HEADER MEMBRANE PROTEIN/INHIBITOR 23-MAR-18 5ZKB TITLE CRYSTAL STRUCTURE OF RATIONALLY THERMOSTABILIZED M2 MUSCARINIC TITLE 2 ACETYLCHOLINE RECEPTOR BOUND WITH AF-DX 384 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M2,APO-CYTOCHROME B562, COMPND 3 MUSCARINIC ACETYLCHOLINE RECEPTOR M2; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: UNP RESIDUES 10-217,UNP RESIDUES 377-466; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CHRM2; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR CRYSTALLOGRAPHY, RATIONALLY THERMOSTABILIZED MUTANT, MEMBRANE KEYWDS 2 PROTEIN-INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR R.SUNO,S.MAEDA,S.YASUDA,K.YAMASHITA,K.HIRATA,S.HORITA,M.S.TAWARAMOTO, AUTHOR 2 H.TSUJIMOTO,T.MURATA,M.KINOSHITA,M.YAMAMOTO,B.K.KOBILKA,S.IWATA, AUTHOR 3 T.KOBAYASHI REVDAT 3 23-MAR-22 5ZKB 1 REMARK REVDAT 2 28-NOV-18 5ZKB 1 JRNL REVDAT 1 21-NOV-18 5ZKB 0 JRNL AUTH R.SUNO,S.LEE,S.MAEDA,S.YASUDA,K.YAMASHITA,K.HIRATA,S.HORITA, JRNL AUTH 2 M.S.TAWARAMOTO,H.TSUJIMOTO,T.MURATA,M.KINOSHITA,M.YAMAMOTO, JRNL AUTH 3 B.K.KOBILKA,N.VAIDEHI,S.IWATA,T.KOBAYASHI JRNL TITL STRUCTURAL INSIGHTS INTO THE SUBTYPE-SELECTIVE ANTAGONIST JRNL TITL 2 BINDING TO THE M2MUSCARINIC RECEPTOR JRNL REF NAT. CHEM. BIOL. V. 14 1150 2018 JRNL REFN ESSN 1552-4469 JRNL PMID 30420692 JRNL DOI 10.1038/S41589-018-0152-Y REMARK 2 REMARK 2 RESOLUTION. 2.95 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) : 2.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.70 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 13188 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.232 REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 661 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 48.7040 - 5.0430 1.00 2572 134 0.2127 0.2366 REMARK 3 2 5.0430 - 4.0034 1.00 2505 129 0.2151 0.2871 REMARK 3 3 4.0034 - 3.4975 1.00 2476 129 0.2199 0.2572 REMARK 3 4 3.4975 - 3.1778 1.00 2488 133 0.2535 0.3105 REMARK 3 5 3.1778 - 2.9500 1.00 2486 136 0.2809 0.3401 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) : 0.420 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.220 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 : 0.002 3137 REMARK 3 ANGLE : 0.475 4275 REMARK 3 CHIRALITY : 0.037 503 REMARK 3 PLANARITY : 0.003 530 REMARK 3 DIHEDRAL : 12.739 1870 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 1081 THROUGH 1106 ) OR (RESID REMARK 3 377 THROUGH 381 )) REMARK 3 ORIGIN FOR THE GROUP (A): -11.6449 -1.8938 -5.4231 REMARK 3 T TENSOR REMARK 3 T11: 0.6269 T22: 1.7009 REMARK 3 T33: 0.7486 T12: 0.1381 REMARK 3 T13: -0.1798 T23: -0.1932 REMARK 3 L TENSOR REMARK 3 L11: 1.4420 L22: 3.5674 REMARK 3 L33: 0.4002 L12: 1.7204 REMARK 3 L13: -0.3841 L23: 0.2124 REMARK 3 S TENSOR REMARK 3 S11: 0.5227 S12: -0.0794 S13: -0.6153 REMARK 3 S21: 0.6806 S22: -0.2751 S23: -0.7937 REMARK 3 S31: 0.0667 S32: 1.1270 S33: -0.2890 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 382 THROUGH 456 ) REMARK 3 ORIGIN FOR THE GROUP (A): -46.687 -13.760 2.333 REMARK 3 T TENSOR REMARK 3 T11: 0.1686 T22: 0.1801 REMARK 3 T33: 0.0472 T12: -0.0786 REMARK 3 T13: -0.0488 T23: 0.0235 REMARK 3 L TENSOR REMARK 3 L11: 2.3177 L22: 1.7366 REMARK 3 L33: 2.0045 L12: -0.0367 REMARK 3 L13: 0.8702 L23: 0.2273 REMARK 3 S TENSOR REMARK 3 S11: -0.1327 S12: 0.3117 S13: -0.0785 REMARK 3 S21: -0.1297 S22: 0.2373 S23: -0.0971 REMARK 3 S31: -0.0460 S32: 0.1332 S33: -0.0379 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 195 ) REMARK 3 ORIGIN FOR THE GROUP (A): -51.2556 -21.6641 9.7515 REMARK 3 T TENSOR REMARK 3 T11: 0.0774 T22: 0.0945 REMARK 3 T33: 0.0817 T12: -0.0060 REMARK 3 T13: -0.0337 T23: 0.0482 REMARK 3 L TENSOR REMARK 3 L11: 1.3281 L22: 1.3152 REMARK 3 L33: 1.1204 L12: 0.4096 REMARK 3 L13: -0.0834 L23: 0.2815 REMARK 3 S TENSOR REMARK 3 S11: 0.0098 S12: -0.2547 S13: -0.0319 REMARK 3 S21: 0.0942 S22: 0.1557 S23: -0.0837 REMARK 3 S31: 0.0469 S32: 0.1277 S33: -0.0629 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 196 THROUGH 217) OR (RESID REMARK 3 1001 THROUGH 1002 )) REMARK 3 ORIGIN FOR THE GROUP (A): -37.2529 -0.6222 14.1738 REMARK 3 T TENSOR REMARK 3 T11: 0.3626 T22: 0.4490 REMARK 3 T33: 0.3770 T12: -0.0002 REMARK 3 T13: -0.1453 T23: -0.1878 REMARK 3 L TENSOR REMARK 3 L11: 4.6892 L22: 2.4850 REMARK 3 L33: 5.5066 L12: -1.6168 REMARK 3 L13: 3.3771 L23: -1.1453 REMARK 3 S TENSOR REMARK 3 S11: -0.3776 S12: 0.3534 S13: 0.6543 REMARK 3 S21: 0.0190 S22: 0.0214 S23: -0.6526 REMARK 3 S31: -0.7640 S32: 1.1446 S33: 0.2253 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1003 THROUGH 1080 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.7325 5.2381 -4.4450 REMARK 3 T TENSOR REMARK 3 T11: 0.2970 T22: 1.0578 REMARK 3 T33: 0.4788 T12: -0.1618 REMARK 3 T13: -0.0892 T23: -0.1284 REMARK 3 L TENSOR REMARK 3 L11: 3.8624 L22: 2.7302 REMARK 3 L33: 3.6060 L12: 0.2986 REMARK 3 L13: 3.7108 L23: 0.5887 REMARK 3 S TENSOR REMARK 3 S11: 0.1163 S12: -1.3609 S13: 0.0745 REMARK 3 S21: 0.6645 S22: -0.0864 S23: -0.0880 REMARK 3 S31: -0.0591 S32: -0.3177 S33: 0.0030 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 5ZKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAR-18. REMARK 100 THE DEPOSITION ID IS D_1300007231. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-OCT-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL32XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225-HS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13188 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 18.10 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.13 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES-NAOH PH 6.2-7.0, 18 % PEG300, REMARK 280 100MM MAGNESIUM ACETATE, 1% 1,2,3-HEPTANETRIOL, 0.5MM AF-DX 384 REMARK 280 AND 5% DMSO, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 106.50500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.04500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 106.50500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.04500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 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: MONOMERIC 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -1 REMARK 465 PRO A 0 REMARK 465 MET A 1 REMARK 465 ASP A 2 REMARK 465 ASP A 3 REMARK 465 SER A 4 REMARK 465 THR A 5 REMARK 465 ASP A 6 REMARK 465 SER A 7 REMARK 465 SER A 8 REMARK 465 ASP A 9 REMARK 465 ASN A 10 REMARK 465 SER A 11 REMARK 465 LEU A 12 REMARK 465 ALA A 13 REMARK 465 LEU A 14 REMARK 465 THR A 15 REMARK 465 SER A 16 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 CYS A 457 REMARK 465 HIS A 458 REMARK 465 TYR A 459 REMARK 465 LYS A 460 REMARK 465 ASN A 461 REMARK 465 ILE A 462 REMARK 465 GLY A 463 REMARK 465 ALA A 464 REMARK 465 THR A 465 REMARK 465 ARG A 466 REMARK 465 LEU A 467 REMARK 465 GLU A 468 REMARK 465 VAL A 469 REMARK 465 LEU A 470 REMARK 465 PHE A 471 REMARK 465 GLN A 472 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ILE A 217 N GLU A 1004 2.18 REMARK 500 REMARK 500 REMARK: NULL 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 GLN A 55 44.10 -108.21 REMARK 500 PHE A 75 -61.36 -104.84 REMARK 500 PHE A 195 -61.56 -133.19 REMARK 500 ARG A 216 -141.78 70.60 REMARK 500 LYS A1042 21.74 -78.68 REMARK 500 GLU A1057 9.83 58.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 82F A 1201 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5ZK8 RELATED DB: PDB REMARK 900 RELATED ID: 5ZK3 RELATED DB: PDB DBREF 5ZKB A 10 217 UNP P08172 ACM2_HUMAN 10 217 DBREF 5ZKB A 1001 1106 PDB 5ZKB 5ZKB 1001 1106 DBREF 5ZKB A 377 466 UNP P08172 ACM2_HUMAN 377 466 SEQADV 5ZKB GLY A -1 UNP P08172 EXPRESSION TAG SEQADV 5ZKB PRO A 0 UNP P08172 EXPRESSION TAG SEQADV 5ZKB MET A 1 UNP P08172 EXPRESSION TAG SEQADV 5ZKB ASP A 2 UNP P08172 EXPRESSION TAG SEQADV 5ZKB ASP A 3 UNP P08172 EXPRESSION TAG SEQADV 5ZKB SER A 4 UNP P08172 EXPRESSION TAG SEQADV 5ZKB THR A 5 UNP P08172 EXPRESSION TAG SEQADV 5ZKB ASP A 6 UNP P08172 EXPRESSION TAG SEQADV 5ZKB SER A 7 UNP P08172 EXPRESSION TAG SEQADV 5ZKB SER A 8 UNP P08172 EXPRESSION TAG SEQADV 5ZKB ASP A 9 UNP P08172 EXPRESSION TAG SEQADV 5ZKB ARG A 110 UNP P08172 SER 110 ENGINEERED MUTATION SEQADV 5ZKB LEU A 467 UNP P08172 EXPRESSION TAG SEQADV 5ZKB GLU A 468 UNP P08172 EXPRESSION TAG SEQADV 5ZKB VAL A 469 UNP P08172 EXPRESSION TAG SEQADV 5ZKB LEU A 470 UNP P08172 EXPRESSION TAG SEQADV 5ZKB PHE A 471 UNP P08172 EXPRESSION TAG SEQADV 5ZKB GLN A 472 UNP P08172 EXPRESSION TAG SEQRES 1 A 421 GLY PRO MET ASP ASP SER THR ASP SER SER ASP ASN SER SEQRES 2 A 421 LEU ALA LEU THR SER PRO TYR LYS THR PHE GLU VAL VAL SEQRES 3 A 421 PHE ILE VAL LEU VAL ALA GLY SER LEU SER LEU VAL THR SEQRES 4 A 421 ILE ILE GLY ASN ILE LEU VAL MET VAL SER ILE LYS VAL SEQRES 5 A 421 ASN ARG HIS LEU GLN THR VAL ASN ASN TYR PHE LEU PHE SEQRES 6 A 421 SER LEU ALA CYS ALA ASP LEU ILE ILE GLY VAL PHE SER SEQRES 7 A 421 MET ASN LEU TYR THR LEU TYR THR VAL ILE GLY TYR TRP SEQRES 8 A 421 PRO LEU GLY PRO VAL VAL CYS ASP LEU TRP LEU ALA LEU SEQRES 9 A 421 ASP TYR VAL VAL SER ASN ALA ARG VAL MET ASN LEU LEU SEQRES 10 A 421 ILE ILE SER PHE ASP ARG TYR PHE CYS VAL THR LYS PRO SEQRES 11 A 421 LEU THR TYR PRO VAL LYS ARG THR THR LYS MET ALA GLY SEQRES 12 A 421 MET MET ILE ALA ALA ALA TRP VAL LEU SER PHE ILE LEU SEQRES 13 A 421 TRP ALA PRO ALA ILE LEU PHE TRP GLN PHE ILE VAL GLY SEQRES 14 A 421 VAL ARG THR VAL GLU ASP GLY GLU CYS TYR ILE GLN PHE SEQRES 15 A 421 PHE SER ASN ALA ALA VAL THR PHE GLY THR ALA ILE ALA SEQRES 16 A 421 ALA PHE TYR LEU PRO VAL ILE ILE MET THR VAL LEU TYR SEQRES 17 A 421 TRP HIS ILE SER ARG ALA SER LYS SER ARG ILE ALA ASP SEQRES 18 A 421 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 19 A 421 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 20 A 421 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 21 A 421 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 22 A 421 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 23 A 421 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 24 A 421 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 25 A 421 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 26 A 421 PRO PRO PRO SER ARG GLU LYS LYS VAL THR ARG THR ILE SEQRES 27 A 421 LEU ALA ILE LEU LEU ALA PHE ILE ILE THR TRP ALA PRO SEQRES 28 A 421 TYR ASN VAL MET VAL LEU ILE ASN THR PHE CYS ALA PRO SEQRES 29 A 421 CYS ILE PRO ASN THR VAL TRP THR ILE GLY TYR TRP LEU SEQRES 30 A 421 CYS TYR ILE ASN SER THR ILE ASN PRO ALA CYS TYR ALA SEQRES 31 A 421 LEU CYS ASN ALA THR PHE LYS LYS THR PHE LYS HIS LEU SEQRES 32 A 421 LEU MET CYS HIS TYR LYS ASN ILE GLY ALA THR ARG LEU SEQRES 33 A 421 GLU VAL LEU PHE GLN HET 82F A1201 35 HETNAM 82F N-[2-[(2S)-2-[(DIPROPYLAMINO)METHYL]PIPERIDIN-1- HETNAM 2 82F YL]ETHYL]-6-OXIDANYLIDENE-5H-PYRIDO[2,3-B][1, HETNAM 3 82F 4]BENZODIAZEPINE-11-CARBOXAMIDE FORMUL 2 82F C27 H38 N6 O2 HELIX 1 AA1 TYR A 18 ASN A 51 1 34 HELIX 2 AA2 THR A 56 PHE A 75 1 20 HELIX 3 AA3 PHE A 75 GLY A 87 1 13 HELIX 4 AA4 GLY A 92 LYS A 127 1 36 HELIX 5 AA5 TYR A 131 ARG A 135 5 5 HELIX 6 AA6 THR A 136 VAL A 166 1 31 HELIX 7 AA7 GLN A 179 SER A 182 5 4 HELIX 8 AA8 ASN A 183 PHE A 195 1 13 HELIX 9 AA9 PHE A 195 SER A 213 1 19 HELIX 10 AB1 ARG A 216 LYS A 1019 1 21 HELIX 11 AB2 ASN A 1022 LYS A 1042 1 21 HELIX 12 AB3 MET A 1058 GLU A 1081 1 24 HELIX 13 AB4 LYS A 1083 LEU A 1106 1 24 HELIX 14 AB5 SER A 380 THR A 411 1 32 HELIX 15 AB6 PRO A 418 ALA A 441 1 24 HELIX 16 AB7 ASN A 444 MET A 456 1 13 SSBOND 1 CYS A 96 CYS A 176 1555 1555 2.04 SSBOND 2 CYS A 413 CYS A 416 1555 1555 2.03 SITE 1 AC1 16 TRP A 99 LEU A 100 ASP A 103 TYR A 104 SITE 2 AC1 16 SER A 107 ASN A 108 THR A 190 ALA A 191 SITE 3 AC1 16 ALA A 194 PHE A 195 TRP A 400 TYR A 403 SITE 4 AC1 16 ASN A 404 TYR A 426 CYS A 429 TYR A 430 CRYST1 213.010 60.090 48.750 90.00 92.66 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.004695 0.000000 0.000218 0.00000 SCALE2 0.000000 0.016642 0.000000 0.00000 SCALE3 0.000000 0.000000 0.020535 0.00000 ATOM 1 N PRO A 17 -70.242 -20.656 -20.629 1.00 70.16 N ANISOU 1 N PRO A 17 9487 9097 8075 -921 -1498 861 N ATOM 2 CA PRO A 17 -69.644 -20.185 -21.885 1.00 77.53 C ANISOU 2 CA PRO A 17 10521 10078 8859 -962 -1505 885 C ATOM 3 C PRO A 17 -68.122 -20.171 -21.826 1.00 83.70 C ANISOU 3 C PRO A 17 11374 10841 9586 -1005 -1389 858 C ATOM 4 O PRO A 17 -67.473 -21.098 -22.308 1.00 79.89 O ANISOU 4 O PRO A 17 10938 10403 9015 -1072 -1348 785 O ATOM 5 CB PRO A 17 -70.196 -18.763 -22.027 1.00 78.48 C ANISOU 5 CB PRO A 17 10636 10177 9005 -893 -1564 985 C ATOM 6 CG PRO A 17 -71.462 -18.771 -21.239 1.00 81.02 C ANISOU 6 CG PRO A 17 10847 10477 9461 -825 -1626 996 C ATOM 7 CD PRO A 17 -71.215 -19.694 -20.083 1.00 71.38 C ANISOU 7 CD PRO A 17 9569 9219 8336 -835 -1551 929 C ATOM 8 N TYR A 18 -67.561 -19.118 -21.236 1.00 86.53 N ANISOU 8 N TYR A 18 11737 11140 10001 -966 -1336 907 N ATOM 9 CA TYR A 18 -66.120 -19.011 -21.061 1.00 84.59 C ANISOU 9 CA TYR A 18 11542 10877 9720 -1001 -1226 880 C ATOM 10 C TYR A 18 -65.629 -19.657 -19.773 1.00 68.86 C ANISOU 10 C TYR A 18 9497 8836 7830 -987 -1151 821 C ATOM 11 O TYR A 18 -64.415 -19.806 -19.598 1.00 66.48 O ANISOU 11 O TYR A 18 9230 8531 7499 -1019 -1062 783 O ATOM 12 CB TYR A 18 -65.690 -17.537 -21.078 1.00 86.70 C ANISOU 12 CB TYR A 18 11841 11107 9995 -970 -1208 956 C ATOM 13 CG TYR A 18 -65.709 -16.875 -19.714 1.00 88.07 C ANISOU 13 CG TYR A 18 11948 11198 10318 -895 -1174 967 C ATOM 14 CD1 TYR A 18 -64.525 -16.603 -19.036 1.00 86.21 C ANISOU 14 CD1 TYR A 18 11719 10927 10110 -899 -1077 939 C ATOM 15 CD2 TYR A 18 -66.908 -16.528 -19.102 1.00 89.33 C ANISOU 15 CD2 TYR A 18 12033 11323 10585 -818 -1239 999 C ATOM 16 CE1 TYR A 18 -64.534 -16.002 -17.790 1.00 84.98 C ANISOU 16 CE1 TYR A 18 11503 10706 10079 -829 -1047 940 C ATOM 17 CE2 TYR A 18 -66.927 -15.926 -17.856 1.00 86.64 C ANISOU 17 CE2 TYR A 18 11633 10916 10369 -748 -1202 999 C ATOM 18 CZ TYR A 18 -65.738 -15.666 -17.204 1.00 84.70 C ANISOU 18 CZ TYR A 18 11401 10639 10143 -754 -1107 968 C ATOM 19 OH TYR A 18 -65.754 -15.068 -15.965 1.00 78.86 O ANISOU 19 OH TYR A 18 10605 9842 9516 -684 -1072 961 O ATOM 20 N LYS A 19 -66.536 -20.051 -18.877 1.00 62.58 N ANISOU 20 N LYS A 19 8619 8009 7151 -941 -1185 815 N ATOM 21 CA LYS A 19 -66.136 -20.501 -17.550 1.00 64.63 C ANISOU 21 CA LYS A 19 8827 8216 7512 -918 -1119 777 C ATOM 22 C LYS A 19 -65.466 -21.869 -17.552 1.00 62.23 C ANISOU 22 C LYS A 19 8549 7931 7164 -976 -1073 699 C ATOM 23 O LYS A 19 -64.891 -22.249 -16.527 1.00 73.39 O ANISOU 23 O LYS A 19 9937 9305 8643 -961 -1013 670 O ATOM 24 CB LYS A 19 -67.346 -20.518 -16.614 1.00 65.81 C ANISOU 24 CB LYS A 19 8879 8334 7790 -856 -1165 798 C ATOM 25 CG LYS A 19 -68.112 -19.205 -16.585 1.00 66.44 C ANISOU 25 CG LYS A 19 8929 8397 7919 -787 -1214 866 C ATOM 26 CD LYS A 19 -68.734 -18.945 -15.221 1.00 66.10 C ANISOU 26 CD LYS A 19 8793 8309 8015 -713 -1201 872 C ATOM 27 CE LYS A 19 -67.667 -18.649 -14.177 1.00 63.18 C ANISOU 27 CE LYS A 19 8420 7895 7689 -691 -1103 844 C ATOM 28 NZ LYS A 19 -68.254 -18.287 -12.857 1.00 59.14 N ANISOU 28 NZ LYS A 19 7823 7350 7298 -616 -1086 847 N ATOM 29 N THR A 20 -65.520 -22.612 -18.660 1.00 45.72 N ANISOU 29 N THR A 20 6508 5901 4962 -1036 -1101 658 N ATOM 30 CA THR A 20 -64.818 -23.892 -18.730 1.00 39.66 C ANISOU 30 CA THR A 20 5772 5152 4147 -1086 -1052 565 C ATOM 31 C THR A 20 -63.307 -23.684 -18.697 1.00 53.91 C ANISOU 31 C THR A 20 7630 6958 5896 -1108 -950 537 C ATOM 32 O THR A 20 -62.601 -24.239 -17.840 1.00 60.39 O ANISOU 32 O THR A 20 8438 7745 6762 -1100 -890 493 O ATOM 33 CB THR A 20 -65.230 -24.645 -19.995 1.00 35.11 C ANISOU 33 CB THR A 20 5235 4648 3459 -1141 -1103 507 C ATOM 34 OG1 THR A 20 -66.642 -24.886 -19.971 1.00 27.47 O ANISOU 34 OG1 THR A 20 4204 3682 2551 -1122 -1200 525 O ATOM 35 CG2 THR A 20 -64.490 -25.972 -20.094 1.00 37.04 C ANISOU 35 CG2 THR A 20 5508 4904 3660 -1185 -1046 385 C ATOM 36 N PHE A 21 -62.794 -22.879 -19.631 1.00 51.33 N ANISOU 36 N PHE A 21 7361 6674 5468 -1137 -932 563 N ATOM 37 CA PHE A 21 -61.382 -22.523 -19.605 1.00 51.67 C ANISOU 37 CA PHE A 21 7442 6725 5465 -1161 -833 544 C ATOM 38 C PHE A 21 -61.014 -21.819 -18.307 1.00 47.86 C ANISOU 38 C PHE A 21 6908 6172 5105 -1103 -796 580 C ATOM 39 O PHE A 21 -59.871 -21.918 -17.850 1.00 57.15 O ANISOU 39 O PHE A 21 8091 7344 6280 -1112 -713 541 O ATOM 40 CB PHE A 21 -61.042 -21.645 -20.810 1.00 49.48 C ANISOU 40 CB PHE A 21 7229 6503 5068 -1202 -828 584 C ATOM 41 CG PHE A 21 -61.696 -22.092 -22.086 1.00 52.12 C ANISOU 41 CG PHE A 21 7606 6910 5286 -1244 -890 567 C ATOM 42 CD1 PHE A 21 -62.834 -21.455 -22.556 1.00 51.77 C ANISOU 42 CD1 PHE A 21 7557 6869 5243 -1220 -992 645 C ATOM 43 CD2 PHE A 21 -61.181 -23.155 -22.809 1.00 47.04 C ANISOU 43 CD2 PHE A 21 7005 6335 4533 -1300 -847 462 C ATOM 44 CE1 PHE A 21 -63.442 -21.864 -23.728 1.00 42.49 C ANISOU 44 CE1 PHE A 21 6420 5770 3956 -1256 -1057 627 C ATOM 45 CE2 PHE A 21 -61.785 -23.570 -23.981 1.00 38.36 C ANISOU 45 CE2 PHE A 21 5942 5308 3324 -1336 -906 434 C ATOM 46 CZ PHE A 21 -62.916 -22.923 -24.441 1.00 39.95 C ANISOU 46 CZ PHE A 21 6141 5518 3522 -1316 -1015 520 C ATOM 47 N GLU A 22 -61.967 -21.110 -17.697 1.00 37.14 N ANISOU 47 N GLU A 22 5494 4765 3853 -1040 -855 644 N ATOM 48 CA GLU A 22 -61.711 -20.517 -16.390 1.00 43.08 C ANISOU 48 CA GLU A 22 6188 5457 4723 -975 -820 658 C ATOM 49 C GLU A 22 -61.464 -21.593 -15.342 1.00 43.73 C ANISOU 49 C GLU A 22 6233 5514 4869 -962 -788 605 C ATOM 50 O GLU A 22 -60.542 -21.475 -14.528 1.00 51.66 O ANISOU 50 O GLU A 22 7220 6498 5909 -939 -723 581 O ATOM 51 CB GLU A 22 -62.879 -19.624 -15.973 1.00 51.57 C ANISOU 51 CB GLU A 22 7207 6495 5892 -905 -884 719 C ATOM 52 CG GLU A 22 -62.551 -18.700 -14.810 1.00 66.04 C ANISOU 52 CG GLU A 22 8991 8278 7822 -835 -842 727 C ATOM 53 CD GLU A 22 -63.774 -18.317 -14.003 1.00 78.95 C ANISOU 53 CD GLU A 22 10551 9879 9567 -760 -888 756 C ATOM 54 OE1 GLU A 22 -64.527 -19.228 -13.601 1.00 80.59 O ANISOU 54 OE1 GLU A 22 10713 10087 9819 -757 -916 742 O ATOM 55 OE2 GLU A 22 -63.984 -17.106 -13.776 1.00 84.86 O ANISOU 55 OE2 GLU A 22 11289 10599 10354 -708 -895 794 O ATOM 56 N VAL A 23 -62.274 -22.654 -15.347 1.00 34.84 N ANISOU 56 N VAL A 23 5093 4390 3756 -974 -836 587 N ATOM 57 CA VAL A 23 -62.074 -23.744 -14.395 1.00 27.78 C ANISOU 57 CA VAL A 23 4173 3465 2917 -966 -814 545 C ATOM 58 C VAL A 23 -60.720 -24.406 -14.624 1.00 34.45 C ANISOU 58 C VAL A 23 5076 4334 3677 -1008 -742 474 C ATOM 59 O VAL A 23 -59.954 -24.634 -13.677 1.00 41.52 O ANISOU 59 O VAL A 23 5958 5203 4615 -984 -694 454 O ATOM 60 CB VAL A 23 -63.227 -24.762 -14.486 1.00 30.81 C ANISOU 60 CB VAL A 23 4531 3847 3327 -978 -883 534 C ATOM 61 CG1 VAL A 23 -62.935 -25.976 -13.617 1.00 28.05 C ANISOU 61 CG1 VAL A 23 4166 3463 3029 -975 -861 483 C ATOM 62 CG2 VAL A 23 -64.538 -24.121 -14.063 1.00 30.88 C ANISOU 62 CG2 VAL A 23 4467 3837 3431 -931 -943 602 C ATOM 63 N VAL A 24 -60.399 -24.717 -15.886 1.00 36.61 N ANISOU 63 N VAL A 24 5414 4669 3829 -1068 -730 425 N ATOM 64 CA VAL A 24 -59.112 -25.347 -16.188 1.00 33.53 C ANISOU 64 CA VAL A 24 5069 4314 3356 -1107 -648 330 C ATOM 65 C VAL A 24 -57.960 -24.463 -15.723 1.00 34.43 C ANISOU 65 C VAL A 24 5184 4429 3469 -1097 -571 355 C ATOM 66 O VAL A 24 -56.984 -24.941 -15.126 1.00 35.24 O ANISOU 66 O VAL A 24 5285 4529 3575 -1091 -508 294 O ATOM 67 CB VAL A 24 -59.008 -25.660 -17.692 1.00 25.58 C ANISOU 67 CB VAL A 24 4120 3383 2215 -1169 -638 269 C ATOM 68 CG1 VAL A 24 -57.687 -26.356 -17.998 1.00 18.87 C ANISOU 68 CG1 VAL A 24 3302 2574 1292 -1200 -537 144 C ATOM 69 CG2 VAL A 24 -60.184 -26.508 -18.142 1.00 22.95 C ANISOU 69 CG2 VAL A 24 3778 3050 1891 -1176 -719 238 C ATOM 70 N PHE A 25 -58.059 -23.160 -15.987 1.00 32.34 N ANISOU 70 N PHE A 25 4914 4164 3209 -1090 -578 430 N ATOM 71 CA PHE A 25 -57.044 -22.222 -15.522 1.00 31.51 C ANISOU 71 CA PHE A 25 4794 4051 3126 -1075 -512 447 C ATOM 72 C PHE A 25 -56.941 -22.240 -14.002 1.00 27.90 C ANISOU 72 C PHE A 25 4272 3536 2793 -1001 -504 452 C ATOM 73 O PHE A 25 -55.839 -22.170 -13.444 1.00 23.72 O ANISOU 73 O PHE A 25 3731 3011 2272 -994 -432 425 O ATOM 74 CB PHE A 25 -57.379 -20.820 -16.032 1.00 34.57 C ANISOU 74 CB PHE A 25 5186 4436 3514 -1067 -542 519 C ATOM 75 CG PHE A 25 -56.318 -19.800 -15.753 1.00 42.83 C ANISOU 75 CG PHE A 25 6226 5478 4570 -1063 -477 529 C ATOM 76 CD1 PHE A 25 -55.228 -19.667 -16.599 1.00 45.61 C ANISOU 76 CD1 PHE A 25 6626 5889 4816 -1137 -403 504 C ATOM 77 CD2 PHE A 25 -56.415 -18.964 -14.652 1.00 45.74 C ANISOU 77 CD2 PHE A 25 6537 5791 5051 -986 -485 557 C ATOM 78 CE1 PHE A 25 -54.249 -18.724 -16.348 1.00 52.34 C ANISOU 78 CE1 PHE A 25 7469 6738 5681 -1142 -343 516 C ATOM 79 CE2 PHE A 25 -55.441 -18.018 -14.395 1.00 53.91 C ANISOU 79 CE2 PHE A 25 7569 6820 6095 -985 -430 564 C ATOM 80 CZ PHE A 25 -54.355 -17.898 -15.245 1.00 58.73 C ANISOU 80 CZ PHE A 25 8226 7483 6605 -1067 -361 547 C ATOM 81 N ILE A 26 -58.081 -22.362 -13.320 1.00 31.12 N ANISOU 81 N ILE A 26 4628 3897 3297 -945 -571 483 N ATOM 82 CA ILE A 26 -58.095 -22.351 -11.861 1.00 29.39 C ANISOU 82 CA ILE A 26 4338 3635 3195 -864 -561 484 C ATOM 83 C ILE A 26 -57.361 -23.566 -11.310 1.00 30.63 C ANISOU 83 C ILE A 26 4508 3781 3349 -873 -519 441 C ATOM 84 O ILE A 26 -56.478 -23.439 -10.452 1.00 39.65 O ANISOU 84 O ILE A 26 5617 4911 4538 -831 -460 425 O ATOM 85 CB ILE A 26 -59.542 -22.279 -11.341 1.00 25.66 C ANISOU 85 CB ILE A 26 3805 3132 2814 -813 -630 519 C ATOM 86 CG1 ILE A 26 -60.088 -20.856 -11.480 1.00 24.12 C ANISOU 86 CG1 ILE A 26 3587 2933 2646 -776 -651 563 C ATOM 87 CG2 ILE A 26 -59.622 -22.747 -9.895 1.00 22.31 C ANISOU 87 CG2 ILE A 26 3312 2679 2488 -741 -612 505 C ATOM 88 CD1 ILE A 26 -61.560 -20.725 -11.139 1.00 28.27 C ANISOU 88 CD1 ILE A 26 4057 3439 3246 -737 -713 598 C ATOM 89 N VAL A 27 -57.705 -24.763 -11.794 1.00 21.90 N ANISOU 89 N VAL A 27 3442 2677 2200 -918 -548 408 N ATOM 90 CA VAL A 27 -57.071 -25.962 -11.253 1.00 16.29 C ANISOU 90 CA VAL A 27 2694 1933 1561 -881 -489 314 C ATOM 91 C VAL A 27 -55.587 -25.993 -11.606 1.00 13.52 C ANISOU 91 C VAL A 27 2354 1622 1162 -892 -392 234 C ATOM 92 O VAL A 27 -54.756 -26.419 -10.795 1.00 26.71 O ANISOU 92 O VAL A 27 3975 3265 2909 -836 -335 189 O ATOM 93 CB VAL A 27 -57.805 -27.234 -11.723 1.00 21.98 C ANISOU 93 CB VAL A 27 3424 2634 2293 -905 -532 252 C ATOM 94 CG1 VAL A 27 -59.228 -27.255 -11.184 1.00 12.79 C ANISOU 94 CG1 VAL A 27 2224 1434 1200 -892 -618 328 C ATOM 95 CG2 VAL A 27 -57.804 -27.347 -13.240 1.00 35.25 C ANISOU 95 CG2 VAL A 27 5175 4382 3837 -985 -545 196 C ATOM 96 N LEU A 28 -55.223 -25.516 -12.801 1.00 13.61 N ANISOU 96 N LEU A 28 2424 1704 1044 -965 -370 219 N ATOM 97 CA LEU A 28 -53.813 -25.506 -13.184 1.00 14.07 C ANISOU 97 CA LEU A 28 2480 1813 1051 -985 -266 139 C ATOM 98 C LEU A 28 -53.007 -24.554 -12.308 1.00 40.16 C ANISOU 98 C LEU A 28 5741 5111 4408 -955 -219 187 C ATOM 99 O LEU A 28 -52.003 -24.950 -11.701 1.00 13.21 O ANISOU 99 O LEU A 28 2267 1693 1058 -910 -153 119 O ATOM 100 CB LEU A 28 -53.668 -25.132 -14.658 1.00 15.25 C ANISOU 100 CB LEU A 28 2709 2052 1035 -1081 -248 126 C ATOM 101 CG LEU A 28 -54.054 -26.217 -15.661 1.00 20.43 C ANISOU 101 CG LEU A 28 3406 2737 1618 -1118 -266 28 C ATOM 102 CD1 LEU A 28 -53.958 -25.686 -17.081 1.00 17.50 C ANISOU 102 CD1 LEU A 28 3118 2467 1064 -1216 -253 34 C ATOM 103 CD2 LEU A 28 -53.176 -27.445 -15.482 1.00 17.20 C ANISOU 103 CD2 LEU A 28 2952 2310 1272 -1073 -186 -121 C ATOM 104 N VAL A 29 -53.435 -23.291 -12.228 1.00 24.48 N ANISOU 104 N VAL A 29 3782 3121 2400 -979 -260 299 N ATOM 105 CA VAL A 29 -52.678 -22.294 -11.475 1.00 23.84 C ANISOU 105 CA VAL A 29 3667 3030 2362 -966 -219 337 C ATOM 106 C VAL A 29 -52.650 -22.643 -9.991 1.00 28.55 C ANISOU 106 C VAL A 29 4186 3568 3093 -871 -227 329 C ATOM 107 O VAL A 29 -51.618 -22.499 -9.324 1.00 28.84 O ANISOU 107 O VAL A 29 4169 3613 3177 -845 -171 291 O ATOM 108 CB VAL A 29 -53.260 -20.889 -11.720 1.00 19.80 C ANISOU 108 CB VAL A 29 3151 2507 1867 -942 -272 396 C ATOM 109 CG1 VAL A 29 -52.554 -19.857 -10.851 1.00 12.50 C ANISOU 109 CG1 VAL A 29 2176 1563 1010 -900 -240 406 C ATOM 110 CG2 VAL A 29 -53.137 -20.521 -13.189 1.00 16.60 C ANISOU 110 CG2 VAL A 29 2808 2153 1345 -1026 -259 400 C ATOM 111 N ALA A 30 -53.780 -23.110 -9.451 1.00 30.07 N ANISOU 111 N ALA A 30 4369 3711 3346 -823 -298 365 N ATOM 112 CA ALA A 30 -53.834 -23.468 -8.036 1.00 21.74 C ANISOU 112 CA ALA A 30 3249 2609 2404 -737 -306 367 C ATOM 113 C ALA A 30 -52.921 -24.651 -7.736 1.00 19.83 C ANISOU 113 C ALA A 30 2965 2366 2205 -697 -253 272 C ATOM 114 O ALA A 30 -52.169 -24.637 -6.752 1.00 20.12 O ANISOU 114 O ALA A 30 2947 2396 2302 -643 -226 255 O ATOM 115 CB ALA A 30 -55.275 -23.777 -7.627 1.00 10.10 C ANISOU 115 CB ALA A 30 1746 1108 983 -677 -376 396 C ATOM 116 N GLY A 31 -52.975 -25.690 -8.576 1.00 21.14 N ANISOU 116 N GLY A 31 3153 2535 2342 -718 -245 203 N ATOM 117 CA GLY A 31 -52.077 -26.820 -8.392 1.00 23.20 C ANISOU 117 CA GLY A 31 3376 2785 2652 -671 -197 104 C ATOM 118 C GLY A 31 -50.616 -26.421 -8.478 1.00 18.44 C ANISOU 118 C GLY A 31 2734 2240 2032 -673 -117 43 C ATOM 119 O GLY A 31 -49.777 -26.927 -7.726 1.00 18.57 O ANISOU 119 O GLY A 31 2688 2244 2123 -604 -89 -5 O ATOM 120 N SER A 32 -50.294 -25.501 -9.390 1.00 19.35 N ANISOU 120 N SER A 32 2882 2421 2050 -753 -81 48 N ATOM 121 CA SER A 32 -48.925 -25.007 -9.488 1.00 17.85 C ANISOU 121 CA SER A 32 2646 2294 1843 -773 2 -4 C ATOM 122 C SER A 32 -48.513 -24.280 -8.213 1.00 21.18 C ANISOU 122 C SER A 32 3009 2699 2341 -728 -8 42 C ATOM 123 O SER A 32 -47.411 -24.493 -7.694 1.00 21.77 O ANISOU 123 O SER A 32 3006 2798 2468 -687 36 -21 O ATOM 124 CB SER A 32 -48.787 -24.091 -10.704 1.00 24.16 C ANISOU 124 CB SER A 32 3504 3161 2514 -884 40 16 C ATOM 125 OG SER A 32 -49.172 -24.763 -11.890 1.00 20.40 O ANISOU 125 OG SER A 32 3088 2714 1950 -928 45 -33 O ATOM 126 N LEU A 33 -49.392 -23.416 -7.693 1.00 21.05 N ANISOU 126 N LEU A 33 3023 2644 2333 -733 -69 146 N ATOM 127 CA LEU A 33 -49.118 -22.739 -6.427 1.00 22.95 C ANISOU 127 CA LEU A 33 3214 2865 2641 -689 -85 181 C ATOM 128 C LEU A 33 -48.825 -23.744 -5.320 1.00 28.93 C ANISOU 128 C LEU A 33 3906 3599 3486 -589 -99 143 C ATOM 129 O LEU A 33 -47.796 -23.654 -4.638 1.00 35.00 O ANISOU 129 O LEU A 33 4606 4395 4297 -554 -74 102 O ATOM 130 CB LEU A 33 -50.301 -21.851 -6.034 1.00 15.26 C ANISOU 130 CB LEU A 33 2285 1844 1670 -693 -152 286 C ATOM 131 CG LEU A 33 -50.423 -20.467 -6.670 1.00 18.31 C ANISOU 131 CG LEU A 33 2717 2239 2001 -757 -152 337 C ATOM 132 CD1 LEU A 33 -51.675 -19.768 -6.163 1.00 21.32 C ANISOU 132 CD1 LEU A 33 3094 2584 2423 -675 -222 382 C ATOM 133 CD2 LEU A 33 -49.189 -19.635 -6.377 1.00 14.93 C ANISOU 133 CD2 LEU A 33 2254 1837 1583 -797 -97 312 C ATOM 134 N SER A 34 -49.722 -24.717 -5.135 1.00 21.73 N ANISOU 134 N SER A 34 3016 2636 2604 -545 -143 161 N ATOM 135 CA SER A 34 -49.538 -25.701 -4.075 1.00 18.34 C ANISOU 135 CA SER A 34 2541 2172 2256 -453 -162 146 C ATOM 136 C SER A 34 -48.227 -26.458 -4.244 1.00 30.67 C ANISOU 136 C SER A 34 4046 3760 3847 -416 -112 44 C ATOM 137 O SER A 34 -47.489 -26.665 -3.272 1.00 38.66 O ANISOU 137 O SER A 34 4995 4777 4917 -345 -118 29 O ATOM 138 CB SER A 34 -50.721 -26.670 -4.051 1.00 16.14 C ANISOU 138 CB SER A 34 2302 1828 2003 -434 -208 180 C ATOM 139 OG SER A 34 -50.602 -27.593 -2.983 1.00 23.09 O ANISOU 139 OG SER A 34 3150 2665 2959 -351 -228 187 O ATOM 140 N LEU A 35 -47.910 -26.866 -5.475 1.00 11.29 N ANISOU 140 N LEU A 35 1610 1330 1351 -459 -65 -31 N ATOM 141 CA LEU A 35 -46.700 -27.653 -5.692 1.00 12.12 C ANISOU 141 CA LEU A 35 1653 1460 1492 -414 -12 -142 C ATOM 142 C LEU A 35 -45.443 -26.833 -5.420 1.00 23.18 C ANISOU 142 C LEU A 35 2974 2939 2895 -422 35 -177 C ATOM 143 O LEU A 35 -44.501 -27.325 -4.785 1.00 15.58 O ANISOU 143 O LEU A 35 1928 1988 2004 -344 41 -231 O ATOM 144 CB LEU A 35 -46.683 -28.211 -7.113 1.00 12.96 C ANISOU 144 CB LEU A 35 1799 1586 1540 -465 38 -227 C ATOM 145 CG LEU A 35 -45.470 -29.083 -7.448 1.00 21.57 C ANISOU 145 CG LEU A 35 2822 2702 2671 -413 103 -361 C ATOM 146 CD1 LEU A 35 -45.299 -30.199 -6.427 1.00 14.07 C ANISOU 146 CD1 LEU A 35 1831 1670 1845 -289 57 -372 C ATOM 147 CD2 LEU A 35 -45.588 -29.648 -8.853 1.00 14.94 C ANISOU 147 CD2 LEU A 35 2033 1882 1762 -466 152 -454 C ATOM 148 N VAL A 36 -45.411 -25.581 -5.884 1.00 19.80 N ANISOU 148 N VAL A 36 2567 2562 2396 -517 63 -144 N ATOM 149 CA VAL A 36 -44.247 -24.731 -5.645 1.00 17.22 C ANISOU 149 CA VAL A 36 2163 2305 2075 -544 109 -176 C ATOM 150 C VAL A 36 -44.076 -24.465 -4.153 1.00 18.68 C ANISOU 150 C VAL A 36 2294 2471 2331 -473 51 -138 C ATOM 151 O VAL A 36 -42.952 -24.464 -3.631 1.00 24.90 O ANISOU 151 O VAL A 36 2985 3308 3168 -438 68 -197 O ATOM 152 CB VAL A 36 -44.368 -23.423 -6.450 1.00 12.78 C ANISOU 152 CB VAL A 36 1653 1780 1422 -670 146 -132 C ATOM 153 CG1 VAL A 36 -43.267 -22.448 -6.059 1.00 13.14 C ANISOU 153 CG1 VAL A 36 1622 1882 1487 -711 185 -153 C ATOM 154 CG2 VAL A 36 -44.314 -23.717 -7.940 1.00 13.62 C ANISOU 154 CG2 VAL A 36 1805 1931 1439 -743 212 -181 C ATOM 155 N THR A 37 -45.186 -24.245 -3.442 1.00 11.20 N ANISOU 155 N THR A 37 1404 1464 1390 -452 -19 -45 N ATOM 156 CA THR A 37 -45.114 -24.060 -1.995 1.00 19.46 C ANISOU 156 CA THR A 37 2409 2499 2488 -384 -74 -10 C ATOM 157 C THR A 37 -44.527 -25.291 -1.314 1.00 24.87 C ANISOU 157 C THR A 37 3031 3176 3241 -274 -97 -53 C ATOM 158 O THR A 37 -43.616 -25.185 -0.477 1.00 24.09 O ANISOU 158 O THR A 37 2852 3119 3182 -226 -112 -83 O ATOM 159 CB THR A 37 -46.506 -23.756 -1.439 1.00 9.93 C ANISOU 159 CB THR A 37 1274 1232 1269 -377 -133 89 C ATOM 160 OG1 THR A 37 -47.041 -22.601 -2.091 1.00 12.38 O ANISOU 160 OG1 THR A 37 1640 1540 1525 -467 -122 131 O ATOM 161 CG2 THR A 37 -46.437 -23.499 0.058 1.00 29.57 C ANISOU 161 CG2 THR A 37 3723 3721 3789 -313 -182 119 C ATOM 162 N ILE A 38 -45.038 -26.472 -1.670 1.00 11.23 N ANISOU 162 N ILE A 38 1342 1393 1534 -233 -105 -56 N ATOM 163 CA ILE A 38 -44.556 -27.713 -1.069 1.00 11.73 C ANISOU 163 CA ILE A 38 1360 1424 1672 -124 -133 -86 C ATOM 164 C ILE A 38 -43.063 -27.882 -1.322 1.00 24.39 C ANISOU 164 C ILE A 38 2861 3094 3313 -94 -88 -194 C ATOM 165 O ILE A 38 -42.286 -28.154 -0.398 1.00 16.08 O ANISOU 165 O ILE A 38 1731 2060 2317 -10 -125 -209 O ATOM 166 CB ILE A 38 -45.362 -28.911 -1.601 1.00 26.42 C ANISOU 166 CB ILE A 38 3287 3199 3553 -105 -141 -82 C ATOM 167 CG1 ILE A 38 -46.819 -28.810 -1.145 1.00 21.85 C ANISOU 167 CG1 ILE A 38 2787 2562 2953 -126 -191 29 C ATOM 168 CG2 ILE A 38 -44.745 -30.220 -1.138 1.00 19.19 C ANISOU 168 CG2 ILE A 38 2330 2234 2727 8 -164 -120 C ATOM 169 CD1 ILE A 38 -47.722 -29.870 -1.729 1.00 11.21 C ANISOU 169 CD1 ILE A 38 1504 1132 1623 -133 -201 34 C ATOM 170 N ILE A 39 -42.638 -27.706 -2.576 1.00 21.91 N ANISOU 170 N ILE A 39 2538 2825 2962 -163 -9 -273 N ATOM 171 CA ILE A 39 -41.230 -27.900 -2.919 1.00 23.74 C ANISOU 171 CA ILE A 39 2659 3130 3230 -139 49 -389 C ATOM 172 C ILE A 39 -40.350 -26.918 -2.156 1.00 21.79 C ANISOU 172 C ILE A 39 2321 2963 2996 -152 41 -392 C ATOM 173 O ILE A 39 -39.309 -27.297 -1.604 1.00 26.30 O ANISOU 173 O ILE A 39 2782 3575 3638 -72 27 -451 O ATOM 174 CB ILE A 39 -41.024 -27.777 -4.441 1.00 14.93 C ANISOU 174 CB ILE A 39 1561 2064 2050 -231 148 -468 C ATOM 175 CG1 ILE A 39 -41.816 -28.855 -5.179 1.00 20.90 C ANISOU 175 CG1 ILE A 39 2400 2744 2797 -213 148 -487 C ATOM 176 CG2 ILE A 39 -39.552 -27.897 -4.787 1.00 16.19 C ANISOU 176 CG2 ILE A 39 1591 2316 2246 -214 222 -594 C ATOM 177 CD1 ILE A 39 -41.834 -28.670 -6.678 1.00 21.00 C ANISOU 177 CD1 ILE A 39 2454 2809 2715 -315 236 -551 C ATOM 178 N GLY A 40 -40.757 -25.647 -2.099 1.00 25.42 N ANISOU 178 N GLY A 40 2822 3442 3394 -249 42 -330 N ATOM 179 CA GLY A 40 -39.932 -24.648 -1.437 1.00 13.93 C ANISOU 179 CA GLY A 40 1285 2056 1953 -279 37 -344 C ATOM 180 C GLY A 40 -39.771 -24.906 0.050 1.00 13.79 C ANISOU 180 C GLY A 40 1220 2029 1988 -174 -56 -315 C ATOM 181 O GLY A 40 -38.651 -24.967 0.570 1.00 14.57 O ANISOU 181 O GLY A 40 1202 2194 2139 -128 -70 -378 O ATOM 182 N ASN A 41 -40.891 -25.068 0.759 1.00 16.16 N ANISOU 182 N ASN A 41 1609 2258 2273 -136 -123 -219 N ATOM 183 CA ASN A 41 -40.791 -25.255 2.203 1.00 16.52 C ANISOU 183 CA ASN A 41 1623 2306 2347 -46 -209 -182 C ATOM 184 C ASN A 41 -40.155 -26.593 2.559 1.00 20.63 C ANISOU 184 C ASN A 41 2083 2818 2940 81 -245 -213 C ATOM 185 O ASN A 41 -39.432 -26.685 3.559 1.00 14.21 O ANISOU 185 O ASN A 41 1192 2048 2158 153 -307 -223 O ATOM 186 CB ASN A 41 -42.166 -25.117 2.849 1.00 25.28 C ANISOU 186 CB ASN A 41 2840 3351 3417 -43 -257 -73 C ATOM 187 CG ASN A 41 -42.668 -23.689 2.829 1.00 24.36 C ANISOU 187 CG ASN A 41 2766 3244 3247 -141 -243 -45 C ATOM 188 OD1 ASN A 41 -42.266 -22.867 3.656 1.00 24.17 O ANISOU 188 OD1 ASN A 41 2704 3264 3217 -150 -272 -56 O ATOM 189 ND2 ASN A 41 -43.545 -23.381 1.876 1.00 21.05 N ANISOU 189 ND2 ASN A 41 2427 2779 2790 -214 -204 -12 N ATOM 190 N ILE A 42 -40.398 -27.632 1.757 1.00 24.03 N ANISOU 190 N ILE A 42 2546 3187 3397 111 -215 -233 N ATOM 191 CA ILE A 42 -39.726 -28.907 1.991 1.00 28.84 C ANISOU 191 CA ILE A 42 3097 3772 4091 237 -246 -273 C ATOM 192 C ILE A 42 -38.220 -28.751 1.815 1.00 27.85 C ANISOU 192 C ILE A 42 2822 3745 4014 260 -217 -388 C ATOM 193 O ILE A 42 -37.432 -29.242 2.633 1.00 24.63 O ANISOU 193 O ILE A 42 2328 3361 3671 368 -281 -404 O ATOM 194 CB ILE A 42 -40.302 -30.001 1.073 1.00 22.39 C ANISOU 194 CB ILE A 42 2349 2860 3297 254 -212 -289 C ATOM 195 CG1 ILE A 42 -41.623 -30.527 1.637 1.00 21.67 C ANISOU 195 CG1 ILE A 42 2374 2664 3194 273 -270 -170 C ATOM 196 CG2 ILE A 42 -39.313 -31.141 0.912 1.00 18.59 C ANISOU 196 CG2 ILE A 42 1785 2363 2914 369 -212 -379 C ATOM 197 CD1 ILE A 42 -42.163 -31.739 0.906 1.00 24.17 C ANISOU 197 CD1 ILE A 42 2757 2875 3553 298 -254 -186 C ATOM 198 N LEU A 43 -37.795 -28.055 0.756 1.00 26.00 N ANISOU 198 N LEU A 43 2553 3577 3750 156 -121 -466 N ATOM 199 CA LEU A 43 -36.368 -27.813 0.557 1.00 21.84 C ANISOU 199 CA LEU A 43 1871 3158 3269 159 -80 -579 C ATOM 200 C LEU A 43 -35.766 -27.061 1.737 1.00 25.48 C ANISOU 200 C LEU A 43 2250 3692 3741 169 -151 -564 C ATOM 201 O LEU A 43 -34.637 -27.348 2.153 1.00 18.62 O ANISOU 201 O LEU A 43 1241 2891 2943 245 -180 -633 O ATOM 202 CB LEU A 43 -36.137 -27.041 -0.741 1.00 17.52 C ANISOU 202 CB LEU A 43 1318 2674 2667 18 42 -644 C ATOM 203 CG LEU A 43 -36.114 -27.863 -2.029 1.00 27.71 C ANISOU 203 CG LEU A 43 2624 3947 3957 19 131 -724 C ATOM 204 CD1 LEU A 43 -36.142 -26.950 -3.240 1.00 25.44 C ANISOU 204 CD1 LEU A 43 2368 3720 3577 -141 243 -750 C ATOM 205 CD2 LEU A 43 -34.890 -28.763 -2.064 1.00 24.58 C ANISOU 205 CD2 LEU A 43 2080 3596 3662 133 148 -846 C ATOM 206 N VAL A 44 -36.507 -26.099 2.294 1.00 21.50 N ANISOU 206 N VAL A 44 1825 3175 3170 96 -184 -480 N ATOM 207 CA VAL A 44 -36.018 -25.378 3.469 1.00 21.31 C ANISOU 207 CA VAL A 44 1736 3216 3146 103 -259 -472 C ATOM 208 C VAL A 44 -35.853 -26.330 4.651 1.00 22.36 C ANISOU 208 C VAL A 44 1840 3334 3320 256 -372 -434 C ATOM 209 O VAL A 44 -34.817 -26.336 5.330 1.00 19.18 O ANISOU 209 O VAL A 44 1313 3014 2963 315 -429 -484 O ATOM 210 CB VAL A 44 -36.959 -24.211 3.814 1.00 18.47 C ANISOU 210 CB VAL A 44 1480 2830 2707 4 -268 -397 C ATOM 211 CG1 VAL A 44 -36.562 -23.588 5.143 1.00 15.78 C ANISOU 211 CG1 VAL A 44 1087 2548 2360 23 -356 -393 C ATOM 212 CG2 VAL A 44 -36.938 -23.171 2.707 1.00 15.39 C ANISOU 212 CG2 VAL A 44 1108 2458 2283 -147 -168 -429 C ATOM 213 N MET A 45 -36.871 -27.159 4.906 1.00 16.48 N ANISOU 213 N MET A 45 1211 2488 2562 320 -409 -342 N ATOM 214 CA MET A 45 -36.844 -28.033 6.076 1.00 19.46 C ANISOU 214 CA MET A 45 1587 2841 2965 456 -518 -279 C ATOM 215 C MET A 45 -35.733 -29.073 5.969 1.00 20.75 C ANISOU 215 C MET A 45 1634 3018 3231 579 -543 -349 C ATOM 216 O MET A 45 -34.967 -29.284 6.918 1.00 21.63 O ANISOU 216 O MET A 45 1659 3185 3375 672 -636 -350 O ATOM 217 CB MET A 45 -38.204 -28.707 6.253 1.00 19.79 C ANISOU 217 CB MET A 45 1779 2765 2976 478 -536 -163 C ATOM 218 CG MET A 45 -39.316 -27.745 6.647 1.00 27.51 C ANISOU 218 CG MET A 45 2857 3735 3858 386 -533 -86 C ATOM 219 SD MET A 45 -40.965 -28.472 6.550 1.00 28.93 S ANISOU 219 SD MET A 45 3194 3787 4011 384 -525 32 S ATOM 220 CE MET A 45 -40.764 -29.918 7.589 1.00 30.83 C ANISOU 220 CE MET A 45 3438 3977 4300 536 -622 106 C ATOM 221 N VAL A 46 -35.632 -29.735 4.815 1.00 25.37 N ANISOU 221 N VAL