HEADER ISOMERASE 02-NOV-99 1DBF TITLE CHORISMATE MUTASE FROM BACILLUS SUBTILIS AT 1.30 ANGSTROM COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHORISMATE MUTASE; COMPND 3 CHAIN: A, B, C; COMPND 4 EC: 5.4.99.5; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 4 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: MZ1; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PRE1-AROQ KEYWDS CHORISMATE MUTASE, SHIKIMATE PATHWAY EXPDTA X-RAY DIFFRACTION AUTHOR G.L.GILLILAND,J.E.LADNER REVDAT 1 07-JUN-00 1DBF 0 JRNL AUTH J.E.LADNER,P.REDDY,A.DAVIS,M.TORDOVA,A.J.HOWARD, JRNL AUTH 2 G.L.GILLILAND JRNL TITL THE 1.30 A RESOLUTION STRUCTURE OF THE BACILLUS JRNL TITL 2 SUBTILIS CHORISMATE MUTASE CATALYTIC HOMOTRIMER JRNL REF ACTA CRYSTALLOGR., SECT.D V. 56 673 2000 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 59.1 REMARK 3 CROSS-VALIDATION METHOD : FREE R REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.169 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.167 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 902 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 89868 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.150 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.148 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 724 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 7248 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3159 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 75 REMARK 3 SOLVENT ATOMS : 424 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 3529.00 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 3 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 3296 REMARK 3 NUMBER OF RESTRAINTS : 4047 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.012 REMARK 3 ANGLE DISTANCES (A) : 0.031 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.027 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.065 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.072 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.016 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.060 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.083 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973) REMARK 3 201-228 REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE EFFECTIVE RESOLUTION IS REMARK 3 1.30 ANGSTROMS, HOWEVER, ALL DATA AVAILABLE WERE USED REMARK 3 DURING THE REFINEMENT. THIS INCLUDES SOME DATA AS HIGH AS REMARK 3 1.20 ANGSTROMS. REMARK 4 REMARK 4 1DBF COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-1999. REMARK 100 THE RCSB ID CODE IS RCSB009947. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-FEB-1998 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 3.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : IMCA REMARK 200 BEAMLINE : 17-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : 4-CCD REMARK 200 DETECTOR MANUFACTURER : BRUKER AXS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XGEN REMARK 200 DATA SCALING SOFTWARE : XGEN REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89868 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 78.0 REMARK 200 DATA REDUNDANCY : 2.100 REMARK 200 R MERGE (I) : 0.09200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.27 REMARK 200 COMPLETENESS FOR SHELL (%) : 23.0 REMARK 200 DATA REDUNDANCY IN SHELL : 1.50 REMARK 200 R MERGE FOR SHELL (I) : 0.45800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REMARK 200 REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: 2CHS REMARK 200 REMARK 200 REMARK: THE MODEL USED FOR MOLECULAR REPLACEMENT WAS ONE REMARK 200 TRIMER (ABC) FROM STRUCTURE 2CHS. THE WATERS ARE GROUPED. REMARK 200 WATERS 301-433 MAKE THEIR CLOSEST CONTACT WITH RESIDUES REMARK 200 IN CHAIN A, WATERS 434-567 WITH RESIDUES IN CHAIN B, REMARK 200 WATERS 568-709 WITH RESIDUES IN CHAIN C, WATERS 710-717 REMARK 200 WITH SO4 IONS AND WATERS 718- 724 WITH GLYCEROL REMARK 200 MOLECULES. THE CLOSEST PROTEIN CHAIN FOR WATER MOLECULES REMARK 200 710, 711, 713, 715, 717, 718, 720, 722, 723, 724 IS CHAIN REMARK 200 A. THE CLOSEST PROTEIN CHAIN FOR WATER MOLECULES 714 AND REMARK 200 719 IS CHAIN B. THE CLOSEST PROTEIN CHAIN FOR WATER REMARK 200 MOLECULES 712, 716 AND 721 IS CHAIN C. REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN DROP: 5 MICROLITERS REMARK 280 PROTEIN SOLUTION, 5 MICROLITERS RESERVOIR. PROTEIN REMARK 280 SOLUTION: 13 MG/ML PROTEIN, 100 MM PMSF, 100 MM NACL, 50 REMARK 280 MM TRIS PH 7.5, 1 MM EDTA, 1 MM DTT. RESERVOIR SOLUTION: REMARK 280 2.2 M AMMONIUM SULFATE, 100 MM SODIUM ACETATE PH 3.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-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 26.10000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.98000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.88500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.98000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.10000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.88500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 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 14 CD - NE - CZ ANGL. DEV. = 14.4 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 0 HOH 531 DISTANCE = 5.33 ANGSTROMS DBREF 1DBF A 1 127 SWS P19080 CHMU_BACSU 1 127 DBREF 1DBF B 1 127 SWS P19080 CHMU_BACSU 1 127 DBREF 1DBF C 1 127 SWS P19080 CHMU_BACSU 1 127 SEQRES 1 A 127 MET MET ILE ARG GLY ILE ARG GLY ALA THR THR VAL GLU SEQRES 2 A 127 ARG ASP THR GLU GLU GLU ILE LEU GLN LYS THR LYS GLN SEQRES 3 A 127 LEU LEU GLU LYS ILE ILE GLU GLU ASN HIS THR LYS PRO SEQRES 4 A 127 GLU ASP VAL VAL GLN MET LEU LEU SER ALA THR PRO ASP SEQRES 5 A 127 LEU HIS ALA VAL PHE PRO ALA LYS ALA VAL ARG GLU LEU SEQRES 6 A 127 SER GLY TRP GLN TYR VAL PRO VAL THR CYS MET GLN GLU SEQRES 7 A 127 MET ASP VAL THR GLY GLY LEU LYS LYS CYS ILE ARG VAL SEQRES 8 A 127 MET MET THR VAL GLN THR ASP VAL PRO GLN ASP GLN ILE SEQRES 9 A 127 ARG HIS VAL TYR LEU GLU LYS ALA VAL VAL LEU ARG PRO SEQRES 10 A 127 ASP LEU SER LEU THR LYS ASN THR GLU LEU SEQRES 1 B 127 MET MET ILE ARG GLY ILE ARG GLY ALA THR THR VAL GLU SEQRES 2 B 127 ARG ASP THR GLU GLU GLU ILE LEU GLN LYS THR LYS GLN SEQRES 3 B 127 LEU LEU GLU LYS ILE ILE GLU GLU ASN HIS THR LYS PRO SEQRES 4 B 127 GLU ASP VAL VAL GLN MET LEU LEU SER ALA THR PRO ASP SEQRES 5 B 127 LEU HIS ALA VAL PHE PRO ALA LYS ALA VAL ARG GLU LEU SEQRES 6 B 127 SER GLY TRP GLN TYR VAL PRO VAL THR CYS MET GLN GLU SEQRES 7 B 127 MET ASP VAL THR GLY GLY LEU LYS LYS CYS ILE ARG VAL SEQRES 8 B 127 MET MET THR VAL GLN THR ASP VAL PRO GLN ASP GLN ILE SEQRES 9 B 127 ARG HIS VAL TYR LEU GLU LYS ALA VAL VAL LEU ARG PRO SEQRES 10 B 127 ASP LEU SER LEU THR LYS ASN THR GLU LEU SEQRES 1 C 127 MET MET ILE ARG GLY ILE ARG GLY ALA THR THR VAL GLU SEQRES 2 C 127 ARG ASP THR GLU GLU GLU ILE LEU GLN LYS THR LYS GLN SEQRES 3 C 127 LEU LEU GLU LYS ILE ILE GLU GLU ASN HIS THR LYS PRO SEQRES 4 C 127 GLU ASP VAL VAL GLN MET LEU LEU SER ALA THR PRO ASP SEQRES 5 C 127 LEU HIS ALA VAL PHE PRO ALA LYS ALA VAL ARG GLU LEU SEQRES 6 C 127 SER GLY TRP GLN TYR VAL PRO VAL THR CYS MET GLN GLU SEQRES 7 C 127 MET ASP VAL THR GLY GLY LEU LYS LYS CYS ILE ARG VAL SEQRES 8 C 127 MET MET THR VAL GLN THR ASP VAL PRO GLN ASP GLN ILE SEQRES 9 C 127 ARG HIS VAL TYR LEU GLU LYS ALA VAL VAL LEU ARG PRO SEQRES 10 C 127 ASP LEU SER LEU THR LYS ASN THR GLU LEU HET SO4 201 5 HET SO4 202 5 HET SO4 203 5 HET SO4 204 5 HET SO4 205 5 HET SO4 206 5 HET SO4 207 5 HET SO4 208 5 HET SO4 209 5 HET GOL 251 6 HET GOL 252 6 HET GOL 253 6 HET GOL 254 6 HET GOL 255 6 HETNAM SO4 SULFATE ION HETNAM GOL GLYCEROL FORMUL 4 SO4 9(O4 S1 2-) FORMUL 13 GOL 5(C3 H8 O3) FORMUL 18 HOH *424(H2 O1) HELIX 1 1 THR A 16 HIS A 36 1 21 HELIX 2 2 LYS A 38 GLU A 40 5 3 HELIX 3 3 PRO A 58 GLU A 64 1 7 HELIX 4 4 PRO A 100 ILE A 104 5 5 HELIX 5 5 GLU A 110 ARG A 116 5 7 HELIX 6 6 SER A 120 THR A 125 1 6 HELIX 7 7 THR B 16 HIS B 36 1 21 HELIX 8 8 LYS B 38 GLU B 40 5 3 HELIX 9 9 PRO B 58 LEU B 65 1 8 HELIX 10 10 PRO B 100 ILE B 104 5 5 HELIX 11 11 GLU B 110 ARG B 116 5 7 HELIX 12 12 THR C 16 HIS C 36 1 21 HELIX 13 13 LYS C 38 GLU C 40 5 3 HELIX 14 14 PRO C 58 LEU C 65 1 8 HELIX 15 15 PRO C 100 ILE C 104 5 5 HELIX 16 16 GLU C 110 ARG C 116 5 7 HELIX 17 17 LEU C 121 GLU C 126 5 6 SHEET 1 A 5 VAL A 73 GLN A 77 0 SHEET 2 A 5 VAL A 42 ALA A 49 1 O MET A 45 N THR A 74 SHEET 3 A 5 CYS A 88 THR A 97 -1 O ARG A 90 N SER A 48 SHEET 4 A 5 MET A 2 THR A 11 -1 O MET A 2 N THR A 97 SHEET 5 A 5 VAL A 107 TYR A 108 1 N VAL A 107 O ARG A 7 SHEET 1 B 5 VAL B 73 GLN B 77 0 SHEET 2 B 5 VAL B 42 ALA B 49 1 O MET B 45 N THR B 74 SHEET 3 B 5 CYS B 88 GLN B 96 -1 O ARG B 90 N SER B 48 SHEET 4 B 5 ILE B 3 THR B 11 -1 O ARG B 4 N VAL B 95 SHEET 5 B 5 VAL B 107 TYR B 108 1 N VAL B 107 O ARG B 7 SHEET 1 C 5 VAL C 73 GLN C 77 0 SHEET 2 C 5 VAL C 42 ALA C 49 1 O MET C 45 N THR C 74 SHEET 3 C 5 CYS C 88 GLN C 96 -1 O ARG C 90 N SER C 48 SHEET 4 C 5 ILE C 3 THR C 11 -1 O ARG C 4 N VAL C 95 SHEET 5 C 5 VAL C 107 TYR C 108 1 N VAL C 107 O ARG C 7 CRYST1 52.200 83.770 85.960 90.00 90.00 90.00 P 21 21 21 12 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 0.019160 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011940 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011630 0.00000 ATOM 1 N MET A 1 26.788 37.634 37.033 1.00 44.16 N ANISOU 1 N MET A 1 8223 6427 2126 -1394 -2442 -927 N ATOM 2 CA MET A 1 26.472 37.459 35.614 1.00 36.55 C ANISOU 2 CA MET A 1 5592 6404 1890 -1905 -1832 -691 C ATOM 3 C MET A 1 25.457 36.353 35.371 1.00 35.29 C ANISOU 3 C MET A 1 5711 5908 1791 -1913 -1416 -78 C ATOM 4 O MET A 1 25.203 35.446 36.170 1.00 41.01 O ANISOU 4 O MET A 1 5976 6890 2716 -1667 -1912 1113 O ATOM 5 CB MET A 1 27.803 37.215 34.877 1.00 38.98 C ANISOU 5 CB MET A 1 5157 6745 2908 -1591 -1876 46 C ATOM 6 CG MET A 1 27.679 37.394 33.373 1.00 28.09 C ANISOU 6 CG MET A 1 4217 3850 2606 -1919 -1550 -996 C ATOM 7 SD MET A 1 27.624 39.148 32.867 1.00 30.34 S ANISOU 7 SD MET A 1 3565 3871 4091 152 -1574 -900 S ATOM 8 CE MET A 1 29.160 39.704 33.611 1.00 60.12 C ANISOU 8 CE MET A 1 4019 3757 15069 -1943 -3633 731 C ATOM 9 N MET A 2 24.808 36.370 34.217 1.00 29.14 N ANISOU 9 N MET A 2 4559 5255 1257 -2581 -624 -106 N ATOM 10 CA MET A 2 23.721 35.457 33.836 1.00 19.71 C ANISOU 10 CA MET A 2 4744 2369 377 -1772 458 -580 C ATOM 11 C MET A 2 23.469 35.662 32.352 1.00 13.83 C ANISOU 11 C MET A 2 2395 1914 944 -5 -348 37 C ATOM 12 O MET A 2 24.071 36.541 31.731 1.00 15.26 O ANISOU 12 O MET A 2 3023 2109 666 -459 -738 132 O ATOM 13 CB MET A 2 22.502 35.780 34.655 1.00 18.79 C ANISOU 13 CB MET A 2 4116 2346 677 -1116 -230 -494 C ATOM 14 CG MET A 2 21.195 35.133 34.396 1.00 24.10 C ANISOU 14 CG MET A 2 4278 2545 2333 -1405 -160 -650 C ATOM 15 SD MET A 2 21.062 33.325 34.295 1.00 18.84 S ANISOU 15 SD MET A 2 3348 2370 1442 -1090 -354 385 S ATOM 16 CE MET A 2 19.250 33.323 34.183 1.00 21.51 C ANISOU 16 CE MET A 2 3302 2915 1956 -1145 -253 103 C ATOM 17 N ILE A 3 22.618 34.776 31.789 1.00 11.48 N ANISOU 17 N ILE A 3 1956 1605 801 257 -80 49 N ATOM 18 CA ILE A 3 22.225 34.914 30.410 1.00 10.32 C ANISOU 18 CA ILE A 3 1688 1286 945 461 -278 -11 C ATOM 19 C ILE A 3 20.777 35.372 30.392 1.00 9.79 C ANISOU 19 C ILE A 3 1502 983 1236 140 17 63 C ATOM 20 O ILE A 3 19.981 34.836 31.198 1.00 13.33 O ANISOU 20 O ILE A 3 2054 1296 1714 -279 339 117 O ATOM 21 CB ILE A 3 22.334 33.546 29.717 1.00 12.73 C ANISOU 21 CB ILE A 3 1836 1655 1346 572 -45 -411 C ATOM 22 CG1 ILE A 3 23.706 32.890 29.931 1.00 13.61 C ANISOU 22 CG1 ILE A 3 1233 1320 2619 44 320 -604 C ATOM 23 CG2 ILE A 3 22.001 33.681 28.258 1.00 14.27 C ANISOU 23 CG2 ILE A 3 2220 2032 1171 -755 177 -378 C ATOM 24 CD1 ILE A 3 24.865 33.741 29.442 1.00 12.42 C ANISOU 24 CD1 ILE A 3 1993 907 1818 -452 -11 -598 C ATOM 25 N ARG A 4 20.414 36.330 29.539 1.00 9.65 N ANISOU 25 N ARG A 4 1410 1247 1010 242 -311 -10 N ATOM 26 CA ARG A 4 19.040 36.832 29.544 1.00 9.01 C ANISOU 26 CA ARG A 4 1400 1224 801 213 55 -89 C ATOM 27 C ARG A 4 18.582 37.071 28.109 1.00 6.93 C ANISOU 27 C ARG A 4 1044 878 710 294 190 -208 C ATOM 28 O ARG A 4 19.380 37.506 27.262 1.00 10.83 O ANISOU 28 O ARG A 4 1702 1633 778 -408 394 -271 O ATOM 29 CB ARG A 4 18.988 38.200 30.209 1.00 11.39 C ANISOU 29 CB ARG A 4 2203 1537 588 467 -119 -354 C ATOM 30 CG ARG A 4 19.505 38.373 31.618 1.00 13.62 C ANISOU 30 CG ARG A 4 1888 2805 483 1077 -15 -570 C ATOM 31 CD ARG A 4 18.373 38.017 32.587 1.00 15.54 C ANISOU 31 CD ARG A 4 2792 2471 643 -297 -52 -229 C ATOM 32 NE ARG A 4 18.826 37.853 33.960 1.00 15.23 N ANISOU 32 NE ARG A 4 2354 2626 809 127 -18 181 N ATOM 33 CZ ARG A 4 18.128 37.041 34.764 1.00 12.43 C ANISOU 33 CZ ARG A 4 2868 1161 694 93 56 -480 C ATOM 34 NH1 ARG A 4 17.051 36.449 34.342 1.00 16.59 N ANISOU 34 NH1 ARG A 4 3185 1298 1820 -138 -666 88 N ATOM 35 NH2 ARG A 4 18.565 36.901 35.994 1.00 16.49 N ANISOU 35 NH2 ARG A 4 2949 2213 1103 -76 -311 438 N ATOM 36 N GLY A 5 17.278 36.825 27.892 1.00 8.52 N ANISOU 36 N GLY A 5 1263 683 1291 -32 -156 14 N ATOM 37 CA GLY A 5 16.685 37.232 26.653 1.00 7.98 C ANISOU 37 CA GLY A 5 1398 563 1070 -229 -156 -39 C ATOM 38 C GLY A 5 16.289 38.710 26.617 1.00 7.19 C ANISOU 38 C GLY A 5 1304 726 702 63 62 -79 C ATOM 39 O GLY A 5 15.833 39.274 27.596 1.00 9.73 O ANISOU 39 O GLY A 5 1608 1077 1013 100 406 -157 O ATOM 40 N ILE A 6 16.489 39.320 25.440 1.00 7.37 N ANISOU 40 N ILE A 6 1039 929 832 278 -47 178 N ATOM 41 CA ILE A 6 15.965 40.649 25.160 1.00 7.10 C ANISOU 41 CA ILE A 6 1070 710 918 -36 -340 -63 C ATOM 42 C ILE A 6 14.999 40.495 23.994 1.00 5.77 C ANISOU 42 C ILE A 6 999 368 824 195 -278 -447 C ATOM 43 O ILE A 6 15.331 39.977 22.917 1.00 8.75 O ANISOU 43 O ILE A 6 1160 1383 782 -106 263 -373 O ATOM 44 CB ILE A 6 17.104 41.632 24.822 1.00 9.18 C ANISOU 44 CB ILE A 6 1216 756 1515 -201 -381 -260 C ATOM 45 CG1 ILE A 6 18.313 41.540 25.803 1.00 9.36 C ANISOU 45 CG1 ILE A 6 1042 999 1515 -145 -301 -514 C ATOM 46 CG2 ILE A 6 16.567 43.052 24.695 1.00 8.86 C ANISOU 46 CG2 ILE A 6 1441 778 1147 -17 -34 -137 C ATOM 47 CD1 ILE A 6 19.364 42.609 25.548 1.00 16.33 C ANISOU 47 CD1 ILE A 6 1084 1663 3456 -401 -751 504 C ATOM 48 N ARG A 7 13.796 41.028 24.217 1.00 7.12 N ANISOU 48 N ARG A 7 1040 456 1207 310 -123 -123 N ATOM 49 CA ARG A 7 12.740 40.996 23.206 1.00 8.21 C ANISOU 49 CA ARG A 7 883 733 1502 -351 -203 509 C ATOM 50 C ARG A 7 12.653 42.354 22.512 1.00 8.31 C ANISOU 50 C ARG A 7 1489 574 1094 -346 -264 217 C ATOM 51 O ARG A 7 12.872 43.437 23.080 1.00 10.98 O ANISOU 51 O ARG A 7 1637 613 1921 -84 -106 -196 O ATOM 52 CB ARG A 7 11.386 40.684 23.821 1.00 8.66 C ANISOU 52 CB ARG A 7 1165 1127 1000 -298 -4 252 C ATOM 53 CG ARG A 7 11.145 39.204 24.071 1.00 10.43 C ANISOU 53 CG ARG A 7 1326 1122 1516 -763 627 -128 C ATOM 54 CD ARG A 7 11.032 38.296 22.838 1.00 11.29 C ANISOU 54 CD ARG A 7 1425 1226 1639 242 -262 -229 C ATOM 55 NE ARG A 7 10.427 39.072 21.767 1.00 10.02 N ANISOU 55 NE ARG A 7 1359 672 1775 363 137 -94 N ATOM 56 CZ ARG A 7 9.125 39.464 21.780 1.00 10.87 C ANISOU 56 CZ ARG A 7 1258 1408 1463 378 119 8 C ATOM 57 NH1 ARG A 7 8.285 39.091 22.748 1.00 9.96 N ANISOU 57 NH1 ARG A 7 1235 842 1709 -104 50 -126 N ATOM 58 NH2 ARG A 7 8.695 40.232 20.773 1.00 10.05 N ANISOU 58 NH2 ARG A 7 1236 1420 1164 178 -205 -313 N ATOM 59 N GLY A 8 12.313 42.275 21.192 1.00 10.62 N ANISOU 59 N GLY A 8 1521 1432 1081 449 -357 173 N ATOM 60 CA GLY A 8 11.988 43.476 20.425 1.00 11.03 C ANISOU 60 CA GLY A 8 1884 1100 1208 584 -696 -158 C ATOM 61 C GLY A 8 10.894 43.114 19.437 1.00 9.08 C ANISOU 61 C GLY A 8 1557 868 1024 123 -360 313 C ATOM 62 O GLY A 8 10.643 41.925 19.162 1.00 9.88 O ANISOU 62 O GLY A 8 1492 902 1362 173 -113 -65 O ATOM 63 N ALA A 9 10.200 44.114 18.942 1.00 8.75 N ANISOU 63 N ALA A 9 1257 998 1071 324 -248 94 N ATOM 64 CA ALA A 9 9.319 43.941 17.825 1.00 9.67 C ANISOU 64 CA ALA A 9 1505 772 1399 3 -562 397 C ATOM 65 C ALA A 9 9.226 45.301 17.109 1.00 8.99 C ANISOU 65 C ALA A 9 1213 585 1619 -16 -579 312 C ATOM 66 O ALA A 9 9.359 46.389 17.684 1.00 12.65 O ANISOU 66 O ALA A 9 1704 808 2296 -355 0 -42 O ATOM 67 CB ALA A 9 7.931 43.521 18.302 1.00 12.92 C ANISOU 67 CB ALA A 9 1788 1121 2002 -614 -712 536 C ATOM 68 N THR A 10 8.939 45.184 15.797 1.00 9.93 N ANISOU 68 N THR A 10 1136 1230 1405 286 -296 474 N ATOM 69 CA THR A 10 8.679 46.358 14.947 1.00 10.80 C ANISOU 69 CA THR A 10 1812 961 1329 202 -266 260 C ATOM 70 C THR A 10 7.737 45.909 13.845 1.00 12.11 C ANISOU 70 C THR A 10 2388 979 1237 -118 -475 672 C ATOM 71 O THR A 10 7.330 44.731 13.772 1.00 11.03 O ANISOU 71 O THR A 10 2034 980 1175 -128 -61 427 O ATOM 72 CB THR A 10 10.019 46.939 14.470 1.00 13.07 C ANISOU 72 CB THR A 10 2215 573 2180 -75 123 19 C ATOM 73 OG1 THR A 10 9.782 48.191 13.804 1.00 15.40 O ANISOU 73 OG1 THR A 10 2243 1024 2583 -139 -241 433 O ATOM 74 CG2 THR A 10 10.739 45.994 13.517 1.00 12.66 C ANISOU 74 CG2 THR A 10 1827 1527 1456 120 -160 -16 C ATOM 75 N THR A 11 7.318 46.847 12.995 1.00 12.70 N ANISOU 75 N THR A 11 2201 1144 1483 660 -322 567 N ATOM 76 CA THR A 11 6.525 46.553 11.834 1.00 12.29 C ANISOU 76 CA THR A 11 1582 1631 1455 331 -189 704 C ATOM 77 C THR A 11 7.041 47.317 10.610 1.00 10.47 C ANISOU 77 C THR A 11 1550 1102 1324 379 -85 327 C ATOM 78 O THR A 11 7.760 48.308 10.726 1.00 12.73 O ANISOU 78 O THR A 11 2376 1121 1342 94 -51 301 O ATOM 79 CB THR A 11 5.048 46.957 12.018 1.00 12.24 C ANISOU 79 CB THR A 11 1852 1334 1465 626 152 604 C ATOM 80 OG1 THR A 11 4.877 48.365 12.295 1.00 15.86 O ANISOU 80 OG1 THR A 11 2457 1356 2213 532 -187 313 O ATOM 81 CG2 THR A 11 4.403 46.181 13.191 1.00 11.29 C ANISOU 81 CG2 THR A 11 2017 1653 618 793 121 302 C ATOM 82 N VAL A 12 6.629 46.895 9.424 1.00 12.57 N ANISOU 82 N VAL A 12 2028 1379 1368 148 -208 338 N ATOM 83 CA VAL A 12 6.864 47.602 8.180 1.00 15.37 C ANISOU 83 CA VAL A 12 2039 2436 1364 471 42 642 C ATOM 84 C VAL A 12 5.531 47.883 7.517 1.00 14.53 C ANISOU 84 C VAL A 12 2099 1700 1722 131 -181 820 C ATOM 85 O VAL A 12 4.508 47.214 7.786 1.00 17.08 O ANISOU 85 O VAL A 12 2564 2040 1885 -422 -650 1297 O ATOM 86 CB VAL A 12 7.748 46.789 7.228 1.00 15.18 C ANISOU 86 CB VAL A 12 1973 2301 1494 4 -189 -32 C ATOM 87 CG1 VAL A 12 9.151 46.612 7.802 1.00 15.88 C ANISOU 87 CG1 VAL A 12 2143 1827 2063 608 -352 482 C ATOM 88 CG2 VAL A 12 7.118 45.420 6.942 1.00 15.62 C ANISOU 88 CG2 VAL A 12 3043 2008 884 -378 -233 939 C ATOM 89 N GLU A 13 5.581 48.857 6.612 1.00 17.13 N ANISOU 89 N GLU A 13 1886 2051 2570 -6 -129 1380 N ATOM 90 CA GLU A 13 4.330 49.226 5.945 1.00 19.08 C ANISOU 90 CA GLU A 13 2653 2243 2356 780 -559 756 C ATOM 91 C GLU A 13 4.064 48.352 4.731 1.00 18.90 C ANISOU 91 C GLU A 13 2607 2082 2492 287 -179 660 C ATOM 92 O GLU A 13 2.960 48.177 4.257 1.00 19.47 O ANISOU 92 O GLU A 13 2557 2424 2418 101 71 411 O ATOM 93 CB GLU A 13 4.414 50.676 5.430 1.00 20.05 C ANISOU 93 CB GLU A 13 3539 2009 2070 1029 -458 443 C ATOM 94 CG GLU A 13 4.435 51.704 6.539 1.00 25.53 C ANISOU 94 CG GLU A 13 4344 2612 2743 1661 239 -222 C ATOM 95 CD GLU A 13 3.110 51.759 7.286 1.00 27.84 C ANISOU 95 CD GLU A 13 4323 4055 2198 1836 78 632 C ATOM 96 OE1 GLU A 13 2.173 52.385 6.767 1.00 39.13 O ANISOU 96 OE1 GLU A 13 4404 4992 5472 2223 1071 3463 O ATOM 97 OE2 GLU A 13 2.978 51.197 8.394 1.00 32.10 O ANISOU 97 OE2 GLU A 13 5743 4751 1702 2220 173 360 O ATOM 98 N ARG A 14 5.188 47.839 4.217 1.00 19.18 N ANISOU 98 N ARG A 14 2684 2395 2209 458 -137 923 N ATOM 99 CA ARG A 14 5.178 47.071 2.998 1.00 20.61 C ANISOU 99 CA ARG A 14 3376 2725 1730 850 35 1235 C ATOM 100 C ARG A 14 6.170 45.914 3.093 1.00 17.42 C ANISOU 100 C ARG A 14 2556 2721 1341 507 232 1187 C ATOM 101 O ARG A 14 7.186 46.064 3.743 1.00 20.20 O ANISOU 101 O ARG A 14 3200 3104 1371 785 -228 581 O ATOM 102 CB AARG A 14 5.548 47.904 1.762 0.55 23.32 C ANISOU 102 CB AARG A 14 3629 2828 2403 885 470 1605 C ATOM 103 CB BARG A 14 5.534 47.924 1.775 0.45 23.29 C ANISOU 103 CB BARG A 14 3708 2715 2425 886 535 1552 C ATOM 104 CG AARG A 14 4.867 49.251 1.575 0.55 22.92 C ANISOU 104 CG AARG A 14 3597 2460 2651 505 153 1457 C ATOM 105 CG BARG A 14 4.332 48.614 1.140 0.45 24.85 C ANISOU 105 CG BARG A 14 3919 3101 2422 574 189 2080 C ATOM 106 CD AARG A 14 5.251 49.880 0.234 0.55 22.86 C ANISOU 106 CD AARG A 14 3823 2181 2684 108 85 1379 C ATOM 107 CD BARG A 14 4.401 48.451 -0.376 0.45 27.25 C ANISOU 107 CD BARG A 14 4391 3496 2467 281 288 1900 C ATOM 108 NE AARG A 14 6.547 50.550 0.286 0.55 23.67 N ANISOU 108 NE AARG A 14 3632 2925 2436 131 383 834 N ATOM 109 NE BARG A 14 5.720 48.846 -0.889 0.45 25.69 N ANISOU 109 NE BARG A 14 4514 2707 2539 249 592 1188 N ATOM 110 CZ AARG A 14 7.298 50.989 -0.702 0.55 22.58 C ANISOU 110 CZ AARG A 14 3401 2604 2575 423 207 1246 C ATOM 111 CZ BARG A 14 6.476 48.000 -1.579 0.45 26.60 C ANISOU 111 CZ BARG A 14 5040 2701 2367 389 594 1155 C ATOM 112 NH1AARG A 14 6.909 50.852 -1.961 0.55 26.19 N ANISOU 112 NH1AARG A 14 3714 3800 2439 -388 637 590 N ATOM 113 NH1BARG A 14 6.025 46.776 -1.809 0.45 28.04 N ANISOU 113 NH1BARG A 14 4685 3066 2902 367 -295 568 N ATOM 114 NH2AARG A 14 8.461 51.577 -0.438 0.55 28.51 N ANISOU 114 NH2AARG A 14 4477 4029 2326 -990 1136 -677 N ATOM 115 NH2BARG A 14 7.662 48.365 -2.033 0.45 26.74 N ANISOU 115 NH2BARG A 14 5567 2776 1816 349 1198 948 N ATOM 116 N ASP A 15 5.851 44.817 2.421 1.00 21.09 N ANISOU 116 N ASP A 15 2870 3320 1822 1192 -655 442 N ATOM 117 CA ASP A 15 6.715 43.652 2.359 1.00 20.04 C ANISOU 117 CA ASP A 15 2389 2940 2287 768 -391 765 C ATOM 118 C ASP A 15 7.774 43.875 1.296 1.00 16.02 C ANISOU 118 C ASP A 15 2346 2473 1268 583 -929 390 C ATOM 119 O ASP A 15 7.739 43.388 0.157 1.00 26.57 O ANISOU 119 O ASP A 15 5548 3182 1367 -1510 -516 220 O ATOM 120 CB ASP A 15 5.904 42.391 2.045 1.00 21.36 C ANISOU 120 CB ASP A 15 2764 3290 2061 372 -126 546 C ATOM 121 CG ASP A 15 6.772 41.144 1.980 1.00 16.88 C ANISOU 121 CG ASP A 15 2181 3338 892 196 -393 -341 C ATOM 122 OD1 ASP A 15 7.853 41.134 2.601 1.00 18.79 O ANISOU 122 OD1 ASP A 15 2146 3333 1660 -478 -668 736 O ATOM 123 OD2 ASP A 15 6.378 40.137 1.345 1.00 21.12 O ANISOU 123 OD2 ASP A 15 3831 3319 876 -243 -1120 79 O ATOM 124 N THR A 16 8.763 44.666 1.606 1.00 16.21 N ANISOU 124 N THR A 16 2672 2050 1437 428 -640 293 N ATOM 125 CA THR A 16 9.875 45.012 0.765 1.00 18.33 C ANISOU 125 CA THR A 16 2875 2543 1548 318 -509 361 C ATOM 126 C THR A 16 11.186 44.782 1.488 1.00 14.82 C ANISOU 126 C THR A 16 2747 2070 812 -331 -122 1090 C ATOM 127 O THR A 16 11.245 44.920 2.693 1.00 17.05 O ANISOU 127 O THR A 16 3012 2579 889 -350 -152 946 O ATOM 128 CB THR A 16 9.635 46.499 0.407 1.00 22.66 C ANISOU 128 CB THR A 16 3790 2841 1977 222 -741 1229 C ATOM 129 OG1 THR A 16 9.888 46.579 -0.978 1.00 34.88 O ANISOU 129 OG1 THR A 16 7548 3436 2267 -1447 349 1077 O ATOM 130 CG2 THR A 16 10.538 47.421 1.162 1.00 16.49 C ANISOU 130 CG2 THR A 16 2102 2153 2009 48 -156 2208 C ATOM 131 N GLU A 17 12.223 44.430 0.730 1.00 15.68 N ANISOU 131 N GLU A 17 2752 1791 1415 -99 -146 441 N ATOM 132 CA GLU A 17 13.479 44.189 1.410 1.00 18.00 C ANISOU 132 CA GLU A 17 2890 2412 1538 -21 -322 326 C ATOM 133 C GLU A 17 13.989 45.437 2.128 1.00 15.66 C ANISOU 133 C GLU A 17 2750 2357 844 -233 7 583 C ATOM 134 O GLU A 17 14.431 45.331 3.288 1.00 17.29 O ANISOU 134 O GLU A 17 3650 1940 981 145 -260 629 O ATOM 135 CB GLU A 17 14.554 43.696 0.424 1.00 16.41 C ANISOU 135 CB GLU A 17 2798 2125 1311 88 -541 403 C ATOM 136 CG GLU A 17 15.908 43.570 1.152 1.00 16.26 C ANISOU 136 CG GLU A 17 2672 2266 1240 -336 -475 703 C ATOM 137 CD GLU A 17 16.996 43.149 0.191 1.00 16.85 C ANISOU 137 CD GLU A 17 2607 2711 1083 -357 -479 782 C ATOM 138 OE1 GLU A 17 16.989 43.669 -0.959 1.00 21.21 O ANISOU 138 OE1 GLU A 17 3999 3050 1009 -161 -372 752 O ATOM 139 OE2 GLU A 17 17.851 42.297 0.510 1.00 16.94 O ANISOU 139 OE2 GLU A 17 2869 2408 1161 -245 -636 269 O ATOM 140 N GLU A 18 13.958 46.585 1.458 1.00 16.42 N ANISOU 140 N GLU A 18 2650 2324 1264 311 -291 710 N ATOM 141 CA GLU A 18 14.552 47.768 2.087 1.00 18.57 C ANISOU 141 CA GLU A 18 3337 2553 1167 -688 374 952 C ATOM 142 C GLU A 18 13.809 48.058 3.373 1.00 16.62 C ANISOU 142 C GLU A 18 2880 2276 1160 594 -138 798 C ATOM 143 O GLU A 18 14.471 48.459 4.346 1.00 18.74 O ANISOU 143 O GLU A 18 3619 2078 1424 791 -589 566 O ATOM 144 CB GLU A 18 14.628 48.975 1.142 1.00 25.36 C ANISOU 144 CB GLU A 18 4557 2742 2339 -133 662 1571 C ATOM 145 CG GLU A 18 13.503 49.935 1.047 1.00 36.88 C ANISOU 145 CG GLU A 18 6503 2854 4653 1023 -292 776 C ATOM 146 CD GLU A 18 13.361 51.029 2.089 1.00 37.25 C ANISOU 146 CD GLU A 18 6264 1861 6028 352 -1431 370 C ATOM 147 OE1 GLU A 18 14.364 51.386 2.748 1.00 40.55 O ANISOU 147 OE1 GLU A 18 6784 5524 3097 -1218 -1003 2087 O ATOM 148 OE2 GLU A 18 12.201 51.465 2.260 1.00 46.36 O ANISOU 148 OE2 GLU A 18 6136 3802 7676 -336 -33 -2058 O ATOM 149 N GLU A 19 12.471 47.918 3.419 1.00 16.63 N ANISOU 149 N GLU A 19 3046 1601 1671 254 191 796 N ATOM 150 CA GLU A 19 11.792 48.241 4.684 1.00 14.50 C ANISOU 150 CA GLU A 19 2597 1183 1731 83 -85 288 C ATOM 151 C GLU A 19 12.077 47.234 5.782 1.00 13.23 C ANISOU 151 C GLU A 19 2168 1417 1441 367 379 283 C ATOM 152 O GLU A 19 12.256 47.570 6.961 1.00 15.42 O ANISOU 152 O GLU A 19 2511 1729 1619 365 49 140 O ATOM 153 CB GLU A 19 10.263 48.304 4.508 1.00 17.33 C ANISOU 153 CB GLU A 19 2532 1687 2365 107 -109 841 C ATOM 154 CG GLU A 19 9.860 49.567 3.787 1.00 26.57 C ANISOU 154 CG GLU A 19 3148 3183 3763 462 -34 2423 C ATOM 155 CD GLU A 19 8.414 49.970 3.808 1.00 30.98 C ANISOU 155 CD GLU A 19 3671 3918 4182 1492 20 2039 C ATOM 156 OE1 GLU A 19 7.582 49.548 4.651 1.00 35.65 O ANISOU 156 OE1 GLU A 19 3878 2901 6767 1758 1460 1979 O ATOM 157 OE2 GLU A 19 8.069 50.778 2.919 1.00 41.63 O ANISOU 157 OE2 GLU A 19 4299 5246 6273 680 -1632 3459 O ATOM 158 N ILE A 20 12.083 45.961 5.436 1.00 13.44 N ANISOU 158 N ILE A 20 2397 1397 1314 475 -253 429 N ATOM 159 CA ILE A 20 12.370 44.949 6.458 1.00 13.61 C ANISOU 159 CA ILE A 20 2355 1592 1225 472 -320 462 C ATOM 160 C ILE A 20 13.798 45.081 6.976 1.00 12.86 C ANISOU 160 C ILE A 20 2297 1158 1433 343 -219 649 C ATOM 161 O ILE A 20 13.983 45.030 8.208 1.00 12.59 O ANISOU 161 O ILE A 20 2115 1277 1391 -519 -241 710 O ATOM 162 CB ILE A 20 12.176 43.528 5.933 1.00 13.33 C ANISOU 162 CB ILE A 20 2126 1461 1476 31 51 754 C ATOM 163 CG1 ILE A 20 10.710 43.262 5.562 1.00 15.82 C ANISOU 163 CG1 ILE A 20 2269 2045 1698 528 -412 -22 C ATOM 164 CG2 ILE A 20 12.786 42.522 6.914 1.00 14.41 C ANISOU 164 CG2 ILE A 20 2348 1609 1517 176 -221 728 C ATOM 165 CD1 ILE A 20 10.454 42.071 4.681 1.00 15.02 C ANISOU 165 CD1 ILE A 20 2743 1125 1840 34 -319 637 C ATOM 166 N LEU A 21 14.798 45.268 6.122 1.00 12.81 N ANISOU 166 N LEU A 21 2494 1181 1193 192 -150 178 N ATOM 167 CA LEU A 21 16.127 45.494 6.700 1.00 14.03 C ANISOU 167 CA LEU A 21 2309 1665 1356 319 61 -167 C ATOM 168 C LEU A 21 16.261 46.799 7.473 1.00 12.35 C ANISOU 168 C LEU A 21 2066 1344 1281 399 -215 157 C ATOM 169 O LEU A 21 16.911 46.864 8.521 1.00 13.92 O ANISOU 169 O LEU A 21 2420 1445 1423 48 -440 238 O ATOM 170 CB LEU A 21 17.172 45.547 5.567 1.00 14.41 C ANISOU 170 CB LEU A 21 2638 1432 1403 310 264 226 C ATOM 171 CG LEU A 21 17.208 44.196 4.809 1.00 16.39 C ANISOU 171 CG LEU A 21 3334 1356 1536 694 720 325 C ATOM 172 CD1 LEU A 21 18.306 44.219 3.768 1.00 17.61 C ANISOU 172 CD1 LEU A 21 2798 3019 874 697 119 78 C ATOM 173 CD2 LEU A 21 17.334 43.048 5.816 1.00 17.15 C ANISOU 173 CD2 LEU A 21 3117 1564 1833 1188 436 494 C ATOM 174 N GLN A 22 15.663 47.882 6.979 1.00 13.85 N ANISOU 174 N GLN A 22 2006 1629 1627 673 194 496 N ATOM 175 CA GLN A 22 15.776 49.171 7.636 1.00 14.36 C ANISOU 175 CA GLN A 22 2150 1219 2087 149 373 748 C ATOM 176 C GLN A 22 15.117 49.096 9.010 1.00 12.15 C ANISOU 176 C GLN A 22 1480 1234 1902 452 73 334 C ATOM 177 O GLN A 22 15.780 49.530 9.969 1.00 16.46 O ANISOU 177 O GLN A 22 2046 2088 2118 -68 -331 602 O ATOM 178 CB GLN A 22 15.127 50.279 6.812 1.00 16.32 C ANISOU 178 CB GLN A 22 2907 1352 1944 172 -388 427 C ATOM 179 CG GLN A 22 15.120 51.637 7.532 1.00 20.13 C ANISOU 179 CG GLN A 22 3809 1287 2552 607 -258 376 C ATOM 180 CD GLN A 22 14.304 52.635 6.732 1.00 26.38 C ANISOU 180 CD GLN A 22 4759 1850 3414 1099 225 1326 C ATOM 181 OE1 GLN A 22 13.175 52.927 7.072 1.00 40.53 O ANISOU 181 OE1 GLN A 22 4413 4514 6474 2007 -210 1863 O ATOM 182 NE2 GLN A 22 14.894 53.154 5.661 1.00 49.81 N ANISOU 182 NE2 GLN A 22 7677 5154 6093 145 1008 4402 N ATOM 183 N LYS A 23 13.881 48.560 9.070 1.00 12.94 N ANISOU 183 N LYS A 23 1806 1117 1992 112 413 -138 N ATOM 184 CA LYS A 23 13.241 48.493 10.393 1.00 13.47 C ANISOU 184 CA LYS A 23 1690 1538 1890 104 202 110 C ATOM 185 C LYS A 23 13.914 47.460 11.279 1.00 13.04 C ANISOU 185 C LYS A 23 1640 1381 1935 -202 -456 -141 C ATOM 186 O LYS A 23 13.983 47.647 12.528 1.00 14.32 O ANISOU 186 O LYS A 23 2376 1155 1911 138 -16 -96 O ATOM 187 CB ALYS A 23 11.743 48.234 10.282 0.71 14.56 C ANISOU 187 CB ALYS A 23 1489 1670 2374 593 302 377 C ATOM 188 CB BLYS A 23 11.773 48.084 10.269 0.29 13.70 C ANISOU 188 CB BLYS A 23 1413 1363 2429 581 277 316 C ATOM 189 CG ALYS A 23 11.001 49.453 9.706 0.71 18.02 C ANISOU 189 CG ALYS A 23 2397 1300 3151 879 57 58 C ATOM 190 CG BLYS A 23 10.956 48.993 9.362 0.29 16.56 C ANISOU 190 CG BLYS A 23 2171 1524 2596 516 -217 400 C ATOM 191 CD ALYS A 23 11.414 50.754 10.368 0.71 23.03 C ANISOU 191 CD ALYS A 23 3750 1446 3556 -87 43 306 C ATOM 192 CD BLYS A 23 11.322 50.449 9.595 0.29 20.75 C ANISOU 192 CD BLYS A 23 3322 1391 3169 456 -112 602 C ATOM 193 CE ALYS A 23 10.876 51.973 9.631 0.71 23.53 C ANISOU 193 CE ALYS A 23 3797 1238 3905 447 437 -17 C ATOM 194 CE BLYS A 23 10.096 51.325 9.345 0.29 23.94 C ANISOU 194 CE BLYS A 23 3621 1656 3820 981 41 -246 C ATOM 195 NZ ALYS A 23 11.633 53.212 9.951 0.71 28.04 N ANISOU 195 NZ ALYS A 23 5040 1009 4605 662 -824 -416 N ATOM 196 NZ BLYS A 23 10.051 51.759 7.921 0.29 26.05 N ANISOU 196 NZ BLYS A 23 3892 2357 3648 1895 -1212 -694 N ATOM 197 N THR A 24 14.444 46.378 10.701 1.00 13.25 N ANISOU 197 N THR A 24 2427 1006 1602 -268 -177 84 N ATOM 198 CA THR A 24 15.122 45.426 11.598 1.00 13.05 C ANISOU 198 CA THR A 24 2550 706 1702 -583 21 360 C ATOM 199 C THR A 24 16.409 46.034 12.120 1.00 13.01 C ANISOU 199 C THR A 24 2403 893 1646 -406 -115 309 C ATOM 200 O THR A 24 16.716 45.946 13.311 1.00 13.48 O ANISOU 200 O THR A 24 2320 1206 1594 268 -47 56 O ATOM 201 CB THR A 24 15.448 44.098 10.897 1.00 13.62 C ANISOU 201 CB THR A 24 2180 1133 1864 -213 -288 -34 C ATOM 202 OG1 THR A 24 14.237 43.472 10.499 1.00 11.63 O ANISOU 202 OG1 THR A 24 1989 1113 1315 -25 -231 -52 O ATOM 203 CG2 THR A 24 16.096 43.102 11.874 1.00 11.59 C ANISOU 203 CG2 THR A 24 1605 1324 1473 10 -70 -197 C ATOM 204 N LYS A 25 17.196 46.692 11.275 1.00 12.34 N ANISOU 204 N LYS A 25 2215 606 1866 -224 360 -131 N ATOM 205 CA LYS A 25 18.387 47.388 11.779 1.00 13.37 C ANISOU 205 CA LYS A 25 2471 1668 940 -675 502 -146 C ATOM 206 C LYS A 25 18.076 48.427 12.848 1.00 11.71 C ANISOU 206 C LYS A 25 1733 1593 1121 -429 238 -162 C ATOM 207 O LYS A 25 18.716 48.561 13.896 1.00 11.54 O ANISOU 207 O LYS A 25 2247 898 1241 -400 -100 -98 O ATOM 208 CB LYS A 25 19.125 48.048 10.605 1.00 15.77 C ANISOU 208 CB LYS A 25 2223 2541 1228 -614 660 151 C ATOM 209 CG LYS A 25 20.377 48.816 11.035 1.00 16.78 C ANISOU 209 CG LYS A 25 2523 2390 1464 -797 228 718 C ATOM 210 CD LYS A 25 21.053 49.432 9.802 1.00 14.98 C ANISOU 210 CD LYS A 25 2296 1862 1534 -386 828 188 C ATOM 211 CE LYS A 25 22.289 50.210 10.183 1.00 18.91 C ANISOU 211 CE LYS A 25 2165 2492 2528 -529 555 604 C ATOM 212 NZ LYS A 25 23.110 50.633 9.023 1.00 23.13 N ANISOU 212 NZ LYS A 25 3186 2653 2950 -1343 1012 424 N ATOM 213 N GLN A 26 16.997 49.187 12.634 1.00 12.52 N ANISOU 213 N GLN A 26 2276 969 1510 -522 -225 273 N ATOM 214 CA GLN A 26 16.646 50.231 13.585 1.00 12.12 C ANISOU 214 CA GLN A 26 1605 838 2161 -471 44 245 C ATOM 215 C GLN A 26 16.237 49.611 14.919 1.00 9.82 C ANISOU 215 C GLN A 26 1362 380 1989 191 90 95 C ATOM 216 O GLN A 26 16.542 50.172 15.971 1.00 13.01 O ANISOU 216 O GLN A 26 1892 907 2145 -101 261 -186 O ATOM 217 CB GLN A 26 15.539 51.148 13.051 1.00 15.88 C ANISOU 217 CB GLN A 26 2125 1599 2309 -71 -65 878 C ATOM 218 CG GLN A 26 16.075 52.041 11.910 1.00 21.77 C ANISOU 218 CG GLN A 26 3255 2374 2645 -438 69 1318 C ATOM 219 CD GLN A 26 15.054 52.948 11.255 1.00 26.04 C ANISOU 219 CD GLN A 26 4081 2930 2884 -117 59 1981 C ATOM 220 OE1 GLN A 26 15.321 53.914 10.539 1.00 33.73 O ANISOU 220 OE1 GLN A 26 5849 2671 4295 -613 -143 2296 O ATOM 221 NE2 GLN A 26 13.786 52.670 11.473 1.00 24.83 N ANISOU 221 NE2 GLN A 26 3732 2171 3532 592 163 1131 N ATOM 222 N LEU A 27 15.554 48.467 14.840 1.00 10.95 N ANISOU 222 N LEU A 27 1591 850 1721 -311 -6 398 N ATOM 223 CA LEU A 27 15.191 47.803 16.076 1.00 10.59 C ANISOU 223 CA LEU A 27 1543 1051 1429 -251 -2 143 C ATOM 224 C LEU A 27 16.440 47.320 16.792 1.00 10.29 C ANISOU 224 C LEU A 27 1563 1035 1314 24 300 258 C ATOM 225 O LEU A 27 16.577 47.466 18.011 1.00 10.33 O ANISOU 225 O LEU A 27 1506 1054 1367 -326 17 216 O ATOM 226 CB LEU A 27 14.248 46.636 15.774 1.00 12.64 C ANISOU 226 CB LEU A 27 1494 723 2588 -198 259 466 C ATOM 227 CG LEU A 27 13.879 45.737 16.953 1.00 11.98 C ANISOU 227 CG LEU A 27 1825 1104 1624 -523 -16 35 C ATOM 228 CD1 LEU A 27 13.065 46.490 17.996 1.00 13.54 C ANISOU 228 CD1 LEU A 27 1890 1234 2021 -222 -73 -151 C ATOM 229 CD2 LEU A 27 13.054 44.576 16.451 1.00 9.85 C ANISOU 229 CD2 LEU A 27 1245 1012 1486 -415 23 178 C ATOM 230 N LEU A 28 17.396 46.696 16.105 1.00 11.36 N ANISOU 230 N LEU A 28 1475 786 2056 -302 273 -343 N ATOM 231 CA LEU A 28 18.648 46.275 16.753 1.00 11.52 C ANISOU 231 CA LEU A 28 1083 1248 2046 -379 573 -335 C ATOM 232 C LEU A 28 19.415 47.442 17.357 1.00 10.11 C ANISOU 232 C LEU A 28 1490 889 1461 -422 331 226 C ATOM 233 O LEU A 28 19.918 47.340 18.502 1.00 12.59 O ANISOU 233 O LEU A 28 2284 881 1616 63 -78 93 O ATOM 234 CB ALEU A 28 19.513 45.618 15.669 0.43 15.80 C ANISOU 234 CB ALEU A 28 1316 2279 2407 -305 575 -973 C ATOM 235 CB BLEU A 28 19.546 45.471 15.800 0.57 15.71 C ANISOU 235 CB BLEU A 28 1705 2125 2139 132 449 -763 C ATOM 236 CG ALEU A 28 18.864 44.426 14.971 0.43 16.48 C ANISOU 236 CG ALEU A 28 1777 2267 2217 -385 518 -955 C ATOM 237 CG BLEU A 28 20.802 44.849 16.444 0.57 14.98 C ANISOU 237 CG BLEU A 28 1283 2206 2201 18 785 -727 C ATOM 238 CD1ALEU A 28 19.530 44.102 13.638 0.43 17.64 C ANISOU 238 CD1ALEU A 28 2510 2567 1627 -24 238 -549 C ATOM 239 CD1BLEU A 28 20.436 44.250 17.793 0.57 15.14 C ANISOU 239 CD1BLEU A 28 1935 1056 2759 -776 264 -226 C ATOM 240 CD2ALEU A 28 18.884 43.229 15.918 0.43 27.60 C ANISOU 240 CD2ALEU A 28 4378 2926 3183 -1416 2207 -82 C ATOM 241 CD2BLEU A 28 21.451 43.802 15.546 0.57 16.91 C ANISOU 241 CD2BLEU A 28 1651 1150 3625 -431 629 -1245 C ATOM 242 N GLU A 29 19.509 48.557 16.611 1.00 11.06 N ANISOU 242 N GLU A 29 1932 905 1368 -104 529 217 N ATOM 243 CA GLU A 29 20.234 49.752 17.069 1.00 12.84 C ANISOU 243 CA GLU A 29 2416 726 1735 -307 849 221 C ATOM 244 C GLU A 29 19.592 50.243 18.358 1.00 9.30 C ANISOU 244 C GLU A 29 1688 651 1194 17 160 450 C ATOM 245 O GLU A 29 20.307 50.597 19.305 1.00 12.84 O ANISOU 245 O GLU A 29 2019 842 2019 -73 -225 -19 O ATOM 246 CB GLU A 29 20.286 50.862 16.012 1.00 15.06 C ANISOU 246 CB GLU A 29 3406 1254 1062 -958 376 146 C ATOM 247 CG GLU A 29 21.186 50.425 14.833 1.00 20.12 C ANISOU 247 CG GLU A 29 3885 2529 1230 -229 617 338 C ATOM 248 CD GLU A 29 21.083 51.473 13.733 1.00 23.38 C ANISOU 248 CD GLU A 29 3352 3793 1737 -814 709 1276 C ATOM 249 OE1 GLU A 29 19.964 51.800 13.267 1.00 30.85 O ANISOU 249 OE1 GLU A 29 4365 3311 4045 -1094 -1044 1587 O ATOM 250 OE2 GLU A 29 22.128 51.990 13.341 1.00 37.59 O ANISOU 250 OE2 GLU A 29 4301 5870 4112 -1765 1628 1858 O ATOM 251 N LYS A 30 18.261 50.273 18.343 1.00 11.53 N ANISOU 251 N LYS A 30 1606 762 2011 -193 261 205 N ATOM 252 CA LYS A 30 17.613 50.754 19.576 1.00 11.82 C ANISOU 252 CA LYS A 30 1657 793 2043 -276 416 255 C ATOM 253 C LYS A 30 17.876 49.840 20.761 1.00 10.97 C ANISOU 253 C LYS A 30 1590 599 1978 -812 -127 169 C ATOM 254 O LYS A 30 18.137 50.277 21.900 1.00 13.46 O ANISOU 254 O LYS A 30 2280 606 2227 -57 -276 -228 O ATOM 255 CB LYS A 30 16.097 50.899 19.353 1.00 14.76 C ANISOU 255 CB LYS A 30 1817 1394 2397 410 185 -3 C ATOM 256 CG LYS A 30 15.384 51.585 20.512 1.00 13.98 C ANISOU 256 CG LYS A 30 2037 865 2410 46 564 294 C ATOM 257 CD LYS A 30 15.804 53.068 20.525 1.00 18.58 C ANISOU 257 CD LYS A 30 2091 1174 3795 -597 -242 -536 C ATOM 258 CE LYS A 30 14.742 53.853 21.295 1.00 29.13 C ANISOU 258 CE LYS A 30 3470 1702 5897 264 33 -1554 C ATOM 259 NZ LYS A 30 15.191 55.250 21.501 1.00 42.89 N ANISOU 259 NZ LYS A 30 2085 2155 12057 339 -775 -2978 N ATOM 260 N ILE A 31 17.775 48.515 20.516 1.00 10.61 N ANISOU 260 N ILE A 31 1489 674 1870 -517 -397 64 N ATOM 261 CA ILE A 31 18.159 47.546 21.550 1.00 9.68 C ANISOU 261 CA ILE A 31 1355 483 1838 -365 -116 6 C ATOM 262 C ILE A 31 19.608 47.807 22.033 1.00 6.81 C ANISOU 262 C ILE A 31 1320 191 1075 -188 145 -135 C ATOM 263 O ILE A 31 19.831 47.776 23.254 1.00 9.56 O ANISOU 263 O ILE A 31 1672 840 1120 64 -15 -240 O ATOM 264 CB ILE A 31 17.977 46.124 21.034 1.00 9.19 C ANISOU 264 CB ILE A 31 1449 644 1400 -459 168 -194 C ATOM 265 CG1 ILE A 31 16.520 45.789 20.794 1.00 12.24 C ANISOU 265 CG1 ILE A 31 1472 1031 2146 -542 -33 -422 C ATOM 266 CG2 ILE A 31 18.622 45.147 22.017 1.00 14.43 C ANISOU 266 CG2 ILE A 31 2090 429 2962 -451 -547 162 C ATOM 267 CD1 ILE A 31 16.193 44.404 20.336 1.00 13.44 C ANISOU 267 CD1 ILE A 31 1927 1107 2074 -629 -398 -400 C ATOM 268 N ILE A 32 20.542 48.030 21.151 1.00 9.88 N ANISOU 268 N ILE A 32 1526 654 1573 -480 461 -120 N ATOM 269 CA ILE A 32 21.914 48.320 21.567 1.00 10.45 C ANISOU 269 CA ILE A 32 1520 695 1754 -487 455 -71 C ATOM 270 C ILE A 32 22.006 49.623 22.319 1.00 9.81 C ANISOU 270 C ILE A 32 1283 833 1610 -325 303 -137 C ATOM 271 O ILE A 32 22.757 49.722 23.303 1.00 12.40 O ANISOU 271 O ILE A 32 1494 1435 1784 -401 85 -148 O ATOM 272 CB ILE A 32 22.811 48.333 20.310 1.00 9.21 C ANISOU 272 CB ILE A 32 1381 509 1608 -175 325 28 C ATOM 273 CG1 ILE A 32 22.883 46.932 19.670 1.00 9.16 C ANISOU 273 CG1 ILE A 32 1818 547 1116 54 -321 53 C ATOM 274 CG2 ILE A 32 24.177 48.910 20.699 1.00 12.88 C ANISOU 274 CG2 ILE A 32 1587 992 2316 -598 676 -485 C ATOM 275 CD1 ILE A 32 23.414 46.959 18.236 1.00 13.33 C ANISOU 275 CD1 ILE A 32 2281 1150 1635 193 475 -49 C ATOM 276 N GLU A 33 21.245 50.627 21.930 1.00 12.47 N ANISOU 276 N GLU A 33 1301 979 2458 -91 138 -263 N ATOM 277 CA GLU A 33 21.283 51.935 22.605 1.00 12.20 C ANISOU 277 CA GLU A 33 1907 552 2178 -605 265 158 C ATOM 278 C GLU A 33 20.835 51.792 24.045 1.00 10.79 C ANISOU 278 C GLU A 33 1638 472 1989 -317 -49 219 C ATOM 279 O GLU A 33 21.363 52.323 25.001 1.00 15.16 O ANISOU 279 O GLU A 33 1632 1809 2318 -271 -31 -474 O ATOM 280 CB GLU A 33 20.430 52.964 21.834 1.00 14.76 C ANISOU 280 CB GLU A 33 3109 697 1801 -295 271 280 C ATOM 281 CG GLU A 33 21.167 53.363 20.549 1.00 19.98 C ANISOU 281 CG GLU A 33 3783 2186 1623 -26 499 301 C ATOM 282 CD GLU A 33 20.367 53.974 19.421 1.00 24.60 C ANISOU 282 CD GLU A 33 4624 2791 1932 -241 170 855 C ATOM 283 OE1 GLU A 33 19.126 54.125 19.569 1.00 23.50 O ANISOU 283 OE1 GLU A 33 4398 1430 3102 -369 -604 347 O ATOM 284 OE2 GLU A 33 20.973 54.308 18.350 1.00 29.61 O ANISOU 284 OE2 GLU A 33 7242 2130 1880 1149 1341 658 O ATOM 285 N GLU A 34 19.754 50.995 24.175 1.00 10.94 N ANISOU 285 N GLU A 34 1772 247 2137 -270 291 138 N ATOM 286 CA GLU A 34 19.129 50.923 25.506 1.00 11.55 C ANISOU 286 CA GLU A 34 1476 935 1977 -251 57 57 C ATOM 287 C GLU A 34 19.754 49.880 26.430 1.00 11.37 C ANISOU 287 C GLU A 34 1706 996 1618 1 -110 -282 C ATOM 288 O GLU A 34 19.696 50.109 27.652 1.00 12.49 O ANISOU 288 O GLU A 34 1896 1186 1663 -121 20 -349 O ATOM 289 CB AGLU A 34 17.631 50.657 25.370 0.64 12.19 C ANISOU 289 CB AGLU A 34 1394 1537 1701 -30 -31 -484 C ATOM 290 CB BGLU A 34 17.645 50.582 25.355 0.36 12.75 C ANISOU 290 CB BGLU A 34 1374 1586 1884 -91 17 -343 C ATOM 291 CG AGLU A 34 16.922 51.624 24.437 0.64 13.42 C ANISOU 291 CG AGLU A 34 1589 821 2691 -238 -285 -330 C ATOM 292 CG BGLU A 34 16.769 51.711 24.851 0.36 17.31 C ANISOU 292 CG BGLU A 34 1627 2249 2703 210 51 254 C ATOM 293 CD AGLU A 34 15.417 51.606 24.615 0.64 16.81 C ANISOU 293 CD AGLU A 34 1647 1734 3004 235 -101 205 C ATOM 294 CD BGLU A 34 16.833 52.910 25.777 0.36 21.29 C ANISOU 294 CD BGLU A 34 2765 1940 3385 890 456 113 C ATOM 295 OE1AGLU A 34 14.860 50.691 25.241 0.64 15.21 O ANISOU 295 OE1AGLU A 34 1427 1822 2531 222 224 -204 O ATOM 296 OE1BGLU A 34 16.765 52.718 27.008 0.36 27.10 O ANISOU 296 OE1BGLU A 34 4539 2501 3257 649 1042 -402 O ATOM 297 OE2AGLU A 34 14.762 52.552 24.114 0.64 31.53 O ANISOU 297 OE2AGLU A 34 2421 3954 5603 1467 841 2381 O ATOM 298 OE2BGLU A 34 16.986 54.028 25.261 0.36 32.15 O ANISOU 298 OE2BGLU A 34 5612 1904 4700 1471 -1904 746 O ATOM 299 N ASN A 35 20.317 48.775 25.891 1.00 10.23 N ANISOU 299 N ASN A 35 1473 628 1787 -366 178 -192 N ATOM 300 CA ASN A 35 20.892 47.715 26.712 1.00 10.68 C ANISOU 300 CA ASN A 35 1526 647 1884 -368 153 -194 C ATOM 301 C ASN A 35 22.405 47.713 26.685 1.00 11.36 C ANISOU 301 C ASN A 35 1468 756 2093 -609 -215 -70 C ATOM 302 O ASN A 35 23.014 46.978 27.438 1.00 13.92 O ANISOU 302 O ASN A 35 1946 1824 1518 -153 -100 77 O ATOM 303 CB ASN A 35 20.383 46.351 26.254 1.00 9.61 C ANISOU 303 CB ASN A 35 1411 711 1531 -621 -309 157 C ATOM 304 CG ASN A 35 18.873 46.240 26.500 1.00 11.54 C ANISOU 304 CG ASN A 35 1484 1581 1320 -508 -29 -983 C ATOM 305 OD1 ASN A 35 18.468 46.001 27.638 1.00 11.90 O ANISOU 305 OD1 ASN A 35 1731 1145 1645 34 273 -428 O ATOM 306 ND2 ASN A 35 18.126 46.466 25.427 1.00 10.80 N ANISOU 306 ND2 ASN A 35 1371 1170 1561 -408 -123 -792 N ATOM 307 N HIS A 36 23.043 48.506 25.842 1.00 9.82 N ANISOU 307 N HIS A 36 1511 852 1369 -453 85 -476 N ATOM 308 CA HIS A 36 24.495 48.602 25.772 1.00 9.38 C ANISOU 308 CA HIS A 36 1428 1217 921 -265 77 -622 C ATOM 309 C HIS A 36 25.164 47.301 25.329 1.00 9.30 C ANISOU 309 C HIS A 36 1554 800 1179 -318 -55 -238 C ATOM 310 O HIS A 36 26.313 46.981 25.602 1.00 12.61 O ANISOU 310 O HIS A 36 1494 983 2315 -290 -270 -290 O ATOM 311 CB HIS A 36 25.088 49.108 27.120 1.00 11.67 C ANISOU 311 CB HIS A 36 1969 1350 1116 -277 -328 -517 C ATOM 312 CG HIS A 36 24.277 50.281 27.602 1.00 13.30 C ANISOU 312 CG HIS A 36 2317 1179 1559 -647 -1 -973 C ATOM 313 ND1 HIS A 36 23.466 50.253 28.734 1.00 19.36 N ANISOU 313 ND1 HIS A 36 3548 2027 1780 -18 606 -803 N ATOM 314 CD2 HIS A 36 24.128 51.522 27.065 1.00 15.46 C ANISOU 314 CD2 HIS A 36 2211 928 2734 -873 80 -809 C ATOM 315 CE1 HIS A 36 22.863 51.441 28.882 1.00 19.35 C ANISOU 315 CE1 HIS A 36 2693 1763 2895 -583 468 -1544 C ATOM 316 NE2 HIS A 36 23.259 52.227 27.883 1.00 18.92 N ANISOU 316 NE2 HIS A 36 2178 1849 3162 29 -257 -821 N ATOM 317 N THR A 37 24.440 46.499 24.561 1.00 9.61 N ANISOU 317 N THR A 37 1442 784 1425 -36 -198 -424 N ATOM 318 CA THR A 37 24.876 45.158 24.183 1.00 8.80 C ANISOU 318 CA THR A 37 1438 416 1491 -406 153 -19 C ATOM 319 C THR A 37 26.081 45.139 23.253 1.00 9.02 C ANISOU 319 C THR A 37 1324 847 1257 -73 -24 -99 C ATOM 320 O THR A 37 25.909 45.746 22.181 1.00 9.81 O ANISOU 320 O THR A 37 1501 965 1263 -164 -65 -16 O ATOM 321 CB THR A 37 23.692 44.448 23.489 1.00 9.79 C ANISOU 321 CB THR A 37 1303 686 1732 -74 -41 -380 C ATOM 322 OG1 THR A 37 22.501 44.641 24.309 1.00 11.38 O ANISOU 322 OG1 THR A 37 1378 1050 1896 -271 104 -528 O ATOM 323 CG2 THR A 37 23.985 42.970 23.352 1.00 9.39 C ANISOU 323 CG2 THR A 37 1686 608 1275 -213 -264 -350 C ATOM 324 N LYS A 38 27.150 44.453 23.579 1.00 11.14 N ANISOU 324 N LYS A 38 1532 922 1778 172 -29 -9 N ATOM 325 CA LYS A 38 28.341 44.282 22.730 1.00 11.85 C ANISOU 325 CA LYS A 38 1305 1071 2125 -72 -50 -343 C ATOM 326 C LYS A 38 28.111 42.978 21.969 1.00 9.44 C ANISOU 326 C LYS A 38 1297 800 1490 -70 -64 83 C ATOM 327 O LYS A 38 27.602 41.981 22.552 1.00 10.49 O ANISOU 327 O LYS A 38 1341 1096 1548 -271 41 83 O ATOM 328 CB LYS A 38 29.641 44.186 23.506 1.00 12.10 C ANISOU 328 CB LYS A 38 1391 415 2791 -303 -349 -85 C ATOM 329 CG LYS A 38 29.848 