342 3026 2889 3012 192 -104 245 C ATOM 2654 CD LYS A 342 8.378 41.856 -3.894 1.00 28.48 C ANISOU 2654 CD LYS A 342 3535 3463 3822 281 149 -48 C ATOM 2655 CE LYS A 342 7.663 42.514 -5.087 1.00 31.78 C ANISOU 2655 CE LYS A 342 4032 3996 4048 173 -114 145 C ATOM 2656 NZ LYS A 342 6.462 43.255 -4.565 1.00 35.37 N ANISOU 2656 NZ LYS A 342 4317 4448 4676 288 59 -25 N ATOM 2657 N LYS A 343 13.135 40.282 -3.800 1.00 16.15 N ANISOU 2657 N LYS A 343 2013 1780 2342 166 22 37 N ATOM 2658 CA LYS A 343 14.282 40.995 -4.363 1.00 17.55 C ANISOU 2658 CA LYS A 343 2239 2023 2407 80 199 73 C ATOM 2659 C LYS A 343 15.187 40.061 -5.152 1.00 15.79 C ANISOU 2659 C LYS A 343 2076 1813 2113 28 41 133 C ATOM 2660 O LYS A 343 15.655 40.409 -6.252 1.00 15.80 O ANISOU 2660 O LYS A 343 2118 1716 2169 75 82 198 O ATOM 2661 CB LYS A 343 15.034 41.665 -3.216 1.00 21.62 C ANISOU 2661 CB LYS A 343 2925 2669 2621 21 -93 10 C ATOM 2662 CG LYS A 343 16.388 42.223 -3.565 1.00 26.16 C ANISOU 2662 CG LYS A 343 3193 3303 3443 -91 109 66 C ATOM 2663 CD LYS A 343 16.906 43.120 -2.431 1.00 30.69 C ANISOU 2663 CD LYS A 343 4070 3859 3733 -96 -97 -162 C ATOM 2664 CE LYS A 343 17.670 42.277 -1.425 1.00 33.48 C ANISOU 2664 CE LYS A 343 4375 4203 4145 33 -103 94 C ATOM 2665 N ASN A 344 15.324 38.814 -4.707 1.00 13.44 N ANISOU 2665 N ASN A 344 1649 1580 1876 -43 61 -25 N ATOM 2666 CA ASN A 344 16.175 37.866 -5.440 1.00 13.68 C ANISOU 2666 CA ASN A 344 1787 1578 1835 6 61 42 C ATOM 2667 C ASN A 344 15.602 37.525 -6.797 1.00 12.51 C ANISOU 2667 C ASN A 344 1637 1372 1745 -18 68 146 C ATOM 2668 O ASN A 344 16.358 37.182 -7.724 1.00 12.93 O ANISOU 2668 O ASN A 344 1832 1390 1692 141 61 219 O ATOM 2669 CB ASN A 344 16.375 36.577 -4.620 1.00 14.84 C ANISOU 2669 CB ASN A 344 1981 1659 2000 42 -26 148 C ATOM 2670 CG ASN A 344 17.405 36.749 -3.516 1.00 15.72 C ANISOU 2670 CG ASN A 344 1927 1821 2223 -93 -32 128 C ATOM 2671 OD1 ASN A 344 18.198 37.714 -3.526 1.00 17.14 O ANISOU 2671 OD1 ASN A 344 2084 1727 2702 -163 -195 108 O ATOM 2672 ND2 ASN A 344 17.438 35.824 -2.555 1.00 15.21 N ANISOU 2672 ND2 ASN A 344 1919 1785 2074 73 38 94 N ATOM 2673 N ILE A 345 14.304 37.667 -7.053 1.00 12.28 N ANISOU 2673 N ILE A 345 1710 1252 1702 50 76 162 N ATOM 2674 CA ILE A 345 13.775 37.492 -8.406 1.00 12.58 C ANISOU 2674 CA ILE A 345 1603 1417 1760 -112 -6 140 C ATOM 2675 C ILE A 345 14.447 38.489 -9.360 1.00 13.59 C ANISOU 2675 C ILE A 345 1856 1576 1733 -23 129 131 C ATOM 2676 O ILE A 345 14.648 38.151 -10.520 1.00 13.46 O ANISOU 2676 O ILE A 345 1902 1545 1666 17 63 196 O ATOM 2677 CB ILE A 345 12.258 37.660 -8.418 1.00 13.35 C ANISOU 2677 CB ILE A 345 1616 1658 1799 -9 71 156 C ATOM 2678 CG1 ILE A 345 11.606 36.532 -7.574 1.00 13.37 C ANISOU 2678 CG1 ILE A 345 1434 1656 1991 19 137 172 C ATOM 2679 CG2 ILE A 345 11.726 37.587 -9.862 1.00 14.36 C ANISOU 2679 CG2 ILE A 345 1855 1821 1779 -11 52 27 C ATOM 2680 CD1 ILE A 345 10.101 36.795 -7.304 1.00 13.55 C ANISOU 2680 CD1 ILE A 345 1430 1724 1995 25 166 139 C ATOM 2681 N ASP A 346 14.829 39.668 -8.854 1.00 13.99 N ANISOU 2681 N ASP A 346 1809 1534 1972 -36 53 83 N ATOM 2682 CA ASP A 346 15.362 40.689 -9.760 1.00 15.63 C ANISOU 2682 CA ASP A 346 2007 1757 2173 -48 119 148 C ATOM 2683 C ASP A 346 16.882 40.654 -9.747 1.00 15.80 C ANISOU 2683 C ASP A 346 2004 1773 2227 -2 21 85 C ATOM 2684 O ASP A 346 17.550 41.567 -10.254 1.00 16.38 O ANISOU 2684 O ASP A 346 2164 1677 2385 5 -25 252 O ATOM 2685 CB ASP A 346 14.827 42.070 -9.356 1.00 18.07 C ANISOU 2685 CB ASP A 346 2373 1875 2618 49 103 10 C ATOM 2686 CG ASP A 346 15.042 43.074 -10.483 1.00 21.68 C ANISOU 2686 CG ASP A 346 3025 2456 2758 -67 95 171 C ATOM 2687 OD1 ASP A 346 14.813 42.756 -11.665 1.00 21.90 O ANISOU 2687 OD1 ASP A 346 3047 2455 2821 -18 85 195 O ATOM 2688 OD2 ASP A 346 15.490 44.203 -10.136 1.00 24.12 O ANISOU 2688 OD2 ASP A 346 3463 2474 3229 -139 58 168 O ATOM 2689 N LEU A 347 17.487 39.592 -9.186 1.00 15.98 N ANISOU 2689 N LEU A 347 2077 1787 2209 26 -24 98 N ATOM 2690 CA LEU A 347 18.971 39.550 -9.179 1.00 17.38 C ANISOU 2690 CA LEU A 347 2118 2038 2447 18 -39 90 C ATOM 2691 C LEU A 347 19.562 39.636 -10.564 1.00 16.88 C ANISOU 2691 C LEU A 347 2086 1903 2424 44 -75 165 C ATOM 2692 O LEU A 347 20.625 40.253 -10.806 1.00 18.25 O ANISOU 2692 O LEU A 347 2227 2046 2661 -75 -65 271 O ATOM 2693 CB LEU A 347 19.404 38.264 -8.444 1.00 20.37 C ANISOU 2693 CB LEU A 347 2728 2171 2841 66 -83 210 C ATOM 2694 CG LEU A 347 20.882 38.048 -8.189 1.00 23.75 C ANISOU 2694 CG LEU A 347 2905 2797 3323 25 -202 173 C ATOM 2695 CD1 LEU A 347 21.471 39.206 -7.346 1.00 24.99 C ANISOU 2695 CD1 LEU A 347 3188 2792 3515 -17 -182 123 C ATOM 2696 CD2 LEU A 347 21.128 36.748 -7.419 1.00 24.68 C ANISOU 2696 CD2 LEU A 347 3096 2711 3569 59 -194 181 C ATOM 2697 N THR A 348 18.927 39.030 -11.570 1.00 15.35 N ANISOU 2697 N THR A 348 1992 1609 2232 210 -53 255 N ATOM 2698 CA THR A 348 19.415 39.051 -12.938 1.00 16.44 C ANISOU 2698 CA THR A 348 2178 1834 2234 122 -16 265 C ATOM 2699 C THR A 348 18.783 40.220 -13.721 1.00 17.11 C ANISOU 2699 C THR A 348 2309 1936 2254 123 -46 258 C ATOM 2700 O THR A 348 18.775 40.214 -14.951 1.00 18.23 O ANISOU 2700 O THR A 348 2633 2002 2293 136 -47 401 O ATOM 2701 CB THR A 348 19.183 37.743 -13.687 1.00 16.00 C ANISOU 2701 CB THR A 348 2039 1908 2132 167 -42 249 C ATOM 2702 OG1 THR A 348 17.783 37.426 -13.791 1.00 17.17 O ANISOU 2702 OG1 THR A 348 2091 1977 2456 67 15 295 O ATOM 2703 CG2 THR A 348 19.890 36.581 -12.955 1.00 15.86 C ANISOU 2703 CG2 THR A 348 2057 1784 2186 189 37 224 C ATOM 2704 N LYS A 349 18.190 41.176 -13.038 1.00 17.31 N ANISOU 2704 N LYS A 349 2229 1871 2479 17 -5 239 N ATOM 2705 CA LYS A 349 17.800 42.464 -13.584 1.00 17.66 C ANISOU 2705 CA LYS A 349 2228 2002 2482 26 -17 300 C ATOM 2706 C LYS A 349 16.781 42.334 -14.695 1.00 17.77 C ANISOU 2706 C LYS A 349 2306 2058 2387 -109 -9 219 C ATOM 2707 O LYS A 349 16.725 43.146 -15.637 1.00 18.64 O ANISOU 2707 O LYS A 349 2496 2137 2451 -71 53 330 O ATOM 2708 CB LYS A 349 19.034 43.277 -14.027 1.00 18.68 C ANISOU 2708 CB LYS A 349 2373 2093 2630 -103 47 280 C ATOM 2709 CG LYS A 349 20.033 43.484 -12.901 1.00 21.23 C ANISOU 2709 CG LYS A 349 2721 2627 2721 -115 -30 89 C ATOM 2710 CD LYS A 349 20.995 44.657 -13.147 1.00 22.63 C ANISOU 2710 CD LYS A 349 2902 2707 2988 -180 20 15 C ATOM 2711 CE LYS A 349 21.821 44.511 -14.416 1.00 23.79 C ANISOU 2711 CE LYS A 349 3011 2958 3071 -105 76 42 C ATOM 2712 NZ LYS A 349 22.898 43.491 -14.280 1.00 24.99 N ANISOU 2712 NZ LYS A 349 3107 3067 3322 -58 52 118 N ATOM 2713 N GLY A 350 15.858 41.368 -14.564 1.00 16.60 N ANISOU 2713 N GLY A 350 2156 1954 2197 1 -22 333 N ATOM 2714 CA GLY A 350 14.798 41.183 -15.543 1.00 16.43 C ANISOU 2714 CA GLY A 350 2024 1932 2286 7 7 186 C ATOM 2715 C GLY A 350 14.958 40.033 -16.494 1.00 16.43 C ANISOU 2715 C GLY A 350 1958 2026 2259 60 4 161 C ATOM 2716 O GLY A 350 14.024 39.648 -17.215 1.00 16.53 O ANISOU 2716 O GLY A 350 1817 1931 2531 58 -10 270 O ATOM 2717 N LEU A 351 16.125 39.359 -16.498 1.00 15.61 N ANISOU 2717 N LEU A 351 1954 1695 2281 56 35 305 N ATOM 2718 CA LEU A 351 16.380 38.293 -17.460 1.00 16.90 C ANISOU 2718 CA LEU A 351 2108 2150 2165 -30 46 147 C ATOM 2719 C LEU A 351 15.538 37.061 -17.230 1.00 17.12 C ANISOU 2719 C LEU A 351 2139 2100 2264 -9 -39 99 C ATOM 2720 O LEU A 351 15.317 36.213 -18.092 1.00 16.37 O ANISOU 2720 O LEU A 351 2054 1953 2211 124 -36 137 O ATOM 2721 CB LEU A 351 17.884 37.937 -17.403 1.00 17.43 C ANISOU 2721 CB LEU A 351 2093 2247 2281 35 110 143 C ATOM 2722 CG LEU A 351 18.807 39.035 -17.988 1.00 18.42 C ANISOU 2722 CG LEU A 351 2105 2496 2398 -53 74 168 C ATOM 2723 CD1 LEU A 351 20.267 38.593 -17.902 1.00 18.37 C ANISOU 2723 CD1 LEU A 351 2100 2510 2371 2 107 190 C ATOM 2724 CD2 LEU A 351 18.433 39.303 -19.442 1.00 19.57 C ANISOU 2724 CD2 LEU A 351 2331 2679 2424 9 29 208 C ATOM 2725 N VAL A 352 14.934 36.919 -16.040 1.00 17.83 N ANISOU 2725 N VAL A 352 2172 2292 2310 63 -3 205 N ATOM 2726 CA VAL A 352 13.997 35.818 -15.790 1.00 18.53 C ANISOU 2726 CA VAL A 352 2249 2319 2470 15 -95 107 C ATOM 2727 C VAL A 352 12.781 35.912 -16.707 1.00 18.48 C ANISOU 2727 C VAL A 352 2313 2313 2396 56 -45 76 C ATOM 2728 O VAL A 352 12.084 34.923 -16.923 1.00 19.10 O ANISOU 2728 O VAL A 352 2353 2313 2590 146 -173 8 O ATOM 2729 CB VAL A 352 13.610 35.974 -14.303 1.00 20.96 C ANISOU 2729 CB VAL A 352 2653 2785 2526 -49 -54 136 C ATOM 2730 CG1 VAL A 352 12.284 35.356 -14.000 1.00 24.52 C ANISOU 2730 CG1 VAL A 352 2766 3410 3140 -133 25 82 C ATOM 2731 CG2 VAL A 352 14.704 35.434 -13.374 1.00 19.13 C ANISOU 2731 CG2 VAL A 352 2448 2341 2481 9 41 21 C ATOM 2732 N PHE A 353 12.470 37.084 -17.259 1.00 17.77 N ANISOU 2732 N PHE A 353 2190 2291 2269 189 29 118 N ATOM 2733 CA PHE A 353 11.378 37.198 -18.216 1.00 18.04 C ANISOU 2733 CA PHE A 353 2272 2234 2349 124 -34 -7 C ATOM 2734 C PHE A 353 11.829 37.084 -19.665 1.00 19.30 C ANISOU 2734 C PHE A 353 2424 2493 2416 128 11 -9 C ATOM 2735 O PHE A 353 11.037 37.365 -20.578 1.00 19.41 O ANISOU 2735 O PHE A 353 2317 2510 2547 400 1 6 O ATOM 2736 CB PHE A 353 10.734 38.591 -18.012 1.00 17.84 C ANISOU 2736 CB PHE A 353 2301 2130 2347 85 8 89 C ATOM 2737 CG PHE A 353 10.277 38.761 -16.586 1.00 17.58 C ANISOU 2737 CG PHE A 353 2244 2045 2390 118 37 32 C ATOM 2738 CD1 PHE A 353 11.000 39.528 -15.696 1.00 18.02 C ANISOU 2738 CD1 PHE A 353 2145 2300 2401 92 -23 48 C ATOM 2739 CD2 PHE A 353 9.126 38.101 -16.167 1.00 17.66 C ANISOU 2739 CD2 PHE A 353 2267 2007 2435 113 21 72 C ATOM 2740 CE1 PHE A 353 10.588 39.680 -14.388 1.00 19.08 C ANISOU 2740 CE1 PHE A 353 2291 2495 2466 41 54 -10 C ATOM 2741 CE2 PHE A 353 8.712 38.231 -14.848 1.00 18.69 C ANISOU 2741 CE2 PHE A 353 2465 2228 2408 25 -21 85 C ATOM 2742 CZ PHE A 353 9.439 39.015 -13.967 1.00 19.43 C ANISOU 2742 CZ PHE A 353 2498 2334 2550 -88 9 35 C ATOM 2743 N SER A 354 13.067 36.643 -19.935 1.00 20.45 N ANISOU 2743 N SER A 354 2408 2613 2749 186 0 131 N ATOM 2744 CA SER A 354 13.555 36.625 -21.312 1.00 21.54 C ANISOU 2744 CA SER A 354 2612 2773 2799 200 72 79 C ATOM 2745 C SER A 354 12.762 35.721 -22.233 1.00 22.93 C ANISOU 2745 C SER A 354 2747 2974 2992 162 48 -50 C ATOM 2746 O SER A 354 12.594 36.083 -23.427 1.00 24.12 O ANISOU 2746 O SER A 354 2938 3091 3134 206 -21 82 O ATOM 2747 CB SER A 354 15.073 36.285 -21.373 1.00 21.88 C ANISOU 2747 CB SER A 354 2610 2801 2903 117 59 83 C ATOM 2748 OG SER A 354 15.194 34.918 -20.994 1.00 21.75 O ANISOU 2748 OG SER A 354 2423 2818 3022 264 68 27 O ATOM 2749 N GLN A 355 12.229 34.588 -21.781 1.00 23.54 N ANISOU 2749 N GLN A 355 2871 3031 3044 212 97 82 N ATOM 2750 CA GLN A 355 11.413 33.763 -22.683 1.00 26.53 C ANISOU 2750 CA GLN A 355 3130 3569 3383 168 -56 -84 C ATOM 2751 C GLN A 355 10.109 34.455 -23.093 1.00 24.85 C ANISOU 2751 C GLN A 355 3139 3227 3075 129 21 -6 C ATOM 2752 O GLN A 355 9.670 34.275 -24.233 1.00 25.05 O ANISOU 2752 O GLN A 355 3042 3297 3181 166 -144 1 O ATOM 2753 CB GLN A 355 11.130 32.397 -22.084 1.00 31.02 C ANISOU 2753 CB GLN A 355 3943 3868 3975 140 93 183 C ATOM 2754 CG GLN A 355 10.467 31.383 -22.985 1.00 36.78 C ANISOU 2754 CG GLN A 355 4612 4596 4765 -81 -192 -108 C ATOM 2755 CD GLN A 355 11.219 31.000 -24.239 1.00 40.91 C ANISOU 2755 CD GLN A 355 5220 5242 5081 49 79 -109 C ATOM 2756 OE1 GLN A 355 12.440 31.146 -24.402 1.00 42.40 O ANISOU 2756 OE1 GLN A 355 5236 5389 5486 28 5 -78 O ATOM 2757 NE2 GLN A 355 10.483 30.463 -25.223 1.00 43.30 N ANISOU 2757 NE2 GLN A 355 5467 5557 5429 -24 -146 -156 N ATOM 2758 N ARG A 356 9.479 35.222 -22.201 1.00 22.37 N ANISOU 2758 N ARG A 356 2780 2800 2917 112 -61 164 N ATOM 2759 CA ARG A 356 8.292 35.977 -22.641 1.00 21.31 C ANISOU 2759 CA ARG A 356 2736 2708 2654 60 49 88 C ATOM 2760 C ARG A 356 8.660 36.998 -23.716 1.00 21.70 C ANISOU 2760 C ARG A 356 2797 2767 2681 2 24 122 C ATOM 2761 O ARG A 356 7.861 37.174 -24.657 1.00 22.15 O ANISOU 2761 O ARG A 356 2789 2971 2656 -105 -3 228 O ATOM 2762 CB ARG A 356 7.664 36.691 -21.438 1.00 20.28 C ANISOU 2762 CB ARG A 356 2592 2506 2607 39 85 146 C ATOM 2763 CG ARG A 356 7.244 35.680 -20.359 1.00 19.77 C ANISOU 2763 CG ARG A 356 2622 2390 2498 30 84 80 C ATOM 2764 CD ARG A 356 6.049 36.252 -19.583 1.00 19.64 C ANISOU 2764 CD ARG A 356 2513 2441 2510 -33 57 135 C ATOM 2765 NE ARG A 356 4.862 36.312 -20.436 1.00 19.68 N ANISOU 2765 NE ARG A 356 2452 2494 2531 -110 64 136 N ATOM 2766 CZ ARG A 356 3.825 37.100 -20.277 1.00 20.64 C ANISOU 2766 CZ ARG A 356 2613 2590 2639 -41 3 81 C ATOM 2767 NH1 ARG A 356 2.782 37.035 -21.121 1.00 21.40 N ANISOU 2767 NH1 ARG A 356 2627 2734 2770 -49 -47 101 N ATOM 2768 NH2 ARG A 356 3.787 37.947 -19.264 1.00 20.21 N ANISOU 2768 NH2 ARG A 356 2522 2542 2615 -46 51 76 N ATOM 2769 N VAL A 357 9.789 37.679 -23.532 1.00 22.19 N ANISOU 2769 N VAL A 357 2767 2860 2804 2 45 132 N ATOM 2770 CA VAL A 357 10.198 38.669 -24.551 1.00 23.26 C ANISOU 2770 CA VAL A 357 2876 2980 2981 -95 12 190 C ATOM 2771 C VAL A 357 10.440 37.954 -25.873 1.00 25.54 C ANISOU 2771 C VAL A 357 3210 3348 3146 -56 38 46 C ATOM 2772 O VAL A 357 9.955 38.388 -26.932 1.00 26.70 O ANISOU 2772 O VAL A 357 3258 3574 3311 33 -59 108 O ATOM 2773 CB VAL A 357 11.421 39.481 -24.107 1.00 21.78 C ANISOU 2773 CB VAL A 357 2841 2717 2718 -38 54 131 C ATOM 2774 CG1 VAL A 357 11.894 40.444 -25.205 1.00 21.62 C ANISOU 2774 CG1 VAL A 357 2668 2900 2646 -45 -17 173 C ATOM 2775 CG2 VAL A 357 11.118 40.305 -22.850 1.00 20.79 C ANISOU 2775 CG2 VAL A 357 2655 2596 2647 35 21 195 C ATOM 2776 N LEU A 358 11.190 36.860 -25.884 1.00 27.07 N ANISOU 2776 N LEU A 358 3355 3413 3516 -5 -23 141 N ATOM 2777 CA LEU A 358 11.469 36.109 -27.091 1.00 29.65 C ANISOU 2777 CA LEU A 358 3765 3842 3657 -22 22 -37 C ATOM 2778 C LEU A 358 10.177 35.742 -27.830 1.00 30.38 C ANISOU 2778 C LEU A 358 3748 3980 3815 32 -40 42 C ATOM 2779 O LEU A 358 10.032 35.951 -29.039 1.00 30.93 O ANISOU 2779 O LEU A 358 3785 4157 3812 67 -15 13 O ATOM 2780 CB LEU A 358 12.251 34.824 -26.792 1.00 31.29 C ANISOU 2780 CB LEU A 358 3958 3984 3946 50 -84 80 C ATOM 2781 CG LEU A 358 13.086 34.268 -27.957 1.00 33.88 C ANISOU 2781 CG LEU A 358 4297 4371 4204 110 26 -67 C ATOM 2782 CD1 LEU A 358 14.055 33.196 -27.472 1.00 35.02 C ANISOU 2782 CD1 LEU A 358 4490 4398 4420 153 12 -39 C ATOM 2783 CD2 LEU A 358 12.220 33.619 -29.014 1.00 35.34 C ANISOU 2783 CD2 LEU A 358 4467 4547 4413 7 -43 -87 C ATOM 2784 N LEU A 359 9.235 35.158 -27.108 1.00 30.18 N ANISOU 2784 N LEU A 359 3780 3943 3742 58 -15 36 N ATOM 2785 CA LEU A 359 7.960 34.765 -27.669 1.00 31.13 C ANISOU 2785 CA LEU A 359 3919 4026 3881 7 -67 -33 C ATOM 2786 C LEU A 359 7.153 35.932 -28.211 1.00 30.55 C ANISOU 2786 C LEU A 359 3826 3990 3793 -24 13 19 C ATOM 2787 O LEU A 359 6.568 35.736 -29.292 1.00 30.39 O ANISOU 2787 O LEU A 359 3766 3980 3799 18 -28 18 O ATOM 2788 CB LEU A 359 7.139 33.940 -26.664 1.00 32.58 C ANISOU 2788 CB LEU A 359 4172 4229 3977 -70 3 -4 C ATOM 2789 CG LEU A 359 7.929 32.666 -26.293 1.00 34.80 C ANISOU 2789 CG LEU A 359 4465 4369 4389 48 -38 -16 C ATOM 2790 CD1 LEU A 359 7.203 31.829 -25.267 1.00 35.89 C ANISOU 2790 CD1 LEU A 359 4588 4585 4464 -38 43 -1 C ATOM 2791 CD2 LEU A 359 8.247 31.847 -27.550 1.00 35.95 C ANISOU 2791 CD2 LEU A 359 4601 4611 4447 58 4 -83 C ATOM 2792 N LYS A 360 7.158 37.065 -27.533 1.00 30.01 N ANISOU 2792 N LYS A 360 3758 3982 3664 -90 70 26 N ATOM 2793 CA LYS A 360 6.418 38.220 -28.043 1.00 31.64 C ANISOU 2793 CA LYS A 360 3900 4124 3997 19 -30 67 C ATOM 2794 C LYS A 360 6.998 38.684 -29.381 1.00 33.33 C ANISOU 2794 C LYS A 360 4189 4426 4047 21 4 85 C ATOM 2795 O LYS A 360 6.257 39.003 -30.317 1.00 33.37 O ANISOU 2795 O LYS A 360 4066 4581 4033 8 -19 54 O ATOM 2796 CB LYS A 360 6.445 39.354 -27.034 1.00 32.24 C ANISOU 2796 CB LYS A 360 3997 4223 4030 -9 14 8 C ATOM 2797 CG LYS A 360 5.723 40.637 -27.418 1.00 33.69 C ANISOU 2797 CG LYS A 360 4342 4250 4207 44 -27 58 C ATOM 2798 CD LYS A 360 4.285 40.415 -27.817 1.00 35.72 C ANISOU 2798 CD LYS A 360 4407 4590 4575 41 -92 20 C ATOM 2799 CE LYS A 360 3.298 40.350 -26.677 1.00 37.75 C ANISOU 2799 CE LYS A 360 4717 4923 4703 14 50 -5 C ATOM 2800 NZ LYS A 360 1.980 40.931 -27.126 1.00 39.58 N ANISOU 2800 NZ LYS A 360 4856 5197 4985 93 -84 -6 N ATOM 2801 N LEU A 361 8.327 38.747 -29.479 1.00 34.63 N ANISOU 2801 N LEU A 361 4203 4582 4372 4 -59 44 N ATOM 2802 CA LEU A 361 8.981 39.139 -30.722 1.00 36.49 C ANISOU 2802 CA LEU A 361 4508 4826 4531 7 49 114 C ATOM 2803 C LEU A 361 8.613 38.196 -31.857 1.00 37.90 C ANISOU 2803 C LEU A 361 4659 4980 4762 -17 32 -19 C ATOM 2804 O LEU A 361 8.306 38.636 -32.978 1.00 38.62 O ANISOU 2804 O LEU A 361 4743 5092 4839 -11 -11 56 O ATOM 2805 CB LEU A 361 10.488 39.270 -30.530 1.00 36.38 C ANISOU 2805 CB LEU A 361 4532 4730 4561 -9 -2 68 C ATOM 2806 CG LEU A 361 11.004 40.393 -29.635 1.00 36.62 C ANISOU 2806 CG LEU A 361 4603 4693 4617 28 -7 49 C ATOM 2807 CD1 LEU A 361 12.511 40.253 -29.427 1.00 36.50 C ANISOU 2807 CD1 LEU A 361 4593 4699 4576 8 -28 53 C ATOM 2808 CD2 LEU A 361 10.726 41.795 -30.183 1.00 36.59 C ANISOU 2808 CD2 LEU A 361 4589 4682 4631 1 -60 54 C ATOM 2809 N ILE A 362 8.574 36.892 -31.633 1.00 39.38 N ANISOU 2809 N ILE A 362 4848 5080 5035 37 16 96 N ATOM 2810 CA ILE A 362 8.056 35.963 -32.628 1.00 41.42 C ANISOU 2810 CA ILE A 362 5287 5287 5164 -10 -2 -44 C ATOM 2811 C ILE A 362 6.577 36.176 -32.923 1.00 43.65 C ANISOU 2811 C ILE A 362 5417 5632 5534 33 -110 12 C ATOM 2812 O ILE A 362 6.216 36.233 -34.107 1.00 43.88 O ANISOU 2812 O ILE A 362 5489 5703 5479 22 -76 -52 O ATOM 2813 CB ILE A 362 8.309 34.511 -32.229 1.00 40.84 C ANISOU 2813 CB ILE A 362 5116 5281 5122 -2 6 -7 C ATOM 2814 CG1 ILE A 362 9.816 34.295 -32.011 1.00 40.63 C ANISOU 2814 CG1 ILE A 362 5132 5217 5089 -15 6 -10 C ATOM 2815 CG2 ILE A 362 7.793 33.562 -33.301 1.00 40.89 C ANISOU 2815 CG2 ILE A 362 5097 5311 5130 1 -10 -7 C ATOM 2816 CD1 ILE A 362 10.154 32.897 -31.528 1.00 40.61 C ANISOU 2816 CD1 ILE A 362 5116 5214 5099 24 -1 -42 C ATOM 2817 N GLU A 363 5.727 36.331 -31.921 1.00 45.59 N ANISOU 2817 N GLU A 363 5845 5867 5609 10 58 -11 N ATOM 2818 CA GLU A 363 4.328 36.685 -32.120 1.00 48.13 C ANISOU 2818 CA GLU A 363 5960 6202 6126 24 -56 -17 C ATOM 2819 C GLU A 363 4.148 37.926 -32.982 1.00 49.08 C ANISOU 2819 C GLU A 363 6231 6281 6136 39 4 12 C ATOM 2820 O GLU A 363 3.229 37.942 -33.804 1.00 49.48 O ANISOU 2820 O GLU A 363 6275 6384 6141 19 -8 40 O ATOM 2821 CB GLU A 363 3.663 36.877 -30.763 1.00 49.46 C ANISOU 2821 CB GLU A 363 6316 6317 6161 37 19 -20 C ATOM 2822 CG GLU A 363 2.147 36.828 -30.705 1.00 51.26 C ANISOU 2822 CG GLU A 363 6382 6554 6542 0 -15 9 C ATOM 2823 CD GLU A 363 1.679 37.471 -29.402 1.00 52.65 C ANISOU 2823 CD GLU A 363 6652 6726 6628 35 68 -13 C ATOM 2824 OE1 GLU A 363 2.106 36.976 -28.329 1.00 53.01 O ANISOU 2824 OE1 GLU A 363 6684 6745 6711 52 18 33 O ATOM 2825 OE2 GLU A 363 0.928 38.467 -29.481 1.00 53.25 O ANISOU 2825 OE2 GLU A 363 6709 6753 6770 64 50 53 O ATOM 2826 N LYS A 364 4.988 38.947 -32.888 1.00 49.78 N ANISOU 2826 N LYS A 364 6267 6411 6237 -19 3 -49 N ATOM 2827 CA LYS A 364 4.876 40.153 -33.687 1.00 51.34 C ANISOU 2827 CA LYS A 364 6525 6508 6476 -13 -31 55 C ATOM 2828 C LYS A 364 5.612 40.036 -35.023 1.00 52.38 C ANISOU 2828 C LYS A 364 6588 6731 6583 -28 -3 15 C ATOM 2829 O LYS A 364 5.970 41.018 -35.677 1.00 52.52 O ANISOU 2829 O LYS A 364 6625 6756 6575 -61 -14 16 O ATOM 2830 CB LYS A 364 5.329 41.385 -32.910 1.00 51.38 C ANISOU 2830 CB LYS A 364 6526 6535 6460 -26 -27 50 C ATOM 2831 CG LYS A 364 4.413 41.878 -31.809 1.00 52.04 C ANISOU 2831 CG LYS A 364 6647 6601 6523 -5 17 32 C ATOM 2832 CD LYS A 364 3.057 42.345 -32.287 1.00 52.80 C ANISOU 2832 CD LYS A 364 6677 6709 6674 -5 -12 49 C ATOM 2833 CE LYS A 364 2.150 42.825 -31.167 1.00 53.33 C ANISOU 2833 CE LYS A 364 6812 6752 6698 9 24 30 C ATOM 2834 NZ LYS A 364 2.740 43.976 -30.431 1.00 53.94 N ANISOU 2834 NZ LYS A 364 6886 6829 6780 -38 -19 33 N ATOM 2835 N GLY A 365 5.836 38.817 -35.495 1.00 53.48 N ANISOU 2835 N GLY A 365 6709 6785 6826 20 -54 -21 N ATOM 2836 CA GLY A 365 6.239 38.557 -36.859 1.00 55.30 C ANISOU 2836 CA GLY A 365 7039 7099 6875 -12 -4 -25 C ATOM 2837 C GLY A 365 7.533 37.759 -36.902 1.00 56.90 C ANISOU 2837 C GLY A 365 7153 7275 7192 64 -28 -22 C ATOM 2838 O GLY A 365 7.604 36.725 -37.569 1.00 57.85 O ANISOU 2838 O GLY A 365 7362 7335 7282 25 -86 -75 O ATOM 2839 N LEU A 366 8.542 38.220 -36.159 1.00 57.19 N ANISOU 2839 N LEU A 366 7230 7324 7175 -7 -10 -49 N ATOM 2840 CA LEU A 366 9.881 37.663 -36.281 1.00 57.13 C ANISOU 2840 CA LEU A 366 7240 7311 7158 2 -14 -10 C ATOM 2841 C LEU A 366 9.947 36.149 -36.148 1.00 57.12 C ANISOU 2841 C LEU A 366 7254 7316 7134 20 -41 -15 C ATOM 2842 O LEU A 366 9.092 35.462 -35.609 1.00 57.51 O ANISOU 2842 O LEU A 366 7286 7394 7171 -11 -14 -26 O ATOM 2843 CB LEU A 366 10.854 38.263 -35.268 1.00 56.91 C ANISOU 2843 CB LEU A 366 7176 7280 7168 0 7 4 C ATOM 2844 CG LEU A 366 10.987 39.781 -35.254 1.00 57.07 C ANISOU 2844 CG LEU A 366 7210 7284 7191 4 13 -1 C ATOM 2845 CD1 LEU A 366 12.008 40.209 -34.207 1.00 57.05 C ANISOU 2845 CD1 LEU A 366 7215 7291 7171 13 18 11 C ATOM 2846 CD2 LEU A 366 11.388 40.331 -36.610 1.00 57.28 C ANISOU 2846 CD2 LEU A 366 7249 7311 7204 9 2 26 C ATOM 2847 N THR A 367 11.045 35.610 -36.683 1.00 57.14 N ANISOU 2847 N THR A 367 7248 7326 7139 21 -57 2 N ATOM 2848 CA THR A 367 11.302 34.179 -36.570 1.00 57.35 C ANISOU 2848 CA THR A 367 7280 7319 7191 19 -59 3 C ATOM 2849 C THR A 367 12.151 33.888 -35.332 1.00 56.31 C ANISOU 2849 C THR A 367 7121 7161 7111 4 9 -24 C ATOM 2850 O THR A 367 12.861 34.768 -34.851 1.00 55.23 O ANISOU 2850 O THR A 367 6910 7195 6880 53 -21 23 O ATOM 2851 CB THR A 367 12.027 33.616 -37.800 1.00 58.27 C ANISOU 2851 CB THR A 367 7384 7437 7320 25 19 -25 C ATOM 2852 OG1 THR A 367 12.116 32.190 -37.649 1.00 59.32 O ANISOU 2852 OG1 THR A 367 7572 7466 7503 27 -5 -22 O ATOM 2853 CG2 THR A 367 13.431 34.190 -37.912 1.00 58.19 C ANISOU 2853 CG2 THR A 367 7391 7418 7299 7 21 -14 C ATOM 2854 N ARG A 368 12.128 32.642 -34.888 1.00 55.85 N ANISOU 2854 N ARG A 368 7043 7151 7028 28 4 -25 N ATOM 2855 CA ARG A 368 12.831 32.235 -33.679 1.00 55.64 C ANISOU 2855 CA ARG A 368 7039 7083 7017 13 14 -31 C ATOM 2856 C ARG A 368 14.244 32.791 -33.606 1.00 55.47 C ANISOU 2856 C ARG A 368 7025 7069 6982 29 23 -29 C ATOM 2857 O ARG A 368 14.625 33.428 -32.622 1.00 55.54 O ANISOU 2857 O ARG A 368 7000 7130 6973 32 -8 -27 O ATOM 2858 CB ARG A 368 12.829 30.720 -33.551 1.00 55.68 C ANISOU 2858 CB ARG A 368 7052 7076 7028 10 11 -44 C ATOM 2859 N LYS A 369 15.048 32.614 -34.649 1.00 55.12 N ANISOU 2859 N LYS A 369 6957 7034 6951 23 -12 -21 N ATOM 2860 CA LYS A 369 16.412 33.096 -34.690 1.00 54.73 C ANISOU 2860 CA LYS A 369 6951 6941 6902 14 10 -17 C ATOM 2861 C LYS A 369 16.555 34.606 -34.623 1.00 53.95 C ANISOU 2861 C LYS A 369 6791 6923 6784 54 17 -5 C ATOM 2862 O LYS A 369 17.417 35.080 -33.854 1.00 54.14 O ANISOU 2862 O LYS A 369 6750 7024 6795 31 39 -22 O ATOM 2863 CB LYS A 369 17.120 32.557 -35.934 1.00 55.12 C ANISOU 2863 CB LYS A 369 6981 7024 6938 34 14 -10 C ATOM 2864 N GLU A 370 15.776 35.389 -35.365 1.00 52.72 N ANISOU 2864 N GLU A 370 6679 6759 6594 -8 53 -46 N ATOM 2865 CA GLU A 370 15.815 36.834 -35.194 1.00 51.87 C ANISOU 2865 CA GLU A 370 6581 6722 6404 -21 93 -49 C ATOM 2866 C GLU A 370 15.478 37.281 -33.768 1.00 49.20 C ANISOU 2866 C GLU A 370 6149 6316 6229 -59 -15 86 C ATOM 2867 O GLU A 370 16.124 38.204 -33.266 1.00 48.60 O ANISOU 2867 O GLU A 370 6141 6322 6004 -21 -18 64 O ATOM 2868 CB GLU A 370 14.857 37.563 -36.131 1.00 54.15 C ANISOU 2868 CB GLU A 370 6790 6944 6841 45 -52 72 C ATOM 2869 CG GLU A 370 14.975 37.238 -37.609 1.00 56.65 C ANISOU 2869 CG GLU A 370 7241 7297 6985 7 19 -40 C ATOM 2870 CD GLU A 370 13.757 37.759 -38.368 1.00 58.24 C ANISOU 2870 CD GLU A 370 7343 7482 7306 38 -71 33 C ATOM 2871 OE1 GLU A 370 13.863 38.861 -38.950 1.00 59.11 O ANISOU 2871 OE1 GLU A 370 7528 7477 7456 17 -65 46 O ATOM 2872 OE2 GLU A 370 12.715 37.071 -38.359 1.00 59.28 O ANISOU 2872 OE2 GLU A 370 7418 7626 7481 -50 -68 7 O ATOM 2873 N ALA A 371 14.437 36.722 -33.160 1.00 46.67 N ANISOU 2873 N ALA A 371 5980 6039 5712 64 -74 -9 N ATOM 2874 CA ALA A 371 14.059 37.118 -31.799 1.00 44.54 C ANISOU 2874 CA ALA A 371 5596 5695 5633 12 -79 57 C ATOM 2875 C ALA A 371 15.145 36.720 -30.796 1.00 42.92 C ANISOU 2875 C ALA A 371 5491 5456 5361 -28 23 0 C ATOM 2876 O ALA A 371 15.528 37.508 -29.941 1.00 41.46 O ANISOU 2876 O ALA A 371 5214 5346 5193 16 7 111 O ATOM 2877 CB ALA A 371 12.724 36.481 -31.471 1.00 44.24 C ANISOU 2877 CB ALA A 371 5597 5705 5510 41 -15 4 C ATOM 2878 N TYR A 372 15.676 35.514 -30.945 1.00 42.54 N ANISOU 2878 N TYR A 372 5410 5459 5294 -1 13 54 N ATOM 2879 CA TYR A 372 16.789 35.031 -30.144 1.00 42.75 C ANISOU 2879 CA TYR A 372 5401 5496 5345 -11 1 32 C ATOM 2880 C TYR A 372 17.939 36.026 -30.217 1.00 42.43 C ANISOU 2880 C TYR A 372 5367 5454 5299 18 0 4 C ATOM 2881 O TYR A 372 18.443 36.390 -29.153 1.00 41.12 O ANISOU 2881 O TYR A 372 5174 5325 5127 63 98 64 O ATOM 2882 CB TYR A 372 17.287 33.630 -30.530 1.00 43.45 C ANISOU 2882 CB TYR A 372 5530 5538 5440 14 38 -13 C ATOM 2883 CG TYR A 372 18.314 33.042 -29.580 1.00 44.30 C ANISOU 2883 CG TYR A 372 5604 5664 5566 46 -29 -13 C ATOM 2884 CD1 TYR A 372 17.953 32.175 -28.554 1.00 44.73 C ANISOU 2884 CD1 TYR A 372 5657 5678 5661 5 3 4 C ATOM 2885 CD2 TYR A 372 19.661 33.351 -29.723 1.00 44.84 C ANISOU 2885 CD2 TYR A 372 5675 5721 5642 -17 15 -7 C ATOM 2886 CE1 TYR A 372 18.896 31.643 -27.694 1.00 45.16 C ANISOU 2886 CE1 TYR A 372 5733 5758 5668 32 -8 7 C ATOM 2887 CE2 TYR A 372 20.621 32.833 -28.862 1.00 45.20 C ANISOU 2887 CE2 TYR A 372 5714 5729 5731 40 3 12 C ATOM 2888 CZ TYR A 372 20.230 31.981 -27.847 1.00 45.41 C ANISOU 2888 CZ TYR A 372 5756 5777 5721 30 -3 13 C ATOM 2889 OH TYR A 372 21.213 31.486 -27.024 1.00 45.42 O ANISOU 2889 OH TYR A 372 5767 5791 5700 14 -30 -3 O ATOM 2890 N ASP A 373 18.331 36.454 -31.421 1.00 42.68 N ANISOU 2890 N ASP A 373 5391 5519 5305 29 16 26 N ATOM 2891 CA ASP A 373 19.463 37.371 -31.501 1.00 42.76 C ANISOU 2891 CA ASP A 373 5405 5409 5433 43 -10 -14 C ATOM 2892 C ASP A 373 19.173 38.686 -30.816 1.00 40.65 C ANISOU 2892 C ASP A 373 5027 5386 5033 27 28 51 C ATOM 2893 O ASP A 373 20.084 39.183 -30.137 1.00 39.73 O ANISOU 2893 O ASP A 373 4852 5408 4834 85 125 48 O ATOM 2894 CB ASP A 373 19.925 37.557 -32.951 1.00 45.54 C ANISOU 2894 CB ASP A 373 5775 5958 5569 -28 44 36 C ATOM 2895 CG ASP A 373 20.559 36.290 -33.500 1.00 47.92 C ANISOU 2895 CG ASP A 373 6068 6083 6058 56 53 -58 C ATOM 2896 OD1 ASP A 373 21.004 35.420 -32.715 1.00 48.62 O ANISOU 2896 OD1 ASP A 373 6193 6243 6038 69 48 11 O ATOM 2897 OD2 ASP A 373 20.615 36.155 -34.747 1.00 49.42 O ANISOU 2897 OD2 ASP A 373 6275 6396 6105 -7 58 -37 O ATOM 2898 N ILE A 374 17.966 39.260 -30.933 1.00 38.38 N ANISOU 2898 N ILE A 374 4966 4983 4635 -10 29 20 N ATOM 2899 CA ILE A 374 17.664 40.503 -30.230 1.00 36.39 C ANISOU 2899 CA ILE A 374 4641 4831 4352 -21 -24 124 C ATOM 2900 C ILE A 374 17.723 40.298 -28.709 1.00 33.68 C ANISOU 2900 C ILE A 374 4222 4318 4255 -42 6 80 C ATOM 2901 O ILE A 374 18.221 41.144 -27.975 1.00 32.25 O ANISOU 2901 O ILE A 374 4002 4439 3813 34 34 156 O ATOM 2902 CB ILE A 374 16.257 41.049 -30.582 1.00 37.30 C ANISOU 2902 CB ILE A 374 4692 4840 4639 30 -54 76 C ATOM 2903 CG1 ILE A 374 16.233 41.450 -32.067 1.00 38.71 C ANISOU 2903 CG1 ILE A 374 4932 5079 4695 -24 -33 103 C ATOM 2904 CG2 ILE A 374 15.865 42.223 -29.698 1.00 36.53 C ANISOU 2904 CG2 ILE A 374 4580 4777 4522 21 -119 111 C ATOM 2905 CD1 ILE A 374 14.883 41.269 -32.725 1.00 39.83 C ANISOU 2905 CD1 ILE A 374 5029 5227 4878 -59 -109 83 C ATOM 2906 N VAL A 375 17.132 39.207 -28.247 1.00 31.85 N ANISOU 2906 N VAL A 375 3984 4242 3875 72 -33 72 N ATOM 2907 CA VAL A 375 17.075 38.960 -26.801 1.00 30.30 C ANISOU 2907 CA VAL A 375 3753 3922 3839 2 34 119 C ATOM 2908 C VAL A 375 18.467 38.701 -26.232 1.00 29.97 C ANISOU 2908 C VAL A 375 3817 3833 3738 -36 -4 122 C ATOM 2909 O VAL A 375 18.860 39.243 -25.206 1.00 28.22 O ANISOU 2909 O VAL A 375 3579 3630 3513 84 134 248 O ATOM 2910 CB VAL A 375 16.155 37.762 -26.519 1.00 29.88 C ANISOU 2910 CB VAL A 375 3694 3918 3742 17 -20 114 C ATOM 2911 CG1 VAL A 375 16.294 37.327 -25.067 1.00 29.23 C ANISOU 2911 CG1 VAL A 375 3587 3831 3689 -43 -28 87 C ATOM 2912 CG2 VAL A 375 14.702 38.131 -26.805 1.00 29.30 C ANISOU 2912 CG2 VAL A 375 3646 3843 3644 -38 -3 100 C ATOM 2913 N GLN A 376 19.237 37.871 -26.950 1.00 31.40 N ANISOU 2913 N GLN A 376 4012 4025 3894 44 82 84 N ATOM 2914 CA GLN A 376 20.611 37.566 -26.522 1.00 32.74 C ANISOU 2914 CA GLN A 376 4093 4232 4114 14 -24 102 C ATOM 2915 C GLN A 376 21.497 38.792 -26.478 1.00 32.05 C ANISOU 2915 C GLN A 376 4040 4200 3937 28 34 118 C ATOM 2916 O GLN A 376 22.256 38.969 -25.510 1.00 31.44 O ANISOU 2916 O GLN A 376 3979 4156 3810 -22 81 230 O ATOM 2917 CB GLN A 376 21.180 36.474 -27.427 1.00 35.12 C ANISOU 2917 CB GLN A 376 4524 4472 4350 22 67 -62 C ATOM 2918 CG GLN A 376 22.373 35.720 -26.844 1.00 37.82 C ANISOU 2918 CG GLN A 376 4781 4827 4760 157 -36 3 C ATOM 2919 CD GLN A 376 23.671 36.474 -27.014 1.00 39.67 C ANISOU 2919 CD GLN A 376 4986 5031 5055 13 37 -17 C ATOM 2920 OE1 GLN A 376 23.752 37.440 -27.779 1.00 40.27 O ANISOU 2920 OE1 GLN A 376 5093 5056 5150 58 48 42 O ATOM 2921 NE2 GLN A 376 24.721 36.046 -26.311 1.00 40.65 N ANISOU 2921 NE2 GLN A 376 5144 5189 5112 72 -27 -6 N ATOM 2922 N ARG A 377 21.426 39.687 -27.480 1.00 31.41 N ANISOU 2922 N ARG A 377 3971 4057 3907 5 6 100 N ATOM 2923 CA ARG A 377 22.201 40.909 -27.457 1.00 30.42 C ANISOU 2923 CA ARG A 377 3887 3932 3739 53 16 122 C ATOM 2924 C ARG A 377 21.857 41.761 -26.244 1.00 29.02 C ANISOU 2924 C ARG A 377 3712 3777 3538 -14 0 268 C ATOM 2925 O ARG A 377 22.765 42.270 -25.594 1.00 28.72 O ANISOU 2925 O ARG A 377 3738 3726 3450 -66 22 325 O ATOM 2926 CB ARG A 377 21.999 41.817 -28.693 1.00 31.23 C ANISOU 2926 CB ARG A 377 3941 4127 3797 29 -38 184 C ATOM 2927 N ASN A 378 20.556 41.962 -25.996 1.00 28.04 N ANISOU 2927 N ASN A 378 3710 3583 3361 66 0 266 N ATOM 2928 CA ASN A 378 20.171 42.769 -24.842 1.00 27.46 C ANISOU 2928 CA ASN A 378 3575 3489 3370 22 -52 222 C ATOM 2929 C ASN A 378 20.416 42.038 -23.525 1.00 25.70 C ANISOU 2929 C ASN A 378 3248 3255 3260 22 -5 135 C ATOM 2930 O ASN A 378 20.696 42.679 -22.517 1.00 24.64 O ANISOU 2930 O ASN A 378 3086 3165 3111 4 8 317 O ATOM 2931 CB ASN A 378 18.693 43.199 -24.951 1.00 28.81 C ANISOU 2931 CB ASN A 378 3611 3730 3603 60 -39 171 C ATOM 2932 CG ASN A 378 18.610 44.201 -26.084 1.00 30.23 C ANISOU 2932 CG ASN A 378 3937 3811 3740 27 -48 203 C ATOM 2933 OD1 ASN A 378 18.925 45.352 -26.073 1.00 30.95 O ANISOU 2933 OD1 ASN A 378 4144 3840 3776 -26 11 335 O ATOM 2934 ND2 ASN A 378 18.195 43.882 -27.261 1.00 30.08 N ANISOU 2934 ND2 ASN A 378 3993 3791 3645 55 -33 310 N ATOM 2935 N ALA A 379 20.368 40.711 -23.543 1.00 25.20 N ANISOU 2935 N ALA A 379 3102 3270 3204 8 33 216 N ATOM 2936 CA ALA A 379 20.678 39.959 -22.313 1.00 24.68 C ANISOU 2936 CA ALA A 379 3144 3152 3081 -2 5 108 C ATOM 2937 C ALA A 379 22.146 40.109 -21.928 1.00 25.49 C ANISOU 2937 C ALA A 379 3218 3262 3205 52 -70 80 C ATOM 2938 O ALA A 379 22.491 40.311 -20.754 1.00 24.10 O ANISOU 2938 O ALA A 379 2959 3122 3075 138 17 111 O ATOM 2939 CB ALA A 379 20.308 38.508 -22.532 1.00 23.42 C ANISOU 2939 CB ALA A 379 3009 3043 2845 88 35 154 C ATOM 2940 N LEU A 380 23.036 39.979 -22.916 1.00 27.05 N ANISOU 2940 N LEU A 380 3452 3454 3370 89 93 125 N ATOM 2941 CA LEU A 380 24.461 40.183 -22.661 1.00 29.18 C ANISOU 2941 CA LEU A 380 3566 3739 3780 -17 -75 94 C ATOM 2942 C LEU A 380 24.773 41.570 -22.159 1.00 28.45 C ANISOU 2942 C LEU A 380 3467 3701 3643 26 38 114 C ATOM 2943 O LEU A 380 25.520 41.726 -21.177 1.00 27.46 O ANISOU 2943 O LEU A 380 3355 3508 3569 -44 84 154 O ATOM 2944 CB LEU A 380 25.262 39.832 -23.915 1.00 32.39 C ANISOU 2944 CB LEU A 380 4168 4200 3939 24 111 46 C ATOM 2945 CG LEU A 380 26.738 39.495 -23.716 1.00 35.52 C ANISOU 2945 CG LEU A 380 4310 4640 4546 60 -7 59 C ATOM 2946 CD1 LEU A 380 26.942 38.395 -22.678 1.00 36.19 C ANISOU 2946 CD1 LEU A 380 4515 4612 4625 65 32 84 C ATOM 2947 CD2 LEU A 380 27.338 39.075 -25.059 1.00 37.02 C ANISOU 2947 CD2 LEU A 380 4653 4783 4631 68 60 -12 C ATOM 2948 N LYS A 381 24.205 42.623 -22.733 1.00 28.29 N ANISOU 2948 N LYS A 381 3414 3719 3618 -24 17 201 N ATOM 2949 CA LYS A 381 24.408 43.967 -22.212 1.00 29.01 C ANISOU 2949 CA LYS A 381 3577 3795 3650 -45 67 64 C ATOM 2950 C LYS A 381 23.967 44.104 -20.764 1.00 27.68 C ANISOU 2950 C LYS A 381 3386 3570 3560 -95 -27 184 C ATOM 2951 O LYS A 381 24.683 44.670 -19.945 1.00 27.34 O ANISOU 2951 O LYS A 381 3391 3461 3536 -212 43 272 O ATOM 2952 CB LYS A 381 23.655 44.993 -23.089 1.00 31.90 C ANISOU 2952 CB LYS A 381 3995 4007 4117 51 -107 183 C ATOM 2953 CG LYS A 381 24.219 44.908 -24.519 1.00 35.02 C ANISOU 2953 CG LYS A 381 4469 4540 4297 10 79 14 C ATOM 2954 CD LYS A 381 23.259 45.534 -25.520 1.00 37.90 C ANISOU 2954 CD LYS A 381 4790 4925 4687 77 -122 90 C ATOM 2955 CE LYS A 381 23.836 46.798 -26.107 1.00 40.20 C ANISOU 2955 CE LYS A 381 5101 5051 5122 -57 -27 92 C ATOM 2956 NZ LYS A 381 23.271 47.151 -27.445 1.00 41.89 N ANISOU 2956 NZ LYS A 381 5293 5444 5180 -33 -119 93 N ATOM 2957 N THR A 382 22.774 43.581 -20.459 1.00 26.10 N ANISOU 2957 N THR A 382 3253 3418 3246 12 -18 172 N ATOM 2958 CA THR A 382 22.266 43.575 -19.091 1.00 24.97 C ANISOU 2958 CA THR A 382 3053 3211 3223 -23 -45 120 C ATOM 2959 C THR A 382 23.243 42.882 -18.146 1.00 23.93 C ANISOU 2959 C THR A 382 2971 3062 3057 -98 33 129 C ATOM 2960 O THR A 382 23.565 43.394 -17.083 1.00 23.38 O ANISOU 2960 O THR A 382 2870 2932 3080 -161 -5 191 O ATOM 2961 CB THR A 382 20.921 42.829 -18.995 1.00 24.76 C ANISOU 2961 CB THR A 382 3000 3298 3110 5 -35 159 C ATOM 2962 OG1 THR A 382 19.981 43.367 -19.949 1.00 24.69 O ANISOU 2962 OG1 THR A 382 2926 3195 3259 -1 -48 234 O ATOM 2963 CG2 THR A 382 20.351 42.962 -17.578 1.00 24.35 C ANISOU 2963 CG2 THR A 382 3007 3132 3115 -10 -8 133 C ATOM 2964 N TRP A 383 23.669 41.683 -18.526 1.00 24.17 N ANISOU 2964 N TRP A 383 2958 3069 3156 -38 101 179 N ATOM 2965 CA TRP A 383 24.510 40.836 -17.679 1.00 25.19 C ANISOU 2965 CA TRP A 383 3063 3225 3282 47 -30 135 C ATOM 2966 C TRP A 383 25.795 41.560 -17.314 1.00 27.11 C ANISOU 2966 C TRP A 383 3266 3497 3537 -70 -54 41 C ATOM 2967 O TRP A 383 26.294 41.446 -16.192 1.00 26.52 O ANISOU 2967 O TRP A 383 3077 3496 3503 -152 -1 47 O ATOM 2968 CB TRP A 383 24.810 39.529 -18.421 1.00 25.22 C ANISOU 2968 CB TRP A 383 3118 3216 3247 30 23 141 C ATOM 2969 CG TRP A 383 25.470 38.447 -17.598 1.00 25.24 C ANISOU 2969 CG TRP A 383 3124 3167 3298 19 15 157 C ATOM 2970 CD1 TRP A 383 26.781 38.096 -17.551 1.00 26.07 C ANISOU 2970 CD1 TRP A 383 3189 3328 3390 30 64 190 C ATOM 2971 CD2 TRP A 383 24.796 37.583 -16.670 1.00 24.74 C ANISOU 2971 CD2 TRP A 383 3034 3135 3229 49 47 115 C ATOM 2972 NE1 TRP A 383 26.984 37.051 -16.655 1.00 25.91 N ANISOU 2972 NE1 TRP A 383 3140 3270 3435 72 40 162 N ATOM 2973 CE2 TRP A 383 25.761 36.738 -16.094 1.00 25.17 C ANISOU 2973 CE2 TRP A 383 3100 3161 3303 12 15 144 C ATOM 2974 CE3 TRP A 383 23.454 37.461 -16.280 1.00 23.86 C ANISOU 2974 CE3 TRP A 383 2952 2977 3136 -11 -55 126 C ATOM 2975 CZ2 TRP A 383 25.430 35.769 -15.157 1.00 24.91 C ANISOU 2975 CZ2 TRP A 383 3016 3269 3178 3 -10 128 C ATOM 2976 CZ3 TRP A 383 23.134 36.511 -15.327 1.00 24.05 C ANISOU 2976 CZ3 TRP A 383 2927 3042 3169 -8 81 102 C ATOM 2977 CH2 TRP A 383 24.113 35.681 -14.767 1.00 24.23 C ANISOU 2977 CH2 TRP A 383 2991 3095 3120 -60 -36 108 C ATOM 2978 N ASN A 384 26.366 42.281 -18.278 1.00 28.88 N ANISOU 2978 N ASN A 384 3613 3674 3687 12 33 187 N ATOM 2979 CA ASN A 384 27.676 42.918 -18.066 1.00 31.21 C ANISOU 2979 CA ASN A 384 3802 4011 4045 -107 -31 60 C ATOM 2980 C ASN A 384 27.571 44.372 -17.637 1.00 32.21 C ANISOU 2980 C ASN A 384 3997 4067 4174 -16 -11 45 C ATOM 2981 O ASN A 384 28.560 45.116 -17.764 1.00 33.45 O ANISOU 2981 O ASN A 384 3981 4278 4452 -58 10 84 O ATOM 2982 CB ASN A 384 28.507 42.800 -19.350 1.00 31.96 C ANISOU 2982 CB ASN A 384 3866 4146 4131 -47 58 73 C ATOM 2983 CG ASN A 384 28.851 41.361 -19.687 1.00 33.13 C ANISOU 2983 CG ASN A 384 4062 4259 4265 -4 27 6 C ATOM 2984 OD1 ASN A 384 29.225 40.558 -18.827 1.00 33.76 O ANISOU 2984 OD1 ASN A 384 4110 4262 4457 45 58 105 O ATOM 2985 ND2 ASN A 384 28.725 40.994 -20.951 1.00 33.85 N ANISOU 2985 ND2 ASN A 384 4148 4435 4277 43 36 -58 N ATOM 2986 N SER A 385 26.414 44.824 -17.163 1.00 31.84 N ANISOU 2986 N SER A 385 3918 4071 4109 -46 -15 98 N ATOM 2987 CA SER A 385 26.305 46.207 -16.735 1.00 32.64 C ANISOU 2987 CA SER A 385 4060 4109 4232 -69 -54 67 C ATOM 2988 C SER A 385 25.350 46.333 -15.559 1.00 32.99 C ANISOU 2988 C SER A 385 4155 4169 4212 -21 -42 60 C ATOM 2989 O SER A 385 24.866 45.344 -15.018 1.00 33.26 O ANISOU 2989 O SER A 385 4216 4077 4345 -27 -21 46 O ATOM 2990 CB SER A 385 25.864 47.121 -17.882 1.00 32.88 C ANISOU 2990 CB SER A 385 4134 4126 4235 -52 -65 69 C ATOM 2991 OG SER A 385 24.559 46.842 -18.353 1.00 33.58 O ANISOU 2991 OG SER A 385 4128 4273 4356 -40 -73 232 O ATOM 2992 N GLU A 386 25.045 47.569 -15.213 1.00 33.25 N ANISOU 2992 N GLU A 386 4250 4077 4306 -89 -124 72 N ATOM 2993 CA GLU A 386 24.077 47.895 -14.210 1.00 35.14 C ANISOU 2993 CA GLU A 386 4364 4479 4508 36 -8 126 C ATOM 2994 C GLU A 386 22.666 48.153 -14.739 1.00 32.59 C ANISOU 2994 C GLU A 386 4250 3977 4157 -100 17 30 C ATOM 2995 O GLU A 386 21.753 48.286 -13.918 1.00 31.65 O ANISOU 2995 O GLU A 386 4075 3749 4202 -12 -44 76 O ATOM 2996 CB GLU A 386 24.484 49.209 -13.497 1.00 39.95 C ANISOU 2996 CB GLU A 386 5080 4858 5242 -130 -9 -161 C ATOM 2997 CG GLU A 386 24.457 48.923 -11.983 1.00 45.28 C ANISOU 2997 CG GLU A 386 5903 5813 5489 -13 -18 80 C ATOM 2998 CD GLU A 386 25.827 48.421 -11.591 1.00 48.46 C ANISOU 2998 CD GLU A 386 6056 6209 6149 33 -108 -51 C ATOM 2999 OE1 GLU A 386 26.686 49.081 -12.221 1.00 50.53 O ANISOU 2999 OE1 GLU A 386 6460 6369 6371 -49 24 100 O ATOM 3000 OE2 GLU A 386 26.001 47.498 -10.784 1.00 50.52 O ANISOU 3000 OE2 GLU A 386 6467 6386 6344 19 -27 113 O ATOM 3001 N LYS A 387 22.507 48.318 -16.049 1.00 30.68 N ANISOU 3001 N LYS A 387 3834 3715 4108 -86 -4 43 N ATOM 3002 CA LYS A 387 21.197 48.710 -16.543 1.00 29.60 C ANISOU 3002 CA LYS A 387 3826 3558 3861 -131 -6 79 C ATOM 3003 C LYS A 387 20.344 47.437 -16.721 1.00 28.12 C ANISOU 3003 C LYS A 387 3586 3418 3680 -30 31 100 C ATOM 3004 O LYS A 387 20.886 46.423 -17.141 1.00 27.45 O ANISOU 3004 O LYS A 387 3563 3240 3627 -121 -13 176 O ATOM 3005 CB LYS A 387 21.166 49.480 -17.852 1.00 30.41 C ANISOU 3005 CB LYS A 387 4039 3696 3820 -160 143 97 C ATOM 3006 N HIS A 388 19.073 47.604 -16.435 1.00 27.03 N ANISOU 3006 N HIS A 388 3497 3213 3561 -114 -20 151 N ATOM 3007 CA HIS A 388 18.154 46.461 -16.431 1.00 25.87 C ANISOU 3007 CA HIS A 388 3368 3101 3361 -34 -68 88 C ATOM 3008 C HIS A 388 17.727 46.063 -17.831 1.00 24.43 C ANISOU 3008 C HIS A 388 3195 2826 3261 -56 -5 170 C ATOM 3009 O HIS A 388 17.698 46.890 -18.760 1.00 24.88 O ANISOU 3009 O HIS A 388 3252 2801 3399 -168 -47 322 O ATOM 3010 CB HIS A 388 16.914 46.837 -15.612 1.00 27.30 C ANISOU 3010 CB HIS A 388 3457 3280 3637 5 41 72 C ATOM 3011 CG HIS A 388 17.180 46.795 -14.143 1.00 29.24 C ANISOU 3011 CG HIS A 388 3779 3633 3698 30 4 14 C ATOM 3012 ND1 HIS A 388 18.272 47.377 -13.556 1.00 30.60 N ANISOU 3012 ND1 HIS A 388 3938 3823 3866 -79 -5 -9 N ATOM 3013 CD2 HIS A 388 16.499 46.219 -13.136 1.00 30.06 C ANISOU 3013 CD2 HIS A 388 3817 3791 3813 7 52 45 C ATOM 3014 CE1 HIS A 388 18.261 47.183 -12.249 1.00 30.99 C ANISOU 3014 CE1 HIS A 388 3994 3900 3882 -53 -6 52 C ATOM 3015 NE2 HIS A 388 17.183 46.470 -11.981 1.00 31.60 N ANISOU 3015 NE2 HIS A 388 4000 4059 3948 -79 -38 28 N ATOM 3016 N PHE A 389 17.308 44.818 -18.004 1.00 21.57 N ANISOU 3016 N PHE A 389 2752 2643 2800 53 11 223 N ATOM 3017 CA PHE A 389 16.897 44.289 -19.304 1.00 21.60 C ANISOU 3017 CA PHE A 389 2773 2519 2914 -66 -53 182 C ATOM 3018 C PHE A 389 15.764 45.116 -19.923 1.00 23.17 C ANISOU 3018 C PHE A 389 2942 2775 3088 81 -75 190 C ATOM 3019 O PHE A 389 15.770 45.426 -21.130 1.00 23.73 O ANISOU 3019 O PHE A 389 3006 2869 3143 189 -261 276 O ATOM 3020 CB PHE A 389 16.394 42.873 -19.102 1.00 19.90 C ANISOU 3020 CB PHE A 389 2636 2373 2553 57 -88 198 C ATOM 3021 CG PHE A 389 16.044 41.970 -20.244 1.00 18.49 C ANISOU 3021 CG PHE A 389 2391 2152 2481 137 -42 265 C ATOM 3022 CD1 PHE A 389 14.938 41.140 -20.164 1.00 18.08 C ANISOU 3022 CD1 PHE A 389 2270 2182 2417 171 -203 240 C ATOM 3023 CD2 PHE A 389 16.848 41.877 -21.369 1.00 18.69 C ANISOU 3023 CD2 PHE A 389 2526 2234 2340 149 -93 210 C ATOM 3024 CE1 PHE A 389 14.640 40.245 -21.177 1.00 18.46 C ANISOU 3024 CE1 PHE A 389 2361 2279 2373 137 -75 213 C ATOM 3025 CE2 PHE A 389 16.544 40.990 -22.383 1.00 18.90 C ANISOU 3025 CE2 PHE A 389 2425 2323 2433 44 -105 153 C ATOM 3026 CZ PHE A 389 15.442 40.164 -22.308 1.00 18.84 C ANISOU 3026 CZ PHE A 389 2344 2366 2449 124 -38 231 C ATOM 3027 N LEU A 390 14.760 45.443 -19.127 1.00 24.37 N ANISOU 3027 N LEU A 390 3098 2866 3294 27 54 158 N ATOM 3028 CA LEU A 390 13.593 46.160 -19.679 1.00 26.20 C ANISOU 3028 CA LEU A 390 3292 3164 3499 97 -81 191 C ATOM 3029 C LEU A 390 14.084 47.460 -20.349 1.00 27.63 C ANISOU 3029 C LEU A 390 3554 3297 3648 -17 -5 213 C ATOM 3030 O LEU A 390 13.733 47.713 -21.504 1.00 28.56 O ANISOU 3030 O LEU A 390 3768 3425 3659 -81 32 278 O ATOM 3031 CB LEU A 390 12.632 46.475 -18.567 1.00 26.74 C ANISOU 3031 CB LEU A 390 3417 3227 3515 10 9 120 C ATOM 3032 CG LEU A 390 11.153 46.756 -18.789 1.00 28.04 C ANISOU 3032 CG LEU A 390 3541 3515 3596 90 -72 57 C ATOM 3033 CD1 LEU A 390 10.603 47.711 -17.749 1.00 27.55 C ANISOU 3033 CD1 LEU A 390 3506 3307 3654 89 -131 49 C ATOM 3034 CD2 LEU A 390 10.797 47.109 -20.215 1.00 27.38 C ANISOU 3034 CD2 LEU A 390 3517 3300 3586 161 17 194 C ATOM 3035 N GLU A 391 14.906 48.213 -19.662 1.00 28.72 N ANISOU 3035 N GLU A 391 3758 3367 3785 -1 -119 130 N ATOM 3036 CA GLU A 391 15.488 49.463 -20.173 1.00 29.74 C ANISOU 3036 CA GLU A 391 3808 3574 3920 -71 -26 169 C ATOM 3037 C GLU A 391 16.288 49.282 -21.439 1.00 30.09 C ANISOU 3037 C GLU A 391 3863 3653 3917 -2 -23 150 C ATOM 3038 O GLU A 391 16.060 50.048 -22.399 1.00 30.45 O ANISOU 3038 O GLU A 391 3943 3512 4116 97 -71 266 O ATOM 3039 CB GLU A 391 16.276 50.157 -19.064 1.00 30.29 C ANISOU 3039 CB GLU A 391 3933 3614 3962 -21 -67 97 C ATOM 3040 N TYR A 392 17.161 48.278 -21.578 1.00 29.87 N ANISOU 3040 N TYR A 392 3880 3590 3878 -11 -43 209 N ATOM 3041 CA TYR A 392 17.778 47.986 -22.868 1.00 30.28 C ANISOU 3041 CA TYR A 392 3869 3724 3914 -65 -8 130 C ATOM 3042 C TYR A 392 16.771 47.657 -23.966 1.00 30.64 C ANISOU 3042 C TYR A 392 3860 3857 3927 -73 -22 198 C ATOM 3043 O TYR A 392 16.938 48.053 -25.142 1.00 30.47 O ANISOU 3043 O TYR A 392 3777 3815 3987 -197 61 307 O ATOM 3044 CB TYR A 392 18.769 46.826 -22.794 1.00 30.47 C ANISOU 3044 CB TYR A 392 3909 3759 3908 -44 22 159 C ATOM 3045 CG TYR A 392 20.090 47.185 -22.164 1.00 31.63 C ANISOU 3045 CG TYR A 392 3985 3957 4075 -85 -25 151 C ATOM 3046 CD1 TYR A 392 20.472 46.774 -20.900 1.00 31.01 C ANISOU 3046 CD1 TYR A 392 3974 3829 3981 -120 47 137 C ATOM 3047 CD2 TYR A 392 20.982 47.991 -22.888 1.00 32.34 C ANISOU 3047 CD2 TYR A 392 4070 4046 4171 -82 23 182 C ATOM 3048 CE1 TYR A 392 21.686 47.123 -20.361 1.00 31.61 C ANISOU 3048 CE1 TYR A 392 3971 3933 4106 -50 11 143 C ATOM 3049 CE2 TYR A 392 22.197 48.368 -22.359 1.00 32.47 C ANISOU 3049 CE2 TYR A 392 4105 4043 4189 -110 -10 175 C ATOM 3050 CZ TYR A 392 22.552 47.927 -21.100 1.00 32.66 C ANISOU 3050 CZ TYR A 392 4101 4124 4183 -158 -17 160 C ATOM 3051 OH TYR A 392 23.778 48.278 -20.581 1.00 31.80 O ANISOU 3051 OH TYR A 392 4002 3863 4217 -221 49 251 O ATOM 3052 N LEU A 393 15.731 46.874 -23.621 1.00 29.70 N ANISOU 3052 N LEU A 393 3814 3594 3878 17 -52 320 N ATOM 3053 CA LEU A 393 14.705 46.586 -24.610 1.00 30.31 C ANISOU 3053 CA LEU A 393 3844 3752 3920 -114 -17 202 C ATOM 3054 C LEU A 393 13.963 47.873 -24.989 1.00 32.23 C ANISOU 3054 C LEU A 393 4067 3937 4242 4 -52 229 C ATOM 3055 O LEU A 393 13.700 48.039 -26.173 1.00 33.03 O ANISOU 3055 O LEU A 393 4205 4072 4271 -11 -114 291 O ATOM 3056 CB LEU A 393 