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*** OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 26-AUG-18 6MA7 ***elNémo ID: 2404101705353327104Job options:ID = 2404101705353327104 JOBID = OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 26-AUG-18 6MA7 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 26-AUG-18 6MA7 TITLE HUMAN CYP3A4 BOUND TO AN INHIBITOR FLUCONAZOLE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME P450 3A4; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 23-503; COMPND 5 SYNONYM: 1,8-CINEOLE 2-EXO-MONOOXYGENASE,ALBENDAZOLE MONOOXYGENASE, COMPND 6 ALBENDAZOLE SULFOXIDASE,CYPIIIA3,CYPIIIA4,CHOLESTEROL 25-HYDROXYLASE, COMPND 7 CYTOCHROME P450 3A3,CYTOCHROME P450 HLP,CYTOCHROME P450 NF-25, COMPND 8 CYTOCHROME P450-PCN1,NIFEDIPINE OXIDASE,QUININE 3-MONOOXYGENASE, COMPND 9 TAUROCHENODEOXYCHOLATE 6-ALPHA-HYDROXYLASE; COMPND 10 EC: 1.14.14.-,1.14.14.56,1.14.14.55; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CYP3A4, CYP3A3; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41; SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PCWORI KEYWDS OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX, KEYWDS 2 CYP3A4 EXPDTA X-RAY DIFFRACTION AUTHOR I.F.SEVRIOUKOVA REVDAT 4 11-OCT-23 6MA7 1 REMARK REVDAT 3 18-DEC-19 6MA7 1 REMARK REVDAT 2 12-JUN-19 6MA7 1 TITLE JRNL REVDAT 1 16-JAN-19 6MA7 0 JRNL AUTH I.SEVRIOUKOVA JRNL TITL INTERACTION OF HUMAN DRUG-METABOLIZING CYP3A4 WITH SMALL JRNL TITL 2 INHIBITORY MOLECULES. JRNL REF BIOCHEMISTRY V. 58 930 2019 JRNL REFN ISSN 0006-2960 JRNL PMID 30676743 JRNL DOI 10.1021/ACS.BIOCHEM.8B01221 REMARK 2 REMARK 2 RESOLUTION. 2.09 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.11.1_2575) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 29446 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 1455 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 65.5286 - 4.5023 1.00 2965 143 0.1523 0.1868 REMARK 3 2 4.5023 - 3.5736 1.00 2866 141 0.1590 0.2061 REMARK 3 3 3.5736 - 3.1219 0.99 2799 145 0.2114 0.3188 REMARK 3 4 3.1219 - 2.8365 0.99 2781 145 0.2441 0.3180 REMARK 3 5 2.8365 - 2.6332 1.00 2766 162 0.2523 0.3130 REMARK 3 6 2.6332 - 2.4779 1.00 2792 132 0.2551 0.3593 REMARK 3 7 2.4779 - 2.3538 0.99 2755 151 0.2780 0.3194 REMARK 3 8 2.3538 - 2.2513 1.00 2751 153 0.2978 0.3648 REMARK 3 9 2.2513 - 2.1647 0.99 2788 127 0.3158 0.3414 REMARK 3 10 2.1647 - 2.0900 0.99 2728 156 0.3244 0.3711 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.470 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 3937 REMARK 3 ANGLE : 1.003 5340 REMARK 3 CHIRALITY : 0.052 583 REMARK 3 PLANARITY : 0.007 674 REMARK 3 DIHEDRAL : 14.456 2382 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -18.9359 -23.8698 -12.6772 REMARK 3 T TENSOR REMARK 3 T11: 0.3390 T22: 0.5328 REMARK 3 T33: 0.4272 T12: 0.0142 REMARK 3 T13: 0.0037 T23: -0.0947 REMARK 3 L TENSOR REMARK 3 L11: 3.9577 L22: 5.9893 REMARK 3 L33: 2.7829 L12: -2.3939 REMARK 3 L13: -0.4661 L23: 0.5137 REMARK 3 S TENSOR REMARK 3 S11: 0.0416 S12: 0.3753 S13: -0.1925 REMARK 3 S21: -0.0552 S22: -0.1035 S23: -0.0832 REMARK 3 S31: 0.2826 S32: 0.1877 S33: 0.0338 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6MA7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-18. REMARK 100 THE DEPOSITION ID IS D_1000236494. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-APR-18 REMARK 200 TEMPERATURE (KELVIN) : 77 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 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 : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29479 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090 REMARK 200 RESOLUTION RANGE LOW (A) : 79.280 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 6.400 REMARK 200 R MERGE (I) : 0.08900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5 REMARK 200 DATA REDUNDANCY IN SHELL : 6.40 REMARK 200 R MERGE FOR SHELL (I) : 1.55300 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 REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 5VCC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.31 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM MALONATE, PH 7.0, REMARK 280 MICROBATCH, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.18900 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.65500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.65950 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.18900 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.65500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.65950 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.18900 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.65500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 63.65950 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.18900 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.65500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.65950 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16530 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 72650 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -76.37800 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 -76.37800 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 21 REMARK 465 ALA A 22 REMARK 465 TYR A 23 REMARK 465 LEU A 24 REMARK 465 TYR A 25 REMARK 465 THR A 264 REMARK 465 GLN A 265 REMARK 465 LYS A 266 REMARK 465 HIS A 267 REMARK 465 ARG A 268 REMARK 465 LYS A 282 REMARK 465 GLU A 283 REMARK 465 THR A 284 REMARK 465 GLU A 285 REMARK 465 GLY A 498 REMARK 465 THR A 499 REMARK 465 VAL A 500 REMARK 465 SER A 501 REMARK 465 GLY A 502 REMARK 465 ALA A 503 REMARK 465 HIS A 504 REMARK 465 HIS A 505 REMARK 465 HIS A 506 REMARK 465 HIS A 507 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR A 27 57.61 -115.92 REMARK 500 PHE A 46 -49.68 72.67 REMARK 500 PHE A 102 53.12 -111.91 REMARK 500 ASP A 123 -127.90 44.55 REMARK 500 PRO A 199 5.48 -63.42 REMARK 500 PHE A 228 -5.58 -59.43 REMARK 500 ASP A 270 154.13 -45.32 REMARK 500 ALA A 289 153.26 103.26 REMARK 500 MET A 371 -56.82 67.21 REMARK 500 GLU A 410 61.62 35.03 REMARK 500 PRO A 429 -6.67 -57.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM A 601 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 442 SG REMARK 620 2 HEM A 601 NA 90.9 REMARK 620 3 HEM A 601 NB 84.3 87.9 REMARK 620 4 HEM A 601 NC 89.1 178.8 90.9 REMARK 620 5 HEM A 601 ND 94.3 91.7 178.5 89.5 REMARK 620 6 TPF A 602 N5 174.6 93.6 92.9 86.3 88.6 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TPF A 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604 DBREF 6MA7 A 23 503 UNP P08684 CP3A4_HUMAN 23 503 SEQADV 6MA7 MET A 21 UNP P08684 INITIATING METHIONINE SEQADV 6MA7 ALA A 22 UNP P08684 EXPRESSION TAG SEQADV 6MA7 THR A 269 UNP P08684 VAL 269 CONFLICT SEQADV 6MA7 HIS A 504 UNP P08684 EXPRESSION TAG SEQADV 6MA7 HIS A 505 UNP P08684 EXPRESSION TAG SEQADV 6MA7 HIS A 506 UNP P08684 EXPRESSION TAG SEQADV 6MA7 HIS A 507 UNP P08684 EXPRESSION TAG SEQRES 1 A 487 MET ALA TYR LEU TYR GLY THR HIS SER HIS GLY LEU PHE SEQRES 2 A 487 LYS LYS LEU GLY ILE PRO GLY PRO THR PRO LEU PRO PHE SEQRES 3 A 487 LEU GLY ASN ILE LEU SER TYR HIS LYS GLY PHE CYS MET SEQRES 4 A 487 PHE ASP MET GLU CYS HIS LYS LYS TYR GLY LYS VAL TRP SEQRES 5 A 487 GLY PHE TYR ASP GLY GLN GLN PRO VAL LEU ALA ILE THR SEQRES 6 A 487 ASP PRO ASP MET ILE LYS THR VAL LEU VAL LYS GLU CYS SEQRES 7 A 487 TYR SER VAL PHE THR ASN ARG ARG PRO PHE GLY PRO VAL SEQRES 8 A 487 GLY PHE MET LYS SER ALA ILE SER ILE ALA GLU ASP GLU SEQRES 9 A 487 GLU TRP LYS ARG LEU ARG SER LEU LEU SER PRO THR PHE SEQRES 10 A 487 THR SER GLY LYS LEU LYS GLU MET VAL PRO ILE ILE ALA SEQRES 11 A 487 GLN TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU SEQRES 12 A 487 ALA GLU THR GLY LYS PRO VAL THR LEU LYS ASP VAL PHE SEQRES 13 A 487 GLY ALA TYR SER MET ASP VAL ILE THR SER THR SER PHE SEQRES 14 A 487 GLY VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO SEQRES 15 A 487 PHE VAL GLU ASN THR LYS LYS LEU LEU ARG PHE ASP PHE SEQRES 16 A 487 LEU ASP PRO PHE PHE LEU SER ILE THR VAL PHE PRO PHE SEQRES 17 A 487 LEU ILE PRO ILE LEU GLU VAL LEU ASN ILE CYS VAL PHE SEQRES 18 A 487 PRO ARG GLU VAL THR ASN PHE LEU ARG LYS SER VAL LYS SEQRES 19 A 487 ARG MET LYS GLU SER ARG LEU GLU ASP THR GLN LYS HIS SEQRES 20 A 487 ARG THR ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SEQRES 21 A 487 SER LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU SEQRES 22 A 487 GLU LEU VAL ALA GLN SER ILE ILE PHE ILE PHE ALA GLY SEQRES 23 A 487 TYR GLU THR THR SER SER VAL LEU SER PHE ILE MET TYR SEQRES 24 A 487 GLU LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN SEQRES 25 A 487 GLU GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO SEQRES 26 A 487 THR TYR ASP THR VAL LEU GLN MET GLU TYR LEU ASP MET SEQRES 27 A 487 VAL VAL ASN GLU THR LEU ARG LEU PHE PRO ILE ALA MET SEQRES 28 A 487 ARG LEU GLU ARG VAL CYS LYS LYS ASP VAL GLU ILE ASN SEQRES 29 A 487 GLY MET PHE ILE PRO LYS GLY VAL VAL VAL MET ILE PRO SEQRES 30 A 487 SER TYR ALA LEU HIS ARG ASP PRO LYS TYR TRP THR GLU SEQRES 31 A 487 PRO GLU LYS PHE LEU PRO GLU ARG PHE SER LYS LYS ASN SEQRES 32 A 487 LYS ASP ASN ILE ASP PRO TYR ILE TYR THR PRO PHE GLY SEQRES 33 A 487 SER GLY PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU SEQRES 34 A 487 MET ASN MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN SEQRES 35 A 487 PHE SER PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU SEQRES 36 A 487 LYS LEU SER LEU GLY GLY LEU LEU GLN PRO GLU LYS PRO SEQRES 37 A 487 VAL VAL LEU LYS VAL GLU SER ARG ASP GLY THR VAL SER SEQRES 38 A 487 GLY ALA HIS HIS HIS HIS HET HEM A 601 43 HET TPF A 602 22 HET DMS A 603 4 HET EDO A 604 4 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM TPF 2-(2,4-DIFLUOROPHENYL)-1,3-DI(1H-1,2,4-TRIAZOL-1-YL) HETNAM 2 TPF PROPAN-2-OL HETNAM DMS DIMETHYL SULFOXIDE HETNAM EDO 1,2-ETHANEDIOL HETSYN HEM HEME HETSYN TPF FLUCONAZOLE; ALPHA-(2,4-DIFLUOROPHENYL)-ALPHA-(1H-1,2, HETSYN 2 TPF 4-TRIAZOLE-1-YLMETHYL)-1H-1,2,4-TRIAZOLE-1-ETHANOL; HETSYN 3 TPF ELAZOR; TRIFLUCAN; BIOZOLENE HETSYN EDO ETHYLENE GLYCOL FORMUL 2 HEM C34 H32 FE N4 O4 FORMUL 3 TPF C13 H12 F2 N6 O FORMUL 4 DMS C2 H6 O S FORMUL 5 EDO C2 H6 O2 FORMUL 6 HOH *89(H2 O) HELIX 1 AA1 GLY A 31 LEU A 36 1 6 HELIX 2 AA2 ASN A 49 HIS A 54 5 6 HELIX 3 AA3 LYS A 55 GLY A 69 1 15 HELIX 4 AA4 ASP A 86 VAL A 95 1 10 HELIX 5 AA5 VAL A 111 ALA A 117 5 7 HELIX 6 AA6 GLU A 122 SER A 134 1 13 HELIX 7 AA7 PRO A 135 PHE A 137 5 3 HELIX 8 AA8 THR A 138 GLU A 165 1 28 HELIX 9 AA9 LEU A 172 GLY A 190 1 19 HELIX 10 AB1 ASP A 201 LYS A 208 1 8 HELIX 11 AB2 ASP A 217 PHE A 226 1 10 HELIX 12 AB3 LEU A 229 LEU A 236 1 8 HELIX 13 AB4 PRO A 242 LEU A 261 1 20 HELIX 14 AB5 ASP A 270 GLN A 279 1 10 HELIX 15 AB6 SER A 291 THR A 323 1 33 HELIX 16 AB7 HIS A 324 LEU A 339 1 16 HELIX 17 AB8 THR A 346 LEU A 351 1 6 HELIX 18 AB9 MET A 353 PHE A 367 1 15 HELIX 19 AC1 PRO A 397 ARG A 403 1 7 HELIX 20 AC2 LEU A 415 SER A 420 5 6 HELIX 21 AC3 ASN A 423 ILE A 427 5 5 HELIX 22 AC4 GLY A 444 ASN A 462 1 19 SHEET 1 AA1 4 VAL A 71 ASP A 76 0 SHEET 2 AA1 4 GLN A 79 ILE A 84 -1 O VAL A 81 N PHE A 74 SHEET 3 AA1 4 VAL A 393 ILE A 396 1 O VAL A 393 N LEU A 82 SHEET 4 AA1 4 LEU A 373 VAL A 376 -1 N ARG A 375 O VAL A 394 SHEET 1 AA2 3 VAL A 170 THR A 171 0 SHEET 2 AA2 3 VAL A 490 SER A 495 -1 O LEU A 491 N VAL A 170 SHEET 3 AA2 3 PHE A 463 PRO A 467 -1 N LYS A 466 O LYS A 492 SHEET 1 AA3 2 VAL A 381 GLU A 382 0 SHEET 2 AA3 2 PHE A 387 ILE A 388 -1 O ILE A 388 N VAL A 381 LINK SG CYS A 442 FE HEM A 601 1555 1555 2.40 LINK FE HEM A 601 N5 TPF A 602 1555 1555 2.20 CISPEP 1 GLY A 109 PRO A 110 0 2.79 CISPEP 2 ILE A 473 PRO A 474 0 -4.07 SITE 1 AC1 22 ARG A 105 ILE A 118 SER A 119 TRP A 126 SITE 2 AC1 22 ARG A 130 PHE A 137 PHE A 302 ALA A 305 SITE 3 AC1 22 GLY A 306 ALA A 370 ARG A 375 PRO A 434 SITE 4 AC1 22 PHE A 435 GLY A 436 SER A 437 ARG A 440 SITE 5 AC1 22 ASN A 441 CYS A 442 ILE A 443 GLY A 444 SITE 6 AC1 22 TPF A 602 HOH A 751 SITE 1 AC2 9 ARG A 105 ARG A 212 ALA A 305 ILE A 369 SITE 2 AC2 9 ALA A 370 HEM A 601 DMS A 603 HOH A 736 SITE 3 AC2 9 HOH A 760 SITE 1 AC3 3 SER A 119 PHE A 304 TPF A 602 SITE 1 AC4 6 GLY A 177 ALA A 178 MET A 181 SER A 195 SITE 2 AC4 6 VAL A 204 TYR A 307 CRYST1 76.378 101.310 127.319 90.00 90.00 90.00 I 2 2 2 8 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 0.013093 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009871 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007854 0.00000 ATOM 1 N GLY A 26 -34.317 8.706 -14.755 1.00128.59 N ANISOU 1 N GLY A 26 16562 13800 18498 2794 437 1597 N ATOM 2 CA GLY A 26 -33.904 7.326 -14.563 1.00126.57 C ANISOU 2 CA GLY A 26 16140 13908 18043 2542 375 1417 C ATOM 3 C GLY A 26 -32.608 6.995 -15.277 1.00128.93 C ANISOU 3 C GLY A 26 16532 14226 18228 2319 463 1607 C ATOM 4 O GLY A 26 -32.168 5.852 -15.299 1.00117.11 O ANISOU 4 O GLY A 26 14921 13024 16553 2131 417 1500 O ATOM 5 N THR A 27 -31.996 8.010 -15.878 1.00144.25 N ANISOU 5 N THR A 27 18681 15832 20295 2349 618 1906 N ATOM 6 CA THR A 27 -30.716 7.829 -16.548 1.00149.54 C ANISOU 6 CA THR A 27 19431 16468 20918 2141 773 2119 C ATOM 7 C THR A 27 -29.647 8.652 -15.842 1.00161.94 C ANISOU 7 C THR A 27 21063 17579 22889 1854 953 2076 C ATOM 8 O THR A 27 -29.018 9.523 -16.456 1.00167.94 O ANISOU 8 O THR A 27 21978 18006 23825 1843 1158 2384 O ATOM 9 CB THR A 27 -30.818 8.232 -18.017 1.00142.27 C ANISOU 9 CB THR A 27 18706 15556 19794 2424 845 2558 C ATOM 10 OG1 THR A 27 -31.069 9.640 -18.105 1.00145.88 O ANISOU 10 OG1 THR A 27 19354 15572 20501 2606 963 2775 O ATOM 11 CG2 THR A 27 -31.950 7.475 -18.695 1.00132.20 C ANISOU 11 CG2 THR A 27 17362 14727 18142 2738 591 2545 C ATOM 12 N HIS A 28 -29.458 8.402 -14.544 1.00162.49 N ANISOU 12 N HIS A 28 21015 17611 23113 1633 877 1692 N ATOM 13 CA HIS A 28 -28.429 9.118 -13.801 1.00158.59 C ANISOU 13 CA HIS A 28 20554 16695 23009 1355 976 1574 C ATOM 14 C HIS A 28 -27.049 8.838 -14.385 1.00151.58 C ANISOU 14 C HIS A 28 19620 15779 22194 1086 1126 1750 C ATOM 15 O HIS A 28 -26.237 9.756 -14.555 1.00153.41 O ANISOU 15 O HIS A 28 19916 15588 22784 946 1306 1908 O ATOM 16 CB HIS A 28 -28.478 8.729 -12.318 1.00151.79 C ANISOU 16 CB HIS A 28 19599 15877 22198 1210 824 1108 C ATOM 17 CG HIS A 28 -29.838 8.846 -11.697 1.00143.48 C ANISOU 17 CG HIS A 28 18561 14900 21054 1476 725 926 C ATOM 18 ND1 HIS A 28 -30.676 7.765 -11.522 1.00136.96 N ANISOU 18 ND1 HIS A 28 17599 14512 19927 1583 616 795 N ATOM 19 CD2 HIS A 28 -30.502 9.918 -11.200 1.00142.83 C ANISOU 19 CD2 HIS A 28 18597 14495 21177 1659 742 850 C ATOM 20 CE1 HIS A 28 -31.799 8.166 -10.953 1.00136.03 C ANISOU 20 CE1 HIS A 28 17494 14350 19843 1816 589 660 C ATOM 21 NE2 HIS A 28 -31.719 9.468 -10.745 1.00140.60 N ANISOU 21 NE2 HIS A 28 18234 14479 20707 1880 660 685 N ATOM 22 N SER A 29 -26.787 7.578 -14.738 1.00138.26 N ANISOU 22 N SER A 29 17811 14523 20197 1018 1075 1734 N ATOM 23 CA SER A 29 -25.465 7.123 -15.151 1.00121.42 C ANISOU 23 CA SER A 29 15591 12421 18123 762 1212 1839 C ATOM 24 C SER A 29 -25.462 6.504 -16.545 1.00105.85 C ANISOU 24 C SER A 29 13670 10760 15790 919 1319 2171 C ATOM 25 O SER A 29 -24.502 5.822 -16.905 1.00 99.73 O ANISOU 25 O SER A 29 12801 10128 14965 748 1419 2223 O ATOM 26 CB SER A 29 -24.925 6.114 -14.140 1.00112.09 C ANISOU 26 CB SER A 29 14222 11445 16921 515 1050 1459 C ATOM 27 OG SER A 29 -25.894 5.111 -13.923 1.00105.45 O ANISOU 27 OG SER A 29 13340 11012 15714 667 868 1291 O ATOM 28 N HIS A 30 -26.510 6.726 -17.339 1.00 97.79 N ANISOU 28 N HIS A 30 12799 9849 14508 1265 1286 2383 N ATOM 29 CA HIS A 30 -26.616 6.116 -18.658 1.00 85.69 C ANISOU 29 CA HIS A 30 11355 8641 12563 1472 1330 2656 C ATOM 30 C HIS A 30 -25.869 6.874 -19.737 1.00 98.56 C ANISOU 30 C HIS A 30 13174 10026 14248 1527 1662 3116 C ATOM 31 O HIS A 30 -25.895 6.447 -20.897 1.00102.96 O ANISOU 31 O HIS A 30 13862 10836 14420 1739 1730 3373 O ATOM 32 CB HIS A 30 -28.073 6.003 -19.073 1.00 79.38 C ANISOU 32 CB HIS A 30 10626 8084 11451 1850 1103 2665 C ATOM 33 CG HIS A 30 -28.803 4.909 -18.378 1.00 73.85 C ANISOU 33 CG HIS A 30 9719 7736 10603 1822 824 2280 C ATOM 34 ND1 HIS A 30 -30.160 4.719 -18.514 1.00 75.71 N ANISOU 34 ND1 HIS A 30 9919 8186 10661 2108 592 2198 N ATOM 35 CD2 HIS A 30 -28.366 3.938 -17.542 1.00 71.54 C ANISOU 35 CD2 HIS A 30 9238 7604 10338 1549 756 1968 C ATOM 36 CE1 HIS A 30 -30.528 3.679 -17.792 1.00 72.63 C ANISOU 36 CE1 HIS A 30 9317 8055 10222 1988 426 1860 C ATOM 37 NE2 HIS A 30 -29.459 3.189 -17.189 1.00 69.77 N ANISOU 37 NE2 HIS A 30 8884 7664 9959 1661 523 1726 N ATOM 38 N GLY A 31 -25.245 7.997 -19.402 1.00102.07 N ANISOU 38 N GLY A 31 13653 9971 15157 1362 1877 3230 N ATOM 39 CA GLY A 31 -24.386 8.715 -20.316 1.00 92.95 C ANISOU 39 CA GLY A 31 12643 8521 14153 1349 2265 3676 C ATOM 40 C GLY A 31 -22.916 8.389 -20.173 1.00 91.81 C ANISOU 40 C GLY A 31 12299 8288 14294 967 2489 3654 C ATOM 41 O GLY A 31 -22.087 9.070 -20.786 1.00 95.75 O ANISOU 41 O GLY A 31 12865 8467 15050 892 2868 4013 O ATOM 42 N LEU A 32 -22.559 7.362 -19.397 1.00 86.66 N ANISOU 42 N LEU A 32 11397 7904 13626 735 2283 3261 N ATOM 43 CA LEU A 32 -21.150 7.103 -19.127 1.00 83.43 C ANISOU 43 CA LEU A 32 10752 7388 13558 372 2451 3195 C ATOM 44 C LEU A 32 -20.417 6.639 -20.379 1.00 88.19 C ANISOU 44 C LEU A 32 11398 8167 13943 432 2783 3560 C ATOM 45 O LEU A 32 -19.328 7.137 -20.687 1.00 97.14 O ANISOU 45 O LEU A 32 12449 9000 15458 238 3140 3792 O ATOM 46 CB LEU A 32 -21.007 6.073 -18.005 1.00 77.25 C ANISOU 46 CB LEU A 32 9728 6871 12754 170 2126 2699 C ATOM 47 CG LEU A 32 -19.580 5.669 -17.637 1.00 72.74 C ANISOU 47 CG LEU A 32 8876 6245 12519 -178 2218 2572 C ATOM 48 CD1 LEU A 32 -18.729 6.894 -17.474 1.00 80.02 C ANISOU 48 CD1 LEU A 32 9717 6609 14079 -412 2448 2690 C ATOM 49 CD2 LEU A 32 -19.597 4.879 -16.349 1.00 75.00 C ANISOU 49 CD2 LEU A 32 8986 6717 12794 -326 1851 2075 C ATOM 50 N PHE A 33 -20.980 5.680 -21.109 1.00 84.53 N ANISOU 50 N PHE A 33 11053 8176 12886 698 2683 3604 N ATOM 51 CA PHE A 33 -20.231 5.160 -22.244 1.00 87.52 C ANISOU 51 CA PHE A 33 11489 8744 13021 769 2997 3904 C ATOM 52 C PHE A 33 -20.243 6.101 -23.441 1.00 99.73 C ANISOU 52 C PHE A 33 13347 10071 14477 1025 3385 4456 C ATOM 53 O PHE A 33 -19.333 6.023 -24.275 1.00 98.47 O ANISOU 53 O PHE A 33 13221 9899 14296 1018 3790 4772 O ATOM 54 CB PHE A 33 -20.752 3.784 -22.625 1.00 79.50 C ANISOU 54 CB PHE A 33 10506 8288 11412 965 2750 3728 C ATOM 55 CG PHE A 33 -20.516 2.757 -21.558 1.00 80.30 C ANISOU 55 CG PHE A 33 10314 8590 11607 706 2466 3257 C ATOM 56 CD1 PHE A 33 -21.577 2.114 -20.943 1.00 74.72 C ANISOU 56 CD1 PHE A 33 9583 8137 10670 789 2059 2917 C ATOM 57 CD2 PHE A 33 -19.227 2.471 -21.140 1.00 79.55 C ANISOU 57 CD2 PHE A 33 9957 8405 11865 387 2618 3166 C ATOM 58 CE1 PHE A 33 -21.350 1.166 -19.934 1.00 66.38 C ANISOU 58 CE1 PHE A 33 8290 7241 9689 568 1831 2519 C ATOM 59 CE2 PHE A 33 -18.990 1.545 -20.142 1.00 77.37 C ANISOU 59 CE2 PHE A 33 9439 8301 11656 184 2346 2751 C ATOM 60 CZ PHE A 33 -20.052 0.878 -19.540 1.00 63.16 C ANISOU 60 CZ PHE A 33 7664 6754 9581 281 1963 2440 C ATOM 61 N LYS A 34 -21.229 7.001 -23.533 1.00106.97 N ANISOU 61 N LYS A 34 14496 10800 15348 1267 3295 4595 N ATOM 62 CA LYS A 34 -21.187 8.034 -24.566 1.00112.63 C ANISOU 62 CA LYS A 34 15530 11224 16042 1507 3686 5150 C ATOM 63 C LYS A 34 -20.104 9.059 -24.264 1.00121.69 C ANISOU 63 C LYS A 34 16546 11783 17908 1167 4092 5340 C ATOM 64 O LYS A 34 -19.429 9.549 -25.177 1.00121.89 O ANISOU 64 O LYS A 34 16678 11679 17956 1210 4508 5698 O ATOM 65 CB LYS A 34 -22.548 8.719 -24.697 1.00111.87 C ANISOU 65 CB LYS A 34 15701 11071 15732 1876 3449 5232 C ATOM 66 CG LYS A 34 -23.616 7.863 -25.363 1.00112.25 C ANISOU 66 CG LYS A 34 15922 11663 15063 2290 3114 5167 C ATOM 67 CD LYS A 34 -24.918 8.627 -25.544 1.00115.37 C ANISOU 67 CD LYS A 34 16554 11979 15304 2678 2891 5276 C ATOM 68 CE LYS A 34 -25.996 7.724 -26.116 1.00113.82 C ANISOU 68 CE LYS A 34 16452 12328 14468 3058 2486 5133 C ATOM 69 NZ LYS A 34 -27.257 8.466 -26.370 1.00118.16 N ANISOU 69 NZ LYS A 34 17204 12817 14873 3474 2255 5251 N ATOM 70 N LYS A 35 -19.925 9.391 -22.983 1.00123.99 N ANISOU 70 N LYS A 35 16562 11797 18750 821 3892 4960 N ATOM 71 CA LYS A 35 -18.860 10.307 -22.583 1.00128.13 C ANISOU 71 CA LYS A 35 16896 11756 20029 450 4200 5036 C ATOM 72 C LYS A 35 -17.481 9.713 -22.854 1.00125.67 C ANISOU 72 C LYS A 35 16298 11579 19872 183 4455 5022 C ATOM 73 O LYS A 35 -16.596 10.398 -23.378 1.00136.37 O ANISOU 73 O LYS A 35 17585 12725 21504 80 4793 5199 O ATOM 74 CB LYS A 35 -19.010 10.664 -21.104 1.00134.15 C ANISOU 74 CB LYS A 35 17440 12263 21268 174 3836 4537 C ATOM 75 CG LYS A 35 -18.126 11.815 -20.631 1.00145.40 C ANISOU 75 CG LYS A 35 18684 13127 23435 -163 4004 4480 C ATOM 76 CD LYS A 35 -17.915 11.815 -19.112 1.00150.88 C ANISOU 76 CD LYS A 35 19102 13610 24616 -498 3651 3938 C ATOM 77 CE LYS A 35 -16.920 10.730 -18.684 1.00156.45 C ANISOU 77 CE LYS A 35 19444 14575 25424 -792 3566 3664 C ATOM 78 NZ LYS A 35 -16.551 10.797 -17.236 1.00158.79 N ANISOU 78 NZ LYS A 35 19472 14701 26162 -1102 3190 3098 N ATOM 79 N LEU A 36 -17.273 8.441 -22.504 1.00118.90 N ANISOU 79 N LEU A 36 15246 11113 18818 89 4261 4754 N ATOM 80 CA LEU A 36 -15.987 7.796 -22.740 1.00109.93 C ANISOU 80 CA LEU A 36 13827 10089 17852 -139 4519 4767 C ATOM 81 C LEU A 36 -15.757 7.463 -24.200 1.00108.19 C ANISOU 81 C LEU A 36 13826 10168 17113 163 4866 5139 C ATOM 82 O LEU A 36 -14.723 6.860 -24.520 1.00110.67 O ANISOU 82 O LEU A 36 13927 10645 17477 45 5067 5120 O ATOM 83 CB LEU A 36 -15.870 6.521 -21.907 1.00101.59 C ANISOU 83 CB LEU A 36 12505 9437 16658 -283 4112 4263 C ATOM 84 CG LEU A 36 -15.943 6.652 -20.385 1.00 99.90 C ANISOU 84 CG LEU A 36 12051 9066 16841 -558 3672 3740 C ATOM 85 CD1 LEU A 36 -15.593 5.331 -19.714 1.00 89.42 C ANISOU 85 CD1 LEU A 36 10470 8143 15364 -683 3359 3318 C ATOM 86 CD2 LEU A 36 -15.020 7.748 -19.907 1.00110.51 C ANISOU 86 CD2 LEU A 36 13162 9819 19007 -906 3864 3757 C ATOM 87 N GLY A 37 -16.681 7.839 -25.083 1.00102.64 N ANISOU 87 N GLY A 37 13543 9543 15912 570 4914 5445 N ATOM 88 CA GLY A 37 -16.582 7.462 -26.480 1.00104.66 C ANISOU 88 CA GLY A 37 14063 10121 15584 913 5177 5749 C ATOM 89 C GLY A 37 -16.611 5.972 -26.715 1.00 98.90 C ANISOU 89 C GLY A 37 13324 9913 14340 1027 5055 5622 C ATOM 90 O GLY A 37 -16.075 5.497 -27.724 1.00 99.81 O ANISOU 90 O GLY A 37 13533 10276 14115 1197 5308 5768 O ATOM 91 N ILE A 38 -17.214 5.220 -25.804 1.00 93.49 N ANISOU 91 N ILE A 38 12514 9426 13582 945 4618 5260 N ATOM 92 CA ILE A 38 -17.251 3.762 -25.865 1.00 90.55 C ANISOU 92 CA ILE A 38 12063 9583 12759 1010 4367 4953 C ATOM 93 C ILE A 38 -18.580 3.334 -26.482 1.00 86.49 C ANISOU 93 C ILE A 38 11899 9444 11521 1451 4039 4931 C ATOM 94 O ILE A 38 -19.630 3.828 -26.051 1.00 89.08 O ANISOU 94 O ILE A 38 12314 9693 11841 1547 3717 4822 O ATOM 95 CB ILE A 38 -17.060 3.151 -24.463 1.00 88.97 C ANISOU 95 CB ILE A 38 11465 9430 12910 649 3972 4404 C ATOM 96 CG1 ILE A 38 -15.607 3.363 -24.013 1.00 92.52 C ANISOU 96 CG1 ILE A 38 11540 9588 14025 249 4272 4403 C ATOM 97 CG2 ILE A 38 -17.456 1.674 -24.430 1.00 81.43 C ANISOU 97 CG2 ILE A 38 10487 8998 11455 762 3624 4063 C ATOM 98 CD1 ILE A 38 -15.256 2.720 -22.695 1.00 91.86 C ANISOU 98 CD1 ILE A 38 11083 9565 14255 -71 3896 3884 C ATOM 99 N PRO A 39 -18.582 2.446 -27.479 1.00 87.49 N ANISOU 99 N PRO A 39 12218 9970 11054 1736 4096 5010 N ATOM 100 CA PRO A 39 -19.829 2.110 -28.169 1.00 86.95 C ANISOU 100 CA PRO A 39 12486 10238 10314 2179 3766 4991 C ATOM 101 C PRO A 39 -20.666 1.135 -27.362 1.00 86.70 C ANISOU 101 C PRO A 39 12261 10506 10174 2110 3179 4446 C ATOM 102 O PRO A 39 -20.190 0.485 -26.424 1.00 77.63 O ANISOU 102 O PRO A 39 10776 9387 9334 1770 3060 4101 O ATOM 103 CB PRO A 39 -19.343 1.466 -29.470 1.00 90.40 C ANISOU 103 CB PRO A 39 13180 10969 10197 2476 4060 5230 C ATOM 104 CG PRO A 39 -18.073 0.808 -29.087 1.00 88.61 C ANISOU 104 CG PRO A 39 12615 10746 10305 2128 4306 5097 C ATOM 105 CD PRO A 39 -17.448 1.658 -27.999 1.00 91.77 C ANISOU 105 CD PRO A 39 12666 10684 11519 1677 4436 5077 C ATOM 106 N GLY A 40 -21.935 1.027 -27.753 1.00 84.74 N ANISOU 106 N GLY A 40 12230 10480 9489 2454 2814 4378 N ATOM 107 CA GLY A 40 -22.814 0.083 -27.098 1.00 76.82 C ANISOU 107 CA GLY A 40 11044 9757 8387 2413 2292 3890 C ATOM 108 C GLY A 40 -24.299 0.289 -27.330 1.00 81.20 C ANISOU 108 C GLY A 40 11753 10443 8656 2747 1886 3822 C ATOM 109 O GLY A 40 -24.763 1.346 -27.790 1.00 80.83 O ANISOU 109 O GLY A 40 11944 10217 8551 3001 1956 4136 O ATOM 110 N PRO A 41 -25.081 -0.736 -26.981 1.00 75.15 N ANISOU 110 N PRO A 41 10830 9976 7748 2748 1450 3401 N ATOM 111 CA PRO A 41 -26.532 -0.656 -27.176 1.00 77.64 C ANISOU 111 CA PRO A 41 11212 10442 7845 3052 1027 3282 C ATOM 112 C PRO A 41 -27.149 0.414 -26.290 1.00 75.71 C ANISOU 112 C PRO A 41 10860 9885 8022 2973 966 3297 C ATOM 113 O PRO A 41 -26.860 0.514 -25.092 1.00 73.74 O ANISOU 113 O PRO A 41 10353 9434 8229 2612 1009 3112 O ATOM 114 CB PRO A 41 -27.015 -2.058 -26.797 1.00 78.35 C ANISOU 114 CB PRO A 41 11067 10851 7851 2950 651 2803 C ATOM 115 CG PRO A 41 -25.963 -2.578 -25.852 1.00 77.03 C ANISOU 115 CG PRO A 41 10647 10583 8037 2509 851 2644 C ATOM 116 CD PRO A 41 -24.672 -2.004 -26.346 1.00 74.23 C ANISOU 116 CD PRO A 41 10441 10044 7719 2462 1335 3019 C ATOM 117 N THR A 42 -28.005 1.206 -26.896 1.00 78.44 N ANISOU 117 N THR A 42 11423 10194 8185 3344 852 3508 N ATOM 118 CA THR A 42 -28.570 2.369 -26.222 1.00 82.63 C ANISOU 118 CA THR A 42 11912 10394 9090 3340 841 3585 C ATOM 119 C THR A 42 -29.554 1.940 -25.132 1.00 74.62 C ANISOU 119 C THR A 42 10567 9465 8321 3206 472 3142 C ATOM 120 O THR A 42 -30.456 1.137 -25.401 1.00 74.14 O ANISOU 120 O THR A 42 10419 9733 8016 3381 105 2899 O ATOM 121 CB THR A 42 -29.239 3.266 -27.259 1.00 91.14 C ANISOU 121 CB THR A 42 13332 11431 9864 3832 806 3949 C ATOM 122 OG1 THR A 42 -28.330 3.461 -28.348 1.00 91.47 O ANISOU 122 OG1 THR A 42 13708 11452 9594 3986 1173 4362 O ATOM 123 CG2 THR A 42 -29.587 4.619 -26.669 1.00 92.36 C ANISOU 123 CG2 THR A 42 13502 11161 10431 3837 902 4114 C ATOM 124 N PRO A 43 -29.399 2.428 -23.897 1.00 72.40 N ANISOU 124 N PRO A 43 10095 8891 8524 2902 567 3017 N ATOM 125 CA PRO A 43 -30.181 1.906 -22.767 1.00 71.42 C ANISOU 125 CA PRO A 43 9664 8853 8621 2745 300 2599 C ATOM 126 C PRO A 43 -31.519 2.609 -22.584 1.00 76.33 C ANISOU 126 C PRO A 43 10253 9409 9339 3012 79 2570 C ATOM 127 O PRO A 43 -31.665 3.810 -22.817 1.00 73.70 O ANISOU 127 O PRO A 43 10104 8802 9097 3201 192 2847 O ATOM 128 CB PRO A 43 -29.264 2.194 -21.572 1.00 66.55 C ANISOU 128 CB PRO A 43 8919 7936 8431 2336 532 2504 C ATOM 129 CG PRO A 43 -28.570 3.497 -21.976 1.00 79.04 C ANISOU 129 CG PRO A 43 10729 9135 10167 2373 855 2899 C ATOM 130 CD PRO A 43 -28.367 3.389 -23.457 1.00 73.20 C ANISOU 130 CD PRO A 43 10248 8566 8998 2660 947 3231 C ATOM 131 N LEU A 44 -32.505 1.847 -22.143 1.00 74.80 N ANISOU 131 N LEU A 44 9806 9452 9161 3028 -223 2233 N ATOM 132 CA LEU A 44 -33.780 2.468 -21.833 1.00 70.28 C ANISOU 132 CA LEU A 44 9133 8819 8753 3260 -414 2168 C ATOM 133 C LEU A 44 -33.726 3.114 -20.456 1.00 68.64 C ANISOU 133 C LEU A 44 8812 8289 8978 3028 -247 2048 C ATOM 134 O LEU A 44 -32.952 2.693 -19.594 1.00 73.40 O ANISOU 134 O LEU A 44 9326 8827 9735 2673 -101 1885 O ATOM 135 CB LEU A 44 -34.894 1.437 -21.865 1.00 69.57 C ANISOU 135 CB LEU A 44 8768 9079 8586 3357 -775 1850 C ATOM 136 CG LEU A 44 -35.258 0.926 -23.249 1.00 72.27 C ANISOU 136 CG LEU A 44 9219 9739 8502 3680 -1051 1910 C ATOM 137 CD1 LEU A 44 -36.280 -0.177 -23.118 1.00 76.91 C ANISOU 137 CD1 LEU A 44 9465 10628 9129 3688 -1408 1528 C ATOM 138 CD2 LEU A 44 -35.778 2.081 -24.111 1.00 77.07 C ANISOU 138 CD2 LEU A 44 10073 10250 8959 4132 -1128 2232 C ATOM 139 N PRO A 45 -34.550 4.126 -20.216 1.00 70.94 N ANISOU 139 N PRO A 45 9116 8379 9460 3250 -283 2108 N ATOM 140 CA PRO A 45 -34.654 4.669 -18.859 1.00 69.67 C ANISOU 140 CA PRO A 45 8848 7939 9683 3073 -158 1930 C ATOM 141 C PRO A 45 -35.040 3.585 -17.858 1.00 72.45 C ANISOU 141 C PRO A 45 8900 8504 10124 2856 -247 1541 C ATOM 142 O PRO A 45 -35.940 2.778 -18.103 1.00 73.21 O ANISOU 142 O PRO A 45 8786 8903 10126 2973 -472 1386 O ATOM 143 CB PRO A 45 -35.741 5.734 -18.991 1.00 73.22 C ANISOU 143 CB PRO A 45 9333 8230 10258 3443 -245 2039 C ATOM 144 CG PRO A 45 -35.667 6.147 -20.423 1.00 79.97 C ANISOU 144 CG PRO A 45 10446 9117 10821 3758 -293 2409 C ATOM 145 CD PRO A 45 -35.363 4.883 -21.180 1.00 75.26 C ANISOU 145 CD PRO A 45 9810 8921 9865 3702 -430 2353 C ATOM 146 N PHE A 46 -34.316 3.567 -16.734 1.00 65.53 N ANISOU 146 N PHE A 46 8011 7451 9438 2540 -67 1386 N ATOM 147 CA PHE A 46 -34.507 2.651 -15.608 1.00 60.78 C ANISOU 147 CA PHE A 46 7193 6980 8919 2325 -78 1053 C ATOM 148 C PHE A 46 -34.045 1.236 -15.937 1.00 59.82 C ANISOU 148 C PHE A 46 6973 7172 8582 2143 -151 960 C ATOM 149 O PHE A 46 -33.277 0.643 -15.175 1.00 66.90 O ANISOU 149 O PHE A 46 7847 8064 9506 1864 -56 815 O ATOM 150 CB PHE A 46 -35.971 2.643 -15.150 1.00 74.81 C ANISOU 150 CB PHE A 46 8751 8842 10831 2528 -184 885 C ATOM 151 CG PHE A 46 -36.508 4.006 -14.719 1.00 85.23 C ANISOU 151 CG PHE A 46 10155 9848 12381 2734 -104 940 C ATOM 152 CD1 PHE A 46 -37.319 4.753 -15.568 1.00 87.78 C ANISOU 152 CD1 PHE A 46 10502 10142 12707 3093 -226 1128 C ATOM 153 CD2 PHE A 46 -36.226 4.526 -13.456 1.00 91.77 C ANISOU 153 CD2 PHE A 46 11051 10408 13408 2598 73 785 C ATOM 154 CE1 PHE A 46 -37.836 6.003 -15.173 1.00 93.13 C ANISOU 154 CE1 PHE A 46 11260 10511 13614 3306 -148 1178 C ATOM 155 CE2 PHE A 46 -36.738 5.769 -13.060 1.00 94.78 C ANISOU 155 CE2 PHE A 46 11523 10483 14005 2804 146 808 C ATOM 156 CZ PHE A 46 -37.543 6.504 -13.922 1.00 95.22 C ANISOU 156 CZ PHE A 46 11590 10496 14092 3153 47 1011 C ATOM 157 N LEU A 47 -34.472 0.675 -17.071 1.00 65.16 N ANISOU 157 N LEU A 47 7607 8115 9034 2316 -336 1031 N ATOM 158 CA LEU A 47 -34.078 -0.700 -17.403 1.00 57.07 C ANISOU 158 CA LEU A 47 6497 7371 7814 2160 -416 912 C ATOM 159 C LEU A 47 -32.643 -0.833 -17.880 1.00 56.23 C ANISOU 159 C LEU A 47 6586 7233 7547 1999 -269 1071 C ATOM 160 O LEU A 47 -32.079 -1.935 -17.815 1.00 56.23 O ANISOU 160 O LEU A 47 6521 7397 7447 1807 -271 943 O ATOM 161 CB LEU A 47 -34.991 -1.275 -18.485 1.00 58.89 C ANISOU 161 CB LEU A 47 6627 7894 7855 2411 -700 888 C ATOM 162 CG LEU A 47 -36.449 -1.230 -18.071 1.00 60.17 C ANISOU 162 CG LEU A 47 6519 8106 8235 2568 -859 715 C ATOM 163 CD1 LEU A 47 -37.373 -1.627 -19.190 1.00 62.85 C ANISOU 163 CD1 LEU A 47 6743 8707 8428 2849 -1198 680 C ATOM 164 CD2 LEU A 47 -36.600 -2.169 -16.884 1.00 61.95 C ANISOU 164 CD2 LEU A 47 6509 8369 8659 2291 -770 438 C ATOM 165 N GLY A 48 -32.022 0.242 -18.340 1.00 72.38 N ANISOU 165 N GLY A 48 8853 9053 9595 2069 -117 1350 N ATOM 166 CA GLY A 48 -30.759 0.046 -19.024 1.00 58.23 C ANISOU 166 CA GLY A 48 7212 7269 7644 1960 38 1530 C ATOM 167 C GLY A 48 -31.003 -0.860 -20.209 1.00 58.95 C ANISOU 167 C GLY A 48 7331 7700 7366 2140 -128 1552 C ATOM 168 O GLY A 48 -31.941 -0.661 -20.977 1.00 68.78 O ANISOU 168 O GLY A 48 8619 9067 8446 2454 -322 1618 O ATOM 169 N ASN A 49 -30.197 -1.900 -20.340 1.00 57.05 N ANISOU 169 N ASN A 49 7060 7622 6993 1960 -86 1463 N ATOM 170 CA ASN A 49 -30.251 -2.771 -21.503 1.00 62.82 C ANISOU 170 CA ASN A 49 7862 8656 7352 2129 -224 1467 C ATOM 171 C ASN A 49 -30.887 -4.119 -21.205 1.00 63.96 C ANISOU 171 C ASN A 49 7778 9050 7475 2052 -471 1114 C ATOM 172 O ASN A 49 -30.818 -5.021 -22.048 1.00 65.59 O ANISOU 172 O ASN A 49 8025 9496 7401 2140 -597 1044 O ATOM 173 CB ASN A 49 -28.840 -2.982 -22.061 1.00 61.20 C ANISOU 173 CB ASN A 49 7810 8446 6995 2026 33 1645 C ATOM 174 CG ASN A 49 -28.173 -1.676 -22.467 1.00 66.95 C ANISOU 174 CG ASN A 49 8756 8903 7780 2094 325 2029 C ATOM 175 OD1 ASN A 49 -27.400 -1.097 -21.704 1.00 68.93 O ANISOU 175 OD1 ASN A 49 8957 8875 8357 1847 546 2080 O ATOM 176 ND2 ASN A 49 -28.488 -1.196 -23.667 1.00 64.62 N ANISOU 176 ND2 ASN A 49 8707 8670 7175 2441 317 2297 N ATOM 177 N ILE A 50 -31.517 -4.281 -20.038 1.00 57.78 N ANISOU 177 N ILE A 50 6768 8201 6986 1900 -526 891 N ATOM 178 CA ILE A 50 -31.870 -5.634 -19.606 1.00 59.69 C ANISOU 178 CA ILE A 50 6792 8617 7270 1751 -662 584 C ATOM 179 C ILE A 50 -32.836 -6.309 -20.557 1.00 61.34 C ANISOU 179 C ILE A 50 6922 9079 7304 1971 -978 451 C ATOM 180 O ILE A 50 -32.887 -7.541 -20.607 1.00 67.34 O ANISOU 180 O ILE A 50 7563 9993 8031 1866 -1092 226 O ATOM 181 CB ILE A 50 -32.448 -5.646 -18.182 1.00 54.56 C ANISOU 181 CB ILE A 50 5935 7842 6953 1585 -617 402 C ATOM 182 CG1 ILE A 50 -33.701 -4.784 -18.120 1.00 68.04 C ANISOU 182 CG1 ILE A 50 7552 9493 8807 1805 -726 419 C ATOM 183 CG2 ILE A 50 -31.406 -5.156 -17.200 1.00 59.53 C ANISOU 183 CG2 ILE A 50 6652 8242 7722 1364 -363 464 C ATOM 184 CD1 ILE A 50 -34.778 -5.391 -17.295 1.00 78.92 C ANISOU 184 CD1 ILE A 50 8638 10919 10428 1745 -800 169 C ATOM 185 N LEU A 51 -33.589 -5.537 -21.342 1.00 61.60 N ANISOU 185 N LEU A 51 7026 9151 7228 2287 -1144 574 N ATOM 186 CA LEU A 51 -34.549 -6.163 -22.239 1.00 67.47 C ANISOU 186 CA LEU A 51 7676 10143 7817 2518 -1514 404 C ATOM 187 C LEU A 51 -33.858 -6.996 -23.309 1.00 68.79 C ANISOU 187 C LEU A 51 8033 10510 7593 2584 -1588 385 C ATOM 188 O LEU A 51 -34.485 -7.889 -23.894 1.00 70.70 O ANISOU 188 O LEU A 51 8171 10960 7732 2687 -1908 138 O ATOM 189 CB LEU A 51 -35.451 -5.098 -22.864 1.00 64.91 C ANISOU 189 CB LEU A 51 7411 9819 7432 2890 -1700 556 C ATOM 190 CG LEU A 51 -36.462 -4.522 -21.871 1.00 70.90 C ANISOU 190 CG LEU A 51 7901 10435 8605 2872 -1709 476 C ATOM 191 CD1 LEU A 51 -37.502 -3.645 -22.578 1.00 70.42 C ANISOU 191 CD1 LEU A 51 7847 10412 8496 3285 -1970 577 C ATOM 192 CD2 LEU A 51 -37.138 -5.633 -21.094 1.00 71.41 C ANISOU 192 CD2 LEU A 51 7585 10575 8971 2648 -1804 125 C ATOM 193 N SER A 52 -32.578 -6.739 -23.559 1.00 65.15 N ANISOU 193 N SER A 52 7833 9978 6942 2525 -1295 621 N ATOM 194 CA SER A 52 -31.827 -7.480 -24.557 1.00 69.35 C ANISOU 194 CA SER A 52 8569 10691 7091 2607 -1296 626 C ATOM 195 C SER A 52 -31.404 -8.850 -24.064 1.00 73.43 C ANISOU 195 C SER A 52 8923 11269 7708 2321 -1287 343 C ATOM 196 O SER A 52 -30.884 -9.640 -24.856 1.00 76.28 O ANISOU 196 O SER A 52 9423 11789 7772 2392 -1321 277 O ATOM 197 CB SER A 52 -30.596 -6.685 -24.974 1.00 74.95 C ANISOU 197 CB SER A 52 9577 11280 7619 2641 -927 1002 C ATOM 198 OG SER A 52 -30.950 -5.655 -25.878 1.00 84.56 O ANISOU 198 OG SER A 52 11042 12495 8591 3002 -963 1283 O ATOM 199 N TYR A 53 -31.603 -9.136 -22.780 1.00 72.49 N ANISOU 199 N TYR A 53 8544 11020 7981 2029 -1224 188 N ATOM 200 CA TYR A 53 -31.406 -10.467 -22.223 1.00 66.49 C ANISOU 200 CA TYR A 53 7615 10294 7352 1779 -1237 -82 C ATOM 201 C TYR A 53 -32.526 -11.434 -22.585 1.00 74.69 C ANISOU 201 C TYR A 53 8461 11487 8431 1850 -1597 -403 C ATOM 202 O TYR A 53 -32.542 -12.547 -22.058 1.00 81.17 O ANISOU 202 O TYR A 53 9115 12295 9429 1636 -1611 -635 O ATOM 203 CB TYR A 53 -31.286 -10.381 -20.704 1.00 61.61 C ANISOU 203 CB TYR A 53 6825 9476 7109 1485 -1034 -110 C ATOM 204 CG TYR A 53 -29.996 -9.764 -20.217 1.00 60.61 C ANISOU 204 CG TYR A 53 6841 9191 6999 1344 -717 108 C ATOM 205 CD1 TYR A 53 -29.982 -8.884 -19.130 1.00 63.67 C ANISOU 205 CD1 TYR A 53 7181 9368 7643 1225 -564 189 C ATOM 206 CD2 TYR A 53 -28.785 -10.086 -20.814 1.00 65.12 C ANISOU 206 CD2 TYR A 53 7573 9813 7357 1329 -575 207 C ATOM 207 CE1 TYR A 53 -28.783 -8.324 -18.667 1.00 70.26 C ANISOU 207 CE1 TYR A 53 8116 10039 8541 1083 -319 344 C ATOM 208 CE2 TYR A 53 -27.576 -9.546 -20.353 1.00 75.76 C ANISOU 208 CE2 TYR A 53 8988 11003 8794 1180 -296 385 C ATOM 209 CZ TYR A 53 -27.579 -8.668 -19.287 1.00 76.66 C ANISOU 209 CZ TYR A 53 9041 10902 9185 1050 -191 442 C ATOM 210 OH TYR A 53 -26.386 -8.133 -18.852 1.00 68.76 O ANISOU 210 OH TYR A 53 8081 9734 8312 897 37 577 O ATOM 211 N HIS A 54 -33.463 -11.044 -23.456 1.00 75.84 N ANISOU 211 N HIS A 54 8616 11759 8441 2146 -1898 -429 N ATOM 212 CA HIS A 54 -34.573 -11.933 -23.783 1.00 88.22 C ANISOU 212 CA HIS A 54 9944 13456 10117 2203 -2286 -776 C ATOM 213 C HIS A 54 -34.100 -13.216 -24.446 1.00 84.87 C ANISOU 213 C HIS A 54 9606 13160 9481 2180 -2409 -1003 C ATOM 214 O HIS A 54 -34.777 -14.244 -24.332 1.00 85.13 O ANISOU 214 O HIS A 54 9388 13214 9745 2072 -2638 -1336 O ATOM 215 CB HIS A 54 -35.607 -11.229 -24.681 1.00 96.17 C ANISOU 215 CB HIS A 54 10958 14594 10987 2576 -2641 -769 C ATOM 216 CG HIS A 54 -35.136 -10.957 -26.082 1.00103.24 C ANISOU 216 CG HIS A 54 12244 15666 11317 2929 -2760 -630 C ATOM 217 ND1 HIS A 54 -34.121 -10.069 -26.371 1.00105.43 N ANISOU 217 ND1 HIS A 54 12872 15885 11303 3026 -2433 -243 N ATOM 218 CD2 HIS A 54 -35.567 -11.434 -27.276 1.00108.83 C ANISOU 218 CD2 HIS A 54 13057 16599 11693 3229 -3165 -824 C ATOM 219 CE1 HIS A 54 -33.939 -10.021 -27.680 1.00108.39 C ANISOU 219 CE1 HIS A 54 13570 16445 11168 3378 -2583 -171 C ATOM 220 NE2 HIS A 54 -34.805 -10.838 -28.252 1.00108.79 N ANISOU 220 NE2 HIS A 54 13499 16683 11154 3524 -3047 -531 N ATOM 221 N LYS A 55 -32.947 -13.184 -25.114 1.00 79.25 N ANISOU 221 N LYS A 55 9230 12512 8371 2274 -2238 -833 N ATOM 222 CA LYS A 55 -32.345 -14.383 -25.680 1.00 78.39 C ANISOU 222 CA LYS A 55 9231 12503 8049 2258 -2290 -1035 C ATOM 223 C LYS A 55 -31.201 -14.926 -24.840 1.00 81.05 C ANISOU 223 C LYS A 55 9563 12704 8528 1949 -1923 -980 C ATOM 224 O LYS A 55 -30.449 -15.775 -25.328 1.00 91.19 O ANISOU 224 O LYS A 55 10990 14056 9601 1960 -1882 -1077 O ATOM 225 CB LYS A 55 -31.863 -14.110 -27.101 1.00 77.42 C ANISOU 225 CB LYS A 55 9497 12572 7345 2628 -2350 -910 C ATOM 226 CG LYS A 55 -32.996 -13.683 -27.997 1.00 85.94 C ANISOU 226 CG LYS A 55 10611 13812 8229 2987 -2781 -996 C ATOM 227 CD LYS A 55 -32.663 -13.773 -29.468 1.00 94.88 C ANISOU 227 CD LYS A 55 12147 15171 8732 3392 -2928 -981 C ATOM 228 CE LYS A 55 -33.941 -13.544 -30.273 1.00103.77 C ANISOU 228 CE LYS A 55 13257 16435 9736 3721 -3435 -1156 C ATOM 229 NZ LYS A 55 -33.793 -13.868 -31.714 1.00113.02 N ANISOU 229 NZ LYS A 55 14798 17718 10427 4018 -3535 -1228 N ATOM 230 N GLY A 56 -31.050 -14.465 -23.596 1.00 68.12 N ANISOU 230 N GLY A 56 7776 10879 7228 1701 -1671 -842 N ATOM 231 CA GLY A 56 -30.023 -14.971 -22.712 1.00 65.98 C ANISOU 231 CA GLY A 56 7486 10481 7104 1429 -1376 -809 C ATOM 232 C GLY A 56 -28.687 -14.257 -22.864 1.00 64.24 C ANISOU 232 C GLY A 56 7487 10229 6691 1450 -1057 -501 C ATOM 233 O GLY A 56 -28.456 -13.474 -23.794 1.00 60.07 O ANISOU 233 O GLY A 56 7173 9781 5872 1683 -1020 -294 O ATOM 234 N PHE A 57 -27.781 -14.561 -21.918 1.00 55.32 N ANISOU 234 N PHE A 57 6299 8972 5749 1206 -817 -468 N ATOM 235 CA PHE A 57 -26.507 -13.837 -21.810 1.00 62.43 C ANISOU 235 CA PHE A 57 7317 9795 6609 1162 -508 -197 C ATOM 236 C PHE A 57 -25.641 -14.031 -23.048 1.00 59.89 C ANISOU 236 C PHE A 57 7211 9612 5932 1349 -402 -98 C ATOM 237 O PHE A 57 -25.073 -13.071 -23.584 1.00 70.16 O ANISOU 237 O PHE A 57 8663 10898 7095 1463 -202 184 O ATOM 238 CB PHE A 57 -25.717 -14.303 -20.573 1.00 58.71 C ANISOU 238 CB PHE A 57 6721 9184 6401 890 -345 -241 C ATOM 239 CG PHE A 57 -26.272 -13.823 -19.270 1.00 58.92 C ANISOU 239 CG PHE A 57 6605 9051 6731 730 -345 -256 C ATOM 240 CD1 PHE A 57 -26.631 -14.720 -18.288 1.00 59.71 C ANISOU 240 CD1 PHE A 57 6569 9092 7026 572 -393 -447 C ATOM 241 CD2 PHE A 57 -26.417 -12.466 -19.022 1.00 66.25 C ANISOU 241 CD2 PHE A 57 7559 9872 7742 754 -270 -70 C ATOM 242 CE1 PHE A 57 -27.149 -14.274 -17.081 1.00 66.40 C ANISOU 242 CE1 PHE A 57 7321 9801 8107 460 -356 -452 C ATOM 243 CE2 PHE A 57 -26.928 -12.015 -17.833 1.00 69.91 C ANISOU 243 CE2 PHE A 57 7919 10190 8453 638 -262 -104 C ATOM 244 CZ PHE A 57 -27.291 -12.916 -16.858 1.00 69.76 C ANISOU 244 CZ PHE A 57 7779 10140 8589 500 -298 -293 C ATOM 245 N CYS A 58 -25.519 -15.272 -23.500 1.00 60.35 N ANISOU 245 N CYS A 58 7296 9786 5850 1387 -505 -323 N ATOM 246 CA CYS A 58 -24.580 -15.606 -24.561 1.00 66.13 C ANISOU 246 CA CYS A 58 8235 10646 6245 1564 -358 -257 C ATOM 247 C CYS A 58 -24.938 -14.918 -25.876 1.00 72.01 C ANISOU 247 C CYS A 58 9235 11541 6583 1905 -415 -111 C ATOM 248 O CYS A 58 -24.069 -14.337 -26.533 1.00 70.51 O ANISOU 248 O CYS A 58 9234 11378 6177 2041 -127 166 O ATOM 249 CB CYS A 58 -24.541 -17.119 -24.694 1.00 68.84 C ANISOU 249 CB CYS A 58 8553 11056 6549 1543 -498 -579 C ATOM 250 SG CYS A 58 -24.224 -17.875 -23.058 1.00 70.49 S ANISOU 250 SG CYS A 58 8493 11063 7226 1176 -431 -705 S ATOM 251 N MET A 59 -26.213 -14.951 -26.265 1.00 71.40 N ANISOU 251 N MET A 59 9163 11556 6409 2058 -776 -280 N ATOM 252 CA MET A 59 -26.630 -14.278 -27.494 1.00 76.73 C ANISOU 252 CA MET A 59 10106 12383 6664 2430 -884 -145 C ATOM 253 C MET A 59 -26.371 -12.775 -27.428 1.00 80.49 C ANISOU 253 C MET A 59 10673 12744 7167 2475 -621 273 C ATOM 254 O MET A 59 -25.878 -12.178 -28.395 1.00 80.06 O ANISOU 254 O MET A 59 10908 12756 6756 2736 -426 550 O ATOM 255 CB MET A 59 -28.109 -14.551 -27.762 1.00 74.48 C ANISOU 255 CB MET A 59 9737 12200 6363 2566 -1375 -433 C ATOM 256 CG MET A 59 -28.433 -16.014 -28.025 1.00 95.23 C ANISOU 256 CG MET A 59 12504 15028 8653 2786 -1679 -764 C ATOM 257 SD MET A 59 -27.646 -16.689 -29.503 1.00111.24 S ANISOU 257 SD MET A 59 14564 17044 10656 2635 -1457 -932 S ATOM 258 CE MET A 59 -26.299 -17.646 -28.805 1.00107.82 C ANISOU 258 CE MET A 59 13703 16396 10866 2183 -1539 -1190 C ATOM 259 N PHE A 60 -26.698 -12.144 -26.299 1.00 70.30 N ANISOU 259 N PHE A 60 9154 11259 6296 2237 -593 329 N ATOM 260 CA PHE A 60 -26.462 -10.713 -26.173 1.00 69.72 C ANISOU 260 CA PHE A 60 9158 11027 6306 2260 -354 696 C ATOM 261 C PHE A 60 -24.981 -10.387 -26.331 1.00 70.86 C ANISOU 261 C PHE A 60 9411 11082 6430 2189 97 979 C ATOM 262 O PHE A 60 -24.615 -9.421 -27.012 1.00 71.98 O ANISOU 262 O PHE A 60 9769 11176 6406 2367 333 1323 O ATOM 263 CB PHE A 60 -26.996 -10.210 -24.827 1.00 61.81 C ANISOU 263 CB PHE A 60 7892 9821 5771 2003 -396 648 C ATOM 264 CG PHE A 60 -26.822 -8.736 -24.629 1.00 66.57 C ANISOU 264 CG PHE A 60 8567 10219 6507 2018 -181 981 C ATOM 265 CD1 PHE A 60 -27.443 -7.835 -25.480 1.00 73.51 C ANISOU 265 CD1 PHE A 60 9647 11126 7157 2335 -254 1189 C ATOM 266 CD2 PHE A 60 -26.034 -8.242 -23.602 1.00 62.00 C ANISOU 266 CD2 PHE A 60 7866 9405 6286 1731 75 1076 C ATOM 267 CE1 PHE A 60 -27.282 -6.471 -25.313 1.00 73.42 C ANISOU 267 CE1 PHE A 60 9718 10884 7296 2353 -40 1506 C ATOM 268 CE2 PHE A 60 -25.880 -6.873 -23.423 1.00 67.16 C ANISOU 268 CE2 PHE A 60 8583 9828 7105 1733 262 1354 C ATOM 269 CZ PHE A 60 -26.505 -5.989 -24.285 1.00 70.64 C ANISOU 269 CZ PHE A 60 9229 10273 7337 2039 222 1580 C ATOM 270 N ASP A 61 -24.116 -11.207 -25.733 1.00 64.01 N ANISOU 270 N ASP A 61 8390 10184 5748 1942 229 845 N ATOM 271 CA ASP A 61 -22.682 -10.947 -25.789 1.00 68.00 C ANISOU 271 CA ASP A 61 8917 10597 6325 1847 646 1082 C ATOM 272 C ASP A 61 -22.118 -11.149 -27.196 1.00 71.62 C ANISOU 272 C ASP A 61 9662 11231 6322 2151 842 1238 C ATOM 273 O ASP A 61 -21.271 -10.363 -27.637 1.00 71.06 O ANISOU 273 O ASP A 61 9700 11070 6228 2204 1230 1585 O ATOM 274 CB ASP A 61 -21.945 -11.824 -24.784 1.00 58.79 C ANISOU 274 CB ASP A 61 7501 9369 5466 1546 689 878 C ATOM 275 CG ASP A 61 -22.169 -11.390 -23.348 1.00 59.20 C ANISOU 275 CG ASP A 61 7320 9214 5961 1259 616 813 C ATOM 276 OD1 ASP A 61 -22.801 -10.331 -23.110 1.00 62.55 O ANISOU 276 OD1 ASP A 61 7759 9517 6491 1273 576 937 O ATOM 277 OD2 ASP A 61 -21.684 -12.106 -22.449 1.00 58.11 O ANISOU 277 OD2 ASP A 61 7003 9029 6046 1044 605 640 O ATOM 278 N MET A 62 -22.565 -12.187 -27.915 1.00 66.56 N ANISOU 278 N MET A 62 9149 10822 5317 2358 599 984 N ATOM 279 CA AMET A 62 -22.095 -12.394 -29.284 0.63 73.07 C ANISOU 279 CA AMET A 62 10300 11833 5629 2702 770 1106 C ATOM 280 CA BMET A 62 -22.085 -12.389 -29.279 0.37 72.97 C ANISOU 280 CA BMET A 62 10287 11819 5619 2700 774 1109 C ATOM 281 C MET A 62 -22.523 -11.250 -30.195 1.00 75.30 C ANISOU 281 C MET A 62 10889 12141 5581 3029 833 1439 C ATOM 282 O MET A 62 -21.735 -10.769 -31.018 1.00 77.50 O ANISOU 282 O MET A 62 11412 12431 5604 3225 1232 1776 O ATOM 283 CB AMET A 62 -22.617 -13.724 -29.828 0.63 75.81 C ANISOU 283 CB AMET A 62 10737 12407 5661 2870 419 704 C ATOM 284 CB BMET A 62 -22.573 -13.733 -29.821 0.37 75.83 C ANISOU 284 CB BMET A 62 10737 12407 5667 2865 433 708 C ATOM 285 CG AMET A 62 -22.151 -14.943 -29.057 0.63 75.19 C ANISOU 285 CG AMET A 62 10411 12292 5867 2596 386 398 C ATOM 286 CG BMET A 62 -22.110 -14.934 -29.007 0.37 74.99 C ANISOU 286 CG BMET A 62 10373 12258 5864 2579 399 404 C ATOM 287 SD AMET A 62 -20.518 -15.513 -29.560 0.63 77.83 S ANISOU 287 SD AMET A 62 10831 12676 6066 2650 857 508 S ATOM 288 SD BMET A 62 -22.643 -16.523 -29.688 0.37 77.54 S ANISOU 288 SD BMET A 62 10810 12786 5864 2766 17 -80 S ATOM 289 CE AMET A 62 -20.817 -16.055 -31.247 0.63 82.52 C ANISOU 289 CE AMET A 62 11877 13561 5916 3163 746 397 C ATOM 290 CE BMET A 62 -21.514 -16.715 -31.069 0.37 83.16 C ANISOU 290 CE BMET A 62 11895 13676 6025 3130 392 86 C ATOM 291 N GLU A 63 -23.775 -10.812 -30.073 1.00 73.66 N ANISOU 291 N GLU A 63 10675 11936 5377 3113 461 1362 N ATOM 292 CA GLU A 63 -24.257 -9.724 -30.912 1.00 86.58 C ANISOU 292 CA GLU A 63 12612 13588 6695 3459 478 1678 C ATOM 293 C GLU A 63 -23.458 -8.457 -30.654 1.00 90.32 C ANISOU 293 C GLU A 63 13097 13791 7430 3337 966 2143 C ATOM 294 O GLU A 63 -22.962 -7.817 -31.590 1.00 92.45 O ANISOU 294 O GLU A 63 13682 14058 7387 3603 1305 2524 O ATOM 295 CB GLU A 63 -25.736 -9.471 -30.649 1.00 93.00 C ANISOU 295 CB GLU A 63 13331 14425 7578 3534 -20 1491 C ATOM 296 CG GLU A 63 -26.666 -10.617 -30.980 1.00102.26 C ANISOU 296 CG GLU A 63 14469 15840 8544 3667 -542 1027 C ATOM 297 CD GLU A 63 -28.123 -10.243 -30.733 1.00116.50 C ANISOU 297 CD GLU A 63 16129 17651 10485 3747 -1002 876 C ATOM 298 OE1 GLU A 63 -28.403 -9.037 -30.529 1.00118.56 O ANISOU 298 OE1 GLU A 63 16412 17761 10873 3796 -907 1170 O ATOM 299 OE2 GLU A 63 -28.983 -11.150 -30.735 1.00122.11 O ANISOU 299 OE2 GLU A 63 16684 18498 11215 3758 -1448 459 O ATOM 300 N CYS A 64 -23.313 -8.090 -29.379 1.00 88.53 N ANISOU 300 N CYS A 64 12536 13318 7785 2940 1015 2111 N ATOM 301 CA CYS A 64 -22.553 -6.899 -29.026 1.00 84.36 C ANISOU 301 CA CYS A 64 11971 12487 7596 2778 1437 2491 C ATOM 302 C CYS A 64 -21.126 -6.986 -29.535 1.00 80.14 C ANISOU 302 C CYS A 64 11504 11926 7021 2755 1950 2736 C ATOM 303 O CYS A 64 -20.600 -6.020 -30.105 1.00 87.12 O ANISOU 303 O CYS A 64 12571 12659 7873 2870 2356 3165 O ATOM 304 CB CYS A 64 -22.569 -6.703 -27.520 1.00 76.36 C ANISOU 304 CB CYS A 64 10586 11243 7185 2358 1352 2320 C ATOM 305 SG CYS A 64 -24.069 -5.935 -26.936 1.00 77.20 S ANISOU 305 SG CYS A 64 10641 11250 7443 2403 973 2239 S ATOM 306 N HIS A 65 -20.494 -8.143 -29.360 1.00 72.78 N ANISOU 306 N HIS A 65 10421 11126 6104 2623 1960 2482 N ATOM 307 CA HIS A 65 -19.159 -8.348 -29.914 1.00 85.46 C ANISOU 307 CA HIS A 65 12071 12744 7657 2641 2448 2686 C ATOM 308 C HIS A 65 -19.121 -8.070 -31.417 1.00 93.06 C ANISOU 308 C HIS A 65 13485 13857 8016 3101 2697 3001 C ATOM 309 O HIS A 65 -18.335 -7.240 -31.895 1.00103.03 O ANISOU 309 O HIS A 65 14862 14967 9318 3158 3213 3436 O ATOM 310 CB HIS A 65 -18.688 -9.767 -29.622 1.00 79.63 C ANISOU 310 CB HIS A 65 11152 12168 6936 2518 2343 2321 C ATOM 311 CG HIS A 65 -17.230 -9.969 -29.888 1.00 93.07 C ANISOU 311 CG HIS A 65 12775 13840 8749 2459 2846 2495 C ATOM 312 ND1 HIS A 65 -16.366 -8.915 -30.100 1.00 95.67 N ANISOU 312 ND1 HIS A 65 13088 13955 9307 2408 3357 2924 N ATOM 313 CD2 HIS A 65 -16.482 -11.094 -29.974 1.00 93.24 C ANISOU 313 CD2 HIS A 65 12702 13998 8726 2446 2933 2299 C ATOM 314 CE1 HIS A 65 -15.148 -9.383 -30.298 1.00 99.27 C ANISOU 314 CE1 HIS A 65 13414 14431 9872 2357 3741 2983 C ATOM 315 NE2 HIS A 65 -15.191 -10.702 -30.227 1.00 96.61 N ANISOU 315 NE2 HIS A 65 13037 14313 9357 2393 3489 2607 N ATOM 316 N LYS A 66 -19.956 -8.771 -32.182 1.00 92.86 N ANISOU 316 N LYS A 66 13729 14125 7429 3445 2341 2783 N ATOM 317 CA LYS A 66 -19.990 -8.554 -33.622 1.00 85.45 C ANISOU 317 CA LYS A 66 13263 13348 5857 3929 2508 3032 C ATOM 318 C LYS A 66 -20.303 -7.095 -33.956 1.00 93.18 C ANISOU 318 C LYS A 66 14417 14102 6883 4053 2659 3445 C ATOM 319 O LYS A 66 -19.601 -6.464 -34.754 1.00 99.49 O ANISOU 319 O LYS A 66 15382 14757 7664 4164 3085 3767 O ATOM 320 CB LYS A 66 -21.009 -9.507 -34.257 1.00 86.27 C ANISOU 320 CB LYS A 66 13549 13742 5488 4218 1938 2606 C ATOM 321 CG LYS A 66 -21.575 -9.037 -35.600 1.00 95.19 C ANISOU 321 CG LYS A 66 15064 14921 6182 4645 1824 2710 C ATOM 322 CD LYS A 66 -22.205 -10.183 -36.401 1.00 99.79 C ANISOU 322 CD LYS A 66 15803 15766 6347 4907 1360 2258 C ATOM 323 CE LYS A 66 -23.020 -9.670 -37.607 1.00 99.92 C ANISOU 323 CE LYS A 66 16173 15846 5946 5340 1136 2313 C ATOM 324 NZ LYS A 66 -22.251 -8.740 -38.497 1.00105.21 N ANISOU 324 NZ LYS A 66 17127 16384 6465 5546 1673 2791 N ATOM 325 N LYS A 67 -21.330 -6.528 -33.321 1.00 94.70 N ANISOU 325 N LYS A 67 14553 14233 7194 4024 2323 3432 N ATOM 326 CA LYS A 67 -21.792 -5.191 -33.682 1.00104.32 C ANISOU 326 CA LYS A 67 15972 15250 8414 4200 2399 3789 C ATOM 327 C LYS A 67 -20.748 -4.127 -33.357 1.00103.41 C ANISOU 327 C LYS A 67 15749 14753 8789 3943 2997 4219 C ATOM 328 O LYS A 67 -20.495 -3.227 -34.168 1.00101.41 O ANISOU 328 O LYS A 67 15715 14327 8489 4114 3297 4544 O ATOM 329 CB LYS A 67 -23.103 -4.878 -32.957 1.00106.90 C ANISOU 329 CB LYS A 67 16174 15557 8886 4177 1879 3607 C ATOM 330 CG LYS A 67 -23.976 -3.842 -33.638 1.00108.75 C ANISOU 330 CG LYS A 67 16706 15732 8882 4543 1751 3852 C ATOM 331 CD LYS A 67 -25.052 -3.317 -32.695 1.00115.11 C ANISOU 331 CD LYS A 67 17297 16414 10025 4437 1366 3737 C ATOM 332 CE LYS A 67 -25.704 -4.442 -31.893 1.00122.34 C ANISOU 332 CE LYS A 67 17843 17506 11133 4199 862 3152 C ATOM 333 NZ LYS A 67 -26.564 -3.958 -30.762 1.00123.96 N ANISOU 333 NZ LYS A 67 17732 17527 11841 3971 590 2989 N ATOM 334 N TYR A 68 -20.143 -4.205 -32.168 1.00 97.91 N ANISOU 334 N TYR A 68 14650 13877 8674 3484 3116 4132 N ATOM 335 CA TYR A 68 -19.332 -3.120 -31.640 1.00 95.19 C ANISOU 335 CA TYR A 68 14128 13121 8918 3185 3566 4464 C ATOM 336 C TYR A 68 -17.842 -3.429 -31.576 1.00 96.58 C ANISOU 336 C TYR A 68 14086 13214 9397 2936 4072 4563 C ATOM 337 O TYR A 68 -17.055 -2.524 -31.270 1.00 92.82 O ANISOU 337 O TYR A 68 13433 12374 9460 2682 4453 4814 O ATOM 338 CB TYR A 68 -19.817 -2.722 -30.236 1.00 87.00 C ANISOU 338 CB TYR A 68 12733 11850 8472 2808 3240 4212 C ATOM 339 CG TYR A 68 -21.267 -2.308 -30.185 1.00 84.98 C ANISOU 339 CG TYR A 68 12622 11632 8033 3025 2782 4126 C ATOM 340 CD1 TYR A 68 -22.215 -3.100 -29.533 1.00 79.30 C ANISOU 340 CD1 TYR A 68 11719 11111 7301 2960 2227 3650 C ATOM 341 CD2 TYR A 68 -21.690 -1.135 -30.786 1.00 86.72 C ANISOU 341 CD2 TYR A 68 13150 11679 8121 3305 2921 4531 C ATOM 342 CE1 TYR A 68 -23.533 -2.736 -29.488 1.00 78.40 C ANISOU 342 CE1 TYR A 68 11683 11034 7072 3158 1825 3564 C ATOM 343 CE2 TYR A 68 -23.014 -0.758 -30.738 1.00 92.91 C ANISOU 343 CE2 TYR A 68 14037 12502 8762 3527 2489 4445 C ATOM 344 CZ TYR A 68 -23.929 -1.559 -30.087 1.00 86.52 C ANISOU 344 CZ TYR A 68 13000 11904 7970 3448 1942 3953 C ATOM 345 OH TYR A 68 -25.249 -1.183 -30.049 1.00 91.31 O ANISOU 345 OH TYR A 68 13663 12551 8482 3673 1528 3866 O ATOM 346 N GLY A 69 -17.432 -4.666 -31.826 1.00102.48 N ANISOU 346 N GLY A 69 14791 14253 9894 2978 4038 4310 N ATOM 347 CA GLY A 69 -16.017 -4.975 -31.975 1.00111.17 C ANISOU 347 CA GLY A 69 15681 15277 11283 2798 4468 4353 C ATOM 348 C GLY A 69 -15.369 -5.423 -30.677 1.00105.82 C ANISOU 348 C GLY A 69 14510 14509 11189 2345 4446 4117 C ATOM 349 O GLY A 69 -15.868 -6.325 -30.012 1.00109.71 O ANISOU 349 O GLY A 69 14852 15167 11666 2241 3966 3671 O ATOM 350 N LYS A 70 -14.259 -4.774 -30.313 1.00100.34 N ANISOU 350 N LYS A 70 13523 13501 11100 2047 4860 4321 N ATOM 351 CA LYS A 70 -13.367 -5.261 -29.262 1.00 97.66 C ANISOU 351 CA LYS A 70 12692 13080 11334 1648 4855 4074 C ATOM 352 C LYS A 70 -13.767 -4.832 -27.851 1.00 88.47 C ANISOU 352 C LYS A 70 11236 11688 10689 1290 4446 3812 C ATOM 353 O LYS A 70 -13.381 -5.497 -26.883 1.00 75.16 O ANISOU 353 O LYS A 70 9212 10023 9320 1027 4214 3468 O ATOM 354 CB LYS A 70 -11.934 -4.787 -29.535 1.00101.16 C ANISOU 354 CB LYS A 70 12904 13271 12262 1479 5334 4277 C ATOM 355 CG LYS A 70 -11.796 -3.286 -29.424 1.00113.48 C ANISOU 355 CG LYS A 70 14430 14407 14281 1326 5538 4569 C ATOM 356 CD LYS A 70 -10.356 -2.824 -29.363 1.00123.52 C ANISOU 356 CD LYS A 70 15349 15388 16195 1063 5897 4657 C ATOM 357 CE LYS A 70 -10.287 -1.415 -28.772 1.00126.81 C ANISOU 357 CE LYS A 70 15615 15347 17222 797 5962 4804 C ATOM 358 NZ LYS A 70 -11.150 -0.441 -29.507 1.00127.68 N ANISOU 358 NZ LYS A 70 16156 15340 17017 1066 6052 5126 N ATOM 359 N VAL A 71 -14.499 -3.729 -27.705 1.00 83.91 N ANISOU 359 N VAL A 71 10797 10886 10199 1296 4366 3973 N ATOM 360 CA VAL A 71 -14.870 -3.173 -26.409 1.00 77.03 C ANISOU 360 CA VAL A 71 9691 9765 9810 990 4034 3753 C ATOM 361 C VAL A 71 -16.259 -2.568 -26.564 1.00 85.68 C ANISOU 361 C VAL A 71 11099 10854 10603 1213 3758 3804 C ATOM 362 O VAL A 71 -16.565 -1.967 -27.599 1.00 93.94 O ANISOU 362 O VAL A 71 12483 11884 11327 1511 3990 4170 O ATOM 363 CB VAL A 71 -13.859 -2.101 -25.929 1.00 89.66 C ANISOU 363 CB VAL A 71 11006 10925 12136 663 4378 3951 C ATOM 364 CG1 VAL A 71 -14.246 -1.563 -24.579 1.00 89.01 C ANISOU 364 CG1 VAL A 71 10720 10597 12503 380 4001 3674 C ATOM 365 CG2 VAL A 71 -12.428 -2.636 -25.886 1.00 95.87 C ANISOU 365 CG2 VAL A 71 11444 11714 13269 466 4687 3934 C ATOM 366 N TRP A 72 -17.107 -2.724 -25.550 1.00 80.93 N ANISOU 366 N TRP A 72 10391 10266 10093 1096 3277 3451 N ATOM 367 CA TRP A 72 -18.395 -2.039 -25.591 1.00 86.40 C ANISOU 367 CA TRP A 72 11312 10910 10606 1286 3031 3497 C ATOM 368 C TRP A 72 -18.967 -1.927 -24.182 1.00 82.68 C ANISOU 368 C TRP A 72 10620 10316 10478 1043 2643 3144 C ATOM 369 O TRP A 72 -18.413 -2.452 -23.215 1.00 73.80 O ANISOU 369 O TRP A 72 9209 9176 9655 760 2535 2862 O ATOM 370 CB TRP A 72 -19.377 -2.745 -26.545 1.00 82.92 C ANISOU 370 CB TRP A 72 11177 10848 9482 1686 2803 3458 C ATOM 371 CG TRP A 72 -19.762 -4.068 -26.080 1.00 70.72 C ANISOU 371 CG TRP A 72 9491 9597 7783 1635 2418 3017 C ATOM 372 CD1 TRP A 72 -20.857 -4.375 -25.340 1.00 68.89 C ANISOU 372 CD1 TRP A 72 9178 9441 7557 1605 1971 2695 C ATOM 373 CD2 TRP A 72 -19.044 -5.291 -26.274 1.00 69.28 C ANISOU 373 CD2 TRP A 72 9217 9643 7462 1598 2470 2847 C ATOM 374 NE1 TRP A 72 -20.873 -5.720 -25.059 1.00 68.79 N ANISOU 374 NE1 TRP A 72 9035 9675 7427 1538 1748 2348 N ATOM 375 CE2 TRP A 72 -19.775 -6.309 -25.630 1.00 69.79 C ANISOU 375 CE2 TRP A 72 9165 9900 7454 1542 2030 2427 C ATOM 376 CE3 TRP A 72 -17.860 -5.626 -26.934 1.00 72.27 C ANISOU 376 CE3 TRP A 72 9599 10073 7788 1619 2870 3018 C ATOM 377 CZ2 TRP A 72 -19.357 -7.644 -25.616 1.00 64.51 C ANISOU 377 CZ2 TRP A 72 8399 9448 6665 1503 1958 2170 C ATOM 378 CZ3 TRP A 72 -17.447 -6.949 -26.927 1.00 71.06 C ANISOU 378 CZ3 TRP A 72 9342 10159 7498 1598 2790 2748 C ATOM 379 CH2 TRP A 72 -18.196 -7.942 -26.276 1.00 70.96 C ANISOU 379 CH2 TRP A 72 9233 10313 7414 1541 2327 2328 C ATOM 380 N GLY A 73 -20.085 -1.209 -24.075 1.00 88.57 N ANISOU 380 N GLY A 73 11517 10972 11163 1187 2444 3174 N ATOM 381 CA GLY A 73 -20.738 -1.016 -22.802 1.00 86.85 C ANISOU 381 CA GLY A 73 11138 10637 11225 1015 2117 2868 C ATOM 382 C GLY A 73 -22.228 -1.284 -22.891 1.00 81.00 C ANISOU 382 C GLY A 73 10525 10112 10139 1270 1750 2719 C ATOM 383 O GLY A 73 -22.835 -1.227 -23.961 1.00 83.68 O ANISOU 383 O GLY A 73 11111 10608 10077 1602 1733 2905 O ATOM 384 N PHE A 74 -22.806 -1.595 -21.734 1.00 66.50 N ANISOU 384 N PHE A 74 8511 8286 8470 1121 1454 2371 N ATOM 385 CA PHE A 74 -24.253 -1.673 -21.580 1.00 64.43 C ANISOU 385 CA PHE A 74 8290 8152 8037 1311 1129 2215 C ATOM 386 C PHE A 74 -24.567 -1.464 -20.106 1.00 62.25 C ANISOU 386 C PHE A 74 7828 7707 8116 1092 977 1939 C ATOM 387 O PHE A 74 -23.667 -1.359 -19.272 1.00 66.62 O ANISOU 387 O PHE A 74 8247 8082 8984 818 1074 1848 O ATOM 388 CB PHE A 74 -24.797 -2.994 -22.115 1.00 65.04 C ANISOU 388 CB PHE A 74 8370 8624 7717 1461 899 2026 C ATOM 389 CG PHE A 74 -24.179 -4.189 -21.476 1.00 65.72 C ANISOU 389 CG PHE A 74 8262 8840 7869 1219 854 1750 C ATOM 390 CD1 PHE A 74 -24.836 -4.850 -20.457 1.00 61.04 C ANISOU 390 CD1 PHE A 74 7496 8314 7381 1100 605 1421 C ATOM 391 CD2 PHE A 74 -22.921 -4.629 -21.863 1.00 64.05 C ANISOU 391 CD2 PHE A 74 8037 8663 7635 1121 1090 1837 C ATOM 392 CE1 PHE A 74 -24.267 -5.937 -19.832 1.00 53.69 C ANISOU 392 CE1 PHE A 74 6415 7476 6508 898 573 1193 C ATOM 393 CE2 PHE A 74 -22.342 -5.729 -21.254 1.00 64.70 C ANISOU 393 CE2 PHE A 74 7941 8852 7788 924 1037 1587 C ATOM 394 CZ PHE A 74 -23.018 -6.397 -20.237 1.00 57.65 C ANISOU 394 CZ PHE A 74 6908 8021 6976 817 768 1268 C ATOM 395 N TYR A 75 -25.852 -1.387 -19.786 1.00 55.89 N ANISOU 395 N TYR A 75 7017 6960 7260 1235 737 1801 N ATOM 396 CA TYR A 75 -26.286 -1.003 -18.449 1.00 64.60 C ANISOU 396 CA TYR A 75 8000 7883 8661 1098 637 1581 C ATOM 397 C TYR A 75 -27.198 -2.085 -17.882 1.00 51.64 C ANISOU 397 C TYR A 75 6214 6496 6910 1104 390 1268 C ATOM 398 O TYR A 75 -28.207 -2.449 -18.502 1.00 52.19 O ANISOU 398 O TYR A 75 6289 6775 6767 1323 222 1251 O ATOM 399 CB TYR A 75 -26.980 0.365 -18.473 1.00 56.89 C ANISOU 399 CB TYR A 75 7143 6646 7829 1268 660 1742 C ATOM 400 CG TYR A 75 -26.051 1.490 -18.903 1.00 64.58 C ANISOU 400 CG TYR A 75 8251 7289 8997 1224 943 2057 C ATOM 401 CD1 TYR A 75 -25.896 1.815 -20.247 1.00 63.00 C ANISOU 401 CD1 TYR A 75 8249 7115 8574 1441 1103 2418 C ATOM 402 CD2 TYR A 75 -25.310 2.199 -17.972 1.00 61.04 C ANISOU 402 CD2 TYR A 75 7738 6495 8959 970 1056 1989 C ATOM 403 CE1 TYR A 75 -25.048 2.836 -20.654 1.00 73.25 C ANISOU 403 CE1 TYR A 75 9667 8079 10084 1394 1421 2744 C ATOM 404 CE2 TYR A 75 -24.457 3.211 -18.369 1.00 74.35 C ANISOU 404 CE2 TYR A 75 9509 7841 10900 899 1329 2270 C ATOM 405 CZ TYR A 75 -24.337 3.535 -19.710 1.00 76.00 C ANISOU 405 CZ TYR A 75 9905 8057 10913 1104 1537 2667 C ATOM 406 OH TYR A 75 -23.497 4.552 -20.109 1.00 79.83 O ANISOU 406 OH TYR A 75 10476 8170 11687 1029 1866 2984 O ATOM 407 N ASP A 76 -26.819 -2.631 -16.729 1.00 49.14 N ANISOU 407 N ASP A 76 5766 6158 6747 871 368 1025 N ATOM 408 CA ASP A 76 -27.715 -3.531 -16.002 1.00 58.13 C ANISOU 408 CA ASP A 76 6775 7465 7847 863 197 755 C ATOM 409 C ASP A 76 -28.511 -2.647 -15.068 1.00 58.88 C ANISOU 409 C ASP A 76 6863 7364 8146 907 178 676 C ATOM 410 O ASP A 76 -28.078 -2.338 -13.954 1.00 59.62 