HEADER LYASE 15-NOV-99 1QOP TITLE CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE TITLE 2 COMPLEXED WITH INDOLE PROPANOL PHOSPHATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRYPTOPHAN SYNTHASE ALPHA CHAIN; COMPND 3 CHAIN: A; COMPND 4 EC: 4.2.1.20; COMPND 5 OTHER_DETAILS: INHIBITOR INDOLE PROPANOL PHOSPHATE BOUND TO COMPND 6 THE ALPHA SITE; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: TRYPTOPHAN SYNTHASE BETA CHAIN; COMPND 9 CHAIN: B; COMPND 10 EC: 4.2.1.20 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM; SOURCE 3 CELL_LINE: CB149; SOURCE 4 PLASMID: PSTB7; SOURCE 5 GENE: TRPA/TRPB SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM; SOURCE 9 CELL_LINE: CB149; SOURCE 10 PLASMID: PSTB7; SOURCE 11 GENE: TRPA/TRPB SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI KEYWDS LYASE, CARBON-OXYGEN LYASE, TRYPTOPHAN BIOSYNTHESIS, KEYWDS 2 PYRIDOXAL PHOSPHATE EXPDTA X-RAY DIFFRACTION AUTHOR M.WEYAND,I.SCHLICHTING REVDAT 1 10-NOV-00 1QOP 0 JRNL AUTH M.WEYAND,I.SCHLICHTING JRNL TITL CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE JRNL TITL 2 COMPLEXED WITH THE NATURAL SUBSTRATE JRNL TITL 3 INDOLE-3-GLYCEROL PHOSPHATE JRNL REF BIOCHEMISTRY V. 38 16469 1999 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. 1.4 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) : 1.4 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : 95 REMARK 3 NUMBER OF REFLECTIONS : 133915 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.150 REMARK 3 FREE R VALUE : 0.177 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 6706 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5044 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 33 REMARK 3 SOLVENT ATOMS : 801 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.0 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): 0.06129 REMARK 3 ESU BASED ON FREE R VALUE (A):0.05539 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A):0.03585 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2):0.91781 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.008 ; 0.02 REMARK 3 ANGLE DISTANCE (A) : 0.023 ; 0.04 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.030 ; 0.05 REMARK 3 H-BOND OR METAL COORDINATION (A) : 0.024 ; 0.05 REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.0212; 0.03 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.103 ; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.18 ; 0.3 REMARK 3 MULTIPLE TORSION (A) : .290 ; 0.3 REMARK 3 H-BOND (X...Y) (A) : 0.134 ; 0.3 REMARK 3 H-BOND (X-H...Y) (A) : 0.3 ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : 15.0 ; NULL REMARK 3 PLANAR (DEGREES) : 3.8 ; 7.0 REMARK 3 STAGGERED (DEGREES) : 12.7 ; 15.0 REMARK 3 TRANSVERSE (DEGREES) : 30.3 ; 20.0 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 3.165 ; 2.0 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.033 ; 3.0 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.798 ; 2.0 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.868 ; 3.0 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES A156, A157 AND A158 REMARK 3 WERE MODELED IN TWO CONFORMATIONS INCLUDING THE MAIN REMARK 3 CHAIN ATOMS. THE SIDE CHAINS OF RESIDUES ILE A30, REMARK 3 GLU A31, CYS A154, SER A178 AND GLU A254 WERE MODELED REMARK 3 IN TWO CONFORMATIONS REMARK 3 THE SIDE CHAINS OF RESIDUES GLU B11, MET B22, REMARK 3 LYS B37, LYS B50, LYS B61, ILE B65, MET B152, REMARK 3 THR B165, LYS B219, MET B240, HIS B260, ARG B341, REMARK 3 GLU B367 AND ARG B379 WERE MODELED IN TWO REMARK 3 CONFORMATIONS REMARK 4 REMARK 4 1QOP COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 16-NOV-1999. REMARK 100 THE EBI ID CODE IS EBI-4202. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUN-1998 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG BEAMLINE X11 REMARK 200 BEAMLINE : X11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9076 REMARK 200 MONOCHROMATOR : SYNCHROTRON REMARK 200 OPTICS : SYNCHROTRON REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH MAR345 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 133934 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.4 REMARK 200 RESOLUTION RANGE LOW (A) : 30.3 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.2 REMARK 200 DATA REDUNDANCY : 2.20 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.057 REMARK 200 FOR THE DATA SET : 10.25 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.4 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.5 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.8 REMARK 200 DATA REDUNDANCY IN SHELL : 1.89 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.258 REMARK 200 FOR SHELL : 2.36 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: 2WSY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.4 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME SOLUTION: 10 MG/ML TRPS REMARK 280 IN 50 MM BICINE PH 7.8, 1 MM EDTA, 5 MM DITHIOERYTHRITOL, REMARK 280 20 MUM PYRIDOXAL-5'-PHOSPHATE. REMARK 280 RESERVOIR SOLUTION: 50 MM BICINE PH 7.8, 5 MM EDTA, REMARK 280 5 MM DITHIOERYTHRITOL, 0.1 MM PYRIDOXAL-5'-PHOSPHATE, REMARK 280 2 MM SPERMINE, 8-12 % PEG 8000. REMARK 280 HANGING DROP GEOMETRY, CRYSTALLIZATION DROP CONSISTED REMARK 280 AN INITIAL INDOLE PROPANOLE PHOSPHATE (IPL) CONCENTRATION REMARK 280 OF 7 MM REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,Z REMARK 290 4555 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 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 91.10000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.15000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.10000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.15000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 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 300 REMARK 300 BIOMOLECULE THE BIOLOGICALLY ACTIVE MOLECULE IS A REMARK 300 TETRAMER OF TWO ALPHA AND TWO BETA CHAINS. 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 182.20000 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 ALA A 190 REMARK 465 LEU A 191 REMARK 465 ALA A 268 REMARK 465 LYS B 392 REMARK 465 ALA B 393 REMARK 465 ARG B 394 REMARK 465 GLY B 395 REMARK 465 GLU B 396 REMARK 465 ILE B 397 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 ARG B 222 CD - NE - CZ ANGL. DEV. = 24.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 REMARK 500 ND2 ASN A 108 OD1 ASN A 109 1.79 REMARK 500 NH2 ARG B 222 O HOH Y 331 2.19 REMARK 500 O GLU B 296 O HOH Y 403 2.05 REMARK 500 O HOH Y 131 O HOH Y 135 2.10 REMARK 500 O HOH Y 131 O HOH Y 324 2.15 REMARK 500 O HOH Y 145 O HOH Y 466 2.14 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 REMARK 500 PHE A 212 104.31 120.40 REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY REMARK 525 ASSOCIATED WITH: REMARK 525 PROTEIN CHAIN SOLVENT CHAIN REMARK 525 A Z REMARK 525 B Y REMARK 600 REMARK 600 HETEROGEN REMARK 600 SUBSTRATE ANALOG IPL BOUND TO THE ALPHA ACTIVE SITE. REMARK 600 REMARK 600 PYRIDOXAL-5'-PHOSPHATE IS COVALENTLY ATTACHED REMARK 600 TO THE NZ NITROGEN ATOM OF LYS B 87 REMARK 600 REMARK 600 FOR METAL ATOM NA NA B 501 THE COORDINATION ANGLES ARE: REMARK 600 1 GLY 232B O REMARK 600 2 SER 308B O 93.8 REMARK 600 3 PHE 306B O 102.4 83.8 REMARK 600 4 HOH 340Y O 90.6 104.7 164.1 REMARK 600 5 HOH 373Y O 104.9 157.5 80.0 87.9 REMARK 600 1 2 3 4 REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: DSSP, KABSCH & SANDER REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: DSSP, KABSCH & SANDER REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: IPL REMARK 800 SITE_DESCRIPTION: SUBSTRATE ANALOG BOUND TO THE ALPHA ACTIVE SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: PLP REMARK 800 SITE_DESCRIPTION: PLP BINDING SITE FOR CHAIN B REMARK 800 REMARK 800 SITE_IDENTIFIER: NA REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR CHAIN B REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2WSY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE REMARK 900 RELATED ID: 1TTP RELATED DB: PDB REMARK 900 TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) IN THE PRESENCE OF CESIUM, REMARK 900 ROOM TEMPERATURE REMARK 900 RELATED ID: 1TTQ RELATED DB: PDB REMARK 900 TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) IN THE PRESENCE OF POTASSIUM REMARK 900 AT ROOM TEMPERATURE REMARK 900 RELATED ID: 2TRS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE REMARK 900 ALPHA-2 BETA-2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES REMARK 900 OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED REMARK 900 CONFORMATIONAL CHANGES REMARK 900 RELATED ID: 2TSY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE REMARK 900 ALPHA-2 BETA-2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES REMARK 900 OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED REMARK 900 CONFORMATIONAL CHANGES REMARK 900 RELATED ID: 1UBS RELATED DB: PDB REMARK 900 TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) WITH A MUTATION OF REMARK 900 LYS 87 ->THR IN THE B SUBUNIT AND IN THE PRESENCE OF REMARK 900 LIGAND L-SERINE REMARK 900 RELATED ID: 1A5A RELATED DB: PDB REMARK 900 CRYO-CRYSTALLOGRAPHY OF A TRUE SUBSTRATE, INDOLE-3-GLYCEROL REMARK 900 PHOSPHATE, BOUND TO A MUTANT (ALPHAD60N) TRYPTOPHAN SYNTHASE REMARK 900 ALPHA2BETA2 COMPLEX REVEALS THE CORRECT ORIENTATION OF REMARK 900 ACTIVE SITE ALPHA GLU 49 REMARK 900 RELATED ID: 1A5B RELATED DB: PDB REMARK 900 CRYO-CRYSTALLOGRAPHY OF A TRUE SUBSTRATE, INDOLE-3-GLYCEROL REMARK 900 PHOSPHATE, BOUND TO A MUTANT (ALPHAD60N) TRYPTOPHAN SYNTHASE REMARK 900 (ALPHA)2(BETA)2 COMPLEX REVEALS THE CORRECT ORIENTATION REMARK 900 OF ACTIVE SITE ALPHA GLU 49 REMARK 900 RELATED ID: 1A5S RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED REMARK 900 WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE AND L-SER BOUND AS REMARK 900 AMINO ACRYLATE TO THE BETA SITE REMARK 900 RELATED ID: 1A50 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED REMARK 900 WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE REMARK 900 RELATED ID: 1BEU RELATED DB: PDB REMARK 900 TRP SYNTHASE (D60N-IPP-SER) WITH K+ REMARK 900 RELATED ID: 1BKS RELATED DB: PDB REMARK 900 TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) FROM SALMONELLA TYPHIMURIUM REMARK 900 RELATED ID: 1QOQ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED REMARK 900 WITH INDOLE GLYCEROL PHOSPHATE REMARK 900 DBREF 1QOP A 1 268 SWS P00929 TRPA_SALTY 1 268 DBREF 1QOP B 2 397 SWS P00933 TRPB_SALTY 1 396 SEQADV 1QOP ILE A 87 SWS P00929 LEU 87 CLONING ARTIFACT SEQADV 1QOP SER B 34 SWS P00929 ARG 33 CLONING ARTIFACT SEQRES 1 A 268 MET GLU ARG TYR GLU ASN LEU PHE ALA GLN LEU ASN ASP SEQRES 2 A 268 ARG ARG GLU GLY ALA PHE VAL PRO PHE VAL THR LEU GLY SEQRES 3 A 268 ASP PRO GLY ILE GLU GLN SER LEU LYS ILE ILE ASP THR SEQRES 4 A 268 LEU ILE ASP ALA GLY ALA ASP ALA LEU GLU LEU GLY VAL SEQRES 5 A 268 PRO PHE SER ASP PRO LEU ALA ASP GLY PRO THR ILE GLN SEQRES 6 A 268 ASN ALA ASN LEU ARG ALA PHE ALA ALA GLY VAL THR PRO SEQRES 7 A 268 ALA GLN CYS PHE GLU MET LEU ALA ILE ILE ARG GLU LYS SEQRES 8 A 268 HIS PRO THR ILE PRO ILE GLY LEU LEU MET TYR ALA ASN SEQRES 9 A 268 LEU VAL PHE ASN ASN GLY ILE ASP ALA PHE TYR ALA ARG SEQRES 10 A 268 CYS GLU GLN VAL GLY VAL ASP SER VAL LEU VAL ALA ASP SEQRES 11 A 268 VAL PRO VAL GLU GLU SER ALA PRO PHE ARG GLN ALA ALA SEQRES 12 A 268 LEU ARG HIS ASN ILE ALA PRO ILE PHE ILE CYS PRO PRO SEQRES 13 A 268 ASN ALA ASP ASP ASP LEU LEU ARG GLN VAL ALA SER TYR SEQRES 14 A 268 GLY ARG GLY TYR THR TYR LEU LEU SER ARG SER GLY VAL SEQRES 15 A 268 THR GLY ALA GLU ASN ARG GLY ALA LEU PRO LEU HIS HIS SEQRES 16 A 268 LEU ILE GLU LYS LEU LYS GLU TYR HIS ALA ALA PRO ALA SEQRES 17 A 268 LEU GLN GLY PHE GLY ILE SER SER PRO GLU GLN VAL SER SEQRES 18 A 268 ALA ALA VAL ARG ALA GLY ALA ALA GLY ALA ILE SER GLY SEQRES 19 A 268 SER ALA ILE VAL LYS ILE ILE GLU LYS ASN LEU ALA SER SEQRES 20 A 268 PRO LYS GLN MET LEU ALA GLU LEU ARG SER PHE VAL SER SEQRES 21 A 268 ALA MET LYS ALA ALA SER ARG ALA SEQRES 1 B 396 THR THR LEU LEU ASN PRO TYR PHE GLY GLU PHE GLY GLY SEQRES 2 B 396 MET TYR VAL PRO GLN ILE LEU MET PRO ALA LEU ASN GLN SEQRES 3 B 396 LEU GLU GLU ALA PHE VAL SER ALA GLN LYS ASP PRO GLU SEQRES 4 B 396 PHE GLN ALA GLN PHE ALA ASP LEU LEU LYS ASN TYR ALA SEQRES 5 B 396 GLY ARG PRO THR ALA LEU THR LYS CYS GLN ASN ILE THR SEQRES 6 B 396 ALA GLY THR ARG THR THR LEU TYR LEU LYS ARG GLU ASP SEQRES 7 B 396 LEU LEU HIS GLY GLY ALA HIS LYS THR ASN GLN VAL LEU SEQRES 8 B 396 GLY GLN ALA LEU LEU ALA LYS ARG MET GLY LYS SER GLU SEQRES 9 B 396 ILE ILE ALA GLU THR GLY ALA GLY GLN HIS GLY VAL ALA SEQRES 10 B 396 SER ALA LEU ALA SER ALA LEU LEU GLY LEU LYS CYS ARG SEQRES 11 B 396 ILE TYR MET GLY ALA LYS ASP VAL GLU ARG GLN SER PRO SEQRES 12 B 396 ASN VAL PHE ARG MET ARG LEU MET GLY ALA GLU VAL ILE SEQRES 13 B 396 PRO VAL HIS SER GLY SER ALA THR LEU LYS ASP ALA CYS SEQRES 14 B 396 ASN GLU ALA LEU ARG ASP TRP SER GLY SER TYR GLU THR SEQRES 15 B 396 ALA HIS TYR MET LEU GLY THR ALA ALA GLY PRO HIS PRO SEQRES 16 B 396 TYR PRO THR ILE VAL ARG GLU PHE GLN ARG MET ILE GLY SEQRES 17 B 396 GLU GLU THR LYS ALA GLN ILE LEU ASP LYS GLU GLY ARG SEQRES 18 B 396 LEU PRO ASP ALA VAL ILE ALA CYS VAL GLY GLY GLY SER SEQRES 19 B 396 ASN ALA ILE GLY MET PHE ALA ASP PHE ILE ASN ASP THR SEQRES 20 B 396 SER VAL GLY LEU ILE GLY VAL GLU PRO GLY GLY HIS GLY SEQRES 21 B 396 ILE GLU THR GLY GLU HIS GLY ALA PRO LEU LYS HIS GLY SEQRES 22 B 396 ARG VAL GLY ILE TYR PHE GLY MET LYS ALA PRO MET MET SEQRES 23 B 396 GLN THR ALA ASP GLY GLN ILE GLU GLU SER TYR SER ILE SEQRES 24 B 396 SER ALA GLY LEU ASP PHE PRO SER VAL GLY PRO GLN HIS SEQRES 25 B 396 ALA TYR LEU ASN SER ILE GLY ARG ALA ASP TYR VAL SER SEQRES 26 B 396 ILE THR ASP ASP GLU ALA LEU GLU ALA PHE LYS THR LEU SEQRES 27 B 396 CYS ARG HIS GLU GLY ILE ILE PRO ALA LEU GLU SER SER SEQRES 28 B 396 HIS ALA LEU ALA HIS ALA LEU LYS MET MET ARG GLU GLN SEQRES 29 B 396 PRO GLU LYS GLU GLN LEU LEU VAL VAL ASN LEU SER GLY SEQRES 30 B 396 ARG GLY ASP LYS ASP ILE PHE THR VAL HIS ASP ILE LEU SEQRES 31 B 396 LYS ALA ARG GLY GLU ILE HET IPL A 300 17 SEE REMARK 600 HET PLP B 500 15 SEE REMARK 600 HET NA B 501 1 HETNAM IPL INDOLE-3-PROPANOL PHOSPHATE HETNAM PLP PYRIDOXAL-5'-PHOSPHATE HETNAM NA SODIUM ION HETSYN IPL INDOLE PROPANOL PHOSPHATE FORMUL 3 IPL C11 H14 N1 O4 P1 FORMUL 4 PLP C8 H10 N1 O6 P1 FORMUL 5 NA NA1 1+ FORMUL 6 HOH *801(H2 O1) HELIX 1 1 GLU A 2 ARG A 14 1 13 HELIX 2 2 GLY A 29 ALA A 43 1 15 HELIX 3 3 GLY A 61 ALA A 74 1 14 HELIX 4 4 THR A 77 HIS A 92 1 16 HELIX 5 5 TYR A 102 ASN A 108 1 7 HELIX 6 6 GLY A 110 GLY A 122 1 13 HELIX 7 7 PRO A 132 GLU A 135 5 4 HELIX 8 8 SER A 136 HIS A 146 1 11 HELIX 9 9 ASP A 159 GLY A 170 1 12 HELIX 10 10 LEU A 193 TYR A 203 1 11 HELIX 11 11 SER A 216 ALA A 226 1 11 HELIX 12 12 GLY A 234 ASN A 244 1 11 HELIX 13 13 SER A 247 ALA A 265 1 19 HELIX 14 14 PRO B 18 ILE B 20 5 3 HELIX 15 15 LEU B 21 LYS B 37 1 17 HELIX 16 16 ASP B 38 TYR B 52 1 15 HELIX 17 17 CYS B 62 ALA B 67 1 6 HELIX 18 18 ASP B 79 LEU B 81 5 3 HELIX 19 19 LYS B 87 MET B 101 1 15 HELIX 20 20 GLY B 113 GLY B 127 1 15 HELIX 21 21 ALA B 136 GLN B 142 1 7 HELIX 22 22 GLN B 142 MET B 152 1 11 HELIX 23 23 THR B 165 TYR B 181 1 17 HELIX 24 24 PRO B 196 PHE B 204 1 9 HELIX 25 25 ARG B 206 GLY B 221 1 16 HELIX 26 26 GLY B 234 ALA B 242 1 9 HELIX 27 27 ASP B 243 ILE B 245 5 3 HELIX 28 28 ILE B 262 GLY B 265 5 4 HELIX 29 29 ALA B 269 GLY B 274 1 6 HELIX 30 30 SER B 301 ASP B 305 5 5 HELIX 31 31 GLY B 310 ILE B 319 1 10 HELIX 32 32 ASP B 329 GLY B 344 1 16 HELIX 33 33 ALA B 348 GLN B 365 1 18 HELIX 34 34 GLY B 380 LYS B 382 5 3 HELIX 35 35 ASP B 383 LEU B 391 1 9 SHEET 1 A 9 ALA A 149 ILE A 151 0 SHEET 2 A 9 SER A 125 VAL A 128 1 O VAL A 126 N ILE A 151 SHEET 3 A 9 ILE A 97 MET A 101 1 O LEU A 99 N LEU A 127 SHEET 4 A 9 LEU A 48 GLY A 51 1 O LEU A 48 N GLY A 98 SHEET 5 A 9 ALA A 18 THR A 24 1 O PRO A 21 N GLU A 49 SHEET 6 A 9 GLY A 230 SER A 233 1 O ALA A 231 N VAL A 20 SHEET 7 A 9 ALA A 208 GLY A 211 1 O GLN A 210 N ILE A 232 SHEET 8 A 9 THR A 174 LEU A 177 1 O THR A 174 N LEU A 209 SHEET 9 A 9 ILE A 153 CYS A 154 1 O CYS A 154 N LEU A 177 SHEET 1 B 4 TYR B 8 PHE B 9 0 SHEET 2 B 4 PHE B 12 TYR B 16 -1 O PHE B 12 N PHE B 9 SHEET 3 B 4 GLY B 281 MET B 286 -1 O GLY B 281 N TYR B 16 SHEET 4 B 4 ARG B 275 TYR B 279 -1 O ARG B 275 N MET B 286 SHEET 1 C 6 LEU B 59 LYS B 61 0 SHEET 2 C 6 THR B 71 ARG B 77 -1 O LEU B 75 N THR B 60 SHEET 3 C 6 GLN B 370 LEU B 376 1 O GLN B 370 N THR B 72 SHEET 4 C 6 ALA B 226 CYS B 230 1 O ALA B 226 N VAL B 373 SHEET 5 C 6 GLY B 251 GLY B 259 1 O GLY B 251 N VAL B 227 SHEET 6 C 6 ASP B 323 THR B 328 1 O ASP B 323 N GLY B 254 SHEET 1 D 4 GLU B 155 VAL B 159 0 SHEET 2 D 4 LYS B 129 GLY B 135 1 O CYS B 130 N GLU B 155 SHEET 3 D 4 GLU B 105 THR B 110 1 O ILE B 106 N ARG B 131 SHEET 4 D 4 ALA B 184 TYR B 186 1 O HIS B 185 N ILE B 107 LINK NZ LYS B 87 C4A PLP B 500 1555 1555 LINK NA NA B 501 O HOH Y 373 1555 1555 LINK NA NA B 501 O SER B 308 1555 1555 LINK NA NA B 501 O PHE B 306 1555 1555 LINK NA NA B 501 O HOH Y 340 1555 1555 LINK NA NA B 501 O GLY B 232 1555 1555 CISPEP 1 ASP A 27 PRO A 28 0 4.22 CISPEP 2 ARG B 55 PRO B 56 0 -1.93 CISPEP 3 HIS B 195 PRO B 196 0 12.25 SITE 1 IPL 13 PHE A 22 ASP A 60 ILE A 64 LEU A 100 SITE 2 IPL 13 TYR A 175 THR A 183 GLY A 184 PHE A 212 SITE 3 IPL 13 GLY A 213 GLY A 234 SER A 235 HOH Z 276 SITE 4 IPL 13 HOH Z 277 SITE 1 PLP 16 HIS B 86 LYS B 87 THR B 190 CYS B 230 SITE 2 PLP 16 GLY B 232 GLY B 233 GLY B 234 SER B 235 SITE 3 PLP 16 ASN B 236 GLY B 303 GLU B 350 SER B 377 SITE 4 PLP 16 GLY B 378 HOH Y 216 HOH Y 298 HOH Y 339 SITE 1 NA 5 GLY B 232 PHE B 306 SER B 308 HOH Y 340 SITE 2 NA 5 HOH Y 373 CRYST1 182.200 60.300 67.400 90.00 94.70 90.00 C 1 2 1 4 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 0.005488 0.000000 0.000451 0.00000 SCALE2 0.000000 0.016584 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014887 0.00000 ATOM 1 N MET A 1 38.084 23.562 34.947 1.00 39.30 N ANISOU 1 N MET A 1 4935 4816 5180 -15 -36 229 N ATOM 2 CA MET A 1 36.957 24.344 34.357 1.00 37.59 C ANISOU 2 CA MET A 1 4678 4833 4774 -185 -91 119 C ATOM 3 C MET A 1 36.435 23.658 33.104 1.00 34.84 C ANISOU 3 C MET A 1 4257 4403 4577 2 20 269 C ATOM 4 O MET A 1 36.939 22.601 32.722 1.00 36.96 O ANISOU 4 O MET A 1 4492 4374 5178 -115 73 150 O ATOM 5 CB MET A 1 37.401 25.775 34.054 1.00 39.37 C ANISOU 5 CB MET A 1 4982 4889 5087 -181 26 217 C ATOM 6 CG MET A 1 37.928 26.544 35.253 1.00 41.92 C ANISOU 6 CG MET A 1 5397 5368 5164 -188 -60 71 C ATOM 7 SD MET A 1 36.613 27.399 36.143 1.00 46.33 S ANISOU 7 SD MET A 1 5867 5989 5747 -13 129 -103 S ATOM 8 CE MET A 1 36.027 28.499 34.847 1.00 44.52 C ANISOU 8 CE MET A 1 5620 5561 5734 -80 173 -88 C ATOM 9 N GLU A 2 35.436 24.250 32.462 1.00 31.82 N ANISOU 9 N GLU A 2 4073 4268 3747 -339 -39 146 N ATOM 10 CA GLU A 2 34.850 23.710 31.243 1.00 28.90 C ANISOU 10 CA GLU A 2 3925 3515 3541 -144 51 362 C ATOM 11 C GLU A 2 34.621 24.818 30.220 1.00 21.67 C ANISOU 11 C GLU A 2 2299 3182 2751 -466 136 -7 C ATOM 12 O GLU A 2 33.546 24.929 29.636 1.00 19.44 O ANISOU 12 O GLU A 2 2275 2718 2393 -733 259 442 O ATOM 13 CB GLU A 2 33.513 23.025 31.570 1.00 35.14 C ANISOU 13 CB GLU A 2 4021 4736 4593 -442 160 71 C ATOM 14 CG GLU A 2 33.669 21.811 32.476 1.00 42.34 C ANISOU 14 CG GLU A 2 5582 5278 5226 27 -38 353 C ATOM 15 CD GLU A 2 32.407 20.994 32.651 1.00 46.76 C ANISOU 15 CD GLU A 2 5754 5953 6061 -216 127 124 C ATOM 16 OE1 GLU A 2 31.375 21.356 32.048 1.00 49.51 O ANISOU 16 OE1 GLU A 2 6100 6391 6320 -78 -42 151 O ATOM 17 OE2 GLU A 2 32.424 19.983 33.388 1.00 48.87 O ANISOU 17 OE2 GLU A 2 6241 6012 6317 -146 149 151 O ATOM 18 N ARG A 3 35.638 25.652 29.974 1.00 18.05 N ANISOU 18 N ARG A 3 2379 2340 2140 -86 252 241 N ATOM 19 CA ARG A 3 35.463 26.785 29.078 1.00 14.85 C ANISOU 19 CA ARG A 3 1805 1994 1844 -108 79 -107 C ATOM 20 C ARG A 3 35.174 26.409 27.639 1.00 13.71 C ANISOU 20 C ARG A 3 1659 1548 2001 -129 16 -324 C ATOM 21 O ARG A 3 34.338 27.075 27.006 1.00 15.08 O ANISOU 21 O ARG A 3 1728 1727 2275 -58 -2 -185 O ATOM 22 CB ARG A 3 36.621 27.775 29.188 1.00 15.29 C ANISOU 22 CB ARG A 3 2072 1913 1824 -187 -15 -207 C ATOM 23 CG ARG A 3 36.722 28.388 30.588 1.00 14.88 C ANISOU 23 CG ARG A 3 1956 1837 1860 -101 214 -243 C ATOM 24 CD ARG A 3 37.653 29.591 30.564 1.00 14.09 C ANISOU 24 CD ARG A 3 2059 1782 1511 -124 -16 -143 C ATOM 25 NE ARG A 3 37.820 30.166 31.893 1.00 15.36 N ANISOU 25 NE ARG A 3 2352 1833 1651 190 487 -515 N ATOM 26 CZ ARG A 3 38.671 29.764 32.820 1.00 15.10 C ANISOU 26 CZ ARG A 3 2583 1757 1399 -27 479 -346 C ATOM 27 NH1 ARG A 3 39.525 28.772 32.607 1.00 15.16 N ANISOU 27 NH1 ARG A 3 2641 1419 1702 -221 707 -287 N ATOM 28 NH2 ARG A 3 38.689 30.381 34.010 1.00 16.94 N ANISOU 28 NH2 ARG A 3 3006 1980 1449 -693 510 -446 N ATOM 29 N TYR A 4 35.842 25.409 27.066 1.00 13.76 N ANISOU 29 N TYR A 4 1905 1377 1945 136 34 41 N ATOM 30 CA TYR A 4 35.542 25.030 25.689 1.00 14.33 C ANISOU 30 CA TYR A 4 1659 1640 2147 245 -20 -288 C ATOM 31 C TYR A 4 34.127 24.459 25.600 1.00 14.22 C ANISOU 31 C TYR A 4 1788 1462 2153 99 261 -91 C ATOM 32 O TYR A 4 33.408 24.785 24.659 1.00 16.65 O ANISOU 32 O TYR A 4 2041 1698 2587 51 -309 -427 O ATOM 33 CB TYR A 4 36.547 24.033 25.114 1.00 13.64 C ANISOU 33 CB TYR A 4 1579 1467 2135 131 187 -139 C ATOM 34 CG TYR A 4 37.882 24.642 24.759 1.00 12.61 C ANISOU 34 CG TYR A 4 1399 1655 1738 247 146 -282 C ATOM 35 CD1 TYR A 4 38.073 25.394 23.607 1.00 12.43 C ANISOU 35 CD1 TYR A 4 1741 1191 1790 245 2 -363 C ATOM 36 CD2 TYR A 4 38.968 24.467 25.619 1.00 12.65 C ANISOU 36 CD2 TYR A 4 1474 1664 1670 259 88 -383 C ATOM 37 CE1 TYR A 4 39.316 25.934 23.303 1.00 13.09 C ANISOU 37 CE1 TYR A 4 1732 1161 2079 193 -96 -342 C ATOM 38 CE2 TYR A 4 40.201 25.012 25.331 1.00 12.21 C ANISOU 38 CE2 TYR A 4 1743 1143 1752 141 160 -306 C ATOM 39 CZ TYR A 4 40.376 25.743 24.175 1.00 11.78 C ANISOU 39 CZ TYR A 4 1675 1133 1665 347 135 -337 C ATOM 40 OH TYR A 4 41.612 26.277 23.888 1.00 12.81 O ANISOU 40 OH TYR A 4 1504 1275 2087 235 -189 -722 O ATOM 41 N GLU A 5 33.768 23.627 26.574 1.00 17.29 N ANISOU 41 N GLU A 5 2043 1963 2566 -377 486 80 N ATOM 42 CA GLU A 5 32.425 23.023 26.527 1.00 17.30 C ANISOU 42 CA GLU A 5 1768 2001 2805 -54 271 106 C ATOM 43 C GLU A 5 31.346 24.095 26.550 1.00 17.31 C ANISOU 43 C GLU A 5 1797 2074 2706 14 164 -157 C ATOM 44 O GLU A 5 30.369 24.037 25.793 1.00 19.38 O ANISOU 44 O GLU A 5 1956 2319 3090 -64 -4 -15 O ATOM 45 CB GLU A 5 32.298 22.037 27.693 1.00 20.61 C ANISOU 45 CB GLU A 5 2601 2436 2792 -393 342 259 C ATOM 46 CG GLU A 5 33.212 20.832 27.593 1.00 27.73 C ANISOU 46 CG GLU A 5 3442 3131 3964 205 112 0 C ATOM 47 CD GLU A 5 34.695 21.105 27.742 1.00 32.58 C ANISOU 47 CD GLU A 5 3661 4010 4708 -65 -93 -179 C ATOM 48 OE1 GLU A 5 35.114 22.099 28.377 1.00 30.47 O ANISOU 48 OE1 GLU A 5 3375 3926 4275 152 -344 -16 O ATOM 49 OE2 GLU A 5 35.472 20.280 27.201 1.00 35.80 O ANISOU 49 OE2 GLU A 5 3923 4477 5202 267 10 -249 O ATOM 50 N ASN A 6 31.517 25.095 27.420 1.00 17.31 N ANISOU 50 N ASN A 6 1729 2251 2599 -85 63 -180 N ATOM 51 CA ASN A 6 30.563 26.201 27.521 1.00 18.07 C ANISOU 51 CA ASN A 6 1933 2297 2637 18 30 -54 C ATOM 52 C ASN A 6 30.518 27.016 26.236 1.00 18.35 C ANISOU 52 C ASN A 6 1781 2456 2735 -31 64 78 C ATOM 53 O ASN A 6 29.451 27.335 25.702 1.00 19.49 O ANISOU 53 O ASN A 6 1282 2925 3199 119 485 -36 O ATOM 54 CB ASN A 6 30.877 27.100 28.714 1.00 19.46 C ANISOU 54 CB ASN A 6 2282 2421 2691 -152 69 -134 C ATOM 55 CG ASN A 6 30.748 26.451 30.070 1.00 23.22 C ANISOU 55 CG ASN A 6 2952 2943 2927 -148 85 151 C ATOM 56 OD1 ASN A 6 31.286 26.931 31.080 1.00 28.13 O ANISOU 56 OD1 ASN A 6 3557 3821 3311 -303 -155 -168 O ATOM 57 ND2 ASN A 6 30.040 25.333 30.146 1.00 22.12 N ANISOU 57 ND2 ASN A 6 2909 2894 2603 -164 75 -27 N ATOM 58 N LEU A 7 31.696 27.312 25.661 1.00 16.53 N ANISOU 58 N LEU A 7 1800 2056 2426 -43 -14 236 N ATOM 59 CA LEU A 7 31.726 28.053 24.404 1.00 14.72 C ANISOU 59 CA LEU A 7 1442 1634 2517 128 -69 196 C ATOM 60 C LEU A 7 31.000 27.331 23.279 1.00 16.92 C ANISOU 60 C LEU A 7 1715 2022 2691 193 -181 -72 C ATOM 61 O LEU A 7 30.176 27.921 22.563 1.00 17.26 O ANISOU 61 O LEU A 7 1497 2218 2843 260 -54 15 O ATOM 62 CB LEU A 7 33.177 28.341 23.967 1.00 15.96 C ANISOU 62 CB LEU A 7 1575 1950 2537 -198 39 -4 C ATOM 63 CG LEU A 7 33.283 28.977 22.576 1.00 15.98 C ANISOU 63 CG LEU A 7 1512 1786 2772 -99 116 188 C ATOM 64 CD1 LEU A 7 32.682 30.382 22.599 1.00 16.54 C ANISOU 64 CD1 LEU A 7 1868 2024 2392 234 -107 -93 C ATOM 65 CD2 LEU A 7 34.718 28.963 22.067 1.00 16.68 C ANISOU 65 CD2 LEU A 7 1486 2294 2558 -62 20 127 C ATOM 66 N PHE A 8 31.328 26.051 23.064 1.00 17.28 N ANISOU 66 N PHE A 8 1820 1968 2780 -8 -199 -115 N ATOM 67 CA PHE A 8 30.736 25.315 21.953 1.00 17.75 C ANISOU 67 CA PHE A 8 1756 2352 2635 -62 -358 46 C ATOM 68 C PHE A 8 29.230 25.167 22.144 1.00 19.45 C ANISOU 68 C PHE A 8 1819 2746 2825 -47 -116 65 C ATOM 69 O PHE A 8 28.516 25.242 21.139 1.00 20.19 O ANISOU 69 O PHE A 8 1559 2708 3404 -56 -422 117 O ATOM 70 CB PHE A 8 31.435 23.976 21.753 1.00 17.16 C ANISOU 70 CB PHE A 8 1697 2450 2373 -112 4 -173 C ATOM 71 CG PHE A 8 32.813 24.127 21.171 1.00 15.13 C ANISOU 71 CG PHE A 8 1487 2145 2116 -26 -260 -99 C ATOM 72 CD1 PHE A 8 33.010 24.861 20.016 1.00 16.15 C ANISOU 72 CD1 PHE A 8 1721 2145 2272 -207 -404 52 C ATOM 73 CD2 PHE A 8 33.915 23.547 21.782 1.00 15.28 C ANISOU 73 CD2 PHE A 8 1746 2082 1979 89 -205 130 C ATOM 74 CE1 PHE A 8 34.271 25.012 19.471 1.00 17.88 C ANISOU 74 CE1 PHE A 8 1745 2359 2688 329 -176 103 C ATOM 75 CE2 PHE A 8 35.175 23.692 21.246 1.00 16.23 C ANISOU 75 CE2 PHE A 8 1972 2254 1943 68 70 -230 C ATOM 76 CZ PHE A 8 35.369 24.422 20.091 1.00 17.16 C ANISOU 76 CZ PHE A 8 1959 2226 2337 309 -195 170 C ATOM 77 N ALA A 9 28.794 25.028 23.393 1.00 19.11 N ANISOU 77 N ALA A 9 1523 2711 3027 -163 81 52 N ATOM 78 CA ALA A 9 27.345 24.928 23.638 1.00 20.85 C ANISOU 78 CA ALA A 9 1635 3254 3033 -254 305 244 C ATOM 79 C ALA A 9 26.648 26.229 23.272 1.00 21.23 C ANISOU 79 C ALA A 9 1775 3184 3107 -161 167 -72 C ATOM 80 O ALA A 9 25.561 26.216 22.663 1.00 24.39 O ANISOU 80 O ALA A 9 1381 4116 3770 -195 300 258 O ATOM 81 CB ALA A 9 27.106 24.530 25.079 1.00 21.77 C ANISOU 81 CB ALA A 9 1859 3377 3037 -335 197 350 C ATOM 82 N GLN A 10 27.255 27.352 23.621 1.00 21.12 N ANISOU 82 N GLN A 10 1805 2863 3357 -26 330 28 N ATOM 83 CA GLN A 10 26.726 28.675 23.311 1.00 21.66 C ANISOU 83 CA GLN A 10 2140 3020 3072 162 45 -8 C ATOM 84 C GLN A 10 26.703 28.904 21.803 1.00 21.76 C ANISOU 84 C GLN A 10 2199 2986 3082 173 4 64 C ATOM 85 O GLN A 10 25.735 29.385 21.221 1.00 22.41 O ANISOU 85 O GLN A 10 1748 3260 3505 329 125 -162 O ATOM 86 CB GLN A 10 27.562 29.762 23.993 1.00 24.06 C ANISOU 86 CB GLN A 10 2570 3148 3425 80 -77 -194 C ATOM 87 CG GLN A 10 27.572 29.708 25.505 1.00 29.10 C ANISOU 87 CG GLN A 10 3712 3782 3562 69 126 51 C ATOM 88 CD GLN A 10 28.739 30.426 26.146 1.00 32.16 C ANISOU 88 CD GLN A 10 4098 4150 3969 -111 -71 -143 C ATOM 89 OE1 GLN A 10 29.590 31.054 25.504 1.00 32.57 O ANISOU 89 OE1 GLN A 10 4278 4127 3969 -22 80 -130 O ATOM 90 NE2 GLN A 10 28.806 30.320 27.474 1.00 33.74 N ANISOU 90 NE2 GLN A 10 4406 4404 4010 61 226 -131 N ATOM 91 N LEU A 11 27.793 28.551 21.129 1.00 20.33 N ANISOU 91 N LEU A 11 1942 2758 3025 31 -194 -97 N ATOM 92 CA LEU A 11 27.886 28.695 19.689 1.00 20.79 C ANISOU 92 CA LEU A 11 1980 2862 3057 -125 -14 -54 C ATOM 93 C LEU A 11 26.844 27.824 18.987 1.00 22.46 C ANISOU 93 C LEU A 11 2353 3085 3096 -216 -371 17 C ATOM 94 O LEU A 11 26.203 28.273 18.034 1.00 24.32 O ANISOU 94 O LEU A 11 2601 3154 3484 -207 -551 227 O ATOM 95 CB LEU A 11 29.296 28.327 19.215 1.00 19.33 C ANISOU 95 CB LEU A 11 2004 2565 2776 62 -124 77 C ATOM 96 CG LEU A 11 30.369 29.353 19.597 1.00 19.62 C ANISOU 96 CG LEU A 11 1908 2521 3027 220 -233 -48 C ATOM 97 CD1 LEU A 11 31.720 28.831 19.135 1.00 19.59 C ANISOU 97 CD1 LEU A 11 1594 2925 2924 -112 -124 112 C ATOM 98 CD2 LEU A 11 30.067 30.706 18.972 1.00 21.84 C ANISOU 98 CD2 LEU A 11 2324 2658 3316 -57 -51 309 C ATOM 99 N ASN A 12 26.664 26.604 19.488 1.00 24.32 N ANISOU 99 N ASN A 12 2360 3189 3692 -206 -42 142 N ATOM 100 CA ASN A 12 25.666 25.718 18.872 1.00 27.55 C ANISOU 100 CA ASN A 12 2934 3752 3783 -302 -369 -190 C ATOM 101 C ASN A 12 24.267 26.290 19.058 1.00 29.87 C ANISOU 101 C ASN A 12 3114 4215 4022 -112 -118 -118 C ATOM 102 O ASN A 12 23.434 26.191 18.151 1.00 30.55 O ANISOU 102 O ASN A 12 2890 4360 4356 -381 -179 -155 O ATOM 103 CB ASN A 12 25.775 24.308 19.444 1.00 30.83 C ANISOU 103 CB ASN A 12 3599 3912 4203 -230 -97 29 C ATOM 104 CG ASN A 12 24.800 23.347 18.783 1.00 33.40 C ANISOU 104 CG ASN A 12 3968 4323 4398 -358 -189 -231 C ATOM 105 OD1 ASN A 12 23.800 22.976 19.397 1.00 37.19 O ANISOU 105 OD1 ASN A 12 4210 5050 4872 -188 119 -65 O ATOM 106 ND2 ASN A 12 25.091 22.957 17.553 1.00 32.00 N ANISOU 106 ND2 ASN A 12 3690 4097 4369 -459 -121 -130 N ATOM 107 N ASP A 13 24.020 26.934 20.195 1.00 30.64 N ANISOU 107 N ASP A 13 3081 4545 4017 -232 -46 -160 N ATOM 108 CA ASP A 13 22.695 27.524 20.418 1.00 32.66 C ANISOU 108 CA ASP A 13 3450 4452 4508 146 -50 81 C ATOM 109 C ASP A 13 22.450 28.655 19.429 1.00 32.94 C ANISOU 109 C ASP A 13 3463 4552 4502 3 1 165 C ATOM 110 O ASP A 13 21.305 28.972 19.089 1.00 34.10 O ANISOU 110 O ASP A 13 3342 4759 4855 111 47 -29 O ATOM 111 CB ASP A 13 22.562 28.006 21.855 1.00 36.35 C ANISOU 111 CB ASP A 13 4226 4952 4634 58 38 -78 C ATOM 112 CG ASP A 13 22.535 26.857 22.846 1.00 39.71 C ANISOU 112 CG ASP A 13 4840 5090 5158 110 20 113 C ATOM 113 OD1 ASP A 13 22.232 25.720 22.423 1.00 41.46 O ANISOU 113 OD1 ASP A 13 5111 5218 5426 6 66 -71 O ATOM 114 OD2 ASP A 13 22.822 27.106 24.038 1.00 41.80 O ANISOU 114 OD2 ASP A 13 5167 5513 5204 232 58 -93 O ATOM 115 N ARG A 14 23.524 29.261 18.935 1.00 29.38 N ANISOU 115 N ARG A 14 2932 4177 4055 349 -194 109 N ATOM 116 CA ARG A 14 23.430 30.355 17.986 1.00 28.27 C ANISOU 116 CA ARG A 14 2754 4185 3804 243 -22 27 C ATOM 117 C ARG A 14 23.739 29.898 16.565 1.00 26.04 C ANISOU 117 C ARG A 14 2232 3940 3721 192 -136 40 C ATOM 118 O ARG A 14 23.838 30.762 15.693 1.00 27.14 O ANISOU 118 O ARG A 14 2136 4341 3836 323 -323 232 O ATOM 119 CB ARG A 14 24.383 31.489 18.369 1.00 31.56 C ANISOU 119 CB ARG A 14 3646 4162 4182 6 -182 -18 C ATOM 120 CG ARG A 14 24.133 32.097 19.737 1.00 36.82 C ANISOU 120 CG ARG A 14 4693 4893 4405 183 123 -101 C ATOM 121 CD ARG A 14 25.185 33.141 20.083 1.00 42.49 C ANISOU 121 CD ARG A 14 5478 5274 5391 -270 -30 -140 C ATOM 122 NE ARG A 14 26.447 32.531 20.491 1.00 48.66 N ANISOU 122 NE ARG A 14 5973 6219 6298 204 27 12 N ATOM 123 CZ ARG A 14 27.399 33.189 21.144 1.00 51.71 C ANISOU 123 CZ ARG A 14 6446 6548 6652 -119 -108 -78 C ATOM 124 NH1 ARG A 14 27.202 34.464 21.450 1.00 53.49 N ANISOU 124 NH1 ARG A 14 6700 6675 6951 27 -35 -28 N ATOM 125 NH2 ARG A 14 28.527 32.590 21.494 1.00 53.46 N ANISOU 125 NH2 ARG A 14 6717 6738 6858 101 -23 -31 N ATOM 126 N ARG A 15 23.893 28.594 16.351 1.00 27.94 N ANISOU 126 N ARG A 15 2561 4029 4025 21 -265 -172 N ATOM 127 CA ARG A 15 24.225 28.118 15.005 1.00 30.45 C ANISOU 127 CA ARG A 15 3218 4367 3986 45 -130 -114 C ATOM 128 C ARG A 15 25.413 28.892 14.451 1.00 28.57 C ANISOU 128 C ARG A 15 2911 4269 3677 154 -464 0 C ATOM 129 O ARG A 15 25.451 29.360 13.314 1.00 27.21 O ANISOU 129 O ARG A 15 2290 4441 3606 298 -676 -36 O ATOM 130 CB ARG A 15 23.025 28.268 14.060 1.00 34.78 C ANISOU 130 CB ARG A 15 3862 5028 4324 255 -533 -34 C ATOM 131 CG ARG A 15 21.860 27.347 14.385 1.00 41.89 C ANISOU 131 CG ARG A 15 4970 5360 5587 -191 107 44 C ATOM 132 CD ARG A 15 20.775 27.448 13.315 1.00 47.81 C ANISOU 132 CD ARG A 15 5852 6314 6002 128 -336 -13 C ATOM 133 NE ARG A 15 19.626 26.610 13.628 1.00 53.16 N ANISOU 133 NE ARG A 15 6615 6701 6881 -187 105 124 N ATOM 134 CZ ARG A 15 18.497 26.525 12.939 1.00 55.71 C ANISOU 134 CZ ARG A 15 6861 7198 7106 -13 -123 26 C ATOM 135 NH1 ARG A 15 18.317 27.245 11.839 1.00 56.93 N ANISOU 135 NH1 ARG A 15 7122 7276 7231 -51 -20 107 N ATOM 136 NH2 ARG A 15 17.528 25.712 13.346 1.00 56.85 N ANISOU 136 NH2 ARG A 15 7103 7265 7232 -54 20 58 N ATOM 137 N GLU A 16 26.468 29.029 15.267 1.00 26.23 N ANISOU 137 N GLU A 16 2532 3779 3655 72 -246 -20 N ATOM 138 CA GLU A 16 27.654 29.754 14.864 1.00 21.65 C ANISOU 138 CA GLU A 16 2160 2944 3120 473 -421 -45 C ATOM 139 C GLU A 16 28.893 28.852 15.008 1.00 19.04 C ANISOU 139 C GLU A 16 1822 2512 2901 68 -492 27 C ATOM 140 O GLU A 16 28.913 27.973 15.868 1.00 21.28 O ANISOU 140 O GLU A 16 2140 2449 3498 267 -449 236 O ATOM 141 CB GLU A 16 27.947 30.962 15.757 1.00 24.29 C ANISOU 141 CB GLU A 16 2639 3264 3325 365 -269 -326 C ATOM 142 CG GLU A 16 27.332 32.292 15.388 1.00 26.71 C ANISOU 142 CG GLU A 16 3162 3150 3837 184 -146 -149 C ATOM 143 CD GLU A 16 27.579 33.291 16.517 1.00 28.72 C ANISOU 143 CD GLU A 16 3238 3713 3962 81 -399 -371 C ATOM 144 OE1 GLU A 16 28.685 33.325 17.100 1.00 24.76 O ANISOU 144 OE1 GLU A 16 2736 2806 3864 805 -34 -38 O ATOM 145 OE2 GLU A 16 26.645 34.050 16.824 1.00 31.94 O ANISOU 145 OE2 GLU A 16 3317 4208 4610 170 -123 -386 O ATOM 146 N GLY A 17 29.856 29.158 14.167 1.00 18.92 N ANISOU 146 N GLY A 17 1726 2552 2912 312 -445 -49 N ATOM 147 CA GLY A 17 31.155 28.471 14.295 1.00 19.02 C ANISOU 147 CA GLY A 17 1844 2378 3004 274 -764 239 C ATOM 148 C GLY A 17 32.015 29.392 15.161 1.00 17.43 C ANISOU 148 C GLY A 17 1724 1995 2902 244 -363 223 C ATOM 149 O GLY A 17 31.716 30.560 15.415 1.00 18.36 O ANISOU 149 O GLY A 17 1757 2028 3191 197 -754 72 O ATOM 150 N ALA A 18 33.099 28.792 15.654 1.00 15.96 N ANISOU 150 N ALA A 18 1646 1890 2528 -94 -543 414 N ATOM 151 CA ALA A 18 34.042 29.564 16.460 1.00 15.68 C ANISOU 151 CA ALA A 18 1792 1737 2430 -132 -389 311 C ATOM 152 C ALA A 18 35.110 30.166 15.552 1.00 14.31 C ANISOU 152 C ALA A 18 2018 1554 1864 126 -332 339 C ATOM 153 O ALA A 18 35.578 29.480 14.633 1.00 16.16 O ANISOU 153 O ALA A 18 2349 1445 2346 -18 -315 -66 O ATOM 154 CB ALA A 18 34.739 28.613 17.439 1.00 16.24 C ANISOU 154 CB ALA A 18 2071 1771 2328 -38 -460 246 C ATOM 155 N PHE A 19 35.511 31.399 15.822 1.00 14.25 N ANISOU 155 N PHE A 19 1786 1705 1922 -162 -113 375 N ATOM 156 CA PHE A 19 36.653 31.987 15.121 1.00 12.66 C ANISOU 156 CA PHE A 19 1345 1596 1868 30 -360 490 C ATOM 157 C PHE A 19 37.743 32.195 16.180 1.00 13.79 C ANISOU 157 C PHE A 19 1370 1668 2200 301 -411 -192 C ATOM 158 O PHE A 19 37.535 32.888 17.168 1.00 14.45 O ANISOU 158 O PHE A 19 1411 1962 2118 210 -210 -179 O ATOM 159 CB PHE A 19 36.351 33.295 14.392 1.00 13.72 C ANISOU 159 CB PHE A 19 1363 1534 2317 270 -496 425 C ATOM 160 CG PHE A 19 37.648 33.829 13.824 1.00 13.26 C ANISOU 160 CG PHE A 19 1476 1547 2015 282 -362 346 C ATOM 161 CD1 PHE A 19 38.304 33.104 12.854 1.00 13.81 C ANISOU 161 CD1 PHE A 19 1472 2090 1687 293 -221 520 C ATOM 162 CD2 PHE A 19 38.206 35.004 14.299 1.00 15.05 C ANISOU 162 CD2 PHE A 19 1734 1971 2013 -23 -344 135 C ATOM 163 CE1 PHE A 19 39.524 33.537 12.359 1.00 13.31 C ANISOU 163 CE1 PHE A 19 1355 1727 1974 194 -393 422 C ATOM 164 CE2 PHE A 19 39.413 35.445 13.798 1.00 14.44 C ANISOU 164 CE2 PHE A 19 1780 2011 1697 100 -283 229 C ATOM 165 CZ PHE A 19 40.062 34.718 12.818 1.00 14.15 C ANISOU 165 CZ PHE A 19 1574 1822 1981 187 -298 210 C ATOM 166 N VAL A 20 38.892 31.539 15.966 1.00 12.81 N ANISOU 166 N VAL A 20 1195 1709 1965 249 -423 -35 N ATOM 167 CA VAL A 20 39.963 31.534 16.956 1.00 12.92 C ANISOU 167 CA VAL A 20 1445 1811 1652 43 -371 87 C ATOM 168 C VAL A 20 41.281 32.006 16.372 1.00 11.37 C ANISOU 168 C VAL A 20 1174 1353 1794 206 -554 90 C ATOM 169 O VAL A 20 41.963 31.277 15.646 1.00 13.80 O ANISOU 169 O VAL A 20 1670 1840 1732 287 -319 21 O ATOM 170 CB VAL A 20 40.144 30.081 17.455 1.00 12.28 C ANISOU 170 CB VAL A 20 1223 1648 1794 -45 -360 -169 C ATOM 171 CG1 VAL A 20 41.215 29.990 18.539 1.00 12.85 C ANISOU 171 CG1 VAL A 20 1728 1439 1716 241 -569 -30 C ATOM 172 CG2 VAL A 20 38.819 29.522 17.934 1.00 14.64 C ANISOU 172 CG2 VAL A 20 1665 1929 1968 -150 197 -131 C ATOM 173 N PRO A 21 41.660 33.262 16.618 1.00 10.72 N ANISOU 173 N PRO A 21 1560 1349 1163 118 -269 83 N ATOM 174 CA PRO A 21 42.938 33.749 16.159 1.00 12.15 C ANISOU 174 CA PRO A 21 1211 1284 2121 206 -475 107 C ATOM 175 C PRO A 21 44.096 33.164 16.976 1.00 11.79 C ANISOU 175 C PRO A 21 1223 1672 1586 64 -382 183 C ATOM 176 O PRO A 21 43.922 32.834 18.145 1.00 12.34 O ANISOU 176 O PRO A 21 1569 1624 1494 279 -340 32 O ATOM 177 CB PRO A 21 42.884 35.247 16.420 1.00 13.95 C ANISOU 177 CB PRO A 21 1664 1374 2261 -23 79 -182 C ATOM 178 CG PRO A 21 41.873 35.408 17.490 1.00 15.60 C ANISOU 178 CG PRO A 21 1961 1517 2450 -9 289 -293 C ATOM 179 CD PRO A 21 40.924 34.252 17.445 1.00 13.69 C ANISOU 179 CD PRO A 21 1707 1241 2255 212 -116 -156 C ATOM 180 N PHE A 22 45.243 33.082 16.324 1.00 11.65 N ANISOU 180 N PHE A 22 1328 1444 1654 -35 -186 350 N ATOM 181 CA PHE A 22 46.482 32.690 16.954 1.00 11.96 C ANISOU 181 CA PHE A 22 1367 1660 1517 6 -196 120 C ATOM 182 C PHE A 22 47.458 33.863 16.875 1.00 12.08 C ANISOU 182 C PHE A 22 1845 1783 964 -227 -91 199 C ATOM 183 O PHE A 22 47.524 34.504 15.820 1.00 13.32 O ANISOU 183 O PHE A 22 1899 1724 1437 58 -317 667 O ATOM 184 CB PHE A 22 47.149 31.487 16.250 1.00 11.62 C ANISOU 184 CB PHE A 22 1466 1570 1379 -42 -291 84 C ATOM 185 CG PHE A 22 48.595 31.329 16.627 1.00 10.13 C ANISOU 185 CG PHE A 22 1391 1304 1154 -108 -154 69 C ATOM 186 CD1 PHE A 22 49.577 32.061 15.991 1.00 11.75 C ANISOU 186 CD1 PHE A 22 1319 1571 1577 -317 -11 -156 C ATOM 187 CD2 PHE A 22 48.971 30.467 17.651 1.00 11.11 C ANISOU 187 CD2 PHE A 22 1830 1240 1152 211 -71 -13 C ATOM 188 CE1 PHE A 22 50.907 31.947 16.364 1.00 11.14 C ANISOU 188 CE1 PHE A 22 1262 1564 1407 134 304 493 C ATOM 189 CE2 PHE A 22 50.305 30.359 18.014 1.00 10.69 C ANISOU 189 CE2 PHE A 22 1745 1305 1011 -73 -55 86 C ATOM 190 CZ PHE A 22 51.291 31.073 17.366 1.00 11.33 C ANISOU 190 CZ PHE A 22 1461 1418 1426 300 111 251 C ATOM 191 N VAL A 23 48.157 34.141 17.963 1.00 11.15 N ANISOU 191 N VAL A 23 1481 1336 1419 -97 -263 -146 N ATOM 192 CA VAL A 23 49.247 35.096 17.969 1.00 11.72 C ANISOU 192 CA VAL A 23 1827 1121 1504 -176 -94 42 C ATOM 193 C VAL A 23 50.349 34.506 18.864 1.00 11.40 C ANISOU 193 C VAL A 23 1537 1389 1406 -218 118 125 C ATOM 194 O VAL A 23 50.097 33.640 19.711 1.00 12.57 O ANISOU 194 O VAL A 23 1949 1413 1412 -131 29 240 O ATOM 195 CB VAL A 23 48.971 36.531 18.435 1.00 13.37 C ANISOU 195 CB VAL A 23 2055 1274 1749 107 -38 -8 C ATOM 196 CG1 VAL A 23 48.028 37.250 17.468 1.00 14.57 C ANISOU 196 CG1 VAL A 23 2069 1207 2261 288 -133 35 C ATOM 197 CG2 VAL A 23 48.366 36.579 19.831 1.00 12.28 C ANISOU 197 CG2 VAL A 23 2321 438 1905 573 208 286 C ATOM 198 N THR A 24 51.561 35.001 18.664 1.00 12.10 N ANISOU 198 N THR A 24 1508 1585 1503 -296 -134 494 N ATOM 199 CA THR A 24 52.701 34.678 19.509 1.00 12.19 C ANISOU 199 CA THR A 24 1413 1830 1388 -144 -87 46 C ATOM 200 C THR A 24 52.717 35.664 20.671 1.00 11.57 C ANISOU 200 C THR A 24 1630 1353 1414 -268 -23 249 C ATOM 201 O THR A 24 52.711 36.880 20.478 1.00 13.54 O ANISOU 201 O THR A 24 1754 1382 2008 -354 -70 371 O ATOM 202 CB THR A 24 54.025 34.757 18.724 1.00 12.74 C ANISOU 202 CB THR A 24 1787 1786 1268 -131 140 69 C ATOM 203 OG1 THR A 24 53.983 33.730 17.712 1.00 14.03 O ANISOU 203 OG1 THR A 24 1719 1869 1743 -595 247 -219 O ATOM 204 CG2 THR A 24 55.216 34.539 19.625 1.00 14.94 C ANISOU 204 CG2 THR A 24 1775 2028 1875 -221 -120 -38 C ATOM 205 N LEU A 25 52.672 35.137 21.896 1.00 11.83 N ANISOU 205 N LEU A 25 2145 1206 1144 -293 26 -35 N ATOM 206 CA LEU A 25 52.725 36.013 23.063 1.00 11.53 C ANISOU 206 CA LEU A 25 2020 1015 1345 -390 65 -84 C ATOM 207 C LEU A 25 54.006 36.844 23.062 1.00 13.35 C ANISOU 207 C LEU A 25 1851 1214 2008 -294 173 -8 C ATOM 208 O LEU A 25 55.110 36.329 22.858 1.00 14.25 O ANISOU 208 O LEU A 25 1951 1401 2061 -262 321 -154 O ATOM 209 CB LEU A 25 52.682 35.206 24.366 1.00 11.02 C ANISOU 209 CB LEU A 25 1684 1176 1325 -58 -215 -5 C ATOM 210 CG LEU A 25 51.301 34.619 24.686 1.00 11.99 C ANISOU 210 CG LEU A 25 1855 1148 1552 -108 77 19 C ATOM 211 CD1 LEU A 25 51.451 33.530 25.741 1.00 12.87 C ANISOU 211 CD1 LEU A 25 1455 1343 2091 -402 713 528 C ATOM 212 CD2 LEU A 25 50.331 35.683 25.167 1.00 14.26 C ANISOU 212 CD2 LEU A 25 1985 1566 1869 335 -7 238 C ATOM 213 N GLY A 26 53.827 38.149 23.293 1.00 12.83 N ANISOU 213 N GLY A 26 1677 1307 1889 -113 130 -199 N ATOM 214 CA GLY A 26 54.994 39.027 23.344 1.00 13.70 C ANISOU 214 CA GLY A 26 1675 1493 2037 -210 -251 -16 C ATOM 215 C GLY A 26 55.455 39.577 22.013 1.00 13.48 C ANISOU 215 C GLY A 26 1597 1375 2149 -148 -364 194 C ATOM 216 O GLY A 26 56.445 40.310 21.970 1.00 14.37 O ANISOU 216 O GLY A 26 2004 1275 2181 -398 -322 14 O ATOM 217 N ASP A 27 54.738 39.286 20.931 1.00 13.61 N ANISOU 217 N ASP A 27 2401 1154 1616 -480 -249 411 N ATOM 218 CA ASP A 27 55.073 39.865 19.624 1.00 12.83 C ANISOU 218 CA ASP A 27 2151 1113 1611 -177 -67 338 C ATOM 219 C ASP A 27 54.166 41.057 19.346 1.00 14.89 C ANISOU 219 C ASP A 27 1798 1393 2469 -132 19 450 C ATOM 220 O ASP A 27 52.939 40.859 19.300 1.00 15.12 O ANISOU 220 O ASP A 27 1783 1693 2270 -169 -135 303 O ATOM 221 CB ASP A 27 54.803 38.778 18.555 1.00 12.59 C ANISOU 221 CB ASP A 27 1913 1303 1565 -448 107 279 C ATOM 222 CG ASP A 27 54.899 39.346 17.146 1.00 14.85 C ANISOU 222 CG ASP A 27 2312 1878 1452 -329 81 246 C ATOM 223 OD1 ASP A 27 55.634 40.339 17.000 1.00 15.72 O ANISOU 223 OD1 ASP A 27 2297 2076 1601 -462 95 230 O ATOM 224 OD2 ASP A 27 54.268 38.826 16.207 1.00 13.56 O ANISOU 224 OD2 ASP A 27 2103 1812 1235 -400 192 468 O ATOM 225 N PRO A 28 54.690 42.260 19.148 1.00 15.47 N ANISOU 225 N PRO A 28 2046 1444 2387 -330 -102 250 N ATOM 226 CA PRO A 28 56.097 42.559 19.084 1.00 14.91 C ANISOU 226 CA PRO A 28 2020 1288 2357 -113 -75 199 C ATOM 227 C PRO A 28 56.755 43.027 20.361 1.00 15.41 C ANISOU 227 C PRO A 28 2015 1572 2269 -181 47 141 C ATOM 228 O PRO A 28 57.943 43.375 20.398 1.00 17.81 O ANISOU 228 O PRO A 28 2246 1620 2902 -579 -23 -85 O ATOM 229 CB PRO A 28 56.086 43.714 18.055 1.00 16.23 C ANISOU 229 CB PRO A 28 2059 1624 2482 -283 236 432 C ATOM 230 CG PRO A 28 54.838 44.469 18.352 1.00 15.54 C ANISOU 230 CG PRO A 28 2045 1317 2544 -403 91 154 C ATOM 231 CD PRO A 28 53.834 43.433 18.785 1.00 15.19 C ANISOU 231 CD PRO A 28 1926 1372 2473 -325 194 161 C ATOM 232 N GLY A 29 55.987 43.087 21.435 1.00 13.99 N ANISOU 232 N GLY A 29 1881 1259 2176 -222 -61 -63 N ATOM 233 CA GLY A 29 56.466 43.430 22.774 1.00 14.82 C ANISOU 233 CA GLY A 29 2216 1424 1991 -301 56 60 C ATOM 234 C GLY A 29 55.348 43.015 23.739 1.00 13.61 C ANISOU 234 C GLY A 29 1695 1393 2084 -188 -121 -59 C ATOM 235 O GLY A 29 54.224 42.766 23.271 1.00 14.02 O ANISOU 235 O GLY A 29 1815 1141 2370 -50 -474 79 O ATOM 236 N ILE A 30 55.643 42.968 25.029 1.00 14.64 N ANISOU 236 N ILE A 30 2200 1333 2029 -88 -8 177 N ATOM 237 CA ILE A 30 54.612 42.534 25.980 1.00 15.60 C ANISOU 237 CA ILE A 30 1986 1728 2213 -77 25 47 C ATOM 238 C ILE A 30 53.410 43.465 25.989 1.00 17.23 C ANISOU 238 C ILE A 30 2076 1949 2521 66 37 -260 C ATOM 239 O ILE A 30 52.276 43.019 25.852 1.00 15.82 O ANISOU 239 O ILE A 30 2411 1495 2103 -238 -71 -221 O ATOM 240 CB ILE A 30 55.193 42.386 27.393 1.00 15.64 C ANISOU 240 CB ILE A 30 2020 1704 2219 -89 -2 142 C ATOM 241 CG1AILE A 30 56.319 41.352 27.428 0.50 17.91 C ANISOU 241 CG1AILE A 30 2102 2066 2638 72 65 8 C ATOM 242 CG2AILE A 30 54.095 42.019 28.386 0.50 16.98 C ANISOU 242 CG2AILE A 30 2150 2025 2276 -65 87 151 C ATOM 243 CD1AILE A 30 55.862 39.938 27.159 0.50 18.58 C ANISOU 243 CD1AILE A 30 2315 2081 2665 57 178 -54 C ATOM 244 CG1BILE A 30 56.066 41.129 27.463 0.50 14.94 C ANISOU 244 CG1BILE A 30 1734 1829 2115 -128 -24 -28 C ATOM 245 CG2BILE A 30 54.090 42.344 28.441 0.50 15.63 C ANISOU 245 CG2BILE A 30 2087 1704 2147 -193 -30 153 C ATOM 246 CD1BILE A 30 56.923 41.023 28.701 0.50 14.35 C ANISOU 246 CD1BILE A 30 1818 1955 1677 39 222 -85 C ATOM 247 N GLU A 31 53.645 44.767 26.119 1.00 19.01 N ANISOU 247 N GLU A 31 2524 1878 2821 -50 141 156 N ATOM 248 CA GLU A 31 52.546 45.728 26.165 1.00 19.96 C ANISOU 248 CA GLU A 31 2362 2484 2738 113 -153 -58 C ATOM 249 C GLU A 31 51.709 45.718 24.892 1.00 16.77 C ANISOU 249 C GLU A 31 2166 1692 2515 -113 52 -166 C ATOM 250 O GLU A 31 50.482 45.675 24.981 1.00 17.03 O ANISOU 250 O GLU A 31 2207 1757 2506 -4 384 -205 O ATOM 251 CB GLU A 31 53.087 47.129 26.446 1.00 23.05 C ANISOU 251 CB GLU A 31 2879 2666 3214 -190 -150 -58 C ATOM 252 CG AGLU A 31 53.715 47.253 27.825 0.50 24.71 C ANISOU 252 CG AGLU A 31 3023 3182 3185 21 -170 5 C ATOM 253 CD AGLU A 31 53.806 48.670 28.342 0.50 27.15 C ANISOU 253 CD AGLU A 31 3549 3258 3509 10 -102 -40 C ATOM 254 OE1AGLU A 31 53.443 49.624 27.619 0.50 27.32 O ANISOU 254 OE1AGLU A 31 3702 3361 3319 -21 -52 9 O ATOM 255 OE2AGLU A 31 54.242 48.851 29.502 0.50 29.60 O ANISOU 255 OE2AGLU A 31 3978 3738 3532 56 -138 21 O ATOM 256 CG BGLU A 31 52.067 48.224 26.680 0.50 26.35 C ANISOU 256 CG BGLU A 31 3264 3162 3586 147 -10 -150 C ATOM 257 CD BGLU A 31 52.710 49.598 26.755 0.50 28.43 C ANISOU 257 CD BGLU A 31 3671 3307 3824 -55 -38 -51 C ATOM 258 OE1BGLU A 31 53.951 49.692 26.643 0.50 29.91 O ANISOU 258 OE1BGLU A 31 3861 3540 3964 -185 182 -48 O ATOM 259 OE2BGLU A 31 51.979 50.591 26.927 0.50 29.73 O ANISOU 259 OE2BGLU A 31 3905 3419 3972 25 -29 -69 O ATOM 260 N GLN A 32 52.354 45.743 23.728 1.00 16.58 N ANISOU 260 N GLN A 32 2384 1572 2342 16 -51 -64 N ATOM 261 CA GLN A 32 51.593 45.759 22.481 1.00 15.41 C ANISOU 261 CA GLN A 32 2141 1485 2231 -356 87 -268 C ATOM 262 C GLN A 32 50.859 44.435 22.291 1.00 14.55 C ANISOU 262 C GLN A 32 2043 1247 2239 -236 42 87 C ATOM 263 O GLN A 32 49.745 44.427 21.775 1.00 14.99 O ANISOU 263 O GLN A 32 2211 1105 2381 -148 -147 537 O ATOM 264 CB GLN A 32 52.462 46.096 21.279 1.00 17.57 C ANISOU 264 CB GLN A 32 2732 1828 2118 -443 156 -91 C ATOM 265 CG GLN A 32 51.718 46.221 19.960 1.00 20.73 C ANISOU 265 CG GLN A 32 2964 2304 2609 -40 -196 156 C ATOM 266 CD GLN A 32 50.755 47.371 19.829 1.00 21.74 C ANISOU 266 CD GLN A 32 3303 2111 2848 -4 -72 214 C ATOM 267 OE1 GLN A 32 50.636 48.256 20.681 1.00 24.72 O ANISOU 267 OE1 GLN A 32 4053 2382 2959 129 68 103 O ATOM 268 NE2 GLN A 32 50.047 47.396 18.705 1.00 22.08 N ANISOU 268 NE2 GLN A 32 3254 2001 3134 -188 -247 208 N ATOM 269 N SER A 33 51.476 43.341 22.704 1.00 14.61 N ANISOU 269 N SER A 33 2133 1105 2312 -298 -105 -29 N ATOM 270 CA SER A 33 50.840 42.022 22.580 1.00 13.59 C ANISOU 270 CA SER A 33 1841 1143 2179 -330 273 -62 C ATOM 271 C SER A 33 49.585 41.959 23.449 1.00 11.97 C ANISOU 271 C SER A 33 1772 790 1986 -49 211 -193 C ATOM 272 O SER A 33 48.529 41.480 23.015 1.00 13.99 O ANISOU 272 O SER A 33 1851 1193 2271 -117 -75 237 O ATOM 273 CB SER A 33 51.835 40.919 22.928 1.00 14.26 C ANISOU 273 CB SER A 33 1851 1169 2400 -327 252 -26 C ATOM 274 OG SER A 33 51.234 39.643 22.769 1.00 13.17 O ANISOU 274 OG SER A 33 1874 852 2277 -36 53 91 O ATOM 275 N LEU A 34 49.630 42.516 24.659 1.00 13.66 N ANISOU 275 N LEU A 34 2086 1245 1860 -83 436 -172 N ATOM 276 CA LEU A 34 48.427 42.533 25.510 1.00 12.57 C ANISOU 276 CA LEU A 34 1671 1439 1667 -18 58 -52 C ATOM 277 C LEU A 34 47.334 43.370 24.843 1.00 13.91 C ANISOU 277 C LEU A 34 1584 1003 2696 150 176 -84 C ATOM 278 O LEU A 34 46.157 43.012 24.862 1.00 14.04 O ANISOU 278 O LEU A 34 1789 970 2576 -142 707 194 O ATOM 279 CB LEU A 34 48.745 43.048 26.910 1.00 15.02 C ANISOU 279 CB LEU A 34 2019 1808 1878 -33 -195 -256 C ATOM 280 CG LEU A 34 49.577 42.140 27.816 1.00 16.66 C ANISOU 280 CG LEU A 34 2717 1628 1986 -159 -166 86 C ATOM 281 CD1 LEU A 34 50.104 42.881 29.036 1.00 16.21 C ANISOU 281 CD1 LEU A 34 2473 1427 2258 -372 128 -187 C ATOM 282 CD2 LEU A 34 48.763 40.926 28.251 1.00 16.23 C ANISOU 282 CD2 LEU A 34 2523 1503 2140 -43 65 -46 C ATOM 283 N LYS A 35 47.713 44.476 24.182 1.00 15.52 N ANISOU 283 N LYS A 35 1942 1214 2742 -113 151 1 N ATOM 284 CA LYS A 35 46.743 45.310 23.476 1.00 17.02 C ANISOU 284 CA LYS A 35 2444 1221 2803 -60 -45 53 C ATOM 285 C LYS A 35 46.160 44.585 22.265 1.00 15.82 C ANISOU 285 C LYS A 35 2043 1478 2491 -80 153 138 C ATOM 286 O LYS A 35 44.963 44.674 21.984 1.00 16.62 O ANISOU 286 O LYS A 35 2239 1295 2780 -13 -238 252 O ATOM 287 CB LYS A 35 47.355 46.637 23.021 1.00 17.50 C ANISOU 287 CB LYS A 35 2288 1590 2769 -240 261 132 C ATOM 288 CG LYS A 35 47.713 47.568 24.166 1.00 20.24 C ANISOU 288 CG LYS A 35 2859 2022 2811 -183 202 -90 C ATOM 289 CD LYS A 35 48.438 48.804 23.637 1.00 22.87 C ANISOU 289 CD LYS A 35 2875 2337 3477 -330 332 93 C ATOM 290 CE LYS A 35 48.492 49.887 24.700 1.00 27.39 C ANISOU 290 CE LYS A 35 3810 3148 3447 -56 211 -220 C ATOM 291 NZ LYS A 35 49.406 49.557 25.820 1.00 32.67 N ANISOU 291 NZ LYS A 35 4052 4051 4308 79 -65 102 N ATOM 292 N ILE A 36 47.024 43.908 21.507 1.00 15.17 N ANISOU 292 N ILE A 36 2297 1039 2426 14 23 87 N ATOM 293 CA ILE A 36 46.588 43.115 20.359 1.00 14.37 C ANISOU 293 CA ILE A 36 1811 1331 2319 -42 12 171 C ATOM 294 C ILE A 36 45.549 42.090 20.791 1.00 14.11 C ANISOU 294 C ILE A 36 1816 1589 1955 -126 -75 250 C ATOM 295 O ILE A 36 44.486 41.938 20.198 1.00 15.27 O ANISOU 295 O ILE A 36 2016 1588 2198 105 -409 524 O ATOM 296 CB ILE A 36 47.808 42.390 19.751 1.00 13.85 C ANISOU 296 CB ILE A 36 1956 1148 2158 -65 15 50 C ATOM 297 CG1 ILE A 36 48.667 43.392 18.984 1.00 14.52 C ANISOU 297 CG1 ILE A 36 1722 2035 1760 -63 96 251 C ATOM 298 CG2 ILE A 36 47.381 41.213 18.886 1.00 14.25 C ANISOU 298 CG2 ILE A 36 2239 1419 1758 -248 -180 143 C ATOM 299 CD1 ILE A 36 50.053 42.913 18.646 1.00 14.13 C ANISOU 299 CD1 ILE A 36 1533 1916 1920 -169 -186 17 C ATOM 300 N ILE A 37 45.843 41.397 21.896 1.00 14.26 N ANISOU 300 N ILE A 37 1896 1496 2027 -1 41 318 N ATOM 301 CA ILE A 37 44.945 40.344 22.380 1.00 13.54 C ANISOU 301 CA ILE A 37 1621 1367 2158 19 -65 128 C ATOM 302 C ILE A 37 43.602 40.907 22.814 1.00 12.55 C ANISOU 302 C ILE A 37 1744 1043 1982 48 -44 92 C ATOM 303 O ILE A 37 42.554 40.363 22.463 1.00 14.61 O ANISOU 303 O ILE A 37 1606 1536 2407 -12 49 77 O ATOM 304 CB ILE A 37 45.642 39.500 23.454 1.00 12.77 C ANISOU 304 CB ILE A 37 1654 1455 1744 73 89 58 C ATOM 305 CG1 ILE A 37 46.748 38.699 22.739 1.00 12.46 C ANISOU 305 CG1 ILE A 37 1939 1363 1434 385 42 305 C ATOM 306 CG2 ILE A 37 44.718 38.569 24.214 1.00 15.17 C ANISOU 306 CG2 ILE A 37 2245 1562 1958 -197 258 59 C ATOM 307 CD1 ILE A 37 47.748 38.052 23.663 1.00 13.42 C ANISOU 307 CD1 ILE A 37 2141 1407 1552 343 132 739 C ATOM 308 N ASP A 38 43.629 42.043 23.515 1.00 14.65 N ANISOU 308 N ASP A 38 2308 1159 2100 261 192 -45 N ATOM 309 CA ASP A 38 42.351 42.649 23.900 1.00 14.55 C ANISOU 309 CA ASP A 38 1992 1370 2167 -48 100 -316 C ATOM 310 C ASP A 38 41.555 43.068 22.664 1.00 13.76 C ANISOU 310 C ASP A 38 1978 980 2271 -111 118 -138 C ATOM 311 O ASP A 38 40.336 42.935 22.665 1.00 16.07 O ANISOU 311 O ASP A 38 1973 1236 2899 159 -264 -130 O ATOM 312 CB ASP A 38 42.564 43.836 24.832 1.00 15.46 C ANISOU 312 CB ASP A 38 2374 1119 2381 -26 158 -261 C ATOM 313 CG ASP A 38 42.928 43.428 26.239 1.00 16.80 C ANISOU 313 CG ASP A 38 2464 1512 2408 34 311 -22 C ATOM 314 OD1 ASP A 38 42.774 42.235 26.608 1.00 17.24 O ANISOU 314 OD1 ASP A 38 2519 1540 2490 430 599 212 O ATOM 315 OD2 ASP A 38 43.378 44.332 26.977 1.00 18.07 O ANISOU 315 OD2 ASP A 38 3026 1268 2572 101 211 -3 O ATOM 316 N THR A 39 42.241 43.537 21.625 1.00 15.33 N ANISOU 316 N THR A 39 2345 1476 2002 -96 -9 8 N ATOM 317 CA THR A 39 41.592 43.923 20.383 1.00 15.28 C ANISOU 317 CA THR A 39 2351 1349 2105 -75 -77 43 C ATOM 318 C THR A 39 40.997 42.708 19.676 1.00 14.66 C ANISOU 318 C THR A 39 1914 1242 2415 184 -228 -13 C ATOM 319 O THR A 39 39.862 42.756 19.185 1.00 16.15 O ANISOU 319 O THR A 39 2033 1604 2501 91 -372 328 O ATOM 320 CB THR A 39 42.589 44.634 19.444 1.00 15.28 C ANISOU 320 CB THR A 39 2362 1276 2168 47 -62 144 C ATOM 321 OG1 THR A 39 43.017 45.838 20.094 1.00 17.70 O ANISOU 321 OG1 THR A 39 2984 1235 2505 -497 42 353 O ATOM 322 CG2 THR A 39 41.923 44.970 18.130 1.00 17.74 C ANISOU 322 CG2 THR A 39 2453 2082 2207 -20 -238 128 C ATOM 323 N LEU A 40 41.746 41.590 19.674 1.00 14.58 N ANISOU 323 N LEU A 40 2157 1177 2205 232 -84 -23 N ATOM 324 CA LEU A 40 41.190 40.391 19.024 1.00 14.43 C ANISOU 324 CA LEU A 40 1975 1257 2251 127 -223 120 C ATOM 325 C LEU A 40 39.883 40.018 19.720 1.00 14.00 C ANISOU 325 C LEU A 40 1791 1366 2161 284 -247 -208 C ATOM 326 O LEU A 40 38.920 39.631 19.075 1.00 16.06 O ANISOU 326 O LEU A 40 1762 1352 2990 196 -475 -140 O ATOM 327 CB LEU A 40 42.166 39.225 19.141 1.00 15.42 C ANISOU 327 CB LEU A 40 1876 1769 2217 468 106 -98 C ATOM 328 CG LEU A 40 43.556 39.379 18.538 1.00 16.56 C ANISOU 328 CG LEU A 40 1889 1903 2501 23 -32 314 C ATOM 329 CD1 LEU A 40 44.417 38.143 18.800 1.00 17.97 C ANISOU 329 CD1 LEU A 40 1572 2451 2803 418 98 115 C ATOM 330 CD2 LEU A 40 43.476 39.699 17.059 1.00 18.67 C ANISOU 330 CD2 LEU A 40 1912 2820 2363 -32 -197 42 C ATOM 331 N ILE A 41 39.913 40.050 21.053 1.00 14.09 N ANISOU 331 N ILE A 41 1869 1374 2110 329 134 206 N ATOM 332 CA ILE A 41 38.715 39.677 21.816 1.00 15.11 C ANISOU 332 CA ILE A 41 1780 1716 2243 352 168 57 C ATOM 333 C ILE A 41 37.575 40.659 21.541 1.00 16.12 C ANISOU 333 C ILE A 41 1595 1847 2682 290 -83 -64 C ATOM 334 O ILE A 41 36.438 40.265 21.267 1.00 16.74 O ANISOU 334 O ILE A 41 1820 2021 2518 128 -301 37 O ATOM 335 CB ILE A 41 39.051 39.605 23.308 1.00 15.66 C ANISOU 335 CB ILE A 41 1834 1883 2234 282 190 78 C ATOM 336 CG1 ILE A 41 40.033 38.451 23.547 1.00 15.83 C ANISOU 336 CG1 ILE A 41 2116 1810 2088 291 10 176 C ATOM 337 CG2 ILE A 41 37.804 39.414 24.165 1.00 16.01 C ANISOU 337 CG2 ILE A 41 1909 1649 2524 -69 274 208 C ATOM 338 CD1 ILE A 41 40.582 38.448 24.963 1.00 15.46 C ANISOU 338 CD1 ILE A 41 2151 1786 1935 581 156 36 C ATOM 339 N ASP A 42 37.877 41.956 21.637 1.00 17.12 N ANISOU 339 N ASP A 42 1699 1780 3027 488 80 -89 N ATOM 340 CA ASP A 42 36.826 42.953 21.412 1.00 18.18 C ANISOU 340 CA ASP A 42 1954 1711 3243 481 -231 -29 C ATOM 341 C ASP A 42 36.238 42.861 20.015 1.00 18.88 C ANISOU 341 C ASP A 42 2204 1988 2983 234 56 -6 C ATOM 342 O ASP A 42 35.060 43.184 19.807 1.00 21.96 O ANISOU 342 O ASP A 42 2413 2006 3923 583 -120 -12 O ATOM 343 CB ASP A 42 37.356 44.362 21.705 1.00 19.68 C ANISOU 343 CB ASP A 42 2492 1748 3240 287 4 -11 C ATOM 344 CG ASP A 42 36.184 45.333 21.845 1.00 21.55 C ANISOU 344 CG ASP A 42 2746 2210 3233 600 17 -51 C ATOM 345 OD1 ASP A 42 35.408 45.169 22.806 1.00 22.70 O ANISOU 345 OD1 ASP A 42 2769 2210 3647 684 166 171 O ATOM 346 OD2 ASP A 42 36.047 46.242 20.999 1.00 23.86 O ANISOU 346 OD2 ASP A 42 3548 2375 3143 418 -48 -35 O ATOM 347 N ALA A 43 37.015 42.430 19.031 1.00 16.81 N ANISOU 347 N ALA A 43 2144 1521 2724 361 -216 19 N ATOM 348 CA ALA A 43 36.593 42.333 17.655 1.00 16.81 C ANISOU 348 CA ALA A 43 2229 1597 2563 143 -11 191 C ATOM 349 C ALA A 43 35.781 41.072 17.370 1.00 17.87 C ANISOU 349 C ALA A 43 2224 1730 2834 67 -248 253 C ATOM 350 O ALA A 43 35.285 40.932 16.245 1.00 20.11 O ANISOU 350 O ALA A 43 2876 2040 2726 64 -188 148 O ATOM 351 CB ALA A 43 37.795 42.417 16.728 1.00 19.27 C ANISOU 351 CB ALA A 43 2227 2488 2607 185 10 119 C ATOM 352 N GLY A 44 35.718 40.159 18.339 1.00 16.67 N ANISOU 352 N GLY A 44 1956 1284 3092 641 -505 273 N ATOM 353 CA GLY A 44 34.897 38.974 18.133 1.00 18.34 C ANISOU 353 CA GLY A 44 1936 1782 3249 360 -477 0 C ATOM 354 C GLY A 44 35.540 37.619 18.286 1.00 16.90 C ANISOU 354 C GLY A 44 1939 1579 2905 184 -379 -52 C ATOM 355 O GLY A 44 34.845 36.628 18.039 1.00 17.84 O ANISOU 355 O GLY A 44 1852 1524 3402 279 -769 139 O ATOM 356 N ALA A 45 36.804 37.523 18.681 1.00 16.37 N ANISOU 356 N ALA A 45 1928 1785 2506 338 -249 -236 N ATOM 357 CA ALA A 45 37.398 36.195 18.836 1.00 15.38 C ANISOU 357 CA ALA A 45 1790 1601 2451 51 -57 -35 C ATOM 358 C ALA A 45 36.603 35.376 19.851 1.00 13.44 C ANISOU 358 C ALA A 45 1815 1274 2018 78 -126 -312 C ATOM 359 O ALA A 45 36.327 35.891 20.940 1.00 16.07 O ANISOU 359 O ALA A 45 2220 2033 1854 273 -47 -210 O ATOM 360 CB ALA A 45 38.834 36.340 19.302 1.00 16.40 C ANISOU 360 CB ALA A 45 1941 1648 2644 -127 -228 -256 C ATOM 361 N ASP A 46 36.321 34.118 19.527 1.00 12.15 N ANISOU 361 N ASP A 46 1413 1072 2132 475 -47 -271 N ATOM 362 CA ASP A 46 35.606 33.262 20.460 1.00 13.91 C ANISOU 362 CA ASP A 46 1618 1457 2211 306 -182 -77 C ATOM 363 C ASP A 46 36.528 32.579 21.459 1.00 14.00 C ANISOU 363 C ASP A 46 1436 1885 1999 257 -80 -13 C ATOM 364 O ASP A 46 36.114 32.154 22.540 1.00 15.15 O ANISOU 364 O ASP A 46 1788 1827 2140 164 -51 40 O ATOM 365 CB ASP A 46 34.862 32.190 19.652 1.00 14.64 C ANISOU 365 CB ASP A 46 1294 1737 2533 175 -377 -56 C ATOM 366 CG ASP A 46 33.702 32.797 18.870 1.00 16.94 C ANISOU 366 CG ASP A 46 1619 2275 2543 479 -386 73 C ATOM 367 OD1 ASP A 46 32.841 33.452 19.500 1.00 18.00 O ANISOU 367 OD1 ASP A 46 1655 2212 2973 409 -281 -11 O ATOM 368 OD2 ASP A 46 33.687 32.609 17.637 1.00 15.57 O ANISOU 368 OD2 ASP A 46 1183 2165 2568 353 -306 24 O ATOM 369 N ALA A 47 37.779 32.392 21.045 1.00 14.10 N ANISOU 369 N ALA A 47 1396 2005 1957 3 -16 161 N ATOM 370 CA ALA A 47 38.786 31.715 21.853 1.00 12.85 C ANISOU 370 CA ALA A 47 1536 1641 1706 -32 -79 -153 C ATOM 371 C ALA A 47 40.136 32.215 21.328 1.00 11.99 C ANISOU 371 C ALA A 47 1403 1718 1436 121 -129 -97 C ATOM 372 O ALA A 47 40.197 32.870 20.277 1.00 13.91 O ANISOU 372 O ALA A 47 1555 1960 1770 197 -109 172 O ATOM 373 CB ALA A 47 38.666 30.203 21.727 1.00 13.81 C ANISOU 373 CB ALA A 47 2026 1597 1622 158 37 0 C ATOM 374 N LEU A 48 41.182 31.937 22.096 1.00 12.05 N ANISOU 374 N LEU A 48 1292 1596 1691 307 -81 -144 N ATOM 375 CA LEU A 48 42.519 32.348 21.709 1.00 12.01 C ANISOU 375 CA LEU A 48 1457 1650 1458 -41 -269 -113 C ATOM 376 C LEU A 48 43.421 31.126 21.609 1.00 12.03 C ANISOU 376 C LEU A 48 1579 1544 1447 -60 75 180 C ATOM 377 O LEU A 48 43.290 30.186 22.406 1.00 12.35 O ANISOU 377 O LEU A 48 1776 1326 1593 108 -160 231 O ATOM 378 CB LEU A 48 43.155 33.290 22.737 1.00 13.11 C ANISOU 378 CB LEU A 48 1895 1101 1984 55 -16 -432 C ATOM 379 CG LEU A 48 42.373 34.586 22.999 1.00 15.11 C ANISOU 379 CG LEU A 48 2106 1342 2294 302 205 -361 C ATOM 380 CD1 LEU A 48 43.009 35.342 24.155 1.00 15.92 C ANISOU 380 CD1 LEU A 48 2434 1640 1974 186 187 -181 C ATOM 381 CD2 LEU A 48 42.281 35.410 21.727 1.00 19.54 C ANISOU 381 CD2 LEU A 48 2770 1846 2810 254 -154 89 C ATOM 382 N GLU A 49 44.343 31.153 20.669 1.00 11.76 N ANISOU 382 N GLU A 49 1464 1712 1291 -67 -58 96 N ATOM 383 CA GLU A 49 45.410 30.174 20.578 1.00 11.34 C ANISOU 383 CA GLU A 49 1645 1477 1188 -41 -130 74 C ATOM 384 C GLU A 49 46.672 31.049 20.686 1.00 11.50 C ANISOU 384 C GLU A 49 1573 1277 1520 106 -150 62 C ATOM 385 O GLU A 49 46.841 31.999 19.931 1.00 12.93 O ANISOU 385 O GLU A 49 1925 1533 1454 126 -89 223 O ATOM 386 CB GLU A 49 45.430 29.388 19.282 1.00 13.28 C ANISOU 386 CB GLU A 49 1880 1865 1300 2 84 -159 C ATOM 387 CG GLU A 49 46.238 28.121 19.344 1.00 16.34 C ANISOU 387 CG GLU A 49 2469 1794 1946 97 527 50 C ATOM 388 CD GLU A 49 45.716 27.093 20.340 1.00 17.34 C ANISOU 388 CD GLU A 49 2681 1728 2181 146 381 238 C ATOM 389 OE1 GLU A 49 44.498 27.000 20.578 1.00 16.79 O ANISOU 389 OE1 GLU A 49 2684 810 2886 260 439 -243 O ATOM 390 OE2 GLU A 49 46.582 26.340 20.826 1.00 18.35 O ANISOU 390 OE2 GLU A 49 3161 2287 1525 431 138 40 O ATOM 391 N LEU A 50 47.553 30.722 21.617 1.00 10.67 N ANISOU 391 N LEU A 50 1467 1166 1423 153 -84 47 N ATOM 392 CA LEU A 50 48.663 31.590 21.943 1.00 10.02 C ANISOU 392 CA LEU A 50 1504 801 1503 94 154 217 C ATOM 393 C LEU A 50 49.980 30.840 21.987 1.00 10.70 C ANISOU 393 C LEU A 50 1390 1296 1380 164 -18 439 C ATOM 394 O LEU A 50 50.088 29.825 22.668 1.00 11.76 O ANISOU 394 O LEU A 50 1974 1351 1144 -10 163 516 O ATOM 395 CB LEU A 50 48.440 32.302 23.299 1.00 12.09 C ANISOU 395 CB LEU A 50 1879 1306 1409 60 167 179 C ATOM 396 CG LEU A 50 47.145 33.121 23.364 1.00 11.89 C ANISOU 396 CG LEU A 50 2022 1257 1240 118 302 12 C ATOM 397 CD1 LEU A 50 46.862 33.629 24.772 1.00 13.48 C ANISOU 397 CD1 LEU A 50 2043 1643 1435 404 379 -205 C ATOM 398 CD2 LEU A 50 47.239 34.288 22.376 1.00 12.99 C ANISOU 398 CD2 LEU A 50 2150 1357 1428 139 261 179 C ATOM 399 N GLY A 51 50.969 31.303 21.226 1.00 12.37 N ANISOU 399 N GLY A 51 1480 1458 1762 238 330 331 N ATOM 400 CA GLY A 51 52.262 30.627 21.205 1.00 11.14 C ANISOU 400 CA GLY A 51 1123 1694 1417 -10 100 417 C ATOM 401 C GLY A 51 53.241 31.255 22.177 1.00 12.49 C ANISOU 401 C GLY A 51 1613 1375 1758 204 -99 76 C ATOM 402 O GLY A 51 53.193 32.420 22.516 1.00 14.21 O ANISOU 402 O GLY A 51 2160 1411 1829 162 -260 -66 O ATOM 403 N VAL A 52 54.095 30.398 22.729 1.00 12.84 N ANISOU 403 N VAL A 52 1550 1520 1810 109 -558 -22 N ATOM 404 CA VAL A 52 55.171 30.840 23.610 1.00 11.51 C ANISOU 404 CA VAL A 52 1233 1469 1672 -65 -177 -157 C ATOM 405 C VAL A 52 56.446 30.834 22.789 1.00 11.95 C ANISOU 405 C VAL A 52 1841 1038 1661 -125 306 118 C ATOM 406 O VAL A 52 56.759 29.793 22.202 1.00 13.23 O ANISOU 406 O VAL A 52 1975 1267 1785 41 -144 -191 O ATOM 407 CB VAL A 52 55.292 29.926 24.835 1.00 11.79 C ANISOU 407 CB VAL A 52 1530 1379 1571 -243 -241 -246 C ATOM 408 CG1 VAL A 52 56.555 30.277 25.622 1.00 13.00 C ANISOU 408 CG1 VAL A 52 1337 2008 1592 -141 -201 -227 C ATOM 409 CG2 VAL A 52 54.090 30.089 25.749 1.00 12.41 C ANISOU 409 CG2 VAL A 52 1770 1339 1608 -139 -86 -393 C ATOM 410 N PRO A 53 57.152 31.950 22.664 1.00 11.79 N ANISOU 410 N PRO A 53 1358 1107 2015 -72 200 -129 N ATOM 411 CA PRO A 53 58.341 32.008 21.833 1.00 11.85 C ANISOU 411 CA PRO A 53 1676 1294 1533 -146 237 27 C ATOM 412 C PRO A 53 59.308 30.884 22.140 1.00 12.82 C ANISOU 412 C PRO A 53 1675 1572 1623 -22 164 -38 C ATOM 413 O PRO A 53 59.674 30.683 23.303 1.00 12.59 O ANISOU 413 O PRO A 53 1171 1912 1700 81 -56 -217 O ATOM 414 CB PRO A 53 58.891 33.398 22.091 1.00 13.83 C ANISOU 414 CB PRO A 53 2061 1256 1937 -277 355 103 C ATOM 415 CG PRO A 53 57.726 34.201 22.558 1.00 13.95 C ANISOU 415 CG PRO A 53 1784 1086 2430 -211 78 431 C ATOM 416 CD PRO A 53 56.815 33.250 23.293 1.00 12.81 C ANISOU 416 CD PRO A 53 1689 1051 2127 -186 452 -60 C ATOM 417 N PHE A 54 59.694 30.179 21.075 1.00 13.36 N ANISOU 417 N PHE A 54 1649 1618 1809 183 128 -116 N ATOM 418 CA PHE A 54 60.605 29.056 21.205 1.00 12.59 C ANISOU 418 CA PHE A 54 1592 1518 1675 113 360 -40 C ATOM 419 C PHE A 54 61.717 29.206 20.156 1.00 12.41 C ANISOU 419 C PHE A 54 1634 1614 1466 231 308 -75 C ATOM 420 O PHE A 54 61.471 29.669 19.046 1.00 13.64 O ANISOU 420 O PHE A 54 1729 1901 1553 -77 94 22 O ATOM 421 CB PHE A 54 59.874 27.727 21.023 1.00 12.14 C ANISOU 421 CB PHE A 54 1473 1614 1525 97 257 -183 C ATOM 422 CG PHE A 54 60.757 26.525 21.162 1.00 12.34 C ANISOU 422 CG PHE A 54 1525 1663 1500 139 166 12 C ATOM 423 CD1 PHE A 54 61.517 26.341 22.305 1.00 13.06 C ANISOU 423 CD1 PHE A 54 1478 1901 1582 1 109 60 C ATOM 424 CD2 PHE A 54 60.841 25.556 20.156 1.00 12.35 C ANISOU 424 CD2 PHE A 54 1550 1725 1418 172 242 64 C ATOM 425 CE1 PHE A 54 62.356 25.250 22.471 1.00 13.71 C ANISOU 425 CE1 PHE A 54 1644 1620 1944 -57 478 -178 C ATOM 426 CE2 PHE A 54 61.652 24.460 20.336 1.00 13.31 C ANISOU 426 CE2 PHE A 54 1598 1685 1774 146 290 -22 C ATOM 427 CZ PHE A 54 62.411 24.301 21.470 1.00 13.44 C ANISOU 427 CZ PHE A 54 1535 1943 1627 107 396 -149 C ATOM 428 N SER A 55 62.906 28.771 20.509 1.00 13.82 N ANISOU 428 N SER A 55 1367 2287 1598 -124 150 -315 N ATOM 429 CA SER A 55 64.052 28.905 19.611 1.00 12.93 C ANISOU 429 CA SER A 55 1628 2233 1052 -97 71 -44 C ATOM 430 C SER A 55 63.916 28.146 18.296 1.00 14.57 C ANISOU 430 C SER A 55 2277 1917 1341 -281 282 -226 C ATOM 431 O SER A 55 64.525 28.580 17.295 1.00 16.19 O ANISOU 431 O SER A 55 2233 2007 1912 -686 415 -19 O ATOM 432 CB SER A 55 65.299 28.396 20.341 1.00 13.02 C ANISOU 432 CB SER A 55 1309 1883 1757 -223 96 12 C ATOM 433 OG SER A 55 65.149 27.056 20.783 1.00 14.82 O ANISOU 433 OG SER A 55 1348 1855 2428 -158 200 100 O ATOM 434 N ASP A 56 63.202 27.026 18.288 1.00 13.84 N ANISOU 434 N ASP A 56 1936 1884 1439 -114 82 -165 N ATOM 435 CA ASP A 56 63.179 26.165 17.103 1.00 14.14 C ANISOU 435 CA ASP A 56 2063 1898 1410 16 -106 -102 C ATOM 436 C ASP A 56 61.793 25.663 16.766 1.00 13.18 C ANISOU 436 C ASP A 56 2014 1785 1209 53 -168 83 C ATOM 437 O ASP A 56 61.483 24.484 16.930 1.00 14.37 O ANISOU 437 O ASP A 56 2111 1904 1446 -163 -25 -16 O ATOM 438 CB ASP A 56 64.162 25.008 17.403 1.00 13.82 C ANISOU 438 CB ASP A 56 1796 2115 1341 72 63 -182 C ATOM 439 CG ASP A 56 65.577 25.538 17.520 1.00 16.70 C ANISOU 439 CG ASP A 56 1914 2743 1689 -145 46 -269 C ATOM 440 OD1 ASP A 56 66.289 25.656 16.501 1.00 18.65 O ANISOU 440 OD1 ASP A 56 2047 3089 1951 -309 269 -271 O ATOM 441 OD2 ASP A 56 65.991 25.882 18.649 1.00 17.44 O ANISOU 441 OD2 ASP A 56 2158 2832 1638 74 75 -420 O ATOM 442 N PRO A 57 60.948 26.546 16.234 1.00 13.15 N ANISOU 442 N PRO A 57 1785 1844 1368 164 -8 -49 N ATOM 443 CA PRO A 57 59.550 26.228 15.964 1.00 13.90 C ANISOU 443 CA PRO A 57 1870 1908 1503 -48 8 -205 C ATOM 444 C PRO A 57 59.397 25.504 14.639 1.00 13.31 C ANISOU 444 C PRO A 57 1981 1857 1219 138 354 -46 C ATOM 445 O PRO A 57 59.017 26.067 13.619 1.00 14.31 O ANISOU 445 O PRO A 57 1823 2077 1537 140 45 17 O ATOM 446 CB PRO A 57 58.874 27.595 16.014 1.00 13.77 C ANISOU 446 CB PRO A 57 1850 1911 1472 -78 153 -337 C ATOM 447 CG PRO A 57 59.928 28.512 15.469 1.00 14.45 C ANISOU 447 CG PRO A 57 1671 2295 1522 6 221 -90 C ATOM 448 CD PRO A 57 61.230 27.984 16.025 1.00 13.73 C ANISOU 448 CD PRO A 57 1765 1829 1622 -31 22 -404 C ATOM 449 N LEU A 58 59.638 24.193 14.697 1.00 15.05 N ANISOU 449 N LEU A 58 2515 1798 1407 3 411 -133 N ATOM 450 CA LEU A 58 59.701 23.387 13.478 1.00 15.54 C ANISOU 450 CA LEU A 58 2232 2215 1458 211 206 -299 C ATOM 451 C LEU A 58 58.387 23.038 12.823 1.00 14.83 C ANISOU 451 C LEU A 58 2443 1987 1204 189 68 -198 C ATOM 452 O LEU A 58 58.423 22.395 11.762 1.00 15.15 O ANISOU 452 O LEU A 58 2685 1953 1120 301 401 -75 O ATOM 453 CB LEU A 58 60.643 22.215 13.736 1.00 18.19 C ANISOU 453 CB LEU A 58 2952 1858 2104 247 69 -382 C ATOM 454 CG LEU A 58 60.263 21.302 14.901 1.00 20.41 C ANISOU 454 CG LEU A 58 3074 1956 2725 321 229 -34 C ATOM 455 CD1 LEU A 58 59.138 20.400 14.445 1.00 24.19 C ANISOU 455 CD1 LEU A 58 3491 2668 3032 -42 -218 0 C ATOM 456 CD2 LEU A 58 61.476 20.506 15.358 1.00 23.95 C ANISOU 456 CD2 LEU A 58 3108 2776 3214 320 -106 129 C ATOM 457 N ALA A 59 57.257 23.518 13.353 1.00 14.88 N ANISOU 457 N ALA A 59 2007 2295 1352 75 17 272 N ATOM 458 CA ALA A 59 55.974 23.311 12.682 1.00 14.97 C ANISOU 458 CA ALA A 59 2128 1881 1678 -35 -93 -29 C ATOM 459 C ALA A 59 55.460 24.641 12.121 1.00 13.69 C ANISOU 459 C ALA A 59 2085 1796 1320 -189 41 -15 C ATOM 460 O ALA A 59 54.331 24.722 11.641 1.00 15.81 O ANISOU 460 O ALA A 59 2355 2469 1183 -152 -139 123 O ATOM 461 CB ALA A 59 54.929 22.683 13.586 1.00 15.42 C ANISOU 461 CB ALA A 59 2148 1959 1753 -48 -24 -118 C ATOM 462 N ASP A 60 56.279 25.687 12.170 1.00 14.08 N ANISOU 462 N ASP A 60 2571 1382 1398 -140 203 -11 N ATOM 463 CA ASP A 60 55.891 27.012 11.715 1.00 13.84 C ANISOU 463 CA ASP A 60 2156 1627 1475 94 -67 1 C ATOM 464 C ASP A 60 56.617 27.521 10.479 1.00 15.10 C ANISOU 464 C ASP A 60 2054 2231 1454 44 -163 149 C ATOM 465 O ASP A 60 57.828 27.336 10.334 1.00 16.31 O ANISOU 465 O ASP A 60 2160 2545 1492 226 -61 400 O ATOM 466 CB ASP A 60 56.118 28.038 12.855 1.00 14.51 C ANISOU 466 CB ASP A 60 1984 2338 1190 17 148 -177 C ATOM 467 CG ASP A 60 55.057 27.904 13.932 1.00 14.70 C ANISOU 467 CG ASP A 60 1604 2516 1466 -76 83 109 C ATOM 468 OD1 ASP A 60 53.877 28.170 13.595 1.00 14.82 O ANISOU 468 OD1 ASP A 60 1740 2335 1556 -7 -31 52 O ATOM 469 OD2 ASP A 60 55.400 27.531 15.081 1.00 15.51 O ANISOU 469 OD2 ASP A 60 1900 2470 1523 4 -156 -37 O ATOM 470 N GLY A 61 55.839 28.140 9.575 1.00 15.05 N ANISOU 470 N GLY A 61 1815 2346 1558 12 -77 334 N ATOM 471 CA GLY A 61 56.393 28.772 8.372 1.00 16.17 C ANISOU 471 CA GLY A 61 2208 2282 1654 -150 153 137 C ATOM 472 C GLY A 61 57.009 30.111 8.739 1.00 16.39 C ANISOU 472 C GLY A 61 2267 2273 1687 -227 256 183 C ATOM 473 O GLY A 61 57.051 30.505 9.915 1.00 16.11 O ANISOU 473 O GLY A 61 2290 2042 1789 -216 156 38 O ATOM 474 N PRO A 62 57.491 30.872 7.754 1.00 15.45 N ANISOU 474 N PRO A 62 2465 1910 1495 -42 81 156 N ATOM 475 CA PRO A 62 58.186 32.110 8.019 1.00 15.91 C ANISOU 475 CA PRO A 62 2639 1925 1481 -88 220 195 C ATOM 476 C PRO A 62 57.419 33.143 8.811 1.00 13.60 C ANISOU 476 C PRO A 62 2012 1879 1275 -53 30 364 C ATOM 477 O PRO A 62 58.030 33.877 9.591 1.00 16.13 O ANISOU 477 O PRO A 62 2446 2224 1459 -529 -260 642 O ATOM 478 CB PRO A 62 58.594 32.644 6.647 1.00 17.94 C ANISOU 478 CB PRO A 62 2798 2481 1536 -190 191 382 C ATOM 479 CG PRO A 62 58.054 31.699 5.655 1.00 20.65 C ANISOU 479 CG PRO A 62 3542 2510 1795 -240 41 244 C ATOM 480 CD PRO A 62 57.506 30.478 6.322 1.00 18.40 C ANISOU 480 CD PRO A 62 2781 2664 1544 -210 296 110 C ATOM 481 N THR A 63 56.119 33.308 8.560 1.00 14.96 N ANISOU 481 N THR A 63 2188 2007 1490 478 -119 497 N ATOM 482 CA THR A 63 55.376 34.355 9.271 1.00 14.97 C ANISOU 482 CA THR A 63 2160 2155 1373 78 -57 65 C ATOM 483 C THR A 63 55.482 34.188 10.784 1.00 14.05 C ANISOU 483 C THR A 63 1922 1975 1442 -80 -3 345 C ATOM 484 O THR A 63 55.860 35.122 11.510 1.00 14.20 O ANISOU 484 O THR A 63 2020 1939 1438 -538 195 580 O ATOM 485 CB THR A 63 53.914 34.407 8.796 1.00 15.07 C ANISOU 485 CB THR A 63 2115 2244 1369 124 37 414 C ATOM 486 OG1 THR A 63 53.888 34.718 7.383 1.00 18.99 O ANISOU 486 OG1 THR A 63 2971 2516 1729 98 -166 1151 O ATOM 487 CG2 THR A 63 53.142 35.461 9.568 1.00 15.18 C ANISOU 487 CG2 THR A 63 2444 1792 1532 92 -42 487 C ATOM 488 N ILE A 64 55.213 32.971 11.262 1.00 14.51 N ANISOU 488 N ILE A 64 1913 1934 1666 88 -39 394 N ATOM 489 CA ILE A 64 55.299 32.736 12.713 1.00 13.82 C ANISOU 489 CA ILE A 64 1699 1931 1619 -145 150 311 C ATOM 490 C ILE A 64 56.735 32.578 13.149 1.00 13.44 C ANISOU 490 C ILE A 64 1823 1826 1457 -10 5 170 C ATOM 491 O ILE A 64 57.079 32.986 14.263 1.00 15.03 O ANISOU 491 O ILE A 64 2161 2032 1518 -297 -308 307 O ATOM 492 CB ILE A 64 54.333 31.636 13.149 1.00 14.35 C ANISOU 492 CB ILE A 64 1797 1936 1721 -249 -33 348 C ATOM 493 CG1 ILE A 64 52.896 32.175 12.972 1.00 14.01 C ANISOU 493 CG1 ILE A 64 1967 1531 1823 -70 135 502 C ATOM 494 CG2 ILE A 64 54.598 31.239 14.593 1.00 14.87 C ANISOU 494 CG2 ILE A 64 1970 2021 1659 -175 278 494 C ATOM 495 CD1 ILE A 64 51.849 31.076 13.008 1.00 14.88 C ANISOU 495 CD1 ILE A 64 1917 1792 1944 -180 -93 353 C ATOM 496 N GLN A 65 57.643 32.104 12.292 1.00 12.89 N ANISOU 496 N GLN A 65 1691 1850 1358 27 -73 292 N ATOM 497 CA GLN A 65 59.063 32.138 12.666 1.00 14.01 C ANISOU 497 CA GLN A 65 1657 2164 1502 -52 -55 40 C ATOM 498 C GLN A 65 59.431 33.581 13.022 1.00 14.48 C ANISOU 498 C GLN A 65 1993 2121 1387 -32 -34 101 C ATOM 499 O GLN A 65 60.164 33.838 13.982 1.00 15.24 O ANISOU 499 O GLN A 65 1811 2702 1276 -49 -101 566 O ATOM 500 CB GLN A 65 59.954 31.712 11.505 1.00 15.34 C ANISOU 500 CB GLN A 65 1795 2287 1748 171 -11 -90 C ATOM 501 CG GLN A 65 59.926 30.236 11.181 1.00 16.35 C ANISOU 501 CG GLN A 65 2098 2274 1840 146 76 -135 C ATOM 502 CD GLN A 65 60.517 29.915 9.818 1.00 15.95 C ANISOU 502 CD GLN A 65 2031 2051 1980 108 210 -91 C ATOM 503 OE1 GLN A 65 61.469 30.573 