13.688 45.541 -24.150 1.00 28.29 C ANISOU 3056 CB LEU A 393 3699 3386 3663 72 -82 204 C ATOM 3057 CG LEU A 393 14.364 44.175 -23.829 1.00 26.67 C ANISOU 3057 CG LEU A 393 3383 3273 3476 -22 21 108 C ATOM 3058 CD1 LEU A 393 13.421 43.359 -22.964 1.00 25.71 C ANISOU 3058 CD1 LEU A 393 3326 3098 3346 -19 -54 112 C ATOM 3059 CD2 LEU A 393 14.754 43.523 -25.132 1.00 25.82 C ANISOU 3059 CD2 LEU A 393 3252 3223 3336 -2 -29 188 C ATOM 3060 N LEU A 394 13.657 48.746 -24.042 1.00 34.76 N ANISOU 3060 N LEU A 394 4455 4302 4449 -78 17 35 N ATOM 3061 CA LEU A 394 12.909 49.958 -24.368 1.00 37.52 C ANISOU 3061 CA LEU A 394 4790 4590 4878 111 -117 91 C ATOM 3062 C LEU A 394 13.722 50.857 -25.296 1.00 40.40 C ANISOU 3062 C LEU A 394 5166 5018 5168 -69 30 160 C ATOM 3063 O LEU A 394 13.166 51.545 -26.172 1.00 41.27 O ANISOU 3063 O LEU A 394 5279 5096 5304 -43 -28 196 O ATOM 3064 CB LEU A 394 12.522 50.704 -23.098 1.00 37.23 C ANISOU 3064 CB LEU A 394 4690 4644 4813 51 -66 122 C ATOM 3065 CG LEU A 394 11.310 50.169 -22.339 1.00 37.51 C ANISOU 3065 CG LEU A 394 4733 4679 4841 39 -53 78 C ATOM 3066 CD1 LEU A 394 11.230 50.802 -20.961 1.00 37.06 C ANISOU 3066 CD1 LEU A 394 4718 4544 4819 56 -65 88 C ATOM 3067 CD2 LEU A 394 10.027 50.419 -23.129 1.00 37.53 C ANISOU 3067 CD2 LEU A 394 4721 4701 4836 17 -60 88 C ATOM 3068 N GLU A 395 15.038 50.850 -25.170 1.00 42.18 N ANISOU 3068 N GLU A 395 5250 5299 5478 31 -99 107 N ATOM 3069 CA GLU A 395 15.919 51.624 -26.029 1.00 44.01 C ANISOU 3069 CA GLU A 395 5516 5530 5676 -48 1 141 C ATOM 3070 C GLU A 395 16.313 50.936 -27.317 1.00 45.65 C ANISOU 3070 C GLU A 395 5759 5857 5729 24 -40 50 C ATOM 3071 O GLU A 395 17.096 51.548 -28.053 1.00 46.68 O ANISOU 3071 O GLU A 395 5904 5907 5927 -74 -54 131 O ATOM 3072 CB GLU A 395 17.232 51.966 -25.294 1.00 43.45 C ANISOU 3072 CB GLU A 395 5540 5384 5584 -8 -8 92 C ATOM 3073 CG GLU A 395 16.993 52.634 -23.958 1.00 43.42 C ANISOU 3073 CG GLU A 395 5590 5319 5587 -25 -20 94 C ATOM 3074 CD GLU A 395 18.230 52.761 -23.099 1.00 43.52 C ANISOU 3074 CD GLU A 395 5595 5336 5607 -61 -10 62 C ATOM 3075 OE1 GLU A 395 19.328 52.297 -23.469 1.00 43.69 O ANISOU 3075 OE1 GLU A 395 5584 5344 5672 -123 22 67 O ATOM 3076 OE2 GLU A 395 18.075 53.337 -22.000 1.00 43.60 O ANISOU 3076 OE2 GLU A 395 5654 5353 5561 -69 -41 95 O ATOM 3077 N ASP A 396 15.913 49.708 -27.572 1.00 46.76 N ANISOU 3077 N ASP A 396 5887 5904 5974 -60 -98 116 N ATOM 3078 CA ASP A 396 16.257 49.000 -28.789 1.00 48.42 C ANISOU 3078 CA ASP A 396 6118 6199 6081 -14 24 31 C ATOM 3079 C ASP A 396 15.269 49.308 -29.916 1.00 49.34 C ANISOU 3079 C ASP A 396 6222 6315 6209 16 -51 71 C ATOM 3080 O ASP A 396 14.065 49.074 -29.826 1.00 48.77 O ANISOU 3080 O ASP A 396 6209 6269 6052 32 -18 153 O ATOM 3081 CB ASP A 396 16.284 47.496 -28.524 1.00 48.93 C ANISOU 3081 CB ASP A 396 6207 6227 6156 -6 -50 73 C ATOM 3082 CG ASP A 396 16.851 46.685 -29.663 1.00 49.86 C ANISOU 3082 CG ASP A 396 6297 6360 6287 -5 39 26 C ATOM 3083 OD1 ASP A 396 16.451 46.931 -30.829 1.00 50.86 O ANISOU 3083 OD1 ASP A 396 6421 6541 6362 8 -31 57 O ATOM 3084 OD2 ASP A 396 17.697 45.794 -29.408 1.00 49.45 O ANISOU 3084 OD2 ASP A 396 6294 6336 6159 -53 6 121 O ATOM 3085 N GLU A 397 15.815 49.749 -31.046 1.00 50.43 N ANISOU 3085 N GLU A 397 6370 6472 6318 -25 38 89 N ATOM 3086 CA GLU A 397 15.007 50.258 -32.155 1.00 51.14 C ANISOU 3086 CA GLU A 397 6491 6552 6387 2 -9 87 C ATOM 3087 C GLU A 397 14.180 49.186 -32.835 1.00 51.36 C ANISOU 3087 C GLU A 397 6550 6576 6389 -24 16 69 C ATOM 3088 O GLU A 397 13.019 49.436 -33.165 1.00 51.98 O ANISOU 3088 O GLU A 397 6602 6658 6489 3 -13 126 O ATOM 3089 CB GLU A 397 15.922 50.951 -33.161 1.00 51.24 C ANISOU 3089 CB GLU A 397 6523 6560 6386 14 6 61 C ATOM 3090 N GLU A 398 14.719 47.985 -33.000 1.00 51.41 N ANISOU 3090 N GLU A 398 6525 6609 6401 -4 32 45 N ATOM 3091 CA GLU A 398 13.933 46.872 -33.517 1.00 51.78 C ANISOU 3091 CA GLU A 398 6585 6630 6457 -12 11 29 C ATOM 3092 C GLU A 398 12.778 46.500 -32.591 1.00 51.80 C ANISOU 3092 C GLU A 398 6590 6672 6418 -7 3 32 C ATOM 3093 O GLU A 398 11.666 46.232 -33.056 1.00 52.79 O ANISOU 3093 O GLU A 398 6622 6849 6586 -45 -29 42 O ATOM 3094 CB GLU A 398 14.857 45.696 -33.789 1.00 51.93 C ANISOU 3094 CB GLU A 398 6617 6646 6466 16 10 43 C ATOM 3095 N VAL A 399 13.004 46.513 -31.278 1.00 50.75 N ANISOU 3095 N VAL A 399 6380 6550 6352 -2 54 57 N ATOM 3096 CA VAL A 399 11.921 46.293 -30.328 1.00 49.16 C ANISOU 3096 CA VAL A 399 6232 6266 6179 22 -46 30 C ATOM 3097 C VAL A 399 10.890 47.404 -30.468 1.00 48.36 C ANISOU 3097 C VAL A 399 6183 6143 6051 -28 -43 73 C ATOM 3098 O VAL A 399 9.694 47.132 -30.606 1.00 47.75 O ANISOU 3098 O VAL A 399 6162 6054 5927 -6 -37 155 O ATOM 3099 CB VAL A 399 12.426 46.193 -28.872 1.00 48.48 C ANISOU 3099 CB VAL A 399 6128 6160 6135 15 -1 51 C ATOM 3100 CG1 VAL A 399 11.300 45.863 -27.915 1.00 47.93 C ANISOU 3100 CG1 VAL A 399 6117 6082 6012 29 -43 51 C ATOM 3101 CG2 VAL A 399 13.523 45.139 -28.794 1.00 48.13 C ANISOU 3101 CG2 VAL A 399 6127 6109 6052 -6 -9 63 C ATOM 3102 N LYS A 400 11.341 48.650 -30.534 1.00 48.11 N ANISOU 3102 N LYS A 400 6118 6124 6036 -16 -78 51 N ATOM 3103 CA LYS A 400 10.438 49.802 -30.517 1.00 48.25 C ANISOU 3103 CA LYS A 400 6127 6111 6093 -27 -46 34 C ATOM 3104 C LYS A 400 9.448 49.822 -31.679 1.00 47.93 C ANISOU 3104 C LYS A 400 6091 6026 6093 -7 -31 89 C ATOM 3105 O LYS A 400 8.352 50.363 -31.552 1.00 47.43 O ANISOU 3105 O LYS A 400 6020 5982 6020 -51 -67 149 O ATOM 3106 CB LYS A 400 11.218 51.116 -30.489 1.00 48.20 C ANISOU 3106 CB LYS A 400 6145 6098 6071 -16 -34 32 C ATOM 3107 N LYS A 401 9.801 49.222 -32.798 1.00 48.39 N ANISOU 3107 N LYS A 401 6184 6112 6090 -25 -12 82 N ATOM 3108 CA LYS A 401 8.962 49.043 -33.956 1.00 49.26 C ANISOU 3108 CA LYS A 401 6257 6262 6195 -30 -60 35 C ATOM 3109 C LYS A 401 7.951 47.907 -33.852 1.00 49.71 C ANISOU 3109 C LYS A 401 6335 6267 6286 -46 -51 64 C ATOM 3110 O LYS A 401 7.040 47.845 -34.693 1.00 50.04 O ANISOU 3110 O LYS A 401 6432 6322 6259 -42 -100 81 O ATOM 3111 CB LYS A 401 9.860 48.736 -35.159 1.00 49.57 C ANISOU 3111 CB LYS A 401 6288 6316 6231 4 -28 17 C ATOM 3112 N LEU A 402 8.140 46.997 -32.894 1.00 48.99 N ANISOU 3112 N LEU A 402 6223 6253 6136 -39 -80 13 N ATOM 3113 CA LEU A 402 7.285 45.824 -32.823 1.00 48.31 C ANISOU 3113 CA LEU A 402 6139 6199 6017 14 -19 20 C ATOM 3114 C LEU A 402 6.335 45.822 -31.644 1.00 47.07 C ANISOU 3114 C LEU A 402 5999 5952 5933 18 -76 54 C ATOM 3115 O LEU A 402 5.334 45.115 -31.747 1.00 46.72 O ANISOU 3115 O LEU A 402 5979 5916 5858 40 -74 67 O ATOM 3116 CB LEU A 402 8.130 44.545 -32.759 1.00 49.16 C ANISOU 3116 CB LEU A 402 6250 6239 6189 38 -43 15 C ATOM 3117 CG LEU A 402 9.010 44.318 -33.997 1.00 49.85 C ANISOU 3117 CG LEU A 402 6320 6367 6255 14 14 3 C ATOM 3118 CD1 LEU A 402 10.106 43.320 -33.701 1.00 49.92 C ANISOU 3118 CD1 LEU A 402 6338 6365 6265 23 -9 13 C ATOM 3119 CD2 LEU A 402 8.154 43.861 -35.175 1.00 50.08 C ANISOU 3119 CD2 LEU A 402 6349 6391 6288 -4 -8 9 C ATOM 3120 N VAL A 403 6.701 46.488 -30.542 1.00 45.91 N ANISOU 3120 N VAL A 403 5779 5857 5806 50 -40 157 N ATOM 3121 CA VAL A 403 5.872 46.380 -29.334 1.00 45.45 C ANISOU 3121 CA VAL A 403 5792 5760 5717 50 -72 48 C ATOM 3122 C VAL A 403 5.786 47.732 -28.644 1.00 44.59 C ANISOU 3122 C VAL A 403 5657 5645 5640 34 -81 149 C ATOM 3123 O VAL A 403 6.734 48.501 -28.568 1.00 44.14 O ANISOU 3123 O VAL A 403 5645 5561 5566 53 -111 232 O ATOM 3124 CB VAL A 403 6.230 45.188 -28.429 1.00 45.60 C ANISOU 3124 CB VAL A 403 5807 5773 5746 46 -36 83 C ATOM 3125 CG1 VAL A 403 7.573 44.534 -28.744 1.00 45.74 C ANISOU 3125 CG1 VAL A 403 5805 5776 5797 52 -34 128 C ATOM 3126 CG2 VAL A 403 6.239 45.535 -26.951 1.00 45.98 C ANISOU 3126 CG2 VAL A 403 5865 5837 5769 49 -44 64 C ATOM 3127 N THR A 404 4.574 48.041 -28.184 1.00 44.54 N ANISOU 3127 N THR A 404 5701 5627 5596 29 -34 142 N ATOM 3128 CA THR A 404 4.361 49.226 -27.368 1.00 44.97 C ANISOU 3128 CA THR A 404 5752 5657 5679 1 -26 80 C ATOM 3129 C THR A 404 5.045 49.051 -26.015 1.00 44.83 C ANISOU 3129 C THR A 404 5709 5608 5715 3 -30 52 C ATOM 3130 O THR A 404 5.360 47.934 -25.598 1.00 45.10 O ANISOU 3130 O THR A 404 5745 5660 5729 49 -44 128 O ATOM 3131 CB THR A 404 2.871 49.524 -27.119 1.00 45.89 C ANISOU 3131 CB THR A 404 5772 5837 5827 7 -10 19 C ATOM 3132 OG1 THR A 404 2.359 48.569 -26.184 1.00 46.00 O ANISOU 3132 OG1 THR A 404 5729 5903 5846 43 -13 66 O ATOM 3133 CG2 THR A 404 2.099 49.479 -28.429 1.00 46.26 C ANISOU 3133 CG2 THR A 404 5820 5900 5858 -2 -48 74 C ATOM 3134 N LYS A 405 5.227 50.163 -25.320 1.00 44.29 N ANISOU 3134 N LYS A 405 5660 5525 5642 34 -25 94 N ATOM 3135 CA LYS A 405 5.882 50.175 -24.024 1.00 43.98 C ANISOU 3135 CA LYS A 405 5547 5562 5602 9 35 89 C ATOM 3136 C LYS A 405 5.025 49.434 -23.002 1.00 42.65 C ANISOU 3136 C LYS A 405 5303 5364 5538 47 -39 50 C ATOM 3137 O LYS A 405 5.557 48.635 -22.231 1.00 42.74 O ANISOU 3137 O LYS A 405 5349 5346 5546 14 -42 108 O ATOM 3138 CB LYS A 405 6.165 51.603 -23.573 1.00 45.29 C ANISOU 3138 CB LYS A 405 5759 5607 5842 -9 11 42 C ATOM 3139 CG LYS A 405 6.702 51.727 -22.163 1.00 47.20 C ANISOU 3139 CG LYS A 405 6034 5988 5914 46 -38 31 C ATOM 3140 CD LYS A 405 7.491 53.019 -21.963 1.00 49.00 C ANISOU 3140 CD LYS A 405 6185 6132 6301 -47 -31 7 C ATOM 3141 CE LYS A 405 7.658 53.290 -20.472 1.00 50.56 C ANISOU 3141 CE LYS A 405 6449 6410 6352 9 -40 -15 C ATOM 3142 NZ LYS A 405 8.647 54.381 -20.210 1.00 51.69 N ANISOU 3142 NZ LYS A 405 6553 6464 6621 -36 -33 -9 N ATOM 3143 N GLU A 406 3.718 49.678 -23.042 1.00 40.41 N ANISOU 3143 N GLU A 406 5193 4935 5225 11 29 119 N ATOM 3144 CA GLU A 406 2.786 48.954 -22.195 1.00 38.91 C ANISOU 3144 CA GLU A 406 4899 4741 5145 74 -44 7 C ATOM 3145 C GLU A 406 2.906 47.451 -22.453 1.00 36.90 C ANISOU 3145 C GLU A 406 4570 4652 4798 33 -26 51 C ATOM 3146 O GLU A 406 2.877 46.670 -21.505 1.00 35.91 O ANISOU 3146 O GLU A 406 4486 4365 4795 98 -38 -22 O ATOM 3147 CB GLU A 406 1.350 49.398 -22.426 1.00 38.93 C ANISOU 3147 CB GLU A 406 4879 4783 5129 73 -29 42 C ATOM 3148 N GLU A 407 2.967 47.039 -23.708 1.00 35.99 N ANISOU 3148 N GLU A 407 4412 4480 4782 70 -55 71 N ATOM 3149 CA GLU A 407 3.068 45.635 -24.057 1.00 36.11 C ANISOU 3149 CA GLU A 407 4414 4530 4777 97 -78 62 C ATOM 3150 C GLU A 407 4.357 44.973 -23.544 1.00 34.42 C ANISOU 3150 C GLU A 407 4254 4308 4517 -26 -22 110 C ATOM 3151 O GLU A 407 4.348 43.839 -23.067 1.00 33.29 O ANISOU 3151 O GLU A 407 3912 4242 4494 20 -82 103 O ATOM 3152 CB GLU A 407 3.008 45.435 -25.559 1.00 38.33 C ANISOU 3152 CB GLU A 407 4908 4849 4806 47 13 65 C ATOM 3153 CG GLU A 407 1.616 45.480 -26.177 1.00 41.14 C ANISOU 3153 CG GLU A 407 5054 5295 5283 10 -116 39 C ATOM 3154 CD GLU A 407 1.798 45.191 -27.666 1.00 43.28 C ANISOU 3154 CD GLU A 407 5480 5582 5382 31 -19 21 C ATOM 3155 OE1 GLU A 407 2.622 45.906 -28.279 1.00 43.89 O ANISOU 3155 OE1 GLU A 407 5522 5618 5536 -16 -56 114 O ATOM 3156 OE2 GLU A 407 1.169 44.248 -28.190 1.00 44.88 O ANISOU 3156 OE2 GLU A 407 5687 5719 5645 -66 -64 -49 O ATOM 3157 N LEU A 408 5.458 45.679 -23.732 1.00 32.78 N ANISOU 3157 N LEU A 408 4135 4040 4279 75 -78 172 N ATOM 3158 CA LEU A 408 6.735 45.251 -23.193 1.00 32.48 C ANISOU 3158 CA LEU A 408 4082 4092 4165 15 -46 119 C ATOM 3159 C LEU A 408 6.726 45.124 -21.672 1.00 30.71 C ANISOU 3159 C LEU A 408 3805 3763 4102 6 -19 100 C ATOM 3160 O LEU A 408 7.139 44.105 -21.140 1.00 29.28 O ANISOU 3160 O LEU A 408 3616 3633 3877 -5 -24 51 O ATOM 3161 CB LEU A 408 7.810 46.305 -23.453 1.00 34.17 C ANISOU 3161 CB LEU A 408 4290 4231 4461 -77 -2 116 C ATOM 3162 CG LEU A 408 8.949 45.934 -24.341 1.00 35.85 C ANISOU 3162 CG LEU A 408 4436 4522 4664 15 34 21 C ATOM 3163 CD1 LEU A 408 10.272 46.491 -23.881 1.00 36.06 C ANISOU 3163 CD1 LEU A 408 4473 4515 4711 -17 -15 47 C ATOM 3164 CD2 LEU A 408 9.428 44.510 -24.395 1.00 36.30 C ANISOU 3164 CD2 LEU A 408 4508 4527 4757 1 35 87 C ATOM 3165 N GLU A 409 6.243 46.184 -21.018 1.00 30.08 N ANISOU 3165 N GLU A 409 3782 3603 4046 -32 -27 151 N ATOM 3166 CA GLU A 409 6.246 46.218 -19.566 1.00 31.40 C ANISOU 3166 CA GLU A 409 3894 3933 4101 -69 7 101 C ATOM 3167 C GLU A 409 5.396 45.126 -18.949 1.00 29.56 C ANISOU 3167 C GLU A 409 3762 3621 3848 84 -22 28 C ATOM 3168 O GLU A 409 5.725 44.592 -17.899 1.00 27.93 O ANISOU 3168 O GLU A 409 3416 3388 3809 91 -28 -63 O ATOM 3169 CB GLU A 409 5.747 47.568 -19.027 1.00 34.96 C ANISOU 3169 CB GLU A 409 4493 4264 4526 179 -15 -30 C ATOM 3170 CG GLU A 409 6.778 48.673 -19.230 1.00 39.07 C ANISOU 3170 CG GLU A 409 4846 4841 5159 -140 -13 90 C ATOM 3171 CD GLU A 409 6.262 50.037 -18.837 1.00 42.64 C ANISOU 3171 CD GLU A 409 5472 5147 5580 75 38 -43 C ATOM 3172 OE1 GLU A 409 5.038 50.277 -18.902 1.00 44.21 O ANISOU 3172 OE1 GLU A 409 5509 5451 5839 74 4 36 O ATOM 3173 OE2 GLU A 409 7.097 50.890 -18.461 1.00 44.71 O ANISOU 3173 OE2 GLU A 409 5697 5450 5842 -97 -19 -71 O ATOM 3174 N GLU A 410 4.294 44.741 -19.599 1.00 28.82 N ANISOU 3174 N GLU A 410 3712 3407 3830 94 28 69 N ATOM 3175 CA GLU A 410 3.451 43.718 -18.969 1.00 29.85 C ANISOU 3175 CA GLU A 410 3856 3447 4037 57 130 42 C ATOM 3176 C GLU A 410 4.098 42.344 -19.056 1.00 26.51 C ANISOU 3176 C GLU A 410 3272 3343 3456 -10 111 68 C ATOM 3177 O GLU A 410 3.713 41.471 -18.278 1.00 25.93 O ANISOU 3177 O GLU A 410 3206 3085 3560 97 38 78 O ATOM 3178 CB GLU A 410 2.087 43.808 -19.640 1.00 34.71 C ANISOU 3178 CB GLU A 410 4122 4351 4716 -11 -72 125 C ATOM 3179 CG GLU A 410 2.120 43.220 -21.040 1.00 40.38 C ANISOU 3179 CG GLU A 410 5234 5118 4991 -78 55 -142 C ATOM 3180 CD GLU A 410 0.910 43.510 -21.870 1.00 44.39 C ANISOU 3180 CD GLU A 410 5681 5623 5564 84 -139 46 C ATOM 3181 OE1 GLU A 410 -0.110 44.120 -21.360 1.00 46.94 O ANISOU 3181 OE1 GLU A 410 6128 5761 5946 94 12 -142 O ATOM 3182 OE2 GLU A 410 0.650 43.030 -22.980 1.00 44.94 O ANISOU 3182 OE2 GLU A 410 5762 5585 5728 -60 -88 -107 O ATOM 3183 N LEU A 411 5.141 42.172 -19.853 1.00 22.81 N ANISOU 3183 N LEU A 411 2984 2611 3070 76 -113 77 N ATOM 3184 CA LEU A 411 5.903 40.904 -19.854 1.00 21.31 C ANISOU 3184 CA LEU A 411 2662 2705 2732 77 4 29 C ATOM 3185 C LEU A 411 6.722 40.729 -18.593 1.00 19.98 C ANISOU 3185 C LEU A 411 2528 2450 2614 43 96 29 C ATOM 3186 O LEU A 411 7.221 39.636 -18.335 1.00 19.57 O ANISOU 3186 O LEU A 411 2431 2487 2516 -13 38 48 O ATOM 3187 CB LEU A 411 6.810 40.846 -21.089 1.00 21.43 C ANISOU 3187 CB LEU A 411 2740 2694 2707 152 2 109 C ATOM 3188 CG LEU A 411 6.083 40.928 -22.443 1.00 21.78 C ANISOU 3188 CG LEU A 411 2711 2793 2770 87 -52 53 C ATOM 3189 CD1 LEU A 411 7.079 40.855 -23.595 1.00 22.27 C ANISOU 3189 CD1 LEU A 411 2819 2903 2740 135 -52 139 C ATOM 3190 CD2 LEU A 411 5.014 39.854 -22.572 1.00 21.64 C ANISOU 3190 CD2 LEU A 411 2768 2648 2807 109 -59 151 C ATOM 3191 N PHE A 412 6.928 41.789 -17.818 1.00 19.22 N ANISOU 3191 N PHE A 412 2366 2389 2547 -12 48 78 N ATOM 3192 CA PHE A 412 7.725 41.756 -16.597 1.00 20.48 C ANISOU 3192 CA PHE A 412 2564 2436 2783 -54 -101 26 C ATOM 3193 C PHE A 412 6.862 41.581 -15.363 1.00 21.91 C ANISOU 3193 C PHE A 412 2842 2584 2899 22 24 65 C ATOM 3194 O PHE A 412 7.257 41.765 -14.201 1.00 23.20 O ANISOU 3194 O PHE A 412 2916 2816 3082 53 -78 -1 O ATOM 3195 CB PHE A 412 8.592 43.050 -16.583 1.00 19.41 C ANISOU 3195 CB PHE A 412 2489 2305 2583 -11 -80 33 C ATOM 3196 CG PHE A 412 9.670 42.952 -17.635 1.00 19.35 C ANISOU 3196 CG PHE A 412 2443 2257 2654 -35 -81 34 C ATOM 3197 CD1 PHE A 412 9.429 43.171 -18.971 1.00 19.43 C ANISOU 3197 CD1 PHE A 412 2423 2305 2657 8 -60 157 C ATOM 3198 CD2 PHE A 412 10.965 42.582 -17.277 1.00 19.27 C ANISOU 3198 CD2 PHE A 412 2384 2267 2670 -62 -48 79 C ATOM 3199 CE1 PHE A 412 10.399 43.029 -19.947 1.00 20.68 C ANISOU 3199 CE1 PHE A 412 2515 2552 2790 62 -35 193 C ATOM 3200 CE2 PHE A 412 11.948 42.457 -18.230 1.00 19.66 C ANISOU 3200 CE2 PHE A 412 2459 2415 2598 -40 -73 39 C ATOM 3201 CZ PHE A 412 11.702 42.669 -19.583 1.00 20.11 C ANISOU 3201 CZ PHE A 412 2467 2509 2665 -52 -38 159 C ATOM 3202 N ASP A 413 5.593 41.209 -15.543 1.00 22.67 N ANISOU 3202 N ASP A 413 2895 2561 3158 37 -61 51 N ATOM 3203 CA ASP A 413 4.639 41.002 -14.471 1.00 24.58 C ANISOU 3203 CA ASP A 413 3355 2811 3172 -3 99 113 C ATOM 3204 C ASP A 413 4.778 39.639 -13.810 1.00 22.24 C ANISOU 3204 C ASP A 413 2877 2744 2831 -20 -5 21 C ATOM 3205 O ASP A 413 4.641 38.600 -14.479 1.00 22.08 O ANISOU 3205 O ASP A 413 2834 2660 2894 -143 51 70 O ATOM 3206 CB ASP A 413 3.281 41.026 -15.186 1.00 30.27 C ANISOU 3206 CB ASP A 413 3723 3904 3872 -66 -193 56 C ATOM 3207 CG ASP A 413 2.207 41.765 -14.465 1.00 35.42 C ANISOU 3207 CG ASP A 413 4460 4412 4587 191 64 -56 C ATOM 3208 OD1 ASP A 413 2.317 41.756 -13.228 1.00 37.23 O ANISOU 3208 OD1 ASP A 413 4719 4743 4684 20 -55 26 O ATOM 3209 OD2 ASP A 413 1.309 42.297 -15.172 1.00 38.13 O ANISOU 3209 OD2 ASP A 413 4758 4778 4951 149 -169 105 O ATOM 3210 N ILE A 414 4.970 39.590 -12.506 1.00 19.91 N ANISOU 3210 N ILE A 414 2494 2358 2715 -29 75 13 N ATOM 3211 CA ILE A 414 5.049 38.308 -11.775 1.00 20.46 C ANISOU 3211 CA ILE A 414 2503 2453 2817 -38 -6 76 C ATOM 3212 C ILE A 414 3.729 37.582 -11.752 1.00 18.48 C ANISOU 3212 C ILE A 414 2358 2174 2490 105 22 65 C ATOM 3213 O ILE A 414 3.636 36.355 -11.618 1.00 17.58 O ANISOU 3213 O ILE A 414 2092 2121 2467 189 0 66 O ATOM 3214 CB ILE A 414 5.548 38.547 -10.330 1.00 23.48 C ANISOU 3214 CB ILE A 414 3045 2963 2915 -86 -62 57 C ATOM 3215 CG1 ILE A 414 7.039 38.880 -10.561 1.00 26.62 C ANISOU 3215 CG1 ILE A 414 3115 3453 3547 -85 -3 102 C ATOM 3216 CG2 ILE A 414 5.484 37.358 -9.401 1.00 24.12 C ANISOU 3216 CG2 ILE A 414 3046 2985 3133 -42 -31 105 C ATOM 3217 CD1 ILE A 414 7.851 39.253 -9.335 1.00 28.57 C ANISOU 3217 CD1 ILE A 414 3521 3715 3620 13 -123 95 C ATOM 3218 N SER A 415 2.626 38.318 -11.898 1.00 17.63 N ANISOU 3218 N SER A 415 2288 2023 2389 88 95 26 N ATOM 3219 CA SER A 415 1.307 37.706 -11.854 1.00 18.04 C ANISOU 3219 CA SER A 415 2274 2218 2362 86 21 -43 C ATOM 3220 C SER A 415 1.081 36.666 -12.934 1.00 16.12 C ANISOU 3220 C SER A 415 1946 1972 2205 143 132 56 C ATOM 3221 O SER A 415 0.346 35.700 -12.703 1.00 15.69 O ANISOU 3221 O SER A 415 2035 1596 2331 289 137 -87 O ATOM 3222 CB SER A 415 0.243 38.829 -11.874 1.00 20.75 C ANISOU 3222 CB SER A 415 2589 2582 2711 305 67 105 C ATOM 3223 OG SER A 415 0.056 39.283 -13.210 1.00 22.36 O ANISOU 3223 OG SER A 415 2870 2762 2865 329 38 145 O ATOM 3224 N TYR A 416 1.696 36.763 -14.118 1.00 14.42 N ANISOU 3224 N TYR A 416 1812 1665 2003 196 -53 170 N ATOM 3225 CA TYR A 416 1.692 35.697 -15.107 1.00 13.87 C ANISOU 3225 CA TYR A 416 1744 1621 1905 129 6 222 C ATOM 3226 C TYR A 416 2.114 34.353 -14.514 1.00 13.60 C ANISOU 3226 C TYR A 416 1641 1593 1933 203 -72 192 C ATOM 3227 O TYR A 416 1.550 33.320 -14.916 1.00 14.29 O ANISOU 3227 O TYR A 416 1699 1803 1926 180 -223 159 O ATOM 3228 CB TYR A 416 2.615 36.073 -16.273 1.00 13.97 C ANISOU 3228 CB TYR A 416 1866 1556 1886 145 31 234 C ATOM 3229 CG TYR A 416 2.796 35.038 -17.350 1.00 15.70 C ANISOU 3229 CG TYR A 416 2075 1906 1985 49 -1 75 C ATOM 3230 CD1 TYR A 416 1.953 34.949 -18.468 1.00 15.72 C ANISOU 3230 CD1 TYR A 416 2051 1941 1982 -62 -11 147 C ATOM 3231 CD2 TYR A 416 3.840 34.096 -17.213 1.00 15.23 C ANISOU 3231 CD2 TYR A 416 1958 1788 2040 11 100 133 C ATOM 3232 CE1 TYR A 416 2.181 33.955 -19.425 1.00 16.46 C ANISOU 3232 CE1 TYR A 416 2109 2036 2110 6 3 88 C ATOM 3233 CE2 TYR A 416 4.079 33.145 -18.180 1.00 15.17 C ANISOU 3233 CE2 TYR A 416 2061 1717 1987 -71 67 156 C ATOM 3234 CZ TYR A 416 3.234 33.074 -19.262 1.00 16.81 C ANISOU 3234 CZ TYR A 416 2203 2017 2167 -10 0 112 C ATOM 3235 OH TYR A 416 3.470 32.116 -20.219 1.00 17.22 O ANISOU 3235 OH TYR A 416 2386 2054 2104 -50 -5 151 O ATOM 3236 N TYR A 417 3.090 34.365 -13.597 1.00 13.19 N ANISOU 3236 N TYR A 417 1586 1485 1942 112 -23 67 N ATOM 3237 CA TYR A 417 3.680 33.085 -13.128 1.00 12.93 C ANISOU 3237 CA TYR A 417 1511 1608 1794 60 -121 200 C ATOM 3238 C TYR A 417 2.870 32.471 -12.000 1.00 13.92 C ANISOU 3238 C TYR A 417 1801 1692 1794 77 -3 113 C ATOM 3239 O TYR A 417 2.986 31.276 -11.726 1.00 13.28 O ANISOU 3239 O TYR A 417 1633 1545 1866 -174 53 35 O ATOM 3240 CB TYR A 417 5.145 33.339 -12.696 1.00 12.15 C ANISOU 3240 CB TYR A 417 1479 1403 1735 134 -22 95 C ATOM 3241 CG TYR A 417 5.940 33.640 -13.968 1.00 12.75 C ANISOU 3241 CG TYR A 417 1569 1597 1680 143 -43 126 C ATOM 3242 CD1 TYR A 417 6.209 34.927 -14.358 1.00 11.90 C ANISOU 3242 CD1 TYR A 417 1342 1562 1619 69 -39 -40 C ATOM 3243 CD2 TYR A 417 6.371 32.568 -14.769 1.00 13.34 C ANISOU 3243 CD2 TYR A 417 1617 1722 1731 106 2 14 C ATOM 3244 CE1 TYR A 417 6.904 35.161 -15.535 1.00 13.61 C ANISOU 3244 CE1 TYR A 417 1663 1762 1743 104 60 139 C ATOM 3245 CE2 TYR A 417 7.074 32.786 -15.939 1.00 13.94 C ANISOU 3245 CE2 TYR A 417 1642 1848 1807 122 -20 134 C ATOM 3246 CZ TYR A 417 7.338 34.096 -16.307 1.00 14.49 C ANISOU 3246 CZ TYR A 417 1821 1843 1840 68 73 58 C ATOM 3247 OH TYR A 417 8.033 34.367 -17.478 1.00 14.64 O ANISOU 3247 OH TYR A 417 1848 2008 1705 242 -19 214 O ATOM 3248 N LEU A 418 2.100 33.293 -11.275 1.00 13.97 N ANISOU 3248 N LEU A 418 1712 1732 1863 123 -20 67 N ATOM 3249 CA LEU A 418 1.386 32.813 -10.100 1.00 14.28 C ANISOU 3249 CA LEU A 418 1716 1869 1839 20 -42 116 C ATOM 3250 C LEU A 418 -0.086 32.559 -10.362 1.00 13.60 C ANISOU 3250 C LEU A 418 1684 1697 1786 99 -42 56 C ATOM 3251 O LEU A 418 -0.840 32.229 -9.422 1.00 13.71 O ANISOU 3251 O LEU A 418 1686 1657 1866 56 -50 88 O ATOM 3252 CB LEU A 418 1.483 33.811 -8.933 1.00 17.14 C ANISOU 3252 CB LEU A 418 2259 2161 2090 74 -73 -66 C ATOM 3253 CG LEU A 418 2.890 34.201 -8.484 1.00 21.15 C ANISOU 3253 CG LEU A 418 2435 2892 2709 -7 -110 -239 C ATOM 3254 CD1 LEU A 418 2.943 34.815 -7.076 1.00 23.34 C ANISOU 3254 CD1 LEU A 418 2799 3343 2725 -145 -79 -336 C ATOM 3255 CD2 LEU A 418 3.831 33.035 -8.493 1.00 21.47 C ANISOU 3255 CD2 LEU A 418 2666 2795 2696 81 -310 -85 C ATOM 3256 N LYS A 419 -0.520 32.633 -11.620 1.00 12.77 N ANISOU 3256 N LYS A 419 1611 1508 1733 68 35 102 N ATOM 3257 CA LYS A 419 -1.961 32.606 -11.894 1.00 13.68 C ANISOU 3257 CA LYS A 419 1691 1564 1942 45 -18 109 C ATOM 3258 C LYS A 419 -2.642 31.280 -11.575 1.00 12.93 C ANISOU 3258 C LYS A 419 1603 1520 1791 127 -19 129 C ATOM 3259 O LYS A 419 -3.881 31.204 -11.547 1.00 12.90 O ANISOU 3259 O LYS A 419 1600 1456 1845 280 -13 309 O ATOM 3260 CB LYS A 419 -2.141 32.950 -13.376 1.00 15.16 C ANISOU 3260 CB LYS A 419 1916 1944 1899 33 -113 75 C ATOM 3261 CG LYS A 419 -1.535 31.923 -14.353 1.00 16.83 C ANISOU 3261 CG LYS A 419 2090 1940 2364 47 29 -24 C ATOM 3262 CD LYS A 419 -1.951 32.374 -15.763 1.00 20.34 C ANISOU 3262 CD LYS A 419 2591 2667 2472 -62 -87 36 C ATOM 3263 CE LYS A 419 -1.230 31.495 -16.791 1.00 22.49 C ANISOU 3263 CE LYS A 419 2954 2799 2793 144 -51 -12 C ATOM 3264 NZ LYS A 419 0.099 32.126 -17.152 1.00 22.05 N ANISOU 3264 NZ LYS A 419 2691 2988 2700 342 -156 -35 N ATOM 3265 N HIS A 420 -1.881 30.175 -11.439 1.00 10.77 N ANISOU 3265 N HIS A 420 1146 1447 1499 165 71 10 N ATOM 3266 CA HIS A 420 -2.514 28.893 -11.147 1.00 11.60 C ANISOU 3266 CA HIS A 420 1566 1374 1468 132 -41 1 C ATOM 3267 C HIS A 420 -2.097 28.346 -9.778 1.00 10.81 C ANISOU 3267 C HIS A 420 1353 1376 1379 199 104 -32 C ATOM 3268 O HIS A 420 -2.458 27.208 -9.432 1.00 10.17 O ANISOU 3268 O HIS A 420 1328 1305 1231 284 39 -14 O ATOM 3269 CB HIS A 420 -2.214 27.806 -12.208 1.00 12.17 C ANISOU 3269 CB HIS A 420 1377 1585 1661 298 45 -136 C ATOM 3270 CG HIS A 420 -2.917 28.155 -13.501 1.00 14.88 C ANISOU 3270 CG HIS A 420 2053 1827 1775 288 -20 -52 C ATOM 3271 ND1 HIS A 420 -4.304 28.298 -13.545 1.00 17.49 N ANISOU 3271 ND1 HIS A 420 2129 2389 2127 185 -38 22 N ATOM 3272 CD2 HIS A 420 -2.443 28.436 -14.722 1.00 16.27 C ANISOU 3272 CD2 HIS A 420 2243 2029 1908 172 30 -12 C ATOM 3273 CE1 HIS A 420 -4.642 28.650 -14.789 1.00 19.38 C ANISOU 3273 CE1 HIS A 420 2488 2672 2202 223 -24 62 C ATOM 3274 NE2 HIS A 420 -3.530 28.719 -15.500 1.00 18.43 N ANISOU 3274 NE2 HIS A 420 2535 2401 2066 306 -12 73 N ATOM 3275 N VAL A 421 -1.481 29.155 -8.955 1.00 11.70 N ANISOU 3275 N VAL A 421 1327 1595 1525 138 -19 14 N ATOM 3276 CA VAL A 421 -1.271 28.725 -7.540 1.00 11.96 C ANISOU 3276 CA VAL A 421 1395 1594 1555 135 12 95 C ATOM 3277 C VAL A 421 -2.546 28.282 -6.840 1.00 12.07 C ANISOU 3277 C VAL A 421 1413 1418 1754 54 -42 122 C ATOM 3278 O VAL A 421 -2.556 27.234 -6.151 1.00 10.39 O ANISOU 3278 O VAL A 421 1088 1186 1675 345 -132 67 O ATOM 3279 CB VAL A 421 -0.633 29.879 -6.754 1.00 13.48 C ANISOU 3279 CB VAL A 421 1669 1779 1673 22 4 65 C ATOM 3280 CG1 VAL A 421 -0.586 29.572 -5.241 1.00 13.88 C ANISOU 3280 CG1 VAL A 421 1766 1872 1635 -60 -112 41 C ATOM 3281 CG2 VAL A 421 0.780 30.200 -7.248 1.00 14.33 C ANISOU 3281 CG2 VAL A 421 1620 1787 2039 121 -33 150 C ATOM 3282 N ASP A 422 -3.642 29.068 -6.947 1.00 11.58 N ANISOU 3282 N ASP A 422 1408 1288 1703 157 -206 -36 N ATOM 3283 CA ASP A 422 -4.873 28.701 -6.241 1.00 15.38 C ANISOU 3283 CA ASP A 422 1686 2028 2129 -22 4 17 C ATOM 3284 C ASP A 422 -5.430 27.354 -6.685 1.00 15.11 C ANISOU 3284 C ASP A 422 1712 1788 2241 257 -162 -12 C ATOM 3285 O ASP A 422 -5.944 26.578 -5.884 1.00 16.37 O ANISOU 3285 O ASP A 422 1940 2167 2113 24 -8 -24 O ATOM 3286 CB ASP A 422 -5.940 29.794 -6.462 1.00 17.23 C ANISOU 3286 CB ASP A 422 2036 2093 2417 178 54 62 C ATOM 3287 CG ASP A 422 -5.654 31.139 -5.833 1.00 22.05 C ANISOU 3287 CG ASP A 422 2792 2502 3084 -32 107 -140 C ATOM 3288 OD1 ASP A 422 -4.642 31.036 -5.043 1.00 23.92 O ANISOU 3288 OD1 ASP A 422 2992 2865 3231 -72 10 -253 O ATOM 3289 OD2 ASP A 422 -6.173 32.259 -5.877 1.00 22.13 O ANISOU 3289 OD2 ASP A 422 2926 2521 2960 143 9 -156 O ATOM 3290 N HIS A 423 -5.367 27.058 -7.978 1.00 15.74 N ANISOU 3290 N HIS A 423 1775 2051 2154 256 -161 55 N ATOM 3291 CA HIS A 423 -5.809 25.773 -8.529 1.00 16.33 C ANISOU 3291 CA HIS A 423 1946 1966 2294 194 -127 20 C ATOM 3292 C HIS A 423 -5.022 24.616 -7.898 1.00 13.39 C ANISOU 3292 C HIS A 423 1499 1774 1814 49 2 -72 C ATOM 3293 O HIS A 423 -5.623 23.569 -7.620 1.00 13.29 O ANISOU 3293 O HIS A 423 1330 1738 1982 124 -123 34 O ATOM 3294 CB HIS A 423 -5.659 25.707 -10.038 1.00 18.52 C ANISOU 3294 CB HIS A 423 2238 2381 2416 34 -75 69 C ATOM 3295 CG HIS A 423 -6.096 24.436 -10.722 1.00 22.61 C ANISOU 3295 CG HIS A 423 2985 2687 2920 28 -89 -161 C ATOM 3296 ND1 HIS A 423 -7.307 24.329 -11.403 1.00 24.98 N ANISOU 3296 ND1 HIS A 423 2973 3089 3431 75 -153 -139 N ATOM 3297 CD2 HIS A 423 -5.481 23.237 -10.887 1.00 23.29 C ANISOU 3297 CD2 HIS A 423 2950 2873 3024 110 13 -128 C ATOM 3298 CE1 HIS A 423 -7.425 23.114 -11.921 1.00 25.40 C ANISOU 3298 CE1 HIS A 423 3103 3130 3418 1 -82 -186 C ATOM 3299 NE2 HIS A 423 -6.332 22.428 -11.609 1.00 24.56 N ANISOU 3299 NE2 HIS A 423 3073 3027 3230 18 -57 -172 N ATOM 3300 N ILE A 424 -3.726 24.810 -7.707 1.00 10.62 N ANISOU 3300 N ILE A 424 1356 1337 1344 236 -95 -14 N ATOM 3301 CA ILE A 424 -2.917 23.689 -7.122 1.00 10.15 C ANISOU 3301 CA ILE A 424 1222 1210 1422 86 -22 -50 C ATOM 3302 C ILE A 424 -3.331 23.492 -5.685 1.00 10.35 C ANISOU 3302 C ILE A 424 1199 1266 1470 35 -25 -5 C ATOM 3303 O ILE A 424 -3.497 22.373 -5.217 1.00 11.25 O ANISOU 3303 O ILE A 424 1370 1303 1599 -58 115 -87 O ATOM 3304 CB ILE A 424 -1.412 23.979 -7.270 1.00 9.91 C ANISOU 3304 CB ILE A 424 1173 1306 1286 151 -66 -71 C ATOM 3305 CG1 ILE A 424 -1.012 24.093 -8.765 1.00 9.64 C ANISOU 3305 CG1 ILE A 424 1044 1199 1418 -149 122 -2 C ATOM 3306 CG2 ILE A 424 -0.539 22.904 -6.574 1.00 9.95 C ANISOU 3306 CG2 ILE A 424 1282 1188 1308 46 -62 83 C ATOM 3307 CD1 ILE A 424 0.375 24.695 -9.011 1.00 10.07 C ANISOU 3307 CD1 ILE A 424 949 1544 1334 -157 -3 -124 C ATOM 3308 N PHE A 425 -3.480 24.568 -4.892 1.00 10.61 N ANISOU 3308 N PHE A 425 1186 1360 1486 87 44 -54 N ATOM 3309 CA PHE A 425 -3.849 24.401 -3.483 1.00 11.12 C ANISOU 3309 CA PHE A 425 1373 1390 1463 122 -72 -37 C ATOM 3310 C PHE A 425 -5.230 23.765 -3.363 1.00 11.70 C ANISOU 3310 C PHE A 425 1427 1396 1623 58 22 -77 C ATOM 3311 O PHE A 425 -5.456 22.998 -2.432 1.00 12.35 O ANISOU 3311 O PHE A 425 1500 1424 1770 261 -62 63 O ATOM 3312 CB PHE A 425 -3.826 25.744 -2.722 1.00 10.82 C ANISOU 3312 CB PHE A 425 1288 1362 1459 55 -96 -56 C ATOM 3313 CG PHE A 425 -2.472 26.123 -2.138 1.00 10.34 C ANISOU 3313 CG PHE A 425 1298 1217 1413 54 -2 -4 C ATOM 3314 CD1 PHE A 425 -1.485 26.654 -2.951 1.00 9.40 C ANISOU 3314 CD1 PHE A 425 1186 961 1424 43 -53 -17 C ATOM 3315 CD2 PHE A 425 -2.197 25.920 -0.798 1.00 10.56 C ANISOU 3315 CD2 PHE A 425 1326 1247 1441 172 -104 -109 C ATOM 3316 CE1 PHE A 425 -0.246 26.998 -2.409 1.00 9.71 C ANISOU 3316 CE1 PHE A 425 1214 1053 1424 145 -56 -4 C ATOM 3317 CE2 PHE A 425 -0.977 26.259 -0.253 1.00 10.56 C ANISOU 3317 CE2 PHE A 425 1265 1196 1552 51 20 -19 C ATOM 3318 CZ PHE A 425 0.034 26.815 -1.053 1.00 9.37 C ANISOU 3318 CZ PHE A 425 1416 792 1354 194 88 12 C ATOM 3319 N GLU A 426 -6.173 24.096 -4.250 1.00 12.29 N ANISOU 3319 N GLU A 426 1750 1348 1574 181 -83 -162 N ATOM 3320 CA GLU A 426 -7.507 23.459 -4.246 1.00 16.08 C ANISOU 3320 CA GLU A 426 1944 1941 2226 -94 13 -95 C ATOM 3321 C GLU A 426 -7.536 21.939 -4.355 1.00 15.96 C ANISOU 3321 C GLU A 426 2143 1843 2079 86 -53 46 C ATOM 3322 O GLU A 426 -8.406 21.296 -3.723 1.00 15.52 O ANISOU 3322 O GLU A 426 1775 1839 2285 110 -5 63 O ATOM 3323 CB GLU A 426 -8.163 24.159 -5.425 1.00 19.02 C ANISOU 3323 CB GLU A 426 2493 2325 2411 31 -10 140 C ATOM 3324 CG GLU A 426 -9.616 23.942 -5.639 1.00 23.95 C ANISOU 3324 CG GLU A 426 2763 2959 3378 11 -16 -32 C ATOM 3325 CD GLU A 426 -10.060 24.387 -7.003 1.00 28.31 C ANISOU 3325 CD GLU A 426 3505 3630 3619 121 -108 135 C ATOM 3326 OE1 GLU A 426 -9.546 25.208 -7.749 1.00 28.68 O ANISOU 3326 OE1 GLU A 426 3521 3720 3654 102 -68 129 O ATOM 3327 OE2 GLU A 426 -11.064 23.896 -7.524 1.00 30.63 O ANISOU 3327 OE2 GLU A 426 3820 3741 4078 148 -217 -20 O ATOM 3328 N ARG A 427 -6.508 21.376 -5.046 1.00 15.71 N ANISOU 3328 N ARG A 427 1989 2031 1947 61 -70 59 N ATOM 3329 CA ARG A 427 -6.424 19.885 -5.117 1.00 16.01 C ANISOU 3329 CA ARG A 427 1993 2050 2041 107 122 -64 C ATOM 3330 C ARG A 427 -6.241 19.216 -3.757 1.00 16.65 C ANISOU 3330 C ARG A 427 2124 2018 2184 76 16 -14 C ATOM 3331 O ARG A 427 -6.492 18.010 -3.614 1.00 17.88 O ANISOU 3331 O ARG A 427 2471 2078 2244 -144 287 98 O ATOM 3332 CB ARG A 427 -5.205 19.510 -5.954 1.00 15.55 C ANISOU 3332 CB ARG A 427 1948 1995 1966 84 72 -50 C ATOM 3333 CG ARG A 427 -5.274 19.968 -7.406 1.00 15.01 C ANISOU 3333 CG ARG A 427 1819 1955 1929 94 229 -22 C ATOM 3334 CD ARG A 427 -3.891 19.817 -8.101 1.00 15.74 C ANISOU 3334 CD ARG A 427 1740 2298 1941 40 183 -80 C ATOM 3335 NE ARG A 427 -4.123 19.837 -9.568 1.00 17.71 N ANISOU 3335 NE ARG A 427 1879 2739 2111 106 54 46 N ATOM 3336 CZ ARG A 427 -3.122 19.878 -10.470 1.00 17.96 C ANISOU 3336 CZ ARG A 427 2077 2618 2130 12 89 76 C ATOM 3337 NH1 ARG A 427 -1.849 19.952 -10.082 1.00 16.18 N ANISOU 3337 NH1 ARG A 427 1927 2137 2084 63 114 127 N ATOM 3338 NH2 ARG A 427 -3.408 19.853 -11.784 1.00 18.70 N ANISOU 3338 NH2 ARG A 427 2169 2671 2267 177 -94 114 N ATOM 3339 N PHE A 428 -5.793 19.982 -2.763 1.00 15.01 N ANISOU 3339 N PHE A 428 1681 1928 2092 121 81 -51 N ATOM 3340 CA PHE A 428 -5.485 19.399 -1.458 1.00 17.45 C ANISOU 3340 CA PHE A 428 2209 2117 2305 44 -65 106 C ATOM 3341 C PHE A 428 -6.580 19.780 -0.417 1.00 22.22 C ANISOU 3341 C PHE A 428 2827 2892 2725 -94 229 -67 C ATOM 3342 O PHE A 428 -6.450 19.396 0.750 1.00 21.29 O ANISOU 3342 O PHE A 428 2597 2718 2773 163 222 69 O ATOM 3343 CB PHE A 428 -4.227 20.040 -0.824 1.00 15.76 C ANISOU 3343 CB PHE A 428 2094 1983 1910 133 33 79 C ATOM 3344 CG PHE A 428 -3.053 19.512 -1.616 1.00 15.06 C ANISOU 3344 CG PHE A 428 1929 1871 1922 69 -29 -11 C ATOM 3345 CD1 PHE A 428 -2.549 20.229 -2.668 1.00 14.37 C ANISOU 3345 CD1 PHE A 428 1743 1843 1876 24 -50 -97 C ATOM 3346 CD2 PHE A 428 -2.495 18.287 -1.275 1.00 15.61 C ANISOU 3346 CD2 PHE A 428 1956 2051 1923 199 -61 -23 C ATOM 3347 CE1 PHE A 428 -1.502 19.750 -3.440 1.00 14.28 C ANISOU 3347 CE1 PHE A 428 1645 1761 2020 78 -67 -105 C ATOM 3348 CE2 PHE A 428 -1.418 17.795 -2.013 1.00 14.14 C ANISOU 3348 CE2 PHE A 428 1683 1834 1856 98 -164 33 C ATOM 3349 CZ PHE A 428 -0.918 18.505 -3.075 1.00 13.51 C ANISOU 3349 CZ PHE A 428 1585 1754 1795 47 -71 -62 C ATOM 3350 N GLU A 429 -7.590 20.550 -0.820 1.00 28.87 N ANISOU 3350 N GLU A 429 3429 3682 3858 3 -229 111 N ATOM 3351 CA GLU A 429 -8.651 20.970 0.103 1.00 36.69 C ANISOU 3351 CA GLU A 429 4594 4858 4488 175 213 -67 C ATOM 3352 C GLU A 429 -9.709 19.774 0.322 1.00 41.34 C ANISOU 3352 C GLU A 429 5028 5183 5498 -111 -79 86 C ATOM 3353 O GLU A 429 -9.573 18.696 -0.269 1.00 41.81 O ANISOU 3353 O GLU A 429 5167 5327 5392 -95 40 36 O ATOM 3354 CB GLU A 429 -9.330 22.233 -0.479 1.00 39.91 C ANISOU 3354 CB GLU A 429 5058 4970 5137 -11 15 6 C ATOM 3355 CG GLU A 429 -8.542 23.524 -0.294 1.00 41.75 C ANISOU 3355 CG GLU A 429 5183 5277 5402 134 28 5 C ATOM 3356 CD GLU A 429 -8.273 23.861 1.164 1.00 41.99 C ANISOU 3356 CD GLU A 429 5236 5286 5433 132 -9 38 C ATOM 3357 OE1 GLU A 429 -7.550 24.850 1.421 1.00 42.57 O ANISOU 3357 OE1 GLU A 429 5318 5521 5334 231 -55 165 O ATOM 3358 OE2 GLU A 429 -8.775 23.137 2.048 1.00 42.97 O ANISOU 3358 OE2 GLU A 429 5325 5550 5450 70 10 49 O ATOM 3359 N LYS A 430 -10.608 19.601 1.172 1.00 46.16 N ANISOU 3359 N LYS A 430 5939 5869 5731 140 96 -95 N ATOM 3360 CA LYS A 430 -11.884 19.202 1.658 1.00 50.57 C ANISOU 3360 CA LYS A 430 6272 6522 6421 -132 155 71 C ATOM 3361 C LYS A 430 -12.841 18.583 0.653 1.00 52.03 C ANISOU 3361 C LYS A 430 6572 6642 6553 -108 17 15 C ATOM 3362 O LYS A 430 -12.487 17.515 0.105 1.00 53.63 O ANISOU 3362 O LYS A 430 6882 6701 6792 -3 81 14 O ATOM 3363 CB LYS A 430 -12.630 20.472 2.174 1.00 52.82 C ANISOU 3363 CB LYS A 430 6637 6730 6703 83 106 3 C ATOM 3364 CG LYS A 430 -11.765 21.389 3.005 1.00 55.09 C ANISOU 3364 CG LYS A 430 6954 6994 6983 -64 -25 -37 C ATOM 3365 CD LYS A 430 -12.476 22.623 3.536 1.00 56.72 C ANISOU 3365 CD LYS A 430 7183 7125 7243 52 19 -57 C ATOM 3366 CE LYS A 430 -11.805 23.037 4.846 1.00 57.64 C ANISOU 3366 CE LYS A 430 7346 7278 7278 -11 -23 -55 C ATOM 3367 NZ LYS A 430 -11.857 24.515 5.028 1.00 58.15 N ANISOU 3367 NZ LYS A 430 7462 7262 7370 53 27 -38 N TER 3368 LYS A 430 ATOM 3369 N VAL B 2 25.729 1.642 -20.113 1.00 35.10 N ANISOU 3369 N VAL B 2 4395 4469 4471 66 36 92 N ATOM 3370 CA VAL B 2 24.976 2.743 -20.810 1.00 34.66 C ANISOU 3370 CA VAL B 2 4447 4343 4380 26 23 23 C ATOM 3371 C VAL B 2 25.860 3.378 -21.872 1.00 35.21 C ANISOU 3371 C VAL B 2 4456 4488 4434 -6 52 2 C ATOM 3372 O VAL B 2 26.783 4.126 -21.575 1.00 36.40 O ANISOU 3372 O VAL B 2 4645 4510 4674 -45 -32 -65 O ATOM 3373 CB VAL B 2 24.417 3.745 -19.795 1.00 34.02 C ANISOU 3373 CB VAL B 2 4320 4293 4313 20 43 97 C ATOM 3374 CG1 VAL B 2 23.851 5.023 -20.393 1.00 33.83 C ANISOU 3374 CG1 VAL B 2 4251 4320 4281 71 19 74 C ATOM 3375 CG2 VAL B 2 23.298 3.111 -18.959 1.00 34.28 C ANISOU 3375 CG2 VAL B 2 4309 4318 4400 1 64 77 C ATOM 3376 N GLU B 3 25.531 3.136 -23.150 1.00 35.67 N ANISOU 3376 N GLU B 3 4515 4599 4437 36 35 -2 N ATOM 3377 CA GLU B 3 26.442 3.442 -24.251 1.00 35.81 C ANISOU 3377 CA GLU B 3 4588 4567 4453 -62 18 16 C ATOM 3378 C GLU B 3 26.804 4.919 -24.315 1.00 35.84 C ANISOU 3378 C GLU B 3 4524 4532 4561 10 52 -44 C ATOM 3379 O GLU B 3 27.939 5.271 -24.663 1.00 36.36 O ANISOU 3379 O GLU B 3 4490 4637 4688 -108 -12 -114 O ATOM 3380 CB GLU B 3 25.829 2.976 -25.571 1.00 36.71 C ANISOU 3380 CB GLU B 3 4650 4779 4519 -30 -35 -78 C ATOM 3381 N ARG B 4 25.869 5.808 -23.949 1.00 35.76 N ANISOU 3381 N ARG B 4 4515 4505 4569 37 4 -20 N ATOM 3382 CA ARG B 4 26.228 7.232 -23.953 1.00 35.50 C ANISOU 3382 CA ARG B 4 4445 4500 4544 35 -33 -45 C ATOM 3383 C ARG B 4 27.390 7.578 -23.032 1.00 35.34 C ANISOU 3383 C ARG B 4 4457 4499 4471 36 -23 2 C ATOM 3384 O ARG B 4 27.954 8.678 -23.267 1.00 36.49 O ANISOU 3384 O ARG B 4 4644 4595 4627 -66 29 11 O ATOM 3385 CB ARG B 4 25.018 8.118 -23.699 1.00 36.26 C ANISOU 3385 CB ARG B 4 4502 4638 4637 88 21 -40 C ATOM 3386 CG ARG B 4 24.458 8.165 -22.300 1.00 36.94 C ANISOU 3386 CG ARG B 4 4640 4735 4658 110 31 -55 C ATOM 3387 CD ARG B 4 23.452 9.304 -22.140 1.00 37.54 C ANISOU 3387 CD ARG B 4 4786 4705 4773 167 -42 50 C ATOM 3388 NE ARG B 4 22.793 9.767 -23.370 1.00 38.79 N ANISOU 3388 NE ARG B 4 5141 4768 4831 108 -129 101 N ATOM 3389 CZ ARG B 4 22.522 11.082 -23.486 1.00 39.38 C ANISOU 3389 CZ ARG B 4 5297 4803 4864 96 -163 38 C ATOM 3390 NH1 ARG B 4 22.881 11.913 -22.490 1.00 40.71 N ANISOU 3390 NH1 ARG B 4 5402 5113 4952 -25 -108 -121 N ATOM 3391 NH2 ARG B 4 21.928 11.611 -24.558 1.00 39.93 N ANISOU 3391 NH2 ARG B 4 5229 5061 4882 143 -184 93 N ATOM 3392 N TYR B 5 27.752 6.798 -22.011 1.00 34.08 N ANISOU 3392 N TYR B 5 4239 4304 4407 54 19 -6 N ATOM 3393 CA TYR B 5 28.949 7.101 -21.238 1.00 34.35 C ANISOU 3393 CA TYR B 5 4307 4356 4390 3 -3 -52 C ATOM 3394 C TYR B 5 30.168 6.275 -21.642 1.00 34.95 C ANISOU 3394 C TYR B 5 4348 4377 4555 49 -18 -30 C ATOM 3395 O TYR B 5 31.218 6.432 -21.025 1.00 35.27 O ANISOU 3395 O TYR B 5 4450 4339 4611 50 -120 -111 O ATOM 3396 CB TYR B 5 28.680 7.004 -19.717 1.00 33.71 C ANISOU 3396 CB TYR B 5 4181 4255 4373 7 -14 -50 C ATOM 3397 CG TYR B 5 27.402 7.742 -19.344 1.00 33.41 C ANISOU 3397 CG TYR B 5 4175 4218 4300 3 -16 -17 C ATOM 3398 CD1 TYR B 5 26.368 7.105 -18.672 1.00 33.54 C ANISOU 3398 CD1 TYR B 5 4252 4277 4215 46 45 -5 C ATOM 3399 CD2 TYR B 5 27.215 9.070 -19.728 1.00 33.06 C ANISOU 3399 CD2 TYR B 5 4109 4141 4313 -11 4 -73 C ATOM 3400 CE1 TYR B 5 25.178 7.771 -18.376 1.00 32.85 C ANISOU 3400 CE1 TYR B 5 4270 4135 4075 78 28 35 C ATOM 3401 CE2 TYR B 5 26.034 9.732 -19.444 1.00 32.55 C ANISOU 3401 CE2 TYR B 5 4152 3991 4224 -23 49 -88 C ATOM 3402 CZ TYR B 5 25.028 9.089 -18.757 1.00 32.23 C ANISOU 3402 CZ TYR B 5 4153 4029 4064 34 78 -60 C ATOM 3403 OH TYR B 5 23.847 9.776 -18.495 1.00 30.69 O ANISOU 3403 OH TYR B 5 4156 3736 3770 -44 116 77 O ATOM 3404 N SER B 6 30.111 5.457 -22.699 1.00 35.63 N ANISOU 3404 N SER B 6 4519 4487 4532 -3 47 -19 N ATOM 3405 CA SER B 6 31.277 4.643 -23.072 1.00 36.68 C ANISOU 3405 CA SER B 6 4495 4720 4722 31 73 0 C ATOM 3406 C SER B 6 32.230 5.440 -23.968 1.00 35.97 C ANISOU 3406 C SER B 6 4396 4656 4615 62 -6 35 C ATOM 3407 O SER B 6 31.787 6.190 -24.837 1.00 36.68 O ANISOU 3407 O SER B 6 4470 4816 4651 122 -32 97 O ATOM 3408 CB SER B 6 30.822 3.385 -23.827 1.00 38.51 C ANISOU 3408 CB SER B 6 4846 4860 4924 12 6 -106 C ATOM 3409 OG SER B 6 30.289 3.840 -25.090 1.00 40.58 O ANISOU 3409 OG SER B 6 5217 5232 4972 54 -29 -19 O ATOM 3410 N LEU B 7 33.534 5.326 -23.742 1.00 33.72 N ANISOU 3410 N LEU B 7 4256 4272 4282 8 98 56 N ATOM 3411 CA LEU B 7 34.590 6.049 -24.415 1.00 31.09 C ANISOU 3411 CA LEU B 7 3978 3862 3971 158 13 -54 C ATOM 3412 C LEU B 7 35.727 5.076 -24.803 1.00 29.23 C ANISOU 3412 C LEU B 7 3822 3628 3654 63 -55 97 C ATOM 3413 O LEU B 7 36.120 4.306 -23.959 1.00 25.76 O ANISOU 3413 O LEU B 7 3504 3090 3192 100 22 -157 O ATOM 3414 CB LEU B 7 35.234 7.109 -23.518 1.00 30.78 C ANISOU 3414 CB LEU B 7 3869 3874 3952 118 -42 3 C ATOM 3415 CG LEU B 7 34.361 8.253 -22.987 1.00 31.16 C ANISOU 3415 CG LEU B 7 3950 3924 3967 88 -36 -93 C ATOM 3416 CD1 LEU B 7 35.097 9.178 -22.025 1.00 29.89 C ANISOU 3416 CD1 LEU B 7 3780 3835 3742 98 41 -28 C ATOM 3417 CD2 LEU B 7 33.805 9.047 -24.172 1.00 31.49 C ANISOU 3417 CD2 LEU B 7 4033 3957 3974 100 -25 -42 C ATOM 3418 N SER B 8 36.252 5.209 -26.023 1.00 30.32 N ANISOU 3418 N SER B 8 3985 3817 3717 -34 54 13 N ATOM 3419 CA SER B 8 37.463 4.474 -26.418 1.00 31.63 C ANISOU 3419 CA SER B 8 4086 3997 3935 53 80 13 C ATOM 3420 C SER B 8 38.540 4.725 -25.418 1.00 33.16 C ANISOU 3420 C SER B 8 4218 4315 4065 60 6 -5 C ATOM 3421 O SER B 8 38.318 5.677 -24.704 1.00 36.46 O ANISOU 3421 O SER B 8 4795 4475 4583 31 -46 -158 O ATOM 3422 CB SER B 8 37.795 4.572 -27.901 1.00 32.20 C ANISOU 3422 CB SER B 8 4250 4089 3895 0 2 28 C ATOM 3423 OG SER B 8 36.840 3.696 -28.528 1.00 32.03 O ANISOU 3423 OG SER B 8 4287 4190 3693 3 -77 146 O ATOM 3424 N PRO B 9 39.629 4.011 -25.563 1.00 32.47 N ANISOU 3424 N PRO B 9 4129 4132 4075 -7 36 137 N ATOM 3425 CA PRO B 9 40.111 2.748 -25.132 1.00 29.86 C ANISOU 3425 CA PRO B 9 3795 3874 3678 -151 72 87 C ATOM 3426 C PRO B 9 39.340 1.842 -24.204 1.00 25.90 C ANISOU 3426 C PRO B 9 3273 3367 3202 37 54 -159 C ATOM 3427 O PRO B 9 39.429 0.621 -24.385 1.00 25.01 O ANISOU 3427 O PRO B 9 3239 3309 2956 26 205 -67 O ATOM 3428 CB PRO B 9 41.572 2.850 -24.663 1.00 31.53 C ANISOU 3428 CB PRO B 9 3827 4070 4083 -88 12 53 C ATOM 3429 CG PRO B 9 41.667 4.330 -24.506 1.00 33.02 C ANISOU 3429 CG PRO B 9 4249 4101 4198 -128 -23 32 C ATOM 3430 CD PRO B 9 40.936 4.717 -25.827 1.00 33.76 C ANISOU 3430 CD PRO B 9 4191 4295 4340 -106 -83 63 C ATOM 3431 N MET B 10 38.642 2.411 -23.238 1.00 22.22 N ANISOU 3431 N MET B 10 2916 2737 2790 -105 -50 95 N ATOM 3432 CA MET B 10 37.983 1.576 -22.249 1.00 19.34 C ANISOU 3432 CA MET B 10 2551 2457 2339 127 -13 -101 C ATOM 3433 C MET B 10 36.876 0.746 -22.867 1.00 20.40 C ANISOU 3433 C MET B 10 2769 2454 2530 45 -68 -62 C ATOM 3434 O MET B 10 36.700 -0.451 -22.594 1.00 20.04 O ANISOU 3434 O MET B 10 2743 2455 2417 25 25 6 O ATOM 3435 CB MET B 10 37.470 2.490 -21.116 1.00 15.72 C ANISOU 3435 CB MET B 10 2227 1743 2004 162 -68 264 C ATOM 3436 CG MET B 10 36.972 1.612 -19.963 1.00 12.71 C ANISOU 3436 CG MET B 10 1599 1299 1933 148 -1 1 C ATOM 3437 SD MET B 10 38.238 0.614 -19.123 1.00 6.98 S ANISOU 3437 SD MET B 10 774 263 1617 27 239 -88 S ATOM 3438 CE MET B 10 38.858 1.930 -18.072 1.00 10.28 C ANISOU 3438 CE MET B 10 1216 721 1967 -81 114 141 C ATOM 3439 N LYS B 11 36.072 1.326 -23.782 1.00 20.92 N ANISOU 3439 N LYS B 11 2869 2527 2552 159 -111 -54 N ATOM 3440 CA LYS B 11 34.918 0.522 -24.211 1.00 22.64 C ANISOU 3440 CA LYS B 11 2963 2768 2870 25 -17 -106 C ATOM 3441 C LYS B 11 35.387 -0.640 -25.095 1.00 21.18 C ANISOU 3441 C LYS B 11 2782 2607 2657 95 -115 34 C ATOM 3442 O LYS B 11 34.740 -1.687 -25.046 1.00 20.77 O ANISOU 3442 O LYS B 11 2745 2469 2679 223 -229 -98 O ATOM 3443 CB LYS B 11 33.897 1.352 -24.951 1.00 26.41 C ANISOU 3443 CB LYS B 11 3291 3227 3516 213 -175 42 C ATOM 3444 CG LYS B 11 34.329 1.760 -26.346 1.00 31.17 C ANISOU 3444 CG LYS B 11 4139 3991 3715 1 64 55 C ATOM 3445 CD LYS B 11 33.130 2.572 -26.894 1.00 35.42 C ANISOU 3445 CD LYS B 11 4390 4539 4527 218 -116 56 C ATOM 3446 CE LYS B 11 33.610 3.440 -28.047 1.00 38.41 C ANISOU 3446 CE LYS B 11 4903 4863 4830 -4 53 149 C ATOM 3447 NZ LYS B 11 34.036 2.591 -29.200 1.00 41.20 N ANISOU 3447 NZ LYS B 11 5345 5204 5104 29 57 -105 N ATOM 3448 N ASP B 12 36.526 -0.530 -25.735 1.00 19.93 N ANISOU 3448 N ASP B 12 2823 2385 2365 124 -120 132 N ATOM 3449 CA ASP B 12 37.073 -1.631 -26.535 1.00 21.70 C ANISOU 3449 CA ASP B 12 3155 2514 2575 222 -113 77 C ATOM 3450 C ASP B 12 37.451 -2.841 -25.694 1.00 19.50 C ANISOU 3450 C ASP B 12 2842 2349 2218 67 -65 -30 C ATOM 3451 O ASP B 12 37.488 -3.977 -26.169 1.00 18.49 O ANISOU 3451 O ASP B 12 2929 2322 1773 88 -80 53 O ATOM 3452 CB ASP B 12 38.310 -1.087 -27.298 1.00 25.92 C ANISOU 3452 CB ASP B 12 3372 3215 3261 -66 46 14 C ATOM 3453 CG ASP B 12 37.786 0.135 -28.083 1.00 31.05 C ANISOU 3453 CG ASP B 12 4283 3661 3852 63 -136 263 C ATOM 3454 OD1 ASP B 12 37.946 1.281 -27.610 1.00 33.49 O ANISOU 3454 OD1 ASP B 12 4615 3813 4298 -66 -45 163 O ATOM 3455 OD2 ASP B 12 37.118 -0.089 -29.112 1.00 33.08 O ANISOU 3455 OD2 ASP B 12 4699 4023 3847 5 -179 168 O ATOM 3456 N LEU B 13 37.786 -2.622 -24.425 1.00 17.19 N ANISOU 3456 N LEU B 13 2391 2041 2099 146 -21 50 N ATOM 3457 CA LEU B 13 38.152 -3.714 -23.532 1.00 16.18 C ANISOU 3457 CA LEU B 13 2128 2088 1933 100 -77 20 C ATOM 3458 C LEU B 13 37.027 -4.681 -23.259 1.00 14.94 C ANISOU 3458 C LEU B 13 2036 1861 1778 184 -106 -91 C ATOM 3459 O LEU B 13 37.262 -5.843 -22.937 1.00 14.84 O ANISOU 3459 O LEU B 13 1998 1818 1824 204 6 -129 O ATOM 3460 CB LEU B 13 38.568 -3.037 -22.208 1.00 18.11 C ANISOU 3460 CB LEU B 13 2544 2257 2081 113 -86 -156 C ATOM 3461 CG LEU B 13 39.362 -3.850 -21.192 1.00 19.58 C ANISOU 3461 CG LEU B 13 2622 2554 2265 175 -168 -159 C ATOM 3462 CD1 LEU B 13 40.605 -4.477 -21.817 1.00 20.28 C ANISOU 3462 CD1 LEU B 13 2673 2536 2496 233 -126 -210 C ATOM 3463 CD2 LEU B 13 39.784 -2.916 -20.041 1.00 19.55 C ANISOU 3463 CD2 LEU B 13 2707 2552 2171 152 -213 -150 C ATOM 3464 N TRP B 14 35.755 -4.211 -23.249 1.00 13.68 N ANISOU 3464 N TRP B 14 1904 1721 1572 182 -82 -109 N ATOM 3465 CA TRP B 14 34.629 -4.959 -22.745 1.00 15.27 C ANISOU 3465 CA TRP B 14 2015 1964 1823 142 14 -194 C ATOM 3466 C TRP B 14 33.726 -5.503 -23.847 1.00 16.80 C ANISOU 3466 C TRP B 14 2181 2293 1909 93 -60 -186 C ATOM 3467 O TRP B 14 32.577 -5.879 -23.589 1.00 19.60 O ANISOU 3467 O TRP B 14 2356 2870 2222 -140 -7 -338 O ATOM 3468 CB TRP B 14 33.834 -4.064 -21.733 1.00 14.16 C ANISOU 3468 CB TRP B 14 1898 1956 1525 124 -26 -153 C ATOM 3469 CG TRP B 14 34.690 -3.720 -20.524 1.00 13.70 C ANISOU 3469 CG TRP B 14 1804 1792 1611 64 6 -131 C ATOM 3470 CD1 TRP B 14 35.202 -2.513 -20.182 1.00 13.64 C ANISOU 3470 CD1 TRP B 14 1834 1825 1522 117 28 -164 C ATOM 3471 CD2 TRP B 14 35.167 -4.632 -19.531 1.00 13.36 C ANISOU 3471 CD2 TRP B 14 1707 1794 1576 73 83 -118 C ATOM 3472 NE1 TRP B 14 35.955 -2.586 -19.024 1.00 12.81 N ANISOU 3472 NE1 TRP B 14 1671 1665 1533 199 30 -97 N ATOM 3473 CE2 TRP B 14 35.915 -3.899 -18.595 1.00 13.25 C ANISOU 3473 CE2 TRP B 14 1731 1721 1583 5 52 -50 C ATOM 3474 CE3 TRP B 14 35.017 -6.006 -19.319 1.00 13.32 C ANISOU 3474 CE3 TRP B 14 1592 1771 1697 111 82 -54 C ATOM 3475 CZ2 TRP B 14 36.562 -4.484 -17.507 1.00 13.02 C ANISOU 3475 CZ2 TRP B 14 1618 1606 1724 146 36 -54 C ATOM 3476 CZ3 TRP B 14 35.610 -6.604 -18.219 1.00 13.08 C ANISOU 3476 CZ3 TRP B 14 1602 1837 1532 57 114 -123 C ATOM 3477 CH2 TRP B 14 36.372 -5.843 -17.316 1.00 12.70 C ANISOU 3477 CH2 TRP B 14 1361 1713 1751 -5 120 -63 C ATOM 3478 N THR B 15 34.196 -5.707 -25.068 1.00 15.56 N ANISOU 3478 N THR B 15 1971 2038 1903 250 -27 -123 N ATOM 3479 CA THR B 15 33.404 -6.321 -26.134 1.00 16.51 C ANISOU 3479 CA THR B 15 2070 2152 2052 124 -97 -68 C ATOM 3480 C THR B 15 33.480 -7.840 -26.082 1.00 17.52 C ANISOU 3480 C THR B 15 2231 2187 2238 107 -116 -83 C ATOM 3481 O THR B 15 34.355 -8.423 -25.412 1.00 16.93 O ANISOU 3481 O THR B 15 2283 2091 2061 136 -213 -151 O ATOM 3482 CB THR B 15 33.961 -5.874 -27.499 1.00 16.99 C ANISOU 3482 CB THR B 15 2108 2277 2069 105 -68 -68 C ATOM 3483 OG1 THR B 15 35.323 -6.339 -27.654 1.00 15.92 O ANISOU 3483 OG1 THR B 15 2120 2282 1649 215 -158 -78 O ATOM 3484 CG2 THR B 15 33.940 -4.364 -27.658 1.00 18.37 C ANISOU 3484 CG2 THR B 15 2442 2315 2223 165 -178 -39 C ATOM 3485 N GLU B 16 32.595 -8.525 -26.801 1.00 18.23 N ANISOU 3485 N GLU B 16 2276 2335 2317 59 -144 -110 N ATOM 3486 CA GLU B 16 32.698 -10.009 -26.790 1.00 19.95 C ANISOU 3486 CA GLU B 16 2639 2408 2533 70 -48 -105 C ATOM 3487 C GLU B 16 33.971 -10.413 -27.494 1.00 18.46 C ANISOU 3487 C GLU B 16 2488 2280 2247 10 -179 -85 C ATOM 3488 O GLU B 16 34.647 -11.359 -27.066 1.00 17.42 O ANISOU 3488 O GLU B 16 2496 2219 1903 26 -152 -212 O ATOM 3489 CB GLU B 16 31.461 -10.582 -27.484 1.00 23.55 C ANISOU 3489 CB GLU B 16 2953 2897 3097 -55 -342 -83 C ATOM 3490 CG GLU B 16 30.212 -10.371 -26.664 1.00 29.58 C ANISOU 3490 CG GLU B 16 3492 3939 3809 67 40 -192 C ATOM 3491 CD GLU B 16 29.901 -11.525 -25.755 1.00 34.96 C ANISOU 3491 CD GLU B 16 4473 4341 4471 -21 22 128 C ATOM 3492 OE1 GLU B 16 30.767 -12.245 -25.232 1.00 36.15 O ANISOU 3492 OE1 GLU B 16 4364 4675 4695 26 -103 55 O ATOM 3493 OE2 GLU B 16 28.666 -11.778 -25.578 1.00 39.15 O ANISOU 3493 OE2 GLU B 16 4636 5044 5194 -70 68 28 O ATOM 3494 N GLU B 17 34.370 -9.709 -28.577 1.00 18.02 N ANISOU 3494 N GLU B 17 2365 2270 2211 22 -141 -124 N ATOM 3495 CA GLU B 17 35.614 -10.080 -29.251 1.00 19.46 C ANISOU 3495 CA GLU B 17 2386 2539 2469 75 -142 -199 C ATOM 3496 C GLU B 17 36.788 -9.966 -28.284 1.00 17.64 C ANISOU 3496 C GLU B 17 2408 2180 2114 167 -85 -178 C ATOM 3497 O GLU B 17 37.688 -10.836 -28.297 1.00 16.45 O ANISOU 3497 O GLU B 17 2362 2144 1745 191 -174 -173 O ATOM 3498 CB GLU B 17 35.863 -9.198 -30.470 1.00 23.05 C ANISOU 3498 CB GLU B 17 3113 2893 2751 80 -44 27 C ATOM 3499 CG GLU B 17 37.215 -9.287 -31.124 1.00 27.90 C ANISOU 3499 CG GLU B 17 3340 3740 3522 85 115 3 C ATOM 3500 CD GLU B 17 37.420 -8.350 -32.323 1.00 30.85 C ANISOU 3500 CD GLU B 17 4022 3901 3797 -18 52 147 C ATOM 3501 N ALA B 18 36.809 -8.890 -27.495 1.00 15.20 N ANISOU 3501 N ALA B 18 1930 1972 1875 135 -52 -51 N ATOM 3502 CA ALA B 18 37.921 -8.714 -26.550 1.00 14.75 C ANISOU 3502 CA ALA B 18 2126 1766 1711 121 -123 -83 C ATOM 3503 C ALA B 18 37.967 -9.833 -25.522 1.00 13.59 C ANISOU 3503 C ALA B 18 1828 1659 1678 70 -30 -102 C ATOM 3504 O ALA B 18 39.082 -10.279 -25.129 1.00 13.80 O ANISOU 3504 O ALA B 18 1885 1794 1564 101 -105 -67 O ATOM 3505 CB ALA B 18 37.785 -7.349 -25.841 1.00 14.25 C ANISOU 3505 CB ALA B 18 1977 1586 1852 119 -60 -2 C ATOM 3506 N LYS B 19 36.824 -10.244 -24.991 1.00 12.86 N ANISOU 3506 N LYS B 19 1721 1654 1513 124 -143 -88 N ATOM 3507 CA LYS B 19 36.783 -11.336 -24.035 1.00 13.57 C ANISOU 3507 CA LYS B 19 1883 1548 1723 113 -73 -79 C ATOM 3508 C LYS B 19 37.342 -12.637 -24.622 1.00 13.23 C ANISOU 3508 C LYS B 19 1790 1614 1623 151 -160 -112 C ATOM 3509 O LYS B 19 38.202 -13.276 -23.988 1.00 12.59 O ANISOU 3509 O LYS B 19 1818 1481 1486 248 -154 -156 O ATOM 3510 CB LYS B 19 35.354 -11.605 -23.592 1.00 15.57 C ANISOU 3510 CB LYS B 19 1940 1974 2003 114 15 -93 C ATOM 3511 CG LYS B 19 35.226 -12.686 -22.545 1.00 18.48 C ANISOU 3511 CG LYS B 19 2617 2165 2238 112 -53 87 C ATOM 3512 CD LYS B 19 33.805 -13.010 -22.175 1.00 22.69 C ANISOU 3512 CD LYS B 19 2859 2799 2963 -6 137 137 C ATOM 3513 CE LYS B 19 32.902 -13.128 -23.345 1.00 26.41 C ANISOU 3513 CE LYS B 19 3458 3379 3197 -39 -115 137 C ATOM 3514 NZ LYS B 19 32.051 -14.278 -23.632 1.00 29.21 N ANISOU 3514 NZ LYS B 19 3979 3433 3686 -183 -55 110 N ATOM 3515 N TYR B 20 36.885 -13.007 -25.815 1.00 13.30 N ANISOU 3515 N TYR B 20 1995 1589 1467 189 -52 -84 N ATOM 3516 CA TYR B 20 37.455 -14.224 -26.413 1.00 14.10 C ANISOU 3516 CA TYR B 20 1983 1736 1639 147 -22 -204 C ATOM 3517 C TYR B 20 38.933 -14.055 -26.730 1.00 14.17 C ANISOU 3517 C TYR B 20 1959 1746 1680 91 -154 -122 C ATOM 3518 O TYR B 20 39.658 -15.067 -26.602 1.00 14.82 O ANISOU 3518 O TYR B 20 2019 1862 1751 247 -27 -98 O ATOM 3519 CB TYR B 20 36.681 -14.587 -27.704 1.00 15.86 C ANISOU 3519 CB TYR B 20 2204 2014 1810 100 -234 -181 C ATOM 3520 CG TYR B 20 35.279 -15.070 -27.429 1.00 18.01 C ANISOU 3520 CG TYR B 20 2380 2334 2130 1 -68 -206 C ATOM 3521 CD1 TYR B 20 34.165 -14.364 -27.889 1.00 20.14 C ANISOU 3521 CD1 TYR B 20 2568 2557 2528 135 -116 -99 C ATOM 3522 CD2 TYR B 20 35.038 -16.229 -26.713 1.00 19.54 C ANISOU 3522 CD2 TYR B 20 2601 2573 2251 40 -105 -14 C ATOM 3523 CE1 TYR B 20 32.865 -14.799 -27.638 1.00 22.19 C ANISOU 3523 CE1 TYR B 20 2771 2788 2871 -34 -11 -48 C ATOM 3524 CE2 TYR B 20 33.765 -16.686 -26.432 1.00 21.63 C ANISOU 3524 CE2 TYR B 20 2696 2929 2593 -52 -40 -98 C ATOM 3525 CZ TYR B 20 32.692 -15.958 -26.922 1.00 23.28 C ANISOU 3525 CZ TYR B 20 2946 2943 2959 66 -16 51 C ATOM 3526 OH TYR B 20 31.432 -16.439 -26.638 1.00 26.20 O ANISOU 3526 OH TYR B 20 3067 3393 3497 -57 -17 -23 O ATOM 3527 N ARG B 21 39.419 -12.891 -27.155 1.00 13.91 N ANISOU 3527 N ARG B 21 1941 1784 1561 105 -121 -12 N ATOM 3528 CA ARG B 21 40.847 -12.706 -27.331 1.00 15.14 C ANISOU 3528 CA ARG B 21 1955 2038 1759 107 -65 -96 C ATOM 3529 C ARG B 21 41.596 -12.938 -26.019 1.00 13.67 C ANISOU 3529 C ARG B 21 1736 1763 1695 158 56 -18 C ATOM 3530 O ARG B 21 42.691 -13.546 -26.054 1.00 13.12 O ANISOU 3530 O ARG B 21 1737 1687 1563 294 45 -57 O ATOM 3531 CB ARG B 21 41.205 -11.326 -27.910 1.00 19.24 C ANISOU 3531 CB ARG B 21 2540 2264 2507 76 92 71 C ATOM 3532 CG ARG B 21 40.736 -11.186 -29.351 1.00 23.66 C ANISOU 3532 CG ARG B 21 3012 3247 2732 150 -115 -2 C ATOM 3533 CD ARG B 21 41.317 -9.949 -30.030 1.00 28.79 C ANISOU 3533 CD ARG B 21 3677 3551 3712 -79 76 188 C ATOM 3534 NE ARG B 21 41.196 -8.779 -29.208 1.00 33.10 N ANISOU 3534 NE ARG B 21 4378 4003 4193 -39 62 -85 N ATOM 3535 CZ ARG B 21 40.522 -7.677 -28.953 1.00 34.45 C ANISOU 3535 CZ ARG B 21 4387 4247 4455 68 74 -20 C ATOM 3536 NH1 ARG B 21 40.997 -6.963 -27.905 1.00 35.07 N ANISOU 3536 NH1 ARG B 21 4585 4331 4410 -32 143 -86 N ATOM 3537 NH2 ARG B 21 39.476 -7.236 -29.660 1.00 34.90 N ANISOU 3537 NH2 ARG B 21 4375 4476 4409 -10 25 166 N ATOM 3538 N ARG B 22 41.084 -12.460 -24.898 1.00 11.79 N ANISOU 3538 N ARG B 22 1606 1426 1446 196 -71 -3 N ATOM 3539 CA ARG B 22 41.727 -12.735 -23.608 1.00 11.67 C ANISOU 3539 CA ARG B 22 1668 1365 1402 143 -6 -46 C ATOM 3540 C ARG B 22 41.663 -14.234 -23.281 1.00 11.30 C ANISOU 3540 C ARG B 22 1548 1315 1429 92 -21 -64 C ATOM 3541 O ARG B 22 42.659 -14.758 -22.774 1.00 11.28 O ANISOU 3541 O ARG B 22 1588 1371 1328 246 -31 -72 O ATOM 3542 CB ARG B 22 41.084 -11.970 -22.433 1.00 10.38 C ANISOU 3542 CB ARG B 22 1307 1270 1367 110 -57 -127 C ATOM 3543 CG ARG B 22 41.392 -10.450 -22.484 1.00 11.17 C ANISOU 3543 CG ARG B 22 1594 1301 1349 99 86 -140 C ATOM 3544 CD ARG B 22 40.821 -9.787 -21.227 1.00 11.07 C ANISOU 3544 CD ARG B 22 1462 1447 1299 52 141 -104 C ATOM 3545 NE ARG B 22 39.364 -9.787 -21.129 1.00 11.57 N ANISOU 3545 NE ARG B 22 1463 1480 1452 101 -83 -81 N ATOM 3546 CZ ARG B 22 38.591 -8.840 -21.672 1.00 12.15 C ANISOU 3546 CZ ARG B 22 1533 1573 1510 81 -56 -107 C ATOM 3547 NH1 ARG B 22 39.202 -7.874 -22.353 1.00 13.25 N ANISOU 3547 NH1 ARG B 22 1922 1714 1399 244 63 96 N ATOM 3548 NH2 ARG B 22 37.274 -8.867 -21.499 1.00 12.42 N ANISOU 3548 NH2 ARG B 22 1535 1834 1351 245 -71 -315 N ATOM 3549 N TRP B 23 40.551 -14.936 -23.553 1.00 10.68 N ANISOU 3549 N TRP B 23 1446 1292 1319 115 140 -35 N ATOM 3550 CA TRP B 23 40.532 -16.366 -23.214 1.00 10.42 C ANISOU 3550 CA TRP B 23 1422 1276 1260 32 161 -63 C ATOM 3551 C TRP B 23 41.572 -17.117 -24.038 1.00 11.33 C ANISOU 3551 C TRP B 23 1468 1441 1395 191 102 -20 C ATOM 3552 O TRP B 23 42.291 -17.966 -23.514 1.00 10.67 O ANISOU 3552 O TRP B 23 1600 1351 1103 122 -49 -66 O ATOM 3553 CB TRP B 23 39.157 -16.990 -23.570 1.00 10.67 C ANISOU 3553 CB TRP B 23 1352 1242 1462 74 45 -56 C ATOM 3554 CG TRP B 23 38.038 -16.509 -22.670 1.00 11.23 C ANISOU 3554 CG TRP B 23 1409 1480 1378 -6 70 -81 C ATOM 3555 CD1 TRP B 23 38.157 -15.648 -21.602 1.00 11.17 C ANISOU 3555 CD1 TRP B 23 1501 1318 1426 221 107 -23 C ATOM 3556 CD2 TRP B 23 36.679 -16.910 -22.710 1.00 12.40 C ANISOU 3556 CD2 TRP B 23 1441 1623 1646 68 2 -35 C ATOM 3557 NE1 TRP B 23 36.935 -15.462 -21.004 1.00 11.64 N ANISOU 3557 NE1 TRP B 23 1386 1569 1469 42 42 64 N ATOM 3558 CE2 TRP B 23 36.011 -16.250 -21.661 1.00 12.64 C ANISOU 3558 CE2 TRP B 23 1595 1547 1659 10 0 -55 C ATOM 3559 CE3 TRP B 23 35.964 -17.785 -23.551 1.00 13.69 C ANISOU 3559 CE3 TRP B 23 1591 1817 1792 50 -74 -125 C ATOM 3560 CZ2 TRP B 23 34.642 -16.366 -21.423 1.00 13.98 C ANISOU 3560 CZ2 TRP B 23 1633 1816 1864 -11 43 -56 C ATOM 3561 CZ3 TRP B 23 34.599 -17.949 -23.274 1.00 14.80 C ANISOU 3561 CZ3 TRP B 23 1755 1997 1873 -87 7 -125 C ATOM 3562 CH2 TRP B 23 33.964 -17.250 -22.243 1.00 15.00 C ANISOU 3562 CH2 TRP B 23 1767 2018 1916 21 -32 -170 C ATOM 3563 N LEU B 24 41.676 -16.739 -25.343 1.00 12.38 N ANISOU 3563 N LEU B 24 1799 1617 1286 109 131 -168 N ATOM 3564 CA LEU B 24 42.771 -17.375 -26.137 1.00 13.71 C ANISOU 3564 CA LEU B 24 1635 1884 1690 204 134 -53 C ATOM 3565 C LEU B 24 44.166 -17.005 -25.673 1.00 13.81 C ANISOU 3565 C LEU B 24 1793 1775 1678 142 26 -67 C ATOM 3566 O LEU B 24 45.048 -17.910 -25.697 1.00 12.86 O ANISOU 3566 O LEU B 24 1657 1676 1552 181 -7 -79 O ATOM 3567 CB LEU B 24 42.620 -16.895 -27.576 1.00 15.78 C ANISOU 3567 CB LEU B 24 2219 2070 1707 121 80 -31 C ATOM 3568 CG LEU B 24 42.995 -17.760 -28.718 1.00 18.14 C ANISOU 3568 CG LEU B 24 2506 2312 2075 224 93 -83 C ATOM 3569 CD1 LEU B 24 43.550 -17.102 -29.935 1.00 17.87 C ANISOU 3569 CD1 LEU B 24 2246 2329 2216 244 225 -43 C ATOM 3570 CD2 LEU B 24 43.780 -18.996 -28.623 1.00 17.75 C ANISOU 3570 CD2 LEU B 24 2346 2435 1963 334 -13 -84 C ATOM 3571 N GLU B 25 44.399 -15.787 -25.246 1.00 13.68 N ANISOU 3571 N GLU B 25 1830 1673 1693 161 62 -27 N ATOM 3572 CA GLU B 25 45.675 -15.397 -24.630 1.00 15.30 C ANISOU 3572 CA GLU B 25 2016 1997 1799 49 -79 31 C ATOM 3573 C GLU B 25 46.066 -16.279 -23.429 1.00 13.21 C ANISOU 3573 C GLU B 25 1685 1690 1644 42 24 -73 C ATOM 3574 O GLU B 25 47.240 -16.707 -23.299 1.00 12.25 O ANISOU 3574 O GLU B 25 1663 1615 1376 48 -60 -216 O ATOM 3575 CB GLU B 25 45.594 -13.994 -24.043 1.00 18.81 C ANISOU 3575 CB GLU B 25 2544 2148 2455 213 2 -164 C ATOM 3576 CG GLU B 25 46.312 -12.887 -24.724 1.00 24.33 C ANISOU 3576 CG GLU B 25 3189 2833 3221 -67 241 53 C ATOM 3577 CD GLU B 25 46.409 -11.643 -23.814 1.00 27.25 C ANISOU 3577 CD GLU B 25 3551 3171 3631 21 106 -207 C ATOM 3578 OE1 GLU B 25 45.349 -11.017 -23.675 1.00 27.36 O ANISOU 3578 OE1 GLU B 25 3566 3112 3717 130 78 -134 O ATOM 3579 OE2 GLU B 25 47.505 -11.357 -23.253 1.00 28.70 O ANISOU 3579 OE2 GLU B 25 3722 3398 3784 -89 -2 -133 O ATOM 3580 N VAL B 26 45.083 -16.526 -22.568 1.00 10.91 N ANISOU 3580 N VAL B 26 1518 1305 1323 92 -68 -130 N ATOM 3581 CA VAL B 26 45.332 -17.375 -21.411 1.00 10.94 C ANISOU 3581 CA VAL B 26 1547 1255 1355 74 71 -49 C ATOM 3582 C VAL B 26 45.661 -18.804 -21.845 1.00 10.99 C ANISOU 3582 C VAL B 26 1385 1344 1445 179 -21 -108 C ATOM 3583 O VAL B 26 46.643 -19.413 -21.366 1.00 10.74 O ANISOU 3583 O VAL B 26 1416 1406 1258 242 -93 -62 O ATOM 3584 CB VAL B 26 44.109 -17.439 -20.455 1.00 10.65 C ANISOU 3584 CB VAL B 26 1528 1217 1303 102 80 -59 C ATOM 3585 CG1 VAL B 26 44.401 -18.389 -19.297 1.00 11.52 C ANISOU 3585 CG1 VAL B 26 1587 1420 1372 164 59 51 C ATOM 3586 CG2 VAL B 26 43.847 -16.032 -19.898 1.00 11.26 C ANISOU 3586 CG2 VAL B 26 1697 1297 1282 230 91 -108 C ATOM 3587 N GLU B 27 44.848 -19.373 -22.722 1.00 10.49 N ANISOU 3587 N GLU B 27 1380 1286 1320 93 22 -78 N ATOM 3588 CA GLU B 27 45.110 -20.745 -23.186 1.00 11.91 C ANISOU 3588 CA GLU B 27 1565 1379 1581 125 15 -166 C ATOM 3589 C GLU B 27 46.466 -20.858 -23.862 1.00 12.08 C ANISOU 3589 C GLU B 27 1485 1434 1670 48 -75 -41 C ATOM 3590 O GLU B 27 47.160 -21.878 -23.687 1.00 12.56 O ANISOU 3590 O GLU B 27 1784 1384 1605 171 -115 -67 O ATOM 3591 CB GLU B 27 44.048 -21.152 -24.228 1.00 12.73 C ANISOU 3591 CB GLU B 27 1539 1565 1733 146 -71 -128 C ATOM 3592 CG GLU B 27 42.630 -21.218 -23.656 1.00 14.53 C ANISOU 3592 CG GLU B 27 1677 1884 1959 103 87 -101 C ATOM 3593 CD GLU B 27 42.261 -22.403 -22.838 1.00 17.06 C ANISOU 3593 CD GLU B 27 2051 2177 2253 43 89 37 C ATOM 3594 OE1 GLU B 27 43.139 -23.194 -22.439 1.00 18.83 O ANISOU 3594 OE1 GLU B 27 2193 2481 2480 121 10 165 O ATOM 3595 OE2 GLU B 27 41.047 -22.657 -22.595 1.00 17.60 O ANISOU 3595 OE2 GLU B 27 2094 2255 2337 8 236 -44 O ATOM 3596 N LEU B 28 46.884 -19.928 -24.708 1.00 11.17 N ANISOU 3596 N LEU B 28 1469 1483 1294 90 -62 -99 N ATOM 3597 CA LEU B 28 48.208 -20.001 -25.294 1.00 12.66 C ANISOU 3597 CA LEU B 28 1639 1652 1518 90 18 -93 C ATOM 3598 C LEU B 28 49.341 -19.773 -24.319 1.00 12.53 C ANISOU 3598 C LEU B 28 1659 1647 1454 191 -4 -98 C ATOM 3599 O LEU B 28 50.435 -20.308 -24.538 1.00 13.16 O ANISOU 3599 O LEU B 28 1706 1824 1471 370 60 35 O ATOM 3600 CB LEU B 28 48.327 -18.953 -26.418 1.00 13.24 C ANISOU 3600 CB LEU B 28 1959 1597 1473 92 119 -82 C ATOM 3601 CG LEU B 28 47.537 -19.328 -27.684 1.00 15.24 C ANISOU 3601 CG LEU B 28 2064 1979 1746 82 -28 -65 C ATOM 3602 CD1 LEU B 28 47.575 -18.168 -28.658 1.00 16.02 C ANISOU 3602 CD1 LEU B 28 2213 2080 1795 147 8 24 C ATOM 3603 CD2 LEU B 28 48.187 -20.558 -28.319 1.00 17.21 C ANISOU 3603 CD2 LEU B 28 2577 2024 1939 122 -2 -132 C ATOM 3604 N ALA B 29 49.143 -18.984 -23.256 1.00 11.61 N ANISOU 3604 N ALA B 29 1552 1471 1387 171 12 -72 N ATOM 3605 CA ALA B 29 50.173 -18.952 -22.217 1.00 11.52 C ANISOU 3605 CA ALA B 29 1669 1316 1391 96 -32 -178 C ATOM 3606 C ALA B 29 50.292 -20.320 -21.545 1.00 11.20 C ANISOU 3606 C ALA B 29 1536 1331 1387 97 24 -119 C ATOM 3607 O ALA B 29 51.429 -20.696 -21.201 1.00 11.37 O ANISOU 3607 O ALA B 29 1578 1342 1399 119 -61 -160 O ATOM 3608 CB ALA B 29 49.871 -17.827 -21.209 1.00 11.09 C ANISOU 3608 CB ALA B 29 1621 1249 1345 183 -28 -166 C ATOM 3609 N VAL B 30 49.176 -21.038 -21.330 1.00 10.06 N ANISOU 3609 N VAL B 30 1587 999 1236 106 7 -243 N ATOM 3610 CA VAL B 30 49.275 -22.343 -20.652 1.00 10.62 C ANISOU 3610 CA VAL B 30 1577 1186 1272 86 98 -90 C ATOM 3611 C VAL B 30 49.948 -23.360 -21.593 1.00 11.14 C ANISOU 3611 C VAL B 30 1487 1379 1365 211 75 -88 C ATOM 3612 O VAL B 30 50.814 -24.117 -21.115 1.00 10.57 O ANISOU 3612 O VAL B 30 1421 1350 1247 241 84 -123 O ATOM 3613 CB VAL B 30 47.864 -22.839 -20.281 1.00 10.95 C ANISOU 3613 CB VAL B 30 1509 1261 1390 120 116 -82 C ATOM 3614 CG1 VAL B 30 47.835 -24.287 -19.766 1.00 11.13 C ANISOU 3614 CG1 VAL B 30 1487 1265 1476 120 127 -86 C ATOM 3615 CG2 VAL B 30 47.325 -21.869 -19.204 1.00 10.42 C ANISOU 3615 CG2 VAL B 30 1263 1443 1252 90 92 -87 C ATOM 3616 N THR B 31 49.579 -23.393 -22.870 1.00 11.41 N ANISOU 3616 N THR B 31 1497 1493 1347 62 64 -56 N ATOM 3617 CA THR B 31 50.276 -24.382 -23.739 1.00 13.21 C ANISOU 3617 CA THR B 31 1776 1667 1575 132 18 -147 C ATOM 3618 C THR B 31 51.744 -24.015 -23.819 1.00 13.33 C ANISOU 3618 C THR B 31 1778 1685 1603 181 90 -8 C ATOM 3619 O THR B 31 52.625 -24.902 -23.806 1.00 13.16 O ANISOU 3619 O THR B 31 1838 1687 1474 312 -87 -72 O ATOM 3620 CB THR B 31 49.665 -24.503 -25.161 1.00 14.97 C ANISOU 3620 CB THR B 31 1917 2002 1771 -2 -126 15 C ATOM 3621 OG1 THR B 31 49.850 -23.250 -25.790 1.00 17.60 O ANISOU 3621 OG1 THR B 31 2503 2243 1941 123 41 86 O ATOM 3622 CG2 THR B 31 48.169 -24.773 -25.096 1.00 13.93 C ANISOU 3622 CG2 THR B 31 1767 1958 1569 100 -84 31 C ATOM 3623 N ARG B 32 52.098 -22.731 -23.979 1.00 12.68 N ANISOU 3623 N ARG B 32 1764 1607 1447 137 51 -168 N ATOM 3624 CA ARG B 32 53.504 -22.333 -23.974 1.00 13.12 C ANISOU 3624 CA ARG B 32 1765 1740 1479 111 74 -28 C ATOM 3625 C ARG B 32 54.237 -22.799 -22.717 1.00 13.08 C ANISOU 3625 C ARG B 32 1686 1749 1535 172 87 -8 C ATOM 3626 O ARG B 32 55.365 -23.333 -22.861 1.00 13.79 O ANISOU 3626 O ARG B 32 1697 1892 1650 296 243 131 O ATOM 3627 CB ARG B 32 53.653 -20.826 -24.138 1.00 13.64 C ANISOU 3627 CB ARG B 32 1898 1716 1569 97 94 -4 C ATOM 3628 CG ARG B 32 55.078 -20.325 -24.121 1.00 16.32 C ANISOU 3628 CG ARG B 32 1978 2169 2054 6 53 -11 C ATOM 3629 CD ARG B 32 55.170 -18.812 -24.375 1.00 19.87 C ANISOU 3629 CD ARG B 32 2657 2274 2616 -13 38 65 C ATOM 3630 NE ARG B 32 56.568 -18.439 -24.138 1.00 23.68 N ANISOU 3630 NE ARG B 32 2813 3056 3129 -74 -57 125 N ATOM 3631 CZ ARG B 32 57.048 -17.212 -23.972 1.00 26.49 C ANISOU 3631 CZ ARG B 32 3339 3128 3597 -92 -20 30 C ATOM 3632 NH1 ARG B 32 56.242 -16.172 -24.036 1.00 26.48 N ANISOU 3632 NH1 ARG B 32 3466 3111 3485 -19 12 65 N ATOM 3633 NH2 ARG B 32 58.377 -17.062 -23.739 1.00 29.01 N ANISOU 3633 NH2 ARG B 32 3457 3701 3862 -107 -91 89 N ATOM 3634 N ALA B 33 53.645 -22.648 -21.537 1.00 12.21 N ANISOU 3634 N ALA B 33 1666 1510 1462 148 56 -49 N ATOM 3635 CA ALA B 33 54.285 -23.115 -20.307 1.00 12.07 C ANISOU 3635 CA ALA B 33 1705 1561 1321 61 150 -21 C ATOM 3636 C ALA B 33 54.438 -24.629 -20.265 1.00 11.75 C ANISOU 3636 C ALA B 33 1616 1575 1276 102 146 -91 C ATOM 3637 O ALA B 33 55.535 -25.120 -19.886 1.00 12.46 O ANISOU 3637 O ALA B 33 1704 1608 1424 149 13 -110 O ATOM 3638 CB ALA B 33 53.483 -22.639 -19.100 1.00 11.95 C ANISOU 3638 CB ALA B 33 1668 1546 1328 72 93 -168 C ATOM 3639 N TYR B 34 53.370 -25.384 -20.590 1.00 11.68 N ANISOU 3639 N TYR B 34 1608 1596 1235 51 253 -77 N ATOM 3640 CA TYR B 34 53.563 -26.847 -20.671 1.00 12.93 C ANISOU 3640 CA TYR B 34 1673 1635 1605 79 209 14 C ATOM 3641 C TYR B 34 54.715 -27.222 -21.610 1.00 14.24 C ANISOU 3641 C TYR B 34 1765 1908 1737 206 216 99 C ATOM 3642 O TYR B 34 55.517 -28.119 -21.283 1.00 15.24 O ANISOU 3642 O TYR B 34 1929 1974 1885 332 224 126 O ATOM 3643 CB TYR B 34 52.304 -27.503 -21.218 1.00 12.34 C ANISOU 3643 CB TYR B 34 1587 1580 1521 102 179 36 C ATOM 3644 CG TYR B 34 51.187 -27.888 -20.278 1.00 12.92 C ANISOU 3644 CG TYR B 34 1560 1659 1688 102 167 50 C ATOM 3645 CD1 TYR B 34 49.912 -27.307 -20.333 1.00 12.37 C ANISOU 3645 CD1 TYR B 34 1514 1545 1640 48 66 -10 C ATOM 3646 CD2 TYR B 34 51.404 -28.879 -19.326 1.00 13.50 C ANISOU 3646 CD2 TYR B 34 1722 1759 1648 130 205 74 C ATOM 3647 CE1 TYR B 34 48.935 -27.732 -19.458 1.00 12.59 C ANISOU 3647 CE1 TYR B 34 1527 1572 1683 131 111 -17 C ATOM 3648 CE2 TYR B 34 50.424 -29.305 -18.469 1.00 13.40 C ANISOU 3648 CE2 TYR B 34 1572 1762 1758 35 145 45 C ATOM 3649 CZ TYR B 34 49.158 -28.723 -18.538 1.00 12.95 C ANISOU 3649 CZ TYR B 34 1643 1643 1634 151 161 41 C ATOM 3650 OH TYR B 34 48.156 -29.192 -17.699 1.00 12.90 O ANISOU 3650 OH TYR B 34 1555 1454 1893 170 162 -29 O ATOM 3651 N GLU B 35 54.792 -26.620 -22.777 1.00 14.87 N ANISOU 3651 N GLU B 35 1912 2067 1670 183 80 128 N ATOM 3652 CA GLU B 35 55.826 -26.899 -23.772 1.00 15.95 C ANISOU 3652 CA GLU B 35 1980 2231 1849 182 150 58 C ATOM 3653 C GLU B 35 57.186 -26.503 -23.261 1.00 15.98 C ANISOU 3653 C GLU B 35 2019 2129 1925 222 58 97 C ATOM 3654 O GLU B 35 58.158 -27.292 -23.379 1.00 16.90 O ANISOU 3654 O GLU B 35 2171 2289 1961 388 160 12 O ATOM 3655 CB GLU B 35 55.498 -26.121 -25.085 1.00 17.92 C ANISOU 3655 CB GLU B 35 2401 2401 2007 210 60 166 C ATOM 3656 CG GLU B 35 56.340 -26.610 -26.278 1.00 19.59 C ANISOU 3656 CG GLU B 35 2598 2642 2202 192 129 33 C ATOM 3657 CD GLU B 35 55.850 -25.955 -27.578 1.00 21.32 C ANISOU 3657 CD GLU B 35 2785 2957 2360 99 -48 78 C ATOM 3658 OE1 GLU B 35 54.622 -25.692 -27.666 1.00 21.01 O ANISOU 3658 OE1 GLU B 35 2826 2871 2286 195 -93 100 O ATOM 3659 OE2 GLU B 35 56.669 -25.768 -28.486 1.00 22.36 O ANISOU 3659 OE2 GLU B 35 2743 3130 2623 -33 -17 158 O ATOM 3660 N GLU B 36 57.339 -25.344 -22.626 1.00 15.37 N ANISOU 3660 N GLU B 36 2010 1971 1860 313 94 112 N ATOM 3661 CA GLU B 36 58.631 -24.906 -22.109 1.00 19.52 C ANISOU 3661 CA GLU B 36 2268 2654 2495 63 -43 143 C ATOM 3662 C GLU B 36 59.141 -25.826 -20.999 1.00 18.76 C ANISOU 3662 C GLU B 36 2307 2330 2492 64 46 62 C ATOM 3663 O GLU B 36 60.358 -26.034 -20.847 1.00 19.69 O ANISOU 3663 O GLU B 36 2338 2514 2631 183 72 124 O ATOM 3664 CB GLU B 36 58.599 -23.429 -21.656 1.00 24.11 C ANISOU 3664 CB GLU B 36 3056 2909 3198 39 29 -131 C ATOM 3665 CG GLU B 36 58.287 -22.603 -22.930 1.00 30.10 C ANISOU 3665 CG GLU B 36 3956 3779 3702 75 -79 202 C ATOM 3666 CD GLU B 36 58.745 -21.172 -23.014 1.00 33.40 C ANISOU 3666 CD GLU B 36 4345 3985 4359 -45 -11 123 C ATOM 3667 OE1 GLU B 36 58.721 -20.523 -24.111 1.00 32.84 O ANISOU 3667 OE1 GLU B 36 4099 4152 4229 29 0 118 O ATOM 3668 OE2 GLU B 36 59.162 -20.676 -21.922 1.00 36.83 O ANISOU 3668 OE2 GLU B 36 4863 4626 4506 32 -128 -28 O ATOM 3669 N LEU B 37 58.241 -26.456 -20.283 1.00 17.09 N ANISOU 3669 N LEU B 37 2157 2129 2206 258 139 -43 N ATOM 3670 CA LEU B 37 58.602 -27.426 -19.252 1.00 18.99 C ANISOU 3670 CA LEU B 37 2453 2385 2377 186 20 53 C ATOM 3671 C LEU B 37 58.832 -28.839 -19.784 1.00 18.52 C ANISOU 3671 C LEU B 37 2384 2329 2323 180 54 66 C ATOM 3672 O LEU B 37 59.080 -29.720 -18.928 1.00 17.83 O ANISOU 3672 O LEU B 37 2203 2352 2219 340 19 29 O ATOM 3673 CB LEU B 37 57.455 -27.472 -18.243 1.00 20.31 C ANISOU 3673 CB LEU B 37 2507 2713 2497 130 89 142 C ATOM 3674 CG LEU B 37 57.492 -26.714 -16.943 1.00 23.73 C ANISOU 3674 CG LEU B 37 2979 3163 2876 19 97 -140 C ATOM 3675 CD1 LEU B 37 58.769 -26.073 -16.444 1.00 23.57 C ANISOU 3675 CD1 LEU B 37 3025 3043 2887 31 74 -189 C ATOM 3676 CD2 LEU B 37 56.291 -25.788 -16.761 1.00 24.52 C ANISOU 3676 CD2 LEU B 37 3211 3059 3046 200 -157 36 C ATOM 3677 N GLY B 38 58.629 -29.073 -21.079 1.00 18.69 N ANISOU 3677 N GLY B 38 2350 2401 2352 195 -71 33 N ATOM 3678 CA GLY B 38 58.822 -30.395 -21.660 1.00 18.33 C ANISOU 3678 CA GLY B 38 2276 2414 2275 183 9 5 C ATOM 3679 C GLY B 38 57.658 -31.334 -21.430 1.00 19.41 C ANISOU 3679 C GLY B 38 2428 2455 2492 150 45 63 C ATOM 3680 O GLY B 38 57.881 -32.545 -21.560 1.00 20.52 O ANISOU 3680 O GLY B 38 2580 2556 2662 421 78 -85 O ATOM 3681 N MET B 39 56.456 -30.806 -21.138 1.00 18.21 N ANISOU 3681 N MET B 39 2350 2298 2272 250 19 33 N ATOM 3682 CA MET B 39 55.330 -31.682 -20.829 1.00 19.18 C ANISOU 3682 CA MET B 39 2556 2376 2355 109 56 52 C ATOM 3683 C MET B 39 54.457 -31.989 -22.022 1.00 19.37 C ANISOU 3683 C MET B 39 2562 2419 2378 87 -10 1 C ATOM 3684 O MET B 39 53.622 -32.883 -21.816 1.00 20.53 O ANISOU 3684 O MET B 39 2912 2505 2385 -23 -73 170 O ATOM 3685 CB MET B 39 54.441 -31.039 -19.739 1.00 19.54 C ANISOU 3685 CB MET B 39 2577 2529 2320 152 35 -48 C ATOM 3686 CG MET B 39 55.316 -30.802 -18.537 1.00 18.29 C ANISOU 3686 CG MET B 39 2646 2558 1744 244 493 -305 C ATOM 3687 SD MET B 39 54.586 -30.133 -17.000 1.00 11.84 S ANISOU 3687 SD MET B 39 1686 1534 1278 685 564 -28 S ATOM 3688 CE MET B 39 55.611 -29.743 -15.919 1.00 18.82 C ANISOU 3688 CE MET B 39 2427 2409 2316 287 111 -38 C ATOM 3689 N ILE B 40 54.540 -31.147 -23.038 1.00 19.09 N ANISOU 3689 N ILE B 40 2491 2306 2456 206 -31 42 N ATOM 3690 CA ILE B 40 53.850 -31.406 -24.296 1.00 18.99 C ANISOU 3690 CA ILE B 40 2510 2194 2510 218 -121 -21 C ATOM 3691 C ILE B 40 54.907 -31.156 -25.371 1.00 20.60 C ANISOU 3691 C ILE B 40 2625 2462 2739 263 57 101 C ATOM 3692 O ILE B 40 55.894 -30.486 -25.132 1.00 20.30 O ANISOU 3692 O ILE B 40 2665 2563 2485 321 29 -80 O ATOM 3693 CB ILE B 40 52.606 -30.515 -24.544 1.00 17.60 C ANISOU 3693 CB ILE B 40 2182 2141 2364 55 18 -34 C ATOM 3694 CG1 ILE B 40 52.973 -29.035 -24.645 1.00 16.63 C ANISOU 3694 CG1 ILE B 40 2100 1991 2230 205 -63 32 C ATOM 3695 CG2 ILE B 40 51.601 -30.727 -23.402 1.00 17.90 C ANISOU 3695 CG2 ILE B 40 2276 2137 2390 89 20 26 C ATOM 3696 CD1 ILE B 40 51.741 -28.151 -24.950 1.00 15.23 C ANISOU 3696 CD1 ILE B 40 1897 1861 2027 82 -54 -50 C ATOM 3697 N PRO B 41 54.657 -31.741 -26.530 1.00 23.79 N ANISOU 3697 N PRO B 41 3210 2891 2939 214 -29 -24 N ATOM 3698 CA PRO B 41 55.630 -31.790 -27.628 1.00 25.38 C ANISOU 3698 CA PRO B 41 3336 3214 3092 140 54 -53 C ATOM 3699 C PRO B 41 55.980 -30.408 -28.151 1.00 24.63 C ANISOU 3699 C PRO B 41 3184 3213 2961 116 -2 -55 C ATOM 3700 O PRO B 41 55.093 -29.557 -28.195 1.00 23.77 O ANISOU 3700 O PRO B 41 3137 3133 2762 181 67 -56 O ATOM 3701 CB PRO B 41 54.915 -32.621 -28.697 1.00 26.55 C ANISOU 3701 CB PRO B 41 3486 3309 3292 85 -13 -150 C ATOM 3702 CG PRO B 41 53.708 -33.208 -28.072 1.00 27.39 C ANISOU 3702 CG PRO B 41 3565 3415 3426 91 85 -114 C ATOM 3703 CD PRO B 41 53.373 -32.361 -26.876 1.00 25.99 C ANISOU 3703 CD PRO B 41 3324 3305 3245 51 12 -44 C ATOM 3704 N LYS B 42 57.234 -30.185 -28.532 1.00 24.72 N ANISOU 3704 N LYS B 42 3111 3213 3068 141 -35 -142 N ATOM 3705 CA LYS B 42 57.659 -28.947 -29.170 1.00 26.04 C ANISOU 3705 CA LYS B 42 3279 3419 3197 54 -10 -24 C ATOM 3706 C LYS B 42 56.838 -28.633 -30.418 1.00 25.45 C ANISOU 3706 C LYS B 42 3272 3273 3123 63 23 -5 C ATOM 3707 O LYS B 42 56.489 -29.593 -31.126 1.00 26.92 O ANISOU 3707 O LYS B 42 3573 3485 3169 65 -26 -101 O ATOM 3708 CB LYS B 42 59.148 -28.994 -29.552 1.00 27.25 C ANISOU 3708 CB LYS B 42 3320 3544 3492 95 37 -106 C ATOM 3709 N GLY B 43 56.495 -27.401 -30.655 1.00 23.55 N ANISOU 3709 N GLY B 43 3010 3208 2730 66 85 -15 N ATOM 3710 CA GLY B 43 55.778 -27.026 -31.873 1.00 23.05 C ANISOU 3710 CA GLY B 43 2887 3139 2730 44 43 -95 C ATOM 3711 C GLY B 43 54.290 -26.840 -31.657 1.00 21.78 C ANISOU 3711 C GLY B 43 2855 2876 2546 57 117 47 C ATOM 3712 O GLY B 43 53.630 -26.202 -32.497 1.00 22.96 O ANISOU 3712 O GLY B 43 3192 3093 2441 130 84 79 O ATOM 3713 N VAL B 44 53.713 -27.402 -30.589 1.00 19.69 N ANISOU 3713 N VAL B 44 2619 2510 2354 124 -7 -3 N ATOM 3714 CA VAL B 44 52.277 -27.289 -30.367 1.00 18.54 C ANISOU 3714 CA VAL B 44 2542 2305 2196 36 42 58 C ATOM 3715 C VAL B 44 51.839 -25.828 -30.250 1.00 18.20 C ANISOU 3715 C VAL B 44 2431 2263 2221 -25 4 67 C ATOM 3716 O VAL B 44 50.794 -25.531 -30.894 1.00 17.92 O ANISOU 3716 O VAL B 44 2303 2273 2233 54 61 10 O ATOM 3717 CB VAL B 44 51.804 -28.002 -29.079 1.00 19.05 C ANISOU 3717 CB VAL B 44 2544 2318 2376 16 49 87 C ATOM 3718 CG1 VAL B 44 50.365 -27.756 -28.690 1.00 18.75 C ANISOU 3718 CG1 VAL B 44 2544 2445 2133 -18 50 40 C ATOM 3719 CG2 VAL B 44 52.001 -29.502 -29.325 1.00 19.48 C ANISOU 3719 CG2 VAL B 44 2755 2310 2336 -37 45 49 C ATOM 3720 N THR B 45 52.518 -25.051 -29.414 1.00 17.46 N ANISOU 3720 N THR B 45 2381 2201 2053 -6 66 111 N ATOM 3721 CA THR B 45 52.015 -23.666 -29.202 1.00 17.72 C ANISOU 3721 CA THR B 45 2490 2174 2067 57 48 84 C ATOM 3722 C THR B 45 52.019 -22.911 -30.524 1.00 18.00 C ANISOU 3722 C THR B 45 2462 2339 2039 116 0 71 C ATOM 3723 O THR B 45 51.079 -22.176 -30.841 1.00 16.73 O ANISOU 3723 O THR B 45 2541 2097 1720 129 -17 -53 O ATOM 3724 CB THR B 45 52.912 -22.959 -28.176 1.00 18.26 C ANISOU 3724 CB THR B 45 2598 2229 2110 60 13 80 C ATOM 3725 OG1 THR B 45 52.865 -23.769 -26.960 1.00 19.07 O ANISOU 3725 OG1 THR B 45 2766 2551 1930 114 -20 79 O ATOM 3726 CG2 THR B 45 52.537 -21.532 -27.832 1.00 18.65 C ANISOU 3726 CG2 THR B 45 2730 2289 2065 49 47 -53 C ATOM 3727 N GLU B 46 53.120 -23.022 -31.294 1.00 19.49 N ANISOU 3727 N GLU B 46 2631 2530 2245 23 136 70 N ATOM 3728 CA GLU B 46 53.175 -22.186 -32.519 1.00 21.10 C ANISOU 3728 CA GLU B 46 2837 2816 2364 -8 32 178 C ATOM 3729 C GLU B 46 52.100 -22.659 -33.473 1.00 20.42 C ANISOU 3729 C GLU B 46 2843 2596 2318 5 119 7 C ATOM 3730 O GLU B 46 51.445 -21.794 -34.073 1.00 21.75 O ANISOU 3730 O GLU B 46 2956 2896 2412 138 -20 2 O ATOM 3731 CB GLU B 46 54.595 -22.159 -33.075 1.00 23.32 C ANISOU 3731 CB GLU B 46 2945 3095 2821 -21 163 124 C ATOM 3732 CG GLU B 46 54.750 -21.251 -34.303 1.00 26.01 C ANISOU 3732 CG GLU B 46 3504 3389 2990 -71 37 252 C ATOM 3733 N ARG B 47 51.760 -23.934 -33.598 1.00 18.78 N ANISOU 3733 N ARG B 47 2574 2612 1947 -1 146 -17 N ATOM 3734 CA ARG B 47 50.674 -24.356 -34.460 1.00 18.46 C ANISOU 3734 CA ARG B 47 2358 2502 2155 65 145 -32 C ATOM 3735 C ARG B 47 49.271 -23.949 -34.028 1.00 17.44 C ANISOU 3735 C ARG B 47 2355 2429 1842 112 88 -12 C ATOM 3736 O ARG B 47 48.451 -23.557 -34.886 1.00 17.23 O ANISOU 3736 O ARG B 47 2349 2659 1538 127 172 -128 O ATOM 3737 CB ARG B 47 50.657 -25.871 -34.647 1.00 19.72 C ANISOU 3737 CB ARG B 47 2531 2527 2436 57 94 -69 C ATOM 3738 CG ARG B 47 51.903 -26.412 -35.360 1.00 20.78 C ANISOU 3738 CG ARG B 47 2621 2687 2586 37 141 -101 C ATOM 3739 CD ARG B 47 51.678 -27.855 -35.804 1.00 21.97 C ANISOU 3739 CD ARG B 47 2924 2661 2764 132 156 -51 C ATOM 3740 NE ARG B 47 51.421 -28.741 -34.656 1.00 22.83 N ANISOU 3740 NE ARG B 47 3126 2870 2679 171 105 -56 N ATOM 3741 CZ ARG B 47 52.393 -29.382 -34.001 1.00 23.47 C ANISOU 3741 CZ ARG B 47 3049 3004 2863 94 69 20 C ATOM 3742 NH1 ARG B 47 52.087 -30.141 -32.949 1.00 23.15 N ANISOU 3742 NH1 ARG B 47 3084 2915 2796 162 73 -8 N ATOM 3743 NH2 ARG B 47 53.669 -29.310 -34.402 1.00 23.71 N ANISOU 3743 NH2 ARG B 47 3014 3042 2954 101 31 -41 N ATOM 3744 N ILE B 48 48.960 -24.064 -32.733 1.00 16.92 N ANISOU 3744 N ILE B 48 2281 2336 1812 119 113 -28 N ATOM 3745 CA ILE B 48 47.718 -23.466 -32.247 1.00 17.05 C ANISOU 3745 CA ILE B 48 2289 2381 1807 97 159 -10 C ATOM 3746 C ILE B 48 47.725 -21.960 -32.447 1.00 17.31 C ANISOU 3746 C ILE B 48 2413 2379 1786 82 150 20 C ATOM 3747 O ILE B 48 46.677 -21.442 -32.878 1.00 17.55 O ANISOU 3747 O ILE B 48 2509 2508 1653 207 182 -58 O ATOM 3748 CB ILE B 48 47.555 -23.815 -30.736 1.00 16.56 C ANISOU 3748 CB ILE B 48 2252 2204 1838 68 132 94 C ATOM 3749 CG1 ILE B 48 47.485 -25.338 -30.598 1.00 16.85 C ANISOU 3749 CG1 ILE B 48 2367 2196 1841 41 141 1 C ATOM 3750 CG2 ILE B 48 46.276 -23.168 -30.188 1.00 16.93 C ANISOU 3750 CG2 ILE B 48 2354 2135 1945 70 193 -43 C ATOM 3751 CD1 ILE B 48 47.395 -25.843 -29.158 1.00 16.30 C ANISOU 3751 CD1 ILE B 48 2254 2112 1828 122 71 -12 C ATOM 3752 N ARG B 49 48.811 -21.227 -32.207 1.00 17.91 N ANISOU 3752 N ARG B 49 2570 2541 1696 24 139 -122 N ATOM 3753 CA ARG B 49 48.756 -19.767 -32.433 1.00 21.01 C ANISOU 3753 CA ARG B 49 3021 2650 2313 95 113 1 C ATOM 3754 C ARG B 49 48.412 -19.426 -33.882 1.00 21.52 C ANISOU 3754 C ARG B 49 3020 2781 2375 168 51 2 C ATOM 3755 O ARG B 49 47.717 -18.465 -34.214 1.00 21.05 O ANISOU 3755 O ARG B 49 3307 2642 2049 246 95 -44 O ATOM 3756 CB ARG B 49 50.088 -19.144 -32.016 1.00 23.35 C ANISOU 3756 CB ARG B 49 3106 3132 2634 -34 29 -112 C ATOM 3757 CG ARG B 49 50.066 -17.630 -32.122 1.00 27.65 C ANISOU 3757 CG ARG B 49 3778 3296 3432 28 39 96 C ATOM 3758 CD ARG B 49 51.293 -16.963 -31.527 1.00 31.66 C ANISOU 3758 CD ARG B 49 4011 3887 4130 -195 -73 -49 C ATOM 3759 NE ARG B 49 51.175 -16.944 -30.037 1.00 35.17 N ANISOU 3759 NE ARG B 49 4585 4446 4334 -201 -71 84 N ATOM 3760 CZ ARG B 49 52.060 -17.661 -29.350 1.00 36.13 C ANISOU 3760 CZ ARG B 49 4632 4497 4598 -105 -70 82 C ATOM 3761 NH1 ARG B 49 53.002 -18.334 -30.014 1.00 37.63 N ANISOU 3761 NH1 ARG B 49 4817 4725 4757 -134 84 -64 N ATOM 3762 NH2 ARG B 49 52.058 -17.700 -28.031 1.00 36.52 N ANISOU 3762 NH2 ARG B 49 4699 4592 4586 -182 61 -29 N ATOM 3763 N ASN B 50 48.956 -20.215 -34.823 1.00 21.87 N ANISOU 3763 N ASN B 50 3095 2739 2475 71 96 -77 N ATOM 3764 CA ASN B 50 48.650 -19.980 -36.244 1.00 22.50 C ANISOU 3764 CA ASN B 50 3106 2884 2559 11 -20 -23 C ATOM 3765 C ASN B 50 47.258 -20.360 -36.700 1.00 22.12 C ANISOU 3765 C ASN B 50 3011 2797 2596 86 82 -7 C ATOM 3766 O ASN B 50 46.716 -19.762 -37.644 1.00 23.52 O ANISOU 3766 O ASN B 50 3214 2885 2836 169 -6 81 O ATOM 3767 CB ASN B 50 49.654 -20.844 -37.036 1.00 24.61 C ANISOU 3767 CB ASN B 50 3346 3189 2815 120 64 -38 C ATOM 3768 CG ASN B 50 51.026 -20.251 -37.026 1.00 26.91 C ANISOU 3768 CG ASN B 50 3490 3521 3213 -13 68 7 C ATOM 3769 OD1 ASN B 50 51.214 -19.047 -36.779 1.00 29.13 O ANISOU 3769 OD1 ASN B 50 3919 3649 3500 -142 63 -36 O ATOM 3770 ND2 ASN B 50 52.057 -21.051 -37.318 1.00 27.88 N ANISOU 3770 ND2 ASN B 50 3675 3685 3232 119 61 0 N ATOM 3771 N ASN B 51 46.626 -21.374 -36.128 1.00 20.46 N ANISOU 3771 N ASN B 51 2806 2592 2374 174 135 -161 N ATOM 3772 CA ASN B 51 45.330 -21.875 -36.483 1.00 21.64 C ANISOU 3772 CA ASN B 51 2861 2826 2536 97 67 -104 C ATOM 3773 C ASN B 51 44.160 -21.332 -35.657 1.00 21.76 C ANISOU 3773 C ASN B 51 2802 2787 2679 122 31 -119 C ATOM 3774 O ASN B 51 43.010 -21.398 -36.152 1.00 21.63 O ANISOU 3774 O ASN B 51 2821 2774 2625 86 57 -180 O ATOM 3775 CB ASN B 51 45.334 -23.407 -36.275 1.00 22.75 C ANISOU 3775 CB ASN B 51 3101 2885 2656 65 33 -68 C ATOM 3776 CG ASN B 51 46.186 -24.072 -37.339 1.00 25.16 C ANISOU 3776 CG ASN B 51 3512 3226 2820 193 61 -156 C ATOM 3777 OD1 ASN B 51 46.050 -23.718 -38.514 1.00 25.53 O ANISOU 3777 OD1 ASN B 51 3784 3163 2752 147 318 -119 O ATOM 3778 ND2 ASN B 51 47.056 -25.037 -37.034 1.00 26.76 N ANISOU 3778 ND2 ASN B 51 3568 3470 3128 301 -46 -261 N ATOM 3779 N ALA B 52 44.426 -20.874 -34.433 1.00 21.73 N ANISOU 3779 N ALA B 52 2936 2781 2538 138 54 24 N ATOM 3780 CA ALA B 52 43.276 -20.506 -33.589 1.00 22.60 C ANISOU 3780 CA ALA B 52 2889 2981 2717 121 93 4 C ATOM 3781 C ALA B 52 42.830 -19.086 -33.904 1.00 24.27 C ANISOU 3781 C ALA B 52 3226 2963 3031 111 67 1 C ATOM 3782 O ALA B 52 43.641 -18.187 -33.751 1.00 25.18 O ANISOU 3782 O ALA B 52 3409 2907 3250 125 74 -14 O ATOM 3783 CB ALA B 52 43.649 -20.608 -32.106 1.00 22.30 C ANISOU 3783 CB ALA B 52 2820 2964 2691 111 50 -86 C ATOM 3784 N LYS B 53 41.602 -18.920 -34.343 1.00 25.83 N ANISOU 3784 N LYS B 53 3318 3384 3111 144 7 -88 N ATOM 3785 CA LYS B 53 41.091 -17.598 -34.705 1.00 27.63 C ANISOU 3785 CA LYS B 53 3627 3402 3469 150 61 -1 C ATOM 3786 C LYS B 53 39.870 -17.276 -33.840 1.00 26.17 C ANISOU 3786 C LYS B 53 3385 3265 3295 96 -81 12 C ATOM 3787 O LYS B 53 39.175 -18.228 -33.498 1.00 25.85 O ANISOU 3787 O LYS B 53 3290 3250 3283 127 -78 -89 O ATOM 3788 CB LYS B 53 40.565 -17.604 -36.140 1.00 31.08 C ANISOU 3788 CB LYS B 53 4125 4011 3673 73 -119 20 C ATOM 3789 CG LYS B 53 41.530 -18.208 -37.147 1.00 33.56 C ANISOU 3789 CG LYS B 53 4263 4324 4166 160 85 -36 C ATOM 3790 CD LYS B 53 42.773 -17.336 -37.258 1.00 35.21 C ANISOU 3790 CD LYS B 53 4421 4472 4486 11 -12 37 C ATOM 3791 CE LYS B 53 43.627 -17.821 -38.432 1.00 36.88 C ANISOU 3791 CE LYS B 53 4681 4702 4630 25 69 -81 C ATOM 3792 NZ LYS B 53 45.026 -17.311 -38.277 1.00 38.07 N ANISOU 3792 NZ LYS B 53 4690 4933 4843 10 68 6 N ATOM 3793 N ILE B 54 39.635 -16.014 -33.548 1.00 24.99 N ANISOU 3793 N ILE B 54 3281 3210 3004 71 -125 -45 N ATOM 3794 CA ILE B 54 38.398 -15.673 -32.836 1.00 25.43 C ANISOU 3794 CA ILE B 54 3310 3203 3151 40 -29 -14 C ATOM 3795 C ILE B 54 37.238 -15.580 -33.824 1.00 26.96 C ANISOU 3795 C ILE B 54 3502 3493 3247 45 -85 -33 C ATOM 3796 O ILE B 54 37.259 -14.738 -34.718 1.00 28.44 O ANISOU 3796 O ILE B 54 3873 3635 3299 59 -168 65 O ATOM 3797 CB ILE B 54 38.580 -14.355 -32.067 1.00 24.83 C ANISOU 3797 CB ILE B 54 3181 3179 3073 88 -47 -13 C ATOM 3798 CG1 ILE B 54 39.739 -14.474 -31.062 1.00 24.23 C ANISOU 3798 CG1 ILE B 54 3099 3012 3096 61 2 -52 C ATOM 3799 CG2 ILE B 54 37.283 -13.951 -31.370 1.00 25.02 C ANISOU 3799 CG2 ILE B 54 3246 3123 3138 129 26 7 C ATOM 3800 CD1 ILE B 54 39.626 -15.609 -30.070 1.00 23.03 C ANISOU 3800 CD1 ILE B 54 2841 3088 2822 148 -84 -72 C ATOM 3801 N ASP B 55 36.232 -16.413 -33.632 1.00 27.85 N ANISOU 3801 N ASP B 55 3591 3574 3416 -8 -57 -113 N ATOM 3802 CA ASP B 55 34.999 -16.340 -34.425 1.00 29.45 C ANISOU 3802 CA ASP B 55 3649 3933 3606 48 -103 -28 C ATOM 3803 C ASP B 55 33.834 -16.293 -33.459 1.00 28.32 C ANISOU 3803 C ASP B 55 3555 3726 3480 -3 -176 -35 C ATOM 3804 O ASP B 55 33.396 -17.368 -33.022 1.00 27.11 O ANISOU 3804 O ASP B 55 3309 3675 3316 10 -322 -128 O ATOM 3805 CB ASP B 55 34.915 -17.581 -35.304 1.00 31.64 C ANISOU 3805 CB ASP B 55 4086 4025 3910 -15 -59 -111 C ATOM 3806 CG ASP B 55 33.729 -17.605 -36.254 1.00 34.14 C ANISOU 3806 CG ASP B 55 4262 4504 4206 52 -184 -77 C ATOM 3807 OD1 ASP B 55 32.728 -16.873 -36.098 1.00 34.55 O ANISOU 3807 OD1 ASP B 55 4336 4592 4199 142 -175 -73 O ATOM 3808 OD2 ASP B 55 33.831 -18.438 -37.185 1.00 35.86 O ANISOU 3808 OD2 ASP B 55 4600 4695 4329 63 -151 -181 O ATOM 3809 N VAL B 56 33.403 -15.085 -33.112 1.00 28.35 N ANISOU 3809 N VAL B 56 3608 3691 3472 50 -197 31 N ATOM 3810 CA VAL B 56 32.344 -14.931 -32.114 1.00 29.54 C ANISOU 3810 CA VAL B 56 3717 3794 3712 53 -74 3 C ATOM 3811 C VAL B 56 31.096 -15.690 -32.507 1.00 30.55 C ANISOU 3811 C VAL B 56 3829 3873 3904 7 -101 -17 C ATOM 3812 O VAL B 56 30.477 -16.367 -31.675 1.00 30.90 O ANISOU 3812 O VAL B 56 3926 3971 3845 70 -126 10 O ATOM 3813 CB VAL B 56 32.038 -13.434 -31.866 1.00 29.65 C ANISOU 3813 CB VAL B 56 3689 3815 3763 26 -74 -22 C ATOM 3814 CG1 VAL B 56 30.930 -13.286 -30.839 1.00 29.41 C ANISOU 3814 CG1 VAL B 56 3708 3761 3705 44 -66 -29 C ATOM 3815 CG2 VAL B 56 33.283 -12.682 -31.398 1.00 29.39 C ANISOU 3815 CG2 VAL B 56 3765 3726 3676 -9 -62 -20 C ATOM 3816 N GLU B 57 30.670 -15.602 -33.772 1.00 31.76 N ANISOU 3816 N GLU B 57 4063 4060 3945 19 -105 8 N ATOM 3817 CA GLU B 57 29.409 -16.232 -34.187 1.00 32.34 C ANISOU 3817 CA GLU B 57 4063 4125 4100 3 -121 26 C ATOM 3818 C GLU B 57 29.446 -17.745 -34.020 1.00 32.05 C ANISOU 3818 C GLU B 57 3996 4141 4039 30 -73 1 C ATOM 3819 O GLU B 57 28.484 -18.382 -33.558 1.00 32.37 O ANISOU 3819 O GLU B 57 3935 4320 4042 -22 -177 39 O ATOM 3820 CB GLU B 57 29.094 -15.870 -35.642 1.00 33.79 C ANISOU 3820 CB GLU B 57 4348 4401 4088 18 -94 -11 C ATOM 3821 N LEU B 58 30.597 -18.353 -34.334 1.00 31.08 N ANISOU 3821 N LEU B 58 3984 3921 3904 28 -50 7 N ATOM 3822 CA LEU B 58 30.754 -19.787 -34.095 1.00 29.93 C ANISOU 3822 CA LEU B 58 3791 3863 3719 -15 -62 -42 C ATOM 3823 C LEU B 58 30.712 -20.150 -32.621 1.00 28.47 C ANISOU 3823 C LEU B 58 3545 3621 3653 -16 -52 -83 C ATOM 3824 O LEU B 58 30.039 -21.109 -32.246 1.00 27.86 O ANISOU 3824 O LEU B 58 3561 3571 3455 -7 -163 -142 O ATOM 3825 CB LEU B 58 32.072 -20.286 -34.686 1.00 30.50 C ANISOU 3825 CB LEU B 58 3811 3910 3869 11 -5 -6 C ATOM 3826 CG LEU B 58 32.385 -21.767 -34.379 1.00 31.38 C ANISOU 3826 CG LEU B 58 3969 3916 4038 -8 13 12 C ATOM 3827 CD1 LEU B 58 31.391 -22.665 -35.095 1.00 31.97 C ANISOU 3827 CD1 LEU B 58 4132 4024 3993 18 -72 -59 C ATOM 3828 CD2 LEU B 58 33.818 -22.110 -34.735 1.00 31.40 C ANISOU 3828 CD2 LEU B 58 3966 3934 4030 47 -44 5 C ATOM 3829 N PHE B 59 31.414 -19.395 -31.762 1.00 27.25 N ANISOU 3829 N PHE B 59 3403 3541 3409 90 -43 -20 N ATOM 3830 CA PHE B 59 31.370 -19.756 -30.337 1.00 26.48 C ANISOU 3830 CA PHE B 59 3337 3363 3359 10 -75 -95 C ATOM 3831 C PHE B 59 29.957 -19.622 -29.801 1.00 27.57 C ANISOU 3831 C PHE B 59 3406 3562 3506 -64 -28 -81 C ATOM 3832 O PHE B 59 29.477 -20.477 -29.051 1.00 27.62 O ANISOU 3832 O PHE B 59 3470 3464 3560 100 -48 -10 O ATOM 3833 CB PHE B 59 32.344 -18.884 -29.545 1.00 24.85 C ANISOU 3833 CB PHE B 59 3060 3262 3119 53 10 -22 C ATOM 3834 CG PHE B 59 33.775 -18.861 -30.018 1.00 23.26 C ANISOU 3834 CG PHE B 59 2971 2987 2879 74 -65 -18 C ATOM 3835 CD1 PHE B 59 34.555 -17.741 -29.845 1.00 22.46 C ANISOU 3835 CD1 PHE B 59 2804 2939 2791 125 -12 41 C ATOM 3836 CD2 PHE B 59 34.354 -19.972 -30.614 1.00 23.27 C ANISOU 3836 CD2 PHE B 59 2883 3054 2903 82 -35 -43 C ATOM 3837 CE1 PHE B 59 35.881 -17.678 -30.268 1.00 22.05 C ANISOU 3837 CE1 PHE B 59 2779 2924 2674 100 -101 11 C ATOM 3838 CE2 PHE B 59 35.676 -19.945 -31.022 1.00 22.66 C ANISOU 3838 CE2 PHE B 59 2870 2951 2787 24 -47 32 C ATOM 3839 CZ PHE B 59 36.440 -18.798 -30.863 1.00 21.78 C ANISOU 3839 CZ PHE B 59 2731 2881 2663 97 -101 32 C ATOM 3840 N LYS B 60 29.279 -18.537 -30.155 1.00 29.29 N ANISOU 3840 N LYS B 60 3684 3700 3744 43 -197 -65 N ATOM 3841 CA LYS B 60 27.916 -18.317 -29.684 1.00 31.91 C ANISOU 3841 CA LYS B 60 3887 4165 4073 -8 20 -85 C ATOM 3842 C LYS B 60 26.982 -19.418 -30.177 1.00 32.16 C ANISOU 3842 C LYS B 60 3981 4105 4135 -1 -52 -36 C ATOM 3843 O LYS B 60 26.148 -19.889 -29.397 1.00 32.35 O ANISOU 3843 O LYS B 60 3961 4147 4183 57 -38 -21 O ATOM 3844 CB LYS B 60 27.405 -16.942 -30.139 1.00 34.16 C ANISOU 3844 CB LYS B 60 4266 4319 4395 84 -8 73 C ATOM 3845 CG LYS B 60 27.988 -15.775 -29.359 1.00 36.95 C ANISOU 3845 CG LYS B 60 4656 4627 4755 -56 -41 -99 C ATOM 3846 CD LYS B 60 27.667 -15.834 -27.875 1.00 39.27 C ANISOU 3846 CD LYS B 60 5029 5028 4863 17 30 -8 C ATOM 3847 CE LYS B 60 28.561 -14.907 -27.048 1.00 40.71 C ANISOU 3847 CE LYS B 60 5148 5141 5180 -44 -57 -30 C ATOM 3848 NZ LYS B 60 28.572 -13.504 -27.533 1.00 41.51 N ANISOU 3848 NZ LYS B 60 5294 5182 5295 -11 -5 31 N ATOM 3849 N LYS B 61 27.145 -19.852 -31.425 1.00 32.20 N ANISOU 3849 N LYS B 61 3975 4157 4102 25 -80 -18 N ATOM 3850 CA LYS B 61 26.322 -20.977 -31.902 1.00 32.43 C ANISOU 3850 CA LYS B 61 3979 4187 4155 -8 -65 -26 C ATOM 3851 C LYS B 61 26.530 -22.249 -31.103 1.00 32.53 C ANISOU 3851 C LYS B 61 3924 4225 4210 -26 -54 -3 C ATOM 3852 O LYS B 61 25.602 -22.994 -30.763 1.00 32.25 O ANISOU 3852 O LYS B 61 3721 4397 4136 -46 -158 24 O ATOM 3853 CB LYS B 61 26.627 -21.245 -33.367 1.00 33.23 C ANISOU 3853 CB LYS B 61 4052 4373 4202 45 -4 -36 C ATOM 3854 N ILE B 62 27.798 -22.570 -30.800 1.00 32.10 N ANISOU 3854 N ILE B 62 3914 4155 4127 10 -109 -38 N ATOM 3855 CA ILE B 62 28.090 -23.763 -30.007 1.00 31.57 C ANISOU 3855 CA ILE B 62 3817 4098 4081 -27 -72 -39 C ATOM 3856 C ILE B 62 27.527 -23.620 -28.610 1.00 31.95 C ANISOU 3856 C ILE B 62 3812 4189 4140 12 -37 18 C ATOM 3857 O ILE B 62 26.980 -24.570 -28.022 1.00 31.65 O ANISOU 3857 O ILE B 62 3769 4079 4176 -47 -72 -76 O ATOM 3858 CB ILE B 62 29.621 -23.968 -29.975 1.00 31.21 C ANISOU 3858 CB ILE B 62 3843 4011 4004 1 -24 -41 C ATOM 3859 CG1 ILE B 62 30.101 -24.189 -31.406 1.00 31.58 C ANISOU 3859 CG1 ILE B 62 3859 4121 4018 -52 0 -47 C ATOM 3860 CG2 ILE B 62 29.968 -25.121 -29.045 1.00 30.74 C ANISOU 3860 CG2 ILE B 62 3795 3963 3922 -34 -58 -69 C ATOM 3861 CD1 ILE B 62 31.597 -24.324 -31.612 1.00 31.56 C ANISOU 3861 CD1 ILE B 62 3869 4029 4092 21 0 -101 C ATOM 3862 N GLU B 63 27.638 -22.416 -28.038 1.00 33.08 N ANISOU 3862 N GLU B 63 3924 4216 4428 26 -96 -12 N ATOM 3863 CA GLU B 63 27.105 -22.195 -26.697 1.00 35.81 C ANISOU 3863 CA GLU B 63 4455 4647 4505 31 4 -32 C ATOM 3864 C GLU B 63 25.597 -22.422 -26.600 1.00 37.93 C ANISOU 3864 C GLU B 63 4575 4914 4922 -57 51 -17 C ATOM 3865 O GLU B 63 25.109 -22.836 -25.537 1.00 36.99 O ANISOU 3865 O GLU B 63 4402 4861 4791 -70 -51 -62 O ATOM 3866 CB GLU B 63 27.461 -20.797 -26.208 