O ANISOU 410 O ASP A 76 6955 7276 8422 756 229 551 O ATOM 411 CB ASP A 76 -26.946 -4.598 -15.242 1.00 58.77 C ANISOU 411 CB ASP A 76 6763 7622 7943 639 200 563 C ATOM 412 CG ASP A 76 -26.488 -5.705 -16.125 1.00 61.47 C ANISOU 412 CG ASP A 76 7090 8201 8066 641 186 580 C ATOM 413 OD1 ASP A 76 -26.978 -5.787 -17.281 1.00 64.83 O ANISOU 413 OD1 ASP A 76 7575 8773 8285 833 131 690 O ATOM 414 OD2 ASP A 76 -25.643 -6.492 -15.669 1.00 56.94 O ANISOU 414 OD2 ASP A 76 6458 7665 7510 476 214 472 O ATOM 415 N GLY A 77 -29.663 -2.192 -15.553 1.00 65.41 N ANISOU 415 N GLY A 77 7695 8223 8935 1144 94 743 N ATOM 416 CA GLY A 77 -30.374 -1.120 -14.889 1.00 55.59 C ANISOU 416 CA GLY A 77 6472 6757 7892 1241 111 725 C ATOM 417 C GLY A 77 -29.528 0.128 -14.981 1.00 59.62 C ANISOU 417 C GLY A 77 7145 6946 8561 1202 261 916 C ATOM 418 O GLY A 77 -29.290 0.622 -16.080 1.00 65.24 O ANISOU 418 O GLY A 77 7974 7621 9193 1323 320 1184 O ATOM 419 N GLN A 78 -29.060 0.650 -13.851 1.00 61.12 N ANISOU 419 N GLN A 78 7357 6888 8979 1043 328 780 N ATOM 420 CA GLN A 78 -28.160 1.793 -13.856 1.00 56.60 C ANISOU 420 CA GLN A 78 6903 5965 8638 953 461 916 C ATOM 421 C GLN A 78 -26.696 1.400 -13.700 1.00 55.82 C ANISOU 421 C GLN A 78 6761 5830 8617 676 531 888 C ATOM 422 O GLN A 78 -25.837 2.289 -13.670 1.00 66.90 O ANISOU 422 O GLN A 78 8212 6924 10283 555 646 979 O ATOM 423 CB GLN A 78 -28.525 2.786 -12.743 1.00 63.91 C ANISOU 423 CB GLN A 78 7885 6584 9813 968 461 756 C ATOM 424 CG GLN A 78 -29.987 3.181 -12.678 1.00 76.36 C ANISOU 424 CG GLN A 78 9467 8181 11366 1245 406 739 C ATOM 425 CD GLN A 78 -30.293 4.530 -13.330 1.00 86.74 C ANISOU 425 CD GLN A 78 10924 9208 12827 1443 477 989 C ATOM 426 OE1 GLN A 78 -29.406 5.235 -13.829 1.00 82.69 O ANISOU 426 OE1 GLN A 78 10523 8444 12452 1361 600 1196 O ATOM 427 NE2 GLN A 78 -31.567 4.899 -13.310 1.00101.59 N ANISOU 427 NE2 GLN A 78 12788 11106 14704 1714 416 979 N ATOM 428 N GLN A 79 -26.388 0.113 -13.596 1.00 64.52 N ANISOU 428 N GLN A 79 7757 7216 9540 575 466 760 N ATOM 429 CA GLN A 79 -25.002 -0.330 -13.439 1.00 60.84 C ANISOU 429 CA GLN A 79 7221 6736 9158 338 516 722 C ATOM 430 C GLN A 79 -24.314 -0.418 -14.793 1.00 51.22 C ANISOU 430 C GLN A 79 6017 5584 7859 352 671 1012 C ATOM 431 O GLN A 79 -24.706 -1.252 -15.623 1.00 53.52 O ANISOU 431 O GLN A 79 6315 6166 7852 482 642 1081 O ATOM 432 CB GLN A 79 -24.937 -1.684 -12.749 1.00 51.34 C ANISOU 432 CB GLN A 79 5920 5790 7796 253 396 479 C ATOM 433 CG GLN A 79 -23.520 -2.320 -12.775 1.00 54.25 C ANISOU 433 CG GLN A 79 6193 6203 8216 54 430 458 C ATOM 434 CD GLN A 79 -22.522 -1.542 -11.953 1.00 58.32 C ANISOU 434 CD GLN A 79 6676 6423 9062 -129 425 354 C ATOM 435 OE1 GLN A 79 -22.726 -1.332 -10.755 1.00 60.26 O ANISOU 435 OE1 GLN A 79 6957 6563 9377 -154 297 114 O ATOM 436 NE2 GLN A 79 -21.428 -1.101 -12.589 1.00 56.05 N ANISOU 436 NE2 GLN A 79 6316 5990 8991 -251 568 523 N ATOM 437 N PRO A 80 -23.288 0.392 -15.048 1.00 57.78 N ANISOU 437 N PRO A 80 6852 6148 8955 226 845 1175 N ATOM 438 CA PRO A 80 -22.515 0.262 -16.289 1.00 56.96 C ANISOU 438 CA PRO A 80 6762 6104 8777 238 1061 1468 C ATOM 439 C PRO A 80 -21.626 -0.975 -16.254 1.00 64.54 C ANISOU 439 C PRO A 80 7572 7301 9647 97 1052 1348 C ATOM 440 O PRO A 80 -20.894 -1.209 -15.288 1.00 60.70 O ANISOU 440 O PRO A 80 6940 6743 9379 -113 974 1126 O ATOM 441 CB PRO A 80 -21.673 1.536 -16.314 1.00 61.72 C ANISOU 441 CB PRO A 80 7366 6286 9800 100 1273 1644 C ATOM 442 CG PRO A 80 -22.052 2.298 -15.102 1.00 66.63 C ANISOU 442 CG PRO A 80 7989 6639 10690 29 1119 1406 C ATOM 443 CD PRO A 80 -22.680 1.376 -14.149 1.00 58.65 C ANISOU 443 CD PRO A 80 6931 5881 9473 46 860 1069 C ATOM 444 N VAL A 81 -21.689 -1.758 -17.325 1.00 57.83 N ANISOU 444 N VAL A 81 6774 6732 8467 239 1115 1486 N ATOM 445 CA VAL A 81 -20.853 -2.934 -17.495 1.00 59.43 C ANISOU 445 CA VAL A 81 6860 7158 8563 151 1141 1407 C ATOM 446 C VAL A 81 -20.021 -2.722 -18.752 1.00 64.85 C ANISOU 446 C VAL A 81 7597 7835 9207 206 1456 1734 C ATOM 447 O VAL A 81 -20.574 -2.519 -19.840 1.00 65.38 O ANISOU 447 O VAL A 81 7862 7995 8986 449 1543 1967 O ATOM 448 CB VAL A 81 -21.687 -4.221 -17.604 1.00 57.41 C ANISOU 448 CB VAL A 81 6626 7249 7937 281 935 1228 C ATOM 449 CG1 VAL A 81 -20.775 -5.419 -17.702 1.00 55.82 C ANISOU 449 CG1 VAL A 81 6313 7234 7660 192 965 1133 C ATOM 450 CG2 VAL A 81 -22.640 -4.367 -16.421 1.00 51.07 C ANISOU 450 CG2 VAL A 81 5787 6440 7176 255 693 958 C ATOM 451 N LEU A 82 -18.699 -2.769 -18.603 1.00 68.94 N ANISOU 451 N LEU A 82 7936 8246 10010 2 1628 1753 N ATOM 452 CA LEU A 82 -17.770 -2.638 -19.720 1.00 65.45 C ANISOU 452 CA LEU A 82 7502 7789 9576 34 1995 2066 C ATOM 453 C LEU A 82 -17.245 -4.022 -20.090 1.00 69.46 C ANISOU 453 C LEU A 82 7936 8619 9837 68 2004 1966 C ATOM 454 O LEU A 82 -16.546 -4.659 -19.293 1.00 55.54 O ANISOU 454 O LEU A 82 5948 6882 8274 -116 1899 1731 O ATOM 455 CB LEU A 82 -16.616 -1.701 -19.354 1.00 66.30 C ANISOU 455 CB LEU A 82 7407 7526 10256 -226 2218 2163 C ATOM 456 CG LEU A 82 -15.510 -1.587 -20.400 1.00 68.26 C ANISOU 456 CG LEU A 82 7598 7729 10610 -233 2665 2493 C ATOM 457 CD1 LEU A 82 -16.038 -0.841 -21.610 1.00 68.07 C ANISOU 457 CD1 LEU A 82 7886 7648 10329 25 2943 2906 C ATOM 458 CD2 LEU A 82 -14.273 -0.897 -19.827 1.00 72.95 C ANISOU 458 CD2 LEU A 82 7874 7967 11877 -554 2828 2489 C ATOM 459 N ALA A 83 -17.575 -4.482 -21.297 1.00 63.03 N ANISOU 459 N ALA A 83 7328 8043 8579 329 2114 2132 N ATOM 460 CA ALA A 83 -17.046 -5.739 -21.801 1.00 66.31 C ANISOU 460 CA ALA A 83 7709 8741 8746 397 2165 2054 C ATOM 461 C ALA A 83 -15.677 -5.504 -22.422 1.00 73.75 C ANISOU 461 C ALA A 83 8543 9588 9891 337 2602 2310 C ATOM 462 O ALA A 83 -15.473 -4.513 -23.130 1.00 79.82 O ANISOU 462 O ALA A 83 9424 10179 10725 402 2927 2659 O ATOM 463 CB ALA A 83 -17.998 -6.341 -22.832 1.00 57.71 C ANISOU 463 CB ALA A 83 6900 7943 7082 722 2065 2078 C ATOM 464 N ILE A 84 -14.734 -6.403 -22.154 1.00 70.01 N ANISOU 464 N ILE A 84 7843 9215 9542 222 2635 2154 N ATOM 465 CA ILE A 84 -13.420 -6.323 -22.772 1.00 68.94 C ANISOU 465 CA ILE A 84 7559 9022 9614 182 3071 2379 C ATOM 466 C ILE A 84 -13.087 -7.675 -23.369 1.00 70.44 C ANISOU 466 C ILE A 84 7779 9532 9452 349 3116 2279 C ATOM 467 O ILE A 84 -13.423 -8.728 -22.813 1.00 63.90 O ANISOU 467 O ILE A 84 6918 8882 8479 347 2779 1955 O ATOM 468 CB ILE A 84 -12.295 -5.903 -21.795 1.00 78.61 C ANISOU 468 CB ILE A 84 8377 9979 11512 -156 3114 2293 C ATOM 469 CG1 ILE A 84 -12.265 -6.841 -20.577 1.00 72.64 C ANISOU 469 CG1 ILE A 84 7432 9331 10838 -286 2688 1870 C ATOM 470 CG2 ILE A 84 -12.426 -4.441 -21.406 1.00 81.72 C ANISOU 470 CG2 ILE A 84 8745 9997 12307 -317 3165 2433 C ATOM 471 CD1 ILE A 84 -10.929 -6.844 -19.859 1.00 62.30 C ANISOU 471 CD1 ILE A 84 5707 7872 10091 -535 2724 1757 C ATOM 472 N THR A 85 -12.387 -7.634 -24.506 1.00 80.48 N ANISOU 472 N THR A 85 9123 10855 10601 503 3569 2570 N ATOM 473 CA THR A 85 -11.995 -8.836 -25.221 1.00 81.28 C ANISOU 473 CA THR A 85 9287 11245 10350 704 3681 2501 C ATOM 474 C THR A 85 -10.518 -8.884 -25.588 1.00 82.38 C ANISOU 474 C THR A 85 9167 11328 10806 644 4163 2679 C ATOM 475 O THR A 85 -10.089 -9.884 -26.163 1.00 85.69 O ANISOU 475 O THR A 85 9620 11975 10964 820 4292 2617 O ATOM 476 CB THR A 85 -12.817 -9.001 -26.515 1.00 84.33 C ANISOU 476 CB THR A 85 10131 11856 10056 1092 3746 2649 C ATOM 477 OG1 THR A 85 -12.509 -7.929 -27.418 1.00 89.81 O ANISOU 477 OG1 THR A 85 10984 12409 10728 1211 4220 3101 O ATOM 478 CG2 THR A 85 -14.310 -8.998 -26.218 1.00 74.84 C ANISOU 478 CG2 THR A 85 9140 10724 8573 1168 3259 2459 C ATOM 479 N ASP A 86 -9.731 -7.853 -25.293 1.00 84.40 N ANISOU 479 N ASP A 86 9151 11277 11639 407 4440 2885 N ATOM 480 CA ASP A 86 -8.306 -7.909 -25.622 1.00 92.63 C ANISOU 480 CA ASP A 86 9889 12251 13057 332 4884 3028 C ATOM 481 C ASP A 86 -7.565 -8.742 -24.584 1.00 85.19 C ANISOU 481 C ASP A 86 8512 11348 12508 128 4644 2684 C ATOM 482 O ASP A 86 -7.552 -8.371 -23.406 1.00 88.33 O ANISOU 482 O ASP A 86 8666 11560 13337 -144 4306 2478 O ATOM 483 CB ASP A 86 -7.684 -6.523 -25.691 1.00 96.92 C ANISOU 483 CB ASP A 86 10310 12405 14111 137 5125 3269 C ATOM 484 CG ASP A 86 -6.220 -6.570 -26.099 1.00 95.12 C ANISOU 484 CG ASP A 86 9823 12086 14233 76 5427 3322 C ATOM 485 OD1 ASP A 86 -5.922 -6.196 -27.250 1.00104.31 O ANISOU 485 OD1 ASP A 86 11204 13215 15213 262 5818 3618 O ATOM 486 OD2 ASP A 86 -5.370 -7.008 -25.282 1.00 89.20 O ANISOU 486 OD2 ASP A 86 8658 11308 13926 -135 5266 3067 O ATOM 487 N PRO A 87 -6.907 -9.833 -24.977 1.00 82.24 N ANISOU 487 N PRO A 87 8084 11187 11976 269 4722 2567 N ATOM 488 CA PRO A 87 -6.313 -10.738 -23.974 1.00 83.70 C ANISOU 488 CA PRO A 87 7896 11435 12471 133 4447 2233 C ATOM 489 C PRO A 87 -5.360 -10.047 -23.011 1.00 93.98 C ANISOU 489 C PRO A 87 8754 12446 14509 -205 4327 2139 C ATOM 490 O PRO A 87 -5.333 -10.414 -21.826 1.00 95.91 O ANISOU 490 O PRO A 87 8749 12680 15012 -356 3939 1849 O ATOM 491 CB PRO A 87 -5.580 -11.784 -24.832 1.00 87.63 C ANISOU 491 CB PRO A 87 8437 12145 12713 363 4666 2206 C ATOM 492 CG PRO A 87 -6.193 -11.680 -26.208 1.00 89.01 C ANISOU 492 CG PRO A 87 9102 12451 12268 671 4942 2448 C ATOM 493 CD PRO A 87 -6.591 -10.236 -26.357 1.00 87.81 C ANISOU 493 CD PRO A 87 9066 12054 12245 568 5066 2735 C ATOM 494 N ASP A 88 -4.577 -9.061 -23.483 1.00 87.46 N ANISOU 494 N ASP A 88 7835 11379 14018 -307 4629 2362 N ATOM 495 CA ASP A 88 -3.697 -8.309 -22.593 1.00 90.05 C ANISOU 495 CA ASP A 88 7756 11410 15048 -619 4489 2252 C ATOM 496 C ASP A 88 -4.492 -7.547 -21.540 1.00 95.04 C ANISOU 496 C ASP A 88 8379 11851 15881 -822 4133 2129 C ATOM 497 O ASP A 88 -4.169 -7.599 -20.346 1.00 96.44 O ANISOU 497 O ASP A 88 8270 11942 16430 -1014 3739 1827 O ATOM 498 CB ASP A 88 -2.834 -7.339 -23.400 1.00102.41 C ANISOU 498 CB ASP A 88 9260 12733 16919 -668 4924 2544 C ATOM 499 CG ASP A 88 -1.697 -8.032 -24.128 1.00115.53 C ANISOU 499 CG ASP A 88 10774 14520 18601 -543 5228 2593 C ATOM 500 OD1 ASP A 88 -1.221 -9.082 -23.643 1.00115.72 O ANISOU 500 OD1 ASP A 88 10580 14728 18660 -523 5016 2331 O ATOM 501 OD2 ASP A 88 -1.273 -7.517 -25.181 1.00124.48 O ANISOU 501 OD2 ASP A 88 12015 15559 19723 -451 5686 2901 O ATOM 502 N MET A 89 -5.515 -6.806 -21.979 1.00 93.28 N ANISOU 502 N MET A 89 8487 11551 15404 -760 4258 2359 N ATOM 503 CA MET A 89 -6.399 -6.095 -21.063 1.00 94.58 C ANISOU 503 CA MET A 89 8688 11537 15710 -920 3951 2260 C ATOM 504 C MET A 89 -7.074 -7.061 -20.093 1.00 89.14 C ANISOU 504 C MET A 89 8049 11068 14754 -886 3427 1888 C ATOM 505 O MET A 89 -7.277 -6.737 -18.916 1.00 88.00 O ANISOU 505 O MET A 89 7808 10779 14847 -1058 3015 1625 O ATOM 506 CB MET A 89 -7.438 -5.319 -21.878 1.00101.25 C ANISOU 506 CB MET A 89 9940 12322 16210 -775 4194 2599 C ATOM 507 CG MET A 89 -8.042 -4.127 -21.190 1.00106.24 C ANISOU 507 CG MET A 89 10616 12630 17121 -953 4003 2586 C ATOM 508 SD MET A 89 -9.042 -3.109 -22.299 1.00117.49 S ANISOU 508 SD MET A 89 12526 13942 18173 -738 4326 3033 S ATOM 509 CE MET A 89 -7.778 -2.346 -23.318 1.00124.72 C ANISOU 509 CE MET A 89 13357 14623 19407 -748 4853 3356 C ATOM 510 N ILE A 90 -7.415 -8.261 -20.571 1.00 82.85 N ANISOU 510 N ILE A 90 7462 10606 13411 -639 3392 1828 N ATOM 511 CA ILE A 90 -8.050 -9.257 -19.716 1.00 77.38 C ANISOU 511 CA ILE A 90 6877 10104 12420 -583 2893 1475 C ATOM 512 C ILE A 90 -7.085 -9.750 -18.651 1.00 78.97 C ANISOU 512 C ILE A 90 6687 10276 13043 -734 2640 1195 C ATOM 513 O ILE A 90 -7.474 -9.969 -17.492 1.00 72.29 O ANISOU 513 O ILE A 90 5854 9418 12194 -799 2187 910 O ATOM 514 CB ILE A 90 -8.601 -10.408 -20.567 1.00 68.97 C ANISOU 514 CB ILE A 90 6117 9361 10729 -292 2941 1478 C ATOM 515 CG1 ILE A 90 -9.691 -9.849 -21.495 1.00 69.99 C ANISOU 515 CG1 ILE A 90 6652 9522 10421 -122 3076 1709 C ATOM 516 CG2 ILE A 90 -9.173 -11.487 -19.654 1.00 61.28 C ANISOU 516 CG2 ILE A 90 5216 8538 9529 -259 2468 1129 C ATOM 517 CD1 ILE A 90 -10.465 -10.852 -22.298 1.00 60.66 C ANISOU 517 CD1 ILE A 90 5809 8636 8604 167 3026 1662 C ATOM 518 N LYS A 91 -5.810 -9.901 -19.011 1.00 80.48 N ANISOU 518 N LYS A 91 6521 10450 13609 -774 2932 1277 N ATOM 519 CA LYS A 91 -4.829 -10.356 -18.034 1.00 83.06 C ANISOU 519 CA LYS A 91 6439 10752 14367 -892 2667 1007 C ATOM 520 C LYS A 91 -4.561 -9.288 -16.976 1.00 81.43 C ANISOU 520 C LYS A 91 6008 10245 14686 -1161 2386 858 C ATOM 521 O LYS A 91 -4.349 -9.617 -15.799 1.00 76.28 O ANISOU 521 O LYS A 91 5209 9590 14183 -1220 1932 540 O ATOM 522 CB LYS A 91 -3.544 -10.778 -18.749 1.00 82.36 C ANISOU 522 CB LYS A 91 6117 10725 14448 -826 2983 1100 C ATOM 523 CG LYS A 91 -2.437 -11.266 -17.834 1.00 81.64 C ANISOU 523 CG LYS A 91 5666 10626 14728 -896 2664 819 C ATOM 524 CD LYS A 91 -1.234 -11.651 -18.669 1.00 82.07 C ANISOU 524 CD LYS A 91 5535 10744 14904 -808 3010 936 C ATOM 525 CE LYS A 91 -0.091 -12.190 -17.834 1.00 89.42 C ANISOU 525 CE LYS A 91 6096 11685 16195 -840 2708 678 C ATOM 526 NZ LYS A 91 0.939 -12.827 -18.711 1.00 93.60 N ANISOU 526 NZ LYS A 91 6469 12334 16761 -698 3062 784 N ATOM 527 N THR A 92 -4.581 -8.007 -17.367 1.00 80.26 N ANISOU 527 N THR A 92 5904 9835 14755 -1291 2611 1066 N ATOM 528 CA THR A 92 -4.482 -6.939 -16.375 1.00 85.21 C ANISOU 528 CA THR A 92 6414 10154 15807 -1520 2310 893 C ATOM 529 C THR A 92 -5.587 -7.060 -15.336 1.00 81.55 C ANISOU 529 C THR A 92 6125 9723 15138 -1526 1870 650 C ATOM 530 O THR A 92 -5.342 -6.923 -14.131 1.00 81.61 O ANISOU 530 O THR A 92 5994 9629 15385 -1633 1432 330 O ATOM 531 CB THR A 92 -4.560 -5.553 -17.029 1.00 91.38 C ANISOU 531 CB THR A 92 7284 10631 16804 -1626 2648 1181 C ATOM 532 OG1 THR A 92 -3.635 -5.454 -18.119 1.00 96.47 O ANISOU 532 OG1 THR A 92 7835 11257 17563 -1581 3108 1446 O ATOM 533 CG2 THR A 92 -4.224 -4.474 -15.998 1.00 89.19 C ANISOU 533 CG2 THR A 92 6842 10011 17037 -1858 2335 957 C ATOM 534 N VAL A 93 -6.818 -7.313 -15.796 1.00 74.05 N ANISOU 534 N VAL A 93 5629 8935 13572 -1340 1910 766 N ATOM 535 CA VAL A 93 -7.980 -7.349 -14.907 1.00 77.26 C ANISOU 535 CA VAL A 93 6351 9374 13629 -1286 1502 554 C ATOM 536 C VAL A 93 -7.933 -8.564 -13.993 1.00 72.88 C ANISOU 536 C VAL A 93 5795 9036 12861 -1193 1115 249 C ATOM 537 O VAL A 93 -8.124 -8.451 -12.777 1.00 78.41 O ANISOU 537 O VAL A 93 6519 9664 13608 -1240 717 -22 O ATOM 538 CB VAL A 93 -9.287 -7.332 -15.717 1.00 72.83 C ANISOU 538 CB VAL A 93 6219 8932 12521 -1107 1655 760 C ATOM 539 CG1 VAL A 93 -10.493 -7.440 -14.770 1.00 55.37 C ANISOU 539 CG1 VAL A 93 4286 6762 9992 -1050 1264 537 C ATOM 540 CG2 VAL A 93 -9.387 -6.095 -16.575 1.00 76.65 C ANISOU 540 CG2 VAL A 93 6758 9188 13177 -1159 2021 1085 C ATOM 541 N LEU A 94 -7.702 -9.742 -14.563 1.00 74.38 N ANISOU 541 N LEU A 94 5990 9480 12790 -1034 1235 292 N ATOM 542 CA LEU A 94 -7.804 -10.967 -13.785 1.00 67.57 C ANISOU 542 CA LEU A 94 5194 8810 11668 -911 905 46 C ATOM 543 C LEU A 94 -6.522 -11.328 -13.046 1.00 67.23 C ANISOU 543 C LEU A 94 4770 8744 12029 -967 702 -153 C ATOM 544 O LEU A 94 -6.590 -11.985 -12.003 1.00 68.21 O ANISOU 544 O LEU A 94 4953 8937 12024 -894 324 -394 O ATOM 545 CB LEU A 94 -8.213 -12.136 -14.681 1.00 64.08 C ANISOU 545 CB LEU A 94 4958 8628 10761 -700 1084 145 C ATOM 546 CG LEU A 94 -9.542 -12.005 -15.404 1.00 63.16 C ANISOU 546 CG LEU A 94 5219 8582 10197 -599 1203 290 C ATOM 547 CD1 LEU A 94 -9.892 -13.326 -16.038 1.00 59.89 C ANISOU 547 CD1 LEU A 94 4984 8413 9359 -396 1256 277 C ATOM 548 CD2 LEU A 94 -10.654 -11.539 -14.458 1.00 63.00 C ANISOU 548 CD2 LEU A 94 5414 8472 10049 -643 904 160 C ATOM 549 N VAL A 95 -5.357 -10.926 -13.542 1.00 72.67 N ANISOU 549 N VAL A 95 5065 9335 13210 -1077 944 -54 N ATOM 550 CA VAL A 95 -4.085 -11.288 -12.920 1.00 81.91 C ANISOU 550 CA VAL A 95 5809 10495 14818 -1116 744 -250 C ATOM 551 C VAL A 95 -3.350 -10.062 -12.380 1.00 85.39 C ANISOU 551 C VAL A 95 6032 10648 15763 -1331 608 -340 C ATOM 552 O VAL A 95 -3.057 -9.984 -11.188 1.00 90.08 O ANISOU 552 O VAL A 95 6577 11176 16472 -1353 149 -630 O ATOM 553 CB VAL A 95 -3.190 -12.101 -13.882 1.00 84.52 C ANISOU 553 CB VAL A 95 5939 10984 15192 -998 1091 -103 C ATOM 554 CG1 VAL A 95 -2.086 -12.764 -13.099 1.00 87.06 C ANISOU 554 CG1 VAL A 95 6018 11354 15707 -939 769 -334 C ATOM 555 CG2 VAL A 95 -3.988 -13.152 -14.622 1.00 67.10 C ANISOU 555 CG2 VAL A 95 4082 9023 12388 -769 1268 7 C ATOM 556 N LYS A 96 -3.050 -9.089 -13.241 1.00 91.35 N ANISOU 556 N LYS A 96 6714 11220 16774 -1461 997 -97 N ATOM 557 CA LYS A 96 -2.096 -8.040 -12.865 1.00 94.05 C ANISOU 557 CA LYS A 96 6816 11277 17639 -1646 915 -179 C ATOM 558 C LYS A 96 -2.636 -7.132 -11.759 1.00 87.69 C ANISOU 558 C LYS A 96 6125 10253 16939 -1765 517 -414 C ATOM 559 O LYS A 96 -2.012 -6.970 -10.705 1.00 83.52 O ANISOU 559 O LYS A 96 5461 9635 16636 -1802 103 -713 O ATOM 560 CB LYS A 96 -1.714 -7.220 -14.092 1.00100.02 C ANISOU 560 CB LYS A 96 7502 11869 18633 -1737 1462 164 C ATOM 561 CG LYS A 96 -1.051 -8.031 -15.195 1.00104.81 C ANISOU 561 CG LYS A 96 8007 12675 19143 -1602 1876 382 C ATOM 562 CD LYS A 96 -0.544 -7.133 -16.328 1.00107.78 C ANISOU 562 CD LYS A 96 8321 12855 19777 -1680 2411 714 C ATOM 563 CE LYS A 96 0.042 -7.952 -17.476 1.00111.97 C ANISOU 563 CE LYS A 96 8809 13596 20137 -1508 2847 932 C ATOM 564 NZ LYS A 96 0.816 -7.133 -18.460 1.00121.31 N ANISOU 564 NZ LYS A 96 9876 14577 21640 -1574 3346 1224 N ATOM 565 N GLU A 97 -3.796 -6.520 -11.976 1.00 83.50 N ANISOU 565 N GLU A 97 5855 9631 16238 -1805 630 -290 N ATOM 566 CA GLU A 97 -4.341 -5.588 -11.000 1.00 81.07 C ANISOU 566 CA GLU A 97 5677 9095 16032 -1907 295 -507 C ATOM 567 C GLU A 97 -5.455 -6.216 -10.178 1.00 75.66 C ANISOU 567 C GLU A 97 5263 8579 14906 -1784 -52 -707 C ATOM 568 O GLU A 97 -6.386 -5.530 -9.746 1.00 75.55 O ANISOU 568 O GLU A 97 5478 8423 14803 -1821 -175 -775 O ATOM 569 CB GLU A 97 -4.800 -4.315 -11.704 1.00 90.24 C ANISOU 569 CB GLU A 97 6934 9973 17382 -2041 642 -249 C ATOM 570 CG GLU A 97 -3.665 -3.627 -12.492 1.00107.89 C ANISOU 570 CG GLU A 97 8911 12006 20078 -2157 1004 -45 C ATOM 571 CD GLU A 97 -2.496 -3.195 -11.610 1.00121.74 C ANISOU 571 CD GLU A 97 10368 13575 22313 -2271 680 -347 C ATOM 572 OE1 GLU A 97 -2.730 -2.869 -10.426 1.00123.09 O ANISOU 572 OE1 GLU A 97 10608 13649 22512 -2295 213 -681 O ATOM 573 OE2 GLU A 97 -1.341 -3.179 -12.098 1.00128.32 O ANISOU 573 OE2 GLU A 97 10905 14361 23492 -2321 892 -256 O ATOM 574 N CYS A 98 -5.381 -7.529 -9.980 1.00 78.13 N ANISOU 574 N CYS A 98 5577 9187 14922 -1616 -191 -792 N ATOM 575 CA CYS A 98 -6.437 -8.229 -9.265 1.00 75.29 C ANISOU 575 CA CYS A 98 5629 9014 13963 -1422 -461 -924 C ATOM 576 C CYS A 98 -6.529 -7.740 -7.830 1.00 77.43 C ANISOU 576 C CYS A 98 5977 9147 14295 -1439 -956 -1276 C ATOM 577 O CYS A 98 -7.596 -7.322 -7.368 1.00 68.86 O ANISOU 577 O CYS A 98 5248 8008 12907 -1391 -1046 -1324 O ATOM 578 CB CYS A 98 -6.180 -9.734 -9.303 1.00 77.50 C ANISOU 578 CB CYS A 98 5917 9595 13935 -1223 -506 -939 C ATOM 579 SG CYS A 98 -7.310 -10.665 -8.236 1.00 76.22 S ANISOU 579 SG CYS A 98 6235 9616 13108 -990 -844 -1111 S ATOM 580 N TYR A 99 -5.405 -7.769 -7.112 1.00 81.39 N ANISOU 580 N TYR A 99 6219 9598 15106 -1459 -1265 -1514 N ATOM 581 CA TYR A 99 -5.404 -7.311 -5.725 1.00 84.05 C ANISOU 581 CA TYR A 99 6707 9821 15405 -1413 -1745 -1855 C ATOM 582 C TYR A 99 -5.569 -5.803 -5.619 1.00 80.07 C ANISOU 582 C TYR A 99 6222 8983 15216 -1593 -1725 -1903 C ATOM 583 O TYR A 99 -6.128 -5.307 -4.635 1.00 77.12 O ANISOU 583 O TYR A 99 6099 8509 14695 -1543 -2033 -2144 O ATOM 584 CB TYR A 99 -4.111 -7.737 -5.026 1.00 86.74 C ANISOU 584 CB TYR A 99 6851 10210 15896 -1325 -2055 -2059 C ATOM 585 CG TYR A 99 -3.935 -9.230 -4.949 1.00 87.73 C ANISOU 585 CG TYR A 99 6996 10636 15703 -1111 -2133 -2044 C ATOM 586 CD1 TYR A 99 -2.888 -9.867 -5.606 1.00 92.40 C ANISOU 586 CD1 TYR A 99 7272 11326 16512 -1101 -1958 -1923 C ATOM 587 CD2 TYR A 99 -4.835 -10.011 -4.237 1.00 86.62 C ANISOU 587 CD2 TYR A 99 7201 10668 15043 -906 -2358 -2143 C ATOM 588 CE1 TYR A 99 -2.743 -11.247 -5.538 1.00 96.73 C ANISOU 588 CE1 TYR A 99 7848 12127 16779 -888 -2027 -1912 C ATOM 589 CE2 TYR A 99 -4.703 -11.383 -4.166 1.00 83.19 C ANISOU 589 CE2 TYR A 99 6804 10478 14327 -699 -2418 -2117 C ATOM 590 CZ TYR A 99 -3.658 -11.997 -4.814 1.00 94.99 C ANISOU 590 CZ TYR A 99 7979 12055 16056 -689 -2262 -2007 C ATOM 591 OH TYR A 99 -3.535 -13.366 -4.731 1.00101.43 O ANISOU 591 OH TYR A 99 8842 13090 16605 -464 -2326 -1988 O ATOM 592 N SER A 100 -5.093 -5.055 -6.602 1.00 79.07 N ANISOU 592 N SER A 100 5861 8670 15510 -1780 -1354 -1674 N ATOM 593 CA SER A 100 -5.063 -3.611 -6.423 1.00 90.22 C ANISOU 593 CA SER A 100 7265 9727 17287 -1942 -1362 -1739 C ATOM 594 C SER A 100 -6.390 -2.949 -6.775 1.00 82.23 C ANISOU 594 C SER A 100 6525 8582 16135 -1991 -1165 -1595 C ATOM 595 O SER A 100 -6.851 -2.062 -6.055 1.00 91.13 O ANISOU 595 O SER A 100 7830 9489 17304 -2015 -1377 -1793 O ATOM 596 CB SER A 100 -3.917 -3.005 -7.250 1.00103.76 C ANISOU 596 CB SER A 100 8617 11254 19553 -2114 -1049 -1559 C ATOM 597 OG SER A 100 -3.930 -3.434 -8.600 1.00106.17 O ANISOU 597 OG SER A 100 8838 11677 19823 -2130 -541 -1169 O ATOM 598 N VAL A 101 -7.028 -3.396 -7.845 1.00 73.93 N ANISOU 598 N VAL A 101 5523 7667 14901 -1981 -775 -1266 N ATOM 599 CA VAL A 101 -8.102 -2.662 -8.493 1.00 71.30 C ANISOU 599 CA VAL A 101 5445 7197 14449 -1999 -470 -1015 C ATOM 600 C VAL A 101 -9.345 -3.532 -8.675 1.00 72.30 C ANISOU 600 C VAL A 101 5988 7651 13832 -1745 -402 -886 C ATOM 601 O VAL A 101 -10.474 -3.090 -8.424 1.00 70.06 O ANISOU 601 O VAL A 101 6038 7318 13264 -1657 -430 -889 O ATOM 602 CB VAL A 101 -7.601 -2.142 -9.848 1.00 72.74 C ANISOU 602 CB VAL A 101 5397 7225 15018 -2149 50 -628 C ATOM 603 CG1 VAL A 101 -8.741 -1.557 -10.651 1.00 75.72 C ANISOU 603 CG1 VAL A 101 6125 7541 15106 -2068 383 -305 C ATOM 604 CG2 VAL A 101 -6.434 -1.137 -9.642 1.00 76.46 C ANISOU 604 CG2 VAL A 101 5623 7388 16039 -2303 18 -720 C ATOM 605 N PHE A 102 -9.142 -4.776 -9.122 1.00 70.66 N ANISOU 605 N PHE A 102 5743 7764 13342 -1625 -308 -782 N ATOM 606 CA PHE A 102 -10.241 -5.639 -9.538 1.00 62.80 C ANISOU 606 CA PHE A 102 5079 7053 11728 -1416 -185 -629 C ATOM 607 C PHE A 102 -10.435 -6.818 -8.593 1.00 60.11 C ANISOU 607 C PHE A 102 4876 6958 11007 -1252 -502 -859 C ATOM 608 O PHE A 102 -10.485 -7.976 -9.016 1.00 63.29 O ANISOU 608 O PHE A 102 5315 7616 11117 -1130 -411 -769 O ATOM 609 CB PHE A 102 -9.999 -6.119 -10.964 1.00 64.86 C ANISOU 609 CB PHE A 102 5254 7463 11927 -1385 230 -297 C ATOM 610 CG PHE A 102 -9.846 -5.002 -11.952 1.00 69.16 C ANISOU 610 CG PHE A 102 5718 7772 12787 -1505 601 -10 C ATOM 611 CD1 PHE A 102 -8.615 -4.683 -12.473 1.00 77.06 C ANISOU 611 CD1 PHE A 102 6348 8632 14299 -1663 831 104 C ATOM 612 CD2 PHE A 102 -10.952 -4.269 -12.364 1.00 74.53 C ANISOU 612 CD2 PHE A 102 6692 8361 13266 -1445 740 163 C ATOM 613 CE1 PHE A 102 -8.485 -3.642 -13.396 1.00 84.11 C ANISOU 613 CE1 PHE A 102 7193 9278 15487 -1767 1231 414 C ATOM 614 CE2 PHE A 102 -10.831 -3.233 -13.278 1.00 75.16 C ANISOU 614 CE2 PHE A 102 6740 8204 13612 -1524 1096 463 C ATOM 615 CZ PHE A 102 -9.601 -2.923 -13.792 1.00 77.76 C ANISOU 615 CZ PHE A 102 6730 8379 14437 -1687 1358 600 C ATOM 616 N THR A 103 -10.571 -6.535 -7.304 1.00 62.48 N ANISOU 616 N THR A 103 5285 7166 11290 -1230 -867 -1156 N ATOM 617 CA THR A 103 -10.581 -7.619 -6.323 1.00 67.50 C ANISOU 617 CA THR A 103 6050 8005 11594 -1059 -1166 -1362 C ATOM 618 C THR A 103 -11.922 -8.348 -6.235 1.00 56.69 C ANISOU 618 C THR A 103 5056 6824 9658 -875 -1085 -1278 C ATOM 619 O THR A 103 -11.944 -9.560 -6.014 1.00 59.23 O ANISOU 619 O THR A 103 5457 7354 9693 -738 -1141 -1292 O ATOM 620 CB THR A 103 -10.176 -7.054 -4.958 1.00 63.53 C ANISOU 620 CB THR A 103 5551 7342 11245 -1065 -1598 -1721 C ATOM 621 OG1 THR A 103 -8.977 -6.294 -5.122 1.00 78.97 O ANISOU 621 OG1 THR A 103 7105 9083 13817 -1272 -1668 -1808 O ATOM 622 CG2 THR A 103 -9.889 -8.174 -3.962 1.00 62.71 C ANISOU 622 CG2 THR A 103 5546 7438 10841 -867 -1922 -1919 C ATOM 623 N ASN A 104 -13.046 -7.648 -6.416 1.00 57.16 N ANISOU 623 N ASN A 104 5332 6799 9587 -868 -945 -1188 N ATOM 624 CA ASN A 104 -14.357 -8.171 -6.061 1.00 52.14 C ANISOU 624 CA ASN A 104 5019 6295 8495 -704 -918 -1173 C ATOM 625 C ASN A 104 -15.236 -8.390 -7.287 1.00 49.54 C ANISOU 625 C ASN A 104 4747 6075 8001 -680 -603 -899 C ATOM 626 O ASN A 104 -14.972 -7.872 -8.372 1.00 56.05 O ANISOU 626 O ASN A 104 5433 6840 9021 -769 -395 -710 O ATOM 627 CB ASN A 104 -15.052 -7.218 -5.063 1.00 54.08 C ANISOU 627 CB ASN A 104 5484 6367 8699 -664 -1064 -1348 C ATOM 628 CG ASN A 104 -14.189 -6.948 -3.836 1.00 62.94 C ANISOU 628 CG ASN A 104 6582 7379 9954 -660 -1430 -1664 C ATOM 629 OD1 ASN A 104 -13.661 -7.878 -3.219 1.00 57.50 O ANISOU 629 OD1 ASN A 104 5899 6833 9115 -561 -1624 -1780 O ATOM 630 ND2 ASN A 104 -14.036 -5.677 -3.474 1.00 56.70 N ANISOU 630 ND2 ASN A 104 5773 6323 9448 -750 -1548 -1817 N ATOM 631 N ARG A 105 -16.264 -9.222 -7.116 1.00 47.36 N ANISOU 631 N ARG A 105 4674 5958 7361 -546 -569 -881 N ATOM 632 CA ARG A 105 -17.327 -9.308 -8.103 1.00 52.30 C ANISOU 632 CA ARG A 105 5376 6669 7826 -501 -348 -687 C ATOM 633 C ARG A 105 -18.482 -8.383 -7.719 1.00 48.34 C ANISOU 633 C ARG A 105 5043 6048 7278 -454 -335 -706 C ATOM 634 O ARG A 105 -18.463 -7.700 -6.692 1.00 49.19 O ANISOU 634 O ARG A 105 5234 6003 7454 -453 -477 -872 O ATOM 635 CB ARG A 105 -17.831 -10.749 -8.246 1.00 48.01 C ANISOU 635 CB ARG A 105 4907 6341 6993 -400 -309 -666 C ATOM 636 CG ARG A 105 -16.692 -11.729 -8.491 1.00 53.86 C ANISOU 636 CG ARG A 105 5504 7189 7770 -412 -335 -674 C ATOM 637 CD ARG A 105 -17.169 -12.984 -9.182 1.00 58.01 C ANISOU 637 CD ARG A 105 6074 7894 8075 -334 -227 -602 C ATOM 638 NE ARG A 105 -16.093 -13.953 -9.433 1.00 59.83 N ANISOU 638 NE ARG A 105 6179 8215 8337 -318 -237 -614 N ATOM 639 CZ ARG A 105 -15.508 -14.676 -8.481 1.00 53.07 C ANISOU 639 CZ ARG A 105 5334 7370 7462 -267 -398 -738 C ATOM 640 NH1 ARG A 105 -15.891 -14.507 -7.216 1.00 50.64 N ANISOU 640 NH1 ARG A 105 5182 6991 7067 -224 -553 -855 N ATOM 641 NH2 ARG A 105 -14.540 -15.552 -8.789 1.00 48.89 N ANISOU 641 NH2 ARG A 105 4675 6921 6981 -231 -399 -742 N ATOM 642 N ARG A 106 -19.487 -8.360 -8.572 1.00 48.08 N ANISOU 642 N ARG A 106 5059 6083 7125 -396 -178 -549 N ATOM 643 CA ARG A 106 -20.642 -7.533 -8.305 1.00 55.64 C ANISOU 643 CA ARG A 106 6146 6941 8053 -325 -150 -551 C ATOM 644 C ARG A 106 -21.318 -7.988 -7.020 1.00 64.17 C ANISOU 644 C ARG A 106 7379 8050 8952 -234 -235 -726 C ATOM 645 O ARG A 106 -21.422 -9.207 -6.757 1.00 51.33 O ANISOU 645 O ARG A 106 5777 6580 7145 -193 -241 -757 O ATOM 646 CB ARG A 106 -21.633 -7.601 -9.463 1.00 67.01 C ANISOU 646 CB ARG A 106 7589 8489 9382 -246 -9 -368 C ATOM 647 CG ARG A 106 -22.118 -6.244 -9.845 1.00 70.54 C ANISOU 647 CG ARG A 106 8077 8761 9964 -215 57 -262 C ATOM 648 CD ARG A 106 -23.160 -6.295 -10.916 1.00 66.03 C ANISOU 648 CD ARG A 106 7522 8309 9257 -90 141 -100 C ATOM 649 NE ARG A 106 -22.841 -7.179 -12.036 1.00 62.12 N ANISOU 649 NE ARG A 106 6966 8015 8623 -77 192 13 N ATOM 650 CZ ARG A 106 -23.519 -7.143 -13.184 1.00 59.66 C ANISOU 650 CZ ARG A 106 6679 7808 8180 48 238 160 C ATOM 651 NH1 ARG A 106 -24.520 -6.274 -13.307 1.00 56.98 N ANISOU 651 NH1 ARG A 106 6399 7389 7862 163 233 222 N ATOM 652 NH2 ARG A 106 -23.225 -7.957 -14.192 1.00 60.14 N ANISOU 652 NH2 ARG A 106 6719 8053 8077 87 271 232 N ATOM 653 N PRO A 107 -21.784 -7.048 -6.202 1.00 75.05 N ANISOU 653 N PRO A 107 8879 9265 10370 -185 -275 -833 N ATOM 654 CA PRO A 107 -22.543 -7.414 -5.003 1.00 73.96 C ANISOU 654 CA PRO A 107 8921 9155 10025 -59 -292 -972 C ATOM 655 C PRO A 107 -23.634 -8.414 -5.346 1.00 63.92 C ANISOU 655 C PRO A 107 7639 8061 8585 11 -142 -870 C ATOM 656 O PRO A 107 -24.308 -8.319 -6.373 1.00 53.38 O ANISOU 656 O PRO A 107 6205 6780 7297 14 -46 -733 O ATOM 657 CB PRO A 107 -23.113 -6.079 -4.515 1.00 85.30 C ANISOU 657 CB PRO A 107 10470 10387 11554 3 -289 -1052 C ATOM 658 CG PRO A 107 -22.797 -5.064 -5.621 1.00 90.04 C ANISOU 658 CG PRO A 107 10939 10849 12423 -96 -251 -911 C ATOM 659 CD PRO A 107 -21.610 -5.593 -6.338 1.00 82.56 C ANISOU 659 CD PRO A 107 9824 9976 11568 -233 -283 -829 C ATOM 660 N PHE A 108 -23.731 -9.429 -4.510 1.00 69.07 N ANISOU 660 N PHE A 108 8390 8798 9053 70 -137 -939 N ATOM 661 CA PHE A 108 -24.616 -10.555 -4.724 1.00 72.92 C ANISOU 661 CA PHE A 108 8849 9421 9436 106 5 -862 C ATOM 662 C PHE A 108 -25.315 -10.806 -3.404 1.00 81.12 C ANISOU 662 C PHE A 108 10080 10429 10314 234 103 -939 C ATOM 663 O PHE A 108 -24.662 -11.049 -2.384 1.00 88.30 O ANISOU 663 O PHE A 108 11161 11313 11075 294 18 -1035 O ATOM 664 CB PHE A 108 -23.840 -11.794 -5.189 1.00 70.24 C ANISOU 664 CB PHE A 108 8432 9203 9053 40 -37 -822 C ATOM 665 CG PHE A 108 -24.693 -13.008 -5.356 1.00 58.29 C ANISOU 665 CG PHE A 108 6891 7783 7474 59 96 -770 C ATOM 666 CD1 PHE A 108 -25.507 -13.140 -6.458 1.00 55.84 C ANISOU 666 CD1 PHE A 108 6426 7540 7249 30 158 -699 C ATOM 667 CD2 PHE A 108 -24.704 -13.999 -4.390 1.00 54.51 C ANISOU 667 CD2 PHE A 108 6546 7305 6859 117 151 -798 C ATOM 668 CE1 PHE A 108 -26.304 -14.246 -6.611 1.00 65.68 C ANISOU 668 CE1 PHE A 108 7613 8842 8500 26 254 -688 C ATOM 669 CE2 PHE A 108 -25.499 -15.112 -4.534 1.00 60.93 C ANISOU 669 CE2 PHE A 108 7318 8156 7678 111 299 -745 C ATOM 670 CZ PHE A 108 -26.298 -15.244 -5.645 1.00 60.31 C ANISOU 670 CZ PHE A 108 7046 8132 7737 50 342 -707 C ATOM 671 N GLY A 109 -26.630 -10.709 -3.414 1.00 74.60 N ANISOU 671 N GLY A 109 9225 9604 9515 296 281 -895 N ATOM 672 CA GLY A 109 -27.401 -10.828 -2.207 1.00 61.91 C ANISOU 672 CA GLY A 109 7793 7956 7775 435 447 -941 C ATOM 673 C GLY A 109 -28.833 -10.843 -2.652 1.00 62.43 C ANISOU 673 C GLY A 109 7695 8046 7981 458 647 -864 C ATOM 674 O GLY A 109 -29.116 -10.766 -3.855 1.00 60.88 O ANISOU 674 O GLY A 109 7279 7904 7949 381 595 -798 O ATOM 675 N PRO A 110 -29.772 -10.928 -1.697 1.00 54.43 N ANISOU 675 N PRO A 110 6780 6994 6907 586 880 -874 N ATOM 676 CA PRO A 110 -29.474 -10.946 -0.271 1.00 51.10 C ANISOU 676 CA PRO A 110 6674 6514 6227 729 950 -948 C ATOM 677 C PRO A 110 -28.875 -12.269 0.148 1.00 53.26 C ANISOU 677 C PRO A 110 7061 6842 6334 713 965 -898 C ATOM 678 O PRO A 110 -29.391 -13.318 -0.298 1.00 49.10 O ANISOU 678 O PRO A 110 6375 6361 5921 632 1113 -787 O ATOM 679 CB PRO A 110 -30.845 -10.744 0.367 1.00 60.60 C ANISOU 679 CB PRO A 110 7896 7675 7453 874 1272 -924 C ATOM 680 CG PRO A 110 -31.795 -11.402 -0.619 1.00 50.51 C ANISOU 680 CG PRO A 110 6271 6464 6458 757 1396 -809 C ATOM 681 CD PRO A 110 -31.197 -11.194 -1.973 1.00 45.60 C ANISOU 681 CD PRO A 110 5455 5899 5971 606 1109 -805 C ATOM 682 N VAL A 111 -27.816 -12.249 0.960 1.00 57.32 N ANISOU 682 N VAL A 111 7835 7338 6607 794 796 -989 N ATOM 683 CA VAL A 111 -27.106 -13.486 1.273 1.00 66.20 C ANISOU 683 CA VAL A 111 9066 8511 7576 800 762 -933 C ATOM 684 C VAL A 111 -27.070 -13.822 2.748 1.00 72.95 C ANISOU 684 C VAL A 111 10302 9336 8082 1033 873 -947 C ATOM 685 O VAL A 111 -26.780 -14.987 3.079 1.00 79.96 O ANISOU 685 O VAL A 111 11301 10244 8836 1074 938 -846 O ATOM 686 CB VAL A 111 -25.670 -13.499 0.703 1.00 56.30 C ANISOU 686 CB VAL A 111 7731 7298 6363 691 417 -1000 C ATOM 687 CG1 VAL A 111 -25.726 -13.667 -0.812 1.00 53.58 C ANISOU 687 CG1 VAL A 111 7050 7010 6298 488 390 -922 C ATOM 688 CG2 VAL A 111 -24.909 -12.243 1.114 1.00 48.55 C ANISOU 688 CG2 VAL A 111 6851 6251 5345 736 155 -1184 C ATOM 689 N GLY A 112 -27.317 -12.878 3.650 1.00 64.36 N ANISOU 689 N GLY A 112 9448 8191 6815 1211 896 -1066 N ATOM 690 CA GLY A 112 -27.249 -13.354 5.022 1.00 66.78 C ANISOU 690 CA GLY A 112 10161 8489 6723 1470 1010 -1059 C ATOM 691 C GLY A 112 -25.854 -13.843 5.380 1.00 59.36 C ANISOU 691 C GLY A 112 9389 7592 5572 1528 666 -1132 C ATOM 692 O GLY A 112 -24.850 -13.381 4.826 1.00 58.21 O ANISOU 692 O GLY A 112 9083 7461 5573 1401 298 -1268 O ATOM 693 N PHE A 113 -25.795 -14.809 6.315 1.00 59.70 N ANISOU 693 N PHE A 113 9749 7649 5287 1735 804 -1024 N ATOM 694 CA PHE A 113 -24.525 -15.418 6.729 1.00 66.64 C ANISOU 694 CA PHE A 113 10804 8575 5942 1842 482 -1071 C ATOM 695 C PHE A 113 -23.780 -16.104 5.582 1.00 64.81 C ANISOU 695 C PHE A 113 10222 8385 6016 1597 304 -1013 C ATOM 696 O PHE A 113 -22.579 -16.370 5.705 1.00 66.18 O ANISOU 696 O PHE A 113 10432 8603 6110 1646 -38 -1099 O ATOM 697 CB PHE A 113 -24.736 -16.439 7.866 1.00 76.44 C ANISOU 697 CB PHE A 113 12466 9807 6771 2132 728 -901 C ATOM 698 CG PHE A 113 -25.121 -17.826 7.403 1.00 82.55 C ANISOU 698 CG PHE A 113 13116 10547 7702 2021 1039 -619 C ATOM 699 CD1 PHE A 113 -24.151 -18.775 7.098 1.00 86.33 C ANISOU 699 CD1 PHE A 113 13548 11050 8203 1990 824 -567 C ATOM 700 CD2 PHE A 113 -26.450 -18.199 7.318 1.00 93.02 C ANISOU 700 CD2 PHE A 113 14366 11797 9178 1960 1548 -420 C ATOM 701 CE1 PHE A 113 -24.500 -20.050 6.683 1.00 84.13 C ANISOU 701 CE1 PHE A 113 13174 10705 8088 1892 1102 -332 C ATOM 702 CE2 PHE A 113 -26.809 -19.474 6.905 1.00 98.68 C ANISOU 702 CE2 PHE A 113 14956 12444 10094 1840 1820 -190 C ATOM 703 CZ PHE A 113 -25.827 -20.401 6.584 1.00 93.85 C ANISOU 703 CZ PHE A 113 14327 11840 9491 1806 1593 -150 C ATOM 704 N MET A 114 -24.434 -16.396 4.470 1.00 63.29 N ANISOU 704 N MET A 114 9691 8187 6168 1355 509 -887 N ATOM 705 CA MET A 114 -23.624 -16.863 3.348 1.00 54.34 C ANISOU 705 CA MET A 114 8253 7103 5292 1150 305 -879 C ATOM 706 C MET A 114 -22.713 -15.768 2.778 1.00 54.05 C ANISOU 706 C MET A 114 8018 7093 5426 1031 -55 -1069 C ATOM 707 O MET A 114 -21.917 -16.049 1.874 1.00 57.02 O ANISOU 707 O MET A 114 8147 7515 6004 882 -219 -1069 O ATOM 708 CB MET A 114 -24.526 -17.465 2.271 1.00 43.54 C ANISOU 708 CB MET A 114 6595 5725 4222 944 572 -730 C ATOM 709 CG MET A 114 -25.003 -18.841 2.663 1.00 62.92 C ANISOU 709 CG MET A 114 9180 8121 6605 1009 862 -543 C ATOM 710 SD MET A 114 -23.615 -19.992 2.887 1.00 59.92 S ANISOU 710 SD MET A 114 8942 7757 6068 1111 634 -510 S ATOM 711 CE MET A 114 -22.948 -19.942 1.231 1.00 49.47 C ANISOU 711 CE MET A 114 7183 6512 5101 842 400 -593 C ATOM 712 N LYS A 115 -22.749 -14.551 3.325 1.00 58.58 N ANISOU 712 N LYS A 115 8705 7620 5931 1105 -172 -1235 N ATOM 713 CA LYS A 115 -21.762 -13.540 2.945 1.00 62.97 C ANISOU 713 CA LYS A 115 9096 8154 6676 998 -519 -1422 C ATOM 714 C LYS A 115 -20.332 -13.999 3.237 1.00 70.39 C ANISOU 714 C LYS A 115 10046 9140 7559 1053 -866 -1522 C ATOM 715 O LYS A 115 -19.381 -13.531 2.593 1.00 75.99 O ANISOU 715 O LYS A 115 10492 9841 8539 899 -1108 -1617 O ATOM 716 CB LYS A 115 -22.030 -12.224 3.690 1.00 73.47 C ANISOU 716 CB LYS A 115 10605 9386 7923 1102 -601 -1616 C ATOM 717 CG LYS A 115 -21.707 -12.309 5.191 1.00 86.39 C ANISOU 717 CG LYS A 115 12660 11022 9143 1403 -753 -1765 C ATOM 718 CD LYS A 115 -21.402 -10.944 5.829 1.00 93.12 C ANISOU 718 CD LYS A 115 13648 11767 9967 1485 -1026 -2065 C ATOM 719 CE LYS A 115 -20.969 -11.077 7.293 1.00 90.88 C ANISOU 719 CE LYS A 115 13805 11504 9221 1819 -1249 -2251 C ATOM 720 NZ LYS A 115 -22.058 -11.598 8.174 1.00 96.49 N ANISOU 720 NZ LYS A 115 14904 12249 9510 2088 -864 -2104 N ATOM 721 N SER A 116 -20.150 -14.899 4.206 1.00 59.15 N ANISOU 721 N SER A 116 8918 7756 5802 1285 -885 -1491 N ATOM 722 CA SER A 116 -18.803 -15.360 4.539 1.00 59.11 C ANISOU 722 CA SER A 116 8922 7802 5735 1381 -1247 -1592 C ATOM 723 C SER A 116 -18.271 -16.415 3.576 1.00 54.72 C ANISOU 723 C SER A 116 8098 7307 5387 1248 -1213 -1441 C ATOM 724 O SER A 116 -17.168 -16.923 3.794 1.00 60.25 O ANISOU 724 O SER A 116 8776 8054 6063 1342 -1488 -1502 O ATOM 725 CB SER A 116 -18.765 -15.920 5.972 1.00 60.50 C ANISOU 725 CB SER A 116 9564 7998 5426 1737 -1308 -1608 C ATOM 726 OG SER A 116 -19.470 -15.072 6.875 1.00 69.03 O ANISOU 726 OG SER A 116 10952 9027 6250 1899 -1244 -1721 O ATOM 727 N ALA A 117 -19.032 -16.795 2.556 1.00 54.79 N ANISOU 727 N ALA A 117 7916 7316 5585 1062 -899 -1262 N ATOM 728 CA ALA A 117 -18.537 -17.773 1.606 1.00 57.45 C ANISOU 728 CA ALA A 117 8021 7703 6104 953 -870 -1152 C ATOM 729 C ALA A 117 -17.533 -17.087 0.706 1.00 57.21 C ANISOU 729 C ALA A 117 7643 7702 6393 776 -1092 -1261 C ATOM 730 O ALA A 117 -17.726 -15.936 0.313 1.00 51.86 O ANISOU 730 O ALA A 117 6833 6983 5886 640 -1102 -1329 O ATOM 731 CB ALA A 117 -19.677 -18.377 0.789 1.00 45.20 C ANISOU 731 CB ALA A 117 6381 6137 4655 821 -506 -971 C ATOM 732 N ILE A 118 -16.445 -17.793 0.406 1.00 55.26 N ANISOU 732 N ILE A 118 7249 7509 6239 793 -1249 -1265 N ATOM 733 CA ILE A 118 -15.309 -17.181 -0.276 1.00 49.92 C ANISOU 733 CA ILE A 118 6235 6853 5880 656 -1456 -1371 C ATOM 734 C ILE A 118 -15.718 -16.597 -1.625 1.00 46.58 C ANISOU 734 C ILE A 118 5557 6424 5717 417 -1242 -1285 C ATOM 735 O ILE A 118 -15.187 -15.560 -2.046 1.00 48.61 O ANISOU 735 O ILE A 118 5600 6640 6230 283 -1335 -1360 O ATOM 736 CB ILE A 118 -14.173 -18.210 -0.417 1.00 57.54 C ANISOU 736 CB ILE A 118 7073 7885 6904 741 -1599 -1363 C ATOM 737 CG1 ILE A 118 -12.916 -17.552 -0.957 1.00 62.28 C ANISOU 737 CG1 ILE A 118 7301 8497 7867 620 -1809 -1484 C ATOM 738 CG2 ILE A 118 -14.611 -19.402 -1.268 1.00 57.58 C ANISOU 738 CG2 ILE A 118 7053 7924 6901 710 -1316 -1178 C ATOM 739 CD1 ILE A 118 -11.865 -18.570 -1.351 1.00 73.78 C ANISOU 739 CD1 ILE A 118 8563 10029 9443 688 -1878 -1455 C ATOM 740 N SER A 119 -16.647 -17.263 -2.338 1.00 45.41 N ANISOU 740 N SER A 119 5428 6306 5520 368 -959 -1127 N ATOM 741 CA SER A 119 -17.075 -16.786 -3.643 1.00 52.18 C ANISOU 741 CA SER A 119 6083 7179 6563 192 -783 -1044 C ATOM 742 C SER A 119 -17.899 -15.500 -3.547 1.00 51.93 C ANISOU 742 C SER A 119 6095 7072 6562 128 -732 -1067 C ATOM 743 O SER A 119 -18.157 -14.866 -4.576 1.00 48.23 O ANISOU 743 O SER A 119 5473 6602 6251 6 -626 -999 O ATOM 744 CB SER A 119 -17.883 -17.871 -4.375 1.00 51.94 C ANISOU 744 CB SER A 119 6068 7198 6469 179 -556 -920 C ATOM 745 OG SER A 119 -19.035 -18.226 -3.633 1.00 54.01 O ANISOU 745 OG SER A 119 6552 7411 6557 251 -427 -885 O ATOM 746 N ILE A 120 -18.301 -15.112 -2.345 1.00 48.35 N ANISOU 746 N ILE A 120 5871 6554 5945 238 -800 -1155 N ATOM 747 CA ILE A 120 -19.088 -13.910 -2.130 1.00 58.63 C ANISOU 747 CA ILE A 120 7241 7767 7267 214 -751 -1198 C ATOM 748 C ILE A 120 -18.298 -12.837 -1.384 1.00 62.27 C ANISOU 748 C ILE A 120 7729 8128 7803 231 -1016 -1392 C ATOM 749 O ILE A 120 -18.657 -11.651 -1.468 1.00 57.27 O ANISOU 749 O ILE A 120 7081 7384 7293 169 -1005 -1441 O ATOM 750 CB ILE A 120 -20.402 -14.274 -1.399 1.00 58.90 C ANISOU 750 CB ILE A 120 7523 7793 7063 337 -554 -1150 C ATOM 751 CG1 ILE A 120 -21.217 -15.190 -2.324 1.00 54.42 C ANISOU 751 CG1 ILE A 120 6847 7291 6537 268 -314 -988 C ATOM 752 CG2 ILE A 120 -21.247 -13.055 -0.995 1.00 58.11 C ANISOU 752 CG2 ILE A 120 7522 7598 6960 363 -495 -1212 C ATOM 753 CD1 ILE A 120 -22.241 -16.010 -1.607 1.00 51.73 C ANISOU 753 CD1 ILE A 120 6697 6936 6022 374 -103 -918 C ATOM 754 N ALA A 121 -17.188 -13.195 -0.745 1.00 53.81 N ANISOU 754 N ALA A 121 6667 7076 6702 308 -1276 -1516 N ATOM 755 CA ALA A 121 -16.515 -12.257 0.133 1.00 60.11 C ANISOU 755 CA ALA A 121 7516 7771 7552 352 -1582 -1755 C ATOM 756 C ALA A 121 -15.729 -11.240 -0.691 1.00 46.13 C ANISOU 756 C ALA A 121 5413 5896 6218 132 -1666 -1804 C ATOM 757 O ALA A 121 -15.549 -11.380 -1.909 1.00 55.71 O ANISOU 757 O ALA A 121 6375 7145 7646 -20 -1489 -1635 O ATOM 758 CB ALA A 121 -15.611 -13.000 1.113 1.00 65.39 C ANISOU 758 CB ALA A 121 8301 8503 8039 540 -1875 -1886 C ATOM 759 N GLU A 122 -15.248 -10.229 -0.007 1.00 48.81 N ANISOU 759 N GLU A 122 5766 6093 6688 128 -1930 -2039 N ATOM 760 CA GLU A 122 -14.638 -9.067 -0.626 1.00 54.81 C ANISOU 760 CA GLU A 122 6242 6680 7904 -89 -1984 -2096 C ATOM 761 C GLU A 122 -13.313 -8.734 0.026 1.00 59.61 C ANISOU 761 C GLU A 122 6692 7203 8754 -104 -2394 -2376 C ATOM 762 O GLU A 122 -13.076 -9.037 1.202 1.00 66.53 O ANISOU 762 O GLU A 122 7779 8122 9377 96 -2697 -2592 O ATOM 763 CB GLU A 122 -15.553 -7.820 -0.536 1.00 57.09 C ANISOU 763 CB GLU A 122 6671 6785 8234 -122 -1883 -2134 C ATOM 764 CG GLU A 122 -16.847 -8.024 -1.273 1.00 60.48 C ANISOU 764 CG GLU A 122 7188 7288 8502 -114 -1509 -1872 C ATOM 765 CD GLU A 122 -17.614 -6.724 -1.486 1.00 70.52 C ANISOU 765 CD GLU A 122 8512 8367 9917 -166 -1390 -1866 C ATOM 766 OE1 GLU A 122 -18.312 -6.632 -2.520 1.00 71.83 O ANISOU 766 OE1 GLU A 122 8602 8557 10133 -227 -1119 -1632 O ATOM 767 OE2 GLU A 122 -17.513 -5.808 -0.628 1.00 74.44 O ANISOU 767 OE2 GLU A 122 9133 8682 10469 -126 -1585 -2107 O ATOM 768 N ASP A 123 -12.459 -8.098 -0.769 1.00 60.33 N ANISOU 768 N ASP A 123 6405 7169 9347 -335 -2393 -2365 N ATOM 769 CA ASP A 123 -11.243 -7.470 -0.294 1.00 65.47 C ANISOU 769 CA ASP A 123 6814 7668 10394 -420 -2766 -2650 C ATOM 770 C ASP A 123 -10.479 -8.355 0.690 1.00 65.65 C ANISOU 770 C ASP A 123 6881 7839 10223 -214 -3158 -2861 C ATOM 771 O ASP A 123 -10.226 -9.531 0.408 1.00 67.77 O ANISOU 771 O ASP A 123 7098 8310 10341 -128 -3080 -2706 O ATOM 772 CB ASP A 123 -11.606 -6.116 0.328 1.00 70.88 C ANISOU 772 CB ASP A 123 7646 8092 11193 -456 -2916 -2883 C ATOM 773 CG ASP A 123 -12.460 -5.240 -0.610 1.00 78.79 C ANISOU 773 CG ASP A 123 8648 8937 12350 -612 -2525 -2652 C ATOM 774 OD1 ASP A 123 -12.209 -5.233 -1.834 1.00 76.34 O ANISOU 774 OD1 ASP A 123 8064 8620 12321 -790 -2237 -2385 O ATOM 775 OD2 ASP A 123 -13.381 -4.542 -0.114 1.00 86.03 O ANISOU 775 OD2 ASP A 123 9856 9736 13095 -530 -2506 -2736 O ATOM 776 N GLU A 124 -10.140 -7.806 1.858 1.00 64.31 N ANISOU 776 N GLU A 124 6837 7566 10032 -107 -3594 -3222 N ATOM 777 CA GLU A 124 -9.247 -8.498 2.782 1.00 82.16 C ANISOU 777 CA GLU A 124 9134 9950 12132 115 -3948 -3377 C ATOM 778 C GLU A 124 -9.887 -9.752 3.357 1.00 74.72 C ANISOU 778 C GLU A 124 8583 9244 10563 418 -3957 -3306 C ATOM 779 O GLU A 124 -9.184 -10.731 3.643 1.00 70.32 O ANISOU 779 O GLU A 124 7991 8835 9891 582 -4098 -3276 O ATOM 780 CB GLU A 124 -8.812 -7.536 3.902 1.00 84.42 C ANISOU 780 CB GLU A 124 9540 10073 12464 205 -4274 -3671 C ATOM 781 CG GLU A 124 -8.299 -6.216 3.362 1.00 99.48 C ANISOU 781 CG GLU A 124 11100 11704 14994 -96 -4239 -3739 C ATOM 782 CD GLU A 124 -7.128 -6.405 2.399 1.00114.43 C ANISOU 782 CD GLU A 124 12463 13586 17429 -314 -4140 -3606 C ATOM 783 OE1 GLU A 124 -6.129 -7.039 2.804 1.00118.63 O ANISOU 783 OE1 GLU A 124 12860 14226 17989 -191 -4368 -3682 O ATOM 784 OE2 GLU A 124 -7.207 -5.937 1.237 1.00118.11 O ANISOU 784 OE2 GLU A 124 12661 13935 18282 -587 -3814 -3413 O ATOM 785 N GLU A 125 -11.205 -9.737 3.544 1.00 62.75 N ANISOU 785 N GLU A 125 7460 7744 8639 513 -3679 -3180 N ATOM 786 CA GLU A 125 -11.902 -10.941 3.976 1.00 68.00 C ANISOU 786 CA GLU A 125 8492 8598 8747 773 -3510 -2994 C ATOM 787 C GLU A 125 -11.747 -12.061 2.962 1.00 71.61 C ANISOU 787 C GLU A 125 8728 9193 9287 691 -3230 -2689 C ATOM 788 O GLU A 125 -11.534 -13.218 3.341 1.00 77.56 O ANISOU 788 O GLU A 125 9617 10086 9766 898 -3285 -2617 O ATOM 789 CB GLU A 125 -13.381 -10.638 4.202 1.00 72.14 C ANISOU 789 CB GLU A 125 9387 9087 8934 839 -3177 -2882 C ATOM 790 CG GLU A 125 -13.693 -9.955 5.522 1.00 92.77 C ANISOU 790 CG GLU A 125 12398 11623 11229 1071 -3425 -3169 C ATOM 791 CD GLU A 125 -13.149 -8.529 5.628 1.00111.90 C ANISOU 791 CD GLU A 125 14647 13826 14046 919 -3735 -3497 C ATOM 792 OE1 GLU A 125 -13.136 -7.813 4.602 1.00116.74 O ANISOU 792 OE1 GLU A 125 14926 14301 15130 615 -3555 -3408 O ATOM 793 OE2 GLU A 125 -12.735 -8.126 6.744 1.00119.64 O ANISOU 793 OE2 GLU A 125 15816 14760 14882 1107 -4049 -3737 O ATOM 794 N TRP A 126 -11.877 -11.742 1.670 1.00 60.78 N ANISOU 794 N TRP A 126 7050 7777 8268 416 -2920 -2503 N ATOM 795 CA TRP A 126 -11.689 -12.744 0.629 1.00 57.34 C ANISOU 795 CA TRP A 126 6406 7466 7915 346 -2663 -2247 C ATOM 796 C TRP A 126 -10.250 -13.249 0.617 1.00 66.63 C ANISOU 796 C TRP A 126 7273 8702 9342 373 -2942 -2348 C ATOM 797 O TRP A 126 -10.003 -14.463 0.602 1.00 60.84 O ANISOU 797 O TRP A 126 6573 8103 8439 520 -2921 -2242 O ATOM 798 CB TRP A 126 -12.067 -12.177 -0.754 1.00 54.61 C ANISOU 798 CB TRP A 126 5822 7061 7866 82 -2302 -2048 C ATOM 799 CG TRP A 126 -11.574 -13.084 -1.842 1.00 55.96 C ANISOU 799 CG TRP A 126 5739 7352 8170 19 -2106 -1852 C ATOM 800 CD1 TRP A 126 -12.126 -14.274 -2.228 1.00 51.90 C ANISOU 800 CD1 TRP A 126 5357 6973 7390 110 -1879 -1664 C ATOM 801 CD2 TRP A 126 -10.362 -12.946 -2.604 1.00 63.56 C ANISOU 801 CD2 TRP A 126 6276 8301 9572 -123 -2128 -1850 C ATOM 802 NE1 TRP A 126 -11.363 -14.869 -3.211 1.00 52.61 N ANISOU 802 NE1 TRP A 126 5160 7139 7690 48 -1767 -1558 N ATOM 803 CE2 TRP A 126 -10.272 -14.081 -3.463 1.00 64.04 C ANISOU 803 CE2 TRP A 126 6261 8510 9563 -88 -1893 -1654 C ATOM 804 CE3 TRP A 126 -9.354 -11.982 -2.654 1.00 67.02 C ANISOU 804 CE3 TRP A 126 6378 8600 10487 -281 -2300 -1997 C ATOM 805 CZ2 TRP A 126 -9.222 -14.261 -4.368 1.00 67.23 C ANISOU 805 CZ2 TRP A 126 6284 8947 10314 -179 -1802 -1590 C ATOM 806 CZ3 TRP A 126 -8.306 -12.158 -3.563 1.00 70.89 C ANISOU 806 CZ3 TRP A 126 6451 9112 11373 -398 -2191 -1914 C ATOM 807 CH2 TRP A 126 -8.244 -13.288 -4.403 1.00 70.76 C ANISOU 807 CH2 TRP A 126 6387 9266 11233 -333 -1934 -1708 C ATOM 808 N LYS A 127 -9.289 -12.317 0.612 1.00 71.08 N ANISOU 808 N LYS A 127 7511 9144 10352 229 -3198 -2555 N ATOM 809 CA LYS A 127 -7.874 -12.666 0.634 1.00 71.75 C ANISOU 809 CA LYS A 127 7228 9270 10764 243 -3491 -2686 C ATOM 810 C LYS A 127 -7.563 -13.654 1.756 1.00 79.32 C ANISOU 810 C LYS A 127 8437 10364 11337 584 -3839 -2807 C ATOM 811 O LYS A 127 -6.900 -14.675 1.537 1.00 72.49 O ANISOU 811 O LYS A 127 7422 9623 10500 692 -3867 -2727 O ATOM 812 CB LYS A 127 -7.048 -11.393 0.794 1.00 83.06 C ANISOU 812 CB LYS A 127 8372 10500 12688 64 -3710 -2909 C ATOM 813 CG LYS A 127 -5.728 -11.416 0.054 1.00 95.31 C ANISOU 813 CG LYS A 127 9424 12023 14768 -87 -3641 -2847 C ATOM 814 CD LYS A 127 -5.695 -10.321 -1.001 1.00102.57 C ANISOU 814 CD LYS A 127 10042 12756 16176 -417 -3334 -2736 C ATOM 815 CE LYS A 127 -6.007 -8.943 -0.406 1.00111.92 C ANISOU 815 CE LYS A 127 11358 13697 17468 -511 -3472 -2924 C ATOM 816 NZ LYS A 127 -5.876 -7.824 -1.398 1.00115.30 N ANISOU 816 NZ LYS A 127 11500 13899 18411 -820 -3171 -2799 N ATOM 817 N ARG A 128 -8.060 -13.366 2.966 1.00 75.35 N ANISOU 817 N ARG A 128 8354 9833 10444 786 -4068 -2975 N ATOM 818 CA ARG A 128 -7.901 -14.280 4.090 1.00 77.15 C ANISOU 818 CA ARG A 128 8935 10169 10211 1152 -4293 -3008 C ATOM 819 C ARG A 128 -8.545 -15.635 3.809 1.00 75.25 C ANISOU 819 C ARG A 128 8915 10074 9602 1299 -4017 -2730 C ATOM 820 O ARG A 128 -7.938 -16.688 4.034 1.00 67.44 O ANISOU 820 O ARG A 128 7931 9188 8504 1510 -4157 -2687 O ATOM 821 CB ARG A 128 -8.506 -13.660 5.339 1.00 80.11 C ANISOU 821 CB ARG A 128 9772 10474 10192 1341 -4440 -3169 C ATOM 822 CG ARG A 128 -8.605 -14.609 6.500 1.00 79.67 C ANISOU 822 CG ARG A 128 10162 10522 9589 1747 -4593 -3152 C ATOM 823 CD ARG A 128 -8.990 -13.870 7.763 1.00 78.18 C ANISOU 823 CD ARG A 128 10404 10259 9043 1943 -4713 -3315 C ATOM 824 NE ARG A 128 -9.491 -14.809 8.755 1.00 85.53 N ANISOU 824 NE ARG A 128 11821 11287 9391 2348 -4751 -3226 N ATOM 825 CZ ARG A 128 -10.776 -15.117 8.901 1.00 82.76 C ANISOU 825 CZ ARG A 128 11904 10992 8550 2506 -4435 -3016 C ATOM 826 NH1 ARG A 128 -11.686 -14.536 8.136 1.00 69.17 N ANISOU 826 NH1 ARG A 128 10183 9252 6847 2296 -4097 -2913 N ATOM 827 NH2 ARG A 128 -11.150 -15.996 9.822 1.00 89.70 N ANISOU 827 NH2 ARG A 128 13220 11930 8932 2879 -4434 -2902 N ATOM 828 N LEU A 129 -9.792 -15.633 3.349 1.00 64.22 N ANISOU 828 N LEU A 129 7720 8652 8030 1194 -3559 -2503 N ATOM 829 CA LEU A 129 -10.483 -16.903 3.171 1.00 69.19 C ANISOU 829 CA LEU A 129 8588 9362 8340 1314 -3225 -2218 C ATOM 830 C LEU A 129 -9.832 -17.734 2.070 1.00 67.93 C ANISOU 830 C LEU A 129 8071 9265 8472 1211 -3080 -2066 C ATOM 831 O LEU A 129 -9.710 -18.958 2.200 1.00 61.85 O ANISOU 831 O LEU A 129 7429 8559 7511 1400 -3039 -1939 O ATOM 832 CB LEU A 129 -11.957 -16.658 2.866 1.00 69.45 C ANISOU 832 CB LEU A 129 8840 9345 8203 1202 -2791 -2041 C ATOM 833 CG LEU A 129 -12.812 -16.025 3.957 1.00 69.81 C ANISOU 833 CG LEU A 129 9299 9335 7892 1350 -2821 -2141 C ATOM 834 CD1 LEU A 129 -14.137 -15.612 3.340 1.00 72.01 C ANISOU 834 CD1 LEU A 129 9619 9558 8185 1170 -2387 -1977 C ATOM 835 CD2 LEU A 129 -13.010 -16.978 5.103 1.00 66.20 C ANISOU 835 CD2 LEU A 129 9293 8933 6929 1708 -2873 -2086 C ATOM 836 N ARG A 130 -9.404 -17.084 0.983 1.00 60.53 N ANISOU 836 N ARG A 130 6707 8297 7994 928 -2978 -2070 N ATOM 837 CA ARG A 130 -8.735 -17.804 -0.093 1.00 62.92 C ANISOU 837 CA ARG A 130 6674 8666 8568 850 -2818 -1940 C ATOM 838 C ARG A 130 -7.429 -18.416 0.393 1.00 69.54 C ANISOU 838 C ARG A 130 7335 9567 9518 1048 -3184 -2071 C ATOM 839 O ARG A 130 -7.081 -19.537 0.012 1.00 66.53 O ANISOU 839 O ARG A 130 6899 9258 9122 1159 -3087 -1948 O ATOM 840 CB ARG A 130 -8.486 -16.868 -1.270 1.00 57.61 C ANISOU 840 CB ARG A 130 5607 7939 8344 541 -2626 -1911 C ATOM 841 CG ARG A 130 -7.831 -17.525 -2.453 1.00 53.13 C ANISOU 841 CG ARG A 130 4712 7444 8031 473 -2404 -1771 C ATOM 842 CD ARG A 130 -8.839 -17.964 -3.510 1.00 55.02 C ANISOU 842 CD ARG A 130 5079 7717 8108 390 -1960 -1533 C ATOM 843 NE ARG A 130 -8.215 -18.767 -4.563 1.00 52.73 N ANISOU 843 NE ARG A 130 4550 7509 7977 392 -1762 -1422 N ATOM 844 CZ ARG A 130 -8.770 -19.074 -5.734 1.00 53.30 C ANISOU 844 CZ ARG A 130 4633 7621 7999 312 -1404 -1254 C ATOM 845 NH1 ARG A 130 -9.988 -18.633 -6.039 1.00 45.22 N ANISOU 845 NH1 ARG A 130 3816 6566 6798 211 -1217 -1167 N ATOM 846 NH2 ARG A 130 -8.096 -19.836 -6.597 1.00 49.89 N ANISOU 846 NH2 ARG A 130 4005 7265 7688 358 -1251 -1188 N ATOM 847 N SER A 131 -6.701 -17.689 1.245 1.00 73.54 N ANISOU 847 N SER A 131 7749 10041 10153 1107 -3632 -2343 N ATOM 848 CA SER A 131 -5.481 -18.216 1.842 1.00 76.23 C ANISOU 848 CA SER A 131 7923 10449 10591 1334 -4063 -2506 C ATOM 849 C SER A 131 -5.788 -19.378 2.776 1.00 77.93 C ANISOU 849 C SER A 131 8611 10737 10262 1712 -4169 -2427 C ATOM 850 O SER A 131 -5.094 -20.402 2.761 1.00 78.78 O ANISOU 850 O SER A 131 8634 10917 10382 1910 -4263 -2374 O ATOM 851 CB SER A 131 -4.762 -17.103 2.609 1.00 84.04 C ANISOU 851 CB SER A 131 8829 11313 11789 1279 -4361 -2754 C ATOM 852 OG SER A 131 -3.590 -17.575 3.248 1.00 96.39 O ANISOU 852 OG SER A 131 9914 12844 13865 1171 -4433 -2817 O ATOM 853 N LEU A 132 -6.796 -19.211 3.634 1.00 72.02 N ANISOU 853 N LEU A 132 8368 9957 9039 1838 -4147 -2415 N ATOM 854 CA LEU A 132 -7.160 -20.263 4.569 1.00 72.37 C ANISOU 854 CA LEU A 132 8910 10043 8544 2206 -4187 -2300 C ATOM 855 C LEU A 132 -7.689 -21.503 3.859 1.00 68.28 C ANISOU 855 C LEU A 132 8482 9526 7934 2204 -3732 -1976 C ATOM 856 O LEU A 132 -7.625 -22.606 4.418 1.00 68.04 O ANISOU 856 O LEU A 132 8738 9511 7602 2508 -3768 -1855 O ATOM 857 CB LEU A 132 -8.201 -19.740 5.559 1.00 65.94 C ANISOU 857 CB LEU A 132 8607 9184 7261 2323 -4166 -2333 C ATOM 858 CG LEU A 132 -7.777 -18.758 6.658 1.00 75.28 C ANISOU 858 CG LEU A 132 9904 10318 8382 2429 -4547 -2620 C ATOM 859 CD1 LEU A 132 -9.005 -18.259 7.397 1.00 72.78 C ANISOU 859 CD1 LEU A 132 10085 9958 7612 2521 -4398 -2612 C ATOM 860 CD2 LEU A 132 -6.819 -19.434 7.621 1.00 77.17 C ANISOU 860 CD2 LEU A 132 10270 10580 8469 2765 -4852 -2674 C ATOM 861 N LEU A 133 -8.215 -21.352 2.648 1.00 59.63 N ANISOU 861 N LEU A 133 7169 8400 7087 1886 -3319 -1840 N ATOM 862 CA LEU A 133 -8.823 -22.483 1.964 1.00 60.50 C ANISOU 862 CA LEU A 133 7382 8491 7113 1872 -2908 -1577 C ATOM 863 C LEU A 133 -7.944 -23.088 0.879 1.00 64.94 C ANISOU 863 C LEU A 133 7538 9097 8038 1801 -2838 -1539 C ATOM 864 O LEU A 133 -8.177 -24.239 0.506 1.00 64.20 O ANISOU 864 O LEU A 133 7554 8980 7860 1881 -2608 -1369 O ATOM 865 CB LEU A 133 -10.179 -22.083 1.349 1.00 54.07 C ANISOU 865 CB LEU A 133 6667 7621 6258 1619 -2483 -1446 C ATOM 866 CG LEU A 133 -11.260 -21.673 2.351 1.00 62.88 C ANISOU 866 CG LEU A 133 8212 8682 6997 1706 -2427 -1432 C ATOM 867 CD1 LEU A 133 -12.505 -21.158 1.592 1.00 66.09 C ANISOU 867 CD1 LEU A 133 8599 9041 7470 1435 -2036 -1330 C ATOM 868 CD2 LEU A 133 -11.607 -22.778 3.347 1.00 55.69 C ANISOU 868 CD2 LEU A 133 7757 7736 5666 2026 -2385 -1289 C ATOM 869 N SER A 134 -6.967 -22.347 0.355 1.00 72.04 N ANISOU 869 N SER A 134 7976 10041 9356 1652 -3001 -1691 N ATOM 870 CA SER A 134 -6.099 -22.861 -0.704 1.00 73.11 C ANISOU 870 CA SER A 134 7708 10224 9847 1598 -2887 -1651 C ATOM 871 C SER A 134 -5.485 -24.221 -0.379 1.00 69.08 C ANISOU 871 C SER A 134 7275 9738 9234 1913 -3004 -1599 C ATOM 872 O SER A 134 -5.520 -25.107 -1.248 1.00 64.00 O ANISOU 872 O SER A 134 6577 9090 8650 1908 -2714 -1463 O ATOM 873 CB SER A 134 -4.973 -21.859 -0.999 1.00 86.53 C ANISOU 873 CB SER A 134 8892 11949 12035 1447 -3102 -1837 C ATOM 874 OG SER A 134 -5.457 -20.571 -1.334 1.00 91.67 O ANISOU 874 OG SER A 134 9521 12539 12772 1220 -3124 -1931 O ATOM 875 N PRO A 135 -4.906 -24.454 0.805 1.00 67.39 N ANISOU 875 N PRO A 135 7198 9545 8862 2214 -3427 -1709 N ATOM 876 CA PRO A 135 -4.271 -25.761 1.053 1.00 78.72 C ANISOU 876 CA PRO A 135 8697 10992 10222 2541 -3537 -1639 C ATOM 877 C PRO A 135 -5.244 -26.910 0.950 1.00 77.43 C ANISOU 877 C PRO A 135 8956 10730 9732 2629 -3172 -1389 C ATOM 878 O PRO A 135 -4.830 -28.055 0.744 1.00 82.15 O ANISOU 878 O PRO A 135 9563 11298 10352 2825 -3119 -1294 O ATOM 879 CB PRO A 135 -3.722 -25.620 2.478 1.00 80.77 C ANISOU 879 CB PRO A 135 9133 11288 10267 2865 -4081 -1800 C ATOM 880 CG PRO A 135 -3.673 -24.137 2.734 1.00 77.85 C ANISOU 880 CG PRO A 135 8591 10939 10050 2654 -4306 -2031 C ATOM 881 CD PRO A 135 -4.834 -23.590 1.999 1.00 66.96 C ANISOU 881 CD PRO A 135 7296 9498 8649 2312 -3841 -1904 C ATOM 882 N THR A 136 -6.537 -26.625 1.065 1.00 69.45 N ANISOU 882 N THR A 136 8273 9652 8464 2483 -2908 -1286 N ATOM 883 CA THR A 136 -7.557 -27.649 0.962 1.00 57.92 C ANISOU 883 CA THR A 136 7177 8068 6764 2519 -2541 -1060 C ATOM 884 C THR A 136 -7.737 -28.150 -0.473 1.00 55.32 C ANISOU 884 C THR A 136 6613 7710 6695 2306 -2179 -990 C ATOM 885 O THR A 136 -8.265 -29.249 -0.671 1.00 63.81 O ANISOU 885 O THR A 136 7908 8663 7674 2370 -1930 -841 O ATOM 886 CB THR A 136 -8.838 -27.053 1.565 1.00 72.12 C ANISOU 886 CB THR A 136 9328 9812 8263 2425 -2390 -1002 C ATOM 887 OG1 THR A 136 -8.759 -27.126 2.992 1.00 81.58 O ANISOU 887 OG1 THR A 136 10907 11001 9090 2747 -2655 -1003 O ATOM 888 CG2 THR A 136 -10.100 -27.714 1.082 1.00 54.05 C ANISOU 888 CG2 THR A 136 7249 7394 5894 2289 -1929 -805 C ATOM 889 N PHE A 137 -7.269 -27.397 -1.477 1.00 57.22 N ANISOU 889 N PHE A 137 6426 8048 7267 2073 -2143 -1096 N ATOM 890 CA PHE A 137 -7.505 -27.736 -2.879 1.00 59.58 C ANISOU 890 CA PHE A 137 6545 8342 7750 1888 -1797 -1043 C ATOM 891 C PHE A 137 -6.231 -28.097 -3.632 1.00 63.04 C ANISOU 891 C PHE A 137 6595 8855 8501 1964 -1833 -1107 C ATOM 892 O PHE A 137 -6.244 -28.137 -4.868 1.00 63.66 O ANISOU 892 O PHE A 137 6478 8965 8743 1816 -1563 -1094 O ATOM 893 CB PHE A 137 -8.222 -26.591 -3.596 1.00 55.78 C ANISOU 893 CB PHE A 137 5947 7903 7344 1565 -1612 -1061 C ATOM 894 CG PHE A 137 -9.637 -26.426 -3.156 1.00 59.36 C ANISOU 894 CG PHE A 137 6750 8273 7530 1479 -1468 -980 C ATOM 895 CD1 PHE A 137 -9.948 -25.626 -2.068 1.00 54.21 C ANISOU 895 CD1 PHE A 137 6273 7615 6708 1504 -1648 -1021 C ATOM 896 CD2 PHE A 137 -10.630 -27.132 -3.778 1.00 48.92 C ANISOU 896 CD2 PHE A 137 5579 6869 6138 1397 -1165 -881 C ATOM 897 CE1 PHE A 137 -11.254 -25.505 -1.631 1.00 49.44 C ANISOU 897 CE1 PHE A 137 5982 6934 5869 1449 -1476 -937 C ATOM 898 CE2 PHE A 137 -11.946 -27.023 -3.365 1.00 48.82 C ANISOU 898 CE2 PHE A 137 5840 6771 5937 1317 -1013 -805 C ATOM 899 CZ PHE A 137 -12.263 -26.218 -2.281 1.00 44.93 C ANISOU 899 CZ PHE A 137 5516 6281 5274 1349 -1146 -818 C ATOM 900 N THR A 138 -5.143 -28.370 -2.924 1.00 63.23 N ANISOU 900 N THR A 138 6509 8914 8604 2215 -2158 -1178 N ATOM 901 CA THR A 138 -3.890 -28.675 -3.595 1.00 72.45 C ANISOU 901 CA THR A 138 7256 10155 10117 2302 -2188 -1245 C ATOM 902 C THR A 138 -3.959 -30.054 -4.242 1.00 79.67 C ANISOU 902 C THR A 138 8290 10989 10992 2445 -1934 -1149 C ATOM 903 O THR A 138 -4.807 -30.891 -3.910 1.00 80.73 O ANISOU 903 O THR A 138 8835 10984 10853 2529 -1825 -1038 O ATOM 904 CB THR A 138 -2.699 -28.619 -2.630 1.00 68.46 C ANISOU 904 CB THR A 138 6565 9708 9738 2557 -2653 -1370 C ATOM 905 OG1 THR A 138 -2.728 -29.747 -1.746 1.00 67.04 O ANISOU 905 OG1 THR A 138 6750 9446 9275 2904 -2809 -1291 O ATOM 906 CG2 THR A 138 -2.758 -27.333 -1.829 1.00 74.31 C ANISOU 906 CG2 THR A 138 7278 10491 10466 2440 -2951 -1500 C ATOM 907 N SER A 139 -3.048 -30.283 -5.190 1.00 74.72 N ANISOU 907 N SER A 139 7289 10431 10669 2473 -1817 -1196 N ATOM 908 CA SER A 139 -3.027 -31.575 -5.861 1.00 78.20 C ANISOU 908 CA SER A 139 7830 10787 11094 2629 -1584 -1143 C ATOM 909 C SER A 139 -2.827 -32.708 -4.863 1.00 77.98 C ANISOU 909 C SER A 139 8083 10633 10913 2975 -1795 -1088 C ATOM 910 O SER A 139 -3.376 -33.802 -5.052 1.00 75.89 O ANISOU 910 O SER A 139 8122 10204 10509 3069 -1603 -1004 O ATOM 911 CB SER A 139 -1.942 -31.591 -6.935 1.00 75.76 C ANISOU 911 CB SER A 139 7063 10588 11135 2656 -1433 -1212 C ATOM 912 OG SER A 139 -0.664 -31.475 -6.342 1.00 81.51 O ANISOU 912 OG SER A 139 7447 11393 12131 2852 -1748 -1294 O ATOM 913 N GLY A 140 -2.073 -32.455 -3.786 1.00 76.68 N ANISOU 913 N GLY A 140 7838 10524 10771 3176 -2200 -1137 N ATOM 914 CA GLY A 140 -1.894 -33.468 -2.757 1.00 73.52 C ANISOU 914 CA GLY A 140 7756 10009 10172 3550 -2424 -1058 C ATOM 915 C GLY A 140 -3.200 -33.894 -2.109 1.00 77.62 C ANISOU 915 C GLY A 140 8854 10350 10289 3541 -2295 -894 C ATOM 916 O GLY A 140 -3.482 -35.089 -1.983 1.00 66.99 O ANISOU 916 O GLY A 140 7819 8812 8821 3733 -2162 -763 O ATOM 917 N LYS A 141 -4.013 -32.921 -1.671 1.00 72.07 N ANISOU 917 N LYS A 141 8295 9687 9403 3323 -2312 -893 N ATOM 918 CA LYS A 141 -5.314 -33.262 -1.100 1.00 72.81 C ANISOU 918 CA LYS A 141 8899 9613 9154 3291 -2126 -728 C ATOM 919 C LYS A 141 -6.199 -33.949 -2.131 1.00 68.43 C ANISOU 919 C LYS A 141 8432 8907 8660 3094 -1690 -655 C ATOM 920 O LYS A 141 -6.879 -34.931 -1.820 1.00 64.70 O ANISOU 920 O LYS A 141 8328 8213 8040 3189 -1513 -504 O ATOM 921 CB LYS A 141 -6.017 -32.013 -0.551 1.00 70.84 C ANISOU 921 CB LYS A 141 8740 9445 8732 3088 -2194 -764 C ATOM 922 CG LYS A 141 -5.188 -31.165 0.379 1.00 63.67 C ANISOU 922 CG LYS A 141 7717 8685 7789 3238 -2656 -904 C ATOM 923 CD LYS A 141 -5.060 -31.798 1.726 1.00 67.10 C ANISOU 923 CD LYS A 141 8570 9051 7874 3642 -2907 -808 C ATOM 924 CE LYS A 141 -3.706 -31.434 2.358 1.00 90.49 C ANISOU 924 CE LYS A 141 11280 12167 10934 3905 -3455 -996 C ATOM 925 NZ LYS A 141 -3.504 -29.969 2.472 1.00 76.67 N ANISOU 925 NZ LYS A 141 