9.383 1.00 19.19 O ANISOU 503 OE1 GLN A 65 2154 2418 2719 -68 399 -100 O ATOM 504 NE2 GLN A 65 59.967 28.920 9.144 1.00 16.17 N ANISOU 504 NE2 GLN A 65 1764 2133 2249 88 -153 43 N ATOM 505 N ASN A 66 59.013 34.543 12.186 1.00 14.40 N ANISOU 505 N ASN A 66 1620 2061 1790 -157 -192 208 N ATOM 506 CA ASN A 66 59.356 35.944 12.422 1.00 15.20 C ANISOU 506 CA ASN A 66 2127 2025 1622 5 -8 10 C ATOM 507 C ASN A 66 58.647 36.517 13.633 1.00 14.84 C ANISOU 507 C ASN A 66 2085 1921 1634 -112 108 102 C ATOM 508 O ASN A 66 59.194 37.413 14.292 1.00 17.34 O ANISOU 508 O ASN A 66 2534 2255 1802 -93 -82 -183 O ATOM 509 CB ASN A 66 59.124 36.787 11.155 1.00 16.57 C ANISOU 509 CB ASN A 66 2227 2215 1854 -138 89 313 C ATOM 510 CG ASN A 66 60.277 36.588 10.174 1.00 20.76 C ANISOU 510 CG ASN A 66 2542 3243 2104 109 267 123 C ATOM 511 OD1 ASN A 66 61.435 36.507 10.595 1.00 22.76 O ANISOU 511 OD1 ASN A 66 2440 3780 2428 46 380 203 O ATOM 512 ND2 ASN A 66 59.953 36.531 8.888 1.00 22.81 N ANISOU 512 ND2 ASN A 66 3239 3283 2144 72 138 223 N ATOM 513 N ALA A 67 57.476 36.010 14.000 1.00 13.79 N ANISOU 513 N ALA A 67 1763 1791 1684 164 -6 -46 N ATOM 514 CA ALA A 67 56.813 36.504 15.213 1.00 12.72 C ANISOU 514 CA ALA A 67 1499 2042 1292 -184 -80 159 C ATOM 515 C ALA A 67 57.652 36.083 16.430 1.00 13.43 C ANISOU 515 C ALA A 67 1436 1977 1690 176 -273 4 C ATOM 516 O ALA A 67 57.796 36.825 17.398 1.00 14.88 O ANISOU 516 O ALA A 67 2162 1703 1790 -62 -182 59 O ATOM 517 CB ALA A 67 55.423 35.916 15.320 1.00 13.88 C ANISOU 517 CB ALA A 67 1708 1776 1791 -347 51 361 C ATOM 518 N ASN A 68 58.168 34.861 16.381 1.00 14.78 N ANISOU 518 N ASN A 68 1861 1826 1929 78 -282 87 N ATOM 519 CA ASN A 68 59.035 34.344 17.436 1.00 16.22 C ANISOU 519 CA ASN A 68 1536 2407 2220 10 -456 -37 C ATOM 520 C ASN A 68 60.286 35.220 17.532 1.00 16.12 C ANISOU 520 C ASN A 68 1807 2352 1967 -186 -216 -223 C ATOM 521 O ASN A 68 60.676 35.620 18.631 1.00 16.70 O ANISOU 521 O ASN A 68 2025 2636 1682 271 -345 31 O ATOM 522 CB ASN A 68 59.404 32.887 17.190 1.00 17.15 C ANISOU 522 CB ASN A 68 1899 2174 2444 -235 -475 119 C ATOM 523 CG ASN A 68 58.343 31.882 17.564 1.00 20.93 C ANISOU 523 CG ASN A 68 2673 2511 2769 -595 -30 125 C ATOM 524 OD1 ASN A 68 58.276 31.447 18.708 1.00 25.06 O ANISOU 524 OD1 ASN A 68 3761 2858 2902 -487 -110 250 O ATOM 525 ND2 ASN A 68 57.500 31.449 16.629 1.00 22.57 N ANISOU 525 ND2 ASN A 68 2708 3019 2847 -433 -210 137 N ATOM 526 N LEU A 69 60.891 35.546 16.391 1.00 17.06 N ANISOU 526 N LEU A 69 1801 2494 2188 -129 -142 71 N ATOM 527 CA LEU A 69 62.075 36.401 16.346 1.00 17.88 C ANISOU 527 CA LEU A 69 1945 2379 2471 -160 -112 -307 C ATOM 528 C LEU A 69 61.752 37.759 16.949 1.00 14.52 C ANISOU 528 C LEU A 69 1525 1948 2044 -281 -12 226 C ATOM 529 O LEU A 69 62.524 38.246 17.768 1.00 17.12 O ANISOU 529 O LEU A 69 1978 2670 1856 -390 -72 -40 O ATOM 530 CB LEU A 69 62.587 36.580 14.920 1.00 22.94 C ANISOU 530 CB LEU A 69 2769 3309 2636 -215 175 -183 C ATOM 531 CG LEU A 69 63.734 37.561 14.655 1.00 27.35 C ANISOU 531 CG LEU A 69 3260 3477 3654 -524 90 -104 C ATOM 532 CD1 LEU A 69 65.025 37.089 15.303 1.00 31.55 C ANISOU 532 CD1 LEU A 69 3669 3974 4347 -36 -56 -88 C ATOM 533 CD2 LEU A 69 63.956 37.741 13.157 1.00 30.90 C ANISOU 533 CD2 LEU A 69 3812 4101 3826 -262 229 35 C ATOM 534 N ARG A 70 60.616 38.369 16.598 1.00 15.83 N ANISOU 534 N ARG A 70 1707 2170 2137 -98 -161 169 N ATOM 535 CA ARG A 70 60.279 39.660 17.195 1.00 15.64 C ANISOU 535 CA ARG A 70 1735 2091 2117 -305 20 186 C ATOM 536 C ARG A 70 60.137 39.558 18.704 1.00 16.26 C ANISOU 536 C ARG A 70 2057 2044 2079 -320 -207 50 C ATOM 537 O ARG A 70 60.662 40.400 19.437 1.00 17.50 O ANISOU 537 O ARG A 70 2445 2183 2021 -530 -167 -12 O ATOM 538 CB ARG A 70 59.030 40.271 16.571 1.00 16.86 C ANISOU 538 CB ARG A 70 1806 2435 2166 -354 -82 363 C ATOM 539 CG ARG A 70 59.262 40.708 15.123 1.00 16.32 C ANISOU 539 CG ARG A 70 1820 2001 2382 -475 199 496 C ATOM 540 CD ARG A 70 58.060 41.507 14.633 1.00 16.68 C ANISOU 540 CD ARG A 70 1951 2037 2351 -386 57 404 C ATOM 541 NE ARG A 70 56.831 40.723 14.582 1.00 15.53 N ANISOU 541 NE ARG A 70 2070 1827 2003 -379 -237 375 N ATOM 542 CZ ARG A 70 56.459 40.008 13.534 1.00 14.52 C ANISOU 542 CZ ARG A 70 1748 1886 1885 -23 26 183 C ATOM 543 NH1 ARG A 70 57.155 39.921 12.399 1.00 16.01 N ANISOU 543 NH1 ARG A 70 1905 2403 1776 -105 48 691 N ATOM 544 NH2 ARG A 70 55.323 39.322 13.589 1.00 14.46 N ANISOU 544 NH2 ARG A 70 1594 1800 2100 111 -205 416 N ATOM 545 N ALA A 71 59.423 38.555 19.194 1.00 15.32 N ANISOU 545 N ALA A 71 1650 2043 2128 -63 -25 109 N ATOM 546 CA ALA A 71 59.250 38.388 20.628 1.00 15.25 C ANISOU 546 CA ALA A 71 1688 1950 2157 -328 35 146 C ATOM 547 C ALA A 71 60.595 38.221 21.323 1.00 14.40 C ANISOU 547 C ALA A 71 1666 1787 2018 -352 37 -54 C ATOM 548 O ALA A 71 60.839 38.812 22.379 1.00 15.43 O ANISOU 548 O ALA A 71 2030 2076 1758 -467 155 65 O ATOM 549 CB ALA A 71 58.349 37.180 20.860 1.00 15.87 C ANISOU 549 CB ALA A 71 2046 1759 2225 -366 156 121 C ATOM 550 N PHE A 72 61.477 37.411 20.734 1.00 15.13 N ANISOU 550 N PHE A 72 1546 1877 2325 -99 -164 91 N ATOM 551 CA PHE A 72 62.807 37.234 21.322 1.00 15.25 C ANISOU 551 CA PHE A 72 1598 1923 2271 -155 -234 160 C ATOM 552 C PHE A 72 63.580 38.547 21.321 1.00 15.11 C ANISOU 552 C PHE A 72 1721 2042 1980 -272 -118 30 C ATOM 553 O PHE A 72 64.327 38.842 22.266 1.00 17.60 O ANISOU 553 O PHE A 72 1974 2181 2531 -664 -356 -174 O ATOM 554 CB PHE A 72 63.579 36.146 20.559 1.00 16.20 C ANISOU 554 CB PHE A 72 1763 1845 2549 -149 -178 130 C ATOM 555 CG PHE A 72 63.192 34.766 21.048 1.00 16.11 C ANISOU 555 CG PHE A 72 2185 1765 2170 -141 -82 15 C ATOM 556 CD1 PHE A 72 63.148 34.499 22.406 1.00 17.91 C ANISOU 556 CD1 PHE A 72 2632 1980 2191 -281 -10 -12 C ATOM 557 CD2 PHE A 72 62.845 33.775 20.150 1.00 16.31 C ANISOU 557 CD2 PHE A 72 1801 1853 2542 -355 -288 -21 C ATOM 558 CE1 PHE A 72 62.800 33.240 22.867 1.00 18.54 C ANISOU 558 CE1 PHE A 72 2461 1959 2626 -250 111 -34 C ATOM 559 CE2 PHE A 72 62.506 32.520 20.611 1.00 17.27 C ANISOU 559 CE2 PHE A 72 2160 2129 2273 -385 -74 221 C ATOM 560 CZ PHE A 72 62.474 32.250 21.961 1.00 16.89 C ANISOU 560 CZ PHE A 72 2069 2168 2180 -63 -231 81 C ATOM 561 N ALA A 73 63.412 39.343 20.268 1.00 17.13 N ANISOU 561 N ALA A 73 2005 2054 2452 -428 130 384 N ATOM 562 CA ALA A 73 64.123 40.629 20.220 1.00 18.48 C ANISOU 562 CA ALA A 73 2357 2124 2540 -545 80 114 C ATOM 563 C ALA A 73 63.673 41.518 21.372 1.00 19.95 C ANISOU 563 C ALA A 73 2462 2116 3003 -360 -24 -160 C ATOM 564 O ALA A 73 64.465 42.367 21.813 1.00 21.28 O ANISOU 564 O ALA A 73 2261 2355 3468 -621 124 -98 O ATOM 565 CB ALA A 73 63.906 41.313 18.888 1.00 19.79 C ANISOU 565 CB ALA A 73 2530 2406 2582 -401 269 289 C ATOM 566 N ALA A 74 62.458 41.305 21.873 1.00 19.46 N ANISOU 566 N ALA A 74 2643 1928 2824 -214 213 15 N ATOM 567 CA ALA A 74 61.918 42.081 22.979 1.00 17.64 C ANISOU 567 CA ALA A 74 2454 1758 2491 -448 -55 39 C ATOM 568 C ALA A 74 62.177 41.413 24.329 1.00 18.35 C ANISOU 568 C ALA A 74 2427 2210 2336 -256 -157 -96 C ATOM 569 O ALA A 74 61.706 41.857 25.372 1.00 19.55 O ANISOU 569 O ALA A 74 2582 2300 2545 -497 44 -250 O ATOM 570 CB ALA A 74 60.426 42.326 22.793 1.00 19.31 C ANISOU 570 CB ALA A 74 2454 2193 2689 -307 178 187 C ATOM 571 N GLY A 75 62.942 40.334 24.314 1.00 17.19 N ANISOU 571 N GLY A 75 2159 2169 2204 -362 -461 202 N ATOM 572 CA GLY A 75 63.350 39.621 25.502 1.00 16.04 C ANISOU 572 CA GLY A 75 1886 2118 2091 -88 -76 211 C ATOM 573 C GLY A 75 62.299 38.746 26.151 1.00 15.60 C ANISOU 573 C GLY A 75 1510 2199 2218 -256 -395 69 C ATOM 574 O GLY A 75 62.413 38.384 27.320 1.00 16.73 O ANISOU 574 O GLY A 75 2108 2000 2249 -202 -230 108 O ATOM 575 N VAL A 76 61.258 38.386 25.384 1.00 14.28 N ANISOU 575 N VAL A 76 1669 1735 2023 -247 -321 -159 N ATOM 576 CA VAL A 76 60.170 37.597 25.936 1.00 15.07 C ANISOU 576 CA VAL A 76 1928 1509 2290 -330 -331 -66 C ATOM 577 C VAL A 76 60.602 36.196 26.331 1.00 14.12 C ANISOU 577 C VAL A 76 1652 1592 2120 -48 -210 -214 C ATOM 578 O VAL A 76 61.226 35.465 25.561 1.00 18.53 O ANISOU 578 O VAL A 76 2649 1974 2416 211 197 -292 O ATOM 579 CB VAL A 76 59.003 37.588 24.929 1.00 15.49 C ANISOU 579 CB VAL A 76 1790 1626 2469 -243 -308 -20 C ATOM 580 CG1 VAL A 76 57.843 36.759 25.448 1.00 15.92 C ANISOU 580 CG1 VAL A 76 1947 1654 2447 -434 -189 -272 C ATOM 581 CG2 VAL A 76 58.535 39.024 24.709 1.00 15.59 C ANISOU 581 CG2 VAL A 76 1944 1546 2433 -358 -466 -55 C ATOM 582 N THR A 77 60.240 35.796 27.542 1.00 12.92 N ANISOU 582 N THR A 77 1660 1120 2129 -364 -260 -337 N ATOM 583 CA THR A 77 60.534 34.474 28.075 1.00 13.63 C ANISOU 583 CA THR A 77 1712 1374 2092 -330 -222 -56 C ATOM 584 C THR A 77 59.241 33.749 28.423 1.00 14.30 C ANISOU 584 C THR A 77 1550 1440 2443 -162 -98 -120 C ATOM 585 O THR A 77 58.186 34.372 28.586 1.00 14.29 O ANISOU 585 O THR A 77 1601 1449 2377 -94 -191 -448 O ATOM 586 CB THR A 77 61.289 34.611 29.412 1.00 14.57 C ANISOU 586 CB THR A 77 1248 2055 2233 -332 -235 99 C ATOM 587 OG1 THR A 77 60.461 35.280 30.366 1.00 14.70 O ANISOU 587 OG1 THR A 77 1483 1764 2340 -697 -239 -266 O ATOM 588 CG2 THR A 77 62.578 35.400 29.236 1.00 15.78 C ANISOU 588 CG2 THR A 77 1393 1906 2698 -455 -225 -194 C ATOM 589 N PRO A 78 59.310 32.449 28.659 1.00 13.70 N ANISOU 589 N PRO A 78 1390 1435 2379 75 90 -64 N ATOM 590 CA PRO A 78 58.112 31.717 29.066 1.00 12.79 C ANISOU 590 CA PRO A 78 1264 1316 2278 47 1 -249 C ATOM 591 C PRO A 78 57.564 32.254 30.374 1.00 12.07 C ANISOU 591 C PRO A 78 1435 1095 2058 -176 -49 -68 C ATOM 592 O PRO A 78 56.336 32.342 30.572 1.00 12.94 O ANISOU 592 O PRO A 78 1437 1150 2329 208 -131 -72 O ATOM 593 CB PRO A 78 58.612 30.281 29.198 1.00 14.86 C ANISOU 593 CB PRO A 78 2030 1333 2283 125 241 108 C ATOM 594 CG PRO A 78 59.731 30.235 28.191 1.00 15.17 C ANISOU 594 CG PRO A 78 2054 1205 2505 35 357 -118 C ATOM 595 CD PRO A 78 60.463 31.552 28.401 1.00 15.70 C ANISOU 595 CD PRO A 78 1881 1146 2938 202 124 -304 C ATOM 596 N ALA A 79 58.431 32.649 31.311 1.00 13.65 N ANISOU 596 N ALA A 79 1716 1368 2102 -69 -236 -187 N ATOM 597 CA ALA A 79 57.919 33.208 32.571 1.00 14.61 C ANISOU 597 CA ALA A 79 1713 1815 2025 4 -264 -188 C ATOM 598 C ALA A 79 57.084 34.456 32.308 1.00 13.60 C ANISOU 598 C ALA A 79 1812 1419 1937 -205 -160 -294 C ATOM 599 O ALA A 79 56.018 34.656 32.916 1.00 13.97 O ANISOU 599 O ALA A 79 1890 1482 1937 -22 -155 -408 O ATOM 600 CB ALA A 79 59.037 33.501 33.559 1.00 15.40 C ANISOU 600 CB ALA A 79 2073 1602 2176 9 -512 -314 C ATOM 601 N GLN A 80 57.568 35.337 31.425 1.00 13.42 N ANISOU 601 N GLN A 80 2060 1133 1905 -100 -167 -386 N ATOM 602 CA GLN A 80 56.782 36.539 31.119 1.00 14.19 C ANISOU 602 CA GLN A 80 2128 1086 2178 -136 -74 -173 C ATOM 603 C GLN A 80 55.478 36.188 30.417 1.00 13.61 C ANISOU 603 C GLN A 80 2115 973 2084 31 -86 -253 C ATOM 604 O GLN A 80 54.455 36.837 30.597 1.00 14.42 O ANISOU 604 O GLN A 80 1919 1341 2219 -20 188 -18 O ATOM 605 CB GLN A 80 57.593 37.508 30.263 1.00 13.17 C ANISOU 605 CB GLN A 80 1944 1476 1583 -488 -231 -457 C ATOM 606 CG GLN A 80 58.712 38.164 31.073 1.00 14.94 C ANISOU 606 CG GLN A 80 2044 1509 2125 -456 -551 -422 C ATOM 607 CD GLN A 80 59.596 39.033 30.221 1.00 19.56 C ANISOU 607 CD GLN A 80 2509 2607 2314 -550 -109 -131 C ATOM 608 OE1 GLN A 80 59.613 38.942 29.001 1.00 20.89 O ANISOU 608 OE1 GLN A 80 3027 2534 2377 -689 143 -473 O ATOM 609 NE2 GLN A 80 60.359 39.921 30.852 1.00 22.86 N ANISOU 609 NE2 GLN A 80 3279 2552 2855 -821 -227 -278 N ATOM 610 N CYS A 81 55.497 35.134 29.593 1.00 13.15 N ANISOU 610 N CYS A 81 1820 1167 2008 33 -132 -388 N ATOM 611 CA CYS A 81 54.279 34.683 28.935 1.00 12.19 C ANISOU 611 CA CYS A 81 1665 1303 1666 36 7 -287 C ATOM 612 C CYS A 81 53.240 34.253 29.964 1.00 12.51 C ANISOU 612 C CYS A 81 1854 1381 1520 -15 -6 -324 C ATOM 613 O CYS A 81 52.057 34.577 29.808 1.00 12.71 O ANISOU 613 O CYS A 81 1833 1114 1883 52 147 -286 O ATOM 614 CB CYS A 81 54.616 33.536 27.977 1.00 12.21 C ANISOU 614 CB CYS A 81 1231 1377 2032 107 -114 -461 C ATOM 615 SG CYS A 81 55.465 34.096 26.473 1.00 13.48 S ANISOU 615 SG CYS A 81 1714 1700 1710 54 -128 -638 S ATOM 616 N PHE A 82 53.681 33.543 30.993 1.00 11.88 N ANISOU 616 N PHE A 82 1799 1134 1580 -258 -76 -294 N ATOM 617 CA PHE A 82 52.728 33.125 32.029 1.00 12.80 C ANISOU 617 CA PHE A 82 2005 1288 1571 119 251 -248 C ATOM 618 C PHE A 82 52.209 34.333 32.816 1.00 12.22 C ANISOU 618 C PHE A 82 2098 1328 1219 -16 65 -308 C ATOM 619 O PHE A 82 51.041 34.303 33.187 1.00 14.82 O ANISOU 619 O PHE A 82 2195 1739 1695 247 216 -416 O ATOM 620 CB PHE A 82 53.298 32.035 32.932 1.00 14.03 C ANISOU 620 CB PHE A 82 2056 1544 1730 -45 -231 -169 C ATOM 621 CG PHE A 82 53.155 30.657 32.325 1.00 13.58 C ANISOU 621 CG PHE A 82 1859 1360 1941 -151 -112 39 C ATOM 622 CD1 PHE A 82 51.931 30.016 32.378 1.00 15.81 C ANISOU 622 CD1 PHE A 82 2098 1373 2535 -352 -56 92 C ATOM 623 CD2 PHE A 82 54.223 30.005 31.747 1.00 17.95 C ANISOU 623 CD2 PHE A 82 2037 1836 2947 -333 391 -351 C ATOM 624 CE1 PHE A 82 51.776 28.757 31.816 1.00 16.73 C ANISOU 624 CE1 PHE A 82 2102 1580 2673 -307 -107 -162 C ATOM 625 CE2 PHE A 82 54.082 28.740 31.200 1.00 19.19 C ANISOU 625 CE2 PHE A 82 2203 1793 3295 -318 218 -335 C ATOM 626 CZ PHE A 82 52.840 28.119 31.241 1.00 18.31 C ANISOU 626 CZ PHE A 82 2217 1848 2892 -375 228 -188 C ATOM 627 N GLU A 83 53.025 35.363 33.028 1.00 13.21 N ANISOU 627 N GLU A 83 2372 968 1679 123 203 -426 N ATOM 628 CA GLU A 83 52.511 36.577 33.679 1.00 14.58 C ANISOU 628 CA GLU A 83 2297 1286 1956 392 16 -595 C ATOM 629 C GLU A 83 51.463 37.199 32.753 1.00 13.27 C ANISOU 629 C GLU A 83 2173 1414 1457 259 237 -509 C ATOM 630 O GLU A 83 50.387 37.601 33.221 1.00 14.29 O ANISOU 630 O GLU A 83 2674 1296 1458 477 635 -570 O ATOM 631 CB GLU A 83 53.645 37.556 33.956 1.00 17.49 C ANISOU 631 CB GLU A 83 2642 1481 2524 67 18 -455 C ATOM 632 CG GLU A 83 54.654 37.082 34.981 1.00 22.40 C ANISOU 632 CG GLU A 83 3037 2645 2828 130 -288 -250 C ATOM 633 CD GLU A 83 55.939 37.891 34.987 1.00 28.98 C ANISOU 633 CD GLU A 83 3438 3490 4084 -362 -300 -167 C ATOM 634 OE1 GLU A 83 56.079 38.886 34.245 1.00 31.30 O ANISOU 634 OE1 GLU A 83 3831 3752 4312 -167 -478 -4 O ATOM 635 OE2 GLU A 83 56.854 37.496 35.746 1.00 33.49 O ANISOU 635 OE2 GLU A 83 3883 4064 4780 -125 -554 0 O ATOM 636 N MET A 84 51.732 37.200 31.440 1.00 12.43 N ANISOU 636 N MET A 84 2037 1223 1461 83 225 -572 N ATOM 637 CA MET A 84 50.748 37.740 30.513 1.00 12.54 C ANISOU 637 CA MET A 84 2193 1027 1543 79 169 -484 C ATOM 638 C MET A 84 49.444 36.945 30.586 1.00 13.19 C ANISOU 638 C MET A 84 1963 1323 1726 212 284 51 C ATOM 639 O MET A 84 48.362 37.520 30.589 1.00 14.14 O ANISOU 639 O MET A 84 2065 1032 2278 262 620 -44 O ATOM 640 CB MET A 84 51.193 37.737 29.047 1.00 13.80 C ANISOU 640 CB MET A 84 2320 1243 1681 -28 375 -207 C ATOM 641 CG MET A 84 52.352 38.675 28.758 1.00 13.91 C ANISOU 641 CG MET A 84 2393 1237 1656 -33 443 -229 C ATOM 642 SD MET A 84 52.914 38.520 27.058 1.00 16.79 S ANISOU 642 SD MET A 84 2789 1366 2225 -423 1359 -349 S ATOM 643 CE MET A 84 51.510 39.147 26.146 1.00 19.65 C ANISOU 643 CE MET A 84 3395 1693 2379 -227 909 -233 C ATOM 644 N LEU A 85 49.570 35.608 30.577 1.00 13.19 N ANISOU 644 N LEU A 85 1903 1254 1856 -78 539 -136 N ATOM 645 CA LEU A 85 48.370 34.772 30.595 1.00 11.99 C ANISOU 645 CA LEU A 85 1960 775 1822 42 339 75 C ATOM 646 C LEU A 85 47.508 35.043 31.829 1.00 12.87 C ANISOU 646 C LEU A 85 1685 1509 1694 -88 134 -90 C ATOM 647 O LEU A 85 46.283 35.098 31.700 1.00 13.23 O ANISOU 647 O LEU A 85 1710 1506 1810 363 213 3 O ATOM 648 CB LEU A 85 48.780 33.303 30.498 1.00 11.62 C ANISOU 648 CB LEU A 85 1670 882 1864 258 167 155 C ATOM 649 CG LEU A 85 49.328 32.881 29.127 1.00 11.60 C ANISOU 649 CG LEU A 85 1562 1136 1708 85 36 178 C ATOM 650 CD1 LEU A 85 50.088 31.565 29.257 1.00 12.45 C ANISOU 650 CD1 LEU A 85 1876 1252 1602 273 -47 87 C ATOM 651 CD2 LEU A 85 48.208 32.743 28.111 1.00 13.51 C ANISOU 651 CD2 LEU A 85 1955 1773 1404 240 -57 -264 C ATOM 652 N ALA A 86 48.146 35.215 32.981 1.00 12.57 N ANISOU 652 N ALA A 86 1712 1701 1365 138 367 -147 N ATOM 653 CA ALA A 86 47.387 35.523 34.194 1.00 14.26 C ANISOU 653 CA ALA A 86 2117 1855 1448 159 436 -325 C ATOM 654 C ALA A 86 46.630 36.838 34.009 1.00 15.26 C ANISOU 654 C ALA A 86 2191 1726 1881 -9 503 -90 C ATOM 655 O ALA A 86 45.468 36.922 34.400 1.00 16.66 O ANISOU 655 O ALA A 86 2254 1974 2100 503 592 -132 O ATOM 656 CB ALA A 86 48.286 35.562 35.410 1.00 15.23 C ANISOU 656 CB ALA A 86 2107 1990 1688 213 280 -256 C ATOM 657 N ILE A 87 47.283 37.854 33.454 1.00 13.82 N ANISOU 657 N ILE A 87 2592 1353 1307 228 277 41 N ATOM 658 CA ILE A 87 46.609 39.145 33.270 1.00 14.41 C ANISOU 658 CA ILE A 87 2198 1550 1727 343 167 -217 C ATOM 659 C ILE A 87 45.463 39.017 32.285 1.00 12.76 C ANISOU 659 C ILE A 87 2228 1302 1320 154 346 -193 C ATOM 660 O ILE A 87 44.394 39.624 32.421 1.00 15.62 O ANISOU 660 O ILE A 87 2418 1774 1742 448 354 -130 O ATOM 661 CB ILE A 87 47.595 40.216 32.794 1.00 15.25 C ANISOU 661 CB ILE A 87 2446 1665 1682 102 150 -274 C ATOM 662 CG1 ILE A 87 48.808 40.480 33.691 1.00 20.16 C ANISOU 662 CG1 ILE A 87 2656 2510 2493 -67 -138 -392 C ATOM 663 CG2 ILE A 87 46.846 41.529 32.562 1.00 21.50 C ANISOU 663 CG2 ILE A 87 3228 2249 2691 549 -256 104 C ATOM 664 CD1 ILE A 87 49.749 41.464 33.004 1.00 23.37 C ANISOU 664 CD1 ILE A 87 3023 2802 3053 -47 198 8 C ATOM 665 N ILE A 88 45.654 38.278 31.195 1.00 11.47 N ANISOU 665 N ILE A 88 1783 1306 1271 396 323 -168 N ATOM 666 CA ILE A 88 44.601 38.090 30.191 1.00 12.26 C ANISOU 666 CA ILE A 88 1382 1596 1681 281 385 -223 C ATOM 667 C ILE A 88 43.387 37.425 30.820 1.00 12.75 C ANISOU 667 C ILE A 88 1877 1190 1778 143 375 81 C ATOM 668 O ILE A 88 42.247 37.832 30.597 1.00 13.75 O ANISOU 668 O ILE A 88 1845 1628 1751 354 658 28 O ATOM 669 CB ILE A 88 45.137 37.274 28.997 1.00 12.06 C ANISOU 669 CB ILE A 88 1786 962 1836 33 523 -184 C ATOM 670 CG1 ILE A 88 46.252 38.056 28.288 1.00 12.71 C ANISOU 670 CG1 ILE A 88 1575 1307 1947 107 607 -135 C ATOM 671 CG2 ILE A 88 44.044 36.911 28.021 1.00 13.00 C ANISOU 671 CG2 ILE A 88 2002 1214 1722 0 526 -454 C ATOM 672 CD1 ILE A 88 47.092 37.170 27.379 1.00 13.48 C ANISOU 672 CD1 ILE A 88 2340 1282 1502 327 451 -162 C ATOM 673 N ARG A 89 43.615 36.370 31.604 1.00 12.32 N ANISOU 673 N ARG A 89 2122 820 1737 169 430 -125 N ATOM 674 CA ARG A 89 42.518 35.674 32.265 1.00 12.59 C ANISOU 674 CA ARG A 89 1893 1045 1845 221 433 -150 C ATOM 675 C ARG A 89 41.842 36.583 33.285 1.00 13.13 C ANISOU 675 C ARG A 89 1958 1290 1739 236 340 -236 C ATOM 676 O ARG A 89 40.624 36.499 33.428 1.00 14.03 O ANISOU 676 O ARG A 89 2062 915 2354 8 492 -314 O ATOM 677 CB ARG A 89 43.010 34.379 32.909 1.00 12.54 C ANISOU 677 CB ARG A 89 1971 1097 1698 107 375 -51 C ATOM 678 CG ARG A 89 41.972 33.689 33.778 1.00 11.82 C ANISOU 678 CG ARG A 89 2261 994 1238 25 346 -146 C ATOM 679 CD ARG A 89 40.745 33.285 32.990 1.00 12.88 C ANISOU 679 CD ARG A 89 2085 1405 1405 123 430 -457 C ATOM 680 NE ARG A 89 41.044 32.213 32.026 1.00 14.14 N ANISOU 680 NE ARG A 89 2379 1545 1448 247 398 -524 N ATOM 681 CZ ARG A 89 40.487 32.091 30.838 1.00 14.03 C ANISOU 681 CZ ARG A 89 2235 1408 1686 267 142 -521 C ATOM 682 NH1 ARG A 89 39.604 32.967 30.355 1.00 13.88 N ANISOU 682 NH1 ARG A 89 2180 1374 1720 203 195 -415 N ATOM 683 NH2 ARG A 89 40.803 31.048 30.064 1.00 13.12 N ANISOU 683 NH2 ARG A 89 2081 1168 1737 621 193 -278 N ATOM 684 N GLU A 90 42.604 37.410 33.986 1.00 13.21 N ANISOU 684 N GLU A 90 1789 1668 1564 132 492 -272 N ATOM 685 CA GLU A 90 42.014 38.325 34.963 1.00 13.59 C ANISOU 685 CA GLU A 90 2002 1348 1812 267 329 -310 C ATOM 686 C GLU A 90 41.072 39.306 34.301 1.00 13.51 C ANISOU 686 C GLU A 90 1741 1596 1795 325 528 -230 C ATOM 687 O GLU A 90 40.125 39.750 34.967 1.00 16.46 O ANISOU 687 O GLU A 90 1994 1972 2289 402 858 -487 O ATOM 688 CB GLU A 90 43.137 39.043 35.712 1.00 14.98 C ANISOU 688 CB GLU A 90 2132 1733 1826 84 195 -199 C ATOM 689 CG AGLU A 90 43.687 38.085 36.761 0.50 14.60 C ANISOU 689 CG AGLU A 90 2021 1648 1880 90 73 -258 C ATOM 690 CD AGLU A 90 44.979 38.556 37.386 0.50 18.65 C ANISOU 690 CD AGLU A 90 2149 2391 2548 -198 -91 -106 C ATOM 691 OE1AGLU A 90 45.472 39.611 36.942 0.50 20.44 O ANISOU 691 OE1AGLU A 90 2478 2381 2907 -243 -70 -65 O ATOM 692 OE2AGLU A 90 45.460 37.851 38.294 0.50 20.76 O ANISOU 692 OE2AGLU A 90 2507 2580 2800 -22 -321 -160 O ATOM 693 CG BGLU A 90 42.776 39.871 36.922 0.50 15.76 C ANISOU 693 CG BGLU A 90 2085 1980 1926 -106 293 -316 C ATOM 694 CD BGLU A 90 44.001 40.447 37.613 0.50 17.16 C ANISOU 694 CD BGLU A 90 2235 2391 1893 -208 91 -126 C ATOM 695 OE1BGLU A 90 44.991 40.793 36.918 0.50 16.88 O ANISOU 695 OE1BGLU A 90 1998 2601 1817 -21 77 -254 O ATOM 696 OE2BGLU A 90 43.978 40.566 38.857 0.50 18.02 O ANISOU 696 OE2BGLU A 90 2492 2511 1846 -31 -84 95 O ATOM 697 N LYS A 91 41.328 39.690 33.054 1.00 12.55 N ANISOU 697 N LYS A 91 2003 1142 1625 160 370 -497 N ATOM 698 CA LYS A 91 40.447 40.606 32.349 1.00 13.18 C ANISOU 698 CA LYS A 91 1900 990 2119 30 369 -305 C ATOM 699 C LYS A 91 39.261 39.910 31.693 1.00 12.71 C ANISOU 699 C LYS A 91 1884 1132 1815 288 196 -417 C ATOM 700 O LYS A 91 38.242 40.534 31.429 1.00 15.34 O ANISOU 700 O LYS A 91 2082 967 2779 334 133 -133 O ATOM 701 CB LYS A 91 41.236 41.302 31.218 1.00 13.61 C ANISOU 701 CB LYS A 91 2135 1269 1767 97 369 -378 C ATOM 702 CG LYS A 91 42.213 42.344 31.733 1.00 14.33 C ANISOU 702 CG LYS A 91 1987 1481 1978 -84 276 -72 C ATOM 703 CD LYS A 91 42.920 43.096 30.616 1.00 15.54 C ANISOU 703 CD LYS A 91 1920 1713 2273 58 278 267 C ATOM 704 CE LYS A 91 43.899 42.208 29.876 1.00 17.89 C ANISOU 704 CE LYS A 91 2286 2342 2169 141 586 168 C ATOM 705 NZ LYS A 91 44.781 43.042 29.001 1.00 18.80 N ANISOU 705 NZ LYS A 91 2194 2542 2406 127 504 460 N ATOM 706 N HIS A 92 39.467 38.656 31.268 1.00 13.08 N ANISOU 706 N HIS A 92 2020 1153 1798 342 528 -481 N ATOM 707 CA HIS A 92 38.514 37.920 30.446 1.00 12.71 C ANISOU 707 CA HIS A 92 1628 1466 1733 134 497 37 C ATOM 708 C HIS A 92 38.242 36.554 31.039 1.00 14.16 C ANISOU 708 C HIS A 92 2324 1112 1945 242 501 -228 C ATOM 709 O HIS A 92 38.971 35.613 30.749 1.00 14.68 O ANISOU 709 O HIS A 92 2630 1146 1800 378 649 -195 O ATOM 710 CB HIS A 92 39.138 37.762 29.049 1.00 14.49 C ANISOU 710 CB HIS A 92 2173 1586 1745 125 560 -146 C ATOM 711 CG HIS A 92 39.601 39.044 28.435 1.00 13.78 C ANISOU 711 CG HIS A 92 2186 1303 1747 309 480 -297 C ATOM 712 ND1 HIS A 92 38.687 39.925 27.869 1.00 15.01 N ANISOU 712 ND1 HIS A 92 2525 1315 1864 292 464 38 N ATOM 713 CD2 HIS A 92 40.821 39.584 28.242 1.00 13.75 C ANISOU 713 CD2 HIS A 92 2333 1275 1616 120 371 -250 C ATOM 714 CE1 HIS A 92 39.352 40.964 27.386 1.00 14.32 C ANISOU 714 CE1 HIS A 92 2359 1219 1863 272 340 -85 C ATOM 715 NE2 HIS A 92 40.644 40.787 27.585 1.00 14.76 N ANISOU 715 NE2 HIS A 92 2362 1329 1916 232 214 -161 N ATOM 716 N PRO A 93 37.220 36.415 31.861 1.00 14.25 N ANISOU 716 N PRO A 93 2457 956 2000 256 656 -407 N ATOM 717 CA PRO A 93 37.003 35.194 32.600 1.00 14.71 C ANISOU 717 CA PRO A 93 2330 1384 1877 -119 767 -266 C ATOM 718 C PRO A 93 36.526 33.974 31.856 1.00 13.19 C ANISOU 718 C PRO A 93 1933 1471 1609 408 639 -457 C ATOM 719 O PRO A 93 36.752 32.888 32.392 1.00 14.69 O ANISOU 719 O PRO A 93 2757 1131 1695 229 721 -641 O ATOM 720 CB PRO A 93 35.962 35.606 33.654 1.00 16.33 C ANISOU 720 CB PRO A 93 2606 1846 1752 72 856 -131 C ATOM 721 CG PRO A 93 35.232 36.746 33.040 1.00 15.86 C ANISOU 721 CG PRO A 93 2295 1578 2153 310 1071 -452 C ATOM 722 CD PRO A 93 36.316 37.522 32.307 1.00 15.95 C ANISOU 722 CD PRO A 93 2643 1251 2166 306 1124 -357 C ATOM 723 N THR A 94 35.859 34.126 30.726 1.00 13.46 N ANISOU 723 N THR A 94 1553 1661 1900 266 402 -723 N ATOM 724 CA THR A 94 35.246 32.959 30.104 1.00 14.68 C ANISOU 724 CA THR A 94 1867 1546 2164 -76 105 -242 C ATOM 725 C THR A 94 35.871 32.536 28.795 1.00 14.11 C ANISOU 725 C THR A 94 1834 1289 2240 115 199 -124 C ATOM 726 O THR A 94 35.612 31.410 28.346 1.00 14.00 O ANISOU 726 O THR A 94 2125 988 2208 236 229 142 O ATOM 727 CB THR A 94 33.733 33.226 29.880 1.00 16.64 C ANISOU 727 CB THR A 94 1932 2193 2197 379 367 -215 C ATOM 728 OG1 THR A 94 33.561 34.313 28.960 1.00 17.94 O ANISOU 728 OG1 THR A 94 1565 2261 2989 828 -93 -40 O ATOM 729 CG2 THR A 94 33.061 33.583 31.199 1.00 18.03 C ANISOU 729 CG2 THR A 94 1828 2444 2579 249 496 -701 C ATOM 730 N ILE A 95 36.660 33.399 28.165 1.00 13.26 N ANISOU 730 N ILE A 95 1588 1552 1900 148 325 -332 N ATOM 731 CA ILE A 95 37.195 32.998 26.853 1.00 12.35 C ANISOU 731 CA ILE A 95 1925 971 1798 63 310 -215 C ATOM 732 C ILE A 95 38.144 31.829 27.005 1.00 12.76 C ANISOU 732 C ILE A 95 1622 1188 2039 115 225 -470 C ATOM 733 O ILE A 95 39.069 31.878 27.812 1.00 13.94 O ANISOU 733 O ILE A 95 1653 1591 2052 322 190 -572 O ATOM 734 CB ILE A 95 37.891 34.210 26.199 1.00 12.64 C ANISOU 734 CB ILE A 95 1803 1093 1908 117 439 -141 C ATOM 735 CG1 ILE A 95 38.255 33.867 24.753 1.00 13.36 C ANISOU 735 CG1 ILE A 95 2166 1060 1848 237 315 -192 C ATOM 736 CG2 ILE A 95 39.116 34.671 26.971 1.00 12.19 C ANISOU 736 CG2 ILE A 95 2135 408 2089 49 401 -519 C ATOM 737 CD1 ILE A 95 38.641 35.087 23.940 1.00 15.68 C ANISOU 737 CD1 ILE A 95 2501 1259 2199 355 496 108 C ATOM 738 N PRO A 96 37.991 30.795 26.180 1.00 12.25 N ANISOU 738 N PRO A 96 1757 1096 1799 214 140 -325 N ATOM 739 CA PRO A 96 38.934 29.683 26.245 1.00 11.80 C ANISOU 739 CA PRO A 96 1479 1068 1934 123 91 -124 C ATOM 740 C PRO A 96 40.295 30.139 25.733 1.00 10.53 C ANISOU 740 C PRO A 96 1577 999 1424 464 318 58 C ATOM 741 O PRO A 96 40.396 30.826 24.709 1.00 12.67 O ANISOU 741 O PRO A 96 2097 1167 1548 600 67 236 O ATOM 742 CB PRO A 96 38.327 28.637 25.322 1.00 10.68 C ANISOU 742 CB PRO A 96 1415 1129 1516 182 214 -119 C ATOM 743 CG PRO A 96 36.878 28.997 25.257 1.00 12.37 C ANISOU 743 CG PRO A 96 1283 1513 1904 -38 -188 -251 C ATOM 744 CD PRO A 96 36.888 30.521 25.243 1.00 13.33 C ANISOU 744 CD PRO A 96 1771 1490 1803 343 76 -209 C ATOM 745 N ILE A 97 41.321 29.740 26.482 1.00 10.72 N ANISOU 745 N ILE A 97 1263 1288 1520 194 248 -73 N ATOM 746 CA ILE A 97 42.697 30.100 26.150 1.00 11.34 C ANISOU 746 CA ILE A 97 1369 1381 1560 98 182 13 C ATOM 747 C ILE A 97 43.490 28.819 25.940 1.00 11.58 C ANISOU 747 C ILE A 97 1707 1444 1250 214 431 94 C ATOM 748 O ILE A 97 43.607 27.989 26.852 1.00 11.62 O ANISOU 748 O ILE A 97 1837 1273 1308 304 510 107 O ATOM 749 CB ILE A 97 43.358 30.958 27.241 1.00 13.28 C ANISOU 749 CB ILE A 97 1540 1410 2098 -56 106 -222 C ATOM 750 CG1 ILE A 97 42.655 32.316 27.368 1.00 14.11 C ANISOU 750 CG1 ILE A 97 1908 1638 1813 285 191 -163 C ATOM 751 CG2 ILE A 97 44.837 31.162 26.935 1.00 13.51 C ANISOU 751 CG2 ILE A 97 1502 1516 2116 -82 23 103 C ATOM 752 CD1 ILE A 97 43.114 33.121 28.572 1.00 15.40 C ANISOU 752 CD1 ILE A 97 1990 1514 2349 377 -106 -385 C ATOM 753 N GLY A 98 43.981 28.640 24.721 1.00 10.57 N ANISOU 753 N GLY A 98 1594 1379 1042 236 356 568 N ATOM 754 CA GLY A 98 44.787 27.473 24.413 1.00 11.37 C ANISOU 754 CA GLY A 98 1713 1269 1336 54 319 165 C ATOM 755 C GLY A 98 46.217 27.882 24.094 1.00 10.09 C ANISOU 755 C GLY A 98 1730 1031 1073 227 465 482 C ATOM 756 O GLY A 98 46.434 28.861 23.372 1.00 12.32 O ANISOU 756 O GLY A 98 1412 1277 1990 168 329 1087 O ATOM 757 N LEU A 99 47.188 27.125 24.581 1.00 9.89 N ANISOU 757 N LEU A 99 1286 1342 1130 169 120 -149 N ATOM 758 CA LEU A 99 48.588 27.388 24.249 1.00 9.15 C ANISOU 758 CA LEU A 99 1296 1272 911 179 98 -11 C ATOM 759 C LEU A 99 49.044 26.450 23.129 1.00 10.60 C ANISOU 759 C LEU A 99 1603 1205 1220 97 379 -63 C ATOM 760 O LEU A 99 48.630 25.290 23.081 1.00 12.56 O ANISOU 760 O LEU A 99 1865 1299 1609 -21 997 81 O ATOM 761 CB LEU A 99 49.500 27.139 25.453 1.00 9.63 C ANISOU 761 CB LEU A 99 1322 1387 951 449 107 35 C ATOM 762 CG LEU A 99 49.179 27.983 26.692 1.00 10.00 C ANISOU 762 CG LEU A 99 1373 1191 1234 113 82 -205 C ATOM 763 CD1 LEU A 99 50.206 27.773 27.782 1.00 11.86 C ANISOU 763 CD1 LEU A 99 1473 1454 1579 267 -107 -49 C ATOM 764 CD2 LEU A 99 49.059 29.447 26.316 1.00 12.66 C ANISOU 764 CD2 LEU A 99 2059 1161 1591 369 154 -332 C ATOM 765 N LEU A 100 49.926 26.978 22.299 1.00 10.61 N ANISOU 765 N LEU A 100 1889 957 1187 322 432 209 N ATOM 766 CA LEU A 100 50.591 26.224 21.238 1.00 11.27 C ANISOU 766 CA LEU A 100 1953 1616 712 215 203 114 C ATOM 767 C LEU A 100 52.053 26.146 21.681 1.00 11.24 C ANISOU 767 C LEU A 100 1921 1259 1089 -22 136 57 C ATOM 768 O LEU A 100 52.724 27.180 21.765 1.00 11.39 O ANISOU 768 O LEU A 100 2149 1018 1160 35 446 114 O ATOM 769 CB LEU A 100 50.480 26.925 19.896 1.00 12.07 C ANISOU 769 CB LEU A 100 1955 1982 649 342 227 232 C ATOM 770 CG LEU A 100 51.018 26.167 18.669 1.00 13.12 C ANISOU 770 CG LEU A 100 1955 2115 914 26 212 -134 C ATOM 771 CD1 LEU A 100 52.528 26.020 18.724 1.00 15.27 C ANISOU 771 CD1 LEU A 100 1983 2732 1087 146 302 -137 C ATOM 772 CD2 LEU A 100 50.352 24.815 18.500 1.00 15.28 C ANISOU 772 CD2 LEU A 100 2384 2052 1369 25 140 -201 C ATOM 773 N MET A 101 52.470 24.962 22.104 1.00 10.51 N ANISOU 773 N MET A 101 1185 1711 1096 304 161 242 N ATOM 774 CA MET A 101 53.783 24.799 22.699 1.00 10.35 C ANISOU 774 CA MET A 101 1280 1562 1090 61 -56 170 C ATOM 775 C MET A 101 54.666 23.862 21.890 1.00 10.97 C ANISOU 775 C MET A 101 1360 1653 1154 115 -212 21 C ATOM 776 O MET A 101 54.171 22.997 21.183 1.00 12.58 O ANISOU 776 O MET A 101 1582 1821 1379 -28 -478 -55 O ATOM 777 CB MET A 101 53.655 24.146 24.092 1.00 10.36 C ANISOU 777 CB MET A 101 1266 1594 1075 276 121 83 C ATOM 778 CG MET A 101 52.849 24.925 25.128 1.00 10.47 C ANISOU 778 CG MET A 101 1451 1105 1423 124 213 -58 C ATOM 779 SD MET A 101 53.467 26.589 25.421 1.00 11.03 S ANISOU 779 SD MET A 101 1676 1226 1289 8 80 -146 S ATOM 780 CE MET A 101 55.144 26.221 25.941 1.00 12.41 C ANISOU 780 CE MET A 101 1967 1258 1491 158 -286 -258 C ATOM 781 N TYR A 102 55.973 24.004 22.083 1.00 11.94 N ANISOU 781 N TYR A 102 1308 1673 1554 -128 -16 -255 N ATOM 782 CA TYR A 102 56.920 23.020 21.584 1.00 11.17 C ANISOU 782 CA TYR A 102 1454 1584 1205 -48 103 40 C ATOM 783 C TYR A 102 57.319 22.201 22.820 1.00 11.10 C ANISOU 783 C TYR A 102 1566 1312 1341 -19 -140 -73 C ATOM 784 O TYR A 102 57.380 22.733 23.941 1.00 11.17 O ANISOU 784 O TYR A 102 1492 1536 1217 337 -50 12 O ATOM 785 CB TYR A 102 58.083 23.651 20.835 1.00 12.52 C ANISOU 785 CB TYR A 102 1473 2051 1234 5 254 162 C ATOM 786 CG TYR A 102 57.610 24.061 19.454 1.00 12.79 C ANISOU 786 CG TYR A 102 1925 1683 1254 176 133 33 C ATOM 787 CD1 TYR A 102 57.649 23.152 18.397 1.00 13.80 C ANISOU 787 CD1 TYR A 102 2286 1669 1287 246 124 11 C ATOM 788 CD2 TYR A 102 57.117 25.331 19.221 1.00 12.44 C ANISOU 788 CD2 TYR A 102 1822 1885 1021 431 293 84 C ATOM 789 CE1 TYR A 102 57.186 23.515 17.137 1.00 12.80 C ANISOU 789 CE1 TYR A 102 2100 1780 985 216 492 -34 C ATOM 790 CE2 TYR A 102 56.667 25.693 17.963 1.00 13.32 C ANISOU 790 CE2 TYR A 102 2042 2133 887 163 217 50 C ATOM 791 CZ TYR A 102 56.709 24.780 16.932 1.00 14.00 C ANISOU 791 CZ TYR A 102 2138 1961 1221 384 45 -36 C ATOM 792 OH TYR A 102 56.273 25.140 15.665 1.00 15.65 O ANISOU 792 OH TYR A 102 2682 2140 1126 191 -83 -100 O ATOM 793 N ALA A 103 57.540 20.916 22.636 1.00 10.40 N ANISOU 793 N ALA A 103 1613 1267 1073 93 -67 122 N ATOM 794 CA ALA A 103 57.768 19.977 23.713 1.00 9.66 C ANISOU 794 CA ALA A 103 1679 1027 964 -45 -160 -75 C ATOM 795 C ALA A 103 58.849 20.399 24.694 1.00 9.87 C ANISOU 795 C ALA A 103 1630 955 1164 -297 -99 -85 C ATOM 796 O ALA A 103 58.635 20.173 25.897 1.00 9.83 O ANISOU 796 O ALA A 103 1553 1223 958 -235 -247 -191 O ATOM 797 CB ALA A 103 58.153 18.609 23.147 1.00 9.29 C ANISOU 797 CB ALA A 103 1423 942 1165 -135 267 23 C ATOM 798 N ASN A 104 59.970 20.931 24.218 1.00 10.18 N ANISOU 798 N ASN A 104 1426 1234 1207 -265 -73 -415 N ATOM 799 CA ASN A 104 61.016 21.197 25.209 1.00 9.63 C ANISOU 799 CA ASN A 104 1196 1153 1311 -137 -111 -260 C ATOM 800 C ASN A 104 60.532 22.169 26.279 1.00 10.14 C ANISOU 800 C ASN A 104 1463 1160 1228 -74 -91 -162 C ATOM 801 O ASN A 104 60.989 22.060 27.420 1.00 11.31 O ANISOU 801 O ASN A 104 1764 1292 1240 -214 -217 -158 O ATOM 802 CB ASN A 104 62.325 21.679 24.573 1.00 9.91 C ANISOU 802 CB ASN A 104 1369 1069 1328 -175 48 -243 C ATOM 803 CG ASN A 104 63.441 21.463 25.581 1.00 11.22 C ANISOU 803 CG ASN A 104 1419 1202 1642 -13 -94 -459 C ATOM 804 OD1 ASN A 104 63.601 20.340 26.079 1.00 12.47 O ANISOU 804 OD1 ASN A 104 1601 1253 1885 41 -620 -469 O ATOM 805 ND2 ASN A 104 64.167 22.534 25.907 1.00 12.10 N ANISOU 805 ND2 ASN A 104 1351 1116 2129 108 -128 -690 N ATOM 806 N LEU A 105 59.722 23.137 25.890 1.00 9.54 N ANISOU 806 N LEU A 105 1662 636 1327 -115 49 -307 N ATOM 807 CA LEU A 105 59.241 24.111 26.875 1.00 9.75 C ANISOU 807 CA LEU A 105 1517 1012 1175 76 28 -289 C ATOM 808 C LEU A 105 58.316 23.494 27.910 1.00 10.76 C ANISOU 808 C LEU A 105 1913 946 1231 -315 15 -292 C ATOM 809 O LEU A 105 58.206 24.018 29.037 1.00 12.16 O ANISOU 809 O LEU A 105 1629 1596 1394 -330 231 -658 O ATOM 810 CB LEU A 105 58.608 25.333 26.238 1.00 10.36 C ANISOU 810 CB LEU A 105 1532 705 1699 -178 70 -142 C ATOM 811 CG LEU A 105 59.546 26.175 25.363 1.00 11.24 C ANISOU 811 CG LEU A 105 1393 824 2053 -65 24 163 C ATOM 812 CD1 LEU A 105 58.777 27.388 24.856 1.00 12.90 C ANISOU 812 CD1 LEU A 105 1565 952 2383 196 259 259 C ATOM 813 CD2 LEU A 105 60.782 26.628 26.122 1.00 13.36 C ANISOU 813 CD2 LEU A 105 1638 1000 2437 -257 -195 145 C ATOM 814 N VAL A 106 57.635 22.409 27.541 1.00 9.39 N ANISOU 814 N VAL A 106 1404 979 1183 -370 35 10 N ATOM 815 CA VAL A 106 56.740 21.759 28.504 1.00 9.33 C ANISOU 815 CA VAL A 106 1360 975 1211 -341 74 -46 C ATOM 816 C VAL A 106 57.513 20.798 29.395 1.00 10.23 C ANISOU 816 C VAL A 106 1012 1612 1265 -56 -14 -91 C ATOM 817 O VAL A 106 57.298 20.669 30.604 1.00 12.07 O ANISOU 817 O VAL A 106 1515 1751 1321 -107 165 -17 O ATOM 818 CB VAL A 106 55.667 20.985 27.703 1.00 9.89 C ANISOU 818 CB VAL A 106 1032 1339 1385 -397 -15 248 C ATOM 819 CG1 VAL A 106 54.780 20.168 28.621 1.00 11.19 C ANISOU 819 CG1 VAL A 106 1456 1450 1346 -625 300 -1 C ATOM 820 CG2 VAL A 106 54.870 21.966 26.851 1.00 11.29 C ANISOU 820 CG2 VAL A 106 1119 1723 1447 -192 -87 317 C ATOM 821 N PHE A 107 58.459 20.074 28.777 1.00 9.92 N ANISOU 821 N PHE A 107 1711 1161 898 146 -38 -122 N ATOM 822 CA PHE A 107 59.237 19.060 29.490 1.00 11.57 C ANISOU 822 CA PHE A 107 1614 1189 1591 33 -11 221 C ATOM 823 C PHE A 107 60.356 19.599 30.364 1.00 14.26 C ANISOU 823 C PHE A 107 1986 2014 1417 150 -299 82 C ATOM 824 O PHE A 107 60.687 19.042 31.411 1.00 13.44 O ANISOU 824 O PHE A 107 1676 2201 1230 36 -322 -66 O ATOM 825 CB PHE A 107 59.837 18.115 28.425 1.00 13.75 C ANISOU 825 CB PHE A 107 1640 1845 1739 294 287 194 C ATOM 826 CG PHE A 107 60.772 17.071 28.964 1.00 12.70 C ANISOU 826 CG PHE A 107 1731 1481 1612 119 6 -44 C ATOM 827 CD1 PHE A 107 60.272 15.900 29.494 1.00 11.89 C ANISOU 827 CD1 PHE A 107 1662 1563 1292 191 115 30 C ATOM 828 CD2 PHE A 107 62.146 17.252 28.928 1.00 15.30 C ANISOU 828 CD2 PHE A 107 1787 1590 2438 32 23 257 C ATOM 829 CE1 PHE A 107 61.101 14.909 29.995 1.00 11.53 C ANISOU 829 CE1 PHE A 107 1794 1062 1526 167 442 -74 C ATOM 830 CE2 PHE A 107 62.976 16.269 29.442 1.00 13.89 C ANISOU 830 CE2 PHE A 107 1213 1603 2461 -58 -175 -79 C ATOM 831 CZ PHE A 107 62.460 15.109 29.974 1.00 12.60 C ANISOU 831 CZ PHE A 107 1753 1535 1498 245 -92 -22 C ATOM 832 N ASN A 108 61.008 20.647 29.913 1.00 17.05 N ANISOU 832 N ASN A 108 1981 2458 2038 -240 -531 316 N ATOM 833 CA ASN A 108 62.174 21.310 30.446 1.00 21.83 C ANISOU 833 CA ASN A 108 2715 2906 2674 -742 -598 -49 C ATOM 834 C ASN A 108 62.411 21.103 31.934 1.00 22.37 C ANISOU 834 C ASN A 108 2886 2901 2711 -328 -386 144 C ATOM 835 O ASN A 108 63.393 20.538 32.455 1.00 23.25 O ANISOU 835 O ASN A 108 3083 3400 2351 -597 -832 394 O ATOM 836 CB ASN A 108 62.033 22.854 30.234 1.00 23.01 C ANISOU 836 CB ASN A 108 2932 2885 2927 63 -244 -648 C ATOM 837 CG ASN A 108 63.242 23.617 30.743 1.00 24.39 C ANISOU 837 CG ASN A 108 2932 3004 3330 -113 -328 -126 C ATOM 838 OD1 ASN A 108 64.364 23.271 30.452 1.00 22.39 O ANISOU 838 OD1 ASN A 108 2785 2904 2819 -422 -243 72 O ATOM 839 ND2 ASN A 108 63.068 24.690 31.509 1.00 24.83 N ANISOU 839 ND2 ASN A 108 3034 3388 3012 -221 -815 -366 N ATOM 840 N ASN A 109 61.445 21.710 32.618 1.00 20.11 N ANISOU 840 N ASN A 109 3106 2216 2319 -765 -149 61 N ATOM 841 CA ASN A 109 61.541 21.751 34.083 1.00 21.52 C ANISOU 841 CA ASN A 109 3127 2692 2358 -590 -352 -173 C ATOM 842 C ASN A 109 60.438 20.966 34.742 1.00 20.28 C ANISOU 842 C ASN A 109 3130 2284 2289 -410 -166 -349 C ATOM 843 O ASN A 109 60.037 21.209 35.874 1.00 23.72 O ANISOU 843 O ASN A 109 3569 3148 2298 -411 -193 -549 O ATOM 844 CB ASN A 109 61.621 23.233 34.472 1.00 22.80 C ANISOU 844 CB ASN A 109 3219 2656 2790 -338 -321 -198 C ATOM 845 CG ASN A 109 62.908 23.860 33.952 1.00 24.71 C ANISOU 845 CG ASN A 109 3222 3025 3140 -213 -159 -31 C ATOM 846 OD1 ASN A 109 62.931 24.903 33.282 1.00 26.49 O ANISOU 846 OD1 ASN A 109 3518 3279 3267 -408 -286 173 O ATOM 847 ND2 ASN A 109 64.035 23.225 34.260 1.00 21.50 N ANISOU 847 ND2 ASN A 109 2726 2596 2849 -601 -116 -355 N ATOM 848 N GLY A 110 59.911 19.972 34.012 1.00 15.46 N ANISOU 848 N GLY A 110 2025 2340 1508 -337 31 -167 N ATOM 849 CA GLY A 110 58.916 19.075 34.569 1.00 14.47 C ANISOU 849 CA GLY A 110 2087 2187 1223 -235 -30 -53 C ATOM 850 C GLY A 110 57.558 19.188 33.899 1.00 12.68 C ANISOU 850 C GLY A 110 1863 1647 1307 -133 186 -6 C ATOM 851 O GLY A 110 56.953 20.248 33.962 1.00 13.73 O ANISOU 851 O GLY A 110 2201 1706 1309 12 94 -245 O ATOM 852 N ILE A 111 57.108 18.093 33.296 1.00 12.52 N ANISOU 852 N ILE A 111 1429 1759 1568 135 -104 -223 N ATOM 853 CA ILE A 111 55.816 18.112 32.614 1.00 11.67 C ANISOU 853 CA ILE A 111 1544 1595 1297 -93 -145 -137 C ATOM 854 C ILE A 111 54.701 18.460 33.579 1.00 11.92 C ANISOU 854 C ILE A 111 1508 1827 1195 247 -230 106 C ATOM 855 O ILE A 111 53.835 19.284 33.292 1.00 12.91 O ANISOU 855 O ILE A 111 1680 2003 1223 328 -123 607 O ATOM 856 CB ILE A 111 55.554 16.758 31.926 1.00 12.12 C ANISOU 856 CB ILE A 111 1494 1493 1620 -309 -67 -88 C ATOM 857 CG1 ILE A 111 56.523 16.516 30.778 1.00 10.92 C ANISOU 857 CG1 ILE A 111 1612 899 1639 -218 29 128 C ATOM 858 CG2 ILE A 111 54.130 16.684 31.381 1.00 14.06 C ANISOU 858 CG2 ILE A 111 1359 1666 2315 -253 -63 4 C ATOM 859 CD1 ILE A 111 56.387 15.179 30.075 1.00 12.90 C ANISOU 859 CD1 ILE A 111 1951 1286 1664 83 -257 -264 C ATOM 860 N ASP A 112 54.685 17.788 34.738 1.00 14.49 N ANISOU 860 N ASP A 112 2001 2127 1379 93 10 344 N ATOM 861 CA ASP A 112 53.601 18.049 35.684 1.00 13.26 C ANISOU 861 CA ASP A 112 1911 1890 1238 120 -70 572 C ATOM 862 C ASP A 112 53.595 19.505 36.123 1.00 13.42 C ANISOU 862 C ASP A 112 2042 2047 1010 164 125 348 C ATOM 863 O ASP A 112 52.527 20.128 36.148 1.00 14.96 O ANISOU 863 O ASP A 112 1887 2250 1549 134 307 544 O ATOM 864 CB ASP A 112 53.723 17.118 36.898 1.00 16.04 C ANISOU 864 CB ASP A 112 2497 2236 1361 324 -255 759 C ATOM 865 CG ASP A 112 52.418 17.070 37.674 1.00 19.81 C ANISOU 865 CG ASP A 112 2842 2735 1949 -285 30 521 C ATOM 866 OD1 ASP A 112 51.481 16.398 37.198 1.00 20.33 O ANISOU 866 OD1 ASP A 112 3097 2140 2486 -233 -439 811 O ATOM 867 OD2 ASP A 112 52.420 17.741 38.723 1.00 24.94 O ANISOU 867 OD2 ASP A 112 3984 3093 2400 5 88 65 O ATOM 868 N ALA A 113 54.762 20.061 36.414 1.00 13.84 N ANISOU 868 N ALA A 113 2431 1781 1046 -72 -7 250 N ATOM 869 CA ALA A 113 54.864 21.453 36.827 1.00 12.63 C ANISOU 869 CA ALA A 113 2094 1749 955 0 136 202 C ATOM 870 C ALA A 113 54.341 22.399 35.738 1.00 13.42 C ANISOU 870 C ALA A 113 2267 1836 998 286 38 113 C ATOM 871 O ALA A 113 53.756 23.439 36.060 1.00 15.12 O ANISOU 871 O ALA A 113 2629 1996 1122 325 128 -159 O ATOM 872 CB ALA A 113 56.276 21.841 37.212 1.00 15.73 C ANISOU 872 CB ALA A 113 2323 2377 1275 -8 -266 -78 C ATOM 873 N PHE A 114 54.598 22.059 34.462 1.00 12.74 N ANISOU 873 N PHE A 114 2043 1793 1004 236 -89 39 N ATOM 874 CA PHE A 114 54.106 22.944 33.399 1.00 12.03 C ANISOU 874 CA PHE A 114 2023 1467 1079 317 154 29 C ATOM 875 C PHE A 114 52.583 23.017 33.398 1.00 11.68 C ANISOU 875 C PHE A 114 2005 1248 1183 95 196 -80 C ATOM 876 O PHE A 114 51.992 24.110 33.299 1.00 12.37 O ANISOU 876 O PHE A 114 2372 1139 1189 130 296 -254 O ATOM 877 CB PHE A 114 54.624 22.439 32.041 1.00 11.74 C ANISOU 877 CB PHE A 114 1965 1452 1045 -19 373 149 C ATOM 878 CG PHE A 114 54.175 23.336 30.912 1.00 10.42 C ANISOU 878 CG PHE A 114 1533 1420 1008 67 295 16 C ATOM 879 CD1 PHE A 114 54.939 24.439 30.585 1.00 10.91 C ANISOU 879 CD1 PHE A 114 1559 1329 1257 49 -36 120 C ATOM 880 CD2 PHE A 114 53.000 23.089 30.226 1.00 11.38 C ANISOU 880 CD2 PHE A 114 1528 1708 1088 85 268 -98 C ATOM 881 CE1 PHE A 114 54.512 25.296 29.572 1.00 11.67 C ANISOU 881 CE1 PHE A 114 1989 1557 889 84 -151 18 C ATOM 882 CE2 PHE A 114 52.569 23.957 29.234 1.00 11.80 C ANISOU 882 CE2 PHE A 114 1600 1566 1316 -293 -271 -137 C ATOM 883 CZ PHE A 114 53.329 25.050 28.894 1.00 11.53 C ANISOU 883 CZ PHE A 114 1628 1436 1319 -42 125 -15 C ATOM 884 N TYR A 115 51.947 21.844 33.438 1.00 10.89 N ANISOU 884 N TYR A 115 1933 1420 783 -21 463 148 N ATOM 885 CA TYR A 115 50.493 21.789 33.430 1.00 10.86 C ANISOU 885 CA TYR A 115 1960 1090 1075 -172 392 168 C ATOM 886 C TYR A 115 49.911 22.417 34.696 1.00 12.27 C ANISOU 886 C TYR A 115 2274 1352 1035 193 225 53 C ATOM 887 O TYR A 115 48.854 23.040 34.606 1.00 13.35 O ANISOU 887 O TYR A 115 2373 1772 927 359 599 186 O ATOM 888 CB TYR A 115 49.956 20.393 33.139 1.00 11.79 C ANISOU 888 CB TYR A 115 2481 1034 965 -145 413 176 C ATOM 889 CG TYR A 115 50.225 20.008 31.689 1.00 10.77 C ANISOU 889 CG TYR A 115 1826 1340 924 16 277 134 C ATOM 890 CD1 TYR A 115 49.327 20.395 30.702 1.00 12.95 C ANISOU 890 CD1 TYR A 115 1894 1814 1213 295 171 201 C ATOM 891 CD2 TYR A 115 51.332 19.266 31.325 1.00 11.20 C ANISOU 891 CD2 TYR A 115 1676 1564 1017 74 171 198 C ATOM 892 CE1 TYR A 115 49.541 20.059 29.370 1.00 11.93 C ANISOU 892 CE1 TYR A 115 2043 1261 1231 -63 202 187 C ATOM 893 CE2 TYR A 115 51.550 18.930 30.009 1.00 11.16 C ANISOU 893 CE2 TYR A 115 1690 1388 1162 -262 213 36 C ATOM 894 CZ TYR A 115 50.656 19.323 29.040 1.00 11.12 C ANISOU 894 CZ TYR A 115 1911 1143 1170 -260 150 65 C ATOM 895 OH TYR A 115 50.892 18.973 27.726 1.00 12.40 O ANISOU 895 OH TYR A 115 2037 1645 1031 268 -74 140 O ATOM 896 N ALA A 116 50.591 22.273 35.826 1.00 14.00 N ANISOU 896 N ALA A 116 2622 1952 746 264 358 9 N ATOM 897 CA ALA A 116 50.123 22.930 37.056 1.00 13.87 C ANISOU 897 CA ALA A 116 2451 1773 1047 482 85 -250 C ATOM 898 C ALA A 116 50.204 24.445 36.895 1.00 13.62 C ANISOU 898 C ALA A 116 2208 1852 1116 162 383 -130 C ATOM 899 O ALA A 116 49.315 25.144 37.369 1.00 15.39 O ANISOU 899 O ALA A 116 2231 2149 1466 365 485 -131 O ATOM 900 CB ALA A 116 50.925 22.452 38.257 1.00 16.24 C ANISOU 900 CB ALA A 116 2908 2412 850 481 132 -62 C ATOM 901 N ARG A 117 51.227 24.971 36.227 1.00 12.60 N ANISOU 901 N ARG A 117 2291 1484 1014 -80 241 -124 N ATOM 902 CA ARG A 117 51.351 26.415 36.030 1.00 12.27 C ANISOU 902 CA ARG A 117 2118 1451 1093 178 -67 -188 C ATOM 903 C ARG A 117 50.219 26.880 35.111 1.00 12.91 C ANISOU 903 C ARG A 117 2038 1582 1285 81 -240 -258 C ATOM 904 O ARG A 117 49.663 27.954 35.303 1.00 13.48 O ANISOU 904 O ARG A 117 2430 1463 1227 20 -79 -305 O ATOM 905 CB ARG A 117 52.702 26.818 35.467 1.00 14.09 C ANISOU 905 CB ARG A 117 2113 2095 1145 -22 -128 -262 C ATOM 906 CG ARG A 117 52.936 28.309 35.343 1.00 19.24 C ANISOU 906 CG ARG A 117 2738 2196 2378 -56 -142 4 C ATOM 907 CD ARG A 117 53.275 28.959 36.688 1.00 23.16 C ANISOU 907 CD ARG A 117 3549 2844 2407 -95 98 -298 C ATOM 908 NE ARG A 117 53.524 30.385 36.487 1.00 23.95 N ANISOU 908 NE ARG A 117 3621 2850 2630 -87 96 -176 N ATOM 909 CZ ARG A 117 52.827 31.413 36.934 1.00 24.95 C ANISOU 909 CZ ARG A 117 3392 3085 3005 -98 159 -284 C ATOM 910 NH1 ARG A 117 51.762 31.265 37.718 1.00 27.00 N ANISOU 910 NH1 ARG A 117 3544 3671 3042 -248 200 -221 N ATOM 911 NH2 ARG A 117 53.216 32.647 36.612 1.00 25.35 N ANISOU 911 NH2 ARG A 117 3634 3128 2869 -90 135 -176 N ATOM 912 N CYS A 118 49.908 26.094 34.070 1.00 12.22 N ANISOU 912 N CYS A 118 2259 1293 1089 46 -98 -73 N ATOM 913 CA CYS A 118 48.795 26.445 33.188 1.00 10.40 C ANISOU 913 CA CYS A 118 1775 1003 1173 -291 25 -277 C ATOM 914 C CYS A 118 47.502 26.558 33.992 1.00 10.59 C ANISOU 914 C CYS A 118 1923 872 1230 11 115 -160 C ATOM 915 O CYS A 118 46.704 27.475 33.818 1.00 11.49 O ANISOU 915 O CYS A 118 2153 910 1303 85 -8 -169 O ATOM 916 CB CYS A 118 48.629 25.360 32.122 1.00 10.27 C ANISOU 916 CB CYS A 118 1945 1193 763 -336 -67 -150 C ATOM 917 SG CYS A 118 49.918 25.346 30.860 1.00 11.67 S ANISOU 917 SG CYS A 118 2458 1181 794 -352 186 -320 S ATOM 918 N GLU A 119 47.275 25.566 34.875 1.00 13.28 N ANISOU 918 N GLU A 119 2295 1638 1113 -299 473 28 N ATOM 919 CA GLU A 119 46.062 25.590 35.675 1.00 12.87 C ANISOU 919 CA GLU A 119 1992 1377 1521 -15 373 -284 C ATOM 920 C GLU A 119 46.021 26.829 36.568 1.00 12.15 C ANISOU 920 C GLU A 119 1868 1386 1362 53 263 -259 C ATOM 921 O GLU A 119 44.971 27.463 36.706 1.00 14.57 O ANISOU 921 O GLU A 119 1821 1801 1915 156 152 -453 O ATOM 922 CB GLU A 119 45.979 24.303 36.506 1.00 14.11 C ANISOU 922 CB GLU A 119 2595 1630 1134 -128 579 -216 C ATOM 923 CG GLU A 119 44.664 24.231 37.263 1.00 15.73 C ANISOU 923 CG GLU A 119 2616 1757 1604 -80 717 -377 C ATOM 924 CD GLU A 119 44.541 22.997 38.137 1.00 16.61 C ANISOU 924 CD GLU A 119 2916 2120 1276 -259 366 -223 C ATOM 925 OE1 GLU A 119 45.562 22.387 38.511 1.00 18.15 O ANISOU 925 OE1 GLU A 119 3470 1755 1671 -126 281 74 O ATOM 926 OE2 GLU A 119 43.374 22.664 38.441 1.00 21.19 O ANISOU 926 OE2 GLU A 119 3245 2938 1868 -632 715 -737 O ATOM 927 N GLN A 120 47.157 27.154 37.163 1.00 12.56 N ANISOU 927 N GLN A 120 2095 1413 1265 112 104 -347 N ATOM 928 CA GLN A 120 47.217 28.320 38.049 1.00 14.27 C ANISOU 928 CA GLN A 120 2235 1568 1618 384 307 -621 C ATOM 929 C GLN A 120 46.847 29.620 37.351 1.00 14.38 C ANISOU 929 C GLN A 120 2272 1732 1459 99 205 -380 C ATOM 930 O GLN A 120 46.172 30.479 37.935 1.00 16.55 O ANISOU 930 O GLN A 120 3152 1565 1570 140 324 -636 O ATOM 931 CB GLN A 120 48.610 28.416 38.674 1.00 18.34 C ANISOU 931 CB GLN A 120 2535 2729 1704 396 -59 -225 C ATOM 932 CG GLN A 120 48.799 29.564 39.649 1.00 25.11 C ANISOU 932 CG GLN A 120 3683 3193 2664 32 -102 -727 C ATOM 933 CD GLN A 120 50.178 29.626 40.266 1.00 30.97 C ANISOU 933 CD GLN A 120 3696 4359 3712 30 -248 -149 C ATOM 934 OE1 GLN A 120 51.168 29.144 39.710 1.00 33.92 O ANISOU 934 OE1 GLN A 120 4081 4950 3859 150 -21 -199 O ATOM 935 NE2 GLN A 120 50.262 30.233 41.452 1.00 35.34 N ANISOU 935 NE2 GLN A 120 4646 4756 4025 -42 -87 -428 N ATOM 936 N VAL A 121 47.303 29.828 36.115 1.00 12.30 N ANISOU 936 N VAL A 121 2123 1249 1304 -21 -58 -373 N ATOM 937 CA VAL A 121 47.030 31.075 35.424 1.00 13.77 C ANISOU 937 CA VAL A 121 2175 1331 1726 -7 275 -153 C ATOM 938 C VAL A 121 45.703 31.046 34.693 1.00 14.24 C ANISOU 938 C VAL A 121 2014 1362 2035 110 299 47 C ATOM 939 O VAL A 121 45.275 32.109 34.235 1.00 17.07 O ANISOU 939 O VAL A 121 2861 683 2941 -221 85 -108 O ATOM 940 CB VAL A 121 48.141 31.504 34.459 1.00 14.39 C ANISOU 940 CB VAL A 121 2408 1770 1292 -56 265 -73 C ATOM 941 CG1 VAL A 121 49.476 31.603 35.192 1.00 17.87 C ANISOU 941 CG1 VAL A 121 2563 2600 1627 -62 61 -185 C ATOM 942 CG2 VAL A 121 48.250 30.558 33.272 1.00 14.55 C ANISOU 942 CG2 VAL A 121 2600 1653 1275 -83 452 -19 C ATOM 943 N GLY A 122 45.048 29.892 34.600 1.00 14.47 N ANISOU 943 N GLY A 122 2176 1674 1650 -87 197 -428 N ATOM 944 CA GLY A 122 43.752 29.841 33.959 1.00 13.62 C ANISOU 944 CA GLY A 122 2102 1661 1412 -377 315 -333 C ATOM 945 C GLY A 122 43.749 29.487 32.480 1.00 12.98 C ANISOU 945 C GLY A 122 2102 1392 1438 -10 28 -371 C ATOM 946 O GLY A 122 42.752 29.769 31.805 1.00 12.68 O ANISOU 946 O GLY A 122 2161 1181 1477 339 117 -393 O ATOM 947 N VAL A 123 44.811 28.858 31.990 1.00 11.82 N ANISOU 947 N VAL A 123 2160 974 1357 -240 354 -128 N ATOM 948 CA VAL A 123 44.814 28.327 30.624 1.00 11.83 C ANISOU 948 CA VAL A 123 1811 1318 1367 -142 -113 -256 C ATOM 949 C VAL A 123 43.842 27.152 30.564 1.00 10.23 C ANISOU 949 C VAL A 123 1873 1070 943 -18 260 -273 C ATOM 950 O VAL A 123 43.694 26.413 31.551 1.00 12.17 O ANISOU 950 O VAL A 123 2106 930 1587 117 161 79 O ATOM 951 CB VAL A 123 46.248 27.853 30.303 1.00 11.24 C ANISOU 951 CB VAL A 123 1949 1066 1256 -247 222 -375 C ATOM 952 CG1 VAL A 123 46.311 26.835 29.186 1.00 11.70 C ANISOU 952 CG1 VAL A 123 1811 1116 1520 369 176 -477 C ATOM 953 CG2 VAL A 123 47.127 29.074 30.012 1.00 13.43 C ANISOU 953 CG2 VAL A 123 2115 1590 1399 -545 561 -279 C ATOM 954 N ASP A 124 43.238 26.910 29.402 1.00 10.50 N ANISOU 954 N ASP A 124 1734 1092 1162 -140 168 -438 N ATOM 955 CA ASP A 124 42.293 25.818 29.235 1.00 11.40 C ANISOU 955 CA ASP A 124 1498 1255 1577 -143 171 -264 C ATOM 956 C ASP A 124 42.820 24.613 28.472 1.00 11.40 C ANISOU 956 C ASP A 124 1638 1229 1466 -218 331 -212 C ATOM 957 O ASP A 124 42.370 23.499 28.710 1.00 11.84 O ANISOU 957 O ASP A 124 1599 1025 1875 -75 213 -220 O ATOM 958 CB ASP A 124 41.053 26.329 28.468 1.00 11.58 C ANISOU 958 CB ASP A 124 1447 1186 1765 119 356 -110 C ATOM 959 CG ASP A 124 40.386 27.438 29.277 1.00 11.98 C ANISOU 959 CG ASP A 124 1646 1319 1584 275 327 -22 C ATOM 960 OD1 ASP A 124 39.871 27.091 30.357 1.00 13.69 O ANISOU 960 OD1 ASP A 124 2393 1321 1488 514 570 -49 O ATOM 961 OD2 ASP A 124 40.441 28.582 28.819 1.00 12.38 O ANISOU 961 OD2 ASP A 124 1826 1213 1667 472 473 -82 O ATOM 962 N SER A 125 43.731 24.816 27.538 1.00 9.32 N ANISOU 962 N SER A 125 1450 679 1411 51 295 -107 N ATOM 963 CA SER A 125 44.269 23.715 26.752 1.00 8.39 C ANISOU 963 CA SER A 125 1289 974 924 156 181 -114 C ATOM 964 C SER A 125 45.717 23.958 26.348 1.00 9.46 C ANISOU 964 C SER A 125 1285 991 1319 256 237 -163 C ATOM 965 O SER A 125 46.216 25.079 26.342 1.00 10.04 O ANISOU 965 O SER A 125 1516 1077 1221 138 151 15 O ATOM 966 CB SER A 125 43.453 23.506 25.453 1.00 10.15 C ANISOU 966 CB SER A 125 1841 1154 860 53 61 -29 C ATOM 967 OG SER A 125 43.705 24.549 24.508 1.00 10.80 O ANISOU 967 OG SER A 125 2023 1041 1040 -316 -135 -108 O ATOM 968 N VAL A 126 46.367 22.843 25.966 1.00 9.25 N ANISOU 968 N VAL A 126 1233 1009 1272 310 -175 -326 N ATOM 969 CA VAL A 126 47.741 22.905 25.495 1.00 9.48 C ANISOU 969 CA VAL A 126 1390 1310 902 115 -63 -86 C ATOM 970 C VAL A 126 47.874 21.937 24.318 1.00 9.27 C ANISOU 970 C VAL A 126 1546 1059 919 13 41 -7 C ATOM 971 O VAL A 126 47.507 20.781 24.448 1.00 9.05 O ANISOU 971 O VAL A 126 1647 845 945 381 -261 -132 O ATOM 972 CB VAL A 126 48.746 22.484 26.581 1.00 9.14 C ANISOU 972 CB VAL A 126 1327 1404 741 8 -72 -263 C ATOM 973 CG1 VAL A 126 50.161 22.356 26.040 1.00 9.81 C ANISOU 973 CG1 VAL A 126 1291 1233 1204 -86 31 -171 C ATOM 974 CG2 VAL A 126 48.743 23.512 27.717 1.00 10.69 C ANISOU 974 CG2 VAL A 126 2023 1003 1036 -66 -4 -295 C ATOM 975 N LEU A 127 48.365 22.452 23.193 1.00 8.98 N ANISOU 975 N LEU A 127 1505 1094 812 124 32 -64 N ATOM 976 CA LEU A 127 48.673 21.658 22.015 1.00 9.11 C ANISOU 976 CA LEU A 127 1489 1122 849 755 -262 -25 C ATOM 977 C LEU A 127 50.201 21.639 21.906 1.00 9.76 C ANISOU 977 C LEU A 127 1545 1129 1033 141 51 -74 C ATOM 978 O LEU A 127 50.791 22.702 21.729 1.00 10.52 O ANISOU 978 O LEU A 127 1638 984 1377 229 -1 -186 O ATOM 979 CB LEU A 127 48.073 22.294 20.755 1.00 10.07 C ANISOU 979 CB LEU A 127 1538 1761 527 162 -403 -47 C ATOM 980 CG LEU A 127 48.037 21.419 19.492 1.00 11.73 C ANISOU 980 CG LEU A 127 1824 2129 506 505 -248 -130 C ATOM 981 CD1 LEU A 127 47.315 22.192 18.395 1.00 11.74 C ANISOU 981 CD1 LEU A 127 1921 1880 661 581 -188 -71 C ATOM 982 CD2 LEU A 127 49.415 20.966 19.053 1.00 13.69 C ANISOU 982 CD2 LEU A 127 1940 2283 977 362 69 -342 C ATOM 983 N VAL A 128 50.813 20.460 22.074 1.00 9.79 N ANISOU 983 N VAL A 128 1278 1260 1183 217 -367 -99 N ATOM 984 CA VAL A 128 52.274 20.380 21.958 1.00 10.74 C ANISOU 984 CA VAL A 128 1368 1435 1276 102 32 -40 C ATOM 985 C VAL A 128 52.572 19.926 20.527 1.00 10.58 C ANISOU 985 C VAL A 128 1384 1525 1113 -77 -55 87 C ATOM 986 O VAL A 128 52.288 18.791 20.155 1.00 11.55 O ANISOU 986 O VAL A 128 1694 1722 974 9 -33 -293 O ATOM 987 CB VAL A 128 52.904 19.455 22.992 1.00 11.05 C ANISOU 987 CB VAL A 128 1519 1649 1032 238 30 -124 C ATOM 988 CG1 VAL A 128 54.416 19.663 23.017 1.00 12.06 C ANISOU 988 CG1 VAL A 128 1582 1942 1058 34 183 -346 C ATOM 989 CG2 VAL A 128 52.365 19.717 24.404 1.00 12.15 C ANISOU 989 CG2 VAL A 128 1630 1873 1112 -84 160 -267 C ATOM 990 N ALA A 129 53.066 20.849 19.705 1.00 10.21 N ANISOU 990 N ALA A 129 1422 1387 1070 7 -65 21 N ATOM 991 CA ALA A 129 53.167 20.581 18.272 1.00 10.47 C ANISOU 991 CA ALA A 129 1708 1308 962 278 -70 300 C ATOM 992 C ALA A 129 53.986 19.370 17.873 1.00 10.64 C ANISOU 992 C ALA A 129 1526 1458 1060 167 -253 -170 C ATOM 993 O ALA A 129 53.621 18.715 16.888 1.00 12.31 O ANISOU 993 O ALA A 129 1492 2155 1031 666 -301 -578 O ATOM 994 CB ALA A 129 53.674 21.839 17.588 1.00 12.78 C ANISOU 994 CB ALA A 129 2120 1517 1216 -64 82 353 C ATOM 995 N ASP A 130 55.060 19.098 18.592 1.00 10.16 N ANISOU 995 N ASP A 130 1218 1326 1316 302 -58 31 N ATOM 996 CA ASP A 130 55.961 18.010 18.258 1.00 10.13 C ANISOU 996 CA ASP A 130 1532 1291 1025 303 -23 -146 C ATOM 997 C ASP A 130 55.850 16.796 19.169 1.00 9.92 C ANISOU 997 C ASP A 130 1269 1613 888 -78 -35 -79 C ATOM 998 O ASP A 130 56.791 16.004 19.299 1.00 12.41 O ANISOU 998 O ASP A 130 1453 2062 1200 223 107 64 O ATOM 999 CB ASP A 130 57.400 18.519 18.191 1.00 10.95 C ANISOU 999 CB ASP A 130 1597 1577 986 110 -335 -125 C ATOM 1000 CG ASP A 130 57.868 19.272 19.412 1.00 10.27 C ANISOU 1000 CG ASP A 130 1419 1654 827 248 -94 -157 C ATOM 1001 OD1 ASP A 130 57.052 19.745 20.224 1.00 11.56 O ANISOU 1001 OD1 ASP A 130 1413 2204 776 108 48 -256 O ATOM 1002 OD2 ASP A 130 59.105 19.414 19.576 1.00 13.61 O ANISOU 1002 OD2 ASP A 130 1348 2820 1003 285 41 -241 O ATOM 1003 N VAL A 131 54.661 16.602 19.730 1.00 10.02 N ANISOU 1003 N VAL A 131 1228 1529 1049 72 37 151 N ATOM 1004 CA VAL A 131 54.376 15.386 20.502 1.00 10.63 C ANISOU 1004 CA VAL A 131 1676 1259 1102 -38 62 -51 C ATOM 1005 C VAL A 131 53.230 14.664 19.815 1.00 9.77 C ANISOU 1005 C VAL A 131 1325 1142 1245 185 143 -77 C ATOM 1006 O VAL A 131 52.052 15.032 19.935 1.00 12.60 O ANISOU 1006 O VAL A 131 1341 1804 1641 464 -103 -387 O ATOM 1007 CB VAL A 131 54.009 15.705 21.953 1.00 10.57 C ANISOU 1007 CB VAL A 131 1733 1265 1020 -302 48 -17 C ATOM 1008 CG1 VAL A 131 53.549 14.442 22.679 1.00 12.20 C ANISOU 1008 CG1 VAL A 131 2166 1260 1209 -287 73 39 C ATOM 1009 CG2 VAL A 131 55.176 16.333 22.704 1.00 12.86 C ANISOU 1009 CG2 VAL A 131 1802 1634 1448 -392 -65 -145 C ATOM 1010 N PRO A 132 53.537 13.623 19.045 1.00 9.46 N ANISOU 1010 N PRO A 132 1294 1202 1098 -30 216 -179 N ATOM 1011 CA PRO A 132 52.476 12.868 18.370 1.00 10.44 C ANISOU 1011 CA PRO A 132 1292 1606 1068 -44 24 -86 C ATOM 1012 C PRO A 132 51.723 12.018 19.369 1.00 10.14 C ANISOU 1012 C PRO A 132 1035 1810 1007 -156 -71 -101 C ATOM 1013 O PRO A 132 52.220 11.824 20.489 1.00 10.47 O ANISOU 1013 O PRO A 132 963 1918 1097 -265 -357 -248 O ATOM 1014 CB PRO A 132 53.246 12.057 17.332 1.00 10.43 C ANISOU 1014 CB PRO A 132 1208 1775 978 2 -73 -187 C ATOM 1015 CG PRO A 132 54.541 11.737 18.029 1.00 10.15 C ANISOU 1015 CG PRO A 132 1239 1753 864 174 -25 -464 C ATOM 1016 CD PRO A 132 54.862 13.019 18.785 1.00 9.83 C ANISOU 1016 CD PRO A 132 1422 1225 1088 110 331 -244 C ATOM 1017 N VAL A 133 50.590 11.447 19.001 1.00 10.61 N ANISOU 1017 N VAL A 133 1128 1823 1082 -281 -118 -182 N ATOM 1018 CA VAL A 133 49.848 10.633 19.975 1.00 11.37 C ANISOU 1018 CA VAL A 133 1473 1968 877 -252 -218 4 C ATOM 1019 C VAL A 133 50.720 9.537 20.571 1.00 10.42 C ANISOU 1019 C VAL A 133 1662 1307 992 -348 -225 -349 C ATOM 1020 O VAL A 133 50.598 9.205 21.749 1.00 11.84 O ANISOU 1020 O VAL A 133 1926 1577 996 -247 -188 -265 O ATOM 1021 CB VAL A 133 48.554 10.027 19.417 1.00 13.83 C ANISOU 1021 CB VAL A 133 1536 1931 1787 -62 -500 -184 C ATOM 1022 CG1 VAL A 133 47.516 11.124 19.184 1.00 16.06 C ANISOU 1022 CG1 VAL A 133 1893 1976 2233 95 -459 26 C ATOM 1023 CG2 VAL A 133 48.828 9.209 18.174 1.00 15.81 C ANISOU 1023 CG2 VAL A 133 2408 1976 1622 -274 -324 -107 C ATOM 1024 N GLU A 134 51.605 8.956 19.781 1.00 12.12 N ANISOU 1024 N GLU A 134 1691 1643 1270 -76 -309 -452 N ATOM 1025 CA GLU A 134 52.481 7.891 20.198 1.00 13.65 C ANISOU 1025 CA GLU A 134 2103 1707 1375 289 -104 -643 C ATOM 1026 C GLU A 134 53.378 8.267 21.362 1.00 12.02 C ANISOU 1026 C GLU A 134 2136 1376 1056 213 -92 -183 C ATOM 1027 O GLU A 134 53.747 7.367 22.123 1.00 14.30 O ANISOU 1027 O GLU A 134 2477 852 2103 381 -344 -210 O ATOM 1028 CB GLU A 134 53.358 7.479 19.004 1.00 15.50 C ANISOU 1028 CB GLU A 134 2620 2031 1239 277 55 -616 C ATOM 1029 CG GLU A 134 52.635 6.806 17.861 1.00 17.23 C ANISOU 1029 CG GLU A 134 2573 2120 1854 5 -382 -504 C ATOM 1030 CD GLU A 134 51.927 7.685 16.863 1.00 16.85 C ANISOU 1030 CD GLU A 134 2560 2440 1403 35 -131 -456 C ATOM 1031 OE1 GLU A 134 51.840 8.924 16.973 1.00 15.50 O ANISOU 1031 OE1 GLU A 134 2347 2425 1119 -359 -224 -595 O ATOM 1032 OE2 GLU A 134 51.427 7.136 15.840 1.00 20.28 O ANISOU 1032 OE2 GLU A 134 2944 2534 2229 -401 -428 -896 O ATOM 1033 N GLU A 135 53.706 9.537 21.524 1.00 10.67 N ANISOU 1033 N GLU A 135 1755 1469 831 27 -163 -201 N ATOM 1034 CA GLU A 135 54.583 9.958 22.627 1.00 9.87 C ANISOU 1034 CA GLU A 135 1719 1288 744 108 -33 -249 C ATOM 1035 C GLU A 135 53.823 10.745 23.683 1.00 9.26 C ANISOU 1035 C GLU A 135 1543 1247 729 299 -222 -190 C ATOM 1036 O GLU A 135 54.415 11.323 24.593 1.00 10.58 O ANISOU 1036 O GLU A 135 1746 1546 726 -184 -199 -90 O ATOM 1037 CB GLU A 135 55.665 10.901 22.079 1.00 10.52 C ANISOU 1037 CB GLU A 135 1686 1523 787 -57 -72 -364 C ATOM 1038 CG GLU A 135 56.657 10.267 21.133 1.00 11.21 C ANISOU 1038 CG GLU A 135 1248 1734 1278 385 -22 60 C ATOM 1039 CD GLU A 135 57.608 9.290 21.765 1.00 10.80 C ANISOU 1039 CD GLU A 135 1158 1866 1079 220 -288 69 C ATOM 1040 OE1 GLU A 135 57.544 9.071 23.009 1.00 14.27 O ANISOU 1040 OE1 GLU A 135 1793 2581 1048 527 -258 98 O ATOM 1041 OE2 GLU A 135 58.461 8.711 21.037 1.00 11.49 O ANISOU 1041 OE2 GLU A 135 1429 1847 1090 322 102 506 O ATOM 1042 N SER A 136 52.491 10.787 23.555 1.00 9.28 N ANISOU 1042 N SER A 136 1398 1011 1117 402 65 -140 N ATOM 1043 CA SER A 136 51.716 11.709 24.354 1.00 8.79 C ANISOU 1043 CA SER A 136 934 1505 900 184 119 -256 C ATOM 1044 C SER A 136 51.367 11.301 25.769 1.00 8.99 C ANISOU 1044 C SER A 136 1119 1300 997 102 83 -54 C ATOM 1045 O SER A 136 50.885 12.173 26.504 1.00 10.33 O ANISOU 1045 O SER A 136 1478 1222 1224 119 111 -176 O ATOM 1046 CB SER A 136 50.371 12.011 23.657 1.00 9.93 C ANISOU 1046 CB SER A 136 1155 1543 1075 127 -87 -36 C ATOM 1047 OG SER A 136 49.550 10.866 23.619 1.00 12.50 O ANISOU 1047 OG SER A 136 616 2511 1622 -338 -364 -186 O ATOM 1048 N ALA A 137 51.577 10.069 26.189 1.00 10.06 N ANISOU 1048 N ALA A 137 1457 1328 1040 -122 -62 67 N ATOM 1049 CA ALA A 137 51.064 9.643 27.478 1.00 10.01 C ANISOU 1049 CA ALA A 137 1449 1364 992 -258 11 -49 C ATOM 1050 C ALA A 137 51.372 10.567 28.640 1.00 9.45 C ANISOU 1050 C ALA A 137 1574 1203 813 -209 -29 76 C ATOM 1051 O ALA A 137 50.439 10.978 29.343 1.00 10.60 O ANISOU 1051 O ALA A 137 1477 1386 1165 -207 52 46 O ATOM 1052 CB ALA A 137 51.450 8.202 27.772 1.00 11.99 C ANISOU 1052 CB ALA A 137 2342 1434 781 34 615 -26 C ATOM 1053 N PRO A 138 52.618 10.894 28.943 1.00 10.35 N ANISOU 1053 N PRO A 138 1490 1193 1251 2 51 -405 N ATOM 1054 CA PRO A 138 52.878 11.722 30.117 1.00 10.03 C ANISOU 1054 CA PRO A 138 1356 1159 1297 -236 -22 -410 C ATOM 1055 C PRO A 138 52.280 13.108 30.017 1.00 10.73 C ANISOU 1055 C PRO A 138 1581 1334 1159 -106 14 -127 C ATOM 1056 O PRO A 138 51.942 13.717 31.042 1.00 10.53 O ANISOU 1056 O PRO A 138 1976 1105 921 -268 -22 -111 O ATOM 1057 CB PRO A 138 54.378 11.710 30.269 1.00 11.21 C ANISOU 1057 CB PRO A 138 1372 1030 1856 298 -12 -411 C ATOM 1058 CG PRO A 138 54.902 11.293 28.946 1.00 13.41 C ANISOU 1058 CG PRO A 138 1189 2270 1638 -129 156 -201 C ATOM 1059 CD PRO A 138 53.845 10.460 28.257 1.00 11.54 C ANISOU 1059 CD PRO A 138 1335 1424 1626 -136 255 0 C ATOM 1060 N PHE A 139 52.166 13.627 28.809 1.00 9.74 N ANISOU 1060 N PHE A 139 1617 990 1095 -249 209 -115 N ATOM 1061 CA PHE A 139 51.619 14.960 28.599 1.00 9.93 C ANISOU 1061 CA PHE A 139 1455 1209 1110 -134 399 209 C ATOM 1062 C PHE A 139 50.118 14.973 28.843 1.00 9.55 C ANISOU 1062 C PHE A 139 1379 1371 879 -148 59 5 C ATOM 1063 O PHE A 139 49.577 15.827 29.548 1.00 11.81 O ANISOU 1063 O PHE A 139 2214 1351 921 105 78 -8 O ATOM 1064 CB PHE A 139 51.929 15.438 27.166 1.00 9.75 C ANISOU 1064 CB PHE A 139 1311 1557 836 11 70 134 C ATOM 1065 CG PHE A 139 53.399 15.605 26.904 1.00 10.19 C ANISOU 1065 CG PHE A 139 1359 1463 1051 30 254 151 C ATOM 1066 CD1 PHE A 139 54.170 14.531 26.469 1.00 11.33 C ANISOU 1066 CD1 PHE A 139 1434 1645 1224 153 76 -127 C ATOM 1067 CD2 PHE A 139 54.012 16.836 27.092 1.00 9.73 C ANISOU 1067 CD2 PHE A 139 1412 1209 1077 277 188 81 C ATOM 1068 CE1 PHE A 139 55.538 14.678 26.242 1.00 11.19 C ANISOU 1068 CE1 PHE A 139 1626 1658 968 -164 296 -94 C ATOM 1069 CE2 PHE A 139 55.377 16.975 26.861 1.00 11.69 C ANISOU 1069 CE2 PHE A 139 1580 1495 1369 -26 552 -201 C ATOM 1070 CZ PHE A 139 56.135 15.900 26.431 1.00 11.01 C ANISOU 1070 CZ PHE A 139 1328 1500 1355 15 408 -25 C ATOM 1071 N ARG A 140 49.438 14.011 28.218 1.00 10.77 N ANISOU 1071 N ARG A 140 1498 1728 865 -383 -82 -33 N ATOM 1072 CA ARG A 140 47.972 13.973 28.368 1.00 11.99 C ANISOU 1072 CA ARG A 140 1500 1752 1303 -248 -118 -277 C ATOM 1073 C ARG A 140 47.594 13.646 29.806 1.00 11.16 C ANISOU 1073 C ARG A 140 1373 1340 1528 -204 63 -93 C ATOM 1074 O ARG A 140 46.594 14.181 30.304 1.00 12.87 O ANISOU 1074 O ARG A 140 1575 1517 1798 100 -43 -304 O ATOM 1075 CB ARG A 140 47.346 13.075 27.312 1.00 14.63 C ANISOU 1075 CB ARG A 140 1306 2016 2236 -434 -390 -539 C ATOM 1076 CG ARG A 140 47.619 11.590 27.356 1.00 16.38 C ANISOU 1076 CG ARG A 140 2027 2089 2105 -297 -384 -142 C ATOM 1077 CD ARG A 140 47.019 10.907 26.089 1.00 18.23 C ANISOU 1077 CD ARG A 140 2349 2606 1972 -671 -411 -61 C ATOM 1078 NE ARG A 140 46.881 9.467 26.444 1.00 23.95 N ANISOU 1078 NE ARG A 140 3683 2503 2915 -46 -633 -120 N ATOM 1079 CZ ARG A 140 47.738 8.559 26.005 1.00 21.41 C ANISOU 1079 CZ ARG A 140 2871 3045 2217 -241 -549 -216 C ATOM 1080 NH1 ARG A 140 48.710 8.941 25.198 1.00 24.82 N ANISOU 1080 NH1 ARG A 140 3134 3476 2822 -81 -107 -145 N ATOM 1081 NH2 ARG A 140 47.646 7.285 26.325 1.00 27.58 N ANISOU 1081 NH2 ARG A 140 3967 3143 3369 198 -112 -52 N ATOM 1082 N GLN A 141 48.349 12.778 30.481 1.00 11.01 N ANISOU 1082 N GLN A 141 1456 1465 1264 -92 116 -102 N ATOM 1083 CA GLN A 141 48.036 12.415 31.865 1.00 10.64 C ANISOU 1083 CA GLN A 141 1696 881 1467 -109 225 64 C ATOM 1084 C GLN A 141 48.187 13.625 32.774 1.00 10.36 C ANISOU 1084 C GLN A 141 1433 1255 1247 -155 398 -92 C ATOM 1085 O GLN A 141 47.348 13.903 33.631 1.00 12.23 O ANISOU 1085 O GLN A 141 1688 1535 1422 -58 704 -2 O ATOM 1086 CB GLN A 141 48.964 11.281 32.333 1.00 11.01 C ANISOU 1086 CB GLN A 141 1654 763 1768 -4 406 -66 C ATOM 1087 CG GLN A 141 48.622 9.990 31.588 1.00 15.08 C ANISOU 1087 CG GLN A 141 2404 875 2451 -317 474 -251 C ATOM 1088 CD GLN A 141 49.767 9.003 31.514 1.00 14.51 C ANISOU 1088 CD GLN A 141 2251 1263 1998 -312 963 -235 C ATOM 1089 OE1 GLN A 141 50.821 9.214 32.082 1.00 15.13 O ANISOU 1089 OE1 GLN A 141 2132 1197 2421 273 787 96 O ATOM 1090 NE2 GLN A 141 49.470 7.911 30.802 1.00 16.08 N ANISOU 1090 NE2 GLN A 141 3102 900 2108 -292 1209 -152 N ATOM 1091 N ALA A 142 49.279 14.359 32.610 1.00 10.39 N ANISOU 1091 N ALA A 142 1637 949 1362 -344 -3 60 N ATOM 1092 CA ALA A 142 49.504 15.562 33.408 1.00 9.69 C ANISOU 1092 CA ALA A 142 1588 1344 748 42 211 -121 C ATOM 1093 C ALA A 142 48.456 16.620 33.105 1.00 10.65 C ANISOU 1093 C ALA A 142 2006 1232 807 80 17 37 C ATOM 1094 O ALA A 142 47.985 17.290 34.030 1.00 11.85 O ANISOU 1094 O ALA A 142 2652 1028 821 54 205 72 O ATOM 1095 CB ALA A 142 50.915 16.074 33.145 1.00 11.73 C ANISOU 1095 CB ALA A 142 1563 2038 857 -118 134 19 C ATOM 1096 N ALA A 143 48.121 16.790 31.827 1.00 11.08 N ANISOU 1096 N ALA A 143 2051 1373 787 -38 1 106 N ATOM 1097 CA ALA A 143 47.108 17.782 31.492 1.00 11.33 C ANISOU 1097 CA ALA A 143 2224 1426 655 76 136 85 C ATOM 1098 C ALA A 143 45.831 17.449 32.255 1.00 11.47 C ANISOU 1098 C ALA A 143 2137 1244 976 243 235 -78 C ATOM 1099 O ALA A 143 45.262 18.306 32.935 1.00 13.69 O ANISOU 1099 O ALA A 143 2727 1498 978 654 615 131 O ATOM 1100 CB ALA A 143 46.874 17.770 29.978 1.00 12.66 C ANISOU 1100 CB ALA A 143 2469 1767 573 -47 235 191 C ATOM 1101 N LEU A 144 45.384 16.208 32.143 1.00 11.34 N ANISOU 1101 N LEU A 144 1582 1318 1410 160 236 31 N ATOM 1102 CA LEU A 144 44.136 15.808 32.790 1.00 12.46 C ANISOU 1102 CA LEU A 144 1720 1667 1347 -6 294 -11 C ATOM 1103 C LEU A 144 44.203 15.972 34.299 1.00 12.61 C ANISOU 1103 C LEU A 144 1639 1736 1414 193 88 -126 C ATOM 1104 O LEU A 144 43.193 16.402 34.884 1.00 14.01 O ANISOU 1104 O LEU A 144 1796 2351 1174 -4 435 -121 O ATOM 1105 CB LEU A 144 43.716 14.400 32.382 1.00 14.71 C ANISOU 1105 CB LEU A 144 1952 2048 1588 -260 308 -408 C ATOM 1106 CG LEU A 144 43.383 14.229 30.891 1.00 15.99 C ANISOU 1106 CG LEU A 144 2014 2331 1730 88 5 -539 C ATOM 1107 CD1 LEU A 144 43.362 12.748 30.562 1.00 19.17 C ANISOU 1107 CD1 LEU A 144 2440 2392 2453 151 -59 -712 C ATOM 1108 CD2 LEU A 144 42.059 14.882 30.532 1.00 18.15 C ANISOU 1108 CD2 LEU A 144 2037 3043 1816 42 -387 -516 C ATOM 1109 N ARG A 145 45.351 15.677 34.915 1.00 11.36 N ANISOU 1109 N ARG A 145 1641 1617 1059 -243 -19 88 N ATOM 1110 CA ARG A 145 45.426 15.849 36.370 1.00 11.92 C ANISOU 1110 CA ARG A 145 1768 1674 1086 -159 309 -183 C ATOM 1111 C ARG A 145 45.266 17.303 36.772 1.00 13.51 C ANISOU 1111 C ARG A 145 2559 1630 945 -45 362 -61 C ATOM 1112 O ARG A 145 44.892 17.571 37.932 1.00 15.15 O ANISOU 1112 O ARG A 145 3221 1513 1022 -208 767 -72 O ATOM 1113 CB ARG A 145 46.734 15.293 36.934 1.00 12.27 C ANISOU 1113 CB ARG A 145 2006 1467 1189 39 384 176 C ATOM 1114 CG ARG A 145 46.794 13.766 36.946 1.00 11.55 C ANISOU 1114 CG ARG A 145 1932 1422 1034 -326 54 157 C ATOM 1115 CD ARG A 145 48.002 13.250 37.707 1.00 12.68 C ANISOU 1115 CD ARG A 145 1739 1836 1243 -149 210 170 C ATOM 1116 NE ARG A 145 49.275 13.779 37.228 1.00 13.34 N ANISOU 1116 NE ARG A 145 1820 1880 1368 -299 16 570 N ATOM 1117 CZ ARG A 145 50.015 13.181 36.298 1.00 13.19 C ANISOU 1117 CZ ARG A 145 1994 1645 1373 -307 -57 506 C ATOM 1118 NH1 ARG A 145 49.636 12.045 35.736 1.00 14.31 N ANISOU 1118 NH1 ARG A 145 2377 1670 1390 -303 -16 380 N ATOM 1119 NH2 ARG A 145 51.161 13.734 35.914 1.00 14.27 N ANISOU 1119 NH2 ARG A 145 1623 2167 1631 -458 -446 306 N ATOM 1120 N HIS A 146 45.608 18.219 35.874 1.00 12.30 N ANISOU 1120 N HIS A 146 2361 1014 1298 21 288 -184 N ATOM 1121 CA HIS A 146 45.520 19.636 36.219 1.00 11.94 C ANISOU 1121 CA HIS A 146 2093 1197 1247 96 432 -488 C ATOM 1122 C HIS A 146 44.393 20.351 35.511 1.00 11.64 C ANISOU 1122 C HIS A 146 1978 1240 1204 -188 388 -214 C ATOM 1123 O HIS A 146 44.448 21.572 35.363 1.00 13.11 O ANISOU 1123 O HIS A 146 2324 1257 1400 -228 467 -116 O ATOM 1124 CB HIS A 146 46.869 20.313 35.916 1.00 13.02 C ANISOU 1124 CB HIS A 146 2035 1499 1414 17 146 -209 C ATOM 1125 CG HIS A 146 47.937 19.738 36.808 1.00 14.31 C ANISOU 1125 CG HIS A 146 2505 1831 1102 95 -10 -207 C ATOM 1126 ND1 HIS A 146 48.846 18.773 36.472 1.00 13.58 N ANISOU 1126 ND1 HIS A 146 2144 1462 1554 -161 173 413 N ATOM 1127 CD2 HIS A 146 48.150 20.063 38.112 1.00 17.24 C ANISOU 1127 CD2 HIS A 146 3074 2221 1255 155 -386 -318 C ATOM 1128 CE1 HIS A 146 49.600 18.509 37.528 1.00 17.14 C ANISOU 1128 CE1 HIS A 146 2434 1929 2150 245 -231 410 C ATOM 1129 NE2 HIS A 146 49.211 19.287 38.516 1.00 21.24 N ANISOU 1129 NE2 HIS A 146 3457 2347 2265 283 -541 0 N ATOM 1130 N ASN A 147 43.387 19.616 35.051 1.00 11.47 N ANISOU 1130 N ASN A 147 1895 1553 910 -264 291 97 N ATOM 1131 CA ASN A 147 42.216 20.213 34.444 1.00 11.94 C ANISOU 1131 CA ASN A 147 1802 1593 1141 20 517 -54 C ATOM 1132 C ASN A 147 42.539 21.045 33.212 1.00 12.32 C ANISOU 1132 C ASN A 147 1946 1358 1376 108 321 158 C ATOM 1133 O ASN A 147 41.865 22.032 32.889 1.00 14.18 O ANISOU 1133 O ASN A 147 2395 1458 1536 548 711 -92 O ATOM 1134 CB ASN A 147 41.494 21.069 35.508 1.00 14.64 C ANISOU 1134 CB ASN A 147 2260 1994 1309 38 794 -212 C ATOM 1135 CG ASN A 147 41.138 20.194 36.707 1.00 16.47 C ANISOU 1135 CG ASN A 147 2414 2180 1664 -134 463 154 C ATOM 1136 OD1 ASN A 147 40.379 19.243 36.524 1.00 20.81 O ANISOU 1136 OD1 ASN A 147 2891 2774 2243 -572 550 -150 O ATOM 1137 ND2 ASN A 147 41.693 20.478 37.874 1.00 18.09 N ANISOU 1137 ND2 ASN A 147 3157 2122 1596 -524 705 -233 N ATOM 1138 N ILE A 148 43.554 20.568 32.486 1.00 11.74 N ANISOU 1138 N ILE A 148 1847 1318 1296 -106 316 119 N ATOM 1139 CA ILE A 148 43.945 21.173 31.216 1.00 10.53 C ANISOU 1139 CA ILE A 148 1638 1380 981 -25 262 -145 C ATOM 1140 C ILE A 148 43.555 20.203 30.096 1.00 11.90 C ANISOU 1140 C ILE A 148 1829 1126 1568 -97 -97 -145 C ATOM 1141 O ILE A 148 43.798 18.999 30.233 1.00 12.53 O ANISOU 1141 O ILE A 148 2568 1021 1172 -232 49 128 O ATOM 1142 CB ILE A 148 45.449 21.450 31.143 1.00 10.33 C ANISOU 1142 CB ILE A 148 1599 1371 957 -2 33 45 C ATOM 1143 CG1 ILE A 148 45.911 22.337 32.304 1.00 11.36 C ANISOU 1143 CG1 ILE A 148 1714 1513 1092 -58 624 -376 C ATOM 1144 CG2 ILE A 148 45.848 22.072 29.804 1.00 11.56 C ANISOU 1144 CG2 ILE A 148 1478 2065 849 -33 0 92 C ATOM 1145 CD1 ILE A 148 45.200 23.671 32.380 1.00 13.46 C ANISOU 1145 CD1 ILE A 148 2171 1522 1421 100 431 -182 C ATOM 1146 N ALA A 149 42.963 20.694 29.028 1.00 11.30 N ANISOU 1146 N ALA A 149 1972 1089 1232 30 79 -332 N ATOM 1147 CA ALA A 149 42.661 19.809 27.902 1.00 10.75 C ANISOU 1147 CA ALA A 149 1875 1120 1090 82 162 -291 C ATOM 1148 C ALA A 149 43.904 19.616 27.035 1.00 11.03 C ANISOU 1148 C ALA A 149 1828 1248 1116 108 129 -84 C ATOM 1149 O ALA A 149 44.473 20.600 26.542 1.00 11.15 O ANISOU 1149 O ALA A 149 1930 1042 1263 217 354 -185 O ATOM 1150 CB ALA A 149 41.576 20.459 27.045 1.00 11.82 C ANISOU 1150 CB ALA A 149 1774 1579 1139 -66 10 -300 C ATOM 1151 N PRO A 150 44.307 18.384 26.812 1.00 10.38 N ANISOU 1151 N PRO A 150 1614 1135 1193 -16 -37 22 N ATOM 1152 CA PRO A 150 45.407 18.118 25.885 1.00 10.05 C ANISOU 1152 CA PRO A 150 1700 995 1122 152 -7 107 C ATOM 1153 C PRO A 150 44.781 18.067 24.487 1.00 11.08 C ANISOU 1153 C PRO A 150 1600 1357 1252 -54 -75 -48 C ATOM 1154 O PRO A 150 43.807 17.356 24.243 1.00 11.26 O ANISOU 1154 O PRO A 150 2095 1189 996 -199 -313 -126 O ATOM 1155 CB PRO A 150 45.915 16.775 26.337 1.00 11.22 C ANISOU 1155 CB PRO A 150 1822 718 1721 208 -81 -192 C ATOM 1156 CG PRO A 150 44.704 16.071 26.895 1.00 11.66 C ANISOU 1156 CG PRO A 150 1593 1445 1393 301 -176 -10 C ATOM 1157 CD PRO A 150 43.755 17.131 27.390 1.00 11.23 C ANISOU 1157 CD PRO A 150 1769 1011 1489 27 101 -63 C ATOM 1158 N ILE A 151 45.348 