A 46 2214 3556 3870 586 -464 -414 N ATOM 222 CA VAL A 46 -34.583 -30.729 4.609 1.00 29.11 C ANISOU 222 CA VAL A 46 2571 4035 4453 710 -476 -499 C ATOM 223 C VAL A 46 -33.209 -30.075 4.679 1.00 30.12 C ANISOU 223 C VAL A 46 2517 4309 4618 701 -470 -608 C ATOM 224 O VAL A 46 -32.267 -30.631 5.259 1.00 23.99 O ANISOU 224 O VAL A 46 1639 3564 3911 816 -538 -633 O ATOM 225 CB VAL A 46 -34.797 -31.458 3.268 1.00 25.93 C ANISOU 225 CB VAL A 46 2204 3559 4087 702 -377 -567 C ATOM 226 CG1 VAL A 46 -33.660 -32.435 2.998 1.00 30.24 C ANISOU 226 CG1 VAL A 46 2619 4114 4758 836 -377 -677 C ATOM 227 CG2 VAL A 46 -36.136 -32.178 3.266 1.00 20.10 C ANISOU 227 CG2 VAL A 46 1636 2676 3326 711 -396 -462 C ATOM 228 N SER A 47 -33.073 -28.882 4.095 1.00 28.15 N ANISOU 228 N SER A 47 2242 4140 4314 551 -384 -659 N ATOM 229 CA SER A 47 -31.793 -28.185 4.143 1.00 26.59 C ANISOU 229 CA SER A 47 1867 4082 4152 518 -370 -763 C ATOM 230 C SER A 47 -31.381 -27.880 5.578 1.00 33.90 C ANISOU 230 C SER A 47 2769 5052 5059 561 -492 -706 C ATOM 231 O SER A 47 -30.204 -28.021 5.935 1.00 23.66 O ANISOU 231 O SER A 47 1374 3813 3802 604 -517 -749 O ATOM 232 CB SER A 47 -31.864 -26.902 3.315 1.00 22.49 C ANISOU 232 CB SER A 47 1361 3618 3567 328 -256 -800 C ATOM 233 OG SER A 47 -31.982 -27.201 1.936 1.00 26.80 O ANISOU 233 OG SER A 47 1933 4140 4108 278 -131 -856 O ATOM 234 N ILE A 48 -32.333 -27.475 6.422 1.00 25.15 N ANISOU 234 N ILE A 48 1768 3910 3876 543 -564 -604 N ATOM 235 CA ILE A 48 -31.986 -27.154 7.804 1.00 22.49 C ANISOU 235 CA ILE A 48 1440 3612 3494 567 -664 -545 C ATOM 236 C ILE A 48 -31.662 -28.421 8.589 1.00 28.87 C ANISOU 236 C ILE A 48 2260 4374 4335 720 -750 -478 C ATOM 237 O ILE A 48 -30.709 -28.450 9.378 1.00 32.44 O ANISOU 237 O ILE A 48 2644 4886 4797 760 -812 -481 O ATOM 238 CB ILE A 48 -33.108 -26.340 8.471 1.00 25.70 C ANISOU 238 CB ILE A 48 1963 4001 3802 499 -700 -463 C ATOM 239 CG1 ILE A 48 -33.226 -24.966 7.811 1.00 29.09 C ANISOU 239 CG1 ILE A 48 2372 4478 4203 337 -622 -529 C ATOM 240 CG2 ILE A 48 -32.837 -26.176 9.959 1.00 20.84 C ANISOU 240 CG2 ILE A 48 1369 3420 3129 534 -801 -400 C ATOM 241 CD1 ILE A 48 -34.324 -24.103 8.389 1.00 30.03 C ANISOU 241 CD1 ILE A 48 2620 4564 4228 265 -642 -454 C ATOM 242 N LYS A 49 -32.435 -29.492 8.384 1.00 25.37 N ANISOU 242 N LYS A 49 1907 3819 3914 801 -758 -413 N ATOM 243 CA LYS A 49 -32.169 -30.732 9.108 1.00 28.06 C ANISOU 243 CA LYS A 49 2274 4100 4289 935 -832 -336 C ATOM 244 C LYS A 49 -30.893 -31.427 8.650 1.00 39.44 C ANISOU 244 C LYS A 49 3588 5562 5835 1015 -817 -427 C ATOM 245 O LYS A 49 -30.347 -32.240 9.403 1.00 49.16 O ANISOU 245 O LYS A 49 4805 6776 7096 1119 -891 -374 O ATOM 246 CB LYS A 49 -33.343 -31.702 8.968 1.00 22.73 C ANISOU 246 CB LYS A 49 1737 3283 3615 985 -835 -241 C ATOM 247 CG LYS A 49 -34.538 -31.375 9.838 1.00 29.66 C ANISOU 247 CG LYS A 49 2752 4131 4386 942 -874 -110 C ATOM 248 CD LYS A 49 -34.253 -31.635 11.306 1.00 29.60 C ANISOU 248 CD LYS A 49 2767 4154 4324 989 -962 -6 C ATOM 249 CE LYS A 49 -35.493 -31.379 12.152 1.00 38.73 C ANISOU 249 CE LYS A 49 4060 5287 5370 940 -979 120 C ATOM 250 NZ LYS A 49 -35.266 -31.677 13.592 1.00 48.25 N ANISOU 250 NZ LYS A 49 5287 6530 6518 979 -1058 223 N ATOM 251 N VAL A 50 -30.411 -31.140 7.444 1.00 37.74 N ANISOU 251 N VAL A 50 3279 5387 5674 967 -718 -560 N ATOM 252 CA VAL A 50 -29.232 -31.830 6.922 1.00 28.94 C ANISOU 252 CA VAL A 50 2043 4293 4658 1043 -688 -657 C ATOM 253 C VAL A 50 -27.955 -31.037 7.176 1.00 40.90 C ANISOU 253 C VAL A 50 3413 5946 6180 997 -691 -733 C ATOM 254 O VAL A 50 -26.990 -31.558 7.740 1.00 33.08 O ANISOU 254 O VAL A 50 2343 4984 5241 1089 -754 -735 O ATOM 255 CB VAL A 50 -29.417 -32.131 5.422 1.00 31.68 C ANISOU 255 CB VAL A 50 2376 4605 5057 1020 -564 -764 C ATOM 256 CG1 VAL A 50 -28.092 -32.525 4.791 1.00 42.67 C ANISOU 256 CG1 VAL A 50 3624 6054 6535 1065 -509 -891 C ATOM 257 CG2 VAL A 50 -30.433 -33.238 5.235 1.00 33.95 C ANISOU 257 CG2 VAL A 50 2794 4736 5369 1099 -579 -699 C ATOM 258 N ASN A 51 -27.926 -29.772 6.770 1.00 52.37 N ANISOU 258 N ASN A 51 4829 7483 7586 853 -624 -793 N ATOM 259 CA ASN A 51 -26.730 -28.958 6.941 1.00 55.31 C ANISOU 259 CA ASN A 51 5069 7978 7968 790 -617 -868 C ATOM 260 C ASN A 51 -26.580 -28.542 8.399 1.00 50.94 C ANISOU 260 C ASN A 51 4531 7461 7362 801 -742 -789 C ATOM 261 O ASN A 51 -27.524 -28.031 9.010 1.00 54.81 O ANISOU 261 O ASN A 51 5133 7925 7768 754 -781 -707 O ATOM 262 CB ASN A 51 -26.799 -27.725 6.036 1.00 57.39 C ANISOU 262 CB ASN A 51 5309 8302 8194 617 -499 -944 C ATOM 263 CG ASN A 51 -25.473 -26.991 5.936 1.00 55.10 C ANISOU 263 CG ASN A 51 4875 8128 7932 544 -465 -1037 C ATOM 264 OD1 ASN A 51 -24.661 -27.013 6.860 1.00 60.98 O ANISOU 264 OD1 ASN A 51 5549 8923 8698 597 -555 -1030 O ATOM 265 ND2 ASN A 51 -25.251 -26.329 4.807 1.00 52.43 N ANISOU 265 ND2 ASN A 51 4496 7835 7590 417 -332 -1119 N ATOM 266 N ARG A 52 -25.389 -28.759 8.958 1.00 50.72 N ANISOU 266 N ARG A 52 4388 7500 7383 863 -802 -817 N ATOM 267 CA ARG A 52 -25.151 -28.393 10.349 1.00 57.79 C ANISOU 267 CA ARG A 52 5288 8442 8227 873 -923 -752 C ATOM 268 C ARG A 52 -24.936 -26.894 10.523 1.00 50.68 C ANISOU 268 C ARG A 52 4356 7627 7272 721 -903 -803 C ATOM 269 O ARG A 52 -25.193 -26.361 11.607 1.00 46.74 O ANISOU 269 O ARG A 52 3911 7148 6699 695 -987 -745 O ATOM 270 CB ARG A 52 -23.951 -29.166 10.894 1.00 68.73 C ANISOU 270 CB ARG A 52 6556 9870 9687 995 -1004 -762 C ATOM 271 CG ARG A 52 -24.159 -30.671 10.905 1.00 75.05 C ANISOU 271 CG ARG A 52 7401 10570 10543 1153 -1040 -694 C ATOM 272 CD ARG A 52 -22.869 -31.411 11.205 1.00 80.93 C ANISOU 272 CD ARG A 52 8009 11358 11382 1272 -1103 -725 C ATOM 273 NE ARG A 52 -23.036 -32.861 11.137 1.00 83.09 N ANISOU 273 NE ARG A 52 8327 11522 11721 1423 -1130 -665 N ATOM 274 CZ ARG A 52 -22.035 -33.734 11.215 1.00 80.75 C ANISOU 274 CZ ARG A 52 7923 11233 11524 1550 -1173 -689 C ATOM 275 NH1 ARG A 52 -20.788 -33.306 11.360 1.00 74.73 N ANISOU 275 NH1 ARG A 52 6995 10593 10808 1544 -1195 -774 N ATOM 276 NH2 ARG A 52 -22.279 -35.037 11.145 1.00 79.76 N ANISOU 276 NH2 ARG A 52 7856 10989 11459 1682 -1194 -630 N ATOM 277 N HIS A 53 -24.470 -26.200 9.480 1.00 44.71 N ANISOU 277 N HIS A 53 3520 6919 6549 613 -790 -910 N ATOM 278 CA HIS A 53 -24.325 -24.749 9.551 1.00 43.17 C ANISOU 278 CA HIS A 53 3310 6784 6307 455 -760 -953 C ATOM 279 C HIS A 53 -25.669 -24.029 9.548 1.00 43.71 C ANISOU 279 C HIS A 53 3530 6790 6289 364 -736 -894 C ATOM 280 O HIS A 53 -25.742 -22.876 9.985 1.00 48.76 O ANISOU 280 O HIS A 53 4192 7456 6878 255 -746 -901 O ATOM 281 CB HIS A 53 -23.463 -24.249 8.391 1.00 47.05 C ANISOU 281 CB HIS A 53 3684 7337 6855 356 -635 -1070 C ATOM 282 CG HIS A 53 -22.024 -24.651 8.494 1.00 58.11 C ANISOU 282 CG HIS A 53 4917 8822 8341 419 -659 -1143 C ATOM 283 ND1 HIS A 53 -21.063 -24.217 7.606 1.00 62.48 N ANISOU 283 ND1 HIS A 53 5345 9449 8946 335 -556 -1249 N ATOM 284 CD2 HIS A 53 -21.383 -25.445 9.384 1.00 61.16 C ANISOU 284 CD2 HIS A 53 5239 9233 8767 556 -776 -1120 C ATOM 285 CE1 HIS A 53 -19.893 -24.728 7.943 1.00 63.80 C ANISOU 285 CE1 HIS A 53 5369 9685 9188 422 -608 -1297 C ATOM 286 NE2 HIS A 53 -20.059 -25.477 9.018 1.00 62.49 N ANISOU 286 NE2 HIS A 53 5237 9489 9017 558 -745 -1218 N ATOM 287 N LEU A 54 -26.728 -24.675 9.062 1.00 44.30 N ANISOU 287 N LEU A 54 3705 6779 6349 407 -705 -840 N ATOM 288 CA LEU A 54 -28.069 -24.111 9.079 1.00 38.19 C ANISOU 288 CA LEU A 54 3071 5943 5497 337 -690 -777 C ATOM 289 C LEU A 54 -28.840 -24.472 10.343 1.00 39.91 C ANISOU 289 C LEU A 54 3397 6119 5647 418 -805 -665 C ATOM 290 O LEU A 54 -30.075 -24.424 10.339 1.00 48.43 O ANISOU 290 O LEU A 54 4600 7133 6671 403 -798 -597 O ATOM 291 CB LEU A 54 -28.850 -24.569 7.846 1.00 29.64 C ANISOU 291 CB LEU A 54 2036 4795 4430 328 -594 -779 C ATOM 292 CG LEU A 54 -28.409 -24.009 6.494 1.00 24.50 C ANISOU 292 CG LEU A 54 1318 4181 3811 208 -456 -875 C ATOM 293 CD1 LEU A 54 -29.109 -24.744 5.366 1.00 23.75 C ANISOU 293 CD1 LEU A 54 1265 4028 3733 229 -374 -880 C ATOM 294 CD2 LEU A 54 -28.685 -22.518 6.418 1.00 23.86 C ANISOU 294 CD2 LEU A 54 1279 4113 3672 39 -413 -878 C ATOM 295 N GLN A 55 -28.148 -24.833 11.420 1.00 31.74 N ANISOU 295 N GLN A 55 2321 5126 4612 498 -906 -641 N ATOM 296 CA GLN A 55 -28.788 -25.273 12.653 1.00 32.56 C ANISOU 296 CA GLN A 55 2528 5199 4645 572 -1009 -526 C ATOM 297 C GLN A 55 -28.659 -24.225 13.756 1.00 40.99 C ANISOU 297 C GLN A 55 3609 6330 5636 504 -1073 -530 C ATOM 298 O GLN A 55 -28.362 -24.543 14.910 1.00 39.46 O ANISOU 298 O GLN A 55 3418 6168 5405 567 -1174 -480 O ATOM 299 CB GLN A 55 -28.219 -26.616 13.101 1.00 27.36 C ANISOU 299 CB GLN A 55 1833 4529 4036 721 -1082 -476 C ATOM 300 CG GLN A 55 -28.536 -27.753 12.137 1.00 27.06 C ANISOU 300 CG GLN A 55 1812 4403 4068 802 -1027 -462 C ATOM 301 CD GLN A 55 -27.914 -29.071 12.550 1.00 46.14 C ANISOU 301 CD GLN A 55 4191 6795 6547 950 -1096 -415 C ATOM 302 OE1 GLN A 55 -27.069 -29.121 13.443 1.00 54.86 O ANISOU 302 OE1 GLN A 55 5229 7964 7653 992 -1183 -405 O ATOM 303 NE2 GLN A 55 -28.330 -30.151 11.899 1.00 40.74 N ANISOU 303 NE2 GLN A 55 3551 6011 5918 1029 -1062 -387 N ATOM 304 N THR A 56 -28.888 -22.964 13.405 1.00 36.04 N ANISOU 304 N THR A 56 2993 5716 4983 371 -1013 -590 N ATOM 305 CA THR A 56 -28.916 -21.865 14.358 1.00 29.41 C ANISOU 305 CA THR A 56 2184 4918 4072 295 -1061 -606 C ATOM 306 C THR A 56 -30.357 -21.558 14.759 1.00 35.02 C ANISOU 306 C THR A 56 3050 5567 4689 273 -1061 -534 C ATOM 307 O THR A 56 -31.316 -22.055 14.163 1.00 33.90 O ANISOU 307 O THR A 56 2985 5353 4544 296 -1015 -477 O ATOM 308 CB THR A 56 -28.244 -20.623 13.768 1.00 31.40 C ANISOU 308 CB THR A 56 2358 5210 4364 158 -996 -717 C ATOM 309 OG1 THR A 56 -29.014 -20.139 12.660 1.00 34.80 O ANISOU 309 OG1 THR A 56 2844 5576 4801 69 -888 -726 O ATOM 310 CG2 THR A 56 -26.839 -20.957 13.289 1.00 27.66 C ANISOU 310 CG2 THR A 56 1724 4802 3985 176 -982 -791 C ATOM 311 N VAL A 57 -30.500 -20.714 15.784 1.00 37.87 N ANISOU 311 N VAL A 57 3454 5960 4974 227 -1113 -542 N ATOM 312 CA VAL A 57 -31.822 -20.428 16.336 1.00 38.64 C ANISOU 312 CA VAL A 57 3694 6012 4976 216 -1117 -479 C ATOM 313 C VAL A 57 -32.694 -19.702 15.316 1.00 38.48 C ANISOU 313 C VAL A 57 3728 5925 4967 125 -1020 -501 C ATOM 314 O VAL A 57 -33.903 -19.965 15.210 1.00 50.20 O ANISOU 314 O VAL A 57 5318 7349 6409 145 -998 -430 O ATOM 315 CB VAL A 57 -31.687 -19.631 17.646 1.00 40.41 C ANISOU 315 CB VAL A 57 3943 6293 5119 186 -1189 -506 C ATOM 316 CG1 VAL A 57 -31.166 -20.530 18.756 1.00 45.39 C ANISOU 316 CG1 VAL A 57 4556 6979 5712 287 -1294 -448 C ATOM 317 CG2 VAL A 57 -30.757 -18.449 17.455 1.00 38.65 C ANISOU 317 CG2 VAL A 57 3630 6113 4940 80 -1174 -626 C ATOM 318 N ASN A 58 -32.103 -18.778 14.550 1.00 37.65 N ANISOU 318 N ASN A 58 3556 5828 4922 18 -961 -592 N ATOM 319 CA ASN A 58 -32.849 -18.114 13.486 1.00 39.47 C ANISOU 319 CA ASN A 58 3836 5991 5171 -77 -867 -604 C ATOM 320 C ASN A 58 -33.458 -19.136 12.539 1.00 44.04 C ANISOU 320 C ASN A 58 4436 6521 5776 -22 -821 -546 C ATOM 321 O ASN A 58 -34.613 -19.000 12.121 1.00 52.80 O ANISOU 321 O ASN A 58 5638 7567 6858 -47 -784 -504 O ATOM 322 CB ASN A 58 -31.942 -17.151 12.717 1.00 44.89 C ANISOU 322 CB ASN A 58 4440 6690 5926 -201 -802 -695 C ATOM 323 CG ASN A 58 -31.281 -16.125 13.615 1.00 51.98 C ANISOU 323 CG ASN A 58 5312 7630 6809 -260 -851 -760 C ATOM 324 OD1 ASN A 58 -30.836 -16.443 14.717 1.00 65.09 O ANISOU 324 OD1 ASN A 58 6944 9352 8434 -191 -941 -760 O ATOM 325 ND2 ASN A 58 -31.218 -14.882 13.149 1.00 46.09 N ANISOU 325 ND2 ASN A 58 4579 6845 6090 -393 -793 -811 N ATOM 326 N ASN A 59 -32.701 -20.183 12.214 1.00 40.97 N ANISOU 326 N ASN A 59 3963 6159 5444 58 -827 -547 N ATOM 327 CA ASN A 59 -33.204 -21.241 11.352 1.00 37.77 C ANISOU 327 CA ASN A 59 3575 5705 5072 121 -789 -503 C ATOM 328 C ASN A 59 -34.148 -22.193 12.075 1.00 35.17 C ANISOU 328 C ASN A 59 3346 5328 4687 232 -850 -392 C ATOM 329 O ASN A 59 -34.868 -22.945 11.412 1.00 37.78 O ANISOU 329 O ASN A 59 3723 5597 5035 273 -820 -345 O ATOM 330 CB ASN A 59 -32.034 -22.013 10.747 1.00 39.40 C ANISOU 330 CB ASN A 59 3656 5948 5366 172 -768 -556 C ATOM 331 CG ASN A 59 -31.081 -21.114 9.990 1.00 49.28 C ANISOU 331 CG ASN A 59 4808 7248 6668 54 -692 -658 C ATOM 332 OD1 ASN A 59 -31.361 -20.699 8.865 1.00 48.28 O ANISOU 332 OD1 ASN A 59 4690 7095 6559 -39 -594 -686 O ATOM 333 ND2 ASN A 59 -29.949 -20.801 10.608 1.00 62.00 N ANISOU 333 ND2 ASN A 59 6330 8930 8299 51 -735 -709 N ATOM 334 N TYR A 60 -34.150 -22.195 13.411 1.00 25.48 N ANISOU 334 N TYR A 60 2159 4129 3395 275 -930 -347 N ATOM 335 CA TYR A 60 -35.212 -22.881 14.141 1.00 20.34 C ANISOU 335 CA TYR A 60 1626 3430 2672 345 -968 -231 C ATOM 336 C TYR A 60 -36.541 -22.165 13.946 1.00 25.87 C ANISOU 336 C TYR A 60 2430 4084 3315 279 -924 -208 C ATOM 337 O TYR A 60 -37.562 -22.792 13.626 1.00 37.32 O ANISOU 337 O TYR A 60 3961 5467 4752 313 -901 -130 O ATOM 338 CB TYR A 60 -34.871 -22.963 15.628 1.00 22.03 C ANISOU 338 CB TYR A 60 1855 3697 2820 387 -1056 -194 C ATOM 339 CG TYR A 60 -34.057 -24.168 16.036 1.00 32.97 C ANISOU 339 CG TYR A 60 3189 5096 4243 494 -1119 -147 C ATOM 340 CD1 TYR A 60 -32.763 -24.350 15.568 1.00 40.49 C ANISOU 340 CD1 TYR A 60 4007 6091 5284 514 -1125 -223 C ATOM 341 CD2 TYR A 60 -34.574 -25.109 16.917 1.00 29.14 C ANISOU 341 CD2 TYR A 60 2786 4579 3707 568 -1169 -25 C ATOM 342 CE1 TYR A 60 -32.013 -25.446 15.952 1.00 38.39 C ANISOU 342 CE1 TYR A 60 3692 5835 5061 619 -1187 -181 C ATOM 343 CE2 TYR A 60 -33.833 -26.205 17.308 1.00 25.53 C ANISOU 343 CE2 TYR A 60 2285 4126 3290 663 -1232 26 C ATOM 344 CZ TYR A 60 -32.554 -26.369 16.822 1.00 34.91 C ANISOU 344 CZ TYR A 60 3339 5355 4570 695 -1244 -54 C ATOM 345 OH TYR A 60 -31.814 -27.462 17.207 1.00 36.96 O ANISOU 345 OH TYR A 60 3551 5616 4876 799 -1309 -4 O ATOM 346 N PHE A 61 -36.544 -20.843 14.138 1.00 21.91 N ANISOU 346 N PHE A 61 1930 3611 2784 183 -912 -277 N ATOM 347 CA PHE A 61 -37.752 -20.066 13.876 1.00 21.35 C ANISOU 347 CA PHE A 61 1948 3493 2671 119 -868 -267 C ATOM 348 C PHE A 61 -38.189 -20.215 12.423 1.00 24.38 C ANISOU 348 C PHE A 61 2337 3812 3115 79 -791 -264 C ATOM 349 O PHE A 61 -39.364 -20.480 12.136 1.00 28.00 O ANISOU 349 O PHE A 61 2905 4187 3548 85 -746 -182 O ATOM 350 CB PHE A 61 -37.508 -18.599 14.225 1.00 18.54 C ANISOU 350 CB PHE A 61 1584 3163 2298 19 -865 -356 C ATOM 351 CG PHE A 61 -37.125 -18.374 15.661 1.00 26.78 C ANISOU 351 CG PHE A 61 2634 4268 3275 47 -936 -368 C ATOM 352 CD1 PHE A 61 -36.273 -17.340 16.013 1.00 37.59 C ANISOU 352 CD1 PHE A 61 3948 5678 4656 -24 -952 -465 C ATOM 353 CD2 PHE A 61 -37.626 -19.192 16.660 1.00 25.53 C ANISOU 353 CD2 PHE A 61 2539 4122 3040 137 -983 -279 C ATOM 354 CE1 PHE A 61 -35.921 -17.131 17.338 1.00 41.46 C ANISOU 354 CE1 PHE A 61 4442 6231 5079 0 -1023 -483 C ATOM 355 CE2 PHE A 61 -37.279 -18.990 17.984 1.00 30.13 C ANISOU 355 CE2 PHE A 61 3129 4768 3551 156 -1048 -291 C ATOM 356 CZ PHE A 61 -36.424 -17.959 18.324 1.00 32.50 C ANISOU 356 CZ PHE A 61 3370 5119 3859 91 -1072 -398 C ATOM 357 N LEU A 62 -37.244 -20.066 11.490 1.00 35.89 N ANISOU 357 N LEU A 62 3700 5286 4651 27 -747 -337 N ATOM 358 CA LEU A 62 -37.563 -20.234 10.078 1.00 28.47 C ANISOU 358 CA LEU A 62 2793 4269 3757 -24 -645 -321 C ATOM 359 C LEU A 62 -38.022 -21.653 9.773 1.00 23.36 C ANISOU 359 C LEU A 62 2186 3568 3123 76 -642 -244 C ATOM 360 O LEU A 62 -38.777 -21.869 8.818 1.00 23.59 O ANISOU 360 O LEU A 62 2290 3516 3159 45 -570 -203 O ATOM 361 CB LEU A 62 -36.353 -19.865 9.218 1.00 20.26 C ANISOU 361 CB LEU A 62 1631 3278 2788 -98 -594 -420 C ATOM 362 CG LEU A 62 -35.947 -18.389 9.267 1.00 16.54 C ANISOU 362 CG LEU A 62 1130 2834 2319 -229 -577 -494 C ATOM 363 CD1 LEU A 62 -34.750 -18.113 8.373 1.00 17.44 C ANISOU 363 CD1 LEU A 62 1125 2997 2503 -311 -512 -578 C ATOM 364 CD2 LEU A 62 -37.120 -17.499 8.896 1.00 15.54 C ANISOU 364 CD2 LEU A 62 1142 2606 2155 -312 -523 -443 C ATOM 365 N PHE A 63 -37.589 -22.630 10.571 1.00 21.01 N ANISOU 365 N PHE A 63 1843 3309 2829 195 -724 -222 N ATOM 366 CA PHE A 63 -38.065 -23.996 10.382 1.00 24.67 C ANISOU 366 CA PHE A 63 2358 3704 3313 291 -729 -142 C ATOM 367 C PHE A 63 -39.524 -24.123 10.798 1.00 23.46 C ANISOU 367 C PHE A 63 2345 3478 3090 294 -727 -33 C ATOM 368 O PHE A 63 -40.324 -24.754 10.098 1.00 20.72 O ANISOU 368 O PHE A 63 2071 3042 2759 295 -678 22 O ATOM 369 CB PHE A 63 -37.197 -24.985 11.163 1.00 16.81 C ANISOU 369 CB PHE A 63 1281 2758 2347 422 -827 -136 C ATOM 370 CG PHE A 63 -37.597 -26.424 10.966 1.00 16.87 C ANISOU 370 CG PHE A 63 1341 2675 2392 522 -836 -57 C ATOM 371 CD1 PHE A 63 -37.012 -27.188 9.969 1.00 17.30 C ANISOU 371 CD1 PHE A 63 1336 2696 2543 559 -794 -109 C ATOM 372 CD2 PHE A 63 -38.565 -27.010 11.771 1.00 16.62 C ANISOU 372 CD2 PHE A 63 1430 2584 2299 560 -862 71 C ATOM 373 CE1 PHE A 63 -37.381 -28.508 9.781 1.00 17.49 C ANISOU 373 CE1 PHE A 63 1413 2620 2612 649 -805 -46 C ATOM 374 CE2 PHE A 63 -38.938 -28.328 11.586 1.00 16.80 C ANISOU 374 CE2 PHE A 63 1509 2512 2363 633 -861 147 C ATOM 375 CZ PHE A 63 -38.346 -29.078 10.591 1.00 17.24 C ANISOU 375 CZ PHE A 63 1502 2523 2525 685 -842 86 C ATOM 376 N SER A 64 -39.888 -23.548 11.947 1.00 21.72 N ANISOU 376 N SER A 64 2160 3303 2791 294 -778 -7 N ATOM 377 CA SER A 64 -41.291 -23.556 12.352 1.00 13.92 C ANISOU 377 CA SER A 64 1293 2260 1735 288 -763 86 C ATOM 378 C SER A 64 -42.161 -22.856 11.313 1.00 23.54 C ANISOU 378 C SER A 64 2572 3406 2966 191 -671 80 C ATOM 379 O SER A 64 -43.225 -23.363 10.925 1.00 21.18 O ANISOU 379 O SER A 64 2352 3030 2664 192 -634 155 O ATOM 380 CB SER A 64 -41.445 -22.893 13.720 1.00 14.30 C ANISOU 380 CB SER A 64 1359 2387 1689 295 -821 88 C ATOM 381 OG SER A 64 -42.813 -22.725 14.048 1.00 28.15 O ANISOU 381 OG SER A 64 3217 4099 3380 278 -788 159 O ATOM 382 N LEU A 65 -41.714 -21.687 10.846 1.00 21.28 N ANISOU 382 N LEU A 65 2249 3142 2696 103 -637 -3 N ATOM 383 CA LEU A 65 -42.451 -20.957 9.819 1.00 21.82 C ANISOU 383 CA LEU A 65 2376 3140 2777 11 -559 -2 C ATOM 384 C LEU A 65 -42.612 -21.799 8.557 1.00 20.48 C ANISOU 384 C LEU A 65 2220 2907 2653 8 -506 22 C ATOM 385 O LEU A 65 -43.709 -21.888 7.990 1.00 18.86 O ANISOU 385 O LEU A 65 2096 2632 2438 -17 -468 79 O ATOM 386 CB LEU A 65 -41.734 -19.641 9.511 1.00 19.62 C ANISOU 386 CB LEU A 65 2050 2889 2517 -85 -537 -92 C ATOM 387 CG LEU A 65 -42.451 -18.625 8.623 1.00 17.15 C ANISOU 387 CG LEU A 65 1805 2503 2209 -184 -472 -86 C ATOM 388 CD1 LEU A 65 -43.773 -18.212 9.253 1.00 15.30 C ANISOU 388 CD1 LEU A 65 1661 2225 1927 -168 -482 -31 C ATOM 389 CD2 LEU A 65 -41.563 -17.414 8.385 1.00 12.28 C ANISOU 389 CD2 LEU A 65 1136 1909 1619 -282 -454 -171 C ATOM 390 N ALA A 66 -41.525 -22.437 8.113 1.00 20.19 N ANISOU 390 N ALA A 66 2101 2901 2668 36 -504 -29 N ATOM 391 CA ALA A 66 -41.593 -23.301 6.939 1.00 12.14 C ANISOU 391 CA ALA A 66 1092 1829 1690 39 -453 -25 C ATOM 392 C ALA A 66 -42.548 -24.466 7.154 1.00 15.30 C ANISOU 392 C ALA A 66 1568 2160 2087 111 -474 64 C ATOM 393 O ALA A 66 -43.198 -24.917 6.206 1.00 23.39 O ANISOU 393 O ALA A 66 2647 3118 3124 86 -429 86 O ATOM 394 CB ALA A 66 -40.199 -23.820 6.586 1.00 13.11 C ANISOU 394 CB ALA A 66 1099 2007 1875 74 -449 -109 C ATOM 395 N CYS A 67 -42.642 -24.966 8.388 1.00 20.53 N ANISOU 395 N CYS A 67 2235 2837 2727 193 -545 118 N ATOM 396 CA CYS A 67 -43.602 -26.023 8.689 1.00 17.81 C ANISOU 396 CA CYS A 67 1968 2423 2377 247 -563 215 C ATOM 397 C CYS A 67 -45.029 -25.526 8.512 1.00 15.96 C ANISOU 397 C CYS A 67 1824 2142 2100 182 -524 273 C ATOM 398 O CYS A 67 -45.853 -26.192 7.871 1.00 16.46 O ANISOU 398 O CYS A 67 1942 2129 2182 171 -496 317 O ATOM 399 CB CYS A 67 -43.387 -26.547 10.108 1.00 12.64 C ANISOU 399 CB CYS A 67 1306 1805 1691 338 -645 272 C ATOM 400 SG CYS A 67 -42.081 -27.776 10.240 1.00 28.48 S ANISOU 400 SG CYS A 67 3231 3817 3774 456 -707 250 S ATOM 401 N ALA A 68 -45.342 -24.354 9.072 1.00 13.04 N ANISOU 401 N ALA A 68 1463 1815 1676 140 -526 266 N ATOM 402 CA ALA A 68 -46.679 -23.798 8.880 1.00 13.51 C ANISOU 402 CA ALA A 68 1594 1832 1706 86 -490 311 C ATOM 403 C ALA A 68 -46.988 -23.610 7.399 1.00 23.44 C ANISOU 403 C ALA A 68 2874 3035 2998 16 -435 291 C ATOM 404 O ALA A 68 -48.076 -23.974 6.931 1.00 19.94 O ANISOU 404 O ALA A 68 2486 2534 2557 -1 -416 346 O ATOM 405 CB ALA A 68 -46.816 -22.477 9.634 1.00 9.93 C ANISOU 405 CB ALA A 68 1140 1428 1204 57 -498 283 C ATOM 406 N ASP A 69 -46.032 -23.068 6.638 1.00 25.86 N ANISOU 406 N ASP A 69 3134 3364 3326 -29 -410 215 N ATOM 407 CA ASP A 69 -46.268 -22.863 5.213 1.00 28.83 C ANISOU 407 CA ASP A 69 3537 3700 3715 -102 -356 199 C ATOM 408 C ASP A 69 -46.434 -24.184 4.468 1.00 21.18 C ANISOU 408 C ASP A 69 2585 2685 2776 -75 -343 212 C ATOM 409 O ASP A 69 -47.170 -24.245 3.476 1.00 16.59 O ANISOU 409 O ASP A 69 2056 2060 2188 -124 -313 229 O ATOM 410 CB ASP A 69 -45.131 -22.046 4.597 1.00 44.06 C ANISOU 410 CB ASP A 69 5412 5674 5655 -164 -323 118 C ATOM 411 CG ASP A 69 -44.909 -20.721 5.304 1.00 44.07 C ANISOU 411 CG ASP A 69 5399 5708 5639 -201 -338 94 C ATOM 412 OD1 ASP A 69 -43.747 -20.417 5.653 1.00 47.64 O ANISOU 412 OD1 ASP A 69 5773 6220 6107 -205 -348 27 O ATOM 413 OD2 ASP A 69 -45.895 -19.989 5.519 1.00 44.42 O ANISOU 413 OD2 ASP A 69 5503 5715 5659 -224 -343 135 O ATOM 414 N LEU A 70 -45.765 -25.246 4.921 1.00 21.06 N ANISOU 414 N LEU A 70 2530 2676 2796 5 -370 201 N ATOM 415 CA LEU A 70 -45.950 -26.550 4.290 1.00 21.95 C ANISOU 415 CA LEU A 70 2665 2726 2948 37 -361 207 C ATOM 416 C LEU A 70 -47.332 -27.115 4.597 1.00 19.81 C ANISOU 416 C LEU A 70 2471 2388 2669 44 -380 300 C ATOM 417 O LEU A 70 -47.975 -27.715 3.724 1.00 9.75 O ANISOU 417 O LEU A 70 1240 1054 1411 16 -359 307 O ATOM 418 CB LEU A 70 -44.857 -27.515 4.747 1.00 18.92 C ANISOU 418 CB LEU A 70 2217 2353 2617 132 -393 174 C ATOM 419 CG LEU A 70 -44.894 -28.925 4.152 1.00 15.63 C ANISOU 419 CG LEU A 70 1820 1857 2261 180 -387 165 C ATOM 420 CD1 LEU A 70 -44.839 -28.873 2.633 1.00 23.71 C ANISOU 420 CD1 LEU A 70 2851 2871 3286 111 -318 89 C ATOM 421 CD2 LEU A 70 -43.752 -29.762 4.700 1.00 12.63 C ANISOU 421 CD2 LEU A 70 1369 1485 1943 289 -429 134 C ATOM 422 N ILE A 71 -47.807 -26.928 5.831 1.00 16.26 N ANISOU 422 N ILE A 71 2034 1955 2189 75 -416 367 N ATOM 423 CA ILE A 71 -49.163 -27.347 6.173 1.00 21.06 C ANISOU 423 CA ILE A 71 2703 2513 2785 68 -422 457 C ATOM 424 C ILE A 71 -50.180 -26.594 5.324 1.00 35.30 C ANISOU 424 C ILE A 71 4542 4301 4570 -13 -389 461 C ATOM 425 O ILE A 71 -51.165 -27.175 4.850 1.00 37.81 O ANISOU 425 O ILE A 71 4900 4563 4903 -39 -383 501 O ATOM 426 CB ILE A 71 -49.422 -27.152 7.679 1.00 18.65 C ANISOU 426 CB ILE A 71 2401 2252 2436 110 -456 519 C ATOM 427 CG1 ILE A 71 -48.442 -27.994 8.500 1.00 17.42 C ANISOU 427 CG1 ILE A 71 2216 2111 2292 196 -499 525 C ATOM 428 CG2 ILE A 71 -50.860 -27.512 8.024 1.00 9.40 C ANISOU 428 CG2 ILE A 71 1277 1058 1238 89 -398 546 C ATOM 429 CD1 ILE A 71 -48.585 -27.824 9.993 1.00 10.74 C ANISOU 429 CD1 ILE A 71 1381 1328 1372 232 -498 544 C ATOM 430 N ILE A 72 -49.953 -25.296 5.106 1.00 38.71 N ANISOU 430 N ILE A 72 4959 4776 4972 -56 -374 421 N ATOM 431 CA ILE A 72 -50.872 -24.518 4.278 1.00 11.65 C ANISOU 431 CA ILE A 72 1567 1329 1529 -125 -354 433 C ATOM 432 C ILE A 72 -50.825 -24.994 2.831 1.00 23.68 C ANISOU 432 C ILE A 72 3112 2819 3067 -171 -331 402 C ATOM 433 O ILE A 72 -51.864 -25.129 2.173 1.00 27.02 O ANISOU 433 O ILE A 72 3574 3206 3487 -209 -332 435 O ATOM 434 CB ILE A 72 -50.555 -23.017 4.393 1.00 7.91 C ANISOU 434 CB ILE A 72 1081 893 1030 -159 -346 401 C ATOM 435 CG1 ILE A 72 -50.894 -22.512 5.795 1.00 7.89 C ANISOU 435 CG1 ILE A 72 1071 923 1006 -119 -368 425 C ATOM 436 CG2 ILE A 72 -51.319 -22.227 3.344 1.00 7.65 C ANISOU 436 CG2 ILE A 72 1088 830 987 -227 -332 414 C ATOM 437 CD1 ILE A 72 -52.349 -22.692 6.177 1.00 7.68 C ANISOU 437 CD1 ILE A 72 1069 877 974 -107 -355 474 C ATOM 438 N GLY A 73 -49.624 -25.267 2.316 1.00 15.04 N ANISOU 438 N GLY A 73 1985 1744 1986 -167 -310 332 N ATOM 439 CA GLY A 73 -49.498 -25.690 0.932 1.00 17.36 C ANISOU 439 CA GLY A 73 2298 2020 2278 -212 -279 287 C ATOM 440 C GLY A 73 -50.053 -27.074 0.659 1.00 22.05 C ANISOU 440 C GLY A 73 2922 2551 2906 -188 -290 299 C ATOM 441 O GLY A 73 -50.462 -27.368 -0.468 1.00 26.43 O ANISOU 441 O GLY A 73 3512 3082 3447 -238 -275 277 O ATOM 442 N VAL A 74 -50.079 -27.941 1.669 1.00 25.44 N ANISOU 442 N VAL A 74 3341 2949 3376 -118 -320 335 N ATOM 443 CA VAL A 74 -50.577 -29.299 1.459 1.00 23.43 C ANISOU 443 CA VAL A 74 3119 2615 3167 -99 -332 350 C ATOM 444 C VAL A 74 -52.091 -29.381 1.634 1.00 26.88 C ANISOU 444 C VAL A 74 3600 3015 3598 -137 -351 432 C ATOM 445 O VAL A 74 -52.771 -30.060 0.860 1.00 13.04 O ANISOU 445 O VAL A 74 1882 1209 1864 -176 -353 426 O ATOM 446 CB VAL A 74 -49.846 -30.284 2.395 1.00 28.54 C ANISOU 446 CB VAL A 74 3741 3233 3869 -6 -358 359 C ATOM 447 CG1 VAL A 74 -50.513 -31.651 2.357 1.00 10.64 C ANISOU 447 CG1 VAL A 74 1521 863 1659 9 -375 395 C ATOM 448 CG2 VAL A 74 -48.384 -30.405 1.996 1.00 21.16 C ANISOU 448 CG2 VAL A 74 2751 2330 2960 35 -338 261 C ATOM 449 N PHE A 75 -52.652 -28.696 2.632 1.00 21.59 N ANISOU 449 N PHE A 75 2919 2382 2900 -129 -360 492 N ATOM 450 CA PHE A 75 -54.065 -28.850 2.976 1.00 23.84 C ANISOU 450 CA PHE A 75 3198 2689 3170 -140 -331 499 C ATOM 451 C PHE A 75 -54.922 -27.673 2.516 1.00 24.60 C ANISOU 451 C PHE A 75 3284 2834 3230 -181 -317 482 C ATOM 452 O PHE A 75 -55.839 -27.850 1.708 1.00 28.90 O ANISOU 452 O PHE A 75 3837 3369 3777 -219 -319 474 O ATOM 453 CB PHE A 75 -54.216 -29.048 4.490 1.00 8.82 C ANISOU 453 CB PHE A 75 1280 817 1255 -87 -317 529 C ATOM 454 CG PHE A 75 -53.569 -30.299 5.007 1.00 9.49 C ANISOU 454 CG PHE A 75 1378 854 1375 -37 -333 554 C ATOM 455 CD1 PHE A 75 -54.164 -31.535 4.810 1.00 26.61 C ANISOU 455 CD1 PHE A 75 3571 2958 3580 -46 -328 570 C ATOM 456 CD2 PHE A 75 -52.374 -30.240 5.704 1.00 21.84 C ANISOU 456 CD2 PHE A 75 2927 2435 2938 23 -361 561 C ATOM 457 CE1 PHE A 75 -53.574 -32.692 5.290 1.00 10.78 C ANISOU 457 CE1 PHE A 75 1586 896 1615 5 -345 595 C ATOM 458 CE2 PHE A 75 -51.778 -31.393 6.188 1.00 16.67 C ANISOU 458 CE2 PHE A 75 2282 1733 2318 83 -382 584 C ATOM 459 CZ PHE A 75 -52.379 -32.621 5.978 1.00 11.05 C ANISOU 459 CZ PHE A 75 1604 947 1646 75 -372 602 C ATOM 460 N SER A 76 -54.639 -26.469 3.020 1.00 21.76 N ANISOU 460 N SER A 76 2906 2520 2842 -171 -311 476 N ATOM 461 CA SER A 76 -55.566 -25.352 2.857 1.00 20.41 C ANISOU 461 CA SER A 76 2723 2381 2652 -190 -300 464 C ATOM 462 C SER A 76 -55.731 -24.952 1.395 1.00 17.06 C ANISOU 462 C SER A 76 2318 1948 2216 -242 -313 446 C ATOM 463 O SER A 76 -56.848 -24.649 0.954 1.00 14.96 O ANISOU 463 O SER A 76 2046 1690 1949 -257 -319 446 O ATOM 464 CB SER A 76 -55.099 -24.159 3.691 1.00 17.26 C ANISOU 464 CB SER A 76 2311 2013 2234 -171 -297 461 C ATOM 465 OG SER A 76 -55.182 -24.446 5.077 1.00 14.58 O ANISOU 465 OG SER A 76 1959 1694 1888 -126 -288 481 O ATOM 466 N MET A 77 -54.638 -24.939 0.629 1.00 16.22 N ANISOU 466 N MET A 77 2240 1827 2097 -273 -320 437 N ATOM 467 CA MET A 77 -54.729 -24.550 -0.776 1.00 19.66 C ANISOU 467 CA MET A 77 2707 2262 2501 -331 -326 423 C ATOM 468 C MET A 77 -55.609 -25.518 -1.560 1.00 21.21 C ANISOU 468 C MET A 77 2922 2436 2702 -355 -344 423 C ATOM 469 O MET A 77 -56.512 -25.101 -2.298 1.00 23.66 O ANISOU 469 O MET A 77 3237 2761 2990 -382 -364 425 O ATOM 470 CB MET A 77 -53.331 -24.470 -1.389 1.00 11.27 C ANISOU 470 CB MET A 77 1677 1189 1417 -381 -315 412 C ATOM 471 CG MET A 77 -52.621 -23.144 -1.162 1.00 7.97 C ANISOU 471 CG MET A 77 1249 800 978 -399 -301 409 C ATOM 472 SD MET A 77 -50.975 -23.117 -1.901 1.00 17.80 S ANISOU 472 SD MET A 77 2478 2084 2201 -438 -248 330 S ATOM 473 CE MET A 77 -50.650 -21.359 -1.967 1.00 8.49 C ANISOU 473 CE MET A 77 1309 924 994 -495 -236 347 C ATOM 474 N ASN A 78 -55.372 -26.820 -1.395 1.00 15.20 N ANISOU 474 N ASN A 78 2172 1628 1975 -348 -347 425 N ATOM 475 CA ASN A 78 -56.133 -27.809 -2.148 1.00 8.75 C ANISOU 475 CA ASN A 78 1380 774 1169 -383 -368 420 C ATOM 476 C ASN A 78 -57.578 -27.887 -1.674 1.00 8.68 C ANISOU 476 C ASN A 78 1333 786 1179 -366 -379 443 C ATOM 477 O ASN A 78 -58.490 -28.092 -2.481 1.00 11.26 O ANISOU 477 O ASN A 78 1670 1109 1498 -409 -411 445 O ATOM 478 CB ASN A 78 -55.455 -29.170 -2.047 1.00 9.21 C ANISOU 478 CB ASN A 78 1465 753 1280 -376 -368 407 C ATOM 479 CG ASN A 78 -54.106 -29.185 -2.718 1.00 9.50 C ANISOU 479 CG ASN A 78 1515 793 1299 -383 -340 335 C ATOM 480 OD1 ASN A 78 -54.014 -29.272 -3.941 1.00 9.89 O ANISOU 480 OD1 ASN A 78 1594 856 1308 -433 -329 275 O ATOM 481 ND2 ASN A 78 -53.049 -29.087 -1.925 1.00 9.42 N ANISOU 481 ND2 ASN A 78 1468 801 1310 -321 -319 321 N ATOM 482 N LEU A 79 -57.810 -27.729 -0.372 1.00 8.42 N ANISOU 482 N LEU A 79 1257 774 1166 -314 -356 461 N ATOM 483 CA LEU A 79 -59.182 -27.761 0.121 1.00 8.48 C ANISOU 483 CA LEU A 79 1230 800 1192 -312 -360 484 C ATOM 484 C LEU A 79 -59.968 -26.544 -0.357 1.00 8.33 C ANISOU 484 C LEU A 79 1192 819 1153 -328 -380 486 C ATOM 485 O LEU A 79 -61.150 -26.660 -0.705 1.00 22.27 O ANISOU 485 O LEU A 79 2939 2588 2933 -357 -412 507 O ATOM 486 CB LEU A 79 -59.190 -27.863 1.647 1.00 12.02 C ANISOU 486 CB LEU A 79 1652 1261 1653 -263 -325 505 C ATOM 487 CG LEU A 79 -58.848 -29.247 2.217 1.00 10.36 C ANISOU 487 CG LEU A 79 1459 1006 1471 -248 -314 523 C ATOM 488 CD1 LEU A 79 -58.760 -29.204 3.729 1.00 8.83 C ANISOU 488 CD1 LEU A 79 1252 837 1268 -203 -284 550 C ATOM 489 CD2 LEU A 79 -59.869 -30.290 1.772 1.00 9.37 C ANISOU 489 CD2 LEU A 79 1338 842 1381 -290 -330 540 C ATOM 490 N TYR A 80 -59.329 -25.372 -0.403 1.00 21.14 N ANISOU 490 N TYR A 80 2819 2463 2750 -314 -369 470 N ATOM 491 CA TYR A 80 -60.024 -24.190 -0.902 1.00 22.60 C ANISOU 491 CA TYR A 80 2995 2668 2924 -326 -392 475 C ATOM 492 C TYR A 80 -60.269 -24.287 -2.403 1.00 20.42 C ANISOU 492 C TYR A 80 2752 2385 2620 -383 -439 477 C ATOM 493 O TYR A 80 -61.321 -23.857 -2.895 1.00 17.16 O ANISOU 493 O TYR A 80 2326 1980 2213 -405 -480 500 O ATOM 494 CB TYR A 80 -59.237 -22.927 -0.563 1.00 7.74 C ANISOU 494 CB TYR A 80 1118 797 1026 -302 -369 460 C ATOM 495 CG TYR A 80 -59.980 -21.656 -0.896 1.00 11.93 C ANISOU 495 CG TYR A 80 1643 1331 1559 -304 -389 472 C ATOM 496 CD1 TYR A 80 -61.189 -21.356 -0.279 1.00 8.43 C ANISOU 496 CD1 TYR A 80 1162 891 1149 -283 -397 497 C ATOM 497 CD2 TYR A 80 -59.474 -20.754 -1.821 1.00 22.44 C ANISOU 497 CD2 TYR A 80 3008 2657 2860 -328 -401 467 C ATOM 498 CE1 TYR A 80 -61.874 -20.195 -0.579 1.00 10.93 C ANISOU 498 CE1 TYR A 80 1474 1200 1477 -277 -422 516 C ATOM 499 CE2 TYR A 80 -60.151 -19.588 -2.125 1.00 25.46 C ANISOU 499 CE2 TYR A 80 3391 3030 3250 -325 -424 486 C ATOM 500 CZ TYR A 80 -61.350 -19.313 -1.501 1.00 20.41 C ANISOU 500 CZ TYR A 80 2714 2388 2652 -295 -436 509 C ATOM 501 OH TYR A 80 -62.026 -18.154 -1.804 1.00 15.15 O ANISOU 501 OH TYR A 80 2051 1703 2002 -284 -465 534 O ATOM 502 N THR A 81 -59.311 -24.850 -3.147 1.00 21.02 N ANISOU 502 N THR A 81 2876 2446 2663 -415 -438 459 N ATOM 503 CA THR A 81 -59.551 -25.121 -4.561 1.00 14.54 C ANISOU 503 CA THR A 81 2105 1621 1799 -483 -484 463 C ATOM 504 C THR A 81 -60.737 -26.062 -4.740 1.00 20.07 C ANISOU 504 C THR A 81 2795 2305 2527 -511 -530 484 C ATOM 505 O THR A 81 -61.593 -25.837 -5.604 1.00 19.26 O ANISOU 505 O THR A 81 2703 2212 2401 -560 -592 506 O ATOM 506 CB THR A 81 -58.301 -25.712 -5.211 1.00 9.26 C ANISOU 506 CB THR A 81 1497 931 1089 -522 -463 436 C ATOM 507 OG1 THR A 81 -57.200 -24.813 -5.040 1.00 27.95 O ANISOU 507 OG1 THR A 81 3869 3318 3434 -508 -422 424 O ATOM 508 CG2 THR A 81 -58.531 -25.942 -6.698 1.00 9.94 C ANISOU 508 CG2 THR A 81 1653 1018 1107 -610 -505 434 C ATOM 509 N LEU A 82 -60.807 -27.116 -3.922 1.00 22.07 N ANISOU 509 N LEU A 82 3026 2529 2829 -486 -507 482 N ATOM 510 CA LEU A 82 -61.942 -28.032 -3.983 1.00 9.91 C ANISOU 510 CA LEU A 82 1470 968 1326 -517 -543 503 C ATOM 511 C LEU A 82 -63.251 -27.297 -3.729 1.00 36.51 C ANISOU 511 C LEU A 82 4781 4373 4717 -517 -579 546 C ATOM 512 O LEU A 82 -64.243 -27.507 -4.443 1.00 10.56 O ANISOU 512 O LEU A 82 1492 1086 1434 -571 -646 574 O ATOM 513 CB LEU A 82 -61.755 -29.158 -2.967 1.00 9.93 C ANISOU 513 CB LEU A 82 1457 932 1384 -485 -498 500 C ATOM 514 CG LEU A 82 -62.669 -30.370 -3.136 1.00 14.38 C ANISOU 514 CG LEU A 82 2018 1453 1993 -529 -522 509 C ATOM 515 CD1 LEU A 82 -62.242 -31.161 -4.357 1.00 18.24 C ANISOU 515 CD1 LEU A 82 2572 1890 2468 -587 -545 461 C ATOM 516 CD2 LEU A 82 -62.664 -31.246 -1.892 1.00 10.74 C ANISOU 516 CD2 LEU A 82 1534 961 1585 -493 -474 525 C ATOM 517 N TYR A 83 -63.264 -26.415 -2.725 1.00 17.13 N ANISOU 517 N TYR A 83 2281 1945 2280 -461 -540 552 N ATOM 518 CA TYR A 83 -64.475 -25.672 -2.395 1.00 23.74 C ANISOU 518 CA TYR A 83 3061 2807 3153 -458 -566 592 C ATOM 519 C TYR A 83 -64.910 -24.779 -3.552 1.00 23.17 C ANISOU 519 C TYR A 83 3001 2743 3058 -494 -629 606 C ATOM 520 O TYR A 83 -66.085 -24.768 -3.937 1.00 18.01 O ANISOU 520 O TYR A 83 2314 2093 2436 -533 -694 651 O ATOM 521 CB TYR A 83 -64.245 -24.845 -1.129 1.00 18.67 C ANISOU 521 CB TYR A 83 2388 2182 2524 -393 -504 587 C ATOM 522 CG TYR A 83 -65.465 -24.096 -0.647 1.00 28.56 C ANISOU 522 CG TYR A 83 3580 3451 3820 -383 -521 632 C ATOM 523 CD1 TYR A 83 -65.647 -22.752 -0.953 1.00 34.87 C ANISOU 523 CD1 TYR A 83 4379 4252 4617 -364 -536 634 C ATOM 524 CD2 TYR A 83 -66.435 -24.732 0.117 1.00 39.20 C ANISOU 524 CD2 TYR A 83 4871 4809 5215 -393 -520 680 C ATOM 525 CE1 TYR A 83 -66.761 -22.064 -0.513 1.00 43.13 C ANISOU 525 CE1 TYR A 83 5369 5305 5713 -344 -552 679 C ATOM 526 CE2 TYR A 83 -67.551 -24.052 0.563 1.00 48.96 C ANISOU 526 CE2 TYR A 83 6041 6063 6500 -384 -536 735 C ATOM 527 CZ TYR A 83 -67.710 -22.719 0.245 1.00 50.05 C ANISOU 527 CZ TYR A 83 6179 6199 6640 -354 -553 732 C ATOM 528 OH TYR A 83 -68.821 -22.041 0.689 1.00 53.15 O ANISOU 528 OH TYR A 83 6501 6604 7089 -327 -569 785 O ATOM 529 N THR A 84 -63.971 -24.020 -4.123 1.00 25.38 N ANISOU 529 N THR A 84 3330 3024 3289 -487 -613 575 N ATOM 530 CA THR A 84 -64.339 -23.083 -5.179 1.00 25.01 C ANISOU 530 CA THR A 84 3305 2981 3218 -516 -661 593 C ATOM 531 C THR A 84 -64.760 -23.814 -6.449 1.00 24.28 C ANISOU 531 C THR A 84 3253 2883 3090 -600 -738 612 C ATOM 532 O THR A 84 -65.734 -23.421 -7.103 1.00 13.10 O ANISOU 532 O THR A 84 1828 1466 1682 -629 -797 650 O ATOM 533 CB THR A 84 -63.180 -22.127 -5.466 1.00 31.23 C ANISOU 533 CB THR A 84 4139 3770 3958 -495 -620 564 C ATOM 534 OG1 THR A 84 -62.029 -22.873 -5.876 1.00 46.05 O ANISOU 534 OG1 THR A 84 6067 5646 5784 -524 -598 532 O ATOM 535 CG2 THR A 84 -62.837 -21.316 -4.224 1.00 28.83 C ANISOU 535 CG2 THR A 84 3802 3465 3686 -424 -560 550 C ATOM 536 N VAL A 85 -64.047 -24.884 -6.807 1.00 28.08 N ANISOU 536 N VAL A 85 3785 3355 3528 -638 -738 586 N ATOM 537 CA VAL A 85 -64.357 -25.610 -8.037 1.00 22.48 C ANISOU 537 CA VAL A 85 3137 2637 2766 -732 -816 599 C ATOM 538 C VAL A 85 -65.696 -26.327 -7.920 1.00 31.25 C ANISOU 538 C VAL A 85 4206 3740 3928 -755 -876 643 C ATOM 539 O VAL A 85 -66.508 -26.309 -8.853 1.00 32.30 O ANISOU 539 O VAL A 85 4361 3868 4045 -806 -930 676 O ATOM 540 CB VAL A 85 -63.219 -26.589 -8.379 1.00 15.03 C ANISOU 540 CB VAL A 85 2272 1673 1764 -755 -778 554 C ATOM 541 CG1 VAL A 85 -63.654 -27.553 -9.474 1.00 12.65 C ANISOU 541 CG1 VAL A 85 2019 1361 1427 -835 -822 525 C ATOM 542 CG2 VAL A 85 -61.982 -25.824 -8.806 1.00 19.79 C ANISOU 542 CG2 VAL A 85 2925 2295 2299 -755 -729 526 C ATOM 543 N ILE A 86 -65.954 -26.967 -6.780 1.00 28.43 N ANISOU 543 N ILE A 86 3790 3373 3640 -710 -841 646 N ATOM 544 CA ILE A 86 -67.207 -27.699 -6.642 1.00 16.52 C ANISOU 544 CA ILE A 86 2230 1853 2192 -736 -871 676 C ATOM 545 C ILE A 86 -68.376 -26.751 -6.393 1.00 18.63 C ANISOU 545 C ILE A 86 2428 2141 2508 -727 -923 758 C ATOM 546 O ILE A 86 -69.495 -27.004 -6.854 1.00 27.38 O ANISOU 546 O ILE A 86 3494 3261 3647 -760 -963 761 O ATOM 547 CB ILE A 86 -67.064 -28.755 -5.533 1.00 24.45 C ANISOU 547 CB ILE A 86 3201 2829 3259 -704 -791 645 C ATOM 548 CG1 ILE A 86 -66.041 -29.805 -5.969 1.00 37.80 C ANISOU 548 CG1 ILE A 86 4964 4474 4925 -722 -750 571 C ATOM 549 CG2 ILE A 86 -68.400 -29.401 -5.209 1.00 13.11 C ANISOU 549 CG2 ILE A 86 1695 1391 1896 -736 -808 671 C ATOM 550 CD1 ILE A 86 -65.885 -30.952 -5.011 1.00 51.79 C ANISOU 550 CD1 ILE A 86 6718 6199 