9253 10565 9312 3688 -3699 -1222 N ATOM 926 N LEU A 142 -6.205 -33.439 -3.362 1.00 63.68 N ANISOU 926 N LEU A 142 7505 8410 8281 2825 -1516 -764 N ATOM 927 CA LEU A 142 -7.050 -34.015 -4.396 1.00 60.72 C ANISOU 927 CA LEU A 142 7208 7915 7949 2646 -1158 -745 C ATOM 928 C LEU A 142 -6.706 -35.475 -4.618 1.00 69.60 C ANISOU 928 C LEU A 142 8449 8855 9140 2885 -1068 -707 C ATOM 929 O LEU A 142 -7.597 -36.323 -4.737 1.00 60.41 O ANISOU 929 O LEU A 142 7568 7464 7922 2846 -847 -634 O ATOM 930 CB LEU A 142 -6.892 -33.235 -5.700 1.00 59.44 C ANISOU 930 CB LEU A 142 6682 7925 7977 2401 -1024 -871 C ATOM 931 CG LEU A 142 -7.526 -33.869 -6.934 1.00 52.89 C ANISOU 931 CG LEU A 142 5894 7010 7192 2278 -714 -907 C ATOM 932 CD1 LEU A 142 -9.028 -34.124 -6.645 1.00 51.46 C ANISOU 932 CD1 LEU A 142 6055 6648 6847 2122 -568 -830 C ATOM 933 CD2 LEU A 142 -7.349 -32.948 -8.159 1.00 51.46 C ANISOU 933 CD2 LEU A 142 5398 7028 7128 2077 -588 -1004 C ATOM 934 N LYS A 143 -5.410 -35.779 -4.674 1.00 70.41 N ANISOU 934 N LYS A 143 8318 9034 9402 3134 -1237 -766 N ATOM 935 CA LYS A 143 -4.982 -37.157 -4.842 1.00 78.27 C ANISOU 935 CA LYS A 143 9420 9845 10475 3405 -1170 -735 C ATOM 936 C LYS A 143 -5.507 -38.027 -3.708 1.00 77.91 C ANISOU 936 C LYS A 143 9846 9541 10215 3608 -1198 -545 C ATOM 937 O LYS A 143 -5.912 -39.169 -3.933 1.00 76.99 O ANISOU 937 O LYS A 143 9967 9157 10127 3679 -992 -480 O ATOM 938 CB LYS A 143 -3.453 -37.210 -4.921 1.00 84.97 C ANISOU 938 CB LYS A 143 9902 10840 11541 3670 -1386 -824 C ATOM 939 CG LYS A 143 -2.881 -38.550 -5.309 1.00 96.75 C ANISOU 939 CG LYS A 143 11429 12167 13166 3961 -1296 -825 C ATOM 940 CD LYS A 143 -1.620 -38.357 -6.147 1.00105.13 C ANISOU 940 CD LYS A 143 11988 13425 14532 4054 -1307 -974 C ATOM 941 CE LYS A 143 -0.659 -37.344 -5.525 1.00109.81 C ANISOU 941 CE LYS A 143 12209 14261 15253 4106 -1653 -1027 C ATOM 942 NZ LYS A 143 0.580 -37.152 -6.341 1.00115.94 N ANISOU 942 NZ LYS A 143 12442 15213 16399 4182 -1617 -1156 N ATOM 943 N GLU A 144 -5.531 -37.498 -2.484 1.00 65.55 N ANISOU 943 N GLU A 144 8442 8035 8430 3709 -1436 -454 N ATOM 944 CA GLU A 144 -6.014 -38.290 -1.359 1.00 67.70 C ANISOU 944 CA GLU A 144 9205 8067 8452 3939 -1426 -234 C ATOM 945 C GLU A 144 -7.510 -38.563 -1.458 1.00 74.21 C ANISOU 945 C GLU A 144 10335 8664 9197 3678 -1057 -116 C ATOM 946 O GLU A 144 -7.969 -39.600 -0.957 1.00 70.97 O ANISOU 946 O GLU A 144 10300 7955 8712 3828 -891 75 O ATOM 947 CB GLU A 144 -5.677 -37.595 -0.033 1.00 74.79 C ANISOU 947 CB GLU A 144 10231 9108 9078 4143 -1781 -186 C ATOM 948 CG GLU A 144 -4.352 -38.059 0.553 1.00 92.18 C ANISOU 948 CG GLU A 144 12373 11362 11290 4590 -2153 -194 C ATOM 949 CD GLU A 144 -3.879 -37.213 1.720 1.00108.08 C ANISOU 949 CD GLU A 144 14428 13572 13066 4784 -2595 -237 C ATOM 950 OE1 GLU A 144 -3.904 -35.969 1.610 1.00108.31 O ANISOU 950 OE1 GLU A 144 14200 13812 13142 4530 -2717 -403 O ATOM 951 OE2 GLU A 144 -3.470 -37.794 2.751 1.00117.94 O ANISOU 951 OE2 GLU A 144 15983 14754 14076 5210 -2837 -113 O ATOM 952 N MET A 145 -8.273 -37.671 -2.121 1.00 62.26 N ANISOU 952 N MET A 145 8652 7270 7734 3296 -916 -222 N ATOM 953 CA MET A 145 -9.713 -37.828 -2.301 1.00 61.99 C ANISOU 953 CA MET A 145 8820 7048 7686 3023 -590 -149 C ATOM 954 C MET A 145 -10.095 -38.694 -3.496 1.00 70.36 C ANISOU 954 C MET A 145 9811 7923 8998 2877 -340 -242 C ATOM 955 O MET A 145 -11.284 -39.005 -3.662 1.00 68.46 O ANISOU 955 O MET A 145 9720 7479 8811 2663 -86 -200 O ATOM 956 CB MET A 145 -10.390 -36.460 -2.492 1.00 61.19 C ANISOU 956 CB MET A 145 8561 7159 7529 2705 -580 -233 C ATOM 957 CG MET A 145 -10.442 -35.598 -1.252 1.00 62.33 C ANISOU 957 CG MET A 145 8864 7419 7399 2794 -759 -150 C ATOM 958 SD MET A 145 -11.058 -33.971 -1.688 1.00 65.14 S ANISOU 958 SD MET A 145 8972 8014 7764 2431 -760 -290 S ATOM 959 CE MET A 145 -10.966 -33.131 -0.080 1.00 63.66 C ANISOU 959 CE MET A 145 9034 7923 7229 2625 -1011 -221 C ATOM 960 N VAL A 146 -9.144 -39.051 -4.361 1.00 68.62 N ANISOU 960 N VAL A 146 9352 7772 8950 2983 -406 -390 N ATOM 961 CA VAL A 146 -9.488 -39.823 -5.558 1.00 70.98 C ANISOU 961 CA VAL A 146 9602 7911 9455 2864 -192 -527 C ATOM 962 C VAL A 146 -10.105 -41.179 -5.223 1.00 74.01 C ANISOU 962 C VAL A 146 10332 7869 9919 2943 1 -405 C ATOM 963 O VAL A 146 -11.072 -41.574 -5.893 1.00 69.52 O ANISOU 963 O VAL A 146 9806 7113 9495 2708 207 -492 O ATOM 964 CB VAL A 146 -8.278 -39.909 -6.495 1.00 70.41 C ANISOU 964 CB VAL A 146 9222 8008 9521 3008 -275 -703 C ATOM 965 CG1 VAL A 146 -8.382 -41.140 -7.446 1.00 68.66 C ANISOU 965 CG1 VAL A 146 9073 7535 9479 3055 -86 -827 C ATOM 966 CG2 VAL A 146 -8.115 -38.584 -7.264 1.00 63.62 C ANISOU 966 CG2 VAL A 146 8015 7499 8658 2789 -315 -841 C ATOM 967 N PRO A 147 -9.647 -41.929 -4.215 1.00 73.18 N ANISOU 967 N PRO A 147 10486 7575 9744 3262 -52 -206 N ATOM 968 CA PRO A 147 -10.317 -43.211 -3.940 1.00 78.97 C ANISOU 968 CA PRO A 147 11561 7851 10595 3307 190 -63 C ATOM 969 C PRO A 147 -11.780 -43.061 -3.562 1.00 78.38 C ANISOU 969 C PRO A 147 11668 7598 10516 3013 435 57 C ATOM 970 O PRO A 147 -12.602 -43.898 -3.955 1.00 91.04 O ANISOU 970 O PRO A 147 13374 8856 12361 2854 679 37 O ATOM 971 CB PRO A 147 -9.478 -43.807 -2.798 1.00 79.66 C ANISOU 971 CB PRO A 147 11906 7827 10534 3747 56 173 C ATOM 972 CG PRO A 147 -8.134 -43.219 -2.994 1.00 74.98 C ANISOU 972 CG PRO A 147 10997 7598 9894 3949 -268 33 C ATOM 973 CD PRO A 147 -8.461 -41.776 -3.355 1.00 72.85 C ANISOU 973 CD PRO A 147 10441 7687 9550 3623 -336 -110 C ATOM 974 N ILE A 148 -12.148 -42.008 -2.840 1.00 70.10 N ANISOU 974 N ILE A 148 10637 6765 9234 2929 381 158 N ATOM 975 CA ILE A 148 -13.558 -41.821 -2.523 1.00 74.73 C ANISOU 975 CA ILE A 148 11353 7198 9844 2653 644 264 C ATOM 976 C ILE A 148 -14.355 -41.552 -3.792 1.00 71.87 C ANISOU 976 C ILE A 148 10708 6872 9727 2271 735 5 C ATOM 977 O ILE A 148 -15.410 -42.159 -4.016 1.00 78.75 O ANISOU 977 O ILE A 148 11645 7438 10840 2062 982 7 O ATOM 978 CB ILE A 148 -13.741 -40.691 -1.498 1.00 80.68 C ANISOU 978 CB ILE A 148 12190 8194 10272 2676 561 402 C ATOM 979 CG1 ILE A 148 -13.019 -41.030 -0.196 1.00 93.71 C ANISOU 979 CG1 ILE A 148 14180 9793 11634 3096 447 652 C ATOM 980 CG2 ILE A 148 -15.212 -40.450 -1.270 1.00 73.06 C ANISOU 980 CG2 ILE A 148 11306 7089 9365 2387 864 494 C ATOM 981 CD1 ILE A 148 -11.616 -40.486 -0.123 1.00 99.57 C ANISOU 981 CD1 ILE A 148 14744 10867 12222 3350 30 531 C ATOM 982 N ILE A 149 -13.855 -40.652 -4.648 1.00 63.11 N ANISOU 982 N ILE A 149 9280 6125 8575 2187 534 -223 N ATOM 983 CA ILE A 149 -14.589 -40.293 -5.863 1.00 66.16 C ANISOU 983 CA ILE A 149 9427 6588 9122 1871 585 -464 C ATOM 984 C ILE A 149 -14.745 -41.516 -6.760 1.00 68.58 C ANISOU 984 C ILE A 149 9752 6599 9706 1846 690 -628 C ATOM 985 O ILE A 149 -15.785 -41.707 -7.408 1.00 59.52 O ANISOU 985 O ILE A 149 8546 5310 8759 1586 800 -771 O ATOM 986 CB ILE A 149 -13.883 -39.133 -6.601 1.00 55.07 C ANISOU 986 CB ILE A 149 7717 5612 7594 1840 378 -633 C ATOM 987 CG1 ILE A 149 -13.644 -37.950 -5.652 1.00 53.72 C ANISOU 987 CG1 ILE A 149 7534 5692 7186 1876 244 -497 C ATOM 988 CG2 ILE A 149 -14.646 -38.729 -7.893 1.00 53.19 C ANISOU 988 CG2 ILE A 149 7275 5472 7463 1560 419 -867 C ATOM 989 CD1 ILE A 149 -12.932 -36.810 -6.326 1.00 55.57 C ANISOU 989 CD1 ILE A 149 7460 6292 7363 1830 68 -642 C ATOM 990 N ALA A 150 -13.709 -42.362 -6.807 1.00 67.27 N ANISOU 990 N ALA A 150 9660 6328 9570 2130 634 -631 N ATOM 991 CA ALA A 150 -13.757 -43.564 -7.626 1.00 68.41 C ANISOU 991 CA ALA A 150 9851 6166 9975 2147 723 -807 C ATOM 992 C ALA A 150 -14.869 -44.496 -7.175 1.00 75.44 C ANISOU 992 C ALA A 150 10968 6578 11119 2007 962 -698 C ATOM 993 O ALA A 150 -15.494 -45.160 -8.010 1.00 76.07 O ANISOU 993 O ALA A 150 11013 6412 11477 1837 1038 -919 O ATOM 994 CB ALA A 150 -12.406 -44.288 -7.575 1.00 66.30 C ANISOU 994 CB ALA A 150 9640 5857 9693 2524 633 -789 C ATOM 995 N GLN A 151 -15.100 -44.592 -5.855 1.00 77.88 N ANISOU 995 N GLN A 151 11517 6729 11345 2092 1087 -361 N ATOM 996 CA GLN A 151 -16.150 -45.470 -5.346 1.00 83.91 C ANISOU 996 CA GLN A 151 12496 7007 12379 1960 1385 -202 C ATOM 997 C GLN A 151 -17.484 -45.149 -5.996 1.00 84.34 C ANISOU 997 C GLN A 151 12346 7020 12679 1546 1484 -391 C ATOM 998 O GLN A 151 -18.271 -46.052 -6.300 1.00 87.58 O ANISOU 998 O GLN A 151 12783 7015 13480 1369 1659 -472 O ATOM 999 CB GLN A 151 -16.273 -45.337 -3.824 1.00 89.76 C ANISOU 999 CB GLN A 151 13528 7674 12903 2115 1531 210 C ATOM 1000 CG GLN A 151 -17.280 -46.299 -3.199 1.00104.48 C ANISOU 1000 CG GLN A 151 15643 9000 15055 2015 1915 447 C ATOM 1001 CD GLN A 151 -17.650 -45.924 -1.774 1.00110.18 C ANISOU 1001 CD GLN A 151 16640 9711 15512 2122 2113 846 C ATOM 1002 OE1 GLN A 151 -16.886 -45.271 -1.071 1.00110.49 O ANISOU 1002 OE1 GLN A 151 16791 10065 15125 2394 1923 977 O ATOM 1003 NE2 GLN A 151 -18.841 -46.337 -1.344 1.00114.77 N ANISOU 1003 NE2 GLN A 151 17327 9921 16360 1913 2504 1029 N ATOM 1004 N TYR A 152 -17.753 -43.861 -6.228 1.00 71.48 N ANISOU 1004 N TYR A 152 10497 5804 10857 1391 1357 -476 N ATOM 1005 CA TYR A 152 -19.058 -43.474 -6.735 1.00 75.78 C ANISOU 1005 CA TYR A 152 10842 6332 11621 1029 1431 -629 C ATOM 1006 C TYR A 152 -19.147 -43.528 -8.255 1.00 80.75 C ANISOU 1006 C TYR A 152 11234 7054 12393 893 1247 -1044 C ATOM 1007 O TYR A 152 -20.260 -43.589 -8.791 1.00 87.78 O ANISOU 1007 O TYR A 152 11973 7816 13561 614 1283 -1225 O ATOM 1008 CB TYR A 152 -19.439 -42.109 -6.139 1.00 65.08 C ANISOU 1008 CB TYR A 152 9407 5317 10002 947 1418 -489 C ATOM 1009 CG TYR A 152 -19.604 -42.325 -4.656 1.00 72.10 C ANISOU 1009 CG TYR A 152 10590 6008 10797 1077 1660 -100 C ATOM 1010 CD1 TYR A 152 -20.732 -42.978 -4.170 1.00 75.64 C ANISOU 1010 CD1 TYR A 152 11131 6048 11561 908 2000 53 C ATOM 1011 CD2 TYR A 152 -18.593 -42.001 -3.756 1.00 71.44 C ANISOU 1011 CD2 TYR A 152 10707 6106 10331 1394 1556 111 C ATOM 1012 CE1 TYR A 152 -20.890 -43.233 -2.846 1.00 76.76 C ANISOU 1012 CE1 TYR A 152 11583 5990 11593 1055 2274 434 C ATOM 1013 CE2 TYR A 152 -18.743 -42.258 -2.408 1.00 74.72 C ANISOU 1013 CE2 TYR A 152 11451 6337 10603 1564 1770 466 C ATOM 1014 CZ TYR A 152 -19.905 -42.879 -1.965 1.00 84.77 C ANISOU 1014 CZ TYR A 152 12843 7213 12154 1399 2156 642 C ATOM 1015 OH TYR A 152 -20.115 -43.170 -0.641 1.00 92.53 O ANISOU 1015 OH TYR A 152 14187 7989 12980 1582 2437 1028 O ATOM 1016 N GLY A 153 -18.012 -43.578 -8.954 1.00 79.10 N ANISOU 1016 N GLY A 153 10996 7044 12015 1104 1057 -1202 N ATOM 1017 CA GLY A 153 -18.030 -44.057 -10.324 1.00 74.36 C ANISOU 1017 CA GLY A 153 10286 6405 11562 1055 941 -1583 C ATOM 1018 C GLY A 153 -18.570 -45.476 -10.430 1.00 75.61 C ANISOU 1018 C GLY A 153 10572 6015 12143 985 1074 -1686 C ATOM 1019 O GLY A 153 -19.364 -45.780 -11.321 1.00 72.36 O ANISOU 1019 O GLY A 153 10044 5468 11983 779 1014 -2001 O ATOM 1020 N ASP A 154 -18.161 -46.356 -9.509 1.00 71.05 N ANISOU 1020 N ASP A 154 10239 5097 11658 1162 1244 -1427 N ATOM 1021 CA ASP A 154 -18.685 -47.725 -9.477 1.00 80.19 C ANISOU 1021 CA ASP A 154 11541 5661 13267 1090 1418 -1472 C ATOM 1022 C ASP A 154 -20.176 -47.753 -9.167 1.00 85.05 C ANISOU 1022 C ASP A 154 12067 6002 14244 725 1606 -1432 C ATOM 1023 O ASP A 154 -20.911 -48.586 -9.712 1.00 79.73 O ANISOU 1023 O ASP A 154 11339 4932 14023 524 1647 -1673 O ATOM 1024 CB ASP A 154 -17.946 -48.562 -8.434 1.00 78.15 C ANISOU 1024 CB ASP A 154 11595 5100 12998 1386 1587 -1128 C ATOM 1025 CG ASP A 154 -16.478 -48.738 -8.748 1.00 94.89 C ANISOU 1025 CG ASP A 154 13773 7415 14865 1763 1410 -1188 C ATOM 1026 OD1 ASP A 154 -16.118 -48.924 -9.936 1.00 96.73 O ANISOU 1026 OD1 ASP A 154 13887 7739 15126 1795 1254 -1556 O ATOM 1027 OD2 ASP A 154 -15.678 -48.698 -7.792 1.00101.58 O ANISOU 1027 OD2 ASP A 154 14787 8326 15482 2049 1428 -871 O ATOM 1028 N VAL A 155 -20.630 -46.906 -8.236 1.00 74.80 N ANISOU 1028 N VAL A 155 10755 4876 12790 647 1736 -1127 N ATOM 1029 CA VAL A 155 -22.063 -46.797 -7.981 1.00 85.23 C ANISOU 1029 CA VAL A 155 11933 5991 14460 303 1932 -1094 C ATOM 1030 C VAL A 155 -22.772 -46.332 -9.245 1.00 85.41 C ANISOU 1030 C VAL A 155 11620 6204 14626 46 1684 -1534 C ATOM 1031 O VAL A 155 -23.859 -46.814 -9.588 1.00 91.70 O ANISOU 1031 O VAL A 155 12253 6679 15908 -239 1745 -1721 O ATOM 1032 CB VAL A 155 -22.337 -45.838 -6.802 1.00 80.44 C ANISOU 1032 CB VAL A 155 11380 5604 13580 315 2105 -710 C ATOM 1033 CG1 VAL A 155 -23.829 -45.664 -6.612 1.00 75.33 C ANISOU 1033 CG1 VAL A 155 10534 4775 13313 -34 2326 -691 C ATOM 1034 CG2 VAL A 155 -21.681 -46.351 -5.512 1.00 78.41 C ANISOU 1034 CG2 VAL A 155 11503 5145 13142 611 2334 -272 C ATOM 1035 N LEU A 156 -22.155 -45.394 -9.962 1.00 72.54 N ANISOU 1035 N LEU A 156 9883 5091 12587 155 1395 -1705 N ATOM 1036 CA LEU A 156 -22.724 -44.901 -11.210 1.00 72.85 C ANISOU 1036 CA LEU A 156 9658 5356 12668 -18 1133 -2108 C ATOM 1037 C LEU A 156 -22.913 -46.034 -12.213 1.00 78.24 C ANISOU 1037 C LEU A 156 10327 5698 13702 -74 1015 -2511 C ATOM 1038 O LEU A 156 -23.983 -46.176 -12.820 1.00 81.93 O ANISOU 1038 O LEU A 156 10590 6023 14518 -330 916 -2802 O ATOM 1039 CB LEU A 156 -21.820 -43.818 -11.788 1.00 68.32 C ANISOU 1039 CB LEU A 156 9038 5350 11571 170 898 -2170 C ATOM 1040 CG LEU A 156 -22.327 -43.114 -13.034 1.00 71.82 C ANISOU 1040 CG LEU A 156 9257 6097 11935 54 633 -2520 C ATOM 1041 CD1 LEU A 156 -23.710 -42.542 -12.751 1.00 76.98 C ANISOU 1041 CD1 LEU A 156 9698 6732 12821 -237 676 -2492 C ATOM 1042 CD2 LEU A 156 -21.353 -42.016 -13.445 1.00 65.93 C ANISOU 1042 CD2 LEU A 156 8496 5875 10680 252 490 -2484 C ATOM 1043 N VAL A 157 -21.885 -46.865 -12.389 1.00 77.78 N ANISOU 1043 N VAL A 157 10481 5494 13578 176 1007 -2553 N ATOM 1044 CA VAL A 157 -21.964 -47.897 -13.413 1.00 86.64 C ANISOU 1044 CA VAL A 157 11621 6314 14985 164 868 -2980 C ATOM 1045 C VAL A 157 -23.069 -48.894 -13.086 1.00 93.38 C ANISOU 1045 C VAL A 157 12435 6551 16492 -119 1037 -3029 C ATOM 1046 O VAL A 157 -23.822 -49.312 -13.973 1.00 99.79 O ANISOU 1046 O VAL A 157 13095 7174 17647 -311 856 -3456 O ATOM 1047 CB VAL A 157 -20.597 -48.582 -13.586 1.00 87.66 C ANISOU 1047 CB VAL A 157 11989 6398 14918 521 862 -2989 C ATOM 1048 CG1 VAL A 157 -20.688 -49.732 -14.599 1.00 88.66 C ANISOU 1048 CG1 VAL A 157 12174 6159 15354 529 736 -3449 C ATOM 1049 CG2 VAL A 157 -19.545 -47.567 -14.015 1.00 75.72 C ANISOU 1049 CG2 VAL A 157 10447 5490 12834 769 708 -2971 C ATOM 1050 N ARG A 158 -23.207 -49.271 -11.810 1.00 91.46 N ANISOU 1050 N ARG A 158 12326 5983 16443 -147 1387 -2595 N ATOM 1051 CA ARG A 158 -24.269 -50.201 -11.429 1.00 91.48 C ANISOU 1051 CA ARG A 158 12278 5363 17119 -433 1626 -2583 C ATOM 1052 C ARG A 158 -25.643 -49.618 -11.718 1.00 92.91 C ANISOU 1052 C ARG A 158 12089 5636 17575 -798 1551 -2751 C ATOM 1053 O ARG A 158 -26.538 -50.320 -12.193 1.00100.37 O ANISOU 1053 O ARG A 158 12844 6390 18903 -1029 1465 -2962 O ATOM 1054 CB ARG A 158 -24.155 -50.564 -9.953 1.00 92.84 C ANISOU 1054 CB ARG A 158 12693 5228 17353 -356 2061 -2015 C ATOM 1055 CG ARG A 158 -22.995 -51.474 -9.663 1.00104.44 C ANISOU 1055 CG ARG A 158 14517 6458 18707 -15 2139 -1864 C ATOM 1056 CD ARG A 158 -23.225 -52.268 -8.404 1.00116.88 C ANISOU 1056 CD ARG A 158 16319 7612 20476 -3 2543 -1370 C ATOM 1057 NE ARG A 158 -23.269 -51.407 -7.233 1.00121.88 N ANISOU 1057 NE ARG A 158 17063 8403 20844 73 2801 -913 N ATOM 1058 CZ ARG A 158 -22.189 -50.955 -6.605 1.00125.24 C ANISOU 1058 CZ ARG A 158 17723 9169 20692 439 2753 -626 C ATOM 1059 NH1 ARG A 158 -20.976 -51.279 -7.042 1.00122.53 N ANISOU 1059 NH1 ARG A 158 17515 8940 20102 755 2523 -752 N ATOM 1060 NH2 ARG A 158 -22.324 -50.181 -5.539 1.00128.38 N ANISOU 1060 NH2 ARG A 158 18211 9791 20775 501 2927 -232 N ATOM 1061 N ASN A 159 -25.830 -48.333 -11.444 1.00 85.12 N ANISOU 1061 N ASN A 159 10974 5112 16257 -817 1528 -2595 N ATOM 1062 CA ASN A 159 -27.116 -47.717 -11.734 1.00 97.90 C ANISOU 1062 CA ASN A 159 12226 6819 18153 -1132 1447 -2768 C ATOM 1063 C ASN A 159 -27.296 -47.451 -13.219 1.00100.15 C ANISOU 1063 C ASN A 159 12312 7366 18374 -1164 970 -3328 C ATOM 1064 O ASN A 159 -28.421 -47.524 -13.726 1.00104.76 O ANISOU 1064 O ASN A 159 12593 7965 19247 -1395 810 -3539 O ATOM 1065 CB ASN A 159 -27.260 -46.418 -10.954 1.00 83.80 C ANISOU 1065 CB ASN A 159 10386 5459 15996 -1110 1572 -2409 C ATOM 1066 CG ASN A 159 -27.132 -46.618 -9.456 1.00 89.33 C ANISOU 1066 CG ASN A 159 11320 5932 16689 -1041 2034 -1860 C ATOM 1067 OD1 ASN A 159 -27.512 -47.655 -8.924 1.00 93.01 O ANISOU 1067 OD1 ASN A 159 11866 5846 17628 -1147 2345 -1720 O ATOM 1068 ND2 ASN A 159 -26.583 -45.616 -8.765 1.00 91.75 N ANISOU 1068 ND2 ASN A 159 11758 6654 16449 -846 2082 -1545 N ATOM 1069 N LEU A 160 -26.211 -47.140 -13.928 1.00 93.94 N ANISOU 1069 N LEU A 160 11691 6962 17041 -874 723 -3464 N ATOM 1070 CA LEU A 160 -26.303 -47.017 -15.378 1.00 94.33 C ANISOU 1070 CA LEU A 160 11633 7232 16978 -845 296 -3993 C ATOM 1071 C LEU A 160 -26.643 -48.356 -16.031 1.00102.59 C ANISOU 1071 C LEU A 160 12686 7944 18351 -911 170 -4272 C ATOM 1072 O LEU A 160 -27.419 -48.410 -16.993 1.00101.01 O ANISOU 1072 O LEU A 160 12287 7862 18228 -1018 -143 -4611 O ATOM 1073 CB LEU A 160 -24.998 -46.470 -15.945 1.00 89.57 C ANISOU 1073 CB LEU A 160 11229 7109 15694 -491 146 -3999 C ATOM 1074 CG LEU A 160 -25.147 -45.149 -16.697 1.00 92.29 C ANISOU 1074 CG LEU A 160 11426 8035 15606 -450 -119 -4117 C ATOM 1075 CD1 LEU A 160 -23.862 -44.760 -17.411 1.00 85.67 C ANISOU 1075 CD1 LEU A 160 10775 7602 14172 -110 -234 -4163 C ATOM 1076 CD2 LEU A 160 -26.300 -45.253 -17.676 1.00 95.57 C ANISOU 1076 CD2 LEU A 160 11613 8386 16314 -641 -441 -4594 C ATOM 1077 N ARG A 161 -26.066 -49.446 -15.529 1.00104.56 N ANISOU 1077 N ARG A 161 13172 7789 18765 -823 396 -4118 N ATOM 1078 CA ARG A 161 -26.307 -50.744 -16.143 1.00113.10 C ANISOU 1078 CA ARG A 161 14289 8549 20134 -871 280 -4376 C ATOM 1079 C ARG A 161 -27.774 -51.131 -16.052 1.00124.93 C ANISOU 1079 C ARG A 161 15471 9816 22181 -1225 289 -4426 C ATOM 1080 O ARG A 161 -28.349 -51.650 -17.016 1.00130.82 O ANISOU 1080 O ARG A 161 16086 10527 23094 -1308 -5 -4811 O ATOM 1081 CB ARG A 161 -25.440 -51.820 -15.501 1.00114.11 C ANISOU 1081 CB ARG A 161 14736 8264 20356 -705 552 -4150 C ATOM 1082 CG ARG A 161 -25.848 -53.216 -15.938 1.00122.51 C ANISOU 1082 CG ARG A 161 15823 8907 21818 -809 492 -4370 C ATOM 1083 CD ARG A 161 -24.703 -54.200 -15.880 1.00129.67 C ANISOU 1083 CD ARG A 161 17092 9546 22631 -526 592 -4325 C ATOM 1084 NE ARG A 161 -23.561 -53.731 -16.657 1.00129.07 N ANISOU 1084 NE ARG A 161 17179 9857 22005 -183 390 -4527 N ATOM 1085 CZ ARG A 161 -22.449 -53.237 -16.127 1.00121.41 C ANISOU 1085 CZ ARG A 161 16382 9056 20693 104 539 -4270 C ATOM 1086 NH1 ARG A 161 -22.318 -53.143 -14.809 1.00122.16 N ANISOU 1086 NH1 ARG A 161 16551 8966 20900 105 868 -3797 N ATOM 1087 NH2 ARG A 161 -21.466 -52.841 -16.919 1.00116.03 N ANISOU 1087 NH2 ARG A 161 15798 8741 19546 409 369 -4475 N ATOM 1088 N ARG A 162 -28.392 -50.901 -14.894 1.00124.33 N ANISOU 1088 N ARG A 162 15269 9582 22391 -1415 637 -4036 N ATOM 1089 CA ARG A 162 -29.787 -51.291 -14.713 1.00129.68 C ANISOU 1089 CA ARG A 162 15611 10031 23629 -1735 711 -4046 C ATOM 1090 C ARG A 162 -30.700 -50.550 -15.681 1.00129.79 C ANISOU 1090 C ARG A 162 15271 10410 23634 -1848 316 -4409 C ATOM 1091 O ARG A 162 -31.722 -51.098 -16.118 1.00129.13 O ANISOU 1091 O ARG A 162 14915 10168 23983 -2039 177 -4642 O ATOM 1092 CB ARG A 162 -30.203 -51.044 -13.270 1.00126.96 C ANISOU 1092 CB ARG A 162 15224 9519 23495 -1862 1204 -3523 C ATOM 1093 CG ARG A 162 -31.590 -51.530 -12.931 1.00134.21 C ANISOU 1093 CG ARG A 162 15801 10168 25027 -2164 1382 -3473 C ATOM 1094 CD ARG A 162 -31.898 -51.276 -11.474 1.00134.20 C ANISOU 1094 CD ARG A 162 15820 10030 25140 -2228 1923 -2921 C ATOM 1095 NE ARG A 162 -31.585 -49.898 -11.120 1.00132.21 N ANISOU 1095 NE ARG A 162 15603 10185 24444 -2125 1945 -2745 N ATOM 1096 CZ ARG A 162 -30.518 -49.526 -10.420 1.00131.96 C ANISOU 1096 CZ ARG A 162 15935 10212 23992 -1898 2136 -2427 C ATOM 1097 NH1 ARG A 162 -30.318 -48.239 -10.168 1.00126.55 N ANISOU 1097 NH1 ARG A 162 15249 9891 22945 -1827 2127 -2313 N ATOM 1098 NH2 ARG A 162 -29.654 -50.437 -9.982 1.00130.89 N ANISOU 1098 NH2 ARG A 162 16164 9767 23801 -1724 2320 -2230 N ATOM 1099 N GLU A 163 -30.324 -49.303 -16.053 1.00132.03 N ANISOU 1099 N GLU A 163 15558 11177 23431 -1710 122 -4461 N ATOM 1100 CA GLU A 163 -31.056 -48.612 -17.093 1.00139.88 C ANISOU 1100 CA GLU A 163 16283 12545 24321 -1741 -296 -4808 C ATOM 1101 C GLU A 163 -30.583 -48.989 -18.487 1.00146.57 C ANISOU 1101 C GLU A 163 17280 13546 24866 -1543 -724 -5258 C ATOM 1102 O GLU A 163 -31.339 -48.821 -19.454 1.00148.93 O ANISOU 1102 O GLU A 163 17373 14035 25180 -1568 -1094 -5592 O ATOM 1103 CB GLU A 163 -30.935 -47.112 -16.906 1.00139.47 C ANISOU 1103 CB GLU A 163 16177 12943 23872 -1672 -317 -4660 C ATOM 1104 CG GLU A 163 -31.576 -46.592 -15.646 1.00145.17 C ANISOU 1104 CG GLU A 163 16504 13779 24876 -1881 -308 -4594 C ATOM 1105 CD GLU A 163 -32.921 -45.950 -15.911 1.00147.45 C ANISOU 1105 CD GLU A 163 16773 13985 25266 -1982 158 -4116 C ATOM 1106 OE1 GLU A 163 -33.206 -45.623 -17.084 1.00146.93 O ANISOU 1106 OE1 GLU A 163 17019 13778 25030 -1879 449 -3838 O ATOM 1107 OE2 GLU A 163 -33.692 -45.775 -14.947 1.00148.77 O ANISOU 1107 OE2 GLU A 163 16627 14230 25669 -2136 237 -4016 O ATOM 1108 N ALA A 164 -29.356 -49.457 -18.601 1.00148.11 N ANISOU 1108 N ALA A 164 17839 13682 24756 -1312 -676 -5265 N ATOM 1109 CA ALA A 164 -28.890 -50.017 -19.859 1.00153.12 C ANISOU 1109 CA ALA A 164 18651 14394 25135 -1112 -1008 -5671 C ATOM 1110 C ALA A 164 -29.433 -51.420 -20.091 1.00156.50 C ANISOU 1110 C ALA A 164 19037 14356 26070 -1257 -1050 -5884 C ATOM 1111 O ALA A 164 -29.555 -51.846 -21.245 1.00158.56 O ANISOU 1111 O ALA A 164 19327 14677 26241 -1171 -1399 -6296 O ATOM 1112 CB ALA A 164 -27.361 -50.032 -19.898 1.00153.90 C ANISOU 1112 CB ALA A 164 19133 14591 24750 -790 -905 -5596 C ATOM 1113 N GLU A 165 -29.770 -52.138 -19.022 1.00155.40 N ANISOU 1113 N GLU A 165 18839 13751 26453 -1466 -691 -5604 N ATOM 1114 CA GLU A 165 -30.333 -53.473 -19.146 1.00153.42 C ANISOU 1114 CA GLU A 165 18527 13020 26745 -1631 -691 -5775 C ATOM 1115 C GLU A 165 -31.833 -53.453 -19.425 1.00157.08 C ANISOU 1115 C GLU A 165 18545 13451 27689 -1905 -871 -5973 C ATOM 1116 O GLU A 165 -32.390 -54.493 -19.801 1.00173.67 O ANISOU 1116 O GLU A 165 20546 15207 30235 -2035 -978 -6230 O ATOM 1117 CB GLU A 165 -30.014 -54.296 -17.887 1.00150.93 C ANISOU 1117 CB GLU A 165 18371 12207 26768 -1704 -201 -5359 C ATOM 1118 CG GLU A 165 -28.569 -54.837 -17.857 1.00150.15 C ANISOU 1118 CG GLU A 165 18728 11996 26326 -1401 -101 -5290 C ATOM 1119 CD GLU A 165 -28.204 -55.559 -16.561 1.00151.25 C ANISOU 1119 CD GLU A 165 19062 11676 26730 -1415 377 -4824 C ATOM 1120 OE1 GLU A 165 -28.775 -55.212 -15.502 1.00149.94 O ANISOU 1120 OE1 GLU A 165 18746 11428 26798 -1591 699 -4437 O ATOM 1121 OE2 GLU A 165 -27.337 -56.467 -16.600 1.00151.78 O ANISOU 1121 OE2 GLU A 165 19451 11474 26746 -1221 440 -4829 O ATOM 1122 N THR A 166 -32.495 -52.305 -19.273 1.00143.98 N ANISOU 1122 N THR A 166 16609 12133 25963 -1981 -916 -5876 N ATOM 1123 CA THR A 166 -33.870 -52.110 -19.730 1.00140.94 C ANISOU 1123 CA THR A 166 15791 11815 25945 -2165 -1167 -6115 C ATOM 1124 C THR A 166 -33.849 -51.081 -20.855 1.00137.32 C ANISOU 1124 C THR A 166 15317 11914 24943 -1960 -1632 -6403 C ATOM 1125 O THR A 166 -33.607 -49.893 -20.611 1.00119.08 O ANISOU 1125 O THR A 166 13019 9981 22243 -1869 -1587 -6196 O ATOM 1126 CB THR A 166 -34.789 -51.660 -18.594 1.00135.54 C ANISOU 1126 CB THR A 166 14778 11039 25681 -2406 -805 -5746 C ATOM 1127 OG1 THR A 166 -34.260 -50.485 -17.964 1.00116.21 O ANISOU 1127 OG1 THR A 166 12440 8919 22794 -2303 -614 -5403 O ATOM 1128 CG2 THR A 166 -34.956 -52.778 -17.568 1.00137.61 C ANISOU 1128 CG2 THR A 166 15047 10726 26511 -2600 -340 -5469 C ATOM 1129 N GLY A 167 -34.116 -51.539 -22.080 1.00151.82 N ANISOU 1129 N GLY A 167 17141 13792 26751 -1876 -2072 -6874 N ATOM 1130 CA GLY A 167 -33.996 -50.720 -23.276 1.00157.06 C ANISOU 1130 CA GLY A 167 17876 14962 26837 -1621 -2519 -7159 C ATOM 1131 C GLY A 167 -34.779 -49.424 -23.240 1.00154.82 C ANISOU 1131 C GLY A 167 17303 15059 26465 -1643 -2631 -7062 C ATOM 1132 O GLY A 167 -35.636 -49.169 -24.094 1.00162.00 O ANISOU 1132 O GLY A 167 17998 16144 27411 -1608 -3026 -7365 O ATOM 1133 N LYS A 168 -34.472 -48.588 -22.254 1.00144.52 N ANISOU 1133 N LYS A 168 16004 13877 25030 -1682 -2290 -6641 N ATOM 1134 CA LYS A 168 -35.198 -47.367 -21.993 1.00141.80 C ANISOU 1134 CA LYS A 168 15388 13836 24653 -1727 -2307 -6483 C ATOM 1135 C LYS A 168 -34.257 -46.176 -22.124 1.00130.68 C ANISOU 1135 C LYS A 168 14237 12890 22527 -1485 -2322 -6322 C ATOM 1136 O LYS A 168 -33.153 -46.206 -21.559 1.00125.71 O ANISOU 1136 O LYS A 168 13891 12219 21654 -1418 -2042 -6092 O ATOM 1137 CB LYS A 168 -35.810 -47.408 -20.586 1.00145.54 C ANISOU 1137 CB LYS A 168 15607 14013 25679 -2011 -1839 -6105 C ATOM 1138 CG LYS A 168 -36.825 -46.318 -20.322 1.00150.21 C ANISOU 1138 CG LYS A 168 15849 14842 26380 -2085 -1853 -5987 C ATOM 1139 CD LYS A 168 -37.519 -46.513 -18.983 1.00153.14 C ANISOU 1139 CD LYS A 168 15968 14883 27334 -2353 -1362 -5636 C ATOM 1140 CE LYS A 168 -38.653 -45.513 -18.804 1.00152.50 C ANISOU 1140 CE LYS A 168 15511 15014 27417 -2414 -1391 -5568 C ATOM 1141 NZ LYS A 168 -39.704 -45.665 -19.853 1.00159.62 N ANISOU 1141 NZ LYS A 168 16109 15964 28576 -2408 -1853 -5991 N ATOM 1142 N PRO A 169 -34.636 -45.132 -22.872 1.00122.60 N ANISOU 1142 N PRO A 169 13131 12297 21154 -1334 -2642 -6436 N ATOM 1143 CA PRO A 169 -33.778 -43.943 -22.989 1.00113.30 C ANISOU 1143 CA PRO A 169 12182 11556 19311 -1111 -2636 -6262 C ATOM 1144 C PRO A 169 -33.412 -43.363 -21.633 1.00105.84 C ANISOU 1144 C PRO A 169 11225 10568 18422 -1242 -2195 -5828 C ATOM 1145 O PRO A 169 -34.122 -43.539 -20.639 1.00108.97 O ANISOU 1145 O PRO A 169 11371 10694 19340 -1494 -1920 -5628 O ATOM 1146 CB PRO A 169 -34.634 -42.963 -23.799 1.00109.37 C ANISOU 1146 CB PRO A 169 11502 11429 18623 -996 -3002 -6403 C ATOM 1147 CG PRO A 169 -35.495 -43.825 -24.607 1.00121.09 C ANISOU 1147 CG PRO A 169 12827 12739 20442 -1025 -3332 -6789 C ATOM 1148 CD PRO A 169 -35.786 -45.066 -23.790 1.00127.71 C ANISOU 1148 CD PRO A 169 13515 13044 21964 -1316 -3061 -6765 C ATOM 1149 N VAL A 170 -32.284 -42.658 -21.606 1.00 99.62 N ANISOU 1149 N VAL A 170 10716 10052 17082 -1050 -2117 -5680 N ATOM 1150 CA VAL A 170 -31.605 -42.303 -20.372 1.00 85.02 C ANISOU 1150 CA VAL A 170 8955 8123 15226 -1124 -1707 -5311 C ATOM 1151 C VAL A 170 -31.397 -40.788 -20.368 1.00 94.71 C ANISOU 1151 C VAL A 170 10184 9799 16002 -1008 -1750 -5156 C ATOM 1152 O VAL A 170 -30.639 -40.254 -21.196 1.00 89.43 O ANISOU 1152 O VAL A 170 9738 9478 14766 -746 -1935 -5250 O ATOM 1153 CB VAL A 170 -30.270 -43.052 -20.233 1.00 88.87 C ANISOU 1153 CB VAL A 170 9797 8440 15527 -990 -1534 -5287 C ATOM 1154 CG1 VAL A 170 -29.530 -42.646 -18.973 1.00 79.50 C ANISOU 1154 CG1 VAL A 170 8722 7175 14311 -1024 -1137 -4916 C ATOM 1155 CG2 VAL A 170 -30.499 -44.587 -20.265 1.00 89.10 C ANISOU 1155 CG2 VAL A 170 9838 8001 16015 -1101 -1497 -5439 C ATOM 1156 N THR A 171 -32.077 -40.091 -19.451 1.00 86.65 N ANISOU 1156 N THR A 171 8922 8772 15230 -1190 -1556 -4906 N ATOM 1157 CA THR A 171 -31.863 -38.656 -19.283 1.00 91.32 C ANISOU 1157 CA THR A 171 9513 9746 15440 -1105 -1554 -4727 C ATOM 1158 C THR A 171 -30.585 -38.441 -18.484 1.00 84.04 C ANISOU 1158 C THR A 171 8871 8856 14206 -1016 -1223 -4400 C ATOM 1159 O THR A 171 -30.490 -38.863 -17.326 1.00 84.02 O ANISOU 1159 O THR A 171 8888 8573 14464 -1145 -852 -4106 O ATOM 1160 CB THR A 171 -33.039 -37.983 -18.576 1.00 98.83 C ANISOU 1160 CB THR A 171 10122 10693 16738 -1295 -1437 -4541 C ATOM 1161 OG1 THR A 171 -32.964 -38.253 -17.172 1.00114.77 O ANISOU 1161 OG1 THR A 171 12115 12396 19096 -1495 -980 -4234 O ATOM 1162 CG2 THR A 171 -34.367 -38.474 -19.122 1.00 80.82 C ANISOU 1162 CG2 THR A 171 7548 8297 14862 -1379 -1654 -4757 C ATOM 1163 N LEU A 172 -29.611 -37.774 -19.103 1.00 81.85 N ANISOU 1163 N LEU A 172 8832 8963 13305 -743 -1319 -4348 N ATOM 1164 CA LEU A 172 -28.267 -37.702 -18.533 1.00 76.13 C ANISOU 1164 CA LEU A 172 8383 8312 12230 -590 -1033 -4014 C ATOM 1165 C LEU A 172 -28.239 -36.960 -17.215 1.00 80.28 C ANISOU 1165 C LEU A 172 8869 8873 12761 -674 -710 -3558 C ATOM 1166 O LEU A 172 -27.536 -37.374 -16.284 1.00 75.82 O ANISOU 1166 O LEU A 172 8457 8144 12206 -659 -426 -3295 O ATOM 1167 CB LEU A 172 -27.317 -37.016 -19.502 1.00 68.95 C ANISOU 1167 CB LEU A 172 7675 7815 10707 -300 -1178 -4045 C ATOM 1168 CG LEU A 172 -27.171 -37.791 -20.793 1.00 82.10 C ANISOU 1168 CG LEU A 172 9464 9464 12268 -150 -1464 -4488 C ATOM 1169 CD1 LEU A 172 -26.079 -37.149 -21.606 1.00 86.26 C ANISOU 1169 CD1 LEU A 172 10224 10379 12171 160 -1484 -4432 C ATOM 1170 CD2 LEU A 172 -26.870 -39.253 -20.474 1.00 82.95 C ANISOU 1170 CD2 LEU A 172 9661 9135 12720 -213 -1348 -4615 C ATOM 1171 N LYS A 173 -28.943 -35.823 -17.135 1.00 77.72 N ANISOU 1171 N LYS A 173 8368 8777 12385 -722 -765 -3463 N ATOM 1172 CA LYS A 173 -28.799 -34.971 -15.960 1.00 73.52 C ANISOU 1172 CA LYS A 173 7846 8329 11759 -748 -481 -3053 C ATOM 1173 C LYS A 173 -29.170 -35.727 -14.700 1.00 71.80 C ANISOU 1173 C LYS A 173 7599 7727 11956 -924 -153 -2864 C ATOM 1174 O LYS A 173 -28.592 -35.487 -13.638 1.00 69.18 O ANISOU 1174 O LYS A 173 7420 7389 11476 -875 116 -2527 O ATOM 1175 CB LYS A 173 -29.656 -33.706 -16.094 1.00 82.29 C ANISOU 1175 CB LYS A 173 8753 9691 12821 -777 -593 -3018 C ATOM 1176 CG LYS A 173 -31.179 -33.943 -16.053 1.00 96.81 C ANISOU 1176 CG LYS A 173 10254 11337 15193 -992 -661 -3195 C ATOM 1177 CD LYS A 173 -31.969 -32.628 -15.834 1.00101.50 C ANISOU 1177 CD LYS A 173 10649 12154 15760 -1004 -676 -3064 C ATOM 1178 CE LYS A 173 -33.486 -32.852 -15.853 1.00106.56 C ANISOU 1178 CE LYS A 173 10896 12618 16974 -1204 -757 -3260 C ATOM 1179 NZ LYS A 173 -34.264 -31.622 -15.498 1.00109.41 N ANISOU 1179 NZ LYS A 173 11056 13164 17352 -1201 -719 -3108 N ATOM 1180 N ASP A 174 -30.100 -36.677 -14.805 1.00 72.36 N ANISOU 1180 N ASP A 174 7486 7457 12549 -1116 -170 -3080 N ATOM 1181 CA ASP A 174 -30.500 -37.417 -13.618 1.00 77.48 C ANISOU 1181 CA ASP A 174 8112 7705 13620 -1283 201 -2865 C ATOM 1182 C ASP A 174 -29.381 -38.334 -13.152 1.00 76.43 C ANISOU 1182 C ASP A 174 8300 7365 13374 -1168 388 -2716 C ATOM 1183 O ASP A 174 -29.009 -38.332 -11.970 1.00 72.64 O ANISOU 1183 O ASP A 174 7987 6792 12819 -1127 710 -2352 O ATOM 1184 CB ASP A 174 -31.773 -38.209 -13.908 1.00 87.38 C ANISOU 1184 CB ASP A 174 9049 8613 15538 -1540 145 -3146 C ATOM 1185 CG ASP A 174 -32.998 -37.321 -13.997 1.00 89.26 C ANISOU 1185 CG ASP A 174 8925 9002 15988 -1664 53 -3206 C ATOM 1186 OD1 ASP A 174 -32.999 -36.260 -13.342 1.00 83.63 O ANISOU 1186 OD1 ASP A 174 8231 8524 15019 -1600 215 -2911 O ATOM 1187 OD2 ASP A 174 -33.959 -37.681 -14.713 1.00 86.32 O ANISOU 1187 OD2 ASP A 174 8241 8505 16052 -1816 -197 -3564 O ATOM 1188 N VAL A 175 -28.823 -39.119 -14.076 1.00 70.98 N ANISOU 1188 N VAL A 175 7713 6607 12648 -1083 174 -3004 N ATOM 1189 CA VAL A 175 -27.822 -40.098 -13.689 1.00 78.87 C ANISOU 1189 CA VAL A 175 8993 7368 13606 -963 340 -2892 C ATOM 1190 C VAL A 175 -26.533 -39.406 -13.245 1.00 75.41 C ANISOU 1190 C VAL A 175 8793 7245 12615 -713 412 -2599 C ATOM 1191 O VAL A 175 -25.884 -39.838 -12.286 1.00 73.50 O ANISOU 1191 O VAL A 175 8756 6839 12331 -622 652 -2318 O ATOM 1192 CB VAL A 175 -27.593 -41.099 -14.837 1.00 87.89 C ANISOU 1192 CB VAL A 175 10179 8352 14863 -920 88 -3312 C ATOM 1193 CG1 VAL A 175 -26.974 -40.427 -16.060 1.00 82.99 C ANISOU 1193 CG1 VAL A 175 9613 8175 13744 -708 -240 -3541 C ATOM 1194 CG2 VAL A 175 -26.746 -42.238 -14.358 1.00103.41 C ANISOU 1194 CG2 VAL A 175 12404 9980 16907 -818 290 -3199 C ATOM 1195 N PHE A 176 -26.152 -38.311 -13.911 1.00 77.66 N ANISOU 1195 N PHE A 176 9048 7972 12487 -593 203 -2652 N ATOM 1196 CA PHE A 176 -24.978 -37.580 -13.456 1.00 68.27 C ANISOU 1196 CA PHE A 176 8025 7061 10855 -393 272 -2384 C ATOM 1197 C PHE A 176 -25.301 -36.770 -12.220 1.00 55.68 C ANISOU 1197 C PHE A 176 6415 5517 9226 -452 476 -2048 C ATOM 1198 O PHE A 176 -24.427 -36.571 -11.362 1.00 60.36 O ANISOU 1198 O PHE A 176 7181 6164 9590 -312 602 -1786 O ATOM 1199 CB PHE A 176 -24.434 -36.687 -14.564 1.00 62.76 C ANISOU 1199 CB PHE A 176 7304 6775 9765 -251 35 -2523 C ATOM 1200 CG PHE A 176 -23.785 -37.453 -15.677 1.00 58.57 C ANISOU 1200 CG PHE A 176 6873 6237 9143 -104 -115 -2805 C ATOM 1201 CD1 PHE A 176 -22.702 -38.304 -15.423 1.00 55.33 C ANISOU 1201 CD1 PHE A 176 6646 5681 8696 53 -5 -2746 C ATOM 1202 CD2 PHE A 176 -24.246 -37.337 -16.975 1.00 59.45 C ANISOU 1202 CD2 PHE A 176 6913 6488 9186 -88 -373 -3137 C ATOM 1203 CE1 PHE A 176 -22.115 -39.015 -16.454 1.00 66.65 C ANISOU 1203 CE1 PHE A 176 8178 7101 10045 210 -120 -3019 C ATOM 1204 CE2 PHE A 176 -23.649 -38.047 -18.005 1.00 66.52 C ANISOU 1204 CE2 PHE A 176 7939 7382 9954 81 -500 -3414 C ATOM 1205 CZ PHE A 176 -22.588 -38.891 -17.746 1.00 62.68 C ANISOU 1205 CZ PHE A 176 7624 6740 9451 225 -358 -3359 C ATOM 1206 N GLY A 177 -26.547 -36.301 -12.104 1.00 61.28 N ANISOU 1206 N GLY A 177 6915 6209 10158 -637 499 -2069 N ATOM 1207 CA GLY A 177 -26.946 -35.621 -10.882 1.00 58.12 C ANISOU 1207 CA GLY A 177 6519 5819 9746 -681 735 -1763 C ATOM 1208 C GLY A 177 -26.719 -36.475 -9.652 1.00 66.68 C ANISOU 1208 C GLY A 177 7809 6580 10945 -653 1050 -1499 C ATOM 1209 O GLY A 177 -26.061 -36.052 -8.701 1.00 64.32 O ANISOU 1209 O GLY A 177 7706 6374 10358 -507 1171 -1229 O ATOM 1210 N ALA A 178 -27.211 -37.714 -9.683 1.00 71.37 N ANISOU 1210 N ALA A 178 8382 6778 11958 -774 1168 -1582 N ATOM 1211 CA ALA A 178 -26.972 -38.622 -8.568 1.00 72.05 C ANISOU 1211 CA ALA A 178 8703 6515 12156 -723 1491 -1305 C ATOM 1212 C ALA A 178 -25.474 -38.791 -8.312 1.00 70.59 C ANISOU 1212 C ALA A 178 8815 6437 11570 -442 1428 -1179 C ATOM 1213 O ALA A 178 -25.009 -38.755 -7.161 1.00 59.93 O ANISOU 1213 O ALA A 178 7702 5051 10018 -290 1617 -864 O ATOM 1214 CB ALA A 178 -27.636 -39.971 -8.852 1.00 69.98 C ANISOU 1214 CB ALA A 178 8361 5779 12450 -902 1598 -1457 C ATOM 1215 N TYR A 179 -24.697 -38.932 -9.387 1.00 64.18 N ANISOU 1215 N TYR A 179 7987 5777 10623 -348 1152 -1429 N ATOM 1216 CA TYR A 179 -23.267 -39.135 -9.244 1.00 65.41 C ANISOU 1216 CA TYR A 179 8360 6030 10464 -82 1087 -1340 C ATOM 1217 C TYR A 179 -22.611 -37.933 -8.579 1.00 58.86 C ANISOU 1217 C TYR A 179 7589 5552 9223 60 1049 -1127 C ATOM 1218 O TYR A 179 -21.801 -38.081 -7.654 1.00 60.22 O ANISOU 1218 O TYR A 179 7975 5699 9206 257 1121 -897 O ATOM 1219 CB TYR A 179 -22.628 -39.386 -10.611 1.00 64.05 C ANISOU 1219 CB TYR A 179 8127 5988 10222 -5 831 -1661 C ATOM 1220 CG TYR A 179 -21.123 -39.326 -10.533 1.00 59.75 C ANISOU 1220 CG TYR A 179 7727 5627 9349 273 759 -1572 C ATOM 1221 CD1 TYR A 179 -20.384 -40.411 -10.046 1.00 61.34 C ANISOU 1221 CD1 TYR A 179 8135 5561 9610 449 856 -1469 C ATOM 1222 CD2 TYR A 179 -20.434 -38.178 -10.911 1.00 55.76 C ANISOU 1222 CD2 TYR A 179 7135 5544 8508 365 604 -1578 C ATOM 1223 CE1 TYR A 179 -18.996 -40.344 -9.959 1.00 65.08 C ANISOU 1223 CE1 TYR A 179 8695 6213 9820 719 772 -1397 C ATOM 1224 CE2 TYR A 179 -19.056 -38.112 -10.831 1.00 54.13 C ANISOU 1224 CE2 TYR A 179 7000 5495 8073 603 546 -1505 C ATOM 1225 CZ TYR A 179 -18.342 -39.191 -10.357 1.00 59.63 C ANISOU 1225 CZ TYR A 179 7871 5950 8838 783 617 -1425 C ATOM 1226 OH TYR A 179 -16.976 -39.115 -10.265 1.00 64.74 O ANISOU 1226 OH TYR A 179 8543 6761 9294 1032 540 -1363 O ATOM 1227 N SER A 180 -22.925 -36.732 -9.071 1.00 55.19 N ANISOU 1227 N SER A 180 6940 5411 8620 -22 908 -1217 N ATOM 1228 CA SER A 180 -22.329 -35.518 -8.513 1.00 57.47 C ANISOU 1228 CA SER A 180 7262 6011 8563 89 851 -1055 C ATOM 1229 C SER A 180 -22.712 -35.349 -7.047 1.00 59.18 C ANISOU 1229 C SER A 180 7637 6111 8740 111 1074 -769 C ATOM 1230 O SER A 180 -21.875 -34.991 -6.213 1.00 57.18 O ANISOU 1230 O SER A 180 7550 5963 8211 298 1052 -598 O ATOM 1231 CB SER A 180 -22.775 -34.316 -9.339 1.00 46.10 C ANISOU 1231 CB SER A 180 5603 4871 7041 -19 694 -1196 C ATOM 1232 OG SER A 180 -22.194 -33.129 -8.890 1.00 54.41 O ANISOU 1232 OG SER A 180 6673 6191 7811 68 633 -1067 O ATOM 1233 N MET A 181 -23.975 -35.633 -6.726 1.00 64.57 N ANISOU 1233 N MET A 181 8264 6565 9703 -64 1291 -724 N ATOM 1234 CA MET A 181 -24.458 -35.661 -5.342 1.00 63.61 C ANISOU 1234 CA MET A 181 8324 6279 9567 -30 1588 -435 C ATOM 1235 C MET A 181 -23.645 -36.627 -4.491 1.00 59.65 C ANISOU 1235 C MET A 181 8145 5559 8961 188 1708 -224 C ATOM 1236 O MET A 181 -23.166 -36.267 -3.407 1.00 61.05 O ANISOU 1236 O MET A 181 8563 5811 8825 389 1759 -1 O ATOM 1237 CB MET A 181 -25.941 -36.046 -5.341 1.00 68.58 C ANISOU 1237 CB MET A 181 8784 6643 10630 -275 1839 -447 C ATOM 1238 CG MET A 181 -26.712 -35.992 -4.009 1.00 87.87 C ANISOU 1238 CG MET A 181 11365 8911 13112 -271 2231 -145 C ATOM 1239 SD MET A 181 -26.394 -34.623 -2.893 1.00 99.08 S ANISOU 1239 SD MET A 181 12984 10642 14022 -68 2249 61 S ATOM 1240 CE MET A 181 -26.722 -33.168 -3.907 1.00107.35 C ANISOU 1240 CE MET A 181 13685 12072 15031 -203 1944 -203 C ATOM 1241 N ASP A 182 -23.469 -37.867 -4.978 1.00 58.14 N ANISOU 1241 N ASP A 182 7980 5090 9021 175 1731 -305 N ATOM 1242 CA ASP A 182 -22.727 -38.864 -4.222 1.00 60.47 C ANISOU 1242 CA ASP A 182 8588 5140 9247 401 1848 -96 C ATOM 1243 C ASP A 182 -21.315 -38.390 -3.932 1.00 61.65 C ANISOU 1243 C ASP A 182 8875 5579 8969 691 1597 -49 C ATOM 1244 O ASP A 182 -20.843 -38.478 -2.793 1.00 64.95 O ANISOU 1244 O ASP A 182 9579 5959 9139 928 1670 206 O ATOM 1245 CB ASP A 182 -22.701 -40.188 -4.985 1.00 75.64 C ANISOU 1245 CB ASP A 182 10484 6727 11527 340 1865 -251 C ATOM 1246 CG ASP A 182 -24.070 -40.842 -5.060 1.00 80.90 C ANISOU 1246 CG ASP A 182 11030 7013 12695 59 2139 -272 C ATOM 1247 OD1 ASP A 182 -24.991 -40.346 -4.378 1.00 71.72 O ANISOU 1247 OD1 ASP A 182 9830 5832 11590 -55 2372 -107 O ATOM 1248 OD2 ASP A 182 -24.215 -41.848 -5.796 1.00 81.05 O ANISOU 1248 OD2 ASP A 182 10979 6742 13074 -44 2122 -468 O ATOM 1249 N VAL A 183 -20.626 -37.881 -4.958 1.00 55.42 N ANISOU 1249 N VAL A 183 7882 5080 8097 689 1301 -293 N ATOM 1250 CA VAL A 183 -19.278 -37.349 -4.769 1.00 53.81 C ANISOU 1250 CA VAL A 183 7722 5157 7568 931 1059 -276 C ATOM 1251 C VAL A 183 -19.277 -36.279 -3.691 1.00 54.78 C ANISOU 1251 C VAL A 183 7947 5472 7395 1011 1042 -108 C ATOM 1252 O VAL A 183 -18.453 -36.295 -2.774 1.00 62.52 O ANISOU 1252 O VAL A 183 9137 6489 8128 1270 962 42 O ATOM 1253 CB VAL A 183 -18.732 -36.796 -6.092 1.00 54.80 C ANISOU 1253 CB VAL A 183 7572 5566 7684 870 819 -547 C ATOM 1254 CG1 VAL A 183 -17.500 -35.945 -5.850 1.00 52.72 C ANISOU 1254 CG1 VAL A 183 7272 5613 7146 1055 597 -524 C ATOM 1255 CG2 VAL A 183 -18.421 -37.937 -7.048 1.00 61.78 C ANISOU 1255 CG2 VAL A 183 8428 6272 8773 895 804 -721 C ATOM 1256 N ILE A 184 -20.213 -35.338 -3.782 1.00 50.87 N ANISOU 1256 N ILE A 184 7312 5099 6919 809 1097 -147 N ATOM 1257 CA ILE A 184 -20.220 -34.212 -2.860 1.00 56.38 C ANISOU 1257 CA ILE A 184 8097 5990 7336 884 1062 -37 C ATOM 1258 C ILE A 184 -20.414 -34.682 -1.425 1.00 53.59 C ANISOU 1258 C ILE A 184 8104 5437 6821 1073 1279 242 C ATOM 1259 O ILE A 184 -19.657 -34.280 -0.537 1.00 60.47 O ANISOU 1259 O ILE A 184 9175 6435 7365 1317 1138 334 O ATOM 1260 CB ILE A 184 -21.285 -33.186 -3.276 1.00 51.58 C ANISOU 1260 CB ILE A 184 7270 5512 6816 642 1110 -132 C ATOM 1261 CG1 ILE A 184 -20.678 -32.265 -4.332 1.00 51.21 C ANISOU 1261 CG1 ILE A 184 6965 5765 6725 580 828 -342 C ATOM 1262 CG2 ILE A 184 -21.779 -32.435 -2.075 1.00 52.53 C ANISOU 1262 CG2 ILE A 184 7563 5667 6728 709 1240 33 C ATOM 1263 CD1 ILE A 184 -21.697 -31.589 -5.177 1.00 54.34 C ANISOU 1263 CD1 ILE A 184 7120 6248 7279 348 847 -474 C ATOM 1264 N THR A 185 -21.441 -35.514 -1.162 1.00 55.71 N ANISOU 1264 N THR A 185 8465 5385 7317 973 1629 380 N ATOM 1265 CA THR A 185 -21.720 -35.863 0.235 1.00 66.38 C ANISOU 1265 CA THR A 185 10192 6549 8482 1167 1907 690 C ATOM 1266 C THR A 185 -20.531 -36.579 0.850 1.00 69.21 C ANISOU 1266 C THR A 185 10856 6845 8596 1510 1779 826 C ATOM 1267 O THR A 185 -20.201 -36.366 2.022 1.00 67.94 O ANISOU 1267 O THR A 185 11024 6729 8062 1790 1781 1017 O ATOM 1268 CB THR A 185 -22.976 -36.746 0.385 1.00 69.07 C ANISOU 1268 CB THR A 185 10559 6503 9181 993 2360 845 C ATOM 1269 OG1 THR A 185 -22.823 -37.991 -0.327 1.00 66.93 O ANISOU 1269 OG1 THR A 185 10228 5950 9252 919 2387 781 O ATOM 1270 CG2 THR A 185 -24.248 -36.011 -0.066 1.00 67.88 C ANISOU 1270 CG2 THR A 185 10094 6413 9286 684 2495 727 C ATOM 1271 N SER A 186 -19.866 -37.423 0.059 1.00 65.00 N ANISOU 1271 N SER A 186 10226 6215 8257 1520 1647 714 N ATOM 1272 CA SER A 186 -18.748 -38.201 0.569 1.00 64.89 C ANISOU 1272 CA SER A 186 10473 6116 8067 1861 1524 839 C ATOM 1273 C SER A 186 -17.491 -37.351 0.710 1.00 63.18 C ANISOU 1273 C SER A 186 10204 6269 7532 2074 1095 720 C ATOM 1274 O SER A 186 -16.841 -37.383 1.758 1.00 67.89 O ANISOU 1274 O SER A 186 11095 6899 7800 2406 981 877 O ATOM 1275 CB SER A 186 -18.490 -39.397 -0.348 1.00 70.03 C ANISOU 1275 CB SER A 186 11026 6518 9064 1808 1545 740 C ATOM 1276 OG SER A 186 -18.262 -38.956 -1.669 1.00 64.43 O ANISOU 1276 OG SER A 186 9935 6025 8519 1608 1320 416 O ATOM 1277 N THR A 187 -17.130 -36.576 -0.327 1.00 61.11 N ANISOU 1277 N THR A 187 9569 6280 7371 1899 851 444 N ATOM 1278 CA THR A 187 -15.904 -35.795 -0.226 1.00 56.76 C ANISOU 1278 CA THR A 187 8917 6041 6608 2074 467 329 C ATOM 1279 C THR A 187 -16.025 -34.605 0.722 1.00 62.55 C ANISOU 1279 C THR A 187 9759 6976 7032 2137 361 365 C ATOM 1280 O THR A 187 -14.997 -34.100 1.178 1.00 65.73 O ANISOU 1280 O THR A 187 10167 7573 7233 2348 34 306 O ATOM 1281 CB THR A 187 -15.434 -35.261 -1.586 1.00 59.05 C ANISOU 1281 CB THR A 187 8789 6551 7095 1882 285 58 C ATOM 1282 OG1 THR A 187 -16.461 -34.466 -2.206 1.00 57.41 O ANISOU 1282 OG1 THR A 187 8391 6424 6998 1566 401 -42 O ATOM 1283 CG2 THR A 187 -14.990 -36.404 -2.495 1.00 57.21 C ANISOU 1283 CG2 THR A 187 8470 6166 7103 1909 315 -21 C ATOM 1284 N SER A 188 -17.225 -34.119 0.981 1.00 66.36 N ANISOU 1284 N SER A 188 10300 7420 7495 1963 606 428 N ATOM 1285 CA SER A 188 -17.297 -32.962 1.865 1.00 70.96 C ANISOU 1285 CA SER A 188 11001 8190 7771 2048 496 431 C ATOM 1286 C SER A 188 -17.688 -33.307 3.295 1.00 74.72 C ANISOU 1286 C SER A 188 11952 8518 7920 2317 693 694 C ATOM 1287 O SER A 188 -17.300 -32.575 4.204 1.00 78.15 O ANISOU 1287 O SER A 188 12578 9112 8002 2534 490 683 O ATOM 1288 CB SER A 188 -18.253 -31.909 1.311 1.00 75.21 C ANISOU 1288 CB SER A 188 11295 8840 8442 1735 597 310 C ATOM 1289 OG SER A 188 -18.416 -32.065 -0.072 1.00 82.82 O ANISOU 1289 OG SER A 188 12137 9614 9719 1489 908 339 O ATOM 1290 N PHE A 189 -18.391 -34.404 3.552 1.00 76.33 N ANISOU 1290 N PHE A 189 12366 8409 8224 2329 1078 928 N ATOM 1291 CA PHE A 189 -18.787 -34.753 4.911 1.00 76.39 C ANISOU 1291 CA PHE A 189 12862 8261 7903 2606 1335 1226 C ATOM 1292 C PHE A 189 -18.596 -36.214 5.290 1.00 79.81 C ANISOU 1292 C PHE A 189 13600 8370 8353 2822 1539 1493 C ATOM 1293 O PHE A 189 -19.003 -36.593 6.393 1.00 82.46 O ANISOU 1293 O PHE A 189 14375 8537 8420 3060 1829 1791 O ATOM 1294 CB PHE A 189 -20.258 -34.405 5.146 1.00 79.35 C ANISOU 1294 CB PHE A 189 13257 8531 8362 2399 1781 1336 C ATOM 1295 CG PHE A 189 -20.622 -33.016 4.770 1.00 76.17 C ANISOU 1295 CG PHE A 189 12571 8395 7976 2186 1643 1103 C ATOM 1296 CD1 PHE A 189 -20.170 -31.945 5.516 1.00 75.75 C ANISOU 1296 CD1 PHE A 189 12671 8587 7523 2388 1379 1018 C ATOM 1297 CD2 PHE A 189 -21.433 -32.777 3.679 1.00 79.10 C ANISOU 1297 CD2 PHE A 189 12534 8755 8765 1802 1762 960 C ATOM 1298 CE1 PHE A 189 -20.516 -30.652 5.181 1.00 74.75 C ANISOU 1298 CE1 PHE A 189 12299 8667 7435 2197 1267 810 C ATOM 1299 CE2 PHE A 189 -21.782 -31.478 3.331 1.00 83.36 C ANISOU 1299 CE2 PHE A 189 12832 9526 9315 1632 1640 767 C ATOM 1300 CZ PHE A 189 -21.322 -30.413 4.090 1.00 75.67 C ANISOU 1300 CZ PHE A 189 12019 8770 7961 1825 1409 702 C ATOM 1301 N GLY A 190 -18.030 -37.051 4.422 1.00 75.00 N ANISOU 1301 N GLY A 190 12800 7650 8047 2763 1433 1410 N ATOM 1302 CA GLY A 190 -17.996 -38.465 4.729 1.00 78.88 C ANISOU 1302 CA GLY A 190 13578 7772 8620 2938 1680 1670 C ATOM 1303 C GLY A 190 -19.345 -39.147 4.751 1.00 80.84 C ANISOU 1303 C GLY A 190 13897 7643 9177 2710 2247 1878 C ATOM 1304 O GLY A 190 -19.451 -40.258 5.267 1.00 81.57 O ANISOU 1304 O GLY A 190 14311 7380 9303 2879 2537 2168 O ATOM 1305 N VAL A 191 -20.382 -38.514 4.218 1.00 80.18 N ANISOU 1305 N VAL A 191 13509 7610 9347 2337 2417 1747 N ATOM 1306 CA VAL A 191 -21.692 -39.145 4.090 1.00 79.74 C ANISOU 1306 CA VAL A 191 13401 7193 9703 2066 2929 1889 C ATOM 1307 C VAL A 191 -21.679 -39.998 2.826 1.00 75.52 C ANISOU 1307 C VAL A 191 12550 6453 9690 1808 2880 1688 C ATOM 1308 O VAL A 191 -21.487 -39.484 1.719 1.00 71.89 O ANISOU 1308 O VAL A 191 11704 6224 9386 1598 2577 1351 O ATOM 1309 CB VAL A 191 -22.808 -38.091 4.032 1.00 85.59 C ANISOU 1309 CB VAL A 191 13914 8086 10522 1799 3094 1806 C ATOM 1310 CG1 VAL A 191 -24.164 -38.749 4.137 1.00 91.13 C ANISOU 1310 CG1 VAL A 191 14578 8400 11649 1566 3660 1996 C ATOM 1311 CG2 VAL A 191 -22.624 -37.048 5.124 1.00 89.68 C ANISOU 1311 CG2 VAL A 191 14713 8882 10480 2070 3021 1898 C ATOM 1312 N ASN A 192 -21.875 -41.304 2.982 1.00 79.67 N ANISOU 1312 N ASN A 192 13261 6532 10476 1841 3185 1893 N ATOM 1313 CA ASN A 192 -21.734 -42.244 1.872 1.00 80.43 C ANISOU 1313 CA ASN A 192 13131 6390 11037 1661 3116 1692 C ATOM 1314 C ASN A 192 -23.100 -42.812 1.511 1.00 89.40 C ANISOU 1314 C ASN A 192 14077 7139 12753 1286 3529 1700 C ATOM 1315 O ASN A 192 -23.588 -43.734 2.164 1.00 95.21 O ANISOU 1315 O ASN A 192 15061 7433 13683 1321 3962 2008 O ATOM 1316 CB ASN A 192 -20.739 -43.333 2.233 1.00 91.22 C ANISOU 1316 CB ASN A 192 14834 7524 12301 2007 3071 1866 C ATOM 1317 CG ASN A 192 -19.328 -42.802 2.294 1.00 96.10 C ANISOU 1317 CG ASN A 192 15497 8541 12478 2329 2577 1753 C ATOM 1318 OD1 ASN A 192 -18.721 -42.490 1.266 1.00 90.62 O ANISOU 1318 OD1 ASN A 192 14475 8086 11871 2234 2227 1421 O ATOM 1319 ND2 ASN A 192 -18.802 -42.672 3.500 1.00101.73 N ANISOU 1319 ND2 ASN A 192 16608 9330 12716 2720 2547 2023 N ATOM 1320 N ILE A 193 -23.698 -42.276 0.452 1.00 90.63 N ANISOU 1320 N ILE A 193 13784 7447 13206 937 3387 1360 N ATOM 1321 CA ILE A 193 -25.075 -42.568 0.083 1.00 93.92 C ANISOU 1321 CA ILE A 193 13927 7572 14185 559 3704 1305 C ATOM 1322 C ILE A 193 -25.134 -42.919 -1.396 1.00 86.90 C ANISOU 1322 C ILE A 193 12662 6645 13710 297 3424 878 C ATOM 1323 O ILE A 193 -24.449 -42.307 -2.219 1.00 84.45 O ANISOU 1323 O ILE A 193 12190 6711 13188 329 2997 591 O ATOM 1324 CB ILE A 193 -25.998 -41.363 0.380 1.00104.48 C ANISOU 1324 CB ILE A 193 15084 9171 15443 412 3817 1314 C ATOM 1325 CG1 ILE A 193 -26.025 -41.042 1.871 1.00111.33 C ANISOU 1325 CG1 ILE A 193 16361 10057 15882 691 4131 1724 C ATOM 1326 CG2 ILE A 193 -27.411 -41.609 -0.125 1.00113.24 C ANISOU 1326 CG2 ILE A 193 15817 10015 17195 11 4083 1202 C ATOM 1327 CD1 ILE A 193 -26.998 -39.925 2.219 1.00114.48 C ANISOU 1327 CD1 ILE A 193 16600 10665 16230 566 4304 1743 C ATOM 1328 N ASP A 194 -25.974 -43.896 -1.733 1.00 88.18 N ANISOU 1328 N ASP A 194 12690 6343 14472 43 3675 832 N ATOM 1329 CA ASP A 194 -26.365 -44.178 -3.116 1.00 94.33 C ANISOU 1329 CA ASP A 194 13081 7057 15701 -249 3432 388 C ATOM 1330 C ASP A 194 -27.612 -43.341 -3.409 1.00 92.76 C ANISOU 1330 C ASP A 194 12491 7004 15749 -558 3474 243 C ATOM 1331 O ASP A 194 -28.748 -43.811 -3.330 1.00 94.69 O ANISOU 1331 O ASP A 194 12542 6887 16548 -826 3781 265 O ATOM 1332 CB ASP A 194 -26.609 -45.675 -3.289 1.00105.45 C ANISOU 1332 CB ASP A 194 14544 7857 17665 -358 3648 382 C ATOM 1333 CG ASP A 194 -26.951 -46.069 -4.718 1.00104.94 C ANISOU 1333 CG ASP A 194 14124 7698 18050 -623 3353 -123 C ATOM 1334 OD1 ASP A 194 -26.889 -45.214 -5.630 1.00103.69 O ANISOU 1334 OD1 ASP A 194 13713 7974 17712 -680 2966 -456 O ATOM 1335 OD2 ASP A 194 -27.292 -47.252 -4.921 1.00110.14 O ANISOU 1335 OD2 ASP A 194 14776 7827 19245 -762 3514 -187 O ATOM 1336 N SER A 195 -27.386 -42.062 -3.748 1.00 89.72 N ANISOU 1336 N SER A 195 11970 7146 14973 -514 3162 96 N ATOM 1337 CA SER A 195 -28.477 -41.092 -3.710 1.00 80.96 C ANISOU 1337 CA SER A 195 10571 6216 13975 -713 3241 61 C ATOM 1338 C SER A 195 -29.565 -41.390 -4.740 1.00 84.66 C ANISOU 1338 C SER A 195 10594 6512 15061 -1063 3162 -285 C ATOM 1339 O SER A 195 -30.732 -41.055 -4.512 1.00 89.50 O ANISOU 1339 O SER A 195 10948 7056 16001 -1267 3383 -251 O ATOM 1340 CB SER A 195 -27.940 -39.670 -3.894 1.00 79.10 C ANISOU 1340 CB SER A 195 10304 6547 13203 -577 2911 -26 C ATOM 1341 OG SER A 195 -27.453 -39.462 -5.210 1.00 72.25 O ANISOU 1341 OG SER A 195 9247 5919 12285 -610 2464 -398 O ATOM 1342 N LEU A 196 -29.215 -41.993 -5.881 1.00 81.37 N ANISOU 1342 N LEU A 196 10074 6033 14811 -1120 2834 -638 N ATOM 1343 CA LEU A 196 -30.244 -42.374 -6.845 1.00 85.19 C ANISOU 1343 CA LEU A 196 10155 6321 15891 -1433 2713 -1005 C ATOM 1344 C LEU A 196 -31.221 -43.381 -6.249 1.00 88.97 C ANISOU 1344 C LEU A 196 10544 6214 17045 -1664 3165 -853 C ATOM 1345 O LEU A 196 -32.403 -43.394 -6.606 1.00 96.71 O ANISOU 1345 O LEU A 196 11120 7047 18579 -1956 3197 -1043 O ATOM 1346 CB LEU A 196 -29.611 -42.950 -8.114 1.00 88.71 C ANISOU 1346 CB LEU A 196 10586 6773 16346 -1403 2295 -1415 C ATOM 1347 CG LEU A 196 -30.614 -43.353 -9.206 1.00 92.94 C ANISOU 1347 CG LEU A 196 10727 7127 17457 -1692 2071 -1869 C ATOM 1348 CD1 LEU A 196 -31.175 -42.120 -9.877 1.00 93.68 C ANISOU 1348 CD1 LEU A 196 10515 7679 17401 -1752 1763 -2087 C ATOM 1349 CD2 LEU A 196 -29.987 -44.288 -10.232 1.00 96.92 C ANISOU 1349 CD2 LEU A 196 11318 7477 18030 -1637 1769 -2234 C ATOM 1350 N ASN A 197 -30.749 -44.222 -5.339 1.00 90.45 N ANISOU 1350 N ASN A 197 11093 6055 17219 -1529 3524 -502 N ATOM 1351 CA ASN A 197 -31.565 -45.247 -4.718 1.00 95.41 C ANISOU 1351 CA ASN A 197 11682 6195 18375 -1680 3966 -294 C ATOM 1352 C ASN A 197 -31.998 -44.885 -3.306 1.00104.61 C ANISOU 1352 C ASN A 197 13009 7362 19377 -1584 4484 206 C ATOM 1353 O ASN A 197 -32.728 -45.654 -2.680 1.00114.23 O ANISOU 1353 O ASN A 197 14185 8317 20898 -1640 4856 412 O ATOM 1354 CB ASN A 197 -30.808 -46.572 -4.726 1.00 97.38 C ANISOU 1354 CB ASN A 197 12227 6092 18681 -1553 3989 -250 C ATOM 1355 CG ASN A 197 -30.547 -47.059 -6.125 1.00100.33 C ANISOU 1355 CG ASN A 197 12426 6447 19248 -1644 3508 -771 C ATOM 1356 OD1 ASN A 197 -31.487 -47.342 -6.873 1.00107.57 O ANISOU 1356 OD1 ASN A 197 12947 7334 20591 -1889 3336 -1094 O ATOM 1357 ND2 ASN A 197 -29.273 -47.150 -6.503 1.00 93.39 N ANISOU 1357 ND2 ASN A 197 11842 5605 18035 -1410 3274 -869 N ATOM 1358 N ASN A 198 -31.573 -43.734 -2.792 1.00109.95 N ANISOU 1358 N ASN A 198 13875 8356 19546 -1413 4506 391 N ATOM 1359 CA ASN A 198 -32.121 -43.184 -1.552 1.00114.95 C ANISOU 1359 CA ASN A 198 14626 9050 19998 -1324 4966 799 C ATOM 1360 C ASN A 198 -32.542 -41.740 -1.775 1.00119.78 C ANISOU 1360 C ASN A 198 14975 10137 20399 -1370 4772 651 C ATOM 1361 O ASN A 198 -32.241 -40.867 -0.962 1.00110.03 O ANISOU 1361 O ASN A 198 13989 9207 18612 -1132 4859 888 O ATOM 1362 CB ASN A 198 -31.107 -43.269 -0.419 1.00108.41 C ANISOU 1362 CB ASN A 198 14402 8227 18563 -935 5171 1231 C ATOM 1363 CG ASN A 198 -30.547 -44.660 -0.247 1.00108.73 C ANISOU 1363 CG ASN A 198 14724 7873 18717 -821 5277 1363 C ATOM 1364 OD1 ASN A 198 -29.453 -44.968 -0.728 1.00101.36 O ANISOU 1364 OD1 ASN A 198 13982 6950 17579 -667 4948 1236 O ATOM 1365 ND2 ASN A 198 -31.293 -45.513 0.440 1.00122.43 N ANISOU 1365 ND2 ASN A 198 16451 9344 20722 -855 5689 1587 N ATOM 1366 N PRO A 199 -33.304 -41.460 -2.857 1.00142.02 N ANISOU 1366 N PRO A 199 17282 13036 23643 -1654 4487 245 N ATOM 1367 CA PRO A 199 -33.432 -40.073 -3.342 1.00155.14 C ANISOU 1367 CA PRO A 199 18725 15230 24992 -1631 4131 35 C ATOM 1368 C PRO A 199 -34.100 -39.176 -2.319 1.00162.23 C ANISOU 1368 C PRO A 199 19627 16261 25752 -1573 4512 328 C ATOM 1369 O PRO A 199 -34.376 -37.992 -2.549 1.00165.59 O ANISOU 1369 O PRO A 199 19868 17073 25976 -1555 4312 205 O ATOM 1370 CB PRO A 199 -34.297 -40.217 -4.605 1.00157.50 C ANISOU 1370 CB PRO A 199 18486 15470 25886 -1945 3827 -421 C ATOM 1371 CG PRO A 199 -34.502 -41.708 -4.812 1.00155.93 C ANISOU 1371 CG PRO A 199 18253 14822 26170 -2062 3913 -492 C ATOM 1372 CD PRO A 199 -34.304 -42.341 -3.478 1.00152.04 C ANISOU 1372 CD PRO A 199 18144 14053 25571 -1908 4454 -7 C ATOM 1373 N GLN A 200 -34.333 -39.768 -1.160 1.00159.24 N ANISOU 1373 N GLN A 200 19499 15549 25457 -1510 5085 734 N ATOM 1374 CA GLN A 200 -35.289 -39.273 -0.199 1.00156.19 C ANISOU 1374 CA GLN A 200 19063 15237 25046 -1436 5480 966 C ATOM 1375 C GLN A 200 -34.772 -39.352 1.233 1.00145.56 C ANISOU 1375 C GLN A 200 18287 13839 23178 -1106 5901 1436 C ATOM 1376 O GLN A 200 -35.501 -38.976 2.156 1.00150.24 O ANISOU 1376 O GLN A 200 18921 14480 23685 -988 6259 1644 O ATOM 1377 CB GLN A 200 -36.584 -40.068 -0.366 1.00167.88 C ANISOU 1377 CB GLN A 200 20134 16456 27199 -1635 5638 856 C ATOM 1378 CG GLN A 200 -37.061 -40.230 -1.826 1.00175.00 C ANISOU 1378 CG GLN A 200 20518 17377 28599 -1916 5155 362 C ATOM 1379 CD GLN A 200 -38.192 -41.243 -1.998 1.00189.01 C ANISOU 1379 CD GLN A 200 21938 18826 31051 -2099 5293 256 C ATOM 1380 OE1 GLN A 200 -38.151 -42.346 -1.448 1.00196.79 O ANISOU 1380 OE1 GLN A 200 23103 19459 32208 -2078 5619 463 O ATOM 1381 NE2 GLN A 200 -39.228 -40.851 -2.738 1.00190.99 N ANISOU 1381 NE2 GLN A 200 21688 19191 31688 -2264 5046 -58 N ATOM 1382 N ASP A 201 -33.563 -39.865 1.443 1.00130.60 N ANISOU 1382 N ASP A 201 16848 11842 20932 -921 5846 1594 N ATOM 1383 CA ASP A 201 -32.778 -39.538 2.624 1.00120.92 C ANISOU 1383 CA ASP A 201 16209 10728 19006 -537 6037 1968 C ATOM 1384 C ASP A 201 -32.746 -38.021 2.800 1.00116.21 C ANISOU 1384 C ASP A 201 15593 10645 17917 -401 5816 1870 C ATOM 1385 O ASP A 201 -32.656 -37.288 1.808 1.00113.60 O ANISOU 1385 O ASP A 201 14933 10628 17602 -528 5329 1501 O ATOM 1386 CB ASP A 201 -31.356 -40.097 2.452 1.00118.04 C ANISOU 1386 CB ASP A 201 16202 10392 18256 -307 5663 1942 C ATOM 1387 CG ASP A 201 -30.360 -39.631 3.531 1.00116.04 C ANISOU 1387 CG ASP A 201 16515 10388 17186 147 5623 2205 C ATOM 1388 OD1 ASP A 201 -30.238 -38.420 3.824 1.00109.73 O ANISOU 1388 OD1 ASP A 201 15757 9997 15939 284 5452 2149 O ATOM 1389 OD2 ASP A 201 -29.639 -40.504 4.062 1.00116.17 O ANISOU 1389 OD2 ASP A 201 16946 10183 17011 384 5721 2448 O ATOM 1390 N PRO A 202 -32.805 -37.515 4.036 1.00114.89 N ANISOU 1390 N PRO A 202 15796 10564 17294 -124 6162 2190 N ATOM 1391 CA PRO A 202 -32.808 -36.051 4.235 1.00104.54 C ANISOU 1391 CA PRO A 202 14475 9705 15540 7 5959 2076 C ATOM 1392 C PRO A 202 -31.607 -35.342 3.625 1.00 98.04 C ANISOU 1392 C PRO A 202 13704 9287 14258 128 5266 1787 C ATOM 1393 O PRO A 202 -31.751 -34.284 2.994 1.00 93.60 O ANISOU 1393 O PRO A 202 12849 9041 13673 31 4940 1513 O ATOM 1394 CB PRO A 202 -32.818 -35.914 5.763 1.00103.18 C ANISOU 1394 CB PRO A 202 14837 9500 14868 364 6428 2483 C ATOM 1395 CG PRO A 202 -33.389 -37.200 6.260 1.00116.86 C ANISOU 1395 CG PRO A 202 16606 10838 16958 361 6811 2677 C ATOM 1396 CD PRO A 202 -32.929 -38.256 5.302 1.00116.80 C ANISOU 1396 CD PRO A 202 16448 10571 17359 139 6620 2566 C ATOM 1397 N PHE A 203 -30.416 -35.908 3.799 1.00100.94 N ANISOU 1397 N PHE A 203 14430 9639 14283 347 5049 1854 N ATOM 1398 CA PHE A 203 -29.199 -35.245 3.345 1.00 95.69 C ANISOU 1398 CA PHE A 203 13823 9346 13191 487 4441 1615 C ATOM 1399 C PHE A 203 -29.161 -35.073 1.834 1.00 94.47 C ANISOU 1399 C PHE A 203 13192 9322 13381 200 4018 1227 C ATOM 1400 O PHE A 203 -28.578 -34.106 1.335 1.00 83.91 O ANISOU 1400 O PHE A 203 11756 8339 11786 234 3591 1003 O ATOM 1401 CB PHE A 203 -27.984 -36.035 3.808 1.00 98.04 C ANISOU 1401 CB PHE A 203 14548 9558 13145 777 4320 1770 C ATOM 1402 CG PHE A 203 -26.838 -35.178 4.176 1.00 93.88 C ANISOU 1402 CG PHE A 203 14264 9399 12008 1072 3897 1694 C ATOM 1403 CD1 PHE A 203 -26.537 -34.936 5.502 1.00 99.17 C ANISOU 1403 CD1 PHE A 203 15418 10119 12142 1436 4033 1942 C ATOM 1404 CD2 PHE A 203 -26.073 -34.589 3.198 1.00 86.99 C ANISOU 1404 CD2 PHE A 203 13134 8817 11103 993 3367 1367 C ATOM 1405 CE1 PHE A 203 -25.486 -34.122 5.846 1.00 96.16 C ANISOU 1405 CE1 PHE A 203 15229 10067 11240 1698 3594 1826 C ATOM 1406 CE2 PHE A 203 -25.015 -33.777 3.536 1.00 89.06 C ANISOU 1406 CE2 PHE A 203 13568 9391 10880 1236 2981 1285 C ATOM 1407 CZ PHE A 203 -24.722 -33.543 4.867 1.00 89.21 C ANISOU 1407 CZ PHE A 203 14040 9451 10403 1582 3071 1496 C ATOM 1408 N VAL A 204 -29.741 -36.011 1.088 1.00100.60 N ANISOU 1408 N VAL A 204 13688 9804 14731 -68 4123 1138 N ATOM 1409 CA VAL A 204 -29.953 -35.785 -0.338 1.00 98.11 C ANISOU 1409 CA VAL A 204 12918 9617 14743 -330 3753 756 C ATOM 1410 C VAL A 204 -31.062 -34.761 -0.543 1.00 89.44 C ANISOU 1410 C VAL A 204 11473 8684 13827 -495 3806 646 C ATOM 1411 O VAL A 204 -30.933 -33.831 -1.344 1.00 88.48 O ANISOU 1411 O VAL A 204 11135 8882 13601 -539 3424 392 O ATOM 1412 CB VAL A 204 -30.285 -37.107 -1.056 1.00106.33 C ANISOU 1412 CB VAL A 204 13771 10276 16354 -555 3818 650 C ATOM 1413 CG1 VAL A 204 -30.169 -36.929 -2.561 1.00112.57 C ANISOU 1413 CG1 VAL A 204 14207 11245 17319 -728 3337 229 C ATOM 1414 CG2 VAL A 204 -29.402 -38.247 -0.566 1.00104.89 C ANISOU 1414 CG2 VAL A 204 13979 9824 16051 -367 3923 854 C ATOM 1415 N GLU A 205 -32.168 -34.923 0.190 1.00 90.85 N ANISOU 1415 N GLU A 205 11594 8632 14291 -571 4308 854 N ATOM 1416 CA GLU A 205 -33.329 -34.057 0.037 1.00 90.49 C ANISOU 1416 CA GLU A 205 11179 8699 14502 -723 4410 761 C ATOM 1417 C GLU A 205 -32.943 -32.595 0.120 1.00 77.77 C ANISOU 1417 C GLU A 205 9643 7518 12387 -551 4131 680 C ATOM 1418 O GLU A 205 -33.398 -31.779 -0.688 1.00 81.15 O ANISOU 1418 O GLU A 205 9722 8157 12955 -674 3874 438 O ATOM 1419 CB GLU A 205 -34.360 -34.390 1.112 1.00105.45 C ANISOU 1419 CB GLU A 205 13107 10300 16657 -739 5075 1079 C ATOM 1420 CG GLU A 205 -35.789 -34.118 0.732 1.00118.11 C ANISOU 1420 CG GLU A 205 14175 11832 18870 -1004 5261 960 C ATOM 1421 CD GLU A 205 -36.749 -34.710 1.745 1.00134.54 C ANISOU 1421 CD GLU A 205 16295 13602 21222 -980 5847 1244 C ATOM 1422 OE1 GLU A 205 -36.772 -34.215 2.894 1.00144.43 O ANISOU 1422 OE1 GLU A 205 17891 14937 22049 -714 6148 1505 O ATOM 1423 OE2 GLU A 205 -37.458 -35.681 1.402 1.00135.81 O