18.839 23.564 1.00 10.01 N ANISOU 1158 N ILE A 151 1599 1423 782 225 -79 -90 N ATOM 1159 CA ILE A 151 44.888 18.957 22.194 1.00 10.82 C ANISOU 1159 CA ILE A 151 1495 1703 911 214 -309 -239 C ATOM 1160 C ILE A 151 45.784 18.147 21.256 1.00 9.88 C ANISOU 1160 C ILE A 151 1074 1493 1185 128 -414 -234 C ATOM 1161 O ILE A 151 47.001 18.237 21.299 1.00 11.41 O ANISOU 1161 O ILE A 151 981 2279 1077 392 -484 -517 O ATOM 1162 CB ILE A 151 44.918 20.416 21.707 1.00 9.77 C ANISOU 1162 CB ILE A 151 1192 1712 807 352 -264 -278 C ATOM 1163 CG1 ILE A 151 44.200 21.364 22.683 1.00 10.97 C ANISOU 1163 CG1 ILE A 151 1337 1710 1120 364 -106 -351 C ATOM 1164 CG2 ILE A 151 44.373 20.560 20.301 1.00 11.11 C ANISOU 1164 CG2 ILE A 151 1322 2013 888 414 -321 -86 C ATOM 1165 CD1 ILE A 151 42.755 20.979 22.953 1.00 11.82 C ANISOU 1165 CD1 ILE A 151 1432 1709 1348 127 -90 -494 C ATOM 1166 N PHE A 152 45.130 17.386 20.374 1.00 11.15 N ANISOU 1166 N PHE A 152 1772 1734 731 369 -366 -594 N ATOM 1167 CA PHE A 152 45.871 16.603 19.395 1.00 10.55 C ANISOU 1167 CA PHE A 152 1640 1694 673 293 -75 -257 C ATOM 1168 C PHE A 152 45.473 17.002 17.991 1.00 10.81 C ANISOU 1168 C PHE A 152 1365 1894 847 167 -324 -87 C ATOM 1169 O PHE A 152 44.355 17.411 17.702 1.00 12.83 O ANISOU 1169 O PHE A 152 1311 2202 1359 329 -197 -246 O ATOM 1170 CB PHE A 152 45.636 15.100 19.585 1.00 12.99 C ANISOU 1170 CB PHE A 152 2433 1489 1013 592 63 -538 C ATOM 1171 CG PHE A 152 46.309 14.737 20.887 1.00 14.82 C ANISOU 1171 CG PHE A 152 1890 2321 1421 262 -49 76 C ATOM 1172 CD1 PHE A 152 47.689 14.635 20.954 1.00 16.18 C ANISOU 1172 CD1 PHE A 152 1966 2448 1731 797 -220 154 C ATOM 1173 CD2 PHE A 152 45.544 14.622 22.035 1.00 13.76 C ANISOU 1173 CD2 PHE A 152 1915 1816 1496 522 42 150 C ATOM 1174 CE1 PHE A 152 48.320 14.347 22.162 1.00 16.06 C ANISOU 1174 CE1 PHE A 152 1888 2638 1577 327 -140 187 C ATOM 1175 CE2 PHE A 152 46.164 14.315 23.239 1.00 14.84 C ANISOU 1175 CE2 PHE A 152 2042 2123 1473 133 -252 -136 C ATOM 1176 CZ PHE A 152 47.542 14.188 23.292 1.00 16.82 C ANISOU 1176 CZ PHE A 152 2100 2591 1700 487 44 98 C ATOM 1177 N ILE A 153 46.461 16.898 17.112 1.00 13.00 N ANISOU 1177 N ILE A 153 1552 2653 733 565 -342 -178 N ATOM 1178 CA ILE A 153 46.282 17.223 15.704 1.00 12.10 C ANISOU 1178 CA ILE A 153 1610 2289 699 232 -408 -219 C ATOM 1179 C ILE A 153 45.875 15.986 14.918 1.00 13.58 C ANISOU 1179 C ILE A 153 2057 1875 1228 394 -465 -132 C ATOM 1180 O ILE A 153 46.458 14.915 15.018 1.00 14.08 O ANISOU 1180 O ILE A 153 2225 2074 1051 645 -365 -309 O ATOM 1181 CB ILE A 153 47.612 17.745 15.106 1.00 13.61 C ANISOU 1181 CB ILE A 153 1757 2129 1284 151 -129 -417 C ATOM 1182 CG1 ILE A 153 47.951 19.117 15.682 1.00 14.44 C ANISOU 1182 CG1 ILE A 153 2027 2193 1266 114 -81 -523 C ATOM 1183 CG2 ILE A 153 47.530 17.781 13.588 1.00 14.37 C ANISOU 1183 CG2 ILE A 153 2010 2156 1295 186 7 -393 C ATOM 1184 CD1 ILE A 153 49.224 19.777 15.219 1.00 14.10 C ANISOU 1184 CD1 ILE A 153 2134 1797 1427 8 -284 -473 C ATOM 1185 N CYS A 154 44.856 16.170 14.083 1.00 13.47 N ANISOU 1185 N CYS A 154 2119 1708 1291 722 -548 -296 N ATOM 1186 CA CYS A 154 44.404 15.155 13.154 1.00 14.69 C ANISOU 1186 CA CYS A 154 2055 1825 1701 150 -488 -231 C ATOM 1187 C CYS A 154 44.872 15.544 11.756 1.00 14.62 C ANISOU 1187 C CYS A 154 1820 2211 1523 372 -591 -325 C ATOM 1188 O CYS A 154 44.321 16.510 11.222 1.00 15.47 O ANISOU 1188 O CYS A 154 2252 1849 1778 352 -636 -385 O ATOM 1189 CB CYS A 154 42.879 15.158 13.145 1.00 16.97 C ANISOU 1189 CB CYS A 154 2102 2138 2208 -71 -572 -415 C ATOM 1190 SG ACYS A 154 42.093 13.861 12.183 0.70 19.42 S ANISOU 1190 SG ACYS A 154 2728 1987 2663 202 -657 -871 S ATOM 1191 SG BCYS A 154 42.098 14.136 14.374 0.30 18.24 S ANISOU 1191 SG BCYS A 154 2632 2085 2213 -44 -355 -397 S ATOM 1192 N PRO A 155 45.803 14.838 11.165 1.00 15.29 N ANISOU 1192 N PRO A 155 1724 2376 1709 722 -701 -217 N ATOM 1193 CA PRO A 155 46.309 15.075 9.813 1.00 19.27 C ANISOU 1193 CA PRO A 155 2426 2713 2183 243 -169 132 C ATOM 1194 C PRO A 155 45.201 14.895 8.798 1.00 21.20 C ANISOU 1194 C PRO A 155 2796 3043 2215 -53 -243 -5 C ATOM 1195 O PRO A 155 44.271 14.156 9.093 1.00 19.94 O ANISOU 1195 O PRO A 155 3136 2962 1477 -426 -629 -311 O ATOM 1196 CB PRO A 155 47.399 14.030 9.621 1.00 22.07 C ANISOU 1196 CB PRO A 155 2652 3203 2530 640 -260 248 C ATOM 1197 CG PRO A 155 47.756 13.619 11.003 1.00 19.61 C ANISOU 1197 CG PRO A 155 1944 3361 2146 419 -492 -335 C ATOM 1198 CD PRO A 155 46.495 13.675 11.809 1.00 15.43 C ANISOU 1198 CD PRO A 155 1601 2508 1753 718 -836 -133 C ATOM 1199 N APRO A 156 45.331 15.616 7.688 0.50 22.39 N ANISOU 1199 N APRO A 156 3243 2945 2321 -152 -30 55 N ATOM 1200 CA APRO A 156 44.322 15.657 6.650 0.50 25.41 C ANISOU 1200 CA APRO A 156 3441 3374 2839 -143 -274 70 C ATOM 1201 C APRO A 156 44.219 14.341 5.910 0.50 28.68 C ANISOU 1201 C APRO A 156 4021 3516 3362 -125 -114 -148 C ATOM 1202 O APRO A 156 43.921 14.346 4.715 0.50 31.11 O ANISOU 1202 O APRO A 156 4413 3925 3484 -130 -137 -20 O ATOM 1203 CB APRO A 156 44.885 16.695 5.664 0.50 23.72 C ANISOU 1203 CB APRO A 156 3382 3240 2392 -60 -303 -120 C ATOM 1204 CG APRO A 156 46.365 16.522 5.810 0.50 23.63 C ANISOU 1204 CG APRO A 156 3292 3164 2524 62 44 42 C ATOM 1205 CD APRO A 156 46.501 16.474 7.318 0.50 22.63 C ANISOU 1205 CD APRO A 156 3086 3007 2505 -110 -177 16 C ATOM 1206 N BPRO A 156 45.279 15.489 7.611 0.50 22.07 N ANISOU 1206 N BPRO A 156 3277 2890 2221 -101 -73 34 N ATOM 1207 CA BPRO A 156 44.231 15.378 6.617 0.50 24.84 C ANISOU 1207 CA BPRO A 156 3403 3357 2677 -142 -248 16 C ATOM 1208 C BPRO A 156 43.812 13.966 6.252 0.50 25.98 C ANISOU 1208 C BPRO A 156 3737 3342 2793 -136 -147 85 C ATOM 1209 O BPRO A 156 42.650 13.663 5.990 0.50 27.81 O ANISOU 1209 O BPRO A 156 3787 3668 3110 -217 24 26 O ATOM 1210 CB BPRO A 156 44.850 16.033 5.379 0.50 24.36 C ANISOU 1210 CB BPRO A 156 3556 3090 2611 -91 -280 23 C ATOM 1211 CG BPRO A 156 45.857 16.985 5.896 0.50 22.88 C ANISOU 1211 CG BPRO A 156 3125 3042 2526 34 -127 113 C ATOM 1212 CD BPRO A 156 46.379 16.394 7.178 0.50 22.21 C ANISOU 1212 CD BPRO A 156 3176 3014 2250 -152 -173 -71 C ATOM 1213 N AASN A 157 44.502 13.268 6.629 0.50 31.51 N ANISOU 1213 N AASN A 157 4342 3751 3880 15 -33 68 N ATOM 1214 CA AASN A 157 44.589 11.983 5.936 0.50 32.13 C ANISOU 1214 CA AASN A 157 4526 3901 3781 -29 -36 4 C ATOM 1215 C AASN A 157 44.743 10.848 6.928 0.50 29.82 C ANISOU 1215 C AASN A 157 4295 3641 3394 -91 71 -233 C ATOM 1216 O AASN A 157 45.109 9.720 6.606 0.50 29.73 O ANISOU 1216 O AASN A 157 4207 3607 3481 -152 40 -348 O ATOM 1217 CB AASN A 157 45.900 12.147 5.138 0.50 36.10 C ANISOU 1217 CB AASN A 157 4703 4596 4417 -34 177 69 C ATOM 1218 CG AASN A 157 47.031 12.563 6.074 0.50 38.13 C ANISOU 1218 CG AASN A 157 4977 4980 4529 -39 -12 14 C ATOM 1219 OD1AASN A 157 47.763 11.658 6.470 0.50 39.73 O ANISOU 1219 OD1AASN A 157 5386 4894 4815 -23 -72 35 O ATOM 1220 ND2AASN A 157 47.148 13.844 6.376 0.50 38.89 N ANISOU 1220 ND2AASN A 157 5112 5054 4612 106 33 8 N ATOM 1221 N BASN A 157 44.788 13.083 6.192 0.50 28.98 N ANISOU 1221 N BASN A 157 4074 3723 3213 92 129 57 N ATOM 1222 CA BASN A 157 44.652 11.693 5.788 0.50 30.98 C ANISOU 1222 CA BASN A 157 4315 3787 3668 -106 -28 -16 C ATOM 1223 C BASN A 157 44.556 10.692 6.923 0.50 28.91 C ANISOU 1223 C BASN A 157 4078 3540 3365 -104 -63 -250 C ATOM 1224 O BASN A 157 44.417 9.483 6.699 0.50 29.63 O ANISOU 1224 O BASN A 157 4032 3563 3664 -148 -91 -370 O ATOM 1225 CB BASN A 157 45.929 11.469 4.964 0.50 34.53 C ANISOU 1225 CB BASN A 157 4504 4441 4175 25 196 -34 C ATOM 1226 CG BASN A 157 46.124 10.115 4.354 0.50 36.37 C ANISOU 1226 CG BASN A 157 4751 4478 4590 4 106 -109 C ATOM 1227 OD1BASN A 157 45.250 9.252 4.416 0.50 37.90 O ANISOU 1227 OD1BASN A 157 4874 4732 4795 -119 206 -6 O ATOM 1228 ND2BASN A 157 47.283 9.896 3.735 0.50 37.25 N ANISOU 1228 ND2BASN A 157 4660 4757 4737 -2 125 -79 N ATOM 1229 N AALA A 158 44.509 11.209 8.185 0.50 26.66 N ANISOU 1229 N AALA A 158 4144 2833 3150 -213 -41 -33 N ATOM 1230 CA AALA A 158 44.632 10.279 9.296 0.50 23.90 C ANISOU 1230 CA AALA A 158 3635 2694 2753 -153 -131 -300 C ATOM 1231 C AALA A 158 43.808 9.023 9.037 0.50 23.75 C ANISOU 1231 C AALA A 158 3385 2692 2948 -85 -268 -221 C ATOM 1232 O AALA A 158 42.667 9.114 8.574 0.50 24.63 O ANISOU 1232 O AALA A 158 3486 2932 2940 -196 -457 -361 O ATOM 1233 CB AALA A 158 44.119 10.956 10.562 0.50 22.24 C ANISOU 1233 CB AALA A 158 3138 2647 2667 -133 -222 -212 C ATOM 1234 N BALA A 158 44.658 11.171 8.161 0.50 26.81 N ANISOU 1234 N BALA A 158 4147 2893 3146 -200 99 8 N ATOM 1235 CA BALA A 158 44.588 10.291 9.323 0.50 23.55 C ANISOU 1235 CA BALA A 158 3524 2692 2732 -116 -59 -282 C ATOM 1236 C BALA A 158 43.828 9.014 8.958 0.50 23.55 C ANISOU 1236 C BALA A 158 3302 2700 2947 -76 -190 -229 C ATOM 1237 O BALA A 158 42.614 9.107 8.708 0.50 24.31 O ANISOU 1237 O BALA A 158 3247 2972 3017 -200 -240 -387 O ATOM 1238 CB BALA A 158 43.875 10.999 10.464 0.50 21.14 C ANISOU 1238 CB BALA A 158 2922 2606 2505 -33 -297 -95 C ATOM 1239 N ASP A 159 44.388 7.878 9.386 1.00 25.10 N ANISOU 1239 N ASP A 159 3953 2797 2785 164 -48 -338 N ATOM 1240 CA ASP A 159 43.640 6.622 9.226 1.00 27.87 C ANISOU 1240 CA ASP A 159 4275 3140 3172 -211 67 -256 C ATOM 1241 C ASP A 159 42.726 6.418 10.426 1.00 28.75 C ANISOU 1241 C ASP A 159 4579 3270 3075 -231 88 -455 C ATOM 1242 O ASP A 159 42.683 7.198 11.384 1.00 25.24 O ANISOU 1242 O ASP A 159 4240 3081 2270 -133 57 -45 O ATOM 1243 CB ASP A 159 44.550 5.443 8.976 1.00 31.05 C ANISOU 1243 CB ASP A 159 4691 3610 3496 120 269 -368 C ATOM 1244 CG ASP A 159 45.313 4.919 10.158 1.00 33.11 C ANISOU 1244 CG ASP A 159 4881 3933 3765 102 166 -141 C ATOM 1245 OD1 ASP A 159 45.165 5.417 11.300 1.00 33.61 O ANISOU 1245 OD1 ASP A 159 5293 3583 3894 75 239 -293 O ATOM 1246 OD2 ASP A 159 46.097 3.964 9.977 1.00 34.74 O ANISOU 1246 OD2 ASP A 159 5365 4162 3671 242 614 -409 O ATOM 1247 N ASP A 160 41.947 5.347 10.383 1.00 28.08 N ANISOU 1247 N ASP A 160 4604 3247 2817 -255 79 -427 N ATOM 1248 CA ASP A 160 40.966 5.041 11.399 1.00 28.24 C ANISOU 1248 CA ASP A 160 4141 3352 3239 -280 18 -304 C ATOM 1249 C ASP A 160 41.526 4.882 12.802 1.00 25.22 C ANISOU 1249 C ASP A 160 3439 2895 3247 -261 42 -395 C ATOM 1250 O ASP A 160 40.928 5.420 13.740 1.00 24.12 O ANISOU 1250 O ASP A 160 3722 2425 3018 -478 -156 -566 O ATOM 1251 CB ASP A 160 40.174 3.778 11.010 1.00 29.21 C ANISOU 1251 CB ASP A 160 4277 3419 3401 -265 -113 -422 C ATOM 1252 CG ASP A 160 38.912 3.742 11.855 1.00 29.20 C ANISOU 1252 CG ASP A 160 4052 3432 3611 -103 -191 -351 C ATOM 1253 OD1 ASP A 160 38.041 4.609 11.642 1.00 31.31 O ANISOU 1253 OD1 ASP A 160 4395 3538 3962 45 -254 -328 O ATOM 1254 OD2 ASP A 160 38.827 2.865 12.735 1.00 31.65 O ANISOU 1254 OD2 ASP A 160 4695 3481 3849 -140 -126 -309 O ATOM 1255 N ASP A 161 42.604 4.133 12.972 1.00 25.69 N ANISOU 1255 N ASP A 161 3825 2576 3362 -137 -22 -412 N ATOM 1256 CA ASP A 161 43.202 3.939 14.279 1.00 26.48 C ANISOU 1256 CA ASP A 161 3885 2846 3329 -180 70 -156 C ATOM 1257 C ASP A 161 43.593 5.295 14.872 1.00 22.49 C ANISOU 1257 C ASP A 161 3232 2725 2589 109 187 -107 C ATOM 1258 O ASP A 161 43.414 5.524 16.062 1.00 22.11 O ANISOU 1258 O ASP A 161 3199 2617 2586 346 202 -149 O ATOM 1259 CB ASP A 161 44.446 3.054 14.236 1.00 33.00 C ANISOU 1259 CB ASP A 161 4214 3848 4478 257 173 -44 C ATOM 1260 CG ASP A 161 44.149 1.569 14.144 1.00 37.23 C ANISOU 1260 CG ASP A 161 4992 4059 5094 -35 60 -90 C ATOM 1261 OD1 ASP A 161 42.961 1.194 14.089 1.00 37.69 O ANISOU 1261 OD1 ASP A 161 5053 4153 5115 -82 -49 -69 O ATOM 1262 OD2 ASP A 161 45.130 0.790 14.138 1.00 39.87 O ANISOU 1262 OD2 ASP A 161 5319 4311 5517 208 84 -243 O ATOM 1263 N LEU A 162 44.181 6.160 14.054 1.00 19.49 N ANISOU 1263 N LEU A 162 3406 2040 1960 279 -113 -337 N ATOM 1264 CA LEU A 162 44.600 7.476 14.543 1.00 17.32 C ANISOU 1264 CA LEU A 162 2528 2247 1805 85 -186 -281 C ATOM 1265 C LEU A 162 43.385 8.310 14.920 1.00 16.61 C ANISOU 1265 C LEU A 162 2422 2107 1783 35 -335 -372 C ATOM 1266 O LEU A 162 43.378 9.008 15.939 1.00 16.73 O ANISOU 1266 O LEU A 162 2430 2088 1839 -44 -78 -510 O ATOM 1267 CB LEU A 162 45.457 8.203 13.503 1.00 17.64 C ANISOU 1267 CB LEU A 162 2334 2408 1961 141 -223 -142 C ATOM 1268 CG LEU A 162 45.952 9.594 13.905 1.00 16.77 C ANISOU 1268 CG LEU A 162 1956 2453 1961 77 -555 106 C ATOM 1269 CD1 LEU A 162 46.686 9.520 15.245 1.00 18.45 C ANISOU 1269 CD1 LEU A 162 2201 3115 1695 43 -373 107 C ATOM 1270 CD2 LEU A 162 46.865 10.179 12.849 1.00 16.88 C ANISOU 1270 CD2 LEU A 162 2051 2595 1768 191 -570 128 C ATOM 1271 N LEU A 163 42.315 8.285 14.128 1.00 16.88 N ANISOU 1271 N LEU A 163 2330 1842 2242 -56 -436 -377 N ATOM 1272 CA LEU A 163 41.113 9.039 14.458 1.00 16.62 C ANISOU 1272 CA LEU A 163 2171 2107 2036 -107 -426 -426 C ATOM 1273 C LEU A 163 40.558 8.594 15.797 1.00 16.08 C ANISOU 1273 C LEU A 163 1860 1975 2273 -52 -225 -412 C ATOM 1274 O LEU A 163 40.137 9.433 16.609 1.00 16.62 O ANISOU 1274 O LEU A 163 2272 1830 2212 -428 -582 -784 O ATOM 1275 CB LEU A 163 40.054 8.873 13.356 1.00 19.53 C ANISOU 1275 CB LEU A 163 2434 2874 2114 -108 -593 -209 C ATOM 1276 CG LEU A 163 40.362 9.605 12.051 1.00 20.46 C ANISOU 1276 CG LEU A 163 2677 2744 2352 -11 -417 -92 C ATOM 1277 CD1 LEU A 163 39.461 9.097 10.927 1.00 23.32 C ANISOU 1277 CD1 LEU A 163 3370 3131 2359 -285 -499 -289 C ATOM 1278 CD2 LEU A 163 40.189 11.100 12.239 1.00 23.34 C ANISOU 1278 CD2 LEU A 163 3373 2836 2661 116 -91 -254 C ATOM 1279 N ARG A 164 40.564 7.292 16.057 1.00 16.48 N ANISOU 1279 N ARG A 164 2353 1953 1956 -123 -249 -493 N ATOM 1280 CA ARG A 164 40.064 6.763 17.313 1.00 17.20 C ANISOU 1280 CA ARG A 164 2320 1972 2244 -112 -105 -313 C ATOM 1281 C ARG A 164 40.946 7.224 18.471 1.00 15.82 C ANISOU 1281 C ARG A 164 2232 1696 2083 153 -18 -440 C ATOM 1282 O ARG A 164 40.396 7.572 19.525 1.00 17.87 O ANISOU 1282 O ARG A 164 2427 1981 2382 68 461 -273 O ATOM 1283 CB ARG A 164 40.011 5.231 17.292 1.00 18.76 C ANISOU 1283 CB ARG A 164 2903 1943 2282 102 4 -279 C ATOM 1284 CG ARG A 164 38.853 4.707 16.446 1.00 23.83 C ANISOU 1284 CG ARG A 164 3218 2885 2953 -149 -339 -250 C ATOM 1285 CD ARG A 164 38.954 3.191 16.299 1.00 27.96 C ANISOU 1285 CD ARG A 164 3857 2966 3801 7 -26 -166 C ATOM 1286 NE ARG A 164 37.941 2.700 15.375 1.00 30.75 N ANISOU 1286 NE ARG A 164 4082 3456 4147 -269 -93 -370 N ATOM 1287 CZ ARG A 164 36.689 2.405 15.706 1.00 32.33 C ANISOU 1287 CZ ARG A 164 4124 3958 4203 -148 92 -201 C ATOM 1288 NH1 ARG A 164 36.283 2.532 16.960 1.00 33.55 N ANISOU 1288 NH1 ARG A 164 4304 4227 4218 -299 112 -224 N ATOM 1289 NH2 ARG A 164 35.856 1.961 14.771 1.00 33.34 N ANISOU 1289 NH2 ARG A 164 4010 4098 4559 -296 -22 -153 N ATOM 1290 N GLN A 165 42.262 7.235 18.288 1.00 16.52 N ANISOU 1290 N GLN A 165 2236 1888 2152 74 -143 -362 N ATOM 1291 CA GLN A 165 43.150 7.673 19.364 1.00 16.16 C ANISOU 1291 CA GLN A 165 1888 2009 2242 105 -162 -228 C ATOM 1292 C GLN A 165 42.991 9.164 19.604 1.00 15.18 C ANISOU 1292 C GLN A 165 2044 1954 1769 122 -210 -27 C ATOM 1293 O GLN A 165 42.924 9.601 20.744 1.00 15.75 O ANISOU 1293 O GLN A 165 2303 1933 1748 65 -590 -116 O ATOM 1294 CB GLN A 165 44.612 7.421 19.022 1.00 19.47 C ANISOU 1294 CB GLN A 165 2041 2536 2822 244 129 -3 C ATOM 1295 CG GLN A 165 45.100 5.980 19.122 1.00 22.59 C ANISOU 1295 CG GLN A 165 3030 2596 2955 325 -34 160 C ATOM 1296 CD GLN A 165 46.589 5.989 18.793 1.00 25.86 C ANISOU 1296 CD GLN A 165 3099 3426 3301 103 56 33 C ATOM 1297 OE1 GLN A 165 46.911 6.123 17.617 1.00 26.42 O ANISOU 1297 OE1 GLN A 165 3228 3511 3300 -102 133 -326 O ATOM 1298 NE2 GLN A 165 47.439 5.897 19.806 1.00 28.51 N ANISOU 1298 NE2 GLN A 165 3530 3826 3478 32 -183 -64 N ATOM 1299 N VAL A 166 42.981 9.958 18.543 1.00 13.37 N ANISOU 1299 N VAL A 166 1884 1662 1533 193 -597 -276 N ATOM 1300 CA VAL A 166 42.781 11.402 18.728 1.00 13.94 C ANISOU 1300 CA VAL A 166 1937 1555 1803 -171 -173 -215 C ATOM 1301 C VAL A 166 41.460 11.669 19.426 1.00 13.29 C ANISOU 1301 C VAL A 166 1728 1777 1542 -159 -392 -127 C ATOM 1302 O VAL A 166 41.348 12.518 20.319 1.00 14.24 O ANISOU 1302 O VAL A 166 1913 1764 1732 116 -486 -233 O ATOM 1303 CB VAL A 166 42.846 12.124 17.373 1.00 14.92 C ANISOU 1303 CB VAL A 166 1957 1740 1971 -6 305 -6 C ATOM 1304 CG1 VAL A 166 42.305 13.536 17.488 1.00 16.75 C ANISOU 1304 CG1 VAL A 166 2290 1737 2338 -7 48 -241 C ATOM 1305 CG2 VAL A 166 44.279 12.098 16.842 1.00 14.88 C ANISOU 1305 CG2 VAL A 166 1862 1449 2341 -292 240 207 C ATOM 1306 N ALA A 167 40.413 10.915 19.061 1.00 13.74 N ANISOU 1306 N ALA A 167 1435 1783 2001 -12 -417 -191 N ATOM 1307 CA ALA A 167 39.113 11.111 19.712 1.00 14.58 C ANISOU 1307 CA ALA A 167 1720 1854 1964 95 -194 -279 C ATOM 1308 C ALA A 167 39.168 10.753 21.192 1.00 15.64 C ANISOU 1308 C ALA A 167 2083 1754 2106 73 -6 -59 C ATOM 1309 O ALA A 167 38.541 11.439 22.006 1.00 17.34 O ANISOU 1309 O ALA A 167 2699 1837 2053 20 221 -117 O ATOM 1310 CB ALA A 167 38.010 10.323 19.017 1.00 16.77 C ANISOU 1310 CB ALA A 167 1863 2080 2427 -61 -336 -279 C ATOM 1311 N SER A 168 39.874 9.673 21.514 1.00 15.03 N ANISOU 1311 N SER A 168 2074 1921 1714 87 -173 22 N ATOM 1312 CA SER A 168 39.963 9.242 22.910 1.00 16.10 C ANISOU 1312 CA SER A 168 2375 1983 1760 -155 -152 117 C ATOM 1313 C SER A 168 40.874 10.111 23.763 1.00 15.39 C ANISOU 1313 C SER A 168 2358 1767 1722 -63 62 -82 C ATOM 1314 O SER A 168 40.616 10.349 24.955 1.00 19.47 O ANISOU 1314 O SER A 168 3495 2183 1722 -76 69 -206 O ATOM 1315 CB SER A 168 40.523 7.807 22.935 1.00 18.40 C ANISOU 1315 CB SER A 168 2841 1914 2235 -188 -213 68 C ATOM 1316 OG SER A 168 40.744 7.374 24.269 1.00 21.67 O ANISOU 1316 OG SER A 168 3457 2473 2305 -307 -313 103 O ATOM 1317 N TYR A 169 42.005 10.514 23.186 1.00 14.29 N ANISOU 1317 N TYR A 169 2152 1603 1674 -79 -262 63 N ATOM 1318 CA TYR A 169 43.035 11.196 23.964 1.00 14.57 C ANISOU 1318 CA TYR A 169 2372 1461 1703 -94 -51 -430 C ATOM 1319 C TYR A 169 42.817 12.688 24.186 1.00 15.89 C ANISOU 1319 C TYR A 169 3000 1524 1514 91 -30 -399 C ATOM 1320 O TYR A 169 43.274 13.225 25.203 1.00 16.44 O ANISOU 1320 O TYR A 169 3378 1442 1426 -60 169 -509 O ATOM 1321 CB TYR A 169 44.401 11.018 23.300 1.00 16.07 C ANISOU 1321 CB TYR A 169 2166 1941 2001 81 -275 -513 C ATOM 1322 CG TYR A 169 44.972 9.618 23.265 1.00 16.04 C ANISOU 1322 CG TYR A 169 2098 1949 2046 129 -569 64 C ATOM 1323 CD1 TYR A 169 44.372 8.543 23.902 1.00 18.56 C ANISOU 1323 CD1 TYR A 169 2329 2127 2596 224 -459 385 C ATOM 1324 CD2 TYR A 169 46.153 9.412 22.561 1.00 18.23 C ANISOU 1324 CD2 TYR A 169 2668 2288 1971 222 -237 -218 C ATOM 1325 CE1 TYR A 169 44.941 7.273 23.831 1.00 21.30 C ANISOU 1325 CE1 TYR A 169 2954 2082 3059 166 -200 -30 C ATOM 1326 CE2 TYR A 169 46.728 8.150 22.503 1.00 21.52 C ANISOU 1326 CE2 TYR A 169 3076 2275 2827 246 -123 -57 C ATOM 1327 CZ TYR A 169 46.110 7.097 23.138 1.00 21.63 C ANISOU 1327 CZ TYR A 169 3105 2393 2720 152 -173 -58 C ATOM 1328 OH TYR A 169 46.687 5.848 23.063 1.00 25.90 O ANISOU 1328 OH TYR A 169 3741 2549 3551 432 -377 -110 O ATOM 1329 N GLY A 170 42.208 13.337 23.208 1.00 14.66 N ANISOU 1329 N GLY A 170 2407 1359 1804 91 154 -229 N ATOM 1330 CA GLY A 170 42.016 14.772 23.268 1.00 14.12 C ANISOU 1330 CA GLY A 170 2102 1329 1934 -43 158 -307 C ATOM 1331 C GLY A 170 40.817 15.220 24.079 1.00 14.27 C ANISOU 1331 C GLY A 170 2054 1342 2026 16 57 -459 C ATOM 1332 O GLY A 170 39.897 14.478 24.405 1.00 18.00 O ANISOU 1332 O GLY A 170 2436 1685 2718 -154 457 -319 O ATOM 1333 N ARG A 171 40.831 16.506 24.423 1.00 12.14 N ANISOU 1333 N ARG A 171 1915 1269 1428 2 -124 -296 N ATOM 1334 CA ARG A 171 39.704 17.115 25.126 1.00 12.85 C ANISOU 1334 CA ARG A 171 1580 1695 1608 257 -352 -164 C ATOM 1335 C ARG A 171 39.579 18.569 24.664 1.00 12.78 C ANISOU 1335 C ARG A 171 1776 1794 1284 245 -86 12 C ATOM 1336 O ARG A 171 40.537 19.100 24.112 1.00 12.40 O ANISOU 1336 O ARG A 171 1808 1679 1226 219 -111 -106 O ATOM 1337 CB ARG A 171 39.901 17.112 26.643 1.00 15.36 C ANISOU 1337 CB ARG A 171 2037 2209 1591 -132 -326 -329 C ATOM 1338 CG ARG A 171 40.031 15.722 27.242 1.00 20.17 C ANISOU 1338 CG ARG A 171 2540 2532 2592 -339 -484 180 C ATOM 1339 CD ARG A 171 38.652 15.042 27.304 1.00 23.10 C ANISOU 1339 CD ARG A 171 2432 3576 2769 -469 -256 70 C ATOM 1340 NE ARG A 171 38.742 14.070 28.405 1.00 27.88 N ANISOU 1340 NE ARG A 171 3454 3298 3842 -239 25 369 N ATOM 1341 CZ ARG A 171 39.426 12.944 28.264 1.00 26.85 C ANISOU 1341 CZ ARG A 171 3048 3426 3726 -254 141 115 C ATOM 1342 NH1 ARG A 171 40.007 12.680 27.100 1.00 26.17 N ANISOU 1342 NH1 ARG A 171 3424 3086 3434 -317 112 340 N ATOM 1343 NH2 ARG A 171 39.487 12.121 29.295 1.00 29.48 N ANISOU 1343 NH2 ARG A 171 3565 4225 3411 -279 24 185 N ATOM 1344 N GLY A 172 38.458 19.216 24.953 1.00 13.74 N ANISOU 1344 N GLY A 172 1910 1609 1701 310 -95 -116 N ATOM 1345 CA GLY A 172 38.334 20.647 24.628 1.00 12.62 C ANISOU 1345 CA GLY A 172 1835 1533 1428 336 -99 -303 C ATOM 1346 C GLY A 172 37.963 20.851 23.168 1.00 11.76 C ANISOU 1346 C GLY A 172 1608 1377 1484 336 -76 -146 C ATOM 1347 O GLY A 172 36.846 21.228 22.836 1.00 13.93 O ANISOU 1347 O GLY A 172 1288 1880 2123 309 211 -97 O ATOM 1348 N TYR A 173 38.949 20.637 22.293 1.00 12.08 N ANISOU 1348 N TYR A 173 1568 1786 1234 106 -238 -547 N ATOM 1349 CA TYR A 173 38.686 20.667 20.862 1.00 11.35 C ANISOU 1349 CA TYR A 173 1638 1406 1270 108 -207 -42 C ATOM 1350 C TYR A 173 39.682 19.719 20.189 1.00 11.51 C ANISOU 1350 C TYR A 173 1097 1700 1578 -47 -342 -292 C ATOM 1351 O TYR A 173 40.727 19.394 20.762 1.00 12.56 O ANISOU 1351 O TYR A 173 1430 1324 2019 215 -615 -355 O ATOM 1352 CB TYR A 173 38.794 22.077 20.298 1.00 11.52 C ANISOU 1352 CB TYR A 173 1582 1520 1275 42 -255 81 C ATOM 1353 CG TYR A 173 40.170 22.664 20.121 1.00 11.55 C ANISOU 1353 CG TYR A 173 1440 1412 1535 314 6 -28 C ATOM 1354 CD1 TYR A 173 40.869 22.491 18.936 1.00 11.97 C ANISOU 1354 CD1 TYR A 173 1233 1764 1550 563 -51 112 C ATOM 1355 CD2 TYR A 173 40.771 23.415 21.122 1.00 12.58 C ANISOU 1355 CD2 TYR A 173 1269 1521 1988 251 -29 -278 C ATOM 1356 CE1 TYR A 173 42.124 23.034 18.764 1.00 13.22 C ANISOU 1356 CE1 TYR A 173 1576 1700 1747 138 -7 -104 C ATOM 1357 CE2 TYR A 173 42.028 23.967 20.971 1.00 11.44 C ANISOU 1357 CE2 TYR A 173 1302 1375 1669 140 -225 -459 C ATOM 1358 CZ TYR A 173 42.703 23.772 19.781 1.00 14.17 C ANISOU 1358 CZ TYR A 173 1700 1527 2156 227 232 -577 C ATOM 1359 OH TYR A 173 43.956 24.300 19.574 1.00 16.63 O ANISOU 1359 OH TYR A 173 2014 1674 2630 -124 371 -795 O ATOM 1360 N THR A 174 39.375 19.331 18.962 1.00 11.87 N ANISOU 1360 N THR A 174 1500 1514 1494 169 -190 -416 N ATOM 1361 CA THR A 174 40.267 18.520 18.148 1.00 11.39 C ANISOU 1361 CA THR A 174 1602 1370 1355 94 -104 -251 C ATOM 1362 C THR A 174 40.879 19.437 17.100 1.00 11.31 C ANISOU 1362 C THR A 174 1423 1657 1218 320 -251 7 C ATOM 1363 O THR A 174 40.122 20.151 16.415 1.00 13.45 O ANISOU 1363 O THR A 174 1864 1919 1327 458 -496 153 O ATOM 1364 CB THR A 174 39.524 17.381 17.422 1.00 11.85 C ANISOU 1364 CB THR A 174 1765 1398 1340 63 -175 -308 C ATOM 1365 OG1 THR A 174 38.905 16.526 18.391 1.00 13.42 O ANISOU 1365 OG1 THR A 174 1690 1661 1746 48 -211 -52 O ATOM 1366 CG2 THR A 174 40.480 16.591 16.537 1.00 13.74 C ANISOU 1366 CG2 THR A 174 1928 1531 1762 192 -18 -328 C ATOM 1367 N TYR A 175 42.183 19.453 16.959 1.00 12.17 N ANISOU 1367 N TYR A 175 1478 1802 1346 66 -169 211 N ATOM 1368 CA TYR A 175 42.815 20.308 15.957 1.00 11.17 C ANISOU 1368 CA TYR A 175 1575 1554 1114 185 -468 295 C ATOM 1369 C TYR A 175 42.817 19.554 14.634 1.00 12.19 C ANISOU 1369 C TYR A 175 1455 1646 1531 314 -518 -99 C ATOM 1370 O TYR A 175 43.403 18.477 14.528 1.00 14.30 O ANISOU 1370 O TYR A 175 1985 1776 1671 513 -661 -440 O ATOM 1371 CB TYR A 175 44.234 20.676 16.365 1.00 10.96 C ANISOU 1371 CB TYR A 175 1557 1071 1536 40 -210 4 C ATOM 1372 CG TYR A 175 44.872 21.648 15.407 1.00 11.13 C ANISOU 1372 CG TYR A 175 1411 1619 1198 -128 -219 -18 C ATOM 1373 CD1 TYR A 175 45.356 21.224 14.167 1.00 14.26 C ANISOU 1373 CD1 TYR A 175 2089 1959 1372 -20 21 -100 C ATOM 1374 CD2 TYR A 175 44.971 22.985 15.708 1.00 13.30 C ANISOU 1374 CD2 TYR A 175 1688 1531 1834 171 65 -3 C ATOM 1375 CE1 TYR A 175 45.942 22.111 13.284 1.00 14.41 C ANISOU 1375 CE1 TYR A 175 2033 2018 1423 -137 -253 22 C ATOM 1376 CE2 TYR A 175 45.534 23.897 14.831 1.00 15.58 C ANISOU 1376 CE2 TYR A 175 1794 2312 1812 -43 237 156 C ATOM 1377 CZ TYR A 175 46.023 23.445 13.622 1.00 14.27 C ANISOU 1377 CZ TYR A 175 1826 1950 1645 -85 -57 55 C ATOM 1378 OH TYR A 175 46.601 24.333 12.747 1.00 15.54 O ANISOU 1378 OH TYR A 175 2185 2679 1042 14 17 179 O ATOM 1379 N LEU A 176 42.133 20.125 13.641 1.00 13.50 N ANISOU 1379 N LEU A 176 2054 1770 1304 147 -669 -85 N ATOM 1380 CA LEU A 176 42.043 19.458 12.341 1.00 13.69 C ANISOU 1380 CA LEU A 176 1894 2075 1232 122 -306 -84 C ATOM 1381 C LEU A 176 42.932 20.187 11.347 1.00 13.18 C ANISOU 1381 C LEU A 176 1742 1963 1302 217 -278 -114 C ATOM 1382 O LEU A 176 42.665 21.338 11.025 1.00 13.88 O ANISOU 1382 O LEU A 176 2242 1855 1176 198 -438 -157 O ATOM 1383 CB LEU A 176 40.590 19.538 11.873 1.00 14.92 C ANISOU 1383 CB LEU A 176 1925 2199 1544 -36 -424 14 C ATOM 1384 CG LEU A 176 40.343 18.967 10.472 1.00 17.99 C ANISOU 1384 CG LEU A 176 2482 2493 1862 -71 -898 -181 C ATOM 1385 CD1 LEU A 176 40.599 17.475 10.430 1.00 20.51 C ANISOU 1385 CD1 LEU A 176 2958 2645 2190 226 -592 -188 C ATOM 1386 CD2 LEU A 176 38.890 19.291 10.117 1.00 19.44 C ANISOU 1386 CD2 LEU A 176 2418 2880 2087 -75 -840 37 C ATOM 1387 N LEU A 177 43.963 19.529 10.858 1.00 13.72 N ANISOU 1387 N LEU A 177 2020 1894 1297 376 -404 -409 N ATOM 1388 CA LEU A 177 44.889 20.139 9.913 1.00 16.11 C ANISOU 1388 CA LEU A 177 2189 1947 1985 85 -307 -98 C ATOM 1389 C LEU A 177 44.262 20.286 8.534 1.00 15.93 C ANISOU 1389 C LEU A 177 2039 2229 1786 -157 -108 -285 C ATOM 1390 O LEU A 177 43.680 19.315 8.061 1.00 18.52 O ANISOU 1390 O LEU A 177 2758 2412 1868 -589 -85 -242 O ATOM 1391 CB LEU A 177 46.061 19.167 9.833 1.00 20.15 C ANISOU 1391 CB LEU A 177 2354 2479 2823 390 -303 -206 C ATOM 1392 CG LEU A 177 47.498 19.574 9.701 1.00 23.03 C ANISOU 1392 CG LEU A 177 2591 2365 3796 192 -226 -76 C ATOM 1393 CD1 LEU A 177 47.866 20.847 10.423 1.00 20.29 C ANISOU 1393 CD1 LEU A 177 2551 2840 2318 419 -9 -292 C ATOM 1394 CD2 LEU A 177 48.378 18.403 10.170 1.00 20.82 C ANISOU 1394 CD2 LEU A 177 2631 2378 2902 265 -232 -121 C ATOM 1395 N SER A 178 44.396 21.433 7.901 1.00 16.32 N ANISOU 1395 N SER A 178 2240 2499 1460 -52 -341 -76 N ATOM 1396 CA SER A 178 43.847 21.664 6.565 1.00 17.51 C ANISOU 1396 CA SER A 178 2342 2765 1544 103 -310 41 C ATOM 1397 C SER A 178 44.686 20.981 5.490 1.00 18.18 C ANISOU 1397 C SER A 178 2253 2916 1739 48 -201 -51 C ATOM 1398 O SER A 178 44.189 20.720 4.387 1.00 20.06 O ANISOU 1398 O SER A 178 2711 3125 1787 -240 -252 -216 O ATOM 1399 CB ASER A 178 43.779 23.158 6.260 0.50 18.42 C ANISOU 1399 CB ASER A 178 2264 2755 1979 28 -185 39 C ATOM 1400 OG ASER A 178 45.068 23.653 5.954 0.50 18.87 O ANISOU 1400 OG ASER A 178 2404 2705 2058 -172 -160 83 O ATOM 1401 CB BSER A 178 43.886 23.164 6.261 0.80 19.19 C ANISOU 1401 CB BSER A 178 2614 2851 1826 244 -440 163 C ATOM 1402 OG BSER A 178 43.348 23.975 7.285 0.80 20.65 O ANISOU 1402 OG BSER A 178 2571 3718 1557 387 -508 48 O ATOM 1403 N ARG A 179 45.952 20.758 5.812 1.00 16.85 N ANISOU 1403 N ARG A 179 2235 2885 1283 114 -96 5 N ATOM 1404 CA ARG A 179 46.925 20.221 4.871 1.00 16.63 C ANISOU 1404 CA ARG A 179 2125 2678 1517 211 -157 0 C ATOM 1405 C ARG A 179 48.230 19.830 5.549 1.00 17.36 C ANISOU 1405 C ARG A 179 2100 3146 1350 181 -201 -275 C ATOM 1406 O ARG A 179 48.438 20.095 6.736 1.00 16.70 O ANISOU 1406 O ARG A 179 2046 3015 1282 407 -298 -293 O ATOM 1407 CB ARG A 179 47.272 21.351 3.876 1.00 16.12 C ANISOU 1407 CB ARG A 179 2274 2630 1221 34 -312 -131 C ATOM 1408 CG ARG A 179 47.683 22.660 4.541 1.00 16.53 C ANISOU 1408 CG ARG A 179 2115 2545 1620 -198 -214 16 C ATOM 1409 CD ARG A 179 48.464 23.577 3.605 1.00 15.76 C ANISOU 1409 CD ARG A 179 2298 2822 869 -151 -378 55 C ATOM 1410 NE ARG A 179 48.733 24.884 4.187 1.00 16.87 N ANISOU 1410 NE ARG A 179 2354 2740 1316 -84 -168 24 N ATOM 1411 CZ ARG A 179 49.726 25.110 5.053 1.00 16.18 C ANISOU 1411 CZ ARG A 179 2384 2251 1512 166 -319 -65 C ATOM 1412 NH1 ARG A 179 50.527 24.107 5.408 1.00 15.96 N ANISOU 1412 NH1 ARG A 179 2158 2633 1273 306 -198 -12 N ATOM 1413 NH2 ARG A 179 49.928 26.314 5.567 1.00 16.68 N ANISOU 1413 NH2 ARG A 179 3060 2259 1017 222 -371 44 N ATOM 1414 N SER A 180 49.111 19.188 4.797 1.00 16.84 N ANISOU 1414 N SER A 180 1759 3399 1241 67 -263 -242 N ATOM 1415 CA SER A 180 50.458 18.888 5.248 1.00 16.52 C ANISOU 1415 CA SER A 180 1779 3042 1457 164 -261 -431 C ATOM 1416 C SER A 180 51.249 20.192 5.230 1.00 17.03 C ANISOU 1416 C SER A 180 2186 2698 1586 344 -122 -190 C ATOM 1417 O SER A 180 50.706 21.272 4.947 1.00 17.91 O ANISOU 1417 O SER A 180 1835 3004 1966 362 -668 -112 O ATOM 1418 CB SER A 180 51.098 17.842 4.332 1.00 18.84 C ANISOU 1418 CB SER A 180 2377 2838 1942 441 -109 -340 C ATOM 1419 OG SER A 180 51.228 18.405 3.040 1.00 20.54 O ANISOU 1419 OG SER A 180 2856 3151 1798 121 -141 -478 O ATOM 1420 N GLY A 181 52.539 20.123 5.566 1.00 15.98 N ANISOU 1420 N GLY A 181 2080 2496 1494 125 -18 -389 N ATOM 1421 CA GLY A 181 53.364 21.316 5.641 1.00 16.64 C ANISOU 1421 CA GLY A 181 2313 2575 1434 -40 239 -238 C ATOM 1422 C GLY A 181 53.353 21.950 7.032 1.00 15.17 C ANISOU 1422 C GLY A 181 1963 2423 1377 12 -194 -115 C ATOM 1423 O GLY A 181 53.141 21.285 8.047 1.00 16.99 O ANISOU 1423 O GLY A 181 2443 2659 1355 14 -525 22 O ATOM 1424 N VAL A 182 53.625 23.238 7.052 1.00 16.02 N ANISOU 1424 N VAL A 182 2374 2377 1336 136 161 -293 N ATOM 1425 CA VAL A 182 53.741 24.048 8.254 1.00 15.59 C ANISOU 1425 CA VAL A 182 2382 2153 1388 -61 -98 -155 C ATOM 1426 C VAL A 182 52.809 25.248 8.199 1.00 15.90 C ANISOU 1426 C VAL A 182 2328 2401 1312 78 16 137 C ATOM 1427 O VAL A 182 52.166 25.507 7.180 1.00 15.95 O ANISOU 1427 O VAL A 182 2176 2480 1405 17 -92 60 O ATOM 1428 CB VAL A 182 55.183 24.543 8.457 1.00 15.33 C ANISOU 1428 CB VAL A 182 2234 2169 1422 -3 56 364 C ATOM 1429 CG1 VAL A 182 56.150 23.377 8.634 1.00 15.79 C ANISOU 1429 CG1 VAL A 182 2136 2584 1279 229 -129 151 C ATOM 1430 CG2 VAL A 182 55.646 25.404 7.282 1.00 14.74 C ANISOU 1430 CG2 VAL A 182 2025 2390 1185 -182 -92 311 C ATOM 1431 N THR A 183 52.705 26.005 9.293 1.00 15.31 N ANISOU 1431 N THR A 183 2178 2083 1558 245 249 105 N ATOM 1432 CA THR A 183 51.801 27.159 9.289 1.00 14.41 C ANISOU 1432 CA THR A 183 2169 2123 1183 262 11 426 C ATOM 1433 C THR A 183 52.149 28.118 8.148 1.00 14.87 C ANISOU 1433 C THR A 183 2007 2431 1212 89 107 463 C ATOM 1434 O THR A 183 53.308 28.282 7.785 1.00 15.94 O ANISOU 1434 O THR A 183 1981 2761 1315 197 46 241 O ATOM 1435 CB THR A 183 51.838 27.938 10.617 1.00 13.93 C ANISOU 1435 CB THR A 183 1724 2001 1568 -148 54 160 C ATOM 1436 OG1 THR A 183 53.170 28.394 10.892 1.00 13.62 O ANISOU 1436 OG1 THR A 183 1427 1958 1789 158 104 344 O ATOM 1437 CG2 THR A 183 51.360 27.061 11.763 1.00 14.23 C ANISOU 1437 CG2 THR A 183 1897 1775 1734 -125 202 174 C ATOM 1438 N GLY A 184 51.099 28.760 7.613 1.00 14.88 N ANISOU 1438 N GLY A 184 1886 2451 1316 171 135 311 N ATOM 1439 CA GLY A 184 51.356 29.768 6.578 1.00 17.59 C ANISOU 1439 CA GLY A 184 2583 2459 1643 -57 -128 503 C ATOM 1440 C GLY A 184 50.072 30.174 5.866 1.00 19.41 C ANISOU 1440 C GLY A 184 2783 2592 1998 59 -351 392 C ATOM 1441 O GLY A 184 49.313 29.311 5.439 1.00 20.46 O ANISOU 1441 O GLY A 184 2534 3126 2115 -53 -644 538 O ATOM 1442 N ALA A 185 49.854 31.482 5.736 1.00 21.08 N ANISOU 1442 N ALA A 185 3020 2673 2316 164 -302 531 N ATOM 1443 CA ALA A 185 48.649 31.987 5.084 1.00 23.59 C ANISOU 1443 CA ALA A 185 2886 3078 2997 270 -383 294 C ATOM 1444 C ALA A 185 48.732 31.890 3.565 1.00 28.15 C ANISOU 1444 C ALA A 185 3952 3649 3094 73 -284 284 C ATOM 1445 O ALA A 185 47.702 31.935 2.892 1.00 31.17 O ANISOU 1445 O ALA A 185 4244 3786 3814 14 -675 432 O ATOM 1446 CB ALA A 185 48.457 33.439 5.514 1.00 23.44 C ANISOU 1446 CB ALA A 185 3070 3117 2719 408 -420 311 C ATOM 1447 N GLU A 186 49.937 31.723 3.042 1.00 30.75 N ANISOU 1447 N GLU A 186 3990 3904 3790 36 -133 354 N ATOM 1448 CA GLU A 186 50.129 31.660 1.591 1.00 36.14 C ANISOU 1448 CA GLU A 186 5143 4572 4017 -34 75 0 C ATOM 1449 C GLU A 186 49.718 30.323 1.016 1.00 35.92 C ANISOU 1449 C GLU A 186 5126 4382 4141 -50 33 215 C ATOM 1450 O GLU A 186 49.294 30.261 -0.145 1.00 38.43 O ANISOU 1450 O GLU A 186 5719 4783 4099 0 -3 214 O ATOM 1451 CB GLU A 186 51.592 32.050 1.302 1.00 43.09 C ANISOU 1451 CB GLU A 186 5279 5686 5409 -36 155 265 C ATOM 1452 CG GLU A 186 51.901 33.339 2.061 1.00 50.62 C ANISOU 1452 CG GLU A 186 6718 6074 6440 -57 -44 -193 C ATOM 1453 CD GLU A 186 53.222 33.998 1.759 1.00 55.13 C ANISOU 1453 CD GLU A 186 6870 6863 7216 -111 94 107 C ATOM 1454 OE1 GLU A 186 53.890 33.624 0.773 1.00 56.91 O ANISOU 1454 OE1 GLU A 186 7312 7051 7262 -33 102 -32 O ATOM 1455 OE2 GLU A 186 53.599 34.917 2.525 1.00 57.28 O ANISOU 1455 OE2 GLU A 186 7327 7011 7424 -45 15 -48 O ATOM 1456 N ASN A 187 49.740 29.259 1.822 1.00 31.81 N ANISOU 1456 N ASN A 187 4519 4139 3427 -67 13 -101 N ATOM 1457 CA ASN A 187 49.326 27.953 1.333 1.00 28.56 C ANISOU 1457 CA ASN A 187 3931 4003 2920 -64 199 182 C ATOM 1458 C ASN A 187 47.962 27.539 1.862 1.00 26.16 C ANISOU 1458 C ASN A 187 3684 3683 2571 91 -57 174 C ATOM 1459 O ASN A 187 47.869 27.203 3.049 1.00 24.49 O ANISOU 1459 O ASN A 187 3553 3364 2389 258 -5 123 O ATOM 1460 CB ASN A 187 50.335 26.860 1.731 1.00 33.16 C ANISOU 1460 CB ASN A 187 4171 4445 3984 177 88 263 C ATOM 1461 CG ASN A 187 50.244 25.740 0.708 1.00 38.21 C ANISOU 1461 CG ASN A 187 5023 4837 4659 15 13 -143 C ATOM 1462 OD1 ASN A 187 49.319 24.933 0.711 1.00 40.42 O ANISOU 1462 OD1 ASN A 187 5156 5221 4981 -138 173 170 O ATOM 1463 ND2 ASN A 187 51.224 25.727 -0.193 1.00 42.33 N ANISOU 1463 ND2 ASN A 187 5486 5670 4928 39 215 27 N ATOM 1464 N ARG A 188 46.940 27.531 1.032 1.00 25.65 N ANISOU 1464 N ARG A 188 3631 3451 2665 -36 -89 24 N ATOM 1465 CA ARG A 188 45.602 27.142 1.443 1.00 27.64 C ANISOU 1465 CA ARG A 188 3672 3607 3222 -69 -48 131 C ATOM 1466 C ARG A 188 45.433 25.632 1.340 1.00 28.02 C ANISOU 1466 C ARG A 188 3790 3614 3242 -145 -95 157 C ATOM 1467 O ARG A 188 45.989 24.997 0.440 1.00 32.97 O ANISOU 1467 O ARG A 188 4434 4135 3957 58 132 -178 O ATOM 1468 CB ARG A 188 44.555 27.839 0.566 1.00 29.78 C ANISOU 1468 CB ARG A 188 3891 3955 3467 103 -218 110 C ATOM 1469 CG ARG A 188 44.585 29.356 0.659 1.00 34.36 C ANISOU 1469 CG ARG A 188 4623 4116 4317 -129 -61 57 C ATOM 1470 CD ARG A 188 43.308 29.949 0.081 1.00 38.28 C ANISOU 1470 CD ARG A 188 4856 4919 4770 126 -109 121 C ATOM 1471 NE ARG A 188 43.276 31.403 0.218 1.00 41.62 N ANISOU 1471 NE ARG A 188 5412 5047 5353 -35 -24 68 N ATOM 1472 CZ ARG A 188 42.156 32.111 0.097 1.00 42.99 C ANISOU 1472 CZ ARG A 188 5446 5369 5519 70 31 82 C ATOM 1473 NH1 ARG A 188 41.010 31.485 -0.150 1.00 43.48 N ANISOU 1473 NH1 ARG A 188 5650 5525 5346 -91 -92 69 N ATOM 1474 NH2 ARG A 188 42.183 33.428 0.230 1.00 43.84 N ANISOU 1474 NH2 ARG A 188 5684 5399 5575 -68 95 -30 N ATOM 1475 N GLY A 189 44.705 25.046 2.281 1.00 26.22 N ANISOU 1475 N GLY A 189 2972 3562 3428 -106 -63 -118 N ATOM 1476 CA GLY A 189 44.480 23.598 2.253 1.00 27.45 C ANISOU 1476 CA GLY A 189 3491 3514 3425 108 -111 38 C ATOM 1477 C GLY A 189 43.114 23.337 1.605 1.00 29.96 C ANISOU 1477 C GLY A 189 3378 3902 4102 242 -136 -47 C ATOM 1478 O GLY A 189 42.357 24.305 1.446 1.00 26.90 O ANISOU 1478 O GLY A 189 3495 3493 3231 -11 -733 282 O ATOM 1479 N PRO A 192 38.988 18.185 0.812 1.00 31.85 N ANISOU 1479 N PRO A 192 4016 4106 3978 -50 -25 -242 N ATOM 1480 CA PRO A 192 37.729 17.938 1.492 1.00 31.99 C ANISOU 1480 CA PRO A 192 4197 4080 3877 -85 40 -139 C ATOM 1481 C PRO A 192 37.933 17.194 2.801 1.00 32.22 C ANISOU 1481 C PRO A 192 4299 4011 3933 19 -56 -155 C ATOM 1482 O PRO A 192 38.435 16.068 2.822 1.00 33.19 O ANISOU 1482 O PRO A 192 4476 3992 4143 46 -214 -204 O ATOM 1483 CB PRO A 192 36.909 17.148 0.485 1.00 32.85 C ANISOU 1483 CB PRO A 192 4075 4281 4127 -172 19 -221 C ATOM 1484 CG PRO A 192 37.916 16.508 -0.409 1.00 33.54 C ANISOU 1484 CG PRO A 192 4220 4237 4285 -144 79 -275 C ATOM 1485 CD PRO A 192 39.067 17.471 -0.496 1.00 32.86 C ANISOU 1485 CD PRO A 192 4177 4235 4074 -149 -1 -318 C ATOM 1486 N LEU A 193 37.554 17.839 3.907 1.00 31.16 N ANISOU 1486 N LEU A 193 4354 3842 3644 -41 -216 -40 N ATOM 1487 CA LEU A 193 37.753 17.242 5.223 1.00 30.07 C ANISOU 1487 CA LEU A 193 4069 3851 3506 -116 -143 -130 C ATOM 1488 C LEU A 193 36.495 16.675 5.839 1.00 31.82 C ANISOU 1488 C LEU A 193 4295 4014 3782 -210 -57 26 C ATOM 1489 O LEU A 193 36.481 16.247 7.002 1.00 30.94 O ANISOU 1489 O LEU A 193 4084 4179 3492 -228 -157 -190 O ATOM 1490 CB LEU A 193 38.360 18.309 6.151 1.00 29.40 C ANISOU 1490 CB LEU A 193 3944 3710 3518 -214 -47 -56 C ATOM 1491 CG LEU A 193 39.668 18.941 5.664 1.00 27.91 C ANISOU 1491 CG LEU A 193 3531 3678 3397 54 -156 -177 C ATOM 1492 CD1 LEU A 193 40.247 19.878 6.720 1.00 29.70 C ANISOU 1492 CD1 LEU A 193 4034 3957 3293 -166 -62 -266 C ATOM 1493 CD2 LEU A 193 40.694 17.873 5.302 1.00 28.87 C ANISOU 1493 CD2 LEU A 193 3593 3537 3841 6 -46 -187 C ATOM 1494 N HIS A 194 35.413 16.636 5.070 1.00 35.88 N ANISOU 1494 N HIS A 194 4600 4875 4160 9 -370 2 N ATOM 1495 CA HIS A 194 34.137 16.124 5.546 1.00 38.99 C ANISOU 1495 CA HIS A 194 4943 5088 4784 -125 -17 76 C ATOM 1496 C HIS A 194 34.200 14.719 6.120 1.00 39.67 C ANISOU 1496 C HIS A 194 5141 5006 4925 4 -47 -29 C ATOM 1497 O HIS A 194 33.603 14.499 7.186 1.00 41.11 O ANISOU 1497 O HIS A 194 5456 5378 4788 -96 -93 -146 O ATOM 1498 CB HIS A 194 33.112 16.162 4.402 1.00 40.59 C ANISOU 1498 CB HIS A 194 5010 5345 5066 -60 -177 73 C ATOM 1499 CG HIS A 194 33.082 17.464 3.664 1.00 41.78 C ANISOU 1499 CG HIS A 194 5204 5320 5350 -32 -56 87 C ATOM 1500 ND1 HIS A 194 34.083 17.855 2.798 1.00 41.71 N ANISOU 1500 ND1 HIS A 194 5183 5459 5207 29 -81 62 N ATOM 1501 CD2 HIS A 194 32.164 18.460 3.648 1.00 41.95 C ANISOU 1501 CD2 HIS A 194 5275 5368 5295 43 35 -1 C ATOM 1502 CE1 HIS A 194 33.791 19.039 2.294 1.00 42.39 C ANISOU 1502 CE1 HIS A 194 5375 5418 5314 -9 69 86 C ATOM 1503 NE2 HIS A 194 32.630 19.431 2.791 1.00 42.78 N ANISOU 1503 NE2 HIS A 194 5345 5503 5406 -32 17 49 N ATOM 1504 N HIS A 195 34.861 13.769 5.459 1.00 39.11 N ANISOU 1504 N HIS A 195 5134 5044 4682 -20 38 32 N ATOM 1505 CA HIS A 195 34.903 12.401 5.969 1.00 38.47 C ANISOU 1505 CA HIS A 195 4998 5016 4601 25 -45 40 C ATOM 1506 C HIS A 195 35.679 12.283 7.279 1.00 36.69 C ANISOU 1506 C HIS A 195 4693 4727 4522 -85 19 -95 C ATOM 1507 O HIS A 195 35.344 11.417 8.090 1.00 36.98 O ANISOU 1507 O HIS A 195 4778 4994 4278 142 -155 33 O ATOM 1508 CB HIS A 195 35.455 11.393 4.960 1.00 39.86 C ANISOU 1508 CB HIS A 195 5223 5059 4862 -7 12 -80 C ATOM 1509 CG HIS A 195 35.584 9.999 5.505 1.00 40.89 C ANISOU 1509 CG HIS A 195 5337 5129 5072 23 -78 19 C ATOM 1510 ND1 HIS A 195 36.780 9.516 5.994 1.00 42.35 N ANISOU 1510 ND1 HIS A 195 5343 5284 5462 135 -36 -46 N ATOM 1511 CD2 HIS A 195 34.692 8.992 5.645 1.00 41.31 C ANISOU 1511 CD2 HIS A 195 5345 5226 5126 -27 -18 20 C ATOM 1512 CE1 HIS A 195 36.619 8.272 6.411 1.00 42.51 C ANISOU 1512 CE1 HIS A 195 5382 5357 5412 39 6 38 C ATOM 1513 NE2 HIS A 195 35.359 7.928 6.206 1.00 42.16 N ANISOU 1513 NE2 HIS A 195 5391 5355 5272 80 -26 -25 N ATOM 1514 N LEU A 196 36.710 13.087 7.475 1.00 34.51 N ANISOU 1514 N LEU A 196 4628 4493 3992 107 -156 -186 N ATOM 1515 CA LEU A 196 37.471 13.034 8.729 1.00 32.39 C ANISOU 1515 CA LEU A 196 4151 4191 3964 218 3 -51 C ATOM 1516 C LEU A 196 36.586 13.636 9.822 1.00 29.83 C ANISOU 1516 C LEU A 196 3913 3820 3600 366 -224 183 C ATOM 1517 O LEU A 196 36.433 13.115 10.933 1.00 27.69 O ANISOU 1517 O LEU A 196 3342 4053 3126 548 -645 -88 O ATOM 1518 CB LEU A 196 38.787 13.772 8.607 1.00 34.53 C ANISOU 1518 CB LEU A 196 4176 4520 4423 139 -37 57 C ATOM 1519 CG LEU A 196 40.068 13.242 9.174 1.00 36.69 C ANISOU 1519 CG LEU A 196 4751 4501 4687 86 -38 -22 C ATOM 1520 CD1 LEU A 196 40.579 12.001 8.492 1.00 37.51 C ANISOU 1520 CD1 LEU A 196 4657 5031 4564 86 -198 -3 C ATOM 1521 CD2 LEU A 196 41.105 14.312 9.369 1.00 39.15 C ANISOU 1521 CD2 LEU A 196 4934 5044 4898 67 -87 17 C ATOM 1522 N ILE A 197 35.908 14.731 9.451 1.00 27.09 N ANISOU 1522 N ILE A 197 3420 3757 3115 261 -267 70 N ATOM 1523 CA ILE A 197 35.008 15.417 10.383 1.00 24.68 C ANISOU 1523 CA ILE A 197 3128 3391 2858 161 -447 195 C ATOM 1524 C ILE A 197 33.910 14.498 10.888 1.00 26.11 C ANISOU 1524 C ILE A 197 3184 3565 3172 73 -281 127 C ATOM 1525 O ILE A 197 33.558 14.505 12.075 1.00 26.94 O ANISOU 1525 O ILE A 197 3189 4044 3003 307 -661 95 O ATOM 1526 CB ILE A 197 34.451 16.712 9.768 1.00 24.06 C ANISOU 1526 CB ILE A 197 2744 3271 3127 68 -322 197 C ATOM 1527 CG1 ILE A 197 35.535 17.798 9.713 1.00 23.30 C ANISOU 1527 CG1 ILE A 197 3091 2826 2936 97 -414 234 C ATOM 1528 CG2 ILE A 197 33.252 17.229 10.554 1.00 24.10 C ANISOU 1528 CG2 ILE A 197 3069 3414 2673 233 -329 163 C ATOM 1529 CD1 ILE A 197 35.124 18.997 8.872 1.00 24.65 C ANISOU 1529 CD1 ILE A 197 3274 2899 3191 65 -378 351 C ATOM 1530 N GLU A 198 33.355 13.649 10.028 1.00 28.56 N ANISOU 1530 N GLU A 198 3519 3952 3380 -1 -445 -51 N ATOM 1531 CA GLU A 198 32.298 12.715 10.383 1.00 31.15 C ANISOU 1531 CA GLU A 198 3848 4083 3904 -44 -165 194 C ATOM 1532 C GLU A 198 32.776 11.568 11.263 1.00 27.90 C ANISOU 1532 C GLU A 198 3359 3926 3315 -91 -316 -170 C ATOM 1533 O GLU A 198 32.107 11.172 12.223 1.00 26.99 O ANISOU 1533 O GLU A 198 2967 4172 3117 -350 -681 -183 O ATOM 1534 CB GLU A 198 31.658 12.172 9.098 1.00 36.23 C ANISOU 1534 CB GLU A 198 4731 4815 4219 -225 -183 -323 C ATOM 1535 CG GLU A 198 30.869 13.227 8.333 1.00 43.29 C ANISOU 1535 CG GLU A 198 5398 5402 5648 112 -144 215 C ATOM 1536 CD GLU A 198 30.472 12.764 6.944 1.00 48.04 C ANISOU 1536 CD GLU A 198 6190 6244 5820 -44 -75 -88 C ATOM 1537 OE1 GLU A 198 30.716 11.582 6.615 1.00 49.82 O ANISOU 1537 OE1 GLU A 198 6364 6246 6317 -33 -21 45 O ATOM 1538 OE2 GLU A 198 29.919 13.585 6.177 1.00 51.30 O ANISOU 1538 OE2 GLU A 198 6518 6550 6424 138 -136 106 O ATOM 1539 N LYS A 199 33.945 11.031 10.934 1.00 26.81 N ANISOU 1539 N LYS A 199 3459 3656 3073 18 -540 -305 N ATOM 1540 CA LYS A 199 34.536 9.948 11.720 1.00 25.77 C ANISOU 1540 CA LYS A 199 3475 3152 3163 -141 -308 -321 C ATOM 1541 C LYS A 199 34.856 10.469 13.119 1.00 23.49 C ANISOU 1541 C LYS A 199 2907 2863 3156 -72 -442 -222 C ATOM 1542 O LYS A 199 34.621 9.788 14.113 1.00 21.99 O ANISOU 1542 O LYS A 199 2728 2667 2960 -194 -764 -415 O ATOM 1543 CB LYS A 199 35.766 9.387 11.015 1.00 28.95 C ANISOU 1543 CB LYS A 199 3640 3608 3752 24 -57 -131 C ATOM 1544 CG LYS A 199 35.419 8.320 9.972 1.00 32.32 C ANISOU 1544 CG LYS A 199 4435 3945 3901 18 -101 -337 C ATOM 1545 CD LYS A 199 34.952 7.068 10.708 1.00 35.59 C ANISOU 1545 CD LYS A 199 4645 4364 4513 -82 134 -40 C ATOM 1546 CE LYS A 199 34.317 6.060 9.770 1.00 37.73 C ANISOU 1546 CE LYS A 199 4897 4668 4770 -42 -24 -255 C ATOM 1547 NZ LYS A 199 33.810 4.883 10.530 1.00 40.67 N ANISOU 1547 NZ LYS A 199 5271 5093 5088 -44 95 -14 N ATOM 1548 N LEU A 200 35.307 11.717 13.219 1.00 21.37 N ANISOU 1548 N LEU A 200 2642 2811 2667 25 -495 -218 N ATOM 1549 CA LEU A 200 35.578 12.278 14.551 1.00 19.35 C ANISOU 1549 CA LEU A 200 2358 2533 2463 -146 -402 -2 C ATOM 1550 C LEU A 200 34.300 12.363 15.367 1.00 19.38 C ANISOU 1550 C LEU A 200 2459 2398 2507 -66 -345 -166 C ATOM 1551 O LEU A 200 34.252 12.012 16.550 1.00 19.88 O ANISOU 1551 O LEU A 200 2481 2637 2436 -330 -912 -234 O ATOM 1552 CB LEU A 200 36.269 13.634 14.458 1.00 16.93 C ANISOU 1552 CB LEU A 200 2382 2319 1732 66 -416 120 C ATOM 1553 CG LEU A 200 37.734 13.637 14.025 1.00 18.09 C ANISOU 1553 CG LEU A 200 2261 2378 2236 -51 -547 -20 C ATOM 1554 CD1 LEU A 200 38.210 15.037 13.677 1.00 19.56 C ANISOU 1554 CD1 LEU A 200 2578 2495 2358 39 -408 355 C ATOM 1555 CD2 LEU A 200 38.640 13.059 15.107 1.00 18.69 C ANISOU 1555 CD2 LEU A 200 2704 2654 1741 40 -453 -37 C ATOM 1556 N LYS A 201 33.202 12.790 14.741 1.00 21.44 N ANISOU 1556 N LYS A 201 2467 2786 2893 15 -421 -179 N ATOM 1557 CA LYS A 201 31.920 12.883 15.440 1.00 22.62 C ANISOU 1557 CA LYS A 201 2681 2806 3108 30 -189 -46 C ATOM 1558 C LYS A 201 31.442 11.499 15.858 1.00 20.96 C ANISOU 1558 C LYS A 201 2267 2812 2886 49 -189 -74 C ATOM 1559 O LYS A 201 30.943 11.298 16.965 1.00 22.04 O ANISOU 1559 O LYS A 201 2347 3173 2853 -141 -305 -127 O ATOM 1560 CB LYS A 201 30.899 13.624 14.575 1.00 23.74 C ANISOU 1560 CB LYS A 201 2732 3025 3261 -24 -299 77 C ATOM 1561 CG LYS A 201 31.191 15.122 14.487 1.00 25.94 C ANISOU 1561 CG LYS A 201 3196 3020 3641 15 -285 -30 C ATOM 1562 CD LYS A 201 30.146 15.836 13.632 1.00 26.98 C ANISOU 1562 CD LYS A 201 3274 3302 3673 -43 -360 84 C ATOM 1563 CE LYS A 201 30.487 17.311 13.493 1.00 27.99 C ANISOU 1563 CE LYS A 201 3476 3233 3927 97 -257 155 C ATOM 1564 NZ LYS A 201 29.433 18.062 12.751 1.00 28.96 N ANISOU 1564 NZ LYS A 201 3463 3633 3907 42 -458 43 N ATOM 1565 N GLU A 202 31.652 10.515 14.985 1.00 22.25 N ANISOU 1565 N GLU A 202 2662 2932 2860 -168 -677 -280 N ATOM 1566 CA GLU A 202 31.299 9.134 15.281 1.00 25.06 C ANISOU 1566 CA GLU A 202 3021 3079 3422 -312 -299 -158 C ATOM 1567 C GLU A 202 31.990 8.600 16.527 1.00 23.58 C ANISOU 1567 C GLU A 202 2883 2782 3295 -211 -123 -220 C ATOM 1568 O GLU A 202 31.423 7.876 17.347 1.00 24.49 O ANISOU 1568 O GLU A 202 2820 2675 3810 -698 -119 -375 O ATOM 1569 CB GLU A 202 31.662 8.232 14.089 1.00 27.12 C ANISOU 1569 CB GLU A 202 3352 3430 3525 -128 -228 -245 C ATOM 1570 CG GLU A 202 31.349 6.770 14.355 1.00 30.26 C ANISOU 1570 CG GLU A 202 3816 3587 4096 -188 -49 -69 C ATOM 1571 CD GLU A 202 31.680 5.854 13.193 1.00 31.36 C ANISOU 1571 CD GLU A 202 4070 3794 4050 -273 -209 -208 C ATOM 1572 OE1 GLU A 202 31.899 6.336 12.065 1.00 32.68 O ANISOU 1572 OE1 GLU A 202 4365 4105 3946 -422 -323 -345 O ATOM 1573 OE2 GLU A 202 31.739 4.629 13.430 1.00 33.26 O ANISOU 1573 OE2 GLU A 202 4427 3762 4447 -320 -180 -416 O ATOM 1574 N TYR A 203 33.260 8.968 16.692 1.00 22.52 N ANISOU 1574 N TYR A 203 2878 2474 3203 -192 -207 -155 N ATOM 1575 CA TYR A 203 34.075 8.535 17.819 1.00 21.86 C ANISOU 1575 CA TYR A 203 2886 2342 3076 -199 -152 -215 C ATOM 1576 C TYR A 203 33.980 9.487 19.005 1.00 20.33 C ANISOU 1576 C TYR A 203 2549 2256 2920 -268 -318 -122 C ATOM 1577 O TYR A 203 34.709 9.361 19.984 1.00 21.24 O ANISOU 1577 O TYR A 203 3025 2028 3017 -240 -529 78 O ATOM 1578 CB TYR A 203 35.525 8.335 17.368 1.00 22.45 C ANISOU 1578 CB TYR A 203 2948 2502 3079 -65 -79 -126 C ATOM 1579 CG TYR A 203 35.704 7.366 16.219 1.00 23.32 C ANISOU 1579 CG TYR A 203 3102 2689 3069 -31 -2 -150 C ATOM 1580 CD1 TYR A 203 34.815 6.308 16.051 1.00 25.12 C ANISOU 1580 CD1 TYR A 203 3031 3044 3471 -180 -104 -168 C ATOM 1581 CD2 TYR A 203 36.747 7.482 15.317 1.00 24.37 C ANISOU 1581 CD2 TYR A 203 2846 3006 3408 -42 -48 -96 C ATOM 1582 CE1 TYR A 203 34.969 5.415 15.005 1.00 26.92 C ANISOU 1582 CE1 TYR A 203 3292 3288 3648 -130 55 -307 C ATOM 1583 CE2 TYR A 203 36.912 6.595 14.270 1.00 26.53 C ANISOU 1583 CE2 TYR A 203 3311 3369 3399 -100 59 -200 C ATOM 1584 CZ TYR A 203 36.012 5.564 14.117 1.00 27.79 C ANISOU 1584 CZ TYR A 203 3521 3412 3625 -207 129 -145 C ATOM 1585 OH TYR A 203 36.161 4.670 13.081 1.00 31.07 O ANISOU 1585 OH TYR A 203 4241 3778 3788 -107 119 -329 O ATOM 1586 N HIS A 204 33.032 10.412 18.986 1.00 19.89 N ANISOU 1586 N HIS A 204 2440 2169 2948 -386 -395 -99 N ATOM 1587 CA HIS A 204 32.760 11.346 20.060 1.00 20.68 C ANISOU 1587 CA HIS A 204 2372 2632 2853 -306 -186 -149 C ATOM 1588 C HIS A 204 33.971 12.191 20.438 1.00 17.96 C ANISOU 1588 C HIS A 204 2367 2178 2279 -179 -223 -12 C ATOM 1589 O HIS A 204 34.242 12.476 21.601 1.00 18.33 O ANISOU 1589 O HIS A 204 2557 2206 2202 -356 -57 54 O ATOM 1590 CB HIS A 204 32.228 10.599 21.292 1.00 26.12 C ANISOU 1590 CB HIS A 204 3402 3311 3212 -146 220 202 C ATOM 1591 CG HIS A 204 31.043 9.752 20.930 1.00 31.65 C ANISOU 1591 CG HIS A 204 3798 4007 4221 -478 3 -67 C ATOM 1592 ND1 HIS A 204 31.038 8.380 21.053 1.00 34.98 N ANISOU 1592 ND1 HIS A 204 4483 4158 4649 -133 -41 120 N ATOM 1593 CD2 HIS A 204 29.843 10.095 20.413 1.00 34.36 C ANISOU 1593 CD2 HIS A 204 4182 4312 4562 -11 -28 176 C ATOM 1594 CE1 HIS A 204 29.869 7.916 20.647 1.00 35.97 C ANISOU 1594 CE1 HIS A 204 4476 4336 4857 -204 27 66 C ATOM 1595 NE2 HIS A 204 29.123 8.932 20.248 1.00 36.82 N ANISOU 1595 NE2 HIS A 204 4568 4463 4961 -166 -24 46 N ATOM 1596 N ALA A 205 34.706 12.627 19.431 1.00 16.24 N ANISOU 1596 N ALA A 205 1806 1989 2375 -248 -369 -102 N ATOM 1597 CA ALA A 205 35.864 13.492 19.639 1.00 15.60 C ANISOU 1597 CA ALA A 205 1827 1722 2378 -189 -333 14 C ATOM 1598 C ALA A 205 35.400 14.892 20.035 1.00 15.06 C ANISOU 1598 C ALA A 205 1799 1738 2186 -84 -477 101 C ATOM 1599 O ALA A 205 34.281 15.331 19.774 1.00 16.98 O ANISOU 1599 O ALA A 205 1575 1920 2957 25 -247 -225 O ATOM 1600 CB ALA A 205 36.650 13.621 18.343 1.00 15.60 C ANISOU 1600 CB ALA A 205 1715 1827 2384 -211 -356 -20 C ATOM 1601 N ALA A 206 36.299 15.637 20.666 1.00 15.43 N ANISOU 1601 N ALA A 206 2022 1885 1955 -173 -483 -59 N ATOM 1602 CA ALA A 206 36.025 17.041 20.995 1.00 15.50 C ANISOU 1602 CA ALA A 206 2042 1918 1930 -12 -309 0 C ATOM 1603 C ALA A 206 35.787 17.776 19.679 1.00 14.09 C ANISOU 1603 C ALA A 206 1781 1541 2030 86 -192 20 C ATOM 1604 O ALA A 206 36.309 17.376 18.626 1.00 14.15 O ANISOU 1604 O ALA A 206 1450 1740 2185 281 -205 -69 O ATOM 1605 CB ALA A 206 37.205 17.589 21.770 1.00 14.46 C ANISOU 1605 CB ALA A 206 2356 1674 1465 -54 -270 -188 C ATOM 1606 N PRO A 207 34.990 18.838 19.684 1.00 14.71 N ANISOU 1606 N PRO A 207 1823 1655 2110 164 -178 19 N ATOM 1607 CA PRO A 207 34.658 19.571 18.463 1.00 14.30 C ANISOU 1607 CA PRO A 207 1856 1841 1736 -34 23 -41 C ATOM 1608 C PRO A 207 35.873 20.000 17.673 1.00 13.30 C ANISOU 1608 C PRO A 207 1475 1684 1895 -52 -155 -250 C ATOM 1609 O PRO A 207 36.884 20.433 18.267 1.00 13.28 O ANISOU 1609 O PRO A 207 1462 1857 1726 251 -470 -21 O ATOM 1610 CB PRO A 207 33.819 20.736 18.978 1.00 14.95 C ANISOU 1610 CB PRO A 207 1804 1826 2048 28 130 114 C ATOM 1611 CG PRO A 207 33.219 20.228 20.244 1.00 15.60 C ANISOU 1611 CG PRO A 207 2185 1715 2029 131 168 134 C ATOM 1612 CD PRO A 207 34.310 19.397 20.877 1.00 15.61 C ANISOU 1612 CD PRO A 207 1844 1939 2147 -10 54 90 C ATOM 1613 N ALA A 208 35.819 19.868 16.346 1.00 13.72 N ANISOU 1613 N ALA A 208 1799 1520 1896 -43 -71 -33 N ATOM 1614 CA ALA A 208 36.989 20.198 15.546 1.00 13.21 C ANISOU 1614 CA ALA A 208 1597 1817 1605 25 -286 33 C ATOM 1615 C ALA A 208 37.136 21.664 15.168 1.00 13.49 C ANISOU 1615 C ALA A 208 1447 1845 1833 123 -462 200 C ATOM 1616 O ALA A 208 36.188 22.336 14.771 1.00 13.89 O ANISOU 1616 O ALA A 208 1362 2072 1842 12 -628 448 O ATOM 1617 CB ALA A 208 37.010 19.394 14.248 1.00 14.09 C ANISOU 1617 CB ALA A 208 1697 1796 1860 5 -363 -169 C ATOM 1618 N LEU A 209 38.371 22.153 15.286 1.00 13.00 N ANISOU 1618 N LEU A 209 1415 1333 2191 234 -306 272 N ATOM 1619 CA LEU A 209 38.742 23.478 14.834 1.00 12.38 C ANISOU 1619 CA LEU A 209 1479 1524 1699 -138 -322 163 C ATOM 1620 C LEU A 209 39.769 23.260 13.725 1.00 12.76 C ANISOU 1620 C LEU A 209 1879 1698 1272 184 -420 242 C ATOM 1621 O LEU A 209 40.772 22.590 13.971 1.00 14.03 O ANISOU 1621 O LEU A 209 1900 1682 1747 190 -551 169 O ATOM 1622 CB LEU A 209 39.364 24.329 15.928 1.00 13.56 C ANISOU 1622 CB LEU A 209 1652 1846 1656 33 -394 -24 C ATOM 1623 CG LEU A 209 38.494 24.749 17.106 1.00 13.93 C ANISOU 1623 CG LEU A 209 1509 1957 1829 53 -260 33 C ATOM 1624 CD1 LEU A 209 39.282 25.632 18.067 1.00 14.48 C ANISOU 1624 CD1 LEU A 209 1842 1887 1773 -31 -151 -38 C ATOM 1625 CD2 LEU A 209 37.243 25.479 16.628 1.00 14.95 C ANISOU 1625 CD2 LEU A 209 1961 1683 2036 267 -322 202 C ATOM 1626 N GLN A 210 39.435 23.736 12.519 1.00 13.22 N ANISOU 1626 N GLN A 210 1779 2048 1195 -126 -527 337 N ATOM 1627 CA GLN A 210 40.359 23.556 11.405 1.00 14.78 C ANISOU 1627 CA GLN A 210 1884 2220 1510 -9 -388 -19 C ATOM 1628 C GLN A 210 41.464 24.604 11.402 1.00 13.49 C ANISOU 1628 C GLN A 210 1903 1890 1331 122 -434 109 C ATOM 1629 O GLN A 210 41.133 25.771 11.627 1.00 15.15 O ANISOU 1629 O GLN A 210 2160 1881 1714 149 -469 38 O ATOM 1630 CB GLN A 210 39.620 23.676 10.067 1.00 16.59 C ANISOU 1630 CB GLN A 210 2156 2452 1697 27 -552 195 C ATOM 1631 CG GLN A 210 40.481 23.167 8.908 1.00 20.20 C ANISOU 1631 CG GLN A 210 2650 3218 1808 -20 -387 -70 C ATOM 1632 CD GLN A 210 39.707 23.423 7.616 1.00 20.20 C ANISOU 1632 CD GLN A 210 2550 3249 1876 3 -422 -119 C ATOM 1633 OE1 GLN A 210 38.499 23.201 7.618 1.00 23.38 O ANISOU 1633 OE1 GLN A 210 2634 3686 2563 -12 -432 -197 O ATOM 1634 NE2 GLN A 210 40.422 23.909 6.630 1.00 22.28 N ANISOU 1634 NE2 GLN A 210 3116 3488 1861 -134 -400 -31 N ATOM 1635 N GLY A 211 42.706 24.199 11.165 1.00 13.96 N ANISOU 1635 N GLY A 211 1797 1895 1612 -107 -316 11 N ATOM 1636 CA GLY A 211 43.799 25.153 11.135 1.00 13.67 C ANISOU 1636 CA GLY A 211 1644 2135 1414 -127 -173 31 C ATOM 1637 C GLY A 211 44.857 24.823 10.089 1.00 15.12 C ANISOU 1637 C GLY A 211 1854 1887 2004 24 137 -30 C ATOM 1638 O GLY A 211 45.066 23.663 9.734 1.00 16.94 O ANISOU 1638 O GLY A 211 2293 1950 2193 67 48 -121 O ATOM 1639 N PHE A 212 45.571 25.846 9.669 1.00 15.02 N ANISOU 1639 N PHE A 212 2109 2220 1376 -141 -43 276 N ATOM 1640 CA PHE A 212 46.604 25.959 8.685 1.00 14.86 C ANISOU 1640 CA PHE A 212 2002 2212 1432 345 -69 364 C ATOM 1641 C PHE A 212 46.013 26.627 7.418 1.00 14.94 C ANISOU 1641 C PHE A 212 1886 2267 1526 -8 -349 371 C ATOM 1642 O PHE A 212 45.058 26.108 6.844 1.00 16.69 O ANISOU 1642 O PHE A 212 2266 2399 1678 -195 -291 -59 O ATOM 1643 CB PHE A 212 47.333 24.685 8.275 1.00 14.97 C ANISOU 1643 CB PHE A 212 1973 2253 1462 418 -388 254 C ATOM 1644 CG PHE A 212 48.475 24.241 9.157 1.00 14.40 C ANISOU 1644 CG PHE A 212 1672 2223 1578 109 -415 160 C ATOM 1645 CD1 PHE A 212 48.601 24.669 10.457 1.00 15.19 C ANISOU 1645 CD1 PHE A 212 1861 2349 1562 56 -428 168 C ATOM 1646 CD2 PHE A 212 49.425 23.365 8.663 1.00 15.33 C ANISOU 1646 CD2 PHE A 212 1844 2346 1636 -104 -1 -48 C ATOM 1647 CE1 PHE A 212 49.652 24.232 11.257 1.00 15.03 C ANISOU 1647 CE1 PHE A 212 1712 2278 1721 86 -318 284 C ATOM 1648 CE2 PHE A 212 50.484 22.923 9.430 1.00 16.94 C ANISOU 1648 CE2 PHE A 212 1975 2709 1754 22 -80 -59 C ATOM 1649 CZ PHE A 212 50.598 23.367 10.739 1.00 15.49 C ANISOU 1649 CZ PHE A 212 2009 2213 1663 -42 -69 136 C ATOM 1650 N GLY A 213 46.572 27.766 7.032 1.00 14.59 N ANISOU 1650 N GLY A 213 2339 2111 1093 20 -502 293 N ATOM 1651 CA GLY A 213 46.161 28.431 5.811 1.00 14.70 C ANISOU 1651 CA GLY A 213 2120 2034 1432 208 -482 476 C ATOM 1652 C GLY A 213 44.843 29.161 5.827 1.00 16.78 C ANISOU 1652 C GLY A 213 1964 2810 1600 259 -300 382 C ATOM 1653 O GLY A 213 44.425 29.659 4.761 1.00 18.12 O ANISOU 1653 O GLY A 213 2399 2891 1595 432 -370 470 O ATOM 1654 N ILE A 214 44.143 29.259 6.952 1.00 16.12 N ANISOU 1654 N ILE A 214 1883 2673 1568 159 -340 181 N ATOM 1655 CA ILE A 214 42.857 29.966 6.969 1.00 16.28 C ANISOU 1655 CA ILE A 214 2066 2316 1802 237 -301 381 C ATOM 1656 C ILE A 214 43.118 31.465 6.994 1.00 17.30 C ANISOU 1656 C ILE A 214 2510 2359 1705 105 -350 259 C ATOM 1657 O ILE A 214 43.642 31.954 8.001 1.00 17.83 O ANISOU 1657 O ILE A 214 2686 2473 1617 133 -505 454 O ATOM 1658 CB ILE A 214 42.013 29.573 8.195 1.00 16.60 C ANISOU 1658 CB ILE A 214 2114 2322 1870 199 -107 84 C ATOM 1659 CG1 ILE A 214 41.790 28.062 8.219 1.00 18.04 C ANISOU 1659 CG1 ILE A 214 2134 2265 2457 420 -121 18 C ATOM 1660 CG2 ILE A 214 40.703 30.343 8.246 1.00 17.26 C ANISOU 1660 CG2 ILE A 214 2064 2305 2188 170 -179 256 C ATOM 1661 CD1 ILE A 214 40.880 27.532 7.146 1.00 21.91 C ANISOU 1661 CD1 ILE A 214 2829 2595 2902 30 -328 -295 C ATOM 1662 N SER A 215 42.753 32.190 5.921 1.00 17.12 N ANISOU 1662 N SER A 215 2249 2529 1728 159 -640 222 N ATOM 1663 CA SER A 215 43.079 33.608 5.903 1.00 18.69 C ANISOU 1663 CA SER A 215 2437 2581 2082 95 -606 186 C ATOM 1664 C SER A 215 41.972 34.479 5.323 1.00 19.14 C ANISOU 1664 C SER A 215 2320 2612 2340 -147 -674 541 C ATOM 1665 O SER A 215 42.174 35.687 5.171 1.00 20.83 O ANISOU 1665 O SER A 215 2527 2597 2791 -181 -1025 480 O ATOM 1666 CB SER A 215 44.334 33.829 5.051 1.00 23.05 C ANISOU 1666 CB SER A 215 2884 3266 2607 -84 -171 156 C ATOM 1667 OG SER A 215 44.036 33.499 3.696 1.00 25.34 O ANISOU 1667 OG SER A 215 3644 3629 2354 220 -30 401 O ATOM 1668 N SER A 216 40.828 33.881 5.021 1.00 18.98 N ANISOU 1668 N SER A 216 2373 2678 2161 -214 -749 593 N ATOM 1669 CA SER A 216 39.737 34.654 4.439 1.00 18.82 C ANISOU 1669 CA SER A 216 2540 2426 2185 8 -408 643 C ATOM 1670 C SER A 216 38.404 34.212 5.012 1.00 18.12 C ANISOU 1670 C SER A 216 2229 2269 2388 24 -620 357 C ATOM 1671 O SER A 216 38.229 33.055 5.405 1.00 18.50 O ANISOU 1671 O SER A 216 2290 2517 2224 117 -1225 875 O ATOM 1672 CB SER A 216 39.691 34.459 2.914 1.00 21.07 C ANISOU 1672 CB SER A 216 2810 2795 2401 -105 -565 -51 C ATOM 1673 OG SER A 216 39.366 33.103 2.635 1.00 23.39 O ANISOU 1673 OG SER A 216 3280 2931 2678 -196 -775 -243 O ATOM 1674 N PRO A 217 37.440 35.117 4.996 1.00 17.62 N ANISOU 1674 N PRO A 217 1992 2278 2426 -70 -442 406 N ATOM 1675 CA PRO A 217 36.117 34.823 5.527 1.00 17.52 C ANISOU 1675 CA PRO A 217 2086 2192 2380 84 -220 140 C ATOM 1676 C PRO A 217 35.490 33.602 4.899 1.00 16.79 C ANISOU 1676 C PRO A 217 2007 2334 2039 -149 -125 271 C ATOM 1677 O PRO A 217 34.917 32.749 5.607 1.00 18.15 O ANISOU 1677 O PRO A 217 2465 2310 2120 66 -391 739 O ATOM 1678 CB PRO A 217 35.367 36.128 5.237 1.00 19.95 C ANISOU 1678 CB PRO A 217 2285 2279 3016 196 -249 225 C ATOM 1679 CG PRO A 217 36.444 37.167 5.333 1.00 21.06 C ANISOU 1679 CG PRO A 217 2535 2156 3308 143 0 239 C ATOM 1680 CD PRO A 217 37.603 36.537 4.599 1.00 19.21 C ANISOU 1680 CD PRO A 217 2303 2277 2721 269 -230 534 C ATOM 1681 N GLU A 218 35.595 33.429 3.588 1.00 17.26 N ANISOU 1681 N GLU A 218 2306 2316 1937 186 -534 462 N ATOM 1682 CA GLU A 218 34.960 32.288 2.924 1.00 19.07 C ANISOU 1682 CA GLU A 218 2762 2541 1943 5 -584 348 C ATOM 1683 C GLU A 218 35.534 30.963 3.399 1.00 18.35 C ANISOU 1683 C GLU A 218 2341 2480 2149 -178 -844 346 C ATOM 1684 O GLU A 218 34.830 29.952 3.403 1.00 17.34 O ANISOU 1684 O GLU A 218 2355 2592 1643 -304 -1291 483 O ATOM 1685 CB GLU A 218 35.015 32.409 1.402 1.00 20.11 C ANISOU 1685 CB GLU A 218 2640 3085 1916 304 -840 594 C ATOM 1686 CG GLU A 218 36.400 32.225 0.812 1.00 25.93 C ANISOU 1686 CG GLU A 218 2974 3715 3163 85 -240 286 C ATOM 1687 CD GLU A 218 36.438 32.398 -0.694 1.00 30.70 C ANISOU 1687 CD GLU A 218 4068 4260 3335 4 -72 318 C ATOM 1688 OE1 GLU A 218 35.358 32.619 -1.281 1.00 31.95 O ANISOU 1688 OE1 GLU A 218 4462 4426 3252 22 -306 683 O ATOM 1689 OE2 GLU A 218 37.556 32.307 -1.247 1.00 34.25 O ANISOU 1689 OE2 GLU A 218 4234 4602 4176 66 121 233 O ATOM 1690 N GLN A 219 36.783 30.948 3.863 1.00 17.42 N ANISOU 1690 N GLN A 219 2394 2100 2127 -1 -966 -79 N ATOM 1691 CA GLN A 219 37.327 29.697 4.400 1.00 16.71 C ANISOU 1691 CA GLN A 219 2083 2126 2141 -19 -566 72 C ATOM 1692 C GLN A 219 36.722 29.371 5.758 1.00 16.92 C ANISOU 1692 C GLN A 219 2444 1968 2016 67 -582 72 C ATOM 1693 O GLN A 219 36.546 28.183 6.052 1.00 16.73 O ANISOU 1693 O GLN A 219 2415 2258 1685 -157 -1160 592 O ATOM 1694 CB GLN A 219 38.838 29.793 4.512 1.00 16.13 C ANISOU 1694 CB GLN A 219 2038 2129 1962 49 -714 99 C ATOM 1695 CG GLN A 219 39.571 29.746 3.185 1.00 16.50 C ANISOU 1695 CG GLN A 219 2313 2146 1811 63 -713 378 C ATOM 1696 CD GLN A 219 41.051 30.000 3.442 1.00 17.31 C ANISOU 1696 CD GLN A 219 2299 2098 2181 -40 -578 181 C ATOM 1697 OE1 GLN A 219 41.375 31.153 3.741 1.00 17.41 O ANISOU 1697 OE1 GLN A 219 2469 1860 2286 -131 -1035 819 O ATOM 1698 NE2 GLN A 219 41.879 28.966 3.400 1.00 17.96 N ANISOU 1698 NE2 GLN A 219 2752 2275 1796 168 -358 -175 N ATOM 1699 N VAL A 220 36.362 30.383 6.541 1.00 15.81 N ANISOU 1699 N VAL A 220 2297 2127 1584 196 -869 105 N ATOM 1700 CA VAL A 220 35.697 30.173 7.824 1.00 16.43 C ANISOU 1700 CA VAL A 220 2010 2289 1944 158 -607 64 C ATOM 1701 C VAL A 220 34.316 29.565 7.586 1.00 16.59 C ANISOU 1701 C VAL A 220 2327 2363 1616 -107 -830 208 C ATOM 1702 O VAL A 220 33.945 28.545 8.154 1.00 18.27 O ANISOU 1702 O VAL A 220 2154 2650 2140 -166 -1195 645 O ATOM 1703 CB VAL A 220 35.589 31.480 8.632 1.00 16.30 C ANISOU 1703 CB VAL A 220 2075 2142 1978 -142 -572 136 C ATOM 1704 CG1 VAL A 220 34.771 31.317 9.898 1.00 16.27 C ANISOU 1704 CG1 VAL A 220 2039 2115 2025 233 -519 232 C ATOM 1705 CG2 VAL A 220 36.978 32.014 8.958 1.00 17.43 C ANISOU 1705 CG2 VAL A 220 1757 2610 2257 152 -613 300 C ATOM 1706 N SER A 221 33.557 30.163 6.646 1.00 17.49 N ANISOU 1706 N SER A 221 2258 2345 2041 392 -918 64 N ATOM 1707 CA SER A 221 32.230 29.620 6.355 1.00 17.00 C ANISOU 1707 CA SER A 221 2107 2209 2145 310 -532 277 C ATOM 1708 C SER A 221 32.302 28.211 5.776 1.00 14.26 C ANISOU 1708 C SER A 221 1639 2164 1617 65 -791 373 C ATOM 1709 O SER A 221 31.476 27.341 6.100 1.00 16.61 O ANISOU 1709 O SER A 221 2388 2011 1910 -280 -1217 645 O ATOM 1710 CB SER A 221 31.411 30.537 5.434 1.00 18.28 C ANISOU 1710 CB SER A 221 2183 2581 2182 535 -471 343 C ATOM 1711 OG SER A 221 32.012 30.763 4.180 1.00 21.07 O ANISOU 1711 OG SER A 221 2311 3281 2414 270 -270 260 O ATOM 1712 N ALA A 222 33.288 27.941 4.949 1.00 15.61 N ANISOU 1712 N ALA A 222 1937 2201 1793 520 -757 351 N ATOM 1713 CA ALA A 222 33.447 26.625 4.338 1.00 16.86 C ANISOU 1713 CA ALA A 222 2240 1914 2253 175 -576 446 C ATOM 1714 C ALA A 222 33.766 25.567 5.402 1.00 18.64 C ANISOU 1714 C ALA A 222 2515 2100 2467 224 -751 579 C ATOM 1715 O ALA A 222 33.217 24.469 5.352 1.00 18.05 O ANISOU 1715 O ALA A 222 2506 2053 2299 333 -1075 387 O ATOM 1716 CB ALA A 222 34.541 26.661 3.287 1.00 18.78 C ANISOU 1716 CB ALA A 222 2666 2168 2303 169 -364 -100 C ATOM 1717 N ALA A 223 34.646 25.922 6.339 1.00 18.71 N ANISOU 1717 N ALA A 223 2832 1989 2290 52 -661 416 N ATOM 1718 CA ALA A 223 35.019 24.960 7.386 1.00 17.80 C ANISOU 1718 CA ALA A 223 2483 2080 2199 -156 -812 399 C ATOM 1719 C ALA A 223 33.785 24.544 8.170 1.00 17.42 C ANISOU 1719 C ALA A 223 2429 2184 2007 16 -847 398 C ATOM 1720 O ALA A 223 33.567 23.358 8.457 1.00 19.26 O ANISOU 1720 O ALA A 223 2792 2383 2143 -226 -1322 856 O ATOM 1721 CB ALA A 223 36.063 25.571 8.305 1.00 17.08 C ANISOU 1721 CB ALA A 223 1988 2063 2441 99 -799 405 C ATOM 1722 N VAL A 224 33.005 25.531 8.588 1.00 17.14 N ANISOU 1722 N VAL A 224 2377 2412 1723 124 -729 498 N ATOM 1723 CA VAL A 224 31.799 25.299 9.366 1.00 19.05 C ANISOU 1723 CA VAL A 224 2702 2415 2121 -190 -377 317 C ATOM 1724 C VAL A 224 30.789 24.494 8.564 1.00 18.71 C ANISOU 1724 C VAL A 224 2408 2718 1983 7 -574 442 C ATOM 1725 O VAL A 224 30.196 23.537 9.062 1.00 20.34 O ANISOU 1725 O VAL A 224 2699 2615 2416 -187 -1070 557 O ATOM 1726 CB VAL A 224 31.202 26.609 9.890 1.00 20.97 C ANISOU 1726 CB VAL A 224 2869 2637 2461 -277 -80 29 C ATOM 1727 CG1 VAL A 224 29.867 26.412 10.594 1.00 23.43 C ANISOU 1727 CG1 VAL A 224 3016 3021 2866 -366 94 -52 C ATOM 1728 CG2 VAL A 224 32.200 27.285 10.830 1.00 23.37 C ANISOU 1728 CG2 VAL A 224 3412 3235 2232 -313 -173 -212 C ATOM 1729 N ARG A 225 30.601 24.858 7.293 1.00 18.83 N ANISOU 1729 N ARG A 225 2398 2554 2204 -3 -864 638 N ATOM 1730 CA ARG A 225 29.652 24.117 6.454 1.00 20.67 C ANISOU 1730 CA ARG A 225 2657 2583 2616 -159 -731 239 C ATOM 1731 C ARG A 225 30.058 22.661 6.326 1.00 20.96 C ANISOU 1731 C ARG A 225 2562 2683 2719 -11 -720 353 C ATOM 1732 O ARG A 225 29.215 21.760 6.261 1.00 21.47 O ANISOU 1732 O ARG A 225 2354 3217 2588 -168 -1438 635 O ATOM 1733 CB ARG A 225 29.579 24.813 5.096 1.00 22.59 C ANISOU 1733 CB ARG A 225 3102 2965 2515 -6 -400 255 C ATOM 1734 CG ARG A 225 28.507 24.241 4.187 1.00 22.86 C ANISOU 1734 CG ARG A 225 3017 3014 2655 149 -643 569 C ATOM 1735 CD ARG A 225 28.075 25.355 3.225 1.00 22.62 C ANISOU 1735 CD ARG A 225 2787 3933 1876 168 -1162 577 C ATOM 1736 NE ARG A 225 29.201 25.893 2.510 1.00 21.75 N ANISOU 1736 NE ARG A 225 2702 3115 2446 -67 -1516 687 N ATOM 1737 CZ ARG A 225 29.797 27.077 2.597 1.00 19.08 C ANISOU 1737 CZ ARG A 225 2711 2788 1749 187 -1071 698 C ATOM 1738 NH1 ARG A 225 29.386 28.050 3.386 1.00 20.87 N ANISOU 1738 NH1 ARG A 225 3365 2748 1818 199 -1512 607 N ATOM 1739 NH2 ARG A 225 30.825 27.252 1.780 1.00 16.20 N ANISOU 1739 NH2 ARG A 225 2791 2155 1210 -255 -1466 449 N ATOM 1740 N ALA A 226 31.357 22.386 6.348 1.00 19.03 N ANISOU 1740 N ALA A 226 2421 1987 2824 -242 -891 129 N ATOM 1741 CA ALA A 226 31.894 21.039 6.274 1.00 19.18 C ANISOU 1741 CA ALA A 226 2535 2226 2528 46 -341 19 C ATOM 1742 C ALA A 226 31.701 20.255 7.572 1.00 19.50 C ANISOU 1742 C ALA A 226 2415 2570 2424 68 -574 78 C ATOM 1743 O ALA A 226 31.944 19.047 7.558 1.00 21.38 O ANISOU 1743 O ALA A 226 2805 2592 2727 40 -1101 200 O ATOM 1744 CB ALA A 226 33.376 21.032 5.936 1.00 19.74 C ANISOU 1744 CB ALA A 226 2488 2014 2997 216 -381 204 C ATOM 1745 N GLY A 227 31.260 20.904 8.641 1.00 19.63 N ANISOU 1745 N GLY A 227 2530 2860 2069 -92 -776 92 N ATOM 1746 CA GLY A 227 31.010 20.170 9.876 1.00 20.23 C ANISOU 1746 CA GLY A 227 2405 3059 2224 -170 -719 238 C ATOM 1747 C GLY A 227 32.001 20.500 10.985 1.00 20.55 C ANISOU 1747 C GLY A 227 2439 3100 2271 -290 -706 208 C ATOM 1748 O GLY A 227 31.778 20.015 12.104 1.00 20.83 O ANISOU 1748 O GLY A 227 2556 3103 2254 -389 -1042 339 O ATOM 1749 N ALA A 228 32.985 21.346 10.699 1.00 19.59 N ANISOU 1749 N ALA A 228 2298 2862 2285 -187 -892 112 N ATOM 1750 CA ALA A 228 33.917 21.707 11.780 1.00 17.05 C ANISOU 1750 CA ALA A 228 2045 2535 1899 -53 -626 181 C ATOM 1751 C ALA A 228 33.192 22.699 12.688 1.00 16.49 C ANISOU 1751 C ALA A 228 1756 2288 2221 76 -693 277 C ATOM 1752 O ALA A 228 32.306 23.441 12.250 1.00 19.29 O ANISOU 1752 O ALA A 228 1998 2665 2666 26 -1234 573 O ATOM 1753 CB ALA A 228 35.204 22.310 11.273 1.00 17.09 C ANISOU 1753 CB ALA A 228 2242 2432 1817 -48 -394 177 C ATOM 1754 N ALA A 229 33.608 22.746 13.943 1.00 15.48 N ANISOU 1754 N ALA A 229 1677 2225 1980 196 -389 197 N ATOM 1755 CA ALA A 229 33.022 23.652 14.919 1.00 14.72 C ANISOU 1755 CA ALA A 229 1195 2057 2341 103 -508 20 C ATOM 1756 C ALA A 229 33.564 25.067 14.796 1.00 15.82 C ANISOU 1756 C ALA A 229 1433 2116 2460 55 -179 153 C ATOM 1757 O ALA A 229 33.040 26.012 15.398 1.00 18.32 O ANISOU 1757 O ALA A 229 1591 1775 3593 0 -117 0 O ATOM 1758 CB ALA A 229 33.212 23.103 16.322 1.00 16.49 C ANISOU 1758 CB ALA A 229 1640 2282 2343 47 -177 170 C ATOM 1759 N GLY A 230 34.641 25.230 14.041 1.00 14.33 N ANISOU 1759 N GLY A 230 1318 1524 2602 26 -224 317 N ATOM 1760 CA GLY A 230 35.248 26.549 13.894 1.00 14.17 C ANISOU 1760 CA GLY A 230 1574 1537 2274 30 -266 595 C ATOM 1761 C GLY A 230 36.587 26.447 13.179 1.00 13.05 C ANISOU 1761 C GLY A 230 1577 1415 1966 163 -395 516 C ATOM 1762 O GLY A 230 36.955 25.409 12.644 1.00 13.71 O ANISOU 1762 O GLY A 230 1544 1831 1834 416 -858 211 O ATOM 1763 N ALA A 231 37.282 27.584 13.172 1.00 12.78 N ANISOU 1763 N ALA A 231 1573 1633 1650 -14 -611 508 N ATOM 1764 CA ALA A 231 38.541 27.696 12.467 1.00 13.55 C ANISOU 1764 CA ALA A 231 1495 1951 1702 135 -640 578 C ATOM 1765 C ALA A 231 39.510 28.594 13.227 1.00 13.14 C ANISOU 1765 C ALA A 231 1656 1472 1864 297 -454 262 C ATOM 1766 O ALA A 231 39.121 29.540 13.907 1.00 14.33 O ANISOU 1766 O ALA A 231 1739 1902 1803 305 -376 37 O ATOM 1767 CB ALA A 231 38.309 28.325 11.088 1.00 16.22 C ANISOU 1767 CB ALA A 231 2450 2127 1586 55 -602 544 C ATOM 1768 N ILE A 232 40.781 28.214 13.107 1.00 12.56 N ANISOU 1768 N ILE A 232 1540 1434 1798 82 -89 273 N ATOM 1769 CA ILE A 232 41.884 28.950 13.709 1.00 12.47 C ANISOU 1769 CA ILE A 232 1629 1614 1494 156 -340 383 C ATOM 1770 C ILE A 232 42.655 29.665 12.606 1.00 12.02 C ANISOU 1770 C ILE A 232 1719 1275 1574 32 -229 201 C ATOM 1771 O ILE A 232 42.842 29.032 11.557 1.00 13.51 O ANISOU 1771 O ILE A 232 2093 1714 1326 -3 -291 231 O ATOM 1772 CB ILE A 232 42.839 27.980 14.438 1.00 13.26 C ANISOU 1772 CB ILE A 232 1689 1688 1661 111 -453 445 C ATOM 1773 CG1 ILE A 232 42.141 27.384 15.649 1.00 12.91 C ANISOU 1773 CG1 ILE A 232 1314 1844 1746 -102 -497 390 C ATOM 1774 CG2 ILE A 232 44.127 28.688 14.815 1.00 13.15 C ANISOU 1774 CG2 ILE A 232 1696 2151 1150 -90 -246 484 C ATOM 1775 CD1 ILE A 232 42.797 26.127 16.195 1.00 13.58 C ANISOU 1775 CD1 ILE A 232 1847 1710 1603 168 -161 223 C ATOM 1776 N SER A 233 43.061 30.910 12.822 1.00 12.67 N ANISOU 1776 N SER A 233 2087 1384 1342 -36 -365 176 N ATOM 1777 CA SER A 233 43.818 31.666 11.830 1.00 13.42 C ANISOU 1777 CA SER A 233 1955 1706 1439 -15 -266 236 C ATOM 1778 C SER A 233 45.000 32.315 12.534 1.00 12.83 C ANISOU 1778 C SER A 233 1788 1852 1236 63 -159 227 C ATOM 1779 O SER A 233 44.759 33.029 13.518 1.00 13.81 O ANISOU 1779 O SER A 233 1938 2002 1307 467 -258 201 O ATOM 1780 CB SER A 233 42.940 32.764 11.222 1.00 14.46 C ANISOU 1780 CB SER A 233 2199 1534 1761 45 -262 262 C ATOM 1781 OG SER A 233 43.649 33.577 10.311 1.00 16.03 O ANISOU 1781 OG SER A 233 2127 2371 1593 -143 -383 427 O ATOM 1782 N GLY A 234 46.216 31.994 12.092 1.00 12.77 N ANISOU 1782 N GLY A 234 1601 1871 1380 -229 -186 184 N ATOM 1783 CA GLY A 234 47.390 32.554 12.758 1.00 11.40 C ANISOU 1783 CA GLY A 234 1509 1946 875 -14 -235 274 C ATOM 1784 C GLY A 234 48.202 33.462 11.856 1.00 10.40 C ANISOU 1784 C GLY A 234 1640 1084 1228 -135 -350 46 C ATOM 1785 O GLY A 234 48.237 34.672 12.102 1.00 12.77 O ANISOU 1785 O GLY A 234 2376 1073 1402 -314 -156 110 O ATOM 1786 N SER A 235 48.842 32.894 10.846 1.00 12.28 N ANISOU 1786 N SER A 235 1635 1951 1079 67 -99 308 N ATOM 1787 CA SER A 235 49.694 33.665 9.943 1.00 13.58 C ANISOU 1787 CA SER A 235 2032 1719 1409 276 40 579 C ATOM 1788 C SER A 235 48.990 34.892 9.366 1.00 13.52 C ANISOU 1788 C SER A 235 2023 1687 1427 160 -336 502 C ATOM 1789 O SER A 235 49.609 35.961 9.338 1.00 13.99 O ANISOU 1789 O SER A 235 2315 1675 1325 140 -170 499 O ATOM 1790 CB SER A 235 50.244 32.764 8.842 1.00 13.75 C ANISOU 1790 CB SER A 235 1921 1963 1342 310 -135 429 C ATOM 1791 OG SER A 235 51.143 31.795 9.372 1.00 15.49 O ANISOU 1791 OG SER A 235 2016 2616 1254 480 -147 715 O ATOM 1792 N ALA A 236 47.708 34.786 9.010 1.00 14.60 N ANISOU 1792 N ALA A 236 2108 2119 1321 201 -333 673 N ATOM 1793 CA ALA A 236 47.023 35.966 8.484 1.00 14.01 C ANISOU 1793 CA ALA A 236 1801 2031 1491 300 -478 286 C ATOM 1794 C ALA A 236 46.934 37.090 9.497 1.00 15.11 C ANISOU 1794 C ALA A 236 2138 1777 1827 251 -296 302 C ATOM 1795 O ALA A 236 46.966 38.274 9.136 1.00 19.30 O ANISOU 1795 O ALA A 236 2970 1879 2485 67 -350 515 O ATOM 1796 CB ALA A 236 45.640 35.568 8.006 1.00 15.63 C ANISOU 1796 CB ALA A 236 1939 2034 1966 -138 -327 104 C ATOM 1797 N ILE A 237 46.778 36.744 10.775 1.00 16.21 N ANISOU 1797 N ILE A 237 2349 2049 1763 177 -320 301 N ATOM 1798 CA ILE A 237 46.705 37.710 11.857 1.00 14.57 C ANISOU 1798 CA ILE A 237 1991 1677 1869 193 -298 406 C ATOM 1799 C ILE A 237 48.095 38.298 12.098 1.00 14.64 C ANISOU 1799 C ILE A 237 2054 1726 1781 134 -240 350 C ATOM 1800 O ILE A 237 48.305 39.492 12.244 1.00 16.24 O