45.448 24.378 1.00 16.96 C ANISOU 329 CG LYS A 38 2542 1343 2560 365 -967 -702 C ATOM 330 CD LYS A 38 31.154 45.401 25.119 1.00 26.81 C ANISOU 330 CD LYS A 38 2995 3026 4166 -66 -1838 -1327 C ATOM 331 CE LYS A 38 31.809 46.786 25.011 1.00 34.89 C ANISOU 331 CE LYS A 38 3449 4326 5482 -1338 -1474 -229 C ATOM 332 NZ LYS A 38 32.010 47.136 23.568 1.00 42.71 N ANISOU 332 NZ LYS A 38 6645 3543 6040 2037 1409 -189 N ATOM 333 N PRO A 39 28.422 42.928 20.662 1.00 11.65 N ANISOU 333 N PRO A 39 1609 1138 1680 -527 271 -28 N ATOM 334 CA PRO A 39 28.116 41.736 19.860 1.00 10.17 C ANISOU 334 CA PRO A 39 1466 959 1439 -122 79 86 C ATOM 335 C PRO A 39 28.769 40.485 20.448 1.00 8.95 C ANISOU 335 C PRO A 39 1160 1203 1038 -42 316 155 C ATOM 336 O PRO A 39 28.110 39.396 20.414 1.00 11.03 O ANISOU 336 O PRO A 39 1589 1014 1587 -66 -206 35 O ATOM 337 CB PRO A 39 28.656 42.073 18.471 1.00 10.64 C ANISOU 337 CB PRO A 39 1513 1192 1337 -269 -168 274 C ATOM 338 CG PRO A 39 29.637 43.198 18.709 1.00 12.16 C ANISOU 338 CG PRO A 39 1688 1167 1766 -339 306 99 C ATOM 339 CD PRO A 39 29.072 43.989 19.866 1.00 13.77 C ANISOU 339 CD PRO A 39 1916 1467 1850 -837 557 -121 C ATOM 340 N GLU A 40 29.948 40.560 21.038 1.00 10.47 N ANISOU 340 N GLU A 40 1320 1062 1596 -88 45 28 N ATOM 341 CA GLU A 40 30.597 39.316 21.495 1.00 10.54 C ANISOU 341 CA GLU A 40 981 1291 1734 55 370 228 C ATOM 342 C GLU A 40 29.898 38.741 22.718 1.00 10.62 C ANISOU 342 C GLU A 40 1524 1267 1243 24 246 20 C ATOM 343 O GLU A 40 30.115 37.591 23.088 1.00 10.75 O ANISOU 343 O GLU A 40 1574 1009 1502 -471 -101 -63 O ATOM 344 CB GLU A 40 32.099 39.547 21.802 1.00 13.45 C ANISOU 344 CB GLU A 40 1225 1692 2192 -103 -83 213 C ATOM 345 CG GLU A 40 32.333 40.573 22.859 1.00 22.10 C ANISOU 345 CG GLU A 40 2793 2444 3161 -910 -401 -369 C ATOM 346 CD GLU A 40 32.447 42.047 22.529 1.00 28.25 C ANISOU 346 CD GLU A 40 3324 2223 5185 -961 -1891 -458 C ATOM 347 OE1 GLU A 40 31.828 42.577 21.568 1.00 20.11 O ANISOU 347 OE1 GLU A 40 1423 2312 3906 -1076 -121 -142 O ATOM 348 OE2 GLU A 40 33.212 42.691 23.305 1.00 29.41 O ANISOU 348 OE2 GLU A 40 2844 2592 5739 -383 -1776 -1366 O ATOM 349 N ASP A 41 29.029 39.506 23.360 1.00 10.48 N ANISOU 349 N ASP A 41 1419 1625 937 8 -6 -236 N ATOM 350 CA ASP A 41 28.281 39.027 24.514 1.00 10.12 C ANISOU 350 CA ASP A 41 1250 1826 769 160 -107 -258 C ATOM 351 C ASP A 41 26.913 38.440 24.129 1.00 9.62 C ANISOU 351 C ASP A 41 1382 746 1525 170 -189 -140 C ATOM 352 O ASP A 41 26.142 37.985 24.970 1.00 11.63 O ANISOU 352 O ASP A 41 1530 1360 1530 -7 -176 -115 O ATOM 353 CB ASP A 41 28.068 40.221 25.454 1.00 11.20 C ANISOU 353 CB ASP A 41 1404 1683 1170 -287 170 -396 C ATOM 354 CG ASP A 41 29.332 40.669 26.175 1.00 12.16 C ANISOU 354 CG ASP A 41 1917 1157 1546 -438 -437 159 C ATOM 355 OD1 ASP A 41 30.244 39.820 26.360 1.00 16.74 O ANISOU 355 OD1 ASP A 41 2043 1805 2513 18 -803 -411 O ATOM 356 OD2 ASP A 41 29.476 41.854 26.530 1.00 16.24 O ANISOU 356 OD2 ASP A 41 2796 1328 2048 -367 -859 -134 O ATOM 357 N VAL A 42 26.613 38.477 22.816 1.00 8.53 N ANISOU 357 N VAL A 42 1051 733 1459 127 -185 -516 N ATOM 358 CA VAL A 42 25.346 37.879 22.357 1.00 7.64 C ANISOU 358 CA VAL A 42 1130 322 1453 -308 -35 269 C ATOM 359 C VAL A 42 25.544 36.388 22.135 1.00 8.62 C ANISOU 359 C VAL A 42 1314 396 1566 -176 167 247 C ATOM 360 O VAL A 42 26.392 35.974 21.308 1.00 9.92 O ANISOU 360 O VAL A 42 1721 695 1354 -134 208 -9 O ATOM 361 CB VAL A 42 24.891 38.533 21.049 1.00 9.41 C ANISOU 361 CB VAL A 42 1356 465 1756 -408 -459 324 C ATOM 362 CG1 VAL A 42 23.615 37.904 20.554 1.00 8.03 C ANISOU 362 CG1 VAL A 42 797 854 1401 -120 100 -301 C ATOM 363 CG2 VAL A 42 24.749 40.040 21.329 1.00 10.34 C ANISOU 363 CG2 VAL A 42 1658 433 1837 -307 -380 417 C ATOM 364 N VAL A 43 24.821 35.547 22.832 1.00 8.02 N ANISOU 364 N VAL A 43 1232 416 1397 -218 18 323 N ATOM 365 CA VAL A 43 24.872 34.099 22.681 1.00 7.11 C ANISOU 365 CA VAL A 43 1416 376 911 22 -396 442 C ATOM 366 C VAL A 43 24.381 33.708 21.302 1.00 6.99 C ANISOU 366 C VAL A 43 630 1193 832 -183 83 72 C ATOM 367 O VAL A 43 24.982 32.949 20.513 1.00 9.00 O ANISOU 367 O VAL A 43 1020 1119 1281 -34 169 -19 O ATOM 368 CB VAL A 43 23.980 33.426 23.745 1.00 9.11 C ANISOU 368 CB VAL A 43 2281 491 691 -28 -394 685 C ATOM 369 CG1 VAL A 43 23.864 31.932 23.589 1.00 8.55 C ANISOU 369 CG1 VAL A 43 1713 546 988 -16 -22 375 C ATOM 370 CG2 VAL A 43 24.492 33.703 25.179 1.00 10.02 C ANISOU 370 CG2 VAL A 43 1689 1276 844 218 -322 22 C ATOM 371 N GLN A 44 23.196 34.273 21.014 1.00 7.50 N ANISOU 371 N GLN A 44 894 1082 876 -68 -241 -17 N ATOM 372 CA GLN A 44 22.529 33.961 19.721 1.00 5.93 C ANISOU 372 CA GLN A 44 1274 378 601 277 -212 337 C ATOM 373 C GLN A 44 21.310 34.860 19.562 1.00 6.81 C ANISOU 373 C GLN A 44 736 731 1119 179 -342 -523 C ATOM 374 O GLN A 44 20.893 35.499 20.544 1.00 8.81 O ANISOU 374 O GLN A 44 1225 929 1195 -74 89 -462 O ATOM 375 CB GLN A 44 22.050 32.498 19.706 1.00 7.23 C ANISOU 375 CB GLN A 44 1696 556 496 -113 142 39 C ATOM 376 CG GLN A 44 20.934 32.236 20.728 1.00 7.48 C ANISOU 376 CG GLN A 44 1335 849 660 50 66 151 C ATOM 377 CD GLN A 44 20.500 30.791 20.832 1.00 8.45 C ANISOU 377 CD GLN A 44 1241 1017 953 -246 295 -84 C ATOM 378 OE1 GLN A 44 19.319 30.434 20.862 1.00 16.55 O ANISOU 378 OE1 GLN A 44 1385 2154 2747 -659 82 -46 O ATOM 379 NE2 GLN A 44 21.494 29.904 20.901 1.00 8.03 N ANISOU 379 NE2 GLN A 44 1692 689 672 -144 203 -352 N ATOM 380 N MET A 45 20.727 34.862 18.361 1.00 6.35 N ANISOU 380 N MET A 45 736 790 886 69 -127 233 N ATOM 381 CA MET A 45 19.524 35.637 18.120 1.00 7.17 C ANISOU 381 CA MET A 45 901 498 1323 116 -355 -73 C ATOM 382 C MET A 45 18.536 34.824 17.282 1.00 7.83 C ANISOU 382 C MET A 45 881 1357 735 67 -181 -344 C ATOM 383 O MET A 45 18.962 34.069 16.401 1.00 8.60 O ANISOU 383 O MET A 45 1302 1258 706 402 -123 -255 O ATOM 384 CB AMET A 45 19.790 36.946 17.372 0.67 8.19 C ANISOU 384 CB AMET A 45 1522 687 902 375 -69 -2 C ATOM 385 CB BMET A 45 19.866 36.959 17.420 0.33 9.35 C ANISOU 385 CB BMET A 45 1547 583 1422 412 250 71 C ATOM 386 CG AMET A 45 20.757 37.839 18.128 0.67 9.26 C ANISOU 386 CG AMET A 45 972 496 2049 103 387 -236 C ATOM 387 CG BMET A 45 18.796 38.027 17.432 0.33 10.79 C ANISOU 387 CG BMET A 45 2090 872 1136 838 -424 -77 C ATOM 388 SD AMET A 45 21.037 39.374 17.211 0.67 12.58 S ANISOU 388 SD AMET A 45 1796 1489 1495 -405 -55 345 S ATOM 389 SD BMET A 45 19.321 39.650 16.839 0.33 21.41 S ANISOU 389 SD BMET A 45 3422 1441 3272 1276 -135 1507 S ATOM 390 CE AMET A 45 19.449 39.716 16.498 0.67 13.35 C ANISOU 390 CE AMET A 45 1336 2650 1086 -144 856 1255 C ATOM 391 CE BMET A 45 21.082 39.387 16.652 0.33 16.03 C ANISOU 391 CE BMET A 45 3732 0 2358 1025 1612 517 C ATOM 392 N LEU A 46 17.239 35.064 17.523 1.00 7.63 N ANISOU 392 N LEU A 46 795 933 1170 -140 -35 -67 N ATOM 393 CA LEU A 46 16.175 34.501 16.699 1.00 7.03 C ANISOU 393 CA LEU A 46 987 405 1280 -213 -287 136 C ATOM 394 C LEU A 46 15.341 35.697 16.237 1.00 7.74 C ANISOU 394 C LEU A 46 1204 608 1127 50 -70 242 C ATOM 395 O LEU A 46 15.098 36.661 16.978 1.00 10.16 O ANISOU 395 O LEU A 46 1043 1306 1510 521 -220 -231 O ATOM 396 CB LEU A 46 15.270 33.567 17.482 1.00 8.61 C ANISOU 396 CB LEU A 46 1449 224 1600 -359 -196 65 C ATOM 397 CG LEU A 46 15.972 32.284 18.010 1.00 10.22 C ANISOU 397 CG LEU A 46 2070 231 1583 -76 150 109 C ATOM 398 CD1 LEU A 46 14.967 31.463 18.837 1.00 13.96 C ANISOU 398 CD1 LEU A 46 2608 251 2446 355 1121 333 C ATOM 399 CD2 LEU A 46 16.536 31.450 16.880 1.00 11.55 C ANISOU 399 CD2 LEU A 46 1720 733 1936 -47 475 -8 C ATOM 400 N LEU A 47 14.961 35.672 14.959 1.00 8.59 N ANISOU 400 N LEU A 47 1031 1118 1115 117 -135 197 N ATOM 401 CA LEU A 47 14.036 36.686 14.444 1.00 7.62 C ANISOU 401 CA LEU A 47 913 687 1298 -84 -71 269 C ATOM 402 C LEU A 47 12.841 35.989 13.839 1.00 8.20 C ANISOU 402 C LEU A 47 974 894 1249 25 -142 0 C ATOM 403 O LEU A 47 13.062 35.010 13.081 1.00 11.24 O ANISOU 403 O LEU A 47 1400 918 1953 41 -130 -275 O ATOM 404 CB LEU A 47 14.743 37.485 13.342 1.00 10.31 C ANISOU 404 CB LEU A 47 1623 863 1430 -277 102 253 C ATOM 405 CG LEU A 47 15.741 38.526 13.806 1.00 13.04 C ANISOU 405 CG LEU A 47 1814 796 2345 -532 213 218 C ATOM 406 CD1 LEU A 47 16.805 38.829 12.767 1.00 26.77 C ANISOU 406 CD1 LEU A 47 2890 3400 3881 -1889 1448 -754 C ATOM 407 CD2 LEU A 47 14.980 39.833 14.061 1.00 19.01 C ANISOU 407 CD2 LEU A 47 3455 1090 2678 164 -524 -390 C ATOM 408 N SER A 48 11.649 36.458 14.139 1.00 8.63 N ANISOU 408 N SER A 48 966 715 1598 175 -495 39 N ATOM 409 CA SER A 48 10.432 35.889 13.552 1.00 7.89 C ANISOU 409 CA SER A 48 972 865 1158 -99 -316 245 C ATOM 410 C SER A 48 9.752 36.954 12.669 1.00 7.70 C ANISOU 410 C SER A 48 1262 756 908 -91 -466 26 C ATOM 411 O SER A 48 9.932 38.165 12.843 1.00 9.45 O ANISOU 411 O SER A 48 1662 716 1210 -13 -365 10 O ATOM 412 CB SER A 48 9.446 35.354 14.581 1.00 8.89 C ANISOU 412 CB SER A 48 1039 888 1450 546 239 314 C ATOM 413 OG SER A 48 8.738 36.427 15.125 1.00 8.35 O ANISOU 413 OG SER A 48 947 545 1681 283 -336 -89 O ATOM 414 N ALA A 49 9.010 36.422 11.671 1.00 8.35 N ANISOU 414 N ALA A 49 1293 963 917 37 -461 -52 N ATOM 415 CA ALA A 49 8.198 37.300 10.833 1.00 11.38 C ANISOU 415 CA ALA A 49 1490 1990 846 153 -485 329 C ATOM 416 C ALA A 49 6.814 36.701 10.670 1.00 9.53 C ANISOU 416 C ALA A 49 1583 1351 687 202 -680 202 C ATOM 417 O ALA A 49 6.653 35.467 10.539 1.00 13.22 O ANISOU 417 O ALA A 49 2202 1307 1516 319 -669 56 O ATOM 418 CB ALA A 49 8.797 37.480 9.451 1.00 11.13 C ANISOU 418 CB ALA A 49 2062 1380 787 20 -290 -7 C ATOM 419 N THR A 50 5.823 37.609 10.686 1.00 11.12 N ANISOU 419 N THR A 50 1521 1230 1474 67 -484 309 N ATOM 420 CA THR A 50 4.452 37.116 10.425 1.00 11.22 C ANISOU 420 CA THR A 50 1413 1699 1150 180 -360 -116 C ATOM 421 C THR A 50 4.446 36.585 9.001 1.00 11.61 C ANISOU 421 C THR A 50 1951 1220 1240 78 -184 -223 C ATOM 422 O THR A 50 5.281 36.957 8.175 1.00 13.75 O ANISOU 422 O THR A 50 1812 2267 1144 -22 -297 -45 O ATOM 423 CB THR A 50 3.421 38.220 10.653 1.00 10.77 C ANISOU 423 CB THR A 50 1565 1505 1023 82 -153 -192 C ATOM 424 OG1 THR A 50 3.967 39.428 10.112 1.00 13.76 O ANISOU 424 OG1 THR A 50 2224 1471 1534 -169 -461 -140 O ATOM 425 CG2 THR A 50 3.233 38.409 12.157 1.00 14.60 C ANISOU 425 CG2 THR A 50 2437 2134 976 264 -369 -419 C ATOM 426 N PRO A 51 3.512 35.705 8.682 1.00 13.24 N ANISOU 426 N PRO A 51 2242 1282 1508 -86 -362 -85 N ATOM 427 CA PRO A 51 3.517 35.115 7.352 1.00 14.58 C ANISOU 427 CA PRO A 51 2363 1593 1582 -533 -534 -200 C ATOM 428 C PRO A 51 3.083 36.023 6.222 1.00 17.58 C ANISOU 428 C PRO A 51 2756 2495 1427 505 -422 -259 C ATOM 429 O PRO A 51 3.034 35.476 5.103 1.00 23.91 O ANISOU 429 O PRO A 51 4527 3249 1308 925 -127 -399 O ATOM 430 CB PRO A 51 2.495 33.963 7.499 1.00 20.99 C ANISOU 430 CB PRO A 51 2869 2860 2245 -1462 69 -748 C ATOM 431 CG PRO A 51 1.591 34.396 8.604 1.00 25.23 C ANISOU 431 CG PRO A 51 3097 3974 2516 -1654 306 -1194 C ATOM 432 CD PRO A 51 2.425 35.208 9.546 1.00 18.40 C ANISOU 432 CD PRO A 51 2501 2376 2115 -753 -5 -476 C ATOM 433 N ASP A 52 2.799 37.293 6.458 1.00 15.94 N ANISOU 433 N ASP A 52 2687 2361 1010 310 -390 112 N ATOM 434 CA ASP A 52 2.558 38.249 5.360 1.00 16.38 C ANISOU 434 CA ASP A 52 2324 2828 1069 193 -532 282 C ATOM 435 C ASP A 52 3.873 38.867 4.926 1.00 18.45 C ANISOU 435 C ASP A 52 2331 3007 1673 303 -434 670 C ATOM 436 O ASP A 52 3.894 39.744 4.065 1.00 22.43 O ANISOU 436 O ASP A 52 2560 4038 1925 266 -288 1300 O ATOM 437 CB ASP A 52 1.561 39.325 5.792 1.00 15.99 C ANISOU 437 CB ASP A 52 2120 2473 1484 64 -754 317 C ATOM 438 CG ASP A 52 1.913 39.918 7.158 1.00 14.76 C ANISOU 438 CG ASP A 52 1428 2357 1822 -376 -427 -45 C ATOM 439 OD1 ASP A 52 3.086 39.741 7.591 1.00 13.97 O ANISOU 439 OD1 ASP A 52 1743 2153 1411 127 -524 74 O ATOM 440 OD2 ASP A 52 1.018 40.598 7.761 1.00 16.30 O ANISOU 440 OD2 ASP A 52 2003 2364 1826 445 -596 291 O ATOM 441 N LEU A 53 4.993 38.430 5.521 1.00 16.51 N ANISOU 441 N LEU A 53 2347 2459 1466 120 -774 -58 N ATOM 442 CA LEU A 53 6.278 38.985 5.111 1.00 16.24 C ANISOU 442 CA LEU A 53 2387 2619 1164 117 -598 -424 C ATOM 443 C LEU A 53 7.164 37.910 4.471 1.00 15.25 C ANISOU 443 C LEU A 53 2853 1861 1080 -28 -205 131 C ATOM 444 O LEU A 53 7.411 36.853 5.083 1.00 17.66 O ANISOU 444 O LEU A 53 2873 2077 1762 -210 -227 541 O ATOM 445 CB LEU A 53 7.031 39.583 6.295 1.00 14.97 C ANISOU 445 CB LEU A 53 2540 1985 1163 125 -864 20 C ATOM 446 CG LEU A 53 6.365 40.794 6.966 1.00 17.96 C ANISOU 446 CG LEU A 53 3414 1655 1755 -253 -609 -286 C ATOM 447 CD1 LEU A 53 7.225 41.349 8.100 1.00 17.08 C ANISOU 447 CD1 LEU A 53 1930 2129 2430 -198 -419 -661 C ATOM 448 CD2 LEU A 53 6.051 41.858 5.914 1.00 18.48 C ANISOU 448 CD2 LEU A 53 3037 1662 2323 -50 -211 90 C ATOM 449 N HIS A 54 7.629 38.230 3.241 1.00 15.16 N ANISOU 449 N HIS A 54 2509 2014 1237 -393 -91 104 N ATOM 450 CA HIS A 54 8.368 37.248 2.476 1.00 13.91 C ANISOU 450 CA HIS A 54 2069 2299 917 -121 -436 249 C ATOM 451 C HIS A 54 9.612 37.796 1.773 1.00 13.26 C ANISOU 451 C HIS A 54 2361 1822 856 -68 -333 415 C ATOM 452 O HIS A 54 10.332 36.990 1.199 1.00 16.54 O ANISOU 452 O HIS A 54 2151 2018 2114 -12 -10 189 O ATOM 453 CB HIS A 54 7.443 36.649 1.399 1.00 19.86 C ANISOU 453 CB HIS A 54 2457 3448 1640 -396 -523 -653 C ATOM 454 CG HIS A 54 6.118 36.110 1.842 1.00 23.35 C ANISOU 454 CG HIS A 54 2623 4229 2020 -908 -487 -936 C ATOM 455 ND1 HIS A 54 6.031 34.884 2.483 1.00 27.15 N ANISOU 455 ND1 HIS A 54 2727 4285 3305 -964 114 -603 N ATOM 456 CD2 HIS A 54 4.837 36.550 1.780 1.00 28.61 C ANISOU 456 CD2 HIS A 54 2507 5191 3172 -963 -451 -135 C ATOM 457 CE1 HIS A 54 4.784 34.600 2.784 1.00 32.03 C ANISOU 457 CE1 HIS A 54 2487 5167 4517 -1122 -459 182 C ATOM 458 NE2 HIS A 54 4.030 35.605 2.364 1.00 31.50 N ANISOU 458 NE2 HIS A 54 2732 5416 3822 -802 -65 255 N ATOM 459 N ALA A 55 9.843 39.117 1.816 1.00 14.05 N ANISOU 459 N ALA A 55 3522 1814 0 -241 -375 440 N ATOM 460 CA ALA A 55 10.781 39.699 0.879 1.00 14.26 C ANISOU 460 CA ALA A 55 3035 1758 627 93 -335 784 C ATOM 461 C ALA A 55 12.224 39.348 1.166 1.00 15.86 C ANISOU 461 C ALA A 55 3233 2227 565 508 -502 73 C ATOM 462 O ALA A 55 13.056 39.241 0.266 1.00 14.86 O ANISOU 462 O ALA A 55 3003 2113 529 51 -537 118 O ATOM 463 CB ALA A 55 10.619 41.225 0.891 1.00 15.58 C ANISOU 463 CB ALA A 55 2777 1785 1359 56 125 632 C ATOM 464 N VAL A 56 12.622 39.201 2.419 1.00 13.72 N ANISOU 464 N VAL A 56 2605 2009 600 -353 -451 282 N ATOM 465 CA VAL A 56 14.024 38.945 2.784 1.00 12.96 C ANISOU 465 CA VAL A 56 2608 1624 693 -75 -286 365 C ATOM 466 C VAL A 56 14.067 38.284 4.151 1.00 13.99 C ANISOU 466 C VAL A 56 2971 1675 669 74 -366 322 C ATOM 467 O VAL A 56 13.102 38.420 4.927 1.00 14.14 O ANISOU 467 O VAL A 56 2867 1831 675 52 -373 597 O ATOM 468 CB VAL A 56 14.801 40.280 2.793 1.00 13.68 C ANISOU 468 CB VAL A 56 2255 1892 1050 -179 -41 246 C ATOM 469 CG1 VAL A 56 14.325 41.179 3.937 1.00 15.71 C ANISOU 469 CG1 VAL A 56 2362 2054 1552 -154 -306 -263 C ATOM 470 CG2 VAL A 56 16.306 40.056 2.866 1.00 16.04 C ANISOU 470 CG2 VAL A 56 2366 1592 2137 189 -185 496 C ATOM 471 N PHE A 57 15.087 37.539 4.546 1.00 13.45 N ANISOU 471 N PHE A 57 2827 1567 716 -87 -348 359 N ATOM 472 CA PHE A 57 15.296 37.166 5.944 1.00 11.36 C ANISOU 472 CA PHE A 57 2200 1576 539 197 -193 71 C ATOM 473 C PHE A 57 15.758 38.368 6.762 1.00 11.28 C ANISOU 473 C PHE A 57 1886 1522 880 67 -10 -8 C ATOM 474 O PHE A 57 16.792 38.966 6.431 1.00 13.59 O ANISOU 474 O PHE A 57 1942 2626 595 -380 -266 414 O ATOM 475 CB PHE A 57 16.383 36.088 6.082 1.00 12.14 C ANISOU 475 CB PHE A 57 2299 1836 479 482 -245 -246 C ATOM 476 CG PHE A 57 15.976 34.786 5.411 1.00 13.84 C ANISOU 476 CG PHE A 57 2656 1669 934 434 -512 -59 C ATOM 477 CD1 PHE A 57 15.175 33.858 6.021 1.00 15.41 C ANISOU 477 CD1 PHE A 57 2782 1762 1310 399 -493 108 C ATOM 478 CD2 PHE A 57 16.403 34.532 4.118 1.00 12.39 C ANISOU 478 CD2 PHE A 57 2779 1019 911 618 -648 -199 C ATOM 479 CE1 PHE A 57 14.799 32.675 5.373 1.00 17.54 C ANISOU 479 CE1 PHE A 57 3504 1606 1555 295 152 -57 C ATOM 480 CE2 PHE A 57 16.050 33.376 3.440 1.00 13.21 C ANISOU 480 CE2 PHE A 57 2357 1135 1526 41 -300 -229 C ATOM 481 CZ PHE A 57 15.233 32.443 4.058 1.00 15.45 C ANISOU 481 CZ PHE A 57 3164 1261 1445 250 93 234 C ATOM 482 N PRO A 58 15.030 38.726 7.812 1.00 10.77 N ANISOU 482 N PRO A 58 2011 1174 909 -44 28 67 N ATOM 483 CA PRO A 58 15.419 39.889 8.626 1.00 10.79 C ANISOU 483 CA PRO A 58 1583 1368 1149 197 19 -150 C ATOM 484 C PRO A 58 16.796 39.709 9.242 1.00 9.44 C ANISOU 484 C PRO A 58 1803 996 789 59 -33 299 C ATOM 485 O PRO A 58 17.474 40.729 9.496 1.00 11.99 O ANISOU 485 O PRO A 58 1835 1086 1634 -200 -100 421 O ATOM 486 CB PRO A 58 14.323 39.954 9.706 1.00 11.51 C ANISOU 486 CB PRO A 58 1852 1147 1373 -351 302 -147 C ATOM 487 CG PRO A 58 13.170 39.173 9.124 1.00 13.52 C ANISOU 487 CG PRO A 58 2274 1567 1297 -764 426 -478 C ATOM 488 CD PRO A 58 13.743 38.115 8.214 1.00 11.94 C ANISOU 488 CD PRO A 58 1806 2062 667 -218 -125 -336 C ATOM 489 N ALA A 59 17.235 38.455 9.432 1.00 10.17 N ANISOU 489 N ALA A 59 2213 1053 599 278 -188 162 N ATOM 490 CA ALA A 59 18.595 38.179 9.918 1.00 10.71 C ANISOU 490 CA ALA A 59 2128 957 985 243 -28 393 C ATOM 491 C ALA A 59 19.666 38.823 9.040 1.00 9.12 C ANISOU 491 C ALA A 59 2200 612 655 62 -182 22 C ATOM 492 O ALA A 59 20.781 39.052 9.560 1.00 12.62 O ANISOU 492 O ALA A 59 1918 1347 1529 212 -295 31 O ATOM 493 CB ALA A 59 18.834 36.645 9.986 1.00 10.14 C ANISOU 493 CB ALA A 59 2010 866 978 31 -158 272 C ATOM 494 N LYS A 60 19.429 39.109 7.774 1.00 11.42 N ANISOU 494 N LYS A 60 2570 1168 603 -69 -32 109 N ATOM 495 CA LYS A 60 20.404 39.766 6.923 1.00 12.02 C ANISOU 495 CA LYS A 60 2781 1118 668 -235 -268 332 C ATOM 496 C LYS A 60 20.870 41.052 7.584 1.00 11.23 C ANISOU 496 C LYS A 60 2189 1366 712 -88 -530 127 C ATOM 497 O LYS A 60 22.030 41.457 7.512 1.00 13.73 O ANISOU 497 O LYS A 60 2463 1348 1405 -312 -15 325 O ATOM 498 CB LYS A 60 19.805 40.049 5.531 1.00 14.32 C ANISOU 498 CB LYS A 60 3219 1535 685 -1125 -540 402 C ATOM 499 CG LYS A 60 20.736 40.795 4.581 1.00 11.68 C ANISOU 499 CG LYS A 60 2757 1120 562 -216 4 117 C ATOM 500 CD LYS A 60 20.168 40.784 3.162 1.00 13.43 C ANISOU 500 CD LYS A 60 2480 2063 561 -575 56 65 C ATOM 501 CE LYS A 60 20.965 41.756 2.285 1.00 14.03 C ANISOU 501 CE LYS A 60 2821 1965 544 -176 340 184 C ATOM 502 NZ LYS A 60 20.560 41.661 0.856 1.00 13.87 N ANISOU 502 NZ LYS A 60 3007 1610 653 -317 106 107 N ATOM 503 N ALA A 61 19.923 41.733 8.256 1.00 12.19 N ANISOU 503 N ALA A 61 2395 921 1318 154 -354 387 N ATOM 504 CA ALA A 61 20.330 43.032 8.767 1.00 12.21 C ANISOU 504 CA ALA A 61 2507 1032 1100 172 -476 358 C ATOM 505 C ALA A 61 21.316 42.867 9.930 1.00 12.00 C ANISOU 505 C ALA A 61 1717 1981 863 -312 -72 797 C ATOM 506 O ALA A 61 22.171 43.728 10.191 1.00 13.49 O ANISOU 506 O ALA A 61 1873 1735 1516 -166 -110 413 O ATOM 507 CB ALA A 61 19.099 43.790 9.223 1.00 12.68 C ANISOU 507 CB ALA A 61 2392 1075 1349 124 -694 27 C ATOM 508 N VAL A 62 21.191 41.783 10.680 1.00 11.52 N ANISOU 508 N VAL A 62 2196 1225 956 278 -157 360 N ATOM 509 CA VAL A 62 22.140 41.474 11.768 1.00 10.72 C ANISOU 509 CA VAL A 62 1828 1354 892 198 58 478 C ATOM 510 C VAL A 62 23.487 41.126 11.153 1.00 11.24 C ANISOU 510 C VAL A 62 1683 1381 1208 -258 90 -93 C ATOM 511 O VAL A 62 24.577 41.618 11.490 1.00 12.59 O ANISOU 511 O VAL A 62 1893 1228 1662 -445 -76 383 O ATOM 512 CB VAL A 62 21.700 40.282 12.639 1.00 11.83 C ANISOU 512 CB VAL A 62 1823 1783 888 28 -11 644 C ATOM 513 CG1 VAL A 62 22.683 40.032 13.764 1.00 14.34 C ANISOU 513 CG1 VAL A 62 2760 1579 1111 -179 -623 590 C ATOM 514 CG2 VAL A 62 20.299 40.597 13.202 1.00 12.55 C ANISOU 514 CG2 VAL A 62 1939 1426 1404 -660 332 -592 C ATOM 515 N ARG A 63 23.444 40.285 10.106 1.00 13.39 N ANISOU 515 N ARG A 63 2246 1255 1587 343 -101 -290 N ATOM 516 CA ARG A 63 24.704 39.774 9.501 1.00 13.30 C ANISOU 516 CA ARG A 63 2384 609 2061 -47 461 33 C ATOM 517 C ARG A 63 25.491 40.925 8.888 1.00 15.10 C ANISOU 517 C ARG A 63 2060 1312 2366 -527 -780 848 C ATOM 518 O ARG A 63 26.737 40.800 8.845 1.00 16.42 O ANISOU 518 O ARG A 63 2193 1825 2219 -154 281 319 O ATOM 519 CB ARG A 63 24.469 38.646 8.500 1.00 12.04 C ANISOU 519 CB ARG A 63 2061 907 1606 40 477 60 C ATOM 520 CG ARG A 63 23.696 37.480 9.096 1.00 12.83 C ANISOU 520 CG ARG A 63 1937 738 2199 -74 -157 257 C ATOM 521 CD ARG A 63 23.609 36.279 8.162 1.00 15.10 C ANISOU 521 CD ARG A 63 2326 1326 2087 -431 62 -90 C ATOM 522 NE ARG A 63 22.921 35.205 8.911 1.00 13.31 N ANISOU 522 NE ARG A 63 2445 892 1720 -252 -215 -110 N ATOM 523 CZ ARG A 63 21.703 34.756 8.654 1.00 12.06 C ANISOU 523 CZ ARG A 63 2124 1165 1295 -89 202 96 C ATOM 524 NH1 ARG A 63 21.005 35.242 7.626 1.00 10.97 N ANISOU 524 NH1 ARG A 63 1807 1005 1357 -8 409 263 N ATOM 525 NH2 ARG A 63 21.223 33.799 9.453 1.00 11.03 N ANISOU 525 NH2 ARG A 63 2342 1072 775 4 197 -94 N ATOM 526 N GLU A 64 24.814 41.986 8.445 1.00 13.92 N ANISOU 526 N GLU A 64 2531 998 1762 -270 -54 541 N ATOM 527 CA GLU A 64 25.510 43.156 7.853 1.00 14.97 C ANISOU 527 CA GLU A 64 2609 1304 1774 -505 -159 723 C ATOM 528 C GLU A 64 25.829 44.231 8.850 1.00 12.71 C ANISOU 528 C GLU A 64 2076 1080 1674 -355 -260 891 C ATOM 529 O GLU A 64 26.499 45.221 8.490 1.00 19.03 O ANISOU 529 O GLU A 64 3120 2107 2004 -1491 -178 816 O ATOM 530 CB GLU A 64 24.642 43.766 6.748 1.00 16.78 C ANISOU 530 CB GLU A 64 3197 1922 1256 -577 -169 743 C ATOM 531 CG GLU A 64 24.500 42.773 5.588 1.00 23.88 C ANISOU 531 CG GLU A 64 4793 2760 1519 -1386 -104 299 C ATOM 532 CD GLU A 64 23.745 43.383 4.432 1.00 26.90 C ANISOU 532 CD GLU A 64 5768 2610 1841 -1996 -985 263 C ATOM 533 OE1 GLU A 64 22.920 44.287 4.670 1.00 33.64 O ANISOU 533 OE1 GLU A 64 8165 1662 2954 -1107 -1616 748 O ATOM 534 OE2 GLU A 64 23.995 42.908 3.296 1.00 35.49 O ANISOU 534 OE2 GLU A 64 6952 4731 1803 -2039 -1212 -295 O ATOM 535 N LEU A 65 25.398 44.119 10.105 1.00 13.76 N ANISOU 535 N LEU A 65 1985 1375 1870 -437 29 635 N ATOM 536 CA LEU A 65 25.676 45.198 11.050 1.00 13.96 C ANISOU 536 CA LEU A 65 1996 1457 1851 -571 46 610 C ATOM 537 C LEU A 65 27.155 45.148 11.457 1.00 15.87 C ANISOU 537 C LEU A 65 2290 1955 1784 -683 -378 1071 C ATOM 538 O LEU A 65 27.621 44.093 11.873 1.00 15.65 O ANISOU 538 O LEU A 65 2446 1893 1608 -129 -76 419 O ATOM 539 CB LEU A 65 24.773 45.075 12.283 1.00 17.07 C ANISOU 539 CB LEU A 65 2818 1744 1922 -679 389 630 C ATOM 540 CG LEU A 65 24.823 46.214 13.294 1.00 16.97 C ANISOU 540 CG LEU A 65 3076 1733 1640 204 -127 740 C ATOM 541 CD1 LEU A 65 24.249 47.518 12.752 1.00 22.35 C ANISOU 541 CD1 LEU A 65 3463 2141 2887 804 464 1227 C ATOM 542 CD2 LEU A 65 24.061 45.914 14.578 1.00 18.57 C ANISOU 542 CD2 LEU A 65 2675 3236 1146 -387 -661 699 C ATOM 543 N SER A 66 27.851 46.278 11.324 1.00 16.40 N ANISOU 543 N SER A 66 2425 2080 1724 -1015 -220 445 N ATOM 544 CA SER A 66 29.272 46.331 11.644 1.00 18.91 C ANISOU 544 CA SER A 66 2384 1605 3194 -520 -377 473 C ATOM 545 C SER A 66 29.568 45.799 13.051 1.00 18.07 C ANISOU 545 C SER A 66 1692 1983 3191 -657 -459 455 C ATOM 546 O SER A 66 29.017 46.262 14.053 1.00 18.85 O ANISOU 546 O SER A 66 2273 1618 3271 -1097 -41 515 O ATOM 547 CB SER A 66 29.860 47.741 11.518 1.00 26.64 C ANISOU 547 CB SER A 66 2794 2502 4826 -1504 -599 1274 C ATOM 548 OG SER A 66 31.237 47.733 11.843 1.00 37.68 O ANISOU 548 OG SER A 66 2460 3350 8507 -1375 -288 2624 O ATOM 549 N GLY A 67 30.503 44.840 13.085 1.00 19.28 N ANISOU 549 N GLY A 67 1839 1629 3856 -797 -19 1153 N ATOM 550 CA GLY A 67 30.913 44.141 14.286 1.00 17.70 C ANISOU 550 CA GLY A 67 2015 1392 3316 -740 -23 634 C ATOM 551 C GLY A 67 30.034 42.955 14.678 1.00 14.86 C ANISOU 551 C GLY A 67 1622 1534 2490 -614 156 504 C ATOM 552 O GLY A 67 30.438 42.232 15.619 1.00 15.10 O ANISOU 552 O GLY A 67 1615 1417 2707 -483 -4 476 O ATOM 553 N TRP A 68 28.891 42.747 14.044 1.00 12.77 N ANISOU 553 N TRP A 68 1607 1117 2129 -279 194 83 N ATOM 554 CA TRP A 68 27.947 41.728 14.439 1.00 10.81 C ANISOU 554 CA TRP A 68 1295 949 1864 -82 262 -153 C ATOM 555 C TRP A 68 28.036 40.496 13.570 1.00 8.88 C ANISOU 555 C TRP A 68 1217 1115 1044 -233 308 59 C ATOM 556 O TRP A 68 27.202 39.563 13.631 1.00 12.08 O ANISOU 556 O TRP A 68 1623 907 2062 -336 213 44 O ATOM 557 CB TRP A 68 26.525 42.352 14.475 1.00 11.26 C ANISOU 557 CB TRP A 68 1407 1196 1674 98 -79 -96 C ATOM 558 CG TRP A 68 26.368 43.173 15.741 1.00 11.09 C ANISOU 558 CG TRP A 68 1364 1077 1773 21 260 -37 C ATOM 559 CD1 TRP A 68 27.089 44.323 16.016 1.00 10.66 C ANISOU 559 CD1 TRP A 68 1722 993 1334 -23 142 98 C ATOM 560 CD2 TRP A 68 25.485 42.943 16.851 1.00 12.52 C ANISOU 560 CD2 TRP A 68 1655 1468 1634 -186 202 56 C ATOM 561 NE1 TRP A 68 26.668 44.780 17.260 1.00 13.12 N ANISOU 561 NE1 TRP A 68 1712 1440 1833 -225 622 -270 N ATOM 562 CE2 TRP A 68 25.699 43.969 17.793 1.00 11.22 C ANISOU 562 CE2 TRP A 68 1389 1185 1689 81 251 143 C ATOM 563 CE3 TRP A 68 24.521 41.942 17.140 1.00 10.60 C ANISOU 563 CE3 TRP A 68 1285 1433 1311 67 257 -108 C ATOM 564 CZ2 TRP A 68 25.008 44.051 19.007 1.00 11.39 C ANISOU 564 CZ2 TRP A 68 1749 863 1715 0 395 254 C ATOM 565 CZ3 TRP A 68 23.835 42.026 18.343 1.00 10.01 C ANISOU 565 CZ3 TRP A 68 1395 1143 1265 300 288 -207 C ATOM 566 CH2 TRP A 68 24.073 43.065 19.263 1.00 9.40 C ANISOU 566 CH2 TRP A 68 1503 706 1363 137 225 88 C ATOM 567 N GLN A 69 29.042 40.391 12.709 1.00 11.82 N ANISOU 567 N GLN A 69 1572 2289 629 43 337 97 N ATOM 568 CA GLN A 69 29.070 39.367 11.691 1.00 13.39 C ANISOU 568 CA GLN A 69 2551 2230 306 132 357 270 C ATOM 569 C GLN A 69 29.285 37.967 12.245 1.00 14.62 C ANISOU 569 C GLN A 69 2180 2236 1138 283 45 333 C ATOM 570 O GLN A 69 29.091 37.015 11.481 1.00 14.55 O ANISOU 570 O GLN A 69 2445 2135 947 168 -76 486 O ATOM 571 CB GLN A 69 30.186 39.660 10.643 1.00 16.23 C ANISOU 571 CB GLN A 69 2530 3043 594 309 612 225 C ATOM 572 CG GLN A 69 31.577 39.639 11.273 1.00 19.66 C ANISOU 572 CG GLN A 69 2454 3043 1974 345 418 160 C ATOM 573 CD GLN A 69 32.082 41.009 11.711 1.00 21.81 C ANISOU 573 CD GLN A 69 2092 3459 2737 -370 1137 44 C ATOM 574 OE1 GLN A 69 31.363 41.854 12.263 1.00 23.31 O ANISOU 574 OE1 GLN A 69 2816 2744 3297 -601 1491 53 O ATOM 575 NE2 GLN A 69 33.362 41.233 11.431 1.00 27.47 N ANISOU 575 NE2 GLN A 69 2019 4830 3588 -399 1064 1484 N ATOM 576 N TYR A 70 29.687 37.891 13.528 1.00 10.53 N ANISOU 576 N TYR A 70 1535 1438 1027 -132 348 414 N ATOM 577 CA TYR A 70 29.880 36.546 14.118 1.00 10.35 C ANISOU 577 CA TYR A 70 971 1376 1587 24 312 494 C ATOM 578 C TYR A 70 28.723 36.194 15.047 1.00 8.38 C ANISOU 578 C TYR A 70 844 1075 1267 -112 97 293 C ATOM 579 O TYR A 70 28.698 35.136 15.703 1.00 12.05 O ANISOU 579 O TYR A 70 1404 1335 1839 59 565 606 O ATOM 580 CB TYR A 70 31.202 36.411 14.877 1.00 11.13 C ANISOU 580 CB TYR A 70 776 1540 1912 316 393 -7 C ATOM 581 CG TYR A 70 32.381 36.690 13.963 1.00 14.31 C ANISOU 581 CG TYR A 70 1018 2976 1444 -246 292 -70 C ATOM 582 CD1 TYR A 70 32.811 35.756 13.037 1.00 16.08 C ANISOU 582 CD1 TYR A 70 1913 3134 1061 -64 720 204 C ATOM 583 CD2 TYR A 70 33.067 37.886 14.041 1.00 16.56 C ANISOU 583 CD2 TYR A 70 2100 2929 1264 -586 564 525 C ATOM 584 CE1 TYR A 70 33.892 36.044 12.221 1.00 20.60 C ANISOU 584 CE1 TYR A 70 2214 3454 2158 245 1358 527 C ATOM 585 CE2 TYR A 70 34.150 38.173 13.219 1.00 21.52 C ANISOU 585 CE2 TYR A 70 2431 3605 2141 -733 1021 679 C ATOM 586 CZ TYR A 70 34.570 37.236 12.289 1.00 21.27 C ANISOU 586 CZ TYR A 70 2243 3780 2057 -72 1146 975 C ATOM 587 OH TYR A 70 35.666 37.537 11.479 1.00 30.10 O ANISOU 587 OH TYR A 70 3125 4822 3492 -537 2153 811 O ATOM 588 N VAL A 71 27.711 37.064 15.087 1.00 9.86 N ANISOU 588 N VAL A 71 769 1296 1681 -62 168 195 N ATOM 589 CA VAL A 71 26.585 36.725 16.012 1.00 8.00 C ANISOU 589 CA VAL A 71 863 862 1313 -33 94 48 C ATOM 590 C VAL A 71 25.700 35.676 15.396 1.00 7.61 C ANISOU 590 C VAL A 71 909 1012 969 -92 175 19 C ATOM 591 O VAL A 71 25.152 35.945 14.297 1.00 11.85 O ANISOU 591 O VAL A 71 1609 1447 1447 -466 -358 436 O ATOM 592 CB VAL A 71 25.792 37.995 16.346 1.00 8.24 C ANISOU 592 CB VAL A 71 1036 754 1340 3 61 211 C ATOM 593 CG1 VAL A 71 24.566 37.680 17.166 1.00 10.44 C ANISOU 593 CG1 VAL A 71 1473 539 1954 311 618 378 C ATOM 594 CG2 VAL A 71 26.736 38.973 17.065 1.00 9.54 C ANISOU 594 CG2 VAL A 71 1525 513 1586 146 -574 370 C ATOM 595 N PRO A 72 25.510 34.485 15.935 1.00 9.45 N ANISOU 595 N PRO A 72 1130 1242 1219 -504 -28 275 N ATOM 596 CA PRO A 72 24.672 33.452 15.282 1.00 9.01 C ANISOU 596 CA PRO A 72 1131 799 1495 170 -328 -88 C ATOM 597 C PRO A 72 23.189 33.844 15.366 1.00 6.62 C ANISOU 597 C PRO A 72 1051 520 946 -155 -137 -83 C ATOM 598 O PRO A 72 22.712 34.228 16.429 1.00 8.98 O ANISOU 598 O PRO A 72 1446 1114 851 -56 -78 -191 O ATOM 599 CB PRO A 72 24.949 32.154 16.041 1.00 10.14 C ANISOU 599 CB PRO A 72 1757 824 1271 249 -689 -261 C ATOM 600 CG PRO A 72 25.428 32.635 17.370 1.00 9.21 C ANISOU 600 CG PRO A 72 2147 550 802 -96 142 -329 C ATOM 601 CD PRO A 72 25.999 34.035 17.259 1.00 9.73 C ANISOU 601 CD PRO A 72 1916 828 951 -390 -54 -66 C ATOM 602 N VAL A 73 22.565 33.773 14.200 1.00 8.28 N ANISOU 602 N VAL A 73 1182 1211 751 269 -78 99 N ATOM 603 CA VAL A 73 21.169 34.203 14.110 1.00 7.41 C ANISOU 603 CA VAL A 73 1278 653 884 316 -236 -143 C ATOM 604 C VAL A 73 20.461 33.306 13.090 1.00 8.21 C ANISOU 604 C VAL A 73 1350 982 788 62 0 -296 C ATOM 605 O VAL A 73 21.042 32.796 12.107 1.00 7.75 O ANISOU 605 O VAL A 73 1596 842 508 18 102 38 O ATOM 606 CB VAL A 73 21.117 35.681 13.714 1.00 9.77 C ANISOU 606 CB VAL A 73 1851 640 1222 287 275 -31 C ATOM 607 CG1 VAL A 73 21.772 35.934 12.347 1.00 12.69 C ANISOU 607 CG1 VAL A 73 2554 1292 976 -42 15 155 C ATOM 608 CG2 VAL A 73 19.682 36.220 13.704 1.00 10.72 C ANISOU 608 CG2 VAL A 73 2077 293 1703 458 -275 -216 C ATOM 609 N THR A 74 19.161 33.086 13.345 1.00 8.22 N ANISOU 609 N THR A 74 1262 1233 628 102 -131 -195 N ATOM 610 CA THR A 74 18.322 32.395 12.374 1.00 7.37 C ANISOU 610 CA THR A 74 1338 805 655 475 -501 74 C ATOM 611 C THR A 74 16.881 32.850 12.547 1.00 8.34 C ANISOU 611 C THR A 74 1247 1146 775 316 -243 194 C ATOM 612 O THR A 74 16.592 33.489 13.566 1.00 9.62 O ANISOU 612 O THR A 74 1033 1661 960 -187 40 -142 O ATOM 613 CB THR A 74 18.531 30.866 12.482 1.00 8.13 C ANISOU 613 CB THR A 74 2050 794 243 387 -17 183 C ATOM 614 OG1 THR A 74 18.092 30.274 11.232 1.00 8.68 O ANISOU 614 OG1 THR A 74 1299 1280 719 124 -87 -290 O ATOM 615 CG2 THR A 74 17.710 30.218 13.548 1.00 11.34 C ANISOU 615 CG2 THR A 74 2117 1417 774 37 232 282 C ATOM 616 N CYS A 75 16.077 32.549 11.522 1.00 8.05 N ANISOU 616 N CYS A 75 1281 819 957 137 -308 147 N ATOM 617 CA CYS A 75 14.689 33.050 11.555 1.00 7.92 C ANISOU 617 CA CYS A 75 1240 1331 438 13 -349 62 C ATOM 618 C CYS A 75 13.691 31.935 11.698 1.00 7.10 C ANISOU 618 C CYS A 75 1269 994 436 160 175 -581 C ATOM 619 O CYS A 75 13.954 30.722 11.674 1.00 11.26 O ANISOU 619 O CYS A 75 1825 1003 1448 370 -34 -487 O ATOM 620 CB CYS A 75 14.434 33.857 10.267 1.00 9.12 C ANISOU 620 CB CYS A 75 1495 1510 459 -184 -867 15 C ATOM 621 SG CYS A 75 15.618 35.205 9.993 1.00 11.46 S ANISOU 621 SG CYS A 75 1848 1268 1239 -85 -59 157 S ATOM 622 N MET A 76 12.440 32.424 11.875 1.00 7.24 N ANISOU 622 N MET A 76 1253 998 499 160 73 -50 N ATOM 623 CA MET A 76 11.313 31.499 11.977 1.00 8.66 C ANISOU 623 CA MET A 76 1213 1125 951 79 3 -240 C ATOM 624 C MET A 76 10.030 32.241 11.616 1.00 9.07 C ANISOU 624 C MET A 76 1311 749 1385 -23 -49 -24 C ATOM 625 O MET A 76 9.970 33.476 11.720 1.00 9.49 O ANISOU 625 O MET A 76 1851 810 946 -51 -303 147 O ATOM 626 CB MET A 76 11.239 30.985 13.436 1.00 10.22 C ANISOU 626 CB MET A 76 1342 1169 1373 -148 139 293 C ATOM 627 CG MET A 76 11.203 32.050 14.528 1.00 17.40 C ANISOU 627 CG MET A 76 3282 2439 889 1403 1307 47 C ATOM 628 SD MET A 76 11.617 31.429 16.156 1.00 13.52 S ANISOU 628 SD MET A 76 1876 1706 1555 -67 -147 35 S ATOM 629 CE MET A 76 11.110 32.927 17.064 1.00 14.50 C ANISOU 629 CE MET A 76 3470 1111 929 -653 -693 -38 C ATOM 630 N GLN A 77 8.993 31.477 11.278 1.00 8.81 N ANISOU 630 N GLN A 77 1101 968 1279 -37 111 8 N ATOM 631 CA GLN A 77 7.707 32.029 10.993 1.00 8.35 C ANISOU 631 CA GLN A 77 1165 671 1338 88 262 -364 C ATOM 632 C GLN A 77 6.965 32.186 12.336 1.00 8.16 C ANISOU 632 C GLN A 77 1363 1016 722 904 -219 398 C ATOM 633 O GLN A 77 6.824 31.235 13.090 1.00 10.57 O ANISOU 633 O GLN A 77 1947 823 1247 186 -68 242 O ATOM 634 CB AGLN A 77 6.883 31.143 10.053 0.61 11.88 C ANISOU 634 CB AGLN A 77 1676 1367 1470 334 -519 -420 C ATOM 635 CB BGLN A 77 6.905 31.080 10.094 0.39 12.96 C ANISOU 635 CB BGLN A 77 1677 1599 1648 112 -444 -622 C ATOM 636 CG AGLN A 77 5.746 31.980 9.475 0.61 16.18 C ANISOU 636 CG AGLN A 77 2514 1813 1820 876 -752 -169 C ATOM 637 CG BGLN A 77 5.739 31.743 9.386 0.39 16.69 C ANISOU 637 CG BGLN A 77 2506 1705 2132 509 -926 -616 C ATOM 638 CD AGLN A 77 5.248 31.292 8.215 0.61 20.10 C ANISOU 638 CD AGLN A 77 2424 2354 2858 731 -1626 -562 C ATOM 639 CD BGLN A 77 6.236 32.595 8.231 0.39 16.18 C ANISOU 639 CD BGLN A 77 2225 1952 1969 637 -893 -633 C ATOM 640 OE1AGLN A 77 4.229 30.633 8.312 0.61 31.66 O ANISOU 640 OE1AGLN A 77 2776 2888 6364 207 -1681 -996 O ATOM 641 OE1BGLN A 77 6.221 33.822 8.336 0.39 20.64 O ANISOU 641 OE1BGLN A 77 3381 1944 2517 -277 -99 -790 O ATOM 642 NE2AGLN A 77 5.971 31.428 7.111 0.61 26.86 N ANISOU 642 NE2AGLN A 77 3536 4591 2077 874 -1637 -1488 N ATOM 643 NE2BGLN A 77 6.672 31.962 7.152 0.39 17.24 N ANISOU 643 NE2BGLN A 77 516 2720 3313 -966 151 -1696 N ATOM 644 N GLU A 78 6.431 33.402 12.504 1.00 8.49 N ANISOU 644 N GLU A 78 1074 893 1259 560 72 -51 N ATOM 645 CA GLU A 78 5.576 33.680 13.680 1.00 8.08 C ANISOU 645 CA GLU A 78 1522 472 1077 -315 193 -449 C ATOM 646 C GLU A 78 4.243 32.987 13.414 1.00 7.52 C ANISOU 646 C GLU A 78 1229 524 1105 5 14 -237 C ATOM 647 O GLU A 78 3.848 32.800 12.237 1.00 12.09 O ANISOU 647 O GLU A 78 1531 1851 1212 -137 -270 -335 O ATOM 648 CB GLU A 78 5.472 35.187 13.943 1.00 7.50 C ANISOU 648 CB GLU A 78 1296 408 1144 -15 -57 -205 C ATOM 649 CG GLU A 78 4.375 35.617 14.919 1.00 8.90 C ANISOU 649 CG GLU A 78 1685 783 913 271 -5 -127 C ATOM 650 CD GLU A 78 4.628 35.255 16.386 1.00 10.56 C ANISOU 650 CD GLU A 78 2109 983 921 -213 -230 -123 C ATOM 651 OE1 GLU A 78 4.573 34.016 16.621 1.00 10.56 O ANISOU 651 OE1 GLU A 78 1651 1060 1302 -19 -297 176 O ATOM 652 OE2 GLU A 78 4.827 36.151 17.257 1.00 9.84 O ANISOU 652 OE2 GLU A 78 1460 1195 1084 4 -96 -338 O ATOM 653 N MET A 79 3.529 32.578 14.462 1.00 9.78 N ANISOU 653 N MET A 79 1140 1211 1367 -196 166 -170 N ATOM 654 CA MET A 79 2.177 32.084 14.292 1.00 12.74 C ANISOU 654 CA MET A 79 1111 2383 1348 -311 111 -172 C ATOM 655 C MET A 79 1.258 33.112 13.659 1.00 12.82 C ANISOU 655 C MET A 79 966 2187 1718 -495 87 -86 C ATOM 656 O MET A 79 1.484 34.335 13.821 1.00 15.52 O ANISOU 656 O MET A 79 1941 2256 1699 -415 -710 -391 O ATOM 657 CB MET A 79 1.538 31.903 15.667 1.00 15.26 C ANISOU 657 CB MET A 79 1859 2326 1612 -1278 268 59 C ATOM 658 CG MET A 79 2.006 30.763 16.507 1.00 17.33 C ANISOU 658 CG MET A 79 2016 2818 1751 -953 17 252 C ATOM 659 SD MET A 79 1.307 30.996 18.158 1.00 13.66 S ANISOU 659 SD MET A 79 2017 1497 1676 -682 -170 127 S ATOM 660 CE MET A 79 -0.410 30.678 17.802 1.00 10.77 C ANISOU 660 CE MET A 79 2005 343 1746 -736 62 -122 C ATOM 661 N ASP A 80 0.231 32.605 12.999 1.00 13.87 N ANISOU 661 N ASP A 80 830 2229 2212 -217 1 -531 N ATOM 662 CA ASP A 80 -0.785 33.476 12.451 1.00 14.88 C ANISOU 662 CA ASP A 80 1232 2739 1682 92 -16 -427 C ATOM 663 C ASP A 80 -1.946 33.554 13.436 1.00 15.77 C ANISOU 663 C ASP A 80 1060 2331 2603 -97 266 -724 C ATOM 664 O ASP A 80 -2.772 32.621 13.495 1.00 19.75 O ANISOU 664 O ASP A 80 2169 2331 3003 -500 630 -249 O ATOM 665 CB ASP A 80 -1.280 32.911 11.119 1.00 19.04 C ANISOU 665 CB ASP A 80 1537 3594 2103 -397 -313 -722 C ATOM 666 CG ASP A 80 -2.036 33.907 10.278 1.00 24.17 C ANISOU 666 CG ASP A 80 3052 4532 1599 53 -597 -527 C ATOM 667 OD1 ASP A 80 -2.287 35.046 10.738 1.00 30.24 O ANISOU 667 OD1 ASP A 80 4436 4299 2755 708 -1697 -450 O ATOM 668 OD2 ASP A 80 -2.377 33.539 9.134 1.00 32.08 O ANISOU 668 OD2 ASP A 80 3729 6821 1641 340 -736 -1072 O ATOM 669 N VAL A 81 -2.037 34.615 14.210 1.00 13.62 N ANISOU 669 N VAL A 81 1209 1837 2130 767 -259 -187 N ATOM 670 CA VAL A 81 -3.136 34.767 15.146 1.00 11.74 C ANISOU 670 CA VAL A 81 1151 1197 2111 527 -249 -108 C ATOM 671 C VAL A 81 -4.170 35.754 14.648 1.00 11.97 C ANISOU 671 C VAL A 81 980 1643 1925 495 -207 238 C ATOM 672 O VAL A 81 -3.860 36.828 14.125 1.00 16.05 O ANISOU 672 O VAL A 81 1821 1915 2361 376 -447 778 O ATOM 673 CB VAL A 81 -2.559 35.267 16.496 1.00 14.86 C ANISOU 673 CB VAL A 81 1531 2181 1934 889 -498 -59 C ATOM 674 CG1 VAL A 81 -3.669 35.785 17.414 1.00 13.73 C ANISOU 674 CG1 VAL A 81 1822 1072 2323 311 -165 -341 C ATOM 675 CG2 VAL A 81 -1.734 34.103 17.067 1.00 11.97 C ANISOU 675 CG2 VAL A 81 1253 1127 2170 80 -402 13 C ATOM 676 N THR A 82 -5.433 35.387 14.793 1.00 16.28 N ANISOU 676 N THR A 82 1017 1950 3219 285 -741 223 N ATOM 677 CA THR A 82 -6.568 36.211 14.439 1.00 15.60 C ANISOU 677 CA THR A 82 943 1329 3654 262 -337 500 C ATOM 678 C THR A 82 -6.502 37.507 15.228 1.00 16.46 C ANISOU 678 C THR A 82 1528 1577 3150 12 -114 494 C ATOM 679 O THR A 82 -6.506 37.493 16.461 1.00 19.03 O ANISOU 679 O THR A 82 1578 2502 3151 665 103 475 O ATOM 680 CB THR A 82 -7.862 35.443 14.799 1.00 21.38 C ANISOU 680 CB THR A 82 1052 1703 5369 81 5 247 C ATOM 681 OG1 THR A 82 -7.822 34.172 14.126 1.00 22.19 O ANISOU 681 OG1 THR A 82 1612 2106 4713 -266 -1155 -42 O ATOM 682 CG2 THR A 82 -9.094 36.196 14.336 1.00 27.68 C ANISOU 682 CG2 THR A 82 924 3828 5766 765 -143 -133 C ATOM 683 N GLY A 83 -6.404 38.626 14.526 1.00 16.88 N ANISOU 683 N GLY A 83 1533 1309 3571 324 303 453 N ATOM 684 CA GLY A 83 -6.206 39.897 15.163 1.00 18.67 C ANISOU 684 CA GLY A 83 1567 1385 4142 779 -108 150 C ATOM 685 C GLY A 83 -4.760 40.180 15.494 1.00 20.86 C ANISOU 685 C GLY A 83 1759 1865 4303 409 -265 58 C ATOM 686 O GLY A 83 -4.460 41.251 16.060 1.00 22.83 O ANISOU 686 O GLY A 83 2553 1800 4321 464 -962 289 O ATOM 687 N GLY A 84 -3.840 39.270 15.169 1.00 16.80 N ANISOU 687 N GLY A 84 1061 2064 3259 29 254 472 N ATOM 688 CA GLY A 84 -2.454 39.488 15.595 1.00 14.49 C ANISOU 688 CA GLY A 84 1261 2060 2185 -312 315 434 C ATOM 689 C GLY A 84 -1.918 40.640 14.763 1.00 13.01 C ANISOU 689 C GLY A 84 1355 1076 2512 -26 -333 313 C ATOM 690 O GLY A 84 -2.416 40.981 13.679 1.00 17.13 O ANISOU 690 O GLY A 84 1748 1420 3341 -151 -954 986 O ATOM 691 N LEU A 85 -0.919 41.295 15.273 1.00 14.38 N ANISOU 691 N LEU A 85 1135 1453 2876 -79 -233 153 N ATOM 692 CA LEU A 85 -0.351 42.456 14.597 1.00 13.22 C ANISOU 692 CA LEU A 85 1653 1098 2273 -210 105 -524 C ATOM 693 C LEU A 85 0.218 42.039 13.240 1.00 12.48 C ANISOU 693 C LEU A 85 1277 1600 1867 477 -485 -356 C ATOM 694 O LEU A 85 1.021 41.099 13.179 1.00 14.54 O ANISOU 694 O LEU A 85 2104 1456 1965 717 -187 -205 O ATOM 695 CB LEU A 85 0.733 43.084 15.482 1.00 13.80 C ANISOU 695 CB LEU A 85 2253 416 2574 117 -395 -811 C ATOM 696 CG LEU A 85 1.362 44.372 14.960 1.00 12.68 C ANISOU 696 CG LEU A 85 1132 844 2842 232 -308 -414 C ATOM 697 CD1 LEU A 85 0.313 45.491 14.907 1.00 18.59 C ANISOU 697 CD1 LEU A 85 2005 942 4114 605 -984 -71 C ATOM 698 CD2 LEU A 85 2.526 44.873 15.803 1.00 12.22 C ANISOU 698 CD2 LEU A 85 1595 1070 1977 46 -378 -147 C ATOM 699 N LYS A 86 -0.132 42.717 12.177 1.00 15.78 N ANISOU 699 N LYS A 86 2094 1533 2369 302 -262 303 N ATOM 700 CA LYS A 86 0.362 42.387 10.848 1.00 15.04 C ANISOU 700 CA LYS A 86 1856 1789 2070 -111 -459 372 C ATOM 701 C LYS A 86 1.756 42.912 10.578 1.00 13.93 C ANISOU 701 C LYS A 86 1762 1635 1897 -29 -693 79 C ATOM 702 O LYS A 86 2.183 43.851 11.236 1.00 14.92 O ANISOU 702 O LYS A 86 1902 1325 2443 253 -876 -20 O ATOM 703 CB LYS A 86 -0.624 43.005 9.819 1.00 18.46 C ANISOU 703 CB LYS A 86 1790 2603 2622 111 -768 296 C ATOM 704 CG LYS A 86 -2.008 42.405 10.000 1.00 21.80 C ANISOU 704 CG LYS A 86 1909 2788 3585 -26 -823 861 C ATOM 705 CD LYS A 86 -2.154 41.099 9.236 1.00 32.81 C ANISOU 705 CD LYS A 86 3539 4268 4659 -1319 -1155 -435 C ATOM 706 CE LYS A 86 -3.587 41.077 8.689 1.00 35.12 C ANISOU 706 CE LYS A 86 3712 4209 5422 -414 -1590 -661 C ATOM 707 NZ LYS A 86 -4.098 42.488 8.610 1.00 50.57 N ANISOU 707 NZ LYS A 86 6485 5601 7129 2218 -175 -1554 N ATOM 708 N LYS A 87 2.444 42.334 9.592 1.00 13.04 N ANISOU 708 N LYS A 87 1844 1223 1886 212 -503 491 N ATOM 709 CA LYS A 87 3.729 42.866 9.081 1.00 14.66 C ANISOU 709 CA LYS A 87 1820 1791 1958 -7 -648 659 C ATOM 710 C LYS A 87 4.690 43.154 10.213 1.00 13.70 C ANISOU 710 C LYS A 87 2012 758 2434 474 -944 419 C ATOM 711 O LYS A 87 5.320 44.224 10.289 1.00 13.00 O ANISOU 711 O LYS A 87 2176 1216 1547 70 -336 344 O ATOM 712 CB LYS A 87 3.464 44.111 8.220 1.00 13.76 C ANISOU 712 CB LYS A 87 1429 1851 1949 -16 -512 724 C ATOM 713 CG LYS A 87 2.594 43.751 6.990 1.00 17.63 C ANISOU 713 CG LYS A 87 2759 1990 1951 73 -951 723 C ATOM 714 CD LYS A 87 2.394 44.919 6.047 1.00 25.49 C ANISOU 714 CD LYS A 87 3540 3025 3121 441 -1423 1700 C ATOM 715 CE LYS A 87 1.372 44.634 4.954 1.00 35.70 C ANISOU 715 CE LYS A 87 3837 5577 4150 104 -2320 2537 C ATOM 716 NZ LYS A 87 -0.002 44.364 5.497 1.00 48.22 N ANISOU 716 NZ LYS A 87 3953 6877 7490 -1097 -2441 4623 N ATOM 717 N CYS A 88 4.861 42.154 11.078 1.00 12.77 N ANISOU 717 N CYS A 88 1901 1134 1816 571 -340 506 N ATOM 718 CA CYS A 88 5.616 42.347 12.282 1.00 12.40 C ANISOU 718 CA CYS A 88 1432 1445 1835 201 -193 508 C ATOM 719 C CYS A 88 6.818 41.433 12.330 1.00 9.15 C ANISOU 719 C CYS A 88 1473 1187 818 73 -44 392 C ATOM 720 O CYS A 88 6.758 40.231 12.073 1.00 11.81 O ANISOU 720 O CYS A 88 1814 1234 1438 60 -231 372 O ATOM 721 CB CYS A 88 4.716 42.038 13.469 1.00 10.02 C ANISOU 721 CB CYS A 88 1521 553 1734 94 -54 -118 C ATOM 722 SG CYS A 88 5.392 42.226 15.122 1.00 12.15 S ANISOU 722 SG CYS A 88 1735 1023 1859 -13 -361 154 S ATOM 723 N ILE A 89 7.891 42.114 12.765 1.00 10.71 N ANISOU 723 N ILE A 89 1374 1469 1225 54 -157 297 N ATOM 724 CA ILE A 89 9.161 41.428 12.948 1.00 10.06 C ANISOU 724 CA ILE A 89 1585 1041 1195 144 -205 641 C ATOM 725 C ILE A 89 9.483 41.418 14.447 1.00 9.78 C ANISOU 725 C ILE A 89 1564 1102 1049 350 -32 286 C ATOM 726 O ILE A 89 9.469 42.482 15.049 1.00 11.88 O ANISOU 726 O ILE A 89 1825 1021 1669 465 -85 194 O ATOM 727 CB ILE A 89 10.310 42.097 12.188 1.00 9.98 C ANISOU 727 CB ILE A 89 1619 967 1207 540 288 241 C ATOM 728 CG1 ILE A 89 10.091 42.115 10.675 1.00 14.50 C ANISOU 728 CG1 ILE A 89 2574 1735 1201 691 218 644 C ATOM 729 CG2 ILE A 89 11.637 41.418 12.561 1.00 12.33 C ANISOU 729 CG2 ILE A 89 1564 1232 1890 464 -108 134 C ATOM 730 CD1 ILE A 89 10.771 43.287 9.991 1.00 21.54 C ANISOU 730 CD1 ILE A 89 4648 1923 1611 285 903 689 C ATOM 731 N ARG A 90 9.723 40.203 14.944 1.00 8.22 N ANISOU 731 N ARG A 90 1626 869 628 -216 -256 137 N ATOM 732 CA ARG A 90 10.076 40.110 16.366 1.00 7.91 C ANISOU 732 CA ARG A 90 1137 1192 678 -38 -260 65 C ATOM 733 C ARG A 90 11.497 39.555 16.526 1.00 9.25 C ANISOU 733 C ARG A 90 1014 1400 1102 -62 -287 -363 C ATOM 734 O ARG A 90 11.960 38.776 15.675 1.00 9.69 O ANISOU 734 O ARG A 90 1899 991 790 383 -271 33 O ATOM 735 CB ARG A 90 9.090 39.175 17.112 1.00 8.10 C ANISOU 735 CB ARG A 90 1213 1214 652 286 352 -21 C ATOM 736 CG ARG A 90 7.670 39.791 17.140 1.00 8.51 C ANISOU 736 CG ARG A 90 1249 524 1459 192 168 -302 C ATOM 737 CD ARG A 90 6.697 38.723 17.611 1.00 10.97 C ANISOU 737 CD ARG A 90 908 716 2545 -168 -315 -477 C ATOM 738 NE ARG A 90 5.339 39.115 17.951 1.00 10.10 N ANISOU 738 NE ARG A 90 1014 960 1864 142 -287 69 N ATOM 739 CZ ARG A 90 4.329 39.209 17.072 1.00 7.91 C ANISOU 739 CZ ARG A 90 1072 443 1490 231 -113 79 C ATOM 740 NH1 ARG A 90 4.527 39.004 15.755 1.00 11.49 N ANISOU 740 NH1 ARG A 90 1392 1352 1623 -58 60 -355 N ATOM 741 NH2 ARG A 90 3.119 39.533 17.478 1.00 9.20 N ANISOU 741 NH2 ARG A 90 977 858 1660 183 -66 -26 N ATOM 742 N VAL A 91 12.121 39.979 17.637 1.00 7.70 N ANISOU 742 N VAL A 91 1283 874 770 463 -371 -70 N ATOM 743 CA VAL A 91 13.453 39.452 17.944 1.00 7.83 C ANISOU 