ANISOU 1423 OE2 GLU A 205 16176 13471 21953 -1170 5913 1163 O ATOM 1424 N ASN A 206 -32.087 -32.244 1.076 1.00 72.34 N ANISOU 1424 N ASN A 206 9414 6954 11117 -254 4152 867 N ATOM 1425 CA ASN A 206 -31.717 -30.838 1.214 1.00 78.83 C ANISOU 1425 CA ASN A 206 10310 8143 11499 -100 3890 774 C ATOM 1426 C ASN A 206 -30.706 -30.411 0.160 1.00 82.71 C ANISOU 1426 C ASN A 206 10707 8895 11824 -117 3311 504 C ATOM 1427 O ASN A 206 -30.920 -29.423 -0.555 1.00 69.56 O ANISOU 1427 O ASN A 206 8784 7458 10187 -198 3055 302 O ATOM 1428 CB ASN A 206 -31.170 -30.571 2.614 1.00 81.20 C ANISOU 1428 CB ASN A 206 11128 8484 11239 234 4073 1023 C ATOM 1429 CG ASN A 206 -32.259 -30.546 3.647 1.00 93.77 C ANISOU 1429 CG ASN A 206 12811 9913 12903 294 4661 1275 C ATOM 1430 OD1 ASN A 206 -32.702 -29.477 4.063 1.00103.94 O ANISOU 1430 OD1 ASN A 206 14101 11371 14019 385 4736 1257 O ATOM 1431 ND2 ASN A 206 -32.730 -31.723 4.044 1.00 92.08 N ANISOU 1431 ND2 ASN A 206 12661 9346 12978 242 5112 1516 N ATOM 1432 N THR A 207 -29.585 -31.132 0.057 1.00 86.44 N ANISOU 1432 N THR A 207 11392 9329 12120 -22 3120 514 N ATOM 1433 CA THR A 207 -28.544 -30.694 -0.865 1.00 80.28 C ANISOU 1433 CA THR A 207 10537 8802 11162 -9 2624 287 C ATOM 1434 C THR A 207 -29.049 -30.709 -2.300 1.00 72.38 C ANISOU 1434 C THR A 207 9115 7840 10544 -260 2420 24 C ATOM 1435 O THR A 207 -28.577 -29.921 -3.127 1.00 71.51 O ANISOU 1435 O THR A 207 8876 7989 10305 -269 2071 -161 O ATOM 1436 CB THR A 207 -27.294 -31.563 -0.712 1.00 84.18 C ANISOU 1436 CB THR A 207 11302 9229 11454 152 2490 348 C ATOM 1437 OG1 THR A 207 -27.665 -32.939 -0.766 1.00 95.02 O ANISOU 1437 OG1 THR A 207 12679 10257 13165 61 2737 436 O ATOM 1438 CG2 THR A 207 -26.640 -31.300 0.619 1.00 87.08 C ANISOU 1438 CG2 THR A 207 12090 9646 11352 453 2553 554 C ATOM 1439 N LYS A 208 -30.038 -31.563 -2.608 1.00 65.10 N ANISOU 1439 N LYS A 208 7976 6658 10102 -458 2633 2 N ATOM 1440 CA LYS A 208 -30.624 -31.567 -3.949 1.00 68.49 C ANISOU 1440 CA LYS A 208 8006 7128 10891 -675 2401 -283 C ATOM 1441 C LYS A 208 -31.208 -30.211 -4.328 1.00 74.62 C ANISOU 1441 C LYS A 208 8551 8174 11627 -704 2254 -397 C ATOM 1442 O LYS A 208 -31.420 -29.942 -5.517 1.00 72.81 O ANISOU 1442 O LYS A 208 8055 8078 11532 -803 1953 -640 O ATOM 1443 CB LYS A 208 -31.711 -32.638 -4.073 1.00 73.62 C ANISOU 1443 CB LYS A 208 8423 7423 12124 -893 2660 -305 C ATOM 1444 CG LYS A 208 -31.166 -34.008 -4.419 1.00 84.30 C ANISOU 1444 CG LYS A 208 9874 8514 13640 -931 2628 -351 C ATOM 1445 CD LYS A 208 -32.125 -34.820 -5.307 1.00 88.97 C ANISOU 1445 CD LYS A 208 10092 8856 14855 -1202 2600 -593 C ATOM 1446 CE LYS A 208 -33.065 -35.679 -4.488 1.00 98.57 C ANISOU 1446 CE LYS A 208 11250 9646 16557 -1345 3099 -393 C ATOM 1447 NZ LYS A 208 -33.250 -37.044 -5.075 1.00100.93 N ANISOU 1447 NZ LYS A 208 11424 9560 17364 -1530 3093 -555 N ATOM 1448 N LYS A 209 -31.494 -29.358 -3.353 1.00 76.22 N ANISOU 1448 N LYS A 209 8870 8453 11638 -594 2460 -230 N ATOM 1449 CA LYS A 209 -32.101 -28.078 -3.680 1.00 76.58 C ANISOU 1449 CA LYS A 209 8699 8718 11678 -608 2343 -330 C ATOM 1450 C LYS A 209 -31.060 -27.016 -4.024 1.00 76.21 C ANISOU 1450 C LYS A 209 8785 8967 11205 -475 1992 -404 C ATOM 1451 O LYS A 209 -31.435 -25.932 -4.475 1.00 74.94 O ANISOU 1451 O LYS A 209 8458 8985 11031 -479 1845 -497 O ATOM 1452 CB LYS A 209 -33.019 -27.633 -2.525 1.00 72.75 C ANISOU 1452 CB LYS A 209 8247 8154 11239 -553 2757 -142 C ATOM 1453 CG LYS A 209 -34.151 -28.657 -2.223 1.00 68.85 C ANISOU 1453 CG LYS A 209 7555 7340 11264 -715 3169 -51 C ATOM 1454 CD LYS A 209 -35.006 -28.295 -1.022 1.00 72.85 C ANISOU 1454 CD LYS A 209 8121 7757 11801 -633 3661 173 C ATOM 1455 CE LYS A 209 -35.948 -29.448 -0.648 1.00 73.53 C ANISOU 1455 CE LYS A 209 8046 7478 12416 -793 4134 314 C ATOM 1456 NZ LYS A 209 -36.503 -29.279 0.729 1.00 92.22 N ANISOU 1456 NZ LYS A 209 10617 9732 14692 -647 4708 616 N ATOM 1457 N LEU A 210 -29.765 -27.316 -3.869 1.00 70.51 N ANISOU 1457 N LEU A 210 8331 8283 10176 -359 1854 -365 N ATOM 1458 CA LEU A 210 -28.698 -26.338 -4.101 1.00 58.35 C ANISOU 1458 CA LEU A 210 6895 6989 8286 -245 1555 -420 C ATOM 1459 C LEU A 210 -28.325 -26.348 -5.583 1.00 58.69 C ANISOU 1459 C LEU A 210 6736 7162 8401 -329 1241 -616 C ATOM 1460 O LEU A 210 -27.310 -26.884 -6.005 1.00 61.97 O ANISOU 1460 O LEU A 210 7233 7600 8711 -289 1089 -658 O ATOM 1461 CB LEU A 210 -27.511 -26.633 -3.195 1.00 63.75 C ANISOU 1461 CB LEU A 210 7922 7656 8643 -66 1549 -297 C ATOM 1462 CG LEU A 210 -27.744 -26.203 -1.743 1.00 65.95 C ANISOU 1462 CG LEU A 210 8464 7891 8702 90 1785 -128 C ATOM 1463 CD1 LEU A 210 -26.690 -26.713 -0.760 1.00 52.36 C ANISOU 1463 CD1 LEU A 210 7112 6123 6659 303 1778 0 C ATOM 1464 CD2 LEU A 210 -27.783 -24.681 -1.727 1.00 67.95 C ANISOU 1464 CD2 LEU A 210 8674 8341 8804 129 1640 -207 C ATOM 1465 N LEU A 211 -29.167 -25.726 -6.388 1.00 60.94 N ANISOU 1465 N LEU A 211 6764 7539 8852 -418 1148 -734 N ATOM 1466 CA LEU A 211 -28.988 -25.688 -7.830 1.00 57.23 C ANISOU 1466 CA LEU A 211 6126 7201 8418 -464 863 -916 C ATOM 1467 C LEU A 211 -28.359 -24.362 -8.235 1.00 50.49 C ANISOU 1467 C LEU A 211 5301 6580 7302 -377 671 -916 C ATOM 1468 O LEU A 211 -28.235 -23.441 -7.430 1.00 52.81 O ANISOU 1468 O LEU A 211 5699 6913 7451 -309 738 -812 O ATOM 1469 CB LEU A 211 -30.329 -25.881 -8.545 1.00 65.18 C ANISOU 1469 CB LEU A 211 6828 8160 9775 -590 836 -1061 C ATOM 1470 CG LEU A 211 -30.923 -27.287 -8.566 1.00 71.78 C ANISOU 1470 CG LEU A 211 7557 8744 10971 -722 956 -1133 C ATOM 1471 CD1 LEU A 211 -32.322 -27.182 -9.074 1.00 77.63 C ANISOU 1471 CD1 LEU A 211 7951 9454 12090 -841 920 -1277 C ATOM 1472 CD2 LEU A 211 -30.100 -28.213 -9.477 1.00 79.66 C ANISOU 1472 CD2 LEU A 211 8619 9728 11920 -720 754 -1282 C ATOM 1473 N ARG A 212 -27.940 -24.288 -9.495 1.00 51.41 N ANISOU 1473 N ARG A 212 5343 6832 7358 -370 444 -1035 N ATOM 1474 CA ARG A 212 -27.484 -23.030 -10.059 1.00 54.06 C ANISOU 1474 CA ARG A 212 5678 7360 7501 -301 296 -1019 C ATOM 1475 C ARG A 212 -28.607 -22.005 -10.011 1.00 53.00 C ANISOU 1475 C ARG A 212 5411 7263 7464 -306 310 -1007 C ATOM 1476 O ARG A 212 -29.777 -22.354 -10.173 1.00 49.45 O ANISOU 1476 O ARG A 212 4781 6751 7255 -369 336 -1085 O ATOM 1477 CB ARG A 212 -27.063 -23.223 -11.502 1.00 53.17 C ANISOU 1477 CB ARG A 212 5515 7376 7312 -271 101 -1135 C ATOM 1478 CG ARG A 212 -25.783 -23.948 -11.711 1.00 53.47 C ANISOU 1478 CG ARG A 212 5675 7421 7220 -226 79 -1142 C ATOM 1479 CD ARG A 212 -25.471 -23.950 -13.193 1.00 54.50 C ANISOU 1479 CD ARG A 212 5772 7701 7234 -162 -79 -1251 C ATOM 1480 NE ARG A 212 -26.302 -24.904 -13.930 1.00 55.39 N ANISOU 1480 NE ARG A 212 5797 7762 7489 -196 -176 -1448 N ATOM 1481 CZ ARG A 212 -26.289 -25.040 -15.254 1.00 51.48 C ANISOU 1481 CZ ARG A 212 5292 7389 6879 -116 -344 -1594 C ATOM 1482 NH1 ARG A 212 -25.497 -24.279 -15.996 1.00 56.12 N ANISOU 1482 NH1 ARG A 212 5960 8160 7204 6 -379 -1521 N ATOM 1483 NH2 ARG A 212 -27.084 -25.918 -15.837 1.00 53.24 N ANISOU 1483 NH2 ARG A 212 5429 7543 7257 -150 -473 -1816 N ATOM 1484 N PHE A 213 -28.241 -20.740 -9.797 1.00 47.62 N ANISOU 1484 N PHE A 213 4798 6665 6631 -240 286 -921 N ATOM 1485 CA PHE A 213 -29.207 -19.655 -9.863 1.00 51.04 C ANISOU 1485 CA PHE A 213 5119 7135 7140 -211 281 -909 C ATOM 1486 C PHE A 213 -29.533 -19.261 -11.307 1.00 60.36 C ANISOU 1486 C PHE A 213 6169 8453 8313 -170 71 -982 C ATOM 1487 O PHE A 213 -28.644 -19.140 -12.160 1.00 64.38 O ANISOU 1487 O PHE A 213 6752 9064 8644 -125 -47 -975 O ATOM 1488 CB PHE A 213 -28.673 -18.424 -9.142 1.00 49.20 C ANISOU 1488 CB PHE A 213 5027 6906 6761 -147 319 -807 C ATOM 1489 CG PHE A 213 -28.487 -18.605 -7.683 1.00 50.91 C ANISOU 1489 CG PHE A 213 5405 7009 6929 -132 493 -751 C ATOM 1490 CD1 PHE A 213 -27.217 -18.522 -7.136 1.00 55.83 C ANISOU 1490 CD1 PHE A 213 6214 7629 7371 -96 450 -717 C ATOM 1491 CD2 PHE A 213 -29.567 -18.852 -6.854 1.00 53.92 C ANISOU 1491 CD2 PHE A 213 5753 7290 7444 -133 701 -732 C ATOM 1492 CE1 PHE A 213 -27.017 -18.664 -5.785 1.00 53.16 C ANISOU 1492 CE1 PHE A 213 6066 7202 6931 -37 568 -677 C ATOM 1493 CE2 PHE A 213 -29.371 -19.000 -5.487 1.00 51.43 C ANISOU 1493 CE2 PHE A 213 5648 6878 7016 -74 883 -661 C ATOM 1494 CZ PHE A 213 -28.083 -18.913 -4.964 1.00 44.87 C ANISOU 1494 CZ PHE A 213 5041 6059 5950 -13 792 -640 C ATOM 1495 N ASP A 214 -30.810 -18.991 -11.563 1.00 51.62 N ANISOU 1495 N ASP A 214 4871 7353 7390 -160 34 -1040 N ATOM 1496 CA ASP A 214 -31.225 -18.426 -12.845 1.00 50.31 C ANISOU 1496 CA ASP A 214 4606 7326 7182 -66 -192 -1096 C ATOM 1497 C ASP A 214 -31.175 -16.908 -12.715 1.00 52.15 C ANISOU 1497 C ASP A 214 4907 7593 7315 35 -176 -959 C ATOM 1498 O ASP A 214 -32.140 -16.267 -12.259 1.00 50.78 O ANISOU 1498 O ASP A 214 4620 7377 7297 70 -121 -945 O ATOM 1499 CB ASP A 214 -32.624 -18.900 -13.230 1.00 55.33 C ANISOU 1499 CB ASP A 214 4970 7953 8100 -87 -294 -1254 C ATOM 1500 CG ASP A 214 -33.042 -18.430 -14.616 1.00 54.64 C ANISOU 1500 CG ASP A 214 4805 8029 7927 53 -590 -1338 C ATOM 1501 OD1 ASP A 214 -32.308 -17.631 -15.258 1.00 57.10 O ANISOU 1501 OD1 ASP A 214 5295 8453 7948 176 -664 -1230 O ATOM 1502 OD2 ASP A 214 -34.098 -18.876 -15.073 1.00 63.14 O ANISOU 1502 OD2 ASP A 214 5643 9115 9233 49 -750 -1511 O ATOM 1503 N PHE A 215 -30.066 -16.328 -13.141 1.00 48.63 N ANISOU 1503 N PHE A 215 4631 7206 6643 84 -209 -860 N ATOM 1504 CA PHE A 215 -29.891 -14.898 -12.965 1.00 51.93 C ANISOU 1504 CA PHE A 215 5128 7601 7004 157 -174 -726 C ATOM 1505 C PHE A 215 -30.801 -14.081 -13.867 1.00 57.48 C ANISOU 1505 C PHE A 215 5743 8378 7720 300 -313 -706 C ATOM 1506 O PHE A 215 -30.830 -12.859 -13.732 1.00 71.99 O ANISOU 1506 O PHE A 215 7638 10165 9549 376 -278 -592 O ATOM 1507 CB PHE A 215 -28.427 -14.532 -13.198 1.00 54.16 C ANISOU 1507 CB PHE A 215 5576 7893 7109 149 -149 -620 C ATOM 1508 CG PHE A 215 -27.499 -15.087 -12.166 1.00 64.71 C ANISOU 1508 CG PHE A 215 6996 9150 8442 45 -45 -632 C ATOM 1509 CD1 PHE A 215 -27.585 -14.659 -10.842 1.00 66.73 C ANISOU 1509 CD1 PHE A 215 7308 9285 8762 18 57 -624 C ATOM 1510 CD2 PHE A 215 -26.521 -16.013 -12.508 1.00 73.44 C ANISOU 1510 CD2 PHE A 215 8141 10303 9459 8 -58 -658 C ATOM 1511 CE1 PHE A 215 -26.727 -15.170 -9.877 1.00 61.43 C ANISOU 1511 CE1 PHE A 215 6741 8553 8048 -35 112 -642 C ATOM 1512 CE2 PHE A 215 -25.662 -16.516 -11.554 1.00 75.27 C ANISOU 1512 CE2 PHE A 215 8447 10466 9687 -54 7 -667 C ATOM 1513 CZ PHE A 215 -25.764 -16.091 -10.235 1.00 72.24 C ANISOU 1513 CZ PHE A 215 8128 9971 9347 -71 77 -658 C ATOM 1514 N LEU A 216 -31.554 -14.710 -14.767 1.00 49.12 N ANISOU 1514 N LEU A 216 4549 7424 6692 353 -490 -828 N ATOM 1515 CA LEU A 216 -32.535 -14.008 -15.585 1.00 48.17 C ANISOU 1515 CA LEU A 216 4327 7385 6590 523 -671 -833 C ATOM 1516 C LEU A 216 -33.978 -14.311 -15.190 1.00 59.39 C ANISOU 1516 C LEU A 216 5462 8775 8327 509 -715 -976 C ATOM 1517 O LEU A 216 -34.894 -13.931 -15.927 1.00 59.80 O ANISOU 1517 O LEU A 216 5374 8912 8435 660 -923 -1028 O ATOM 1518 CB LEU A 216 -32.331 -14.339 -17.065 1.00 55.71 C ANISOU 1518 CB LEU A 216 5348 8507 7311 654 -900 -881 C ATOM 1519 CG LEU A 216 -31.065 -13.772 -17.703 1.00 66.03 C ANISOU 1519 CG LEU A 216 6917 9859 8311 730 -831 -694 C ATOM 1520 CD1 LEU A 216 -31.055 -14.128 -19.187 1.00 69.52 C ANISOU 1520 CD1 LEU A 216 7448 10484 8484 913 -1047 -751 C ATOM 1521 CD2 LEU A 216 -30.992 -12.273 -17.479 1.00 72.01 C ANISOU 1521 CD2 LEU A 216 7762 10530 9066 812 -728 -477 C ATOM 1522 N ASP A 217 -34.210 -14.980 -14.062 1.00 61.09 N ANISOU 1522 N ASP A 217 5583 8869 8759 348 -518 -1030 N ATOM 1523 CA ASP A 217 -35.569 -15.268 -13.637 1.00 65.63 C ANISOU 1523 CA ASP A 217 5856 9391 9690 321 -489 -1143 C ATOM 1524 C ASP A 217 -36.197 -14.002 -13.047 1.00 70.91 C ANISOU 1524 C ASP A 217 6482 10010 10452 437 -377 -1038 C ATOM 1525 O ASP A 217 -35.491 -13.028 -12.777 1.00 67.90 O ANISOU 1525 O ASP A 217 6333 9595 9873 499 -296 -891 O ATOM 1526 CB ASP A 217 -35.568 -16.452 -12.660 1.00 69.29 C ANISOU 1526 CB ASP A 217 6264 9720 10342 124 -260 -1198 C ATOM 1527 CG ASP A 217 -35.142 -16.084 -11.240 1.00 72.13 C ANISOU 1527 CG ASP A 217 6802 9954 10652 84 64 -1054 C ATOM 1528 OD1 ASP A 217 -35.240 -16.964 -10.367 1.00 79.38 O ANISOU 1528 OD1 ASP A 217 7702 10754 11703 -35 284 -1062 O ATOM 1529 OD2 ASP A 217 -34.723 -14.946 -10.971 1.00 78.32 O ANISOU 1529 OD2 ASP A 217 7754 10738 11264 180 102 -938 O ATOM 1530 N PRO A 218 -37.531 -13.970 -12.870 1.00 68.43 N ANISOU 1530 N PRO A 218 5854 9676 10471 475 -375 -1125 N ATOM 1531 CA PRO A 218 -38.171 -12.732 -12.383 1.00 69.16 C ANISOU 1531 CA PRO A 218 5899 9721 10657 624 -272 -1036 C ATOM 1532 C PRO A 218 -37.484 -12.091 -11.189 1.00 65.55 C ANISOU 1532 C PRO A 218 5714 9136 10058 604 26 -899 C ATOM 1533 O PRO A 218 -37.180 -10.887 -11.230 1.00 62.24 O ANISOU 1533 O PRO A 218 5464 8689 9495 735 8 -793 O ATOM 1534 CB PRO A 218 -39.592 -13.198 -12.053 1.00 62.48 C ANISOU 1534 CB PRO A 218 4640 8840 10260 600 -205 -1164 C ATOM 1535 CG PRO A 218 -39.852 -14.277 -13.045 1.00 68.91 C ANISOU 1535 CG PRO A 218 5250 9743 11190 525 -491 -1348 C ATOM 1536 CD PRO A 218 -38.527 -14.946 -13.349 1.00 69.77 C ANISOU 1536 CD PRO A 218 5671 9875 10963 415 -530 -1327 C ATOM 1537 N PHE A 219 -37.153 -12.876 -10.162 1.00 66.21 N ANISOU 1537 N PHE A 219 5872 9126 10157 453 279 -903 N ATOM 1538 CA PHE A 219 -36.478 -12.325 -8.991 1.00 52.37 C ANISOU 1538 CA PHE A 219 4403 7262 8232 460 516 -809 C ATOM 1539 C PHE A 219 -35.175 -11.629 -9.365 1.00 57.25 C ANISOU 1539 C PHE A 219 5312 7894 8546 480 376 -730 C ATOM 1540 O PHE A 219 -34.975 -10.448 -9.040 1.00 55.43 O ANISOU 1540 O PHE A 219 5227 7590 8245 580 409 -669 O ATOM 1541 CB PHE A 219 -36.218 -13.423 -7.947 1.00 54.94 C ANISOU 1541 CB PHE A 219 4808 7507 8561 323 768 -814 C ATOM 1542 CG PHE A 219 -35.516 -12.910 -6.709 1.00 53.41 C ANISOU 1542 CG PHE A 219 4934 7215 8144 367 966 -747 C ATOM 1543 CD1 PHE A 219 -36.200 -12.109 -5.784 1.00 58.74 C ANISOU 1543 CD1 PHE A 219 5635 7807 8877 497 1188 -731 C ATOM 1544 CD2 PHE A 219 -34.186 -13.180 -6.491 1.00 45.84 C ANISOU 1544 CD2 PHE A 219 4244 6251 6922 303 909 -721 C ATOM 1545 CE1 PHE A 219 -35.548 -11.619 -4.654 1.00 59.15 C ANISOU 1545 CE1 PHE A 219 6013 7772 8689 565 1327 -711 C ATOM 1546 CE2 PHE A 219 -33.519 -12.708 -5.366 1.00 50.03 C ANISOU 1546 CE2 PHE A 219 5064 6699 7247 359 1023 -699 C ATOM 1547 CZ PHE A 219 -34.204 -11.922 -4.443 1.00 56.01 C ANISOU 1547 CZ PHE A 219 5881 7374 8028 494 1222 -704 C ATOM 1548 N PHE A 220 -34.245 -12.356 -10.014 1.00 52.10 N ANISOU 1548 N PHE A 220 4742 7315 7740 381 243 -734 N ATOM 1549 CA PHE A 220 -32.886 -11.826 -10.161 1.00 56.92 C ANISOU 1549 CA PHE A 220 5605 7912 8109 368 186 -652 C ATOM 1550 C PHE A 220 -32.838 -10.694 -11.176 1.00 54.21 C ANISOU 1550 C PHE A 220 5288 7603 7707 495 31 -564 C ATOM 1551 O PHE A 220 -31.982 -9.812 -11.071 1.00 58.88 O ANISOU 1551 O PHE A 220 6060 8113 8198 506 50 -474 O ATOM 1552 CB PHE A 220 -31.886 -12.929 -10.558 1.00 58.64 C ANISOU 1552 CB PHE A 220 5890 8196 8194 249 123 -674 C ATOM 1553 CG PHE A 220 -31.416 -13.744 -9.401 1.00 54.46 C ANISOU 1553 CG PHE A 220 5464 7589 7638 150 285 -700 C ATOM 1554 CD1 PHE A 220 -31.916 -15.023 -9.190 1.00 53.84 C ANISOU 1554 CD1 PHE A 220 5274 7502 7679 71 362 -768 C ATOM 1555 CD2 PHE A 220 -30.502 -13.225 -8.499 1.00 43.92 C ANISOU 1555 CD2 PHE A 220 4342 6172 6174 149 353 -662 C ATOM 1556 CE1 PHE A 220 -31.498 -15.776 -8.100 1.00 55.59 C ANISOU 1556 CE1 PHE A 220 5630 7637 7855 14 534 -756 C ATOM 1557 CE2 PHE A 220 -30.080 -13.971 -7.417 1.00 43.82 C ANISOU 1557 CE2 PHE A 220 4456 6100 6093 106 475 -682 C ATOM 1558 CZ PHE A 220 -30.585 -15.256 -7.208 1.00 40.52 C ANISOU 1558 CZ PHE A 220 3960 5676 5760 49 582 -709 C ATOM 1559 N LEU A 221 -33.735 -10.706 -12.164 1.00 60.59 N ANISOU 1559 N LEU A 221 5919 8514 8587 600 -129 -587 N ATOM 1560 CA LEU A 221 -33.930 -9.525 -12.994 1.00 69.44 C ANISOU 1560 CA LEU A 221 7081 9647 9658 779 -252 -477 C ATOM 1561 C LEU A 221 -34.313 -8.324 -12.140 1.00 74.94 C ANISOU 1561 C LEU A 221 7822 10182 10470 865 -115 -426 C ATOM 1562 O LEU A 221 -33.644 -7.287 -12.170 1.00 81.94 O ANISOU 1562 O LEU A 221 8898 10957 11279 906 -87 -308 O ATOM 1563 CB LEU A 221 -35.005 -9.794 -14.041 1.00 81.07 C ANISOU 1563 CB LEU A 221 8339 11265 11198 915 -480 -546 C ATOM 1564 CG LEU A 221 -34.502 -10.332 -15.371 1.00 86.06 C ANISOU 1564 CG LEU A 221 9041 12056 11602 956 -690 -546 C ATOM 1565 CD1 LEU A 221 -35.665 -10.438 -16.337 1.00 88.23 C ANISOU 1565 CD1 LEU A 221 9115 12470 11939 1138 -973 -646 C ATOM 1566 CD2 LEU A 221 -33.421 -9.409 -15.891 1.00 87.68 C ANISOU 1566 CD2 LEU A 221 9522 12226 11565 1025 -648 -336 C ATOM 1567 N SER A 222 -35.392 -8.461 -11.356 1.00 74.03 N ANISOU 1567 N SER A 222 7528 10034 10567 892 -7 -519 N ATOM 1568 CA SER A 222 -35.881 -7.371 -10.506 1.00 69.55 C ANISOU 1568 CA SER A 222 6999 9316 10111 1007 143 -499 C ATOM 1569 C SER A 222 -34.795 -6.774 -9.615 1.00 71.98 C ANISOU 1569 C SER A 222 7597 9462 10288 939 274 -468 C ATOM 1570 O SER A 222 -34.734 -5.556 -9.442 1.00 87.41 O ANISOU 1570 O SER A 222 9675 11271 12265 1046 297 -416 O ATOM 1571 CB SER A 222 -37.027 -7.872 -9.656 1.00 59.43 C ANISOU 1571 CB SER A 222 5492 8029 9061 1015 317 -605 C ATOM 1572 OG SER A 222 -38.129 -8.184 -10.467 1.00 66.22 O ANISOU 1572 OG SER A 222 6032 9007 10122 1098 164 -657 O ATOM 1573 N ILE A 223 -33.929 -7.608 -9.044 1.00 69.58 N ANISOU 1573 N ILE A 223 7402 9168 9866 772 339 -513 N ATOM 1574 CA ILE A 223 -32.804 -7.116 -8.254 1.00 64.49 C ANISOU 1574 CA ILE A 223 7012 8388 9104 708 394 -519 C ATOM 1575 C ILE A 223 -31.862 -6.276 -9.093 1.00 78.28 C ANISOU 1575 C ILE A 223 8868 10073 10800 697 267 -408 C ATOM 1576 O ILE A 223 -31.128 -5.441 -8.557 1.00 87.57 O ANISOU 1576 O ILE A 223 10213 11081 11979 675 288 -416 O ATOM 1577 CB ILE A 223 -32.074 -8.319 -7.605 1.00 67.91 C ANISOU 1577 CB ILE A 223 7516 8872 9415 559 446 -582 C ATOM 1578 CG1 ILE A 223 -32.921 -8.876 -6.479 1.00 72.37 C ANISOU 1578 CG1 ILE A 223 8053 9420 10024 594 654 -657 C ATOM 1579 CG2 ILE A 223 -30.706 -7.954 -7.082 1.00 77.99 C ANISOU 1579 CG2 ILE A 223 9013 10049 10571 485 405 -601 C ATOM 1580 CD1 ILE A 223 -33.783 -7.800 -5.808 1.00 68.16 C ANISOU 1580 CD1 ILE A 223 7543 8770 9583 760 786 -686 C ATOM 1581 N THR A 224 -31.854 -6.479 -10.411 1.00 85.08 N ANISOU 1581 N THR A 224 9646 11059 11623 718 143 -309 N ATOM 1582 CA THR A 224 -31.040 -5.639 -11.285 1.00 84.98 C ANISOU 1582 CA THR A 224 9745 10977 11565 735 85 -155 C ATOM 1583 C THR A 224 -31.723 -4.302 -11.586 1.00 73.47 C ANISOU 1583 C THR A 224 8316 9384 10213 920 80 -54 C ATOM 1584 O THR A 224 -31.071 -3.253 -11.607 1.00 73.63 O ANISOU 1584 O THR A 224 8480 9208 10286 919 120 42 O ATOM 1585 CB THR A 224 -30.721 -6.404 -12.565 1.00 92.40 C ANISOU 1585 CB THR A 224 10639 12108 12360 726 -19 -79 C ATOM 1586 OG1 THR A 224 -29.874 -7.525 -12.252 1.00 87.62 O ANISOU 1586 OG1 THR A 224 10038 11581 11675 556 1 -161 O ATOM 1587 CG2 THR A 224 -30.047 -5.487 -13.587 1.00 96.48 C ANISOU 1587 CG2 THR A 224 11282 12560 12818 792 -24 130 C ATOM 1588 N VAL A 225 -33.042 -4.317 -11.774 1.00 69.70 N ANISOU 1588 N VAL A 225 7687 8988 9808 1082 34 -83 N ATOM 1589 CA VAL A 225 -33.820 -3.087 -11.932 1.00 82.40 C ANISOU 1589 CA VAL A 225 9306 10465 11538 1295 28 -4 C ATOM 1590 C VAL A 225 -34.018 -2.327 -10.604 1.00 89.69 C ANISOU 1590 C VAL A 225 10307 11168 12602 1313 181 -107 C ATOM 1591 O VAL A 225 -34.118 -1.094 -10.606 1.00 93.82 O ANISOU 1591 O VAL A 225 10938 11485 13224 1441 205 -33 O ATOM 1592 CB VAL A 225 -35.168 -3.434 -12.590 1.00 82.73 C ANISOU 1592 CB VAL A 225 9112 10687 11636 1477 -106 -27 C ATOM 1593 CG1 VAL A 225 -36.054 -2.180 -12.779 1.00 84.97 C ANISOU 1593 CG1 VAL A 225 9384 10845 12057 1743 -132 59 C ATOM 1594 CG2 VAL A 225 -34.936 -4.139 -13.904 1.00 81.27 C ANISOU 1594 CG2 VAL A 225 8898 10711 11269 1490 -292 38 C ATOM 1595 N PHE A 226 -34.092 -3.012 -9.459 1.00 88.96 N ANISOU 1595 N PHE A 226 10191 11100 12509 1214 294 -274 N ATOM 1596 CA PHE A 226 -34.188 -2.343 -8.156 1.00 91.21 C ANISOU 1596 CA PHE A 226 10607 11190 12857 1257 441 -394 C ATOM 1597 C PHE A 226 -33.171 -2.894 -7.159 1.00 84.01 C ANISOU 1597 C PHE A 226 9855 10251 11813 1079 492 -515 C ATOM 1598 O PHE A 226 -33.555 -3.418 -6.107 1.00 91.67 O ANISOU 1598 O PHE A 226 10841 11251 12737 1093 627 -638 O ATOM 1599 CB PHE A 226 -35.586 -2.469 -7.546 1.00 98.55 C ANISOU 1599 CB PHE A 226 11373 12163 13907 1413 577 -482 C ATOM 1600 CG PHE A 226 -36.718 -2.601 -8.534 1.00102.30 C ANISOU 1600 CG PHE A 226 11569 12783 14518 1554 482 -411 C ATOM 1601 CD1 PHE A 226 -37.108 -1.535 -9.324 1.00104.66 C ANISOU 1601 CD1 PHE A 226 11862 13000 14904 1750 373 -295 C ATOM 1602 CD2 PHE A 226 -37.453 -3.778 -8.600 1.00 99.52 C ANISOU 1602 CD2 PHE A 226 10952 12627 14234 1508 499 -474 C ATOM 1603 CE1 PHE A 226 -38.171 -1.662 -10.195 1.00106.01 C ANISOU 1603 CE1 PHE A 226 11773 13318 15188 1916 238 -253 C ATOM 1604 CE2 PHE A 226 -38.514 -3.911 -9.477 1.00 99.53 C ANISOU 1604 CE2 PHE A 226 10661 12758 14397 1640 363 -456 C ATOM 1605 CZ PHE A 226 -38.873 -2.853 -10.273 1.00103.54 C ANISOU 1605 CZ PHE A 226 11170 13217 14955 1857 213 -352 C ATOM 1606 N PRO A 227 -31.866 -2.760 -7.428 1.00 57.47 N ANISOU 1606 N PRO A 227 6615 6825 8395 931 397 -476 N ATOM 1607 CA PRO A 227 -30.872 -3.261 -6.454 1.00 60.73 C ANISOU 1607 CA PRO A 227 7165 7216 8695 790 397 -611 C ATOM 1608 C PRO A 227 -30.925 -2.534 -5.115 1.00 63.40 C ANISOU 1608 C PRO A 227 7697 7362 9030 875 460 -787 C ATOM 1609 O PRO A 227 -30.494 -3.083 -4.098 1.00 72.56 O ANISOU 1609 O PRO A 227 8982 8545 10043 839 474 -926 O ATOM 1610 CB PRO A 227 -29.521 -3.039 -7.161 1.00 62.34 C ANISOU 1610 CB PRO A 227 7402 7361 8924 634 280 -525 C ATOM 1611 CG PRO A 227 -29.792 -1.931 -8.136 1.00 65.98 C ANISOU 1611 CG PRO A 227 7848 7694 9527 724 272 -359 C ATOM 1612 CD PRO A 227 -31.241 -2.117 -8.592 1.00 64.65 C ANISOU 1612 CD PRO A 227 7542 7667 9356 905 304 -302 C ATOM 1613 N PHE A 228 -31.444 -1.311 -5.087 1.00 65.39 N ANISOU 1613 N PHE A 228 8002 7420 9422 1014 491 -792 N ATOM 1614 CA PHE A 228 -31.696 -0.640 -3.826 1.00 78.88 C ANISOU 1614 CA PHE A 228 9905 8953 11111 1143 567 -986 C ATOM 1615 C PHE A 228 -32.661 -1.411 -2.933 1.00 92.77 C ANISOU 1615 C PHE A 228 11656 10859 12732 1268 762 -1065 C ATOM 1616 O PHE A 228 -32.889 -0.995 -1.793 1.00 98.80 O ANISOU 1616 O PHE A 228 12617 11511 13411 1407 862 -1232 O ATOM 1617 CB PHE A 228 -32.237 0.744 -4.110 1.00 69.11 C ANISOU 1617 CB PHE A 228 8700 7483 10077 1296 587 -954 C ATOM 1618 CG PHE A 228 -33.456 0.755 -4.971 1.00 68.30 C ANISOU 1618 CG PHE A 228 8381 7491 10077 1444 657 -789 C ATOM 1619 CD1 PHE A 228 -34.723 0.605 -4.411 1.00 75.30 C ANISOU 1619 CD1 PHE A 228 9183 8452 10978 1635 830 -851 C ATOM 1620 CD2 PHE A 228 -33.347 0.934 -6.343 1.00 69.36 C ANISOU 1620 CD2 PHE A 228 8396 7658 10299 1415 552 -572 C ATOM 1621 CE1 PHE A 228 -35.869 0.620 -5.205 1.00 83.82 C ANISOU 1621 CE1 PHE A 228 10012 9636 12201 1780 855 -724 C ATOM 1622 CE2 PHE A 228 -34.484 0.955 -7.149 1.00 84.01 C ANISOU 1622 CE2 PHE A 228 10057 9628 12233 1588 558 -442 C ATOM 1623 CZ PHE A 228 -35.749 0.799 -6.577 1.00 90.14 C ANISOU 1623 CZ PHE A 228 10703 10478 13069 1764 688 -531 C ATOM 1624 N LEU A 229 -33.238 -2.509 -3.427 1.00 91.54 N ANISOU 1624 N LEU A 229 11281 10934 12564 1229 832 -954 N ATOM 1625 CA LEU A 229 -34.111 -3.379 -2.651 1.00 80.20 C ANISOU 1625 CA LEU A 229 9796 9622 11053 1308 1060 -992 C ATOM 1626 C LEU A 229 -33.371 -4.534 -1.995 1.00 70.87 C ANISOU 1626 C LEU A 229 8737 8542 9647 1190 1075 -1034 C ATOM 1627 O LEU A 229 -33.942 -5.211 -1.135 1.00 86.82 O ANISOU 1627 O LEU A 229 10799 10620 11569 1267 1304 -1059 O ATOM 1628 CB LEU A 229 -35.220 -3.939 -3.534 1.00 79.03 C ANISOU 1628 CB LEU A 229 9307 9633 11090 1324 1120 -870 C ATOM 1629 CG LEU A 229 -36.282 -3.025 -4.131 1.00 80.73 C ANISOU 1629 CG LEU A 229 9342 9796 11537 1500 1129 -819 C ATOM 1630 CD1 LEU A 229 -37.377 -3.877 -4.755 1.00 84.67 C ANISOU 1630 CD1 LEU A 229 9477 10480 12213 1507 1175 -757 C ATOM 1631 CD2 LEU A 229 -36.868 -2.048 -3.125 1.00 84.28 C ANISOU 1631 CD2 LEU A 229 9933 10072 12016 1719 1317 -926 C ATOM 1632 N ILE A 230 -32.124 -4.768 -2.374 1.00 50.63 N ANISOU 1632 N ILE A 230 6231 5992 7014 1023 861 -1027 N ATOM 1633 CA ILE A 230 -31.311 -5.812 -1.723 1.00 48.26 C ANISOU 1633 CA ILE A 230 6064 5774 6498 939 839 -1072 C ATOM 1634 C ILE A 230 -31.160 -5.590 -0.217 1.00 63.16 C ANISOU 1634 C ILE A 230 8271 7572 8156 1090 916 -1236 C ATOM 1635 O ILE A 230 -31.318 -6.559 0.546 1.00 60.18 O ANISOU 1635 O ILE A 230 7996 7281 7588 1140 1072 -1228 O ATOM 1636 CB ILE A 230 -29.967 -5.952 -2.410 1.00 55.04 C ANISOU 1636 CB ILE A 230 6901 6648 7363 757 590 -1049 C ATOM 1637 CG1 ILE A 230 -30.116 -6.625 -3.772 1.00 62.28 C ANISOU 1637 CG1 ILE A 230 7556 7713 8394 639 556 -888 C ATOM 1638 CG2 ILE A 230 -28.955 -6.787 -1.554 1.00 50.05 C ANISOU 1638 CG2 ILE A 230 6447 6061 6507 716 513 -1136 C ATOM 1639 CD1 ILE A 230 -28.852 -7.302 -4.209 1.00 54.63 C ANISOU 1639 CD1 ILE A 230 6576 6816 7366 481 402 -863 C ATOM 1640 N PRO A 231 -30.812 -4.389 0.270 1.00 65.73 N ANISOU 1640 N PRO A 231 8786 7715 8474 1175 809 -1391 N ATOM 1641 CA PRO A 231 -30.645 -4.259 1.724 1.00 69.68 C ANISOU 1641 CA PRO A 231 9631 8150 8696 1352 849 -1580 C ATOM 1642 C PRO A 231 -31.946 -4.497 2.440 1.00 64.37 C ANISOU 1642 C PRO A 231 9015 7520 7923 1563 1215 -1549 C ATOM 1643 O PRO A 231 -31.949 -4.964 3.579 1.00 64.54 O ANISOU 1643 O PRO A 231 9308 7573 7641 1714 1349 -1617 O ATOM 1644 CB PRO A 231 -30.148 -2.814 1.918 1.00 76.41 C ANISOU 1644 CB PRO A 231 10628 8763 9640 1392 647 -1774 C ATOM 1645 CG PRO A 231 -29.979 -2.245 0.523 1.00 74.45 C ANISOU 1645 CG PRO A 231 10106 8449 9732 1216 531 -1636 C ATOM 1646 CD PRO A 231 -30.834 -3.066 -0.388 1.00 55.57 C ANISOU 1646 CD PRO A 231 7434 6253 7428 1170 701 -1401 C ATOM 1647 N ILE A 232 -33.061 -4.195 1.782 1.00 53.46 N ANISOU 1647 N ILE A 232 7377 6140 6794 1592 1388 -1438 N ATOM 1648 CA ILE A 232 -34.373 -4.432 2.365 1.00 56.18 C ANISOU 1648 CA ILE A 232 7689 6524 7135 1778 1772 -1393 C ATOM 1649 C ILE A 232 -34.607 -5.919 2.605 1.00 56.94 C ANISOU 1649 C ILE A 232 7720 6778 7135 1718 1987 -1256 C ATOM 1650 O ILE A 232 -35.093 -6.327 3.674 1.00 57.14 O ANISOU 1650 O ILE A 232 7934 6813 6964 1888 2304 -1253 O ATOM 1651 CB ILE A 232 -35.444 -3.836 1.452 1.00 67.99 C ANISOU 1651 CB ILE A 232 8850 8000 8984 1806 1846 -1305 C ATOM 1652 CG1 ILE A 232 -35.172 -2.343 1.321 1.00 75.31 C ANISOU 1652 CG1 ILE A 232 9897 8722 9993 1890 1661 -1427 C ATOM 1653 CG2 ILE A 232 -36.782 -4.134 2.000 1.00 75.05 C ANISOU 1653 CG2 ILE A 232 9634 8937 9946 1979 2250 -1257 C ATOM 1654 CD1 ILE A 232 -35.591 -1.777 0.029 1.00 70.93 C ANISOU 1654 CD1 ILE A 232 9047 8145 9759 1842 1545 -1307 C ATOM 1655 N LEU A 233 -34.301 -6.746 1.598 1.00 52.19 N ANISOU 1655 N LEU A 233 6864 6286 6681 1488 1845 -1133 N ATOM 1656 CA LEU A 233 -34.432 -8.186 1.747 1.00 53.99 C ANISOU 1656 CA LEU A 233 7029 6623 6861 1405 2020 -1011 C ATOM 1657 C LEU A 233 -33.559 -8.700 2.884 1.00 56.49 C ANISOU 1657 C LEU A 233 7742 6936 6787 1485 2026 -1059 C ATOM 1658 O LEU A 233 -34.005 -9.526 3.691 1.00 54.50 O ANISOU 1658 O LEU A 233 7609 6703 6394 1581 2345 -973 O ATOM 1659 CB LEU A 233 -34.081 -8.882 0.415 1.00 48.83 C ANISOU 1659 CB LEU A 233 6077 6068 6408 1158 1798 -919 C ATOM 1660 CG LEU A 233 -34.925 -8.393 -0.771 1.00 52.49 C ANISOU 1660 CG LEU A 233 6176 6558 7212 1117 1738 -877 C ATOM 1661 CD1 LEU A 233 -34.455 -8.882 -2.161 1.00 46.08 C ANISOU 1661 CD1 LEU A 233 5138 5845 6524 918 1465 -817 C ATOM 1662 CD2 LEU A 233 -36.421 -8.685 -0.567 1.00 55.82 C ANISOU 1662 CD2 LEU A 233 6351 6992 7867 1203 2073 -825 C ATOM 1663 N GLU A 234 -32.318 -8.218 2.971 1.00 51.58 N ANISOU 1663 N GLU A 234 7322 6277 5998 1459 1680 -1191 N ATOM 1664 CA GLU A 234 -31.432 -8.650 4.053 1.00 60.75 C ANISOU 1664 CA GLU A 234 8862 7444 6776 1568 1609 -1268 C ATOM 1665 C GLU A 234 -32.047 -8.355 5.411 1.00 63.18 C ANISOU 1665 C GLU A 234 9514 7699 6792 1870 1897 -1336 C ATOM 1666 O GLU A 234 -31.982 -9.182 6.328 1.00 71.09 O ANISOU 1666 O GLU A 234 10785 8742 7483 2010 2078 -1275 O ATOM 1667 CB GLU A 234 -30.070 -7.961 3.941 1.00 63.74 C ANISOU 1667 CB GLU A 234 9349 7768 7101 1502 1162 -1449 C ATOM 1668 CG GLU A 234 -29.285 -8.325 2.698 1.00 65.82 C ANISOU 1668 CG GLU A 234 9322 8090 7597 1232 911 -1371 C ATOM 1669 CD GLU A 234 -28.467 -9.606 2.884 1.00 74.00 C ANISOU 1669 CD GLU A 234 10427 9229 8460 1182 832 -1309 C ATOM 1670 OE1 GLU A 234 -28.711 -10.360 3.873 1.00 73.30 O ANISOU 1670 OE1 GLU A 234 10582 9170 8097 1345 1028 -1266 O ATOM 1671 OE2 GLU A 234 -27.568 -9.843 2.047 1.00 71.97 O ANISOU 1671 OE2 GLU A 234 9994 9012 8339 999 593 -1291 O ATOM 1672 N VAL A 235 -32.687 -7.198 5.546 1.00 57.91 N ANISOU 1672 N VAL A 235 8858 6935 6210 1998 1973 -1446 N ATOM 1673 CA VAL A 235 -33.203 -6.840 6.848 1.00 69.61 C ANISOU 1673 CA VAL A 235 10706 8364 7379 2318 2245 -1539 C ATOM 1674 C VAL A 235 -34.387 -7.733 7.191 1.00 74.66 C ANISOU 1674 C VAL A 235 11263 9065 8039 2405 2785 -1315 C ATOM 1675 O VAL A 235 -34.683 -7.941 8.370 1.00 80.28 O ANISOU 1675 O VAL A 235 12329 9772 8401 2673 3093 -1308 O ATOM 1676 CB VAL A 235 -33.503 -5.318 6.885 1.00 70.42 C ANISOU 1676 CB VAL A 235 10851 8318 7586 2441 2165 -1741 C ATOM 1677 CG1 VAL A 235 -34.161 -4.874 8.174 1.00 66.95 C ANISOU 1677 CG1 VAL A 235 10127 7859 7452 2504 2533 -1630 C ATOM 1678 CG2 VAL A 235 -32.250 -4.524 6.688 1.00 79.68 C ANISOU 1678 CG2 VAL A 235 12538 9413 8325 2749 2146 -1981 C ATOM 1679 N LEU A 236 -35.044 -8.315 6.190 1.00 65.53 N ANISOU 1679 N LEU A 236 9651 7960 7287 2188 2909 -1132 N ATOM 1680 CA LEU A 236 -36.134 -9.248 6.426 1.00 63.02 C ANISOU 1680 CA LEU A 236 9176 7673 7097 2213 3409 -922 C ATOM 1681 C LEU A 236 -35.668 -10.704 6.511 1.00 72.73 C ANISOU 1681 C LEU A 236 10455 8956 8224 2091 3467 -753 C ATOM 1682 O LEU A 236 -36.512 -11.603 6.556 1.00 74.21 O ANISOU 1682 O LEU A 236 10456 9136 8604 2048 3868 -561 O ATOM 1683 CB LEU A 236 -37.180 -9.099 5.330 1.00 62.15 C ANISOU 1683 CB LEU A 236 8519 7572 7523 2060 3490 -851 C ATOM 1684 CG LEU A 236 -37.777 -7.682 5.213 1.00 69.76 C ANISOU 1684 CG LEU A 236 9409 8466 8631 2210 3471 -986 C ATOM 1685 CD1 LEU A 236 -38.562 -7.487 3.931 1.00 70.15 C ANISOU 1685 CD1 LEU A 236 8922 8543 9187 2058 3389 -932 C ATOM 1686 CD2 LEU A 236 -38.663 -7.424 6.393 1.00 67.70 C ANISOU 1686 CD2 LEU A 236 9347 8152 8224 2516 3965 -985 C ATOM 1687 N ASN A 237 -34.355 -10.952 6.508 1.00 60.32 N ANISOU 1687 N ASN A 237 9100 7417 6401 2030 3079 -821 N ATOM 1688 CA ASN A 237 -33.810 -12.306 6.618 1.00 77.68 C ANISOU 1688 CA ASN A 237 11382 9651 8480 1948 3102 -670 C ATOM 1689 C ASN A 237 -34.249 -13.164 5.450 1.00 75.94 C ANISOU 1689 C ASN A 237 10685 9452 8718 1653 3144 -529 C ATOM 1690 O ASN A 237 -34.462 -14.367 5.586 1.00 89.09 O ANISOU 1690 O ASN A 237 12324 11093 10432 1596 3394 -352 O ATOM 1691 CB ASN A 237 -34.199 -12.970 7.940 1.00 82.90 C ANISOU 1691 CB ASN A 237 12422 10278 8798 2209 3563 -524 C ATOM 1692 CG ASN A 237 -33.651 -12.219 9.133 1.00 96.29 C ANISOU 1692 CG ASN A 237 14660 11971 9954 2541 3464 -695 C ATOM 1693 OD1 ASN A 237 -32.440 -11.976 9.220 1.00107.52 O ANISOU 1693 OD1 ASN A 237 16292 13426 11136 2558 2992 -863 O ATOM 1694 ND2 ASN A 237 -34.537 -11.816 10.045 1.00 92.24 N ANISOU 1694 ND2 ASN A 237 14332 11418 9297 2783 3847 -664 N ATOM 1695 N ILE A 238 -34.427 -12.531 4.316 1.00 59.91 N ANISOU 1695 N ILE A 238 8293 7449 7021 1486 2906 -610 N ATOM 1696 CA ILE A 238 -34.665 -13.222 3.075 1.00 58.59 C ANISOU 1696 CA ILE A 238 7701 7321 7240 1222 2815 -539 C ATOM 1697 C ILE A 238 -33.314 -13.535 2.455 1.00 61.42 C ANISOU 1697 C ILE A 238 8111 7737 7491 1078 2390 -588 C ATOM 1698 O ILE A 238 -32.427 -12.678 2.397 1.00 58.63 O ANISOU 1698 O ILE A 238 7899 7398 6981 1108 2070 -718 O ATOM 1699 CB ILE A 238 -35.525 -12.370 2.141 1.00 53.10 C ANISOU 1699 CB ILE A 238 6623 6641 6910 1164 2753 -597 C ATOM 1700 CG1 ILE A 238 -36.935 -12.290 2.724 1.00 55.97 C ANISOU 1700 CG1 ILE A 238 6857 6950 7459 1295 3220 -531 C ATOM 1701 CG2 ILE A 238 -35.479 -12.973 0.718 1.00 50.21 C ANISOU 1701 CG2 ILE A 238 5881 6343 6855 913 2510 -577 C ATOM 1702 CD1 ILE A 238 -37.817 -11.394 1.991 1.00 56.27 C ANISOU 1702 CD1 ILE A 238 6549 6999 7831 1303 3169 -592 C ATOM 1703 N CYS A 239 -33.132 -14.766 2.029 1.00 52.87 N ANISOU 1703 N CYS A 239 6910 6666 6511 927 2403 -490 N ATOM 1704 CA CYS A 239 -31.830 -15.170 1.531 1.00 52.02 C ANISOU 1704 CA CYS A 239 6863 6612 6290 822 2049 -527 C ATOM 1705 C CYS A 239 -31.998 -15.993 0.260 1.00 50.98 C ANISOU 1705 C CYS A 239 6378 6515 6478 596 1962 -491 C ATOM 1706 O CYS A 239 -32.958 -16.759 0.133 1.00 52.37 O ANISOU 1706 O CYS A 239 6353 6640 6904 525 2219 -410 O ATOM 1707 CB CYS A 239 -31.080 -15.948 2.608 1.00 56.44 C ANISOU 1707 CB CYS A 239 7801 7140 6502 953 2112 -466 C ATOM 1708 SG CYS A 239 -29.485 -16.574 1.994 1.00 70.66 S ANISOU 1708 SG CYS A 239 9624 9007 8218 839 1695 -508 S ATOM 1709 N VAL A 240 -31.053 -15.825 -0.675 1.00 53.61 N ANISOU 1709 N VAL A 240 6634 6925 6812 489 1606 -562 N ATOM 1710 CA VAL A 240 -31.101 -16.527 -1.953 1.00 62.66 C ANISOU 1710 CA VAL A 240 7491 8120 8196 310 1481 -560 C ATOM 1711 C VAL A 240 -30.782 -17.996 -1.777 1.00 64.58 C ANISOU 1711 C VAL A 240 7794 8313 8429 253 1573 -489 C ATOM 1712 O VAL A 240 -31.159 -18.803 -2.624 1.00 60.92 O ANISOU 1712 O VAL A 240 7096 7843 8206 116 1565 -494 O ATOM 1713 CB VAL A 240 -30.151 -15.931 -3.015 1.00 58.93 C ANISOU 1713 CB VAL A 240 6949 7742 7700 241 1128 -631 C ATOM 1714 CG1 VAL A 240 -30.714 -14.638 -3.562 1.00 62.49 C ANISOU 1714 CG1 VAL A 240 7261 8217 8265 268 1055 -671 C ATOM 1715 CG2 VAL A 240 -28.770 -15.744 -2.459 1.00 57.47 C ANISOU 1715 CG2 VAL A 240 7019 7561 7258 296 962 -662 C ATOM 1716 N PHE A 241 -30.106 -18.367 -0.698 1.00 57.81 N ANISOU 1716 N PHE A 241 7259 7409 7297 372 1643 -434 N ATOM 1717 CA PHE A 241 -29.912 -19.770 -0.374 1.00 61.07 C ANISOU 1717 CA PHE A 241 7770 7735 7698 357 1787 -330 C ATOM 1718 C PHE A 241 -31.073 -20.224 0.496 1.00 75.56 C ANISOU 1718 C PHE A 241 9650 9438 9622 413 2232 -197 C ATOM 1719 O PHE A 241 -31.259 -19.674 1.588 1.00 82.19 O ANISOU 1719 O PHE A 241 10742 10259 10227 598 2411 -153 O ATOM 1720 CB PHE A 241 -28.565 -19.974 0.325 1.00 58.52 C ANISOU 1720 CB PHE A 241 7778 7430 7026 493 1620 -323 C ATOM 1721 CG PHE A 241 -27.380 -19.633 -0.556 1.00 59.39 C ANISOU 1721 CG PHE A 241 7792 7653 7119 421 1227 -440 C ATOM 1722 CD1 PHE A 241 -26.764 -18.390 -0.480 1.00 55.93 C ANISOU 1722 CD1 PHE A 241 7403 7288 6560 472 995 -549 C ATOM 1723 CD2 PHE A 241 -26.916 -20.537 -1.505 1.00 56.91 C ANISOU 1723 CD2 PHE A 241 7323 7355 6946 300 1115 -445 C ATOM 1724 CE1 PHE A 241 -25.678 -18.060 -1.323 1.00 45.67 C ANISOU 1724 CE1 PHE A 241 5980 6071 5301 390 689 -632 C ATOM 1725 CE2 PHE A 241 -25.835 -20.218 -2.336 1.00 53.19 C ANISOU 1725 CE2 PHE A 241 6755 6989 6466 248 813 -533 C ATOM 1726 CZ PHE A 241 -25.233 -18.963 -2.251 1.00 48.12 C ANISOU 1726 CZ PHE A 241 6139 6416 5729 286 618 -614 C ATOM 1727 N PRO A 242 -31.904 -21.171 0.036 1.00 76.17 N ANISOU 1727 N PRO A 242 9475 9412 10053 261 2431 -143 N ATOM 1728 CA PRO A 242 -33.040 -21.653 0.840 1.00 74.83 C ANISOU 1728 CA PRO A 242 9296 9085 10050 288 2915 7 C ATOM 1729 C PRO A 242 -32.719 -21.864 2.309 1.00 76.88 C ANISOU 1729 C PRO A 242 10017 9269 9924 523 3191 176 C ATOM 1730 O PRO A 242 -31.832 -22.652 2.649 1.00 77.70 O ANISOU 1730 O PRO A 242 10385 9326 9810 588 3133 254 O ATOM 1731 CB PRO A 242 -33.406 -22.980 0.163 1.00 72.97 C ANISOU 1731 CB PRO A 242 8808 8707 10208 79 2995 32 C ATOM 1732 CG PRO A 242 -32.513 -23.105 -1.080 1.00 72.89 C ANISOU 1732 CG PRO A 242 8680 8814 10203 -37 2528 -132 C ATOM 1733 CD PRO A 242 -31.896 -21.763 -1.310 1.00 77.30 C ANISOU 1733 CD PRO A 242 9303 9573 10494 55 2216 -240 C ATOM 1734 N ARG A 243 -33.450 -21.158 3.180 1.00 73.97 N ANISOU 1734 N ARG A 243 9761 8892 9455 682 3492 230 N ATOM 1735 CA ARG A 243 -33.085 -21.086 4.593 1.00 87.43 C ANISOU 1735 CA ARG A 243 11972 10570 10678 974 3697 352 C ATOM 1736 C ARG A 243 -33.190 -22.443 5.279 1.00 81.11 C ANISOU 1736 C ARG A 243 11380 9582 9855 1024 4088 607 C ATOM 1737 O ARG A 243 -32.446 -22.724 6.227 1.00 83.64 O ANISOU 1737 O ARG A 243 12171 9891 9717 1266 4108 711 O ATOM 1738 CB ARG A 243 -33.972 -20.054 5.302 1.00104.23 C ANISOU 1738 CB ARG A 243 14158 12718 12727 1143 3980 345 C ATOM 1739 CG ARG A 243 -33.612 -19.767 6.762 1.00119.59 C ANISOU 1739 CG ARG A 243 16673 14666 14099 1498 4152 418 C ATOM 1740 CD ARG A 243 -32.226 -19.132 6.905 1.00129.24 C ANISOU 1740 CD ARG A 243 18191 16023 14893 1627 3613 230 C ATOM 1741 NE ARG A 243 -32.091 -17.828 6.246 1.00131.24 N ANISOU 1741 NE ARG A 243 18236 16386 15244 1549 3250 -16 N ATOM 1742 CZ ARG A 243 -31.021 -17.040 6.367 1.00129.94 C ANISOU 1742 CZ ARG A 243 18266 16310 14797 1640 2807 -210 C ATOM 1743 NH1 ARG A 243 -29.998 -17.415 7.128 1.00128.10 N ANISOU 1743 NH1 ARG A 243 18423 16095 14153 1825 2632 -212 N ATOM 1744 NH2 ARG A 243 -30.972 -15.868 5.740 1.00127.88 N ANISOU 1744 NH2 ARG A 243 17804 16102 14683 1554 2535 -402 N ATOM 1745 N GLU A 244 -34.115 -23.290 4.834 1.00 70.29 N ANISOU 1745 N GLU A 244 9674 8048 8985 811 4397 709 N ATOM 1746 CA GLU A 244 -34.246 -24.608 5.443 1.00 89.24 C ANISOU 1746 CA GLU A 244 12258 10216 11433 836 4807 973 C ATOM 1747 C GLU A 244 -33.011 -25.451 5.160 1.00 86.93 C ANISOU 1747 C GLU A 244 12151 9905 10973 827 4473 971 C ATOM 1748 O GLU A 244 -32.425 -26.053 6.069 1.00 88.02 O ANISOU 1748 O GLU A 244 12736 9961 10746 1049 4608 1161 O ATOM 1749 CB GLU A 244 -35.509 -25.298 4.922 1.00102.91 C ANISOU 1749 CB GLU A 244 13513 11745 13842 563 5171 1039 C ATOM 1750 CG GLU A 244 -35.682 -25.197 3.406 1.00112.78 C ANISOU 1750 CG GLU A 244 14228 13070 15552 259 4754 774 C ATOM 1751 CD GLU A 244 -36.476 -26.357 2.826 1.00127.63 C ANISOU 1751 CD GLU A 244 15715 14702 18075 -22 4971 809 C ATOM 1752 OE1 GLU A 244 -37.306 -26.945 3.558 1.00137.01 O ANISOU 1752 OE1 GLU A 244 16894 15657 19508 -27 5542 1035 O ATOM 1753 OE2 GLU A 244 -36.265 -26.688 1.638 1.00128.55 O ANISOU 1753 OE2 GLU A 244 15539 14843 18460 -233 4580 605 O ATOM 1754 N VAL A 245 -32.587 -25.481 3.901 1.00 83.63 N ANISOU 1754 N VAL A 245 11409 9572 10796 603 4032 760 N ATOM 1755 CA VAL A 245 -31.419 -26.266 3.526 1.00 82.96 C ANISOU 1755 CA VAL A 245 11450 9475 10595 594 3718 737 C ATOM 1756 C VAL A 245 -30.203 -25.823 4.333 1.00 79.89 C ANISOU 1756 C VAL A 245 11518 9230 9607 890 3467 739 C ATOM 1757 O VAL A 245 -29.506 -26.646 4.941 1.00 84.49 O ANISOU 1757 O VAL A 245 12438 9720 9944 1058 3500 889 O ATOM 1758 CB VAL A 245 -31.182 -26.159 2.009 1.00 74.07 C ANISOU 1758 CB VAL A 245 9913 8458 9774 343 3292 485 C ATOM 1759 CG1 VAL A 245 -29.940 -26.948 1.591 1.00 64.31 C ANISOU 1759 CG1 VAL A 245 8796 7218 8422 353 2986 450 C ATOM 1760 CG2 VAL A 245 -32.409 -26.659 1.257 1.00 74.96 C ANISOU 1760 CG2 VAL A 245 9582 8422 10477 75 3493 449 C ATOM 1761 N THR A 246 -29.951 -24.512 4.384 1.00 67.90 N ANISOU 1761 N THR A 246 10017 7920 7862 972 3206 569 N ATOM 1762 CA THR A 246 -28.765 -24.036 5.087 1.00 69.65 C ANISOU 1762 CA THR A 246 10619 8273 7573 1231 2895 510 C ATOM 1763 C THR A 246 -28.851 -24.335 6.571 1.00 72.04 C ANISOU 1763 C THR A 246 11429 8489 7454 1557 3218 722 C ATOM 1764 O THR A 246 -27.848 -24.688 7.195 1.00 78.82 O ANISOU 1764 O THR A 246 12647 9370 7930 1790 3028 762 O ATOM 1765 CB THR A 246 -28.568 -22.542 4.863 1.00 71.29 C ANISOU 1765 CB THR A 246 10731 8670 7686 1234 2580 275 C ATOM 1766 OG1 THR A 246 -29.712 -21.835 5.360 1.00 81.50 O ANISOU 1766 OG1 THR A 246 12025 9941 8999 1289 2914 305 O ATOM 1767 CG2 THR A 246 -28.381 -22.253 3.375 1.00 67.70 C ANISOU 1767 CG2 THR A 246 9828 8303 7591 951 2264 100 C ATOM 1768 N ASN A 247 -30.035 -24.189 7.160 1.00 74.48 N ANISOU 1768 N ASN A 247 11781 8707 7813 1607 3712 862 N ATOM 1769 CA ASN A 247 -30.179 -24.562 8.557 1.00 82.48 C ANISOU 1769 CA ASN A 247 13311 9624 8403 1942 4099 1106 C ATOM 1770 C ASN A 247 -29.962 -26.054 8.726 1.00 84.12 C ANISOU 1770 C ASN A 247 13676 9623 8663 1961 4319 1370 C ATOM 1771 O ASN A 247 -29.246 -26.484 9.638 1.00 83.09 O ANISOU 1771 O ASN A 247 14038 9475 8058 2280 4298 1510 O ATOM 1772 CB ASN A 247 -31.548 -24.142 9.085 1.00 94.46 C ANISOU 1772 CB ASN A 247 14800 11072 10020 1981 4657 1221 C ATOM 1773 CG ASN A 247 -31.677 -22.635 9.229 1.00105.35 C ANISOU 1773 CG ASN A 247 16175 12638 11215 2076 4464 979 C ATOM 1774 OD1 ASN A 247 -30.679 -21.906 9.226 1.00105.30 O ANISOU 1774 OD1 ASN A 247 16307 12794 10907 2174 3947 752 O ATOM 1775 ND2 ASN A 247 -32.910 -22.160 9.358 1.00111.50 N ANISOU 1775 ND2 ASN A 247 16775 13374 12214 2047 4886 1021 N ATOM 1776 N PHE A 248 -30.549 -26.857 7.837 1.00 82.00 N ANISOU 1776 N PHE A 248 12999 9184 8974 1637 4498 1427 N ATOM 1777 CA PHE A 248 -30.330 -28.297 7.898 1.00 84.74 C ANISOU 1777 CA PHE A 248 13468 9287 9443 1626 4692 1658 C ATOM 1778 C PHE A 248 -28.845 -28.615 7.904 1.00 81.40 C ANISOU 1778 C PHE A 248 13302 8958 8668 1798 4198 1592 C ATOM 1779 O PHE A 248 -28.366 -29.394 8.736 1.00 79.43 O ANISOU 1779 O PHE A 248 13494 8590 8097 2070 4326 1823 O ATOM 1780 CB PHE A 248 -31.012 -29.007 6.727 1.00 85.07 C ANISOU 1780 CB PHE A 248 12974 9151 10197 1218 4794 1614 C ATOM 1781 CG PHE A 248 -30.696 -30.476 6.654 1.00 90.17 C ANISOU 1781 CG PHE A 248 13720 9520 11020 1181 4929 1801 C ATOM 1782 CD1 PHE A 248 -31.375 -31.385 7.464 1.00 98.42 C ANISOU 1782 CD1 PHE A 248 14980 10248 12166 1253 5553 2155 C ATOM 1783 CD2 PHE A 248 -29.701 -30.947 5.809 1.00 90.56 C ANISOU 1783 CD2 PHE A 248 13670 9607 11133 1095 4465 1638 C ATOM 1784 CE1 PHE A 248 -31.083 -32.736 7.418 1.00 97.49 C ANISOU 1784 CE1 PHE A 248 14977 9833 12233 1227 5692 2341 C ATOM 1785 CE2 PHE A 248 -29.400 -32.303 5.757 1.00 95.34 C ANISOU 1785 CE2 PHE A 248 14385 9934 11906 1084 4591 1802 C ATOM 1786 CZ PHE A 248 -30.092 -33.197 6.562 1.00 95.20 C ANISOU 1786 CZ PHE A 248 14586 9579 12006 1146 5194 2152 C ATOM 1787 N LEU A 249 -28.093 -28.001 6.991 1.00 77.71 N ANISOU 1787 N LEU A 249 12564 8703 8260 1661 3640 1287 N ATOM 1788 CA LEU A 249 -26.670 -28.292 6.925 1.00 81.69 C ANISOU 1788 CA LEU A 249 13232 9299 8507 1807 3173 1207 C ATOM 1789 C LEU A 249 -25.908 -27.706 8.111 1.00 89.13 C ANISOU 1789 C LEU A 249 14659 10391 8814 2209 2970 1203 C ATOM 1790 O LEU A 249 -24.955 -28.332 8.595 1.00 93.89 O ANISOU 1790 O LEU A 249 15574 10978 9122 2459 2784 1284 O ATOM 1791 CB LEU A 249 -26.104 -27.784 5.600 1.00 80.83 C ANISOU 1791 CB LEU A 249 12682 9364 8668 1549 2694 901 C ATOM 1792 CG LEU A 249 -26.640 -28.486 4.340 1.00 78.67 C ANISOU 1792 CG LEU A 249 11971 8959 8961 1199 2783 859 C ATOM 1793 CD1 LEU A 249 -26.099 -27.833 3.069 1.00 73.00 C ANISOU 1793 CD1 LEU A 249 10875 8445 8416 999 2333 570 C ATOM 1794 CD2 LEU A 249 -26.342 -29.986 4.332 1.00 73.82 C ANISOU 1794 CD2 LEU A 249 11477 8100 8471 1223 2921 1032 C ATOM 1795 N ARG A 250 -26.322 -26.535 8.610 1.00 87.23 N ANISOU 1795 N ARG A 250 14500 10287 8358 2298 2990 1097 N ATOM 1796 CA ARG A 250 -25.587 -25.871 9.686 1.00 90.73 C ANISOU 1796 CA ARG A 250 15392 10882 8200 2678 2722 1017 C ATOM 1797 C ARG A 250 -25.564 -26.716 10.942 1.00 91.87 C ANISOU 1797 C ARG A 250 16118 10898 7890 3069 3028 1325 C ATOM 1798 O ARG A 250 -24.531 -26.834 11.614 1.00 98.99 O ANISOU 1798 O ARG A 250 17390 11883 8339 3400 2684 1300 O ATOM 1799 CB ARG A 250 -26.210 -24.518 10.001 1.00 98.26 C ANISOU 1799 CB ARG A 250 16343 11955 9038 2703 2765 853 C ATOM 1800 CG ARG A 250 -25.575 -23.373 9.279 1.00100.11 C ANISOU 1800 CG ARG A 250 16269 12376 9393 2542 2228 498 C ATOM 1801 CD ARG A 250 -26.291 -22.085 9.575 1.00101.81 C ANISOU 1801 CD ARG A 250 16487 12660 9538 2567 2317 353 C ATOM 1802 NE ARG A 250 -25.963 -21.551 10.891 1.00103.55 N ANISOU 1802 NE ARG A 250 17236 12945 9161 2974 2224 288 N ATOM 1803 CZ ARG A 250 -26.315 -20.333 11.275 1.00104.10 C ANISOU 1803 CZ ARG A 250 17387 13083 9084 3064 2189 96 C ATOM 1804 NH1 ARG A 250 -26.995 -19.564 10.436 1.00 97.50 N ANISOU 1804 NH1 ARG A 250 16128 12250 8667 2775 2253 -15 N ATOM 1805 NH2 ARG A 250 -25.991 -19.891 12.481 1.00114.34 N ANISOU 1805 NH2 ARG A 250 19159 14427 9858 3435 2054 10 N ATOM 1806 N LYS A 251 -26.712 -27.279 11.300 1.00 92.93 N ANISOU 1806 N LYS A 251 16342 10826 8140 3055 3682 1623 N ATOM 1807 CA LYS A 251 -26.757 -28.146 12.464 1.00111.08 C ANISOU 1807 CA LYS A 251 19149 12955 10100 3402 4003 1947 C ATOM 1808 C LYS A 251 -26.129 -29.496 12.152 1.00110.58 C ANISOU 1808 C LYS A 251 19165 12723 10126 3410 4003 2153 C ATOM 1809 O LYS A 251 -25.458 -30.088 13.006 1.00106.27 O ANISOU 1809 O LYS A 251 19009 12125 9242 3754 3872 2270 O ATOM 1810 CB LYS A 251 -28.202 -28.299 12.940 1.00126.48 C ANISOU 1810 CB LYS A 251 21028 14697 12332 3328 4633 2156 C ATOM 1811 CG LYS A 251 -29.170 -28.685 11.831 1.00132.88 C ANISOU 1811 CG LYS A 251 21315 15350 13822 2874 5014 2219 C ATOM 1812 CD LYS A 251 -30.623 -28.576 12.273 1.00141.38 C ANISOU 1812 CD LYS A 251 22238 16265 15216 2793 5547 2349 C ATOM 1813 CE LYS A 251 -31.567 -29.094 11.190 1.00141.09 C ANISOU 1813 CE LYS A 251 21633 16043 15931 2341 5864 2384 C ATOM 1814 NZ LYS A 251 -31.325 -30.536 10.865 1.00141.85 N ANISOU 1814 NZ LYS A 251 21722 15868 16307 2233 6011 2584 N ATOM 1815 N SER A 252 -26.330 -29.995 10.929 1.00106.75 N ANISOU 1815 N SER A 252 18166 12126 10269 2992 4008 2097 N ATOM 1816 CA SER A 252 -25.659 -31.222 10.527 1.00106.87 C ANISOU 1816 CA SER A 252 18175 11971 10460 2969 3906 2210 C ATOM 1817 C SER A 252 -24.155 -31.071 10.655 1.00 98.25 C ANISOU 1817 C SER A 252 17259 11088 8985 3229 3253 2032 C ATOM 1818 O SER A 252 -23.484 -31.955 11.199 1.00 97.26 O ANISOU 1818 O SER A 252 17500 10856 8599 3527 3214 2229 O ATOM 1819 CB SER A 252 -26.043 -31.602 9.098 1.00110.37 C ANISOU 1819 CB SER A 252 18009 12306 11621 2482 3902 2074 C ATOM 1820 OG SER A 252 -27.426 -31.899 9.007 1.00116.98 O ANISOU 1820 OG SER A 252 18658 12912 12876 2247 4496 2242 O ATOM 1821 N VAL A 253 -23.611 -29.935 10.203 1.00 86.69 N ANISOU 1821 N VAL A 253 15537 9909 7492 3138 2741 1668 N ATOM 1822 CA VAL A 253 -22.176 -29.719 10.353 1.00 86.41 C ANISOU 1822 CA VAL A 253 15611 10070 7151 3372 2114 1475 C ATOM 1823 C VAL A 253 -21.828 -29.578 11.823 1.00 91.05 C ANISOU 1823 C VAL A 253 16831 10720 7043 3891 2058 1585 C ATOM 1824 O VAL A 253 -20.883 -30.209 12.315 1.00 82.93 O ANISOU 1824 O VAL A 253 16106 9690 5715 4220 1797 1662 O ATOM 1825 CB VAL A 253 -21.702 -28.505 9.538 1.00 77.90 C ANISOU 1825 CB VAL A 253 14096 9245 6258 3135 1627 1075 C ATOM 1826 CG1 VAL A 253 -20.297 -28.099 9.978 1.00 75.66 C ANISOU 1826 CG1 VAL A 253 13961 9162 5626 3421 1006 866 C ATOM 1827 CG2 VAL A 253 -21.701 -28.851 8.050 1.00 68.73 C ANISOU 1827 CG2 VAL A 253 12380 8040 5693 2717 1582 974 C ATOM 1828 N LYS A 254 -22.615 -28.784 12.556 1.00 99.67 N ANISOU 1828 N LYS A 254 18153 11864 7852 4003 2313 1597 N ATOM 1829 CA LYS A 254 -22.411 -28.691 13.999 1.00106.55 C ANISOU 1829 CA LYS A 254 19496 12747 8241 4441 2251 1637 C ATOM 1830 C LYS A 254 -22.490 -30.058 14.680 1.00107.93 C ANISOU 1830 C LYS A 254 19987 12668 8353 4671 2597 1993 C ATOM 1831 O LYS A 254 -21.784 -30.295 15.669 1.00 99.62 O ANISOU 1831 O LYS A 254 19283 11642 6926 5064 2351 1987 O ATOM 1832 CB LYS A 254 -23.422 -27.721 14.611 1.00110.60 C ANISOU 1832 CB LYS A 254 20056 13283 8685 4442 2523 1579 C ATOM 1833 CG LYS A 254 -23.263 -27.485 16.103 1.00114.25 C ANISOU 1833 CG LYS A 254 20780 13506 9124 4589 3154 1913 C ATOM 1834 CD LYS A 254 -24.280 -26.479 16.578 1.00123.34 C ANISOU 1834 CD LYS A 254 22146 14733 9986 4803 3189 1805 C ATOM 1835 CE LYS A 254 -24.140 -26.259 18.074 1.00129.62 C ANISOU 1835 CE LYS A 254 23263 15695 10293 5191 2583 1572 C ATOM 1836 NZ LYS A 254 -25.132 -25.270 18.576 1.00132.97 N ANISOU 1836 NZ LYS A 254 23933 16173 10415 5425 2607 1460 N ATOM 1837 N ARG A 255 -23.325 -30.970 14.169 1.00113.06 N ANISOU 1837 N ARG A 255 20503 13058 9395 4429 3158 2284 N ATOM 1838 CA ARG A 255 -23.397 -32.311 14.749 1.00123.48 C ANISOU 1838 CA ARG A 255 22093 14102 10721 4618 3501 2612 C ATOM 1839 C ARG A 255 -22.149 -33.120 14.412 1.00117.29 C ANISOU 1839 C ARG A 255 21363 13315 9885 4748 3091 2615 C ATOM 1840 O ARG A 255 -21.541 -33.737 15.294 1.00113.60 O ANISOU 1840 O ARG A 255 21247 12806 9112 5123 2984 2707 O ATOM 1841 CB ARG A 255 -24.655 -33.048 14.263 1.00135.41 C ANISOU 1841 CB ARG A 255 23376 15300 12774 4279 4195 2881 C ATOM 1842 CG ARG A 255 -25.989 -32.556 14.858 1.00149.11 C ANISOU 1842 CG ARG A 255 25095 16963 14597 4229 4706 2958 C ATOM 1843 CD ARG A 255 -27.196 -33.418 14.413 1.00152.64 C ANISOU 1843 CD ARG A 255 25256 17070 15669 3893 5362 3203 C ATOM 1844 NE ARG A 255 -28.491 -32.860 14.826 1.00149.50 N ANISOU 1844 NE ARG A 255 24741 16623 15439 3808 5807 3242 N ATOM 1845 CZ ARG A 255 -29.363 -32.283 14.000 1.00141.61 C ANISOU 1845 CZ ARG A 255 23267 15645 14895 3418 5956 3122 C ATOM 1846 NH1 ARG A 255 -29.095 -32.188 12.700 1.00137.02 N ANISOU 1846 NH1 ARG A 255 22296 15131 14633 3070 5720 2958 N ATOM 1847 NH2 ARG A 255 -30.510 -31.804 14.473 1.00137.66 N ANISOU 1847 NH2 ARG A 255 22676 15096 14534 3391 6340 3166 N ATOM 1848 N MET A 256 -21.752 -33.136 13.135 1.00116.23 N ANISOU 1848 N MET A 256 20885 13223 10054 4461 2859 2516 N ATOM 1849 CA MET A 256 -20.586 -33.921 12.738 1.00119.02 C ANISOU 1849 CA MET A 256 21246 13552 10425 4586 2471 2521 C ATOM 1850 C MET A 256 -19.322 -33.414 13.417 1.00114.23 C ANISOU 1850 C MET A 256 20804 13227 9372 4959 1801 2261 C ATOM 1851 O MET A 256 -18.500 -34.208 13.889 1.00111.95 O ANISOU 1851 O MET A 256 20716 12888 8932 5257 1604 2327 O ATOM 1852 CB MET A 256 -20.408 -33.891 11.219 1.00118.09 C ANISOU 1852 CB MET A 256 20491 13457 10922 4117 2265 2276 C ATOM 1853 CG MET A 256 -21.555 -34.455 10.437 1.00119.13 C ANISOU 1853 CG MET A 256 20309 13312 11645 3688 2805 2401 C ATOM 1854 SD MET A 256 -21.319 -34.062 8.701 1.00114.22 S ANISOU 1854 SD MET A 256 18928 12828 11642 3173 2444 1990 S ATOM 1855 CE MET A 256 -22.994 -33.649 8.220 1.00115.06 C ANISOU 1855 CE MET A 256 18709 12827 12183 2739 2965 1997 C ATOM 1856 N LYS A 257 -19.145 -32.089 13.459 1.00113.17 N ANISOU 1856 N LYS A 257 20550 13377 9072 4930 1436 1939 N ATOM 1857 CA LYS A 257 -17.946 -31.517 14.062 1.00113.18 C ANISOU 1857 CA LYS A 257 20622 13622 8759 5227 767 1633 C ATOM 1858 C LYS A 257 -17.715 -32.073 15.461 1.00116.46 C ANISOU 1858 C LYS A 257 21500 13960 8790 5671 815 1756 C ATOM 1859 O LYS A 257 -16.579 -32.392 15.838 1.00116.33 O ANISOU 1859 O LYS A 257 21566 14023 8610 5951 357 1646 O ATOM 1860 CB LYS A 257 -18.052 -29.989 14.104 1.00108.99 C ANISOU 1860 CB LYS A 257 19937 13329 8145 5117 493 1288 C ATOM 1861 CG LYS A 257 -17.715 -29.303 12.792 1.00102.85 C ANISOU 1861 CG LYS A 257 18677 12717 7684 4767 172 1036 C ATOM 1862 CD LYS A 257 -17.639 -27.795 12.958 1.00104.65 C ANISOU 1862 CD LYS A 257 18774 13159 7827 4701 -165 663 C ATOM 1863 CE LYS A 257 -16.534 -27.385 13.915 1.00105.93 C ANISOU 1863 CE LYS A 257 19051 13443 7756 5019 -741 397 C ATOM 1864 NZ LYS A 257 -16.142 -25.960 13.700 1.00101.46 N ANISOU 1864 NZ LYS A 257 18191 13057 7301 4859 -1191 -20 N ATOM 1865 N GLU A 258 -18.791 -32.233 16.231 1.00113.30 N ANISOU 1865 N GLU A 258 21391 13398 8260 5749 1382 1991 N ATOM 1866 CA GLU A 258 -18.685 -32.729 17.592 1.00122.31 C ANISOU 1866 CA GLU A 258 23012 14460 9000 6195 1487 2131 C ATOM 1867 C GLU A 258 -18.642 -34.249 17.678 1.00119.27 C ANISOU 1867 C GLU A 258 22813 13814 8689 6314 1822 2482 C ATOM 1868 O GLU A 258 -18.114 -34.780 18.658 1.00119.69 O ANISOU 1868 O GLU A 258 23238 13843 8395 6727 1727 2555 O ATOM 1869 CB GLU A 258 -19.847 -32.195 18.436 1.00130.23 C ANISOU 1869 CB GLU A 258 24251 15401 9831 6263 1955 2228 C ATOM 1870 CG GLU A 258 -21.071 -33.082 18.433 1.00136.59 C ANISOU 1870 CG GLU A 258 25124 15898 10877 6129 2756 2632 C ATOM 1871 CD GLU A 258 -22.364 -32.308 18.596 1.00142.51 C ANISOU 1871 CD GLU A 258 25810 16616 11722 5958 3203 2662 C ATOM 1872 OE1 GLU A 258 -22.366 -31.072 18.384 1.00144.46 O ANISOU 1872 OE1 GLU A 258 25879 17078 11932 5841 2905 2369 O ATOM 1873 OE2 GLU A 258 -23.381 -32.949 18.938 1.00146.11 O ANISOU 1873 OE2 GLU A 258 26373 16821 12322 5939 3859 2977 O ATOM 1874 N SER A 259 -19.163 -34.967 16.681 1.00117.94 N ANISOU 1874 N SER A 259 22399 13438 8976 5969 2198 2692 N ATOM 1875 CA SER A 259 -19.051 -36.421 16.710 1.00117.50 C ANISOU 1875 CA SER A 259 22491 13107 9047 6061 2480 3000 C ATOM 1876 C SER A 259 -17.648 -36.872 16.325 1.00117.67 C ANISOU 1876 C SER A 259 22428 13226 9056 6206 1893 2867 C ATOM 1877 O SER A 259 -17.074 -37.747 16.978 1.00125.27 O ANISOU 1877 O SER A 259 23679 14103 9816 6540 1848 3001 O ATOM 1878 CB SER A 259 -20.090 -37.052 15.788 1.00114.65 C ANISOU 1878 CB SER A 259 21870 12447 9246 5628 3069 3237 C ATOM 1879 OG SER A 259 -21.395 -36.791 16.259 1.00120.56 O ANISOU 1879 OG SER A 259 22298 13154 10355 5404 2814 3178 O ATOM 1880 N ARG A 260 -17.102 -36.276 15.270 1.00121.88 N ANISOU 1880 N ARG A 260 22557 13938 9813 5975 1444 2605 N ATOM 1881 CA ARG A 260 -15.765 -36.620 14.803 1.00125.48 C ANISOU 1881 CA ARG A 260 22869 14528 10280 6130 831 2424 C ATOM 1882 C ARG A 260 -14.713 -36.306 15.862 1.00125.75 C ANISOU 1882 C ARG A 260 23130 14798 9852 6547 323 2197 C ATOM 1883 O ARG A 260 -13.643 -36.913 15.887 1.00119.57 O ANISOU 1883 O ARG A 260 22346 14068 9018 6785 -82 2124 O ATOM 1884 CB ARG A 260 -15.443 -35.876 13.505 1.00118.25 C ANISOU 1884 CB ARG A 260 21451 13775 9704 5807 464 2166 C ATOM 1885 CG ARG A 260 -16.441 -36.121 12.385 1.00111.36 C ANISOU 1885 CG ARG A 260 20338 12670 9306 5398 909 2347 C ATOM 1886 CD ARG A 260 -16.445 -34.974 11.388 1.00100.85 C ANISOU 1886 CD ARG A 260 18518 11566 8233 5024 663 2018 C ATOM 1887 NE ARG A 260 -16.932 -35.391 10.076 1.00 90.45 N ANISOU 1887 NE ARG A 260 16718 10084 7564 4516 962 1982 N ATOM 1888 CZ ARG A 260 -16.230 -35.294 8.953 1.00 84.87 C ANISOU 1888 CZ ARG A 260 15489 9486 7273 4251 647 1701 C ATOM 1889 NH1 ARG A 260 -15.003 -34.791 8.977 1.00 84.16 N ANISOU 1889 NH1 ARG A 260 15245 9655 7076 4417 57 1446 N ATOM 1890 NH2 ARG A 260 -16.753 -35.698 7.804 1.00 79.65 N ANISOU 1890 NH2 ARG A 260 14451 8674 7137 3829 923 1665 N ATOM 1891 N LEU A 261 -15.026 -35.353 16.734 1.00128.82 N ANISOU 1891 N LEU A 261 23690 15319 9937 6636 323 2064 N ATOM 1892 CA LEU A 261 -14.109 -34.956 17.796 1.00131.54 C ANISOU 1892 CA LEU A 261 24307 15837 9836 7050 -102 1855 C ATOM 1893 C LEU A 261 -13.714 -36.151 18.658 1.00145.46 C ANISOU 1893 C LEU A 261 26602 17395 11272 7422 311 2191 C ATOM 1894 O LEU A 261 -12.714 -36.108 19.375 1.00151.05 O ANISOU 1894 O LEU A 261 27651 18046 11695 7580 664 2302 O ATOM 1895 CB LEU A 261 -14.738 -33.866 18.666 1.00130.52 C ANISOU 1895 CB LEU A 261 24158 15881 9552 6993 -229 1590 C ATOM 1896 CG LEU A 261 -13.839 -32.679 19.019 1.00132.38 C ANISOU 1896 CG LEU A 261 24414 16356 9529 7254 -908 1187 C ATOM 1897 CD1 LEU A 261 -12.883 -32.370 17.878 1.00126.36 C ANISOU 1897 CD1 LEU A 261 23143 15768 9098 7069 -1528 868 C ATOM 1898 CD2 LEU A 261 -14.675 -31.457 19.369 1.00133.94 C ANISOU 1898 CD2 LEU A 261 24673 16639 9579 7201 -867 1007 C ATOM 1899 N GLU A 262 -14.505 -37.216 18.582 1.00153.07 N ANISOU 1899 N GLU A 262 27627 18251 12282 7585 241 2344 N ATOM 1900 CA GLU A 262 -14.239 -38.424 19.354 1.00160.86 C ANISOU 1900 CA GLU A 262 28994 18955 13172 7797 743 2753 C ATOM 1901 C GLU A 262 -14.055 -39.632 18.441 1.00159.01 C ANISOU 1901 C GLU A 262 28471 18559 13385 7578 769 2884 C ATOM 1902 O GLU A 262 -14.403 -39.589 17.261 1.00157.00 O ANISOU 1902 O GLU A 262 27782 18328 13544 7178 716 2775 O ATOM 1903 CB GLU A 262 -15.373 -38.685 20.349 1.00163.81 C ANISOU 1903 CB GLU A 262 29582 19092 13564 7677 1531 3068 C ATOM 1904 CG GLU A 262 -15.911 -37.431 21.018 1.00173.07 C ANISOU 1904 CG GLU A 262 31244 20283 14231 8063 1722 3128 C ATOM 1905 CD GLU A 262 -17.346 -37.589 21.483 1.00176.95 C ANISOU 1905 CD GLU A 262 31752 20622 14858 7830 2398 3314 C ATOM 1906 OE1 GLU A 262 -18.132 -38.252 20.774 1.00175.49 O ANISOU 1906 OE1 GLU A 262 31297 20226 15154 7430 2846 3509 O ATOM 1907 OE2 GLU A 262 -17.687 -37.051 22.557 1.00182.15 O ANISOU 1907 OE2 GLU A 262 32669 21364 15175 8042 2468 3249 O ATOM 1908 N ASP A 263 -13.507 -40.708 18.996 1.00163.81 N ANISOU 1908 N ASP A 263 29320 18992 13926 7842 854 3116 N ATOM 1909 CA ASP A 263 -13.276 -41.929 18.233 1.00162.03 C ANISOU 1909 CA ASP A 263 28838 18561 14166 7633 935 3256 C ATOM 1910 C ASP A 263 -12.115 -41.759 17.258 1.00155.68 C ANISOU 1910 C ASP A 263 27549 17996 13607 7507 268 2902 C ATOM 1911 O ASP A 263 -11.166 -42.543 17.265 1.00154.72 O ANISOU 1911 O ASP A 263 27344 17877 13567 7681 -67 2868 O ATOM 1912 CB ASP A 263 -14.542 -42.337 17.477 1.00160.90 C ANISOU 1912 CB ASP A 263 28552 18125 14460 7188 1611 3495 C ATOM 1913 CG ASP A 263 -14.287 -43.434 16.462 1.00159.85 C ANISOU 1913 CG ASP A 263 28084 17770 14882 6906 1658 3563 C ATOM 1914 OD1 ASP A 263 -13.319 -44.201 16.645 1.00160.97 O ANISOU 1914 OD1 ASP A 263 28164 17931 15066 7093 1273 3505 O ATOM 1915 OD2 ASP A 263 -15.055 -43.528 15.482 1.00156.54 O ANISOU 1915 OD2 ASP A 263 27451 17142 14887 6496 2091 3661 O ATOM 1916 N THR A 269 -9.747 -36.698 5.429 1.00128.63 N ANISOU 1916 N THR A 269 19483 15365 14025 4484 -1066 880 N ATOM 1917 CA THR A 269 -9.769 -36.560 3.978 1.00114.05 C ANISOU 1917 CA THR A 269 17063 13666 12604 4183 -1182 601 C ATOM 1918 C THR A 269 -10.852 -35.582 3.534 1.00103.49 C ANISOU 1918 C THR A 269 15501 12424 11398 3727 -979 476 C ATOM 1919 O THR A 269 -10.574 -34.608 2.834 1.00110.40 O ANISOU 1919 O THR A 269 15930 13489 12529 3479 -1108 238 O ATOM 1920 CB THR A 269 -9.999 -37.916 3.285 1.00 20.00 C ATOM 1921 OG1 THR A 269 -8.887 -38.782 3.543 1.00 20.00 O ATOM 1922 CG2 THR A 269 -10.152 -37.728 1.783 1.00 20.00 C ATOM 1923 N ASP A 270 -12.088 -35.849 3.944 1.00 91.75 N ANISOU 1923 N ASP A 270 14316 10801 9745 3631 -642 650 N ATOM 1924 CA ASP A 270 -13.214 -34.994 3.590 1.00 81.84 C ANISOU 1924 CA ASP A 270 12840 9608 8648 3213 -427 545 C ATOM 1925 C ASP A 270 -12.868 -33.521 3.776 1.00 73.83 C ANISOU 1925 C ASP A 270 11673 8894 7485 3170 -742 342 C ATOM 1926 O ASP A 270 -12.004 -33.173 4.581 1.00 64.55 O ANISOU 1926 O ASP A 270 10629 7853 6045 3469 -1102 295 O ATOM 1927 CB ASP A 270 -14.444 -35.355 4.426 1.00 76.55 C ANISOU 1927 CB ASP A 270 12485 8687 7916 3119 55 788 C ATOM 1928 CG ASP A 270 -14.160 -35.347 5.915 1.00 85.10 