ANISOU 1800 O ILE A 237 2676 1676 1817 21 -207 661 O ATOM 1801 CB ILE A 237 46.244 37.049 13.180 1.00 15.69 C ANISOU 1801 CB ILE A 237 1966 2276 1721 179 39 154 C ATOM 1802 CG1 ILE A 237 44.852 36.436 13.083 1.00 19.20 C ANISOU 1802 CG1 ILE A 237 2303 2512 2482 -88 -289 -198 C ATOM 1803 CG2 ILE A 237 46.345 38.019 14.345 1.00 17.47 C ANISOU 1803 CG2 ILE A 237 2423 2410 1803 62 330 75 C ATOM 1804 CD1 ILE A 237 43.709 37.371 13.354 1.00 22.74 C ANISOU 1804 CD1 ILE A 237 2433 3133 3073 210 -264 -220 C ATOM 1805 N VAL A 238 49.082 37.393 12.183 1.00 14.79 N ANISOU 1805 N VAL A 238 1851 1862 1907 99 -160 537 N ATOM 1806 CA VAL A 238 50.457 37.802 12.452 1.00 13.40 C ANISOU 1806 CA VAL A 238 1885 1637 1570 -52 -42 503 C ATOM 1807 C VAL A 238 50.972 38.741 11.368 1.00 14.57 C ANISOU 1807 C VAL A 238 2016 1761 1759 -376 -29 504 C ATOM 1808 O VAL A 238 51.768 39.652 11.657 1.00 15.12 O ANISOU 1808 O VAL A 238 2184 1498 2062 -251 -130 522 O ATOM 1809 CB VAL A 238 51.348 36.572 12.662 1.00 14.52 C ANISOU 1809 CB VAL A 238 1721 1900 1897 2 -94 471 C ATOM 1810 CG1 VAL A 238 52.809 36.951 12.883 1.00 15.44 C ANISOU 1810 CG1 VAL A 238 1715 2229 1921 -158 -56 473 C ATOM 1811 CG2 VAL A 238 50.834 35.760 13.858 1.00 14.61 C ANISOU 1811 CG2 VAL A 238 2102 1631 1818 -251 -201 336 C ATOM 1812 N LYS A 239 50.558 38.516 10.113 1.00 15.08 N ANISOU 1812 N LYS A 239 2145 1774 1811 -272 -23 404 N ATOM 1813 CA LYS A 239 51.017 39.401 9.037 1.00 16.02 C ANISOU 1813 CA LYS A 239 2357 1890 1839 -223 -42 534 C ATOM 1814 C LYS A 239 50.569 40.843 9.254 1.00 17.12 C ANISOU 1814 C LYS A 239 2110 2052 2342 -138 -56 373 C ATOM 1815 O LYS A 239 51.245 41.779 8.810 1.00 17.87 O ANISOU 1815 O LYS A 239 2203 2244 2342 -105 -115 818 O ATOM 1816 CB LYS A 239 50.477 38.928 7.684 1.00 18.47 C ANISOU 1816 CB LYS A 239 2616 2291 2111 -191 -233 243 C ATOM 1817 CG LYS A 239 51.174 37.700 7.128 1.00 20.91 C ANISOU 1817 CG LYS A 239 2898 2569 2479 145 -1 334 C ATOM 1818 CD LYS A 239 50.400 37.153 5.925 1.00 27.45 C ANISOU 1818 CD LYS A 239 3696 3453 3282 -175 -345 -151 C ATOM 1819 CE LYS A 239 51.270 36.152 5.179 1.00 31.36 C ANISOU 1819 CE LYS A 239 4141 3879 3893 163 -46 -111 C ATOM 1820 NZ LYS A 239 52.576 36.764 4.804 1.00 35.98 N ANISOU 1820 NZ LYS A 239 4520 4430 4719 -126 -141 47 N ATOM 1821 N ILE A 240 49.404 41.014 9.851 1.00 15.67 N ANISOU 1821 N ILE A 240 2291 1771 1893 151 -6 480 N ATOM 1822 CA ILE A 240 48.892 42.361 10.143 1.00 14.80 C ANISOU 1822 CA ILE A 240 2307 1594 1722 -36 -216 457 C ATOM 1823 C ILE A 240 49.808 43.018 11.165 1.00 16.60 C ANISOU 1823 C ILE A 240 2570 1570 2169 -166 -346 284 C ATOM 1824 O ILE A 240 50.107 44.210 11.048 1.00 18.34 O ANISOU 1824 O ILE A 240 2684 1819 2463 -683 -203 364 O ATOM 1825 CB ILE A 240 47.425 42.325 10.568 1.00 15.98 C ANISOU 1825 CB ILE A 240 2342 1931 1798 17 -189 326 C ATOM 1826 CG1 ILE A 240 46.536 41.826 9.419 1.00 15.84 C ANISOU 1826 CG1 ILE A 240 2064 2026 1930 -3 -170 302 C ATOM 1827 CG2 ILE A 240 46.959 43.684 11.055 1.00 17.65 C ANISOU 1827 CG2 ILE A 240 2586 1803 2318 -19 -180 344 C ATOM 1828 CD1 ILE A 240 45.125 41.453 9.831 1.00 16.99 C ANISOU 1828 CD1 ILE A 240 1791 2002 2663 188 -351 203 C ATOM 1829 N ILE A 241 50.293 42.265 12.152 1.00 16.38 N ANISOU 1829 N ILE A 241 2521 1775 1929 -381 -148 441 N ATOM 1830 CA ILE A 241 51.261 42.801 13.114 1.00 14.89 C ANISOU 1830 CA ILE A 241 2210 1551 1895 -168 -8 372 C ATOM 1831 C ILE A 241 52.533 43.215 12.383 1.00 15.62 C ANISOU 1831 C ILE A 241 2217 1485 2231 -54 139 357 C ATOM 1832 O ILE A 241 53.047 44.338 12.501 1.00 18.88 O ANISOU 1832 O ILE A 241 2776 1720 2678 -507 180 633 O ATOM 1833 CB ILE A 241 51.583 41.748 14.189 1.00 14.97 C ANISOU 1833 CB ILE A 241 2022 1869 1795 -5 -508 245 C ATOM 1834 CG1 ILE A 241 50.307 41.417 14.973 1.00 15.39 C ANISOU 1834 CG1 ILE A 241 2506 1715 1626 140 -206 525 C ATOM 1835 CG2 ILE A 241 52.676 42.232 15.135 1.00 14.59 C ANISOU 1835 CG2 ILE A 241 1760 1990 1793 131 -475 237 C ATOM 1836 CD1 ILE A 241 50.450 40.233 15.915 1.00 15.40 C ANISOU 1836 CD1 ILE A 241 2462 1482 1909 -330 -343 587 C ATOM 1837 N GLU A 242 53.086 42.299 11.613 1.00 15.94 N ANISOU 1837 N GLU A 242 2533 1777 1748 -102 219 317 N ATOM 1838 CA GLU A 242 54.320 42.498 10.851 1.00 18.66 C ANISOU 1838 CA GLU A 242 2740 2262 2087 -205 391 542 C ATOM 1839 C GLU A 242 54.231 43.716 9.930 1.00 20.44 C ANISOU 1839 C GLU A 242 2918 2424 2424 -272 101 714 C ATOM 1840 O GLU A 242 55.171 44.514 9.891 1.00 23.82 O ANISOU 1840 O GLU A 242 3303 2490 3255 -512 -1 790 O ATOM 1841 CB GLU A 242 54.630 41.251 10.016 1.00 19.33 C ANISOU 1841 CB GLU A 242 2847 2450 2049 -78 313 446 C ATOM 1842 CG GLU A 242 55.937 41.312 9.234 1.00 22.93 C ANISOU 1842 CG GLU A 242 3021 3150 2541 -32 493 597 C ATOM 1843 CD GLU A 242 56.164 40.075 8.389 1.00 29.75 C ANISOU 1843 CD GLU A 242 4152 3623 3528 -9 260 12 C ATOM 1844 OE1 GLU A 242 55.368 39.111 8.455 1.00 29.45 O ANISOU 1844 OE1 GLU A 242 4246 3730 3215 -63 276 207 O ATOM 1845 OE2 GLU A 242 57.164 40.055 7.635 1.00 33.42 O ANISOU 1845 OE2 GLU A 242 4364 4228 4108 -31 486 178 O ATOM 1846 N LYS A 243 53.105 43.844 9.241 1.00 19.87 N ANISOU 1846 N LYS A 243 3099 2659 1793 -310 127 789 N ATOM 1847 CA LYS A 243 52.965 44.975 8.305 1.00 20.84 C ANISOU 1847 CA LYS A 243 3289 2266 2363 -339 30 752 C ATOM 1848 C LYS A 243 52.911 46.339 8.962 1.00 22.11 C ANISOU 1848 C LYS A 243 3369 2475 2556 -163 105 527 C ATOM 1849 O LYS A 243 53.317 47.348 8.358 1.00 25.10 O ANISOU 1849 O LYS A 243 3918 2271 3347 -145 213 664 O ATOM 1850 CB LYS A 243 51.682 44.754 7.484 1.00 25.62 C ANISOU 1850 CB LYS A 243 3495 3334 2904 -306 -216 319 C ATOM 1851 CG LYS A 243 51.205 45.979 6.727 1.00 30.06 C ANISOU 1851 CG LYS A 243 4151 3649 3623 15 -111 502 C ATOM 1852 CD LYS A 243 50.092 45.639 5.743 1.00 35.09 C ANISOU 1852 CD LYS A 243 4488 4552 4294 -157 -293 50 C ATOM 1853 CE LYS A 243 49.711 46.897 4.967 1.00 38.19 C ANISOU 1853 CE LYS A 243 4965 4649 4895 22 -249 176 C ATOM 1854 NZ LYS A 243 49.174 46.580 3.619 1.00 41.27 N ANISOU 1854 NZ LYS A 243 5408 5215 5057 -5 -155 -2 N ATOM 1855 N ASN A 244 52.378 46.447 10.159 1.00 19.93 N ANISOU 1855 N ASN A 244 3073 1957 2540 -272 46 575 N ATOM 1856 CA ASN A 244 52.144 47.669 10.886 1.00 18.63 C ANISOU 1856 CA ASN A 244 2887 1966 2227 -424 20 612 C ATOM 1857 C ASN A 244 52.986 47.900 12.128 1.00 17.43 C ANISOU 1857 C ASN A 244 2531 1720 2372 -422 31 650 C ATOM 1858 O ASN A 244 52.542 48.637 13.024 1.00 20.82 O ANISOU 1858 O ASN A 244 3041 1928 2941 -445 240 348 O ATOM 1859 CB ASN A 244 50.660 47.684 11.288 1.00 19.75 C ANISOU 1859 CB ASN A 244 2894 1788 2821 -280 47 557 C ATOM 1860 CG ASN A 244 49.700 47.742 10.135 1.00 23.07 C ANISOU 1860 CG ASN A 244 3095 2512 3160 -226 -191 340 C ATOM 1861 OD1 ASN A 244 49.520 48.807 9.523 1.00 25.79 O ANISOU 1861 OD1 ASN A 244 3586 2769 3443 -466 -138 739 O ATOM 1862 ND2 ASN A 244 49.040 46.633 9.806 1.00 21.54 N ANISOU 1862 ND2 ASN A 244 3142 2018 3025 -126 -52 781 N ATOM 1863 N LEU A 245 54.204 47.377 12.170 1.00 17.79 N ANISOU 1863 N LEU A 245 2557 1611 2589 -425 271 740 N ATOM 1864 CA LEU A 245 55.048 47.573 13.341 1.00 20.25 C ANISOU 1864 CA LEU A 245 2691 2221 2782 -262 134 340 C ATOM 1865 C LEU A 245 55.264 49.046 13.670 1.00 22.07 C ANISOU 1865 C LEU A 245 3043 2345 2996 -222 135 44 C ATOM 1866 O LEU A 245 55.347 49.398 14.843 1.00 23.29 O ANISOU 1866 O LEU A 245 3562 2113 3176 -465 13 -77 O ATOM 1867 CB LEU A 245 56.405 46.883 13.160 1.00 22.67 C ANISOU 1867 CB LEU A 245 2769 2604 3239 -142 155 316 C ATOM 1868 CG LEU A 245 56.357 45.353 13.061 1.00 22.08 C ANISOU 1868 CG LEU A 245 2835 2592 2963 -110 151 369 C ATOM 1869 CD1 LEU A 245 57.699 44.793 12.632 1.00 24.26 C ANISOU 1869 CD1 LEU A 245 2926 3082 3210 -98 325 316 C ATOM 1870 CD2 LEU A 245 55.911 44.758 14.392 1.00 20.46 C ANISOU 1870 CD2 LEU A 245 2497 2508 2767 -338 133 117 C ATOM 1871 N ALA A 246 55.380 49.870 12.633 1.00 23.13 N ANISOU 1871 N ALA A 246 2947 2531 3310 -154 44 292 N ATOM 1872 CA ALA A 246 55.655 51.296 12.813 1.00 24.42 C ANISOU 1872 CA ALA A 246 3108 2595 3575 -208 35 159 C ATOM 1873 C ALA A 246 54.434 52.120 13.162 1.00 24.58 C ANISOU 1873 C ALA A 246 2886 2902 3552 -286 15 130 C ATOM 1874 O ALA A 246 54.536 53.304 13.503 1.00 26.98 O ANISOU 1874 O ALA A 246 3071 2914 4264 -586 60 209 O ATOM 1875 CB ALA A 246 56.311 51.835 11.543 1.00 27.04 C ANISOU 1875 CB ALA A 246 3331 3056 3886 -331 287 182 C ATOM 1876 N SER A 247 53.248 51.518 13.073 1.00 23.75 N ANISOU 1876 N SER A 247 3034 2551 3438 -428 114 320 N ATOM 1877 CA SER A 247 52.020 52.208 13.418 1.00 23.32 C ANISOU 1877 CA SER A 247 3193 2258 3409 -319 55 504 C ATOM 1878 C SER A 247 51.136 51.320 14.294 1.00 22.52 C ANISOU 1878 C SER A 247 2918 2434 3204 -417 -101 450 C ATOM 1879 O SER A 247 50.224 50.683 13.771 1.00 22.01 O ANISOU 1879 O SER A 247 3197 1600 3565 -128 -509 578 O ATOM 1880 CB SER A 247 51.234 52.615 12.172 1.00 27.62 C ANISOU 1880 CB SER A 247 3686 3243 3564 -309 -305 403 C ATOM 1881 OG SER A 247 51.264 51.548 11.238 1.00 35.03 O ANISOU 1881 OG SER A 247 4659 4033 4619 11 -70 -112 O ATOM 1882 N PRO A 248 51.391 51.337 15.586 1.00 23.01 N ANISOU 1882 N PRO A 248 3094 2452 3197 -486 -99 211 N ATOM 1883 CA PRO A 248 50.636 50.538 16.540 1.00 24.31 C ANISOU 1883 CA PRO A 248 3307 2785 3146 -432 104 207 C ATOM 1884 C PRO A 248 49.137 50.756 16.446 1.00 26.77 C ANISOU 1884 C PRO A 248 3406 3045 3722 -177 67 -73 C ATOM 1885 O PRO A 248 48.342 49.819 16.573 1.00 26.86 O ANISOU 1885 O PRO A 248 3585 2678 3941 -73 368 -382 O ATOM 1886 CB PRO A 248 51.166 50.984 17.899 1.00 26.89 C ANISOU 1886 CB PRO A 248 3594 3307 3317 -313 -83 63 C ATOM 1887 CG PRO A 248 52.529 51.509 17.626 1.00 27.17 C ANISOU 1887 CG PRO A 248 3625 3442 3256 -365 -156 -4 C ATOM 1888 CD PRO A 248 52.500 52.073 16.241 1.00 24.77 C ANISOU 1888 CD PRO A 248 3194 2766 3453 -640 -170 232 C ATOM 1889 N LYS A 249 48.703 51.998 16.233 1.00 28.12 N ANISOU 1889 N LYS A 249 3488 3033 4162 -197 -51 -117 N ATOM 1890 CA LYS A 249 47.280 52.306 16.130 1.00 28.48 C ANISOU 1890 CA LYS A 249 3487 3421 3912 -81 -46 -105 C ATOM 1891 C LYS A 249 46.671 51.666 14.891 1.00 25.25 C ANISOU 1891 C LYS A 249 3142 2694 3757 -30 170 79 C ATOM 1892 O LYS A 249 45.607 51.039 14.967 1.00 27.58 O ANISOU 1892 O LYS A 249 3382 2566 4530 -238 94 -39 O ATOM 1893 CB LYS A 249 47.059 53.818 16.112 1.00 33.23 C ANISOU 1893 CB LYS A 249 4340 3573 4713 -50 54 -14 C ATOM 1894 CG LYS A 249 47.629 54.521 17.332 1.00 38.53 C ANISOU 1894 CG LYS A 249 4966 4860 4815 -106 -161 -175 C ATOM 1895 CD LYS A 249 47.299 56.007 17.299 1.00 42.66 C ANISOU 1895 CD LYS A 249 5556 5064 5588 -6 -2 55 C ATOM 1896 CE LYS A 249 48.226 56.800 18.207 1.00 45.33 C ANISOU 1896 CE LYS A 249 5788 5635 5801 -80 -143 -59 C ATOM 1897 NZ LYS A 249 48.046 58.270 18.034 1.00 46.42 N ANISOU 1897 NZ LYS A 249 5805 5698 6136 -63 -54 -1 N ATOM 1898 N GLN A 250 47.310 51.826 13.738 1.00 20.39 N ANISOU 1898 N GLN A 250 2492 1590 3666 -269 -105 357 N ATOM 1899 CA GLN A 250 46.821 51.218 12.511 1.00 22.73 C ANISOU 1899 CA GLN A 250 2930 2133 3574 -131 -232 329 C ATOM 1900 C GLN A 250 46.832 49.691 12.654 1.00 21.08 C ANISOU 1900 C GLN A 250 2492 2116 3401 -306 -255 409 C ATOM 1901 O GLN A 250 45.943 49.026 12.116 1.00 21.65 O ANISOU 1901 O GLN A 250 2305 2133 3788 -193 -455 477 O ATOM 1902 CB GLN A 250 47.595 51.641 11.276 1.00 25.06 C ANISOU 1902 CB GLN A 250 2988 2702 3831 -39 18 381 C ATOM 1903 CG GLN A 250 47.158 50.979 9.982 1.00 31.08 C ANISOU 1903 CG GLN A 250 4009 3609 4193 -6 -142 -62 C ATOM 1904 CD GLN A 250 47.776 51.671 8.781 1.00 37.29 C ANISOU 1904 CD GLN A 250 4852 4713 4605 -78 193 233 C ATOM 1905 OE1 GLN A 250 48.081 52.865 8.866 1.00 40.33 O ANISOU 1905 OE1 GLN A 250 5251 4815 5258 7 130 145 O ATOM 1906 NE2 GLN A 250 47.964 50.948 7.684 1.00 39.47 N ANISOU 1906 NE2 GLN A 250 5221 4826 4949 30 71 16 N ATOM 1907 N MET A 251 47.831 49.157 13.345 1.00 20.12 N ANISOU 1907 N MET A 251 2378 1724 3542 -482 -191 550 N ATOM 1908 CA MET A 251 47.873 47.710 13.581 1.00 18.91 C ANISOU 1908 CA MET A 251 2243 1780 3163 -171 -217 573 C ATOM 1909 C MET A 251 46.583 47.265 14.267 1.00 18.45 C ANISOU 1909 C MET A 251 2371 1893 2745 -174 -103 355 C ATOM 1910 O MET A 251 45.936 46.310 13.821 1.00 18.77 O ANISOU 1910 O MET A 251 2535 1624 2972 -114 -594 746 O ATOM 1911 CB MET A 251 49.061 47.374 14.489 1.00 19.00 C ANISOU 1911 CB MET A 251 2404 1937 2880 -200 -288 423 C ATOM 1912 CG MET A 251 49.245 45.876 14.664 1.00 19.02 C ANISOU 1912 CG MET A 251 2423 1993 2810 -119 -436 426 C ATOM 1913 SD MET A 251 50.448 45.453 15.929 1.00 18.55 S ANISOU 1913 SD MET A 251 2870 1587 2593 -484 -598 641 S ATOM 1914 CE MET A 251 51.904 46.314 15.338 1.00 19.28 C ANISOU 1914 CE MET A 251 2524 1920 2881 -270 -305 274 C ATOM 1915 N LEU A 252 46.221 47.926 15.363 1.00 19.47 N ANISOU 1915 N LEU A 252 2440 2014 2944 -150 -113 197 N ATOM 1916 CA LEU A 252 45.002 47.543 16.077 1.00 18.96 C ANISOU 1916 CA LEU A 252 2613 1994 2598 -251 -106 274 C ATOM 1917 C LEU A 252 43.765 47.723 15.204 1.00 21.01 C ANISOU 1917 C LEU A 252 2503 2284 3195 -274 -204 298 C ATOM 1918 O LEU A 252 42.887 46.851 15.203 1.00 20.22 O ANISOU 1918 O LEU A 252 2497 1936 3250 -133 -355 331 O ATOM 1919 CB LEU A 252 44.856 48.247 17.414 1.00 20.63 C ANISOU 1919 CB LEU A 252 2717 2211 2911 -131 -115 -49 C ATOM 1920 CG LEU A 252 45.987 48.068 18.429 1.00 21.27 C ANISOU 1920 CG LEU A 252 2699 2248 3133 71 -150 83 C ATOM 1921 CD1 LEU A 252 45.705 48.837 19.709 1.00 21.73 C ANISOU 1921 CD1 LEU A 252 2816 2391 3049 37 -407 16 C ATOM 1922 CD2 LEU A 252 46.206 46.589 18.735 1.00 20.81 C ANISOU 1922 CD2 LEU A 252 2758 2120 3030 -164 -249 -67 C ATOM 1923 N ALA A 253 43.701 48.798 14.415 1.00 21.53 N ANISOU 1923 N ALA A 253 2828 2017 3336 -8 -451 149 N ATOM 1924 CA ALA A 253 42.531 49.000 13.567 1.00 21.40 C ANISOU 1924 CA ALA A 253 2830 2252 3048 -95 -354 150 C ATOM 1925 C ALA A 253 42.409 47.876 12.544 1.00 18.22 C ANISOU 1925 C ALA A 253 2464 1623 2834 -80 -252 540 C ATOM 1926 O ALA A 253 41.310 47.377 12.282 1.00 21.47 O ANISOU 1926 O ALA A 253 2413 2366 3379 -128 -439 636 O ATOM 1927 CB ALA A 253 42.609 50.361 12.890 1.00 22.97 C ANISOU 1927 CB ALA A 253 2932 2364 3433 30 -413 316 C ATOM 1928 N GLU A 254 43.511 47.517 11.900 1.00 18.34 N ANISOU 1928 N GLU A 254 2695 1693 2579 121 -243 634 N ATOM 1929 CA GLU A 254 43.498 46.470 10.890 1.00 17.59 C ANISOU 1929 CA GLU A 254 2554 1848 2282 -46 -21 634 C ATOM 1930 C GLU A 254 43.224 45.094 11.513 1.00 17.74 C ANISOU 1930 C GLU A 254 2634 1737 2370 -258 -233 488 C ATOM 1931 O GLU A 254 42.498 44.286 10.927 1.00 17.77 O ANISOU 1931 O GLU A 254 3161 1141 2449 -77 -307 391 O ATOM 1932 CB AGLU A 254 44.755 46.469 10.036 0.50 18.31 C ANISOU 1932 CB AGLU A 254 2311 2091 2554 12 -147 535 C ATOM 1933 CG AGLU A 254 44.995 47.784 9.306 0.50 17.44 C ANISOU 1933 CG AGLU A 254 2107 2069 2449 -79 -264 497 C ATOM 1934 CD AGLU A 254 46.055 47.698 8.237 0.50 20.77 C ANISOU 1934 CD AGLU A 254 2580 2542 2770 -88 -47 398 C ATOM 1935 OE1AGLU A 254 46.765 46.680 8.108 0.50 20.65 O ANISOU 1935 OE1AGLU A 254 2728 2260 2857 -161 -8 626 O ATOM 1936 OE2AGLU A 254 46.188 48.690 7.484 0.50 21.77 O ANISOU 1936 OE2AGLU A 254 2629 2791 2850 -337 -172 624 O ATOM 1937 CB BGLU A 254 44.805 46.457 10.108 0.50 20.21 C ANISOU 1937 CB BGLU A 254 2618 2404 2656 -13 64 432 C ATOM 1938 CG BGLU A 254 44.847 45.513 8.926 0.50 24.24 C ANISOU 1938 CG BGLU A 254 3382 2955 2873 4 -145 127 C ATOM 1939 CD BGLU A 254 46.067 45.656 8.043 0.50 27.17 C ANISOU 1939 CD BGLU A 254 3624 3417 3282 -7 11 133 C ATOM 1940 OE1BGLU A 254 46.900 46.561 8.265 0.50 28.31 O ANISOU 1940 OE1BGLU A 254 3784 3469 3506 -146 -41 288 O ATOM 1941 OE2BGLU A 254 46.214 44.847 7.097 0.50 28.20 O ANISOU 1941 OE2BGLU A 254 4036 3517 3160 31 -50 157 O ATOM 1942 N LEU A 255 43.725 44.856 12.711 1.00 15.81 N ANISOU 1942 N LEU A 255 2394 1303 2311 -507 -276 242 N ATOM 1943 CA LEU A 255 43.419 43.578 13.380 1.00 15.10 C ANISOU 1943 CA LEU A 255 2160 1369 2208 -325 -354 337 C ATOM 1944 C LEU A 255 41.921 43.521 13.628 1.00 16.57 C ANISOU 1944 C LEU A 255 2249 1551 2495 -297 -83 349 C ATOM 1945 O LEU A 255 41.270 42.484 13.404 1.00 16.98 O ANISOU 1945 O LEU A 255 1880 1701 2869 -316 -689 590 O ATOM 1946 CB LEU A 255 44.207 43.445 14.676 1.00 16.72 C ANISOU 1946 CB LEU A 255 2122 1882 2350 25 -426 328 C ATOM 1947 CG LEU A 255 45.692 43.084 14.540 1.00 17.95 C ANISOU 1947 CG LEU A 255 2154 2178 2488 -39 -199 54 C ATOM 1948 CD1 LEU A 255 46.401 43.310 15.868 1.00 18.98 C ANISOU 1948 CD1 LEU A 255 2225 2448 2540 -259 -252 63 C ATOM 1949 CD2 LEU A 255 45.850 41.640 14.067 1.00 16.74 C ANISOU 1949 CD2 LEU A 255 2010 2003 2348 -231 -465 196 C ATOM 1950 N ARG A 256 41.363 44.616 14.135 1.00 17.43 N ANISOU 1950 N ARG A 256 2030 1657 2936 62 -182 591 N ATOM 1951 CA ARG A 256 39.937 44.668 14.418 1.00 18.34 C ANISOU 1951 CA ARG A 256 2117 1975 2875 36 22 273 C ATOM 1952 C ARG A 256 39.112 44.382 13.174 1.00 20.54 C ANISOU 1952 C ARG A 256 2734 2333 2735 -1 -112 438 C ATOM 1953 O ARG A 256 38.176 43.578 13.231 1.00 21.24 O ANISOU 1953 O ARG A 256 2162 2478 3432 268 -393 697 O ATOM 1954 CB ARG A 256 39.530 46.014 15.028 1.00 19.18 C ANISOU 1954 CB ARG A 256 2319 1912 3056 145 -181 267 C ATOM 1955 CG ARG A 256 38.029 46.128 15.284 1.00 20.95 C ANISOU 1955 CG ARG A 256 2433 2293 3234 189 39 243 C ATOM 1956 CD ARG A 256 37.719 47.494 15.896 1.00 24.78 C ANISOU 1956 CD ARG A 256 3322 2623 3470 482 -38 -11 C ATOM 1957 NE ARG A 256 38.315 47.627 17.219 1.00 26.47 N ANISOU 1957 NE ARG A 256 3596 2928 3534 329 -44 17 N ATOM 1958 CZ ARG A 256 37.806 47.094 18.327 1.00 25.72 C ANISOU 1958 CZ ARG A 256 3372 2623 3777 289 81 49 C ATOM 1959 NH1 ARG A 256 36.676 46.389 18.280 1.00 24.68 N ANISOU 1959 NH1 ARG A 256 3514 1725 4137 433 153 32 N ATOM 1960 NH2 ARG A 256 38.446 47.282 19.471 1.00 27.48 N ANISOU 1960 NH2 ARG A 256 3896 2641 3904 452 -39 -136 N ATOM 1961 N SER A 257 39.452 45.035 12.053 1.00 18.99 N ANISOU 1961 N SER A 257 2551 2174 2490 14 -499 420 N ATOM 1962 CA SER A 257 38.692 44.832 10.827 1.00 20.10 C ANISOU 1962 CA SER A 257 2723 2422 2490 -136 -438 -1 C ATOM 1963 C SER A 257 38.744 43.387 10.347 1.00 18.21 C ANISOU 1963 C SER A 257 2167 2166 2584 -34 -386 337 C ATOM 1964 O SER A 257 37.746 42.798 9.931 1.00 18.76 O ANISOU 1964 O SER A 257 2499 2193 2435 -59 -787 305 O ATOM 1965 CB SER A 257 39.213 45.747 9.708 1.00 24.60 C ANISOU 1965 CB SER A 257 3429 2685 3233 -189 -141 372 C ATOM 1966 OG SER A 257 38.957 47.106 10.019 1.00 29.51 O ANISOU 1966 OG SER A 257 4004 2985 4223 51 -161 69 O ATOM 1967 N PHE A 258 39.926 42.786 10.401 1.00 17.61 N ANISOU 1967 N PHE A 258 2185 1981 2525 -31 -697 187 N ATOM 1968 CA PHE A 258 40.113 41.415 9.944 1.00 17.29 C ANISOU 1968 CA PHE A 258 2101 2053 2417 -150 -376 114 C ATOM 1969 C PHE A 258 39.382 40.422 10.828 1.00 17.48 C ANISOU 1969 C PHE A 258 2305 2078 2258 -119 -468 213 C ATOM 1970 O PHE A 258 38.637 39.577 10.315 1.00 17.22 O ANISOU 1970 O PHE A 258 1845 2002 2697 -21 -786 524 O ATOM 1971 CB PHE A 258 41.613 41.094 9.876 1.00 18.75 C ANISOU 1971 CB PHE A 258 2238 2259 2628 136 -392 127 C ATOM 1972 CG PHE A 258 41.849 39.699 9.376 1.00 18.98 C ANISOU 1972 CG PHE A 258 2331 2199 2683 18 -284 120 C ATOM 1973 CD1 PHE A 258 41.705 39.406 8.037 1.00 22.38 C ANISOU 1973 CD1 PHE A 258 3265 2526 2714 45 -136 104 C ATOM 1974 CD2 PHE A 258 42.189 38.678 10.253 1.00 19.77 C ANISOU 1974 CD2 PHE A 258 2555 2198 2759 135 -368 67 C ATOM 1975 CE1 PHE A 258 41.911 38.129 7.555 1.00 22.73 C ANISOU 1975 CE1 PHE A 258 3227 2572 2837 92 -100 42 C ATOM 1976 CE2 PHE A 258 42.395 37.393 9.781 1.00 19.42 C ANISOU 1976 CE2 PHE A 258 2433 2316 2631 237 -244 -39 C ATOM 1977 CZ PHE A 258 42.260 37.122 8.435 1.00 20.92 C ANISOU 1977 CZ PHE A 258 2963 2368 2616 77 30 -71 C ATOM 1978 N VAL A 259 39.520 40.528 12.145 1.00 15.93 N ANISOU 1978 N VAL A 259 1838 1910 2306 -290 -571 110 N ATOM 1979 CA VAL A 259 38.843 39.617 13.059 1.00 16.40 C ANISOU 1979 CA VAL A 259 1966 2147 2118 -124 -250 40 C ATOM 1980 C VAL A 259 37.332 39.777 12.939 1.00 18.46 C ANISOU 1980 C VAL A 259 2004 2173 2838 -79 -396 -9 C ATOM 1981 O VAL A 259 36.605 38.775 12.883 1.00 19.05 O ANISOU 1981 O VAL A 259 1931 2157 3150 -54 -726 418 O ATOM 1982 CB VAL A 259 39.287 39.823 14.518 1.00 16.41 C ANISOU 1982 CB VAL A 259 1820 2054 2360 -267 -551 -108 C ATOM 1983 CG1 VAL A 259 38.421 39.022 15.469 1.00 16.72 C ANISOU 1983 CG1 VAL A 259 1968 1985 2402 248 -217 66 C ATOM 1984 CG2 VAL A 259 40.751 39.438 14.692 1.00 18.35 C ANISOU 1984 CG2 VAL A 259 2007 2183 2784 61 -563 -34 C ATOM 1985 N SER A 260 36.856 41.024 12.819 1.00 18.93 N ANISOU 1985 N SER A 260 1609 2409 3174 99 -313 275 N ATOM 1986 CA SER A 260 35.412 41.226 12.656 1.00 18.75 C ANISOU 1986 CA SER A 260 1580 2368 3177 -68 -363 -91 C ATOM 1987 C SER A 260 34.909 40.513 11.412 1.00 16.40 C ANISOU 1987 C SER A 260 1401 2135 2694 417 -437 235 C ATOM 1988 O SER A 260 33.860 39.838 11.449 1.00 17.82 O ANISOU 1988 O SER A 260 1755 2029 2986 157 -586 514 O ATOM 1989 CB SER A 260 35.112 42.731 12.562 1.00 23.17 C ANISOU 1989 CB SER A 260 2608 2555 3640 340 -276 189 C ATOM 1990 OG SER A 260 33.710 42.899 12.417 1.00 28.61 O ANISOU 1990 OG SER A 260 2769 3639 4462 346 -416 -49 O ATOM 1991 N ALA A 261 35.617 40.641 10.296 1.00 16.91 N ANISOU 1991 N ALA A 261 1746 2338 2340 98 -733 393 N ATOM 1992 CA ALA A 261 35.191 39.989 9.054 1.00 17.27 C ANISOU 1992 CA ALA A 261 1981 2218 2361 25 -451 164 C ATOM 1993 C ALA A 261 35.230 38.471 9.161 1.00 18.79 C ANISOU 1993 C ALA A 261 2236 2265 2638 96 -864 438 C ATOM 1994 O ALA A 261 34.341 37.769 8.655 1.00 18.78 O ANISOU 1994 O ALA A 261 2560 2038 2536 211 -909 115 O ATOM 1995 CB ALA A 261 36.015 40.430 7.853 1.00 18.60 C ANISOU 1995 CB ALA A 261 2486 2555 2027 -137 -617 309 C ATOM 1996 N MET A 262 36.264 37.940 9.833 1.00 16.79 N ANISOU 1996 N MET A 262 1757 1974 2650 172 -554 192 N ATOM 1997 CA MET A 262 36.371 36.490 9.976 1.00 16.03 C ANISOU 1997 CA MET A 262 1698 1945 2446 124 -507 116 C ATOM 1998 C MET A 262 35.299 35.949 10.905 1.00 14.97 C ANISOU 1998 C MET A 262 1586 1847 2255 166 -624 105 C ATOM 1999 O MET A 262 34.696 34.895 10.631 1.00 16.94 O ANISOU 1999 O MET A 262 1647 1968 2822 171 -1033 -6 O ATOM 2000 CB MET A 262 37.777 36.131 10.480 1.00 15.19 C ANISOU 2000 CB MET A 262 1665 2001 2107 -69 -554 150 C ATOM 2001 CG MET A 262 38.855 36.507 9.485 1.00 16.03 C ANISOU 2001 CG MET A 262 1607 2371 2115 -90 -610 223 C ATOM 2002 SD MET A 262 38.933 35.521 7.990 1.00 16.59 S ANISOU 2002 SD MET A 262 2257 2014 2033 -108 -1048 399 S ATOM 2003 CE MET A 262 39.804 34.065 8.577 1.00 17.64 C ANISOU 2003 CE MET A 262 2523 2005 2174 39 -766 423 C ATOM 2004 N LYS A 263 35.031 36.653 12.000 1.00 16.04 N ANISOU 2004 N LYS A 263 1881 1678 2534 454 -337 145 N ATOM 2005 CA LYS A 263 33.989 36.222 12.931 1.00 16.33 C ANISOU 2005 CA LYS A 263 2114 1792 2298 263 -374 134 C ATOM 2006 C LYS A 263 32.625 36.301 12.252 1.00 17.50 C ANISOU 2006 C LYS A 263 2030 1956 2662 107 -426 249 C ATOM 2007 O LYS A 263 31.810 35.385 12.417 1.00 18.68 O ANISOU 2007 O LYS A 263 1980 2003 3116 58 -895 356 O ATOM 2008 CB LYS A 263 34.021 36.996 14.253 1.00 17.24 C ANISOU 2008 CB LYS A 263 2165 1995 2392 44 -102 -24 C ATOM 2009 CG LYS A 263 32.847 36.706 15.184 1.00 14.67 C ANISOU 2009 CG LYS A 263 2036 1421 2115 14 -237 -223 C ATOM 2010 CD LYS A 263 32.832 35.231 15.590 1.00 16.20 C ANISOU 2010 CD LYS A 263 1975 1663 2517 73 -408 217 C ATOM 2011 CE LYS A 263 31.476 34.773 16.091 1.00 17.40 C ANISOU 2011 CE LYS A 263 2169 2073 2369 -48 -236 226 C ATOM 2012 NZ LYS A 263 31.432 33.287 16.280 1.00 16.80 N ANISOU 2012 NZ LYS A 263 1197 2048 3139 56 -136 139 N ATOM 2013 N ALA A 264 32.375 37.338 11.458 1.00 18.18 N ANISOU 2013 N ALA A 264 2024 1885 3001 -15 -458 318 N ATOM 2014 CA ALA A 264 31.070 37.448 10.805 1.00 18.05 C ANISOU 2014 CA ALA A 264 2070 2053 2735 -122 -484 150 C ATOM 2015 C ALA A 264 30.802 36.236 9.917 1.00 18.48 C ANISOU 2015 C ALA A 264 2041 2111 2870 -50 -293 -2 C ATOM 2016 O ALA A 264 29.657 35.776 9.788 1.00 21.45 O ANISOU 2016 O ALA A 264 1861 2945 3344 151 -1037 262 O ATOM 2017 CB ALA A 264 31.026 38.707 9.939 1.00 19.13 C ANISOU 2017 CB ALA A 264 1985 2210 3072 29 -455 376 C ATOM 2018 N ALA A 265 31.843 35.720 9.266 1.00 17.93 N ANISOU 2018 N ALA A 265 2233 2312 2266 239 -471 152 N ATOM 2019 CA ALA A 265 31.674 34.583 8.376 1.00 18.55 C ANISOU 2019 CA ALA A 265 2578 2253 2215 -27 -519 219 C ATOM 2020 C ALA A 265 31.324 33.289 9.100 1.00 19.40 C ANISOU 2020 C ALA A 265 2795 2282 2295 47 -642 319 C ATOM 2021 O ALA A 265 30.970 32.285 8.464 1.00 21.63 O ANISOU 2021 O ALA A 265 3209 2697 2312 -16 -1049 118 O ATOM 2022 CB ALA A 265 32.928 34.343 7.549 1.00 18.80 C ANISOU 2022 CB ALA A 265 2611 2340 2194 221 -527 483 C ATOM 2023 N SER A 266 31.446 33.267 10.421 1.00 20.17 N ANISOU 2023 N SER A 266 2940 2437 2285 -155 -531 35 N ATOM 2024 CA SER A 266 31.131 32.062 11.172 1.00 18.43 C ANISOU 2024 CA SER A 266 2198 2487 2319 71 -716 218 C ATOM 2025 C SER A 266 29.653 31.968 11.523 1.00 22.59 C ANISOU 2025 C SER A 266 2341 3187 3053 -202 -526 245 C ATOM 2026 O SER A 266 29.230 30.992 12.143 1.00 22.10 O ANISOU 2026 O SER A 266 2040 2973 3385 45 -1146 572 O ATOM 2027 CB SER A 266 31.980 32.001 12.441 1.00 17.63 C ANISOU 2027 CB SER A 266 2485 2121 2093 164 -697 -69 C ATOM 2028 OG SER A 266 31.540 32.923 13.427 1.00 19.38 O ANISOU 2028 OG SER A 266 2361 2666 2338 494 -739 -298 O ATOM 2029 N ARG A 267 28.898 32.996 11.146 1.00 26.16 N ANISOU 2029 N ARG A 267 2940 3335 3664 201 -361 292 N ATOM 2030 CA ARG A 267 27.464 33.031 11.437 1.00 29.44 C ANISOU 2030 CA ARG A 267 3194 3998 3992 4 -16 67 C ATOM 2031 C ARG A 267 26.644 32.438 10.299 1.00 31.02 C ANISOU 2031 C ARG A 267 3530 4314 3941 176 -305 84 C ATOM 2032 O ARG A 267 27.244 32.217 9.215 1.00 34.50 O ANISOU 2032 O ARG A 267 4113 4877 4121 76 -136 153 O ATOM 2033 CB ARG A 267 27.060 34.488 11.709 1.00 31.27 C ANISOU 2033 CB ARG A 267 3527 4059 4294 147 81 75 C ATOM 2034 CG ARG A 267 27.921 35.135 12.784 1.00 33.35 C ANISOU 2034 CG ARG A 267 4066 4231 4375 -3 -32 4 C ATOM 2035 CD ARG A 267 27.368 36.458 13.285 1.00 35.50 C ANISOU 2035 CD ARG A 267 4334 4478 4677 69 98 -148 C ATOM 2036 NE ARG A 267 28.065 36.910 14.486 1.00 36.09 N ANISOU 2036 NE ARG A 267 4403 4583 4728 47 -38 -11 N ATOM 2037 CZ ARG A 267 29.022 37.820 14.576 1.00 34.73 C ANISOU 2037 CZ ARG A 267 4271 4373 4553 184 14 -5 C ATOM 2038 NH1 ARG A 267 29.452 38.465 13.498 1.00 34.01 N ANISOU 2038 NH1 ARG A 267 4077 4194 4653 305 14 79 N ATOM 2039 NH2 ARG A 267 29.557 38.107 15.759 1.00 35.51 N ANISOU 2039 NH2 ARG A 267 4539 4375 4577 410 -39 -73 N TER 2040 ARG A 267 ANISOU 2057 O4P IPL A 300 2339 2007 977 5 -140 187 O ATOM 2058 N THR B 2 52.927 2.855 16.992 1.00 30.88 N ANISOU 2058 N THR B 2 3491 3966 4278 280 125 38 N ATOM 2059 CA THR B 2 53.323 1.417 16.835 1.00 28.76 C ANISOU 2059 CA THR B 2 3247 3945 3734 220 277 -143 C ATOM 2060 C THR B 2 54.573 1.295 15.986 1.00 24.68 C ANISOU 2060 C THR B 2 2845 3385 3146 318 -117 9 C ATOM 2061 O THR B 2 54.623 1.962 14.949 1.00 25.94 O ANISOU 2061 O THR B 2 2818 3735 3303 310 -129 204 O ATOM 2062 CB THR B 2 52.151 0.637 16.228 1.00 31.09 C ANISOU 2062 CB THR B 2 3545 4125 4143 -9 125 -76 C ATOM 2063 OG1 THR B 2 51.191 0.422 17.277 1.00 34.21 O ANISOU 2063 OG1 THR B 2 3753 4935 4311 11 313 -125 O ATOM 2064 CG2 THR B 2 52.537 -0.697 15.629 1.00 32.04 C ANISOU 2064 CG2 THR B 2 3480 4227 4467 119 194 -106 C ATOM 2065 N THR B 3 55.570 0.523 16.415 1.00 18.10 N ANISOU 2065 N THR B 3 1895 2913 2068 -280 -29 -471 N ATOM 2066 CA THR B 3 56.769 0.387 15.582 1.00 15.11 C ANISOU 2066 CA THR B 3 1524 2296 1922 -115 -360 -474 C ATOM 2067 C THR B 3 57.255 -1.050 15.564 1.00 13.34 C ANISOU 2067 C THR B 3 1575 2110 1384 -343 -6 -609 C ATOM 2068 O THR B 3 56.940 -1.875 16.424 1.00 17.05 O ANISOU 2068 O THR B 3 2483 2251 1746 -528 274 -506 O ATOM 2069 CB THR B 3 57.921 1.298 16.060 1.00 14.79 C ANISOU 2069 CB THR B 3 1661 1954 2004 -89 -314 -418 C ATOM 2070 OG1 THR B 3 58.263 0.907 17.386 1.00 16.10 O ANISOU 2070 OG1 THR B 3 2030 2379 1706 -177 -327 -740 O ATOM 2071 CG2 THR B 3 57.503 2.759 15.999 1.00 15.28 C ANISOU 2071 CG2 THR B 3 1863 1899 2043 -129 -529 -528 C ATOM 2072 N LEU B 4 58.099 -1.363 14.562 1.00 12.98 N ANISOU 2072 N LEU B 4 1363 2123 1447 -266 -67 -695 N ATOM 2073 CA LEU B 4 58.676 -2.697 14.465 1.00 14.32 C ANISOU 2073 CA LEU B 4 1643 2116 1681 -189 -110 -425 C ATOM 2074 C LEU B 4 59.874 -2.874 15.394 1.00 13.27 C ANISOU 2074 C LEU B 4 2032 1574 1437 -181 -270 -496 C ATOM 2075 O LEU B 4 60.182 -3.973 15.838 1.00 16.78 O ANISOU 2075 O LEU B 4 2502 1611 2262 -385 -486 -190 O ATOM 2076 CB LEU B 4 59.188 -2.903 13.027 1.00 14.35 C ANISOU 2076 CB LEU B 4 1739 2185 1529 -577 -209 -491 C ATOM 2077 CG LEU B 4 58.079 -2.932 11.964 1.00 15.83 C ANISOU 2077 CG LEU B 4 2131 2614 1271 -602 -286 -251 C ATOM 2078 CD1 LEU B 4 58.705 -2.926 10.578 1.00 17.29 C ANISOU 2078 CD1 LEU B 4 2163 2897 1510 -558 -44 -573 C ATOM 2079 CD2 LEU B 4 57.171 -4.146 12.165 1.00 18.21 C ANISOU 2079 CD2 LEU B 4 2479 2650 1790 -679 19 -352 C ATOM 2080 N LEU B 5 60.571 -1.761 15.601 1.00 12.97 N ANISOU 2080 N LEU B 5 1390 1790 1747 -259 -218 -361 N ATOM 2081 CA LEU B 5 61.781 -1.723 16.402 1.00 12.58 C ANISOU 2081 CA LEU B 5 1590 1651 1540 -8 -292 -607 C ATOM 2082 C LEU B 5 61.612 -0.757 17.575 1.00 12.62 C ANISOU 2082 C LEU B 5 1985 1371 1440 -9 -455 -457 C ATOM 2083 O LEU B 5 60.846 0.204 17.510 1.00 13.53 O ANISOU 2083 O LEU B 5 2159 1379 1602 -4 -989 -336 O ATOM 2084 CB LEU B 5 62.973 -1.224 15.564 1.00 13.51 C ANISOU 2084 CB LEU B 5 1709 1812 1611 -81 -186 -734 C ATOM 2085 CG LEU B 5 63.264 -1.997 14.270 1.00 13.70 C ANISOU 2085 CG LEU B 5 1762 1892 1553 104 -27 -588 C ATOM 2086 CD1 LEU B 5 64.378 -1.313 13.490 1.00 15.06 C ANISOU 2086 CD1 LEU B 5 2418 2225 1081 -171 -12 -346 C ATOM 2087 CD2 LEU B 5 63.608 -3.447 14.557 1.00 15.78 C ANISOU 2087 CD2 LEU B 5 2275 1783 1937 -56 56 -546 C ATOM 2088 N ASN B 6 62.438 -0.964 18.612 1.00 12.59 N ANISOU 2088 N ASN B 6 1635 1538 1610 -309 -424 -250 N ATOM 2089 CA ASN B 6 62.332 -0.054 19.760 1.00 11.90 C ANISOU 2089 CA ASN B 6 1787 1529 1207 -161 -380 15 C ATOM 2090 C ASN B 6 62.837 1.343 19.448 1.00 11.33 C ANISOU 2090 C ASN B 6 1563 1479 1265 -51 -355 -20 C ATOM 2091 O ASN B 6 64.007 1.453 19.072 1.00 12.37 O ANISOU 2091 O ASN B 6 1464 2005 1230 -213 -506 -458 O ATOM 2092 CB ASN B 6 63.158 -0.699 20.893 1.00 12.61 C ANISOU 2092 CB ASN B 6 1681 1642 1469 -71 -334 200 C ATOM 2093 CG ASN B 6 62.916 -0.016 22.221 1.00 14.13 C ANISOU 2093 CG ASN B 6 2003 1914 1453 -154 -599 29 C ATOM 2094 OD1 ASN B 6 62.310 1.046 22.294 1.00 12.78 O ANISOU 2094 OD1 ASN B 6 2105 1384 1366 -598 -756 131 O ATOM 2095 ND2 ASN B 6 63.409 -0.655 23.285 1.00 18.05 N ANISOU 2095 ND2 ASN B 6 2839 2348 1671 -194 -669 400 N ATOM 2096 N PRO B 7 62.032 2.383 19.597 1.00 10.60 N ANISOU 2096 N PRO B 7 1414 1657 957 2 -236 41 N ATOM 2097 CA PRO B 7 62.466 3.748 19.315 1.00 10.34 C ANISOU 2097 CA PRO B 7 1396 1674 859 -118 -488 -50 C ATOM 2098 C PRO B 7 63.340 4.356 20.413 1.00 8.64 C ANISOU 2098 C PRO B 7 1326 1378 580 -247 -78 -148 C ATOM 2099 O PRO B 7 63.861 5.453 20.225 1.00 9.64 O ANISOU 2099 O PRO B 7 1402 1529 733 -331 -141 -124 O ATOM 2100 CB PRO B 7 61.183 4.562 19.199 1.00 11.78 C ANISOU 2100 CB PRO B 7 1602 1714 1162 20 -413 -243 C ATOM 2101 CG PRO B 7 60.081 3.565 19.196 1.00 14.69 C ANISOU 2101 CG PRO B 7 1764 1614 2206 2 -181 51 C ATOM 2102 CD PRO B 7 60.593 2.348 19.929 1.00 11.42 C ANISOU 2102 CD PRO B 7 1419 1905 1013 -47 -225 18 C ATOM 2103 N TYR B 8 63.468 3.653 21.544 1.00 10.14 N ANISOU 2103 N TYR B 8 1125 2137 590 -258 -377 10 N ATOM 2104 CA TYR B 8 64.208 4.196 22.669 1.00 9.62 C ANISOU 2104 CA TYR B 8 1355 1803 498 -138 -238 -117 C ATOM 2105 C TYR B 8 65.422 3.364 23.044 1.00 10.00 C ANISOU 2105 C TYR B 8 1532 1382 887 -199 -446 -80 C ATOM 2106 O TYR B 8 65.467 2.165 22.829 1.00 13.04 O ANISOU 2106 O TYR B 8 1698 1484 1774 171 -638 -309 O ATOM 2107 CB TYR B 8 63.269 4.187 23.915 1.00 7.47 C ANISOU 2107 CB TYR B 8 808 1408 624 -20 -308 185 C ATOM 2108 CG TYR B 8 62.362 5.399 23.921 1.00 9.14 C ANISOU 2108 CG TYR B 8 971 1393 1111 56 -52 -188 C ATOM 2109 CD1 TYR B 8 62.782 6.607 24.471 1.00 10.19 C ANISOU 2109 CD1 TYR B 8 1584 1509 780 -28 -83 -271 C ATOM 2110 CD2 TYR B 8 61.084 5.374 23.365 1.00 10.68 C ANISOU 2110 CD2 TYR B 8 1166 1801 1090 -149 -276 37 C ATOM 2111 CE1 TYR B 8 61.993 7.735 24.484 1.00 9.66 C ANISOU 2111 CE1 TYR B 8 1422 1865 383 147 48 -216 C ATOM 2112 CE2 TYR B 8 60.290 6.499 23.375 1.00 10.96 C ANISOU 2112 CE2 TYR B 8 1334 1768 1063 -123 -81 49 C ATOM 2113 CZ TYR B 8 60.715 7.675 23.946 1.00 10.40 C ANISOU 2113 CZ TYR B 8 1370 1579 1004 89 58 84 C ATOM 2114 OH TYR B 8 59.961 8.809 23.965 1.00 11.80 O ANISOU 2114 OH TYR B 8 1644 1724 1116 272 -64 -54 O ATOM 2115 N PHE B 9 66.389 4.051 23.641 1.00 8.93 N ANISOU 2115 N PHE B 9 1231 1397 764 -85 -376 -46 N ATOM 2116 CA PHE B 9 67.598 3.482 24.231 1.00 8.51 C ANISOU 2116 CA PHE B 9 1177 1391 667 -75 -196 170 C ATOM 2117 C PHE B 9 67.485 3.942 25.689 1.00 9.02 C ANISOU 2117 C PHE B 9 1452 1139 836 55 107 35 C ATOM 2118 O PHE B 9 67.786 5.084 26.045 1.00 9.67 O ANISOU 2118 O PHE B 9 1699 1342 632 76 -550 -103 O ATOM 2119 CB PHE B 9 68.843 4.076 23.578 1.00 9.28 C ANISOU 2119 CB PHE B 9 1127 1724 676 -88 10 -249 C ATOM 2120 CG PHE B 9 68.876 3.790 22.102 1.00 8.87 C ANISOU 2120 CG PHE B 9 1496 1210 663 -97 -262 -160 C ATOM 2121 CD1 PHE B 9 69.491 2.623 21.680 1.00 9.84 C ANISOU 2121 CD1 PHE B 9 1485 1413 842 -52 -213 -377 C ATOM 2122 CD2 PHE B 9 68.347 4.658 21.169 1.00 9.12 C ANISOU 2122 CD2 PHE B 9 1498 1440 526 -164 -345 -159 C ATOM 2123 CE1 PHE B 9 69.576 2.308 20.327 1.00 10.56 C ANISOU 2123 CE1 PHE B 9 1637 1549 826 43 -51 -273 C ATOM 2124 CE2 PHE B 9 68.423 4.344 19.802 1.00 9.43 C ANISOU 2124 CE2 PHE B 9 1601 1455 527 70 -328 -224 C ATOM 2125 CZ PHE B 9 69.028 3.169 19.412 1.00 10.45 C ANISOU 2125 CZ PHE B 9 1704 1429 837 -33 -187 -327 C ATOM 2126 N GLY B 10 66.877 3.072 26.503 1.00 10.07 N ANISOU 2126 N GLY B 10 1617 1575 634 -192 -242 309 N ATOM 2127 CA GLY B 10 66.548 3.493 27.877 1.00 11.57 C ANISOU 2127 CA GLY B 10 2146 1436 814 -68 -17 195 C ATOM 2128 C GLY B 10 65.546 4.638 27.785 1.00 8.66 C ANISOU 2128 C GLY B 10 1361 1306 622 -490 -147 131 C ATOM 2129 O GLY B 10 64.551 4.542 27.052 1.00 11.62 O ANISOU 2129 O GLY B 10 1618 2272 527 169 -442 -187 O ATOM 2130 N GLU B 11 65.806 5.738 28.474 1.00 10.09 N ANISOU 2130 N GLU B 11 1800 1389 645 -198 58 -149 N ATOM 2131 C GLU B 11 65.076 7.780 27.231 1.00 8.95 C ANISOU 2131 C GLU B 11 1089 1287 1023 -18 140 -134 C ATOM 2132 O GLU B 11 64.246 8.655 26.991 1.00 12.70 O ANISOU 2132 O GLU B 11 1473 2159 1192 465 35 41 O ATOM 2133 CA AGLU B 11 64.963 6.917 28.483 0.50 11.36 C ANISOU 2133 CA AGLU B 11 1801 1658 858 48 -127 -77 C ATOM 2134 CB AGLU B 11 65.355 7.846 29.664 0.50 14.48 C ANISOU 2134 CB AGLU B 11 2412 2029 1062 228 -194 -366 C ATOM 2135 CG AGLU B 11 64.820 9.263 29.665 0.50 16.62 C ANISOU 2135 CG AGLU B 11 2474 2113 1729 327 -100 -168 C ATOM 2136 CD AGLU B 11 65.305 10.230 30.721 0.50 17.91 C ANISOU 2136 CD AGLU B 11 2397 2437 1970 238 -276 -220 C ATOM 2137 OE1AGLU B 11 66.283 9.913 31.437 0.50 16.77 O ANISOU 2137 OE1AGLU B 11 2095 2379 1898 240 -150 -271 O ATOM 2138 OE2AGLU B 11 64.764 11.363 30.881 0.50 16.02 O ANISOU 2138 OE2AGLU B 11 2695 2493 897 311 -164 -434 O ATOM 2139 CA BGLU B 11 64.945 6.904 28.476 0.50 11.04 C ANISOU 2139 CA BGLU B 11 1777 1583 837 -13 -137 -108 C ATOM 2140 CB BGLU B 11 65.220 7.721 29.754 0.50 13.06 C ANISOU 2140 CB BGLU B 11 2233 1698 1032 156 -145 -305 C ATOM 2141 CG BGLU B 11 66.563 8.403 29.784 0.50 14.94 C ANISOU 2141 CG BGLU B 11 2326 1811 1539 38 -62 -92 C ATOM 2142 CD BGLU B 11 67.164 8.818 31.111 0.50 15.69 C ANISOU 2142 CD BGLU B 11 2540 1838 1584 84 -266 142 C ATOM 2143 OE1BGLU B 11 67.176 10.057 31.361 0.50 14.30 O ANISOU 2143 OE1BGLU B 11 2426 1708 1300 71 211 340 O ATOM 2144 OE2BGLU B 11 67.666 7.958 31.889 0.50 11.52 O ANISOU 2144 OE2BGLU B 11 2248 1787 344 -350 -241 -49 O ATOM 2145 N PHE B 12 66.133 7.520 26.456 1.00 8.94 N ANISOU 2145 N PHE B 12 1355 1488 553 94 154 22 N ATOM 2146 CA PHE B 12 66.490 8.429 25.388 1.00 7.47 C ANISOU 2146 CA PHE B 12 1282 1049 507 -87 -153 -97 C ATOM 2147 C PHE B 12 66.015 8.017 23.994 1.00 8.49 C ANISOU 2147 C PHE B 12 1372 1388 466 65 -276 -116 C ATOM 2148 O PHE B 12 66.051 6.827 23.686 1.00 10.37 O ANISOU 2148 O PHE B 12 1920 1338 683 130 -358 104 O ATOM 2149 CB PHE B 12 68.026 8.568 25.349 1.00 9.24 C ANISOU 2149 CB PHE B 12 1325 1699 488 -225 -188 0 C ATOM 2150 CG PHE B 12 68.611 8.889 26.707 1.00 9.22 C ANISOU 2150 CG PHE B 12 1411 1726 364 -59 72 -113 C ATOM 2151 CD1 PHE B 12 68.502 10.167 27.210 1.00 9.58 C ANISOU 2151 CD1 PHE B 12 1400 1580 659 -370 -91 -76 C ATOM 2152 CD2 PHE B 12 69.229 7.892 27.441 1.00 8.81 C ANISOU 2152 CD2 PHE B 12 1226 1735 386 -320 116 82 C ATOM 2153 CE1 PHE B 12 69.042 10.464 28.471 1.00 9.30 C ANISOU 2153 CE1 PHE B 12 1891 1088 556 -186 45 -155 C ATOM 2154 CE2 PHE B 12 69.763 8.176 28.692 1.00 9.83 C ANISOU 2154 CE2 PHE B 12 1480 1621 635 -199 -68 -316 C ATOM 2155 CZ PHE B 12 69.661 9.459 29.190 1.00 9.29 C ANISOU 2155 CZ PHE B 12 1418 1512 600 -301 -531 -223 C ATOM 2156 N GLY B 13 65.633 9.001 23.181 1.00 8.88 N ANISOU 2156 N GLY B 13 1149 1918 307 93 -225 26 N ATOM 2157 CA GLY B 13 65.231 8.650 21.811 1.00 8.95 C ANISOU 2157 CA GLY B 13 1399 1559 442 99 -363 -145 C ATOM 2158 C GLY B 13 63.796 9.091 21.565 1.00 8.20 C ANISOU 2158 C GLY B 13 1194 1055 868 -193 -172 155 C ATOM 2159 O GLY B 13 63.400 10.203 21.912 1.00 8.85 O ANISOU 2159 O GLY B 13 1051 1244 1068 -39 -101 82 O ATOM 2160 N GLY B 14 63.042 8.192 20.926 1.00 8.97 N ANISOU 2160 N GLY B 14 1321 1637 452 73 -400 -299 N ATOM 2161 CA GLY B 14 61.642 8.479 20.656 1.00 9.39 C ANISOU 2161 CA GLY B 14 1192 1709 667 34 -216 -130 C ATOM 2162 C GLY B 14 61.425 9.076 19.261 1.00 9.50 C ANISOU 2162 C GLY B 14 1083 1892 635 7 -186 -147 C ATOM 2163 O GLY B 14 62.342 9.138 18.426 1.00 8.83 O ANISOU 2163 O GLY B 14 1026 1936 395 161 -329 -174 O ATOM 2164 N MET B 15 60.177 9.501 19.064 1.00 9.01 N ANISOU 2164 N MET B 15 1273 1648 504 360 15 -168 N ATOM 2165 CA MET B 15 59.725 10.060 17.796 1.00 10.49 C ANISOU 2165 CA MET B 15 1234 1799 952 206 -522 -6 C ATOM 2166 C MET B 15 58.923 11.328 18.024 1.00 10.06 C ANISOU 2166 C MET B 15 1164 1895 762 209 -284 130 C ATOM 2167 O MET B 15 57.691 11.343 17.833 1.00 10.48 O ANISOU 2167 O MET B 15 1131 1721 1129 163 -454 -197 O ATOM 2168 CB MET B 15 58.862 9.011 17.046 1.00 11.98 C ANISOU 2168 CB MET B 15 1682 1803 1066 224 -433 -378 C ATOM 2169 CG MET B 15 59.657 7.756 16.728 1.00 11.72 C ANISOU 2169 CG MET B 15 1354 1805 1293 99 -351 -385 C ATOM 2170 SD MET B 15 58.676 6.336 16.189 1.00 11.98 S ANISOU 2170 SD MET B 15 1329 2414 810 -120 -327 -752 S ATOM 2171 CE MET B 15 58.463 6.725 14.454 1.00 14.01 C ANISOU 2171 CE MET B 15 1758 2507 1060 27 -621 -445 C ATOM 2172 N TYR B 16 59.608 12.379 18.456 1.00 10.86 N ANISOU 2172 N TYR B 16 1804 1408 915 200 -84 225 N ATOM 2173 CA TYR B 16 58.964 13.634 18.811 1.00 10.39 C ANISOU 2173 CA TYR B 16 1701 1609 639 191 -350 -117 C ATOM 2174 C TYR B 16 58.869 14.562 17.600 1.00 9.93 C ANISOU 2174 C TYR B 16 1235 1509 1028 256 -287 102 C ATOM 2175 O TYR B 16 59.521 15.577 17.518 1.00 11.19 O ANISOU 2175 O TYR B 16 1395 1824 1032 80 -77 87 O ATOM 2176 CB TYR B 16 59.704 14.309 19.969 1.00 9.84 C ANISOU 2176 CB TYR B 16 1612 1318 810 128 -378 -97 C ATOM 2177 CG TYR B 16 59.606 13.526 21.266 1.00 9.95 C ANISOU 2177 CG TYR B 16 1752 1339 689 128 -53 -234 C ATOM 2178 CD1 TYR B 16 58.547 13.752 22.139 1.00 10.07 C ANISOU 2178 CD1 TYR B 16 1333 1516 976 128 -120 103 C ATOM 2179 CD2 TYR B 16 60.542 12.577 21.636 1.00 9.92 C ANISOU 2179 CD2 TYR B 16 1649 1483 637 150 -6 -224 C ATOM 2180 CE1 TYR B 16 58.438 13.071 23.330 1.00 10.13 C ANISOU 2180 CE1 TYR B 16 1397 1692 759 138 159 -76 C ATOM 2181 CE2 TYR B 16 60.445 11.887 22.825 1.00 9.75 C ANISOU 2181 CE2 TYR B 16 1192 1707 804 -546 -79 -61 C ATOM 2182 CZ TYR B 16 59.388 12.142 23.673 1.00 9.77 C ANISOU 2182 CZ TYR B 16 1537 1487 689 -9 -64 26 C ATOM 2183 OH TYR B 16 59.297 11.467 24.864 1.00 11.92 O ANISOU 2183 OH TYR B 16 1775 1992 761 -404 -181 258 O ATOM 2184 N VAL B 17 58.020 14.146 16.655 1.00 11.06 N ANISOU 2184 N VAL B 17 1364 2148 691 294 -334 287 N ATOM 2185 CA VAL B 17 57.761 14.990 15.490 1.00 10.15 C ANISOU 2185 CA VAL B 17 1410 1769 676 180 -210 169 C ATOM 2186 C VAL B 17 56.261 15.266 15.441 1.00 10.65 C ANISOU 2186 C VAL B 17 1349 1789 910 67 -318 133 C ATOM 2187 O VAL B 17 55.457 14.519 15.977 1.00 11.46 O ANISOU 2187 O VAL B 17 1147 2494 714 44 -369 395 O ATOM 2188 CB VAL B 17 58.148 14.278 14.171 1.00 11.23 C ANISOU 2188 CB VAL B 17 1252 2023 993 298 -61 -24 C ATOM 2189 CG1 VAL B 17 59.667 14.119 14.122 1.00 12.47 C ANISOU 2189 CG1 VAL B 17 1278 1996 1464 514 -41 333 C ATOM 2190 CG2 VAL B 17 57.472 12.927 14.043 1.00 12.89 C ANISOU 2190 CG2 VAL B 17 1376 2002 1522 224 122 208 C ATOM 2191 N PRO B 18 55.875 16.323 14.751 1.00 10.90 N ANISOU 2191 N PRO B 18 1385 1812 946 147 -327 114 N ATOM 2192 CA PRO B 18 54.464 16.581 14.511 1.00 11.68 C ANISOU 2192 CA PRO B 18 1329 1795 1312 125 -237 80 C ATOM 2193 C PRO B 18 53.819 15.347 13.907 1.00 10.91 C ANISOU 2193 C PRO B 18 1436 1670 1039 258 -204 108 C ATOM 2194 O PRO B 18 54.438 14.629 13.105 1.00 12.69 O ANISOU 2194 O PRO B 18 1161 2348 1312 338 -278 -240 O ATOM 2195 CB PRO B 18 54.455 17.778 13.581 1.00 12.23 C ANISOU 2195 CB PRO B 18 1309 1833 1506 22 -99 164 C ATOM 2196 CG PRO B 18 55.766 18.452 13.868 1.00 14.14 C ANISOU 2196 CG PRO B 18 1261 2113 2000 76 -296 -23 C ATOM 2197 CD PRO B 18 56.736 17.311 14.090 1.00 12.65 C ANISOU 2197 CD PRO B 18 1696 1710 1398 -7 -286 148 C ATOM 2198 N GLN B 19 52.558 15.108 14.254 1.00 11.26 N ANISOU 2198 N GLN B 19 1349 1824 1104 276 -344 169 N ATOM 2199 CA GLN B 19 51.812 13.961 13.788 1.00 10.77 C ANISOU 2199 CA GLN B 19 1352 1976 766 67 -260 323 C ATOM 2200 C GLN B 19 51.911 13.731 12.277 1.00 10.33 C ANISOU 2200 C GLN B 19 1489 1635 802 306 -408 149 C ATOM 2201 O GLN B 19 51.950 12.588 11.817 1.00 12.14 O ANISOU 2201 O GLN B 19 1709 2069 836 230 -505 -303 O ATOM 2202 CB GLN B 19 50.331 14.085 14.183 1.00 12.04 C ANISOU 2202 CB GLN B 19 1448 2170 955 133 -99 9 C ATOM 2203 CG GLN B 19 49.568 12.769 14.075 1.00 13.35 C ANISOU 2203 CG GLN B 19 1773 2046 1251 131 23 185 C ATOM 2204 CD GLN B 19 49.996 11.826 15.184 1.00 13.16 C ANISOU 2204 CD GLN B 19 1678 2304 1019 169 -6 122 C ATOM 2205 OE1 GLN B 19 49.913 12.202 16.366 1.00 14.27 O ANISOU 2205 OE1 GLN B 19 1687 2934 802 144 -60 239 O ATOM 2206 NE2 GLN B 19 50.398 10.613 14.859 1.00 15.78 N ANISOU 2206 NE2 GLN B 19 1729 2611 1656 289 679 -21 N ATOM 2207 N ILE B 20 51.919 14.837 11.523 1.00 11.49 N ANISOU 2207 N ILE B 20 2066 1648 651 131 -186 89 N ATOM 2208 CA ILE B 20 51.971 14.713 10.058 1.00 11.50 C ANISOU 2208 CA ILE B 20 1641 2008 720 368 -297 -139 C ATOM 2209 C ILE B 20 53.157 13.913 9.575 1.00 11.80 C ANISOU 2209 C ILE B 20 1826 2040 616 453 -91 114 C ATOM 2210 O ILE B 20 53.073 13.329 8.484 1.00 14.32 O ANISOU 2210 O ILE B 20 2126 2531 783 536 -561 -143 O ATOM 2211 CB ILE B 20 51.945 16.114 9.428 1.00 14.07 C ANISOU 2211 CB ILE B 20 2122 2210 1012 -89 -75 145 C ATOM 2212 CG1 ILE B 20 51.655 16.041 7.923 1.00 16.61 C ANISOU 2212 CG1 ILE B 20 2404 2757 1149 270 -227 -218 C ATOM 2213 CG2 ILE B 20 53.231 16.884 9.652 1.00 14.49 C ANISOU 2213 CG2 ILE B 20 2086 2277 1144 -170 83 180 C ATOM 2214 CD1 ILE B 20 50.217 15.658 7.653 1.00 18.57 C ANISOU 2214 CD1 ILE B 20 2324 3089 1645 532 -554 -98 C ATOM 2215 N LEU B 21 54.265 13.886 10.322 1.00 12.79 N ANISOU 2215 N LEU B 21 1814 2081 965 177 -188 79 N ATOM 2216 CA LEU B 21 55.456 13.169 9.884 1.00 12.29 C ANISOU 2216 CA LEU B 21 1879 1765 1024 74 -136 -17 C ATOM 2217 C LEU B 21 55.530 11.726 10.358 1.00 11.01 C ANISOU 2217 C LEU B 21 1338 1785 1059 354 -192 -40 C ATOM 2218 O LEU B 21 56.421 10.987 9.926 1.00 12.59 O ANISOU 2218 O LEU B 21 1549 2367 866 562 91 -170 O ATOM 2219 CB LEU B 21 56.706 13.916 10.355 1.00 13.35 C ANISOU 2219 CB LEU B 21 1443 2323 1305 119 -111 214 C ATOM 2220 CG LEU B 21 57.173 15.070 9.483 1.00 14.50 C ANISOU 2220 CG LEU B 21 2059 2144 1308 75 225 -20 C ATOM 2221 CD1 LEU B 21 58.360 15.775 10.115 1.00 16.36 C ANISOU 2221 CD1 LEU B 21 2135 2340 1740 -331 492 -149 C ATOM 2222 CD2 LEU B 21 57.577 14.551 8.102 1.00 16.14 C ANISOU 2222 CD2 LEU B 21 2332 2630 1169 -9 20 -152 C ATOM 2223 N MET B 22 54.587 11.295 11.191 1.00 11.57 N ANISOU 2223 N MET B 22 1786 1983 628 139 -140 -94 N ATOM 2224 CA MET B 22 54.648 9.913 11.680 1.00 11.59 C ANISOU 2224 CA MET B 22 1510 1836 1059 150 -206 -245 C ATOM 2225 C MET B 22 54.566 8.885 10.569 1.00 12.94 C ANISOU 2225 C MET B 22 1504 2484 927 152 -200 -490 C ATOM 2226 O MET B 22 55.369 7.956 10.575 1.00 12.89 O ANISOU 2226 O MET B 22 1786 2407 704 216 -296 -467 O ATOM 2227 CB MET B 22 53.684 9.697 12.837 1.00 12.20 C ANISOU 2227 CB MET B 22 1388 2209 1039 123 -245 -183 C ATOM 2228 CG MET B 22 54.106 10.445 14.103 1.00 14.01 C ANISOU 2228 CG MET B 22 1540 2677 1105 281 -369 -366 C ATOM 2229 SD MET B 22 55.652 9.843 14.840 1.00 14.97 S ANISOU 2229 SD MET B 22 1686 2937 1064 338 -458 -240 S ATOM 2230 CE AMET B 22 55.359 8.087 14.542 0.70 13.11 C ANISOU 2230 CE AMET B 22 1015 2745 1222 640 -780 -57 C ATOM 2231 CE BMET B 22 55.098 8.454 15.808 0.30 11.21 C ANISOU 2231 CE BMET B 22 867 2595 798 226 -452 -631 C ATOM 2232 N PRO B 23 53.706 9.042 9.573 1.00 13.26 N ANISOU 2232 N PRO B 23 1651 2492 894 410 -248 -521 N ATOM 2233 CA PRO B 23 53.676 8.019 8.521 1.00 12.93 C ANISOU 2233 CA PRO B 23 1247 2366 1302 131 -438 -664 C ATOM 2234 C PRO B 23 55.000 7.893 7.784 1.00 11.89 C ANISOU 2234 C PRO B 23 1291 2090 1134 189 -452 -229 C ATOM 2235 O PRO B 23 55.423 6.771 7.442 1.00 13.57 O ANISOU 2235 O PRO B 23 1510 2570 1078 537 -524 -638 O ATOM 2236 CB PRO B 23 52.510 8.470 7.637 1.00 14.10 C ANISOU 2236 CB PRO B 23 1330 2725 1302 374 -407 -692 C ATOM 2237 CG PRO B 23 51.600 9.183 8.606 1.00 13.48 C ANISOU 2237 CG PRO B 23 1029 2833 1259 120 -245 -588 C ATOM 2238 CD PRO B 23 52.577 9.985 9.476 1.00 13.70 C ANISOU 2238 CD PRO B 23 1190 2721 1294 181 -418 -539 C ATOM 2239 N ALA B 24 55.688 8.998 7.532 1.00 11.74 N ANISOU 2239 N ALA B 24 1226 2594 638 4 -166 69 N ATOM 2240 CA ALA B 24 56.989 8.951 6.865 1.00 11.02 C ANISOU 2240 CA ALA B 24 1358 1982 848 402 -85 -212 C ATOM 2241 C ALA B 24 57.981 8.166 7.718 1.00 12.57 C ANISOU 2241 C ALA B 24 1554 2506 714 343 -408 -210 C ATOM 2242 O ALA B 24 58.786 7.376 7.207 1.00 13.63 O ANISOU 2242 O ALA B 24 1561 2811 805 253 -341 -506 O ATOM 2243 CB ALA B 24 57.468 10.361 6.591 1.00 13.14 C ANISOU 2243 CB ALA B 24 1811 2091 1088 299 -74 61 C ATOM 2244 N LEU B 25 57.971 8.380 9.045 1.00 12.19 N ANISOU 2244 N LEU B 25 1632 2237 763 391 -492 -377 N ATOM 2245 CA LEU B 25 58.927 7.634 9.872 1.00 10.68 C ANISOU 2245 CA LEU B 25 1351 1948 759 110 -291 -126 C ATOM 2246 C LEU B 25 58.563 6.162 9.900 1.00 11.90 C ANISOU 2246 C LEU B 25 1444 2078 998 -39 -312 -330 C ATOM 2247 O LEU B 25 59.437 5.305 9.867 1.00 12.58 O ANISOU 2247 O LEU B 25 1354 2785 641 288 -472 -510 O ATOM 2248 CB LEU B 25 58.949 8.211 11.286 1.00 12.02 C ANISOU 2248 CB LEU B 25 1793 1828 947 350 -236 -365 C ATOM 2249 CG LEU B 25 59.484 9.626 11.451 1.00 11.61 C ANISOU 2249 CG LEU B 25 1517 1997 899 167 -398 -198 C ATOM 2250 CD1 LEU B 25 59.366 10.055 12.914 1.00 12.56 C ANISOU 2250 CD1 LEU B 25 1335 2378 1061 569 -379 -519 C ATOM 2251 CD2 LEU B 25 60.921 9.799 11.008 1.00 11.74 C ANISOU 2251 CD2 LEU B 25 1755 2119 586 -342 -229 -203 C ATOM 2252 N ASN B 26 57.261 5.864 9.983 1.00 11.87 N ANISOU 2252 N ASN B 26 1286 2133 1090 180 -132 -363 N ATOM 2253 CA ASN B 26 56.890 4.446 9.998 1.00 11.83 C ANISOU 2253 CA ASN B 26 1339 2198 958 -44 -131 -286 C ATOM 2254 C ASN B 26 57.243 3.789 8.659 1.00 12.62 C ANISOU 2254 C ASN B 26 1612 2046 1136 -23 -228 -450 C ATOM 2255 O ASN B 26 57.674 2.641 8.663 1.00 13.06 O ANISOU 2255 O ASN B 26 1670 2005 1286 -109 -583 -913 O ATOM 2256 CB ASN B 26 55.405 4.283 10.291 1.00 13.54 C ANISOU 2256 CB ASN B 26 1193 2913 1036 -153 -447 -253 C ATOM 2257 CG ASN B 26 55.000 4.546 11.732 1.00 19.44 C ANISOU 2257 CG ASN B 26 2398 3385 1601 153 456 -356 C ATOM 2258 OD1 ASN B 26 53.993 5.198 12.008 1.00 23.94 O ANISOU 2258 OD1 ASN B 26 2656 3588 2851 355 405 -461 O ATOM 2259 ND2 ASN B 26 55.787 3.996 12.622 1.00 21.47 N ANISOU 2259 ND2 ASN B 26 2455 4296 1408 288 610 -204 N ATOM 2260 N GLN B 27 57.031 4.497 7.561 1.00 12.46 N ANISOU 2260 N GLN B 27 1462 2312 962 158 -388 -643 N ATOM 2261 CA GLN B 27 57.340 3.931 6.250 1.00 12.77 C ANISOU 2261 CA GLN B 27 1522 2286 1043 171 -200 -639 C ATOM 2262 C GLN B 27 58.837 3.651 6.145 1.00 12.59 C ANISOU 2262 C GLN B 27 1427 2265 1094 -16 -260 -731 C ATOM 2263 O GLN B 27 59.277 2.608 5.671 1.00 13.43 O ANISOU 2263 O GLN B 27 1564 2208 1331 13 -360 -732 O ATOM 2264 CB GLN B 27 56.926 4.915 5.147 1.00 14.26 C ANISOU 2264 CB GLN B 27 1921 2720 778 134 -347 -616 C ATOM 2265 CG GLN B 27 57.369 4.421 3.764 1.00 15.02 C ANISOU 2265 CG GLN B 27 2213 2597 897 41 -292 -766 C ATOM 2266 CD GLN B 27 57.316 5.468 2.691 1.00 16.36 C ANISOU 2266 CD GLN B 27 2106 3037 1073 -291 -177 -443 C ATOM 2267 OE1 GLN B 27 57.632 6.642 2.860 1.00 16.38 O ANISOU 2267 OE1 GLN B 27 1721 3055 1446 -19 -328 -629 O ATOM 2268 NE2 GLN B 27 56.914 5.038 1.465 1.00 20.54 N ANISOU 2268 NE2 GLN B 27 2741 3817 1248 -360 -418 -664 N ATOM 2269 N LEU B 28 59.637 4.589 6.653 1.00 11.42 N ANISOU 2269 N LEU B 28 1267 2387 684 -134 -36 -659 N ATOM 2270 CA LEU B 28 61.096 4.468 6.587 1.00 10.80 C ANISOU 2270 CA LEU B 28 1353 1794 957 8 -118 -521 C ATOM 2271 C LEU B 28 61.567 3.289 7.429 1.00 10.89 C ANISOU 2271 C LEU B 28 1185 2122 831 24 -371 -466 C ATOM 2272 O LEU B 28 62.423 2.517 7.021 1.00 12.20 O ANISOU 2272 O LEU B 28 1551 2059 1027 -146 -87 -881 O ATOM 2273 CB LEU B 28 61.743 5.771 7.053 1.00 11.12 C ANISOU 2273 CB LEU B 28 1469 1714 1040 84 -71 -673 C ATOM 2274 CG LEU B 28 63.268 5.747 7.169 1.00 10.41 C ANISOU 2274 CG LEU B 28 1448 1704 805 180 -20 -554 C ATOM 2275 CD1 LEU B 28 63.927 5.463 5.816 1.00 11.90 C ANISOU 2275 CD1 LEU B 28 1674 2100 748 74 91 -314 C ATOM 2276 CD2 LEU B 28 63.735 7.072 7.744 1.00 12.61 C ANISOU 2276 CD2 LEU B 28 2043 1851 897 -116 -312 -466 C ATOM 2277 N GLU B 29 60.996 3.164 8.633 1.00 11.64 N ANISOU 2277 N GLU B 29 1814 1773 835 8 -171 -464 N ATOM 2278 CA GLU B 29 61.357 2.032 9.479 1.00 10.82 C ANISOU 2278 CA GLU B 29 1564 1777 771 -388 -134 -275 C ATOM 2279 C GLU B 29 61.042 0.695 8.804 1.00 12.17 C ANISOU 2279 C GLU B 29 1816 1675 1132 75 -499 -365 C ATOM 2280 O GLU B 29 61.864 -0.214 8.852 1.00 12.29 O ANISOU 2280 O GLU B 29 2166 1327 1177 40 -286 -856 O ATOM 2281 CB GLU B 29 60.633 2.086 10.826 1.00 10.78 C ANISOU 2281 CB GLU B 29 1648 1593 855 -123 -14 -108 C ATOM 2282 CG GLU B 29 61.092 0.996 11.784 1.00 11.88 C ANISOU 2282 CG GLU B 29 1546 1841 1126 -87 -350 -36 C ATOM 2283 CD GLU B 29 60.112 0.717 12.901 1.00 12.75 C ANISOU 2283 CD GLU B 29 1507 2060 1279 73 -202 -188 C ATOM 2284 OE1 GLU B 29 58.907 0.522 12.608 1.00 14.00 O ANISOU 2284 OE1 GLU B 29 1786 2456 1077 -333 -407 -526 O ATOM 2285 OE2 GLU B 29 60.582 0.662 14.062 1.00 12.81 O ANISOU 2285 OE2 GLU B 29 1520 2168 1179 -281 -217 -735 O ATOM 2286 N GLU B 30 59.832 0.584 8.248 1.00 12.64 N ANISOU 2286 N GLU B 30 1476 1882 1443 -29 -195 -715 N ATOM 2287 CA GLU B 30 59.458 -0.657 7.570 1.00 14.61 C ANISOU 2287 CA GLU B 30 1972 2000 1580 -208 -232 -806 C ATOM 2288 C GLU B 30 60.403 -0.922 6.400 1.00 13.02 C ANISOU 2288 C GLU B 30 1623 1741 1584 -204 -382 -708 C ATOM 2289 O GLU B 30 60.810 -2.076 6.183 1.00 14.37 O ANISOU 2289 O GLU B 30 2191 1733 1536 -198 -467 -1115 O ATOM 2290 CB GLU B 30 58.007 -0.565 7.078 1.00 19.05 C ANISOU 2290 CB GLU B 30 2086 2963 2191 82 -388 -650 C ATOM 2291 CG GLU B 30 57.431 -1.846 6.509 1.00 26.56 C ANISOU 2291 CG GLU B 30 3506 3190 3394 -201 -285 -1009 C ATOM 2292 CD GLU B 30 56.809 -2.786 7.510 1.00 35.42 C ANISOU 2292 CD GLU B 30 4718 4401 4338 -275 -43 -69 C ATOM 2293 OE1 GLU B 30 56.039 -2.360 8.405 1.00 40.43 O ANISOU 2293 OE1 GLU B 30 5259 5150 4954 70 81 -319 O ATOM 2294 OE2 GLU B 30 57.074 -4.007 7.410 1.00 40.15 O ANISOU 2294 OE2 GLU B 30 5425 4771 5059 78 22 -188 O ATOM 2295 N ALA B 31 60.719 0.089 5.603 1.00 11.96 N ANISOU 2295 N ALA B 31 1364 2068 1112 -503 -470 -775 N ATOM 2296 CA ALA B 31 61.593 -0.123 4.441 1.00 12.40 C ANISOU 2296 CA ALA B 31 1528 1824 1359 -83 -206 -392 C ATOM 2297 C ALA B 31 62.977 -0.582 4.883 1.00 11.73 C ANISOU 2297 C ALA B 31 1399 2126 933 -95 -127 -675 C ATOM 2298 O ALA B 31 63.653 -1.385 4.240 1.00 13.76 O ANISOU 2298 O ALA B 31 2144 2221 863 -48 -204 -1049 O ATOM 2299 CB ALA B 31 61.675 1.115 3.573 1.00 12.38 C ANISOU 2299 CB ALA B 31 1658 1961 1086 4 29 -390 C ATOM 2300 N PHE B 32 63.448 0.008 5.996 1.00 12.26 N ANISOU 2300 N PHE B 32 1500 2185 975 -76 -213 -686 N ATOM 2301 CA PHE B 32 64.747 -0.355 6.534 1.00 10.80 C ANISOU 2301 CA PHE B 32 1674 1794 637 22 -212 -596 C ATOM 2302 C PHE B 32 64.755 -1.790 7.031 1.00 11.00 C ANISOU 2302 C PHE B 32 1608 1725 846 -355 -153 -725 C ATOM 2303 O PHE B 32 65.701 -2.523 6.728 1.00 13.40 O ANISOU 2303 O PHE B 32 1582 2219 1290 -132 -240 -867 O ATOM 2304 CB PHE B 32 65.087 0.618 7.677 1.00 11.23 C ANISOU 2304 CB PHE B 32 1480 1742 1045 -196 -146 -724 C ATOM 2305 CG PHE B 32 66.313 0.201 8.429 1.00 12.22 C ANISOU 2305 CG PHE B 32 1458 2071 1115 -404 -173 -518 C ATOM 2306 CD1 PHE B 32 67.572 0.283 7.847 1.00 12.97 C ANISOU 2306 CD1 PHE B 32 1393 2387 1150 -255 -206 -799 C ATOM 2307 CD2 PHE B 32 66.183 -0.270 9.730 1.00 12.88 C ANISOU 2307 CD2 PHE B 32 1244 2509 1141 -196 -157 -370 C ATOM 2308 CE1 PHE B 32 68.694 -0.087 8.557 1.00 12.70 C ANISOU 2308 CE1 PHE B 32 1068 2344 1412 -156 164 -413 C ATOM 2309 CE2 PHE B 32 67.310 -0.658 10.433 1.00 12.24 C ANISOU 2309 CE2 PHE B 32 1271 2214 1166 -67 -59 -353 C ATOM 2310 CZ PHE B 32 68.548 -0.559 9.839 1.00 12.40 C ANISOU 2310 CZ PHE B 32 1011 2461 1238 -16 -296 -467 C ATOM 2311 N VAL B 33 63.754 -2.194 7.806 1.00 11.01 N ANISOU 2311 N VAL B 33 1381 1770 1033 -359 -292 -422 N ATOM 2312 CA VAL B 33 63.713 -3.588 8.286 1.00 12.07 C ANISOU 2312 CA VAL B 33 1550 1894 1143 -342 -286 -238 C ATOM 2313 C VAL B 33 63.698 -4.547 7.099 1.00 13.88 C ANISOU 2313 C VAL B 33 1805 1898 1570 -244 -346 -453 C ATOM 2314 O VAL B 33 64.380 -5.562 7.109 1.00 15.12 O ANISOU 2314 O VAL B 33 1964 1904 1876 -218 -247 -315 O ATOM 2315 CB VAL B 33 62.499 -3.789 9.196 1.00 12.64 C ANISOU 2315 CB VAL B 33 1933 1822 1047 -532 -55 -403 C ATOM 2316 CG1 VAL B 33 62.179 -5.240 9.498 1.00 15.52 C ANISOU 2316 CG1 VAL B 33 2348 1790 1759 -320 -4 -228 C ATOM 2317 CG2 VAL B 33 62.739 -3.035 10.516 1.00 14.37 C ANISOU 2317 CG2 VAL B 33 1972 2346 1140 -229 -78 -679 C ATOM 2318 N SER B 34 62.912 -4.207 6.077 1.00 12.20 N ANISOU 2318 N SER B 34 1686 1864 1085 -356 -213 -853 N ATOM 2319 CA SER B 34 62.876 -5.066 4.880 1.00 12.77 C ANISOU 2319 CA SER B 34 1761 1583 1508 -335 -161 -1005 C ATOM 2320 C SER B 34 64.209 -5.091 4.160 1.00 13.22 C ANISOU 2320 C SER B 34 1742 1739 1544 -308 -180 -611 C ATOM 2321 O SER B 34 64.668 -6.164 3.748 1.00 14.69 O ANISOU 2321 O SER B 34 2178 1692 1712 -414 33 -745 O ATOM 2322 CB SER B 34 61.733 -4.577 4.001 1.00 13.30 C ANISOU 2322 CB SER B 34 2334 1569 1151 -273 -182 -628 C ATOM 2323 OG ASER B 34 61.691 -5.274 2.764 0.70 13.01 O ANISOU 2323 OG ASER B 34 1783 2325 834 -374 -530 -668 O ATOM 2324 OG BSER B 34 61.970 -3.293 3.475 0.30 14.58 O ANISOU 2324 OG BSER B 34 2321 1679 1538 -29 -270 -243 O ATOM 2325 N ALA B 35 64.826 -3.933 3.961 1.00 11.65 N ANISOU 2325 N ALA B 35 1511 1780 1134 -283 26 -647 N ATOM 2326 CA ALA B 35 66.126 -3.867 3.301 1.00 11.10 C ANISOU 2326 CA ALA B 35 1363 1670 1183 -209 -120 -487 C ATOM 2327 C ALA B 35 67.199 -4.660 4.027 1.00 13.14 C ANISOU 2327 C ALA B 35 1522 2127 1345 -6 -175 -463 C ATOM 2328 O ALA B 35 68.041 -5.309 3.402 1.00 14.31 O ANISOU 2328 O ALA B 35 1578 2189 1669 -181 -241 -1075 O ATOM 2329 CB ALA B 35 66.560 -2.416 3.183 1.00 11.32 C ANISOU 2329 CB ALA B 35 1264 1989 1049 -665 198 -97 C ATOM 2330 N GLN B 36 67.176 -4.635 5.360 1.00 12.99 N ANISOU 2330 N GLN B 36 1566 2033 1338 -153 -84 -432 N ATOM 2331 CA GLN B 36 68.195 -5.347 6.126 1.00 14.69 C ANISOU 2331 CA GLN B 36 1971 2098 1512 -4 -131 -202 C ATOM 2332 C GLN B 36 68.112 -6.852 5.938 1.00 16.51 C ANISOU 2332 C GLN B 36 2257 2092 1922 -17 -347 -253 C ATOM 2333 O GLN B 36 69.116 -7.551 6.157 1.00 19.12 O ANISOU 2333 O GLN B 36 2326 2264 2673 49 -416 -321 O ATOM 2334 CB GLN B 36 68.087 -4.958 7.610 1.00 15.32 C ANISOU 2334 CB GLN B 36 2155 2181 1482 -182 -448 -233 C ATOM 2335 CG GLN B 36 68.521 -3.509 7.819 1.00 17.95 C ANISOU 2335 CG GLN B 36 2631 2124 2064 32 -302 -611 C ATOM 2336 CD GLN B 36 69.984 -3.306 7.463 1.00 21.24 C ANISOU 2336 CD GLN B 36 2770 2504 2796 -134 -142 -382 C ATOM 2337 OE1 GLN B 36 70.312 -2.985 6.321 1.00 24.78 O ANISOU 2337 OE1 GLN B 36 3266 2842 3306 -315 589 -383 O ATOM 2338 NE2 GLN B 36 70.834 -3.490 8.471 1.00 22.80 N ANISOU 2338 NE2 GLN B 36 2676 2768 3218 -181 -353 -466 N ATOM 2339 N LYS B 37 66.945 -7.349 5.530 1.00 17.37 N ANISOU 2339 N LYS B 37 2409 2177 2014 -361 -151 -256 N ATOM 2340 CA LYS B 37 66.780 -8.773 5.283 1.00 19.68 C ANISOU 2340 CA LYS B 37 3024 2124 2328 -135 -9 -158 C ATOM 2341 C LYS B 37 66.864 -9.102 3.791 1.00 19.19 C ANISOU 2341 C LYS B 37 2826 2182 2282 -468 182 -45 C ATOM 2342 O LYS B 37 66.705 -10.271 3.434 1.00 21.89 O ANISOU 2342 O LYS B 37 3182 2186 2950 -288 340 -243 O ATOM 2343 CB LYS B 37 65.432 -9.291 5.773 1.00 24.22 C ANISOU 2343 CB LYS B 37 3268 2690 3244 -492 61 -89 C ATOM 2344 CG LYS B 37 64.976 -8.892 7.156 1.00 28.39 C ANISOU 2344 CG LYS B 37 3839 3556 3393 -207 238 -51 C ATOM 2345 CD LYS B 37 63.485 -9.207 7.298 1.00 31.80 C ANISOU 2345 CD LYS B 37 3930 4078 4074 -262 142 -13 C ATOM 2346 CE LYS B 37 62.915 -8.608 8.572 1.00 33.32 C ANISOU 2346 CE LYS B 37 4202 4239 4219 -42 111 -91 C ATOM 2347 NZ ALYS B 37 63.724 -8.984 9.764 0.50 32.78 N ANISOU 2347 NZ ALYS B 37 4115 4111 4229 -80 82 38 N ATOM 2348 NZ BLYS B 37 61.421 -8.682 8.574 0.50 32.61 N ANISOU 2348 NZ BLYS B 37 4116 4175 4102 -98 23 19 N ATOM 2349 N ASP B 38 67.112 -8.107 2.953 1.00 14.53 N ANISOU 2349 N ASP B 38 1829 1741 1952 -607 -92 -387 N ATOM 2350 CA ASP B 38 67.121 -8.345 1.502 1.00 14.39 C ANISOU 2350 CA ASP B 38 1733 1775 1962 -595 -46 -490 C ATOM 2351 C ASP B 38 68.533 -8.522 0.979 1.00 16.99 C ANISOU 2351 C ASP B 38 1680 2012 2764 -211 -57 -414 C ATOM 2352 O ASP B 38 69.295 -7.543 0.958 1.00 16.87 O ANISOU 2352 O ASP B 38 1823 2303 2284 -519 171 -1119 O ATOM 2353 CB ASP B 38 66.462 -7.145 0.825 1.00 15.92 C ANISOU 2353 CB ASP B 38 1787 2129 2133 -167 -127 -608 C ATOM 2354 CG ASP B 38 66.327 -7.255 -0.681 1.00 17.47 C ANISOU 2354 CG ASP B 38 1956 2481 2202 -57 -333 -762 C ATOM 2355 OD1 ASP B 38 66.951 -8.175 -1.247 1.00 18.59 O ANISOU 2355 OD1 ASP B 38 2103 2826 2135 -275 -95 -1204 O ATOM 2356 OD2 ASP B 38 65.646 -6.409 -1.289 1.00 18.55 O ANISOU 2356 OD2 ASP B 38 2529 2790 1731 -15 -614 -780 O ATOM 2357 N PRO B 39 68.920 -9.712 0.550 1.00 18.68 N ANISOU 2357 N PRO B 39 1952 2106 3038 -381 205 -664 N ATOM 2358 CA PRO B 39 70.278 -9.956 0.078 1.00 18.67 C ANISOU 2358 CA PRO B 39 1965 2030 3098 -230 205 -608 C ATOM 2359 C PRO B 39 70.673 -9.108 -1.108 1.00 16.26 C ANISOU 2359 C PRO B 39 1742 1494 2941 -183 65 -827 C ATOM 2360 O PRO B 39 71.867 -8.740 -1.236 1.00 18.64 O ANISOU 2360 O PRO B 39 1682 1958 3442 -184 502 -1056 O ATOM 2361 CB PRO B 39 70.305 -11.450 -0.245 1.00 20.92 C ANISOU 2361 CB PRO B 39 2628 2011 3308 -150 90 -502 C ATOM 2362 CG PRO B 39 68.870 -11.766 -0.487 1.00 22.09 C ANISOU 2362 CG PRO B 39 2641 2195 3558 -287 239 -597 C ATOM 2363 CD PRO B 39 68.084 -10.941 0.506 1.00 20.69 C ANISOU 2363 CD PRO B 39 2565 1912 3384 -398 47 -656 C ATOM 2364 N GLU B 40 69.729 -8.702 -1.929 1.00 15.63 N ANISOU 2364 N GLU B 40 2064 1469 2406 -314 -37 -1090 N ATOM 2365 CA GLU B 40 69.988 -7.856 -3.078 1.00 18.33 C ANISOU 2365 CA GLU B 40 2201 2046 2716 -224 172 -655 C ATOM 2366 C GLU B 40 70.346 -6.435 -2.636 1.00 17.38 C ANISOU 2366 C GLU B 40 2207 2293 2105 -446 243 -812 C ATOM 2367 O GLU B 40 71.245 -5.832 -3.218 1.00 16.81 O ANISOU 2367 O GLU B 40 1902 2450 2034 -575 202 -1259 O ATOM 2368 CB GLU B 40 68.831 -7.838 -4.070 1.00 23.80 C ANISOU 2368 CB GLU B 40 2618 3306 3119 -234 -171 -311 C ATOM 2369 CG GLU B 40 68.641 -9.217 -4.711 1.00 30.88 C ANISOU 2369 CG GLU B 40 4150 3421 4162 -207 63 -460 C ATOM 2370 CD GLU B 40 67.270 -9.292 -5.354 1.00 36.25 C ANISOU 2370 CD GLU B 40 4428 4603 4744 -17 -291 -188 C ATOM 2371 OE1 GLU B 40 66.844 -8.271 -5.932 1.00 38.82 O ANISOU 2371 OE1 GLU B 40 5058 4678 5014 -2 -66 -108 O ATOM 2372 OE2 GLU B 40 66.635 -10.359 -5.256 1.00 40.69 O ANISOU 2372 OE2 GLU B 40 5189 4823 5450 -74 -9 -18 O ATOM 2373 N PHE B 41 69.644 -5.933 -1.626 1.00 16.52 N ANISOU 2373 N PHE B 41 1818 2075 2384 -391 220 -892 N ATOM 2374 CA PHE B 41 69.965 -4.598 -1.112 1.00 13.96 C ANISOU 2374 CA PHE B 41 1363 1891 2050 -47 352 -794 C ATOM 2375 C PHE B 41 71.351 -4.625 -0.466 1.00 12.87 C ANISOU 2375 C PHE B 41 1525 1725 1641 -15 304 -497 C ATOM 2376 O PHE B 41 72.191 -3.759 -0.716 1.00 14.39 O ANISOU 2376 O PHE B 41 1777 2046 1643 -439 82 -917 O ATOM 2377 CB PHE B 41 68.919 -4.187 -0.072 1.00 13.74 C ANISOU 2377 CB PHE B 41 1313 1771 2138 -25 383 -776 C ATOM 2378 CG PHE B 41 69.106 -2.801 0.491 1.00 13.66 C ANISOU 2378 CG PHE B 41 1905 1718 1566 -88 294 -560 C ATOM 2379 CD1 PHE B 41 69.992 -2.619 1.534 1.00 13.62 C ANISOU 2379 CD1 PHE B 41 1445 2106 1623 -106 459 -430 C ATOM 2380 CD2 PHE B 41 68.397 -1.718 -0.001 1.00 14.03 C ANISOU 2380 CD2 PHE B 41 1718 1936 1677 -102 347 -395 C ATOM 2381 CE1 PHE B 41 70.204 -1.349 2.047 1.00 14.03 C ANISOU 2381 CE1 PHE B 41 1564 1902 1864 13 482 -340 C ATOM 2382 CE2 PHE B 41 68.577 -0.459 0.543 1.00 14.45 C ANISOU 2382 CE2 PHE B 41 2057 1903 1532 21 0 -313 C ATOM 2383 CZ PHE B 41 69.500 -0.274 1.557 1.00 14.45 C ANISOU 2383 CZ PHE B 41 1995 2263 1233 -190 119 193 C ATOM 2384 N GLN B 42 71.588 -5.677 0.323 1.00 13.29 N ANISOU 2384 N GLN B 42 1381 1856 1812 47 68 -398 N ATOM 2385 CA GLN B 42 72.881 -5.796 0.996 1.00 14.21 C ANISOU 2385 CA GLN B 42 1474 2117 1808 4 44 -258 C ATOM 2386 C GLN B 42 74.000 -5.873 -0.029 1.00 14.12 C ANISOU 2386 C GLN B 42 1669 1901 1796 -317 164 -460 C ATOM 2387 O GLN B 42 75.043 -5.270 0.201 1.00 15.25 O ANISOU 2387 O GLN B 42 1520 1842 2433 -251 185 -605 O ATOM 2388 CB GLN B 42 72.934 -6.953 1.985 1.00 15.74 C ANISOU 2388 CB GLN B 42 1690 2232 2058 -48 20 -99 C ATOM 2389 CG GLN B 42 71.886 -6.844 3.094 1.00 16.92 C ANISOU 2389 CG GLN B 42 2009 2594 1825 -22 26 -299 C ATOM 2390 CD GLN B 42 72.010 -5.543 3.869 1.00 17.55 C ANISOU 2390 CD GLN B 42 1975 2760 1934 -270 -90 -405 C ATOM 2391 OE1 GLN B 42 73.128 -5.190 4.263 1.00 19.66 O ANISOU 2391 OE1 GLN B 42 2120 3211 2138 -438 -219 -646 O ATOM 2392 NE2 GLN B 42 70.920 -4.825 4.070 1.00 18.31 N ANISOU 2392 NE2 GLN B 42 2028 2960 1970 -199 -251 -587 N ATOM 2393 N ALA B 43 73.806 -6.626 -1.108 1.00 15.79 N ANISOU 2393 N ALA B 43 2042 2349 1611 -460 76 -485 N ATOM 2394 CA ALA B 43 74.872 -6.745 -2.110 1.00 15.19 C ANISOU 2394 CA ALA B 43 2036 1848 1888 -298 162 -696 C ATOM 2395 C ALA B 43 75.093 -5.430 -2.836 1.00 13.62 C ANISOU 2395 C ALA B 43 1856 1750 1567 -75 67 -813 C ATOM 2396 O ALA B 43 76.239 -5.075 -3.144 1.00 15.99 O ANISOU 2396 O ALA B 43 1852 2408 1816 -177 171 -870 O ATOM 2397 CB ALA B 43 74.526 -7.869 -3.086 1.00 15.56 C ANISOU 2397 CB ALA B 43 2141 1598 2173 -142 475 -832 C ATOM 2398 N GLN B 44 74.024 -4.706 -3.165 1.00 13.13 N ANISOU 2398 N GLN B 44 1949 1484 1555 -122 -100 -989 N ATOM 2399 CA GLN B 44 74.164 -3.427 -3.833 1.00 12.04 C ANISOU 2399 CA GLN B 44 1758 1848 969 17 -105 -743 C ATOM 2400 C GLN B 44 74.933 -2.439 -2.936 1.00 11.34 C ANISOU 2400 C GLN B 44 1651 1751 907 -254 -170 -320 C ATOM 2401 O GLN B 44 75.815 -1.722 -3.376 1.00 12.20 O ANISOU 2401 O GLN B 44 1799 1940 896 -457 -31 -574 O ATOM 2402 CB GLN B 44 72.830 -2.792 -4.243 1.00 13.95 C ANISOU 2402 CB GLN B 44 1618 2186 1496 -56 -262 -791 C ATOM 2403 CG GLN B 44 73.065 -1.521 -5.041 1.00 18.02 C ANISOU 2403 CG GLN B 44 2460 2704 1685 -148 -303 -366 C ATOM 2404 CD GLN B 44 71.899 -0.947 -5.815 1.00 21.25 C ANISOU 2404 CD GLN B 44 2770 3174 2132 131 -359 -127 C ATOM 2405 OE1 GLN B 44 72.116 -0.059 -6.650 1.00 24.86 O ANISOU 2405 OE1 GLN B 44 3899 3251 2295 164 -371 -32 O ATOM 2406 NE2 GLN B 44 70.701 -1.414 -5.534 1.00 22.12 N ANISOU 2406 NE2 GLN B 44 2670 3491 2242 -2 -603 -319 N ATOM 2407 N PHE B 45 74.560 -2.427 -1.656 1.00 11.84 N ANISOU 2407 N PHE B 45 1662 1990 848 -342 -149 -495 N ATOM 2408 CA PHE B 45 75.228 -1.505 -0.714 1.00 10.28 C ANISOU 2408 CA PHE B 45 1331 1519 1056 -133 -47 -469 C ATOM 2409 C PHE B 45 76.697 -1.884 -0.585 1.00 11.16 C ANISOU 2409 C PHE B 45 1493 1623 1126 140 -74 -128 C ATOM 2410 O PHE B 45 77.577 -1.022 -0.700 1.00 10.66 O ANISOU 2410 O PHE B 45 1584 1975 491 -53 -32 -300 O ATOM 2411 CB PHE B 45 74.465 -1.534 0.597 1.00 10.52 C ANISOU 2411 CB PHE B 45 1520 1578 900 -159 -95 -652 C ATOM 2412 CG PHE B 45 74.892 -0.572 1.683 1.00 10.52 C ANISOU 2412 CG PHE B 45 1730 1425 840 -166 -289 -460 C ATOM 2413 CD1 PHE B 45 75.502 0.629 1.403 1.00 10.22 C ANISOU 2413 CD1 PHE B 45 1388 1512 981 -70 -198 -316 C ATOM 2414 CD2 PHE B 45 74.673 -0.905 3.017 1.00 12.35 C ANISOU 2414 CD2 PHE B 45 1848 1880 963 -220 -114 -291 C ATOM 2415 CE1 PHE B 45 75.860 1.516 2.400 1.00 11.45 C ANISOU 2415 CE1 PHE B 45 1550 1852 950 -122 -157 -395 C ATOM 2416 CE2 PHE B 45 75.044 -0.025 4.026 1.00 12.22 C ANISOU 2416 CE2 PHE B 45 2011 1819 815 -228 -77 -202 C ATOM 2417 CZ PHE B 45 75.631 1.188 3.721 1.00 10.60 C ANISOU 2417 CZ PHE B 45 1449 1723 855 -175 -103 -551 C ATOM 2418 N ALA B 46 76.964 -3.179 -0.404 1.00 10.57 N ANISOU 2418 N ALA B 46 1346 1597 1074 83 334 -24 N ATOM 2419 CA ALA B 46 78.354 -3.630 -0.305 1.00 10.25 C ANISOU 2419 CA ALA B 46 1377 1328 1188 -50 -293 263 C ATOM 2420 C ALA B 46 79.168 -3.267 -1.543 1.00 10.83 C ANISOU 2420 C ALA B 46 1088 1921 1106 -14 -73 -425 C ATOM 2421 O ALA B 46 80.347 -2.893 -1.438 1.00 11.85 O ANISOU 2421 O ALA B 46 1074 2104 1324 -11 -141 -364 O ATOM 2422 CB ALA B 46 78.400 -5.134 -0.058 1.00 12.52 C ANISOU 2422 CB ALA B 46 1397 1263 2097 349 -130 108 C ATOM 2423 N ASP B 47 78.549 -3.417 -2.718 1.00 11.58 N ANISOU 2423 N ASP B 47 1374 1959 1068 -155 -117 -390 N ATOM 2424 CA ASP B 47 79.267 -3.103 -3.960 1.00 12.54 C ANISOU 2424 CA ASP B 47 1446 2150 1170 -416 -162 -239 C ATOM 2425 C ASP B 47 79.610 -1.625 -4.049 1.00 10.72 C ANISOU 2425 C ASP B 47 1405 2004 665 -33 -107 -75 C ATOM 2426 O ASP B 47 80.735 -1.288 -4.428 1.00 11.39 O ANISOU 2426 O ASP B 47 1469 2267 590 -250 -18 -492 O ATOM 2427 CB ASP B 47 78.452 -3.568 -5.176 1.00 14.50 C ANISOU 2427 CB ASP B 47 1959 2514 1038 -177 -151 -611 C ATOM 2428 CG ASP B 47 79.281 -3.324 -6.444 1.00 18.37 C ANISOU 2428 CG ASP B 47 2985 3110 884 -123 2 -594 C ATOM 2429 OD1 ASP B 47 80.142 -4.165 -6.745 1.00 25.12 O ANISOU 2429 OD1 ASP B 47 2977 3828 2739 191 48 -563 O ATOM 2430 OD2 ASP B 47 79.076 -2.287 -7.070 1.00 24.41 O ANISOU 2430 OD2 ASP B 47 4600 3308 1365 -79 -11 -422 O ATOM 2431 N LEU B 48 78.689 -0.729 -3.689 1.00 10.46 N ANISOU 2431 N LEU B 48 1601 1966 407 -66 -163 -370 N ATOM 2432 CA LEU B 48 78.990 0.692 -3.695 1.00 10.67 C ANISOU 2432 CA LEU B 48 1532 1985 538 -84 -300 -137 C ATOM 2433 C LEU B 48 80.103 0.997 -2.678 1.00 9.96 C ANISOU 2433 C LEU B 48 1229 1954 601 -147 -167 -45 C ATOM 2434 O LEU B 48 80.997 1.778 -2.961 1.00 10.08 O ANISOU 2434 O LEU B 48 1533 1899 399 -293 -47 -268 O ATOM 2435 CB LEU B 48 77.745 1.498 -3.317 1.00 12.10 C ANISOU 2435 CB LEU B 48 1683 2022 891 165 -524 -93 C ATOM 2436 CG LEU B 48 76.667 1.471 -4.417 1.00 14.41 C ANISOU 2436 CG LEU B 48 1640 2676 1159 -14 -618 -102 C ATOM 2437 CD1 LEU B 48 75.422 2.164 -3.910 1.00 15.69 C ANISOU 2437 CD1 LEU B 48 1927 2529 1506 89 -312 39 C ATOM 2438 CD2 LEU B 48 77.207 2.152 -5.661 1.00 18.98 C ANISOU 2438 CD2 LEU B 48 2082 3361 1771 -55 -356 447 C ATOM 2439 N LEU B 49 79.981 0.381 -1.497 1.00 9.68 N ANISOU 2439 N LEU B 49 1219 2119 341 -13 -242 -163 N ATOM 2440 CA LEU B 49 81.001 0.667 -0.472 1.00 9.81 C ANISOU 2440 CA LEU B 49 1111 2041 577 -287 -212 -39 C ATOM 2441 C LEU B 49 82.384 0.278 -0.954 1.00 8.74 C ANISOU 2441 C LEU B 49 1330 1439 551 36 -206 86 C ATOM 2442 O LEU B 49 83.355 1.012 -0.735 1.00 9.69 O ANISOU 2442 O LEU B 49 1291 1943 448 -74 -402 -47 O ATOM 2443 CB LEU B 49 80.633 -0.079 0.819 1.00 9.69 C ANISOU 2443 CB LEU B 49 1213 1880 591 -92 -346 59 C ATOM 2444 CG LEU B 49 79.407 0.486 1.539 1.00 9.51 C ANISOU 2444 CG LEU B 49 1348 1380 883 -249 -92 97 C ATOM 2445 CD1 LEU B 49 78.971 -0.441 2.666 1.00 12.19 C ANISOU 2445 CD1 LEU B 49 1391 2304 937 -81 232 429 C ATOM 2446 CD2 LEU B 49 79.661 1.893 2.069 1.00 10.67 C ANISOU 2446 CD2 LEU B 49 1261 1566 1227 40 115 -365 C ATOM 2447 N LYS B 50 82.472 -0.896 -1.579 1.00 8.86 N ANISOU 2447 N LYS B 50 1328 1676 364 146 133 -29 N ATOM 2448 CA LYS B 50 83.761 -1.395 -2.032 1.00 9.40 C ANISOU 2448 CA LYS B 50 1284 1489 797 132 102 43 C ATOM 2449 C LYS B 50 84.303 -0.669 -3.256 1.00 10.31 C ANISOU 2449 C LYS B 50 1659 1700 559 158 -123 123 C ATOM 2450 O LYS B 50 85.400 -0.148 -3.273 1.00 11.51 O ANISOU 2450 O LYS B 50 1725 2050 596 7 18 -19 O ATOM 2451 CB ALYS B 50 83.631 -2.893 -2.363 0.50 8.83 C ANISOU 2451 CB ALYS B 50 1491 1362 504 147 274 276 C ATOM 2452 CG ALYS B 50 84.937 -3.517 -2.818 0.50 12.70 C ANISOU 2452 CG ALYS B 50 1492 1718 1614 112 405 33 C ATOM 2453 CD ALYS B 50 84.784 -4.993 -3.153 0.50 15.69 C ANISOU 2453 CD ALYS B 50 1955 1827 2180 73 160 -96 C ATOM 2454 CE ALYS B 50 86.135 -5.538 -3.612 0.50 19.66 C ANISOU 2454 CE ALYS B 50 2229 2503 2738 327 253 -182 C ATOM 2455 NZ ALYS B 50 86.010 -6.935 -4.118 0.50 23.10 N ANISOU 2455 NZ ALYS B 50 2891 2643 3243 225 204 -283 N ATOM 2456 CB BLYS B 50 83.673 -2.883 -2.398 0.50 11.57 C ANISOU 2456 CB BLYS B 50 1726 1524 1148 199 119 -75 C ATOM 2457 CG BLYS B 50 83.372 -3.820 -1.248 0.50 15.15 C ANISOU 2457 CG BLYS B 50 2180 2038 1539 -149 141 214 C ATOM 2458 CD BLYS B 50 83.221 -5.251 -1.738 0.50 19.63 C ANISOU 2458 CD BLYS B 50 2927 2186 2345 -83 86 84 C ATOM 2459 CE BLYS B 50 82.339 -6.056 -0.783 0.50 19.69 C ANISOU 2459 CE BLYS B 50 2916 2400 2164 -32 66 216 C ATOM 2460 NZ BLYS B 50 82.083 -7.404 -1.359 0.50 22.16 N ANISOU 2460 NZ BLYS B 50 3146 2653 2621 -243 -51 154 N ATOM 2461 N ASN B 51 83.491 -0.662 -4.313 1.00 10.46 N ANISOU 2461 N ASN B 51 1766 1783 426 35 -110 81 N ATOM 2462 CA ASN B 51 83.974 -0.201 -5.611 1.00 10.86 C ANISOU 2462 CA ASN B 51 1971 1605 549 -209 148 -145 C ATOM 2463 C ASN B 51 83.806 1.258 -5.925 1.00 10.05 C ANISOU 2463 C ASN B 51 1575 1720 522 -26 -153 70 C ATOM 2464 O ASN B 51 84.473 1.758 -6.840 1.00 12.20 O ANISOU 2464 O ASN B 51 1892 2182 563 -114 105 32 O ATOM 2465 CB ASN B 51 83.275 -1.051 -6.682 1.00 11.10 C ANISOU 2465 CB ASN B 51 2173 1676 369 -223 289 -252 C ATOM 2466 CG ASN B 51 83.644 -2.514 -6.515 1.00 13.16 C ANISOU 2466 CG ASN B 51 2018 1686 1298 -101 -3 -586 C ATOM 2467 OD1 ASN B 51 84.835 -2.816 -6.409 1.00 16.70 O ANISOU 2467 OD1 ASN B 51 1855 1990 2502 -50 948 -320 O ATOM 