743 CA VAL A 91 1119 794 1062 93 -430 247 C ATOM 744 C VAL A 91 13.488 38.878 19.363 1.00 6.94 C ANISOU 744 C VAL A 91 1118 686 835 254 -349 -66 C ATOM 745 O VAL A 91 12.859 39.344 20.278 1.00 8.95 O ANISOU 745 O VAL A 91 1349 962 1089 168 -140 -276 O ATOM 746 CB AVAL A 91 14.536 40.524 17.782 0.62 10.92 C ANISOU 746 CB AVAL A 91 1314 414 2422 269 -211 475 C ATOM 747 CB BVAL A 91 14.565 40.511 17.876 0.38 11.80 C ANISOU 747 CB BVAL A 91 1470 822 2192 -76 -301 425 C ATOM 748 CG1AVAL A 91 14.313 41.730 18.673 0.62 10.15 C ANISOU 748 CG1AVAL A 91 2063 466 1327 188 -997 641 C ATOM 749 CG1BVAL A 91 14.292 41.537 16.790 0.38 17.93 C ANISOU 749 CG1BVAL A 91 2224 1879 2712 -237 169 1396 C ATOM 750 CG2AVAL A 91 15.915 39.927 18.078 0.62 10.80 C ANISOU 750 CG2AVAL A 91 904 1426 1773 91 360 1454 C ATOM 751 CG2BVAL A 91 14.756 41.204 19.222 0.38 12.87 C ANISOU 751 CG2BVAL A 91 2105 45 2741 -107 -638 174 C ATOM 752 N MET A 92 14.286 37.837 19.497 1.00 7.14 N ANISOU 752 N MET A 92 1205 663 843 284 -358 85 N ATOM 753 CA MET A 92 14.704 37.299 20.788 1.00 7.11 C ANISOU 753 CA MET A 92 1087 847 768 11 -227 231 C ATOM 754 C MET A 92 16.240 37.219 20.764 1.00 9.12 C ANISOU 754 C MET A 92 1074 927 1464 486 -454 -352 C ATOM 755 O MET A 92 16.825 36.338 20.124 1.00 10.69 O ANISOU 755 O MET A 92 1563 1039 1460 380 -159 -392 O ATOM 756 CB MET A 92 14.233 35.875 21.065 1.00 10.89 C ANISOU 756 CB MET A 92 2114 769 1255 -16 242 255 C ATOM 757 CG MET A 92 14.704 35.413 22.435 1.00 13.35 C ANISOU 757 CG MET A 92 2994 1281 799 -508 643 442 C ATOM 758 SD MET A 92 13.871 36.087 23.870 1.00 10.30 S ANISOU 758 SD MET A 92 1389 1183 1342 -14 9 -129 S ATOM 759 CE MET A 92 12.373 35.144 23.926 1.00 11.27 C ANISOU 759 CE MET A 92 1484 705 2092 -119 -44 -303 C ATOM 760 N MET A 93 16.905 38.167 21.450 1.00 9.08 N ANISOU 760 N MET A 93 1298 1041 1111 -1 -341 -162 N ATOM 761 CA MET A 93 18.360 38.231 21.505 1.00 11.30 C ANISOU 761 CA MET A 93 1224 1650 1420 -208 -165 461 C ATOM 762 C MET A 93 18.828 37.710 22.856 1.00 11.37 C ANISOU 762 C MET A 93 1168 2220 933 742 117 -102 C ATOM 763 O MET A 93 18.431 38.320 23.837 1.00 20.89 O ANISOU 763 O MET A 93 2011 4421 1505 1987 325 -645 O ATOM 764 CB AMET A 93 18.870 39.668 21.321 0.54 11.43 C ANISOU 764 CB AMET A 93 1598 1540 1206 -339 634 -491 C ATOM 765 CB BMET A 93 18.837 39.651 21.242 0.46 11.36 C ANISOU 765 CB BMET A 93 1662 1450 1206 -282 560 -474 C ATOM 766 CG AMET A 93 20.344 39.995 21.561 0.54 12.91 C ANISOU 766 CG AMET A 93 2040 1621 1243 -647 -157 -1292 C ATOM 767 CG BMET A 93 20.294 39.868 20.805 0.46 9.88 C ANISOU 767 CG BMET A 93 1387 2308 57 -629 -340 379 C ATOM 768 SD AMET A 93 20.824 41.730 21.215 0.54 17.43 S ANISOU 768 SD AMET A 93 1398 2050 3173 -478 -610 283 S ATOM 769 SD BMET A 93 20.706 41.625 21.093 0.46 22.11 S ANISOU 769 SD BMET A 93 2775 2055 3569 -971 -471 1140 S ATOM 770 CE AMET A 93 19.472 42.089 20.092 0.54 21.05 C ANISOU 770 CE AMET A 93 3311 1766 2922 1574 -1696 -2418 C ATOM 771 CE BMET A 93 19.419 41.918 22.324 0.46 36.38 C ANISOU 771 CE BMET A 93 1142 308 12372 279 1982 -1264 C ATOM 772 N THR A 94 19.667 36.657 22.831 1.00 8.55 N ANISOU 772 N THR A 94 1228 1174 847 88 106 -36 N ATOM 773 CA THR A 94 20.090 36.025 24.079 1.00 8.22 C ANISOU 773 CA THR A 94 1208 1000 916 -216 -11 -36 C ATOM 774 C THR A 94 21.475 36.547 24.414 1.00 10.28 C ANISOU 774 C THR A 94 1453 1581 873 -754 -33 -171 C ATOM 775 O THR A 94 22.376 36.393 23.550 1.00 10.04 O ANISOU 775 O THR A 94 1384 1351 1080 -395 130 51 O ATOM 776 CB THR A 94 20.113 34.498 23.859 1.00 9.90 C ANISOU 776 CB THR A 94 1209 964 1587 -516 13 167 C ATOM 777 OG1 THR A 94 18.858 34.042 23.389 1.00 9.49 O ANISOU 777 OG1 THR A 94 1290 1365 949 -462 -5 -37 O ATOM 778 CG2 THR A 94 20.419 33.836 25.203 1.00 10.19 C ANISOU 778 CG2 THR A 94 1115 1017 1738 -165 -346 100 C ATOM 779 N VAL A 95 21.629 37.153 25.608 1.00 9.06 N ANISOU 779 N VAL A 95 1447 1068 928 -504 -87 31 N ATOM 780 CA VAL A 95 22.895 37.833 25.910 1.00 8.75 C ANISOU 780 CA VAL A 95 1520 882 921 -328 -57 -504 C ATOM 781 C VAL A 95 23.424 37.474 27.292 1.00 10.40 C ANISOU 781 C VAL A 95 1265 1617 1069 -121 -34 -146 C ATOM 782 O VAL A 95 22.697 37.101 28.174 1.00 10.91 O ANISOU 782 O VAL A 95 1659 1514 974 -454 -19 -282 O ATOM 783 CB VAL A 95 22.754 39.378 25.908 1.00 9.63 C ANISOU 783 CB VAL A 95 1765 917 975 -322 -66 -475 C ATOM 784 CG1 VAL A 95 22.097 39.780 24.590 1.00 11.62 C ANISOU 784 CG1 VAL A 95 1663 1672 1079 -386 258 330 C ATOM 785 CG2 VAL A 95 21.974 39.868 27.112 1.00 9.50 C ANISOU 785 CG2 VAL A 95 1583 863 1165 -7 -107 -433 C ATOM 786 N GLN A 96 24.747 37.682 27.427 1.00 10.34 N ANISOU 786 N GLN A 96 1406 1433 1089 -311 -91 -453 N ATOM 787 CA GLN A 96 25.362 37.581 28.735 1.00 11.83 C ANISOU 787 CA GLN A 96 1764 1317 1413 125 -477 -483 C ATOM 788 C GLN A 96 25.332 38.982 29.348 1.00 11.45 C ANISOU 788 C GLN A 96 2370 1138 844 -366 -335 -156 C ATOM 789 O GLN A 96 25.845 39.922 28.714 1.00 13.39 O ANISOU 789 O GLN A 96 1830 1628 1629 -512 -289 194 O ATOM 790 CB GLN A 96 26.800 37.041 28.635 1.00 14.14 C ANISOU 790 CB GLN A 96 1910 2801 661 513 83 163 C ATOM 791 CG GLN A 96 27.449 36.846 30.005 1.00 19.61 C ANISOU 791 CG GLN A 96 2447 3693 1311 449 -506 890 C ATOM 792 CD GLN A 96 28.883 36.399 29.927 1.00 19.34 C ANISOU 792 CD GLN A 96 2651 3517 1180 754 -884 -622 C ATOM 793 OE1 GLN A 96 29.254 35.403 30.556 1.00 31.87 O ANISOU 793 OE1 GLN A 96 4060 4620 3430 1766 -1239 366 O ATOM 794 NE2 GLN A 96 29.699 37.132 29.185 1.00 25.08 N ANISOU 794 NE2 GLN A 96 2151 5339 2039 164 -696 -492 N ATOM 795 N THR A 97 24.763 39.047 30.570 1.00 12.55 N ANISOU 795 N THR A 97 2323 1500 946 -77 -173 -253 N ATOM 796 CA THR A 97 24.678 40.388 31.181 1.00 15.64 C ANISOU 796 CA THR A 97 2856 1792 1293 -23 -349 -668 C ATOM 797 C THR A 97 24.401 40.297 32.666 1.00 15.39 C ANISOU 797 C THR A 97 2673 1871 1304 -220 -340 -728 C ATOM 798 O THR A 97 23.853 39.279 33.134 1.00 17.13 O ANISOU 798 O THR A 97 2726 1865 1918 200 -416 -51 O ATOM 799 CB THR A 97 23.527 41.185 30.538 1.00 15.60 C ANISOU 799 CB THR A 97 2889 1320 1718 -76 297 235 C ATOM 800 OG1 THR A 97 23.435 42.484 31.118 1.00 16.18 O ANISOU 800 OG1 THR A 97 2659 2115 1374 176 -189 -563 O ATOM 801 CG2 THR A 97 22.200 40.517 30.837 1.00 15.99 C ANISOU 801 CG2 THR A 97 2595 1647 1833 252 665 103 C ATOM 802 N ASP A 98 24.738 41.342 33.406 1.00 17.33 N ANISOU 802 N ASP A 98 2707 2469 1411 -231 -618 -997 N ATOM 803 CA ASP A 98 24.505 41.384 34.831 1.00 19.33 C ANISOU 803 CA ASP A 98 3361 2694 1292 422 -854 -946 C ATOM 804 C ASP A 98 23.282 42.234 35.150 1.00 15.07 C ANISOU 804 C ASP A 98 2971 1435 1320 -361 94 161 C ATOM 805 O ASP A 98 22.921 42.332 36.330 1.00 19.54 O ANISOU 805 O ASP A 98 3182 3208 1032 1 -376 -375 O ATOM 806 CB ASP A 98 25.729 41.940 35.584 1.00 26.87 C ANISOU 806 CB ASP A 98 3254 5481 1475 -32 -796 -1439 C ATOM 807 CG ASP A 98 26.397 43.110 34.894 1.00 38.60 C ANISOU 807 CG ASP A 98 4149 7550 2966 -2184 -868 -955 C ATOM 808 OD1 ASP A 98 26.115 43.404 33.696 1.00 57.49 O ANISOU 808 OD1 ASP A 98 5921 9973 5949 -2891 -3518 3332 O ATOM 809 OD2 ASP A 98 27.261 43.782 35.507 1.00 62.67 O ANISOU 809 OD2 ASP A 98 7198 11145 5470 -5190 -1157 -2116 O ATOM 810 N VAL A 99 22.684 42.828 34.124 1.00 14.65 N ANISOU 810 N VAL A 99 1924 2644 1000 -415 61 -197 N ATOM 811 CA VAL A 99 21.454 43.608 34.301 1.00 16.58 C ANISOU 811 CA VAL A 99 1694 2730 1876 -551 10 -20 C ATOM 812 C VAL A 99 20.322 42.710 34.788 1.00 13.82 C ANISOU 812 C VAL A 99 1953 2145 1152 -665 27 -501 C ATOM 813 O VAL A 99 20.103 41.629 34.237 1.00 14.97 O ANISOU 813 O VAL A 99 2231 1935 1523 -87 -371 -446 O ATOM 814 CB VAL A 99 21.078 44.354 33.006 1.00 13.48 C ANISOU 814 CB VAL A 99 1965 1594 1563 -386 230 -512 C ATOM 815 CG1 VAL A 99 19.747 45.103 33.221 1.00 14.41 C ANISOU 815 CG1 VAL A 99 1959 1911 1604 -369 633 -34 C ATOM 816 CG2 VAL A 99 22.222 45.299 32.616 1.00 15.11 C ANISOU 816 CG2 VAL A 99 1748 2645 1349 -698 -13 -373 C ATOM 817 N PRO A 100 19.592 43.120 35.848 1.00 16.18 N ANISOU 817 N PRO A 100 2536 2326 1283 -830 296 -527 N ATOM 818 CA PRO A 100 18.526 42.259 36.329 1.00 15.42 C ANISOU 818 CA PRO A 100 2329 2541 991 -783 152 -352 C ATOM 819 C PRO A 100 17.415 42.142 35.293 1.00 11.81 C ANISOU 819 C PRO A 100 2719 837 931 -522 23 -478 C ATOM 820 O PRO A 100 17.183 43.004 34.446 1.00 12.81 O ANISOU 820 O PRO A 100 2364 1278 1224 -345 389 -131 O ATOM 821 CB PRO A 100 17.999 42.968 37.603 1.00 18.48 C ANISOU 821 CB PRO A 100 3367 2866 789 -1348 296 -612 C ATOM 822 CG PRO A 100 19.102 43.910 37.985 1.00 22.30 C ANISOU 822 CG PRO A 100 3330 3589 1553 -1681 831 -1121 C ATOM 823 CD PRO A 100 19.750 44.323 36.682 1.00 21.89 C ANISOU 823 CD PRO A 100 3691 2713 1914 -1275 1306 -1051 C ATOM 824 N GLN A 101 16.723 40.992 35.420 1.00 11.08 N ANISOU 824 N GLN A 101 1940 863 1408 -202 213 -328 N ATOM 825 CA GLN A 101 15.628 40.688 34.498 1.00 11.27 C ANISOU 825 CA GLN A 101 1741 1026 1513 -260 284 -335 C ATOM 826 C GLN A 101 14.642 41.846 34.378 1.00 10.75 C ANISOU 826 C GLN A 101 1335 1163 1587 -334 566 -227 C ATOM 827 O GLN A 101 14.248 42.150 33.231 1.00 12.50 O ANISOU 827 O GLN A 101 2335 740 1673 -112 203 -421 O ATOM 828 CB GLN A 101 14.946 39.382 34.949 1.00 12.70 C ANISOU 828 CB GLN A 101 1645 1017 2165 -271 597 -528 C ATOM 829 CG GLN A 101 13.794 38.932 34.069 1.00 13.99 C ANISOU 829 CG GLN A 101 2032 859 2423 -313 180 -404 C ATOM 830 CD GLN A 101 13.171 37.638 34.556 1.00 14.45 C ANISOU 830 CD GLN A 101 2672 1058 1761 -691 529 -780 C ATOM 831 OE1 GLN A 101 13.435 36.528 34.101 1.00 13.11 O ANISOU 831 OE1 GLN A 101 2339 866 1776 -107 163 -359 O ATOM 832 NE2 GLN A 101 12.301 37.819 35.550 1.00 11.71 N ANISOU 832 NE2 GLN A 101 2229 1244 974 88 -112 -291 N ATOM 833 N ASP A 102 14.218 42.490 35.475 1.00 12.24 N ANISOU 833 N ASP A 102 1546 1532 1572 28 436 -176 N ATOM 834 CA ASP A 102 13.204 43.568 35.325 1.00 11.38 C ANISOU 834 CA ASP A 102 1690 1500 1134 77 343 -270 C ATOM 835 C ASP A 102 13.798 44.890 34.848 1.00 13.37 C ANISOU 835 C ASP A 102 2312 1586 1183 171 680 -114 C ATOM 836 O ASP A 102 13.005 45.825 34.758 1.00 15.24 O ANISOU 836 O ASP A 102 2248 1436 2104 51 504 -259 O ATOM 837 CB ASP A 102 12.389 43.710 36.601 1.00 11.79 C ANISOU 837 CB ASP A 102 1719 1740 1021 177 303 -107 C ATOM 838 CG ASP A 102 13.120 44.365 37.755 1.00 13.62 C ANISOU 838 CG ASP A 102 1976 2076 1124 319 292 -394 C ATOM 839 OD1 ASP A 102 14.237 44.936 37.599 1.00 16.98 O ANISOU 839 OD1 ASP A 102 2348 3592 511 -477 254 -532 O ATOM 840 OD2 ASP A 102 12.536 44.309 38.869 1.00 12.83 O ANISOU 840 OD2 ASP A 102 2093 1715 1066 113 289 -199 O ATOM 841 N GLN A 103 15.078 44.975 34.502 1.00 12.30 N ANISOU 841 N GLN A 103 2206 1146 1323 -117 488 -406 N ATOM 842 CA GLN A 103 15.687 46.153 33.937 1.00 11.15 C ANISOU 842 CA GLN A 103 2428 902 905 -242 244 -662 C ATOM 843 C GLN A 103 16.115 46.002 32.466 1.00 10.76 C ANISOU 843 C GLN A 103 2409 912 769 -297 -14 -475 C ATOM 844 O GLN A 103 16.508 47.019 31.897 1.00 13.42 O ANISOU 844 O GLN A 103 2675 1134 1290 -457 399 -303 O ATOM 845 CB GLN A 103 16.925 46.601 34.750 1.00 12.48 C ANISOU 845 CB GLN A 103 2265 2176 302 -505 232 45 C ATOM 846 CG GLN A 103 16.596 47.030 36.173 1.00 13.31 C ANISOU 846 CG GLN A 103 2229 2402 426 475 6 -175 C ATOM 847 CD GLN A 103 15.730 48.309 36.103 1.00 15.93 C ANISOU 847 CD GLN A 103 2355 2241 1456 403 -239 13 C ATOM 848 OE1 GLN A 103 16.269 49.410 35.847 1.00 21.37 O ANISOU 848 OE1 GLN A 103 3613 2223 2282 54 83 -154 O ATOM 849 NE2 GLN A 103 14.414 48.216 36.330 1.00 19.64 N ANISOU 849 NE2 GLN A 103 2115 2663 2683 413 -680 -1305 N ATOM 850 N ILE A 104 16.027 44.788 31.960 1.00 11.32 N ANISOU 850 N ILE A 104 2086 1107 1108 -348 465 -836 N ATOM 851 CA ILE A 104 16.303 44.590 30.523 1.00 9.16 C ANISOU 851 CA ILE A 104 2025 544 912 -359 160 -375 C ATOM 852 C ILE A 104 15.319 45.466 29.765 1.00 11.41 C ANISOU 852 C ILE A 104 1991 839 1504 94 607 -186 C ATOM 853 O ILE A 104 14.139 45.505 30.117 1.00 12.24 O ANISOU 853 O ILE A 104 1929 1299 1422 -49 608 -108 O ATOM 854 CB ILE A 104 16.172 43.099 30.152 1.00 9.67 C ANISOU 854 CB ILE A 104 1776 727 1170 123 395 -750 C ATOM 855 CG1 ILE A 104 17.115 42.200 30.974 1.00 10.58 C ANISOU 855 CG1 ILE A 104 1507 674 1838 -124 354 -376 C ATOM 856 CG2 ILE A 104 16.324 42.945 28.650 1.00 13.50 C ANISOU 856 CG2 ILE A 104 2500 1477 1151 -62 651 -859 C ATOM 857 CD1 ILE A 104 18.596 42.437 30.621 1.00 14.09 C ANISOU 857 CD1 ILE A 104 1482 1215 2655 -252 317 -649 C ATOM 858 N ARG A 105 15.844 46.130 28.740 1.00 11.04 N ANISOU 858 N ARG A 105 1648 1354 1191 -204 150 10 N ATOM 859 CA ARG A 105 14.965 47.034 27.980 1.00 11.06 C ANISOU 859 CA ARG A 105 1285 1511 1408 -566 -156 55 C ATOM 860 C ARG A 105 14.508 46.334 26.714 1.00 10.97 C ANISOU 860 C ARG A 105 1418 1137 1613 -248 -106 -195 C ATOM 861 O ARG A 105 15.273 46.249 25.758 1.00 12.33 O ANISOU 861 O ARG A 105 1628 1298 1759 -108 90 -264 O ATOM 862 CB ARG A 105 15.730 48.319 27.654 1.00 14.22 C ANISOU 862 CB ARG A 105 2439 1212 1751 -715 -124 -39 C ATOM 863 CG ARG A 105 16.206 49.001 28.924 1.00 17.24 C ANISOU 863 CG ARG A 105 2266 1938 2346 -792 2 -793 C ATOM 864 CD ARG A 105 15.101 49.358 29.879 1.00 23.97 C ANISOU 864 CD ARG A 105 3356 2880 2871 59 506 -1043 C ATOM 865 NE ARG A 105 14.234 50.438 29.455 1.00 32.30 N ANISOU 865 NE ARG A 105 4501 3028 4743 862 793 -871 N ATOM 866 CZ ARG A 105 14.498 51.719 29.230 1.00 39.57 C ANISOU 866 CZ ARG A 105 5702 2815 6520 606 -259 -1041 C ATOM 867 NH1 ARG A 105 15.728 52.219 29.372 1.00 48.41 N ANISOU 867 NH1 ARG A 105 6641 3922 7831 -703 56 -2846 N ATOM 868 NH2 ARG A 105 13.553 52.579 28.842 1.00 50.98 N ANISOU 868 NH2 ARG A 105 8215 2965 8189 1973 -1067 -1489 N ATOM 869 N HIS A 106 13.256 45.852 26.768 1.00 10.92 N ANISOU 869 N HIS A 106 1331 1264 1553 -103 -129 -646 N ATOM 870 CA HIS A 106 12.638 45.293 25.589 1.00 10.44 C ANISOU 870 CA HIS A 106 1571 1157 1239 -221 -283 -156 C ATOM 871 C HIS A 106 12.111 46.432 24.748 1.00 9.60 C ANISOU 871 C HIS A 106 1465 1099 1085 -25 477 -151 C ATOM 872 O HIS A 106 11.589 47.427 25.312 1.00 12.33 O ANISOU 872 O HIS A 106 2167 1568 951 485 -5 -457 O ATOM 873 CB HIS A 106 11.518 44.371 26.052 1.00 10.57 C ANISOU 873 CB HIS A 106 1717 1014 1285 -293 -447 -46 C ATOM 874 CG HIS A 106 12.068 43.358 27.029 1.00 8.63 C ANISOU 874 CG HIS A 106 739 1716 824 34 225 22 C ATOM 875 ND1 HIS A 106 11.882 43.244 28.386 1.00 10.85 N ANISOU 875 ND1 HIS A 106 1902 1461 758 19 176 -273 N ATOM 876 CD2 HIS A 106 12.927 42.353 26.691 1.00 7.68 C ANISOU 876 CD2 HIS A 106 1171 981 767 -268 241 -98 C ATOM 877 CE1 HIS A 106 12.577 42.182 28.813 1.00 8.29 C ANISOU 877 CE1 HIS A 106 1641 890 618 -478 42 -281 C ATOM 878 NE2 HIS A 106 13.224 41.643 27.791 1.00 10.14 N ANISOU 878 NE2 HIS A 106 1817 1101 937 -132 132 -81 N ATOM 879 N VAL A 107 12.215 46.308 23.443 1.00 8.83 N ANISOU 879 N VAL A 107 1279 1049 1026 183 402 -206 N ATOM 880 CA VAL A 107 11.981 47.442 22.553 1.00 10.84 C ANISOU 880 CA VAL A 107 1372 1272 1475 -129 -79 130 C ATOM 881 C VAL A 107 10.858 47.179 21.554 1.00 7.97 C ANISOU 881 C VAL A 107 1029 732 1267 60 343 -94 C ATOM 882 O VAL A 107 10.902 46.165 20.853 1.00 13.98 O ANISOU 882 O VAL A 107 2099 722 2489 268 -502 -511 O ATOM 883 CB VAL A 107 13.294 47.757 21.797 1.00 10.00 C ANISOU 883 CB VAL A 107 1368 864 1567 -388 -183 133 C ATOM 884 CG1 VAL A 107 13.039 48.852 20.756 1.00 12.73 C ANISOU 884 CG1 VAL A 107 2207 595 2033 42 215 277 C ATOM 885 CG2 VAL A 107 14.374 48.203 22.788 1.00 11.88 C ANISOU 885 CG2 VAL A 107 1407 1439 1667 -255 63 -782 C ATOM 886 N TYR A 108 9.874 48.054 21.532 1.00 9.93 N ANISOU 886 N TYR A 108 1663 685 1427 392 -42 366 N ATOM 887 CA TYR A 108 8.710 47.978 20.645 1.00 13.06 C ANISOU 887 CA TYR A 108 1823 1547 1593 320 -310 515 C ATOM 888 C TYR A 108 8.665 49.248 19.817 1.00 12.00 C ANISOU 888 C TYR A 108 1937 1048 1573 491 -456 125 C ATOM 889 O TYR A 108 8.498 50.383 20.313 1.00 17.98 O ANISOU 889 O TYR A 108 2680 1437 2716 969 349 -292 O ATOM 890 CB TYR A 108 7.447 47.824 21.502 1.00 14.76 C ANISOU 890 CB TYR A 108 1631 1641 2338 477 -170 480 C ATOM 891 CG TYR A 108 7.604 46.557 22.323 1.00 13.58 C ANISOU 891 CG TYR A 108 1566 1631 1965 698 411 381 C ATOM 892 CD1 TYR A 108 7.441 45.327 21.682 1.00 18.46 C ANISOU 892 CD1 TYR A 108 2928 1692 2394 402 -141 332 C ATOM 893 CD2 TYR A 108 7.929 46.546 23.671 1.00 14.91 C ANISOU 893 CD2 TYR A 108 1965 2007 1694 701 863 411 C ATOM 894 CE1 TYR A 108 7.574 44.113 22.352 1.00 14.51 C ANISOU 894 CE1 TYR A 108 2125 1663 1727 85 445 199 C ATOM 895 CE2 TYR A 108 8.067 45.334 24.365 1.00 13.27 C ANISOU 895 CE2 TYR A 108 1422 1753 1867 -85 65 337 C ATOM 896 CZ TYR A 108 7.889 44.133 23.701 1.00 16.16 C ANISOU 896 CZ TYR A 108 2480 2036 1622 -765 608 305 C ATOM 897 OH TYR A 108 8.016 42.904 24.315 1.00 14.03 O ANISOU 897 OH TYR A 108 2127 1760 1443 -344 -256 -190 O ATOM 898 N LEU A 109 8.847 49.100 18.507 1.00 10.71 N ANISOU 898 N LEU A 109 1435 1016 1617 73 -13 356 N ATOM 899 CA LEU A 109 8.907 50.258 17.613 1.00 11.99 C ANISOU 899 CA LEU A 109 1443 976 2138 195 -92 581 C ATOM 900 C LEU A 109 7.797 50.209 16.545 1.00 11.63 C ANISOU 900 C LEU A 109 1650 764 2005 149 -134 444 C ATOM 901 O LEU A 109 7.112 49.150 16.411 1.00 12.11 O ANISOU 901 O LEU A 109 1492 856 2253 165 191 271 O ATOM 902 CB LEU A 109 10.260 50.362 16.913 1.00 12.41 C ANISOU 902 CB LEU A 109 1651 1079 1986 -427 57 197 C ATOM 903 CG LEU A 109 11.490 50.470 17.814 1.00 12.28 C ANISOU 903 CG LEU A 109 1482 1028 2156 -330 161 -4 C ATOM 904 CD1 LEU A 109 12.799 50.506 17.016 1.00 13.45 C ANISOU 904 CD1 LEU A 109 1507 1289 2315 -69 217 320 C ATOM 905 CD2 LEU A 109 11.422 51.746 18.637 1.00 15.28 C ANISOU 905 CD2 LEU A 109 2304 1363 2140 -344 96 -293 C ATOM 906 N GLU A 110 7.621 51.326 15.864 1.00 12.56 N ANISOU 906 N GLU A 110 2081 762 1929 175 -482 322 N ATOM 907 CA GLU A 110 6.607 51.391 14.804 1.00 13.55 C ANISOU 907 CA GLU A 110 2015 1573 1561 125 -262 250 C ATOM 908 C GLU A 110 5.254 50.946 15.351 1.00 11.68 C ANISOU 908 C GLU A 110 1757 590 2090 709 -168 131 C ATOM 909 O GLU A 110 4.851 51.311 16.466 1.00 13.53 O ANISOU 909 O GLU A 110 2208 855 2076 271 128 189 O ATOM 910 CB GLU A 110 7.083 50.585 13.588 1.00 11.56 C ANISOU 910 CB GLU A 110 1888 770 1734 -39 -88 418 C ATOM 911 CG GLU A 110 8.417 51.003 12.994 1.00 16.84 C ANISOU 911 CG GLU A 110 2482 569 3346 173 908 487 C ATOM 912 CD GLU A 110 8.469 52.419 12.471 1.00 15.89 C ANISOU 912 CD GLU A 110 2492 672 2874 69 559 609 C ATOM 913 OE1 GLU A 110 7.467 53.119 12.245 1.00 21.29 O ANISOU 913 OE1 GLU A 110 3081 1363 3643 261 -656 1014 O ATOM 914 OE2 GLU A 110 9.598 52.906 12.238 1.00 22.71 O ANISOU 914 OE2 GLU A 110 2908 1334 4388 -432 625 994 O ATOM 915 N LYS A 111 4.450 50.161 14.627 1.00 14.71 N ANISOU 915 N LYS A 111 2361 968 2259 -6 -123 234 N ATOM 916 CA LYS A 111 3.141 49.824 15.184 1.00 13.52 C ANISOU 916 CA LYS A 111 2131 1240 1764 240 -337 331 C ATOM 917 C LYS A 111 3.232 48.774 16.284 1.00 11.49 C ANISOU 917 C LYS A 111 1865 1167 1332 975 220 67 C ATOM 918 O LYS A 111 2.245 48.507 17.003 1.00 13.33 O ANISOU 918 O LYS A 111 1813 1085 2168 527 367 131 O ATOM 919 CB LYS A 111 2.152 49.351 14.107 1.00 14.85 C ANISOU 919 CB LYS A 111 2189 1345 2109 534 -694 297 C ATOM 920 CG LYS A 111 1.881 50.410 13.058 1.00 13.12 C ANISOU 920 CG LYS A 111 1654 1642 1690 428 -50 413 C ATOM 921 CD LYS A 111 1.002 49.822 11.971 1.00 16.64 C ANISOU 921 CD LYS A 111 2014 2033 2277 597 -717 407 C ATOM 922 CE LYS A 111 0.677 50.885 10.929 1.00 21.69 C ANISOU 922 CE LYS A 111 2110 3540 2589 907 -563 1302 C ATOM 923 NZ LYS A 111 0.075 50.254 9.723 1.00 31.83 N ANISOU 923 NZ LYS A 111 5786 4478 1832 741 -675 1150 N ATOM 924 N ALA A 112 4.406 48.155 16.437 1.00 11.32 N ANISOU 924 N ALA A 112 1576 505 2219 481 164 32 N ATOM 925 CA ALA A 112 4.555 47.151 17.513 1.00 12.40 C ANISOU 925 CA ALA A 112 1732 786 2194 740 -277 -25 C ATOM 926 C ALA A 112 4.555 47.811 18.881 1.00 11.49 C ANISOU 926 C ALA A 112 1430 735 2199 268 -55 1 C ATOM 927 O ALA A 112 4.565 47.091 19.882 1.00 12.32 O ANISOU 927 O ALA A 112 1456 995 2232 489 -244 142 O ATOM 928 CB ALA A 112 5.789 46.278 17.294 1.00 12.78 C ANISOU 928 CB ALA A 112 1437 1176 2243 628 429 449 C ATOM 929 N VAL A 113 4.532 49.169 18.944 1.00 11.97 N ANISOU 929 N VAL A 113 1569 756 2223 671 319 -81 N ATOM 930 CA VAL A 113 4.319 49.815 20.242 1.00 13.14 C ANISOU 930 CA VAL A 113 2071 811 2109 -123 -12 -158 C ATOM 931 C VAL A 113 3.009 49.306 20.838 1.00 10.30 C ANISOU 931 C VAL A 113 1817 547 1549 397 38 -320 C ATOM 932 O VAL A 113 2.887 49.291 22.064 1.00 13.66 O ANISOU 932 O VAL A 113 2511 1155 1525 661 23 -195 O ATOM 933 CB AVAL A 113 4.300 51.357 20.209 0.49 13.98 C ANISOU 933 CB AVAL A 113 2320 820 2170 19 147 -275 C ATOM 934 CB BVAL A 113 4.319 51.348 20.078 0.51 11.71 C ANISOU 934 CB BVAL A 113 2234 819 1395 -34 -502 -158 C ATOM 935 CG1AVAL A 113 5.682 51.918 19.903 0.49 10.30 C ANISOU 935 CG1AVAL A 113 2423 472 1019 123 201 29 C ATOM 936 CG1BVAL A 113 3.039 51.848 19.414 0.51 15.10 C ANISOU 936 CG1BVAL A 113 2202 1739 1796 436 -247 47 C ATOM 937 CG2AVAL A 113 3.308 51.919 19.199 0.49 11.45 C ANISOU 937 CG2AVAL A 113 2217 449 1683 -780 447 349 C ATOM 938 CG2BVAL A 113 4.507 52.039 21.417 0.51 13.32 C ANISOU 938 CG2BVAL A 113 2603 1195 1262 -124 67 -299 C ATOM 939 N VAL A 114 2.018 48.859 20.069 1.00 11.00 N ANISOU 939 N VAL A 114 1638 787 1755 408 -129 64 N ATOM 940 CA VAL A 114 0.753 48.374 20.653 1.00 12.52 C ANISOU 940 CA VAL A 114 1730 1486 1541 330 -12 -3 C ATOM 941 C VAL A 114 0.935 47.108 21.473 1.00 13.20 C ANISOU 941 C VAL A 114 1704 1597 1713 143 59 222 C ATOM 942 O VAL A 114 -0.003 46.694 22.200 1.00 16.78 O ANISOU 942 O VAL A 114 1954 2418 2003 -223 227 269 O ATOM 943 CB AVAL A 114 -0.269 48.035 19.549 0.37 13.39 C ANISOU 943 CB AVAL A 114 2057 1101 1930 -252 -265 336 C ATOM 944 CB BVAL A 114 -0.330 48.219 19.566 0.63 13.57 C ANISOU 944 CB BVAL A 114 1811 1275 2070 -7 -270 245 C ATOM 945 CG1AVAL A 114 0.022 46.630 19.033 0.37 11.43 C ANISOU 945 CG1AVAL A 114 1403 215 2726 -1413 113 870 C ATOM 946 CG1BVAL A 114 -0.505 49.571 18.868 0.63 13.42 C ANISOU 946 CG1BVAL A 114 2521 1167 1413 671 -138 -196 C ATOM 947 CG2AVAL A 114 -1.679 48.146 20.079 0.37 15.80 C ANISOU 947 CG2AVAL A 114 2013 1872 2118 -825 -204 -14 C ATOM 948 CG2BVAL A 114 0.042 47.135 18.581 0.63 13.44 C ANISOU 948 CG2BVAL A 114 3176 732 1198 246 -768 802 C ATOM 949 N LEU A 115 2.104 46.474 21.377 1.00 12.89 N ANISOU 949 N LEU A 115 1652 1182 2064 13 -291 32 N ATOM 950 CA LEU A 115 2.401 45.210 22.038 1.00 11.66 C ANISOU 950 CA LEU A 115 2540 698 1194 129 -142 -614 C ATOM 951 C LEU A 115 3.027 45.455 23.413 1.00 12.98 C ANISOU 951 C LEU A 115 2896 1191 844 -621 58 -333 C ATOM 952 O LEU A 115 3.257 44.520 24.186 1.00 13.72 O ANISOU 952 O LEU A 115 2762 1297 1153 -378 77 -145 O ATOM 953 CB LEU A 115 3.347 44.353 21.204 1.00 11.20 C ANISOU 953 CB LEU A 115 2264 1200 792 173 25 -208 C ATOM 954 CG LEU A 115 2.963 44.018 19.757 1.00 10.10 C ANISOU 954 CG LEU A 115 2363 577 896 -95 68 -283 C ATOM 955 CD1 LEU A 115 4.043 43.114 19.185 1.00 12.68 C ANISOU 955 CD1 LEU A 115 2811 1060 948 342 326 -92 C ATOM 956 CD2 LEU A 115 1.641 43.285 19.647 1.00 15.58 C ANISOU 956 CD2 LEU A 115 2320 1050 2552 -95 -674 -121 C ATOM 957 N ARG A 116 3.336 46.749 23.721 1.00 11.74 N ANISOU 957 N ARG A 116 2127 1091 1243 -19 -253 -482 N ATOM 958 CA ARG A 116 4.110 46.890 24.946 1.00 14.78 C ANISOU 958 CA ARG A 116 2820 1870 925 -608 -104 -696 C ATOM 959 C ARG A 116 3.218 46.581 26.146 1.00 12.21 C ANISOU 959 C ARG A 116 2337 1004 1298 814 130 -360 C ATOM 960 O ARG A 116 2.006 46.839 26.160 1.00 17.84 O ANISOU 960 O ARG A 116 2456 2467 1853 1123 -97 62 O ATOM 961 CB ARG A 116 4.738 48.271 24.998 1.00 18.44 C ANISOU 961 CB ARG A 116 3381 1920 1706 -834 -564 -570 C ATOM 962 CG ARG A 116 3.774 49.387 25.200 1.00 22.17 C ANISOU 962 CG ARG A 116 4294 1883 2246 -346 -1186 -511 C ATOM 963 CD ARG A 116 4.436 50.770 25.181 1.00 23.11 C ANISOU 963 CD ARG A 116 5455 1820 1505 -538 -1709 -58 C ATOM 964 NE ARG A 116 5.386 50.914 26.288 1.00 19.50 N ANISOU 964 NE ARG A 116 4057 1570 1784 126 -1291 -606 N ATOM 965 CZ ARG A 116 5.926 52.067 26.668 1.00 20.28 C ANISOU 965 CZ ARG A 116 4311 1427 1969 -115 -1401 -175 C ATOM 966 NH1 ARG A 116 5.601 53.189 26.026 1.00 31.79 N ANISOU 966 NH1 ARG A 116 6400 1968 3711 -100 -1225 995 N ATOM 967 NH2 ARG A 116 6.784 52.144 27.671 1.00 37.10 N ANISOU 967 NH2 ARG A 116 7366 2340 4392 -83 -3977 -1059 N ATOM 968 N PRO A 117 3.762 45.932 27.161 1.00 12.77 N ANISOU 968 N PRO A 117 1996 1276 1579 252 7 60 N ATOM 969 CA PRO A 117 2.931 45.450 28.298 1.00 13.58 C ANISOU 969 CA PRO A 117 2313 825 2019 360 331 177 C ATOM 970 C PRO A 117 2.576 46.552 29.282 1.00 16.01 C ANISOU 970 C PRO A 117 3002 1325 1754 926 223 110 C ATOM 971 O PRO A 117 1.686 46.338 30.125 1.00 19.40 O ANISOU 971 O PRO A 117 3150 2880 1341 793 63 41 O ATOM 972 CB PRO A 117 3.833 44.382 28.939 1.00 13.16 C ANISOU 972 CB PRO A 117 2306 1199 1494 574 360 -41 C ATOM 973 CG PRO A 117 5.199 44.940 28.726 1.00 13.79 C ANISOU 973 CG PRO A 117 2235 2315 690 486 307 -81 C ATOM 974 CD PRO A 117 5.150 45.518 27.323 1.00 12.66 C ANISOU 974 CD PRO A 117 2126 1821 863 381 -63 -27 C ATOM 975 N ASP A 118 3.211 47.725 29.211 1.00 15.48 N ANISOU 975 N ASP A 118 3289 1256 1336 732 -811 -269 N ATOM 976 CA ASP A 118 2.875 48.818 30.142 1.00 18.22 C ANISOU 976 CA ASP A 118 3965 1806 1153 1186 -766 -366 C ATOM 977 C ASP A 118 2.912 48.410 31.599 1.00 18.57 C ANISOU 977 C ASP A 118 3059 2851 1148 403 -718 -170 C ATOM 978 O ASP A 118 1.968 48.670 32.373 1.00 22.82 O ANISOU 978 O ASP A 118 3586 2981 2104 39 194 -6 O ATOM 979 CB ASP A 118 1.463 49.363 29.885 1.00 19.62 C ANISOU 979 CB ASP A 118 4172 1530 1753 1349 -841 -292 C ATOM 980 CG ASP A 118 1.438 49.989 28.489 1.00 25.51 C ANISOU 980 CG ASP A 118 5286 2115 2292 2863 -275 408 C ATOM 981 OD1 ASP A 118 2.514 50.517 28.119 1.00 39.41 O ANISOU 981 OD1 ASP A 118 5869 6079 3025 2317 646 1866 O ATOM 982 OD2 ASP A 118 0.360 49.961 27.848 1.00 33.32 O ANISOU 982 OD2 ASP A 118 6822 3300 2538 2144 -1601 785 O ATOM 983 N LEU A 119 4.009 47.773 31.980 1.00 18.29 N ANISOU 983 N LEU A 119 3830 1945 1175 582 -1049 -338 N ATOM 984 CA LEU A 119 4.159 47.291 33.338 1.00 16.50 C ANISOU 984 CA LEU A 119 3175 2228 865 804 -740 -684 C ATOM 985 C LEU A 119 4.511 48.458 34.244 1.00 16.83 C ANISOU 985 C LEU A 119 4079 1582 734 491 -17 -325 C ATOM 986 O LEU A 119 5.077 49.455 33.778 1.00 24.43 O ANISOU 986 O LEU A 119 5429 2426 1427 -455 -593 422 O ATOM 987 CB LEU A 119 5.235 46.188 33.363 1.00 14.99 C ANISOU 987 CB LEU A 119 3176 1258 1263 336 25 18 C ATOM 988 CG LEU A 119 4.889 44.993 32.484 1.00 17.06 C ANISOU 988 CG LEU A 119 3071 1784 1625 253 135 -471 C ATOM 989 CD1 LEU A 119 6.061 44.036 32.300 1.00 17.80 C ANISOU 989 CD1 LEU A 119 3640 1432 1692 596 -288 -161 C ATOM 990 CD2 LEU A 119 3.697 44.236 33.072 1.00 17.71 C ANISOU 990 CD2 LEU A 119 3241 2000 1487 -129 -669 325 C ATOM 991 N SER A 120 4.194 48.299 35.538 1.00 16.48 N ANISOU 991 N SER A 120 3951 1642 670 1039 -57 -388 N ATOM 992 CA SER A 120 4.567 49.324 36.494 1.00 16.24 C ANISOU 992 CA SER A 120 3462 1936 771 889 -206 -440 C ATOM 993 C SER A 120 5.444 48.747 37.576 1.00 15.95 C ANISOU 993 C SER A 120 2876 2173 1012 447 -77 -47 C ATOM 994 O SER A 120 4.948 48.128 38.507 1.00 15.70 O ANISOU 994 O SER A 120 2789 2518 659 275 -245 -198 O ATOM 995 CB SER A 120 3.330 49.928 37.168 1.00 19.82 C ANISOU 995 CB SER A 120 4027 1463 2040 1409 -159 -965 C ATOM 996 OG SER A 120 3.745 50.782 38.251 1.00 22.04 O ANISOU 996 OG SER A 120 4128 2274 1972 1633 -511 -1172 O ATOM 997 N LEU A 121 6.747 48.938 37.445 1.00 16.92 N ANISOU 997 N LEU A 121 2848 1914 1665 1048 449 159 N ATOM 998 CA LEU A 121 7.622 48.398 38.490 1.00 17.04 C ANISOU 998 CA LEU A 121 2123 2698 1652 724 846 696 C ATOM 999 C LEU A 121 7.493 49.278 39.725 1.00 17.45 C ANISOU 999 C LEU A 121 2727 2518 1384 -114 686 853 C ATOM 1000 O LEU A 121 7.699 48.823 40.854 1.00 19.71 O ANISOU 1000 O LEU A 121 2554 3377 1560 315 149 985 O ATOM 1001 CB LEU A 121 9.006 48.325 37.852 1.00 23.57 C ANISOU 1001 CB LEU A 121 2259 2762 3933 887 1535 767 C ATOM 1002 CG LEU A 121 10.111 47.489 38.460 1.00 19.62 C ANISOU 1002 CG LEU A 121 1744 2119 3592 88 832 1 C ATOM 1003 CD1 LEU A 121 9.644 46.082 38.785 1.00 17.11 C ANISOU 1003 CD1 LEU A 121 3347 1985 1169 -40 615 -236 C ATOM 1004 CD2 LEU A 121 11.335 47.520 37.529 1.00 15.27 C ANISOU 1004 CD2 LEU A 121 1172 2861 1769 -122 -177 -472 C ATOM 1005 N THR A 122 7.119 50.555 39.526 1.00 14.99 N ANISOU 1005 N THR A 122 1867 2594 1235 6 -130 344 N ATOM 1006 CA THR A 122 7.009 51.453 40.686 1.00 19.48 C ANISOU 1006 CA THR A 122 2216 3338 1848 -121 67 -333 C ATOM 1007 C THR A 122 5.977 50.873 41.620 1.00 20.14 C ANISOU 1007 C THR A 122 2805 3694 1152 -564 -97 -571 C ATOM 1008 O THR A 122 6.058 50.862 42.847 1.00 24.68 O ANISOU 1008 O THR A 122 4672 3545 1159 -1282 -463 -238 O ATOM 1009 CB ATHR A 122 6.679 52.887 40.253 0.47 22.47 C ANISOU 1009 CB ATHR A 122 3202 3226 2108 254 911 -489 C ATOM 1010 CB BTHR A 122 6.639 52.873 40.224 0.53 23.15 C ANISOU 1010 CB BTHR A 122 3419 3215 2164 317 1044 -464 C ATOM 1011 OG1ATHR A 122 5.333 52.951 39.784 0.47 25.90 O ANISOU 1011 OG1ATHR A 122 3940 3696 2205 176 -134 1083 O ATOM 1012 OG1BTHR A 122 7.787 53.518 39.634 0.53 26.75 O ANISOU 1012 OG1BTHR A 122 3603 4110 2449 -383 245 513 O ATOM 1013 CG2ATHR A 122 7.544 53.318 39.069 0.47 25.54 C ANISOU 1013 CG2ATHR A 122 4665 2961 2079 1048 1668 -429 C ATOM 1014 CG2BTHR A 122 6.250 53.812 41.355 0.53 24.97 C ANISOU 1014 CG2BTHR A 122 3597 4139 1750 831 -629 -1148 C ATOM 1015 N LYS A 123 4.939 50.261 41.042 1.00 17.50 N ANISOU 1015 N LYS A 123 2649 2545 1456 -353 -703 609 N ATOM 1016 CA LYS A 123 3.934 49.680 41.929 1.00 15.82 C ANISOU 1016 CA LYS A 123 2678 1814 1519 253 25 -58 C ATOM 1017 C LYS A 123 4.278 48.234 42.262 1.00 12.53 C ANISOU 1017 C LYS A 123 2164 1747 850 29 -333 -196 C ATOM 1018 O LYS A 123 4.096 47.838 43.440 1.00 14.19 O ANISOU 1018 O LYS A 123 2667 1771 952 34 -33 -254 O ATOM 1019 CB LYS A 123 2.559 49.795 41.238 1.00 18.13 C ANISOU 1019 CB LYS A 123 2252 2837 1799 1090 606 252 C ATOM 1020 CG LYS A 123 1.502 49.034 42.016 1.00 19.38 C ANISOU 1020 CG LYS A 123 2403 3206 1755 582 529 31 C ATOM 1021 CD LYS A 123 0.135 49.151 41.336 1.00 24.47 C ANISOU 1021 CD LYS A 123 2326 3452 3518 936 308 1285 C ATOM 1022 CE LYS A 123 -0.940 48.595 42.259 1.00 25.70 C ANISOU 1022 CE LYS A 123 2250 3111 4402 1234 831 1148 C ATOM 1023 NZ LYS A 123 -2.311 48.702 41.666 1.00 39.22 N ANISOU 1023 NZ LYS A 123 2474 5994 6436 -141 -135 983 N ATOM 1024 N ASN A 124 4.814 47.492 41.304 1.00 14.26 N ANISOU 1024 N ASN A 124 2846 1588 984 -167 -32 -277 N ATOM 1025 CA ASN A 124 5.045 46.050 41.517 1.00 13.96 C ANISOU 1025 CA ASN A 124 3218 1683 401 -2 -412 -179 C ATOM 1026 C ASN A 124 6.074 45.787 42.629 1.00 16.23 C ANISOU 1026 C ASN A 124 2556 2961 648 -369 -252 377 C ATOM 1027 O ASN A 124 5.990 44.741 43.269 1.00 16.78 O ANISOU 1027 O ASN A 124 3276 2627 471 -238 -603 144 O ATOM 1028 CB ASN A 124 5.433 45.326 40.226 1.00 15.00 C ANISOU 1028 CB ASN A 124 2964 1889 847 365 -147 -337 C ATOM 1029 CG ASN A 124 5.255 43.816 40.384 1.00 13.57 C ANISOU 1029 CG ASN A 124 2736 2038 382 -272 -223 -575 C ATOM 1030 OD1 ASN A 124 4.146 43.276 40.391 1.00 25.86 O ANISOU 1030 OD1 ASN A 124 2986 3196 3642 -796 -59 -1141 O ATOM 1031 ND2 ASN A 124 6.367 43.091 40.507 1.00 17.76 N ANISOU 1031 ND2 ASN A 124 3179 1529 2041 -209 -776 206 N ATOM 1032 N THR A 125 7.007 46.713 42.824 1.00 13.10 N ANISOU 1032 N THR A 125 2066 2235 677 352 234 -378 N ATOM 1033 CA THR A 125 8.021 46.562 43.867 1.00 13.54 C ANISOU 1033 CA THR A 125 2384 2039 723 -139 25 -356 C ATOM 1034 C THR A 125 7.448 46.776 45.263 1.00 12.13 C ANISOU 1034 C THR A 125 2562 1312 737 171 -59 -440 C ATOM 1035 O THR A 125 8.181 46.503 46.229 1.00 15.91 O ANISOU 1035 O THR A 125 2817 2449 781 552 -142 -281 O ATOM 1036 CB THR A 125 9.205 47.529 43.692 1.00 12.86 C ANISOU 1036 CB THR A 125 2626 1401 859 19 -54 -297 C ATOM 1037 OG1 THR A 125 8.701 48.861 43.674 1.00 15.46 O ANISOU 1037 OG1 THR A 125 3258 1593 1021 424 -108 -331 O ATOM 1038 CG2 THR A 125 9.987 47.247 42.383 1.00 13.19 C ANISOU 1038 CG2 THR A 125 2448 1545 1019 133 157 -68 C ATOM 1039 N GLU A 126 6.224 47.238 45.403 1.00 12.43 N ANISOU 1039 N GLU A 126 2389 1523 810 3 -79 -476 N ATOM 1040 CA GLU A 126 5.603 47.712 46.623 1.00 12.32 C ANISOU 1040 CA GLU A 126 2444 1331 905 -30 96 -391 C ATOM 1041 C GLU A 126 4.432 46.880 47.125 1.00 11.27 C ANISOU 1041 C GLU A 126 2510 1177 595 -266 -155 -618 C ATOM 1042 O GLU A 126 4.204 46.851 48.358 1.00 13.81 O ANISOU 1042 O GLU A 126 3068 1625 553 -494 -200 -228 O ATOM 1043 CB GLU A 126 5.004 49.113 46.381 1.00 10.07 C ANISOU 1043 CB GLU A 126 2111 1341 375 -119 -200 -302 C ATOM 1044 CG GLU A 126 6.025 50.160 45.920 1.00 12.73 C ANISOU 1044 CG GLU A 126 2279 1679 877 -431 -362 -68 C ATOM 1045 CD GLU A 126 6.742 50.847 47.048 1.00 8.39 C ANISOU 1045 CD GLU A 126 1603 843 742 317 -267 -7 C ATOM 1046 OE1 GLU A 126 6.885 50.376 48.208 1.00 12.32 O ANISOU 1046 OE1 GLU A 126 1994 1978 710 -159 -167 357 O ATOM 1047 OE2 GLU A 126 7.215 51.988 46.792 1.00 12.82 O ANISOU 1047 OE2 GLU A 126 2589 1402 879 -574 -14 8 O ATOM 1048 N LEU A 127 3.694 46.289 46.197 1.00 15.79 N ANISOU 1048 N LEU A 127 2744 2326 930 -302 -704 -586 N ATOM 1049 CA LEU A 127 2.432 45.650 46.533 1.00 16.64 C ANISOU 1049 CA LEU A 127 2457 2128 1738 -226 -1037 -575 C ATOM 1050 C LEU A 127 2.184 44.331 45.819 1.00 18.93 C ANISOU 1050 C LEU A 127 2701 2068 2423 -93 -376 -888 C ATOM 1051 O LEU A 127 2.732 44.123 44.716 1.00 23.70 O ANISOU 1051 O LEU A 127 3684 3458 1862 13 -684 -1105 O ATOM 1052 CB LEU A 127 1.301 46.589 46.108 1.00 20.28 C ANISOU 1052 CB LEU A 127 2973 2590 2144 694 -199 -585 C ATOM 1053 CG LEU A 127 1.254 47.907 46.889 1.00 21.51 C ANISOU 1053 CG LEU A 127 3650 2605 1917 529 -1055 -585 C ATOM 1054 CD1 LEU A 127 0.663 49.019 46.031 1.00 23.39 C ANISOU 1054 CD1 LEU A 127 3155 2678 3053 814 -1522 -598 C ATOM 1055 CD2 LEU A 127 0.470 47.743 48.195 1.00 24.86 C ANISOU 1055 CD2 LEU A 127 4035 3149 2262 573 -493 -1279 C ATOM 1056 OXT LEU A 127 1.366 43.567 46.419 1.00 25.17 O ANISOU 1056 OXT LEU A 127 4153 2440 2972 -1020 -381 -653 O TER 1057 LEU A 127 ATOM 1058 N MET B 1 29.355 28.866 32.759 1.00 57.30 N ANISOU 1058 N MET B 1 10638 6067 5066 1437 1632 3302 N ATOM 1059 CA MET B 1 30.160 29.845 32.025 1.00 42.75 C ANISOU 1059 CA MET B 1 6457 5628 4157 407 -1516 2237 C ATOM 1060 C MET B 1 29.443 30.419 30.809 1.00 32.57 C ANISOU 1060 C MET B 1 5687 3099 3587 -77 -1386 1271 C ATOM 1061 O MET B 1 28.210 30.527 30.859 1.00 30.91 O ANISOU 1061 O MET B 1 5638 3706 2402 -388 -1121 664 O ATOM 1062 CB MET B 1 31.467 29.162 31.622 1.00 42.51 C ANISOU 1062 CB MET B 1 6271 5589 4292 544 -2578 1138 C ATOM 1063 CG MET B 1 31.235 27.779 31.004 1.00 46.83 C ANISOU 1063 CG MET B 1 6868 6385 4540 327 -3185 329 C ATOM 1064 SD MET B 1 32.019 27.706 29.390 1.00 66.69 S ANISOU 1064 SD MET B 1 6553 8964 9822 -3818 2105 -3552 S ATOM 1065 CE MET B 1 32.398 25.965 29.234 1.00 39.68 C ANISOU 1065 CE MET B 1 3329 10339 1408 1595 290 3609 C ATOM 1066 N MET B 2 30.181 30.801 29.757 1.00 25.90 N ANISOU 1066 N MET B 2 4564 2596 2679 -13 -1785 -113 N ATOM 1067 CA MET B 2 29.556 31.422 28.577 1.00 19.13 C ANISOU 1067 CA MET B 2 2750 1952 2567 -376 -1160 -116 C ATOM 1068 C MET B 2 28.916 30.309 27.744 1.00 15.72 C ANISOU 1068 C MET B 2 2009 1599 2366 -112 -677 -113 C ATOM 1069 O MET B 2 29.312 29.144 27.751 1.00 13.56 O ANISOU 1069 O MET B 2 1645 1757 1752 67 -90 78 O ATOM 1070 CB MET B 2 30.529 32.236 27.740 1.00 19.75 C ANISOU 1070 CB MET B 2 2336 1510 3658 -211 -986 -53 C ATOM 1071 CG MET B 2 29.871 33.033 26.621 1.00 20.44 C ANISOU 1071 CG MET B 2 1380 2560 3828 258 40 765 C ATOM 1072 SD MET B 2 28.485 34.076 27.166 1.00 14.72 S ANISOU 1072 SD MET B 2 2008 1615 1968 -126 -182 -226 S ATOM 1073 CE MET B 2 28.084 34.761 25.536 1.00 13.14 C ANISOU 1073 CE MET B 2 1825 1270 1899 -32 -250 -379 C ATOM 1074 N ILE B 3 27.871 30.764 27.051 1.00 13.67 N ANISOU 1074 N ILE B 3 2358 1392 1446 129 -541 -277 N ATOM 1075 CA ILE B 3 27.149 29.858 26.164 1.00 10.46 C ANISOU 1075 CA ILE B 3 1564 1559 854 -616 338 11 C ATOM 1076 C ILE B 3 27.142 30.496 24.786 1.00 9.47 C ANISOU 1076 C ILE B 3 1480 1229 888 -394 401 -55 C ATOM 1077 O ILE B 3 27.216 31.722 24.693 1.00 10.59 O ANISOU 1077 O ILE B 3 1435 1161 1426 -440 -416 57 O ATOM 1078 CB ILE B 3 25.752 29.469 26.650 1.00 14.76 C ANISOU 1078 CB ILE B 3 1463 2828 1316 -74 627 900 C ATOM 1079 CG1 ILE B 3 24.698 30.538 26.694 1.00 17.99 C ANISOU 1079 CG1 ILE B 3 1706 2663 2468 -37 100 -18 C ATOM 1080 CG2 ILE B 3 25.830 28.811 28.079 1.00 17.34 C ANISOU 1080 CG2 ILE B 3 2028 3934 625 -35 739 474 C ATOM 1081 CD1 ILE B 3 23.310 29.973 27.022 1.00 15.31 C ANISOU 1081 CD1 ILE B 3 1533 2044 2239 384 137 -17 C ATOM 1082 N ARG B 4 27.127 29.712 23.716 1.00 9.13 N ANISOU 1082 N ARG B 4 1176 1456 838 141 -245 -173 N ATOM 1083 CA ARG B 4 27.209 30.189 22.348 1.00 9.41 C ANISOU 1083 CA ARG B 4 1319 1395 862 -267 -307 -61 C ATOM 1084 C ARG B 4 26.281 29.418 21.427 1.00 7.43 C ANISOU 1084 C ARG B 4 1371 932 520 -629 -22 424 C ATOM 1085 O ARG B 4 26.113 28.201 21.551 1.00 8.71 O ANISOU 1085 O ARG B 4 1375 717 1219 -26 -305 254 O ATOM 1086 CB ARG B 4 28.649 30.015 21.808 1.00 10.83 C ANISOU 1086 CB ARG B 4 1318 1245 1550 -813 40 -13 C ATOM 1087 CG ARG B 4 29.790 30.711 22.530 1.00 11.44 C ANISOU 1087 CG ARG B 4 1676 1259 1413 -817 -284 -22 C ATOM 1088 CD ARG B 4 29.695 32.218 22.267 1.00 13.65 C ANISOU 1088 CD ARG B 4 2530 1049 1607 -448 -483 -531 C ATOM 1089 NE ARG B 4 30.680 33.017 23.025 1.00 11.72 N ANISOU 1089 NE ARG B 4 1832 975 1645 -643 -377 333 N ATOM 1090 CZ ARG B 4 30.603 34.343 23.014 1.00 10.53 C ANISOU 1090 CZ ARG B 4 1434 945 1623 -404 -307 -62 C ATOM 1091 NH1 ARG B 4 29.656 34.967 22.297 1.00 12.91 N ANISOU 1091 NH1 ARG B 4 1740 1900 1263 532 103 -5 N ATOM 1092 NH2 ARG B 4 31.472 35.075 23.697 1.00 16.09 N ANISOU 1092 NH2 ARG B 4 2023 1857 2233 -879 -271 -745 N ATOM 1093 N GLY B 5 25.690 30.160 20.492 1.00 8.23 N ANISOU 1093 N GLY B 5 1659 945 524 200 -272 -61 N ATOM 1094 CA GLY B 5 24.951 29.505 19.407 1.00 9.10 C ANISOU 1094 CA GLY B 5 1339 1452 669 211 -70 -468 C ATOM 1095 C GLY B 5 25.870 29.001 18.275 1.00 7.38 C ANISOU 1095 C GLY B 5 1715 665 423 -109 217 47 C ATOM 1096 O GLY B 5 26.861 29.634 17.885 1.00 9.44 O ANISOU 1096 O GLY B 5 1331 1099 1156 -86 145 -25 O ATOM 1097 N ILE B 6 25.513 27.796 17.836 1.00 8.62 N ANISOU 1097 N ILE B 6 1542 752 980 55 19 -270 N ATOM 1098 CA ILE B 6 26.198 27.178 16.696 1.00 8.70 C ANISOU 1098 CA ILE B 6 1697 830 779 484 -295 -201 C ATOM 1099 C ILE B 6 25.121 26.987 15.615 1.00 8.15 C ANISOU 1099 C ILE B 6 781 1723 592 592 219 -125 C ATOM 1100 O ILE B 6 24.076 26.355 15.790 1.00 9.78 O ANISOU 1100 O ILE B 6 1159 1524 1034 327 169 -101 O ATOM 1101 CB ILE B 6 26.929 25.839 16.936 1.00 9.69 C ANISOU 1101 CB ILE B 6 1305 1075 1304 545 5 179 C ATOM 1102 CG1 ILE B 6 27.719 25.913 18.233 1.00 11.07 C ANISOU 1102 CG1 ILE B 6 1081 1796 1330 674 24 513 C ATOM 1103 CG2 ILE B 6 27.833 25.406 15.762 1.00 10.62 C ANISOU 1103 CG2 ILE B 6 1478 870 1685 181 265 -208 C ATOM 1104 CD1 ILE B 6 28.542 24.661 18.545 1.00 12.64 C ANISOU 1104 CD1 ILE B 6 1315 1825 1664 970 46 259 C ATOM 1105 N ARG B 7 25.365 27.487 14.420 1.00 8.92 N ANISOU 1105 N ARG B 7 1361 1492 535 413 185 -288 N ATOM 1106 CA ARG B 7 24.461 27.424 13.284 1.00 9.67 C ANISOU 1106 CA ARG B 7 2092 948 636 393 -184 -281 C ATOM 1107 C ARG B 7 24.884 26.330 12.307 1.00 10.77 C ANISOU 1107 C ARG B 7 1505 1289 1298 290 -168 -752 C ATOM 1108 O ARG B 7 26.069 26.069 12.107 1.00 10.27 O ANISOU 1108 O ARG B 7 1495 1081 1325 167 115 -97 O ATOM 1109 CB ARG B 7 24.443 28.764 12.555 1.00 11.11 C ANISOU 1109 CB ARG B 7 1606 1209 1406 675 204 200 C ATOM 1110 CG ARG B 7 23.557 29.869 13.092 1.00 8.98 C ANISOU 1110 CG ARG B 7 1169 1206 1039 484 -114 -69 C ATOM 1111 CD ARG B 7 22.072 29.491 13.201 1.00 9.96 C ANISOU 1111 CD ARG B 7 1251 1376 1158 216 -8 -172 C ATOM 1112 NE ARG B 7 21.716 28.764 11.967 1.00 9.63 N ANISOU 1112 NE ARG B 7 1559 1123 977 28 -47 208 N ATOM 1113 CZ ARG B 7 21.694 29.288 10.759 1.00 10.67 C ANISOU 1113 CZ ARG B 7 1693 1196 1164 220 -483 405 C ATOM 1114 NH1 ARG B 7 21.896 30.599 10.592 1.00 9.65 N ANISOU 1114 NH1 ARG B 7 1507 1304 855 -29 342 319 N ATOM 1115 NH2 ARG B 7 21.413 28.509 9.740 1.00 12.12 N ANISOU 1115 NH2 ARG B 7 2250 1309 1046 78 66 256 N ATOM 1116 N GLY B 8 23.854 25.715 11.706 1.00 10.22 N ANISOU 1116 N GLY B 8 1668 1252 964 -12 -80 -450 N ATOM 1117 CA GLY B 8 24.170 24.918 10.539 1.00 11.09 C ANISOU 1117 CA GLY B 8 2247 1309 656 -30 -270 -301 C ATOM 1118 C GLY B 8 22.985 24.968 9.594 1.00 10.66 C ANISOU 1118 C GLY B 8 1833 1755 461 9 60 -139 C ATOM 1119 O GLY B 8 21.891 25.416 9.969 1.00 11.14 O ANISOU 1119 O GLY B 8 2049 1483 702 94 160 -489 O ATOM 1120 N ALA B 9 23.260 24.538 8.361 1.00 9.27 N ANISOU 1120 N ALA B 9 1787 1138 598 -5 81 -305 N ATOM 1121 CA ALA B 9 22.160 24.386 7.403 1.00 10.58 C ANISOU 1121 CA ALA B 9 2158 1034 827 -114 -184 -494 C ATOM 1122 C ALA B 9 22.517 23.280 6.418 1.00 11.02 C ANISOU 1122 C ALA B 9 1970 1467 749 -298 288 -621 C ATOM 1123 O ALA B 9 23.688 23.087 6.134 1.00 12.71 O ANISOU 1123 O ALA B 9 1969 1639 1221 -77 264 -236 O ATOM 1124 CB ALA B 9 21.867 25.646 6.613 1.00 12.58 C ANISOU 1124 CB ALA B 9 2515 1471 793 105 -310 -266 C ATOM 1125 N THR B 10 21.505 22.580 5.966 1.00 10.42 N ANISOU 1125 N THR B 10 2168 765 1026 -238 -61 -326 N ATOM 1126 CA THR B 10 21.660 21.536 4.937 1.00 10.96 C ANISOU 1126 CA THR B 10 2106 1265 792 -95 -78 -450 C ATOM 1127 C THR B 10 20.390 21.464 4.087 1.00 12.57 C ANISOU 1127 C THR B 10 1703 2077 996 -335 192 -715 C ATOM 1128 O THR B 10 19.431 22.198 4.363 1.00 12.38 O ANISOU 1128 O THR B 10 1852 1829 1025 -221 176 -531 O ATOM 1129 CB THR B 10 22.039 20.170 5.536 1.00 12.92 C ANISOU 1129 CB THR B 10 2087 972 1851 65 546 -485 C ATOM 1130 OG1 THR B 10 22.464 19.270 4.492 1.00 14.22 O ANISOU 1130 OG1 THR B 10 2112 1611 1681 197 471 -629 O ATOM 1131 CG2 THR B 10 20.868 19.503 6.261 1.00 10.91 C ANISOU 1131 CG2 THR B 10 1896 1062 1187 69 107 -393 C ATOM 1132 N THR B 11 20.420 20.650 3.029 1.00 12.03 N ANISOU 1132 N THR B 11 2248 1386 937 95 -363 -427 N ATOM 1133 CA THR B 11 19.244 20.522 2.179 1.00 12.16 C ANISOU 1133 CA THR B 11 2252 1581 785 -590 -230 83 C ATOM 1134 C THR B 11 18.994 19.044 1.866 1.00 11.58 C ANISOU 1134 C THR B 11 2223 1688 488 -538 299 -327 C ATOM 1135 O THR B 11 19.924 18.234 1.995 1.00 16.19 O ANISOU 1135 O THR B 11 2801 1940 1411 -147 -206 -753 O ATOM 1136 CB THR B 11 19.370 21.294 0.851 1.00 12.37 C ANISOU 1136 CB THR B 11 2460 1590 649 406 216 -34 C ATOM 1137 OG1 THR B 11 20.486 20.851 0.077 1.00 15.58 O ANISOU 1137 OG1 THR B 11 2468 2455 996 542 270 -171 O ATOM 1138 CG2 THR B 11 19.570 22.789 1.132 1.00 14.45 C ANISOU 1138 CG2 THR B 11 2646 1459 1386 235 364 336 C ATOM 1139 N VAL B 12 17.801 18.694 1.455 1.00 13.89 N ANISOU 1139 N VAL B 12 2598 1939 741 -737 -104 -414 N ATOM 1140 CA VAL B 12 17.425 17.368 0.945 1.00 14.41 C ANISOU 1140 CA VAL B 12 2813 1925 737 -541 -166 -635 C ATOM 1141 C VAL B 12 16.938 17.506 -0.510 1.00 15.47 C ANISOU 1141 C VAL B 12 3021 2002 855 -26 -293 -784 C ATOM 1142 O VAL B 12 16.451 18.581 -0.914 1.00 17.58 O ANISOU 1142 O VAL B 12 2916 2663 1102 566 -181 -609 O ATOM 1143 CB VAL B 12 16.381 16.650 1.831 1.00 13.38 C ANISOU 1143 CB VAL B 12 2527 1053 1503 5 -110 -179 C ATOM 1144 CG1 VAL B 12 16.881 16.413 3.248 1.00 16.74 C ANISOU 1144 CG1 VAL B 12 2114 2836 1410 176 173 235 C ATOM 1145 CG2 VAL B 12 15.096 17.453 1.984 1.00 15.08 C ANISOU 1145 CG2 VAL B 12 2650 1604 1476 270 -211 -344 C ATOM 1146 N GLU B 13 17.081 16.417 -1.275 1.00 16.65 N ANISOU 1146 N GLU B 13 3289 2307 730 -431 257 -1005 N ATOM 1147 CA GLU B 13 16.626 16.415 -2.674 1.00 17.56 C ANISOU 1147 CA GLU B 13 3033 2872 769 -331 273 -1062 C ATOM 1148 C GLU B 13 15.112 16.279 -2.742 1.00 19.07 C ANISOU 1148 C GLU B 13 3000 2875 1372 -141 116 279 C ATOM 1149 O GLU B 13 14.523 16.836 -3.686 1.00 21.20 O ANISOU 1149 