C ANISOU 1928 CG ASP A 270 14075 9732 8527 3459 96 1009 C ATOM 1929 OD1 ASP A 270 -13.478 -34.413 6.386 1.00 89.60 O ANISOU 1929 OD1 ASP A 270 14714 10540 8791 3662 -268 894 O ATOM 1930 OD2 ASP A 270 -14.619 -36.275 6.614 1.00 84.42 O ANISOU 1930 OD2 ASP A 270 14330 9364 8381 3529 505 1297 O ATOM 1931 N PHE A 271 -13.548 -32.659 3.026 1.00 65.99 N ANISOU 1931 N PHE A 271 10395 7992 6684 2801 -624 207 N ATOM 1932 CA PHE A 271 -13.313 -31.222 3.107 1.00 66.77 C ANISOU 1932 CA PHE A 271 10319 8334 6718 2718 -892 6 C ATOM 1933 C PHE A 271 -13.568 -30.699 4.517 1.00 69.55 C ANISOU 1933 C PHE A 271 11075 8706 6643 2952 -953 77 C ATOM 1934 O PHE A 271 -12.797 -29.895 5.039 1.00 70.95 O ANISOU 1934 O PHE A 271 11228 9060 6671 3076 -1332 -97 O ATOM 1935 CB PHE A 271 -14.196 -30.479 2.103 1.00 60.34 C ANISOU 1935 CB PHE A 271 9197 7571 6157 2311 -699 -99 C ATOM 1936 CG PHE A 271 -13.695 -30.547 0.688 1.00 66.45 C ANISOU 1936 CG PHE A 271 9556 8400 7290 2107 -723 -229 C ATOM 1937 CD1 PHE A 271 -12.526 -29.902 0.321 1.00 73.19 C ANISOU 1937 CD1 PHE A 271 10091 9441 8275 2111 -1036 -408 C ATOM 1938 CD2 PHE A 271 -14.393 -31.258 -0.274 1.00 69.76 C ANISOU 1938 CD2 PHE A 271 9900 8681 7926 1915 -422 -183 C ATOM 1939 CE1 PHE A 271 -12.062 -29.963 -0.980 1.00 72.64 C ANISOU 1939 CE1 PHE A 271 9666 9428 8505 1951 -1001 -505 C ATOM 1940 CE2 PHE A 271 -13.935 -31.323 -1.576 1.00 67.57 C ANISOU 1940 CE2 PHE A 271 9290 8467 7916 1769 -440 -315 C ATOM 1941 CZ PHE A 271 -12.768 -30.675 -1.930 1.00 66.44 C ANISOU 1941 CZ PHE A 271 8864 8520 7859 1797 -704 -459 C ATOM 1942 N LEU A 272 -14.654 -31.162 5.127 1.00 71.77 N ANISOU 1942 N LEU A 272 11736 8799 6736 3021 -572 322 N ATOM 1943 CA LEU A 272 -15.012 -30.741 6.478 1.00 76.63 C ANISOU 1943 CA LEU A 272 12793 9431 6893 3284 -566 412 C ATOM 1944 C LEU A 272 -13.854 -30.983 7.436 1.00 81.83 C ANISOU 1944 C LEU A 272 13717 10168 7207 3736 -987 399 C ATOM 1945 O LEU A 272 -13.462 -30.091 8.198 1.00 84.21 O ANISOU 1945 O LEU A 272 14140 10638 7220 3917 -1327 238 O ATOM 1946 CB LEU A 272 -16.268 -31.475 6.960 1.00 79.57 C ANISOU 1946 CB LEU A 272 13520 9554 7157 3303 -12 727 C ATOM 1947 CG LEU A 272 -16.644 -31.289 8.443 1.00 89.85 C ANISOU 1947 CG LEU A 272 15380 10841 7919 3658 90 894 C ATOM 1948 CD1 LEU A 272 -16.851 -29.813 8.797 1.00 91.18 C ANISOU 1948 CD1 LEU A 272 15521 11221 7903 3615 -89 668 C ATOM 1949 CD2 LEU A 272 -17.888 -32.086 8.810 1.00 92.06 C ANISOU 1949 CD2 LEU A 272 15955 10841 8183 3644 723 1241 C ATOM 1950 N GLN A 273 -13.268 -32.178 7.384 1.00 80.21 N ANISOU 1950 N GLN A 273 13592 9837 7046 3934 -1005 543 N ATOM 1951 CA GLN A 273 -12.163 -32.491 8.281 1.00 83.69 C ANISOU 1951 CA GLN A 273 14283 10350 7167 4404 -1429 542 C ATOM 1952 C GLN A 273 -10.944 -31.635 7.975 1.00 79.34 C ANISOU 1952 C GLN A 273 13313 10059 6774 4390 -2012 187 C ATOM 1953 O GLN A 273 -10.275 -31.152 8.892 1.00 79.93 O ANISOU 1953 O GLN A 273 13556 10279 6535 4704 -2453 54 O ATOM 1954 CB GLN A 273 -11.811 -33.969 8.186 1.00 90.31 C ANISOU 1954 CB GLN A 273 15262 10974 8077 4612 -1305 777 C ATOM 1955 CG GLN A 273 -10.833 -34.402 9.248 1.00 98.57 C ANISOU 1955 CG GLN A 273 16661 12064 8727 5166 -1699 840 C ATOM 1956 CD GLN A 273 -11.355 -34.155 10.637 1.00104.18 C ANISOU 1956 CD GLN A 273 17980 12773 8830 5504 -1640 1004 C ATOM 1957 OE1 GLN A 273 -12.508 -34.469 10.946 1.00104.49 O ANISOU 1957 OE1 GLN A 273 18349 12614 8736 5448 -1098 1281 O ATOM 1958 NE2 GLN A 273 -10.516 -33.571 11.486 1.00108.81 N ANISOU 1958 NE2 GLN A 273 18601 13569 9173 5734 -2114 754 N ATOM 1959 N LEU A 274 -10.652 -31.413 6.694 1.00 74.86 N ANISOU 1959 N LEU A 274 12199 9546 6699 4032 -2017 21 N ATOM 1960 CA LEU A 274 -9.561 -30.510 6.343 1.00 75.83 C ANISOU 1960 CA LEU A 274 11876 9891 7046 3964 -2492 -299 C ATOM 1961 C LEU A 274 -9.785 -29.121 6.936 1.00 81.15 C ANISOU 1961 C LEU A 274 12593 10704 7539 3908 -2701 -498 C ATOM 1962 O LEU A 274 -8.856 -28.520 7.491 1.00 90.30 O ANISOU 1962 O LEU A 274 13676 12006 8626 4095 -3210 -728 O ATOM 1963 CB LEU A 274 -9.401 -30.448 4.823 1.00 66.58 C ANISOU 1963 CB LEU A 274 10159 8740 6400 3574 -2343 -397 C ATOM 1964 CG LEU A 274 -8.885 -31.756 4.198 1.00 73.93 C ANISOU 1964 CG LEU A 274 10993 9557 7542 3672 -2243 -285 C ATOM 1965 CD1 LEU A 274 -8.890 -31.758 2.667 1.00 68.59 C ANISOU 1965 CD1 LEU A 274 9857 8891 7313 3309 -2026 -369 C ATOM 1966 CD2 LEU A 274 -7.485 -32.063 4.733 1.00 74.77 C ANISOU 1966 CD2 LEU A 274 11036 9756 7616 4055 -2725 -375 C ATOM 1967 N MET A 275 -11.023 -28.615 6.872 1.00 71.46 N ANISOU 1967 N MET A 275 11491 9418 6243 3672 -2327 -427 N ATOM 1968 CA MET A 275 -11.306 -27.285 7.406 1.00 67.71 C ANISOU 1968 CA MET A 275 11072 9048 5606 3621 -2489 -621 C ATOM 1969 C MET A 275 -11.254 -27.274 8.933 1.00 76.66 C ANISOU 1969 C MET A 275 12760 10204 6162 4076 -2707 -601 C ATOM 1970 O MET A 275 -10.683 -26.356 9.531 1.00 82.63 O ANISOU 1970 O MET A 275 13519 11091 6785 4204 -3162 -874 O ATOM 1971 CB MET A 275 -12.658 -26.800 6.897 1.00 63.76 C ANISOU 1971 CB MET A 275 10545 8477 5206 3276 -2017 -541 C ATOM 1972 CG MET A 275 -12.668 -26.534 5.388 1.00 73.31 C ANISOU 1972 CG MET A 275 11214 9705 6936 2848 -1887 -617 C ATOM 1973 SD MET A 275 -14.125 -25.637 4.769 1.00 69.61 S ANISOU 1973 SD MET A 275 10643 9200 6605 2462 -1479 -603 S ATOM 1974 CE MET A 275 -14.167 -24.318 5.954 1.00 87.50 C ANISOU 1974 CE MET A 275 13153 11547 8545 2620 -1749 -793 C ATOM 1975 N ILE A 276 -11.836 -28.288 9.579 1.00 77.22 N ANISOU 1975 N ILE A 276 13318 10136 5884 4338 -2390 -285 N ATOM 1976 CA ILE A 276 -11.661 -28.465 11.022 1.00 85.87 C ANISOU 1976 CA ILE A 276 14999 11255 6371 4854 -2594 -222 C ATOM 1977 C ILE A 276 -10.186 -28.484 11.391 1.00 83.61 C ANISOU 1977 C ILE A 276 14510 11067 6193 5045 -3156 -474 C ATOM 1978 O ILE A 276 -9.776 -27.914 12.410 1.00 92.10 O ANISOU 1978 O ILE A 276 15727 12194 7072 5226 -3430 -679 O ATOM 1979 CB ILE A 276 -12.357 -29.753 11.495 1.00 96.83 C ANISOU 1979 CB ILE A 276 16877 12431 7484 5083 -2103 210 C ATOM 1980 CG1 ILE A 276 -13.873 -29.625 11.378 1.00105.28 C ANISOU 1980 CG1 ILE A 276 18079 13361 8561 4825 -1454 412 C ATOM 1981 CG2 ILE A 276 -11.989 -30.051 12.928 1.00105.73 C ANISOU 1981 CG2 ILE A 276 18413 13528 8230 5482 -2202 222 C ATOM 1982 CD1 ILE A 276 -14.599 -30.885 11.792 1.00107.27 C ANISOU 1982 CD1 ILE A 276 18763 13360 8636 5000 -914 850 C ATOM 1983 N ASP A 277 -9.364 -29.149 10.580 1.00 85.62 N ANISOU 1983 N ASP A 277 14416 11332 6782 5016 -3318 -467 N ATOM 1984 CA ASP A 277 -7.946 -29.249 10.925 1.00 97.96 C ANISOU 1984 CA ASP A 277 15757 12978 8487 5188 -3803 -693 C ATOM 1985 C ASP A 277 -7.273 -27.887 10.847 1.00102.25 C ANISOU 1985 C ASP A 277 15875 13663 9310 4978 -4217 -1105 C ATOM 1986 O ASP A 277 -6.423 -27.558 11.687 1.00100.20 O ANISOU 1986 O ASP A 277 15621 13452 8998 5158 -4597 -1331 O ATOM 1987 CB ASP A 277 -7.232 -30.250 10.011 1.00 97.98 C ANISOU 1987 CB ASP A 277 15441 12951 8837 5192 -3834 -596 C ATOM 1988 CG ASP A 277 -7.541 -31.702 10.369 1.00 99.63 C ANISOU 1988 CG ASP A 277 16093 12972 8791 5486 -3521 -223 C ATOM 1989 OD1 ASP A 277 -8.411 -31.928 11.235 1.00 99.63 O ANISOU 1989 OD1 ASP A 277 16628 12861 8367 5644 -3214 -9 O ATOM 1990 OD2 ASP A 277 -6.909 -32.616 9.782 1.00 94.94 O ANISOU 1990 OD2 ASP A 277 15300 12321 8452 5553 -3549 -143 O ATOM 1991 N SER A 278 -7.666 -27.075 9.854 1.00 94.14 N ANISOU 1991 N SER A 278 14491 12686 8594 4597 -4135 -1203 N ATOM 1992 CA SER A 278 -7.083 -25.752 9.666 1.00 94.14 C ANISOU 1992 CA SER A 278 14061 12770 8937 4344 -4456 -1565 C ATOM 1993 C SER A 278 -7.345 -24.834 10.849 1.00 94.63 C ANISOU 1993 C SER A 278 14443 12820 8693 4458 -4587 -1738 C ATOM 1994 O SER A 278 -6.584 -23.887 11.066 1.00104.16 O ANISOU 1994 O SER A 278 15374 14057 10145 4370 -4944 -2055 O ATOM 1995 CB SER A 278 -7.637 -25.123 8.395 1.00 88.11 C ANISOU 1995 CB SER A 278 12929 12036 8511 3932 -4262 -1584 C ATOM 1996 OG SER A 278 -9.045 -24.979 8.499 1.00 87.83 O ANISOU 1996 OG SER A 278 13260 11935 8177 3854 -3837 -1405 O ATOM 1997 N GLN A 279 -8.402 -25.091 11.613 1.00 89.04 N ANISOU 1997 N GLN A 279 14301 12048 7482 4655 -4280 -1532 N ATOM 1998 CA GLN A 279 -8.687 -24.302 12.801 1.00100.15 C ANISOU 1998 CA GLN A 279 16052 13437 8563 4824 -4372 -1679 C ATOM 1999 C GLN A 279 -7.664 -24.537 13.893 1.00113.19 C ANISOU 1999 C GLN A 279 17855 15103 10050 5190 -4774 -1829 C ATOM 2000 O GLN A 279 -7.744 -23.897 14.946 1.00113.60 O ANISOU 2000 O GLN A 279 18190 15143 9828 5384 -4924 -1987 O ATOM 2001 CB GLN A 279 -10.096 -24.622 13.307 1.00 98.07 C ANISOU 2001 CB GLN A 279 16340 13093 7830 4953 -3858 -1378 C ATOM 2002 CG GLN A 279 -11.122 -24.683 12.181 1.00 99.79 C ANISOU 2002 CG GLN A 279 16436 13288 8191 4628 -3425 -1180 C ATOM 2003 CD GLN A 279 -12.541 -24.587 12.673 1.00100.97 C ANISOU 2003 CD GLN A 279 17029 13356 7979 4672 -2919 -967 C ATOM 2004 OE1 GLN A 279 -13.102 -25.553 13.182 1.00106.20 O ANISOU 2004 OE1 GLN A 279 18098 13916 8336 4895 -2550 -646 O ATOM 2005 NE2 GLN A 279 -13.138 -23.422 12.511 1.00 97.14 N ANISOU 2005 NE2 GLN A 279 16447 12894 7567 4449 -2864 -1134 N ATOM 2006 N ASN A 280 -6.693 -25.415 13.640 1.00121.95 N ANISOU 2006 N ASN A 280 18769 16239 11329 5296 -4966 -1798 N ATOM 2007 CA ASN A 280 -5.617 -25.738 14.576 1.00139.13 C ANISOU 2007 CA ASN A 280 21040 18439 13382 5648 -5378 -1946 C ATOM 2008 C ASN A 280 -4.294 -25.388 13.899 1.00146.61 C ANISOU 2008 C ASN A 280 21335 19455 14914 5444 -5792 -2227 C ATOM 2009 O ASN A 280 -3.636 -26.248 13.308 1.00145.83 O ANISOU 2009 O ASN A 280 20984 19378 15047 5453 -5822 -2131 O ATOM 2010 CB ASN A 280 -5.674 -27.217 14.993 1.00140.50 C ANISOU 2010 CB ASN A 280 21618 18560 13205 6007 -5185 -1616 C ATOM 2011 CG ASN A 280 -7.067 -27.650 15.389 1.00137.06 C ANISOU 2011 CG ASN A 280 21745 18022 12312 6120 -4639 -1269 C ATOM 2012 OD1 ASN A 280 -7.848 -26.859 15.919 1.00132.73 O ANISOU 2012 OD1 ASN A 280 21442 17458 11533 6111 -4506 -1318 O ATOM 2013 ND2 ASN A 280 -7.393 -28.912 15.120 1.00136.91 N ANISOU 2013 ND2 ASN A 280 21916 17909 12194 6220 -4291 -908 N ATOM 2014 N SER A 281 -3.900 -24.122 14.012 1.00152.06 N ANISOU 2014 N SER A 281 21754 20160 15862 5268 -6089 -2569 N ATOM 2015 CA SER A 281 -2.653 -23.639 13.429 1.00153.13 C ANISOU 2015 CA SER A 281 21253 20331 16600 5047 -6446 -2844 C ATOM 2016 C SER A 281 -1.445 -24.353 14.032 1.00159.20 C ANISOU 2016 C SER A 281 21992 21138 17357 5378 -6831 -2938 C ATOM 2017 O SER A 281 -0.839 -25.220 13.396 1.00156.34 O ANISOU 2017 O SER A 281 21362 20809 17231 5374 -6811 -2819 O ATOM 2018 CB SER A 281 -2.518 -22.128 13.631 1.00151.35 C ANISOU 2018 CB SER A 281 20825 20067 16612 4838 -6679 -3184 C ATOM 2019 OG SER A 281 -2.396 -21.804 15.006 1.00152.58 O ANISOU 2019 OG SER A 281 21382 20207 16384 5189 -6983 -3372 O ATOM 2020 N SER A 286 -0.691 -17.243 9.762 1.00125.72 N ANISOU 2020 N SER A 286 15340 16514 15914 3081 -6892 -4043 N ATOM 2021 CA SER A 286 -0.662 -15.947 10.429 1.00130.81 C ANISOU 2021 CA SER A 286 15937 17019 16746 2902 -7006 -4286 C ATOM 2022 C SER A 286 -2.022 -15.261 10.361 1.00128.28 C ANISOU 2022 C SER A 286 15896 16661 16183 2748 -6641 -4146 C ATOM 2023 O SER A 286 -2.140 -14.066 10.633 1.00135.02 O ANISOU 2023 O SER A 286 16951 17418 16930 2760 -6745 -4325 O ATOM 2024 CB SER A 286 0.411 -15.049 9.809 1.00133.59 C ANISOU 2024 CB SER A 286 15625 17260 17874 2536 -7075 -4439 C ATOM 2025 OG SER A 286 0.279 -14.996 8.399 1.00132.13 O ANISOU 2025 OG SER A 286 15103 17093 18007 2212 -6657 -4190 O ATOM 2026 N HIS A 287 -3.047 -16.025 9.998 1.00111.11 N ANISOU 2026 N HIS A 287 13731 14559 13929 2618 -6231 -3844 N ATOM 2027 CA HIS A 287 -4.400 -15.493 9.893 1.00105.44 C ANISOU 2027 CA HIS A 287 13326 13824 12912 2532 -5897 -3705 C ATOM 2028 C HIS A 287 -5.148 -15.626 11.216 1.00112.15 C ANISOU 2028 C HIS A 287 14835 14738 13040 2931 -5875 -3617 C ATOM 2029 O HIS A 287 -4.629 -16.189 12.180 1.00112.25 O ANISOU 2029 O HIS A 287 15063 14839 12747 3234 -5936 -3500 O ATOM 2030 CB HIS A 287 -5.171 -16.204 8.779 1.00 97.37 C ANISOU 2030 CB HIS A 287 12111 12862 12026 2288 -5485 -3424 C ATOM 2031 CG HIS A 287 -4.840 -15.710 7.405 1.00 90.94 C ANISOU 2031 CG HIS A 287 10740 11959 11855 1864 -5362 -3458 C ATOM 2032 ND1 HIS A 287 -5.127 -14.430 6.985 1.00 90.34 N ANISOU 2032 ND1 HIS A 287 10596 11740 11988 1619 -5298 -3572 N ATOM 2033 CD2 HIS A 287 -4.245 -16.326 6.356 1.00 87.54 C ANISOU 2033 CD2 HIS A 287 9810 11549 11902 1658 -5257 -3373 C ATOM 2034 CE1 HIS A 287 -4.724 -14.277 5.736 1.00 86.55 C ANISOU 2034 CE1 HIS A 287 9610 11188 12086 1279 -5150 -3538 C ATOM 2035 NE2 HIS A 287 -4.185 -15.413 5.331 1.00 85.74 N ANISOU 2035 NE2 HIS A 287 9237 11189 12151 1297 -5111 -3416 N ATOM 2036 N LYS A 288 -6.370 -15.105 11.254 1.00121.12 N ANISOU 2036 N LYS A 288 16297 15816 13906 2930 -5732 -3641 N ATOM 2037 CA LYS A 288 -7.192 -15.165 12.457 1.00129.30 C ANISOU 2037 CA LYS A 288 17962 16882 14282 3314 -5696 -3587 C ATOM 2038 C LYS A 288 -7.666 -16.602 12.643 1.00126.71 C ANISOU 2038 C LYS A 288 17980 16654 13510 3510 -5358 -3235 C ATOM 2039 O LYS A 288 -7.837 -17.068 13.769 1.00137.08 O ANISOU 2039 O LYS A 288 19825 17982 14277 3853 -5275 -3140 O ATOM 2040 CB LYS A 288 -8.238 -14.049 12.447 1.00134.49 C ANISOU 2040 CB LYS A 288 18834 17450 14817 3228 -5551 -3677 C ATOM 2041 CG LYS A 288 -9.096 -13.990 13.700 1.00140.87 C ANISOU 2041 CG LYS A 288 19256 18118 16151 2952 -5799 -3987 C ATOM 2042 CD LYS A 288 -10.078 -12.831 13.644 1.00138.01 C ANISOU 2042 CD LYS A 288 18473 17695 16268 2500 -5529 -3901 C ATOM 2043 CE LYS A 288 -10.952 -12.788 14.887 1.00144.60 C ANISOU 2043 CE LYS A 288 18849 18365 17726 2204 -5748 -4159 C ATOM 2044 NZ LYS A 288 -11.920 -11.657 14.846 1.00147.83 N ANISOU 2044 NZ LYS A 288 19434 18628 18108 2136 -5719 -4319 N ATOM 2045 N ALA A 289 -7.873 -17.292 11.533 1.00110.20 N ANISOU 2045 N ALA A 289 15612 14616 11641 3312 -5145 -3032 N ATOM 2046 CA ALA A 289 -8.362 -18.650 11.579 1.00 99.92 C ANISOU 2046 CA ALA A 289 14589 13386 9991 3498 -4862 -2705 C ATOM 2047 C ALA A 289 -9.824 -18.528 11.205 1.00 88.04 C ANISOU 2047 C ALA A 289 13542 11865 8045 3552 -4419 -2484 C ATOM 2048 O ALA A 289 -10.438 -17.481 11.413 1.00 86.62 O ANISOU 2048 O ALA A 289 13665 11635 7610 3648 -4378 -2571 O ATOM 2049 CB ALA A 289 -8.210 -19.228 12.975 1.00 20.00 C ATOM 2050 N LEU A 290 -10.382 -19.588 10.646 1.00 82.13 N ANISOU 2050 N LEU A 290 12848 11150 7206 3511 -4073 -2192 N ATOM 2051 CA LEU A 290 -11.777 -19.564 10.221 1.00 72.31 C ANISOU 2051 CA LEU A 290 11892 9883 5699 3447 -3594 -1986 C ATOM 2052 C LEU A 290 -12.584 -20.053 11.418 1.00 87.76 C ANISOU 2052 C LEU A 290 14435 11786 7121 3767 -3382 -1875 C ATOM 2053 O LEU A 290 -12.186 -20.994 12.105 1.00 86.52 O ANISOU 2053 O LEU A 290 14600 11620 6654 4107 -3410 -1746 O ATOM 2054 CB LEU A 290 -12.041 -20.458 9.008 1.00 70.27 C ANISOU 2054 CB LEU A 290 11549 9611 5539 3344 -3205 -1658 C ATOM 2055 CG LEU A 290 -11.699 -19.864 7.640 1.00 69.26 C ANISOU 2055 CG LEU A 290 10793 9488 6033 2948 -3194 -1692 C ATOM 2056 CD1 LEU A 290 -11.169 -20.940 6.704 1.00 73.45 C ANISOU 2056 CD1 LEU A 290 11235 10011 6661 2994 -3049 -1461 C ATOM 2057 CD2 LEU A 290 -12.911 -19.172 7.036 1.00 69.33 C ANISOU 2057 CD2 LEU A 290 10633 9432 6276 2580 -2768 -1618 C ATOM 2058 N SER A 291 -13.720 -19.408 11.663 1.00 77.79 N ANISOU 2058 N SER A 291 13311 10481 5765 3668 -3134 -1910 N ATOM 2059 CA SER A 291 -14.586 -19.776 12.777 1.00 83.26 C ANISOU 2059 CA SER A 291 14534 11120 5982 3939 -2776 -1726 C ATOM 2060 C SER A 291 -15.517 -20.922 12.396 1.00 79.71 C ANISOU 2060 C SER A 291 14280 10639 5366 3951 -2228 -1334 C ATOM 2061 O SER A 291 -15.367 -21.530 11.336 1.00 73.08 O ANISOU 2061 O SER A 291 13116 9801 4850 3671 -2072 -1227 O ATOM 2062 CB SER A 291 -15.401 -18.569 13.244 1.00 87.02 C ANISOU 2062 CB SER A 291 15066 11549 6447 3831 -2636 -1873 C ATOM 2063 OG SER A 291 -16.301 -18.141 12.237 1.00 84.56 O ANISOU 2063 OG SER A 291 14581 11228 6319 3531 -2252 -1767 O ATOM 2064 N ASP A 292 -16.478 -21.212 13.267 1.00 89.98 N ANISOU 2064 N ASP A 292 16051 11867 6271 4239 -1879 -1095 N ATOM 2065 CA ASP A 292 -17.434 -22.284 13.023 1.00 97.05 C ANISOU 2065 CA ASP A 292 17131 12679 7064 4235 -1285 -699 C ATOM 2066 C ASP A 292 -18.418 -21.901 11.931 1.00 97.91 C ANISOU 2066 C ASP A 292 16935 12761 7506 3838 -901 -656 C ATOM 2067 O ASP A 292 -18.731 -22.713 11.049 1.00 93.17 O ANISOU 2067 O ASP A 292 16059 12078 7265 3585 -596 -435 O ATOM 2068 CB ASP A 292 -18.167 -22.634 14.311 1.00 93.70 C ANISOU 2068 CB ASP A 292 17204 12151 6248 4560 -911 -468 C ATOM 2069 CG ASP A 292 -17.281 -23.348 15.284 1.00 97.02 C ANISOU 2069 CG ASP A 292 17910 12558 6397 4947 -1182 -428 C ATOM 2070 OD1 ASP A 292 -16.312 -23.994 14.818 1.00 87.07 O ANISOU 2070 OD1 ASP A 292 16472 11336 5276 4946 -1486 -447 O ATOM 2071 OD2 ASP A 292 -17.540 -23.260 16.500 1.00109.03 O ANISOU 2071 OD2 ASP A 292 19825 14031 7569 5266 -1092 -385 O ATOM 2072 N LEU A 293 -18.888 -20.652 11.951 1.00 88.06 N ANISOU 2072 N LEU A 293 15620 11537 6301 3726 -916 -872 N ATOM 2073 CA LEU A 293 -19.834 -20.222 10.933 1.00 82.04 C ANISOU 2073 CA LEU A 293 14459 10713 5999 3318 -555 -821 C ATOM 2074 C LEU A 293 -19.153 -19.993 9.585 1.00 75.41 C ANISOU 2074 C LEU A 293 13025 9906 5723 2932 -823 -956 C ATOM 2075 O LEU A 293 -19.750 -20.265 8.538 1.00 70.64 O ANISOU 2075 O LEU A 293 12083 9252 5507 2618 -520 -815 O ATOM 2076 CB LEU A 293 -20.565 -18.964 11.392 1.00 88.92 C ANISOU 2076 CB LEU A 293 15465 11583 6737 3355 -470 -995 C ATOM 2077 CG LEU A 293 -21.528 -18.411 10.336 1.00 90.08 C ANISOU 2077 CG LEU A 293 15314 11654 7258 3037 19 -864 C ATOM 2078 CD1 LEU A 293 -22.629 -19.420 10.049 1.00 97.41 C ANISOU 2078 CD1 LEU A 293 16514 12493 8005 3168 642 -519 C ATOM 2079 CD2 LEU A 293 -22.102 -17.086 10.764 1.00 84.10 C ANISOU 2079 CD2 LEU A 293 14507 10899 6550 2984 -67 -1121 C ATOM 2080 N GLU A 294 -17.913 -19.490 9.583 1.00 79.90 N ANISOU 2080 N GLU A 294 13454 10554 6351 2958 -1384 -1233 N ATOM 2081 CA GLU A 294 -17.155 -19.396 8.335 1.00 77.74 C ANISOU 2081 CA GLU A 294 12634 10307 6598 2629 -1594 -1319 C ATOM 2082 C GLU A 294 -16.920 -20.762 7.724 1.00 69.95 C ANISOU 2082 C GLU A 294 11518 9306 5754 2579 -1440 -1080 C ATOM 2083 O GLU A 294 -16.773 -20.891 6.508 1.00 70.19 O ANISOU 2083 O GLU A 294 11124 9337 6208 2278 -1382 -1053 O ATOM 2084 CB GLU A 294 -15.801 -18.741 8.572 1.00 83.90 C ANISOU 2084 CB GLU A 294 13284 11155 7439 2696 -2207 -1645 C ATOM 2085 CG GLU A 294 -15.811 -17.240 8.620 1.00 84.11 C ANISOU 2085 CG GLU A 294 13204 11155 7600 2575 -2415 -1940 C ATOM 2086 CD GLU A 294 -14.508 -16.712 9.172 1.00 88.80 C ANISOU 2086 CD GLU A 294 13755 11790 8196 2714 -3046 -2283 C ATOM 2087 OE1 GLU A 294 -13.838 -17.464 9.915 1.00 90.95 O ANISOU 2087 OE1 GLU A 294 14246 12126 8186 3022 -3295 -2282 O ATOM 2088 OE2 GLU A 294 -14.143 -15.563 8.848 1.00 88.93 O ANISOU 2088 OE2 GLU A 294 13493 11754 8544 2510 -3284 -2542 O ATOM 2089 N LEU A 295 -16.834 -21.779 8.558 1.00 75.02 N ANISOU 2089 N LEU A 295 12543 9928 6034 2897 -1384 -910 N ATOM 2090 CA LEU A 295 -16.585 -23.114 8.055 1.00 72.97 C ANISOU 2090 CA LEU A 295 12199 9619 5909 2881 -1244 -689 C ATOM 2091 C LEU A 295 -17.834 -23.663 7.373 1.00 71.09 C ANISOU 2091 C LEU A 295 11871 9259 5882 2640 -677 -442 C ATOM 2092 O LEU A 295 -17.756 -24.258 6.288 1.00 67.94 O ANISOU 2092 O LEU A 295 11142 8825 5846 2405 -581 -378 O ATOM 2093 CB LEU A 295 -16.112 -23.985 9.219 1.00 73.64 C ANISOU 2093 CB LEU A 295 12760 9693 5528 3330 -1363 -570 C ATOM 2094 CG LEU A 295 -15.475 -25.345 8.986 1.00 81.11 C ANISOU 2094 CG LEU A 295 13695 10585 6539 3441 -1379 -389 C ATOM 2095 CD1 LEU A 295 -14.602 -25.709 10.157 1.00 85.78 C ANISOU 2095 CD1 LEU A 295 14688 11231 6673 3922 -1753 -409 C ATOM 2096 CD2 LEU A 295 -16.573 -26.349 8.837 1.00 83.67 C ANISOU 2096 CD2 LEU A 295 14174 10727 6889 3375 -783 -47 C ATOM 2097 N VAL A 296 -18.999 -23.437 7.983 1.00 73.09 N ANISOU 2097 N VAL A 296 12396 9445 5929 2700 -306 -325 N ATOM 2098 CA VAL A 296 -20.257 -23.898 7.404 1.00 73.55 C ANISOU 2098 CA VAL A 296 12331 9378 6235 2469 221 -115 C ATOM 2099 C VAL A 296 -20.514 -23.216 6.071 1.00 68.21 C ANISOU 2099 C VAL A 296 11147 8748 6023 2076 197 -255 C ATOM 2100 O VAL A 296 -21.041 -23.828 5.127 1.00 65.09 O ANISOU 2100 O VAL A 296 10494 8280 5958 1839 436 -150 O ATOM 2101 CB VAL A 296 -21.417 -23.654 8.384 1.00 78.92 C ANISOU 2101 CB VAL A 296 13374 9990 6623 2630 626 20 C ATOM 2102 CG1 VAL A 296 -22.655 -24.311 7.859 1.00 85.63 C ANISOU 2102 CG1 VAL A 296 14069 10685 7779 2408 1167 249 C ATOM 2103 CG2 VAL A 296 -21.080 -24.205 9.734 1.00 86.77 C ANISOU 2103 CG2 VAL A 296 14930 10960 7080 3072 625 155 C ATOM 2104 N ALA A 297 -20.149 -21.939 5.966 1.00 62.69 N ANISOU 2104 N ALA A 297 10310 8154 5355 2015 -101 -498 N ATOM 2105 CA ALA A 297 -20.430 -21.222 4.733 1.00 61.74 C ANISOU 2105 CA ALA A 297 9756 8066 5636 1678 -97 -596 C ATOM 2106 C ALA A 297 -19.627 -21.800 3.571 1.00 56.15 C ANISOU 2106 C ALA A 297 8705 7393 5237 1501 -249 -608 C ATOM 2107 O ALA A 297 -20.140 -21.908 2.448 1.00 54.63 O ANISOU 2107 O ALA A 297 8222 7189 5347 1253 -83 -569 O ATOM 2108 CB ALA A 297 -20.166 -19.719 4.916 1.00 58.76 C ANISOU 2108 CB ALA A 297 9331 7750 5243 1663 -366 -838 C ATOM 2109 N GLN A 298 -18.377 -22.199 3.829 1.00 60.03 N ANISOU 2109 N GLN A 298 9232 7932 5646 1651 -567 -669 N ATOM 2110 CA GLN A 298 -17.582 -22.864 2.798 1.00 51.18 C ANISOU 2110 CA GLN A 298 7809 6839 4797 1529 -670 -668 C ATOM 2111 C GLN A 298 -18.206 -24.184 2.409 1.00 46.85 C ANISOU 2111 C GLN A 298 7298 6179 4322 1492 -340 -464 C ATOM 2112 O GLN A 298 -18.288 -24.524 1.220 1.00 52.12 O ANISOU 2112 O GLN A 298 7680 6845 5279 1282 -254 -461 O ATOM 2113 CB GLN A 298 -16.151 -23.113 3.272 1.00 54.33 C ANISOU 2113 CB GLN A 298 8238 7301 5103 1740 -1065 -766 C ATOM 2114 CG GLN A 298 -15.422 -21.910 3.811 1.00 61.85 C ANISOU 2114 CG GLN A 298 9160 8334 6004 1802 -1452 -1005 C ATOM 2115 CD GLN A 298 -15.879 -20.605 3.179 1.00 63.78 C ANISOU 2115 CD GLN A 298 9169 8590 6477 1536 -1406 -1119 C ATOM 2116 OE1 GLN A 298 -15.901 -20.442 1.955 1.00 58.19 O ANISOU 2116 OE1 GLN A 298 8121 7897 6094 1280 -1301 -1101 O ATOM 2117 NE2 GLN A 298 -16.232 -19.660 4.031 1.00 66.38 N ANISOU 2117 NE2 GLN A 298 9707 8903 6612 1624 -1489 -1237 N ATOM 2118 N SER A 299 -18.580 -24.981 3.411 1.00 56.57 N ANISOU 2118 N SER A 299 8900 7303 5290 1714 -162 -295 N ATOM 2119 CA SER A 299 -19.158 -26.289 3.131 1.00 56.60 C ANISOU 2119 CA SER A 299 8952 7145 5407 1677 166 -95 C ATOM 2120 C SER A 299 -20.360 -26.138 2.217 1.00 51.97 C ANISOU 2120 C SER A 299 8116 6507 5122 1374 461 -82 C ATOM 2121 O SER A 299 -20.502 -26.848 1.213 1.00 55.46 O ANISOU 2121 O SER A 299 8339 6888 5844 1203 549 -74 O ATOM 2122 CB SER A 299 -19.544 -26.978 4.439 1.00 57.51 C ANISOU 2122 CB SER A 299 9536 7127 5190 1960 388 121 C ATOM 2123 OG SER A 299 -18.380 -27.296 5.173 1.00 67.65 O ANISOU 2123 OG SER A 299 11049 8458 6199 2272 74 111 O ATOM 2124 N ILE A 300 -21.215 -25.168 2.525 1.00 53.18 N ANISOU 2124 N ILE A 300 8290 6691 5224 1321 582 -109 N ATOM 2125 CA ILE A 300 -22.386 -24.968 1.696 1.00 51.26 C ANISOU 2125 CA ILE A 300 7791 6411 5274 1063 826 -108 C ATOM 2126 C ILE A 300 -21.988 -24.497 0.305 1.00 42.53 C ANISOU 2126 C ILE A 300 6306 5426 4428 846 607 -270 C ATOM 2127 O ILE A 300 -22.507 -25.001 -0.696 1.00 51.96 O ANISOU 2127 O ILE A 300 7279 6577 5887 664 720 -272 O ATOM 2128 CB ILE A 300 -23.349 -23.991 2.381 1.00 56.11 C ANISOU 2128 CB ILE A 300 8512 7033 5773 1095 1003 -101 C ATOM 2129 CG1 ILE A 300 -23.809 -24.608 3.691 1.00 63.43 C ANISOU 2129 CG1 ILE A 300 9838 7830 6433 1327 1305 99 C ATOM 2130 CG2 ILE A 300 -24.542 -23.761 1.494 1.00 54.52 C ANISOU 2130 CG2 ILE A 300 8004 6805 5905 846 1214 -113 C ATOM 2131 CD1 ILE A 300 -24.280 -23.604 4.683 1.00 66.16 C ANISOU 2131 CD1 ILE A 300 10417 8218 6503 1488 1389 77 C ATOM 2132 N ILE A 301 -21.067 -23.532 0.211 1.00 51.76 N ANISOU 2132 N ILE A 301 7398 6735 5533 868 297 -412 N ATOM 2133 CA ILE A 301 -20.800 -22.962 -1.110 1.00 39.40 C ANISOU 2133 CA ILE A 301 5493 5272 4206 669 163 -525 C ATOM 2134 C ILE A 301 -20.140 -24.005 -2.023 1.00 42.82 C ANISOU 2134 C ILE A 301 5782 5706 4784 626 116 -525 C ATOM 2135 O ILE A 301 -20.351 -23.981 -3.245 1.00 41.62 O ANISOU 2135 O ILE A 301 5392 5597 4824 465 138 -572 O ATOM 2136 CB ILE A 301 -19.961 -21.681 -1.008 1.00 49.78 C ANISOU 2136 CB ILE A 301 6738 6693 5484 681 -115 -661 C ATOM 2137 CG1 ILE A 301 -20.172 -20.795 -2.248 1.00 43.28 C ANISOU 2137 CG1 ILE A 301 5620 5939 4887 476 -128 -721 C ATOM 2138 CG2 ILE A 301 -18.455 -22.001 -0.864 1.00 52.24 C ANISOU 2138 CG2 ILE A 301 7028 7056 5764 793 -395 -723 C ATOM 2139 CD1 ILE A 301 -21.590 -20.198 -2.423 1.00 40.69 C ANISOU 2139 CD1 ILE A 301 5264 5580 4617 384 75 -692 C ATOM 2140 N PHE A 302 -19.358 -24.938 -1.455 1.00 43.43 N ANISOU 2140 N PHE A 302 6019 5731 4750 796 50 -474 N ATOM 2141 CA PHE A 302 -18.720 -25.975 -2.278 1.00 50.33 C ANISOU 2141 CA PHE A 302 6772 6586 5764 785 20 -481 C ATOM 2142 C PHE A 302 -19.745 -26.936 -2.857 1.00 49.38 C ANISOU 2142 C PHE A 302 6629 6326 5808 666 279 -425 C ATOM 2143 O PHE A 302 -19.599 -27.375 -4.000 1.00 50.71 O ANISOU 2143 O PHE A 302 6610 6511 6147 568 265 -500 O ATOM 2144 CB PHE A 302 -17.674 -26.766 -1.482 1.00 42.79 C ANISOU 2144 CB PHE A 302 6002 5592 4664 1029 -118 -434 C ATOM 2145 CG PHE A 302 -16.546 -25.933 -0.981 1.00 47.03 C ANISOU 2145 CG PHE A 302 6510 6263 5098 1149 -438 -535 C ATOM 2146 CD1 PHE A 302 -16.182 -24.765 -1.645 1.00 47.68 C ANISOU 2146 CD1 PHE A 302 6320 6476 5320 998 -578 -667 C ATOM 2147 CD2 PHE A 302 -15.830 -26.315 0.149 1.00 57.22 C ANISOU 2147 CD2 PHE A 302 8039 7534 6169 1421 -612 -504 C ATOM 2148 CE1 PHE A 302 -15.136 -23.985 -1.178 1.00 49.23 C ANISOU 2148 CE1 PHE A 302 6446 6761 5497 1080 -881 -783 C ATOM 2149 CE2 PHE A 302 -14.772 -25.535 0.611 1.00 54.81 C ANISOU 2149 CE2 PHE A 302 7667 7348 5809 1530 -965 -644 C ATOM 2150 CZ PHE A 302 -14.430 -24.383 -0.046 1.00 49.12 C ANISOU 2150 CZ PHE A 302 6640 6735 5287 1343 -1095 -792 C ATOM 2151 N ILE A 303 -20.772 -27.291 -2.070 1.00 51.70 N ANISOU 2151 N ILE A 303 7110 6469 6064 683 524 -303 N ATOM 2152 CA ILE A 303 -21.891 -28.074 -2.593 1.00 52.55 C ANISOU 2152 CA ILE A 303 7137 6417 6411 528 774 -272 C ATOM 2153 C ILE A 303 -22.554 -27.322 -3.730 1.00 53.03 C ANISOU 2153 C ILE A 303 6905 6591 6652 321 737 -407 C ATOM 2154 O ILE A 303 -22.794 -27.864 -4.823 1.00 50.96 O ANISOU 2154 O ILE A 303 6466 6305 6592 200 728 -502 O ATOM 2155 CB ILE A 303 -22.904 -28.384 -1.472 1.00 48.39 C ANISOU 2155 CB ILE A 303 6831 5710 5844 576 1089 -97 C ATOM 2156 CG1 ILE A 303 -22.256 -29.199 -0.350 1.00 53.97 C ANISOU 2156 CG1 ILE A 303 7887 6295 6326 828 1139 70 C ATOM 2157 CG2 ILE A 303 -24.145 -29.080 -2.038 1.00 47.99 C ANISOU 2157 CG2 ILE A 303 6616 5479 6138 374 1347 -90 C ATOM 2158 CD1 ILE A 303 -23.186 -29.464 0.842 1.00 56.88 C ANISOU 2158 CD1 ILE A 303 8532 6486 6593 922 1501 287 C ATOM 2159 N PHE A 304 -22.828 -26.047 -3.492 1.00 45.26 N ANISOU 2159 N PHE A 304 5887 5731 5580 305 692 -428 N ATOM 2160 CA PHE A 304 -23.551 -25.255 -4.469 1.00 39.60 C ANISOU 2160 CA PHE A 304 4925 5111 5012 146 665 -525 C ATOM 2161 C PHE A 304 -22.754 -25.096 -5.739 1.00 43.34 C ANISOU 2161 C PHE A 304 5221 5724 5523 100 459 -638 C ATOM 2162 O PHE A 304 -23.326 -25.119 -6.834 1.00 46.85 O ANISOU 2162 O PHE A 304 5488 6205 6107 -9 446 -722 O ATOM 2163 CB PHE A 304 -23.890 -23.878 -3.866 1.00 48.07 C ANISOU 2163 CB PHE A 304 6031 6262 5970 172 658 -514 C ATOM 2164 CG PHE A 304 -24.121 -22.794 -4.894 1.00 43.95 C ANISOU 2164 CG PHE A 304 5286 5876 5536 68 538 -606 C ATOM 2165 CD1 PHE A 304 -25.324 -22.703 -5.576 1.00 52.69 C ANISOU 2165 CD1 PHE A 304 6215 6975 6831 -43 626 -639 C ATOM 2166 CD2 PHE A 304 -23.136 -21.866 -5.173 1.00 50.22 C ANISOU 2166 CD2 PHE A 304 6045 6791 6246 91 338 -652 C ATOM 2167 CE1 PHE A 304 -25.536 -21.692 -6.514 1.00 54.80 C ANISOU 2167 CE1 PHE A 304 6314 7366 7143 -95 505 -701 C ATOM 2168 CE2 PHE A 304 -23.343 -20.838 -6.101 1.00 51.59 C ANISOU 2168 CE2 PHE A 304 6049 7061 6491 14 264 -695 C ATOM 2169 CZ PHE A 304 -24.543 -20.766 -6.777 1.00 53.06 C ANISOU 2169 CZ PHE A 304 6101 7251 6808 -62 343 -712 C ATOM 2170 N ALA A 305 -21.428 -24.945 -5.609 1.00 45.09 N ANISOU 2170 N ALA A 305 5487 6025 5620 200 297 -646 N ATOM 2171 CA ALA A 305 -20.583 -24.759 -6.786 1.00 45.75 C ANISOU 2171 CA ALA A 305 5399 6241 5743 174 157 -728 C ATOM 2172 C ALA A 305 -20.411 -26.058 -7.569 1.00 42.99 C ANISOU 2172 C ALA A 305 5019 5834 5481 179 187 -780 C ATOM 2173 O ALA A 305 -20.343 -26.040 -8.802 1.00 47.20 O ANISOU 2173 O ALA A 305 5416 6457 6061 133 147 -866 O ATOM 2174 CB ALA A 305 -19.212 -24.206 -6.385 1.00 44.03 C ANISOU 2174 CB ALA A 305 5181 6108 5440 268 -8 -728 C ATOM 2175 N GLY A 306 -20.380 -27.195 -6.882 1.00 46.43 N ANISOU 2175 N GLY A 306 5607 6107 5929 251 267 -729 N ATOM 2176 CA GLY A 306 -20.056 -28.427 -7.565 1.00 45.98 C ANISOU 2176 CA GLY A 306 5539 5966 5966 278 280 -793 C ATOM 2177 C GLY A 306 -21.231 -29.264 -8.046 1.00 48.15 C ANISOU 2177 C GLY A 306 5784 6079 6431 158 404 -858 C ATOM 2178 O GLY A 306 -21.083 -30.080 -8.962 1.00 47.24 O ANISOU 2178 O GLY A 306 5619 5921 6408 153 374 -981 O ATOM 2179 N TYR A 307 -22.398 -29.084 -7.449 1.00 50.46 N ANISOU 2179 N TYR A 307 6094 6272 6808 66 542 -797 N ATOM 2180 CA TYR A 307 -23.442 -30.076 -7.626 1.00 48.86 C ANISOU 2180 CA TYR A 307 5856 5847 6862 -47 685 -842 C ATOM 2181 C TYR A 307 -23.983 -30.076 -9.037 1.00 52.85 C ANISOU 2181 C TYR A 307 6150 6423 7508 -161 561 -1055 C ATOM 2182 O TYR A 307 -23.792 -31.050 -9.778 1.00 44.87 O ANISOU 2182 O TYR A 307 5126 5319 6602 -162 510 -1193 O ATOM 2183 CB TYR A 307 -24.567 -29.851 -6.639 1.00 49.94 C ANISOU 2183 CB TYR A 307 6025 5860 7092 -114 903 -713 C ATOM 2184 CG TYR A 307 -25.795 -30.680 -6.905 1.00 55.53 C ANISOU 2184 CG TYR A 307 6602 6338 8157 -279 1059 -775 C ATOM 2185 CD1 TYR A 307 -27.037 -30.077 -6.975 1.00 43.79 C ANISOU 2185 CD1 TYR A 307 4923 4867 6849 -410 1133 -807 C ATOM 2186 CD2 TYR A 307 -25.713 -32.067 -7.080 1.00 56.38 C ANISOU 2186 CD2 TYR A 307 6759 6194 8468 -302 1129 -813 C ATOM 2187 CE1 TYR A 307 -28.174 -30.815 -7.189 1.00 64.37 C ANISOU 2187 CE1 TYR A 307 7353 7252 9851 -575 1265 -880 C ATOM 2188 CE2 TYR A 307 -26.850 -32.822 -7.320 1.00 67.11 C ANISOU 2188 CE2 TYR A 307 7965 7306 10228 -480 1263 -893 C ATOM 2189 CZ TYR A 307 -28.082 -32.178 -7.366 1.00 71.86 C ANISOU 2189 CZ TYR A 307 8340 7939 11026 -623 1326 -929 C ATOM 2190 OH TYR A 307 -29.233 -32.885 -7.597 1.00 76.56 O ANISOU 2190 OH TYR A 307 8720 8285 12083 -815 1445 -1028 O ATOM 2191 N GLU A 308 -24.650 -28.999 -9.434 1.00 43.95 N ANISOU 2191 N GLU A 308 4877 5456 6368 -231 496 -1096 N ATOM 2192 CA GLU A 308 -25.316 -29.051 -10.725 1.00 47.14 C ANISOU 2192 CA GLU A 308 5101 5918 6892 -310 356 -1303 C ATOM 2193 C GLU A 308 -24.402 -28.645 -11.868 1.00 51.10 C ANISOU 2193 C GLU A 308 5598 6647 7170 -210 172 -1396 C ATOM 2194 O GLU A 308 -24.686 -28.978 -13.025 1.00 58.79 O ANISOU 2194 O GLU A 308 6498 7664 8175 -213 38 -1589 O ATOM 2195 CB GLU A 308 -26.570 -28.182 -10.737 1.00 50.03 C ANISOU 2195 CB GLU A 308 5297 6337 7374 -405 360 -1314 C ATOM 2196 CG GLU A 308 -27.510 -28.560 -11.891 1.00 65.60 C ANISOU 2196 CG GLU A 308 7070 8298 9555 -489 204 -1554 C ATOM 2197 CD GLU A 308 -28.263 -27.378 -12.487 1.00 81.83 C ANISOU 2197 CD GLU A 308 8965 10551 11576 -487 63 -1602 C ATOM 2198 OE1 GLU A 308 -28.378 -26.327 -11.813 1.00 86.36 O ANISOU 2198 OE1 GLU A 308 9550 11201 12064 -466 152 -1439 O ATOM 2199 OE2 GLU A 308 -28.734 -27.507 -13.637 1.00 84.64 O ANISOU 2199 OE2 GLU A 308 9201 10979 11979 -483 -153 -1812 O ATOM 2200 N THR A 309 -23.292 -27.979 -11.565 1.00 46.30 N ANISOU 2200 N THR A 309 5069 6174 6348 -110 167 -1269 N ATOM 2201 CA THR A 309 -22.300 -27.682 -12.589 1.00 54.90 C ANISOU 2201 CA THR A 309 6149 7452 7260 -10 65 -1321 C ATOM 2202 C THR A 309 -21.692 -28.966 -13.156 1.00 52.85 C ANISOU 2202 C THR A 309 5949 7111 7021 66 53 -1448 C ATOM 2203 O THR A 309 -21.651 -29.162 -14.374 1.00 48.92 O ANISOU 2203 O THR A 309 5429 6705 6453 118 -33 -1603 O ATOM 2204 CB THR A 309 -21.214 -26.778 -11.993 1.00 43.69 C ANISOU 2204 CB THR A 309 4757 6141 5701 55 81 -1163 C ATOM 2205 OG1 THR A 309 -20.682 -27.413 -10.837 1.00 46.92 O ANISOU 2205 OG1 THR A 309 5275 6412 6139 102 140 -1079 O ATOM 2206 CG2 THR A 309 -21.855 -25.415 -11.572 1.00 38.97 C ANISOU 2206 CG2 THR A 309 4111 5612 5084 -11 80 -1071 C ATOM 2207 N THR A 310 -21.190 -29.831 -12.272 1.00 43.52 N ANISOU 2207 N THR A 310 4868 5756 5911 105 136 -1380 N ATOM 2208 CA THR A 310 -20.562 -31.086 -12.677 1.00 50.34 C ANISOU 2208 CA THR A 310 5804 6505 6818 199 139 -1488 C ATOM 2209 C THR A 310 -21.524 -31.941 -13.493 1.00 55.62 C ANISOU 2209 C THR A 310 6445 7036 7651 121 91 -1713 C ATOM 2210 O THR A 310 -21.137 -32.509 -14.521 1.00 47.83 O ANISOU 2210 O THR A 310 5481 6078 6613 210 19 -1895 O ATOM 2211 CB THR A 310 -20.103 -31.866 -11.447 1.00 50.01 C ANISOU 2211 CB THR A 310 5896 6256 6848 259 240 -1350 C ATOM 2212 OG1 THR A 310 -19.264 -31.040 -10.633 1.00 50.11 O ANISOU 2212 OG1 THR A 310 5928 6400 6713 339 225 -1180 O ATOM 2213 CG2 THR A 310 -19.351 -33.168 -11.859 1.00 51.88 C ANISOU 2213 CG2 THR A 310 6214 6356 7141 388 245 -1452 C ATOM 2214 N SER A 311 -22.790 -32.047 -13.050 1.00 46.82 N ANISOU 2214 N SER A 311 5272 5764 6755 -39 130 -1722 N ATOM 2215 CA SER A 311 -23.710 -32.873 -13.818 1.00 55.89 C ANISOU 2215 CA SER A 311 6348 6759 8128 -131 48 -1973 C ATOM 2216 C SER A 311 -24.026 -32.229 -15.166 1.00 58.77 C ANISOU 2216 C SER A 311 6621 7369 8340 -97 -163 -2169 C ATOM 2217 O SER A 311 -24.212 -32.947 -16.164 1.00 57.19 O ANISOU 2217 O SER A 311 6424 7124 8179 -66 -305 -2439 O ATOM 2218 CB SER A 311 -24.966 -33.180 -12.998 1.00 47.39 C ANISOU 2218 CB SER A 311 5183 5431 7391 -319 171 -1929 C ATOM 2219 OG SER A 311 -25.744 -32.054 -12.676 1.00 59.91 O ANISOU 2219 OG SER A 311 6642 7152 8967 -398 183 -1831 O ATOM 2220 N SER A 312 -24.011 -30.889 -15.235 1.00 52.28 N ANISOU 2220 N SER A 312 5748 6800 7316 -73 -192 -2041 N ATOM 2221 CA SER A 312 -24.291 -30.221 -16.503 1.00 50.65 C ANISOU 2221 CA SER A 312 5495 6828 6921 -1 -377 -2182 C ATOM 2222 C SER A 312 -23.179 -30.472 -17.500 1.00 55.85 C ANISOU 2222 C SER A 312 6284 7628 7310 190 -410 -2265 C ATOM 2223 O SER A 312 -23.434 -30.816 -18.659 1.00 63.15 O ANISOU 2223 O SER A 312 7243 8617 8135 278 -571 -2506 O ATOM 2224 CB SER A 312 -24.473 -28.715 -16.326 1.00 41.89 C ANISOU 2224 CB SER A 312 4325 5921 5671 -4 -368 -1994 C ATOM 2225 OG SER A 312 -25.690 -28.451 -15.684 1.00 68.22 O ANISOU 2225 OG SER A 312 7522 9156 9243 -149 -361 -1973 O ATOM 2226 N VAL A 313 -21.936 -30.306 -17.069 1.00 54.38 N ANISOU 2226 N VAL A 313 6165 7494 7004 273 -263 -2081 N ATOM 2227 CA VAL A 313 -20.838 -30.524 -18.001 1.00 60.01 C ANISOU 2227 CA VAL A 313 6971 8342 7489 466 -241 -2141 C ATOM 2228 C VAL A 313 -20.801 -31.983 -18.452 1.00 59.44 C ANISOU 2228 C VAL A 313 6987 8090 7506 527 -289 -2397 C ATOM 2229 O VAL A 313 -20.614 -32.273 -19.637 1.00 57.26 O ANISOU 2229 O VAL A 313 6797 7916 7042 680 -365 -2594 O ATOM 2230 CB VAL A 313 -19.506 -30.071 -17.382 1.00 55.15 C ANISOU 2230 CB VAL A 313 6346 7799 6809 530 -80 -1905 C ATOM 2231 CG1 VAL A 313 -18.386 -30.386 -18.322 1.00 46.96 C ANISOU 2231 CG1 VAL A 313 5369 6883 5593 731 -9 -1964 C ATOM 2232 CG2 VAL A 313 -19.568 -28.570 -17.089 1.00 49.95 C ANISOU 2232 CG2 VAL A 313 5605 7300 6076 468 -54 -1697 C ATOM 2233 N LEU A 314 -21.029 -32.916 -17.528 1.00 53.81 N ANISOU 2233 N LEU A 314 6276 7091 7077 423 -240 -2400 N ATOM 2234 CA LEU A 314 -20.975 -34.324 -17.889 1.00 60.30 C ANISOU 2234 CA LEU A 314 7190 7687 8036 472 -273 -2637 C ATOM 2235 C LEU A 314 -22.037 -34.647 -18.929 1.00 61.12 C ANISOU 2235 C LEU A 314 7274 7766 8184 437 -492 -2969 C ATOM 2236 O LEU A 314 -21.804 -35.455 -19.836 1.00 66.93 O ANISOU 2236 O LEU A 314 8118 8458 8854 568 -582 -3239 O ATOM 2237 CB LEU A 314 -21.124 -35.195 -16.632 1.00 57.84 C ANISOU 2237 CB LEU A 314 6896 7036 8045 359 -150 -2531 C ATOM 2238 CG LEU A 314 -19.864 -35.259 -15.736 1.00 60.33 C ANISOU 2238 CG LEU A 314 7283 7346 8294 480 8 -2280 C ATOM 2239 CD1 LEU A 314 -20.090 -35.977 -14.414 1.00 48.51 C ANISOU 2239 CD1 LEU A 314 5850 5533 7047 402 134 -2122 C ATOM 2240 CD2 LEU A 314 -18.708 -35.884 -16.489 1.00 56.62 C ANISOU 2240 CD2 LEU A 314 6900 6921 7693 706 20 -2398 C ATOM 2241 N SER A 315 -23.190 -33.984 -18.837 1.00 52.89 N ANISOU 2241 N SER A 315 6092 6762 7240 284 -598 -2971 N ATOM 2242 CA SER A 315 -24.247 -34.173 -19.812 1.00 54.93 C ANISOU 2242 CA SER A 315 6292 7025 7552 260 -865 -3300 C ATOM 2243 C SER A 315 -23.867 -33.563 -21.143 1.00 59.15 C ANISOU 2243 C SER A 315 6943 7890 7640 497 -1005 -3409 C ATOM 2244 O SER A 315 -24.096 -34.175 -22.194 1.00 70.22 O ANISOU 2244 O SER A 315 8434 9292 8954 613 -1215 -3749 O ATOM 2245 CB SER A 315 -25.566 -33.579 -19.305 1.00 64.40 C ANISOU 2245 CB SER A 315 7273 8187 9008 53 -933 -3254 C ATOM 2246 OG SER A 315 -26.090 -34.322 -18.214 1.00 67.73 O ANISOU 2246 OG SER A 315 7596 8265 9872 -159 -787 -3197 O ATOM 2247 N PHE A 316 -23.268 -32.374 -21.133 1.00 57.48 N ANISOU 2247 N PHE A 316 6754 7947 7139 585 -884 -3129 N ATOM 2248 CA PHE A 316 -22.793 -31.815 -22.395 1.00 63.63 C ANISOU 2248 CA PHE A 316 7680 9022 7476 836 -940 -3176 C ATOM 2249 C PHE A 316 -21.726 -32.712 -23.030 1.00 65.78 C ANISOU 2249 C PHE A 316 8137 9285 7573 1044 -853 -3316 C ATOM 2250 O PHE A 316 -21.701 -32.884 -24.252 1.00 66.13 O ANISOU 2250 O PHE A 316 8343 9468 7314 1262 -980 -3545 O ATOM 2251 CB PHE A 316 -22.253 -30.398 -22.194 1.00 55.70 C ANISOU 2251 CB PHE A 316 6654 8249 6262 871 -768 -2817 C ATOM 2252 CG PHE A 316 -23.335 -29.327 -22.091 1.00 55.69 C ANISOU 2252 CG PHE A 316 6533 8338 6288 777 -900 -2734 C ATOM 2253 CD1 PHE A 316 -23.518 -28.623 -20.915 1.00 47.29 C ANISOU 2253 CD1 PHE A 316 5325 7210 5432 594 -779 -2479 C ATOM 2254 CD2 PHE A 316 -24.138 -29.010 -23.179 1.00 60.93 C ANISOU 2254 CD2 PHE A 316 7245 9156 6748 906 -1153 -2916 C ATOM 2255 CE1 PHE A 316 -24.488 -27.638 -20.803 1.00 64.09 C ANISOU 2255 CE1 PHE A 316 7344 9410 7599 529 -879 -2403 C ATOM 2256 CE2 PHE A 316 -25.116 -28.026 -23.077 1.00 69.05 C ANISOU 2256 CE2 PHE A 316 8153 10264 7820 847 -1280 -2833 C ATOM 2257 CZ PHE A 316 -25.287 -27.334 -21.885 1.00 67.72 C ANISOU 2257 CZ PHE A 316 7825 10015 7889 653 -1126 -2572 C ATOM 2258 N ILE A 317 -20.827 -33.278 -22.221 1.00 62.67 N ANISOU 2258 N ILE A 317 7734 8735 7343 1013 -640 -3184 N ATOM 2259 CA ILE A 317 -19.787 -34.129 -22.782 1.00 57.54 C ANISOU 2259 CA ILE A 317 7238 8068 6557 1229 -538 -3309 C ATOM 2260 C ILE A 317 -20.406 -35.349 -23.448 1.00 67.22 C ANISOU 2260 C ILE A 317 8571 9100 7870 1270 -757 -3737 C ATOM 2261 O ILE A 317 -20.021 -35.740 -24.560 1.00 69.77 O ANISOU 2261 O ILE A 317 9080 9523 7907 1519 -802 -3970 O ATOM 2262 CB ILE A 317 -18.786 -34.530 -21.694 1.00 61.67 C ANISOU 2262 CB ILE A 317 7706 8441 7285 1195 -310 -3091 C ATOM 2263 CG1 ILE A 317 -18.090 -33.290 -21.129 1.00 58.82 C ANISOU 2263 CG1 ILE A 317 7231 8280 6839 1170 -135 -2721 C ATOM 2264 CG2 ILE A 317 -17.751 -35.451 -22.269 1.00 64.12 C ANISOU 2264 CG2 ILE A 317 8151 8717 7493 1434 -205 -3233 C ATOM 2265 CD1 ILE A 317 -17.041 -33.590 -20.069 1.00 59.79 C ANISOU 2265 CD1 ILE A 317 7286 8292 7138 1172 34 -2521 C ATOM 2266 N MET A 318 -21.391 -35.960 -22.794 1.00 67.73 N ANISOU 2266 N MET A 318 8524 8870 8341 1033 -888 -3857 N ATOM 2267 CA MET A 318 -21.938 -37.194 -23.341 1.00 74.89 C ANISOU 2267 CA MET A 318 9503 9524 9426 1039 -1095 -4282 C ATOM 2268 C MET A 318 -22.731 -36.940 -24.610 1.00 78.40 C ANISOU 2268 C MET A 318 10009 10152 9628 1152 -1423 -4617 C ATOM 2269 O MET A 318 -22.721 -37.777 -25.522 1.00 79.40 O ANISOU 2269 O MET A 318 10300 10211 9658 1315 -1596 -5004 O ATOM 2270 CB MET A 318 -22.798 -37.890 -22.297 1.00 73.28 C ANISOU 2270 CB MET A 318 9136 8928 9779 737 -1108 -4298 C ATOM 2271 CG MET A 318 -22.012 -38.348 -21.104 1.00 73.53 C ANISOU 2271 CG MET A 318 9179 8748 10012 686 -814 -4005 C ATOM 2272 SD MET A 318 -20.477 -39.168 -21.609 1.00 88.67 S ANISOU 2272 SD MET A 318 11325 10660 11706 1003 -672 -4079 S ATOM 2273 CE MET A 318 -21.047 -40.482 -22.695 1.00 68.97 C ANISOU 2273 CE MET A 318 8963 7902 9339 1067 -932 -4650 C ATOM 2274 N TYR A 319 -23.426 -35.801 -24.681 1.00 76.07 N ANISOU 2274 N TYR A 319 9600 10082 9223 1093 -1531 -4489 N ATOM 2275 CA TYR A 319 -24.054 -35.400 -25.935 1.00 83.65 C ANISOU 2275 CA TYR A 319 10652 11277 9853 1273 -1850 -4758 C ATOM 2276 C TYR A 319 -23.028 -35.348 -27.049 1.00 81.10 C ANISOU 2276 C TYR A 319 10636 11209 8971 1646 -1768 -4811 C ATOM 2277 O TYR A 319 -23.274 -35.833 -28.160 1.00 85.04 O ANISOU 2277 O TYR A 319 11287 11733 9290 1809 -1964 -5016 O ATOM 2278 CB TYR A 319 -24.741 -34.034 -25.795 1.00 80.64 C ANISOU 2278 CB TYR A 319 10125 11125 9390 1205 -1915 -4521 C ATOM 2279 CG TYR A 319 -25.178 -33.451 -27.138 1.00 82.49 C ANISOU 2279 CG TYR A 319 10511 11657 9172 1473 -2204 -4696 C ATOM 2280 CD1 TYR A 319 -26.426 -33.745 -27.678 1.00 88.25 C ANISOU 2280 CD1 TYR A 319 11132 12307 10091 1423 -2562 -4920 C ATOM 2281 CD2 TYR A 319 -24.343 -32.606 -27.864 1.00 85.01 C ANISOU 2281 CD2 TYR A 319 11065 12305 8931 1765 -2044 -4489 C ATOM 2282 CE1 TYR A 319 -26.825 -33.216 -28.909 1.00 96.82 C ANISOU 2282 CE1 TYR A 319 12364 13639 10786 1682 -2790 -4959 C ATOM 2283 CE2 TYR A 319 -24.737 -32.077 -29.095 1.00 89.99 C ANISOU 2283 CE2 TYR A 319 11859 13162 9172 2013 -2233 -4495 C ATOM 2284 CZ TYR A 319 -25.972 -32.384 -29.608 1.00 94.45 C ANISOU 2284 CZ TYR A 319 12335 13648 9903 1982 -2622 -4739 C ATOM 2285 OH TYR A 319 -26.343 -31.857 -30.824 1.00 98.41 O ANISOU 2285 OH TYR A 319 13016 14373 10003 2262 -2819 -4750 O ATOM 2286 N GLU A 320 -21.876 -34.736 -26.775 1.00 72.44 N ANISOU 2286 N GLU A 320 9584 10272 7667 1736 -1404 -4425 N ATOM 2287 CA GLU A 320 -20.854 -34.635 -27.803 1.00 76.20 C ANISOU 2287 CA GLU A 320 10324 10990 7639 2091 -1243 -4426 C ATOM 2288 C GLU A 320 -20.315 -36.007 -28.193 1.00 83.41 C ANISOU 2288 C GLU A 320 11390 11703 8598 2217 -1222 -4692 C ATOM 2289 O GLU A 320 -19.960 -36.236 -29.356 1.00 85.84 O ANISOU 2289 O GLU A 320 11926 12134 8556 2474 -1220 -4765 O ATOM 2290 CB GLU A 320 -19.730 -33.717 -27.325 1.00 69.33 C ANISOU 2290 CB GLU A 320 9392 10283 6669 2108 -837 -3943 C ATOM 2291 CG GLU A 320 -20.167 -32.272 -27.174 1.00 71.65 C ANISOU 2291 CG GLU A 320 9583 10777 6864 2023 -832 -3636 C ATOM 2292 CD GLU A 320 -20.875 -31.731 -28.411 1.00 85.93 C ANISOU 2292 CD GLU A 320 11583 12826 8241 2250 -1072 -3788 C ATOM 2293 OE1 GLU A 320 -21.734 -30.847 -28.249 1.00 87.22 O ANISOU 2293 OE1 GLU A 320 11639 13062 8439 2143 -1226 -3676 O ATOM 2294 OE2 GLU A 320 -20.576 -32.174 -29.547 1.00 92.52 O ANISOU 2294 OE2 GLU A 320 12682 13768 8705 2548 -1105 -3989 O ATOM 2295 N LEU A 321 -20.267 -36.940 -27.251 1.00 70.86 N ANISOU 2295 N LEU A 321 9687 9781 7457 2035 -1191 -4797 N ATOM 2296 CA LEU A 321 -19.752 -38.253 -27.603 1.00 83.11 C ANISOU 2296 CA LEU A 321 11382 11107 9087 2146 -1156 -5000 C ATOM 2297 C LEU A 321 -20.770 -39.035 -28.424 1.00 88.62 C ANISOU 2297 C LEU A 321 12150 11654 9866 2110 -1516 -5342 C ATOM 2298 O LEU A 321 -20.409 -39.711 -29.397 1.00 95.64 O ANISOU 2298 O LEU A 321 13253 12546 10538 2325 -1544 -5518 O ATOM 2299 CB LEU A 321 -19.354 -38.998 -26.333 1.00 83.80 C ANISOU 2299 CB LEU A 321 11345 10859 9635 1984 -991 -4951 C ATOM 2300 CG LEU A 321 -18.268 -38.276 -25.533 1.00 77.45 C ANISOU 2300 CG LEU A 321 10426 10200 8802 1983 -633 -4461 C ATOM 2301 CD1 LEU A 321 -17.902 -39.104 -24.313 1.00 74.08 C ANISOU 2301 CD1 LEU A 321 9902 9429 8816 1837 -498 -4335 C ATOM 2302 CD2 LEU A 321 -17.054 -38.022 -26.413 1.00 80.78 C ANISOU 2302 CD2 LEU A 321 11002 10902 8789 2331 -398 -4404 C ATOM 2303 N ALA A 322 -22.050 -38.931 -28.064 1.00 78.14 N ANISOU 2303 N ALA A 322 10626 10203 8861 1849 -1788 -5439 N ATOM 2304 CA ALA A 322 -23.092 -39.666 -28.771 1.00 89.03 C ANISOU 2304 CA ALA A 322 12001 11427 10399 1794 -2146 -5769 C ATOM 2305 C ALA A 322 -23.308 -39.132 -30.181 1.00 95.74 C ANISOU 2305 C ALA A 322 13036 12607 10736 2068 -2347 -5849 C ATOM 2306 O ALA A 322 -23.627 -39.903 -31.094 1.00 98.52 O ANISOU 2306 O ALA A 322 13513 12885 11034 2180 -2576 -6146 O ATOM 2307 CB ALA A 322 -24.397 -39.612 -27.983 1.00 85.71 C ANISOU 2307 CB ALA A 322 11265 10799 10501 1444 -2340 -5809 C ATOM 2308 N THR A 323 -23.142 -37.829 -30.383 1.00 98.25 N ANISOU 2308 N THR A 323 13385 13273 10674 2192 -2264 -5586 N ATOM 2309 CA THR A 323 -23.237 -37.244 -31.709 1.00104.84 C ANISOU 2309 CA THR A 323 14437 14417 10981 2494 -2397 -5597 C ATOM 2310 C THR A 323 -21.903 -37.268 -32.458 1.00103.42 C ANISOU 2310 C THR A 323 14562 14418 10316 2823 -2085 -5483 C ATOM 2311 O THR A 323 -21.809 -36.697 -33.549 1.00115.72 O ANISOU 2311 O THR A 323 16338 16243 11388 3104 -2106 -5424 O ATOM 2312 CB THR A 323 -23.771 -35.802 -31.623 1.00104.02 C ANISOU 2312 CB THR A 323 14234 14574 10714 2482 -2447 -5345 C ATOM 2313 OG1 THR A 323 -22.818 -34.957 -30.969 1.00100.64 O ANISOU 2313 OG1 THR A 323 13797 14295 10145 2488 -2060 -4983 O ATOM 2314 CG2 THR A 323 -25.085 -35.761 -30.851 1.00 99.40 C ANISOU 2314 CG2 THR A 323 13314 13810 10643 2157 -2718 -5443 C ATOM 2315 N HIS A 324 -20.876 -37.923 -31.907 1.00 95.63 N ANISOU 2315 N HIS A 324 13590 13280 9464 2809 -1780 -5438 N ATOM 2316 CA HIS A 324 -19.569 -38.034 -32.567 1.00 95.04 C ANISOU 2316 CA HIS A 324 13757 13350 9004 3113 -1444 -5328 C ATOM 2317 C HIS A 324 -18.946 -39.382 -32.215 1.00 94.39 C ANISOU 2317 C HIS A 324 13695 12962 9206 3089 -1330 -5512 C ATOM 2318 O HIS A 324 -17.946 -39.453 -31.490 1.00 86.95 O ANISOU 2318 O HIS A 324 12683 11971 8381 3087 -993 -5320 O ATOM 2319 CB HIS A 324 -18.655 -36.872 -32.160 1.00 88.38 C ANISOU 2319 CB HIS A 324 12862 12751 7967 3171 -1046 -4898 C ATOM 2320 CG HIS A 324 -19.134 -35.527 -32.621 1.00 90.50 C ANISOU 2320 CG HIS A 324 13161 13312 7911 3240 -1104 -4683 C ATOM 2321 ND1 HIS A 324 -19.897 -34.693 -31.826 1.00 85.67 N ANISOU 2321 ND1 HIS A 324 12329 12725 7496 3011 -1230 -4559 N ATOM 2322 CD2 HIS A 324 -18.964 -34.873 -33.797 1.00 91.54 C ANISOU 2322 CD2 HIS A 324 13531 13708 7542 3527 -1043 -4559 C ATOM 2323 CE1 HIS A 324 -20.171 -33.583 -32.490 1.00 85.35 C ANISOU 2323 CE1 HIS A 324 12389 12947 7094 3157 -1252 -4368 C ATOM 2324 NE2 HIS A 324 -19.618 -33.668 -33.689 1.00 90.25 N ANISOU 2324 NE2 HIS A 324 13293 13710 7287 3472 -1137 -4356 N ATOM 2325 N PRO A 325 -19.508 -40.485 -32.739 1.00 93.97 N ANISOU 2325 N PRO A 325 13736 12692 9279 3090 -1613 -5887 N ATOM 2326 CA PRO A 325 -19.143 -41.817 -32.221 1.00 94.85 C ANISOU 2326 CA PRO A 325 13834 12431 9775 3004 -1548 -6071 C ATOM 2327 C PRO A 325 -17.668 -42.157 -32.378 1.00102.52 C ANISOU 2327 C PRO A 325 14957 13444 10554 3254 -1145 -5951 C ATOM 2328 O PRO A 325 -17.110 -42.866 -31.527 1.00 96.80 O ANISOU 2328 O PRO A 325 14150 12457 10173 3175 -970 -5927 O ATOM 2329 CB PRO A 325 -20.028 -42.770 -33.040 1.00105.98 C ANISOU 2329 CB PRO A 325 15347 13661 11258 3009 -1936 -6498 C ATOM 2330 CG PRO A 325 -21.097 -41.922 -33.633 1.00105.21 C ANISOU 2330 CG PRO A 325 15211 13792 10970 3006 -2262 -6535 C ATOM 2331 CD PRO A 325 -20.499 -40.565 -33.823 1.00101.65 C ANISOU 2331 CD PRO A 325 14824 13735 10063 3182 -2011 -6160 C ATOM 2332 N ASP A 326 -17.030 -41.669 -33.447 1.00104.37 N ANISOU 2332 N ASP A 326 15401 13990 10264 3565 -981 -5859 N ATOM 2333 CA ASP A 326 -15.595 -41.866 -33.643 1.00103.73 C ANISOU 2333 CA ASP A 326 15420 13982 10010 3809 -552 -5706 C ATOM 2334 C ASP A 326 -14.796 -41.278 -32.490 1.00 93.32 C ANISOU 2334 C ASP A 326 13859 12696 8902 3710 -216 -5343 C ATOM 2335 O ASP A 326 -13.845 -41.895 -31.998 1.00 92.99 O ANISOU 2335 O ASP A 326 13762 12507 9062 3768 40 -5292 O ATOM 2336 CB ASP A 326 -15.175 -41.206 -34.948 1.00106.60 C ANISOU 2336 CB ASP A 326 16020 14697 9785 4128 -409 -5606 C ATOM 2337 CG ASP A 326 -15.618 -39.757 -35.006 1.00106.32 C ANISOU 2337 CG ASP A 326 15922 14955 9520 4089 -430 -5323 C ATOM 2338 OD1 ASP A 326 -16.787 -39.489 -34.651 1.00102.04 O ANISOU 2338 OD1 ASP A 326 15263 14359 9147 3872 -786 -5414 O ATOM 2339 OD2 ASP A 326 -14.795 -38.891 -35.360 1.00109.09 O ANISOU 2339 OD2 ASP A 326 16318 15567 9566 4262 -73 -5000 O ATOM 2340 N VAL A 327 -15.146 -40.061 -32.075 1.00 93.68 N ANISOU 2340 N VAL A 327 13755 12942 8898 3583 -217 -5089 N ATOM 2341 CA VAL A 327 -14.570 -39.486 -30.864 1.00 88.16 C ANISOU 2341 CA VAL A 327 12796 12254 8447 3452 29 -4782 C ATOM 2342 C VAL A 327 -14.791 -40.428 -29.690 1.00 90.11 C ANISOU 2342 C VAL A 327 12897 12123 9218 3240 -81 -4917 C ATOM 2343 O VAL A 327 -13.850 -40.798 -28.974 1.00 88.46 O ANISOU 2343 O VAL A 327 12581 11802 9225 3284 164 -4793 O ATOM 2344 CB VAL A 327 -15.179 -38.098 -30.597 1.00 81.31 C ANISOU 2344 CB VAL A 327 11804 11617 7472 3315 -35 -4553 C ATOM 2345 CG1 VAL A 327 -14.448 -37.415 -29.457 1.00 76.87 C ANISOU 2345 CG1 VAL A 327 10982 11111 7115 3222 249 -4229 C ATOM 2346 CG2 VAL A 327 -15.125 -37.260 -31.864 1.00 84.02 C ANISOU 2346 CG2 VAL A 327 12346 12281 7297 3538 35 -4434 C ATOM 2347 N GLN A 328 -16.041 -40.860 -29.501 1.00 83.13 N ANISOU 2347 N GLN A 328 11998 11020 8569 3017 -447 -5164 N ATOM 2348 CA GLN A 328 -16.345 -41.776 -28.414 1.00 82.02 C ANISOU 2348 CA GLN A 328 11736 10473 8954 2798 -528 -5271 C ATOM 2349 C GLN A 328 -15.541 -43.066 -28.537 1.00 85.06 C ANISOU 2349 C GLN A 328 12251 10603 9464 2959 -393 -5409 C ATOM 2350 O GLN A 328 -15.014 -43.565 -27.534 1.00 83.47 O ANISOU 2350 O GLN A 328 11952 10166 9597 2920 -241 -5308 O ATOM 2351 CB GLN A 328 -17.844 -42.060 -28.373 1.00 82.98 C ANISOU 2351 CB GLN A 328 11804 10391 9332 2530 -916 -5516 C ATOM 2352 CG GLN A 328 -18.255 -42.917 -27.187 1.00 81.99 C ANISOU 2352 CG GLN A 328 11539 9816 9797 2265 -955 -5572 C ATOM 2353 CD GLN A 328 -19.731 -43.267 -27.194 1.00 97.30 C ANISOU 2353 CD GLN A 328 13380 11529 12060 1982 -1298 -5803 C ATOM 2354 OE1 GLN A 328 -20.182 -44.113 -26.424 1.00 97.67 O ANISOU 2354 OE1 GLN A 328 13336 11165 12609 1760 -1326 -5873 O ATOM 2355 NE2 GLN A 328 -20.493 -42.613 -28.063 1.00 95.93 N ANISOU 2355 NE2 GLN A 328 13210 11616 11622 1998 -1547 -5901 N ATOM 2356 N GLN A 329 -15.416 -43.607 -29.761 1.00 90.57 N ANISOU 2356 N GLN A 329 13180 11345 9886 3164 -443 -5634 N ATOM 2357 CA GLN A 329 -14.630 -44.826 -29.967 1.00 98.37 C ANISOU 2357 CA GLN A 329 14307 12099 10969 3340 -303 -5780 C ATOM 2358 C GLN A 329 -13.158 -44.593 -29.636 1.00 91.65 C ANISOU 2358 C GLN A 329 13385 11385 10051 3553 112 -5489 C ATOM 2359 O GLN A 329 -12.557 -45.330 -28.845 1.00 91.25 O ANISOU 2359 O GLN A 329 13268 11072 10329 3570 247 -5443 O ATOM 2360 CB GLN A 329 -14.791 -45.345 -31.415 1.00 98.82 C ANISOU 2360 CB GLN A 329 14636 12218 10694 3540 -438 -6089 C ATOM 2361 CG GLN A 329 -13.779 -46.427 -31.803 1.00102.66 C ANISOU 2361 CG GLN A 329 15288 12546 11174 3789 -222 -6214 C ATOM 2362 CD GLN A 329 -14.262 -47.367 -32.927 1.00111.23 C ANISOU 2362 CD GLN A 329 16632 13501 12129 3895 -464 -6636 C ATOM 2363 OE1 GLN A 329 -15.333 -47.172 -33.505 1.00110.56 O ANISOU 2363 OE1 GLN A 329 16600 13478 11930 3805 -809 -6835 O ATOM 2364 NE2 GLN A 329 -13.467 -48.396 -33.221 1.00112.51 N ANISOU 2364 NE2 GLN A 329 16942 13479 12326 4097 -293 -6781 N ATOM 2365 N LYS A 330 -12.561 -43.568 -30.242 1.00 91.24 N ANISOU 2365 N LYS A 330 13333 11733 9602 3722 323 -5275 N ATOM 2366 CA LYS A 330 -11.159 -43.266 -29.983 1.00 90.34 C ANISOU 2366 CA LYS A 330 13090 11766 9469 3906 729 -4985 C ATOM 2367 C LYS A 330 -10.900 -43.100 -28.487 1.00 85.91 C ANISOU 2367 C LYS A 330 12253 11076 9312 3754 788 -4763 C ATOM 2368 O LYS A 330 -9.955 -43.678 -27.942 1.00 86.22 O ANISOU 2368 O LYS A 330 12199 10977 9585 3871 978 -4678 O ATOM 2369 CB LYS A 330 -10.761 -42.008 -30.752 1.00 92.06 C ANISOU 2369 CB LYS A 330 13306 12409 9262 4033 942 -4744 C ATOM 2370 CG LYS A 330 -9.329 -41.595 -30.547 1.00 98.16 C ANISOU 2370 CG LYS A 330 13887 13343 10064 4191 1377 -4430 C ATOM 2371 CD LYS A 330 -8.953 -40.413 -31.438 1.00105.82 C ANISOU 2371 CD LYS A 330 14882 14687 10638 4308 1626 -4188 C ATOM 2372 CE LYS A 330 -7.454 -40.123 -31.341 1.00109.16 C ANISOU 2372 CE LYS A 330 15079 15234 11162 4457 2088 -3901 C ATOM 2373 NZ LYS A 330 -7.018 -39.008 -32.226 1.00111.88 N ANISOU 2373 NZ LYS A 330 15440 15895 11174 4559 2389 -3639 N ATOM 2374 N LEU A 331 -11.763 -42.343 -27.798 1.00 82.11 N ANISOU 2374 N LEU A 331 11643 10630 8925 3504 609 -4677 N ATOM 2375 CA LEU A 331 -11.618 -42.182 -26.352 1.00 85.06 C ANISOU 2375 CA LEU A 331 11778 10875 9667 3363 636 -4486 C ATOM 2376 C LEU A 331 -11.770 -43.514 -25.617 1.00 88.96 C ANISOU 2376 C LEU A 331 12320 10906 10575 3307 532 -4642 C ATOM 2377 O LEU A 331 -11.029 -43.804 -24.667 1.00 78.21 O ANISOU 2377 O LEU A 331 10829 9411 9476 3372 663 -4476 O ATOM 2378 CB LEU A 331 -12.638 -41.161 -25.836 1.00 78.28 C ANISOU 2378 CB LEU A 331 10798 10120 8825 3085 457 -4386 C ATOM 2379 CG LEU A 331 -12.721 -40.915 -24.322 1.00 72.19 C ANISOU 2379 CG LEU A 331 9792 9198 8441 2793 446 -4051 C ATOM 2380 CD1 LEU A 331 -11.341 -40.717 -23.734 1.00 73.02 C ANISOU 2380 CD1 LEU A 331 9716 9396 8631 2929 707 -3745 C ATOM 2381 CD2 LEU A 331 -13.650 -39.720 -23.954 1.00 67.64 C ANISOU 2381 CD2 LEU A 331 9088 8779 7834 2498 318 -3857 C ATOM 2382 N GLN A 332 -12.746 -44.324 -26.019 1.00 81.71 N ANISOU 2382 N GLN A 332 11576 9724 9744 3186 289 -4945 N ATOM 2383 CA GLN A 332 -12.895 -45.618 -25.379 1.00 86.46 C ANISOU 2383 CA GLN A 332 12239 9846 10765 3124 228 -5071 C ATOM 2384 C GLN A 332 -11.667 -46.487 -25.602 1.00 86.24 C ANISOU 2384 C GLN A 332 12296 9724 10748 3422 452 -5069 C ATOM 2385 O GLN A 332 -11.282 -47.241 -24.706 1.00 86.36 O ANISOU 2385 O GLN A 332 12286 9422 11104 3452 517 -4989 O ATOM 2386 CB GLN A 332 -14.150 -46.315 -25.884 1.00 87.15 C ANISOU 2386 CB GLN A 332 12466 9673 10974 2927 -64 -5402 C ATOM 2387 CG GLN A 332 -15.391 -45.910 -25.112 1.00 88.65 C ANISOU 2387 CG GLN A 332 12510 9733 11441 2576 -265 -5380 C ATOM 2388 CD GLN A 332 -16.651 -46.415 -25.759 1.00 93.16 C ANISOU 2388 CD GLN A 332 13148 10128 12120 2379 -569 -5700 C ATOM 2389 OE1 GLN A 332 -16.694 -46.610 -26.973 1.00 90.05 O ANISOU 2389 OE1 GLN A 332 12910 9874 11430 2521 -681 -5928 O ATOM 2390 NE2 GLN A 332 -17.684 -46.643 -24.959 1.00 92.44 N ANISOU 2390 NE2 GLN A 332 12928 9723 12471 2057 -698 -5712 N ATOM 2391 N GLU A 333 -11.016 -46.358 -26.762 1.00 88.83 N ANISOU 2391 N GLU A 333 12722 10322 10706 3658 590 -5129 N ATOM 2392 CA GLU A 333 -9.784 -47.108 -27.004 1.00 96.94 C ANISOU 2392 CA GLU A 333 13794 11289 11750 3951 839 -5117 C ATOM 2393 C GLU A 333 -8.637 -46.560 -26.165 1.00 94.89 C ANISOU 2393 C GLU A 333 13268 11187 11598 4073 1087 -4761 C ATOM 2394 O GLU A 333 -7.802 -47.329 -25.671 1.00 90.64 O ANISOU 2394 O GLU A 333 12687 10449 11304 4236 1213 -4698 O ATOM 2395 CB GLU A 333 -9.429 -47.082 -28.492 1.00 95.74 C ANISOU 2395 CB GLU A 333 13817 11383 11177 4167 946 -5273 C ATOM 2396 CG GLU A 333 -10.428 -47.848 -29.356 1.00110.29 C ANISOU 2396 CG GLU A 333 15931 13036 12938 4103 671 -5668 C ATOM 2397 CD GLU A 333 -10.247 -47.623 -30.851 1.00111.35 C ANISOU 2397 CD GLU A 333 16263 13465 12579 4317 728 -5814 C ATOM 2398 OE1 GLU A 333 -9.828 -46.510 -31.246 1.00112.51 O ANISOU 2398 OE1 GLU A 333 16340 14008 12401 4407 907 -5587 O ATOM 2399 OE2 GLU A 333 -10.535 -48.561 -31.629 1.00108.10 O ANISOU 2399 OE2 GLU A 333 16087 12875 12110 4399 598 -6151 O ATOM 2400 N GLU A 334 -8.596 -45.232 -25.967 1.00 92.15 N ANISOU 2400 N GLU A 334 12727 11189 11096 3995 1140 -4525 N ATOM 2401 CA GLU A 334 -7.551 -44.644 -25.126 1.00 89.42 C ANISOU 2401 CA GLU A 334 12083 10998 10893 4083 1335 -4195 C ATOM 2402 C GLU A 334 -7.689 -45.105 -23.683 1.00 86.34 C ANISOU 2402 C GLU A 334 11604 10297 10904 3996 1200 -4102 C ATOM 2403 O GLU A 334 -6.708 -45.514 -23.054 1.00 93.41 O ANISOU 2403 O GLU A 334 12369 11107 12016 4172 1309 -3951 O ATOM 2404 CB GLU A 334 -7.578 -43.114 -25.200 1.00 80.52 C ANISOU 2404 CB GLU A 334 10769 10276 9550 3985 1408 -3972 C ATOM 2405 CG GLU A 334 -6.555 -42.450 -24.263 1.00 83.11 C ANISOU 2405 CG GLU A 334 10741 10756 10081 4035 1566 -3644 C ATOM 2406 CD GLU A 334 -6.604 -40.919 -24.259 1.00 89.33 C ANISOU 2406 CD GLU A 334 11325 11890 10725 3859 1634 -3376 C ATOM 2407 OE1 GLU A 334 -5.697 -40.295 -24.853 1.00 95.62 O ANISOU 2407 OE1 GLU A 334 11969 12960 11401 4018 1922 -3243 O ATOM 2408 OE2 GLU A 334 -7.542 -40.338 -23.660 1.00 92.51 O ANISOU 2408 OE2 GLU A 334 11715 12268 11167 3539 1420 -3271 O ATOM 2409 N ILE A 335 -8.904 -45.051 -23.144 1.00 81.40 N ANISOU 2409 N ILE A 335 11047 9490 10390 3717 964 -4160 N ATOM 2410 CA ILE A 335 -9.145 -45.552 -21.797 1.00 81.51 C ANISOU 2410 CA ILE A 335 11029 9167 10775 3551 863 -3973 C ATOM 2411 C ILE A 335 -8.690 -47.003 -21.681 1.00 89.82 C ANISOU 2411 C ILE A 335 12243 9818 12068 3793 902 -4135 C ATOM 2412 O ILE A 335 -8.012 -47.390 -20.722 1.00 88.18 O ANISOU 2412 O ILE A 335 11961 9458 12087 3899 949 -3905 O ATOM 2413 CB ILE A 335 -10.631 -45.405 -21.445 1.00 82.20 C ANISOU 2413 CB ILE A 335 11186 9086 10962 3174 651 -4012 C ATOM 2414 CG1 ILE A 335 -11.005 -43.919 -21.317 1.00 79.61 C ANISOU 2414 CG1 ILE A 335 10676 9133 10439 2948 619 -3783 C ATOM 2415 CG2 ILE A 335 -10.928 -46.165 -20.187 1.00 83.76 C ANISOU 2415 CG2 ILE A 335 11427 8864 11536 3050 605 -3856 C ATOM 2416 CD1 ILE A 335 -12.497 -43.653 -21.182 1.00 74.77 C ANISOU 2416 CD1 ILE A 335 10101 8417 9890 2605 421 -3856 C ATOM 2417 N ASP A 336 -9.064 -47.826 -22.665 1.00 89.63 N ANISOU 2417 N ASP A 336 12447 9624 11984 3827 870 -4460 N ATOM 2418 CA ASP A 336 -8.727 -49.241 -22.649 1.00 93.31 C ANISOU 2418 CA ASP A 336 13086 9686 12682 3973 914 -4574 C ATOM 2419 C ASP A 336 -7.217 -49.475 -22.724 1.00 95.54 C ANISOU 2419 C ASP A 336 13262 10097 12943 4320 1144 -4433 C ATOM 2420 O ASP A 336 -6.720 -50.470 -22.186 1.00 96.24 O ANISOU 2420 O ASP A 336 13408 9860 13299 4474 1190 -4385 O ATOM 2421 CB ASP A 336 -9.443 -49.941 -23.803 1.00102.43 C ANISOU 2421 CB ASP A 336 14486 10694 13739 3904 816 -4946 C ATOM 2422 CG ASP A 336 -10.919 -50.175 -23.529 1.00101.61 C ANISOU 2422 CG ASP A 336 14471 10288 13849 3557 573 -5099 C ATOM 2423 OD1 ASP A 336 -11.341 -50.030 -22.365 1.00 97.41 O ANISOU 2423 OD1 ASP A 336 13850 9566 13597 3385 529 -4907 O ATOM 2424 OD2 ASP A 336 -11.651 -50.514 -24.488 1.00105.20 O ANISOU 2424 OD2 ASP A 336 15073 10693 14205 3459 426 -5408 O