2468 ND2 ASN B 51 82.654 -3.395 -6.445 1.00 15.69 N ANISOU 2468 ND2 ASN B 51 2359 2160 1441 -483 401 -759 N ATOM 2469 N TYR B 52 83.003 1.966 -5.159 1.00 10.48 N ANISOU 2469 N TYR B 52 1819 1618 546 2 -273 -192 N ATOM 2470 CA TYR B 52 82.811 3.392 -5.343 1.00 9.98 C ANISOU 2470 CA TYR B 52 1433 1649 709 11 -176 61 C ATOM 2471 C TYR B 52 83.466 4.161 -4.200 1.00 10.51 C ANISOU 2471 C TYR B 52 1802 1533 657 -33 -397 319 C ATOM 2472 O TYR B 52 84.179 5.132 -4.403 1.00 10.07 O ANISOU 2472 O TYR B 52 1844 1682 301 -142 -168 176 O ATOM 2473 CB TYR B 52 81.311 3.727 -5.465 1.00 9.74 C ANISOU 2473 CB TYR B 52 1495 1703 502 191 -162 -299 C ATOM 2474 CG TYR B 52 81.060 5.214 -5.540 1.00 10.00 C ANISOU 2474 CG TYR B 52 1641 1723 437 275 -172 -21 C ATOM 2475 CD1 TYR B 52 81.272 5.919 -6.719 1.00 10.02 C ANISOU 2475 CD1 TYR B 52 1489 1348 970 1 -36 229 C ATOM 2476 CD2 TYR B 52 80.584 5.935 -4.447 1.00 10.44 C ANISOU 2476 CD2 TYR B 52 1967 1517 484 78 -331 -283 C ATOM 2477 CE1 TYR B 52 81.046 7.279 -6.801 1.00 9.95 C ANISOU 2477 CE1 TYR B 52 1427 1343 1011 82 -11 114 C ATOM 2478 CE2 TYR B 52 80.340 7.292 -4.527 1.00 11.02 C ANISOU 2478 CE2 TYR B 52 2151 1555 483 30 -9 66 C ATOM 2479 CZ TYR B 52 80.566 7.972 -5.709 1.00 10.46 C ANISOU 2479 CZ TYR B 52 1737 1549 689 102 -77 256 C ATOM 2480 OH TYR B 52 80.348 9.323 -5.793 1.00 12.03 O ANISOU 2480 OH TYR B 52 2001 1637 935 298 129 -32 O ATOM 2481 N ALA B 53 83.199 3.730 -2.957 1.00 9.42 N ANISOU 2481 N ALA B 53 1751 1394 435 -241 -228 -31 N ATOM 2482 CA ALA B 53 83.704 4.495 -1.813 1.00 10.14 C ANISOU 2482 CA ALA B 53 1564 1762 525 -126 -243 -229 C ATOM 2483 C ALA B 53 85.094 4.062 -1.356 1.00 9.76 C ANISOU 2483 C ALA B 53 1426 1782 501 -171 -68 -36 C ATOM 2484 O ALA B 53 85.719 4.879 -0.664 1.00 11.05 O ANISOU 2484 O ALA B 53 1797 2081 322 -422 -246 90 O ATOM 2485 CB ALA B 53 82.747 4.351 -0.631 1.00 10.04 C ANISOU 2485 CB ALA B 53 1602 1728 484 -230 -290 170 C ATOM 2486 N GLY B 54 85.540 2.858 -1.685 1.00 10.34 N ANISOU 2486 N GLY B 54 1773 1734 421 157 -174 455 N ATOM 2487 CA GLY B 54 86.876 2.430 -1.293 1.00 11.06 C ANISOU 2487 CA GLY B 54 1580 1746 876 9 42 655 C ATOM 2488 C GLY B 54 86.978 1.576 -0.045 1.00 11.54 C ANISOU 2488 C GLY B 54 1361 2446 578 -59 -372 544 C ATOM 2489 O GLY B 54 88.109 1.488 0.460 1.00 15.37 O ANISOU 2489 O GLY B 54 1276 3017 1545 200 -289 1573 O ATOM 2490 N ARG B 55 85.903 0.974 0.437 1.00 9.16 N ANISOU 2490 N ARG B 55 1645 1288 547 245 -52 281 N ATOM 2491 CA ARG B 55 86.071 0.081 1.601 1.00 8.09 C ANISOU 2491 CA ARG B 55 1361 1318 395 144 -155 241 C ATOM 2492 C ARG B 55 86.695 -1.238 1.191 1.00 9.13 C ANISOU 2492 C ARG B 55 1421 1720 329 320 -18 -19 C ATOM 2493 O ARG B 55 86.509 -1.675 0.039 1.00 11.35 O ANISOU 2493 O ARG B 55 1815 2044 453 347 -183 -263 O ATOM 2494 CB ARG B 55 84.693 -0.165 2.212 1.00 9.09 C ANISOU 2494 CB ARG B 55 1352 1275 826 192 -73 141 C ATOM 2495 CG ARG B 55 83.988 1.110 2.680 1.00 9.68 C ANISOU 2495 CG ARG B 55 1424 1595 658 248 275 -140 C ATOM 2496 CD ARG B 55 83.096 0.870 3.901 1.00 8.23 C ANISOU 2496 CD ARG B 55 1049 1690 389 125 -113 84 C ATOM 2497 NE ARG B 55 83.970 0.672 5.077 1.00 9.25 N ANISOU 2497 NE ARG B 55 1115 1914 485 -311 -315 -233 N ATOM 2498 CZ ARG B 55 84.430 1.692 5.796 1.00 7.76 C ANISOU 2498 CZ ARG B 55 1186 1447 316 40 -229 -124 C ATOM 2499 NH1 ARG B 55 84.087 2.948 5.543 1.00 9.76 N ANISOU 2499 NH1 ARG B 55 1795 1520 392 121 -462 -120 N ATOM 2500 NH2 ARG B 55 85.277 1.441 6.801 1.00 8.61 N ANISOU 2500 NH2 ARG B 55 1252 1484 535 305 -456 -151 N ATOM 2501 N PRO B 56 87.393 -1.947 2.076 1.00 8.49 N ANISOU 2501 N PRO B 56 1463 1351 412 261 -99 -149 N ATOM 2502 CA PRO B 56 87.641 -1.515 3.441 1.00 9.47 C ANISOU 2502 CA PRO B 56 1690 1490 419 -144 -334 55 C ATOM 2503 C PRO B 56 88.710 -0.440 3.525 1.00 7.57 C ANISOU 2503 C PRO B 56 1368 1209 299 133 -130 166 C ATOM 2504 O PRO B 56 89.612 -0.353 2.655 1.00 9.50 O ANISOU 2504 O PRO B 56 1284 1821 505 265 137 -400 O ATOM 2505 CB PRO B 56 88.140 -2.803 4.130 1.00 10.24 C ANISOU 2505 CB PRO B 56 2054 1297 538 -75 173 42 C ATOM 2506 CG PRO B 56 88.833 -3.531 3.014 1.00 10.75 C ANISOU 2506 CG PRO B 56 1948 1516 622 549 -364 -157 C ATOM 2507 CD PRO B 56 88.004 -3.259 1.785 1.00 10.02 C ANISOU 2507 CD PRO B 56 1996 1346 464 356 -246 -130 C ATOM 2508 N THR B 57 88.575 0.395 4.563 1.00 8.45 N ANISOU 2508 N THR B 57 1422 1507 281 109 -6 24 N ATOM 2509 CA THR B 57 89.599 1.401 4.817 1.00 9.03 C ANISOU 2509 CA THR B 57 1239 1506 686 194 -163 -49 C ATOM 2510 C THR B 57 90.718 0.791 5.652 1.00 8.54 C ANISOU 2510 C THR B 57 1395 1407 442 171 -103 -23 C ATOM 2511 O THR B 57 90.488 -0.147 6.405 1.00 9.25 O ANISOU 2511 O THR B 57 1537 1678 300 107 -162 151 O ATOM 2512 CB THR B 57 89.067 2.654 5.510 1.00 8.93 C ANISOU 2512 CB THR B 57 1574 1221 599 282 -3 329 C ATOM 2513 OG1 THR B 57 88.508 2.187 6.753 1.00 9.27 O ANISOU 2513 OG1 THR B 57 1515 1708 300 -57 -178 107 O ATOM 2514 CG2 THR B 57 87.988 3.331 4.694 1.00 9.26 C ANISOU 2514 CG2 THR B 57 1124 1662 733 497 125 33 C ATOM 2515 N ALA B 58 91.923 1.308 5.472 1.00 9.39 N ANISOU 2515 N ALA B 58 1261 1899 408 150 -253 -267 N ATOM 2516 CA ALA B 58 93.065 0.805 6.225 1.00 9.46 C ANISOU 2516 CA ALA B 58 1221 2069 305 -2 -232 25 C ATOM 2517 C ALA B 58 92.951 1.005 7.743 1.00 8.43 C ANISOU 2517 C ALA B 58 1429 1378 398 232 -52 -231 C ATOM 2518 O ALA B 58 92.213 1.847 8.222 1.00 8.59 O ANISOU 2518 O ALA B 58 1245 1647 373 428 -68 -59 O ATOM 2519 CB ALA B 58 94.334 1.509 5.723 1.00 11.53 C ANISOU 2519 CB ALA B 58 1327 2102 951 -80 -67 -86 C ATOM 2520 N LEU B 59 93.752 0.212 8.442 1.00 9.38 N ANISOU 2520 N LEU B 59 1459 1638 467 262 -242 -302 N ATOM 2521 CA LEU B 59 93.926 0.381 9.902 1.00 10.05 C ANISOU 2521 CA LEU B 59 1437 1871 513 17 -444 -4 C ATOM 2522 C LEU B 59 95.434 0.601 10.038 1.00 10.06 C ANISOU 2522 C LEU B 59 1382 1450 989 -38 -93 53 C ATOM 2523 O LEU B 59 96.218 -0.319 9.785 1.00 12.11 O ANISOU 2523 O LEU B 59 1128 1935 1537 73 -364 -450 O ATOM 2524 CB LEU B 59 93.446 -0.830 10.674 1.00 9.12 C ANISOU 2524 CB LEU B 59 1607 1334 523 277 -372 -281 C ATOM 2525 CG LEU B 59 93.551 -0.666 12.199 1.00 9.77 C ANISOU 2525 CG LEU B 59 1821 1448 444 297 -513 -14 C ATOM 2526 CD1 LEU B 59 92.480 0.290 12.700 1.00 10.24 C ANISOU 2526 CD1 LEU B 59 1808 1723 361 295 -292 -67 C ATOM 2527 CD2 LEU B 59 93.440 -2.026 12.857 1.00 11.69 C ANISOU 2527 CD2 LEU B 59 2362 1653 426 135 -533 210 C ATOM 2528 N THR B 60 95.848 1.811 10.367 1.00 8.82 N ANISOU 2528 N THR B 60 1076 1562 714 -185 -259 324 N ATOM 2529 CA THR B 60 97.241 2.208 10.365 1.00 8.83 C ANISOU 2529 CA THR B 60 980 1665 709 -9 -580 13 C ATOM 2530 C THR B 60 97.854 2.256 11.756 1.00 9.28 C ANISOU 2530 C THR B 60 1175 2048 304 241 -209 -165 C ATOM 2531 O THR B 60 97.330 2.948 12.636 1.00 10.55 O ANISOU 2531 O THR B 60 1099 2586 323 363 -148 -221 O ATOM 2532 CB THR B 60 97.361 3.618 9.752 1.00 10.08 C ANISOU 2532 CB THR B 60 1471 1690 670 -230 -358 -2 C ATOM 2533 OG1 THR B 60 96.716 3.628 8.463 1.00 10.86 O ANISOU 2533 OG1 THR B 60 2014 1847 265 -307 -59 160 O ATOM 2534 CG2 THR B 60 98.795 4.082 9.595 1.00 10.42 C ANISOU 2534 CG2 THR B 60 1301 2329 330 -89 -276 129 C ATOM 2535 N LYS B 61 98.954 1.542 11.941 1.00 10.20 N ANISOU 2535 N LYS B 61 1091 2172 613 171 -363 29 N ATOM 2536 CA LYS B 61 99.677 1.615 13.219 1.00 9.96 C ANISOU 2536 CA LYS B 61 1487 1846 450 -87 -232 3 C ATOM 2537 C LYS B 61 100.526 2.874 13.250 1.00 11.69 C ANISOU 2537 C LYS B 61 1422 2197 824 -343 -325 32 C ATOM 2538 O LYS B 61 101.208 3.185 12.270 1.00 14.34 O ANISOU 2538 O LYS B 61 1914 2938 597 -624 -279 -83 O ATOM 2539 CB ALYS B 61 100.531 0.373 13.419 0.80 12.07 C ANISOU 2539 CB ALYS B 61 1443 2196 948 154 -232 48 C ATOM 2540 CG ALYS B 61 101.044 0.231 14.854 0.80 15.56 C ANISOU 2540 CG ALYS B 61 1883 2806 1224 228 -554 363 C ATOM 2541 CD ALYS B 61 101.722 -1.092 15.135 0.80 19.22 C ANISOU 2541 CD ALYS B 61 2297 2744 2264 369 -217 111 C ATOM 2542 CE ALYS B 61 102.960 -1.306 14.287 0.80 22.77 C ANISOU 2542 CE ALYS B 61 2616 3373 2660 363 41 -16 C ATOM 2543 NZ ALYS B 61 103.669 -2.549 14.712 0.80 27.90 N ANISOU 2543 NZ ALYS B 61 3500 3529 3572 434 -60 202 N ATOM 2544 CB BLYS B 61 100.552 0.380 13.393 0.20 10.41 C ANISOU 2544 CB BLYS B 61 1313 1884 759 -68 -128 15 C ATOM 2545 CG BLYS B 61 101.279 0.318 14.732 0.20 9.01 C ANISOU 2545 CG BLYS B 61 1049 1582 793 174 -62 136 C ATOM 2546 CD BLYS B 61 102.189 -0.896 14.782 0.20 9.26 C ANISOU 2546 CD BLYS B 61 1069 1580 871 165 13 67 C ATOM 2547 CE BLYS B 61 102.795 -1.104 16.159 0.20 9.15 C ANISOU 2547 CE BLYS B 61 1296 1465 717 266 185 -47 C ATOM 2548 NZ BLYS B 61 103.556 -2.385 16.196 0.20 10.00 N ANISOU 2548 NZ BLYS B 61 1445 1381 972 258 166 -45 N ATOM 2549 N CYS B 62 100.552 3.604 14.343 1.00 12.01 N ANISOU 2549 N CYS B 62 1393 2019 1151 6 298 -154 N ATOM 2550 CA CYS B 62 101.297 4.811 14.542 1.00 12.96 C ANISOU 2550 CA CYS B 62 1692 2011 1222 -180 232 164 C ATOM 2551 C CYS B 62 102.465 4.684 15.517 1.00 15.96 C ANISOU 2551 C CYS B 62 1794 2702 1567 -37 -1 -56 C ATOM 2552 O CYS B 62 102.449 5.240 16.640 1.00 19.94 O ANISOU 2552 O CYS B 62 2709 3531 1338 691 570 -1 O ATOM 2553 CB CYS B 62 100.361 5.895 15.135 1.00 16.63 C ANISOU 2553 CB CYS B 62 2452 1310 2554 -447 498 -156 C ATOM 2554 SG CYS B 62 99.108 6.370 13.916 1.00 24.14 S ANISOU 2554 SG CYS B 62 1256 1913 6001 -221 -129 464 S ATOM 2555 N GLN B 63 103.482 3.962 15.117 1.00 17.18 N ANISOU 2555 N GLN B 63 2330 2671 1528 295 -199 -409 N ATOM 2556 CA GLN B 63 104.676 3.810 15.953 1.00 16.74 C ANISOU 2556 CA GLN B 63 2047 2583 1731 163 -65 -105 C ATOM 2557 C GLN B 63 105.391 5.105 16.276 1.00 14.94 C ANISOU 2557 C GLN B 63 2236 2530 911 5 60 225 C ATOM 2558 O GLN B 63 105.928 5.200 17.405 1.00 16.50 O ANISOU 2558 O GLN B 63 2546 2911 814 -62 9 423 O ATOM 2559 CB GLN B 63 105.670 2.845 15.287 1.00 21.41 C ANISOU 2559 CB GLN B 63 3065 2935 2134 661 21 -442 C ATOM 2560 CG GLN B 63 105.044 1.588 14.714 1.00 31.72 C ANISOU 2560 CG GLN B 63 4249 3637 4168 -370 -235 -325 C ATOM 2561 CD GLN B 63 106.056 0.511 14.375 1.00 36.52 C ANISOU 2561 CD GLN B 63 4707 4454 4714 185 119 -333 C ATOM 2562 OE1 GLN B 63 107.263 0.735 14.340 1.00 40.01 O ANISOU 2562 OE1 GLN B 63 4906 4978 5318 124 -28 -291 O ATOM 2563 NE2 GLN B 63 105.562 -0.698 14.125 1.00 39.80 N ANISOU 2563 NE2 GLN B 63 5239 4682 5201 12 69 -233 N ATOM 2564 N ASN B 64 105.512 6.082 15.352 1.00 12.35 N ANISOU 2564 N ASN B 64 1498 2511 684 -212 -153 149 N ATOM 2565 CA ASN B 64 106.269 7.274 15.746 1.00 10.48 C ANISOU 2565 CA ASN B 64 1535 2059 390 -75 231 410 C ATOM 2566 C ASN B 64 105.652 8.017 16.921 1.00 10.64 C ANISOU 2566 C ASN B 64 1385 2254 402 129 -100 207 C ATOM 2567 O ASN B 64 106.346 8.494 17.834 1.00 14.79 O ANISOU 2567 O ASN B 64 1526 3123 971 51 -426 -168 O ATOM 2568 CB ASN B 64 106.412 8.246 14.571 1.00 12.27 C ANISOU 2568 CB ASN B 64 1827 2047 786 146 370 661 C ATOM 2569 CG ASN B 64 107.287 7.675 13.483 1.00 13.17 C ANISOU 2569 CG ASN B 64 1913 2330 760 361 198 543 C ATOM 2570 OD1 ASN B 64 108.142 6.819 13.656 1.00 15.31 O ANISOU 2570 OD1 ASN B 64 2245 2678 893 741 513 565 O ATOM 2571 ND2 ASN B 64 107.066 8.231 12.295 1.00 12.90 N ANISOU 2571 ND2 ASN B 64 1701 2457 743 363 354 746 N ATOM 2572 N ILE B 65 104.342 8.144 16.919 1.00 11.15 N ANISOU 2572 N ILE B 65 1387 2295 554 299 59 -100 N ATOM 2573 CA ILE B 65 103.655 8.882 17.976 1.00 12.17 C ANISOU 2573 CA ILE B 65 1677 2257 691 309 333 -16 C ATOM 2574 C ILE B 65 103.768 8.213 19.342 1.00 11.62 C ANISOU 2574 C ILE B 65 1713 1888 814 -277 86 54 C ATOM 2575 O ILE B 65 103.831 8.918 20.355 1.00 14.67 O ANISOU 2575 O ILE B 65 2711 2359 502 -376 136 126 O ATOM 2576 CB ILE B 65 102.173 9.074 17.613 1.00 14.12 C ANISOU 2576 CB ILE B 65 1803 2523 1039 443 241 -212 C ATOM 2577 CG1AILE B 65 102.016 10.286 16.702 0.50 14.57 C ANISOU 2577 CG1AILE B 65 1848 2423 1265 162 234 -173 C ATOM 2578 CG2AILE B 65 101.363 9.250 18.903 0.50 11.68 C ANISOU 2578 CG2AILE B 65 1426 2018 994 141 184 -118 C ATOM 2579 CD1AILE B 65 100.577 10.563 16.341 0.50 16.13 C ANISOU 2579 CD1AILE B 65 2082 2435 1611 243 -174 59 C ATOM 2580 CG1BILE B 65 101.403 7.766 17.552 0.50 18.24 C ANISOU 2580 CG1BILE B 65 2527 2699 1706 124 93 -58 C ATOM 2581 CG2BILE B 65 102.066 9.827 16.295 0.50 17.14 C ANISOU 2581 CG2BILE B 65 2716 2432 1364 251 85 -23 C ATOM 2582 CD1BILE B 65 99.989 7.933 17.036 0.50 21.70 C ANISOU 2582 CD1BILE B 65 2733 3151 2359 43 14 -101 C ATOM 2583 N THR B 66 103.811 6.897 19.384 1.00 10.40 N ANISOU 2583 N THR B 66 1632 1905 413 -50 -282 318 N ATOM 2584 CA THR B 66 103.805 6.206 20.694 1.00 10.97 C ANISOU 2584 CA THR B 66 1243 2410 516 -116 -34 534 C ATOM 2585 C THR B 66 105.189 5.820 21.184 1.00 12.04 C ANISOU 2585 C THR B 66 1169 2850 557 -23 -26 321 C ATOM 2586 O THR B 66 105.328 5.174 22.228 1.00 12.53 O ANISOU 2586 O THR B 66 1473 2859 431 -123 77 301 O ATOM 2587 CB THR B 66 102.945 4.934 20.587 1.00 11.43 C ANISOU 2587 CB THR B 66 1300 2438 604 -79 -102 37 C ATOM 2588 OG1 THR B 66 103.500 4.075 19.571 1.00 13.81 O ANISOU 2588 OG1 THR B 66 1430 2984 833 -79 126 -153 O ATOM 2589 CG2 THR B 66 101.489 5.271 20.264 1.00 10.75 C ANISOU 2589 CG2 THR B 66 974 2247 862 -419 127 -268 C ATOM 2590 N ALA B 67 106.235 6.178 20.431 1.00 13.70 N ANISOU 2590 N ALA B 67 1099 3397 709 -260 -144 496 N ATOM 2591 CA ALA B 67 107.585 5.791 20.788 1.00 14.56 C ANISOU 2591 CA ALA B 67 1151 3492 888 -256 -236 662 C ATOM 2592 C ALA B 67 107.933 6.122 22.234 1.00 13.65 C ANISOU 2592 C ALA B 67 1163 2895 1128 -220 -222 250 C ATOM 2593 O ALA B 67 107.634 7.198 22.704 1.00 16.26 O ANISOU 2593 O ALA B 67 1863 2796 1517 -379 -371 181 O ATOM 2594 CB ALA B 67 108.564 6.510 19.858 1.00 16.69 C ANISOU 2594 CB ALA B 67 639 4050 1652 -476 -113 614 C ATOM 2595 N GLY B 68 108.508 5.153 22.927 1.00 15.95 N ANISOU 2595 N GLY B 68 1446 3556 1059 -160 -345 617 N ATOM 2596 CA GLY B 68 108.931 5.382 24.315 1.00 15.54 C ANISOU 2596 CA GLY B 68 1122 3739 1042 -241 -369 576 C ATOM 2597 C GLY B 68 107.848 5.131 25.345 1.00 14.49 C ANISOU 2597 C GLY B 68 1433 3327 746 -339 -318 348 C ATOM 2598 O GLY B 68 108.070 5.292 26.565 1.00 20.52 O ANISOU 2598 O GLY B 68 2058 4877 860 -539 -588 197 O ATOM 2599 N THR B 69 106.685 4.712 24.927 1.00 12.36 N ANISOU 2599 N THR B 69 1324 2824 547 -246 -101 47 N ATOM 2600 CA THR B 69 105.564 4.405 25.817 1.00 11.38 C ANISOU 2600 CA THR B 69 1469 2308 547 -264 -125 231 C ATOM 2601 C THR B 69 105.095 2.979 25.601 1.00 10.47 C ANISOU 2601 C THR B 69 1238 2161 579 47 -205 5 C ATOM 2602 O THR B 69 105.563 2.281 24.692 1.00 13.44 O ANISOU 2602 O THR B 69 1686 2787 633 222 -8 -133 O ATOM 2603 CB THR B 69 104.354 5.339 25.620 1.00 11.38 C ANISOU 2603 CB THR B 69 1474 2284 566 -277 -204 -24 C ATOM 2604 OG1 THR B 69 103.615 4.883 24.474 1.00 10.27 O ANISOU 2604 OG1 THR B 69 929 2583 391 -146 -6 -75 O ATOM 2605 CG2 THR B 69 104.744 6.778 25.440 1.00 10.94 C ANISOU 2605 CG2 THR B 69 1056 2375 726 -414 -300 49 C ATOM 2606 N ARG B 70 104.179 2.521 26.438 1.00 10.02 N ANISOU 2606 N ARG B 70 1640 1796 371 45 -105 17 N ATOM 2607 CA ARG B 70 103.613 1.184 26.307 1.00 10.04 C ANISOU 2607 CA ARG B 70 1575 1949 289 -129 -32 1 C ATOM 2608 C ARG B 70 102.246 1.224 25.635 1.00 10.21 C ANISOU 2608 C ARG B 70 1558 1899 425 106 -16 94 C ATOM 2609 O ARG B 70 101.492 0.253 25.702 1.00 11.33 O ANISOU 2609 O ARG B 70 1608 2136 562 -8 -397 311 O ATOM 2610 CB ARG B 70 103.579 0.486 27.678 1.00 11.98 C ANISOU 2610 CB ARG B 70 1607 2541 404 131 -398 256 C ATOM 2611 CG ARG B 70 104.993 0.259 28.225 1.00 14.71 C ANISOU 2611 CG ARG B 70 1599 2929 1060 137 -544 233 C ATOM 2612 CD ARG B 70 104.997 -0.755 29.366 1.00 20.07 C ANISOU 2612 CD ARG B 70 3099 2734 1791 274 -164 464 C ATOM 2613 NE ARG B 70 104.746 -2.110 28.882 1.00 26.37 N ANISOU 2613 NE ARG B 70 3638 3202 3180 -51 -285 -181 N ATOM 2614 CZ ARG B 70 104.510 -3.186 29.623 1.00 30.93 C ANISOU 2614 CZ ARG B 70 4393 3712 3647 -47 -80 199 C ATOM 2615 NH1 ARG B 70 104.476 -3.100 30.946 1.00 31.90 N ANISOU 2615 NH1 ARG B 70 4438 4097 3584 37 -69 130 N ATOM 2616 NH2 ARG B 70 104.287 -4.377 29.073 1.00 32.34 N ANISOU 2616 NH2 ARG B 70 4422 3683 4184 28 -133 67 N ATOM 2617 N THR B 71 101.950 2.339 24.955 1.00 9.09 N ANISOU 2617 N THR B 71 1158 1955 342 -17 -269 50 N ATOM 2618 CA THR B 71 100.740 2.432 24.145 1.00 9.41 C ANISOU 2618 CA THR B 71 1303 1881 390 380 -313 -16 C ATOM 2619 C THR B 71 100.999 1.968 22.700 1.00 9.43 C ANISOU 2619 C THR B 71 1307 1798 476 -46 -29 -30 C ATOM 2620 O THR B 71 102.028 2.369 22.148 1.00 10.27 O ANISOU 2620 O THR B 71 1160 2420 323 -132 -259 22 O ATOM 2621 CB THR B 71 100.216 3.870 24.074 1.00 8.87 C ANISOU 2621 CB THR B 71 1019 1969 384 420 -97 -100 C ATOM 2622 OG1 THR B 71 99.737 4.261 25.381 1.00 10.47 O ANISOU 2622 OG1 THR B 71 1415 2235 327 102 90 -166 O ATOM 2623 CG2 THR B 71 99.037 4.022 23.130 1.00 8.57 C ANISOU 2623 CG2 THR B 71 1183 1747 325 343 -184 65 C ATOM 2624 N THR B 72 100.089 1.175 22.178 1.00 9.29 N ANISOU 2624 N THR B 72 1498 1700 330 18 -15 -139 N ATOM 2625 CA THR B 72 100.127 0.829 20.733 1.00 9.24 C ANISOU 2625 CA THR B 72 1308 1862 342 166 -313 -60 C ATOM 2626 C THR B 72 98.858 1.481 20.189 1.00 8.46 C ANISOU 2626 C THR B 72 968 1676 570 -25 -66 -81 C ATOM 2627 O THR B 72 97.786 1.275 20.745 1.00 10.18 O ANISOU 2627 O THR B 72 1088 2473 308 -97 -76 215 O ATOM 2628 CB THR B 72 100.089 -0.676 20.498 1.00 10.54 C ANISOU 2628 CB THR B 72 1354 1903 746 484 -226 -243 C ATOM 2629 OG1 THR B 72 101.236 -1.285 21.111 1.00 12.98 O ANISOU 2629 OG1 THR B 72 1638 2117 1178 714 -356 -48 O ATOM 2630 CG2 THR B 72 100.087 -1.031 19.019 1.00 12.04 C ANISOU 2630 CG2 THR B 72 1929 2045 601 360 -165 55 C ATOM 2631 N LEU B 73 99.023 2.330 19.184 1.00 9.31 N ANISOU 2631 N LEU B 73 1508 1686 345 18 -342 -75 N ATOM 2632 CA LEU B 73 97.913 3.094 18.650 1.00 9.55 C ANISOU 2632 CA LEU B 73 1640 1730 257 246 -96 21 C ATOM 2633 C LEU B 73 97.683 2.842 17.155 1.00 9.60 C ANISOU 2633 C LEU B 73 982 2368 299 148 -3 103 C ATOM 2634 O LEU B 73 98.604 2.932 16.370 1.00 10.71 O ANISOU 2634 O LEU B 73 1016 2645 410 -98 84 -54 O ATOM 2635 CB LEU B 73 98.221 4.595 18.806 1.00 10.32 C ANISOU 2635 CB LEU B 73 1705 1663 551 311 -202 197 C ATOM 2636 CG LEU B 73 97.248 5.601 18.190 1.00 10.86 C ANISOU 2636 CG LEU B 73 1820 1378 928 263 -42 427 C ATOM 2637 CD1 LEU B 73 95.876 5.463 18.828 1.00 11.00 C ANISOU 2637 CD1 LEU B 73 1737 1886 558 562 -85 -73 C ATOM 2638 CD2 LEU B 73 97.766 7.020 18.361 1.00 13.35 C ANISOU 2638 CD2 LEU B 73 2209 1782 1081 -112 -24 -86 C ATOM 2639 N TYR B 74 96.447 2.488 16.848 1.00 9.56 N ANISOU 2639 N TYR B 74 1091 2197 344 173 -277 27 N ATOM 2640 CA TYR B 74 96.047 2.334 15.442 1.00 8.88 C ANISOU 2640 CA TYR B 74 1386 1736 253 -175 -69 17 C ATOM 2641 C TYR B 74 94.993 3.395 15.128 1.00 8.54 C ANISOU 2641 C TYR B 74 898 2048 297 -168 129 16 C ATOM 2642 O TYR B 74 94.210 3.780 15.989 1.00 8.66 O ANISOU 2642 O TYR B 74 975 1957 359 315 44 202 O ATOM 2643 CB TYR B 74 95.418 0.970 15.188 1.00 8.24 C ANISOU 2643 CB TYR B 74 1203 1590 339 116 -117 -331 C ATOM 2644 CG TYR B 74 96.375 -0.189 15.135 1.00 9.59 C ANISOU 2644 CG TYR B 74 1452 1726 467 315 -295 -228 C ATOM 2645 CD1 TYR B 74 96.823 -0.823 16.295 1.00 10.86 C ANISOU 2645 CD1 TYR B 74 1608 1686 832 255 -320 72 C ATOM 2646 CD2 TYR B 74 96.852 -0.678 13.923 1.00 10.67 C ANISOU 2646 CD2 TYR B 74 1271 2044 737 527 69 -178 C ATOM 2647 CE1 TYR B 74 97.682 -1.897 16.238 1.00 11.10 C ANISOU 2647 CE1 TYR B 74 1877 1719 620 395 -305 -130 C ATOM 2648 CE2 TYR B 74 97.720 -1.742 13.868 1.00 10.50 C ANISOU 2648 CE2 TYR B 74 1637 1512 842 349 -152 -60 C ATOM 2649 CZ TYR B 74 98.142 -2.365 15.022 1.00 10.68 C ANISOU 2649 CZ TYR B 74 1690 1597 771 332 -135 -134 C ATOM 2650 OH TYR B 74 98.994 -3.433 14.941 1.00 12.90 O ANISOU 2650 OH TYR B 74 1916 1624 1363 421 -58 -252 O ATOM 2651 N LEU B 75 94.996 3.810 13.848 1.00 9.00 N ANISOU 2651 N LEU B 75 951 2060 409 136 -170 384 N ATOM 2652 CA LEU B 75 94.016 4.752 13.341 1.00 7.90 C ANISOU 2652 CA LEU B 75 807 1629 565 -72 -238 57 C ATOM 2653 C LEU B 75 93.133 4.050 12.311 1.00 7.83 C ANISOU 2653 C LEU B 75 908 1590 476 157 -237 -134 C ATOM 2654 O LEU B 75 93.699 3.523 11.340 1.00 9.19 O ANISOU 2654 O LEU B 75 1041 1951 499 225 -134 -173 O ATOM 2655 CB LEU B 75 94.645 5.961 12.653 1.00 9.48 C ANISOU 2655 CB LEU B 75 1698 1353 552 -208 -171 -106 C ATOM 2656 CG LEU B 75 95.689 6.711 13.456 1.00 10.88 C ANISOU 2656 CG LEU B 75 2110 1496 529 -740 37 -44 C ATOM 2657 CD1 LEU B 75 96.250 7.871 12.624 1.00 12.40 C ANISOU 2657 CD1 LEU B 75 1744 1652 1316 -791 -110 392 C ATOM 2658 CD2 LEU B 75 95.139 7.230 14.775 1.00 12.03 C ANISOU 2658 CD2 LEU B 75 2097 1415 1058 -268 561 24 C ATOM 2659 N LYS B 76 91.828 4.079 12.505 1.00 7.88 N ANISOU 2659 N LYS B 76 863 1612 518 -115 -379 -145 N ATOM 2660 CA LYS B 76 90.918 3.513 11.480 1.00 8.29 C ANISOU 2660 CA LYS B 76 1251 1480 418 -356 -252 -252 C ATOM 2661 C LYS B 76 90.768 4.654 10.475 1.00 8.62 C ANISOU 2661 C LYS B 76 1443 1270 563 -145 -195 -317 C ATOM 2662 O LYS B 76 90.307 5.730 10.808 1.00 8.66 O ANISOU 2662 O LYS B 76 1650 1351 290 129 -31 206 O ATOM 2663 CB LYS B 76 89.615 3.107 12.126 1.00 8.82 C ANISOU 2663 CB LYS B 76 960 1516 874 -388 -512 44 C ATOM 2664 CG LYS B 76 88.619 2.561 11.116 1.00 7.73 C ANISOU 2664 CG LYS B 76 1062 1329 545 -271 -308 -259 C ATOM 2665 CD LYS B 76 89.140 1.381 10.319 1.00 8.71 C ANISOU 2665 CD LYS B 76 1524 1367 418 -233 -271 -233 C ATOM 2666 CE LYS B 76 88.052 0.732 9.477 1.00 8.39 C ANISOU 2666 CE LYS B 76 1255 1519 416 -197 -165 -240 C ATOM 2667 NZ LYS B 76 88.619 -0.220 8.491 1.00 9.35 N ANISOU 2667 NZ LYS B 76 1555 1720 276 385 -188 -43 N ATOM 2668 N ARG B 77 91.165 4.362 9.209 1.00 8.11 N ANISOU 2668 N ARG B 77 1423 1313 347 102 -339 -20 N ATOM 2669 CA ARG B 77 91.311 5.405 8.206 1.00 8.37 C ANISOU 2669 CA ARG B 77 1075 1415 691 325 -153 193 C ATOM 2670 C ARG B 77 90.099 5.825 7.418 1.00 9.39 C ANISOU 2670 C ARG B 77 1016 2067 484 93 -297 -126 C ATOM 2671 O ARG B 77 90.051 5.694 6.188 1.00 9.09 O ANISOU 2671 O ARG B 77 1338 1809 307 27 -93 -202 O ATOM 2672 CB ARG B 77 92.488 5.021 7.260 1.00 8.64 C ANISOU 2672 CB ARG B 77 1350 1566 368 211 -200 -218 C ATOM 2673 CG ARG B 77 93.803 4.718 8.002 1.00 8.88 C ANISOU 2673 CG ARG B 77 1385 1550 440 230 -220 -40 C ATOM 2674 CD ARG B 77 94.406 5.962 8.689 1.00 9.45 C ANISOU 2674 CD ARG B 77 1507 1582 503 -124 24 36 C ATOM 2675 NE ARG B 77 94.635 7.013 7.697 1.00 8.77 N ANISOU 2675 NE ARG B 77 1459 1485 389 -84 -62 -59 N ATOM 2676 CZ ARG B 77 95.651 7.001 6.828 1.00 8.91 C ANISOU 2676 CZ ARG B 77 1065 1659 661 -193 -170 165 C ATOM 2677 NH1 ARG B 77 96.590 6.070 6.854 1.00 9.75 N ANISOU 2677 NH1 ARG B 77 1237 2031 437 11 -414 0 N ATOM 2678 NH2 ARG B 77 95.680 7.991 5.917 1.00 10.26 N ANISOU 2678 NH2 ARG B 77 1585 1653 662 -354 -431 136 N ATOM 2679 N GLU B 78 89.088 6.378 8.091 1.00 8.72 N ANISOU 2679 N GLU B 78 1180 1823 310 163 -157 66 N ATOM 2680 CA GLU B 78 87.918 6.858 7.360 1.00 9.29 C ANISOU 2680 CA GLU B 78 1118 1905 505 97 -137 220 C ATOM 2681 C GLU B 78 88.297 8.097 6.555 1.00 8.92 C ANISOU 2681 C GLU B 78 1174 1822 392 -90 -211 48 C ATOM 2682 O GLU B 78 87.546 8.498 5.652 1.00 10.63 O ANISOU 2682 O GLU B 78 1721 1883 434 290 -281 265 O ATOM 2683 CB GLU B 78 86.730 7.086 8.299 1.00 9.90 C ANISOU 2683 CB GLU B 78 1176 1766 820 261 -37 120 C ATOM 2684 CG GLU B 78 86.288 5.799 9.005 1.00 8.93 C ANISOU 2684 CG GLU B 78 1483 1437 473 48 -45 -357 C ATOM 2685 CD GLU B 78 85.861 4.728 8.025 1.00 9.00 C ANISOU 2685 CD GLU B 78 1455 1456 508 179 -299 -278 C ATOM 2686 OE1 GLU B 78 84.868 4.959 7.289 1.00 10.07 O ANISOU 2686 OE1 GLU B 78 1276 1999 550 -31 -267 -164 O ATOM 2687 OE2 GLU B 78 86.494 3.657 7.969 1.00 9.56 O ANISOU 2687 OE2 GLU B 78 1510 1565 558 267 -192 -204 O ATOM 2688 N ASP B 79 89.444 8.678 6.824 1.00 8.66 N ANISOU 2688 N ASP B 79 1239 1763 290 -223 -141 206 N ATOM 2689 CA ASP B 79 89.946 9.808 6.047 1.00 9.37 C ANISOU 2689 CA ASP B 79 1479 1617 465 -125 -49 230 C ATOM 2690 C ASP B 79 90.238 9.373 4.610 1.00 9.43 C ANISOU 2690 C ASP B 79 1620 1259 706 82 33 -3 C ATOM 2691 O ASP B 79 90.319 10.243 3.730 1.00 10.77 O ANISOU 2691 O ASP B 79 1963 1549 579 -138 82 70 O ATOM 2692 CB ASP B 79 91.213 10.402 6.667 1.00 9.84 C ANISOU 2692 CB ASP B 79 1133 1971 634 113 75 133 C ATOM 2693 CG ASP B 79 92.358 9.409 6.759 1.00 8.73 C ANISOU 2693 CG ASP B 79 1003 1942 374 3 -197 168 C ATOM 2694 OD1 ASP B 79 92.198 8.361 7.417 1.00 10.36 O ANISOU 2694 OD1 ASP B 79 1436 1615 885 -57 -198 98 O ATOM 2695 OD2 ASP B 79 93.441 9.668 6.177 1.00 10.81 O ANISOU 2695 OD2 ASP B 79 1053 2365 689 -125 -120 433 O ATOM 2696 N LEU B 80 90.431 8.083 4.389 1.00 8.79 N ANISOU 2696 N LEU B 80 1606 1310 423 18 165 -182 N ATOM 2697 CA LEU B 80 90.683 7.576 3.031 1.00 8.90 C ANISOU 2697 CA LEU B 80 1494 1512 377 -263 -41 -341 C ATOM 2698 C LEU B 80 89.399 7.198 2.319 1.00 9.89 C ANISOU 2698 C LEU B 80 1320 2018 420 -100 -26 -189 C ATOM 2699 O LEU B 80 89.484 6.774 1.154 1.00 11.26 O ANISOU 2699 O LEU B 80 1296 2596 387 -322 -34 -544 O ATOM 2700 CB LEU B 80 91.622 6.379 3.094 1.00 10.10 C ANISOU 2700 CB LEU B 80 1750 1426 661 -217 72 -16 C ATOM 2701 CG LEU B 80 93.028 6.690 3.642 1.00 9.84 C ANISOU 2701 CG LEU B 80 1551 1197 991 9 70 298 C ATOM 2702 CD1 LEU B 80 93.795 5.390 3.750 1.00 10.91 C ANISOU 2702 CD1 LEU B 80 1434 1617 1093 329 -172 84 C ATOM 2703 CD2 LEU B 80 93.676 7.765 2.784 1.00 10.33 C ANISOU 2703 CD2 LEU B 80 1050 1649 1227 -112 -13 498 C ATOM 2704 N LEU B 81 88.242 7.316 2.930 1.00 10.01 N ANISOU 2704 N LEU B 81 1236 2019 549 -86 -26 -34 N ATOM 2705 CA LEU B 81 86.975 6.999 2.259 1.00 9.30 C ANISOU 2705 CA LEU B 81 1178 1747 608 111 -60 -51 C ATOM 2706 C LEU B 81 86.710 8.062 1.203 1.00 10.48 C ANISOU 2706 C LEU B 81 1750 1547 685 -13 -183 -120 C ATOM 2707 O LEU B 81 87.053 9.219 1.400 1.00 10.88 O ANISOU 2707 O LEU B 81 2034 1493 608 115 -461 -44 O ATOM 2708 CB LEU B 81 85.843 6.948 3.297 1.00 10.13 C ANISOU 2708 CB LEU B 81 1343 1905 601 -29 -13 -108 C ATOM 2709 CG LEU B 81 84.548 6.272 2.868 1.00 9.94 C ANISOU 2709 CG LEU B 81 1227 1825 726 111 73 -137 C ATOM 2710 CD1 LEU B 81 84.739 4.789 2.598 1.00 10.22 C ANISOU 2710 CD1 LEU B 81 1924 1621 341 -255 27 134 C ATOM 2711 CD2 LEU B 81 83.522 6.438 3.988 1.00 10.34 C ANISOU 2711 CD2 LEU B 81 1342 2042 544 278 26 -59 C ATOM 2712 N HIS B 82 86.023 7.675 0.121 1.00 10.51 N ANISOU 2712 N HIS B 82 1609 1828 557 123 -203 -25 N ATOM 2713 CA HIS B 82 85.652 8.679 -0.879 1.00 10.32 C ANISOU 2713 CA HIS B 82 1802 1466 654 46 -405 -224 C ATOM 2714 C HIS B 82 84.864 9.792 -0.201 1.00 9.36 C ANISOU 2714 C HIS B 82 1650 1575 332 -36 -275 -116 C ATOM 2715 O HIS B 82 83.917 9.507 0.544 1.00 10.92 O ANISOU 2715 O HIS B 82 1818 1504 825 303 178 -49 O ATOM 2716 CB HIS B 82 84.809 7.979 -1.953 1.00 9.85 C ANISOU 2716 CB HIS B 82 1535 1689 518 35 -390 -104 C ATOM 2717 CG HIS B 82 84.263 8.941 -2.958 1.00 10.33 C ANISOU 2717 CG HIS B 82 1652 1737 537 433 -135 -151 C ATOM 2718 ND1 HIS B 82 85.068 9.759 -3.715 1.00 11.74 N ANISOU 2718 ND1 HIS B 82 1864 2144 454 513 5 -55 N ATOM 2719 CD2 HIS B 82 82.979 9.179 -3.320 1.00 11.71 C ANISOU 2719 CD2 HIS B 82 1545 1978 924 307 -14 -62 C ATOM 2720 CE1 HIS B 82 84.303 10.484 -4.519 1.00 12.59 C ANISOU 2720 CE1 HIS B 82 1955 2518 309 855 135 -34 C ATOM 2721 NE2 HIS B 82 83.049 10.140 -4.302 1.00 13.05 N ANISOU 2721 NE2 HIS B 82 2024 2299 634 651 20 1 N ATOM 2722 N GLY B 83 85.242 11.034 -0.451 1.00 11.10 N ANISOU 2722 N GLY B 83 2342 1446 428 70 -232 -117 N ATOM 2723 CA GLY B 83 84.606 12.184 0.206 1.00 10.76 C ANISOU 2723 CA GLY B 83 2040 1530 520 253 -377 -31 C ATOM 2724 C GLY B 83 85.454 12.713 1.358 1.00 9.90 C ANISOU 2724 C GLY B 83 1949 1460 354 51 -39 -70 C ATOM 2725 O GLY B 83 85.293 13.873 1.742 1.00 13.13 O ANISOU 2725 O GLY B 83 2561 1500 927 21 -13 -261 O ATOM 2726 N GLY B 84 86.340 11.869 1.871 1.00 10.54 N ANISOU 2726 N GLY B 84 1798 1827 380 -17 -172 177 N ATOM 2727 CA GLY B 84 87.249 12.289 2.934 1.00 11.70 C ANISOU 2727 CA GLY B 84 1542 2386 519 -145 28 -113 C ATOM 2728 C GLY B 84 86.696 12.159 4.342 1.00 10.49 C ANISOU 2728 C GLY B 84 1486 2045 456 -266 -56 -45 C ATOM 2729 O GLY B 84 87.378 12.607 5.280 1.00 10.89 O ANISOU 2729 O GLY B 84 1352 2452 334 -532 109 -148 O ATOM 2730 N ALA B 85 85.554 11.560 4.517 1.00 10.34 N ANISOU 2730 N ALA B 85 1574 2059 297 -266 95 251 N ATOM 2731 CA ALA B 85 85.003 11.356 5.875 1.00 8.90 C ANISOU 2731 CA ALA B 85 1532 1539 310 -317 113 221 C ATOM 2732 C ALA B 85 84.076 10.149 5.867 1.00 8.49 C ANISOU 2732 C ALA B 85 1357 1527 341 -311 -203 312 C ATOM 2733 O ALA B 85 83.535 9.768 4.817 1.00 9.82 O ANISOU 2733 O ALA B 85 1458 1959 315 -92 -215 103 O ATOM 2734 CB ALA B 85 84.290 12.616 6.317 1.00 10.87 C ANISOU 2734 CB ALA B 85 2027 1783 320 13 -243 -108 C ATOM 2735 N HIS B 86 83.816 9.609 7.066 1.00 8.59 N ANISOU 2735 N HIS B 86 1220 1673 372 -171 151 330 N ATOM 2736 CA HIS B 86 82.980 8.451 7.231 1.00 8.73 C ANISOU 2736 CA HIS B 86 1448 1492 376 -182 -284 313 C ATOM 2737 C HIS B 86 81.541 8.705 6.783 1.00 7.89 C ANISOU 2737 C HIS B 86 1236 1414 348 -123 45 65 C ATOM 2738 O HIS B 86 80.835 7.715 6.603 1.00 9.09 O ANISOU 2738 O HIS B 86 1605 1567 283 -267 -67 -77 O ATOM 2739 CB HIS B 86 82.966 8.073 8.736 1.00 9.48 C ANISOU 2739 CB HIS B 86 1947 1359 296 157 119 5 C ATOM 2740 CG HIS B 86 82.174 9.085 9.517 1.00 7.56 C ANISOU 2740 CG HIS B 86 1204 1148 521 236 -493 -1 C ATOM 2741 ND1 HIS B 86 82.624 10.357 9.789 1.00 9.39 N ANISOU 2741 ND1 HIS B 86 1836 1191 542 128 -359 -52 N ATOM 2742 CD2 HIS B 86 80.925 8.987 10.038 1.00 8.76 C ANISOU 2742 CD2 HIS B 86 1191 1662 476 127 -456 -157 C ATOM 2743 CE1 HIS B 86 81.671 10.990 10.459 1.00 8.68 C ANISOU 2743 CE1 HIS B 86 1718 1165 416 103 -376 23 C ATOM 2744 NE2 HIS B 86 80.625 10.197 10.597 1.00 9.10 N ANISOU 2744 NE2 HIS B 86 1486 1518 453 192 -379 139 N ATOM 2745 N LYS B 87 81.119 9.965 6.636 1.00 8.49 N ANISOU 2745 N LYS B 87 1165 1759 300 248 51 199 N ATOM 2746 CA LYS B 87 79.731 10.244 6.300 1.00 9.02 C ANISOU 2746 CA LYS B 87 1219 1659 550 38 -249 -2 C ATOM 2747 C LYS B 87 79.252 9.529 5.029 1.00 8.85 C ANISOU 2747 C LYS B 87 1146 1725 493 -81 -49 -30 C ATOM 2748 O LYS B 87 78.077 9.185 4.897 1.00 10.15 O ANISOU 2748 O LYS B 87 1094 2305 457 32 -419 29 O ATOM 2749 CB LYS B 87 79.486 11.745 6.115 1.00 11.23 C ANISOU 2749 CB LYS B 87 1648 1670 949 443 -351 -419 C ATOM 2750 CG LYS B 87 79.703 12.571 7.391 1.00 12.54 C ANISOU 2750 CG LYS B 87 2075 1717 971 297 -406 -404 C ATOM 2751 CD LYS B 87 79.217 13.994 7.126 1.00 16.75 C ANISOU 2751 CD LYS B 87 2915 1710 1738 274 -453 -233 C ATOM 2752 CE LYS B 87 79.045 14.818 8.383 1.00 15.39 C ANISOU 2752 CE LYS B 87 2502 1401 1942 236 -422 -266 C ATOM 2753 NZ LYS B 87 80.320 14.944 9.150 1.00 16.94 N ANISOU 2753 NZ LYS B 87 2880 2431 1126 316 -505 -617 N ATOM 2754 N THR B 88 80.196 9.302 4.120 1.00 9.42 N ANISOU 2754 N THR B 88 1364 1798 416 301 -79 121 N ATOM 2755 CA THR B 88 79.836 8.634 2.868 1.00 9.83 C ANISOU 2755 CA THR B 88 1626 1406 704 132 -126 -12 C ATOM 2756 C THR B 88 79.192 7.280 3.040 1.00 8.35 C ANISOU 2756 C THR B 88 1258 1528 387 59 -245 -24 C ATOM 2757 O THR B 88 78.359 6.875 2.217 1.00 10.18 O ANISOU 2757 O THR B 88 1227 2206 435 195 -399 -82 O ATOM 2758 CB THR B 88 81.108 8.522 2.005 1.00 9.60 C ANISOU 2758 CB THR B 88 1713 1535 398 52 -107 -98 C ATOM 2759 OG1 THR B 88 81.519 9.853 1.718 1.00 10.57 O ANISOU 2759 OG1 THR B 88 1976 1670 368 66 65 55 O ATOM 2760 CG2 THR B 88 80.880 7.721 0.720 1.00 11.85 C ANISOU 2760 CG2 THR B 88 2187 1840 476 49 -269 -220 C ATOM 2761 N ASN B 89 79.577 6.519 4.070 1.00 8.06 N ANISOU 2761 N ASN B 89 1342 1407 315 71 -82 29 N ATOM 2762 CA ASN B 89 79.014 5.185 4.211 1.00 9.15 C ANISOU 2762 CA ASN B 89 1354 1501 621 39 -82 63 C ATOM 2763 C ASN B 89 77.491 5.211 4.258 1.00 8.93 C ANISOU 2763 C ASN B 89 1348 1423 621 -63 -14 11 C ATOM 2764 O ASN B 89 76.795 4.498 3.543 1.00 10.54 O ANISOU 2764 O ASN B 89 1609 2017 378 -66 -418 43 O ATOM 2765 CB ASN B 89 79.510 4.469 5.469 1.00 9.63 C ANISOU 2765 CB ASN B 89 1117 1695 848 363 -320 22 C ATOM 2766 CG ASN B 89 80.993 4.256 5.493 1.00 9.23 C ANISOU 2766 CG ASN B 89 1189 1878 441 413 -423 -140 C ATOM 2767 OD1 ASN B 89 81.597 3.778 4.522 1.00 10.11 O ANISOU 2767 OD1 ASN B 89 1277 2263 301 326 -228 -18 O ATOM 2768 ND2 ASN B 89 81.637 4.612 6.625 1.00 9.73 N ANISOU 2768 ND2 ASN B 89 1298 1876 524 163 -538 -81 N ATOM 2769 N GLN B 90 76.985 6.039 5.184 1.00 9.13 N ANISOU 2769 N GLN B 90 1155 1856 457 115 -268 -177 N ATOM 2770 CA GLN B 90 75.556 5.986 5.484 1.00 9.06 C ANISOU 2770 CA GLN B 90 1219 1692 533 98 -104 22 C ATOM 2771 C GLN B 90 74.728 6.711 4.433 1.00 9.93 C ANISOU 2771 C GLN B 90 1303 2027 441 -97 -106 309 C ATOM 2772 O GLN B 90 73.572 6.302 4.268 1.00 11.27 O ANISOU 2772 O GLN B 90 1332 2493 459 -18 -367 236 O ATOM 2773 CB GLN B 90 75.307 6.429 6.918 1.00 9.02 C ANISOU 2773 CB GLN B 90 1177 1558 692 -192 -195 -255 C ATOM 2774 CG GLN B 90 75.417 7.927 7.169 1.00 9.20 C ANISOU 2774 CG GLN B 90 1182 1407 906 305 -320 -135 C ATOM 2775 CD GLN B 90 74.020 8.550 7.168 1.00 8.86 C ANISOU 2775 CD GLN B 90 1152 1600 616 258 -308 -116 C ATOM 2776 OE1 GLN B 90 73.016 7.842 7.130 1.00 11.96 O ANISOU 2776 OE1 GLN B 90 1076 2179 1289 116 -324 -438 O ATOM 2777 NE2 GLN B 90 73.961 9.871 7.252 1.00 11.09 N ANISOU 2777 NE2 GLN B 90 1584 1580 1051 556 -367 219 N ATOM 2778 N VAL B 91 75.284 7.728 3.772 1.00 9.63 N ANISOU 2778 N VAL B 91 1799 1180 679 191 -332 147 N ATOM 2779 CA VAL B 91 74.465 8.367 2.733 1.00 10.72 C ANISOU 2779 CA VAL B 91 1716 1787 570 35 -388 221 C ATOM 2780 C VAL B 91 74.250 7.385 1.588 1.00 10.17 C ANISOU 2780 C VAL B 91 1423 1699 742 337 -103 84 C ATOM 2781 O VAL B 91 73.187 7.454 0.961 1.00 11.35 O ANISOU 2781 O VAL B 91 1460 2126 727 301 -275 -144 O ATOM 2782 CB VAL B 91 75.062 9.678 2.232 1.00 11.03 C ANISOU 2782 CB VAL B 91 1900 1307 986 172 -293 -190 C ATOM 2783 CG1 VAL B 91 75.010 10.751 3.311 1.00 10.02 C ANISOU 2783 CG1 VAL B 91 2030 1091 688 241 0 20 C ATOM 2784 CG2 VAL B 91 76.473 9.481 1.690 1.00 13.86 C ANISOU 2784 CG2 VAL B 91 2015 2296 956 187 -121 140 C ATOM 2785 N LEU B 92 75.215 6.513 1.310 1.00 9.89 N ANISOU 2785 N LEU B 92 1616 1669 471 361 -60 -98 N ATOM 2786 CA LEU B 92 74.971 5.533 0.240 1.00 10.61 C ANISOU 2786 CA LEU B 92 1646 1499 885 296 -219 -186 C ATOM 2787 C LEU B 92 73.810 4.646 0.631 1.00 10.72 C ANISOU 2787 C LEU B 92 1759 1796 518 37 -373 -175 C ATOM 2788 O LEU B 92 72.933 4.343 -0.183 1.00 11.63 O ANISOU 2788 O LEU B 92 1535 2079 806 54 -455 -389 O ATOM 2789 CB LEU B 92 76.225 4.752 -0.129 1.00 11.22 C ANISOU 2789 CB LEU B 92 1671 2002 589 346 -143 -278 C ATOM 2790 CG LEU B 92 77.291 5.649 -0.771 1.00 10.64 C ANISOU 2790 CG LEU B 92 1538 1973 533 411 -418 62 C ATOM 2791 CD1 LEU B 92 78.650 4.962 -0.756 1.00 12.19 C ANISOU 2791 CD1 LEU B 92 1485 2665 483 560 -104 -294 C ATOM 2792 CD2 LEU B 92 76.894 6.037 -2.191 1.00 11.42 C ANISOU 2792 CD2 LEU B 92 1887 2133 318 316 -110 86 C ATOM 2793 N GLY B 93 73.794 4.169 1.877 1.00 9.97 N ANISOU 2793 N GLY B 93 1685 1583 521 -56 -246 -207 N ATOM 2794 CA GLY B 93 72.727 3.301 2.340 1.00 10.98 C ANISOU 2794 CA GLY B 93 1710 1652 809 95 -21 -21 C ATOM 2795 C GLY B 93 71.380 4.007 2.324 1.00 9.77 C ANISOU 2795 C GLY B 93 1346 1635 730 -181 104 -325 C ATOM 2796 O GLY B 93 70.371 3.440 1.883 1.00 10.83 O ANISOU 2796 O GLY B 93 1552 2114 448 -16 -327 -444 O ATOM 2797 N GLN B 94 71.357 5.245 2.841 1.00 9.77 N ANISOU 2797 N GLN B 94 1291 1640 782 355 -401 -329 N ATOM 2798 CA GLN B 94 70.098 5.988 2.863 1.00 9.68 C ANISOU 2798 CA GLN B 94 1331 1695 651 403 -122 -321 C ATOM 2799 C GLN B 94 69.618 6.274 1.433 1.00 9.78 C ANISOU 2799 C GLN B 94 1133 2028 555 129 -72 -390 C ATOM 2800 O GLN B 94 68.399 6.299 1.205 1.00 11.28 O ANISOU 2800 O GLN B 94 1232 2502 553 275 -277 -283 O ATOM 2801 CB GLN B 94 70.170 7.285 3.650 1.00 9.65 C ANISOU 2801 CB GLN B 94 1392 1608 667 9 -203 -232 C ATOM 2802 CG GLN B 94 70.181 7.112 5.175 1.00 10.72 C ANISOU 2802 CG GLN B 94 1723 1639 709 320 -470 -360 C ATOM 2803 CD GLN B 94 69.696 8.391 5.832 1.00 10.13 C ANISOU 2803 CD GLN B 94 1585 1806 457 568 -208 -171 C ATOM 2804 OE1 GLN B 94 68.596 8.868 5.573 1.00 11.19 O ANISOU 2804 OE1 GLN B 94 1277 2291 686 395 -330 -776 O ATOM 2805 NE2 GLN B 94 70.520 8.938 6.715 1.00 11.92 N ANISOU 2805 NE2 GLN B 94 1866 2066 597 522 -446 -216 N ATOM 2806 N ALA B 95 70.529 6.540 0.493 1.00 10.45 N ANISOU 2806 N ALA B 95 1579 2105 286 -20 -132 -83 N ATOM 2807 CA ALA B 95 70.078 6.781 -0.886 1.00 11.71 C ANISOU 2807 CA ALA B 95 1172 2541 738 18 -581 -57 C ATOM 2808 C ALA B 95 69.453 5.519 -1.465 1.00 11.24 C ANISOU 2808 C ALA B 95 1333 1948 989 251 -294 74 C ATOM 2809 O ALA B 95 68.424 5.594 -2.159 1.00 12.36 O ANISOU 2809 O ALA B 95 1761 2419 517 -133 -593 -223 O ATOM 2810 CB ALA B 95 71.261 7.266 -1.691 1.00 11.89 C ANISOU 2810 CB ALA B 95 2093 1982 444 13 3 -23 C ATOM 2811 N LEU B 96 70.012 4.347 -1.174 1.00 11.07 N ANISOU 2811 N LEU B 96 1672 1672 860 46 -475 -3 N ATOM 2812 CA LEU B 96 69.408 3.092 -1.596 1.00 11.38 C ANISOU 2812 CA LEU B 96 1671 1875 777 97 -671 -328 C ATOM 2813 C LEU B 96 68.060 2.912 -0.908 1.00 12.91 C ANISOU 2813 C LEU B 96 1795 2226 883 -116 -530 -623 C ATOM 2814 O LEU B 96 67.146 2.383 -1.576 1.00 13.94 O ANISOU 2814 O LEU B 96 1912 2141 1245 -217 -783 -658 O ATOM 2815 CB LEU B 96 70.315 1.898 -1.364 1.00 11.27 C ANISOU 2815 CB LEU B 96 1706 1737 841 78 -427 -332 C ATOM 2816 CG LEU B 96 71.602 1.859 -2.190 1.00 11.68 C ANISOU 2816 CG LEU B 96 1886 1997 554 235 -410 -505 C ATOM 2817 CD1 LEU B 96 72.469 0.696 -1.730 1.00 15.10 C ANISOU 2817 CD1 LEU B 96 2287 2001 1448 328 -351 -208 C ATOM 2818 CD2 LEU B 96 71.303 1.759 -3.674 1.00 14.39 C ANISOU 2818 CD2 LEU B 96 2472 2332 663 116 -705 -355 C ATOM 2819 N LEU B 97 67.871 3.277 0.364 1.00 12.17 N ANISOU 2819 N LEU B 97 1851 2019 752 146 -514 -404 N ATOM 2820 CA LEU B 97 66.556 3.172 0.990 1.00 12.71 C ANISOU 2820 CA LEU B 97 2020 2080 732 -244 -445 -318 C ATOM 2821 C LEU B 97 65.550 4.080 0.283 1.00 12.13 C ANISOU 2821 C LEU B 97 1475 2038 1097 -348 -243 -258 C ATOM 2822 O LEU B 97 64.394 3.681 0.094 1.00 13.81 O ANISOU 2822 O LEU B 97 1707 2480 1061 -655 -608 -257 O ATOM 2823 CB LEU B 97 66.573 3.565 2.471 1.00 15.72 C ANISOU 2823 CB LEU B 97 2679 2507 789 -211 -512 -493 C ATOM 2824 CG LEU B 97 67.194 2.566 3.437 1.00 16.48 C ANISOU 2824 CG LEU B 97 2898 2287 1075 7 -110 -341 C ATOM 2825 CD1 LEU B 97 67.065 3.155 4.846 1.00 15.78 C ANISOU 2825 CD1 LEU B 97 2723 2578 694 134 -161 -49 C ATOM 2826 CD2 LEU B 97 66.503 1.206 3.400 1.00 17.95 C ANISOU 2826 CD2 LEU B 97 3223 2420 1176 -193 115 -473 C ATOM 2827 N ALA B 98 65.973 5.302 -0.036 1.00 11.71 N ANISOU 2827 N ALA B 98 1812 1878 758 31 -323 -54 N ATOM 2828 CA ALA B 98 65.076 6.224 -0.737 1.00 12.41 C ANISOU 2828 CA ALA B 98 1774 2045 896 77 -453 -144 C ATOM 2829 C ALA B 98 64.581 5.577 -2.032 1.00 12.53 C ANISOU 2829 C ALA B 98 1421 2358 982 113 -553 -210 C ATOM 2830 O ALA B 98 63.391 5.654 -2.310 1.00 14.01 O ANISOU 2830 O ALA B 98 1342 3123 857 -13 -539 -353 O ATOM 2831 CB ALA B 98 65.782 7.538 -1.000 1.00 12.63 C ANISOU 2831 CB ALA B 98 2245 1824 728 145 -250 -243 C ATOM 2832 N LYS B 99 65.494 4.976 -2.767 1.00 13.52 N ANISOU 2832 N LYS B 99 2068 2286 782 222 -637 -571 N ATOM 2833 CA LYS B 99 65.103 4.335 -4.039 1.00 12.17 C ANISOU 2833 CA LYS B 99 1633 2402 588 22 -492 -428 C ATOM 2834 C LYS B 99 64.234 3.118 -3.790 1.00 14.69 C ANISOU 2834 C LYS B 99 1716 2564 1301 -76 -563 -212 C ATOM 2835 O LYS B 99 63.276 2.863 -4.557 1.00 16.31 O ANISOU 2835 O LYS B 99 2185 3065 947 -124 -776 -406 O ATOM 2836 CB LYS B 99 66.381 4.036 -4.836 1.00 14.22 C ANISOU 2836 CB LYS B 99 1820 2672 912 -92 -144 -99 C ATOM 2837 CG LYS B 99 67.089 5.306 -5.289 1.00 17.92 C ANISOU 2837 CG LYS B 99 1958 2903 1949 -350 -384 134 C ATOM 2838 CD LYS B 99 68.533 5.081 -5.689 1.00 22.14 C ANISOU 2838 CD LYS B 99 2463 3353 2597 10 247 -23 C ATOM 2839 CE LYS B 99 68.644 4.150 -6.882 1.00 24.66 C ANISOU 2839 CE LYS B 99 2974 3503 2892 -33 -119 -255 C ATOM 2840 NZ LYS B 99 68.266 4.860 -8.139 1.00 27.29 N ANISOU 2840 NZ LYS B 99 3735 3688 2946 -216 -86 -89 N ATOM 2841 N ARG B 100 64.467 2.350 -2.732 1.00 14.19 N ANISOU 2841 N ARG B 100 1924 2519 948 -359 -437 -361 N ATOM 2842 CA ARG B 100 63.640 1.201 -2.398 1.00 13.90 C ANISOU 2842 CA ARG B 100 2041 2199 1041 -166 -309 -402 C ATOM 2843 C ARG B 100 62.191 1.608 -2.143 1.00 14.65 C ANISOU 2843 C ARG B 100 1911 2271 1385 -224 -443 -446 C ATOM 2844 O ARG B 100 61.258 0.894 -2.544 1.00 16.53 O ANISOU 2844 O ARG B 100 1848 2734 1699 -298 -587 -539 O ATOM 2845 CB ARG B 100 64.176 0.505 -1.148 1.00 14.75 C ANISOU 2845 CB ARG B 100 2309 2219 1077 -304 -186 -140 C ATOM 2846 CG ARG B 100 63.464 -0.772 -0.754 1.00 14.90 C ANISOU 2846 CG ARG B 100 2199 2130 1333 -244 -214 -257 C ATOM 2847 CD ARG B 100 64.098 -1.392 0.479 1.00 15.96 C ANISOU 2847 CD ARG B 100 2034 2383 1649 -239 -306 -30 C ATOM 2848 NE ARG B 100 63.542 -2.702 0.793 1.00 15.76 N ANISOU 2848 NE ARG B 100 2153 2035 1801 -21 -362 -278 N ATOM 2849 CZ ARG B 100 64.003 -3.841 0.280 1.00 13.20 C ANISOU 2849 CZ ARG B 100 1704 2109 1201 -192 -513 -370 C ATOM 2850 NH1 ARG B 100 65.054 -3.771 -0.526 1.00 15.06 N ANISOU 2850 NH1 ARG B 100 1626 2582 1516 -662 -474 -514 N ATOM 2851 NH2 ARG B 100 63.463 -4.995 0.623 1.00 15.33 N ANISOU 2851 NH2 ARG B 100 1959 2124 1741 -305 -574 -419 N ATOM 2852 N MET B 101 61.988 2.768 -1.531 1.00 14.24 N ANISOU 2852 N MET B 101 1823 2486 1102 -93 -602 -529 N ATOM 2853 CA MET B 101 60.666 3.282 -1.237 1.00 14.88 C ANISOU 2853 CA MET B 101 1917 2274 1465 -62 -321 -331 C ATOM 2854 C MET B 101 60.055 4.010 -2.433 1.00 14.76 C ANISOU 2854 C MET B 101 1597 2642 1367 18 -278 -364 C ATOM 2855 O MET B 101 58.905 4.440 -2.370 1.00 16.48 O ANISOU 2855 O MET B 101 1689 3224 1349 264 -213 -566 O ATOM 2856 CB MET B 101 60.699 4.268 -0.065 1.00 14.86 C ANISOU 2856 CB MET B 101 2001 2281 1365 -24 -337 -259 C ATOM 2857 CG MET B 101 61.089 3.626 1.255 1.00 15.29 C ANISOU 2857 CG MET B 101 2240 2379 1191 -30 -860 -674 C ATOM 2858 SD MET B 101 61.042 4.772 2.650 1.00 17.28 S ANISOU 2858 SD MET B 101 2775 2924 866 -431 -531 -704 S ATOM 2859 CE MET B 101 62.419 5.836 2.268 1.00 16.70 C ANISOU 2859 CE MET B 101 2179 2586 1578 -12 -916 -282 C ATOM 2860 N GLY B 102 60.818 4.164 -3.514 1.00 14.96 N ANISOU 2860 N GLY B 102 1631 2969 1084 -182 -514 -208 N ATOM 2861 CA GLY B 102 60.309 4.827 -4.713 1.00 15.93 C ANISOU 2861 CA GLY B 102 1747 2618 1689 163 -692 -47 C ATOM 2862 C GLY B 102 60.435 6.334 -4.673 1.00 18.41 C ANISOU 2862 C GLY B 102 2243 2667 2085 -76 -404 65 C ATOM 2863 O GLY B 102 59.814 7.018 -5.486 1.00 22.76 O ANISOU 2863 O GLY B 102 2419 3684 2543 66 -837 297 O ATOM 2864 N LYS B 103 61.218 6.882 -3.743 1.00 19.31 N ANISOU 2864 N LYS B 103 1853 2921 2562 -94 -533 -16 N ATOM 2865 CA LYS B 103 61.404 8.322 -3.620 1.00 19.11 C ANISOU 2865 CA LYS B 103 1962 2834 2465 103 -366 34 C ATOM 2866 C LYS B 103 62.406 8.804 -4.667 1.00 18.39 C ANISOU 2866 C LYS B 103 2231 2848 1909 30 -576 23 C ATOM 2867 O LYS B 103 63.372 8.099 -4.952 1.00 21.15 O ANISOU 2867 O LYS B 103 2686 3149 2200 252 -115 -2 O ATOM 2868 CB LYS B 103 61.880 8.721 -2.223 1.00 20.85 C ANISOU 2868 CB LYS B 103 2285 3212 2426 -160 -215 -27 C ATOM 2869 CG LYS B 103 61.081 8.275 -1.019 1.00 23.55 C ANISOU 2869 CG LYS B 103 2879 3181 2888 -100 139 202 C ATOM 2870 CD LYS B 103 59.812 9.045 -0.755 1.00 22.58 C ANISOU 2870 CD LYS B 103 2796 3213 2569 -130 46 69 C ATOM 2871 CE LYS B 103 58.979 8.505 0.394 1.00 22.37 C ANISOU 2871 CE LYS B 103 3370 3269 1861 -278 -54 -244 C ATOM 2872 NZ LYS B 103 59.194 9.253 1.677 1.00 21.23 N ANISOU 2872 NZ LYS B 103 2656 3649 1760 -419 -634 -63 N ATOM 2873 N SER B 104 62.204 10.006 -5.202 1.00 16.84 N ANISOU 2873 N SER B 104 2196 2675 1529 -269 -741 -134 N ATOM 2874 CA SER B 104 63.098 10.546 -6.211 1.00 17.90 C ANISOU 2874 CA SER B 104 2583 2852 1367 -343 -686 -105 C ATOM 2875 C SER B 104 63.906 11.754 -5.784 1.00 16.68 C ANISOU 2875 C SER B 104 2261 2620 1458 -222 -326 -23 C ATOM 2876 O SER B 104 64.781 12.216 -6.522 1.00 17.27 O ANISOU 2876 O SER B 104 2219 3303 1040 -107 -440 174 O ATOM 2877 CB SER B 104 62.276 10.924 -7.465 1.00 20.15 C ANISOU 2877 CB SER B 104 2437 3244 1973 -20 -910 76 C ATOM 2878 OG SER B 104 61.351 11.953 -7.150 1.00 20.99 O ANISOU 2878 OG SER B 104 2467 3412 2098 290 -1539 190 O ATOM 2879 N GLU B 105 63.607 12.281 -4.594 1.00 15.84 N ANISOU 2879 N GLU B 105 2078 2923 1016 -127 -965 74 N ATOM 2880 CA GLU B 105 64.265 13.482 -4.122 1.00 14.77 C ANISOU 2880 CA GLU B 105 1998 2600 1015 37 -699 154 C ATOM 2881 C GLU B 105 64.841 13.241 -2.726 1.00 14.29 C ANISOU 2881 C GLU B 105 2036 2562 832 141 -386 304 C ATOM 2882 O GLU B 105 64.338 12.409 -1.989 1.00 14.87 O ANISOU 2882 O GLU B 105 1901 2765 985 25 -516 424 O ATOM 2883 CB GLU B 105 63.270 14.647 -4.063 1.00 17.00 C ANISOU 2883 CB GLU B 105 2501 2738 1221 316 -643 388 C ATOM 2884 CG GLU B 105 62.640 14.810 -5.451 1.00 18.93 C ANISOU 2884 CG GLU B 105 2584 3456 1153 307 -675 220 C ATOM 2885 CD GLU B 105 61.744 16.006 -5.598 1.00 24.54 C ANISOU 2885 CD GLU B 105 3066 3564 2694 548 -345 -45 C ATOM 2886 OE1 GLU B 105 61.517 16.728 -4.620 1.00 24.54 O ANISOU 2886 OE1 GLU B 105 2318 4193 2814 880 -1005 -460 O ATOM 2887 OE2 GLU B 105 61.253 16.247 -6.732 1.00 28.23 O ANISOU 2887 OE2 GLU B 105 3433 4048 3246 498 -959 200 O ATOM 2888 N ILE B 106 65.886 13.999 -2.473 1.00 13.09 N ANISOU 2888 N ILE B 106 2013 2421 542 304 -413 105 N ATOM 2889 CA ILE B 106 66.570 13.912 -1.181 1.00 12.15 C ANISOU 2889 CA ILE B 106 1669 2293 653 279 -424 -68 C ATOM 2890 C ILE B 106 66.632 15.305 -0.580 1.00 12.48 C ANISOU 2890 C ILE B 106 1941 2223 579 116 -248 -11 C ATOM 2891 O ILE B 106 66.969 16.271 -1.258 1.00 14.00 O ANISOU 2891 O ILE B 106 2348 2272 701 471 33 154 O ATOM 2892 CB ILE B 106 68.030 13.447 -1.368 1.00 11.96 C ANISOU 2892 CB ILE B 106 1466 2083 995 65 -499 151 C ATOM 2893 CG1 ILE B 106 68.080 11.973 -1.776 1.00 12.59 C ANISOU 2893 CG1 ILE B 106 1847 2035 900 151 -216 218 C ATOM 2894 CG2 ILE B 106 68.890 13.641 -0.111 1.00 12.66 C ANISOU 2894 CG2 ILE B 106 1603 2429 777 209 -444 194 C ATOM 2895 CD1 ILE B 106 67.497 11.014 -0.757 1.00 14.81 C ANISOU 2895 CD1 ILE B 106 1707 2302 1620 28 254 327 C ATOM 2896 N ILE B 107 66.354 15.380 0.727 1.00 12.34 N ANISOU 2896 N ILE B 107 1985 2142 560 218 -17 -52 N ATOM 2897 CA ILE B 107 66.549 16.571 1.531 1.00 12.45 C ANISOU 2897 CA ILE B 107 1596 1886 1249 331 6 -100 C ATOM 2898 C ILE B 107 67.674 16.261 2.546 1.00 10.63 C ANISOU 2898 C ILE B 107 1631 1479 927 322 143 -82 C ATOM 2899 O ILE B 107 67.652 15.160 3.114 1.00 12.41 O ANISOU 2899 O ILE B 107 2405 1674 636 214 306 51 O ATOM 2900 CB ILE B 107 65.323 16.907 2.400 1.00 12.95 C ANISOU 2900 CB ILE B 107 1503 2316 1101 136 -10 -125 C ATOM 2901 CG1 ILE B 107 64.105 17.121 1.489 1.00 13.61 C ANISOU 2901 CG1 ILE B 107 1343 2510 1318 231 53 102 C ATOM 2902 CG2 ILE B 107 65.582 18.098 3.315 1.00 15.15 C ANISOU 2902 CG2 ILE B 107 1860 2266 1630 -11 -42 -216 C ATOM 2903 CD1 ILE B 107 62.793 16.986 2.255 1.00 16.02 C ANISOU 2903 CD1 ILE B 107 1365 3044 1678 32 138 148 C ATOM 2904 N ALA B 108 68.585 17.187 2.779 1.00 12.05 N ANISOU 2904 N ALA B 108 1602 2063 912 152 97 -271 N ATOM 2905 CA ALA B 108 69.593 16.926 3.818 1.00 13.00 C ANISOU 2905 CA ALA B 108 1666 1994 1279 108 -11 65 C ATOM 2906 C ALA B 108 69.979 18.230 4.490 1.00 14.93 C ANISOU 2906 C ALA B 108 2519 2110 1045 145 243 -162 C ATOM 2907 O ALA B 108 69.942 19.259 3.826 1.00 17.13 O ANISOU 2907 O ALA B 108 3447 1960 1102 123 -38 -268 O ATOM 2908 CB ALA B 108 70.859 16.320 3.241 1.00 14.83 C ANISOU 2908 CB ALA B 108 2052 2112 1469 218 218 -207 C ATOM 2909 N GLU B 109 70.336 18.161 5.764 1.00 15.40 N ANISOU 2909 N GLU B 109 2438 2119 1292 258 -250 -318 N ATOM 2910 CA GLU B 109 70.831 19.327 6.465 1.00 13.71 C ANISOU 2910 CA GLU B 109 2254 1950 1003 -127 203 33 C ATOM 2911 C GLU B 109 72.354 19.243 6.482 1.00 13.20 C ANISOU 2911 C GLU B 109 2242 1825 948 17 -165 -264 C ATOM 2912 O GLU B 109 72.896 18.140 6.409 1.00 16.08 O ANISOU 2912 O GLU B 109 2600 1856 1651 90 -67 -171 O ATOM 2913 CB GLU B 109 70.371 19.368 7.933 1.00 14.04 C ANISOU 2913 CB GLU B 109 2451 2002 883 300 144 38 C ATOM 2914 CG GLU B 109 71.115 18.446 8.883 1.00 13.08 C ANISOU 2914 CG GLU B 109 2224 1646 1101 143 3 -84 C ATOM 2915 CD GLU B 109 70.897 16.956 8.700 1.00 12.26 C ANISOU 2915 CD GLU B 109 1571 1716 1372 123 141 -199 C ATOM 2916 OE1 GLU B 109 69.941 16.542 8.024 1.00 15.05 O ANISOU 2916 OE1 GLU B 109 1947 2464 1308 -298 86 -163 O ATOM 2917 OE2 GLU B 109 71.679 16.171 9.295 1.00 15.70 O ANISOU 2917 OE2 GLU B 109 2603 1694 1670 220 -460 -189 O ATOM 2918 N THR B 110 73.043 20.364 6.669 1.00 13.68 N ANISOU 2918 N THR B 110 1986 2085 1127 -76 -115 -352 N ATOM 2919 CA THR B 110 74.491 20.315 6.872 1.00 13.95 C ANISOU 2919 CA THR B 110 1943 2142 1214 150 10 -473 C ATOM 2920 C THR B 110 74.931 21.532 7.677 1.00 14.64 C ANISOU 2920 C THR B 110 2081 1812 1671 152 -103 -281 C ATOM 2921 O THR B 110 74.359 22.611 7.560 1.00 14.75 O ANISOU 2921 O THR B 110 2326 1559 1720 81 -238 -727 O ATOM 2922 CB THR B 110 75.274 20.112 5.563 1.00 13.66 C ANISOU 2922 CB THR B 110 2044 2239 909 335 -131 -129 C ATOM 2923 OG1 THR B 110 76.617 19.710 5.863 1.00 15.69 O ANISOU 2923 OG1 THR B 110 1714 2976 1271 137 -105 -1010 O ATOM 2924 CG2 THR B 110 75.331 21.378 4.731 1.00 14.59 C ANISOU 2924 CG2 THR B 110 2271 2035 1237 404 -32 -169 C ATOM 2925 N GLY B 111 75.969 21.326 8.488 1.00 15.10 N ANISOU 2925 N GLY B 111 2366 1986 1386 -59 -273 -333 N ATOM 2926 CA GLY B 111 76.525 22.412 9.297 1.00 17.32 C ANISOU 2926 CA GLY B 111 2682 1959 1941 -145 -100 -533 C ATOM 2927 C GLY B 111 77.763 22.948 8.574 1.00 17.80 C ANISOU 2927 C GLY B 111 2624 2129 2009 78 -145 -73 C ATOM 2928 O GLY B 111 77.736 23.979 7.904 1.00 19.77 O ANISOU 2928 O GLY B 111 3227 1813 2473 -170 169 -121 O ATOM 2929 N ALA B 112 78.863 22.219 8.693 1.00 17.04 N ANISOU 2929 N ALA B 112 2150 2904 1419 3 -321 -298 N ATOM 2930 CA ALA B 112 80.132 22.569 8.091 1.00 19.08 C ANISOU 2930 CA ALA B 112 2378 3052 1818 -61 -6 -317 C ATOM 2931 C ALA B 112 80.177 22.198 6.613 1.00 18.45 C ANISOU 2931 C ALA B 112 2189 2943 1877 -215 -64 -369 C ATOM 2932 O ALA B 112 81.057 22.633 5.886 1.00 19.90 O ANISOU 2932 O ALA B 112 2845 3014 1700 -467 342 -782 O ATOM 2933 CB ALA B 112 81.265 21.896 8.851 1.00 21.47 C ANISOU 2933 CB ALA B 112 2262 3723 2174 242 57 -291 C ATOM 2934 N GLY B 113 79.194 21.412 6.177 1.00 17.19 N ANISOU 2934 N GLY B 113 2304 2500 1726 -28 -252 -453 N ATOM 2935 CA GLY B 113 79.110 21.080 4.764 1.00 15.01 C ANISOU 2935 CA GLY B 113 1738 2249 1719 130 -212 -447 C ATOM 2936 C GLY B 113 79.452 19.660 4.383 1.00 14.75 C ANISOU 2936 C GLY B 113 1943 2128 1532 134 -271 -267 C ATOM 2937 O GLY B 113 79.129 19.278 3.245 1.00 15.44 O ANISOU 2937 O GLY B 113 1850 2617 1400 233 -344 -255 O ATOM 2938 N GLN B 114 80.147 18.881 5.213 1.00 15.03 N ANISOU 2938 N GLN B 114 1934 2355 1422 118 -303 -218 N ATOM 2939 CA GLN B 114 80.528 17.537 4.794 1.00 14.56 C ANISOU 2939 CA GLN B 114 1838 2100 1593 -144 -135 75 C ATOM 2940 C GLN B 114 79.313 16.670 4.523 1.00 13.31 C ANISOU 2940 C GLN B 114 1882 2235 940 -158 -78 -176 C ATOM 2941 O GLN B 114 79.346 15.901 3.556 1.00 14.08 O ANISOU 2941 O GLN B 114 2005 2572 773 -447 42 -208 O ATOM 2942 CB GLN B 114 81.449 16.850 5.811 1.00 16.10 C ANISOU 2942 CB GLN B 114 2018 2454 1647 -46 -469 -169 C ATOM 2943 CG GLN B 114 81.978 15.511 5.332 1.00 19.50 C ANISOU 2943 CG GLN B 114 2692 2445 2271 -84 -50 -219 C ATOM 2944 CD GLN B 114 82.939 15.651 4.170 1.00 22.82 C ANISOU 2944 CD GLN B 114 3492 2651 2525 -127 390 -183 C ATOM 2945 OE1 GLN B 114 83.665 16.642 4.088 1.00 25.24 O ANISOU 2945 OE1 GLN B 114 3410 2824 3356 -133 672 -132 O ATOM 2946 NE2 GLN B 114 82.946 14.652 3.282 1.00 22.46 N ANISOU 2946 NE2 GLN B 114 3637 2344 2551 -56 704 -20 N ATOM 2947 N HIS B 115 78.297 16.730 5.391 1.00 14.19 N ANISOU 2947 N HIS B 115 1607 2498 1287 -345 -72 -86 N ATOM 2948 CA HIS B 115 77.122 15.896 5.131 1.00 12.13 C ANISOU 2948 CA HIS B 115 1743 2214 653 -377 83 -20 C ATOM 2949 C HIS B 115 76.433 16.336 3.840 1.00 13.64 C ANISOU 2949 C HIS B 115 2176 2124 883 -164 -155 -15 C ATOM 2950 O HIS B 115 75.897 15.501 3.102 1.00 13.18 O ANISOU 2950 O HIS B 115 2029 2379 599 -255 -229 74 O ATOM 2951 CB HIS B 115 76.144 15.877 6.300 1.00 11.81 C ANISOU 2951 CB HIS B 115 1681 2355 450 -161 -27 -287 C ATOM 2952 CG HIS B 115 74.982 14.971 6.007 1.00 11.23 C ANISOU 2952 CG HIS B 115 1953 1987 327 -232 56 -59 C ATOM 2953 ND1 HIS B 115 75.127 13.612 5.790 1.00 10.93 N ANISOU 2953 ND1 HIS B 115 1824 1925 404 -130 80 72 N ATOM 2954 CD2 HIS B 115 73.667 15.276 5.887 1.00 11.48 C ANISOU 2954 CD2 HIS B 115 1896 2193 275 -321 -79 219 C ATOM 2955 CE1 HIS B 115 73.925 13.122 5.513 1.00 12.06 C ANISOU 2955 CE1 HIS B 115 1830 2104 649 43 -210 -380 C ATOM 2956 NE2 HIS B 115 73.031 14.108 5.564 1.00 11.99 N ANISOU 2956 NE2 HIS B 115 2307 1733 514 76 -307 227 N ATOM 2957 N GLY B 116 76.448 17.622 3.556 1.00 13.65 N ANISOU 2957 N GLY B 116 2538 2033 615 -314 -9 -227 N ATOM 2958 CA GLY B 116 75.841 18.138 2.324 1.00 13.43 C ANISOU 2958 CA GLY B 116 1991 2358 753 -164 109 -81 C ATOM 2959 C GLY B 116 76.611 17.570 1.122 1.00 12.78 C ANISOU 2959 C GLY B 116 1816 1960 1080 -240 17 -384 C ATOM 2960 O GLY B 116 75.986 17.121 0.156 1.00 13.63 O ANISOU 2960 O GLY B 116 2376 2153 649 -267 115 -444 O ATOM 2961 N VAL B 117 77.941 17.599 1.223 1.00 12.92 N ANISOU 2961 N VAL B 117 1813 2173 924 156 -73 -144 N ATOM 2962 CA VAL B 117 78.732 17.060 0.107 1.00 13.99 C ANISOU 2962 CA VAL B 117 1993 1987 1336 -225 245 -423 C ATOM 2963 C VAL B 117 78.465 15.580 -0.052 1.00 12.20 C ANISOU 2963 C VAL B 117 2062 1950 622 -289 58 -65 C ATOM 2964 O VAL B 117 78.307 15.072 -1.164 1.00 12.30 O ANISOU 2964 O VAL B 117 2010 1910 752 -32 -170 -364 O ATOM 2965 CB VAL B 117 80.227 17.353 0.303 1.00 14.62 C ANISOU 2965 CB VAL B 117 1706 2094 1754 208 688 -478 C ATOM 2966 CG1 VAL B 117 81.097 16.613 -0.708 1.00 15.68 C ANISOU 2966 CG1 VAL B 117 1684 2461 1812 91 959 -460 C ATOM 2967 CG2 VAL B 117 80.485 18.854 0.194 1.00 17.41 C ANISOU 2967 CG2 VAL B 117 2374 2150 2090 25 360 -410 C ATOM 2968 N ALA B 118 78.437 14.846 1.060 1.00 12.39 N ANISOU 2968 N ALA B 118 1753 2033 922 -107 -236 250 N ATOM 2969 CA ALA B 118 78.198 13.411 1.014 1.00 12.36 C ANISOU 2969 CA ALA B 118 1685 2052 959 -113 -473 -13 C ATOM 2970 C ALA B 118 76.821 13.138 0.405 1.00 10.43 C ANISOU 2970 C ALA B 118 1316 1734 913 29 -101 -119 C ATOM 2971 O ALA B 118 76.656 12.231 -0.413 1.00 10.89 O ANISOU 2971 O ALA B 118 1898 1609 631 293 -342 43 O ATOM 2972 CB ALA B 118 78.329 12.842 2.421 1.00 12.20 C ANISOU 2972 CB ALA B 118 1545 1846 1245 -86 -539 246 C ATOM 2973 N SER B 119 75.810 13.906 0.827 1.00 10.86 N ANISOU 2973 N SER B 119 1432 1960 732 238 111 335 N ATOM 2974 CA SER B 119 74.460 13.677 0.314 1.00 10.88 C ANISOU 2974 CA SER B 119 1474 1938 720 257 65 249 C ATOM 2975 C SER B 119 74.421 13.965 -1.184 1.00 10.40 C ANISOU 2975 C SER B 119 1639 1735 576 21 -43 -200 C ATOM 2976 O SER B 119 73.775 13.245 -1.950 1.00 10.77 O ANISOU 2976 O SER B 119 1534 1628 929 -40 -92 -160 O ATOM 2977 CB SER B 119 73.450 14.551 1.060 1.00 12.32 C ANISOU 2977 CB SER B 119 2061 2046 572 273 205 -29 C ATOM 2978 OG SER B 119 73.380 14.172 2.445 1.00 14.97 O ANISOU 2978 OG SER B 119 2462 2661 566 406 27 4 O ATOM 2979 N ALA B 120 75.114 15.034 -1.563 1.00 10.15 N ANISOU 2979 N ALA B 120 1752 1788 316 149 222 -73 N ATOM 2980 CA ALA B 120 75.120 15.407 -2.986 1.00 10.13 C ANISOU 2980 CA ALA B 120 1868 1515 465 239 190 56 C ATOM 2981 C ALA B 120 75.825 14.334 -3.809 1.00 10.63 C ANISOU 2981 C ALA B 120 1805 1550 685 281 -175 -275 C ATOM 2982 O ALA B 120 75.340 14.052 -4.909 1.00 11.77 O ANISOU 2982 O ALA B 120 2034 1983 454 267 -58 -335 O ATOM 2983 CB ALA B 120 75.816 16.738 -3.180 1.00 11.84 C ANISOU 2983 CB ALA B 120 1598 1838 1061 -75 -34 -57 C ATOM 2984 N LEU B 121 76.968 13.822 -3.357 1.00 11.23 N ANISOU 2984 N LEU B 121 1683 1868 715 514 206 -143 N ATOM 2985 CA LEU B 121 77.665 12.834 -4.213 1.00 11.18 C ANISOU 2985 CA LEU B 121 1826 1630 794 425 93 -213 C ATOM 2986 C LEU B 121 76.848 11.553 -4.338 1.00 12.06 C ANISOU 2986 C LEU B 121 1737 1882 963 281 -114 -235 C ATOM 2987 O LEU B 121 76.800 10.933 -5.410 1.00 13.48 O ANISOU 2987 O LEU B 121 2391 2334 396 393 -164 64 O ATOM 2988 CB LEU B 121 79.088 12.572 -3.754 1.00 12.61 C ANISOU 2988 CB LEU B 121 1739 2049 1004 272 92 102 C ATOM 2989 CG LEU B 121 79.329 11.903 -2.395 1.00 11.68 C ANISOU 2989 CG LEU B 121 1501 1853 1084 286 -218 21 C ATOM 2990 CD1 LEU B 121 79.362 10.387 -2.523 1.00 12.88 C ANISOU 2990 CD1 LEU B 121 1933 1897 1063 206 -75 -167 C ATOM 2991 CD2 LEU B 121 80.671 12.370 -1.822 1.00 12.71 C ANISOU 2991 CD2 LEU B 121 1711 2116 1003 117 -203 -397 C ATOM 2992 N ALA B 122 76.216 11.127 -3.239 1.00 11.19 N ANISOU 2992 N ALA B 122 1614 1713 924 235 -288 -64 N ATOM 2993 CA ALA B 122 75.401 9.915 -3.302 1.00 11.20 C ANISOU 2993 CA ALA B 122 1509 1715 1032 244 -231 314 C ATOM 2994 C ALA B 122 74.228 10.121 -4.260 1.00 11.05 C ANISOU 2994 C ALA B 122 1443 1764 993 61 -351 -306 C ATOM 2995 O ALA B 122 73.830 9.204 -4.983 1.00 12.57 O ANISOU 2995 O ALA B 122 1902 2024 849 392 -392 -684 O ATOM 2996 CB ALA B 122 74.859 9.532 -1.935 1.00 12.00 C ANISOU 2996 CB ALA B 122 1755 1912 892 134 -315 313 C ATOM 2997 N SER B 123 73.645 11.310 -4.178 1.00 11.46 N ANISOU 2997 N SER B 123 1559 1950 846 288 -309 -49 N ATOM 2998 CA SER B 123 72.472 11.619 -5.017 1.00 11.98 C ANISOU 2998 CA SER B 123 1462 2279 812 761 -18 63 C ATOM 2999 C SER B 123 72.863 11.680 -6.491 1.00 12.46 C ANISOU 2999 C SER B 123 1815 2246 672 102 -217 -313 C ATOM 3000 O SER B 123 72.120 11.184 -7.350 1.00 14.62 O ANISOU 3000 O SER B 123 1413 3345 796 146 -340 -364 O ATOM 3001 CB SER B 123 71.861 12.943 -4.559 1.00 12.77 C ANISOU 3001 CB SER B 123 1957 2089 805 675 -130 45 C ATOM 3002 OG SER B 123 71.290 12.772 -3.263 1.00 12.99 O ANISOU 3002 OG SER B 123 2128 2163 644 635 -155 -193 O ATOM 3003 N ALA B 124 74.032 12.260 -6.750 1.00 12.27 N ANISOU 3003 N ALA B 124 1967 2236 459 58 -22 -83 N ATOM 3004 CA ALA B 124 74.505 12.350 -8.139 1.00 12.54 C ANISOU 3004 CA ALA B 124 2226 2016 521 88 40 -79 C ATOM 3005 C ALA B 124 74.713 10.948 -8.694 1.00 13.79 C ANISOU 3005 C ALA B 124 2348 2139 752 303 -231 -300 C ATOM 3006 O ALA B 124 74.321 10.641 -9.830 1.00 16.59 O ANISOU 3006 O ALA B 124 2912 2830 562 489 -88 -469 O ATOM 3007 CB ALA B 124 75.802 13.137 -8.214 1.00 12.37 C ANISOU 3007 CB ALA B 124 2318 2019 363 38 482 63 C ATOM 3008 N LEU B 125 75.361 10.082 -7.919 1.00 12.48 N ANISOU 3008 N LEU B 125 1994 1748 1002 183 -138 -384 N ATOM 3009 CA LEU B 125 75.633 8.731 -8.385 1.00 12.13 C ANISOU 3009 CA LEU B 125 2014 1735 859 187 -9 -257 C ATOM 3010 C LEU B 125 74.369 7.928 -8.638 1.00 12.40 C ANISOU 3010 C LEU B 125 1770 2156 785 245 10 -359 C ATOM 3011 O LEU B 125 74.273 7.161 -9.617 1.00 13.44 O ANISOU 3011 O LEU B 125 2326 2320 462 -57 318 -255 O ATOM 3012 CB LEU B 125 76.493 8.015 -7.316 1.00 12.79 C ANISOU 3012 CB LEU B 125 1988 1809 1062 274 -49 -195 C ATOM 3013 CG LEU B 125 76.835 6.550 -7.634 1.00 13.34 C ANISOU 3013 CG LEU B 125 2232 1636 1202 208 279 139 C ATOM 3014 CD1 LEU B 125 77.750 6.450 -8.854 1.00 15.09 C ANISOU 3014 CD1 LEU B 125 1976 2193 1563 257 384 -8 C ATOM 3015 CD2 LEU B 125 77.464 5.876 -6.420 1.00 13.87 C ANISOU 3015 CD2 LEU B 125 1894 1621 1754 453 -352 -156 C ATOM 3016 N LEU B 126 73.389 8.068 -7.745 1.00 12.89 N ANISOU 3016 N LEU B 126 1844 2416 637 165 18 -329 N ATOM 3017 CA LEU B 126 72.199 7.240 -7.749 1.00 12.84 C ANISOU 3017 CA LEU B 126 2108 2300 470 48 -80 -205 C ATOM 3018 C LEU B 126 70.948 7.847 -8.344 1.00 14.09 C ANISOU 3018 C LEU B 126 2090 2547 717 -39 -325 -310 C ATOM 3019 O LEU B 126 69.863 7.260 -8.239 1.00 16.84 O ANISOU 3019 O LEU B 126 2041 3259 1100 -185 -563 -365 O ATOM 3020 CB LEU B 126 71.989 6.724 -6.302 1.00 13.17 C ANISOU 3020 CB LEU B 126 2217 2347 438 96 139 -312 C ATOM 3021 CG LEU B 126 73.179 5.871 -5.842 1.00 14.82 C ANISOU 3021 CG LEU B 126 2599 2114 918 164 -27 -264 C ATOM 3022 CD1 LEU B 126 73.117 5.599 -4.351 1.00 17.18 C ANISOU 3022 CD1 LEU B 126 2927 2659 942 157 84 -263 C ATOM 3023 CD2 LEU B 126 73.233 4.561 -6.612 1.00 16.47 C ANISOU 3023 CD2 LEU B 126 3040 2002 1216 359 -169 -236 C ATOM 3024 N GLY B 127 71.097 8.967 -9.025 1.00 14.47 N ANISOU 3024 N GLY B 127 2419 2572 505 470 -391 -246 N ATOM 3025 CA GLY B 127 69.986 9.540 -9.793 1.00 15.86 C ANISOU 3025 CA GLY B 127 2248 2785 994 384 -602 -269 C ATOM 3026 C GLY B 127 68.882 10.152 -8.965 1.00 16.91 C ANISOU 3026 C GLY B 127 2157 2735 1534 257 -565 -512 C ATOM 3027 O GLY B 127 67.692 10.098 -9.303 1.00 19.02 O ANISOU 3027 O GLY B 127 2191 3186 1850 346 -685 -735 O ATOM 3028 N LEU B 128 69.249 10.788 -7.859 1.00 14.16 N ANISOU 3028 N LEU B 128 2059 2446 875 323 -481 -50 N ATOM 3029 CA LEU B 128 68.281 11.451 -6.993 1.00 13.31 C ANISOU 3029 CA LEU B 128 2000 2050 1008 238 -385 135 C ATOM 3030 C LEU B 128 68.459 12.957 -7.060 1.00 11.45 C ANISOU 3030 C LEU B 128 1497 1974 881 425 -357 179 C ATOM 3031 O LEU B 128 69.592 13.437 -7.190 1.00 15.68 O ANISOU 3031 O LEU B 128 1470 3065 1424 283 -590 384 O ATOM 3032 CB LEU B 128 68.498 10.960 -5.550 1.00 13.52 C ANISOU 3032 CB LEU B 128 1986 2144 1007 115 -343 236 C ATOM 3033 CG LEU B 128 68.156 9.489 -5.304 1.00 14.42 C ANISOU 3033 CG LEU B 128 2224 1984 1270 159 -630 -25 C ATOM 3034 CD1 LEU B 128 68.771 8.971 -4.008 1.00 15.07 C ANISOU 3034 CD1 LEU B 128 2342 2403 980 -184 -465 166 C ATOM 3035 CD2 LEU B 128 66.646 9.297 -5.241 1.00 17.45 C ANISOU 3035 CD2 LEU B 128 2368 1895 2366 -182 -360 220 C ATOM 3036 N LYS B 129 67.381 13.733 -6.940 1.00 14.08 N ANISOU 3036 N LYS B 129 1325 2446 1579 457 -503 -56 N ATOM 3037 CA LYS B 129 67.447 15.180 -6.951 1.00 14.46 C ANISOU 3037 CA LYS B 129 1748 2471 1275 104 -451 -40 C ATOM 3038 C LYS B 129 67.609 15.659 -5.503 1.00 15.15 C ANISOU 3038 C LYS B 129 1830 2753 1175 113 1 -27 C ATOM 3039 O LYS B 129 66.704 15.481 -4.682 1.00 18.04 O ANISOU 3039 O LYS B 129 1776 3629 1449 -364 -101 275 O ATOM 3040 CB LYS B 129 66.158 15.794 -7.509 1.00 18.97 C ANISOU 3040 CB LYS B 129 1830 3179 2197 444 -410 145 C ATOM 3041 CG LYS B 129 65.713 15.146 -8.806 1.00 25.29 C ANISOU 3041 CG LYS B 129 3635 3169 2803 -31 -471 -261 C ATOM 3042 CD LYS B 129 64.316 15.640 -9.187 1.00 32.08 C ANISOU 3042 CD LYS B 129 3643 4383 4164 148 -219 29 C ATOM 3043 CE LYS B 129 63.826 14.873 -10.408 1.00 36.12 C ANISOU 3043 CE LYS B 129 4601 4707 4415 -21 -144 -168 C ATOM 3044 NZ LYS B 129 62.549 15.421 -10.939 1.00 38.76 N ANISOU 3044 NZ LYS B 129 4717 5073 4938 92 -156 -5 N ATOM 3045 N CYS B 130 68.742 16.270 -5.238 1.00 14.62 N ANISOU 3045 N CYS B 130 2043 2632 878 161 -502 214 N ATOM 3046 CA CYS B 130 69.121 16.625 -3.882 1.00 13.61 C ANISOU 3046 CA CYS B 130 2185 2189 797 318 -8 -40 C ATOM 3047 C CYS B 130 69.035 18.105 -3.574 1.00 15.37 C ANISOU 3047 C CYS B 130 2464 2173 1204 253 190 -126 C ATOM 3048 O CYS B 130 69.544 18.922 -4.342 1.00 16.21 O ANISOU 3048 O CYS B 130 2310 2596 1253 599 766 -87 O ATOM 3049 CB CYS B 130 70.580 16.169 -3.724 1.00 13.56 C ANISOU 3049 CB CYS B 130 2151 2026 976 174 -99 330 C ATOM 3050 SG CYS B 130 71.278 16.353 -2.072 1.00 14.74 S ANISOU 3050 SG CYS B 130 2093 2466 1043 863 -248 -142 S ATOM 3051 N ARG B 131 68.444 18.425 -2.419 1.00 14.18 N ANISOU 3051 N ARG B 131 2129 2109 1151 277 259 165 N ATOM 3052 CA ARG B 131 68.399 19.797 -1.920 1.00 13.57 C ANISOU 3052 CA ARG B 131 1906 2146 1105 213 42 123 C ATOM 3053 C ARG B 131 68.931 19.757 -0.477 1.00 13.66 C ANISOU 3053 C ARG B 131 2123 2113 954 -20 236 -125 C ATOM 3054 O ARG B 131 68.567 18.872 0.295 1.00 15.11 O ANISOU 3054 O ARG B 131 2292 2198 1251 41 142 146 O ATOM 3055 CB ARG B 131 67.035 20.440 -1.998 1.00 15.03 C ANISOU 3055 CB ARG B 131 1852 2227 1632 147 19 192 C ATOM 3056 CG ARG B 131 65.897 19.715 -1.302 1.00 15.75 C ANISOU 3056 CG ARG B 131 1629 2604 1749 105 70 46 C ATOM 3057 CD ARG B 131 64.600 20.461 -1.572 1.00 15.11 C ANISOU 3057 CD ARG B 131 1748 2548 1446 68 -96 343 C ATOM 3058 NE ARG B 131 63.413 19.830 -1.050 1.00 13.89 N ANISOU 3058 NE ARG B 131 1913 2036 1328 82 -45 338 N ATOM 3059 CZ ARG B 131 62.676 18.871 -1.576 1.00 14.29 C ANISOU 3059 CZ ARG B 131 1848 2350 1232 -6 -17 143 C ATOM 3060 NH1 ARG B 131 63.009 18.328 -2.749 1.00 15.92 N ANISOU 3060 NH1 ARG B 131 2078 2685 1287 398 53 150 N ATOM 3061 NH2 ARG B 131 61.583 18.416 -0.974 1.00 16.08 N ANISOU 3061 NH2 ARG B 131 1923 2818 1368 34 264 -132 N ATOM 3062 N ILE B 132 69.795 20.703 -0.178 1.00 13.54 N ANISOU 3062 N ILE B 132 2047 2213 885 67 67 -229 N ATOM 3063 CA ILE B 132 70.478 20.759 1.106 1.00 13.74 C ANISOU 3063 CA ILE B 132 2312 1995 914 56 -6 40 C ATOM 3064 C ILE B 132 70.203 22.066 1.799 1.00 14.11 C ANISOU 3064 C ILE B 132 2437 1993 932 -15 -53 -26 C ATOM 3065 O ILE B 132 70.384 23.127 1.225 1.00 15.14 O ANISOU 3065 O ILE B 132 2723 1950 1079 115 287 -56 O ATOM 3066 CB ILE B 132 71.992 20.647 0.864 1.00 13.66 C ANISOU 3066 CB ILE B 132 2300 1687 1204 251 -80 32 C ATOM 3067 CG1 ILE B 132 72.273 19.264 0.242 1.00 17.74 C ANISOU 3067 CG1 ILE B 132 2511 2429 1800 580 4 -755 C ATOM 3068 CG2 ILE B 132 72.799 20.831 2.136 1.00 14.19 C ANISOU 3068 CG2 ILE B 132 1998 2070 1325 486 -50 -191 C ATOM 3069 CD1 ILE B 132 73.587 19.239 -0.497 1.00 21.41 C ANISOU 3069 CD1 ILE B 132 2669 2881 2586 60 254 221 C ATOM 3070 N TYR B 133 69.830 21.981 3.070 1.00 13.15 N ANISOU 3070 N TYR B 133 2222 1795 977 179 108 -56 N ATOM 3071 CA TYR B 133 69.595 23.149 3.903 1.00 13.45 C ANISOU 3071 CA TYR B 133 2010 1905 1197 227 123 -215 C ATOM 3072 C TYR B 133 70.850 23.383 4.740 1.00 14.49 C ANISOU 3072 C TYR B 133 2115 1852 1541 41 -38 19 C ATOM 3073 O TYR B 133 71.390 22.438 5.319 1.00 14.69 O ANISOU 3073 O TYR B 133 2640 1858 1084 189 265 22 O ATOM 3074 CB TYR B 133 68.396 22.934 4.833 1.00 13.47 C ANISOU 3074 CB TYR B 133 1648 2050 1421 241 14 -36 C ATOM 3075 CG TYR B 133 67.107 22.979 4.036 1.00 13.28 C ANISOU 3075 CG TYR B 133 1626 1873 1546 278 18 -75 C ATOM 3076 CD1 TYR B 133 66.648 24.203 3.570 1.00 13.61 C ANISOU 3076 CD1 TYR B 133 1569 1845 1758 457 263 -168 C ATOM 3077 CD2 TYR B 133 66.404 21.831 3.730 1.00 14.41 C ANISOU 3077 CD2 TYR B 133 1775 2237 1463 43 41 -264 C ATOM 3078 CE1 TYR B 133 65.488 24.269 2.824 1.00 15.40 C ANISOU 3078 CE1 TYR B 133 1631 2323 1895 44 118 -134 C ATOM 3079 CE2 TYR B 133 65.249 21.890 2.968 1.00 15.40 C ANISOU 3079 CE2 TYR B 133 1509 2069 2274 144 -23 -29 C ATOM 3080 CZ TYR B 133 64.794 23.120 2.532 1.00 15.81 C ANISOU 3080 CZ TYR B 133 1980 2096 1930 27 93 201 C ATOM 3081 OH TYR B 133 63.639 23.204 1.790 1.00 17.89 O ANISOU 3081 OH TYR B 133 1898 2888 2012 480 191 348 O ATOM 3082 N MET B 134 71.266 24.630 4.765 1.00 14.83 N ANISOU 3082 N MET B 134 2181 1931 1523 -106 91 -291 N ATOM 3083 CA MET B 134 72.470 25.027 5.491 1.00 14.39 C ANISOU 3083 CA MET B 134 2058 1908 1501 -33 104 -97 C ATOM 3084 C MET B 134 72.275 26.408 6.096 1.00 15.90 C ANISOU 3084 C MET B 134 2603 1969 1470 164 127 -72 C ATOM 3085 O MET B 134 71.838 27.330 5.408 1.00 16.90 O ANISOU 3085 O MET B 134 3082 1679 1662 204 420 -24 O ATOM 3086 CB MET B 134 73.619 25.033 4.487 1.00 14.62 C ANISOU 3086 CB MET B 134 2172 1663 1720 -352 241 30 C ATOM 3087 CG MET B 134 75.011 25.206 5.086 1.00 16.45 C ANISOU 3087 CG MET B 134 2055 2556 1637 16 310 -178 C ATOM 3088 SD MET B 134 76.211 24.889 3.772 1.00 17.64 S ANISOU 3088 SD MET B 134 2493 2652 1557 71 496 -134 S ATOM 3089 CE MET B 134 77.731 24.749 4.694 1.00 19.17 C ANISOU 3089 CE MET B 134 2353 2685 2246 -137 339 116 C ATOM 3090 N GLY B 135 72.550 26.541 7.390 1.00 15.17 N ANISOU 3090 N GLY B 135 2697 1772 1295 112 446 -25 N ATOM 3091 CA GLY B 135 72.400 27.855 8.033 1.00 16.74 C ANISOU 3091 CA GLY B 135 2828 1657 1876 -46 453 -34 C ATOM 3092 C GLY B 135 73.212 28.894 7.262 1.00 16.93 C ANISOU 3092 C GLY B 135 2447 1853 2131 67 419 184 C ATOM 3093 O GLY B 135 74.340 28.632 6.852 1.00 17.32 O ANISOU 3093 O GLY B 135 2619 2267 1697 153 553 182 O ATOM 3094 N ALA B 136 72.637 30.074 7.075 1.00 17.68 N ANISOU 3094 N ALA B 136 2708 1865 2146 123 453 139 N ATOM 3095 CA ALA B 136 73.327 31.127 6.326 1.00 17.46 C ANISOU 3095 CA ALA B 136 2495 2023 2117 7 418 131 C ATOM 3096 C ALA B 136 74.683 31.480 6.906 1.00 17.89 C ANISOU 3096 C ALA B 136 2464 2283 2049 76 434 56 C ATOM 3097 O ALA B 136 75.583 31.850 6.140 1.00 18.51 O ANISOU 3097 O ALA B 136 2713 2176 2146 -401 394 191 O ATOM 3098 CB ALA B 136 72.419 32.349 6.235 1.00 20.10 C ANISOU 3098 CB ALA B 136 2601 2425 2613 289 492 191 C ATOM 3099 N LYS B 137 74.898 31.398 8.219 1.00 19.19 N ANISOU 3099 N LYS B 137 2680 2466 2147 5 47 30 N ATOM 3100 CA LYS B 137 76.207 31.704 8.803 1.00 19.96 C ANISOU 3100 CA LYS B 137 2478 2661 2446 -61 272 -15 C ATOM 3101 C LYS B 137 77.197 30.632 8.348 1.00 19.60 C ANISOU 3101 C LYS B 137 2301 2651 2494 -84 60 -121 C ATOM 3102 O LYS B 137 78.371 30.903 8.091 1.00 21.23 O ANISOU 3102 O LYS B 137 2403 2851 2813 70 521 -75 O ATOM 3103 CB LYS B 137 76.142 31.791 10.328 1.00 21.39 C ANISOU 3103 CB LYS B 137 2698 3002 2428 -123 293 131 C ATOM 3104 CG LYS B 137 75.428 33.031 10.854 1.00 27.02 C ANISOU 3104 CG LYS B 137 3512 3140 3614 -15 364 -112 C ATOM 3105 CD LYS B 137 75.529 33.056 12.378 1.00 32.23 C ANISOU 3105 CD LYS B 137 4306 4148 3791 -91 138 -128 C ATOM 3106 CE LYS B 137 74.556 34.056 12.980 1.00 34.55 C ANISOU 3106 CE LYS B 137 4536 4212 4380 59 110 -181 C ATOM 3107 NZ LYS B 137 74.335 33.755 14.427 1.00 37.15 N ANISOU 3107 NZ LYS B 137 4913 4731 4470 0 -10 -107 N ATOM 3108 N ASP B 138 76.715 29.404 8.208 1.00 19.31 N ANISOU 3108 N ASP B 138 2746 2450 2141 21 291 14 N ATOM 3109 CA ASP B 138 77.574 28.312 7.744 1.00 20.05 C ANISOU 3109 CA ASP B 138 2677 2666 2276 69 340 -35 C ATOM 3110 C ASP B 138 77.847 28.449 6.251 1.00 20.09 C ANISOU 3110 C ASP B 138 2630 2781 2221 91 192 29 C ATOM 3111 O ASP B 138 78.989 28.227 5.820 1.00 20.51 O ANISOU 3111 O ASP B 138 2372 2876 2545 -198 79 45 O ATOM 3112 CB ASP B 138 76.964 26.966 8.100 1.00 19.28 C ANISOU 3112 CB ASP B 138 2785 2593 1947 77 207 -46 C ATOM 3113 CG ASP B 138 77.057 26.723 9.604 1.00 20.08 C ANISOU 3113 CG ASP B 138 2740 2912 1978 -39 69 -22 C ATOM 3114 OD1 ASP B 138 78.119 27.050 10.185 1.00 22.36 O ANISOU 3114 OD1 ASP B 138 2827 3257 2411 -324 49 64 O ATOM 3115 OD2 ASP B 138 76.073 26.190 10.146 1.00 20.70 O ANISOU 3115 OD2 ASP B 138 2702 3355 1808 214 268 127 O ATOM 3116 N VAL B 139 76.828 28.833 5.489 1.00 18.58 N ANISOU 3116 N VAL B 139 2656 2476 1928 133 294 -114 N ATOM 3117 CA VAL B 139 77.027 29.027 4.043 1.00 18.09 C ANISOU 3117 CA VAL B 139 2442 2517 1915 -47 230 -53 C ATOM 3118 C VAL B 139 78.142 30.022 3.799 1.00 19.39 C ANISOU 3118 C VAL B 139 2637 2486 2243 -104 361 -185 C ATOM 3119 O VAL B 139 79.034 29.837 2.956 1.00 20.55 O ANISOU 3119 O VAL B 139 2720 2714 2374 -96 516 -223 O ATOM 3120 CB VAL B 139 75.725 29.512 3.388 1.00 17.16 C ANISOU 3120 CB VAL B 139 2722 2119 1679 -151 182 412 C ATOM 3121 CG1 VAL B 139 75.964 29.962 1.953 1.00 17.90 C ANISOU 3121 CG1 VAL B 139 3052 2374 1377 13 187 68 C ATOM 3122 CG2 VAL B 139 74.689 28.391 3.411 1.00 19.52 C ANISOU 3122 CG2 VAL B 139 2739 2290 2386 -239 62 263 C ATOM 3123 N GLU B 140 78.127 31.122 4.556 1.00 19.86 N ANISOU 3123 N GLU B 140 2714 2500 2330 127 535 -235 N ATOM 3124 CA GLU