6762 -698 -684 551 C ATOM 551 N GLY A 87 -68.141 -25.639 -5.703 1.00 18.66 N ANISOU 551 N GLY A 87 2383 2161 2544 -679 -875 741 N ATOM 552 CA GLY A 87 -69.186 -24.693 -5.382 1.00 14.18 C ANISOU 552 CA GLY A 87 1748 1602 2037 -649 -882 788 C ATOM 553 C GLY A 87 -69.788 -24.869 -4.006 1.00 24.68 C ANISOU 553 C GLY A 87 2985 2945 3445 -619 -849 824 C ATOM 554 O GLY A 87 -70.584 -24.021 -3.584 1.00 31.60 O ANISOU 554 O GLY A 87 3802 3842 4364 -565 -842 850 O ATOM 555 N TYR A 88 -69.440 -25.943 -3.304 1.00 27.40 N ANISOU 555 N TYR A 88 3324 3298 3789 -614 -822 814 N ATOM 556 CA TYR A 88 -69.884 -26.162 -1.934 1.00 18.46 C ANISOU 556 CA TYR A 88 2124 2178 2711 -579 -754 842 C ATOM 557 C TYR A 88 -68.893 -27.104 -1.266 1.00 19.78 C ANISOU 557 C TYR A 88 2345 2326 2846 -554 -664 784 C ATOM 558 O TYR A 88 -67.966 -27.611 -1.902 1.00 26.64 O ANISOU 558 O TYR A 88 3288 3168 3666 -561 -661 731 O ATOM 559 CB TYR A 88 -71.314 -26.716 -1.887 1.00 15.41 C ANISOU 559 CB TYR A 88 1657 1802 2395 -627 -779 891 C ATOM 560 CG TYR A 88 -71.496 -28.082 -2.515 1.00 15.10 C ANISOU 560 CG TYR A 88 1650 1738 2347 -688 -786 846 C ATOM 561 CD1 TYR A 88 -71.390 -29.238 -1.752 1.00 16.08 C ANISOU 561 CD1 TYR A 88 1780 1840 2490 -699 -713 825 C ATOM 562 CD2 TYR A 88 -71.795 -28.214 -3.865 1.00 14.35 C ANISOU 562 CD2 TYR A 88 1585 1640 2227 -735 -862 821 C ATOM 563 CE1 TYR A 88 -71.563 -30.488 -2.317 1.00 22.95 C ANISOU 563 CE1 TYR A 88 2679 2673 3370 -759 -719 783 C ATOM 564 CE2 TYR A 88 -71.971 -29.461 -4.441 1.00 14.99 C ANISOU 564 CE2 TYR A 88 1691 1697 2307 -795 -867 768 C ATOM 565 CZ TYR A 88 -71.854 -30.595 -3.661 1.00 25.70 C ANISOU 565 CZ TYR A 88 3049 3019 3699 -808 -796 750 C ATOM 566 OH TYR A 88 -72.027 -31.841 -4.222 1.00 24.69 O ANISOU 566 OH TYR A 88 2947 2851 3585 -871 -801 696 O ATOM 567 N TRP A 89 -69.093 -27.328 0.035 1.00 20.04 N ANISOU 567 N TRP A 89 2337 2371 2906 -526 -595 804 N ATOM 568 CA TRP A 89 -68.221 -28.210 0.797 1.00 15.32 C ANISOU 568 CA TRP A 89 1786 1750 2284 -502 -520 767 C ATOM 569 C TRP A 89 -68.721 -29.645 0.664 1.00 19.08 C ANISOU 569 C TRP A 89 2267 2190 2794 -558 -519 773 C ATOM 570 O TRP A 89 -69.813 -29.952 1.171 1.00 15.60 O ANISOU 570 O TRP A 89 1762 1763 2401 -592 -508 820 O ATOM 571 CB TRP A 89 -68.168 -27.794 2.260 1.00 11.25 C ANISOU 571 CB TRP A 89 1240 1265 1769 -454 -451 790 C ATOM 572 CG TRP A 89 -67.246 -28.644 3.074 1.00 11.07 C ANISOU 572 CG TRP A 89 1269 1219 1717 -428 -389 765 C ATOM 573 CD1 TRP A 89 -67.597 -29.558 4.023 1.00 11.63 C ANISOU 573 CD1 TRP A 89 1332 1283 1805 -443 -344 801 C ATOM 574 CD2 TRP A 89 -65.817 -28.676 2.994 1.00 14.96 C ANISOU 574 CD2 TRP A 89 1828 1690 2165 -388 -369 707 C ATOM 575 NE1 TRP A 89 -66.475 -30.151 4.547 1.00 36.47 N ANISOU 575 NE1 TRP A 89 4539 4399 4917 -409 -307 775 N ATOM 576 CE2 TRP A 89 -65.368 -29.626 3.933 1.00 21.14 C ANISOU 576 CE2 TRP A 89 2638 2451 2943 -373 -322 717 C ATOM 577 CE3 TRP A 89 -64.872 -27.988 2.226 1.00 9.83 C ANISOU 577 CE3 TRP A 89 1214 1039 1481 -366 -385 655 C ATOM 578 CZ2 TRP A 89 -64.015 -29.907 4.123 1.00 26.11 C ANISOU 578 CZ2 TRP A 89 3321 3056 3542 -333 -301 681 C ATOM 579 CZ3 TRP A 89 -63.529 -28.269 2.416 1.00 9.45 C ANISOU 579 CZ3 TRP A 89 1216 971 1404 -333 -355 616 C ATOM 580 CH2 TRP A 89 -63.114 -29.221 3.355 1.00 9.68 C ANISOU 580 CH2 TRP A 89 1263 979 1437 -314 -317 631 C ATOM 581 N PRO A 90 -67.982 -30.535 0.015 1.00 21.88 N ANISOU 581 N PRO A 90 2689 2492 3130 -574 -522 726 N ATOM 582 CA PRO A 90 -68.479 -31.895 -0.263 1.00 19.88 C ANISOU 582 CA PRO A 90 2447 2188 2919 -635 -525 720 C ATOM 583 C PRO A 90 -67.997 -32.983 0.687 1.00 22.38 C ANISOU 583 C PRO A 90 2795 2457 3253 -622 -457 722 C ATOM 584 O PRO A 90 -68.417 -34.132 0.523 1.00 36.25 O ANISOU 584 O PRO A 90 4562 4158 5052 -675 -454 719 O ATOM 585 CB PRO A 90 -67.915 -32.142 -1.664 1.00 19.66 C ANISOU 585 CB PRO A 90 2480 2126 2863 -663 -574 665 C ATOM 586 CG PRO A 90 -66.558 -31.480 -1.596 1.00 13.99 C ANISOU 586 CG PRO A 90 1808 1417 2089 -599 -550 636 C ATOM 587 CD PRO A 90 -66.708 -30.276 -0.683 1.00 19.87 C ANISOU 587 CD PRO A 90 2503 2223 2824 -547 -529 671 C ATOM 588 N LEU A 91 -67.137 -32.670 1.652 1.00 20.97 N ANISOU 588 N LEU A 91 2634 2292 3042 -556 -408 726 N ATOM 589 CA LEU A 91 -66.509 -33.718 2.444 1.00 33.58 C ANISOU 589 CA LEU A 91 4275 3836 4648 -539 -358 733 C ATOM 590 C LEU A 91 -67.317 -34.064 3.691 1.00 47.77 C ANISOU 590 C LEU A 91 6040 5648 6464 -555 -312 797 C ATOM 591 O LEU A 91 -67.586 -35.241 3.951 1.00 71.92 O ANISOU 591 O LEU A 91 9120 8647 9559 -594 -291 818 O ATOM 592 CB LEU A 91 -65.084 -33.300 2.814 1.00 32.69 C ANISOU 592 CB LEU A 91 4202 3729 4488 -465 -335 705 C ATOM 593 CG LEU A 91 -64.199 -33.061 1.586 1.00 23.85 C ANISOU 593 CG LEU A 91 3119 2592 3351 -459 -370 645 C ATOM 594 CD1 LEU A 91 -62.790 -32.655 1.981 1.00 15.15 C ANISOU 594 CD1 LEU A 91 2045 1498 2213 -393 -345 621 C ATOM 595 CD2 LEU A 91 -64.180 -34.299 0.698 1.00 18.41 C ANISOU 595 CD2 LEU A 91 2472 1820 2705 -507 -391 620 C ATOM 596 N GLY A 92 -67.714 -33.059 4.465 1.00 31.01 N ANISOU 596 N GLY A 92 3866 3599 4317 -530 -293 829 N ATOM 597 CA GLY A 92 -68.519 -33.290 5.638 1.00 23.42 C ANISOU 597 CA GLY A 92 2869 2664 3364 -552 -243 894 C ATOM 598 C GLY A 92 -68.248 -32.287 6.738 1.00 32.89 C ANISOU 598 C GLY A 92 4052 3933 4514 -496 -206 916 C ATOM 599 O GLY A 92 -67.288 -31.512 6.688 1.00 29.89 O ANISOU 599 O GLY A 92 3697 3568 4093 -436 -216 876 O ATOM 600 N PRO A 93 -69.102 -32.289 7.765 1.00 25.72 N ANISOU 600 N PRO A 93 3098 3069 3604 -520 -157 978 N ATOM 601 CA PRO A 93 -68.914 -31.328 8.865 1.00 19.57 C ANISOU 601 CA PRO A 93 2301 2362 2771 -471 -116 1002 C ATOM 602 C PRO A 93 -67.686 -31.614 9.710 1.00 21.87 C ANISOU 602 C PRO A 93 2672 2636 3000 -419 -95 995 C ATOM 603 O PRO A 93 -67.032 -30.672 10.178 1.00 26.65 O ANISOU 603 O PRO A 93 3285 3285 3556 -362 -90 976 O ATOM 604 CB PRO A 93 -70.211 -31.473 9.671 1.00 15.31 C ANISOU 604 CB PRO A 93 1691 1879 2248 -525 -59 1073 C ATOM 605 CG PRO A 93 -70.659 -32.871 9.393 1.00 16.22 C ANISOU 605 CG PRO A 93 1828 1926 2407 -595 -57 1089 C ATOM 606 CD PRO A 93 -70.287 -33.140 7.963 1.00 18.35 C ANISOU 606 CD PRO A 93 2125 2128 2717 -600 -129 1028 C ATOM 607 N VAL A 94 -67.357 -32.889 9.927 1.00 14.59 N ANISOU 607 N VAL A 94 1811 1649 2083 -436 -85 1012 N ATOM 608 CA VAL A 94 -66.161 -33.228 10.694 1.00 28.55 C ANISOU 608 CA VAL A 94 3653 3396 3798 -383 -76 1013 C ATOM 609 C VAL A 94 -64.919 -32.682 10.003 1.00 13.44 C ANISOU 609 C VAL A 94 1767 1468 1873 -323 -117 938 C ATOM 610 O VAL A 94 -64.099 -31.985 10.614 1.00 15.35 O ANISOU 610 O VAL A 94 2024 1747 2060 -269 -114 923 O ATOM 611 CB VAL A 94 -66.066 -34.752 10.898 1.00 32.39 C ANISOU 611 CB VAL A 94 4200 3798 4306 -412 -65 1054 C ATOM 612 CG1 VAL A 94 -64.843 -35.102 11.735 1.00 15.73 C ANISOU 612 CG1 VAL A 94 2165 1668 2143 -351 -65 1069 C ATOM 613 CG2 VAL A 94 -67.334 -35.285 11.546 1.00 23.57 C ANISOU 613 CG2 VAL A 94 3057 2696 3202 -485 -17 1129 C ATOM 614 N VAL A 95 -64.769 -32.983 8.711 1.00 13.08 N ANISOU 614 N VAL A 95 1725 1371 1875 -339 -153 891 N ATOM 615 CA VAL A 95 -63.617 -32.494 7.961 1.00 12.17 C ANISOU 615 CA VAL A 95 1630 1246 1748 -294 -183 822 C ATOM 616 C VAL A 95 -63.637 -30.974 7.872 1.00 33.33 C ANISOU 616 C VAL A 95 4270 3993 4400 -270 -190 791 C ATOM 617 O VAL A 95 -62.581 -30.328 7.899 1.00 40.34 O ANISOU 617 O VAL A 95 5177 4895 5256 -224 -195 751 O ATOM 618 CB VAL A 95 -63.580 -33.152 6.567 1.00 15.40 C ANISOU 618 CB VAL A 95 2051 1592 2208 -327 -217 786 C ATOM 619 CG1 VAL A 95 -62.377 -32.668 5.773 1.00 11.38 C ANISOU 619 CG1 VAL A 95 1563 1077 1684 -289 -241 723 C ATOM 620 CG2 VAL A 95 -63.559 -34.668 6.700 1.00 13.13 C ANISOU 620 CG2 VAL A 95 1809 1221 1958 -350 -209 818 C ATOM 621 N CYS A 96 -64.828 -30.375 7.787 1.00 22.02 N ANISOU 621 N CYS A 96 2779 2601 2986 -303 -190 815 N ATOM 622 CA CYS A 96 -64.925 -28.919 7.738 1.00 19.97 C ANISOU 622 CA CYS A 96 2483 2394 2709 -278 -197 796 C ATOM 623 C CYS A 96 -64.377 -28.288 9.013 1.00 23.35 C ANISOU 623 C CYS A 96 2923 2867 3081 -231 -164 808 C ATOM 624 O CYS A 96 -63.544 -27.374 8.957 1.00 27.16 O ANISOU 624 O CYS A 96 3422 3361 3536 -192 -174 763 O ATOM 625 CB CYS A 96 -66.376 -28.494 7.503 1.00 19.14 C ANISOU 625 CB CYS A 96 2304 2322 2646 -318 -204 840 C ATOM 626 SG CYS A 96 -66.709 -26.757 7.877 1.00 29.08 S ANISOU 626 SG CYS A 96 3511 3645 3894 -281 -199 853 S ATOM 627 N ASP A 97 -64.827 -28.767 10.177 1.00 13.06 N ANISOU 627 N ASP A 97 1617 1592 1755 -239 -125 869 N ATOM 628 CA ASP A 97 -64.324 -28.211 11.430 1.00 13.63 C ANISOU 628 CA ASP A 97 1704 1717 1757 -197 -97 886 C ATOM 629 C ASP A 97 -62.843 -28.518 11.628 1.00 11.46 C ANISOU 629 C ASP A 97 1496 1411 1447 -154 -117 848 C ATOM 630 O ASP A 97 -62.114 -27.704 12.209 1.00 14.61 O ANISOU 630 O ASP A 97 1907 1848 1796 -112 -120 829 O ATOM 631 CB ASP A 97 -65.139 -28.731 12.614 1.00 29.41 C ANISOU 631 CB ASP A 97 3688 3761 3724 -222 -46 966 C ATOM 632 CG ASP A 97 -66.619 -28.422 12.485 1.00 31.71 C ANISOU 632 CG ASP A 97 3896 4099 4054 -267 -16 1011 C ATOM 633 OD1 ASP A 97 -67.441 -29.316 12.785 1.00 35.99 O ANISOU 633 OD1 ASP A 97 4423 4640 4613 -319 17 1064 O ATOM 634 OD2 ASP A 97 -66.962 -27.295 12.066 1.00 26.65 O ANISOU 634 OD2 ASP A 97 3203 3491 3433 -252 -25 998 O ATOM 635 N LEU A 98 -62.378 -29.678 11.157 1.00 11.58 N ANISOU 635 N LEU A 98 1550 1360 1490 -161 -132 841 N ATOM 636 CA LEU A 98 -60.949 -29.963 11.218 1.00 11.38 C ANISOU 636 CA LEU A 98 1573 1307 1444 -115 -154 811 C ATOM 637 C LEU A 98 -60.156 -28.942 10.414 1.00 10.46 C ANISOU 637 C LEU A 98 1444 1197 1331 -93 -178 741 C ATOM 638 O LEU A 98 -59.121 -28.446 10.873 1.00 11.22 O ANISOU 638 O LEU A 98 1556 1316 1390 -51 -190 722 O ATOM 639 CB LEU A 98 -60.667 -31.380 10.716 1.00 11.80 C ANISOU 639 CB LEU A 98 1662 1283 1539 -126 -165 823 C ATOM 640 CG LEU A 98 -61.130 -32.528 11.618 1.00 15.23 C ANISOU 640 CG LEU A 98 2130 1691 1966 -142 -144 900 C ATOM 641 CD1 LEU A 98 -60.792 -33.872 10.998 1.00 13.40 C ANISOU 641 CD1 LEU A 98 1938 1367 1788 -150 -159 908 C ATOM 642 CD2 LEU A 98 -60.525 -32.403 13.011 1.00 13.44 C ANISOU 642 CD2 LEU A 98 1936 1506 1663 -98 -140 938 C ATOM 643 N TRP A 99 -60.637 -28.599 9.218 1.00 13.03 N ANISOU 643 N TRP A 99 1743 1507 1699 -124 -188 708 N ATOM 644 CA TRP A 99 -59.914 -27.650 8.379 1.00 15.61 C ANISOU 644 CA TRP A 99 2066 1838 2028 -113 -207 649 C ATOM 645 C TRP A 99 -59.985 -26.234 8.944 1.00 14.45 C ANISOU 645 C TRP A 99 1901 1740 1849 -93 -202 642 C ATOM 646 O TRP A 99 -59.017 -25.471 8.836 1.00 13.93 O ANISOU 646 O TRP A 99 1845 1681 1766 -72 -215 606 O ATOM 647 CB TRP A 99 -60.461 -27.693 6.953 1.00 12.41 C ANISOU 647 CB TRP A 99 1646 1405 1666 -154 -225 625 C ATOM 648 CG TRP A 99 -59.715 -26.807 6.013 1.00 14.86 C ANISOU 648 CG TRP A 99 1959 1714 1971 -152 -243 575 C ATOM 649 CD1 TRP A 99 -58.387 -26.487 6.063 1.00 9.20 C ANISOU 649 CD1 TRP A 99 1261 999 1235 -127 -247 549 C ATOM 650 CD2 TRP A 99 -60.252 -26.111 4.885 1.00 16.02 C ANISOU 650 CD2 TRP A 99 2093 1862 2133 -182 -263 554 C ATOM 651 NE1 TRP A 99 -58.066 -25.641 5.031 1.00 9.85 N ANISOU 651 NE1 TRP A 99 1343 1080 1319 -146 -262 515 N ATOM 652 CE2 TRP A 99 -59.194 -25.392 4.295 1.00 12.71 C ANISOU 652 CE2 TRP A 99 1690 1441 1697 -177 -272 517 C ATOM 653 CE3 TRP A 99 -61.527 -26.024 4.318 1.00 8.38 C ANISOU 653 CE3 TRP A 99 1097 896 1190 -216 -282 572 C ATOM 654 CZ2 TRP A 99 -59.372 -24.597 3.166 1.00 9.53 C ANISOU 654 CZ2 TRP A 99 1290 1037 1295 -204 -293 497 C ATOM 655 CZ3 TRP A 99 -61.700 -25.237 3.197 1.00 8.20 C ANISOU 655 CZ3 TRP A 99 1073 873 1169 -236 -312 551 C ATOM 656 CH2 TRP A 99 -60.629 -24.532 2.634 1.00 8.03 C ANISOU 656 CH2 TRP A 99 1079 848 1123 -230 -314 513 C ATOM 657 N LEU A 100 -61.122 -25.859 9.537 1.00 17.81 N ANISOU 657 N LEU A 100 2296 2199 2270 -103 -185 681 N ATOM 658 CA LEU A 100 -61.227 -24.551 10.182 1.00 9.32 C ANISOU 658 CA LEU A 100 1206 1171 1165 -79 -181 685 C ATOM 659 C LEU A 100 -60.252 -24.441 11.346 1.00 13.19 C ANISOU 659 C LEU A 100 1723 1697 1590 -39 -179 688 C ATOM 660 O LEU A 100 -59.503 -23.460 11.461 1.00 22.50 O ANISOU 660 O LEU A 100 2910 2893 2745 -15 -198 657 O ATOM 661 CB LEU A 100 -62.658 -24.315 10.665 1.00 9.86 C ANISOU 661 CB LEU A 100 1223 1281 1241 -93 -156 746 C ATOM 662 CG LEU A 100 -63.739 -24.030 9.622 1.00 22.02 C ANISOU 662 CG LEU A 100 2719 2802 2847 -123 -172 754 C ATOM 663 CD1 LEU A 100 -65.115 -24.074 10.264 1.00 14.90 C ANISOU 663 CD1 LEU A 100 1750 1953 1958 -139 -138 836 C ATOM 664 CD2 LEU A 100 -63.496 -22.680 8.977 1.00 9.36 C ANISOU 664 CD2 LEU A 100 1116 1183 1257 -102 -201 714 C ATOM 665 N ALA A 101 -60.253 -25.446 12.225 1.00 22.52 N ANISOU 665 N ALA A 101 2923 2893 2741 -36 -163 730 N ATOM 666 CA ALA A 101 -59.318 -25.450 13.342 1.00 10.51 C ANISOU 666 CA ALA A 101 1432 1413 1150 3 -173 737 C ATOM 667 C ALA A 101 -57.878 -25.410 12.852 1.00 10.07 C ANISOU 667 C ALA A 101 1397 1327 1103 28 -212 686 C ATOM 668 O ALA A 101 -57.048 -24.680 13.401 1.00 10.11 O ANISOU 668 O ALA A 101 1405 1375 1062 58 -237 666 O ATOM 669 CB ALA A 101 -59.553 -26.680 14.215 1.00 11.37 C ANISOU 669 CB ALA A 101 1566 1523 1229 -1 -155 798 C ATOM 670 N LEU A 102 -57.568 -26.183 11.810 1.00 15.15 N ANISOU 670 N LEU A 102 2046 1907 1802 14 -219 667 N ATOM 671 CA LEU A 102 -56.208 -26.216 11.284 1.00 12.77 C ANISOU 671 CA LEU A 102 1752 1588 1513 36 -250 630 C ATOM 672 C LEU A 102 -55.786 -24.850 10.754 1.00 15.76 C ANISOU 672 C LEU A 102 2110 1984 1896 27 -265 586 C ATOM 673 O LEU A 102 -54.723 -24.333 11.114 1.00 15.09 O ANISOU 673 O LEU A 102 2020 1931 1784 51 -296 568 O ATOM 674 CB LEU A 102 -56.106 -27.282 10.192 1.00 13.05 C ANISOU 674 CB LEU A 102 1793 1559 1605 17 -251 626 C ATOM 675 CG LEU A 102 -54.733 -27.558 9.583 1.00 13.04 C ANISOU 675 CG LEU A 102 1792 1536 1626 37 -282 603 C ATOM 676 CD1 LEU A 102 -54.555 -29.053 9.402 1.00 18.11 C ANISOU 676 CD1 LEU A 102 2457 2121 2302 50 -288 631 C ATOM 677 CD2 LEU A 102 -54.576 -26.838 8.254 1.00 8.68 C ANISOU 677 CD2 LEU A 102 1224 970 1106 -2 -286 561 C ATOM 678 N ASP A 103 -56.615 -24.246 9.898 1.00 13.56 N ANISOU 678 N ASP A 103 1818 1686 1650 -8 -250 571 N ATOM 679 CA ASP A 103 -56.281 -22.940 9.337 1.00 14.24 C ANISOU 679 CA ASP A 103 1895 1773 1744 -22 -266 538 C ATOM 680 C ASP A 103 -56.098 -21.894 10.430 1.00 14.53 C ANISOU 680 C ASP A 103 1929 1861 1732 4 -283 542 C ATOM 681 O ASP A 103 -55.170 -21.075 10.368 1.00 9.34 O ANISOU 681 O ASP A 103 1270 1214 1064 1 -316 517 O ATOM 682 CB ASP A 103 -57.364 -22.500 8.350 1.00 16.94 C ANISOU 682 CB ASP A 103 2228 2085 2124 -56 -255 531 C ATOM 683 CG ASP A 103 -56.835 -22.331 6.935 1.00 25.77 C ANISOU 683 CG ASP A 103 3353 3168 3271 -91 -268 498 C ATOM 684 OD1 ASP A 103 -55.688 -22.750 6.670 1.00 23.88 O ANISOU 684 OD1 ASP A 103 3121 2922 3029 -94 -281 488 O ATOM 685 OD2 ASP A 103 -57.563 -21.773 6.088 1.00 21.64 O ANISOU 685 OD2 ASP A 103 2826 2626 2768 -115 -270 490 O ATOM 686 N TYR A 104 -56.965 -21.911 11.447 1.00 15.98 N ANISOU 686 N TYR A 104 2109 2085 1879 23 -264 577 N ATOM 687 CA TYR A 104 -56.886 -20.893 12.492 1.00 17.96 C ANISOU 687 CA TYR A 104 2353 2405 2067 49 -281 581 C ATOM 688 C TYR A 104 -55.668 -21.104 13.387 1.00 22.40 C ANISOU 688 C TYR A 104 2923 3023 2564 78 -314 565 C ATOM 689 O TYR A 104 -54.943 -20.151 13.702 1.00 26.90 O ANISOU 689 O TYR A 104 3485 3631 3104 86 -344 511 O ATOM 690 CB TYR A 104 -58.171 -20.889 13.316 1.00 16.95 C ANISOU 690 CB TYR A 104 2208 2328 1903 62 -243 630 C ATOM 691 CG TYR A 104 -59.130 -19.796 12.913 1.00 18.47 C ANISOU 691 CG TYR A 104 2375 2504 2139 62 -227 607 C ATOM 692 CD1 TYR A 104 -59.936 -19.932 11.791 1.00 23.72 C ANISOU 692 CD1 TYR A 104 3026 3106 2880 33 -230 642 C ATOM 693 CD2 TYR A 104 -59.226 -18.623 13.653 1.00 23.65 C ANISOU 693 CD2 TYR A 104 3021 3198 2766 95 -210 527 C ATOM 694 CE1 TYR A 104 -60.815 -18.933 11.416 1.00 25.52 C ANISOU 694 CE1 TYR A 104 3229 3310 3159 43 -222 610 C ATOM 695 CE2 TYR A 104 -60.102 -17.617 13.287 1.00 30.15 C ANISOU 695 CE2 TYR A 104 3821 3986 3647 107 -195 488 C ATOM 696 CZ TYR A 104 -60.895 -17.778 12.167 1.00 28.07 C ANISOU 696 CZ TYR A 104 3541 3660 3463 85 -204 535 C ATOM 697 OH TYR A 104 -61.767 -16.781 11.793 1.00 26.47 O ANISOU 697 OH TYR A 104 3313 3421 3325 108 -201 503 O ATOM 698 N VAL A 105 -55.434 -22.346 13.814 1.00 26.30 N ANISOU 698 N VAL A 105 3433 3514 3045 94 -305 589 N ATOM 699 CA VAL A 105 -54.268 -22.644 14.641 1.00 23.75 C ANISOU 699 CA VAL A 105 3117 3239 2669 129 -346 577 C ATOM 700 C VAL A 105 -52.985 -22.292 13.900 1.00 15.11 C ANISOU 700 C VAL A 105 2000 2132 1610 127 -392 530 C ATOM 701 O VAL A 105 -52.047 -21.735 14.484 1.00 41.72 O ANISOU 701 O VAL A 105 5350 5568 4933 143 -441 493 O ATOM 702 CB VAL A 105 -54.287 -24.122 15.080 1.00 10.90 C ANISOU 702 CB VAL A 105 1519 1585 1037 146 -338 624 C ATOM 703 CG1 VAL A 105 -52.945 -24.530 15.678 1.00 11.46 C ANISOU 703 CG1 VAL A 105 1595 1684 1075 189 -395 613 C ATOM 704 CG2 VAL A 105 -55.407 -24.364 16.080 1.00 11.53 C ANISOU 704 CG2 VAL A 105 1616 1704 1060 139 -299 677 C ATOM 705 N VAL A 106 -52.929 -22.585 12.599 1.00 9.49 N ANISOU 705 N VAL A 106 1283 1347 975 97 -378 525 N ATOM 706 CA VAL A 106 -51.710 -22.322 11.841 1.00 9.30 C ANISOU 706 CA VAL A 106 1233 1317 985 83 -420 489 C ATOM 707 C VAL A 106 -51.512 -20.824 11.630 1.00 9.15 C ANISOU 707 C VAL A 106 1201 1311 965 45 -433 431 C ATOM 708 O VAL A 106 -50.384 -20.324 11.700 1.00 38.57 O ANISOU 708 O VAL A 106 4897 5065 4692 38 -457 361 O ATOM 709 CB VAL A 106 -51.725 -23.092 10.508 1.00 8.89 C ANISOU 709 CB VAL A 106 1186 1190 1002 57 -398 498 C ATOM 710 CG1 VAL A 106 -50.583 -22.635 9.619 1.00 8.77 C ANISOU 710 CG1 VAL A 106 1143 1171 1019 27 -435 461 C ATOM 711 CG2 VAL A 106 -51.611 -24.586 10.770 1.00 36.05 C ANISOU 711 CG2 VAL A 106 4638 4609 4451 97 -391 527 C ATOM 712 N SER A 107 -52.590 -20.078 11.375 1.00 8.88 N ANISOU 712 N SER A 107 1186 1245 944 21 -401 434 N ATOM 713 CA SER A 107 -52.423 -18.634 11.212 1.00 22.63 C ANISOU 713 CA SER A 107 2926 2972 2700 -9 -397 357 C ATOM 714 C SER A 107 -51.985 -17.982 12.521 1.00 26.47 C ANISOU 714 C SER A 107 3400 3531 3128 18 -415 293 C ATOM 715 O SER A 107 -51.067 -17.149 12.529 1.00 24.64 O ANISOU 715 O SER A 107 3153 3305 2906 -7 -434 213 O ATOM 716 CB SER A 107 -53.711 -17.997 10.681 1.00 8.66 C ANISOU 716 CB SER A 107 1179 1146 966 -25 -369 378 C ATOM 717 OG SER A 107 -54.816 -18.251 11.526 1.00 13.20 O ANISOU 717 OG SER A 107 1753 1756 1507 13 -348 415 O ATOM 718 N ASN A 108 -52.609 -18.370 13.639 1.00 16.30 N ANISOU 718 N ASN A 108 2118 2302 1771 63 -408 325 N ATOM 719 CA ASN A 108 -52.214 -17.834 14.939 1.00 16.21 C ANISOU 719 CA ASN A 108 2101 2376 1682 90 -427 261 C ATOM 720 C ASN A 108 -50.770 -18.200 15.271 1.00 15.38 C ANISOU 720 C ASN A 108 1968 2325 1551 99 -484 231 C ATOM 721 O ASN A 108 -50.014 -17.376 15.806 1.00 15.76 O ANISOU 721 O ASN A 108 1998 2417 1575 90 -514 139 O ATOM 722 CB ASN A 108 -53.167 -18.349 16.020 1.00 18.93 C ANISOU 722 CB ASN A 108 2462 2788 1944 131 -401 315 C ATOM 723 CG ASN A 108 -52.986 -17.640 17.353 1.00 19.90 C ANISOU 723 CG ASN A 108 2586 3005 1971 156 -409 237 C ATOM 724 OD1 ASN A 108 -53.696 -16.682 17.658 1.00 15.93 O ANISOU 724 OD1 ASN A 108 2089 2502 1462 158 -373 175 O ATOM 725 ND2 ASN A 108 -52.038 -18.114 18.155 1.00 19.29 N ANISOU 725 ND2 ASN A 108 2504 3010 1817 178 -462 236 N ATOM 726 N ALA A 109 -50.369 -19.435 14.955 1.00 17.94 N ANISOU 726 N ALA A 109 2283 2644 1889 117 -504 303 N ATOM 727 CA ALA A 109 -48.983 -19.846 15.145 1.00 20.74 C ANISOU 727 CA ALA A 109 2598 3045 2240 136 -562 276 C ATOM 728 C ALA A 109 -48.038 -19.050 14.256 1.00 26.07 C ANISOU 728 C ALA A 109 3231 3687 2985 83 -566 187 C ATOM 729 O ALA A 109 -46.883 -18.818 14.632 1.00 33.76 O ANISOU 729 O ALA A 109 4156 4719 3950 84 -613 121 O ATOM 730 CB ALA A 109 -48.835 -21.343 14.870 1.00 17.15 C ANISOU 730 CB ALA A 109 2144 2567 1805 175 -578 369 C ATOM 731 N ARG A 110 -48.503 -18.625 13.078 1.00 18.97 N ANISOU 731 N ARG A 110 2351 2702 2156 31 -519 188 N ATOM 732 CA ARG A 110 -47.677 -17.786 12.217 1.00 11.68 C ANISOU 732 CA ARG A 110 1398 1747 1292 -34 -512 115 C ATOM 733 C ARG A 110 -47.476 -16.409 12.835 1.00 10.98 C ANISOU 733 C ARG A 110 1307 1675 1188 -66 -523 23 C ATOM 734 O ARG A 110 -46.350 -15.896 12.884 1.00 11.50 O ANISOU 734 O ARG A 110 1326 1771 1271 -102 -548 -55 O ATOM 735 CB ARG A 110 -48.310 -17.664 10.832 1.00 10.12 C ANISOU 735 CB ARG A 110 1235 1457 1153 -83 -464 152 C ATOM 736 CG ARG A 110 -47.578 -16.710 9.896 1.00 19.66 C ANISOU 736 CG ARG A 110 2429 2628 2413 -163 -446 92 C ATOM 737 CD ARG A 110 -48.341 -16.525 8.592 1.00 27.00 C ANISOU 737 CD ARG A 110 3406 3472 3380 -210 -406 141 C ATOM 738 NE ARG A 110 -48.765 -17.810 8.046 1.00 31.00 N ANISOU 738 NE ARG A 110 3922 3970 3887 -180 -396 209 N ATOM 739 CZ ARG A 110 -48.007 -18.579 7.273 1.00 26.31 C ANISOU 739 CZ ARG A 110 3300 3383 3312 -192 -385 204 C ATOM 740 NH1 ARG A 110 -46.782 -18.187 6.945 1.00 22.88 N ANISOU 740 NH1 ARG A 110 2818 2977 2897 -236 -378 138 N ATOM 741 NH2 ARG A 110 -48.474 -19.740 6.830 1.00 22.11 N ANISOU 741 NH2 ARG A 110 2785 2831 2785 -164 -379 258 N ATOM 742 N VAL A 111 -48.561 -15.797 13.316 1.00 14.28 N ANISOU 742 N VAL A 111 1771 2073 1581 -54 -503 25 N ATOM 743 CA VAL A 111 -48.450 -14.487 13.952 1.00 20.11 C ANISOU 743 CA VAL A 111 2515 2816 2309 -77 -512 -74 C ATOM 744 C VAL A 111 -47.514 -14.557 15.153 1.00 16.74 C ANISOU 744 C VAL A 111 2049 2499 1813 -53 -568 -140 C ATOM 745 O VAL A 111 -46.601 -13.734 15.303 1.00 17.66 O ANISOU 745 O VAL A 111 2134 2629 1948 -100 -596 -237 O ATOM 746 CB VAL A 111 -49.840 -13.963 14.352 1.00 18.07 C ANISOU 746 CB VAL A 111 2306 2526 2035 -48 -477 -65 C ATOM 747 CG1 VAL A 111 -49.716 -12.606 15.032 1.00 23.32 C ANISOU 747 CG1 VAL A 111 2980 3185 2696 -65 -486 -183 C ATOM 748 CG2 VAL A 111 -50.742 -13.876 13.136 1.00 13.74 C ANISOU 748 CG2 VAL A 111 1788 1874 1558 -68 -438 1 C ATOM 749 N MET A 112 -47.718 -15.552 16.022 1.00 15.19 N ANISOU 749 N MET A 112 1854 2385 1533 15 -590 -84 N ATOM 750 CA MET A 112 -46.873 -15.662 17.207 1.00 16.64 C ANISOU 750 CA MET A 112 2005 2685 1634 44 -656 -136 C ATOM 751 C MET A 112 -45.429 -15.983 16.845 1.00 13.88 C ANISOU 751 C MET A 112 1582 2366 1327 27 -708 -166 C ATOM 752 O MET A 112 -44.505 -15.523 17.524 1.00 14.84 O ANISOU 752 O MET A 112 1657 2562 1418 15 -766 -256 O ATOM 753 CB MET A 112 -47.438 -16.713 18.159 1.00 17.26 C ANISOU 753 CB MET A 112 2111 2839 1609 118 -667 -47 C ATOM 754 CG MET A 112 -48.838 -16.379 18.637 1.00 33.64 C ANISOU 754 CG MET A 112 4241 4907 3633 133 -608 -29 C ATOM 755 SD MET A 112 -49.117 -16.823 20.357 1.00 50.75 S ANISOU 755 SD MET A 112 6435 7221 5627 193 -633 -10 S ATOM 756 CE MET A 112 -48.959 -18.596 20.264 1.00 41.47 C ANISOU 756 CE MET A 112 5266 6042 4450 233 -653 151 C ATOM 757 N ASN A 113 -45.215 -16.755 15.780 1.00 13.24 N ANISOU 757 N ASN A 113 1481 2232 1317 24 -687 -103 N ATOM 758 CA ASN A 113 -43.855 -17.037 15.334 1.00 20.74 C ANISOU 758 CA ASN A 113 2348 3211 2320 9 -723 -141 C ATOM 759 C ASN A 113 -43.159 -15.764 14.864 1.00 17.96 C ANISOU 759 C ASN A 113 1959 2837 2029 -86 -711 -251 C ATOM 760 O ASN A 113 -42.001 -15.509 15.223 1.00 14.75 O ANISOU 760 O ASN A 113 1475 2501 1628 -106 -763 -332 O ATOM 761 CB ASN A 113 -43.885 -18.088 14.224 1.00 26.38 C ANISOU 761 CB ASN A 113 3057 3868 3098 24 -689 -63 C ATOM 762 CG ASN A 113 -42.501 -18.474 13.747 1.00 42.97 C ANISOU 762 CG ASN A 113 5063 6006 5258 20 -716 -108 C ATOM 763 OD1 ASN A 113 -41.947 -17.851 12.841 1.00 46.43 O ANISOU 763 OD1 ASN A 113 5464 6416 5762 -57 -678 -167 O ATOM 764 ND2 ASN A 113 -41.933 -19.510 14.355 1.00 46.58 N ANISOU 764 ND2 ASN A 113 5479 6527 5693 104 -780 -77 N ATOM 765 N LEU A 114 -43.857 -14.946 14.071 1.00 25.85 N ANISOU 765 N LEU A 114 3011 3734 3076 -149 -648 -251 N ATOM 766 CA LEU A 114 -43.286 -13.682 13.617 1.00 13.71 C ANISOU 766 CA LEU A 114 1456 2155 1600 -248 -632 -341 C ATOM 767 C LEU A 114 -43.005 -12.747 14.785 1.00 14.69 C ANISOU 767 C LEU A 114 1571 2327 1682 -262 -681 -448 C ATOM 768 O LEU A 114 -42.002 -12.024 14.782 1.00 27.72 O ANISOU 768 O LEU A 114 3166 3996 3372 -335 -703 -542 O ATOM 769 CB LEU A 114 -44.228 -13.016 12.618 1.00 15.35 C ANISOU 769 CB LEU A 114 1738 2235 1858 -298 -566 -301 C ATOM 770 CG LEU A 114 -44.365 -13.749 11.288 1.00 17.80 C ANISOU 770 CG LEU A 114 2055 2498 2209 -311 -518 -217 C ATOM 771 CD1 LEU A 114 -45.495 -13.165 10.480 1.00 11.71 C ANISOU 771 CD1 LEU A 114 1367 1615 1468 -341 -471 -164 C ATOM 772 CD2 LEU A 114 -43.059 -13.670 10.524 1.00 15.00 C ANISOU 772 CD2 LEU A 114 1627 2164 1908 -385 -506 -264 C ATOM 773 N LEU A 115 -43.884 -12.738 15.790 1.00 14.77 N ANISOU 773 N LEU A 115 1635 2364 1611 -199 -694 -441 N ATOM 774 CA LEU A 115 -43.616 -11.950 16.989 1.00 15.84 C ANISOU 774 CA LEU A 115 1766 2564 1689 -204 -743 -553 C ATOM 775 C LEU A 115 -42.367 -12.448 17.709 1.00 17.81 C ANISOU 775 C LEU A 115 1928 2946 1892 -187 -828 -599 C ATOM 776 O LEU A 115 -41.562 -11.647 18.199 1.00 20.47 O ANISOU 776 O LEU A 115 2236 3303 2240 -238 -855 -695 O ATOM 777 CB LEU A 115 -44.827 -11.982 17.919 1.00 15.85 C ANISOU 777 CB LEU A 115 1838 2587 1597 -134 -729 -532 C ATOM 778 CG LEU A 115 -45.988 -11.063 17.543 1.00 15.50 C ANISOU 778 CG LEU A 115 1865 2424 1599 -152 -663 -541 C ATOM 779 CD1 LEU A 115 -47.226 -11.409 18.349 1.00 15.45 C ANISOU 779 CD1 LEU A 115 1909 2457 1503 -72 -636 -500 C ATOM 780 CD2 LEU A 115 -45.606 -9.609 17.743 1.00 16.41 C ANISOU 780 CD2 LEU A 115 1987 2488 1760 -221 -675 -681 C ATOM 781 N ILE A 116 -42.186 -13.771 17.778 1.00 19.65 N ANISOU 781 N ILE A 116 2135 3239 2091 -112 -852 -504 N ATOM 782 CA ILE A 116 -40.987 -14.330 18.400 1.00 17.47 C ANISOU 782 CA ILE A 116 1797 3038 1803 -84 -905 -501 C ATOM 783 C ILE A 116 -39.737 -13.875 17.656 1.00 33.23 C ANISOU 783 C ILE A 116 3705 5019 3902 -161 -903 -569 C ATOM 784 O ILE A 116 -38.739 -13.477 18.272 1.00 24.08 O ANISOU 784 O ILE A 116 2495 3909 2743 -185 -945 -635 O ATOM 785 CB ILE A 116 -41.085 -15.867 18.460 1.00 23.87 C ANISOU 785 CB ILE A 116 2610 3874 2587 10 -920 -375 C ATOM 786 CG1 ILE A 116 -42.146 -16.302 19.475 1.00 17.20 C ANISOU 786 CG1 ILE A 116 1850 3056 1628 75 -920 -303 C ATOM 787 CG2 ILE A 116 -39.736 -16.478 18.802 1.00 18.18 C ANISOU 787 CG2 ILE A 116 1809 3211 1887 37 -977 -376 C ATOM 788 CD1 ILE A 116 -42.486 -17.777 19.413 1.00 16.83 C ANISOU 788 CD1 ILE A 116 1829 2995 1572 150 -917 -164 C ATOM 789 N ILE A 117 -39.773 -13.922 16.321 1.00 18.86 N ANISOU 789 N ILE A 117 1864 3134 2168 -207 -852 -552 N ATOM 790 CA ILE A 117 -38.629 -13.482 15.523 1.00 19.95 C ANISOU 790 CA ILE A 117 1921 3257 2402 -292 -829 -609 C ATOM 791 C ILE A 117 -38.346 -12.001 15.764 1.00 26.26 C ANISOU 791 C ILE A 117 2732 4018 3227 -392 -821 -707 C ATOM 792 O ILE A 117 -37.190 -11.588 15.947 1.00 19.43 O ANISOU 792 O ILE A 117 1798 3186 2398 -439 -840 -768 O ATOM 793 CB ILE A 117 -38.880 -13.773 14.032 1.00 21.41 C ANISOU 793 CB ILE A 117 2099 3379 2659 -333 -761 -568 C ATOM 794 CG1 ILE A 117 -38.926 -15.279 13.775 1.00 16.07 C ANISOU 794 CG1 ILE A 117 1396 2739 1972 -233 -773 -484 C ATOM 795 CG2 ILE A 117 -37.826 -13.114 13.167 1.00 25.17 C ANISOU 795 CG2 ILE A 117 2509 3830 3225 -441 -715 -623 C ATOM 796 CD1 ILE A 117 -39.169 -15.634 12.327 1.00 15.24 C ANISOU 796 CD1 ILE A 117 1309 2553 1930 -266 -687 -429 C ATOM 797 N SER A 118 -39.403 -11.183 15.773 1.00 23.21 N ANISOU 797 N SER A 118 2434 3555 2829 -423 -795 -726 N ATOM 798 CA SER A 118 -39.241 -9.741 15.938 1.00 22.59 C ANISOU 798 CA SER A 118 2383 3411 2789 -515 -785 -816 C ATOM 799 C SER A 118 -38.629 -9.403 17.293 1.00 20.02 C ANISOU 799 C SER A 118 2037 3164 2405 -496 -849 -891 C ATOM 800 O SER A 118 -37.674 -8.621 17.378 1.00 23.52 O ANISOU 800 O SER A 118 2439 3601 2896 -572 -859 -961 O ATOM 801 CB SER A 118 -40.590 -9.043 15.767 1.00 18.07 C ANISOU 801 CB SER A 118 1913 2736 2218 -527 -750 -822 C ATOM 802 OG SER A 118 -41.110 -9.256 14.466 1.00 20.12 O ANISOU 802 OG SER A 118 2200 2910 2537 -555 -689 -744 O ATOM 803 N PHE A 119 -39.171 -9.983 18.368 1.00 20.04 N ANISOU 803 N PHE A 119 2072 3244 2300 -400 -891 -872 N ATOM 804 CA PHE A 119 -38.627 -9.722 19.697 1.00 21.42 C ANISOU 804 CA PHE A 119 2234 3503 2403 -382 -953 -937 C ATOM 805 C PHE A 119 -37.207 -10.255 19.832 1.00 28.97 C ANISOU 805 C PHE A 119 3086 4541 3381 -380 -1004 -936 C ATOM 806 O PHE A 119 -36.366 -9.634 20.494 1.00 23.71 O ANISOU 806 O PHE A 119 2382 3915 2712 -421 -1048 -1018 O ATOM 807 CB PHE A 119 -39.530 -10.331 20.768 1.00 21.34 C ANISOU 807 CB PHE A 119 2285 3561 2261 -281 -977 -898 C ATOM 808 CG PHE A 119 -40.627 -9.418 21.222 1.00 25.84 C ANISOU 808 CG PHE A 119 2943 4086 2790 -288 -947 -962 C ATOM 809 CD1 PHE A 119 -40.366 -8.404 22.128 1.00 22.98 C ANISOU 809 CD1 PHE A 119 2598 3736 2399 -324 -972 -1077 C ATOM 810 CD2 PHE A 119 -41.920 -9.570 20.745 1.00 23.69 C ANISOU 810 CD2 PHE A 119 2733 3759 2511 -255 -896 -915 C ATOM 811 CE1 PHE A 119 -41.369 -7.558 22.551 1.00 22.96 C ANISOU 811 CE1 PHE A 119 2674 3686 2365 -322 -939 -1149 C ATOM 812 CE2 PHE A 119 -42.929 -8.727 21.168 1.00 20.42 C ANISOU 812 CE2 PHE A 119 2391 3302 2066 -251 -866 -986 C ATOM 813 CZ PHE A 119 -42.652 -7.720 22.073 1.00 21.80 C ANISOU 813 CZ PHE A 119 2584 3484 2216 -282 -885 -1105 C ATOM 814 N ASP A 120 -36.918 -11.400 19.209 1.00 21.67 N ANISOU 814 N ASP A 120 2111 3642 2482 -331 -999 -850 N ATOM 815 CA ASP A 120 -35.576 -11.966 19.291 1.00 22.62 C ANISOU 815 CA ASP A 120 2124 3839 2633 -317 -1046 -853 C ATOM 816 C ASP A 120 -34.554 -11.038 18.649 1.00 23.39 C ANISOU 816 C ASP A 120 2148 3907 2833 -430 -1022 -934 C ATOM 817 O ASP A 120 -33.491 -10.769 19.223 1.00 24.83 O ANISOU 817 O ASP A 120 2259 4154 3022 -453 -1075 -997 O ATOM 818 CB ASP A 120 -35.540 -13.339 18.626 1.00 21.81 C ANISOU 818 CB ASP A 120 1986 3748 2554 -241 -1035 -753 C ATOM 819 CG ASP A 120 -34.176 -13.983 18.714 1.00 29.13 C ANISOU 819 CG ASP A 120 2797 4751 3519 -212 -1084 -759 C ATOM 820 OD1 ASP A 120 -33.868 -14.576 19.768 1.00 40.92 O ANISOU 820 OD1 ASP A 120 4282 6320 4946 -137 -1161 -735 O ATOM 821 OD2 ASP A 120 -33.405 -13.886 17.739 1.00 37.04 O ANISOU 821 OD2 ASP A 120 3717 5739 4617 -264 -1044 -788 O ATOM 822 N ARG A 121 -34.862 -10.539 17.451 1.00 33.26 N ANISOU 822 N ARG A 121 3417 5059 4161 -506 -942 -929 N ATOM 823 CA ARG A 121 -33.962 -9.600 16.791 1.00 25.85 C ANISOU 823 CA ARG A 121 2424 4081 3317 -626 -907 -991 C ATOM 824 C ARG A 121 -33.839 -8.306 17.590 1.00 24.57 C ANISOU 824 C ARG A 121 2296 3893 3146 -695 -937 -1085 C ATOM 825 O ARG A 121 -32.735 -7.766 17.753 1.00 25.97 O ANISOU 825 O ARG A 121 2400 4101 3367 -761 -960 -1152 O ATOM 826 CB ARG A 121 -34.462 -9.323 15.373 1.00 26.55 C ANISOU 826 CB ARG A 121 2551 4061 3477 -694 -813 -948 C ATOM 827 CG ARG A 121 -33.505 -8.527 14.524 1.00 23.21 C ANISOU 827 CG ARG A 121 2073 3598 3149 -816 -762 -984 C ATOM 828 CD ARG A 121 -32.138 -9.168 14.533 1.00 41.19 C ANISOU 828 CD ARG A 121 4211 5986 5453 -801 -785 -1007 C ATOM 829 NE ARG A 121 -31.147 -8.324 13.879 1.00 44.43 N ANISOU 829 NE ARG A 121 4560 6374 5948 -924 -739 -1052 N ATOM 830 CZ ARG A 121 -29.848 -8.591 13.850 1.00 35.37 C ANISOU 830 CZ ARG A 121 3282 5317 4839 -937 -751 -1092 C ATOM 831 NH1 ARG A 121 -29.022 -7.762 13.233 1.00 37.26 N ANISOU 831 NH1 ARG A 121 3472 5534 5153 -1058 -703 -1129 N ATOM 832 NH2 ARG A 121 -29.378 -9.682 14.438 1.00 28.41 N ANISOU 832 NH2 ARG A 121 2321 4546 3927 -828 -814 -1091 N ATOM 833 N TYR A 122 -34.965 -7.807 18.110 1.00 24.15 N ANISOU 833 N TYR A 122 2350 3786 3038 -679 -937 -1098 N ATOM 834 CA TYR A 122 -34.952 -6.570 18.885 1.00 36.92 C ANISOU 834 CA TYR A 122 4011 5369 4646 -737 -962 -1197 C ATOM 835 C TYR A 122 -34.052 -6.688 20.109 1.00 38.36 C ANISOU 835 C TYR A 122 4131 5675 4769 -711 -1050 -1260 C ATOM 836 O TYR A 122 -33.288 -5.766 20.418 1.00 28.31 O ANISOU 836 O TYR A 122 2829 4396 3533 -793 -1076 -1349 O ATOM 837 CB TYR A 122 -36.379 -6.204 19.294 1.00 24.65 C ANISOU 837 CB TYR A 122 2578 3753 3035 -698 -945 -1204 C ATOM 838 CG TYR A 122 -36.470 -5.099 20.321 1.00 28.38 C ANISOU 838 CG TYR A 122 3100 4208 3476 -729 -978 -1315 C ATOM 839 CD1 TYR A 122 -36.335 -3.767 19.952 1.00 26.76 C ANISOU 839 CD1 TYR A 122 2928 3880 3358 -836 -951 -1381 C ATOM 840 CD2 TYR A 122 -36.703 -5.388 21.660 1.00 31.79 C ANISOU 840 CD2 TYR A 122 3551 4743 3787 -652 -1034 -1351 C ATOM 841 CE1 TYR A 122 -36.423 -2.756 20.891 1.00 28.10 C ANISOU 841 CE1 TYR A 122 3147 4026 3505 -861 -980 -1491 C ATOM 842 CE2 TYR A 122 -36.792 -4.383 22.604 1.00 27.95 C ANISOU 842 CE2 TYR A 122 3111 4245 3265 -680 -1060 -1464 C ATOM 843 CZ TYR A 122 -36.651 -3.071 22.214 1.00 28.69 C ANISOU 843 CZ TYR A 122 3234 4212 3455 -783 -1034 -1539 C ATOM 844 OH TYR A 122 -36.738 -2.070 23.153 1.00 42.34 O ANISOU 844 OH TYR A 122 5012 5922 5155 -808 -1060 -1658 O ATOM 845 N PHE A 123 -34.127 -7.817 20.818 1.00 29.70 N ANISOU 845 N PHE A 123 3018 4687 3581 -600 -1101 -1211 N ATOM 846 CA PHE A 123 -33.258 -8.021 21.971 1.00 28.25 C ANISOU 846 CA PHE A 123 2777 4623 3334 -571 -1193 -1256 C ATOM 847 C PHE A 123 -31.811 -8.235 21.553 1.00 36.47 C ANISOU 847 C PHE A 123 3684 5715 4457 -609 -1218 -1271 C ATOM 848 O PHE A 123 -30.894 -7.826 22.274 1.00 30.89 O ANISOU 848 O PHE A 123 2919 5075 3743 -643 -1285 -1347 O ATOM 849 CB PHE A 123 -33.753 -9.206 22.800 1.00 27.92 C ANISOU 849 CB PHE A 123 2765 4671 3174 -443 -1240 -1178 C ATOM 850 CG PHE A 123 -35.056 -8.952 23.498 1.00 32.38 C ANISOU 850 CG PHE A 123 3449 5217 3638 -405 -1225 -1181 C ATOM 851 CD1 PHE A 123 -35.334 -7.708 24.040 1.00 28.34 C ANISOU 851 CD1 PHE A 123 2992 4667 3108 -465 -1222 -1291 C ATOM 852 CD2 PHE A 123 -36.007 -9.953 23.605 1.00 26.38 C ANISOU 852 CD2 PHE A 123 2746 4475 2804 -309 -1209 -1077 C ATOM 853 CE1 PHE A 123 -36.530 -7.469 24.680 1.00 28.10 C ANISOU 853 CE1 PHE A 123 3063 4625 2986 -425 -1199 -1306 C ATOM 854 CE2 PHE A 123 -37.207 -9.719 24.244 1.00 26.13 C ANISOU 854 CE2 PHE A 123 2815 4436 2677 -276 -1186 -1083 C ATOM 855 CZ PHE A 123 -37.468 -8.475 24.782 1.00 26.99 C ANISOU 855 CZ PHE A 123 2971 4515 2768 -330 -1179 -1202 C ATOM 856 N CYS A 124 -31.584 -8.873 20.400 1.00 44.56 N ANISOU 856 N CYS A 124 4656 6718 5558 -605 -1164 -1204 N ATOM 857 CA CYS A 124 -30.220 -9.026 19.905 1.00 29.27 C ANISOU 857 CA CYS A 124 2584 4829 3706 -645 -1171 -1228 C ATOM 858 C CYS A 124 -29.572 -7.679 19.617 1.00 30.41 C ANISOU 858 C CYS A 124 2701 4923 3931 -787 -1147 -1320 C ATOM 859 O CYS A 124 -28.361 -7.521 19.805 1.00 31.97 O ANISOU 859 O CYS A 124 2789 5190 4170 -828 -1188 -1377 O ATOM 860 CB CYS A 124 -30.203 -9.894 18.646 1.00 28.27 C ANISOU 860 CB CYS A 124 2417 4680 3643 -619 -1102 -1149 C ATOM 861 SG CYS A 124 -30.271 -11.669 18.951 1.00 41.53 S ANISOU 861 SG CYS A 124 4068 6444 5268 -456 -1152 -1051 S ATOM 862 N VAL A 125 -30.352 -6.701 19.166 1.00 29.81 N ANISOU 862 N VAL A 125 2722 4723 3882 -863 -1085 -1332 N ATOM 863 CA VAL A 125 -29.788 -5.396 18.833 1.00 30.98 C ANISOU 863 CA VAL A 125 2858 4800 4114 -1002 -1060 -1405 C ATOM 864 C VAL A 125 -29.723 -4.478 20.052 1.00 49.10 C ANISOU 864 C VAL A 125 5189 7103 6364 -1033 -1131 -1508 C ATOM 865 O VAL A 125 -28.779 -3.698 20.199 1.00 34.10 O ANISOU 865 O VAL A 125 3229 5210 4519 -1128 -1156 -1586 O ATOM 866 CB VAL A 125 -30.596 -4.760 17.685 1.00 42.97 C ANISOU 866 CB VAL A 125 4466 6164 5694 -1071 -962 -1360 C ATOM 867 CG1 VAL A 125 -30.028 -3.400 17.315 1.00 31.21 C ANISOU 867 CG1 VAL A 125 2978 4586 4296 -1218 -936 -1419 C ATOM 868 CG2 VAL A 125 -30.596 -5.680 16.474 1.00 41.43 C ANISOU 868 CG2 VAL A 125 4233 5973 5537 -1046 -892 -1267 C ATOM 869 N THR A 126 -30.706 -4.555 20.949 1.00 45.21 N ANISOU 869 N THR A 126 4792 6615 5770 -958 -1163 -1514 N ATOM 870 CA THR A 126 -30.784 -3.619 22.063 1.00 37.90 C ANISOU 870 CA THR A 126 3917 5688 4796 -989 -1218 -1620 C ATOM 871 C THR A 126 -30.031 -4.080 23.304 1.00 38.74 C ANISOU 871 C THR A 126 3956 5948 4817 -937 -1324 -1666 C ATOM 872 O THR A 126 -29.714 -3.245 24.159 1.00 50.00 O ANISOU 872 O THR A 126 5392 7389 6218 -988 -1379 -1771 O ATOM 873 CB THR A 126 -32.248 -3.352 22.430 1.00 32.40 C ANISOU 873 CB THR A 126 3360 4921 4031 -938 -1190 -1617 C ATOM 874 OG1 THR A 126 -32.917 -4.593 22.689 1.00 34.21 O ANISOU 874 OG1 THR A 126 3606 