1.00 36.35 C ANISOU 3866 CB GLU B 63 4457 4603 4752 7 -19 14 C ATOM 3867 CG GLU B 63 27.270 -20.603 -24.717 1.00 38.18 C ANISOU 3867 CG GLU B 63 4798 4912 4796 27 6 7 C ATOM 3868 CD GLU B 63 27.573 -19.162 -24.324 1.00 40.26 C ANISOU 3868 CD GLU B 63 5119 5023 5154 -54 -16 -43 C ATOM 3869 OE1 GLU B 63 26.891 -18.652 -23.400 1.00 41.23 O ANISOU 3869 OE1 GLU B 63 5226 5266 5172 -47 28 -51 O ATOM 3870 OE2 GLU B 63 28.476 -18.551 -24.945 1.00 41.03 O ANISOU 3870 OE2 GLU B 63 5237 5169 5182 -65 53 18 O ATOM 3871 N GLU B 64 24.849 -22.170 -27.675 1.00 40.65 N ANISOU 3871 N GLU B 64 5068 5282 5094 49 -130 2 N ATOM 3872 CA GLU B 64 23.422 -22.517 -27.670 1.00 43.28 C ANISOU 3872 CA GLU B 64 5220 5705 5519 -50 -36 -1 C ATOM 3873 C GLU B 64 23.231 -24.005 -27.414 1.00 45.16 C ANISOU 3873 C GLU B 64 5659 5760 5741 -61 -69 23 C ATOM 3874 O GLU B 64 22.325 -24.356 -26.649 1.00 46.10 O ANISOU 3874 O GLU B 64 5673 5987 5855 -58 -41 12 O ATOM 3875 CB GLU B 64 22.746 -22.076 -28.962 1.00 43.56 C ANISOU 3875 CB GLU B 64 5366 5665 5519 -1 -57 -5 C ATOM 3876 N LYS B 65 24.049 -24.879 -27.978 1.00 46.61 N ANISOU 3876 N LYS B 65 5792 5994 5923 16 -8 -52 N ATOM 3877 CA LYS B 65 24.011 -26.294 -27.622 1.00 48.09 C ANISOU 3877 CA LYS B 65 6023 6055 6195 -34 4 4 C ATOM 3878 C LYS B 65 24.571 -26.543 -26.229 1.00 49.52 C ANISOU 3878 C LYS B 65 6234 6320 6263 -18 -33 7 C ATOM 3879 O LYS B 65 23.947 -27.168 -25.368 1.00 50.82 O ANISOU 3879 O LYS B 65 6376 6476 6456 -47 82 42 O ATOM 3880 CB LYS B 65 24.766 -27.096 -28.673 1.00 47.92 C ANISOU 3880 CB LYS B 65 6019 6065 6125 -42 -6 4 C ATOM 3881 N THR B 66 25.784 -26.054 -25.970 1.00 49.78 N ANISOU 3881 N THR B 66 6267 6339 6308 -33 -58 -11 N ATOM 3882 CA THR B 66 26.495 -26.299 -24.731 1.00 49.35 C ANISOU 3882 CA THR B 66 6233 6295 6221 -21 11 -36 C ATOM 3883 C THR B 66 25.795 -25.739 -23.499 1.00 48.59 C ANISOU 3883 C THR B 66 6133 6128 6201 -28 1 14 C ATOM 3884 O THR B 66 25.813 -26.334 -22.417 1.00 49.43 O ANISOU 3884 O THR B 66 6282 6301 6199 -80 -3 40 O ATOM 3885 CB THR B 66 27.886 -25.622 -24.816 1.00 49.85 C ANISOU 3885 CB THR B 66 6210 6411 6319 -10 -8 -4 C ATOM 3886 OG1 THR B 66 28.621 -26.190 -25.910 1.00 50.60 O ANISOU 3886 OG1 THR B 66 6344 6495 6385 -13 28 -56 O ATOM 3887 CG2 THR B 66 28.651 -25.847 -23.528 1.00 50.40 C ANISOU 3887 CG2 THR B 66 6353 6486 6310 -10 -29 -38 C ATOM 3888 N ASN B 67 25.342 -24.497 -23.599 1.00 46.96 N ANISOU 3888 N ASN B 67 5847 6062 5933 -37 18 -66 N ATOM 3889 CA ASN B 67 24.977 -23.658 -22.470 1.00 45.40 C ANISOU 3889 CA ASN B 67 5592 5897 5761 -58 -55 1 C ATOM 3890 C ASN B 67 26.117 -23.330 -21.520 1.00 43.87 C ANISOU 3890 C ASN B 67 5363 5707 5599 -12 112 -16 C ATOM 3891 O ASN B 67 25.874 -22.910 -20.377 1.00 44.99 O ANISOU 3891 O ASN B 67 5610 5839 5644 -43 59 -73 O ATOM 3892 CB ASN B 67 23.837 -24.316 -21.703 1.00 46.02 C ANISOU 3892 CB ASN B 67 5769 5912 5806 -83 3 5 C ATOM 3893 N HIS B 68 27.377 -23.469 -21.893 1.00 40.74 N ANISOU 3893 N HIS B 68 5138 5243 5098 -69 -68 -60 N ATOM 3894 CA HIS B 68 28.544 -23.192 -21.080 1.00 37.76 C ANISOU 3894 CA HIS B 68 4751 4861 4735 -140 234 19 C ATOM 3895 C HIS B 68 29.548 -22.440 -21.960 1.00 32.96 C ANISOU 3895 C HIS B 68 4145 4119 4261 19 -76 -126 C ATOM 3896 O HIS B 68 29.973 -23.005 -22.968 1.00 31.31 O ANISOU 3896 O HIS B 68 3714 4015 4166 -141 -8 26 O ATOM 3897 CB HIS B 68 29.269 -24.425 -20.562 1.00 41.30 C ANISOU 3897 CB HIS B 68 5220 5209 5263 114 -47 5 C ATOM 3898 CG HIS B 68 28.467 -25.403 -19.773 1.00 44.63 C ANISOU 3898 CG HIS B 68 5637 5620 5700 -89 70 115 C ATOM 3899 ND1 HIS B 68 28.196 -26.687 -20.223 1.00 46.14 N ANISOU 3899 ND1 HIS B 68 5897 5743 5890 -56 24 -8 N ATOM 3900 CD2 HIS B 68 27.862 -25.274 -18.562 1.00 45.73 C ANISOU 3900 CD2 HIS B 68 5827 5812 5735 -14 65 7 C ATOM 3901 CE1 HIS B 68 27.456 -27.305 -19.314 1.00 46.84 C ANISOU 3901 CE1 HIS B 68 5986 5881 5932 -61 57 30 C ATOM 3902 NE2 HIS B 68 27.246 -26.474 -18.299 1.00 46.82 N ANISOU 3902 NE2 HIS B 68 5978 5872 5940 -65 86 35 N ATOM 3903 N ASP B 69 29.860 -21.205 -21.610 1.00 28.70 N ANISOU 3903 N ASP B 69 3407 3941 3558 15 70 69 N ATOM 3904 CA ASP B 69 30.574 -20.338 -22.556 1.00 27.03 C ANISOU 3904 CA ASP B 69 3150 3586 3533 54 7 -26 C ATOM 3905 C ASP B 69 32.003 -20.783 -22.823 1.00 23.92 C ANISOU 3905 C ASP B 69 3019 3126 2945 -38 -37 49 C ATOM 3906 O ASP B 69 32.447 -20.832 -23.992 1.00 21.75 O ANISOU 3906 O ASP B 69 2498 2906 2859 10 -88 -18 O ATOM 3907 CB ASP B 69 30.497 -18.892 -22.069 1.00 28.93 C ANISOU 3907 CB ASP B 69 3542 3610 3840 13 87 -50 C ATOM 3908 CG ASP B 69 30.837 -18.677 -20.608 1.00 31.29 C ANISOU 3908 CG ASP B 69 3845 4088 3955 -19 -12 -26 C ATOM 3909 OD1 ASP B 69 30.717 -17.530 -20.087 1.00 32.64 O ANISOU 3909 OD1 ASP B 69 4026 4185 4193 -27 -16 -144 O ATOM 3910 OD2 ASP B 69 31.226 -19.632 -19.900 1.00 32.34 O ANISOU 3910 OD2 ASP B 69 4001 4129 4159 -16 23 36 O ATOM 3911 N VAL B 70 32.761 -21.163 -21.776 1.00 22.17 N ANISOU 3911 N VAL B 70 2725 2873 2826 -22 35 -8 N ATOM 3912 CA VAL B 70 34.162 -21.542 -22.028 1.00 20.86 C ANISOU 3912 CA VAL B 70 2671 2600 2654 -11 -22 -24 C ATOM 3913 C VAL B 70 34.261 -22.869 -22.783 1.00 20.70 C ANISOU 3913 C VAL B 70 2617 2728 2521 -13 -9 -59 C ATOM 3914 O VAL B 70 35.094 -23.035 -23.664 1.00 19.06 O ANISOU 3914 O VAL B 70 2410 2457 2376 -30 -106 -115 O ATOM 3915 CB VAL B 70 34.971 -21.673 -20.734 1.00 21.16 C ANISOU 3915 CB VAL B 70 2804 2642 2595 10 -27 -48 C ATOM 3916 CG1 VAL B 70 36.430 -22.094 -20.951 1.00 20.84 C ANISOU 3916 CG1 VAL B 70 2749 2648 2523 -32 -148 -26 C ATOM 3917 CG2 VAL B 70 34.948 -20.321 -20.017 1.00 21.37 C ANISOU 3917 CG2 VAL B 70 2903 2593 2623 64 -122 3 C ATOM 3918 N VAL B 71 33.390 -23.796 -22.403 1.00 21.66 N ANISOU 3918 N VAL B 71 2796 2663 2770 -48 -6 14 N ATOM 3919 CA VAL B 71 33.352 -25.092 -23.096 1.00 23.52 C ANISOU 3919 CA VAL B 71 3156 2891 2890 -50 -40 -122 C ATOM 3920 C VAL B 71 33.073 -24.885 -24.570 1.00 21.34 C ANISOU 3920 C VAL B 71 2675 2566 2865 -44 2 -22 C ATOM 3921 O VAL B 71 33.729 -25.527 -25.405 1.00 20.61 O ANISOU 3921 O VAL B 71 2717 2399 2714 -99 -23 15 O ATOM 3922 CB VAL B 71 32.319 -26.035 -22.451 1.00 26.31 C ANISOU 3922 CB VAL B 71 3462 3208 3327 -151 49 26 C ATOM 3923 CG1 VAL B 71 32.095 -27.288 -23.296 1.00 27.95 C ANISOU 3923 CG1 VAL B 71 3805 3289 3525 -91 -11 -73 C ATOM 3924 CG2 VAL B 71 32.785 -26.473 -21.061 1.00 27.99 C ANISOU 3924 CG2 VAL B 71 3753 3502 3379 4 37 37 C ATOM 3925 N ALA B 72 32.151 -23.999 -24.938 1.00 20.57 N ANISOU 3925 N ALA B 72 2642 2471 2702 -78 -77 -73 N ATOM 3926 CA ALA B 72 31.896 -23.745 -26.354 1.00 20.65 C ANISOU 3926 CA ALA B 72 2566 2593 2686 7 -35 -13 C ATOM 3927 C ALA B 72 33.098 -23.133 -27.043 1.00 20.24 C ANISOU 3927 C ALA B 72 2470 2612 2610 25 -105 -123 C ATOM 3928 O ALA B 72 33.383 -23.446 -28.215 1.00 20.79 O ANISOU 3928 O ALA B 72 2466 2810 2623 60 -56 -142 O ATOM 3929 CB ALA B 72 30.671 -22.833 -26.496 1.00 21.37 C ANISOU 3929 CB ALA B 72 2635 2738 2745 97 -107 -89 C ATOM 3930 N PHE B 73 33.773 -22.185 -26.351 1.00 18.32 N ANISOU 3930 N PHE B 73 2198 2296 2465 90 -73 -38 N ATOM 3931 CA PHE B 73 35.012 -21.665 -26.935 1.00 17.32 C ANISOU 3931 CA PHE B 73 2264 2133 2182 66 -89 -125 C ATOM 3932 C PHE B 73 36.045 -22.775 -27.109 1.00 16.90 C ANISOU 3932 C PHE B 73 2196 2117 2109 12 3 -97 C ATOM 3933 O PHE B 73 36.681 -22.815 -28.166 1.00 16.79 O ANISOU 3933 O PHE B 73 2198 2092 2089 296 -6 -69 O ATOM 3934 CB PHE B 73 35.528 -20.568 -25.989 1.00 17.28 C ANISOU 3934 CB PHE B 73 2298 2127 2141 -8 -58 -123 C ATOM 3935 CG PHE B 73 36.949 -20.140 -26.183 1.00 16.36 C ANISOU 3935 CG PHE B 73 2253 1953 2008 62 -16 -223 C ATOM 3936 CD1 PHE B 73 37.274 -19.217 -27.138 1.00 16.61 C ANISOU 3936 CD1 PHE B 73 2258 2022 2029 -22 57 -256 C ATOM 3937 CD2 PHE B 73 37.945 -20.658 -25.352 1.00 16.63 C ANISOU 3937 CD2 PHE B 73 2182 2000 2138 44 -4 -285 C ATOM 3938 CE1 PHE B 73 38.587 -18.792 -27.325 1.00 17.04 C ANISOU 3938 CE1 PHE B 73 2213 2110 2152 47 -6 -236 C ATOM 3939 CE2 PHE B 73 39.249 -20.228 -25.525 1.00 16.49 C ANISOU 3939 CE2 PHE B 73 2215 2006 2044 45 50 -247 C ATOM 3940 CZ PHE B 73 39.569 -19.304 -26.485 1.00 16.66 C ANISOU 3940 CZ PHE B 73 2333 1969 2028 43 -7 -258 C ATOM 3941 N VAL B 74 36.226 -23.640 -26.113 1.00 16.88 N ANISOU 3941 N VAL B 74 2247 2051 2116 30 -192 -183 N ATOM 3942 CA VAL B 74 37.257 -24.698 -26.266 1.00 18.40 C ANISOU 3942 CA VAL B 74 2418 2205 2369 109 -71 -119 C ATOM 3943 C VAL B 74 36.896 -25.616 -27.435 1.00 19.16 C ANISOU 3943 C VAL B 74 2575 2356 2349 37 -8 -121 C ATOM 3944 O VAL B 74 37.750 -26.053 -28.216 1.00 18.27 O ANISOU 3944 O VAL B 74 2509 2062 2370 -7 -59 -142 O ATOM 3945 CB VAL B 74 37.382 -25.474 -24.938 1.00 19.49 C ANISOU 3945 CB VAL B 74 2573 2425 2406 88 -79 -90 C ATOM 3946 CG1 VAL B 74 38.268 -26.721 -25.073 1.00 20.33 C ANISOU 3946 CG1 VAL B 74 2726 2432 2567 149 -148 37 C ATOM 3947 CG2 VAL B 74 37.979 -24.534 -23.857 1.00 19.99 C ANISOU 3947 CG2 VAL B 74 2572 2593 2430 114 -107 -119 C ATOM 3948 N GLU B 75 35.627 -25.979 -27.554 1.00 20.90 N ANISOU 3948 N GLU B 75 2613 2632 2697 10 -94 -47 N ATOM 3949 CA GLU B 75 35.173 -26.788 -28.695 1.00 23.18 C ANISOU 3949 CA GLU B 75 3096 2889 2823 -30 -80 -119 C ATOM 3950 C GLU B 75 35.348 -26.082 -30.032 1.00 21.92 C ANISOU 3950 C GLU B 75 2777 2800 2751 36 -50 -163 C ATOM 3951 O GLU B 75 35.815 -26.748 -30.969 1.00 21.96 O ANISOU 3951 O GLU B 75 2804 2803 2738 36 -76 -211 O ATOM 3952 CB GLU B 75 33.683 -27.139 -28.519 1.00 26.76 C ANISOU 3952 CB GLU B 75 3150 3436 3583 -48 4 -125 C ATOM 3953 CG GLU B 75 33.504 -27.965 -27.249 1.00 31.34 C ANISOU 3953 CG GLU B 75 4110 3979 3818 3 -24 91 C ATOM 3954 CD GLU B 75 32.173 -28.679 -27.196 1.00 35.14 C ANISOU 3954 CD GLU B 75 4291 4502 4558 -146 25 39 C ATOM 3955 OE1 GLU B 75 31.305 -28.445 -28.072 1.00 37.08 O ANISOU 3955 OE1 GLU B 75 4464 4773 4850 -65 -113 94 O ATOM 3956 OE2 GLU B 75 31.994 -29.508 -26.279 1.00 36.97 O ANISOU 3956 OE2 GLU B 75 4762 4712 4572 -114 29 95 O ATOM 3957 N GLY B 76 35.026 -24.798 -30.115 1.00 20.62 N ANISOU 3957 N GLY B 76 2657 2680 2499 -75 -167 -10 N ATOM 3958 CA GLY B 76 35.216 -24.021 -31.313 1.00 20.02 C ANISOU 3958 CA GLY B 76 2525 2617 2463 -65 -29 -120 C ATOM 3959 C GLY B 76 36.665 -23.925 -31.727 1.00 19.65 C ANISOU 3959 C GLY B 76 2497 2593 2376 15 -80 -144 C ATOM 3960 O GLY B 76 37.003 -24.191 -32.904 1.00 20.28 O ANISOU 3960 O GLY B 76 2673 2721 2310 -1 -129 -169 O ATOM 3961 N ILE B 77 37.544 -23.573 -30.769 1.00 18.55 N ANISOU 3961 N ILE B 77 2395 2329 2322 73 -32 -199 N ATOM 3962 CA ILE B 77 38.977 -23.582 -31.085 1.00 18.42 C ANISOU 3962 CA ILE B 77 2346 2310 2342 -4 -37 -172 C ATOM 3963 C ILE B 77 39.404 -25.008 -31.446 1.00 19.58 C ANISOU 3963 C ILE B 77 2540 2424 2478 72 -10 -132 C ATOM 3964 O ILE B 77 40.104 -25.240 -32.429 1.00 20.74 O ANISOU 3964 O ILE B 77 2657 2671 2554 120 15 -237 O ATOM 3965 CB ILE B 77 39.827 -23.046 -29.938 1.00 17.41 C ANISOU 3965 CB ILE B 77 2164 2228 2222 50 25 -176 C ATOM 3966 CG1 ILE B 77 39.477 -21.566 -29.623 1.00 16.95 C ANISOU 3966 CG1 ILE B 77 2175 2133 2132 99 -58 -60 C ATOM 3967 CG2 ILE B 77 41.325 -23.132 -30.237 1.00 16.72 C ANISOU 3967 CG2 ILE B 77 2184 2199 1969 185 -3 -357 C ATOM 3968 CD1 ILE B 77 39.855 -20.558 -30.710 1.00 18.05 C ANISOU 3968 CD1 ILE B 77 2155 2273 2432 62 180 -20 C ATOM 3969 N GLY B 78 38.938 -26.013 -30.742 1.00 21.12 N ANISOU 3969 N GLY B 78 2778 2558 2688 -95 -100 -45 N ATOM 3970 CA GLY B 78 39.272 -27.414 -31.030 1.00 23.17 C ANISOU 3970 CA GLY B 78 3077 2763 2963 78 44 -107 C ATOM 3971 C GLY B 78 39.038 -27.755 -32.492 1.00 24.79 C ANISOU 3971 C GLY B 78 3246 3098 3075 -5 -1 -120 C ATOM 3972 O GLY B 78 39.882 -28.422 -33.095 1.00 26.06 O ANISOU 3972 O GLY B 78 3522 3235 3146 76 110 -224 O ATOM 3973 N SER B 79 37.983 -27.246 -33.097 1.00 25.71 N ANISOU 3973 N SER B 79 3254 3270 3243 33 -50 -81 N ATOM 3974 CA SER B 79 37.603 -27.463 -34.471 1.00 26.62 C ANISOU 3974 CA SER B 79 3476 3430 3207 -10 36 -88 C ATOM 3975 C SER B 79 38.553 -26.811 -35.456 1.00 26.14 C ANISOU 3975 C SER B 79 3402 3348 3184 -126 -45 -141 C ATOM 3976 O SER B 79 38.507 -27.175 -36.655 1.00 27.99 O ANISOU 3976 O SER B 79 3684 3726 3224 -31 -32 -382 O ATOM 3977 CB SER B 79 36.161 -26.949 -34.689 1.00 27.21 C ANISOU 3977 CB SER B 79 3493 3510 3336 -24 -81 -77 C ATOM 3978 OG SER B 79 36.149 -25.545 -34.994 1.00 28.43 O ANISOU 3978 OG SER B 79 3764 3612 3425 86 -122 -121 O ATOM 3979 N MET B 80 39.382 -25.862 -35.069 1.00 23.76 N ANISOU 3979 N MET B 80 3069 3194 2763 3 -37 -178 N ATOM 3980 CA MET B 80 40.371 -25.272 -35.955 1.00 21.89 C ANISOU 3980 CA MET B 80 2962 2720 2635 53 -112 -124 C ATOM 3981 C MET B 80 41.766 -25.868 -35.809 1.00 21.25 C ANISOU 3981 C MET B 80 2911 2670 2493 53 6 -50 C ATOM 3982 O MET B 80 42.673 -25.555 -36.609 1.00 21.41 O ANISOU 3982 O MET B 80 3086 2687 2361 65 24 -134 O ATOM 3983 CB MET B 80 40.452 -23.780 -35.641 1.00 21.44 C ANISOU 3983 CB MET B 80 2734 2610 2804 179 -57 -20 C ATOM 3984 CG MET B 80 39.102 -23.053 -35.779 1.00 19.49 C ANISOU 3984 CG MET B 80 2706 2020 2679 26 -118 -192 C ATOM 3985 SD MET B 80 39.334 -21.370 -35.209 1.00 17.11 S ANISOU 3985 SD MET B 80 2174 1875 2452 327 -284 -250 S ATOM 3986 CE MET B 80 37.662 -21.024 -34.673 1.00 19.41 C ANISOU 3986 CE MET B 80 2206 2581 2589 -34 12 -29 C ATOM 3987 N ILE B 81 42.056 -26.642 -34.753 1.00 20.72 N ANISOU 3987 N ILE B 81 2834 2650 2390 94 17 -156 N ATOM 3988 CA ILE B 81 43.471 -26.879 -34.407 1.00 20.33 C ANISOU 3988 CA ILE B 81 2845 2614 2264 40 -68 -104 C ATOM 3989 C ILE B 81 43.822 -28.349 -34.526 1.00 21.43 C ANISOU 3989 C ILE B 81 2940 2739 2466 135 -41 -56 C ATOM 3990 O ILE B 81 44.914 -28.782 -34.150 1.00 21.48 O ANISOU 3990 O ILE B 81 2970 2926 2264 278 86 -190 O ATOM 3991 CB ILE B 81 43.869 -26.336 -33.024 1.00 19.67 C ANISOU 3991 CB ILE B 81 2780 2474 2221 -20 8 -39 C ATOM 3992 CG1 ILE B 81 43.025 -26.976 -31.914 1.00 19.11 C ANISOU 3992 CG1 ILE B 81 2634 2456 2171 20 -49 24 C ATOM 3993 CG2 ILE B 81 43.762 -24.812 -33.037 1.00 18.96 C ANISOU 3993 CG2 ILE B 81 2793 2436 1976 14 -28 22 C ATOM 3994 CD1 ILE B 81 43.590 -26.606 -30.522 1.00 19.10 C ANISOU 3994 CD1 ILE B 81 2638 2391 2227 69 -25 -64 C ATOM 3995 N GLY B 82 42.865 -29.147 -35.001 1.00 22.99 N ANISOU 3995 N GLY B 82 3161 2801 2771 -11 -40 -44 N ATOM 3996 CA GLY B 82 43.201 -30.528 -35.382 1.00 24.60 C ANISOU 3996 CA GLY B 82 3377 2962 3006 116 -9 -121 C ATOM 3997 C GLY B 82 43.653 -31.341 -34.189 1.00 25.36 C ANISOU 3997 C GLY B 82 3387 3224 3024 10 -22 -30 C ATOM 3998 O GLY B 82 43.060 -31.272 -33.102 1.00 25.06 O ANISOU 3998 O GLY B 82 3331 3133 3059 19 -53 -104 O ATOM 3999 N GLU B 83 44.763 -32.073 -34.298 1.00 26.11 N ANISOU 3999 N GLU B 83 3477 3324 3119 78 -27 -155 N ATOM 4000 CA GLU B 83 45.207 -33.006 -33.295 1.00 28.34 C ANISOU 4000 CA GLU B 83 3858 3600 3309 -58 -162 6 C ATOM 4001 C GLU B 83 45.797 -32.267 -32.089 1.00 25.43 C ANISOU 4001 C GLU B 83 3460 3028 3173 14 31 13 C ATOM 4002 O GLU B 83 45.843 -32.851 -30.997 1.00 25.12 O ANISOU 4002 O GLU B 83 3556 2927 3062 42 43 -156 O ATOM 4003 CB GLU B 83 46.319 -33.930 -33.809 1.00 33.46 C ANISOU 4003 CB GLU B 83 4277 4095 4339 235 97 58 C ATOM 4004 CG GLU B 83 45.958 -34.638 -35.092 1.00 39.77 C ANISOU 4004 CG GLU B 83 5283 5057 4772 70 -108 -213 C ATOM 4005 CD GLU B 83 45.079 -35.851 -34.842 1.00 44.15 C ANISOU 4005 CD GLU B 83 5624 5488 5662 -140 17 14 C ATOM 4006 OE1 GLU B 83 44.368 -35.921 -33.810 1.00 45.79 O ANISOU 4006 OE1 GLU B 83 5894 5805 5700 -31 111 -94 O ATOM 4007 OE2 GLU B 83 45.116 -36.764 -35.712 1.00 46.66 O ANISOU 4007 OE2 GLU B 83 6040 5784 5903 7 48 -159 O ATOM 4008 N ASP B 84 46.167 -31.020 -32.229 1.00 22.37 N ANISOU 4008 N ASP B 84 3038 2941 2522 30 26 -85 N ATOM 4009 CA ASP B 84 46.706 -30.220 -31.134 1.00 21.08 C ANISOU 4009 CA ASP B 84 2808 2697 2506 42 62 -68 C ATOM 4010 C ASP B 84 45.626 -29.935 -30.105 1.00 19.80 C ANISOU 4010 C ASP B 84 2603 2540 2380 -35 -21 -67 C ATOM 4011 O ASP B 84 45.964 -29.478 -28.986 1.00 19.56 O ANISOU 4011 O ASP B 84 2621 2552 2261 -2 103 -76 O ATOM 4012 CB ASP B 84 47.315 -28.926 -31.668 1.00 21.82 C ANISOU 4012 CB ASP B 84 2913 2695 2682 -41 7 -55 C ATOM 4013 CG ASP B 84 48.611 -29.184 -32.405 1.00 23.80 C ANISOU 4013 CG ASP B 84 3047 2990 3005 48 90 -17 C ATOM 4014 OD1 ASP B 84 49.300 -30.161 -32.006 1.00 25.96 O ANISOU 4014 OD1 ASP B 84 3443 3026 3393 128 27 18 O ATOM 4015 OD2 ASP B 84 49.015 -28.507 -33.357 1.00 24.57 O ANISOU 4015 OD2 ASP B 84 3289 3030 3017 95 144 10 O ATOM 4016 N SER B 85 44.359 -30.223 -30.335 1.00 19.49 N ANISOU 4016 N SER B 85 2609 2458 2339 42 -73 -129 N ATOM 4017 CA SER B 85 43.326 -30.086 -29.306 1.00 20.62 C ANISOU 4017 CA SER B 85 2624 2598 2612 68 45 -17 C ATOM 4018 C SER B 85 43.596 -30.931 -28.086 1.00 21.26 C ANISOU 4018 C SER B 85 2747 2667 2666 160 13 -31 C ATOM 4019 O SER B 85 43.194 -30.557 -26.967 1.00 20.66 O ANISOU 4019 O SER B 85 2423 2670 2758 326 -34 -83 O ATOM 4020 CB SER B 85 41.912 -30.353 -29.847 1.00 22.42 C ANISOU 4020 CB SER B 85 2782 2854 2882 -21 -60 -70 C ATOM 4021 OG SER B 85 41.828 -31.747 -30.120 1.00 25.12 O ANISOU 4021 OG SER B 85 3238 2967 3337 -82 -56 -54 O ATOM 4022 N ARG B 86 44.306 -32.062 -28.175 1.00 20.98 N ANISOU 4022 N ARG B 86 2666 2548 2756 152 -11 -78 N ATOM 4023 CA ARG B 86 44.721 -32.867 -27.055 1.00 22.76 C ANISOU 4023 CA ARG B 86 2987 2891 2772 21 -87 -1 C ATOM 4024 C ARG B 86 45.441 -32.053 -25.990 1.00 20.52 C ANISOU 4024 C ARG B 86 2743 2454 2602 91 111 34 C ATOM 4025 O ARG B 86 45.377 -32.387 -24.806 1.00 21.84 O ANISOU 4025 O ARG B 86 3020 2603 2673 87 56 103 O ATOM 4026 CB ARG B 86 45.712 -33.984 -27.516 1.00 26.89 C ANISOU 4026 CB ARG B 86 3474 3163 3580 306 53 -7 C ATOM 4027 CG ARG B 86 45.290 -34.745 -28.775 1.00 32.63 C ANISOU 4027 CG ARG B 86 4300 4063 4037 -37 -121 -185 C ATOM 4028 CD ARG B 86 46.361 -35.765 -29.235 1.00 36.65 C ANISOU 4028 CD ARG B 86 4672 4468 4785 188 104 -191 C ATOM 4029 NE ARG B 86 47.171 -35.212 -30.320 1.00 39.62 N ANISOU 4029 NE ARG B 86 5080 4980 4993 -25 132 17 N ATOM 4030 CZ ARG B 86 48.346 -35.598 -30.777 1.00 40.98 C ANISOU 4030 CZ ARG B 86 5190 5195 5186 75 125 -46 C ATOM 4031 NH1 ARG B 86 49.002 -36.628 -30.273 1.00 42.26 N ANISOU 4031 NH1 ARG B 86 5449 5316 5291 103 43 13 N ATOM 4032 NH2 ARG B 86 48.938 -34.951 -31.772 1.00 41.62 N ANISOU 4032 NH2 ARG B 86 5333 5287 5194 22 100 -13 N ATOM 4033 N PHE B 87 46.198 -31.040 -26.296 1.00 18.37 N ANISOU 4033 N PHE B 87 2497 2229 2255 173 6 -88 N ATOM 4034 CA PHE B 87 47.054 -30.276 -25.410 1.00 17.94 C ANISOU 4034 CA PHE B 87 2420 2144 2254 181 -15 -60 C ATOM 4035 C PHE B 87 46.496 -28.870 -25.136 1.00 16.76 C ANISOU 4035 C PHE B 87 2190 2042 2136 75 35 -33 C ATOM 4036 O PHE B 87 47.152 -28.046 -24.497 1.00 17.11 O ANISOU 4036 O PHE B 87 2357 1986 2160 236 21 -159 O ATOM 4037 CB PHE B 87 48.426 -30.041 -26.060 1.00 19.75 C ANISOU 4037 CB PHE B 87 2470 2528 2505 31 9 -57 C ATOM 4038 CG PHE B 87 49.098 -31.365 -26.387 1.00 22.70 C ANISOU 4038 CG PHE B 87 2831 2780 3015 175 -18 -151 C ATOM 4039 CD1 PHE B 87 49.417 -31.677 -27.693 1.00 24.65 C ANISOU 4039 CD1 PHE B 87 3132 3135 3099 101 38 -200 C ATOM 4040 CD2 PHE B 87 49.381 -32.237 -25.385 1.00 23.85 C ANISOU 4040 CD2 PHE B 87 3060 2900 3101 72 -36 -83 C ATOM 4041 CE1 PHE B 87 50.038 -32.886 -27.969 1.00 25.92 C ANISOU 4041 CE1 PHE B 87 3351 3151 3346 166 -12 -85 C ATOM 4042 CE2 PHE B 87 50.018 -33.466 -25.663 1.00 25.43 C ANISOU 4042 CE2 PHE B 87 3245 3102 3315 162 -14 -139 C ATOM 4043 CZ PHE B 87 50.334 -33.763 -26.966 1.00 25.26 C ANISOU 4043 CZ PHE B 87 3258 3076 3264 111 44 -148 C ATOM 4044 N PHE B 88 45.292 -28.606 -25.615 1.00 16.37 N ANISOU 4044 N PHE B 88 2296 1962 1961 249 42 -35 N ATOM 4045 CA PHE B 88 44.695 -27.272 -25.404 1.00 15.60 C ANISOU 4045 CA PHE B 88 2196 1912 1819 194 63 -42 C ATOM 4046 C PHE B 88 43.737 -27.358 -24.225 1.00 15.01 C ANISOU 4046 C PHE B 88 2013 1795 1893 101 55 -12 C ATOM 4047 O PHE B 88 43.023 -28.361 -24.047 1.00 15.36 O ANISOU 4047 O PHE B 88 2066 1775 1996 149 152 -132 O ATOM 4048 CB PHE B 88 43.994 -26.839 -26.695 1.00 15.75 C ANISOU 4048 CB PHE B 88 2116 2016 1852 82 -55 -24 C ATOM 4049 CG PHE B 88 43.392 -25.453 -26.681 1.00 16.07 C ANISOU 4049 CG PHE B 88 2153 2091 1861 89 -9 -85 C ATOM 4050 CD1 PHE B 88 44.159 -24.344 -26.951 1.00 15.91 C ANISOU 4050 CD1 PHE B 88 2318 1982 1745 119 18 -63 C ATOM 4051 CD2 PHE B 88 42.028 -25.314 -26.405 1.00 16.69 C ANISOU 4051 CD2 PHE B 88 2162 2261 1919 185 -108 -122 C ATOM 4052 CE1 PHE B 88 43.602 -23.063 -26.953 1.00 16.48 C ANISOU 4052 CE1 PHE B 88 2270 2182 1810 213 -94 -184 C ATOM 4053 CE2 PHE B 88 41.493 -24.026 -26.396 1.00 16.92 C ANISOU 4053 CE2 PHE B 88 2284 2183 1963 78 -107 -97 C ATOM 4054 CZ PHE B 88 42.257 -22.932 -26.674 1.00 16.23 C ANISOU 4054 CZ PHE B 88 2209 2179 1777 74 -96 -111 C ATOM 4055 N HIS B 89 43.760 -26.350 -23.340 1.00 13.57 N ANISOU 4055 N HIS B 89 1833 1640 1683 227 -24 95 N ATOM 4056 CA HIS B 89 42.887 -26.400 -22.143 1.00 14.74 C ANISOU 4056 CA HIS B 89 1851 1844 1907 177 52 75 C ATOM 4057 C HIS B 89 43.167 -27.664 -21.332 1.00 14.95 C ANISOU 4057 C HIS B 89 1828 1815 2037 91 18 122 C ATOM 4058 O HIS B 89 42.278 -28.322 -20.791 1.00 15.85 O ANISOU 4058 O HIS B 89 1988 1907 2126 223 130 217 O ATOM 4059 CB HIS B 89 41.416 -26.273 -22.532 1.00 15.56 C ANISOU 4059 CB HIS B 89 1862 1993 2056 78 26 -48 C ATOM 4060 CG HIS B 89 40.513 -25.776 -21.434 1.00 16.65 C ANISOU 4060 CG HIS B 89 2004 2191 2131 52 77 -96 C ATOM 4061 ND1 HIS B 89 39.645 -26.588 -20.747 1.00 18.49 N ANISOU 4061 ND1 HIS B 89 2358 2436 2231 23 148 46 N ATOM 4062 CD2 HIS B 89 40.310 -24.539 -20.937 1.00 15.48 C ANISOU 4062 CD2 HIS B 89 1835 1983 2062 -21 -52 -13 C ATOM 4063 CE1 HIS B 89 38.938 -25.887 -19.855 1.00 16.56 C ANISOU 4063 CE1 HIS B 89 1982 2127 2182 15 -34 -21 C ATOM 4064 NE2 HIS B 89 39.330 -24.626 -19.977 1.00 17.47 N ANISOU 4064 NE2 HIS B 89 2174 2273 2192 -30 37 -67 N ATOM 4065 N TYR B 90 44.458 -28.007 -21.199 1.00 14.64 N ANISOU 4065 N TYR B 90 1944 1721 1896 307 15 -42 N ATOM 4066 CA TYR B 90 44.791 -29.365 -20.712 1.00 15.73 C ANISOU 4066 CA TYR B 90 2163 1856 1958 249 -1 139 C ATOM 4067 C TYR B 90 44.797 -29.363 -19.191 1.00 14.69 C ANISOU 4067 C TYR B 90 1819 1826 1938 204 66 -33 C ATOM 4068 O TYR B 90 45.616 -28.674 -18.568 1.00 15.40 O ANISOU 4068 O TYR B 90 1897 1881 2073 210 69 -138 O ATOM 4069 CB TYR B 90 46.149 -29.780 -21.335 1.00 18.68 C ANISOU 4069 CB TYR B 90 2255 2502 2339 97 146 -4 C ATOM 4070 CG TYR B 90 46.435 -31.239 -21.005 1.00 23.80 C ANISOU 4070 CG TYR B 90 3225 2706 3109 311 51 41 C ATOM 4071 CD1 TYR B 90 47.517 -31.608 -20.236 1.00 27.46 C ANISOU 4071 CD1 TYR B 90 3522 3446 3465 183 -193 -5 C ATOM 4072 CD2 TYR B 90 45.574 -32.229 -21.434 1.00 26.92 C ANISOU 4072 CD2 TYR B 90 3477 3200 3550 3 -36 9 C ATOM 4073 CE1 TYR B 90 47.710 -32.971 -19.915 1.00 29.97 C ANISOU 4073 CE1 TYR B 90 3975 3454 3959 136 -121 71 C ATOM 4074 CE2 TYR B 90 45.792 -33.567 -21.143 1.00 29.67 C ANISOU 4074 CE2 TYR B 90 3967 3391 3914 136 -77 82 C ATOM 4075 CZ TYR B 90 46.854 -33.924 -20.371 1.00 30.79 C ANISOU 4075 CZ TYR B 90 3969 3723 4007 60 -151 11 C ATOM 4076 OH TYR B 90 47.065 -35.282 -20.065 1.00 33.04 O ANISOU 4076 OH TYR B 90 4433 3837 4282 157 -137 8 O ATOM 4077 N GLY B 91 43.848 -30.031 -18.546 1.00 13.27 N ANISOU 4077 N GLY B 91 1833 1547 1663 231 -44 4 N ATOM 4078 CA GLY B 91 43.702 -30.049 -17.097 1.00 13.42 C ANISOU 4078 CA GLY B 91 1855 1593 1652 176 -4 4 C ATOM 4079 C GLY B 91 43.008 -28.866 -16.457 1.00 13.44 C ANISOU 4079 C GLY B 91 1790 1695 1621 135 6 -13 C ATOM 4080 O GLY B 91 42.874 -28.755 -15.217 1.00 14.61 O ANISOU 4080 O GLY B 91 2041 1861 1648 163 62 2 O ATOM 4081 N LEU B 92 42.615 -27.867 -17.249 1.00 13.59 N ANISOU 4081 N LEU B 92 1810 1564 1791 103 -22 4 N ATOM 4082 CA LEU B 92 42.048 -26.644 -16.723 1.00 13.72 C ANISOU 4082 CA LEU B 92 1702 1590 1922 77 105 -5 C ATOM 4083 C LEU B 92 40.566 -26.785 -16.351 1.00 13.74 C ANISOU 4083 C LEU B 92 1660 1618 1944 -14 3 -55 C ATOM 4084 O LEU B 92 39.870 -27.610 -16.920 1.00 13.66 O ANISOU 4084 O LEU B 92 1488 1654 2048 133 -44 -273 O ATOM 4085 CB LEU B 92 42.132 -25.530 -17.807 1.00 15.19 C ANISOU 4085 CB LEU B 92 1899 1816 2056 -9 68 182 C ATOM 4086 CG LEU B 92 43.518 -25.180 -18.350 1.00 16.64 C ANISOU 4086 CG LEU B 92 2046 2049 2228 -64 78 268 C ATOM 4087 CD1 LEU B 92 43.494 -23.761 -18.971 1.00 16.50 C ANISOU 4087 CD1 LEU B 92 1985 1997 2288 -125 89 280 C ATOM 4088 CD2 LEU B 92 44.623 -25.296 -17.323 1.00 16.79 C ANISOU 4088 CD2 LEU B 92 2192 2174 2012 -197 14 70 C ATOM 4089 N THR B 93 40.125 -25.943 -15.423 1.00 13.57 N ANISOU 4089 N THR B 93 1613 1733 1811 106 16 -14 N ATOM 4090 CA THR B 93 38.695 -25.754 -15.178 1.00 13.90 C ANISOU 4090 CA THR B 93 1626 1778 1876 141 13 74 C ATOM 4091 C THR B 93 38.305 -24.446 -15.879 1.00 13.62 C ANISOU 4091 C THR B 93 1538 1648 1990 83 -16 0 C ATOM 4092 O THR B 93 39.137 -23.550 -16.142 1.00 12.76 O ANISOU 4092 O THR B 93 1533 1478 1839 212 38 -35 O ATOM 4093 CB THR B 93 38.405 -25.760 -13.672 1.00 14.88 C ANISOU 4093 CB THR B 93 1876 1877 1899 29 -8 -16 C ATOM 4094 OG1 THR B 93 36.976 -25.870 -13.410 1.00 16.11 O ANISOU 4094 OG1 THR B 93 1940 2127 2053 -50 46 147 O ATOM 4095 CG2 THR B 93 38.922 -24.506 -12.979 1.00 13.83 C ANISOU 4095 CG2 THR B 93 1807 1738 1711 73 -27 71 C ATOM 4096 N SER B 94 36.978 -24.291 -16.145 1.00 12.76 N ANISOU 4096 N SER B 94 1573 1493 1781 149 -181 -69 N ATOM 4097 CA SER B 94 36.574 -23.071 -16.862 1.00 12.69 C ANISOU 4097 CA SER B 94 1572 1509 1742 55 -124 -48 C ATOM 4098 C SER B 94 36.994 -21.800 -16.165 1.00 11.74 C ANISOU 4098 C SER B 94 1447 1516 1496 47 -42 8 C ATOM 4099 O SER B 94 37.394 -20.858 -16.899 1.00 11.50 O ANISOU 4099 O SER B 94 1585 1347 1437 104 -131 -6 O ATOM 4100 CB SER B 94 35.027 -22.995 -17.053 1.00 14.83 C ANISOU 4100 CB SER B 94 1597 1902 2137 26 -120 -97 C ATOM 4101 OG SER B 94 34.694 -24.086 -17.903 1.00 16.84 O ANISOU 4101 OG SER B 94 1924 2058 2416 -157 -226 -91 O ATOM 4102 N SER B 95 36.878 -21.760 -14.840 1.00 11.28 N ANISOU 4102 N SER B 95 1381 1465 1439 154 -103 -28 N ATOM 4103 CA SER B 95 37.268 -20.510 -14.180 1.00 11.58 C ANISOU 4103 CA SER B 95 1392 1455 1552 112 -55 -53 C ATOM 4104 C SER B 95 38.747 -20.228 -14.201 1.00 11.96 C ANISOU 4104 C SER B 95 1473 1463 1606 87 33 -32 C ATOM 4105 O SER B 95 39.134 -19.088 -13.914 1.00 11.71 O ANISOU 4105 O SER B 95 1617 1377 1456 41 -85 88 O ATOM 4106 CB SER B 95 36.759 -20.465 -12.720 1.00 13.23 C ANISOU 4106 CB SER B 95 1631 1761 1635 75 -2 2 C ATOM 4107 OG SER B 95 35.344 -20.279 -12.769 1.00 15.20 O ANISOU 4107 OG SER B 95 1633 1977 2164 10 275 -15 O ATOM 4108 N ASP B 96 39.651 -21.199 -14.471 1.00 11.40 N ANISOU 4108 N ASP B 96 1497 1411 1422 154 75 8 N ATOM 4109 CA ASP B 96 41.043 -20.817 -14.706 1.00 11.24 C ANISOU 4109 CA ASP B 96 1417 1374 1481 114 0 -21 C ATOM 4110 C ASP B 96 41.123 -19.831 -15.864 1.00 11.67 C ANISOU 4110 C ASP B 96 1504 1412 1517 92 -111 -12 C ATOM 4111 O ASP B 96 41.881 -18.869 -15.804 1.00 12.79 O ANISOU 4111 O ASP B 96 1672 1565 1625 -41 -89 185 O ATOM 4112 CB ASP B 96 41.880 -22.045 -15.160 1.00 11.74 C ANISOU 4112 CB ASP B 96 1331 1376 1754 144 -27 -25 C ATOM 4113 CG ASP B 96 42.104 -22.978 -14.004 1.00 12.12 C ANISOU 4113 CG ASP B 96 1339 1565 1700 39 49 10 C ATOM 4114 OD1 ASP B 96 42.267 -22.568 -12.820 1.00 13.43 O ANISOU 4114 OD1 ASP B 96 1468 1805 1828 108 -7 -114 O ATOM 4115 OD2 ASP B 96 42.152 -24.196 -14.262 1.00 13.58 O ANISOU 4115 OD2 ASP B 96 1679 1531 1950 140 135 94 O ATOM 4116 N VAL B 97 40.346 -20.070 -16.927 1.00 10.50 N ANISOU 4116 N VAL B 97 1367 1365 1259 242 5 -141 N ATOM 4117 CA VAL B 97 40.337 -19.100 -18.037 1.00 11.38 C ANISOU 4117 CA VAL B 97 1533 1411 1380 132 -1 -66 C ATOM 4118 C VAL B 97 39.511 -17.870 -17.694 1.00 11.45 C ANISOU 4118 C VAL B 97 1518 1362 1470 43 -1 -55 C ATOM 4119 O VAL B 97 39.950 -16.741 -17.950 1.00 11.59 O ANISOU 4119 O VAL B 97 1707 1323 1372 50 -119 6 O ATOM 4120 CB VAL B 97 39.711 -19.816 -19.274 1.00 12.64 C ANISOU 4120 CB VAL B 97 1790 1555 1458 86 -70 -104 C ATOM 4121 CG1 VAL B 97 39.562 -18.881 -20.460 1.00 14.88 C ANISOU 4121 CG1 VAL B 97 2247 1830 1576 101 -88 -3 C ATOM 4122 CG2 VAL B 97 40.621 -20.989 -19.681 1.00 14.01 C ANISOU 4122 CG2 VAL B 97 1867 1708 1747 131 13 -181 C ATOM 4123 N LEU B 98 38.297 -18.034 -17.153 1.00 12.31 N ANISOU 4123 N LEU B 98 1515 1576 1584 41 21 -58 N ATOM 4124 CA LEU B 98 37.442 -16.875 -16.891 1.00 12.56 C ANISOU 4124 CA LEU B 98 1444 1631 1698 100 27 12 C ATOM 4125 C LEU B 98 38.080 -15.896 -15.931 1.00 12.47 C ANISOU 4125 C LEU B 98 1371 1765 1601 56 73 9 C ATOM 4126 O LEU B 98 38.064 -14.670 -16.185 1.00 13.63 O ANISOU 4126 O LEU B 98 1584 1849 1744 198 82 69 O ATOM 4127 CB LEU B 98 36.108 -17.318 -16.248 1.00 14.06 C ANISOU 4127 CB LEU B 98 1647 1850 1844 -12 25 131 C ATOM 4128 CG LEU B 98 35.216 -18.193 -17.129 1.00 15.42 C ANISOU 4128 CG LEU B 98 1951 1923 1986 -18 -44 6 C ATOM 4129 CD1 LEU B 98 34.132 -18.855 -16.274 1.00 16.30 C ANISOU 4129 CD1 LEU B 98 2072 2063 2059 5 95 -21 C ATOM 4130 CD2 LEU B 98 34.562 -17.240 -18.133 1.00 17.51 C ANISOU 4130 CD2 LEU B 98 2311 2258 2085 66 -133 147 C ATOM 4131 N ASP B 99 38.580 -16.393 -14.786 1.00 12.16 N ANISOU 4131 N ASP B 99 1264 1779 1578 106 63 -23 N ATOM 4132 CA ASP B 99 39.099 -15.467 -13.760 1.00 11.99 C ANISOU 4132 CA ASP B 99 1386 1653 1518 64 57 32 C ATOM 4133 C ASP B 99 40.433 -14.897 -14.171 1.00 11.31 C ANISOU 4133 C ASP B 99 1398 1517 1384 123 70 -35 C ATOM 4134 O ASP B 99 40.722 -13.723 -13.898 1.00 12.09 O ANISOU 4134 O ASP B 99 1567 1657 1369 126 177 -268 O ATOM 4135 CB ASP B 99 39.262 -16.146 -12.372 1.00 12.39 C ANISOU 4135 CB ASP B 99 1557 1654 1498 122 -2 28 C ATOM 4136 CG ASP B 99 37.958 -16.394 -11.665 1.00 14.12 C ANISOU 4136 CG ASP B 99 1768 1855 1742 49 88 82 C ATOM 4137 OD1 ASP B 99 36.871 -15.977 -12.204 1.00 16.35 O ANISOU 4137 OD1 ASP B 99 1951 2145 2115 282 13 22 O ATOM 4138 OD2 ASP B 99 37.923 -16.978 -10.563 1.00 13.78 O ANISOU 4138 OD2 ASP B 99 1690 1815 1730 118 65 109 O ATOM 4139 N THR B 100 41.290 -15.697 -14.827 1.00 9.99 N ANISOU 4139 N THR B 100 1225 1314 1258 107 26 -112 N ATOM 4140 CA THR B 100 42.566 -15.120 -15.279 1.00 10.01 C ANISOU 4140 CA THR B 100 1226 1328 1248 99 21 -66 C ATOM 4141 C THR B 100 42.314 -14.064 -16.339 1.00 10.24 C ANISOU 4141 C THR B 100 1188 1268 1434 96 -13 -74 C ATOM 4142 O THR B 100 42.933 -13.005 -16.346 1.00 10.03 O ANISOU 4142 O THR B 100 1083 1190 1540 238 94 -36 O ATOM 4143 CB THR B 100 43.549 -16.224 -15.760 1.00 9.81 C ANISOU 4143 CB THR B 100 1138 1218 1370 56 19 22 C ATOM 4144 OG1 THR B 100 43.733 -17.146 -14.646 1.00 10.76 O ANISOU 4144 OG1 THR B 100 1508 1290 1290 198 -61 -65 O ATOM 4145 CG2 THR B 100 44.868 -15.593 -16.207 1.00 9.57 C ANISOU 4145 CG2 THR B 100 1137 1265 1236 138 95 118 C ATOM 4146 N ALA B 101 41.355 -14.292 -17.242 1.00 10.07 N ANISOU 4146 N ALA B 101 1248 1418 1159 203 -17 -14 N ATOM 4147 CA ALA B 101 41.025 -13.258 -18.233 1.00 10.37 C ANISOU 4147 CA ALA B 101 1392 1210 1339 224 -108 -112 C ATOM 4148 C ALA B 101 40.390 -12.021 -17.564 1.00 10.68 C ANISOU 4148 C ALA B 101 1434 1197 1425 112 -70 -115 C ATOM 4149 O ALA B 101 40.662 -10.927 -18.050 1.00 10.56 O ANISOU 4149 O ALA B 101 1352 1165 1497 128 -65 -195 O ATOM 4150 CB ALA B 101 40.078 -13.897 -19.249 1.00 10.30 C ANISOU 4150 CB ALA B 101 1387 1140 1385 23 -91 3 C ATOM 4151 N ASN B 102 39.592 -12.215 -16.536 1.00 10.61 N ANISOU 4151 N ASN B 102 1365 1391 1276 181 -110 -198 N ATOM 4152 CA ASN B 102 39.092 -11.007 -15.837 1.00 12.29 C ANISOU 4152 CA ASN B 102 1667 1394 1607 129 -101 -230 C ATOM 4153 C ASN B 102 40.192 -10.281 -15.080 1.00 11.43 C ANISOU 4153 C ASN B 102 1490 1314 1538 105 -30 -105 C ATOM 4154 O ASN B 102 40.154 -9.036 -14.988 1.00 11.17 O ANISOU 4154 O ASN B 102 1433 1222 1588 153 30 -21 O ATOM 4155 CB ASN B 102 37.888 -11.357 -14.981 1.00 15.38 C ANISOU 4155 CB ASN B 102 1973 1816 2053 54 139 -224 C ATOM 4156 CG ASN B 102 36.635 -11.224 -15.864 1.00 19.05 C ANISOU 4156 CG ASN B 102 2154 2461 2622 47 -38 -131 C ATOM 4157 OD1 ASN B 102 36.483 -10.436 -16.838 1.00 21.92 O ANISOU 4157 OD1 ASN B 102 2657 2861 2810 180 -45 -38 O ATOM 4158 ND2 ASN B 102 35.703 -12.064 -15.529 1.00 19.10 N ANISOU 4158 ND2 ASN B 102 2204 2326 2728 90 179 -230 N ATOM 4159 N SER B 103 41.207 -10.996 -14.561 1.00 11.26 N ANISOU 4159 N SER B 103 1416 1420 1440 132 -69 -157 N ATOM 4160 CA SER B 103 42.348 -10.271 -13.987 1.00 11.36 C ANISOU 4160 CA SER B 103 1340 1482 1493 91 12 -86 C ATOM 4161 C SER B 103 43.048 -9.469 -15.073 1.00 11.32 C ANISOU 4161 C SER B 103 1501 1396 1404 178 -61 -36 C ATOM 4162 O SER B 103 43.353 -8.301 -14.845 1.00 11.94 O ANISOU 4162 O SER B 103 1494 1537 1507 45 -58 -77 O ATOM 4163 CB SER B 103 43.341 -11.298 -13.377 1.00 14.23 C ANISOU 4163 CB SER B 103 2067 1663 1679 227 -164 109 C ATOM 4164 OG SER B 103 42.559 -11.839 -12.248 1.00 18.90 O ANISOU 4164 OG SER B 103 2176 2566 2437 -25 178 117 O ATOM 4165 N LEU B 104 43.312 -10.070 -16.255 1.00 10.88 N ANISOU 4165 N LEU B 104 1423 1460 1251 69 -2 -65 N ATOM 4166 CA LEU B 104 43.862 -9.285 -17.352 1.00 11.03 C ANISOU 4166 CA LEU B 104 1526 1245 1421 108 -44 1 C ATOM 4167 C LEU B 104 43.063 -8.014 -17.655 1.00 10.76 C ANISOU 4167 C LEU B 104 1297 1288 1505 132 12 -72 C ATOM 4168 O LEU B 104 43.650 -6.922 -17.877 1.00 10.14 O ANISOU 4168 O LEU B 104 1262 1216 1375 274 -18 177 O ATOM 4169 CB LEU B 104 43.887 -10.097 -18.662 1.00 12.61 C ANISOU 4169 CB LEU B 104 1663 1564 1566 193 29 -153 C ATOM 4170 CG LEU B 104 44.925 -11.234 -18.693 1.00 13.76 C ANISOU 4170 CG LEU B 104 1639 1692 1897 182 -50 -191 C ATOM 4171 CD1 LEU B 104 44.734 -12.031 -19.991 1.00 13.66 C ANISOU 4171 CD1 LEU B 104 1747 1684 1759 96 123 -162 C ATOM 4172 CD2 LEU B 104 46.343 -10.652 -18.579 1.00 14.90 C ANISOU 4172 CD2 LEU B 104 1710 1871 2081 27 -16 -137 C ATOM 4173 N ALA B 105 41.754 -8.202 -17.779 1.00 10.54 N ANISOU 4173 N ALA B 105 1282 1272 1453 201 -105 -123 N ATOM 4174 CA ALA B 105 40.879 -7.037 -18.032 1.00 11.02 C ANISOU 4174 CA ALA B 105 1265 1228 1694 175 -49 -155 C ATOM 4175 C ALA B 105 40.892 -6.013 -16.909 1.00 10.79 C ANISOU 4175 C ALA B 105 1279 1403 1416 24 -27 -66 C ATOM 4176 O ALA B 105 40.927 -4.815 -17.231 1.00 11.16 O ANISOU 4176 O ALA B 105 1325 1326 1588 175 77 -224 O ATOM 4177 CB ALA B 105 39.432 -7.554 -18.187 1.00 10.63 C ANISOU 4177 CB ALA B 105 1313 1172 1553 130 -136 -110 C ATOM 4178 N LEU B 106 40.836 -6.382 -15.624 1.00 10.33 N ANISOU 4178 N LEU B 106 1126 1401 1399 132 -56 -101 N ATOM 4179 CA LEU B 106 40.805 -5.372 -14.577 1.00 10.35 C ANISOU 4179 CA LEU B 106 1256 1426 1250 2 33 -18 C ATOM 4180 C LEU B 106 42.148 -4.690 -14.422 1.00 10.57 C ANISOU 4180 C LEU B 106 1210 1370 1437 67 50 -13 C ATOM 4181 O LEU B 106 42.191 -3.491 -14.095 1.00 10.60 O ANISOU 4181 O LEU B 106 1223 1352 1454 -46 29 -157 O ATOM 4182 CB LEU B 106 40.338 -6.005 -13.240 1.00 10.09 C ANISOU 4182 CB LEU B 106 1271 1284 1278 107 112 100 C ATOM 4183 CG LEU B 106 38.880 -6.509 -13.330 1.00 11.26 C ANISOU 4183 CG LEU B 106 1356 1482 1439 90 72 185 C ATOM 4184 CD1 LEU B 106 38.494 -7.184 -12.017 1.00 12.34 C ANISOU 4184 CD1 LEU B 106 1480 1668 1540 35 148 281 C ATOM 4185 CD2 LEU B 106 37.878 -5.351 -13.563 1.00 12.56 C ANISOU 4185 CD2 LEU B 106 1424 1636 1712 182 100 61 C ATOM 4186 N VAL B 107 43.237 -5.426 -14.688 1.00 10.28 N ANISOU 4186 N VAL B 107 1210 1253 1441 163 -24 -15 N ATOM 4187 CA VAL B 107 44.562 -4.812 -14.732 1.00 10.27 C ANISOU 4187 CA VAL B 107 1145 1217 1541 181 63 87 C ATOM 4188 C VAL B 107 44.622 -3.788 -15.870 1.00 10.54 C ANISOU 4188 C VAL B 107 1241 1278 1484 106 61 12 C ATOM 4189 O VAL B 107 45.078 -2.655 -15.682 1.00 10.64 O ANISOU 4189 O VAL B 107 1185 1241 1616 119 117 49 O ATOM 4190 CB VAL B 107 45.703 -5.876 -14.924 1.00 9.66 C ANISOU 4190 CB VAL B 107 1057 1256 1358 167 100 162 C ATOM 4191 CG1 VAL B 107 47.024 -5.160 -15.135 1.00 11.41 C ANISOU 4191 CG1 VAL B 107 1247 1516 1573 17 154 -10 C ATOM 4192 CG2 VAL B 107 45.796 -6.691 -13.586 1.00 8.95 C ANISOU 4192 CG2 VAL B 107 983 1204 1212 227 24 86 C ATOM 4193 N GLU B 108 44.195 -4.147 -17.072 1.00 10.69 N ANISOU 4193 N GLU B 108 1169 1515 1376 203 62 15 N ATOM 4194 CA GLU B 108 44.256 -3.217 -18.195 1.00 12.74 C ANISOU 4194 CA GLU B 108 1577 1499 1763 202 154 154 C ATOM 4195 C GLU B 108 43.347 -2.006 -17.968 1.00 11.66 C ANISOU 4195 C GLU B 108 1357 1440 1635 54 61 9 C ATOM 4196 O GLU B 108 43.747 -0.873 -18.235 1.00 11.92 O ANISOU 4196 O GLU B 108 1420 1381 1729 130 88 18 O ATOM 4197 CB GLU B 108 43.855 -3.915 -19.498 1.00 17.15 C ANISOU 4197 CB GLU B 108 2218 2193 2105 76 -5 -161 C ATOM 4198 CG GLU B 108 44.033 -3.022 -20.741 1.00 23.32 C ANISOU 4198 CG GLU B 108 3308 2884 2668 119 39 217 C ATOM 4199 CD GLU B 108 45.371 -2.341 -20.822 1.00 29.18 C ANISOU 4199 CD GLU B 108 3606 3729 3751 -108 136 96 C ATOM 4200 OE1 GLU B 108 46.440 -2.941 -20.518 1.00 31.19 O ANISOU 4200 OE1 GLU B 108 4003 3941 3908 198 73 46 O ATOM 4201 OE2 GLU B 108 45.454 -1.134 -21.160 1.00 32.69 O ANISOU 4201 OE2 GLU B 108 4120 3794 4505 46 130 237 O ATOM 4202 N ALA B 109 42.143 -2.256 -17.483 1.00 10.75 N ANISOU 4202 N ALA B 109 1260 1345 1481 238 151 -80 N ATOM 4203 CA ALA B 109 41.219 -1.125 -17.212 1.00 9.82 C ANISOU 4203 CA ALA B 109 1065 1176 1492 88 195 -71 C ATOM 4204 C ALA B 109 41.843 -0.233 -16.157 1.00 10.39 C ANISOU 4204 C ALA B 109 1097 1390 1462 52 5 -4 C ATOM 4205 O ALA B 109 41.719 1.022 -16.201 1.00 10.59 O ANISOU 4205 O ALA B 109 1076 1441 1508 81 9 41 O ATOM 4206 CB ALA B 109 39.887 -1.666 -16.627 1.00 9.58 C ANISOU 4206 CB ALA B 109 1108 1178 1352 -4 191 7 C ATOM 4207 N GLY B 110 42.430 -0.879 -15.116 1.00 9.95 N ANISOU 4207 N GLY B 110 1183 1325 1273 58 85 -64 N ATOM 4208 CA GLY B 110 43.123 -0.122 -14.078 1.00 10.33 C ANISOU 4208 CA GLY B 110 1287 1262 1375 28 2 -51 C ATOM 4209 C GLY B 110 44.231 0.760 -14.603 1.00 11.22 C ANISOU 4209 C GLY B 110 1386 1366 1512 46 10 -8 C ATOM 4210 O GLY B 110 44.349 1.932 -14.151 1.00 11.68 O ANISOU 4210 O GLY B 110 1433 1331 1675 -13 -162 -21 O ATOM 4211 N LYS B 111 45.046 0.258 -15.519 1.00 11.75 N ANISOU 4211 N LYS B 111 1396 1554 1514 200 35 64 N ATOM 4212 CA LYS B 111 46.090 1.100 -16.109 1.00 12.57 C ANISOU 4212 CA LYS B 111 1564 1490 1723 85 66 29 C ATOM 4213 C LYS B 111 45.524 2.227 -16.941 1.00 11.81 C ANISOU 4213 C LYS B 111 1502 1405 1581 73 98 -76 C ATOM 4214 O LYS B 111 46.111 3.331 -16.936 1.00 12.65 O ANISOU 4214 O LYS B 111 1552 1464 1791 -25 216 18 O ATOM 4215 CB LYS B 111 47.032 0.216 -16.981 1.00 14.72 C ANISOU 4215 CB LYS B 111 1806 1723 2065 174 192 -136 C ATOM 4216 CG LYS B 111 47.825 -0.779 -16.086 1.00 17.91 C ANISOU 4216 CG LYS B 111 2219 2168 2417 201 -77 42 C ATOM 4217 CD LYS B 111 48.564 -1.709 -17.088 1.00 20.66 C ANISOU 4217 CD LYS B 111 2572 2503 2774 241 85 -129 C ATOM 4218 CE LYS B 111 49.454 -2.735 -16.372 1.00 23.22 C ANISOU 4218 CE LYS B 111 2980 2706 3136 222 -44 110 C ATOM 4219 NZ LYS B 111 50.091 -3.529 -17.503 1.00 26.02 N ANISOU 4219 NZ LYS B 111 3328 3106 3454 253 171 11 N ATOM 4220 N ILE B 112 44.436 2.014 -17.639 1.00 11.71 N ANISOU 4220 N ILE B 112 1481 1392 1577 63 58 -51 N ATOM 4221 CA ILE B 112 43.795 3.086 -18.433 1.00 12.47 C ANISOU 4221 CA ILE B 112 1677 1478 1581 37 -8 -60 C ATOM 4222 C ILE B 112 43.279 4.147 -17.461 1.00 12.12 C ANISOU 4222 C ILE B 112 1582 1452 1571 48 136 30 C ATOM 4223 O ILE B 112 43.507 5.363 -17.639 1.00 12.05 O ANISOU 4223 O ILE B 112 1679 1430 1472 -92 48 -137 O ATOM 4224 CB ILE B 112 42.667 2.522 -19.303 1.00 12.63 C ANISOU 4224 CB ILE B 112 1607 1510 1682 75 -62 10 C ATOM 4225 CG1 ILE B 112 43.261 1.680 -20.446 1.00 13.44 C ANISOU 4225 CG1 ILE B 112 1796 1548 1763 -10 -33 -67 C ATOM 4226 CG2 ILE B 112 41.816 3.687 -19.858 1.00 12.54 C ANISOU 4226 CG2 ILE B 112 1639 1472 1653 18 -83 74 C ATOM 4227 CD1 ILE B 112 42.184 0.887 -21.191 1.00 14.35 C ANISOU 4227 CD1 ILE B 112 1790 1789 1872 2 -62 -162 C ATOM 4228 N LEU B 113 42.589 3.685 -16.430 1.00 11.17 N ANISOU 4228 N LEU B 113 1434 1459 1350 71 43 -19 N ATOM 4229 CA LEU B 113 42.113 4.616 -15.387 1.00 10.85 C ANISOU 4229 CA LEU B 113 1404 1184 1534 -26 82 37 C ATOM 4230 C LEU B 113 43.249 5.426 -14.766 1.00 11.45 C ANISOU 4230 C LEU B 113 1276 1427 1646 28 4 67 C ATOM 4231 O LEU B 113 43.139 6.612 -14.440 1.00 12.15 O ANISOU 4231 O LEU B 113 1397 1445 1773 -32 124 27 O ATOM 4232 CB LEU B 113 41.423 3.798 -14.314 1.00 10.83 C ANISOU 4232 CB LEU B 113 1314 1320 1481 155 206 54 C ATOM 4233 CG LEU B 113 39.953 3.539 -14.225 1.00 12.27 C ANISOU 4233 CG LEU B 113 1425 1384 1851 -26 -67 262 C ATOM 4234 CD1 LEU B 113 38.941 4.285 -15.062 1.00 11.76 C ANISOU 4234 CD1 LEU B 113 1457 1580 1433 -82 -145 196 C ATOM 4235 CD2 LEU B 113 39.536 2.176 -13.744 1.00 10.42 C ANISOU 4235 CD2 LEU B 113 1210 953 1795 82 -77 -60 C ATOM 4236 N LEU B 114 44.353 4.749 -14.420 1.00 11.08 N ANISOU 4236 N LEU B 114 1296 1323 1593 93 -18 77 N ATOM 4237 CA LEU B 114 45.478 5.380 -13.745 1.00 11.23 C ANISOU 4237 CA LEU B 114 1192 1400 1674 140 -25 124 C ATOM 4238 C LEU B 114 46.114 6.453 -14.609 1.00 11.97 C ANISOU 4238 C LEU B 114 1441 1434 1674 56 -6 65 C ATOM 4239 O LEU B 114 46.448 7.549 -14.121 1.00 12.65 O ANISOU 4239 O LEU B 114 1392 1457 1956 113 -18 -82 O ATOM 4240 CB LEU B 114 46.525 4.266 -13.432 1.00 11.10 C ANISOU 4240 CB LEU B 114 1235 1336 1647 225 -67 50 C ATOM 4241 CG LEU B 114 47.766 4.773 -12.675 1.00 12.27 C ANISOU 4241 CG LEU B 114 1379 1639 1645 193 -85 -81 C ATOM 4242 CD1 LEU B 114 47.423 5.329 -11.299 1.00 12.43 C ANISOU 4242 CD1 LEU B 114 1315 1790 1619 118 -171 -111 C ATOM 4243 CD2 LEU B 114 48.790 3.616 -12.528 1.00 13.45 C ANISOU 4243 CD2 LEU B 114 1513 1740 1859 250 -108 39 C ATOM 4244 N GLU B 115 46.317 6.160 -15.887 1.00 11.90 N ANISOU 4244 N GLU B 115 1554 1328 1639 46 28 -36 N ATOM 4245 CA GLU B 115 46.875 7.166 -16.797 1.00 13.35 C ANISOU 4245 CA GLU B 115 1698 1582 1793 18 100 65 C ATOM 4246 C GLU B 115 45.955 8.397 -16.865 1.00 13.45 C ANISOU 4246 C GLU B 115 1676 1615 1820 8 17 -3 C ATOM 4247 O GLU B 115 46.424 9.530 -16.876 1.00 13.56 O ANISOU 4247 O GLU B 115 1690 1598 1864 32 107 -2 O ATOM 4248 CB GLU B 115 47.081 6.614 -18.192 1.00 16.22 C ANISOU 4248 CB GLU B 115 2124 2102 1935 -3 68 -158 C ATOM 4249 N SER B 116 44.647 8.169 -16.915 1.00 13.18 N ANISOU 4249 N SER B 116 1607 1728 1672 79 -41 55 N ATOM 4250 CA SER B 116 43.723 9.303 -17.007 1.00 13.94 C ANISOU 4250 CA SER B 116 1776 1675 1847 97 -65 -143 C ATOM 4251 C SER B 116 43.700 10.035 -15.680 1.00 11.95 C ANISOU 4251 C SER B 116 1408 1574 1559 73 14 125 C ATOM 4252 O SER B 116 43.596 11.267 -15.657 1.00 11.18 O ANISOU 4252 O SER B 116 1415 1437 1396 -97 107 -11 O ATOM 4253 CB SER B 116 42.341 8.813 -17.519 1.00 16.74 C ANISOU 4253 CB SER B 116 1835 2093 2432 -3 -120 36 C ATOM 4254 OG SER B 116 41.723 8.140 -16.444 1.00 21.55 O ANISOU 4254 OG SER B 116 2802 2633 2753 -38 119 87 O ATOM 4255 N LEU B 117 43.867 9.367 -14.549 1.00 10.26 N ANISOU 4255 N LEU B 117 983 1471 1443 -32 79 108 N ATOM 4256 CA LEU B 117 43.864 10.041 -13.259 1.00 11.14 C ANISOU 4256 CA LEU B 117 1274 1439 1520 -45 82 61 C ATOM 4257 C LEU B 117 45.137 10.858 -13.091 1.00 11.34 C ANISOU 4257 C LEU B 117 1296 1389 1625 12 55 19 C ATOM 4258 O LEU B 117 45.113 11.955 -12.534 1.00 11.60 O ANISOU 4258 O LEU B 117 1298 1502 1606 49 122 -29 O ATOM 4259 CB LEU B 117 43.751 8.979 -12.138 1.00 13.45 C ANISOU 4259 CB LEU B 117 1819 1580 1709 156 75 203 C ATOM 4260 CG LEU B 117 43.441 9.499 -10.736 1.00 16.38 C ANISOU 4260 CG LEU B 117 2222 2091 1910 192 115 102 C ATOM 4261 CD1 LEU B 117 42.142 10.335 -10.730 1.00 16.36 C ANISOU 4261 CD1 LEU B 117 2244 2070 1901 234 180 -18 C ATOM 4262 CD2 LEU B 117 43.289 8.296 -9.791 1.00 17.04 C ANISOU 4262 CD2 LEU B 117 2271 2193 2009 122 73 208 C ATOM 4263 N LYS B 118 46.267 10.298 -13.534 1.00 10.72 N ANISOU 4263 N LYS B 118 1121 1447 1504 -135 181 -22 N ATOM 4264 CA LYS B 118 47.496 11.144 -13.484 1.00 11.58 C ANISOU 4264 CA LYS B 118 1227 1493 1679 -99 58 -11 C ATOM 4265 C LYS B 118 47.342 12.379 -14.345 1.00 12.13 C ANISOU 4265 C LYS B 118 1361 1565 1681 4 70 -19 C ATOM 4266 O LYS B 118 47.840 13.447 -13.930 1.00 12.69 O ANISOU 4266 O LYS B 118 1606 1578 1639 24 38 -131 O ATOM 4267 CB LYS B 118 48.701 10.317 -13.917 1.00 12.14 C ANISOU 4267 CB LYS B 118 1336 1541 1735 19 44 -51 C ATOM 4268 CG LYS B 118 49.096 9.242 -12.880 1.00 14.37 C ANISOU 4268 CG LYS B 118 