O GLU B 13 3861 3053 1144 -451 -511 -56 O ATOM 1150 CB GLU B 13 17.365 15.329 -3.466 1.00 22.26 C ANISOU 1150 CB GLU B 13 3486 3804 1170 -100 264 -1746 C ATOM 1151 CG GLU B 13 18.831 15.717 -3.645 1.00 26.21 C ANISOU 1151 CG GLU B 13 3354 4832 1773 178 650 -1207 C ATOM 1152 CD GLU B 13 18.996 16.895 -4.580 1.00 31.78 C ANISOU 1152 CD GLU B 13 3886 6218 1973 -963 -187 -321 C ATOM 1153 OE1 GLU B 13 18.436 16.903 -5.692 1.00 42.34 O ANISOU 1153 OE1 GLU B 13 7731 6637 1719 119 -934 -1122 O ATOM 1154 OE2 GLU B 13 19.688 17.867 -4.227 1.00 39.78 O ANISOU 1154 OE2 GLU B 13 5065 6345 3704 -1694 -622 138 O ATOM 1155 N ARG B 14 14.526 15.588 -1.765 1.00 18.44 N ANISOU 1155 N ARG B 14 3431 2476 1098 -597 219 -313 N ATOM 1156 CA ARG B 14 13.115 15.267 -1.708 1.00 20.29 C ANISOU 1156 CA ARG B 14 3688 2376 1646 -1245 420 -1251 C ATOM 1157 C ARG B 14 12.665 15.186 -0.253 1.00 19.06 C ANISOU 1157 C ARG B 14 3202 2389 1653 -1076 170 -309 C ATOM 1158 O ARG B 14 13.456 14.897 0.625 1.00 20.26 O ANISOU 1158 O ARG B 14 3453 2180 2065 -710 -101 -404 O ATOM 1159 CB ARG B 14 12.708 13.929 -2.360 1.00 29.07 C ANISOU 1159 CB ARG B 14 4614 2241 4189 -773 711 -2305 C ATOM 1160 CG ARG B 14 13.836 12.986 -2.691 1.00 44.84 C ANISOU 1160 CG ARG B 14 6032 4172 6834 586 1256 -3036 C ATOM 1161 CD ARG B 14 14.331 13.106 -4.113 1.00 57.33 C ANISOU 1161 CD ARG B 14 7885 6412 7484 1653 2714 -3509 C ATOM 1162 NE ARG B 14 15.107 12.023 -4.660 1.00 64.11 N ANISOU 1162 NE ARG B 14 8794 6626 8938 2245 2953 -3602 N ATOM 1163 CZ ARG B 14 16.326 11.546 -4.576 1.00 63.26 C ANISOU 1163 CZ ARG B 14 8568 5816 9653 1809 2662 -4068 C ATOM 1164 NH1 ARG B 14 17.254 12.091 -3.802 1.00 63.41 N ANISOU 1164 NH1 ARG B 14 11074 2453 10564 849 -238 -51 N ATOM 1165 NH2 ARG B 14 16.688 10.463 -5.282 1.00 76.52 N ANISOU 1165 NH2 ARG B 14 10677 6601 11794 2772 3371 -4832 N ATOM 1166 N ASP B 15 11.369 15.449 -0.139 1.00 17.27 N ANISOU 1166 N ASP B 15 3378 2182 1004 -774 -28 -859 N ATOM 1167 CA ASP B 15 10.764 15.448 1.182 1.00 16.91 C ANISOU 1167 CA ASP B 15 3475 2005 944 -143 -103 -771 C ATOM 1168 C ASP B 15 10.421 14.016 1.545 1.00 17.48 C ANISOU 1168 C ASP B 15 2847 2358 1436 -521 209 -602 C ATOM 1169 O ASP B 15 9.275 13.614 1.340 1.00 20.58 O ANISOU 1169 O ASP B 15 3100 2842 1876 -561 -582 -722 O ATOM 1170 CB ASP B 15 9.524 16.331 1.129 1.00 19.07 C ANISOU 1170 CB ASP B 15 2826 2596 1824 -382 -126 -380 C ATOM 1171 CG ASP B 15 8.768 16.282 2.429 1.00 15.21 C ANISOU 1171 CG ASP B 15 2171 2027 1580 -661 -556 -654 C ATOM 1172 OD1 ASP B 15 9.416 16.033 3.466 1.00 15.52 O ANISOU 1172 OD1 ASP B 15 2231 1842 1824 -298 -545 -356 O ATOM 1173 OD2 ASP B 15 7.530 16.480 2.401 1.00 20.29 O ANISOU 1173 OD2 ASP B 15 2300 3756 1654 -38 -675 -748 O ATOM 1174 N THR B 16 11.425 13.275 2.012 1.00 15.58 N ANISOU 1174 N THR B 16 2794 1526 1600 -1039 -231 -720 N ATOM 1175 CA THR B 16 11.156 11.916 2.483 1.00 17.04 C ANISOU 1175 CA THR B 16 3595 1480 1400 -1310 63 -952 C ATOM 1176 C THR B 16 11.757 11.806 3.887 1.00 14.60 C ANISOU 1176 C THR B 16 2167 1772 1608 -387 282 -677 C ATOM 1177 O THR B 16 12.720 12.516 4.219 1.00 16.80 O ANISOU 1177 O THR B 16 2757 1815 1811 -637 -232 -448 O ATOM 1178 CB THR B 16 11.735 10.778 1.624 1.00 21.11 C ANISOU 1178 CB THR B 16 3993 1841 2188 -364 -736 -1310 C ATOM 1179 OG1 THR B 16 13.179 10.776 1.704 1.00 20.42 O ANISOU 1179 OG1 THR B 16 3985 1847 1928 -235 -693 -722 O ATOM 1180 CG2 THR B 16 11.410 10.935 0.144 1.00 27.45 C ANISOU 1180 CG2 THR B 16 3737 4729 1964 324 -694 -2292 C ATOM 1181 N GLU B 17 11.230 10.899 4.712 1.00 15.55 N ANISOU 1181 N GLU B 17 2954 1379 1575 -296 361 -747 N ATOM 1182 CA GLU B 17 11.870 10.781 6.005 1.00 16.06 C ANISOU 1182 CA GLU B 17 2805 1343 1954 -399 8 -497 C ATOM 1183 C GLU B 17 13.328 10.351 5.948 1.00 15.19 C ANISOU 1183 C GLU B 17 2762 666 2342 -655 209 -695 C ATOM 1184 O GLU B 17 14.142 10.891 6.705 1.00 18.47 O ANISOU 1184 O GLU B 17 2690 1211 3118 -698 85 -1173 O ATOM 1185 CB GLU B 17 11.095 9.729 6.827 1.00 14.93 C ANISOU 1185 CB GLU B 17 2647 1429 1597 -401 175 -748 C ATOM 1186 CG GLU B 17 11.791 9.548 8.164 1.00 19.28 C ANISOU 1186 CG GLU B 17 3635 2602 1088 -933 221 -940 C ATOM 1187 CD GLU B 17 11.148 8.479 9.011 1.00 19.60 C ANISOU 1187 CD GLU B 17 3131 2441 1874 -225 167 -272 C ATOM 1188 OE1 GLU B 17 10.616 7.484 8.490 1.00 24.23 O ANISOU 1188 OE1 GLU B 17 4592 1509 3107 -91 78 -218 O ATOM 1189 OE2 GLU B 17 11.187 8.637 10.265 1.00 19.29 O ANISOU 1189 OE2 GLU B 17 2661 2862 1806 709 472 65 O ATOM 1190 N GLU B 18 13.665 9.382 5.099 1.00 18.40 N ANISOU 1190 N GLU B 18 3642 987 2362 82 -278 -852 N ATOM 1191 CA GLU B 18 15.044 8.883 5.037 1.00 18.12 C ANISOU 1191 CA GLU B 18 3646 1103 2138 58 -19 -808 C ATOM 1192 C GLU B 18 15.964 10.061 4.741 1.00 19.38 C ANISOU 1192 C GLU B 18 3730 1247 2389 -92 -127 -868 C ATOM 1193 O GLU B 18 17.011 10.191 5.362 1.00 19.64 O ANISOU 1193 O GLU B 18 3295 2307 1860 -156 367 -866 O ATOM 1194 CB AGLU B 18 15.288 7.767 4.011 0.66 24.84 C ANISOU 1194 CB AGLU B 18 5269 774 3394 343 536 -1050 C ATOM 1195 CB BGLU B 18 15.197 7.773 4.003 0.34 24.51 C ANISOU 1195 CB BGLU B 18 5140 873 3298 116 685 -1125 C ATOM 1196 CG AGLU B 18 16.671 7.144 4.071 0.66 27.95 C ANISOU 1196 CG AGLU B 18 5257 1718 3644 600 1086 -1065 C ATOM 1197 CG BGLU B 18 16.287 6.753 4.244 0.34 28.10 C ANISOU 1197 CG BGLU B 18 5515 1581 3579 677 873 -1045 C ATOM 1198 CD AGLU B 18 17.791 7.753 3.262 0.66 32.17 C ANISOU 1198 CD AGLU B 18 5586 2582 4054 731 1148 14 C ATOM 1199 CD BGLU B 18 17.694 7.282 4.351 0.34 30.94 C ANISOU 1199 CD BGLU B 18 5301 2538 3917 748 898 -499 C ATOM 1200 OE1AGLU B 18 17.566 8.731 2.517 0.66 36.91 O ANISOU 1200 OE1AGLU B 18 7812 3662 2550 -535 -761 200 O ATOM 1201 OE1BGLU B 18 18.049 8.269 3.662 0.34 34.59 O ANISOU 1201 OE1BGLU B 18 6612 2135 4394 -145 1135 -1047 O ATOM 1202 OE2AGLU B 18 18.961 7.273 3.331 0.66 39.85 O ANISOU 1202 OE2AGLU B 18 5438 4391 5312 1052 1675 -636 O ATOM 1203 OE2BGLU B 18 18.485 6.736 5.155 0.34 36.30 O ANISOU 1203 OE2BGLU B 18 6995 3847 2951 274 -839 -1518 O ATOM 1204 N GLU B 19 15.597 10.921 3.789 1.00 19.29 N ANISOU 1204 N GLU B 19 3336 1340 2653 -312 73 -593 N ATOM 1205 CA GLU B 19 16.500 12.017 3.425 1.00 16.72 C ANISOU 1205 CA GLU B 19 2613 1551 2189 -195 94 -858 C ATOM 1206 C GLU B 19 16.627 13.055 4.520 1.00 15.78 C ANISOU 1206 C GLU B 19 2581 1366 2049 -252 453 -667 C ATOM 1207 O GLU B 19 17.723 13.483 4.921 1.00 15.75 O ANISOU 1207 O GLU B 19 2673 1476 1835 -597 647 -766 O ATOM 1208 CB GLU B 19 16.020 12.628 2.100 1.00 19.10 C ANISOU 1208 CB GLU B 19 3570 1379 2308 -429 -97 -704 C ATOM 1209 CG GLU B 19 16.400 11.728 0.930 1.00 22.55 C ANISOU 1209 CG GLU B 19 4470 1964 2133 -909 540 -756 C ATOM 1210 CD GLU B 19 16.234 12.280 -0.461 1.00 25.97 C ANISOU 1210 CD GLU B 19 4809 2776 2284 431 -210 -827 C ATOM 1211 OE1 GLU B 19 16.258 13.510 -0.648 1.00 27.86 O ANISOU 1211 OE1 GLU B 19 6198 2926 1462 -405 -683 -618 O ATOM 1212 OE2 GLU B 19 16.112 11.454 -1.410 1.00 31.42 O ANISOU 1212 OE2 GLU B 19 6930 3044 1966 -1226 1132 -778 O ATOM 1213 N ILE B 20 15.490 13.516 5.039 1.00 16.64 N ANISOU 1213 N ILE B 20 2541 2207 1577 414 -284 -787 N ATOM 1214 CA ILE B 20 15.538 14.455 6.162 1.00 13.58 C ANISOU 1214 CA ILE B 20 2144 1716 1299 69 -27 -435 C ATOM 1215 C ILE B 20 16.365 13.919 7.320 1.00 12.46 C ANISOU 1215 C ILE B 20 2061 1223 1449 69 -48 -505 C ATOM 1216 O ILE B 20 17.186 14.648 7.850 1.00 12.28 O ANISOU 1216 O ILE B 20 1623 1510 1534 -177 54 -147 O ATOM 1217 CB ILE B 20 14.096 14.828 6.605 1.00 14.07 C ANISOU 1217 CB ILE B 20 2035 2280 1033 44 -231 -555 C ATOM 1218 CG1 ILE B 20 13.327 15.567 5.506 1.00 15.17 C ANISOU 1218 CG1 ILE B 20 2469 1913 1381 363 -112 -389 C ATOM 1219 CG2 ILE B 20 14.149 15.588 7.904 1.00 14.58 C ANISOU 1219 CG2 ILE B 20 2655 1766 1121 -263 308 -482 C ATOM 1220 CD1 ILE B 20 11.867 15.770 5.791 1.00 16.02 C ANISOU 1220 CD1 ILE B 20 2058 1909 2120 -238 -653 -636 C ATOM 1221 N LEU B 21 16.212 12.636 7.685 1.00 14.27 N ANISOU 1221 N LEU B 21 2587 1321 1513 -157 54 -442 N ATOM 1222 CA LEU B 21 16.929 12.117 8.838 1.00 13.49 C ANISOU 1222 CA LEU B 21 2086 1280 1759 -62 312 -126 C ATOM 1223 C LEU B 21 18.412 12.002 8.505 1.00 13.09 C ANISOU 1223 C LEU B 21 2037 1405 1533 -661 378 -545 C ATOM 1224 O LEU B 21 19.272 12.382 9.311 1.00 13.38 O ANISOU 1224 O LEU B 21 2258 981 1844 -1 -242 -344 O ATOM 1225 CB LEU B 21 16.351 10.757 9.292 1.00 13.60 C ANISOU 1225 CB LEU B 21 1713 1671 1783 -624 68 -136 C ATOM 1226 CG LEU B 21 14.938 10.806 9.918 1.00 12.69 C ANISOU 1226 CG LEU B 21 1779 937 2105 -24 196 -557 C ATOM 1227 CD1 LEU B 21 14.579 9.412 10.380 1.00 17.32 C ANISOU 1227 CD1 LEU B 21 2753 1387 2440 -965 1143 -764 C ATOM 1228 CD2 LEU B 21 14.801 11.847 11.037 1.00 15.58 C ANISOU 1228 CD2 LEU B 21 2574 1251 2095 282 -457 -754 C ATOM 1229 N GLN B 22 18.688 11.482 7.294 1.00 13.95 N ANISOU 1229 N GLN B 22 2460 1316 1524 -100 363 -466 N ATOM 1230 CA GLN B 22 20.098 11.292 6.982 1.00 16.38 C ANISOU 1230 CA GLN B 22 2573 1181 2471 148 640 -786 C ATOM 1231 C GLN B 22 20.874 12.591 6.950 1.00 15.31 C ANISOU 1231 C GLN B 22 2301 1291 2227 202 764 -721 C ATOM 1232 O GLN B 22 22.006 12.767 7.439 1.00 17.22 O ANISOU 1232 O GLN B 22 2337 1057 3148 177 530 -235 O ATOM 1233 CB GLN B 22 20.251 10.652 5.592 1.00 18.88 C ANISOU 1233 CB GLN B 22 3152 1347 2673 -359 1253 -897 C ATOM 1234 CG GLN B 22 21.712 10.354 5.300 1.00 24.53 C ANISOU 1234 CG GLN B 22 3457 2244 3619 -168 1988 -836 C ATOM 1235 CD GLN B 22 21.952 9.848 3.893 1.00 28.65 C ANISOU 1235 CD GLN B 22 4792 2308 3784 568 2281 -896 C ATOM 1236 OE1 GLN B 22 21.649 10.567 2.941 1.00 43.69 O ANISOU 1236 OE1 GLN B 22 10440 2448 3713 -1004 898 -607 O ATOM 1237 NE2 GLN B 22 22.484 8.644 3.753 1.00 38.18 N ANISOU 1237 NE2 GLN B 22 4060 3688 6758 1717 439 -2832 N ATOM 1238 N LYS B 23 20.264 13.600 6.303 1.00 14.76 N ANISOU 1238 N LYS B 23 2277 1312 2017 113 703 -615 N ATOM 1239 CA LYS B 23 20.991 14.849 6.154 1.00 14.24 C ANISOU 1239 CA LYS B 23 2242 1600 1567 -133 512 -530 C ATOM 1240 C LYS B 23 21.016 15.632 7.463 1.00 12.12 C ANISOU 1240 C LYS B 23 2001 1248 1354 85 429 -253 C ATOM 1241 O LYS B 23 22.005 16.325 7.747 1.00 13.16 O ANISOU 1241 O LYS B 23 2107 1670 1224 -165 349 -165 O ATOM 1242 CB LYS B 23 20.379 15.724 5.069 1.00 15.14 C ANISOU 1242 CB LYS B 23 2385 2300 1066 -600 875 -70 C ATOM 1243 CG LYS B 23 20.488 15.118 3.687 1.00 17.02 C ANISOU 1243 CG LYS B 23 2019 3147 1300 -764 1019 -561 C ATOM 1244 CD LYS B 23 21.821 14.388 3.483 1.00 27.20 C ANISOU 1244 CD LYS B 23 2431 6081 1823 298 1107 -1052 C ATOM 1245 CE LYS B 23 22.034 13.895 2.055 1.00 30.45 C ANISOU 1245 CE LYS B 23 3621 5637 2314 483 1310 -1592 C ATOM 1246 NZ LYS B 23 23.446 13.495 1.778 1.00 31.89 N ANISOU 1246 NZ LYS B 23 3692 5916 2510 296 1750 -1519 N ATOM 1247 N THR B 24 19.966 15.535 8.245 1.00 12.44 N ANISOU 1247 N THR B 24 1679 1516 1530 530 376 -136 N ATOM 1248 CA THR B 24 20.006 16.185 9.587 1.00 10.80 C ANISOU 1248 CA THR B 24 1709 957 1438 470 409 79 C ATOM 1249 C THR B 24 21.076 15.543 10.442 1.00 11.90 C ANISOU 1249 C THR B 24 1763 910 1849 542 83 -230 C ATOM 1250 O THR B 24 21.872 16.201 11.122 1.00 12.33 O ANISOU 1250 O THR B 24 1575 1144 1965 202 242 -97 O ATOM 1251 CB THR B 24 18.641 16.100 10.276 1.00 12.23 C ANISOU 1251 CB THR B 24 1724 1302 1623 570 507 -66 C ATOM 1252 OG1 THR B 24 17.660 16.823 9.495 1.00 11.98 O ANISOU 1252 OG1 THR B 24 1629 1387 1535 306 125 -342 O ATOM 1253 CG2 THR B 24 18.697 16.742 11.653 1.00 10.90 C ANISOU 1253 CG2 THR B 24 1748 1186 1207 281 405 378 C ATOM 1254 N LYS B 25 21.137 14.205 10.414 1.00 12.79 N ANISOU 1254 N LYS B 25 1842 880 2136 353 16 224 N ATOM 1255 CA LYS B 25 22.139 13.483 11.212 1.00 11.47 C ANISOU 1255 CA LYS B 25 1724 950 1684 344 165 177 C ATOM 1256 C LYS B 25 23.527 13.859 10.749 1.00 12.48 C ANISOU 1256 C LYS B 25 1733 1179 1830 483 398 -536 C ATOM 1257 O LYS B 25 24.427 14.103 11.561 1.00 13.22 O ANISOU 1257 O LYS B 25 1699 1262 2063 142 360 -456 O ATOM 1258 CB LYS B 25 21.895 11.969 11.107 1.00 14.77 C ANISOU 1258 CB LYS B 25 2485 810 2316 701 1120 360 C ATOM 1259 CG LYS B 25 22.986 11.169 11.815 1.00 14.38 C ANISOU 1259 CG LYS B 25 2623 761 2081 531 667 57 C ATOM 1260 CD LYS B 25 22.849 9.681 11.537 1.00 19.75 C ANISOU 1260 CD LYS B 25 3700 764 3041 827 -369 48 C ATOM 1261 CE LYS B 25 23.446 9.395 10.152 1.00 29.85 C ANISOU 1261 CE LYS B 25 5424 2065 3853 786 193 -1625 C ATOM 1262 NZ LYS B 25 23.402 7.943 9.821 1.00 46.15 N ANISOU 1262 NZ LYS B 25 8295 2364 6876 2329 -1761 -2819 N ATOM 1263 N GLN B 26 23.740 13.896 9.421 1.00 12.63 N ANISOU 1263 N GLN B 26 1850 1072 1878 226 480 -323 N ATOM 1264 CA GLN B 26 25.087 14.202 8.944 1.00 12.95 C ANISOU 1264 CA GLN B 26 1957 950 2013 275 631 -531 C ATOM 1265 C GLN B 26 25.477 15.609 9.349 1.00 12.83 C ANISOU 1265 C GLN B 26 1831 1053 1990 207 522 -505 C ATOM 1266 O GLN B 26 26.631 15.898 9.693 1.00 14.64 O ANISOU 1266 O GLN B 26 1940 1709 1913 -160 493 -394 O ATOM 1267 CB GLN B 26 25.154 14.052 7.414 1.00 14.23 C ANISOU 1267 CB GLN B 26 2574 873 1961 -112 711 -412 C ATOM 1268 CG GLN B 26 25.142 12.571 6.991 1.00 17.79 C ANISOU 1268 CG GLN B 26 3871 914 1975 266 723 -482 C ATOM 1269 CD GLN B 26 25.097 12.350 5.487 1.00 17.84 C ANISOU 1269 CD GLN B 26 3701 1098 1979 -404 296 -480 C ATOM 1270 OE1 GLN B 26 24.833 13.270 4.685 1.00 25.27 O ANISOU 1270 OE1 GLN B 26 5852 1667 2085 61 1285 151 O ATOM 1271 NE2 GLN B 26 25.368 11.107 5.111 1.00 22.57 N ANISOU 1271 NE2 GLN B 26 4946 1526 2102 307 372 -785 N ATOM 1272 N LEU B 27 24.518 16.533 9.281 1.00 12.25 N ANISOU 1272 N LEU B 27 2346 693 1614 268 447 -198 N ATOM 1273 CA LEU B 27 24.787 17.939 9.648 1.00 10.90 C ANISOU 1273 CA LEU B 27 1799 830 1512 100 81 -187 C ATOM 1274 C LEU B 27 25.158 18.046 11.127 1.00 12.17 C ANISOU 1274 C LEU B 27 1635 1537 1451 45 76 -137 C ATOM 1275 O LEU B 27 26.164 18.706 11.461 1.00 12.03 O ANISOU 1275 O LEU B 27 1887 1087 1596 27 141 -369 O ATOM 1276 CB LEU B 27 23.601 18.829 9.365 1.00 11.21 C ANISOU 1276 CB LEU B 27 1944 387 1930 -58 -91 136 C ATOM 1277 CG LEU B 27 23.639 20.295 9.787 1.00 9.36 C ANISOU 1277 CG LEU B 27 1744 479 1333 -152 -12 104 C ATOM 1278 CD1 LEU B 27 24.710 21.064 9.055 1.00 15.75 C ANISOU 1278 CD1 LEU B 27 2426 680 2879 -553 811 -153 C ATOM 1279 CD2 LEU B 27 22.306 21.045 9.620 1.00 12.73 C ANISOU 1279 CD2 LEU B 27 2099 1097 1639 489 2 -616 C ATOM 1280 N LEU B 28 24.350 17.396 11.963 1.00 11.00 N ANISOU 1280 N LEU B 28 1432 1317 1430 310 195 -348 N ATOM 1281 CA LEU B 28 24.663 17.397 13.399 1.00 11.04 C ANISOU 1281 CA LEU B 28 1475 1246 1474 397 156 -45 C ATOM 1282 C LEU B 28 26.025 16.773 13.666 1.00 11.23 C ANISOU 1282 C LEU B 28 1433 706 2127 143 -178 -324 C ATOM 1283 O LEU B 28 26.868 17.320 14.389 1.00 11.50 O ANISOU 1283 O LEU B 28 1459 1178 1733 -102 101 -325 O ATOM 1284 CB LEU B 28 23.605 16.618 14.193 1.00 12.95 C ANISOU 1284 CB LEU B 28 1733 1417 1769 237 355 77 C ATOM 1285 CG LEU B 28 23.886 16.535 15.705 1.00 18.71 C ANISOU 1285 CG LEU B 28 2409 2649 2053 171 -199 1329 C ATOM 1286 CD1 LEU B 28 24.159 17.925 16.283 1.00 21.38 C ANISOU 1286 CD1 LEU B 28 2558 4019 1545 738 -367 -418 C ATOM 1287 CD2 LEU B 28 22.757 15.872 16.475 1.00 29.73 C ANISOU 1287 CD2 LEU B 28 3524 4547 3228 531 1248 2232 C ATOM 1288 N GLU B 29 26.330 15.638 13.066 1.00 12.38 N ANISOU 1288 N GLU B 29 1694 882 2127 278 118 -353 N ATOM 1289 CA GLU B 29 27.628 14.977 13.256 1.00 13.26 C ANISOU 1289 CA GLU B 29 1732 1046 2258 385 203 -161 C ATOM 1290 C GLU B 29 28.793 15.879 12.858 1.00 13.52 C ANISOU 1290 C GLU B 29 1667 1221 2249 387 151 -132 C ATOM 1291 O GLU B 29 29.822 15.898 13.534 1.00 14.72 O ANISOU 1291 O GLU B 29 1522 1471 2601 594 138 -494 O ATOM 1292 CB GLU B 29 27.651 13.631 12.506 1.00 14.25 C ANISOU 1292 CB GLU B 29 1948 1041 2424 505 262 -207 C ATOM 1293 CG GLU B 29 26.684 12.632 13.154 1.00 13.79 C ANISOU 1293 CG GLU B 29 2104 1079 2055 266 -251 -113 C ATOM 1294 CD GLU B 29 26.663 11.295 12.458 1.00 16.29 C ANISOU 1294 CD GLU B 29 2547 1115 2528 338 -609 -276 C ATOM 1295 OE1 GLU B 29 27.115 11.237 11.287 1.00 31.64 O ANISOU 1295 OE1 GLU B 29 5664 2212 4145 -946 1951 -1727 O ATOM 1296 OE2 GLU B 29 26.187 10.310 13.077 1.00 20.50 O ANISOU 1296 OE2 GLU B 29 2913 1188 3689 -14 -713 8 O ATOM 1297 N LYS B 30 28.639 16.610 11.750 1.00 13.45 N ANISOU 1297 N LYS B 30 2262 927 1922 247 401 -394 N ATOM 1298 CA LYS B 30 29.746 17.503 11.367 1.00 16.00 C ANISOU 1298 CA LYS B 30 2579 1514 1986 -144 863 -733 C ATOM 1299 C LYS B 30 29.885 18.655 12.350 1.00 14.08 C ANISOU 1299 C LYS B 30 1807 1570 1974 -106 802 -730 C ATOM 1300 O LYS B 30 31.008 19.073 12.686 1.00 13.95 O ANISOU 1300 O LYS B 30 1908 1745 1649 -286 657 -166 O ATOM 1301 CB LYS B 30 29.538 18.037 9.951 1.00 15.32 C ANISOU 1301 CB LYS B 30 2271 1594 1957 -461 872 -720 C ATOM 1302 CG LYS B 30 30.720 18.828 9.407 1.00 20.76 C ANISOU 1302 CG LYS B 30 2623 1340 3925 -77 1675 19 C ATOM 1303 CD LYS B 30 31.927 17.941 9.160 1.00 24.00 C ANISOU 1303 CD LYS B 30 2461 1951 4709 -144 1482 -1362 C ATOM 1304 CE LYS B 30 33.053 18.642 8.438 1.00 31.45 C ANISOU 1304 CE LYS B 30 3019 2583 6346 179 2566 -834 C ATOM 1305 NZ LYS B 30 34.369 17.972 8.670 1.00 36.92 N ANISOU 1305 NZ LYS B 30 2892 4524 6611 526 2617 -547 N ATOM 1306 N ILE B 31 28.772 19.211 12.822 1.00 12.38 N ANISOU 1306 N ILE B 31 1889 1163 1650 122 633 -314 N ATOM 1307 CA ILE B 31 28.846 20.286 13.802 1.00 10.93 C ANISOU 1307 CA ILE B 31 1288 1260 1605 577 129 -263 C ATOM 1308 C ILE B 31 29.580 19.772 15.039 1.00 10.23 C ANISOU 1308 C ILE B 31 899 841 2148 246 -90 20 C ATOM 1309 O ILE B 31 30.433 20.456 15.591 1.00 12.73 O ANISOU 1309 O ILE B 31 1029 1524 2283 -263 -104 221 O ATOM 1310 CB AILE B 31 27.457 20.843 14.176 0.50 10.44 C ANISOU 1310 CB AILE B 31 1219 1073 1675 627 29 29 C ATOM 1311 CB BILE B 31 27.451 20.791 14.237 0.50 9.49 C ANISOU 1311 CB BILE B 31 1089 998 1520 491 -183 -204 C ATOM 1312 CG1AILE B 31 26.947 21.910 13.222 0.50 10.51 C ANISOU 1312 CG1AILE B 31 1196 734 2064 -13 -348 184 C ATOM 1313 CG1BILE B 31 26.651 21.242 13.042 0.50 6.81 C ANISOU 1313 CG1BILE B 31 1106 201 1280 -110 -75 -51 C ATOM 1314 CG2AILE B 31 27.444 21.364 15.617 0.50 10.05 C ANISOU 1314 CG2AILE B 31 1009 1212 1597 23 606 93 C ATOM 1315 CG2BILE B 31 27.534 21.858 15.325 0.50 9.81 C ANISOU 1315 CG2BILE B 31 2070 1107 552 472 324 148 C ATOM 1316 CD1AILE B 31 26.415 21.456 11.906 0.50 28.49 C ANISOU 1316 CD1AILE B 31 5038 2953 2832 -861 -2355 511 C ATOM 1317 CD1BILE B 31 25.334 21.917 13.269 0.50 4.65 C ANISOU 1317 CD1BILE B 31 1121 384 262 78 -299 -154 C ATOM 1318 N ILE B 32 29.213 18.566 15.471 1.00 13.38 N ANISOU 1318 N ILE B 32 1810 698 2577 206 250 67 N ATOM 1319 CA ILE B 32 29.862 18.014 16.662 1.00 14.09 C ANISOU 1319 CA ILE B 32 1371 1024 2958 402 375 481 C ATOM 1320 C ILE B 32 31.344 17.825 16.443 1.00 16.06 C ANISOU 1320 C ILE B 32 1306 1064 3733 222 324 -458 C ATOM 1321 O ILE B 32 32.176 18.152 17.303 1.00 16.31 O ANISOU 1321 O ILE B 32 1623 806 3767 -22 -48 227 O ATOM 1322 CB ILE B 32 29.197 16.669 17.056 1.00 15.60 C ANISOU 1322 CB ILE B 32 1910 1402 2616 5 387 545 C ATOM 1323 CG1 ILE B 32 27.746 16.859 17.527 1.00 12.10 C ANISOU 1323 CG1 ILE B 32 1693 1114 1792 -210 -13 178 C ATOM 1324 CG2 ILE B 32 30.042 15.907 18.059 1.00 18.17 C ANISOU 1324 CG2 ILE B 32 1967 652 4287 30 -290 598 C ATOM 1325 CD1 ILE B 32 26.938 15.554 17.402 1.00 17.83 C ANISOU 1325 CD1 ILE B 32 2491 1225 3059 -583 369 -88 C ATOM 1326 N GLU B 33 31.693 17.313 15.260 1.00 16.54 N ANISOU 1326 N GLU B 33 1527 904 3852 394 492 -330 N ATOM 1327 CA GLU B 33 33.120 17.076 14.995 1.00 17.12 C ANISOU 1327 CA GLU B 33 1557 1177 3770 581 621 23 C ATOM 1328 C GLU B 33 33.887 18.378 14.956 1.00 15.02 C ANISOU 1328 C GLU B 33 1608 1546 2552 292 808 40 C ATOM 1329 O GLU B 33 34.986 18.471 15.520 1.00 16.45 O ANISOU 1329 O GLU B 33 2116 1588 2547 372 293 -196 O ATOM 1330 CB GLU B 33 33.346 16.423 13.645 1.00 21.29 C ANISOU 1330 CB GLU B 33 1377 2189 4522 830 183 -1108 C ATOM 1331 CG GLU B 33 34.807 16.284 13.224 1.00 34.11 C ANISOU 1331 CG GLU B 33 2227 4883 5852 1186 1654 -1052 C ATOM 1332 CD GLU B 33 35.181 17.107 12.009 1.00 42.38 C ANISOU 1332 CD GLU B 33 3131 6354 6616 911 2128 -234 C ATOM 1333 OE1 GLU B 33 34.290 17.489 11.215 1.00 58.86 O ANISOU 1333 OE1 GLU B 33 4716 10329 7320 613 1287 1901 O ATOM 1334 OE2 GLU B 33 36.398 17.371 11.853 1.00 53.84 O ANISOU 1334 OE2 GLU B 33 4133 7700 8625 -1529 1780 78 O ATOM 1335 N GLU B 34 33.345 19.391 14.260 1.00 15.36 N ANISOU 1335 N GLU B 34 1426 926 3484 170 173 -467 N ATOM 1336 CA GLU B 34 34.104 20.643 14.147 1.00 14.67 C ANISOU 1336 CA GLU B 34 1585 1349 2638 -134 622 -252 C ATOM 1337 C GLU B 34 34.158 21.433 15.450 1.00 12.86 C ANISOU 1337 C GLU B 34 1635 743 2507 -370 642 87 C ATOM 1338 O GLU B 34 35.143 22.177 15.656 1.00 15.55 O ANISOU 1338 O GLU B 34 1583 1324 3001 -442 543 -178 O ATOM 1339 CB GLU B 34 33.502 21.557 13.066 1.00 17.85 C ANISOU 1339 CB GLU B 34 2344 2185 2253 53 1066 250 C ATOM 1340 CG GLU B 34 33.490 20.917 11.685 1.00 21.58 C ANISOU 1340 CG GLU B 34 2065 3712 2421 -304 913 -249 C ATOM 1341 CD GLU B 34 33.224 21.962 10.612 1.00 24.42 C ANISOU 1341 CD GLU B 34 4452 2855 1969 -970 580 -758 C ATOM 1342 OE1 GLU B 34 33.051 21.532 9.467 1.00 38.20 O ANISOU 1342 OE1 GLU B 34 7592 5024 1898 1611 303 -1460 O ATOM 1343 OE2 GLU B 34 33.193 23.196 10.882 1.00 32.63 O ANISOU 1343 OE2 GLU B 34 5261 2809 4329 -815 1077 -971 O ATOM 1344 N ASN B 35 33.126 21.300 16.281 1.00 12.39 N ANISOU 1344 N ASN B 35 1108 1140 2459 203 417 14 N ATOM 1345 CA ASN B 35 33.115 22.116 17.504 1.00 14.11 C ANISOU 1345 CA ASN B 35 1476 1385 2500 307 325 -60 C ATOM 1346 C ASN B 35 33.488 21.303 18.732 1.00 13.09 C ANISOU 1346 C ASN B 35 1150 1355 2470 533 277 -195 C ATOM 1347 O ASN B 35 33.535 21.896 19.809 1.00 14.70 O ANISOU 1347 O ASN B 35 1938 1135 2513 -177 167 -208 O ATOM 1348 CB ASN B 35 31.749 22.785 17.705 1.00 11.14 C ANISOU 1348 CB ASN B 35 1415 853 1964 220 25 -64 C ATOM 1349 CG ASN B 35 31.570 23.843 16.621 1.00 12.80 C ANISOU 1349 CG ASN B 35 1559 1192 2113 -249 -57 264 C ATOM 1350 OD1 ASN B 35 32.094 24.952 16.725 1.00 12.37 O ANISOU 1350 OD1 ASN B 35 1458 1248 1995 -282 647 47 O ATOM 1351 ND2 ASN B 35 30.835 23.467 15.573 1.00 12.17 N ANISOU 1351 ND2 ASN B 35 1488 1214 1924 172 60 42 N ATOM 1352 N HIS B 36 33.757 20.030 18.600 1.00 12.84 N ANISOU 1352 N HIS B 36 1144 1189 2544 213 508 -118 N ATOM 1353 CA HIS B 36 34.109 19.136 19.698 1.00 15.27 C ANISOU 1353 CA HIS B 36 773 1813 3216 351 232 473 C ATOM 1354 C HIS B 36 32.991 19.090 20.746 1.00 13.07 C ANISOU 1354 C HIS B 36 915 1666 2385 184 4 125 C ATOM 1355 O HIS B 36 33.273 19.036 21.944 1.00 17.73 O ANISOU 1355 O HIS B 36 1597 2544 2595 29 -524 723 O ATOM 1356 CB AHIS B 36 35.400 19.543 20.407 0.66 17.64 C ANISOU 1356 CB AHIS B 36 988 2272 3442 -163 175 544 C ATOM 1357 CB BHIS B 36 35.417 19.550 20.378 0.34 17.48 C ANISOU 1357 CB BHIS B 36 904 2272 3467 193 167 137 C ATOM 1358 CG AHIS B 36 36.584 19.635 19.492 0.66 16.60 C ANISOU 1358 CG AHIS B 36 922 1868 3517 187 283 -167 C ATOM 1359 CG BHIS B 36 36.638 19.412 19.520 0.34 17.61 C ANISOU 1359 CG BHIS B 36 850 2172 3670 11 204 -232 C ATOM 1360 ND1AHIS B 36 37.857 19.513 19.997 0.66 20.52 N ANISOU 1360 ND1AHIS B 36 920 3248 3629 -448 66 -723 N ATOM 1361 ND1BHIS B 36 36.974 20.348 18.565 0.34 19.40 N ANISOU 1361 ND1BHIS B 36 1282 2250 3838 147 641 -193 N ATOM 1362 CD2AHIS B 36 36.707 19.818 18.155 0.66 14.60 C ANISOU 1362 CD2AHIS B 36 1093 1104 3351 -153 329 -788 C ATOM 1363 CD2BHIS B 36 37.613 18.473 19.459 0.34 16.19 C ANISOU 1363 CD2BHIS B 36 469 1770 3914 -384 -135 -671 C ATOM 1364 CE1AHIS B 36 38.733 19.628 19.002 0.66 20.83 C ANISOU 1364 CE1AHIS B 36 992 2917 4004 -200 321 -643 C ATOM 1365 CE1BHIS B 36 38.082 20.001 17.953 0.34 18.97 C ANISOU 1365 CE1BHIS B 36 1212 2359 3637 11 488 -538 C ATOM 1366 NE2AHIS B 36 38.040 19.820 17.883 0.66 19.79 N ANISOU 1366 NE2AHIS B 36 1173 2561 3784 -222 519 -400 N ATOM 1367 NE2BHIS B 36 38.497 18.856 18.477 0.34 19.63 N ANISOU 1367 NE2BHIS B 36 1497 2188 3774 194 536 -776 N ATOM 1368 N THR B 37 31.750 19.066 20.315 1.00 12.18 N ANISOU 1368 N THR B 37 799 1671 2158 408 108 182 N ATOM 1369 CA THR B 37 30.642 19.243 21.249 1.00 11.96 C ANISOU 1369 CA THR B 37 1035 1175 2336 447 303 259 C ATOM 1370 C THR B 37 30.188 17.953 21.916 1.00 12.81 C ANISOU 1370 C THR B 37 1392 1223 2250 200 305 66 C ATOM 1371 O THR B 37 29.848 17.008 21.229 1.00 15.16 O ANISOU 1371 O THR B 37 2097 1520 2143 -234 374 70 O ATOM 1372 CB THR B 37 29.403 19.787 20.472 1.00 13.67 C ANISOU 1372 CB THR B 37 880 1702 2613 394 162 276 C ATOM 1373 OG1 THR B 37 29.799 20.965 19.756 1.00 13.16 O ANISOU 1373 OG1 THR B 37 1496 1437 2066 545 -73 107 O ATOM 1374 CG2 THR B 37 28.261 20.158 21.408 1.00 15.23 C ANISOU 1374 CG2 THR B 37 1115 2580 2092 761 -30 197 C ATOM 1375 N LYS B 38 30.144 17.927 23.242 1.00 12.36 N ANISOU 1375 N LYS B 38 1324 1194 2177 319 376 94 N ATOM 1376 CA LYS B 38 29.586 16.808 23.993 1.00 12.35 C ANISOU 1376 CA LYS B 38 1504 1005 2185 182 176 -26 C ATOM 1377 C LYS B 38 28.123 17.069 24.368 1.00 9.79 C ANISOU 1377 C LYS B 38 1548 696 1477 129 212 -165 C ATOM 1378 O LYS B 38 27.783 18.215 24.682 1.00 11.10 O ANISOU 1378 O LYS B 38 1565 662 1989 132 29 -96 O ATOM 1379 CB LYS B 38 30.425 16.539 25.253 1.00 15.46 C ANISOU 1379 CB LYS B 38 1932 1674 2267 902 59 144 C ATOM 1380 CG LYS B 38 31.902 16.224 24.937 1.00 16.22 C ANISOU 1380 CG LYS B 38 1615 2423 2126 201 -47 126 C ATOM 1381 CD LYS B 38 32.724 16.204 26.208 1.00 23.57 C ANISOU 1381 CD LYS B 38 2643 3474 2838 870 -873 775 C ATOM 1382 CE LYS B 38 34.092 15.575 26.118 1.00 25.94 C ANISOU 1382 CE LYS B 38 2747 4008 3100 1057 -1038 -304 C ATOM 1383 NZ LYS B 38 34.496 15.202 24.745 1.00 38.80 N ANISOU 1383 NZ LYS B 38 4349 6282 4111 -689 1552 -455 N ATOM 1384 N PRO B 39 27.264 16.064 24.255 1.00 12.91 N ANISOU 1384 N PRO B 39 1409 529 2968 365 -19 -81 N ATOM 1385 CA PRO B 39 25.815 16.282 24.360 1.00 11.64 C ANISOU 1385 CA PRO B 39 1407 599 2415 321 20 -66 C ATOM 1386 C PRO B 39 25.491 16.894 25.721 1.00 10.07 C ANISOU 1386 C PRO B 39 1120 386 2319 68 -370 -138 C ATOM 1387 O PRO B 39 24.611 17.746 25.813 1.00 11.45 O ANISOU 1387 O PRO B 39 1202 944 2204 358 -204 -164 O ATOM 1388 CB PRO B 39 25.239 14.863 24.202 1.00 11.30 C ANISOU 1388 CB PRO B 39 1547 734 2013 209 -151 -233 C ATOM 1389 CG PRO B 39 26.382 13.917 24.460 1.00 13.91 C ANISOU 1389 CG PRO B 39 1652 499 3134 349 521 -173 C ATOM 1390 CD PRO B 39 27.600 14.639 23.971 1.00 14.06 C ANISOU 1390 CD PRO B 39 1571 279 3494 368 82 451 C ATOM 1391 N GLU B 40 26.164 16.490 26.809 1.00 12.36 N ANISOU 1391 N GLU B 40 1553 705 2439 -63 -344 423 N ATOM 1392 CA GLU B 40 25.880 17.088 28.120 1.00 15.24 C ANISOU 1392 CA GLU B 40 2746 929 2115 66 -380 675 C ATOM 1393 C GLU B 40 26.154 18.586 28.200 1.00 11.68 C ANISOU 1393 C GLU B 40 1481 909 2049 314 -107 395 C ATOM 1394 O GLU B 40 25.652 19.300 29.061 1.00 13.63 O ANISOU 1394 O GLU B 40 1902 1329 1946 282 102 318 O ATOM 1395 CB AGLU B 40 26.707 16.338 29.179 0.52 17.71 C ANISOU 1395 CB AGLU B 40 3015 1335 2377 785 -217 749 C ATOM 1396 CB BGLU B 40 26.694 16.345 29.198 0.48 17.98 C ANISOU 1396 CB BGLU B 40 3075 1374 2383 697 -214 861 C ATOM 1397 CG AGLU B 40 28.198 16.386 29.016 0.52 20.86 C ANISOU 1397 CG AGLU B 40 3003 2116 2807 1207 -92 712 C ATOM 1398 CG BGLU B 40 25.968 15.095 29.699 0.48 22.71 C ANISOU 1398 CG BGLU B 40 4662 1505 2463 312 -137 1129 C ATOM 1399 CD AGLU B 40 28.869 15.240 28.283 0.52 22.12 C ANISOU 1399 CD AGLU B 40 2712 1641 4052 1520 -1210 405 C ATOM 1400 CD BGLU B 40 26.759 14.389 30.778 0.48 23.57 C ANISOU 1400 CD BGLU B 40 4359 1857 2740 1243 457 1312 C ATOM 1401 OE1AGLU B 40 28.286 14.644 27.345 0.52 13.68 O ANISOU 1401 OE1AGLU B 40 1203 712 3282 601 -50 1173 O ATOM 1402 OE1BGLU B 40 26.282 14.314 31.929 0.48 32.20 O ANISOU 1402 OE1BGLU B 40 6369 3677 2187 1115 234 1158 O ATOM 1403 OE2AGLU B 40 30.044 14.964 28.667 0.52 24.79 O ANISOU 1403 OE2AGLU B 40 2592 2334 4492 1293 -1422 115 O ATOM 1404 OE2BGLU B 40 27.878 13.900 30.497 0.48 29.73 O ANISOU 1404 OE2BGLU B 40 3173 2527 5596 296 -13 269 O ATOM 1405 N ASP B 41 27.005 19.139 27.325 1.00 11.45 N ANISOU 1405 N ASP B 41 1413 1019 1918 32 -148 61 N ATOM 1406 CA ASP B 41 27.266 20.578 27.313 1.00 12.01 C ANISOU 1406 CA ASP B 41 1589 1088 1886 -111 -219 237 C ATOM 1407 C ASP B 41 26.298 21.298 26.376 1.00 11.25 C ANISOU 1407 C ASP B 41 1477 1022 1776 249 -54 -50 C ATOM 1408 O ASP B 41 26.429 22.508 26.207 1.00 12.21 O ANISOU 1408 O ASP B 41 1738 1002 1900 168 -21 35 O ATOM 1409 CB ASP B 41 28.698 20.862 26.846 1.00 13.71 C ANISOU 1409 CB ASP B 41 1470 1308 2429 -2 -287 616 C ATOM 1410 CG ASP B 41 29.692 20.269 27.826 1.00 14.75 C ANISOU 1410 CG ASP B 41 1625 1907 2072 455 125 909 C ATOM 1411 OD1 ASP B 41 29.361 20.256 29.036 1.00 21.62 O ANISOU 1411 OD1 ASP B 41 1954 4315 1945 -755 10 719 O ATOM 1412 OD2 ASP B 41 30.762 19.785 27.375 1.00 18.90 O ANISOU 1412 OD2 ASP B 41 1474 2633 3073 599 -447 -536 O ATOM 1413 N VAL B 42 25.329 20.652 25.745 1.00 9.69 N ANISOU 1413 N VAL B 42 1064 990 1629 406 211 -74 N ATOM 1414 CA VAL B 42 24.335 21.323 24.901 1.00 10.45 C ANISOU 1414 CA VAL B 42 1162 931 1877 562 34 -356 C ATOM 1415 C VAL B 42 23.167 21.806 25.757 1.00 9.25 C ANISOU 1415 C VAL B 42 1168 674 1671 444 124 -37 C ATOM 1416 O VAL B 42 22.486 20.978 26.395 1.00 14.20 O ANISOU 1416 O VAL B 42 1936 1125 2334 443 534 488 O ATOM 1417 CB VAL B 42 23.835 20.393 23.777 1.00 11.39 C ANISOU 1417 CB VAL B 42 1240 987 2102 532 -93 -509 C ATOM 1418 CG1 VAL B 42 22.763 21.113 22.956 1.00 10.75 C ANISOU 1418 CG1 VAL B 42 1341 962 1783 181 -8 -84 C ATOM 1419 CG2 VAL B 42 25.035 19.898 22.967 1.00 11.41 C ANISOU 1419 CG2 VAL B 42 1359 1059 1918 194 129 -487 C ATOM 1420 N VAL B 43 22.959 23.092 25.825 1.00 7.97 N ANISOU 1420 N VAL B 43 1549 804 675 720 -240 -137 N ATOM 1421 CA VAL B 43 21.856 23.755 26.533 1.00 8.30 C ANISOU 1421 CA VAL B 43 1499 678 977 158 -168 -889 C ATOM 1422 C VAL B 43 20.543 23.277 25.921 1.00 7.72 C ANISOU 1422 C VAL B 43 1468 422 1042 129 -319 30 C ATOM 1423 O VAL B 43 19.658 22.792 26.637 1.00 10.74 O ANISOU 1423 O VAL B 43 1579 734 1768 147 -26 384 O ATOM 1424 CB VAL B 43 21.983 25.278 26.411 1.00 9.67 C ANISOU 1424 CB VAL B 43 1329 641 1704 257 -447 -614 C ATOM 1425 CG1 VAL B 43 20.781 25.951 26.998 1.00 8.95 C ANISOU 1425 CG1 VAL B 43 1325 753 1321 402 -393 -259 C ATOM 1426 CG2 VAL B 43 23.284 25.775 27.068 1.00 10.11 C ANISOU 1426 CG2 VAL B 43 1261 679 1901 99 -348 -515 C ATOM 1427 N GLN B 44 20.465 23.377 24.569 1.00 9.48 N ANISOU 1427 N GLN B 44 1555 1085 964 504 -430 -359 N ATOM 1428 CA GLN B 44 19.210 23.092 23.870 1.00 8.18 C ANISOU 1428 CA GLN B 44 1209 1153 745 414 -7 -231 C ATOM 1429 C GLN B 44 19.503 23.211 22.380 1.00 7.10 C ANISOU 1429 C GLN B 44 887 1089 719 193 50 -347 C ATOM 1430 O GLN B 44 20.579 23.768 22.031 1.00 8.24 O ANISOU 1430 O GLN B 44 939 1023 1169 149 -68 93 O ATOM 1431 CB GLN B 44 18.067 24.051 24.208 1.00 6.38 C ANISOU 1431 CB GLN B 44 972 540 911 -134 324 -346 C ATOM 1432 CG GLN B 44 18.307 25.469 23.733 1.00 7.34 C ANISOU 1432 CG GLN B 44 1389 625 774 -158 86 -246 C ATOM 1433 CD GLN B 44 17.313 26.521 24.207 1.00 7.85 C ANISOU 1433 CD GLN B 44 1251 573 1158 -41 -236 -125 C ATOM 1434 OE1 GLN B 44 16.818 27.382 23.439 1.00 16.52 O ANISOU 1434 OE1 GLN B 44 3267 1140 1869 669 -307 429 O ATOM 1435 NE2 GLN B 44 17.045 26.378 25.503 1.00 8.79 N ANISOU 1435 NE2 GLN B 44 1597 773 968 704 -244 -449 N ATOM 1436 N MET B 45 18.566 22.769 21.570 1.00 7.60 N ANISOU 1436 N MET B 45 1287 901 697 -70 -104 -34 N ATOM 1437 CA MET B 45 18.710 22.893 20.127 1.00 7.17 C ANISOU 1437 CA MET B 45 1052 1000 672 113 -13 -75 C ATOM 1438 C MET B 45 17.382 23.220 19.485 1.00 6.43 C ANISOU 1438 C MET B 45 950 956 536 -177 38 -13 C ATOM 1439 O MET B 45 16.370 22.676 19.913 1.00 8.75 O ANISOU 1439 O MET B 45 1177 1316 833 -503 -73 246 O ATOM 1440 CB AMET B 45 19.305 21.583 19.585 0.68 9.23 C ANISOU 1440 CB AMET B 45 1753 898 856 236 327 144 C ATOM 1441 CB BMET B 45 19.216 21.580 19.513 0.32 8.89 C ANISOU 1441 CB BMET B 45 1328 970 1079 26 245 -155 C ATOM 1442 CG AMET B 45 19.567 21.583 18.088 0.68 7.82 C ANISOU 1442 CG AMET B 45 1127 902 942 -303 669 58 C ATOM 1443 CG BMET B 45 20.671 21.283 19.788 0.32 11.63 C ANISOU 1443 CG BMET B 45 1703 1327 1392 690 -41 371 C ATOM 1444 SD AMET B 45 20.206 19.969 17.588 0.68 14.32 S ANISOU 1444 SD AMET B 45 2702 1302 1436 256 410 -388 S ATOM 1445 SD BMET B 45 21.239 19.760 19.021 0.32 19.68 S ANISOU 1445 SD BMET B 45 2800 1478 3201 1068 825 277 S ATOM 1446 CE AMET B 45 20.881 19.326 19.097 0.68 17.70 C ANISOU 1446 CE AMET B 45 2612 542 3573 -1004 -1769 246 C ATOM 1447 CE BMET B 45 20.523 19.825 17.386 0.32 21.47 C ANISOU 1447 CE BMET B 45 3956 0 4202 573 -676 -1395 C ATOM 1448 N LEU B 46 17.431 23.979 18.419 1.00 8.27 N ANISOU 1448 N LEU B 46 1211 1264 669 -23 89 260 N ATOM 1449 CA LEU B 46 16.278 24.227 17.589 1.00 6.95 C ANISOU 1449 CA LEU B 46 1302 706 632 299 82 -57 C ATOM 1450 C LEU B 46 16.576 23.825 16.163 1.00 6.83 C ANISOU 1450 C LEU B 46 1309 709 577 -91 166 13 C ATOM 1451 O LEU B 46 17.696 24.009 15.661 1.00 9.69 O ANISOU 1451 O LEU B 46 1243 1573 865 67 225 16 O ATOM 1452 CB LEU B 46 15.917 25.726 17.525 1.00 8.41 C ANISOU 1452 CB LEU B 46 1409 541 1245 -43 153 -103 C ATOM 1453 CG LEU B 46 15.630 26.358 18.876 1.00 9.89 C ANISOU 1453 CG LEU B 46 1524 487 1746 -58 522 -412 C ATOM 1454 CD1 LEU B 46 15.471 27.877 18.758 1.00 12.93 C ANISOU 1454 CD1 LEU B 46 2439 433 2041 -135 379 -232 C ATOM 1455 CD2 LEU B 46 14.371 25.724 19.480 1.00 11.04 C ANISOU 1455 CD2 LEU B 46 1673 927 1594 -53 464 174 C ATOM 1456 N LEU B 47 15.599 23.207 15.498 1.00 8.06 N ANISOU 1456 N LEU B 47 1531 600 931 123 -235 -113 N ATOM 1457 CA LEU B 47 15.792 22.892 14.082 1.00 8.36 C ANISOU 1457 CA LEU B 47 1663 779 734 -127 -282 80 C ATOM 1458 C LEU B 47 14.646 23.517 13.310 1.00 8.01 C ANISOU 1458 C LEU B 47 1455 833 756 -103 -54 91 C ATOM 1459 O LEU B 47 13.498 23.346 13.739 1.00 11.24 O ANISOU 1459 O LEU B 47 1569 1404 1298 133 240 451 O ATOM 1460 CB LEU B 47 15.795 21.396 13.877 1.00 10.47 C ANISOU 1460 CB LEU B 47 1666 811 1500 283 26 -351 C ATOM 1461 CG LEU B 47 16.853 20.425 14.358 1.00 15.97 C ANISOU 1461 CG LEU B 47 1749 1741 2577 987 -319 -643 C ATOM 1462 CD1 LEU B 47 17.851 20.225 13.215 1.00 30.77 C ANISOU 1462 CD1 LEU B 47 2772 6501 2420 2997 -93 -100 C ATOM 1463 CD2 LEU B 47 17.482 20.710 15.688 1.00 32.76 C ANISOU 1463 CD2 LEU B 47 5432 4644 2370 3296 -1502 -974 C ATOM 1464 N SER B 48 14.962 24.202 12.211 1.00 8.44 N ANISOU 1464 N SER B 48 1759 939 508 186 30 50 N ATOM 1465 CA SER B 48 13.834 24.688 11.400 1.00 9.95 C ANISOU 1465 CA SER B 48 2076 925 778 188 -383 -139 C ATOM 1466 C SER B 48 13.807 23.977 10.063 1.00 9.02 C ANISOU 1466 C SER B 48 1435 1283 711 -253 -71 -98 C ATOM 1467 O SER B 48 14.817 23.451 9.582 1.00 10.45 O ANISOU 1467 O SER B 48 1559 1478 935 -225 97 -160 O ATOM 1468 CB SER B 48 13.934 26.205 11.183 1.00 11.33 C ANISOU 1468 CB SER B 48 2431 918 954 403 295 165 C ATOM 1469 OG SER B 48 14.957 26.459 10.222 1.00 9.84 O ANISOU 1469 OG SER B 48 1745 1247 748 237 -107 -187 O ATOM 1470 N ALA B 49 12.600 23.940 9.476 1.00 9.96 N ANISOU 1470 N ALA B 49 1718 1267 799 -169 -505 228 N ATOM 1471 CA ALA B 49 12.452 23.418 8.118 1.00 9.25 C ANISOU 1471 CA ALA B 49 1790 930 797 -146 -403 254 C ATOM 1472 C ALA B 49 11.659 24.408 7.283 1.00 7.68 C ANISOU 1472 C ALA B 49 1707 726 486 50 -255 -65 C ATOM 1473 O ALA B 49 10.687 25.083 7.709 1.00 12.71 O ANISOU 1473 O ALA B 49 1723 1394 1713 327 -277 -423 O ATOM 1474 CB ALA B 49 11.711 22.087 8.150 1.00 11.77 C ANISOU 1474 CB ALA B 49 2831 549 1091 -98 415 -81 C ATOM 1475 N THR B 50 11.986 24.469 5.996 1.00 11.46 N ANISOU 1475 N THR B 50 2621 1384 349 -222 -403 1 N ATOM 1476 CA THR B 50 11.191 25.264 5.038 1.00 12.93 C ANISOU 1476 CA THR B 50 2477 1951 487 -1 -306 159 C ATOM 1477 C THR B 50 9.833 24.601 4.897 1.00 14.28 C ANISOU 1477 C THR B 50 2325 1951 1152 62 -226 -39 C ATOM 1478 O THR B 50 9.683 23.413 5.173 1.00 14.04 O ANISOU 1478 O THR B 50 2595 2034 705 -29 -483 37 O ATOM 1479 CB THR B 50 11.964 25.380 3.720 1.00 11.89 C ANISOU 1479 CB THR B 50 2571 1539 407 -101 -374 68 C ATOM 1480 OG1 THR B 50 12.495 24.088 3.363 1.00 14.17 O ANISOU 1480 OG1 THR B 50 2595 1770 1018 3 -226 -183 O ATOM 1481 CG2 THR B 50 13.096 26.418 3.879 1.00 11.97 C ANISOU 1481 CG2 THR B 50 2273 1695 580 0 -473 120 C ATOM 1482 N PRO B 51 8.797 25.343 4.529 1.00 16.48 N ANISOU 1482 N PRO B 51 2641 1724 1897 35 -831 -464 N ATOM 1483 CA PRO B 51 7.426 24.823 4.446 1.00 15.44 C ANISOU 1483 CA PRO B 51 2496 1785 1585 201 -784 -326 C ATOM 1484 C PRO B 51 7.170 23.835 3.306 1.00 15.00 C ANISOU 1484 C PRO B 51 2384 2355 959 -294 -671 -108 C ATOM 1485 O PRO B 51 6.023 23.397 3.118 1.00 17.35 O ANISOU 1485 O PRO B 51 2505 2399 1688 -481 -684 -107 O ATOM 1486 CB PRO B 51 6.584 26.095 4.270 1.00 21.64 C ANISOU 1486 CB PRO B 51 2916 1727 3580 171 -1147 204 C ATOM 1487 CG PRO B 51 7.512 27.155 3.798 1.00 22.16 C ANISOU 1487 CG PRO B 51 2901 1869 3647 -41 -1278 68 C ATOM 1488 CD PRO B 51 8.898 26.791 4.258 1.00 19.65 C ANISOU 1488 CD PRO B 51 3095 1926 2447 -158 -1497 134 C ATOM 1489 N ASP B 52 8.198 23.424 2.566 1.00 14.91 N ANISOU 1489 N ASP B 52 2589 2096 982 -170 -599 -82 N ATOM 1490 CA ASP B 52 8.076 22.346 1.592 1.00 15.72 C ANISOU 1490 CA ASP B 52 2812 2132 1028 -657 -255 -54 C ATOM 1491 C ASP B 52 8.493 20.983 2.157 1.00 16.72 C ANISOU 1491 C ASP B 52 3091 1898 1365 -986 -347 -24 C ATOM 1492 O ASP B 52 8.579 20.020 1.384 1.00 18.29 O ANISOU 1492 O ASP B 52 3217 2296 1435 -287 -798 -267 O ATOM 1493 CB ASP B 52 8.942 22.590 0.354 1.00 15.21 C ANISOU 1493 CB ASP B 52 2661 1886 1232 -534 -100 -101 C ATOM 1494 CG ASP B 52 10.343 23.043 0.716 1.00 16.14 C ANISOU 1494 CG ASP B 52 2938 2069 1126 -868 -105 -449 C ATOM 1495 OD1 ASP B 52 10.772 22.897 1.873 1.00 17.36 O ANISOU 1495 OD1 ASP B 52 2762 2744 1091 -676 -66 -622 O ATOM 1496 OD2 ASP B 52 11.042 23.549 -0.214 1.00 16.65 O ANISOU 1496 OD2 ASP B 52 2667 2096 1562 -619 -139 -8 O ATOM 1497 N LEU B 53 8.751 20.935 3.457 1.00 14.63 N ANISOU 1497 N LEU B 53 2150 2009 1400 -334 -532 -198 N ATOM 1498 CA LEU B 53 9.178 19.649 4.044 1.00 15.69 C ANISOU 1498 CA LEU B 53 2185 1987 1789 -577 -379 55 C ATOM 1499 C LEU B 53 8.172 19.179 5.083 1.00 15.22 C ANISOU 1499 C LEU B 53 2320 1772 1689 -690 -152 -464 C ATOM 1500 O LEU B 53 7.887 19.907 6.048 1.00 17.28 O ANISOU 1500 O LEU B 53 2651 2050 1862 -713 -337 -785 O ATOM 1501 CB LEU B 53 10.536 19.822 4.707 1.00 13.14 C ANISOU 1501 CB LEU B 53 1878 1785 1330 92 -84 -566 C ATOM 1502 CG LEU B 53 11.726 20.061 3.759 1.00 15.89 C ANISOU 1502 CG LEU B 53 2245 1960 1831 -344 315 -1025 C ATOM 1503 CD1 LEU B 53 12.996 20.257 4.559 1.00 19.63 C ANISOU 1503 CD1 LEU B 53 2055 2729 2673 -423 251 -1368 C ATOM 1504 CD2 LEU B 53 11.814 18.862 2.812 1.00 17.88 C ANISOU 1504 CD2 LEU B 53 3047 2009 1737 -661 672 -1035 C ATOM 1505 N HIS B 54 7.607 17.987 4.990 1.00 14.02 N ANISOU 1505 N HIS B 54 2537 1358 1434 -294 -25 -171 N ATOM 1506 CA HIS B 54 6.542 17.528 5.865 1.00 13.23 C ANISOU 1506 CA HIS B 54 2136 1539 1351 -228 -339 99 C ATOM 1507 C HIS B 54 6.703 16.086 6.319 1.00 12.32 C ANISOU 1507 C HIS B 54 2256 1487 936 -202 -245 -97 C ATOM 1508 O HIS B 54 5.853 15.607 7.088 1.00 15.02 O ANISOU 1508 O HIS B 54 2760 1793 1154 -174 95 125 O ATOM 1509 CB HIS B 54 5.179 17.620 5.146 1.00 16.22 C ANISOU 1509 CB HIS B 54 2366 2669 1128 -53 -456 415 C ATOM 1510 CG HIS B 54 4.921 18.969 4.531 1.00 15.90 C ANISOU 1510 CG HIS B 54 2604 2144 1295 -484 -1365 -117 C ATOM 1511 ND1 HIS B 54 4.611 20.079 5.270 1.00 21.06 N ANISOU 1511 ND1 HIS B 54 3133 2858 2010 247 -704 -439 N ATOM 1512 CD2 HIS B 54 4.943 19.356 3.226 1.00 14.25 C ANISOU 1512 CD2 HIS B 54 1838 1991 1586 115 -810 308 C ATOM 1513 CE1 HIS B 54 4.448 21.113 4.466 1.00 23.48 C ANISOU 1513 CE1 HIS B 54 3514 2720 2689 986 -1334 -514 C ATOM 1514 NE2 HIS B 54 4.637 20.715 3.215 1.00 21.36 N ANISOU 1514 NE2 HIS B 54 3569 2104 2443 499 -742 182 N ATOM 1515 N ALA B 55 7.736 15.350 5.882 1.00 13.59 N ANISOU 1515 N ALA B 55 2567 1360 1238 -236 -84 -517 N ATOM 1516 CA ALA B 55 7.735 13.911 6.155 1.00 12.17 C ANISOU 1516 CA ALA B 55 1816 1372 1435 -622 -145 -537 C ATOM 1517 C ALA B 55 8.003 13.539 7.624 1.00 13.66 C ANISOU 1517 C ALA B 55 1883 1527 1778 -443 -574 -194 C ATOM 1518 O ALA B 55 7.511 12.508 8.085 1.00 14.95 O ANISOU 1518 O ALA B 55 1971 1740 1969 -535 -396 -15 O ATOM 1519 CB ALA B 55 8.790 13.205 5.319 1.00 17.86 C ANISOU 1519 CB ALA B 55 2458 2166 2164 258 -518 -1386 C ATOM 1520 N VAL B 56 8.774 14.347 8.340 1.00 14.49 N ANISOU 1520 N VAL B 56 1915 1982 1606 -538 -519 -430 N ATOM 1521 CA VAL B 56 9.217 13.951 9.685 1.00 10.68 C ANISOU 1521 CA VAL B 56 1656 1204 1197 -219 136 -742 C ATOM 1522 C VAL B 56 9.714 15.204 10.366 1.00 9.90 C ANISOU 1522 C VAL B 56 1467 1153 1143 -322 275 -660 C ATOM 1523 O VAL B 56 10.135 16.145 9.667 1.00 12.73 O ANISOU 1523 O VAL B 56 1760 1387 1688 -399 -95 -136 O ATOM 1524 CB VAL B 56 10.274 12.839 9.548 1.00 11.78 C ANISOU 1524 CB VAL B 56 1762 1165 1550 -226 180 -726 C ATOM 1525 CG1 VAL B 56 11.555 13.426 8.963 1.00 12.62 C ANISOU 1525 CG1 VAL B 56 1552 1977 1265 -153 94 -622 C ATOM 1526 CG2 VAL B 56 10.547 12.115 10.878 1.00 14.09 C ANISOU 1526 CG2 VAL B 56 2076 1350 1927 -108 195 -323 C ATOM 1527 N PHE B 57 9.704 15.221 11.704 1.00 10.66 N ANISOU 1527 N PHE B 57 1698 1148 1203 -184 65 -752 N ATOM 1528 CA PHE B 57 10.405 16.270 12.461 1.00 9.30 C ANISOU 1528 CA PHE B 57 1618 863 1054 -142 29 -502 C ATOM 1529 C PHE B 57 11.901 16.009 12.420 1.00 9.76 C ANISOU 1529 C PHE B 57 1619 652 1437 -171 194 -598 C ATOM 1530 O PHE B 57 12.328 14.887 12.812 1.00 11.79 O ANISOU 1530 O PHE B 57 1612 916 1951 -93 383 -120 O ATOM 1531 CB PHE B 57 9.968 16.269 13.934 1.00 9.52 C ANISOU 1531 CB PHE B 57 1810 771 1034 -56 151 -513 C ATOM 1532 CG PHE B 57 8.522 16.758 14.046 1.00 9.86 C ANISOU 1532 CG PHE B 57 1860 1338 550 110 -121 -662 C ATOM 1533 CD1 PHE B 57 8.234 18.133 13.995 1.00 11.89 C ANISOU 1533 CD1 PHE B 57 1815 1463 1241 318 268 -245 C ATOM 1534 CD2 PHE B 57 7.486 15.854 14.185 1.00 12.11 C ANISOU 1534 CD2 PHE B 57 1580 1382 1641 306 -119 -594 C ATOM 1535 CE1 PHE B 57 6.909 18.548 14.114 1.00 14.40 C ANISOU 1535 CE1 PHE B 57 1771 1925 1776 347 107 -317 C ATOM 1536 CE2 PHE B 57 6.165 16.259 14.313 1.00 12.58 C ANISOU 1536 CE2 PHE B 57 1820 1721 1239 670 438 -274 C ATOM 1537 CZ PHE B 57 5.895 17.619 14.249 1.00 11.89 C ANISOU 1537 CZ PHE B 57 1657 1667 1194 509 -6 -424 C ATOM 1538 N PRO B 58 12.725 16.931 11.904 1.00 9.71 N ANISOU 1538 N PRO B 58 1500 586 1604 -139 -126 -449 N ATOM 1539 CA PRO B 58 14.173 16.649 11.837 1.00 9.58 C ANISOU 1539 CA PRO B 58 1496 971 1173 -138 -56 -222 C ATOM 1540 C PRO B 58 14.774 16.356 13.220 1.00 9.85 C ANISOU 1540 C PRO B 58 994 1707 1043 -302 281 -40 C ATOM 1541 O PRO B 58 15.792 15.656 13.315 1.00 10.13 O ANISOU 1541 O PRO B 58 1229 1856 763 -32 84 -392 O ATOM 1542 CB PRO B 58 14.766 17.934 11.242 1.00 11.57 C ANISOU 1542 CB PRO B 58 1740 1118 1539 -69 279 38 C ATOM 1543 CG PRO B 58 13.624 18.670 10.602 1.00 16.10 C ANISOU 1543 CG PRO B 58 1934 1727 2457 398 586 725 C ATOM 1544 CD PRO B 58 12.345 18.207 11.279 1.00 11.00 C ANISOU 1544 CD PRO B 58 1812 1172 1194 192 240 -11 C ATOM 1545 N ALA B 59 14.165 16.820 14.289 1.00 9.50 N ANISOU 1545 N ALA B 59 1326 1216 1068 -26 383 186 N ATOM 1546 CA ALA B 59 14.614 16.552 15.663 1.00 8.98 C ANISOU 1546 CA ALA B 59 1833 500 1079 9 -32 -435 C ATOM 1547 C ALA B 59 14.685 15.042 15.938 1.00 9.85 C ANISOU 1547 C ALA B 59 1939 606 1198 -167 -25 -173 C ATOM 1548 O ALA B 59 15.422 14.582 16.802 1.00 11.39 O ANISOU 1548 O ALA B 59 1901 799 1627 -11 -115 32 O ATOM 1549 CB ALA B 59 13.664 17.255 16.648 1.00 11.25 C ANISOU 1549 CB ALA B 59 1665 1351 1257 128 -109 -823 C ATOM 1550 N LYS B 60 13.953 14.215 15.195 1.00 10.31 N ANISOU 1550 N LYS B 60 1392 586 1939 -339 267 -494 N ATOM 1551 CA LYS B 60 14.039 12.754 15.368 1.00 9.75 C ANISOU 1551 CA LYS B 60 1785 646 1273 -40 382 -626 C ATOM 1552 C LYS B 60 15.458 12.243 15.251 1.00 12.93 C ANISOU 1552 C LYS B 60 2126 1409 1376 503 556 -247 C ATOM 1553 O