5225 4165 -811 -1197 -1530 O ATOM 875 CG2 THR A 126 -32.951 -2.629 21.295 1.00 31.42 C ANISOU 875 CG2 THR A 126 3310 4628 4000 -1004 -1099 -1588 C ATOM 876 N LYS A 127 -29.741 -5.373 23.433 1.00 34.40 N ANISOU 876 N LYS A 127 3342 5508 4221 -838 -1360 -1591 N ATOM 877 CA LYS A 127 -28.969 -5.905 24.556 1.00 40.36 C ANISOU 877 CA LYS A 127 4030 6408 4897 -784 -1470 -1617 C ATOM 878 C LYS A 127 -27.840 -6.775 24.017 1.00 37.86 C ANISOU 878 C LYS A 127 3572 6167 4648 -762 -1490 -1571 C ATOM 879 O LYS A 127 -27.857 -8.003 24.162 1.00 35.71 O ANISOU 879 O LYS A 127 3275 5964 4328 -651 -1521 -1485 O ATOM 880 CB LYS A 127 -29.862 -6.690 25.517 1.00 35.39 C ANISOU 880 CB LYS A 127 3483 5841 4121 -662 -1509 -1562 C ATOM 881 CG LYS A 127 -30.991 -5.872 26.121 1.00 35.26 C ANISOU 881 CG LYS A 127 3599 5766 4030 -672 -1484 -1617 C ATOM 882 CD LYS A 127 -31.576 -6.553 27.348 1.00 46.54 C ANISOU 882 CD LYS A 127 5091 7295 5296 -568 -1541 -1585 C ATOM 883 CE LYS A 127 -32.148 -7.918 27.009 1.00 51.17 C ANISOU 883 CE LYS A 127 5693 7902 5848 -460 -1517 -1439 C ATOM 884 NZ LYS A 127 -32.772 -8.564 28.199 1.00 52.34 N ANISOU 884 NZ LYS A 127 5915 8139 5834 -367 -1564 -1394 N ATOM 885 N PRO A 128 -26.827 -6.162 23.395 1.00 37.21 N ANISOU 885 N PRO A 128 3392 6068 4678 -868 -1472 -1628 N ATOM 886 CA PRO A 128 -25.787 -6.963 22.731 1.00 37.51 C ANISOU 886 CA PRO A 128 3288 6171 4791 -849 -1472 -1591 C ATOM 887 C PRO A 128 -24.902 -7.734 23.694 1.00 50.37 C ANISOU 887 C PRO A 128 4822 7949 6369 -771 -1592 -1599 C ATOM 888 O PRO A 128 -24.225 -8.676 23.264 1.00 39.14 O ANISOU 888 O PRO A 128 3293 6586 4992 -713 -1600 -1551 O ATOM 889 CB PRO A 128 -24.975 -5.915 21.953 1.00 38.50 C ANISOU 889 CB PRO A 128 3343 6243 5041 -999 -1420 -1662 C ATOM 890 CG PRO A 128 -25.796 -4.649 21.991 1.00 38.26 C ANISOU 890 CG PRO A 128 3441 6085 5010 -1088 -1379 -1710 C ATOM 891 CD PRO A 128 -26.574 -4.719 23.260 1.00 38.26 C ANISOU 891 CD PRO A 128 3539 6120 4879 -1010 -1449 -1728 C ATOM 892 N LEU A 129 -24.888 -7.375 24.978 1.00 43.62 N ANISOU 892 N LEU A 129 4001 7154 5419 -764 -1688 -1658 N ATOM 893 CA LEU A 129 -23.976 -7.989 25.936 1.00 42.17 C ANISOU 893 CA LEU A 129 3726 7113 5185 -703 -1815 -1669 C ATOM 894 C LEU A 129 -24.604 -9.175 26.662 1.00 41.57 C ANISOU 894 C LEU A 129 3715 7093 4985 -557 -1871 -1566 C ATOM 895 O LEU A 129 -23.972 -10.226 26.799 1.00 53.45 O ANISOU 895 O LEU A 129 5136 8681 6492 -469 -1936 -1506 O ATOM 896 CB LEU A 129 -23.500 -6.946 26.953 1.00 44.30 C ANISOU 896 CB LEU A 129 3990 7427 5414 -786 -1899 -1795 C ATOM 897 CG LEU A 129 -22.403 -5.960 26.536 1.00 51.93 C ANISOU 897 CG LEU A 129 4844 8386 6501 -926 -1894 -1901 C ATOM 898 CD1 LEU A 129 -21.205 -6.700 25.957 1.00 53.28 C ANISOU 898 CD1 LEU A 129 4841 8636 6767 -906 -1911 -1876 C ATOM 899 CD2 LEU A 129 -22.916 -4.904 25.563 1.00 50.57 C ANISOU 899 CD2 LEU A 129 4738 8059 6418 -1043 -1771 -1929 C ATOM 900 N THR A 130 -25.842 -9.025 27.128 1.00 40.52 N ANISOU 900 N THR A 130 3732 6915 4750 -529 -1847 -1542 N ATOM 901 CA THR A 130 -26.461 -10.040 27.973 1.00 49.85 C ANISOU 901 CA THR A 130 4987 8154 5799 -405 -1903 -1447 C ATOM 902 C THR A 130 -27.274 -11.065 27.193 1.00 44.54 C ANISOU 902 C THR A 130 4362 7421 5142 -320 -1827 -1316 C ATOM 903 O THR A 130 -27.310 -12.238 27.583 1.00 49.70 O ANISOU 903 O THR A 130 5019 8126 5738 -213 -1881 -1213 O ATOM 904 CB THR A 130 -27.366 -9.376 29.015 1.00 55.55 C ANISOU 904 CB THR A 130 5842 8878 6387 -418 -1917 -1496 C ATOM 905 OG1 THR A 130 -28.500 -8.788 28.363 1.00 53.13 O ANISOU 905 OG1 THR A 130 5636 8448 6104 -454 -1799 -1500 O ATOM 906 CG2 THR A 130 -26.606 -8.293 29.768 1.00 59.16 C ANISOU 906 CG2 THR A 130 6261 9387 6831 -509 -1990 -1638 C ATOM 907 N TYR A 131 -27.925 -10.659 26.106 1.00 43.53 N ANISOU 907 N TYR A 131 4273 7177 5088 -369 -1709 -1313 N ATOM 908 CA TYR A 131 -28.875 -11.529 25.419 1.00 34.37 C ANISOU 908 CA TYR A 131 3177 5954 3929 -296 -1636 -1197 C ATOM 909 C TYR A 131 -28.224 -12.638 24.591 1.00 49.30 C ANISOU 909 C TYR A 131 4968 7857 5908 -236 -1630 -1121 C ATOM 910 O TYR A 131 -28.673 -13.788 24.680 1.00 47.67 O ANISOU 910 O TYR A 131 4798 7656 5659 -132 -1642 -1010 O ATOM 911 CB TYR A 131 -29.807 -10.702 24.528 1.00 39.10 C ANISOU 911 CB TYR A 131 3852 6428 4577 -369 -1520 -1219 C ATOM 912 CG TYR A 131 -30.959 -11.504 23.965 1.00 30.78 C ANISOU 912 CG TYR A 131 2879 5313 3504 -298 -1453 -1107 C ATOM 913 CD1 TYR A 131 -31.872 -12.123 24.809 1.00 30.46 C ANISOU 913 CD1 TYR A 131 2934 5300 3339 -211 -1479 -1036 C ATOM 914 CD2 TYR A 131 -31.135 -11.644 22.597 1.00 29.37 C ANISOU 914 CD2 TYR A 131 2682 5051 3427 -322 -1363 -1071 C ATOM 915 CE1 TYR A 131 -32.926 -12.861 24.308 1.00 28.78 C ANISOU 915 CE1 TYR A 131 2792 5031 3112 -152 -1419 -933 C ATOM 916 CE2 TYR A 131 -32.192 -12.376 22.086 1.00 37.76 C ANISOU 916 CE2 TYR A 131 3816 6059 4471 -261 -1309 -973 C ATOM 917 CZ TYR A 131 -33.084 -12.985 22.948 1.00 27.38 C ANISOU 917 CZ TYR A 131 2592 4771 3041 -176 -1338 -904 C ATOM 918 OH TYR A 131 -34.137 -13.719 22.449 1.00 32.77 O ANISOU 918 OH TYR A 131 3344 5400 3709 -119 -1284 -805 O ATOM 919 N PRO A 132 -27.198 -12.359 23.765 1.00 42.67 N ANISOU 919 N PRO A 132 4005 7018 5190 -298 -1605 -1176 N ATOM 920 CA PRO A 132 -26.687 -13.415 22.867 1.00 45.56 C ANISOU 920 CA PRO A 132 4282 7388 5642 -237 -1579 -1112 C ATOM 921 C PRO A 132 -26.289 -14.708 23.564 1.00 49.36 C ANISOU 921 C PRO A 132 4726 7949 6080 -107 -1679 -1032 C ATOM 922 O PRO A 132 -26.502 -15.790 23.002 1.00 53.34 O ANISOU 922 O PRO A 132 5228 8424 6615 -23 -1652 -942 O ATOM 923 CB PRO A 132 -25.482 -12.741 22.199 1.00 46.46 C ANISOU 923 CB PRO A 132 4259 7520 5874 -335 -1555 -1207 C ATOM 924 CG PRO A 132 -25.826 -11.307 22.197 1.00 45.83 C ANISOU 924 CG PRO A 132 4239 7380 5794 -463 -1512 -1291 C ATOM 925 CD PRO A 132 -26.522 -11.072 23.505 1.00 43.81 C ANISOU 925 CD PRO A 132 4092 7147 5407 -432 -1584 -1296 C ATOM 926 N VAL A 133 -25.725 -14.636 24.771 1.00 44.81 N ANISOU 926 N VAL A 133 4125 7467 5435 -89 -1796 -1059 N ATOM 927 CA VAL A 133 -25.326 -15.856 25.463 1.00 54.70 C ANISOU 927 CA VAL A 133 5347 8789 6646 32 -1900 -972 C ATOM 928 C VAL A 133 -26.530 -16.663 25.936 1.00 51.21 C ANISOU 928 C VAL A 133 5049 8310 6098 118 -1902 -847 C ATOM 929 O VAL A 133 -26.408 -17.872 26.165 1.00 59.42 O ANISOU 929 O VAL A 133 6082 9367 7129 224 -1957 -742 O ATOM 930 CB VAL A 133 -24.394 -15.530 26.644 1.00 60.47 C ANISOU 930 CB VAL A 133 6014 9638 7324 21 -2034 -1032 C ATOM 931 CG1 VAL A 133 -23.100 -14.905 26.141 1.00 62.14 C ANISOU 931 CG1 VAL A 133 6063 9893 7656 -57 -2037 -1145 C ATOM 932 CG2 VAL A 133 -25.088 -14.609 27.633 1.00 59.35 C ANISOU 932 CG2 VAL A 133 5989 9507 7054 -36 -2057 -1083 C ATOM 933 N LYS A 134 -27.697 -16.030 26.085 1.00 46.48 N ANISOU 933 N LYS A 134 4580 7657 5423 74 -1841 -854 N ATOM 934 CA LYS A 134 -28.893 -16.746 26.513 1.00 40.76 C ANISOU 934 CA LYS A 134 3992 6899 4598 145 -1831 -739 C ATOM 935 C LYS A 134 -29.614 -17.430 25.359 1.00 37.05 C ANISOU 935 C LYS A 134 3554 6327 4197 180 -1731 -657 C ATOM 936 O LYS A 134 -30.458 -18.300 25.603 1.00 31.98 O ANISOU 936 O LYS A 134 3003 5653 3494 250 -1727 -542 O ATOM 937 CB LYS A 134 -29.856 -15.791 27.224 1.00 46.50 C ANISOU 937 CB LYS A 134 4838 7621 5210 90 -1807 -788 C ATOM 938 CG LYS A 134 -29.323 -15.207 28.527 1.00 56.62 C ANISOU 938 CG LYS A 134 6114 9005 6393 64 -1911 -862 C ATOM 939 CD LYS A 134 -29.101 -16.286 29.581 1.00 62.48 C ANISOU 939 CD LYS A 134 6875 9828 7036 159 -2025 -758 C ATOM 940 CE LYS A 134 -28.527 -15.699 30.865 1.00 63.45 C ANISOU 940 CE LYS A 134 6991 10063 7054 129 -2137 -836 C ATOM 941 NZ LYS A 134 -28.299 -16.744 31.903 1.00 63.71 N ANISOU 941 NZ LYS A 134 7047 10175 6984 217 -2257 -726 N ATOM 942 N ARG A 135 -29.306 -17.063 24.117 1.00 40.47 N ANISOU 942 N ARG A 135 3915 6709 4751 126 -1650 -712 N ATOM 943 CA ARG A 135 -29.952 -17.653 22.946 1.00 34.15 C ANISOU 943 CA ARG A 135 3142 5818 4017 151 -1555 -648 C ATOM 944 C ARG A 135 -29.410 -19.057 22.723 1.00 30.46 C ANISOU 944 C ARG A 135 2613 5359 3603 257 -1594 -561 C ATOM 945 O ARG A 135 -28.307 -19.236 22.205 1.00 36.65 O ANISOU 945 O ARG A 135 3267 6173 4484 263 -1604 -605 O ATOM 946 CB ARG A 135 -29.721 -16.791 21.711 1.00 29.24 C ANISOU 946 CB ARG A 135 2463 5147 3501 52 -1460 -736 C ATOM 947 CG ARG A 135 -30.324 -15.410 21.776 1.00 28.75 C ANISOU 947 CG ARG A 135 2468 5048 3408 -55 -1414 -815 C ATOM 948 CD ARG A 135 -30.718 -14.957 20.386 1.00 27.31 C ANISOU 948 CD ARG A 135 2291 4774 3313 -126 -1299 -833 C ATOM 949 NE ARG A 135 -29.684 -15.253 19.403 1.00 32.15 N ANISOU 949 NE ARG A 135 2779 5398 4039 -142 -1268 -857 N ATOM 950 CZ ARG A 135 -29.883 -15.235 18.089 1.00 33.47 C ANISOU 950 CZ ARG A 135 2936 5500 4283 -184 -1171 -852 C ATOM 951 NH1 ARG A 135 -31.080 -14.941 17.605 1.00 29.08 N ANISOU 951 NH1 ARG A 135 2486 4859 3706 -213 -1105 -819 N ATOM 952 NH2 ARG A 135 -28.890 -15.521 17.258 1.00 36.08 N ANISOU 952 NH2 ARG A 135 3147 5854 4708 -198 -1139 -882 N ATOM 953 N THR A 136 -30.191 -20.061 23.099 1.00 30.02 N ANISOU 953 N THR A 136 2649 5270 3489 341 -1611 -437 N ATOM 954 CA THR A 136 -29.836 -21.452 22.881 1.00 30.43 C ANISOU 954 CA THR A 136 2663 5305 3596 445 -1643 -341 C ATOM 955 C THR A 136 -30.894 -22.115 22.011 1.00 41.86 C ANISOU 955 C THR A 136 4189 6645 5069 473 -1554 -261 C ATOM 956 O THR A 136 -32.004 -21.601 21.846 1.00 37.93 O ANISOU 956 O THR A 136 3791 6099 4523 423 -1487 -256 O ATOM 957 CB THR A 136 -29.696 -22.207 24.208 1.00 44.28 C ANISOU 957 CB THR A 136 4453 7111 5262 521 -1761 -249 C ATOM 958 OG1 THR A 136 -30.934 -22.142 24.927 1.00 46.41 O ANISOU 958 OG1 THR A 136 4872 7356 5407 511 -1750 -182 O ATOM 959 CG2 THR A 136 -28.595 -21.589 25.053 1.00 33.93 C ANISOU 959 CG2 THR A 136 3055 5912 3924 497 -1860 -331 C ATOM 960 N THR A 137 -30.534 -23.268 21.444 1.00 38.88 N ANISOU 960 N THR A 137 3764 6231 4776 555 -1555 -201 N ATOM 961 CA THR A 137 -31.495 -24.014 20.637 1.00 39.30 C ANISOU 961 CA THR A 137 3890 6181 4859 586 -1479 -123 C ATOM 962 C THR A 137 -32.635 -24.558 21.488 1.00 47.48 C ANISOU 962 C THR A 137 5069 7177 5793 615 -1500 4 C ATOM 963 O THR A 137 -33.774 -24.643 21.013 1.00 52.24 O ANISOU 963 O THR A 137 5763 7704 6382 596 -1425 49 O ATOM 964 CB THR A 137 -30.797 -25.155 19.896 1.00 34.93 C ANISOU 964 CB THR A 137 3253 5596 4421 674 -1479 -98 C ATOM 965 OG1 THR A 137 -30.245 -26.078 20.843 1.00 35.71 O ANISOU 965 OG1 THR A 137 3336 5725 4509 765 -1585 -15 O ATOM 966 CG2 THR A 137 -29.685 -24.612 19.009 1.00 28.30 C ANISOU 966 CG2 THR A 137 2269 4803 3683 637 -1444 -230 C ATOM 967 N LYS A 138 -32.353 -24.923 22.743 1.00 41.60 N ANISOU 967 N LYS A 138 4344 6486 4975 655 -1600 65 N ATOM 968 CA LYS A 138 -33.405 -25.424 23.622 1.00 40.38 C ANISOU 968 CA LYS A 138 4326 6301 4716 670 -1618 185 C ATOM 969 C LYS A 138 -34.440 -24.345 23.916 1.00 32.51 C ANISOU 969 C LYS A 138 3423 5312 3618 589 -1562 141 C ATOM 970 O LYS A 138 -35.640 -24.634 23.999 1.00 27.22 O ANISOU 970 O LYS A 138 2865 4582 2897 583 -1513 218 O ATOM 971 CB LYS A 138 -32.802 -25.956 24.921 1.00 46.25 C ANISOU 971 CB LYS A 138 5067 7112 5394 722 -1745 253 C ATOM 972 CG LYS A 138 -31.919 -27.179 24.746 1.00 60.17 C ANISOU 972 CG LYS A 138 6751 8857 7256 819 -1808 324 C ATOM 973 CD LYS A 138 -31.443 -27.706 26.092 1.00 68.37 C ANISOU 973 CD LYS A 138 7801 9960 8218 867 -1943 410 C ATOM 974 CE LYS A 138 -30.531 -28.911 25.923 1.00 69.25 C ANISOU 974 CE LYS A 138 7824 10052 8436 973 -2008 483 C ATOM 975 NZ LYS A 138 -30.065 -29.445 27.231 1.00 68.02 N ANISOU 975 NZ LYS A 138 7679 9958 8206 1021 -2151 580 N ATOM 976 N MET A 139 -33.995 -23.095 24.075 1.00 27.65 N ANISOU 976 N MET A 139 2760 4768 2978 525 -1566 13 N ATOM 977 CA MET A 139 -34.937 -22.002 24.291 1.00 38.85 C ANISOU 977 CA MET A 139 4258 6191 4314 452 -1508 -43 C ATOM 978 C MET A 139 -35.746 -21.712 23.032 1.00 36.02 C ANISOU 978 C MET A 139 3921 5745 4021 415 -1395 -60 C ATOM 979 O MET A 139 -36.947 -21.424 23.111 1.00 34.93 O ANISOU 979 O MET A 139 3879 5571 3821 390 -1337 -36 O ATOM 980 CB MET A 139 -34.193 -20.750 24.755 1.00 54.93 C ANISOU 980 CB MET A 139 6234 8313 6322 390 -1544 -179 C ATOM 981 CG MET A 139 -33.682 -20.830 26.185 1.00 70.67 C ANISOU 981 CG MET A 139 8237 10404 8212 415 -1656 -168 C ATOM 982 SD MET A 139 -35.011 -21.104 27.375 1.00 81.56 S ANISOU 982 SD MET A 139 9778 11790 9420 431 -1655 -73 S ATOM 983 CE MET A 139 -36.058 -19.687 27.049 1.00 74.73 C ANISOU 983 CE MET A 139 8969 10903 8523 347 -1544 -182 C ATOM 984 N ALA A 140 -35.108 -21.788 21.862 1.00 34.77 N ANISOU 984 N ALA A 140 3670 5556 3983 410 -1363 -103 N ATOM 985 CA ALA A 140 -35.826 -21.576 20.610 1.00 30.28 C ANISOU 985 CA ALA A 140 3122 4909 3476 374 -1264 -115 C ATOM 986 C ALA A 140 -36.917 -22.625 20.422 1.00 31.84 C ANISOU 986 C ALA A 140 3411 5024 3660 423 -1229 12 C ATOM 987 O ALA A 140 -38.095 -22.290 20.233 1.00 31.85 O ANISOU 987 O ALA A 140 3497 4981 3623 390 -1168 32 O ATOM 988 CB ALA A 140 -34.845 -21.594 19.438 1.00 28.61 C ANISOU 988 CB ALA A 140 2791 4691 3389 363 -1239 -183 C ATOM 989 N GLY A 141 -36.541 -23.906 20.481 1.00 28.02 N ANISOU 989 N GLY A 141 2912 4517 3217 500 -1269 99 N ATOM 990 CA GLY A 141 -37.524 -24.965 20.338 1.00 28.79 C ANISOU 990 CA GLY A 141 3098 4526 3314 538 -1239 223 C ATOM 991 C GLY A 141 -38.587 -24.939 21.418 1.00 36.32 C ANISOU 991 C GLY A 141 4172 5480 4148 523 -1245 294 C ATOM 992 O GLY A 141 -39.753 -25.253 21.159 1.00 36.49 O ANISOU 992 O GLY A 141 4279 5428 4158 511 -1186 358 O ATOM 993 N MET A 142 -38.206 -24.556 22.639 1.00 36.90 N ANISOU 993 N MET A 142 4252 5639 4130 522 -1313 276 N ATOM 994 CA MET A 142 -39.177 -24.464 23.723 1.00 46.37 C ANISOU 994 CA MET A 142 5562 6855 5199 508 -1313 328 C ATOM 995 C MET A 142 -40.191 -23.356 23.460 1.00 40.48 C ANISOU 995 C MET A 142 4862 6109 4410 447 -1226 261 C ATOM 996 O MET A 142 -41.384 -23.513 23.756 1.00 43.72 O ANISOU 996 O MET A 142 5367 6488 4757 438 -1176 320 O ATOM 997 CB MET A 142 -38.449 -24.239 25.048 1.00 53.53 C ANISOU 997 CB MET A 142 6460 7869 6012 520 -1409 310 C ATOM 998 CG MET A 142 -39.216 -24.687 26.282 1.00 59.70 C ANISOU 998 CG MET A 142 7355 8668 6660 531 -1433 401 C ATOM 999 SD MET A 142 -38.130 -25.431 27.520 1.00 64.17 S ANISOU 999 SD MET A 142 7905 9306 7169 585 -1581 467 S ATOM 1000 CE MET A 142 -36.934 -24.121 27.765 1.00 55.67 C ANISOU 1000 CE MET A 142 6718 8352 6081 555 -1634 304 C ATOM 1001 N MET A 143 -39.742 -22.237 22.884 1.00 31.70 N ANISOU 1001 N MET A 143 3682 5025 3337 402 -1205 139 N ATOM 1002 CA MET A 143 -40.656 -21.130 22.624 1.00 29.10 C ANISOU 1002 CA MET A 143 3391 4690 2977 345 -1132 73 C ATOM 1003 C MET A 143 -41.548 -21.396 21.415 1.00 27.18 C ANISOU 1003 C MET A 143 3173 4350 2803 336 -1051 116 C ATOM 1004 O MET A 143 -42.719 -20.999 21.413 1.00 23.81 O ANISOU 1004 O MET A 143 2813 3903 2332 315 -990 126 O ATOM 1005 CB MET A 143 -39.878 -19.827 22.440 1.00 28.70 C ANISOU 1005 CB MET A 143 3266 4688 2951 288 -1144 -73 C ATOM 1006 CG MET A 143 -39.217 -19.324 23.709 1.00 43.68 C ANISOU 1006 CG MET A 143 5152 6683 4762 283 -1217 -133 C ATOM 1007 SD MET A 143 -39.120 -17.526 23.801 1.00 60.50 S ANISOU 1007 SD MET A 143 7263 8846 6879 195 -1198 -303 S ATOM 1008 CE MET A 143 -40.846 -17.109 24.038 1.00 59.64 C ANISOU 1008 CE MET A 143 7266 8710 6683 190 -1117 -285 C ATOM 1009 N ILE A 144 -41.031 -22.062 20.378 1.00 22.29 N ANISOU 1009 N ILE A 144 2501 3678 2292 355 -1047 138 N ATOM 1010 CA ILE A 144 -41.897 -22.383 19.245 1.00 25.42 C ANISOU 1010 CA ILE A 144 2927 3984 2747 347 -976 181 C ATOM 1011 C ILE A 144 -42.893 -23.472 19.631 1.00 23.61 C ANISOU 1011 C ILE A 144 2791 3693 2487 380 -959 307 C ATOM 1012 O ILE A 144 -44.053 -23.455 19.195 1.00 19.87 O ANISOU 1012 O ILE A 144 2377 3161 2010 360 -893 341 O ATOM 1013 CB ILE A 144 -41.072 -22.773 18.002 1.00 25.98 C ANISOU 1013 CB ILE A 144 2914 4022 2935 356 -972 156 C ATOM 1014 CG1 ILE A 144 -40.302 -24.074 18.229 1.00 42.28 C ANISOU 1014 CG1 ILE A 144 4946 6076 5041 428 -1024 222 C ATOM 1015 CG2 ILE A 144 -40.125 -21.651 17.615 1.00 20.61 C ANISOU 1015 CG2 ILE A 144 2144 3398 2290 304 -979 24 C ATOM 1016 CD1 ILE A 144 -39.516 -24.533 17.022 1.00 53.76 C ANISOU 1016 CD1 ILE A 144 6314 7505 6609 451 -1011 187 C ATOM 1017 N ALA A 145 -42.465 -24.424 20.465 1.00 18.42 N ANISOU 1017 N ALA A 145 2148 3044 1809 425 -1019 375 N ATOM 1018 CA ALA A 145 -43.396 -25.424 20.976 1.00 18.65 C ANISOU 1018 CA ALA A 145 2274 3011 1800 445 -1009 485 C ATOM 1019 C ALA A 145 -44.492 -24.763 21.798 1.00 18.60 C ANISOU 1019 C ALA A 145 2342 3048 1677 415 -963 484 C ATOM 1020 O ALA A 145 -45.680 -25.064 21.633 1.00 21.04 O ANISOU 1020 O ALA A 145 2719 3301 1975 402 -896 535 O ATOM 1021 CB ALA A 145 -42.646 -26.465 21.807 1.00 20.16 C ANISOU 1021 CB ALA A 145 2467 3209 1983 496 -1098 557 C ATOM 1022 N ALA A 146 -44.109 -23.840 22.685 1.00 29.14 N ANISOU 1022 N ALA A 146 3659 4489 2925 403 -994 417 N ATOM 1023 CA ALA A 146 -45.104 -23.084 23.436 1.00 24.81 C ANISOU 1023 CA ALA A 146 3166 3998 2264 377 -945 397 C ATOM 1024 C ALA A 146 -46.028 -22.301 22.511 1.00 21.71 C ANISOU 1024 C ALA A 146 2773 3570 1908 340 -859 355 C ATOM 1025 O ALA A 146 -47.217 -22.141 22.810 1.00 24.03 O ANISOU 1025 O ALA A 146 3119 3869 2143 328 -794 382 O ATOM 1026 CB ALA A 146 -44.414 -22.143 24.424 1.00 20.49 C ANISOU 1026 CB ALA A 146 2593 3567 1626 368 -998 305 C ATOM 1027 N ALA A 147 -45.510 -21.817 21.382 1.00 29.80 N ANISOU 1027 N ALA A 147 3734 4561 3028 322 -857 292 N ATOM 1028 CA ALA A 147 -46.349 -21.070 20.451 1.00 15.91 C ANISOU 1028 CA ALA A 147 1977 2765 1305 287 -789 259 C ATOM 1029 C ALA A 147 -47.409 -21.969 19.821 1.00 38.31 C ANISOU 1029 C ALA A 147 4863 5508 4185 293 -729 360 C ATOM 1030 O ALA A 147 -48.606 -21.652 19.846 1.00 39.79 O ANISOU 1030 O ALA A 147 5087 5690 4340 276 -666 379 O ATOM 1031 CB ALA A 147 -45.485 -20.414 19.376 1.00 15.37 C ANISOU 1031 CB ALA A 147 1833 2682 1324 259 -806 173 C ATOM 1032 N TRP A 148 -46.990 -23.107 19.261 1.00 15.04 N ANISOU 1032 N TRP A 148 1913 2487 1315 316 -747 416 N ATOM 1033 CA TRP A 148 -47.957 -24.014 18.649 1.00 14.44 C ANISOU 1033 CA TRP A 148 1888 2314 1286 319 -691 491 C ATOM 1034 C TRP A 148 -48.966 -24.525 19.672 1.00 22.53 C ANISOU 1034 C TRP A 148 2982 3347 2231 321 -658 562 C ATOM 1035 O TRP A 148 -50.165 -24.619 19.377 1.00 22.31 O ANISOU 1035 O TRP A 148 2985 3282 2211 297 -586 597 O ATOM 1036 CB TRP A 148 -47.234 -25.180 17.976 1.00 14.51 C ANISOU 1036 CB TRP A 148 1886 2248 1380 357 -724 518 C ATOM 1037 CG TRP A 148 -46.554 -24.797 16.700 1.00 13.80 C ANISOU 1037 CG TRP A 148 1727 2143 1373 348 -725 459 C ATOM 1038 CD1 TRP A 148 -45.258 -24.397 16.549 1.00 14.15 C ANISOU 1038 CD1 TRP A 148 1685 2242 1449 349 -782 400 C ATOM 1039 CD2 TRP A 148 -47.137 -24.771 15.392 1.00 12.76 C ANISOU 1039 CD2 TRP A 148 1594 1955 1300 324 -659 459 C ATOM 1040 NE1 TRP A 148 -44.997 -24.125 15.228 1.00 16.92 N ANISOU 1040 NE1 TRP A 148 1986 2574 1871 331 -758 358 N ATOM 1041 CE2 TRP A 148 -46.134 -24.347 14.496 1.00 17.74 C ANISOU 1041 CE2 TRP A 148 2143 2608 1988 312 -684 401 C ATOM 1042 CE3 TRP A 148 -48.409 -25.066 14.892 1.00 12.11 C ANISOU 1042 CE3 TRP A 148 1562 1806 1234 295 -583 505 C ATOM 1043 CZ2 TRP A 148 -46.363 -24.211 13.127 1.00 11.74 C ANISOU 1043 CZ2 TRP A 148 1367 1794 1299 261 -645 401 C ATOM 1044 CZ3 TRP A 148 -48.636 -24.930 13.534 1.00 19.54 C ANISOU 1044 CZ3 TRP A 148 2484 2694 2245 251 -546 498 C ATOM 1045 CH2 TRP A 148 -47.617 -24.507 12.667 1.00 17.36 C ANISOU 1045 CH2 TRP A 148 2143 2430 2021 233 -580 451 C ATOM 1046 N VAL A 149 -48.503 -24.849 20.883 1.00 36.90 N ANISOU 1046 N VAL A 149 4822 5225 3974 345 -710 586 N ATOM 1047 CA VAL A 149 -49.411 -25.332 21.921 1.00 27.69 C ANISOU 1047 CA VAL A 149 3722 4082 2717 342 -678 658 C ATOM 1048 C VAL A 149 -50.421 -24.254 22.292 1.00 26.61 C ANISOU 1048 C VAL A 149 3585 4021 2505 310 -610 626 C ATOM 1049 O VAL A 149 -51.619 -24.531 22.441 1.00 35.07 O ANISOU 1049 O VAL A 149 4689 5082 3554 291 -539 679 O ATOM 1050 CB VAL A 149 -48.615 -25.811 23.150 1.00 18.61 C ANISOU 1050 CB VAL A 149 2596 2987 1486 374 -757 690 C ATOM 1051 CG1 VAL A 149 -49.534 -25.980 24.345 1.00 19.61 C ANISOU 1051 CG1 VAL A 149 2789 3174 1488 362 -718 750 C ATOM 1052 CG2 VAL A 149 -47.904 -27.116 22.839 1.00 19.02 C ANISOU 1052 CG2 VAL A 149 2663 2950 1614 415 -819 746 C ATOM 1053 N LEU A 150 -49.962 -23.008 22.435 1.00 18.03 N ANISOU 1053 N LEU A 150 2456 3013 1381 306 -630 529 N ATOM 1054 CA LEU A 150 -50.876 -21.921 22.774 1.00 22.40 C ANISOU 1054 CA LEU A 150 3009 3642 1861 288 -571 479 C ATOM 1055 C LEU A 150 -51.917 -21.720 21.681 1.00 20.02 C ANISOU 1055 C LEU A 150 2696 3273 1636 266 -500 495 C ATOM 1056 O LEU A 150 -53.112 -21.583 21.965 1.00 21.88 O ANISOU 1056 O LEU A 150 2946 3538 1828 256 -430 523 O ATOM 1057 CB LEU A 150 -50.098 -20.629 23.022 1.00 30.14 C ANISOU 1057 CB LEU A 150 3950 4701 2801 288 -615 349 C ATOM 1058 CG LEU A 150 -49.427 -20.483 24.387 1.00 45.79 C ANISOU 1058 CG LEU A 150 5945 6783 4668 301 -668 312 C ATOM 1059 CD1 LEU A 150 -48.744 -19.128 24.495 1.00 54.21 C ANISOU 1059 CD1 LEU A 150 6971 7910 5716 288 -705 161 C ATOM 1060 CD2 LEU A 150 -50.437 -20.672 25.507 1.00 45.32 C ANISOU 1060 CD2 LEU A 150 5942 6796 4483 304 -613 356 C ATOM 1061 N SER A 151 -51.480 -21.710 20.419 1.00 15.45 N ANISOU 1061 N SER A 151 2087 2611 1171 256 -517 480 N ATOM 1062 CA SER A 151 -52.415 -21.542 19.310 1.00 13.53 C ANISOU 1062 CA SER A 151 1836 2299 1006 231 -461 501 C ATOM 1063 C SER A 151 -53.452 -22.660 19.291 1.00 28.70 C ANISOU 1063 C SER A 151 3792 4161 2953 220 -405 595 C ATOM 1064 O SER A 151 -54.659 -22.407 19.152 1.00 18.67 O ANISOU 1064 O SER A 151 2517 2894 1682 201 -343 619 O ATOM 1065 CB SER A 151 -51.647 -21.495 17.989 1.00 15.36 C ANISOU 1065 CB SER A 151 2036 2453 1346 219 -492 473 C ATOM 1066 OG SER A 151 -50.580 -20.566 18.050 1.00 21.16 O ANISOU 1066 OG SER A 151 2731 3247 2061 220 -547 382 O ATOM 1067 N PHE A 152 -52.997 -23.909 19.439 1.00 13.94 N ANISOU 1067 N PHE A 152 1952 2240 1106 233 -430 645 N ATOM 1068 CA PHE A 152 -53.912 -25.045 19.398 1.00 14.12 C ANISOU 1068 CA PHE A 152 2008 2200 1155 217 -383 724 C ATOM 1069 C PHE A 152 -54.925 -24.980 20.535 1.00 31.81 C ANISOU 1069 C PHE A 152 4268 4522 3296 203 -332 770 C ATOM 1070 O PHE A 152 -56.132 -25.137 20.317 1.00 19.19 O ANISOU 1070 O PHE A 152 2662 2910 1719 171 -266 808 O ATOM 1071 CB PHE A 152 -53.124 -26.354 19.454 1.00 26.88 C ANISOU 1071 CB PHE A 152 3660 3755 2800 245 -430 763 C ATOM 1072 CG PHE A 152 -53.988 -27.582 19.393 1.00 23.63 C ANISOU 1072 CG PHE A 152 3288 3276 2416 227 -387 838 C ATOM 1073 CD1 PHE A 152 -54.441 -28.067 18.177 1.00 15.51 C ANISOU 1073 CD1 PHE A 152 2248 2158 1487 205 -353 834 C ATOM 1074 CD2 PHE A 152 -54.345 -28.253 20.552 1.00 21.40 C ANISOU 1074 CD2 PHE A 152 3054 3024 2055 228 -380 912 C ATOM 1075 CE1 PHE A 152 -55.237 -29.198 18.119 1.00 20.71 C ANISOU 1075 CE1 PHE A 152 2938 2757 2173 182 -317 897 C ATOM 1076 CE2 PHE A 152 -55.142 -29.383 20.501 1.00 18.17 C ANISOU 1076 CE2 PHE A 152 2681 2551 1673 204 -340 984 C ATOM 1077 CZ PHE A 152 -55.588 -29.857 19.284 1.00 15.83 C ANISOU 1077 CZ PHE A 152 2368 2164 1483 180 -310 974 C ATOM 1078 N ILE A 153 -54.450 -24.748 21.761 1.00 27.68 N ANISOU 1078 N ILE A 153 3764 4094 2660 225 -361 764 N ATOM 1079 CA ILE A 153 -55.356 -24.701 22.904 1.00 30.20 C ANISOU 1079 CA ILE A 153 4103 4506 2864 213 -305 802 C ATOM 1080 C ILE A 153 -56.313 -23.519 22.794 1.00 24.55 C ANISOU 1080 C ILE A 153 3344 3864 2119 203 -238 754 C ATOM 1081 O ILE A 153 -57.460 -23.595 23.252 1.00 20.70 O ANISOU 1081 O ILE A 153 2854 3427 1583 183 -161 794 O ATOM 1082 CB ILE A 153 -54.547 -24.670 24.215 1.00 26.79 C ANISOU 1082 CB ILE A 153 3706 4164 2308 239 -358 794 C ATOM 1083 CG1 ILE A 153 -53.741 -25.960 24.368 1.00 26.61 C ANISOU 1083 CG1 ILE A 153 3731 4068 2314 258 -425 862 C ATOM 1084 CG2 ILE A 153 -55.456 -24.483 25.420 1.00 24.50 C ANISOU 1084 CG2 ILE A 153 3439 3989 1882 225 -292 818 C ATOM 1085 CD1 ILE A 153 -52.975 -26.050 25.667 1.00 32.41 C ANISOU 1085 CD1 ILE A 153 4503 4885 2925 283 -488 871 C ATOM 1086 N LEU A 154 -55.879 -22.422 22.169 1.00 23.90 N ANISOU 1086 N LEU A 154 3225 3790 2065 218 -264 667 N ATOM 1087 CA LEU A 154 -56.746 -21.255 22.044 1.00 27.39 C ANISOU 1087 CA LEU A 154 3631 4301 2474 224 -208 613 C ATOM 1088 C LEU A 154 -57.859 -21.490 21.027 1.00 34.17 C ANISOU 1088 C LEU A 154 4462 5086 3434 198 -153 671 C ATOM 1089 O LEU A 154 -59.033 -21.218 21.306 1.00 30.05 O ANISOU 1089 O LEU A 154 3916 4628 2871 195 -76 688 O ATOM 1090 CB LEU A 154 -55.925 -20.023 21.661 1.00 36.06 C ANISOU 1090 CB LEU A 154 4709 5418 3575 247 -262 497 C ATOM 1091 CG LEU A 154 -55.166 -19.300 22.775 1.00 48.89 C ANISOU 1091 CG LEU A 154 6346 7154 5078 271 -301 394 C ATOM 1092 CD1 LEU A 154 -54.447 -18.079 22.215 1.00 49.47 C ANISOU 1092 CD1 LEU A 154 6395 7170 5233 263 -339 251 C ATOM 1093 CD2 LEU A 154 -56.101 -18.905 23.906 1.00 52.60 C ANISOU 1093 CD2 LEU A 154 6825 7739 5420 282 -225 361 C ATOM 1094 N TRP A 155 -57.517 -21.993 19.840 1.00 28.22 N ANISOU 1094 N TRP A 155 3706 4204 2812 177 -189 692 N ATOM 1095 CA TRP A 155 -58.489 -22.025 18.751 1.00 24.27 C ANISOU 1095 CA TRP A 155 3176 3632 2415 149 -152 724 C ATOM 1096 C TRP A 155 -59.183 -23.368 18.567 1.00 23.20 C ANISOU 1096 C TRP A 155 3050 3426 2338 109 -120 799 C ATOM 1097 O TRP A 155 -60.375 -23.395 18.245 1.00 22.07 O ANISOU 1097 O TRP A 155 2872 3283 2231 83 -68 836 O ATOM 1098 CB TRP A 155 -57.820 -21.622 17.435 1.00 23.80 C ANISOU 1098 CB TRP A 155 3108 3477 2460 142 -204 680 C ATOM 1099 CG TRP A 155 -57.515 -20.164 17.368 1.00 29.14 C ANISOU 1099 CG TRP A 155 3768 4167 3138 159 -216 567 C ATOM 1100 CD1 TRP A 155 -56.287 -19.579 17.456 1.00 36.77 C ANISOU 1100 CD1 TRP A 155 4741 5139 4089 170 -270 488 C ATOM 1101 CD2 TRP A 155 -58.459 -19.098 17.215 1.00 31.11 C ANISOU 1101 CD2 TRP A 155 3990 4404 3427 163 -171 502 C ATOM 1102 NE1 TRP A 155 -56.406 -18.214 17.357 1.00 38.62 N ANISOU 1102 NE1 TRP A 155 4963 5356 4353 171 -259 379 N ATOM 1103 CE2 TRP A 155 -57.730 -17.894 17.210 1.00 34.30 C ANISOU 1103 CE2 TRP A 155 4398 4793 3841 174 -201 387 C ATOM 1104 CE3 TRP A 155 -59.849 -19.045 17.078 1.00 36.88 C ANISOU 1104 CE3 TRP A 155 4688 5133 4194 160 -111 528 C ATOM 1105 CZ2 TRP A 155 -58.345 -16.651 17.076 1.00 35.47 C ANISOU 1105 CZ2 TRP A 155 4530 4910 4037 188 -175 301 C ATOM 1106 CZ3 TRP A 155 -60.457 -17.810 16.943 1.00 36.33 C ANISOU 1106 CZ3 TRP A 155 4589 5042 4171 182 -88 439 C ATOM 1107 CH2 TRP A 155 -59.705 -16.631 16.943 1.00 36.65 C ANISOU 1107 CH2 TRP A 155 4647 5055 4224 199 -121 329 C ATOM 1108 N ALA A 156 -58.476 -24.481 18.760 1.00 26.94 N ANISOU 1108 N ALA A 156 3567 3846 2822 107 -154 822 N ATOM 1109 CA ALA A 156 -59.028 -25.785 18.391 1.00 27.67 C ANISOU 1109 CA ALA A 156 3675 3857 2980 72 -134 878 C ATOM 1110 C ALA A 156 -60.285 -26.162 19.169 1.00 34.37 C ANISOU 1110 C ALA A 156 4515 4763 3781 40 -64 948 C ATOM 1111 O ALA A 156 -61.292 -26.517 18.528 1.00 14.58 O ANISOU 1111 O ALA A 156 1977 2217 1346 -1 -28 976 O ATOM 1112 CB ALA A 156 -57.941 -26.856 18.528 1.00 23.65 C ANISOU 1112 CB ALA A 156 3220 3288 2478 94 -185 889 C ATOM 1113 N PRO A 157 -60.317 -26.120 20.510 1.00 31.38 N ANISOU 1113 N PRO A 157 4159 4483 3282 51 -40 978 N ATOM 1114 CA PRO A 157 -61.533 -26.582 21.204 1.00 28.86 C ANISOU 1114 CA PRO A 157 3830 4218 2919 10 38 1048 C ATOM 1115 C PRO A 157 -62.761 -25.737 20.906 1.00 25.02 C ANISOU 1115 C PRO A 157 3264 3797 2445 -7 110 1039 C ATOM 1116 O PRO A 157 -63.870 -26.279 20.821 1.00 31.46 O ANISOU 1116 O PRO A 157 4047 4608 3296 -56 168 1092 O ATOM 1117 CB PRO A 157 -61.136 -26.517 22.686 1.00 22.53 C ANISOU 1117 CB PRO A 157 3074 3520 1967 31 44 1062 C ATOM 1118 CG PRO A 157 -60.070 -25.495 22.743 1.00 23.60 C ANISOU 1118 CG PRO A 157 3209 3697 2061 84 -13 978 C ATOM 1119 CD PRO A 157 -59.293 -25.667 21.472 1.00 28.33 C ANISOU 1119 CD PRO A 157 3805 4171 2789 94 -81 946 C ATOM 1120 N ALA A 158 -62.599 -24.424 20.736 1.00 22.65 N ANISOU 1120 N ALA A 158 2929 3559 2119 34 109 973 N ATOM 1121 CA ALA A 158 -63.748 -23.573 20.439 1.00 22.23 C ANISOU 1121 CA ALA A 158 2796 3573 2076 34 181 966 C ATOM 1122 C ALA A 158 -64.346 -23.916 19.079 1.00 28.54 C ANISOU 1122 C ALA A 158 3555 4262 3028 -3 165 995 C ATOM 1123 O ALA A 158 -65.567 -24.072 18.943 1.00 29.63 O ANISOU 1123 O ALA A 158 3629 4427 3203 -39 230 1036 O ATOM 1124 CB ALA A 158 -63.338 -22.102 20.498 1.00 17.31 C ANISOU 1124 CB ALA A 158 2159 2997 1422 96 168 845 C ATOM 1125 N ILE A 159 -63.494 -24.047 18.060 1.00 26.13 N ANISOU 1125 N ILE A 159 3282 3837 2810 1 81 962 N ATOM 1126 CA ILE A 159 -63.969 -24.348 16.713 1.00 18.53 C ANISOU 1126 CA ILE A 159 2290 2772 1980 -34 56 966 C ATOM 1127 C ILE A 159 -64.556 -25.751 16.644 1.00 24.35 C ANISOU 1127 C ILE A 159 3033 3456 2762 -92 73 1016 C ATOM 1128 O ILE A 159 -65.525 -25.990 15.912 1.00 27.39 O ANISOU 1128 O ILE A 159 3367 3813 3228 -133 86 1037 O ATOM 1129 CB ILE A 159 -62.824 -24.164 15.698 1.00 12.45 C ANISOU 1129 CB ILE A 159 1559 1902 1271 -17 -24 898 C ATOM 1130 CG1 ILE A 159 -62.341 -22.713 15.696 1.00 12.09 C ANISOU 1130 CG1 ILE A 159 1505 1898 1189 32 -44 853 C ATOM 1131 CG2 ILE A 159 -63.257 -24.580 14.302 1.00 11.84 C ANISOU 1131 CG2 ILE A 159 1463 1727 1308 -56 -49 885 C ATOM 1132 CD1 ILE A 159 -61.148 -22.473 14.802 1.00 11.19 C ANISOU 1132 CD1 ILE A 159 1427 1698 1126 39 -113 784 C ATOM 1133 N LEU A 160 -64.005 -26.695 17.410 1.00 14.65 N ANISOU 1133 N LEU A 160 1868 2216 1484 -95 68 1039 N ATOM 1134 CA LEU A 160 -64.472 -28.073 17.310 1.00 16.60 C ANISOU 1134 CA LEU A 160 2134 2398 1774 -146 78 1088 C ATOM 1135 C LEU A 160 -65.702 -28.352 18.168 1.00 19.51 C ANISOU 1135 C LEU A 160 2467 2845 2101 -193 160 1159 C ATOM 1136 O LEU A 160 -66.472 -29.264 17.846 1.00 24.88 O ANISOU 1136 O LEU A 160 3135 3478 2841 -251 179 1199 O ATOM 1137 CB LEU A 160 -63.353 -29.041 17.691 1.00 19.57 C ANISOU 1137 CB LEU A 160 2598 2714 2125 -125 36 1095 C ATOM 1138 CG LEU A 160 -62.166 -29.135 16.733 1.00 21.21 C ANISOU 1138 CG LEU A 160 2837 2835 2389 -89 -33 1028 C ATOM 1139 CD1 LEU A 160 -61.307 -30.339 17.083 1.00 27.62 C ANISOU 1139 CD1 LEU A 160 3721 3585 3187 -71 -63 1056 C ATOM 1140 CD2 LEU A 160 -62.633 -29.204 15.289 1.00 13.67 C ANISOU 1140 CD2 LEU A 160 1844 1813 1537 -119 -46 991 C ATOM 1141 N PHE A 161 -65.916 -27.601 19.250 1.00 17.19 N ANISOU 1141 N PHE A 161 2154 2677 1701 -173 217 1168 N ATOM 1142 CA PHE A 161 -66.959 -27.948 20.210 1.00 18.65 C ANISOU 1142 CA PHE A 161 2313 2947 1825 -219 308 1227 C ATOM 1143 C PHE A 161 -67.959 -26.825 20.472 1.00 27.63 C ANISOU 1143 C PHE A 161 3349 4219 2931 -212 394 1206 C ATOM 1144 O PHE A 161 -68.840 -26.984 21.333 1.00 25.96 O ANISOU 1144 O PHE A 161 3104 4099 2660 -248 486 1236 O ATOM 1145 CB PHE A 161 -66.325 -28.403 21.527 1.00 28.07 C ANISOU 1145 CB PHE A 161 3591 4181 2893 -207 315 1259 C ATOM 1146 CG PHE A 161 -65.300 -29.488 21.359 1.00 26.27 C ANISOU 1146 CG PHE A 161 3457 3830 2694 -199 236 1281 C ATOM 1147 CD1 PHE A 161 -65.657 -30.720 20.836 1.00 29.64 C ANISOU 1147 CD1 PHE A 161 3906 4151 3206 -250 230 1327 C ATOM 1148 CD2 PHE A 161 -63.981 -29.279 21.727 1.00 26.55 C ANISOU 1148 CD2 PHE A 161 3554 3862 2672 -139 171 1250 C ATOM 1149 CE1 PHE A 161 -64.715 -31.721 20.678 1.00 34.91 C ANISOU 1149 CE1 PHE A 161 4657 4709 3897 -231 166 1342 C ATOM 1150 CE2 PHE A 161 -63.034 -30.276 21.573 1.00 28.68 C ANISOU 1150 CE2 PHE A 161 3900 4026 2971 -122 104 1268 C ATOM 1151 CZ PHE A 161 -63.402 -31.498 21.047 1.00 29.93 C ANISOU 1151 CZ PHE A 161 4082 4080 3212 -164 105 1314 C ATOM 1152 N TRP A 162 -67.863 -25.701 19.754 1.00 28.27 N ANISOU 1152 N TRP A 162 3378 4314 3050 -165 376 1153 N ATOM 1153 CA TRP A 162 -68.864 -24.653 19.925 1.00 30.53 C ANISOU 1153 CA TRP A 162 3554 4725 3321 -147 469 1124 C ATOM 1154 C TRP A 162 -70.259 -25.156 19.574 1.00 26.11 C ANISOU 1154 C TRP A 162 2897 4169 2855 -215 526 1162 C ATOM 1155 O TRP A 162 -71.244 -24.756 20.209 1.00 20.38 O ANISOU 1155 O TRP A 162 2081 3564 2098 -218 631 1141 O ATOM 1156 CB TRP A 162 -68.515 -23.429 19.079 1.00 29.99 C ANISOU 1156 CB TRP A 162 3463 4606 3325 -75 409 1015 C ATOM 1157 CG TRP A 162 -69.507 -22.320 19.246 1.00 34.76 C ANISOU 1157 CG TRP A 162 3964 5280 3962 -28 472 910 C ATOM 1158 CD1 TRP A 162 -70.607 -22.083 18.476 1.00 39.27 C ANISOU 1158 CD1 TRP A 162 4431 5829 4661 -35 482 890 C ATOM 1159 CD2 TRP A 162 -69.498 -21.304 20.256 1.00 38.45 C ANISOU 1159 CD2 TRP A 162 4420 5850 4338 38 529 805 C ATOM 1160 NE1 TRP A 162 -71.282 -20.982 18.941 1.00 44.50 N ANISOU 1160 NE1 TRP A 162 5013 6570 5327 32 543 782 N ATOM 1161 CE2 TRP A 162 -70.621 -20.484 20.033 1.00 41.88 C ANISOU 1161 CE2 TRP A 162 4739 6312 4861 77 577 722 C ATOM 1162 CE3 TRP A 162 -68.648 -21.007 21.325 1.00 40.43 C ANISOU 1162 CE3 TRP A 162 4744 6175 4441 72 540 765 C ATOM 1163 CZ2 TRP A 162 -70.915 -19.386 20.837 1.00 45.98 C ANISOU 1163 CZ2 TRP A 162 5218 6920 5333 151 643 595 C ATOM 1164 CZ3 TRP A 162 -68.942 -19.918 22.124 1.00 47.26 C ANISOU 1164 CZ3 TRP A 162 5573 7135 5247 136 603 637 C ATOM 1165 CH2 TRP A 162 -70.066 -19.120 21.875 1.00 48.93 C ANISOU 1165 CH2 TRP A 162 5673 7362 5557 176 658 550 C ATOM 1166 N GLN A 163 -70.362 -26.033 18.571 1.00 36.40 N ANISOU 1166 N GLN A 163 4214 5343 4273 -267 458 1198 N ATOM 1167 CA GLN A 163 -71.659 -26.593 18.205 1.00 19.42 C ANISOU 1167 CA GLN A 163 1975 3191 2212 -340 499 1227 C ATOM 1168 C GLN A 163 -72.311 -27.295 19.388 1.00 21.08 C ANISOU 1168 C GLN A 163 2188 3473 2348 -394 591 1265 C ATOM 1169 O GLN A 163 -73.528 -27.197 19.586 1.00 22.16 O ANISOU 1169 O GLN A 163 2216 3690 2514 -432 675 1261 O ATOM 1170 CB GLN A 163 -71.495 -27.557 17.033 1.00 26.80 C ANISOU 1170 CB GLN A 163 2952 3975 3256 -386 404 1245 C ATOM 1171 CG GLN A 163 -70.335 -28.520 17.195 1.00 28.49 C ANISOU 1171 CG GLN A 163 3304 4088 3432 -382 342 1255 C ATOM 1172 CD GLN A 163 -70.115 -29.377 15.966 1.00 39.75 C ANISOU 1172 CD GLN A 163 4766 5378 4961 -411 259 1242 C ATOM 1173 OE1 GLN A 163 -71.060 -29.706 15.247 1.00 41.21 O ANISOU 1173 OE1 GLN A 163 4886 5539 5231 -467 258 1250 O ATOM 1174 NE2 GLN A 163 -68.861 -29.739 15.713 1.00 43.53 N ANISOU 1174 NE2 GLN A 163 5340 5771 5428 -373 191 1212 N ATOM 1175 N PHE A 164 -71.514 -27.992 20.198 1.00 36.16 N ANISOU 1175 N PHE A 164 4217 5358 4165 -397 578 1298 N ATOM 1176 CA PHE A 164 -72.043 -28.671 21.372 1.00 23.16 C ANISOU 1176 CA PHE A 164 2592 3774 2435 -452 664 1347 C ATOM 1177 C PHE A 164 -72.223 -27.731 22.554 1.00 24.09 C ANISOU 1177 C PHE A 164 2679 4056 2420 -411 758 1307 C ATOM 1178 O PHE A 164 -73.023 -28.028 23.448 1.00 25.74 O ANISOU 1178 O PHE A 164 2863 4348 2568 -461 858 1329 O ATOM 1179 CB PHE A 164 -71.125 -29.830 21.762 1.00 23.38 C ANISOU 1179 CB PHE A 164 2761 3703 2420 -467 609 1406 C ATOM 1180 CG PHE A 164 -70.783 -30.736 20.619 1.00 22.50 C ANISOU 1180 CG PHE A 164 2691 3430 2430 -490 518 1418 C ATOM 1181 CD1 PHE A 164 -69.532 -30.689 20.029 1.00 21.14 C ANISOU 1181 CD1 PHE A 164 2586 3168 2278 -428 417 1382 C ATOM 1182 CD2 PHE A 164 -71.718 -31.626 20.123 1.00 23.16 C ANISOU 1182 CD2 PHE A 164 2740 3457 2604 -573 539 1454 C ATOM 1183 CE1 PHE A 164 -69.217 -31.521 18.970 1.00 26.88 C ANISOU 1183 CE1 PHE A 164 3348 3758 3109 -444 345 1375 C ATOM 1184 CE2 PHE A 164 -71.411 -32.460 19.064 1.00 22.48 C ANISOU 1184 CE2 PHE A 164 2693 3229 2620 -591 460 1450 C ATOM 1185 CZ PHE A 164 -70.158 -32.408 18.486 1.00 27.19 C ANISOU 1185 CZ PHE A 164 3359 3743 3230 -523 366 1408 C ATOM 1186 N ILE A 165 -71.502 -26.608 22.578 1.00 39.38 N ANISOU 1186 N ILE A 165 4617 6041 4305 -324 732 1239 N ATOM 1187 CA ILE A 165 -71.688 -25.633 23.649 1.00 44.17 C ANISOU 1187 CA ILE A 165 5191 6808 4785 -275 823 1170 C ATOM 1188 C ILE A 165 -73.068 -24.989 23.556 1.00 38.40 C ANISOU 1188 C ILE A 165 4304 6176 4111 -279 929 1113 C ATOM 1189 O ILE A 165 -73.776 -24.849 24.561 1.00 38.95 O ANISOU 1189 O ILE A 165 4334 6364 4100 -293 1039 1083 O ATOM 1190 CB ILE A 165 -70.565 -24.580 23.614 1.00 48.70 C ANISOU 1190 CB ILE A 165 5804 7400 5298 -180 765 1095 C ATOM 1191 CG1 ILE A 165 -69.238 -25.212 24.033 1.00 45.09 C ANISOU 1191 CG1 ILE A 165 5491 6874 4766 -174 672 1136 C ATOM 1192 CG2 ILE A 165 -70.907 -23.402 24.511 1.00 52.65 