1713 1720 2029 54 -64 104 C ATOM 4269 CD LYS B 118 50.199 8.369 -13.548 1.00 16.90 C ANISOU 4269 CD LYS B 118 2052 2090 2278 173 181 -20 C ATOM 4270 CE LYS B 118 50.674 7.307 -12.546 1.00 20.27 C ANISOU 4270 CE LYS B 118 2522 2550 2630 228 54 189 C ATOM 4271 NZ LYS B 118 51.788 6.502 -13.197 1.00 22.48 N ANISOU 4271 NZ LYS B 118 2622 2810 3110 351 112 252 N ATOM 4272 N GLU B 119 46.771 12.275 -15.554 1.00 12.26 N ANISOU 4272 N GLU B 119 1391 1679 1589 -56 135 -88 N ATOM 4273 CA GLU B 119 46.475 13.479 -16.322 1.00 13.82 C ANISOU 4273 CA GLU B 119 1658 1759 1834 48 161 23 C ATOM 4274 C GLU B 119 45.580 14.472 -15.601 1.00 12.25 C ANISOU 4274 C GLU B 119 1535 1617 1504 -154 90 1 C ATOM 4275 O GLU B 119 45.815 15.703 -15.677 1.00 11.76 O ANISOU 4275 O GLU B 119 1442 1521 1506 -25 244 48 O ATOM 4276 CB GLU B 119 45.892 13.146 -17.711 1.00 18.24 C ANISOU 4276 CB GLU B 119 2236 2493 2201 -233 -99 -124 C ATOM 4277 CG GLU B 119 46.914 12.335 -18.527 1.00 25.11 C ANISOU 4277 CG GLU B 119 3113 3164 3264 191 278 -186 C ATOM 4278 CD GLU B 119 46.415 11.964 -19.919 1.00 31.13 C ANISOU 4278 CD GLU B 119 4096 4164 3568 56 -81 -170 C ATOM 4279 OE1 GLU B 119 45.502 12.662 -20.432 1.00 33.37 O ANISOU 4279 OE1 GLU B 119 4114 4508 4058 186 -53 -77 O ATOM 4280 OE2 GLU B 119 46.938 10.974 -20.525 1.00 33.77 O ANISOU 4280 OE2 GLU B 119 4493 4270 4067 150 91 -234 O ATOM 4281 N PHE B 120 44.529 13.983 -14.930 1.00 11.39 N ANISOU 4281 N PHE B 120 1320 1514 1493 -43 93 7 N ATOM 4282 CA PHE B 120 43.701 14.837 -14.095 1.00 10.85 C ANISOU 4282 CA PHE B 120 1312 1370 1440 -156 140 -40 C ATOM 4283 C PHE B 120 44.519 15.539 -13.024 1.00 11.13 C ANISOU 4283 C PHE B 120 1410 1376 1443 -54 40 21 C ATOM 4284 O PHE B 120 44.364 16.758 -12.799 1.00 11.59 O ANISOU 4284 O PHE B 120 1501 1323 1581 -74 139 17 O ATOM 4285 CB PHE B 120 42.553 14.018 -13.452 1.00 9.85 C ANISOU 4285 CB PHE B 120 1209 1202 1331 -96 74 43 C ATOM 4286 CG PHE B 120 41.446 14.811 -12.802 1.00 10.84 C ANISOU 4286 CG PHE B 120 1352 1439 1327 -48 60 -18 C ATOM 4287 CD1 PHE B 120 41.103 16.090 -13.205 1.00 11.67 C ANISOU 4287 CD1 PHE B 120 1377 1561 1495 105 -59 -78 C ATOM 4288 CD2 PHE B 120 40.710 14.217 -11.780 1.00 11.48 C ANISOU 4288 CD2 PHE B 120 1302 1570 1490 -73 78 -30 C ATOM 4289 CE1 PHE B 120 40.089 16.804 -12.598 1.00 11.28 C ANISOU 4289 CE1 PHE B 120 1374 1694 1219 16 -44 -107 C ATOM 4290 CE2 PHE B 120 39.670 14.899 -11.158 1.00 12.27 C ANISOU 4290 CE2 PHE B 120 1463 1523 1675 -6 107 -98 C ATOM 4291 CZ PHE B 120 39.346 16.189 -11.597 1.00 11.95 C ANISOU 4291 CZ PHE B 120 1465 1629 1446 -82 -79 35 C ATOM 4292 N CYS B 121 45.412 14.839 -12.330 1.00 10.80 N ANISOU 4292 N CYS B 121 1239 1422 1442 -126 121 59 N ATOM 4293 CA CYS B 121 46.264 15.488 -11.329 1.00 11.56 C ANISOU 4293 CA CYS B 121 1410 1509 1475 -128 -14 94 C ATOM 4294 C CYS B 121 47.119 16.583 -11.955 1.00 11.82 C ANISOU 4294 C CYS B 121 1553 1384 1556 -68 61 87 C ATOM 4295 O CYS B 121 47.295 17.641 -11.312 1.00 11.25 O ANISOU 4295 O CYS B 121 1368 1562 1344 -166 83 51 O ATOM 4296 CB CYS B 121 47.206 14.433 -10.709 1.00 12.05 C ANISOU 4296 CB CYS B 121 1455 1531 1591 -35 41 172 C ATOM 4297 SG CYS B 121 46.341 13.323 -9.553 1.00 12.90 S ANISOU 4297 SG CYS B 121 1598 1604 1701 -205 9 195 S ATOM 4298 N ASP B 122 47.644 16.366 -13.145 1.00 12.31 N ANISOU 4298 N ASP B 122 1608 1498 1569 15 81 40 N ATOM 4299 CA ASP B 122 48.465 17.368 -13.823 1.00 13.73 C ANISOU 4299 CA ASP B 122 1742 1558 1916 -65 64 110 C ATOM 4300 C ASP B 122 47.618 18.612 -14.086 1.00 13.07 C ANISOU 4300 C ASP B 122 1592 1635 1740 -27 50 2 C ATOM 4301 O ASP B 122 48.118 19.736 -13.896 1.00 14.14 O ANISOU 4301 O ASP B 122 1653 1769 1950 -160 102 21 O ATOM 4302 CB ASP B 122 49.064 16.895 -15.147 1.00 16.21 C ANISOU 4302 CB ASP B 122 2048 2054 2058 -72 140 9 C ATOM 4303 CG ASP B 122 50.083 15.784 -15.026 1.00 19.76 C ANISOU 4303 CG ASP B 122 2445 2428 2636 137 62 33 C ATOM 4304 OD1 ASP B 122 50.678 15.548 -13.940 1.00 20.36 O ANISOU 4304 OD1 ASP B 122 2362 2604 2769 153 -6 39 O ATOM 4305 OD2 ASP B 122 50.284 15.124 -16.079 1.00 21.84 O ANISOU 4305 OD2 ASP B 122 2758 2710 2831 67 243 -86 O ATOM 4306 N VAL B 123 46.378 18.459 -14.528 1.00 11.80 N ANISOU 4306 N VAL B 123 1511 1426 1545 -15 90 -3 N ATOM 4307 CA VAL B 123 45.470 19.587 -14.754 1.00 12.20 C ANISOU 4307 CA VAL B 123 1593 1481 1563 32 49 -29 C ATOM 4308 C VAL B 123 45.148 20.301 -13.444 1.00 11.59 C ANISOU 4308 C VAL B 123 1451 1472 1480 -64 36 35 C ATOM 4309 O VAL B 123 45.183 21.548 -13.373 1.00 12.29 O ANISOU 4309 O VAL B 123 1695 1486 1489 65 157 -81 O ATOM 4310 CB VAL B 123 44.197 19.103 -15.479 1.00 12.44 C ANISOU 4310 CB VAL B 123 1647 1565 1512 45 -7 -16 C ATOM 4311 CG1 VAL B 123 43.062 20.128 -15.351 1.00 13.81 C ANISOU 4311 CG1 VAL B 123 1722 1710 1815 58 -9 -126 C ATOM 4312 CG2 VAL B 123 44.478 18.826 -16.982 1.00 13.94 C ANISOU 4312 CG2 VAL B 123 1969 1669 1658 -50 105 -82 C ATOM 4313 N LEU B 124 44.815 19.582 -12.371 1.00 11.02 N ANISOU 4313 N LEU B 124 1369 1470 1349 -50 -72 4 N ATOM 4314 CA LEU B 124 44.572 20.195 -11.072 1.00 10.74 C ANISOU 4314 CA LEU B 124 1396 1316 1370 -181 20 41 C ATOM 4315 C LEU B 124 45.810 20.931 -10.555 1.00 11.21 C ANISOU 4315 C LEU B 124 1376 1392 1490 -79 -56 -33 C ATOM 4316 O LEU B 124 45.642 22.017 -9.964 1.00 11.11 O ANISOU 4316 O LEU B 124 1345 1413 1462 -266 -18 -165 O ATOM 4317 CB LEU B 124 44.131 19.124 -10.039 1.00 9.52 C ANISOU 4317 CB LEU B 124 1282 1207 1128 -146 -78 -16 C ATOM 4318 CG LEU B 124 42.753 18.533 -10.401 1.00 8.94 C ANISOU 4318 CG LEU B 124 1195 929 1274 -102 21 68 C ATOM 4319 CD1 LEU B 124 42.617 17.163 -9.742 1.00 9.72 C ANISOU 4319 CD1 LEU B 124 1452 963 1277 -135 -110 168 C ATOM 4320 CD2 LEU B 124 41.593 19.411 -9.914 1.00 9.95 C ANISOU 4320 CD2 LEU B 124 1200 1122 1457 28 -74 3 C ATOM 4321 N TRP B 125 47.004 20.377 -10.753 1.00 11.19 N ANISOU 4321 N TRP B 125 1274 1558 1421 -139 36 19 N ATOM 4322 CA TRP B 125 48.195 21.151 -10.309 1.00 11.91 C ANISOU 4322 CA TRP B 125 1328 1502 1694 -103 14 44 C ATOM 4323 C TRP B 125 48.325 22.448 -11.085 1.00 11.97 C ANISOU 4323 C TRP B 125 1421 1512 1615 -37 77 39 C ATOM 4324 O TRP B 125 48.587 23.501 -10.483 1.00 12.39 O ANISOU 4324 O TRP B 125 1471 1610 1627 -151 254 44 O ATOM 4325 CB TRP B 125 49.430 20.279 -10.513 1.00 12.47 C ANISOU 4325 CB TRP B 125 1450 1511 1776 24 47 39 C ATOM 4326 CG TRP B 125 50.709 20.938 -10.062 1.00 14.08 C ANISOU 4326 CG TRP B 125 1628 1761 1960 -29 -55 -32 C ATOM 4327 CD1 TRP B 125 51.725 21.335 -10.884 1.00 15.61 C ANISOU 4327 CD1 TRP B 125 1869 2050 2013 -171 27 -22 C ATOM 4328 CD2 TRP B 125 51.121 21.232 -8.731 1.00 14.40 C ANISOU 4328 CD2 TRP B 125 1749 1842 1881 -64 -13 -38 C ATOM 4329 NE1 TRP B 125 52.776 21.857 -10.135 1.00 15.61 N ANISOU 4329 NE1 TRP B 125 1763 2223 1945 -164 22 7 N ATOM 4330 CE2 TRP B 125 52.414 21.816 -8.817 1.00 15.31 C ANISOU 4330 CE2 TRP B 125 1821 2070 1924 -76 22 -17 C ATOM 4331 CE3 TRP B 125 50.528 21.061 -7.475 1.00 14.25 C ANISOU 4331 CE3 TRP B 125 1743 1779 1892 -44 -85 43 C ATOM 4332 CZ2 TRP B 125 53.107 22.254 -7.695 1.00 15.25 C ANISOU 4332 CZ2 TRP B 125 1799 2063 1934 -69 -35 88 C ATOM 4333 CZ3 TRP B 125 51.216 21.486 -6.341 1.00 15.07 C ANISOU 4333 CZ3 TRP B 125 1851 1997 1879 -69 -45 52 C ATOM 4334 CH2 TRP B 125 52.494 22.101 -6.463 1.00 15.16 C ANISOU 4334 CH2 TRP B 125 1777 2055 1929 -25 -36 58 C ATOM 4335 N GLU B 126 48.152 22.421 -12.387 1.00 12.96 N ANISOU 4335 N GLU B 126 1492 1816 1618 34 100 -13 N ATOM 4336 CA GLU B 126 48.256 23.620 -13.227 1.00 15.26 C ANISOU 4336 CA GLU B 126 1850 1804 2144 21 114 104 C ATOM 4337 C GLU B 126 47.243 24.648 -12.788 1.00 13.32 C ANISOU 4337 C GLU B 126 1608 1692 1759 -142 32 53 C ATOM 4338 O GLU B 126 47.573 25.829 -12.564 1.00 13.38 O ANISOU 4338 O GLU B 126 1644 1686 1752 -190 8 -7 O ATOM 4339 CB GLU B 126 48.069 23.215 -14.710 1.00 20.97 C ANISOU 4339 CB GLU B 126 2718 2822 2429 -55 -70 -211 C ATOM 4340 CG GLU B 126 48.278 24.348 -15.707 1.00 28.81 C ANISOU 4340 CG GLU B 126 3903 3416 3629 -24 53 336 C ATOM 4341 CD GLU B 126 47.898 23.973 -17.141 1.00 35.51 C ANISOU 4341 CD GLU B 126 4845 4625 4023 -14 -76 -64 C ATOM 4342 OE1 GLU B 126 47.931 24.853 -18.043 1.00 38.44 O ANISOU 4342 OE1 GLU B 126 5251 4855 4501 -20 0 212 O ATOM 4343 OE2 GLU B 126 47.530 22.796 -17.426 1.00 38.37 O ANISOU 4343 OE2 GLU B 126 5195 4744 4641 -100 -2 -82 O ATOM 4344 N VAL B 127 45.978 24.278 -12.608 1.00 11.16 N ANISOU 4344 N VAL B 127 1409 1398 1434 -67 76 27 N ATOM 4345 CA VAL B 127 44.938 25.227 -12.185 1.00 10.47 C ANISOU 4345 CA VAL B 127 1223 1333 1422 -137 31 77 C ATOM 4346 C VAL B 127 45.164 25.686 -10.759 1.00 10.60 C ANISOU 4346 C VAL B 127 1189 1355 1482 -135 44 67 C ATOM 4347 O VAL B 127 44.988 26.903 -10.471 1.00 11.56 O ANISOU 4347 O VAL B 127 1423 1349 1622 -106 58 91 O ATOM 4348 CB VAL B 127 43.549 24.559 -12.341 1.00 10.13 C ANISOU 4348 CB VAL B 127 1170 1340 1339 -66 -23 30 C ATOM 4349 CG1 VAL B 127 42.427 25.448 -11.788 1.00 12.16 C ANISOU 4349 CG1 VAL B 127 1370 1708 1540 64 86 9 C ATOM 4350 CG2 VAL B 127 43.327 24.293 -13.841 1.00 11.83 C ANISOU 4350 CG2 VAL B 127 1537 1574 1385 -156 2 42 C ATOM 4351 N ALA B 128 45.591 24.816 -9.819 1.00 10.18 N ANISOU 4351 N ALA B 128 1077 1304 1485 -174 102 113 N ATOM 4352 CA ALA B 128 45.819 25.326 -8.453 1.00 10.68 C ANISOU 4352 CA ALA B 128 1227 1296 1536 -127 0 116 C ATOM 4353 C ALA B 128 46.928 26.395 -8.468 1.00 11.63 C ANISOU 4353 C ALA B 128 1464 1258 1697 -146 57 42 C ATOM 4354 O ALA B 128 46.786 27.423 -7.769 1.00 11.27 O ANISOU 4354 O ALA B 128 1487 1213 1582 -335 86 35 O ATOM 4355 CB ALA B 128 46.184 24.164 -7.544 1.00 11.83 C ANISOU 4355 CB ALA B 128 1429 1493 1572 -39 63 145 C ATOM 4356 N ASN B 129 47.996 26.142 -9.227 1.00 12.10 N ANISOU 4356 N ASN B 129 1489 1419 1690 -143 61 109 N ATOM 4357 CA ASN B 129 49.074 27.167 -9.279 1.00 12.98 C ANISOU 4357 CA ASN B 129 1614 1444 1872 -213 58 74 C ATOM 4358 C ASN B 129 48.664 28.423 -10.014 1.00 12.93 C ANISOU 4358 C ASN B 129 1627 1527 1760 -87 91 4 C ATOM 4359 O ASN B 129 49.048 29.561 -9.609 1.00 13.97 O ANISOU 4359 O ASN B 129 1727 1429 2153 -253 44 165 O ATOM 4360 CB ASN B 129 50.329 26.529 -9.901 1.00 13.81 C ANISOU 4360 CB ASN B 129 1657 1579 2012 -107 -13 -5 C ATOM 4361 CG ASN B 129 51.050 25.708 -8.840 1.00 15.38 C ANISOU 4361 CG ASN B 129 1895 1782 2165 -82 -118 13 C ATOM 4362 OD1 ASN B 129 51.878 26.286 -8.105 1.00 16.06 O ANISOU 4362 OD1 ASN B 129 1788 1886 2430 -143 -103 -81 O ATOM 4363 ND2 ASN B 129 50.723 24.432 -8.673 1.00 14.84 N ANISOU 4363 ND2 ASN B 129 1832 1660 2147 59 -52 -4 N ATOM 4364 N ARG B 130 47.859 28.321 -11.044 1.00 13.15 N ANISOU 4364 N ARG B 130 1587 1599 1812 -112 21 88 N ATOM 4365 CA ARG B 130 47.362 29.498 -11.780 1.00 14.39 C ANISOU 4365 CA ARG B 130 1849 1622 1996 86 65 89 C ATOM 4366 C ARG B 130 46.618 30.427 -10.822 1.00 14.13 C ANISOU 4366 C ARG B 130 1865 1557 1945 -57 172 117 C ATOM 4367 O ARG B 130 46.710 31.663 -10.940 1.00 14.40 O ANISOU 4367 O ARG B 130 1844 1468 2161 -137 266 20 O ATOM 4368 CB ARG B 130 46.441 29.034 -12.929 1.00 15.63 C ANISOU 4368 CB ARG B 130 1980 1868 2091 -31 27 45 C ATOM 4369 CG ARG B 130 45.791 30.203 -13.709 1.00 18.82 C ANISOU 4369 CG ARG B 130 2442 2145 2563 179 -46 161 C ATOM 4370 CD ARG B 130 45.090 29.667 -14.955 1.00 23.18 C ANISOU 4370 CD ARG B 130 3024 2903 2879 -52 -190 11 C ATOM 4371 NE ARG B 130 46.039 28.948 -15.832 1.00 26.76 N ANISOU 4371 NE ARG B 130 3365 3369 3434 33 88 -41 N ATOM 4372 CZ ARG B 130 45.750 27.796 -16.439 1.00 28.44 C ANISOU 4372 CZ ARG B 130 3650 3469 3686 -9 37 -106 C ATOM 4373 NH1 ARG B 130 46.724 27.285 -17.191 1.00 29.97 N ANISOU 4373 NH1 ARG B 130 3625 3910 3852 -57 226 1 N ATOM 4374 NH2 ARG B 130 44.569 27.174 -16.273 1.00 28.31 N ANISOU 4374 NH2 ARG B 130 3602 3461 3691 -8 103 -22 N ATOM 4375 N TYR B 131 45.819 29.907 -9.881 1.00 12.27 N ANISOU 4375 N TYR B 131 1507 1440 1714 -43 56 53 N ATOM 4376 CA TYR B 131 45.015 30.757 -9.001 1.00 11.65 C ANISOU 4376 CA TYR B 131 1339 1488 1599 -70 -55 42 C ATOM 4377 C TYR B 131 45.530 30.746 -7.576 1.00 11.24 C ANISOU 4377 C TYR B 131 1386 1281 1602 -82 -1 44 C ATOM 4378 O TYR B 131 44.842 31.031 -6.596 1.00 11.78 O ANISOU 4378 O TYR B 131 1451 1490 1534 -159 -34 78 O ATOM 4379 CB TYR B 131 43.527 30.300 -9.036 1.00 11.74 C ANISOU 4379 CB TYR B 131 1386 1519 1556 -183 20 -4 C ATOM 4380 CG TYR B 131 43.014 30.373 -10.463 1.00 12.83 C ANISOU 4380 CG TYR B 131 1630 1642 1604 -100 -65 48 C ATOM 4381 CD1 TYR B 131 42.767 29.206 -11.211 1.00 13.06 C ANISOU 4381 CD1 TYR B 131 1641 1715 1605 -72 -90 -10 C ATOM 4382 CD2 TYR B 131 42.807 31.632 -11.062 1.00 13.81 C ANISOU 4382 CD2 TYR B 131 1763 1708 1774 -17 -146 78 C ATOM 4383 CE1 TYR B 131 42.332 29.315 -12.536 1.00 12.99 C ANISOU 4383 CE1 TYR B 131 1600 1748 1588 -56 -58 40 C ATOM 4384 CE2 TYR B 131 42.354 31.715 -12.369 1.00 13.29 C ANISOU 4384 CE2 TYR B 131 1656 1736 1659 -60 11 36 C ATOM 4385 CZ TYR B 131 42.118 30.562 -13.080 1.00 14.00 C ANISOU 4385 CZ TYR B 131 1797 1763 1758 -21 -78 25 C ATOM 4386 OH TYR B 131 41.664 30.710 -14.389 1.00 14.88 O ANISOU 4386 OH TYR B 131 2076 1780 1798 -19 -121 73 O ATOM 4387 N LYS B 132 46.828 30.431 -7.408 1.00 11.82 N ANISOU 4387 N LYS B 132 1350 1430 1709 -140 -47 125 N ATOM 4388 CA LYS B 132 47.432 30.309 -6.106 1.00 13.22 C ANISOU 4388 CA LYS B 132 1526 1748 1750 -108 -108 27 C ATOM 4389 C LYS B 132 47.166 31.531 -5.235 1.00 14.18 C ANISOU 4389 C LYS B 132 1613 1907 1868 -55 -44 -6 C ATOM 4390 O LYS B 132 46.957 31.456 -4.025 1.00 16.17 O ANISOU 4390 O LYS B 132 1695 2503 1945 -156 -9 -44 O ATOM 4391 CB LYS B 132 48.954 30.154 -6.353 1.00 14.40 C ANISOU 4391 CB LYS B 132 1611 1847 2012 59 -11 -61 C ATOM 4392 CG LYS B 132 49.699 29.885 -5.034 1.00 17.13 C ANISOU 4392 CG LYS B 132 2152 2235 2120 -26 -57 51 C ATOM 4393 CD LYS B 132 51.107 29.463 -5.526 1.00 21.77 C ANISOU 4393 CD LYS B 132 2346 2911 3015 27 148 61 C ATOM 4394 CE LYS B 132 52.086 29.778 -4.445 1.00 26.00 C ANISOU 4394 CE LYS B 132 3262 3329 3287 -88 -198 -7 C ATOM 4395 NZ LYS B 132 53.316 28.935 -4.646 1.00 28.71 N ANISOU 4395 NZ LYS B 132 3654 3237 4017 55 19 -1 N ATOM 4396 N HIS B 133 47.270 32.720 -5.814 1.00 14.65 N ANISOU 4396 N HIS B 133 1600 1807 2161 -88 -89 -8 N ATOM 4397 CA HIS B 133 47.072 33.938 -5.014 1.00 17.06 C ANISOU 4397 CA HIS B 133 1947 2197 2338 61 -25 -199 C ATOM 4398 C HIS B 133 45.732 34.606 -5.266 1.00 16.62 C ANISOU 4398 C HIS B 133 1834 2027 2453 -59 -107 -169 C ATOM 4399 O HIS B 133 45.545 35.804 -4.973 1.00 17.65 O ANISOU 4399 O HIS B 133 1680 2121 2904 -140 -89 -295 O ATOM 4400 CB HIS B 133 48.270 34.892 -5.181 1.00 20.45 C ANISOU 4400 CB HIS B 133 2436 2419 2913 -208 -8 -114 C ATOM 4401 CG HIS B 133 49.584 34.273 -4.728 1.00 23.28 C ANISOU 4401 CG HIS B 133 2735 2903 3209 79 -104 -74 C ATOM 4402 ND1 HIS B 133 49.737 33.737 -3.444 1.00 26.07 N ANISOU 4402 ND1 HIS B 133 3107 3424 3375 -19 -89 71 N ATOM 4403 CD2 HIS B 133 50.736 34.050 -5.377 1.00 23.75 C ANISOU 4403 CD2 HIS B 133 2896 3017 3111 -136 51 5 C ATOM 4404 CE1 HIS B 133 50.993 33.229 -3.308 1.00 25.74 C ANISOU 4404 CE1 HIS B 133 3160 3157 3461 40 100 72 C ATOM 4405 NE2 HIS B 133 51.579 33.386 -4.513 1.00 25.72 N ANISOU 4405 NE2 HIS B 133 2884 3400 3490 9 46 -9 N ATOM 4406 N THR B 134 44.749 33.940 -5.869 1.00 13.66 N ANISOU 4406 N THR B 134 1535 1533 2123 -21 50 26 N ATOM 4407 CA THR B 134 43.425 34.517 -6.103 1.00 12.68 C ANISOU 4407 CA THR B 134 1500 1449 1868 -90 0 17 C ATOM 4408 C THR B 134 42.597 34.432 -4.845 1.00 12.88 C ANISOU 4408 C THR B 134 1633 1437 1826 -8 2 59 C ATOM 4409 O THR B 134 42.261 33.294 -4.411 1.00 13.68 O ANISOU 4409 O THR B 134 1590 1446 2161 -67 26 81 O ATOM 4410 CB THR B 134 42.777 33.645 -7.204 1.00 13.61 C ANISOU 4410 CB THR B 134 1667 1700 1805 -4 -22 -67 C ATOM 4411 OG1 THR B 134 43.673 33.688 -8.336 1.00 13.85 O ANISOU 4411 OG1 THR B 134 1571 1687 2006 -174 32 -124 O ATOM 4412 CG2 THR B 134 41.376 34.060 -7.615 1.00 13.53 C ANISOU 4412 CG2 THR B 134 1674 1694 1774 -29 -88 -10 C ATOM 4413 N PRO B 135 42.170 35.520 -4.245 1.00 12.94 N ANISOU 4413 N PRO B 135 1704 1454 1759 -84 26 -5 N ATOM 4414 CA PRO B 135 41.373 35.503 -3.027 1.00 12.01 C ANISOU 4414 CA PRO B 135 1472 1357 1733 -173 33 21 C ATOM 4415 C PRO B 135 39.947 35.061 -3.322 1.00 11.65 C ANISOU 4415 C PRO B 135 1390 1426 1611 -59 21 119 C ATOM 4416 O PRO B 135 39.362 35.392 -4.362 1.00 12.10 O ANISOU 4416 O PRO B 135 1232 1609 1759 -196 -141 7 O ATOM 4417 CB PRO B 135 41.321 36.958 -2.527 1.00 13.58 C ANISOU 4417 CB PRO B 135 1772 1452 1936 -170 35 -42 C ATOM 4418 CG PRO B 135 42.280 37.692 -3.414 1.00 14.98 C ANISOU 4418 CG PRO B 135 2028 1704 1958 -145 227 -34 C ATOM 4419 CD PRO B 135 42.609 36.907 -4.628 1.00 13.25 C ANISOU 4419 CD PRO B 135 1734 1451 1850 -111 19 -7 C ATOM 4420 N THR B 136 39.366 34.330 -2.377 1.00 10.62 N ANISOU 4420 N THR B 136 1259 1153 1623 -143 -101 121 N ATOM 4421 CA THR B 136 37.946 33.913 -2.482 1.00 10.83 C ANISOU 4421 CA THR B 136 1188 1373 1556 -61 -34 29 C ATOM 4422 C THR B 136 37.460 33.745 -1.051 1.00 11.27 C ANISOU 4422 C THR B 136 1228 1455 1598 -53 -9 -25 C ATOM 4423 O THR B 136 38.288 33.728 -0.145 1.00 12.49 O ANISOU 4423 O THR B 136 1272 2028 1447 -55 81 70 O ATOM 4424 CB THR B 136 37.845 32.616 -3.317 1.00 12.35 C ANISOU 4424 CB THR B 136 1465 1373 1853 -52 -123 9 C ATOM 4425 OG1 THR B 136 36.466 32.296 -3.565 1.00 14.64 O ANISOU 4425 OG1 THR B 136 1614 1768 2180 -230 -147 106 O ATOM 4426 CG2 THR B 136 38.437 31.443 -2.520 1.00 11.35 C ANISOU 4426 CG2 THR B 136 1463 1355 1493 -33 -62 -74 C ATOM 4427 N ILE B 137 36.176 33.689 -0.759 1.00 10.54 N ANISOU 4427 N ILE B 137 1224 1229 1553 -69 58 -49 N ATOM 4428 CA ILE B 137 35.664 33.510 0.587 1.00 11.23 C ANISOU 4428 CA ILE B 137 1392 1331 1543 12 -1 7 C ATOM 4429 C ILE B 137 35.527 32.034 0.921 1.00 11.16 C ANISOU 4429 C ILE B 137 1400 1323 1516 -60 -86 -58 C ATOM 4430 O ILE B 137 34.996 31.260 0.108 1.00 11.78 O ANISOU 4430 O ILE B 137 1658 989 1829 -162 -119 -55 O ATOM 4431 CB ILE B 137 34.333 34.261 0.764 1.00 11.22 C ANISOU 4431 CB ILE B 137 1308 1414 1541 0 -24 -6 C ATOM 4432 CG1 ILE B 137 33.923 34.280 2.252 1.00 11.75 C ANISOU 4432 CG1 ILE B 137 1352 1610 1502 0 -78 -116 C ATOM 4433 CG2 ILE B 137 33.211 33.649 -0.071 1.00 11.39 C ANISOU 4433 CG2 ILE B 137 1323 1514 1490 52 -54 -53 C ATOM 4434 CD1 ILE B 137 34.920 34.951 3.176 1.00 12.82 C ANISOU 4434 CD1 ILE B 137 1490 1577 1803 -71 -114 -188 C ATOM 4435 N GLY B 138 36.202 31.574 1.998 1.00 11.28 N ANISOU 4435 N GLY B 138 1353 1381 1551 -76 -131 19 N ATOM 4436 CA GLY B 138 35.984 30.222 2.478 1.00 11.07 C ANISOU 4436 CA GLY B 138 1248 1398 1560 -30 -76 72 C ATOM 4437 C GLY B 138 34.575 30.121 3.058 1.00 11.80 C ANISOU 4437 C GLY B 138 1423 1389 1672 -55 83 39 C ATOM 4438 O GLY B 138 34.105 31.091 3.625 1.00 12.15 O ANISOU 4438 O GLY B 138 1652 1302 1664 -118 67 -24 O ATOM 4439 N ARG B 139 33.897 28.971 2.878 1.00 11.48 N ANISOU 4439 N ARG B 139 1306 1387 1669 -67 -71 22 N ATOM 4440 CA ARG B 139 32.498 28.870 3.283 1.00 10.88 C ANISOU 4440 CA ARG B 139 1368 1365 1400 -98 28 160 C ATOM 4441 C ARG B 139 32.313 27.608 4.124 1.00 10.66 C ANISOU 4441 C ARG B 139 1272 1290 1490 -53 -11 99 C ATOM 4442 O ARG B 139 32.751 26.525 3.722 1.00 10.05 O ANISOU 4442 O ARG B 139 1176 1240 1403 -110 -34 154 O ATOM 4443 CB ARG B 139 31.603 28.757 2.027 1.00 11.94 C ANISOU 4443 CB ARG B 139 1439 1545 1551 6 -62 214 C ATOM 4444 CG ARG B 139 31.630 29.999 1.110 1.00 11.36 C ANISOU 4444 CG ARG B 139 1510 1324 1482 -131 -24 135 C ATOM 4445 CD ARG B 139 30.850 29.679 -0.177 1.00 12.47 C ANISOU 4445 CD ARG B 139 1795 1465 1479 -16 -106 69 C ATOM 4446 NE ARG B 139 30.593 30.862 -0.996 1.00 13.01 N ANISOU 4446 NE ARG B 139 1767 1528 1648 -33 -31 99 N ATOM 4447 CZ ARG B 139 31.347 31.294 -2.010 1.00 12.56 C ANISOU 4447 CZ ARG B 139 1689 1400 1682 -18 28 68 C ATOM 4448 NH1 ARG B 139 32.451 30.650 -2.364 1.00 12.07 N ANISOU 4448 NH1 ARG B 139 1536 1308 1742 -193 -47 -75 N ATOM 4449 NH2 ARG B 139 30.959 32.413 -2.627 1.00 11.89 N ANISOU 4449 NH2 ARG B 139 1693 1376 1450 -79 -81 20 N ATOM 4450 N THR B 140 31.722 27.777 5.307 1.00 10.35 N ANISOU 4450 N THR B 140 1197 1332 1403 -18 -106 110 N ATOM 4451 CA THR B 140 31.437 26.617 6.142 1.00 10.87 C ANISOU 4451 CA THR B 140 1311 1355 1462 -70 58 46 C ATOM 4452 C THR B 140 29.953 26.621 6.417 1.00 11.43 C ANISOU 4452 C THR B 140 1328 1356 1659 -10 34 -13 C ATOM 4453 O THR B 140 29.351 27.651 6.745 1.00 11.08 O ANISOU 4453 O THR B 140 1283 1195 1732 -157 55 -63 O ATOM 4454 CB THR B 140 32.243 26.626 7.471 1.00 12.37 C ANISOU 4454 CB THR B 140 1371 1664 1667 -21 -42 -13 C ATOM 4455 OG1 THR B 140 31.932 27.877 8.133 1.00 13.59 O ANISOU 4455 OG1 THR B 140 1610 1802 1751 28 -19 -73 O ATOM 4456 CG2 THR B 140 33.725 26.538 7.184 1.00 11.83 C ANISOU 4456 CG2 THR B 140 1364 1635 1495 -116 -71 31 C ATOM 4457 N HIS B 141 29.299 25.453 6.291 1.00 11.10 N ANISOU 4457 N HIS B 141 1349 1343 1525 -38 117 -52 N ATOM 4458 CA HIS B 141 27.834 25.383 6.419 1.00 12.06 C ANISOU 4458 CA HIS B 141 1417 1583 1582 20 12 15 C ATOM 4459 C HIS B 141 27.171 26.240 5.358 1.00 12.43 C ANISOU 4459 C HIS B 141 1595 1543 1585 30 -6 24 C ATOM 4460 O HIS B 141 26.038 26.694 5.563 1.00 12.84 O ANISOU 4460 O HIS B 141 1710 1509 1662 59 57 28 O ATOM 4461 CB HIS B 141 27.366 25.822 7.829 1.00 11.16 C ANISOU 4461 CB HIS B 141 1395 1293 1552 -41 5 7 C ATOM 4462 CG HIS B 141 28.176 25.244 8.945 1.00 12.53 C ANISOU 4462 CG HIS B 141 1592 1601 1570 -17 -44 3 C ATOM 4463 ND1 HIS B 141 28.133 23.922 9.324 1.00 13.17 N ANISOU 4463 ND1 HIS B 141 1700 1577 1727 -49 -113 25 N ATOM 4464 CD2 HIS B 141 29.063 25.864 9.767 1.00 13.30 C ANISOU 4464 CD2 HIS B 141 1671 1639 1745 -103 -69 25 C ATOM 4465 CE1 HIS B 141 28.983 23.732 10.332 1.00 14.10 C ANISOU 4465 CE1 HIS B 141 1797 1796 1765 -97 -141 40 C ATOM 4466 NE2 HIS B 141 29.581 24.904 10.620 1.00 13.90 N ANISOU 4466 NE2 HIS B 141 1857 1710 1714 -11 -89 40 N ATOM 4467 N GLY B 142 27.782 26.462 4.190 1.00 12.26 N ANISOU 4467 N GLY B 142 1608 1347 1701 -54 37 74 N ATOM 4468 CA GLY B 142 27.260 27.350 3.180 1.00 12.67 C ANISOU 4468 CA GLY B 142 1604 1497 1713 -16 -116 20 C ATOM 4469 C GLY B 142 27.326 28.827 3.534 1.00 12.73 C ANISOU 4469 C GLY B 142 1535 1493 1808 -96 -35 16 C ATOM 4470 O GLY B 142 26.738 29.645 2.813 1.00 13.65 O ANISOU 4470 O GLY B 142 1497 1572 2119 -89 -154 53 O ATOM 4471 N VAL B 143 28.027 29.182 4.610 1.00 12.08 N ANISOU 4471 N VAL B 143 1576 1274 1742 26 -2 -19 N ATOM 4472 CA VAL B 143 27.993 30.551 5.142 1.00 11.40 C ANISOU 4472 CA VAL B 143 1439 1326 1567 -91 15 -78 C ATOM 4473 C VAL B 143 29.401 31.133 5.063 1.00 11.08 C ANISOU 4473 C VAL B 143 1403 1281 1528 -48 52 81 C ATOM 4474 O VAL B 143 30.383 30.412 5.329 1.00 11.06 O ANISOU 4474 O VAL B 143 1386 1285 1530 1 4 32 O ATOM 4475 CB VAL B 143 27.483 30.546 6.587 1.00 11.07 C ANISOU 4475 CB VAL B 143 1342 1297 1568 -79 44 -57 C ATOM 4476 CG1 VAL B 143 27.693 31.877 7.313 1.00 11.93 C ANISOU 4476 CG1 VAL B 143 1483 1548 1503 -170 92 -165 C ATOM 4477 CG2 VAL B 143 25.987 30.191 6.558 1.00 12.76 C ANISOU 4477 CG2 VAL B 143 1388 1598 1862 -5 121 -107 C ATOM 4478 N HIS B 144 29.515 32.407 4.703 1.00 11.56 N ANISOU 4478 N HIS B 144 1554 1260 1579 -108 96 43 N ATOM 4479 CA HIS B 144 30.854 32.997 4.592 1.00 11.74 C ANISOU 4479 CA HIS B 144 1433 1299 1729 -33 -23 156 C ATOM 4480 C HIS B 144 31.626 32.907 5.899 1.00 12.92 C ANISOU 4480 C HIS B 144 1543 1634 1731 20 10 18 C ATOM 4481 O HIS B 144 31.122 33.276 6.975 1.00 12.16 O ANISOU 4481 O HIS B 144 1287 1559 1775 -6 76 33 O ATOM 4482 CB HIS B 144 30.755 34.488 4.159 1.00 11.71 C ANISOU 4482 CB HIS B 144 1537 1278 1635 -56 46 146 C ATOM 4483 CG HIS B 144 30.371 34.668 2.720 1.00 11.60 C ANISOU 4483 CG HIS B 144 1404 1348 1655 -27 24 82 C ATOM 4484 ND1 HIS B 144 29.799 33.770 1.858 1.00 12.96 N ANISOU 4484 ND1 HIS B 144 1506 1752 1666 -39 -33 -23 N ATOM 4485 CD2 HIS B 144 30.494 35.837 2.020 1.00 10.31 C ANISOU 4485 CD2 HIS B 144 1161 1249 1508 -61 10 87 C ATOM 4486 CE1 HIS B 144 29.578 34.332 0.673 1.00 10.73 C ANISOU 4486 CE1 HIS B 144 1192 1338 1547 1 41 36 C ATOM 4487 NE2 HIS B 144 30.019 35.560 0.777 1.00 12.95 N ANISOU 4487 NE2 HIS B 144 1500 1647 1771 -20 -75 -24 N ATOM 4488 N ALA B 145 32.877 32.445 5.810 1.00 12.48 N ANISOU 4488 N ALA B 145 1394 1445 1901 -108 71 113 N ATOM 4489 CA ALA B 145 33.685 32.217 7.014 1.00 13.41 C ANISOU 4489 CA ALA B 145 1622 1524 1947 -73 -23 0 C ATOM 4490 C ALA B 145 34.857 33.168 6.917 1.00 14.99 C ANISOU 4490 C ALA B 145 1660 1856 2179 -164 17 -11 C ATOM 4491 O ALA B 145 34.698 34.325 7.355 1.00 17.05 O ANISOU 4491 O ALA B 145 1836 1975 2667 -203 18 -63 O ATOM 4492 CB ALA B 145 34.097 30.740 7.093 1.00 13.54 C ANISOU 4492 CB ALA B 145 1654 1527 1963 -80 -84 205 C ATOM 4493 N GLU B 146 35.993 32.754 6.409 1.00 14.74 N ANISOU 4493 N GLU B 146 1760 1756 2084 -94 -25 -71 N ATOM 4494 CA GLU B 146 37.191 33.611 6.342 1.00 14.93 C ANISOU 4494 CA GLU B 146 1750 1898 2025 -149 120 101 C ATOM 4495 C GLU B 146 37.707 33.535 4.932 1.00 13.27 C ANISOU 4495 C GLU B 146 1648 1570 1826 -138 -59 55 C ATOM 4496 O GLU B 146 37.498 32.537 4.230 1.00 12.75 O ANISOU 4496 O GLU B 146 1406 1299 2141 -245 -53 154 O ATOM 4497 CB GLU B 146 38.300 33.038 7.264 1.00 16.81 C ANISOU 4497 CB GLU B 146 2019 2216 2152 -200 -89 102 C ATOM 4498 CG GLU B 146 38.009 33.258 8.719 1.00 19.68 C ANISOU 4498 CG GLU B 146 2539 2569 2370 -144 46 -18 C ATOM 4499 CD GLU B 146 39.097 32.836 9.671 1.00 20.46 C ANISOU 4499 CD GLU B 146 2654 2539 2579 -88 -3 71 C ATOM 4500 OE1 GLU B 146 40.071 32.164 9.272 1.00 20.77 O ANISOU 4500 OE1 GLU B 146 2735 2560 2596 -106 98 -47 O ATOM 4501 OE2 GLU B 146 38.964 33.234 10.853 1.00 22.19 O ANISOU 4501 OE2 GLU B 146 3047 2743 2642 -108 87 -21 O ATOM 4502 N PRO B 147 38.393 34.589 4.452 1.00 12.58 N ANISOU 4502 N PRO B 147 1573 1485 1723 -132 3 12 N ATOM 4503 CA PRO B 147 39.050 34.548 3.168 1.00 11.64 C ANISOU 4503 CA PRO B 147 1536 1257 1632 -112 2 22 C ATOM 4504 C PRO B 147 40.037 33.401 3.040 1.00 11.24 C ANISOU 4504 C PRO B 147 1454 1320 1494 -140 -78 15 C ATOM 4505 O PRO B 147 40.696 32.994 4.009 1.00 11.40 O ANISOU 4505 O PRO B 147 1522 1354 1454 -73 -134 101 O ATOM 4506 CB PRO B 147 39.813 35.907 3.103 1.00 11.72 C ANISOU 4506 CB PRO B 147 1430 1293 1729 -155 54 -103 C ATOM 4507 CG PRO B 147 38.914 36.786 3.958 1.00 12.07 C ANISOU 4507 CG PRO B 147 1635 1326 1623 -19 57 -23 C ATOM 4508 CD PRO B 147 38.615 35.878 5.146 1.00 12.33 C ANISOU 4508 CD PRO B 147 1542 1514 1629 -94 100 1 C ATOM 4509 N THR B 148 40.214 32.915 1.822 1.00 10.83 N ANISOU 4509 N THR B 148 1333 1302 1481 -149 36 -18 N ATOM 4510 CA THR B 148 41.260 31.930 1.515 1.00 10.96 C ANISOU 4510 CA THR B 148 1341 1315 1507 -68 -20 46 C ATOM 4511 C THR B 148 41.613 32.101 0.059 1.00 11.72 C ANISOU 4511 C THR B 148 1507 1403 1545 -33 -27 -14 C ATOM 4512 O THR B 148 41.275 33.159 -0.521 1.00 11.96 O ANISOU 4512 O THR B 148 1441 1552 1553 -93 71 196 O ATOM 4513 CB THR B 148 40.764 30.495 1.874 1.00 12.13 C ANISOU 4513 CB THR B 148 1662 1323 1622 -8 -80 -25 C ATOM 4514 OG1 THR B 148 41.927 29.639 1.800 1.00 12.56 O ANISOU 4514 OG1 THR B 148 1496 1510 1765 -7 -50 3 O ATOM 4515 CG2 THR B 148 39.707 30.069 0.875 1.00 13.12 C ANISOU 4515 CG2 THR B 148 1470 1675 1841 -146 -36 -23 C ATOM 4516 N SER B 149 42.370 31.178 -0.521 1.00 12.19 N ANISOU 4516 N SER B 149 1456 1629 1548 -56 67 -55 N ATOM 4517 CA SER B 149 42.788 31.301 -1.923 1.00 11.74 C ANISOU 4517 CA SER B 149 1455 1515 1492 -77 -57 -101 C ATOM 4518 C SER B 149 42.008 30.284 -2.734 1.00 11.05 C ANISOU 4518 C SER B 149 1306 1419 1472 -75 -21 55 C ATOM 4519 O SER B 149 41.950 29.123 -2.308 1.00 10.57 O ANISOU 4519 O SER B 149 1355 1213 1447 -53 5 -64 O ATOM 4520 CB SER B 149 44.271 30.886 -1.887 1.00 13.18 C ANISOU 4520 CB SER B 149 1404 1807 1796 -189 13 -186 C ATOM 4521 OG SER B 149 44.754 30.364 -3.093 1.00 13.84 O ANISOU 4521 OG SER B 149 1633 1542 2083 -165 20 -235 O ATOM 4522 N PHE B 150 41.561 30.637 -3.940 1.00 11.23 N ANISOU 4522 N PHE B 150 1319 1490 1456 -76 -133 -25 N ATOM 4523 CA PHE B 150 40.938 29.650 -4.792 1.00 10.83 C ANISOU 4523 CA PHE B 150 1329 1309 1477 -86 -20 -3 C ATOM 4524 C PHE B 150 41.940 28.589 -5.210 1.00 11.51 C ANISOU 4524 C PHE B 150 1339 1360 1675 -32 -46 13 C ATOM 4525 O PHE B 150 41.584 27.418 -5.385 1.00 11.50 O ANISOU 4525 O PHE B 150 1351 1348 1669 -140 -93 52 O ATOM 4526 CB PHE B 150 40.318 30.343 -6.026 1.00 12.86 C ANISOU 4526 CB PHE B 150 1673 1690 1522 11 -188 -32 C ATOM 4527 CG PHE B 150 39.572 29.341 -6.884 1.00 12.59 C ANISOU 4527 CG PHE B 150 1518 1634 1632 -100 -134 -33 C ATOM 4528 CD1 PHE B 150 38.432 28.719 -6.391 1.00 12.22 C ANISOU 4528 CD1 PHE B 150 1519 1553 1573 0 -101 14 C ATOM 4529 CD2 PHE B 150 40.028 29.059 -8.159 1.00 13.12 C ANISOU 4529 CD2 PHE B 150 1678 1662 1644 11 -126 -16 C ATOM 4530 CE1 PHE B 150 37.736 27.814 -7.219 1.00 12.32 C ANISOU 4530 CE1 PHE B 150 1462 1663 1556 -88 -144 17 C ATOM 4531 CE2 PHE B 150 39.340 28.153 -8.975 1.00 12.76 C ANISOU 4531 CE2 PHE B 150 1587 1568 1693 -17 -96 67 C ATOM 4532 CZ PHE B 150 38.218 27.527 -8.490 1.00 12.38 C ANISOU 4532 CZ PHE B 150 1356 1681 1668 63 -121 2 C ATOM 4533 N GLY B 151 43.216 28.976 -5.412 1.00 11.55 N ANISOU 4533 N GLY B 151 1320 1430 1637 19 88 -89 N ATOM 4534 CA GLY B 151 44.218 27.937 -5.757 1.00 11.38 C ANISOU 4534 CA GLY B 151 1248 1351 1723 63 -20 -22 C ATOM 4535 C GLY B 151 44.309 26.869 -4.696 1.00 11.38 C ANISOU 4535 C GLY B 151 1329 1424 1569 -40 -7 -71 C ATOM 4536 O GLY B 151 44.560 25.686 -4.941 1.00 10.51 O ANISOU 4536 O GLY B 151 1140 1278 1576 10 -53 140 O ATOM 4537 N LEU B 152 44.267 27.277 -3.416 1.00 12.38 N ANISOU 4537 N LEU B 152 1373 1748 1584 -89 40 -75 N ATOM 4538 CA LEU B 152 44.317 26.346 -2.318 1.00 12.82 C ANISOU 4538 CA LEU B 152 1495 1602 1774 15 -68 -26 C ATOM 4539 C LEU B 152 43.075 25.442 -2.311 1.00 12.06 C ANISOU 4539 C LEU B 152 1358 1596 1627 108 -53 16 C ATOM 4540 O LEU B 152 43.205 24.268 -2.015 1.00 11.69 O ANISOU 4540 O LEU B 152 1307 1420 1713 -33 -47 -22 O ATOM 4541 CB LEU B 152 44.361 27.192 -1.040 1.00 15.86 C ANISOU 4541 CB LEU B 152 2060 2069 1899 173 -45 -220 C ATOM 4542 CG LEU B 152 44.909 26.618 0.207 1.00 18.04 C ANISOU 4542 CG LEU B 152 2235 2510 2110 270 -166 -136 C ATOM 4543 CD1 LEU B 152 46.352 26.155 0.113 1.00 18.25 C ANISOU 4543 CD1 LEU B 152 2262 2576 2097 341 -35 -136 C ATOM 4544 CD2 LEU B 152 45.053 27.623 1.334 1.00 17.79 C ANISOU 4544 CD2 LEU B 152 2214 2437 2108 336 -84 -186 C ATOM 4545 N LYS B 153 41.914 25.992 -2.660 1.00 10.88 N ANISOU 4545 N LYS B 153 1156 1579 1400 129 13 -4 N ATOM 4546 CA LYS B 153 40.756 25.083 -2.798 1.00 11.88 C ANISOU 4546 CA LYS B 153 1345 1425 1742 98 -27 -34 C ATOM 4547 C LYS B 153 41.005 24.014 -3.849 1.00 11.40 C ANISOU 4547 C LYS B 153 1399 1424 1508 5 -6 74 C ATOM 4548 O LYS B 153 40.813 22.835 -3.549 1.00 10.73 O ANISOU 4548 O LYS B 153 1207 1460 1409 -106 136 230 O ATOM 4549 CB LYS B 153 39.533 25.909 -3.222 1.00 12.67 C ANISOU 4549 CB LYS B 153 1494 1484 1837 167 -139 125 C ATOM 4550 CG LYS B 153 38.252 25.112 -3.348 1.00 15.13 C ANISOU 4550 CG LYS B 153 1752 1802 2195 -10 -41 -46 C ATOM 4551 CD LYS B 153 37.118 26.031 -3.892 1.00 17.42 C ANISOU 4551 CD LYS B 153 2025 2179 2415 155 -211 -73 C ATOM 4552 CE LYS B 153 36.697 26.972 -2.766 1.00 17.67 C ANISOU 4552 CE LYS B 153 2133 2131 2449 190 -59 -61 C ATOM 4553 NZ LYS B 153 35.370 27.575 -3.144 1.00 17.02 N ANISOU 4553 NZ LYS B 153 2090 2259 2120 84 -171 -175 N ATOM 4554 N VAL B 154 41.514 24.380 -5.021 1.00 10.41 N ANISOU 4554 N VAL B 154 1252 1352 1352 -32 -49 13 N ATOM 4555 CA VAL B 154 41.865 23.409 -6.060 1.00 10.30 C ANISOU 4555 CA VAL B 154 1290 1255 1369 100 -5 77 C ATOM 4556 C VAL B 154 43.002 22.493 -5.608 1.00 9.07 C ANISOU 4556 C VAL B 154 1037 1205 1206 -19 12 44 C ATOM 4557 O VAL B 154 42.996 21.303 -5.920 1.00 10.11 O ANISOU 4557 O VAL B 154 1299 1201 1343 -4 -71 84 O ATOM 4558 CB VAL B 154 42.243 24.097 -7.379 1.00 10.48 C ANISOU 4558 CB VAL B 154 1408 1221 1355 93 13 45 C ATOM 4559 CG1 VAL B 154 42.556 23.150 -8.539 1.00 10.78 C ANISOU 4559 CG1 VAL B 154 1385 1299 1412 16 179 -7 C ATOM 4560 CG2 VAL B 154 41.014 24.951 -7.806 1.00 10.71 C ANISOU 4560 CG2 VAL B 154 1206 1249 1615 66 37 -11 C ATOM 4561 N LEU B 155 43.953 22.980 -4.845 1.00 8.60 N ANISOU 4561 N LEU B 155 1030 1198 1041 -27 28 81 N ATOM 4562 CA LEU B 155 45.051 22.109 -4.362 1.00 9.35 C ANISOU 4562 CA LEU B 155 1124 1253 1176 -33 -156 13 C ATOM 4563 C LEU B 155 44.498 20.994 -3.484 1.00 8.99 C ANISOU 4563 C LEU B 155 1041 1223 1151 -56 -129 -58 C ATOM 4564 O LEU B 155 45.038 19.881 -3.447 1.00 9.95 O ANISOU 4564 O LEU B 155 1137 1269 1374 -1 -104 -84 O ATOM 4565 CB LEU B 155 45.963 22.945 -3.472 1.00 10.90 C ANISOU 4565 CB LEU B 155 1297 1522 1321 -196 -37 -144 C ATOM 4566 CG LEU B 155 47.419 22.695 -3.388 1.00 13.69 C ANISOU 4566 CG LEU B 155 1567 1946 1687 95 -126 -102 C ATOM 4567 CD1 LEU B 155 48.175 22.931 -2.145 1.00 12.39 C ANISOU 4567 CD1 LEU B 155 1575 1702 1432 42 -97 184 C ATOM 4568 CD2 LEU B 155 48.099 21.712 -4.245 1.00 13.45 C ANISOU 4568 CD2 LEU B 155 1724 1553 1833 53 -132 -34 C ATOM 4569 N GLY B 156 43.396 21.255 -2.767 1.00 9.50 N ANISOU 4569 N GLY B 156 1120 1262 1226 -65 12 36 N ATOM 4570 CA GLY B 156 42.707 20.262 -1.956 1.00 8.93 C ANISOU 4570 CA GLY B 156 1082 1124 1188 -138 -18 -34 C ATOM 4571 C GLY B 156 42.182 19.129 -2.853 1.00 9.96 C ANISOU 4571 C GLY B 156 1262 1215 1306 -101 -30 -63 C ATOM 4572 O GLY B 156 42.247 17.941 -2.476 1.00 10.32 O ANISOU 4572 O GLY B 156 1255 1243 1423 157 -41 -13 O ATOM 4573 N TRP B 157 41.615 19.481 -4.006 1.00 9.61 N ANISOU 4573 N TRP B 157 1041 1362 1250 -140 -52 -40 N ATOM 4574 CA TRP B 157 41.224 18.481 -4.993 1.00 10.94 C ANISOU 4574 CA TRP B 157 1351 1433 1371 -16 -38 -134 C ATOM 4575 C TRP B 157 42.415 17.698 -5.546 1.00 10.46 C ANISOU 4575 C TRP B 157 1318 1187 1471 -81 0 1 C ATOM 4576 O TRP B 157 42.370 16.473 -5.697 1.00 10.06 O ANISOU 4576 O TRP B 157 1372 1122 1328 -282 -50 -151 O ATOM 4577 CB TRP B 157 40.497 19.139 -6.172 1.00 11.03 C ANISOU 4577 CB TRP B 157 1325 1378 1488 -40 -120 -11 C ATOM 4578 CG TRP B 157 39.343 20.046 -5.813 1.00 11.78 C ANISOU 4578 CG TRP B 157 1358 1538 1579 -84 -103 -189 C ATOM 4579 CD1 TRP B 157 38.647 20.118 -4.640 1.00 13.10 C ANISOU 4579 CD1 TRP B 157 1432 1840 1704 -16 -67 -148 C ATOM 4580 CD2 TRP B 157 38.735 20.985 -6.713 1.00 12.86 C ANISOU 4580 CD2 TRP B 157 1524 1643 1721 -28 -133 -96 C ATOM 4581 NE1 TRP B 157 37.635 21.083 -4.769 1.00 14.42 N ANISOU 4581 NE1 TRP B 157 1694 1896 1887 110 -16 -84 N ATOM 4582 CE2 TRP B 157 37.663 21.590 -6.032 1.00 14.15 C ANISOU 4582 CE2 TRP B 157 1690 1852 1836 60 -48 -55 C ATOM 4583 CE3 TRP B 157 38.970 21.322 -8.054 1.00 12.58 C ANISOU 4583 CE3 TRP B 157 1412 1504 1865 -224 -55 130 C ATOM 4584 CZ2 TRP B 157 36.856 22.587 -6.620 1.00 14.65 C ANISOU 4584 CZ2 TRP B 157 1793 1783 1989 23 -17 -21 C ATOM 4585 CZ3 TRP B 157 38.160 22.295 -8.640 1.00 13.90 C ANISOU 4585 CZ3 TRP B 157 1631 1454 2197 -67 -33 -26 C ATOM 4586 CH2 TRP B 157 37.115 22.910 -7.932 1.00 14.36 C ANISOU 4586 CH2 TRP B 157 1724 1702 2029 -44 10 17 C ATOM 4587 N TYR B 158 43.482 18.435 -5.899 1.00 10.17 N ANISOU 4587 N TYR B 158 1175 1232 1457 -105 48 -48 N ATOM 4588 CA TYR B 158 44.740 17.796 -6.267 1.00 10.00 C ANISOU 4588 CA TYR B 158 1115 1182 1503 -101 -26 73 C ATOM 4589 C TYR B 158 45.206 16.784 -5.232 1.00 9.90 C ANISOU 4589 C TYR B 158 1213 1219 1331 -108 56 32 C ATOM 4590 O TYR B 158 45.588 15.654 -5.601 1.00 10.51 O ANISOU 4590 O TYR B 158 1198 1252 1544 -58 47 19 O ATOM 4591 CB TYR B 158 45.839 18.882 -6.454 1.00 9.18 C ANISOU 4591 CB TYR B 158 991 1143 1355 -84 -127 82 C ATOM 4592 CG TYR B 158 47.187 18.281 -6.801 1.00 10.46 C ANISOU 4592 CG TYR B 158 1265 1168 1542 -29 44 55 C ATOM 4593 CD1 TYR B 158 47.515 17.805 -8.056 1.00 11.37 C ANISOU 4593 CD1 TYR B 158 1440 1333 1546 12 123 65 C ATOM 4594 CD2 TYR B 158 48.156 18.243 -5.795 1.00 11.33 C ANISOU 4594 CD2 TYR B 158 1326 1272 1705 -68 -61 96 C ATOM 4595 CE1 TYR B 158 48.790 17.257 -8.274 1.00 12.40 C ANISOU 4595 CE1 TYR B 158 1364 1543 1805 5 25 128 C ATOM 4596 CE2 TYR B 158 49.419 17.730 -6.013 1.00 12.23 C ANISOU 4596 CE2 TYR B 158 1394 1490 1762 14 19 23 C ATOM 4597 CZ TYR B 158 49.722 17.259 -7.258 1.00 13.27 C ANISOU 4597 CZ TYR B 158 1522 1665 1857 3 3 -61 C ATOM 4598 OH TYR B 158 50.987 16.724 -7.504 1.00 15.49 O ANISOU 4598 OH TYR B 158 1367 2110 2409 -42 -55 -251 O ATOM 4599 N SER B 159 45.227 17.177 -3.954 1.00 8.69 N ANISOU 4599 N SER B 159 915 1114 1273 -91 -88 34 N ATOM 4600 CA SER B 159 45.726 16.287 -2.910 1.00 9.60 C ANISOU 4600 CA SER B 159 1247 1168 1234 -199 -47 34 C ATOM 4601 C SER B 159 44.899 14.993 -2.855 1.00 9.76 C ANISOU 4601 C SER B 159 1252 1078 1379 -84 -21 3 C ATOM 4602 O SER B 159 45.466 13.905 -2.728 1.00 9.27 O ANISOU 4602 O SER B 159 1397 1012 1114 -57 76 -19 O ATOM 4603 CB SER B 159 45.623 17.086 -1.599 1.00 10.01 C ANISOU 4603 CB SER B 159 1349 1280 1174 -120 -127 -19 C ATOM 4604 OG SER B 159 46.313 16.327 -0.588 1.00 11.99 O ANISOU 4604 OG SER B 159 1773 1319 1464 16 -122 101 O ATOM 4605 N GLU B 160 43.582 15.145 -2.963 1.00 9.63 N ANISOU 4605 N GLU B 160 1168 1217 1272 -183 20 -28 N ATOM 4606 CA GLU B 160 42.699 13.967 -2.995 1.00 9.90 C ANISOU 4606 CA GLU B 160 1187 1173 1403 -187 -18 -59 C ATOM 4607 C GLU B 160 42.964 13.081 -4.206 1.00 10.36 C ANISOU 4607 C GLU B 160 1225 1218 1494 -37 18 -42 C ATOM 4608 O GLU B 160 43.018 11.824 -4.051 1.00 10.56 O ANISOU 4608 O GLU B 160 1150 1134 1730 -5 -79 -210 O ATOM 4609 CB GLU B 160 41.238 14.440 -2.971 1.00 10.94 C ANISOU 4609 CB GLU B 160 1250 1377 1530 -106 23 -107 C ATOM 4610 CG GLU B 160 40.231 13.279 -2.871 1.00 12.31 C ANISOU 4610 CG GLU B 160 1519 1388 1770 -230 48 64 C ATOM 4611 CD GLU B 160 38.830 13.675 -2.449 1.00 16.82 C ANISOU 4611 CD GLU B 160 1707 2168 2514 -67 38 60 C ATOM 4612 OE1 GLU B 160 38.494 14.896 -2.421 1.00 19.31 O ANISOU 4612 OE1 GLU B 160 2103 2266 2969 -66 62 36 O ATOM 4613 OE2 GLU B 160 37.959 12.795 -2.095 1.00 17.18 O ANISOU 4613 OE2 GLU B 160 1990 2255 2283 -175 30 221 O ATOM 4614 N MET B 161 43.085 13.646 -5.403 1.00 10.33 N ANISOU 4614 N MET B 161 1223 1176 1527 -42 43 -50 N ATOM 4615 CA MET B 161 43.329 12.826 -6.598 1.00 9.53 C ANISOU 4615 CA MET B 161 1049 1320 1253 -70 1 32 C ATOM 4616 C MET B 161 44.715 12.190 -6.509 1.00 9.45 C ANISOU 4616 C MET B 161 1056 1276 1258 -64 45 77 C ATOM 4617 O MET B 161 44.908 11.065 -6.992 1.00 10.42 O ANISOU 4617 O MET B 161 1265 1247 1446 -145 56 67 O ATOM 4618 CB MET B 161 43.061 13.559 -7.916 1.00 8.61 C ANISOU 4618 CB MET B 161 626 1240 1404 -173 -1 169 C ATOM 4619 CG MET B 161 41.582 13.958 -8.084 1.00 9.39 C ANISOU 4619 CG MET B 161 850 1284 1433 -154 -97 40 C ATOM 4620 SD MET B 161 40.464 12.461 -8.142 1.00 4.27 S ANISOU 4620 SD MET B 161 542 778 303 -142 -63 -76 S ATOM 4621 CE MET B 161 39.371 12.872 -6.840 1.00 8.39 C ANISOU 4621 CE MET B 161 1573 1327 290 -94 -166 -115 C ATOM 4622 N LYS B 162 45.724 12.850 -5.921 1.00 9.34 N ANISOU 4622 N LYS B 162 1137 1224 1188 -26 -24 -6 N ATOM 4623 CA LYS B 162 47.025 12.180 -5.697 1.00 11.46 C ANISOU 4623 CA LYS B 162 1343 1402 1609 53 -49 86 C ATOM 4624 C LYS B 162 46.901 11.021 -4.711 1.00 10.41 C ANISOU 4624 C LYS B 162 1240 1297 1418 4 -48 -10 C ATOM 4625 O LYS B 162 47.531 9.974 -4.959 1.00 10.92 O ANISOU 4625 O LYS B 162 1192 1419 1538 72 49 62 O ATOM 4626 CB LYS B 162 48.040 13.200 -5.140 1.00 14.64 C ANISOU 4626 CB LYS B 162 1682 1824 2055 -150 -35 -194 C ATOM 4627 CG LYS B 162 48.430 14.196 -6.232 1.00 19.38 C ANISOU 4627 CG LYS B 162 2475 2379 2511 -79 24 163 C ATOM 4628 CD LYS B 162 49.439 13.591 -7.221 1.00 23.79 C ANISOU 4628 CD LYS B 162 2932 3080 3028 84 250 -65 C ATOM 4629 CE LYS B 162 50.861 13.678 -6.654 1.00 26.80 C ANISOU 4629 CE LYS B 162 3151 3504 3529 40 8 26 C ATOM 4630 NZ LYS B 162 51.776 13.083 -7.703 1.00 29.15 N ANISOU 4630 NZ LYS B 162 3530 3811 3736 64 194 -39 N ATOM 4631 N ARG B 163 46.069 11.101 -3.666 1.00 9.93 N ANISOU 4631 N ARG B 163 1322 1249 1201 -64 -149 -18 N ATOM 4632 CA ARG B 163 45.825 9.942 -2.805 1.00 10.31 C ANISOU 4632 CA ARG B 163 1360 1277 1280 -90 41 -47 C ATOM 4633 C ARG B 163 45.197 8.826 -3.649 1.00 10.49 C ANISOU 4633 C ARG B 163 1273 1296 1417 -65 0 -48 C ATOM 4634 O ARG B 163 45.525 7.628 -3.467 1.00 11.16 O ANISOU 4634 O ARG B 163 1343 1327 1572 -35 -61 9 O ATOM 4635 CB ARG B 163 44.924 10.232 -1.597 1.00 10.37 C ANISOU 4635 CB ARG B 163 1434 1279 1229 -56 21 -115 C ATOM 4636 CG ARG B 163 45.557 11.217 -0.563 1.00 11.43 C ANISOU 4636 CG ARG B 163 1427 1586 1329 -122 -66 -134 C ATOM 4637 CD ARG B 163 44.674 11.278 0.659 1.00 11.97 C ANISOU 4637 CD ARG B 163 1469 1681 1400 20 -41 -119 C ATOM 4638 NE ARG B 163 43.405 12.045 0.551 1.00 11.37 N ANISOU 4638 NE ARG B 163 1427 1404 1489 -39 109 -58 N ATOM 4639 CZ ARG B 163 43.241 13.364 0.517 1.00 12.31 C ANISOU 4639 CZ ARG B 163 1505 1446 1727 -76 11 -72 C ATOM 4640 NH1 ARG B 163 42.023 13.918 0.439 1.00 11.56 N ANISOU 4640 NH1 ARG B 163 1584 1487 1322 -37 34 -116 N ATOM 4641 NH2 ARG B 163 44.328 14.183 0.570 1.00 11.47 N ANISOU 4641 NH2 ARG B 163 1549 1287 1522 -111 -86 -152 N ATOM 4642 N ASN B 164 44.301 9.222 -4.564 1.00 10.19 N ANISOU 4642 N ASN B 164 1242 1323 1308 -95 36 -23 N ATOM 4643 CA ASN B 164 43.601 8.210 -5.377 1.00 10.27 C ANISOU 4643 CA ASN B 164 1324 1256 1322 45 -38 -65 C ATOM 4644 C ASN B 164 44.535 7.589 -6.399 1.00 10.30 C ANISOU 4644 C ASN B 164 1222 1207 1483 -37 60 53 C ATOM 4645 O ASN B 164 44.362 6.391 -6.698 1.00 10.17 O ANISOU 4645 O ASN B 164 1401 1148 1317 -91 80 -130 O ATOM 4646 CB ASN B 164 42.397 8.843 -6.068 1.00 10.09 C ANISOU 4646 CB ASN B 164 1101 1326 1408 -76 1 -74 C ATOM 4647 CG ASN B 164 41.246 9.065 -5.097 1.00 10.60 C ANISOU 4647 CG ASN B 164 1181 1432 1415 -23 -21 -87 C ATOM 4648 OD1 ASN B 164 41.111 8.201 -4.226 1.00 11.99 O ANISOU 4648 OD1 ASN B 164 1287 1744 1525 -101 52 -30 O ATOM 4649 ND2 ASN B 164 40.467 10.104 -5.278 1.00 10.33 N ANISOU 4649 ND2 ASN B 164 1025 1315 1585 -92 89 -207 N ATOM 4650 N VAL B 165 45.551 8.289 -6.925 1.00 9.87 N ANISOU 4650 N VAL B 165 1084 1161 1505 -36 54 172 N ATOM 4651 CA VAL B 165 46.575 7.599 -7.719 1.00 10.55 C ANISOU 4651 CA VAL B 165 1208 1197 1603 -59 138 75 C ATOM 4652 C VAL B 165 47.189 6.482 -6.921 1.00 10.53 C ANISOU 4652 C VAL B 165 1201 1305 1495 -53 61 31 C ATOM 4653 O VAL B 165 47.329 5.326 -7.422 1.00 10.86 O ANISOU 4653 O VAL B 165 1215 1224 1685 -75 -23 -47 O ATOM 4654 CB VAL B 165 47.686 8.631 -8.155 1.00 10.64 C ANISOU 4654 CB VAL B 165 1096 1318 1628 20 194 154 C ATOM 4655 CG1 VAL B 165 48.890 7.884 -8.734 1.00 11.78 C ANISOU 4655 CG1 VAL B 165 1211 1358 1908 61 198 12 C ATOM 4656 CG2 VAL B 165 47.043 9.546 -9.194 1.00 11.61 C ANISOU 4656 CG2 VAL B 165 1527 1300 1582 19 144 133 C ATOM 4657 N GLN B 166 47.598 6.756 -5.667 1.00 10.47 N ANISOU 4657 N GLN B 166 1217 1298 1464 -174 99 -48 N ATOM 4658 CA GLN B 166 48.296 5.668 -4.916 1.00 13.02 C ANISOU 4658 CA GLN B 166 1533 1494 1920 -99 14 133 C ATOM 4659 C GLN B 166 47.316 4.526 -4.637 1.00 11.96 C ANISOU 4659 C GLN B 166 1390 1441 1712 -54 38 -7 C ATOM 4660 O GLN B 166 47.651 3.335 -4.691 1.00 11.70 O ANISOU 4660 O GLN B 166 1139 1453 1853 -34 -38 77 O ATOM 4661 CB GLN B 166 48.823 6.234 -3.593 1.00 16.98 C ANISOU 4661 CB GLN B 166 2202 2138 2112 28 -133 -81 C ATOM 4662 CG GLN B 166 49.907 7.307 -3.875 1.00 23.12 C ANISOU 4662 CG GLN B 166 2829 2826 3130 -317 -51 88 C ATOM 4663 CD GLN B 166 51.093 6.749 -4.642 1.00 26.87 C ANISOU 4663 CD GLN B 166 3180 3457 3573 -11 54 -41 C ATOM 4664 OE1 GLN B 166 51.437 7.200 -5.749 1.00 29.69 O ANISOU 4664 OE1 GLN B 166 3683 3852 3748 -58 71 105 O ATOM 4665 NE2 GLN B 166 51.726 5.708 -4.099 1.00 28.75 N ANISOU 4665 NE2 GLN B 166 3498 3588 3837 47 -50 37 N ATOM 4666 N ARG B 167 46.075 4.868 -4.320 1.00 10.21 N ANISOU 4666 N ARG B 167 1233 1138 1507 -103 -34 -41 N ATOM 4667 CA ARG B 167 45.071 3.812 -4.048 1.00 10.35 C ANISOU 4667 CA ARG B 167 1108 1303 1521 -32 126 -57 C ATOM 4668 C ARG B 167 44.834 2.956 -5.278 1.00 10.23 C ANISOU 4668 C ARG B 167 1120 1270 1498 -70 12 -16 C ATOM 4669 O ARG B 167 44.641 1.724 -5.189 1.00 10.30 O ANISOU 4669 O ARG B 167 1182 1253 1480 10 124 76 O ATOM 4670 CB ARG B 167 43.761 4.447 -3.584 1.00 9.93 C ANISOU 4670 CB ARG B 167 1163 1259 1351 41 105 -65 C ATOM 4671 CG ARG B 167 43.887 5.086 -2.169 