ATOM 2425 N ALA A 337 -6.470 -48.578 -23.372 1.00 94.75 N ANISOU 2425 N ALA A 337 12992 10450 12559 4444 1303 -4349 N ATOM 2426 CA ALA A 337 -5.014 -48.709 -23.387 1.00 95.62 C ANISOU 2426 CA ALA A 337 12922 10692 12718 4744 1536 -4194 C ATOM 2427 C ALA A 337 -4.414 -48.436 -22.010 1.00 93.43 C ANISOU 2427 C ALA A 337 12394 10403 12703 4795 1504 -3874 C ATOM 2428 O ALA A 337 -3.681 -49.269 -21.464 1.00 92.22 O ANISOU 2428 O ALA A 337 12217 10026 12795 4997 1538 -3794 O ATOM 2429 CB ALA A 337 -4.408 -47.769 -24.429 1.00 96.93 C ANISOU 2429 CB ALA A 337 12951 11318 12559 4828 1752 -4158 C ATOM 2430 N VAL A 338 -4.707 -47.267 -21.430 1.00 91.25 N ANISOU 2430 N VAL A 338 11931 10370 12370 4627 1421 -3691 N ATOM 2431 CA VAL A 338 -4.151 -46.946 -20.118 1.00 91.44 C ANISOU 2431 CA VAL A 338 11723 10407 12611 4684 1347 -3400 C ATOM 2432 C VAL A 338 -4.679 -47.901 -19.059 1.00 88.45 C ANISOU 2432 C VAL A 338 11554 9565 12486 4635 1178 -3341 C ATOM 2433 O VAL A 338 -3.975 -48.229 -18.101 1.00 91.24 O ANISOU 2433 O VAL A 338 11821 9811 13036 4804 1136 -3127 O ATOM 2434 CB VAL A 338 -4.460 -45.478 -19.745 1.00 95.80 C ANISOU 2434 CB VAL A 338 12057 11299 13043 4382 1282 -3161 C ATOM 2435 CG1 VAL A 338 -4.039 -45.192 -18.313 1.00 97.60 C ANISOU 2435 CG1 VAL A 338 12100 11508 13476 4340 1142 -2836 C ATOM 2436 CG2 VAL A 338 -3.749 -44.518 -20.685 1.00 98.02 C ANISOU 2436 CG2 VAL A 338 12103 12010 13131 4471 1501 -3153 C ATOM 2437 N LEU A 339 -5.917 -48.359 -19.203 1.00 92.63 N ANISOU 2437 N LEU A 339 12356 9808 13032 4405 1081 -3515 N ATOM 2438 CA LEU A 339 -6.585 -49.168 -18.186 1.00 92.76 C ANISOU 2438 CA LEU A 339 12573 9363 13311 4285 971 -3412 C ATOM 2439 C LEU A 339 -7.115 -50.457 -18.805 1.00 95.05 C ANISOU 2439 C LEU A 339 13162 9200 13753 4344 980 -3762 C ATOM 2440 O LEU A 339 -8.324 -50.601 -19.034 1.00 91.49 O ANISOU 2440 O LEU A 339 12858 8552 13354 4054 889 -3936 O ATOM 2441 CB LEU A 339 -7.718 -48.375 -17.544 1.00 80.85 C ANISOU 2441 CB LEU A 339 11050 7898 11771 3869 851 -3238 C ATOM 2442 CG LEU A 339 -7.329 -47.141 -16.741 1.00 81.80 C ANISOU 2442 CG LEU A 339 10918 8386 11778 3781 808 -2897 C ATOM 2443 CD1 LEU A 339 -8.594 -46.420 -16.319 1.00 76.39 C ANISOU 2443 CD1 LEU A 339 10258 7720 11046 3381 715 -2800 C ATOM 2444 CD2 LEU A 339 -6.505 -47.506 -15.524 1.00 82.88 C ANISOU 2444 CD2 LEU A 339 11025 8398 12067 4000 770 -2610 C ATOM 2445 N PRO A 340 -6.236 -51.415 -19.089 1.00 98.47 N ANISOU 2445 N PRO A 340 13654 9485 14273 4612 1098 -3800 N ATOM 2446 CA PRO A 340 -6.695 -52.679 -19.667 1.00100.51 C ANISOU 2446 CA PRO A 340 14191 9320 14678 4587 1124 -4064 C ATOM 2447 C PRO A 340 -7.477 -53.495 -18.650 1.00107.15 C ANISOU 2447 C PRO A 340 15238 9607 15869 4450 1058 -3962 C ATOM 2448 O PRO A 340 -7.328 -53.335 -17.437 1.00106.84 O ANISOU 2448 O PRO A 340 15162 9476 15957 4499 1029 -3644 O ATOM 2449 CB PRO A 340 -5.395 -53.378 -20.065 1.00103.30 C ANISOU 2449 CB PRO A 340 14509 9687 15054 4943 1290 -4073 C ATOM 2450 CG PRO A 340 -4.374 -52.810 -19.143 1.00101.76 C ANISOU 2450 CG PRO A 340 14046 9725 14891 5139 1303 -3727 C ATOM 2451 CD PRO A 340 -4.774 -51.379 -18.931 1.00 96.70 C ANISOU 2451 CD PRO A 340 13218 9477 14047 4939 1212 -3617 C ATOM 2452 N ASN A 341 -8.319 -54.390 -19.176 1.00115.18 N ANISOU 2452 N ASN A 341 16487 10243 17034 4282 1039 -4226 N ATOM 2453 CA ASN A 341 -9.220 -55.221 -18.368 1.00117.91 C ANISOU 2453 CA ASN A 341 17040 10012 17749 4091 1018 -4149 C ATOM 2454 C ASN A 341 -10.182 -54.375 -17.539 1.00108.72 C ANISOU 2454 C ASN A 341 15783 8867 16659 3783 924 -3975 C ATOM 2455 O ASN A 341 -10.521 -54.727 -16.405 1.00104.00 O ANISOU 2455 O ASN A 341 15282 7899 16336 3720 971 -3703 O ATOM 2456 CB ASN A 341 -8.446 -56.173 -17.452 1.00123.08 C ANISOU 2456 CB ASN A 341 17820 10299 18647 4374 1146 -3876 C ATOM 2457 CG ASN A 341 -7.791 -57.273 -18.194 1.00129.43 C ANISOU 2457 CG ASN A 341 18757 10913 19508 4607 1258 -4075 C ATOM 2458 OD1 ASN A 341 -8.343 -57.792 -19.156 1.00137.36 O ANISOU 2458 OD1 ASN A 341 19908 11776 20508 4479 1232 -4419 O ATOM 2459 ND2 ASN A 341 -6.591 -57.647 -17.763 1.00129.51 N ANISOU 2459 ND2 ASN A 341 18695 10924 19587 4957 1361 -3876 N ATOM 2460 N LYS A 342 -10.624 -53.256 -18.110 1.00108.58 N ANISOU 2460 N LYS A 342 15587 9274 16393 3600 817 -4113 N ATOM 2461 CA LYS A 342 -11.481 -52.290 -17.418 1.00103.86 C ANISOU 2461 CA LYS A 342 14854 8814 15794 3274 756 -3906 C ATOM 2462 C LYS A 342 -10.869 -51.881 -16.075 1.00 96.45 C ANISOU 2462 C LYS A 342 13852 7984 14809 3365 830 -3392 C ATOM 2463 O LYS A 342 -11.549 -51.819 -15.047 1.00 89.72 O ANISOU 2463 O LYS A 342 13047 6940 14104 3152 864 -3108 O ATOM 2464 CB LYS A 342 -12.896 -52.848 -17.222 1.00103.95 C ANISOU 2464 CB LYS A 342 14968 8349 16181 2909 723 -4020 C ATOM 2465 CG LYS A 342 -13.709 -53.092 -18.480 1.00106.22 C ANISOU 2465 CG LYS A 342 15283 8629 16447 2712 576 -4460 C ATOM 2466 CD LYS A 342 -15.119 -53.510 -18.073 1.00109.18 C ANISOU 2466 CD LYS A 342 15672 8586 17227 2301 542 -4471 C ATOM 2467 CE LYS A 342 -15.986 -53.953 -19.236 1.00116.65 C ANISOU 2467 CE LYS A 342 16640 9473 18210 2096 349 -4890 C ATOM 2468 NZ LYS A 342 -17.411 -54.064 -18.797 1.00116.63 N ANISOU 2468 NZ LYS A 342 16533 9174 18608 1664 302 -4871 N ATOM 2469 N ALA A 343 -9.558 -51.627 -16.087 1.00 87.72 N ANISOU 2469 N ALA A 343 12641 7184 13506 3707 855 -3285 N ATOM 2470 CA ALA A 343 -8.825 -51.395 -14.848 1.00 92.76 C ANISOU 2470 CA ALA A 343 13229 7897 14117 3872 868 -2856 C ATOM 2471 C ALA A 343 -9.281 -50.102 -14.171 1.00 88.04 C ANISOU 2471 C ALA A 343 12472 7646 13332 3600 803 -2591 C ATOM 2472 O ALA A 343 -9.568 -49.109 -14.841 1.00 79.68 O ANISOU 2472 O ALA A 343 11236 6968 12073 3415 754 -2715 O ATOM 2473 CB ALA A 343 -7.323 -51.326 -15.107 1.00 94.44 C ANISOU 2473 CB ALA A 343 13286 8393 14205 4283 881 -2849 C ATOM 2474 N PRO A 344 -9.349 -50.097 -12.842 1.00 82.02 N ANISOU 2474 N PRO A 344 11798 6753 12615 3601 805 -2221 N ATOM 2475 CA PRO A 344 -9.845 -48.929 -12.124 1.00 78.35 C ANISOU 2475 CA PRO A 344 11223 6570 11976 3358 750 -1983 C ATOM 2476 C PRO A 344 -8.929 -47.746 -12.353 1.00 76.69 C ANISOU 2476 C PRO A 344 10716 6919 11501 3452 646 -1959 C ATOM 2477 O PRO A 344 -7.697 -47.889 -12.337 1.00 78.76 O ANISOU 2477 O PRO A 344 10876 7308 11740 3781 612 -1928 O ATOM 2478 CB PRO A 344 -9.822 -49.374 -10.654 1.00 79.75 C ANISOU 2478 CB PRO A 344 11617 6466 12218 3478 785 -1599 C ATOM 2479 CG PRO A 344 -9.685 -50.880 -10.711 1.00 87.11 C ANISOU 2479 CG PRO A 344 12801 6864 13432 3683 894 -1655 C ATOM 2480 CD PRO A 344 -8.891 -51.153 -11.927 1.00 86.53 C ANISOU 2480 CD PRO A 344 12597 6917 13361 3880 859 -1996 C ATOM 2481 N PRO A 345 -9.490 -46.572 -12.599 1.00 80.44 N ANISOU 2481 N PRO A 345 11030 7722 11813 3171 603 -1978 N ATOM 2482 CA PRO A 345 -8.652 -45.392 -12.788 1.00 82.83 C ANISOU 2482 CA PRO A 345 11042 8518 11911 3228 529 -1936 C ATOM 2483 C PRO A 345 -8.055 -44.924 -11.472 1.00 84.74 C ANISOU 2483 C PRO A 345 11235 8869 12094 3347 416 -1622 C ATOM 2484 O PRO A 345 -8.637 -45.081 -10.392 1.00 80.75 O ANISOU 2484 O PRO A 345 10926 8159 11596 3282 399 -1406 O ATOM 2485 CB PRO A 345 -9.631 -44.357 -13.355 1.00 74.12 C ANISOU 2485 CB PRO A 345 9843 7644 10675 2879 521 -2030 C ATOM 2486 CG PRO A 345 -10.954 -44.780 -12.794 1.00 74.69 C ANISOU 2486 CG PRO A 345 10124 7374 10879 2633 549 -1976 C ATOM 2487 CD PRO A 345 -10.928 -46.261 -12.690 1.00 77.92 C ANISOU 2487 CD PRO A 345 10765 7314 11525 2790 625 -2032 C ATOM 2488 N THR A 346 -6.871 -44.336 -11.580 1.00 86.40 N ANISOU 2488 N THR A 346 11176 9406 12248 3534 340 -1606 N ATOM 2489 CA THR A 346 -6.187 -43.725 -10.452 1.00 85.05 C ANISOU 2489 CA THR A 346 10892 9405 12018 3654 166 -1374 C ATOM 2490 C THR A 346 -5.835 -42.292 -10.814 1.00 79.35 C ANISOU 2490 C THR A 346 9828 9117 11203 3502 111 -1403 C ATOM 2491 O THR A 346 -6.015 -41.859 -11.956 1.00 72.62 O ANISOU 2491 O THR A 346 8846 8430 10316 3357 235 -1571 O ATOM 2492 CB THR A 346 -4.911 -44.494 -10.083 1.00 81.00 C ANISOU 2492 CB THR A 346 10332 8820 11625 4078 85 -1324 C ATOM 2493 OG1 THR A 346 -3.869 -44.105 -10.985 1.00 81.38 O ANISOU 2493 OG1 THR A 346 10020 9161 11738 4199 118 -1477 O ATOM 2494 CG2 THR A 346 -5.140 -45.991 -10.190 1.00 79.24 C ANISOU 2494 CG2 THR A 346 10417 8152 11540 4248 205 -1366 C ATOM 2495 N TYR A 347 -5.303 -41.563 -9.831 1.00 80.43 N ANISOU 2495 N TYR A 347 9834 9426 11299 3558 -84 -1241 N ATOM 2496 CA TYR A 347 -4.956 -40.163 -10.057 1.00 82.03 C ANISOU 2496 CA TYR A 347 9706 9995 11468 3398 -145 -1258 C ATOM 2497 C TYR A 347 -3.977 -40.027 -11.217 1.00 86.49 C ANISOU 2497 C TYR A 347 9942 10762 12158 3504 -17 -1407 C ATOM 2498 O TYR A 347 -4.170 -39.204 -12.121 1.00 88.63 O ANISOU 2498 O TYR A 347 10057 11237 12382 3305 117 -1484 O ATOM 2499 CB TYR A 347 -4.371 -39.554 -8.772 1.00 79.70 C ANISOU 2499 CB TYR A 347 9316 9813 11153 3499 -423 -1107 C ATOM 2500 CG TYR A 347 -3.966 -38.101 -8.885 1.00 68.31 C ANISOU 2500 CG TYR A 347 7520 8697 9737 3327 -511 -1132 C ATOM 2501 CD1 TYR A 347 -4.829 -37.077 -8.486 1.00 78.33 C ANISOU 2501 CD1 TYR A 347 8859 10044 10860 3043 -560 -1075 C ATOM 2502 CD2 TYR A 347 -2.717 -37.747 -9.377 1.00 78.13 C ANISOU 2502 CD2 TYR A 347 8347 10148 11191 3449 -527 -1208 C ATOM 2503 CE1 TYR A 347 -4.454 -35.730 -8.583 1.00 73.61 C ANISOU 2503 CE1 TYR A 347 7945 9703 10321 2881 -637 -1100 C ATOM 2504 CE2 TYR A 347 -2.337 -36.420 -9.482 1.00 80.19 C ANISOU 2504 CE2 TYR A 347 8268 10661 11540 3271 -582 -1222 C ATOM 2505 CZ TYR A 347 -3.197 -35.420 -9.087 1.00 78.70 C ANISOU 2505 CZ TYR A 347 8176 10524 11202 2988 -646 -1171 C ATOM 2506 OH TYR A 347 -2.796 -34.110 -9.206 1.00 80.34 O ANISOU 2506 OH TYR A 347 8051 10941 11534 2813 -694 -1189 O ATOM 2507 N ASP A 348 -2.928 -40.849 -11.222 1.00 80.42 N ANISOU 2507 N ASP A 348 9078 9931 11546 3842 -30 -1436 N ATOM 2508 CA ASP A 348 -1.870 -40.671 -12.209 1.00 83.13 C ANISOU 2508 CA ASP A 348 9065 10484 12037 3978 118 -1552 C ATOM 2509 C ASP A 348 -2.309 -41.123 -13.603 1.00 79.62 C ANISOU 2509 C ASP A 348 8746 9996 11510 3942 410 -1734 C ATOM 2510 O ASP A 348 -1.929 -40.504 -14.605 1.00 72.03 O ANISOU 2510 O ASP A 348 7554 9271 10543 3903 602 -1809 O ATOM 2511 CB ASP A 348 -0.612 -41.414 -11.751 1.00 94.86 C ANISOU 2511 CB ASP A 348 10385 11919 13738 4378 5 -1533 C ATOM 2512 CG ASP A 348 -0.015 -40.816 -10.493 1.00103.53 C ANISOU 2512 CG ASP A 348 11295 13129 14915 4445 -330 -1398 C ATOM 2513 OD1 ASP A 348 0.274 -39.609 -10.483 1.00105.88 O ANISOU 2513 OD1 ASP A 348 11273 13682 15274 4262 -392 -1389 O ATOM 2514 OD2 ASP A 348 0.136 -41.555 -9.506 1.00110.95 O ANISOU 2514 OD2 ASP A 348 12428 13883 15846 4688 -541 -1304 O ATOM 2515 N THR A 349 -3.100 -42.200 -13.697 1.00 81.00 N ANISOU 2515 N THR A 349 9294 9859 11624 3966 451 -1813 N ATOM 2516 CA THR A 349 -3.583 -42.627 -15.009 1.00 81.95 C ANISOU 2516 CA THR A 349 9558 9929 11649 3935 668 -2037 C ATOM 2517 C THR A 349 -4.608 -41.651 -15.589 1.00 79.25 C ANISOU 2517 C THR A 349 9253 9752 11105 3588 714 -2076 C ATOM 2518 O THR A 349 -4.695 -41.506 -16.816 1.00 75.13 O ANISOU 2518 O THR A 349 8729 9360 10457 3585 889 -2242 O ATOM 2519 CB THR A 349 -4.181 -44.030 -14.929 1.00 85.19 C ANISOU 2519 CB THR A 349 10337 9922 12109 4029 670 -2141 C ATOM 2520 OG1 THR A 349 -5.192 -44.079 -13.912 1.00 84.40 O ANISOU 2520 OG1 THR A 349 10466 9608 11995 3817 532 -1994 O ATOM 2521 CG2 THR A 349 -3.097 -45.042 -14.637 1.00 79.17 C ANISOU 2521 CG2 THR A 349 9547 8998 11536 4429 669 -2133 C ATOM 2522 N VAL A 350 -5.402 -40.990 -14.741 1.00 68.19 N ANISOU 2522 N VAL A 350 7910 8349 9651 3324 564 -1927 N ATOM 2523 CA VAL A 350 -6.307 -39.963 -15.248 1.00 62.73 C ANISOU 2523 CA VAL A 350 7213 7832 8788 3019 593 -1946 C ATOM 2524 C VAL A 350 -5.508 -38.900 -15.988 1.00 69.54 C ANISOU 2524 C VAL A 350 7765 9045 9611 3031 721 -1927 C ATOM 2525 O VAL A 350 -5.779 -38.583 -17.152 1.00 71.00 O ANISOU 2525 O VAL A 350 7972 9368 9638 2987 879 -2042 O ATOM 2526 CB VAL A 350 -7.137 -39.343 -14.114 1.00 60.62 C ANISOU 2526 CB VAL A 350 7018 7522 8495 2772 428 -1772 C ATOM 2527 CG1 VAL A 350 -7.854 -38.119 -14.648 1.00 57.41 C ANISOU 2527 CG1 VAL A 350 6537 7338 7937 2498 458 -1774 C ATOM 2528 CG2 VAL A 350 -8.165 -40.320 -13.589 1.00 60.26 C ANISOU 2528 CG2 VAL A 350 7292 7119 8485 2707 389 -1784 C ATOM 2529 N LEU A 351 -4.484 -38.364 -15.328 1.00 71.89 N ANISOU 2529 N LEU A 351 7770 9479 10065 3109 655 -1782 N ATOM 2530 CA LEU A 351 -3.662 -37.313 -15.907 1.00 80.85 C ANISOU 2530 CA LEU A 351 8558 10908 11253 3095 798 -1733 C ATOM 2531 C LEU A 351 -2.769 -37.828 -17.023 1.00 87.47 C ANISOU 2531 C LEU A 351 9280 11824 12129 3361 1068 -1848 C ATOM 2532 O LEU A 351 -2.072 -37.030 -17.653 1.00 98.49 O ANISOU 2532 O LEU A 351 10393 13450 13580 3368 1271 -1797 O ATOM 2533 CB LEU A 351 -2.818 -36.648 -14.815 1.00 82.93 C ANISOU 2533 CB LEU A 351 8510 11260 11740 3096 608 -1583 C ATOM 2534 CG LEU A 351 -3.596 -35.894 -13.717 1.00 80.79 C ANISOU 2534 CG LEU A 351 8332 10962 11402 2847 359 -1468 C ATOM 2535 CD1 LEU A 351 -2.649 -35.252 -12.715 1.00 88.51 C ANISOU 2535 CD1 LEU A 351 8998 12035 12596 2889 137 -1377 C ATOM 2536 CD2 LEU A 351 -4.502 -34.833 -14.299 1.00 74.00 C ANISOU 2536 CD2 LEU A 351 7519 10222 10375 2553 459 -1448 C ATOM 2537 N GLN A 352 -2.778 -39.133 -17.279 1.00 72.02 N ANISOU 2537 N GLN A 352 7542 9663 10158 3584 1103 -1998 N ATOM 2538 CA GLN A 352 -2.051 -39.676 -18.401 1.00 78.52 C ANISOU 2538 CA GLN A 352 8317 10546 10971 3859 1380 -2141 C ATOM 2539 C GLN A 352 -2.844 -39.579 -19.701 1.00 79.46 C ANISOU 2539 C GLN A 352 8685 10734 10771 3797 1562 -2300 C ATOM 2540 O GLN A 352 -2.242 -39.604 -20.778 1.00 88.62 O ANISOU 2540 O GLN A 352 9785 12042 11843 3998 1850 -2382 O ATOM 2541 CB GLN A 352 -1.667 -41.132 -18.077 1.00 79.35 C ANISOU 2541 CB GLN A 352 8559 10377 11215 4157 1321 -2248 C ATOM 2542 CG GLN A 352 -0.787 -41.792 -19.022 1.00 92.72 C ANISOU 2542 CG GLN A 352 10184 12101 12944 4494 1586 -2395 C ATOM 2543 CD GLN A 352 -0.526 -43.229 -18.614 1.00100.25 C ANISOU 2543 CD GLN A 352 11310 12735 14047 4778 1500 -2496 C ATOM 2544 OE1 GLN A 352 -0.305 -43.514 -17.431 1.00103.73 O ANISOU 2544 OE1 GLN A 352 11707 13031 14677 4821 1265 -2359 O ATOM 2545 NE2 GLN A 352 -0.594 -44.137 -19.567 1.00 97.48 N ANISOU 2545 NE2 GLN A 352 11197 12247 13593 4945 1672 -2714 N ATOM 2546 N MET A 353 -4.168 -39.443 -19.630 1.00 74.53 N ANISOU 2546 N MET A 353 8332 10019 9969 3544 1404 -2346 N ATOM 2547 CA MET A 353 -5.040 -39.557 -20.799 1.00 80.98 C ANISOU 2547 CA MET A 353 9428 10858 10484 3518 1483 -2552 C ATOM 2548 C MET A 353 -5.189 -38.209 -21.500 1.00 87.11 C ANISOU 2548 C MET A 353 10104 11943 11049 3382 1622 -2443 C ATOM 2549 O MET A 353 -5.912 -37.329 -21.018 1.00 86.96 O ANISOU 2549 O MET A 353 10061 11972 11007 3100 1478 -2311 O ATOM 2550 CB MET A 353 -6.400 -40.100 -20.377 1.00 84.09 C ANISOU 2550 CB MET A 353 10114 10982 10854 3315 1233 -2667 C ATOM 2551 CG MET A 353 -6.273 -41.353 -19.554 1.00 90.38 C ANISOU 2551 CG MET A 353 11018 11434 11890 3428 1120 -2709 C ATOM 2552 SD MET A 353 -7.839 -42.187 -19.297 1.00 92.80 S ANISOU 2552 SD MET A 353 11666 11363 12230 3212 919 -2879 S ATOM 2553 CE MET A 353 -7.300 -43.503 -18.203 1.00 99.30 C ANISOU 2553 CE MET A 353 12568 11798 13365 3403 871 -2810 C ATOM 2554 N GLU A 354 -4.545 -38.065 -22.667 1.00 76.82 N ANISOU 2554 N GLU A 354 8774 10836 9578 3603 1926 -2493 N ATOM 2555 CA GLU A 354 -4.558 -36.787 -23.378 1.00 83.36 C ANISOU 2555 CA GLU A 354 9518 11944 10209 3517 2122 -2342 C ATOM 2556 C GLU A 354 -5.894 -36.521 -24.058 1.00 77.65 C ANISOU 2556 C GLU A 354 9124 11253 9125 3394 2000 -2467 C ATOM 2557 O GLU A 354 -6.441 -35.417 -23.944 1.00 69.51 O ANISOU 2557 O GLU A 354 8047 10339 8025 3166 1945 -2303 O ATOM 2558 CB GLU A 354 -3.441 -36.736 -24.412 1.00 85.55 C ANISOU 2558 CB GLU A 354 9682 12413 10409 3820 2542 -2324 C ATOM 2559 CG GLU A 354 -2.065 -36.688 -23.820 1.00102.40 C ANISOU 2559 CG GLU A 354 11385 14573 12948 3918 2690 -2164 C ATOM 2560 CD GLU A 354 -0.997 -36.703 -24.887 1.00115.80 C ANISOU 2560 CD GLU A 354 12994 16367 14638 4090 3099 -2106 C ATOM 2561 OE1 GLU A 354 -1.181 -36.023 -25.922 1.00118.76 O ANISOU 2561 OE1 GLU A 354 13505 16894 14725 4056 3329 -2035 O ATOM 2562 OE2 GLU A 354 0.017 -37.407 -24.698 1.00122.58 O ANISOU 2562 OE2 GLU A 354 13661 17137 15779 4256 3181 -2130 O ATOM 2563 N TYR A 355 -6.403 -37.514 -24.796 1.00 82.65 N ANISOU 2563 N TYR A 355 10081 11779 9541 3562 1944 -2775 N ATOM 2564 CA TYR A 355 -7.632 -37.347 -25.563 1.00 79.42 C ANISOU 2564 CA TYR A 355 9977 11411 8789 3495 1791 -2952 C ATOM 2565 C TYR A 355 -8.826 -37.147 -24.642 1.00 82.04 C ANISOU 2565 C TYR A 355 10317 11585 9269 3145 1444 -2930 C ATOM 2566 O TYR A 355 -9.758 -36.401 -24.974 1.00 76.96 O ANISOU 2566 O TYR A 355 9764 11050 8426 2999 1327 -2920 O ATOM 2567 CB TYR A 355 -7.852 -38.564 -26.462 1.00 75.21 C ANISOU 2567 CB TYR A 355 9768 10751 8058 3742 1754 -3328 C ATOM 2568 CG TYR A 355 -8.845 -38.349 -27.570 1.00 79.44 C ANISOU 2568 CG TYR A 355 10608 11376 8199 3720 1619 -3490 C ATOM 2569 CD1 TYR A 355 -8.535 -37.543 -28.662 1.00 86.54 C ANISOU 2569 CD1 TYR A 355 11587 12546 8748 3832 1848 -3339 C ATOM 2570 CD2 TYR A 355 -10.081 -38.978 -27.550 1.00 76.39 C ANISOU 2570 CD2 TYR A 355 10423 10784 7816 3595 1257 -3789 C ATOM 2571 CE1 TYR A 355 -9.436 -37.362 -29.701 1.00 91.20 C ANISOU 2571 CE1 TYR A 355 12475 13224 8953 3856 1687 -3482 C ATOM 2572 CE2 TYR A 355 -10.989 -38.804 -28.581 1.00 85.02 C ANISOU 2572 CE2 TYR A 355 11765 11965 8572 3591 1078 -3952 C ATOM 2573 CZ TYR A 355 -10.661 -37.999 -29.653 1.00 89.50 C ANISOU 2573 CZ TYR A 355 12433 12825 8748 3741 1278 -3799 C ATOM 2574 OH TYR A 355 -11.562 -37.826 -30.673 1.00 88.84 O ANISOU 2574 OH TYR A 355 12608 12834 8314 3775 1066 -3952 O ATOM 2575 N LEU A 356 -8.824 -37.824 -23.489 1.00 79.10 N ANISOU 2575 N LEU A 356 9865 10951 9237 3035 1291 -2914 N ATOM 2576 CA LEU A 356 -9.811 -37.524 -22.466 1.00 72.25 C ANISOU 2576 CA LEU A 356 8968 9948 8536 2712 1040 -2820 C ATOM 2577 C LEU A 356 -9.755 -36.047 -22.107 1.00 68.43 C ANISOU 2577 C LEU A 356 8276 9688 8035 2530 1083 -2523 C ATOM 2578 O LEU A 356 -10.785 -35.361 -22.072 1.00 65.68 O ANISOU 2578 O LEU A 356 7975 9381 7598 2323 943 -2494 O ATOM 2579 CB LEU A 356 -9.574 -38.391 -21.228 1.00 72.05 C ANISOU 2579 CB LEU A 356 8893 9632 8852 2680 945 -2773 C ATOM 2580 CG LEU A 356 -10.414 -37.967 -20.019 1.00 68.02 C ANISOU 2580 CG LEU A 356 8335 9004 8504 2377 757 -2606 C ATOM 2581 CD1 LEU A 356 -11.900 -38.100 -20.315 1.00 59.11 C ANISOU 2581 CD1 LEU A 356 7382 7760 7317 2184 585 -2787 C ATOM 2582 CD2 LEU A 356 -10.046 -38.780 -18.786 1.00 63.94 C ANISOU 2582 CD2 LEU A 356 7805 8222 8267 2405 699 -2510 C ATOM 2583 N ASP A 357 -8.542 -35.530 -21.885 1.00 70.40 N ANISOU 2583 N ASP A 357 8276 10077 8396 2613 1279 -2314 N ATOM 2584 CA ASP A 357 -8.396 -34.115 -21.566 1.00 68.47 C ANISOU 2584 CA ASP A 357 7819 10012 8185 2438 1329 -2048 C ATOM 2585 C ASP A 357 -8.902 -33.236 -22.703 1.00 62.20 C ANISOU 2585 C ASP A 357 7139 9427 7066 2436 1441 -2030 C ATOM 2586 O ASP A 357 -9.560 -32.216 -22.467 1.00 64.18 O ANISOU 2586 O ASP A 357 7361 9741 7284 2228 1354 -1894 O ATOM 2587 CB ASP A 357 -6.940 -33.799 -21.255 1.00 68.50 C ANISOU 2587 CB ASP A 357 7500 10106 8419 2540 1522 -1872 C ATOM 2588 CG ASP A 357 -6.771 -32.416 -20.656 1.00 77.72 C ANISOU 2588 CG ASP A 357 8419 11381 9729 2321 1515 -1622 C ATOM 2589 OD1 ASP A 357 -7.460 -32.141 -19.664 1.00 72.97 O ANISOU 2589 OD1 ASP A 357 7837 10679 9211 2109 1269 -1576 O ATOM 2590 OD2 ASP A 357 -5.951 -31.618 -21.164 1.00 86.80 O ANISOU 2590 OD2 ASP A 357 9357 12697 10925 2363 1772 -1475 O ATOM 2591 N MET A 358 -8.626 -33.636 -23.941 1.00 70.29 N ANISOU 2591 N MET A 358 8326 10557 7825 2696 1629 -2170 N ATOM 2592 CA MET A 358 -9.032 -32.850 -25.099 1.00 71.73 C ANISOU 2592 CA MET A 358 8669 10951 7632 2767 1751 -2142 C ATOM 2593 C MET A 358 -10.544 -32.824 -25.244 1.00 62.44 C ANISOU 2593 C MET A 358 7724 9725 6273 2631 1432 -2305 C ATOM 2594 O MET A 358 -11.123 -31.778 -25.562 1.00 67.20 O ANISOU 2594 O MET A 358 8363 10466 6702 2545 1413 -2175 O ATOM 2595 CB MET A 358 -8.379 -33.424 -26.360 1.00 78.97 C ANISOU 2595 CB MET A 358 9757 11984 8264 3131 2025 -2282 C ATOM 2596 CG MET A 358 -6.866 -33.373 -26.332 1.00 81.45 C ANISOU 2596 CG MET A 358 9798 12368 8781 3284 2395 -2108 C ATOM 2597 SD MET A 358 -6.106 -34.496 -27.527 1.00 84.08 S ANISOU 2597 SD MET A 358 10340 12717 8890 3685 2660 -2323 S ATOM 2598 CE MET A 358 -7.022 -34.052 -29.008 1.00 90.86 C ANISOU 2598 CE MET A 358 11629 13719 9173 3754 2643 -2380 C ATOM 2599 N VAL A 359 -11.199 -33.968 -25.014 1.00 68.41 N ANISOU 2599 N VAL A 359 8622 10269 7104 2613 1182 -2588 N ATOM 2600 CA VAL A 359 -12.658 -34.033 -25.094 1.00 61.67 C ANISOU 2600 CA VAL A 359 7925 9337 6171 2463 863 -2773 C ATOM 2601 C VAL A 359 -13.294 -33.173 -24.008 1.00 62.21 C ANISOU 2601 C VAL A 359 7814 9360 6462 2143 727 -2554 C ATOM 2602 O VAL A 359 -14.276 -32.456 -24.263 1.00 64.88 O ANISOU 2602 O VAL A 359 8204 9781 6667 2039 582 -2547 O ATOM 2603 CB VAL A 359 -13.134 -35.494 -25.007 1.00 63.40 C ANISOU 2603 CB VAL A 359 8286 9280 6523 2486 660 -3118 C ATOM 2604 CG1 VAL A 359 -14.587 -35.564 -24.642 1.00 64.92 C ANISOU 2604 CG1 VAL A 359 8509 9320 6838 2237 338 -3255 C ATOM 2605 CG2 VAL A 359 -12.836 -36.284 -26.346 1.00 70.19 C ANISOU 2605 CG2 VAL A 359 9409 10197 7063 2828 723 -3432 C ATOM 2606 N VAL A 360 -12.759 -33.228 -22.783 1.00 56.54 N ANISOU 2606 N VAL A 360 6899 8515 6071 2012 760 -2384 N ATOM 2607 CA VAL A 360 -13.324 -32.413 -21.704 1.00 57.95 C ANISOU 2607 CA VAL A 360 6937 8650 6431 1739 643 -2190 C ATOM 2608 C VAL A 360 -13.175 -30.935 -22.037 1.00 61.40 C ANISOU 2608 C VAL A 360 7282 9317 6729 1700 762 -1956 C ATOM 2609 O VAL A 360 -14.124 -30.146 -21.913 1.00 61.01 O ANISOU 2609 O VAL A 360 7244 9300 6639 1545 637 -1898 O ATOM 2610 CB VAL A 360 -12.663 -32.765 -20.356 1.00 55.33 C ANISOU 2610 CB VAL A 360 6452 8156 6414 1668 646 -2061 C ATOM 2611 CG1 VAL A 360 -13.110 -31.791 -19.264 1.00 51.43 C ANISOU 2611 CG1 VAL A 360 5836 7652 6054 1429 553 -1856 C ATOM 2612 CG2 VAL A 360 -13.015 -34.183 -19.944 1.00 59.27 C ANISOU 2612 CG2 VAL A 360 7076 8378 7067 1685 530 -2254 C ATOM 2613 N ASN A 361 -11.979 -30.545 -22.493 1.00 61.12 N ANISOU 2613 N ASN A 361 7148 9428 6646 1849 1029 -1815 N ATOM 2614 CA ASN A 361 -11.698 -29.137 -22.751 1.00 61.56 C ANISOU 2614 CA ASN A 361 7096 9654 6642 1800 1195 -1558 C ATOM 2615 C ASN A 361 -12.461 -28.618 -23.958 1.00 63.26 C ANISOU 2615 C ASN A 361 7533 10024 6479 1901 1206 -1585 C ATOM 2616 O ASN A 361 -12.882 -27.456 -23.975 1.00 67.22 O ANISOU 2616 O ASN A 361 8010 10598 6934 1794 1209 -1403 O ATOM 2617 CB ASN A 361 -10.202 -28.917 -22.970 1.00 64.60 C ANISOU 2617 CB ASN A 361 7284 10128 7132 1930 1517 -1399 C ATOM 2618 CG ASN A 361 -9.403 -29.060 -21.706 1.00 70.24 C ANISOU 2618 CG ASN A 361 7725 10725 8240 1823 1468 -1325 C ATOM 2619 OD1 ASN A 361 -9.899 -28.790 -20.621 1.00 73.80 O ANISOU 2619 OD1 ASN A 361 8119 11066 8855 1619 1247 -1288 O ATOM 2620 ND2 ASN A 361 -8.147 -29.511 -21.841 1.00 70.24 N ANISOU 2620 ND2 ASN A 361 7559 10749 8380 1991 1671 -1311 N ATOM 2621 N GLU A 362 -12.606 -29.434 -24.998 1.00 65.77 N ANISOU 2621 N GLU A 362 8084 10395 6511 2135 1209 -1813 N ATOM 2622 CA GLU A 362 -13.382 -28.967 -26.138 1.00 67.17 C ANISOU 2622 CA GLU A 362 8507 10732 6283 2271 1160 -1863 C ATOM 2623 C GLU A 362 -14.840 -28.821 -25.762 1.00 69.59 C ANISOU 2623 C GLU A 362 8855 10960 6625 2082 793 -1981 C ATOM 2624 O GLU A 362 -15.523 -27.928 -26.273 1.00 71.98 O ANISOU 2624 O GLU A 362 9251 11387 6712 2102 728 -1897 O ATOM 2625 CB GLU A 362 -13.229 -29.905 -27.327 1.00 62.74 C ANISOU 2625 CB GLU A 362 8215 10247 5375 2593 1205 -2128 C ATOM 2626 CG GLU A 362 -14.195 -29.650 -28.486 1.00 77.07 C ANISOU 2626 CG GLU A 362 10338 12216 6728 2773 1039 -2271 C ATOM 2627 CD GLU A 362 -13.811 -28.454 -29.354 1.00 80.22 C ANISOU 2627 CD GLU A 362 10844 12849 6787 2952 1340 -1966 C ATOM 2628 OE1 GLU A 362 -14.230 -28.416 -30.526 1.00 87.83 O ANISOU 2628 OE1 GLU A 362 12128 13977 7268 3233 1294 -2079 O ATOM 2629 OE2 GLU A 362 -13.091 -27.552 -28.874 1.00 80.23 O ANISOU 2629 OE2 GLU A 362 10622 12858 7004 2824 1620 -1615 O ATOM 2630 N THR A 363 -15.332 -29.661 -24.850 1.00 65.53 N ANISOU 2630 N THR A 363 8263 10231 6403 1906 570 -2152 N ATOM 2631 CA THR A 363 -16.711 -29.492 -24.413 1.00 58.73 C ANISOU 2631 CA THR A 363 7387 9282 5646 1709 269 -2241 C ATOM 2632 C THR A 363 -16.854 -28.246 -23.565 1.00 60.09 C ANISOU 2632 C THR A 363 7384 9468 5980 1502 310 -1942 C ATOM 2633 O THR A 363 -17.857 -27.527 -23.674 1.00 62.04 O ANISOU 2633 O THR A 363 7645 9762 6163 1433 156 -1920 O ATOM 2634 CB THR A 363 -17.202 -30.717 -23.648 1.00 57.77 C ANISOU 2634 CB THR A 363 7230 8896 5825 1571 85 -2469 C ATOM 2635 OG1 THR A 363 -17.026 -31.882 -24.446 1.00 57.66 O ANISOU 2635 OG1 THR A 363 7386 8835 5687 1767 44 -2769 O ATOM 2636 CG2 THR A 363 -18.679 -30.584 -23.351 1.00 62.09 C ANISOU 2636 CG2 THR A 363 7741 9356 6497 1384 -193 -2580 C ATOM 2637 N LEU A 364 -15.846 -27.949 -22.732 1.00 60.19 N ANISOU 2637 N LEU A 364 7223 9439 6207 1420 499 -1728 N ATOM 2638 CA LEU A 364 -15.915 -26.707 -21.964 1.00 57.63 C ANISOU 2638 CA LEU A 364 6748 9120 6030 1239 529 -1473 C ATOM 2639 C LEU A 364 -15.716 -25.480 -22.847 1.00 58.83 C ANISOU 2639 C LEU A 364 6942 9452 5958 1335 695 -1269 C ATOM 2640 O LEU A 364 -16.121 -24.387 -22.455 1.00 55.29 O ANISOU 2640 O LEU A 364 6426 9001 5581 1205 671 -1099 O ATOM 2641 CB LEU A 364 -14.907 -26.715 -20.802 1.00 49.45 C ANISOU 2641 CB LEU A 364 5514 7983 5293 1134 626 -1339 C ATOM 2642 CG LEU A 364 -15.381 -27.581 -19.635 1.00 52.04 C ANISOU 2642 CG LEU A 364 5823 8107 5843 1004 447 -1453 C ATOM 2643 CD1 LEU A 364 -14.242 -28.071 -18.771 1.00 53.13 C ANISOU 2643 CD1 LEU A 364 5840 8159 6190 1022 515 -1398 C ATOM 2644 CD2 LEU A 364 -16.428 -26.815 -18.764 1.00 58.68 C ANISOU 2644 CD2 LEU A 364 6625 8881 6789 800 309 -1376 C ATOM 2645 N ARG A 365 -15.127 -25.620 -24.035 1.00 59.66 N ANISOU 2645 N ARG A 365 7180 9702 5786 1576 883 -1271 N ATOM 2646 CA ARG A 365 -15.082 -24.460 -24.917 1.00 69.03 C ANISOU 2646 CA ARG A 365 8459 11043 6727 1689 1059 -1049 C ATOM 2647 C ARG A 365 -16.468 -24.141 -25.464 1.00 67.89 C ANISOU 2647 C ARG A 365 8501 10963 6330 1740 797 -1144 C ATOM 2648 O ARG A 365 -16.916 -22.993 -25.412 1.00 70.28 O ANISOU 2648 O ARG A 365 8792 11288 6624 1679 793 -946 O ATOM 2649 CB ARG A 365 -14.093 -24.679 -26.060 1.00 70.05 C ANISOU 2649 CB ARG A 365 8710 11316 6589 1969 1379 -999 C ATOM 2650 CG ARG A 365 -13.922 -23.441 -26.924 1.00 71.55 C ANISOU 2650 CG ARG A 365 9005 11639 6540 2095 1642 -701 C ATOM 2651 CD ARG A 365 -13.073 -23.720 -28.169 1.00 76.87 C ANISOU 2651 CD ARG A 365 9862 12470 6875 2422 1994 -653 C ATOM 2652 NE ARG A 365 -13.685 -24.737 -29.012 1.00 75.05 N ANISOU 2652 NE ARG A 365 9936 12334 6244 2673 1784 -983 N ATOM 2653 CZ ARG A 365 -14.653 -24.493 -29.886 1.00 76.66 C ANISOU 2653 CZ ARG A 365 10440 12663 6023 2861 1593 -1059 C ATOM 2654 NH1 ARG A 365 -15.120 -23.264 -30.038 1.00 80.56 N ANISOU 2654 NH1 ARG A 365 10980 13201 6427 2839 1613 -797 N ATOM 2655 NH2 ARG A 365 -15.164 -25.483 -30.599 1.00 80.66 N ANISOU 2655 NH2 ARG A 365 11201 13239 6208 3082 1356 -1415 N ATOM 2656 N LEU A 366 -17.175 -25.149 -25.973 1.00 65.72 N ANISOU 2656 N LEU A 366 8385 10703 5880 1855 554 -1463 N ATOM 2657 CA LEU A 366 -18.493 -24.881 -26.530 1.00 66.05 C ANISOU 2657 CA LEU A 366 8569 10816 5709 1921 257 -1590 C ATOM 2658 C LEU A 366 -19.510 -24.540 -25.454 1.00 64.25 C ANISOU 2658 C LEU A 366 8152 10450 5812 1646 24 -1595 C ATOM 2659 O LEU A 366 -20.465 -23.799 -25.727 1.00 67.69 O ANISOU 2659 O LEU A 366 8625 10948 6145 1670 -146 -1563 O ATOM 2660 CB LEU A 366 -18.977 -26.073 -27.359 1.00 76.23 C ANISOU 2660 CB LEU A 366 10054 12140 6770 2110 18 -1980 C ATOM 2661 CG LEU A 366 -18.216 -26.263 -28.677 1.00 78.92 C ANISOU 2661 CG LEU A 366 10672 12668 6646 2470 221 -1997 C ATOM 2662 CD1 LEU A 366 -18.378 -27.670 -29.239 1.00 72.76 C ANISOU 2662 CD1 LEU A 366 10054 11858 5733 2628 23 -2425 C ATOM 2663 CD2 LEU A 366 -18.682 -25.227 -29.687 1.00 80.98 C ANISOU 2663 CD2 LEU A 366 11159 13135 6475 2703 204 -1847 C ATOM 2664 N PHE A 367 -19.346 -25.058 -24.240 1.00 61.08 N ANISOU 2664 N PHE A 367 7558 9862 5787 1412 21 -1627 N ATOM 2665 CA PHE A 367 -20.316 -24.837 -23.167 1.00 56.93 C ANISOU 2665 CA PHE A 367 6871 9195 5563 1170 -155 -1636 C ATOM 2666 C PHE A 367 -19.621 -24.335 -21.894 1.00 60.08 C ANISOU 2666 C PHE A 367 7099 9483 6246 977 20 -1406 C ATOM 2667 O PHE A 367 -19.523 -25.054 -20.892 1.00 57.76 O ANISOU 2667 O PHE A 367 6713 9031 6204 840 -1 -1472 O ATOM 2668 CB PHE A 367 -21.125 -26.110 -22.891 1.00 58.46 C ANISOU 2668 CB PHE A 367 7038 9240 5934 1088 -388 -1954 C ATOM 2669 CG PHE A 367 -21.804 -26.675 -24.103 1.00 65.44 C ANISOU 2669 CG PHE A 367 8073 10212 6578 1271 -623 -2247 C ATOM 2670 CD1 PHE A 367 -21.320 -27.823 -24.711 1.00 55.74 C ANISOU 2670 CD1 PHE A 367 6978 8964 5238 1412 -630 -2484 C ATOM 2671 CD2 PHE A 367 -22.911 -26.043 -24.647 1.00 60.83 C ANISOU 2671 CD2 PHE A 367 7507 9732 5874 1329 -857 -2304 C ATOM 2672 CE1 PHE A 367 -21.936 -28.344 -25.839 1.00 71.31 C ANISOU 2672 CE1 PHE A 367 9112 11014 6969 1601 -885 -2800 C ATOM 2673 CE2 PHE A 367 -23.532 -26.543 -25.766 1.00 73.51 C ANISOU 2673 CE2 PHE A 367 9256 11431 7243 1524 -1131 -2606 C ATOM 2674 CZ PHE A 367 -23.051 -27.706 -26.373 1.00 80.07 C ANISOU 2674 CZ PHE A 367 10236 12238 7948 1659 -1156 -2871 C ATOM 2675 N PRO A 368 -19.128 -23.105 -21.894 1.00 50.88 N ANISOU 2675 N PRO A 368 5899 8382 5051 974 186 -1140 N ATOM 2676 CA PRO A 368 -18.545 -22.592 -20.655 1.00 42.14 C ANISOU 2676 CA PRO A 368 4625 7158 4228 791 287 -976 C ATOM 2677 C PRO A 368 -19.672 -22.098 -19.762 1.00 54.62 C ANISOU 2677 C PRO A 368 6143 8642 5970 630 125 -976 C ATOM 2678 O PRO A 368 -20.213 -21.002 -19.952 1.00 58.00 O ANISOU 2678 O PRO A 368 6580 9108 6351 630 109 -854 O ATOM 2679 CB PRO A 368 -17.611 -21.480 -21.142 1.00 49.34 C ANISOU 2679 CB PRO A 368 5517 8151 5078 850 530 -718 C ATOM 2680 CG PRO A 368 -18.286 -20.953 -22.363 1.00 55.15 C ANISOU 2680 CG PRO A 368 6429 9024 5501 1022 510 -680 C ATOM 2681 CD PRO A 368 -19.009 -22.136 -22.995 1.00 51.16 C ANISOU 2681 CD PRO A 368 6058 8577 4805 1147 301 -972 C ATOM 2682 N ILE A 369 -20.051 -22.943 -18.797 1.00 50.47 N ANISOU 2682 N ILE A 369 5564 7977 5635 512 28 -1106 N ATOM 2683 CA ILE A 369 -21.353 -22.810 -18.164 1.00 48.64 C ANISOU 2683 CA ILE A 369 5289 7659 5534 397 -112 -1164 C ATOM 2684 C ILE A 369 -21.455 -21.616 -17.223 1.00 47.51 C ANISOU 2684 C ILE A 369 5077 7463 5511 290 -65 -987 C ATOM 2685 O ILE A 369 -22.577 -21.228 -16.884 1.00 48.50 O ANISOU 2685 O ILE A 369 5167 7549 5714 233 -150 -1005 O ATOM 2686 CB ILE A 369 -21.746 -24.092 -17.415 1.00 46.94 C ANISOU 2686 CB ILE A 369 5052 7282 5501 308 -170 -1325 C ATOM 2687 CG1 ILE A 369 -20.596 -24.621 -16.563 1.00 44.30 C ANISOU 2687 CG1 ILE A 369 4717 6859 5257 289 -56 -1263 C ATOM 2688 CG2 ILE A 369 -22.334 -25.154 -18.407 1.00 47.60 C ANISOU 2688 CG2 ILE A 369 5187 7375 5524 384 -308 -1577 C ATOM 2689 CD1 ILE A 369 -21.066 -25.592 -15.444 1.00 41.79 C ANISOU 2689 CD1 ILE A 369 4402 6338 5138 191 -69 -1327 C ATOM 2690 N ALA A 370 -20.338 -21.007 -16.800 1.00 48.68 N ANISOU 2690 N ALA A 370 5191 7601 5703 267 59 -836 N ATOM 2691 CA ALA A 370 -20.460 -19.703 -16.135 1.00 47.36 C ANISOU 2691 CA ALA A 370 4980 7384 5631 188 81 -694 C ATOM 2692 C ALA A 370 -20.751 -18.567 -17.105 1.00 49.21 C ANISOU 2692 C ALA A 370 5248 7702 5748 261 115 -568 C ATOM 2693 O ALA A 370 -21.211 -17.507 -16.660 1.00 54.96 O ANISOU 2693 O ALA A 370 5958 8368 6557 211 105 -478 O ATOM 2694 CB ALA A 370 -19.192 -19.347 -15.353 1.00 41.11 C ANISOU 2694 CB ALA A 370 4118 6531 4973 129 160 -606 C ATOM 2695 N MET A 371 -20.469 -18.786 -18.387 1.00 49.26 N ANISOU 2695 N MET A 371 5324 7836 5555 402 177 -542 N ATOM 2696 CA MET A 371 -20.713 -17.807 -19.449 1.00 51.55 C ANISOU 2696 CA MET A 371 5707 8220 5660 532 208 -413 C ATOM 2697 C MET A 371 -19.849 -16.542 -19.389 1.00 54.86 C ANISOU 2697 C MET A 371 6098 8579 6167 499 401 -161 C ATOM 2698 O MET A 371 -19.157 -16.215 -20.354 1.00 54.33 O ANISOU 2698 O MET A 371 6116 8588 5937 630 562 -2 O ATOM 2699 CB MET A 371 -22.207 -17.472 -19.518 1.00 51.30 C ANISOU 2699 CB MET A 371 5687 8187 5618 546 10 -487 C ATOM 2700 CG MET A 371 -23.109 -18.685 -19.676 1.00 61.00 C ANISOU 2700 CG MET A 371 6917 9461 6799 581 -188 -742 C ATOM 2701 SD MET A 371 -24.857 -18.249 -19.737 1.00 62.46 S ANISOU 2701 SD MET A 371 7046 9656 7031 612 -421 -825 S ATOM 2702 CE MET A 371 -25.269 -18.255 -17.995 1.00 50.48 C ANISOU 2702 CE MET A 371 5374 7944 5860 384 -373 -838 C ATOM 2703 N ARG A 372 -19.901 -15.829 -18.270 1.00 54.76 N ANISOU 2703 N ARG A 372 5976 8416 6412 335 398 -126 N ATOM 2704 CA ARG A 372 -19.165 -14.585 -18.116 1.00 55.29 C ANISOU 2704 CA ARG A 372 5995 8373 6638 272 546 74 C ATOM 2705 C ARG A 372 -18.286 -14.560 -16.872 1.00 49.29 C ANISOU 2705 C ARG A 372 5085 7483 6161 103 538 22 C ATOM 2706 O ARG A 372 -18.627 -15.145 -15.848 1.00 53.34 O ANISOU 2706 O ARG A 372 5581 7958 6729 40 387 -137 O ATOM 2707 CB ARG A 372 -20.206 -13.447 -17.967 1.00 59.02 C ANISOU 2707 CB ARG A 372 6524 8764 7138 277 478 153 C ATOM 2708 CG ARG A 372 -21.093 -13.162 -19.154 1.00 59.84 C ANISOU 2708 CG ARG A 372 6774 8981 6981 471 450 234 C ATOM 2709 CD ARG A 372 -22.188 -12.197 -18.705 1.00 64.16 C ANISOU 2709 CD ARG A 372 7334 9429 7617 469 341 264 C ATOM 2710 NE ARG A 372 -22.815 -11.443 -19.788 1.00 62.03 N ANISOU 2710 NE ARG A 372 7203 9214 7151 670 344 425 N ATOM 2711 CZ ARG A 372 -23.674 -10.458 -19.581 1.00 63.32 C ANISOU 2711 CZ ARG A 372 7388 9283 7388 713 278 495 C ATOM 2712 NH1 ARG A 372 -24.003 -10.121 -18.340 1.00 59.48 N ANISOU 2712 NH1 ARG A 372 6797 8646 7155 565 225 405 N ATOM 2713 NH2 ARG A 372 -24.205 -9.805 -20.602 1.00 69.58 N ANISOU 2713 NH2 ARG A 372 8324 10129 7982 932 267 657 N ATOM 2714 N LEU A 373 -17.208 -13.797 -16.934 1.00 47.12 N ANISOU 2714 N LEU A 373 4703 7122 6077 39 698 161 N ATOM 2715 CA LEU A 373 -16.479 -13.395 -15.741 1.00 47.79 C ANISOU 2715 CA LEU A 373 4637 7053 6468 -118 636 103 C ATOM 2716 C LEU A 373 -16.693 -11.909 -15.514 1.00 54.24 C ANISOU 2716 C LEU A 373 5453 7691 7464 -198 666 215 C ATOM 2717 O LEU A 373 -16.898 -11.158 -16.468 1.00 63.86 O ANISOU 2717 O LEU A 373 6742 8894 8629 -136 829 411 O ATOM 2718 CB LEU A 373 -14.974 -13.685 -15.887 1.00 47.98 C ANISOU 2718 CB LEU A 373 4469 7081 6681 -155 767 131 C ATOM 2719 CG LEU A 373 -14.559 -15.032 -16.494 1.00 58.97 C ANISOU 2719 CG LEU A 373 5864 8644 7900 -35 826 73 C ATOM 2720 CD1 LEU A 373 -13.045 -15.098 -16.749 1.00 58.10 C ANISOU 2720 CD1 LEU A 373 5524 8528 8023 -56 1010 138 C ATOM 2721 CD2 LEU A 373 -15.014 -16.209 -15.624 1.00 56.62 C ANISOU 2721 CD2 LEU A 373 5625 8381 7506 -18 596 -142 C ATOM 2722 N GLU A 374 -16.607 -11.478 -14.248 1.00 52.43 N ANISOU 2722 N GLU A 374 5168 7314 7441 -314 510 91 N ATOM 2723 CA GLU A 374 -16.824 -10.082 -13.881 1.00 52.32 C ANISOU 2723 CA GLU A 374 5163 7092 7625 -392 509 147 C ATOM 2724 C GLU A 374 -15.908 -9.674 -12.738 1.00 57.99 C ANISOU 2724 C GLU A 374 5732 7641 8660 -536 380 4 C ATOM 2725 O GLU A 374 -15.636 -10.467 -11.830 1.00 48.76 O ANISOU 2725 O GLU A 374 4537 6527 7462 -537 200 -183 O ATOM 2726 CB GLU A 374 -18.271 -9.822 -13.434 1.00 60.60 C ANISOU 2726 CB GLU A 374 6382 8126 8518 -327 386 85 C ATOM 2727 CG GLU A 374 -19.338 -10.478 -14.300 1.00 82.34 C ANISOU 2727 CG GLU A 374 9254 11066 10965 -179 402 128 C ATOM 2728 CD GLU A 374 -20.733 -9.949 -14.014 1.00 83.41 C ANISOU 2728 CD GLU A 374 9496 11161 11035 -114 318 105 C ATOM 2729 OE1 GLU A 374 -20.964 -9.409 -12.899 1.00 78.89 O ANISOU 2729 OE1 GLU A 374 8936 10445 10594 -172 236 5 O ATOM 2730 OE2 GLU A 374 -21.583 -10.061 -14.924 1.00 86.98 O ANISOU 2730 OE2 GLU A 374 10019 11728 11303 16 327 177 O ATOM 2731 N ARG A 375 -15.487 -8.404 -12.765 1.00 54.48 N ANISOU 2731 N ARG A 375 5206 6973 8520 -643 455 87 N ATOM 2732 CA ARG A 375 -14.808 -7.757 -11.647 1.00 53.75 C ANISOU 2732 CA ARG A 375 4989 6673 8761 -781 279 -90 C ATOM 2733 C ARG A 375 -15.298 -6.327 -11.539 1.00 53.47 C ANISOU 2733 C ARG A 375 5032 6381 8906 -835 309 -37 C ATOM 2734 O ARG A 375 -15.435 -5.632 -12.549 1.00 58.18 O ANISOU 2734 O ARG A 375 5649 6894 9561 -830 551 211 O ATOM 2735 CB ARG A 375 -13.275 -7.723 -11.797 1.00 50.61 C ANISOU 2735 CB ARG A 375 4286 6205 8739 -912 340 -84 C ATOM 2736 CG ARG A 375 -12.603 -9.085 -11.972 1.00 56.20 C ANISOU 2736 CG ARG A 375 4881 7143 9329 -846 335 -126 C ATOM 2737 CD ARG A 375 -12.595 -9.905 -10.707 1.00 50.47 C ANISOU 2737 CD ARG A 375 4200 6495 8481 -794 7 -395 C ATOM 2738 NE ARG A 375 -11.870 -11.162 -10.881 1.00 47.03 N ANISOU 2738 NE ARG A 375 3648 6243 7980 -722 6 -424 N ATOM 2739 CZ ARG A 375 -12.401 -12.291 -11.339 1.00 52.50 C ANISOU 2739 CZ ARG A 375 4487 7133 8328 -586 76 -380 C ATOM 2740 NH1 ARG A 375 -13.685 -12.339 -11.670 1.00 47.84 N ANISOU 2740 NH1 ARG A 375 4140 6599 7437 -516 135 -314 N ATOM 2741 NH2 ARG A 375 -11.639 -13.387 -11.466 1.00 62.18 N ANISOU 2741 NH2 ARG A 375 5598 8488 9538 -514 75 -419 N ATOM 2742 N VAL A 376 -15.526 -5.885 -10.315 1.00 53.30 N ANISOU 2742 N VAL A 376 5072 6221 8960 -866 70 -267 N ATOM 2743 CA VAL A 376 -15.816 -4.479 -10.077 1.00 62.86 C ANISOU 2743 CA VAL A 376 6338 7137 10411 -928 74 -268 C ATOM 2744 C VAL A 376 -14.509 -3.707 -10.106 1.00 69.09 C ANISOU 2744 C VAL A 376 6866 7668 11716 -1129 102 -278 C ATOM 2745 O VAL A 376 -13.529 -4.109 -9.467 1.00 63.18 O ANISOU 2745 O VAL A 376 5927 6931 11149 -1214 -85 -478 O ATOM 2746 CB VAL A 376 -16.544 -4.286 -8.741 1.00 54.79 C ANISOU 2746 CB VAL A 376 5500 6056 9263 -860 -182 -537 C ATOM 2747 CG1 VAL A 376 -16.661 -2.796 -8.423 1.00 51.89 C ANISOU 2747 CG1 VAL A 376 5175 5341 9202 -930 -202 -586 C ATOM 2748 CG2 VAL A 376 -17.922 -4.968 -8.778 1.00 51.17 C ANISOU 2748 CG2 VAL A 376 5257 5818 8368 -676 -149 -495 C ATOM 2749 N CYS A 377 -14.496 -2.603 -10.853 1.00 72.40 N ANISOU 2749 N CYS A 377 7266 7846 12398 -1200 337 -56 N ATOM 2750 CA CYS A 377 -13.371 -1.678 -10.860 1.00 70.57 C ANISOU 2750 CA CYS A 377 6777 7287 12748 -1421 400 -56 C ATOM 2751 C CYS A 377 -13.478 -0.797 -9.623 1.00 68.98 C ANISOU 2751 C CYS A 377 6623 6803 12784 -1495 98 -372 C ATOM 2752 O CYS A 377 -14.356 0.068 -9.544 1.00 77.08 O ANISOU 2752 O CYS A 377 7862 7646 13779 -1437 127 -339 O ATOM 2753 CB CYS A 377 -13.371 -0.835 -12.131 1.00 71.09 C ANISOU 2753 CB CYS A 377 6847 7172 12994 -1450 808 336 C ATOM 2754 SG CYS A 377 -12.114 0.440 -12.071 1.00 84.07 S ANISOU 2754 SG CYS A 377 8170 8325 15449 -1751 924 346 S ATOM 2755 N LYS A 378 -12.588 -0.996 -8.659 1.00 65.05 N ANISOU 2755 N LYS A 378 5935 6263 12517 -1600 -207 -694 N ATOM 2756 CA LYS A 378 -12.788 -0.370 -7.361 1.00 74.85 C ANISOU 2756 CA LYS A 378 7292 7304 13842 -1604 -561 -1061 C ATOM 2757 C LYS A 378 -12.105 0.983 -7.218 1.00 73.46 C ANISOU 2757 C LYS A 378 6931 6663 14317 -1830 -592 -1161 C ATOM 2758 O LYS A 378 -12.363 1.677 -6.231 1.00 78.19 O ANISOU 2758 O LYS A 378 7665 7046 14996 -1822 -868 -1468 O ATOM 2759 CB LYS A 378 -12.310 -1.301 -6.243 1.00 91.68 C ANISOU 2759 CB LYS A 378 9389 9642 15802 -1539 -952 -1404 C ATOM 2760 CG LYS A 378 -10.827 -1.308 -6.028 1.00 98.94 C ANISOU 2760 CG LYS A 378 9914 10456 17222 -1723 -1130 -1577 C ATOM 2761 CD LYS A 378 -10.489 -1.876 -4.668 1.00105.03 C ANISOU 2761 CD LYS A 378 10731 11347 17828 -1616 -1617 -1986 C ATOM 2762 CE LYS A 378 -10.961 -3.301 -4.510 1.00100.78 C ANISOU 2762 CE LYS A 378 10390 11218 16684 -1386 -1634 -1928 C ATOM 2763 NZ LYS A 378 -10.156 -3.947 -3.431 1.00107.85 N ANISOU 2763 NZ LYS A 378 11210 12221 17546 -1306 -2070 -2260 N ATOM 2764 N LYS A 379 -11.265 1.375 -8.178 1.00 70.25 N ANISOU 2764 N LYS A 379 6230 6082 14380 -2022 -294 -909 N ATOM 2765 CA LYS A 379 -10.575 2.656 -8.188 1.00 80.97 C ANISOU 2765 CA LYS A 379 7367 6950 16446 -2272 -249 -951 C ATOM 2766 C LYS A 379 -10.519 3.149 -9.624 1.00 89.59 C ANISOU 2766 C LYS A 379 8398 7897 17743 -2342 300 -448 C ATOM 2767 O LYS A 379 -10.353 2.352 -10.546 1.00 97.68 O ANISOU 2767 O LYS A 379 9365 9208 18541 -2273 583 -152 O ATOM 2768 CB LYS A 379 -9.125 2.559 -7.640 1.00 90.65 C ANISOU 2768 CB LYS A 379 8231 8155 18055 -2403 -494 -1215 C ATOM 2769 CG LYS A 379 -8.941 1.817 -6.308 1.00102.79 C ANISOU 2769 CG LYS A 379 9813 9920 19322 -2283 -1030 -1666 C ATOM 2770 CD LYS A 379 -9.554 2.578 -5.136 1.00118.66 C ANISOU 2770 CD LYS A 379 12106 11734 21246 -2208 -1387 -2028 C ATOM 2771 CE LYS A 379 -9.333 1.877 -3.791 1.00123.91 C ANISOU 2771 CE LYS A 379 12870 12634 21576 -2037 -1897 -2448 C ATOM 2772 NZ LYS A 379 -9.792 2.740 -2.649 1.00133.64 N ANISOU 2772 NZ LYS A 379 14385 13664 22728 -1943 -2216 -2801 N ATOM 2773 N ASP A 380 -10.660 4.457 -9.812 1.00 87.98 N ANISOU 2773 N ASP A 380 8242 7247 17939 -2450 456 -348 N ATOM 2774 CA ASP A 380 -10.355 5.084 -11.091 1.00 88.09 C ANISOU 2774 CA ASP A 380 8203 7091 18176 -2497 974 125 C ATOM 2775 C ASP A 380 -9.022 4.573 -11.641 1.00 98.23 C ANISOU 2775 C ASP A 380 9139 8540 19643 -2577 1155 237 C ATOM 2776 O ASP A 380 -7.974 4.850 -11.050 1.00103.51 O ANISOU 2776 O ASP A 380 9545 9104 20681 -2699 946 -29 O ATOM 2777 CB ASP A 380 -10.292 6.597 -10.904 1.00 90.45 C ANISOU 2777 CB ASP A 380 8556 6922 18887 -2582 1002 95 C ATOM 2778 CG ASP A 380 -11.636 7.211 -10.658 1.00 92.97 C ANISOU 2778 CG ASP A 380 9228 7029 19068 -2458 1248 394 C ATOM 2779 OD1 ASP A 380 -12.675 6.553 -10.900 1.00 83.27 O ANISOU 2779 OD1 ASP A 380 8283 5923 17433 -2285 1059 282 O ATOM 2780 OD2 ASP A 380 -11.641 8.363 -10.173 1.00104.14 O ANISOU 2780 OD2 ASP A 380 10658 8186 20724 -2482 1621 735 O ATOM 2781 N VAL A 381 -9.023 3.819 -12.747 1.00 99.45 N ANISOU 2781 N VAL A 381 9291 8956 19540 -2488 1531 611 N ATOM 2782 CA VAL A 381 -7.783 3.282 -13.308 1.00 95.53 C ANISOU 2782 CA VAL A 381 8491 8622 19186 -2527 1730 715 C ATOM 2783 C VAL A 381 -7.779 3.385 -14.828 1.00 89.91 C ANISOU 2783 C VAL A 381 7873 7934 18355 -2432 2328 1255 C ATOM 2784 O VAL A 381 -8.770 3.745 -15.464 1.00 94.34 O ANISOU 2784 O VAL A 381 8747 8439 18658 -2309 2568 1561 O ATOM 2785 CB VAL A 381 -7.521 1.813 -12.911 1.00100.92 C ANISOU 2785 CB VAL A 381 9044 9729 19573 -2458 1479 501 C ATOM 2786 CG1 VAL A 381 -7.435 1.677 -11.408 1.00105.10 C ANISOU 2786 CG1 VAL A 381 9517 10259 20157 -2500 881 -24 C ATOM 2787 CG2 VAL A 381 -8.575 0.893 -13.518 1.00 76.99 C ANISOU 2787 CG2 VAL A 381 6249 7017 15988 -2283 1640 726 C ATOM 2788 N GLU A 382 -6.628 3.030 -15.394 1.00 94.06 N ANISOU 2788 N GLU A 382 8139 8555 19043 -2458 2558 1361 N ATOM 2789 CA GLU A 382 -6.364 3.017 -16.823 1.00 92.28 C ANISOU 2789 CA GLU A 382 7981 8388 18693 -2342 3126 1834 C ATOM 2790 C GLU A 382 -5.563 1.758 -17.101 1.00104.24 C ANISOU 2790 C GLU A 382 9286 10264 20057 -2281 3172 1795 C ATOM 2791 O GLU A 382 -4.552 1.513 -16.437 1.00109.22 O ANISOU 2791 O GLU A 382 9578 10889 21030 -2407 2933 1501 O ATOM 2792 CB GLU A 382 -5.580 4.273 -17.262 1.00 99.95 C ANISOU 2792 CB GLU A 382 8824 8953 20198 -2462 3436 2016 C ATOM 2793 CG GLU A 382 -5.420 4.447 -18.762 1.00102.23 C ANISOU 2793 CG GLU A 382 9260 9254 20328 -2307 4049 2535 C ATOM 2794 CD GLU A 382 -4.875 5.825 -19.140 1.00119.69 C ANISOU 2794 CD GLU A 382 11399 11013 23064 -2418 4359 2734 C ATOM 2795 OE1 GLU A 382 -5.534 6.846 -18.825 1.00123.24 O ANISOU 2795 OE1 GLU A 382 12019 11156 23651 -2462 4280 2736 O ATOM 2796 OE2 GLU A 382 -3.780 5.887 -19.748 1.00115.94 O ANISOU 2796 OE2 GLU A 382 10691 10478 22884 -2457 4693 2887 O ATOM 2797 N ILE A 383 -6.015 0.949 -18.054 1.00106.45 N ANISOU 2797 N ILE A 383 9774 10859 19812 -2065 3453 2073 N ATOM 2798 CA ILE A 383 -5.399 -0.349 -18.313 1.00104.14 C ANISOU 2798 CA ILE A 383 9329 10932 19306 -1971 3482 2017 C ATOM 2799 C ILE A 383 -5.219 -0.515 -19.815 1.00105.88 C ANISOU 2799 C ILE A 383 9716 11278 19237 -1769 4041 2452 C ATOM 2800 O ILE A 383 -6.200 -0.519 -20.570 1.00100.72 O ANISOU 2800 O ILE A 383 9435 10735 18100 -1566 4246 2729 O ATOM 2801 CB ILE A 383 -6.217 -1.509 -17.721 1.00 96.66 C ANISOU 2801 CB ILE A 383 8480 10332 17913 -1873 3132 1788 C ATOM 2802 CG1 ILE A 383 -7.638 -1.532 -18.260 1.00 89.98 C ANISOU 2802 CG1 ILE A 383 8033 9599 16556 -1693 3264 2030 C ATOM 2803 CG2 ILE A 383 -6.287 -1.397 -16.210 1.00101.72 C ANISOU 2803 CG2 ILE A 383 8975 10863 18809 -2038 2566 1336 C ATOM 2804 CD1 ILE A 383 -8.327 -2.836 -17.994 1.00 89.25 C ANISOU 2804 CD1 ILE A 383 8105 9925 15880 -1504 2964 1825 C ATOM 2805 N ASN A 384 -3.966 -0.650 -20.248 1.00114.81 N ANISOU 2805 N ASN A 384 10585 12392 20645 -1801 4278 2506 N ATOM 2806 CA ASN A 384 -3.644 -0.756 -21.667 1.00116.53 C ANISOU 2806 CA ASN A 384 10953 12700 20622 -1602 4826 2900 C ATOM 2807 C ASN A 384 -4.294 0.387 -22.441 1.00116.34 C ANISOU 2807 C ASN A 384 11263 12434 20507 -1514 5157 3280 C ATOM 2808 O ASN A 384 -5.050 0.181 -23.394 1.00116.28 O ANISOU 2808 O ASN A 384 11647 12610 19924 -1243 5398 3567 O ATOM 2809 CB ASN A 384 -4.079 -2.113 -22.229 1.00114.40 C ANISOU 2809 CB ASN A 384 10890 12888 19689 -1338 4868 2933 C ATOM 2810 CG ASN A 384 -3.627 -3.283 -21.368 1.00112.78 C ANISOU 2810 CG ASN A 384 10398 12924 19528 -1397 4493 2546 C ATOM 2811 OD1 ASN A 384 -4.193 -3.549 -20.305 1.00107.90 O ANISOU 2811 OD1 ASN A 384 9745 12356 18898 -1483 4041 2250 O ATOM 2812 ND2 ASN A 384 -2.619 -4.000 -21.836 1.00117.26 N ANISOU 2812 ND2 ASN A 384 10779 13643 20132 -1327 4684 2555 N ATOM 2813 N GLY A 385 -4.035 1.607 -21.983 1.00116.18 N ANISOU 2813 N GLY A 385 11102 11998 21045 -1727 5130 3257 N ATOM 2814 CA GLY A 385 -4.526 2.787 -22.673 1.00119.58 C ANISOU 2814 CA GLY A 385 11816 12145 21475 -1652 5453 3615 C ATOM 2815 C GLY A 385 -6.032 2.941 -22.752 1.00119.77 C ANISOU 2815 C GLY A 385 12281 12241 20987 -1478 5339 3731 C ATOM 2816 O GLY A 385 -6.536 3.526 -23.715 1.00123.67 O ANISOU 2816 O GLY A 385 13120 12661 21206 -1270 5673 4112 O ATOM 2817 N MET A 386 -6.774 2.433 -21.773 1.00117.67 N ANISOU 2817 N MET A 386 12018 12113 20578 -1537 4877 3418 N ATOM 2818 CA MET A 386 -8.201 2.708 -21.693 1.00111.12 C ANISOU 2818 CA MET A 386 11559 11286 19376 -1406 4742 3503 C ATOM 2819 C MET A 386 -8.539 3.115 -20.273 1.00108.32 C ANISOU 2819 C MET A 386 11054 10712 19392 -1647 4269 3120 C ATOM 2820 O MET A 386 -8.199 2.401 -19.326 1.00116.23 O ANISOU 2820 O MET A 386 11790 11847 20526 -1792 3907 2734 O ATOM 2821 CB MET A 386 -9.041 1.506 -22.108 1.00108.38 C ANISOU 2821 CB MET A 386 11465 11401 18314 -1144 4693 3552 C ATOM 2822 CG MET A 386 -10.536 1.764 -21.980 1.00111.43 C ANISOU 2822 CG MET A 386 12209 11792 18337 -998 4531 3636 C ATOM 2823 SD MET A 386 -11.532 0.382 -22.562 1.00105.76 S ANISOU 2823 SD MET A 386 11829 11664 16690 -621 4365 3606 S ATOM 2824 CE MET A 386 -10.929 0.254 -24.249 1.00117.11 C ANISOU 2824 CE MET A 386 13455 13233 17807 -353 4982 4084 C ATOM 2825 N PHE A 387 -9.206 4.253 -20.124 1.00102.21 N ANISOU 2825 N PHE A 387 10473 9603 18760 -1662 4258 3214 N ATOM 2826 CA PHE A 387 -9.660 4.674 -18.810 1.00100.12 C ANISOU 2826 CA PHE A 387 10139 9122 18778 -1844 3807 2842 C ATOM 2827 C PHE A 387 -10.875 3.856 -18.387 1.00 94.48 C ANISOU 2827 C PHE A 387 9628 8676 17594 -1721 3526 2727 C ATOM 2828 O PHE A 387 -11.780 3.616 -19.188 1.00 96.62 O ANISOU 2828 O PHE A 387 10262 9183 17264 -1418 3639 2979 O ATOM 2829 CB PHE A 387 -10.003 6.162 -18.805 1.00 94.48 C ANISOU 2829 CB PHE A 387 9584 7948 18366 -1876 3895 2972 C ATOM 2830 CG PHE A 387 -10.712 6.591 -17.570 1.00106.78 C ANISOU 2830 CG PHE A 387 11182 9299 20089 -1984 3450 2614 C ATOM 2831 CD1 PHE A 387 -12.049 6.947 -17.607 1.00107.27 C ANISOU 2831 CD1 PHE A 387 11615 9285 19859 -1805 3405 2746 C ATOM 2832 CD2 PHE A 387 -10.056 6.586 -16.353 1.00108.58 C ANISOU 2832 CD2 PHE A 387 11099 9431 20726 -2225 3050 2127 C ATOM 2833 CE1 PHE A 387 -12.704 7.334 -16.457 1.00107.21 C ANISOU 2833 CE1 PHE A 387 11662 9074 19999 -1878 3005 2395 C ATOM 2834 CE2 PHE A 387 -10.706 6.960 -15.198 1.00111.35 C ANISOU 2834 CE2 PHE A 387 11529 9609 21170 -2285 2627 1763 C ATOM 2835 CZ PHE A 387 -12.032 7.341 -15.250 1.00110.22 C ANISOU 2835 CZ PHE A 387 11753 9362 20762 -2118 2619 1893 C ATOM 2836 N ILE A 388 -10.881 3.421 -17.125 1.00 92.15 N ANISOU 2836 N ILE A 388 9174 8461 17377 -1845 3023 2235 N ATOM 2837 CA ILE A 388 -12.024 2.724 -16.522 1.00 82.30 C ANISOU 2837 CA ILE A 388 8189 7555 15528 -1638 2588 1956 C ATOM 2838 C ILE A 388 -12.448 3.432 -15.244 1.00 85.86 C ANISOU 2838 C ILE A 388 8663 7737 16222 -1747 2191 1591 C ATOM 2839 O ILE A 388 -11.688 3.448 -14.264 1.00 88.21 O ANISOU 2839 O ILE A 388 8680 7900 16937 -1972 1928 1241 O ATOM 2840 CB ILE A 388 -11.698 1.260 -16.225 1.00 79.34 C ANISOU 2840 CB ILE A 388 7674 7622 14849 -1598 2369 1711 C ATOM 2841 CG1 ILE A 388 -11.266 0.553 -17.503 1.00 81.04 C ANISOU 2841 CG1 ILE A 388 7884 8096 14810 -1466 2769 2044 C ATOM 2842 CG2 ILE A 388 -12.905 0.537 -15.596 1.00 72.93 C ANISOU 2842 CG2 ILE A 388 7126 7125 13458 -1398 1968 1449 C ATOM 2843 CD1 ILE A 388 -11.052 -0.895 -17.298 1.00 83.33 C ANISOU 2843 CD1 ILE A 388 8084 8805 14772 -1391 2570 1821 C ATOM 2844 N PRO A 389 -13.647 4.013 -15.209 1.00 89.46 N ANISOU 2844 N PRO A 389 9452 8118 16422 -1571 2120 1642 N ATOM 2845 CA PRO A 389 -14.088 4.736 -14.010 1.00 90.73 C ANISOU 2845 CA PRO A 389 9669 8009 16794 -1641 1777 1295 C ATOM 2846 C PRO A 389 -14.374 3.778 -12.870 1.00 82.10 C ANISOU 2846 C PRO A 389 8571 7234 15389 -1596 1323 848 C ATOM 2847 O PRO A 389 -14.898 2.689 -13.085 1.00 74.41 O ANISOU 2847 O PRO A 389 7703 6690 13879 -1414 1266 860 O ATOM 2848 CB PRO A 389 -15.376 5.439 -14.464 1.00 86.24 C ANISOU 2848 CB PRO A 389 9468 7354 15946 -1394 1874 1525 C ATOM 2849 CG PRO A 389 -15.462 5.248 -15.941 1.00 87.50 C ANISOU 2849 CG PRO A 389 9750 7671 15824 -1220 2277 2016 C ATOM 2850 CD PRO A 389 -14.654 4.042 -16.278 1.00 87.42 C ANISOU 2850 CD PRO A 389 9533 8019 15662 -1270 2339 2009 C ATOM 2851 N LYS A 390 -14.027 4.201 -11.654 1.00 83.87 N ANISOU 2851 N LYS A 390 8688 7224 15955 -1755 1003 451 N ATOM 2852 CA LYS A 390 -14.378 3.456 -10.451 1.00 78.36 C ANISOU 2852 CA LYS A 390 8057 6774 14942 -1675 578 32 C ATOM 2853 C LYS A 390 -15.842 3.057 -10.463 1.00 76.15 C ANISOU 2853 C LYS A 390 8111 6770 14054 -1388 539 78 C ATOM 2854 O LYS A 390 -16.710 3.864 -10.795 1.00 75.18 O ANISOU 2854 O LYS A 390 8195 6479 13892 -1269 665 242 O ATOM 2855 CB LYS A 390 -14.086 4.312 -9.218 1.00 86.25 C ANISOU 2855 CB LYS A 390 9016 7411 16344 -1813 258 -373 C ATOM 2856 CG LYS A 390 -14.716 3.799 -7.935 1.00 85.20 C ANISOU 2856 CG LYS A 390 9078 7481 15812 -1657 -141 -775 C ATOM 2857 CD LYS A 390 -14.448 4.801 -6.831 1.00104.14 C ANISOU 2857 CD LYS A 390 11486 9483 18600 -1762 -439 -1170 C ATOM 2858 CE LYS A 390 -14.936 4.330 -5.473 1.00112.00 C ANISOU 2858 CE LYS A 390 12698 10665 19193 -1588 -830 -1587 C ATOM 2859 NZ LYS A 390 -14.692 5.384 -4.435 1.00119.01 N ANISOU 2859 NZ LYS A 390 13634 11146 20436 -1660 -1132 -1998 N ATOM 2860 N GLY A 391 -16.119 1.795 -10.115 1.00 61.64 N ANISOU 2860 N GLY A 391 6307 5344 11770 -1272 373 -59 N ATOM 2861 CA GLY A 391 -17.469 1.313 -9.968 1.00 58.39 C ANISOU 2861 CA GLY A 391 6150 5187 10847 -1029 311 -72 C ATOM 2862 C GLY A 391 -18.029 0.621 -11.193 1.00 61.81 C ANISOU 2862 C GLY A 391 6648 5921 10914 -875 534 252 C ATOM 2863 O GLY A 391 -19.064 -0.045 -11.094 1.00 63.17 O ANISOU 2863 O GLY A 391 6964 6356 10681 -695 458 214 O ATOM 2864 N VAL A 392 -17.396 0.792 -12.350 1.00 59.16 N ANISOU 2864 N VAL A 392 6215 5540 10721 -930 815 565 N ATOM 2865 CA VAL A 392 -17.808 0.052 -13.530 1.00 64.12 C ANISOU 2865 CA VAL A 392 6923 6479 10962 -760 997 836 C ATOM 2866 C VAL A 392 -17.562 -1.421 -13.279 1.00 61.67 C ANISOU 2866 C VAL A 392 6524 6530 10379 -751 857 665 C ATOM 2867 O VAL A 392 -16.576 -1.802 -12.636 1.00 71.20 O ANISOU 2867 O VAL A 392 7538 7725 11790 -908 746 473 O ATOM 2868 CB VAL A 392 -17.024 0.554 -14.758 1.00 70.40 C ANISOU 2868 CB VAL A 392 7652 7134 11962 -809 1362 1208 C ATOM 2869 CG1 VAL A 392 -17.224 -0.363 -15.987 1.00 63.91 C ANISOU 2869 CG1 VAL A 392 6917 6669 10699 -619 1537 1448 C ATOM 2870 CG2 VAL A 392 -17.423 1.961 -15.073 1.00 73.41 C ANISOU 2870 CG2 VAL A 392 8175 7151 12568 -776 1521 1421 C ATOM 2871 N VAL A 393 -18.457 -2.262 -13.771 1.00 55.19 N ANISOU 2871 N VAL A 393 5833 6017 9118 -561 842 719 N ATOM 2872 CA VAL A 393 -18.209 -3.695 -13.782 1.00 63.13 C ANISOU 2872 CA VAL A 393 6770 7343 9874 -540 767 611 C ATOM 2873 C VAL A 393 -17.517 -4.023 -15.098 1.00 64.49 C ANISOU 2873 C VAL A 393 6888 7628 9989 -510 1032 874 C ATOM 2874 O VAL A 393 -18.055 -3.751 -16.174 1.00 64.63 O ANISOU 2874 O VAL A 393 7055 7696 9806 -351 1197 1123 O ATOM 2875 CB VAL A 393 -19.507 -4.498 -13.606 1.00 57.68 C ANISOU 2875 CB VAL A 393 6223 6899 8795 -371 613 502 C ATOM 2876 CG1 VAL A 393 -19.227 -5.978 -13.709 1.00 50.77 C ANISOU 2876 CG1 VAL A 393 5286 6308 7697 -354 561 409 C ATOM 2877 CG2 VAL A 393 -20.129 -4.176 -12.254 1.00 54.15 C ANISOU 2877 CG2 VAL A 393 5834 6337 8404 -385 412 257 C ATOM 2878 N VAL A 394 -16.312 -4.572 -15.013 1.00 55.99 N ANISOU 2878 N VAL A 394 5604 6587 9081 -637 1077 820 N ATOM 2879 CA VAL A 394 -15.592 -5.062 -16.179 1.00 57.51 C ANISOU 2879 CA VAL A 394 5736 6920 9197 -589 1348 1036 C ATOM 2880 C VAL A 394 -15.949 -6.524 -16.384 1.00 60.55 C ANISOU 2880 C VAL A 394 6185 7651 9171 -450 1237 919 C ATOM 2881 O VAL A 394 -15.756 -7.360 -15.491 1.00 58.14 O ANISOU 2881 O VAL A 394 5790 7434 8865 -506 1021 666 O ATOM 2882 CB VAL A 394 -14.079 -4.875 -16.011 1.00 62.67 C ANISOU 2882 CB VAL A 394 6086 7417 10309 -793 1479 1039 C ATOM 2883 CG1 VAL A 394 -13.319 -5.429 -17.213 1.00 56.96 C ANISOU 2883 CG1 VAL A 394 5295 6849 9499 -719 1811 1268 C ATOM 2884 CG2 VAL A 394 -13.766 -3.405 -15.810 1.00 66.11 C ANISOU 2884 CG2 VAL A 394 6446 7460 11212 -954 1583 1136 C ATOM 2885 N MET A 395 -16.490 -6.835 -17.550 1.00 63.87 N ANISOU 2885 N MET A 395 6779 8252 9237 -253 1371 1095 N ATOM 2886 CA MET A 395 -17.020 -8.160 -17.817 1.00 54.25 C ANISOU 2886 CA MET A 395 5647 7329 7634 -111 1241 961 C ATOM 2887 C MET A 395 -16.233 -8.805 -18.947 1.00 62.78 C ANISOU 2887 C MET A 395 6720 8572 8560 -10 1485 1100 C ATOM 2888 O MET A 395 -15.931 -8.159 -19.955 1.00 66.22 O ANISOU 2888 O MET A 395 7230 8964 8966 74 1773 1381 O ATOM 2889 CB MET A 395 -18.504 -8.094 -18.151 1.00 52.46 C ANISOU 2889 CB MET A 395 5636 7199 7098 65 1102 963 C ATOM 2890 CG MET A 395 -19.177 -9.446 -18.322 1.00 54.01 C ANISOU 2890 CG MET A 395 5893 7657 6972 180 925 778 C ATOM 2891 SD MET A 395 -19.084 -10.039 -20.021 1.00 59.52 S ANISOU 2891 SD MET A 395 6750 8593 7274 424 1082 927 S ATOM 2892 CE MET A 395 -20.358 -9.043 -20.777 1.00 61.63 C ANISOU 2892 CE MET A 395 7235 8851 7329 637 1033 1101 C ATOM 2893 N ILE A 396 -15.851 -10.060 -18.751 1.00 54.58 N ANISOU 2893 N ILE A 396 5601 7702 7433 -7 1397 915 N ATOM 2894 CA ILE A 396 -15.209 -10.839 -19.801 1.00 55.94 C ANISOU 2894 CA ILE A 396 5792 8054 7408 128 1609 997 C ATOM 2895 C ILE A 396 -16.228 -11.862 -20.299 1.00 58.78 C ANISOU 2895 C ILE A 396 6359 8645 7328 321 1431 858 C ATOM 2896 O ILE A 396 -16.638 -12.769 -19.548 1.00 52.95 O ANISOU 2896 O ILE A 396 5589 7965 6564 277 1179 606 O ATOM 2897 CB ILE A 396 -13.916 -11.519 -19.327 1.00 64.42 C ANISOU 2897 CB ILE A 396 6606 9129 8741 15 1660 889 C ATOM 2898 CG1 ILE A 396 -12.880 -10.473 -18.931 1.00 69.73 C ANISOU 2898 CG1 ILE A 396 7029 9561 9906 -183 1823 1009 C ATOM 2899 CG2 ILE A 396 -13.317 -12.368 -20.441 1.00 60.15 C ANISOU 2899 CG2 ILE A 396 6102 8780 7973 189 1899 961 C ATOM 2900 CD1 ILE A 396 -12.966 -10.050 -17.505 1.00 66.09 C ANISOU 2900 CD1 ILE A 396 6444 8923 9744 -374 1528 810 C ATOM 2901 N PRO A 397 -16.659 -11.760 -21.521 1.00 60.57 N ANISOU 2901 N PRO A 397 6800 8994 7219 539 1544 1005 N ATOM 2902 CA PRO A 397 -17.664 -12.679 -22.073 1.00 61.63 C ANISOU 2902 CA PRO A 397 7121 9339 6957 730 1331 839 C ATOM 2903 C PRO A 397 -17.049 -13.978 -22.586 1.00 65.25 C ANISOU 2903 C PRO A 397 7589 9967 7236 830 1388 708 C ATOM 2904 O PRO A 397 -16.799 -14.155 -23.775 1.00 63.90 O ANISOU 2904 O PRO A 397 7586 9934 6761 1048 1570 814 O ATOM 2905 CB PRO A 397 -18.274 -11.852 -23.205 1.00 64.15 C ANISOU 2905 CB PRO A 397 7685 9706 6985 957 1421 1070 C ATOM 2906 CG PRO A 397 -17.119 -11.000 -23.682 1.00 66.71 C ANISOU 2906 CG PRO A 397 7983 9913 7452 943 1838 1393 C ATOM 2907 CD PRO A 397 -16.281 -10.702 -22.477 1.00 66.69 C ANISOU 2907 CD PRO A 397 7676 9699 7963 636 1875 1348 C ATOM 2908 N SER A 398 -16.843 -14.919 -21.650 1.00 63.14 N ANISOU 2908 N SER A 398 7168 9684 7139 692 1227 470 N ATOM 2909 CA SER A 398 -16.144 -16.177 -21.956 1.00 63.99 C ANISOU 2909 CA SER A 398 7255 9906 7154 769 1282 332 C ATOM 2910 C SER A 398 -16.824 -16.941 -23.076 1.00 61.06 C ANISOU 2910 C SER A 398 7125 9720 6355 1015 1201 219 C ATOM 2911 O SER A 398 -16.165 -17.425 -24.007 1.00 65.06 O ANISOU 2911 O SER A 398 7724 10346 6650 1194 1398 246 O ATOM 2912 CB SER A 398 -16.078 -17.087 -20.730 1.00 57.97 C ANISOU 2912 CB SER A 398 6341 9077 6607 615 1071 95 C ATOM 2913 OG SER A 398 -15.349 -16.487 -19.695 1.00 57.64 O ANISOU 2913 OG SER A 398 6089 8883 6928 424 1103 155 O ATOM 2914 N TYR A 399 -18.142 -17.120 -22.969 1.00 57.81 N ANISOU 2914 N TYR A 399 6804 9333 5826 1033 899 61 N ATOM 2915 CA TYR A 399 -18.849 -17.863 -24.007 1.00 68.60 C ANISOU 2915 CA TYR A 399 8380 10866 6818 1263 747 -105 C ATOM 2916 C TYR A 399 -18.574 -17.270 -25.377 1.00 73.65 C ANISOU 2916 C TYR A 399 9250 11640 7094 1533 962 109 C ATOM 2917 O TYR A 399 -18.310 -18.000 -26.341 1.00 83.57 O ANISOU 2917 O TYR A 399 10680 13045 8029 1757 1016 20 O ATOM 2918 CB TYR A 399 -20.350 -17.886 -23.729 1.00 64.24 C ANISOU 2918 CB TYR A 399 7841 10306 6263 1237 398 -275 C ATOM 2919 CG TYR A 399 -21.181 -18.575 -24.788 1.00 58.38 C ANISOU 2919 CG TYR A 399 7283 9723 5175 1468 165 -488 C ATOM 2920 CD1 TYR A 399 -21.664 -19.857 -24.590 1.00 52.25 C ANISOU 2920 CD1 TYR A 399 6460 8937 4455 1424 -69 -820 C ATOM 2921 CD2 TYR A 399 -21.493 -17.932 -25.991 1.00 64.52 C ANISOU 2921 CD2 TYR A 399 8294 10647 5575 1745 166 -363 C ATOM 2922 CE1 TYR A 399 -22.434 -20.497 -25.580 1.00 62.01 C ANISOU 2922 CE1 TYR A 399 7850 10302 5407 1632 -330 -1068 C ATOM 2923 CE2 TYR A 399 -22.253 -18.543 -26.960 1.00 72.46 C ANISOU 2923 CE2 TYR A 399 9480 11809 6243 1985 -103 -594 C ATOM 2924 CZ TYR A 399 -22.725 -19.822 -26.758 1.00 74.89 