C ANISOU 1192 CG2 ILE A 165 6249 8063 5691 -118 861 985 C ATOM 1193 CD1 ILE A 165 -69.286 -25.867 25.398 1.00 53.67 C ANISOU 1193 CD1 ILE A 165 6646 8025 5722 -211 723 1179 C ATOM 1194 N VAL A 166 -73.472 -24.585 22.346 1.00 45.35 N ANISOU 1194 N VAL A 166 5088 7007 5137 -262 896 1091 N ATOM 1195 CA VAL A 166 -74.787 -23.983 22.141 1.00 33.53 C ANISOU 1195 CA VAL A 166 3424 5589 3726 -254 979 1027 C ATOM 1196 C VAL A 166 -75.873 -25.021 21.893 1.00 25.73 C ANISOU 1196 C VAL A 166 2379 4569 2827 -360 1007 1091 C ATOM 1197 O VAL A 166 -77.052 -24.657 21.781 1.00 26.66 O ANISOU 1197 O VAL A 166 2352 4754 3024 -363 1075 1038 O ATOM 1198 CB VAL A 166 -74.760 -22.980 20.971 1.00 23.54 C ANISOU 1198 CB VAL A 166 2076 4276 2591 -174 915 959 C ATOM 1199 CG1 VAL A 166 -73.866 -21.798 21.303 1.00 22.98 C ANISOU 1199 CG1 VAL A 166 2074 4202 2456 -60 877 836 C ATOM 1200 CG2 VAL A 166 -74.288 -23.668 19.701 1.00 31.29 C ANISOU 1200 CG2 VAL A 166 3114 5095 3680 -219 788 1034 C ATOM 1201 N GLY A 167 -75.516 -26.301 21.803 1.00 29.19 N ANISOU 1201 N GLY A 167 2926 4903 3264 -441 955 1190 N ATOM 1202 CA GLY A 167 -76.494 -27.354 21.623 1.00 32.09 C ANISOU 1202 CA GLY A 167 3252 5233 3706 -547 985 1244 C ATOM 1203 C GLY A 167 -77.090 -27.459 20.239 1.00 40.12 C ANISOU 1203 C GLY A 167 4178 6173 4894 -573 919 1237 C ATOM 1204 O GLY A 167 -78.044 -28.220 20.049 1.00 26.99 O ANISOU 1204 O GLY A 167 2458 4494 3302 -662 948 1264 O ATOM 1205 N VAL A 168 -76.559 -26.726 19.262 1.00 34.39 N ANISOU 1205 N VAL A 168 3437 5396 4233 -504 829 1203 N ATOM 1206 CA VAL A 168 -77.099 -26.736 17.909 1.00 31.20 C ANISOU 1206 CA VAL A 168 2948 4921 3985 -523 754 1192 C ATOM 1207 C VAL A 168 -75.970 -26.432 16.935 1.00 26.71 C ANISOU 1207 C VAL A 168 2459 4245 3446 -472 632 1194 C ATOM 1208 O VAL A 168 -75.039 -25.685 17.245 1.00 21.14 O ANISOU 1208 O VAL A 168 1807 3559 2667 -395 625 1174 O ATOM 1209 CB VAL A 168 -78.265 -25.726 17.757 1.00 35.92 C ANISOU 1209 CB VAL A 168 3356 5624 4665 -478 807 1110 C ATOM 1210 CG1 VAL A 168 -77.766 -24.294 17.917 1.00 32.72 C ANISOU 1210 CG1 VAL A 168 2918 5281 4232 -349 815 1035 C ATOM 1211 CG2 VAL A 168 -78.976 -25.910 16.420 1.00 24.36 C ANISOU 1211 CG2 VAL A 168 1804 4092 3360 -512 720 1103 C ATOM 1212 N ARG A 169 -76.050 -27.039 15.754 1.00 34.47 N ANISOU 1212 N ARG A 169 3452 5113 4531 -519 537 1213 N ATOM 1213 CA ARG A 169 -75.138 -26.768 14.649 1.00 19.72 C ANISOU 1213 CA ARG A 169 1646 3139 2707 -483 421 1205 C ATOM 1214 C ARG A 169 -75.909 -25.977 13.597 1.00 29.17 C ANISOU 1214 C ARG A 169 2707 4347 4030 -462 375 1164 C ATOM 1215 O ARG A 169 -76.764 -26.533 12.898 1.00 36.83 O ANISOU 1215 O ARG A 169 3620 5288 5086 -523 339 1162 O ATOM 1216 CB ARG A 169 -74.575 -28.066 14.076 1.00 19.27 C ANISOU 1216 CB ARG A 169 1715 2946 2663 -539 342 1234 C ATOM 1217 CG ARG A 169 -73.930 -27.921 12.711 1.00 17.93 C ANISOU 1217 CG ARG A 169 1588 2669 2554 -519 224 1207 C ATOM 1218 CD ARG A 169 -72.456 -28.259 12.750 1.00 23.26 C ANISOU 1218 CD ARG A 169 2413 3261 3162 -479 173 1195 C ATOM 1219 NE ARG A 169 -71.857 -28.204 11.421 1.00 28.72 N ANISOU 1219 NE ARG A 169 3148 3857 3905 -465 71 1153 N ATOM 1220 CZ ARG A 169 -70.549 -28.223 11.192 1.00 32.13 C ANISOU 1220 CZ ARG A 169 3685 4227 4298 -417 21 1112 C ATOM 1221 NH1 ARG A 169 -69.700 -28.291 12.208 1.00 36.98 N ANISOU 1221 NH1 ARG A 169 4367 4857 4828 -378 53 1113 N ATOM 1222 NH2 ARG A 169 -70.088 -28.166 9.950 1.00 35.68 N ANISOU 1222 NH2 ARG A 169 4165 4605 4786 -409 -59 1062 N ATOM 1223 N THR A 170 -75.621 -24.680 13.500 1.00 21.63 N ANISOU 1223 N THR A 170 1738 3407 3073 -352 349 1085 N ATOM 1224 CA THR A 170 -76.303 -23.807 12.554 1.00 24.45 C ANISOU 1224 CA THR A 170 1999 3750 3540 -296 280 1017 C ATOM 1225 C THR A 170 -75.653 -23.797 11.178 1.00 30.48 C ANISOU 1225 C THR A 170 2845 4388 4349 -295 143 1016 C ATOM 1226 O THR A 170 -76.210 -23.197 10.252 1.00 35.65 O ANISOU 1226 O THR A 170 3432 5023 5090 -262 67 979 O ATOM 1227 CB THR A 170 -76.356 -22.371 13.091 1.00 19.26 C ANISOU 1227 CB THR A 170 1304 3147 2868 -168 311 918 C ATOM 1228 OG1 THR A 170 -75.047 -21.789 13.042 1.00 22.93 O ANISOU 1228 OG1 THR A 170 1908 3536 3267 -105 258 886 O ATOM 1229 CG2 THR A 170 -76.857 -22.357 14.526 1.00 20.55 C ANISOU 1229 CG2 THR A 170 1402 3446 2958 -164 457 906 C ATOM 1230 N VAL A 171 -74.493 -24.433 11.023 1.00 29.45 N ANISOU 1230 N VAL A 171 2855 4177 4158 -329 109 1055 N ATOM 1231 CA VAL A 171 -73.823 -24.489 9.730 1.00 29.52 C ANISOU 1231 CA VAL A 171 2944 4076 4197 -335 -7 1050 C ATOM 1232 C VAL A 171 -74.628 -25.385 8.798 1.00 33.69 C ANISOU 1232 C VAL A 171 3414 4577 4808 -431 -55 1085 C ATOM 1233 O VAL A 171 -74.832 -26.572 9.077 1.00 26.57 O ANISOU 1233 O VAL A 171 2525 3667 3902 -516 -19 1133 O ATOM 1234 CB VAL A 171 -72.381 -24.989 9.884 1.00 27.40 C ANISOU 1234 CB VAL A 171 2825 3740 3848 -342 -19 1073 C ATOM 1235 CG1 VAL A 171 -71.739 -25.199 8.522 1.00 23.62 C ANISOU 1235 CG1 VAL A 171 2419 3158 3396 -363 -123 1064 C ATOM 1236 CG2 VAL A 171 -71.570 -24.005 10.714 1.00 14.35 C ANISOU 1236 CG2 VAL A 171 1222 2116 2116 -250 13 1025 C ATOM 1237 N GLU A 172 -75.092 -24.817 7.687 1.00 41.48 N ANISOU 1237 N GLU A 172 4352 5544 5863 -410 -147 1050 N ATOM 1238 CA GLU A 172 -75.933 -25.550 6.751 1.00 40.43 C ANISOU 1238 CA GLU A 172 4153 5399 5809 -498 -207 1069 C ATOM 1239 C GLU A 172 -75.136 -26.641 6.045 1.00 30.35 C ANISOU 1239 C GLU A 172 3015 4021 4496 -561 -256 1079 C ATOM 1240 O GLU A 172 -73.920 -26.538 5.866 1.00 30.67 O ANISOU 1240 O GLU A 172 3172 4000 4481 -533 -279 1074 O ATOM 1241 CB GLU A 172 -76.540 -24.600 5.716 1.00 49.76 C ANISOU 1241 CB GLU A 172 5266 6587 7055 -443 -308 1027 C ATOM 1242 CG GLU A 172 -77.392 -23.473 6.294 1.00 61.58 C ANISOU 1242 CG GLU A 172 6635 8167 8596 -347 -272 989 C ATOM 1243 CD GLU A 172 -76.571 -22.281 6.763 1.00 67.80 C ANISOU 1243 CD GLU A 172 7496 8933 9330 -230 -254 948 C ATOM 1244 OE1 GLU A 172 -75.348 -22.437 6.971 1.00 67.13 O ANISOU 1244 OE1 GLU A 172 7550 8795 9163 -232 -240 955 O ATOM 1245 OE2 GLU A 172 -77.149 -21.183 6.921 1.00 69.67 O ANISOU 1245 OE2 GLU A 172 7650 9205 9614 -134 -257 903 O ATOM 1246 N ASP A 173 -75.840 -27.699 5.647 1.00 30.23 N ANISOU 1246 N ASP A 173 2990 3989 4508 -633 -270 1071 N ATOM 1247 CA ASP A 173 -75.211 -28.800 4.929 1.00 36.50 C ANISOU 1247 CA ASP A 173 3903 4691 5273 -676 -314 1050 C ATOM 1248 C ASP A 173 -74.654 -28.306 3.599 1.00 30.23 C ANISOU 1248 C ASP A 173 3164 3852 4472 -656 -420 1019 C ATOM 1249 O ASP A 173 -75.386 -27.743 2.778 1.00 36.49 O ANISOU 1249 O ASP A 173 3885 4669 5309 -660 -490 1008 O ATOM 1250 CB ASP A 173 -76.226 -29.927 4.715 1.00 50.89 C ANISOU 1250 CB ASP A 173 5683 6510 7142 -764 -308 1042 C ATOM 1251 CG ASP A 173 -75.632 -31.132 4.002 1.00 67.87 C ANISOU 1251 CG ASP A 173 7946 8566 9275 -807 -345 1011 C ATOM 1252 OD1 ASP A 173 -75.472 -31.083 2.763 1.00 77.03 O ANISOU 1252 OD1 ASP A 173 9137 9693 10439 -815 -432 973 O ATOM 1253 OD2 ASP A 173 -75.320 -32.131 4.685 1.00 73.12 O ANISOU 1253 OD2 ASP A 173 8670 9191 9921 -831 -285 1022 O ATOM 1254 N GLY A 174 -73.353 -28.501 3.394 1.00 25.35 N ANISOU 1254 N GLY A 174 2669 3173 3790 -627 -431 995 N ATOM 1255 CA GLY A 174 -72.678 -28.066 2.188 1.00 14.13 C ANISOU 1255 CA GLY A 174 1313 1713 2343 -611 -515 962 C ATOM 1256 C GLY A 174 -71.834 -26.820 2.351 1.00 23.39 C ANISOU 1256 C GLY A 174 2515 2890 3481 -541 -518 965 C ATOM 1257 O GLY A 174 -71.040 -26.512 1.453 1.00 39.97 O ANISOU 1257 O GLY A 174 4689 4959 5539 -526 -570 926 O ATOM 1258 N GLU A 175 -71.978 -26.092 3.453 1.00 13.54 N ANISOU 1258 N GLU A 175 1214 1683 2245 -501 -458 1002 N ATOM 1259 CA GLU A 175 -71.175 -24.911 3.730 1.00 20.79 C ANISOU 1259 CA GLU A 175 2175 2597 3127 -425 -451 996 C ATOM 1260 C GLU A 175 -70.157 -25.214 4.825 1.00 28.54 C ANISOU 1260 C GLU A 175 3224 3585 4036 -383 -370 956 C ATOM 1261 O GLU A 175 -70.198 -26.262 5.476 1.00 17.45 O ANISOU 1261 O GLU A 175 1825 2187 2618 -409 -321 963 O ATOM 1262 CB GLU A 175 -72.070 -23.728 4.121 1.00 28.96 C ANISOU 1262 CB GLU A 175 3111 3693 4199 -353 -444 982 C ATOM 1263 CG GLU A 175 -72.888 -23.181 2.960 1.00 52.51 C ANISOU 1263 CG GLU A 175 6040 6679 7234 -348 -542 975 C ATOM 1264 CD GLU A 175 -73.733 -21.980 3.345 1.00 65.55 C ANISOU 1264 CD GLU A 175 7591 8377 8936 -258 -541 957 C ATOM 1265 OE1 GLU A 175 -74.134 -21.887 4.523 1.00 66.90 O ANISOU 1265 OE1 GLU A 175 7694 8606 9121 -228 -452 950 O ATOM 1266 OE2 GLU A 175 -73.991 -21.128 2.467 1.00 66.40 O ANISOU 1266 OE2 GLU A 175 7699 8464 9067 -216 -623 946 O ATOM 1267 N CYS A 176 -69.224 -24.280 5.018 1.00 24.66 N ANISOU 1267 N CYS A 176 2785 3088 3498 -318 -361 910 N ATOM 1268 CA CYS A 176 -68.133 -24.476 5.969 1.00 13.67 C ANISOU 1268 CA CYS A 176 1456 1701 2039 -283 -301 868 C ATOM 1269 C CYS A 176 -67.707 -23.118 6.510 1.00 20.56 C ANISOU 1269 C CYS A 176 2337 2587 2886 -216 -286 855 C ATOM 1270 O CYS A 176 -67.014 -22.365 5.820 1.00 26.70 O ANISOU 1270 O CYS A 176 3163 3333 3649 -194 -316 792 O ATOM 1271 CB CYS A 176 -66.963 -25.197 5.308 1.00 14.20 C ANISOU 1271 CB CYS A 176 1606 1724 2066 -290 -313 791 C ATOM 1272 SG CYS A 176 -65.686 -25.709 6.459 1.00 27.98 S ANISOU 1272 SG CYS A 176 3414 3468 3748 -253 -255 761 S ATOM 1273 N TYR A 177 -68.108 -22.810 7.741 1.00 17.91 N ANISOU 1273 N TYR A 177 1958 2304 2541 -186 -235 915 N ATOM 1274 CA TYR A 177 -67.709 -21.568 8.393 1.00 13.86 C ANISOU 1274 CA TYR A 177 1455 1814 1999 -111 -217 874 C ATOM 1275 C TYR A 177 -67.810 -21.760 9.903 1.00 23.57 C ANISOU 1275 C TYR A 177 2662 3123 3171 -91 -132 878 C ATOM 1276 O TYR A 177 -68.236 -22.812 10.389 1.00 24.47 O ANISOU 1276 O TYR A 177 2754 3270 3272 -139 -89 936 O ATOM 1277 CB TYR A 177 -68.561 -20.395 7.907 1.00 11.40 C ANISOU 1277 CB TYR A 177 1082 1498 1751 -64 -248 839 C ATOM 1278 CG TYR A 177 -70.045 -20.608 8.071 1.00 23.97 C ANISOU 1278 CG TYR A 177 2557 3147 3401 -71 -223 859 C ATOM 1279 CD1 TYR A 177 -70.807 -21.163 7.049 1.00 12.56 C ANISOU 1279 CD1 TYR A 177 1070 1686 2018 -124 -278 894 C ATOM 1280 CD2 TYR A 177 -70.687 -20.255 9.251 1.00 20.91 C ANISOU 1280 CD2 TYR A 177 2098 2841 3007 -27 -143 833 C ATOM 1281 CE1 TYR A 177 -72.166 -21.361 7.199 1.00 13.55 C ANISOU 1281 CE1 TYR A 177 1072 1871 2204 -136 -257 908 C ATOM 1282 CE2 TYR A 177 -72.043 -20.448 9.411 1.00 27.83 C ANISOU 1282 CE2 TYR A 177 2852 3781 3941 -36 -111 846 C ATOM 1283 CZ TYR A 177 -72.778 -21.001 8.382 1.00 35.52 C ANISOU 1283 CZ TYR A 177 3776 4736 4986 -91 -170 885 C ATOM 1284 OH TYR A 177 -74.131 -21.195 8.542 1.00 37.39 O ANISOU 1284 OH TYR A 177 3876 5043 5289 -106 -140 893 O ATOM 1285 N ILE A 178 -67.406 -20.731 10.647 1.00 26.62 N ANISOU 1285 N ILE A 178 3059 3537 3517 -25 -108 817 N ATOM 1286 CA ILE A 178 -67.386 -20.763 12.107 1.00 23.06 C ANISOU 1286 CA ILE A 178 2599 3175 2989 -1 -31 808 C ATOM 1287 C ILE A 178 -68.638 -20.083 12.638 1.00 25.86 C ANISOU 1287 C ILE A 178 2854 3599 3372 39 26 770 C ATOM 1288 O ILE A 178 -68.960 -18.956 12.241 1.00 27.57 O ANISOU 1288 O ILE A 178 3040 3788 3648 95 0 708 O ATOM 1289 CB ILE A 178 -66.123 -20.088 12.666 1.00 26.33 C ANISOU 1289 CB ILE A 178 3085 3587 3332 43 -41 748 C ATOM 1290 CG1 ILE A 178 -64.898 -20.977 12.445 1.00 27.60 C ANISOU 1290 CG1 ILE A 178 3325 3707 3453 7 -79 789 C ATOM 1291 CG2 ILE A 178 -66.299 -19.784 14.140 1.00 26.80 C ANISOU 1291 CG2 ILE A 178 3124 3750 3307 80 35 713 C ATOM 1292 CD1 ILE A 178 -63.614 -20.377 12.975 1.00 18.56 C ANISOU 1292 CD1 ILE A 178 2237 2570 2244 43 -96 730 C ATOM 1293 N GLN A 179 -69.335 -20.762 13.552 1.00 30.98 N ANISOU 1293 N GLN A 179 3452 4337 3982 12 107 809 N ATOM 1294 CA GLN A 179 -70.586 -20.228 14.083 1.00 41.68 C ANISOU 1294 CA GLN A 179 4695 5775 5365 46 177 771 C ATOM 1295 C GLN A 179 -70.346 -19.007 14.964 1.00 43.77 C ANISOU 1295 C GLN A 179 4964 6085 5582 133 216 666 C ATOM 1296 O GLN A 179 -70.995 -17.969 14.787 1.00 41.95 O ANISOU 1296 O GLN A 179 4667 5850 5423 200 215 592 O ATOM 1297 CB GLN A 179 -71.327 -21.309 14.869 1.00 41.50 C ANISOU 1297 CB GLN A 179 4621 5845 5302 -20 267 844 C ATOM 1298 CG GLN A 179 -71.774 -22.495 14.045 1.00 35.52 C ANISOU 1298 CG GLN A 179 3845 5041 4611 -113 236 936 C ATOM 1299 CD GLN A 179 -72.557 -23.490 14.869 1.00 36.62 C ANISOU 1299 CD GLN A 179 3931 5267 4718 -188 332 1011 C ATOM 1300 OE1 GLN A 179 -72.456 -24.700 14.664 1.00 50.89 O ANISOU 1300 OE1 GLN A 179 5775 7032 6528 -274 322 1102 O ATOM 1301 NE2 GLN A 179 -73.343 -22.985 15.815 1.00 27.79 N ANISOU 1301 NE2 GLN A 179 2725 4267 3568 -158 431 971 N ATOM 1302 N PHE A 180 -69.424 -19.111 15.926 1.00 43.69 N ANISOU 1302 N PHE A 180 5030 6118 5453 137 244 655 N ATOM 1303 CA PHE A 180 -69.299 -18.048 16.917 1.00 35.52 C ANISOU 1303 CA PHE A 180 3994 5146 4358 210 292 546 C ATOM 1304 C PHE A 180 -68.744 -16.752 16.341 1.00 45.60 C ANISOU 1304 C PHE A 180 5304 6326 5697 274 222 451 C ATOM 1305 O PHE A 180 -68.762 -15.735 17.042 1.00 52.02 O ANISOU 1305 O PHE A 180 6108 7170 6488 340 256 343 O ATOM 1306 CB PHE A 180 -68.445 -18.504 18.109 1.00 21.74 C ANISOU 1306 CB PHE A 180 2323 3482 2456 194 329 559 C ATOM 1307 CG PHE A 180 -67.041 -18.922 17.753 1.00 24.22 C ANISOU 1307 CG PHE A 180 2741 3723 2737 168 244 597 C ATOM 1308 CD1 PHE A 180 -66.048 -17.978 17.544 1.00 14.86 C ANISOU 1308 CD1 PHE A 180 1610 2478 1557 209 183 511 C ATOM 1309 CD2 PHE A 180 -66.704 -20.265 17.683 1.00 33.47 C ANISOU 1309 CD2 PHE A 180 3955 4888 3876 104 230 715 C ATOM 1310 CE1 PHE A 180 -64.756 -18.365 17.235 1.00 16.49 C ANISOU 1310 CE1 PHE A 180 1896 2632 1737 185 112 540 C ATOM 1311 CE2 PHE A 180 -65.412 -20.659 17.379 1.00 27.04 C ANISOU 1311 CE2 PHE A 180 3224 4011 3038 92 155 741 C ATOM 1312 CZ PHE A 180 -64.437 -19.707 17.153 1.00 19.29 C ANISOU 1312 CZ PHE A 180 2282 2985 2061 133 98 652 C ATOM 1313 N PHE A 181 -68.266 -16.752 15.096 1.00 44.65 N ANISOU 1313 N PHE A 181 5225 6088 5652 253 129 485 N ATOM 1314 CA PHE A 181 -67.869 -15.522 14.425 1.00 36.89 C ANISOU 1314 CA PHE A 181 4272 5004 4741 302 64 414 C ATOM 1315 C PHE A 181 -69.040 -14.824 13.742 1.00 36.13 C ANISOU 1315 C PHE A 181 4092 4867 4768 350 47 394 C ATOM 1316 O PHE A 181 -68.823 -13.949 12.896 1.00 24.98 O ANISOU 1316 O PHE A 181 2710 3349 3434 380 -24 370 O ATOM 1317 CB PHE A 181 -66.758 -15.797 13.411 1.00 24.92 C ANISOU 1317 CB PHE A 181 2842 3391 3234 252 -22 460 C ATOM 1318 CG PHE A 181 -65.377 -15.727 13.996 1.00 29.89 C ANISOU 1318 CG PHE A 181 3554 4029 3775 243 -31 425 C ATOM 1319 CD1 PHE A 181 -64.889 -14.538 14.507 1.00 34.65 C ANISOU 1319 CD1 PHE A 181 4183 4616 4367 291 -32 318 C ATOM 1320 CD2 PHE A 181 -64.564 -16.846 14.028 1.00 36.56 C ANISOU 1320 CD2 PHE A 181 4444 4890 4555 189 -45 492 C ATOM 1321 CE1 PHE A 181 -63.619 -14.467 15.042 1.00 41.78 C ANISOU 1321 CE1 PHE A 181 5150 5534 5192 277 -48 279 C ATOM 1322 CE2 PHE A 181 -63.293 -16.782 14.564 1.00 42.31 C ANISOU 1322 CE2 PHE A 181 5234 5632 5208 187 -62 458 C ATOM 1323 CZ PHE A 181 -62.820 -15.591 15.071 1.00 42.49 C ANISOU 1323 CZ PHE A 181 5275 5652 5215 227 -65 351 C ATOM 1324 N SER A 182 -70.275 -15.199 14.084 1.00 35.69 N ANISOU 1324 N SER A 182 3931 4894 4737 357 109 410 N ATOM 1325 CA SER A 182 -71.432 -14.471 13.579 1.00 40.58 C ANISOU 1325 CA SER A 182 4450 5489 5478 421 94 378 C ATOM 1326 C SER A 182 -71.579 -13.120 14.263 1.00 54.14 C ANISOU 1326 C SER A 182 6149 7201 7219 524 127 250 C ATOM 1327 O SER A 182 -72.022 -12.152 13.634 1.00 60.28 O ANISOU 1327 O SER A 182 6898 7895 8111 595 74 212 O ATOM 1328 CB SER A 182 -72.699 -15.303 13.768 1.00 46.26 C ANISOU 1328 CB SER A 182 5045 6310 6221 391 156 426 C ATOM 1329 OG SER A 182 -73.847 -14.586 13.349 1.00 56.56 O ANISOU 1329 OG SER A 182 6235 7605 7650 463 140 387 O ATOM 1330 N ASN A 183 -71.218 -13.033 15.541 1.00 50.55 N ANISOU 1330 N ASN A 183 5716 6833 6659 537 210 181 N ATOM 1331 CA ASN A 183 -71.256 -11.762 16.252 1.00 56.28 C ANISOU 1331 CA ASN A 183 6436 7552 7397 632 244 39 C ATOM 1332 C ASN A 183 -70.110 -10.878 15.776 1.00 58.01 C ANISOU 1332 C ASN A 183 6770 7633 7640 644 157 -2 C ATOM 1333 O ASN A 183 -68.944 -11.284 15.821 1.00 58.39 O ANISOU 1333 O ASN A 183 6913 7670 7602 580 129 29 O ATOM 1334 CB ASN A 183 -71.169 -11.995 17.758 1.00 55.88 C ANISOU 1334 CB ASN A 183 6381 7647 7203 631 357 -24 C ATOM 1335 CG ASN A 183 -71.270 -10.709 18.552 1.00 61.99 C ANISOU 1335 CG ASN A 183 7145 8424 7984 729 401 -190 C ATOM 1336 OD1 ASN A 183 -71.773 -9.699 18.059 1.00 66.32 O ANISOU 1336 OD1 ASN A 183 7654 8878 8668 812 367 -256 O ATOM 1337 ND2 ASN A 183 -70.794 -10.739 19.790 1.00 64.19 N ANISOU 1337 ND2 ASN A 183 7463 8810 8116 722 471 -260 N ATOM 1338 N ALA A 184 -70.442 -9.670 15.315 1.00 57.65 N ANISOU 1338 N ALA A 184 6712 7478 7716 725 113 -69 N ATOM 1339 CA ALA A 184 -69.420 -8.766 14.800 1.00 46.41 C ANISOU 1339 CA ALA A 184 5397 5909 6329 727 33 -101 C ATOM 1340 C ALA A 184 -68.436 -8.329 15.875 1.00 45.37 C ANISOU 1340 C ALA A 184 5337 5803 6098 724 70 -210 C ATOM 1341 O ALA A 184 -67.307 -7.949 15.547 1.00 47.96 O ANISOU 1341 O ALA A 184 5761 6042 6419 684 10 -217 O ATOM 1342 CB ALA A 184 -70.074 -7.539 14.162 1.00 42.29 C ANISOU 1342 CB ALA A 184 4849 5256 5965 821 -20 -145 C ATOM 1343 N ALA A 185 -68.834 -8.374 17.147 1.00 44.67 N ANISOU 1343 N ALA A 185 5199 5844 5928 760 167 -299 N ATOM 1344 CA ALA A 185 -67.941 -7.941 18.217 1.00 47.20 C ANISOU 1344 CA ALA A 185 5587 6204 6143 759 197 -414 C ATOM 1345 C ALA A 185 -66.736 -8.866 18.344 1.00 45.49 C ANISOU 1345 C ALA A 185 5448 6038 5799 660 170 -338 C ATOM 1346 O ALA A 185 -65.598 -8.401 18.480 1.00 33.64 O ANISOU 1346 O ALA A 185 4028 4488 4265 634 125 -393 O ATOM 1347 CB ALA A 185 -68.705 -7.870 19.538 1.00 56.16 C ANISOU 1347 CB ALA A 185 6651 7487 7200 815 314 -520 C ATOM 1348 N VAL A 186 -66.965 -10.181 18.305 1.00 45.20 N ANISOU 1348 N VAL A 186 5383 6095 5696 605 194 -215 N ATOM 1349 CA VAL A 186 -65.850 -11.113 18.427 1.00 54.17 C ANISOU 1349 CA VAL A 186 6588 7272 6721 524 164 -140 C ATOM 1350 C VAL A 186 -64.971 -11.066 17.181 1.00 55.78 C ANISOU 1350 C VAL A 186 6853 7340 7000 477 65 -78 C ATOM 1351 O VAL A 186 -63.759 -11.307 17.259 1.00 58.36 O ANISOU 1351 O VAL A 186 7246 7665 7263 429 25 -71 O ATOM 1352 CB VAL A 186 -66.368 -12.536 18.718 1.00 48.04 C ANISOU 1352 CB VAL A 186 5771 6614 5868 478 217 -21 C ATOM 1353 CG1 VAL A 186 -67.047 -13.130 17.499 1.00 48.06 C ANISOU 1353 CG1 VAL A 186 5730 6552 5980 451 185 94 C ATOM 1354 CG2 VAL A 186 -65.232 -13.436 19.196 1.00 45.18 C ANISOU 1354 CG2 VAL A 186 5481 6312 5375 418 196 37 C ATOM 1355 N THR A 187 -65.549 -10.740 16.020 1.00 47.40 N ANISOU 1355 N THR A 187 5769 6171 6070 491 23 -36 N ATOM 1356 CA THR A 187 -64.738 -10.591 14.817 1.00 36.37 C ANISOU 1356 CA THR A 187 4435 4650 4733 443 -64 17 C ATOM 1357 C THR A 187 -63.873 -9.340 14.892 1.00 30.43 C ANISOU 1357 C THR A 187 3746 3804 4010 455 -99 -86 C ATOM 1358 O THR A 187 -62.714 -9.352 14.463 1.00 27.79 O ANISOU 1358 O THR A 187 3476 3422 3661 394 -148 -70 O ATOM 1359 CB THR A 187 -65.625 -10.545 13.573 1.00 37.04 C ANISOU 1359 CB THR A 187 4483 4654 4936 453 -105 94 C ATOM 1360 OG1 THR A 187 -66.352 -9.312 13.549 1.00 47.92 O ANISOU 1360 OG1 THR A 187 5833 5960 6415 536 -109 17 O ATOM 1361 CG2 THR A 187 -66.608 -11.698 13.575 1.00 37.49 C ANISOU 1361 CG2 THR A 187 4464 4805 4977 440 -66 177 C ATOM 1362 N PHE A 188 -64.417 -8.250 15.436 1.00 28.53 N ANISOU 1362 N PHE A 188 3486 3535 3819 530 -73 -199 N ATOM 1363 CA PHE A 188 -63.645 -7.017 15.536 1.00 32.39 C ANISOU 1363 CA PHE A 188 4040 3920 4349 537 -107 -306 C ATOM 1364 C PHE A 188 -62.542 -7.146 16.579 1.00 29.86 C ANISOU 1364 C PHE A 188 3758 3684 3903 498 -92 -384 C ATOM 1365 O PHE A 188 -61.375 -6.837 16.307 1.00 31.94 O ANISOU 1365 O PHE A 188 4083 3888 4166 439 -143 -401 O ATOM 1366 CB PHE A 188 -64.567 -5.843 15.864 1.00 36.50 C ANISOU 1366 CB PHE A 188 4527 4376 4964 637 -83 -417 C ATOM 1367 CG PHE A 188 -64.033 -4.517 15.412 1.00 45.06 C ANISOU 1367 CG PHE A 188 5682 5285 6155 643 -141 -483 C ATOM 1368 CD1 PHE A 188 -63.119 -3.821 16.186 1.00 50.00 C ANISOU 1368 CD1 PHE A 188 6362 5893 6742 624 -139 -613 C ATOM 1369 CD2 PHE A 188 -64.435 -3.973 14.203 1.00 45.97 C ANISOU 1369 CD2 PHE A 188 5812 5250 6405 660 -203 -411 C ATOM 1370 CE1 PHE A 188 -62.621 -2.601 15.767 1.00 51.79 C ANISOU 1370 CE1 PHE A 188 6657 5946 7076 617 -191 -672 C ATOM 1371 CE2 PHE A 188 -63.942 -2.755 13.778 1.00 49.77 C ANISOU 1371 CE2 PHE A 188 6368 5557 6986 658 -256 -457 C ATOM 1372 CZ PHE A 188 -63.034 -2.067 14.562 1.00 53.04 C ANISOU 1372 CZ PHE A 188 6835 5944 7372 633 -247 -589 C ATOM 1373 N GLY A 189 -62.892 -7.603 17.783 1.00 32.34 N ANISOU 1373 N GLY A 189 4035 4148 4105 527 -24 -431 N ATOM 1374 CA GLY A 189 -61.878 -7.815 18.802 1.00 27.60 C ANISOU 1374 CA GLY A 189 3471 3647 3368 492 -20 -493 C ATOM 1375 C GLY A 189 -60.839 -8.838 18.385 1.00 33.26 C ANISOU 1375 C GLY A 189 4218 4391 4027 412 -68 -384 C ATOM 1376 O GLY A 189 -59.656 -8.701 18.705 1.00 43.05 O ANISOU 1376 O GLY A 189 5499 5644 5213 371 -108 -432 O ATOM 1377 N THR A 190 -61.267 -9.876 17.661 1.00 33.22 N ANISOU 1377 N THR A 190 4188 4396 4038 391 -68 -242 N ATOM 1378 CA THR A 190 -60.319 -10.866 17.157 1.00 35.19 C ANISOU 1378 CA THR A 190 4463 4656 4251 324 -113 -143 C ATOM 1379 C THR A 190 -59.403 -10.263 16.099 1.00 35.18 C ANISOU 1379 C THR A 190 4504 4525 4336 277 -179 -147 C ATOM 1380 O THR A 190 -58.218 -10.608 16.026 1.00 38.81 O ANISOU 1380 O THR A 190 4989 4999 4756 226 -218 -138 O ATOM 1381 CB THR A 190 -61.068 -12.072 16.589 1.00 28.13 C ANISOU 1381 CB THR A 190 3535 3786 3366 310 -95 -5 C ATOM 1382 OG1 THR A 190 -61.948 -12.603 17.587 1.00 35.74 O ANISOU 1382 OG1 THR A 190 4457 4871 4251 341 -24 4 O ATOM 1383 CG2 THR A 190 -60.087 -13.155 16.158 1.00 20.64 C ANISOU 1383 CG2 THR A 190 2614 2848 2379 251 -137 85 C ATOM 1384 N ALA A 191 -59.934 -9.366 15.266 1.00 28.88 N ANISOU 1384 N ALA A 191 3713 3603 3658 293 -194 -157 N ATOM 1385 CA ALA A 191 -59.094 -8.709 14.272 1.00 25.22 C ANISOU 1385 CA ALA A 191 3297 3015 3271 240 -249 -155 C ATOM 1386 C ALA A 191 -58.099 -7.760 14.926 1.00 29.34 C ANISOU 1386 C ALA A 191 3853 3515 3779 220 -266 -282 C ATOM 1387 O ALA A 191 -56.970 -7.619 14.441 1.00 33.42 O ANISOU 1387 O ALA A 191 4400 3990 4309 150 -305 -281 O ATOM 1388 CB ALA A 191 -59.961 -7.962 13.258 1.00 16.17 C ANISOU 1388 CB ALA A 191 2156 1738 2249 265 -268 -121 C ATOM 1389 N ILE A 192 -58.490 -7.114 16.026 1.00 25.90 N ANISOU 1389 N ILE A 192 3408 3114 3318 276 -235 -400 N ATOM 1390 CA ILE A 192 -57.583 -6.198 16.711 1.00 33.03 C ANISOU 1390 CA ILE A 192 4344 3998 4206 254 -255 -538 C ATOM 1391 C ILE A 192 -56.494 -6.974 17.443 1.00 35.18 C ANISOU 1391 C ILE A 192 4611 4406 4351 211 -271 -549 C ATOM 1392 O ILE A 192 -55.301 -6.672 17.316 1.00 37.88 O ANISOU 1392 O ILE A 192 4972 4722 4698 146 -316 -590 O ATOM 1393 CB ILE A 192 -58.365 -5.285 17.673 1.00 31.05 C ANISOU 1393 CB ILE A 192 4087 3747 3963 332 -214 -675 C ATOM 1394 CG1 ILE A 192 -59.334 -4.388 16.896 1.00 39.33 C ANISOU 1394 CG1 ILE A 192 5140 4640 5163 384 -214 -670 C ATOM 1395 CG2 ILE A 192 -57.408 -4.459 18.522 1.00 18.77 C ANISOU 1395 CG2 ILE A 192 2566 2194 2373 304 -236 -833 C ATOM 1396 CD1 ILE A 192 -58.671 -3.530 15.839 1.00 46.57 C ANISOU 1396 CD1 ILE A 192 6117 5379 6200 324 -273 -654 C ATOM 1397 N ALA A 193 -56.886 -7.989 18.216 1.00 26.54 N ANISOU 1397 N ALA A 193 3486 3457 3141 245 -237 -509 N ATOM 1398 CA ALA A 193 -55.923 -8.701 19.047 1.00 28.89 C ANISOU 1398 CA ALA A 193 3782 3888 3309 220 -260 -518 C ATOM 1399 C ALA A 193 -55.063 -9.673 18.249 1.00 28.39 C ANISOU 1399 C ALA A 193 3712 3824 3250 166 -303 -403 C ATOM 1400 O ALA A 193 -53.907 -9.913 18.615 1.00 30.66 O ANISOU 1400 O ALA A 193 3997 4171 3480 133 -348 -431 O ATOM 1401 CB ALA A 193 -56.651 -9.447 20.166 1.00 16.65 C ANISOU 1401 CB ALA A 193 2211 2489 1627 272 -208 -502 C ATOM 1402 N ALA A 194 -55.593 -10.236 17.165 1.00 23.00 N ANISOU 1402 N ALA A 194 3023 3080 2637 160 -292 -284 N ATOM 1403 CA ALA A 194 -54.892 -11.283 16.434 1.00 25.07 C ANISOU 1403 CA ALA A 194 3279 3350 2899 118 -322 -181 C ATOM 1404 C ALA A 194 -54.071 -10.767 15.258 1.00 29.86 C ANISOU 1404 C ALA A 194 3899 3847 3600 53 -356 -182 C ATOM 1405 O ALA A 194 -53.194 -11.492 14.773 1.00 24.10 O ANISOU 1405 O ALA A 194 3158 3136 2863 14 -381 -133 O ATOM 1406 CB ALA A 194 -55.888 -12.329 15.924 1.00 21.12 C ANISOU 1406 CB ALA A 194 2764 2855 2407 138 -290 -54 C ATOM 1407 N PHE A 195 -54.326 -9.548 14.782 1.00 47.61 N ANISOU 1407 N PHE A 195 6173 5981 5938 39 -355 -234 N ATOM 1408 CA PHE A 195 -53.615 -9.072 13.603 1.00 25.01 C ANISOU 1408 CA PHE A 195 3331 3013 3158 -34 -380 -216 C ATOM 1409 C PHE A 195 -53.072 -7.659 13.775 1.00 17.22 C ANISOU 1409 C PHE A 195 2372 1944 2228 -71 -398 -330 C ATOM 1410 O PHE A 195 -51.857 -7.449 13.718 1.00 13.93 O ANISOU 1410 O PHE A 195 1948 1532 1812 -140 -424 -375 O ATOM 1411 CB PHE A 195 -54.522 -9.131 12.372 1.00 12.24 C ANISOU 1411 CB PHE A 195 1732 1305 1614 -32 -370 -115 C ATOM 1412 CG PHE A 195 -53.827 -8.760 11.092 1.00 13.91 C ANISOU 1412 CG PHE A 195 1973 1422 1890 -113 -389 -77 C ATOM 1413 CD1 PHE A 195 -52.934 -9.637 10.493 1.00 11.40 C ANISOU 1413 CD1 PHE A 195 1638 1150 1544 -166 -394 -28 C ATOM 1414 CD2 PHE A 195 -54.060 -7.536 10.489 1.00 12.58 C ANISOU 1414 CD2 PHE A 195 1851 1121 1810 -136 -399 -90 C ATOM 1415 CE1 PHE A 195 -52.290 -9.300 9.319 1.00 11.34 C ANISOU 1415 CE1 PHE A 195 1655 1072 1583 -246 -399 3 C ATOM 1416 CE2 PHE A 195 -53.419 -7.196 9.313 1.00 14.80 C ANISOU 1416 CE2 PHE A 195 2165 1321 2135 -220 -411 -44 C ATOM 1417 CZ PHE A 195 -52.533 -8.080 8.728 1.00 11.91 C ANISOU 1417 CZ PHE A 195 1778 1018 1729 -279 -406 0 C ATOM 1418 N TYR A 196 -53.960 -6.686 13.986 1.00 25.74 N ANISOU 1418 N TYR A 196 3477 2943 3361 -27 -384 -382 N ATOM 1419 CA TYR A 196 -53.554 -5.285 13.916 1.00 28.44 C ANISOU 1419 CA TYR A 196 3859 3162 3786 -68 -402 -476 C ATOM 1420 C TYR A 196 -52.586 -4.920 15.036 1.00 24.53 C ANISOU 1420 C TYR A 196 3351 2734 3235 -95 -421 -615 C ATOM 1421 O TYR A 196 -51.529 -4.326 14.786 1.00 27.13 O ANISOU 1421 O TYR A 196 3691 3011 3606 -181 -449 -665 O ATOM 1422 CB TYR A 196 -54.791 -4.386 13.936 1.00 22.25 C ANISOU 1422 CB TYR A 196 3103 2272 3081 4 -387 -504 C ATOM 1423 CG TYR A 196 -55.559 -4.415 12.633 1.00 20.02 C ANISOU 1423 CG TYR A 196 2839 1888 2878 11 -391 -375 C ATOM 1424 CD1 TYR A 196 -55.090 -3.732 11.517 1.00 15.70 C ANISOU 1424 CD1 TYR A 196 2345 1205 2417 -63 -420 -328 C ATOM 1425 CD2 TYR A 196 -56.745 -5.130 12.513 1.00 21.83 C ANISOU 1425 CD2 TYR A 196 3036 2167 3092 85 -370 -297 C ATOM 1426 CE1 TYR A 196 -55.782 -3.752 10.322 1.00 15.38 C ANISOU 1426 CE1 TYR A 196 2329 1083 2433 -57 -433 -206 C ATOM 1427 CE2 TYR A 196 -57.445 -5.157 11.319 1.00 14.71 C ANISOU 1427 CE2 TYR A 196 2149 1183 2259 90 -386 -184 C ATOM 1428 CZ TYR A 196 -56.957 -4.465 10.229 1.00 14.88 C ANISOU 1428 CZ TYR A 196 2229 1073 2353 22 -421 -138 C ATOM 1429 OH TYR A 196 -57.643 -4.488 9.038 1.00 26.03 O ANISOU 1429 OH TYR A 196 3661 2412 3816 26 -447 -21 O ATOM 1430 N LEU A 197 -52.929 -5.262 16.278 1.00 19.86 N ANISOU 1430 N LEU A 197 2736 2265 2544 -29 -407 -679 N ATOM 1431 CA LEU A 197 -52.003 -5.019 17.384 1.00 27.79 C ANISOU 1431 CA LEU A 197 3728 3358 3474 -53 -435 -809 C ATOM 1432 C LEU A 197 -50.666 -5.724 17.182 1.00 29.73 C ANISOU 1432 C LEU A 197 3936 3680 3679 -124 -476 -775 C ATOM 1433 O LEU A 197 -49.620 -5.061 17.312 1.00 22.73 O ANISOU 1433 O LEU A 197 3044 2774 2819 -197 -513 -870 O ATOM 1434 CB LEU A 197 -52.666 -5.415 18.710 1.00 29.92 C ANISOU 1434 CB LEU A 197 3983 3766 3619 31 -409 -862 C ATOM 1435 CG LEU A 197 -51.843 -5.245 19.988 1.00 24.86 C ANISOU 1435 CG LEU A 197 3332 3245 2868 19 -443 -997 C ATOM 1436 CD1 LEU A 197 -51.569 -3.776 20.265 1.00 20.88 C ANISOU 1436 CD1 LEU A 197 2862 2636 2437 -14 -459 -1165 C ATOM 1437 CD2 LEU A 197 -52.549 -5.898 21.163 1.00 20.38 C ANISOU 1437 CD2 LEU A 197 2754 2836 2153 98 -408 -1005 C ATOM 1438 N PRO A 198 -50.610 -7.026 16.857 1.00 15.95 N ANISOU 1438 N PRO A 198 2159 2018 1881 -108 -473 -653 N ATOM 1439 CA PRO A 198 -49.299 -7.629 16.566 1.00 21.37 C ANISOU 1439 CA PRO A 198 2803 2764 2553 -169 -513 -630 C ATOM 1440 C PRO A 198 -48.543 -6.928 15.449 1.00 33.25 C ANISOU 1440 C PRO A 198 4313 4152 4170 -267 -519 -634 C ATOM 1441 O PRO A 198 -47.316 -6.798 15.534 1.00 38.19 O ANISOU 1441 O PRO A 198 4897 4815 4798 -334 -554 -693 O ATOM 1442 CB PRO A 198 -49.659 -9.074 16.195 1.00 21.13 C ANISOU 1442 CB PRO A 198 2754 2798 2478 -124 -497 -488 C ATOM 1443 CG PRO A 198 -50.927 -9.335 16.910 1.00 14.61 C ANISOU 1443 CG PRO A 198 1948 2012 1591 -42 -462 -468 C ATOM 1444 CD PRO A 198 -51.680 -8.043 16.851 1.00 15.18 C ANISOU 1444 CD PRO A 198 2058 1974 1737 -35 -436 -542 C ATOM 1445 N VAL A 199 -49.236 -6.463 14.406 1.00 27.81 N ANISOU 1445 N VAL A 199 3669 3328 3570 -282 -488 -569 N ATOM 1446 CA VAL A 199 -48.556 -5.762 13.318 1.00 26.59 C ANISOU 1446 CA VAL A 199 3531 3061 3512 -384 -488 -559 C ATOM 1447 C VAL A 199 -47.934 -4.465 13.822 1.00 27.89 C ANISOU 1447 C VAL A 199 3709 3160 3726 -448 -511 -696 C ATOM 1448 O VAL A 199 -46.796 -4.126 13.468 1.00 21.47 O ANISOU 1448 O VAL A 199 2871 2333 2952 -551 -524 -731 O ATOM 1449 CB VAL A 199 -49.525 -5.512 12.146 1.00 24.13 C ANISOU 1449 CB VAL A 199 3276 2619 3272 -379 -459 -452 C ATOM 1450 CG1 VAL A 199 -48.937 -4.501 11.169 1.00 15.58 C ANISOU 1450 CG1 VAL A 199 2233 1402 2286 -488 -459 -448 C ATOM 1451 CG2 VAL A 199 -49.832 -6.814 11.428 1.00 13.81 C ANISOU 1451 CG2 VAL A 199 1948 1373 1924 -352 -442 -324 C ATOM 1452 N ILE A 200 -48.662 -3.720 14.660 1.00 22.97 N ANISOU 1452 N ILE A 200 3124 2499 3107 -392 -512 -785 N ATOM 1453 CA ILE A 200 -48.100 -2.501 15.238 1.00 25.17 C ANISOU 1453 CA ILE A 200 3420 2712 3433 -449 -537 -935 C ATOM 1454 C ILE A 200 -46.872 -2.829 16.076 1.00 31.10 C ANISOU 1454 C ILE A 200 4102 3608 4108 -493 -580 -1029 C ATOM 1455 O ILE A 200 -45.841 -2.145 15.995 1.00 20.33 O ANISOU 1455 O ILE A 200 2721 2206 2798 -599 -606 -1109 O ATOM 1456 CB ILE A 200 -49.165 -1.756 16.064 1.00 28.63 C ANISOU 1456 CB ILE A 200 3904 3096 3877 -363 -526 -1028 C ATOM 1457 CG1 ILE A 200 -50.302 -1.280 15.160 1.00 33.18 C ANISOU 1457 CG1 ILE A 200 4541 3513 4556 -322 -496 -940 C ATOM 1458 CG2 ILE A 200 -48.544 -0.584 16.806 1.00 21.37 C ANISOU 1458 CG2 ILE A 200 3002 2122 2995 -419 -557 -1206 C ATOM 1459 CD1 ILE A 200 -51.424 -0.591 15.905 1.00 35.92 C ANISOU 1459 CD1 ILE A 200 4919 3805 4923 -221 -479 -1031 C ATOM 1460 N ILE A 201 -46.959 -3.891 16.882 1.00 36.91 N ANISOU 1460 N ILE A 201 4794 4511 4717 -416 -592 -1016 N ATOM 1461 CA ILE A 201 -45.818 -4.317 17.689 1.00 28.79 C ANISOU 1461 CA ILE A 201 3698 3635 3608 -442 -647 -1089 C ATOM 1462 C ILE A 201 -44.611 -4.601 16.800 1.00 32.07 C ANISOU 1462 C ILE A 201 4052 4056 4078 -538 -662 -1046 C ATOM 1463 O ILE A 201 -43.505 -4.109 17.053 1.00 29.28 O ANISOU 1463 O ILE A 201 3658 3725 3744 -616 -693 -1123 O ATOM 1464 CB ILE A 201 -46.195 -5.542 18.543 1.00 21.91 C ANISOU 1464 CB ILE A 201 2802 2931 2593 -338 -657 -1039 C ATOM 1465 CG1 ILE A 201 -47.320 -5.180 19.513 1.00 19.59 C ANISOU 1465 CG1 ILE A 201 2559 2651 2234 -255 -633 -1102 C ATOM 1466 CG2 ILE A 201 -44.983 -6.067 19.295 1.00 19.65 C ANISOU 1466 CG2 ILE A 201 2442 2803 2223 -356 -728 -1094 C ATOM 1467 CD1 ILE A 201 -47.920 -6.364 20.229 1.00 19.14 C ANISOU 1467 CD1 ILE A 201 2493 2740 2040 -159 -622 -1026 C ATOM 1468 N MET A 202 -44.807 -5.390 15.737 1.00 18.08 N ANISOU 1468 N MET A 202 2275 2264 2329 -529 -625 -902 N ATOM 1469 CA MET A 202 -43.701 -5.705 14.837 1.00 21.46 C ANISOU 1469 CA MET A 202 2641 2707 2805 -616 -624 -865 C ATOM 1470 C MET A 202 -43.139 -4.452 14.180 1.00 23.36 C ANISOU 1470 C MET A 202 2899 2817 3159 -747 -610 -919 C ATOM 1471 O MET A 202 -41.929 -4.366 13.936 1.00 27.67 O ANISOU 1471 O MET A 202 3388 3399 3726 -822 -613 -922 O ATOM 1472 CB MET A 202 -44.152 -6.696 13.765 1.00 21.89 C ANISOU 1472 CB MET A 202 2704 2751 2863 -582 -579 -712 C ATOM 1473 CG MET A 202 -44.658 -8.026 14.289 1.00 32.49 C ANISOU 1473 CG MET A 202 4030 4207 4109 -467 -590 -643 C ATOM 1474 SD MET A 202 -45.395 -9.002 12.961 1.00 46.54 S ANISOU 1474 SD MET A 202 5837 5937 5908 -438 -535 -479 S ATOM 1475 CE MET A 202 -46.271 -10.256 13.894 1.00 49.10 C ANISOU 1475 CE MET A 202 6164 6363 6127 -307 -547 -417 C ATOM 1476 N THR A 203 -43.998 -3.473 13.892 1.00 25.40 N ANISOU 1476 N THR A 203 3250 2919 3483 -755 -584 -917 N ATOM 1477 CA THR A 203 -43.540 -2.243 13.254 1.00 20.00 C ANISOU 1477 CA THR A 203 2611 2095 2894 -867 -562 -921 C ATOM 1478 C THR A 203 -42.655 -1.435 14.193 1.00 36.29 C ANISOU 1478 C THR A 203 4656 4185 4948 -909 -597 -1031 C ATOM 1479 O THR A 203 -41.589 -0.949 13.795 1.00 42.10 O ANISOU 1479 O THR A 203 5365 4902 5728 -1006 -598 -1024 O ATOM 1480 CB THR A 203 -44.741 -1.415 12.800 1.00 22.00 C ANISOU 1480 CB THR A 203 2970 2168 3221 -846 -536 -890 C ATOM 1481 OG1 THR A 203 -45.631 -2.247 12.047 1.00 18.71 O ANISOU 1481 OG1 THR A 203 2573 1747 2790 -777 -513 -759 O ATOM 1482 CG2 THR A 203 -44.289 -0.246 11.934 1.00 21.06 C ANISOU 1482 CG2 THR A 203 2914 1909 3178 -962 -502 -846 C ATOM 1483 N VAL A 204 -43.082 -1.279 15.449 1.00 33.84 N ANISOU 1483 N VAL A 204 4355 3921 4579 -836 -627 -1135 N ATOM 1484 CA VAL A 204 -42.258 -0.565 16.422 1.00 34.43 C ANISOU 1484 CA VAL A 204 4413 4033 4636 -873 -665 -1245 C ATOM 1485 C VAL A 204 -40.952 -1.312 16.663 1.00 25.10 C ANISOU 1485 C VAL A 204 3123 3009 3406 -899 -701 -1242 C ATOM 1486 O VAL A 204 -39.870 -0.709 16.701 1.00 24.85 O ANISOU 1486 O VAL A 204 3057 2972 3414 -985 -721 -1281 O ATOM 1487 CB VAL A 204 -43.043 -0.352 17.730 1.00 37.71 C ANISOU 1487 CB VAL A 204 4863 4486 4981 -779 -684 -1354 C ATOM 1488 CG1 VAL A 204 -42.164 0.310 18.777 1.00 32.77 C ANISOU 1488 CG1 VAL A 204 4217 3910 4323 -819 -728 -1470 C ATOM 1489 CG2 VAL A 204 -44.286 0.483 17.468 1.00 32.67 C ANISOU 1489 CG2 VAL A 204 4322 3678 4412 -745 -646 -1367 C ATOM 1490 N LEU A 205 -41.030 -2.637 16.812 1.00 23.87 N ANISOU 1490 N LEU A 205 2909 2989 3170 -821 -714 -1194 N ATOM 1491 CA LEU A 205 -39.836 -3.435 17.072 1.00 29.93 C ANISOU 1491 CA LEU A 205 3572 3903 3896 -824 -751 -1185 C ATOM 1492 C LEU A 205 -38.826 -3.305 15.940 1.00 44.53 C ANISOU 1492 C LEU A 205 5368 5713 5836 -924 -723 -1133 C ATOM 1493 O LEU A 205 -37.645 -3.035 16.181 1.00 47.42 O ANISOU 1493 O LEU A 205 5666 6128 6222 -980 -750 -1179 O ATOM 1494 CB LEU A 205 -40.216 -4.899 17.289 1.00 21.60 C ANISOU 1494 CB LEU A 205 2480 2976 2751 -716 -766 -1119 C ATOM 1495 CG LEU A 205 -40.897 -5.212 18.620 1.00 21.78 C ANISOU 1495 CG LEU A 205 2531 3090 2653 -614 -803 -1164 C ATOM 1496 CD1 LEU A 205 -41.142 -6.705 18.755 1.00 23.95 C ANISOU 1496 CD1 LEU A 205 2772 3486 2842 -516 -820 -1073 C ATOM 1497 CD2 LEU A 205 -40.068 -4.689 19.782 1.00 23.39 C ANISOU 1497 CD2 LEU A 205 2710 3365 2813 -632 -857 -1263 C ATOM 1498 N TYR A 206 -39.272 -3.489 14.693 1.00 41.41 N ANISOU 1498 N TYR A 206 5003 5236 5494 -947 -667 -1039 N ATOM 1499 CA TYR A 206 -38.359 -3.321 13.566 1.00 36.50 C ANISOU 1499 CA TYR A 206 4338 4580 4951 -1043 -629 -987 C ATOM 1500 C TYR A 206 -37.834 -1.892 13.492 1.00 30.59 C ANISOU 1500 C TYR A 206 3621 3722 4279 -1150 -629 -1034 C ATOM 1501 O TYR A 206 -36.677 -1.666 13.117 1.00 25.45 O ANISOU 1501 O TYR A 206 2900 3095 3676 -1230 -622 -1039 O ATOM 1502 CB TYR A 206 -39.043 -3.700 12.251 1.00 26.63 C ANISOU 1502 CB TYR A 206 3130 3256 3733 -1048 -567 -874 C ATOM 1503 CG TYR A 206 -38.213 -3.331 11.041 1.00 26.95 C ANISOU 1503 CG TYR A 206 3143 3247 3850 -1148 -516 -818 C ATOM 1504 CD1 TYR A 206 -38.419 -2.129 10.372 1.00 39.28 C ANISOU 1504 CD1 TYR A 206 4783 4653 5491 -1226 -490 -788 C ATOM 1505 CD2 TYR A 206 -37.203 -4.168 10.584 1.00 30.76 C ANISOU 1505 CD2 TYR A 206 3520 3842 4327 -1160 -493 -799 C ATOM 1506 CE1 TYR A 206 -37.653 -1.778 9.277 1.00 39.23 C ANISOU 1506 CE1 TYR A 206 4748 4612 5547 -1316 -439 -734 C ATOM 1507 CE2 TYR A 206 -36.432 -3.825 9.488 1.00 30.55 C ANISOU 1507 CE2 TYR A 206 3462 3785 4359 -1252 -434 -758 C ATOM 1508 CZ TYR A 206 -36.663 -2.629 8.840 1.00 39.42 C ANISOU 1508 CZ TYR A 206 4666 4762 5551 -1332 -405 -722 C ATOM 1509 OH TYR A 206 -35.901 -2.280 7.749 1.00 53.40 O ANISOU 1509 OH TYR A 206 6408 6510 7371 -1425 -342 -676 O ATOM 1510 N TRP A 207 -38.678 -0.915 13.834 1.00 37.14 