1.00 9.45 C ANISOU 4671 CG ARG B 167 1059 1220 1310 -7 9 -80 C ATOM 4672 CD ARG B 167 42.618 5.988 -2.006 1.00 10.17 C ANISOU 4672 CD ARG B 167 1238 1324 1300 87 45 -98 C ATOM 4673 NE ARG B 167 42.758 6.625 -0.665 1.00 11.91 N ANISOU 4673 NE ARG B 167 1618 1560 1347 94 110 -117 N ATOM 4674 CZ ARG B 167 42.107 7.760 -0.394 1.00 11.95 C ANISOU 4674 CZ ARG B 167 1621 1444 1478 20 77 -33 C ATOM 4675 NH1 ARG B 167 41.360 8.402 -1.298 1.00 11.41 N ANISOU 4675 NH1 ARG B 167 1335 1371 1628 120 53 -123 N ATOM 4676 NH2 ARG B 167 42.265 8.260 0.821 1.00 12.73 N ANISOU 4676 NH2 ARG B 167 1709 1634 1492 -81 48 -25 N ATOM 4677 N LEU B 168 44.706 3.563 -6.453 1.00 10.14 N ANISOU 4677 N LEU B 168 1048 1363 1440 -143 -2 7 N ATOM 4678 CA LEU B 168 44.473 2.806 -7.691 1.00 11.88 C ANISOU 4678 CA LEU B 168 1347 1558 1610 4 7 -118 C ATOM 4679 C LEU B 168 45.719 1.986 -8.026 1.00 11.15 C ANISOU 4679 C LEU B 168 1263 1383 1589 -10 -23 15 C ATOM 4680 O LEU B 168 45.531 0.871 -8.475 1.00 11.46 O ANISOU 4680 O LEU B 168 1216 1536 1601 11 15 -64 O ATOM 4681 CB LEU B 168 44.207 3.766 -8.848 1.00 14.58 C ANISOU 4681 CB LEU B 168 1725 1850 1965 -124 -35 199 C ATOM 4682 CG LEU B 168 43.852 3.209 -10.216 1.00 17.80 C ANISOU 4682 CG LEU B 168 2324 2276 2164 -152 -97 50 C ATOM 4683 CD1 LEU B 168 42.701 2.202 -10.108 1.00 18.90 C ANISOU 4683 CD1 LEU B 168 2348 2449 2384 -219 -172 117 C ATOM 4684 CD2 LEU B 168 43.414 4.348 -11.166 1.00 19.23 C ANISOU 4684 CD2 LEU B 168 2395 2403 2507 -115 -41 244 C ATOM 4685 N GLU B 169 46.945 2.478 -7.808 1.00 10.35 N ANISOU 4685 N GLU B 169 1134 1374 1424 27 13 -5 N ATOM 4686 CA GLU B 169 48.084 1.530 -7.979 1.00 11.54 C ANISOU 4686 CA GLU B 169 1424 1381 1579 94 39 57 C ATOM 4687 C GLU B 169 47.937 0.334 -7.056 1.00 11.70 C ANISOU 4687 C GLU B 169 1519 1439 1487 -8 31 15 C ATOM 4688 O GLU B 169 48.271 -0.771 -7.499 1.00 12.40 O ANISOU 4688 O GLU B 169 1552 1539 1620 1 79 -106 O ATOM 4689 CB GLU B 169 49.400 2.272 -7.712 1.00 13.66 C ANISOU 4689 CB GLU B 169 1479 1705 2007 -38 38 56 C ATOM 4690 CG GLU B 169 49.592 3.335 -8.824 1.00 17.14 C ANISOU 4690 CG GLU B 169 2221 2194 2097 -29 59 233 C ATOM 4691 CD GLU B 169 50.725 4.296 -8.542 1.00 21.67 C ANISOU 4691 CD GLU B 169 2598 2745 2889 -242 -35 105 C ATOM 4692 OE1 GLU B 169 51.160 4.383 -7.372 1.00 23.68 O ANISOU 4692 OE1 GLU B 169 2747 3131 3119 -330 -230 -15 O ATOM 4693 OE2 GLU B 169 51.180 5.028 -9.450 1.00 23.50 O ANISOU 4693 OE2 GLU B 169 2663 3067 3198 -297 215 220 O ATOM 4694 N ARG B 170 47.540 0.516 -5.793 1.00 10.57 N ANISOU 4694 N ARG B 170 1124 1468 1424 -41 4 6 N ATOM 4695 CA ARG B 170 47.354 -0.662 -4.939 1.00 11.62 C ANISOU 4695 CA ARG B 170 1398 1443 1576 -19 -98 46 C ATOM 4696 C ARG B 170 46.231 -1.576 -5.390 1.00 10.77 C ANISOU 4696 C ARG B 170 1281 1399 1411 20 60 19 C ATOM 4697 O ARG B 170 46.359 -2.816 -5.301 1.00 10.52 O ANISOU 4697 O ARG B 170 1142 1339 1516 50 22 -23 O ATOM 4698 CB ARG B 170 47.147 -0.245 -3.460 1.00 14.06 C ANISOU 4698 CB ARG B 170 1861 1856 1624 260 136 41 C ATOM 4699 CG ARG B 170 48.509 0.314 -3.021 1.00 21.19 C ANISOU 4699 CG ARG B 170 2473 2652 2927 -201 -57 -32 C ATOM 4700 CD ARG B 170 48.693 0.563 -1.549 1.00 26.38 C ANISOU 4700 CD ARG B 170 3479 3486 3060 -111 -47 -30 C ATOM 4701 NE ARG B 170 48.092 1.839 -1.178 1.00 30.20 N ANISOU 4701 NE ARG B 170 3896 3648 3930 79 20 -19 N ATOM 4702 CZ ARG B 170 48.698 3.023 -1.244 1.00 31.84 C ANISOU 4702 CZ ARG B 170 4076 3864 4157 -73 13 -42 C ATOM 4703 NH1 ARG B 170 49.972 3.133 -1.637 1.00 31.18 N ANISOU 4703 NH1 ARG B 170 4052 3801 3994 -96 33 -26 N ATOM 4704 NH2 ARG B 170 47.991 4.110 -0.895 1.00 32.43 N ANISOU 4704 NH2 ARG B 170 4242 3861 4219 6 16 -10 N ATOM 4705 N ALA B 171 45.149 -0.998 -5.912 1.00 10.70 N ANISOU 4705 N ALA B 171 1246 1437 1384 -47 -57 -63 N ATOM 4706 CA ALA B 171 44.043 -1.869 -6.386 1.00 10.09 C ANISOU 4706 CA ALA B 171 1201 1213 1421 -8 -20 -36 C ATOM 4707 C ALA B 171 44.476 -2.634 -7.624 1.00 9.81 C ANISOU 4707 C ALA B 171 1251 1113 1364 30 9 24 C ATOM 4708 O ALA B 171 44.083 -3.796 -7.816 1.00 9.27 O ANISOU 4708 O ALA B 171 1169 1131 1223 -7 66 -105 O ATOM 4709 CB ALA B 171 42.839 -0.975 -6.709 1.00 10.39 C ANISOU 4709 CB ALA B 171 1140 1195 1614 -42 -59 -36 C ATOM 4710 N ILE B 172 45.280 -2.048 -8.528 1.00 9.54 N ANISOU 4710 N ILE B 172 1290 1178 1157 143 38 -21 N ATOM 4711 CA ILE B 172 45.801 -2.820 -9.675 1.00 9.97 C ANISOU 4711 CA ILE B 172 1402 1183 1202 171 73 31 C ATOM 4712 C ILE B 172 46.649 -3.993 -9.185 1.00 10.29 C ANISOU 4712 C ILE B 172 1339 1232 1338 85 53 80 C ATOM 4713 O ILE B 172 46.508 -5.125 -9.725 1.00 11.17 O ANISOU 4713 O ILE B 172 1399 1460 1385 -84 12 -66 O ATOM 4714 CB ILE B 172 46.641 -1.891 -10.576 1.00 10.52 C ANISOU 4714 CB ILE B 172 1453 1297 1246 165 108 58 C ATOM 4715 CG1 ILE B 172 45.675 -0.913 -11.297 1.00 10.91 C ANISOU 4715 CG1 ILE B 172 1490 1365 1292 87 14 129 C ATOM 4716 CG2 ILE B 172 47.420 -2.722 -11.614 1.00 11.33 C ANISOU 4716 CG2 ILE B 172 1675 1457 1174 220 114 28 C ATOM 4717 CD1 ILE B 172 46.454 0.309 -11.865 1.00 12.84 C ANISOU 4717 CD1 ILE B 172 1910 1410 1556 -68 27 99 C ATOM 4718 N GLU B 173 47.481 -3.749 -8.182 1.00 10.95 N ANISOU 4718 N GLU B 173 1369 1440 1353 -112 9 136 N ATOM 4719 CA GLU B 173 48.295 -4.864 -7.642 1.00 13.44 C ANISOU 4719 CA GLU B 173 1698 1587 1823 110 102 179 C ATOM 4720 C GLU B 173 47.385 -5.942 -7.089 1.00 12.20 C ANISOU 4720 C GLU B 173 1636 1447 1553 48 2 2 C ATOM 4721 O GLU B 173 47.620 -7.128 -7.321 1.00 11.70 O ANISOU 4721 O GLU B 173 1483 1430 1531 174 130 175 O ATOM 4722 CB GLU B 173 49.267 -4.413 -6.516 1.00 18.49 C ANISOU 4722 CB GLU B 173 2329 2460 2237 113 -174 -163 C ATOM 4723 CG GLU B 173 50.291 -3.450 -7.090 1.00 25.90 C ANISOU 4723 CG GLU B 173 3142 3248 3449 -137 198 191 C ATOM 4724 CD GLU B 173 51.126 -2.628 -6.150 1.00 32.06 C ANISOU 4724 CD GLU B 173 3989 4171 4023 -180 -162 -139 C ATOM 4725 OE1 GLU B 173 50.806 -2.435 -4.941 1.00 34.62 O ANISOU 4725 OE1 GLU B 173 4260 4665 4228 -18 107 -123 O ATOM 4726 OE2 GLU B 173 52.177 -2.100 -6.635 1.00 35.92 O ANISOU 4726 OE2 GLU B 173 4239 4820 4591 -267 108 4 O ATOM 4727 N GLU B 174 46.325 -5.593 -6.359 1.00 12.51 N ANISOU 4727 N GLU B 174 1602 1548 1603 -16 71 127 N ATOM 4728 CA GLU B 174 45.435 -6.585 -5.752 1.00 12.44 C ANISOU 4728 CA GLU B 174 1565 1521 1640 -99 63 -28 C ATOM 4729 C GLU B 174 44.753 -7.455 -6.794 1.00 11.30 C ANISOU 4729 C GLU B 174 1428 1345 1522 73 86 -11 C ATOM 4730 O GLU B 174 44.490 -8.632 -6.486 1.00 11.25 O ANISOU 4730 O GLU B 174 1285 1236 1754 22 110 -28 O ATOM 4731 CB GLU B 174 44.276 -5.885 -4.984 1.00 14.58 C ANISOU 4731 CB GLU B 174 1777 1839 1925 65 157 -56 C ATOM 4732 CG GLU B 174 44.739 -5.260 -3.692 1.00 18.10 C ANISOU 4732 CG GLU B 174 2509 2287 2082 -148 111 -129 C ATOM 4733 CD GLU B 174 44.334 -6.076 -2.464 1.00 21.59 C ANISOU 4733 CD GLU B 174 3245 2600 2360 -169 93 83 C ATOM 4734 OE1 GLU B 174 43.772 -7.185 -2.724 1.00 26.35 O ANISOU 4734 OE1 GLU B 174 3787 2933 3293 -508 96 -85 O ATOM 4735 OE2 GLU B 174 44.533 -5.643 -1.341 1.00 19.47 O ANISOU 4735 OE2 GLU B 174 2944 2257 2198 -176 64 142 O ATOM 4736 N VAL B 175 44.488 -6.907 -7.984 1.00 10.46 N ANISOU 4736 N VAL B 175 1334 1232 1410 211 108 -69 N ATOM 4737 CA VAL B 175 43.789 -7.740 -8.996 1.00 11.81 C ANISOU 4737 CA VAL B 175 1506 1517 1465 92 55 -52 C ATOM 4738 C VAL B 175 44.762 -8.360 -9.996 1.00 12.05 C ANISOU 4738 C VAL B 175 1517 1543 1520 151 -42 -174 C ATOM 4739 O VAL B 175 44.324 -9.021 -10.949 1.00 12.44 O ANISOU 4739 O VAL B 175 1594 1470 1663 240 8 -424 O ATOM 4740 CB VAL B 175 42.657 -7.021 -9.770 1.00 12.08 C ANISOU 4740 CB VAL B 175 1511 1592 1486 54 84 34 C ATOM 4741 CG1 VAL B 175 41.596 -6.670 -8.749 1.00 12.94 C ANISOU 4741 CG1 VAL B 175 1611 1646 1660 202 111 70 C ATOM 4742 CG2 VAL B 175 43.144 -5.817 -10.563 1.00 11.26 C ANISOU 4742 CG2 VAL B 175 1546 1241 1491 32 -44 -71 C ATOM 4743 N SER B 176 46.069 -8.261 -9.786 1.00 11.70 N ANISOU 4743 N SER B 176 1443 1420 1582 11 13 -103 N ATOM 4744 CA SER B 176 47.084 -8.816 -10.668 1.00 12.15 C ANISOU 4744 CA SER B 176 1538 1401 1678 114 55 -114 C ATOM 4745 C SER B 176 47.361 -10.304 -10.445 1.00 12.94 C ANISOU 4745 C SER B 176 1709 1420 1789 -7 47 169 C ATOM 4746 O SER B 176 48.545 -10.722 -10.528 1.00 14.31 O ANISOU 4746 O SER B 176 1929 1337 2169 138 350 159 O ATOM 4747 CB SER B 176 48.425 -8.049 -10.436 1.00 13.66 C ANISOU 4747 CB SER B 176 1535 1580 2076 -14 280 -88 C ATOM 4748 OG SER B 176 48.205 -6.753 -11.049 1.00 17.25 O ANISOU 4748 OG SER B 176 2076 2148 2328 12 -38 129 O ATOM 4749 N TYR B 177 46.394 -11.049 -9.984 1.00 12.52 N ANISOU 4749 N TYR B 177 1648 1294 1815 9 35 -32 N ATOM 4750 CA TYR B 177 46.528 -12.458 -9.598 1.00 12.24 C ANISOU 4750 CA TYR B 177 1694 1380 1577 30 -64 5 C ATOM 4751 C TYR B 177 45.566 -13.251 -10.482 1.00 12.69 C ANISOU 4751 C TYR B 177 1646 1344 1831 48 -72 -109 C ATOM 4752 O TYR B 177 44.373 -12.864 -10.638 1.00 14.66 O ANISOU 4752 O TYR B 177 1814 1560 2198 187 -173 -169 O ATOM 4753 CB TYR B 177 46.144 -12.629 -8.122 1.00 12.53 C ANISOU 4753 CB TYR B 177 1715 1406 1639 41 -38 24 C ATOM 4754 CG TYR B 177 47.250 -12.103 -7.227 1.00 12.50 C ANISOU 4754 CG TYR B 177 1712 1570 1466 11 9 5 C ATOM 4755 CD1 TYR B 177 47.304 -10.728 -6.897 1.00 13.55 C ANISOU 4755 CD1 TYR B 177 1817 1621 1710 64 -1 -55 C ATOM 4756 CD2 TYR B 177 48.194 -12.962 -6.709 1.00 12.91 C ANISOU 4756 CD2 TYR B 177 1546 1608 1751 47 78 -5 C ATOM 4757 CE1 TYR B 177 48.319 -10.250 -6.094 1.00 14.36 C ANISOU 4757 CE1 TYR B 177 1703 1860 1893 95 16 -151 C ATOM 4758 CE2 TYR B 177 49.201 -12.490 -5.868 1.00 14.31 C ANISOU 4758 CE2 TYR B 177 1815 1896 1724 100 -14 -107 C ATOM 4759 CZ TYR B 177 49.247 -11.148 -5.599 1.00 15.30 C ANISOU 4759 CZ TYR B 177 1910 1932 1970 4 -73 -26 C ATOM 4760 OH TYR B 177 50.228 -10.653 -4.773 1.00 17.55 O ANISOU 4760 OH TYR B 177 1935 2463 2271 162 -260 -254 O ATOM 4761 N GLY B 178 46.090 -14.300 -11.104 1.00 10.74 N ANISOU 4761 N GLY B 178 1392 1320 1368 48 -209 -90 N ATOM 4762 CA GLY B 178 45.216 -15.209 -11.843 1.00 9.75 C ANISOU 4762 CA GLY B 178 1181 1060 1464 -15 -181 87 C ATOM 4763 C GLY B 178 45.313 -16.608 -11.213 1.00 9.97 C ANISOU 4763 C GLY B 178 1220 1168 1401 38 -85 76 C ATOM 4764 O GLY B 178 45.891 -16.783 -10.122 1.00 10.39 O ANISOU 4764 O GLY B 178 1472 1287 1189 102 -46 15 O ATOM 4765 N LYS B 179 44.706 -17.563 -11.881 1.00 10.45 N ANISOU 4765 N LYS B 179 1284 1239 1446 -63 95 -33 N ATOM 4766 CA LYS B 179 44.768 -18.930 -11.330 1.00 11.58 C ANISOU 4766 CA LYS B 179 1510 1336 1554 180 29 24 C ATOM 4767 C LYS B 179 44.749 -19.885 -12.520 1.00 11.80 C ANISOU 4767 C LYS B 179 1531 1415 1537 101 -47 -15 C ATOM 4768 O LYS B 179 44.029 -19.666 -13.497 1.00 12.25 O ANISOU 4768 O LYS B 179 1675 1361 1620 249 -88 -99 O ATOM 4769 CB LYS B 179 43.621 -19.253 -10.353 1.00 13.32 C ANISOU 4769 CB LYS B 179 1527 1787 1747 -45 25 18 C ATOM 4770 CG LYS B 179 42.289 -19.409 -11.089 1.00 14.50 C ANISOU 4770 CG LYS B 179 1537 1948 2024 30 -37 55 C ATOM 4771 CD LYS B 179 41.146 -19.897 -10.222 1.00 15.57 C ANISOU 4771 CD LYS B 179 1846 1972 2098 6 83 143 C ATOM 4772 CE LYS B 179 41.374 -21.285 -9.651 1.00 15.48 C ANISOU 4772 CE LYS B 179 1991 1813 2077 -48 -38 -4 C ATOM 4773 NZ LYS B 179 40.859 -22.429 -10.458 1.00 14.18 N ANISOU 4773 NZ LYS B 179 1648 1803 1935 35 112 -99 N ATOM 4774 N ILE B 180 45.601 -20.887 -12.462 1.00 10.79 N ANISOU 4774 N ILE B 180 1402 1259 1439 85 149 6 N ATOM 4775 CA ILE B 180 45.638 -21.993 -13.407 1.00 11.82 C ANISOU 4775 CA ILE B 180 1678 1310 1501 -11 32 6 C ATOM 4776 C ILE B 180 45.842 -23.253 -12.543 1.00 12.15 C ANISOU 4776 C ILE B 180 1702 1439 1475 40 22 56 C ATOM 4777 O ILE B 180 46.925 -23.854 -12.495 1.00 14.17 O ANISOU 4777 O ILE B 180 1793 1718 1873 16 74 104 O ATOM 4778 CB ILE B 180 46.765 -21.869 -14.434 1.00 13.02 C ANISOU 4778 CB ILE B 180 1786 1535 1627 54 60 9 C ATOM 4779 CG1 ILE B 180 46.930 -20.545 -15.168 1.00 13.60 C ANISOU 4779 CG1 ILE B 180 1819 1538 1809 -25 9 63 C ATOM 4780 CG2 ILE B 180 46.629 -22.998 -15.450 1.00 13.81 C ANISOU 4780 CG2 ILE B 180 2070 1611 1566 66 88 -53 C ATOM 4781 CD1 ILE B 180 45.876 -20.140 -16.195 1.00 14.93 C ANISOU 4781 CD1 ILE B 180 1947 1798 1930 147 -24 -12 C ATOM 4782 N SER B 181 44.809 -23.630 -11.802 1.00 11.21 N ANISOU 4782 N SER B 181 1618 1264 1378 58 -33 1 N ATOM 4783 CA SER B 181 44.965 -24.568 -10.691 1.00 11.20 C ANISOU 4783 CA SER B 181 1603 1370 1282 39 -39 -33 C ATOM 4784 C SER B 181 43.952 -25.690 -10.778 1.00 11.59 C ANISOU 4784 C SER B 181 1535 1401 1466 62 55 -32 C ATOM 4785 O SER B 181 43.993 -26.644 -9.967 1.00 12.44 O ANISOU 4785 O SER B 181 1623 1432 1673 83 -52 70 O ATOM 4786 CB SER B 181 44.889 -23.880 -9.313 1.00 10.69 C ANISOU 4786 CB SER B 181 1408 1351 1303 178 -54 -106 C ATOM 4787 OG SER B 181 43.630 -23.199 -9.181 1.00 11.75 O ANISOU 4787 OG SER B 181 1536 1478 1453 218 -62 -161 O ATOM 4788 N GLY B 182 43.084 -25.636 -11.771 1.00 11.10 N ANISOU 4788 N GLY B 182 1379 1190 1648 106 -4 -104 N ATOM 4789 CA GLY B 182 42.117 -26.682 -12.018 1.00 12.16 C ANISOU 4789 CA GLY B 182 1368 1409 1842 -29 73 47 C ATOM 4790 C GLY B 182 40.939 -26.663 -11.039 1.00 11.88 C ANISOU 4790 C GLY B 182 1429 1469 1617 4 1 -8 C ATOM 4791 O GLY B 182 40.636 -25.723 -10.270 1.00 12.31 O ANISOU 4791 O GLY B 182 1421 1546 1709 35 -21 -47 O ATOM 4792 N ALA B 183 40.199 -27.780 -11.148 1.00 12.31 N ANISOU 4792 N ALA B 183 1479 1515 1682 -87 9 29 N ATOM 4793 CA ALA B 183 38.846 -27.862 -10.661 1.00 12.57 C ANISOU 4793 CA ALA B 183 1533 1485 1758 -47 66 30 C ATOM 4794 C ALA B 183 38.634 -27.321 -9.267 1.00 13.73 C ANISOU 4794 C ALA B 183 1784 1628 1803 -55 -66 -33 C ATOM 4795 O ALA B 183 37.598 -26.653 -9.074 1.00 15.91 O ANISOU 4795 O ALA B 183 1857 1885 2305 54 -137 -64 O ATOM 4796 CB ALA B 183 38.345 -29.304 -10.669 1.00 12.63 C ANISOU 4796 CB ALA B 183 1707 1541 1551 -204 74 -85 C ATOM 4797 N VAL B 184 39.395 -27.765 -8.253 1.00 13.39 N ANISOU 4797 N VAL B 184 1552 1606 1929 -98 -91 93 N ATOM 4798 CA VAL B 184 39.159 -27.159 -6.925 1.00 15.16 C ANISOU 4798 CA VAL B 184 1758 1845 2156 30 -50 -147 C ATOM 4799 C VAL B 184 40.445 -26.532 -6.397 1.00 13.12 C ANISOU 4799 C VAL B 184 1665 1577 1742 117 38 -18 C ATOM 4800 O VAL B 184 40.604 -26.264 -5.191 1.00 12.42 O ANISOU 4800 O VAL B 184 1636 1388 1696 54 82 -39 O ATOM 4801 CB VAL B 184 38.592 -28.177 -5.917 1.00 19.43 C ANISOU 4801 CB VAL B 184 2458 2574 2352 -86 95 63 C ATOM 4802 CG1 VAL B 184 37.225 -28.776 -6.261 1.00 19.88 C ANISOU 4802 CG1 VAL B 184 2514 2422 2618 -108 68 63 C ATOM 4803 CG2 VAL B 184 39.531 -29.385 -5.794 1.00 20.36 C ANISOU 4803 CG2 VAL B 184 2631 2525 2578 -87 -20 85 C ATOM 4804 N GLY B 185 41.356 -26.126 -7.290 1.00 11.52 N ANISOU 4804 N GLY B 185 1300 1183 1892 116 14 -43 N ATOM 4805 CA GLY B 185 42.412 -25.177 -6.875 1.00 11.41 C ANISOU 4805 CA GLY B 185 1291 1375 1671 110 -89 -85 C ATOM 4806 C GLY B 185 43.657 -25.865 -6.344 1.00 11.98 C ANISOU 4806 C GLY B 185 1410 1423 1719 122 -90 19 C ATOM 4807 O GLY B 185 44.550 -25.177 -5.846 1.00 13.02 O ANISOU 4807 O GLY B 185 1540 1577 1830 200 -137 -158 O ATOM 4808 N ASN B 186 43.705 -27.186 -6.373 1.00 11.40 N ANISOU 4808 N ASN B 186 1374 1353 1604 287 -32 -33 N ATOM 4809 CA ASN B 186 44.862 -27.896 -5.770 1.00 10.89 C ANISOU 4809 CA ASN B 186 1352 1403 1383 233 -13 86 C ATOM 4810 C ASN B 186 45.781 -28.549 -6.777 1.00 10.63 C ANISOU 4810 C ASN B 186 1304 1267 1470 281 -29 145 C ATOM 4811 O ASN B 186 46.671 -29.356 -6.403 1.00 10.32 O ANISOU 4811 O ASN B 186 1134 1164 1625 223 -111 183 O ATOM 4812 CB ASN B 186 44.337 -28.955 -4.807 1.00 11.48 C ANISOU 4812 CB ASN B 186 1335 1342 1684 71 11 83 C ATOM 4813 CG ASN B 186 43.447 -30.011 -5.424 1.00 11.81 C ANISOU 4813 CG ASN B 186 1461 1357 1670 99 -10 71 C ATOM 4814 OD1 ASN B 186 43.376 -30.225 -6.632 1.00 11.60 O ANISOU 4814 OD1 ASN B 186 1322 1342 1745 240 165 16 O ATOM 4815 ND2 ASN B 186 42.745 -30.695 -4.519 1.00 12.37 N ANISOU 4815 ND2 ASN B 186 1311 1464 1925 129 222 66 N ATOM 4816 N TYR B 187 45.744 -28.174 -8.041 1.00 9.94 N ANISOU 4816 N TYR B 187 1209 1269 1299 83 71 -34 N ATOM 4817 CA TYR B 187 46.719 -28.659 -9.038 1.00 10.84 C ANISOU 4817 CA TYR B 187 1261 1284 1576 68 145 -86 C ATOM 4818 C TYR B 187 46.654 -30.158 -9.263 1.00 10.35 C ANISOU 4818 C TYR B 187 1286 1283 1362 38 72 -45 C ATOM 4819 O TYR B 187 47.582 -30.726 -9.857 1.00 11.63 O ANISOU 4819 O TYR B 187 1358 1229 1834 197 79 -45 O ATOM 4820 CB TYR B 187 48.188 -28.213 -8.778 1.00 11.08 C ANISOU 4820 CB TYR B 187 1331 1359 1519 34 -10 -161 C ATOM 4821 CG TYR B 187 48.249 -26.709 -8.500 1.00 10.46 C ANISOU 4821 CG TYR B 187 1278 1252 1443 97 -11 -47 C ATOM 4822 CD1 TYR B 187 48.272 -26.298 -7.171 1.00 11.66 C ANISOU 4822 CD1 TYR B 187 1447 1429 1556 32 -16 -136 C ATOM 4823 CD2 TYR B 187 48.237 -25.751 -9.491 1.00 10.27 C ANISOU 4823 CD2 TYR B 187 1186 1294 1422 27 29 -80 C ATOM 4824 CE1 TYR B 187 48.270 -24.953 -6.798 1.00 11.45 C ANISOU 4824 CE1 TYR B 187 1487 1385 1478 42 27 -106 C ATOM 4825 CE2 TYR B 187 48.239 -24.392 -9.162 1.00 10.26 C ANISOU 4825 CE2 TYR B 187 1188 1263 1449 90 -27 -40 C ATOM 4826 CZ TYR B 187 48.254 -24.025 -7.829 1.00 11.32 C ANISOU 4826 CZ TYR B 187 1398 1385 1517 28 -61 -68 C ATOM 4827 OH TYR B 187 48.236 -22.675 -7.486 1.00 12.73 O ANISOU 4827 OH TYR B 187 1613 1520 1704 157 15 -220 O ATOM 4828 N ALA B 188 45.554 -30.836 -8.927 1.00 11.34 N ANISOU 4828 N ALA B 188 1353 1312 1645 -32 31 34 N ATOM 4829 CA ALA B 188 45.404 -32.262 -9.227 1.00 11.59 C ANISOU 4829 CA ALA B 188 1453 1346 1603 -37 56 -11 C ATOM 4830 C ALA B 188 45.605 -32.531 -10.707 1.00 13.19 C ANISOU 4830 C ALA B 188 1724 1668 1619 39 8 37 C ATOM 4831 O ALA B 188 46.253 -33.529 -11.095 1.00 14.33 O ANISOU 4831 O ALA B 188 1965 1759 1720 164 -33 30 O ATOM 4832 CB ALA B 188 44.106 -32.858 -8.751 1.00 11.34 C ANISOU 4832 CB ALA B 188 1459 1278 1573 -20 68 7 C ATOM 4833 N ASN B 189 45.080 -31.630 -11.555 1.00 12.92 N ANISOU 4833 N ASN B 189 1410 1690 1807 36 -63 64 N ATOM 4834 CA ASN B 189 45.034 -31.881 -12.975 1.00 13.38 C ANISOU 4834 CA ASN B 189 1640 1657 1786 -6 57 14 C ATOM 4835 C ASN B 189 45.947 -30.979 -13.786 1.00 12.30 C ANISOU 4835 C ASN B 189 1510 1562 1603 92 -16 -45 C ATOM 4836 O ASN B 189 46.055 -31.182 -15.001 1.00 12.26 O ANISOU 4836 O ASN B 189 1714 1411 1532 36 -32 -191 O ATOM 4837 CB ASN B 189 43.577 -31.769 -13.492 1.00 14.16 C ANISOU 4837 CB ASN B 189 1692 1744 1945 31 -3 90 C ATOM 4838 CG ASN B 189 42.599 -32.576 -12.634 1.00 15.82 C ANISOU 4838 CG ASN B 189 1942 1878 2190 -17 99 171 C ATOM 4839 OD1 ASN B 189 42.839 -33.781 -12.387 1.00 15.73 O ANISOU 4839 OD1 ASN B 189 2004 1752 2220 -102 -19 129 O ATOM 4840 ND2 ASN B 189 41.506 -31.980 -12.161 1.00 16.29 N ANISOU 4840 ND2 ASN B 189 1940 2037 2213 26 54 118 N ATOM 4841 N VAL B 190 46.539 -29.950 -13.199 1.00 12.11 N ANISOU 4841 N VAL B 190 1351 1497 1753 94 -17 -55 N ATOM 4842 CA VAL B 190 47.458 -29.083 -13.961 1.00 13.13 C ANISOU 4842 CA VAL B 190 1514 1710 1763 66 -13 78 C ATOM 4843 C VAL B 190 48.537 -28.650 -12.975 1.00 13.37 C ANISOU 4843 C VAL B 190 1624 1728 1727 -19 24 -40 C ATOM 4844 O VAL B 190 48.211 -28.308 -11.859 1.00 13.12 O ANISOU 4844 O VAL B 190 1565 1653 1765 19 106 38 O ATOM 4845 CB VAL B 190 46.754 -27.868 -14.621 1.00 13.25 C ANISOU 4845 CB VAL B 190 1703 1567 1762 76 144 50 C ATOM 4846 CG1 VAL B 190 45.854 -27.173 -13.579 1.00 12.93 C ANISOU 4846 CG1 VAL B 190 1640 1486 1787 87 111 28 C ATOM 4847 CG2 VAL B 190 47.744 -26.847 -15.142 1.00 12.90 C ANISOU 4847 CG2 VAL B 190 1483 1629 1791 78 100 60 C ATOM 4848 N PRO B 191 49.820 -28.736 -13.330 1.00 13.93 N ANISOU 4848 N PRO B 191 1567 1884 1841 137 -28 -72 N ATOM 4849 CA PRO B 191 50.885 -28.559 -12.357 1.00 14.32 C ANISOU 4849 CA PRO B 191 1654 1860 1929 54 -16 -154 C ATOM 4850 C PRO B 191 51.071 -27.113 -11.946 1.00 13.07 C ANISOU 4850 C PRO B 191 1523 1741 1702 85 46 -58 C ATOM 4851 O PRO B 191 50.922 -26.199 -12.765 1.00 12.34 O ANISOU 4851 O PRO B 191 1469 1825 1395 68 143 -133 O ATOM 4852 CB PRO B 191 52.135 -29.030 -13.105 1.00 15.42 C ANISOU 4852 CB PRO B 191 1659 2119 2082 73 20 -181 C ATOM 4853 CG PRO B 191 51.718 -29.601 -14.378 1.00 16.25 C ANISOU 4853 CG PRO B 191 1810 2362 2003 183 -17 -127 C ATOM 4854 CD PRO B 191 50.280 -29.214 -14.665 1.00 14.43 C ANISOU 4854 CD PRO B 191 1673 1952 1859 101 -3 -106 C ATOM 4855 N PRO B 192 51.470 -26.842 -10.718 1.00 13.20 N ANISOU 4855 N PRO B 192 1580 1697 1738 69 22 3 N ATOM 4856 CA PRO B 192 51.713 -25.471 -10.274 1.00 12.79 C ANISOU 4856 CA PRO B 192 1550 1628 1683 31 0 -5 C ATOM 4857 C PRO B 192 52.863 -24.818 -11.023 1.00 13.34 C ANISOU 4857 C PRO B 192 1713 1705 1651 68 60 19 C ATOM 4858 O PRO B 192 52.874 -23.569 -11.212 1.00 12.24 O ANISOU 4858 O PRO B 192 1555 1605 1489 194 99 -108 O ATOM 4859 CB PRO B 192 52.051 -25.588 -8.799 1.00 14.20 C ANISOU 4859 CB PRO B 192 1872 1728 1794 1 -36 69 C ATOM 4860 CG PRO B 192 52.476 -27.007 -8.612 1.00 14.31 C ANISOU 4860 CG PRO B 192 1886 1670 1883 79 -29 -93 C ATOM 4861 CD PRO B 192 51.708 -27.834 -9.628 1.00 13.98 C ANISOU 4861 CD PRO B 192 1722 1805 1782 20 -77 40 C ATOM 4862 N GLU B 193 53.827 -25.625 -11.518 1.00 14.25 N ANISOU 4862 N GLU B 193 1627 2036 1751 196 25 -13 N ATOM 4863 CA GLU B 193 54.841 -25.093 -12.410 1.00 16.45 C ANISOU 4863 CA GLU B 193 1916 2309 2027 79 112 52 C ATOM 4864 C GLU B 193 54.225 -24.513 -13.686 1.00 16.06 C ANISOU 4864 C GLU B 193 1763 2356 1983 164 115 -75 C ATOM 4865 O GLU B 193 54.799 -23.541 -14.219 1.00 16.61 O ANISOU 4865 O GLU B 193 1919 2303 2089 151 73 -29 O ATOM 4866 CB GLU B 193 55.954 -26.108 -12.834 1.00 18.45 C ANISOU 4866 CB GLU B 193 2015 2629 2366 186 229 -52 C ATOM 4867 CG GLU B 193 56.723 -26.604 -11.627 1.00 21.96 C ANISOU 4867 CG GLU B 193 2560 3013 2771 141 -19 108 C ATOM 4868 CD GLU B 193 56.021 -27.744 -10.898 1.00 23.80 C ANISOU 4868 CD GLU B 193 2817 3108 3117 -45 31 94 C ATOM 4869 OE1 GLU B 193 54.881 -28.134 -11.187 1.00 22.41 O ANISOU 4869 OE1 GLU B 193 2641 2808 3065 94 -29 78 O ATOM 4870 OE2 GLU B 193 56.743 -28.248 -10.027 1.00 26.79 O ANISOU 4870 OE2 GLU B 193 3218 3615 3347 38 -164 201 O ATOM 4871 N VAL B 194 53.178 -25.065 -14.239 1.00 13.55 N ANISOU 4871 N VAL B 194 1696 1843 1608 210 170 -28 N ATOM 4872 CA VAL B 194 52.576 -24.497 -15.434 1.00 13.89 C ANISOU 4872 CA VAL B 194 1739 1784 1754 99 44 -77 C ATOM 4873 C VAL B 194 51.856 -23.213 -15.062 1.00 12.67 C ANISOU 4873 C VAL B 194 1548 1678 1589 5 6 -48 C ATOM 4874 O VAL B 194 51.969 -22.224 -15.773 1.00 14.22 O ANISOU 4874 O VAL B 194 1852 1769 1784 134 180 27 O ATOM 4875 CB VAL B 194 51.603 -25.540 -16.030 1.00 14.30 C ANISOU 4875 CB VAL B 194 1871 1759 1805 46 -24 -133 C ATOM 4876 CG1 VAL B 194 50.711 -24.926 -17.075 1.00 14.84 C ANISOU 4876 CG1 VAL B 194 1916 1883 1838 43 -8 -14 C ATOM 4877 CG2 VAL B 194 52.484 -26.669 -16.588 1.00 14.51 C ANISOU 4877 CG2 VAL B 194 1840 1896 1778 49 155 -133 C ATOM 4878 N GLU B 195 51.163 -23.202 -13.927 1.00 11.21 N ANISOU 4878 N GLU B 195 1382 1397 1479 134 -39 -110 N ATOM 4879 CA GLU B 195 50.481 -21.956 -13.526 1.00 11.15 C ANISOU 4879 CA GLU B 195 1341 1483 1412 62 128 -161 C ATOM 4880 C GLU B 195 51.501 -20.830 -13.410 1.00 11.60 C ANISOU 4880 C GLU B 195 1466 1523 1418 42 163 -61 C ATOM 4881 O GLU B 195 51.267 -19.725 -13.908 1.00 11.41 O ANISOU 4881 O GLU B 195 1426 1490 1420 -77 211 14 O ATOM 4882 CB GLU B 195 49.775 -22.186 -12.168 1.00 11.03 C ANISOU 4882 CB GLU B 195 1444 1309 1437 109 143 -22 C ATOM 4883 CG GLU B 195 49.201 -20.834 -11.643 1.00 10.67 C ANISOU 4883 CG GLU B 195 1353 1252 1449 80 30 -60 C ATOM 4884 CD GLU B 195 48.566 -21.065 -10.280 1.00 12.56 C ANISOU 4884 CD GLU B 195 1622 1609 1541 -6 31 72 C ATOM 4885 OE1 GLU B 195 49.288 -21.353 -9.281 1.00 13.19 O ANISOU 4885 OE1 GLU B 195 1529 1741 1743 -25 -122 -48 O ATOM 4886 OE2 GLU B 195 47.314 -20.962 -10.156 1.00 13.98 O ANISOU 4886 OE2 GLU B 195 1678 1646 1990 106 -13 177 O ATOM 4887 N GLU B 196 52.603 -21.100 -12.703 1.00 11.73 N ANISOU 4887 N GLU B 196 1390 1749 1319 8 126 -36 N ATOM 4888 CA GLU B 196 53.535 -20.002 -12.411 1.00 13.66 C ANISOU 4888 CA GLU B 196 1737 1846 1606 -117 120 47 C ATOM 4889 C GLU B 196 54.114 -19.465 -13.734 1.00 13.97 C ANISOU 4889 C GLU B 196 1887 1790 1630 -52 95 36 C ATOM 4890 O GLU B 196 54.240 -18.228 -13.845 1.00 13.35 O ANISOU 4890 O GLU B 196 1913 1750 1408 40 237 100 O ATOM 4891 CB GLU B 196 54.605 -20.533 -11.432 1.00 16.35 C ANISOU 4891 CB GLU B 196 1913 2267 2031 82 -123 -13 C ATOM 4892 CG GLU B 196 53.957 -20.775 -10.057 1.00 19.39 C ANISOU 4892 CG GLU B 196 2389 2732 2248 39 57 9 C ATOM 4893 CD GLU B 196 54.677 -21.706 -9.097 1.00 23.32 C ANISOU 4893 CD GLU B 196 2809 3227 2826 207 -50 204 C ATOM 4894 OE1 GLU B 196 55.785 -22.143 -9.462 1.00 24.84 O ANISOU 4894 OE1 GLU B 196 2654 3667 3119 254 -57 259 O ATOM 4895 OE2 GLU B 196 54.137 -22.053 -8.015 1.00 24.03 O ANISOU 4895 OE2 GLU B 196 2847 3530 2753 85 -45 160 O ATOM 4896 N LYS B 197 54.500 -20.365 -14.617 1.00 14.16 N ANISOU 4896 N LYS B 197 1780 1914 1686 14 52 -75 N ATOM 4897 CA LYS B 197 55.079 -19.914 -15.890 1.00 15.46 C ANISOU 4897 CA LYS B 197 1947 2119 1806 22 -10 152 C ATOM 4898 C LYS B 197 54.007 -19.209 -16.736 1.00 13.29 C ANISOU 4898 C LYS B 197 1706 1641 1703 15 65 -105 C ATOM 4899 O LYS B 197 54.313 -18.113 -17.227 1.00 13.30 O ANISOU 4899 O LYS B 197 1458 1879 1714 -4 161 123 O ATOM 4900 CB LYS B 197 55.621 -21.087 -16.719 1.00 20.63 C ANISOU 4900 CB LYS B 197 2748 2431 2660 99 76 -194 C ATOM 4901 CG LYS B 197 56.944 -21.711 -16.320 1.00 26.94 C ANISOU 4901 CG LYS B 197 3117 3490 3628 199 -144 19 C ATOM 4902 CD LYS B 197 57.400 -22.604 -17.500 1.00 31.19 C ANISOU 4902 CD LYS B 197 4022 3881 3946 115 61 -238 C ATOM 4903 CE LYS B 197 58.896 -22.861 -17.465 1.00 34.24 C ANISOU 4903 CE LYS B 197 4093 4385 4533 78 -4 -46 C ATOM 4904 NZ LYS B 197 59.580 -21.545 -17.257 1.00 36.83 N ANISOU 4904 NZ LYS B 197 4574 4553 4867 -96 10 -95 N ATOM 4905 N ALA B 198 52.842 -19.824 -16.915 1.00 11.29 N ANISOU 4905 N ALA B 198 1386 1597 1306 218 123 -29 N ATOM 4906 CA ALA B 198 51.799 -19.250 -17.783 1.00 11.10 C ANISOU 4906 CA ALA B 198 1316 1455 1446 44 36 -72 C ATOM 4907 C ALA B 198 51.409 -17.863 -17.278 1.00 11.70 C ANISOU 4907 C ALA B 198 1513 1475 1459 41 60 -83 C ATOM 4908 O ALA B 198 51.366 -16.892 -18.062 1.00 12.11 O ANISOU 4908 O ALA B 198 1530 1535 1535 74 57 -53 O ATOM 4909 CB ALA B 198 50.543 -20.140 -17.822 1.00 10.20 C ANISOU 4909 CB ALA B 198 1286 1197 1393 153 65 -160 C ATOM 4910 N LEU B 199 51.248 -17.719 -15.945 1.00 10.96 N ANISOU 4910 N LEU B 199 1175 1529 1459 -28 164 -163 N ATOM 4911 CA LEU B 199 50.807 -16.394 -15.468 1.00 11.57 C ANISOU 4911 CA LEU B 199 1515 1424 1458 1 89 -14 C ATOM 4912 C LEU B 199 51.921 -15.378 -15.624 1.00 12.95 C ANISOU 4912 C LEU B 199 1637 1621 1661 -60 128 48 C ATOM 4913 O LEU B 199 51.611 -14.201 -15.868 1.00 12.93 O ANISOU 4913 O LEU B 199 1687 1616 1609 0 178 101 O ATOM 4914 CB LEU B 199 50.344 -16.437 -13.991 1.00 10.91 C ANISOU 4914 CB LEU B 199 1333 1360 1451 51 142 -32 C ATOM 4915 CG LEU B 199 49.056 -17.281 -13.870 1.00 10.24 C ANISOU 4915 CG LEU B 199 1257 1434 1202 72 79 146 C ATOM 4916 CD1 LEU B 199 48.672 -17.462 -12.400 1.00 11.13 C ANISOU 4916 CD1 LEU B 199 1473 1647 1109 127 70 -48 C ATOM 4917 CD2 LEU B 199 47.861 -16.648 -14.630 1.00 11.41 C ANISOU 4917 CD2 LEU B 199 1330 1703 1300 120 18 64 C ATOM 4918 N SER B 200 53.172 -15.769 -15.425 1.00 14.17 N ANISOU 4918 N SER B 200 1682 1948 1755 47 9 -41 N ATOM 4919 CA SER B 200 54.253 -14.799 -15.667 1.00 15.78 C ANISOU 4919 CA SER B 200 1969 1941 2085 -96 19 31 C ATOM 4920 C SER B 200 54.266 -14.323 -17.108 1.00 15.02 C ANISOU 4920 C SER B 200 1755 1902 2049 4 -12 -36 C ATOM 4921 O SER B 200 54.532 -13.089 -17.307 1.00 14.63 O ANISOU 4921 O SER B 200 1653 1828 2077 50 29 -25 O ATOM 4922 CB SER B 200 55.651 -15.341 -15.277 1.00 19.65 C ANISOU 4922 CB SER B 200 2320 2517 2631 185 -238 82 C ATOM 4923 OG SER B 200 56.006 -16.239 -16.327 1.00 25.60 O ANISOU 4923 OG SER B 200 3156 3299 3273 154 96 -172 O ATOM 4924 N TYR B 201 53.955 -15.120 -18.142 1.00 13.76 N ANISOU 4924 N TYR B 201 1544 1775 1908 140 84 -11 N ATOM 4925 CA TYR B 201 53.873 -14.631 -19.501 1.00 14.67 C ANISOU 4925 CA TYR B 201 1792 1875 1908 154 85 -38 C ATOM 4926 C TYR B 201 52.772 -13.567 -19.661 1.00 15.05 C ANISOU 4926 C TYR B 201 1830 1898 1992 147 147 71 C ATOM 4927 O TYR B 201 52.898 -12.661 -20.490 1.00 16.66 O ANISOU 4927 O TYR B 201 2088 2174 2068 242 339 196 O ATOM 4928 CB TYR B 201 53.526 -15.717 -20.537 1.00 14.94 C ANISOU 4928 CB TYR B 201 1864 1957 1855 40 106 -61 C ATOM 4929 CG TYR B 201 54.494 -16.892 -20.591 1.00 16.79 C ANISOU 4929 CG TYR B 201 2230 2075 2074 163 76 -32 C ATOM 4930 CD1 TYR B 201 53.985 -18.180 -20.701 1.00 17.88 C ANISOU 4930 CD1 TYR B 201 2386 2185 2223 36 46 -16 C ATOM 4931 CD2 TYR B 201 55.866 -16.697 -20.544 1.00 19.10 C ANISOU 4931 CD2 TYR B 201 2323 2458 2476 112 29 -36 C ATOM 4932 CE1 TYR B 201 54.836 -19.276 -20.776 1.00 19.93 C ANISOU 4932 CE1 TYR B 201 2546 2444 2584 173 41 5 C ATOM 4933 CE2 TYR B 201 56.727 -17.805 -20.628 1.00 20.93 C ANISOU 4933 CE2 TYR B 201 2600 2504 2851 148 14 35 C ATOM 4934 CZ TYR B 201 56.195 -19.067 -20.739 1.00 21.32 C ANISOU 4934 CZ TYR B 201 2640 2580 2880 74 -42 -32 C ATOM 4935 OH TYR B 201 57.081 -20.129 -20.815 1.00 22.97 O ANISOU 4935 OH TYR B 201 2743 2840 3146 228 -57 -24 O ATOM 4936 N LEU B 202 51.706 -13.660 -18.867 1.00 13.97 N ANISOU 4936 N LEU B 202 1695 1847 1765 128 67 53 N ATOM 4937 CA LEU B 202 50.632 -12.675 -18.918 1.00 13.44 C ANISOU 4937 CA LEU B 202 1629 1741 1735 46 27 -23 C ATOM 4938 C LEU B 202 50.842 -11.441 -18.070 1.00 14.30 C ANISOU 4938 C LEU B 202 1795 1797 1842 62 -12 -49 C ATOM 4939 O LEU B 202 49.934 -10.575 -18.013 1.00 14.81 O ANISOU 4939 O LEU B 202 1877 1788 1962 140 -79 -31 O ATOM 4940 CB LEU B 202 49.357 -13.414 -18.446 1.00 13.16 C ANISOU 4940 CB LEU B 202 1610 1700 1692 32 -3 0 C ATOM 4941 CG LEU B 202 48.933 -14.629 -19.283 1.00 13.88 C ANISOU 4941 CG LEU B 202 1758 1773 1744 -17 19 -3 C ATOM 4942 CD1 LEU B 202 47.701 -15.288 -18.622 1.00 14.03 C ANISOU 4942 CD1 LEU B 202 1652 1863 1816 -76 -36 1 C ATOM 4943 CD2 LEU B 202 48.627 -14.246 -20.730 1.00 14.25 C ANISOU 4943 CD2 LEU B 202 1889 1824 1701 100 -3 -56 C ATOM 4944 N GLY B 203 51.922 -11.331 -17.298 1.00 13.33 N ANISOU 4944 N GLY B 203 1652 1714 1698 -11 93 -15 N ATOM 4945 CA GLY B 203 52.151 -10.218 -16.392 1.00 13.83 C ANISOU 4945 CA GLY B 203 1886 1688 1679 15 2 4 C ATOM 4946 C GLY B 203 51.390 -10.357 -15.082 1.00 13.74 C ANISOU 4946 C GLY B 203 1701 1693 1827 -11 66 -71 C ATOM 4947 O GLY B 203 51.276 -9.356 -14.370 1.00 14.68 O ANISOU 4947 O GLY B 203 1918 1572 2089 79 88 -38 O ATOM 4948 N LEU B 204 50.986 -11.573 -14.709 1.00 12.43 N ANISOU 4948 N LEU B 204 1451 1605 1665 -11 79 -61 N ATOM 4949 CA LEU B 204 50.176 -11.811 -13.520 1.00 12.34 C ANISOU 4949 CA LEU B 204 1453 1661 1575 -35 -23 -116 C ATOM 4950 C LEU B 204 50.898 -12.707 -12.512 1.00 13.02 C ANISOU 4950 C LEU B 204 1651 1618 1678 19 43 -49 C ATOM 4951 O LEU B 204 51.896 -13.346 -12.893 1.00 15.06 O ANISOU 4951 O LEU B 204 1700 2017 2003 286 43 55 O ATOM 4952 CB LEU B 204 48.831 -12.484 -13.878 1.00 11.54 C ANISOU 4952 CB LEU B 204 1364 1519 1502 50 0 -165 C ATOM 4953 CG LEU B 204 47.957 -11.678 -14.844 1.00 12.46 C ANISOU 4953 CG LEU B 204 1500 1492 1742 82 -58 -174 C ATOM 4954 CD1 LEU B 204 46.736 -12.539 -15.208 1.00 12.33 C ANISOU 4954 CD1 LEU B 204 1404 1589 1692 87 -101 -192 C ATOM 4955 CD2 LEU B 204 47.526 -10.351 -14.225 1.00 12.86 C ANISOU 4955 CD2 LEU B 204 1595 1462 1827 178 -71 -122 C ATOM 4956 N LYS B 205 50.434 -12.720 -11.269 1.00 12.49 N ANISOU 4956 N LYS B 205 1548 1607 1591 -95 59 -28 N ATOM 4957 CA LYS B 205 51.022 -13.599 -10.262 1.00 13.06 C ANISOU 4957 CA LYS B 205 1623 1560 1778 -62 24 -2 C ATOM 4958 C LYS B 205 50.039 -14.701 -9.946 1.00 12.03 C ANISOU 4958 C LYS B 205 1449 1493 1629 41 40 -54 C ATOM 4959 O LYS B 205 48.824 -14.492 -10.127 1.00 11.88 O ANISOU 4959 O LYS B 205 1441 1186 1889 233 -68 -120 O ATOM 4960 CB LYS B 205 51.192 -12.784 -8.944 1.00 16.43 C ANISOU 4960 CB LYS B 205 2155 2137 1950 -79 -73 -139 C ATOM 4961 CG LYS B 205 52.384 -11.832 -9.125 1.00 20.68 C ANISOU 4961 CG LYS B 205 2570 2534 2754 -360 3 -37 C ATOM 4962 CD LYS B 205 52.600 -11.144 -7.760 1.00 23.92 C ANISOU 4962 CD LYS B 205 3127 3067 2893 -161 37 -186 C ATOM 4963 CE LYS B 205 51.627 -10.007 -7.773 1.00 27.34 C ANISOU 4963 CE LYS B 205 3417 3430 3542 67 95 -119 C ATOM 4964 NZ LYS B 205 51.685 -9.146 -8.993 1.00 29.86 N ANISOU 4964 NZ LYS B 205 3763 4028 3555 120 67 -13 N ATOM 4965 N PRO B 206 50.498 -15.836 -9.441 1.00 12.21 N ANISOU 4965 N PRO B 206 1494 1512 1633 83 89 24 N ATOM 4966 CA PRO B 206 49.571 -16.895 -9.075 1.00 11.48 C ANISOU 4966 CA PRO B 206 1431 1463 1466 92 142 -7 C ATOM 4967 C PRO B 206 48.884 -16.571 -7.734 1.00 10.64 C ANISOU 4967 C PRO B 206 1222 1388 1433 106 29 -95 C ATOM 4968 O PRO B 206 49.547 -16.149 -6.786 1.00 10.06 O ANISOU 4968 O PRO B 206 1063 1411 1347 146 197 -247 O ATOM 4969 CB PRO B 206 50.512 -18.113 -8.911 1.00 13.57 C ANISOU 4969 CB PRO B 206 1618 1718 1822 247 -13 -55 C ATOM 4970 CG PRO B 206 51.853 -17.539 -8.725 1.00 15.42 C ANISOU 4970 CG PRO B 206 1800 1871 2189 97 103 118 C ATOM 4971 CD PRO B 206 51.938 -16.191 -9.361 1.00 13.85 C ANISOU 4971 CD PRO B 206 1637 1822 1803 203 115 73 C ATOM 4972 N GLU B 207 47.547 -16.768 -7.674 1.00 10.26 N ANISOU 4972 N GLU B 207 1293 1307 1299 16 159 58 N ATOM 4973 CA GLU B 207 46.896 -16.719 -6.358 1.00 10.71 C ANISOU 4973 CA GLU B 207 1252 1423 1392 23 105 28 C ATOM 4974 C GLU B 207 47.604 -17.728 -5.484 1.00 11.16 C ANISOU 4974 C GLU B 207 1350 1394 1495 -7 9 51 C ATOM 4975 O GLU B 207 47.713 -18.884 -5.937 1.00 11.71 O ANISOU 4975 O GLU B 207 1334 1453 1661 35 90 -26 O ATOM 4976 CB GLU B 207 45.432 -17.124 -6.591 1.00 11.34 C ANISOU 4976 CB GLU B 207 1359 1465 1484 -126 138 42 C ATOM 4977 CG GLU B 207 44.579 -16.990 -5.338 1.00 11.87 C ANISOU 4977 CG GLU B 207 1615 1475 1418 55 167 -68 C ATOM 4978 CD GLU B 207 44.562 -15.547 -4.876 1.00 12.60 C ANISOU 4978 CD GLU B 207 1678 1455 1653 -8 18 -20 C ATOM 4979 OE1 GLU B 207 44.944 -15.205 -3.748 1.00 14.00 O ANISOU 4979 OE1 GLU B 207 1837 1774 1709 113 53 -111 O ATOM 4980 OE2 GLU B 207 44.180 -14.716 -5.729 1.00 13.89 O ANISOU 4980 OE2 GLU B 207 1888 1650 1741 -37 92 122 O ATOM 4981 N PRO B 208 48.015 -17.387 -4.260 1.00 11.23 N ANISOU 4981 N PRO B 208 1391 1322 1553 8 -53 -17 N ATOM 4982 CA PRO B 208 48.873 -18.295 -3.508 1.00 11.49 C ANISOU 4982 CA PRO B 208 1544 1345 1479 -13 -80 108 C ATOM 4983 C PRO B 208 48.060 -19.541 -3.112 1.00 11.94 C ANISOU 4983 C PRO B 208 1526 1341 1670 12 -41 68 C ATOM 4984 O PRO B 208 48.574 -20.672 -3.221 1.00 12.19 O ANISOU 4984 O PRO B 208 1396 1517 1717 184 -155 30 O ATOM 4985 CB PRO B 208 49.287 -17.491 -2.296 1.00 13.60 C ANISOU 4985 CB PRO B 208 1893 1530 1744 -123 -183 9 C ATOM 4986 CG PRO B 208 49.017 -16.056 -2.589 1.00 14.24 C ANISOU 4986 CG PRO B 208 2023 1594 1795 73 -257 -70 C ATOM 4987 CD PRO B 208 48.156 -15.947 -3.831 1.00 12.40 C ANISOU 4987 CD PRO B 208 1708 1410 1594 -13 -120 -96 C ATOM 4988 N VAL B 209 46.757 -19.352 -2.796 1.00 10.96 N ANISOU 4988 N VAL B 209 1496 1289 1379 11 24 217 N ATOM 4989 CA VAL B 209 45.868 -20.510 -2.699 1.00 12.68 C ANISOU 4989 CA VAL B 209 1468 1629 1722 -172 -73 -69 C ATOM 4990 C VAL B 209 44.546 -20.139 -3.366 1.00 12.16 C ANISOU 4990 C VAL B 209 1546 1584 1489 -48 -23 -20 C ATOM 4991 O VAL B 209 43.841 -19.260 -2.788 1.00 12.53 O ANISOU 4991 O VAL B 209 1429 1725 1608 -120 -43 -202 O ATOM 4992 CB VAL B 209 45.307 -20.900 -1.308 1.00 17.16 C ANISOU 4992 CB VAL B 209 2412 2174 1932 -248 -19 217 C ATOM 4993 CG1 VAL B 209 44.870 -22.383 -1.281 1.00 18.75 C ANISOU 4993 CG1 VAL B 209 2748 2154 2223 -230 2 219 C ATOM 4994 CG2 VAL B 209 46.062 -20.434 -0.123 1.00 18.92 C ANISOU 4994 CG2 VAL B 209 2516 2593 2081 -322 -60 119 C ATOM 4995 N SER B 210 44.193 -20.827 -4.435 1.00 11.64 N ANISOU 4995 N SER B 210 1473 1414 1536 59 -50 -72 N ATOM 4996 CA SER B 210 42.866 -20.596 -5.021 1.00 12.08 C ANISOU 4996 CA SER B 210 1459 1563 1568 -110 -33 76 C ATOM 4997 C SER B 210 41.922 -21.766 -4.706 1.00 12.22 C ANISOU 4997 C SER B 210 1450 1421 1774 -8 -57 77 C ATOM 4998 O SER B 210 42.423 -22.784 -4.256 1.00 13.03 O ANISOU 4998 O SER B 210 1612 1452 1886 -15 -151 138 O ATOM 4999 CB SER B 210 42.954 -20.396 -6.551 1.00 12.60 C ANISOU 4999 CB SER B 210 1701 1613 1472 -56 -45 33 C ATOM 5000 OG SER B 210 43.794 -21.407 -7.147 1.00 14.84 O ANISOU 5000 OG SER B 210 1929 1986 1725 86 3 31 O ATOM 5001 N THR B 211 40.635 -21.562 -4.951 1.00 10.99 N ANISOU 5001 N THR B 211 1242 1259 1673 -109 16 25 N ATOM 5002 CA THR B 211 39.705 -22.707 -4.901 1.00 10.61 C ANISOU 5002 CA THR B 211 1336 1197 1498 -14 -10 36 C ATOM 5003 C THR B 211 39.397 -23.004 -6.348 1.00 9.89 C ANISOU 5003 C THR B 211 1096 1174 1488 2 -3 -63 C ATOM 5004 O THR B 211 40.319 -22.901 -7.177 1.00 10.88 O ANISOU 5004 O THR B 211 1219 1427 1487 -80 23 102 O ATOM 5005 CB THR B 211 38.436 -22.372 -4.096 1.00 11.14 C ANISOU 5005 CB THR B 211 1352 1310 1569 13 14 117 C ATOM 5006 OG1 THR B 211 37.882 -21.144 -4.616 1.00 11.18 O ANISOU 5006 OG1 THR B 211 1444 1121 1682 -23 -41 -10 O ATOM 5007 CG2 THR B 211 38.772 -22.165 -2.628 1.00 13.20 C ANISOU 5007 CG2 THR B 211 1897 1495 1624 -30 15 39 C ATOM 5008 N GLN B 212 38.162 -23.259 -6.762 1.00 9.31 N ANISOU 5008 N GLN B 212 1120 1059 1359 -10 -21 -129 N ATOM 5009 CA GLN B 212 37.857 -23.203 -8.193 1.00 9.97 C ANISOU 5009 CA GLN B 212 1212 1240 1336 -90 -70 -24 C ATOM 5010 C GLN B 212 37.991 -21.775 -8.727 1.00 11.19 C ANISOU 5010 C GLN B 212 1457 1311 1482 1 41 -8 C ATOM 5011 O GLN B 212 38.222 -21.639 -9.943 1.00 10.66 O ANISOU 5011 O GLN B 212 1340 1263 1448 -38 -6 -60 O ATOM 5012 CB GLN B 212 36.454 -23.761 -8.466 1.00 10.14 C ANISOU 5012 CB GLN B 212 1216 1391 1248 -73 -78 -54 C ATOM 5013 CG GLN B 212 36.129 -23.786 -9.965 1.00 10.71 C ANISOU 5013 CG GLN B 212 1424 1381 1264 -97 -90 -28 C ATOM 5014 CD GLN B 212 34.939 -24.684 -10.236 1.00 11.30 C ANISOU 5014 CD GLN B 212 1383 1406 1502 -75 -41 -26 C ATOM 5015 OE1 GLN B 212 33.817 -24.208 -10.342 1.00 11.39 O ANISOU 5015 OE1 GLN B 212 1569 1391 1369 133 97 -153 O ATOM 5016 NE2 GLN B 212 35.151 -25.984 -10.375 1.00 11.85 N ANISOU 5016 NE2 GLN B 212 1503 1403 1596 19 -39 -45 N ATOM 5017 N VAL B 213 37.897 -20.730 -7.893 1.00 10.29 N ANISOU 5017 N VAL B 213 1083 1218 1607 -3 5 -54 N ATOM 5018 CA VAL B 213 37.969 -19.359 -8.353 1.00 11.08 C ANISOU 5018 CA VAL B 213 1223 1286 1701 67 -5 -11 C ATOM 5019 C VAL B 213 39.070 -18.578 -7.636 1.00 10.58 C ANISOU 5019 C VAL B 213 1178 1318 1523 95 37 23 C ATOM 5020 O VAL B 213 39.643 -19.006 -6.643 1.00 11.77 O ANISOU 5020 O VAL B 213 1458 1457 1558 88 -9 177 O ATOM 5021 CB VAL B 213 36.612 -18.627 -8.077 1.00 11.15 C ANISOU 5021 CB VAL B 213 1261 1479 1496 141 -4 -30 C ATOM 5022 CG1 VAL B 213 35.502 -19.306 -8.893 1.00 11.81 C ANISOU 5022 CG1 VAL B 213 1341 1595 1552 85 -27 -153 C ATOM 5023 CG2 VAL B 213 36.265 -18.682 -6.579 1.00 11.21 C ANISOU 5023 CG2 VAL B 213 1426 1337 1495 165 -23 -78 C ATOM 5024 N VAL B 214 39.433 -17.400 -8.140 1.00 10.57 N ANISOU 5024 N VAL B 214 1181 1257 1576 16 123 -60 N ATOM 5025 CA VAL B 214 40.196 -16.366 -7.456 1.00 10.11 C ANISOU 5025 CA VAL B 214 1258 1281 1301 22 62 -41 C ATOM 5026 C VAL B 214 39.301 -15.749 -6.381 1.00 9.90 C ANISOU 5026 C VAL B 214 1217 1264 1280 45 7 -75 C ATOM 5027 O VAL B 214 38.127 -15.456 -6.661 1.00 11.04 O ANISOU 5027 O VAL B 214 1226 1421 1548 127 97 -186 O ATOM 5028 CB VAL B 214 40.651 -15.297 -8.486 1.00 10.14 C ANISOU 5028 CB VAL B 214 1304 1273 1275 -89 119 -130 C ATOM 5029 CG1 VAL B 214 41.248 -14.077 -7.768 1.00 10.63 C ANISOU 5029 CG1 VAL B 214 1357 1218 1462 -116 61 -39 C ATOM 5030 CG2 VAL B 214 41.618 -15.893 -9.513 1.00 11.05 C ANISOU 5030 CG2 VAL B 214 1328 1458 1413 -62 222 -34 C ATOM 5031 N PRO B 215 39.762 -15.617 -5.148 1.00 9.86 N ANISOU 5031 N PRO B 215 1119 1359 1268 109 -20 -12 N ATOM 5032 CA PRO B 215 38.974 -15.097 -4.040 1.00 8.88 C ANISOU 5032 CA PRO B 215 1095 1163 1116 116 -139 -38 C ATOM 5033 C PRO B 215 38.470 -13.696 -4.344 1.00 9.67 C ANISOU 5033 C PRO B 215 1106 1182 1385 32 11 10 C ATOM 5034 O PRO B 215 39.201 -12.841 -4.862 1.00 9.62 O ANISOU 5034 O PRO B 215 1154 1168 1332 92 190 37 O ATOM 5035 CB PRO B 215 39.916 -15.195 -2.825 1.00 9.34 C ANISOU 5035 CB PRO B 215 1021 1372 1155 95 -118 -43 C ATOM 5036 CG PRO B 215 41.285 -15.135 -3.421 1.00 9.49 C ANISOU 5036 CG PRO B 215 1135 1276 1196 -6 87 -120 C ATOM 5037 CD PRO B 215 41.184 -15.861 -4.763 1.00 9.48 C ANISOU 5037 CD PRO B 215 1038 1404 1157 -8 -82 -84 C ATOM 5038 N ARG B 216 37.193 -13.428 -4.013 1.00 8.99 N ANISOU 5038 N ARG B 216 995 1180 1240 76 -33 26 N ATOM 5039 CA ARG B 216 36.496 -12.233 -4.468 1.00 8.82 C ANISOU 5039 CA ARG B 216 949 1150 1251 49 -24 -55 C ATOM 5040 C ARG B 216 36.698 -11.059 -3.560 1.00 8.63 C ANISOU 5040 C ARG B 216 958 1120 1202 73 10 41 C ATOM 5041 O ARG B 216 36.239 -9.964 -3.913 1.00 9.14 O ANISOU 5041 O ARG B 216 1114 981 1377 99 97 14 O ATOM 5042 CB ARG B 216 34.972 -12.566 -4.625 1.00 8.99 C ANISOU 5042 CB ARG B 216 971 1318 1126 72 7 -116 C ATOM 5043 CG ARG B 216 34.627 -12.476 -6.125 1.00 9.42 C ANISOU 5043 CG ARG B 216 1234 1203 1141 221 -18 -150 C ATOM 5044 CD ARG B 216 35.396 -13.597 -6.892 1.00 9.96 C ANISOU 5044 CD ARG B 216 1276 1255 1252 179 122 -194 C ATOM 5045 NE ARG B 216 35.113 -13.402 -8.313 1.00 11.49 N ANISOU 5045 NE ARG B 216 1408 1599 1358 85 5 -141 N ATOM 5046 CZ ARG B 216 35.646 -14.167 -9.281 1.00 12.24 C ANISOU 5046 CZ ARG B 216 1503 1682 1466 148 88 -49 C ATOM 5047 NH1 ARG B 216 35.289 -13.912 -10.549 1.00 12.74 N ANISOU 5047 NH1 ARG B 216 1423 1854 1565 33 -42 37 N ATOM 5048 NH2 ARG B 216 36.529 -15.126 -9.010 1.00 11.89 N ANISOU 5048 NH2 ARG B 216 1328 1653 1535 170 115 -15 N ATOM 5049 N ASP B 217 37.504 -11.180 -2.484 1.00 7.95 N ANISOU 5049 N ASP B 217 809 1180 1031 -2 65 -17 N ATOM 5050 CA ASP B 217 37.855 -9.982 -1.732 1.00 9.20 C ANISOU 5050 CA ASP B 217 1146 1162 1187 -37 15 -11 C ATOM 5051 C ASP B 217 38.799 -9.114 -2.567 1.00 9.26 C ANISOU 5051 C ASP B 217 1159 1137 1221 -24 28 -38 C ATOM 5052 O ASP B 217 38.790 -7.883 -2.364 1.00 9.29 O ANISOU 5052 O ASP B 217 1094 1014 1421 -62 65 63 O ATOM 5053 CB ASP B 217 38.513 -10.329 -0.389 1.00 9.03 C ANISOU 5053 CB ASP B 217 1322 1064 1044 73 -1 -78 C ATOM 5054 CG ASP B 217 39.775 -11.149 -0.554 1.00 11.32 C ANISOU 5054 CG ASP B 217 1345 1445 1512 65 -84 -12 C ATOM 5055 OD1 ASP B 217 40.913 -10.736 -0.221 1.00 12.51 O ANISOU 5055 OD1 ASP B 217 1490 1602 1662 -21 -221 -113 O ATOM 5056 OD2 ASP B 217 39.673 -12.318 -1.044 1.00 12.56 O ANISOU 5056 OD2 ASP B 217 1572 1499 1699 209 -55 -231 O ATOM 5057 N ARG B 218 39.534 -9.670 -3.507 1.00 9.05 N ANISOU 5057 N ARG B 218 1008 1106 1326 93 63 30 N ATOM 5058 CA ARG B 218 40.375 -8.823 -4.367 1.00 9.32 C ANISOU 5058 CA ARG B 218 1129 1175 1235 127 51 115 C ATOM 5059 C ARG B 218 39.542 -7.881 -5.234 1.00 8.78 C ANISOU 5059 C ARG B 218 1024 1035 1279 68 5 33 C ATOM 5060 O ARG B 218 39.785 -6.678 -5.354 1.00 9.12 O ANISOU 5060 O ARG B 218 1179 1022 1262 18 26 138 O ATOM 5061 CB ARG B 218 41.178 -9.702 -5.342 1.00 9.38 C ANISOU 5061 CB ARG B 218 1078 1090 1397 116 -5 -33 C ATOM 5062 CG ARG B 218 42.184 -10.588 -4.542 1.00 10.20 C ANISOU 5062 CG ARG B 218 1195 1338 1343 116 -65 53 C ATOM 5063 CD ARG B 218 43.011 -11.380 -5.536 1.00 11.02 C ANISOU 5063 CD ARG B 218 1268 1455 1464 120 -53 -101 C ATOM 5064 NE ARG B 218 44.059 -12.178 -4.880 1.00 12.06 N ANISOU 5064 NE ARG B 218 1404 1596 1582 117 -50 95 N ATOM 5065 CZ ARG B 218 45.162 -11.698 -4.290 1.00 11.74 C ANISOU 5065 CZ ARG B 218 1416 1561 1484 53 25 -3 C ATOM 5066 NH1 ARG B 218 45.417 -10.390 -4.237 1.00 10.55 N ANISOU 5066 NH1 ARG B 218 1197 1585 1228 18 78 23 N ATOM 5067 NH2 ARG B 218 45.979 -12.565 -3.706 1.00 12.12 N ANISOU 5067 NH2 ARG B 218 1396 1885 1327 115 92 44 N ATOM 5068 N HIS B 219 38.509 -8.435 -5.845 1.00 8.74 N ANISOU 5068 N HIS B 219 1199 1131 992 38 -62 14 N ATOM 5069 CA HIS B 219 37.624 -7.642 -6.706 1.00 8.32 C ANISOU 5069 CA HIS B 219 1060 935 1168 133 -50 -22 C ATOM 5070 C HIS B 219 36.848 -6.623 -5.876 1.00 8.92 C ANISOU 5070 C HIS B 219 1269 1041 1079 82 39 -52 C ATOM 5071 O HIS B 219 36.666 -5.508 -6.385 1.00 8.53 O ANISOU 5071 O