B 140 79.142 32.160 4.414 1.00 23.88 C ANISOU 3124 CA GLU B 140 2783 3095 3196 -180 277 -7 C ATOM 3125 C GLU B 140 80.539 31.660 4.737 1.00 21.31 C ANISOU 3125 C GLU B 140 2812 2798 2486 -202 147 -174 C ATOM 3126 O GLU B 140 81.503 32.100 4.096 1.00 24.41 O ANISOU 3126 O GLU B 140 2768 3392 3112 -373 254 -105 O ATOM 3127 CB GLU B 140 78.790 33.360 5.305 1.00 30.25 C ANISOU 3127 CB GLU B 140 4084 3718 3691 174 316 -414 C ATOM 3128 CG GLU B 140 79.708 34.560 5.092 1.00 38.19 C ANISOU 3128 CG GLU B 140 4928 4441 5143 -351 186 -132 C ATOM 3129 CD GLU B 140 79.428 35.258 3.773 1.00 43.94 C ANISOU 3129 CD GLU B 140 5832 5450 5416 36 22 99 C ATOM 3130 OE1 GLU B 140 78.514 34.809 3.046 1.00 46.60 O ANISOU 3130 OE1 GLU B 140 6120 5781 5806 -107 -96 5 O ATOM 3131 OE2 GLU B 140 80.109 36.256 3.457 1.00 47.19 O ANISOU 3131 OE2 GLU B 140 6140 5779 6011 -131 75 170 O ATOM 3132 N ARG B 141 80.687 30.758 5.699 1.00 21.14 N ANISOU 3132 N ARG B 141 2828 2650 2553 29 -46 -288 N ATOM 3133 CA ARG B 141 81.991 30.260 6.119 1.00 22.03 C ANISOU 3133 CA ARG B 141 2720 2868 2782 103 -2 -447 C ATOM 3134 C ARG B 141 82.425 28.959 5.456 1.00 22.81 C ANISOU 3134 C ARG B 141 2927 2791 2949 13 -322 -573 C ATOM 3135 O ARG B 141 83.510 28.434 5.733 1.00 23.85 O ANISOU 3135 O ARG B 141 3161 3085 2817 306 -337 -887 O ATOM 3136 CB ARG B 141 82.042 30.118 7.636 1.00 25.24 C ANISOU 3136 CB ARG B 141 3336 3334 2921 17 2 -41 C ATOM 3137 CG ARG B 141 80.960 29.320 8.335 1.00 28.53 C ANISOU 3137 CG ARG B 141 3619 3675 3548 -225 135 -10 C ATOM 3138 CD ARG B 141 81.043 29.552 9.845 1.00 30.72 C ANISOU 3138 CD ARG B 141 4146 3929 3598 -51 64 -59 C ATOM 3139 NE ARG B 141 79.968 28.867 10.562 1.00 33.78 N ANISOU 3139 NE ARG B 141 4259 4359 4216 -156 174 9 N ATOM 3140 CZ ARG B 141 79.638 29.160 11.817 1.00 34.01 C ANISOU 3140 CZ ARG B 141 4336 4404 4182 -186 166 -70 C ATOM 3141 NH1 ARG B 141 80.309 30.114 12.457 1.00 36.37 N ANISOU 3141 NH1 ARG B 141 4556 4529 4734 -163 101 -242 N ATOM 3142 NH2 ARG B 141 78.658 28.517 12.432 1.00 32.91 N ANISOU 3142 NH2 ARG B 141 4104 4295 4103 -228 -82 -126 N ATOM 3143 N GLN B 142 81.590 28.432 4.564 1.00 20.99 N ANISOU 3143 N GLN B 142 2916 2586 2475 113 -115 -613 N ATOM 3144 CA GLN B 142 81.906 27.156 3.920 1.00 19.44 C ANISOU 3144 CA GLN B 142 2627 2496 2264 116 120 -381 C ATOM 3145 C GLN B 142 81.748 27.205 2.411 1.00 18.93 C ANISOU 3145 C GLN B 142 2326 2560 2306 -214 -139 -255 C ATOM 3146 O GLN B 142 81.224 26.276 1.773 1.00 18.97 O ANISOU 3146 O GLN B 142 2340 2553 2316 -61 94 -515 O ATOM 3147 CB GLN B 142 81.032 26.067 4.539 1.00 20.84 C ANISOU 3147 CB GLN B 142 2747 2942 2230 140 189 0 C ATOM 3148 CG GLN B 142 81.162 25.960 6.053 1.00 21.39 C ANISOU 3148 CG GLN B 142 2681 3258 2188 129 83 -316 C ATOM 3149 CD GLN B 142 82.505 25.411 6.481 1.00 23.86 C ANISOU 3149 CD GLN B 142 2984 3620 2463 242 -156 -93 C ATOM 3150 OE1 GLN B 142 83.328 24.968 5.678 1.00 23.53 O ANISOU 3150 OE1 GLN B 142 2790 3712 2438 295 -248 -101 O ATOM 3151 NE2 GLN B 142 82.759 25.421 7.787 1.00 23.38 N ANISOU 3151 NE2 GLN B 142 2853 3564 2469 103 -373 -309 N ATOM 3152 N SER B 143 82.289 28.259 1.799 1.00 20.60 N ANISOU 3152 N SER B 143 2832 2532 2462 -176 -56 -149 N ATOM 3153 CA SER B 143 82.209 28.412 0.349 1.00 21.75 C ANISOU 3153 CA SER B 143 3111 2709 2444 -67 -43 -169 C ATOM 3154 C SER B 143 82.707 27.205 -0.428 1.00 20.57 C ANISOU 3154 C SER B 143 2524 2811 2483 -100 133 -179 C ATOM 3155 O SER B 143 82.030 26.782 -1.378 1.00 21.21 O ANISOU 3155 O SER B 143 3043 3104 1912 -326 291 69 O ATOM 3156 CB SER B 143 82.909 29.685 -0.128 1.00 25.44 C ANISOU 3156 CB SER B 143 3565 2953 3149 -262 128 20 C ATOM 3157 OG SER B 143 82.303 30.823 0.467 1.00 32.18 O ANISOU 3157 OG SER B 143 4341 3680 4207 279 305 -191 O ATOM 3158 N PRO B 144 83.811 26.593 -0.041 1.00 21.48 N ANISOU 3158 N PRO B 144 2710 2997 2454 -3 34 -241 N ATOM 3159 CA PRO B 144 84.326 25.433 -0.759 1.00 21.02 C ANISOU 3159 CA PRO B 144 2641 2876 2471 -217 242 -227 C ATOM 3160 C PRO B 144 83.312 24.305 -0.818 1.00 20.38 C ANISOU 3160 C PRO B 144 2776 2913 2053 -320 167 -309 C ATOM 3161 O PRO B 144 83.009 23.757 -1.890 1.00 19.83 O ANISOU 3161 O PRO B 144 2663 2680 2192 -388 135 -361 O ATOM 3162 CB PRO B 144 85.605 25.064 -0.027 1.00 21.73 C ANISOU 3162 CB PRO B 144 2549 3038 2669 -129 254 -400 C ATOM 3163 CG PRO B 144 86.032 26.354 0.603 1.00 22.09 C ANISOU 3163 CG PRO B 144 2496 3044 2853 -195 129 -377 C ATOM 3164 CD PRO B 144 84.741 27.038 1.025 1.00 21.28 C ANISOU 3164 CD PRO B 144 2389 2848 2850 -271 107 -327 C ATOM 3165 N ASN B 145 82.759 23.936 0.343 1.00 18.04 N ANISOU 3165 N ASN B 145 2044 2629 2182 -254 243 -430 N ATOM 3166 CA ASN B 145 81.783 22.854 0.376 1.00 16.85 C ANISOU 3166 CA ASN B 145 2265 2251 1887 -134 355 -82 C ATOM 3167 C ASN B 145 80.524 23.203 -0.401 1.00 16.72 C ANISOU 3167 C ASN B 145 2464 1970 1918 6 212 -142 C ATOM 3168 O ASN B 145 79.922 22.351 -1.075 1.00 17.12 O ANISOU 3168 O ASN B 145 2345 2289 1871 -54 703 -569 O ATOM 3169 CB ASN B 145 81.451 22.397 1.792 1.00 16.06 C ANISOU 3169 CB ASN B 145 1839 2550 1712 -121 356 -286 C ATOM 3170 CG ASN B 145 82.503 21.460 2.348 1.00 18.24 C ANISOU 3170 CG ASN B 145 2100 2769 2060 -16 242 -77 C ATOM 3171 OD1 ASN B 145 83.274 20.867 1.573 1.00 20.45 O ANISOU 3171 OD1 ASN B 145 2171 3176 2422 110 66 -562 O ATOM 3172 ND2 ASN B 145 82.524 21.325 3.673 1.00 19.33 N ANISOU 3172 ND2 ASN B 145 2365 2920 2059 -32 217 -91 N ATOM 3173 N VAL B 146 80.077 24.455 -0.290 1.00 17.62 N ANISOU 3173 N VAL B 146 2103 2143 2448 155 140 -218 N ATOM 3174 CA VAL B 146 78.889 24.870 -1.038 1.00 17.94 C ANISOU 3174 CA VAL B 146 2592 2372 1852 245 -73 -198 C ATOM 3175 C VAL B 146 79.135 24.689 -2.535 1.00 18.55 C ANISOU 3175 C VAL B 146 2453 2631 1965 -94 274 -115 C ATOM 3176 O VAL B 146 78.282 24.149 -3.254 1.00 18.72 O ANISOU 3176 O VAL B 146 2190 2745 2178 51 480 -514 O ATOM 3177 CB VAL B 146 78.478 26.304 -0.672 1.00 18.00 C ANISOU 3177 CB VAL B 146 2774 2384 1679 212 142 -183 C ATOM 3178 CG1 VAL B 146 77.441 26.810 -1.665 1.00 20.45 C ANISOU 3178 CG1 VAL B 146 3123 2268 2381 412 -86 85 C ATOM 3179 CG2 VAL B 146 77.961 26.379 0.764 1.00 20.16 C ANISOU 3179 CG2 VAL B 146 2963 2860 1839 262 360 -282 C ATOM 3180 N PHE B 147 80.313 25.067 -3.019 1.00 19.31 N ANISOU 3180 N PHE B 147 2667 2506 2164 -68 561 -147 N ATOM 3181 CA PHE B 147 80.636 24.902 -4.441 1.00 19.56 C ANISOU 3181 CA PHE B 147 2877 2467 2087 -76 372 -165 C ATOM 3182 C PHE B 147 80.693 23.429 -4.830 1.00 17.04 C ANISOU 3182 C PHE B 147 2239 2258 1977 -57 403 152 C ATOM 3183 O PHE B 147 80.217 23.061 -5.913 1.00 17.49 O ANISOU 3183 O PHE B 147 2370 2165 2110 132 817 -597 O ATOM 3184 CB PHE B 147 81.928 25.634 -4.788 1.00 21.62 C ANISOU 3184 CB PHE B 147 2894 2694 2627 -187 340 -166 C ATOM 3185 CG PHE B 147 82.241 25.654 -6.265 1.00 23.56 C ANISOU 3185 CG PHE B 147 3291 3050 2610 -193 212 64 C ATOM 3186 CD1 PHE B 147 81.333 26.149 -7.181 1.00 24.57 C ANISOU 3186 CD1 PHE B 147 3167 3127 3042 32 259 196 C ATOM 3187 CD2 PHE B 147 83.452 25.166 -6.722 1.00 26.34 C ANISOU 3187 CD2 PHE B 147 3391 3469 3147 -33 187 -41 C ATOM 3188 CE1 PHE B 147 81.625 26.165 -8.532 1.00 26.30 C ANISOU 3188 CE1 PHE B 147 3428 3505 3059 97 98 146 C ATOM 3189 CE2 PHE B 147 83.754 25.182 -8.074 1.00 26.47 C ANISOU 3189 CE2 PHE B 147 3467 3516 3072 -116 44 101 C ATOM 3190 CZ PHE B 147 82.838 25.680 -8.974 1.00 25.96 C ANISOU 3190 CZ PHE B 147 3317 3322 3226 27 132 133 C ATOM 3191 N ARG B 148 81.258 22.576 -3.980 1.00 16.36 N ANISOU 3191 N ARG B 148 2251 1958 2005 89 319 -159 N ATOM 3192 CA ARG B 148 81.262 21.142 -4.266 1.00 14.76 C ANISOU 3192 CA ARG B 148 1954 1904 1749 59 458 24 C ATOM 3193 C ARG B 148 79.843 20.630 -4.453 1.00 14.53 C ANISOU 3193 C ARG B 148 2087 1881 1552 4 271 -332 C ATOM 3194 O ARG B 148 79.541 19.853 -5.364 1.00 14.79 O ANISOU 3194 O ARG B 148 2427 1872 1319 -16 509 -311 O ATOM 3195 CB ARG B 148 81.941 20.353 -3.149 1.00 15.29 C ANISOU 3195 CB ARG B 148 1960 2133 1715 430 371 -216 C ATOM 3196 CG ARG B 148 83.427 20.631 -2.981 1.00 17.11 C ANISOU 3196 CG ARG B 148 2206 2331 1966 -169 331 -237 C ATOM 3197 CD ARG B 148 83.959 19.754 -1.856 1.00 19.75 C ANISOU 3197 CD ARG B 148 2399 2829 2277 206 60 -201 C ATOM 3198 NE ARG B 148 85.393 19.806 -1.711 1.00 22.38 N ANISOU 3198 NE ARG B 148 2390 3285 2829 85 207 -475 N ATOM 3199 CZ ARG B 148 86.098 20.592 -0.920 1.00 24.27 C ANISOU 3199 CZ ARG B 148 2835 3294 3091 55 24 -556 C ATOM 3200 NH1 ARG B 148 85.519 21.473 -0.114 1.00 24.69 N ANISOU 3200 NH1 ARG B 148 2713 3436 3232 280 256 -398 N ATOM 3201 NH2 ARG B 148 87.421 20.477 -0.940 1.00 27.98 N ANISOU 3201 NH2 ARG B 148 2872 3969 3791 36 60 -529 N ATOM 3202 N MET B 149 78.960 20.984 -3.514 1.00 15.04 N ANISOU 3202 N MET B 149 1980 1813 1920 28 441 -340 N ATOM 3203 CA MET B 149 77.577 20.529 -3.596 1.00 14.98 C ANISOU 3203 CA MET B 149 1900 2218 1575 153 360 -355 C ATOM 3204 C MET B 149 76.973 20.930 -4.939 1.00 14.60 C ANISOU 3204 C MET B 149 1777 2072 1699 46 412 -61 C ATOM 3205 O MET B 149 76.281 20.140 -5.580 1.00 16.42 O ANISOU 3205 O MET B 149 2090 2414 1734 125 363 -456 O ATOM 3206 CB MET B 149 76.771 21.091 -2.414 1.00 14.54 C ANISOU 3206 CB MET B 149 1882 1993 1650 236 374 -336 C ATOM 3207 CG MET B 149 77.141 20.458 -1.074 1.00 15.36 C ANISOU 3207 CG MET B 149 1965 2185 1685 356 546 -208 C ATOM 3208 SD MET B 149 76.247 21.245 0.277 1.00 16.06 S ANISOU 3208 SD MET B 149 2214 2702 1185 504 329 -165 S ATOM 3209 CE MET B 149 77.535 21.929 1.302 1.00 19.13 C ANISOU 3209 CE MET B 149 2232 2995 2041 -129 403 -267 C ATOM 3210 N ARG B 150 77.200 22.176 -5.350 1.00 16.60 N ANISOU 3210 N ARG B 150 2210 2145 1954 358 447 237 N ATOM 3211 CA ARG B 150 76.632 22.647 -6.612 1.00 16.77 C ANISOU 3211 CA ARG B 150 2280 2306 1787 373 362 12 C ATOM 3212 C ARG B 150 77.264 21.971 -7.828 1.00 16.46 C ANISOU 3212 C ARG B 150 2213 2193 1848 362 310 -5 C ATOM 3213 O ARG B 150 76.537 21.627 -8.764 1.00 16.29 O ANISOU 3213 O ARG B 150 2569 1937 1684 242 322 110 O ATOM 3214 CB ARG B 150 76.697 24.182 -6.678 1.00 20.18 C ANISOU 3214 CB ARG B 150 3077 2360 2230 271 409 95 C ATOM 3215 CG ARG B 150 75.752 24.767 -5.615 1.00 22.21 C ANISOU 3215 CG ARG B 150 3119 2731 2588 402 460 -161 C ATOM 3216 CD ARG B 150 75.742 26.284 -5.568 1.00 26.25 C ANISOU 3216 CD ARG B 150 3757 2821 3397 101 312 -39 C ATOM 3217 NE ARG B 150 74.670 26.774 -4.691 1.00 28.65 N ANISOU 3217 NE ARG B 150 3712 3360 3815 185 396 -118 N ATOM 3218 CZ ARG B 150 74.711 27.851 -3.921 1.00 29.06 C ANISOU 3218 CZ ARG B 150 3819 3373 3849 -59 179 -84 C ATOM 3219 NH1 ARG B 150 75.796 28.612 -3.873 1.00 28.89 N ANISOU 3219 NH1 ARG B 150 3937 3337 3702 -142 130 -19 N ATOM 3220 NH2 ARG B 150 73.659 28.183 -3.170 1.00 29.52 N ANISOU 3220 NH2 ARG B 150 4034 3250 3932 37 292 -51 N ATOM 3221 N LEU B 151 78.567 21.705 -7.780 1.00 16.40 N ANISOU 3221 N LEU B 151 2230 2046 1956 415 296 90 N ATOM 3222 CA LEU B 151 79.198 20.976 -8.892 1.00 16.73 C ANISOU 3222 CA LEU B 151 2465 2223 1669 114 135 -109 C ATOM 3223 C LEU B 151 78.529 19.619 -9.057 1.00 14.52 C ANISOU 3223 C LEU B 151 2097 2060 1358 302 101 46 C ATOM 3224 O LEU B 151 78.464 19.038 -10.136 1.00 15.98 O ANISOU 3224 O LEU B 151 2457 2432 1183 497 11 135 O ATOM 3225 CB LEU B 151 80.682 20.729 -8.627 1.00 16.40 C ANISOU 3225 CB LEU B 151 2380 2078 1774 106 357 -98 C ATOM 3226 CG LEU B 151 81.633 21.911 -8.825 1.00 17.72 C ANISOU 3226 CG LEU B 151 2485 2227 2022 -58 232 -195 C ATOM 3227 CD1 LEU B 151 82.986 21.626 -8.201 1.00 17.96 C ANISOU 3227 CD1 LEU B 151 2402 2383 2041 -138 254 -213 C ATOM 3228 CD2 LEU B 151 81.780 22.229 -10.305 1.00 19.39 C ANISOU 3228 CD2 LEU B 151 2859 2324 2184 115 190 192 C ATOM 3229 N MET B 152 78.128 19.006 -7.937 1.00 14.21 N ANISOU 3229 N MET B 152 2305 1799 1293 176 114 -64 N ATOM 3230 CA MET B 152 77.497 17.704 -7.926 1.00 14.01 C ANISOU 3230 CA MET B 152 2409 1895 1020 62 106 98 C ATOM 3231 C MET B 152 76.007 17.735 -8.187 1.00 12.23 C ANISOU 3231 C MET B 152 2432 1593 622 -40 -12 61 C ATOM 3232 O MET B 152 75.357 16.690 -8.144 1.00 15.73 O ANISOU 3232 O MET B 152 2661 1824 1493 -257 182 112 O ATOM 3233 CB MET B 152 77.782 16.950 -6.624 1.00 14.48 C ANISOU 3233 CB MET B 152 2636 1809 1056 -120 -310 2 C ATOM 3234 CG MET B 152 79.270 16.632 -6.543 1.00 17.80 C ANISOU 3234 CG MET B 152 2685 2307 1773 -104 -404 65 C ATOM 3235 SD MET B 152 79.552 15.990 -4.864 1.00 23.34 S ANISOU 3235 SD MET B 152 3326 2652 2890 -354 -668 1391 S ATOM 3236 CE AMET B 152 81.251 15.498 -5.157 0.70 20.78 C ANISOU 3236 CE AMET B 152 3762 1831 2304 -236 277 508 C ATOM 3237 CE BMET B 152 79.344 17.476 -3.894 0.30 25.57 C ANISOU 3237 CE BMET B 152 3157 3504 3053 -244 -308 691 C ATOM 3238 N GLY B 153 75.494 18.900 -8.571 1.00 14.24 N ANISOU 3238 N GLY B 153 2046 2154 1210 527 276 243 N ATOM 3239 CA GLY B 153 74.109 19.016 -8.988 1.00 14.43 C ANISOU 3239 CA GLY B 153 2070 2167 1247 616 179 399 C ATOM 3240 C GLY B 153 73.098 19.237 -7.885 1.00 15.34 C ANISOU 3240 C GLY B 153 1984 2459 1385 374 253 318 C ATOM 3241 O GLY B 153 71.894 19.249 -8.173 1.00 17.33 O ANISOU 3241 O GLY B 153 1911 3070 1604 227 393 -178 O ATOM 3242 N ALA B 154 73.526 19.402 -6.641 1.00 15.03 N ANISOU 3242 N ALA B 154 1928 2365 1417 413 345 -27 N ATOM 3243 CA ALA B 154 72.567 19.630 -5.552 1.00 14.60 C ANISOU 3243 CA ALA B 154 1923 2341 1282 336 356 259 C ATOM 3244 C ALA B 154 72.203 21.099 -5.415 1.00 16.40 C ANISOU 3244 C ALA B 154 2074 2335 1820 218 376 52 C ATOM 3245 O ALA B 154 73.007 21.986 -5.729 1.00 19.22 O ANISOU 3245 O ALA B 154 2057 2429 2817 236 806 -21 O ATOM 3246 CB ALA B 154 73.183 19.140 -4.248 1.00 15.30 C ANISOU 3246 CB ALA B 154 2124 2521 1167 596 282 -32 C ATOM 3247 N GLU B 155 70.991 21.356 -4.925 1.00 15.54 N ANISOU 3247 N GLU B 155 1981 2274 1650 246 234 66 N ATOM 3248 CA GLU B 155 70.527 22.722 -4.675 1.00 16.90 C ANISOU 3248 CA GLU B 155 2373 2286 1763 277 -37 -38 C ATOM 3249 C GLU B 155 70.889 23.075 -3.235 1.00 16.95 C ANISOU 3249 C GLU B 155 2574 2228 1637 64 103 84 C ATOM 3250 O GLU B 155 70.551 22.263 -2.368 1.00 20.30 O ANISOU 3250 O GLU B 155 3279 2520 1915 -433 128 215 O ATOM 3251 CB GLU B 155 69.010 22.769 -4.837 1.00 17.59 C ANISOU 3251 CB GLU B 155 2371 2617 1697 337 91 -104 C ATOM 3252 CG GLU B 155 68.365 24.114 -4.534 1.00 20.83 C ANISOU 3252 CG GLU B 155 2925 2667 2322 581 23 -17 C ATOM 3253 CD GLU B 155 66.858 24.070 -4.665 1.00 22.96 C ANISOU 3253 CD GLU B 155 2949 3004 2769 302 94 -24 C ATOM 3254 OE1 GLU B 155 66.252 22.982 -4.767 1.00 24.34 O ANISOU 3254 OE1 GLU B 155 2166 3338 3742 297 -278 277 O ATOM 3255 OE2 GLU B 155 66.242 25.163 -4.675 1.00 27.95 O ANISOU 3255 OE2 GLU B 155 3346 3667 3606 896 80 344 O ATOM 3256 N VAL B 156 71.562 24.185 -2.979 1.00 15.41 N ANISOU 3256 N VAL B 156 2300 2243 1312 198 56 -17 N ATOM 3257 CA VAL B 156 71.920 24.557 -1.599 1.00 15.69 C ANISOU 3257 CA VAL B 156 2309 2351 1301 308 22 113 C ATOM 3258 C VAL B 156 71.035 25.728 -1.205 1.00 18.21 C ANISOU 3258 C VAL B 156 2925 2161 1834 417 321 289 C ATOM 3259 O VAL B 156 70.993 26.749 -1.903 1.00 18.88 O ANISOU 3259 O VAL B 156 3152 2136 1887 409 304 332 O ATOM 3260 CB VAL B 156 73.414 24.891 -1.495 1.00 16.88 C ANISOU 3260 CB VAL B 156 2382 2134 1898 203 -78 161 C ATOM 3261 CG1 VAL B 156 73.775 25.301 -0.082 1.00 20.24 C ANISOU 3261 CG1 VAL B 156 2558 2891 2241 78 -289 -223 C ATOM 3262 CG2 VAL B 156 74.236 23.665 -1.901 1.00 17.04 C ANISOU 3262 CG2 VAL B 156 1925 2536 2012 265 3 7 C ATOM 3263 N ILE B 157 70.271 25.567 -0.132 1.00 16.57 N ANISOU 3263 N ILE B 157 2624 1972 1698 455 89 462 N ATOM 3264 CA ILE B 157 69.325 26.566 0.338 1.00 17.13 C ANISOU 3264 CA ILE B 157 2656 2104 1749 407 85 261 C ATOM 3265 C ILE B 157 69.718 27.130 1.689 1.00 17.01 C ANISOU 3265 C ILE B 157 2721 1934 1810 208 212 158 C ATOM 3266 O ILE B 157 69.601 26.423 2.703 1.00 17.72 O ANISOU 3266 O ILE B 157 2749 2032 1952 516 328 346 O ATOM 3267 CB ILE B 157 67.930 25.915 0.474 1.00 17.15 C ANISOU 3267 CB ILE B 157 2569 2157 1790 428 -10 108 C ATOM 3268 CG1 ILE B 157 67.537 25.247 -0.843 1.00 19.02 C ANISOU 3268 CG1 ILE B 157 2704 2662 1863 -96 -26 78 C ATOM 3269 CG2 ILE B 157 66.902 26.949 0.903 1.00 19.08 C ANISOU 3269 CG2 ILE B 157 2596 2426 2227 604 98 196 C ATOM 3270 CD1 ILE B 157 66.331 24.340 -0.792 1.00 18.92 C ANISOU 3270 CD1 ILE B 157 2417 2866 1904 0 83 109 C ATOM 3271 N PRO B 158 70.172 28.366 1.734 1.00 17.11 N ANISOU 3271 N PRO B 158 3023 1884 1594 187 -90 497 N ATOM 3272 CA PRO B 158 70.544 29.001 2.987 1.00 18.67 C ANISOU 3272 CA PRO B 158 2861 2293 1938 29 166 -11 C ATOM 3273 C PRO B 158 69.346 29.175 3.904 1.00 18.19 C ANISOU 3273 C PRO B 158 2485 2464 1963 134 -16 218 C ATOM 3274 O PRO B 158 68.237 29.478 3.459 1.00 18.69 O ANISOU 3274 O PRO B 158 2439 2515 2147 443 187 83 O ATOM 3275 CB PRO B 158 71.095 30.361 2.558 1.00 19.31 C ANISOU 3275 CB PRO B 158 3071 2236 2028 167 77 223 C ATOM 3276 CG PRO B 158 71.436 30.189 1.114 1.00 19.21 C ANISOU 3276 CG PRO B 158 3172 2138 1990 -39 42 300 C ATOM 3277 CD PRO B 158 70.376 29.263 0.558 1.00 16.62 C ANISOU 3277 CD PRO B 158 3028 1798 1488 46 246 312 C ATOM 3278 N VAL B 159 69.559 28.978 5.199 1.00 18.28 N ANISOU 3278 N VAL B 159 2704 2337 1904 346 61 19 N ATOM 3279 CA VAL B 159 68.526 29.117 6.219 1.00 17.59 C ANISOU 3279 CA VAL B 159 2593 2035 2056 3 125 159 C ATOM 3280 C VAL B 159 68.852 30.293 7.126 1.00 17.00 C ANISOU 3280 C VAL B 159 2535 2090 1832 230 171 106 C ATOM 3281 O VAL B 159 69.905 30.289 7.755 1.00 17.04 O ANISOU 3281 O VAL B 159 2869 2083 1522 45 -14 -100 O ATOM 3282 CB VAL B 159 68.414 27.808 7.019 1.00 15.41 C ANISOU 3282 CB VAL B 159 2351 2148 1357 193 191 90 C ATOM 3283 CG1 VAL B 159 67.414 27.983 8.154 1.00 17.23 C ANISOU 3283 CG1 VAL B 159 2657 2246 1643 307 419 -23 C ATOM 3284 CG2 VAL B 159 67.983 26.670 6.102 1.00 17.54 C ANISOU 3284 CG2 VAL B 159 2661 2257 1747 29 -53 57 C ATOM 3285 N HIS B 160 68.003 31.317 7.158 1.00 19.20 N ANISOU 3285 N HIS B 160 2833 2231 2232 417 267 204 N ATOM 3286 CA HIS B 160 68.293 32.537 7.896 1.00 21.17 C ANISOU 3286 CA HIS B 160 3131 2601 2310 246 197 -35 C ATOM 3287 C HIS B 160 67.544 32.661 9.216 1.00 20.25 C ANISOU 3287 C HIS B 160 2814 2545 2333 65 175 9 C ATOM 3288 O HIS B 160 67.787 33.634 9.935 1.00 22.91 O ANISOU 3288 O HIS B 160 3724 2590 2390 -63 383 -25 O ATOM 3289 CB HIS B 160 67.875 33.752 7.040 1.00 24.00 C ANISOU 3289 CB HIS B 160 3560 2783 2777 251 192 258 C ATOM 3290 CG HIS B 160 68.625 33.842 5.747 1.00 24.96 C ANISOU 3290 CG HIS B 160 3552 2930 3002 265 380 195 C ATOM 3291 ND1 HIS B 160 69.845 34.461 5.639 1.00 26.13 N ANISOU 3291 ND1 HIS B 160 3501 3138 3289 270 259 96 N ATOM 3292 CD2 HIS B 160 68.303 33.382 4.513 1.00 27.93 C ANISOU 3292 CD2 HIS B 160 3982 3394 3236 67 206 111 C ATOM 3293 CE1 HIS B 160 70.261 34.375 4.379 1.00 26.59 C ANISOU 3293 CE1 HIS B 160 3683 3276 3146 128 130 295 C ATOM 3294 NE2 HIS B 160 69.346 33.733 3.680 1.00 26.67 N ANISOU 3294 NE2 HIS B 160 3934 2993 3205 60 243 72 N ATOM 3295 N SER B 161 66.669 31.714 9.496 1.00 19.29 N ANISOU 3295 N SER B 161 2835 2527 1967 169 365 97 N ATOM 3296 CA SER B 161 65.908 31.728 10.739 1.00 18.75 C ANISOU 3296 CA SER B 161 2462 2487 2174 108 385 -4 C ATOM 3297 C SER B 161 66.788 31.355 11.921 1.00 18.09 C ANISOU 3297 C SER B 161 2469 2222 2182 186 403 8 C ATOM 3298 O SER B 161 67.837 30.732 11.786 1.00 17.27 O ANISOU 3298 O SER B 161 2508 1939 2114 249 96 463 O ATOM 3299 CB SER B 161 64.730 30.754 10.656 1.00 20.81 C ANISOU 3299 CB SER B 161 2585 2621 2699 13 135 -174 C ATOM 3300 OG SER B 161 65.158 29.480 10.190 1.00 21.27 O ANISOU 3300 OG SER B 161 2391 2751 2940 312 296 -36 O ATOM 3301 N GLY B 162 66.330 31.764 13.104 1.00 18.73 N ANISOU 3301 N GLY B 162 2715 2472 1930 193 227 76 N ATOM 3302 CA GLY B 162 67.011 31.470 14.350 1.00 18.54 C ANISOU 3302 CA GLY B 162 2650 2480 1915 163 161 -15 C ATOM 3303 C GLY B 162 68.471 31.867 14.353 1.00 18.47 C ANISOU 3303 C GLY B 162 2633 2490 1895 214 219 -16 C ATOM 3304 O GLY B 162 68.802 33.011 14.047 1.00 21.98 O ANISOU 3304 O GLY B 162 3468 2507 2374 93 382 -21 O ATOM 3305 N SER B 163 69.354 30.934 14.698 1.00 18.40 N ANISOU 3305 N SER B 163 2664 2345 1980 187 1 -220 N ATOM 3306 CA SER B 163 70.779 31.235 14.740 1.00 19.37 C ANISOU 3306 CA SER B 163 2701 2570 2090 90 167 -117 C ATOM 3307 C SER B 163 71.462 31.066 13.384 1.00 19.71 C ANISOU 3307 C SER B 163 2914 2567 2009 75 166 64 C ATOM 3308 O SER B 163 72.670 31.282 13.307 1.00 21.62 O ANISOU 3308 O SER B 163 3053 2840 2322 -168 236 -308 O ATOM 3309 CB SER B 163 71.475 30.413 15.825 1.00 20.74 C ANISOU 3309 CB SER B 163 3153 2493 2236 125 -135 -207 C ATOM 3310 OG SER B 163 71.271 29.017 15.675 1.00 23.57 O ANISOU 3310 OG SER B 163 3289 2556 3112 -115 -480 -22 O ATOM 3311 N ALA B 164 70.723 30.705 12.346 1.00 17.68 N ANISOU 3311 N ALA B 164 2811 1979 1929 15 322 61 N ATOM 3312 CA ALA B 164 71.275 30.543 11.005 1.00 17.30 C ANISOU 3312 CA ALA B 164 2589 2056 1927 -44 248 255 C ATOM 3313 C ALA B 164 72.440 29.572 10.978 1.00 16.05 C ANISOU 3313 C ALA B 164 2452 1943 1706 -177 33 -78 C ATOM 3314 O ALA B 164 73.438 29.784 10.286 1.00 17.07 O ANISOU 3314 O ALA B 164 2582 2221 1684 -458 8 -46 O ATOM 3315 CB ALA B 164 71.655 31.898 10.415 1.00 17.20 C ANISOU 3315 CB ALA B 164 2821 1767 1949 4 164 44 C ATOM 3316 N THR B 165 72.320 28.507 11.773 1.00 15.89 N ANISOU 3316 N THR B 165 2239 1842 1955 -148 -234 16 N ATOM 3317 CA THR B 165 73.362 27.484 11.807 1.00 15.71 C ANISOU 3317 CA THR B 165 2253 1863 1854 -90 16 -31 C ATOM 3318 C THR B 165 72.742 26.094 11.748 1.00 15.00 C ANISOU 3318 C THR B 165 2186 1815 1697 -42 8 174 C ATOM 3319 O THR B 165 71.588 25.957 11.294 1.00 15.66 O ANISOU 3319 O THR B 165 2297 2203 1450 -10 -73 403 O ATOM 3320 CB ATHR B 165 74.286 27.539 13.036 0.50 15.42 C ANISOU 3320 CB ATHR B 165 2223 2039 1598 11 194 62 C ATOM 3321 OG1ATHR B 165 73.522 27.465 14.255 0.50 11.50 O ANISOU 3321 OG1ATHR B 165 1873 1460 1035 325 -203 -378 O ATOM 3322 CG2ATHR B 165 75.154 28.782 13.057 0.50 17.82 C ANISOU 3322 CG2ATHR B 165 2187 2284 2299 -77 82 -41 C ATOM 3323 CB BTHR B 165 74.346 27.774 12.941 0.50 16.27 C ANISOU 3323 CB BTHR B 165 2124 2037 2023 37 -63 70 C ATOM 3324 OG1BTHR B 165 74.685 29.177 12.889 0.50 21.23 O ANISOU 3324 OG1BTHR B 165 2924 2146 2998 26 2 -10 O ATOM 3325 CG2BTHR B 165 75.614 26.962 12.763 0.50 12.71 C ANISOU 3325 CG2BTHR B 165 2039 1550 1241 -158 217 111 C ATOM 3326 N LEU B 166 73.449 25.051 12.198 1.00 14.32 N ANISOU 3326 N LEU B 166 2691 1558 1192 97 310 -16 N ATOM 3327 CA LEU B 166 72.980 23.688 11.959 1.00 14.93 C ANISOU 3327 CA LEU B 166 2263 1698 1713 -27 112 56 C ATOM 3328 C LEU B 166 71.605 23.376 12.501 1.00 15.55 C ANISOU 3328 C LEU B 166 2428 2139 1339 -203 231 -79 C ATOM 3329 O LEU B 166 70.782 22.785 11.790 1.00 15.79 O ANISOU 3329 O LEU B 166 2623 1857 1518 101 -61 -155 O ATOM 3330 CB LEU B 166 73.993 22.673 12.493 1.00 13.77 C ANISOU 3330 CB LEU B 166 2296 1703 1231 -39 -42 -71 C ATOM 3331 CG LEU B 166 73.642 21.191 12.386 1.00 15.60 C ANISOU 3331 CG LEU B 166 2486 1682 1759 79 -89 -216 C ATOM 3332 CD1 LEU B 166 73.366 20.754 10.950 1.00 17.56 C ANISOU 3332 CD1 LEU B 166 2430 2480 1762 66 4 -384 C ATOM 3333 CD2 LEU B 166 74.760 20.327 12.969 1.00 17.51 C ANISOU 3333 CD2 LEU B 166 2523 2513 1619 276 -254 -208 C ATOM 3334 N LYS B 167 71.345 23.722 13.764 1.00 15.31 N ANISOU 3334 N LYS B 167 2277 2123 1417 -170 115 -397 N ATOM 3335 CA LYS B 167 70.024 23.375 14.300 1.00 14.66 C ANISOU 3335 CA LYS B 167 2308 2252 1009 22 155 93 C ATOM 3336 C LYS B 167 68.925 23.983 13.445 1.00 13.34 C ANISOU 3336 C LYS B 167 2285 1965 817 -62 213 50 C ATOM 3337 O LYS B 167 67.854 23.404 13.269 1.00 16.11 O ANISOU 3337 O LYS B 167 2400 2424 1295 -195 13 -86 O ATOM 3338 CB LYS B 167 69.892 23.793 15.770 1.00 14.28 C ANISOU 3338 CB LYS B 167 2454 1904 1068 -59 35 -29 C ATOM 3339 CG LYS B 167 69.692 25.280 16.032 1.00 15.54 C ANISOU 3339 CG LYS B 167 2391 2017 1497 26 271 -207 C ATOM 3340 CD LYS B 167 69.534 25.545 17.528 1.00 17.11 C ANISOU 3340 CD LYS B 167 2484 2570 1449 89 119 -187 C ATOM 3341 CE LYS B 167 69.383 27.037 17.791 1.00 18.22 C ANISOU 3341 CE LYS B 167 2400 2638 1884 339 102 -245 C ATOM 3342 NZ LYS B 167 68.165 27.600 17.142 1.00 19.07 N ANISOU 3342 NZ LYS B 167 2493 3000 1751 169 -205 -376 N ATOM 3343 N ASP B 168 69.154 25.187 12.931 1.00 14.10 N ANISOU 3343 N ASP B 168 2388 1917 1054 119 421 48 N ATOM 3344 CA ASP B 168 68.150 25.885 12.129 1.00 14.99 C ANISOU 3344 CA ASP B 168 2368 2057 1271 178 231 -130 C ATOM 3345 C ASP B 168 67.950 25.175 10.802 1.00 14.78 C ANISOU 3345 C ASP B 168 1846 2409 1361 79 -12 -178 C ATOM 3346 O ASP B 168 66.833 25.103 10.285 1.00 14.19 O ANISOU 3346 O ASP B 168 1808 2601 982 42 73 -188 O ATOM 3347 CB ASP B 168 68.594 27.345 11.988 1.00 16.49 C ANISOU 3347 CB ASP B 168 2543 2232 1491 -161 -40 -90 C ATOM 3348 CG ASP B 168 68.962 27.878 13.371 1.00 16.59 C ANISOU 3348 CG ASP B 168 2430 2323 1551 -99 287 -339 C ATOM 3349 OD1 ASP B 168 68.039 28.091 14.187 1.00 17.34 O ANISOU 3349 OD1 ASP B 168 2602 2340 1646 252 437 -40 O ATOM 3350 OD2 ASP B 168 70.163 28.037 13.619 1.00 16.77 O ANISOU 3350 OD2 ASP B 168 2366 2296 1710 -262 473 5 O ATOM 3351 N ALA B 169 69.041 24.636 10.253 1.00 14.62 N ANISOU 3351 N ALA B 169 2179 2421 956 123 312 10 N ATOM 3352 CA ALA B 169 68.944 23.848 9.021 1.00 14.75 C ANISOU 3352 CA ALA B 169 2227 2197 1181 -46 153 -77 C ATOM 3353 C ALA B 169 68.212 22.549 9.305 1.00 14.56 C ANISOU 3353 C ALA B 169 2286 2253 993 -97 87 -11 C ATOM 3354 O ALA B 169 67.414 22.084 8.476 1.00 16.03 O ANISOU 3354 O ALA B 169 2081 2740 1268 21 62 -212 O ATOM 3355 CB ALA B 169 70.335 23.621 8.471 1.00 16.09 C ANISOU 3355 CB ALA B 169 2247 2446 1419 242 115 76 C ATOM 3356 N CYS B 170 68.410 21.967 10.497 1.00 12.95 N ANISOU 3356 N CYS B 170 2218 1954 748 122 513 -276 N ATOM 3357 CA CYS B 170 67.688 20.777 10.899 1.00 14.49 C ANISOU 3357 CA CYS B 170 2275 1985 1244 70 295 -101 C ATOM 3358 C CYS B 170 66.188 21.083 10.915 1.00 14.72 C ANISOU 3358 C CYS B 170 2311 1905 1377 215 184 -11 C ATOM 3359 O CYS B 170 65.377 20.318 10.405 1.00 15.25 O ANISOU 3359 O CYS B 170 2563 1594 1639 132 360 -51 O ATOM 3360 CB CYS B 170 68.091 20.309 12.298 1.00 15.06 C ANISOU 3360 CB CYS B 170 2030 2023 1668 -28 -179 146 C ATOM 3361 SG CYS B 170 69.726 19.540 12.379 1.00 14.55 S ANISOU 3361 SG CYS B 170 2258 2096 1175 171 -59 192 S ATOM 3362 N ASN B 171 65.795 22.214 11.523 1.00 15.37 N ANISOU 3362 N ASN B 171 2282 1995 1564 348 89 -99 N ATOM 3363 CA ASN B 171 64.388 22.580 11.570 1.00 14.28 C ANISOU 3363 CA ASN B 171 2047 2098 1280 -39 40 18 C ATOM 3364 C ASN B 171 63.815 22.720 10.147 1.00 13.72 C ANISOU 3364 C ASN B 171 1678 2316 1218 -7 173 -63 C ATOM 3365 O ASN B 171 62.716 22.235 9.911 1.00 15.23 O ANISOU 3365 O ASN B 171 1872 2513 1401 -220 193 -257 O ATOM 3366 CB ASN B 171 64.117 23.914 12.270 1.00 16.04 C ANISOU 3366 CB ASN B 171 2331 2289 1473 98 40 -167 C ATOM 3367 CG ASN B 171 64.687 24.004 13.666 1.00 15.09 C ANISOU 3367 CG ASN B 171 2256 1852 1627 -124 -111 -98 C ATOM 3368 OD1 ASN B 171 64.826 22.967 14.324 1.00 16.50 O ANISOU 3368 OD1 ASN B 171 2772 2225 1274 -189 -18 91 O ATOM 3369 ND2 ASN B 171 65.022 25.223 14.066 1.00 14.66 N ANISOU 3369 ND2 ASN B 171 1873 1892 1806 133 146 -405 N ATOM 3370 N GLU B 172 64.556 23.397 9.275 1.00 14.64 N ANISOU 3370 N GLU B 172 1745 2599 1219 -254 97 -19 N ATOM 3371 CA GLU B 172 64.045 23.651 7.933 1.00 14.28 C ANISOU 3371 CA GLU B 172 2031 2178 1216 -59 119 -121 C ATOM 3372 C GLU B 172 63.890 22.364 7.143 1.00 14.50 C ANISOU 3372 C GLU B 172 2070 2018 1422 -19 -156 -79 C ATOM 3373 O GLU B 172 62.907 22.197 6.408 1.00 15.61 O ANISOU 3373 O GLU B 172 2263 2398 1270 360 -199 -381 O ATOM 3374 CB GLU B 172 64.958 24.644 7.193 1.00 15.07 C ANISOU 3374 CB GLU B 172 2117 2414 1193 -82 -61 230 C ATOM 3375 CG GLU B 172 64.273 25.216 5.959 1.00 16.90 C ANISOU 3375 CG GLU B 172 2493 2681 1248 239 -79 212 C ATOM 3376 CD GLU B 172 63.153 26.177 6.297 1.00 18.95 C ANISOU 3376 CD GLU B 172 2561 2826 1812 230 102 44 C ATOM 3377 OE1 GLU B 172 63.061 26.699 7.435 1.00 18.57 O ANISOU 3377 OE1 GLU B 172 2947 2408 1700 313 629 349 O ATOM 3378 OE2 GLU B 172 62.336 26.416 5.377 1.00 22.08 O ANISOU 3378 OE2 GLU B 172 2987 3539 1865 346 -96 56 O ATOM 3379 N ALA B 173 64.844 21.442 7.285 1.00 15.19 N ANISOU 3379 N ALA B 173 2416 2140 1214 164 -78 -144 N ATOM 3380 CA ALA B 173 64.722 20.155 6.606 1.00 14.67 C ANISOU 3380 CA ALA B 173 2230 2147 1199 287 -3 -172 C ATOM 3381 C ALA B 173 63.429 19.475 7.023 1.00 15.47 C ANISOU 3381 C ALA B 173 2097 2731 1048 172 -219 43 C ATOM 3382 O ALA B 173 62.711 18.913 6.194 1.00 16.52 O ANISOU 3382 O ALA B 173 2031 3100 1145 -29 -357 222 O ATOM 3383 CB ALA B 173 65.918 19.268 6.882 1.00 14.72 C ANISOU 3383 CB ALA B 173 2140 2172 1282 305 11 -362 C ATOM 3384 N LEU B 174 63.114 19.510 8.324 1.00 15.05 N ANISOU 3384 N LEU B 174 1967 2592 1159 10 87 22 N ATOM 3385 CA LEU B 174 61.890 18.898 8.836 1.00 14.84 C ANISOU 3385 CA LEU B 174 1899 2713 1028 48 9 233 C ATOM 3386 C LEU B 174 60.649 19.670 8.410 1.00 13.58 C ANISOU 3386 C LEU B 174 1909 2204 1046 -47 -11 37 C ATOM 3387 O LEU B 174 59.611 19.045 8.125 1.00 16.79 O ANISOU 3387 O LEU B 174 2030 2820 1529 -54 -478 -180 O ATOM 3388 CB LEU B 174 61.927 18.772 10.370 1.00 15.22 C ANISOU 3388 CB LEU B 174 2416 2360 1007 73 -77 181 C ATOM 3389 CG LEU B 174 62.907 17.705 10.894 1.00 16.63 C ANISOU 3389 CG LEU B 174 2529 2486 1303 243 -28 130 C ATOM 3390 CD1 LEU B 174 62.949 17.756 12.422 1.00 18.96 C ANISOU 3390 CD1 LEU B 174 2817 3066 1322 -30 20 101 C ATOM 3391 CD2 LEU B 174 62.534 16.315 10.416 1.00 16.90 C ANISOU 3391 CD2 LEU B 174 2275 2482 1665 290 -477 233 C ATOM 3392 N ARG B 175 60.754 20.996 8.299 1.00 14.34 N ANISOU 3392 N ARG B 175 1986 2186 1275 180 -102 20 N ATOM 3393 CA ARG B 175 59.622 21.775 7.796 1.00 15.03 C ANISOU 3393 CA ARG B 175 2058 2107 1544 154 -160 77 C ATOM 3394 C ARG B 175 59.310 21.362 6.359 1.00 14.76 C ANISOU 3394 C ARG B 175 1675 2473 1460 240 -148 125 C ATOM 3395 O ARG B 175 58.143 21.214 5.995 1.00 14.86 O ANISOU 3395 O ARG B 175 1888 2478 1280 -22 -270 -59 O ATOM 3396 CB ARG B 175 59.933 23.272 7.787 1.00 14.72 C ANISOU 3396 CB ARG B 175 2331 2270 991 -322 310 -94 C ATOM 3397 CG ARG B 175 59.986 23.851 9.199 1.00 13.96 C ANISOU 3397 CG ARG B 175 2327 1773 1205 71 -142 -243 C ATOM 3398 CD ARG B 175 60.167 25.363 9.135 1.00 14.16 C ANISOU 3398 CD ARG B 175 2140 1746 1496 70 -92 -202 C ATOM 3399 NE ARG B 175 60.330 25.928 10.472 1.00 15.65 N ANISOU 3399 NE ARG B 175 2405 2252 1289 152 -240 6 N ATOM 3400 CZ ARG B 175 61.449 26.456 10.945 1.00 14.23 C ANISOU 3400 CZ ARG B 175 2267 1796 1345 -10 125 92 C ATOM 3401 NH1 ARG B 175 62.554 26.541 10.210 1.00 15.07 N ANISOU 3401 NH1 ARG B 175 2146 2076 1505 250 97 215 N ATOM 3402 NH2 ARG B 175 61.451 26.906 12.206 1.00 16.08 N ANISOU 3402 NH2 ARG B 175 2540 2267 1304 192 90 51 N ATOM 3403 N ASP B 176 60.360 21.214 5.552 1.00 15.48 N ANISOU 3403 N ASP B 176 2150 2556 1176 531 -118 55 N ATOM 3404 CA ASP B 176 60.171 20.838 4.144 1.00 14.31 C ANISOU 3404 CA ASP B 176 1793 2389 1256 135 -175 -5 C ATOM 3405 C ASP B 176 59.607 19.435 4.078 1.00 13.41 C ANISOU 3405 C ASP B 176 1753 2397 945 159 -142 86 C ATOM 3406 O ASP B 176 58.601 19.215 3.402 1.00 16.53 O ANISOU 3406 O ASP B 176 1345 3405 1529 169 -94 15 O ATOM 3407 CB ASP B 176 61.522 20.940 3.448 1.00 15.02 C ANISOU 3407 CB ASP B 176 2044 2444 1220 160 44 97 C ATOM 3408 CG ASP B 176 61.531 20.560 1.983 1.00 16.00 C ANISOU 3408 CG ASP B 176 2091 2787 1202 53 -72 56 C ATOM 3409 OD1 ASP B 176 60.636 19.833 1.512 1.00 16.95 O ANISOU 3409 OD1 ASP B 176 2076 3352 1014 -276 121 163 O ATOM 3410 OD2 ASP B 176 62.486 21.017 1.318 1.00 16.81 O ANISOU 3410 OD2 ASP B 176 2177 3117 1093 184 18 105 O ATOM 3411 N TRP B 177 60.209 18.506 4.817 1.00 13.02 N ANISOU 3411 N TRP B 177 1909 2007 1030 318 203 47 N ATOM 3412 CA TRP B 177 59.736 17.123 4.775 1.00 13.18 C ANISOU 3412 CA TRP B 177 1709 2142 1156 116 -27 94 C ATOM 3413 C TRP B 177 58.273 17.050 5.182 1.00 13.94 C ANISOU 3413 C TRP B 177 1666 2451 1180 71 -147 -135 C ATOM 3414 O TRP B 177 57.551 16.217 4.666 1.00 15.24 O ANISOU 3414 O TRP B 177 2094 2727 971 -221 -121 -97 O ATOM 3415 CB TRP B 177 60.625 16.232 5.642 1.00 14.52 C ANISOU 3415 CB TRP B 177 2100 2130 1289 186 -136 155 C ATOM 3416 CG TRP B 177 60.666 14.787 5.265 1.00 13.30 C ANISOU 3416 CG TRP B 177 1750 2135 1170 -33 17 100 C ATOM 3417 CD1 TRP B 177 60.596 14.261 3.997 1.00 14.13 C ANISOU 3417 CD1 TRP B 177 2069 2090 1210 -114 -226 69 C ATOM 3418 CD2 TRP B 177 60.868 13.669 6.132 1.00 13.39 C ANISOU 3418 CD2 TRP B 177 1653 2010 1424 203 -140 38 C ATOM 3419 NE1 TRP B 177 60.709 12.900 4.035 1.00 14.99 N ANISOU 3419 NE1 TRP B 177 1942 2164 1590 248 -184 -18 N ATOM 3420 CE2 TRP B 177 60.885 12.502 5.345 1.00 14.36 C ANISOU 3420 CE2 TRP B 177 1800 2142 1515 -180 -151 -80 C ATOM 3421 CE3 TRP B 177 61.040 13.558 7.519 1.00 12.69 C ANISOU 3421 CE3 TRP B 177 1536 1904 1381 52 -55 -76 C ATOM 3422 CZ2 TRP B 177 61.068 11.235 5.884 1.00 14.94 C ANISOU 3422 CZ2 TRP B 177 1857 2274 1545 78 -460 -117 C ATOM 3423 CZ3 TRP B 177 61.220 12.295 8.051 1.00 14.77 C ANISOU 3423 CZ3 TRP B 177 1461 1973 2178 110 -291 134 C ATOM 3424 CH2 TRP B 177 61.233 11.156 7.245 1.00 14.71 C ANISOU 3424 CH2 TRP B 177 1750 2289 1550 246 -418 129 C ATOM 3425 N SER B 178 57.859 17.902 6.129 1.00 15.44 N ANISOU 3425 N SER B 178 2048 2721 1096 425 51 -43 N ATOM 3426 CA SER B 178 56.481 17.898 6.583 1.00 16.70 C ANISOU 3426 CA SER B 178 2038 2944 1362 156 29 -269 C ATOM 3427 C SER B 178 55.490 18.141 5.455 1.00 16.76 C ANISOU 3427 C SER B 178 1876 2791 1702 85 -36 40 C ATOM 3428 O SER B 178 54.311 17.790 5.584 1.00 17.92 O ANISOU 3428 O SER B 178 1792 3668 1348 134 -16 301 O ATOM 3429 CB SER B 178 56.256 18.913 7.714 1.00 16.90 C ANISOU 3429 CB SER B 178 1805 3411 1206 321 -30 -419 C ATOM 3430 OG SER B 178 57.113 18.617 8.817 1.00 19.53 O ANISOU 3430 OG SER B 178 2556 3413 1451 125 -374 -73 O ATOM 3431 N GLY B 179 55.943 18.698 4.341 1.00 17.08 N ANISOU 3431 N GLY B 179 1997 3289 1205 209 -64 -235 N ATOM 3432 CA GLY B 179 55.069 18.928 3.197 1.00 18.18 C ANISOU 3432 CA GLY B 179 1902 3453 1552 432 -194 -132 C ATOM 3433 C GLY B 179 55.459 18.091 1.989 1.00 18.58 C ANISOU 3433 C GLY B 179 1938 3294 1827 470 -177 -261 C ATOM 3434 O GLY B 179 54.648 17.900 1.069 1.00 21.90 O ANISOU 3434 O GLY B 179 2142 4303 1874 727 -388 -205 O ATOM 3435 N SER B 180 56.672 17.561 1.959 1.00 15.84 N ANISOU 3435 N SER B 180 2131 2910 979 613 -291 -196 N ATOM 3436 CA SER B 180 57.142 16.827 0.784 1.00 14.50 C ANISOU 3436 CA SER B 180 1894 2777 838 346 -280 -105 C ATOM 3437 C SER B 180 57.437 15.356 0.958 1.00 15.49 C ANISOU 3437 C SER B 180 1977 2841 1069 410 -420 141 C ATOM 3438 O SER B 180 57.960 14.730 0.011 1.00 16.06 O ANISOU 3438 O SER B 180 1672 3375 1056 756 -557 152 O ATOM 3439 CB SER B 180 58.436 17.519 0.315 1.00 16.04 C ANISOU 3439 CB SER B 180 2247 2962 886 13 -397 208 C ATOM 3440 OG SER B 180 59.468 17.278 1.259 1.00 16.84 O ANISOU 3440 OG SER B 180 1941 3524 933 290 -262 -61 O ATOM 3441 N TYR B 181 57.156 14.730 2.089 1.00 16.89 N ANISOU 3441 N TYR B 181 2362 2981 1075 334 -289 170 N ATOM 3442 CA TYR B 181 57.482 13.341 2.345 1.00 18.61 C ANISOU 3442 CA TYR B 181 2612 2697 1760 -40 -245 -34 C ATOM 3443 C TYR B 181 56.984 12.353 1.305 1.00 18.58 C ANISOU 3443 C TYR B 181 2503 2753 1804 191 -369 -84 C ATOM 3444 O TYR B 181 57.557 11.270 1.146 1.00 17.31 O ANISOU 3444 O TYR B 181 2577 2618 1382 194 -572 148 O ATOM 3445 CB TYR B 181 56.998 12.904 3.754 1.00 19.60 C ANISOU 3445 CB TYR B 181 2791 2990 1666 199 -221 -42 C ATOM 3446 CG TYR B 181 55.513 13.141 3.939 1.00 19.99 C ANISOU 3446 CG TYR B 181 2774 2993 1827 -166 199 -197 C ATOM 3447 CD1 TYR B 181 54.594 12.181 3.525 1.00 22.83 C ANISOU 3447 CD1 TYR B 181 2860 3342 2472 -254 -104 -160 C ATOM 3448 CD2 TYR B 181 55.032 14.322 4.473 1.00 20.64 C ANISOU 3448 CD2 TYR B 181 2691 2854 2296 190 101 148 C ATOM 3449 CE1 TYR B 181 53.232 12.387 3.670 1.00 22.14 C ANISOU 3449 CE1 TYR B 181 2809 3232 2373 -161 -81 -173 C ATOM 3450 CE2 TYR B 181 53.673 14.545 4.605 1.00 22.51 C ANISOU 3450 CE2 TYR B 181 2658 3447 2448 -128 164 -136 C ATOM 3451 CZ TYR B 181 52.780 13.572 4.209 1.00 22.47 C ANISOU 3451 CZ TYR B 181 2873 3346 2319 -121 46 -203 C ATOM 3452 OH TYR B 181 51.421 13.786 4.333 1.00 25.83 O ANISOU 3452 OH TYR B 181 2915 4391 2508 -106 -160 -98 O ATOM 3453 N GLU B 182 55.903 12.672 0.581 1.00 17.76 N ANISOU 3453 N GLU B 182 2269 2750 1727 98 -324 -345 N ATOM 3454 CA GLU B 182 55.457 11.654 -0.380 1.00 18.99 C ANISOU 3454 CA GLU B 182 2601 2817 1797 8 -361 -388 C ATOM 3455 C GLU B 182 56.478 11.466 -1.490 1.00 18.39 C ANISOU 3455 C GLU B 182 2195 2771 2019 85 -433 -232 C ATOM 3456 O GLU B 182 56.541 10.367 -2.057 1.00 22.26 O ANISOU 3456 O GLU B 182 3383 3010 2065 -31 -282 -510 O ATOM 3457 CB GLU B 182 54.096 12.035 -0.966 1.00 22.69 C ANISOU 3457 CB GLU B 182 2508 3529 2583 -139 -518 -189 C ATOM 3458 CG GLU B 182 53.004 11.961 0.097 1.00 27.77 C ANISOU 3458 CG GLU B 182 3413 4144 2993 18 92 -277 C ATOM 3459 CD GLU B 182 51.617 12.128 -0.483 1.00 32.40 C ANISOU 3459 CD GLU B 182 3650 4698 3962 93 -194 -86 C ATOM 3460 OE1 GLU B 182 51.515 12.347 -1.705 1.00 34.13 O ANISOU 3460 OE1 GLU B 182 3841 5125 4001 63 -89 -40 O ATOM 3461 OE2 GLU B 182 50.649 12.033 0.301 1.00 35.43 O ANISOU 3461 OE2 GLU B 182 4025 4981 4455 -35 102 -181 O ATOM 3462 N THR B 183 57.246 12.501 -1.811 1.00 17.28 N ANISOU 3462 N THR B 183 2393 2861 1311 94 -525 61 N ATOM 3463 CA THR B 183 58.211 12.350 -2.898 1.00 19.26 C ANISOU 3463 CA THR B 183 2167 3351 1799 236 -363 84 C ATOM 3464 C THR B 183 59.667 12.416 -2.474 1.00 18.26 C ANISOU 3464 C THR B 183 2161 3391 1388 134 -288 -231 C ATOM 3465 O THR B 183 60.542 11.991 -3.243 1.00 17.78 O ANISOU 3465 O THR B 183 1943 3715 1099 410 -504 83 O ATOM 3466 CB THR B 183 57.974 13.392 -4.015 1.00 22.34 C ANISOU 3466 CB THR B 183 3011 3364 2113 37 -547 265 C ATOM 3467 OG1 THR B 183 58.053 14.728 -3.508 1.00 23.43 O ANISOU 3467 OG1 THR B 183 3595 3229 2079 649 -968 475 O ATOM 3468 CG2 THR B 183 56.593 13.222 -4.637 1.00 23.96 C ANISOU 3468 CG2 THR B 183 2903 3823 2378 369 -506 357 C ATOM 3469 N ALA B 184 59.905 12.954 -1.273 1.00 16.01 N ANISOU 3469 N ALA B 184 1825 3327 931 638 -428 239 N ATOM 3470 CA ALA B 184 61.279 13.136 -0.844 1.00 14.24 C ANISOU 3470 CA ALA B 184 1932 2395 1084 403 -468 154 C ATOM 3471 C ALA B 184 61.628 12.320 0.407 1.00 13.56 C ANISOU 3471 C ALA B 184 1576 2762 815 328 -354 179 C ATOM 3472 O ALA B 184 60.781 12.126 1.272 1.00 14.80 O ANISOU 3472 O ALA B 184 1379 3198 1046 432 -353 208 O ATOM 3473 CB ALA B 184 61.524 14.610 -0.505 1.00 15.44 C ANISOU 3473 CB ALA B 184 2277 2455 1136 96 -144 185 C ATOM 3474 N HIS B 185 62.867 11.859 0.434 1.00 12.83 N ANISOU 3474 N HIS B 185 1693 2580 601 425 -361 -56 N ATOM 3475 CA HIS B 185 63.385 11.196 1.625 1.00 11.99 C ANISOU 3475 CA HIS B 185 1903 1865 787 172 -458 -36 C ATOM 3476 C HIS B 185 64.291 12.197 2.355 1.00 11.70 C ANISOU 3476 C HIS B 185 1563 2249 632 17 -320 8 C ATOM 3477 O HIS B 185 65.094 12.860 1.691 1.00 11.87 O ANISOU 3477 O HIS B 185 1973 2085 452 110 -245 54 O ATOM 3478 CB HIS B 185 64.219 9.981 1.218 1.00 11.25 C ANISOU 3478 CB HIS B 185 1626 2243 407 291 -454 -206 C ATOM 3479 CG HIS B 185 64.973 9.442 2.409 1.00 11.13 C ANISOU 3479 CG HIS B 185 1462 2110 658 206 -499 -9 C ATOM 3480 ND1 HIS B 185 64.267 8.983 3.502 1.00 12.45 N ANISOU 3480 ND1 HIS B 185 1733 2314 684 100 -423 -85 N ATOM 3481 CD2 HIS B 185 66.289 9.327 2.665 1.00 11.52 C ANISOU 3481 CD2 HIS B 185 1432 2456 488 231 -357 -68 C ATOM 3482 CE1 HIS B 185 65.166 8.585 4.404 1.00 11.56 C ANISOU 3482 CE1 HIS B 185 1420 2272 702 139 -319 -95 C ATOM 3483 NE2 HIS B 185 66.382 8.794 3.938 1.00 11.33 N ANISOU 3483 NE2 HIS B 185 1359 2459 486 294 -383 -30 N ATOM 3484 N TYR B 186 64.191 12.265 3.682 1.00 12.78 N ANISOU 3484 N TYR B 186 1805 2421 629 37 -566 46 N ATOM 3485 CA TYR B 186 65.068 13.131 4.466 1.00 11.08 C ANISOU 3485 CA TYR B 186 1391 1838 979 220 -79 -239 C ATOM 3486 C TYR B 186 66.311 12.339 4.878 1.00 9.94 C ANISOU 3486 C TYR B 186 1560 1405 811 91 -151 2 C ATOM 3487 O TYR B 186 66.247 11.404 5.687 1.00 11.02 O ANISOU 3487 O TYR B 186 1950 1533 704 -230 -199 -40 O ATOM 3488 CB TYR B 186 64.303 13.643 5.697 1.00 11.21 C ANISOU 3488 CB TYR B 186 1544 1957 757 -50 19 -104 C ATOM 3489 CG TYR B 186 65.181 14.436 6.644 1.00 12.29 C ANISOU 3489 CG TYR B 186 1709 1944 1018 -97 76 -381 C ATOM 3490 CD1 TYR B 186 66.212 15.232 6.173 1.00 13.34 C ANISOU 3490 CD1 TYR B 186 1726 1972 1372 -16 66 -97 C ATOM 3491 CD2 TYR B 186 64.959 14.406 8.022 1.00 12.64 C ANISOU 3491 CD2 TYR B 186 1741 2161 901 -132 -266 -61 C ATOM 3492 CE1 TYR B 186 67.028 15.950 7.028 1.00 14.04 C ANISOU 3492 CE1 TYR B 186 1962 2275 1097 192 -138 -156 C ATOM 3493 CE2 TYR B 186 65.773 15.129 8.881 1.00 13.57 C ANISOU 3493 CE2 TYR B 186 1458 2227 1472 -48 -293 -276 C ATOM 3494 CZ TYR B 186 66.780 15.908 8.390 1.00 12.76 C ANISOU 3494 CZ TYR B 186 1597 2176 1077 -2 -170 -351 C ATOM 3495 OH TYR B 186 67.588 16.637 9.248 1.00 14.60 O ANISOU 3495 OH TYR B 186 2114 2619 813 -71 -364 -413 O ATOM 3496 N MET B 187 67.436 12.695 4.267 1.00 11.14 N ANISOU 3496 N MET B 187 1334 2206 693 348 -152 -115 N ATOM 3497 CA MET B 187 68.716 12.031 4.521 1.00 9.78 C ANISOU 3497 CA MET B 187 1056 2070 589 238 260 -168 C ATOM 3498 C MET B 187 69.422 12.723 5.694 1.00 11.98 C ANISOU 3498 C MET B 187 1536 2200 815 19 -11 -117 C ATOM 3499 O MET B 187 70.291 13.564 5.526 1.00 12.28 O ANISOU 3499 O MET B 187 1825 2225 615 -91 -228 78 O ATOM 3500 CB MET B 187 69.568 12.027 3.254 1.00 11.39 C ANISOU 3500 CB MET B 187 1326 2607 395 355 216 -180 C ATOM 3501 CG MET B 187 70.877 11.254 3.296 1.00 13.61 C ANISOU 3501 CG MET B 187 1374 2794 1002 451 -315 38 C ATOM 3502 SD MET B 187 71.732 11.337 1.689 1.00 16.20 S ANISOU 3502 SD MET B 187 1626 3428 1103 1047 -147 -735 S ATOM 3503 CE MET B 187 70.804 10.169 0.709 1.00 15.81 C ANISOU 3503 CE MET B 187 2226 2797 983 649 73 -400 C ATOM 3504 N LEU B 188 68.984 12.363 6.904 1.00 11.40 N ANISOU 3504 N LEU B 188 1406 2221 705 -102 -73 -185 N ATOM 3505 CA LEU B 188 69.521 12.944 8.142 1.00 11.08 C ANISOU 3505 CA LEU B 188 1372 1994 843 -116 -189 -210 C ATOM 3506 C LEU B 188 71.005 12.596 8.255 1.00 10.70 C ANISOU 3506 C LEU B 188 1462 2079 524 -72 -89 -349 C ATOM 3507 O LEU B 188 71.391 11.476 7.916 1.00 11.45 O ANISOU 3507 O LEU B 188 1549 2116 687 389 -616 -104 O ATOM 3508 CB LEU B 188 68.694 12.413 9.322 1.00 11.91 C ANISOU 3508 CB LEU B 188 1174 2482 870 112 -154 -180 C ATOM 3509 CG LEU B 188 68.582 13.306 10.555 1.00 13.09 C ANISOU 3509 CG LEU B 188 1595 2327 1053 119 24 -196 C ATOM 3510 CD1 LEU B 188 67.355 12.868 11.360 1.00 13.61 C ANISOU 3510 CD1 LEU B 188 1860 2250 1060 115 190 -213 C ATOM 3511 CD2 LEU B 188 69.826 13.231 11.425 1.00 14.72 C ANISOU 3511 CD2 LEU B 188 1651 2750 1190 492 -16 -191 C ATOM 3512 N GLY B 189 71.831 13.519 8.751 1.00 10.11 N ANISOU 3512 N GLY B 189 1101 2454 286 -398 -167 170 N ATOM 3513 CA GLY B 189 73.253 13.351 8.748 1.00 10.97 C ANISOU 3513 CA GLY B 189 1190 2367 612 -153 -579 -27 C ATOM 3514 C GLY B 189 73.978 12.782 9.950 1.00 10.23 C ANISOU 3514 C GLY B 189 1451 1909 526 -280 -309 253 C ATOM 3515 O GLY B 189 75.208 12.746 9.911 1.00 11.93 O ANISOU 3515 O GLY B 189 1478 2602 454 -116 -126 413 O ATOM 3516 N THR B 190 73.245 12.369 10.980 1.00 10.04 N ANISOU 3516 N THR B 190 1581 1882 350 227 -123 175 N ATOM 3517 CA THR B 190 73.943 11.774 12.130 1.00 9.69 C ANISOU 3517 CA THR B 190 1594 1642 445 -36 -175 288 C ATOM 3518 C THR B 190 73.046 10.747 12.802 1.00 8.47 C ANISOU 3518 C THR B 190 1265 1680 275 88 131 -13 C ATOM 3519 O THR B 190 71.916 10.523 12.381 1.00 9.33 O ANISOU 3519 O THR B 190 1496 1778 270 72 -127 106 O ATOM 3520 CB THR B 190 74.424 12.868 13.090 1.00 8.51 C ANISOU 3520 CB THR B 190 1253 1336 643 353 -133 214 C ATOM 3521 OG1 THR B 190 75.347 12.228 14.011 1.00 8.60 O ANISOU 3521 OG1 THR B 190 1222 1458 588 262 -248 104 O ATOM 3522 CG2 THR B 190 73.269 13.510 13.829 1.00 10.22 C ANISOU 3522 CG2 THR B 190 1041 1797 1045 603 -307 208 C ATOM 3523 N ALA B 191 73.583 10.078 13.831 1.00 8.38 N ANISOU 3523 N ALA B 191 1371 1501 314 210 48 -67 N ATOM 3524 CA ALA B 191 72.850 9.042 14.547 1.00 8.67 C ANISOU 3524 CA ALA B 191 1561 1178 557 253 -90 13 C ATOM 3525 C ALA B 191 72.003 9.656 15.664 1.00 9.78 C ANISOU 3525 C ALA B 191 1544 1629 544 381 -101 -11 C ATOM 3526 O ALA B 191 72.110 9.368 16.860 1.00 9.26 O ANISOU 3526 O ALA B 191 1657 1449 411 138 15 -270 O ATOM 3527 CB ALA B 191 73.816 8.018 15.130 1.00 8.49 C ANISOU 3527 CB ALA B 191 1425 1358 443 223 -361 -119 C ATOM 3528 N ALA B 192 71.150 10.588 15.225 1.00 8.90 N ANISOU 3528 N ALA B 192 1292 1544 545 453 223 -33 N ATOM 3529 CA ALA B 192 70.291 11.357 16.096 1.00 8.36 C ANISOU 3529 CA ALA B 192 1125 1405 645 309 161 -103 C ATOM 3530 C ALA B 192 68.984 11.665 15.374 1.00 9.41 C ANISOU 3530 C ALA B 192 1393 1691 491 608 105 54 C ATOM 3531 O ALA B 192 68.803 11.140 14.259 1.00 10.47 O ANISOU 3531 O ALA B 192 1406 2029 545 379 76 -95 O ATOM 3532 CB ALA B 192 70.970 12.633 16.574 1.00 8.82 C ANISOU 3532 CB ALA B 192 998 1873 482 79 291 -409 C ATOM 3533 N GLY B 193 68.125 12.471 15.978 1.00 8.92 N ANISOU 3533 N GLY B 193 796 1684 908 141 316 -107 N ATOM 3534 CA GLY B 193 66.829 12.719 15.338 1.00 10.27 C ANISOU 3534 CA GLY B 193 1259 1513 1131 38 -198 86 C ATOM 3535 C GLY B 193 65.849 11.643 15.779 1.00 8.65 C ANISOU 3535 C GLY B 193 1073 1562 653 217 12 154 C ATOM 3536 O GLY B 193 66.095 10.806 16.663 1.00 8.97 O ANISOU 3536 O GLY B 193 1233 1522 652 136 -107 156 O ATOM 3537 N PRO B 194 64.645 11.654 15.211 1.00 9.29 N ANISOU 3537 N PRO B 194 1294 1800 435 203 -135 -68 N ATOM 3538 CA PRO B 194 63.616 10.708 15.590 1.00 9.44 C ANISOU 3538 CA PRO B 194 1151 1598 836 310 -319 3 C ATOM 3539 C PRO B 194 63.916 9.312 15.096 1.00 7.74 C ANISOU 3539 C PRO B 194 859 1520 561 65 -240 9 C ATOM 3540 O PRO B 194 64.537 9.158 14.025 1.00 10.56 O ANISOU 3540 O PRO B 194 1508 2004 499 -229 81 89 O ATOM 3541 CB PRO B 194 62.368 11.262 14.886 1.00 9.59 C ANISOU 3541 CB PRO B 194 997 1736 910 -96 -529 0 C ATOM 3542 CG PRO B 194 62.921 11.934 13.674 1.00 11.20 C ANISOU 3542 CG PRO B 194 1733 1949 573 133 -298 -160 C ATOM 3543 CD PRO B 194 64.214 12.571 14.131 1.00 10.86 C ANISOU 3543 CD PRO B 194 1567 1711 847 224 -279 92 C ATOM 3544 N HIS B 195 63.473 8.298 15.831 1.00 9.27 N ANISOU 3544 N HIS B 195 1577 1469 476 282 84 15 N ATOM 3545 CA HIS B 195 63.524 6.924 15.328 1.00 9.05 C ANISOU 3545 CA HIS B 195 1523 1287 628 126 -100 115 C ATOM 3546 C HIS B 195 62.782 6.912 13.993 1.00 10.39 C ANISOU 3546 C HIS B 195 1611 1514 823 270 -263 -360 C ATOM 3547 O HIS B 195 61.736 7.551 13.841 1.00 11.25 O ANISOU 3547 O HIS B 195 1515 1963 798 348 -307 -692 O ATOM 3548 CB HIS B 195 62.810 6.008 16.321 1.00 9.29 C ANISOU 3548 CB HIS B 195 1258 1283 989 -209 -147 -35 C ATOM 3549 CG HIS B 195 62.703 4.589 15.880 1.00 9.42 C ANISOU 3549 CG HIS B 195 1347 1384 847 94 75 -263 C ATOM 3550 ND1 HIS B 195 63.752 3.720 15.999 1.00 9.14 N ANISOU 3550 ND1 HIS B 195 1302 1202 968 -38 -141 -216 N ATOM 3551 CD2 HIS B 195 61.656 3.883 15.386 1.00 10.27 C ANISOU 3551 CD2 HIS B 195 1705 1212 986 56 -264 -157 C ATOM 3552 CE1 HIS B 195 63.390 2.522 15.552 1.00 10.05 C ANISOU 3552 CE1 HIS B 195 1340 1345 1135 -240 -213 -274 C ATOM 3553 NE2 HIS B 195 62.115 2.600 15.175 1.00 10.30 N ANISOU 3553 NE2 HIS B 195 1381 1364 1169 125 -236 -430 N ATOM 3554 N PRO B 196 63.314 6.217 12.988 1.00 9.56 N ANISOU 3554 N PRO B 196 812 2018 802 283 -221 -398 N ATOM 3555 CA PRO B 196 64.386 5.278 13.097 1.00 9.08 C ANISOU 3555 CA PRO B 196 1117 1626 709 259 -333 -567 C ATOM 3556 C PRO B 196 65.799 5.729 12.777 1.00 8.95 C ANISOU 3556 C PRO B 196 1285 1557 558 173 -391 -51 C ATOM 3557 O PRO B 196 66.674 4.869 12.643 1.00 9.56 O ANISOU 3557 O PRO B 196 1507 1555 569 288 -462 -174 O ATOM 3558 CB PRO B 196 63.964 4.214 12.034 1.00 9.82 C ANISOU 3558 CB PRO B 196 1266 1774 691 38 -586 -421 C ATOM 3559 CG PRO B 196 63.371 5.060 10.940 1.00 9.58 C ANISOU 3559 CG PRO B 196 1088 1924 629 537 -261 -467 C ATOM 3560 CD PRO B 196 62.564 6.102 11.674 1.00 9.99 C ANISOU 3560 CD PRO B 196 1030 2018 748 492 -209 -525 C ATOM 3561 N TYR B 197 66.022 7.030 12.688 1.00 8.71 N ANISOU 3561 N TYR B 197 1229 1615 466 12 -277 66 N ATOM 3562 CA TYR B 197 67.339 7.515 12.276 1.00 8.78 C ANISOU 3562 CA TYR B 197 1109 1294 932 360 -78 -145 C ATOM 3563 C TYR B 197 68.486 7.057 13.136 1.00 9.28 C ANISOU 3563 C TYR B 197 1230 1722 575 252 -174 -166 C ATOM 3564 O TYR B 197 69.503 6.614 12.570 1.00 9.29 O ANISOU 3564 O TYR B 197 1291 1741 497 255 -142 -417 O ATOM 3565 CB TYR B 197 67.360 8.997 11.944 1.00 9.19 C ANISOU 3565 CB TYR B 197 1665 1394 433 278 -448 -68 C ATOM 3566 CG TYR B 197 66.536 9.373 10.728 1.00 8.77 C ANISOU 3566 CG TYR B 197 1173 1779 380 252 -302 -300 C ATOM 3567 CD1 TYR B 197 67.130 9.197 9.479 1.00 9.31 C ANISOU 3567 CD1 TYR B 197 1183 1809 545 123 -92 -389 C ATOM 3568 CD2 TYR B 197 65.262 9.864 10.850 1.00 9.49 C ANISOU 3568 CD2 TYR B 197 1005 1839 763 101 -360 -17 C ATOM 3569 CE1 TYR B 197 66.422 9.562 8.331 1.00 10.75 C ANISOU 3569 CE1 TYR B 197 1309 2047 728 67 -394 -435 C ATOM 3570 CE2 TYR B 197 64.563 10.242 9.705 1.00 9.86 C ANISOU 3570 CE2 TYR B 197 903 2133 712 782 -107 -181 C ATOM 3571 CZ TYR B 197 65.141 10.055 8.457 1.00 11.06 C ANISOU 3571 CZ TYR B 197 1449 2329 423 288 -240 -104 C ATOM 3572 OH TYR B 197 64.407 10.441 7.357 1.00 11.89 O ANISOU 3572 OH TYR B 197 1958 2189 371 220 -443 -118 O ATOM 3573 N PRO B 198 68.459 7.138 14.461 1.00 9.07 N ANISOU 3573 N PRO B 198 1192 1684 571 370 -231 -160 N ATOM 3574 CA PRO B 198 69.637 6.710 15.216 1.00 7.87 C ANISOU 3574 CA PRO B 198 861 1562 566 343 -11 -116 C ATOM 3575 C PRO B 198 70.023 5.277 14.921 1.00 7.92 C ANISOU 3575 C PRO B 198 1181 1391 439 -155 -152 -327 C ATOM 3576 O PRO B 198 71.195 4.908 14.867 1.00 10.11 O ANISOU 3576 O PRO B 198 1215 2178 447 -8 -254 -237 O ATOM 3577 CB PRO B 198 69.199 6.956 16.661 1.00 8.60 C ANISOU 3577 CB PRO B 198 1201 1735 333 177 -271 -150 C ATOM 3578 CG PRO B 198 68.224 8.079 16.565 1.00 10.07 C ANISOU 3578 CG PRO B 198 1685 1796 345 359 -295 154 C ATOM 3579 CD PRO B 198 67.427 7.744 15.310 1.00 9.32 C ANISOU 3579 CD PRO B 198 1380 1866 295 301 -105 -107 C ATOM 3580 N THR B 199 69.018 4.419 14.713 1.00 8.47 N ANISOU 3580 N THR B 199 1176 1306 736 -165 -50 -205 N ATOM 3581 CA THR B 199 69.215 3.014 14.417 1.00 8.35 C ANISOU 3581 CA THR B 199 1093 1283 796 37 -61 -38 C ATOM 3582 C THR B 199 69.777 2.811 13.005 1.00 9.17 C ANISOU 3582 C THR B 199 1278 1496 712 89 -284 -235 C ATOM 3583 O THR B 199 70.708 2.050 12.800 1.00 9.54 O ANISOU 3583 O THR B 199 1450 1605 571 146 -272 -393 O ATOM 3584 CB THR B 199 67.903 2.247 14.633 1.00 9.18 C ANISOU 3584 CB THR B 199 1148 1547 793 -21 93 -128 C ATOM 3585 OG1 THR B 199 67.553 2.300 16.033 1.00 10.14 O ANISOU 3585 OG1 THR B 199 1252 1860 741 -291 7 -364 O ATOM 3586 CG2 THR B 199 68.014 0.801 14.206 1.00 9.57 C ANISOU 3586 CG2 THR B 199 1488 1551 597 242 -274 -94 C ATOM 3587 N ILE B 200 69.121 3.451 12.021 1.00 8.95 N ANISOU 3587 N ILE B 200 1193 1745 463 156 -247 -310 N ATOM 3588 CA ILE B 200 69.566 3.281 10.626 1.00 8.90 C ANISOU 3588 CA ILE B 200 1095 1774 513 99 -154 -123 C ATOM 3589 C ILE B 200 70.995 3.755 10.461 1.00 8.71 C ANISOU 3589 C ILE B 200 1295 1448 567 -185 -224 -245 C ATOM 3590 O ILE B 200 71.816 3.078 9.834 1.00 10.45 O ANISOU 3590 O ILE B 200 1188 2149 633 -106 -197 -421 O ATOM 3591 CB ILE B 200 68.669 4.087 9.666 1.00 8.91 C ANISOU 3591 CB ILE B 200 1309 1708 369 7 -139 -57 C ATOM 3592 CG1 ILE B 200 67.289 3.408 9.647 1.00 9.53 C ANISOU 3592 CG1 ILE B 200 1303 1892 425 -47 -174 -137 C ATOM 3593 CG2 ILE B 200 69.230 4.160 8.250 1.00 10.99 C ANISOU 3593 CG2 ILE B 200 1389 2369 417 -310 -133 -51 C ATOM 3594 CD1 ILE B 200 66.277 4.235 8.876 1.00 10.88 C ANISOU 3594 CD1 ILE B 200 1112 2225 796 300 -81 -216 C ATOM 3595 N VAL B 201 71.285 4.938 11.027 1.00 8.72 N ANISOU 3595 N VAL B 201 1348 1450 515 -73 -143 -350 N ATOM 3596 CA VAL B 201 72.618 5.506 10.822 1.00 8.58 C ANISOU 3596 CA VAL B 201 1322 1462 476 62 67 -268 C ATOM 3597 C VAL B 201 73.665 4.612 11.447 1.00 8.53 C ANISOU 3597 C VAL B 201 1545 1180 515 104 80 -308 C ATOM 3598 O VAL B 201 74.744 4.400 10.898 1.00 9.23 O ANISOU 3598 O VAL B 201 1345 1601 560 333 -198 -220 O ATOM 3599 CB VAL B 201 72.669 6.975 11.272 1.00 8.51 C ANISOU 3599 CB VAL B 201 1292 1276 664 84 -64 -46 C ATOM 3600 CG1 VAL B 201 74.092 7.502 11.187 1.00 10.13 C ANISOU 3600 CG1 VAL B 201 1337 1415 1098 -81 -266 -81 C ATOM 3601 CG2 VAL B 201 71.736 7.827 10.412 1.00 10.09 C ANISOU 3601 CG2 VAL B 201 1634 1357 844 87 -276 10 C ATOM 3602 N ARG B 202 73.394 4.114 12.678 1.00 8.72 N ANISOU 3602 N ARG B 202 1410 1329 573 249 109 -188 N ATOM 3603 CA ARG B 202 74.346 3.172 13.260 1.00 7.84 C ANISOU 3603 CA ARG B 202 1219 1144 616 -46 30 -103 C ATOM 3604 C ARG B 202 74.557 1.963 12.335 1.00 7.54 C ANISOU 3604 C ARG B 202 1044 1405 415 -270 -9 -254 C ATOM 3605 O ARG B 202 75.698 1.578 12.060 1.00 8.78 O ANISOU 3605 O ARG B 202 1200 1730 407 26 -53 -333 O ATOM 3606 CB ARG B 202 73.817 2.654 14.608 1.00 9.03 C ANISOU 3606 CB ARG B 202 1124 1842 466 -36 -208 99 C ATOM 3607 CG ARG B 202 74.680 1.529 15.165 1.00 9.40 C ANISOU 3607 CG ARG B 202 1575 1386 610 -192 -186 143 C ATOM 3608 CD ARG B 202 73.997 0.866 16.355 1.00 9.54 C ANISOU 3608 CD ARG B 202 663 1776 1185 -215 167 90 C ATOM 3609 NE ARG B 202 72.881 0.015 15.953 1.00 9.76 N ANISOU 3609 NE ARG B 202 1207 2086 417 -396 108 -266 N ATOM 3610 CZ ARG B 202 71.671 -0.021 16.473 1.00 9.96 C ANISOU 3610 CZ ARG B 202 1324 1751 711 -187 247 -142 C ATOM 3611 NH1 ARG B 202 71.328 0.842 17.432 1.00 11.56 N ANISOU 3611 NH1 ARG B 202 1347 2302 745 -235 220 -521 N ATOM 3612 NH2 ARG B 202 70.768 -0.887 16.023 1.00 11.99 N ANISOU 3612 NH2 ARG B 202 1720 1870 967 -263 -65 -264 N ATOM 3613 N GLU B 203 73.452 1.352 11.874 1.00 8.16 N ANISOU 3613 N GLU B 203 1139 1621 343 -285 -114 -278 N ATOM 3614 CA GLU B 203 73.627 0.140 11.058 1.00 8.56 C ANISOU 3614 CA GLU B 203 1078 1542 633 -90 48 -287 C ATOM 3615 C GLU B 203 74.346 0.406 9.741 1.00 9.03 C ANISOU 3615 C GLU B 203 1304 1442 685 -225 -59 17 C ATOM 3616 O GLU B 203 75.046 -0.473 9.245 1.00 11.50 O ANISOU 3616 O GLU B 203 1795 1822 754 230 -152 6 O ATOM 3617 CB GLU B 203 72.264 -0.515 10.838 1.00 9.70 C ANISOU 3617 CB GLU B 203 1319 1600 769 -346 31 -307 C ATOM 3618 CG GLU B 203 71.666 -1.071 12.130 1.00 10.31 C ANISOU 3618 CG GLU B 203 1451 1535 934 -88 181 -118 C ATOM 3619 CD GLU B 203 72.538 -2.124 12.757 1.00 11.46 C ANISOU 3619 CD GLU B 203 1827 1382 1147 35 -109 -400 C ATOM 3620 OE1 GLU B 203 72.843 -3.146 12.115 1.00 13.94 O ANISOU 3620 OE1 GLU B 203 2475 1439 1382 165 103 -479 O ATOM 3621 OE2 GLU B 203 72.982 -1.935 13.914 1.00 14.50 O ANISOU 3621 OE2 GLU B 203 2998 1527 983 360 -223 -400 O ATOM 3622 N PHE B 204 74.205 1.615 9.210 1.00 8.01 N ANISOU 3622 N PHE B 204 1205 1344 495 -239 -267 -159 N ATOM 3623 CA PHE B 204 74.878 1.974 7.974 1.00 8.17 C ANISOU 3623 CA PHE B 204 1074 1630 400 -186 -237 -234 C ATOM 3624 C PHE B 204 76.279 2.527 8.183 1.00 9.07 C ANISOU 3624 C PHE B 204 1086 1830 529 -240 -280 -121 C ATOM 3625 O PHE B 204 76.943 2.903 7.215 1.00 10.33 O ANISOU 3625 O PHE B 204 1344 2182 400 -151 -233 -104 O ATOM 3626 CB PHE B 204 74.018 2.910 7.123 1.00 10.10 C ANISOU 3626 CB PHE B 204 1166 2260 412 3 -371 -162 C ATOM 3627 CG PHE B 204 72.781 2.310 6.508 1.00 9.52 C ANISOU 3627 CG PHE B 204 1149 1940 529 -71 -145 -400 C ATOM 3628 CD1 PHE B 204 72.524 0.956 6.480 1.00 10.51 C ANISOU 3628 CD1 PHE B 204 1443 1930 619 -43 -495 -372 C ATOM 3629 CD2 PHE B 204 71.855 3.172 5.926 1.00 10.39 C ANISOU 3629 CD2 PHE B 204 1211 2049 688 -124 -134 -232 C ATOM 3630 CE1 PHE B 204 71.376 0.442 5.876 1.00 11.08 C ANISOU 3630 CE1 PHE B 204 1409 2047 756 -4 -463 -433 C ATOM 3631 CE2 PHE B 204 70.698 2.671 5.342 1.00 10.13 C ANISOU 3631 CE2 PHE B 204 1091 1859 901 -241 -56 -200 C ATOM 3632 CZ PHE B 204 70.470 1.309 5.299 1.00 10.35 C ANISOU 3632 CZ PHE B 204 1765 1727 440 163 -236 -500 C ATOM 3633 N GLN B 205 76.759 2.558 9.430 1.00 8.53 N ANISOU 3633 N GLN B 205 1097 1547 598 17 -460 75 N ATOM 3634 CA GLN B 205 78.107 2.953 9.771 1.00 7.77 C ANISOU 3634 CA GLN B 205 856 1481 614 233 46 -240 C ATOM 3635 C GLN B 205 78.832 1.815 10.503 1.00 8.14 C ANISOU 3635 C GLN B 205 1376 1382 334 198 229 -166 C ATOM 3636 O GLN B 205 80.008 1.957 10.805 1.00 9.74 O ANISOU 3636 O GLN B 205 1587 1647 466 107 -228 -196 O ATOM 3637 CB GLN B 205 78.144 4.182 10.693 1.00 8.73 C ANISOU 3637 CB GLN B 205 1592 1264 462 272 -176 -25 C ATOM 3638 CG GLN B 205 77.764 5.501 10.027 1.00 8.43 C ANISOU 3638 CG GLN B 205 1338 1299 565 480 38 8 C ATOM 3639 CD GLN B 205 78.806 5.899 8.985 1.00 8.02 C ANISOU 3639 CD GLN B 205 1393 1119 537 212 -24 -259 C ATOM 3640 OE1 GLN B 205 79.826 5.261 8.783 1.00 9.11 O ANISOU 3640 OE1 GLN B 205 1382 1707 373 483 -59 193 O ATOM 3641 NE2 GLN B 205 78.540 7.011 8.296 1.00 9.38 N ANISOU 3641 NE2 GLN B 205 1508 1490 566 179 -606 -48 N ATOM 3642 N ARG B 206 78.141 0.718 10.777 1.00 8.88 N ANISOU 3642 N ARG B 206 1373 1239 761 231 -130 -26 N ATOM 3643 CA ARG B 206 78.716 -0.310 11.654 1.00 10.25 C ANISOU 3643 CA ARG B 206 1377 1305 1210 226 192 322 C ATOM 3644 C ARG B 206 79.884 -1.058 11.037 1.00 8.38 C ANISOU 3644 C ARG B 206 1587 790 806 111 2 -70 C ATOM 3645 O ARG B 206 80.599 -1.770 11.754 1.00 9.52 O ANISOU 3645 O ARG B 206 2017 975 626 124 -111 25 O ATOM 3646 CB ARG B 206 77.622 -1.231 12.158 1.00 13.71 C ANISOU 3646 CB ARG B 206 1988 1547 1674 94 661 555 C ATOM 3647 CG ARG B 206 77.141 -2.287 11.202 1.00 16.68 C ANISOU 3647 CG ARG B 206 2006 2282 2048 -250 -343 609 C ATOM 3648 CD ARG B 206 76.058 -3.100 11.948 1.00 21.07 C ANISOU 3648 CD ARG B 206 2458 2545 3003 -547 143 438 C ATOM 3649 NE ARG B 206 76.649 -3.801 13.075 1.00 22.92 N ANISOU 3649 NE ARG B 206 2764 2960 2983 -479 -118 304 N ATOM 3650 CZ ARG B 206 76.317 -3.888 14.350 1.00 22.23 C ANISOU 3650 CZ ARG B 206 2695 2904 2846 -245 -208 87 C ATOM 3651 NH1 ARG B 206 77.059 -4.637 15.173 1.00 23.29 N ANISOU 3651 NH1 ARG B 206 2577 2758 3515 -362 -429 165 N ATOM 3652 NH2 ARG B 206 75.283 -3.245 14.882 1.00 23.60 N ANISOU 3652 NH2 ARG B 206 2470 3155 3342 -107 -566 -40 N ATOM 3653 N MET B 207 80.052 -0.916 9.716 1.00 8.36 N ANISOU 3653 N MET B 207 1286 1143 749 -77 -76 -145 N ATOM 3654 CA MET B 207 81.193 -1.545 9.072 1.00 8.52 C ANISOU 3654 CA MET B 207 1428 1341 470 -9 -27 -152 C ATOM 3655 C MET B 207 82.516 -0.951 9.555 1.00 7.95 C ANISOU 3655 C MET B 207 1558 1066 398 41 -247 -5 C ATOM 3656 O MET B 207 83.550 -1.600 9.448 1.00 10.04 O ANISOU 3656 O MET B 207 1548 1506 760 191 -277 79 O ATOM 3657 CB MET B 207 81.134 -1.466 7.554 1.00 9.11 C ANISOU 3657 CB MET B 207 1821 1198 444 339 -78 -83 C ATOM 3658 CG MET B 207 81.150 -0.104 6.883 1.00 10.12 C ANISOU 3658 CG MET B 207 1730 1493 621 18 -186 271 C ATOM 3659 SD MET B 207 79.723 0.961 7.188 1.00 10.34 S ANISOU 3659 SD MET B 207 1755 1835 338 136 -177 59 S ATOM 3660 CE MET B 207 78.426 0.039 6.368 1.00 11.53 C ANISOU 3660 CE MET B 207 1974 1894 514 412 -363 -428 C ATOM 3661 N ILE B 208 82.459 0.269 10.108 1.00 7.51 N ANISOU 3661 N ILE B 208 1260 1215 378 161 -282 -168 N ATOM 3662 CA ILE B 208 83.707 0.822 10.653 1.00 8.68 C ANISOU 3662 CA ILE B 208 1578 1220 498 -185 -402 -23 C ATOM 3663 C ILE B 208 84.250 -0.101 11.748 1.00 9.40 C ANISOU 3663 C ILE B 208 1495 1345 732 -39 -111 225 C ATOM 3664 O ILE B 208 85.430 -0.502 11.708 1.00 9.64 O ANISOU 3664 O ILE B 208 1623 1575 463 135 194 183 O ATOM 3665 CB ILE B 208 83.481 2.232 11.209 1.00 8.52 C ANISOU 3665 CB ILE B 208 1484 1235 517 -125 -421 -9 C ATOM 3666 CG1 ILE B 208 83.033 3.166 10.069 1.00 8.25 C ANISOU 3666 CG1 ILE B 208 1505 835 795 -286 -425 54 C ATOM 3667 CG2 ILE B 208 84.743 2.773 11.874 1.00 9.60 C ANISOU 3667 CG2 ILE B 208 1297 1684 667 -30 -458 20 C ATOM 3668 CD1 ILE B 208 82.645 4.547 10.539 1.00 9.94 C ANISOU 3668 CD1 ILE B 208 2021 1179 576 300 -418 25 C ATOM 3669 N GLY B 209 83.396 -0.373 12.741 1.00 8.25 N ANISOU 3669 N GLY B 209 1578 1057 499 -12 -105 -39 N ATOM 3670 CA GLY B 209 83.835 -1.245 13.819 1.00 8.73 C ANISOU 3670 CA GLY B 209 1585 723 1009 44 -124 124 C ATOM 3671 C GLY B 209 84.027 -2.700 13.391 1.00 8.39 C ANISOU 3671 C GLY B 209 1777 870 542 -40 -173 -4 C ATOM 3672 O GLY B 209 84.924 -3.357 13.900 1.00 9.13 O ANISOU 3672 O GLY B 209 1795 1339 335 46 -365 2 O ATOM 3673 N GLU B 210 83.204 -3.186 12.456 1.00 9.03 N ANISOU 3673 N GLU B 210 1565 1350 515 -129 -258 166 N ATOM 3674 CA GLU B 210 83.373 -4.574 12.032 1.00 9.73 C ANISOU 3674 CA GLU B 210 1235 1427 1035 -299 -225 -21 C ATOM 3675 C GLU B 210 84.743 -4.764 11.398 1.00 9.67 C ANISOU 3675 C GLU B 210 1495 1587 591 -183 -76 -181 C ATOM 3676 O GLU B 210 85.460 -5.724 11.662 1.00 10.82 O ANISOU 3676 O GLU B 210 1975 1551 584 -46 -83 -107 O ATOM 3677 CB GLU B 210 82.280 -4.923 11.020 1.00 11.57 C ANISOU 3677 CB GLU B 210 1192 2061 1144 -339 -322 53 C ATOM 3678 CG GLU B 210 80.923 -5.122 11.660 1.00 12.75 C ANISOU 3678 CG GLU B 210 1352 1949 1544 -38 83 -287 C ATOM 3679 CD GLU B 210 79.782 -5.167 10.668 1.00 17.19 C ANISOU 3679 CD GLU B 210 1573 2947 2010 -201 -227 -196 C ATOM 3680 OE1 GLU B 210 80.032 -4.874 9.473 1.00 19.94 O ANISOU 3680 OE1 GLU B 210 2271 3309 1996 -719 -704 93 O ATOM 3681 OE2 GLU B 210 78.646 -5.470 11.117 1.00 19.14 O ANISOU 3681 OE2 GLU B 210 1518 2983 2772 -706 -493 -234 O ATOM 3682 N GLU B 211 85.106 -3.864 10.482 1.00 8.38 N ANISOU 3682 N GLU B 211 1256 1290 640 -99 -297 -153 N ATOM 3683 CA GLU B 211 86.417 -3.939 9.836 1.00 9.44 C ANISOU 3683 CA GLU B 211 1444 1561 583 49 -74 321 C ATOM 3684 C GLU B 211 87.512 -3.793 10.911 1.00 8.31 C ANISOU 3684 C GLU B 211 1855 1013 291 267 -143 122 C ATOM 3685 O GLU B 211 88.481 -4.547 10.913 1.00 9.60 O ANISOU 3685 O GLU B 211 2126 964 559 459 -163 -129 O ATOM 3686 CB GLU B 211 86.609 -2.889 8.742 1.00 9.92 C ANISOU 3686 CB GLU B 211 1933 1496 341 -280 -227 99 C ATOM 3687 CG GLU B 211 85.710 -3.078 7.522 1.00 9.40 C ANISOU 3687 CG GLU B 211 1321 1872 379 -142 -89 180 C ATOM 3688 CD GLU B 211 85.811 -1.910 6.567 1.00 8.78 C ANISOU 3688 CD GLU B 211 1432 1538 368 -177 -68 -57 C ATOM 3689 OE1 GLU B 211 86.687 -1.039 6.701 1.00 8.91 O ANISOU 3689 OE1 GLU B 211 1473 1607 307 -285 -45 218 O ATOM 3690 OE2 GLU B 211 84.974 -1.886 5.620 1.00 11.08 O ANISOU 3690 OE2 GLU B 211 1601 2054 553 -98 -331 -299 O ATOM 3691 N THR B 212 87.355 -2.805 11.806 1.00 8.55 N ANISOU 3691 N THR B 212 1428 1476 346 -50 -175 -253 N ATOM 3692 CA THR B 212 88.399 -2.587 12.824 1.00 8.56 C ANISOU 3692 CA THR B 212 1214 1493 545 175 -257 -49 C ATOM 3693 C THR B 212 88.623 -3.870 13.617 1.00 8.95 C ANISOU 3693 C THR B 212 1374 1421 607 205 -109 -113 C ATOM 3694 O THR B 212 89.764 -4.202 13.901 1.00 8.98 O ANISOU 3694 O THR B 212 1326 1394 692 153 -233 44 O ATOM 3695 CB THR B 212 87.980 -1.454 13.779 1.00 8.58 C ANISOU 3695 CB THR B 212 1691 1179 389 -72 -279 15 C ATOM 3696 OG1 THR B 212 87.875 -0.224 13.032 1.00 9.17 O ANISOU 3696 OG1 THR B 212 1861 1114 508 346 7 -32 O ATOM 3697 CG2 THR B 212 88.994 -1.199 14.883 1.00 9.50 C ANISOU 3697 CG2 THR B 212 1468 1638 504 282 -205 -303 C ATOM 3698 N LYS B 213 87.525 -4.525 13.999 1.00 9.40 N ANISOU 3698 N LYS B 213 1651 1120 799 283 77 363 N ATOM 3699 CA LYS B 213 87.696 -5.776 14.755 1.00 8.82 C ANISOU 3699 CA LYS B 213 1500 981 870 274 -187 220 C ATOM 3700 C LYS B 213 88.499 -6.812 13.976 1.00 9.88 C ANISOU 3700 C LYS B 213 1858 988 909 135 -40 71 C ATOM 3701 O LYS B 213 89.432 -7.394 14.508 1.00 10.88 O ANISOU 3701 O LYS B 213 1802 1053 1279 182 -194 -107 O ATOM 3702 CB LYS B 213 86.334 -6.346 15.147 1.00 11.60 C ANISOU 3702 CB LYS B 213 1743 1474 1191 -76 -130 471 C ATOM 3703 CG LYS B 213 86.473 -7.677 15.886 1.00 12.61 C ANISOU 3703 CG LYS B 213 2087 1526 1176 -117 177 522 C ATOM 3704 CD LYS B 213 85.102 -8.249 16.234 1.00 14.31 C ANISOU 3704 CD LYS B 213 1987 1975 1475 -87 363 223 C ATOM 3705 CE LYS B 213 84.509 -7.489 17.405 1.00 14.76 C ANISOU 3705 CE LYS B 213 1980 2061 1569 -243 334 5 C ATOM 3706 NZ LYS B 213 83.164 -8.038 17.770 1.00 14.52 N ANISOU 3706 NZ LYS B 213 1872 2080 1566 -96 521 -287 N ATOM 3707 N ALA B 214 88.138 -7.004 12.704 1.00 10.75 N ANISOU 3707 N ALA B 214 2006 1136 943 228 -151 -76 N ATOM 3708 CA ALA B 214 88.860 -8.018 11.926 1.00 10.81 C ANISOU 3708 CA ALA B 214 1928 1130 1047 177 -103 -49 C ATOM 3709 C ALA B 214 90.317 -7.628 11.744 1.00 10.54 C ANISOU 3709 C ALA B 214 1897 1334 773 299 180 -5 C ATOM 3710 O ALA B 214 91.230 -8.460 11.786 1.00 12.07 O ANISOU 3710 O ALA B 214 2242 1166 1178 430 14 14 O ATOM 3711 CB ALA B 214 88.192 -8.167 10.557 1.00 12.04 C ANISOU 3711 CB ALA B 214 2061 1426 1090 -46 -125 -431 C ATOM 3712 N GLN B 215 90.546 -6.342 11.483 1.00 10.56 N ANISOU 3712 N GLN B 215 1924 1336 751 225 67 23 N ATOM 3713 CA GLN B 215 91.903 -5.836 11.251 1.00 10.85 C ANISOU 3713 CA GLN B 215 1904 1384 834 152 -219 201 C ATOM 3714 C GLN B 215 92.772 -5.955 12.504 1.00 12.36 C ANISOU 3714 C GLN B 215 1795 2051 849 4 -170 183 C ATOM 3715 O GLN B 215 93.932 -6.375 12.398 1.00 12.22 O ANISOU 3715 O GLN B 215 2108 1814 722 332 -120 220 O ATOM 3716 CB GLN B 215 91.824 -4.403 10.699 1.00 10.29 C ANISOU 3716 CB GLN B 215 2020 1394 494 367 -108 135 C ATOM 3717 CG GLN B 215 91.268 -4.363 9.271 1.00 11.44 C ANISOU 3717 CG GLN B 215 2081 1544 722 4 -355 -13 C ATOM 3718 CD GLN B 215 90.937 -2.952 8.838 1.00 10.93 C ANISOU 3718 CD GLN B 215 1738 1516 897 70 48 40 C ATOM 3719 OE1 GLN B 215 90.348 -2.175 9.594 1.00 9.75 O ANISOU 3719 OE1 GLN B 215 1654 1431 618 464 -498 114 O ATOM 3720 NE2 GLN B 215 91.313 -2.601 7.596 1.00 11.81 N ANISOU 3720 NE2 GLN B 215 1830 1836 822 269 -179 238 N ATOM 3721 N ILE B 216 92.218 -5.545 13.649 1.00 11.17 N ANISOU 3721 N ILE B 216 1709 1734 803 -85 -344 35 N ATOM 3722 CA ILE B 216 93.058 -5.640 14.862 1.00 11.43 C ANISOU 3722 CA ILE B 216 1775 1830 740 343 -315 147 C ATOM 3723 C ILE B 216 93.295 -7.089 15.256 1.00 11.46 C ANISOU 3723 C ILE B 216 1456 1706 1191 84 -221 52 C ATOM 3724 O ILE B 216 94.380 -7.418 15.755 1.00 12.01 O ANISOU 3724 O ILE B 216 1412 2038 1113 246 -81 208 O ATOM 3725 CB ILE B 216 92.448 -4.771 15.976 1.00 12.31 C ANISOU 3725 CB ILE B 216 1779 2093 804 145 -450 -178 C ATOM 3726 CG1 ILE B 216 93.522 -4.487 17.038 1.00 13.99 C ANISOU 3726 CG1 ILE B 216 1832 2180 1303 306 -859 230 C ATOM 3727 CG2 ILE B 216 91.229 -5.418 16.584 1.00 13.05 C ANISOU 3727 CG2 ILE B 216 1779 1697 1483 -244 -741 -277 C ATOM 3728 CD1 ILE B 216 94.437 -3.372 16.595 1.00 17.30 C ANISOU 3728 CD1 ILE B 216 2485 2387 1701 -159 -554 -56 C ATOM 3729 N LEU B 217 92.320 -7.961 15.005 1.00 9.46 N ANISOU 3729 N LEU B 217 1782 925 886 255 -188 17 N ATOM 3730 CA LEU B 217 92.547 -9.385 15.328 1.00 12.03 C ANISOU 3730 CA LEU B 217 1853 985 1731 317 -4 162 C ATOM 3731 C LEU B 217 93.663 -9.916 14.440 1.00 12.85 C ANISOU 3731 C LEU B 217 1820 1736 1328 221 -85 10 C ATOM 3732 O LEU B 217 94.535 -10.647 14.907 1.00 14.56 O ANISOU 3732 O LEU B 217 2115 2040 1377 556 -240 -89 O ATOM 3733 CB LEU B 217 91.282 -10.209 15.164 1.00 13.28 C ANISOU 3733 CB LEU B 217 2021 1616 1407 -5 -45 225 C ATOM 3734 CG LEU B 217 90.257 -10.036 16.292 1.00 13.74 C ANISOU 3734 CG LEU B 217 1793 1454 1973 128 109 216 C ATOM 3735 CD1 LEU B 217 88.960 -10.743 15.921 1.00 14.94 C ANISOU 3735 CD1 LEU B 217 2132 1656 1889 -257 126 183 C ATOM 3736 CD2 LEU B 217 90.801 -10.560 17.611 1.00 17.14 C ANISOU 3736 CD2 LEU B 217 2609 2049 1856 121 80 338 C ATOM 3737 N ASP B 218 93.630 -9.555 13.157 1.00 12.12 N ANISOU 3737 N ASP B 218 1622 1842 1141 283 -173 -295 N ATOM 3738 CA ASP B 218 94.684 -10.009 12.240 1.00 13.69 C ANISOU 3738 CA ASP B 218 1873 2077 1252 615 -108 -212 C ATOM 3739 C ASP B 218 96.053 -9.493 12.663 1.00 12.84 C ANISOU 3739 C ASP B 218 1954 1532 1393 366 169 -146 C ATOM 3740 O ASP B 218 97.041 -10.247 12.668 1.00 16.03 O ANISOU 3740 O ASP B 218 2357 1620 2115 713 -184 -349 O ATOM 3741 CB ASP B 218 94.346 -9.500 10.837 1.00 15.17 C ANISOU 3741 CB ASP B 218 2027 2423 1315 404 -111 -37 C ATOM 3742 CG ASP B 218 95.356 -9.844 9.768 1.00 19.01 C ANISOU 3742 CG ASP B 218 2944 2316 1961 389 580 -44 C ATOM 3743 OD1 ASP B 218 95.656 -11.046 9.584 1.00 20.29 O ANISOU 3743 OD1 ASP B 218 3216 2329 2164 547 742 -6 O ATOM 3744 OD2 ASP B 218 95.841 -8.896 9.125 1.00 20.16 O ANISOU 3744 OD2 ASP B 218 2869 2436 2354 281 786 19 O ATOM 3745 N LYS B 219 96.113 -8.224 13.062 1.00 12.46 N ANISOU 3745 N LYS B 219 2414 1643 677 110 -312 -150 N ATOM 3746 CA LYS B 219 97.408 -7.628 13.347 1.00 11.77 C ANISOU 3746 CA LYS B 219 2087 1621 763 364 -248 -32 C ATOM 3747 C LYS B 219 97.940 -7.821 14.761 1.00 12.47 C ANISOU 3747 C LYS B 219 1534 2376 827 278 -203 52 C ATOM 3748 O LYS B 219 99.156 -7.795 14.920 1.00 15.02 O ANISOU 3748 O LYS B 219 1565 3025 1118 223 -396 -35 O ATOM 3749 CB LYS B 219 97.361 -6.115 13.046 1.00 13.88 C ANISOU 3749 CB LYS B 219 2283 1650 1341 277 -204 94 C ATOM 3750 CG ALYS B 219 96.979 -5.875 11.582 0.50 15.30 C ANISOU 3750 CG ALYS B 219 2421 1994 1400 187 -224 215 C ATOM 3751 CD ALYS B 219 96.582 -4.418 11.404 0.50 17.36 C ANISOU 3751 CD ALYS B 219 2559 1985 2053 168 -225 69 C ATOM 3752 CE ALYS B 219 96.785 -3.984 9.956 0.50 18.26 C ANISOU 3752 CE ALYS B 219 2646 1971 2322 107 -276 369 C ATOM 3753 NZ ALYS B 219 97.252 -2.569 9.922 0.50 16.17 N ANISOU 3753 NZ ALYS B 219 2660 1545 1939 576 -192 637 N ATOM 3754 CG BLYS B 219 97.235 -5.819 11.556 0.50 13.60 C ANISOU 3754 CG BLYS B 219 1995 1837 1335 310 -53 111 C ATOM 3755 CD BLYS B 219 98.368 -6.425 10.745 0.50 13.86 C ANISOU 3755 CD BLYS B 219 1995 1705 1565 61 23 -176 C ATOM 3756 CE BLYS B 219 98.178 -6.139 9.261 0.50 16.17 C ANISOU 3756 CE BLYS B 219 2248 2051 1845 190 -129 267 C ATOM 3757 NZ BLYS B 219 99.373 -6.538 8.475 0.50 17.94 N ANISOU 3757 NZ BLYS B 219 2521 2259 2038 165 148 337 N ATOM 3758 N GLU B 220 97.056 -7.955 15.725 1.00 12.48 N ANISOU 3758 N GLU B 220 1733 2043 964 561 19 139 N ATOM 3759 CA GLU B 220 97.473 -8.065 17.123 1.00 12.12 C ANISOU 3759 CA GLU B 220 1698 1818 1087 534 -233 -43 C ATOM 3760 C GLU B 220 96.979 -9.331 17.801 1.00 14.32 C ANISOU 3760 C GLU B 220 2063 1986 1392 314 -177 85 C ATOM 3761 O GLU B 220 97.439 -9.618 18.926 1.00 16.61 O ANISOU 3761 O GLU B 220 2267 2580 1462 432 -370 135 O ATOM 3762 CB GLU B 220 96.978 -6.845 17.895 1.00 12.09 C ANISOU 3762 CB GLU B 220 1967 1353 1276 225 -156 41 C ATOM 3763 CG GLU B 220 97.551 -5.531 17.420 1.00 12.34 C ANISOU 3763 CG GLU B 220 1982 1226 1480 360 -318 190 C ATOM 3764 CD GLU B 220 98.987 -5.298 17.819 1.00 14.35 C ANISOU 3764 CD GLU B 220 2008 1589 1857 328 -416 326 C ATOM 3765 OE1 GLU B 220 99.459 -5.972 18.763 1.00 18.68 O ANISOU 3765 OE1 GLU B 220 2564 2303 2229 168 -870 765 O ATOM 3766 OE2 GLU B 220 99.668 -4.437 17.224 1.00 15.30 O ANISOU 3766 OE2 GLU B 220 2168 2076 1568 83 -560 459 O ATOM 3767 N GLY B 221 96.048 -10.054 17.191 1.00 13.50 N ANISOU 3767 N GLY B 221 2107 1673 1348 379 -151 203 N ATOM 3768 CA GLY B 221 95.590 -11.309 17.782 1.00 13.96 C ANISOU 3768 CA GLY B 221 2179 1617 1508 293 101 24 C ATOM 3769 C GLY B 221 94.688 -11.128 18.987 1.00 13.80 C ANISOU 3769 C GLY B 221 2128 1522 1594 348 147 193 C ATOM 3770 O GLY B 221 94.482 -12.105 19.715 1.00 16.10 O ANISOU 3770 O GLY B 221 2807 