N ANISOU 1510 N TRP A 207 4555 4429 5128 -1151 -636 -1071 N ATOM 1511 CA TRP A 207 -38.242 0.477 13.815 1.00 25.76 C ANISOU 1511 CA TRP A 207 3156 2869 3762 -1250 -644 -1117 C ATOM 1512 C TRP A 207 -37.071 0.696 14.765 1.00 50.46 C ANISOU 1512 C TRP A 207 6203 6097 6874 -1287 -694 -1223 C ATOM 1513 O TRP A 207 -36.083 1.351 14.407 1.00 46.44 O ANISOU 1513 O TRP A 207 5657 5556 6434 -1392 -694 -1234 O ATOM 1514 CB TRP A 207 -39.410 1.393 14.173 1.00 26.03 C ANISOU 1514 CB TRP A 207 3317 2762 3812 -1222 -644 -1154 C ATOM 1515 CG TRP A 207 -39.147 2.833 13.878 1.00 41.00 C ANISOU 1515 CG TRP A 207 5281 4496 5799 -1324 -647 -1171 C ATOM 1516 CD1 TRP A 207 -39.354 3.478 12.692 1.00 43.09 C ANISOU 1516 CD1 TRP A 207 5614 4607 6150 -1387 -619 -1070 C ATOM 1517 CD2 TRP A 207 -38.631 3.814 14.783 1.00 46.41 C ANISOU 1517 CD2 TRP A 207 5977 5154 6501 -1373 -688 -1292 C ATOM 1518 NE1 TRP A 207 -38.998 4.799 12.803 1.00 52.35 N ANISOU 1518 NE1 TRP A 207 6843 5653 7394 -1474 -641 -1116 N ATOM 1519 CE2 TRP A 207 -38.548 5.032 14.077 1.00 56.80 C ANISOU 1519 CE2 TRP A 207 7373 6290 7918 -1470 -680 -1258 C ATOM 1520 CE3 TRP A 207 -38.227 3.782 16.121 1.00 47.81 C ANISOU 1520 CE3 TRP A 207 6107 5442 6615 -1344 -735 -1423 C ATOM 1521 CZ2 TRP A 207 -38.080 6.206 14.664 1.00 54.81 C ANISOU 1521 CZ2 TRP A 207 7155 5958 7711 -1544 -714 -1358 C ATOM 1522 CZ3 TRP A 207 -37.762 4.948 16.703 1.00 50.36 C ANISOU 1522 CZ3 TRP A 207 6461 5693 6979 -1416 -768 -1525 C ATOM 1523 CH2 TRP A 207 -37.693 6.144 15.974 1.00 51.23 C ANISOU 1523 CH2 TRP A 207 6651 5616 7197 -1517 -756 -1496 C ATOM 1524 N HIS A 208 -37.156 0.141 15.977 1.00 44.73 N ANISOU 1524 N HIS A 208 5444 5497 6055 -1202 -741 -1298 N ATOM 1525 CA HIS A 208 -36.037 0.250 16.907 1.00 46.95 C ANISOU 1525 CA HIS A 208 5643 5886 6311 -1228 -798 -1392 C ATOM 1526 C HIS A 208 -34.854 -0.607 16.477 1.00 43.67 C ANISOU 1526 C HIS A 208 5096 5594 5904 -1248 -800 -1351 C ATOM 1527 O HIS A 208 -33.705 -0.273 16.791 1.00 43.62 O ANISOU 1527 O HIS A 208 5012 5639 5923 -1314 -833 -1412 O ATOM 1528 CB HIS A 208 -36.481 -0.131 18.315 1.00 54.73 C ANISOU 1528 CB HIS A 208 6635 6977 7183 -1125 -851 -1470 C ATOM 1529 CG HIS A 208 -37.232 0.951 19.020 1.00 58.53 C ANISOU 1529 CG HIS A 208 7218 7359 7662 -1124 -858 -1562 C ATOM 1530 ND1 HIS A 208 -38.431 1.447 18.557 1.00 57.51 N ANISOU 1530 ND1 HIS A 208 7196 7084 7570 -1104 -810 -1535 N ATOM 1531 CD2 HIS A 208 -36.952 1.638 20.153 1.00 61.73 C ANISOU 1531 CD2 HIS A 208 7633 7787 8033 -1136 -907 -1686 C ATOM 1532 CE1 HIS A 208 -38.860 2.389 19.377 1.00 61.27 C ANISOU 1532 CE1 HIS A 208 7743 7497 8041 -1098 -825 -1642 C ATOM 1533 NE2 HIS A 208 -37.981 2.524 20.353 1.00 64.47 N ANISOU 1533 NE2 HIS A 208 8093 8003 8399 -1120 -882 -1737 N ATOM 1534 N ILE A 209 -35.107 -1.711 15.772 1.00 46.03 N ANISOU 1534 N ILE A 209 5366 5941 6183 -1192 -764 -1256 N ATOM 1535 CA ILE A 209 -34.015 -2.501 15.213 1.00 38.56 C ANISOU 1535 CA ILE A 209 4298 5096 5257 -1209 -751 -1219 C ATOM 1536 C ILE A 209 -33.221 -1.667 14.214 1.00 50.84 C ANISOU 1536 C ILE A 209 5830 6571 6916 -1342 -703 -1204 C ATOM 1537 O ILE A 209 -31.987 -1.746 14.155 1.00 48.87 O ANISOU 1537 O ILE A 209 5470 6401 6698 -1394 -709 -1235 O ATOM 1538 CB ILE A 209 -34.566 -3.792 14.576 1.00 29.26 C ANISOU 1538 CB ILE A 209 3111 3965 4043 -1123 -715 -1123 C ATOM 1539 CG1 ILE A 209 -35.110 -4.733 15.654 1.00 24.58 C ANISOU 1539 CG1 ILE A 209 2518 3478 3344 -993 -772 -1133 C ATOM 1540 CG2 ILE A 209 -33.500 -4.492 13.759 1.00 25.37 C ANISOU 1540 CG2 ILE A 209 2503 3548 3587 -1149 -682 -1086 C ATOM 1541 CD1 ILE A 209 -35.936 -5.885 15.110 1.00 22.87 C ANISOU 1541 CD1 ILE A 209 2320 3280 3092 -908 -742 -1040 C ATOM 1542 N SER A 210 -33.913 -0.839 13.427 1.00 53.89 N ANISOU 1542 N SER A 210 6319 6797 7358 -1399 -656 -1154 N ATOM 1543 CA SER A 210 -33.228 0.000 12.451 1.00 55.97 C ANISOU 1543 CA SER A 210 6574 6975 7718 -1527 -610 -1125 C ATOM 1544 C SER A 210 -32.554 1.200 13.108 1.00 59.68 C ANISOU 1544 C SER A 210 7042 7399 8236 -1619 -655 -1220 C ATOM 1545 O SER A 210 -31.440 1.571 12.724 1.00 68.18 O ANISOU 1545 O SER A 210 8039 8492 9373 -1720 -640 -1234 O ATOM 1546 CB SER A 210 -34.209 0.472 11.377 1.00 49.46 C ANISOU 1546 CB SER A 210 5865 5990 6937 -1547 -555 -1024 C ATOM 1547 OG SER A 210 -34.675 -0.613 10.598 1.00 51.71 O ANISOU 1547 OG SER A 210 6142 6321 7186 -1483 -506 -934 O ATOM 1548 N ARG A 211 -33.211 1.823 14.090 1.00 54.09 N ANISOU 1548 N ARG A 211 6418 6633 7502 -1590 -707 -1293 N ATOM 1549 CA ARG A 211 -32.628 3.005 14.719 1.00 58.97 C ANISOU 1549 CA ARG A 211 7045 7195 8166 -1681 -752 -1392 C ATOM 1550 C ARG A 211 -31.418 2.645 15.573 1.00 71.35 C ANISOU 1550 C ARG A 211 8479 8926 9703 -1691 -806 -1483 C ATOM 1551 O ARG A 211 -30.422 3.378 15.583 1.00 76.62 O ANISOU 1551 O ARG A 211 9095 9582 10437 -1803 -822 -1535 O ATOM 1552 CB ARG A 211 -33.676 3.734 15.558 1.00 65.49 C ANISOU 1552 CB ARG A 211 7996 7920 8965 -1638 -786 -1457 C ATOM 1553 CG ARG A 211 -34.801 4.357 14.751 1.00 67.93 C ANISOU 1553 CG ARG A 211 8443 8043 9326 -1641 -744 -1378 C ATOM 1554 CD ARG A 211 -34.265 5.170 13.584 1.00 65.45 C ANISOU 1554 CD ARG A 211 8140 7602 9126 -1769 -711 -1305 C ATOM 1555 NE ARG A 211 -34.359 4.434 12.327 1.00 60.61 N ANISOU 1555 NE ARG A 211 7498 7005 8526 -1759 -647 -1171 N ATOM 1556 CZ ARG A 211 -35.369 4.547 11.471 1.00 58.44 C ANISOU 1556 CZ ARG A 211 7317 6608 8278 -1729 -613 -1068 C ATOM 1557 NH1 ARG A 211 -35.378 3.838 10.352 1.00 57.25 N ANISOU 1557 NH1 ARG A 211 7130 6489 8133 -1720 -552 -957 N ATOM 1558 NH2 ARG A 211 -36.370 5.376 11.730 1.00 59.88 N ANISOU 1558 NH2 ARG A 211 7631 6641 8481 -1706 -637 -1080 N ATOM 1559 N ALA A 212 -31.481 1.524 16.296 1.00 74.25 N ANISOU 1559 N ALA A 212 8791 9447 9975 -1576 -841 -1500 N ATOM 1560 CA ALA A 212 -30.373 1.153 17.171 1.00 80.46 C ANISOU 1560 CA ALA A 212 9453 10389 10728 -1571 -906 -1581 C ATOM 1561 C ALA A 212 -29.153 0.683 16.385 1.00 80.44 C ANISOU 1561 C ALA A 212 9312 10468 10782 -1627 -875 -1546 C ATOM 1562 O ALA A 212 -28.024 0.792 16.876 1.00 85.97 O ANISOU 1562 O ALA A 212 9907 11260 11500 -1673 -923 -1620 O ATOM 1563 CB ALA A 212 -30.818 0.071 18.156 1.00 77.11 C ANISOU 1563 CB ALA A 212 9016 10098 10182 -1425 -958 -1592 C ATOM 1564 N SER A 213 -29.355 0.161 15.177 1.00 74.05 N ANISOU 1564 N SER A 213 8501 9633 10001 -1623 -796 -1442 N ATOM 1565 CA SER A 213 -28.273 -0.344 14.340 1.00 74.75 C ANISOU 1565 CA SER A 213 8462 9803 10138 -1669 -749 -1410 C ATOM 1566 C SER A 213 -27.738 0.703 13.368 1.00 79.50 C ANISOU 1566 C SER A 213 9064 10298 10842 -1823 -687 -1391 C ATOM 1567 O SER A 213 -27.057 0.345 12.403 1.00 73.14 O ANISOU 1567 O SER A 213 8176 9536 10076 -1867 -618 -1345 O ATOM 1568 CB SER A 213 -28.753 -1.578 13.564 1.00 77.50 C ANISOU 1568 CB SER A 213 8802 10195 10450 -1576 -692 -1313 C ATOM 1569 OG SER A 213 -30.057 -1.359 13.040 1.00 78.84 O ANISOU 1569 OG SER A 213 9111 10234 10609 -1556 -651 -1239 O ATOM 1570 N LYS A 214 -28.014 1.984 13.608 1.00 87.68 N ANISOU 1570 N LYS A 214 10194 11198 11924 -1906 -708 -1426 N ATOM 1571 CA LYS A 214 -27.803 3.001 12.586 1.00 95.09 C ANISOU 1571 CA LYS A 214 11170 12000 12960 -2043 -647 -1377 C ATOM 1572 C LYS A 214 -26.529 3.813 12.790 1.00100.52 C ANISOU 1572 C LYS A 214 11767 12704 13723 -2179 -669 -1455 C ATOM 1573 O LYS A 214 -25.951 4.297 11.810 1.00105.95 O ANISOU 1573 O LYS A 214 12426 13343 14489 -2296 -603 -1408 O ATOM 1574 CB LYS A 214 -29.014 3.940 12.540 1.00 91.74 C ANISOU 1574 CB LYS A 214 10920 11383 12554 -2048 -653 -1347 C ATOM 1575 CG LYS A 214 -28.984 4.945 11.398 1.00 91.93 C ANISOU 1575 CG LYS A 214 11004 11246 12679 -2172 -595 -1268 C ATOM 1576 CD LYS A 214 -29.442 6.321 11.862 1.00 93.25 C ANISOU 1576 CD LYS A 214 11292 11235 12902 -2231 -646 -1313 C ATOM 1577 CE LYS A 214 -29.071 7.406 10.855 1.00 86.71 C ANISOU 1577 CE LYS A 214 10495 10258 12191 -2377 -604 -1248 C ATOM 1578 NZ LYS A 214 -29.193 8.797 11.382 1.00 82.48 N ANISOU 1578 NZ LYS A 214 10054 9556 11728 -2458 -665 -1311 N ATOM 1579 N SER A 215 -26.058 3.950 14.024 1.00101.42 N ANISOU 1579 N SER A 215 11831 12892 13812 -2170 -758 -1573 N ATOM 1580 CA SER A 215 -25.160 5.044 14.355 1.00101.55 C ANISOU 1580 CA SER A 215 11809 12871 13905 -2309 -794 -1658 C ATOM 1581 C SER A 215 -23.705 4.742 13.989 1.00 98.04 C ANISOU 1581 C SER A 215 11184 12557 13510 -2388 -770 -1679 C ATOM 1582 O SER A 215 -23.339 3.635 13.578 1.00 88.44 O ANISOU 1582 O SER A 215 9867 11473 12263 -2322 -731 -1640 O ATOM 1583 CB SER A 215 -25.278 5.389 15.839 1.00104.67 C ANISOU 1583 CB SER A 215 12231 13289 14249 -2273 -902 -1783 C ATOM 1584 OG SER A 215 -24.989 4.268 16.653 1.00105.79 O ANISOU 1584 OG SER A 215 12276 13618 14300 -2156 -955 -1825 O ATOM 1585 N ARG A 216 -22.884 5.789 14.111 1.00 99.54 N ANISOU 1585 N ARG A 216 11337 12700 13784 -2536 -792 -1743 N ATOM 1586 CA ARG A 216 -21.430 5.741 14.001 1.00 99.98 C ANISOU 1586 CA ARG A 216 11216 12876 13897 -2630 -787 -1794 C ATOM 1587 C ARG A 216 -20.948 5.486 12.581 1.00 94.92 C ANISOU 1587 C ARG A 216 10508 12247 13309 -2697 -666 -1698 C ATOM 1588 O ARG A 216 -21.508 6.018 11.616 1.00100.68 O ANISOU 1588 O ARG A 216 11344 12833 14078 -2754 -592 -1602 O ATOM 1589 CB ARG A 216 -20.852 4.696 14.959 1.00 98.30 C ANISOU 1589 CB ARG A 216 10869 12868 13613 -2520 -862 -1872 C ATOM 1590 CG ARG A 216 -20.930 5.133 16.407 1.00101.17 C ANISOU 1590 CG ARG A 216 11263 13243 13933 -2499 -985 -1990 C ATOM 1591 CD ARG A 216 -20.099 4.250 17.310 1.00107.59 C ANISOU 1591 CD ARG A 216 11924 14262 14693 -2420 -1068 -2066 C ATOM 1592 NE ARG A 216 -20.315 4.588 18.712 1.00110.34 N ANISOU 1592 NE ARG A 216 12320 14629 14976 -2384 -1185 -2171 N ATOM 1593 CZ ARG A 216 -19.741 3.954 19.725 1.00112.07 C ANISOU 1593 CZ ARG A 216 12436 15014 15131 -2310 -1283 -2242 C ATOM 1594 NH1 ARG A 216 -18.910 2.949 19.490 1.00113.37 N ANISOU 1594 NH1 ARG A 216 12442 15332 15300 -2259 -1282 -2220 N ATOM 1595 NH2 ARG A 216 -19.998 4.323 20.970 1.00113.67 N ANISOU 1595 NH2 ARG A 216 12696 15228 15265 -2284 -1384 -2335 N ATOM 1596 N ILE A 217 -19.886 4.692 12.461 1.00149.67 N ANISOU 1596 N ILE A 217 16749 28962 11157 -2059 168 -1075 N ATOM 1597 CA ILE A 217 -19.273 4.465 11.161 1.00136.89 C ANISOU 1597 CA ILE A 217 15101 26937 9973 -2056 -32 -998 C ATOM 1598 C ILE A 217 -20.278 3.844 10.206 1.00132.60 C ANISOU 1598 C ILE A 217 14353 26399 9631 -2182 161 -761 C ATOM 1599 O ILE A 217 -20.387 4.263 9.050 1.00131.68 O ANISOU 1599 O ILE A 217 14102 26057 9874 -2088 174 -939 O ATOM 1600 CB ILE A 217 -18.022 3.586 11.315 1.00135.13 C ANISOU 1600 CB ILE A 217 15112 26473 9757 -2159 -394 -667 C ATOM 1601 CG1 ILE A 217 -17.138 4.123 12.436 1.00141.89 C ANISOU 1601 CG1 ILE A 217 16184 27364 10362 -2050 -568 -872 C ATOM 1602 CG2 ILE A 217 -17.248 3.544 10.023 1.00124.91 C ANISOU 1602 CG2 ILE A 217 13784 24738 8938 -2104 -623 -676 C ATOM 1603 CD1 ILE A 217 -16.132 3.125 12.908 1.00142.84 C ANISOU 1603 CD1 ILE A 217 16548 27332 10392 -2173 -888 -509 C ATOM 1604 N ALA A1001 -21.055 2.868 10.687 1.00133.79 N ANISOU 1604 N ALA A1001 14481 26796 9559 -2400 312 -362 N ATOM 1605 CA ALA A1001 -21.995 2.127 9.849 1.00127.78 C ANISOU 1605 CA ALA A1001 13541 26012 8999 -2548 465 -65 C ATOM 1606 C ALA A1001 -22.792 3.036 8.916 1.00131.47 C ANISOU 1606 C ALA A1001 13765 26425 9764 -2380 686 -443 C ATOM 1607 O ALA A1001 -22.815 2.828 7.697 1.00125.29 O ANISOU 1607 O ALA A1001 12900 25374 9329 -2381 641 -370 O ATOM 1608 CB ALA A1001 -22.941 1.309 10.736 1.00124.00 C ANISOU 1608 CB ALA A1001 13032 25865 8217 -2769 663 287 C ATOM 1609 N ASP A1002 -23.442 4.057 9.482 1.00133.42 N ANISOU 1609 N ASP A1002 13904 26904 9887 -2222 907 -856 N ATOM 1610 CA ASP A1002 -24.121 5.067 8.674 1.00138.07 C ANISOU 1610 CA ASP A1002 14285 27390 10786 -2023 1066 -1282 C ATOM 1611 C ASP A1002 -23.169 5.683 7.656 1.00136.84 C ANISOU 1611 C ASP A1002 14187 26845 10963 -1870 837 -1532 C ATOM 1612 O ASP A1002 -23.477 5.769 6.461 1.00140.78 O ANISOU 1612 O ASP A1002 14564 27107 11819 -1833 872 -1582 O ATOM 1613 CB ASP A1002 -24.694 6.155 9.586 1.00142.15 C ANISOU 1613 CB ASP A1002 14729 28177 11104 -1842 1240 -1726 C ATOM 1614 CG ASP A1002 -25.626 7.112 8.858 1.00143.36 C ANISOU 1614 CG ASP A1002 14652 28234 11582 -1649 1405 -2136 C ATOM 1615 OD1 ASP A1002 -26.242 7.958 9.539 1.00147.81 O ANISOU 1615 OD1 ASP A1002 15130 29014 12017 -1498 1545 -2489 O ATOM 1616 OD2 ASP A1002 -25.764 7.012 7.620 1.00141.06 O ANISOU 1616 OD2 ASP A1002 14274 27646 11679 -1643 1385 -2106 O ATOM 1617 N LEU A1003 -22.002 6.124 8.126 1.00133.56 N ANISOU 1617 N LEU A1003 13960 26336 10449 -1782 593 -1689 N ATOM 1618 CA LEU A1003 -21.024 6.770 7.259 1.00123.25 C ANISOU 1618 CA LEU A1003 12715 24638 9475 -1643 347 -1937 C ATOM 1619 C LEU A1003 -20.304 5.752 6.380 1.00115.76 C ANISOU 1619 C LEU A1003 11843 23417 8725 -1787 122 -1550 C ATOM 1620 O LEU A1003 -19.986 6.040 5.221 1.00114.69 O ANISOU 1620 O LEU A1003 11665 22877 9036 -1706 11 -1653 O ATOM 1621 CB LEU A1003 -20.039 7.551 8.124 1.00124.31 C ANISOU 1621 CB LEU A1003 13017 24736 9480 -1508 153 -2206 C ATOM 1622 CG LEU A1003 -18.951 8.443 7.546 1.00116.22 C ANISOU 1622 CG LEU A1003 12065 23303 8790 -1349 -113 -2509 C ATOM 1623 CD1 LEU A1003 -19.470 9.384 6.466 1.00101.04 C ANISOU 1623 CD1 LEU A1003 9982 21155 7253 -1205 -35 -2860 C ATOM 1624 CD2 LEU A1003 -18.392 9.229 8.716 1.00118.18 C ANISOU 1624 CD2 LEU A1003 12450 23637 8815 -1219 -212 -2770 C ATOM 1625 N GLU A1004 -20.050 4.552 6.912 1.00117.43 N ANISOU 1625 N GLU A1004 12169 23731 8719 -1984 32 -1079 N ATOM 1626 CA GLU A1004 -19.406 3.472 6.172 1.00110.12 C ANISOU 1626 CA GLU A1004 11314 22508 8019 -2110 -218 -672 C ATOM 1627 C GLU A1004 -20.315 2.855 5.118 1.00104.76 C ANISOU 1627 C GLU A1004 10477 21602 7726 -2173 -72 -426 C ATOM 1628 O GLU A1004 -19.832 2.076 4.293 1.00104.23 O ANISOU 1628 O GLU A1004 10444 21144 8013 -2216 -279 -146 O ATOM 1629 CB GLU A1004 -18.935 2.397 7.155 1.00120.01 C ANISOU 1629 CB GLU A1004 12748 23878 8972 -2286 -376 -251 C ATOM 1630 CG GLU A1004 -17.997 1.345 6.593 1.00128.08 C ANISOU 1630 CG GLU A1004 13881 24542 10242 -2372 -724 118 C ATOM 1631 CD GLU A1004 -17.734 0.233 7.587 1.00139.61 C ANISOU 1631 CD GLU A1004 15521 26089 11437 -2552 -861 546 C ATOM 1632 OE1 GLU A1004 -17.966 0.453 8.796 1.00145.57 O ANISOU 1632 OE1 GLU A1004 16353 27159 11799 -2584 -737 494 O ATOM 1633 OE2 GLU A1004 -17.305 -0.861 7.163 1.00140.55 O ANISOU 1633 OE2 GLU A1004 15708 25936 11759 -2653 -1106 925 O ATOM 1634 N ASP A1005 -21.612 3.177 5.123 1.00105.17 N ANISOU 1634 N ASP A1005 10348 21886 7726 -2168 264 -539 N ATOM 1635 CA ASP A1005 -22.496 2.693 4.066 1.00106.07 C ANISOU 1635 CA ASP A1005 10302 21751 8251 -2207 386 -349 C ATOM 1636 C ASP A1005 -21.972 3.090 2.692 1.00102.07 C ANISOU 1636 C ASP A1005 9785 20675 8323 -2048 219 -513 C ATOM 1637 O ASP A1005 -22.185 2.374 1.707 1.00 96.95 O ANISOU 1637 O ASP A1005 9093 19691 8051 -2090 163 -251 O ATOM 1638 CB ASP A1005 -23.914 3.227 4.270 1.00105.89 C ANISOU 1638 CB ASP A1005 10058 22058 8117 -2181 766 -558 C ATOM 1639 CG ASP A1005 -24.661 2.494 5.367 1.00112.13 C ANISOU 1639 CG ASP A1005 10809 23387 8408 -2402 976 -251 C ATOM 1640 OD1 ASP A1005 -24.303 1.335 5.668 1.00113.95 O ANISOU 1640 OD1 ASP A1005 11167 23626 8501 -2614 820 236 O ATOM 1641 OD2 ASP A1005 -25.613 3.079 5.925 1.00116.37 O ANISOU 1641 OD2 ASP A1005 11209 24158 8849 -2332 1220 -496 O ATOM 1642 N ASN A1006 -21.270 4.225 2.615 1.00 96.79 N ANISOU 1642 N ASN A1006 9163 19891 7722 -1870 126 -941 N ATOM 1643 CA ASN A1006 -20.591 4.672 1.403 1.00 83.80 C ANISOU 1643 CA ASN A1006 7533 17736 6572 -1741 -49 -1096 C ATOM 1644 C ASN A1006 -19.723 3.562 0.830 1.00 74.34 C ANISOU 1644 C ASN A1006 6431 16222 5593 -1827 -310 -707 C ATOM 1645 O ASN A1006 -19.540 3.457 -0.388 1.00 75.70 O ANISOU 1645 O ASN A1006 6576 15979 6209 -1770 -392 -674 O ATOM 1646 CB ASN A1006 -19.724 5.898 1.698 1.00 83.63 C ANISOU 1646 CB ASN A1006 7583 17695 6498 -1595 -172 -1533 C ATOM 1647 CG ASN A1006 -20.515 7.045 2.291 1.00 92.59 C ANISOU 1647 CG ASN A1006 8632 19127 7420 -1478 41 -1967 C ATOM 1648 OD1 ASN A1006 -21.546 7.448 1.752 1.00 97.37 O ANISOU 1648 OD1 ASN A1006 9092 19685 8219 -1410 235 -2119 O ATOM 1649 ND2 ASN A1006 -20.037 7.576 3.410 1.00 98.40 N ANISOU 1649 ND2 ASN A1006 9458 20169 7760 -1439 -15 -2186 N ATOM 1650 N TRP A1007 -19.183 2.728 1.715 1.00 73.13 N ANISOU 1650 N TRP A1007 6398 16270 5120 -1957 -454 -421 N ATOM 1651 CA TRP A1007 -18.283 1.668 1.291 1.00 78.21 C ANISOU 1651 CA TRP A1007 7136 16628 5951 -2020 -745 -80 C ATOM 1652 C TRP A1007 -19.042 0.540 0.599 1.00 80.45 C ANISOU 1652 C TRP A1007 7359 16747 6461 -2122 -714 314 C ATOM 1653 O TRP A1007 -18.631 0.066 -0.468 1.00 80.81 O ANISOU 1653 O TRP A1007 7404 16392 6908 -2074 -878 429 O ATOM 1654 CB TRP A1007 -17.500 1.154 2.497 1.00 88.26 C ANISOU 1654 CB TRP A1007 8569 18155 6810 -2123 -944 92 C ATOM 1655 CG TRP A1007 -16.319 0.377 2.115 1.00 93.76 C ANISOU 1655 CG TRP A1007 9361 18544 7719 -2128 -1294 299 C ATOM 1656 CD1 TRP A1007 -15.106 0.863 1.730 1.00 95.14 C ANISOU 1656 CD1 TRP A1007 9563 18476 8110 -2005 -1506 75 C ATOM 1657 CD2 TRP A1007 -16.220 -1.044 2.070 1.00100.05 C ANISOU 1657 CD2 TRP A1007 10225 19238 8552 -2260 -1492 766 C ATOM 1658 NE1 TRP A1007 -14.253 -0.173 1.449 1.00 97.10 N ANISOU 1658 NE1 TRP A1007 9902 18413 8579 -2013 -1766 353 N ATOM 1659 CE2 TRP A1007 -14.917 -1.355 1.650 1.00 97.50 C ANISOU 1659 CE2 TRP A1007 9976 18565 8504 -2171 -1798 771 C ATOM 1660 CE3 TRP A1007 -17.108 -2.088 2.345 1.00107.71 C ANISOU 1660 CE3 TRP A1007 11203 20338 9385 -2441 -1435 1180 C ATOM 1661 CZ2 TRP A1007 -14.482 -2.661 1.498 1.00 94.57 C ANISOU 1661 CZ2 TRP A1007 9711 17908 8313 -2212 -2029 1133 C ATOM 1662 CZ3 TRP A1007 -16.669 -3.388 2.191 1.00106.22 C ANISOU 1662 CZ3 TRP A1007 11105 19944 9311 -2534 -1740 1584 C ATOM 1663 CH2 TRP A1007 -15.367 -3.662 1.773 1.00 97.90 C ANISOU 1663 CH2 TRP A1007 10146 18476 8578 -2397 -2022 1535 C ATOM 1664 N GLU A1008 -20.157 0.100 1.187 1.00 83.63 N ANISOU 1664 N GLU A1008 7702 17461 6613 -2263 -507 519 N ATOM 1665 CA GLU A1008 -21.030 -0.824 0.473 1.00 89.37 C ANISOU 1665 CA GLU A1008 8341 18018 7597 -2355 -458 852 C ATOM 1666 C GLU A1008 -21.603 -0.190 -0.786 1.00 72.79 C ANISOU 1666 C GLU A1008 6105 15606 5945 -2203 -326 608 C ATOM 1667 O GLU A1008 -21.960 -0.910 -1.724 1.00 68.12 O ANISOU 1667 O GLU A1008 5473 14709 5700 -2219 -387 835 O ATOM 1668 CB GLU A1008 -22.163 -1.306 1.382 1.00103.93 C ANISOU 1668 CB GLU A1008 10116 20294 9080 -2555 -230 1101 C ATOM 1669 CG GLU A1008 -21.722 -2.277 2.468 1.00120.33 C ANISOU 1669 CG GLU A1008 12352 22616 10754 -2762 -403 1492 C ATOM 1670 CD GLU A1008 -22.869 -2.713 3.364 1.00138.09 C ANISOU 1670 CD GLU A1008 14523 25325 12618 -2988 -147 1751 C ATOM 1671 OE1 GLU A1008 -23.998 -2.209 3.176 1.00142.17 O ANISOU 1671 OE1 GLU A1008 14838 25994 13185 -2966 179 1588 O ATOM 1672 OE2 GLU A1008 -22.643 -3.558 4.257 1.00144.22 O ANISOU 1672 OE2 GLU A1008 15437 26316 13044 -3195 -277 2120 O ATOM 1673 N THR A1009 -21.685 1.141 -0.828 1.00 69.88 N ANISOU 1673 N THR A1009 5680 15291 5581 -2051 -175 147 N ATOM 1674 CA THR A1009 -22.134 1.831 -2.031 1.00 68.29 C ANISOU 1674 CA THR A1009 5381 14763 5804 -1903 -91 -104 C ATOM 1675 C THR A1009 -21.126 1.664 -3.161 1.00 60.88 C ANISOU 1675 C THR A1009 4528 13351 5253 -1815 -342 -82 C ATOM 1676 O THR A1009 -21.486 1.263 -4.274 1.00 58.36 O ANISOU 1676 O THR A1009 4171 12701 5301 -1783 -368 35 O ATOM 1677 CB THR A1009 -22.367 3.313 -1.728 1.00 65.48 C ANISOU 1677 CB THR A1009 4967 14565 5348 -1765 75 -608 C ATOM 1678 OG1 THR A1009 -23.439 3.451 -0.787 1.00 69.15 O ANISOU 1678 OG1 THR A1009 5314 15483 5476 -1826 341 -655 O ATOM 1679 CG2 THR A1009 -22.702 4.077 -2.998 1.00 69.98 C ANISOU 1679 CG2 THR A1009 5472 14752 6366 -1615 106 -868 C ATOM 1680 N LEU A1010 -19.851 1.960 -2.893 1.00 60.65 N ANISOU 1680 N LEU A1010 4607 13292 5144 -1772 -529 -198 N ATOM 1681 CA LEU A1010 -18.842 1.782 -3.932 1.00 59.38 C ANISOU 1681 CA LEU A1010 4502 12729 5332 -1695 -750 -181 C ATOM 1682 C LEU A1010 -18.633 0.308 -4.264 1.00 57.02 C ANISOU 1682 C LEU A1010 4245 12268 5152 -1772 -941 248 C ATOM 1683 O LEU A1010 -18.225 -0.020 -5.385 1.00 54.15 O ANISOU 1683 O LEU A1010 3888 11546 5139 -1696 -1069 297 O ATOM 1684 CB LEU A1010 -17.527 2.449 -3.516 1.00 57.73 C ANISOU 1684 CB LEU A1010 4368 12548 5020 -1643 -906 -411 C ATOM 1685 CG LEU A1010 -16.863 2.101 -2.182 1.00 71.76 C ANISOU 1685 CG LEU A1010 6236 14636 6393 -1728 -1038 -311 C ATOM 1686 CD1 LEU A1010 -15.963 0.879 -2.310 1.00 69.11 C ANISOU 1686 CD1 LEU A1010 5974 14146 6138 -1778 -1323 19 C ATOM 1687 CD2 LEU A1010 -16.077 3.291 -1.656 1.00 67.79 C ANISOU 1687 CD2 LEU A1010 5766 14231 5758 -1652 -1082 -689 C ATOM 1688 N ASN A1011 -18.918 -0.591 -3.318 1.00 59.76 N ANISOU 1688 N ASN A1011 4626 12871 5208 -1922 -972 561 N ATOM 1689 CA ASN A1011 -18.817 -2.020 -3.606 1.00 63.68 C ANISOU 1689 CA ASN A1011 5169 13194 5831 -2003 -1187 983 C ATOM 1690 C ASN A1011 -19.926 -2.476 -4.545 1.00 71.60 C ANISOU 1690 C ASN A1011 6084 13985 7136 -2006 -1089 1136 C ATOM 1691 O ASN A1011 -19.661 -3.102 -5.580 1.00 71.90 O ANISOU 1691 O ASN A1011 6139 13661 7518 -1937 -1263 1256 O ATOM 1692 CB ASN A1011 -18.853 -2.823 -2.308 1.00 65.59 C ANISOU 1692 CB ASN A1011 5490 13763 5668 -2190 -1266 1297 C ATOM 1693 CG ASN A1011 -17.506 -2.891 -1.634 1.00 78.60 C ANISOU 1693 CG ASN A1011 7267 15471 7128 -2181 -1524 1271 C ATOM 1694 OD1 ASN A1011 -16.754 -3.845 -1.825 1.00 84.97 O ANISOU 1694 OD1 ASN A1011 8150 16075 8058 -2190 -1830 1504 O ATOM 1695 ND2 ASN A1011 -17.186 -1.874 -0.845 1.00 87.54 N ANISOU 1695 ND2 ASN A1011 8418 16867 7976 -2149 -1424 971 N ATOM 1696 N ASP A1012 -21.181 -2.180 -4.194 1.00 73.78 N ANISOU 1696 N ASP A1012 6255 14489 7290 -2079 -816 1121 N ATOM 1697 CA ASP A1012 -22.295 -2.569 -5.051 1.00 76.12 C ANISOU 1697 CA ASP A1012 6450 14587 7885 -2085 -726 1253 C ATOM 1698 C ASP A1012 -22.195 -1.904 -6.416 1.00 68.72 C ANISOU 1698 C ASP A1012 5493 13262 7356 -1891 -723 977 C ATOM 1699 O ASP A1012 -22.532 -2.514 -7.437 1.00 75.71 O ANISOU 1699 O ASP A1012 6368 13820 8576 -1853 -814 1128 O ATOM 1700 CB ASP A1012 -23.628 -2.228 -4.383 1.00 80.11 C ANISOU 1700 CB ASP A1012 6811 15444 8184 -2187 -412 1227 C ATOM 1701 CG ASP A1012 -23.871 -3.032 -3.120 1.00 91.45 C ANISOU 1701 CG ASP A1012 8264 17268 9215 -2417 -398 1572 C ATOM 1702 OD1 ASP A1012 -24.216 -2.427 -2.083 1.00 99.53 O ANISOU 1702 OD1 ASP A1012 9237 18726 9854 -2474 -175 1427 O ATOM 1703 OD2 ASP A1012 -23.705 -4.269 -3.160 1.00 96.40 O ANISOU 1703 OD2 ASP A1012 8962 17765 9899 -2540 -625 1987 O ATOM 1704 N ASN A1013 -21.728 -0.653 -6.458 1.00 71.28 N ANISOU 1704 N ASN A1013 5824 13608 7652 -1774 -638 578 N ATOM 1705 CA ASN A1013 -21.523 0.000 -7.746 1.00 50.37 C ANISOU 1705 CA ASN A1013 3198 10576 5366 -1607 -653 336 C ATOM 1706 C ASN A1013 -20.380 -0.639 -8.522 1.00 48.26 C ANISOU 1706 C ASN A1013 3116 9905 5314 -1505 -884 447 C ATOM 1707 O ASN A1013 -20.415 -0.666 -9.757 1.00 45.68 O ANISOU 1707 O ASN A1013 2886 9148 5322 -1366 -903 402 O ATOM 1708 CB ASN A1013 -21.270 1.493 -7.551 1.00 50.29 C ANISOU 1708 CB ASN A1013 3164 10672 5272 -1526 -534 -99 C ATOM 1709 CG ASN A1013 -22.530 2.252 -7.191 1.00 51.79 C ANISOU 1709 CG ASN A1013 3237 11060 5380 -1521 -278 -301 C ATOM 1710 OD1 ASN A1013 -23.241 2.744 -8.064 1.00 50.23 O ANISOU 1710 OD1 ASN A1013 3012 10614 5457 -1426 -196 -451 O ATOM 1711 ND2 ASN A1013 -22.815 2.349 -5.899 1.00 70.25 N ANISOU 1711 ND2 ASN A1013 5532 13826 7335 -1605 -155 -315 N ATOM 1712 N LEU A1014 -19.362 -1.156 -7.828 1.00 49.50 N ANISOU 1712 N LEU A1014 3329 10194 5284 -1559 -1060 572 N ATOM 1713 CA LEU A1014 -18.330 -1.932 -8.508 1.00 47.99 C ANISOU 1713 CA LEU A1014 3299 9624 5311 -1448 -1269 680 C ATOM 1714 C LEU A1014 -18.925 -3.182 -9.144 1.00 57.93 C ANISOU 1714 C LEU A1014 4604 10626 6782 -1442 -1365 981 C ATOM 1715 O LEU A1014 -18.621 -3.515 -10.298 1.00 52.35 O ANISOU 1715 O LEU A1014 4004 9509 6378 -1284 -1433 943 O ATOM 1716 CB LEU A1014 -17.216 -2.308 -7.530 1.00 49.92 C ANISOU 1716 CB LEU A1014 3600 10045 5322 -1502 -1448 758 C ATOM 1717 CG LEU A1014 -16.019 -1.364 -7.421 1.00 49.47 C ANISOU 1717 CG LEU A1014 3588 9966 5241 -1412 -1463 457 C ATOM 1718 CD1 LEU A1014 -15.026 -1.895 -6.403 1.00 56.14 C ANISOU 1718 CD1 LEU A1014 4500 10957 5873 -1462 -1661 565 C ATOM 1719 CD2 LEU A1014 -15.353 -1.177 -8.776 1.00 46.56 C ANISOU 1719 CD2 LEU A1014 3301 9145 5245 -1232 -1477 308 C ATOM 1720 N LYS A1015 -19.782 -3.886 -8.401 1.00 57.58 N ANISOU 1720 N LYS A1015 4476 10834 6568 -1620 -1374 1277 N ATOM 1721 CA LYS A1015 -20.445 -5.061 -8.957 1.00 61.99 C ANISOU 1721 CA LYS A1015 5079 11137 7338 -1632 -1475 1577 C ATOM 1722 C LYS A1015 -21.315 -4.686 -10.152 1.00 57.25 C ANISOU 1722 C LYS A1015 4470 10236 7047 -1506 -1336 1431 C ATOM 1723 O LYS A1015 -21.385 -5.431 -11.137 1.00 57.98 O ANISOU 1723 O LYS A1015 4675 9939 7414 -1392 -1448 1514 O ATOM 1724 CB LYS A1015 -21.275 -5.755 -7.877 1.00 75.93 C ANISOU 1724 CB LYS A1015 6729 13269 8851 -1891 -1490 1939 C ATOM 1725 CG LYS A1015 -21.726 -7.158 -8.253 1.00 85.37 C ANISOU 1725 CG LYS A1015 8005 14187 10244 -1934 -1675 2312 C ATOM 1726 CD LYS A1015 -20.538 -8.103 -8.378 1.00 87.66 C ANISOU 1726 CD LYS A1015 8506 14183 10619 -1839 -1955 2407 C ATOM 1727 CE LYS A1015 -20.921 -9.377 -9.113 1.00 84.68 C ANISOU 1727 CE LYS A1015 8243 13397 10534 -1800 -2122 2650 C ATOM 1728 NZ LYS A1015 -21.296 -9.100 -10.529 1.00 77.95 N ANISOU 1728 NZ LYS A1015 7426 12179 10011 -1588 -2027 2425 N ATOM 1729 N VAL A1016 -21.982 -3.530 -10.085 1.00 60.02 N ANISOU 1729 N VAL A1016 4703 10751 7352 -1512 -1099 1187 N ATOM 1730 CA VAL A1016 -22.763 -3.050 -11.223 1.00 44.86 C ANISOU 1730 CA VAL A1016 2798 8515 5731 -1379 -986 1011 C ATOM 1731 C VAL A1016 -21.857 -2.812 -12.423 1.00 51.93 C ANISOU 1731 C VAL A1016 3854 9010 6867 -1179 -1075 813 C ATOM 1732 O VAL A1016 -22.209 -3.146 -13.562 1.00 52.96 O ANISOU 1732 O VAL A1016 4069 8790 7262 -1062 -1114 806 O ATOM 1733 CB VAL A1016 -23.542 -1.777 -10.839 1.00 45.53 C ANISOU 1733 CB VAL A1016 2744 8841 5717 -1404 -732 743 C ATOM 1734 CG1 VAL A1016 -24.117 -1.108 -12.075 1.00 43.13 C ANISOU 1734 CG1 VAL A1016 2487 8160 5739 -1245 -662 515 C ATOM 1735 CG2 VAL A1016 -24.648 -2.112 -9.853 1.00 52.92 C ANISOU 1735 CG2 VAL A1016 3505 10149 6451 -1585 -597 930 C ATOM 1736 N ILE A1017 -20.672 -2.244 -12.187 1.00 52.35 N ANISOU 1736 N ILE A1017 3946 9131 6811 -1143 -1104 644 N ATOM 1737 CA ILE A1017 -19.713 -2.032 -13.269 1.00 45.37 C ANISOU 1737 CA ILE A1017 3189 7918 6130 -978 -1171 470 C ATOM 1738 C ILE A1017 -19.291 -3.363 -13.877 1.00 48.97 C ANISOU 1738 C ILE A1017 3759 8132 6716 -892 -1352 644 C ATOM 1739 O ILE A1017 -19.071 -3.466 -15.091 1.00 36.81 O ANISOU 1739 O ILE A1017 2313 6306 5367 -745 -1371 532 O ATOM 1740 CB ILE A1017 -18.503 -1.227 -12.757 1.00 43.79 C ANISOU 1740 CB ILE A1017 2993 7860 5784 -981 -1173 288 C ATOM 1741 CG1 ILE A1017 -18.923 0.203 -12.409 1.00 42.99 C ANISOU 1741 CG1 ILE A1017 2820 7931 5584 -1024 -994 47 C ATOM 1742 CG2 ILE A1017 -17.379 -1.215 -13.782 1.00 37.79 C ANISOU 1742 CG2 ILE A1017 2338 6799 5221 -838 -1255 166 C ATOM 1743 CD1 ILE A1017 -17.848 1.001 -11.720 1.00 40.72 C ANISOU 1743 CD1 ILE A1017 2533 7825 5114 -1047 -1002 -128 C ATOM 1744 N GLU A1018 -19.186 -4.408 -13.049 1.00 50.46 N ANISOU 1744 N GLU A1018 3947 8451 6772 -984 -1487 915 N ATOM 1745 CA GLU A1018 -18.814 -5.722 -13.569 1.00 54.18 C ANISOU 1745 CA GLU A1018 4544 8674 7369 -895 -1671 1073 C ATOM 1746 C GLU A1018 -19.843 -6.246 -14.566 1.00 57.69 C ANISOU 1746 C GLU A1018 5044 8853 8021 -835 -1661 1154 C ATOM 1747 O GLU A1018 -19.480 -6.808 -15.606 1.00 50.53 O ANISOU 1747 O GLU A1018 4265 7674 7261 -682 -1730 1101 O ATOM 1748 CB GLU A1018 -18.631 -6.716 -12.422 1.00 55.98 C ANISOU 1748 CB GLU A1018 4772 9069 7428 -1033 -1836 1373 C ATOM 1749 CG GLU A1018 -17.195 -6.853 -11.948 1.00 66.39 C ANISOU 1749 CG GLU A1018 6141 10436 8648 -984 -1965 1292 C ATOM 1750 CD GLU A1018 -16.997 -8.037 -11.021 1.00 79.24 C ANISOU 1750 CD GLU A1018 7822 12127 10159 -1092 -2171 1592 C ATOM 1751 OE1 GLU A1018 -17.965 -8.427 -10.334 1.00 83.19 O ANISOU 1751 OE1 GLU A1018 8273 12792 10543 -1285 -2179 1884 O ATOM 1752 OE2 GLU A1018 -15.873 -8.584 -10.985 1.00 84.33 O ANISOU 1752 OE2 GLU A1018 8550 12660 10829 -989 -2327 1534 O ATOM 1753 N LYS A1019 -21.132 -6.070 -14.272 1.00 62.37 N ANISOU 1753 N LYS A1019 5540 9543 8615 -953 -1565 1272 N ATOM 1754 CA LYS A1019 -22.205 -6.600 -15.105 1.00 70.75 C ANISOU 1754 CA LYS A1019 6648 10353 9881 -913 -1572 1373 C ATOM 1755 C LYS A1019 -22.848 -5.531 -15.985 1.00 65.42 C ANISOU 1755 C LYS A1019 5957 9568 9331 -824 -1402 1108 C ATOM 1756 O LYS A1019 -24.035 -5.631 -16.315 1.00 71.98 O ANISOU 1756 O LYS A1019 6761 10301 10288 -841 -1356 1174 O ATOM 1757 CB LYS A1019 -23.261 -7.280 -14.234 1.00 73.25 C ANISOU 1757 CB LYS A1019 6860 10828 10145 -1111 -1600 1713 C ATOM 1758 CG LYS A1019 -22.758 -8.522 -13.513 1.00 80.84 C ANISOU 1758 CG LYS A1019 7875 11825 11016 -1215 -1814 2031 C ATOM 1759 CD LYS A1019 -23.858 -9.180 -12.696 1.00 89.31 C ANISOU 1759 CD LYS A1019 8832 13074 12027 -1450 -1843 2409 C ATOM 1760 CE LYS A1019 -24.364 -8.256 -11.600 1.00 94.77 C ANISOU 1760 CE LYS A1019 9303 14255 12449 -1631 -1635 2391 C ATOM 1761 NZ LYS A1019 -25.430 -8.899 -10.781 1.00 99.52 N ANISOU 1761 NZ LYS A1019 9766 15097 12952 -1885 -1629 2765 N ATOM 1762 N ALA A1020 -22.087 -4.517 -16.384 1.00 54.65 N ANISOU 1762 N ALA A1020 4611 8207 7945 -735 -1322 814 N ATOM 1763 CA ALA A1020 -22.641 -3.445 -17.194 1.00 46.57 C ANISOU 1763 CA ALA A1020 3586 7084 7025 -669 -1182 568 C ATOM 1764 C ALA A1020 -22.690 -3.848 -18.666 1.00 50.39 C ANISOU 1764 C ALA A1020 4249 7250 7649 -523 -1232 559 C ATOM 1765 O ALA A1020 -22.134 -4.868 -19.082 1.00 58.52 O ANISOU 1765 O ALA A1020 5397 8133 8706 -453 -1360 683 O ATOM 1766 CB ALA A1020 -21.827 -2.166 -17.019 1.00 33.85 C ANISOU 1766 CB ALA A1020 1927 5593 5342 -664 -1091 290 C ATOM 1767 N ASP A1021 -23.371 -3.021 -19.462 1.00 48.09 N ANISOU 1767 N ASP A1021 3988 6844 7439 -480 -1134 415 N ATOM 1768 CA ASP A1021 -23.529 -3.271 -20.890 1.00 34.93 C ANISOU 1768 CA ASP A1021 2511 4852 5908 -356 -1177 428 C ATOM 1769 C ASP A1021 -23.211 -2.079 -21.778 1.00 27.93 C ANISOU 1769 C ASP A1021 1702 3883 5027 -305 -1093 229 C ATOM 1770 O ASP A1021 -22.924 -2.287 -22.963 1.00 28.29 O ANISOU 1770 O ASP A1021 1911 3676 5161 -206 -1139 228 O ATOM 1771 CB ASP A1021 -24.959 -3.739 -21.198 1.00 29.79 C ANISOU 1771 CB ASP A1021 1883 4007 5428 -356 -1203 554 C ATOM 1772 CG ASP A1021 -25.183 -5.194 -20.844 1.00 44.12 C ANISOU 1772 CG ASP A1021 3711 5755 7298 -389 -1339 820 C ATOM 1773 OD1 ASP A1021 -24.489 -6.059 -21.418 1.00 41.63 O ANISOU 1773 OD1 ASP A1021 3540 5270 7009 -318 -1449 886 O ATOM 1774 OD2 ASP A1021 -26.045 -5.473 -19.984 1.00 47.40 O ANISOU 1774 OD2 ASP A1021 3986 6296 7728 -502 -1333 963 O ATOM 1775 N ASN A1022 -23.251 -0.851 -21.268 1.00 28.17 N ANISOU 1775 N ASN A1022 1628 4101 4976 -381 -983 70 N ATOM 1776 CA ASN A1022 -22.979 0.325 -22.081 1.00 32.70 C ANISOU 1776 CA ASN A1022 2296 4546 5582 -355 -929 -83 C ATOM 1777 C ASN A1022 -22.223 1.354 -21.253 1.00 38.26 C ANISOU 1777 C ASN A1022 2894 5511 6131 -459 -859 -198 C ATOM 1778 O ASN A1022 -22.016 1.190 -20.048 1.00 29.01 O ANISOU 1778 O ASN A1022 1563 4639 4822 -551 -848 -164 O ATOM 1779 CB ASN A1022 -24.271 0.930 -22.645 1.00 29.64 C ANISOU 1779 CB ASN A1022 1964 3934 5363 -320 -901 -152 C ATOM 1780 CG ASN A1022 -25.301 1.207 -21.571 1.00 36.97 C ANISOU 1780 CG ASN A1022 2713 5068 6268 -405 -832 -170 C ATOM 1781 OD1 ASN A1022 -25.198 2.189 -20.835 1.00 52.34 O ANISOU 1781 OD1 ASN A1022 4554 7204 8129 -479 -758 -292 O ATOM 1782 ND2 ASN A1022 -26.307 0.344 -21.478 1.00 28.76 N ANISOU 1782 ND2 ASN A1022 1630 3978 5318 -397 -862 -42 N ATOM 1783 N ALA A1023 -21.812 2.432 -21.923 1.00 37.35 N ANISOU 1783 N ALA A1023 2876 5255 6059 -447 -828 -335 N ATOM 1784 CA ALA A1023 -21.013 3.462 -21.271 1.00 43.28 C ANISOU 1784 CA ALA A1023 3574 6156 6714 -533 -789 -442 C ATOM 1785 C ALA A1023 -21.825 4.308 -20.299 1.00 42.87 C ANISOU 1785 C ALA A1023 3421 6204 6663 -585 -733 -561 C ATOM 1786 O ALA A1023 -21.245 4.901 -19.382 1.00 51.39 O ANISOU 1786 O ALA A1023 4429 7445 7653 -643 -711 -654 O ATOM 1787 CB ALA A1023 -20.356 4.361 -22.319 1.00 42.98 C ANISOU 1787 CB ALA A1023 3673 5925 6733 -507 -777 -578 C ATOM 1788 N ALA A1024 -23.146 4.384 -20.476 1.00 34.79 N ANISOU 1788 N ALA A1024 2389 5081 5750 -547 -706 -600 N ATOM 1789 CA ALA A1024 -23.959 5.172 -19.555 1.00 37.41 C ANISOU 1789 CA ALA A1024 2598 5535 6082 -576 -636 -761 C ATOM 1790 C ALA A1024 -24.082 4.495 -18.196 1.00 41.49 C ANISOU 1790 C ALA A1024 2913 6362 6488 -652 -607 -642 C ATOM 1791 O ALA A1024 -24.172 5.181 -17.169 1.00 33.74 O ANISOU 1791 O ALA A1024 1824 5595 5401 -685 -528 -828 O ATOM 1792 CB ALA A1024 -25.342 5.423 -20.156 1.00 30.19 C ANISOU 1792 CB ALA A1024 1712 4417 5340 -505 -621 -843 C ATOM 1793 N GLN A1025 -24.076 3.160 -18.169 1.00 32.03 N ANISOU 1793 N GLN A1025 1666 5210 5293 -680 -674 -359 N ATOM 1794 CA GLN A1025 -24.153 2.438 -16.903 1.00 33.94 C ANISOU 1794 CA GLN A1025 1728 5663 5504 -749 -669 -255 C ATOM 1795 C GLN A1025 -22.876 2.614 -16.088 1.00 52.08 C ANISOU 1795 C GLN A1025 4031 8162 7596 -786 -674 -341 C ATOM 1796 O GLN A1025 -22.928 2.953 -14.899 1.00 53.63 O ANISOU 1796 O GLN A1025 4123 8693 7562 -856 -583 -443 O ATOM 1797 CB GLN A1025 -24.429 0.958 -17.164 1.00 33.79 C ANISOU 1797 CB GLN A1025 1707 5508 5625 -703 -742 -170 C ATOM 1798 CG GLN A1025 -25.775 0.689 -17.812 1.00 33.53 C ANISOU 1798 CG GLN A1025 1668 5565 5507 -709 -678 -148 C ATOM 1799 CD GLN A1025 -25.944 -0.760 -18.220 1.00 33.31 C ANISOU 1799 CD GLN A1025 1731 5327 5597 -666 -801 96 C ATOM 1800 OE1 GLN A1025 -24.966 -1.481 -18.407 1.00 33.01 O ANISOU 1800 OE1 GLN A1025 1804 5214 5523 -627 -910 210 O ATOM 1801 NE2 GLN A1025 -27.191 -1.196 -18.359 1.00 33.97 N ANISOU 1801 NE2 GLN A1025 1781 5323 5803 -676 -791 205 N ATOM 1802 N VAL A1026 -21.717 2.390 -16.714 1.00 33.32 N ANISOU 1802 N VAL A1026 1770 5627 5261 -748 -780 -285 N ATOM 1803 CA VAL A1026 -20.452 2.576 -16.010 1.00 35.42 C ANISOU 1803 CA VAL A1026 2044 6071 5342 -780 -800 -356 C ATOM 1804 C VAL A1026 -20.211 4.049 -15.710 1.00 43.89 C ANISOU 1804 C VAL A1026 3135 7248 6295 -801 -708 -621 C ATOM 1805 O VAL A1026 -19.495 4.386 -14.759 1.00 56.34 O ANISOU 1805 O VAL A1026 4670 9061 7676 -850 -700 -720 O ATOM 1806 CB VAL A1026 -19.287 1.970 -16.815 1.00 36.97 C ANISOU 1806 CB VAL A1026 2338 6063 5646 -720 -927 -256 C ATOM 1807 CG1 VAL A1026 -19.427 0.461 -16.897 1.00 36.48 C ANISOU 1807 CG1 VAL A1026 2259 5946 5658 -658 -1025 -154 C ATOM 1808 CG2 VAL A1026 -19.226 2.578 -18.203 1.00 39.06 C ANISOU 1808 CG2 VAL A1026 2730 6132 5980 -692 -904 -249 C ATOM 1809 N LYS A1027 -20.786 4.947 -16.512 1.00 33.53 N ANISOU 1809 N LYS A1027 1892 5751 5097 -761 -659 -756 N ATOM 1810 CA LYS A1027 -20.716 6.372 -16.204 1.00 34.25 C ANISOU 1810 CA LYS A1027 1997 5900 5118 -769 -598 -1051 C ATOM 1811 C LYS A1027 -21.484 6.689 -14.926 1.00 42.59 C ANISOU 1811 C LYS A1027 2894 7274 6013 -803 -507 -1211 C ATOM 1812 O LYS A1027 -20.961 7.351 -14.019 1.00 37.95 O ANISOU 1812 O LYS A1027 2259 6916 5244 -838 -491 -1395 O ATOM 1813 CB LYS A1027 -21.261 7.184 -17.379 1.00 32.98 C ANISOU 1813 CB LYS A1027 1956 5442 5132 -713 -592 -1164 C ATOM 1814 CG LYS A1027 -21.666 8.611 -17.034 1.00 34.10 C ANISOU 1814 CG LYS A1027 2088 5603 5266 -701 -550 -1488 C ATOM 1815 CD LYS A1027 -20.522 9.589 -17.224 1.00 46.03 C ANISOU 1815 CD LYS A1027 3699 7041 6751 -729 -594 -1609 C ATOM 1816 CE LYS A1027 -20.993 11.025 -17.039 1.00 50.74 C ANISOU 1816 CE LYS A1027 4307 7583 7387 -701 -593 -1919 C ATOM 1817 NZ LYS A1027 -19.911 12.015 -17.309 1.00 59.03 N ANISOU 1817 NZ LYS A1027 5468 8522 8440 -741 -655 -1990 N ATOM 1818 N ASP A1028 -22.727 6.210 -14.835 1.00 41.37 N ANISOU 1818 N ASP A1028 2646 7162 5912 -794 -446 -1144 N ATOM 1819 CA ASP A1028 -23.546 6.474 -13.656 1.00 39.42 C ANISOU 1819 CA ASP A1028 2222 7268 5489 -830 -327 -1293 C ATOM 1820 C ASP A1028 -22.935 5.844 -12.409 1.00 43.38 C ANISOU 1820 C ASP A1028 2624 8165 5695 -928 -318 -1188 C ATOM 1821 O ASP A1028 -22.710 6.525 -11.398 1.00 52.15 O ANISOU 1821 O ASP A1028 3650 9596 6569 -961 -269 -1406 O ATOM 1822 CB ASP A1028 -24.964 5.954 -13.890 1.00 45.60 C ANISOU 1822 CB ASP A1028 2916 8002 6409 -812 -257 -1189 C ATOM 1823 CG ASP A1028 -25.925 6.371 -12.800 1.00 57.22 C ANISOU 1823 CG ASP A1028 4193 9837 7712 -834 -100 -1378 C ATOM 1824 OD1 ASP A1028 -26.052 7.590 -12.558 1.00 67.93 O ANISOU 1824 OD1 ASP A1028 5526 11254 9032 -779 -62 -1729 O ATOM 1825 OD2 ASP A1028 -26.560 5.482 -12.193 1.00 66.63 O ANISOU 1825 OD2 ASP A1028 5251 11257 8808 -908 -18 -1179 O ATOM 1826 N ALA A1029 -22.652 4.538 -12.465 1.00 41.95 N ANISOU 1826 N ALA A1029 2453 7968 5517 -975 -390 -862 N ATOM 1827 CA ALA A1029 -22.059 3.861 -11.317 1.00 44.92 C ANISOU 1827 CA ALA A1029 2758 8708 5604 -1080 -419 -722 C ATOM 1828 C ALA A1029 -20.702 4.451 -10.960 1.00 42.72 C ANISOU 1828 C ALA A1029 2545 8493 5192 -1080 -499 -869 C ATOM 1829 O ALA A1029 -20.327 4.478 -9.783 1.00 44.86 O ANISOU 1829 O ALA A1029 2735 9145 5166 -1160 -500 -905 O ATOM 1830 CB ALA A1029 -21.931 2.363 -11.596 1.00 42.07 C ANISOU 1830 CB ALA A1029 2431 8234 5321 -1114 -535 -353 C ATOM 1831 N LEU A1030 -19.961 4.938 -11.956 1.00 40.65 N ANISOU 1831 N LEU A1030 2426 7879 5138 -1000 -568 -944 N ATOM 1832 CA LEU A1030 -18.646 5.510 -11.692 1.00 40.84 C ANISOU 1832 CA LEU A1030 2512 7926 5079 -1003 -642 -1065 C ATOM 1833 C LEU A1030 -18.760 6.844 -10.963 1.00 42.43 C ANISOU 1833 C LEU A1030 2661 8329 5133 -1011 -580 -1402 C ATOM 1834 O LEU A1030 -18.017 7.101 -10.008 1.00 44.08 O ANISOU 1834 O LEU A1030 2839 8783 5125 -1054 -627 -1495 O ATOM 1835 CB LEU A1030 -17.882 5.668 -13.005 1.00 42.71 C ANISOU 1835 CB LEU A1030 2896 7762 5572 -936 -708 -1028 C ATOM 1836 CG LEU A1030 -16.389 5.348 -13.003 1.00 46.32 C ANISOU 1836 CG LEU A1030 3405 8178 6017 -939 -819 -950 C ATOM 1837 CD1 LEU A1030 -16.097 4.130 -12.147 1.00 39.63 C ANISOU 1837 CD1 LEU A1030 2498 7543 5018 -977 -905 -756 C ATOM 1838 CD2 LEU A1030 -15.934 5.107 -14.427 1.00 36.24 C ANISOU 1838 CD2 LEU A1030 2233 6553 4984 -877 -857 -842 C ATOM 1839 N THR A1031 -19.688 7.705 -11.395 1.00 49.68 N ANISOU 1839 N THR A1031 3572 9132 6172 -960 -499 -1603 N ATOM 1840 CA THR A1031 -19.893 8.969 -10.693 1.00 43.97 C ANISOU 1840 CA THR A1031 2788 8589 5330 -944 -463 -1962 C ATOM 1841 C THR A1031 -20.400 8.734 -9.276 1.00 48.77 C ANISOU 1841 C THR A1031 3207 9715 5608 -1002 -388 -2037 C ATOM 1842 O THR A1031 -19.968 9.411 -8.333 1.00 55.60 O ANISOU 1842 O THR A1031 4029 10842 6254 -1012 -418 -2268 O ATOM 1843 CB THR A1031 -20.863 9.861 -11.468 1.00 43.31 C ANISOU 1843 CB THR A1031 2731 8257 5467 -863 -416 -2164 C ATOM 1844 OG1 THR A1031 -22.100 9.167 -11.671 1.00 52.56 O ANISOU 1844 OG1 THR A1031 3815 9449 6705 -850 -322 -2043 O ATOM 1845 CG2 THR A1031 -20.272 10.253 -12.816 1.00 40.94 C ANISOU 1845 CG2 THR A1031 2625 7500 5430 -829 -498 -2099 C ATOM 1846 N LYS A1032 -21.316 7.775 -9.103 1.00 47.30 N ANISOU 1846 N LYS A1032 2909 9691 5370 -1044 -292 -1830 N ATOM 1847 CA LYS A1032 -21.769 7.432 -7.757 1.00 50.32 C ANISOU 1847 CA LYS A1032 3106 10616 5399 -1130 -197 -1830 C ATOM 1848 C LYS A1032 -20.613 6.929 -6.899 1.00 51.43 C ANISOU 1848 C LYS A1032 3310 10966 5265 -1208 -313 -1684 C ATOM 1849 O LYS A1032 -20.529 7.245 -5.704 1.00 54.18 O ANISOU 1849 O LYS A1032 3650 11662 5276 -1224 -272 -1809 O ATOM 1850 CB LYS A1032 -22.885 6.390 -7.828 1.00 50.67 C ANISOU 1850 CB LYS A1032 3055 10729 5467 -1182 -73 -1545 C ATOM 1851 CG LYS A1032 -24.164 6.903 -8.468 1.00 50.28 C ANISOU 1851 CG LYS A1032 2959 10491 5654 -1087 52 -1703 C ATOM 1852 CD LYS A1032 -25.236 5.829 -8.503 1.00 50.88 C ANISOU 1852 CD LYS A1032 2955 10609 5767 -1147 159 -1396 C ATOM 1853 CE LYS A1032 -26.548 6.377 -9.042 1.00 50.92 C ANISOU 1853 CE LYS A1032 2912 10433 6003 -1042 271 -1573 C ATOM 1854 NZ LYS A1032 -27.596 5.323 -9.126 1.00 51.60 N ANISOU 1854 NZ LYS A1032 2922 10516 6166 -1105 356 -1262 N ATOM 1855 N MET A1033 -19.706 6.150 -7.495 1.00 49.52 N ANISOU 1855 N MET A1033 3166 10485 5164 -1234 -461 -1427 N ATOM 1856 CA MET A1033 -18.505 5.734 -6.780 1.00 50.50 C ANISOU 1856 CA MET A1033 3346 10759 5084 -1292 -613 -1320 C ATOM 1857 C MET A1033 -17.667 6.936 -6.367 1.00 52.39 C ANISOU 1857 C MET A1033 3645 11014 5248 -1242 -674 -1646 C ATOM 1858 O MET A1033 -17.098 6.956 -5.270 1.00 53.53 O ANISOU 1858 O MET A1033 3787 11461 5092 -1289 -753 -1691 O ATOM 1859 CB MET A1033 -17.673 4.785 -7.640 1.00 48.30 C ANISOU 1859 CB MET A1033 3203 10108 5040 -1266 -744 -1028 C ATOM 1860 CG MET A1033 -18.239 3.390 -7.765 1.00 48.21 C ANISOU 1860 CG MET A1033 3160 10109 5048 -1327 -764 -664 C ATOM 1861 SD MET A1033 -16.968 2.223 -8.269 1.00 46.92 S ANISOU 1861 SD MET A1033 3142 9641 5045 -1289 -985 -386 S ATOM 1862 CE MET A1033 -15.955 2.218 -6.791 1.00 55.46 C ANISOU 1862 CE MET A1033 4223 11089 5759 -1371 -1118 -403 C ATOM 1863 N ARG A1034 -17.572 7.945 -7.238 1.00 53.86 N ANISOU 1863 N ARG A1034 3910 10849 5705 -1149 -656 -1854 N ATOM 1864 CA ARG A1034 -16.813 9.143 -6.891 1.00 57.84 C ANISOU 1864 CA ARG A1034 4479 11316 6181 -1106 -725 -2142 C ATOM 1865 C ARG A1034 -17.452 9.877 -5.720 1.00 60.35 C ANISOU 1865 C ARG A1034 4693 12040 6196 -1096 -675 -2455 C ATOM 1866 O ARG A1034 -16.750 10.381 -4.835 1.00 61.82 O ANISOU 1866 O ARG A1034 4926 12376 6188 -1086 -761 -2606 O ATOM 1867 CB ARG A1034 -16.696 10.065 -8.103 1.00 54.16 C ANISOU 1867 CB ARG A1034 4121 10395 6062 -1034 -725 -2256 C ATOM 1868 CG ARG A1034 -15.727 11.219 -7.903 1.00 54.84 C ANISOU 1868 CG ARG A1034 4293 10359 6184 -1008 -825 -2463 C ATOM 1869 CD ARG A1034 -15.585 12.053 -9.164 1.00 58.06 C ANISOU 1869 CD ARG A1034 4814 10329 6918 -973 -836 -2501 C ATOM 1870 NE ARG A1034 -14.448 12.967 -9.086 1.00 61.54 N ANISOU 1870 NE ARG A1034 5336 10624 7423 -985 -951 -2592 N ATOM 1871 CZ ARG A1034 -14.504 14.193 -8.577 1.00 58.81 C ANISOU 1871 CZ ARG A1034 5010 10279 7054 -945 -1004 -2866 C ATOM 1872 NH1 ARG A1034 -13.416 14.952 -8.551 1.00 50.67 N ANISOU 1872 NH1 ARG A1034 4053 9093 6106 -973 -1126 -2898 N ATOM 1873 NH2 ARG A1034 -15.648 14.662 -8.095 1.00 53.98 N ANISOU 1873 NH2 ARG A1034 4337 9822 6350 -872 -943 -3108 N ATOM 1874 N ALA A1035 -18.786 9.948 -5.697 1.00 64.58 N ANISOU 1874 N ALA A1035 5092 12750 6694 -1084 -535 -2562 N ATOM 1875 CA ALA A1035 -19.472 10.563 -4.565 1.00 69.49 C ANISOU 1875 CA ALA A1035 5668 13725 7012 -1026 -424 -2827 C ATOM 1876 C ALA A1035 -19.189 9.801 -3.275 1.00 68.93 C ANISOU 1876 C ALA A1035 5611 14067 6511 -1101 -407 -2651 C ATOM 1877 O ALA A1035 -18.876 10.402 -2.239 1.00 62.70 O ANISOU 1877 O ALA A1035 4855 13538 5430 -1066 -446 -2883 O ATOM 1878 CB ALA A1035 -20.976 10.629 -4.835 1.00 57.70 C ANISOU 1878 CB ALA A1035 4063 12261 5600 -969 -218 -2893 C ATOM 1879 N ALA A1036 -19.285 8.468 -3.325 1.00 68.05 N ANISOU 1879 N ALA A1036 5493 14007 6355 -1205 -375 -2238 N ATOM 1880 CA ALA A1036 -19.043 7.664 -2.130 1.00 62.18 C ANISOU 1880 CA ALA A1036 4787 13636 5202 -1301 -383 -2023 C ATOM 1881 C ALA A1036 -17.605 7.808 -1.646 1.00 67.89 C ANISOU 1881 C ALA A1036 5621 14362 5814 -1314 -622 -2065 C ATOM 1882 O ALA A1036 -17.346 7.833 -0.436 1.00 66.34 O ANISOU 1882 O ALA A1036 5478 14501 5226 -1337 -652 -2110 O ATOM 1883 CB ALA A1036 -19.372 6.198 -2.408 1.00 61.41 C ANISOU 1883 CB ALA A1036 4673 13516 5143 -1419 -359 -1552 C ATOM 1884 N ALA A1037 -16.655 7.910 -2.578 1.00 69.17 N ANISOU 1884 N ALA A1037 5813 14160 6310 -1300 -795 -2055 N ATOM 1885 CA ALA A1037 -15.256 8.055 -2.193 1.00 60.40 C ANISOU 1885 CA ALA A1037 4809 12965 5174 -1293 -998 -2074 C ATOM 1886 C ALA A1037 -14.984 9.433 -1.606 1.00 62.17 C ANISOU 1886 C ALA A1037 5087 13207 5328 -1195 -1014 -2460 C ATOM 1887 O ALA A1037 -14.191 9.569 -0.666 1.00 64.33 O ANISOU 1887 O ALA A1037 5450 13589 5405 -1185 -1131 -2498 O ATOM 1888 CB ALA A1037 -14.351 7.796 -3.396 1.00 57.26 C ANISOU 1888 CB ALA A1037 4478 12069 5210 -1265 -1085 -1910 C ATOM 1889 N LEU A1038 -15.631 10.469 -2.145 1.00 61.47 N ANISOU 1889 N LEU A1038 4955 12977 5423 -1111 -920 -2742 N ATOM 1890 CA LEU A1038 -15.405 11.816 -1.631 1.00 66.68 C ANISOU 1890 CA LEU A1038 5674 13596 6066 -1001 -961 -3098 C ATOM 1891 C LEU A1038 -16.039 12.002 -0.257 1.00 67.12 C ANISOU 1891 C LEU A1038 5705 14131 5665 -963 -884 -3287 C ATOM 1892 O LEU A1038 -15.448 12.642 0.621 1.00 69.52 O ANISOU 1892 O LEU A1038 6097 14484 5833 -895 -979 -3452 O ATOM 1893 CB LEU A1038 -15.932 12.855 -2.620 1.00 66.08 C ANISOU 1893 CB LEU A1038 5583 13187 6338 -915 -909 -3319 C ATOM 1894 CG LEU A1038 -14.957 13.226 -3.742 1.00 66.09 C ANISOU 1894 CG LEU A1038 5685 12672 6752 -922 -1017 -3216 C ATOM 1895 CD1 LEU A1038 -15.547 14.299 -4.641 1.00 67.21 C ANISOU 1895 CD1 LEU A1038 5849 12495 7194 -845 -980 -3410 C ATOM 1896 CD2 LEU A1038 -13.626 13.683 -3.160 1.00 60.45 C ANISOU 1896 CD2 LEU A1038 5069 11876 6021 -920 -1192 -3247 C ATOM 1897 N ASP A1039 -17.240 11.454 -0.044 1.00 70.53 N ANISOU 1897 N ASP A1039 6023 14924 5852 -1004 -705 -3257 N ATOM 1898 CA ASP A1039 -17.834 11.538 1.288 1.00 76.53 C ANISOU 1898 CA ASP A1039 6775 16166 6138 -971 -580 -3389 C ATOM 1899 C ASP A1039 -17.095 10.655 2.284 1.00 75.74 C ANISOU 1899 C ASP A1039 6783 16300 5695 -1070 -668 -3107 C ATOM 1900 O ASP A1039 -16.972 11.014 3.461 1.00 77.47 O ANISOU 1900 O ASP A1039 7074 16754 5607 -1013 -664 -3236 O ATOM 1901 CB ASP A1039 -19.314 11.161 1.246 1.00 80.02 C ANISOU 1901 CB ASP A1039 7078 16862 6465 -983 -299 -3351 C ATOM 1902 CG ASP A1039 -19.990 11.318 2.595 1.00 91.81 C ANISOU 1902 CG ASP A1039 8541 18898 7443 -945 -127 -3518 C ATOM 1903 OD1 ASP A1039 -20.357 12.458 2.952 1.00 94.36 O ANISOU 1903 OD1 ASP A1039 8830 19220 7801 -773 -85 -3902 O ATOM 1904 OD2 ASP A1039 -20.152 10.302 3.303 1.00100.73 O ANISOU 1904 OD2 ASP A1039 9689 20353 8232 -1075 -28 -3193 O ATOM 1905 N ALA A1040 -16.588 9.509 1.833 1.00 81.69 N ANISOU 1905 N ALA A1040 7556 16957 6524 -1208 -769 -2721 N ATOM 1906 CA ALA A1040 -15.844 8.622 2.715 1.00 80.58 C ANISOU 1906 CA ALA A1040 7537 16971 6111 -1300 -893 -2431 C ATOM 1907 C ALA A1040 -14.429 9.114 2.992 1.00 82.07 C ANISOU 1907 C ALA A1040 7858 16881 6442 -1231 -1129 -2521 C ATOM 1908 O ALA A1040 -13.792 8.630 3.935 1.00 76.39 O ANISOU 1908 O ALA A1040 7260 16293 5470 -1272 -1254 -2375 O ATOM 1909 CB ALA A1040 -15.787 7.214 2.120 1.00 80.21 C ANISOU 1909 CB ALA A1040 7467 16858 6151 -1449 -953 -1980 C ATOM 1910 N GLN A1041 -13.926 10.064 2.200 1.00 78.13 N ANISOU 1910 N GLN A1041 7349 15993 6343 -1137 -1200 -2740 N ATOM 1911 CA GLN A1041 -12.561 10.538 2.395 1.00 78.47 C ANISOU 1911 CA GLN A1041 7506 15767 6545 -1091 -1425 -2804 C ATOM 1912 C GLN A1041 -12.448 11.383 3.657 1.00 90.09 C ANISOU 1912 C GLN A1041 9066 17432 7731 -999 -1472 -3074 C ATOM 1913 O GLN A1041 -11.559 11.161 4.487 1.00101.10 O ANISOU 1913 O GLN A1041 10580 18864 8970 -1011 -1649 -3006 O ATOM 1914 CB GLN A1041 -12.095 11.333 1.177 1.00 78.05 C ANISOU 1914 CB GLN A1041 7424 15247 6983 -1043 -1468 -2919 C ATOM 1915 CG GLN A1041 -10.671 11.849 1.290 1.00 74.20 C ANISOU 1915 CG GLN A1041 7030 14479 6683 -1019 -1693 -2966 C ATOM 1916 CD GLN A1041 -10.215 12.583 0.044 1.00 70.98 C ANISOU 1916 CD GLN A1041 6602 13630 6737 -1005 -1715 -3019 C ATOM 1917 OE1 GLN A1041 -11.027 13.125 -0.705 1.00 74.24 O ANISOU 1917 OE1 GLN A1041 6966 13933 7308 -973 -1581 -3131 O ATOM 1918 NE2 GLN A1041 -8.909 12.601 -0.185 1.00 72.91 N ANISOU 1918 NE2 GLN A1041 6889 13620 7194 -1036 -1887 -2928 N ATOM 1919 N LYS A1042 -13.339 12.361 3.819 1.00 92.07 N ANISOU 1919 N LYS A1042 9266 17790 7927 -892 -1333 -3390 N ATOM 1920 CA LYS A1042 -13.363 13.194 5.013 1.00103.28 C ANISOU 1920 CA LYS A1042 10764 19396 9081 -777 -1365 -3666 C ATOM 1921 C LYS A1042 -14.025 12.497 6.198 1.00106.70 C ANISOU 1921 C LYS A1042 11223 20333 8985 -814 -1229 -3567 C ATOM 1922 O LYS A1042 -14.482 13.167 7.132 1.00108.73 O ANISOU 1922 O LYS A1042 11504 20822 8986 -703 -1163 -3818 O ATOM 1923 CB LYS A1042 -14.061 14.524 4.708 1.00105.85 C ANISOU 1923 CB LYS A1042 11022 19605 9592 -627 -1287 -4044 C ATOM 1924 CG LYS A1042 -13.358 15.327 3.619 1.00107.53 C ANISOU 1924 CG LYS A1042 11247 19298 10309 -605 -1435 -4118 C ATOM 1925 CD LYS A1042 -11.869 15.451 3.924 1.00109.15 C ANISOU 1925 CD LYS A1042 11581 19287 10603 -636 -1698 -4047 C ATOM 1926 CE LYS A1042 -11.117 16.117 2.784 1.00103.00 C ANISOU 1926 CE LYS A1042 10809 18014 10314 -658 -1820 -4044 C ATOM 1927 NZ LYS A1042 -11.575 17.513 2.543 1.00102.08 N ANISOU 1927 NZ LYS A1042 10694 17702 10390 -541 -1829 -4351 N ATOM 1928 N ALA A1043 -14.078 11.168 6.169 1.00104.67 N ANISOU 1928 N ALA A1043 10965 20231 8572 -970 -1193 -3188 N ATOM 1929 CA ALA A1043 -14.716 10.354 7.194 1.00102.26 C ANISOU 1929 CA ALA A1043 10694 20381 7777 -1054 -1055 -2997 C ATOM 1930 C ALA A1043 -13.635 9.668 8.016 1.00 99.18 C ANISOU 1930 C ALA A1043 10494 19996 7196 -1127 -1287 -2762 C ATOM 1931 O ALA A1043 -12.869 8.857 7.482 1.00103.75 O ANISOU 1931 O ALA A1043 11105 20346 7972 -1220 -1457 -2482 O ATOM 1932 CB ALA A1043 -15.644 9.316 6.562 1.00103.47 C ANISOU 1932 CB ALA A1043 10723 20688 7903 -1199 -863 -2696 C ATOM 1933 N THR A1044 -13.576 9.985 9.300 1.00102.65 N ANISOU 1933 N THR A1044 11059 20676 7267 -1072 -1306 -2882 N ATOM 1934 CA THR A1044 -12.513 9.454 10.143 1.00102.57 C ANISOU 1934 CA THR A1044 11255 20641 7077 -1121 -1562 -2703 C ATOM 1935 C THR A1044 -12.802 8.000 10.505 1.00102.09 C ANISOU 1935 C THR A1044 11251 20810 6728 -1310 -1519 -2249 C ATOM 1936 O THR A1044 -13.901 7.690 10.975 1.00105.12 O ANISOU 1936 O THR A1044 11590 21567 6784 -1376 -1262 -2160 O ATOM 1937 CB THR A1044 -12.357 10.290 11.410 1.00100.02 C ANISOU 1937 CB THR A1044 11073 20486 6444 -996 -1616 -2986 C ATOM 1938 OG1 THR A1044 -13.571 10.248 12.169 1.00107.20 O ANISOU 1938 OG1 THR A1044 11948 21844 6938 -998 -1329 -3016 O ATOM 1939 CG2 THR A1044 -12.041 11.730 11.054 1.00 99.12 C ANISOU 1939 CG2 THR A1044 10914 20100 6646 -817 -1699 -3409 C ATOM 1940 N PRO A1045 -11.853 7.092 10.297 1.00 99.86 N ANISOU 1940 N PRO A1045 11061 20297 6583 -1401 -1770 -1950 N ATOM 1941 CA PRO A1045 -12.056 5.687 10.671 1.00 96.73 C ANISOU 1941 CA PRO A1045 10748 20061 5945 -1583 -1786 -1494 C ATOM 1942 C PRO A1045 -12.009 5.515 12.180 1.00102.03 C ANISOU 1942 C PRO A1045 11631 21022 6114 -1613 -1828 -1438 C ATOM 1943 O PRO A1045 -11.656 6.458 12.905 1.00104.40 O ANISOU 1943 O PRO A1045 12024 21363 6280 -1477 -1890 -1759 O ATOM 1944 CB PRO A1045 -10.881 4.975 9.985 1.00 93.90 C ANISOU 1944 CB PRO A1045 10429 19285 5963 -1612 -2098 -1282 C ATOM 1945 CG PRO A1045 -9.827 6.018 9.883 1.00103.79 C ANISOU 1945 CG PRO A1045 11706 20254 7476 -1455 -2289 -1623 C ATOM 1946 CD PRO A1045 -10.554 7.311 9.639 1.00 97.94 C ANISOU 1946 CD PRO A1045 10835 19605 6773 -1340 -2056 -2011 C ATOM 1947 N PRO A1046 -12.349 4.327 12.699 1.00109.41 N ANISOU 1947 N PRO A1046 12661 22145 6766 -1792 -1813 -1028 N ATOM 1948 CA PRO A1046 -12.369 4.165 14.161 1.00109.75 C ANISOU 1948 CA PRO A1046 12921 22476 6302 -1831 -1836 -965 C ATOM 1949 C PRO A1046 -10.991 4.195 14.789 1.00111.25 C ANISOU 1949 C PRO A1046 13349 22434 6485 -1758 -2226 -1011 C ATOM 1950 O PRO A1046 -10.851 4.697 15.910 1.00115.36 O ANISOU 1950 O PRO A1046 14040 23136 6656 -1690 -2262 -1183 O ATOM 1951 CB PRO A1046 -13.044 2.801 14.355 1.00111.31 C ANISOU 1951 CB PRO A1046 13147 22854 6290 -2070 -1745 -463 C ATOM 1952 CG PRO A1046 -12.666 2.046 13.128 1.00108.77 C ANISOU 1952 CG PRO A1046 12732 22171 6427 -2129 -1900 -224 C ATOM 1953 CD PRO A1046 -12.686 3.064 12.013 1.00102.25 C ANISOU 1953 CD PRO A1046 11690 21166 5995 -1970 -1804 -589 C ATOM 1954 N LYS A1047 -9.973 3.678 14.105 1.00108.25 N ANISOU 1954 N LYS A1047 12985 21654 6491 -1760 -2525 -876 N ATOM 1955 CA LYS A1047 -8.629 3.601 14.660 1.00110.35 C ANISOU 1955 CA LYS A1047 13461 21674 6794 -1694 -2923 -902 C ATOM 1956 C LYS A1047 -8.016 4.990 14.771 1.00110.03 C ANISOU 1956 C LYS A1047 13416 21514 6876 -1505 -3008 -1364 C ATOM 1957 O LYS A1047 -7.297 5.433 13.875 1.00106.12 O ANISOU 1957 O LYS A1047 12800 20674 6845 -1423 -3136 -1520 O ATOM 1958 CB LYS A1047 -7.768 2.660 13.808 1.00106.58 C ANISOU 1958 CB LYS A1047 12955 20792 6749 -1730 -3198 -653 C ATOM 1959 CG LYS A1047 -8.366 1.255 13.677 1.00106.81 C ANISOU 1959 CG LYS A1047 12999 20887 6697 -1916 -3153 -181 C ATOM 1960 CD LYS A1047 -7.558 0.365 12.768 1.00106.83 C ANISOU 1960 CD LYS A1047 12957 20466 7168 -1912 -3419 20 C ATOM 1961 CE LYS A1047 -8.180 -1.007 12.671 1.00104.27 C ANISOU 1961 CE LYS A1047 12662 20177 6780 -2093 -3398 483 C ATOM 1962 NZ LYS A1047 -7.442 -1.919 11.762 1.00101.46 N ANISOU 1962 NZ LYS A1047 12261 19389 6901 -2061 -3657 659 N ATOM 1963 N LEU A1048 -8.313 5.681 15.864 1.00115.35 N ANISOU 1963 N LEU A1048 14220 22462 7144 -1441 -2935 -1578 N ATOM 1964 CA LEU A1048 -7.779 7.007 16.126 1.00117.09 C ANISOU 1964 CA LEU A1048 14468 22576 7444 -1265 -3039 -2010 C ATOM 1965 C LEU A1048 -7.260 7.142 17.561 1.00123.18 C ANISOU 1965 C LEU A1048 15538 23463 7801 -1222 -3258 -2076 C ATOM 1966 O LEU A1048 -6.056 7.253 17.786 1.00120.14 O ANISOU 1966 O LEU A1048 15287 22792 7567 -1170 -3627 -2135 O ATOM 1967 CB LEU A1048 -8.845 8.073 15.863 1.00116.36 C ANISOU 1967 CB LEU A1048 14191 22685 7335 -1171 -2688 -2330 C ATOM 1968 CG LEU A1048 -9.212 8.348 14.405 1.00114.60 C ANISOU 1968 CG LEU A1048 13687 22273 7581 -1160 -2522 -2395 C ATOM 1969 CD1 LEU A1048 -10.343 9.367 14.321 1.00116.28 C ANISOU 1969 CD1 LEU A1048 13747 22706 7729 -1054 -2198 -2718 C ATOM 1970 CD2 LEU A1048 -7.998 8.837 13.640 1.00111.92 C ANISOU 1970 CD2 LEU A1048 13307 21466 7750 -1090 -2800 -2530 C ATOM 1971 N SER A1055 -1.936 11.558 12.347 1.00101.69 N ANISOU 1971 N SER A1055 12004 18385 8250 -912 -4178 -3132 N ATOM 1972 CA SER A1055 -1.436 11.934 11.027 1.00 97.87 C ANISOU 1972 CA SER A1055 11308 17569 8312 -941 -4154 -3142 C ATOM 1973 C SER A1055 -0.431 10.926 10.429 1.00106.85 C ANISOU 1973 C SER A1055 12374 18467 9758 -1026 -4331 -2871 C ATOM 1974 O SER A1055 -0.567 10.565 9.260 1.00 99.44 O ANISOU 1974 O SER A1055 11264 17396 9121 -1059 -4179 -2747 O ATOM 1975 CB SER A1055 -0.817 13.336 11.074 1.00 98.89 C ANISOU 1975 CB SER A1055 11421 17494 8658 -900 -4283 -3424 C ATOM 1976 OG SER A1055 -1.797 14.311 11.387 1.00100.09 O ANISOU 1976 OG SER A1055 11602 17811 8617 -800 -4105 -3693 O ATOM 1977 N PRO A1056 0.567 10.470 11.196 1.00 99.89 N ANISOU 1977 N PRO A1056 11621 17519 8814 -1053 -4656 -2785 N ATOM 1978 CA PRO A1056 1.476 9.444 10.658 1.00103.52 C ANISOU 1978 CA PRO A1056 12005 17758 9568 -1117 -4832 -2536 C ATOM 1979 C PRO A1056 0.742 8.125 10.458 1.00110.09 C ANISOU 1979 C PRO A1056 12858 18723 10249 -1128 -4715 -2273 C ATOM 1980 O PRO A1056 0.054 7.639 11.358 1.00114.57 O ANISOU 1980 O PRO A1056 13601 19563 10368 -1121 -4694 -2198 O ATOM 1981 CB PRO A1056 2.564 9.331 11.731 1.00114.76 C ANISOU 1981 CB PRO A1056 13593 19124 10887 -1144 -5217 -2529 C ATOM 1982 CG PRO A1056 1.900 9.773 12.977 1.00120.04 C ANISOU 1982 CG PRO A1056 14490 20072 11047 -1089 -5212 -2679 C ATOM 1983 CD PRO A1056 0.977 10.876 12.554 1.00112.63 C ANISOU 1983 CD PRO A1056 13451 19229 10114 -1027 -4899 -2917 C ATOM 1984 N GLU A1057 0.891 7.554 9.262 1.00108.38 N ANISOU 1984 N GLU A1057 12459 18317 10402 -1152 -4631 -2122 N ATOM 1985 CA GLU A1057 0.123 6.405 8.784 1.00108.14 C ANISOU 1985 CA GLU A1057 12399 18372 10318 -1165 -4479 -1880 C ATOM 1986 C GLU A1057 -1.381 6.681 8.772 1.00109.19 C ANISOU 1986 C GLU A1057 12526 18813 10149 -1171 -4124 -1918 C ATOM 1987 O GLU A1057 -2.181 5.759 8.564 1.00108.57 O ANISOU 1987 O GLU A1057 12441 18872 9938 -1212 -3982 -1699 O ATOM 1988 CB GLU A1057 0.442 5.134 9.592 1.00111.42 C ANISOU 1988 CB GLU A1057 12991 18819 10525 -1171 -4748 -1650 C ATOM 1989 CG GLU A1057 0.148 3.821 8.858 1.00107.63 C ANISOU 1989 CG GLU A1057 12443 18267 10184 -1180 -4702 -1375 C ATOM 1990 CD GLU A1057 1.374 2.945 8.667 1.00103.22 C ANISOU 1990 CD GLU A1057 11874 17393 9953 -1135 -5048 -1266 C ATOM 1991 OE1 GLU A1057 2.480 3.369 9.062 1.00103.80 O ANISOU 1991 OE1 GLU A1057 11975 17303 10159 -1132 -5318 -1377 O ATOM 1992 OE2 GLU A1057 1.229 1.829 8.122 1.00 98.32 O ANISOU 1992 OE2 GLU A1057 11210 16683 9463 -1107 -5055 -1072 O ATOM 1993 N MET A1058 -1.784 7.934 8.985 1.00109.09 N ANISOU 1993 N MET A1058 12506 18902 10042 -1135 -3988 -2192 N ATOM 1994 CA MET A1058 -3.153 8.378 8.767 1.00107.28 C ANISOU 1994 CA MET A1058 12218 18914 9631 -1126 -3644 -2285 C ATOM 1995 C MET A1058 -3.315 9.187 7.494 1.00 99.56 C ANISOU 1995 C MET A1058 11046 17729 9053 -1106 -3460 -2425 C ATOM 1996 O MET A1058 -4.376 9.128 6.870 1.00 96.63 O ANISOU 1996 O MET A1058 10580 17467 8670 -1118 -3188 -2400 O ATOM 1997 CB MET A1058 -3.644 9.215 9.955 1.00118.81 C ANISOU 1997 CB MET A1058 13819 20647 10675 -1070 -3611 -2519 C ATOM 1998 CG MET A1058 -3.789 8.431 11.248 1.00133.63 C ANISOU 1998 CG MET A1058 15912 22800 12060 -1099 -3717 -2366 C ATOM 1999 SD MET A1058 -4.920 7.038 11.076 1.00142.99 S ANISOU 1999 SD MET A1058 17076 24254 12998 -1210 -3488 -1997 S ATOM 2000 CE MET A1058 -6.403 7.872 10.520 1.00135.26 C ANISOU 2000 CE MET A1058 15923 23504 11968 -1184 -3055 -2195 C ATOM 2001 N LYS A1059 -2.289 9.945 7.098 1.00101.25 N ANISOU 2001 N LYS A1059 11206 17646 9619 -1091 -3607 -2558 N ATOM 2002 CA LYS A1059 -2.232 10.464 5.738 1.00 95.25 C ANISOU 2002 CA LYS A1059 10273 16633 9285 -1102 -3464 -2598 C ATOM 2003 C LYS A1059 -2.182 9.336 4.720 1.00 92.48 C ANISOU 2003 C LYS A1059 9816 16161 9162 -1144 -3396 -2328 C ATOM 2004 O LYS A1059 -2.433 9.570 3.533 1.00 91.02 O ANISOU 2004 O LYS A1059 9505 15818 9261 -1154 -3218 -2322 O ATOM 2005 CB LYS A1059 -1.019 11.379 5.568 1.00 93.25 C ANISOU 2005 CB LYS A1059 9985 16101 9347 -1112 -3652 -2731 C ATOM 2006 CG LYS A1059 -0.952 12.521 6.565 1.00 93.27 C ANISOU 2006 CG LYS A1059 10100 16174 9165 -1064 -3764 -3000 C ATOM 2007 CD LYS A1059 0.331 13.317 6.394 1.00 92.70 C ANISOU 2007 CD LYS A1059 9981 15824 9416 -1107 -3973 -3081 C ATOM 2008 CE LYS A1059 1.552 12.420 6.523 1.00 93.79 C ANISOU 2008 CE LYS A1059 10101 15858 9678 -1167 -4211 -2884 C ATOM 2009 NZ LYS A1059 2.822 13.175 6.339 1.00 94.94 N ANISOU 2009 NZ LYS A1059 10164 15773 10135 -1232 -4391 -2946 N ATOM 2010 N ASP A1060 -1.835 8.124 5.158 1.00 80.07 N ANISOU 2010 N ASP A1060 8309 14634 7478 -1164 -3555 -2107 N ATOM 2011 CA ASP A1060 -2.028 6.942 4.328 1.00 85.04 C ANISOU 2011 CA ASP A1060 8865 15187 8258 -1185 -3489 -1849 C ATOM 2012 C ASP A1060 -3.505 6.758 3.996 1.00 81.61 C ANISOU 2012 C ASP A1060 8399 14965 7642 -1206 -3193 -1793 C ATOM 2013 O ASP A1060 -3.880 6.620 2.825 1.00 73.05 O ANISOU 2013 O ASP A1060 7197 13748 6810 -1210 -3020 -1729 O ATOM 2014 CB ASP A1060 -1.477 5.712 5.055 1.00 82.07 C ANISOU 2014 CB ASP A1060 8601 14827 7753 -1192 -3753 -1636 C ATOM 2015 CG ASP A1060 -1.142 4.572 4.115 1.00 77.57 C ANISOU 2015 CG ASP A1060 7946 14039 7489 -1183 -3795 -1411 C ATOM 2016 OD1 ASP A1060 -0.848 4.839 2.932 1.00 84.08 O ANISOU 2016 OD1 ASP A1060 8620 14642 8685 -1170 -3686 -1442 O ATOM 2017 OD2 ASP A1060 -1.174 3.406 4.562 1.00 78.82 O ANISOU 2017 OD2 ASP A1060 8198 14240 7510 -1184 -3943 -1204 O ATOM 2018 N PHE A1061 -4.360 6.784 5.023 1.00 81.58 N ANISOU 2018 N PHE A1061 8501 15302 7194 -1222 -3127 -1818 N ATOM 2019 CA PHE A1061 -5.794 6.578 4.835 1.00 77.68 C ANISOU 2019 CA PHE A1061 7963 15061 6491 -1261 -2847 -1754 C ATOM 2020 C PHE A1061 -6.380 7.593 3.859 1.00 91.02 C ANISOU 2020 C PHE A1061 9519 16654 8411 -1225 -2618 -1964 C ATOM 2021 O PHE A1061 -7.087 7.225 2.914 1.00 88.07 O ANISOU 2021 O PHE A1061 9045 16240 8178 -1251 -2442 -1853 O ATOM 2022 CB PHE A1061 -6.505 6.650 6.190 1.00 81.37 C ANISOU 2022 CB PHE A1061 8559 15930 6427 -1281 -2802 -1792 C ATOM 2023 CG PHE A1061 -8.005 6.755 6.095 1.00 81.85 C ANISOU 2023 CG PHE A1061 8547 16292 6261 -1315 -2489 -1807 C ATOM 2024 CD1 PHE A1061 -8.634 7.987 6.199 1.00 81.56 C ANISOU 2024 CD1 PHE A1061 8464 16369 6156 -1240 -2318 -2137 C ATOM 2025 CD2 PHE A1061 -8.785 5.625 5.915 1.00 80.55 C ANISOU 2025 CD2 PHE A1061 8356 16283 5967 -1420 -2382 -1494 C ATOM 2026 CE1 PHE A1061 -10.009 8.090 6.116 1.00 81.53 C ANISOU 2026 CE1 PHE A1061 8374 16643 5961 -1258 -2036 -2178 C ATOM 2027 CE2 PHE A1061 -10.162 5.722 5.833 1.00 80.51 C ANISOU 2027 CE2 PHE A1061 8263 16567 5760 -1463 -2096 -1505 C ATOM 2028 CZ PHE A1061 -10.774 6.956 5.934 1.00 81.00 C ANISOU 2028 CZ PHE A1061 8265 16756 5756 -1376 -1917 -1861 C ATOM 2029 N ARG A1062 -6.100 8.881 4.074 1.00 79.96 N ANISOU 2029 N ARG A1062 8129 15189 7062 -1164 -2640 -2262 N ATOM 2030 CA ARG A1062 -6.649 9.903 3.189 1.00 82.82 C ANISOU 2030 CA ARG A1062 8393 15424 7651 -1127 -2455 -2464 C ATOM 2031 C ARG A1062 -5.975 9.884 1.824 1.00 76.30 C ANISOU 2031 C ARG A1062 7474 14216 7299 -1144 -2464 -2375 C ATOM 2032 O ARG A1062 -6.603 10.234 0.817 1.00 84.09 O ANISOU 2032 O ARG A1062 8384 15085 8481 -1140 -2283 -2411 O ATOM 2033 CB ARG A1062 -6.521 11.282 3.836 1.00 92.01 C ANISOU 2033 CB ARG A1062 9615 16595 8751 -1053 -2510 -2794 C ATOM 2034 CG ARG A1062 -7.206 11.374 5.190 1.00103.63 C ANISOU 2034 CG ARG A1062 11185 18453 9735 -1013 -2479 -2910 C ATOM 2035 CD ARG A1062 -7.703 12.780 5.484 1.00109.48 C ANISOU 2035 CD ARG A1062 11936 19221 10441 -909 -2415 -3269 C ATOM 2036 NE ARG A1062 -8.822 12.763 6.423 1.00110.09 N ANISOU 2036 NE ARG A1062 12047 19711 10072 -862 -2253 -3371 N ATOM 2037 CZ ARG A1062 -9.547 13.829 6.747 1.00103.62 C ANISOU 2037 CZ ARG A1062 11217 18988 9166 -748 -2152 -3686 C ATOM 2038 NH1 ARG A1062 -9.273 15.009 6.207 1.00100.00 N ANISOU 2038 NH1 ARG A1062 10737 18217 9042 -677 -2222 -3916 N ATOM 2039 NH2 ARG A1062 -10.549 13.715 7.608 1.00100.61 N ANISOU 2039 NH2 ARG A1062 10848 19009 8369 -706 -1983 -3760 N ATOM 2040 N HIS A1063 -4.707 9.475 1.768 1.00 77.09 N ANISOU 2040 N HIS A1063 7585 14122 7585 -1160 -2670 -2261 N ATOM 2041 CA HIS A1063 -4.024 9.349 0.487 1.00 68.06 C ANISOU 2041 CA HIS A1063 6347 12652 6861 -1176 -2660 -2159 C ATOM 2042 C HIS A1063 -4.636 8.247 -0.368 1.00 67.84 C ANISOU 2042 C HIS A1063 6265 12603 6908 -1187 -2523 -1926 C ATOM 2043 O HIS A1063 -4.659 8.360 -1.599 1.00 62.92 O ANISOU 2043 O HIS A1063 5571 11759 6577 -1186 -2402 -1888 O ATOM 2044 CB HIS A1063 -2.535 9.087 0.714 1.00 69.28 C ANISOU 2044 CB HIS A1063 6504 12645 7176 -1187 -2915 -2097 C ATOM 2045 CG HIS A1063 -1.801 8.657 -0.518 1.00 66.98 C ANISOU 2045 CG HIS A1063 6106 12081 7264 -1200 -2900 -1952 C ATOM 2046 ND1 HIS A1063 -1.565 7.333 -0.819 1.00 66.80 N ANISOU 2046 ND1 HIS A1063 6060 12010 7310 -1185 -2957 -1728 N ATOM 2047 CD2 HIS A1063 -1.252 9.375 -1.526 1.00 65.58 C ANISOU 2047 CD2 HIS A1063 5843 11672 7401 -1226 -2835 -1998 C ATOM 2048 CE1 HIS A1063 -0.903 7.254 -1.959 1.00 64.43 C ANISOU 2048 CE1 HIS A1063 5660 11474 7347 -1186 -2916 -1662 C ATOM 2049 NE2 HIS A1063 -0.701 8.479 -2.409 1.00 64.04 N ANISOU 2049 NE2 HIS A1063 5570 11326 7436 -1221 -2832 -1812 N ATOM 2050 N GLY A1064 -5.139 7.183 0.263 1.00 66.52 N ANISOU 2050 N GLY A1064 6145 12657 6474 -1204 -2550 -1755 N ATOM 2051 CA GLY A1064 -5.760 6.111 -0.498 1.00 64.41 C ANISOU 2051 CA GLY A1064 5835 12360 6279 -1219 -2446 -1519 C ATOM 2052 C GLY A1064 -7.007 6.559 -1.233 1.00 62.38 C ANISOU 2052 C GLY A1064 5517 12141 6045 -1225 -2184 -1581 C ATOM 2053 O GLY A1064 -7.254 6.142 -2.367 1.00 59.77 O ANISOU 2053 O GLY A1064 5135 11619 5957 -1214 -2087 -1461 O ATOM 2054 N PHE A1065 -7.818 7.404 -0.594 1.00 63.75 N ANISOU 2054 N PHE A1065 5701 12553 5969 -1228 -2077 -1783 N ATOM 2055 CA PHE A1065 -8.951 8.000 -1.292 1.00 71.35 C ANISOU 2055 CA PHE A1065 6598 13520 6993 -1218 -1852 -1900 C ATOM 2056 C PHE A1065 -8.494 9.061 -2.284 1.00 60.25 C ANISOU 2056 C PHE A1065 5174 11773 5945 -1178 -1822 -2062 C ATOM 2057 O PHE A1065 -9.108 9.219 -3.346 1.00 71.50 O ANISOU 2057 O PHE A1065 6560 13036 7569 -1169 -1677 -2052 O ATOM 2058 CB PHE A1065 -9.940 8.596 -0.290 1.00 77.05 C ANISOU 2058 CB PHE A1065 7326 14605 7346 -1213 -1753 -2100 C ATOM 2059 CG PHE A1065 -10.793 7.571 0.405 1.00 76.68 C ANISOU 2059 CG PHE A1065 7272 14927 6934 -1285 -1694 -1901 C ATOM 2060 CD1 PHE A1065 -10.685 7.369 1.771 1.00 69.38 C ANISOU 2060 CD1 PHE A1065 6437 14315 5608 -1311 -1775 -1889 C ATOM 2061 CD2 PHE A1065 -11.702 6.809 -0.312 1.00 64.07 C ANISOU 2061 CD2 PHE A1065 5593 13356 5395 -1338 -1563 -1702 C ATOM 2062 CE1 PHE A1065 -11.471 6.428 2.409 1.00 71.06 C ANISOU 2062 CE1 PHE A1065 6662 14875 5464 -1405 -1709 -1661 C ATOM 2063 CE2 PHE A1065 -12.489 5.866 0.320 1.00 65.68 C ANISOU 2063 CE2 PHE A1065 5787 13904 5264 -1435 -1516 -1477 C ATOM 2064 CZ PHE A1065 -12.375 5.675 1.683 1.00 69.23 C ANISOU 2064 CZ PHE A1065 6332 14678 5294 -1477 -1580 -1445 C ATOM 2065 N ASP A1066 -7.423 9.792 -1.956 1.00 62.81 N ANISOU 2065 N ASP A1066 5537 11977 6352 -1164 -1970 -2192 N ATOM 2066 CA ASP A1066 -6.870 10.764 -2.893 1.00 69.80 C ANISOU 2066 CA ASP A1066 6410 12540 7569 -1161 -1963 -2290 C ATOM 2067 C ASP A1066 -6.451 10.104 -4.201 1.00 64.47 C ANISOU 2067 C ASP A1066 5695 11607 7194 -1177 -1917 -2075 C ATOM 2068 O ASP A1066 -6.572 10.712 -5.271 1.00 62.09 O ANISOU 2068 O ASP A1066 5387 11081 7123 -1183 -1817 -2103 O ATOM 2069 CB ASP A1066 -5.686 11.489 -2.250 1.00 72.78 C ANISOU 2069 CB ASP A1066 6823 12850 7979 -1167 -2160 -2414 C ATOM 2070 CG ASP A1066 -5.015 12.469 -3.192 1.00 81.35 C ANISOU 2070 CG ASP A1066 7891 13622 9395 -1199 -2170 -2470 C ATOM 2071 OD1 ASP A1066 -5.726 13.310 -3.781 1.00 91.41 O ANISOU 2071 OD1 ASP A1066 9179 14793 10760 -1191 -2054 -2584 O ATOM 2072 OD2 ASP A1066 -3.776 12.407 -3.335 1.00 84.16 O ANISOU 2072 OD2 ASP A1066 8218 13841 9916 -1238 -2302 -2395 O ATOM 2073 N ILE A1067 -5.963 8.864 -4.139 1.00 72.53 N ANISOU 2073 N ILE A1067 6701 12648 8209 -1178 -2000 -1861 N ATOM 2074 CA ILE A1067 -5.644 8.128 -5.358 1.00 73.41 C ANISOU 2074 CA ILE A1067 6776 12532 8584 -1166 -1956 -1670 C ATOM 2075 C ILE A1067 -6.893 7.467 -5.931 1.00 63.61 C ANISOU 2075 C ILE A1067 5536 11320 7315 -1150 -1800 -1551 C ATOM 2076 O ILE A1067 -7.050 7.378 -7.156 1.00 76.32 O ANISOU 2076 O ILE A1067 7138 12713 9147 -1131 -1697 -1478 O ATOM 2077 CB ILE A1067 -4.538 7.094 -5.078 1.00 76.91 C ANISOU 2077 CB ILE A1067 7203 12944 9077 -1153 -2145 -1516 C ATOM 2078 CG1 ILE A1067 -3.264 7.788 -4.585 1.00 78.36 C ANISOU 2078 CG1 ILE A1067 7370 13078 9324 -1176 -2307 -1632 C ATOM 2079 CG2 ILE A1067 -4.251 6.254 -6.316 1.00 74.69 C ANISOU 2079 CG2 ILE A1067 6882 12445 9052 -1116 -2103 -1340 C ATOM 2080 CD1 ILE A1067 -2.618 8.701 -5.609 1.00 75.19 C ANISOU 2080 CD1 ILE A1067 6917 12454 9199 -1208 -2240 -1694 C ATOM 2081 N LEU A1068 -7.801 7.014 -5.064 1.00 60.98 N ANISOU 2081 N LEU A1068 5209 11263 6697 -1165 -1782 -1524 N ATOM 2082 CA LEU A1068 -8.998 6.316 -5.520 1.00 59.76 C ANISOU 2082 CA LEU A1068 5036 11158 6512 -1168 -1651 -1385 C ATOM 2083 C LEU A1068 -9.851 7.211 -6.411 1.00 51.02 C ANISOU 2083 C LEU A1068 3920 9921 5545 -1151 -1471 -1521 C ATOM 2084 O LEU A1068 -10.282 6.798 -7.495 1.00 48.81 O ANISOU 2084 O LEU A1068 3643 9447 5457 -1127 -1386 -1400 O ATOM 2085 CB LEU A1068 -9.802 5.828 -4.314 1.00 56.17 C ANISOU 2085 CB LEU A1068 4574 11086 5681 -1221 -1657 -1335 C ATOM 2086 CG LEU A1068 -10.746 4.645 -4.529 1.00 54.26 C ANISOU 2086 CG LEU A1068 4307 10929 5381 -1256 -1604 -1076 C ATOM 2087 CD1 LEU A1068 -9.956 3.355 -4.680 1.00 57.42 C ANISOU 2087 CD1 LEU A1068 4749 11175 5894 -1239 -1781 -816 C ATOM 2088 CD2 LEU A1068 -11.733 4.541 -3.382 1.00 56.67 C ANISOU 2088 CD2 LEU A1068 4581 11673 5278 -1341 -1550 -1066 C ATOM 2089 N VAL A1069 -10.103 8.447 -5.971 1.00 56.03 N ANISOU 2089 N VAL A1069 4557 10637 6095 -1153 -1432 -1780 N ATOM 2090 CA VAL A1069 -10.893 9.370 -6.782 1.00 56.65 C ANISOU 2090 CA VAL A1069 4642 10559 6323 -1129 -1296 -1927 C ATOM 2091 C VAL A1069 -10.170 9.697 -8.081 1.00 54.02 C ANISOU 2091 C VAL A1069 4356 9854 6315 -1122 -1297 -1867 C ATOM 2092 O VAL A1069 -10.810 9.952 -9.110 1.00 50.66 O ANISOU 2092 O VAL A1069 3958 9236 6054 -1105 -1194 -1859 O ATOM 2093 CB VAL A1069 -11.230 10.647 -5.982 1.00 52.78 C ANISOU 2093 CB VAL A1069 4155 10209 5691 -1112 -1293 -2238 C ATOM 2094 CG1 VAL A1069 -11.992 10.292 -4.714 1.00 55.80 C ANISOU 2094 CG1 VAL A1069 4483 11018 5700 -1120 -1268 -2301 C ATOM 2095 CG2 VAL A1069 -9.970 11.432 -5.650 1.00 54.17 C ANISOU 2095 CG2 VAL A1069 4378 10273 5932 -1119 -1441 -2343 C ATOM 2096 N GLY A1070 -8.835 9.686 -8.065 1.00 49.26 N ANISOU 2096 N GLY A1070 3759 9159 5800 -1140 -1416 -1821 N ATOM 2097 CA GLY A1070 -8.093 9.910 -9.293 1.00 52.31 C ANISOU 2097 CA GLY A1070 4165 9256 6454 -1151 -1404 -1744 C ATOM 2098 C GLY A1070 -8.285 8.788 -10.293 1.00 51.27 C ANISOU 2098 C GLY A1070 4034 9003 6443 -1115 -1344 -1523 C ATOM 2099 O GLY A1070 -8.456 9.033 -11.492 1.00 59.78 O ANISOU 2099 O GLY A1070 5149 9873 7692 -1111 -1260 -1483 O ATOM 2100 N GLN A1071 -8.260 7.541 -9.817 1.00 48.18 N ANISOU 2100 N GLN A1071 3613 8732 5961 -1088 -1407 -1375 N ATOM 2101 CA GLN A1071 -8.533 6.416 -10.703 1.00 46.48 C ANISOU 2101 CA GLN A1071 3406 8388 5866 -1039 -1378 -1174 C ATOM 2102 C GLN A1071 -9.977 6.432 -11.185 1.00 47.38 C ANISOU 2102 C GLN A1071 3550 8472 5979 -1024 -1247 -1161 C ATOM 2103 O GLN A1071 -10.249 6.055 -12.331 1.00 49.51 O ANISOU 2103 O GLN A1071 3855 8540 6418 -984 -1193 -1054 O ATOM 2104 CB GLN A1071 -8.216 5.101 -9.996 1.00 45.22 C ANISOU 2104 CB GLN A1071 3220 8346 5616 -1016 -1515 -1020 C ATOM 2105 CG GLN A1071 -6.787 4.989 -9.513 1.00 46.78 C ANISOU 2105 CG GLN A1071 3385 8553 5838 -1019 -1673 -1032 C ATOM 2106 CD GLN A1071 -6.492 3.637 -8.898 1.00 63.24 C ANISOU 2106 CD GLN A1071 5463 10705 7861 -986 -1843 -874 C ATOM 2107 OE1 GLN A1071 -6.081 2.704 -9.589 1.00 62.40 O ANISOU 2107 OE1 GLN A1071 5349 10434 7926 -922 -1907 -748 O ATOM 2108 NE2 GLN A1071 -6.711 3.519 -7.593 1.00 68.74 N ANISOU 2108 NE2 GLN A1071 6173 11646 8300 -1028 -1930 -883 N ATOM 2109 N ILE A1072 -10.910 6.862 -10.330 1.00 54.35 N ANISOU 2109 N ILE A1072 4411 9565 6673 -1052 -1198 -1279 N ATOM 2110 CA ILE A1072 -12.294 7.021 -10.765 1.00 42.78 C ANISOU 2110 CA ILE A1072 2952 8073 5228 -1039 -1071 -1302 C ATOM 2111 C ILE A1072 -12.392 8.075 -11.860 1.00 58.76 C ANISOU 2111 C ILE A1072 5044 9833 7450 -1025 -1002 -1413 C ATOM 2112 O ILE A1072 -13.214 7.956 -12.777 1.00 55.25 O ANISOU 2112 O ILE A1072 4637 9222 7132 -993 -929 -1356 O ATOM 2113 CB ILE A1072 -13.201 7.362 -9.565 1.00 47.64 C ANISOU 2113 CB ILE A1072 3498 9020 5582 -1074 -1026 -1447 C ATOM 2114 CG1 ILE A1072 -13.256 6.194 -8.581 1.00 46.17 C ANISOU 2114 CG1 ILE A1072 3255 9121 5167 -1116 -1092 -1272 C ATOM 2115 CG2 ILE A1072 -14.602 7.718 -10.028 1.00 43.87 C ANISOU 2115 CG2 ILE A1072 3004 8506 5161 -1054 -893 -1525 C ATOM 2116 CD1 ILE A1072 -14.129 6.458 -7.366 1.00 48.49 C ANISOU 2116 CD1 ILE A1072 3462 9822 5140 -1172 -1035 -1394 C ATOM 2117 N ASP A1073 -11.551 9.112 -11.799 1.00 49.39 N ANISOU 2117 N ASP A1073 3880 8591 6294 -1055 -1041 -1556 N ATOM 2118 CA ASP A1073 -11.538 10.110 -12.865 1.00 44.63 C ANISOU 2118 CA ASP A1073 3352 7736 5870 -1065 -1001 -1624 C ATOM 2119 C ASP A1073 -10.936 9.544 -14.145 1.00 46.39 C ANISOU 2119 C ASP A1073 3611 7754 6261 -1058 -992 -1434 C ATOM 2120 O ASP A1073 -11.430 9.821 -15.246 1.00 38.37 O ANISOU 2120 O ASP A1073 2665 6547 5367 -1050 -932 -1408 O ATOM 2121 CB ASP A1073 -10.772 11.353 -12.417 1.00 42.73 C ANISOU 2121 CB ASP A1073 3120 7492 5623 -1116 -1070 -1802 C ATOM 2122 CG ASP A1073 -11.523 12.154 -11.374 1.00 53.57 C ANISOU 2122 CG ASP A1073 4476 9026 6853 -1101 -1075 -2043 C ATOM 2123 OD1 ASP A1073 -12.592 11.691 -10.922 1.00 55.99 O ANISOU 2123 OD1 ASP A1073 4736 9499 7037 -1062 -1009 -2074 O ATOM 2124 OD2 ASP A1073 -11.047 13.251 -11.011 1.00 56.63 O ANISOU 2124 OD2 ASP A1073 4887 9380 7250 -1128 -1149 -2206 O ATOM 2125 N ASP A1074 -9.865 8.754 -14.022 1.00 50.12 N ANISOU 2125 N ASP A1074 4036 8273 6737 -1055 -1059 -1315 N ATOM 2126 CA ASP A1074 -9.266 8.135 -15.199 1.00 51.99 C ANISOU 2126 CA ASP A1074 4282 8359 7115 -1032 -1047 -1162 C ATOM 2127 C ASP A1074 -10.256 7.211 -15.895 1.00 43.84 C ANISOU 2127 C ASP A1074 3287 7238 6131 -962 -1002 -1027 C ATOM 2128 O ASP A1074 -10.381 7.234 -17.125 1.00 50.40 O ANISOU 2128 O ASP A1074 4170 7907 7071 -948 -950 -971 O ATOM 2129 CB ASP A1074 -7.999 7.373 -14.807 1.00 62.80 C ANISOU 2129 CB ASP A1074 5572 9808 8482 -1021 -1144 -1086 C ATOM 2130 CG ASP A1074 -6.895 8.291 -14.304 1.00 80.36 C ANISOU 2130 CG ASP A1074 7750 12085 10699 -1094 -1201 -1203 C ATOM 2131 OD1 ASP A1074 -7.130 9.515 -14.213 1.00 88.08 O ANISOU 2131 OD1 ASP A1074 8764 