LYS B 60 15.913 11.361 15.951 1.00 13.06 O ANISOU 1553 O LYS B 60 1577 1280 2104 -188 106 40 O ATOM 1554 CB LYS B 60 13.126 12.039 14.365 1.00 12.03 C ANISOU 1554 CB LYS B 60 2567 630 1376 -121 183 -853 C ATOM 1555 CG LYS B 60 13.219 10.531 14.403 1.00 11.76 C ANISOU 1555 CG LYS B 60 2795 614 1058 -361 -270 -352 C ATOM 1556 CD LYS B 60 12.069 9.884 13.636 1.00 15.41 C ANISOU 1556 CD LYS B 60 3514 1017 1325 -559 -714 -514 C ATOM 1557 CE LYS B 60 12.321 8.357 13.582 1.00 14.97 C ANISOU 1557 CE LYS B 60 2560 1059 2069 -779 71 -995 C ATOM 1558 NZ LYS B 60 11.198 7.646 12.939 1.00 16.39 N ANISOU 1558 NZ LYS B 60 1723 1274 3232 -373 15 -1188 N ATOM 1559 N ALA B 61 16.202 12.849 14.300 1.00 10.61 N ANISOU 1559 N ALA B 61 1441 1416 1174 185 79 -339 N ATOM 1560 CA ALA B 61 17.568 12.360 14.135 1.00 11.30 C ANISOU 1560 CA ALA B 61 1720 1733 840 614 51 -388 C ATOM 1561 C ALA B 61 18.466 12.679 15.324 1.00 10.33 C ANISOU 1561 C ALA B 61 1519 1039 1368 310 -53 -315 C ATOM 1562 O ALA B 61 19.370 11.939 15.646 1.00 13.51 O ANISOU 1562 O ALA B 61 1674 1380 2081 455 -460 -216 O ATOM 1563 CB ALA B 61 18.126 12.968 12.831 1.00 13.05 C ANISOU 1563 CB ALA B 61 1925 1791 1241 401 417 -292 C ATOM 1564 N VAL B 62 18.214 13.833 15.951 1.00 11.51 N ANISOU 1564 N VAL B 62 1713 793 1867 -202 88 -434 N ATOM 1565 CA VAL B 62 18.944 14.235 17.163 1.00 10.71 C ANISOU 1565 CA VAL B 62 1699 681 1690 -115 206 -359 C ATOM 1566 C VAL B 62 18.597 13.266 18.280 1.00 10.41 C ANISOU 1566 C VAL B 62 1193 687 2074 32 218 -55 C ATOM 1567 O VAL B 62 19.463 12.751 18.985 1.00 12.95 O ANISOU 1567 O VAL B 62 1503 1310 2108 3 -176 -62 O ATOM 1568 CB VAL B 62 18.657 15.680 17.618 1.00 11.17 C ANISOU 1568 CB VAL B 62 2541 667 1035 251 67 -141 C ATOM 1569 CG1 VAL B 62 19.517 16.012 18.811 1.00 13.31 C ANISOU 1569 CG1 VAL B 62 2979 943 1137 158 -124 -259 C ATOM 1570 CG2 VAL B 62 18.954 16.609 16.463 1.00 12.73 C ANISOU 1570 CG2 VAL B 62 2404 1101 1333 364 38 244 C ATOM 1571 N ARG B 63 17.284 12.995 18.407 1.00 11.25 N ANISOU 1571 N ARG B 63 1226 1096 1952 99 249 -152 N ATOM 1572 CA ARG B 63 16.830 12.154 19.508 1.00 12.94 C ANISOU 1572 CA ARG B 63 1291 1124 2503 186 571 153 C ATOM 1573 C ARG B 63 17.342 10.727 19.410 1.00 13.43 C ANISOU 1573 C ARG B 63 1447 1355 2303 507 490 219 C ATOM 1574 O ARG B 63 17.504 10.087 20.455 1.00 15.91 O ANISOU 1574 O ARG B 63 2861 1026 2158 119 52 5 O ATOM 1575 CB ARG B 63 15.286 12.177 19.559 1.00 15.03 C ANISOU 1575 CB ARG B 63 1272 833 3606 272 581 411 C ATOM 1576 CG ARG B 63 14.813 13.583 19.986 1.00 12.40 C ANISOU 1576 CG ARG B 63 1335 1090 2285 251 -22 19 C ATOM 1577 CD ARG B 63 13.273 13.604 20.115 1.00 13.08 C ANISOU 1577 CD ARG B 63 1372 1033 2564 474 -6 -342 C ATOM 1578 NE ARG B 63 12.903 14.992 20.345 1.00 10.42 N ANISOU 1578 NE ARG B 63 1484 652 1825 81 82 144 N ATOM 1579 CZ ARG B 63 12.130 15.742 19.599 1.00 9.79 C ANISOU 1579 CZ ARG B 63 1409 434 1877 -196 -184 -49 C ATOM 1580 NH1 ARG B 63 11.534 15.282 18.500 1.00 10.68 N ANISOU 1580 NH1 ARG B 63 1386 1103 1568 -197 126 -300 N ATOM 1581 NH2 ARG B 63 11.913 17.006 19.921 1.00 11.01 N ANISOU 1581 NH2 ARG B 63 1404 609 2170 180 104 -345 N ATOM 1582 N GLU B 64 17.651 10.258 18.192 1.00 12.14 N ANISOU 1582 N GLU B 64 1544 929 2137 139 -214 -106 N ATOM 1583 CA GLU B 64 18.169 8.912 17.983 1.00 12.97 C ANISOU 1583 CA GLU B 64 1306 981 2641 116 -163 -121 C ATOM 1584 C GLU B 64 19.684 8.835 18.086 1.00 13.72 C ANISOU 1584 C GLU B 64 1377 760 3076 46 109 338 C ATOM 1585 O GLU B 64 20.226 7.717 18.185 1.00 17.15 O ANISOU 1585 O GLU B 64 1624 845 4047 286 -175 169 O ATOM 1586 CB GLU B 64 17.659 8.437 16.603 1.00 14.34 C ANISOU 1586 CB GLU B 64 1906 867 2674 -87 78 -344 C ATOM 1587 CG GLU B 64 16.155 8.219 16.650 1.00 20.08 C ANISOU 1587 CG GLU B 64 2009 1822 3798 -664 -848 16 C ATOM 1588 CD GLU B 64 15.458 7.522 15.521 1.00 23.67 C ANISOU 1588 CD GLU B 64 2726 2352 3915 -400 -1026 -399 C ATOM 1589 OE1 GLU B 64 15.981 7.423 14.402 1.00 30.99 O ANISOU 1589 OE1 GLU B 64 4462 3228 4084 1383 -671 -916 O ATOM 1590 OE2 GLU B 64 14.316 7.038 15.720 1.00 32.91 O ANISOU 1590 OE2 GLU B 64 3976 2596 5932 -2202 -1392 -627 O ATOM 1591 N LEU B 65 20.397 9.973 18.053 1.00 11.48 N ANISOU 1591 N LEU B 65 1346 865 2152 -80 7 202 N ATOM 1592 CA LEU B 65 21.865 9.892 18.048 1.00 10.60 C ANISOU 1592 CA LEU B 65 1359 561 2107 172 152 184 C ATOM 1593 C LEU B 65 22.359 9.388 19.386 1.00 10.18 C ANISOU 1593 C LEU B 65 1196 676 1997 224 145 -116 C ATOM 1594 O LEU B 65 22.006 9.974 20.410 1.00 12.87 O ANISOU 1594 O LEU B 65 1722 1065 2102 468 273 -127 O ATOM 1595 CB LEU B 65 22.501 11.254 17.737 1.00 11.77 C ANISOU 1595 CB LEU B 65 1454 805 2214 -222 89 -32 C ATOM 1596 CG LEU B 65 24.023 11.285 17.530 1.00 13.09 C ANISOU 1596 CG LEU B 65 1459 750 2763 73 225 350 C ATOM 1597 CD1 LEU B 65 24.499 10.492 16.313 1.00 19.19 C ANISOU 1597 CD1 LEU B 65 2247 1420 3625 349 828 -183 C ATOM 1598 CD2 LEU B 65 24.528 12.720 17.367 1.00 15.28 C ANISOU 1598 CD2 LEU B 65 1796 1187 2821 -648 -298 271 C ATOM 1599 N SER B 66 23.211 8.360 19.382 1.00 9.63 N ANISOU 1599 N SER B 66 1336 650 1672 228 190 68 N ATOM 1600 CA SER B 66 23.632 7.818 20.678 1.00 12.04 C ANISOU 1600 CA SER B 66 1917 930 1728 397 10 -47 C ATOM 1601 C SER B 66 24.290 8.848 21.579 1.00 11.93 C ANISOU 1601 C SER B 66 1911 897 1724 324 -39 -2 C ATOM 1602 O SER B 66 25.249 9.522 21.219 1.00 12.23 O ANISOU 1602 O SER B 66 1631 1073 1942 444 140 -229 O ATOM 1603 CB SER B 66 24.564 6.618 20.434 1.00 11.96 C ANISOU 1603 CB SER B 66 1923 1203 1420 677 -370 -162 C ATOM 1604 OG SER B 66 24.726 5.908 21.671 1.00 11.31 O ANISOU 1604 OG SER B 66 1602 1033 1664 153 51 124 O ATOM 1605 N GLY B 67 23.778 8.916 22.823 1.00 12.12 N ANISOU 1605 N GLY B 67 1861 844 1901 67 55 -111 N ATOM 1606 CA GLY B 67 24.290 9.843 23.817 1.00 11.49 C ANISOU 1606 CA GLY B 67 1250 1392 1723 456 -233 -187 C ATOM 1607 C GLY B 67 23.503 11.138 23.858 1.00 11.71 C ANISOU 1607 C GLY B 67 1539 1363 1548 519 -88 -386 C ATOM 1608 O GLY B 67 23.729 11.885 24.804 1.00 12.51 O ANISOU 1608 O GLY B 67 2241 1017 1494 -66 -52 -37 O ATOM 1609 N TRP B 68 22.639 11.405 22.887 1.00 11.73 N ANISOU 1609 N TRP B 68 1493 993 1972 178 -280 117 N ATOM 1610 CA TRP B 68 21.916 12.668 22.778 1.00 12.12 C ANISOU 1610 CA TRP B 68 1519 1152 1933 353 161 69 C ATOM 1611 C TRP B 68 20.486 12.549 23.285 1.00 16.36 C ANISOU 1611 C TRP B 68 1760 1609 2847 296 698 157 C ATOM 1612 O TRP B 68 19.720 13.508 23.069 1.00 14.83 O ANISOU 1612 O TRP B 68 1464 1348 2824 65 270 -143 O ATOM 1613 CB TRP B 68 21.970 13.102 21.289 1.00 10.98 C ANISOU 1613 CB TRP B 68 1675 621 1876 183 -13 9 C ATOM 1614 CG TRP B 68 23.366 13.672 21.072 1.00 10.79 C ANISOU 1614 CG TRP B 68 1709 866 1525 103 -4 -266 C ATOM 1615 CD1 TRP B 68 24.523 12.928 21.090 1.00 12.24 C ANISOU 1615 CD1 TRP B 68 1680 928 2041 139 364 -324 C ATOM 1616 CD2 TRP B 68 23.758 15.022 20.822 1.00 14.04 C ANISOU 1616 CD2 TRP B 68 1684 785 2865 -57 -223 -330 C ATOM 1617 NE1 TRP B 68 25.591 13.737 20.870 1.00 11.32 N ANISOU 1617 NE1 TRP B 68 1722 871 1708 15 98 -382 N ATOM 1618 CE2 TRP B 68 25.164 15.042 20.699 1.00 13.74 C ANISOU 1618 CE2 TRP B 68 1754 1019 2446 80 225 11 C ATOM 1619 CE3 TRP B 68 23.070 16.234 20.685 1.00 13.39 C ANISOU 1619 CE3 TRP B 68 1909 872 2307 123 -260 -420 C ATOM 1620 CZ2 TRP B 68 25.885 16.209 20.454 1.00 11.56 C ANISOU 1620 CZ2 TRP B 68 1783 724 1885 25 376 -826 C ATOM 1621 CZ3 TRP B 68 23.775 17.416 20.440 1.00 10.38 C ANISOU 1621 CZ3 TRP B 68 2037 880 1027 274 102 -116 C ATOM 1622 CH2 TRP B 68 25.173 17.383 20.328 1.00 11.93 C ANISOU 1622 CH2 TRP B 68 2178 938 1415 292 960 -462 C ATOM 1623 N GLN B 69 20.103 11.443 23.947 1.00 14.48 N ANISOU 1623 N GLN B 69 1873 1020 2610 43 593 -473 N ATOM 1624 CA GLN B 69 18.709 11.251 24.334 1.00 15.26 C ANISOU 1624 CA GLN B 69 1892 796 3112 36 774 -547 C ATOM 1625 C GLN B 69 18.166 12.262 25.333 1.00 14.43 C ANISOU 1625 C GLN B 69 2022 1130 2332 293 539 -317 C ATOM 1626 O GLN B 69 16.918 12.402 25.445 1.00 17.25 O ANISOU 1626 O GLN B 69 2072 1347 3137 255 941 -469 O ATOM 1627 CB GLN B 69 18.488 9.820 24.903 1.00 19.00 C ANISOU 1627 CB GLN B 69 3213 986 3020 -435 927 -474 C ATOM 1628 CG GLN B 69 19.400 9.561 26.085 1.00 26.87 C ANISOU 1628 CG GLN B 69 4469 2476 3265 59 575 458 C ATOM 1629 CD GLN B 69 20.735 8.935 25.721 1.00 29.39 C ANISOU 1629 CD GLN B 69 4771 2882 3514 798 -81 93 C ATOM 1630 OE1 GLN B 69 21.325 9.049 24.644 1.00 26.95 O ANISOU 1630 OE1 GLN B 69 4267 1295 4677 419 771 397 O ATOM 1631 NE2 GLN B 69 21.291 8.205 26.700 1.00 38.39 N ANISOU 1631 NE2 GLN B 69 8186 1965 4436 2319 -30 269 N ATOM 1632 N TYR B 70 19.010 12.962 26.064 1.00 15.51 N ANISOU 1632 N TYR B 70 2515 1012 2367 -256 724 -235 N ATOM 1633 CA TYR B 70 18.510 13.974 27.018 1.00 12.79 C ANISOU 1633 CA TYR B 70 2284 1226 1348 114 421 181 C ATOM 1634 C TYR B 70 18.700 15.393 26.498 1.00 10.64 C ANISOU 1634 C TYR B 70 1705 1060 1279 88 129 -5 C ATOM 1635 O TYR B 70 18.428 16.348 27.240 1.00 12.66 O ANISOU 1635 O TYR B 70 2151 1290 1370 308 541 51 O ATOM 1636 CB TYR B 70 19.182 13.855 28.402 1.00 14.61 C ANISOU 1636 CB TYR B 70 2397 1285 1869 -21 -28 458 C ATOM 1637 CG TYR B 70 18.913 12.456 28.967 1.00 18.96 C ANISOU 1637 CG TYR B 70 2583 1774 2846 146 194 1326 C ATOM 1638 CD1 TYR B 70 17.621 12.082 29.301 1.00 20.65 C ANISOU 1638 CD1 TYR B 70 2861 1639 3345 470 1143 1367 C ATOM 1639 CD2 TYR B 70 19.913 11.523 29.155 1.00 18.67 C ANISOU 1639 CD2 TYR B 70 2461 1504 3131 -27 -333 790 C ATOM 1640 CE1 TYR B 70 17.356 10.809 29.816 1.00 25.61 C ANISOU 1640 CE1 TYR B 70 3163 2175 4391 222 971 2095 C ATOM 1641 CE2 TYR B 70 19.675 10.255 29.662 1.00 20.80 C ANISOU 1641 CE2 TYR B 70 3022 1133 3749 54 -405 408 C ATOM 1642 CZ TYR B 70 18.377 9.896 30.001 1.00 24.82 C ANISOU 1642 CZ TYR B 70 3430 1289 4711 -75 94 1362 C ATOM 1643 OH TYR B 70 18.162 8.628 30.497 1.00 41.89 O ANISOU 1643 OH TYR B 70 4280 1867 9770 -876 -1520 3011 O ATOM 1644 N VAL B 71 19.148 15.539 25.216 1.00 9.09 N ANISOU 1644 N VAL B 71 1591 668 1195 -217 10 -149 N ATOM 1645 CA VAL B 71 19.344 16.932 24.766 1.00 8.73 C ANISOU 1645 CA VAL B 71 1433 549 1336 -9 180 -240 C ATOM 1646 C VAL B 71 18.002 17.526 24.379 1.00 9.99 C ANISOU 1646 C VAL B 71 1381 391 2023 -69 27 -628 C ATOM 1647 O VAL B 71 17.329 16.960 23.505 1.00 11.39 O ANISOU 1647 O VAL B 71 1719 691 1917 137 -234 -577 O ATOM 1648 CB VAL B 71 20.322 16.982 23.572 1.00 10.23 C ANISOU 1648 CB VAL B 71 1561 782 1545 393 312 191 C ATOM 1649 CG1 VAL B 71 20.372 18.391 22.994 1.00 11.17 C ANISOU 1649 CG1 VAL B 71 2333 605 1307 278 494 -76 C ATOM 1650 CG2 VAL B 71 21.695 16.518 24.047 1.00 12.86 C ANISOU 1650 CG2 VAL B 71 1534 1052 2300 586 97 -396 C ATOM 1651 N PRO B 72 17.581 18.656 24.964 1.00 9.57 N ANISOU 1651 N PRO B 72 1716 369 1549 224 -435 -271 N ATOM 1652 CA PRO B 72 16.251 19.204 24.628 1.00 8.16 C ANISOU 1652 CA PRO B 72 1348 1033 720 238 262 -239 C ATOM 1653 C PRO B 72 16.299 19.846 23.238 1.00 6.37 C ANISOU 1653 C PRO B 72 670 814 937 -41 71 -133 C ATOM 1654 O PRO B 72 17.153 20.707 23.039 1.00 10.29 O ANISOU 1654 O PRO B 72 1380 881 1649 -527 -91 -6 O ATOM 1655 CB PRO B 72 15.954 20.115 25.813 1.00 10.30 C ANISOU 1655 CB PRO B 72 1464 1459 990 61 -206 -709 C ATOM 1656 CG PRO B 72 17.297 20.578 26.279 1.00 10.34 C ANISOU 1656 CG PRO B 72 1308 537 2085 319 -445 -476 C ATOM 1657 CD PRO B 72 18.256 19.436 26.036 1.00 10.35 C ANISOU 1657 CD PRO B 72 1716 690 1526 446 -250 -702 C ATOM 1658 N VAL B 73 15.324 19.431 22.412 1.00 7.01 N ANISOU 1658 N VAL B 73 711 1010 944 22 11 -199 N ATOM 1659 CA VAL B 73 15.305 19.887 21.046 1.00 8.24 C ANISOU 1659 CA VAL B 73 1167 984 979 334 -82 -165 C ATOM 1660 C VAL B 73 13.864 20.143 20.618 1.00 7.31 C ANISOU 1660 C VAL B 73 1106 678 993 -182 -219 9 C ATOM 1661 O VAL B 73 13.007 19.373 21.095 1.00 8.36 O ANISOU 1661 O VAL B 73 1423 579 1176 -316 -218 -10 O ATOM 1662 CB AVAL B 73 15.882 18.858 20.050 0.42 12.23 C ANISOU 1662 CB AVAL B 73 2337 1405 906 863 261 21 C ATOM 1663 CB BVAL B 73 16.084 18.921 20.134 0.58 9.92 C ANISOU 1663 CB BVAL B 73 1724 938 1108 169 469 -95 C ATOM 1664 CG1AVAL B 73 16.242 19.560 18.738 0.42 13.67 C ANISOU 1664 CG1AVAL B 73 1599 2422 1171 58 417 197 C ATOM 1665 CG1BVAL B 73 15.590 17.489 20.291 0.58 8.41 C ANISOU 1665 CG1BVAL B 73 998 954 1243 80 -3 -283 C ATOM 1666 CG2AVAL B 73 17.076 18.095 20.579 0.42 10.30 C ANISOU 1666 CG2AVAL B 73 1185 1246 1484 324 557 -160 C ATOM 1667 CG2BVAL B 73 15.972 19.320 18.665 0.58 12.60 C ANISOU 1667 CG2BVAL B 73 2036 1707 1045 -281 441 -89 C ATOM 1668 N THR B 74 13.665 21.154 19.770 1.00 8.95 N ANISOU 1668 N THR B 74 1068 1045 1289 124 -8 374 N ATOM 1669 CA THR B 74 12.280 21.258 19.215 1.00 8.19 C ANISOU 1669 CA THR B 74 1311 953 848 331 -148 -224 C ATOM 1670 C THR B 74 12.407 21.882 17.823 1.00 8.23 C ANISOU 1670 C THR B 74 1276 904 946 140 -167 -185 C ATOM 1671 O THR B 74 13.465 22.414 17.522 1.00 9.17 O ANISOU 1671 O THR B 74 1236 1307 943 90 -160 -130 O ATOM 1672 CB THR B 74 11.291 21.930 20.157 1.00 7.43 C ANISOU 1672 CB THR B 74 1157 422 1244 4 54 -207 C ATOM 1673 OG1 THR B 74 9.939 21.608 19.789 1.00 10.21 O ANISOU 1673 OG1 THR B 74 1177 785 1917 -114 12 91 O ATOM 1674 CG2 THR B 74 11.420 23.441 20.062 1.00 10.43 C ANISOU 1674 CG2 THR B 74 1811 370 1783 -69 -92 -344 C ATOM 1675 N CYS B 75 11.367 21.829 17.018 1.00 8.15 N ANISOU 1675 N CYS B 75 1314 1011 773 11 -92 -58 N ATOM 1676 CA CYS B 75 11.400 22.298 15.654 1.00 8.50 C ANISOU 1676 CA CYS B 75 1691 945 594 114 -39 -217 C ATOM 1677 C CYS B 75 10.518 23.535 15.482 1.00 11.07 C ANISOU 1677 C CYS B 75 2129 858 1222 262 -450 -252 C ATOM 1678 O CYS B 75 9.736 23.986 16.307 1.00 11.76 O ANISOU 1678 O CYS B 75 1535 1046 1887 118 -69 56 O ATOM 1679 CB CYS B 75 11.011 21.172 14.672 1.00 9.27 C ANISOU 1679 CB CYS B 75 1195 1197 1132 225 -71 -618 C ATOM 1680 SG CYS B 75 11.983 19.704 14.903 1.00 11.19 S ANISOU 1680 SG CYS B 75 1569 1022 1660 151 84 -249 S ATOM 1681 N MET B 76 10.676 24.092 14.277 1.00 10.30 N ANISOU 1681 N MET B 76 1843 562 1507 190 -303 -114 N ATOM 1682 CA MET B 76 9.859 25.253 13.925 1.00 8.77 C ANISOU 1682 CA MET B 76 1072 718 1543 11 -197 43 C ATOM 1683 C MET B 76 9.857 25.391 12.405 1.00 10.54 C ANISOU 1683 C MET B 76 1386 1099 1521 183 -450 -157 C ATOM 1684 O MET B 76 10.773 24.883 11.750 1.00 11.15 O ANISOU 1684 O MET B 76 1607 1047 1583 174 -238 -210 O ATOM 1685 CB MET B 76 10.435 26.512 14.592 1.00 10.76 C ANISOU 1685 CB MET B 76 2281 521 1285 -6 81 10 C ATOM 1686 CG MET B 76 11.908 26.815 14.197 1.00 20.06 C ANISOU 1686 CG MET B 76 3643 1519 2459 -2297 1269 -118 C ATOM 1687 SD MET B 76 12.697 27.915 15.359 1.00 15.30 S ANISOU 1687 SD MET B 76 2120 2170 1522 -95 -301 210 S ATOM 1688 CE MET B 76 14.237 28.270 14.534 1.00 11.87 C ANISOU 1688 CE MET B 76 1919 850 1742 -380 -287 -892 C ATOM 1689 N GLN B 77 8.862 26.104 11.889 1.00 9.80 N ANISOU 1689 N GLN B 77 1368 772 1583 -94 -388 127 N ATOM 1690 CA GLN B 77 8.851 26.413 10.459 1.00 9.97 C ANISOU 1690 CA GLN B 77 1203 1172 1412 101 -405 -176 C ATOM 1691 C GLN B 77 9.763 27.609 10.183 1.00 10.17 C ANISOU 1691 C GLN B 77 1731 1005 1127 224 56 -5 C ATOM 1692 O GLN B 77 9.582 28.674 10.800 1.00 11.19 O ANISOU 1692 O GLN B 77 1735 987 1531 206 62 -150 O ATOM 1693 CB GLN B 77 7.454 26.782 9.929 1.00 14.73 C ANISOU 1693 CB GLN B 77 1434 2087 2075 683 -552 191 C ATOM 1694 CG GLN B 77 7.250 26.218 8.531 1.00 29.74 C ANISOU 1694 CG GLN B 77 4582 4725 1993 824 -2321 424 C ATOM 1695 CD GLN B 77 5.788 25.805 8.310 1.00 36.52 C ANISOU 1695 CD GLN B 77 5265 5134 3478 91 -3536 547 C ATOM 1696 OE1 GLN B 77 5.062 26.682 7.864 1.00 42.04 O ANISOU 1696 OE1 GLN B 77 4543 7348 4084 1192 -2118 1825 O ATOM 1697 NE2 GLN B 77 5.422 24.568 8.624 1.00 56.57 N ANISOU 1697 NE2 GLN B 77 6965 9093 5437 -2240 -3046 6092 N ATOM 1698 N GLU B 78 10.681 27.454 9.228 1.00 10.21 N ANISOU 1698 N GLU B 78 1542 1287 1052 297 -85 8 N ATOM 1699 CA GLU B 78 11.432 28.646 8.762 1.00 9.89 C ANISOU 1699 CA GLU B 78 1404 1458 895 297 -115 137 C ATOM 1700 C GLU B 78 10.449 29.595 8.077 1.00 11.19 C ANISOU 1700 C GLU B 78 1934 1252 1065 376 -386 -2 C ATOM 1701 O GLU B 78 9.437 29.159 7.509 1.00 14.31 O ANISOU 1701 O GLU B 78 1770 1904 1762 140 -673 644 O ATOM 1702 CB GLU B 78 12.528 28.189 7.822 1.00 11.09 C ANISOU 1702 CB GLU B 78 1680 1116 1419 6 184 -353 C ATOM 1703 CG GLU B 78 13.230 29.265 7.025 1.00 11.66 C ANISOU 1703 CG GLU B 78 1911 1913 606 -351 -54 -148 C ATOM 1704 CD GLU B 78 14.078 30.214 7.847 1.00 12.91 C ANISOU 1704 CD GLU B 78 1948 2165 794 -770 399 -338 C ATOM 1705 OE1 GLU B 78 13.535 31.009 8.641 1.00 11.78 O ANISOU 1705 OE1 GLU B 78 2020 1776 679 -248 -95 -83 O ATOM 1706 OE2 GLU B 78 15.349 30.203 7.701 1.00 10.85 O ANISOU 1706 OE2 GLU B 78 1839 1557 725 -266 -120 275 O ATOM 1707 N MET B 79 10.775 30.879 8.149 1.00 12.92 N ANISOU 1707 N MET B 79 2631 1207 1069 239 305 125 N ATOM 1708 CA MET B 79 9.930 31.828 7.417 1.00 18.17 C ANISOU 1708 CA MET B 79 3170 1431 2302 94 -146 818 C ATOM 1709 C MET B 79 10.001 31.576 5.913 1.00 18.44 C ANISOU 1709 C MET B 79 3001 1898 2108 -135 -313 1368 C ATOM 1710 O MET B 79 10.993 31.160 5.312 1.00 22.47 O ANISOU 1710 O MET B 79 2697 4455 1386 -118 -331 1563 O ATOM 1711 CB MET B 79 10.318 33.259 7.761 1.00 24.13 C ANISOU 1711 CB MET B 79 5231 1342 2597 -424 -1205 1539 C ATOM 1712 CG MET B 79 11.620 33.811 7.343 1.00 28.94 C ANISOU 1712 CG MET B 79 5291 1885 3821 -1089 -1625 1407 C ATOM 1713 SD MET B 79 11.610 35.612 7.680 1.00 24.68 S ANISOU 1713 SD MET B 79 2779 2739 3861 -1120 307 -902 S ATOM 1714 CE MET B 79 10.598 36.272 6.392 1.00 22.88 C ANISOU 1714 CE MET B 79 2122 1546 5025 135 1569 512 C ATOM 1715 N ASP B 80 8.871 31.804 5.236 1.00 21.45 N ANISOU 1715 N ASP B 80 2794 2768 2588 -188 -405 1033 N ATOM 1716 CA ASP B 80 8.809 31.527 3.811 1.00 18.20 C ANISOU 1716 CA ASP B 80 2110 2212 2594 -174 -433 1064 C ATOM 1717 C ASP B 80 9.284 32.695 2.959 1.00 18.84 C ANISOU 1717 C ASP B 80 2407 2092 2660 -188 -355 990 C ATOM 1718 O ASP B 80 8.430 33.522 2.619 1.00 25.06 O ANISOU 1718 O ASP B 80 3008 2170 4345 148 -410 1424 O ATOM 1719 CB ASP B 80 7.329 31.208 3.502 1.00 23.59 C ANISOU 1719 CB ASP B 80 2145 4108 2709 -693 -255 1264 C ATOM 1720 CG ASP B 80 7.204 30.646 2.104 1.00 29.34 C ANISOU 1720 CG ASP B 80 3032 5433 2683 -1553 -621 1147 C ATOM 1721 OD1 ASP B 80 8.206 30.503 1.384 1.00 29.94 O ANISOU 1721 OD1 ASP B 80 3596 4867 2912 -1080 -375 203 O ATOM 1722 OD2 ASP B 80 6.061 30.319 1.719 1.00 42.35 O ANISOU 1722 OD2 ASP B 80 3562 9933 2595 -2437 -1260 1870 O ATOM 1723 N VAL B 81 10.564 32.804 2.646 1.00 18.51 N ANISOU 1723 N VAL B 81 2576 2796 1660 -366 -204 828 N ATOM 1724 CA VAL B 81 11.113 33.951 1.939 1.00 16.00 C ANISOU 1724 CA VAL B 81 2315 2598 1168 -242 -348 581 C ATOM 1725 C VAL B 81 11.086 33.658 0.452 1.00 14.67 C ANISOU 1725 C VAL B 81 2421 1848 1306 22 -402 423 C ATOM 1726 O VAL B 81 11.503 32.601 -0.015 1.00 18.06 O ANISOU 1726 O VAL B 81 2357 2341 2163 384 -842 -103 O ATOM 1727 CB VAL B 81 12.556 34.233 2.410 1.00 13.56 C ANISOU 1727 CB VAL B 81 1890 2508 755 212 111 258 C ATOM 1728 CG1 VAL B 81 13.232 35.241 1.479 1.00 16.44 C ANISOU 1728 CG1 VAL B 81 2150 3314 782 -224 108 389 C ATOM 1729 CG2 VAL B 81 12.528 34.691 3.862 1.00 14.78 C ANISOU 1729 CG2 VAL B 81 2948 1859 808 -614 152 199 C ATOM 1730 N THR B 82 10.526 34.574 -0.278 1.00 15.42 N ANISOU 1730 N THR B 82 2525 2116 1216 -29 -478 562 N ATOM 1731 CA THR B 82 10.475 34.480 -1.740 1.00 18.13 C ANISOU 1731 CA THR B 82 2806 2869 1213 549 22 577 C ATOM 1732 C THR B 82 11.890 34.495 -2.296 1.00 18.63 C ANISOU 1732 C THR B 82 2682 2508 1887 305 84 419 C ATOM 1733 O THR B 82 12.609 35.491 -2.153 1.00 18.79 O ANISOU 1733 O THR B 82 3112 2726 1303 87 -339 305 O ATOM 1734 CB THR B 82 9.637 35.660 -2.232 1.00 16.55 C ANISOU 1734 CB THR B 82 2656 2807 826 347 -387 454 C ATOM 1735 OG1 THR B 82 8.317 35.512 -1.640 1.00 24.47 O ANISOU 1735 OG1 THR B 82 2562 5154 1581 862 -170 486 O ATOM 1736 CG2 THR B 82 9.496 35.588 -3.719 1.00 25.49 C ANISOU 1736 CG2 THR B 82 4703 4203 779 1762 -207 109 C ATOM 1737 N GLY B 83 12.263 33.374 -2.901 1.00 15.42 N ANISOU 1737 N GLY B 83 2345 2262 1252 350 -200 836 N ATOM 1738 CA GLY B 83 13.622 33.175 -3.421 1.00 15.15 C ANISOU 1738 CA GLY B 83 2146 2085 1525 87 -267 442 C ATOM 1739 C GLY B 83 14.505 32.527 -2.382 1.00 14.50 C ANISOU 1739 C GLY B 83 2366 1876 1265 191 -365 93 C ATOM 1740 O GLY B 83 15.693 32.196 -2.611 1.00 17.70 O ANISOU 1740 O GLY B 83 2743 2240 1744 849 -366 269 O ATOM 1741 N GLY B 84 14.024 32.265 -1.158 1.00 17.35 N ANISOU 1741 N GLY B 84 3170 1986 1438 -269 -228 450 N ATOM 1742 CA GLY B 84 14.854 31.517 -0.207 1.00 16.01 C ANISOU 1742 CA GLY B 84 2932 1720 1431 -237 -33 431 C ATOM 1743 C GLY B 84 15.197 30.101 -0.593 1.00 17.77 C ANISOU 1743 C GLY B 84 3312 2188 1250 208 -329 -62 C ATOM 1744 O GLY B 84 14.483 29.472 -1.387 1.00 20.41 O ANISOU 1744 O GLY B 84 3802 2305 1650 366 -826 -224 O ATOM 1745 N LEU B 85 16.286 29.524 -0.082 1.00 16.54 N ANISOU 1745 N LEU B 85 3156 1933 1195 31 -184 -16 N ATOM 1746 CA LEU B 85 16.677 28.147 -0.330 1.00 14.05 C ANISOU 1746 CA LEU B 85 3125 1769 445 -100 -164 263 C ATOM 1747 C LEU B 85 15.541 27.183 -0.012 1.00 12.69 C ANISOU 1747 C LEU B 85 2716 1939 166 11 -324 121 C ATOM 1748 O LEU B 85 14.988 27.263 1.078 1.00 14.99 O ANISOU 1748 O LEU B 85 3215 2056 425 -164 30 -47 O ATOM 1749 CB LEU B 85 17.896 27.812 0.526 1.00 13.29 C ANISOU 1749 CB LEU B 85 2544 2180 326 -60 192 -96 C ATOM 1750 CG LEU B 85 18.713 26.572 0.220 1.00 20.38 C ANISOU 1750 CG LEU B 85 3556 3568 618 1221 181 -296 C ATOM 1751 CD1 LEU B 85 19.224 26.559 -1.228 1.00 20.35 C ANISOU 1751 CD1 LEU B 85 4344 2709 680 1030 427 -216 C ATOM 1752 CD2 LEU B 85 19.895 26.460 1.179 1.00 25.21 C ANISOU 1752 CD2 LEU B 85 3529 5114 934 1617 79 -76 C ATOM 1753 N LYS B 86 15.273 26.289 -0.959 1.00 16.03 N ANISOU 1753 N LYS B 86 3272 2691 128 -474 -441 -89 N ATOM 1754 CA LYS B 86 14.236 25.275 -0.798 1.00 18.08 C ANISOU 1754 CA LYS B 86 3338 2724 809 -562 -714 -132 C ATOM 1755 C LYS B 86 14.745 24.022 -0.060 1.00 17.09 C ANISOU 1755 C LYS B 86 3155 2336 1002 -213 67 -364 C ATOM 1756 O LYS B 86 15.964 23.805 -0.028 1.00 14.45 O ANISOU 1756 O LYS B 86 3057 1672 761 -471 286 -504 O ATOM 1757 CB LYS B 86 13.714 24.804 -2.158 1.00 21.16 C ANISOU 1757 CB LYS B 86 2969 4173 899 -756 -479 -702 C ATOM 1758 CG LYS B 86 12.856 25.834 -2.878 1.00 26.86 C ANISOU 1758 CG LYS B 86 3718 5090 1399 -1231 -1335 367 C ATOM 1759 CD LYS B 86 13.689 26.977 -3.408 1.00 35.32 C ANISOU 1759 CD LYS B 86 4009 5959 3451 -711 331 1513 C ATOM 1760 CE LYS B 86 14.817 26.552 -4.351 1.00 42.45 C ANISOU 1760 CE LYS B 86 3236 7992 4900 -817 178 142 C ATOM 1761 NZ LYS B 86 16.187 26.695 -3.749 1.00 28.64 N ANISOU 1761 NZ LYS B 86 3913 5990 980 -1735 530 120 N ATOM 1762 N LYS B 87 13.814 23.235 0.463 1.00 14.37 N ANISOU 1762 N LYS B 87 2561 2216 683 -263 -504 -553 N ATOM 1763 CA LYS B 87 14.065 21.954 1.112 1.00 14.99 C ANISOU 1763 CA LYS B 87 2862 2240 595 -315 -657 -460 C ATOM 1764 C LYS B 87 15.277 22.036 2.051 1.00 13.57 C ANISOU 1764 C LYS B 87 2273 1787 1095 -139 -454 -722 C ATOM 1765 O LYS B 87 16.224 21.237 2.029 1.00 13.92 O ANISOU 1765 O LYS B 87 2122 1840 1326 -237 85 -518 O ATOM 1766 CB LYS B 87 14.277 20.860 0.075 1.00 13.77 C ANISOU 1766 CB LYS B 87 2487 2146 601 -413 -304 -381 C ATOM 1767 CG LYS B 87 13.008 20.672 -0.774 1.00 22.50 C ANISOU 1767 CG LYS B 87 3343 3545 1660 -832 -1140 -1108 C ATOM 1768 CD LYS B 87 13.337 19.770 -1.963 1.00 28.62 C ANISOU 1768 CD LYS B 87 4389 4036 2451 -597 -1492 -1917 C ATOM 1769 CE LYS B 87 12.089 19.601 -2.821 1.00 31.61 C ANISOU 1769 CE LYS B 87 4510 4753 2748 -137 -1746 -2443 C ATOM 1770 NZ LYS B 87 12.243 20.367 -4.085 1.00 42.87 N ANISOU 1770 NZ LYS B 87 4908 6931 4448 -46 -2679 -313 N ATOM 1771 N CYS B 88 15.249 23.001 2.933 1.00 13.16 N ANISOU 1771 N CYS B 88 2503 1803 692 -478 -172 -663 N ATOM 1772 CA CYS B 88 16.377 23.370 3.774 1.00 10.07 C ANISOU 1772 CA CYS B 88 2012 1176 640 15 -130 -437 C ATOM 1773 C CYS B 88 16.083 23.180 5.251 1.00 10.21 C ANISOU 1773 C CYS B 88 1925 1292 660 122 -101 -427 C ATOM 1774 O CYS B 88 15.052 23.603 5.782 1.00 10.50 O ANISOU 1774 O CYS B 88 2024 1173 792 36 -13 -387 O ATOM 1775 CB CYS B 88 16.735 24.869 3.548 1.00 12.50 C ANISOU 1775 CB CYS B 88 2070 1354 1325 -291 64 -254 C ATOM 1776 SG CYS B 88 18.176 25.435 4.510 1.00 13.41 S ANISOU 1776 SG CYS B 88 2309 1622 1162 -429 16 -201 S ATOM 1777 N ILE B 89 16.990 22.519 5.938 1.00 10.21 N ANISOU 1777 N ILE B 89 2031 1172 677 56 -55 -294 N ATOM 1778 CA ILE B 89 16.924 22.275 7.359 1.00 9.53 C ANISOU 1778 CA ILE B 89 2173 779 669 -121 4 -369 C ATOM 1779 C ILE B 89 18.060 23.069 7.991 1.00 10.59 C ANISOU 1779 C ILE B 89 2177 1093 754 -396 106 -509 C ATOM 1780 O ILE B 89 19.218 23.031 7.571 1.00 11.39 O ANISOU 1780 O ILE B 89 2134 1366 830 -98 72 -290 O ATOM 1781 CB ILE B 89 17.052 20.786 7.727 1.00 8.83 C ANISOU 1781 CB ILE B 89 1693 842 821 -158 61 -293 C ATOM 1782 CG1 ILE B 89 15.980 19.908 7.100 1.00 10.40 C ANISOU 1782 CG1 ILE B 89 1857 952 1143 -354 -488 220 C ATOM 1783 CG2 ILE B 89 17.171 20.628 9.251 1.00 10.55 C ANISOU 1783 CG2 ILE B 89 2582 676 750 218 -120 -476 C ATOM 1784 CD1 ILE B 89 16.525 18.553 6.694 1.00 22.88 C ANISOU 1784 CD1 ILE B 89 3761 910 4023 -271 -1125 -827 C ATOM 1785 N ARG B 90 17.655 23.833 9.003 1.00 10.78 N ANISOU 1785 N ARG B 90 2145 973 978 -353 111 -535 N ATOM 1786 CA ARG B 90 18.616 24.691 9.675 1.00 8.01 C ANISOU 1786 CA ARG B 90 2056 503 485 146 -39 -370 C ATOM 1787 C ARG B 90 18.681 24.316 11.165 1.00 9.60 C ANISOU 1787 C ARG B 90 1895 999 754 -138 34 248 C ATOM 1788 O ARG B 90 17.690 23.860 11.750 1.00 11.71 O ANISOU 1788 O ARG B 90 1791 1652 1006 -129 316 -22 O ATOM 1789 CB ARG B 90 18.260 26.194 9.577 1.00 9.25 C ANISOU 1789 CB ARG B 90 2721 536 255 269 -86 -287 C ATOM 1790 CG ARG B 90 18.257 26.683 8.107 1.00 11.64 C ANISOU 1790 CG ARG B 90 2035 1771 616 705 -1 400 C ATOM 1791 CD ARG B 90 17.815 28.132 8.027 1.00 10.18 C ANISOU 1791 CD ARG B 90 1498 1639 730 403 -451 418 C ATOM 1792 NE ARG B 90 17.904 28.845 6.797 1.00 9.56 N ANISOU 1792 NE ARG B 90 2045 1238 348 208 -284 -107 N ATOM 1793 CZ ARG B 90 17.185 28.762 5.698 1.00 10.01 C ANISOU 1793 CZ ARG B 90 2083 1721 0 -393 69 -111 C ATOM 1794 NH1 ARG B 90 16.237 27.812 5.639 1.00 11.92 N ANISOU 1794 NH1 ARG B 90 2016 1431 1082 -251 -103 -271 N ATOM 1795 NH2 ARG B 90 17.382 29.531 4.654 1.00 14.35 N ANISOU 1795 NH2 ARG B 90 2907 2384 160 -402 199 293 N ATOM 1796 N VAL B 91 19.861 24.514 11.770 1.00 7.84 N ANISOU 1796 N VAL B 91 1720 884 376 160 145 85 N ATOM 1797 CA VAL B 91 20.090 24.284 13.182 1.00 7.58 C ANISOU 1797 CA VAL B 91 2163 460 256 247 360 -23 C ATOM 1798 C VAL B 91 20.557 25.555 13.887 1.00 7.11 C ANISOU 1798 C VAL B 91 2164 278 262 175 234 244 C ATOM 1799 O VAL B 91 21.362 26.311 13.350 1.00 9.70 O ANISOU 1799 O VAL B 91 1384 1092 1211 -12 165 373 O ATOM 1800 CB VAL B 91 21.186 23.186 13.294 1.00 11.55 C ANISOU 1800 CB VAL B 91 3238 373 776 653 24 163 C ATOM 1801 CG1 VAL B 91 21.709 23.071 14.721 1.00 21.88 C ANISOU 1801 CG1 VAL B 91 4948 1943 1424 1178 -1026 499 C ATOM 1802 CG2 VAL B 91 20.699 21.820 12.832 1.00 17.94 C ANISOU 1802 CG2 VAL B 91 5112 371 1332 217 1269 -270 C ATOM 1803 N MET B 92 20.099 25.678 15.135 1.00 9.26 N ANISOU 1803 N MET B 92 1938 1229 351 -101 203 -327 N ATOM 1804 CA MET B 92 20.625 26.577 16.161 1.00 7.74 C ANISOU 1804 CA MET B 92 1445 972 524 240 -129 -191 C ATOM 1805 C MET B 92 20.874 25.717 17.408 1.00 7.86 C ANISOU 1805 C MET B 92 1135 1385 466 477 223 -57 C ATOM 1806 O MET B 92 19.916 25.424 18.110 1.00 9.42 O ANISOU 1806 O MET B 92 1189 1291 1098 77 401 -57 O ATOM 1807 CB MET B 92 19.763 27.782 16.502 1.00 9.14 C ANISOU 1807 CB MET B 92 1209 875 1389 187 -210 -358 C ATOM 1808 CG MET B 92 20.390 28.697 17.556 1.00 10.98 C ANISOU 1808 CG MET B 92 1192 534 2447 -142 -384 -532 C ATOM 1809 SD MET B 92 21.756 29.698 16.928 1.00 10.02 S ANISOU 1809 SD MET B 92 1448 1043 1317 24 -144 -64 S ATOM 1810 CE MET B 92 20.792 31.042 16.237 1.00 9.45 C ANISOU 1810 CE MET B 92 1579 898 1115 447 147 -484 C ATOM 1811 N MET B 93 22.146 25.354 17.583 1.00 8.18 N ANISOU 1811 N MET B 93 969 1267 871 88 42 137 N ATOM 1812 CA MET B 93 22.492 24.528 18.742 1.00 10.17 C ANISOU 1812 CA MET B 93 1710 1025 1130 205 -645 -92 C ATOM 1813 C MET B 93 23.152 25.422 19.781 1.00 9.16 C ANISOU 1813 C MET B 93 2151 566 763 -512 -18 290 C ATOM 1814 O MET B 93 24.149 26.124 19.476 1.00 14.72 O ANISOU 1814 O MET B 93 2396 2279 920 -1268 155 27 O ATOM 1815 CB MET B 93 23.453 23.413 18.343 1.00 11.68 C ANISOU 1815 CB MET B 93 2308 835 1297 287 -165 123 C ATOM 1816 CG MET B 93 23.904 22.503 19.489 1.00 12.28 C ANISOU 1816 CG MET B 93 2296 529 1840 137 -363 304 C ATOM 1817 SD MET B 93 25.089 21.243 18.976 1.00 20.41 S ANISOU 1817 SD MET B 93 3880 1518 2357 1347 -819 -415 S ATOM 1818 CE MET B 93 24.559 21.040 17.265 1.00 47.93 C ANISOU 1818 CE MET B 93 3039 12447 2727 -2106 527 -4584 C ATOM 1819 N THR B 94 22.648 25.460 21.011 1.00 8.63 N ANISOU 1819 N THR B 94 1586 996 697 -30 -109 298 N ATOM 1820 CA THR B 94 23.199 26.348 22.046 1.00 10.07 C ANISOU 1820 CA THR B 94 1575 1380 872 111 -198 67 C ATOM 1821 C THR B 94 24.086 25.524 22.979 1.00 9.82 C ANISOU 1821 C THR B 94 1464 1580 688 174 -45 173 C ATOM 1822 O THR B 94 23.606 24.526 23.545 1.00 9.76 O ANISOU 1822 O THR B 94 1309 1258 1143 238 -124 86 O ATOM 1823 CB THR B 94 22.034 26.984 22.813 1.00 10.78 C ANISOU 1823 CB THR B 94 1451 1142 1503 62 -305 -315 C ATOM 1824 OG1 THR B 94 21.093 27.589 21.900 1.00 10.18 O ANISOU 1824 OG1 THR B 94 1619 1131 1119 147 -115 -145 O ATOM 1825 CG2 THR B 94 22.524 28.098 23.732 1.00 11.83 C ANISOU 1825 CG2 THR B 94 1771 901 1821 -9 -521 -275 C ATOM 1826 N VAL B 95 25.339 25.917 23.115 1.00 10.53 N ANISOU 1826 N VAL B 95 1607 1099 1294 52 -245 -12 N ATOM 1827 CA VAL B 95 26.308 25.074 23.827 1.00 9.53 C ANISOU 1827 CA VAL B 95 1373 828 1420 131 -170 -282 C ATOM 1828 C VAL B 95 27.027 25.857 24.913 1.00 10.51 C ANISOU 1828 C VAL B 95 1794 833 1365 -23 -334 -152 C ATOM 1829 O VAL B 95 27.259 27.081 24.791 1.00 11.87 O ANISOU 1829 O VAL B 95 2063 954 1495 -301 -578 -4 O ATOM 1830 CB VAL B 95 27.351 24.445 22.876 1.00 13.98 C ANISOU 1830 CB VAL B 95 1306 1630 2377 -221 61 -1138 C ATOM 1831 CG1 VAL B 95 26.626 23.797 21.717 1.00 14.22 C ANISOU 1831 CG1 VAL B 95 2171 1568 1664 -232 -90 -684 C ATOM 1832 CG2 VAL B 95 28.350 25.496 22.416 1.00 15.77 C ANISOU 1832 CG2 VAL B 95 1417 2703 1870 -545 -22 -528 C ATOM 1833 N GLN B 96 27.451 25.245 26.002 1.00 11.53 N ANISOU 1833 N GLN B 96 1383 1160 1839 -4 -614 119 N ATOM 1834 CA GLN B 96 28.352 25.845 26.957 1.00 12.27 C ANISOU 1834 CA GLN B 96 1075 2022 1564 104 -271 -288 C ATOM 1835 C GLN B 96 29.771 25.630 26.433 1.00 9.65 C ANISOU 1835 C GLN B 96 1126 1175 1365 227 -296 420 C ATOM 1836 O GLN B 96 30.220 24.516 26.190 1.00 12.23 O ANISOU 1836 O GLN B 96 1262 1395 1990 167 -314 -287 O ATOM 1837 CB GLN B 96 28.232 25.205 28.332 1.00 16.64 C ANISOU 1837 CB GLN B 96 1518 3409 1394 -160 32 -264 C ATOM 1838 CG GLN B 96 29.105 25.868 29.364 1.00 20.16 C ANISOU 1838 CG GLN B 96 2015 4189 1456 -517 -273 -248 C ATOM 1839 CD GLN B 96 29.025 25.099 30.680 1.00 22.86 C ANISOU 1839 CD GLN B 96 2441 4678 1566 -1335 -293 -36 C ATOM 1840 OE1 GLN B 96 29.294 23.892 30.673 1.00 40.35 O ANISOU 1840 OE1 GLN B 96 6262 5512 3557 1138 -1845 1066 O ATOM 1841 NE2 GLN B 96 28.672 25.783 31.759 1.00 36.86 N ANISOU 1841 NE2 GLN B 96 4973 7769 1263 -1386 -464 -1054 N ATOM 1842 N THR B 97 30.470 26.738 26.256 1.00 13.04 N ANISOU 1842 N THR B 97 1463 1437 2053 -112 -179 263 N ATOM 1843 CA THR B 97 31.804 26.680 25.668 1.00 14.77 C ANISOU 1843 CA THR B 97 1369 2121 2121 -473 -230 41 C ATOM 1844 C THR B 97 32.571 27.967 25.957 1.00 14.21 C ANISOU 1844 C THR B 97 1415 1842 2140 -316 -745 473 C ATOM 1845 O THR B 97 31.917 29.025 26.013 1.00 14.84 O ANISOU 1845 O THR B 97 1841 1951 1847 -74 -416 651 O ATOM 1846 CB THR B 97 31.749 26.434 24.148 1.00 12.70 C ANISOU 1846 CB THR B 97 1133 1624 2067 -15 -224 255 C ATOM 1847 OG1 THR B 97 33.068 26.270 23.626 1.00 14.30 O ANISOU 1847 OG1 THR B 97 1142 1737 2555 -398 4 76 O ATOM 1848 CG2 THR B 97 31.165 27.601 23.359 1.00 14.55 C ANISOU 1848 CG2 THR B 97 2212 1190 2124 310 696 354 C ATOM 1849 N ASP B 98 33.885 27.804 26.108 1.00 13.52 N ANISOU 1849 N ASP B 98 1301 2155 1682 -425 -196 280 N ATOM 1850 CA ASP B 98 34.808 28.909 26.239 1.00 19.36 C ANISOU 1850 CA ASP B 98 1786 3417 2151 -1414 -5 282 C ATOM 1851 C ASP B 98 35.294 29.398 24.889 1.00 16.64 C ANISOU 1851 C ASP B 98 2265 1864 2194 -657 390 -66 C ATOM 1852 O ASP B 98 36.047 30.374 24.792 1.00 18.54 O ANISOU 1852 O ASP B 98 2493 2347 2205 -987 215 226 O ATOM 1853 CB AASP B 98 36.042 28.471 27.059 0.63 23.15 C ANISOU 1853 CB AASP B 98 2304 3622 2868 -1823 -798 495 C ATOM 1854 CB BASP B 98 36.038 28.467 27.056 0.37 23.61 C ANISOU 1854 CB BASP B 98 2279 3640 3053 -1951 -817 781 C ATOM 1855 CG AASP B 98 35.758 28.482 28.541 0.63 23.93 C ANISOU 1855 CG AASP B 98 2621 3678 2793 -2361 -1023 435 C ATOM 1856 CG BASP B 98 35.727 28.301 28.525 0.37 25.34 C ANISOU 1856 CG BASP B 98 2799 3903 2926 -1868 -1055 704 C ATOM 1857 OD1AASP B 98 34.734 29.099 28.939 0.63 25.11 O ANISOU 1857 OD1AASP B 98 3477 2835 3227 -2431 -231 -86 O ATOM 1858 OD1BASP B 98 34.948 27.380 28.863 0.37 25.98 O ANISOU 1858 OD1BASP B 98 3262 3804 2805 -1765 -235 462 O ATOM 1859 OD2AASP B 98 36.544 27.873 29.307 0.63 30.18 O ANISOU 1859 OD2AASP B 98 4293 3709 3466 -2174 -1634 1182 O ATOM 1860 OD2BASP B 98 36.257 29.094 29.330 0.37 30.03 O ANISOU 1860 OD2BASP B 98 3137 4885 3386 -2120 -1152 149 O ATOM 1861 N VAL B 99 34.965 28.703 23.811 1.00 13.37 N ANISOU 1861 N VAL B 99 1379 1567 2135 320 -243 142 N ATOM 1862 CA VAL B 99 35.489 29.119 22.518 1.00 13.22 C ANISOU 1862 CA VAL B 99 1577 1222 2226 213 88 -206 C ATOM 1863 C VAL B 99 34.960 30.480 22.107 1.00 10.96 C ANISOU 1863 C VAL B 99 1309 1296 1558 72 -160 -248 C ATOM 1864 O VAL B 99 33.754 30.712 22.171 1.00 15.47 O ANISOU 1864 O VAL B 99 1289 1441 3149 15 -100 691 O ATOM 1865 CB VAL B 99 35.114 28.099 21.446 1.00 11.78 C ANISOU 1865 CB VAL B 99 1422 1037 2016 58 -542 253 C ATOM 1866 CG1 VAL B 99 35.543 28.670 20.093 1.00 12.38 C ANISOU 1866 CG1 VAL B 99 1283 1214 2206 -208 124 -30 C ATOM 1867 CG2 VAL B 99 35.771 26.750 21.695 1.00 12.63 C ANISOU 1867 CG2 VAL B 99 1112 1006 2681 102 -370 -53 C ATOM 1868 N PRO B 100 35.811 31.435 21.737 1.00 11.84 N ANISOU 1868 N PRO B 100 1231 1686 1583 184 -69 378 N ATOM 1869 CA PRO B 100 35.269 32.758 21.412 1.00 12.85 C ANISOU 1869 CA PRO B 100 1407 1490 1987 49 -531 260 C ATOM 1870 C PRO B 100 34.261 32.731 20.265 1.00 10.95 C ANISOU 1870 C PRO B 100 1081 1403 1677 175 -204 41 C ATOM 1871 O PRO B 100 34.315 31.864 19.402 1.00 12.30 O ANISOU 1871 O PRO B 100 1125 1137 2412 -27 -313 -232 O ATOM 1872 CB PRO B 100 36.494 33.548 20.941 1.00 14.14 C ANISOU 1872 CB PRO B 100 1263 1417 2692 68 -514 169 C ATOM 1873 CG PRO B 100 37.595 32.884 21.742 1.00 15.85 C ANISOU 1873 CG PRO B 100 1458 1194 3371 218 -843 10 C ATOM 1874 CD PRO B 100 37.272 31.400 21.646 1.00 14.79 C ANISOU 1874 CD PRO B 100 1235 1282 3104 -46 -471 164 C ATOM 1875 N GLN B 101 33.402 33.753 20.282 1.00 10.86 N ANISOU 1875 N GLN B 101 1006 1487 1634 209 -76 -21 N ATOM 1876 CA GLN B 101 32.358 33.856 19.242 1.00 10.36 C ANISOU 1876 CA GLN B 101 1099 1290 1547 366 -68 -32 C ATOM 1877 C GLN B 101 32.940 33.761 17.825 1.00 11.01 C ANISOU 1877 C GLN B 101 1264 1320 1598 152 14 -49 C ATOM 1878 O GLN B 101 32.377 33.104 16.921 1.00 10.45 O ANISOU 1878 O GLN B 101 1173 1079 1717 329 78 -236 O ATOM 1879 CB GLN B 101 31.565 35.145 19.430 1.00 9.93 C ANISOU 1879 CB GLN B 101 1109 938 1726 65 -106 -39 C ATOM 1880 CG GLN B 101 30.488 35.394 18.331 1.00 9.73 C ANISOU 1880 CG GLN B 101 932 1157 1608 273 107 133 C ATOM 1881 CD GLN B 101 29.761 36.676 18.672 1.00 9.47 C ANISOU 1881 CD GLN B 101 1194 1308 1096 276 -25 -158 C ATOM 1882 OE1 GLN B 101 28.699 36.740 19.360 1.00 12.71 O ANISOU 1882 OE1 GLN B 101 1140 1919 1771 386 177 -360 O ATOM 1883 NE2 GLN B 101 30.406 37.759 18.230 1.00 9.27 N ANISOU 1883 NE2 GLN B 101 1023 1080 1419 275 -319 -191 N ATOM 1884 N ASP B 102 34.044 34.445 17.540 1.00 11.32 N ANISOU 1884 N ASP B 102 1409 1101 1793 125 159 -212 N ATOM 1885 CA ASP B 102 34.583 34.442 16.166 1.00 10.90 C ANISOU 1885 CA ASP B 102 1209 1140 1792 49 84 -55 C ATOM 1886 C ASP B 102 35.376 33.167 15.825 1.00 12.31 C ANISOU 1886 C ASP B 102 1394 1318 1967 222 600 158 C ATOM 1887 O ASP B 102 35.915 33.127 14.711 1.00 15.63 O ANISOU 1887 O ASP B 102 2550 1206 2182 88 1133 211 O ATOM 1888 CB ASP B 102 35.414 35.706 15.918 1.00 14.26 C ANISOU 1888 CB ASP B 102 1356 1376 2688 -199 276 22 C ATOM 1889 CG ASP B 102 36.696 35.794 16.699 1.00 13.19 C ANISOU 1889 CG ASP B 102 1303 1168 2539 -313 400 174 C ATOM 1890 OD1 ASP B 102 37.060 34.804 17.399 1.00 15.51 O ANISOU 1890 OD1 ASP B 102 1400 1473 3021 90 468 370 O ATOM 1891 OD2 ASP B 102 37.395 36.812 16.666 1.00 22.31 O ANISOU 1891 OD2 ASP B 102 1630 1603 5244 -818 -93 618 O ATOM 1892 N GLN B 103 35.422 32.163 16.688 1.00 11.07 N ANISOU 1892 N GLN B 103 1429 1154 1624 -17 248 -44 N ATOM 1893 CA GLN B 103 36.041 30.876 16.369 1.00 11.60 C ANISOU 1893 CA GLN B 103 859 1211 2336 44 188 111 C ATOM 1894 C GLN B 103 35.034 29.745 16.381 1.00 12.24 C ANISOU 1894 C GLN B 103 1051 1247 2352 -108 86 -174 C ATOM 1895 O GLN B 103 35.435 28.590 16.088 1.00 14.33 O ANISOU 1895 O GLN B 103 1280 1373 2794 -101 188 -433 O ATOM 1896 CB GLN B 103 37.161 30.557 17.378 1.00 11.91 C ANISOU 1896 CB GLN B 103 1142 1407 1976 -19 85 -352 C ATOM 1897 CG GLN B 103 38.327 31.519 17.115 1.00 14.49 C ANISOU 1897 CG GLN B 103 1006 1516 2983 -16 -202 81 C ATOM 1898 CD GLN B 103 39.446 31.142 18.066 1.00 15.13 C ANISOU 1898 CD GLN B 103 1090 1590 3069 271 -197 -60 C ATOM 1899 OE1 GLN B 103 39.638 31.690 19.149 1.00 18.95 O ANISOU 1899 OE1 GLN B 103 1650 2599 2949 44 -389 -131 O ATOM 1900 NE2 GLN B 103 40.253 30.149 17.659 1.00 21.20 N ANISOU 1900 NE2 GLN B 103 2050 2149 3856 1123 268 339 N ATOM 1901 N ILE B 104 33.773 29.986 16.707 1.00 11.98 N ANISOU 1901 N ILE B 104 1059 1233 2260 -109 224 323 N ATOM 1902 CA ILE B 104 32.771 28.920 16.610 1.00 10.02 C ANISOU 1902 CA ILE B 104 973 1217 1618 -8 419 -102 C ATOM 1903 C ILE B 104 32.625 28.528 15.144 1.00 12.60 C ANISOU 1903 C ILE B 104 1834 1388 1565 378 663 -264 C ATOM 1904 O ILE B 104 32.651 29.410 14.281 1.00 13.69 O ANISOU 1904 O ILE B 104 1961 1595 1646 -299 292 -110 O ATOM 1905 CB ILE B 104 31.426 29.395 17.174 1.00 9.57 C ANISOU 1905 CB ILE B 104 1060 1124 1454 -84 403 -471 C ATOM 1906 CG1 ILE B 104 31.509 29.787 18.657 1.00 10.20 C ANISOU 1906 CG1 ILE B 104 1182 1348 1344 -128 256 -222 C ATOM 1907 CG2 ILE B 104 30.299 28.388 16.924 1.00 11.29 C ANISOU 1907 CG2 ILE B 104 881 1433 1974 -110 92 -450 C ATOM 1908 CD1 ILE B 104 31.669 28.571 19.561 1.00 13.09 C ANISOU 1908 CD1 ILE B 104 1147 1829 1997 497 -321 159 C ATOM 1909 N ARG B 105 32.526 27.222 14.879 1.00 11.87 N ANISOU 1909 N ARG B 105 1449 1433 1629 231 -92 -170 N ATOM 1910 CA ARG B 105 32.454 26.704 13.528 1.00 13.89 C ANISOU 1910 CA ARG B 105 1827 1588 1862 34 -362 -411 C ATOM 1911 C ARG B 105 31.023 26.363 13.095 1.00 13.31 C ANISOU 1911 C ARG B 105 1732 1514 1809 -179 -152 -104 C ATOM 1912 O ARG B 105 30.466 25.315 13.441 1.00 14.06 O ANISOU 1912 O ARG B 105 1965 1324 2054 -28 -3 -68 O ATOM 1913 CB ARG B 105 33.343 25.451 13.344 1.00 14.14 C ANISOU 1913 CB ARG B 105 2005 1693 1675 178 -72 -358 C ATOM 1914 CG ARG B 105 34.827 25.904 13.496 1.00 20.05 C ANISOU 1914 CG ARG B 105 1755 2960 2902 62 683 322 C ATOM 1915 CD ARG B 105 35.805 24.813 13.156 1.00 24.34 C ANISOU 1915 CD ARG B 105 2098 2885 4266 356 784 733 C ATOM 1916 NE ARG B 105 37.147 25.031 13.636 1.00 31.24 N ANISOU 1916 NE ARG B 105 2184 3707 5980 690 402 -489 N ATOM 1917 CZ ARG B 105 37.959 24.046 14.039 1.00 33.71 C ANISOU 1917 CZ ARG B 105 2229 3111 7469 -185 -805 -123 C ATOM 1918 NH1 ARG B 105 37.576 22.762 14.037 1.00 38.12 N ANISOU 1918 NH1 ARG B 105 2303 2801 9381 218 338 -2342 N ATOM 1919 NH2 ARG B 105 39.175 24.369 14.458 1.00 45.83 N ANISOU 1919 NH2 ARG B 105 1890 3983 11541 -767 -1052 969 N ATOM 1920 N HIS B 106 30.466 27.266 12.306 1.00 11.58 N ANISOU 1920 N HIS B 106 1149 1137 2114 -102 197 -139 N ATOM 1921 CA HIS B 106 29.113 27.091 11.764 1.00 12.09 C ANISOU 1921 CA HIS B 106 1340 1242 2010 -12 30 -491 C ATOM 1922 C HIS B 106 29.253 26.219 10.533 1.00 13.07 C ANISOU 1922 C HIS B 106 1762 1169 2036 -239 411 -480 C ATOM 1923 O HIS B 106 30.296 26.283 9.884 1.00 15.20 O ANISOU 1923 O HIS B 106 1860 2069 1844 -353 480 -258 O ATOM 1924 CB HIS B 106 28.539 28.470 11.433 1.00 13.32 C ANISOU 1924 CB HIS B 106 1509 1394 2160 230 -274 -682 C ATOM 1925 CG HIS B 106 28.573 29.308 12.689 1.00 13.69 C ANISOU 1925 CG HIS B 106 1664 1277 2261 -302 481 -675 C ATOM 1926 ND1 HIS B 106 29.405 30.375 12.998 1.00 14.53 N ANISOU 1926 ND1 HIS B 106 2454 1801 1265 -920 154 -285 N ATOM 1927 CD2 HIS B 106 27.756 29.127 13.770 1.00 10.61 C ANISOU 1927 CD2 HIS B 106 1201 585 2245 384 325 41 C ATOM 1928 CE1 HIS B 106 29.102 30.822 14.218 1.00 9.60 C ANISOU 1928 CE1 HIS B 106 1227 1375 1045 17 -94 -30 C ATOM 1929 NE2 HIS B 106 28.102 30.064 14.679 1.00 13.26 N ANISOU 1929 NE2 HIS B 106 1757 1502 1779 -44 264 10 N ATOM 1930 N VAL B 107 28.286 25.377 10.210 1.00 13.83 N ANISOU 1930 N VAL B 107 2292 1440 1523 -728 368 -287 N ATOM 1931 CA VAL B 107 28.483 24.411 9.129 1.00 14.44 C ANISOU 1931 CA VAL B 107 2144 1340 2003 259 -385 -501 C ATOM 1932 C VAL B 107 27.363 24.385 8.088 1.00 11.14 C ANISOU 1932 C VAL B 107 1578 1173 1483 155 224 -366 C ATOM 1933 O VAL B 107 26.181 24.310 8.451 1.00 12.78 O ANISOU 1933 O VAL B 107 1693 2000 1165 92 364 -300 O ATOM 1934 CB AVAL B 107 28.422 23.014 9.805 0.50 9.64 C ANISOU 1934 CB AVAL B 107 924 1574 1163 -96 96 -518 C ATOM 1935 CB BVAL B 107 28.770 23.002 9.662 0.50 17.56 C ANISOU 1935 CB BVAL B 107 2474 1834 2366 767 10 29 C ATOM 1936 CG1AVAL B 107 28.412 21.878 8.787 0.50 6.76 C ANISOU 1936 CG1AVAL B 107 680 1298 590 217 16 -177 C ATOM 1937 CG1BVAL B 107 27.452 22.480 10.134 0.50 23.72 C ANISOU 1937 CG1BVAL B 107 3037 2353 3625 -10 33 634 C ATOM 1938 CG2AVAL B 107 29.599 22.881 10.774 0.50 7.79 C ANISOU 1938 CG2AVAL B 107 681 800 1478 -159 31 -765 C ATOM 1939 CG2BVAL B 107 29.369 22.099 8.598 0.50 24.64 C ANISOU 1939 CG2BVAL B 107 2637 2951 3774 2326 -1071 -1146 C ATOM 1940 N TYR B 108 27.746 24.473 6.831 1.00 11.66 N ANISOU 1940 N TYR B 108 1605 1290 1537 -206 424 -234 N ATOM 1941 CA TYR B 108 26.766 24.626 5.747 1.00 15.27 C ANISOU 1941 CA TYR B 108 2628 1653 1520 -256 -20 -357 C ATOM 1942 C TYR B 108 27.011 23.513 4.747 1.00 14.67 C ANISOU 1942 C TYR B 108 2123 1779 1673 -388 313 -434 C ATOM 1943 O TYR B 108 28.127 23.473 4.210 1.00 18.49 O ANISOU 1943 O TYR B 108 2195 2542 2288 -601 534 -717 O ATOM 1944 CB TYR B 108 26.863 26.024 5.093 1.00 15.25 C ANISOU 1944 CB TYR B 108 2479 1724 1591 -76 -4 -155 C ATOM 1945 CG TYR B 108 26.574 27.084 6.121 1.00 14.20 C ANISOU 1945 CG TYR B 108 2487 1519 1388 -431 504 123 C ATOM 1946 CD1 TYR B 108 25.270 27.295 6.560 1.00 18.05 C ANISOU 1946 CD1 TYR B 108 2442 1098 3318 106 457 -50 C ATOM 1947 CD2 TYR B 108 27.575 27.865 6.655 1.00 15.49 C ANISOU 1947 CD2 TYR B 108 2655 1809 1423 -355 275 -132 C ATOM 1948 CE1 TYR B 108 25.019 28.264 7.510 1.00 21.79 C ANISOU 1948 CE1 TYR B 108 2523 2136 3621 -49 780 -658 C ATOM 1949 CE2 TYR B 108 27.311 28.835 7.607 1.00 16.16 C ANISOU 1949 CE2 TYR B 108 2479 1486 2175 319 -90 -279 C ATOM 1950 CZ TYR B 108 26.020 29.044 8.036 1.00 18.09 C ANISOU 1950 CZ TYR B 108 2523 1793 2558 528 -68 -137 C ATOM 1951 OH TYR B 108 25.717 29.994 8.983 1.00 16.55 O ANISOU 1951 OH TYR B 108 2797 1542 1949 189 567 340 O ATOM 1952 N LEU B 109 26.041 22.627 4.568 1.00 13.72 N ANISOU 1952 N LEU B 109 2246 1329 1637 -327 398 -191 N ATOM 1953 CA LEU B 109 26.292 21.472 3.710 1.00 15.77 C ANISOU 1953 CA LEU B 109 2745 1216 2032 218 -301 -282 C ATOM 1954 C LEU B 109 25.312 21.364 2.559 1.00 13.81 C ANISOU 1954 C LEU B 109 2097 1726 1425 290 345 -322 C ATOM 1955 O LEU B 109 24.315 22.075 2.580 1.00 15.57 O ANISOU 1955 O LEU B 109 2406 1859 1651 593 170 -482 O ATOM 1956 CB LEU B 109 26.167 20.190 4.554 1.00 15.50 C ANISOU 1956 CB LEU B 109 2473 1440 1975 372 131 -97 C ATOM 1957 CG LEU B 109 27.102 20.108 5.783 1.00 14.91 C ANISOU 1957 CG LEU B 109 1924 1972 1768 23 548 240 C ATOM 1958 CD1 LEU B 109 26.860 18.816 6.565 1.00 14.86 C ANISOU 1958 CD1 LEU B 109 2340 2024 1281 -67 806 101 C ATOM 1959 CD2 LEU B 109 28.556 20.251 5.338 1.00 16.98 C ANISOU 1959 CD2 LEU B 109 2001 2000 2448 -459 807 -285 C ATOM 1960 N GLU B 110 25.580 20.450 1.623 1.00 16.48 N ANISOU 1960 N GLU B 110 2148 2390 1722 599 278 -704 N ATOM 1961 CA GLU B 110 24.699 20.168 0.485 1.00 17.16 C ANISOU 1961 CA GLU B 110 2795 2342 1382 -145 375 -471 C ATOM 1962 C GLU B 110 24.429 21.478 -0.241 1.00 14.22 C ANISOU 1962 C GLU B 110 2395 2096 912 -386 298 -786 C ATOM 1963 O GLU B 110 25.401 22.229 -0.464 1.00 18.74 O ANISOU 1963 O GLU B 110 2784 2994 1343 -950 97 -292 O ATOM 1964 CB GLU B 110 23.418 19.460 0.922 1.00 16.58 C ANISOU 1964 CB GLU B 110 2675 2170 1454 -1 49 -28 C ATOM 1965 CG GLU B 110 23.606 18.197 1.752 1.00 16.37 C ANISOU 1965 CG GLU B 110 2666 1830 1725 210 35 -250 C ATOM 1966 CD GLU B 110 24.302 17.065 1.025 1.00 22.57 C ANISOU 1966 CD GLU B 110 3887 2672 2018 906 217 -611 C ATOM 1967 OE1 GLU B 110 24.318 17.037 -0.222 1.00 29.81 O ANISOU 1967 OE1 GLU B 110 6130 3156 2039 1298 -425 -1157 O ATOM 1968 OE2 GLU B 110 24.885 16.140 1.653 1.00 26.12 O ANISOU 1968 OE2 GLU B 110 5205 2570 2149 1571 1074 -370 O ATOM 1969 N LYS B 111 23.201 21.778 -0.637 1.00 15.66 N ANISOU 1969 N LYS B 111 2373 2642 937 -48 663 -536 N ATOM 1970 CA LYS B 111 23.030 23.003 -1.444 1.00 16.89 C ANISOU 1970 CA LYS B 111 2861 2699 858 -32 229 -618 C ATOM 1971 C LYS B 111 23.118 24.250 -0.576 1.00 17.83 C ANISOU 1971 C LYS B 111 3154 2629 993 -88 68 -607 C ATOM 1972 O LYS B 111 23.147 25.365 -1.102 1.00 21.36 O ANISOU 1972 O LYS B 111 4178 2717 1222 -283 900 -464 O ATOM 1973 CB LYS B 111 21.738 22.918 -2.234 1.00 20.33 C ANISOU 1973 CB LYS B 111 3421 3390 914 -323 -222 -532 C ATOM 1974 CG LYS B 111 21.750 21.787 -3.261 1.00 22.43 C ANISOU 1974 CG LYS B 111 3900 3158 1464 -187 -621 -640 C ATOM 1975 CD LYS B 111 20.378 21.737 -3.949 1.00 26.45 C ANISOU 1975 CD LYS B 111 3987 3971 2090 -480 -824 -1059 C ATOM 1976 CE LYS B 111 20.275 20.529 -4.857 1.00 27.54 C ANISOU 1976 CE LYS B 111 4651 3213 2598 -939 -913 -713 C ATOM 1977 NZ LYS B 111 19.063 20.597 -5.713 1.00 41.32 N ANISOU 1977 NZ LYS B 111 7136 4084 4480 -907 -3312 -1153 N ATOM 1978 N ALA B 112 23.179 24.062 0.762 1.00 15.60 N ANISOU 1978 N ALA B 112 2452 2466 1010 557 -211 -727 N ATOM 1979 CA ALA B 112 23.293 25.235 1.630 1.00 16.78 C ANISOU 1979 CA ALA B 112 2639 2614 1123 -30 221 -804 C ATOM 1980 C ALA B 112 24.730 25.752 1.647 1.00 16.71 C ANISOU 1980 C ALA B 112 2483 2687 1181 182 101 -767 C ATOM 1981 O ALA B 112 24.996 26.766 2.307 1.00 14.82 O ANISOU 1981 O ALA B 112 2488 2377 764 127 89 -413 O ATOM 1982 CB ALA B 112 22.798 24.957 3.026 1.00 16.54 C ANISOU 1982 CB ALA B 112 2843 2346 1095 -39 184 -743 C ATOM 1983 N VAL B 113 25.659 25.154 0.884 1.00 16.92 N ANISOU 1983 N VAL B 113 2784 2371 1273 44 455 -510 N ATOM 1984 CA VAL B 113 27.020 25.727 0.890 1.00 16.78 C ANISOU 1984 CA VAL B 113 2912 2520 942 -175 715 -870 C ATOM 1985 C VAL B 113 27.021 27.161 0.385 1.00 18.82 C ANISOU 1985 C VAL B 113 2974 2622 1556 -147 884 -586 C ATOM 1986 O VAL B 113 27.946 27.934 0.710 1.00 21.54 O ANISOU 1986 O VAL B 113 3705 2813 1668 -612 792 -705 O ATOM 1987 CB VAL B 113 28.013 24.895 0.049 1.00 20.24 C ANISOU 1987 CB VAL B 113 3212 3116 1362 496 842 -601 C ATOM 1988 CG1 VAL B 113 28.236 23.513 0.670 1.00 25.87 C ANISOU 1988 CG1 VAL B 113 3555 3199 3075 810 120 -322 C ATOM 1989 CG2 VAL B 113 27.554 24.792 -1.390 1.00 27.07 C ANISOU 1989 CG2 VAL B 113 4288 4774 1222 1951 884 -1199 C ATOM 1990 N VAL B 114 26.000 27.531 -0.382 1.00 20.16 N ANISOU 1990 N VAL B 114 3392 3066 1203 -4 863 -357 N ATOM 1991 CA VAL B 114 25.888 28.894 -0.888 1.00 23.53 C ANISOU 1991 CA VAL B 114 4313 3334 1292 269 1116 -14 C ATOM 1992 C VAL B 114 25.573 29.894 0.225 1.00 23.23 C ANISOU 1992 C VAL B 114 4385 2803 1639 -178 1293 -8 C ATOM 1993 O VAL B 114 25.581 31.116 -0.027 1.00 25.84 O ANISOU 1993 O VAL B 114 4704 2795 2319 -843 460 1 O ATOM 1994 CB VAL B 114 24.794 29.028 -1.958 1.00 30.16 C ANISOU 1994 CB VAL B 114 5741 3700 2019 519 39 -14 C ATOM 1995 CG1 VAL B 114 25.033 27.988 -3.053 1.00 29.03 C ANISOU 1995 CG1 VAL B 114 5039 4059 1933 944 -181 -57 C ATOM 1996 CG2 VAL B 114 23.422 28.919 -1.295 1.00 27.09 C ANISOU 1996 CG2 VAL B 114 4916 3366 2013 1378 -673 -349 C ATOM 1997 N LEU B 115 25.299 29.413 1.433 1.00 19.48 N ANISOU 1997 N LEU B 115 2771 3352 1280 -481 1012 -232 N ATOM 1998 CA LEU B 115 25.024 30.291 2.563 1.00 19.22 C ANISOU 1998 CA LEU B 115 3279 2302 1721 -41 1093 -52 C ATOM 1999 C LEU B 115 26.321 30.641 3.286 1.00 19.81 C ANISOU 1999 C LEU B 115 3392 2548 1586 -271 1257 -656 C ATOM 2000 O LEU B 115 26.346 31.379 4.287 1.00 23.52 O ANISOU 2000 O LEU B 115 4074 2374 2490 -415 1500 -1207 O ATOM 2001 CB LEU B 115 24.016 29.633 3.531 1.00 16.05 C ANISOU 2001 CB LEU B 115 2631 2173 1296 653 872 147 C ATOM 2002 CG LEU B 115 22.614 29.346 2.932 1.00 19.39 C ANISOU 2002 CG LEU B 115 2513 2848 2004 747 711 465 C ATOM 2003 CD1 LEU B 115 21.795 28.520 3.913 1.00 21.85 C ANISOU 2003 CD1 LEU B 115 3263 2339 2700 -131 740 164 C ATOM 2004 CD2 LEU B 115 21.903 30.618 2.517 1.00 25.02 C ANISOU 2004 CD2 LEU B 115 4031 3760 1714 1415 93 1029 C ATOM 2005 N ARG B 116 27.454 30.098 2.829 1.00 19.11 N ANISOU 2005 N ARG B 116 3418 2272 1572 175 753 -532 N ATOM 2006 CA ARG B 116 28.668 30.475 3.560 1.00 22.24 C ANISOU 2006 CA ARG B 116 3826 2604 2020 731 -61 -534 C ATOM 2007 C ARG B 116 28.967 31.968 3.451 1.00 19.28 C ANISOU 2007 C ARG B 116 3065 2767 1494 410 -659 -255 C ATOM 2008 O ARG B 116 29.011 32.578 2.393 1.00 24.95 O ANISOU 2008 O ARG B 116 4965 3059 1458 1056 -227 -156 O ATOM 2009 CB ARG B 116 29.853 29.647 3.073 1.00 24.07 C ANISOU 2009 CB ARG B 116 3596 2913 2638 502 519 -334 C ATOM 2010 CG ARG B 116 29.653 28.142 3.192 1.00 27.69 C ANISOU 2010 CG ARG B 116 4480 2694 3347 830 304 -811 C ATOM 2011 CD ARG B 116 30.469 27.401 2.143 1.00 38.41 C ANISOU 2011 CD ARG B 116 5961 3878 4753 847 1339 -1674 C ATOM 2012 NE ARG B 116 31.837 27.904 2.089 1.00 42.58 N ANISOU 2012 NE ARG B 116 6238 5084 4855 385 2428 -1799 N ATOM 2013 CZ ARG B 116 32.659 27.896 1.055 1.00 48.56 C ANISOU 2013 CZ ARG B 116 7507 6124 4819 891 2939 -1094 C ATOM 2014 NH1 ARG B 116 32.219 27.373 -0.084 1.00 52.64 N ANISOU 2014 NH1 ARG B 116 8422 8073 3506 5 2583 299 N ATOM 2015 NH2 ARG B 116 33.888 28.397 1.163 1.00 37.97 N ANISOU 2015 NH2 ARG B 116 6966 3993 3466 1849 3107 305 N ATOM 2016 N PRO B 117 29.191 32.614 4.591 1.00 21.10 N ANISOU 2016 N PRO B 117 3579 3020 1417 -129 -39 -389 N ATOM 2017 CA PRO B 117 29.446 34.060 4.600 1.00 24.38 C ANISOU 2017 CA PRO B 117 4512 3187 1565 -642 262 -498 C ATOM 2018 C PRO B 117 30.811 34.427 4.011 1.00 29.82 C ANISOU 2018 C PRO B 117 4690 4058 2582 -872 411 298 C ATOM 2019 O PRO B 117 30.943 35.585 3.582 1.00 35.86 O ANISOU 2019 O PRO B 117 6484 4378 2763 -1000 1310 616 O ATOM 2020 CB PRO B 117 29.389 34.414 6.085 1.00 26.64 C ANISOU 2020 CB PRO B 117 4948 3467 1706 98 -90 -824 C ATOM 2021 CG PRO B 117 29.685 33.141 6.811 1.00 28.01 C ANISOU 2021 CG PRO B 117 5114 3841 1687 -196 -713 -546 C ATOM 2022 CD PRO B 117 29.163 32.027 5.940 1.00 25.52 C ANISOU 2022 CD PRO B 117 4741 3462 1494 -358 -563 -167 C ATOM 2023 N ASP B 118 31.746 33.501 3.975 1.00 33.48 N ANISOU 2023 N ASP B 118 4397 5170 3152 -482 503 633 N ATOM 2024 CA ASP B 118 33.129 33.603 3.588 1.00 44.88 C ANISOU 2024 CA ASP B 118 4825 7241 4985 -135 1424 2129 C ATOM 2025 C ASP B 118 33.339 33.848 2.092 1.00 52.76 C ANISOU 2025 C ASP B 118 5778 9553 4716 -370 1952 1242 C ATOM 2026 O ASP B 118 34.421 34.282 1.693 1.00 60.10 O ANISOU 2026 O ASP B 118 5547 12438 4850 -229 2735 1224 O ATOM 2027 CB ASP B 118 33.946 32.349 3.922 1.00 49.17 C ANISOU 2027 CB ASP B 118 4437 6945 7302 -66 916 1099 C ATOM 2028 CG ASP B 118 33.258 31.226 4.647 1.00 52.86 C ANISOU 2028 CG ASP B 118 6041 6484 7559 -177 -2 1750 C ATOM 2029 OD1 ASP B 118 32.055 31.242 4.988 1.00 53.90 O ANISOU 2029 OD1 ASP B 118 6672 6078 7729 -1988 1151 485 O ATOM 2030 OD2 ASP B 118 33.996 30.231 4.897 1.00 66.73 O ANISOU 2030 OD2 ASP B 118 8095 7364 9897 409 -3248 2044 O ATOM 2031 N LEU B 119 32.344 33.561 1.283 1.00 57.30 N ANISOU 2031 N LEU B 119 6498 10524 4749 -256 1833 94 N ATOM 2032 CA LEU B 119 32.422 33.540 -0.163 1.00 53.16 C ANISOU 2032 CA LEU B 119 5933 9455 4810 830 2476 -743 C ATOM 2033 C LEU B 119 31.915 34.780 -0.870 1.00 49.42 C ANISOU 2033 C LEU B 119 5878 9324 3577 1043 1273 -1831 C ATOM 2034 O LEU B 119 30.846 35.259 -0.468 1.00 52.63 O ANISOU 2034 O LEU B 119 6058 11731 2208 1887 1103 -1145 O ATOM 2035 CB LEU B 119 31.542 32.367 -0.615 1.00 57.66 C ANISOU 2035 CB LEU B 119 6483 9393 6030 903 2900 -1757 C ATOM 2036 CG LEU B 119 31.911 30.940 -0.250 1.00 65.16 C ANISOU 2036 CG LEU B 119 6844 9480 8435 521 2962 -658 C ATOM 2037 CD1 LEU B 119 30.847 29.959 -0.754 1.00 70.63 C ANISOU 2037 CD1 LEU B 119 6758 9586 10491 449 4004 -2205 C ATOM 2038 CD2 LEU B 119 33.266 30.554 -0.832 1.00 78.23 C ANISOU 2038 CD2 LEU B 119 6104 10576 13045 1628 2790 -398 C ATOM 2039 N SER B 120 32.553 35.299 -1.924 1.00 45.26 N ANISOU 2039 N SER B 120 4342 8431 4425 1422 970 -1301 N ATOM 2040 CA SER B 120 31.820 36.227 -2.800 1.00 46.79 C ANISOU 2040 CA SER B 120 5138 7476 5164 1840 1063 -1521 C ATOM 2041 C SER B 120 31.412 35.507 -4.084 1.00 42.00 C ANISOU 2041 C SER B 120 4754 6771 4434 2274 1007 -731 C ATOM 2042 O SER B 120 32.000 34.468 -4.365 1.00 33.39 O ANISOU 2042 O SER B 120 3538 4881 4269 896 322 191 O ATOM 2043 CB SER B 120 32.572 37.504 -3.129 1.00 50.59 C ANISOU 2043 CB SER B 120 6189 7539 5494 1523 1879 -1790 C ATOM 2044 OG SER B 120 33.832 37.305 -3.714 1.00 58.45 O ANISOU 2044 OG SER B 120 7162 8375 6670 1491 3134 -883 O ATOM 2045 N LEU B 121 30.440 35.966 -4.877 1.00 36.36 N ANISOU 2045 N LEU B 121 4492 5275 4047 2076 1789 32 N ATOM 2046 CA LEU B 121 30.048 35.140 -6.039 1.00 39.44 C ANISOU 2046 CA LEU B 121 3655 6453 4878 1048 1235 -331 C ATOM 2047 C LEU B 121 31.031 35.181 -7.202 1.00 30.29 C ANISOU 2047 C LEU B 121 3166 4982 3360 387 111 -502 C ATOM 2048 O LEU B 121 31.582 36.191 -7.628 1.00 33.54 O ANISOU 2048 O LEU B 121 5337 4310 3096 1161 222 325 O ATOM 2049 CB LEU B 121 28.678 35.508 -6.607 1.00 44.02 C ANISOU 2049 CB LEU B 121 3487 6777 6461 728 1206 786 C ATOM 2050 CG LEU B 121 28.161 36.933 -6.505 1.00 48.94 C ANISOU 2050 CG LEU B 121 4003 6598 7994 784 836 1664 C ATOM 2051 CD1 LEU B 121 28.832 37.825 -7.549 1.00 63.15 C ANISOU 2051 CD1 LEU B 121 7148 6940 9907 -1286 2261 1305 C ATOM 2052 CD2 LEU B 121 26.640 36.987 -6.657 1.00 47.00 C ANISOU 2052 CD2 LEU B 121 4119 5473 8266 647 -53 914 C ATOM 2053 N THR B 122 31.273 34.009 -7.807 1.00 27.63 N ANISOU 2053 N THR B 122 3341 4554 2603 524 -380 73 N ATOM 2054 CA THR B 122 32.216 34.030 -8.916 1.00 27.46 C ANISOU 2054 CA THR B 122 3596 3671 3166 1255 40 369 C ATOM 2055 C THR B 122 31.594 34.516 -10.215 1.00 22.72 C ANISOU 2055 C THR B 122 3312 2566 2754 480 75 -82 C ATOM 2056 O THR B 122 30.699 33.843 -10.749 1.00 30.81 O ANISOU 2056 O THR B 122 4626 3490 3589 -216 -340 -793 O ATOM 2057 CB THR B 122 32.769 32.598 -9.095 1.00 27.99 C ANISOU 2057 CB THR B 122 4480 2999 3154 655 -106 473 C ATOM 2058 OG1 THR B 122 33.620 32.305 -7.977 1.00 23.20 O ANISOU 2058 OG1 THR B 122 3858 1807 3148 363 -1 74 O ATOM 2059 CG2 THR B 122 33.579 32.527 -10.371 1.00 25.28 C ANISOU 2059 CG2 THR B 122 4501 2109 2995 -212 -285 -818 C ATOM 2060 N LYS B 123 32.041 35.641 -10.748 1.00 23.45 N ANISOU 2060 N LYS B 123 3901 2078 2931 998 847 -325 N ATOM 2061 CA LYS B 123 31.359 36.270 -11.883 1.00 21.22 C ANISOU 2061 CA LYS B 123 3469 1577 3015 1012 991 -416 C ATOM 2062 C LYS B 123 31.597 35.470 -13.159 1.00 17.93 C ANISOU 2062 C LYS B 123 2425 1284 3104 663 622 -540 C ATOM 2063 O LYS B 123 30.688 35.235 -13.941 1.00 23.71 O ANISOU 2063 O LYS B 123 2901 2742 3366 1161 25 -448 O ATOM 2064 CB LYS B 123 31.803 37.711 -12.124 1.00 24.68 C ANISOU 2064 CB LYS B 123 4050 1122 4204 1233 342 -701 C ATOM 2065 CG LYS B 123 30.985 38.507 -13.137 1.00 27.62 C ANISOU 2065 CG LYS B 123 3929 1447 5120 259 -234 100 C ATOM 2066 CD LYS B 123 31.330 39.996 -13.204 1.00 31.61 C ANISOU 2066 CD LYS B 123 4881 1661 5470 -206 -803 691 C ATOM 2067 CE LYS B 123 30.709 40.654 -14.433 1.00 32.61 C ANISOU 2067 CE LYS B 123 4329 2077 5983 769 -749 717 C ATOM 2068 NZ LYS B 123 31.167 42.070 -14.648 1.00 28.56 N ANISOU 2068 NZ LYS B 123 4261 1864 4727 1050 -822 481 N ATOM 2069 N ASN B 124 32.837 35.048 -13.366 1.00 16.38 N ANISOU 2069 N ASN B 124 2238 1116 2872 264 1042 -201 N ATOM 2070 CA ASN B 124 33.099 34.135 -14.491 1.00 15.00 C ANISOU 2070 CA ASN B 124 1983 1663 2053 769 481 32 C ATOM 2071 C ASN B 124 33.772 32.877 -13.969 1.00 13.62 C ANISOU 2071 C ASN B 124 2032 1248 1896 449 164 -210 C ATOM 2072 O ASN B 124 34.927 32.870 -13.527 1.00 16.63 O ANISOU 2072 O ASN B 124 2056 1698 2562 406 -74 212 O ATOM 2073 CB ASN B 124 33.905 34.810 -15.601 1.00 18.03 C ANISOU 2073 CB ASN B 124 2603 1917 2332 542 603 339 C ATOM 2074 CG ASN B 124 33.866 34.073 -16.935 1.00 18.49 C ANISOU 2074 CG ASN B 124 3329 1453 2242 922 994 507 C ATOM 2075 OD1 ASN B 124 33.931 32.821 -17.006 1.00 19.76 O ANISOU 2075 OD1 ASN B 124 2402 1470 3637 1128 350 213 O ATOM 2076 ND2 ASN B 124 33.754 34.778 -18.066 1.00 23.56 N ANISOU 2076 ND2 ASN B 124 4110 2463 2377 712 256 871 N ATOM 2077 N THR B 125 33.020 31.768 -14.006 1.00 15.40 N ANISOU 2077 N THR B 125 2116 1347 2388 386 544 -695 N ATOM 2078 CA THR B 125 33.603 30.555 -13.422 1.00 15.86 C ANISOU 2078 CA THR B 125 2371 1072 2583 194 849 -554 C ATOM 2079 C THR B 125 34.594 29.840 -14.329 1.00 12.16 C ANISOU 2079 C THR B 125 1434 1473 1713 385 -252 -704 C ATOM 2080 O THR B 125 35.310 28.943 -13.902 1.00 14.77 O ANISOU 2080 O THR B 125 1587 1091 2935 166 -77 -128 O ATOM 2081 CB THR B 125 32.473 29.552 -13.080 1.00 18.41 C ANISOU 2081 CB THR B 125 2889 2006 2100 -483 870 -570 C ATOM 2082 OG1 THR B 125 31.752 29.253 -14.292 1.00 19.87 O ANISOU 2082 OG1 THR B 125 2378 2237 2936 346 319 -1124 O ATOM 2083 CG2 THR B 125 31.554 30.188 -12.039 1.00 16.00 C ANISOU 2083 CG2 THR B 125 2399 1444 2237 82 630 -119 C ATOM 2084 N GLU B 126 34.612 30.247 -15.600 1.00 12.95 N ANISOU 2084 N GLU B 126 1798 1148 1974 -176 162 -372 N ATOM 2085 CA GLU B 126 35.329 29.490 -16.608 1.00 12.77 C ANISOU 2085 CA GLU B 126 1786 1304 1762 -231 163 -381 C ATOM 2086 C GLU B 126 36.569 30.141 -17.171 1.00 13.03 C ANISOU 2086 C GLU B 126 1550 898 2503 64 141 -88 C ATOM 2087 O GLU B 126 37.479 29.379 -17.565 1.00 14.33 O ANISOU 2087 O GLU B 126 1731 1179 2535 9 345 -508 O ATOM 2088 CB GLU B 126 34.393 29.277 -17.811 1.00 14.15 C ANISOU 2088 CB GLU B 126 1993 1098 2286 -128 -256 -545 C ATOM 2089 CG GLU B 126 33.078 28.589 -17.425 1.00 10.83 C ANISOU 2089 CG GLU B 126 1518 620 1978 569 -260 -221 C ATOM 2090 CD GLU B 126 33.251 27.076 -17.501 1.00 10.20 C ANISOU 2090 CD GLU B 126 1537 616 1722 482 -52 -518 C ATOM 2091 OE1 GLU B 126 34.404 26.516 -17.561 1.00 11.84 O ANISOU 2091 OE1 GLU B 126 1744 718 2038 795 -37 -99 O ATOM 2092 OE2 GLU B 126 32.182 26.394 -17.493 1.00 12.61 O ANISOU 2092 OE2 GLU B 126 1842 1138 1810 -33 110 -198 O ATOM 2093 N LEU B 127 36.605 31.476 -17.261 1.00 14.29 N ANISOU 2093 N LEU B 127 2263 860 2307 -178 -359 -296 N ATOM 2094 CA LEU B 127 37.859 32.036 -17.757 1.00 17.69 C ANISOU 2094 CA LEU B 127 2899 1297 2524 -583 -104 331 C ATOM 2095 C LEU B 127 38.075 33.475 -17.298 1.00 18.93 C ANISOU 2095 C LEU B 127 2803 1008 3384 -441 401 586 C ATOM 2096 O LEU B 127 37.191 33.990 -16.572 1.00 18.26 O ANISOU 2096 O LEU B 127 2106 1518 3314 -467 -243 20 O ATOM 2097 CB LEU B 127 37.899 31.842 -19.262 1.00 24.36 C ANISOU 2097 CB LEU B 127 4318 2527 2410 -1515 -117 730 C ATOM 2098 CG LEU B 127 36.764 32.468 -20.060 1.00 27.25 C ANISOU 2098 CG LEU B 127 5518 2593 2243 -664 -372 589 C ATOM 2099 CD1 LEU B 127 37.108 33.909 -20.419 1.00 32.55 C ANISOU 2099 CD1 LEU B 127 7732 2017 2620 -371 -70 -15 C ATOM 2100 CD2 LEU B 127 36.497 31.651 -21.309 1.00 35.76 C ANISOU 2100 CD2 LEU B 127 7372 2909 3306 -1917 -1714 321 C ATOM 2101 OXT LEU B 127 39.126 34.041 -17.662 1.00 20.18 O ANISOU 2101 OXT LEU B 127 2331 1821 3515 -781 41 -162 O TER 2102 LEU B 127 ATOM 2103 N MET C 1 26.870 29.259 36.473 1.00 31.76 N ANISOU 2103 N MET C 1 2715 5550 3801 -999 -428 -2462 N ATOM 2104 CA MET C 1 25.975 28.108 36.517 1.00 33.21 C ANISOU 2104 CA MET C 1 2911 6060 3647 -1387 -893 -2073 C ATOM 2105 C MET C 1 25.506 27.765 35.108 1.00 28.40 C ANISOU 2105 C MET C 1 3147 4555 3088 -1292 -614 -1311 C ATOM 2106 O MET C 1 25.331 28.670 34.281 1.00 35.58 O ANISOU 2106 O MET C 1 5617 3457 4447 -961 -1711 -1476 O ATOM 2107 CB MET C 1 24.776 28.369 37.435 1.00 32.12 C ANISOU 2107 CB MET C 1 3500 5857 2847 -1393 -624 -1138 C ATOM 2108 CG MET C 1 23.863 27.143 37.492 1.00 28.85 C ANISOU 2108 CG MET C 1 3621 4982 2357 -815 -673 -858 C ATOM 2109 SD MET C 1 22.559 27.382 38.698 1.00 32.33 S ANISOU 2109 SD MET C 1 4803 4565 2917 -946 301 -339 S ATOM 2110 CE MET C 1 23.500 27.936 40.118 1.00 67.66 C ANISOU 2110 CE MET C 1 4705 20000 1002 3350 -1714 -1632 C ATOM 2111 N MET C 2 25.327 26.469 34.880 1.00 20.87 N ANISOU 2111 N MET C 2 2308 3991 1633 541 -695 -800 N ATOM 2112 CA MET C 2 24.940 25.943 33.573 1.00 14.98 C ANISOU 2112 CA MET C 2 2309 2348 1036 597 -280 1 C ATOM 2113 C MET C 2 23.531 26.419 33.263 1.00 12.10 C ANISOU 2113 C MET C 2 2160 1583 852 115 -328 -84 C ATOM 2114 O MET C 2 22.736 26.755 34.139 1.00 14.69 O ANISOU 2114 O MET C 2 1956 2883 742 257 -401 25 O ATOM 2115 CB MET C 2 25.107 24.427 33.561 1.00 15.20 C ANISOU 2115 CB MET C 2 1913 2228 1633 262 -468 670 C ATOM 2116 CG MET C 2 24.782 23.730 32.266 1.00 17.87 C ANISOU 2116 CG MET C 2 3565 1545 1679 698 14 430 C ATOM 2117 SD MET C 2 25.637 24.358 30.801 1.00 17.34 S ANISOU 2117 SD MET C 2 2027 2747 1814 167 -110 62 S ATOM 2118 CE MET C 2 25.074 23.185 29.572 1.00 16.24 C ANISOU 2118 CE MET C 2 1983 2681 1505 -708 -232 588 C ATOM 2119 N ILE C 3 23.259 26.463 31.966 1.00 11.49 N ANISOU 2119 N ILE C 3 1799 1723 843 -434 -320 -164 N ATOM 2120 CA ILE C 3 21.944 26.794 31.432 1.00 12.22 C ANISOU 2120 CA ILE C 3 2099 1064 1479 -312 -701 -28 C ATOM 2121 C ILE C 3 21.412 25.550 30.740 1.00 9.88 C ANISOU 2121 C ILE C 3 1332 987 1436 -268 -180 -72 C ATOM 2122 O ILE C 3 22.202 24.821 30.050 1.00 11.87 O ANISOU 2122 O ILE C 3 1175 1517 1818 -110 -171 -302 O ATOM 2123 CB ILE C 3 22.103 27.952 30.436 1.00 15.09 C ANISOU 2123 CB ILE C 3 2116 851 2767 -83 -294 282 C ATOM 2124 CG1 ILE C 3 22.904 29.105 31.042 1.00 14.43 C ANISOU 2124 CG1 ILE C 3 2162 1191 2129 -287 -10 113 C ATOM 2125 CG2 ILE C 3 20.758 28.385 29.907 1.00 12.70 C ANISOU 2125 CG2 ILE C 3 2132 960 1734 261 -94 14 C ATOM 2126 CD1 ILE C 3 22.226 29.720 32.254 1.00 17.86 C ANISOU 2126 CD1 ILE C 3 2759 2867 1158 -260 -209 108 C ATOM 2127 N ARG C 4 20.131 25.245 30.856 1.00 9.09 N ANISOU 2127 N ARG C 4 1252 1449 752 -157 -159 -23 N ATOM 2128 CA ARG C 4 19.525 24.024 30.303 1.00 10.13 C ANISOU 2128 CA ARG C 4 1084 1316 1449 -244 -170 69 C ATOM 2129 C ARG C 4 18.128 24.296 29.794 1.00 8.54 C ANISOU 2129 C ARG C 4 1035 1237 973 -46 47 -241 C ATOM 2130 O ARG C 4 17.354 25.064 30.394 1.00 9.85 O ANISOU 2130 O ARG C 4 1586 1335 821 275 224 -30 O ATOM 2131 CB ARG C 4 19.415 22.853 31.311 1.00 14.60 C ANISOU 2131 CB ARG C 4 1641 1578 2328 -79 -227 606 C ATOM 2132 CG ARG C 4 20.849 22.439 31.660 1.00 21.29 C ANISOU 2132 CG ARG C 4 2294 3029 2767 602 -1048 586 C ATOM 2133 CD ARG C 4 21.055 20.989 31.870 1.00 18.83 C ANISOU 2133 CD ARG C 4 1890 2837 2429 1312 105 -675 C ATOM 2134 NE ARG C 4 22.435 20.669 32.225 1.00 17.27 N ANISOU 2134 NE ARG C 4 1840 3395 1325 1014 72 -1 N ATOM 2135 CZ ARG C 4 23.386 20.313 31.353 1.00 15.15 C ANISOU 2135 CZ ARG C 4 1329 3238 1188 566 87 452 C ATOM 2136 NH1 ARG C 4 23.131 20.236 30.049 1.00 12.74 N ANISOU 2136 NH1 ARG C 4 2545 1099 1197 162 -70 -94 N ATOM 2137 NH2 ARG C 4 24.629 20.031 31.759 1.00 15.17 N ANISOU 2137 NH2 ARG C 4 1341 1908 2512 364 -226 611 N ATOM 2138 N GLY C 5 17.796 23.657 28.665 1.00 9.94 N ANISOU 2138 N GLY C 5 1253 1157 1367 -112 -189 -430 N ATOM 2139 CA GLY C 5 16.407 23.773 28.209 1.00 8.15 C ANISOU 2139 CA GLY C 5 1054 1056 986 -244 104 -295 C ATOM 2140 C GLY C 5 15.510 22.757 28.868 1.00 7.97 C ANISOU 2140 C GLY C 5 1204 1122 702 -49 -107 -3 C ATOM 2141 O GLY C 5 15.938 21.631 29.165 1.00 11.40 O ANISOU 2141 O GLY C 5 1371 1057 1904 -37 9 175 O ATOM 2142 N ILE C 6 14.256 23.195 29.077 1.00 9.31 N ANISOU 2142 N ILE C 6 1016 1155 1368 -190 57 331 N ATOM 2143 CA ILE C 6 13.210 22.292 29.524 1.00 7.37 C ANISOU 2143 CA ILE C 6 1408 1052 340 -457 -114 95 C ATOM 2144 C ILE C 6 12.130 22.285 28.429 1.00 6.80 C ANISOU 2144 C ILE C 6 1444 903 234 -360 -83 48 C ATOM 2145 O ILE C 6 11.643 23.335 28.039 1.00 9.38 O ANISOU 2145 O ILE C 6 1372 1062 1129 -42 -84 145 O ATOM 2146 CB AILE C 6 12.610 22.718 30.882 0.83 8.61 C ANISOU 2146 CB AILE C 6 2051 1008 212 -712 -99 167 C ATOM 2147 CB BILE C 6 12.522 22.680 30.839 0.17 9.17 C ANISOU 2147 CB BILE C 6 1956 1360 169 -406 -82 188 C ATOM 2148 CG1AILE C 6 13.668 22.948 31.978 0.83 11.62 C ANISOU 2148 CG1AILE C 6 2101 2017 296 -393 -111 -205 C ATOM 2149 CG1BILE C 6 13.388 23.450 31.837 0.17 10.52 C ANISOU 2149 CG1BILE C 6 2354 1406 238 -603 -70 100 C ATOM 2150 CG2AILE C 6 11.534 21.740 31.351 0.83 10.03 C ANISOU 2150 CG2AILE C 6 2063 973 775 -522 344 281 C ATOM 2151 CG2BILE C 6 11.924 21.434 31.493 0.17 7.41 C ANISOU 2151 CG2BILE C 6 1910 701 205 40 353 -242 C ATOM 2152 CD1AILE C 6 13.156 23.552 33.262 0.83 12.26 C ANISOU 2152 CD1AILE C 6 3101 1395 163 -1007 253 -90 C ATOM 2153 CD1BILE C 6 14.748 22.834 32.073 0.17 13.63 C ANISOU 2153 CD1BILE C 6 1627 3550 0 -838 482 685 C ATOM 2154 N ARG C 7 11.746 21.087 28.058 1.00 8.40 N ANISOU 2154 N ARG C 7 1360 986 846 -174 -200 -250 N ATOM 2155 CA ARG C 7 10.757 20.894 27.024 1.00 7.59 C ANISOU 2155 CA ARG C 7 1008 1103 771 -268 13 -313 C ATOM 2156 C ARG C 7 9.390 20.556 27.632 1.00 8.91 C ANISOU 2156 C ARG C 7 1089 1026 1271 40 104 279 C ATOM 2157 O ARG C 7 9.343 19.883 28.672 1.00 10.35 O ANISOU 2157 O ARG C 7 1254 1481 1196 -167 114 307 O ATOM 2158 CB ARG C 7 11.178 19.761 26.072 1.00 9.87 C ANISOU 2158 CB ARG C 7 1941 977 834 -282 228 -342 C ATOM 2159 CG ARG C 7 12.126 20.153 24.965 1.00 10.50 C ANISOU 2159 CG ARG C 7 1731 1517 741 190 218 -117 C ATOM 2160 CD ARG C 7 11.651 21.225 23.936 1.00 11.57 C ANISOU 2160 CD ARG C 7 1407 1629 1361 -178 -2 294 C ATOM 2161 NE ARG C 7 10.215 20.976 23.737 1.00 13.41 N ANISOU 2161 NE ARG C 7 1509 2023 1562 -307 -207 41 N ATOM 2162 CZ ARG C 7 9.685 19.943 23.083 1.00 11.88 C ANISOU 2162 CZ ARG C 7 1316 1744 1455 -15 -73 27 C ATOM 2163 NH1 ARG C 7 10.504 19.048 22.501 1.00 13.40 N ANISOU 2163 NH1 ARG C 7 1954 2434 703 422 388 273 N ATOM 2164 NH2 ARG C 7 8.348 19.824 23.014 1.00 12.14 N ANISOU 2164 NH2 ARG C 7 1304 1385 1922 -232 -55 467 N ATOM 2165 N GLY C 8 8.327 21.038 26.986 1.00 9.79 N ANISOU 2165 N GLY C 8 973 864 1882 -157 -26 507 N ATOM 2166 CA GLY C 8 6.992 20.615 27.349 1.00 11.32 C ANISOU 2166 CA GLY C 8 1177 1799 1324 -560 -25 105 C ATOM 2167 C GLY C 8 6.127 20.621 26.099 1.00 9.16 C ANISOU 2167 C GLY C 8 1326 752 1401 -487 -140 235 C ATOM 2168 O GLY C 8 6.554 21.172 25.063 1.00 8.72 O ANISOU 2168 O GLY C 8 1132 689 1491 -118 177 268 O ATOM 2169 N ALA C 9 4.998 19.943 26.246 1.00 8.26 N ANISOU 2169 N ALA C 9 1014 881 1242 -230 149 68 N ATOM 2170 CA ALA C 9 3.976 20.045 25.215 1.00 10.61 C ANISOU 2170 CA ALA C 9 1029 1472 1530 -345 10 -78 C ATOM 2171 C ALA C 9 2.600 19.721 25.769 1.00 10.01 C ANISOU 2171 C ALA C 9 1012 851 1942 10 86 184 C ATOM 2172 O ALA C 9 2.507 19.007 26.764 1.00 12.80 O ANISOU 2172 O ALA C 9 1251 1504 2107 -163 45 583 O ATOM 2173 CB ALA C 9 4.254 19.120 24.025 1.00 10.83 C ANISOU 2173 CB ALA C 9 1333 1491 1289 -92 -90 45 C ATOM 2174 N THR C 10 1.577 20.240 25.108 1.00 11.00 N ANISOU 2174 N THR C 10 1009 1114 2056 -161 -182 169 N ATOM 2175 CA THR C 10 0.221 19.936 25.543 1.00 12.19 C ANISOU 2175 CA THR C 10 1057 1343 2233 -588 -356 -168 C ATOM 2176 C THR C 10 -0.643 20.124 24.302 1.00 10.53 C ANISOU 2176 C THR C 10 906 645 2451 -162 -221 552 C ATOM 2177 O THR C 10 -0.178 20.509 23.233 1.00 13.25 O ANISOU 2177 O THR C 10 1485 1202 2345 -401 -22 304 O ATOM 2178 CB THR C 10 -0.237 20.798 26.723 1.00 13.46 C ANISOU 2178 CB THR C 10 1525 1199 2392 -528 444 176 C ATOM 2179 OG1 THR C 10 -1.485 20.260 27.182 1.00 13.32 O ANISOU 2179 OG1 THR C 10 1140 959 2961 -525 17 -71 O ATOM 2180 CG2 THR C 10 -0.473 22.245 26.309 1.00 13.26 C ANISOU 2180 CG2 THR C 10 1377 1255 2404 -445 273 168 C ATOM 2181 N THR C 11 -1.918 19.768 24.460 1.00 11.55 N ANISOU 2181 N THR C 11 820 1271 2295 -202 -200 -50 N ATOM 2182 CA THR C 11 -2.847 19.974 23.362 1.00 10.52 C ANISOU 2182 CA THR C 11 984 577 2437 -70 -323 -105 C ATOM 2183 C THR C 11 -4.165 20.586 23.838 1.00 11.60 C ANISOU 2183 C THR C 11 1064 1027 2317 58 -271 -284 C ATOM 2184 O THR C 11 -4.445 20.505 25.039 1.00 15.05 O ANISOU 2184 O THR C 11 1311 1896 2510 -625 106 -104 O ATOM 2185 CB THR C 11 -3.186 18.673 22.619 1.00 10.75 C ANISOU 2185 CB THR C 11 1044 405 2636 -138 -253 -22 C ATOM 2186 OG1 THR C 11 -3.834 17.703 23.502 1.00 13.14 O ANISOU 2186 OG1 THR C 11 1244 680 3070 -311 44 102 O ATOM 2187 CG2 THR C 11 -1.965 18.021 22.007 1.00 12.03 C ANISOU 2187 CG2 THR C 11 1251 1264 2057 106 -215 -274 C ATOM 2188 N VAL C 12 -4.933 21.160 22.909 1.00 13.72 N ANISOU 2188 N VAL C 12 936 1062 3215 -23 -105 603 N ATOM 2189 CA VAL C 12 -6.249 21.673 23.232 1.00 14.88 C ANISOU 2189 CA VAL C 12 916 1145 3595 -24 -245 169 C ATOM 2190 C VAL C 12 -7.303 20.944 22.387 1.00 15.32 C ANISOU 2190 C VAL C 12 910 1531 3380 -346 131 -91 C ATOM 2191 O VAL C 12 -6.992 20.440 21.290 1.00 16.67 O ANISOU 2191 O VAL C 12 1215 1230 3886 -73 354 -393 O ATOM 2192 CB VAL C 12 -6.393 23.190 22.994 1.00 13.20 C ANISOU 2192 CB VAL C 12 1527 1096 2394 146 78 -123 C ATOM 2193 CG1 VAL C 12 -5.532 23.935 23.995 1.00 13.59 C ANISOU 2193 CG1 VAL C 12 1394 1552 2217 -445 464 -107 C ATOM 2194 CG2 VAL C 12 -6.050 23.598 21.570 1.00 13.90 C ANISOU 2194 CG2 VAL C 12 851 2000 2429 -116 -154 151 C ATOM 2195 N GLU C 13 -8.558 20.866 22.812 1.00 13.84 N ANISOU 2195 N GLU C 13 1006 979 3273 -417 208 268 N ATOM 2196 CA GLU C 13 -9.630 20.268 22.043 1.00 17.14 C ANISOU 2196 CA GLU C 13 1056 1352 4105 -622 -113 538 C ATOM 2197 C GLU C 13 -10.188 21.221 20.985 1.00 14.56 C ANISOU 2197 C GLU C 13 800 1072 3660 -130 23 -33 C ATOM 2198 O GLU C 13 -10.658 20.792 19.946 1.00 18.50 O ANISOU 2198 O GLU C 13 1375 1291 4364 -492 -759 -183 O ATOM 2199 CB AGLU C 13 -10.785 19.839 22.971 0.70 20.89 C ANISOU 2199 CB AGLU C 13 1397 2042 4498 -1124 67 654 C ATOM 2200 CB BGLU C 13 -10.770 19.844 22.986 0.30 20.28 C ANISOU 2200 CB BGLU C 13 1371 1867 4469 -1030 69 608 C ATOM 2201 CG AGLU C 13 -10.466 18.525 23.657 0.70 23.58 C ANISOU 2201 CG AGLU C 13 2207 2337 4414 -1040 181 950 C ATOM 2202 CG BGLU C 13 -10.223 18.930 24.082 0.30 21.48 C ANISOU 2202 CG BGLU C 13 1930 1785 4447 -1211 75 732 C ATOM 2203 CD AGLU C 13 -10.250 17.449 22.593 0.70 25.28 C ANISOU 2203 CD AGLU C 13 2588 2056 4963 -814 -453 724 C ATOM 2204 CD BGLU C 13 -9.901 17.578 23.449 0.30 24.33 C ANISOU 2204 CD BGLU C 13 2460 2164 4622 -474 -497 495 C ATOM 2205 OE1AGLU C 13 -11.226 17.160 21.869 0.70 28.76 O ANISOU 2205 OE1AGLU C 13 2538 3628 4761 -1148 -246 487 O ATOM 2206 OE1BGLU C 13 -10.777 16.696 23.533 0.30 23.71 O ANISOU 2206 OE1BGLU C 13 2131 734 6143 456 -587 1054 O ATOM 2207 OE2AGLU C 13 -9.126 16.940 22.484 0.70 28.97 O ANISOU 2207 OE2AGLU C 13 3083 2942 4983 9 -893 174 O ATOM 2208 OE2BGLU C 13 -8.807 17.450 22.870 0.30 26.81 O ANISOU 2208 OE2BGLU C 13 3186 2078 4924 -285 263 918 O ATOM 2209 N ARG C 14 -10.090 22.513 21.296 1.00 15.81 N ANISOU 2209 N ARG C 14 1131 1113 3763 -259 -209 -120 N ATOM 2210 CA ARG C 14 -10.602 23.582 20.469 1.00 15.32 C ANISOU 2210 CA ARG C 14 1756 980 3084 15 659 -114 C ATOM 2211 C ARG C 14 -9.553 24.691 20.332 1.00 14.71 C ANISOU 2211 C ARG C 14 1614 1126 2849 -31 426 -264 C ATOM 2212 O ARG C 14 -8.860 25.003 21.280 1.00 15.74 O ANISOU 2212 O ARG C 14 1785 1153 3043 320 46 -120 O ATOM 2213 CB AARG C 14 -11.869 24.236 21.040 0.64 15.42 C ANISOU 2213 CB AARG C 14 1386 1250 3221 38 165 -325 C ATOM 2214 CB BARG C 14 -11.879 24.194 21.024 0.35 14.53 C ANISOU 2214 CB BARG C 14 1314 1123 3084 -57 38 -509 C ATOM 2215 CG AARG C 14 -13.084 23.359 21.194 0.64 15.28 C ANISOU 2215 CG AARG C 14 1414 1373 3017 -35 143 -399 C ATOM 2216 CG BARG C 14 -12.947 23.228 21.522 0.35 13.93 C ANISOU 2216 CG BARG C 14 1098 1197 2996 115 -16 -294 C ATOM 2217 CD AARG C 14 -13.567 22.800 19.890 0.64 18.82 C ANISOU 2217 CD AARG C 14 1820 2275 3054 -334 -153 -322 C ATOM 2218 CD BARG C 14 -14.124 24.094 21.898 0.35 14.72 C ANISOU 2218 CD BARG C 14 1042 1967 2584 460 -349 -316 C ATOM 2219 NE AARG C 14 -13.950 23.727 18.833 0.64 20.87 N ANISOU 2219 NE AARG C 14 1227 3673 3028 846 433 56 N ATOM 2220 NE BARG C 14 -15.322 23.480 22.447 0.35 11.77 N ANISOU 2220 NE BARG C 14 1588 1252 1633 559 165 -711 N ATOM 2221 CZ AARG C 14 -15.131 24.292 18.703 0.64 26.09 C ANISOU 2221 CZ AARG C 14 1921 2987 5003 1538 946 -326 C ATOM 2222 CZ BARG C 14 -16.313 23.139 21.626 0.35 11.13 C ANISOU 2222 CZ BARG C 14 1343 1178 1707 104 371 -389 C ATOM 2223 NH1AARG C 14 -16.071 24.021 19.613 0.64 27.40 N ANISOU 2223 NH1AARG C 14 1004 4851 4557 135 421 -1949 N ATOM 2224 NH1BARG C 14 -16.118 23.383 20.334 0.35 8.63 N ANISOU 2224 NH1BARG C 14 1185 548 1547 -527 440 -979 N ATOM 2225 NH2AARG C 14 -15.395 25.116 17.704 0.64 29.64 N ANISOU 2225 NH2AARG C 14 2378 1962 6920 1475 -28 130 N ATOM 2226 NH2BARG C 14 -17.426 22.595 22.077 0.35 12.83 N ANISOU 2226 NH2BARG C 14 2232 534 2107 -364 263 736 N ATOM 2227 N ASP C 15 -9.500 25.276 19.129 1.00 14.07 N ANISOU 2227 N ASP C 15 995 1278 3073 -131 207 14 N ATOM 2228 CA ASP C 15 -8.705 26.493 18.959 1.00 13.56 C ANISOU 2228 CA ASP C 15 1176 1183 2794 -193 -152 -113 C ATOM 2229 C ASP C 15 -9.426 27.706 19.546 1.00 15.40 C ANISOU 2229 C ASP C 15 1657 1291 2905 134 -234 -25 C ATOM 2230 O ASP C 15 -9.898 28.576 18.802 1.00 16.78 O ANISOU 2230 O ASP C 15 1950 1218 3208 20 -490 70 O ATOM 2231 CB ASP C 15 -8.433 26.662 17.471 1.00 14.46 C ANISOU 2231 CB ASP C 15 938 1636 2920 -92 36 178 C ATOM 2232 CG ASP C 15 -7.650 27.905 17.126 1.00 13.92 C ANISOU 2232 CG ASP C 15 1465 1264 2561 -129 -231 -64 C ATOM 2233 OD1 ASP C 15 -6.863 28.301 18.003 1.00 14.26 O ANISOU 2233 OD1 ASP C 15 1666 1149 2605 138 -321 -366 O ATOM 2234 OD2 ASP C 15 -7.801 28.450 15.994 1.00 16.85 O ANISOU 2234 OD2 ASP C 15 2220 1691 2493 -454 -324 21 O ATOM 2235 N THR C 16 -9.533 27.778 20.889 1.00 12.95 N ANISOU 2235 N THR C 16 808 1172 2941 -299 79 -38 N ATOM 2236 CA THR C 16 -10.092 28.999 21.469 1.00 14.48 C ANISOU 2236 CA THR C 16 1023 1218 3261 -271 148 -181 C ATOM 2237 C THR C 16 -9.039 29.579 22.389 1.00 13.20 C ANISOU 2237 C THR C 16 835 1128 3051 -396 356 -27 C ATOM 2238 O THR C 16 -8.168 28.862 22.884 1.00 13.64 O ANISOU 2238 O THR C 16 950 1448 2786 -60 375 -346 O ATOM 2239 CB THR C 16 -11.372 28.755 22.294 1.00 15.18 C ANISOU 2239 CB THR C 16 795 1206 3765 -318 165 -311 C ATOM 2240 OG1 THR C 16 -11.064 27.823 23.345 1.00 17.93 O ANISOU 2240 OG1 THR C 16 1912 2322 2579 -354 375 -407 O ATOM 2241 CG2 THR C 16 -12.455 28.146 21.431 1.00 15.52 C ANISOU 2241 CG2 THR C 16 1030 1102 3765 -300 -55 -118 C ATOM 2242 N GLU C 17 -9.113 30.883 22.651 1.00 14.40 N ANISOU 2242 N GLU C 17 1449 1479 2543 23 122 -530 N ATOM 2243 CA GLU C 17 -8.220 31.515 23.594 1.00 12.89 C ANISOU 2243 CA GLU C 17 1161 1308 2428 4 172 -269 C ATOM 2244 C GLU C 17 -8.321 30.881 24.971 1.00 11.59 C ANISOU 2244 C GLU C 17 1025 842 2536 -279 134 -345 C ATOM 2245 O GLU C 17 -7.332 30.607 25.670 1.00 14.37 O ANISOU 2245 O GLU C 17 1232 1714 2512 -145 -1 -161 O ATOM 2246 CB GLU C 17 -8.611 33.000 23.687 1.00 14.17 C ANISOU 2246 CB GLU C 17 2236 1359 1790 355 -185 -298 C ATOM 2247 CG GLU C 17 -7.691 33.672 24.697 1.00 15.02 C ANISOU 2247 CG GLU C 17 1674 1530 2505 195 -108 -499 C ATOM 2248 CD GLU C 17 -7.886 35.160 24.771 1.00 18.19 C ANISOU 2248 CD GLU C 17 2060 1611 3241 507 -512 -832 C ATOM 2249 OE1 GLU C 17 -9.029 35.639 24.566 1.00 33.72 O ANISOU 2249 OE1 GLU C 17 2548 2463 7802 1145 -1281 -938 O ATOM 2250 OE2 GLU C 17 -6.932 35.877 25.110 1.00 22.07 O ANISOU 2250 OE2 GLU C 17 2634 1619 4132 -19 -516 -552 O ATOM 2251 N GLU C 18 -9.565 30.586 25.366 1.00 14.24 N ANISOU 2251 N GLU C 18 1174 1317 2920 -528 239 -318 N ATOM 2252 CA GLU C 18 -9.768 30.085 26.729 1.00 16.04 C ANISOU 2252 CA GLU C 18 1289 1765 3041 142 727 -122 C ATOM 2253 C GLU C 18 -9.045 28.756 26.912 1.00 17.39 C ANISOU 2253 C GLU C 18 1908 1627 3071 69 76 -290 C ATOM 2254 O GLU C 18 -8.373 28.552 27.916 1.00 17.71 O ANISOU 2254 O GLU C 18 1349 1800 3581 -234 -217 -264 O ATOM 2255 CB GLU C 18 -11.269 29.978 27.008 1.00 18.99 C ANISOU 2255 CB GLU C 18 1205 3085 2926 -135 267 468 C ATOM 2256 CG GLU C 18 -11.647 29.747 28.459 1.00 29.94 C ANISOU 2256 CG GLU C 18 1808 6412 3157 -737 787 677 C ATOM 2257 CD GLU C 18 -13.076 30.132 28.798 1.00 36.22 C ANISOU 2257 CD GLU C 18 1730 8682 3350 -446 847 1184 C ATOM 2258 OE1 GLU C 18 -13.929 30.358 27.913 1.00 55.14 O ANISOU 2258 OE1 GLU C 18 3054 13029 4867 1613 -430 343 O ATOM 2259 OE2 GLU C 18 -13.428 30.240 30.001 1.00 48.70 O ANISOU 2259 OE2 GLU C 18 2999 11526 3980 338 928 -1977 O ATOM 2260 N GLU C 19 -9.187 27.830 25.944 1.00 15.68 N ANISOU 2260 N GLU C 19 1086 1630 3240 -333 486 -413 N ATOM 2261 CA GLU C 19 -8.523 26.541 26.130 1.00 15.61 C ANISOU 2261 CA GLU C 19 1412 1631 2889 -200 691 -185 C ATOM 2262 C GLU C 19 -7.022 26.601 25.964 1.00 16.38 C ANISOU 2262 C GLU C 19 1365 1441 3416 -246 386 547 C ATOM 2263 O GLU C 19 -6.312 25.892 26.691 1.00 14.69 O ANISOU 2263 O GLU C 19 1707 1104 2769 -85 282 9 O ATOM 2264 CB GLU C 19 -9.119 25.544 25.111 1.00 18.19 C ANISOU 2264 CB GLU C 19 1941 1406 3566 -452 285 -132 C ATOM 2265 CG GLU C 19 -10.589 25.260 25.444 1.00 20.33 C ANISOU 2265 CG GLU C 19 1431 2109 4185 148 -96 -784 C ATOM 2266 CD GLU C 19 -11.112 23.982 24.839 1.00 18.87 C ANISOU 2266 CD GLU C 19 1139 2448 3584 -112 -329 -624 C ATOM 2267 OE1 GLU C 19 -10.303 23.222 24.247 1.00 18.67 O ANISOU 2267 OE1 GLU C 19 1528 1430 4135 -243 66 -300 O ATOM 2268 OE2 GLU C 19 -12.358 23.756 24.941 1.00 25.79 O ANISOU 2268 OE2 GLU C 19 1281 2596 5923 -270 153 -243 O ATOM 2269 N ILE C 20 -6.579 27.430 24.993 1.00 11.64 N ANISOU 2269 N ILE C 20 1015 1079 2329 -95 254 -201 N ATOM 2270 CA ILE C 20 -5.127 27.578 24.816 1.00 14.74 C ANISOU 2270 CA ILE C 20 1103 2594 1905 -426 370 -340 C ATOM 2271 C ILE C 20 -4.516 28.164 26.072 1.00 12.38 C ANISOU 2271 C ILE C 20 1116 1407 2180 -71 107 -142 C ATOM 2272 O ILE C 20 -3.467 27.631 26.470 1.00 13.48 O ANISOU 2272 O ILE C 20 1116 1320 2685 -156 -44 103 O ATOM 2273 CB ILE C 20 -4.789 28.401 23.550 1.00 13.85 C ANISOU 2273 CB ILE C 20 1062 2099 2102 -348 241 -283 C ATOM 2274 CG1 ILE C 20 -5.209 27.653 22.276 1.00 12.01 C ANISOU 2274 CG1 ILE C 20 994 1597 1972 254 -210 -53 C ATOM 2275 CG2 ILE C 20 -3.328 28.811 23.505 1.00 11.46 C ANISOU 2275 CG2 ILE C 20 939 1594 1821 -64 11 152 C ATOM 2276 CD1 ILE C 20 -5.217 28.456 20.992 1.00 15.08 C ANISOU 2276 CD1 ILE C 20 1323 2261 2145 -438 134 259 C ATOM 2277 N LEU C 21 -5.127 29.161 26.691 1.00 14.54 N ANISOU 2277 N LEU C 21 1530 1271 2722 -40 159 -330 N ATOM 2278 CA LEU C 21 -4.517 29.744 27.907 1.00 14.33 C ANISOU 2278 CA LEU C 21 1954 923 2567 -42 114 -134 C ATOM 2279 C LEU C 21 -4.615 28.728 29.040 1.00 14.82 C ANISOU 2279 C LEU C 21 1722 931 2978 -102 -110 110 C ATOM 2280 O LEU C 21 -3.638 28.520 29.776 1.00 14.14 O ANISOU 2280 O LEU C 21 1643 1386 2344 218 191 -274 O ATOM 2281 CB LEU C 21 -5.160 31.068 28.338 1.00 13.08 C ANISOU 2281 CB LEU C 21 1702 1194 2073 452 -143 39 C ATOM 2282 CG LEU C 21 -5.087 32.210 27.337 1.00 13.78 C ANISOU 2282 CG LEU C 21 1648 1274 2311 272 512 161 C ATOM 2283 CD1 LEU C 21 -5.750 33.473 27.850 1.00 17.42 C ANISOU 2283 CD1 LEU C 21 2575 1033 3010 526 -457 -113 C ATOM 2284 CD2 LEU C 21 -3.624 32.499 26.983 1.00 17.85 C ANISOU 2284 CD2 LEU C 21 1462 1674 3648 -609 -303 -147 C ATOM 2285 N GLN C 22 -5.802 28.108 29.117 1.00 15.07 N ANISOU 2285 N GLN C 22 1507 1014 3203 5 410 -126 N ATOM 2286 CA GLN C 22 -5.928 27.115 30.204 1.00 15.46 C ANISOU 2286 CA GLN C 22 1430 1742 2701 -124 442 -109 C ATOM 2287 C GLN C 22 -4.884 26.017 30.134 1.00 14.82 C ANISOU 2287 C GLN C 22 1999 1204 2429 -129 354 123 C ATOM 2288 O GLN C 22 -4.207 25.672 31.108 1.00 16.35 O ANISOU 2288 O GLN C 22 2247 1936 2028 508 614 -140 O ATOM 2289 CB GLN C 22 -7.315 26.477 30.176 1.00 17.93 C ANISOU 2289 CB GLN C 22 1796 1787 3231 -582 781 -496 C ATOM 2290 CG GLN C 22 -7.436 25.336 31.171 1.00 22.54 C ANISOU 2290 CG GLN C 22 2021 2165 4378 -382 935 216 C ATOM 2291 CD GLN C 22 -8.675 24.522 30.885 1.00 30.15 C ANISOU 2291 CD GLN C 22 3330 3149 4977 -1779 1270 85 C ATOM 2292 OE1 GLN C 22 -8.978 24.032 29.790 1.00 41.93 O ANISOU 2292 OE1 GLN C 22 4109 4991 6831 -2281 1752 -2622 O ATOM 2293 NE2 GLN C 22 -9.416 24.380 31.987 1.00 44.91 N ANISOU 2293 NE2 GLN C 22 3174 7772 6118 -2328 2064 -35 N ATOM 2294 N LYS C 23 -4.690 25.425 28.950 1.00 12.07 N ANISOU 2294 N LYS C 23 1266 903 2416 -304 -123 32 N ATOM 2295 CA LYS C 23 -3.787 24.282 28.869 1.00 12.40 C ANISOU 2295 CA LYS C 23 1556 1207 1949 -65 86 275 C ATOM 2296 C LYS C 23 -2.333 24.741 28.887 1.00 12.40 C ANISOU 2296 C LYS C 23 1450 1059 2203 85 270 -77 C ATOM 2297 O LYS C 23 -1.451 24.049 29.436 1.00 12.68 O ANISOU 2297 O LYS C 23 1714 1591 1512 208 16 -185 O ATOM 2298 CB LYS C 23 -4.132 23.444 27.645 1.00 13.76 C ANISOU 2298 CB LYS C 23 1712 1247 2268 -503 539 -70 C ATOM 2299 CG LYS C 23 -5.534 22.817 27.675 1.00 14.92 C ANISOU 2299 CG LYS C 23 1759 1452 2457 -599 731 -223 C ATOM 2300 CD LYS C 23 -5.739 22.175 29.030 1.00 20.34 C ANISOU 2300 CD LYS C 23 3213 1582 2931 -843 1390 82 C ATOM 2301 CE LYS C 23 -6.985 21.349 29.195 1.00 21.85 C ANISOU 2301 CE LYS C 23 2271 2135 3896 -204 1500 664 C ATOM 2302 NZ LYS C 23 -6.996 20.708 30.542 1.00 29.77 N ANISOU 2302 NZ LYS C 23 5025 1951 4337 -73 2840 1034 N ATOM 2303 N THR C 24 -2.000 25.916 28.324 1.00 12.01 N ANISOU 2303 N THR C 24 1456 1154 1953 -29 426 -165 N ATOM 2304 CA THR C 24 -0.618 26.387 28.406 1.00 11.65 C ANISOU 2304 CA THR C 24 1434 1492 1500 -21 443 -15 C ATOM 2305 C THR C 24 -0.255 26.698 29.852 1.00 10.20 C ANISOU 2305 C THR C 24 1342 1246 1289 -269 653 350 C ATOM 2306 O THR C 24 0.846 26.383 30.274 1.00 12.68 O ANISOU 2306 O THR C 24 1444 1515 1860 -200 236 -256 O ATOM 2307 CB THR C 24 -0.410 27.611 27.517 1.00 12.90 C ANISOU 2307 CB THR C 24 1237 2404 1260 -197 435 487 C ATOM 2308 OG1 THR C 24 -0.753 27.252 26.151 1.00 12.22 O ANISOU 2308 OG1 THR C 24 1189 1900 1554 302 218 78 O ATOM 2309 CG2 THR C 24 1.026 28.104 27.539 1.00 11.10 C ANISOU 2309 CG2 THR C 24 1157 1583 1476 93 242 275 C ATOM 2310 N LYS C 25 -1.162 27.330 30.582 1.00 12.49 N ANISOU 2310 N LYS C 25 1537 1706 1504 -48 415 -125 N ATOM 2311 CA LYS C 25 -0.892 27.679 31.987 1.00 12.12 C ANISOU 2311 CA LYS C 25 1761 1143 1701 630 -2 -300 C ATOM 2312 C LYS C 25 -0.672 26.400 32.787 1.00 12.01 C ANISOU 2312 C LYS C 25 1798 1094 1672 365 180 -253 C ATOM 2313 O LYS C 25 0.215 26.345 33.648 1.00 14.17 O ANISOU 2313 O LYS C 25 1941 1806 1636 265 95 205 O ATOM 2314 CB LYS C 25 -2.035 28.499 32.597 1.00 12.82 C ANISOU 2314 CB LYS C 25 1810 1088 1973 359 643 -23 C ATOM 2315 CG LYS C 25 -1.848 28.768 34.092 1.00 17.74 C ANISOU 2315 CG LYS C 25 1624 2936 2182 148 660 -774 C ATOM 2316 CD LYS C 25 -2.970 29.665 34.631 1.00 18.24 C ANISOU 2316 CD LYS C 25 2213 2707 2011 454 878 -363 C ATOM 2317 CE LYS C 25 -2.712 30.078 36.059 1.00 18.82 C ANISOU 2317 CE LYS C 25 2115 2809 2225 303 795 -653 C ATOM 2318 NZ LYS C 25 -3.801 30.913 36.626 1.00 19.18 N ANISOU 2318 NZ LYS C 25 2959 2240 2090 488 1432 26 N ATOM 2319 N GLN C 26 -1.508 25.391 32.545 1.00 13.82 N ANISOU 2319 N GLN C 26 1832 1569 1849 -78 655 -175 N ATOM 2320 CA GLN C 26 -1.381 24.094 33.238 1.00 14.16 C ANISOU 2320 CA GLN C 26 1881 1538 1960 -178 1017 -157 C ATOM 2321 C GLN C 26 -0.027 23.470 32.978 1.00 12.52 C ANISOU 2321 C GLN C 26 1798 1366 1591 -193 809 -36 C ATOM 2322 O GLN C 26 0.663 22.940 33.845 1.00 17.47 O ANISOU 2322 O GLN C 26 2313 2460 1865 57 751 580 O ATOM 2323 CB AGLN C 26 -2.499 23.148 32.761 0.56 15.60 C ANISOU 2323 CB AGLN C 26 1782 1864 2282 -338 887 93 C ATOM 2324 CB BGLN C 26 -2.554 23.165 32.880 0.44 14.67 C ANISOU 2324 CB BGLN C 26 1757 1690 2128 -115 589 235 C ATOM 2325 CG AGLN C 26 -2.459 21.758 33.327 0.56 14.75 C ANISOU 2325 CG AGLN C 26 1991 1709 1906 -466 96 -248 C ATOM 2326 CG BGLN C 26 -3.822 23.658 33.581 0.44 15.14 C ANISOU 2326 CG BGLN C 26 1661 2254 1839 -260 321 -462 C ATOM 2327 CD AGLN C 26 -3.458 20.752 32.787 0.56 15.24 C ANISOU 2327 CD AGLN C 26 1811 2093 1886 -636 519 -539 C ATOM 2328 CD BGLN C 26 -5.107 23.102 33.009 0.44 19.03 C ANISOU 2328 CD BGLN C 26 1668 2751 2811 -37 -115 -608 C ATOM 2329 OE1AGLN C 26 -3.470 20.300 31.638 0.56 13.28 O ANISOU 2329 OE1AGLN C 26 1814 2318 914 -1125 -160 650 O ATOM 2330 OE1BGLN C 26 -5.088 22.250 32.122 0.44 20.72 O ANISOU 2330 OE1BGLN C 26 2068 3969 1837 -1248 418 -685 O ATOM 2331 NE2AGLN C 26 -4.351 20.359 33.703 0.56 24.01 N ANISOU 2331 NE2AGLN C 26 4056 3388 1677 -2384 1101 -1058 N ATOM 2332 NE2BGLN C 26 -6.216 23.625 33.540 0.44 24.63 N ANISOU 2332 NE2BGLN C 26 1635 3694 4028 201 193 -499 N ATOM 2333 N LEU C 27 0.402 23.589 31.722 1.00 13.49 N ANISOU 2333 N LEU C 27 1780 1812 1531 379 701 -98 N ATOM 2334 CA LEU C 27 1.689 23.030 31.315 1.00 10.50 C ANISOU 2334 CA LEU C 27 1343 1353 1295 -119 549 -4 C ATOM 2335 C LEU C 27 2.821 23.772 32.011 1.00 10.21 C ANISOU 2335 C LEU C 27 1951 951 978 -140 294 240 C ATOM 2336 O LEU C 27 3.692 23.098 32.593 1.00 12.31 O ANISOU 2336 O LEU C 27 1925 1611 1140 184 130 133 O ATOM 2337 CB LEU C 27 1.848 23.089 29.797 1.00 10.76 C ANISOU 2337 CB LEU C 27 1273 1573 1243 105 383 -203 C ATOM 2338 CG LEU C 27 3.244 22.682 29.282 1.00 8.91 C ANISOU 2338 CG LEU C 27 1449 847 1090 319 262 -492 C ATOM 2339 CD1 LEU C 27 3.558 21.235 29.651 1.00 12.78 C ANISOU 2339 CD1 LEU C 27 1718 1134 2005 201 102 252 C ATOM 2340 CD2 LEU C 27 3.277 22.842 27.786 1.00 11.39 C ANISOU 2340 CD2 LEU C 27 1539 1605 1182 134 503 68 C ATOM 2341 N LEU C 28 2.781 25.092 31.946 1.00 11.37 N ANISOU 2341 N LEU C 28 2170 927 1224 49 419 -223 N ATOM 2342 CA LEU C 28 3.776 25.899 32.667 1.00 12.10 C ANISOU 2342 CA LEU C 28 2409 1110 1079 -178 461 -166 C ATOM 2343 C LEU C 28 3.821 25.581 34.153 1.00 11.83 C ANISOU 2343 C LEU C 28 1943 1470 1081 339 434 -136 C ATOM 2344 O LEU C 28 4.921 25.400 34.685 1.00 13.17 O ANISOU 2344 O LEU C 28 1859 1430 1715 -9 188 -35 O ATOM 2345 CB ALEU C 28 3.458 27.387 32.511 0.60 12.75 C ANISOU 2345 CB ALEU C 28 2010 1081 1755 -458 -66 49 C ATOM 2346 CB BLEU C 28 3.395 27.365 32.484 0.40 12.95 C ANISOU 2346 CB BLEU C 28 2165 1052 1703 -469 204 79 C ATOM 2347 CG ALEU C 28 3.408 27.817 31.042 0.60 16.07 C ANISOU 2347 CG ALEU C 28 2256 1868 1982 -132 231 595 C ATOM 2348 CG BLEU C 28 4.278 28.491 32.989 0.40 15.79 C ANISOU 2348 CG BLEU C 28 2441 1311 2248 -330 419 -924 C ATOM 2349 CD1ALEU C 28 2.821 29.220 30.922 0.60 19.62 C ANISOU 2349 CD1ALEU C 28 2158 2039 3259 -121 -1319 707 C ATOM 2350 CD1BLEU C 28 5.717 28.297 32.533 0.40 19.74 C ANISOU 2350 CD1BLEU C 28 2922 1710 2868 -1615 1890 -462 C ATOM 2351 CD2ALEU C 28 4.807 27.733 30.455 0.60 18.27 C ANISOU 2351 CD2ALEU C 28 2459 1872 2609 -811 677 17 C ATOM 2352 CD2BLEU C 28 3.747 29.835 32.490 0.40 18.59 C ANISOU 2352 CD2BLEU C 28 4594 1121 1350 -803 853 -208 C ATOM 2353 N GLU C 29 2.636 25.528 34.786 1.00 12.62 N ANISOU 2353 N GLU C 29 1927 1534 1335 -525 476 -107 N ATOM 2354 CA GLU C 29 2.673 25.269 36.230 1.00 13.01 C ANISOU 2354 CA GLU C 29 1860 1824 1259 -81 536 -198 C ATOM 2355 C GLU C 29 3.304 23.919 36.546 1.00 13.82 C ANISOU 2355 C GLU C 29 1856 1717 1678 -217 205 -108 C ATOM 2356 O GLU C 29 4.026 23.765 37.547 1.00 15.27 O ANISOU 2356 O GLU C 29 2603 2093 1108 -111 424 141 O ATOM 2357 CB GLU C 29 1.246 25.382 36.793 1.00 15.36 C ANISOU 2357 CB GLU C 29 1919 2211 1705 13 738 202 C ATOM 2358 CG GLU C 29 0.693 26.805 36.671 1.00 24.72 C ANISOU 2358 CG GLU C 29 2660 2950 3783 1102 3 171 C ATOM 2359 CD GLU C 29 -0.678 26.802 37.333 1.00 33.90 C ANISOU 2359 CD GLU C 29 3577 3975 5330 1839 1286 302 C ATOM 2360 OE1 GLU C 29 -1.258 25.693 37.423 1.00 46.16 O ANISOU 2360 OE1 GLU C 29 3672 4896 8969 1068 3022 226 O ATOM 2361 OE2 GLU C 29 -1.134 27.879 37.757 1.00 38.81 O ANISOU 2361 OE2 GLU C 29 5817 5009 3920 2751 1291 -292 O ATOM 2362 N LYS C 30 3.037 22.907 35.722 1.00 13.72 N ANISOU 2362 N LYS C 30 2080 1778 1356 -269 774 -154 N ATOM 2363 CA LYS C 30 3.591 21.595 35.978 1.00 15.78 C ANISOU 2363 CA LYS C 30 2235 1723 2037 -324 545 -205 C ATOM 2364 C LYS C 30 5.095 21.576 35.749 1.00 16.50 C ANISOU 2364 C LYS C 30 2100 1939 2231 -286 218 838 C ATOM 2365 O LYS C 30 5.825 20.921 36.503 1.00 15.69 O ANISOU 2365 O LYS C 30 2646 1606 1710 -12 347 544 O ATOM 2366 CB LYS C 30 2.887 20.578 35.057 1.00 16.06 C ANISOU 2366 CB LYS C 30 2662 1493 1947 -654 268 295 C ATOM 2367 CG LYS C 30 3.236 19.135 35.371 1.00 17.75 C ANISOU 2367 CG LYS C 30 3354 1507 1885 -492 514 399 C ATOM 2368 CD LYS C 30 2.795 18.762 36.787 1.00 25.66 C ANISOU 2368 CD LYS C 30 5225 2079 2444 -1286 1228 747 C ATOM 2369 CE LYS C 30 3.039 17.283 37.049 1.00 33.16 C ANISOU 2369 CE LYS C 30 6487 2328 3783 -1233 1350 1546 C ATOM 2370 NZ LYS C 30 2.480 16.863 38.359 1.00 48.58 N ANISOU 2370 NZ LYS C 30 10297 4970 3191 -2575 356 2774 N ATOM 2371 N ILE C 31 5.565 22.263 34.692 1.00 13.94 N ANISOU 2371 N ILE C 31 1963 1711 1622 -310 7 445 N ATOM 2372 CA ILE C 31 7.020 22.367 34.490 1.00 11.98 C ANISOU 2372 CA ILE C 31 2006 1733 813 -64 213 -251 C ATOM 2373 C ILE C 31 7.659 23.035 35.708 1.00 11.88 C ANISOU 2373 C ILE C 31 2502 909 1105 -100 -288 110 C ATOM 2374 O ILE C 31 8.669 22.618 36.241 1.00 14.77 O ANISOU 2374 O ILE C 31 2167 2163 1283 -172 -192 198 O ATOM 2375 CB ILE C 31 7.363 23.139 33.205 1.00 11.61 C ANISOU 2375 CB ILE C 31 1538 1923 950 437 153 69 C ATOM 2376 CG1 ILE C 31 6.986 22.351 31.948 1.00 11.56 C ANISOU 2376 CG1 ILE C 31 1925 1671 798 241 509 154 C ATOM 2377 CG2 ILE C 31 8.824 23.567 33.160 1.00 14.42 C ANISOU 2377 CG2 ILE C 31 1595 2794 1090 207 538 -165 C ATOM 2378 CD1 ILE C 31 7.070 23.196 30.687 1.00 16.34 C ANISOU 2378 CD1 ILE C 31 2890 2476 842 -773 322 439 C ATOM 2379 N ILE C 32 7.030 24.142 36.149 1.00 14.52 N ANISOU 2379 N ILE C 32 2776 1483 1256 -118 452 -424 N ATOM 2380 CA ILE C 32 7.575 24.874 37.286 1.00 13.06 C ANISOU 2380 CA ILE C 32 2496 1241 1227 5 133 -100 C ATOM 2381 C ILE C 32 7.589 23.979 38.516 1.00 15.64 C ANISOU 2381 C ILE C 32 2600 1767 1574 58 31 297 C ATOM 2382 O ILE C 32 8.566 23.966 39.274 1.00 17.57 O ANISOU 2382 O ILE C 32 3156 2237 1285 434 -225 -248 O ATOM 2383 CB ILE C 32 6.749 26.149 37.519 1.00 12.89 C ANISOU 2383 CB ILE C 32 2327 1375 1195 40 -152 -348 C ATOM 2384 CG1 ILE C 32 6.878 27.167 36.376 1.00 13.64 C ANISOU 2384 CG1 ILE C 32 1740 1654 1789 539 250 111 C ATOM 2385 CG2 ILE C 32 7.109 26.761 38.852 1.00 17.31 C ANISOU 2385 CG2 ILE C 32 3100 1957 1521 32 -298 -802 C ATOM 2386 CD1 ILE C 32 5.809 28.240 36.399 1.00 19.30 C ANISOU 2386 CD1 ILE C 32 2321 1733 3277 885 -242 -248 C ATOM 2387 N GLU C 33 6.495 23.213 38.738 1.00 16.68 N ANISOU 2387 N GLU C 33 3046 1693 1600 -63 684 192 N ATOM 2388 CA GLU C 33 6.523 22.475 40.003 1.00 17.80 C ANISOU 2388 CA GLU C 33 3239 2401 1123 507 1198 26 C ATOM 2389 C GLU C 33 7.509 21.327 39.876 1.00 17.93 C ANISOU 2389 C GLU C 33 3265 2741 808 795 273 -64 C ATOM 2390 O GLU C 33 8.197 21.044 40.874 1.00 23.39 O ANISOU 2390 O GLU C 33 3243 4543 1100 340 78 691 O ATOM 2391 CB GLU C 33 5.116 22.041 40.343 1.00 21.55 C ANISOU 2391 CB GLU C 33 3352 3274 1560 452 1380 481 C ATOM 2392 CG GLU C 33 4.539 20.865 39.591 1.00 33.19 C ANISOU 2392 CG GLU C 33 4489 3896 4225 -1025 1567 -56 C ATOM 2393 CD GLU C 33 4.786 19.573 40.367 1.00 33.42 C ANISOU 2393 CD GLU C 33 5285 4044 3368 -2451 81 18 C ATOM 2394 OE1 GLU C 33 5.370 19.712 41.462 1.00 44.53 O ANISOU 2394 OE1 GLU C 33 4275 9232 3413 -2588 95 479 O ATOM 2395 OE2 GLU C 33 4.458 18.466 39.909 1.00 53.26 O ANISOU 2395 OE2 GLU C 33 9566 3616 7054 -1797 52 -1132 O ATOM 2396 N GLU C 34 7.613 20.610 38.755 1.00 15.30 N ANISOU 2396 N GLU C 34 2762 1829 1223 186 707 -59 N ATOM 2397 CA GLU C 34 8.567 19.494 38.714 1.00 15.48 C ANISOU 2397 CA GLU C 34 2782 1235 1866 -171 580 144 C ATOM 2398 C GLU C 34 10.034 19.917 38.742 1.00 14.87 C ANISOU 2398 C GLU C 34 2704 994 1952 15 626 -400 C ATOM 2399 O GLU C 34 10.924 19.183 39.181 1.00 19.71 O ANISOU 2399 O GLU C 34 2838 2475 2177 393 842 555 O ATOM 2400 CB GLU C 34 8.335 18.707 37.416 1.00 16.81 C ANISOU 2400 CB GLU C 34 2131 1838 2416 -65 718 -519 C ATOM 2401 CG GLU C 34 6.948 18.073 37.443 1.00 19.22 C ANISOU 2401 CG GLU C 34 2082 2506 2714 -221 442 -171 C ATOM 2402 CD GLU C 34 6.796 17.011 36.389 1.00 22.05 C ANISOU 2402 CD GLU C 34 2033 2945 3400 -519 429 -687 C ATOM 2403 OE1 GLU C 34 5.659 16.588 36.139 1.00 34.03 O ANISOU 2403 OE1 GLU C 34 2488 4192 6250 -1284 331 -1635 O ATOM 2404 OE2 GLU C 34 7.795 16.593 35.786 1.00 22.07 O ANISOU 2404 OE2 GLU C 34 2677 3419 2291 -132 621 -272 O ATOM 2405 N ASN C 35 10.336 21.126 38.259 1.00 15.88 N ANISOU 2405 N ASN C 35 2864 1406 1763 -396 573 -255 N ATOM 2406 CA ASN C 35 11.718 21.594 38.165 1.00 14.42 C ANISOU 2406 CA ASN C 35 2644 1890 945 -238 394 191 C ATOM 2407 C ASN C 35 12.086 22.679 39.171 1.00 16.22 C ANISOU 2407 C ASN C 35 2571 2668 922 -469 166 -22 C ATOM 2408 O ASN C 35 13.188 23.211 39.169 1.00 16.50 O ANISOU 2408 O ASN C 35 2424 2412 1433 -210 -162 175 O ATOM 2409 CB ASN C 35 11.942 22.059 36.710 1.00 13.62 C ANISOU 2409 CB ASN C 35 2756 1570 846 -241 -125 290 C ATOM 2410 CG ASN C 35 11.922 20.889 35.747 1.00 12.10 C ANISOU 2410 CG ASN C 35 2030 1686 881 -17 -93 216 C ATOM 2411 OD1 ASN C 35 12.906 20.135 35.634 1.00 14.64 O ANISOU 2411 OD1 ASN C 35 2145 2078 1339 274 -213 301 O ATOM 2412 ND2 ASN C 35 10.820 20.696 35.024 1.00 13.68 N ANISOU 2412 ND2 ASN C 35 1813 2188 1196 66 10 -223 N ATOM 2413 N HIS C 36 11.171 23.051 40.062 1.00 14.75 N ANISOU 2413 N HIS C 36 2691 2071 844 170 41 183 N ATOM 2414 CA HIS C 36 11.324 24.078 41.064 1.00 16.82 C ANISOU 2414 CA HIS C 36 3118 2521 751 -380 -103 70 C ATOM 2415 C HIS C 36 11.778 25.383 40.409 1.00 18.41 C ANISOU 2415 C HIS C 36 3449 2371 1176 -455 -293 164 C ATOM 2416 O HIS C 36 12.661 26.102 40.922 1.00 17.67 O ANISOU 2416 O HIS C 36 3235 2593 887 -437 -231 232 O ATOM 2417 CB HIS C 36 12.310 23.612 42.126 1.00 20.98 C ANISOU 2417 CB HIS C 36 3834 2763 1374 -375 -694 331 C ATOM 2418 CG HIS C 36 11.891 22.345 42.804 1.00 25.87 C ANISOU 2418 CG HIS C 36 4816 2900 2113 -222 -439 834 C ATOM 2419 ND1 HIS C 36 11.963 21.103 42.217 1.00 31.24 N ANISOU 2419 ND1 HIS C 36 5580 2786 3503 -216 421 679 N ATOM 2420 CD2 HIS C 36 11.388 22.120 44.044 1.00 30.00 C ANISOU 2420 CD2 HIS C 36 5095 3690 2615 -794 162 901 C ATOM 2421 CE1 HIS C 36 11.530 20.161 43.051 1.00 31.40 C ANISOU 2421 CE1 HIS C 36 5048 3055 3828 -548 -577 1207 C ATOM 2422 NE2 HIS C 36 11.165 20.757 44.182 1.00 33.38 N ANISOU 2422 NE2 HIS C 36 5036 3839 3807 -879 274 1456 N ATOM 2423 N THR C 37 11.221 25.708 39.254 1.00 17.22 N ANISOU 2423 N THR C 37 3209 1776 1557 -336 -539 171 N ATOM 2424 CA THR C 37 11.692 26.898 38.517 1.00 17.82 C ANISOU 2424 CA THR C 37 4133 1545 1094 -287 -215 -206 C ATOM 2425 C THR C 37 11.198 28.234 39.062 1.00 14.97 C ANISOU 2425 C THR C 37 2949 1704 1035 -472 758 101 C ATOM 2426 O THR C 37 9.998 28.448 39.265 1.00 20.26 O ANISOU 2426 O THR C 37 2703 3463 1533 -153 67 114 O ATOM 2427 CB THR C 37 11.258 26.775 37.030 1.00 15.17 C ANISOU 2427 CB THR C 37 3107 1289 1367 -315 -535 -58 C ATOM 2428 OG1 THR C 37 11.558 25.431 36.587 1.00 15.66 O ANISOU 2428 OG1 THR C 37 2606 1926 1419 -50 526 -623 O ATOM 2429 CG2 THR C 37 12.046 27.746 36.188 1.00 16.06 C ANISOU 2429 CG2 THR C 37 2684 2084 1333 15 376 -119 C ATOM 2430 N LYS C 38 12.161 29.116 39.319 1.00 13.90 N ANISOU 2430 N LYS C 38 2904 1324 1054 -160 135 87 N ATOM 2431 CA LYS C 38 11.902 30.485 39.739 1.00 15.28 C ANISOU 2431 CA LYS C 38 3441 1473 891 185 3 20 C ATOM 2432 C LYS C 38 12.039 31.427 38.545 1.00 13.35 C ANISOU 2432 C LYS C 38 2880 1281 910 290 195 -33 C ATOM 2433 O LYS C 38 12.987 31.258 37.759 1.00 13.18 O ANISOU 2433 O LYS C 38 1962 1692 1355 -66 -57 -71 O ATOM 2434 CB ALYS C 38 12.846 30.859 40.885 0.55 16.67 C ANISOU 2434 CB ALYS C 38 3759 1958 618 126 163 -283 C ATOM 2435 CB BLYS C 38 12.873 30.872 40.861 0.45 16.49 C ANISOU 2435 CB BLYS C 38 3741 1759 764 259 23 -257 C ATOM 2436 CG ALYS C 38 12.614 29.996 42.136 0.55 16.73 C ANISOU 2436 CG ALYS C 38 4049 1836 470 217 278 -441 C ATOM 2437 CG BLYS C 38 13.439 29.671 41.605 0.45 18.34 C ANISOU 2437 CG BLYS C 38 3906 2213 848 367 -185 -7 C ATOM 2438 CD ALYS C 38 13.925 29.836 42.898 0.55 21.17 C ANISOU 2438 CD ALYS C 38 4402 2554 1088 442 -95 39 C ATOM 2439 CD BLYS C 38 13.294 29.743 43.111 0.45 20.66 C ANISOU 2439 CD BLYS C 38 4108 2856 885 162 165 179 C ATOM 2440 CE ALYS C 38 13.612 29.639 44.374 0.55 21.24 C ANISOU 2440 CE ALYS C 38 3885 2975 1211 208 -186 451 C ATOM 2441 CE BLYS C 38 13.466 28.368 43.728 0.45 22.03 C ANISOU 2441 CE BLYS C 38 4337 3105 929 363 -315 343 C ATOM 2442 NZ ALYS C 38 12.141 29.443 44.549 0.55 26.10 N ANISOU 2442 NZ ALYS C 38 4330 2118 3469 -1221 366 1052 N ATOM 2443 NZ BLYS C 38 14.882 27.929 43.875 0.45 27.12 N ANISOU 2443 NZ BLYS C 38 4452 4072 1778 1165 1253 997 N ATOM 2444 N PRO C 39 11.120 32.381 38.376 1.00 15.51 N ANISOU 2444 N PRO C 39 2464 1324 2105 97 775 529 N ATOM 2445 CA PRO C 39 11.107 33.142 37.122 1.00 13.03 C ANISOU 2445 CA PRO C 39 1756 1268 1927 265 501 411 C ATOM 2446 C PRO C 39 12.406 33.905 36.898 1.00 12.98 C ANISOU 2446 C PRO C 39 1719 1706 1506 0 -79 809 C ATOM 2447 O PRO C 39 12.798 34.066 35.735 1.00 13.05 O ANISOU 2447 O PRO C 39 2205 1133 1622 -270 531 -290 O ATOM 2448 CB PRO C 39 9.943 34.151 37.291 1.00 15.20 C ANISOU 2448 CB PRO C 39 2232 1466 2078 469 1186 431 C ATOM 2449 CG PRO C 39 9.616 34.154 38.756 1.00 18.33 C ANISOU 2449 CG PRO C 39 3671 1451 1843 469 800 -279 C ATOM 2450 CD PRO C 39 10.068 32.822 39.298 1.00 16.85 C ANISOU 2450 CD PRO C 39 3047 1899 1458 521 511 -11 C ATOM 2451 N GLU C 40 13.080 34.407 37.937 1.00 14.35 N ANISOU 2451 N GLU C 40 2498 1399 1556 -3 326 50 N ATOM 2452 CA GLU C 40 14.309 35.176 37.659 1.00 14.24 C ANISOU 2452 CA GLU C 40 2515 1822 1073 -277 108 -472 C ATOM 2453 C GLU C 40 15.428 34.310 37.106 1.00 13.87 C ANISOU 2453 C GLU C 40 2074 1873 1325 -74 -367 -204 C ATOM 2454 O GLU C 40 16.428 34.822 36.573 1.00 14.78 O ANISOU 2454 O GLU C 40 2055 1655 1906 127 -174 -87 O ATOM 2455 CB GLU C 40 14.725 35.905 38.952 1.00 20.71 C ANISOU 2455 CB GLU C 40 3260 3567 1040 -254 -287 -861 C ATOM 2456 CG GLU C 40 15.305 34.924 39.962 1.00 31.75 C ANISOU 2456 CG GLU C 40 5513 5084 1468 52 -874 -65 C ATOM 2457 CD GLU C 40 14.253 34.330 40.875 1.00 37.47 C ANISOU 2457 CD GLU C 40 6247 5065 2926 -535 -844 1093 C ATOM 2458 OE1 GLU C 40 13.034 34.425 40.586 1.00 27.05 O ANISOU 2458 OE1 GLU C 40 5876 1727 2674 176 -25 -1008 O ATOM 2459 OE2 GLU C 40 14.712 33.766 41.919 1.00 44.72 O ANISOU 2459 OE2 GLU C 40 7794 4208 4991 -947 -1395 2855 O ATOM 2460 N ASP C 41 15.351 32.994 37.211 1.00 14.74 N ANISOU 2460 N ASP C 41 2745 1902 953 -75 357 -248 N ATOM 2461 CA ASP C 41 16.324 32.057 36.676 1.00 12.09 C ANISOU 2461 CA ASP C 41 2120 1946 527 10 -113 -56 C ATOM 2462 C ASP C 41 15.963 31.642 35.240 1.00 11.01 C ANISOU 2462 C ASP C 41 2046 1375 761 92 -330 -158 C ATOM 2463 O ASP C 41 16.708 30.851 34.637 1.00 12.16 O ANISOU 2463 O ASP C 41 1988 1624 1008 -108 -60 -345 O ATOM 2464 CB ASP C 41 16.362 30.804 37.560 1.00 13.52 C ANISOU 2464 CB ASP C 41 2558 2029 549 -64 86 -92 C ATOM 2465 CG ASP C 41 16.914 31.140 38.934 1.00 18.11 C ANISOU 2465 CG ASP C 41 3501 2368 1012 96 -964 168 C ATOM 2466 OD1 ASP C 41 17.761 32.059 38.939 1.00 26.30 O ANISOU 2466 OD1 ASP C 41 4421 4267 1303 -1340 -1614 544 O ATOM 2467 OD2 ASP C 41 16.521 30.571 39.946 1.00 21.32 O ANISOU 2467 OD2 ASP C 41 4508 2830 761 -347 -944 18 O ATOM 2468 N VAL C 42 14.828 32.134 34.723 1.00 10.57 N ANISOU 2468 N VAL C 42 1965 969 1082 -336 -411 238 N ATOM 2469 CA VAL C 42 14.479 31.819 33.319 1.00 9.66 C ANISOU 2469 CA VAL C 42 1443 1377 852 423 -70 203 C ATOM 2470 C VAL C 42 15.147 32.818 32.388 1.00 8.77 C ANISOU 2470 C VAL C 42 1718 968 647 -311 71 -714 C ATOM 2471 O VAL C 42 14.865 34.009 32.456 1.00 10.88 O ANISOU 2471 O VAL C 42 1746 1144 1243 261 333 -100 O ATOM 2472 CB VAL C 42 12.964 31.751 33.168 1.00 9.94 C ANISOU 2472 CB VAL C 42 1375 1964 438 135 188 99 C ATOM 2473 CG1 VAL C 42 12.583 31.407 31.730 1.00 10.92 C ANISOU 2473 CG1 VAL C 42 1932 1528 689 666 -368 14 C ATOM 2474 CG2 VAL C 42 12.319 30.718 34.140 1.00 11.03 C ANISOU 2474 CG2 VAL C 42 2460 951 780 -262 306 -333 C ATOM 2475 N VAL C 43 16.033 32.299 31.547 1.00 9.57 N ANISOU 2475 N VAL C 43 1318 1433 884 321 14 -189 N ATOM 2476 CA VAL C 43 16.711 33.088 30.524 1.00 9.59 C ANISOU 2476 CA VAL C 43 919 1730 995 122 -61 -188 C ATOM 2477 C VAL C 43 15.685 33.671 29.563 1.00 8.91 C ANISOU 2477 C VAL C 43 1078 1119 1189 -79 -217 -90 C ATOM 2478 O VAL C 43 15.589 34.870 29.300 1.00 9.88 O ANISOU 2478 O VAL C 43 1905 1060 788 45 339 -217 O ATOM 2479 CB VAL C 43 17.737 32.210 29.830 1.00 9.06 C ANISOU 2479 CB VAL C 43 1295 1231 918 178 66 57 C ATOM 2480 CG1 VAL C 43 18.385 32.954 28.679 1.00 10.03 C ANISOU 2480 CG1 VAL C 43 1687 1015 1108 -424 344 -348 C ATOM 2481 CG2 VAL C 43 18.789 31.748 30.854 1.00 11.53 C ANISOU 2481 CG2 VAL C 43 1702 1035 1644 383 -531 -317 C ATOM 2482 N GLN C 44 14.860 32.740 29.075 1.00 7.24 N ANISOU 2482 N GLN C 44 837 1308 604 -73 180 -316 N ATOM 2483 CA GLN C 44 13.860 33.045 28.064 1.00 7.38 C ANISOU 2483 CA GLN C 44 1030 988 787 -154 30 -309 C ATOM 2484 C GLN C 44 13.008 31.815 27.831 1.00 7.00 C ANISOU 2484 C GLN C 44 969 865 826 -94 7 -329 C ATOM 2485 O GLN C 44 13.363 30.710 28.274 1.00 9.79 O ANISOU 2485 O GLN C 44 1591 1006 1121 -78 -293 -103 O ATOM 2486 CB GLN C 44 14.515 33.424 26.708 1.00 7.12 C ANISOU 2486 CB GLN C 44 1312 429 965 322 73 132 C ATOM 2487 CG GLN C 44 15.275 32.309 26.081 1.00 8.44 C ANISOU 2487 CG GLN C 44 1304 1204 698 683 -26 1 C ATOM 2488 CD GLN C 44 16.042 32.605 24.807 1.00 10.34 C ANISOU 2488 CD GLN C 44 1836 1664 430 259 -62 -122 C ATOM 2489 OE1 GLN C 44 15.929 31.893 23.779 1.00 13.82 O ANISOU 2489 OE1 GLN C 44 2277 2202 772 281 -224 -589 O ATOM 2490 NE2 GLN C 44 16.823 33.652 24.979 1.00 9.70 N ANISOU 2490 NE2 GLN C 44 1428 1613 642 436 217 -296 N ATOM 2491 N MET C 45 11.931 32.051 27.065 1.00 7.44 N ANISOU 2491 N MET C 45 1117 910 800 -145 -69 -212 N ATOM 2492 CA MET C 45 11.087 30.939 26.657 1.00 7.73 C ANISOU 2492 CA MET C 45 936 1052 951 -62 -215 -299 C ATOM 2493 C MET C 45 10.667 31.113 25.201 1.00 7.17 C ANISOU 2493 C MET C 45 1333 444 948 -157 -261 -298 C ATOM 2494 O MET C 45 10.449 32.256 24.782 1.00 10.10 O ANISOU 2494 O MET C 45 1756 466 1616 -46 -325 -100 O ATOM 2495 CB AMET C 45 9.802 30.819 27.475 0.65 10.01 C ANISOU 2495 CB AMET C 45 1160 1502 1142 -284 -66 -40 C ATOM 2496 CB BMET C 45 9.887 30.935 27.603 0.35 9.29 C ANISOU 2496 CB BMET C 45 1386 966 1179 -421 184 -801 C ATOM 2497 CG AMET C 45 10.118 30.621 28.939 0.65 8.91 C ANISOU 2497 CG AMET C 45 1110 1281 996 -588 -213 -458 C ATOM 2498 CG BMET C 45 8.951 29.746 27.514 0.35 8.87 C ANISOU 2498 CG BMET C 45 1446 597 1325 -275 -165 -126 C ATOM 2499 SD AMET C 45 8.589 30.649 29.901 0.65 11.69 S ANISOU 2499 SD AMET C 45 1447 1722 1273 30 57 37 S ATOM 2500 SD BMET C 45 8.029 29.542 29.053 0.35 18.69 S ANISOU 2500 SD BMET C 45 1712 2697 2690 -222 1000 180 S ATOM 2501 CE AMET C 45 7.518 29.510 29.053 0.65 15.89 C ANISOU 2501 CE AMET C 45 1084 1729 3223 -601 1715 -1198 C ATOM 2502 CE BMET C 45 6.584 28.656 28.497 0.35 23.03 C ANISOU 2502 CE BMET C 45 2665 3467 2617 -1251 995 318 C ATOM 2503 N LEU C 46 10.488 29.951 24.577 1.00 6.60 N ANISOU 2503 N LEU C 46 1288 382 840 -26 -130 -206 N ATOM 2504 CA LEU C 46 9.841 29.891 23.260 1.00 7.54 C ANISOU 2504 CA LEU C 46 1459 652 756 -407 -62 -351 C ATOM 2505 C LEU C 46 8.604 29.011 23.327 1.00 7.32 C ANISOU 2505 C LEU C 46 1254 630 898 -203 -226 59 C ATOM 2506 O LEU C 46 8.644 27.939 23.941 1.00 8.85 O ANISOU 2506 O LEU C 46 1384 690 1288 -291 -543 163 O ATOM 2507 CB LEU C 46 10.800 29.310 22.195 1.00 9.16 C ANISOU 2507 CB LEU C 46 1560 1094 825 -256 43 -284 C ATOM 2508 CG LEU C 46 12.085 30.105 21.992 1.00 10.15 C ANISOU 2508 CG LEU C 46 1652 393 1810 94 509 47 C ATOM 2509 CD1 LEU C 46 13.006 29.377 21.034 1.00 14.28 C ANISOU 2509 CD1 LEU C 46 2246 591 2589 147 1204 -122 C ATOM 2510 CD2 LEU C 46 11.765 31.525 21.476 1.00 14.52 C ANISOU 2510 CD2 LEU C 46 3034 390 2095 403 471 -58 C ATOM 2511 N LEU C 47 7.508 29.384 22.651 1.00 7.61 N ANISOU 2511 N LEU C 47 1306 439 1145 -226 -282 136 N ATOM 2512 CA LEU C 47 6.379 28.466 22.581 1.00 7.72 C ANISOU 2512 CA LEU C 47 1228 1003 704 -394 -24 -341 C ATOM 2513 C LEU C 47 5.977 28.340 21.122 1.00 7.32 C ANISOU 2513 C LEU C 47 1194 849 740 396 -212 -331 C ATOM 2514 O LEU C 47 5.819 29.393 20.458 1.00 10.67 O ANISOU 2514 O LEU C 47 2043 878 1135 -154 -267 -27 O ATOM 2515 CB LEU C 47 5.154 28.998 23.351 1.00 8.99 C ANISOU 2515 CB LEU C 47 1727 766 923 -303 381 -296 C ATOM 2516 CG LEU C 47 5.242 28.914 24.882 1.00 14.16 C ANISOU 2516 CG LEU C 47 1822 2647 910 691 50 -512 C ATOM 2517 CD1 LEU C 47 5.977 30.137 25.360 1.00 25.38 C ANISOU 2517 CD1 LEU C 47 3409 5007 1228 -1350 -764 -687 C ATOM 2518 CD2 LEU C 47 3.914 28.848 25.592 1.00 16.57 C ANISOU 2518 CD2 LEU C 47 2083 3706 506 307 170 -286 C ATOM 2519 N SER C 48 5.819 27.072 20.685 1.00 7.89 N ANISOU 2519 N SER C 48 1525 927 544 -345 -74 -108 N ATOM 2520 CA SER C 48 5.378 26.924 19.293 1.00 7.97 C ANISOU 2520 CA SER C 48 1000 1352 675 -168 -63 -464 C ATOM 2521 C SER C 48 3.936 26.401 19.310 1.00 9.34 C ANISOU 2521 C SER C 48 1046 931 1573 -211 -262 137 C ATOM 2522 O SER C 48 3.459 25.744 20.267 1.00 9.66 O ANISOU 2522 O SER C 48 1332 867 1471 -98 91 -65 O ATOM 2523 CB SER C 48 6.222 25.915 18.505 1.00 9.75 C ANISOU 2523 CB SER C 48 1435 1015 1255 -471 274 -681 C ATOM 2524 OG SER C 48 5.993 24.597 18.996 1.00 10.34 O ANISOU 2524 OG SER C 48 1224 1191 1515 -288 222 -237 O ATOM 2525 N ALA C 49 3.275 26.675 18.196 1.00 8.12 N ANISOU 2525 N ALA C 49 939 1043 1102 -299 -70 -438 N ATOM 2526 CA ALA C 49 1.908 26.195 17.957 1.00 9.46 C ANISOU 2526 CA ALA C 49 1057 691 1846 -334 -421 -104 C ATOM 2527 C ALA C 49 1.827 25.574 16.573 1.00 8.94 C ANISOU 2527 C ALA C 49 808 827 1761 -188 -642 -25 C ATOM 2528 O ALA C 49 2.447 26.123 15.637 1.00 11.60 O ANISOU 2528 O ALA C 49 1779 653 1977 -339 -148 -120 O ATOM 2529 CB ALA C 49 0.876 27.335 18.059 1.00 11.40 C ANISOU 2529 CB ALA C 49 1109 1505 1718 112 -20 86 C ATOM 2530 N THR C 50 1.107 24.477 16.487 1.00 9.30 N ANISOU 2530 N THR C 50 1074 748 1713 -202 -319 -247 N ATOM 2531 CA THR C 50 0.779 23.917 15.168 1.00 10.23 C ANISOU 2531 CA THR C 50 1473 691 1722 -323 -342 -266 C ATOM 2532 C THR C 50 -0.029 24.907 14.359 1.00 10.87 C ANISOU 2532 C THR C 50 1574 1148 1408 -72 -99 -115 C ATOM 2533 O THR C 50 -0.668 25.796 14.917 1.00 12.14 O ANISOU 2533 O THR C 50 1760 1273 1581 95 -185 -208 O ATOM 2534 CB THR C 50 0.033 22.583 15.340 1.00 11.18 C ANISOU 2534 CB THR C 50 1434 571 2242 -180 -44 -553 C ATOM 2535 OG1 THR C 50 -0.933 22.676 16.384 1.00 11.73 O ANISOU 2535 OG1 THR C 50 1232 1143 2084 -255 -158 -241 O ATOM 2536 CG2 THR C 50 1.107 21.549 15.747 1.00 12.58 C ANISOU 2536 CG2 THR C 50 1631 578 2569 -66 -95 -507 C ATOM 2537 N PRO C 51 0.000 24.798 13.016 1.00 13.18 N ANISOU 2537 N PRO C 51 1748 1820 1439 -127 -318 -383 N ATOM 2538 CA PRO C 51 -0.619 25.829 12.188 1.00 14.69 C ANISOU 2538 CA PRO C 51 2071 2389 1122 247 -486 -505 C ATOM 2539 C PRO C 51 -2.139 25.776 12.228 1.00 15.94 C ANISOU 2539 C PRO C 51 2122 2881 1055 68 -775 -97 C ATOM 2540 O PRO C 51 -2.747 26.558 11.485 1.00 17.93 O ANISOU 2540 O PRO C 51 2445 2298 2071 184 -1090 -47 O ATOM 2541 CB PRO C 51 -0.041 25.559 10.790 1.00 14.35 C ANISOU 2541 CB PRO C 51 2561 1666 1227 -56 -419 -740 C ATOM 2542 CG PRO C 51 0.294 24.090 10.837 1.00 19.47 C ANISOU 2542 CG PRO C 51 3911 2096 1391 964 -441 -326 C ATOM 2543 CD PRO C 51 0.741 23.789 12.264 1.00 17.40 C ANISOU 2543 CD PRO C 51 3368 1869 1374 291 -703 -792 C ATOM 2544 N ASP C 52 -2.734 24.930 13.070 1.00 17.28 N ANISOU 2544 N ASP C 52 1956 2317 2292 72 -702 123 N ATOM 2545 CA ASP C 52 -4.192 24.881 13.217 1.00 16.48 C ANISOU 2545 CA ASP C 52 1898 1476 2889 -121 -990 -194 C ATOM 2546 C ASP C 52 -4.630 25.759 14.398 1.00 16.17 C ANISOU 2546 C ASP C 52 1639 1173 3330 13 -743 -150 C ATOM 2547 O ASP C 52 -5.848 25.804 14.638 1.00 19.82 O ANISOU 2547 O ASP C 52 1381 1463 4687 488 -1123 -563 O ATOM 2548 CB ASP C 52 -4.744 23.469 13.390 1.00 17.84 C ANISOU 2548 CB ASP C 52 2435 1346 2996 -33 -908 -253 C ATOM 2549 CG ASP C 52 -3.949 22.650 14.396 1.00 16.30 C ANISOU 2549 CG ASP C 52 1875 960 3359 379 -825 -616 C ATOM 2550 OD1 ASP C 52 -3.163 23.263 15.163 1.00 17.13 O ANISOU 2550 OD1 ASP C 52 2046 921 3542 -261 -998 129 O ATOM 2551 OD2 ASP C 52 -4.113 21.412 14.417 1.00 15.52 O ANISOU 2551 OD2 ASP C 52 2118 1165 2614 -220 -386 -304 O ATOM 2552 N LEU C 53 -3.673 26.422 15.050 1.00 13.80 N ANISOU 2552 N LEU C 53 1541 715 2987 -334 -77 -160 N ATOM 2553 CA LEU C 53 -4.027 27.268 16.217 1.00 13.24 C ANISOU 2553 CA LEU C 53 1516 1084 2431 -168 -46 189 C ATOM 2554 C LEU C 53 -3.860 28.738 15.912 1.00 11.09 C ANISOU 2554 C LEU C 53 858 907 2449 -235 -490 -317 C ATOM 2555 O LEU C 53 -2.763 29.185 15.543 1.00 14.12 O ANISOU 2555 O LEU C 53 1176 1259 2928 -209 -12 174 O ATOM 2556 CB LEU C 53 -3.174 26.821 17.421 1.00 14.74 C ANISOU 2556 CB LEU C 53 1487 982 3129 -60 -579 -36 C ATOM 2557 CG LEU C 53 -3.450 25.407 17.939 1.00 13.23 C ANISOU 2557 CG LEU C 53 1133 952 2944 326 -286 77 C ATOM 2558 CD1 LEU C 53 -2.555 25.131 19.152 1.00 15.74 C ANISOU 2558 CD1 LEU C 53 1666 1619 2695 -5 -418 87 C ATOM 2559 CD2 LEU C 53 -4.925 25.170 18.273 1.00 13.96 C ANISOU 2559 CD2 LEU C 53 1321 1507 2474 142 79 -194 C ATOM 2560 N HIS C 54 -4.921 29.515 16.032 1.00 12.80 N ANISOU 2560 N HIS C 54 1236 1289 2340 143 -330 -330 N ATOM 2561 CA HIS C 54 -4.863 30.934 15.685 1.00 13.73 C ANISOU 2561 CA HIS C 54 1812 1280 2126 377 -172 -247 C ATOM 2562 C HIS C 54 -5.496 31.799 16.740 1.00 12.11 C ANISOU 2562 C HIS C 54 1083 1264 2254 271 -131 -160 C ATOM 2563 O HIS C 54 -5.463 33.047 16.620 1.00 14.71 O ANISOU 2563 O HIS C 54 1823 1288 2480 439 46 -144 O ATOM 2564 CB HIS C 54 -5.622 31.192 14.367 1.00 16.26 C ANISOU 2564 CB HIS C 54 2773 930 2475 -268 -894 -367 C ATOM 2565 CG HIS C 54 -5.224 30.258 13.284 1.00 16.97 C ANISOU 2565 CG HIS C 54 2625 1431 2394 -1 -870 -362 C ATOM 2566 ND1 HIS C 54 -4.034 30.416 12.599 1.00 20.34 N ANISOU 2566 ND1 HIS C 54 3278 2010 2440 -426 -413 -240 N ATOM 2567 CD2 HIS C 54 -5.813 29.142 12.808 1.00 16.10 C ANISOU 2567 CD2 HIS C 54 2486 1545 2086 168 -959 -635 C ATOM 2568 CE1 HIS C 54 -3.904 29.446 11.704 1.00 20.67 C ANISOU 2568 CE1 HIS C 54 3049 1951 2851 -86 -352 -374 C ATOM 2569 NE2 HIS C 54 -4.978 28.669 11.815 1.00 20.03 N ANISOU 2569 NE2 HIS C 54 3007 1635 2970 67 -195 -626 N ATOM 2570 N ALA C 55 -6.117 31.245 17.779 1.00 13.94 N ANISOU 2570 N ALA C 55 1156 1657 2483 -47 37 -185 N ATOM 2571 CA ALA C 55 -6.966 32.129 18.601 1.00 11.35 C ANISOU 2571 CA ALA C 55 899 1478 1934 72 -333 48 C ATOM 2572 C ALA C 55 -6.177 33.104 19.483 1.00 12.15 C ANISOU 2572 C ALA C 55 940 1337 2340 2 -317 -6 C ATOM 2573 O ALA C 55 -6.714 34.163 19.819 1.00 14.96 O ANISOU 2573 O ALA C 55 1436 1547 2700 141 -52 -242 O ATOM 2574 CB ALA C 55 -7.927 31.270 19.407 1.00 13.68 C ANISOU 2574 CB ALA C 55 693 1607 2897 -64 -34 -130 C ATOM 2575 N VAL C 56 -4.957 32.797 19.884 1.00 12.06 N ANISOU 2575 N VAL C 56 1107 1668 1809 -179 -470 344 N ATOM 2576 CA VAL C 56 -4.181 33.608 20.808 1.00 12.34 C ANISOU 2576 CA VAL C 56 1189 1563 1938 27 -520 173 C ATOM 2577 C VAL C 56 -2.724 33.179 20.720 1.00 10.24 C ANISOU 2577 C VAL C 56 1111 933 1845 -213 -365 427 C ATOM 2578 O VAL C 56 -2.492 32.016 20.314 1.00 12.28 O ANISOU 2578 O VAL C 56 1381 1220 2065 -214 -263 -86 O ATOM 2579 CB VAL C 56 -4.734 33.467 22.266 1.00 11.40 C ANISOU 2579 CB VAL C 56 1210 1102 2018 43 -375 -32 C ATOM 2580 CG1 VAL C 56 -4.390 32.091 22.849 1.00 12.81 C ANISOU 2580 CG1 VAL C 56 1557 1281 2028 231 -134 140 C ATOM 2581 CG2 VAL C 56 -4.248 34.648 23.133 1.00 13.06 C ANISOU 2581 CG2 VAL C 56 1190 1404 2367 -272 -16 -286 C ATOM 2582 N PHE C 57 -1.819 34.082 21.095 1.00 10.55 N ANISOU 2582 N PHE C 57 1110 997 1900 -132 -345 215 N ATOM 2583 CA PHE C 57 -0.425 33.640 21.294 1.00 10.09 C ANISOU 2583 CA PHE C 57 1071 1082 1679 13 -398 -113 C ATOM 2584 C PHE C 57 -0.331 32.866 22.585 1.00 10.43 C ANISOU 2584 C PHE C 57 1076 1145 1742 490 181 14 C ATOM 2585 O PHE C 57 -0.709 33.440 23.628 1.00 11.52 O ANISOU 2585 O PHE C 57 1256 1208 1914 330 411 -58 O ATOM 2586 CB PHE C 57 0.514 34.853 21.371 1.00 11.08 C ANISOU 2586 CB PHE C 57 1005 1121 2084 69 -457 66 C ATOM 2587 CG PHE C 57 0.605 35.497 19.977 1.00 10.49 C ANISOU 2587 CG PHE C 57 1101 858 2028 -79 -327 -174 C ATOM 2588 CD1 PHE C 57 1.451 34.946 19.014 1.00 11.94 C ANISOU 2588 CD1 PHE C 57 1175 1124 2237 -103 -180 -227 C ATOM 2589 CD2 PHE C 57 -0.177 36.615 19.729 1.00 12.46 C ANISOU 2589 CD2 PHE C 57 1722 1246 1769 370 -342 4 C ATOM 2590 CE1 PHE C 57 1.470 35.561 17.764 1.00 13.11 C ANISOU 2590 CE1 PHE C 57 1008 1996 1976 -413 -445 -273 C ATOM 2591 CE2 PHE C 57 -0.150 37.225 18.472 1.00 13.62 C ANISOU 2591 CE2 PHE C 57 2298 800 2077 -396 -67 165 C ATOM 2592 CZ PHE C 57 0.693 36.671 17.517 1.00 12.73 C ANISOU 2592 CZ PHE C 57 1882 1168 1789 -712 -293 -34 C ATOM 2593 N PRO C 58 0.132 31.593 22.641 1.00 9.50 N ANISOU 2593 N PRO C 58 774 976 1861 118 -167 -136 N ATOM 2594 CA PRO C 58 0.162 30.889 23.922 1.00 11.35 C ANISOU 2594 CA PRO C 58 1567 824 1924 131 -265 -163 C ATOM 2595 C PRO C 58 1.074 31.591 24.934 1.00 10.68 C ANISOU 2595 C PRO C 58 1480 815 1762 -137 -202 33 C ATOM 2596 O PRO C 58 0.953 31.418 26.170 1.00 12.10 O ANISOU 2596 O PRO C 58 1385 1437 1777 -201 13 64 O ATOM 2597 CB PRO C 58 0.716 29.504 23.592 1.00 11.40 C ANISOU 2597 CB PRO C 58 1602 1088 1641 375 -203 -266 C ATOM 2598 CG PRO C 58 0.582 29.365 22.125 1.00 15.28 C ANISOU 2598 CG PRO C 58 3275 1015 1515 527 31 68 C ATOM 2599 CD PRO C 58 0.530 30.756 21.555 1.00 11.66 C ANISOU 2599 CD PRO C 58 1653 766 2011 198 198 -19 C ATOM 2600 N ALA C 59 2.019 32.418 24.502 1.00 10.71 N ANISOU 2600 N ALA C 59 1534 866 1668 -64 205 -286 N ATOM 2601 CA ALA C 59 2.894 33.180 25.378 1.00 10.67 C ANISOU 2601 CA ALA C 59 1172 728 2153 49 227 -420 C ATOM 2602 C ALA C 59 2.062 34.098 26.295 1.00 10.90 C ANISOU 2602 C ALA C 59 1173 1043 1925 221 -54 -595 C ATOM 2603 O ALA C 59 2.583 34.501 27.353 1.00 11.66 O ANISOU 2603 O ALA C 59 1532 1442 1457 -193 156 -185 O ATOM 2604 CB ALA C 59 3.864 34.071 24.600 1.00 11.84 C ANISOU 2604 CB ALA C 59 1067 1309 2121 -59 -43 28 C ATOM 2605 N LYS C 60 0.806 34.448 25.957 1.00 10.39 N ANISOU 2605 N LYS C 60 1218 820 1911 243 186 -180 N ATOM 2606 CA LYS C 60 -0.014 35.252 26.849 1.00 12.71 C ANISOU 2606 CA LYS C 60 1137 1670 2021 306 512 -123 C ATOM 2607 C LYS C 60 -0.122 34.577 28.214 1.00 14.00 C ANISOU 2607 C LYS C 60 1567 1728 2023 -879 454 -224 C ATOM 2608 O LYS C 60 -0.156 35.244 29.257 1.00 15.21 O ANISOU 2608 O LYS C 60 2190 1669 1919 -160 -183 -181 O ATOM 2609 CB LYS C 60 -1.382 35.512 26.225 1.00 15.86 C ANISOU 2609 CB LYS C 60 1195 1921 2911 485 286 -486 C ATOM 2610 CG LYS C 60 -2.393 36.180 27.131 1.00 14.21 C ANISOU 2610 CG LYS C 60 966 1266 3169 121 402 -436 C ATOM 2611 CD LYS C 60 -3.660 36.608 26.392 1.00 16.22 C ANISOU 2611 CD LYS C 60 1373 2215 2576 803 581 -105 C ATOM 2612 CE LYS C 60 -4.670 37.182 27.398 1.00 15.60 C ANISOU 2612 CE LYS C 60 1016 2239 2674 339 688 -195 C ATOM 2613 NZ LYS C 60 -5.825 37.881 26.718 1.00 15.28 N ANISOU 2613 NZ LYS C 60 1025 1716 3063 331 734 -37 N ATOM 2614 N ALA C 61 -0.189 33.247 28.242 1.00 13.61 N ANISOU 2614 N ALA C 61 1540 1709 1923 -777 622 -211 N ATOM 2615 CA ALA C 61 -0.301 32.576 29.560 1.00 12.33 C ANISOU 2615 CA ALA C 61 1419 1564 1702 -901 412 -447 C ATOM 2616 C ALA C 61 0.927 32.806 30.409 1.00 13.49 C ANISOU 2616 C ALA C 61 1260 1957 1909 -346 394 -1133 C ATOM 2617 O ALA C 61 0.855 32.890 31.648 1.00 17.51 O ANISOU 2617 O ALA C 61 1759 3132 1762 -617 229 -663 O ATOM 2618 CB ALA C 61 -0.579 31.077 29.385 1.00 12.85 C ANISOU 2618 CB ALA C 61 1670 1485 1727 -681 -22 -304 C ATOM 2619 N VAL C 62 2.125 32.923 29.780 1.00 12.23 N ANISOU 2619 N VAL C 62 1142 1261 2246 -132 347 -287 N ATOM 2620 CA VAL C 62 3.339 33.222 30.530 1.00 10.74 C ANISOU 2620 CA VAL C 62 1191 1243 1648 -200 481 -266 C ATOM 2621 C VAL C 62 3.309 34.678 31.012 1.00 10.70 C ANISOU 2621 C VAL C 62 1527 1310 1230 -81 364 -189 C ATOM 2622 O VAL C 62 3.594 34.980 32.174 1.00 12.21 O ANISOU 2622 O VAL C 62 1761 1502 1377 -311 26 -243 O ATOM 2623 CB VAL C 62 4.630 33.016 29.679 1.00 10.22 C ANISOU 2623 CB VAL C 62 1127 1406 1349 -77 384 -112 C ATOM 2624 CG1 VAL C 62 5.865 33.299 30.534 1.00 12.36 C ANISOU 2624 CG1 VAL C 62 1230 2273 1195 -480 349 232 C ATOM 2625 CG2 VAL C 62 4.717 31.626 29.065 1.00 11.10 C ANISOU 2625 CG2 VAL C 62 2113 1207 897 -288 943 171 C ATOM 2626 N ARG C 63 2.917 35.604 30.142 1.00 12.21 N ANISOU 2626 N ARG C 63 1732 1448 1461 203 217 -100 N ATOM 2627 CA ARG C 63 2.960 37.017 30.487 1.00 13.18 C ANISOU 2627 CA ARG C 63 1996 1332 1680 -310 788 79 C ATOM 2628 C ARG C 63 1.975 37.318 31.600 1.00 14.48 C ANISOU 2628 C ARG C 63 2395 861 2244 -135 1255 171 C ATOM 2629 O ARG C 63 2.122 38.299 32.347 1.00 22.15 O ANISOU 2629 O ARG C 63 3499 1836 3080 -660 1811 -774 O ATOM 2630 CB ARG C 63 2.672 37.865 29.250 1.00 11.28 C ANISOU 2630 CB ARG C 63 1706 1135 1446 -443 244 -382 C ATOM 2631 CG ARG C 63 3.668 37.610 28.129 1.00 11.55 C ANISOU 2631 CG ARG C 63 1376 1845 1166 -516 55 -138 C ATOM 2632 CD ARG C 63 3.662 38.717 27.064 1.00 13.92 C ANISOU 2632 CD ARG C 63 2426 1512 1350 262 469 -215 C ATOM 2633 NE ARG C 63 4.686 38.355 26.080 1.00 10.99 N ANISOU 2633 NE ARG C 63 2009 1042 1126 -6 244 -165 N ATOM 2634 CZ ARG C 63 4.485 37.848 24.885 1.00 12.17 C ANISOU 2634 CZ ARG C 63 1364 2498 764 226 182 82 C ATOM 2635 NH1 ARG C 63 3.273 37.594 24.405 1.00 9.28 N ANISOU 2635 NH1 ARG C 63 1419 781 1325 34 210 157 N ATOM 2636 NH2 ARG C 63 5.563 37.583 24.163 1.00 10.87 N ANISOU 2636 NH2 ARG C 63 1506 1403 1220 262 379 14 N ATOM 2637 N GLU C 64 0.933 36.465 31.678 1.00 14.09 N ANISOU 2637 N GLU C 64 1633 1316 2406 99 806 454 N ATOM 2638 CA GLU C 64 -0.075 36.722 32.717 1.00 16.92 C ANISOU 2638 CA GLU C 64 1334 2857 2237 -60 549 32 C ATOM 2639 C GLU C 64 0.183 35.964 34.012 1.00 15.17 C ANISOU 2639 C GLU C 64 1740 2324 1700 -135 487 -566 C ATOM 2640 O GLU C 64 -0.513 36.181 35.019 1.00 19.03 O ANISOU 2640 O GLU C 64 2788 2240 2204 -1 1217 -536 O ATOM 2641 CB GLU C 64 -1.480 36.343 32.219 1.00 19.33 C ANISOU 2641 CB GLU C 64 1508 3787 2050 -70 427 -520 C ATOM 2642 CG GLU C 64 -2.131 37.299 31.238 1.00 24.63 C ANISOU 2642 CG GLU C 64 2233 4145 2981 -3 -544 -398 C ATOM 2643 CD GLU C 64 -3.559 36.977 30.843 1.00 27.97 C ANISOU 2643 CD GLU C 64 1811 5820 2997 288 -112 -569 C ATOM 2644 OE1 GLU C 64 -3.911 35.776 30.753 1.00 30.93 O ANISOU 2644 OE1 GLU C 64 2200 6575 2978 -1427 -342 784 O ATOM 2645 OE2 GLU C 64 -4.390 37.884 30.595 1.00 33.50 O ANISOU 2645 OE2 GLU C 64 2626 7811 2292 1788 31 -712 O ATOM 2646 N LEU C 65 1.142 35.045 34.046 1.00 14.50 N ANISOU 2646 N LEU C 65 1599 2283 1626 -258 594 -297 N ATOM 2647 CA LEU C 65 1.408 34.294 35.278 1.00 17.56 C ANISOU 2647 CA LEU C 65 2586 2632 1452 402 548 -548 C ATOM 2648 C LEU C 65 2.103 35.171 36.315 1.00 16.86 C ANISOU 2648 C LEU C 65 2492 2657 1259 192 788 -396 C ATOM 2649 O LEU C 65 3.137 35.794 36.021 1.00 16.82 O ANISOU 2649 O LEU C 65 2543 2264 1586 239 893 -327 O ATOM 2650 CB LEU C 65 2.317 33.091 34.966 1.00 17.82 C ANISOU 2650 CB LEU C 65 2383 1989 2398 -43 823 -277 C ATOM 2651 CG LEU C 65 2.357 32.038 36.083 1.00 22.63 C ANISOU 2651 CG LEU C 65 2872 2696 3031 261 1236 392 C ATOM 2652 CD1 LEU C 65 0.992 31.360 36.194 1.00 21.80 C ANISOU 2652 CD1 LEU C 65 2928 3018 2338 99 1076 651 C ATOM 2653 CD2 LEU C 65 3.481 31.055 35.812 1.00 24.30 C ANISOU 2653 CD2 LEU C 65 2997 1789 4447 -45 1565 560 C ATOM 2654 N SER C 66 1.572 35.257 37.529 1.00 18.12 N ANISOU 2654 N SER C 66 2643 3311 929 -36 530 -58 N ATOM 2655 CA SER C 66 2.143 36.129 38.555 1.00 18.96 C ANISOU 2655 CA SER C 66 2618 3315 1270 351 530 -488 C ATOM 2656 C SER C 66 3.646 35.917 38.738 1.00 15.15 C ANISOU 2656 C SER C 66 2631 2339 786 230 579 -276 C ATOM 2657 O SER C 66 4.121 34.807 38.951 1.00 19.07 O ANISOU 2657 O SER C 66 2744 2120 2382 268 1151 -458 O ATOM 2658 CB SER C 66 1.428 35.879 39.899 1.00 18.39 C ANISOU 2658 CB SER C 66 2543 3138 1305 458 638 -671 C ATOM 2659 OG SER C 66 0.041 36.160 39.713 1.00 32.31 O ANISOU 2659 OG SER C 66 2495 5126 4657 1192 1238 -1379 O ATOM 2660 N GLY C 67 4.390 37.008 38.631 1.00 17.81 N ANISOU 2660 N GLY C 67 2684 2371 1712 294 1399 310 N ATOM 2661 CA GLY C 67 5.811 37.011 38.817 1.00 15.56 C ANISOU 2661 CA GLY C 67 2814 1928 1170 174 735 -150 C ATOM 2662 C GLY C 67 6.587 36.665 37.561 1.00 14.11 C ANISOU 2662 C GLY C 67 2010 1771 1580 71 544 -871 C ATOM 2663 O GLY C 67 7.821 36.772 37.624 1.00 15.45 O ANISOU 2663 O GLY C 67 2016 1500 2353 38 406 -4 O ATOM 2664 N TRP C 68 5.931 36.288 36.476 1.00 12.92 N ANISOU 2664 N TRP C 68 2622 904 1383 219 261 -366 N ATOM 2665 CA TRP C 68 6.624 35.903 35.233 1.00 11.80 C ANISOU 2665 CA TRP C 68 1905 1194 1383 -103 109 -455 C ATOM 2666 C TRP C 68 6.571 37.052 34.229 1.00 13.89 C ANISOU 2666 C TRP C 68 2134 1285 1860 148 847 -165 C ATOM 2667 O TRP C 68 6.939 36.840 33.058 1.00 13.51 O ANISOU 2667 O TRP C 68 2174 1053 1905 -298 952 -288 O ATOM 2668 CB TRP C 68 6.012 34.582 34.732 1.00 12.26 C ANISOU 2668 CB TRP C 68 2224 1130 1303 -22 115 -466 C ATOM 2669 CG TRP C 68 6.513 33.427 35.561 1.00 12.89 C ANISOU 2669 CG TRP C 68 2216 1240 1442 49 483 -315 C ATOM 2670 CD1 TRP C 68 6.278 33.201 36.899 1.00 13.81 C ANISOU 2670 CD1 TRP C 68 2450 1464 1332 268 281 -311 C ATOM 2671 CD2 TRP C 68 7.338 32.337 35.112 1.00 11.93 C ANISOU 2671 CD2 TRP C 68 1667 1167 1698 -70 546 -214 C ATOM 2672 NE1 TRP C 68 6.914 32.034 37.281 1.00 14.81 N ANISOU 2672 NE1 TRP C 68 2778 1250 1599 250 469 -273 N ATOM 2673 CE2 TRP C 68 7.564 31.499 36.208 1.00 16.28 C ANISOU 2673 CE2 TRP C 68 2685 1866 1633 599 608 -79 C ATOM 2674 CE3 TRP C 68 7.910 32.004 33.857 1.00 11.20 C ANISOU 2674 CE3 TRP C 68 1477 1304 1472 -31 243 -357 C ATOM 2675 CZ2 TRP C 68 8.340 30.331 36.117 1.00 12.35 C ANISOU 2675 CZ2 TRP C 68 2138 1476 1077 140 312 -188 C ATOM 2676 CZ3 TRP C 68 8.697 30.830 33.728 1.00 10.29 C ANISOU 2676 CZ3 TRP C 68 1323 1573 1015 109 154 -200 C ATOM 2677 CH2 TRP C 68 8.874 30.044 34.885 1.00 13.15 C ANISOU 2677 CH2 TRP C 68 2098 1832 1066 368 206 -149 C ATOM 2678 N GLN C 69 6.124 38.266 34.641 1.00 13.03 N ANISOU 2678 N GLN C 69 1850 968 2134 -373 575 -446 N ATOM 2679 CA GLN C 69 5.878 39.311 33.630 1.00 13.79 C ANISOU 2679 CA GLN C 69 1483 1198 2557 -121 356 -241 C ATOM 2680 C GLN C 69 7.133 39.916 32.989 1.00 12.79 C ANISOU 2680 C GLN C 69 1383 1104 2373 253 418 108 C ATOM 2681 O GLN C 69 7.033 40.640 31.984 1.00 15.09 O ANISOU 2681 O GLN C 69 2182 1259 2294 -416 -155 69 O ATOM 2682 CB GLN C 69 5.013 40.450 34.189 1.00 12.41 C ANISOU 2682 CB GLN C 69 1376 1722 1618 95 71 -432 C ATOM 2683 CG GLN C 69 5.690 41.170 35.353 1.00 14.69 C ANISOU 2683 CG GLN C 69 2644 1376 1561 246 -743 31 C ATOM 2684 CD GLN C 69 5.315 40.615 36.712 1.00 15.24 C ANISOU 2684 CD GLN C 69 2943 1234 1615 281 -419 -149 C ATOM 2685 OE1 GLN C 69 5.155 39.383 36.831 1.00 15.60 O ANISOU 2685 OE1 GLN C 69 2832 1275 1823 456 455 -163 O ATOM 2686 NE2 GLN C 69 5.140 41.449 37.723 1.00 18.88 N ANISOU 2686 NE2 GLN C 69 3494 1429 2251 520 758 -325 N ATOM 2687 N TYR C 70 8.297 39.591 33.558 1.00 13.33 N ANISOU 2687 N TYR C 70 1417 1612 2037 512 439 -434 N ATOM 2688 CA TYR C 70 9.573 40.006 33.001 1.00 11.50 C ANISOU 2688 CA TYR C 70 1279 1097 1993 209 70 -817 C ATOM 2689 C TYR C 70 10.322 38.839 32.376 1.00 12.33 C ANISOU 2689 C TYR C 70 2000 1167 1518 -294 1055 -978 C ATOM 2690 O TYR C 70 11.489 38.957 31.953 1.00 13.40 O ANISOU 2690 O TYR C 70 2015 1078 1996 26 1222 -274 O ATOM 2691 CB TYR C 70 10.489 40.708 34.042 1.00 11.80 C ANISOU 2691 CB TYR C 70 2256 976 1250 355 -274 -637 C ATOM 2692 CG TYR C 70 9.787 41.959 34.550 1.00 12.50 C ANISOU 2692 CG TYR C 70 2283 1114 1352 594 -371 -526 C ATOM 2693 CD1 TYR C 70 9.774 43.134 33.805 1.00 13.40 C ANISOU 2693 CD1 TYR C 70 1766 1035 2291 422 34 -315 C ATOM 2694 CD2 TYR C 70 9.139 41.957 35.773 1.00 12.19 C ANISOU 2694 CD2 TYR C 70 1881 1409 1342 821 -478 -598 C ATOM 2695 CE1 TYR C 70 9.141 44.300 34.240 1.00 14.95 C ANISOU 2695 CE1 TYR C 70 2489 1010 2182 415 320 -364 C ATOM 2696 CE2 TYR C 70 8.485 43.112 36.224 1.00 14.54 C ANISOU 2696 CE2 TYR C 70 2289 1335 1902 865 110 -302 C ATOM 2697 CZ TYR C 70 8.501 44.268 35.477 1.00 13.90 C ANISOU 2697 CZ TYR C 70 2375 1049 1858 241 -9 -533 C ATOM 2698 OH TYR C 70 7.841 45.406 35.889 1.00 14.43 O ANISOU 2698 OH TYR C 70 2565 1201 1718 522 112 -245 O ATOM 2699 N VAL C 71 9.706 37.661 32.282 1.00 9.97 N ANISOU 2699 N VAL C 71 1896 876 1016 -52 322 -456 N ATOM 2700 CA VAL C 71 10.351 36.546 31.553 1.00 8.64 C ANISOU 2700 CA VAL C 71 1335 1018 931 -588 516 -697 C ATOM 2701 C VAL C 71 10.217 36.763 30.046 1.00 8.30 C ANISOU 2701 C VAL C 71 1224 883 1045 -187 442 -484 C ATOM 2702 O VAL C 71 9.080 36.729 29.564 1.00 10.79 O ANISOU 2702 O VAL C 71 1314 1402 1383 -130 317 -161 O ATOM 2703 CB VAL C 71 9.784 35.181 31.950 1.00 8.95 C ANISOU 2703 CB VAL C 71 1364 869 1168 -295 363 -431 C ATOM 2704 CG1 VAL C 71 10.370 34.044 31.133 1.00 9.72 C ANISOU 2704 CG1 VAL C 71 1248 834 1610 503 -95 -270 C ATOM 2705 CG2 VAL C 71 10.011 34.929 33.437 1.00 10.81 C ANISOU 2705 CG2 VAL C 71 1554 1206 1347 65 123 -108 C ATOM 2706 N PRO C 72 11.309 36.930 29.282 1.00 8.10 N ANISOU 2706 N PRO C 72 1267 975 835 127 430 -449 N ATOM 2707 CA PRO C 72 11.131 37.173 27.839 1.00 7.22 C ANISOU 2707 CA PRO C 72 1350 476 918 -314 277 -444 C ATOM 2708 C PRO C 72 10.649 35.902 27.146 1.00 6.50 C ANISOU 2708 C PRO C 72 1175 284 1010 10 -63 -197 C ATOM 2709 O PRO C 72 11.239 34.845 27.371 1.00 8.40 O ANISOU 2709 O PRO C 72 1566 455 1170 443 2 -468 O ATOM 2710 CB PRO C 72 12.490 37.627 27.367 1.00 8.48 C ANISOU 2710 CB PRO C 72 1250 855 1117 -296 136 94 C ATOM 2711 CG PRO C 72 13.447 37.074 28.352 1.00 9.02 C ANISOU 2711 CG PRO C 72 1421 1182 823 524 510 47 C ATOM 2712 CD PRO C 72 12.741 36.874 29.656 1.00 9.57 C ANISOU 2712 CD PRO C 72 1194 1534 909 486 557 0 C ATOM 2713 N VAL C 73 9.638 36.085 26.318 1.00 8.21 N ANISOU 2713 N VAL C 73 968 789 1364 -245 -162 -139 N ATOM 2714 CA VAL C 73 9.031 34.918 25.649 1.00 7.87 C ANISOU 2714 CA VAL C 73 1307 616 1069 -570 -89 215 C ATOM 2715 C VAL C 73 8.617 35.337 24.262 1.00 7.18 C ANISOU 2715 C VAL C 73 1204 420 1105 -209 -72 -45 C ATOM 2716 O VAL C 73 8.251 36.500 24.035 1.00 7.72 O ANISOU 2716 O VAL C 73 1274 611 1051 212 28 -63 O ATOM 2717 CB VAL C 73 7.887 34.326 26.510 1.00 9.72 C ANISOU 2717 CB VAL C 73 1409 475 1808 -310 258 403 C ATOM 2718 CG1 VAL C 73 6.861 35.439 26.777 1.00 10.97 C ANISOU 2718 CG1 VAL C 73 1510 1354 1303 226 -84 253 C ATOM 2719 CG2 VAL C 73 7.277 33.092 25.892 1.00 11.86 C ANISOU 2719 CG2 VAL C 73 1901 872 1733 -929 456 404 C ATOM 2720 N THR C 74 8.595 34.419 23.337 1.00 8.08 N ANISOU 2720 N THR C 74 1380 605 1084 -59 -151 -119 N ATOM 2721 CA THR C 74 8.009 34.695 22.005 1.00 9.10 C ANISOU 2721 CA THR C 74 1556 793 1108 -605 -238 46 C ATOM 2722 C THR C 74 7.581 33.336 21.419 1.00 8.50 C ANISOU 2722 C THR C 74 1495 708 1027 -248 -187 -45 C ATOM 2723 O THR C 74 7.975 32.271 21.913 1.00 8.73 O ANISOU 2723 O THR C 74 1378 669 1271 -313 -67 75 O ATOM 2724 CB THR C 74 8.914 35.552 21.122 1.00 8.22 C ANISOU 2724 CB THR C 74 1281 409 1431 161 175 149 C ATOM 2725 OG1 THR C 74 8.172 36.169 20.065 1.00 9.28 O ANISOU 2725 OG1 THR C 74 1373 696 1457 -160 -91 233 O ATOM 2726 CG2 THR C 74 10.013 34.684 20.507 1.00 11.11 C ANISOU 2726 CG2 THR C 74 1320 549 2351 54 111 -587 C ATOM 2727 N CYS C 75 6.796 33.458 20.334 1.00 8.12 N ANISOU 2727 N CYS C 75 1149 661 1276 -313 -272 -154 N ATOM 2728 CA CYS C 75 6.177 32.273 19.762 1.00 8.65 C ANISOU 2728 CA CYS C 75 1179 726 1381 -393 -131 -254 C ATOM 2729 C CYS C 75 6.668 32.022 18.329 1.00 11.47 C ANISOU 2729 C CYS C 75 1698 1394 1267 -421 -130 -438 C ATOM 2730 O CYS C 75 7.336 32.840 17.692 1.00 9.18 O ANISOU 2730 O CYS C 75 1178 1089 1219 112 -168 -247 O ATOM 2731 CB CYS C 75 4.618 32.374 19.728 1.00 7.45 C ANISOU 2731 CB CYS C 75 1226 538 1065 -219 -552 -24 C ATOM 2732 SG CYS C 75 3.977 32.611 21.425 1.00 10.21 S ANISOU 2732 SG CYS C 75 1426 1075 1377 -29 -145 -75 S ATOM 2733 N MET C 76 6.375 30.808 17.871 1.00 8.51 N ANISOU 2733 N MET C 76 1102 1304 829 -135 -519 -154 N ATOM 2734 CA MET C 76 6.636 30.516 16.455 1.00 8.92 C ANISOU 2734 CA MET C 76 1345 1110 932 74 -411 -206 C ATOM 2735 C MET C 76 5.698 29.409 16.035 1.00 9.26 C ANISOU 2735 C MET C 76 1556 995 966 -22 -191 -283 C ATOM 2736 O MET C 76 5.105 28.715 16.865 1.00 10.18 O ANISOU 2736 O MET C 76 1366 1181 1320 206 12 -62 O ATOM 2737 CB AMET C 76 8.090 30.175 16.146 0.58 9.83 C ANISOU 2737 CB AMET C 76 1430 888 1416 151 -162 22 C ATOM 2738 CB BMET C 76 8.107 30.075 16.390 0.42 9.96 C ANISOU 2738 CB BMET C 76 1465 895 1424 205 -340 -352 C ATOM 2739 CG AMET C 76 8.541 28.786 16.595 0.58 9.35 C ANISOU 2739 CG AMET C 76 1718 678 1156 80 -294 -324 C ATOM 2740 CG BMET C 76 8.408 28.800 17.170 0.42 5.54 C ANISOU 2740 CG BMET C 76 1513 593 0 213 -400 -1111 C ATOM 2741 SD AMET C 76 8.701 28.837 18.393 0.58 9.03 S ANISOU 2741 SD AMET C 76 1390 947 1096 -88 -161 -165 S ATOM 2742 SD BMET C 76 10.104 28.583 17.754 0.42 9.97 S ANISOU 2742 SD BMET C 76 1305 1017 1468 -283 -429 121 S ATOM 2743 CE AMET C 76 10.113 27.738 18.536 0.58 13.10 C ANISOU 2743 CE AMET C 76 2040 1610 1327 572 -663 -714 C ATOM 2744 CE BMET C 76 9.891 27.056 18.670 0.42 6.17 C ANISOU 2744 CE BMET C 76 610 267 1469 -116 -127 -492 C ATOM 2745 N GLN C 77 5.569 29.256 14.714 1.00 8.98 N ANISOU 2745 N GLN C 77 1665 700 1047 -80 37 -635 N ATOM 2746 CA GLN C 77 4.808 28.124 14.188 1.00 9.29 C ANISOU 2746 CA GLN C 77 1848 580 1103 -136 -420 -115 C ATOM 2747 C GLN C 77 5.643 26.868 14.136 1.00 10.91 C ANISOU 2747 C GLN C 77 1902 539 1704 -231 147 -400 C ATOM 2748 O GLN C 77 6.755 26.898 13.629 1.00 10.54 O ANISOU 2748 O GLN C 77 1646 1198 1163 -97 -194 187 O ATOM 2749 CB GLN C 77 4.374 28.424 12.745 1.00 13.46 C ANISOU 2749 CB GLN C 77 2256 2033 826 -486 -297 -25 C ATOM 2750 CG GLN C 77 3.213 27.513 12.323 1.00 21.74 C ANISOU 2750 CG GLN C 77 2851 3212 2198 -872 -1453 100 C ATOM 2751 CD GLN C 77 2.691 28.059 10.996 1.00 31.63 C ANISOU 2751 CD GLN C 77 4111 6101 1806 -1329 -1692 362 C ATOM 2752 OE1 GLN C 77 1.880 28.970 11.022 1.00 40.37 O ANISOU 2752 OE1 GLN C 77 5026 6209 4105 -767 -2674 2507 O ATOM 2753 NE2 GLN C 77 3.184 27.497 9.900 1.00 49.73 N ANISOU 2753 NE2 GLN C 77 4917 11851 2129 -3402 435 -636 N ATOM 2754 N GLU C 78 5.057 25.775 14.637 1.00 7.46 N ANISOU 2754 N GLU C 78 1505 571 759 174 -158 -119 N ATOM 2755 CA GLU C 78 5.683 24.459 14.527 1.00 8.59 C ANISOU 2755 CA GLU C 78 1723 634 906 245 156 0 C ATOM 2756 C GLU C 78 5.591 24.076 13.042 1.00 9.53 C ANISOU 2756 C GLU C 78 2324 381 916 170 35 -31 C ATOM 2757 O GLU C 78 4.694 24.486 12.307 1.00 10.55 O ANISOU 2757 O GLU C 78 1767 1298 942 -221 90 98 O ATOM 2758 CB GLU C 78 4.935 23.478 15.412 1.00 8.00 C ANISOU 2758 CB GLU C 78 1593 594 852 -81 -85 -94 C ATOM 2759 CG GLU C 78 5.275 22.032 15.232 1.00 7.99 C ANISOU 2759 CG GLU C 78 1277 650 1110 103 222 -275 C ATOM 2760 CD GLU C 78 6.669 21.574 15.637 1.00 12.55 C ANISOU 2760 CD GLU C 78 1270 