C ANISOU 2924 CZ TYR A 399 9711 12102 6641 1919 -368 -967 C ATOM 2925 OH TYR A 399 -23.484 -20.403 -27.752 1.00 78.04 O ANISOU 2925 OH TYR A 399 10279 12644 6729 2158 -678 -1238 O ATOM 2926 N ALA A 400 -18.603 -15.944 -25.480 1.00 62.77 N ANISOU 2926 N ALA A 400 7900 10196 5752 1533 1109 402 N ATOM 2927 CA ALA A 400 -18.470 -15.351 -26.801 1.00 67.10 C ANISOU 2927 CA ALA A 400 8717 10861 5915 1825 1323 642 C ATOM 2928 C ALA A 400 -17.066 -15.532 -27.353 1.00 74.41 C ANISOU 2928 C ALA A 400 9654 11823 6797 1902 1755 808 C ATOM 2929 O ALA A 400 -16.896 -15.712 -28.564 1.00 77.78 O ANISOU 2929 O ALA A 400 10351 12414 6790 2210 1915 881 O ATOM 2930 CB ALA A 400 -18.856 -13.877 -26.749 1.00 64.74 C ANISOU 2930 CB ALA A 400 8457 10443 5701 1810 1396 939 C ATOM 2931 N LEU A 401 -16.058 -15.524 -26.484 1.00 76.56 N ANISOU 2931 N LEU A 401 9631 11950 7506 1648 1938 851 N ATOM 2932 CA LEU A 401 -14.686 -15.674 -26.941 1.00 82.76 C ANISOU 2932 CA LEU A 401 10350 12755 8339 1704 2364 1007 C ATOM 2933 C LEU A 401 -14.381 -17.113 -27.317 1.00 86.20 C ANISOU 2933 C LEU A 401 10845 13347 8561 1854 2321 738 C ATOM 2934 O LEU A 401 -13.599 -17.352 -28.243 1.00 94.73 O ANISOU 2934 O LEU A 401 12037 14535 9421 2072 2662 846 O ATOM 2935 CB LEU A 401 -13.721 -15.170 -25.867 1.00 82.73 C ANISOU 2935 CB LEU A 401 9972 12541 8921 1387 2518 1108 C ATOM 2936 CG LEU A 401 -14.062 -13.755 -25.364 1.00 84.27 C ANISOU 2936 CG LEU A 401 10103 12536 9381 1214 2519 1321 C ATOM 2937 CD1 LEU A 401 -13.054 -13.212 -24.368 1.00 86.34 C ANISOU 2937 CD1 LEU A 401 9997 12578 10229 913 2648 1388 C ATOM 2938 CD2 LEU A 401 -14.204 -12.795 -26.522 1.00 94.50 C ANISOU 2938 CD2 LEU A 401 11662 13847 10398 1432 2814 1666 C ATOM 2939 N HIS A 402 -15.018 -18.077 -26.652 1.00 80.35 N ANISOU 2939 N HIS A 402 10050 12606 7874 1760 1930 395 N ATOM 2940 CA HIS A 402 -14.825 -19.476 -27.012 1.00 73.95 C ANISOU 2940 CA HIS A 402 9318 11903 6876 1906 1859 115 C ATOM 2941 C HIS A 402 -15.270 -19.782 -28.441 1.00 72.33 C ANISOU 2941 C HIS A 402 9489 11901 6091 2274 1858 53 C ATOM 2942 O HIS A 402 -14.842 -20.795 -29.004 1.00 77.89 O ANISOU 2942 O HIS A 402 10304 12703 6590 2460 1922 -128 O ATOM 2943 CB HIS A 402 -15.557 -20.360 -25.998 1.00 64.33 C ANISOU 2943 CB HIS A 402 7984 10598 5860 1720 1449 -210 C ATOM 2944 CG HIS A 402 -14.933 -20.346 -24.639 1.00 62.64 C ANISOU 2944 CG HIS A 402 7453 10215 6132 1435 1457 -191 C ATOM 2945 ND1 HIS A 402 -15.272 -21.248 -23.649 1.00 62.50 N ANISOU 2945 ND1 HIS A 402 7331 10100 6314 1289 1190 -433 N ATOM 2946 CD2 HIS A 402 -13.996 -19.528 -24.097 1.00 59.98 C ANISOU 2946 CD2 HIS A 402 6889 9779 6122 1284 1686 37 C ATOM 2947 CE1 HIS A 402 -14.568 -20.986 -22.559 1.00 56.25 C ANISOU 2947 CE1 HIS A 402 6295 9183 5895 1091 1239 -354 C ATOM 2948 NE2 HIS A 402 -13.786 -19.949 -22.805 1.00 59.36 N ANISOU 2948 NE2 HIS A 402 6591 9572 6389 1076 1515 -93 N ATOM 2949 N ARG A 403 -16.094 -18.916 -29.046 1.00 77.30 N ANISOU 2949 N ARG A 403 10336 12594 6440 2411 1782 194 N ATOM 2950 CA ARG A 403 -16.649 -19.123 -30.383 1.00 84.45 C ANISOU 2950 CA ARG A 403 11636 13706 6745 2798 1700 120 C ATOM 2951 C ARG A 403 -16.264 -18.011 -31.346 1.00 91.66 C ANISOU 2951 C ARG A 403 12786 14691 7350 3041 2094 535 C ATOM 2952 O ARG A 403 -16.884 -17.865 -32.409 1.00 97.75 O ANISOU 2952 O ARG A 403 13925 15629 7587 3386 1995 542 O ATOM 2953 CB ARG A 403 -18.168 -19.248 -30.321 1.00 80.26 C ANISOU 2953 CB ARG A 403 11187 13206 6101 2810 1162 -139 C ATOM 2954 CG ARG A 403 -18.608 -20.405 -29.480 1.00 77.63 C ANISOU 2954 CG ARG A 403 10653 12785 6058 2593 816 -535 C ATOM 2955 CD ARG A 403 -20.053 -20.274 -29.113 1.00 73.59 C ANISOU 2955 CD ARG A 403 10088 12240 5631 2502 360 -714 C ATOM 2956 NE ARG A 403 -20.508 -21.448 -28.380 1.00 77.69 N ANISOU 2956 NE ARG A 403 10431 12655 6434 2306 71 -1082 N ATOM 2957 CZ ARG A 403 -21.195 -22.452 -28.921 1.00 81.38 C ANISOU 2957 CZ ARG A 403 11012 13182 6728 2437 -257 -1459 C ATOM 2958 NH1 ARG A 403 -21.517 -22.423 -30.212 1.00 85.98 N ANISOU 2958 NH1 ARG A 403 11904 13959 6804 2792 -382 -1545 N ATOM 2959 NH2 ARG A 403 -21.561 -23.482 -28.165 1.00 73.87 N ANISOU 2959 NH2 ARG A 403 9875 12079 6111 2222 -464 -1751 N ATOM 2960 N ASP A 404 -15.263 -17.229 -30.996 1.00 95.59 N ANISOU 2960 N ASP A 404 13082 15054 8183 2877 2531 880 N ATOM 2961 CA ASP A 404 -14.777 -16.181 -31.879 1.00107.86 C ANISOU 2961 CA ASP A 404 14838 16627 9517 3084 2996 1321 C ATOM 2962 C ASP A 404 -14.031 -16.800 -33.052 1.00113.37 C ANISOU 2962 C ASP A 404 15762 17424 9888 3368 3257 1320 C ATOM 2963 O ASP A 404 -13.052 -17.529 -32.837 1.00111.12 O ANISOU 2963 O ASP A 404 15276 17116 9830 3282 3457 1226 O ATOM 2964 CB ASP A 404 -13.865 -15.233 -31.106 1.00113.77 C ANISOU 2964 CB ASP A 404 15233 17134 10859 2761 3363 1644 C ATOM 2965 CG ASP A 404 -13.444 -14.016 -31.922 1.00121.72 C ANISOU 2965 CG ASP A 404 16415 18069 11765 2907 3841 2130 C ATOM 2966 OD1 ASP A 404 -13.674 -13.984 -33.150 1.00126.64 O ANISOU 2966 OD1 ASP A 404 17415 18774 11929 3227 3854 2196 O ATOM 2967 OD2 ASP A 404 -12.883 -13.075 -31.322 1.00121.69 O ANISOU 2967 OD2 ASP A 404 16142 17843 12253 2646 4117 2405 O ATOM 2968 N PRO A 405 -14.452 -16.547 -34.294 1.00114.74 N ANISOU 2968 N PRO A 405 16329 17667 9599 3688 3214 1404 N ATOM 2969 CA PRO A 405 -13.649 -16.990 -35.444 1.00115.93 C ANISOU 2969 CA PRO A 405 16684 17858 9507 3934 3491 1446 C ATOM 2970 C PRO A 405 -12.223 -16.459 -35.435 1.00119.47 C ANISOU 2970 C PRO A 405 16913 18151 10329 3800 4095 1802 C ATOM 2971 O PRO A 405 -11.328 -17.111 -35.986 1.00121.57 O ANISOU 2971 O PRO A 405 17193 18445 10553 3907 4343 1763 O ATOM 2972 CB PRO A 405 -14.445 -16.458 -36.644 1.00111.35 C ANISOU 2972 CB PRO A 405 16544 17355 8411 4290 3351 1555 C ATOM 2973 CG PRO A 405 -15.846 -16.398 -36.163 1.00111.47 C ANISOU 2973 CG PRO A 405 16586 17434 8332 4263 2798 1332 C ATOM 2974 CD PRO A 405 -15.760 -16.008 -34.706 1.00112.93 C ANISOU 2974 CD PRO A 405 16377 17507 9023 3873 2843 1397 C ATOM 2975 N LYS A 406 -11.977 -15.304 -34.812 1.00117.36 N ANISOU 2975 N LYS A 406 16421 17704 10467 3558 4328 2131 N ATOM 2976 CA LYS A 406 -10.641 -14.713 -34.801 1.00117.73 C ANISOU 2976 CA LYS A 406 16214 17563 10955 3398 4870 2455 C ATOM 2977 C LYS A 406 -9.657 -15.457 -33.898 1.00115.39 C ANISOU 2977 C LYS A 406 15469 17223 11150 3129 4967 2278 C ATOM 2978 O LYS A 406 -8.507 -15.019 -33.783 1.00119.93 O ANISOU 2978 O LYS A 406 15759 17635 12174 2962 5366 2498 O ATOM 2979 CB LYS A 406 -10.736 -13.239 -34.395 1.00123.34 C ANISOU 2979 CB LYS A 406 16813 18049 12001 3205 5038 2823 C ATOM 2980 CG LYS A 406 -11.713 -12.443 -35.263 1.00136.96 C ANISOU 2980 CG LYS A 406 18977 19798 13262 3494 4939 3018 C ATOM 2981 CD LYS A 406 -11.395 -10.947 -35.296 1.00148.07 C ANISOU 2981 CD LYS A 406 20334 20929 14996 3383 5300 3473 C ATOM 2982 CE LYS A 406 -12.034 -10.270 -36.514 1.00154.93 C ANISOU 2982 CE LYS A 406 21689 21825 15353 3773 5329 3710 C ATOM 2983 NZ LYS A 406 -11.805 -8.796 -36.553 1.00156.69 N ANISOU 2983 NZ LYS A 406 21890 21751 15893 3683 5672 4151 N ATOM 2984 N TYR A 407 -10.077 -16.555 -33.262 1.00109.82 N ANISOU 2984 N TYR A 407 14685 16645 10396 3091 4598 1882 N ATOM 2985 CA TYR A 407 -9.198 -17.435 -32.491 1.00 99.37 C ANISOU 2985 CA TYR A 407 12984 15301 9471 2911 4643 1676 C ATOM 2986 C TYR A 407 -9.461 -18.914 -32.712 1.00103.21 C ANISOU 2986 C TYR A 407 13627 15954 9632 3101 4367 1263 C ATOM 2987 O TYR A 407 -8.568 -19.726 -32.439 1.00 99.89 O ANISOU 2987 O TYR A 407 12977 15520 9457 3054 4480 1122 O ATOM 2988 CB TYR A 407 -9.328 -17.158 -30.992 1.00 96.02 C ANISOU 2988 CB TYR A 407 12156 14773 9556 2563 4474 1623 C ATOM 2989 CG TYR A 407 -8.896 -15.785 -30.549 1.00105.75 C ANISOU 2989 CG TYR A 407 13133 15778 11269 2301 4723 1972 C ATOM 2990 CD1 TYR A 407 -9.824 -14.761 -30.384 1.00103.75 C ANISOU 2990 CD1 TYR A 407 13010 15461 10948 2252 4610 2144 C ATOM 2991 CD2 TYR A 407 -7.565 -15.512 -30.266 1.00110.93 C ANISOU 2991 CD2 TYR A 407 13401 16264 12483 2096 5041 2106 C ATOM 2992 CE1 TYR A 407 -9.439 -13.496 -29.962 1.00 99.55 C ANISOU 2992 CE1 TYR A 407 12252 14675 10896 2000 4823 2441 C ATOM 2993 CE2 TYR A 407 -7.168 -14.249 -29.842 1.00112.09 C ANISOU 2993 CE2 TYR A 407 13301 16163 13126 1832 5222 2379 C ATOM 2994 CZ TYR A 407 -8.113 -13.245 -29.691 1.00105.78 C ANISOU 2994 CZ TYR A 407 12659 15277 12254 1782 5117 2545 C ATOM 2995 OH TYR A 407 -7.735 -11.990 -29.266 1.00 99.61 O ANISOU 2995 OH TYR A 407 11647 14210 11989 1517 5282 2792 O ATOM 2996 N TRP A 408 -10.651 -19.301 -33.166 1.00111.36 N ANISOU 2996 N TRP A 408 15022 17122 10166 3307 3981 1043 N ATOM 2997 CA TRP A 408 -11.052 -20.699 -33.280 1.00108.73 C ANISOU 2997 CA TRP A 408 14827 16901 9587 3446 3640 601 C ATOM 2998 C TRP A 408 -11.628 -20.924 -34.668 1.00108.33 C ANISOU 2998 C TRP A 408 15251 16968 8940 3800 3507 523 C ATOM 2999 O TRP A 408 -12.721 -20.433 -34.979 1.00109.18 O ANISOU 2999 O TRP A 408 15595 17133 8757 3900 3219 523 O ATOM 3000 CB TRP A 408 -12.092 -21.072 -32.230 1.00102.49 C ANISOU 3000 CB TRP A 408 13931 16130 8881 3289 3168 306 C ATOM 3001 CG TRP A 408 -11.797 -20.579 -30.867 1.00 97.11 C ANISOU 3001 CG TRP A 408 12823 15322 8753 2942 3216 419 C ATOM 3002 CD1 TRP A 408 -12.209 -19.410 -30.321 1.00 96.89 C ANISOU 3002 CD1 TRP A 408 12677 15172 8964 2716 3157 647 C ATOM 3003 CD2 TRP A 408 -11.036 -21.252 -29.861 1.00 93.31 C ANISOU 3003 CD2 TRP A 408 11967 14718 8767 2710 3200 280 C ATOM 3004 NE1 TRP A 408 -11.749 -19.305 -29.033 1.00 97.43 N ANISOU 3004 NE1 TRP A 408 12331 15056 9632 2356 3098 640 N ATOM 3005 CE2 TRP A 408 -11.026 -20.426 -28.727 1.00 94.77 C ANISOU 3005 CE2 TRP A 408 11833 14724 9452 2353 3113 423 C ATOM 3006 CE3 TRP A 408 -10.357 -22.471 -29.813 1.00 87.96 C ANISOU 3006 CE3 TRP A 408 11211 14061 8148 2797 3242 45 C ATOM 3007 CZ2 TRP A 408 -10.367 -20.779 -27.552 1.00 88.93 C ANISOU 3007 CZ2 TRP A 408 10712 13845 9233 2095 3041 334 C ATOM 3008 CZ3 TRP A 408 -9.705 -22.821 -28.649 1.00 82.96 C ANISOU 3008 CZ3 TRP A 408 10187 13281 8056 2539 3183 -19 C ATOM 3009 CH2 TRP A 408 -9.715 -21.976 -27.534 1.00 86.03 C ANISOU 3009 CH2 TRP A 408 10274 13510 8901 2198 3072 124 C ATOM 3010 N THR A 409 -10.906 -21.669 -35.491 1.00109.49 N ANISOU 3010 N THR A 409 15529 17153 8919 4002 3697 444 N ATOM 3011 CA THR A 409 -11.459 -22.114 -36.753 1.00113.99 C ANISOU 3011 CA THR A 409 16542 17839 8928 4353 3508 284 C ATOM 3012 C THR A 409 -12.677 -22.998 -36.502 1.00106.99 C ANISOU 3012 C THR A 409 15758 17002 7889 4363 2890 -183 C ATOM 3013 O THR A 409 -12.743 -23.715 -35.500 1.00106.70 O ANISOU 3013 O THR A 409 15473 16905 8162 4149 2701 -441 O ATOM 3014 CB THR A 409 -10.389 -22.869 -37.536 1.00122.99 C ANISOU 3014 CB THR A 409 17764 19003 9965 4549 3834 250 C ATOM 3015 OG1 THR A 409 -9.898 -23.952 -36.733 1.00127.03 O ANISOU 3015 OG1 THR A 409 18000 19458 10805 4391 3780 -34 O ATOM 3016 CG2 THR A 409 -9.231 -21.935 -37.843 1.00120.47 C ANISOU 3016 CG2 THR A 409 17325 18620 9828 4535 4444 718 C ATOM 3017 N GLU A 410 -13.652 -22.936 -37.419 1.00101.29 N ANISOU 3017 N GLU A 410 15391 16373 6720 4616 2567 -295 N ATOM 3018 CA GLU A 410 -14.929 -23.641 -37.330 1.00104.05 C ANISOU 3018 CA GLU A 410 15830 16753 6951 4629 1944 -732 C ATOM 3019 C GLU A 410 -15.416 -23.726 -35.879 1.00109.17 C ANISOU 3019 C GLU A 410 16135 17319 8027 4274 1703 -876 C ATOM 3020 O GLU A 410 -15.558 -24.824 -35.331 1.00108.14 O ANISOU 3020 O GLU A 410 15877 17123 8086 4154 1463 -1242 O ATOM 3021 CB GLU A 410 -14.833 -25.031 -37.950 1.00107.02 C ANISOU 3021 CB GLU A 410 16368 17140 7153 4801 1771 -1132 C ATOM 3022 CG GLU A 410 -14.901 -25.052 -39.477 1.00116.68 C ANISOU 3022 CG GLU A 410 18012 18476 7845 5210 1778 -1126 C ATOM 3023 CD GLU A 410 -14.652 -26.451 -40.040 1.00124.05 C ANISOU 3023 CD GLU A 410 19091 19404 8638 5372 1661 -1516 C ATOM 3024 OE1 GLU A 410 -13.944 -27.247 -39.381 1.00121.10 O ANISOU 3024 OE1 GLU A 410 18497 18935 8579 5202 1806 -1644 O ATOM 3025 OE2 GLU A 410 -15.139 -26.751 -41.155 1.00134.51 O ANISOU 3025 OE2 GLU A 410 20754 20814 9540 5688 1430 -1692 O ATOM 3026 N PRO A 411 -15.666 -22.587 -35.225 1.00106.29 N ANISOU 3026 N PRO A 411 15619 16939 7828 4108 1776 -590 N ATOM 3027 CA PRO A 411 -15.881 -22.617 -33.770 1.00 96.47 C ANISOU 3027 CA PRO A 411 14026 15622 7008 3776 1656 -676 C ATOM 3028 C PRO A 411 -17.098 -23.412 -33.349 1.00 95.58 C ANISOU 3028 C PRO A 411 13884 15495 6937 3693 1072 -1129 C ATOM 3029 O PRO A 411 -17.128 -23.898 -32.211 1.00 96.30 O ANISOU 3029 O PRO A 411 13707 15507 7377 3447 976 -1304 O ATOM 3030 CB PRO A 411 -16.029 -21.137 -33.407 1.00 89.42 C ANISOU 3030 CB PRO A 411 13053 14722 6199 3677 1831 -269 C ATOM 3031 CG PRO A 411 -16.561 -20.504 -34.642 1.00 95.35 C ANISOU 3031 CG PRO A 411 14161 15549 6520 3971 1764 -123 C ATOM 3032 CD PRO A 411 -15.922 -21.252 -35.796 1.00107.58 C ANISOU 3032 CD PRO A 411 15953 17143 7780 4239 1913 -208 C ATOM 3033 N GLU A 412 -18.097 -23.572 -34.218 1.00 95.90 N ANISOU 3033 N GLU A 412 14170 15592 6677 3885 679 -1329 N ATOM 3034 CA GLU A 412 -19.314 -24.264 -33.820 1.00102.98 C ANISOU 3034 CA GLU A 412 14977 16437 7715 3766 117 -1753 C ATOM 3035 C GLU A 412 -19.151 -25.772 -33.721 1.00100.32 C ANISOU 3035 C GLU A 412 14597 15990 7531 3714 -34 -2162 C ATOM 3036 O GLU A 412 -19.994 -26.428 -33.099 1.00 99.06 O ANISOU 3036 O GLU A 412 14273 15719 7645 3523 -421 -2495 O ATOM 3037 CB GLU A 412 -20.442 -23.985 -34.805 1.00119.28 C ANISOU 3037 CB GLU A 412 17263 18578 9478 3989 -279 -1857 C ATOM 3038 CG GLU A 412 -20.571 -22.559 -35.251 1.00131.07 C ANISOU 3038 CG GLU A 412 18900 20171 10731 4145 -122 -1446 C ATOM 3039 CD GLU A 412 -21.805 -22.361 -36.104 1.00141.08 C ANISOU 3039 CD GLU A 412 20344 21505 11756 4366 -583 -1600 C ATOM 3040 OE1 GLU A 412 -22.886 -22.827 -35.679 1.00142.66 O ANISOU 3040 OE1 GLU A 412 20363 21652 12189 4224 -1062 -1944 O ATOM 3041 OE2 GLU A 412 -21.692 -21.761 -37.197 1.00146.40 O ANISOU 3041 OE2 GLU A 412 21318 22269 12038 4684 -461 -1382 O ATOM 3042 N LYS A 413 -18.118 -26.346 -34.324 1.00 96.70 N ANISOU 3042 N LYS A 413 14274 15535 6933 3873 264 -2143 N ATOM 3043 CA LYS A 413 -18.046 -27.797 -34.385 1.00100.17 C ANISOU 3043 CA LYS A 413 14723 15854 7482 3868 90 -2543 C ATOM 3044 C LYS A 413 -17.228 -28.342 -33.222 1.00 95.38 C ANISOU 3044 C LYS A 413 13845 15117 7277 3642 320 -2556 C ATOM 3045 O LYS A 413 -16.269 -27.724 -32.746 1.00 79.71 O ANISOU 3045 O LYS A 413 11719 13168 5399 3586 742 -2228 O ATOM 3046 CB LYS A 413 -17.471 -28.270 -35.720 1.00108.60 C ANISOU 3046 CB LYS A 413 16106 16991 8168 4197 230 -2581 C ATOM 3047 CG LYS A 413 -18.366 -29.292 -36.420 1.00119.20 C ANISOU 3047 CG LYS A 413 17611 18280 9401 4312 -256 -3038 C ATOM 3048 CD LYS A 413 -18.508 -30.586 -35.608 1.00117.61 C ANISOU 3048 CD LYS A 413 17214 17856 9618 4079 -462 -3415 C ATOM 3049 CE LYS A 413 -19.799 -31.325 -35.951 1.00117.39 C ANISOU 3049 CE LYS A 413 17215 17729 9659 4060 -1034 -3849 C ATOM 3050 NZ LYS A 413 -20.930 -30.897 -35.065 1.00109.85 N ANISOU 3050 NZ LYS A 413 15991 16707 9041 3781 -1354 -3897 N ATOM 3051 N PHE A 414 -17.653 -29.499 -32.744 1.00101.87 N ANISOU 3051 N PHE A 414 14576 15765 8366 3506 26 -2937 N ATOM 3052 CA PHE A 414 -16.936 -30.224 -31.710 1.00 97.23 C ANISOU 3052 CA PHE A 414 13768 15020 8154 3336 192 -3002 C ATOM 3053 C PHE A 414 -15.712 -30.862 -32.365 1.00 96.48 C ANISOU 3053 C PHE A 414 13801 14928 7930 3550 528 -2974 C ATOM 3054 O PHE A 414 -15.808 -31.916 -32.997 1.00 95.66 O ANISOU 3054 O PHE A 414 13867 14737 7744 3672 368 -3272 O ATOM 3055 CB PHE A 414 -17.875 -31.242 -31.070 1.00 91.49 C ANISOU 3055 CB PHE A 414 12929 14065 7767 3129 -227 -3400 C ATOM 3056 CG PHE A 414 -17.244 -32.079 -30.009 1.00 89.32 C ANISOU 3056 CG PHE A 414 12462 13589 7885 2977 -95 -3484 C ATOM 3057 CD1 PHE A 414 -17.123 -31.605 -28.721 1.00 85.73 C ANISOU 3057 CD1 PHE A 414 11703 13023 7847 2665 4 -3210 C ATOM 3058 CD2 PHE A 414 -16.795 -33.358 -30.295 1.00 89.53 C ANISOU 3058 CD2 PHE A 414 12585 13449 7984 3068 -88 -3720 C ATOM 3059 CE1 PHE A 414 -16.550 -32.386 -27.734 1.00 83.36 C ANISOU 3059 CE1 PHE A 414 11227 12493 7953 2507 100 -3206 C ATOM 3060 CE2 PHE A 414 -16.228 -34.142 -29.318 1.00 86.34 C ANISOU 3060 CE2 PHE A 414 12019 12837 7950 2957 23 -3782 C ATOM 3061 CZ PHE A 414 -16.106 -33.652 -28.029 1.00 83.80 C ANISOU 3061 CZ PHE A 414 11402 12421 8018 2663 112 -3489 C ATOM 3062 N LEU A 415 -14.559 -30.200 -32.237 1.00 93.27 N ANISOU 3062 N LEU A 415 13293 14613 7530 3591 1001 -2612 N ATOM 3063 CA LEU A 415 -13.283 -30.664 -32.783 1.00 95.19 C ANISOU 3063 CA LEU A 415 13591 14865 7712 3777 1387 -2530 C ATOM 3064 C LEU A 415 -12.256 -30.714 -31.658 1.00 93.66 C ANISOU 3064 C LEU A 415 13051 14593 7942 3628 1684 -2374 C ATOM 3065 O LEU A 415 -11.592 -29.707 -31.371 1.00 90.75 O ANISOU 3065 O LEU A 415 12494 14311 7677 3569 2017 -2009 O ATOM 3066 CB LEU A 415 -12.808 -29.754 -33.916 1.00 87.60 C ANISOU 3066 CB LEU A 415 12822 14086 6375 3997 1707 -2211 C ATOM 3067 CG LEU A 415 -13.787 -29.612 -35.085 1.00 94.76 C ANISOU 3067 CG LEU A 415 14082 15092 6829 4199 1408 -2334 C ATOM 3068 CD1 LEU A 415 -13.357 -28.515 -36.057 1.00100.92 C ANISOU 3068 CD1 LEU A 415 15045 16038 7262 4408 1750 -1947 C ATOM 3069 CD2 LEU A 415 -13.939 -30.941 -35.816 1.00 98.42 C ANISOU 3069 CD2 LEU A 415 14769 15488 7140 4374 1182 -2739 C ATOM 3070 N PRO A 416 -12.085 -31.867 -31.002 1.00 88.68 N ANISOU 3070 N PRO A 416 12318 13781 7598 3569 1567 -2634 N ATOM 3071 CA PRO A 416 -11.128 -31.948 -29.884 1.00 84.42 C ANISOU 3071 CA PRO A 416 11434 13164 7477 3458 1798 -2495 C ATOM 3072 C PRO A 416 -9.679 -31.733 -30.279 1.00 87.86 C ANISOU 3072 C PRO A 416 11756 13674 7955 3595 2280 -2228 C ATOM 3073 O PRO A 416 -8.849 -31.485 -29.395 1.00 81.89 O ANISOU 3073 O PRO A 416 10657 12892 7566 3494 2480 -2042 O ATOM 3074 CB PRO A 416 -11.341 -33.371 -29.345 1.00 79.76 C ANISOU 3074 CB PRO A 416 10851 12334 7122 3427 1543 -2856 C ATOM 3075 CG PRO A 416 -12.734 -33.707 -29.736 1.00 83.32 C ANISOU 3075 CG PRO A 416 11535 12721 7404 3377 1111 -3157 C ATOM 3076 CD PRO A 416 -12.936 -33.066 -31.083 1.00 86.61 C ANISOU 3076 CD PRO A 416 12212 13342 7356 3558 1158 -3065 C ATOM 3077 N GLU A 417 -9.347 -31.817 -31.571 1.00 93.84 N ANISOU 3077 N GLU A 417 12766 14517 8371 3821 2462 -2211 N ATOM 3078 CA GLU A 417 -7.959 -31.677 -31.990 1.00 95.38 C ANISOU 3078 CA GLU A 417 12835 14764 8640 3945 2940 -1980 C ATOM 3079 C GLU A 417 -7.361 -30.327 -31.602 1.00 97.66 C ANISOU 3079 C GLU A 417 12827 15137 9141 3797 3261 -1555 C ATOM 3080 O GLU A 417 -6.137 -30.227 -31.451 1.00101.01 O ANISOU 3080 O GLU A 417 12972 15548 9858 3796 3615 -1373 O ATOM 3081 CB GLU A 417 -7.843 -31.899 -33.498 1.00112.36 C ANISOU 3081 CB GLU A 417 15347 17009 10335 4224 3072 -2029 C ATOM 3082 CG GLU A 417 -7.787 -33.362 -33.882 1.00119.39 C ANISOU 3082 CG GLU A 417 16424 17787 11154 4395 2929 -2409 C ATOM 3083 CD GLU A 417 -6.775 -34.146 -33.058 1.00122.08 C ANISOU 3083 CD GLU A 417 16462 17982 11942 4364 3087 -2454 C ATOM 3084 OE1 GLU A 417 -5.588 -33.753 -33.018 1.00124.58 O ANISOU 3084 OE1 GLU A 417 16522 18352 12459 4389 3499 -2193 O ATOM 3085 OE2 GLU A 417 -7.173 -35.159 -32.444 1.00123.58 O ANISOU 3085 OE2 GLU A 417 16656 17987 12310 4314 2788 -2747 O ATOM 3086 N ARG A 418 -8.191 -29.282 -31.438 1.00 93.38 N ANISOU 3086 N ARG A 418 12318 14663 8498 3665 3135 -1402 N ATOM 3087 CA ARG A 418 -7.673 -27.966 -31.064 1.00 94.77 C ANISOU 3087 CA ARG A 418 12217 14878 8912 3502 3428 -1001 C ATOM 3088 C ARG A 418 -6.834 -28.041 -29.797 1.00 91.04 C ANISOU 3088 C ARG A 418 11271 14311 9010 3315 3511 -937 C ATOM 3089 O ARG A 418 -5.882 -27.269 -29.618 1.00 95.34 O ANISOU 3089 O ARG A 418 11509 14845 9872 3210 3835 -644 O ATOM 3090 CB ARG A 418 -8.810 -26.968 -30.822 1.00101.96 C ANISOU 3090 CB ARG A 418 13211 15842 9688 3369 3208 -898 C ATOM 3091 CG ARG A 418 -10.019 -27.063 -31.704 1.00101.00 C ANISOU 3091 CG ARG A 418 13517 15795 9062 3521 2901 -1073 C ATOM 3092 CD ARG A 418 -11.177 -26.290 -31.052 1.00 88.51 C ANISOU 3092 CD ARG A 418 11909 14236 7484 3347 2602 -1047 C ATOM 3093 NE ARG A 418 -12.400 -26.421 -31.835 1.00 91.74 N ANISOU 3093 NE ARG A 418 12680 14709 7470 3484 2234 -1252 N ATOM 3094 CZ ARG A 418 -12.675 -25.682 -32.904 1.00 93.48 C ANISOU 3094 CZ ARG A 418 13171 15029 7318 3659 2300 -1068 C ATOM 3095 NH1 ARG A 418 -11.816 -24.751 -33.305 1.00 93.89 N ANISOU 3095 NH1 ARG A 418 13187 15109 7377 3698 2756 -662 N ATOM 3096 NH2 ARG A 418 -13.808 -25.870 -33.564 1.00 92.77 N ANISOU 3096 NH2 ARG A 418 13369 14993 6887 3792 1901 -1289 N ATOM 3097 N PHE A 419 -7.205 -28.931 -28.881 1.00 81.77 N ANISOU 3097 N PHE A 419 10022 13050 7999 3265 3190 -1211 N ATOM 3098 CA PHE A 419 -6.512 -29.068 -27.613 1.00 77.15 C ANISOU 3098 CA PHE A 419 9019 12342 7954 3077 3149 -1164 C ATOM 3099 C PHE A 419 -5.492 -30.183 -27.632 1.00 85.20 C ANISOU 3099 C PHE A 419 9925 13312 9134 3276 3298 -1307 C ATOM 3100 O PHE A 419 -5.058 -30.622 -26.564 1.00 88.28 O ANISOU 3100 O PHE A 419 10040 13572 9931 3165 3147 -1349 O ATOM 3101 CB PHE A 419 -7.516 -29.297 -26.479 1.00 76.26 C ANISOU 3101 CB PHE A 419 8900 12057 8017 2794 2641 -1307 C ATOM 3102 CG PHE A 419 -8.425 -28.148 -26.255 1.00 74.72 C ANISOU 3102 CG PHE A 419 8739 11878 7774 2564 2487 -1149 C ATOM 3103 CD1 PHE A 419 -8.045 -27.098 -25.440 1.00 76.87 C ANISOU 3103 CD1 PHE A 419 8702 12105 8399 2318 2534 -892 C ATOM 3104 CD2 PHE A 419 -9.657 -28.097 -26.874 1.00 78.88 C ANISOU 3104 CD2 PHE A 419 9597 12457 7916 2608 2278 -1275 C ATOM 3105 CE1 PHE A 419 -8.884 -26.020 -25.248 1.00 74.65 C ANISOU 3105 CE1 PHE A 419 8467 11821 8077 2126 2405 -752 C ATOM 3106 CE2 PHE A 419 -10.498 -27.021 -26.685 1.00 75.08 C ANISOU 3106 CE2 PHE A 419 9137 11990 7400 2425 2140 -1124 C ATOM 3107 CZ PHE A 419 -10.108 -25.985 -25.872 1.00 76.06 C ANISOU 3107 CZ PHE A 419 8974 12058 7868 2187 2220 -857 C ATOM 3108 N SER A 420 -5.113 -30.661 -28.818 1.00 93.13 N ANISOU 3108 N SER A 420 11167 14344 9874 3489 3504 -1367 N ATOM 3109 CA SER A 420 -4.008 -31.596 -28.918 1.00100.94 C ANISOU 3109 CA SER A 420 12025 15263 11065 3643 3681 -1458 C ATOM 3110 C SER A 420 -2.718 -30.915 -28.495 1.00110.93 C ANISOU 3110 C SER A 420 12810 16541 12799 3540 3991 -1181 C ATOM 3111 O SER A 420 -2.557 -29.698 -28.628 1.00112.21 O ANISOU 3111 O SER A 420 12834 16772 13029 3394 4184 -900 O ATOM 3112 CB SER A 420 -3.862 -32.113 -30.344 1.00108.86 C ANISOU 3112 CB SER A 420 13379 16319 11664 3895 3865 -1564 C ATOM 3113 OG SER A 420 -3.431 -31.073 -31.206 1.00118.26 O ANISOU 3113 OG SER A 420 14577 17643 12713 3911 4225 -1270 O ATOM 3114 N LYS A 421 -1.781 -31.726 -27.997 1.00121.16 N ANISOU 3114 N LYS A 421 13842 17748 14447 3618 4020 -1274 N ATOM 3115 CA LYS A 421 -0.516 -31.194 -27.501 1.00128.36 C ANISOU 3115 CA LYS A 421 14237 18658 15875 3516 4234 -1073 C ATOM 3116 C LYS A 421 0.229 -30.394 -28.565 1.00129.68 C ANISOU 3116 C LYS A 421 14349 18931 15993 3527 4678 -845 C ATOM 3117 O LYS A 421 1.011 -29.498 -28.231 1.00129.54 O ANISOU 3117 O LYS A 421 13925 18921 16373 3351 4841 -625 O ATOM 3118 CB LYS A 421 0.355 -32.337 -26.985 1.00135.32 C ANISOU 3118 CB LYS A 421 14899 19436 17079 3666 4178 -1244 C ATOM 3119 CG LYS A 421 0.589 -32.326 -25.478 1.00131.76 C ANISOU 3119 CG LYS A 421 14063 18897 17103 3537 3883 -1230 C ATOM 3120 CD LYS A 421 1.263 -33.620 -25.034 1.00131.77 C ANISOU 3120 CD LYS A 421 13958 18774 17333 3747 3776 -1419 C ATOM 3121 CE LYS A 421 2.391 -34.024 -25.991 1.00132.83 C ANISOU 3121 CE LYS A 421 13996 18950 17523 3934 4144 -1446 C ATOM 3122 NZ LYS A 421 2.816 -35.429 -25.776 1.00130.10 N ANISOU 3122 NZ LYS A 421 13682 18463 17288 4182 4046 -1664 N ATOM 3123 N LYS A 422 0.000 -30.695 -29.844 1.00129.86 N ANISOU 3123 N LYS A 422 14779 19026 15537 3734 4861 -897 N ATOM 3124 CA LYS A 422 0.611 -29.896 -30.901 1.00130.10 C ANISOU 3124 CA LYS A 422 14818 19156 15457 3773 5295 -646 C ATOM 3125 C LYS A 422 -0.038 -28.522 -31.013 1.00132.47 C ANISOU 3125 C LYS A 422 15201 19495 15636 3581 5325 -374 C ATOM 3126 O LYS A 422 0.647 -27.522 -31.263 1.00134.78 O ANISOU 3126 O LYS A 422 15272 19799 16139 3472 5643 -82 O ATOM 3127 CB LYS A 422 0.513 -30.624 -32.236 1.00128.59 C ANISOU 3127 CB LYS A 422 15076 19035 14746 4085 5455 -780 C ATOM 3128 CG LYS A 422 0.865 -29.739 -33.410 1.00131.09 C ANISOU 3128 CG LYS A 422 15526 19460 14821 4162 5877 -495 C ATOM 3129 CD LYS A 422 -0.123 -29.908 -34.531 1.00136.32 C ANISOU 3129 CD LYS A 422 16793 20206 14796 4380 5800 -581 C ATOM 3130 CE LYS A 422 0.142 -28.896 -35.626 1.00146.56 C ANISOU 3130 CE LYS A 422 18249 21597 15842 4467 6205 -244 C ATOM 3131 NZ LYS A 422 -0.706 -29.145 -36.818 1.00152.78 N ANISOU 3131 NZ LYS A 422 19635 22482 15934 4746 6121 -344 N ATOM 3132 N ASN A 423 -1.357 -28.448 -30.833 1.00131.42 N ANISOU 3132 N ASN A 423 15379 19367 15188 3541 4994 -465 N ATOM 3133 CA ASN A 423 -2.092 -27.226 -31.117 1.00130.50 C ANISOU 3133 CA ASN A 423 15425 19293 14865 3421 5014 -227 C ATOM 3134 C ASN A 423 -2.366 -26.377 -29.889 1.00127.15 C ANISOU 3134 C ASN A 423 14680 18795 14835 3110 4828 -104 C ATOM 3135 O ASN A 423 -2.850 -25.252 -30.038 1.00118.88 O ANISOU 3135 O ASN A 423 13707 17755 13706 2987 4876 125 O ATOM 3136 CB ASN A 423 -3.418 -27.554 -31.808 1.00129.36 C ANISOU 3136 CB ASN A 423 15829 19221 14102 3588 4754 -400 C ATOM 3137 CG ASN A 423 -3.220 -28.042 -33.226 1.00140.46 C ANISOU 3137 CG ASN A 423 17604 20712 15052 3897 4960 -455 C ATOM 3138 OD1 ASN A 423 -2.219 -27.719 -33.870 1.00146.36 O ANISOU 3138 OD1 ASN A 423 18255 21489 15867 3976 5383 -246 O ATOM 3139 ND2 ASN A 423 -4.173 -28.822 -33.724 1.00141.72 N ANISOU 3139 ND2 ASN A 423 18182 20905 14758 4074 4651 -746 N ATOM 3140 N LYS A 424 -2.062 -26.870 -28.689 1.00135.97 N ANISOU 3140 N LYS A 424 15455 19834 16375 2998 4611 -243 N ATOM 3141 CA LYS A 424 -2.396 -26.117 -27.484 1.00138.99 C ANISOU 3141 CA LYS A 424 15559 20149 17100 2722 4387 -153 C ATOM 3142 C LYS A 424 -1.530 -24.874 -27.304 1.00128.99 C ANISOU 3142 C LYS A 424 13906 18819 16285 2488 4631 141 C ATOM 3143 O LYS A 424 -1.889 -23.999 -26.504 1.00127.91 O ANISOU 3143 O LYS A 424 13599 18613 16388 2244 4476 251 O ATOM 3144 CB LYS A 424 -2.293 -27.029 -26.253 1.00148.26 C ANISOU 3144 CB LYS A 424 16501 21257 18576 2709 4061 -378 C ATOM 3145 CG LYS A 424 -1.002 -27.844 -26.172 1.00155.02 C ANISOU 3145 CG LYS A 424 17072 22072 19757 2826 4186 -469 C ATOM 3146 CD LYS A 424 -0.855 -28.590 -24.839 1.00151.36 C ANISOU 3146 CD LYS A 424 16355 21523 19632 2816 3838 -637 C ATOM 3147 CE LYS A 424 -1.926 -29.655 -24.639 1.00146.48 C ANISOU 3147 CE LYS A 424 16128 20868 18661 2934 3496 -901 C ATOM 3148 NZ LYS A 424 -1.546 -30.593 -23.547 1.00144.44 N ANISOU 3148 NZ LYS A 424 15700 20469 18713 2948 3183 -1061 N ATOM 3149 N ASP A 425 -0.422 -24.761 -28.040 1.00115.99 N ANISOU 3149 N ASP A 425 12124 17181 14764 2553 5003 264 N ATOM 3150 CA ASP A 425 0.464 -23.607 -27.905 1.00113.08 C ANISOU 3150 CA ASP A 425 11377 16727 14862 2324 5232 528 C ATOM 3151 C ASP A 425 -0.148 -22.325 -28.456 1.00103.38 C ANISOU 3151 C ASP A 425 10371 15464 13445 2218 5392 811 C ATOM 3152 O ASP A 425 0.284 -21.230 -28.078 1.00100.18 O ANISOU 3152 O ASP A 425 9672 14931 13461 1965 5476 1014 O ATOM 3153 CB ASP A 425 1.784 -23.895 -28.616 1.00131.08 C ANISOU 3153 CB ASP A 425 13469 19033 17303 2454 5611 584 C ATOM 3154 CG ASP A 425 2.615 -24.926 -27.878 1.00143.12 C ANISOU 3154 CG ASP A 425 15015 20628 18739 2704 5526 295 C ATOM 3155 OD1 ASP A 425 2.297 -25.190 -26.691 1.00148.72 O ANISOU 3155 OD1 ASP A 425 15720 21316 19472 2707 5139 64 O ATOM 3156 OD2 ASP A 425 3.565 -25.485 -28.470 1.00146.17 O ANISOU 3156 OD2 ASP A 425 15436 21073 19029 2908 5850 304 O ATOM 3157 N ASN A 426 -1.127 -22.430 -29.345 1.00 96.99 N ANISOU 3157 N ASN A 426 10079 14752 12023 2415 5413 821 N ATOM 3158 CA AASN A 426 -1.786 -21.260 -29.895 0.34103.70 C ANISOU 3158 CA AASN A 426 11182 15573 12644 2365 5532 1092 C ATOM 3159 CA BASN A 426 -1.796 -21.260 -29.895 0.66103.79 C ANISOU 3159 CA BASN A 426 11196 15585 12653 2366 5530 1091 C ATOM 3160 C ASN A 426 -3.090 -20.940 -29.172 1.00108.68 C ANISOU 3160 C ASN A 426 11949 16199 13147 2247 5151 1026 C ATOM 3161 O ASN A 426 -3.855 -20.096 -29.643 1.00119.76 O ANISOU 3161 O ASN A 426 13630 17600 14273 2257 5185 1211 O ATOM 3162 CB AASN A 426 -2.031 -21.442 -31.396 0.34107.20 C ANISOU 3162 CB AASN A 426 12119 16134 12477 2686 5777 1170 C ATOM 3163 CB BASN A 426 -2.053 -21.466 -31.394 0.66107.33 C ANISOU 3163 CB BASN A 426 12142 16153 12484 2690 5768 1163 C ATOM 3164 CG AASN A 426 -2.786 -22.714 -31.719 0.34104.91 C ANISOU 3164 CG AASN A 426 12199 15986 11675 2948 5506 838 C ATOM 3165 CG BASN A 426 -0.773 -21.596 -32.193 0.66114.54 C ANISOU 3165 CG BASN A 426 12937 17068 13516 2814 6217 1290 C ATOM 3166 OD1AASN A 426 -3.798 -23.018 -31.091 0.34 99.29 O ANISOU 3166 OD1AASN A 426 11594 15296 10834 2905 5111 641 O ATOM 3167 OD1BASN A 426 0.284 -21.131 -31.770 0.66121.09 O ANISOU 3167 OD1BASN A 426 13315 17785 14910 2620 6416 1423 O ATOM 3168 ND2AASN A 426 -2.298 -23.467 -32.695 0.34110.99 N ANISOU 3168 ND2AASN A 426 13164 16838 12168 3220 5712 763 N ATOM 3169 ND2BASN A 426 -0.866 -22.230 -33.353 0.66119.95 N ANISOU 3169 ND2BASN A 426 14022 17878 13675 3143 6363 1236 N ATOM 3170 N ILE A 427 -3.341 -21.593 -28.040 1.00104.74 N ANISOU 3170 N ILE A 427 11258 15694 12846 2157 4798 779 N ATOM 3171 CA ILE A 427 -4.555 -21.434 -27.251 1.00 97.00 C ANISOU 3171 CA ILE A 427 10372 14721 11763 2059 4430 690 C ATOM 3172 C ILE A 427 -4.265 -20.439 -26.136 1.00 92.00 C ANISOU 3172 C ILE A 427 9322 13923 11711 1723 4353 821 C ATOM 3173 O ILE A 427 -3.458 -20.711 -25.239 1.00 85.81 O ANISOU 3173 O ILE A 427 8133 13059 11412 1590 4248 722 O ATOM 3174 CB ILE A 427 -5.040 -22.781 -26.693 1.00 91.55 C ANISOU 3174 CB ILE A 427 9761 14094 10928 2168 4061 335 C ATOM 3175 CG1 ILE A 427 -5.747 -23.568 -27.797 1.00 90.06 C ANISOU 3175 CG1 ILE A 427 10067 14055 10098 2484 4049 174 C ATOM 3176 CG2 ILE A 427 -5.959 -22.586 -25.492 1.00 85.37 C ANISOU 3176 CG2 ILE A 427 8963 13183 10289 1884 3526 205 C ATOM 3177 CD1 ILE A 427 -6.279 -24.889 -27.349 1.00 84.99 C ANISOU 3177 CD1 ILE A 427 9553 13395 9346 2538 3636 -200 C ATOM 3178 N ASP A 428 -4.935 -19.291 -26.179 1.00 85.58 N ANISOU 3178 N ASP A 428 8619 13048 10852 1596 4368 1024 N ATOM 3179 CA ASP A 428 -4.596 -18.191 -25.292 1.00 84.33 C ANISOU 3179 CA ASP A 428 8099 12686 11255 1269 4327 1157 C ATOM 3180 C ASP A 428 -5.329 -18.346 -23.966 1.00 76.39 C ANISOU 3180 C ASP A 428 7068 11594 10365 1058 3731 904 C ATOM 3181 O ASP A 428 -6.564 -18.228 -23.932 1.00 80.57 O ANISOU 3181 O ASP A 428 7929 12141 10545 1057 3458 844 O ATOM 3182 CB ASP A 428 -4.954 -16.861 -25.937 1.00 93.00 C ANISOU 3182 CB ASP A 428 9384 13686 12264 1206 4550 1466 C ATOM 3183 CG ASP A 428 -4.446 -15.665 -25.138 1.00 99.04 C ANISOU 3183 CG ASP A 428 9781 14192 13658 862 4538 1592 C ATOM 3184 OD1 ASP A 428 -4.640 -15.635 -23.902 1.00 97.72 O ANISOU 3184 OD1 ASP A 428 9372 13946 13813 662 4191 1425 O ATOM 3185 OD2 ASP A 428 -3.853 -14.743 -25.750 1.00101.94 O ANISOU 3185 OD2 ASP A 428 10119 14416 14199 798 4857 1847 O ATOM 3186 N PRO A 429 -4.616 -18.556 -22.854 1.00 72.54 N ANISOU 3186 N PRO A 429 6196 11008 10359 891 3516 758 N ATOM 3187 CA PRO A 429 -5.292 -18.784 -21.561 1.00 74.05 C ANISOU 3187 CA PRO A 429 6413 11124 10600 735 2966 520 C ATOM 3188 C PRO A 429 -6.228 -17.661 -21.136 1.00 77.81 C ANISOU 3188 C PRO A 429 7019 11477 11069 539 2783 594 C ATOM 3189 O PRO A 429 -6.942 -17.828 -20.139 1.00 81.02 O ANISOU 3189 O PRO A 429 7509 11833 11441 440 2366 412 O ATOM 3190 CB PRO A 429 -4.127 -18.943 -20.577 1.00 80.00 C ANISOU 3190 CB PRO A 429 6700 11790 11907 620 2844 413 C ATOM 3191 CG PRO A 429 -2.886 -18.499 -21.338 1.00 83.07 C ANISOU 3191 CG PRO A 429 6748 12170 12645 642 3350 626 C ATOM 3192 CD PRO A 429 -3.164 -18.764 -22.768 1.00 78.41 C ANISOU 3192 CD PRO A 429 6484 11731 11578 892 3760 782 C ATOM 3193 N TYR A 430 -6.261 -16.540 -21.861 1.00 70.10 N ANISOU 3193 N TYR A 430 6081 10442 10114 500 3103 867 N ATOM 3194 CA TYR A 430 -7.167 -15.439 -21.563 1.00 69.27 C ANISOU 3194 CA TYR A 430 6121 10206 9993 348 2960 954 C ATOM 3195 C TYR A 430 -8.352 -15.368 -22.522 1.00 68.91 C ANISOU 3195 C TYR A 430 6528 10277 9380 535 3007 1050 C ATOM 3196 O TYR A 430 -9.293 -14.619 -22.258 1.00 70.04 O ANISOU 3196 O TYR A 430 6828 10335 9448 452 2829 1085 O ATOM 3197 CB TYR A 430 -6.385 -14.113 -21.539 1.00 80.81 C ANISOU 3197 CB TYR A 430 7285 11453 11965 149 3239 1190 C ATOM 3198 CG TYR A 430 -5.276 -14.172 -20.513 1.00 85.82 C ANISOU 3198 CG TYR A 430 7445 11972 13192 -38 3096 1036 C ATOM 3199 CD1 TYR A 430 -3.954 -14.390 -20.890 1.00 93.36 C ANISOU 3199 CD1 TYR A 430 8033 12935 14504 -16 3429 1113 C ATOM 3200 CD2 TYR A 430 -5.565 -14.073 -19.160 1.00 87.56 C ANISOU 3200 CD2 TYR A 430 7587 12089 13591 -205 2611 795 C ATOM 3201 CE1 TYR A 430 -2.947 -14.480 -19.939 1.00 95.35 C ANISOU 3201 CE1 TYR A 430 7862 13091 15276 -166 3204 928 C ATOM 3202 CE2 TYR A 430 -4.576 -14.159 -18.208 1.00 91.08 C ANISOU 3202 CE2 TYR A 430 7626 12446 14532 -335 2414 624 C ATOM 3203 CZ TYR A 430 -3.269 -14.368 -18.597 1.00 95.49 C ANISOU 3203 CZ TYR A 430 7793 13015 15472 -318 2704 688 C ATOM 3204 OH TYR A 430 -2.298 -14.450 -17.628 1.00 93.74 O ANISOU 3204 OH TYR A 430 7205 12712 15700 -429 2413 482 O ATOM 3205 N ILE A 431 -8.343 -16.159 -23.597 1.00 77.27 N ANISOU 3205 N ILE A 431 7798 11528 10032 804 3207 1064 N ATOM 3206 CA ILE A 431 -9.526 -16.390 -24.431 1.00 72.12 C ANISOU 3206 CA ILE A 431 7585 11022 8796 1021 3121 1047 C ATOM 3207 C ILE A 431 -10.343 -17.578 -23.923 1.00 63.93 C ANISOU 3207 C ILE A 431 6679 10069 7541 1057 2681 700 C ATOM 3208 O ILE A 431 -11.571 -17.517 -23.789 1.00 59.48 O ANISOU 3208 O ILE A 431 6328 9517 6753 1054 2385 605 O ATOM 3209 CB ILE A 431 -9.098 -16.614 -25.895 1.00 73.41 C ANISOU 3209 CB ILE A 431 7949 11347 8598 1326 3557 1220 C ATOM 3210 CG1 ILE A 431 -8.212 -15.470 -26.390 1.00 81.30 C ANISOU 3210 CG1 ILE A 431 8796 12232 9863 1284 4074 1605 C ATOM 3211 CG2 ILE A 431 -10.321 -16.778 -26.789 1.00 69.90 C ANISOU 3211 CG2 ILE A 431 7968 11059 7531 1578 3415 1182 C ATOM 3212 CD1 ILE A 431 -8.903 -14.139 -26.372 1.00 76.47 C ANISOU 3212 CD1 ILE A 431 8304 11472 9280 1179 4064 1832 C ATOM 3213 N TYR A 432 -9.676 -18.696 -23.672 1.00 68.45 N ANISOU 3213 N TYR A 432 7120 10688 8198 1104 2653 516 N ATOM 3214 CA TYR A 432 -10.317 -19.896 -23.148 1.00 71.13 C ANISOU 3214 CA TYR A 432 7564 11060 8401 1129 2284 205 C ATOM 3215 C TYR A 432 -10.301 -19.791 -21.629 1.00 71.67 C ANISOU 3215 C TYR A 432 7406 10974 8853 877 1991 106 C ATOM 3216 O TYR A 432 -9.249 -19.953 -21.005 1.00 74.96 O ANISOU 3216 O TYR A 432 7535 11330 9615 806 2028 90 O ATOM 3217 CB TYR A 432 -9.589 -21.139 -23.646 1.00 71.39 C ANISOU 3217 CB TYR A 432 7600 11193 8332 1334 2416 69 C ATOM 3218 CG TYR A 432 -10.158 -22.460 -23.183 1.00 71.44 C ANISOU 3218 CG TYR A 432 7720 11191 8233 1371 2082 -242 C ATOM 3219 CD1 TYR A 432 -9.480 -23.237 -22.249 1.00 66.23 C ANISOU 3219 CD1 TYR A 432 6848 10448 7869 1314 1970 -370 C ATOM 3220 CD2 TYR A 432 -11.351 -22.953 -23.704 1.00 72.80 C ANISOU 3220 CD2 TYR A 432 8207 11424 8030 1476 1879 -407 C ATOM 3221 CE1 TYR A 432 -9.993 -24.459 -21.823 1.00 60.69 C ANISOU 3221 CE1 TYR A 432 6269 9699 7091 1353 1703 -621 C ATOM 3222 CE2 TYR A 432 -11.863 -24.180 -23.291 1.00 70.08 C ANISOU 3222 CE2 TYR A 432 7946 11026 7656 1488 1603 -687 C ATOM 3223 CZ TYR A 432 -11.177 -24.922 -22.355 1.00 62.24 C ANISOU 3223 CZ TYR A 432 6764 9928 6958 1424 1541 -775 C ATOM 3224 OH TYR A 432 -11.654 -26.129 -21.926 1.00 68.50 O ANISOU 3224 OH TYR A 432 7652 10629 7747 1438 1307 -1016 O ATOM 3225 N THR A 433 -11.459 -19.472 -21.033 1.00 69.85 N ANISOU 3225 N THR A 433 7301 10682 8558 763 1702 40 N ATOM 3226 CA THR A 433 -11.488 -19.298 -19.581 1.00 66.89 C ANISOU 3226 CA THR A 433 6763 10164 8487 558 1444 -44 C ATOM 3227 C THR A 433 -12.665 -20.001 -18.924 1.00 56.73 C ANISOU 3227 C THR A 433 5648 8855 7051 535 1125 -242 C ATOM 3228 O THR A 433 -13.382 -19.366 -18.133 1.00 52.26 O ANISOU 3228 O THR A 433 5099 8197 6560 399 954 -242 O ATOM 3229 CB THR A 433 -11.556 -17.818 -19.190 1.00 64.64 C ANISOU 3229 CB THR A 433 6382 9757 8422 384 1468 120 C ATOM 3230 OG1 THR A 433 -12.700 -17.219 -19.798 1.00 64.06 O ANISOU 3230 OG1 THR A 433 6547 9712 8082 428 1460 204 O ATOM 3231 CG2 THR A 433 -10.307 -17.082 -19.625 1.00 68.82 C ANISOU 3231 CG2 THR A 433 6671 10244 9233 350 1792 319 C ATOM 3232 N PRO A 434 -12.862 -21.302 -19.162 1.00 53.84 N ANISOU 3232 N PRO A 434 5397 8543 6516 658 1054 -414 N ATOM 3233 CA PRO A 434 -14.013 -21.980 -18.543 1.00 53.91 C ANISOU 3233 CA PRO A 434 5545 8493 6445 614 790 -585 C ATOM 3234 C PRO A 434 -14.020 -21.901 -17.028 1.00 50.76 C ANISOU 3234 C PRO A 434 5051 7959 6278 465 614 -615 C ATOM 3235 O PRO A 434 -15.095 -21.982 -16.437 1.00 51.60 O ANISOU 3235 O PRO A 434 5259 7999 6347 394 454 -682 O ATOM 3236 CB PRO A 434 -13.865 -23.427 -19.028 1.00 53.52 C ANISOU 3236 CB PRO A 434 5588 8478 6268 767 788 -760 C ATOM 3237 CG PRO A 434 -12.393 -23.593 -19.218 1.00 59.36 C ANISOU 3237 CG PRO A 434 6161 9256 7138 853 991 -696 C ATOM 3238 CD PRO A 434 -11.916 -22.269 -19.758 1.00 57.62 C ANISOU 3238 CD PRO A 434 5838 9094 6960 824 1213 -472 C ATOM 3239 N PHE A 435 -12.853 -21.763 -16.384 1.00 52.78 N ANISOU 3239 N PHE A 435 5112 8173 6768 434 637 -576 N ATOM 3240 CA PHE A 435 -12.734 -21.615 -14.935 1.00 49.05 C ANISOU 3240 CA PHE A 435 4573 7587 6478 335 443 -613 C ATOM 3241 C PHE A 435 -12.229 -20.220 -14.534 1.00 49.49 C ANISOU 3241 C PHE A 435 4457 7592 6755 208 450 -510 C ATOM 3242 O PHE A 435 -11.811 -20.025 -13.383 1.00 51.83 O ANISOU 3242 O PHE A 435 4665 7806 7222 153 278 -562 O ATOM 3243 CB PHE A 435 -11.800 -22.709 -14.363 1.00 45.75 C ANISOU 3243 CB PHE A 435 4074 7145 6165 433 375 -702 C ATOM 3244 CG PHE A 435 -12.304 -24.119 -14.602 1.00 44.56 C ANISOU 3244 CG PHE A 435 4104 6981 5846 546 357 -816 C ATOM 3245 CD1 PHE A 435 -13.238 -24.703 -13.739 1.00 44.07 C ANISOU 3245 CD1 PHE A 435 4213 6809 5722 515 208 -884 C ATOM 3246 CD2 PHE A 435 -11.869 -24.849 -15.702 1.00 48.53 C ANISOU 3246 CD2 PHE A 435 4612 7562 6267 687 511 -857 C ATOM 3247 CE1 PHE A 435 -13.716 -25.984 -13.964 1.00 49.17 C ANISOU 3247 CE1 PHE A 435 5007 7394 6280 592 205 -989 C ATOM 3248 CE2 PHE A 435 -12.343 -26.152 -15.945 1.00 51.81 C ANISOU 3248 CE2 PHE A 435 5199 7929 6558 786 479 -996 C ATOM 3249 CZ PHE A 435 -13.244 -26.721 -15.073 1.00 50.22 C ANISOU 3249 CZ PHE A 435 5140 7590 6352 725 322 -1061 C ATOM 3250 N GLY A 436 -12.267 -19.235 -15.451 1.00 53.18 N ANISOU 3250 N GLY A 436 4894 8091 7221 173 635 -368 N ATOM 3251 CA GLY A 436 -11.681 -17.940 -15.108 1.00 55.32 C ANISOU 3251 CA GLY A 436 4980 8266 7773 38 665 -272 C ATOM 3252 C GLY A 436 -10.165 -17.987 -15.159 1.00 54.31 C ANISOU 3252 C GLY A 436 4552 8135 7948 39 770 -251 C ATOM 3253 O GLY A 436 -9.577 -18.947 -15.637 1.00 63.45 O ANISOU 3253 O GLY A 436 5659 9385 9062 168 871 -279 O ATOM 3254 N SER A 437 -9.534 -16.928 -14.656 1.00 59.96 N ANISOU 3254 N SER A 437 5047 8728 9006 -106 742 -217 N ATOM 3255 CA SER A 437 -8.075 -16.857 -14.580 1.00 58.27 C ANISOU 3255 CA SER A 437 4472 8485 9184 -137 808 -219 C ATOM 3256 C SER A 437 -7.665 -15.978 -13.405 1.00 60.55 C ANISOU 3256 C SER A 437 4570 8611 9824 -297 548 -325 C ATOM 3257 O SER A 437 -8.482 -15.259 -12.826 1.00 57.55 O ANISOU 3257 O SER A 437 4356 8134 9377 -384 393 -358 O ATOM 3258 CB SER A 437 -7.464 -16.338 -15.877 1.00 65.20 C ANISOU 3258 CB SER A 437 5200 9381 10192 -139 1229 -1 C ATOM 3259 OG SER A 437 -6.051 -16.240 -15.749 1.00 75.92 O ANISOU 3259 OG SER A 437 6278 10805 11763 -55 1366 -16 O ATOM 3260 N GLY A 438 -6.378 -16.061 -13.046 1.00 64.09 N ANISOU 3260 N GLY A 438 4661 9030 10661 -319 481 -403 N ATOM 3261 CA GLY A 438 -5.820 -15.239 -11.992 1.00 65.68 C ANISOU 3261 CA GLY A 438 4633 9073 11247 -462 199 -547 C ATOM 3262 C GLY A 438 -6.126 -15.704 -10.580 1.00 66.87 C ANISOU 3262 C GLY A 438 4950 9226 11232 -384 -255 -780 C ATOM 3263 O GLY A 438 -6.647 -16.801 -10.353 1.00 67.23 O ANISOU 3263 O GLY A 438 5249 9385 10909 -218 -337 -817 O ATOM 3264 N PRO A 439 -5.812 -14.850 -9.599 1.00 65.92 N ANISOU 3264 N PRO A 439 4703 8960 11384 -495 -552 -941 N ATOM 3265 CA PRO A 439 -5.994 -15.234 -8.185 1.00 66.47 C ANISOU 3265 CA PRO A 439 4949 9034 11271 -381 -997 -1169 C ATOM 3266 C PRO A 439 -7.420 -15.592 -7.794 1.00 62.26 C ANISOU 3266 C PRO A 439 4898 8543 10215 -288 -1027 -1149 C ATOM 3267 O PRO A 439 -7.614 -16.303 -6.801 1.00 63.28 O ANISOU 3267 O PRO A 439 5231 8716 10096 -130 -1289 -1271 O ATOM 3268 CB PRO A 439 -5.525 -13.984 -7.425 1.00 61.62 C ANISOU 3268 CB PRO A 439 4138 8230 11045 -540 -1263 -1346 C ATOM 3269 CG PRO A 439 -4.592 -13.300 -8.363 1.00 69.37 C ANISOU 3269 CG PRO A 439 4679 9117 12561 -723 -991 -1234 C ATOM 3270 CD PRO A 439 -5.162 -13.537 -9.732 1.00 70.44 C ANISOU 3270 CD PRO A 439 4951 9342 12472 -715 -497 -936 C ATOM 3271 N ARG A 440 -8.402 -15.075 -8.528 1.00 51.07 N ANISOU 3271 N ARG A 440 3663 7100 8642 -373 -770 -996 N ATOM 3272 CA ARG A 440 -9.809 -15.319 -8.211 1.00 52.89 C ANISOU 3272 CA ARG A 440 4289 7359 8449 -301 -785 -983 C ATOM 3273 C ARG A 440 -10.484 -16.322 -9.139 1.00 59.84 C ANISOU 3273 C ARG A 440 5317 8371 9049 -220 -524 -835 C ATOM 3274 O ARG A 440 -11.704 -16.306 -9.305 1.00 55.49 O ANISOU 3274 O ARG A 440 5007 7828 8248 -219 -432 -773 O ATOM 3275 CB ARG A 440 -10.590 -14.002 -8.214 1.00 53.75 C ANISOU 3275 CB ARG A 440 4511 7330 8581 -426 -764 -968 C ATOM 3276 CG ARG A 440 -11.958 -14.090 -7.558 1.00 59.29 C ANISOU 3276 CG ARG A 440 5555 8017 8958 -338 -921 -1060 C ATOM 3277 CD ARG A 440 -12.059 -13.157 -6.363 1.00 53.02 C ANISOU 3277 CD ARG A 440 4854 7055 8236 -408 -1067 -1173 C ATOM 3278 NE ARG A 440 -13.226 -13.450 -5.536 1.00 56.13 N ANISOU 3278 NE ARG A 440 5590 7485 8251 -277 -1114 -1212 N ATOM 3279 CZ ARG A 440 -13.771 -12.591 -4.681 1.00 56.81 C ANISOU 3279 CZ ARG A 440 5885 7473 8226 -246 -1220 -1317 C ATOM 3280 NH1 ARG A 440 -13.255 -11.378 -4.538 1.00 48.40 N ANISOU 3280 NH1 ARG A 440 4748 6238 7403 -343 -1344 -1434 N ATOM 3281 NH2 ARG A 440 -14.833 -12.944 -3.970 1.00 48.25 N ANISOU 3281 NH2 ARG A 440 5089 6448 6796 -110 -1179 -1305 N ATOM 3282 N ASN A 441 -9.685 -17.195 -9.737 1.00 56.56 N ANISOU 3282 N ASN A 441 4747 8054 8690 -141 -419 -801 N ATOM 3283 CA ASN A 441 -10.199 -18.213 -10.638 1.00 49.65 C ANISOU 3283 CA ASN A 441 4016 7293 7557 -41 -215 -715 C ATOM 3284 C ASN A 441 -10.936 -19.273 -9.835 1.00 44.32 C ANISOU 3284 C ASN A 441 3612 6629 6599 78 -366 -795 C ATOM 3285 O ASN A 441 -10.948 -19.251 -8.603 1.00 47.41 O ANISOU 3285 O ASN A 441 4090 6961 6963 114 -604 -894 O ATOM 3286 CB ASN A 441 -9.054 -18.822 -11.455 1.00 52.35 C ANISOU 3286 CB ASN A 441 4115 7718 8059 31 -54 -676 C ATOM 3287 CG ASN A 441 -8.284 -19.904 -10.688 1.00 57.61 C ANISOU 3287 CG ASN A 441 4715 8409 8765 180 -259 -800 C ATOM 3288 OD1 ASN A 441 -8.235 -19.925 -9.453 1.00 57.17 O ANISOU 3288 OD1 ASN A 441 4718 8298 8708 213 -555 -916 O ATOM 3289 ND2 ASN A 441 -7.671 -20.807 -11.438 1.00 62.70 N ANISOU 3289 ND2 ASN A 441 5260 9137 9425 301 -98 -775 N ATOM 3290 N CYS A 442 -11.545 -20.245 -10.536 1.00 43.33 N ANISOU 3290 N CYS A 442 3634 6567 6261 154 -220 -757 N ATOM 3291 CA CYS A 442 -12.270 -21.301 -9.828 1.00 39.24 C ANISOU 3291 CA CYS A 442 3360 6017 5531 248 -313 -811 C ATOM 3292 C CYS A 442 -11.342 -22.089 -8.904 1.00 51.51 C ANISOU 3292 C CYS A 442 4884 7550 7138 387 -497 -884 C ATOM 3293 O CYS A 442 -10.442 -22.780 -9.373 1.00 47.56 O ANISOU 3293 O CYS A 442 4239 7097 6734 481 -455 -894 O ATOM 3294 CB CYS A 442 -12.926 -22.244 -10.842 1.00 39.10 C ANISOU 3294 CB CYS A 442 3454 6045 5356 293 -141 -792 C ATOM 3295 SG CYS A 442 -13.745 -23.610 -10.041 1.00 49.88 S ANISOU 3295 SG CYS A 442 5079 7314 6558 382 -205 -844 S ATOM 3296 N ILE A 443 -11.529 -21.992 -7.590 1.00 46.88 N ANISOU 3296 N ILE A 443 4444 6896 6473 433 -702 -935 N ATOM 3297 CA ILE A 443 -10.659 -22.754 -6.698 1.00 46.65 C ANISOU 3297 CA ILE A 443 4420 6853 6451 613 -909 -996 C ATOM 3298 C ILE A 443 -10.882 -24.270 -6.839 1.00 48.81 C ANISOU 3298 C ILE A 443 4862 7099 6586 757 -814 -957 C ATOM 3299 O ILE A 443 -9.987 -25.053 -6.509 1.00 48.98 O ANISOU 3299 O ILE A 443 4836 7120 6655 930 -931 -984 O ATOM 3300 CB ILE A 443 -10.887 -22.305 -5.235 1.00 50.28 C ANISOU 3300 CB ILE A 443 5072 7252 6781 674 -1154 -1059 C ATOM 3301 CG1 ILE A 443 -9.681 -22.605 -4.360 1.00 55.17 C ANISOU 3301 CG1 ILE A 443 5609 7884 7470 857 -1459 -1157 C ATOM 3302 CG2 ILE A 443 -12.137 -22.977 -4.615 1.00 49.86 C ANISOU 3302 CG2 ILE A 443 5393 7124 6427 742 -1060 -989 C ATOM 3303 CD1 ILE A 443 -9.825 -22.061 -2.923 1.00 58.11 C ANISOU 3303 CD1 ILE A 443 6195 8213 7672 953 -1743 -1252 C ATOM 3304 N GLY A 444 -12.063 -24.698 -7.304 1.00 47.72 N ANISOU 3304 N GLY A 444 4907 6920 6307 695 -621 -904 N ATOM 3305 CA GLY A 444 -12.387 -26.099 -7.429 1.00 39.99 C ANISOU 3305 CA GLY A 444 4090 5863 5242 800 -526 -884 C ATOM 3306 C GLY A 444 -12.029 -26.700 -8.773 1.00 50.62 C ANISOU 3306 C GLY A 444 5301 7260 6671 811 -374 -912 C ATOM 3307 O GLY A 444 -12.465 -27.813 -9.084 1.00 50.11 O ANISOU 3307 O GLY A 444 5374 7110 6557 866 -278 -926 O ATOM 3308 N MET A 445 -11.261 -25.978 -9.590 1.00 48.63 N ANISOU 3308 N MET A 445 4793 7131 6552 764 -330 -924 N ATOM 3309 CA MET A 445 -11.006 -26.399 -10.962 1.00 47.52 C ANISOU 3309 CA MET A 445 4559 7061 6436 791 -141 -943 C ATOM 3310 C MET A 445 -10.414 -27.810 -11.016 1.00 47.39 C ANISOU 3310 C MET A 445 4580 6988 6438 985 -132 -994 C ATOM 3311 O MET A 445 -10.958 -28.697 -11.683 1.00 43.60 O ANISOU 3311 O MET A 445 4240 6456 5871 1021 -20 -1045 O ATOM 3312 CB MET A 445 -10.060 -25.421 -11.646 1.00 50.70 C ANISOU 3312 CB MET A 445 4673 7586 7005 745 -60 -909 C ATOM 3313 CG MET A 445 -9.616 -25.898 -13.009 1.00 50.22 C ANISOU 3313 CG MET A 445 4531 7611 6938 832 167 -917 C ATOM 3314 SD MET A 445 -8.649 -24.694 -13.946 1.00 62.14 S ANISOU 3314 SD MET A 445 5725 9245 8639 770 376 -818 S ATOM 3315 CE MET A 445 -7.186 -24.565 -12.884 1.00 68.31 C ANISOU 3315 CE MET A 445 6178 9999 9777 815 187 -849 C ATOM 3316 N ARG A 446 -9.291 -28.024 -10.325 1.00 47.40 N ANISOU 3316 N ARG A 446 4450 6989 6570 1124 -270 -998 N ATOM 3317 CA ARG A 446 -8.612 -29.320 -10.398 1.00 51.09 C ANISOU 3317 CA ARG A 446 4931 7400 7082 1341 -262 -1038 C ATOM 3318 C ARG A 446 -9.533 -30.433 -9.922 1.00 49.02 C ANISOU 3318 C ARG A 446 5000 6953 6674 1396 -265 -1035 C ATOM 3319 O ARG A 446 -9.612 -31.495 -10.547 1.00 53.34 O ANISOU 3319 O ARG A 446 5637 7417 7215 1488 -150 -1090 O ATOM 3320 CB ARG A 446 -7.341 -29.313 -9.548 1.00 54.78 C ANISOU 3320 CB ARG A 446 5203 7892 7718 1500 -472 -1044 C ATOM 3321 CG ARG A 446 -6.146 -28.656 -10.151 1.00 79.23 C ANISOU 3321 CG ARG A 446 7901 11130 11073 1499 -424 -1066 C ATOM 3322 CD ARG A 446 -4.920 -29.029 -9.322 1.00100.71 C ANISOU 3322 CD ARG A 446 10429 13851 13986 1710 -665 -1107 C ATOM 3323 NE ARG A 446 -4.202 -27.856 -8.836 1.00112.99 N ANISOU 3323 NE ARG A 446 11674 15482 15777 1618 -853 -1138 N ATOM 3324 CZ ARG A 446 -4.601 -27.103 -7.816 1.00113.25 C ANISOU 3324 CZ ARG A 446 11813 15483 15734 1528 -1098 -1156 C ATOM 3325 NH1 ARG A 446 -5.726 -27.391 -7.167 1.00101.73 N ANISOU 3325 NH1 ARG A 446 10762 13934 13958 1526 -1145 -1115 N ATOM 3326 NH2 ARG A 446 -3.869 -26.056 -7.446 1.00120.63 N ANISOU 3326 NH2 ARG A 446 12437 16465 16933 1442 -1285 -1225 N ATOM 3327 N PHE A 447 -10.235 -30.195 -8.799 1.00 47.77 N ANISOU 3327 N PHE A 447 5029 6709 6411 1344 -379 -971 N ATOM 3328 CA PHE A 447 -11.165 -31.185 -8.275 1.00 48.52 C ANISOU 3328 CA PHE A 447 5431 6599 6403 1376 -328 -929 C ATOM 3329 C PHE A 447 -12.246 -31.513 -9.290 1.00 50.13 C ANISOU 3329 C PHE A 447 5705 6746 6597 1226 -142 -992 C ATOM 3330 O PHE A 447 -12.586 -32.685 -9.494 1.00 47.36 O ANISOU 3330 O PHE A 447 5500 6219 6276 1283 -58 -1027 O ATOM 3331 CB PHE A 447 -11.812 -30.683 -6.996 1.00 47.11 C ANISOU 3331 CB PHE A 447 5437 6366 6096 1338 -419 -836 C ATOM 3332 CG PHE A 447 -12.790 -31.644 -6.400 1.00 48.25 C ANISOU 3332 CG PHE A 447 5889 6282 6163 1363 -304 -752 C ATOM 3333 CD1 PHE A 447 -14.137 -31.639 -6.792 1.00 50.47 C ANISOU 3333 CD1 PHE A 447 6245 6479 6453 1162 -129 -758 C ATOM 3334 CD2 PHE A 447 -12.366 -32.566 -5.441 1.00 49.19 C ANISOU 3334 CD2 PHE A 447 6213 6254 6224 1597 -364 -659 C ATOM 3335 CE1 PHE A 447 -15.035 -32.525 -6.234 1.00 51.50 C ANISOU 3335 CE1 PHE A 447 6615 6369 6584 1162 13 -672 C ATOM 3336 CE2 PHE A 447 -13.259 -33.477 -4.886 1.00 52.86 C ANISOU 3336 CE2 PHE A 447 6969 6468 6646 1620 -203 -544 C ATOM 3337 CZ PHE A 447 -14.596 -33.457 -5.278 1.00 50.19 C ANISOU 3337 CZ PHE A 447 6672 6032 6366 1386 2 -551 C ATOM 3338 N ALA A 448 -12.813 -30.483 -9.929 1.00 44.82 N ANISOU 3338 N ALA A 448 4933 6204 5893 1041 -96 -1016 N ATOM 3339 CA ALA A 448 -13.940 -30.721 -10.825 1.00 44.78 C ANISOU 3339 CA ALA A 448 4994 6156 5864 914 19 -1094 C ATOM 3340 C ALA A 448 -13.502 -31.499 -12.075 1.00 50.01 C ANISOU 3340 C ALA A 448 5615 6838 6548 1010 99 -1226 C ATOM 3341 O ALA A 448 -14.226 -32.389 -12.537 1.00 53.46 O ANISOU 3341 O ALA A 448 6174 7136 7003 993 148 -1333 O ATOM 3342 CB ALA A 448 -14.608 -29.399 -11.214 1.00 39.44 C ANISOU 3342 CB ALA A 448 4231 5622 5131 739 27 -1079 C ATOM 3343 N LEU A 449 -12.334 -31.165 -12.648 1.00 49.27 N ANISOU 3343 N LEU A 449 5342 6908 6470 1115 124 -1232 N ATOM 3344 CA LEU A 449 -11.829 -31.903 -13.814 1.00 48.89 C ANISOU 3344 CA LEU A 449 5274 6890 6413 1252 234 -1356 C ATOM 3345 C LEU A 449 -11.581 -33.366 -13.475 1.00 54.26 C ANISOU 3345 C LEU A 449 6087 7356 7172 1413 224 -1418 C ATOM 3346 O LEU A 449 -11.969 -34.269 -14.223 1.00 52.96 O ANISOU 3346 O LEU A 449 6044 7084 6994 1457 283 -1568 O ATOM 3347 CB LEU A 449 -10.529 -31.267 -14.333 1.00 50.82 C ANISOU 3347 CB LEU A 449 5273 7334 6702 1349 313 -1313 C ATOM 3348 CG LEU A 449 -10.791 -29.865 -14.931 1.00 52.45 C ANISOU 3348 CG LEU A 449 5372 7720 6835 1200 381 -1244 C ATOM 3349 CD1 LEU A 449 -9.503 -29.059 -15.189 1.00 48.83 C ANISOU 3349 CD1 LEU A 449 4631 7416 6507 1246 482 -1153 C ATOM 3350 CD2 LEU A 449 -11.654 -29.971 -16.211 1.00 49.28 C ANISOU 3350 CD2 LEU A 449 5112 7371 6239 1187 476 -1348 C ATOM 3351 N MET A 450 -10.923 -33.613 -12.347 1.00 53.99 N ANISOU 3351 N MET A 450 6046 7247 7221 1519 132 -1313 N ATOM 3352 CA MET A 450 -10.652 -34.973 -11.915 1.00 52.56 C ANISOU 3352 CA MET A 450 6014 6838 7117 1701 123 -1331 C ATOM 3353 C MET A 450 -11.954 -35.717 -11.656 1.00 63.69 C ANISOU 3353 C MET A 450 7676 7988 8536 1586 159 -1352 C ATOM 3354 O MET A 450 -12.152 -36.845 -12.130 1.00 65.15 O ANISOU 3354 O MET A 450 7983 7974 8796 1652 226 -1472 O ATOM 3355 CB MET A 450 -9.777 -34.939 -10.666 1.00 49.78 C ANISOU 3355 CB MET A 450 5625 6477 6811 1855 -23 -1194 C ATOM 3356 CG MET A 450 -9.665 -36.261 -9.961 1.00 51.82 C ANISOU 3356 CG MET A 450 6101 6468 7118 2051 -45 -1149 C ATOM 3357 SD MET A 450 -8.589 -37.435 -10.871 1.00 65.27 S ANISOU 3357 SD MET A 450 7733 8113 8953 2328 38 -1286 S ATOM 3358 CE MET A 450 -7.194 -36.392 -11.339 1.00 54.97 C ANISOU 3358 CE MET A 450 6014 7157 7716 2405 3 -1303 C ATOM 3359 N ASN A 451 -12.864 -35.075 -10.921 1.00 58.78 N ANISOU 3359 N ASN A 451 7116 7348 7868 1408 131 -1249 N ATOM 3360 CA ASN A 451 -14.190 -35.624 -10.678 1.00 47.20 C ANISOU 3360 CA ASN A 451 5828 5643 6463 1261 203 -1255 C ATOM 3361 C ASN A 451 -14.847 -36.082 -11.973 1.00 57.30 C ANISOU 3361 C ASN A 451 7095 6874 7801 1169 253 -1478 C ATOM 3362 O ASN A 451 -15.277 -37.235 -12.090 1.00 52.73 O ANISOU 3362 O ASN A 451 6648 6020 7367 1177 306 -1570 O ATOM 3363 CB ASN A 451 -15.046 -34.564 -9.976 1.00 51.95 C ANISOU 3363 CB ASN A 451 6427 6316 6993 1079 189 -1138 C ATOM 3364 CG ASN A 451 -16.345 -35.113 -9.440 1.00 56.66 C ANISOU 3364 CG ASN A 451 7183 6650 7694 944 301 -1092 C ATOM 3365 OD1 ASN A 451 -16.587 -36.326 -9.486 1.00 53.75 O ANISOU 3365 OD1 ASN A 451 6937 6008 7476 976 385 -1131 O ATOM 3366 ND2 ASN A 451 -17.192 -34.224 -8.903 1.00 52.30 N ANISOU 3366 ND2 ASN A 451 6621 6156 7095 794 325 -1004 N ATOM 3367 N MET A 452 -14.926 -35.190 -12.962 1.00 55.18 N ANISOU 3367 N MET A 452 6686 6859 7422 1097 228 -1574 N ATOM 3368 CA MET A 452 -15.616 -35.523 -14.206 1.00 58.36 C ANISOU 3368 CA MET A 452 7104 7250 7822 1038 228 -1806 C ATOM 3369 C MET A 452 -14.867 -36.593 -14.990 1.00 54.92 C ANISOU 3369 C MET A 452 6728 6736 7405 1239 261 -1979 C ATOM 3370 O MET A 452 -15.482 -37.538 -15.515 1.00 56.63 O ANISOU 3370 O MET A 452 7050 6745 7721 1220 247 -2186 O ATOM 3371 CB MET A 452 -15.800 -34.271 -15.065 1.00 55.40 C ANISOU 3371 CB MET A 452 6604 7176 7269 969 197 -1832 C ATOM 3372 CG MET A 452 -16.685 -33.240 -14.412 1.00 60.31 C ANISOU 3372 CG MET A 452 7175 7850 7890 775 162 -1700 C ATOM 3373 SD MET A 452 -17.128 -31.899 -15.518 1.00 51.75 S ANISOU 3373 SD MET A 452 5988 7058 6618 708 120 -1739 S ATOM 3374 CE MET A 452 -15.566 -31.008 -15.577 1.00 51.40 C ANISOU 3374 CE MET A 452 5817 7245 6467 836 199 -1577 C ATOM 3375 N LYS A 453 -13.541 -36.476 -15.053 1.00 57.40 N ANISOU 3375 N LYS A 453 6960 7195 7656 1436 303 -1914 N ATOM 3376 CA LYS A 453 -12.736 -37.475 -15.755 1.00 58.76 C ANISOU 3376 CA LYS A 453 7180 7301 7847 1666 363 -2069 C ATOM 3377 C LYS A 453 -12.909 -38.868 -15.153 1.00 65.08 C ANISOU 3377 C LYS A 453 8156 7723 8848 1728 364 -2106 C ATOM 3378 O LYS A 453 -13.041 -39.859 -15.888 1.00 73.05 O ANISOU 3378 O LYS A 453 9282 8558 9918 1809 384 -2334 O ATOM 3379 CB LYS A 453 -11.271 -37.047 -15.753 1.00 56.71 C ANISOU 3379 CB LYS A 453 6744 7255 7550 1860 425 -1958 C ATOM 3380 CG LYS A 453 -10.990 -35.887 -16.706 1.00 57.89 C ANISOU 3380 CG LYS A 453 6737 7731 7526 1838 501 -1954 C ATOM 3381 CD LYS A 453 -9.517 -35.468 -16.682 1.00 54.43 C ANISOU 3381 CD LYS A 453 6067 7476 7140 2006 597 -1838 C ATOM 3382 CE LYS A 453 -9.257 -34.354 -17.674 1.00 63.38 C ANISOU 3382 CE LYS A 453 7061 8892 8130 1981 738 -1804 C ATOM 3383 NZ LYS A 453 -7.842 -33.877 -17.626 1.00 60.81 N ANISOU 3383 NZ LYS A 453 6448 8721 7935 2106 860 -1680 N ATOM 3384 N LEU A 454 -12.930 -38.966 -13.824 1.00 58.15 N ANISOU 3384 N LEU A 454 7328 6699 8069 1704 346 -1887 N ATOM 3385 CA LEU A 454 -13.137 -40.264 -13.190 1.00 63.83 C ANISOU 3385 CA LEU A 454 8246 7027 8981 1769 384 -1868 C ATOM 3386 C LEU A 454 -14.464 -40.880 -13.612 1.00 66.57 C ANISOU 3386 C LEU A 454 8701 7108 9485 1565 406 -2048 C ATOM 3387 O LEU A 454 -14.547 -42.088 -13.870 1.00 65.78 O ANISOU 3387 O LEU A 454 8736 6692 9565 1635 444 -2194 O ATOM 3388 CB LEU A 454 -13.073 -40.118 -11.672 1.00 63.59 C ANISOU 3388 CB LEU A 454 8289 6909 8963 1785 374 -1573 C ATOM 3389 CG LEU A 454 -11.620 -39.958 -11.232 1.00 67.77 C ANISOU 3389 CG LEU A 454 8728 7601 9420 2056 304 -1455 C ATOM 3390 CD1 LEU A 454 -11.525 -39.541 -9.776 1.00 63.39 C ANISOU 3390 CD1 LEU A 454 8243 7047 8795 2091 228 -1192 C ATOM 3391 CD2 LEU A 454 -10.863 -41.272 -11.496 1.00 59.23 C ANISOU 3391 CD2 LEU A 454 7741 6298 8467 2325 345 -1539 C ATOM 3392 N ALA A 455 -15.503 -40.056 -13.706 1.00 67.51 N ANISOU 3392 N ALA A 455 8742 7338 9571 1317 370 -2058 N ATOM 3393 CA ALA A 455 -16.813 -40.545 -14.111 1.00 68.31 C ANISOU 3393 CA ALA A 455 8880 7206 9870 1106 358 -2249 C ATOM 3394 C ALA A 455 -16.816 -40.981 -15.571 1.00 68.79 C ANISOU 3394 C ALA A 455 8943 7297 9896 1169 270 -2612 C ATOM 3395 O ALA A 455 -17.373 -42.031 -15.913 1.00 63.44 O ANISOU 3395 O ALA A 455 8355 6295 9453 1121 251 -2836 O ATOM 3396 CB ALA A 455 -17.871 -39.459 -13.872 1.00 54.26 C ANISOU 3396 CB ALA A 455 6979 5577 8059 858 326 -2171 C ATOM 3397 N LEU A 456 -16.236 -40.165 -16.453 1.00 67.60 N ANISOU 3397 N LEU A 456 8706 7522 9456 1278 221 -2680 N ATOM 3398 CA LEU A 456 -16.229 -40.506 -17.872 1.00 64.85 C ANISOU 3398 CA LEU A 456 8408 7242 8991 1386 146 -3020 C ATOM 3399 C LEU A 456 -15.468 -41.798 -18.109 1.00 70.23 C ANISOU 3399 C LEU A 456 9230 7680 9774 1612 205 -3171 C ATOM 3400 O LEU A 456 -15.901 -42.655 -18.896 1.00 67.64 O ANISOU 3400 O LEU A 456 9014 7152 9533 1634 128 -3503 O ATOM 3401 CB LEU A 456 -15.627 -39.360 -18.688 1.00 64.59 C ANISOU 3401 CB LEU A 456 8284 7653 8603 1499 156 -2990 C ATOM 3402 CG LEU A 456 -16.426 -38.060 -18.610 1.00 64.71 C ANISOU 3402 CG LEU A 456 8180 7895 8512 1297 86 -2869 C ATOM 3403 CD1 LEU A 456 -15.581 -36.823 -18.981 1.00 66.76 C ANISOU 3403 CD1 LEU A 456 8335 8542 8489 1400 167 -2697 C ATOM 3404 CD2 LEU A 456 -17.689 -38.169 -19.472 1.00 61.53 C ANISOU 3404 CD2 LEU A 456 7812 7455 8112 1181 -93 -3163 C ATOM 3405 N ILE A 457 -14.350 -41.976 -17.407 1.00 71.75 N ANISOU 3405 N ILE A 457 9418 7866 9979 1792 321 -2949 N ATOM 3406 CA ILE A 457 -13.556 -43.180 -17.604 1.00 76.22 C ANISOU 3406 CA ILE A 457 10109 8202 10648 2046 386 -3074 C ATOM 3407 C ILE A 457 -14.365 -44.417 -17.238 1.00 81.66 C ANISOU 3407 C ILE A 457 10962 8386 11679 1938 370 -3191 C ATOM 3408 O ILE A 457 -14.475 -45.364 -18.025 1.00 83.52 O ANISOU 3408 O ILE A 457 11323 8398 12012 2022 337 -3513 O ATOM 3409 CB ILE A 457 -12.256 -43.103 -16.794 1.00 71.04 C ANISOU 3409 CB ILE A 457 9383 7629 9978 2263 478 -2794 C ATOM 3410 CG1 ILE A 457 -11.323 -42.058 -17.396 1.00 66.29 C ANISOU 3410 CG1 ILE A 457 8592 7478 9117 2391 526 -2744 C ATOM 3411 CG2 ILE A 457 -11.581 -44.469 -16.774 1.00 67.97 C ANISOU 3411 CG2 ILE A 457 9140 6922 9763 2523 540 -2889 C ATOM 3412 CD1 ILE A 457 -10.193 -41.668 -16.468 1.00 66.38 C ANISOU 3412 CD1 ILE A 457 8447 7617 9159 2528 558 -2458 C ATOM 3413 N ARG A 458 -14.933 -44.428 -16.028 1.00 80.82 N ANISOU 3413 N ARG A 458 10866 8074 11769 1758 411 -2932 N ATOM 3414 CA ARG A 458 -15.626 -45.616 -15.543 1.00 75.54 C ANISOU 3414 CA ARG A 458 10347 6879 11474 1657 465 -2969 C ATOM 3415 C ARG A 458 -16.816 -45.942 -16.431 1.00 75.93 C ANISOU 3415 C ARG A 458 10383 6760 11706 1434 350 -3340 C ATOM 3416 O ARG A 458 -17.013 -47.096 -16.838 1.00 80.04 O ANISOU 3416 O ARG A 458 11028 6896 12488 1458 336 -3602 O ATOM 3417 CB ARG A 458 -16.064 -45.406 -14.095 1.00 72.49 C ANISOU 3417 CB ARG A 458 9981 6351 11210 1514 575 -2586 C ATOM 3418 CG ARG A 458 -15.794 -46.574 -13.165 1.00 77.02 C ANISOU 3418 CG ARG A 458 10766 6468 12031 1641 722 -2397 C ATOM 3419 CD ARG A 458 -14.402 -47.109 -13.361 1.00 81.92 C ANISOU 3419 CD ARG A 458 11463 7116 12545 2013 716 -2413 C ATOM 3420 NE ARG A 458 -14.107 -48.234 -12.479 1.00 83.89 N ANISOU 3420 NE ARG A 458 11938 6921 13017 2179 843 -2215 N ATOM 3421 CZ ARG A 458 -13.322 -49.266 -12.803 1.00 98.81 C ANISOU 3421 CZ ARG