HIS B 219 1004 958 1279 73 18 -62 O ATOM 5072 CB HIS B 219 36.653 -8.540 -7.481 1.00 9.36 C ANISOU 5072 CB HIS B 219 1274 1128 1154 32 -47 -114 C ATOM 5073 CG HIS B 219 37.365 -9.700 -8.128 1.00 10.72 C ANISOU 5073 CG HIS B 219 1283 1338 1453 186 30 -81 C ATOM 5074 ND1 HIS B 219 37.730 -10.796 -7.331 1.00 12.13 N ANISOU 5074 ND1 HIS B 219 1546 1541 1523 102 147 85 N ATOM 5075 CD2 HIS B 219 37.791 -9.987 -9.375 1.00 11.39 C ANISOU 5075 CD2 HIS B 219 1460 1446 1421 181 -24 7 C ATOM 5076 CE1 HIS B 219 38.331 -11.706 -8.092 1.00 12.24 C ANISOU 5076 CE1 HIS B 219 1657 1505 1489 125 107 28 C ATOM 5077 NE2 HIS B 219 38.384 -11.243 -9.351 1.00 11.61 N ANISOU 5077 NE2 HIS B 219 1720 1344 1348 181 18 -72 N ATOM 5078 N ALA B 220 36.455 -6.959 -4.655 1.00 8.43 N ANISOU 5078 N ALA B 220 1102 987 1116 1 31 -67 N ATOM 5079 CA ALA B 220 35.711 -6.006 -3.816 1.00 9.06 C ANISOU 5079 CA ALA B 220 1170 1091 1181 -20 173 -30 C ATOM 5080 C ALA B 220 36.615 -4.850 -3.401 1.00 8.70 C ANISOU 5080 C ALA B 220 945 1070 1291 77 58 8 C ATOM 5081 O ALA B 220 36.216 -3.684 -3.365 1.00 9.29 O ANISOU 5081 O ALA B 220 1150 968 1413 46 144 102 O ATOM 5082 CB ALA B 220 35.215 -6.688 -2.528 1.00 10.12 C ANISOU 5082 CB ALA B 220 1420 1294 1132 -40 149 37 C ATOM 5083 N PHE B 221 37.895 -5.165 -3.169 1.00 8.59 N ANISOU 5083 N PHE B 221 821 1241 1203 -43 -55 33 N ATOM 5084 CA PHE B 221 38.855 -4.102 -2.845 1.00 9.26 C ANISOU 5084 CA PHE B 221 966 1146 1408 -33 -55 94 C ATOM 5085 C PHE B 221 39.017 -3.164 -4.031 1.00 9.46 C ANISOU 5085 C PHE B 221 1112 1229 1254 13 -35 10 C ATOM 5086 O PHE B 221 39.037 -1.932 -3.835 1.00 9.79 O ANISOU 5086 O PHE B 221 1062 1216 1443 -88 51 24 O ATOM 5087 CB PHE B 221 40.218 -4.778 -2.487 1.00 9.88 C ANISOU 5087 CB PHE B 221 954 1324 1475 99 -158 25 C ATOM 5088 CG PHE B 221 41.219 -3.702 -2.100 1.00 13.09 C ANISOU 5088 CG PHE B 221 1337 1634 2003 -40 -159 -65 C ATOM 5089 CD1 PHE B 221 41.291 -3.305 -0.792 1.00 15.13 C ANISOU 5089 CD1 PHE B 221 1799 1948 2002 7 -271 -71 C ATOM 5090 CD2 PHE B 221 42.014 -3.115 -3.078 1.00 15.62 C ANISOU 5090 CD2 PHE B 221 1847 1975 2112 -77 -65 57 C ATOM 5091 CE1 PHE B 221 42.184 -2.289 -0.435 1.00 17.56 C ANISOU 5091 CE1 PHE B 221 2056 2256 2361 -267 -138 -35 C ATOM 5092 CE2 PHE B 221 42.939 -2.130 -2.705 1.00 17.23 C ANISOU 5092 CE2 PHE B 221 2199 2077 2270 -154 -106 -40 C ATOM 5093 CZ PHE B 221 43.006 -1.717 -1.383 1.00 17.76 C ANISOU 5093 CZ PHE B 221 2235 2275 2238 -143 -122 -8 C ATOM 5094 N TYR B 222 39.146 -3.687 -5.239 1.00 9.41 N ANISOU 5094 N TYR B 222 1089 1335 1150 1 93 73 N ATOM 5095 CA TYR B 222 39.311 -2.857 -6.441 1.00 8.93 C ANISOU 5095 CA TYR B 222 1181 1147 1064 73 22 -60 C ATOM 5096 C TYR B 222 38.083 -1.984 -6.648 1.00 7.99 C ANISOU 5096 C TYR B 222 1068 963 1003 -21 -17 -26 C ATOM 5097 O TYR B 222 38.173 -0.767 -6.850 1.00 8.39 O ANISOU 5097 O TYR B 222 1095 932 1161 -42 29 103 O ATOM 5098 CB TYR B 222 39.465 -3.820 -7.633 1.00 8.26 C ANISOU 5098 CB TYR B 222 1086 1111 940 182 207 37 C ATOM 5099 CG TYR B 222 39.660 -3.276 -9.028 1.00 8.31 C ANISOU 5099 CG TYR B 222 1130 1107 922 78 74 -17 C ATOM 5100 CD1 TYR B 222 40.946 -3.182 -9.570 1.00 8.09 C ANISOU 5100 CD1 TYR B 222 1183 957 935 -29 186 14 C ATOM 5101 CD2 TYR B 222 38.564 -2.942 -9.819 1.00 9.09 C ANISOU 5101 CD2 TYR B 222 1242 1124 1087 23 -53 71 C ATOM 5102 CE1 TYR B 222 41.116 -2.737 -10.872 1.00 8.97 C ANISOU 5102 CE1 TYR B 222 1380 1104 924 26 49 26 C ATOM 5103 CE2 TYR B 222 38.732 -2.511 -11.133 1.00 9.49 C ANISOU 5103 CE2 TYR B 222 1248 1140 1219 133 87 83 C ATOM 5104 CZ TYR B 222 39.999 -2.431 -11.649 1.00 10.18 C ANISOU 5104 CZ TYR B 222 1256 1332 1280 -19 72 154 C ATOM 5105 OH TYR B 222 40.143 -2.035 -12.970 1.00 11.11 O ANISOU 5105 OH TYR B 222 1473 1513 1234 134 27 128 O ATOM 5106 N LEU B 223 36.895 -2.584 -6.503 1.00 8.04 N ANISOU 5106 N LEU B 223 983 1064 1006 14 96 -81 N ATOM 5107 CA LEU B 223 35.689 -1.754 -6.766 1.00 9.04 C ANISOU 5107 CA LEU B 223 1127 1215 1094 93 -111 -34 C ATOM 5108 C LEU B 223 35.421 -0.783 -5.631 1.00 8.87 C ANISOU 5108 C LEU B 223 1091 1141 1137 4 -56 -16 C ATOM 5109 O LEU B 223 34.882 0.308 -5.909 1.00 9.55 O ANISOU 5109 O LEU B 223 1502 992 1134 -127 71 -47 O ATOM 5110 CB LEU B 223 34.489 -2.693 -7.025 1.00 11.06 C ANISOU 5110 CB LEU B 223 1551 1247 1405 -212 50 105 C ATOM 5111 CG LEU B 223 34.642 -3.523 -8.311 1.00 13.54 C ANISOU 5111 CG LEU B 223 2064 1642 1438 -97 -15 45 C ATOM 5112 CD1 LEU B 223 33.747 -4.753 -8.353 1.00 14.81 C ANISOU 5112 CD1 LEU B 223 2190 1710 1729 -128 -21 -15 C ATOM 5113 CD2 LEU B 223 34.298 -2.670 -9.558 1.00 13.91 C ANISOU 5113 CD2 LEU B 223 2013 1749 1524 -65 -122 124 C ATOM 5114 N SER B 224 35.734 -1.058 -4.379 1.00 9.32 N ANISOU 5114 N SER B 224 1113 1283 1143 -117 -44 10 N ATOM 5115 CA SER B 224 35.622 -0.072 -3.292 1.00 10.29 C ANISOU 5115 CA SER B 224 1247 1340 1323 -103 -54 -45 C ATOM 5116 C SER B 224 36.573 1.100 -3.595 1.00 10.21 C ANISOU 5116 C SER B 224 1298 1194 1389 23 81 36 C ATOM 5117 O SER B 224 36.180 2.246 -3.402 1.00 10.26 O ANISOU 5117 O SER B 224 1108 1251 1541 88 4 -88 O ATOM 5118 CB SER B 224 36.123 -0.706 -1.953 1.00 12.49 C ANISOU 5118 CB SER B 224 1807 1719 1221 -99 11 80 C ATOM 5119 OG SER B 224 35.138 -1.738 -1.654 1.00 17.23 O ANISOU 5119 OG SER B 224 1923 2338 2284 -188 -80 131 O ATOM 5120 N THR B 225 37.780 0.761 -4.076 1.00 9.73 N ANISOU 5120 N THR B 225 1015 1275 1408 -63 -58 48 N ATOM 5121 CA THR B 225 38.713 1.833 -4.481 1.00 9.98 C ANISOU 5121 CA THR B 225 1170 1237 1387 -6 57 103 C ATOM 5122 C THR B 225 38.106 2.711 -5.557 1.00 8.93 C ANISOU 5122 C THR B 225 1121 1105 1168 -29 89 -67 C ATOM 5123 O THR B 225 38.207 3.952 -5.457 1.00 8.65 O ANISOU 5123 O THR B 225 1197 1026 1064 42 -109 42 O ATOM 5124 CB THR B 225 40.043 1.222 -5.011 1.00 11.07 C ANISOU 5124 CB THR B 225 1094 1483 1631 -83 44 103 C ATOM 5125 OG1 THR B 225 40.624 0.528 -3.885 1.00 12.28 O ANISOU 5125 OG1 THR B 225 1230 1828 1606 210 124 106 O ATOM 5126 CG2 THR B 225 40.998 2.329 -5.494 1.00 11.30 C ANISOU 5126 CG2 THR B 225 1180 1466 1647 -77 149 106 C ATOM 5127 N LEU B 226 37.548 2.137 -6.616 1.00 7.67 N ANISOU 5127 N LEU B 226 730 1122 1063 -86 77 48 N ATOM 5128 CA LEU B 226 36.932 2.915 -7.689 1.00 9.40 C ANISOU 5128 CA LEU B 226 1139 1074 1360 70 -2 -13 C ATOM 5129 C LEU B 226 35.840 3.827 -7.133 1.00 8.64 C ANISOU 5129 C LEU B 226 1054 1079 1149 -30 93 -43 C ATOM 5130 O LEU B 226 35.699 4.960 -7.602 1.00 9.16 O ANISOU 5130 O LEU B 226 1154 1152 1175 -1 -21 5 O ATOM 5131 CB LEU B 226 36.347 1.992 -8.766 1.00 9.17 C ANISOU 5131 CB LEU B 226 1178 1282 1023 -133 -30 59 C ATOM 5132 CG LEU B 226 37.314 1.585 -9.892 1.00 13.02 C ANISOU 5132 CG LEU B 226 1534 1696 1719 -31 88 -319 C ATOM 5133 CD1 LEU B 226 38.799 1.601 -9.597 1.00 11.14 C ANISOU 5133 CD1 LEU B 226 1546 1342 1345 533 -132 -139 C ATOM 5134 CD2 LEU B 226 36.812 0.584 -10.857 1.00 10.88 C ANISOU 5134 CD2 LEU B 226 1589 990 1555 112 140 -136 C ATOM 5135 N ALA B 227 35.029 3.320 -6.199 1.00 8.41 N ANISOU 5135 N ALA B 227 848 1161 1186 -149 0 -152 N ATOM 5136 CA ALA B 227 33.948 4.166 -5.672 1.00 9.09 C ANISOU 5136 CA ALA B 227 1099 1072 1284 -93 136 -124 C ATOM 5137 C ALA B 227 34.497 5.370 -4.884 1.00 9.15 C ANISOU 5137 C ALA B 227 1079 1045 1352 -44 -68 -57 C ATOM 5138 O ALA B 227 33.858 6.441 -4.899 1.00 8.55 O ANISOU 5138 O ALA B 227 1061 919 1268 -35 -16 -79 O ATOM 5139 CB ALA B 227 33.052 3.277 -4.807 1.00 9.30 C ANISOU 5139 CB ALA B 227 1056 1073 1403 -110 104 40 C ATOM 5140 N ILE B 228 35.629 5.167 -4.202 1.00 8.28 N ANISOU 5140 N ILE B 228 913 1038 1195 -73 -13 -132 N ATOM 5141 CA ILE B 228 36.223 6.308 -3.446 1.00 9.09 C ANISOU 5141 CA ILE B 228 1194 956 1304 -118 -35 -34 C ATOM 5142 C ILE B 228 36.760 7.337 -4.427 1.00 9.02 C ANISOU 5142 C ILE B 228 1219 1057 1151 -14 -52 -32 C ATOM 5143 O ILE B 228 36.602 8.549 -4.181 1.00 9.07 O ANISOU 5143 O ILE B 228 1324 1035 1088 36 -44 -78 O ATOM 5144 CB ILE B 228 37.327 5.816 -2.488 1.00 10.32 C ANISOU 5144 CB ILE B 228 1389 1256 1277 -196 -154 -38 C ATOM 5145 CG1 ILE B 228 36.635 4.998 -1.385 1.00 11.55 C ANISOU 5145 CG1 ILE B 228 1578 1390 1419 -69 -7 88 C ATOM 5146 CG2 ILE B 228 38.133 6.960 -1.879 1.00 10.67 C ANISOU 5146 CG2 ILE B 228 1356 1367 1332 -195 -148 -61 C ATOM 5147 CD1 ILE B 228 37.663 4.233 -0.509 1.00 13.48 C ANISOU 5147 CD1 ILE B 228 1699 1896 1526 -59 -186 65 C ATOM 5148 N VAL B 229 37.350 6.911 -5.543 1.00 8.84 N ANISOU 5148 N VAL B 229 1035 1222 1102 1 -18 18 N ATOM 5149 CA VAL B 229 37.784 7.893 -6.545 1.00 9.50 C ANISOU 5149 CA VAL B 229 1186 1157 1267 39 -7 77 C ATOM 5150 C VAL B 229 36.573 8.678 -7.047 1.00 9.51 C ANISOU 5150 C VAL B 229 1163 1153 1296 34 -46 -39 C ATOM 5151 O VAL B 229 36.575 9.921 -7.210 1.00 9.70 O ANISOU 5151 O VAL B 229 1291 1176 1218 9 153 -9 O ATOM 5152 CB VAL B 229 38.488 7.171 -7.719 1.00 9.81 C ANISOU 5152 CB VAL B 229 1287 1219 1222 137 38 114 C ATOM 5153 CG1 VAL B 229 38.968 8.183 -8.757 1.00 10.42 C ANISOU 5153 CG1 VAL B 229 1305 1360 1293 -71 63 110 C ATOM 5154 CG2 VAL B 229 39.664 6.267 -7.289 1.00 9.86 C ANISOU 5154 CG2 VAL B 229 1141 1415 1188 80 -108 -85 C ATOM 5155 N ALA B 230 35.487 7.988 -7.380 1.00 8.98 N ANISOU 5155 N ALA B 230 1013 1047 1353 30 -10 90 N ATOM 5156 CA ALA B 230 34.261 8.612 -7.905 1.00 8.92 C ANISOU 5156 CA ALA B 230 918 1007 1463 -82 3 -27 C ATOM 5157 C ALA B 230 33.725 9.650 -6.922 1.00 8.86 C ANISOU 5157 C ALA B 230 1112 1022 1234 -61 -127 -45 C ATOM 5158 O ALA B 230 33.246 10.704 -7.355 1.00 9.24 O ANISOU 5158 O ALA B 230 1410 944 1155 -186 -178 -13 O ATOM 5159 CB ALA B 230 33.185 7.532 -8.144 1.00 8.54 C ANISOU 5159 CB ALA B 230 984 912 1350 -82 -194 42 C ATOM 5160 N ALA B 231 33.766 9.349 -5.626 1.00 8.53 N ANISOU 5160 N ALA B 231 1038 1048 1154 19 36 -119 N ATOM 5161 CA ALA B 231 33.223 10.227 -4.594 1.00 8.88 C ANISOU 5161 CA ALA B 231 1425 896 1052 -91 24 -83 C ATOM 5162 C ALA B 231 34.080 11.491 -4.459 1.00 9.03 C ANISOU 5162 C ALA B 231 1191 992 1247 -95 1 -9 C ATOM 5163 O ALA B 231 33.589 12.593 -4.201 1.00 9.74 O ANISOU 5163 O ALA B 231 1410 1021 1271 116 -94 -105 O ATOM 5164 CB ALA B 231 33.146 9.575 -3.205 1.00 8.16 C ANISOU 5164 CB ALA B 231 1269 847 986 -20 -17 -39 C ATOM 5165 N GLY B 232 35.370 11.361 -4.680 1.00 8.87 N ANISOU 5165 N GLY B 232 1169 1096 1105 3 -46 29 N ATOM 5166 CA GLY B 232 36.235 12.552 -4.788 1.00 9.52 C ANISOU 5166 CA GLY B 232 1205 1061 1350 -53 -79 73 C ATOM 5167 C GLY B 232 35.876 13.425 -5.973 1.00 10.01 C ANISOU 5167 C GLY B 232 1335 1187 1283 -38 -10 18 C ATOM 5168 O GLY B 232 35.891 14.669 -5.862 1.00 11.03 O ANISOU 5168 O GLY B 232 1472 1124 1595 -122 -64 13 O ATOM 5169 N ILE B 233 35.568 12.828 -7.127 1.00 9.61 N ANISOU 5169 N ILE B 233 1120 1296 1235 -75 -32 -70 N ATOM 5170 CA ILE B 233 35.085 13.609 -8.273 1.00 10.16 C ANISOU 5170 CA ILE B 233 1291 1210 1358 65 39 -13 C ATOM 5171 C ILE B 233 33.726 14.254 -7.975 1.00 10.10 C ANISOU 5171 C ILE B 233 1287 1148 1403 9 46 28 C ATOM 5172 O ILE B 233 33.467 15.406 -8.389 1.00 9.49 O ANISOU 5172 O ILE B 233 1261 992 1355 35 13 -50 O ATOM 5173 CB ILE B 233 35.004 12.734 -9.558 1.00 10.52 C ANISOU 5173 CB ILE B 233 1330 1289 1379 32 -66 -51 C ATOM 5174 CG1 ILE B 233 36.453 12.336 -9.967 1.00 11.51 C ANISOU 5174 CG1 ILE B 233 1391 1403 1581 41 62 -139 C ATOM 5175 CG2 ILE B 233 34.355 13.491 -10.720 1.00 11.16 C ANISOU 5175 CG2 ILE B 233 1440 1334 1467 28 -123 -18 C ATOM 5176 CD1 ILE B 233 36.566 11.238 -11.027 1.00 12.51 C ANISOU 5176 CD1 ILE B 233 1583 1543 1627 79 43 -178 C ATOM 5177 N GLU B 234 32.806 13.516 -7.337 1.00 8.85 N ANISOU 5177 N GLU B 234 1101 1153 1106 -39 -39 -76 N ATOM 5178 CA GLU B 234 31.538 14.069 -6.878 1.00 9.74 C ANISOU 5178 CA GLU B 234 1228 1187 1287 -99 49 -96 C ATOM 5179 C GLU B 234 31.766 15.304 -6.004 1.00 9.32 C ANISOU 5179 C GLU B 234 1281 1060 1202 12 -25 -30 C ATOM 5180 O GLU B 234 31.037 16.290 -6.141 1.00 9.65 O ANISOU 5180 O GLU B 234 1167 1048 1450 -52 -47 -104 O ATOM 5181 CB GLU B 234 30.792 12.961 -6.082 1.00 11.20 C ANISOU 5181 CB GLU B 234 1401 1320 1534 -107 89 126 C ATOM 5182 CG GLU B 234 29.407 13.359 -5.538 1.00 13.48 C ANISOU 5182 CG GLU B 234 1543 1725 1855 111 31 23 C ATOM 5183 CD GLU B 234 28.869 12.244 -4.606 1.00 17.30 C ANISOU 5183 CD GLU B 234 2206 2175 2193 -93 131 162 C ATOM 5184 OE1 GLU B 234 29.494 11.149 -4.399 1.00 17.65 O ANISOU 5184 OE1 GLU B 234 2317 2228 2161 -37 99 208 O ATOM 5185 OE2 GLU B 234 27.769 12.471 -4.053 1.00 18.74 O ANISOU 5185 OE2 GLU B 234 2322 2494 2306 -120 149 -9 O ATOM 5186 N ARG B 235 32.728 15.245 -5.086 1.00 8.89 N ANISOU 5186 N ARG B 235 1037 1076 1265 -125 12 -193 N ATOM 5187 CA ARG B 235 33.045 16.421 -4.253 1.00 10.14 C ANISOU 5187 CA ARG B 235 1385 1131 1338 -118 -176 -105 C ATOM 5188 C ARG B 235 33.412 17.657 -5.100 1.00 10.24 C ANISOU 5188 C ARG B 235 1314 1209 1368 -19 -1 -18 C ATOM 5189 O ARG B 235 32.937 18.764 -4.779 1.00 9.88 O ANISOU 5189 O ARG B 235 1251 1105 1398 -16 60 28 O ATOM 5190 CB ARG B 235 34.209 16.127 -3.304 1.00 10.62 C ANISOU 5190 CB ARG B 235 1360 1304 1369 21 -170 -69 C ATOM 5191 CG ARG B 235 34.423 17.313 -2.326 1.00 11.45 C ANISOU 5191 CG ARG B 235 1498 1422 1430 12 -177 -104 C ATOM 5192 CD ARG B 235 35.329 16.868 -1.172 1.00 13.70 C ANISOU 5192 CD ARG B 235 1569 1848 1786 112 -207 115 C ATOM 5193 NE ARG B 235 36.720 16.750 -1.541 1.00 15.85 N ANISOU 5193 NE ARG B 235 1780 2160 2083 49 28 117 N ATOM 5194 CZ ARG B 235 37.615 17.749 -1.371 1.00 17.41 C ANISOU 5194 CZ ARG B 235 1999 2323 2294 -54 -10 -39 C ATOM 5195 NH1 ARG B 235 37.196 18.890 -0.853 1.00 18.85 N ANISOU 5195 NH1 ARG B 235 2292 2229 2643 -53 -23 -14 N ATOM 5196 NH2 ARG B 235 38.884 17.567 -1.692 1.00 17.69 N ANISOU 5196 NH2 ARG B 235 1904 2424 2393 -60 -61 -78 N ATOM 5197 N ILE B 236 34.244 17.466 -6.128 1.00 8.52 N ANISOU 5197 N ILE B 236 985 1107 1143 -41 -169 2 N ATOM 5198 CA ILE B 236 34.584 18.578 -7.022 1.00 8.86 C ANISOU 5198 CA ILE B 236 1071 1121 1176 5 -13 18 C ATOM 5199 C ILE B 236 33.370 19.060 -7.810 1.00 9.52 C ANISOU 5199 C ILE B 236 1198 1120 1299 -4 -112 -14 C ATOM 5200 O ILE B 236 33.078 20.262 -7.900 1.00 9.99 O ANISOU 5200 O ILE B 236 1220 1116 1458 4 -97 20 O ATOM 5201 CB ILE B 236 35.665 18.095 -8.038 1.00 9.15 C ANISOU 5201 CB ILE B 236 1058 1156 1261 56 -2 25 C ATOM 5202 CG1 ILE B 236 36.921 17.652 -7.288 1.00 9.59 C ANISOU 5202 CG1 ILE B 236 1085 1187 1370 105 2 -68 C ATOM 5203 CG2 ILE B 236 35.914 19.187 -9.069 1.00 9.96 C ANISOU 5203 CG2 ILE B 236 1190 1275 1319 17 21 74 C ATOM 5204 CD1 ILE B 236 37.989 17.026 -8.174 1.00 10.12 C ANISOU 5204 CD1 ILE B 236 1204 1215 1426 40 34 -222 C ATOM 5205 N ALA B 237 32.589 18.123 -8.329 1.00 9.50 N ANISOU 5205 N ALA B 237 1158 1187 1265 -74 -123 -39 N ATOM 5206 CA ALA B 237 31.370 18.459 -9.108 1.00 9.51 C ANISOU 5206 CA ALA B 237 1077 1108 1430 -37 -79 -71 C ATOM 5207 C ALA B 237 30.370 19.197 -8.227 1.00 10.17 C ANISOU 5207 C ALA B 237 1368 1079 1417 -4 -29 -65 C ATOM 5208 O ALA B 237 29.788 20.176 -8.712 1.00 9.66 O ANISOU 5208 O ALA B 237 1217 1127 1325 28 -88 -122 O ATOM 5209 CB ALA B 237 30.756 17.160 -9.652 1.00 8.70 C ANISOU 5209 CB ALA B 237 1040 1066 1197 2 -7 -73 C ATOM 5210 N VAL B 238 30.200 18.849 -6.940 1.00 9.76 N ANISOU 5210 N VAL B 238 1272 1028 1409 -43 2 -83 N ATOM 5211 CA VAL B 238 29.221 19.586 -6.117 1.00 10.64 C ANISOU 5211 CA VAL B 238 1392 1176 1474 -80 54 -126 C ATOM 5212 C VAL B 238 29.704 21.006 -5.865 1.00 10.83 C ANISOU 5212 C VAL B 238 1243 1177 1695 -45 -46 -40 C ATOM 5213 O VAL B 238 28.965 22.000 -5.866 1.00 9.95 O ANISOU 5213 O VAL B 238 1065 1088 1627 -89 -103 -28 O ATOM 5214 CB VAL B 238 28.980 18.824 -4.814 1.00 11.25 C ANISOU 5214 CB VAL B 238 1611 1188 1476 -124 40 -108 C ATOM 5215 CG1 VAL B 238 28.266 19.602 -3.719 1.00 12.81 C ANISOU 5215 CG1 VAL B 238 1722 1531 1614 118 48 -108 C ATOM 5216 CG2 VAL B 238 28.107 17.582 -5.128 1.00 11.72 C ANISOU 5216 CG2 VAL B 238 1435 1329 1689 -157 -14 -78 C ATOM 5217 N GLU B 239 31.030 21.116 -5.668 1.00 10.23 N ANISOU 5217 N GLU B 239 1221 1203 1463 -122 -171 38 N ATOM 5218 CA GLU B 239 31.606 22.459 -5.499 1.00 10.71 C ANISOU 5218 CA GLU B 239 1402 1173 1494 -105 -80 57 C ATOM 5219 C GLU B 239 31.331 23.322 -6.718 1.00 10.71 C ANISOU 5219 C GLU B 239 1387 1276 1406 -56 -62 21 C ATOM 5220 O GLU B 239 30.855 24.455 -6.582 1.00 11.54 O ANISOU 5220 O GLU B 239 1451 1336 1597 -16 64 -97 O ATOM 5221 CB GLU B 239 33.128 22.399 -5.277 1.00 11.26 C ANISOU 5221 CB GLU B 239 1329 1310 1639 -79 -86 28 C ATOM 5222 CG GLU B 239 33.688 23.824 -5.104 1.00 14.00 C ANISOU 5222 CG GLU B 239 1759 1487 2073 -126 -42 103 C ATOM 5223 CD GLU B 239 33.555 24.341 -3.695 1.00 17.20 C ANISOU 5223 CD GLU B 239 2127 2180 2229 -68 31 -25 C ATOM 5224 OE1 GLU B 239 33.615 25.570 -3.488 1.00 19.61 O ANISOU 5224 OE1 GLU B 239 2410 2290 2750 6 118 -155 O ATOM 5225 OE2 GLU B 239 33.409 23.501 -2.766 1.00 19.12 O ANISOU 5225 OE2 GLU B 239 2508 2572 2186 -42 -92 154 O ATOM 5226 N ILE B 240 31.586 22.791 -7.926 1.00 10.06 N ANISOU 5226 N ILE B 240 1191 1311 1318 -105 -8 69 N ATOM 5227 CA ILE B 240 31.364 23.621 -9.137 1.00 10.66 C ANISOU 5227 CA ILE B 240 1375 1297 1378 -55 -22 48 C ATOM 5228 C ILE B 240 29.895 23.938 -9.260 1.00 10.73 C ANISOU 5228 C ILE B 240 1355 1321 1402 -26 49 0 C ATOM 5229 O ILE B 240 29.530 25.063 -9.638 1.00 12.04 O ANISOU 5229 O ILE B 240 1655 1455 1467 -9 50 138 O ATOM 5230 CB ILE B 240 31.931 22.891 -10.371 1.00 11.21 C ANISOU 5230 CB ILE B 240 1449 1446 1365 -66 88 45 C ATOM 5231 CG1 ILE B 240 33.469 22.873 -10.230 1.00 13.14 C ANISOU 5231 CG1 ILE B 240 1524 1682 1789 134 76 31 C ATOM 5232 CG2 ILE B 240 31.509 23.600 -11.665 1.00 12.45 C ANISOU 5232 CG2 ILE B 240 1571 1658 1500 119 -33 36 C ATOM 5233 CD1 ILE B 240 34.192 22.052 -11.296 1.00 15.71 C ANISOU 5233 CD1 ILE B 240 2159 2039 1773 69 134 -142 C ATOM 5234 N ARG B 241 28.997 23.004 -8.932 1.00 10.19 N ANISOU 5234 N ARG B 241 1289 1418 1166 -71 28 -41 N ATOM 5235 CA ARG B 241 27.551 23.319 -8.979 1.00 9.46 C ANISOU 5235 CA ARG B 241 1240 1089 1265 2 60 -84 C ATOM 5236 C ARG B 241 27.209 24.477 -8.043 1.00 10.16 C ANISOU 5236 C ARG B 241 1407 1148 1305 43 11 -29 C ATOM 5237 O ARG B 241 26.421 25.367 -8.433 1.00 11.05 O ANISOU 5237 O ARG B 241 1377 1315 1508 160 26 55 O ATOM 5238 CB ARG B 241 26.779 22.065 -8.525 1.00 9.62 C ANISOU 5238 CB ARG B 241 1239 1196 1221 -68 13 -50 C ATOM 5239 CG ARG B 241 26.787 20.988 -9.646 1.00 10.49 C ANISOU 5239 CG ARG B 241 1421 1140 1424 -104 3 -70 C ATOM 5240 CD ARG B 241 26.255 19.657 -9.141 1.00 11.05 C ANISOU 5240 CD ARG B 241 1384 1274 1541 -53 88 67 C ATOM 5241 NE ARG B 241 24.852 19.783 -8.638 1.00 11.91 N ANISOU 5241 NE ARG B 241 1318 1516 1693 -113 11 -59 N ATOM 5242 CZ ARG B 241 24.254 18.862 -7.924 1.00 12.80 C ANISOU 5242 CZ ARG B 241 1447 1573 1844 37 61 66 C ATOM 5243 NH1 ARG B 241 22.981 19.170 -7.584 1.00 12.87 N ANISOU 5243 NH1 ARG B 241 1454 1465 1971 2 202 -60 N ATOM 5244 NH2 ARG B 241 24.827 17.687 -7.555 1.00 12.81 N ANISOU 5244 NH2 ARG B 241 1731 1309 1826 -70 35 -20 N ATOM 5245 N HIS B 242 27.704 24.471 -6.810 1.00 9.43 N ANISOU 5245 N HIS B 242 1168 1137 1276 -2 -13 -89 N ATOM 5246 CA HIS B 242 27.432 25.611 -5.903 1.00 9.50 C ANISOU 5246 CA HIS B 242 1199 1162 1248 -51 61 -23 C ATOM 5247 C HIS B 242 28.019 26.928 -6.448 1.00 10.15 C ANISOU 5247 C HIS B 242 1283 1122 1451 -8 -9 38 C ATOM 5248 O HIS B 242 27.397 27.996 -6.305 1.00 10.93 O ANISOU 5248 O HIS B 242 1464 1016 1672 -29 -53 -24 O ATOM 5249 CB HIS B 242 28.144 25.411 -4.562 1.00 9.83 C ANISOU 5249 CB HIS B 242 1152 1335 1247 -20 115 125 C ATOM 5250 CG HIS B 242 27.490 24.380 -3.685 1.00 10.14 C ANISOU 5250 CG HIS B 242 1118 1396 1338 -41 112 121 C ATOM 5251 ND1 HIS B 242 26.169 24.516 -3.312 1.00 10.68 N ANISOU 5251 ND1 HIS B 242 1067 1436 1556 126 9 61 N ATOM 5252 CD2 HIS B 242 27.974 23.304 -3.060 1.00 9.98 C ANISOU 5252 CD2 HIS B 242 1143 1150 1501 -43 80 -58 C ATOM 5253 CE1 HIS B 242 25.863 23.495 -2.503 1.00 10.95 C ANISOU 5253 CE1 HIS B 242 1151 1442 1566 21 28 99 C ATOM 5254 NE2 HIS B 242 26.964 22.713 -2.317 1.00 10.60 N ANISOU 5254 NE2 HIS B 242 1097 1480 1450 3 97 -12 N ATOM 5255 N LEU B 243 29.206 26.848 -7.030 1.00 9.53 N ANISOU 5255 N LEU B 243 1214 1151 1258 -39 15 55 N ATOM 5256 CA LEU B 243 29.912 28.065 -7.464 1.00 10.12 C ANISOU 5256 CA LEU B 243 1264 1185 1394 -50 -56 94 C ATOM 5257 C LEU B 243 29.326 28.623 -8.764 1.00 11.08 C ANISOU 5257 C LEU B 243 1393 1379 1437 -18 -97 61 C ATOM 5258 O LEU B 243 29.530 29.820 -9.049 1.00 11.59 O ANISOU 5258 O LEU B 243 1446 1331 1628 -66 -240 113 O ATOM 5259 CB LEU B 243 31.426 27.833 -7.605 1.00 10.51 C ANISOU 5259 CB LEU B 243 1331 1291 1371 67 -34 12 C ATOM 5260 CG LEU B 243 32.200 27.480 -6.329 1.00 10.52 C ANISOU 5260 CG LEU B 243 1293 1295 1408 100 -60 -53 C ATOM 5261 CD1 LEU B 243 33.710 27.342 -6.687 1.00 11.02 C ANISOU 5261 CD1 LEU B 243 1294 1340 1551 54 -14 61 C ATOM 5262 CD2 LEU B 243 31.974 28.540 -5.251 1.00 12.28 C ANISOU 5262 CD2 LEU B 243 1829 1485 1352 102 -105 -38 C ATOM 5263 N GLN B 244 28.573 27.831 -9.524 1.00 9.87 N ANISOU 5263 N GLN B 244 1015 1268 1468 -42 62 13 N ATOM 5264 CA GLN B 244 27.939 28.312 -10.748 1.00 11.97 C ANISOU 5264 CA GLN B 244 1450 1565 1532 1 -70 24 C ATOM 5265 C GLN B 244 26.527 28.852 -10.485 1.00 12.86 C ANISOU 5265 C GLN B 244 1588 1643 1657 106 32 20 C ATOM 5266 O GLN B 244 25.844 29.366 -11.420 1.00 12.93 O ANISOU 5266 O GLN B 244 1746 1582 1586 134 63 99 O ATOM 5267 CB GLN B 244 27.922 27.163 -11.783 1.00 12.41 C ANISOU 5267 CB GLN B 244 1687 1527 1502 82 22 24 C ATOM 5268 CG GLN B 244 27.475 27.598 -13.187 1.00 13.90 C ANISOU 5268 CG GLN B 244 1938 1760 1583 23 -76 5 C ATOM 5269 CD GLN B 244 27.950 26.653 -14.277 1.00 14.31 C ANISOU 5269 CD GLN B 244 1965 1780 1692 -1 50 -2 C ATOM 5270 OE1 GLN B 244 28.928 25.920 -14.159 1.00 14.89 O ANISOU 5270 OE1 GLN B 244 2004 1875 1778 -2 -50 29 O ATOM 5271 NE2 GLN B 244 27.209 26.691 -15.398 1.00 15.83 N ANISOU 5271 NE2 GLN B 244 2162 2004 1850 -43 -18 -66 N ATOM 5272 N ARG B 245 26.034 28.710 -9.244 1.00 12.10 N ANISOU 5272 N ARG B 245 1476 1524 1598 93 13 11 N ATOM 5273 CA ARG B 245 24.637 29.116 -8.990 1.00 13.02 C ANISOU 5273 CA ARG B 245 1510 1532 1907 66 46 131 C ATOM 5274 C ARG B 245 24.495 30.622 -9.218 1.00 12.50 C ANISOU 5274 C ARG B 245 1385 1477 1886 71 -90 -8 C ATOM 5275 O ARG B 245 25.484 31.363 -9.088 1.00 12.23 O ANISOU 5275 O ARG B 245 1284 1415 1949 43 39 155 O ATOM 5276 CB ARG B 245 24.152 28.666 -7.607 1.00 14.26 C ANISOU 5276 CB ARG B 245 1642 2026 1752 145 12 -23 C ATOM 5277 CG ARG B 245 24.623 29.490 -6.431 1.00 15.32 C ANISOU 5277 CG ARG B 245 1939 2042 1842 -71 2 38 C ATOM 5278 CD ARG B 245 24.072 28.797 -5.118 1.00 15.77 C ANISOU 5278 CD ARG B 245 1713 2308 1972 51 107 189 C ATOM 5279 NE ARG B 245 22.640 29.164 -5.088 1.00 14.44 N ANISOU 5279 NE ARG B 245 1628 2060 1799 -20 33 34 N ATOM 5280 CZ ARG B 245 21.658 28.328 -4.787 1.00 14.82 C ANISOU 5280 CZ ARG B 245 1728 1856 2048 58 8 94 C ATOM 5281 NH1 ARG B 245 21.840 27.085 -4.371 1.00 13.23 N ANISOU 5281 NH1 ARG B 245 1528 1825 1673 153 -256 78 N ATOM 5282 NH2 ARG B 245 20.392 28.751 -4.854 1.00 14.93 N ANISOU 5282 NH2 ARG B 245 1638 1930 2103 2 -30 14 N ATOM 5283 N THR B 246 23.280 31.091 -9.566 1.00 10.69 N ANISOU 5283 N THR B 246 1269 1068 1725 26 -92 28 N ATOM 5284 CA THR B 246 23.105 32.490 -9.989 1.00 11.09 C ANISOU 5284 CA THR B 246 1305 1201 1709 91 -134 88 C ATOM 5285 C THR B 246 23.533 33.482 -8.936 1.00 11.59 C ANISOU 5285 C THR B 246 1353 1298 1754 72 -1 24 C ATOM 5286 O THR B 246 24.036 34.574 -9.311 1.00 12.94 O ANISOU 5286 O THR B 246 1423 1401 2093 -14 50 69 O ATOM 5287 CB THR B 246 21.596 32.700 -10.325 1.00 11.13 C ANISOU 5287 CB THR B 246 1340 1203 1688 128 -128 93 C ATOM 5288 OG1 THR B 246 21.239 31.748 -11.348 1.00 10.65 O ANISOU 5288 OG1 THR B 246 1364 1191 1492 165 -58 259 O ATOM 5289 CG2 THR B 246 21.303 34.128 -10.788 1.00 12.26 C ANISOU 5289 CG2 THR B 246 1652 1223 1784 88 -47 149 C ATOM 5290 N GLU B 247 23.425 33.177 -7.634 1.00 11.84 N ANISOU 5290 N GLU B 247 1388 1400 1712 136 -83 -25 N ATOM 5291 CA GLU B 247 23.785 34.093 -6.575 1.00 11.64 C ANISOU 5291 CA GLU B 247 1305 1490 1627 13 21 -35 C ATOM 5292 C GLU B 247 25.283 34.083 -6.326 1.00 11.25 C ANISOU 5292 C GLU B 247 1338 1385 1551 68 -44 -27 C ATOM 5293 O GLU B 247 25.758 34.926 -5.550 1.00 12.38 O ANISOU 5293 O GLU B 247 1439 1389 1875 56 -66 -137 O ATOM 5294 CB GLU B 247 23.049 33.807 -5.246 1.00 12.13 C ANISOU 5294 CB GLU B 247 1411 1589 1607 35 -43 88 C ATOM 5295 CG GLU B 247 21.519 33.850 -5.343 1.00 12.97 C ANISOU 5295 CG GLU B 247 1422 1739 1765 19 40 -102 C ATOM 5296 CD GLU B 247 20.880 32.525 -5.750 1.00 14.38 C ANISOU 5296 CD GLU B 247 1667 1719 2078 -13 77 -34 C ATOM 5297 OE1 GLU B 247 19.616 32.459 -5.740 1.00 14.06 O ANISOU 5297 OE1 GLU B 247 1679 1690 1973 136 24 -85 O ATOM 5298 OE2 GLU B 247 21.552 31.529 -6.131 1.00 14.25 O ANISOU 5298 OE2 GLU B 247 1544 1708 2164 114 -30 68 O ATOM 5299 N VAL B 248 26.048 33.200 -6.955 1.00 10.29 N ANISOU 5299 N VAL B 248 1259 1145 1505 12 -64 74 N ATOM 5300 CA VAL B 248 27.470 33.088 -6.610 1.00 10.47 C ANISOU 5300 CA VAL B 248 1193 1232 1552 -9 13 84 C ATOM 5301 C VAL B 248 28.284 33.472 -7.829 1.00 10.94 C ANISOU 5301 C VAL B 248 1294 1363 1501 36 -24 109 C ATOM 5302 O VAL B 248 29.088 34.420 -7.750 1.00 12.36 O ANISOU 5302 O VAL B 248 1583 1367 1746 -104 7 -12 O ATOM 5303 CB VAL B 248 27.823 31.668 -6.095 1.00 10.41 C ANISOU 5303 CB VAL B 248 1168 1410 1378 72 79 206 C ATOM 5304 CG1 VAL B 248 29.345 31.565 -5.873 1.00 10.23 C ANISOU 5304 CG1 VAL B 248 1185 1329 1375 51 -20 44 C ATOM 5305 CG2 VAL B 248 27.061 31.384 -4.796 1.00 9.21 C ANISOU 5305 CG2 VAL B 248 1244 1015 1240 -54 22 156 C ATOM 5306 N LEU B 249 28.096 32.806 -8.958 1.00 11.64 N ANISOU 5306 N LEU B 249 1438 1294 1692 61 -103 45 N ATOM 5307 CA LEU B 249 28.755 33.130 -10.219 1.00 13.51 C ANISOU 5307 CA LEU B 249 1628 1677 1828 62 -20 112 C ATOM 5308 C LEU B 249 30.268 33.204 -10.183 1.00 13.34 C ANISOU 5308 C LEU B 249 1623 1559 1887 23 -129 207 C ATOM 5309 O LEU B 249 30.870 34.047 -10.883 1.00 13.30 O ANISOU 5309 O LEU B 249 1504 1766 1784 58 -157 314 O ATOM 5310 CB LEU B 249 28.187 34.445 -10.817 1.00 15.55 C ANISOU 5310 CB LEU B 249 1922 1834 2153 148 -127 210 C ATOM 5311 CG LEU B 249 26.668 34.413 -11.117 1.00 17.34 C ANISOU 5311 CG LEU B 249 2023 2155 2409 58 -40 72 C ATOM 5312 CD1 LEU B 249 26.240 35.786 -11.626 1.00 18.55 C ANISOU 5312 CD1 LEU B 249 2302 2341 2405 166 -32 235 C ATOM 5313 CD2 LEU B 249 26.317 33.368 -12.142 1.00 18.24 C ANISOU 5313 CD2 LEU B 249 2293 2283 2354 -16 -99 67 C ATOM 5314 N GLU B 250 30.935 32.284 -9.434 1.00 11.98 N ANISOU 5314 N GLU B 250 1539 1330 1684 -17 -119 120 N ATOM 5315 CA GLU B 250 32.366 32.274 -9.367 1.00 11.73 C ANISOU 5315 CA GLU B 250 1523 1433 1501 -69 -55 5 C ATOM 5316 C GLU B 250 33.045 31.427 -10.416 1.00 12.87 C ANISOU 5316 C GLU B 250 1651 1554 1686 -18 3 -15 C ATOM 5317 O GLU B 250 34.205 31.685 -10.780 1.00 13.84 O ANISOU 5317 O GLU B 250 1555 1654 2051 -123 -135 -41 O ATOM 5318 CB GLU B 250 32.848 31.843 -7.947 1.00 11.23 C ANISOU 5318 CB GLU B 250 1383 1393 1490 -34 42 58 C ATOM 5319 CG GLU B 250 32.577 33.016 -6.982 1.00 11.29 C ANISOU 5319 CG GLU B 250 1413 1336 1540 -162 -4 -55 C ATOM 5320 CD GLU B 250 32.813 32.728 -5.518 1.00 13.01 C ANISOU 5320 CD GLU B 250 1646 1663 1634 -88 55 5 C ATOM 5321 OE1 GLU B 250 33.337 31.637 -5.147 1.00 14.64 O ANISOU 5321 OE1 GLU B 250 1853 1742 1967 -50 32 57 O ATOM 5322 OE2 GLU B 250 32.541 33.590 -4.624 1.00 14.13 O ANISOU 5322 OE2 GLU B 250 1917 1501 1949 -226 107 -88 O ATOM 5323 N VAL B 251 32.385 30.367 -10.918 1.00 12.42 N ANISOU 5323 N VAL B 251 1531 1489 1698 -28 -99 50 N ATOM 5324 CA VAL B 251 32.996 29.520 -11.939 1.00 14.76 C ANISOU 5324 CA VAL B 251 1886 1896 1827 10 -7 -80 C ATOM 5325 C VAL B 251 31.894 29.181 -12.934 1.00 15.48 C ANISOU 5325 C VAL B 251 1828 2027 2025 -9 2 -124 C ATOM 5326 O VAL B 251 30.695 29.244 -12.554 1.00 15.80 O ANISOU 5326 O VAL B 251 1685 2087 2231 48 -11 -301 O ATOM 5327 CB VAL B 251 33.538 28.217 -11.285 1.00 17.53 C ANISOU 5327 CB VAL B 251 2279 2198 2183 282 -144 -5 C ATOM 5328 CG1 VAL B 251 34.006 27.161 -12.278 1.00 20.01 C ANISOU 5328 CG1 VAL B 251 2688 2596 2319 196 -28 -167 C ATOM 5329 CG2 VAL B 251 34.699 28.478 -10.339 1.00 17.10 C ANISOU 5329 CG2 VAL B 251 2166 2088 2243 34 -30 -16 C ATOM 5330 N GLU B 252 32.260 28.716 -14.116 1.00 15.74 N ANISOU 5330 N GLU B 252 1891 2182 1909 -25 83 -17 N ATOM 5331 CA GLU B 252 31.261 28.229 -15.080 1.00 17.16 C ANISOU 5331 CA GLU B 252 2170 2127 2223 -96 -62 -166 C ATOM 5332 C GLU B 252 31.888 27.051 -15.816 1.00 16.44 C ANISOU 5332 C GLU B 252 2085 1965 2198 -108 -29 -50 C ATOM 5333 O GLU B 252 32.977 27.166 -16.372 1.00 15.74 O ANISOU 5333 O GLU B 252 2070 1843 2069 -109 -100 -153 O ATOM 5334 CB GLU B 252 30.877 29.368 -16.030 1.00 20.90 C ANISOU 5334 CB GLU B 252 2787 2565 2589 56 71 169 C ATOM 5335 CG GLU B 252 29.897 29.087 -17.153 1.00 25.88 C ANISOU 5335 CG GLU B 252 3315 3385 3134 -43 -179 -37 C ATOM 5336 CD GLU B 252 29.834 30.350 -18.032 1.00 30.14 C ANISOU 5336 CD GLU B 252 4059 3681 3713 77 -83 218 C ATOM 5337 OE1 GLU B 252 30.209 30.277 -19.219 1.00 31.97 O ANISOU 5337 OE1 GLU B 252 4277 4026 3844 136 32 104 O ATOM 5338 OE2 GLU B 252 29.455 31.437 -17.518 1.00 31.74 O ANISOU 5338 OE2 GLU B 252 4291 3924 3845 156 -54 61 O ATOM 5339 N GLU B 253 31.211 25.892 -15.784 1.00 15.84 N ANISOU 5339 N GLU B 253 2058 1845 2113 -60 -10 -44 N ATOM 5340 CA GLU B 253 31.764 24.733 -16.491 1.00 15.49 C ANISOU 5340 CA GLU B 253 1986 1807 2093 -25 84 -12 C ATOM 5341 C GLU B 253 31.713 25.008 -17.991 1.00 15.98 C ANISOU 5341 C GLU B 253 2031 1917 2125 37 48 55 C ATOM 5342 O GLU B 253 30.974 25.866 -18.478 1.00 15.44 O ANISOU 5342 O GLU B 253 1691 2096 2080 68 110 -57 O ATOM 5343 CB GLU B 253 31.001 23.451 -16.108 1.00 16.43 C ANISOU 5343 CB GLU B 253 2066 1875 2301 -39 55 -17 C ATOM 5344 CG GLU B 253 29.597 23.379 -16.595 1.00 16.89 C ANISOU 5344 CG GLU B 253 2069 2087 2262 -104 74 47 C ATOM 5345 CD GLU B 253 28.872 22.058 -16.424 1.00 17.19 C ANISOU 5345 CD GLU B 253 2160 1982 2389 -7 82 51 C ATOM 5346 OE1 GLU B 253 28.116 21.664 -17.339 1.00 18.31 O ANISOU 5346 OE1 GLU B 253 2472 2195 2289 -69 136 61 O ATOM 5347 OE2 GLU B 253 28.996 21.424 -15.333 1.00 17.30 O ANISOU 5347 OE2 GLU B 253 2086 2068 2418 -57 62 95 O ATOM 5348 N PRO B 254 32.612 24.411 -18.756 1.00 16.85 N ANISOU 5348 N PRO B 254 2096 2033 2272 12 96 -32 N ATOM 5349 CA PRO B 254 32.673 24.609 -20.192 1.00 20.16 C ANISOU 5349 CA PRO B 254 2646 2625 2389 123 69 42 C ATOM 5350 C PRO B 254 31.404 24.091 -20.868 1.00 23.55 C ANISOU 5350 C PRO B 254 2893 3024 3032 -138 12 -40 C ATOM 5351 O PRO B 254 30.691 23.239 -20.317 1.00 20.76 O ANISOU 5351 O PRO B 254 2895 2614 2380 0 -82 -56 O ATOM 5352 CB PRO B 254 33.879 23.792 -20.639 1.00 20.45 C ANISOU 5352 CB PRO B 254 2598 2780 2391 141 71 69 C ATOM 5353 CG PRO B 254 34.296 22.954 -19.511 1.00 18.96 C ANISOU 5353 CG PRO B 254 2364 2492 2349 194 163 36 C ATOM 5354 CD PRO B 254 33.533 23.336 -18.260 1.00 17.09 C ANISOU 5354 CD PRO B 254 2034 2181 2278 88 93 -5 C ATOM 5355 N PHE B 255 31.065 24.660 -22.031 1.00 28.31 N ANISOU 5355 N PHE B 255 3917 3631 3207 93 100 190 N ATOM 5356 CA PHE B 255 29.802 24.273 -22.661 1.00 34.96 C ANISOU 5356 CA PHE B 255 4296 4586 4402 -162 -153 4 C ATOM 5357 C PHE B 255 29.881 24.256 -24.185 1.00 38.33 C ANISOU 5357 C PHE B 255 4996 5040 4527 -24 53 16 C ATOM 5358 O PHE B 255 30.879 24.615 -24.759 1.00 38.15 O ANISOU 5358 O PHE B 255 4938 5067 4492 -18 17 8 O ATOM 5359 CB PHE B 255 28.658 25.213 -22.247 1.00 37.42 C ANISOU 5359 CB PHE B 255 4674 4870 4673 40 -21 -49 C ATOM 5360 CG PHE B 255 28.901 26.635 -22.656 1.00 39.88 C ANISOU 5360 CG PHE B 255 5069 5001 5083 -19 -5 69 C ATOM 5361 CD1 PHE B 255 29.505 27.513 -21.775 1.00 40.64 C ANISOU 5361 CD1 PHE B 255 5172 5188 5081 8 -14 -22 C ATOM 5362 CD2 PHE B 255 28.525 27.097 -23.912 1.00 40.86 C ANISOU 5362 CD2 PHE B 255 5215 5245 5064 -10 -18 34 C ATOM 5363 CE1 PHE B 255 29.749 28.827 -22.130 1.00 41.69 C ANISOU 5363 CE1 PHE B 255 5365 5223 5252 28 9 14 C ATOM 5364 CE2 PHE B 255 28.769 28.412 -24.275 1.00 41.38 C ANISOU 5364 CE2 PHE B 255 5283 5220 5219 46 4 13 C ATOM 5365 CZ PHE B 255 29.384 29.278 -23.392 1.00 41.81 C ANISOU 5365 CZ PHE B 255 5357 5257 5271 48 -34 1 C ATOM 5366 N ARG B 256 28.757 23.904 -24.779 1.00 41.69 N ANISOU 5366 N ARG B 256 5182 5444 5214 -57 -112 -10 N ATOM 5367 CA ARG B 256 28.446 23.852 -26.193 1.00 43.40 C ANISOU 5367 CA ARG B 256 5556 5648 5285 0 -56 -8 C ATOM 5368 C ARG B 256 29.471 24.455 -27.131 1.00 44.11 C ANISOU 5368 C ARG B 256 5662 5586 5512 4 22 47 C ATOM 5369 O ARG B 256 30.351 23.721 -27.610 1.00 46.88 O ANISOU 5369 O ARG B 256 5901 5951 5961 193 47 -93 O ATOM 5370 CB ARG B 256 27.088 24.535 -26.421 1.00 44.40 C ANISOU 5370 CB ARG B 256 5625 5723 5521 39 -85 5 C ATOM 5371 N LYS B 257 29.366 25.741 -27.427 1.00 43.22 N ANISOU 5371 N LYS B 257 5490 5545 5385 20 47 69 N ATOM 5372 CA LYS B 257 30.239 26.463 -28.336 1.00 42.23 C ANISOU 5372 CA LYS B 257 5220 5524 5301 128 -9 50 C ATOM 5373 C LYS B 257 29.414 26.972 -29.535 1.00 42.52 C ANISOU 5373 C LYS B 257 5232 5567 5355 142 -24 98 C ATOM 5374 O LYS B 257 28.221 27.312 -29.257 1.00 43.80 O ANISOU 5374 O LYS B 257 5287 5791 5566 160 57 44 O ATOM 5375 CB LYS B 257 31.440 25.678 -28.846 1.00 42.44 C ANISOU 5375 CB LYS B 257 5289 5470 5368 119 34 -5 C ATOM 5376 N SER B 263 25.018 33.216 -30.054 1.00 49.35 N ANISOU 5376 N SER B 263 6276 6340 6134 45 -13 45 N ATOM 5377 CA SER B 263 25.749 32.725 -28.847 1.00 48.40 C ANISOU 5377 CA SER B 263 6121 6237 6032 36 100 61 C ATOM 5378 C SER B 263 24.788 32.378 -27.716 1.00 46.50 C ANISOU 5378 C SER B 263 5922 5975 5771 105 -65 84 C ATOM 5379 O SER B 263 23.599 32.699 -27.765 1.00 46.71 O ANISOU 5379 O SER B 263 5857 6144 5748 67 32 64 O ATOM 5380 CB SER B 263 26.815 33.721 -28.405 1.00 49.99 C ANISOU 5380 CB SER B 263 6336 6372 6284 -38 -5 -4 C ATOM 5381 OG SER B 263 26.303 35.041 -28.342 1.00 51.78 O ANISOU 5381 OG SER B 263 6636 6469 6571 45 9 36 O ATOM 5382 N ALA B 264 25.294 31.684 -26.693 1.00 43.40 N ANISOU 5382 N ALA B 264 5444 5627 5420 14 156 -16 N ATOM 5383 CA ALA B 264 24.472 31.221 -25.581 1.00 40.35 C ANISOU 5383 CA ALA B 264 5154 5070 5108 115 -8 -88 C ATOM 5384 C ALA B 264 23.990 32.356 -24.678 1.00 37.06 C ANISOU 5384 C ALA B 264 4567 4832 4684 -34 47 89 C ATOM 5385 O ALA B 264 24.617 33.407 -24.564 1.00 36.26 O ANISOU 5385 O ALA B 264 4548 4732 4499 55 22 54 O ATOM 5386 CB ALA B 264 25.292 30.249 -24.735 1.00 41.00 C ANISOU 5386 CB ALA B 264 5202 5216 5159 95 26 48 C ATOM 5387 N MET B 265 22.853 32.135 -24.016 1.00 33.69 N ANISOU 5387 N MET B 265 4421 4216 4165 57 -65 -64 N ATOM 5388 CA MET B 265 22.285 33.114 -23.100 1.00 30.06 C ANISOU 5388 CA MET B 265 3725 3864 3831 -39 -107 158 C ATOM 5389 C MET B 265 23.117 33.146 -21.819 1.00 28.84 C ANISOU 5389 C MET B 265 3679 3598 3681 -37 -10 16 C ATOM 5390 O MET B 265 23.334 32.100 -21.177 1.00 28.78 O ANISOU 5390 O MET B 265 3562 3625 3748 55 -142 -35 O ATOM 5391 CB MET B 265 20.834 32.810 -22.740 1.00 27.91 C ANISOU 5391 CB MET B 265 3632 3534 3438 104 -178 229 C ATOM 5392 CG MET B 265 19.850 32.936 -23.902 1.00 25.82 C ANISOU 5392 CG MET B 265 3529 2895 3387 156 -83 323 C ATOM 5393 SD MET B 265 19.482 34.688 -24.289 1.00 20.06 S ANISOU 5393 SD MET B 265 2671 2843 2109 358 -237 681 S ATOM 5394 CE MET B 265 18.420 34.404 -25.716 1.00 24.58 C ANISOU 5394 CE MET B 265 3182 3384 2774 23 -335 71 C ATOM 5395 N PRO B 266 23.530 34.338 -21.416 1.00 27.01 N ANISOU 5395 N PRO B 266 3346 3484 3433 21 58 72 N ATOM 5396 CA PRO B 266 24.417 34.537 -20.291 1.00 26.01 C ANISOU 5396 CA PRO B 266 3269 3299 3316 36 120 56 C ATOM 5397 C PRO B 266 23.862 34.065 -18.958 1.00 24.82 C ANISOU 5397 C PRO B 266 3008 3151 3272 61 41 65 C ATOM 5398 O PRO B 266 24.579 33.597 -18.059 1.00 24.07 O ANISOU 5398 O PRO B 266 2809 3047 3288 157 102 -27 O ATOM 5399 CB PRO B 266 24.646 36.050 -20.258 1.00 26.64 C ANISOU 5399 CB PRO B 266 3344 3323 3456 -1 69 24 C ATOM 5400 CG PRO B 266 23.442 36.643 -20.927 1.00 27.44 C ANISOU 5400 CG PRO B 266 3471 3470 3487 14 -13 48 C ATOM 5401 CD PRO B 266 22.995 35.630 -21.954 1.00 27.47 C ANISOU 5401 CD PRO B 266 3480 3452 3505 -8 32 52 C ATOM 5402 N HIS B 267 22.544 34.209 -18.802 1.00 23.38 N ANISOU 5402 N HIS B 267 2945 2905 3034 139 27 154 N ATOM 5403 CA HIS B 267 21.891 33.902 -17.533 1.00 23.46 C ANISOU 5403 CA HIS B 267 2898 2932 3084 128 83 79 C ATOM 5404 C HIS B 267 21.458 32.450 -17.431 1.00 23.84 C ANISOU 5404 C HIS B 267 2989 2970 3100 103 53 104 C ATOM 5405 O HIS B 267 20.931 32.085 -16.377 1.00 26.12 O ANISOU 5405 O HIS B 267 3434 3157 3334 34 190 294 O ATOM 5406 CB HIS B 267 20.678 34.805 -17.279 1.00 23.04 C ANISOU 5406 CB HIS B 267 2918 2881 2956 143 92 54 C ATOM 5407 CG HIS B 267 19.624 34.781 -18.343 1.00 24.03 C ANISOU 5407 CG HIS B 267 3004 3021 3103 72 26 -38 C ATOM 5408 ND1 HIS B 267 19.924 35.109 -19.658 1.00 24.46 N ANISOU 5408 ND1 HIS B 267 3088 3052 3155 119 48 29 N ATOM 5409 CD2 HIS B 267 18.285 34.539 -18.318 1.00 23.78 C ANISOU 5409 CD2 HIS B 267 2992 2956 3089 51 82 14 C ATOM 5410 CE1 HIS B 267 18.834 35.029 -20.397 1.00 24.68 C ANISOU 5410 CE1 HIS B 267 3119 3099 3161 37 18 56 C ATOM 5411 NE2 HIS B 267 17.822 34.675 -19.609 1.00 24.50 N ANISOU 5411 NE2 HIS B 267 2995 3141 3174 147 51 22 N ATOM 5412 N LYS B 268 21.614 31.624 -18.432 1.00 23.07 N ANISOU 5412 N LYS B 268 2925 2855 2987 109 -79 159 N ATOM 5413 CA LYS B 268 21.080 30.270 -18.414 1.00 24.50 C ANISOU 5413 CA LYS B 268 3044 2967 3299 60 51 96 C ATOM 5414 C LYS B 268 22.205 29.254 -18.567 1.00 21.76 C ANISOU 5414 C LYS B 268 2800 2728 2742 -49 -99 88 C ATOM 5415 O LYS B 268 22.057 28.255 -19.275 1.00 21.79 O ANISOU 5415 O LYS B 268 2752 2634 2893 -89 -184 134 O ATOM 5416 CB LYS B 268 20.028 30.119 -19.529 1.00 28.41 C ANISOU 5416 CB LYS B 268 3586 3662 3546 -112 -183 78 C ATOM 5417 CG LYS B 268 18.773 30.947 -19.221 1.00 33.07 C ANISOU 5417 CG LYS B 268 4035 4106 4425 112 99 -20 C ATOM 5418 CD LYS B 268 17.998 31.273 -20.486 1.00 37.39 C ANISOU 5418 CD LYS B 268 4723 4855 4628 90 -113 88 C ATOM 5419 CE LYS B 268 17.014 30.196 -20.903 1.00 40.44 C ANISOU 5419 CE LYS B 268 5035 5106 5225 -111 -37 -16 C ATOM 5420 NZ LYS B 268 15.589 30.600 -20.628 1.00 42.38 N ANISOU 5420 NZ LYS B 268 5198 5431 5475 119 33 12 N ATOM 5421 N LYS B 269 23.341 29.502 -17.927 1.00 18.20 N ANISOU 5421 N LYS B 269 2462 2154 2298 19 140 180 N ATOM 5422 CA LYS B 269 24.444 28.533 -18.019 1.00 17.81 C ANISOU 5422 CA LYS B 269 2503 2103 2162 26 25 244 C ATOM 5423 C LYS B 269 24.314 27.530 -16.866 1.00 15.98 C ANISOU 5423 C LYS B 269 2197 1839 2037 -32 20 98 C ATOM 5424 O LYS B 269 24.568 27.900 -15.721 1.00 15.68 O ANISOU 5424 O LYS B 269 2222 1827 1910 -73 5 252 O ATOM 5425 CB LYS B 269 25.800 29.224 -17.952 1.00 20.23 C ANISOU 5425 CB LYS B 269 2512 2439 2734 -5 18 114 C ATOM 5426 CG LYS B 269 26.019 30.252 -19.044 1.00 23.96 C ANISOU 5426 CG LYS B 269 3227 2849 3027 7 50 352 C ATOM 5427 CD LYS B 269 26.404 29.709 -20.394 1.00 27.01 C ANISOU 5427 CD LYS B 269 3620 3322 3320 26 39 28 C ATOM 5428 CE LYS B 269 26.813 30.853 -21.344 1.00 29.38 C ANISOU 5428 CE LYS B 269 3891 3678 3593 -75 55 232 C ATOM 5429 NZ LYS B 269 27.925 31.710 -20.831 1.00 31.11 N ANISOU 5429 NZ LYS B 269 4054 3901 3864 -104 0 38 N ATOM 5430 N ASN B 270 23.917 26.303 -17.148 1.00 14.17 N ANISOU 5430 N ASN B 270 1896 1740 1749 34 -5 224 N ATOM 5431 CA ASN B 270 23.615 25.359 -16.067 1.00 13.13 C ANISOU 5431 CA ASN B 270 1637 1603 1747 92 -37 214 C ATOM 5432 C ASN B 270 24.771 24.365 -15.903 1.00 12.78 C ANISOU 5432 C ASN B 270 1696 1502 1658 121 -2 152 C ATOM 5433 O ASN B 270 25.332 23.927 -16.901 1.00 12.93 O ANISOU 5433 O ASN B 270 1804 1393 1714 187 88 265 O ATOM 5434 CB ASN B 270 22.408 24.529 -16.520 1.00 13.12 C ANISOU 5434 CB ASN B 270 1577 1697 1710 77 -90 180 C ATOM 5435 CG ASN B 270 21.180 25.438 -16.642 1.00 14.16 C ANISOU 5435 CG ASN B 270 1777 1767 1836 170 -74 16 C ATOM 5436 OD1 ASN B 270 20.918 26.182 -15.714 1.00 13.79 O ANISOU 5436 OD1 ASN B 270 1788 1549 1901 164 -84 39 O ATOM 5437 ND2 ASN B 270 20.436 25.294 -17.745 1.00 15.49 N ANISOU 5437 ND2 ASN B 270 1798 2145 1942 170 -206 258 N ATOM 5438 N PRO B 271 25.090 23.947 -14.701 1.00 12.04 N ANISOU 5438 N PRO B 271 1579 1369 1627 143 -52 70 N ATOM 5439 CA PRO B 271 26.211 23.029 -14.461 1.00 11.69 C ANISOU 5439 CA PRO B 271 1481 1356 1605 78 -73 -17 C ATOM 5440 C PRO B 271 25.791 21.577 -14.700 1.00 12.09 C ANISOU 5440 C PRO B 271 1495 1407 1691 15 -114 6 C ATOM 5441 O PRO B 271 25.945 20.700 -13.835 1.00 11.58 O ANISOU 5441 O PRO B 271 1416 1457 1529 -85 -194 29 O ATOM 5442 CB PRO B 271 26.596 23.313 -13.020 1.00 11.52 C ANISOU 5442 CB PRO B 271 1419 1449 1509 145 0 49 C ATOM 5443 CG PRO B 271 25.291 23.746 -12.374 1.00 11.04 C ANISOU 5443 CG PRO B 271 1363 1372 1461 85 8 100 C ATOM 5444 CD PRO B 271 24.582 24.549 -13.440 1.00 12.57 C ANISOU 5444 CD PRO B 271 1616 1642 1519 141 -49 129 C ATOM 5445 N ILE B 272 25.308 21.282 -15.897 1.00 11.33 N ANISOU 5445 N ILE B 272 1396 1385 1524 253 5 -97 N ATOM 5446 CA ILE B 272 24.738 19.980 -16.228 1.00 13.04 C ANISOU 5446 CA ILE B 272 1519 1475 1961 84 26 -3 C ATOM 5447 C ILE B 272 25.773 18.861 -16.185 1.00 11.74 C ANISOU 5447 C ILE B 272 1434 1360 1666 49 70 22 C ATOM 5448 O ILE B 272 25.490 17.718 -15.782 1.00 12.87 O ANISOU 5448 O ILE B 272 1510 1496 1884 16 53 137 O ATOM 5449 CB ILE B 272 24.274 20.069 -17.719 1.00 17.38 C ANISOU 5449 CB ILE B 272 2249 2142 2213 122 -273 -76 C ATOM 5450 CG1 ILE B 272 23.191 21.127 -17.858 1.00 19.98 C ANISOU 5450 CG1 ILE B 272 2408 2422 2762 203 -87 -83 C ATOM 5451 CG2 ILE B 272 23.715 18.727 -18.171 1.00 19.07 C ANISOU 5451 CG2 ILE B 272 2378 2148 2719 17 -185 19 C ATOM 5452 CD1 ILE B 272 22.019 20.823 -16.956 1.00 20.92 C ANISOU 5452 CD1 ILE B 272 2531 2544 2874 18 47 -40 C ATOM 5453 N THR B 273 26.969 19.157 -16.687 1.00 10.75 N ANISOU 5453 N THR B 273 1301 1156 1629 71 11 51 N ATOM 5454 CA THR B 273 28.031 18.117 -16.665 1.00 11.16 C ANISOU 5454 CA THR B 273 1261 1399 1581 109 72 118 C ATOM 5455 C THR B 273 28.318 17.677 -15.234 1.00 11.06 C ANISOU 5455 C THR B 273 1365 1269 1567 3 43 34 C ATOM 5456 O THR B 273 28.368 16.473 -14.977 1.00 10.32 O ANISOU 5456 O THR B 273 1270 1061 1591 -38 -2 -109 O ATOM 5457 CB THR B 273 29.342 18.646 -17.282 1.00 12.61 C ANISOU 5457 CB THR B 273 1361 1668 1761 132 126 177 C ATOM 5458 OG1 THR B 273 29.030 19.047 -18.620 1.00 13.36 O ANISOU 5458 OG1 THR B 273 1610 1866 1599 -44 99 22 O ATOM 5459 CG2 THR B 273 30.376 17.513 -17.354 1.00 12.49 C ANISOU 5459 CG2 THR B 273 1305 1722 1718 168 103 66 C ATOM 5460 N CYS B 274 28.422 18.616 -14.301 1.00 10.28 N ANISOU 5460 N CYS B 274 1185 1332 1390 -62 57 1 N ATOM 5461 CA CYS B 274 28.745 18.304 -12.914 1.00 10.48 C ANISOU 5461 CA CYS B 274 1218 1359 1405 -125 48 21 C ATOM 5462 C CYS B 274 27.559 17.628 -12.250 1.00 9.98 C ANISOU 5462 C CYS B 274 1033 1382 1376 29 -37 66 C ATOM 5463 O CYS B 274 27.759 16.783 -11.354 1.00 9.65 O ANISOU 5463 O CYS B 274 1005 1301 1359 53 -42 0 O ATOM 5464 CB CYS B 274 29.171 19.604 -12.202 1.00 10.63 C ANISOU 5464 CB CYS B 274 1181 1427 1431 -115 114 -21 C ATOM 5465 SG CYS B 274 30.819 20.164 -12.725 1.00 12.64 S ANISOU 5465 SG CYS B 274 1296 1642 1866 -419 121 34 S ATOM 5466 N GLU B 275 26.310 17.980 -12.637 1.00 8.91 N ANISOU 5466 N GLU B 275 919 1221 1245 64 -97 39 N ATOM 5467 CA GLU B 275 25.164 17.252 -12.103 1.00 9.49 C ANISOU 5467 CA GLU B 275 1070 1096 1439 108 6 13 C ATOM 5468 C GLU B 275 25.191 15.808 -12.622 1.00 9.25 C ANISOU 5468 C GLU B 275 1103 1145 1267 44 -55 11 C ATOM 5469 O GLU B 275 24.953 14.898 -11.832 1.00 8.67 O ANISOU 5469 O GLU B 275 840 1207 1248 -47 -49 53 O ATOM 5470 CB GLU B 275 23.804 17.897 -12.531 1.00 9.90 C ANISOU 5470 CB GLU B 275 1099 1248 1416 144 -104 -50 C ATOM 5471 CG GLU B 275 23.654 19.241 -11.790 1.00 11.28 C ANISOU 5471 CG GLU B 275 1360 1222 1704 218 -86 -54 C ATOM 5472 CD GLU B 275 22.469 20.070 -12.299 1.00 13.24 C ANISOU 5472 CD GLU B 275 1574 1511 1947 223 -277 7 C ATOM 5473 OE1 GLU B 275 21.606 19.539 -13.049 1.00 12.22 O ANISOU 5473 OE1 GLU B 275 1548 1389 1708 222 -153 -40 O ATOM 5474 OE2 GLU B 275 22.475 21.283 -11.895 1.00 14.50 O ANISOU 5474 OE2 GLU B 275 1784 1534 2190 269 -159 10 O ATOM 5475 N ARG B 276 25.546 