1136 2175 362 391 194 O ATOM 3771 N ARG B 222 94.149 -9.929 19.169 1.00 14.16 N ANISOU 3771 N ARG B 222 1971 1849 1558 748 142 310 N ATOM 3772 CA ARG B 222 93.282 -9.658 20.309 1.00 13.85 C ANISOU 3772 CA ARG B 222 1912 2017 1334 755 -35 279 C ATOM 3773 C ARG B 222 92.508 -8.370 20.035 1.00 13.71 C ANISOU 3773 C ARG B 222 2077 1872 1261 668 181 369 C ATOM 3774 O ARG B 222 92.824 -7.674 19.058 1.00 15.66 O ANISOU 3774 O ARG B 222 2635 2260 1054 996 220 531 O ATOM 3775 CB ARG B 222 94.093 -9.495 21.601 1.00 15.09 C ANISOU 3775 CB ARG B 222 1636 2418 1678 352 -85 65 C ATOM 3776 CG ARG B 222 95.070 -8.312 21.523 1.00 17.18 C ANISOU 3776 CG ARG B 222 2293 1937 2297 410 -109 262 C ATOM 3777 CD ARG B 222 95.854 -8.341 22.824 1.00 23.18 C ANISOU 3777 CD ARG B 222 2740 3557 2511 156 -352 112 C ATOM 3778 NE ARG B 222 96.015 -7.153 23.562 1.00 30.04 N ANISOU 3778 NE ARG B 222 4101 3502 3812 232 -6 -46 N ATOM 3779 CZ ARG B 222 95.470 -6.204 24.269 1.00 29.63 C ANISOU 3779 CZ ARG B 222 3952 3596 3712 166 69 -150 C ATOM 3780 NH1 ARG B 222 94.181 -6.021 24.565 1.00 27.04 N ANISOU 3780 NH1 ARG B 222 3682 3557 3036 -78 -139 62 N ATOM 3781 NH2 ARG B 222 96.356 -5.312 24.725 1.00 31.25 N ANISOU 3781 NH2 ARG B 222 3559 4379 3936 94 -409 55 N ATOM 3782 N LEU B 223 91.508 -8.115 20.848 1.00 12.29 N ANISOU 3782 N LEU B 223 1979 1646 1046 702 -24 -10 N ATOM 3783 CA LEU B 223 90.703 -6.902 20.727 1.00 12.34 C ANISOU 3783 CA LEU B 223 1774 1308 1605 336 -3 94 C ATOM 3784 C LEU B 223 91.404 -5.722 21.368 1.00 12.12 C ANISOU 3784 C LEU B 223 1791 1536 1278 122 82 157 C ATOM 3785 O LEU B 223 92.295 -5.889 22.222 1.00 13.34 O ANISOU 3785 O LEU B 223 1653 2296 1120 63 180 144 O ATOM 3786 CB LEU B 223 89.332 -7.117 21.379 1.00 14.08 C ANISOU 3786 CB LEU B 223 2014 1410 1925 -78 241 -253 C ATOM 3787 CG LEU B 223 88.484 -8.236 20.778 1.00 14.99 C ANISOU 3787 CG LEU B 223 2344 1366 1986 -237 218 -156 C ATOM 3788 CD1 LEU B 223 87.201 -8.403 21.568 1.00 19.13 C ANISOU 3788 CD1 LEU B 223 2122 1885 3261 -363 384 -334 C ATOM 3789 CD2 LEU B 223 88.168 -7.935 19.314 1.00 18.98 C ANISOU 3789 CD2 LEU B 223 2901 1917 2392 15 -439 151 C ATOM 3790 N PRO B 224 91.034 -4.506 20.979 1.00 11.23 N ANISOU 3790 N PRO B 224 1612 1598 1056 233 -157 78 N ATOM 3791 CA PRO B 224 91.613 -3.328 21.597 1.00 11.14 C ANISOU 3791 CA PRO B 224 1667 1660 904 269 -215 35 C ATOM 3792 C PRO B 224 91.239 -3.197 23.077 1.00 9.79 C ANISOU 3792 C PRO B 224 1348 1433 939 59 -40 296 C ATOM 3793 O PRO B 224 90.186 -3.693 23.506 1.00 11.36 O ANISOU 3793 O PRO B 224 1622 1935 761 -309 -273 552 O ATOM 3794 CB PRO B 224 91.001 -2.154 20.820 1.00 11.03 C ANISOU 3794 CB PRO B 224 2171 1249 773 -162 -269 76 C ATOM 3795 CG PRO B 224 90.315 -2.748 19.629 1.00 12.50 C ANISOU 3795 CG PRO B 224 2356 1277 1115 172 -609 -98 C ATOM 3796 CD PRO B 224 89.960 -4.162 20.019 1.00 10.96 C ANISOU 3796 CD PRO B 224 1417 1710 1035 -109 -90 203 C ATOM 3797 N ASP B 225 92.089 -2.494 23.828 1.00 10.24 N ANISOU 3797 N ASP B 225 1646 1426 818 367 -320 232 N ATOM 3798 CA ASP B 225 91.690 -2.138 25.188 1.00 10.26 C ANISOU 3798 CA ASP B 225 1250 1755 893 80 -304 14 C ATOM 3799 C ASP B 225 90.600 -1.072 25.136 1.00 10.27 C ANISOU 3799 C ASP B 225 1630 1559 713 151 -155 312 C ATOM 3800 O ASP B 225 89.725 -1.026 26.001 1.00 11.01 O ANISOU 3800 O ASP B 225 1209 1932 1043 302 -168 385 O ATOM 3801 CB ASP B 225 92.864 -1.636 26.013 1.00 10.58 C ANISOU 3801 CB ASP B 225 1452 1762 806 7 -520 301 C ATOM 3802 CG ASP B 225 93.804 -2.802 26.266 1.00 10.61 C ANISOU 3802 CG ASP B 225 1038 1844 1149 -73 -320 342 C ATOM 3803 OD1 ASP B 225 93.361 -3.850 26.780 1.00 13.54 O ANISOU 3803 OD1 ASP B 225 1239 1804 2101 215 -49 762 O ATOM 3804 OD2 ASP B 225 94.983 -2.663 25.924 1.00 10.72 O ANISOU 3804 OD2 ASP B 225 1087 2318 667 325 -73 477 O ATOM 3805 N ALA B 226 90.647 -0.197 24.126 1.00 9.13 N ANISOU 3805 N ALA B 226 1688 1386 394 356 -375 129 N ATOM 3806 CA ALA B 226 89.631 0.830 23.978 1.00 7.73 C ANISOU 3806 CA ALA B 226 1478 915 544 22 -195 63 C ATOM 3807 C ALA B 226 89.590 1.314 22.526 1.00 8.34 C ANISOU 3807 C ALA B 226 1117 1554 497 12 91 162 C ATOM 3808 O ALA B 226 90.625 1.327 21.842 1.00 8.99 O ANISOU 3808 O ALA B 226 1163 1831 423 246 109 281 O ATOM 3809 CB ALA B 226 89.910 2.059 24.841 1.00 9.46 C ANISOU 3809 CB ALA B 226 1495 1319 781 -356 -148 -216 C ATOM 3810 N VAL B 227 88.406 1.717 22.117 1.00 8.74 N ANISOU 3810 N VAL B 227 1327 1460 535 230 37 270 N ATOM 3811 CA VAL B 227 88.220 2.370 20.806 1.00 8.39 C ANISOU 3811 CA VAL B 227 1324 1542 321 -16 -273 -19 C ATOM 3812 C VAL B 227 87.716 3.772 21.141 1.00 8.91 C ANISOU 3812 C VAL B 227 1239 1499 648 -74 142 221 C ATOM 3813 O VAL B 227 86.883 3.938 22.046 1.00 9.88 O ANISOU 3813 O VAL B 227 1509 1876 369 129 63 -73 O ATOM 3814 CB VAL B 227 87.300 1.610 19.869 1.00 8.70 C ANISOU 3814 CB VAL B 227 1029 1519 757 187 -437 -189 C ATOM 3815 CG1 VAL B 227 87.871 0.228 19.565 1.00 9.85 C ANISOU 3815 CG1 VAL B 227 1303 1472 970 140 -25 -139 C ATOM 3816 CG2 VAL B 227 85.883 1.476 20.407 1.00 10.26 C ANISOU 3816 CG2 VAL B 227 1383 1788 728 -258 -93 119 C ATOM 3817 N ILE B 228 88.227 4.782 20.455 1.00 8.50 N ANISOU 3817 N ILE B 228 1728 1069 431 -9 -179 159 N ATOM 3818 CA ILE B 228 88.020 6.173 20.787 1.00 7.06 C ANISOU 3818 CA ILE B 228 1166 1203 314 190 134 96 C ATOM 3819 C ILE B 228 87.541 6.957 19.570 1.00 8.11 C ANISOU 3819 C ILE B 228 1096 1526 458 336 -93 122 C ATOM 3820 O ILE B 228 88.163 6.851 18.496 1.00 8.78 O ANISOU 3820 O ILE B 228 1116 1886 333 51 -10 48 O ATOM 3821 CB ILE B 228 89.349 6.785 21.290 1.00 9.17 C ANISOU 3821 CB ILE B 228 1281 1738 465 294 -367 242 C ATOM 3822 CG1 ILE B 228 89.885 5.928 22.459 1.00 10.43 C ANISOU 3822 CG1 ILE B 228 1684 1646 633 119 -359 459 C ATOM 3823 CG2 ILE B 228 89.163 8.221 21.723 1.00 9.51 C ANISOU 3823 CG2 ILE B 228 1221 1814 580 -85 -258 -41 C ATOM 3824 CD1 ILE B 228 91.370 5.797 22.426 1.00 15.45 C ANISOU 3824 CD1 ILE B 228 1738 2934 1198 486 -200 648 C ATOM 3825 N ALA B 229 86.478 7.697 19.755 1.00 7.32 N ANISOU 3825 N ALA B 229 1040 1446 293 309 -177 4 N ATOM 3826 CA ALA B 229 85.899 8.400 18.607 1.00 6.75 C ANISOU 3826 CA ALA B 229 754 1413 399 374 -238 9 C ATOM 3827 C ALA B 229 85.308 9.724 19.048 1.00 7.69 C ANISOU 3827 C ALA B 229 1163 1321 438 388 -65 98 C ATOM 3828 O ALA B 229 84.763 9.836 20.167 1.00 9.01 O ANISOU 3828 O ALA B 229 1861 1187 377 183 66 -184 O ATOM 3829 CB ALA B 229 84.829 7.530 17.945 1.00 7.82 C ANISOU 3829 CB ALA B 229 1390 1244 338 -28 -218 100 C ATOM 3830 N CYS B 230 85.420 10.729 18.185 1.00 7.67 N ANISOU 3830 N CYS B 230 1265 1047 602 -134 -180 -13 N ATOM 3831 CA CYS B 230 84.799 12.016 18.484 1.00 7.10 C ANISOU 3831 CA CYS B 230 1261 1063 376 -166 -276 -156 C ATOM 3832 C CYS B 230 83.281 11.919 18.370 1.00 6.77 C ANISOU 3832 C CYS B 230 1183 647 744 202 -304 -156 C ATOM 3833 O CYS B 230 82.762 11.062 17.634 1.00 7.79 O ANISOU 3833 O CYS B 230 1132 1318 509 162 -269 -480 O ATOM 3834 CB CYS B 230 85.378 13.141 17.639 1.00 8.91 C ANISOU 3834 CB CYS B 230 1712 1391 283 -72 -171 137 C ATOM 3835 SG CYS B 230 84.927 13.059 15.876 1.00 9.10 S ANISOU 3835 SG CYS B 230 1652 1487 320 -266 -306 131 S ATOM 3836 N VAL B 231 82.560 12.787 19.074 1.00 7.31 N ANISOU 3836 N VAL B 231 750 1464 565 161 218 -9 N ATOM 3837 CA VAL B 231 81.110 12.784 19.138 1.00 7.85 C ANISOU 3837 CA VAL B 231 779 1700 506 -175 122 -23 C ATOM 3838 C VAL B 231 80.547 14.178 18.919 1.00 8.85 C ANISOU 3838 C VAL B 231 1277 1770 317 85 -137 -248 C ATOM 3839 O VAL B 231 80.660 15.046 19.789 1.00 9.09 O ANISOU 3839 O VAL B 231 1550 1332 570 202 -337 -152 O ATOM 3840 CB VAL B 231 80.589 12.244 20.494 1.00 8.83 C ANISOU 3840 CB VAL B 231 991 1619 745 -21 255 235 C ATOM 3841 CG1 VAL B 231 79.072 12.265 20.592 1.00 10.02 C ANISOU 3841 CG1 VAL B 231 1001 1958 846 -24 44 -206 C ATOM 3842 CG2 VAL B 231 81.079 10.821 20.700 1.00 9.60 C ANISOU 3842 CG2 VAL B 231 1371 1676 602 47 258 418 C ATOM 3843 N GLY B 232 80.008 14.400 17.721 1.00 9.66 N ANISOU 3843 N GLY B 232 1568 1625 477 124 -266 -26 N ATOM 3844 CA GLY B 232 79.311 15.633 17.356 1.00 10.22 C ANISOU 3844 CA GLY B 232 1568 1467 848 -67 -466 -6 C ATOM 3845 C GLY B 232 77.817 15.333 17.507 1.00 9.64 C ANISOU 3845 C GLY B 232 1527 1785 349 63 -313 -204 C ATOM 3846 O GLY B 232 77.140 15.832 18.385 1.00 12.51 O ANISOU 3846 O GLY B 232 1248 2808 697 -41 43 -330 O ATOM 3847 N GLY B 233 77.328 14.485 16.596 1.00 8.79 N ANISOU 3847 N GLY B 233 1702 1289 348 -134 -330 21 N ATOM 3848 CA GLY B 233 75.977 13.955 16.661 1.00 9.23 C ANISOU 3848 CA GLY B 233 1239 1887 382 437 -81 230 C ATOM 3849 C GLY B 233 76.042 12.484 17.089 1.00 9.03 C ANISOU 3849 C GLY B 233 1423 1713 295 -67 -223 -65 C ATOM 3850 O GLY B 233 75.077 11.949 17.643 1.00 10.81 O ANISOU 3850 O GLY B 233 1491 2030 586 -45 106 -18 O ATOM 3851 N GLY B 234 77.148 11.793 16.783 1.00 8.97 N ANISOU 3851 N GLY B 234 1520 1537 353 -14 -73 147 N ATOM 3852 CA GLY B 234 77.290 10.413 17.221 1.00 8.27 C ANISOU 3852 CA GLY B 234 1513 1250 380 -12 -247 -285 C ATOM 3853 C GLY B 234 77.450 9.335 16.176 1.00 7.92 C ANISOU 3853 C GLY B 234 1480 1224 304 48 179 -161 C ATOM 3854 O GLY B 234 77.611 8.158 16.530 1.00 8.28 O ANISOU 3854 O GLY B 234 1368 1401 377 383 -208 -118 O ATOM 3855 N SER B 235 77.425 9.673 14.875 1.00 8.47 N ANISOU 3855 N SER B 235 1314 1588 316 390 8 21 N ATOM 3856 CA SER B 235 77.515 8.616 13.861 1.00 7.73 C ANISOU 3856 CA SER B 235 1070 1394 474 115 -337 4 C ATOM 3857 C SER B 235 78.856 7.917 13.719 1.00 6.80 C ANISOU 3857 C SER B 235 1195 1132 255 33 -62 -48 C ATOM 3858 O SER B 235 78.841 6.684 13.665 1.00 8.13 O ANISOU 3858 O SER B 235 1459 1094 537 -250 -155 106 O ATOM 3859 CB SER B 235 77.016 9.091 12.483 1.00 9.07 C ANISOU 3859 CB SER B 235 1480 1398 567 -273 -583 94 C ATOM 3860 OG SER B 235 77.887 10.053 11.908 1.00 8.49 O ANISOU 3860 OG SER B 235 1446 1468 312 -82 -274 41 O ATOM 3861 N ASN B 236 79.982 8.617 13.646 1.00 8.33 N ANISOU 3861 N ASN B 236 932 1976 258 -45 -70 63 N ATOM 3862 CA ASN B 236 81.244 7.900 13.462 1.00 7.49 C ANISOU 3862 CA ASN B 236 951 1314 579 -173 -336 66 C ATOM 3863 C ASN B 236 81.516 7.077 14.724 1.00 7.34 C ANISOU 3863 C ASN B 236 1069 1262 458 65 -173 -48 C ATOM 3864 O ASN B 236 82.009 5.963 14.629 1.00 7.96 O ANISOU 3864 O ASN B 236 1424 1223 379 84 -67 -14 O ATOM 3865 CB ASN B 236 82.418 8.780 13.074 1.00 7.90 C ANISOU 3865 CB ASN B 236 1167 1499 335 -215 74 -67 C ATOM 3866 CG ASN B 236 83.157 9.381 14.257 1.00 7.02 C ANISOU 3866 CG ASN B 236 992 1405 270 122 68 -120 C ATOM 3867 OD1 ASN B 236 84.085 8.778 14.775 1.00 8.64 O ANISOU 3867 OD1 ASN B 236 1149 1671 463 148 -241 -59 O ATOM 3868 ND2 ASN B 236 82.749 10.580 14.610 1.00 8.82 N ANISOU 3868 ND2 ASN B 236 1455 1302 594 389 37 186 N ATOM 3869 N ALA B 237 81.150 7.662 15.876 1.00 8.02 N ANISOU 3869 N ALA B 237 1100 1578 370 27 -180 -52 N ATOM 3870 CA ALA B 237 81.443 6.909 17.103 1.00 7.25 C ANISOU 3870 CA ALA B 237 1230 1108 415 26 -302 -205 C ATOM 3871 C ALA B 237 80.593 5.664 17.251 1.00 7.35 C ANISOU 3871 C ALA B 237 1267 1040 485 104 -156 -288 C ATOM 3872 O ALA B 237 81.121 4.616 17.632 1.00 8.17 O ANISOU 3872 O ALA B 237 1397 1317 389 81 -167 36 O ATOM 3873 CB ALA B 237 81.302 7.803 18.352 1.00 9.00 C ANISOU 3873 CB ALA B 237 1518 1453 448 457 -246 -394 C ATOM 3874 N ILE B 238 79.285 5.768 16.983 1.00 6.91 N ANISOU 3874 N ILE B 238 1209 990 426 -1 -88 -99 N ATOM 3875 CA ILE B 238 78.458 4.564 17.089 1.00 7.54 C ANISOU 3875 CA ILE B 238 1237 1257 372 -188 -129 -32 C ATOM 3876 C ILE B 238 78.846 3.570 16.001 1.00 7.41 C ANISOU 3876 C ILE B 238 1113 1141 560 58 -8 33 C ATOM 3877 O ILE B 238 78.769 2.376 16.222 1.00 8.45 O ANISOU 3877 O ILE B 238 1728 1125 355 12 -350 -146 O ATOM 3878 CB ILE B 238 76.959 4.847 17.145 1.00 8.35 C ANISOU 3878 CB ILE B 238 1187 1609 378 -200 -248 -28 C ATOM 3879 CG1 ILE B 238 76.200 3.724 17.862 1.00 9.07 C ANISOU 3879 CG1 ILE B 238 1735 1282 430 -298 -509 22 C ATOM 3880 CG2 ILE B 238 76.360 5.078 15.758 1.00 9.36 C ANISOU 3880 CG2 ILE B 238 1634 1592 333 -333 -288 -22 C ATOM 3881 CD1 ILE B 238 76.458 3.687 19.368 1.00 10.52 C ANISOU 3881 CD1 ILE B 238 1646 2021 329 -226 -209 117 C ATOM 3882 N GLY B 239 79.311 4.045 14.844 1.00 7.73 N ANISOU 3882 N GLY B 239 1585 1071 282 292 -211 -55 N ATOM 3883 CA GLY B 239 79.747 3.107 13.797 1.00 7.55 C ANISOU 3883 CA GLY B 239 1405 1120 344 394 -216 -135 C ATOM 3884 C GLY B 239 80.976 2.324 14.251 1.00 6.98 C ANISOU 3884 C GLY B 239 970 1336 344 289 49 -280 C ATOM 3885 O GLY B 239 81.120 1.131 13.934 1.00 9.00 O ANISOU 3885 O GLY B 239 1614 1349 455 409 -472 -222 O ATOM 3886 N MET B 240 81.888 2.999 14.978 1.00 7.98 N ANISOU 3886 N MET B 240 1090 1400 543 136 -155 -56 N ATOM 3887 CA MET B 240 83.030 2.281 15.519 1.00 8.27 C ANISOU 3887 CA MET B 240 1464 1164 513 71 -368 80 C ATOM 3888 C MET B 240 82.641 1.390 16.679 1.00 8.00 C ANISOU 3888 C MET B 240 1584 956 499 50 19 -223 C ATOM 3889 O MET B 240 83.085 0.266 16.794 1.00 9.75 O ANISOU 3889 O MET B 240 2130 1132 441 302 -280 33 O ATOM 3890 CB AMET B 240 84.098 3.282 15.981 0.40 7.99 C ANISOU 3890 CB AMET B 240 1304 1271 459 -24 -136 52 C ATOM 3891 CG AMET B 240 85.239 2.643 16.763 0.40 7.90 C ANISOU 3891 CG AMET B 240 1543 1181 277 106 -120 80 C ATOM 3892 SD AMET B 240 86.139 1.416 15.796 0.40 8.80 S ANISOU 3892 SD AMET B 240 1314 1495 536 118 20 75 S ATOM 3893 CE AMET B 240 87.198 2.471 14.809 0.40 9.35 C ANISOU 3893 CE AMET B 240 1581 1406 567 -174 -298 226 C ATOM 3894 CB BMET B 240 84.117 3.263 15.964 0.60 7.92 C ANISOU 3894 CB BMET B 240 1229 1429 352 -69 -98 91 C ATOM 3895 CG BMET B 240 85.283 2.642 16.722 0.60 8.39 C ANISOU 3895 CG BMET B 240 1563 1323 302 107 -87 194 C ATOM 3896 SD BMET B 240 86.296 1.534 15.727 0.60 9.00 S ANISOU 3896 SD BMET B 240 1086 1869 465 -61 164 183 S ATOM 3897 CE BMET B 240 87.376 2.704 14.899 0.60 8.70 C ANISOU 3897 CE BMET B 240 1482 1558 266 -164 -56 142 C ATOM 3898 N PHE B 241 81.780 1.891 17.569 1.00 7.27 N ANISOU 3898 N PHE B 241 1351 1062 348 79 33 85 N ATOM 3899 CA PHE B 241 81.456 1.154 18.777 1.00 7.56 C ANISOU 3899 CA PHE B 241 1562 758 553 -5 105 123 C ATOM 3900 C PHE B 241 80.583 -0.063 18.561 1.00 7.69 C ANISOU 3900 C PHE B 241 1464 913 547 -51 -53 53 C ATOM 3901 O PHE B 241 80.689 -1.032 19.316 1.00 9.27 O ANISOU 3901 O PHE B 241 1649 1118 755 98 -489 209 O ATOM 3902 CB PHE B 241 80.647 2.026 19.757 1.00 8.66 C ANISOU 3902 CB PHE B 241 1258 1485 548 -120 159 -129 C ATOM 3903 CG PHE B 241 81.309 3.200 20.376 1.00 8.51 C ANISOU 3903 CG PHE B 241 1295 1466 473 -64 144 -150 C ATOM 3904 CD1 PHE B 241 82.665 3.472 20.219 1.00 8.35 C ANISOU 3904 CD1 PHE B 241 1275 1549 349 -188 -96 -45 C ATOM 3905 CD2 PHE B 241 80.550 4.040 21.179 1.00 7.60 C ANISOU 3905 CD2 PHE B 241 1353 1120 414 291 -358 -124 C ATOM 3906 CE1 PHE B 241 83.244 4.569 20.824 1.00 8.43 C ANISOU 3906 CE1 PHE B 241 1525 1257 422 143 -464 13 C ATOM 3907 CE2 PHE B 241 81.125 5.151 21.794 1.00 8.82 C ANISOU 3907 CE2 PHE B 241 1296 1428 628 108 -486 -212 C ATOM 3908 CZ PHE B 241 82.459 5.401 21.602 1.00 9.07 C ANISOU 3908 CZ PHE B 241 1239 1690 517 202 -515 -97 C ATOM 3909 N ALA B 242 79.638 -0.023 17.615 1.00 9.79 N ANISOU 3909 N ALA B 242 1635 1373 711 -109 -258 -276 N ATOM 3910 CA ALA B 242 78.572 -1.017 17.579 1.00 9.22 C ANISOU 3910 CA ALA B 242 1303 1437 764 57 -227 -296 C ATOM 3911 C ALA B 242 79.016 -2.457 17.700 1.00 9.76 C ANISOU 3911 C ALA B 242 1564 1190 952 -327 -22 -249 C ATOM 3912 O ALA B 242 78.508 -3.214 18.546 1.00 10.30 O ANISOU 3912 O ALA B 242 2019 1244 653 -225 -213 -136 O ATOM 3913 CB ALA B 242 77.684 -0.770 16.360 1.00 9.60 C ANISOU 3913 CB ALA B 242 1426 1471 749 3 -249 -173 C ATOM 3914 N ASP B 243 79.974 -2.866 16.870 1.00 9.90 N ANISOU 3914 N ASP B 243 1514 1354 892 -122 -30 14 N ATOM 3915 CA ASP B 243 80.402 -4.249 16.838 1.00 10.29 C ANISOU 3915 CA ASP B 243 1596 1551 761 149 131 -105 C ATOM 3916 C ASP B 243 81.173 -4.655 18.080 1.00 9.50 C ANISOU 3916 C ASP B 243 1811 1030 770 39 80 -55 C ATOM 3917 O ASP B 243 81.362 -5.844 18.264 1.00 12.41 O ANISOU 3917 O ASP B 243 2901 955 861 156 -244 -264 O ATOM 3918 CB ASP B 243 81.239 -4.543 15.582 1.00 11.04 C ANISOU 3918 CB ASP B 243 1812 1673 710 -76 222 -196 C ATOM 3919 CG ASP B 243 81.178 -6.019 15.229 1.00 12.30 C ANISOU 3919 CG ASP B 243 1890 1729 1056 -117 113 -260 C ATOM 3920 OD1 ASP B 243 80.036 -6.530 15.058 1.00 16.70 O ANISOU 3920 OD1 ASP B 243 2127 2241 1975 -453 292 -687 O ATOM 3921 OD2 ASP B 243 82.258 -6.627 15.133 1.00 15.90 O ANISOU 3921 OD2 ASP B 243 2287 1856 1899 259 -20 -221 O ATOM 3922 N PHE B 244 81.572 -3.696 18.905 1.00 10.25 N ANISOU 3922 N PHE B 244 1903 1483 509 -3 -293 -67 N ATOM 3923 CA PHE B 244 82.284 -4.012 20.134 1.00 9.27 C ANISOU 3923 CA PHE B 244 1525 1205 793 52 -230 292 C ATOM 3924 C PHE B 244 81.380 -3.903 21.362 1.00 10.35 C ANISOU 3924 C PHE B 244 1746 1213 974 463 -44 124 C ATOM 3925 O PHE B 244 81.863 -4.191 22.467 1.00 11.25 O ANISOU 3925 O PHE B 244 1982 1488 803 -88 3 346 O ATOM 3926 CB PHE B 244 83.466 -3.055 20.330 1.00 9.53 C ANISOU 3926 CB PHE B 244 1470 1450 700 -70 132 19 C ATOM 3927 CG PHE B 244 84.530 -3.125 19.279 1.00 8.67 C ANISOU 3927 CG PHE B 244 1370 1180 744 124 81 40 C ATOM 3928 CD1 PHE B 244 85.435 -4.175 19.319 1.00 9.62 C ANISOU 3928 CD1 PHE B 244 1393 1505 758 328 112 -53 C ATOM 3929 CD2 PHE B 244 84.646 -2.170 18.272 1.00 9.38 C ANISOU 3929 CD2 PHE B 244 1139 1502 924 143 -87 226 C ATOM 3930 CE1 PHE B 244 86.448 -4.285 18.379 1.00 10.15 C ANISOU 3930 CE1 PHE B 244 1571 1269 1016 215 307 -118 C ATOM 3931 CE2 PHE B 244 85.660 -2.276 17.347 1.00 10.11 C ANISOU 3931 CE2 PHE B 244 1680 1720 442 103 8 86 C ATOM 3932 CZ PHE B 244 86.558 -3.324 17.391 1.00 10.96 C ANISOU 3932 CZ PHE B 244 1722 1619 822 101 84 -1 C ATOM 3933 N ILE B 245 80.124 -3.507 21.250 1.00 9.43 N ANISOU 3933 N ILE B 245 1558 1335 689 175 203 -21 N ATOM 3934 CA ILE B 245 79.304 -3.322 22.460 1.00 9.19 C ANISOU 3934 CA ILE B 245 1522 1073 895 50 338 -55 C ATOM 3935 C ILE B 245 79.268 -4.579 23.298 1.00 9.69 C ANISOU 3935 C ILE B 245 1779 1158 745 -309 242 -63 C ATOM 3936 O ILE B 245 79.348 -4.499 24.534 1.00 12.48 O ANISOU 3936 O ILE B 245 2379 1678 683 -626 123 -137 O ATOM 3937 CB ILE B 245 77.903 -2.810 22.089 1.00 10.46 C ANISOU 3937 CB ILE B 245 1540 1483 951 55 242 -3 C ATOM 3938 CG1 ILE B 245 77.981 -1.350 21.603 1.00 10.86 C ANISOU 3938 CG1 ILE B 245 1627 1547 952 99 -174 146 C ATOM 3939 CG2 ILE B 245 76.935 -2.912 23.262 1.00 11.65 C ANISOU 3939 CG2 ILE B 245 1612 1592 1222 108 484 75 C ATOM 3940 CD1 ILE B 245 76.688 -0.843 20.993 1.00 12.30 C ANISOU 3940 CD1 ILE B 245 1575 2138 962 261 22 343 C ATOM 3941 N ASN B 246 79.135 -5.739 22.676 1.00 11.94 N ANISOU 3941 N ASN B 246 2189 1154 1195 -342 50 -195 N ATOM 3942 CA ASN B 246 79.050 -6.994 23.415 1.00 13.17 C ANISOU 3942 CA ASN B 246 1922 1515 1568 -35 -180 262 C ATOM 3943 C ASN B 246 80.393 -7.554 23.860 1.00 12.40 C ANISOU 3943 C ASN B 246 1676 1541 1494 -135 -2 160 C ATOM 3944 O ASN B 246 80.452 -8.622 24.498 1.00 17.06 O ANISOU 3944 O ASN B 246 2451 1656 2375 -344 -167 542 O ATOM 3945 CB ASN B 246 78.314 -8.045 22.576 1.00 17.36 C ANISOU 3945 CB ASN B 246 2368 1977 2251 -417 -391 77 C ATOM 3946 CG ASN B 246 76.847 -7.712 22.384 1.00 19.91 C ANISOU 3946 CG ASN B 246 2361 2338 2865 -285 -36 135 C ATOM 3947 OD1 ASN B 246 76.189 -8.284 21.499 1.00 26.36 O ANISOU 3947 OD1 ASN B 246 2972 3534 3509 -594 -778 204 O ATOM 3948 ND2 ASN B 246 76.333 -6.814 23.199 1.00 18.60 N ANISOU 3948 ND2 ASN B 246 1150 2505 3413 -300 86 72 N ATOM 3949 N ASP B 247 81.487 -6.929 23.462 1.00 12.01 N ANISOU 3949 N ASP B 247 1799 1886 878 -218 33 282 N ATOM 3950 CA ASP B 247 82.832 -7.315 23.896 1.00 12.63 C ANISOU 3950 CA ASP B 247 1817 1840 1142 -129 144 453 C ATOM 3951 C ASP B 247 83.128 -6.464 25.130 1.00 13.44 C ANISOU 3951 C ASP B 247 1895 1874 1338 -73 102 294 C ATOM 3952 O ASP B 247 83.724 -5.400 25.008 1.00 13.12 O ANISOU 3952 O ASP B 247 1937 1677 1370 133 -252 490 O ATOM 3953 CB ASP B 247 83.845 -7.027 22.787 1.00 12.29 C ANISOU 3953 CB ASP B 247 1996 1667 1009 -514 96 321 C ATOM 3954 CG ASP B 247 83.543 -7.847 21.542 1.00 13.95 C ANISOU 3954 CG ASP B 247 2503 1601 1197 -177 303 39 C ATOM 3955 OD1 ASP B 247 83.546 -9.095 21.657 1.00 16.00 O ANISOU 3955 OD1 ASP B 247 3237 1537 1306 -221 371 -235 O ATOM 3956 OD2 ASP B 247 83.306 -7.220 20.491 1.00 15.41 O ANISOU 3956 OD2 ASP B 247 2918 1569 1370 100 6 -13 O ATOM 3957 N THR B 248 82.665 -6.935 26.289 1.00 15.56 N ANISOU 3957 N THR B 248 2383 2351 1178 -188 -3 333 N ATOM 3958 CA THR B 248 82.740 -6.158 27.510 1.00 16.53 C ANISOU 3958 CA THR B 248 2342 2459 1480 -392 7 63 C ATOM 3959 C THR B 248 84.116 -5.655 27.901 1.00 13.56 C ANISOU 3959 C THR B 248 2268 1919 965 -296 203 207 C ATOM 3960 O THR B 248 84.154 -4.633 28.599 1.00 16.56 O ANISOU 3960 O THR B 248 2774 2450 1068 -386 222 -188 O ATOM 3961 CB THR B 248 82.106 -6.956 28.681 1.00 19.11 C ANISOU 3961 CB THR B 248 2741 2894 1624 -313 406 56 C ATOM 3962 OG1 THR B 248 82.841 -8.153 28.914 1.00 24.60 O ANISOU 3962 OG1 THR B 248 3777 3060 2511 -178 214 563 O ATOM 3963 CG2 THR B 248 80.674 -7.310 28.317 1.00 23.90 C ANISOU 3963 CG2 THR B 248 2851 3648 2584 -301 197 -111 C ATOM 3964 N SER B 249 85.191 -6.303 27.494 1.00 14.40 N ANISOU 3964 N SER B 249 1992 2091 1387 13 -33 1041 N ATOM 3965 CA SER B 249 86.531 -5.873 27.825 1.00 15.16 C ANISOU 3965 CA SER B 249 2038 2150 1572 -201 176 875 C ATOM 3966 C SER B 249 86.975 -4.659 27.002 1.00 14.47 C ANISOU 3966 C SER B 249 2124 1898 1477 -364 -157 688 C ATOM 3967 O SER B 249 87.986 -4.041 27.335 1.00 15.33 O ANISOU 3967 O SER B 249 2078 2174 1573 -408 -264 660 O ATOM 3968 CB SER B 249 87.566 -6.990 27.591 1.00 18.60 C ANISOU 3968 CB SER B 249 2406 2292 2369 75 11 783 C ATOM 3969 OG SER B 249 87.716 -7.265 26.191 1.00 22.40 O ANISOU 3969 OG SER B 249 2798 3062 2649 197 76 267 O ATOM 3970 N VAL B 250 86.266 -4.345 25.918 1.00 13.01 N ANISOU 3970 N VAL B 250 2022 1680 1241 -11 9 303 N ATOM 3971 CA VAL B 250 86.685 -3.227 25.085 1.00 11.26 C ANISOU 3971 CA VAL B 250 1913 1323 1043 -43 75 -34 C ATOM 3972 C VAL B 250 86.052 -1.919 25.545 1.00 9.61 C ANISOU 3972 C VAL B 250 1481 1242 927 -111 56 208 C ATOM 3973 O VAL B 250 84.834 -1.796 25.533 1.00 11.44 O ANISOU 3973 O VAL B 250 1448 1908 991 -100 393 214 O ATOM 3974 CB VAL B 250 86.297 -3.489 23.616 1.00 11.18 C ANISOU 3974 CB VAL B 250 1957 1270 1021 51 84 8 C ATOM 3975 CG1 VAL B 250 86.744 -2.294 22.760 1.00 11.63 C ANISOU 3975 CG1 VAL B 250 2136 951 1333 -7 44 -115 C ATOM 3976 CG2 VAL B 250 86.907 -4.785 23.126 1.00 11.39 C ANISOU 3976 CG2 VAL B 250 2123 855 1350 -171 -348 -38 C ATOM 3977 N GLY B 251 86.873 -0.965 25.969 1.00 9.22 N ANISOU 3977 N GLY B 251 1567 1546 389 -230 35 128 N ATOM 3978 CA GLY B 251 86.364 0.332 26.371 1.00 10.14 C ANISOU 3978 CA GLY B 251 1604 1843 406 260 -166 195 C ATOM 3979 C GLY B 251 85.850 1.077 25.118 1.00 9.43 C ANISOU 3979 C GLY B 251 1371 1809 403 221 231 419 C ATOM 3980 O GLY B 251 86.414 0.926 24.024 1.00 8.82 O ANISOU 3980 O GLY B 251 1325 1581 445 -239 304 140 O ATOM 3981 N LEU B 252 84.777 1.809 25.352 1.00 9.11 N ANISOU 3981 N LEU B 252 1506 1634 321 256 -99 -71 N ATOM 3982 CA LEU B 252 84.183 2.638 24.304 1.00 8.38 C ANISOU 3982 CA LEU B 252 1245 1373 565 161 -42 69 C ATOM 3983 C LEU B 252 84.274 4.065 24.838 1.00 8.95 C ANISOU 3983 C LEU B 252 1439 1478 481 -195 221 -49 C ATOM 3984 O LEU B 252 83.637 4.394 25.845 1.00 10.64 O ANISOU 3984 O LEU B 252 2018 1611 414 -137 210 -400 O ATOM 3985 CB LEU B 252 82.737 2.266 24.008 1.00 9.05 C ANISOU 3985 CB LEU B 252 1141 1476 822 401 -203 -97 C ATOM 3986 CG LEU B 252 82.462 0.781 23.759 1.00 9.97 C ANISOU 3986 CG LEU B 252 1312 1510 968 14 105 98 C ATOM 3987 CD1 LEU B 252 80.961 0.539 23.690 1.00 9.87 C ANISOU 3987 CD1 LEU B 252 1390 1946 414 -181 -47 -243 C ATOM 3988 CD2 LEU B 252 83.144 0.252 22.491 1.00 9.80 C ANISOU 3988 CD2 LEU B 252 1204 1461 1060 -82 35 -96 C ATOM 3989 N ILE B 253 85.087 4.911 24.194 1.00 7.66 N ANISOU 3989 N ILE B 253 1334 1186 392 -266 -105 -71 N ATOM 3990 CA ILE B 253 85.317 6.261 24.692 1.00 7.88 C ANISOU 3990 CA ILE B 253 1194 1009 793 163 -81 29 C ATOM 3991 C ILE B 253 84.874 7.260 23.624 1.00 7.46 C ANISOU 3991 C ILE B 253 1265 1029 539 42 116 57 C ATOM 3992 O ILE B 253 85.458 7.281 22.528 1.00 8.53 O ANISOU 3992 O ILE B 253 1117 1696 428 120 9 67 O ATOM 3993 CB ILE B 253 86.807 6.460 25.047 1.00 9.05 C ANISOU 3993 CB ILE B 253 1278 1354 809 -105 -189 358 C ATOM 3994 CG1 ILE B 253 87.241 5.393 26.070 1.00 9.14 C ANISOU 3994 CG1 ILE B 253 1275 1553 644 39 -243 289 C ATOM 3995 CG2 ILE B 253 87.025 7.873 25.541 1.00 9.47 C ANISOU 3995 CG2 ILE B 253 1259 1565 774 -163 -8 142 C ATOM 3996 CD1 ILE B 253 88.700 5.500 26.445 1.00 9.88 C ANISOU 3996 CD1 ILE B 253 1309 1647 798 -198 -197 62 C ATOM 3997 N GLY B 254 83.883 8.055 23.992 1.00 8.02 N ANISOU 3997 N GLY B 254 1312 1046 689 260 -409 -50 N ATOM 3998 CA GLY B 254 83.411 9.097 23.081 1.00 7.76 C ANISOU 3998 CA GLY B 254 1549 1014 386 255 -3 36 C ATOM 3999 C GLY B 254 83.948 10.445 23.530 1.00 7.97 C ANISOU 3999 C GLY B 254 1331 1422 277 -227 170 4 C ATOM 4000 O GLY B 254 83.963 10.767 24.732 1.00 10.04 O ANISOU 4000 O GLY B 254 1605 1951 260 -155 -50 -120 O ATOM 4001 N VAL B 255 84.392 11.271 22.591 1.00 7.63 N ANISOU 4001 N VAL B 255 1278 1192 430 -549 -264 104 N ATOM 4002 CA VAL B 255 85.007 12.542 22.914 1.00 7.27 C ANISOU 4002 CA VAL B 255 1639 825 299 -196 46 26 C ATOM 4003 C VAL B 255 84.218 13.714 22.350 1.00 8.65 C ANISOU 4003 C VAL B 255 1614 1246 426 76 -103 3 C ATOM 4004 O VAL B 255 84.135 13.862 21.123 1.00 9.03 O ANISOU 4004 O VAL B 255 1591 1473 366 4 -338 -68 O ATOM 4005 CB VAL B 255 86.451 12.613 22.372 1.00 8.08 C ANISOU 4005 CB VAL B 255 1573 946 549 3 34 -192 C ATOM 4006 CG1 VAL B 255 87.067 13.935 22.802 1.00 9.83 C ANISOU 4006 CG1 VAL B 255 1972 1184 580 -390 -261 -33 C ATOM 4007 CG2 VAL B 255 87.276 11.402 22.750 1.00 9.24 C ANISOU 4007 CG2 VAL B 255 2099 978 432 47 -301 -141 C ATOM 4008 N GLU B 256 83.582 14.478 23.234 1.00 7.96 N ANISOU 4008 N GLU B 256 1490 1023 512 -70 -85 38 N ATOM 4009 CA GLU B 256 82.853 15.662 22.835 1.00 7.63 C ANISOU 4009 CA GLU B 256 1344 1018 538 -49 -146 -38 C ATOM 4010 C GLU B 256 83.789 16.865 22.820 1.00 7.86 C ANISOU 4010 C GLU B 256 1444 949 593 -10 -11 -23 C ATOM 4011 O GLU B 256 84.803 16.888 23.541 1.00 9.25 O ANISOU 4011 O GLU B 256 1786 1288 441 197 -257 -146 O ATOM 4012 CB GLU B 256 81.726 15.937 23.829 1.00 8.27 C ANISOU 4012 CB GLU B 256 1350 930 861 251 -117 -109 C ATOM 4013 CG GLU B 256 80.714 14.813 23.994 1.00 10.05 C ANISOU 4013 CG GLU B 256 1432 1678 708 -180 57 -192 C ATOM 4014 CD GLU B 256 79.529 15.246 24.840 1.00 10.57 C ANISOU 4014 CD GLU B 256 1643 1858 516 -9 103 8 C ATOM 4015 OE1 GLU B 256 79.637 15.281 26.083 1.00 10.73 O ANISOU 4015 OE1 GLU B 256 1663 1933 481 -51 94 -377 O ATOM 4016 OE2 GLU B 256 78.461 15.570 24.260 1.00 10.49 O ANISOU 4016 OE2 GLU B 256 1757 1747 484 178 -1 -232 O ATOM 4017 N PRO B 257 83.479 17.889 22.053 1.00 9.15 N ANISOU 4017 N PRO B 257 1381 1254 844 140 -218 138 N ATOM 4018 CA PRO B 257 84.306 19.081 22.030 1.00 9.59 C ANISOU 4018 CA PRO B 257 1543 1367 734 -9 -91 107 C ATOM 4019 C PRO B 257 84.158 19.908 23.292 1.00 8.89 C ANISOU 4019 C PRO B 257 1329 1033 1016 -75 -105 22 C ATOM 4020 O PRO B 257 83.051 20.269 23.693 1.00 10.94 O ANISOU 4020 O PRO B 257 1204 1930 1022 -37 -273 -146 O ATOM 4021 CB PRO B 257 83.795 19.838 20.797 1.00 10.91 C ANISOU 4021 CB PRO B 257 1512 1628 1004 -1 -331 276 C ATOM 4022 CG PRO B 257 82.377 19.391 20.642 1.00 9.81 C ANISOU 4022 CG PRO B 257 1394 1280 1053 182 -157 207 C ATOM 4023 CD PRO B 257 82.324 17.959 21.112 1.00 10.94 C ANISOU 4023 CD PRO B 257 1778 1339 1038 263 -524 335 C ATOM 4024 N GLY B 258 85.302 20.194 23.901 1.00 9.55 N ANISOU 4024 N GLY B 258 1453 1312 866 116 -268 -74 N ATOM 4025 CA GLY B 258 85.319 21.028 25.096 1.00 9.98 C ANISOU 4025 CA GLY B 258 1489 1469 834 -49 -68 -128 C ATOM 4026 C GLY B 258 85.456 22.504 24.762 1.00 10.72 C ANISOU 4026 C GLY B 258 1625 1357 1092 126 -326 -253 C ATOM 4027 O GLY B 258 85.367 23.366 25.651 1.00 11.05 O ANISOU 4027 O GLY B 258 1898 1420 880 269 -58 -154 O ATOM 4028 N GLY B 259 85.645 22.838 23.483 1.00 10.38 N ANISOU 4028 N GLY B 259 1682 1031 1229 38 -397 -26 N ATOM 4029 CA GLY B 259 85.709 24.235 23.059 1.00 10.59 C ANISOU 4029 CA GLY B 259 1606 1074 1342 -130 -9 -55 C ATOM 4030 C GLY B 259 86.767 25.020 23.821 1.00 11.41 C ANISOU 4030 C GLY B 259 1591 1351 1392 38 -216 -171 C ATOM 4031 O GLY B 259 87.921 24.594 23.875 1.00 11.07 O ANISOU 4031 O GLY B 259 1606 925 1674 19 -25 -165 O ATOM 4032 N HIS B 260 86.364 26.168 24.384 1.00 11.17 N ANISOU 4032 N HIS B 260 1777 997 1469 -69 -377 28 N ATOM 4033 CA HIS B 260 87.344 26.952 25.138 1.00 13.36 C ANISOU 4033 CA HIS B 260 1804 1559 1711 -214 -373 -198 C ATOM 4034 C HIS B 260 87.530 26.437 26.561 1.00 14.36 C ANISOU 4034 C HIS B 260 2017 1692 1749 -303 -325 -144 C ATOM 4035 O HIS B 260 88.343 27.006 27.297 1.00 15.49 O ANISOU 4035 O HIS B 260 2356 2074 1455 -354 -463 -248 O ATOM 4036 CB HIS B 260 86.926 28.422 25.169 1.00 14.89 C ANISOU 4036 CB HIS B 260 2134 1593 1932 -157 -93 -83 C ATOM 4037 CG AHIS B 260 86.830 29.064 23.822 0.50 15.78 C ANISOU 4037 CG AHIS B 260 2142 1905 1947 -151 -173 9 C ATOM 4038 ND1AHIS B 260 85.740 29.776 23.376 0.50 17.90 N ANISOU 4038 ND1AHIS B 260 2529 1958 2313 11 -181 175 N ATOM 4039 CD2AHIS B 260 87.737 29.084 22.812 0.50 17.14 C ANISOU 4039 CD2AHIS B 260 2285 2154 2073 -103 -67 -63 C ATOM 4040 CE1AHIS B 260 85.975 30.209 22.152 0.50 16.49 C ANISOU 4040 CE1AHIS B 260 2135 1992 2139 -113 30 -80 C ATOM 4041 NE2AHIS B 260 87.177 29.804 21.782 0.50 18.12 N ANISOU 4041 NE2AHIS B 260 2218 2025 2641 48 -103 93 N ATOM 4042 CG BHIS B 260 86.936 29.032 23.796 0.50 13.71 C ANISOU 4042 CG BHIS B 260 1684 1616 1909 -77 -185 -48 C ATOM 4043 ND1BHIS B 260 88.047 28.955 22.978 0.50 14.12 N ANISOU 4043 ND1BHIS B 260 1837 1742 1787 -7 -135 45 N ATOM 4044 CD2BHIS B 260 86.010 29.723 23.100 0.50 15.02 C ANISOU 4044 CD2BHIS B 260 1945 1662 2101 20 -160 90 C ATOM 4045 CE1BHIS B 260 87.795 29.574 21.838 0.50 13.88 C ANISOU 4045 CE1BHIS B 260 1722 1544 2009 57 -5 191 C ATOM 4046 NE2BHIS B 260 86.556 30.048 21.890 0.50 14.15 N ANISOU 4046 NE2BHIS B 260 1684 1488 2205 -34 -66 -25 N ATOM 4047 N GLY B 261 86.781 25.422 26.923 1.00 12.62 N ANISOU 4047 N GLY B 261 1979 1640 1176 -227 -48 -300 N ATOM 4048 CA GLY B 261 86.842 24.793 28.237 1.00 12.89 C ANISOU 4048 CA GLY B 261 1893 1694 1311 -276 -1 -165 C ATOM 4049 C GLY B 261 85.429 24.655 28.799 1.00 11.80 C ANISOU 4049 C GLY B 261 1866 1551 1064 -109 -60 -235 C ATOM 4050 O GLY B 261 84.620 25.569 28.638 1.00 13.41 O ANISOU 4050 O GLY B 261 2080 1734 1281 89 -445 -511 O ATOM 4051 N ILE B 262 85.126 23.518 29.425 1.00 11.51 N ANISOU 4051 N ILE B 262 1928 1513 934 -269 -387 -301 N ATOM 4052 CA ILE B 262 83.778 23.315 29.932 1.00 13.77 C ANISOU 4052 CA ILE B 262 2112 1743 1376 -49 41 -234 C ATOM 4053 C ILE B 262 83.329 24.454 30.850 1.00 14.69 C ANISOU 4053 C ILE B 262 2297 1740 1545 -4 -35 -318 C ATOM 4054 O ILE B 262 82.202 24.939 30.772 1.00 14.90 O ANISOU 4054 O ILE B 262 2300 1630 1732 -43 240 -510 O ATOM 4055 CB ILE B 262 83.671 21.972 30.672 1.00 13.61 C ANISOU 4055 CB ILE B 262 1935 1819 1419 -20 185 -149 C ATOM 4056 CG1 ILE B 262 83.957 20.801 29.725 1.00 12.02 C ANISOU 4056 CG1 ILE B 262 1652 1375 1541 127 -479 -71 C ATOM 4057 CG2 ILE B 262 82.321 21.800 31.351 1.00 14.00 C ANISOU 4057 CG2 ILE B 262 1787 1974 1557 -212 109 -501 C ATOM 4058 CD1 ILE B 262 83.026 20.746 28.528 1.00 13.17 C ANISOU 4058 CD1 ILE B 262 1896 1669 1440 -39 -515 82 C ATOM 4059 N GLU B 263 84.249 24.920 31.691 1.00 16.22 N ANISOU 4059 N GLU B 263 2696 1817 1650 -107 -79 -630 N ATOM 4060 CA GLU B 263 83.899 25.971 32.658 1.00 17.29 C ANISOU 4060 CA GLU B 263 2746 1963 1860 174 25 -652 C ATOM 4061 C GLU B 263 83.522 27.292 32.019 1.00 18.03 C ANISOU 4061 C GLU B 263 2719 2128 2003 44 65 -380 C ATOM 4062 O GLU B 263 82.901 28.143 32.676 1.00 21.22 O ANISOU 4062 O GLU B 263 3483 2284 2297 72 371 -610 O ATOM 4063 CB GLU B 263 85.065 26.152 33.636 1.00 20.12 C ANISOU 4063 CB GLU B 263 2834 2582 2228 7 -146 -646 C ATOM 4064 CG GLU B 263 86.318 26.756 33.074 1.00 23.96 C ANISOU 4064 CG GLU B 263 3177 3022 2905 -280 -157 -259 C ATOM 4065 CD GLU B 263 87.135 25.956 32.089 1.00 24.46 C ANISOU 4065 CD GLU B 263 3015 3064 3214 -98 31 -49 C ATOM 4066 OE1 GLU B 263 87.019 24.712 31.991 1.00 23.43 O ANISOU 4066 OE1 GLU B 263 2661 3079 3162 82 -306 -749 O ATOM 4067 OE2 GLU B 263 87.939 26.611 31.379 1.00 25.70 O ANISOU 4067 OE2 GLU B 263 2735 3716 3314 -239 -210 248 O ATOM 4068 N THR B 264 83.908 27.521 30.767 1.00 15.92 N ANISOU 4068 N THR B 264 2729 1429 1892 -71 -30 -522 N ATOM 4069 CA THR B 264 83.575 28.741 30.061 1.00 15.29 C ANISOU 4069 CA THR B 264 2522 1507 1779 56 111 -538 C ATOM 4070 C THR B 264 82.151 28.703 29.522 1.00 16.68 C ANISOU 4070 C THR B 264 2438 1592 2308 291 116 -456 C ATOM 4071 O THR B 264 81.660 29.756 29.114 1.00 19.67 O ANISOU 4071 O THR B 264 3187 1720 2566 482 -52 -349 O ATOM 4072 CB THR B 264 84.478 29.027 28.846 1.00 14.52 C ANISOU 4072 CB THR B 264 2273 1342 1902 -204 -29 -295 C ATOM 4073 OG1 THR B 264 84.202 28.078 27.797 1.00 14.79 O ANISOU 4073 OG1 THR B 264 2249 1494 1875 91 -100 -435 O ATOM 4074 CG2 THR B 264 85.949 29.009 29.199 1.00 15.41 C ANISOU 4074 CG2 THR B 264 2227 1326 2302 -337 31 -403 C ATOM 4075 N GLY B 265 81.564 27.515 29.409 1.00 16.65 N ANISOU 4075 N GLY B 265 2052 1871 2402 31 109 -306 N ATOM 4076 CA GLY B 265 80.246 27.373 28.806 1.00 17.89 C ANISOU 4076 CA GLY B 265 2146 2409 2242 263 16 -267 C ATOM 4077 C GLY B 265 80.325 27.368 27.283 1.00 17.33 C ANISOU 4077 C GLY B 265 1982 2343 2257 -1 -12 -278 C ATOM 4078 O GLY B 265 79.305 27.115 26.626 1.00 20.00 O ANISOU 4078 O GLY B 265 1896 3111 2591 159 -205 -182 O ATOM 4079 N GLU B 266 81.487 27.676 26.718 1.00 16.02 N ANISOU 4079 N GLU B 266 1938 1974 2174 -17 -48 -390 N ATOM 4080 CA GLU B 266 81.664 27.702 25.269 1.00 14.77 C ANISOU 4080 CA GLU B 266 1621 1815 2178 94 -233 -277 C ATOM 4081 C GLU B 266 82.240 26.354 24.849 1.00 14.64 C ANISOU 4081 C GLU B 266 1841 1642 2078 20 -116 -105 C ATOM 4082 O GLU B 266 83.449 26.201 24.735 1.00 13.55 O ANISOU 4082 O GLU B 266 1731 1788 1630 -424 -223 -284 O ATOM 4083 CB GLU B 266 82.535 28.893 24.863 1.00 17.45 C ANISOU 4083 CB GLU B 266 1992 2063 2575 -1 -24 27 C ATOM 4084 CG GLU B 266 81.945 30.198 25.380 1.00 23.03 C ANISOU 4084 CG GLU B 266 2656 2448 3646 261 -12 -446 C ATOM 4085 CD GLU B 266 82.636 31.450 24.889 1.00 31.18 C ANISOU 4085 CD GLU B 266 3887 3330 4631 -268 212 117 C ATOM 4086 OE1 GLU B 266 83.575 31.364 24.077 1.00 33.53 O ANISOU 4086 OE1 GLU B 266 4070 3725 4946 -157 377 -4 O ATOM 4087 OE2 GLU B 266 82.212 32.545 25.331 1.00 34.78 O ANISOU 4087 OE2 GLU B 266 4427 3454 5333 -113 174 -40 O ATOM 4088 N HIS B 267 81.343 25.373 24.687 1.00 15.23 N ANISOU 4088 N HIS B 267 1836 1778 2172 -43 -28 -99 N ATOM 4089 CA HIS B 267 81.728 24.012 24.351 1.00 12.82 C ANISOU 4089 CA HIS B 267 1466 1448 1956 -399 -61 214 C ATOM 4090 C HIS B 267 80.598 23.361 23.552 1.00 10.78 C ANISOU 4090 C HIS B 267 1462 1276 1357 12 -124 199 C ATOM 4091 O HIS B 267 79.607 24.037 23.274 1.00 13.00 O ANISOU 4091 O HIS B 267 1438 1916 1585 118 -432 219 O ATOM 4092 CB HIS B 267 82.018 23.194 25.615 1.00 13.06 C ANISOU 4092 CB HIS B 267 1578 1734 1651 -351 -174 -43 C ATOM 4093 CG HIS B 267 80.867 23.070 26.555 1.00 12.41 C ANISOU 4093 CG HIS B 267 1897 1473 1344 -110 -60 -187 C ATOM 4094 ND1 HIS B 267 79.820 22.192 26.351 1.00 12.31 N ANISOU 4094 ND1 HIS B 267 1563 1763 1351 -22 -167 -324 N ATOM 4095 CD2 HIS B 267 80.601 23.705 27.723 1.00 13.17 C ANISOU 4095 CD2 HIS B 267 2110 1497 1395 21 -103 -223 C ATOM 4096 CE1 HIS B 267 78.952 22.304 27.341 1.00 12.64 C ANISOU 4096 CE1 HIS B 267 1577 1615 1609 -287 16 -196 C ATOM 4097 NE2 HIS B 267 79.415 23.217 28.203 1.00 14.01 N ANISOU 4097 NE2 HIS B 267 1576 1721 2028 100 -405 -450 N ATOM 4098 N GLY B 268 80.772 22.093 23.221 1.00 10.56 N ANISOU 4098 N GLY B 268 1589 1285 1137 -232 -83 117 N ATOM 4099 CA GLY B 268 79.761 21.326 22.520 1.00 11.30 C ANISOU 4099 CA GLY B 268 1307 1476 1510 -107 85 -263 C ATOM 4100 C GLY B 268 79.660 19.947 23.161 1.00 10.36 C ANISOU 4100 C GLY B 268 1507 1693 735 38 -141 -123 C ATOM 4101 O GLY B 268 79.667 18.912 22.475 1.00 10.47 O ANISOU 4101 O GLY B 268 1476 1877 624 10 -7 -200 O ATOM 4102 N ALA B 269 79.526 19.927 24.499 1.00 9.54 N ANISOU 4102 N ALA B 269 1401 1454 772 -1 80 -16 N ATOM 4103 CA ALA B 269 79.523 18.664 25.231 1.00 10.06 C ANISOU 4103 CA ALA B 269 1101 1534 1188 -78 -199 171 C ATOM 4104 C ALA B 269 78.229 18.461 26.007 1.00 9.76 C ANISOU 4104 C ALA B 269 1177 1865 665 -166 -231 -113 C ATOM 4105 O ALA B 269 78.201 18.349 27.240 1.00 9.90 O ANISOU 4105 O ALA B 269 1664 1445 652 -97 0 -205 O ATOM 4106 CB ALA B 269 80.702 18.560 26.193 1.00 10.61 C ANISOU 4106 CB ALA B 269 947 1822 1264 -191 -136 -110 C ATOM 4107 N PRO B 270 77.106 18.376 25.289 1.00 9.22 N ANISOU 4107 N PRO B 270 1100 1903 501 -157 -106 -258 N ATOM 4108 CA PRO B 270 75.828 18.172 25.931 1.00 9.71 C ANISOU 4108 CA PRO B 270 1088 1568 1035 -242 -26 -166 C ATOM 4109 C PRO B 270 75.693 16.849 26.657 1.00 9.52 C ANISOU 4109 C PRO B 270 1505 1378 735 177 -81 -319 C ATOM 4110 O PRO B 270 74.955 16.760 27.646 1.00 9.85 O ANISOU 4110 O PRO B 270 1200 1934 608 120 -251 -663 O ATOM 4111 CB PRO B 270 74.811 18.269 24.793 1.00 9.79 C ANISOU 4111 CB PRO B 270 459 1906 1356 6 72 -246 C ATOM 4112 CG PRO B 270 75.616 17.863 23.594 1.00 9.95 C ANISOU 4112 CG PRO B 270 1416 1775 591 -101 -25 -49 C ATOM 4113 CD PRO B 270 76.990 18.452 23.816 1.00 9.97 C ANISOU 4113 CD PRO B 270 1429 1802 557 4 -399 -235 C ATOM 4114 N LEU B 271 76.341 15.785 26.163 1.00 9.20 N ANISOU 4114 N LEU B 271 1344 1273 877 -7 109 -266 N ATOM 4115 CA LEU B 271 76.139 14.495 26.834 1.00 9.05 C ANISOU 4115 CA LEU B 271 1417 1369 654 44 -126 -155 C ATOM 4116 C LEU B 271 76.533 14.587 28.302 1.00 8.30 C ANISOU 4116 C LEU B 271 981 1659 515 193 197 -75 C ATOM 4117 O LEU B 271 75.774 14.169 29.177 1.00 10.23 O ANISOU 4117 O LEU B 271 1583 1808 494 -180 397 -197 O ATOM 4118 CB LEU B 271 76.868 13.361 26.115 1.00 10.73 C ANISOU 4118 CB LEU B 271 1986 1448 643 250 109 -65 C ATOM 4119 CG LEU B 271 76.444 11.940 26.480 1.00 10.39 C ANISOU 4119 CG LEU B 271 2007 1305 636 415 -357 -7 C ATOM 4120 CD1 LEU B 271 76.774 10.950 25.363 1.00 12.50 C ANISOU 4120 CD1 LEU B 271 2378 1592 779 173 -36 -234 C ATOM 4121 CD2 LEU B 271 77.095 11.418 27.753 1.00 12.16 C ANISOU 4121 CD2 LEU B 271 2320 1683 617 139 -519 58 C ATOM 4122 N LYS B 272 77.713 15.142 28.557 1.00 9.34 N ANISOU 4122 N LYS B 272 1481 1417 649 -174 -49 26 N ATOM 4123 CA LYS B 272 78.196 15.210 29.937 1.00 10.41 C ANISOU 4123 CA LYS B 272 1633 1482 842 132 -345 -255 C ATOM 4124 C LYS B 272 77.912 16.538 30.616 1.00 9.98 C ANISOU 4124 C LYS B 272 1606 1646 539 204 -55 -212 C ATOM 4125 O LYS B 272 78.059 16.580 31.850 1.00 13.56 O ANISOU 4125 O LYS B 272 2405 2272 476 136 -54 -172 O ATOM 4126 CB LYS B 272 79.697 14.897 29.981 1.00 10.68 C ANISOU 4126 CB LYS B 272 1637 1694 726 140 -362 -338 C ATOM 4127 CG LYS B 272 80.011 13.477 29.542 1.00 10.14 C ANISOU 4127 CG LYS B 272 1524 1384 946 133 -187 162 C ATOM 4128 CD LYS B 272 79.365 12.385 30.386 1.00 10.95 C ANISOU 4128 CD LYS B 272 1752 1959 449 4 -216 269 C ATOM 4129 CE LYS B 272 79.879 12.342 31.812 1.00 11.00 C ANISOU 4129 CE LYS B 272 1632 2070 479 10 -287 -283 C ATOM 4130 NZ LYS B 272 81.284 11.894 31.886 1.00 11.41 N ANISOU 4130 NZ LYS B 272 1701 2114 519 129 -412 -49 N ATOM 4131 N HIS B 273 77.554 17.575 29.870 1.00 10.08 N ANISOU 4131 N HIS B 273 1684 1416 730 255 -297 -435 N ATOM 4132 CA HIS B 273 77.401 18.888 30.484 1.00 11.21 C ANISOU 4132 CA HIS B 273 1684 1584 991 83 -6 -643 C ATOM 4133 C HIS B 273 76.154 19.608 30.030 1.00 16.16 C ANISOU 4133 C HIS B 273 1939 2011 2191 312 -481 -666 C ATOM 4134 O HIS B 273 76.131 20.834 30.115 1.00 21.55 O ANISOU 4134 O HIS B 273 2078 2015 4095 68 -1319 -683 O ATOM 4135 CB HIS B 273 78.634 19.761 30.189 1.00 12.51 C ANISOU 4135 CB HIS B 273 1689 1991 1074 -103 -168 -625 C ATOM 4136 CG HIS B 273 79.865 19.093 30.710 1.00 12.93 C ANISOU 4136 CG HIS B 273 1833 2054 1026 53 81 -265 C ATOM 4137 ND1 HIS B 273 80.207 19.055 32.044 1.00 14.55 N ANISOU 4137 ND1 HIS B 273 1767 2454 1308 -198 -447 -236 N ATOM 4138 CD2 HIS B 273 80.816 18.394 30.050 1.00 13.43 C ANISOU 4138 CD2 HIS B 273 1637 2096 1371 -105 297 -221 C ATOM 4139 CE1 HIS B 273 81.321 18.354 32.172 1.00 15.88 C ANISOU 4139 CE1 HIS B 273 1737 2469 1827 -154 -455 -414 C ATOM 4140 NE2 HIS B 273 81.726 17.962 30.978 1.00 16.42 N ANISOU 4140 NE2 HIS B 273 1848 2462 1929 -77 28 18 N ATOM 4141 N GLY B 274 75.154 18.894 29.563 1.00 13.95 N ANISOU 4141 N GLY B 274 1824 2003 1473 375 -258 -785 N ATOM 4142 CA GLY B 274 73.892 19.476 29.146 1.00 14.70 C ANISOU 4142 CA GLY B 274 1635 2146 1805 235 -142 -611 C ATOM 4143 C GLY B 274 72.812 19.046 30.135 1.00 16.95 C ANISOU 4143 C GLY B 274 1628 2652 2160 215 -116 -248 C ATOM 4144 O GLY B 274 73.108 18.689 31.273 1.00 20.16 O ANISOU 4144 O GLY B 274 1580 3884 2194 -95 -458 -285 O ATOM 4145 N ARG B 275 71.585 19.100 29.651 1.00 14.53 N ANISOU 4145 N ARG B 275 1676 2251 1594 -206 -227 -641 N ATOM 4146 CA ARG B 275 70.392 18.750 30.401 1.00 14.87 C ANISOU 4146 CA ARG B 275 1691 2214 1746 -289 -326 -466 C ATOM 4147 C ARG B 275 69.433 18.085 29.400 1.00 12.94 C ANISOU 4147 C ARG B 275 1507 1995 1414 -70 -441 -155 C ATOM 4148 O ARG B 275 69.363 18.541 28.263 1.00 12.81 O ANISOU 4148 O ARG B 275 1696 1722 1448 -5 -380 -222 O ATOM 4149 CB ARG B 275 69.768 19.999 30.981 1.00 18.23 C ANISOU 4149 CB ARG B 275 2630 2111 2185 114 -460 -363 C ATOM 4150 CG ARG B 275 68.800 19.978 32.124 1.00 21.20 C ANISOU 4150 CG ARG B 275 2728 2682 2643 164 -264 -201 C ATOM 4151 CD ARG B 275 68.916 21.299 32.902 1.00 20.13 C ANISOU 4151 CD ARG B 275 2978 2766 1904 386 -211 -203 C ATOM 4152 NE ARG B 275 68.571 22.467 32.085 1.00 17.90 N ANISOU 4152 NE ARG B 275 2544 2342 1914 432 -213 -574 N ATOM 4153 CZ ARG B 275 67.302 22.652 31.715 1.00 16.00 C ANISOU 4153 CZ ARG B 275 2483 2154 1442 -150 -372 -401 C ATOM 4154 NH1 ARG B 275 66.373 21.771 32.086 1.00 19.14 N ANISOU 4154 NH1 ARG B 275 2899 2440 1934 -305 -161 -186 N ATOM 4155 NH2 ARG B 275 66.957 23.690 30.971 1.00 17.96 N ANISOU 4155 NH2 ARG B 275 2671 1758 2397 -208 -421 -363 N ATOM 4156 N VAL B 276 68.801 17.021 29.863 1.00 12.57 N ANISOU 4156 N VAL B 276 1861 1640 1276 -229 -515 -646 N ATOM 4157 CA VAL B 276 67.899 16.315 28.927 1.00 12.49 C ANISOU 4157 CA VAL B 276 1596 1789 1359 -211 -677 -383 C ATOM 4158 C VAL B 276 66.777 17.250 28.504 1.00 12.78 C ANISOU 4158 C VAL B 276 1799 1608 1450 20 -418 -515 C ATOM 4159 O VAL B 276 66.208 18.011 29.292 1.00 12.72 O ANISOU 4159 O VAL B 276 1598 1700 1536 -63 -337 -598 O ATOM 4160 CB VAL B 276 67.339 15.039 29.544 1.00 14.44 C ANISOU 4160 CB VAL B 276 1516 1964 2005 -363 -712 -226 C ATOM 4161 CG1 VAL B 276 66.348 14.345 28.616 1.00 13.10 C ANISOU 4161 CG1 VAL B 276 1644 2010 1323 -406 -617 -28 C ATOM 4162 CG2 VAL B 276 68.460 14.075 29.901 1.00 16.53 C ANISOU 4162 CG2 VAL B 276 2527 1622 2131 108 -665 -261 C ATOM 4163 N GLY B 277 66.469 17.178 27.215 1.00 11.52 N ANISOU 4163 N GLY B 277 1321 1792 1266 235 -129 -325 N ATOM 4164 CA GLY B 277 65.380 17.940 26.621 1.00 10.20 C ANISOU 4164 CA GLY B 277 1378 1380 1117 180 -248 -574 C ATOM 4165 C GLY B 277 64.770 17.141 25.464 1.00 8.60 C ANISOU 4165 C GLY B 277 1272 1199 796 184 16 -396 C ATOM 4166 O GLY B 277 65.180 16.014 25.196 1.00 10.53 O ANISOU 4166 O GLY B 277 1772 1055 1173 282 -294 -328 O ATOM 4167 N ILE B 278 63.799 17.793 24.830 1.00 9.67 N ANISOU 4167 N ILE B 278 955 1599 1119 -173 -115 -41 N ATOM 4168 CA ILE B 278 63.149 17.179 23.672 1.00 10.61 C ANISOU 4168 CA ILE B 278 1404 1713 913 114 -248 -61 C ATOM 4169 C ILE B 278 63.286 18.146 22.502 1.00 11.85 C ANISOU 4169 C ILE B 278 1880 1532 1089 19 202 -115 C ATOM 4170 O ILE B 278 62.765 19.262 22.553 1.00 12.57 O ANISOU 4170 O ILE B 278 2140 1478 1160 44 -13 -384 O ATOM 4171 CB ILE B 278 61.665 16.901 23.940 1.00 10.71 C ANISOU 4171 CB ILE B 278 1452 1718 898 -88 -204 -105 C ATOM 4172 CG1 ILE B 278 61.512 15.881 25.071 1.00 11.21 C ANISOU 4172 CG1 ILE B 278 1333 1973 954 14 17 12 C ATOM 4173 CG2 ILE B 278 60.970 16.389 22.673 1.00 12.12 C ANISOU 4173 CG2 ILE B 278 1734 2057 813 338 -227 -374 C ATOM 4174 CD1 ILE B 278 60.070 15.733 25.539 1.00 11.51 C ANISOU 4174 CD1 ILE B 278 1294 2224 854 17 -34 -293 C ATOM 4175 N TYR B 279 64.026 17.751 21.465 1.00 10.30 N ANISOU 4175 N TYR B 279 2012 1269 633 225 -53 -5 N ATOM 4176 CA TYR B 279 64.229 18.636 20.312 1.00 10.91 C ANISOU 4176 CA TYR B 279 2158 1210 778 35 271 -84 C ATOM 4177 C TYR B 279 64.760 17.760 19.177 1.00 10.98 C ANISOU 4177 C TYR B 279 2013 1453 706 245 313 35 C ATOM 4178 O TYR B 279 65.313 16.688 19.421 1.00 11.15 O ANISOU 4178 O TYR B 279 1867 1443 927 107 161 120 O ATOM 4179 CB TYR B 279 65.196 19.776 20.684 1.00 14.25 C ANISOU 4179 CB TYR B 279 2396 1647 1371 -391 78 159 C ATOM 4180 CG TYR B 279 65.747 20.420 19.419 1.00 16.12 C ANISOU 4180 CG TYR B 279 2749 2145 1232 -75 159 176 C ATOM 4181 CD1 TYR B 279 64.866 21.128 18.605 1.00 16.35 C ANISOU 4181 CD1 TYR B 279 2670 1923 1618 -90 -23 82 C ATOM 4182 CD2 TYR B 279 67.056 20.256 19.018 1.00 18.41 C ANISOU 4182 CD2 TYR B 279 2634 2294 2066 -258 123 305 C ATOM 4183 CE1 TYR B 279 65.312 21.680 17.413 1.00 17.56 C ANISOU 4183 CE1 TYR B 279 2860 2220 1593 -157 115 34 C ATOM 4184 CE2 TYR B 279 67.515 20.815 17.830 1.00 19.48 C ANISOU 4184 CE2 TYR B 279 2835 2580 1988 49 72 461 C ATOM 4185 CZ TYR B 279 66.624 21.523 17.047 1.00 18.52 C ANISOU 4185 CZ TYR B 279 2751 2550 1737 -143 -11 344 C ATOM 4186 OH TYR B 279 67.076 22.057 15.854 1.00 19.71 O ANISOU 4186 OH TYR B 279 2979 2652 1857 -587 -116 533 O ATOM 4187 N PHE B 280 64.508 18.207 17.956 1.00 12.52 N ANISOU 4187 N PHE B 280 2490 1667 599 190 263 -37 N ATOM 4188 CA PHE B 280 64.940 17.464 16.771 1.00 12.23 C ANISOU 4188 CA PHE B 280 2091 1777 779 95 393 -110 C ATOM 4189 C PHE B 280 64.415 16.038 16.794 1.00 10.09 C ANISOU 4189 C PHE B 280 1495 1682 656 306 312 55 C ATOM 4190 O PHE B 280 65.052 15.085 16.338 1.00 11.53 O ANISOU 4190 O PHE B 280 1660 2010 709 486 416 -48 O ATOM 4191 CB PHE B 280 66.445 17.528 16.573 1.00 13.99 C ANISOU 4191 CB PHE B 280 2108 1763 1446 -98 452 -139 C ATOM 4192 CG PHE B 280 66.949 17.053 15.232 1.00 14.50 C ANISOU 4192 CG PHE B 280 2217 2037 1255 97 189 -63 C ATOM 4193 CD1 PHE B 280 66.369 17.506 14.059 1.00 16.17 C ANISOU 4193 CD1 PHE B 280 2651 2302 1191 222 263 126 C ATOM 4194 CD2 PHE B 280 68.022 16.196 15.173 1.00 15.69 C ANISOU 4194 CD2 PHE B 280 2335 2102 1526 171 416 118 C ATOM 4195 CE1 PHE B 280 66.848 17.079 12.824 1.00 16.26 C ANISOU 4195 CE1 PHE B 280 2459 2244 1475 527 310 -33 C ATOM 4196 CE2 PHE B 280 68.509 15.763 13.943 1.00 16.14 C ANISOU 4196 CE2 PHE B 280 2567 2035 1529 379 78 -286 C ATOM 4197 CZ PHE B 280 67.923 16.211 12.774 1.00 15.68 C ANISOU 4197 CZ PHE B 280 2291 1888 1780 287 192 133 C ATOM 4198 N GLY B 281 63.188 15.890 17.297 1.00 10.48 N ANISOU 4198 N GLY B 281 1442 2031 510 82 172 181 N ATOM 4199 CA GLY B 281 62.522 14.617 17.286 1.00 10.72 C ANISOU 4199 CA GLY B 281 1540 1760 773 259 52 66 C ATOM 4200 C GLY B 281 62.935 13.571 18.283 1.00 8.56 C ANISOU 4200 C GLY B 281 1449 1141 663 376 17 -384 C ATOM 4201 O GLY B 281 62.481 12.431 18.224 1.00 10.95 O ANISOU 4201 O GLY B 281 1625 1503 1033 15 -221 -447 O ATOM 4202 N MET B 282 63.733 13.992 19.273 1.00 9.97 N ANISOU 4202 N MET B 282 1375 1843 569 399 -210 -16 N ATOM 4203 CA MET B 282 64.223 13.039 20.251 1.00 9.22 C ANISOU 4203 CA MET B 282 1371 1477 656 317 -114 -74 C ATOM 4204 C MET B 282 64.375 13.637 21.648 1.00 8.59 C ANISOU 4204 C MET B 282 1470 1166 626 258 -56 -6 C ATOM 4205 O MET B 282 64.478 14.850 21.803 1.00 9.78 O ANISOU 4205 O MET B 282 1722 1171 822 224 -48 248 O ATOM 4206 CB MET B 282 65.609 12.539 19.817 1.00 10.27 C ANISOU 4206 CB MET B 282 1581 1316 1007 372 125 -94 C ATOM 4207 CG MET B 282 66.637 13.641 19.680 1.00 10.00 C ANISOU 4207 CG MET B 282 1280 1851 668 177 -145 -188 C ATOM 4208 SD MET B 282 68.300 13.008 19.360 1.00 10.00 S ANISOU 4208 SD MET B 282 1480 1949 369 389 -91 -111 S ATOM 4209 CE MET B 282 69.256 14.507 19.496 1.00 12.66 C ANISOU 4209 CE MET B 282 1993 2258 557 -11 -53 163 C ATOM 4210 N LYS B 283 64.327 12.742 22.626 1.00 8.76 N ANISOU 4210 N LYS B 283 1583 1197 549 89 -281 -34 N ATOM 4211 CA LYS B 283 64.621 13.077 24.016 1.00 8.46 C ANISOU 4211 CA LYS B 283 1039 1615 558 242 -240 -47 C ATOM 4212 C LYS B 283 66.104 12.718 24.216 1.00 7.92 C ANISOU 4212 C LYS B 283 997 1244 769 109 -265 -132 C ATOM 4213 O LYS B 283 66.534 11.558 24.069 1.00 8.60 O ANISOU 4213 O LYS B 283 1360 1172 735 53 -399 -309 O ATOM 4214 CB LYS B 283 63.743 12.257 24.949 1.00 10.57 C ANISOU 4214 CB LYS B 283 1460 1952 603 167 -36 47 C ATOM 4215 CG LYS B 283 64.039 12.612 26.412 1.00 10.35 C ANISOU 4215 CG LYS B 283 1574 1737 623 -126 27 -70 C ATOM 4216 CD LYS B 283 63.072 11.863 27.314 1.00 12.26 C ANISOU 4216 CD LYS B 283 1568 1982 1110 -380 -52 132 C ATOM 4217 CE LYS B 283 61.692 12.514 27.246 1.00 12.01 C ANISOU 4217 CE LYS B 283 1587 2051 927 -278 347 -263 C ATOM 4218 NZ LYS B 283 60.726 11.796 28.118 1.00 14.68 N ANISOU 4218 NZ LYS B 283 2516 1736 1325 -437 1039 -609 N ATOM 4219 N ALA B 284 66.936 13.703 24.530 1.00 8.93 N ANISOU 4219 N ALA B 284 1207 1752 432 -237 -197 -117 N ATOM 4220 CA ALA B 284 68.372 13.516 24.650 1.00 8.63 C ANISOU 4220 CA ALA B 284 1173 1511 597 -337 -320 -320 C ATOM 4221 C ALA B 284 68.971 14.704 25.391 1.00 8.51 C ANISOU 4221 C ALA B 284 1113 1178 942 -84 -475 -294 C ATOM 4222 O ALA B 284 68.357 15.761 25.474 1.00 10.01 O ANISOU 4222 O ALA B 284 1393 983 1427 -148 -400 -359 O ATOM 4223 CB ALA B 284 68.982 13.429 23.235 1.00 9.50 C ANISOU 4223 CB ALA B 284 1286 1641 685 58 -233 77 C ATOM 4224 N PRO B 285 70.193 14.567 25.887 1.00 9.79 N ANISOU 4224 N PRO B 285 903 1566 1249 -146 -320 -246 N ATOM 4225 CA PRO B 285 70.893 15.699 26.484 1.00 11.20 C ANISOU 4225 CA PRO B 285 1266 1309 1681 -68 -557 -233 C ATOM 4226 C PRO B 285 71.088 16.810 25.460 1.00 10.36 C ANISOU 4226 C PRO B 285 1202 1073 1662 -246 -129 -455 C ATOM 4227 O PRO B 285 71.453 16.541 24.306 1.00 13.09 O ANISOU 4227 O PRO B 285 1325 1898 1751 -291 133 -337 O ATOM 4228 CB PRO B 285 72.240 15.122 26.870 1.00 13.17 C ANISOU 4228 CB PRO B 285 1092 1604 2308 -170 -607 -259 C ATOM 4229 CG PRO B 285 72.190 13.654 26.702 1.00 12.88 C ANISOU 4229 CG PRO B 285 1691 1638 1565 -63 -630 -431 C ATOM 4230 CD PRO B 285 71.001 13.340 25.860 1.00 10.73 C ANISOU 4230 CD PRO B 285 1096 1709 1274 22 -236 -293 C ATOM 4231 N MET B 286 70.834 18.058 25.835 1.00 11.97 N ANISOU 4231 N MET B 286 1700 1005 1845 -34 349 -219 N ATOM 4232 CA MET B 286 70.847 19.194 24.932 1.00 15.22 C ANISOU 4232 CA MET B 286 2284 1106 2396 -37 141 26 C ATOM 4233 C MET B 286 71.687 20.344 25.509 1.00 14.92 C ANISOU 4233 C MET B 286 1523 1389 2756 292 -293 -8 C ATOM 4234 O MET B 286 71.715 20.442 26.725 1.00 15.55 O ANISOU 4234 O MET B 286 1415 1567 2928 -360 -968 -638 O ATOM 4235 CB MET B 286 69.418 19.827 24.888 1.00 16.86 C ANISOU 4235 CB MET B 286 2431 1687 2287 126 -43 470 C ATOM 4236 CG MET B 286 68.228 19.100 24.336 1.00 19.97 C ANISOU 4236 CG MET B 286 2968 2032 2587 -642 707 -14 C ATOM 4237 SD MET B 286 68.483 18.677 22.586 1.00 19.34 S ANISOU 4237 SD MET B 286 1931 2880 2537 -280 314 -158 S ATOM 4238 CE MET B 286 67.369 17.272 22.526 1.00 17.90 C ANISOU 4238 CE MET B 286 1498 2795 2509 -122 -307 230 C ATOM 4239 N MET B 287 72.209 21.178 24.649 1.00 15.50 N ANISOU 4239 N MET B 287 1195 1478 3216 57 -178 -22 N ATOM 4240 CA MET B 287 72.743 22.480 25.007 1.00 18.72 C ANISOU 4240 CA MET B 287 1829 1453 3830 -4 -63 -90 C ATOM 4241 C MET B 287 71.472 23.374 25.080 1.00 14.60 C ANISOU 4241 C MET B 287 1263 1271 3012 -436 6 43 C ATOM 4242 O MET B 287 70.849 23.585 24.034 1.00 16.67 O ANISOU 4242 O MET B 287 1213 1529 3592 360 -149 303 O ATOM 4243 CB MET B 287 73.626 23.071 23.923 1.00 19.68 C ANISOU 4243 CB MET B 287 1818 1906 3754 65 -50 -58 C ATOM 4244 CG MET B 287 74.823 22.305 23.406 1.00 18.35 C ANISOU 4244 CG MET B 287 1503 2336 3132 369 -860 -109 C ATOM 4245 SD MET B 287 76.159 22.236 24.593 1.00 20.65 S ANISOU 4245 SD MET B 287 2174 2003 3669 1001 -1637 -1618 S ATOM 4246 CE MET B 287 76.654 23.911 24.911 1.00 16.35 C ANISOU 4246 CE MET B 287 1641 2066 2503 -217 -278 43 C ATOM 4247 N GLN B 288 71.077 23.839 26.249 1.00 16.25 N ANISOU 4247 N GLN B 288 1255 1424 3497 54 -2 -373 N ATOM 4248 CA GLN B 288 69.868 24.668 26.341 1.00 14.97 C ANISOU 4248 CA GLN B 288 1655 1086 2948 222 -48 -254 C ATOM 4249 C GLN B 288 69.945 25.642 27.505 1.00 15.85 C ANISOU 4249 C GLN B 288 1794 1745 2482 -106 -433 -179 C ATOM 4250 O GLN B 288 70.715 25.475 28.448 1.00 17.77 O ANISOU 4250 O GLN B 288 1999 1669 3084 79 -1000 -693 O ATOM 4251 CB GLN B 288 68.608 23.806 26.481 1.00 15.69 C ANISOU 4251 CB GLN B 288 1751 1534 2678 8 -197 -70 C ATOM 4252 CG GLN B 288 68.649 22.836 27.656 1.00 16.03 C ANISOU 4252 CG GLN B 288 1728 1995 2369 -125 -626 -45 C ATOM 4253 CD GLN B 288 67.349 22.095 27.892 1.00 14.87 C ANISOU 4253 CD GLN B 288 1613 1656 2382 20 -683 -203 C ATOM 4254 OE1 GLN B 288 66.286 22.705 27.778 1.00 16.44 O ANISOU 4254 OE1 GLN B 288 1205 1819 3223 -264 -811 -1013 O ATOM 4255 NE2 GLN B 288 67.380 20.802 28.218 1.00 14.16 N ANISOU 4255 NE2 GLN B 288 1456 1523 2401 -193 -964 -481 N ATOM 4256 N THR B 289 69.189 26.724 27.395 1.00 14.62 N ANISOU 4256 N THR B 289 1290 1612 2652 -320 -382 -408 N ATOM 4257 CA THR B 289 69.133 27.734 28.447 1.00 14.78 C ANISOU 4257 CA THR B 289 1476 1673 2466 -39 -322 -317 C ATOM 4258 C THR B 289 68.356 27.190 29.640 1.00 14.60 C ANISOU 4258 C THR B 289 1476 1642 2430 -136 -459 -197 C ATOM 4259 O THR B 289 67.680 26.154 29.527 1.00 15.55 O ANISOU 4259 O THR B 289 1431 1410 3067 63 -696 -327 O ATOM 4260 CB THR B 289 68.455 29.034 27.968 1.00 14.75 C ANISOU 4260 CB THR B 289 1415 1518 2670 -131 -365 -410 C ATOM 4261 OG1 THR B 289 67.070 28.732 27.712 1.00 16.44 O ANISOU 4261 OG1 THR B 289 1426 1949 2870 -22 -612 -682 O ATOM 4262 CG2 THR B 289 69.123 29.632 26.759 1.00 15.50 C ANISOU 4262 CG2 THR B 289 2186 1463 2239 -178 -579 -472 C ATOM 4263 N ALA B 290 68.374 27.860 30.786 1.00 16.16 N ANISOU 4263 N ALA B 290 1486 2171 2483 -46 -585 -401 N ATOM 4264 CA ALA B 290 67.648 27.402 31.958 1.00 16.76 C ANISOU 4264 CA ALA B 290 1776 2077 2514 -445 -599 -503 C ATOM 4265 C ALA B 290 66.135 27.316 31.674 1.00 15.81 C ANISOU 4265 C ALA B 290 1686 2078 2242 -221 -427 -524 C ATOM 4266 O ALA B 290 65.478 26.499 32.310 1.00 17.01 O ANISOU 4266 O ALA B 290 1380 2481 2601 -620 -547 -687 O ATOM 4267 CB ALA B 290 67.916 28.261 33.185 1.00 17.50 C ANISOU 4267 CB ALA B 290 2016 2218 2415 -78 -556 -533 C ATOM 4268 N ASP B 291 65.638 28.128 30.761 1.00 15.80 N ANISOU 4268 N ASP B 291 1567 2009 2427 -163 -537 -620 N ATOM 4269 CA ASP B 291 64.261 28.211 30.361 1.00 16.32 C ANISOU 4269 CA ASP B 291 1700 2508 1994 -85 -518 -233 C ATOM 4270 C ASP B 291 63.836 27.216 29.284 1.00 16.17 C ANISOU 4270 C ASP B 291 1559 2137 2447 218 -254 -507 C ATOM 4271 O ASP B 291 62.656 27.198 28.953 1.00 16.36 O ANISOU 4271 O ASP B 291 1391 2410 2415 -58 -2 -729 O ATOM 4272 CB ASP B 291 64.062 29.559 29.632 1.00 22.04 C ANISOU 4272 CB ASP B 291 2727 2711 2937 478 -824 -48 C ATOM 4273 CG ASP B 291 63.720 30.710 30.529 1.00 22.29 C ANISOU 4273 CG ASP B 291 2433 2920 3117 277 -321 -99 C ATOM 4274 OD1 ASP B 291 63.696 30.489 31.756 1.00 28.70 O ANISOU 4274 OD1 ASP B 291 3674 3971 3260 116 -108 5 O ATOM 4275 OD2 ASP B 291 63.504 31.764 29.901 1.00 20.27 O ANISOU 4275 OD2 ASP B 291 1843 3000 2858 75 -454 -39 O ATOM 4276 N GLY B 292 64.801 26.508 28.707 1.00 13.46 N ANISOU 4276 N GLY B 292 1405 1569 2141 22 -423 -576 N ATOM 4277 CA GLY B 292 64.468 25.546 27.677 1.00 13.17 C ANISOU 4277 CA GLY B 292 1503 1514 1987 -78 -482 -421 C ATOM 4278 C GLY B 292 64.659 26.004 26.248 1.00 13.54 C ANISOU 4278 C GLY B 292 1482 1518 2146 -235 -125 -329 C ATOM 4279 O GLY B 292 64.161 25.318 25.336 1.00 15.25 O ANISOU 4279 O GLY B 292 2090 1412 2292 -98 -499 -389 O ATOM 4280 N GLN B 293 65.390 27.079 25.972 1.00 14.24 N ANISOU 4280 N GLN B 293 1878 1174 2360 -137 -369 -164 N ATOM 4281 CA GLN B 293 65.654 27.483 24.592 1.00 14.66 C ANISOU 4281 CA GLN B 293 1715 1483 2371 -72 -62 -276 C ATOM 4282 C GLN B 293 66.893 26.721 24.122 1.00 14.12 C ANISOU 4282 C GLN B 293 1409 1466 2490 -231 -250 -375 C ATOM 4283 O GLN B 293 67.812 26.606 24.935 1.00 15.86 O ANISOU 4283 O GLN B 293 1691 1270 3066 370 -591 -549 O ATOM 4284 CB GLN B 293 65.837 28.984 24.468 1.00 14.03 C ANISOU 4284 CB GLN B 293 1513 1445 2373 45 106 -342 C ATOM 4285 CG GLN B 293 64.696 29.824 25.034 1.00 13.10 C ANISOU 4285 CG GLN B 293 1543 1023 2412 40 -26 -316 C ATOM 4286 CD GLN B 293 63.364 29.654 24.349 1.00 11.49 C ANISOU 4286 CD GLN B 293 1663 1200 1501 53 97 -473 C ATOM 4287 OE1 GLN B 293 63.214 28.950 23.344 1.00 12.67 O ANISOU 4287 OE1 GLN B 293 2064 1280 1471 148 -298 -424 O ATOM 4288 NE2 GLN B 293 62.323 30.273 24.929 1.00 13.10 N ANISOU 4288 NE2 GLN B 293 1645 1131 2202 414 -47 -341 N ATOM 4289 N ILE B 294 66.918 26.192 22.913 1.00 15.22 N ANISOU 4289 N ILE B 294 1739 1822 2220 133 281 -91 N ATOM 4290 CA ILE B 294 68.081 25.437 22.444 1.00 16.19 C ANISOU 4290 CA ILE B 294 1715 1951 2484 84 399 -36 C ATOM 4291 C ILE B 294 69.197 26.407 22.062 1.00 18.76 C ANISOU 4291 C ILE B 294 1888 2133 3108 1 519 202 C ATOM 4292 O ILE B 294 68.944 27.456 21.475 1.00 19.68 O ANISOU 4292 O ILE B 294 1808 2373 3296 178 425 307 O ATOM 4293 CB ILE B 294 67.727 24.566 21.226 1.00 16.67 C ANISOU 4293 CB ILE B 294 2045 1988 2300 131 258 69 C ATOM 4294 CG1 ILE B 294 66.430 23.787 21.481 1.00 16.14 C ANISOU 4294 CG1 ILE B 294 2331 1633 2168 2 214 -10 C ATOM 4295 CG2 ILE B 294 68.879 23.636 20.875 1.00 17.94 C ANISOU 4295 CG2 ILE B 294 2311 1930 2574 146 413 -49 C ATOM 4296 CD1 ILE B 294 66.511 22.822 22.640 1.00 15.67 C ANISOU 4296 CD1 ILE B 294 2374 1752 1829 -430 201 -150 C ATOM 4297 N GLU B 295 70.420 26.011 22.374 1.00 20.74 N ANISOU 4297 N GLU B 295 2139 2096 3643 3 80 321 N ATOM 4298 CA GLU B 295 71.602 26.820 22.073 1.00 21.83 C ANISOU 4298 CA GLU B 295 2415 2363 3518 -177 264 198 C ATOM 4299 C GLU B 295 72.557 26.112 21.136 1.00 21.52 C ANISOU 4299 C GLU B 295 2325 2516 3335 155 34 239 C ATOM 4300 O GLU B 295 72.377 24.933 20.850 1.00 21.63 O ANISOU 4300 O GLU B 295 2683 2500 3035 336 213 330 O ATOM 4301 CB GLU B 295 72.235 27.112 23.435 1.00 24.07 C ANISOU 4301 CB GLU B 295 2573 2763 3809 -279 56 -162 C ATOM 4302 CG GLU B 295 71.350 28.018 24.295 1.00 27.15 C ANISOU 4302 CG GLU B 295 3041 3195 4081 -13 137 -260 C ATOM 4303 CD GLU B 295 72.133 28.498 25.508 1.00 29.12 C ANISOU 4303 CD GLU B 295 3363 3690 4012 15 -28 -139 C ATOM 4304 OE1 GLU B 295 72.467 27.660 26.364 1.00 31.27 O ANISOU 4304 OE1 GLU B 295 3551 3953 4379 157 200 183 O ATOM 4305 OE2 GLU B 295 72.416 29.705 25.585 1.00 31.24 O ANISOU 4305 OE2 GLU B 295 3354 3820 4695 -211 2 -47 O ATOM 4306 N GLU B 296 73.535 26.813 20.568 1.00 24.58 N ANISOU 4306 N GLU B 296 2817 3089 3435 77 389 291 N ATOM 4307 CA GLU B 296 74.479 26.192 19.641 1.00 24.27 C ANISOU 4307 CA GLU B 296 2211 3445 3566 177 82 157 C ATOM 4308 C GLU B 296 75.616 25.499 20.392 1.00 24.32 C ANISOU 4308 C GLU B 296 2410 3598 3232 193 -40 145 C ATOM 4309 O GLU B 296 75.833 25.842 21.550 1.00 25.52 O ANISOU 4309 O GLU B 296 1818 4330 3548 218 -50 -293 O ATOM 4310 CB GLU B 296 75.128 27.269 18.771 1.00 27.39 C ANISOU 4310 CB GLU B 296 3144 3488 3777 -140 -32 267 C ATOM 4311 CG GLU B 296 74.193 28.015 17.836 1.00 28.97 C ANISOU 4311 CG GLU B 296 3273 3594 4139 137 -151 148 C ATOM 4312 CD GLU B 296 74.791 29.375 17.489 1.00 31.62 C ANISOU 4312 CD GLU B 296 3838 3804 4374 -112 88 118 C ATOM 4313 OE1 GLU B 296 75.636 29.433 16.575 1.00 34.12 O ANISOU 4313 OE1 GLU B 296 4540 4115 4308 -347 284 135 O ATOM 4314 OE2 GLU B 296 74.408 30.348 18.164 1.00 33.29 O ANISOU 4314 OE2 GLU B 296 4097 3898 4653 -94 -50 -51 O ATOM 4315 N SER B 297 76.275 24.544 19.746 1.00 22.14 N ANISOU 4315 N SER B 297 2048 3267 3099 -64 -231 268 N ATOM 4316 CA SER B 297 77.475 23.971 20.364 1.00 20.10 C ANISOU 4316 CA SER B 297 1818 2944 2876 -50 14 173 C ATOM 4317 C SER B 297 78.657 24.813 19.833 1.00 20.60 C ANISOU 4317 C SER B 297 2105 3219 2502 -371 -305 486 C ATOM 4318 O SER B 297 78.583 25.226 18.653 1.00 22.92 O ANISOU 4318 O SER B 297 1764 3956 2990 -229 -543 1199 O ATOM 4319 CB SER B 297 77.708 22.525 19.954 1.00 23.06 C ANISOU 4319 CB SER B 297 2700 2843 3219 -365 190 254 C ATOM 4320 OG SER B 297 76.933 21.591 20.683 1.00 23.33 O ANISOU 4320 OG SER B 297 2883 2626 3355 -444 548 -89 O ATOM 4321 N TYR B 298 79.689 25.085 20.622 1.00 15.14 N ANISOU 4321 N TYR B 298 1833 2257 1662 89 145 -18 N ATOM 4322 CA TYR B 298 80.850 25.803 20.147 1.00 14.19 C ANISOU 4322 CA TYR B 298 1833 1722 1836 108 -127 -72 C ATOM 4323 C TYR B 298 82.048 24.850 20.093 1.00 12.77 C ANISOU 4323 C TYR B 298 1720 1923 1210 122 -2 43 C ATOM 4324 O TYR B 298 82.263 24.074 21.030 1.00 12.21 O ANISOU 4324 O TYR B 298 1636 1720 1285 -82 -167 19 O ATOM 4325 CB TYR B 298 81.282 27.044 21.009 1.00 13.47 C ANISOU 4325 CB TYR B 298 1754 1884 1481 317 -174 -182 C ATOM 4326 CG TYR B 298 82.703 27.354 20.542 1.00 14.59 C ANISOU 4326 CG TYR B 298 1793 1924 1826 65 -326 93 C ATOM 4327 CD1 TYR B 298 82.957 27.986 19.343 1.00 15.66 C ANISOU 4327 CD1 TYR B 298 2088 1850 2013 402 54 186 C ATOM 4328 CD2 TYR B 298 83.786 26.931 21.305 1.00 13.12 C ANISOU 4328 CD2 TYR B 298 1485 1589 1910 137 -228 -122 C ATOM 4329 CE1 TYR B 298 84.239 28.203 18.896 1.00 15.53 C ANISOU 4329 CE1 TYR B 298 1887 1976 2038 107 -447 359 C ATOM 4330 CE2 TYR B 298 85.084 27.112 20.860 1.00 12.51 C ANISOU 4330 CE2 TYR B 298 1732 1411 1609 -161 -39 -35 C ATOM 4331 CZ TYR B 298 85.308 27.758 19.667 1.00 14.72 C ANISOU 4331 CZ TYR B 298 2005 1858 1731 83 -410 302 C ATOM 4332 OH TYR B 298 86.563 27.947 19.167 1.00 15.92 O ANISOU 4332 OH TYR B 298 2217 1936 1897 -191 -308 600 O ATOM 4333 N SER B 299 82.826 24.891 19.017 1.00 12.55 N ANISOU 4333 N SER B 299 2058 1730 979 204 -11 -74 N ATOM 4334 CA SER B 299 84.069 24.160 18.898 1.00 12.29 C ANISOU 4334 CA SER B 299 1973 1648 1049 4 335 -237 C ATOM 4335 C SER B 299 84.942 24.805 17.815 1.00 12.51 C ANISOU 4335 C SER B 299 1991 1552 1211 -67 110 110 C ATOM 4336 O SER B 299 84.375 25.375 16.874 1.00 14.96 O ANISOU 4336 O SER B 299 2122 2210 1352 256 44 262 O ATOM 4337 CB SER B 299 83.884 22.688 18.501 1.00 12.32 C ANISOU 4337 CB SER B 299 1997 1512 1174 29 -128 27 C ATOM 4338 OG SER B 299 85.112 21.999 18.338 1.00 11.29 O ANISOU 4338 OG SER B 299 2306 1199 785 127 47 -61 O ATOM 4339 N ILE B 300 86.246 24.687 17.948 1.00 12.92 N ANISOU 4339 N ILE B 300 1980 1722 1208 -184 160 13 N ATOM 4340 CA ILE B 300 87.148 25.098 16.877 1.00 14.27 C ANISOU 4340 CA ILE B 300 2140 1882 1399 -302 268 117 C ATOM 4341 C ILE B 300 86.818 24.310 15.611 1.00 14.99 C ANISOU 4341 C ILE B 300 2343 2017 1336 -449 104 244 C ATOM 4342 O ILE B 300 87.055 24.775 14.496 1.00 16.39 O ANISOU 4342 O ILE B 300 2964 2246 1017 -439 -156 119 O ATOM 4343 CB ILE B 300 88.619 24.874 17.262 1.00 16.34 C ANISOU 4343 CB ILE B 300 2160 2193 1854 -222 222 74 C ATOM 4344 CG1 ILE B 300 89.534 25.450 16.168 1.00 18.98 C ANISOU 4344 CG1 ILE B 300 2358 2896 1957 -331 438 3 C ATOM 4345 CG2 ILE B 300 88.944 23.404 17.491 1.00 14.98 C ANISOU 4345 CG2 ILE B 300 1955 2437 1299 373 305 -97 C ATOM 4346 CD1 ILE B 300 90.985 25.105 16.446 1.00 23.02 C ANISOU 4346 CD1 ILE B 300 2554 3322 2871 -205 236 115 C ATOM 4347 N SER B 301 86.285 23.106 15.765 1.00 13.01 N ANISOU 4347 N SER B 301 2513 1698 732 -259 -138 -195 N ATOM 4348 CA SER B 301 85.900 22.228 14.672 1.00 13.38 C ANISOU 4348 CA SER B 301 2418 1731 935 -177 35 -379 C ATOM 4349 C SER B 301 84.426 22.442 14.344 1.00 15.57 C ANISOU 4349 C SER B 301 2481 2187 1249 -218 -131 -282 C ATOM 4350 O SER B 301 83.532 22.025 15.080 1.00 15.83 O ANISOU 4350 O SER B 301 1971 2928 1117 -125 -359 -268 O ATOM 4351 CB SER B 301 86.159 20.767 15.021 1.00 15.26 C ANISOU 4351 CB SER B 301 2628 1828 1343 -81 -76 -214 C ATOM 4352 OG SER B 301 85.733 19.959 13.928 1.00 17.60 O ANISOU 4352 OG SER B 301 2808 2444 1434 -112 177 -572 O ATOM 4353 N ALA B 302 84.173 23.019 13.166 1.00 19.32 N ANISOU 4353 N ALA B 302 3166 2380 1794 27 -310 117 N ATOM 4354 CA ALA B 302 82.819 23.316 12.741 1.00 20.25 C ANISOU 4354 CA ALA B 302 3062 2496 2135 -50 -260 -28 C ATOM 4355 C ALA B 302 81.928 22.098 12.587 1.00 18.49 C ANISOU 4355 C ALA B 302 2649 2467 1911 139 -281 -332 C ATOM 4356 O ALA B 302 80.704 22.197 12.677 1.00 24.28 O ANISOU 4356 O ALA B 302 2685 3358 3181 -15 -319 -663 O ATOM 4357 CB ALA B 302 82.902 24.125 11.441 1.00 23.06 C ANISOU 4357 CB ALA B 302 3712 2428 2621 66 -160 329 C ATOM 4358 N GLY B 303 82.454 20.904 12.415 1.00 16.33 N ANISOU 4358 N GLY B 303 2790 2235 1179 -51 -325 -107 N ATOM 4359 CA GLY B 303 81.711 19.685 12.267 1.00 14.26 C ANISOU 4359 CA GLY B 303 1874 2494 1050 -4 -318 -314 C ATOM 4360 C GLY B 303 81.225 19.054 13.549 1.00 13.91 C ANISOU 4360 C GLY B 303 2000 2057 1226 -164 -474 -195 C ATOM 4361 O GLY B 303 80.505 18.072 13.532 1.00 16.46 O ANISOU 4361 O GLY B 303 2768 1470 2014 2 -773 -790 O ATOM 4362 N LEU B 304 81.681 19.551 14.709 1.00 14.62 N ANISOU 4362 N LEU B 304 2155 2478 923 -124 -297 -332 N ATOM 4363 CA LEU B 304 81.237 19.063 16.029 1.00 14.30 C ANISOU 4363 CA LEU B 304 1887 1968 1576 -190 -390 405 C ATOM 4364 C LEU B 304 80.193 20.026 16.598 1.00 18.47 C ANISOU 4364 C LEU B 304 2306 3078 1635 -45 79 -183 C ATOM 4365 O LEU B 304 79.972 20.172 17.813 1.00 21.65 O ANISOU 4365 O LEU B 304 2241 4125 1859 -38 19 -740 O ATOM 4366 CB LEU B 304 82.410 18.840 16.982 1.00 14.97 C ANISOU 4366 CB LEU B 304 1718 2125 1846 64 -369 -55 C ATOM 4367 CG LEU B 304 83.452 17.807 16.570 1.00 13.34 C ANISOU 4367 CG LEU B 304 1340 2253 1475 -149 -449 -470 C ATOM 4368 CD1 LEU B 304 84.599 17.703 17.608 1.00 13.03 C ANISOU 4368 CD1 LEU B 304 880 2814 1258 -309 -105 -435 C ATOM 4369 CD2 LEU B 304 82.878 16.409 16.367 1.00 13.63 C ANISOU 4369 CD2 LEU B 304 1194 2200 1785 -74 -188 -485 C ATOM 4370 N ASP B 305 79.342 20.580 15.727 1.00 21.00 N ANISOU 4370 N ASP B 305 2962 2523 2493 308 188 488 N ATOM 4371 CA ASP B 305 78.299 21.550 15.985 1.00 22.14 C ANISOU 4371 CA ASP B 305 2850 2605 2956 168 108 172 C ATOM 4372 C ASP B 305 76.903 21.080 16.315 1.00 21.00 C ANISOU 4372 C ASP B 305 2960 2468 2550 86 257 -18 C ATOM 4373 O ASP B 305 76.041 21.915 16.646 1.00 25.85 O ANISOU 4373 O ASP B 305 2826 2972 4025 200 -5 -489 O ATOM 4374 CB ASP B 305 78.190 22.487 14.747 1.00 25.35 C ANISOU 4374 CB ASP B 305 3606 3271 2755 0 166 283 C ATOM 4375 CG ASP B 305 77.941 21.808 13.419 1.00 27.66 C ANISOU 4375 CG ASP B 305 3961 3511 3039 48 87 30 C ATOM 4376 OD1 ASP B 305 78.098 20.578 13.300 1.00 26.99 O ANISOU 4376 OD1 ASP B 305 3975 3500 2781 156 116 156 O ATOM 4377 OD2 ASP B 305 77.568 22.496 12.431 1.00 25.67 O ANISOU 4377 OD2 ASP B 305 3836 3598 2318 -55 551 -130 O ATOM 4378 N PHE B 306 76.598 19.788 16.250 1.00 19.34 N ANISOU 4378 N PHE B 306 2286 2671 2390 -213 -133 -200 N ATOM 4379 CA PHE B 306 75.231 19.349 16.630 1.00 19.07 C ANISOU 4379 CA PHE B 306 2275 2239 2733 -92 -34 -27 C ATOM 4380 C PHE B 306 75.028 19.638 18.094 1.00 21.45 C ANISOU 4380 C PHE B 306 2628 2705 2818 161 20 -109 C ATOM 4381 O PHE B 306 75.761 19.179 18.990 1.00 23.40 O ANISOU 4381 O PHE B 306 2017 3301 3574 -97 252 902 O ATOM 4382 CB PHE B 306 75.070 17.913 16.139 1.00 17.90 C ANISOU 4382 CB PHE B 306 2237 2353 2212 -3 106 -125 C ATOM 4383 CG PHE B 306 73.675 17.378 16.286 1.00 17.67 C ANISOU 4383 CG PHE B 306 2182 2484 2046 -14 -30 119 C ATOM 4384 CD1 PHE B 306 72.647 17.746 15.431 1.00 18.99 C ANISOU 4384 CD1 PHE B 306 2331 2953 1929 75 -21 220 C ATOM 4385 CD2 PHE B 306 73.394 16.494 17.310 1.00 18.41 C ANISOU 4385 CD2 PHE B 306 2428 2701 1867 30 162 109 C ATOM 4386 CE1 PHE B 306 71.375 17.233 15.591 1.00 20.25 C ANISOU 4386 CE1 PHE B 306 2565 2879 2249 -125 121 195 C ATOM 4387 CE2 PHE B 306 72.127 15.976 17.490 1.00 18.17 C ANISOU 4387 CE2 PHE B 306 2169 2698 2036 248 48 -73 C ATOM 4388 CZ PHE B 306 71.115 16.346 16.628 1.00 20.13 C ANISOU 4388 CZ PHE B 306 2448 3074 2127 110 -64 322 C ATOM 4389 N PRO B 307 73.986 20.403 18.457 1.00 20.17 N ANISOU 4389 N PRO B 307 2857 2670 2135 250 44 -37 N ATOM 4390 CA PRO B 307 73.803 20.876 19.832 1.00 18.31 C ANISOU 4390 CA PRO B 307 3053 1785 2118 181 -88 -74 C ATOM 4391 C PRO B 307 73.178 19.926 20.845 1.00 18.52 C ANISOU 4391 C PRO B 307 2172 2066 2798 126 177 35 C ATOM 4392 O PRO B 307 72.731 20.195 21.970 1.00 18.30 O ANISOU 4392 O PRO B 307 3129 1083 2741 -77 258 138 O ATOM 4393 CB PRO B 307 72.981 22.150 19.618 1.00 19.22 C ANISOU 4393 CB PRO B 307 2671 2142 2490 176 -576 196 C ATOM 4394 CG PRO B 307 72.156 21.877 18.407 1.00 19.94 C ANISOU 4394 CG PRO B 307 2643 2655 2278 257 -270 -132 C ATOM 4395 CD PRO B 307 73.065 21.074 17.514 1.00 20.43 C ANISOU 4395 CD PRO B 307 3049 2495 2219 282 -92 -83 C ATOM 4396 N SER B 308 73.133 18.666 20.490 1.00 15.03 N ANISOU 4396 N SER B 308 1458 1721 2531 148 254 644 N ATOM 4397 CA SER B 308 72.627 17.547 21.266 1.00 12.30 C ANISOU 4397 CA SER B 308 1419 1585 1668 52 -45 328 C ATOM 4398 C SER B 308 73.538 16.376 20.928 1.00 9.50 C ANISOU 4398 C SER B 308 1245 1573 792 -153 -19 176 C ATOM 4399 O SER B 308 74.677 16.584 20.497 1.00 11.30 O ANISOU 4399 O SER B 308 1066 2399 829 -16 -161 205 O ATOM 4400 CB SER B 308 71.163 17.274 20.928 1.00 11.59 C ANISOU 4400 CB SER B 308 1214 1678 1512 56 445 -3 C ATOM 4401 OG SER B 308 70.612 16.251 21.746 1.00 11.92 O ANISOU 4401 OG SER B 308 1025 1788 1718 -165 114 134 O ATOM 4402 N VAL B 309 73.045 15.167 21.087 1.00 9.71 N ANISOU 4402 N VAL B 309 1616 1288 785 -64 -195 -112 N ATOM 4403 CA VAL B 309 73.846 13.962 20.864 1.00 9.45 C ANISOU 4403 CA VAL B 309 1194 1525 871 -32 -229 -162 C ATOM 4404 C VAL B 309 72.896 12.791 20.648 1.00 8.75 C ANISOU 4404 C VAL B 309 1339 1365 620 -115 102 73 C ATOM 4405 O VAL B 309 71.775 12.793 21.164 1.00 9.36 O ANISOU 4405 O VAL B 309 1159 1632 766 133 -15 -47 O ATOM 4406 CB VAL B 309 74.783 13.712 22.063 1.00 10.00 C ANISOU 4406 CB VAL B 309 1246 2009 546 345 -33 -308 C ATOM 4407 CG1 VAL B 309 73.974 13.358 23.316 1.00 11.93 C ANISOU 4407 CG1 VAL B 309 1298 2453 780 186 47 -129 C ATOM 4408 CG2 VAL B 309 75.837 12.652 21.749 1.00 10.75 C ANISOU 4408 CG2 VAL B 309 1200 2014 872 382 -146 -279 C ATOM 4409 N GLY B 310 73.355 11.811 19.868 1.00 9.06 N ANISOU 4409 N GLY B 310 1640 1268 535 -171 -261 -96 N ATOM 4410 CA GLY B 310 72.484 10.652 19.584 1.00 9.98 C ANISOU 4410 CA GLY B 310 1716 1440 636 -461 107 106 C ATOM 4411 C GLY B 310 72.030 9.978 20.870 1.00 7.52 C ANISOU 4411 C GLY B 310 1046 1372 440 -194 -179 138 C ATOM 4412 O GLY B 310 72.801 9.852 21.835 1.00 8.18 O ANISOU 4412 O GLY B 310 1086 1606 416 -17 -320 -239 O ATOM 4413 N PRO B 311 70.815 9.459 20.895 1.00 7.75 N ANISOU 4413 N PRO B 311 854 1595 495 -33 -180 62 N ATOM 4414 CA PRO B 311 70.260 8.868 22.116 1.00 8.08 C ANISOU 4414 CA PRO B 311 1104 1445 522 100 142 -163 C ATOM 4415 C PRO B 311 70.971 7.629 22.574 1.00 7.45 C ANISOU 4415 C PRO B 311 