1104 2396 -41 -73 335 C ATOM 2761 OE1 GLU C 78 7.623 22.051 14.953 1.00 10.48 O ANISOU 2761 OE1 GLU C 78 1280 706 1995 391 172 29 O ATOM 2762 OE2 GLU C 78 6.860 20.739 16.543 1.00 10.59 O ANISOU 2762 OE2 GLU C 78 1373 1086 1564 -256 -267 -106 O ATOM 2763 N MET C 79 6.524 23.214 12.637 1.00 12.42 N ANISOU 2763 N MET C 79 2703 769 1246 365 -22 -437 N ATOM 2764 CA MET C 79 6.443 22.733 11.269 1.00 12.59 C ANISOU 2764 CA MET C 79 1847 1726 1210 387 152 -510 C ATOM 2765 C MET C 79 5.245 21.800 11.117 1.00 16.27 C ANISOU 2765 C MET C 79 3167 1799 1216 -412 -170 -279 C ATOM 2766 O MET C 79 4.830 21.146 12.072 1.00 15.79 O ANISOU 2766 O MET C 79 2613 1950 1438 -80 5 -134 O ATOM 2767 CB MET C 79 7.794 22.119 10.939 1.00 24.26 C ANISOU 2767 CB MET C 79 2574 4333 2310 1881 -161 -1291 C ATOM 2768 CG MET C 79 8.117 20.762 11.439 1.00 29.26 C ANISOU 2768 CG MET C 79 3060 4274 3783 2479 -226 -1483 C ATOM 2769 SD MET C 79 9.834 20.374 10.901 1.00 20.56 S ANISOU 2769 SD MET C 79 2766 2438 2607 1217 400 461 S ATOM 2770 CE MET C 79 9.500 19.668 9.308 1.00 17.25 C ANISOU 2770 CE MET C 79 1800 1476 3280 -143 921 6 C ATOM 2771 N ASP C 80 4.688 21.784 9.914 1.00 14.35 N ANISOU 2771 N ASP C 80 2522 1491 1441 208 -359 -284 N ATOM 2772 CA ASP C 80 3.519 20.990 9.564 1.00 15.29 C ANISOU 2772 CA ASP C 80 2004 1744 2061 454 -330 -226 C ATOM 2773 C ASP C 80 3.950 19.615 9.075 1.00 15.92 C ANISOU 2773 C ASP C 80 2786 1357 1905 -316 627 -144 C ATOM 2774 O ASP C 80 4.253 19.422 7.871 1.00 21.15 O ANISOU 2774 O ASP C 80 4169 2283 1582 785 155 -65 O ATOM 2775 CB ASP C 80 2.716 21.679 8.450 1.00 19.34 C ANISOU 2775 CB ASP C 80 2454 2981 1914 575 -509 -125 C ATOM 2776 CG ASP C 80 1.382 20.993 8.177 1.00 29.10 C ANISOU 2776 CG ASP C 80 3459 4892 2705 -440 -1642 -337 C ATOM 2777 OD1 ASP C 80 0.931 20.178 9.014 1.00 32.37 O ANISOU 2777 OD1 ASP C 80 2969 3393 5936 -238 -1124 353 O ATOM 2778 OD2 ASP C 80 0.783 21.278 7.120 1.00 58.04 O ANISOU 2778 OD2 ASP C 80 6618 10295 5141 -1482 -4501 1380 O ATOM 2779 N VAL C 81 4.015 18.655 9.957 1.00 13.76 N ANISOU 2779 N VAL C 81 2496 1437 1296 25 -223 -499 N ATOM 2780 CA VAL C 81 4.437 17.312 9.535 1.00 13.96 C ANISOU 2780 CA VAL C 81 1968 1363 1974 5 -625 -537 C ATOM 2781 C VAL C 81 3.190 16.494 9.267 1.00 16.20 C ANISOU 2781 C VAL C 81 2126 1805 2223 -230 -249 -887 C ATOM 2782 O VAL C 81 2.268 16.627 10.074 1.00 17.47 O ANISOU 2782 O VAL C 81 2130 1969 2538 -145 -142 -1002 O ATOM 2783 CB VAL C 81 5.313 16.717 10.646 1.00 13.22 C ANISOU 2783 CB VAL C 81 2193 1216 1612 -717 -141 476 C ATOM 2784 CG1 VAL C 81 5.624 15.249 10.469 1.00 15.14 C ANISOU 2784 CG1 VAL C 81 3094 990 1671 -951 -805 537 C ATOM 2785 CG2 VAL C 81 6.628 17.492 10.723 1.00 11.66 C ANISOU 2785 CG2 VAL C 81 2009 829 1591 -376 -587 -169 C ATOM 2786 N THR C 82 3.151 15.722 8.190 1.00 16.40 N ANISOU 2786 N THR C 82 2503 1660 2067 -498 -301 -761 N ATOM 2787 CA THR C 82 2.008 14.847 7.944 1.00 16.34 C ANISOU 2787 CA THR C 82 2123 1911 2174 -287 -598 -623 C ATOM 2788 C THR C 82 1.838 13.858 9.075 1.00 16.37 C ANISOU 2788 C THR C 82 2094 1901 2227 -595 -357 -736 C ATOM 2789 O THR C 82 2.771 13.151 9.448 1.00 19.96 O ANISOU 2789 O THR C 82 2518 2766 2302 -544 -784 52 O ATOM 2790 CB THR C 82 2.281 14.195 6.569 1.00 21.46 C ANISOU 2790 CB THR C 82 3187 2984 1984 -998 -848 -900 C ATOM 2791 OG1 THR C 82 2.424 15.288 5.639 1.00 21.21 O ANISOU 2791 OG1 THR C 82 2882 2899 2276 -44 108 -818 O ATOM 2792 CG2 THR C 82 1.141 13.289 6.134 1.00 23.86 C ANISOU 2792 CG2 THR C 82 2665 3905 2496 -1147 -207 -1547 C ATOM 2793 N GLY C 83 0.647 13.745 9.663 1.00 21.23 N ANISOU 2793 N GLY C 83 2595 3462 2011 -779 118 -1267 N ATOM 2794 CA GLY C 83 0.475 12.892 10.837 1.00 23.66 C ANISOU 2794 CA GLY C 83 3296 3704 1988 -1262 364 -1329 C ATOM 2795 C GLY C 83 1.118 13.439 12.096 1.00 22.65 C ANISOU 2795 C GLY C 83 3452 2793 2360 -1075 -522 -625 C ATOM 2796 O GLY C 83 1.147 12.711 13.105 1.00 22.66 O ANISOU 2796 O GLY C 83 2657 3505 2446 -1632 6 -261 O ATOM 2797 N GLY C 84 1.604 14.683 12.149 1.00 17.77 N ANISOU 2797 N GLY C 84 2091 2572 2088 -489 6 -750 N ATOM 2798 CA GLY C 84 2.013 15.326 13.382 1.00 14.94 C ANISOU 2798 CA GLY C 84 1990 1779 1910 -201 -18 -372 C ATOM 2799 C GLY C 84 0.810 15.609 14.267 1.00 13.76 C ANISOU 2799 C GLY C 84 1760 1648 1819 -447 -216 -435 C ATOM 2800 O GLY C 84 -0.323 15.768 13.819 1.00 15.50 O ANISOU 2800 O GLY C 84 1769 2278 1842 -419 -250 -252 O ATOM 2801 N LEU C 85 1.128 15.671 15.569 1.00 12.74 N ANISOU 2801 N LEU C 85 1980 1064 1795 55 -243 -433 N ATOM 2802 CA LEU C 85 0.080 15.936 16.550 1.00 12.52 C ANISOU 2802 CA LEU C 85 1779 1248 1730 -62 -202 -2 C ATOM 2803 C LEU C 85 -0.682 17.213 16.240 1.00 10.72 C ANISOU 2803 C LEU C 85 1418 1004 1651 -263 6 -224 C ATOM 2804 O LEU C 85 -0.067 18.267 16.065 1.00 13.00 O ANISOU 2804 O LEU C 85 1380 1142 2417 -261 -146 -14 O ATOM 2805 CB LEU C 85 0.751 16.012 17.921 1.00 16.77 C ANISOU 2805 CB LEU C 85 2485 2282 1606 -118 -276 195 C ATOM 2806 CG LEU C 85 -0.243 16.016 19.083 1.00 16.12 C ANISOU 2806 CG LEU C 85 2761 1698 1666 -1009 -130 155 C ATOM 2807 CD1 LEU C 85 -1.208 14.853 18.955 1.00 22.10 C ANISOU 2807 CD1 LEU C 85 3631 1375 3390 -1159 175 -318 C ATOM 2808 CD2 LEU C 85 0.449 16.040 20.452 1.00 16.22 C ANISOU 2808 CD2 LEU C 85 2198 2252 1714 172 -136 544 C ATOM 2809 N LYS C 86 -1.996 17.222 16.133 1.00 14.37 N ANISOU 2809 N LYS C 86 1453 874 3134 -195 -145 -696 N ATOM 2810 CA LYS C 86 -2.736 18.466 15.940 1.00 12.35 C ANISOU 2810 CA LYS C 86 1386 900 2407 -251 7 -364 C ATOM 2811 C LYS C 86 -2.927 19.261 17.228 1.00 11.29 C ANISOU 2811 C LYS C 86 1062 889 2338 -98 86 -212 C ATOM 2812 O LYS C 86 -2.802 18.730 18.344 1.00 13.66 O ANISOU 2812 O LYS C 86 1618 1189 2384 -395 2 -31 O ATOM 2813 CB LYS C 86 -4.147 18.155 15.411 1.00 23.87 C ANISOU 2813 CB LYS C 86 2194 3363 3513 75 -1543 -541 C ATOM 2814 CG LYS C 86 -4.150 17.403 14.089 1.00 33.63 C ANISOU 2814 CG LYS C 86 3273 5158 4349 -675 -1725 -1720 C ATOM 2815 CD LYS C 86 -5.618 17.100 13.726 1.00 39.20 C ANISOU 2815 CD LYS C 86 3247 6807 4840 -1247 -1353 -2348 C ATOM 2816 CE LYS C 86 -6.475 17.309 14.971 1.00 49.23 C ANISOU 2816 CE LYS C 86 4325 8299 6084 -1049 -65 -2319 C ATOM 2817 NZ LYS C 86 -7.826 17.874 14.647 1.00 61.23 N ANISOU 2817 NZ LYS C 86 6001 10579 6684 1466 1196 -545 N ATOM 2818 N LYS C 87 -3.282 20.525 17.061 1.00 12.38 N ANISOU 2818 N LYS C 87 1289 878 2537 -50 -189 -379 N ATOM 2819 CA LYS C 87 -3.659 21.433 18.155 1.00 10.46 C ANISOU 2819 CA LYS C 87 1070 717 2187 -239 -230 -183 C ATOM 2820 C LYS C 87 -2.674 21.361 19.302 1.00 10.11 C ANISOU 2820 C LYS C 87 1177 461 2203 -215 -199 186 C ATOM 2821 O LYS C 87 -3.098 21.215 20.457 1.00 10.98 O ANISOU 2821 O LYS C 87 976 927 2267 -226 -241 272 O ATOM 2822 CB LYS C 87 -5.085 21.124 18.648 1.00 11.60 C ANISOU 2822 CB LYS C 87 1135 882 2391 -306 -112 48 C ATOM 2823 CG LYS C 87 -6.136 21.450 17.609 1.00 17.70 C ANISOU 2823 CG LYS C 87 1235 2269 3223 -469 -753 -297 C ATOM 2824 CD LYS C 87 -7.565 21.246 18.162 1.00 20.14 C ANISOU 2824 CD LYS C 87 1134 2195 4324 -223 -509 -785 C ATOM 2825 CE LYS C 87 -8.478 21.610 16.998 1.00 24.79 C ANISOU 2825 CE LYS C 87 1211 3517 4692 -546 -864 -620 C ATOM 2826 NZ LYS C 87 -8.503 20.438 16.047 1.00 40.50 N ANISOU 2826 NZ LYS C 87 2984 6665 5741 -1864 -753 -2931 N ATOM 2827 N CYS C 88 -1.401 21.494 18.965 1.00 10.37 N ANISOU 2827 N CYS C 88 1091 712 2138 -338 -239 146 N ATOM 2828 CA CYS C 88 -0.376 21.252 19.967 1.00 10.09 C ANISOU 2828 CA CYS C 88 1185 722 1926 -255 -152 -78 C ATOM 2829 C CYS C 88 0.479 22.471 20.229 1.00 11.26 C ANISOU 2829 C CYS C 88 1118 1133 2029 -427 61 -288 C ATOM 2830 O CYS C 88 0.936 23.101 19.269 1.00 10.75 O ANISOU 2830 O CYS C 88 1275 827 1982 -461 -228 -160 O ATOM 2831 CB CYS C 88 0.514 20.112 19.474 1.00 11.53 C ANISOU 2831 CB CYS C 88 939 819 2622 -209 104 135 C ATOM 2832 SG CYS C 88 1.862 19.616 20.597 1.00 12.12 S ANISOU 2832 SG CYS C 88 1457 1019 2131 -107 -92 17 S ATOM 2833 N ILE C 89 0.687 22.697 21.538 1.00 9.97 N ANISOU 2833 N ILE C 89 993 759 2034 -392 -120 -72 N ATOM 2834 CA ILE C 89 1.542 23.776 22.002 1.00 8.73 C ANISOU 2834 CA ILE C 89 489 537 2291 -147 48 -203 C ATOM 2835 C ILE C 89 2.802 23.145 22.597 1.00 9.29 C ANISOU 2835 C ILE C 89 634 1006 1889 26 138 13 C ATOM 2836 O ILE C 89 2.672 22.294 23.471 1.00 10.97 O ANISOU 2836 O ILE C 89 1283 961 1923 -329 -142 41 O ATOM 2837 CB AILE C 89 0.851 24.651 23.067 0.63 11.75 C ANISOU 2837 CB AILE C 89 800 800 2864 -87 300 -489 C ATOM 2838 CB BILE C 89 0.813 24.684 23.003 0.37 11.65 C ANISOU 2838 CB BILE C 89 861 796 2769 48 180 -422 C ATOM 2839 CG1AILE C 89 -0.417 25.359 22.590 0.63 13.21 C ANISOU 2839 CG1AILE C 89 946 911 3163 132 364 -459 C ATOM 2840 CG1BILE C 89 -0.473 25.303 22.446 0.37 12.07 C ANISOU 2840 CG1BILE C 89 598 698 3291 -125 101 -575 C ATOM 2841 CG2AILE C 89 1.879 25.647 23.597 0.63 9.11 C ANISOU 2841 CG2AILE C 89 1723 1052 688 -747 218 244 C ATOM 2842 CG2BILE C 89 1.747 25.779 23.492 0.37 10.99 C ANISOU 2842 CG2BILE C 89 836 656 2684 352 -255 -456 C ATOM 2843 CD1AILE C 89 -1.677 24.731 23.164 0.63 13.33 C ANISOU 2843 CD1AILE C 89 690 388 3986 -374 -780 190 C ATOM 2844 CD1BILE C 89 -1.402 25.822 23.523 0.37 12.77 C ANISOU 2844 CD1BILE C 89 1575 6 3273 580 468 189 C ATOM 2845 N ARG C 90 3.968 23.579 22.120 1.00 8.59 N ANISOU 2845 N ARG C 90 500 963 1802 -51 62 -374 N ATOM 2846 CA ARG C 90 5.234 23.051 22.628 1.00 7.97 C ANISOU 2846 CA ARG C 90 527 743 1759 -69 107 -374 C ATOM 2847 C ARG C 90 5.996 24.181 23.291 1.00 7.22 C ANISOU 2847 C ARG C 90 900 372 1471 80 -269 -65 C ATOM 2848 O ARG C 90 5.881 25.333 22.860 1.00 9.39 O ANISOU 2848 O ARG C 90 1753 512 1303 218 -345 96 O ATOM 2849 CB ARG C 90 6.100 22.430 21.527 1.00 7.10 C ANISOU 2849 CB ARG C 90 680 454 1563 -143 274 -115 C ATOM 2850 CG ARG C 90 5.474 21.125 20.972 1.00 9.30 C ANISOU 2850 CG ARG C 90 1470 547 1515 -288 -15 -166 C ATOM 2851 CD ARG C 90 6.172 20.722 19.698 1.00 11.98 C ANISOU 2851 CD ARG C 90 1267 1175 2109 -705 243 -792 C ATOM 2852 NE ARG C 90 5.854 19.445 19.057 1.00 9.82 N ANISOU 2852 NE ARG C 90 671 982 2079 -275 -41 -588 N ATOM 2853 CZ ARG C 90 4.881 19.182 18.206 1.00 8.16 C ANISOU 2853 CZ ARG C 90 598 613 1887 -391 37 -239 C ATOM 2854 NH1 ARG C 90 4.014 20.164 17.949 1.00 10.42 N ANISOU 2854 NH1 ARG C 90 1151 1121 1686 163 -113 -411 N ATOM 2855 NH2 ARG C 90 4.691 18.003 17.636 1.00 10.53 N ANISOU 2855 NH2 ARG C 90 1658 551 1791 -465 -101 -143 N ATOM 2856 N VAL C 91 6.740 23.861 24.335 1.00 8.88 N ANISOU 2856 N VAL C 91 1272 477 1625 102 -465 108 N ATOM 2857 CA VAL C 91 7.523 24.836 25.072 1.00 10.60 C ANISOU 2857 CA VAL C 91 1033 1400 1597 -127 -89 -616 C ATOM 2858 C VAL C 91 8.998 24.472 25.093 1.00 7.62 C ANISOU 2858 C VAL C 91 1115 737 1041 -163 97 -294 C ATOM 2859 O VAL C 91 9.322 23.291 25.172 1.00 9.62 O ANISOU 2859 O VAL C 91 1245 741 1669 -332 156 -85 O ATOM 2860 CB VAL C 91 7.080 24.936 26.572 1.00 13.56 C ANISOU 2860 CB VAL C 91 1468 1704 1979 -398 660 -894 C ATOM 2861 CG1 VAL C 91 7.972 25.910 27.313 1.00 22.77 C ANISOU 2861 CG1 VAL C 91 3583 3369 1701 -1087 -855 -784 C ATOM 2862 CG2 VAL C 91 5.606 25.326 26.662 1.00 15.75 C ANISOU 2862 CG2 VAL C 91 1942 1760 2284 421 694 -183 C ATOM 2863 N MET C 92 9.890 25.469 24.947 1.00 7.83 N ANISOU 2863 N MET C 92 1048 594 1332 -102 64 -256 N ATOM 2864 CA MET C 92 11.306 25.363 25.249 1.00 8.51 C ANISOU 2864 CA MET C 92 1131 754 1348 -91 -8 -455 C ATOM 2865 C MET C 92 11.602 26.444 26.293 1.00 7.14 C ANISOU 2865 C MET C 92 1170 450 1092 268 -289 -88 C ATOM 2866 O MET C 92 11.662 27.628 25.955 1.00 9.62 O ANISOU 2866 O MET C 92 1716 484 1456 -76 -292 -16 O ATOM 2867 CB MET C 92 12.170 25.513 23.984 1.00 10.79 C ANISOU 2867 CB MET C 92 1011 1712 1376 287 41 -323 C ATOM 2868 CG MET C 92 13.632 25.410 24.435 1.00 11.45 C ANISOU 2868 CG MET C 92 1014 1399 1938 320 -30 -13 C ATOM 2869 SD MET C 92 14.211 23.733 24.710 1.00 10.91 S ANISOU 2869 SD MET C 92 1572 1333 1241 263 -148 -77 S ATOM 2870 CE MET C 92 14.388 23.145 23.027 1.00 11.35 C ANISOU 2870 CE MET C 92 1445 1734 1131 -92 -230 -236 C ATOM 2871 N MET C 93 11.792 26.052 27.552 1.00 8.77 N ANISOU 2871 N MET C 93 1144 1358 829 -152 100 141 N ATOM 2872 CA MET C 93 12.041 26.987 28.646 1.00 11.33 C ANISOU 2872 CA MET C 93 1444 1832 1028 236 182 -303 C ATOM 2873 C MET C 93 13.529 26.936 28.976 1.00 10.53 C ANISOU 2873 C MET C 93 1691 761 1549 141 -335 -462 C ATOM 2874 O MET C 93 13.986 25.851 29.351 1.00 14.85 O ANISOU 2874 O MET C 93 2034 733 2876 28 -663 -111 O ATOM 2875 CB MET C 93 11.159 26.648 29.870 1.00 12.20 C ANISOU 2875 CB MET C 93 2396 786 1453 1029 852 -133 C ATOM 2876 CG MET C 93 11.352 27.633 31.029 1.00 15.61 C ANISOU 2876 CG MET C 93 3547 839 1546 1194 1096 -317 C ATOM 2877 SD MET C 93 10.567 27.148 32.552 1.00 15.52 S ANISOU 2877 SD MET C 93 2274 2446 1179 -100 190 -394 S ATOM 2878 CE MET C 93 8.860 27.035 32.071 1.00 20.49 C ANISOU 2878 CE MET C 93 2749 1557 3480 -848 -899 1082 C ATOM 2879 N THR C 94 14.272 28.047 28.814 1.00 8.05 N ANISOU 2879 N THR C 94 1542 705 811 359 -206 -215 N ATOM 2880 CA THR C 94 15.719 28.039 29.056 1.00 9.24 C ANISOU 2880 CA THR C 94 1493 1560 458 89 24 -179 C ATOM 2881 C THR C 94 16.015 28.548 30.457 1.00 8.24 C ANISOU 2881 C THR C 94 1621 1114 397 71 -109 88 C ATOM 2882 O THR C 94 15.640 29.717 30.718 1.00 9.33 O ANISOU 2882 O THR C 94 1646 1216 682 231 -128 -128 O ATOM 2883 CB THR C 94 16.398 28.926 27.996 1.00 9.14 C ANISOU 2883 CB THR C 94 1526 1577 370 799 189 74 C ATOM 2884 OG1 THR C 94 15.976 28.571 26.691 1.00 9.83 O ANISOU 2884 OG1 THR C 94 1896 1275 565 606 -147 66 O ATOM 2885 CG2 THR C 94 17.925 28.745 28.070 1.00 8.45 C ANISOU 2885 CG2 THR C 94 1393 570 1248 66 2 98 C ATOM 2886 N VAL C 95 16.672 27.737 31.275 1.00 8.05 N ANISOU 2886 N VAL C 95 1367 1175 518 -47 -159 104 N ATOM 2887 CA VAL C 95 16.779 28.083 32.690 1.00 8.73 C ANISOU 2887 CA VAL C 95 1494 1388 436 80 -139 79 C ATOM 2888 C VAL C 95 18.211 27.921 33.142 1.00 9.21 C ANISOU 2888 C VAL C 95 1497 1430 572 222 -226 -419 C ATOM 2889 O VAL C 95 18.988 27.131 32.663 1.00 11.02 O ANISOU 2889 O VAL C 95 1715 1194 1281 278 -408 -563 O ATOM 2890 CB VAL C 95 15.851 27.239 33.582 1.00 10.50 C ANISOU 2890 CB VAL C 95 1882 1408 700 -111 400 -323 C ATOM 2891 CG1 VAL C 95 14.429 27.286 33.034 1.00 13.12 C ANISOU 2891 CG1 VAL C 95 1647 1948 1388 10 599 -108 C ATOM 2892 CG2 VAL C 95 16.353 25.819 33.710 1.00 13.17 C ANISOU 2892 CG2 VAL C 95 1976 1513 1517 -110 466 266 C ATOM 2893 N GLN C 96 18.573 28.705 34.156 1.00 11.45 N ANISOU 2893 N GLN C 96 1821 2079 450 187 -236 -600 N ATOM 2894 CA GLN C 96 19.823 28.536 34.905 1.00 12.80 C ANISOU 2894 CA GLN C 96 2144 1812 908 -415 -693 -18 C ATOM 2895 C GLN C 96 19.585 27.475 35.967 1.00 12.67 C ANISOU 2895 C GLN C 96 1238 1997 1578 -230 -331 313 C ATOM 2896 O GLN C 96 18.624 27.588 36.761 1.00 13.45 O ANISOU 2896 O GLN C 96 1836 2208 1068 190 -291 -30 O ATOM 2897 CB GLN C 96 20.283 29.856 35.539 1.00 15.84 C ANISOU 2897 CB GLN C 96 2772 1650 1598 -233 -1187 -33 C ATOM 2898 CG GLN C 96 21.610 29.781 36.264 1.00 19.78 C ANISOU 2898 CG GLN C 96 2539 2447 2531 -600 -1290 -504 C ATOM 2899 CD GLN C 96 22.027 31.077 36.930 1.00 19.47 C ANISOU 2899 CD GLN C 96 3117 2167 2113 -295 -1480 -343 C ATOM 2900 OE1 GLN C 96 23.183 31.493 36.817 1.00 34.92 O ANISOU 2900 OE1 GLN C 96 3870 4648 4749 -1918 -1141 -2130 O ATOM 2901 NE2 GLN C 96 21.092 31.703 37.645 1.00 29.93 N ANISOU 2901 NE2 GLN C 96 4427 4351 2596 700 -1496 -1513 N ATOM 2902 N THR C 97 20.426 26.435 35.949 1.00 14.13 N ANISOU 2902 N THR C 97 2127 2363 879 371 -117 211 N ATOM 2903 CA THR C 97 20.219 25.313 36.871 1.00 15.00 C ANISOU 2903 CA THR C 97 2305 1959 1436 305 -59 102 C ATOM 2904 C THR C 97 21.465 24.432 36.935 1.00 16.82 C ANISOU 2904 C THR C 97 2608 1755 2028 453 -716 -422 C ATOM 2905 O THR C 97 22.165 24.312 35.933 1.00 19.25 O ANISOU 2905 O THR C 97 2213 2043 3060 616 -20 199 O ATOM 2906 CB THR C 97 19.003 24.475 36.461 1.00 16.23 C ANISOU 2906 CB THR C 97 2450 2477 1241 103 -309 257 C ATOM 2907 OG1 THR C 97 18.872 23.376 37.349 1.00 15.91 O ANISOU 2907 OG1 THR C 97 1835 2105 2105 476 -80 446 O ATOM 2908 CG2 THR C 97 19.159 23.860 35.067 1.00 14.90 C ANISOU 2908 CG2 THR C 97 1874 1900 1887 303 55 -178 C ATOM 2909 N ASP C 98 21.684 23.868 38.122 1.00 19.97 N ANISOU 2909 N ASP C 98 2724 2487 2376 109 -1333 -54 N ATOM 2910 CA ASP C 98 22.790 22.944 38.303 1.00 20.04 C ANISOU 2910 CA ASP C 98 2765 2351 2498 -3 -1363 101 C ATOM 2911 C ASP C 98 22.286 21.507 38.170 1.00 18.83 C ANISOU 2911 C ASP C 98 2508 2395 2251 -110 -520 370 C ATOM 2912 O ASP C 98 23.080 20.566 38.351 1.00 21.00 O ANISOU 2912 O ASP C 98 3038 2367 2575 1 -1130 400 O ATOM 2913 CB ASP C 98 23.503 23.236 39.629 1.00 26.81 C ANISOU 2913 CB ASP C 98 4048 3121 3017 1228 -2169 -770 C ATOM 2914 CG ASP C 98 22.644 23.099 40.852 1.00 31.85 C ANISOU 2914 CG ASP C 98 5785 3883 2432 1197 -2090 -75 C ATOM 2915 OD1 ASP C 98 21.448 22.792 40.688 1.00 38.74 O ANISOU 2915 OD1 ASP C 98 6271 4649 3798 -637 -546 -727 O ATOM 2916 OD2 ASP C 98 23.141 23.300 41.989 1.00 48.51 O ANISOU 2916 OD2 ASP C 98 9725 6147 2558 520 -3073 108 O ATOM 2917 N VAL C 99 21.014 21.305 37.838 1.00 16.11 N ANISOU 2917 N VAL C 99 2428 2281 1412 -93 -191 -123 N ATOM 2918 CA VAL C 99 20.484 19.947 37.702 1.00 15.00 C ANISOU 2918 CA VAL C 99 2197 2083 1420 24 229 380 C ATOM 2919 C VAL C 99 21.069 19.255 36.477 1.00 12.22 C ANISOU 2919 C VAL C 99 1961 1892 791 209 -709 386 C ATOM 2920 O VAL C 99 21.081 19.815 35.373 1.00 15.63 O ANISOU 2920 O VAL C 99 2423 2543 972 345 -531 683 O ATOM 2921 CB VAL C 99 18.938 19.949 37.611 1.00 15.12 C ANISOU 2921 CB VAL C 99 2277 2103 1364 0 -173 242 C ATOM 2922 CG1 VAL C 99 18.358 18.581 37.325 1.00 15.25 C ANISOU 2922 CG1 VAL C 99 2145 1614 2037 159 31 875 C ATOM 2923 CG2 VAL C 99 18.376 20.483 38.926 1.00 17.59 C ANISOU 2923 CG2 VAL C 99 2150 2815 1721 634 46 274 C ATOM 2924 N PRO C 100 21.563 18.030 36.572 1.00 14.70 N ANISOU 2924 N PRO C 100 2217 1872 1497 273 -578 338 N ATOM 2925 CA PRO C 100 22.108 17.325 35.426 1.00 17.34 C ANISOU 2925 CA PRO C 100 2522 2292 1774 700 -778 17 C ATOM 2926 C PRO C 100 21.111 17.173 34.289 1.00 15.05 C ANISOU 2926 C PRO C 100 2347 1952 1421 -280 -371 434 C ATOM 2927 O PRO C 100 19.889 17.073 34.506 1.00 15.90 O ANISOU 2927 O PRO C 100 2314 1956 1772 -275 -330 469 O ATOM 2928 CB PRO C 100 22.434 15.927 35.989 1.00 19.75 C ANISOU 2928 CB PRO C 100 2839 2490 2175 1086 -352 312 C ATOM 2929 CG PRO C 100 22.661 16.165 37.443 1.00 22.15 C ANISOU 2929 CG PRO C 100 3687 2605 2125 1474 -391 457 C ATOM 2930 CD PRO C 100 21.679 17.251 37.832 1.00 19.54 C ANISOU 2930 CD PRO C 100 3539 2115 1768 1313 -805 506 C ATOM 2931 N GLN C 101 21.643 17.147 33.077 1.00 13.67 N ANISOU 2931 N GLN C 101 2579 1071 1542 -144 -194 -28 N ATOM 2932 CA GLN C 101 20.813 17.075 31.898 1.00 13.73 C ANISOU 2932 CA GLN C 101 2288 1508 1421 -63 -48 -184 C ATOM 2933 C GLN C 101 19.847 15.883 31.954 1.00 13.40 C ANISOU 2933 C GLN C 101 2079 1338 1674 122 -214 18 C ATOM 2934 O GLN C 101 18.701 16.025 31.522 1.00 13.63 O ANISOU 2934 O GLN C 101 2076 1363 1742 179 -230 230 O ATOM 2935 CB GLN C 101 21.733 16.996 30.671 1.00 14.81 C ANISOU 2935 CB GLN C 101 2191 1922 1513 259 -33 269 C ATOM 2936 CG GLN C 101 20.929 16.973 29.373 1.00 13.86 C ANISOU 2936 CG GLN C 101 2183 1720 1364 164 108 165 C ATOM 2937 CD GLN C 101 21.883 16.958 28.191 1.00 12.79 C ANISOU 2937 CD GLN C 101 1801 1533 1526 1032 26 1051 C ATOM 2938 OE1 GLN C 101 22.130 17.978 27.543 1.00 14.37 O ANISOU 2938 OE1 GLN C 101 2515 1247 1699 174 -47 605 O ATOM 2939 NE2 GLN C 101 22.452 15.785 27.928 1.00 11.43 N ANISOU 2939 NE2 GLN C 101 1304 1228 1812 446 -227 512 N ATOM 2940 N ASP C 102 20.345 14.749 32.470 1.00 15.71 N ANISOU 2940 N ASP C 102 1691 1900 2376 125 31 866 N ATOM 2941 CA ASP C 102 19.496 13.555 32.520 1.00 15.37 C ANISOU 2941 CA ASP C 102 2024 1673 2142 236 251 814 C ATOM 2942 C ASP C 102 18.516 13.618 33.695 1.00 16.04 C ANISOU 2942 C ASP C 102 1891 1985 2218 -217 260 246 C ATOM 2943 O ASP C 102 17.748 12.661 33.881 1.00 19.54 O ANISOU 2943 O ASP C 102 2624 1856 2944 -276 726 515 O ATOM 2944 CB ASP C 102 20.326 12.290 32.603 1.00 20.26 C ANISOU 2944 CB ASP C 102 2255 1826 3619 477 -85 69 C ATOM 2945 CG ASP C 102 21.151 12.135 33.875 1.00 21.82 C ANISOU 2945 CG ASP C 102 2084 1944 4263 906 -337 577 C ATOM 2946 OD1 ASP C 102 21.120 12.970 34.800 1.00 22.53 O ANISOU 2946 OD1 ASP C 102 2912 2551 3100 378 -332 930 O ATOM 2947 OD2 ASP C 102 21.871 11.101 33.947 1.00 31.96 O ANISOU 2947 OD2 ASP C 102 3004 2792 6348 1836 162 1399 O ATOM 2948 N GLN C 103 18.483 14.686 34.486 1.00 15.48 N ANISOU 2948 N GLN C 103 2509 1641 1730 387 -256 664 N ATOM 2949 CA GLN C 103 17.471 14.711 35.543 1.00 14.73 C ANISOU 2949 CA GLN C 103 2917 1261 1417 495 -265 735 C ATOM 2950 C GLN C 103 16.461 15.823 35.316 1.00 16.37 C ANISOU 2950 C GLN C 103 2100 1949 2171 379 -235 1189 C ATOM 2951 O GLN C 103 15.519 15.952 36.106 1.00 17.83 O ANISOU 2951 O GLN C 103 2360 2396 2018 447 -202 853 O ATOM 2952 CB GLN C 103 18.133 14.891 36.909 1.00 19.54 C ANISOU 2952 CB GLN C 103 3481 2356 1587 1006 -657 668 C ATOM 2953 CG GLN C 103 18.741 13.577 37.427 1.00 26.85 C ANISOU 2953 CG GLN C 103 4300 3059 2841 1394 -1364 1186 C ATOM 2954 CD GLN C 103 19.604 13.775 38.642 1.00 33.65 C ANISOU 2954 CD GLN C 103 5449 4359 2975 1274 -1949 1532 C ATOM 2955 OE1 GLN C 103 19.179 14.269 39.687 1.00 49.18 O ANISOU 2955 OE1 GLN C 103 6251 8332 4104 1938 -2641 -1077 O ATOM 2956 NE2 GLN C 103 20.859 13.345 38.516 1.00 39.57 N ANISOU 2956 NE2 GLN C 103 5260 5022 4751 1225 -3029 -636 N ATOM 2957 N ILE C 104 16.656 16.640 34.277 1.00 15.45 N ANISOU 2957 N ILE C 104 2389 1489 1991 500 -405 969 N ATOM 2958 CA ILE C 104 15.659 17.687 33.970 1.00 13.06 C ANISOU 2958 CA ILE C 104 1537 1472 1953 292 289 957 C ATOM 2959 C ILE C 104 14.318 16.997 33.738 1.00 14.47 C ANISOU 2959 C ILE C 104 1834 1105 2560 99 407 656 C ATOM 2960 O ILE C 104 14.316 15.911 33.140 1.00 14.61 O ANISOU 2960 O ILE C 104 2074 1522 1956 595 -134 423 O ATOM 2961 CB ILE C 104 16.123 18.528 32.781 1.00 12.08 C ANISOU 2961 CB ILE C 104 1561 1214 1817 248 101 891 C ATOM 2962 CG1 ILE C 104 17.478 19.238 33.038 1.00 12.04 C ANISOU 2962 CG1 ILE C 104 1751 1691 1132 -41 18 723 C ATOM 2963 CG2 ILE C 104 15.061 19.545 32.402 1.00 11.00 C ANISOU 2963 CG2 ILE C 104 2045 921 1215 415 -501 12 C ATOM 2964 CD1 ILE C 104 17.286 20.396 34.013 1.00 15.49 C ANISOU 2964 CD1 ILE C 104 2138 2152 1595 -75 231 297 C ATOM 2965 N ARG C 105 13.206 17.605 34.173 1.00 12.74 N ANISOU 2965 N ARG C 105 1548 1300 1991 -136 147 195 N ATOM 2966 CA ARG C 105 11.915 16.941 34.028 1.00 13.31 C ANISOU 2966 CA ARG C 105 1766 1781 1509 -457 -136 1002 C ATOM 2967 C ARG C 105 11.100 17.653 32.953 1.00 12.38 C ANISOU 2967 C ARG C 105 2093 1214 1398 -191 -146 633 C ATOM 2968 O ARG C 105 10.543 18.756 33.109 1.00 14.05 O ANISOU 2968 O ARG C 105 2082 1539 1717 73 -42 378 O ATOM 2969 CB ARG C 105 11.175 16.828 35.367 1.00 19.17 C ANISOU 2969 CB ARG C 105 2470 3151 1663 -642 146 1483 C ATOM 2970 CG ARG C 105 11.909 15.883 36.330 1.00 21.72 C ANISOU 2970 CG ARG C 105 2691 4085 1477 -668 -221 1626 C ATOM 2971 CD ARG C 105 11.128 15.838 37.643 1.00 31.82 C ANISOU 2971 CD ARG C 105 4830 5295 1963 -1628 769 2242 C ATOM 2972 NE ARG C 105 10.036 14.887 37.519 1.00 36.80 N ANISOU 2972 NE ARG C 105 6113 5367 2502 -2430 1471 1816 N ATOM 2973 CZ ARG C 105 8.821 14.842 38.016 1.00 34.69 C ANISOU 2973 CZ ARG C 105 6302 4872 2007 -3255 1628 251 C ATOM 2974 NH1 ARG C 105 8.311 15.773 38.806 1.00 44.16 N ANISOU 2974 NH1 ARG C 105 8669 6848 1262 -3071 2119 -668 N ATOM 2975 NH2 ARG C 105 8.069 13.790 37.691 1.00 40.23 N ANISOU 2975 NH2 ARG C 105 6568 4178 4538 -2847 -304 1115 N ATOM 2976 N HIS C 106 11.092 16.970 31.804 1.00 12.94 N ANISOU 2976 N HIS C 106 1907 1337 1672 -150 -442 312 N ATOM 2977 CA HIS C 106 10.353 17.465 30.651 1.00 12.24 C ANISOU 2977 CA HIS C 106 1482 1523 1647 -155 -288 293 C ATOM 2978 C HIS C 106 8.907 17.064 30.791 1.00 12.90 C ANISOU 2978 C HIS C 106 1558 1195 2147 -212 -222 226 C ATOM 2979 O HIS C 106 8.697 15.945 31.251 1.00 15.92 O ANISOU 2979 O HIS C 106 1592 1483 2976 -129 -393 791 O ATOM 2980 CB HIS C 106 10.960 16.923 29.336 1.00 11.24 C ANISOU 2980 CB HIS C 106 1674 899 1696 -441 -241 260 C ATOM 2981 CG HIS C 106 12.404 17.355 29.316 1.00 11.02 C ANISOU 2981 CG HIS C 106 1628 942 1617 -329 -186 -476 C ATOM 2982 ND1 HIS C 106 13.498 16.554 29.547 1.00 13.57 N ANISOU 2982 ND1 HIS C 106 1585 1280 2292 -339 -60 83 N ATOM 2983 CD2 HIS C 106 12.905 18.581 29.084 1.00 8.14 C ANISOU 2983 CD2 HIS C 106 1373 1026 693 -315 451 -505 C ATOM 2984 CE1 HIS C 106 14.628 17.287 29.455 1.00 10.68 C ANISOU 2984 CE1 HIS C 106 1591 993 1473 -425 -48 51 C ATOM 2985 NE2 HIS C 106 14.254 18.549 29.169 1.00 13.76 N ANISOU 2985 NE2 HIS C 106 1483 1384 2361 -168 443 357 N ATOM 2986 N VAL C 107 7.935 17.901 30.418 1.00 9.40 N ANISOU 2986 N VAL C 107 1375 1062 1136 -240 -49 85 N ATOM 2987 CA VAL C 107 6.525 17.633 30.769 1.00 11.18 C ANISOU 2987 CA VAL C 107 1468 2043 737 -490 179 3 C ATOM 2988 C VAL C 107 5.647 17.595 29.544 1.00 10.38 C ANISOU 2988 C VAL C 107 1461 1525 956 -791 65 271 C ATOM 2989 O VAL C 107 5.552 18.541 28.732 1.00 11.28 O ANISOU 2989 O VAL C 107 1958 1437 889 -430 148 162 O ATOM 2990 CB VAL C 107 6.033 18.749 31.721 1.00 11.79 C ANISOU 2990 CB VAL C 107 1320 1865 1295 -442 37 -174 C ATOM 2991 CG1 VAL C 107 4.559 18.571 32.048 1.00 11.18 C ANISOU 2991 CG1 VAL C 107 1475 1166 1609 -163 302 420 C ATOM 2992 CG2 VAL C 107 6.839 18.767 33.008 1.00 11.19 C ANISOU 2992 CG2 VAL C 107 1778 1455 1019 147 96 -231 C ATOM 2993 N TYR C 108 4.936 16.488 29.378 1.00 11.03 N ANISOU 2993 N TYR C 108 1266 1163 1762 -345 119 -203 N ATOM 2994 CA TYR C 108 4.107 16.279 28.176 1.00 12.15 C ANISOU 2994 CA TYR C 108 1182 1415 2019 -559 -26 -223 C ATOM 2995 C TYR C 108 2.710 15.842 28.655 1.00 12.19 C ANISOU 2995 C TYR C 108 1188 948 2495 -289 -60 525 C ATOM 2996 O TYR C 108 2.596 14.770 29.271 1.00 14.94 O ANISOU 2996 O TYR C 108 1898 1271 2509 -340 -237 863 O ATOM 2997 CB TYR C 108 4.700 15.227 27.240 1.00 13.05 C ANISOU 2997 CB TYR C 108 1585 1720 1652 -407 -181 -229 C ATOM 2998 CG TYR C 108 6.120 15.503 26.821 1.00 12.79 C ANISOU 2998 CG TYR C 108 1673 1655 1532 -96 82 29 C ATOM 2999 CD1 TYR C 108 6.367 16.402 25.794 1.00 14.74 C ANISOU 2999 CD1 TYR C 108 2001 1643 1955 -141 22 256 C ATOM 3000 CD2 TYR C 108 7.202 14.886 27.437 1.00 11.86 C ANISOU 3000 CD2 TYR C 108 1598 1595 1311 -336 -152 -182 C ATOM 3001 CE1 TYR C 108 7.682 16.688 25.391 1.00 15.68 C ANISOU 3001 CE1 TYR C 108 2224 1847 1885 -581 141 114 C ATOM 3002 CE2 TYR C 108 8.514 15.156 27.044 1.00 13.53 C ANISOU 3002 CE2 TYR C 108 1664 1651 1824 -73 272 -296 C ATOM 3003 CZ TYR C 108 8.731 16.059 26.019 1.00 15.55 C ANISOU 3003 CZ TYR C 108 1788 2237 1883 -753 84 -152 C ATOM 3004 OH TYR C 108 10.026 16.352 25.594 1.00 17.52 O ANISOU 3004 OH TYR C 108 2033 1686 2937 -818 713 -744 O ATOM 3005 N LEU C 109 1.717 16.705 28.365 1.00 11.32 N ANISOU 3005 N LEU C 109 1203 1152 1945 -216 3 558 N ATOM 3006 CA LEU C 109 0.361 16.529 28.854 1.00 11.04 C ANISOU 3006 CA LEU C 109 1144 1048 2002 -457 11 98 C ATOM 3007 C LEU C 109 -0.698 16.370 27.762 1.00 9.78 C ANISOU 3007 C LEU C 109 1254 642 1819 -488 174 96 C ATOM 3008 O LEU C 109 -0.397 16.570 26.581 1.00 12.06 O ANISOU 3008 O LEU C 109 1668 1003 1912 -581 31 396 O ATOM 3009 CB LEU C 109 -0.009 17.718 29.766 1.00 13.51 C ANISOU 3009 CB LEU C 109 1670 1571 1891 -622 128 -248 C ATOM 3010 CG LEU C 109 1.006 18.126 30.825 1.00 14.23 C ANISOU 3010 CG LEU C 109 1878 1294 2236 164 -414 -276 C ATOM 3011 CD1 LEU C 109 0.560 19.404 31.547 1.00 16.10 C ANISOU 3011 CD1 LEU C 109 2406 1653 2060 105 -194 -551 C ATOM 3012 CD2 LEU C 109 1.194 16.924 31.732 1.00 16.38 C ANISOU 3012 CD2 LEU C 109 2713 1659 1853 -14 207 -70 C ATOM 3013 N GLU C 110 -1.926 15.984 28.196 1.00 11.96 N ANISOU 3013 N GLU C 110 1139 860 2545 -667 56 248 N ATOM 3014 CA GLU C 110 -3.078 15.854 27.295 1.00 13.34 C ANISOU 3014 CA GLU C 110 1454 1155 2458 -467 -174 114 C ATOM 3015 C GLU C 110 -2.718 14.884 26.190 1.00 14.78 C ANISOU 3015 C GLU C 110 1792 1115 2710 -623 -21 -63 C ATOM 3016 O GLU C 110 -2.064 13.852 26.495 1.00 16.41 O ANISOU 3016 O GLU C 110 1919 921 3396 -682 408 118 O ATOM 3017 CB GLU C 110 -3.562 17.242 26.843 1.00 15.16 C ANISOU 3017 CB GLU C 110 1424 1312 3023 -179 130 312 C ATOM 3018 CG GLU C 110 -3.761 18.222 28.020 1.00 16.16 C ANISOU 3018 CG GLU C 110 1595 1275 3269 31 386 270 C ATOM 3019 CD GLU C 110 -4.940 17.916 28.891 1.00 19.45 C ANISOU 3019 CD GLU C 110 1840 2158 3392 62 587 421 C ATOM 3020 OE1 GLU C 110 -5.831 17.153 28.447 1.00 29.37 O ANISOU 3020 OE1 GLU C 110 1756 5870 3532 -1237 666 -171 O ATOM 3021 OE2 GLU C 110 -5.081 18.368 30.047 1.00 30.01 O ANISOU 3021 OE2 GLU C 110 3568 3684 4152 -1148 1697 -684 O ATOM 3022 N LYS C 111 -3.123 15.163 24.943 1.00 15.00 N ANISOU 3022 N LYS C 111 1418 1728 2552 -1070 94 -125 N ATOM 3023 CA LYS C 111 -2.808 14.197 23.887 1.00 14.75 C ANISOU 3023 CA LYS C 111 1367 1548 2688 -761 -224 -121 C ATOM 3024 C LYS C 111 -1.309 14.185 23.581 1.00 13.62 C ANISOU 3024 C LYS C 111 1513 944 2717 -814 57 166 C ATOM 3025 O LYS C 111 -0.859 13.240 22.884 1.00 15.45 O ANISOU 3025 O LYS C 111 1304 1029 3538 -537 -439 -198 O ATOM 3026 CB LYS C 111 -3.610 14.454 22.611 1.00 14.31 C ANISOU 3026 CB LYS C 111 1762 1126 2549 -1135 -244 227 C ATOM 3027 CG LYS C 111 -5.111 14.305 22.885 1.00 14.31 C ANISOU 3027 CG LYS C 111 1594 1313 2531 -648 -343 104 C ATOM 3028 CD LYS C 111 -5.918 14.644 21.680 1.00 16.02 C ANISOU 3028 CD LYS C 111 1943 1522 2622 -1245 -511 534 C ATOM 3029 CE LYS C 111 -7.411 14.600 21.985 1.00 19.35 C ANISOU 3029 CE LYS C 111 1795 2426 3129 -967 -705 696 C ATOM 3030 NZ LYS C 111 -8.269 15.198 20.917 1.00 28.94 N ANISOU 3030 NZ LYS C 111 3044 4334 3617 -132 -1857 5 N ATOM 3031 N ALA C 112 -0.564 15.184 24.080 1.00 11.98 N ANISOU 3031 N ALA C 112 1406 942 2205 -803 24 322 N ATOM 3032 CA ALA C 112 0.890 15.157 23.866 1.00 12.09 C ANISOU 3032 CA ALA C 112 1426 805 2362 -578 -53 -19 C ATOM 3033 C ALA C 112 1.560 14.188 24.825 1.00 13.33 C ANISOU 3033 C ALA C 112 1591 1221 2254 -423 1 137 C ATOM 3034 O ALA C 112 2.795 14.081 24.788 1.00 14.23 O ANISOU 3034 O ALA C 112 1500 1226 2681 -537 -117 -2 O ATOM 3035 CB ALA C 112 1.526 16.535 23.991 1.00 11.32 C ANISOU 3035 CB ALA C 112 1232 943 2125 -663 131 -227 C ATOM 3036 N VAL C 113 0.795 13.428 25.619 1.00 13.53 N ANISOU 3036 N VAL C 113 1698 644 2798 -557 -10 85 N ATOM 3037 CA VAL C 113 1.465 12.360 26.347 1.00 12.22 C ANISOU 3037 CA VAL C 113 1039 1492 2112 -350 177 244 C ATOM 3038 C VAL C 113 2.189 11.389 25.435 1.00 13.25 C ANISOU 3038 C VAL C 113 1276 1287 2470 -258 36 59 C ATOM 3039 O VAL C 113 3.164 10.699 25.817 1.00 16.16 O ANISOU 3039 O VAL C 113 1351 1912 2877 79 350 525 O ATOM 3040 CB VAL C 113 0.487 11.551 27.226 1.00 14.98 C ANISOU 3040 CB VAL C 113 1809 1522 2361 -846 347 226 C ATOM 3041 CG1 VAL C 113 -0.042 12.451 28.348 1.00 23.15 C ANISOU 3041 CG1 VAL C 113 2901 3469 2424 -1632 1047 -725 C ATOM 3042 CG2 VAL C 113 -0.697 10.937 26.472 1.00 15.76 C ANISOU 3042 CG2 VAL C 113 1738 1320 2932 -760 294 -54 C ATOM 3043 N VAL C 114 1.752 11.288 24.185 1.00 13.00 N ANISOU 3043 N VAL C 114 1785 695 2458 -571 3 -51 N ATOM 3044 CA VAL C 114 2.431 10.411 23.239 1.00 16.18 C ANISOU 3044 CA VAL C 114 1765 1645 2738 -346 178 -299 C ATOM 3045 C VAL C 114 3.842 10.887 22.896 1.00 19.01 C ANISOU 3045 C VAL C 114 2062 2069 3090 -430 551 133 C ATOM 3046 O VAL C 114 4.576 10.065 22.361 1.00 23.22 O ANISOU 3046 O VAL C 114 1518 3678 3628 -264 -46 -1413 O ATOM 3047 CB VAL C 114 1.627 10.289 21.928 1.00 16.80 C ANISOU 3047 CB VAL C 114 2610 1357 2416 -73 85 -165 C ATOM 3048 CG1 VAL C 114 1.650 11.627 21.172 1.00 19.54 C ANISOU 3048 CG1 VAL C 114 2149 1744 3530 -497 127 446 C ATOM 3049 CG2 VAL C 114 2.195 9.147 21.091 1.00 25.04 C ANISOU 3049 CG2 VAL C 114 3180 2396 3937 795 -1007 -1457 C ATOM 3050 N LEU C 115 4.176 12.140 23.191 1.00 18.11 N ANISOU 3050 N LEU C 115 1714 2185 2984 -582 176 404 N ATOM 3051 CA LEU C 115 5.534 12.638 22.986 1.00 19.19 C ANISOU 3051 CA LEU C 115 1918 2657 2718 -756 402 253 C ATOM 3052 C LEU C 115 6.455 12.277 24.145 1.00 18.21 C ANISOU 3052 C LEU C 115 1560 2564 2795 -739 362 -119 C ATOM 3053 O LEU C 115 7.670 12.594 24.105 1.00 24.23 O ANISOU 3053 O LEU C 115 1661 3726 3821 -1345 379 -1294 O ATOM 3054 CB LEU C 115 5.537 14.156 22.805 1.00 16.83 C ANISOU 3054 CB LEU C 115 1966 2446 1982 -1058 -86 -380 C ATOM 3055 CG LEU C 115 4.620 14.771 21.769 1.00 14.50 C ANISOU 3055 CG LEU C 115 2009 1831 1671 -1462 -142 -503 C ATOM 3056 CD1 LEU C 115 4.741 16.282 21.768 1.00 15.18 C ANISOU 3056 CD1 LEU C 115 2197 1798 1773 -1351 756 -495 C ATOM 3057 CD2 LEU C 115 4.934 14.230 20.381 1.00 16.01 C ANISOU 3057 CD2 LEU C 115 2487 1747 1848 -1421 157 -570 C ATOM 3058 N ARG C 116 5.979 11.660 25.217 1.00 20.30 N ANISOU 3058 N ARG C 116 2230 3231 2254 -417 396 -184 N ATOM 3059 CA ARG C 116 6.909 11.200 26.260 1.00 22.44 C ANISOU 3059 CA ARG C 116 2615 3265 2647 171 185 -296 C ATOM 3060 C ARG C 116 7.821 10.118 25.717 1.00 23.19 C ANISOU 3060 C ARG C 116 1841 3373 3599 -412 -2 -1130 C ATOM 3061 O ARG C 116 7.281 9.138 25.213 1.00 24.91 O ANISOU 3061 O ARG C 116 2471 3539 3456 -569 -319 -1139 O ATOM 3062 CB ARG C 116 6.100 10.620 27.423 1.00 21.12 C ANISOU 3062 CB ARG C 116 2541 2914 2568 348 -56 -13 C ATOM 3063 CG ARG C 116 5.275 11.701 28.115 1.00 18.85 C ANISOU 3063 CG ARG C 116 1901 2242 3018 -531 214 -201 C ATOM 3064 CD ARG C 116 4.440 11.118 29.248 1.00 23.88 C ANISOU 3064 CD ARG C 116 2315 3253 3505 -1055 682 -337 C ATOM 3065 NE ARG C 116 3.610 12.116 29.912 1.00 25.02 N ANISOU 3065 NE ARG C 116 2438 3372 3699 -420 916 386 N ATOM 3066 CZ ARG C 116 2.949 11.999 31.061 1.00 22.98 C ANISOU 3066 CZ ARG C 116 3973 1583 3177 -1115 912 -460 C ATOM 3067 NH1 ARG C 116 2.966 10.888 31.807 1.00 24.22 N ANISOU 3067 NH1 ARG C 116 3048 2372 3784 -260 797 336 N ATOM 3068 NH2 ARG C 116 2.228 13.038 31.497 1.00 19.48 N ANISOU 3068 NH2 ARG C 116 3178 1768 2454 -950 -177 -602 N ATOM 3069 N PRO C 117 9.145 10.250 25.782 1.00 24.00 N ANISOU 3069 N PRO C 117 1825 3461 3835 -226 -459 -64 N ATOM 3070 CA PRO C 117 10.041 9.205 25.246 1.00 25.84 C ANISOU 3070 CA PRO C 117 1930 3554 4332 303 -575 367 C ATOM 3071 C PRO C 117 9.653 7.815 25.740 1.00 26.98 C ANISOU 3071 C PRO C 117 2493 3496 4262 -24 -500 32 C ATOM 3072 O PRO C 117 9.731 6.844 25.004 1.00 31.61 O ANISOU 3072 O PRO C 117 3252 3696 5062 56 265 -344 O ATOM 3073 CB PRO C 117 11.397 9.636 25.792 1.00 28.27 C ANISOU 3073 CB PRO C 117 1755 4434 4555 -193 -220 782 C ATOM 3074 CG PRO C 117 11.290 11.131 25.777 1.00 27.92 C ANISOU 3074 CG PRO C 117 1551 4453 4604 -53 -205 -481 C ATOM 3075 CD PRO C 117 9.912 11.401 26.325 1.00 25.37 C ANISOU 3075 CD PRO C 117 1597 4499 3545 -780 6 -473 C ATOM 3076 N ASP C 118 9.170 7.761 26.982 1.00 28.97 N ANISOU 3076 N ASP C 118 2786 3523 4697 -567 135 -141 N ATOM 3077 CA ASP C 118 8.757 6.494 27.580 1.00 33.28 C ANISOU 3077 CA ASP C 118 3991 3662 4993 -976 -3 1 C ATOM 3078 C ASP C 118 7.354 6.071 27.141 1.00 33.49 C ANISOU 3078 C ASP C 118 3772 3722 5230 -1137 437 -14 C ATOM 3079 O ASP C 118 6.901 4.952 27.447 1.00 46.30 O ANISOU 3079 O ASP C 118 4723 4672 8197 -1920 -465 1566 O ATOM 3080 CB ASP C 118 8.918 6.569 29.104 1.00 33.37 C ANISOU 3080 CB ASP C 118 4611 3118 4950 -442 141 -14 C ATOM 3081 CG ASP C 118 7.933 7.458 29.839 1.00 41.52 C ANISOU 3081 CG ASP C 118 5118 5123 5534 629 204 -342 C ATOM 3082 OD1 ASP C 118 6.911 7.872 29.228 1.00 50.15 O ANISOU 3082 OD1 ASP C 118 3244 5907 9905 -606 -1829 -3387 O ATOM 3083 OD2 ASP C 118 8.146 7.769 31.047 1.00 51.37 O ANISOU 3083 OD2 ASP C 118 6580 7891 5048 1328 1038 -530 O ATOM 3084 N LEU C 119 6.600 6.864 26.388 1.00 30.48 N ANISOU 3084 N LEU C 119 3523 2943 5116 -824 264 -1065 N ATOM 3085 CA LEU C 119 5.324 6.410 25.862 1.00 25.35 C ANISOU 3085 CA LEU C 119 3654 1709 4268 -1238 716 -795 C ATOM 3086 C LEU C 119 5.299 6.395 24.330 1.00 30.07 C ANISOU 3086 C LEU C 119 4369 2783 4274 -1790 1035 -1487 C ATOM 3087 O LEU C 119 4.578 5.585 23.764 1.00 42.35 O ANISOU 3087 O LEU C 119 6635 3988 5469 -2649 76 -2131 O ATOM 3088 CB LEU C 119 4.161 7.286 26.305 1.00 23.03 C ANISOU 3088 CB LEU C 119 3739 2424 2589 -374 25 201 C ATOM 3089 CG LEU C 119 3.574 7.088 27.688 1.00 20.37 C ANISOU 3089 CG LEU C 119 3799 1241 2698 -136 78 584 C ATOM 3090 CD1 LEU C 119 2.288 7.901 27.793 1.00 22.91 C ANISOU 3090 CD1 LEU C 119 4496 2093 2117 669 -149 231 C ATOM 3091 CD2 LEU C 119 3.339 5.610 27.974 1.00 28.32 C ANISOU 3091 CD2 LEU C 119 4933 1091 4735 -174 1474 128 C ATOM 3092 N SER C 120 6.022 7.273 23.655 1.00 34.62 N ANISOU 3092 N SER C 120 3975 4702 4476 -1744 1261 -542 N ATOM 3093 CA SER C 120 6.013 7.413 22.202 1.00 36.04 C ANISOU 3093 CA SER C 120 4349 4899 4445 -1304 1270 -791 C ATOM 3094 C SER C 120 6.113 6.100 21.419 1.00 41.15 C ANISOU 3094 C SER C 120 5142 5321 5171 -680 1066 -1328 C ATOM 3095 O SER C 120 5.585 6.045 20.289 1.00 41.26 O ANISOU 3095 O SER C 120 8180 3976 3522 -1352 1955 -156 O ATOM 3096 CB SER C 120 7.152 8.374 21.826 1.00 39.23 C ANISOU 3096 CB SER C 120 4702 5852 4351 -1624 1401 -134 C ATOM 3097 OG SER C 120 7.441 8.421 20.442 1.00 41.44 O ANISOU 3097 OG SER C 120 3895 8066 3784 -2473 -81 175 O ATOM 3098 N LEU C 121 6.743 5.080 21.952 1.00 39.33 N ANISOU 3098 N LEU C 121 3556 5430 5958 -841 569 -1735 N ATOM 3099 CA LEU C 121 7.051 3.732 21.542 1.00 36.74 C ANISOU 3099 CA LEU C 121 1717 6008 6234 -360 2042 -1899 C ATOM 3100 C LEU C 121 6.047 2.634 21.932 1.00 35.62 C ANISOU 3100 C LEU C 121 2474 5371 5687 -546 1584 -2103 C ATOM 3101 O LEU C 121 6.201 1.490 21.473 1.00 38.97 O ANISOU 3101 O LEU C 121 3344 6178 5287 -775 847 -3190 O ATOM 3102 CB LEU C 121 8.329 3.199 22.201 1.00 45.28 C ANISOU 3102 CB LEU C 121 2258 7419 7530 -107 1086 -1964 C ATOM 3103 CG LEU C 121 9.042 3.995 23.288 1.00 54.63 C ANISOU 3103 CG LEU C 121 4517 8747 7492 -1473 -50 -1188 C ATOM 3104 CD1 LEU C 121 9.640 5.268 22.699 1.00 72.37 C ANISOU 3104 CD1 LEU C 121 6859 9755 10884 -3580 -1518 -231 C ATOM 3105 CD2 LEU C 121 8.133 4.310 24.468 1.00 58.65 C ANISOU 3105 CD2 LEU C 121 4000 11662 6624 -195 -1500 -2583 C ATOM 3106 N THR C 122 5.097 2.992 22.785 1.00 31.74 N ANISOU 3106 N THR C 122 1706 5056 5296 -1257 1226 -2140 N ATOM 3107 CA THR C 122 4.136 2.020 23.336 1.00 26.68 C ANISOU 3107 CA THR C 122 1446 3171 5521 -394 629 -1795 C ATOM 3108 C THR C 122 3.350 1.395 22.208 1.00 22.91 C ANISOU 3108 C THR C 122 2145 1904 4655 -189 381 -716 C ATOM 3109 O THR C 122 2.974 0.238 22.240 1.00 20.47 O ANISOU 3109 O THR C 122 2149 1489 4138 440 -412 -496 O ATOM 3110 CB THR C 122 3.209 2.722 24.348 1.00 26.13 C ANISOU 3110 CB THR C 122 2146 2698 5085 -868 1310 -1263 C ATOM 3111 OG1 THR C 122 4.042 3.254 25.392 1.00 34.37 O ANISOU 3111 OG1 THR C 122 2805 4373 5879 -1441 1320 -2435 O ATOM 3112 CG2 THR C 122 2.248 1.777 25.045 1.00 23.13 C ANISOU 3112 CG2 THR C 122 1821 1873 5096 -85 444 -60 C ATOM 3113 N LYS C 123 3.130 2.216 21.191 1.00 25.45 N ANISOU 3113 N LYS C 123 2219 2063 5388 -522 935 78 N ATOM 3114 CA LYS C 123 2.338 1.740 20.065 1.00 22.19 C ANISOU 3114 CA LYS C 123 2520 1276 4635 -364 899 883 C ATOM 3115 C LYS C 123 3.077 0.613 19.374 1.00 22.18 C ANISOU 3115 C LYS C 123 2521 1294 4613 -272 821 864 C ATOM 3116 O LYS C 123 2.431 -0.230 18.764 1.00 19.35 O ANISOU 3116 O LYS C 123 2066 1622 3666 -244 1052 990 O ATOM 3117 CB LYS C 123 2.003 2.916 19.159 1.00 32.08 C ANISOU 3117 CB LYS C 123 4548 2187 5454 1127 1681 1530 C ATOM 3118 CG LYS C 123 2.610 3.000 17.791 1.00 36.96 C ANISOU 3118 CG LYS C 123 5217 3514 5310 1405 1620 2199 C ATOM 3119 CD LYS C 123 1.905 4.057 16.944 1.00 41.53 C ANISOU 3119 CD LYS C 123 5931 4404 5446 1868 602 1979 C ATOM 3120 CE LYS C 123 2.306 4.024 15.481 1.00 47.21 C ANISOU 3120 CE LYS C 123 6674 6050 5214 1648 285 2231 C ATOM 3121 NZ LYS C 123 1.447 4.886 14.611 1.00 52.22 N ANISOU 3121 NZ LYS C 123 6681 8753 4406 3136 -1820 -576 N ATOM 3122 N ASN C 124 4.394 0.506 19.479 1.00 20.77 N ANISOU 3122 N ASN C 124 2486 1120 4287 -633 1050 612 N ATOM 3123 CA ASN C 124 5.131 -0.586 18.843 1.00 18.33 C ANISOU 3123 CA ASN C 124 2254 1510 3202 -533 778 553 C ATOM 3124 C ASN C 124 4.794 -1.972 19.388 1.00 15.58 C ANISOU 3124 C ASN C 124 1704 1296 2920 -223 -18 572 C ATOM 3125 O ASN C 124 4.994 -2.959 18.674 1.00 19.73 O ANISOU 3125 O ASN C 124 2466 1525 3507 -421 395 193 O ATOM 3126 CB ASN C 124 6.648 -0.352 18.946 1.00 24.51 C ANISOU 3126 CB ASN C 124 2240 2480 4594 -903 1054 -86 C ATOM 3127 CG ASN C 124 7.018 0.912 18.190 1.00 32.91 C ANISOU 3127 CG ASN C 124 2975 3825 5704 -1735 1012 1040 C ATOM 3128 OD1 ASN C 124 6.332 1.304 17.234 1.00 32.61 O ANISOU 3128 OD1 ASN C 124 3447 3519 5425 -1602 1065 989 O ATOM 3129 ND2 ASN C 124 8.107 1.546 18.616 1.00 35.30 N ANISOU 3129 ND2 ASN C 124 2667 3721 7025 -1593 900 1176 N ATOM 3130 N THR C 125 4.322 -2.084 20.626 1.00 14.98 N ANISOU 3130 N THR C 125 1447 1256 2989 -250 57 721 N ATOM 3131 CA THR C 125 3.825 -3.373 21.088 1.00 15.36 C ANISOU 3131 CA THR C 125 1980 1243 2613 -565 -506 548 C ATOM 3132 C THR C 125 2.499 -3.764 20.457 1.00 12.57 C ANISOU 3132 C THR C 125 1645 1314 1817 -378 -136 716 C ATOM 3133 O THR C 125 2.067 -4.924 20.645 1.00 11.43 O ANISOU 3133 O THR C 125 1413 880 2052 -45 -14 121 O ATOM 3134 CB THR C 125 3.573 -3.390 22.610 1.00 18.56 C ANISOU 3134 CB THR C 125 2148 2396 2507 -1222 -946 1043 C ATOM 3135 OG1 THR C 125 2.518 -2.443 22.868 1.00 21.34 O ANISOU 3135 OG1 THR C 125 2406 3451 2252 -1054 -365 -84 O ATOM 3136 CG2 THR C 125 4.809 -2.985 23.410 1.00 24.27 C ANISOU 3136 CG2 THR C 125 2459 3762 2999 -1875 -1149 1117 C ATOM 3137 N GLU C 126 1.825 -2.829 19.769 1.00 13.43 N ANISOU 3137 N GLU C 126 1515 1265 2324 -5 164 637 N ATOM 3138 CA GLU C 126 0.473 -3.072 19.287 1.00 13.52 C ANISOU 3138 CA GLU C 126 1283 1724 2131 276 337 553 C ATOM 3139 C GLU C 126 0.259 -3.100 17.777 1.00 14.33 C ANISOU 3139 C GLU C 126 1799 1456 2189 107 122 687 C ATOM 3140 O GLU C 126 -0.721 -3.677 17.260 1.00 14.52 O ANISOU 3140 O GLU C 126 1665 1792 2061 184 274 445 O ATOM 3141 CB GLU C 126 -0.389 -1.873 19.748 1.00 16.77 C ANISOU 3141 CB GLU C 126 1477 1631 3263 28 1149 326 C ATOM 3142 CG GLU C 126 -0.348 -1.574 21.245 1.00 16.71 C ANISOU 3142 CG GLU C 126 2131 716 3502 -961 1023 -112 C ATOM 3143 CD GLU C 126 -1.390 -2.371 22.016 1.00 12.17 C ANISOU 3143 CD GLU C 126 1300 565 2758 -660 532 -163 C ATOM 3144 OE1 GLU C 126 -1.958 -3.362 21.490 1.00 10.26 O ANISOU 3144 OE1 GLU C 126 1068 814 2015 -657 -204 261 O ATOM 3145 OE2 GLU C 126 -1.618 -1.973 23.208 1.00 12.69 O ANISOU 3145 OE2 GLU C 126 1227 1002 2594 -673 120 -262 O ATOM 3146 N LEU C 127 1.141 -2.376 17.066 1.00 16.40 N ANISOU 3146 N LEU C 127 1927 2170 2135 -70 346 640 N ATOM 3147 CA LEU C 127 0.931 -2.338 15.626 1.00 16.50 C ANISOU 3147 CA LEU C 127 1759 2420 2088 567 610 396 C ATOM 3148 C LEU C 127 2.237 -1.950 14.940 1.00 16.49 C ANISOU 3148 C LEU C 127 2195 1740 2330 -105 672 442 C ATOM 3149 O LEU C 127 3.200 -1.640 15.653 1.00 18.94 O ANISOU 3149 O LEU C 127 2657 1839 2700 -843 835 -447 O ATOM 3150 CB ALEU C 127 -0.202 -1.361 15.283 0.64 19.25 C ANISOU 3150 CB ALEU C 127 2148 2102 3065 366 -109 579 C ATOM 3151 CB BLEU C 127 -0.168 -1.384 15.177 0.36 19.00 C ANISOU 3151 CB BLEU C 127 2351 2112 2755 535 128 627 C ATOM 3152 CG ALEU C 127 0.047 0.004 15.947 0.64 21.46 C ANISOU 3152 CG ALEU C 127 2724 2243 3186 421 835 156 C ATOM 3153 CG BLEU C 127 -0.430 -0.086 15.923 0.36 19.60 C ANISOU 3153 CG BLEU C 127 2491 1927 3030 447 483 709 C ATOM 3154 CD1ALEU C 127 0.695 0.961 14.960 0.64 23.62 C ANISOU 3154 CD1ALEU C 127 2623 3358 2992 -1753 1166 -1128 C ATOM 3155 CD1BLEU C 127 -1.444 -0.351 17.021 0.36 25.87 C ANISOU 3155 CD1BLEU C 127 3296 2654 3880 208 1361 389 C ATOM 3156 CD2ALEU C 127 -1.260 0.553 16.475 0.64 19.55 C ANISOU 3156 CD2ALEU C 127 2933 2543 1951 835 1102 1526 C ATOM 3157 CD2BLEU C 127 0.807 0.545 16.535 0.36 22.88 C ANISOU 3157 CD2BLEU C 127 3640 3030 2024 -682 389 725 C ATOM 3158 OXT LEU C 127 2.271 -1.930 13.700 1.00 18.40 O ANISOU 3158 OXT LEU C 127 2896 1746 2350 -618 880 402 O TER 3159 LEU C 127 END