15.584 -13.876 1.00 8.78 N ANISOU 5475 N ARG B 276 1024 1141 1172 -5 64 75 N ATOM 5476 CA ARG B 276 25.697 14.218 -14.384 1.00 10.74 C ANISOU 5476 CA ARG B 276 1320 1345 1416 139 9 -35 C ATOM 5477 C ARG B 276 26.779 13.461 -13.610 1.00 10.64 C ANISOU 5477 C ARG B 276 1237 1358 1448 55 33 41 C ATOM 5478 O ARG B 276 26.594 12.300 -13.211 1.00 10.31 O ANISOU 5478 O ARG B 276 1225 1314 1378 30 78 -8 O ATOM 5479 CB ARG B 276 25.977 14.247 -15.900 1.00 11.75 C ANISOU 5479 CB ARG B 276 1550 1513 1400 41 54 -5 C ATOM 5480 CG ARG B 276 26.273 12.825 -16.444 1.00 15.13 C ANISOU 5480 CG ARG B 276 2058 1616 2073 20 36 -147 C ATOM 5481 CD ARG B 276 26.700 12.900 -17.936 1.00 19.79 C ANISOU 5481 CD ARG B 276 2753 2500 2264 25 211 -62 C ATOM 5482 NE ARG B 276 25.764 13.766 -18.651 1.00 23.54 N ANISOU 5482 NE ARG B 276 3112 3033 2800 134 -95 -6 N ATOM 5483 CZ ARG B 276 26.200 14.798 -19.380 1.00 26.90 C ANISOU 5483 CZ ARG B 276 3595 3420 3207 -23 9 150 C ATOM 5484 NH1 ARG B 276 27.500 15.051 -19.515 1.00 28.98 N ANISOU 5484 NH1 ARG B 276 3677 3763 3571 -72 39 41 N ATOM 5485 NH2 ARG B 276 25.339 15.611 -19.977 1.00 28.12 N ANISOU 5485 NH2 ARG B 276 3747 3492 3444 173 -14 106 N ATOM 5486 N LEU B 277 27.936 14.094 -13.378 1.00 10.01 N ANISOU 5486 N LEU B 277 1118 1390 1294 112 -15 -110 N ATOM 5487 CA LEU B 277 28.995 13.421 -12.598 1.00 9.32 C ANISOU 5487 CA LEU B 277 1083 1191 1267 -18 12 78 C ATOM 5488 C LEU B 277 28.532 13.051 -11.198 1.00 9.38 C ANISOU 5488 C LEU B 277 1068 1238 1259 -25 -10 2 C ATOM 5489 O LEU B 277 28.866 11.980 -10.681 1.00 9.37 O ANISOU 5489 O LEU B 277 908 1323 1330 77 12 -10 O ATOM 5490 CB LEU B 277 30.235 14.327 -12.419 1.00 10.76 C ANISOU 5490 CB LEU B 277 1182 1392 1514 -123 60 115 C ATOM 5491 CG LEU B 277 30.961 14.602 -13.773 1.00 12.29 C ANISOU 5491 CG LEU B 277 1563 1531 1574 -125 208 -41 C ATOM 5492 CD1 LEU B 277 32.063 15.642 -13.536 1.00 13.14 C ANISOU 5492 CD1 LEU B 277 1419 1741 1833 -159 177 -51 C ATOM 5493 CD2 LEU B 277 31.565 13.314 -14.287 1.00 13.40 C ANISOU 5493 CD2 LEU B 277 1734 1652 1704 -2 213 -100 C ATOM 5494 N THR B 278 27.751 13.897 -10.530 1.00 9.62 N ANISOU 5494 N THR B 278 1098 1294 1262 79 1 13 N ATOM 5495 CA THR B 278 27.221 13.551 -9.224 1.00 9.87 C ANISOU 5495 CA THR B 278 1190 1353 1208 9 5 11 C ATOM 5496 C THR B 278 26.367 12.283 -9.296 1.00 10.29 C ANISOU 5496 C THR B 278 1302 1240 1368 73 -29 30 C ATOM 5497 O THR B 278 26.491 11.372 -8.468 1.00 9.79 O ANISOU 5497 O THR B 278 1312 1203 1203 -72 -40 16 O ATOM 5498 CB THR B 278 26.394 14.714 -8.655 1.00 11.27 C ANISOU 5498 CB THR B 278 1521 1402 1358 97 53 17 C ATOM 5499 OG1 THR B 278 27.094 15.936 -8.700 1.00 12.94 O ANISOU 5499 OG1 THR B 278 1580 1687 1650 -39 43 -62 O ATOM 5500 CG2 THR B 278 25.917 14.444 -7.233 1.00 11.59 C ANISOU 5500 CG2 THR B 278 1591 1461 1351 70 32 -78 C ATOM 5501 N GLY B 279 25.470 12.174 -10.283 1.00 9.85 N ANISOU 5501 N GLY B 279 1154 1128 1460 90 -28 -60 N ATOM 5502 CA GLY B 279 24.640 10.975 -10.469 1.00 10.19 C ANISOU 5502 CA GLY B 279 1058 1178 1634 115 35 8 C ATOM 5503 C GLY B 279 25.482 9.736 -10.721 1.00 9.61 C ANISOU 5503 C GLY B 279 1163 1032 1456 -1 97 44 C ATOM 5504 O GLY B 279 25.211 8.689 -10.160 1.00 9.33 O ANISOU 5504 O GLY B 279 899 1046 1599 79 103 200 O ATOM 5505 N LEU B 280 26.473 9.836 -11.593 1.00 8.71 N ANISOU 5505 N LEU B 280 907 1015 1389 133 56 -30 N ATOM 5506 CA LEU B 280 27.337 8.662 -11.886 1.00 8.68 C ANISOU 5506 CA LEU B 280 1096 1006 1194 175 -20 30 C ATOM 5507 C LEU B 280 28.098 8.274 -10.633 1.00 8.21 C ANISOU 5507 C LEU B 280 1025 1005 1091 120 -41 -54 C ATOM 5508 O LEU B 280 28.339 7.043 -10.450 1.00 8.56 O ANISOU 5508 O LEU B 280 1177 955 1120 104 -174 -55 O ATOM 5509 CB LEU B 280 28.285 9.080 -13.029 1.00 8.95 C ANISOU 5509 CB LEU B 280 1211 1134 1055 144 -5 -50 C ATOM 5510 CG LEU B 280 27.623 9.226 -14.407 1.00 9.22 C ANISOU 5510 CG LEU B 280 1169 1181 1151 -39 -38 56 C ATOM 5511 CD1 LEU B 280 28.682 9.599 -15.437 1.00 9.80 C ANISOU 5511 CD1 LEU B 280 1319 1444 962 2 51 -31 C ATOM 5512 CD2 LEU B 280 26.856 7.961 -14.788 1.00 9.73 C ANISOU 5512 CD2 LEU B 280 1201 1345 1151 -102 -91 -74 C ATOM 5513 N SER B 281 28.511 9.200 -9.761 1.00 8.18 N ANISOU 5513 N SER B 281 945 953 1208 137 -75 -75 N ATOM 5514 CA SER B 281 29.095 8.753 -8.475 1.00 9.69 C ANISOU 5514 CA SER B 281 1414 1143 1125 -105 -63 -15 C ATOM 5515 C SER B 281 28.140 7.889 -7.666 1.00 9.36 C ANISOU 5515 C SER B 281 1145 1097 1317 -14 -50 -66 C ATOM 5516 O SER B 281 28.589 6.946 -6.974 1.00 10.36 O ANISOU 5516 O SER B 281 1317 1147 1472 7 71 89 O ATOM 5517 CB SER B 281 29.499 10.001 -7.644 1.00 11.71 C ANISOU 5517 CB SER B 281 1696 1207 1547 -318 -177 -23 C ATOM 5518 OG SER B 281 30.193 9.478 -6.496 1.00 16.52 O ANISOU 5518 OG SER B 281 2014 2161 2102 14 -324 78 O ATOM 5519 N ARG B 282 26.805 8.168 -7.687 1.00 9.28 N ANISOU 5519 N ARG B 282 1049 1057 1418 -39 2 -85 N ATOM 5520 CA ARG B 282 25.857 7.306 -7.000 1.00 9.10 C ANISOU 5520 CA ARG B 282 981 1110 1366 84 -59 93 C ATOM 5521 C ARG B 282 25.866 5.889 -7.550 1.00 9.10 C ANISOU 5521 C ARG B 282 1019 1217 1221 60 -54 -42 C ATOM 5522 O ARG B 282 25.782 4.932 -6.760 1.00 10.08 O ANISOU 5522 O ARG B 282 1223 1168 1438 -38 -83 -96 O ATOM 5523 CB ARG B 282 24.405 7.847 -7.119 1.00 9.88 C ANISOU 5523 CB ARG B 282 939 1242 1571 132 34 2 C ATOM 5524 CG ARG B 282 24.300 9.230 -6.433 1.00 10.52 C ANISOU 5524 CG ARG B 282 935 1353 1708 181 -68 -25 C ATOM 5525 CD ARG B 282 22.857 9.782 -6.680 1.00 9.33 C ANISOU 5525 CD ARG B 282 898 1224 1422 195 -97 111 C ATOM 5526 NE ARG B 282 22.949 11.167 -6.156 1.00 11.59 N ANISOU 5526 NE ARG B 282 1345 1325 1734 59 0 38 N ATOM 5527 CZ ARG B 282 22.192 12.185 -6.597 1.00 12.82 C ANISOU 5527 CZ ARG B 282 1605 1412 1853 106 -105 10 C ATOM 5528 NH1 ARG B 282 21.262 12.018 -7.510 1.00 11.62 N ANISOU 5528 NH1 ARG B 282 1285 1317 1813 148 -38 155 N ATOM 5529 NH2 ARG B 282 22.406 13.426 -6.108 1.00 12.96 N ANISOU 5529 NH2 ARG B 282 1668 1429 1828 56 35 -45 N ATOM 5530 N MET B 283 26.000 5.699 -8.857 1.00 9.88 N ANISOU 5530 N MET B 283 1090 1335 1329 30 1 -49 N ATOM 5531 CA MET B 283 26.079 4.331 -9.401 1.00 9.65 C ANISOU 5531 CA MET B 283 1130 1275 1260 140 -50 -18 C ATOM 5532 C MET B 283 27.411 3.694 -9.017 1.00 9.79 C ANISOU 5532 C MET B 283 1096 1287 1336 16 -47 53 C ATOM 5533 O MET B 283 27.381 2.510 -8.676 1.00 10.86 O ANISOU 5533 O MET B 283 1189 1253 1685 -1 -24 38 O ATOM 5534 CB MET B 283 26.011 4.412 -10.944 1.00 9.76 C ANISOU 5534 CB MET B 283 1065 1406 1239 -23 -77 40 C ATOM 5535 CG MET B 283 24.585 4.754 -11.424 1.00 10.40 C ANISOU 5535 CG MET B 283 1338 1052 1560 4 -197 283 C ATOM 5536 SD MET B 283 23.293 3.596 -10.923 1.00 4.25 S ANISOU 5536 SD MET B 283 539 260 816 34 -79 -40 S ATOM 5537 CE MET B 283 23.920 1.993 -11.310 1.00 9.62 C ANISOU 5537 CE MET B 283 1430 257 1967 -46 -182 47 C ATOM 5538 N MET B 284 28.549 4.404 -8.966 1.00 9.30 N ANISOU 5538 N MET B 284 1111 1236 1186 -19 -33 -54 N ATOM 5539 CA MET B 284 29.811 3.770 -8.589 1.00 8.88 C ANISOU 5539 CA MET B 284 1005 1185 1183 -108 58 -1 C ATOM 5540 C MET B 284 29.753 3.257 -7.162 1.00 9.91 C ANISOU 5540 C MET B 284 1271 1184 1311 -71 -10 22 C ATOM 5541 O MET B 284 30.201 2.165 -6.812 1.00 10.98 O ANISOU 5541 O MET B 284 1308 1265 1599 99 -61 36 O ATOM 5542 CB MET B 284 30.961 4.823 -8.696 1.00 8.20 C ANISOU 5542 CB MET B 284 977 1120 1018 -95 26 -80 C ATOM 5543 CG MET B 284 31.260 5.282 -10.115 1.00 8.47 C ANISOU 5543 CG MET B 284 1117 1209 892 68 238 -346 C ATOM 5544 SD MET B 284 31.851 3.864 -11.244 1.00 3.35 S ANISOU 5544 SD MET B 284 255 684 333 18 -3 -34 S ATOM 5545 CE MET B 284 33.321 3.328 -10.235 1.00 5.74 C ANISOU 5545 CE MET B 284 320 968 894 -84 -195 39 C ATOM 5546 N ARG B 285 29.129 4.065 -6.262 1.00 10.37 N ANISOU 5546 N ARG B 285 1233 1221 1486 -3 39 -31 N ATOM 5547 CA ARG B 285 29.055 3.505 -4.897 1.00 11.86 C ANISOU 5547 CA ARG B 285 1522 1473 1510 -38 75 -14 C ATOM 5548 C ARG B 285 27.974 2.447 -4.827 1.00 10.46 C ANISOU 5548 C ARG B 285 1350 1349 1274 115 86 -43 C ATOM 5549 O ARG B 285 28.162 1.553 -3.984 1.00 10.70 O ANISOU 5549 O ARG B 285 1358 1176 1532 122 174 53 O ATOM 5550 CB ARG B 285 28.921 4.583 -3.843 1.00 16.09 C ANISOU 5550 CB ARG B 285 2148 2015 1950 75 50 -267 C ATOM 5551 CG ARG B 285 27.654 5.340 -3.810 1.00 17.72 C ANISOU 5551 CG ARG B 285 2207 2235 2290 167 64 -256 C ATOM 5552 CD ARG B 285 27.637 6.180 -2.467 1.00 17.61 C ANISOU 5552 CD ARG B 285 2272 2171 2248 20 -166 -233 C ATOM 5553 NE ARG B 285 26.986 7.438 -2.799 1.00 15.60 N ANISOU 5553 NE ARG B 285 1908 2130 1889 39 -48 -234 N ATOM 5554 CZ ARG B 285 27.531 8.542 -3.259 1.00 16.25 C ANISOU 5554 CZ ARG B 285 1975 2209 1989 43 -79 -91 C ATOM 5555 NH1 ARG B 285 28.845 8.656 -3.469 1.00 16.52 N ANISOU 5555 NH1 ARG B 285 1920 2308 2050 67 -97 -116 N ATOM 5556 NH2 ARG B 285 26.745 9.600 -3.503 1.00 16.55 N ANISOU 5556 NH2 ARG B 285 1925 2270 2094 108 -126 -118 N ATOM 5557 N ALA B 286 26.960 2.438 -5.677 1.00 9.29 N ANISOU 5557 N ALA B 286 1148 1033 1349 146 115 -109 N ATOM 5558 CA ALA B 286 25.981 1.331 -5.652 1.00 10.09 C ANISOU 5558 CA ALA B 286 1064 1240 1530 130 16 -113 C ATOM 5559 C ALA B 286 26.631 -0.028 -5.945 1.00 11.18 C ANISOU 5559 C ALA B 286 1378 1180 1692 99 59 27 C ATOM 5560 O ALA B 286 26.142 -1.042 -5.444 1.00 10.91 O ANISOU 5560 O ALA B 286 1214 1194 1739 97 -67 134 O ATOM 5561 CB ALA B 286 24.868 1.636 -6.677 1.00 10.09 C ANISOU 5561 CB ALA B 286 1005 1378 1453 -36 33 -64 C ATOM 5562 N TYR B 287 27.717 -0.053 -6.734 1.00 10.56 N ANISOU 5562 N TYR B 287 1187 1288 1536 99 -28 -86 N ATOM 5563 CA TYR B 287 28.375 -1.328 -7.073 1.00 11.21 C ANISOU 5563 CA TYR B 287 1389 1270 1602 141 -20 -17 C ATOM 5564 C TYR B 287 29.165 -1.929 -5.930 1.00 12.28 C ANISOU 5564 C TYR B 287 1622 1467 1574 44 -86 1 C ATOM 5565 O TYR B 287 29.537 -3.133 -5.994 1.00 13.54 O ANISOU 5565 O TYR B 287 1743 1510 1893 -17 -116 -56 O ATOM 5566 CB TYR B 287 29.340 -1.108 -8.259 1.00 12.07 C ANISOU 5566 CB TYR B 287 1663 1422 1503 133 -40 -42 C ATOM 5567 CG TYR B 287 28.679 -0.617 -9.536 1.00 12.27 C ANISOU 5567 CG TYR B 287 1650 1542 1471 72 -28 -83 C ATOM 5568 CD1 TYR B 287 29.253 0.366 -10.310 1.00 11.81 C ANISOU 5568 CD1 TYR B 287 1610 1402 1474 102 64 -176 C ATOM 5569 CD2 TYR B 287 27.462 -1.149 -9.946 1.00 12.57 C ANISOU 5569 CD2 TYR B 287 1529 1571 1677 87 7 -47 C ATOM 5570 CE1 TYR B 287 28.655 0.806 -11.494 1.00 13.01 C ANISOU 5570 CE1 TYR B 287 1657 1635 1653 193 58 -39 C ATOM 5571 CE2 TYR B 287 26.851 -0.732 -11.121 1.00 13.55 C ANISOU 5571 CE2 TYR B 287 1740 1670 1738 108 -11 -2 C ATOM 5572 CZ TYR B 287 27.452 0.244 -11.875 1.00 14.17 C ANISOU 5572 CZ TYR B 287 1864 1803 1719 44 24 -43 C ATOM 5573 OH TYR B 287 26.821 0.701 -13.007 1.00 16.88 O ANISOU 5573 OH TYR B 287 2323 2153 1938 156 -100 81 O ATOM 5574 N VAL B 288 29.445 -1.180 -4.854 1.00 10.95 N ANISOU 5574 N VAL B 288 1431 1147 1584 -81 -95 82 N ATOM 5575 CA VAL B 288 30.291 -1.713 -3.774 1.00 12.14 C ANISOU 5575 CA VAL B 288 1640 1474 1499 -72 -90 109 C ATOM 5576 C VAL B 288 29.579 -2.823 -3.005 1.00 12.80 C ANISOU 5576 C VAL B 288 1605 1476 1782 -156 -80 11 C ATOM 5577 O VAL B 288 30.147 -3.891 -2.750 1.00 12.37 O ANISOU 5577 O VAL B 288 1494 1389 1816 -222 -23 -144 O ATOM 5578 CB VAL B 288 30.716 -0.588 -2.821 1.00 12.58 C ANISOU 5578 CB VAL B 288 1790 1486 1506 -166 -139 152 C ATOM 5579 CG1 VAL B 288 31.544 -1.122 -1.620 1.00 13.82 C ANISOU 5579 CG1 VAL B 288 1879 1735 1636 1 -205 85 C ATOM 5580 CG2 VAL B 288 31.570 0.455 -3.588 1.00 13.04 C ANISOU 5580 CG2 VAL B 288 1610 1587 1758 -93 -46 170 C ATOM 5581 N ASP B 289 28.317 -2.610 -2.610 1.00 13.11 N ANISOU 5581 N ASP B 289 1701 1525 1756 -34 39 -167 N ATOM 5582 CA ASP B 289 27.637 -3.601 -1.807 1.00 14.73 C ANISOU 5582 CA ASP B 289 1981 1664 1951 -202 -61 -69 C ATOM 5583 C ASP B 289 27.545 -4.988 -2.454 1.00 12.92 C ANISOU 5583 C ASP B 289 1622 1650 1636 59 31 -48 C ATOM 5584 O ASP B 289 27.843 -5.987 -1.776 1.00 12.35 O ANISOU 5584 O ASP B 289 1408 1572 1710 -121 -26 -26 O ATOM 5585 CB ASP B 289 26.241 -3.138 -1.382 1.00 18.94 C ANISOU 5585 CB ASP B 289 2210 2400 2587 80 59 44 C ATOM 5586 CG ASP B 289 26.271 -2.088 -0.293 1.00 24.25 C ANISOU 5586 CG ASP B 289 3245 3008 2962 -41 27 -182 C ATOM 5587 OD1 ASP B 289 27.269 -1.876 0.445 1.00 26.94 O ANISOU 5587 OD1 ASP B 289 3376 3525 3335 -41 -138 -218 O ATOM 5588 OD2 ASP B 289 25.236 -1.404 -0.156 1.00 27.66 O ANISOU 5588 OD2 ASP B 289 3413 3413 3682 92 57 -74 O ATOM 5589 N PRO B 290 27.145 -5.117 -3.698 1.00 11.37 N ANISOU 5589 N PRO B 290 1412 1304 1602 63 -141 -63 N ATOM 5590 CA PRO B 290 27.009 -6.440 -4.329 1.00 10.87 C ANISOU 5590 CA PRO B 290 1323 1325 1484 124 -108 -31 C ATOM 5591 C PRO B 290 28.409 -7.034 -4.502 1.00 10.49 C ANISOU 5591 C PRO B 290 1185 1372 1428 -9 -30 -12 C ATOM 5592 O PRO B 290 28.571 -8.235 -4.347 1.00 10.84 O ANISOU 5592 O PRO B 290 1214 1406 1500 -18 -64 -65 O ATOM 5593 CB PRO B 290 26.320 -6.207 -5.657 1.00 11.13 C ANISOU 5593 CB PRO B 290 1469 1357 1405 -26 -52 33 C ATOM 5594 CG PRO B 290 26.539 -4.745 -5.925 1.00 12.04 C ANISOU 5594 CG PRO B 290 1713 1352 1509 24 -68 68 C ATOM 5595 CD PRO B 290 26.541 -4.055 -4.564 1.00 11.83 C ANISOU 5595 CD PRO B 290 1650 1260 1584 74 -104 -45 C ATOM 5596 N SER B 291 29.442 -6.204 -4.748 1.00 10.00 N ANISOU 5596 N SER B 291 1241 1357 1199 -25 15 29 N ATOM 5597 CA SER B 291 30.784 -6.762 -4.774 1.00 10.46 C ANISOU 5597 CA SER B 291 1191 1447 1338 -53 -109 68 C ATOM 5598 C SER B 291 31.200 -7.320 -3.421 1.00 9.44 C ANISOU 5598 C SER B 291 1150 1245 1190 -99 80 79 C ATOM 5599 O SER B 291 31.936 -8.305 -3.382 1.00 10.89 O ANISOU 5599 O SER B 291 1334 1323 1482 -20 -32 -183 O ATOM 5600 CB SER B 291 31.782 -5.643 -5.213 1.00 12.77 C ANISOU 5600 CB SER B 291 1533 1620 1701 -22 337 333 C ATOM 5601 OG SER B 291 31.192 -5.192 -6.455 1.00 16.98 O ANISOU 5601 OG SER B 291 2256 2150 2044 8 -11 195 O ATOM 5602 N LEU B 292 30.853 -6.686 -2.311 1.00 8.15 N ANISOU 5602 N LEU B 292 734 1090 1274 -104 -30 -28 N ATOM 5603 CA LEU B 292 31.168 -7.216 -0.979 1.00 9.16 C ANISOU 5603 CA LEU B 292 1097 1117 1268 -100 44 33 C ATOM 5604 C LEU B 292 30.369 -8.488 -0.691 1.00 10.23 C ANISOU 5604 C LEU B 292 1198 1129 1558 -89 52 0 C ATOM 5605 O LEU B 292 30.885 -9.436 -0.103 1.00 10.36 O ANISOU 5605 O LEU B 292 1128 1411 1397 -112 -66 125 O ATOM 5606 CB LEU B 292 30.856 -6.198 0.125 1.00 9.70 C ANISOU 5606 CB LEU B 292 1124 1210 1354 -68 51 -34 C ATOM 5607 CG LEU B 292 31.820 -5.000 0.174 1.00 12.08 C ANISOU 5607 CG LEU B 292 1477 1281 1833 -107 -164 -183 C ATOM 5608 CD1 LEU B 292 31.203 -3.884 1.009 1.00 14.84 C ANISOU 5608 CD1 LEU B 292 1966 1671 2002 105 123 -174 C ATOM 5609 CD2 LEU B 292 33.146 -5.464 0.752 1.00 13.47 C ANISOU 5609 CD2 LEU B 292 1496 1676 1945 -17 -188 -109 C ATOM 5610 N GLU B 293 29.114 -8.525 -1.140 1.00 11.37 N ANISOU 5610 N GLU B 293 1295 1379 1646 -81 -64 -32 N ATOM 5611 CA GLU B 293 28.279 -9.731 -0.925 1.00 10.74 C ANISOU 5611 CA GLU B 293 1301 1236 1544 -10 110 -82 C ATOM 5612 C GLU B 293 28.812 -10.920 -1.727 1.00 11.01 C ANISOU 5612 C GLU B 293 1355 1247 1581 53 74 -24 C ATOM 5613 O GLU B 293 28.586 -12.081 -1.360 1.00 12.80 O ANISOU 5613 O GLU B 293 1615 1352 1897 -90 467 66 O ATOM 5614 CB GLU B 293 26.863 -9.471 -1.405 1.00 13.34 C ANISOU 5614 CB GLU B 293 1525 1803 1740 24 -50 -34 C ATOM 5615 CG GLU B 293 26.098 -8.480 -0.500 1.00 16.14 C ANISOU 5615 CG GLU B 293 1916 1974 2241 199 109 -145 C ATOM 5616 CD GLU B 293 24.614 -8.597 -0.883 1.00 20.15 C ANISOU 5616 CD GLU B 293 2193 2728 2734 90 -82 -37 C ATOM 5617 OE1 GLU B 293 24.040 -7.574 -1.261 1.00 21.87 O ANISOU 5617 OE1 GLU B 293 2385 2813 3114 215 -128 13 O ATOM 5618 OE2 GLU B 293 24.046 -9.698 -0.809 1.00 22.28 O ANISOU 5618 OE2 GLU B 293 2598 2900 2969 -65 -56 -115 O ATOM 5619 N ASN B 294 29.552 -10.697 -2.789 1.00 9.92 N ANISOU 5619 N ASN B 294 1140 1236 1392 70 3 -173 N ATOM 5620 CA ASN B 294 30.142 -11.789 -3.603 1.00 9.87 C ANISOU 5620 CA ASN B 294 1183 1170 1399 123 -74 -100 C ATOM 5621 C ASN B 294 31.295 -12.488 -2.894 1.00 10.64 C ANISOU 5621 C ASN B 294 1270 1347 1426 97 -118 -50 C ATOM 5622 O ASN B 294 31.730 -13.521 -3.422 1.00 11.85 O ANISOU 5622 O ASN B 294 1439 1206 1857 103 -241 10 O ATOM 5623 CB ASN B 294 30.653 -11.242 -4.926 1.00 9.99 C ANISOU 5623 CB ASN B 294 1234 1231 1330 160 -64 -96 C ATOM 5624 CG ASN B 294 29.625 -10.901 -5.995 1.00 10.66 C ANISOU 5624 CG ASN B 294 1248 1366 1437 47 -58 -53 C ATOM 5625 OD1 ASN B 294 28.465 -11.292 -5.941 1.00 11.75 O ANISOU 5625 OD1 ASN B 294 1363 1376 1725 -154 -202 -132 O ATOM 5626 ND2 ASN B 294 30.049 -10.154 -7.010 1.00 11.05 N ANISOU 5626 ND2 ASN B 294 1399 1227 1571 -30 -122 57 N ATOM 5627 N ILE B 295 31.823 -11.929 -1.784 1.00 9.63 N ANISOU 5627 N ILE B 295 1104 1166 1388 94 -121 18 N ATOM 5628 CA ILE B 295 32.998 -12.576 -1.160 1.00 9.01 C ANISOU 5628 CA ILE B 295 1099 1151 1171 -31 -74 82 C ATOM 5629 C ILE B 295 32.647 -13.928 -0.558 1.00 9.84 C ANISOU 5629 C ILE B 295 1185 1105 1450 51 50 53 C ATOM 5630 O ILE B 295 33.390 -14.920 -0.701 1.00 10.23 O ANISOU 5630 O ILE B 295 1409 939 1541 66 -155 17 O ATOM 5631 CB ILE B 295 33.604 -11.624 -0.113 1.00 8.29 C ANISOU 5631 CB ILE B 295 1047 992 1113 -35 -84 145 C ATOM 5632 CG1 ILE B 295 34.202 -10.418 -0.872 1.00 7.61 C ANISOU 5632 CG1 ILE B 295 999 978 915 -113 136 -8 C ATOM 5633 CG2 ILE B 295 34.677 -12.340 0.740 1.00 8.44 C ANISOU 5633 CG2 ILE B 295 1065 1130 1013 34 -98 187 C ATOM 5634 CD1 ILE B 295 34.540 -9.225 0.046 1.00 8.86 C ANISOU 5634 CD1 ILE B 295 1123 1157 1086 -216 24 -65 C ATOM 5635 N ALA B 296 31.489 -13.993 0.114 1.00 9.86 N ANISOU 5635 N ALA B 296 1143 1318 1284 78 52 66 N ATOM 5636 CA ALA B 296 31.123 -15.240 0.805 1.00 11.29 C ANISOU 5636 CA ALA B 296 1462 1297 1531 22 170 6 C ATOM 5637 C ALA B 296 30.511 -16.288 -0.121 1.00 12.54 C ANISOU 5637 C ALA B 296 1538 1615 1612 -8 94 -117 C ATOM 5638 O ALA B 296 29.367 -16.741 0.004 1.00 13.39 O ANISOU 5638 O ALA B 296 1533 1607 1948 -24 242 -99 O ATOM 5639 CB ALA B 296 30.244 -14.863 2.008 1.00 11.33 C ANISOU 5639 CB ALA B 296 1494 1298 1512 47 247 118 C ATOM 5640 N LEU B 297 31.306 -16.800 -1.072 1.00 12.00 N ANISOU 5640 N LEU B 297 1644 1435 1481 49 84 -4 N ATOM 5641 CA LEU B 297 30.901 -17.899 -1.938 1.00 11.62 C ANISOU 5641 CA LEU B 297 1577 1350 1489 -51 39 66 C ATOM 5642 C LEU B 297 30.894 -19.221 -1.144 1.00 11.34 C ANISOU 5642 C LEU B 297 1491 1342 1476 -20 -49 39 C ATOM 5643 O LEU B 297 31.690 -19.391 -0.201 1.00 11.85 O ANISOU 5643 O LEU B 297 1623 1454 1425 63 -116 7 O ATOM 5644 CB LEU B 297 31.917 -18.007 -3.100 1.00 13.11 C ANISOU 5644 CB LEU B 297 1733 1620 1627 46 71 31 C ATOM 5645 CG LEU B 297 32.016 -16.734 -3.953 1.00 13.84 C ANISOU 5645 CG LEU B 297 1754 1790 1713 -63 57 111 C ATOM 5646 CD1 LEU B 297 33.047 -16.978 -5.027 1.00 16.28 C ANISOU 5646 CD1 LEU B 297 1848 2284 2054 131 183 91 C ATOM 5647 CD2 LEU B 297 30.646 -16.449 -4.625 1.00 14.51 C ANISOU 5647 CD2 LEU B 297 1837 1754 1921 -21 1 217 C ATOM 5648 N TRP B 298 30.043 -20.162 -1.549 1.00 10.51 N ANISOU 5648 N TRP B 298 1262 1275 1459 -12 38 121 N ATOM 5649 CA TRP B 298 29.943 -21.444 -0.835 1.00 10.34 C ANISOU 5649 CA TRP B 298 1208 1215 1506 15 -35 129 C ATOM 5650 C TRP B 298 31.096 -22.355 -1.190 1.00 10.22 C ANISOU 5650 C TRP B 298 1216 1265 1402 -75 -15 55 C ATOM 5651 O TRP B 298 31.311 -22.634 -2.370 1.00 11.21 O ANISOU 5651 O TRP B 298 1306 1512 1440 8 -42 100 O ATOM 5652 CB TRP B 298 28.602 -22.123 -1.194 1.00 10.93 C ANISOU 5652 CB TRP B 298 1207 1411 1535 0 34 81 C ATOM 5653 CG TRP B 298 27.388 -21.425 -0.627 1.00 11.74 C ANISOU 5653 CG TRP B 298 1364 1581 1516 97 82 74 C ATOM 5654 CD1 TRP B 298 27.303 -20.206 -0.045 1.00 12.15 C ANISOU 5654 CD1 TRP B 298 1493 1588 1535 -19 48 75 C ATOM 5655 CD2 TRP B 298 26.038 -21.961 -0.639 1.00 12.00 C ANISOU 5655 CD2 TRP B 298 1446 1629 1485 -4 34 138 C ATOM 5656 NE1 TRP B 298 26.009 -19.937 0.363 1.00 12.03 N ANISOU 5656 NE1 TRP B 298 1444 1622 1504 65 -77 3 N ATOM 5657 CE2 TRP B 298 25.227 -21.002 0.004 1.00 12.43 C ANISOU 5657 CE2 TRP B 298 1474 1580 1667 -11 36 160 C ATOM 5658 CE3 TRP B 298 25.473 -23.150 -1.079 1.00 12.31 C ANISOU 5658 CE3 TRP B 298 1515 1691 1473 10 -20 108 C ATOM 5659 CZ2 TRP B 298 23.841 -21.163 0.192 1.00 13.34 C ANISOU 5659 CZ2 TRP B 298 1465 1738 1864 3 -104 117 C ATOM 5660 CZ3 TRP B 298 24.104 -23.355 -0.894 1.00 12.58 C ANISOU 5660 CZ3 TRP B 298 1504 1695 1583 135 -88 91 C ATOM 5661 CH2 TRP B 298 23.309 -22.359 -0.262 1.00 13.17 C ANISOU 5661 CH2 TRP B 298 1564 1749 1690 71 -72 -49 C ATOM 5662 N HIS B 299 31.758 -22.892 -0.160 1.00 9.46 N ANISOU 5662 N HIS B 299 1083 1085 1428 17 -59 57 N ATOM 5663 CA HIS B 299 32.835 -23.855 -0.317 1.00 10.42 C ANISOU 5663 CA HIS B 299 1312 1179 1467 83 158 -123 C ATOM 5664 C HIS B 299 33.806 -23.482 -1.414 1.00 10.96 C ANISOU 5664 C HIS B 299 1391 1313 1462 40 72 23 C ATOM 5665 O HIS B 299 34.342 -22.367 -1.387 1.00 12.15 O ANISOU 5665 O HIS B 299 1529 1440 1647 -15 108 -81 O ATOM 5666 CB HIS B 299 32.217 -25.228 -0.627 1.00 10.96 C ANISOU 5666 CB HIS B 299 1332 1278 1552 -54 77 34 C ATOM 5667 CG HIS B 299 31.236 -25.730 0.394 1.00 11.67 C ANISOU 5667 CG HIS B 299 1464 1416 1555 -23 136 37 C ATOM 5668 ND1 HIS B 299 31.590 -26.036 1.706 1.00 12.24 N ANISOU 5668 ND1 HIS B 299 1472 1610 1569 39 118 35 N ATOM 5669 CD2 HIS B 299 29.930 -26.036 0.238 1.00 10.92 C ANISOU 5669 CD2 HIS B 299 1443 1175 1529 -15 137 -60 C ATOM 5670 CE1 HIS B 299 30.509 -26.520 2.323 1.00 12.41 C ANISOU 5670 CE1 HIS B 299 1530 1485 1702 33 105 61 C ATOM 5671 NE2 HIS B 299 29.508 -26.523 1.461 1.00 11.81 N ANISOU 5671 NE2 HIS B 299 1594 1392 1503 -99 146 -79 N ATOM 5672 N GLU B 300 34.131 -24.371 -2.377 1.00 11.03 N ANISOU 5672 N GLU B 300 1350 1401 1441 144 85 -14 N ATOM 5673 CA GLU B 300 35.141 -24.051 -3.389 1.00 10.87 C ANISOU 5673 CA GLU B 300 1359 1286 1485 131 45 87 C ATOM 5674 C GLU B 300 34.592 -23.262 -4.564 1.00 11.48 C ANISOU 5674 C GLU B 300 1446 1450 1464 71 18 59 C ATOM 5675 O GLU B 300 35.372 -22.929 -5.515 1.00 11.96 O ANISOU 5675 O GLU B 300 1533 1542 1470 194 63 114 O ATOM 5676 CB GLU B 300 35.879 -25.339 -3.869 1.00 12.24 C ANISOU 5676 CB GLU B 300 1603 1409 1639 90 101 -112 C ATOM 5677 CG GLU B 300 36.777 -25.876 -2.735 1.00 13.69 C ANISOU 5677 CG GLU B 300 1647 1578 1978 112 -71 -6 C ATOM 5678 CD GLU B 300 36.161 -26.243 -1.414 1.00 17.16 C ANISOU 5678 CD GLU B 300 2157 2123 2239 -169 69 42 C ATOM 5679 OE1 GLU B 300 35.197 -27.076 -1.311 1.00 16.00 O ANISOU 5679 OE1 GLU B 300 1857 1885 2335 -6 -15 53 O ATOM 5680 OE2 GLU B 300 36.591 -25.684 -0.340 1.00 20.36 O ANISOU 5680 OE2 GLU B 300 2701 2511 2524 -259 -148 -30 O ATOM 5681 N ARG B 301 33.334 -22.867 -4.518 1.00 10.27 N ANISOU 5681 N ARG B 301 1315 1279 1310 28 20 -43 N ATOM 5682 CA ARG B 301 32.743 -21.732 -5.208 1.00 10.75 C ANISOU 5682 CA ARG B 301 1336 1432 1316 3 10 42 C ATOM 5683 C ARG B 301 31.247 -21.981 -5.451 1.00 11.15 C ANISOU 5683 C ARG B 301 1366 1397 1474 62 -19 17 C ATOM 5684 O ARG B 301 30.822 -23.156 -5.558 1.00 11.58 O ANISOU 5684 O ARG B 301 1412 1312 1674 152 -68 174 O ATOM 5685 CB ARG B 301 33.315 -21.300 -6.580 1.00 10.18 C ANISOU 5685 CB ARG B 301 1156 1433 1280 -1 19 -39 C ATOM 5686 CG ARG B 301 33.114 -22.337 -7.678 1.00 11.43 C ANISOU 5686 CG ARG B 301 1303 1615 1427 -67 -73 -137 C ATOM 5687 CD ARG B 301 31.941 -22.050 -8.625 1.00 12.14 C ANISOU 5687 CD ARG B 301 1488 1546 1578 105 -117 41 C ATOM 5688 NE ARG B 301 32.016 -20.720 -9.240 1.00 12.55 N ANISOU 5688 NE ARG B 301 1602 1488 1680 24 31 -36 N ATOM 5689 CZ ARG B 301 32.740 -20.477 -10.330 1.00 13.50 C ANISOU 5689 CZ ARG B 301 1771 1574 1786 138 132 17 C ATOM 5690 NH1 ARG B 301 33.423 -21.443 -10.990 1.00 12.62 N ANISOU 5690 NH1 ARG B 301 1624 1546 1623 106 68 -89 N ATOM 5691 NH2 ARG B 301 32.818 -19.250 -10.816 1.00 13.71 N ANISOU 5691 NH2 ARG B 301 1692 1516 2000 182 42 -44 N ATOM 5692 N ASP B 302 30.467 -20.900 -5.566 1.00 11.00 N ANISOU 5692 N ASP B 302 1409 1294 1475 94 -34 -7 N ATOM 5693 CA ASP B 302 29.207 -20.999 -6.311 1.00 11.22 C ANISOU 5693 CA ASP B 302 1338 1367 1557 42 25 29 C ATOM 5694 C ASP B 302 29.272 -19.943 -7.396 1.00 11.51 C ANISOU 5694 C ASP B 302 1430 1380 1562 27 49 -25 C ATOM 5695 O ASP B 302 30.249 -19.171 -7.365 1.00 13.05 O ANISOU 5695 O ASP B 302 1583 1414 1961 -40 41 -122 O ATOM 5696 CB ASP B 302 28.006 -20.826 -5.355 1.00 11.21 C ANISOU 5696 CB ASP B 302 1344 1371 1544 83 31 53 C ATOM 5697 CG ASP B 302 27.945 -19.445 -4.732 1.00 12.95 C ANISOU 5697 CG ASP B 302 1650 1558 1713 77 -22 -45 C ATOM 5698 OD1 ASP B 302 27.659 -18.482 -5.493 1.00 13.74 O ANISOU 5698 OD1 ASP B 302 1885 1410 1924 43 30 17 O ATOM 5699 OD2 ASP B 302 28.164 -19.251 -3.525 1.00 13.24 O ANISOU 5699 OD2 ASP B 302 1637 1684 1708 41 -6 63 O ATOM 5700 N ILE B 303 28.378 -19.871 -8.371 1.00 11.45 N ANISOU 5700 N ILE B 303 1470 1386 1495 119 23 -119 N ATOM 5701 CA ILE B 303 28.552 -18.903 -9.457 1.00 13.51 C ANISOU 5701 CA ILE B 303 1765 1568 1798 16 81 32 C ATOM 5702 C ILE B 303 27.676 -17.701 -9.322 1.00 11.72 C ANISOU 5702 C ILE B 303 1452 1533 1468 -79 -49 -11 C ATOM 5703 O ILE B 303 27.511 -16.902 -10.287 1.00 11.78 O ANISOU 5703 O ILE B 303 1522 1304 1651 -61 39 -27 O ATOM 5704 CB ILE B 303 28.370 -19.664 -10.808 1.00 17.72 C ANISOU 5704 CB ILE B 303 2370 2342 2023 -68 -123 -145 C ATOM 5705 CG1 ILE B 303 29.058 -18.846 -11.890 1.00 22.15 C ANISOU 5705 CG1 ILE B 303 2957 2821 2639 -142 155 37 C ATOM 5706 CG2 ILE B 303 26.903 -19.915 -11.139 1.00 17.59 C ANISOU 5706 CG2 ILE B 303 2321 2124 2239 -106 40 -31 C ATOM 5707 CD1 ILE B 303 29.883 -19.669 -12.873 1.00 25.47 C ANISOU 5707 CD1 ILE B 303 3234 3300 3144 131 198 -206 C ATOM 5708 N SER B 304 27.121 -17.444 -8.138 1.00 10.07 N ANISOU 5708 N SER B 304 1226 1159 1440 -6 -66 -10 N ATOM 5709 CA SER B 304 26.296 -16.232 -7.934 1.00 10.19 C ANISOU 5709 CA SER B 304 1231 1233 1408 -21 -33 -24 C ATOM 5710 C SER B 304 27.044 -14.960 -8.337 1.00 10.47 C ANISOU 5710 C SER B 304 1256 1311 1409 -51 12 29 C ATOM 5711 O SER B 304 26.420 -13.995 -8.812 1.00 11.07 O ANISOU 5711 O SER B 304 1258 1484 1465 43 -7 49 O ATOM 5712 CB SER B 304 25.838 -16.119 -6.471 1.00 11.02 C ANISOU 5712 CB SER B 304 1354 1391 1441 80 54 -18 C ATOM 5713 OG SER B 304 27.003 -16.027 -5.611 1.00 11.56 O ANISOU 5713 OG SER B 304 1516 1470 1405 172 76 -134 O ATOM 5714 N HIS B 305 28.360 -14.878 -8.104 1.00 10.18 N ANISOU 5714 N HIS B 305 1193 1292 1383 -81 16 -23 N ATOM 5715 CA HIS B 305 29.131 -13.660 -8.437 1.00 9.68 C ANISOU 5715 CA HIS B 305 1123 1241 1313 -35 -29 -59 C ATOM 5716 C HIS B 305 29.185 -13.366 -9.926 1.00 9.98 C ANISOU 5716 C HIS B 305 1101 1310 1382 47 -55 0 C ATOM 5717 O HIS B 305 29.355 -12.212 -10.355 1.00 10.60 O ANISOU 5717 O HIS B 305 1065 1399 1562 -112 -140 -5 O ATOM 5718 CB HIS B 305 30.579 -13.825 -7.890 1.00 9.45 C ANISOU 5718 CB HIS B 305 1047 1266 1278 25 91 -96 C ATOM 5719 CG HIS B 305 31.290 -14.925 -8.649 1.00 10.56 C ANISOU 5719 CG HIS B 305 1437 1024 1552 68 16 -100 C ATOM 5720 ND1 HIS B 305 31.261 -16.273 -8.348 1.00 12.25 N ANISOU 5720 ND1 HIS B 305 1693 1153 1808 140 68 -54 N ATOM 5721 CD2 HIS B 305 32.066 -14.766 -9.760 1.00 9.17 C ANISOU 5721 CD2 HIS B 305 1383 581 1521 107 -27 66 C ATOM 5722 CE1 HIS B 305 31.967 -16.940 -9.264 1.00 10.07 C ANISOU 5722 CE1 HIS B 305 1313 668 1844 87 84 -31 C ATOM 5723 NE2 HIS B 305 32.451 -16.029 -10.133 1.00 11.95 N ANISOU 5723 NE2 HIS B 305 1721 927 1891 276 136 -46 N ATOM 5724 N SER B 306 29.001 -14.392 -10.771 1.00 10.01 N ANISOU 5724 N SER B 306 1159 1321 1323 42 -66 -58 N ATOM 5725 CA SER B 306 29.251 -14.205 -12.221 1.00 12.25 C ANISOU 5725 CA SER B 306 1564 1627 1463 -37 -59 31 C ATOM 5726 C SER B 306 28.218 -13.258 -12.798 1.00 12.54 C ANISOU 5726 C SER B 306 1628 1516 1621 -32 -68 -32 C ATOM 5727 O SER B 306 28.554 -12.380 -13.598 1.00 12.98 O ANISOU 5727 O SER B 306 1638 1724 1568 -64 -192 -12 O ATOM 5728 CB SER B 306 29.228 -15.579 -12.904 1.00 15.71 C ANISOU 5728 CB SER B 306 2243 1914 1811 -138 34 -219 C ATOM 5729 OG SER B 306 29.170 -15.347 -14.309 1.00 19.92 O ANISOU 5729 OG SER B 306 2750 2656 2162 49 -81 89 O ATOM 5730 N SER B 307 26.940 -13.418 -12.421 1.00 12.51 N ANISOU 5730 N SER B 307 1522 1414 1818 -31 -116 -67 N ATOM 5731 CA SER B 307 25.945 -12.477 -12.969 1.00 14.60 C ANISOU 5731 CA SER B 307 1745 1658 2145 55 -160 28 C ATOM 5732 C SER B 307 26.151 -11.067 -12.438 1.00 14.87 C ANISOU 5732 C SER B 307 1880 1841 1927 -95 -146 -102 C ATOM 5733 O SER B 307 26.046 -10.135 -13.256 1.00 16.82 O ANISOU 5733 O SER B 307 2325 1863 2203 -83 -361 -96 O ATOM 5734 CB SER B 307 24.514 -12.961 -12.658 1.00 15.23 C ANISOU 5734 CB SER B 307 1775 2010 2001 112 1 -55 C ATOM 5735 OG SER B 307 24.366 -13.056 -11.250 1.00 15.88 O ANISOU 5735 OG SER B 307 1809 2308 1919 180 -203 27 O ATOM 5736 N VAL B 308 26.537 -10.826 -11.202 1.00 12.59 N ANISOU 5736 N VAL B 308 1495 1591 1697 -74 100 12 N ATOM 5737 CA VAL B 308 26.832 -9.499 -10.697 1.00 11.16 C ANISOU 5737 CA VAL B 308 1223 1619 1397 -174 59 -15 C ATOM 5738 C VAL B 308 27.980 -8.895 -11.515 1.00 10.12 C ANISOU 5738 C VAL B 308 1197 1383 1266 -10 53 -13 C ATOM 5739 O VAL B 308 27.994 -7.745 -11.944 1.00 10.13 O ANISOU 5739 O VAL B 308 1210 1447 1190 204 -74 1 O ATOM 5740 CB VAL B 308 27.265 -9.569 -9.213 1.00 11.23 C ANISOU 5740 CB VAL B 308 1399 1440 1430 -214 65 66 C ATOM 5741 CG1 VAL B 308 27.764 -8.200 -8.707 1.00 11.21 C ANISOU 5741 CG1 VAL B 308 1381 1423 1456 -22 -4 -81 C ATOM 5742 CG2 VAL B 308 26.056 -10.072 -8.384 1.00 12.28 C ANISOU 5742 CG2 VAL B 308 1245 1906 1513 -63 103 63 C ATOM 5743 N GLU B 309 29.073 -9.676 -11.664 1.00 9.56 N ANISOU 5743 N GLU B 309 1124 1327 1181 -38 69 -53 N ATOM 5744 CA GLU B 309 30.262 -9.162 -12.328 1.00 9.32 C ANISOU 5744 CA GLU B 309 1068 1250 1224 33 7 85 C ATOM 5745 C GLU B 309 30.047 -8.843 -13.786 1.00 9.41 C ANISOU 5745 C GLU B 309 1206 1140 1231 -44 -41 41 C ATOM 5746 O GLU B 309 30.766 -8.011 -14.371 1.00 9.10 O ANISOU 5746 O GLU B 309 1300 948 1209 78 -4 29 O ATOM 5747 CB GLU B 309 31.400 -10.227 -12.146 1.00 9.20 C ANISOU 5747 CB GLU B 309 1076 1197 1224 57 83 66 C ATOM 5748 CG GLU B 309 31.820 -10.230 -10.670 1.00 9.96 C ANISOU 5748 CG GLU B 309 1237 1276 1272 145 -81 -57 C ATOM 5749 CD GLU B 309 32.722 -11.354 -10.248 1.00 11.56 C ANISOU 5749 CD GLU B 309 1489 1421 1480 157 -48 37 C ATOM 5750 OE1 GLU B 309 32.928 -12.292 -11.059 1.00 12.01 O ANISOU 5750 OE1 GLU B 309 1667 1508 1389 94 23 9 O ATOM 5751 OE2 GLU B 309 33.267 -11.331 -9.112 1.00 12.56 O ANISOU 5751 OE2 GLU B 309 1474 1737 1562 164 -148 154 O ATOM 5752 N ARG B 310 29.090 -9.452 -14.477 1.00 10.77 N ANISOU 5752 N ARG B 310 1261 1273 1558 -101 -72 -53 N ATOM 5753 CA ARG B 310 28.736 -9.080 -15.828 1.00 12.28 C ANISOU 5753 CA ARG B 310 1561 1608 1498 -104 -65 -20 C ATOM 5754 C ARG B 310 28.203 -7.663 -15.872 1.00 12.15 C ANISOU 5754 C ARG B 310 1514 1625 1477 -124 -61 16 C ATOM 5755 O ARG B 310 28.417 -7.030 -16.929 1.00 13.70 O ANISOU 5755 O ARG B 310 1898 2038 1269 -244 -124 -28 O ATOM 5756 CB ARG B 310 27.635 -9.982 -16.455 1.00 15.50 C ANISOU 5756 CB ARG B 310 1864 1968 2059 -308 -85 -196 C ATOM 5757 CG ARG B 310 28.143 -11.391 -16.712 1.00 20.20 C ANISOU 5757 CG ARG B 310 2507 2310 2858 45 -1 -34 C ATOM 5758 CD ARG B 310 26.993 -12.155 -17.463 1.00 25.29 C ANISOU 5758 CD ARG B 310 3027 3387 3196 -277 -223 -216 C ATOM 5759 NE ARG B 310 27.447 -13.480 -17.659 1.00 29.43 N ANISOU 5759 NE ARG B 310 3580 3673 3930 -77 -151 -195 N ATOM 5760 CZ ARG B 310 27.581 -14.669 -17.157 1.00 33.37 C ANISOU 5760 CZ ARG B 310 4270 4058 4352 -20 -116 53 C ATOM 5761 NH1 ARG B 310 27.133 -15.098 -15.966 1.00 34.30 N ANISOU 5761 NH1 ARG B 310 4273 4519 4239 -79 -68 -118 N ATOM 5762 NH2 ARG B 310 28.235 -15.528 -17.974 1.00 36.02 N ANISOU 5762 NH2 ARG B 310 4521 4593 4572 68 33 -179 N ATOM 5763 N TYR B 311 27.528 -7.170 -14.850 1.00 12.55 N ANISOU 5763 N TYR B 311 1672 1671 1424 -32 -32 0 N ATOM 5764 CA TYR B 311 27.183 -5.750 -14.774 1.00 13.86 C ANISOU 5764 CA TYR B 311 1848 1677 1740 -19 -89 95 C ATOM 5765 C TYR B 311 28.376 -4.906 -14.321 1.00 13.26 C ANISOU 5765 C TYR B 311 1847 1619 1571 -2 -16 52 C ATOM 5766 O TYR B 311 28.838 -3.956 -14.973 1.00 15.34 O ANISOU 5766 O TYR B 311 2190 1791 1847 -94 -22 222 O ATOM 5767 CB TYR B 311 26.070 -5.551 -13.717 1.00 16.73 C ANISOU 5767 CB TYR B 311 2099 2121 2135 160 59 -11 C ATOM 5768 CG TYR B 311 24.740 -6.108 -14.187 1.00 20.53 C ANISOU 5768 CG TYR B 311 2389 2649 2761 -8 -72 -101 C ATOM 5769 CD1 TYR B 311 24.439 -7.437 -13.994 1.00 21.58 C ANISOU 5769 CD1 TYR B 311 2611 2724 2865 22 90 71 C ATOM 5770 CD2 TYR B 311 23.808 -5.297 -14.834 1.00 23.38 C ANISOU 5770 CD2 TYR B 311 2844 2882 3156 159 -151 8 C ATOM 5771 CE1 TYR B 311 23.254 -7.991 -14.436 1.00 24.01 C ANISOU 5771 CE1 TYR B 311 2897 3097 3127 -88 -59 -24 C ATOM 5772 CE2 TYR B 311 22.596 -5.831 -15.252 1.00 25.27 C ANISOU 5772 CE2 TYR B 311 2971 3110 3519 65 -145 -107 C ATOM 5773 CZ TYR B 311 22.332 -7.173 -15.047 1.00 25.98 C ANISOU 5773 CZ TYR B 311 3115 3203 3552 50 -47 39 C ATOM 5774 OH TYR B 311 21.115 -7.709 -15.457 1.00 28.80 O ANISOU 5774 OH TYR B 311 3261 3557 4124 41 -139 -279 O ATOM 5775 N VAL B 312 28.972 -5.295 -13.205 1.00 10.92 N ANISOU 5775 N VAL B 312 1327 1367 1454 63 54 -91 N ATOM 5776 CA VAL B 312 29.831 -4.401 -12.432 1.00 11.38 C ANISOU 5776 CA VAL B 312 1325 1486 1514 19 31 -40 C ATOM 5777 C VAL B 312 31.192 -4.204 -13.085 1.00 11.61 C ANISOU 5777 C VAL B 312 1421 1453 1537 42 102 -41 C ATOM 5778 O VAL B 312 31.647 -3.047 -13.077 1.00 12.12 O ANISOU 5778 O VAL B 312 1442 1516 1648 -28 104 5 O ATOM 5779 CB VAL B 312 29.939 -4.934 -10.985 1.00 12.49 C ANISOU 5779 CB VAL B 312 1436 1843 1467 -33 130 -83 C ATOM 5780 CG1 VAL B 312 30.942 -4.102 -10.193 1.00 13.38 C ANISOU 5780 CG1 VAL B 312 1703 1752 1630 -71 30 -59 C ATOM 5781 CG2 VAL B 312 28.564 -4.912 -10.279 1.00 12.23 C ANISOU 5781 CG2 VAL B 312 1383 1774 1490 14 108 -51 C ATOM 5782 N PHE B 313 31.839 -5.266 -13.601 1.00 11.31 N ANISOU 5782 N PHE B 313 1351 1423 1523 102 124 -40 N ATOM 5783 CA PHE B 313 33.199 -5.063 -14.125 1.00 11.32 C ANISOU 5783 CA PHE B 313 1392 1337 1570 29 107 92 C ATOM 5784 C PHE B 313 33.229 -4.076 -15.288 1.00 11.24 C ANISOU 5784 C PHE B 313 1450 1322 1501 13 32 -15 C ATOM 5785 O PHE B 313 33.936 -3.050 -15.242 1.00 11.43 O ANISOU 5785 O PHE B 313 1532 1299 1510 -79 -107 19 O ATOM 5786 CB PHE B 313 33.870 -6.415 -14.477 1.00 10.80 C ANISOU 5786 CB PHE B 313 1316 1412 1376 58 119 10 C ATOM 5787 CG PHE B 313 34.248 -7.321 -13.324 1.00 11.55 C ANISOU 5787 CG PHE B 313 1347 1498 1543 -35 17 78 C ATOM 5788 CD1 PHE B 313 34.774 -8.583 -13.595 1.00 11.65 C ANISOU 5788 CD1 PHE B 313 1329 1513 1585 -41 23 58 C ATOM 5789 CD2 PHE B 313 34.138 -6.901 -12.005 1.00 11.90 C ANISOU 5789 CD2 PHE B 313 1428 1588 1507 -28 12 84 C ATOM 5790 CE1 PHE B 313 35.139 -9.432 -12.534 1.00 12.05 C ANISOU 5790 CE1 PHE B 313 1322 1652 1606 -3 -41 39 C ATOM 5791 CE2 PHE B 313 34.505 -7.739 -10.948 1.00 12.18 C ANISOU 5791 CE2 PHE B 313 1416 1584 1628 -15 -33 85 C ATOM 5792 CZ PHE B 313 35.016 -9.016 -11.220 1.00 11.21 C ANISOU 5792 CZ PHE B 313 1196 1508 1555 -75 -1 87 C ATOM 5793 N PRO B 314 32.424 -4.258 -16.334 1.00 11.14 N ANISOU 5793 N PRO B 314 1498 1286 1448 157 -5 55 N ATOM 5794 CA PRO B 314 32.448 -3.320 -17.437 1.00 11.65 C ANISOU 5794 CA PRO B 314 1614 1351 1462 101 -1 53 C ATOM 5795 C PRO B 314 31.817 -1.979 -17.036 1.00 11.57 C ANISOU 5795 C PRO B 314 1538 1327 1531 90 -31 50 C ATOM 5796 O PRO B 314 32.301 -0.940 -17.502 1.00 12.07 O ANISOU 5796 O PRO B 314 1538 1470 1579 52 60 122 O ATOM 5797 CB PRO B 314 31.646 -3.990 -18.545 1.00 12.44 C ANISOU 5797 CB PRO B 314 1721 1423 1583 11 -95 -8 C ATOM 5798 CG PRO B 314 31.087 -5.263 -18.001 1.00 14.06 C ANISOU 5798 CG PRO B 314 1931 1791 1618 -126 -94 192 C ATOM 5799 CD PRO B 314 31.663 -5.495 -16.624 1.00 12.11 C ANISOU 5799 CD PRO B 314 1617 1441 1543 32 -99 61 C ATOM 5800 N ASP B 315 30.773 -1.986 -16.217 1.00 11.71 N ANISOU 5800 N ASP B 315 1522 1477 1449 116 -51 80 N ATOM 5801 CA ASP B 315 30.067 -0.713 -15.931 1.00 12.17 C ANISOU 5801 CA ASP B 315 1628 1452 1545 47 -74 -152 C ATOM 5802 C ASP B 315 30.868 0.146 -14.961 1.00 11.42 C ANISOU 5802 C ASP B 315 1392 1522 1424 44 -52 -16 C ATOM 5803 O ASP B 315 31.016 1.358 -15.205 1.00 12.78 O ANISOU 5803 O ASP B 315 1597 1597 1662 -92 -192 -111 O ATOM 5804 CB ASP B 315 28.650 -0.960 -15.396 1.00 14.69 C ANISOU 5804 CB ASP B 315 1740 1849 1992 35 36 -5 C ATOM 5805 CG ASP B 315 27.732 -1.523 -16.458 1.00 19.34 C ANISOU 5805 CG ASP B 315 2271 2610 2469 -81 -162 -158 C ATOM 5806 OD1 ASP B 315 28.125 -1.709 -17.630 1.00 23.14 O ANISOU 5806 OD1 ASP B 315 2894 3380 2519 -147 -162 -227 O ATOM 5807 OD2 ASP B 315 26.554 -1.857 -16.208 1.00 22.68 O ANISOU 5807 OD2 ASP B 315 2344 3125 3148 -162 -183 -146 O ATOM 5808 N ALA B 316 31.494 -0.386 -13.934 1.00 10.36 N ANISOU 5808 N ALA B 316 1278 1305 1354 202 55 -64 N ATOM 5809 CA ALA B 316 32.233 0.434 -12.972 1.00 10.64 C ANISOU 5809 CA ALA B 316 1321 1368 1353 -38 -28 143 C ATOM 5810 C ALA B 316 33.452 1.050 -13.676 1.00 10.52 C ANISOU 5810 C ALA B 316 1446 1164 1389 -18 66 50 C ATOM 5811 O ALA B 316 33.754 2.242 -13.476 1.00 9.10 O ANISOU 5811 O ALA B 316 1304 848 1305 254 261 -68 O ATOM 5812 CB ALA B 316 32.690 -0.400 -11.766 1.00 8.76 C ANISOU 5812 CB ALA B 316 1159 971 1197 216 88 -57 C ATOM 5813 N THR B 317 34.144 0.250 -14.471 1.00 10.21 N ANISOU 5813 N THR B 317 1369 1254 1256 52 5 42 N ATOM 5814 CA THR B 317 35.383 0.756 -15.098 1.00 10.57 C ANISOU 5814 CA THR B 317 1306 1330 1381 83 -33 63 C ATOM 5815 C THR B 317 35.049 1.777 -16.174 1.00 10.84 C ANISOU 5815 C THR B 317 1423 1256 1440 34 -52 44 C ATOM 5816 O THR B 317 35.732 2.822 -16.252 1.00 10.67 O ANISOU 5816 O THR B 317 1221 1342 1491 43 -132 -12 O ATOM 5817 CB THR B 317 36.242 -0.365 -15.685 1.00 11.33 C ANISOU 5817 CB THR B 317 1409 1423 1472 127 -97 -45 C ATOM 5818 OG1 THR B 317 35.530 -1.179 -16.587 1.00 11.28 O ANISOU 5818 OG1 THR B 317 1423 1280 1583 161 -77 -102 O ATOM 5819 CG2 THR B 317 36.786 -1.267 -14.550 1.00 11.23 C ANISOU 5819 CG2 THR B 317 1288 1408 1570 182 -7 63 C ATOM 5820 N GLN B 318 34.022 1.537 -16.987 1.00 10.48 N ANISOU 5820 N GLN B 318 1444 1213 1324 101 -81 25 N ATOM 5821 CA GLN B 318 33.686 2.514 -18.049 1.00 10.39 C ANISOU 5821 CA GLN B 318 1475 1111 1361 109 -65 -19 C ATOM 5822 C GLN B 318 33.098 3.785 -17.451 1.00 9.94 C ANISOU 5822 C GLN B 318 1278 1178 1321 69 16 -27 C ATOM 5823 O GLN B 318 33.427 4.888 -17.936 1.00 9.85 O ANISOU 5823 O GLN B 318 1416 1121 1207 78 -139 -47 O ATOM 5824 CB GLN B 318 32.708 1.893 -19.052 1.00 12.04 C ANISOU 5824 CB GLN B 318 1610 1535 1431 -5 -138 13 C ATOM 5825 CG GLN B 318 33.345 0.797 -19.881 1.00 14.54 C ANISOU 5825 CG GLN B 318 1981 1669 1874 52 23 -45 C ATOM 5826 CD GLN B 318 32.356 0.203 -20.860 1.00 17.55 C ANISOU 5826 CD GLN B 318 2290 2221 2158 -18 -128 -94 C ATOM 5827 OE1 GLN B 318 32.158 0.747 -21.935 1.00 20.96 O ANISOU 5827 OE1 GLN B 318 2916 2788 2260 -53 -106 30 O ATOM 5828 NE2 GLN B 318 31.714 -0.897 -20.543 1.00 18.74 N ANISOU 5828 NE2 GLN B 318 2369 2430 2322 -204 -118 -137 N ATOM 5829 N THR B 319 32.277 3.660 -16.422 1.00 9.32 N ANISOU 5829 N THR B 319 1322 1094 1127 20 -54 -126 N ATOM 5830 CA THR B 319 31.687 4.864 -15.797 1.00 9.66 C ANISOU 5830 CA THR B 319 1311 1094 1265 41 -34 -153 C ATOM 5831 C THR B 319 32.815 5.704 -15.193 1.00 9.89 C ANISOU 5831 C THR B 319 1212 1099 1448 37 -84 23 C ATOM 5832 O THR B 319 32.833 6.944 -15.344 1.00 9.34 O ANISOU 5832 O THR B 319 1151 1010 1387 23 -59 55 O ATOM 5833 CB THR B 319 30.641 4.474 -14.723 1.00 10.39 C ANISOU 5833 CB THR B 319 1403 1143 1403 11 46 -187 C ATOM 5834 OG1 THR B 319 29.556 3.823 -15.435 1.00 12.33 O ANISOU 5834 OG1 THR B 319 1388 1520 1778 -60 -91 -40 O ATOM 5835 CG2 THR B 319 30.075 5.693 -14.017 1.00 11.27 C ANISOU 5835 CG2 THR B 319 1522 1300 1462 173 184 -111 C ATOM 5836 N LEU B 320 33.683 5.069 -14.375 1.00 9.31 N ANISOU 5836 N LEU B 320 1003 1213 1322 172 -101 -186 N ATOM 5837 CA LEU B 320 34.747 5.909 -13.777 1.00 10.33 C ANISOU 5837 CA LEU B 320 1095 1414 1418 54 -193 13 C ATOM 5838 C LEU B 320 35.646 6.545 -14.837 1.00 10.11 C ANISOU 5838 C LEU B 320 1366 1265 1210 108 -136 13 C ATOM 5839 O LEU B 320 36.061 7.706 -14.664 1.00 8.98 O ANISOU 5839 O LEU B 320 1073 1323 1017 71 40 -50 O ATOM 5840 CB LEU B 320 35.651 5.094 -12.841 1.00 11.08 C ANISOU 5840 CB LEU B 320 1481 1429 1302 229 -238 14 C ATOM 5841 CG LEU B 320 36.351 5.732 -11.659 1.00 12.95 C ANISOU 5841 CG LEU B 320 1569 1578 1775 254 -461 -62 C ATOM 5842 CD1 LEU B 320 37.624 5.067 -11.171 1.00 9.20 C ANISOU 5842 CD1 LEU B 320 831 1323 1339 -42 -124 -193 C ATOM 5843 CD2 LEU B 320 36.227 7.166 -11.290 1.00 12.70 C ANISOU 5843 CD2 LEU B 320 1560 1418 1848 -108 -520 67 C ATOM 5844 N TYR B 321 35.968 5.833 -15.925 1.00 10.07 N ANISOU 5844 N TYR B 321 1180 1252 1395 194 113 42 N ATOM 5845 CA TYR B 321 36.789 6.429 -16.978 1.00 10.16 C ANISOU 5845 CA TYR B 321 1343 1205 1312 129 29 100 C ATOM 5846 C TYR B 321 36.087 7.660 -17.556 1.00 10.28 C ANISOU 5846 C TYR B 321 1266 1109 1532 83 -5 10 C ATOM 5847 O TYR B 321 36.704 8.725 -17.703 1.00 10.22 O ANISOU 5847 O TYR B 321 1135 1162 1587 71 54 109 O ATOM 5848 CB TYR B 321 37.039 5.386 -18.066 1.00 10.41 C ANISOU 5848 CB TYR B 321 1380 1199 1378 112 68 83 C ATOM 5849 CG TYR B 321 37.932 5.919 -19.178 1.00 11.98 C ANISOU 5849 CG TYR B 321 1683 1360 1510 8 173 92 C ATOM 5850 CD1 TYR B 321 39.244 6.285 -18.908 1.00 13.47 C ANISOU 5850 CD1 TYR B 321 1671 1689 1759 59 256 31 C ATOM 5851 CD2 TYR B 321 37.401 6.019 -20.455 1.00 13.23 C ANISOU 5851 CD2 TYR B 321 1953 1510 1562 2 80 -13 C ATOM 5852 CE1 TYR B 321 40.031 6.814 -19.943 1.00 14.53 C ANISOU 5852 CE1 TYR B 321 1901 1744 1874 52 225 166 C ATOM 5853 CE2 TYR B 321 38.213 6.553 -21.479 1.00 15.64 C ANISOU 5853 CE2 TYR B 321 2068 1995 1881 -31 218 34 C ATOM 5854 CZ TYR B 321 39.492 6.927 -21.196 1.00 15.77 C ANISOU 5854 CZ TYR B 321 2112 1957 1923 -25 151 16 C ATOM 5855 OH TYR B 321 40.303 7.394 -22.213 1.00 18.49 O ANISOU 5855 OH TYR B 321 2453 2390 2182 4 295 235 O ATOM 5856 N TYR B 322 34.793 7.518 -17.893 1.00 9.83 N ANISOU 5856 N TYR B 322 1198 1123 1413 181 -14 -61 N ATOM 5857 CA TYR B 322 34.039 8.702 -18.336 1.00 10.14 C ANISOU 5857 CA TYR B 322 1220 1187 1444 98 9 -23 C ATOM 5858 C TYR B 322 34.139 9.800 -17.285 1.00 9.57 C ANISOU 5858 C TYR B 322 1138 1189 1308 49 -57 -3 C ATOM 5859 O TYR B 322 34.327 10.966 -17.654 1.00 10.43 O ANISOU 5859 O TYR B 322 1430 1220 1315 -21 -4 -115 O ATOM 5860 CB TYR B 322 32.559 8.295 -18.567 1.00 10.77 C ANISOU 5860 CB TYR B 322 1279 1309 1505 41 -115 27 C ATOM 5861 CG TYR B 322 31.700 9.470 -18.984 1.00 12.14 C ANISOU 5861 CG TYR B 322 1522 1364 1729 107 -70 54 C ATOM 5862 CD1 TYR B 322 31.621 9.844 -20.320 1.00 14.02 C ANISOU 5862 CD1 TYR B 322 1758 1748 1820 81 -78 140 C ATOM 5863 CD2 TYR B 322 31.036 10.205 -17.988 1.00 11.94 C ANISOU 5863 CD2 TYR B 322 1359 1454 1724 49 -33 43 C ATOM 5864 CE1 TYR B 322 30.827 10.941 -20.682 1.00 14.81 C ANISOU 5864 CE1 TYR B 322 1830 1744 2054 124 33 154 C ATOM 5865 CE2 TYR B 322 30.296 11.323 -18.345 1.00 13.83 C ANISOU 5865 CE2 TYR B 322 1640 1608 2005 148 -69 127 C ATOM 5866 CZ TYR B 322 30.219 11.653 -19.688 1.00 15.40 C ANISOU 5866 CZ TYR B 322 1900 1905 2045 131 55 157 C ATOM 5867 OH TYR B 322 29.437 12.750 -20.019 1.00 18.03 O ANISOU 5867 OH TYR B 322 2194 2145 2512 274 87 392 O ATOM 5868 N MET B 323 33.936 9.515 -15.997 1.00 9.26 N ANISOU 5868 N MET B 323 992 1244 1284 104 3 -112 N ATOM 5869 CA MET B 323 33.991 10.533 -14.953 1.00 9.31 C ANISOU 5869 CA MET B 323 1141 1260 1136 79 -8 -8 C ATOM 5870 C MET B 323 35.317 11.272 -14.930 1.00 8.91 C ANISOU 5870 C MET B 323 1153 1065 1166 97 19 38 C ATOM 5871 O MET B 323 35.392 12.508 -14.761 1.00 9.40 O ANISOU 5871 O MET B 323 1094 1020 1459 13 20 -78 O ATOM 5872 CB MET B 323 33.691 9.970 -13.552 1.00 8.96 C ANISOU 5872 CB MET B 323 936 1345 1123 -87 205 -36 C ATOM 5873 CG MET B 323 32.257 9.433 -13.319 1.00 7.05 C ANISOU 5873 CG MET B 323 890 1475 314 -16 187 -84 C ATOM 5874 SD MET B 323 32.002 8.749 -11.641 1.00 2.63 S ANISOU 5874 SD MET B 323 405 258 337 15 -1 15 S ATOM 5875 CE MET B 323 32.080 10.320 -10.785 1.00 6.51 C ANISOU 5875 CE MET B 323 1173 906 396 -92 -312 -121 C ATOM 5876 N ILE B 324 36.447 10.544 -14.988 1.00 9.62 N ANISOU 5876 N ILE B 324 -Err-TimeOut: Server timeout, connection closed