A 458 13955 8578 15013 2457 865 -2333 C ATOM 3422 NH1 ARG A 458 -13.103 -50.235 -11.924 1.00104.46 N ANISOU 3422 NH1 ARG A 458 14894 8872 15924 2617 987 -2108 N ATOM 3423 NH2 ARG A 458 -12.758 -49.357 -14.007 1.00 96.09 N ANISOU 3423 NH2 ARG A 458 13537 8403 14570 2602 785 -2668 N ATOM 3424 N VAL A 459 -17.581 -44.926 -16.800 1.00 73.70 N ANISOU 3424 N VAL A 459 9946 6764 11292 1237 238 -3394 N ATOM 3425 CA VAL A 459 -18.757 -45.164 -17.620 1.00 81.53 C ANISOU 3425 CA VAL A 459 10890 7624 12464 1033 72 -3760 C ATOM 3426 C VAL A 459 -18.365 -45.683 -19.004 1.00 82.59 C ANISOU 3426 C VAL A 459 11129 7802 12449 1241 -73 -4192 C ATOM 3427 O VAL A 459 -18.967 -46.633 -19.523 1.00 87.82 O ANISOU 3427 O VAL A 459 11858 8119 13389 1174 -187 -4550 O ATOM 3428 CB VAL A 459 -19.589 -43.880 -17.709 1.00 79.09 C ANISOU 3428 CB VAL A 459 10390 7651 12012 829 -30 -3703 C ATOM 3429 CG1 VAL A 459 -20.599 -44.045 -18.752 1.00 88.55 C ANISOU 3429 CG1 VAL A 459 11527 8801 13316 701 -267 -4124 C ATOM 3430 CG2 VAL A 459 -20.269 -43.630 -16.401 1.00 79.09 C ANISOU 3430 CG2 VAL A 459 10310 7491 12251 599 117 -3369 C ATOM 3431 N LEU A 460 -17.354 -45.065 -19.620 1.00 78.21 N ANISOU 3431 N LEU A 460 10591 7662 11465 1500 -59 -4174 N ATOM 3432 CA LEU A 460 -16.978 -45.416 -20.985 1.00 78.94 C ANISOU 3432 CA LEU A 460 10807 7860 11325 1736 -162 -4567 C ATOM 3433 C LEU A 460 -16.309 -46.783 -21.054 1.00 78.55 C ANISOU 3433 C LEU A 460 10942 7439 11465 1949 -82 -4733 C ATOM 3434 O LEU A 460 -16.428 -47.472 -22.069 1.00 82.13 O ANISOU 3434 O LEU A 460 11536 7780 11892 2063 -205 -5146 O ATOM 3435 CB LEU A 460 -16.078 -44.329 -21.567 1.00 74.79 C ANISOU 3435 CB LEU A 460 10238 7867 10310 1952 -94 -4441 C ATOM 3436 CG LEU A 460 -16.844 -43.028 -21.834 1.00 74.64 C ANISOU 3436 CG LEU A 460 10086 8196 10079 1777 -213 -4374 C ATOM 3437 CD1 LEU A 460 -15.931 -41.883 -22.231 1.00 68.32 C ANISOU 3437 CD1 LEU A 460 9228 7872 8857 1957 -87 -4164 C ATOM 3438 CD2 LEU A 460 -17.914 -43.268 -22.891 1.00 73.20 C ANISOU 3438 CD2 LEU A 460 9973 7970 9872 1717 -487 -4817 C ATOM 3439 N GLN A 461 -15.623 -47.194 -19.981 1.00 78.74 N ANISOU 3439 N GLN A 461 10983 7269 11667 2019 108 -4410 N ATOM 3440 CA GLN A 461 -15.170 -48.575 -19.857 1.00 81.61 C ANISOU 3440 CA GLN A 461 11524 7180 12302 2189 186 -4529 C ATOM 3441 C GLN A 461 -16.310 -49.567 -19.903 1.00 92.59 C ANISOU 3441 C GLN A 461 12996 8043 14141 1956 82 -4813 C ATOM 3442 O GLN A 461 -16.064 -50.747 -20.167 1.00 99.70 O ANISOU 3442 O GLN A 461 14069 8610 15202 2062 110 -4955 O ATOM 3443 CB GLN A 461 -14.431 -48.795 -18.548 1.00 80.55 C ANISOU 3443 CB GLN A 461 11399 6904 12301 2283 376 -4091 C ATOM 3444 CG GLN A 461 -13.075 -48.190 -18.506 1.00 87.18 C ANISOU 3444 CG GLN A 461 12157 8145 12821 2576 471 -3878 C ATOM 3445 CD GLN A 461 -12.455 -48.302 -17.144 1.00 85.08 C ANISOU 3445 CD GLN A 461 11886 7769 12673 2662 583 -3456 C ATOM 3446 OE1 GLN A 461 -13.133 -48.129 -16.134 1.00 81.34 O ANISOU 3446 OE1 GLN A 461 11411 7150 12344 2440 599 -3203 O ATOM 3447 NE2 GLN A 461 -11.160 -48.620 -17.100 1.00 79.91 N ANISOU 3447 NE2 GLN A 461 11233 7177 11952 3013 662 -3383 N ATOM 3448 N ASN A 462 -17.546 -49.134 -19.623 1.00 93.67 N ANISOU 3448 N ASN A 462 12992 8135 14463 1599 -11 -4794 N ATOM 3449 CA ASN A 462 -18.660 -50.061 -19.483 1.00100.87 C ANISOU 3449 CA ASN A 462 13914 8547 15866 1313 -66 -4942 C ATOM 3450 C ASN A 462 -19.777 -49.877 -20.495 1.00 98.56 C ANISOU 3450 C ASN A 462 13511 8391 15548 1092 -350 -5271 C ATOM 3451 O ASN A 462 -20.545 -50.823 -20.712 1.00107.30 O ANISOU 3451 O ASN A 462 14627 9141 17000 906 -438 -5449 O ATOM 3452 CB ASN A 462 -19.270 -49.966 -18.076 1.00101.64 C ANISOU 3452 CB ASN A 462 13919 8358 16342 1058 125 -4572 C ATOM 3453 CG ASN A 462 -18.462 -50.719 -17.048 1.00102.90 C ANISOU 3453 CG ASN A 462 14257 8200 16641 1233 386 -4221 C ATOM 3454 OD1 ASN A 462 -18.667 -51.905 -16.831 1.00102.74 O ANISOU 3454 OD1 ASN A 462 14370 7652 17013 1194 472 -4267 O ATOM 3455 ND2 ASN A 462 -17.532 -50.024 -16.407 1.00101.68 N ANISOU 3455 ND2 ASN A 462 14105 8394 16134 1428 495 -3834 N ATOM 3456 N PHE A 463 -19.888 -48.715 -21.126 1.00 90.46 N ANISOU 3456 N PHE A 463 12378 7861 14130 1123 -503 -5350 N ATOM 3457 CA PHE A 463 -21.066 -48.405 -21.913 1.00 93.79 C ANISOU 3457 CA PHE A 463 12664 8421 14552 914 -789 -5600 C ATOM 3458 C PHE A 463 -20.681 -47.614 -23.147 1.00 92.73 C ANISOU 3458 C PHE A 463 12592 8819 13823 1152 -959 -5768 C ATOM 3459 O PHE A 463 -19.664 -46.923 -23.175 1.00 91.89 O ANISOU 3459 O PHE A 463 12547 9039 13327 1400 -819 -5613 O ATOM 3460 CB PHE A 463 -22.087 -47.607 -21.099 1.00 94.69 C ANISOU 3460 CB PHE A 463 12519 8537 14923 597 -783 -5419 C ATOM 3461 CG PHE A 463 -22.568 -48.318 -19.879 1.00102.21 C ANISOU 3461 CG PHE A 463 13413 8972 16452 351 -561 -5198 C ATOM 3462 CD1 PHE A 463 -23.453 -49.375 -19.985 1.00107.52 C ANISOU 3462 CD1 PHE A 463 14032 9242 17579 130 -626 -5348 C ATOM 3463 CD2 PHE A 463 -22.135 -47.933 -18.622 1.00102.60 C ANISOU 3463 CD2 PHE A 463 13467 8947 16570 355 -270 -4804 C ATOM 3464 CE1 PHE A 463 -23.895 -50.041 -18.862 1.00110.64 C ANISOU 3464 CE1 PHE A 463 14386 9159 18494 -88 -369 -5093 C ATOM 3465 CE2 PHE A 463 -22.577 -48.595 -17.494 1.00106.58 C ANISOU 3465 CE2 PHE A 463 13964 8971 17562 159 -20 -4546 C ATOM 3466 CZ PHE A 463 -23.458 -49.653 -17.618 1.00109.33 C ANISOU 3466 CZ PHE A 463 14263 8913 18363 -66 -52 -4680 C ATOM 3467 N SER A 464 -21.502 -47.740 -24.177 1.00 97.56 N ANISOU 3467 N SER A 464 13184 9509 14375 1090 -1252 -6070 N ATOM 3468 CA SER A 464 -21.506 -46.796 -25.280 1.00 97.45 C ANISOU 3468 CA SER A 464 13199 10001 13824 1261 -1439 -6180 C ATOM 3469 C SER A 464 -22.820 -46.028 -25.241 1.00100.98 C ANISOU 3469 C SER A 464 13395 10565 14407 1001 -1668 -6197 C ATOM 3470 O SER A 464 -23.806 -46.474 -24.647 1.00101.68 O ANISOU 3470 O SER A 464 13290 10322 15023 696 -1722 -6221 O ATOM 3471 CB SER A 464 -21.299 -47.506 -26.626 1.00 99.76 C ANISOU 3471 CB SER A 464 13713 10338 13852 1484 -1606 -6514 C ATOM 3472 OG SER A 464 -19.940 -47.892 -26.775 1.00 95.34 O ANISOU 3472 OG SER A 464 13376 9806 13044 1787 -1358 -6453 O ATOM 3473 N PHE A 465 -22.812 -44.846 -25.846 1.00 99.97 N ANISOU 3473 N PHE A 465 13261 10910 13814 1133 -1769 -6151 N ATOM 3474 CA PHE A 465 -23.917 -43.903 -25.721 1.00 93.14 C ANISOU 3474 CA PHE A 465 12154 10211 13025 935 -1950 -6102 C ATOM 3475 C PHE A 465 -24.394 -43.493 -27.103 1.00 98.90 C ANISOU 3475 C PHE A 465 12948 11268 13362 1103 -2272 -6320 C ATOM 3476 O PHE A 465 -23.629 -42.919 -27.886 1.00 88.53 O ANISOU 3476 O PHE A 465 11842 10313 11484 1404 -2233 -6275 O ATOM 3477 CB PHE A 465 -23.505 -42.682 -24.906 1.00 82.84 C ANISOU 3477 CB PHE A 465 10766 9148 11561 924 -1739 -5764 C ATOM 3478 CG PHE A 465 -23.322 -42.979 -23.460 1.00 88.64 C ANISOU 3478 CG PHE A 465 11402 9547 12731 729 -1467 -5546 C ATOM 3479 CD1 PHE A 465 -22.196 -43.646 -23.011 1.00 95.79 C ANISOU 3479 CD1 PHE A 465 12472 10270 13654 878 -1212 -5454 C ATOM 3480 CD2 PHE A 465 -24.289 -42.607 -22.543 1.00 88.18 C ANISOU 3480 CD2 PHE A 465 11090 9343 13070 419 -1449 -5416 C ATOM 3481 CE1 PHE A 465 -22.034 -43.915 -21.678 1.00 90.78 C ANISOU 3481 CE1 PHE A 465 11772 9354 13366 725 -948 -5134 C ATOM 3482 CE2 PHE A 465 -24.128 -42.875 -21.199 1.00 85.02 C ANISOU 3482 CE2 PHE A 465 10634 8659 13009 257 -1143 -5086 C ATOM 3483 CZ PHE A 465 -23.009 -43.528 -20.770 1.00 82.69 C ANISOU 3483 CZ PHE A 465 10529 8216 12675 414 -903 -4922 C ATOM 3484 N LYS A 466 -25.661 -43.771 -27.386 1.00107.66 N ANISOU 3484 N LYS A 466 13872 12249 14784 923 -2572 -6535 N ATOM 3485 CA LYS A 466 -26.197 -43.656 -28.725 1.00113.86 C ANISOU 3485 CA LYS A 466 14730 13260 15270 1100 -2926 -6804 C ATOM 3486 C LYS A 466 -27.380 -42.695 -28.749 1.00109.12 C ANISOU 3486 C LYS A 466 13866 12847 14749 978 -3160 -6766 C ATOM 3487 O LYS A 466 -28.185 -42.682 -27.813 1.00 94.87 O ANISOU 3487 O LYS A 466 11755 10826 13466 666 -3128 -6679 O ATOM 3488 CB LYS A 466 -26.630 -45.041 -29.248 1.00102.67 C ANISOU 3488 CB LYS A 466 13343 11502 14164 1057 -3135 -7182 C ATOM 3489 CG LYS A 466 -25.583 -46.136 -29.022 1.00104.03 C ANISOU 3489 CG LYS A 466 13739 11388 14399 1127 -2884 -7214 C ATOM 3490 CD LYS A 466 -25.004 -46.638 -30.352 1.00109.18 C ANISOU 3490 CD LYS A 466 14717 12171 14596 1467 -3011 -7492 C ATOM 3491 CE LYS A 466 -23.662 -47.324 -30.150 1.00111.50 C ANISOU 3491 CE LYS A 466 15262 12325 14779 1634 -2678 -7420 C ATOM 3492 NZ LYS A 466 -22.872 -47.370 -31.410 1.00111.73 N ANISOU 3492 NZ LYS A 466 15618 12624 14209 2026 -2694 -7568 N ATOM 3493 N PRO A 467 -27.503 -41.872 -29.794 1.00111.57 N ANISOU 3493 N PRO A 467 14292 13548 14552 1234 -3370 -6806 N ATOM 3494 CA PRO A 467 -28.694 -41.024 -29.929 1.00109.91 C ANISOU 3494 CA PRO A 467 13838 13498 14426 1159 -3632 -6800 C ATOM 3495 C PRO A 467 -29.972 -41.844 -30.054 1.00118.84 C ANISOU 3495 C PRO A 467 14705 14339 16111 959 -3942 -7117 C ATOM 3496 O PRO A 467 -30.026 -42.849 -30.762 1.00121.29 O ANISOU 3496 O PRO A 467 15123 14490 16469 1036 -4130 -7442 O ATOM 3497 CB PRO A 467 -28.415 -40.221 -31.208 1.00103.22 C ANISOU 3497 CB PRO A 467 13261 13080 12877 1545 -3789 -6812 C ATOM 3498 CG PRO A 467 -26.943 -40.227 -31.355 1.00105.19 C ANISOU 3498 CG PRO A 467 13837 13456 12675 1768 -3466 -6657 C ATOM 3499 CD PRO A 467 -26.473 -41.541 -30.795 1.00111.89 C ANISOU 3499 CD PRO A 467 14697 13914 13902 1621 -3306 -6781 C ATOM 3500 N CYS A 468 -30.996 -41.413 -29.327 1.00126.12 N ANISOU 3500 N CYS A 468 15264 15181 17474 699 -3975 -7016 N ATOM 3501 CA CYS A 468 -32.357 -41.887 -29.494 1.00131.76 C ANISOU 3501 CA CYS A 468 15663 15695 18704 531 -4278 -7280 C ATOM 3502 C CYS A 468 -33.068 -41.022 -30.523 1.00126.91 C ANISOU 3502 C CYS A 468 15035 15425 17758 767 -4655 -7397 C ATOM 3503 O CYS A 468 -32.591 -39.953 -30.912 1.00122.24 O ANISOU 3503 O CYS A 468 14645 15206 16595 1010 -4628 -7205 O ATOM 3504 CB CYS A 468 -33.120 -41.834 -28.170 1.00138.03 C ANISOU 3504 CB CYS A 468 16060 16227 20157 150 -4071 -7084 C ATOM 3505 SG CYS A 468 -32.648 -43.057 -26.953 1.00144.66 S ANISOU 3505 SG CYS A 468 16864 16554 21545 -154 -3670 -6981 S ATOM 3506 N LYS A 469 -34.237 -41.488 -30.960 1.00127.62 N ANISOU 3506 N LYS A 469 14882 15375 18234 700 -5005 -7713 N ATOM 3507 CA LYS A 469 -35.108 -40.621 -31.746 1.00127.65 C ANISOU 3507 CA LYS A 469 14799 15662 18039 892 -5366 -7806 C ATOM 3508 C LYS A 469 -35.399 -39.325 -30.998 1.00125.11 C ANISOU 3508 C LYS A 469 14296 15526 17712 809 -5191 -7435 C ATOM 3509 O LYS A 469 -35.385 -38.239 -31.588 1.00119.06 O ANISOU 3509 O LYS A 469 13670 15116 16450 1070 -5313 -7324 O ATOM 3510 CB LYS A 469 -36.401 -41.355 -32.089 1.00124.63 C ANISOU 3510 CB LYS A 469 14095 15044 18216 775 -5741 -8195 C ATOM 3511 CG LYS A 469 -37.634 -40.478 -32.135 1.00126.14 C ANISOU 3511 CG LYS A 469 13961 15369 18599 768 -5977 -8191 C ATOM 3512 CD LYS A 469 -38.846 -41.307 -32.518 1.00140.71 C ANISOU 3512 CD LYS A 469 15479 16959 21023 663 -6356 -8616 C ATOM 3513 CE LYS A 469 -40.063 -40.956 -31.678 1.00138.63 C ANISOU 3513 CE LYS A 469 14702 16550 21420 381 -6309 -8520 C ATOM 3514 NZ LYS A 469 -41.148 -41.954 -31.894 1.00144.51 N ANISOU 3514 NZ LYS A 469 15093 16969 22844 221 -6602 -8929 N ATOM 3515 N GLU A 470 -35.623 -39.419 -29.688 1.00130.09 N ANISOU 3515 N GLU A 470 14642 15912 18876 459 -4880 -7224 N ATOM 3516 CA GLU A 470 -35.957 -38.272 -28.851 1.00130.28 C ANISOU 3516 CA GLU A 470 14466 16065 18969 348 -4690 -6884 C ATOM 3517 C GLU A 470 -34.764 -37.380 -28.545 1.00118.02 C ANISOU 3517 C GLU A 470 13201 14772 16869 473 -4398 -6536 C ATOM 3518 O GLU A 470 -34.950 -36.357 -27.876 1.00114.85 O ANISOU 3518 O GLU A 470 12668 14498 16473 402 -4244 -6252 O ATOM 3519 CB GLU A 470 -36.594 -38.745 -27.541 1.00133.58 C ANISOU 3519 CB GLU A 470 14498 16111 20143 -55 -4421 -6774 C ATOM 3520 CG GLU A 470 -36.007 -40.029 -26.967 1.00138.94 C ANISOU 3520 CG GLU A 470 15237 16414 21141 -253 -4170 -6812 C ATOM 3521 CD GLU A 470 -36.581 -41.283 -27.613 1.00152.52 C ANISOU 3521 CD GLU A 470 16865 17859 23228 -295 -4446 -7221 C ATOM 3522 OE1 GLU A 470 -36.536 -41.394 -28.857 1.00158.26 O ANISOU 3522 OE1 GLU A 470 17781 18761 23589 -25 -4817 -7515 O ATOM 3523 OE2 GLU A 470 -37.087 -42.154 -26.878 1.00157.42 O ANISOU 3523 OE2 GLU A 470 17227 18080 24504 -590 -4282 -7245 O ATOM 3524 N THR A 471 -33.559 -37.726 -28.994 1.00116.15 N ANISOU 3524 N THR A 471 13338 14611 16181 658 -4308 -6551 N ATOM 3525 CA THR A 471 -32.421 -36.841 -28.784 1.00105.43 C ANISOU 3525 CA THR A 471 12239 13516 14303 800 -4037 -6233 C ATOM 3526 C THR A 471 -32.603 -35.581 -29.610 1.00107.98 C ANISOU 3526 C THR A 471 12683 14236 14110 1090 -4221 -6136 C ATOM 3527 O THR A 471 -32.832 -35.644 -30.823 1.00109.97 O ANISOU 3527 O THR A 471 13099 14634 14053 1360 -4526 -6350 O ATOM 3528 CB THR A 471 -31.100 -37.510 -29.161 1.00 96.01 C ANISOU 3528 CB THR A 471 11411 12319 12750 966 -3883 -6279 C ATOM 3529 OG1 THR A 471 -30.994 -38.767 -28.492 1.00 99.92 O ANISOU 3529 OG1 THR A 471 11816 12412 13738 724 -3746 -6394 O ATOM 3530 CG2 THR A 471 -29.929 -36.623 -28.741 1.00 88.12 C ANISOU 3530 CG2 THR A 471 10610 11549 11323 1067 -3549 -5931 C ATOM 3531 N GLN A 472 -32.508 -34.437 -28.945 1.00100.87 N ANISOU 3531 N GLN A 472 11712 13496 13117 1044 -4032 -5809 N ATOM 3532 CA GLN A 472 -32.521 -33.159 -29.634 1.00 96.60 C ANISOU 3532 CA GLN A 472 11323 13318 12061 1324 -4136 -5648 C ATOM 3533 C GLN A 472 -31.228 -33.023 -30.422 1.00 89.20 C ANISOU 3533 C GLN A 472 10825 12607 10460 1637 -4007 -5565 C ATOM 3534 O GLN A 472 -30.137 -32.999 -29.848 1.00 86.34 O ANISOU 3534 O GLN A 472 10585 12249 9972 1595 -3670 -5371 O ATOM 3535 CB GLN A 472 -32.681 -32.027 -28.624 1.00 93.03 C ANISOU 3535 CB GLN A 472 10682 12945 11719 1174 -3936 -5316 C ATOM 3536 CG GLN A 472 -32.808 -30.658 -29.257 1.00 95.06 C ANISOU 3536 CG GLN A 472 11070 13539 11510 1446 -4038 -5126 C ATOM 3537 CD GLN A 472 -32.975 -29.572 -28.231 1.00 96.02 C ANISOU 3537 CD GLN A 472 10997 13716 11770 1293 -3846 -4814 C ATOM 3538 OE1 GLN A 472 -32.057 -29.290 -27.446 1.00 90.72 O ANISOU 3538 OE1 GLN A 472 10387 13063 11018 1199 -3528 -4586 O ATOM 3539 NE2 GLN A 472 -34.158 -28.957 -28.213 1.00101.43 N ANISOU 3539 NE2 GLN A 472 11438 14423 12679 1275 -4041 -4813 N ATOM 3540 N ILE A 473 -31.336 -32.979 -31.740 1.00 99.86 N ANISOU 3540 N ILE A 473 12412 14134 11396 1964 -4259 -5716 N ATOM 3541 CA ILE A 473 -30.158 -32.829 -32.585 1.00108.12 C ANISOU 3541 CA ILE A 473 13883 15398 11799 2292 -4102 -5616 C ATOM 3542 C ILE A 473 -30.497 -31.850 -33.702 1.00116.73 C ANISOU 3542 C ILE A 473 15176 16788 12389 2647 -4300 -5543 C ATOM 3543 O ILE A 473 -31.464 -32.066 -34.449 1.00120.63 O ANISOU 3543 O ILE A 473 15624 17278 12931 2762 -4692 -5812 O ATOM 3544 CB ILE A 473 -29.679 -34.181 -33.137 1.00106.95 C ANISOU 3544 CB ILE A 473 13909 15095 11631 2361 -4144 -5918 C ATOM 3545 CG1 ILE A 473 -29.153 -35.059 -32.002 1.00100.15 C ANISOU 3545 CG1 ILE A 473 12906 13938 11209 2048 -3880 -5921 C ATOM 3546 CG2 ILE A 473 -28.595 -33.970 -34.180 1.00109.26 C ANISOU 3546 CG2 ILE A 473 14642 15635 11236 2748 -3991 -5820 C ATOM 3547 CD1 ILE A 473 -28.528 -36.332 -32.456 1.00108.61 C ANISOU 3547 CD1 ILE A 473 14171 14846 12248 2125 -3861 -6172 C ATOM 3548 N PRO A 474 -29.752 -30.743 -33.826 1.00114.36 N ANISOU 3548 N PRO A 474 15093 16736 11622 2833 -4036 -5178 N ATOM 3549 CA PRO A 474 -28.696 -30.448 -32.847 1.00106.43 C ANISOU 3549 CA PRO A 474 14083 15728 10629 2674 -3597 -4879 C ATOM 3550 C PRO A 474 -29.246 -29.826 -31.568 1.00106.02 C ANISOU 3550 C PRO A 474 13680 15596 11008 2358 -3544 -4717 C ATOM 3551 O PRO A 474 -30.301 -29.184 -31.569 1.00110.60 O ANISOU 3551 O PRO A 474 14082 16214 11725 2340 -3775 -4709 O ATOM 3552 CB PRO A 474 -27.794 -29.464 -33.590 1.00101.86 C ANISOU 3552 CB PRO A 474 13858 15439 9406 3012 -3347 -4553 C ATOM 3553 CG PRO A 474 -28.721 -28.770 -34.539 1.00110.04 C ANISOU 3553 CG PRO A 474 14978 16631 10200 3264 -3667 -4575 C ATOM 3554 CD PRO A 474 -29.777 -29.768 -34.931 1.00113.32 C ANISOU 3554 CD PRO A 474 15247 16887 10920 3220 -4112 -5024 C ATOM 3555 N LEU A 475 -28.520 -30.049 -30.481 1.00102.99 N ANISOU 3555 N LEU A 475 13199 15093 10838 2124 -3238 -4599 N ATOM 3556 CA LEU A 475 -28.894 -29.512 -29.181 1.00 92.50 C ANISOU 3556 CA LEU A 475 11562 13683 9902 1825 -3140 -4439 C ATOM 3557 C LEU A 475 -29.038 -27.997 -29.245 1.00 86.88 C ANISOU 3557 C LEU A 475 10880 13222 8910 1955 -3106 -4129 C ATOM 3558 O LEU A 475 -28.248 -27.308 -29.896 1.00 92.05 O ANISOU 3558 O LEU A 475 11828 14103 9045 2225 -2942 -3909 O ATOM 3559 CB LEU A 475 -27.837 -29.912 -28.153 1.00 83.33 C ANISOU 3559 CB LEU A 475 10386 12403 8874 1642 -2787 -4340 C ATOM 3560 CG LEU A 475 -27.890 -29.381 -26.729 1.00 81.83 C ANISOU 3560 CG LEU A 475 9935 12113 9045 1345 -2566 -4085 C ATOM 3561 CD1 LEU A 475 -27.307 -30.430 -25.819 1.00 75.43 C ANISOU 3561 CD1 LEU A 475 9058 11012 8590 1120 -2318 -4089 C ATOM 3562 CD2 LEU A 475 -27.112 -28.080 -26.608 1.00 81.63 C ANISOU 3562 CD2 LEU A 475 10025 12291 8697 1448 -2251 -3618 C ATOM 3563 N LYS A 476 -30.054 -27.482 -28.566 1.00 76.34 N ANISOU 3563 N LYS A 476 9237 11826 7943 1768 -3232 -4092 N ATOM 3564 CA LYS A 476 -30.336 -26.057 -28.530 1.00 78.43 C ANISOU 3564 CA LYS A 476 9492 12287 8023 1873 -3226 -3810 C ATOM 3565 C LYS A 476 -30.277 -25.570 -27.085 1.00 78.80 C ANISOU 3565 C LYS A 476 9277 12236 8427 1574 -2983 -3586 C ATOM 3566 O LYS A 476 -30.752 -26.249 -26.169 1.00 82.01 O ANISOU 3566 O LYS A 476 9399 12398 9361 1272 -2963 -3705 O ATOM 3567 CB LYS A 476 -31.708 -25.763 -29.158 1.00 83.97 C ANISOU 3567 CB LYS A 476 10067 13005 8833 1976 -3598 -3942 C ATOM 3568 CG LYS A 476 -31.866 -26.301 -30.587 1.00 88.21 C ANISOU 3568 CG LYS A 476 10851 13609 9055 2270 -3858 -4177 C ATOM 3569 CD LYS A 476 -33.240 -25.981 -31.176 1.00 96.54 C ANISOU 3569 CD LYS A 476 11765 14689 10228 2384 -4249 -4326 C ATOM 3570 CE LYS A 476 -33.373 -26.464 -32.631 1.00110.43 C ANISOU 3570 CE LYS A 476 13795 16535 11629 2712 -4532 -4571 C ATOM 3571 NZ LYS A 476 -33.279 -27.952 -32.887 1.00106.15 N ANISOU 3571 NZ LYS A 476 13247 15813 11273 2628 -4643 -4938 N ATOM 3572 N LEU A 477 -29.678 -24.401 -26.881 1.00 80.08 N ANISOU 3572 N LEU A 477 9553 12506 8365 1640 -2688 -3161 N ATOM 3573 CA LEU A 477 -29.515 -23.841 -25.544 1.00 77.60 C ANISOU 3573 CA LEU A 477 9049 12044 8393 1369 -2359 -2846 C ATOM 3574 C LEU A 477 -30.776 -23.113 -25.084 1.00 74.79 C ANISOU 3574 C LEU A 477 8420 11662 8334 1289 -2524 -2821 C ATOM 3575 O LEU A 477 -31.501 -22.510 -25.878 1.00 74.33 O ANISOU 3575 O LEU A 477 8384 11767 8092 1513 -2817 -2880 O ATOM 3576 CB LEU A 477 -28.328 -22.872 -25.501 1.00 79.14 C ANISOU 3576 CB LEU A 477 9455 12332 8284 1456 -1988 -2433 C ATOM 3577 CG LEU A 477 -26.953 -23.533 -25.623 1.00 85.66 C ANISOU 3577 CG LEU A 477 10464 13145 8937 1477 -1719 -2392 C ATOM 3578 CD1 LEU A 477 -25.864 -22.509 -25.910 1.00 81.74 C ANISOU 3578 CD1 LEU A 477 10162 12771 8125 1617 -1396 -2016 C ATOM 3579 CD2 LEU A 477 -26.647 -24.305 -24.349 1.00 86.41 C ANISOU 3579 CD2 LEU A 477 10374 12999 9459 1170 -1540 -2406 C ATOM 3580 N SER A 478 -31.031 -23.180 -23.782 1.00 75.86 N ANISOU 3580 N SER A 478 8308 11593 8922 995 -2328 -2728 N ATOM 3581 CA SER A 478 -32.166 -22.499 -23.180 1.00 77.56 C ANISOU 3581 CA SER A 478 8245 11760 9462 907 -2399 -2680 C ATOM 3582 C SER A 478 -31.988 -20.982 -23.265 1.00 90.44 C ANISOU 3582 C SER A 478 9999 13526 10837 1068 -2291 -2343 C ATOM 3583 O SER A 478 -30.872 -20.465 -23.377 1.00 84.00 O ANISOU 3583 O SER A 478 9432 12769 9714 1144 -2046 -2086 O ATOM 3584 CB SER A 478 -32.336 -22.944 -21.727 1.00 72.15 C ANISOU 3584 CB SER A 478 7333 10822 9259 584 -2133 -2624 C ATOM 3585 OG SER A 478 -33.163 -22.058 -20.993 1.00 80.65 O ANISOU 3585 OG SER A 478 8198 11860 10584 521 -2070 -2480 O ATOM 3586 N LEU A 479 -33.115 -20.264 -23.214 1.00105.90 N ANISOU 3586 N LEU A 479 11760 15514 12965 1122 -2469 -2348 N ATOM 3587 CA LEU A 479 -33.111 -18.809 -23.314 1.00108.51 C ANISOU 3587 CA LEU A 479 12194 15937 13097 1292 -2397 -2045 C ATOM 3588 C LEU A 479 -33.024 -18.096 -21.959 1.00102.84 C ANISOU 3588 C LEU A 479 11364 15056 12655 1092 -2059 -1790 C ATOM 3589 O LEU A 479 -32.984 -16.861 -21.935 1.00109.64 O ANISOU 3589 O LEU A 479 12311 15947 13401 1209 -1973 -1540 O ATOM 3590 CB LEU A 479 -34.355 -18.333 -24.083 1.00109.89 C ANISOU 3590 CB LEU A 479 12244 16244 13264 1526 -2804 -2185 C ATOM 3591 CG LEU A 479 -35.729 -18.874 -23.684 1.00114.10 C ANISOU 3591 CG LEU A 479 12347 16690 14315 1391 -3050 -2482 C ATOM 3592 CD1 LEU A 479 -36.346 -18.066 -22.554 1.00114.89 C ANISOU 3592 CD1 LEU A 479 12201 16664 14788 1262 -2837 -2295 C ATOM 3593 CD2 LEU A 479 -36.655 -18.895 -24.891 1.00122.74 C ANISOU 3593 CD2 LEU A 479 13394 17951 15291 1667 -3559 -2741 C ATOM 3594 N GLY A 480 -32.969 -18.822 -20.840 1.00 78.87 N ANISOU 3594 N GLY A 480 8173 11838 9955 815 -1861 -1842 N ATOM 3595 CA GLY A 480 -32.851 -18.210 -19.528 1.00 64.00 C ANISOU 3595 CA GLY A 480 6231 9809 8276 658 -1552 -1627 C ATOM 3596 C GLY A 480 -31.417 -17.877 -19.122 1.00 62.41 C ANISOU 3596 C GLY A 480 6276 9575 7861 611 -1263 -1390 C ATOM 3597 O GLY A 480 -30.506 -17.792 -19.951 1.00 73.32 O ANISOU 3597 O GLY A 480 7876 11063 8918 733 -1261 -1318 O ATOM 3598 N GLY A 481 -31.220 -17.690 -17.816 1.00 61.26 N ANISOU 3598 N GLY A 481 6089 9278 7911 444 -1013 -1275 N ATOM 3599 CA GLY A 481 -29.955 -17.205 -17.281 1.00 62.10 C ANISOU 3599 CA GLY A 481 6378 9335 7882 397 -779 -1069 C ATOM 3600 C GLY A 481 -29.015 -18.302 -16.814 1.00 67.35 C ANISOU 3600 C GLY A 481 7105 9933 8551 266 -656 -1118 C ATOM 3601 O GLY A 481 -28.152 -18.097 -15.952 1.00 70.30 O ANISOU 3601 O GLY A 481 7557 10224 8928 185 -473 -995 O ATOM 3602 N LEU A 482 -29.214 -19.479 -17.384 1.00 67.95 N ANISOU 3602 N LEU A 482 7142 10033 8642 260 -784 -1319 N ATOM 3603 CA LEU A 482 -28.446 -20.686 -17.143 1.00 70.10 C ANISOU 3603 CA LEU A 482 7472 10233 8928 170 -705 -1400 C ATOM 3604 C LEU A 482 -27.988 -21.222 -18.485 1.00 62.03 C ANISOU 3604 C LEU A 482 6562 9345 7660 309 -850 -1522 C ATOM 3605 O LEU A 482 -28.758 -21.218 -19.450 1.00 61.99 O ANISOU 3605 O LEU A 482 6524 9443 7585 427 -1082 -1667 O ATOM 3606 CB LEU A 482 -29.294 -21.770 -16.467 1.00 82.73 C ANISOU 3606 CB LEU A 482 8909 11669 10853 20 -701 -1563 C ATOM 3607 CG LEU A 482 -29.576 -21.687 -14.981 1.00 85.59 C ANISOU 3607 CG LEU A 482 9213 11867 11442 -115 -480 -1451 C ATOM 3608 CD1 LEU A 482 -30.158 -22.998 -14.535 1.00 81.79 C ANISOU 3608 CD1 LEU A 482 8616 11206 11254 -250 -430 -1592 C ATOM 3609 CD2 LEU A 482 -28.269 -21.425 -14.298 1.00 91.72 C ANISOU 3609 CD2 LEU A 482 10174 12625 12049 -115 -312 -1277 C ATOM 3610 N LEU A 483 -26.759 -21.717 -18.543 1.00 55.33 N ANISOU 3610 N LEU A 483 5848 8498 6678 318 -726 -1483 N ATOM 3611 CA LEU A 483 -26.314 -22.412 -19.749 1.00 59.17 C ANISOU 3611 CA LEU A 483 6456 9094 6933 462 -827 -1628 C ATOM 3612 C LEU A 483 -26.721 -23.873 -19.650 1.00 59.74 C ANISOU 3612 C LEU A 483 6461 9035 7202 374 -927 -1897 C ATOM 3613 O LEU A 483 -26.059 -24.667 -18.983 1.00 53.81 O ANISOU 3613 O LEU A 483 5732 8151 6562 281 -783 -1892 O ATOM 3614 CB LEU A 483 -24.817 -22.277 -19.930 1.00 55.03 C ANISOU 3614 CB LEU A 483 6076 8627 6205 530 -625 -1469 C ATOM 3615 CG LEU A 483 -24.450 -22.862 -21.300 1.00 63.88 C ANISOU 3615 CG LEU A 483 7352 9888 7033 731 -706 -1612 C ATOM 3616 CD1 LEU A 483 -24.995 -21.948 -22.360 1.00 66.43 C ANISOU 3616 CD1 LEU A 483 7765 10386 7090 926 -835 -1566 C ATOM 3617 CD2 LEU A 483 -22.943 -23.046 -21.471 1.00 64.84 C ANISOU 3617 CD2 LEU A 483 7578 10046 7014 797 -471 -1494 C ATOM 3618 N GLN A 484 -27.805 -24.228 -20.329 1.00 61.84 N ANISOU 3618 N GLN A 484 6642 9323 7531 412 -1189 -2139 N ATOM 3619 CA GLN A 484 -28.388 -25.563 -20.292 1.00 64.23 C ANISOU 3619 CA GLN A 484 6840 9461 8104 306 -1316 -2430 C ATOM 3620 C GLN A 484 -29.122 -25.807 -21.603 1.00 70.14 C ANISOU 3620 C GLN A 484 7586 10330 8734 461 -1673 -2730 C ATOM 3621 O GLN A 484 -29.500 -24.852 -22.293 1.00 71.24 O ANISOU 3621 O GLN A 484 7756 10663 8649 628 -1826 -2684 O ATOM 3622 CB GLN A 484 -29.367 -25.714 -19.120 1.00 59.87 C ANISOU 3622 CB GLN A 484 6045 8703 8000 79 -1241 -2417 C ATOM 3623 CG GLN A 484 -30.464 -24.689 -19.158 1.00 59.86 C ANISOU 3623 CG GLN A 484 5873 8788 8084 100 -1363 -2381 C ATOM 3624 CD GLN A 484 -31.427 -24.825 -18.014 1.00 73.81 C ANISOU 3624 CD GLN A 484 7390 10356 10297 -104 -1236 -2358 C ATOM 3625 OE1 GLN A 484 -31.429 -25.830 -17.315 1.00 73.98 O ANISOU 3625 OE1 GLN A 484 7364 10159 10587 -266 -1089 -2403 O ATOM 3626 NE2 GLN A 484 -32.262 -23.806 -17.813 1.00 84.70 N ANISOU 3626 NE2 GLN A 484 8620 11800 11763 -80 -1264 -2272 N ATOM 3627 N PRO A 485 -29.345 -27.069 -21.971 1.00 70.68 N ANISOU 3627 N PRO A 485 7632 10276 8948 426 -1832 -3050 N ATOM 3628 CA PRO A 485 -30.123 -27.346 -23.184 1.00 75.02 C ANISOU 3628 CA PRO A 485 8169 10928 9408 578 -2239 -3399 C ATOM 3629 C PRO A 485 -31.602 -27.015 -23.022 1.00 73.89 C ANISOU 3629 C PRO A 485 7708 10749 9617 484 -2475 -3522 C ATOM 3630 O PRO A 485 -32.180 -27.142 -21.940 1.00 73.06 O ANISOU 3630 O PRO A 485 7351 10442 9967 238 -2321 -3451 O ATOM 3631 CB PRO A 485 -29.914 -28.848 -23.400 1.00 65.50 C ANISOU 3631 CB PRO A 485 7002 9529 8356 519 -2312 -3719 C ATOM 3632 CG PRO A 485 -28.627 -29.139 -22.707 1.00 70.98 C ANISOU 3632 CG PRO A 485 7852 10136 8982 468 -1931 -3474 C ATOM 3633 CD PRO A 485 -28.645 -28.274 -21.491 1.00 62.88 C ANISOU 3633 CD PRO A 485 6704 9075 8113 313 -1663 -3112 C ATOM 3634 N GLU A 486 -32.211 -26.599 -24.137 1.00 73.28 N ANISOU 3634 N GLU A 486 7651 10879 9313 711 -2851 -3708 N ATOM 3635 CA GLU A 486 -33.654 -26.361 -24.193 1.00 82.31 C ANISOU 3635 CA GLU A 486 8486 11992 10798 670 -3122 -3852 C ATOM 3636 C GLU A 486 -34.427 -27.556 -23.634 1.00 85.64 C ANISOU 3636 C GLU A 486 8627 12076 11837 388 -3104 -4058 C ATOM 3637 O GLU A 486 -35.119 -27.455 -22.616 1.00 86.12 O ANISOU 3637 O GLU A 486 8387 11971 12362 160 -2942 -3964 O ATOM 3638 CB GLU A 486 -34.061 -26.072 -25.645 1.00 89.67 C ANISOU 3638 CB GLU A 486 9596 13114 11362 995 -3462 -3974 C ATOM 3639 CG GLU A 486 -35.429 -25.426 -25.853 1.00 93.10 C ANISOU 3639 CG GLU A 486 9794 13572 12009 1050 -3695 -3997 C ATOM 3640 CD GLU A 486 -35.864 -25.498 -27.313 1.00106.79 C ANISOU 3640 CD GLU A 486 11703 15437 13437 1356 -4066 -4201 C ATOM 3641 OE1 GLU A 486 -35.318 -26.353 -28.048 1.00108.29 O ANISOU 3641 OE1 GLU A 486 12121 15622 13404 1456 -4144 -4391 O ATOM 3642 OE2 GLU A 486 -36.745 -24.708 -27.726 1.00115.05 O ANISOU 3642 OE2 GLU A 486 12666 16587 14462 1512 -4280 -4177 O ATOM 3643 N LYS A 487 -34.300 -28.656 -24.256 1.00 88.85 N ANISOU 3643 N LYS A 487 9135 12370 12253 410 -3230 -4313 N ATOM 3644 CA LYS A 487 -34.799 -29.970 -23.902 1.00 94.53 C ANISOU 3644 CA LYS A 487 9665 12752 13502 175 -3210 -4525 C ATOM 3645 C LYS A 487 -33.694 -30.777 -23.231 1.00 92.44 C ANISOU 3645 C LYS A 487 9539 12316 13268 33 -2925 -4488 C ATOM 3646 O LYS A 487 -32.525 -30.660 -23.611 1.00 78.11 O ANISOU 3646 O LYS A 487 8034 10667 10979 202 -2875 -4447 O ATOM 3647 CB LYS A 487 -35.283 -30.714 -25.150 1.00 97.32 C ANISOU 3647 CB LYS A 487 10078 13088 13812 331 -3570 -4862 C ATOM 3648 CG LYS A 487 -36.756 -30.984 -25.174 1.00114.56 C ANISOU 3648 CG LYS A 487 11905 15109 16513 217 -3763 -5036 C ATOM 3649 CD LYS A 487 -37.538 -29.689 -25.166 1.00124.72 C ANISOU 3649 CD LYS A 487 13041 16592 17757 312 -3854 -4882 C ATOM 3650 CE LYS A 487 -38.921 -29.903 -24.569 1.00134.29 C ANISOU 3650 CE LYS A 487 13812 17577 19635 92 -3851 -4948 C ATOM 3651 NZ LYS A 487 -38.847 -30.364 -23.149 1.00132.42 N ANISOU 3651 NZ LYS A 487 13389 17062 19864 -239 -3424 -4776 N ATOM 3652 N PRO A 488 -34.022 -31.623 -22.251 1.00 96.26 N ANISOU 3652 N PRO A 488 9814 12457 14302 -259 -2714 -4495 N ATOM 3653 CA PRO A 488 -32.977 -32.398 -21.576 1.00 86.28 C ANISOU 3653 CA PRO A 488 8701 11001 13080 -378 -2439 -4451 C ATOM 3654 C PRO A 488 -32.332 -33.404 -22.515 1.00 83.45 C ANISOU 3654 C PRO A 488 8601 10597 12509 -229 -2588 -4707 C ATOM 3655 O PRO A 488 -32.959 -33.932 -23.439 1.00 80.10 O ANISOU 3655 O PRO A 488 8150 10143 12142 -147 -2871 -4961 O ATOM 3656 CB PRO A 488 -33.727 -33.112 -20.442 1.00 88.90 C ANISOU 3656 CB PRO A 488 8750 10944 14085 -697 -2190 -4393 C ATOM 3657 CG PRO A 488 -35.081 -32.486 -20.388 1.00 94.21 C ANISOU 3657 CG PRO A 488 9107 11659 15031 -744 -2282 -4359 C ATOM 3658 CD PRO A 488 -35.363 -31.990 -21.772 1.00 97.68 C ANISOU 3658 CD PRO A 488 9630 12389 15096 -471 -2700 -4546 C ATOM 3659 N VAL A 489 -31.054 -33.656 -22.265 1.00 78.52 N ANISOU 3659 N VAL A 489 8230 9968 11636 -179 -2388 -4637 N ATOM 3660 CA VAL A 489 -30.277 -34.589 -23.071 1.00 82.00 C ANISOU 3660 CA VAL A 489 8942 10365 11848 -12 -2465 -4852 C ATOM 3661 C VAL A 489 -30.700 -36.007 -22.710 1.00 82.06 C ANISOU 3661 C VAL A 489 8834 9936 12409 -223 -2419 -5019 C ATOM 3662 O VAL A 489 -30.600 -36.425 -21.551 1.00 80.56 O ANISOU 3662 O VAL A 489 8555 9454 12601 -450 -2128 -4879 O ATOM 3663 CB VAL A 489 -28.769 -34.384 -22.859 1.00 77.69 C ANISOU 3663 CB VAL A 489 8694 9948 10875 143 -2161 -4581 C ATOM 3664 CG1 VAL A 489 -27.971 -35.245 -23.834 1.00 87.70 C ANISOU 3664 CG1 VAL A 489 10239 11218 11864 365 -2268 -4867 C ATOM 3665 CG2 VAL A 489 -28.398 -32.923 -23.026 1.00 74.38 C ANISOU 3665 CG2 VAL A 489 8356 9910 9995 309 -2091 -4266 C ATOM 3666 N VAL A 490 -31.204 -36.743 -23.700 1.00 83.56 N ANISOU 3666 N VAL A 490 9032 10067 12652 -142 -2698 -5308 N ATOM 3667 CA VAL A 490 -31.589 -38.135 -23.515 1.00 80.69 C ANISOU 3667 CA VAL A 490 8572 9288 12798 -320 -2682 -5494 C ATOM 3668 C VAL A 490 -30.933 -38.959 -24.615 1.00 90.37 C ANISOU 3668 C VAL A 490 10087 10527 13721 -91 -2858 -5764 C ATOM 3669 O VAL A 490 -30.947 -38.569 -25.791 1.00 84.70 O ANISOU 3669 O VAL A 490 9510 10104 12569 169 -3136 -5910 O ATOM 3670 CB VAL A 490 -33.122 -38.312 -23.498 1.00 88.65 C ANISOU 3670 CB VAL A 490 9209 10142 14333 -505 -2848 -5610 C ATOM 3671 CG1 VAL A 490 -33.746 -37.293 -22.537 1.00 86.03 C ANISOU 3671 CG1 VAL A 490 8615 9874 14198 -665 -2668 -5323 C ATOM 3672 CG2 VAL A 490 -33.741 -38.187 -24.887 1.00 88.01 C ANISOU 3672 CG2 VAL A 490 9133 10275 14032 -290 -3295 -5903 C ATOM 3673 N LEU A 491 -30.325 -40.079 -24.221 1.00 96.26 N ANISOU 3673 N LEU A 491 10948 10948 14678 -166 -2671 -5808 N ATOM 3674 CA LEU A 491 -29.537 -40.911 -25.117 1.00 97.81 C ANISOU 3674 CA LEU A 491 11444 11126 14592 55 -2763 -6033 C ATOM 3675 C LEU A 491 -29.813 -42.381 -24.829 1.00103.25 C ANISOU 3675 C LEU A 491 12071 11332 15827 -132 -2719 -6203 C ATOM 3676 O LEU A 491 -30.378 -42.743 -23.792 1.00108.20 O ANISOU 3676 O LEU A 491 12467 11631 17014 -424 -2526 -6074 O ATOM 3677 CB LEU A 491 -28.036 -40.636 -24.968 1.00 82.16 C ANISOU 3677 CB LEU A 491 9769 9301 12146 261 -2507 -5857 C ATOM 3678 CG LEU A 491 -27.540 -39.192 -25.060 1.00 83.82 C ANISOU 3678 CG LEU A 491 10057 9953 11838 433 -2450 -5628 C ATOM 3679 CD1 LEU A 491 -26.048 -39.132 -24.776 1.00 74.97 C ANISOU 3679 CD1 LEU A 491 9186 8912 10388 609 -2150 -5465 C ATOM 3680 CD2 LEU A 491 -27.863 -38.585 -26.420 1.00 80.49 C ANISOU 3680 CD2 LEU A 491 9733 9892 10957 687 -2759 -5760 C ATOM 3681 N LYS A 492 -29.396 -43.232 -25.763 1.00 93.53 N ANISOU 3681 N LYS A 492 11064 10052 14420 48 -2874 -6478 N ATOM 3682 CA LYS A 492 -29.396 -44.671 -25.562 1.00104.84 C ANISOU 3682 CA LYS A 492 12516 11024 16293 -81 -2811 -6638 C ATOM 3683 C LYS A 492 -28.058 -45.086 -24.959 1.00101.39 C ANISOU 3683 C LYS A 492 12347 10447 15730 7 -2462 -6457 C ATOM 3684 O LYS A 492 -27.010 -44.550 -25.326 1.00 95.40 O ANISOU 3684 O LYS A 492 11836 9994 14419 279 -2393 -6379 O ATOM 3685 CB LYS A 492 -29.656 -45.388 -26.894 1.00103.23 C ANISOU 3685 CB LYS A 492 12423 10828 15973 82 -3174 -7056 C ATOM 3686 CG LYS A 492 -29.918 -46.878 -26.811 1.00117.49 C ANISOU 3686 CG LYS A 492 14200 12142 18299 -77 -3181 -7283 C ATOM 3687 CD LYS A 492 -30.658 -47.364 -28.073 1.00122.36 C ANISOU 3687 CD LYS A 492 14790 12782 18918 17 -3630 -7730 C ATOM 3688 CE LYS A 492 -30.093 -46.717 -29.339 1.00121.91 C ANISOU 3688 CE LYS A 492 15031 13195 18092 414 -3857 -7860 C ATOM 3689 NZ LYS A 492 -30.978 -46.867 -30.523 1.00134.47 N ANISOU 3689 NZ LYS A 492 16566 14885 19640 528 -4330 -8255 N ATOM 3690 N VAL A 493 -28.101 -46.023 -24.011 1.00108.17 N ANISOU 3690 N VAL A 493 13148 10837 17114 -209 -2221 -6363 N ATOM 3691 CA VAL A 493 -26.920 -46.476 -23.274 1.00102.01 C ANISOU 3691 CA VAL A 493 12599 9859 16302 -129 -1876 -6158 C ATOM 3692 C VAL A 493 -26.858 -47.982 -23.388 1.00105.06 C ANISOU 3692 C VAL A 493 13094 9791 17033 -166 -1856 -6343 C ATOM 3693 O VAL A 493 -27.610 -48.680 -22.701 1.00109.30 O ANISOU 3693 O VAL A 493 13453 9915 18161 -444 -1750 -6292 O ATOM 3694 CB VAL A 493 -26.957 -46.077 -21.798 1.00 95.18 C ANISOU 3694 CB VAL A 493 11604 8830 15730 -330 -1532 -5768 C ATOM 3695 CG1 VAL A 493 -25.775 -46.712 -21.061 1.00 87.71 C ANISOU 3695 CG1 VAL A 493 10909 7624 14792 -211 -1205 -5573 C ATOM 3696 CG2 VAL A 493 -27.010 -44.566 -21.637 1.00 91.26 C ANISOU 3696 CG2 VAL A 493 11002 8765 14907 -302 -1546 -5593 C ATOM 3697 N GLU A 494 -25.942 -48.486 -24.210 1.00102.91 N ANISOU 3697 N GLU A 494 13117 9581 16402 118 -1917 -6533 N ATOM 3698 CA GLU A 494 -25.790 -49.917 -24.420 1.00106.90 C ANISOU 3698 CA GLU A 494 13767 9666 17185 121 -1910 -6737 C ATOM 3699 C GLU A 494 -24.563 -50.431 -23.670 1.00103.11 C ANISOU 3699 C GLU A 494 13527 8963 16686 264 -1552 -6499 C ATOM 3700 O GLU A 494 -23.529 -49.762 -23.615 1.00 98.53 O ANISOU 3700 O GLU A 494 13091 8683 15663 510 -1414 -6332 O ATOM 3701 CB GLU A 494 -25.683 -50.231 -25.916 1.00111.70 C ANISOU 3701 CB GLU A 494 14548 10465 17427 358 -2233 -7145 C ATOM 3702 CG GLU A 494 -26.836 -49.673 -26.759 1.00114.02 C ANISOU 3702 CG GLU A 494 14633 11019 17672 294 -2628 -7386 C ATOM 3703 CD GLU A 494 -26.647 -49.942 -28.244 1.00125.47 C ANISOU 3703 CD GLU A 494 16307 12675 18692 580 -2937 -7770 C ATOM 3704 OE1 GLU A 494 -25.495 -50.186 -28.652 1.00126.52 O ANISOU 3704 OE1 GLU A 494 16759 12893 18420 866 -2802 -7785 O ATOM 3705 OE2 GLU A 494 -27.641 -49.920 -29.004 1.00134.03 O ANISOU 3705 OE2 GLU A 494 17248 13833 19843 540 -3304 -8055 O ATOM 3706 N SER A 495 -24.693 -51.614 -23.076 1.00105.73 N ANISOU 3706 N SER A 495 13890 8765 17519 120 -1397 -6469 N ATOM 3707 CA ASER A 495 -23.593 -52.215 -22.336 0.51104.75 C ANISOU 3707 CA ASER A 495 14001 8377 17422 278 -1070 -6232 C ATOM 3708 CA BSER A 495 -23.590 -52.215 -22.335 0.49104.75 C ANISOU 3708 CA BSER A 495 14002 8377 17421 278 -1070 -6232 C ATOM 3709 C SER A 495 -22.545 -52.775 -23.291 1.00109.78 C ANISOU 3709 C SER A 495 14940 9095 17677 630 -1126 -6468 C ATOM 3710 O SER A 495 -22.875 -53.429 -24.282 1.00111.73 O ANISOU 3710 O SER A 495 15251 9273 17929 652 -1362 -6839 O ATOM 3711 CB ASER A 495 -24.122 -53.323 -21.423 0.51108.16 C ANISOU 3711 CB ASER A 495 14393 8198 18506 25 -873 -6095 C ATOM 3712 CB BSER A 495 -24.096 -53.337 -21.422 0.49108.17 C ANISOU 3712 CB BSER A 495 14401 8196 18503 31 -869 -6094 C ATOM 3713 OG ASER A 495 -23.076 -54.121 -20.890 0.51108.66 O ANISOU 3713 OG ASER A 495 14732 7962 18593 226 -608 -5917 O ATOM 3714 OG BSER A 495 -24.914 -52.844 -20.374 0.49106.15 O ANISOU 3714 OG BSER A 495 13893 7848 18591 -261 -706 -5790 O ATOM 3715 N ARG A 496 -21.270 -52.509 -22.994 1.00107.41 N ANISOU 3715 N ARG A 496 14814 8947 17051 921 -902 -6255 N ATOM 3716 CA ARG A 496 -20.186 -53.172 -23.712 1.00110.69 C ANISOU 3716 CA ARG A 496 15506 9372 17180 1265 -861 -6416 C ATOM 3717 C ARG A 496 -19.972 -54.591 -23.209 1.00125.23 C ANISOU 3717 C ARG A 496 17508 10628 19448 1258 -700 -6396 C ATOM 3718 O ARG A 496 -19.046 -55.269 -23.678 1.00119.17 O ANISOU 3718 O ARG A 496 16975 9795 18508 1549 -627 -6508 O ATOM 3719 CB ARG A 496 -18.877 -52.379 -23.599 1.00105.05 C ANISOU 3719 CB ARG A 496 14869 9047 15997 1596 -667 -6188 C ATOM 3720 CG ARG A 496 -18.974 -50.931 -24.101 1.00105.96 C ANISOU 3720 CG ARG A 496 14855 9749 15657 1632 -787 -6169 C ATOM 3721 CD ARG A 496 -17.706 -50.129 -23.818 1.00 93.88 C ANISOU 3721 CD ARG A 496 13347 8569 13754 1919 -557 -5896 C ATOM 3722 NE ARG A 496 -16.557 -50.580 -24.607 1.00103.04 N ANISOU 3722 NE ARG A 496 14708 9848 14595 2282 -450 -5998 N ATOM 3723 CZ ARG A 496 -15.333 -50.057 -24.519 1.00100.45 C ANISOU 3723 CZ ARG A 496 14382 9816 13969 2568 -231 -5786 C ATOM 3724 NH1 ARG A 496 -15.089 -49.052 -23.677 1.00 89.13 N ANISOU 3724 NH1 ARG A 496 12773 8594 12498 2540 -127 -5479 N ATOM 3725 NH2 ARG A 496 -14.352 -50.537 -25.275 1.00 99.64 N ANISOU 3725 NH2 ARG A 496 14437 9796 13626 2882 -109 -5884 N ATOM 3726 N ASP A 497 -20.800 -55.026 -22.255 1.00144.16 N ANISOU 3726 N ASP A 497 19782 12601 22391 943 -615 -6228 N ATOM 3727 CA ASP A 497 -20.893 -56.407 -21.777 1.00155.55 C ANISOU 3727 CA ASP A 497 21356 13432 24313 866 -479 -6201 C ATOM 3728 C ASP A 497 -19.615 -56.877 -21.095 1.00156.50 C ANISOU 3728 C ASP A 497 21724 13376 24363 1177 -185 -5917 C ATOM 3729 O ASP A 497 -19.435 -56.653 -19.894 1.00151.48 O ANISOU 3729 O ASP A 497 21064 12621 23869 1153 50 -5501 O ATOM 3730 CB ASP A 497 -21.269 -57.343 -22.931 1.00161.49 C ANISOU 3730 CB ASP A 497 22199 14014 25146 856 -726 -6678 C ATOM 3731 CG ASP A 497 -22.664 -57.061 -23.474 1.00163.85 C ANISOU 3731 CG ASP A 497 22221 14396 25639 535 -1037 -6947 C ATOM 3732 OD1 ASP A 497 -23.582 -56.806 -22.664 1.00163.34 O ANISOU 3732 OD1 ASP A 497 21899 14192 25970 212 -973 -6741 O ATOM 3733 OD2 ASP A 497 -22.842 -57.081 -24.708 1.00167.42 O ANISOU 3733 OD2 ASP A 497 22706 15063 25842 625 -1338 -7355 O TER 3734 ASP A 497 HETATM 3735 CHA HEM A 601 -15.300 -19.651 -9.279 1.00 42.50 C ANISOU 3735 CHA HEM A 601 4140 6322 5688 50 -273 -757 C HETATM 3736 CHB HEM A 601 -16.180 -22.481 -13.088 1.00 45.45 C ANISOU 3736 CHB HEM A 601 4576 6920 5771 211 98 -793 C HETATM 3737 CHC HEM A 601 -16.854 -26.224 -10.126 1.00 35.75 C ANISOU 3737 CHC HEM A 601 3757 5260 4565 363 -24 -922 C HETATM 3738 CHD HEM A 601 -15.649 -23.507 -6.308 1.00 43.62 C ANISOU 3738 CHD HEM A 601 4865 6249 5459 446 -422 -814 C HETATM 3739 C1A HEM A 601 -15.509 -20.056 -10.578 1.00 42.15 C ANISOU 3739 C1A HEM A 601 4058 6356 5602 54 -122 -714 C HETATM 3740 C2A HEM A 601 -15.518 -19.238 -11.778 1.00 46.50 C ANISOU 3740 C2A HEM A 601 4517 6969 6181 7 9 -628 C HETATM 3741 C3A HEM A 601 -15.733 -20.026 -12.811 1.00 42.49 C ANISOU 3741 C3A HEM A 601 4044 6545 5556 73 108 -632 C HETATM 3742 C4A HEM A 601 -15.903 -21.369 -12.316 1.00 44.19 C ANISOU 3742 C4A HEM A 601 4353 6726 5710 138 46 -728 C HETATM 3743 CMA HEM A 601 -15.826 -19.596 -14.292 1.00 39.89 C ANISOU 3743 CMA HEM A 601 3699 6318 5141 105 264 -546 C HETATM 3744 CAA HEM A 601 -15.282 -17.727 -11.894 1.00 39.86 C ANISOU 3744 CAA HEM A 601 3577 6085 5483 -87 41 -545 C HETATM 3745 CBA HEM A 601 -13.755 -17.593 -12.026 1.00 52.88 C ANISOU 3745 CBA HEM A 601 5000 7737 7353 -98 71 -527 C HETATM 3746 CGA HEM A 601 -13.314 -16.152 -12.144 1.00 53.09 C ANISOU 3746 CGA HEM A 601 4884 7675 7613 -214 124 -444 C HETATM 3747 O1A HEM A 601 -12.190 -15.920 -12.664 1.00 57.10 O ANISOU 3747 O1A HEM A 601 5172 8185 8340 -241 245 -381 O HETATM 3748 O2A HEM A 601 -14.083 -15.262 -11.700 1.00 49.84 O ANISOU 3748 O2A HEM A 601 4569 7171 7195 -277 62 -443 O HETATM 3749 C1B HEM A 601 -16.463 -23.722 -12.601 1.00 47.95 C ANISOU 3749 C1B HEM A 601 4995 7153 6072 254 56 -875 C HETATM 3750 C2B HEM A 601 -16.835 -24.870 -13.408 1.00 47.30 C ANISOU 3750 C2B HEM A 601 4983 7065 5926 315 92 -978 C HETATM 3751 C3B HEM A 601 -17.046 -25.901 -12.589 1.00 48.13 C ANISOU 3751 C3B HEM A 601 5181 7028 6079 333 59 -1022 C HETATM 3752 C4B HEM A 601 -16.776 -25.429 -11.250 1.00 46.99 C ANISOU 3752 C4B HEM A 601 5051 6826 5975 315 1 -937 C HETATM 3753 CMB HEM A 601 -16.992 -24.811 -14.921 1.00 37.89 C ANISOU 3753 CMB HEM A 601 3787 5998 4613 368 154 -1025 C HETATM 3754 CAB HEM A 601 -17.445 -27.377 -12.886 1.00 45.31 C ANISOU 3754 CAB HEM A 601 4922 6551 5743 379 77 -1144 C HETATM 3755 CBB HEM A 601 -17.179 -27.997 -14.039 1.00 50.76 C ANISOU 3755 CBB HEM A 601 5612 7291 6385 462 104 -1258 C HETATM 3756 C1C HEM A 601 -16.479 -25.841 -8.853 1.00 43.24 C ANISOU 3756 C1C HEM A 601 4765 6173 5493 404 -106 -857 C HETATM 3757 C2C HEM A 601 -16.271 -26.749 -7.760 1.00 45.74 C ANISOU 3757 C2C HEM A 601 5247 6359 5772 525 -135 -819 C HETATM 3758 C3C HEM A 601 -15.932 -26.025 -6.697 1.00 47.47 C ANISOU 3758 C3C HEM A 601 5516 6596 5927 571 -251 -781 C HETATM 3759 C4C HEM A 601 -15.914 -24.624 -7.071 1.00 43.36 C ANISOU 3759 C4C HEM A 601 4842 6190 5445 455 -294 -805 C HETATM 3760 CMC HEM A 601 -16.405 -28.297 -7.855 1.00 48.44 C ANISOU 3760 CMC HEM A 601 5708 6548 6150 604 -50 -828 C HETATM 3761 CAC HEM A 601 -15.643 -26.696 -5.357 1.00 49.55 C ANISOU 3761 CAC HEM A 601 5999 6752 6077 748 -320 -722 C HETATM 3762 CBC HEM A 601 -15.085 -26.077 -4.356 1.00 51.79 C ANISOU 3762 CBC HEM A 601 6340 7072 6268 847 -496 -725 C HETATM 3763 C1D HEM A 601 -15.524 -22.211 -6.800 1.00 43.18 C ANISOU 3763 C1D HEM A 601 4645 6263 5497 329 -446 -833 C HETATM 3764 C2D HEM A 601 -15.288 -21.040 -5.975 1.00 40.92 C ANISOU 3764 C2D HEM A 601 4359 5962 5227 311 -592 -874 C HETATM 3765 C3D HEM A 601 -15.177 -19.978 -6.784 1.00 49.17 C ANISOU 3765 C3D HEM A 601 5224 7045 6415 182 -553 -867 C HETATM 3766 C4D HEM A 601 -15.325 -20.443 -8.156 1.00 42.18 C ANISOU 3766 C4D HEM A 601 4240 6227 5558 141 -381 -811 C HETATM 3767 CMD HEM A 601 -15.198 -21.086 -4.451 1.00 39.89 C ANISOU 3767 CMD HEM A 601 4439 5770 4947 448 -757 -918 C HETATM 3768 CAD HEM A 601 -14.921 -18.509 -6.356 1.00 40.46 C ANISOU 3768 CAD HEM A 601 4050 5897 5427 105 -671 -917 C HETATM 3769 CBD HEM A 601 -13.413 -18.331 -6.189 1.00 42.95 C ANISOU 3769 CBD HEM A 601 4148 6222 5948 121 -848 -993 C HETATM 3770 CGD HEM A 601 -13.074 -16.978 -5.550 1.00 46.17 C ANISOU 3770 CGD HEM A 601 4491 6543 6510 48 -1024 -1095 C HETATM 3771 O1D HEM A 601 -11.960 -16.827 -4.979 1.00 50.04 O ANISOU 3771 O1D HEM A 601 4837 7014 7162 83 -1260 -1217 O HETATM 3772 O2D HEM A 601 -13.900 -16.036 -5.617 1.00 50.34 O ANISOU 3772 O2D HEM A 601 5094 7006 7026 -39 -948 -1073 O HETATM 3773 NA HEM A 601 -15.774 -21.340 -10.952 1.00 45.25 N ANISOU 3773 NA HEM A 601 4527 6770 5896 128 -76 -752 N HETATM 3774 NB HEM A 601 -16.425 -24.088 -11.298 1.00 43.38 N ANISOU 3774 NB HEM A 601 4486 6463 5533 262 -20 -873 N HETATM 3775 NC HEM A 601 -16.265 -24.550 -8.382 1.00 41.99 N ANISOU 3775 NC HEM A 601 4548 6079 5329 359 -187 -827 N HETATM 3776 ND HEM A 601 -15.565 -21.798 -8.124 1.00 37.40 N ANISOU 3776 ND HEM A 601 3748 5607 4857 228 -336 -815 N HETATM 3777 FE HEM A 601 -16.010 -22.914 -9.665 1.00 43.96 FE ANISOU 3777 FE HEM A 601 4558 6488 5657 231 -158 -815 FE HETATM 3778 O TPF A 602 -21.619 -18.200 -10.308 1.00 49.31 O ANISOU 3778 O TPF A 602 5303 7138 6296 -95 -3 -679 O HETATM 3779 C1 TPF A 602 -20.749 -19.204 -10.490 1.00 33.51 C ANISOU 3779 C1 TPF A 602 3295 5164 4272 -70 -13 -708 C HETATM 3780 C2 TPF A 602 -19.277 -18.609 -10.831 1.00 41.15 C ANISOU 3780 C2 TPF A 602 4173 6175 5289 -69 -34 -661 C HETATM 3781 C5 TPF A 602 -20.677 -19.970 -9.145 1.00 36.85 C ANISOU 3781 C5 TPF A 602 3831 5490 4680 -42 -22 -740 C HETATM 3782 C8 TPF A 602 -21.256 -20.149 -11.592 1.00 40.06 C ANISOU 3782 C8 TPF A 602 4098 6057 5064 -50 8 -761 C HETATM 3783 N1 TPF A 602 -18.922 -17.617 -9.836 1.00 49.85 N ANISOU 3783 N1 TPF A 602 5282 7194 6465 -101 -101 -656 N HETATM 3784 C3 TPF A 602 -18.262 -17.795 -8.641 1.00 45.83 C ANISOU 3784 C3 TPF A 602 4820 6625 5970 -72 -206 -716 C HETATM 3785 N3 TPF A 602 -19.320 -16.312 -9.957 1.00 54.43 N ANISOU 3785 N3 TPF A 602 5846 7733 7102 -146 -87 -608 N HETATM 3786 N2 TPF A 602 -18.190 -16.610 -8.008 1.00 55.43 N ANISOU 3786 N2 TPF A 602 6044 7764 7252 -107 -277 -736 N HETATM 3787 C4 TPF A 602 -18.851 -15.725 -8.846 1.00 50.12 C ANISOU 3787 C4 TPF A 602 5329 7093 6621 -160 -185 -662 C HETATM 3788 N4 TPF A 602 -19.879 -21.154 -9.256 1.00 44.74 N ANISOU 3788 N4 TPF A 602 4839 6493 5666 9 -34 -768 N HETATM 3789 C6 TPF A 602 -18.510 -21.209 -9.009 1.00 47.00 C ANISOU 3789 C6 TPF A 602 5089 6801 5968 60 -109 -768 C HETATM 3790 N6 TPF A 602 -20.318 -22.376 -9.721 1.00 47.70 N ANISOU 3790 N6 TPF A 602 5234 6843 6047 19 18 -813 N HETATM 3791 N5 TPF A 602 -18.133 -22.477 -9.298 1.00 48.53 N ANISOU 3791 N5 TPF A 602 5297 6988 6153 122 -89 -798 N HETATM 3792 C7 TPF A 602 -19.235 -23.125 -9.717 1.00 41.25 C ANISOU 3792 C7 TPF A 602 4422 6029 5223 89 -11 -828 C HETATM 3793 C9 TPF A 602 -22.599 -20.209 -11.937 1.00 44.04 C ANISOU 3793 C9 TPF A 602 4586 6560 5587 -68 6 -803 C HETATM 3794 C13 TPF A 602 -20.399 -21.051 -12.324 1.00 46.81 C ANISOU 3794 C13 TPF A 602 4937 6970 5881 2 15 -799 C HETATM 3795 C10 TPF A 602 -23.107 -21.062 -12.910 1.00 42.71 C ANISOU 3795 C10 TPF A 602 4388 6437 5405 -48 -30 -901 C HETATM 3796 C11 TPF A 602 -22.233 -21.927 -13.601 1.00 45.67 C ANISOU 3796 C11 TPF A 602 4783 6858 5710 7 -35 -955 C HETATM 3797 F1 TPF A 602 -22.707 -22.726 -14.545 1.00 50.84 F ANISOU 3797 F1 TPF A 602 5434 7547 6337 42 -94 -1086 F HETATM 3798 C12 TPF A 602 -20.866 -21.925 -13.317 1.00 40.20 C ANISOU 3798 C12 TPF A 602 4105 6176 4995 38 7 -892 C HETATM 3799 F2 TPF A 602 -19.103 -21.108 -12.094 1.00 51.66 F ANISOU 3799 F2 TPF A 602 5520 7592 6515 32 17 -770 F HETATM 3800 S DMS A 603 -21.935 -17.019 -5.774 0.84 62.29 S ANISOU 3800 S DMS A 603 7365 8484 7820 17 -49 -757 S HETATM 3801 O DMS A 603 -21.098 -18.243 -5.821 0.84 59.44 O ANISOU 3801 O DMS A 603 7009 8153 7422 45 -88 -758 O HETATM 3802 C1 DMS A 603 -20.921 -15.559 -6.171 0.84 64.87 C ANISOU 3802 C1 DMS A 603 7580 8799 8267 -41 -192 -782 C HETATM 3803 C2 DMS A 603 -22.999 -16.965 -7.245 0.84 61.75 C ANISOU 3803 C2 DMS A 603 7127 8481 7855 -57 48 -707 C HETATM 3804 C1 EDO A 604 -29.863 -37.244 -7.036 1.00107.42 C ANISOU 3804 C1 EDO A 604 12756 10916 17143 -1098 2055 -985 C HETATM 3805 O1 EDO A 604 -29.322 -37.558 -5.749 1.00108.61 O ANISOU 3805 O1 EDO A 604 13261 10922 17084 -930 2378 -613 O HETATM 3806 C2 EDO A 604 -29.261 -35.931 -7.525 1.00 97.43 C ANISOU 3806 C2 EDO A 604 11485 10142 15391 -960 1731 -1069 C HETATM 3807 O2 EDO A 604 -29.616 -35.699 -8.897 1.00 96.44 O ANISOU 3807 O2 EDO A 604 11087 10174 15383 -1059 1380 -1428 O HETATM 3808 O HOH A 701 -20.859 -53.255 -19.038 1.00108.17 O ANISOU 3808 O HOH A 701 14930 8058 18113 689 -41 -5136 O HETATM 3809 O HOH A 702 -3.120 -31.812 -22.425 1.00 81.58 O ANISOU 3809 O HOH A 702 8182 12264 10552 2835 2500 -1361 O HETATM 3810 O HOH A 703 -23.913 6.073 -21.993 1.00 77.60 O ANISOU 3810 O HOH A 703 10673 7610 11204 1516 2246 3755 O HETATM 3811 O HOH A 704 -30.177 -19.614 3.698 1.00 55.87 O ANISOU 3811 O HOH A 704 8160 6905 6164 1008 2477 -70 O HETATM 3812 O HOH A 705 -2.974 -49.509 -16.334 1.00 92.61 O ANISOU 3812 O HOH A 705 12047 9542 13598 5204 1009 -2811 O HETATM 3813 O HOH A 706 1.010 -37.706 -11.774 1.00 89.39 O ANISOU 3813 O HOH A 706 8507 12042 13415 3947 -133 -1459 O HETATM 3814 O HOH A 707 -6.530 -16.390 -34.048 1.00 95.63 O ANISOU 3814 O HOH A 707 12344 14594 9397 2980 5771 2337 O HETATM 3815 O HOH A 708 -33.878 -14.644 -21.392 1.00 78.81 O ANISOU 3815 O HOH A 708 8327 11989 9628 1364 -1897 -1201 O HETATM 3816 O HOH A 709 -28.682 -3.826 -11.273 1.00 59.83 O ANISOU 3816 O HOH A 709 6849 7405 8479 578 161 21 O HETATM 3817 O HOH A 710 -10.494 -49.725 -19.888 1.00 94.04 O ANISOU 3817 O HOH A 710 13213 8986 13533 3457 673 -4245 O HETATM 3818 O HOH A 711 -16.938 -31.276 -1.936 1.00 76.83 O ANISOU 3818 O HOH A 711 10591 9395 9205 1324 170 -197 O HETATM 3819 O HOH A 712 -2.126 -42.379 -8.735 1.00 76.43 O ANISOU 3819 O HOH A 712 8906 9034 11102 4435 -470 -1146 O HETATM 3820 O HOH A 713 -28.907 -21.555 -21.962 1.00 67.59 O ANISOU 3820 O HOH A 713 7443 10453 7786 809 -1493 -1934 O HETATM 3821 O HOH A 714 -8.468 -6.210 -0.961 1.00 80.58 O ANISOU 3821 O HOH A 714 7757 9229 13631 -873 -3082 -2893 O HETATM 3822 O HOH A 715 -25.056 -21.490 -16.283 1.00 52.50 O ANISOU 3822 O HOH A 715 5538 7937 6475 119 -333 -1185 O HETATM 3823 O HOH A 716 -11.000 -26.810 -19.412 1.00 54.91 O ANISOU 3823 O HOH A 716 5629 8639 6594 1217 1028 -1051 O HETATM 3824 O HOH A 717 -8.464 -13.579 -10.845 1.00 57.08 O ANISOU 3824 O HOH A 717 4212 7770 9706 -611 -93 -601 O HETATM 3825 O HOH A 718 -15.780 -41.633 -10.026 1.00 59.91 O ANISOU 3825 O HOH A 718 8247 5586 8931 1419 643 -1360 O HETATM 3826 O HOH A 719 -13.223 -4.955 -7.007 1.00 60.30 O ANISOU 3826 O HOH A 719 5648 6665 10601 -1123 -753 -1087 O HETATM 3827 O HOH A 720 -19.878 -33.418 -7.696 1.00 50.63 O ANISOU 3827 O HOH A 720 6473 5769 6996 447 566 -839 O HETATM 3828 O HOH A 721 -28.050 -17.126 -20.646 1.00 69.04 O ANISOU 3828 O HOH A 721 7746 10606 7878 847 -924 -961 O HETATM 3829 O HOH A 722 -20.287 -14.280 -23.009 1.00 55.90 O ANISOU 3829 O HOH A 722 6708 8963 5570 1074 718 403 O HETATM 3830 O HOH A 723 -27.240 -6.030 -29.236 1.00 90.85 O ANISOU 3830 O HOH A 723 12890 13549 8082 3457 0 2086 O HETATM 3831 O HOH A 724 -16.858 -31.589 -9.268 1.00 43.87 O ANISOU 3831 O HOH A 724 5271 5600 5800 680 157 -997 O HETATM 3832 O HOH A 725 -1.232 -19.661 16.137 1.00121.69 O ANISOU 3832 O HOH A 725 17205 16209 12823 5184 -7791 -4113 O HETATM 3833 O HOH A 726 -11.925 -15.522 -22.013 1.00 60.86 O ANISOU 3833 O HOH A 726 6223 9343 7557 598 2164 745 O HETATM 3834 O HOH A 727 -5.449 -37.240 -30.929 1.00 99.21 O ANISOU 3834 O HOH A 727 13132 14515 10047 4390 2921 -2953 O HETATM 3835 O HOH A 728 -14.419 -45.990 -10.341 1.00 74.84 O ANISOU 3835 O HOH A 728 10672 6323 11440 2007 848 -1531 O HETATM 3836 O HOH A 729 -22.108 -40.658 -1.029 1.00 67.92 O ANISOU 3836 O HOH A 729 10509 5421 9877 998 2481 789 O HETATM 3837 O HOH A 730 -25.319 -26.839 -7.848 1.00 50.96 O ANISOU 3837 O HOH A 730 5802 6483 7079 -216 625 -857 O HETATM 3838 O HOH A 731 -1.522 -28.209 1.823 1.00 73.86 O ANISOU 3838 O HOH A 731 7806 10460 9797 3428 -4222 -1690 O HETATM 3839 O HOH A 732 -26.069 -19.999 -12.527 1.00 51.75 O ANISOU 3839 O HOH A 732 5382 7520 6762 -109 -54 -934 O HETATM 3840 O HOH A 733 -10.308 -21.166 -17.231 1.00 56.52 O ANISOU 3840 O HOH A 733 5156 8725 7594 504 1030 -389 O HETATM 3841 O HOH A 734 -25.551 -43.133 -9.358 1.00 72.44 O ANISOU 3841 O HOH A 734 9221 5349 12953 -581 1586 -1607 O HETATM 3842 O HOH A 735 -26.765 -42.688 -6.949 1.00 71.06 O ANISOU 3842 O HOH A 735 9150 4929 12922 -700 2283 -892 O HETATM 3843 O HOH A 736 -21.771 -16.528 -12.504 1.00 52.23 O ANISOU 3843 O HOH A 736 5567 7638 6641 -69 25 -537 O HETATM 3844 O HOH A 737 -30.577 -2.561 -24.867 1.00 71.08 O ANISOU 3844 O HOH A 737 9487 10096 7423 2956 -412 1940 O HETATM 3845 O HOH A 738 -7.458 -32.449 -12.022 1.00 58.73 O ANISOU 3845 O HOH A 738 5962 8226 8126 1830 23 -1209 O HETATM 3846 O HOH A 739 -33.537 -2.713 -21.965 1.00 61.83 O ANISOU 3846 O HOH A 739 7466 8821 7207 2703 -933 1190 O HETATM 3847 O HOH A 740 -17.530 -21.384 -17.675 1.00 51.59 O ANISOU 3847 O HOH A 740 5499 8083 6018 416 348 -719 O HETATM 3848 O HOH A 741 -35.261 -16.907 -7.566 1.00 65.86 O ANISOU 3848 O HOH A 741 6246 8791 9985 -48 935 -867 O HETATM 3849 O HOH A 742 -20.261 -1.153 -8.801 1.00 68.88 O ANISOU 3849 O HOH A 742 7876 7343 10950 -534 25 -351 O HETATM 3850 O HOH A 743 -22.898 -42.365 -8.269 1.00 64.03 O ANISOU 3850 O HOH A 743 8639 4809 10879 50 1514 -1143 O HETATM 3851 O HOH A 744 -18.602 -19.239 14.427 1.00 83.37 O ANISOU 3851 O HOH A 744 15601 10936 5142 4275 -1326 -1191 O HETATM 3852 O HOH A 745 -15.201 -3.860 -5.362 1.00 59.78 O ANISOU 3852 O HOH A 745 6142 6410 10163 -923 -985 -1375 O HETATM 3853 O HOH A 746 -15.887 -36.215 -35.375 1.00 95.02 O ANISOU 3853 O HOH A 746 14434 14228 7440 4155 -175 -4487 O HETATM 3854 O HOH A 747 -27.820 -16.750 -24.445 1.00 72.21 O ANISOU 3854 O HOH A 747 8705 11495 7236 1597 -1226 -919 O HETATM 3855 O HOH A 748 -8.395 -30.027 -5.321 1.00 59.09 O ANISOU 3855 O HOH A 748 6555 8118 7778 1808 -1078 -900 O HETATM 3856 O HOH A 749 -9.541 -27.953 -7.093 1.00 52.59 O ANISOU 3856 O HOH A 749 5454 7472 7058 1265 -766 -947 O HETATM 3857 O HOH A 750 -27.519 -10.846 -6.290 1.00 56.62 O ANISOU 3857 O HOH A 750 6508 7494 7511 172 275 -687 O HETATM 3858 O HOH A 751 -16.502 -13.833 -12.478 1.00 52.78 O ANISOU 3858 O HOH A 751 5227 7496 7330 -281 180 -284 O HETATM 3859 O HOH A 752 -10.310 -5.135 -24.397 1.00 75.21 O ANISOU 3859 O HOH A 752 7937 9428 11210 36 4421 3174 O HETATM 3860 O HOH A 753 -21.720 -46.794 -1.096 1.00 97.15 O ANISOU 3860 O HOH A 753 14958 7017 14937 1226 3293 1193 O HETATM 3861 O HOH A 754 -17.587 -13.698 -30.571 1.00 75.43 O ANISOU 3861 O HOH A 754 10675 12222 5764 2768 2210 1505 O HETATM 3862 O HOH A 755 -25.512 -18.908 -14.964 1.00 51.11 O ANISOU 3862 O HOH A 755 5321 7705 6394 67 -218 -883 O HETATM 3863 O HOH A 756 -2.872 -8.732 -8.522 1.00 90.90 O ANISOU 3863 O HOH A 756 6747 10949 16842 -1467 -828 -1255 O HETATM 3864 O HOH A 757 -5.339 -19.395 -4.590 1.00 79.79 O ANISOU 3864 O HOH A 757 7235 11020 12061 543 -2112 -1604 O HETATM 3865 O HOH A 758 -32.880 -18.802 -9.477 1.00 53.37 O ANISOU 3865 O HOH A 758 4883 7341 8054 -212 460 -984 O HETATM 3866 O HOH A 759 -16.319 -19.068 -18.024 1.00 53.52 O ANISOU 3866 O HOH A 759 5599 8345 6394 366 618 -354 O HETATM 3867 O HOH A 760 -23.232 -22.812 -9.449 1.00 49.38 O ANISOU 3867 O HOH A 760 5454 6908 6402 -98 168 -856 O HETATM 3868 O HOH A 761 -16.794 -10.351 -4.430 1.00 46.60 O ANISOU 3868 O HOH A 761 4984 5942 6780 -284 -940 -1244 O HETATM 3869 O HOH A 762 -35.248 -16.721 2.722 1.00 65.39 O ANISOU 3869 O HOH A 762 8241 8080 8525 882 3301 -179 O HETATM 3870 O HOH A 763 -19.126 -15.966 -13.041 1.00 61.73 O ANISOU 3870 O HOH A 763 6645 8861 7950 -95 128 -401 O HETATM 3871 O HOH A 764 -25.275 -20.601 -9.847 1.00 50.14 O ANISOU 3871 O HOH A 764 5379 7086 6586 -157 166 -835 O HETATM 3872 O HOH A 765 -21.270 -42.499 5.975 1.00 85.45 O ANISOU 3872 O HOH A 765 15244 6848 10373 2758 3698 2828 O HETATM 3873 O HOH A 766 -8.962 -31.335 -2.681 1.00 59.59 O ANISOU 3873 O HOH A 766 7367 7907 7368 2247 -1298 -690 O HETATM 3874 O HOH A 767 -26.140 -4.662 -11.325 1.00 62.32 O ANISOU 3874 O HOH A 767 7171 7735 8771 258 176 22 O HETATM 3875 O HOH A 768 -23.436 -21.954 12.540 1.00 97.44 O ANISOU 3875 O HOH A 768 17371 12314 7338 3741 1379 205 O HETATM 3876 O HOH A 769 -23.433 -17.319 -14.581 1.00 47.98 O ANISOU 3876 O HOH A 769 5016 7288 5924 61 -52 -614 O HETATM 3877 O HOH A 770 -5.811 -41.151 -34.055 1.00118.39 O ANISOU 3877 O HOH A 770 16856 16520 11609 5095 2451 -4272 O HETATM 3878 O HOH A 771 -16.390 -9.874 2.846 1.00 58.48 O ANISOU 3878 O HOH A 771 7819 7265 7137 625 -2185 -2404 O HETATM 3879 O HOH A 772 -29.599 -10.991 7.174 1.00 78.23 O ANISOU 3879 O HOH A 772 12159 9768 7795 2035 1619 -1266 O HETATM 3880 O HOH A 773 -18.085 -30.075 -4.445 1.00 59.38 O ANISOU 3880 O HOH A 773 7810 7392 7358 801 239 -481 O HETATM 3881 O HOH A 774 -4.957 -19.203 -9.175 1.00 69.87 O ANISOU 3881 O HOH A 774 5371 9880 11296 180 -775 -1073 O HETATM 3882 O HOH A 775 -3.040 -16.957 -9.443 1.00 67.21 O ANISOU 3882 O HOH A 775 4154 9342 12040 -189 -742 -1123 O HETATM 3883 O HOH A 776 -26.740 -23.334 13.918 1.00 92.54 O ANISOU 3883 O HOH A 776 16968 11260 6932 3773 3069 977 O HETATM 3884 O HOH A 777 -4.907 -40.669 -28.358 1.00 87.05 O ANISOU 3884 O HOH A 777 11373 12161 9543 4445 2463 -3462 O HETATM 3885 O HOH A 778 -18.275 -31.205 -6.986 1.00 42.74 O ANISOU 3885 O HOH A 778 5401 5250 5590 613 291 -735 O HETATM 3886 O HOH A 779 -33.958 -17.573 -4.598 1.00 80.26 O ANISOU 3886 O HOH A 779 8729 10389 11377 6 1504 -644 O HETATM 3887 O HOH A 780 -3.543 -25.921 -11.899 1.00 74.50 O ANISOU 3887 O HOH A 780 6171 10826 11312 1242 -69 -1005 O HETATM 3888 O HOH A 781 -27.450 -18.308 -22.641 1.00 71.00 O ANISOU 3888 O HOH A 781 8251 11098 7627 1129 -1094 -1160 O HETATM 3889 O HOH A 782 -20.077 -13.749 -12.518 1.00 64.34 O ANISOU 3889 O HOH A 782 7020 9010 8417 -154 107 -316 O HETATM 3890 O HOH A 783 -0.945 -28.027 4.329 1.00 98.73 O ANISOU 3890 O HOH A 783 11520 13588 12407 3830 -4864 -1844 O HETATM 3891 O HOH A 784 -9.313 -25.852 -18.313 1.00 67.83 O ANISOU 3891 O HOH A 784 6821 10260 8693 1117 1102 -846 O HETATM 3892 O HOH A 785 -35.697 -15.998 -2.566 1.00 74.08 O ANISOU 3892 O HOH A 785 8008 9486 10652 287 2094 -552 O HETATM 3893 O HOH A 786 -23.153 -14.078 -15.185 1.00 76.99 O ANISOU 3893 O HOH A 786 8733 10893 9626 124 56 -262 O HETATM 3894 O HOH A 787 -4.081 -38.260 -28.293 1.00 93.22 O ANISOU 3894 O HOH A 787 11688 13416 10315 4300 2871 -2875 O HETATM 3895 O HOH A 788 -8.050 -22.722 -17.657 1.00 74.44 O ANISOU 3895 O HOH A 788 7092 11081 10109 765 1262 -464 O HETATM 3896 O HOH A 789 -22.865 -23.204 14.587 1.00104.76 O ANISOU 3896 O HOH A 789 18877 13146 7782 4257 1318 451 O CONECT 3295 3777 CONECT 3735 3739 3766 CONECT 3736 3742 3749 CONECT 3737 3752 3756 CONECT 3738 3759 3763 CONECT 3739 3735 3740 3773 CONECT 3740 3739 3741 3744 CONECT 3741 3740 3742 3743 CONECT 3742 3736 3741 3773 CONECT 3743 3741 CONECT 3744 3740 3745 CONECT 3745 3744 3746 CONECT 3746 3745 3747 3748 CONECT 3747 3746 CONECT 3748 3746 CONECT 3749 3736 3750 3774 CONECT 3750 3749 3751 3753 CONECT 3751 3750 3752 3754 CONECT 3752 3737 3751 3774 CONECT 3753 3750 CONECT 3754 3751 3755 CONECT 3755 3754 CONECT 3756 3737 3757 3775 CONECT 3757 3756 3758 3760 CONECT 3758 3757 3759 3761 CONECT 3759 3738 3758 3775 CONECT 3760 3757 CONECT 3761 3758 3762 CONECT 3762 3761 CONECT 3763 3738 3764 3776 CONECT 3764 3763 3765 3767 CONECT 3765 3764 3766 3768 CONECT 3766 3735 3765 3776 CONECT 3767 3764 CONECT 3768 3765 3769 CONECT 3769 3768 3770 CONECT 3770 3769 3771 3772 CONECT 3771 3770 CONECT 3772 3770 CONECT 3773 3739 3742 3777 CONECT 3774 3749 3752 3777 CONECT 3775 3756 3759 3777 CONECT 3776 3763 3766 3777 CONECT 3777 3295 3773 3774 3775 CONECT 3777 3776 3791 CONECT 3778 3779 CONECT 3779 3778 3780 3781 3782 CONECT 3780 3779 3783 CONECT 3781 3779 3788 CONECT 3782 3779 3793 3794 CONECT 3783 3780 3784 3785 CONECT 3784 3783 3786 CONECT 3785 3783 3787 CONECT 3786 3784 3787 CONECT 3787 3785 3786 CONECT 3788 3781 3789 3790 CONECT 3789 3788 3791 CONECT 3790 3788 3792 CONECT 3791 3777 3789 3792 CONECT 3792 3790 3791 CONECT 3793 3782 3795 CONECT 3794 3782 3798 3799 CONECT 3795 3793 3796 CONECT 3796 3795 3797 3798 CONECT 3797 3796 CONECT 3798 3794 3796 CONECT 3799 3794 CONECT 3800 3801 3802 3803 CONECT 3801 3800 CONECT 3802 3800 CONECT 3803 3800 CONECT 3804 3805 3806 CONECT 3805 3804 CONECT 3806 3804 3807 CONECT 3807 3806 MASTER 341 0 4 22 9 0 12 6 3882 1 75 38 END If you find results from this site helpful for 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