882 1594 356 72 -73 -106 C ATOM 4416 O PRO B 311 70.986 7.308 23.759 1.00 9.09 O ANISOU 4416 O PRO B 311 1351 1774 328 -173 102 -35 O ATOM 4417 CB PRO B 311 68.792 8.630 21.747 1.00 8.36 C ANISOU 4417 CB PRO B 311 1338 1533 305 -198 -176 -154 C ATOM 4418 CG PRO B 311 68.796 8.476 20.249 1.00 8.35 C ANISOU 4418 CG PRO B 311 1272 1599 304 67 -64 -231 C ATOM 4419 CD PRO B 311 69.812 9.512 19.796 1.00 9.50 C ANISOU 4419 CD PRO B 311 1213 1933 462 -257 -342 -293 C ATOM 4420 N GLN B 312 71.507 6.832 21.630 1.00 7.62 N ANISOU 4420 N GLN B 312 1112 1353 432 76 -206 -193 N ATOM 4421 CA GLN B 312 72.186 5.598 22.006 1.00 7.80 C ANISOU 4421 CA GLN B 312 1491 913 561 -176 -151 -333 C ATOM 4422 C GLN B 312 73.424 5.938 22.824 1.00 7.92 C ANISOU 4422 C GLN B 312 1349 1315 344 -263 -53 -5 C ATOM 4423 O GLN B 312 73.786 5.174 23.733 1.00 8.80 O ANISOU 4423 O GLN B 312 1651 1324 366 -159 -372 -99 O ATOM 4424 CB GLN B 312 72.483 4.717 20.783 1.00 8.44 C ANISOU 4424 CB GLN B 312 1516 953 740 211 17 -338 C ATOM 4425 CG GLN B 312 73.019 3.355 21.233 1.00 9.14 C ANISOU 4425 CG GLN B 312 1351 962 1159 171 -86 -307 C ATOM 4426 CD GLN B 312 73.084 2.348 20.105 1.00 9.10 C ANISOU 4426 CD GLN B 312 1448 1370 640 -236 313 -135 C ATOM 4427 OE1 GLN B 312 72.966 2.703 18.928 1.00 8.95 O ANISOU 4427 OE1 GLN B 312 1160 1639 603 -119 -109 -164 O ATOM 4428 NE2 GLN B 312 73.266 1.085 20.471 1.00 10.56 N ANISOU 4428 NE2 GLN B 312 1635 1566 813 29 75 114 N ATOM 4429 N HIS B 313 74.098 7.038 22.496 1.00 7.48 N ANISOU 4429 N HIS B 313 1090 1460 293 -275 68 -55 N ATOM 4430 CA HIS B 313 75.265 7.420 23.324 1.00 7.60 C ANISOU 4430 CA HIS B 313 1130 1226 533 -259 -27 -102 C ATOM 4431 C HIS B 313 74.823 7.806 24.736 1.00 7.90 C ANISOU 4431 C HIS B 313 1230 1362 410 93 -196 105 C ATOM 4432 O HIS B 313 75.474 7.422 25.727 1.00 8.79 O ANISOU 4432 O HIS B 313 1536 1420 381 128 -401 53 O ATOM 4433 CB HIS B 313 76.000 8.592 22.683 1.00 7.51 C ANISOU 4433 CB HIS B 313 1381 931 543 -169 72 -258 C ATOM 4434 CG HIS B 313 76.715 8.178 21.429 1.00 7.63 C ANISOU 4434 CG HIS B 313 1222 1251 428 90 -59 -147 C ATOM 4435 ND1 HIS B 313 77.796 7.340 21.464 1.00 8.68 N ANISOU 4435 ND1 HIS B 313 1669 1079 548 318 89 -226 N ATOM 4436 CD2 HIS B 313 76.442 8.442 20.124 1.00 7.95 C ANISOU 4436 CD2 HIS B 313 1052 1533 435 93 189 174 C ATOM 4437 CE1 HIS B 313 78.217 7.120 20.222 1.00 7.55 C ANISOU 4437 CE1 HIS B 313 868 1580 420 263 -152 -252 C ATOM 4438 NE2 HIS B 313 77.389 7.776 19.381 1.00 8.04 N ANISOU 4438 NE2 HIS B 313 883 1758 413 235 -63 29 N ATOM 4439 N ALA B 314 73.749 8.572 24.854 1.00 7.73 N ANISOU 4439 N ALA B 314 1227 1261 450 26 103 -114 N ATOM 4440 CA ALA B 314 73.281 8.972 26.193 1.00 7.07 C ANISOU 4440 CA ALA B 314 1208 1044 435 234 84 34 C ATOM 4441 C ALA B 314 72.979 7.706 26.967 1.00 7.57 C ANISOU 4441 C ALA B 314 1295 1052 528 25 -297 111 C ATOM 4442 O ALA B 314 73.234 7.587 28.184 1.00 8.25 O ANISOU 4442 O ALA B 314 1114 1667 355 53 -256 192 O ATOM 4443 CB ALA B 314 72.088 9.898 26.060 1.00 8.68 C ANISOU 4443 CB ALA B 314 1401 1219 678 428 256 -186 C ATOM 4444 N TYR B 315 72.390 6.701 26.323 1.00 8.12 N ANISOU 4444 N TYR B 315 1452 1227 406 -68 -10 -149 N ATOM 4445 CA TYR B 315 72.048 5.444 26.974 1.00 7.94 C ANISOU 4445 CA TYR B 315 845 1506 664 -236 -295 18 C ATOM 4446 C TYR B 315 73.282 4.657 27.375 1.00 7.58 C ANISOU 4446 C TYR B 315 1068 1483 329 -40 -199 199 C ATOM 4447 O TYR B 315 73.410 4.179 28.513 1.00 9.58 O ANISOU 4447 O TYR B 315 1541 1792 306 -337 -263 140 O ATOM 4448 CB TYR B 315 71.162 4.617 26.034 1.00 8.39 C ANISOU 4448 CB TYR B 315 1071 1592 526 -510 -185 25 C ATOM 4449 CG TYR B 315 70.890 3.241 26.591 1.00 8.84 C ANISOU 4449 CG TYR B 315 1151 1408 800 -51 -206 62 C ATOM 4450 CD1 TYR B 315 70.153 3.098 27.763 1.00 10.28 C ANISOU 4450 CD1 TYR B 315 1345 1735 824 -316 -165 204 C ATOM 4451 CD2 TYR B 315 71.393 2.103 25.972 1.00 10.07 C ANISOU 4451 CD2 TYR B 315 1850 1200 778 -97 -334 26 C ATOM 4452 CE1 TYR B 315 69.917 1.833 28.287 1.00 10.68 C ANISOU 4452 CE1 TYR B 315 1189 1652 1217 -211 -372 259 C ATOM 4453 CE2 TYR B 315 71.166 0.836 26.491 1.00 12.93 C ANISOU 4453 CE2 TYR B 315 2284 1418 1210 -257 -417 269 C ATOM 4454 CZ TYR B 315 70.423 0.720 27.656 1.00 12.08 C ANISOU 4454 CZ TYR B 315 1766 1413 1409 -426 -427 99 C ATOM 4455 OH TYR B 315 70.235 -0.544 28.145 1.00 16.07 O ANISOU 4455 OH TYR B 315 2664 1640 1802 -618 -377 362 O ATOM 4456 N LEU B 316 74.211 4.481 26.438 1.00 7.81 N ANISOU 4456 N LEU B 316 932 1480 556 -23 -177 -76 N ATOM 4457 CA LEU B 316 75.428 3.722 26.736 1.00 7.85 C ANISOU 4457 CA LEU B 316 799 1643 542 2 104 -54 C ATOM 4458 C LEU B 316 76.191 4.360 27.896 1.00 8.63 C ANISOU 4458 C LEU B 316 1414 1379 485 0 -157 150 C ATOM 4459 O LEU B 316 76.784 3.631 28.708 1.00 8.56 O ANISOU 4459 O LEU B 316 1242 1652 359 -121 -306 185 O ATOM 4460 CB LEU B 316 76.337 3.646 25.493 1.00 7.63 C ANISOU 4460 CB LEU B 316 725 1725 450 292 10 -80 C ATOM 4461 CG LEU B 316 75.819 2.727 24.374 1.00 9.69 C ANISOU 4461 CG LEU B 316 1677 1486 518 190 -158 -5 C ATOM 4462 CD1 LEU B 316 76.700 2.911 23.154 1.00 12.02 C ANISOU 4462 CD1 LEU B 316 2107 1929 530 119 38 2 C ATOM 4463 CD2 LEU B 316 75.773 1.282 24.784 1.00 10.38 C ANISOU 4463 CD2 LEU B 316 2209 1351 384 -123 -176 -350 C ATOM 4464 N ASN B 317 76.144 5.680 27.968 1.00 8.88 N ANISOU 4464 N ASN B 317 1572 1369 435 -229 -448 -67 N ATOM 4465 CA ASN B 317 76.756 6.365 29.116 1.00 7.89 C ANISOU 4465 CA ASN B 317 1450 1214 334 -443 -67 -77 C ATOM 4466 C ASN B 317 76.028 6.045 30.423 1.00 8.31 C ANISOU 4466 C ASN B 317 986 1583 590 -132 -95 537 C ATOM 4467 O ASN B 317 76.657 5.737 31.437 1.00 9.37 O ANISOU 4467 O ASN B 317 1248 1960 353 96 -184 257 O ATOM 4468 CB ASN B 317 76.702 7.882 28.914 1.00 8.70 C ANISOU 4468 CB ASN B 317 1702 1246 357 -341 -119 -127 C ATOM 4469 CG ASN B 317 77.374 8.587 30.101 1.00 8.23 C ANISOU 4469 CG ASN B 317 1110 1567 451 -83 -27 -338 C ATOM 4470 OD1 ASN B 317 78.529 8.317 30.358 1.00 9.51 O ANISOU 4470 OD1 ASN B 317 1156 1871 587 -274 -329 -25 O ATOM 4471 ND2 ASN B 317 76.582 9.441 30.694 1.00 12.22 N ANISOU 4471 ND2 ASN B 317 1124 2254 1265 148 -66 -842 N ATOM 4472 N SER B 318 74.709 6.133 30.403 1.00 9.22 N ANISOU 4472 N SER B 318 981 1964 557 -160 -104 185 N ATOM 4473 CA SER B 318 73.916 5.948 31.598 1.00 9.10 C ANISOU 4473 CA SER B 318 1102 1608 749 171 143 223 C ATOM 4474 C SER B 318 74.169 4.602 32.260 1.00 9.01 C ANISOU 4474 C SER B 318 1341 1625 458 231 -11 113 C ATOM 4475 O SER B 318 74.162 4.549 33.494 1.00 9.97 O ANISOU 4475 O SER B 318 1838 1689 260 -127 -126 42 O ATOM 4476 CB SER B 318 72.440 6.158 31.241 1.00 10.14 C ANISOU 4476 CB SER B 318 1178 1959 717 126 -28 -117 C ATOM 4477 OG SER B 318 71.906 5.071 30.524 1.00 13.92 O ANISOU 4477 OG SER B 318 1909 2591 790 -241 -318 -323 O ATOM 4478 N ILE B 319 74.359 3.544 31.482 1.00 8.84 N ANISOU 4478 N ILE B 319 1466 1459 435 110 -11 129 N ATOM 4479 CA ILE B 319 74.577 2.201 32.008 1.00 8.20 C ANISOU 4479 CA ILE B 319 1334 1211 569 -188 141 -71 C ATOM 4480 C ILE B 319 76.054 1.914 32.254 1.00 8.83 C ANISOU 4480 C ILE B 319 1485 1435 436 -16 -88 -15 C ATOM 4481 O ILE B 319 76.384 0.834 32.748 1.00 10.66 O ANISOU 4481 O ILE B 319 1871 1616 562 48 -406 90 O ATOM 4482 CB ILE B 319 73.941 1.108 31.136 1.00 9.51 C ANISOU 4482 CB ILE B 319 1424 1681 509 -129 180 -396 C ATOM 4483 CG1 ILE B 319 74.638 1.015 29.783 1.00 10.66 C ANISOU 4483 CG1 ILE B 319 1613 1785 653 217 359 -561 C ATOM 4484 CG2 ILE B 319 72.464 1.438 30.952 1.00 10.91 C ANISOU 4484 CG2 ILE B 319 1351 1772 1023 -259 92 -529 C ATOM 4485 CD1 ILE B 319 74.113 -0.080 28.866 1.00 12.43 C ANISOU 4485 CD1 ILE B 319 2108 1723 894 -74 8 -304 C ATOM 4486 N GLY B 320 76.924 2.867 31.939 1.00 9.18 N ANISOU 4486 N GLY B 320 1150 1929 411 -203 -243 -74 N ATOM 4487 CA GLY B 320 78.344 2.668 32.158 1.00 9.74 C ANISOU 4487 CA GLY B 320 1259 2061 379 84 -197 110 C ATOM 4488 C GLY B 320 79.060 1.837 31.113 1.00 8.91 C ANISOU 4488 C GLY B 320 1338 1578 470 -98 -217 63 C ATOM 4489 O GLY B 320 80.220 1.460 31.306 1.00 11.91 O ANISOU 4489 O GLY B 320 1488 2453 586 169 -361 41 O ATOM 4490 N ARG B 321 78.387 1.538 29.991 1.00 8.88 N ANISOU 4490 N ARG B 321 1266 1736 373 60 -140 -171 N ATOM 4491 CA ARG B 321 79.069 0.751 28.954 1.00 9.06 C ANISOU 4491 CA ARG B 321 1245 1632 568 -43 -78 -167 C ATOM 4492 C ARG B 321 80.054 1.607 28.172 1.00 8.57 C ANISOU 4492 C ARG B 321 1126 1398 731 -25 -202 -163 C ATOM 4493 O ARG B 321 81.116 1.080 27.810 1.00 11.17 O ANISOU 4493 O ARG B 321 1556 1231 1460 271 278 239 O ATOM 4494 CB ARG B 321 78.026 0.134 28.016 1.00 9.61 C ANISOU 4494 CB ARG B 321 1352 1641 659 -4 -224 -256 C ATOM 4495 CG ARG B 321 78.689 -0.579 26.827 1.00 9.12 C ANISOU 4495 CG ARG B 321 1224 1378 863 107 136 24 C ATOM 4496 CD ARG B 321 79.490 -1.790 27.275 1.00 9.18 C ANISOU 4496 CD ARG B 321 1258 1372 859 106 432 134 C ATOM 4497 NE ARG B 321 80.281 -2.406 26.216 1.00 9.36 N ANISOU 4497 NE ARG B 321 1342 1425 790 261 52 -161 N ATOM 4498 CZ ARG B 321 81.574 -2.185 26.033 1.00 8.65 C ANISOU 4498 CZ ARG B 321 1352 1410 526 160 -86 158 C ATOM 4499 NH1 ARG B 321 82.245 -1.349 26.810 1.00 9.54 N ANISOU 4499 NH1 ARG B 321 1814 1438 372 -149 -143 372 N ATOM 4500 NH2 ARG B 321 82.213 -2.795 25.037 1.00 10.67 N ANISOU 4500 NH2 ARG B 321 1297 2035 720 432 67 151 N ATOM 4501 N ALA B 322 79.726 2.867 27.933 1.00 9.01 N ANISOU 4501 N ALA B 322 1498 1418 506 -135 -238 -15 N ATOM 4502 CA ALA B 322 80.642 3.771 27.235 1.00 9.06 C ANISOU 4502 CA ALA B 322 1904 1077 460 -51 -294 254 C ATOM 4503 C ALA B 322 80.977 4.912 28.192 1.00 8.32 C ANISOU 4503 C ALA B 322 1446 1216 499 -195 -29 192 C ATOM 4504 O ALA B 322 80.133 5.291 29.018 1.00 9.09 O ANISOU 4504 O ALA B 322 1361 1616 478 -486 66 150 O ATOM 4505 CB ALA B 322 80.063 4.271 25.917 1.00 9.73 C ANISOU 4505 CB ALA B 322 1683 1538 478 -23 -440 84 C ATOM 4506 N ASP B 323 82.156 5.499 28.038 1.00 9.15 N ANISOU 4506 N ASP B 323 1496 1431 549 -293 -140 35 N ATOM 4507 CA ASP B 323 82.574 6.636 28.824 1.00 7.82 C ANISOU 4507 CA ASP B 323 1185 1163 622 117 -82 11 C ATOM 4508 C ASP B 323 82.728 7.817 27.872 1.00 8.54 C ANISOU 4508 C ASP B 323 1489 1135 621 -66 209 -64 C ATOM 4509 O ASP B 323 83.271 7.611 26.787 1.00 9.02 O ANISOU 4509 O ASP B 323 1665 1260 504 154 155 -168 O ATOM 4510 CB ASP B 323 83.913 6.340 29.498 1.00 9.00 C ANISOU 4510 CB ASP B 323 1146 1598 674 90 -139 199 C ATOM 4511 CG ASP B 323 83.741 5.157 30.444 1.00 11.77 C ANISOU 4511 CG ASP B 323 1307 2017 1149 322 27 648 C ATOM 4512 OD1 ASP B 323 82.892 5.249 31.358 1.00 12.22 O ANISOU 4512 OD1 ASP B 323 1841 2125 677 493 -32 349 O ATOM 4513 OD2 ASP B 323 84.443 4.142 30.257 1.00 15.21 O ANISOU 4513 OD2 ASP B 323 1856 2434 1489 493 761 284 O ATOM 4514 N TYR B 324 82.366 8.999 28.298 1.00 8.07 N ANISOU 4514 N TYR B 324 1571 1182 312 17 94 -121 N ATOM 4515 CA TYR B 324 82.423 10.209 27.493 1.00 8.44 C ANISOU 4515 CA TYR B 324 1363 1100 745 71 -126 12 C ATOM 4516 C TYR B 324 83.272 11.242 28.212 1.00 7.72 C ANISOU 4516 C TYR B 324 1031 1621 281 5 118 -81 C ATOM 4517 O TYR B 324 83.127 11.430 29.445 1.00 10.62 O ANISOU 4517 O TYR B 324 1725 2052 257 -1 -78 -85 O ATOM 4518 CB TYR B 324 81.017 10.754 27.119 1.00 8.76 C ANISOU 4518 CB TYR B 324 1157 1171 1002 -164 -378 -180 C ATOM 4519 CG TYR B 324 80.307 9.719 26.251 1.00 7.82 C ANISOU 4519 CG TYR B 324 1260 1273 440 -124 -136 -258 C ATOM 4520 CD1 TYR B 324 79.646 8.661 26.846 1.00 7.20 C ANISOU 4520 CD1 TYR B 324 802 1280 656 29 -141 -162 C ATOM 4521 CD2 TYR B 324 80.354 9.747 24.862 1.00 8.50 C ANISOU 4521 CD2 TYR B 324 1428 1375 425 -11 -308 -197 C ATOM 4522 CE1 TYR B 324 79.039 7.657 26.113 1.00 8.22 C ANISOU 4522 CE1 TYR B 324 1634 1227 260 -219 -107 0 C ATOM 4523 CE2 TYR B 324 79.739 8.757 24.113 1.00 7.80 C ANISOU 4523 CE2 TYR B 324 1237 1202 526 -81 -520 97 C ATOM 4524 CZ TYR B 324 79.096 7.712 24.733 1.00 8.22 C ANISOU 4524 CZ TYR B 324 1230 1541 351 -264 -299 -33 C ATOM 4525 OH TYR B 324 78.517 6.699 23.999 1.00 8.70 O ANISOU 4525 OH TYR B 324 1501 1349 455 -464 -141 14 O ATOM 4526 N VAL B 325 84.153 11.849 27.463 1.00 7.81 N ANISOU 4526 N VAL B 325 1260 1153 555 -361 -159 14 N ATOM 4527 CA VAL B 325 85.101 12.842 27.906 1.00 8.53 C ANISOU 4527 CA VAL B 325 1214 1354 674 -502 -54 20 C ATOM 4528 C VAL B 325 85.067 14.027 26.946 1.00 8.69 C ANISOU 4528 C VAL B 325 1560 1373 369 -190 -186 -104 C ATOM 4529 O VAL B 325 84.356 13.969 25.942 1.00 9.11 O ANISOU 4529 O VAL B 325 1358 1770 334 -105 -148 70 O ATOM 4530 CB VAL B 325 86.536 12.284 27.958 1.00 9.21 C ANISOU 4530 CB VAL B 325 1467 1781 251 -82 -55 1 C ATOM 4531 CG1 VAL B 325 86.581 11.112 28.949 1.00 10.78 C ANISOU 4531 CG1 VAL B 325 1552 1648 897 6 -205 154 C ATOM 4532 CG2 VAL B 325 87.002 11.799 26.583 1.00 9.80 C ANISOU 4532 CG2 VAL B 325 1404 1854 465 -165 226 -46 C ATOM 4533 N SER B 326 85.802 15.078 27.263 1.00 8.90 N ANISOU 4533 N SER B 326 1457 1569 354 -364 -38 -39 N ATOM 4534 CA SER B 326 85.884 16.205 26.348 1.00 9.19 C ANISOU 4534 CA SER B 326 1456 1204 832 -179 -16 -51 C ATOM 4535 C SER B 326 87.342 16.596 26.143 1.00 9.56 C ANISOU 4535 C SER B 326 1363 1444 823 -145 -219 20 C ATOM 4536 O SER B 326 88.218 16.257 26.940 1.00 9.59 O ANISOU 4536 O SER B 326 1370 1626 648 -131 -281 -341 O ATOM 4537 CB SER B 326 85.046 17.397 26.785 1.00 10.37 C ANISOU 4537 CB SER B 326 1505 1487 947 115 -322 -189 C ATOM 4538 OG SER B 326 85.527 17.915 28.018 1.00 13.43 O ANISOU 4538 OG SER B 326 2254 1854 994 87 -222 -638 O ATOM 4539 N ILE B 327 87.597 17.267 25.032 1.00 9.08 N ANISOU 4539 N ILE B 327 1222 1573 656 3 -83 -139 N ATOM 4540 CA ILE B 327 88.912 17.726 24.612 1.00 8.24 C ANISOU 4540 CA ILE B 327 1273 1171 688 27 -135 -281 C ATOM 4541 C ILE B 327 88.762 19.148 24.118 1.00 8.47 C ANISOU 4541 C ILE B 327 1443 1197 577 -185 -158 -195 C ATOM 4542 O ILE B 327 87.788 19.472 23.406 1.00 10.14 O ANISOU 4542 O ILE B 327 1672 1773 406 15 -184 -15 O ATOM 4543 CB ILE B 327 89.421 16.818 23.480 1.00 8.85 C ANISOU 4543 CB ILE B 327 1705 1076 583 77 76 -137 C ATOM 4544 CG1 ILE B 327 89.963 15.503 24.035 1.00 8.61 C ANISOU 4544 CG1 ILE B 327 1213 1370 689 200 -372 -169 C ATOM 4545 CG2 ILE B 327 90.413 17.512 22.565 1.00 9.10 C ANISOU 4545 CG2 ILE B 327 1832 1313 311 -213 -52 -243 C ATOM 4546 CD1 ILE B 327 91.234 15.594 24.860 1.00 8.85 C ANISOU 4546 CD1 ILE B 327 1113 1756 493 -309 -170 -430 C ATOM 4547 N THR B 328 89.616 20.053 24.578 1.00 9.28 N ANISOU 4547 N THR B 328 1958 928 640 -434 -31 -99 N ATOM 4548 CA THR B 328 89.492 21.457 24.212 1.00 9.48 C ANISOU 4548 CA THR B 328 1775 1106 720 -38 -94 15 C ATOM 4549 C THR B 328 90.049 21.757 22.817 1.00 9.26 C ANISOU 4549 C THR B 328 1718 1016 785 -103 -83 57 C ATOM 4550 O THR B 328 90.731 20.938 22.206 1.00 10.88 O ANISOU 4550 O THR B 328 1712 1604 818 94 -348 -335 O ATOM 4551 CB THR B 328 90.291 22.335 25.192 1.00 10.51 C ANISOU 4551 CB THR B 328 1673 1647 671 -311 -15 -16 C ATOM 4552 OG1 THR B 328 91.686 22.005 25.039 1.00 12.12 O ANISOU 4552 OG1 THR B 328 1631 1915 1059 -320 -257 -311 O ATOM 4553 CG2 THR B 328 89.831 22.189 26.624 1.00 11.67 C ANISOU 4553 CG2 THR B 328 2209 1705 522 -138 -211 24 C ATOM 4554 N ASP B 329 89.748 22.971 22.365 1.00 9.39 N ANISOU 4554 N ASP B 329 1578 963 1027 -23 -56 -52 N ATOM 4555 CA ASP B 329 90.270 23.414 21.083 1.00 10.04 C ANISOU 4555 CA ASP B 329 1550 1212 1052 -34 -8 -28 C ATOM 4556 C ASP B 329 91.792 23.245 21.049 1.00 9.62 C ANISOU 4556 C ASP B 329 1502 1235 919 -220 -127 -134 C ATOM 4557 O ASP B 329 92.340 22.767 20.047 1.00 11.60 O ANISOU 4557 O ASP B 329 1608 1628 1170 -197 177 -150 O ATOM 4558 CB ASP B 329 89.960 24.887 20.862 1.00 11.31 C ANISOU 4558 CB ASP B 329 1752 1139 1406 -206 -139 -14 C ATOM 4559 CG ASP B 329 88.539 25.293 20.567 1.00 12.57 C ANISOU 4559 CG ASP B 329 1773 1423 1581 -187 -207 -248 C ATOM 4560 OD1 ASP B 329 87.676 24.405 20.419 1.00 12.41 O ANISOU 4560 OD1 ASP B 329 1955 1673 1087 -492 -289 38 O ATOM 4561 OD2 ASP B 329 88.287 26.514 20.437 1.00 15.14 O ANISOU 4561 OD2 ASP B 329 2164 1562 2027 -52 -263 183 O ATOM 4562 N ASP B 330 92.460 23.705 22.132 1.00 11.38 N ANISOU 4562 N ASP B 330 1341 1767 1215 -325 -256 -294 N ATOM 4563 CA ASP B 330 93.928 23.655 22.105 1.00 11.57 C ANISOU 4563 CA ASP B 330 1407 1459 1531 -336 -417 -389 C ATOM 4564 C ASP B 330 94.443 22.225 22.088 1.00 10.06 C ANISOU 4564 C ASP B 330 1124 1525 1173 -302 -238 -240 C ATOM 4565 O ASP B 330 95.435 21.959 21.414 1.00 10.88 O ANISOU 4565 O ASP B 330 1230 1757 1149 -112 -220 -375 O ATOM 4566 CB ASP B 330 94.523 24.462 23.255 1.00 13.76 C ANISOU 4566 CB ASP B 330 1765 1913 1550 -361 -658 -440 C ATOM 4567 CG ASP B 330 94.452 25.954 23.017 1.00 15.22 C ANISOU 4567 CG ASP B 330 1840 1903 2041 -522 -504 -395 C ATOM 4568 OD1 ASP B 330 94.142 26.428 21.915 1.00 17.31 O ANISOU 4568 OD1 ASP B 330 2309 2001 2266 -598 -431 -109 O ATOM 4569 OD2 ASP B 330 94.749 26.712 23.981 1.00 20.85 O ANISOU 4569 OD2 ASP B 330 3079 2124 2717 -755 -689 -856 O ATOM 4570 N GLU B 331 93.790 21.336 22.827 1.00 9.91 N ANISOU 4570 N GLU B 331 1616 1383 767 -457 -546 -207 N ATOM 4571 CA GLU B 331 94.222 19.934 22.812 1.00 10.21 C ANISOU 4571 CA GLU B 331 1594 1511 776 -236 -185 -97 C ATOM 4572 C GLU B 331 94.037 19.359 21.401 1.00 10.05 C ANISOU 4572 C GLU B 331 1469 1388 963 -199 -274 -237 C ATOM 4573 O GLU B 331 94.870 18.578 20.940 1.00 10.58 O ANISOU 4573 O GLU B 331 1560 1506 953 -2 -485 -304 O ATOM 4574 CB GLU B 331 93.430 19.164 23.873 1.00 10.21 C ANISOU 4574 CB GLU B 331 1413 1998 470 -257 -267 -111 C ATOM 4575 CG GLU B 331 93.808 19.554 25.314 1.00 10.75 C ANISOU 4575 CG GLU B 331 1365 2116 604 -471 -366 -184 C ATOM 4576 CD GLU B 331 92.904 18.910 26.347 1.00 10.80 C ANISOU 4576 CD GLU B 331 1573 2069 461 -116 -265 9 C ATOM 4577 OE1 GLU B 331 91.692 18.797 26.086 1.00 11.11 O ANISOU 4577 OE1 GLU B 331 1625 2025 570 -508 -132 -31 O ATOM 4578 OE2 GLU B 331 93.401 18.517 27.432 1.00 19.29 O ANISOU 4578 OE2 GLU B 331 1049 5272 1010 -152 -362 754 O ATOM 4579 N ALA B 332 92.910 19.685 20.780 1.00 9.05 N ANISOU 4579 N ALA B 332 1141 1457 840 -234 -45 -325 N ATOM 4580 CA ALA B 332 92.661 19.140 19.430 1.00 9.13 C ANISOU 4580 CA ALA B 332 1240 1536 692 -370 -227 -90 C ATOM 4581 C ALA B 332 93.711 19.665 18.450 1.00 9.27 C ANISOU 4581 C ALA B 332 1340 1476 705 -256 -159 -46 C ATOM 4582 O ALA B 332 94.179 18.907 17.583 1.00 10.19 O ANISOU 4582 O ALA B 332 1568 1647 657 -514 -87 -177 O ATOM 4583 CB ALA B 332 91.267 19.522 18.942 1.00 10.47 C ANISOU 4583 CB ALA B 332 1382 1776 819 -254 -456 -399 C ATOM 4584 N LEU B 333 94.015 20.959 18.562 1.00 10.68 N ANISOU 4584 N LEU B 333 1842 1531 686 -395 -174 16 N ATOM 4585 CA LEU B 333 95.008 21.534 17.650 1.00 10.54 C ANISOU 4585 CA LEU B 333 1805 1296 905 -264 -79 13 C ATOM 4586 C LEU B 333 96.371 20.884 17.798 1.00 9.84 C ANISOU 4586 C LEU B 333 1547 1584 609 -373 -25 -173 C ATOM 4587 O LEU B 333 97.083 20.642 16.825 1.00 11.23 O ANISOU 4587 O LEU B 333 1731 1905 630 -586 135 -144 O ATOM 4588 CB LEU B 333 95.152 23.041 17.884 1.00 13.18 C ANISOU 4588 CB LEU B 333 2317 1385 1307 -413 -92 -266 C ATOM 4589 CG LEU B 333 93.993 23.880 17.358 1.00 17.38 C ANISOU 4589 CG LEU B 333 2710 2024 1871 30 -81 -106 C ATOM 4590 CD1 LEU B 333 93.990 25.245 18.040 1.00 18.51 C ANISOU 4590 CD1 LEU B 333 3218 2174 1640 21 54 -211 C ATOM 4591 CD2 LEU B 333 94.103 24.066 15.850 1.00 19.93 C ANISOU 4591 CD2 LEU B 333 3273 2456 1843 -232 -215 -52 C ATOM 4592 N GLU B 334 96.757 20.629 19.061 1.00 9.73 N ANISOU 4592 N GLU B 334 1607 1319 770 -238 -400 -291 N ATOM 4593 CA GLU B 334 98.052 19.978 19.285 1.00 10.08 C ANISOU 4593 CA GLU B 334 1367 1766 696 -379 -358 -156 C ATOM 4594 C GLU B 334 98.072 18.585 18.668 1.00 9.62 C ANISOU 4594 C GLU B 334 1270 1477 907 -79 -253 133 C ATOM 4595 O GLU B 334 99.066 18.155 18.110 1.00 11.51 O ANISOU 4595 O GLU B 334 1103 1999 1272 -269 -48 197 O ATOM 4596 CB GLU B 334 98.415 19.939 20.772 1.00 11.63 C ANISOU 4596 CB GLU B 334 1687 1919 815 -259 -563 40 C ATOM 4597 CG GLU B 334 99.762 19.330 21.065 1.00 13.59 C ANISOU 4597 CG GLU B 334 1960 2212 989 95 -448 307 C ATOM 4598 CD GLU B 334 99.798 17.845 21.307 1.00 16.51 C ANISOU 4598 CD GLU B 334 2356 2326 1592 231 -93 601 C ATOM 4599 OE1 GLU B 334 98.910 17.339 22.024 1.00 19.41 O ANISOU 4599 OE1 GLU B 334 2194 2659 2520 -93 -187 967 O ATOM 4600 OE2 GLU B 334 100.711 17.121 20.853 1.00 18.13 O ANISOU 4600 OE2 GLU B 334 3428 2697 762 637 206 514 O ATOM 4601 N ALA B 335 96.970 17.844 18.792 1.00 9.72 N ANISOU 4601 N ALA B 335 1525 1425 742 -356 -314 -234 N ATOM 4602 CA ALA B 335 96.882 16.512 18.191 1.00 8.85 C ANISOU 4602 CA ALA B 335 1425 1353 585 -375 39 -161 C ATOM 4603 C ALA B 335 96.990 16.595 16.662 1.00 9.89 C ANISOU 4603 C ALA B 335 1473 1666 617 48 9 17 C ATOM 4604 O ALA B 335 97.650 15.750 16.048 1.00 10.20 O ANISOU 4604 O ALA B 335 1200 1997 678 -181 -49 -349 O ATOM 4605 CB ALA B 335 95.602 15.806 18.596 1.00 10.32 C ANISOU 4605 CB ALA B 335 1358 1791 773 -286 87 252 C ATOM 4606 N PHE B 336 96.323 17.589 16.083 1.00 9.33 N ANISOU 4606 N PHE B 336 1380 1591 576 -57 -10 -41 N ATOM 4607 CA PHE B 336 96.396 17.803 14.640 1.00 10.18 C ANISOU 4607 CA PHE B 336 1378 1937 553 -145 -370 12 C ATOM 4608 C PHE B 336 97.849 17.998 14.205 1.00 10.08 C ANISOU 4608 C PHE B 336 1483 1276 1070 -55 -48 -126 C ATOM 4609 O PHE B 336 98.349 17.346 13.291 1.00 10.16 O ANISOU 4609 O PHE B 336 1577 1788 495 -416 -35 -131 O ATOM 4610 CB PHE B 336 95.566 19.035 14.296 1.00 9.76 C ANISOU 4610 CB PHE B 336 1448 1694 568 -154 -279 -199 C ATOM 4611 CG PHE B 336 95.551 19.458 12.855 1.00 11.40 C ANISOU 4611 CG PHE B 336 1985 1761 587 -203 98 -172 C ATOM 4612 CD1 PHE B 336 96.589 20.187 12.308 1.00 12.71 C ANISOU 4612 CD1 PHE B 336 1908 2132 790 -285 9 -44 C ATOM 4613 CD2 PHE B 336 94.473 19.123 12.039 1.00 13.14 C ANISOU 4613 CD2 PHE B 336 2105 2169 719 -102 -120 16 C ATOM 4614 CE1 PHE B 336 96.581 20.588 10.971 1.00 13.26 C ANISOU 4614 CE1 PHE B 336 2057 2108 874 -293 -6 47 C ATOM 4615 CE2 PHE B 336 94.447 19.518 10.699 1.00 13.68 C ANISOU 4615 CE2 PHE B 336 2505 1946 746 -147 87 -5 C ATOM 4616 CZ PHE B 336 95.498 20.230 10.188 1.00 12.68 C ANISOU 4616 CZ PHE B 336 2137 1962 720 53 -144 101 C ATOM 4617 N LYS B 337 98.538 18.911 14.902 1.00 10.37 N ANISOU 4617 N LYS B 337 1126 1649 1166 -375 -67 -26 N ATOM 4618 CA LYS B 337 99.943 19.173 14.548 1.00 10.90 C ANISOU 4618 CA LYS B 337 1217 1467 1457 -325 111 -220 C ATOM 4619 C LYS B 337 100.796 17.926 14.717 1.00 10.37 C ANISOU 4619 C LYS B 337 1126 1796 1017 -199 -259 -302 C ATOM 4620 O LYS B 337 101.667 17.612 13.893 1.00 12.69 O ANISOU 4620 O LYS B 337 1654 2057 1112 -211 80 -604 O ATOM 4621 CB LYS B 337 100.504 20.305 15.410 1.00 14.14 C ANISOU 4621 CB LYS B 337 1522 1789 2061 -485 -35 -495 C ATOM 4622 CG LYS B 337 99.900 21.659 15.061 1.00 19.90 C ANISOU 4622 CG LYS B 337 2596 2287 2677 -94 -3 141 C ATOM 4623 CD LYS B 337 100.384 22.700 16.059 1.00 26.31 C ANISOU 4623 CD LYS B 337 3699 3068 3229 -242 -131 -413 C ATOM 4624 CE LYS B 337 99.617 24.003 15.943 1.00 32.96 C ANISOU 4624 CE LYS B 337 4283 3849 4392 285 -29 -82 C ATOM 4625 NZ LYS B 337 100.205 25.036 16.853 1.00 37.53 N ANISOU 4625 NZ LYS B 337 4875 4482 4900 -113 -25 -342 N ATOM 4626 N THR B 338 100.586 17.209 15.815 1.00 11.23 N ANISOU 4626 N THR B 338 1587 1887 794 -217 -375 -393 N ATOM 4627 CA THR B 338 101.370 16.012 16.084 1.00 11.85 C ANISOU 4627 CA THR B 338 1848 1853 802 -107 -170 -359 C ATOM 4628 C THR B 338 101.205 14.930 15.041 1.00 10.36 C ANISOU 4628 C THR B 338 1631 1626 681 112 -364 -202 C ATOM 4629 O THR B 338 102.202 14.322 14.626 1.00 11.09 O ANISOU 4629 O THR B 338 1539 1814 860 -100 -228 -412 O ATOM 4630 CB THR B 338 100.984 15.485 17.474 1.00 12.71 C ANISOU 4630 CB THR B 338 2222 1823 784 204 -365 -97 C ATOM 4631 OG1 THR B 338 101.517 16.457 18.406 1.00 14.70 O ANISOU 4631 OG1 THR B 338 2511 2502 571 164 -493 -332 O ATOM 4632 CG2 THR B 338 101.524 14.104 17.768 1.00 13.80 C ANISOU 4632 CG2 THR B 338 2605 1724 914 105 5 197 C ATOM 4633 N LEU B 339 99.970 14.722 14.564 1.00 10.08 N ANISOU 4633 N LEU B 339 1410 1721 699 39 -54 -195 N ATOM 4634 CA LEU B 339 99.789 13.660 13.554 1.00 10.71 C ANISOU 4634 CA LEU B 339 1545 1907 618 -135 54 -269 C ATOM 4635 C LEU B 339 100.430 14.078 12.234 1.00 9.09 C ANISOU 4635 C LEU B 339 842 1777 834 115 23 -92 C ATOM 4636 O LEU B 339 101.020 13.236 11.530 1.00 10.75 O ANISOU 4636 O LEU B 339 1317 1975 792 29 -43 -461 O ATOM 4637 CB LEU B 339 98.318 13.317 13.343 1.00 9.05 C ANISOU 4637 CB LEU B 339 1524 1500 415 -43 -3 176 C ATOM 4638 CG LEU B 339 98.030 12.007 12.599 1.00 10.04 C ANISOU 4638 CG LEU B 339 1329 1611 876 -2 367 -157 C ATOM 4639 CD1 LEU B 339 98.443 10.782 13.390 1.00 11.61 C ANISOU 4639 CD1 LEU B 339 1786 1716 910 175 176 -198 C ATOM 4640 CD2 LEU B 339 96.573 11.896 12.171 1.00 10.42 C ANISOU 4640 CD2 LEU B 339 1604 1549 808 16 -173 412 C ATOM 4641 N CYS B 340 100.289 15.346 11.866 1.00 10.57 N ANISOU 4641 N CYS B 340 1567 1827 621 -425 14 80 N ATOM 4642 CA CYS B 340 100.882 15.793 10.608 1.00 10.80 C ANISOU 4642 CA CYS B 340 1675 1896 532 -196 131 -96 C ATOM 4643 C CYS B 340 102.394 15.548 10.626 1.00 10.91 C ANISOU 4643 C CYS B 340 1547 1721 877 -487 310 -437 C ATOM 4644 O CYS B 340 103.000 15.044 9.678 1.00 12.39 O ANISOU 4644 O CYS B 340 1531 2465 710 -320 433 -317 O ATOM 4645 CB CYS B 340 100.669 17.293 10.403 1.00 11.27 C ANISOU 4645 CB CYS B 340 1769 1890 624 -405 37 229 C ATOM 4646 SG CYS B 340 98.981 17.815 10.022 1.00 11.52 S ANISOU 4646 SG CYS B 340 1869 1812 694 -340 -83 207 S ATOM 4647 N ARG B 341 102.996 15.986 11.743 1.00 11.58 N ANISOU 4647 N ARG B 341 1517 2145 739 -515 46 67 N ATOM 4648 CA ARG B 341 104.440 15.946 11.828 1.00 11.66 C ANISOU 4648 CA ARG B 341 1550 2039 841 -214 -59 -286 C ATOM 4649 C ARG B 341 105.042 14.566 11.997 1.00 11.07 C ANISOU 4649 C ARG B 341 1232 2032 944 -288 -53 -191 C ATOM 4650 O ARG B 341 106.115 14.288 11.422 1.00 12.99 O ANISOU 4650 O ARG B 341 1512 2677 746 -200 150 -174 O ATOM 4651 CB ARG B 341 104.880 16.849 12.996 1.00 13.75 C ANISOU 4651 CB ARG B 341 1957 2316 954 -157 -124 -486 C ATOM 4652 CG ARG B 341 106.387 16.821 13.212 1.00 15.30 C ANISOU 4652 CG ARG B 341 1955 2520 1338 -500 -153 -543 C ATOM 4653 CD ARG B 341 107.050 17.454 11.983 1.00 18.73 C ANISOU 4653 CD ARG B 341 2546 2383 2188 -395 185 34 C ATOM 4654 NE AARG B 341 108.505 17.284 12.052 0.80 23.75 N ANISOU 4654 NE AARG B 341 2690 3154 3181 -245 129 -136 N ATOM 4655 CZ AARG B 341 109.140 16.345 11.343 0.80 26.19 C ANISOU 4655 CZ AARG B 341 3185 3373 3391 -20 161 -240 C ATOM 4656 NH1AARG B 341 108.472 15.526 10.530 0.80 23.19 N ANISOU 4656 NH1AARG B 341 2813 3039 2958 -114 394 15 N ATOM 4657 NH2AARG B 341 110.460 16.259 11.455 0.80 29.44 N ANISOU 4657 NH2AARG B 341 3320 3900 3966 -161 -53 -157 N ATOM 4658 NE BARG B 341 106.770 18.895 11.948 0.20 17.21 N ANISOU 4658 NE BARG B 341 2202 2386 1951 -247 -4 -117 N ATOM 4659 CZ BARG B 341 107.679 19.735 12.461 0.20 16.51 C ANISOU 4659 CZ BARG B 341 2175 2049 2048 -70 -67 -57 C ATOM 4660 NH1BARG B 341 108.795 19.214 12.952 0.20 16.07 N ANISOU 4660 NH1BARG B 341 2106 2116 1884 -131 -121 -53 N ATOM 4661 NH2BARG B 341 107.492 21.040 12.463 0.20 16.94 N ANISOU 4661 NH2BARG B 341 2300 2035 2103 -36 -25 -129 N ATOM 4662 N HIS B 342 104.370 13.688 12.745 1.00 10.41 N ANISOU 4662 N HIS B 342 1425 1900 630 -118 -167 -159 N ATOM 4663 CA HIS B 342 104.943 12.393 13.064 1.00 12.20 C ANISOU 4663 CA HIS B 342 1878 1779 979 -75 98 -32 C ATOM 4664 C HIS B 342 104.418 11.239 12.244 1.00 11.12 C ANISOU 4664 C HIS B 342 1468 1885 873 35 -33 -30 C ATOM 4665 O HIS B 342 105.065 10.198 12.228 1.00 13.14 O ANISOU 4665 O HIS B 342 1797 1921 1274 166 -697 134 O ATOM 4666 CB HIS B 342 104.785 12.076 14.575 1.00 13.69 C ANISOU 4666 CB HIS B 342 1920 2513 768 240 -278 -353 C ATOM 4667 CG HIS B 342 105.556 13.096 15.367 1.00 15.73 C ANISOU 4667 CG HIS B 342 1990 2858 1129 294 -587 -528 C ATOM 4668 ND1 HIS B 342 106.933 13.026 15.461 1.00 19.67 N ANISOU 4668 ND1 HIS B 342 1996 3351 2127 146 -594 -606 N ATOM 4669 CD2 HIS B 342 105.161 14.193 16.048 1.00 17.37 C ANISOU 4669 CD2 HIS B 342 2124 2796 1678 313 -368 -555 C ATOM 4670 CE1 HIS B 342 107.346 14.047 16.207 1.00 20.26 C ANISOU 4670 CE1 HIS B 342 2122 3269 2305 132 -475 -673 C ATOM 4671 NE2 HIS B 342 106.299 14.773 16.559 1.00 20.82 N ANISOU 4671 NE2 HIS B 342 2119 3456 2334 190 -475 -698 N ATOM 4672 N GLU B 343 103.291 11.408 11.550 1.00 10.43 N ANISOU 4672 N GLU B 343 1355 2030 579 -347 56 -26 N ATOM 4673 CA GLU B 343 102.788 10.298 10.748 1.00 10.46 C ANISOU 4673 CA GLU B 343 1572 1785 617 -212 223 -115 C ATOM 4674 C GLU B 343 102.497 10.748 9.314 1.00 9.31 C ANISOU 4674 C GLU B 343 1359 1315 863 -283 -198 -40 C ATOM 4675 O GLU B 343 102.170 9.872 8.499 1.00 10.85 O ANISOU 4675 O GLU B 343 1478 1696 947 -342 -192 -328 O ATOM 4676 CB GLU B 343 101.558 9.623 11.349 1.00 11.53 C ANISOU 4676 CB GLU B 343 1615 1981 784 -34 327 203 C ATOM 4677 CG GLU B 343 101.750 9.156 12.787 1.00 12.40 C ANISOU 4677 CG GLU B 343 1745 2379 588 349 352 -86 C ATOM 4678 CD GLU B 343 102.693 7.998 13.003 1.00 13.55 C ANISOU 4678 CD GLU B 343 1481 2575 1094 258 -101 -9 C ATOM 4679 OE1 GLU B 343 103.051 7.252 12.056 1.00 14.71 O ANISOU 4679 OE1 GLU B 343 2026 2115 1446 -194 -317 -386 O ATOM 4680 OE2 GLU B 343 103.122 7.789 14.165 1.00 14.49 O ANISOU 4680 OE2 GLU B 343 1667 2772 1066 446 -166 -107 O ATOM 4681 N GLY B 344 102.594 12.021 9.002 1.00 10.04 N ANISOU 4681 N GLY B 344 1521 1492 800 -74 -259 269 N ATOM 4682 CA GLY B 344 102.311 12.471 7.635 1.00 10.25 C ANISOU 4682 CA GLY B 344 1488 1844 560 -579 -124 212 C ATOM 4683 C GLY B 344 100.843 12.290 7.257 1.00 11.85 C ANISOU 4683 C GLY B 344 1270 2524 710 -266 171 7 C ATOM 4684 O GLY B 344 100.507 12.106 6.075 1.00 11.47 O ANISOU 4684 O GLY B 344 1372 2237 748 -348 54 15 O ATOM 4685 N ILE B 345 99.947 12.390 8.229 1.00 9.83 N ANISOU 4685 N ILE B 345 1032 2021 683 -674 74 -40 N ATOM 4686 CA ILE B 345 98.525 12.289 8.012 1.00 8.78 C ANISOU 4686 CA ILE B 345 1053 1477 807 -337 68 -240 C ATOM 4687 C ILE B 345 97.883 13.572 8.538 1.00 9.16 C ANISOU 4687 C ILE B 345 1414 1672 393 32 76 -139 C ATOM 4688 O ILE B 345 98.160 13.952 9.686 1.00 10.72 O ANISOU 4688 O ILE B 345 1554 2028 490 -97 -150 -232 O ATOM 4689 CB ILE B 345 97.885 11.071 8.706 1.00 8.99 C ANISOU 4689 CB ILE B 345 1341 1489 585 -1 161 56 C ATOM 4690 CG1 ILE B 345 98.523 9.756 8.282 1.00 9.52 C ANISOU 4690 CG1 ILE B 345 1460 1361 796 -308 68 -317 C ATOM 4691 CG2 ILE B 345 96.386 11.103 8.411 1.00 10.82 C ANISOU 4691 CG2 ILE B 345 1331 1922 857 -154 223 39 C ATOM 4692 CD1 ILE B 345 98.130 8.564 9.143 1.00 11.24 C ANISOU 4692 CD1 ILE B 345 1778 1624 870 42 9 93 C ATOM 4693 N ILE B 346 97.119 14.287 7.728 1.00 8.98 N ANISOU 4693 N ILE B 346 1184 1406 823 97 186 -52 N ATOM 4694 CA ILE B 346 96.457 15.521 8.178 1.00 9.89 C ANISOU 4694 CA ILE B 346 1669 1163 924 94 83 103 C ATOM 4695 C ILE B 346 95.044 15.140 8.590 1.00 10.27 C ANISOU 4695 C ILE B 346 1618 1726 559 -130 0 -222 C ATOM 4696 O ILE B 346 94.228 14.759 7.739 1.00 12.17 O ANISOU 4696 O ILE B 346 2006 2120 497 -382 -296 179 O ATOM 4697 CB ILE B 346 96.396 16.565 7.058 1.00 12.39 C ANISOU 4697 CB ILE B 346 2033 1676 1000 116 -94 348 C ATOM 4698 CG1 ILE B 346 97.782 16.784 6.463 1.00 14.04 C ANISOU 4698 CG1 ILE B 346 2330 1924 1080 126 267 293 C ATOM 4699 CG2 ILE B 346 95.789 17.858 7.596 1.00 13.76 C ANISOU 4699 CG2 ILE B 346 2183 1635 1410 9 -127 131 C ATOM 4700 CD1 ILE B 346 97.858 17.893 5.418 1.00 18.40 C ANISOU 4700 CD1 ILE B 346 3152 2307 1531 87 466 641 C ATOM 4701 N PRO B 347 94.744 15.127 9.875 1.00 9.90 N ANISOU 4701 N PRO B 347 1464 1893 405 -287 -202 44 N ATOM 4702 CA PRO B 347 93.436 14.698 10.352 1.00 10.02 C ANISOU 4702 CA PRO B 347 1382 1946 479 114 7 61 C ATOM 4703 C PRO B 347 92.420 15.812 10.393 1.00 8.90 C ANISOU 4703 C PRO B 347 1217 1681 484 -81 -72 -193 C ATOM 4704 O PRO B 347 92.785 16.973 10.598 1.00 11.21 O ANISOU 4704 O PRO B 347 1901 1697 661 -343 -117 -79 O ATOM 4705 CB PRO B 347 93.740 14.283 11.797 1.00 9.05 C ANISOU 4705 CB PRO B 347 1377 1624 436 -100 -26 -31 C ATOM 4706 CG PRO B 347 94.814 15.239 12.236 1.00 10.72 C ANISOU 4706 CG PRO B 347 1348 2101 623 -380 179 -37 C ATOM 4707 CD PRO B 347 95.610 15.591 11.003 1.00 9.43 C ANISOU 4707 CD PRO B 347 1302 1926 357 -398 -67 91 C ATOM 4708 N ALA B 348 91.139 15.479 10.195 1.00 8.84 N ANISOU 4708 N ALA B 348 1076 1442 839 -45 198 176 N ATOM 4709 CA ALA B 348 90.115 16.493 10.412 1.00 8.91 C ANISOU 4709 CA ALA B 348 1609 957 820 -42 30 -155 C ATOM 4710 C ALA B 348 90.203 17.005 11.863 1.00 9.51 C ANISOU 4710 C ALA B 348 1500 1528 585 138 -255 196 C ATOM 4711 O ALA B 348 90.567 16.226 12.761 1.00 8.95 O ANISOU 4711 O ALA B 348 1694 1262 443 -39 -126 232 O ATOM 4712 CB ALA B 348 88.750 15.872 10.209 1.00 9.64 C ANISOU 4712 CB ALA B 348 1476 1433 753 22 -272 308 C ATOM 4713 N LEU B 349 89.854 18.261 12.059 1.00 9.48 N ANISOU 4713 N LEU B 349 1584 1448 570 -243 18 39 N ATOM 4714 CA LEU B 349 89.825 18.757 13.436 1.00 9.07 C ANISOU 4714 CA LEU B 349 1272 1427 746 -367 113 -220 C ATOM 4715 C LEU B 349 88.816 17.993 14.282 1.00 8.75 C ANISOU 4715 C LEU B 349 1359 1526 439 -306 -133 99 C ATOM 4716 O LEU B 349 89.017 17.908 15.506 1.00 10.32 O ANISOU 4716 O LEU B 349 1829 1675 417 -437 -234 244 O ATOM 4717 CB LEU B 349 89.606 20.257 13.494 1.00 11.75 C ANISOU 4717 CB LEU B 349 1768 1493 1202 -73 267 -169 C ATOM 4718 CG LEU B 349 90.829 21.104 13.140 1.00 11.60 C ANISOU 4718 CG LEU B 349 1988 1317 1102 -167 184 -67 C ATOM 4719 CD1 LEU B 349 90.419 22.550 12.944 1.00 13.93 C ANISOU 4719 CD1 LEU B 349 2379 1325 1589 95 457 -354 C ATOM 4720 CD2 LEU B 349 91.913 20.976 14.203 1.00 12.19 C ANISOU 4720 CD2 LEU B 349 1732 1132 1768 -175 -50 -310 C ATOM 4721 N GLU B 350 87.736 17.504 13.694 1.00 9.50 N ANISOU 4721 N GLU B 350 1166 1741 703 -333 68 -30 N ATOM 4722 CA GLU B 350 86.798 16.687 14.462 1.00 9.19 C ANISOU 4722 CA GLU B 350 1072 1394 1025 -326 -158 75 C ATOM 4723 C GLU B 350 87.548 15.507 15.063 1.00 8.43 C ANISOU 4723 C GLU B 350 1396 1451 355 -206 -147 -40 C ATOM 4724 O GLU B 350 87.586 15.237 16.271 1.00 9.89 O ANISOU 4724 O GLU B 350 1361 2004 393 -79 -87 253 O ATOM 4725 CB GLU B 350 85.674 16.130 13.558 1.00 10.00 C ANISOU 4725 CB GLU B 350 1323 1422 1055 -153 -502 111 C ATOM 4726 CG GLU B 350 84.712 17.173 13.008 1.00 10.91 C ANISOU 4726 CG GLU B 350 1390 1783 972 30 -208 348 C ATOM 4727 CD GLU B 350 85.156 17.827 11.724 1.00 13.06 C ANISOU 4727 CD GLU B 350 1383 2315 1263 -194 -112 641 C ATOM 4728 OE1 GLU B 350 86.332 17.769 11.320 1.00 10.75 O ANISOU 4728 OE1 GLU B 350 1596 1739 748 98 -72 350 O ATOM 4729 OE2 GLU B 350 84.282 18.434 11.040 1.00 19.00 O ANISOU 4729 OE2 GLU B 350 1865 3383 1971 211 -173 1235 O ATOM 4730 N SER B 351 88.166 14.729 14.157 1.00 8.16 N ANISOU 4730 N SER B 351 1490 998 613 -43 -221 26 N ATOM 4731 CA SER B 351 88.872 13.511 14.510 1.00 7.63 C ANISOU 4731 CA SER B 351 1344 906 649 54 -200 -317 C ATOM 4732 C SER B 351 90.032 13.777 15.464 1.00 7.16 C ANISOU 4732 C SER B 351 1213 844 665 -19 -142 -75 C ATOM 4733 O SER B 351 90.399 12.894 16.244 1.00 8.02 O ANISOU 4733 O SER B 351 1427 1031 590 196 -407 -201 O ATOM 4734 CB SER B 351 89.454 12.868 13.234 1.00 9.34 C ANISOU 4734 CB SER B 351 1471 1464 611 265 -75 -266 C ATOM 4735 OG SER B 351 88.503 12.918 12.166 1.00 10.60 O ANISOU 4735 OG SER B 351 2000 1717 310 143 -138 -88 O ATOM 4736 N SER B 352 90.625 14.960 15.329 1.00 8.01 N ANISOU 4736 N SER B 352 1331 1232 480 -420 -183 -72 N ATOM 4737 CA SER B 352 91.729 15.367 16.186 1.00 7.87 C ANISOU 4737 CA SER B 352 962 1563 464 -416 -98 237 C ATOM 4738 C SER B 352 91.305 15.342 17.663 1.00 7.80 C ANISOU 4738 C SER B 352 904 1711 348 1 -253 -46 C ATOM 4739 O SER B 352 92.194 15.205 18.516 1.00 9.83 O ANISOU 4739 O SER B 352 757 2481 496 216 -337 -23 O ATOM 4740 CB SER B 352 92.203 16.759 15.779 1.00 8.86 C ANISOU 4740 CB SER B 352 1126 1473 767 -351 196 138 C ATOM 4741 OG SER B 352 92.811 16.720 14.491 1.00 9.31 O ANISOU 4741 OG SER B 352 1508 1495 534 -288 65 -19 O ATOM 4742 N HIS B 353 90.024 15.524 17.940 1.00 8.10 N ANISOU 4742 N HIS B 353 1047 1689 343 68 -25 -165 N ATOM 4743 CA HIS B 353 89.551 15.445 19.330 1.00 7.63 C ANISOU 4743 CA HIS B 353 1176 1367 356 138 52 -331 C ATOM 4744 C HIS B 353 89.747 14.022 19.850 1.00 8.54 C ANISOU 4744 C HIS B 353 1360 1304 580 -45 -127 -280 C ATOM 4745 O HIS B 353 90.169 13.838 21.012 1.00 9.64 O ANISOU 4745 O HIS B 353 1262 1926 476 -133 34 -188 O ATOM 4746 CB HIS B 353 88.096 15.896 19.439 1.00 9.05 C ANISOU 4746 CB HIS B 353 1255 1534 650 226 121 -154 C ATOM 4747 CG HIS B 353 87.917 17.370 19.361 1.00 8.05 C ANISOU 4747 CG HIS B 353 1277 1494 286 56 -137 -34 C ATOM 4748 ND1 HIS B 353 88.009 18.069 18.171 1.00 9.29 N ANISOU 4748 ND1 HIS B 353 1469 1379 682 -110 -172 340 N ATOM 4749 CD2 HIS B 353 87.637 18.301 20.306 1.00 9.48 C ANISOU 4749 CD2 HIS B 353 1719 1277 604 8 -202 -191 C ATOM 4750 CE1 HIS B 353 87.812 19.358 18.394 1.00 9.62 C ANISOU 4750 CE1 HIS B 353 1761 1466 428 103 -312 271 C ATOM 4751 NE2 HIS B 353 87.592 19.529 19.698 1.00 9.79 N ANISOU 4751 NE2 HIS B 353 1637 1491 594 -45 -191 -29 N ATOM 4752 N ALA B 354 89.397 13.006 19.043 1.00 7.69 N ANISOU 4752 N ALA B 354 1230 1218 474 -225 -465 44 N ATOM 4753 CA ALA B 354 89.598 11.628 19.471 1.00 8.16 C ANISOU 4753 CA ALA B 354 1428 1133 539 -321 24 -21 C ATOM 4754 C ALA B 354 91.076 11.334 19.646 1.00 7.58 C ANISOU 4754 C ALA B 354 1445 985 449 -361 81 32 C ATOM 4755 O ALA B 354 91.488 10.726 20.636 1.00 8.70 O ANISOU 4755 O ALA B 354 1454 1597 254 -116 -36 -26 O ATOM 4756 CB ALA B 354 88.995 10.663 18.456 1.00 9.28 C ANISOU 4756 CB ALA B 354 1493 1141 892 -221 -95 -203 C ATOM 4757 N LEU B 355 91.885 11.782 18.692 1.00 7.96 N ANISOU 4757 N LEU B 355 777 1771 476 -340 92 -167 N ATOM 4758 CA LEU B 355 93.316 11.546 18.771 1.00 6.42 C ANISOU 4758 CA LEU B 355 720 1179 540 -351 72 57 C ATOM 4759 C LEU B 355 93.886 12.203 20.028 1.00 7.17 C ANISOU 4759 C LEU B 355 680 1476 566 137 -175 44 C ATOM 4760 O LEU B 355 94.706 11.587 20.726 1.00 9.11 O ANISOU 4760 O LEU B 355 1234 1808 417 340 -361 103 O ATOM 4761 CB LEU B 355 94.040 12.095 17.515 1.00 8.46 C ANISOU 4761 CB LEU B 355 856 1936 425 -452 128 -46 C ATOM 4762 CG LEU B 355 95.560 11.899 17.559 1.00 9.11 C ANISOU 4762 CG LEU B 355 896 1562 1005 -395 288 148 C ATOM 4763 CD1 LEU B 355 95.962 10.445 17.695 1.00 10.50 C ANISOU 4763 CD1 LEU B 355 1492 1700 796 -39 89 -142 C ATOM 4764 CD2 LEU B 355 96.175 12.507 16.295 1.00 11.76 C ANISOU 4764 CD2 LEU B 355 1417 2299 752 -310 173 406 C ATOM 4765 N ALA B 356 93.425 13.421 20.294 1.00 8.33 N ANISOU 4765 N ALA B 356 1394 1334 439 -253 -204 -353 N ATOM 4766 CA ALA B 356 93.955 14.115 21.471 1.00 8.16 C ANISOU 4766 CA ALA B 356 1420 1210 471 -460 -323 -195 C ATOM 4767 C ALA B 356 93.702 13.314 22.741 1.00 8.20 C ANISOU 4767 C ALA B 356 1245 1398 473 -135 -248 -74 C ATOM 4768 O ALA B 356 94.565 13.309 23.643 1.00 9.19 O ANISOU 4768 O ALA B 356 1105 1943 443 -126 -219 -377 O ATOM 4769 CB ALA B 356 93.319 15.479 21.552 1.00 8.39 C ANISOU 4769 CB ALA B 356 1367 1224 596 -387 -98 -377 C ATOM 4770 N HIS B 357 92.518 12.739 22.866 1.00 8.84 N ANISOU 4770 N HIS B 357 1337 1616 405 -148 -123 212 N ATOM 4771 CA HIS B 357 92.232 11.953 24.074 1.00 7.45 C ANISOU 4771 CA HIS B 357 1231 1348 250 -94 -28 -17 C ATOM 4772 C HIS B 357 93.145 10.743 24.150 1.00 7.44 C ANISOU 4772 C HIS B 357 1315 1187 325 -168 -154 -197 C ATOM 4773 O HIS B 357 93.674 10.420 25.228 1.00 9.91 O ANISOU 4773 O HIS B 357 1294 2093 377 -149 -252 -40 O ATOM 4774 CB HIS B 357 90.725 11.633 24.172 1.00 9.19 C ANISOU 4774 CB HIS B 357 1297 1798 396 -318 -82 211 C ATOM 4775 CG HIS B 357 90.518 10.974 25.512 1.00 8.76 C ANISOU 4775 CG HIS B 357 1285 1632 410 -54 -388 170 C ATOM 4776 ND1 HIS B 357 90.557 11.711 26.698 1.00 10.20 N ANISOU 4776 ND1 HIS B 357 1329 2116 430 225 -8 15 N ATOM 4777 CD2 HIS B 357 90.416 9.676 25.831 1.00 9.95 C ANISOU 4777 CD2 HIS B 357 1549 1682 549 -70 -1 225 C ATOM 4778 CE1 HIS B 357 90.425 10.842 27.667 1.00 8.75 C ANISOU 4778 CE1 HIS B 357 1117 1620 589 -49 63 -110 C ATOM 4779 NE2 HIS B 357 90.327 9.614 27.210 1.00 9.20 N ANISOU 4779 NE2 HIS B 357 1415 1571 510 -35 -75 13 N ATOM 4780 N ALA B 358 93.361 10.024 23.041 1.00 8.53 N ANISOU 4780 N ALA B 358 1444 1444 355 52 -80 -350 N ATOM 4781 CA ALA B 358 94.302 8.902 23.064 1.00 8.74 C ANISOU 4781 CA ALA B 358 1465 1387 469 14 -157 -479 C ATOM 4782 C ALA B 358 95.687 9.373 23.467 1.00 8.11 C ANISOU 4782 C ALA B 358 1325 1398 360 -26 171 -185 C ATOM 4783 O ALA B 358 96.387 8.667 24.191 1.00 10.50 O ANISOU 4783 O ALA B 358 1727 1964 296 216 -92 -165 O ATOM 4784 CB ALA B 358 94.329 8.278 21.652 1.00 10.16 C ANISOU 4784 CB ALA B 358 1788 1639 435 22 -54 -506 C ATOM 4785 N LEU B 359 96.120 10.531 22.971 1.00 8.63 N ANISOU 4785 N LEU B 359 1222 1579 477 -205 -409 119 N ATOM 4786 CA LEU B 359 97.452 11.042 23.329 1.00 8.81 C ANISOU 4786 CA LEU B 359 1030 1777 542 -306 42 23 C ATOM 4787 C LEU B 359 97.504 11.272 24.849 1.00 9.37 C ANISOU 4787 C LEU B 359 1006 1895 661 21 -315 -96 C ATOM 4788 O LEU B 359 98.577 11.041 25.446 1.00 10.02 O ANISOU 4788 O LEU B 359 942 2202 662 258 -232 220 O ATOM 4789 CB LEU B 359 97.776 12.326 22.564 1.00 11.02 C ANISOU 4789 CB LEU B 359 1822 1792 573 -350 42 0 C ATOM 4790 CG LEU B 359 97.955 12.129 21.047 1.00 11.38 C ANISOU 4790 CG LEU B 359 1894 1871 557 -361 4 36 C ATOM 4791 CD1 LEU B 359 98.186 13.482 20.372 1.00 13.04 C ANISOU 4791 CD1 LEU B 359 1637 2036 1282 -563 -303 381 C ATOM 4792 CD2 LEU B 359 99.111 11.189 20.739 1.00 13.48 C ANISOU 4792 CD2 LEU B 359 2002 2516 605 -81 168 224 C ATOM 4793 N LYS B 360 96.420 11.776 25.412 1.00 8.33 N ANISOU 4793 N LYS B 360 1171 1557 438 -168 -191 -34 N ATOM 4794 CA LYS B 360 96.392 12.017 26.870 1.00 8.69 C ANISOU 4794 CA LYS B 360 1584 1187 529 -136 -450 -299 C ATOM 4795 C LYS B 360 96.422 10.682 27.604 1.00 7.88 C ANISOU 4795 C LYS B 360 1155 1482 357 -314 -233 -20 C ATOM 4796 O LYS B 360 97.124 10.540 28.623 1.00 9.39 O ANISOU 4796 O LYS B 360 1045 2064 458 -141 -340 -278 O ATOM 4797 CB LYS B 360 95.142 12.797 27.225 1.00 11.53 C ANISOU 4797 CB LYS B 360 1332 1997 1052 -79 -386 -324 C ATOM 4798 CG LYS B 360 94.890 13.181 28.645 1.00 15.14 C ANISOU 4798 CG LYS B 360 2136 2538 1078 361 -23 -87 C ATOM 4799 CD LYS B 360 93.561 13.929 28.780 1.00 16.09 C ANISOU 4799 CD LYS B 360 2188 2281 1645 334 -20 -214 C ATOM 4800 CE LYS B 360 93.663 15.346 28.249 1.00 16.51 C ANISOU 4800 CE LYS B 360 1930 2351 1992 91 -25 -120 C ATOM 4801 NZ LYS B 360 92.438 16.125 28.589 1.00 16.10 N ANISOU 4801 NZ LYS B 360 2088 2434 1597 263 -305 -343 N ATOM 4802 N MET B 361 95.687 9.667 27.142 1.00 8.18 N ANISOU 4802 N MET B 361 1272 1297 540 -178 34 -311 N ATOM 4803 CA MET B 361 95.712 8.361 27.758 1.00 8.44 C ANISOU 4803 CA MET B 361 1391 1535 280 32 -5 -199 C ATOM 4804 C MET B 361 97.150 7.843 27.846 1.00 8.64 C ANISOU 4804 C MET B 361 1370 1602 311 34 -21 71 C ATOM 4805 O MET B 361 97.605 7.240 28.815 1.00 10.11 O ANISOU 4805 O MET B 361 1405 2057 378 407 -295 -103 O ATOM 4806 CB MET B 361 94.841 7.345 27.022 1.00 9.70 C ANISOU 4806 CB MET B 361 1580 1507 598 -208 3 -128 C ATOM 4807 CG MET B 361 93.357 7.696 27.179 1.00 9.91 C ANISOU 4807 CG MET B 361 1534 1623 608 -136 -175 -52 C ATOM 4808 SD MET B 361 92.331 6.791 26.001 1.00 10.60 S ANISOU 4808 SD MET B 361 1275 2273 480 -92 -285 47 S ATOM 4809 CE MET B 361 92.468 5.140 26.678 1.00 11.27 C ANISOU 4809 CE MET B 361 1535 1876 870 73 -32 -324 C ATOM 4810 N MET B 362 97.870 8.026 26.740 1.00 8.73 N ANISOU 4810 N MET B 362 959 1925 433 -27 20 -135 N ATOM 4811 CA MET B 362 99.247 7.580 26.610 1.00 9.78 C ANISOU 4811 CA MET B 362 1039 2247 429 90 -42 -207 C ATOM 4812 C MET B 362 100.165 8.380 27.527 1.00 9.22 C ANISOU 4812 C MET B 362 1314 1481 708 170 -226 -40 C ATOM 4813 O MET B 362 100.941 7.835 28.318 1.00 10.54 O ANISOU 4813 O MET B 362 1467 2134 401 328 -194 -3 O ATOM 4814 CB MET B 362 99.698 7.752 25.147 1.00 10.20 C ANISOU 4814 CB MET B 362 1359 2126 390 -319 -188 -163 C ATOM 4815 CG MET B 362 101.189 7.507 24.932 1.00 10.82 C ANISOU 4815 CG MET B 362 1470 2300 339 -258 209 18 C ATOM 4816 SD MET B 362 101.630 7.728 23.183 1.00 11.68 S ANISOU 4816 SD MET B 362 1375 2758 305 -79 234 -52 S ATOM 4817 CE MET B 362 101.662 9.498 23.074 1.00 12.17 C ANISOU 4817 CE MET B 362 1367 2657 599 54 -33 115 C ATOM 4818 N ARG B 363 100.118 9.695 27.382 1.00 8.72 N ANISOU 4818 N ARG B 363 1522 1398 393 -60 -323 -252 N ATOM 4819 CA ARG B 363 101.041 10.575 28.091 1.00 9.72 C ANISOU 4819 CA ARG B 363 1729 1657 309 -433 -247 -81 C ATOM 4820 C ARG B 363 100.818 10.591 29.609 1.00 9.63 C ANISOU 4820 C ARG B 363 1426 1887 346 -184 -270 11 C ATOM 4821 O ARG B 363 101.823 10.710 30.317 1.00 10.87 O ANISOU 4821 O ARG B 363 1316 2302 512 -104 -339 -31 O ATOM 4822 CB ARG B 363 100.927 11.996 27.540 1.00 9.96 C ANISOU 4822 CB ARG B 363 1399 1685 700 -135 -346 -12 C ATOM 4823 CG ARG B 363 101.452 12.147 26.106 1.00 11.86 C ANISOU 4823 CG ARG B 363 1600 2152 755 -135 -334 45 C ATOM 4824 CD ARG B 363 100.915 13.456 25.539 1.00 12.15 C ANISOU 4824 CD ARG B 363 2278 1880 460 -320 -363 -4 C ATOM 4825 NE ARG B 363 101.408 13.673 24.173 1.00 11.15 N ANISOU 4825 NE ARG B 363 1532 1914 789 34 -188 321 N ATOM 4826 CZ ARG B 363 100.885 14.587 23.353 1.00 11.66 C ANISOU 4826 CZ ARG B 363 1705 1841 884 -158 -233 430 C ATOM 4827 NH1 ARG B 363 99.847 15.323 23.698 1.00 14.72 N ANISOU 4827 NH1 ARG B 363 1572 2499 1524 -171 -78 187 N ATOM 4828 NH2 ARG B 363 101.427 14.728 22.137 1.00 13.47 N ANISOU 4828 NH2 ARG B 363 1794 2787 538 -159 -550 231 N ATOM 4829 N GLU B 364 99.583 10.478 30.033 1.00 9.99 N ANISOU 4829 N GLU B 364 1400 2017 380 -214 -388 48 N ATOM 4830 CA GLU B 364 99.351 10.518 31.492 1.00 9.69 C ANISOU 4830 CA GLU B 364 1748 1544 392 162 -239 -31 C ATOM 4831 C GLU B 364 99.900 9.266 32.159 1.00 10.75 C ANISOU 4831 C GLU B 364 1969 1450 664 64 -564 -129 C ATOM 4832 O GLU B 364 100.271 9.390 33.349 1.00 12.12 O ANISOU 4832 O GLU B 364 2189 1994 423 -10 -545 -188 O ATOM 4833 CB GLU B 364 97.864 10.678 31.784 1.00 10.36 C ANISOU 4833 CB GLU B 364 1885 1770 282 185 -25 -131 C ATOM 4834 CG GLU B 364 97.358 12.083 31.502 1.00 10.43 C ANISOU 4834 CG GLU B 364 1757 1760 445 170 -50 -98 C ATOM 4835 CD GLU B 364 95.913 12.246 31.928 1.00 11.03 C ANISOU 4835 CD GLU B 364 1721 1923 546 483 -231 -75 C ATOM 4836 OE1 GLU B 364 95.296 11.337 32.519 1.00 12.27 O ANISOU 4836 OE1 GLU B 364 1715 2354 595 60 -416 -96 O ATOM 4837 OE2 GLU B 364 95.367 13.346 31.689 1.00 17.26 O ANISOU 4837 OE2 GLU B 364 2363 2335 1858 1009 95 342 O ATOM 4838 N GLN B 365 99.950 8.139 31.494 1.00 9.86 N ANISOU 4838 N GLN B 365 1689 1739 319 228 -236 -251 N ATOM 4839 CA GLN B 365 100.384 6.879 32.109 1.00 9.80 C ANISOU 4839 CA GLN B 365 1143 1874 707 289 143 52 C ATOM 4840 C GLN B 365 101.210 6.133 31.070 1.00 7.22 C ANISOU 4840 C GLN B 365 1130 1234 380 126 -44 161 C ATOM 4841 O GLN B 365 100.749 5.163 30.462 1.00 10.33 O ANISOU 4841 O GLN B 365 1393 1967 565 -321 -16 -151 O ATOM 4842 CB GLN B 365 99.152 6.075 32.516 1.00 8.91 C ANISOU 4842 CB GLN B 365 1316 1643 427 166 -33 -34 C ATOM 4843 CG GLN B 365 98.238 6.858 33.450 1.00 9.75 C ANISOU 4843 CG GLN B 365 1673 1731 302 77 17 -279 C ATOM 4844 CD GLN B 365 97.049 6.090 33.947 1.00 10.35 C ANISOU 4844 CD GLN B 365 1538 1929 463 60 -173 -145 C ATOM 4845 OE1 GLN B 365 96.291 5.558 33.128 1.00 11.96 O ANISOU 4845 OE1 GLN B 365 1652 2536 357 -470 8 -257 O ATOM 4846 NE2 GLN B 365 96.795 5.990 35.253 1.00 11.13 N ANISOU 4846 NE2 GLN B 365 2017 1758 454 -138 -199 40 N ATOM 4847 N PRO B 366 102.416 6.617 30.863 1.00 9.34 N ANISOU 4847 N PRO B 366 1151 1773 624 13 1 18 N ATOM 4848 CA PRO B 366 103.226 6.139 29.731 1.00 9.50 C ANISOU 4848 CA PRO B 366 1448 1597 563 186 50 108 C ATOM 4849 C PRO B 366 103.709 4.727 29.861 1.00 10.41 C ANISOU 4849 C PRO B 366 1792 1692 472 431 -134 -8 C ATOM 4850 O PRO B 366 104.111 4.123 28.845 1.00 12.42 O ANISOU 4850 O PRO B 366 1639 2753 328 682 40 99 O ATOM 4851 CB PRO B 366 104.345 7.152 29.606 1.00 10.87 C ANISOU 4851 CB PRO B 366 1643 1967 521 -142 -70 -81 C ATOM 4852 CG PRO B 366 104.467 7.741 30.974 1.00 11.03 C ANISOU 4852 CG PRO B 366 1495 2317 381 -58 13 -19 C ATOM 4853 CD PRO B 366 103.041 7.801 31.486 1.00 9.60 C ANISOU 4853 CD PRO B 366 1378 1918 352 -20 -141 -6 C ATOM 4854 N GLU B 367 103.687 4.152 31.072 1.00 9.77 N ANISOU 4854 N GLU B 367 1308 1922 481 72 -234 97 N ATOM 4855 C GLU B 367 102.881 1.859 31.389 1.00 8.97 C ANISOU 4855 C GLU B 367 1320 1687 401 301 -36 -223 C ATOM 4856 O GLU B 367 103.031 0.672 31.702 1.00 11.78 O ANISOU 4856 O GLU B 367 1576 1918 980 299 -215 265 O ATOM 4857 CA AGLU B 367 104.090 2.772 31.243 0.50 9.72 C ANISOU 4857 CA AGLU B 367 1368 1891 435 158 -225 -35 C ATOM 4858 CB AGLU B 367 105.075 2.560 32.400 0.50 8.79 C ANISOU 4858 CB AGLU B 367 789 1824 726 158 -156 21 C ATOM 4859 CG AGLU B 367 106.484 3.005 32.017 0.50 7.47 C ANISOU 4859 CG AGLU B 367 1048 1392 400 155 259 -24 C ATOM 4860 CD AGLU B 367 106.614 4.511 31.952 0.50 8.63 C ANISOU 4860 CD AGLU B 367 953 1391 937 103 351 -15 C ATOM 4861 OE1AGLU B 367 106.431 5.212 32.979 0.50 10.29 O ANISOU 4861 OE1AGLU B 367 1484 2079 347 32 59 131 O ATOM 4862 OE2AGLU B 367 106.908 5.060 30.861 0.50 12.79 O ANISOU 4862 OE2AGLU B 367 1414 2362 1084 341 396 322 O ATOM 4863 CA BGLU B 367 104.094 2.766 31.231 0.50 10.60 C ANISOU 4863 CA BGLU B 367 1514 1858 657 94 -195 -31 C ATOM 4864 CB BGLU B 367 105.036 2.629 32.438 0.50 12.30 C ANISOU 4864 CB BGLU B 367 1388 2175 1109 128 -408 50 C ATOM 4865 CG BGLU B 367 106.185 3.628 32.377 0.50 14.97 C ANISOU 4865 CG BGLU B 367 1801 2101 1786 -6 -172 91 C ATOM 4866 CD BGLU B 367 107.084 3.408 31.177 0.50 16.55 C ANISOU 4866 CD BGLU B 367 1848 2362 2080 49 -20 -51 C ATOM 4867 OE1BGLU B 367 107.172 2.255 30.703 0.50 18.12 O ANISOU 4867 OE1BGLU B 367 2099 2560 2226 336 -161 -179 O ATOM 4868 OE2BGLU B 367 107.688 4.406 30.728 0.50 18.59 O ANISOU 4868 OE2BGLU B 367 2456 2560 2046 148 237 190 O ATOM 4869 N LYS B 368 101.677 2.362 31.116 1.00 9.96 N ANISOU 4869 N LYS B 368 1207 2284 292 125 -201 -57 N ATOM 4870 CA LYS B 368 100.487 1.517 31.075 1.00 9.92 C ANISOU 4870 CA LYS B 368 1245 2082 442 223 -123 -75 C ATOM 4871 C LYS B 368 100.429 0.808 29.708 1.00 10.32 C ANISOU 4871 C LYS B 368 1734 1530 656 337 -324 -106 C ATOM 4872 O LYS B 368 100.415 1.507 28.683 1.00 11.83 O ANISOU 4872 O LYS B 368 1798 2122 574 455 -15 79 O ATOM 4873 CB LYS B 368 99.224 2.358 31.270 1.00 10.22 C ANISOU 4873 CB LYS B 368 1386 1761 734 236 -197 97 C ATOM 4874 CG LYS B 368 97.935 1.587 31.242 1.00 10.84 C ANISOU 4874 CG LYS B 368 1208 1945 966 321 -125 -254 C ATOM 4875 CD LYS B 368 96.707 2.468 31.419 1.00 9.24 C ANISOU 4875 CD LYS B 368 942 2007 562 199 -194 -238 C ATOM 4876 CE LYS B 368 95.412 1.674 31.426 1.00 12.95 C ANISOU 4876 CE LYS B 368 1124 2537 1258 -45 -288 -450 C ATOM 4877 NZ LYS B 368 94.225 2.507 31.718 1.00 13.28 N ANISOU 4877 NZ LYS B 368 1654 2627 766 416 -214 -28 N ATOM 4878 N GLU B 369 100.363 -0.500 29.671 1.00 10.43 N ANISOU 4878 N GLU B 369 1954 1530 477 323 -326 -92 N ATOM 4879 CA GLU B 369 100.244 -1.254 28.423 1.00 11.93 C ANISOU 4879 CA GLU B 369 2046 1806 681 112 -210 -313 C ATOM 4880 C GLU B 369 98.813 -1.096 27.944 1.00 11.88 C ANISOU 4880 C GLU B 369 1902 1971 639 195 92 -93 C ATOM 4881 O GLU B 369 97.851 -1.390 28.657 1.00 13.56 O ANISOU 4881 O GLU B 369 2198 2571 381 -217 92 -51 O ATOM 4882 CB GLU B 369 100.601 -2.736 28.601 1.00 16.84 C ANISOU 4882 CB GLU B 369 3144 1872 1384 204 -90 -114 C ATOM 4883 CG GLU B 369 100.853 -3.386 27.225 1.00 22.39 C ANISOU 4883 CG GLU B 369 3970 3054 1483 266 -134 -459 C ATOM 4884 CD GLU B 369 101.115 -4.875 27.274 1.00 30.45 C ANISOU 4884 CD GLU B 369 4589 3205 3775 177 -28 -83 C ATOM 4885 OE1 GLU B 369 101.262 -5.440 28.379 1.00 33.19 O ANISOU 4885 OE1 GLU B 369 4903 3427 4279 341 51 336 O ATOM 4886 OE2 GLU B 369 101.169 -5.488 26.185 1.00 32.31 O ANISOU 4886 OE2 GLU B 369 4613 3578 4087 249 243 -338 O ATOM 4887 N GLN B 370 98.649 -0.512 26.757 1.00 10.50 N ANISOU 4887 N GLN B 370 1534 1931 523 108 -115 -184 N ATOM 4888 CA GLN B 370 97.297 -0.339 26.240 1.00 10.28 C ANISOU 4888 CA GLN B 370 1663 1748 494 258 -226 -86 C ATOM 4889 C GLN B 370 97.330 -0.332 24.706 1.00 9.59 C ANISOU 4889 C GLN B 370 1732 1456 454 -181 -176 75 C ATOM 4890 O GLN B 370 98.203 0.282 24.098 1.00 11.43 O ANISOU 4890 O GLN B 370 1676 2260 406 -309 -82 49 O ATOM 4891 CB GLN B 370 96.626 0.912 26.774 1.00 12.73 C ANISOU 4891 CB GLN B 370 1908 1789 1138 140 -318 -575 C ATOM 4892 CG GLN B 370 97.359 2.213 26.643 1.00 13.53 C ANISOU 4892 CG GLN B 370 1316 1945 1881 199 6 -321 C ATOM 4893 CD GLN B 370 96.821 3.358 27.492 1.00 11.42 C ANISOU 4893 CD GLN B 370 1268 2255 817 42 -323 -434 C ATOM 4894 OE1 GLN B 370 95.614 3.468 27.777 1.00 11.49 O ANISOU 4894 OE1 GLN B 370 1351 2392 622 108 -214 -48 O ATOM 4895 NE2 GLN B 370 97.649 4.309 27.907 1.00 11.51 N ANISOU 4895 NE2 GLN B 370 1486 1598 1288 63 -94 -113 N ATOM 4896 N LEU B 371 96.319 -1.015 24.177 1.00 8.83 N ANISOU 4896 N LEU B 371 1407 1674 273 24 -168 -20 N ATOM 4897 CA LEU B 371 96.156 -1.120 22.715 1.00 9.16 C ANISOU 4897 CA LEU B 371 1439 1643 397 130 -420 -66 C ATOM 4898 C LEU B 371 94.907 -0.326 22.340 1.00 7.44 C ANISOU 4898 C LEU B 371 1300 1158 370 -74 -240 -27 C ATOM 4899 O LEU B 371 93.804 -0.666 22.757 1.00 10.17 O ANISOU 4899 O LEU B 371 1366 1939 560 208 102 439 O ATOM 4900 CB LEU B 371 95.961 -2.574 22.339 1.00 9.41 C ANISOU 4900 CB LEU B 371 1429 1599 548 -96 -336 26 C ATOM 4901 CG LEU B 371 95.601 -2.874 20.869 1.00 10.32 C ANISOU 4901 CG LEU B 371 2004 1444 472 -200 -194 -25 C ATOM 4902 CD1 LEU B 371 96.670 -2.335 19.942 1.00 12.32 C ANISOU 4902 CD1 LEU B 371 2055 2022 603 -368 -130 10 C ATOM 4903 CD2 LEU B 371 95.419 -4.367 20.701 1.00 11.88 C ANISOU 4903 CD2 LEU B 371 1989 1497 1029 -231 -452 -234 C ATOM 4904 N LEU B 372 95.120 0.786 21.656 1.00 8.24 N ANISOU 4904 N LEU B 372 1250 1570 311 12 52 281 N ATOM 4905 CA LEU B 372 94.061 1.721 21.369 1.00 9.14 C ANISOU 4905 CA LEU B 372 1354 1609 510 118 -135 58 C ATOM 4906 C LEU B 372 93.804 1.881 19.868 1.00 8.20 C ANISOU 4906 C LEU B 372 1016 1462 636 -36 -122 343 C ATOM 4907 O LEU B 372 94.751 1.858 19.095 1.00 10.06 O ANISOU 4907 O LEU B 372 1051 2428 344 121 -207 28 O ATOM 4908 CB LEU B 372 94.467 3.101 21.915 1.00 9.06 C ANISOU 4908 CB LEU B 372 1313 1656 475 90 -219 125 C ATOM 4909 CG LEU B 372 94.908 3.153 23.390 1.00 9.97 C ANISOU 4909 CG LEU B 372 1572 1789 427 64 -159 -26 C ATOM 4910 CD1 LEU B 372 95.219 4.605 23.718 1.00 10.74 C ANISOU 4910 CD1 LEU B 372 1727 1785 570 126 -306 -63 C ATOM 4911 CD2 LEU B 372 93.822 2.575 24.283 1.00 11.69 C ANISOU 4911 CD2 LEU B 372 1908 1974 558 -196 -91 27 C ATOM 4912 N VAL B 373 92.537 2.100 19.574 1.00 9.30 N ANISOU 4912 N VAL B 373 1071 2095 368 203 -215 189 N ATOM 4913 CA VAL B 373 92.174 2.452 18.197 1.00 8.35 C ANISOU 4913 CA VAL B 373 1243 1317 613 214 -389 260 C ATOM 4914 C VAL B 373 91.443 3.790 18.246 1.00 8.26 C ANISOU 4914 C VAL B 373 1077 1280 783 102 -187 194 C ATOM 4915 O VAL B 373 90.443 3.914 18.957 1.00 9.68 O ANISOU 4915 O VAL B 373 1461 1650 567 -83 76 174 O ATOM 4916 CB VAL B 373 91.254 1.433 17.523 1.00 9.26 C ANISOU 4916 CB VAL B 373 1446 1574 500 2 -188 92 C ATOM 4917 CG1 VAL B 373 90.940 1.923 16.111 1.00 10.38 C ANISOU 4917 CG1 VAL B 373 2055 1325 565 13 -364 69 C ATOM 4918 CG2 VAL B 373 91.911 0.066 17.483 1.00 9.89 C ANISOU 4918 CG2 VAL B 373 1763 1525 471 3 153 -69 C ATOM 4919 N VAL B 374 91.909 4.739 17.465 1.00 8.13 N ANISOU 4919 N VAL B 374 1261 1419 408 -200 -232 22 N ATOM 4920 CA VAL B 374 91.227 6.002 17.267 1.00 8.71 C ANISOU 4920 CA VAL B 374 1260 1695 354 96 -7 -188 C ATOM 4921 C VAL B 374 90.494 5.936 15.921 1.00 8.73 C ANISOU 4921 C VAL B 374 1195 1831 290 123 97 2 C ATOM 4922 O VAL B 374 91.106 5.545 14.911 1.00 9.44 O ANISOU 4922 O VAL B 374 1072 2241 273 175 -3 -218 O ATOM 4923 CB VAL B 374 92.214 7.180 17.253 1.00 8.85 C ANISOU 4923 CB VAL B 374 1596 1445 323 88 -314 -54 C ATOM 4924 CG1 VAL B 374 91.590 8.413 16.640 1.00 9.51 C ANISOU 4924 CG1 VAL B 374 1834 1404 376 277 -181 -135 C ATOM 4925 CG2 VAL B 374 92.664 7.474 18.683 1.00 10.97 C ANISOU 4925 CG2 VAL B 374 1919 1847 402 61 -495 -113 C ATOM 4926 N ASN B 375 89.233 6.337 15.896 1.00 9.36 N ANISOU 4926 N ASN B 375 1100 2126 330 11 -261 -57 N ATOM 4927 CA ASN B 375 88.523 6.384 14.609 1.00 7.98 C ANISOU 4927 CA ASN B 375 1055 1683 295 48 -186 58 C ATOM 4928 C ASN B 375 88.907 7.709 13.949 1.00 8.02 C ANISOU 4928 C ASN B 375 797 1514 736 24 -88 -63 C ATOM 4929 O ASN B 375 88.528 8.773 14.416 1.00 8.87 O ANISOU 4929 O ASN B 375 1604 1281 486 -6 -223 108 O ATOM 4930 CB ASN B 375 87.020 6.272 14.806 1.00 8.29 C ANISOU 4930 CB ASN B 375 983 1554 615 182 -402 -15 C ATOM 4931 CG ASN B 375 86.325 5.979 13.490 1.00 8.81 C ANISOU 4931 CG ASN B 375 1167 1527 655 84 -332 -118 C ATOM 4932 OD1 ASN B 375 86.925 5.355 12.610 1.00 10.68 O ANISOU 4932 OD1 ASN B 375 1394 2231 433 -30 -199 -242 O ATOM 4933 ND2 ASN B 375 85.069 6.379 13.396 1.00 9.47 N ANISOU 4933 ND2 ASN B 375 1361 1523 713 384 -424 -268 N ATOM 4934 N LEU B 376 89.702 7.621 12.871 1.00 8.51 N ANISOU 4934 N LEU B 376 1128 1671 436 -62 -93 98 N ATOM 4935 CA LEU B 376 90.099 8.862 12.190 1.00 8.63 C ANISOU 4935 CA LEU B 376 1208 1428 641 200 36 82 C ATOM 4936 C LEU B 376 88.997 9.180 11.182 1.00 9.48 C ANISOU 4936 C LEU B 376 1141 1652 809 281 8 -29 C ATOM 4937 O LEU B 376 89.040 8.801 10.017 1.00 9.49 O ANISOU 4937 O LEU B 376 1519 1410 678 -135 -228 77 O ATOM 4938 CB LEU B 376 91.465 8.766 11.530 1.00 9.13 C ANISOU 4938 CB LEU B 376 1337 1625 509 -38 184 354 C ATOM 4939 CG LEU B 376 92.137 10.134 11.376 1.00 12.06 C ANISOU 4939 CG LEU B 376 1773 1953 856 -505 463 180 C ATOM 4940 CD1 LEU B 376 92.637 10.576 12.756 1.00 16.11 C ANISOU 4940 CD1 LEU B 376 2263 2681 1177 -235 -102 43 C ATOM 4941 CD2 LEU B 376 93.299 9.977 10.403 1.00 12.33 C ANISOU 4941 CD2 LEU B 376 1686 2120 877 -340 362 70 C ATOM 4942 N SER B 377 87.971 9.829 11.682 1.00 8.70 N ANISOU 4942 N SER B 377 917 1926 464 298 -211 -83 N ATOM 4943 CA SER B 377 86.727 10.012 10.950 1.00 8.36 C ANISOU 4943 CA SER B 377 736 1993 449 389 -31 277 C ATOM 4944 C SER B 377 86.872 10.793 9.652 1.00 8.38 C ANISOU 4944 C SER B 377 1001 1659 523 -250 -108 146 C ATOM 4945 O SER B 377 86.038 10.567 8.757 1.00 9.23 O ANISOU 4945 O SER B 377 1101 2054 352 115 -115 -325 O ATOM 4946 CB SER B 377 85.683 10.597 11.900 1.00 9.35 C ANISOU 4946 CB SER B 377 1136 1722 697 89 199 -169 C ATOM 4947 OG SER B 377 86.102 11.841 12.435 1.00 9.49 O ANISOU 4947 OG SER B 377 1398 1926 282 -89 71 -215 O ATOM 4948 N GLY B 378 87.883 11.652 9.528 1.00 8.15 N ANISOU 4948 N GLY B 378 1227 1497 374 -353 182 178 N ATOM 4949 CA GLY B 378 88.023 12.360 8.240 1.00 9.70 C ANISOU 4949 CA GLY B 378 1365 1831 488 -272 342 368 C ATOM 4950 C GLY B 378 89.410 12.954 8.097 1.00 10.35 C ANISOU 4950 C GLY B 378 1253 2037 644 -231 52 165 C ATOM 4951 O GLY B 378 90.205 12.996 9.043 1.00 11.16 O ANISOU 4951 O GLY B 378 1529 2361 351 -119 60 -119 O ATOM 4952 N ARG B 379 89.694 13.431 6.884 1.00 10.64 N ANISOU 4952 N ARG B 379 1848 1817 377 -78 118 -2 N ATOM 4953 CA ARG B 379 90.939 14.108 6.551 1.00 11.99 C ANISOU 4953 CA ARG B 379 1898 1831 827 -304 -119 -208 C ATOM 4954 C ARG B 379 90.775 15.605 6.844 1.00 9.78 C ANISOU 4954 C ARG B 379 1562 1788 366 -76 45 133 C ATOM 4955 O ARG B 379 89.680 16.161 6.875 1.00 9.85 O ANISOU 4955 O ARG B 379 1390 1872 478 -162 -2 -177 O ATOM 4956 CB ARG B 379 91.421 13.848 5.126 1.00 15.03 C ANISOU 4956 CB ARG B 379 2547 1961 1201 -133 426 -201 C ATOM 4957 CG ARG B 379 90.459 14.251 4.031 1.00 17.20 C ANISOU 4957 CG ARG B 379 1900 2756 1879 -67 306 -262 C ATOM 4958 CD ARG B 379 91.177 14.192 2.652 1.00 18.90 C ANISOU 4958 CD ARG B 379 2515 2934 1731 -163 299 -105 C ATOM 4959 NE AARG B 379 90.201 14.691 1.660 0.80 19.33 N ANISOU 4959 NE AARG B 379 2268 3751 1325 -195 498 -126 N ATOM 4960 CZ AARG B 379 89.576 13.825 0.875 0.80 16.48 C ANISOU 4960 CZ AARG B 379 2136 2901 1227 -159 546 283 C ATOM 4961 NH1AARG B 379 89.898 12.541 0.978 0.80 22.07 N ANISOU 4961 NH1AARG B 379 2725 3228 2432 107 705 359 N ATOM 4962 NH2AARG B 379 88.664 14.229 0.027 0.80 20.22 N ANISOU 4962 NH2AARG B 379 1274 5435 973 -580 660 -117 N ATOM 4963 NE BARG B 379 91.172 12.775 2.248 0.20 17.86 N ANISOU 4963 NE BARG B 379 2127 2769 1889 -66 293 -18 N ATOM 4964 CZ BARG B 379 90.261 12.331 1.386 0.20 16.93 C ANISOU 4964 CZ BARG B 379 2194 2282 1955 126 141 50 C ATOM 4965 NH1BARG B 379 89.392 13.211 0.885 0.20 17.20 N ANISOU 4965 NH1BARG B 379 2277 2131 2125 222 221 48 N ATOM 4966 NH2BARG B 379 90.168 11.073 0.990 0.20 15.29 N ANISOU 4966 NH2BARG B 379 2057 2225 1527 394 4 -22 N ATOM 4967 N GLY B 380 91.894 16.277 7.067 1.00 10.99 N ANISOU 4967 N GLY B 380 1942 1742 492 -348 38 -248 N ATOM 4968 CA GLY B 380 91.922 17.650 7.517 1.00 11.52 C ANISOU 4968 CA GLY B 380 2017 1517 842 -355 -232 2 C ATOM 4969 C GLY B 380 92.361 18.699 6.528 1.00 12.03 C ANISOU 4969 C GLY B 380 2094 1465 1012 -367 -66 9 C ATOM 4970 O GLY B 380 92.666 19.826 6.900 1.00 13.37 O ANISOU 4970 O GLY B 380 2483 1406 1193 -330 103 -34 O ATOM 4971 N ASP B 381 92.415 18.332 5.242 1.00 15.04 N ANISOU 4971 N ASP B 381 3011 1737 967 -264 223 96 N ATOM 4972 CA ASP B 381 92.732 19.353 4.235 1.00 17.48 C ANISOU 4972 CA ASP B 381 3249 2027 1366 -120 549 340 C ATOM 4973 C ASP B 381 91.832 20.568 4.385 1.00 16.72 C ANISOU 4973 C ASP B 381 3043 2086 1223 -156 351 343 C ATOM 4974 O ASP B 381 92.287 21.717 4.244 1.00 19.56 O ANISOU 4974 O ASP B 381 3527 2491 1416 -621 923 669 O ATOM 4975 CB ASP B 381 92.535 18.699 2.860 1.00 18.33 C ANISOU 4975 CB ASP B 381 3295 2489 1182 -126 440 464 C ATOM 4976 CG ASP B 381 93.566 17.597 2.694 1.00 23.29 C ANISOU 4976 CG ASP B 381 3538 2742 2568 84 229 133 C ATOM 4977 OD1 ASP B 381 94.749 17.921 2.465 1.00 28.72 O ANISOU 4977 OD1 ASP B 381 3951 3557 3404 45 939 305 O ATOM 4978 OD2 ASP B 381 93.193 16.423 2.847 1.00 26.04 O ANISOU 4978 OD2 ASP B 381 4137 2897 2861 -289 -125 -64 O ATOM 4979 N LYS B 382 90.562 20.329 4.688 1.00 15.55 N ANISOU 4979 N LYS B 382 2881 2195 833 165 232 412 N ATOM 4980 CA LYS B 382 89.556 21.346 4.871 1.00 14.30 C ANISOU 4980 CA LYS B 382 2722 2074 636 158 -83 831 C ATOM 4981 C LYS B 382 89.858 22.300 6.020 1.00 16.22 C ANISOU 4981 C LYS B 382 2769 1966 1428 124 97 347 C ATOM 4982 O LYS B 382 89.257 23.370 6.136 1.00 20.27 O ANISOU 4982 O LYS B 382 3845 2000 1856 504 61 786 O ATOM 4983 CB LYS B 382 88.189 20.702 5.163 1.00 16.20 C ANISOU 4983 CB LYS B 382 2786 2325 1046 108 211 621 C ATOM 4984 CG LYS B 382 88.144 20.015 6.535 1.00 15.74 C ANISOU 4984 CG LYS B 382 2671 2276 1031 103 114 629 C ATOM 4985 CD LYS B 382 86.915 19.134 6.639 1.00 15.64 C ANISOU 4985 CD LYS B 382 2742 2234 968 17 -162 301 C ATOM 4986 CE LYS B 382 86.921 18.337 7.949 1.00 15.73 C ANISOU 4986 CE LYS B 382 3023 1954 1001 43 16 214 C ATOM 4987 NZ LYS B 382 86.902 19.234 9.126 1.00 16.18 N ANISOU 4987 NZ LYS B 382 2688 2274 1187 62 203 -38 N ATOM 4988 N ASP B 383 90.714 21.855 6.934 1.00 14.54 N ANISOU 4988 N ASP B 383 2617 1638 1271 129 229 226 N ATOM 4989 CA ASP B 383 91.019 22.626 8.128 1.00 15.20 C ANISOU 4989 CA ASP B 383 2620 1846 1310 -65 164 192 C ATOM 4990 C ASP B 383 92.338 23.367 8.090 1.00 15.71 C ANISOU 4990 C ASP B 383 2540 1878 1553 -15 232 43 C ATOM 4991 O ASP B 383 92.678 24.036 9.064 1.00 16.79 O ANISOU 4991 O ASP B 383 3209 1556 1613 -277 494 59 O ATOM 4992 CB ASP B 383 91.065 21.647 9.325 1.00 15.15 C ANISOU 4992 CB ASP B 383 2669 1535 1554 -262 -28 221 C ATOM 4993 CG ASP B 383 89.707 21.054 9.622 1.00 14.23 C ANISOU 4993 CG ASP B 383 2370 1827 1210 101 -3 387 C ATOM 4994 OD1 ASP B 383 88.715 21.818 9.713 1.00 16.62 O ANISOU 4994 OD1 ASP B 383 2307 2199 1809 164 375 232 O ATOM 4995 OD2 ASP B 383 89.623 19.812 9.735 1.00 14.70 O ANISOU 4995 OD2 ASP B 383 2952 1861 773 -12 40 644 O ATOM 4996 N ILE B 384 93.102 23.219 7.003 1.00 17.32 N ANISOU 4996 N ILE B 384 2596 2117 1866 -265 627 476 N ATOM 4997 CA ILE B 384 94.417 23.850 6.946 1.00 19.74 C ANISOU 4997 CA ILE B 384 2363 2662 2476 -148 308 53 C ATOM 4998 C ILE B 384 94.369 25.360 7.058 1.00 19.44 C ANISOU 4998 C ILE B 384 2443 2666 2277 -114 594 10 C ATOM 4999 O ILE B 384 95.234 25.928 7.726 1.00 22.53 O ANISOU 4999 O ILE B 384 3094 3076 2389 -797 627 142 O ATOM 5000 CB ILE B 384 95.185 23.408 5.682 1.00 23.35 C ANISOU 5000 CB ILE B 384 2702 3065 3104 135 688 -192 C ATOM 5001 CG1 ILE B 384 95.775 22.025 5.944 1.00 20.88 C ANISOU 5001 CG1 ILE B 384 2439 3274 2222 287 551 -53 C ATOM 5002 CG2 ILE B 384 96.271 24.404 5.310 1.00 26.86 C ANISOU 5002 CG2 ILE B 384 3384 3258 3563 -205 431 127 C ATOM 5003 CD1 ILE B 384 94.839 20.933 6.337 1.00 27.39 C ANISOU 5003 CD1 ILE B 384 3504 3527 3377 -187 346 -70 C ATOM 5004 N PHE B 385 93.370 25.996 6.469 1.00 21.97 N ANISOU 5004 N PHE B 385 2891 2944 2515 -25 387 295 N ATOM 5005 CA PHE B 385 93.245 27.452 6.560 1.00 25.78 C ANISOU 5005 CA PHE B 385 3430 3059 3305 24 409 -132 C ATOM 5006 C PHE B 385 92.956 27.849 8.006 1.00 24.35 C ANISOU 5006 C PHE B 385 3184 2894 3174 -78 265 -51 C ATOM 5007 O PHE B 385 93.567 28.760 8.566 1.00 24.39 O ANISOU 5007 O PHE B 385 3188 2417 3663 -164 497 127 O ATOM 5008 CB PHE B 385 92.157 27.938 5.604 1.00 31.15 C ANISOU 5008 CB PHE B 385 3872 4209 3756 30 28 89 C ATOM 5009 CG PHE B 385 92.085 29.428 5.448 1.00 37.85 C ANISOU 5009 CG PHE B 385 4980 4409 4993 117 -3 91 C ATOM 5010 CD1 PHE B 385 92.781 30.063 4.433 1.00 40.92 C ANISOU 5010 CD1 PHE B 385 5266 5084 5196 -37 230 121 C ATOM 5011 CD2 PHE B 385 91.327 30.198 6.315 1.00 39.74 C ANISOU 5011 CD2 PHE B 385 5123 4989 4986 143 128 -31 C ATOM 5012 CE1 PHE B 385 92.719 31.438 4.281 1.00 42.48 C ANISOU 5012 CE1 PHE B 385 5481 5118 5539 45 115 41 C ATOM 5013 CE2 PHE B 385 91.263 31.570 6.172 1.00 41.32 C ANISOU 5013 CE2 PHE B 385 5381 5014 5305 73 81 25 C ATOM 5014 CZ PHE B 385 91.960 32.190 5.156 1.00 42.43 C ANISOU 5014 CZ PHE B 385 5421 5228 5472 25 145 59 C ATOM 5015 N THR B 386 92.040 27.131 8.655 1.00 24.66 N ANISOU 5015 N THR B 386 3644 2628 3098 -25 427 12 N ATOM 5016 CA THR B 386 91.697 27.421 10.044 1.00 23.31 C ANISOU 5016 CA THR B 386 3164 2725 2967 -67 265 33 C ATOM 5017 C THR B 386 92.904 27.316 10.965 1.00 23.33 C ANISOU 5017 C THR B 386 3127 2744 2995 -1 283 -98 C ATOM 5018 O THR B 386 93.139 28.159 11.833 1.00 25.94 O ANISOU 5018 O THR B 386 3633 2783 3440 -321 308 -252 O ATOM 5019 CB THR B 386 90.626 26.447 10.575 1.00 23.35 C ANISOU 5019 CB THR B 386 3183 2874 2816 -146 371 -133 C ATOM 5020 OG1 THR B 386 89.447 26.631 9.801 1.00 26.81 O ANISOU 5020 OG1 THR B 386 3384 3456 3348 -21 249 192 O ATOM 5021 CG2 THR B 386 90.337 26.722 12.046 1.00 24.85 C ANISOU 5021 CG2 THR B 386 3351 3257 2834 49 416 -63 C ATOM 5022 N VAL B 387 93.643 26.223 10.795 1.00 21.05 N ANISOU 5022 N VAL B 387 2938 2699 2360 -88 383 -62 N ATOM 5023 CA VAL B 387 94.817 25.965 11.609 1.00 22.00 C ANISOU 5023 CA VAL B 387 2769 2740 2852 -125 320 -124 C ATOM 5024 C VAL B 387 95.878 27.019 11.301 1.00 24.24 C ANISOU 5024 C VAL B 387 3097 2917 3195 -328 319 44 C ATOM 5025 O VAL B 387 96.425 27.615 12.224 1.00 24.51 O ANISOU 5025 O VAL B 387 3281 2870 3163 -564 489 88 O ATOM 5026 CB VAL B 387 95.348 24.541 11.406 1.00 19.73 C ANISOU 5026 CB VAL B 387 2411 2590 2494 -341 478 -62 C ATOM 5027 CG1 VAL B 387 96.672 24.336 12.125 1.00 20.67 C ANISOU 5027 CG1 VAL B 387 2602 2873 2379 -140 400 -319 C ATOM 5028 CG2 VAL B 387 94.299 23.528 11.882 1.00 19.02 C ANISOU 5028 CG2 VAL B 387 2550 2440 2238 -297 496 0 C ATOM 5029 N HIS B 388 96.119 27.257 10.010 1.00 27.21 N ANISOU 5029 N HIS B 388 3722 3375 3240 -344 281 102 N ATOM 5030 CA HIS B 388 97.122 28.257 9.640 1.00 28.92 C ANISOU 5030 CA HIS B 388 3652 3471 3867 -384 224 72 C ATOM 5031 C HIS B 388 96.849 29.595 10.318 1.00 28.51 C ANISOU 5031 C HIS B 388 3740 3498 3595 -244 133 116 C ATOM 5032 O HIS B 388 97.748 30.206 10.897 1.00 31.29 O ANISOU 5032 O HIS B 388 4230 3458 4200 -636 92 171 O ATOM 5033 CB HIS B 388 97.161 28.450 8.123 1.00 31.45 C ANISOU 5033 CB HIS B 388 4172 3899 3877 -75 124 12 C ATOM 5034 CG HIS B 388 98.151 29.488 7.689 1.00 35.25 C ANISOU 5034 CG HIS B 388 4514 4223 4658 -257 212 128 C ATOM 5035 ND1 HIS B 388 97.823 30.824 7.613 1.00 36.74 N ANISOU 5035 ND1 HIS B 388 4785 4285 4888 -90 123 116 N ATOM 5036 CD2 HIS B 388 99.447 29.387 7.317 1.00 36.17 C ANISOU 5036 CD2 HIS B 388 4478 4490 4776 -89 145 22 C ATOM 5037 CE1 HIS B 388 98.880 31.507 7.205 1.00 37.45 C ANISOU 5037 CE1 HIS B 388 4688 4529 5011 -76 171 106 C ATOM 5038 NE2 HIS B 388 99.875 30.660 7.018 1.00 37.55 N ANISOU 5038 NE2 HIS B 388 4736 4544 4989 -76 140 109 N ATOM 5039 N ASP B 389 95.609 30.058 10.224 1.00 29.84 N ANISOU 5039 N ASP B 389 3862 3633 3843 -125 233 242 N ATOM 5040 CA ASP B 389 95.218 31.334 10.802 1.00 32.51 C ANISOU 5040 CA ASP B 389 4444 3770 4140 -150 158 -13 C ATOM 5041 C ASP B 389 95.420 31.373 12.308 1.00 33.94 C ANISOU 5041 C ASP B 389 4699 3999 4198 -167 77 69 C ATOM 5042 O ASP B 389 95.866 32.395 12.834 1.00 35.38 O ANISOU 5042 O ASP B 389 5028 3746 4668 -186 122 121 O ATOM 5043 CB ASP B 389 93.766 31.666 10.443 1.00 36.32 C ANISOU 5043 CB ASP B 389 4684 4354 4763 74 -21 -8 C ATOM 5044 CG ASP B 389 93.679 32.169 9.010 1.00 39.44 C ANISOU 5044 CG ASP B 389 5202 4841 4944 62 -23 143 C ATOM 5045 OD1 ASP B 389 94.757 32.357 8.404 1.00 41.90 O ANISOU 5045 OD1 ASP B 389 5323 5195 5402 -53 53 120 O ATOM 5046 OD2 ASP B 389 92.562 32.372 8.503 1.00 41.42 O ANISOU 5046 OD2 ASP B 389 5303 5124 5312 15 -171 -19 O ATOM 5047 N ILE B 390 95.126 30.274 13.002 1.00 32.67 N ANISOU 5047 N ILE B 390 4536 3813 4063 -109 145 -28 N ATOM 5048 CA ILE B 390 95.309 30.263 14.455 1.00 33.41 C ANISOU 5048 CA ILE B 390 4521 4013 4162 -49 37 -8 C ATOM 5049 C ILE B 390 96.778 30.357 14.830 1.00 34.00 C ANISOU 5049 C ILE B 390 4492 4165 4260 -86 58 -17 C ATOM 5050 O ILE B 390 97.184 31.172 15.662 1.00 36.00 O ANISOU 5050 O ILE B 390 5020 4188 4470 -194 94 -91 O ATOM 5051 CB ILE B 390 94.722 28.983 15.081 1.00 33.47 C ANISOU 5051 CB ILE B 390 4351 4121 4244 -128 96 -14 C ATOM 5052 CG1 ILE B 390 93.200 29.089 15.074 1.00 33.07 C ANISOU 5052 CG1 ILE B 390 4327 4018 4222 -10 213 -108 C ATOM 5053 CG2 ILE B 390 95.285 28.772 16.475 1.00 35.44 C ANISOU 5053 CG2 ILE B 390 4827 4259 4378 9 36 11 C ATOM 5054 CD1 ILE B 390 92.482 27.761 15.141 1.00 33.32 C ANISOU 5054 CD1 ILE B 390 4402 4011 4246 1 233 -1 C ATOM 5055 N LEU B 391 97.579 29.499 14.205 1.00 34.12 N ANISOU 5055 N LEU B 391 4409 4016 4537 -132 66 27 N ATOM 5056 CA LEU B 391 99.013 29.468 14.462 1.00 35.12 C ANISOU 5056 CA LEU B 391 4395 4320 4631 -81 40 -70 C ATOM 5057 C LEU B 391 99.654 30.815 14.129 1.00 37.14 C ANISOU 5057 C LEU B 391 4728 4440 4944 -198 39 -69 C ATOM 5058 O LEU B 391 100.624 31.184 14.835 1.00 38.70 O ANISOU 5058 O LEU B 391 4769 4680 5254 -174 -70 -79 O ATOM 5059 CB LEU B 391 99.670 28.349 13.650 1.00 34.91 C ANISOU 5059 CB LEU B 391 4461 4250 4553 -84 -13 -34 C ATOM 5060 CG LEU B 391 99.179 26.932 13.967 1.00 33.82 C ANISOU 5060 CG LEU B 391 4248 4249 4352 -59 50 -62 C ATOM 5061 CD1 LEU B 391 100.044 25.892 13.281 1.00 34.37 C ANISOU 5061 CD1 LEU B 391 4315 4312 4434 17 71 -84 C ATOM 5062 CD2 LEU B 391 99.151 26.715 15.473 1.00 34.54 C ANISOU 5062 CD2 LEU B 391 4399 4357 4368 -86 -46 -55 C TER 5063 LEU B 391 END