13033 11668 -1154 -1177 -1340 O ATOM 2132 OD2 ASP A1074 -5.789 7.789 -14.003 1.00 84.69 O ANISOU 2132 OD2 ASP A1074 8223 12689 11265 -1089 -1289 -1160 O ATOM 2133 N ALA A1075 -10.980 6.398 -15.122 1.00 46.07 N ANISOU 2133 N ALA A1075 3541 7637 6326 -928 -1029 -969 N ATOM 2134 CA ALA A1075 -11.976 5.510 -15.707 1.00 49.93 C ANISOU 2134 CA ALA A1075 4056 8032 6882 -871 -1007 -830 C ATOM 2135 C ALA A1075 -13.229 6.254 -16.151 1.00 46.84 C ANISOU 2135 C ALA A1075 3719 7555 6524 -876 -912 -913 C ATOM 2136 O ALA A1075 -13.961 5.752 -17.009 1.00 33.49 O ANISOU 2136 O ALA A1075 2070 5721 4934 -831 -891 -807 O ATOM 2137 CB ALA A1075 -12.346 4.406 -14.714 1.00 36.62 C ANISOU 2137 CB ALA A1075 2312 6506 5097 -855 -1080 -726 C ATOM 2138 N LEU A1076 -13.493 7.436 -15.589 1.00 46.38 N ANISOU 2138 N LEU A1076 3660 7572 6392 -920 -872 -1112 N ATOM 2139 CA LEU A1076 -14.670 8.203 -15.983 1.00 49.97 C ANISOU 2139 CA LEU A1076 4160 7927 6898 -911 -801 -1227 C ATOM 2140 C LEU A1076 -14.443 8.905 -17.315 1.00 59.86 C ANISOU 2140 C LEU A1076 5521 8931 8293 -920 -785 -1240 C ATOM 2141 O LEU A1076 -15.309 8.874 -18.196 1.00 63.08 O ANISOU 2141 O LEU A1076 5995 9176 8798 -885 -753 -1209 O ATOM 2142 CB LEU A1076 -15.034 9.214 -14.894 1.00 48.40 C ANISOU 2142 CB LEU A1076 3916 7899 6577 -939 -784 -1468 C ATOM 2143 CG LEU A1076 -16.374 9.929 -15.076 1.00 51.41 C ANISOU 2143 CG LEU A1076 4312 8211 7011 -907 -723 -1627 C ATOM 2144 CD1 LEU A1076 -17.516 8.928 -15.123 1.00 37.75 C ANISOU 2144 CD1 LEU A1076 2528 6521 5295 -869 -674 -1502 C ATOM 2145 CD2 LEU A1076 -16.598 10.947 -13.967 1.00 66.43 C ANISOU 2145 CD2 LEU A1076 6153 10302 8786 -917 -722 -1906 C ATOM 2146 N LYS A1077 -13.285 9.549 -17.479 1.00 62.43 N ANISOU 2146 N LYS A1077 5862 9233 8628 -976 -814 -1281 N ATOM 2147 CA LYS A1077 -12.926 10.059 -18.797 1.00 70.01 C ANISOU 2147 CA LYS A1077 6907 9995 9697 -1010 -799 -1253 C ATOM 2148 C LYS A1077 -12.724 8.921 -19.788 1.00 63.84 C ANISOU 2148 C LYS A1077 6133 9155 8969 -962 -785 -1070 C ATOM 2149 O LYS A1077 -13.005 9.079 -20.982 1.00 63.33 O ANISOU 2149 O LYS A1077 6149 8932 8980 -961 -756 -1045 O ATOM 2150 CB LYS A1077 -11.668 10.925 -18.710 1.00 77.22 C ANISOU 2150 CB LYS A1077 7804 10924 10611 -1101 -835 -1314 C ATOM 2151 CG LYS A1077 -11.876 12.247 -17.988 1.00 82.77 C ANISOU 2151 CG LYS A1077 8530 11627 11290 -1150 -874 -1507 C ATOM 2152 CD LYS A1077 -10.716 13.202 -18.233 1.00 85.79 C ANISOU 2152 CD LYS A1077 8922 11955 11719 -1262 -928 -1531 C ATOM 2153 CE LYS A1077 -10.981 14.566 -17.611 1.00 84.08 C ANISOU 2153 CE LYS A1077 8753 11693 11500 -1303 -999 -1716 C ATOM 2154 NZ LYS A1077 -9.896 15.537 -17.920 1.00 80.65 N ANISOU 2154 NZ LYS A1077 8338 11176 11128 -1436 -1075 -1710 N ATOM 2155 N LEU A1078 -12.245 7.768 -19.312 1.00 59.82 N ANISOU 2155 N LEU A1078 5543 8765 8420 -918 -821 -953 N ATOM 2156 CA LEU A1078 -12.151 6.583 -20.156 1.00 47.35 C ANISOU 2156 CA LEU A1078 3964 7134 6893 -850 -832 -791 C ATOM 2157 C LEU A1078 -13.523 6.046 -20.541 1.00 54.43 C ANISOU 2157 C LEU A1078 4916 7940 7826 -789 -819 -723 C ATOM 2158 O LEU A1078 -13.637 5.324 -21.537 1.00 65.94 O ANISOU 2158 O LEU A1078 6408 9316 9331 -733 -821 -628 O ATOM 2159 CB LEU A1078 -11.339 5.501 -19.439 1.00 44.89 C ANISOU 2159 CB LEU A1078 3559 6949 6548 -812 -910 -691 C ATOM 2160 CG LEU A1078 -10.903 4.269 -20.232 1.00 43.23 C ANISOU 2160 CG LEU A1078 3330 6704 6393 -735 -951 -546 C ATOM 2161 CD1 LEU A1078 -10.053 4.676 -21.424 1.00 42.46 C ANISOU 2161 CD1 LEU A1078 3231 6564 6338 -749 -892 -597 C ATOM 2162 CD2 LEU A1078 -10.146 3.301 -19.337 1.00 42.43 C ANISOU 2162 CD2 LEU A1078 3143 6704 6275 -701 -1065 -470 C ATOM 2163 N ALA A1079 -14.566 6.388 -19.782 1.00 52.52 N ANISOU 2163 N ALA A1079 4669 7726 7558 -795 -805 -789 N ATOM 2164 CA ALA A1079 -15.924 5.958 -20.083 1.00 43.52 C ANISOU 2164 CA ALA A1079 3561 6505 6470 -745 -790 -736 C ATOM 2165 C ALA A1079 -16.731 6.991 -20.857 1.00 51.46 C ANISOU 2165 C ALA A1079 4668 7332 7553 -744 -741 -875 C ATOM 2166 O ALA A1079 -17.752 6.633 -21.455 1.00 48.26 O ANISOU 2166 O ALA A1079 4311 6801 7225 -686 -735 -838 O ATOM 2167 CB ALA A1079 -16.670 5.610 -18.789 1.00 37.85 C ANISOU 2167 CB ALA A1079 2745 5944 5693 -750 -798 -727 C ATOM 2168 N ASN A1080 -16.307 8.258 -20.859 1.00 54.51 N ANISOU 2168 N ASN A1080 5092 7683 7934 -802 -725 -1033 N ATOM 2169 CA ASN A1080 -17.036 9.283 -21.598 1.00 54.17 C ANISOU 2169 CA ASN A1080 5162 7437 7985 -801 -712 -1158 C ATOM 2170 C ASN A1080 -16.913 9.114 -23.105 1.00 52.41 C ANISOU 2170 C ASN A1080 5049 7020 7843 -784 -713 -1086 C ATOM 2171 O ASN A1080 -17.734 9.668 -23.843 1.00 62.90 O ANISOU 2171 O ASN A1080 6489 8145 9267 -754 -719 -1146 O ATOM 2172 CB ASN A1080 -16.553 10.675 -21.193 1.00 57.93 C ANISOU 2172 CB ASN A1080 5657 7916 8436 -876 -725 -1322 C ATOM 2173 CG ASN A1080 -17.163 11.143 -19.888 1.00 63.04 C ANISOU 2173 CG ASN A1080 6224 8699 9030 -861 -723 -1486 C ATOM 2174 OD1 ASN A1080 -18.338 10.894 -19.615 1.00 56.50 O ANISOU 2174 OD1 ASN A1080 5359 7877 8230 -797 -699 -1532 O ATOM 2175 ND2 ASN A1080 -16.366 11.824 -19.071 1.00 72.11 N ANISOU 2175 ND2 ASN A1080 7330 9970 10100 -919 -749 -1589 N ATOM 2176 N GLU A1081 -15.914 8.370 -23.579 1.00 85.73 N ANISOU 2176 N GLU A1081 8853 15854 7866 -4418 1262 77 N ATOM 2177 CA GLU A1081 -15.775 8.075 -24.998 1.00 85.28 C ANISOU 2177 CA GLU A1081 8788 15898 7717 -4435 1408 26 C ATOM 2178 C GLU A1081 -16.122 6.625 -25.318 1.00 80.31 C ANISOU 2178 C GLU A1081 8067 15309 7138 -4219 1494 -93 C ATOM 2179 O GLU A1081 -15.960 6.190 -26.463 1.00 89.11 O ANISOU 2179 O GLU A1081 9159 16514 8184 -4208 1631 -154 O ATOM 2180 CB GLU A1081 -14.360 8.423 -25.472 1.00100.82 C ANISOU 2180 CB GLU A1081 10587 18058 9664 -4568 1527 30 C ATOM 2181 CG GLU A1081 -14.195 8.545 -26.991 1.00110.74 C ANISOU 2181 CG GLU A1081 11889 19399 10789 -4656 1668 11 C ATOM 2182 CD GLU A1081 -15.387 9.201 -27.671 1.00109.18 C ANISOU 2182 CD GLU A1081 11982 19037 10463 -4729 1598 68 C ATOM 2183 OE1 GLU A1081 -15.765 10.325 -27.276 1.00109.80 O ANISOU 2183 OE1 GLU A1081 12231 18983 10507 -4857 1471 171 O ATOM 2184 OE2 GLU A1081 -15.951 8.586 -28.602 1.00105.03 O ANISOU 2184 OE2 GLU A1081 11519 18511 9878 -4655 1669 11 O ATOM 2185 N GLY A1082 -16.600 5.868 -24.334 1.00 75.76 N ANISOU 2185 N GLY A1082 7447 14663 6674 -4049 1420 -130 N ATOM 2186 CA GLY A1082 -17.191 4.572 -24.598 1.00 67.69 C ANISOU 2186 CA GLY A1082 6396 13634 5688 -3850 1477 -236 C ATOM 2187 C GLY A1082 -16.267 3.380 -24.528 1.00 74.54 C ANISOU 2187 C GLY A1082 7001 14655 6666 -3692 1608 -344 C ATOM 2188 O GLY A1082 -16.602 2.327 -25.081 1.00 77.75 O ANISOU 2188 O GLY A1082 7391 15076 7074 -3546 1699 -445 O ATOM 2189 N LYS A1083 -15.115 3.501 -23.874 1.00 70.44 N ANISOU 2189 N LYS A1083 6277 14246 6241 -3711 1621 -324 N ATOM 2190 CA LYS A1083 -14.267 2.338 -23.617 1.00 71.59 C ANISOU 2190 CA LYS A1083 6157 14519 6526 -3532 1725 -414 C ATOM 2191 C LYS A1083 -14.826 1.633 -22.388 1.00 78.82 C ANISOU 2191 C LYS A1083 7047 15330 7572 -3357 1609 -434 C ATOM 2192 O LYS A1083 -14.406 1.876 -21.255 1.00 80.42 O ANISOU 2192 O LYS A1083 7156 15527 7874 -3361 1508 -379 O ATOM 2193 CB LYS A1083 -12.813 2.747 -23.428 1.00 80.52 C ANISOU 2193 CB LYS A1083 7067 15813 7715 -3622 1779 -375 C ATOM 2194 CG LYS A1083 -12.007 2.783 -24.718 1.00 77.40 C ANISOU 2194 CG LYS A1083 6592 15574 7243 -3696 1968 -409 C ATOM 2195 CD LYS A1083 -12.313 4.014 -25.551 1.00 77.92 C ANISOU 2195 CD LYS A1083 6872 15604 7129 -3932 1953 -335 C ATOM 2196 CE LYS A1083 -11.789 5.273 -24.886 1.00 78.50 C ANISOU 2196 CE LYS A1083 6952 15680 7196 -4131 1843 -216 C ATOM 2197 NZ LYS A1083 -11.794 6.428 -25.822 1.00 86.04 N ANISOU 2197 NZ LYS A1083 8071 16634 7985 -4362 1865 -149 N ATOM 2198 N VAL A1084 -15.792 0.744 -22.622 1.00 67.43 N ANISOU 2198 N VAL A1084 5694 13802 6124 -3207 1623 -513 N ATOM 2199 CA VAL A1084 -16.540 0.140 -21.522 1.00 74.41 C ANISOU 2199 CA VAL A1084 6599 14565 7110 -3056 1505 -527 C ATOM 2200 C VAL A1084 -15.670 -0.857 -20.763 1.00 85.64 C ANISOU 2200 C VAL A1084 7757 16071 8711 -2873 1542 -583 C ATOM 2201 O VAL A1084 -15.460 -0.729 -19.550 1.00 91.31 O ANISOU 2201 O VAL A1084 8402 16755 9535 -2850 1422 -529 O ATOM 2202 CB VAL A1084 -17.826 -0.520 -22.048 1.00 63.01 C ANISOU 2202 CB VAL A1084 5330 13010 5603 -2959 1512 -595 C ATOM 2203 CG1 VAL A1084 -18.699 -0.982 -20.891 1.00 60.26 C ANISOU 2203 CG1 VAL A1084 5026 12524 5345 -2832 1379 -594 C ATOM 2204 CG2 VAL A1084 -18.586 0.441 -22.950 1.00 62.71 C ANISOU 2204 CG2 VAL A1084 5533 12902 5393 -3135 1485 -533 C ATOM 2205 N LYS A1085 -15.150 -1.865 -21.469 1.00 83.41 N ANISOU 2205 N LYS A1085 7336 15891 8467 -2736 1709 -689 N ATOM 2206 CA LYS A1085 -14.375 -2.910 -20.804 1.00 90.90 C ANISOU 2206 CA LYS A1085 8035 16904 9597 -2532 1750 -743 C ATOM 2207 C LYS A1085 -13.065 -2.374 -20.234 1.00 87.20 C ANISOU 2207 C LYS A1085 7352 16561 9220 -2608 1731 -665 C ATOM 2208 O LYS A1085 -12.616 -2.838 -19.177 1.00 90.71 O ANISOU 2208 O LYS A1085 7632 17010 9823 -2487 1662 -652 O ATOM 2209 CB LYS A1085 -14.118 -4.062 -21.775 1.00 96.86 C ANISOU 2209 CB LYS A1085 8711 17727 10365 -2369 1949 -873 C ATOM 2210 CG LYS A1085 -14.138 -3.658 -23.240 1.00 93.34 C ANISOU 2210 CG LYS A1085 8380 17337 9748 -2503 2084 -898 C ATOM 2211 CD LYS A1085 -14.135 -4.880 -24.145 1.00 93.00 C ANISOU 2211 CD LYS A1085 8315 17316 9703 -2329 2270 -1037 C ATOM 2212 CE LYS A1085 -15.342 -5.767 -23.875 1.00 84.47 C ANISOU 2212 CE LYS A1085 7380 16080 8633 -2174 2212 -1112 C ATOM 2213 NZ LYS A1085 -15.353 -6.975 -24.745 1.00 82.92 N ANISOU 2213 NZ LYS A1085 7188 15889 8430 -2006 2392 -1253 N ATOM 2214 N GLU A1086 -12.442 -1.404 -20.909 1.00 77.65 N ANISOU 2214 N GLU A1086 6142 15449 7911 -2809 1786 -610 N ATOM 2215 CA GLU A1086 -11.257 -0.763 -20.348 1.00 78.25 C ANISOU 2215 CA GLU A1086 6034 15638 8058 -2914 1752 -526 C ATOM 2216 C GLU A1086 -11.583 -0.081 -19.025 1.00 73.80 C ANISOU 2216 C GLU A1086 5545 14965 7529 -2989 1539 -428 C ATOM 2217 O GLU A1086 -10.836 -0.210 -18.046 1.00 75.93 O ANISOU 2217 O GLU A1086 5633 15280 7936 -2945 1469 -389 O ATOM 2218 CB GLU A1086 -10.681 0.242 -21.344 1.00 84.16 C ANISOU 2218 CB GLU A1086 6810 16494 8673 -3139 1842 -482 C ATOM 2219 CG GLU A1086 -10.309 -0.358 -22.690 1.00 88.85 C ANISOU 2219 CG GLU A1086 7340 17198 9219 -3083 2064 -574 C ATOM 2220 CD GLU A1086 -9.608 0.635 -23.599 1.00 93.59 C ANISOU 2220 CD GLU A1086 7942 17919 9701 -3309 2154 -523 C ATOM 2221 OE1 GLU A1086 -9.197 1.709 -23.108 1.00 93.45 O ANISOU 2221 OE1 GLU A1086 7923 17919 9663 -3494 2052 -419 O ATOM 2222 OE2 GLU A1086 -9.471 0.343 -24.807 1.00 95.40 O ANISOU 2222 OE2 GLU A1086 8181 18216 9849 -3304 2327 -588 O ATOM 2223 N ALA A1087 -12.705 0.643 -18.977 1.00 70.13 N ANISOU 2223 N ALA A1087 5354 14349 6945 -3100 1433 -385 N ATOM 2224 CA ALA A1087 -13.149 1.241 -17.724 1.00 73.12 C ANISOU 2224 CA ALA A1087 5835 14596 7350 -3156 1240 -301 C ATOM 2225 C ALA A1087 -13.439 0.179 -16.672 1.00 72.75 C ANISOU 2225 C ALA A1087 5703 14481 7458 -2933 1166 -341 C ATOM 2226 O ALA A1087 -13.250 0.425 -15.475 1.00 85.61 O ANISOU 2226 O ALA A1087 7300 16061 9169 -2944 1029 -276 O ATOM 2227 CB ALA A1087 -14.387 2.105 -17.964 1.00 65.79 C ANISOU 2227 CB ALA A1087 5219 13507 6271 -3285 1161 -255 C ATOM 2228 N GLN A1088 -13.890 -1.005 -17.094 1.00 65.75 N ANISOU 2228 N GLN A1088 4789 13583 6610 -2734 1253 -447 N ATOM 2229 CA GLN A1088 -14.152 -2.073 -16.135 1.00 64.42 C ANISOU 2229 CA GLN A1088 4538 13346 6591 -2514 1188 -489 C ATOM 2230 C GLN A1088 -12.857 -2.608 -15.529 1.00 81.40 C ANISOU 2230 C GLN A1088 6396 15619 8913 -2409 1201 -482 C ATOM 2231 O GLN A1088 -12.782 -2.838 -14.313 1.00 80.95 O ANISOU 2231 O GLN A1088 6277 15505 8976 -2333 1069 -443 O ATOM 2232 CB GLN A1088 -14.951 -3.189 -16.806 1.00 63.43 C ANISOU 2232 CB GLN A1088 4471 13176 6455 -2335 1286 -609 C ATOM 2233 CG GLN A1088 -16.368 -2.770 -17.178 1.00 60.99 C ANISOU 2233 CG GLN A1088 4448 12725 6000 -2415 1237 -605 C ATOM 2234 CD GLN A1088 -17.138 -3.853 -17.913 1.00 60.27 C ANISOU 2234 CD GLN A1088 4420 12595 5883 -2259 1336 -726 C ATOM 2235 OE1 GLN A1088 -16.647 -4.433 -18.881 1.00 62.15 O ANISOU 2235 OE1 GLN A1088 4576 12932 6107 -2197 1499 -809 O ATOM 2236 NE2 GLN A1088 -18.355 -4.129 -17.455 1.00 57.65 N ANISOU 2236 NE2 GLN A1088 4244 12115 5544 -2197 1242 -737 N ATOM 2237 N ALA A1089 -11.824 -2.806 -16.352 1.00 72.74 N ANISOU 2237 N ALA A1089 5115 14689 7833 -2404 1359 -515 N ATOM 2238 CA ALA A1089 -10.530 -3.216 -15.812 1.00 78.68 C ANISOU 2238 CA ALA A1089 5574 15568 8751 -2318 1372 -493 C ATOM 2239 C ALA A1089 -9.955 -2.144 -14.892 1.00 81.67 C ANISOU 2239 C ALA A1089 5923 15966 9142 -2503 1221 -368 C ATOM 2240 O ALA A1089 -9.411 -2.452 -13.820 1.00 89.53 O ANISOU 2240 O ALA A1089 6763 16971 10283 -2424 1119 -327 O ATOM 2241 CB ALA A1089 -9.559 -3.529 -16.950 1.00 82.26 C ANISOU 2241 CB ALA A1089 5848 16197 9210 -2295 1584 -545 C ATOM 2242 N ALA A1090 -10.070 -0.874 -15.296 1.00 76.00 N ANISOU 2242 N ALA A1090 5362 15248 8268 -2753 1203 -307 N ATOM 2243 CA ALA A1090 -9.675 0.221 -14.417 1.00 80.28 C ANISOU 2243 CA ALA A1090 5930 15777 8797 -2945 1055 -193 C ATOM 2244 C ALA A1090 -10.407 0.142 -13.082 1.00 78.88 C ANISOU 2244 C ALA A1090 5868 15428 8676 -2885 868 -157 C ATOM 2245 O ALA A1090 -9.820 0.403 -12.024 1.00 88.36 O ANISOU 2245 O ALA A1090 6980 16636 9958 -2924 745 -87 O ATOM 2246 CB ALA A1090 -9.940 1.563 -15.100 1.00 72.70 C ANISOU 2246 CB ALA A1090 5179 14799 7646 -3206 1064 -141 C ATOM 2247 N ALA A1091 -11.690 -0.231 -13.112 1.00 69.00 N ANISOU 2247 N ALA A1091 4813 14022 7382 -2792 844 -204 N ATOM 2248 CA ALA A1091 -12.434 -0.429 -11.874 1.00 64.88 C ANISOU 2248 CA ALA A1091 4396 13333 6922 -2714 681 -179 C ATOM 2249 C ALA A1091 -11.911 -1.626 -11.091 1.00 75.03 C ANISOU 2249 C ALA A1091 5456 14652 8401 -2487 649 -209 C ATOM 2250 O ALA A1091 -12.051 -1.669 -9.863 1.00 82.79 O ANISOU 2250 O ALA A1091 6461 15537 9460 -2453 496 -162 O ATOM 2251 CB ALA A1091 -13.923 -0.600 -12.174 1.00 63.59 C ANISOU 2251 CB ALA A1091 4479 13009 6672 -2664 677 -224 C ATOM 2252 N GLU A1092 -11.313 -2.606 -11.773 1.00 67.20 N ANISOU 2252 N GLU A1092 4256 13786 7490 -2327 794 -286 N ATOM 2253 CA GLU A1092 -10.708 -3.725 -11.056 1.00 77.40 C ANISOU 2253 CA GLU A1092 5319 15112 8976 -2106 768 -305 C ATOM 2254 C GLU A1092 -9.467 -3.278 -10.288 1.00 72.34 C ANISOU 2254 C GLU A1092 4483 14578 8426 -2192 683 -211 C ATOM 2255 O GLU A1092 -9.295 -3.622 -9.111 1.00 70.24 O ANISOU 2255 O GLU A1092 4149 14259 8279 -2108 541 -169 O ATOM 2256 CB GLU A1092 -10.374 -4.857 -12.028 1.00 78.31 C ANISOU 2256 CB GLU A1092 5274 15325 9154 -1909 960 -410 C ATOM 2257 CG GLU A1092 -11.598 -5.561 -12.592 1.00 79.96 C ANISOU 2257 CG GLU A1092 5660 15417 9303 -1782 1026 -514 C ATOM 2258 CD GLU A1092 -12.414 -6.260 -11.519 1.00 87.95 C ANISOU 2258 CD GLU A1092 6747 16266 10401 -1622 888 -523 C ATOM 2259 OE1 GLU A1092 -11.812 -6.789 -10.560 1.00 92.30 O ANISOU 2259 OE1 GLU A1092 7134 16824 11112 -1499 802 -488 O ATOM 2260 OE2 GLU A1092 -13.659 -6.277 -11.631 1.00 88.34 O ANISOU 2260 OE2 GLU A1092 7021 16183 10362 -1623 861 -561 O ATOM 2261 N GLN A1093 -8.590 -2.503 -10.935 1.00 72.85 N ANISOU 2261 N GLN A1093 4456 14792 8430 -2366 763 -176 N ATOM 2262 CA GLN A1093 -7.444 -1.953 -10.210 1.00 78.92 C ANISOU 2262 CA GLN A1093 5054 15666 9267 -2482 673 -82 C ATOM 2263 C GLN A1093 -7.902 -1.051 -9.066 1.00 83.23 C ANISOU 2263 C GLN A1093 5795 16073 9757 -2637 470 4 C ATOM 2264 O GLN A1093 -7.317 -1.061 -7.970 1.00 98.73 O ANISOU 2264 O GLN A1093 7649 18045 11820 -2635 335 67 O ATOM 2265 CB GLN A1093 -6.533 -1.194 -11.173 1.00 77.87 C ANISOU 2265 CB GLN A1093 4819 15710 9057 -2665 799 -61 C ATOM 2266 CG GLN A1093 -5.970 -2.060 -12.288 1.00 86.69 C ANISOU 2266 CG GLN A1093 5733 16970 10234 -2515 1014 -143 C ATOM 2267 CD GLN A1093 -5.238 -3.280 -11.761 1.00 95.18 C ANISOU 2267 CD GLN A1093 6525 18109 11529 -2264 1021 -161 C ATOM 2268 OE1 GLN A1093 -4.496 -3.199 -10.782 1.00 96.75 O ANISOU 2268 OE1 GLN A1093 6567 18354 11839 -2277 895 -85 O ATOM 2269 NE2 GLN A1093 -5.453 -4.423 -12.404 1.00 97.14 N ANISOU 2269 NE2 GLN A1093 6716 18355 11839 -2033 1167 -261 N ATOM 2270 N LEU A1094 -8.953 -0.265 -9.312 1.00 80.70 N ANISOU 2270 N LEU A1094 5770 15617 9274 -2770 450 7 N ATOM 2271 CA LEU A1094 -9.619 0.472 -8.245 1.00 75.33 C ANISOU 2271 CA LEU A1094 5316 14765 8542 -2879 276 74 C ATOM 2272 C LEU A1094 -9.967 -0.450 -7.081 1.00 67.66 C ANISOU 2272 C LEU A1094 4319 13682 7707 -2682 151 66 C ATOM 2273 O LEU A1094 -9.734 -0.114 -5.912 1.00 72.23 O ANISOU 2273 O LEU A1094 4914 14204 8324 -2739 -3 134 O ATOM 2274 CB LEU A1094 -10.877 1.135 -8.807 1.00 66.63 C ANISOU 2274 CB LEU A1094 4525 13518 7272 -2977 299 60 C ATOM 2275 CG LEU A1094 -11.577 2.263 -8.057 1.00 64.93 C ANISOU 2275 CG LEU A1094 4589 13129 6953 -3149 164 134 C ATOM 2276 CD1 LEU A1094 -10.766 3.535 -8.137 1.00 67.02 C ANISOU 2276 CD1 LEU A1094 4865 13473 7127 -3408 151 212 C ATOM 2277 CD2 LEU A1094 -12.952 2.474 -8.652 1.00 63.50 C ANISOU 2277 CD2 LEU A1094 4673 12801 6654 -3152 201 103 C ATOM 2278 N LYS A1095 -10.506 -1.634 -7.390 1.00 66.53 N ANISOU 2278 N LYS A1095 4139 13505 7635 -2449 217 -19 N ATOM 2279 CA LYS A1095 -10.833 -2.596 -6.343 1.00 65.32 C ANISOU 2279 CA LYS A1095 3958 13246 7616 -2248 105 -30 C ATOM 2280 C LYS A1095 -9.582 -3.129 -5.655 1.00 67.89 C ANISOU 2280 C LYS A1095 3998 13691 8108 -2161 49 9 C ATOM 2281 O LYS A1095 -9.652 -3.557 -4.497 1.00 80.10 O ANISOU 2281 O LYS A1095 5537 15148 9750 -2068 -96 39 O ATOM 2282 CB LYS A1095 -11.658 -3.748 -6.921 1.00 67.70 C ANISOU 2282 CB LYS A1095 4283 13492 7950 -2023 201 -135 C ATOM 2283 CG LYS A1095 -12.151 -4.745 -5.881 1.00 66.10 C ANISOU 2283 CG LYS A1095 4087 13157 7871 -1816 86 -149 C ATOM 2284 CD LYS A1095 -13.111 -5.763 -6.478 1.00 65.84 C ANISOU 2284 CD LYS A1095 4122 13052 7843 -1622 179 -255 C ATOM 2285 CE LYS A1095 -13.662 -6.691 -5.403 1.00 64.98 C ANISOU 2285 CE LYS A1095 4043 12798 7848 -1430 55 -264 C ATOM 2286 NZ LYS A1095 -14.733 -7.586 -5.923 1.00 60.51 N ANISOU 2286 NZ LYS A1095 3579 12143 7267 -1265 131 -367 N ATOM 2287 N THR A1096 -8.432 -3.117 -6.335 1.00 70.87 N ANISOU 2287 N THR A1096 4138 14268 8522 -2189 159 11 N ATOM 2288 CA THR A1096 -7.195 -3.512 -5.665 1.00 73.60 C ANISOU 2288 CA THR A1096 4203 14736 9027 -2126 97 62 C ATOM 2289 C THR A1096 -6.787 -2.480 -4.618 1.00 74.15 C ANISOU 2289 C THR A1096 4323 14791 9060 -2339 -77 166 C ATOM 2290 O THR A1096 -6.535 -2.827 -3.454 1.00 85.20 O ANISOU 2290 O THR A1096 5661 16148 10564 -2272 -230 211 O ATOM 2291 CB THR A1096 -6.072 -3.717 -6.684 1.00 85.78 C ANISOU 2291 CB THR A1096 5475 16498 10620 -2108 270 40 C ATOM 2292 OG1 THR A1096 -5.729 -2.463 -7.286 1.00 87.92 O ANISOU 2292 OG1 THR A1096 5802 16857 10746 -2378 319 79 O ATOM 2293 CG2 THR A1096 -6.503 -4.697 -7.767 1.00 80.20 C ANISOU 2293 CG2 THR A1096 4747 15795 9930 -1907 458 -72 C ATOM 2294 N THR A1097 -6.718 -1.202 -5.012 1.00 74.45 N ANISOU 2294 N THR A1097 4486 14859 8945 -2600 -57 205 N ATOM 2295 CA THR A1097 -6.401 -0.146 -4.049 1.00 81.67 C ANISOU 2295 CA THR A1097 5485 15744 9802 -2818 -213 298 C ATOM 2296 C THR A1097 -7.362 -0.182 -2.863 1.00 82.22 C ANISOU 2296 C THR A1097 5784 15592 9864 -2780 -376 315 C ATOM 2297 O THR A1097 -6.947 -0.187 -1.687 1.00 72.98 O ANISOU 2297 O THR A1097 4568 14401 8759 -2793 -532 372 O ATOM 2298 CB THR A1097 -6.455 1.220 -4.736 1.00 75.20 C ANISOU 2298 CB THR A1097 4829 14944 8798 -3092 -155 326 C ATOM 2299 OG1 THR A1097 -5.693 1.180 -5.950 1.00 77.50 O ANISOU 2299 OG1 THR A1097 4930 15430 9088 -3114 16 299 O ATOM 2300 CG2 THR A1097 -5.892 2.300 -3.823 1.00 76.47 C ANISOU 2300 CG2 THR A1097 5040 15109 8905 -3325 -296 421 C ATOM 2301 N ARG A1098 -8.664 -0.205 -3.166 1.00 78.48 N ANISOU 2301 N ARG A1098 5560 14953 9308 -2736 -342 265 N ATOM 2302 CA ARG A1098 -9.681 -0.420 -2.150 1.00 87.31 C ANISOU 2302 CA ARG A1098 6885 15855 10432 -2661 -471 267 C ATOM 2303 C ARG A1098 -9.271 -1.559 -1.226 1.00 93.57 C ANISOU 2303 C ARG A1098 7495 16654 11402 -2455 -570 268 C ATOM 2304 O ARG A1098 -9.108 -1.355 -0.022 1.00 98.26 O ANISOU 2304 O ARG A1098 8131 17182 12022 -2500 -729 326 O ATOM 2305 CB ARG A1098 -11.030 -0.713 -2.812 1.00 83.09 C ANISOU 2305 CB ARG A1098 6552 15185 9832 -2568 -387 195 C ATOM 2306 CG ARG A1098 -12.217 -0.657 -1.865 1.00 78.41 C ANISOU 2306 CG ARG A1098 6223 14357 9214 -2539 -506 203 C ATOM 2307 CD ARG A1098 -13.320 -1.589 -2.332 1.00 82.37 C ANISOU 2307 CD ARG A1098 6800 14763 9736 -2343 -441 120 C ATOM 2308 NE ARG A1098 -12.907 -2.985 -2.237 1.00 87.66 N ANISOU 2308 NE ARG A1098 7240 15501 10566 -2099 -429 73 N ATOM 2309 CZ ARG A1098 -13.651 -4.018 -2.616 1.00 86.51 C ANISOU 2309 CZ ARG A1098 7105 15300 10465 -1898 -369 -7 C ATOM 2310 NH1 ARG A1098 -13.186 -5.253 -2.483 1.00 82.02 N ANISOU 2310 NH1 ARG A1098 6329 14790 10046 -1678 -359 -42 N ATOM 2311 NH2 ARG A1098 -14.855 -3.818 -3.132 1.00 88.55 N ANISOU 2311 NH2 ARG A1098 7582 15445 10618 -1918 -318 -48 N ATOM 2312 N ASN A1099 -9.035 -2.746 -1.799 1.00 94.07 N ANISOU 2312 N ASN A1099 7354 16803 11585 -2230 -474 207 N ATOM 2313 CA ASN A1099 -8.670 -3.929 -1.017 1.00 92.50 C ANISOU 2313 CA ASN A1099 6978 16603 11563 -2006 -557 207 C ATOM 2314 C ASN A1099 -7.563 -3.628 -0.015 1.00 86.13 C ANISOU 2314 C ASN A1099 6018 15882 10825 -2093 -701 296 C ATOM 2315 O ASN A1099 -7.666 -3.978 1.172 1.00 84.01 O ANISOU 2315 O ASN A1099 5783 15516 10621 -2027 -862 330 O ATOM 2316 CB ASN A1099 -8.250 -5.063 -1.954 1.00 95.84 C ANISOU 2316 CB ASN A1099 7163 17151 12103 -1786 -401 138 C ATOM 2317 CG ASN A1099 -9.311 -6.140 -2.080 1.00 93.40 C ANISOU 2317 CG ASN A1099 6954 16703 11833 -1555 -365 57 C ATOM 2318 OD1 ASN A1099 -10.469 -5.933 -1.716 1.00 88.19 O ANISOU 2318 OD1 ASN A1099 6554 15864 11090 -1581 -428 45 O ATOM 2319 ND2 ASN A1099 -8.920 -7.298 -2.596 1.00 97.30 N ANISOU 2319 ND2 ASN A1099 7243 17274 12454 -1326 -256 1 N ATOM 2320 N ALA A1100 -6.496 -2.971 -0.480 1.00 88.38 N ANISOU 2320 N ALA A1100 6137 16354 11089 -2249 -648 334 N ATOM 2321 CA ALA A1100 -5.425 -2.560 0.423 1.00 96.59 C ANISOU 2321 CA ALA A1100 7035 17492 12175 -2366 -785 421 C ATOM 2322 C ALA A1100 -5.981 -1.800 1.621 1.00101.93 C ANISOU 2322 C ALA A1100 7973 18000 12756 -2516 -961 473 C ATOM 2323 O ALA A1100 -5.672 -2.119 2.780 1.00104.85 O ANISOU 2323 O ALA A1100 8296 18341 13202 -2471 -1121 518 O ATOM 2324 CB ALA A1100 -4.399 -1.708 -0.327 1.00 79.06 C ANISOU 2324 CB ALA A1100 4663 15475 9901 -2566 -695 455 C ATOM 2325 N TYR A1101 -6.840 -0.809 1.368 1.00 97.83 N ANISOU 2325 N TYR A1101 7744 17360 12067 -2686 -931 467 N ATOM 2326 CA TYR A1101 -7.273 0.000 2.507 1.00 88.96 C ANISOU 2326 CA TYR A1101 6868 16082 10850 -2840 -1083 519 C ATOM 2327 C TYR A1101 -8.353 -0.673 3.358 1.00 79.21 C ANISOU 2327 C TYR A1101 5816 14632 9650 -2676 -1175 491 C ATOM 2328 O TYR A1101 -8.478 -0.349 4.549 1.00 71.84 O ANISOU 2328 O TYR A1101 5015 13591 8689 -2746 -1323 535 O ATOM 2329 CB TYR A1101 -7.707 1.377 2.017 1.00 87.91 C ANISOU 2329 CB TYR A1101 6978 15895 10530 -3089 -1024 534 C ATOM 2330 CG TYR A1101 -6.492 2.222 1.718 1.00 98.43 C ANISOU 2330 CG TYR A1101 8158 17421 11819 -3304 -1006 591 C ATOM 2331 CD1 TYR A1101 -5.949 3.051 2.687 1.00 99.32 C ANISOU 2331 CD1 TYR A1101 8322 17539 11878 -3503 -1141 666 C ATOM 2332 CD2 TYR A1101 -5.846 2.134 0.492 1.00104.17 C ANISOU 2332 CD2 TYR A1101 8680 18335 12564 -3306 -855 568 C ATOM 2333 CE1 TYR A1101 -4.823 3.801 2.430 1.00104.39 C ANISOU 2333 CE1 TYR A1101 8817 18364 12480 -3706 -1130 720 C ATOM 2334 CE2 TYR A1101 -4.719 2.879 0.223 1.00103.80 C ANISOU 2334 CE2 TYR A1101 8485 18472 12484 -3504 -838 620 C ATOM 2335 CZ TYR A1101 -4.209 3.713 1.196 1.00108.46 C ANISOU 2335 CZ TYR A1101 9128 19064 13020 -3706 -979 698 C ATOM 2336 OH TYR A1101 -3.086 4.466 0.936 1.00118.10 O ANISOU 2336 OH TYR A1101 10200 20471 14202 -3914 -966 752 O ATOM 2337 N ILE A1102 -9.118 -1.615 2.793 1.00 84.96 N ANISOU 2337 N ILE A1102 6552 15295 10433 -2463 -1089 418 N ATOM 2338 CA ILE A1102 -9.964 -2.486 3.610 1.00 88.72 C ANISOU 2338 CA ILE A1102 7138 15597 10975 -2276 -1180 392 C ATOM 2339 C ILE A1102 -9.111 -3.214 4.628 1.00 98.38 C ANISOU 2339 C ILE A1102 8164 16879 12337 -2171 -1321 434 C ATOM 2340 O ILE A1102 -9.296 -3.077 5.843 1.00 91.82 O ANISOU 2340 O ILE A1102 7460 15935 11492 -2206 -1475 473 O ATOM 2341 CB ILE A1102 -10.721 -3.511 2.746 1.00 86.37 C ANISOU 2341 CB ILE A1102 6824 15261 10730 -2054 -1057 307 C ATOM 2342 CG1 ILE A1102 -11.192 -2.930 1.423 1.00 85.84 C ANISOU 2342 CG1 ILE A1102 6848 15222 10547 -2145 -889 263 C ATOM 2343 CG2 ILE A1102 -11.895 -4.101 3.514 1.00 82.78 C ANISOU 2343 CG2 ILE A1102 6574 14587 10292 -1918 -1141 280 C ATOM 2344 CD1 ILE A1102 -11.710 -4.005 0.497 1.00 85.03 C ANISOU 2344 CD1 ILE A1102 6682 15127 10499 -1930 -758 175 C ATOM 2345 N GLN A1103 -8.169 -4.023 4.133 1.00106.31 N ANISOU 2345 N GLN A1103 8855 18061 13478 -2032 -1265 427 N ATOM 2346 CA GLN A1103 -7.339 -4.820 5.027 1.00115.25 C ANISOU 2346 CA GLN A1103 9777 19255 14759 -1904 -1396 469 C ATOM 2347 C GLN A1103 -6.482 -3.959 5.943 1.00108.87 C ANISOU 2347 C GLN A1103 8938 18520 13908 -2114 -1539 555 C ATOM 2348 O GLN A1103 -5.941 -4.475 6.928 1.00111.33 O ANISOU 2348 O GLN A1103 9136 18851 14313 -2039 -1686 600 O ATOM 2349 CB GLN A1103 -6.455 -5.772 4.220 1.00122.38 C ANISOU 2349 CB GLN A1103 10342 20338 15817 -1718 -1286 447 C ATOM 2350 CG GLN A1103 -7.229 -6.861 3.494 1.00122.76 C ANISOU 2350 CG GLN A1103 10404 20312 15929 -1471 -1161 361 C ATOM 2351 CD GLN A1103 -6.324 -7.847 2.784 1.00127.23 C ANISOU 2351 CD GLN A1103 10644 21042 16657 -1269 -1047 338 C ATOM 2352 OE1 GLN A1103 -5.116 -7.633 2.673 1.00130.34 O ANISOU 2352 OE1 GLN A1103 10791 21622 17112 -1328 -1040 384 O ATOM 2353 NE2 GLN A1103 -6.904 -8.939 2.301 1.00126.25 N ANISOU 2353 NE2 GLN A1103 10517 20846 16604 -1029 -952 267 N ATOM 2354 N LYS A1104 -6.346 -2.663 5.654 1.00104.71 N ANISOU 2354 N LYS A1104 8516 18031 13237 -2377 -1504 582 N ATOM 2355 CA LYS A1104 -5.589 -1.803 6.558 1.00 98.49 C ANISOU 2355 CA LYS A1104 7726 17301 12392 -2593 -1641 664 C ATOM 2356 C LYS A1104 -6.450 -1.231 7.687 1.00 90.67 C ANISOU 2356 C LYS A1104 7066 16099 11287 -2697 -1768 683 C ATOM 2357 O LYS A1104 -6.142 -1.443 8.864 1.00 99.10 O ANISOU 2357 O LYS A1104 8122 17145 12387 -2690 -1930 727 O ATOM 2358 CB LYS A1104 -4.898 -0.683 5.773 1.00 96.45 C ANISOU 2358 CB LYS A1104 7411 17198 12039 -2835 -1550 692 C ATOM 2359 CG LYS A1104 -3.621 -1.127 5.079 1.00 98.12 C ANISOU 2359 CG LYS A1104 7243 17663 12375 -2778 -1479 705 C ATOM 2360 CD LYS A1104 -2.508 -0.096 5.220 1.00103.30 C ANISOU 2360 CD LYS A1104 7792 18490 12970 -3042 -1524 782 C ATOM 2361 CE LYS A1104 -1.955 -0.041 6.641 1.00106.67 C ANISOU 2361 CE LYS A1104 8185 18924 13419 -3105 -1736 856 C ATOM 2362 NZ LYS A1104 -1.138 -1.239 6.990 1.00107.89 N ANISOU 2362 NZ LYS A1104 8016 19203 13773 -2884 -1804 873 N ATOM 2363 N TYR A1105 -7.531 -0.510 7.360 1.00 79.66 N ANISOU 2363 N TYR A1105 5968 14544 9756 -2792 -1695 651 N ATOM 2364 CA TYR A1105 -8.171 0.302 8.395 1.00 75.11 C ANISOU 2364 CA TYR A1105 5698 13788 9053 -2942 -1798 680 C ATOM 2365 C TYR A1105 -9.677 0.073 8.519 1.00 90.55 C ANISOU 2365 C TYR A1105 7936 15499 10968 -2833 -1770 625 C ATOM 2366 O TYR A1105 -10.403 0.992 8.909 1.00 91.22 O ANISOU 2366 O TYR A1105 8310 15427 10921 -2979 -1781 636 O ATOM 2367 CB TYR A1105 -7.909 1.792 8.158 1.00 72.41 C ANISOU 2367 CB TYR A1105 5482 13476 8554 -3239 -1764 723 C ATOM 2368 CG TYR A1105 -6.463 2.164 7.920 1.00 83.05 C ANISOU 2368 CG TYR A1105 6565 15069 9921 -3381 -1776 778 C ATOM 2369 CD1 TYR A1105 -5.565 2.252 8.974 1.00 84.68 C ANISOU 2369 CD1 TYR A1105 6668 15359 10149 -3467 -1931 845 C ATOM 2370 CD2 TYR A1105 -6.002 2.452 6.642 1.00 86.66 C ANISOU 2370 CD2 TYR A1105 6879 15678 10369 -3437 -1631 766 C ATOM 2371 CE1 TYR A1105 -4.240 2.599 8.760 1.00 89.01 C ANISOU 2371 CE1 TYR A1105 6963 16139 10718 -3602 -1946 899 C ATOM 2372 CE2 TYR A1105 -4.679 2.800 6.415 1.00 88.46 C ANISOU 2372 CE2 TYR A1105 6860 16135 10618 -3570 -1636 817 C ATOM 2373 CZ TYR A1105 -3.801 2.873 7.476 1.00 92.44 C ANISOU 2373 CZ TYR A1105 7251 16720 11150 -3652 -1795 885 C ATOM 2374 OH TYR A1105 -2.487 3.221 7.247 1.00 84.72 O ANISOU 2374 OH TYR A1105 6018 15978 10195 -3790 -1802 939 O ATOM 2375 N LEU A1106 -10.177 -1.134 8.234 1.00 92.48 N ANISOU 2375 N LEU A1106 8111 15704 11325 -2579 -1735 568 N ATOM 2376 CA LEU A1106 -11.632 -1.254 8.278 1.00 91.69 C ANISOU 2376 CA LEU A1106 8284 15380 11176 -2499 -1701 517 C ATOM 2377 C LEU A1106 -12.084 -2.269 9.325 1.00 95.81 C ANISOU 2377 C LEU A1106 8847 15776 11779 -2311 -1820 505 C ATOM 2378 O LEU A1106 -11.451 -3.320 9.482 1.00 97.70 O ANISOU 2378 O LEU A1106 8854 16111 12155 -2143 -1871 506 O ATOM 2379 CB LEU A1106 -12.198 -1.653 6.903 1.00 92.38 C ANISOU 2379 CB LEU A1106 8337 15484 11280 -2387 -1535 450 C ATOM 2380 CG LEU A1106 -13.709 -1.480 6.716 1.00 94.79 C ANISOU 2380 CG LEU A1106 8934 15578 11505 -2359 -1477 404 C ATOM 2381 CD1 LEU A1106 -14.100 -0.002 6.749 1.00 93.10 C ANISOU 2381 CD1 LEU A1106 8970 15275 11128 -2602 -1456 439 C ATOM 2382 CD2 LEU A1106 -14.177 -2.130 5.424 1.00 94.59 C ANISOU 2382 CD2 LEU A1106 8834 15592 11514 -2218 -1331 335 C ATOM 2383 N PRO A 377 -13.158 -1.978 10.060 1.00100.09 N ANISOU 2383 N PRO A 377 9683 16104 12242 -2334 -1863 497 N ATOM 2384 CA PRO A 377 -13.705 -2.943 11.027 1.00 98.23 C ANISOU 2384 CA PRO A 377 9515 15738 12071 -2157 -1966 481 C ATOM 2385 C PRO A 377 -14.400 -4.101 10.327 1.00 95.01 C ANISOU 2385 C PRO A 377 9054 15287 11757 -1916 -1890 413 C ATOM 2386 O PRO A 377 -14.570 -4.083 9.100 1.00 94.75 O ANISOU 2386 O PRO A 377 8963 15313 11725 -1897 -1751 374 O ATOM 2387 CB PRO A 377 -14.706 -2.099 11.835 1.00 93.06 C ANISOU 2387 CB PRO A 377 9205 14871 11283 -2280 -1995 489 C ATOM 2388 CG PRO A 377 -15.040 -0.949 10.940 1.00 92.22 C ANISOU 2388 CG PRO A 377 9221 14752 11066 -2449 -1869 486 C ATOM 2389 CD PRO A 377 -13.762 -0.645 10.224 1.00 97.18 C ANISOU 2389 CD PRO A 377 9598 15612 11715 -2547 -1836 517 C ATOM 2390 N PRO A 378 -14.811 -5.125 11.076 1.00 97.03 N ANISOU 2390 N PRO A 378 9337 15443 12086 -1735 -1978 397 N ATOM 2391 CA PRO A 378 -15.446 -6.302 10.456 1.00 99.05 C ANISOU 2391 CA PRO A 378 9543 15657 12436 -1502 -1913 336 C ATOM 2392 C PRO A 378 -16.760 -5.944 9.793 1.00100.25 C ANISOU 2392 C PRO A 378 9918 15670 12502 -1521 -1797 283 C ATOM 2393 O PRO A 378 -17.416 -4.954 10.166 1.00 99.33 O ANISOU 2393 O PRO A 378 10047 15429 12266 -1672 -1798 296 O ATOM 2394 CB PRO A 378 -15.661 -7.253 11.648 1.00102.02 C ANISOU 2394 CB PRO A 378 9961 15928 12875 -1349 -2056 344 C ATOM 2395 CG PRO A 378 -14.646 -6.840 12.637 1.00104.32 C ANISOU 2395 CG PRO A 378 10184 16300 13153 -1463 -2189 413 C ATOM 2396 CD PRO A 378 -14.493 -5.359 12.494 1.00101.59 C ANISOU 2396 CD PRO A 378 9946 15979 12675 -1727 -2145 441 C ATOM 2397 N PRO A 379 -17.203 -6.738 8.816 1.00101.32 N ANISOU 2397 N PRO A 379 9981 15820 12695 -1367 -1694 226 N ATOM 2398 CA PRO A 379 -18.426 -6.411 8.071 1.00103.00 C ANISOU 2398 CA PRO A 379 10385 15923 12825 -1387 -1582 177 C ATOM 2399 C PRO A 379 -19.689 -6.609 8.902 1.00105.15 C ANISOU 2399 C PRO A 379 10918 15968 13065 -1330 -1642 161 C ATOM 2400 O PRO A 379 -19.693 -7.232 9.966 1.00107.83 O ANISOU 2400 O PRO A 379 11283 16234 13453 -1239 -1760 176 O ATOM 2401 CB PRO A 379 -18.390 -7.383 6.888 1.00 98.15 C ANISOU 2401 CB PRO A 379 9587 15414 12290 -1220 -1466 118 C ATOM 2402 CG PRO A 379 -16.967 -7.838 6.794 1.00 97.71 C ANISOU 2402 CG PRO A 379 9231 15553 12340 -1168 -1483 145 C ATOM 2403 CD PRO A 379 -16.482 -7.869 8.205 1.00101.16 C ANISOU 2403 CD PRO A 379 9678 15946 12812 -1182 -1657 206 C ATOM 2404 N SER A 380 -20.791 -6.088 8.362 1.00101.81 N ANISOU 2404 N SER A 380 10689 15437 12556 -1381 -1552 131 N ATOM 2405 CA SER A 380 -22.077 -6.061 9.062 1.00 97.99 C ANISOU 2405 CA SER A 380 10471 14735 12026 -1353 -1584 118 C ATOM 2406 C SER A 380 -22.952 -7.233 8.615 1.00 94.12 C ANISOU 2406 C SER A 380 9982 14184 11595 -1157 -1548 57 C ATOM 2407 O SER A 380 -23.901 -7.099 7.837 1.00 92.69 O ANISOU 2407 O SER A 380 9904 13946 11367 -1153 -1453 19 O ATOM 2408 CB SER A 380 -22.772 -4.722 8.834 1.00 99.74 C ANISOU 2408 CB SER A 380 10911 14863 12121 -1528 -1514 133 C ATOM 2409 OG SER A 380 -22.912 -4.454 7.449 1.00100.08 O ANISOU 2409 OG SER A 380 10901 14992 12134 -1560 -1386 107 O ATOM 2410 N ARG A 381 -22.615 -8.407 9.153 1.00 94.01 N ANISOU 2410 N ARG A 381 9853 14183 11684 -993 -1632 54 N ATOM 2411 CA ARG A 381 -23.397 -9.608 8.875 1.00 87.88 C ANISOU 2411 CA ARG A 381 9082 13342 10967 -801 -1612 4 C ATOM 2412 C ARG A 381 -24.797 -9.499 9.466 1.00 89.48 C ANISOU 2412 C ARG A 381 9563 13330 11106 -799 -1632 -11 C ATOM 2413 O ARG A 381 -25.770 -9.982 8.874 1.00 78.20 O ANISOU 2413 O ARG A 381 8202 11838 9673 -716 -1567 -58 O ATOM 2414 CB ARG A 381 -22.666 -10.831 9.428 1.00 83.21 C ANISOU 2414 CB ARG A 381 8316 12799 10499 -630 -1706 19 C ATOM 2415 CG ARG A 381 -23.349 -12.166 9.195 1.00 79.94 C ANISOU 2415 CG ARG A 381 7896 12325 10154 -420 -1689 -24 C ATOM 2416 CD ARG A 381 -22.524 -13.301 9.791 1.00 84.94 C ANISOU 2416 CD ARG A 381 8358 13000 10916 -250 -1785 10 C ATOM 2417 NE ARG A 381 -21.201 -13.410 9.179 1.00 89.79 N ANISOU 2417 NE ARG A 381 8691 13817 11608 -223 -1739 22 N ATOM 2418 CZ ARG A 381 -20.085 -12.901 9.696 1.00 89.43 C ANISOU 2418 CZ ARG A 381 8530 13866 11584 -313 -1816 79 C ATOM 2419 NH1 ARG A 381 -20.121 -12.237 10.844 1.00 89.37 N ANISOU 2419 NH1 ARG A 381 8672 13773 11513 -436 -1940 121 N ATOM 2420 NH2 ARG A 381 -18.930 -13.056 9.061 1.00 87.27 N ANISOU 2420 NH2 ARG A 381 7991 13778 11388 -278 -1761 87 N ATOM 2421 N GLU A 382 -24.918 -8.847 10.626 1.00 92.58 N ANISOU 2421 N GLU A 382 10119 13617 11442 -891 -1710 27 N ATOM 2422 CA GLU A 382 -26.210 -8.715 11.290 1.00 92.50 C ANISOU 2422 CA GLU A 382 10369 13408 11370 -884 -1715 16 C ATOM 2423 C GLU A 382 -27.148 -7.786 10.523 1.00 76.23 C ANISOU 2423 C GLU A 382 8459 11280 9227 -982 -1597 1 C ATOM 2424 O GLU A 382 -28.377 -7.925 10.614 1.00 79.99 O ANISOU 2424 O GLU A 382 9106 11612 9676 -933 -1565 -23 O ATOM 2425 CB GLU A 382 -25.998 -8.215 12.721 1.00 90.89 C ANISOU 2425 CB GLU A 382 10287 13132 11114 -965 -1807 62 C ATOM 2426 CG GLU A 382 -25.106 -9.113 13.571 1.00 94.33 C ANISOU 2426 CG GLU A 382 10589 13632 11620 -869 -1935 85 C ATOM 2427 CD GLU A 382 -24.826 -8.531 14.945 1.00106.06 C ANISOU 2427 CD GLU A 382 12193 15071 13034 -976 -2019 136 C ATOM 2428 OE1 GLU A 382 -25.318 -7.418 15.228 1.00109.25 O ANISOU 2428 OE1 GLU A 382 12784 15385 13341 -1125 -1972 154 O ATOM 2429 OE2 GLU A 382 -24.115 -9.182 15.741 1.00111.97 O ANISOU 2429 OE2 GLU A 382 12850 15871 13823 -912 -2132 164 O ATOM 2430 N LYS A 383 -26.591 -6.850 9.753 1.00 62.62 N ANISOU 2430 N LYS A 383 6669 9661 7462 -1118 -1532 18 N ATOM 2431 CA LYS A 383 -27.417 -5.900 9.012 1.00 60.22 C ANISOU 2431 CA LYS A 383 6507 9298 7076 -1215 -1426 15 C ATOM 2432 C LYS A 383 -28.217 -6.601 7.916 1.00 53.70 C ANISOU 2432 C LYS A 383 5655 8477 6270 -1106 -1346 -41 C ATOM 2433 O LYS A 383 -29.413 -6.331 7.731 1.00 54.93 O ANISOU 2433 O LYS A 383 5983 8506 6381 -1104 -1295 -52 O ATOM 2434 CB LYS A 383 -26.533 -4.801 8.424 1.00 61.88 C ANISOU 2434 CB LYS A 383 6642 9636 7233 -1388 -1380 52 C ATOM 2435 CG LYS A 383 -27.279 -3.551 7.992 1.00 67.31 C ANISOU 2435 CG LYS A 383 7515 10239 7820 -1524 -1297 76 C ATOM 2436 CD LYS A 383 -26.319 -2.547 7.378 1.00 75.93 C ANISOU 2436 CD LYS A 383 8524 11469 8856 -1696 -1256 114 C ATOM 2437 CE LYS A 383 -25.677 -3.116 6.124 1.00 76.27 C ANISOU 2437 CE LYS A 383 8335 11709 8937 -1652 -1191 78 C ATOM 2438 NZ LYS A 383 -26.714 -3.493 5.124 1.00 72.10 N ANISOU 2438 NZ LYS A 383 7851 11149 8396 -1570 -1104 29 N ATOM 2439 N LYS A 384 -27.571 -7.502 7.172 1.00 47.71 N ANISOU 2439 N LYS A 384 4678 7872 5578 -1013 -1327 -77 N ATOM 2440 CA LYS A 384 -28.295 -8.304 6.192 1.00 34.14 C ANISOU 2440 CA LYS A 384 2930 6169 3873 -901 -1253 -140 C ATOM 2441 C LYS A 384 -29.377 -9.135 6.866 1.00 33.19 C ANISOU 2441 C LYS A 384 2949 5882 3780 -774 -1304 -162 C ATOM 2442 O LYS A 384 -30.448 -9.368 6.290 1.00 34.34 O ANISOU 2442 O LYS A 384 3187 5963 3898 -731 -1245 -201 O ATOM 2443 CB LYS A 384 -27.326 -9.207 5.430 1.00 35.24 C ANISOU 2443 CB LYS A 384 2801 6506 4081 -804 -1218 -182 C ATOM 2444 CG LYS A 384 -27.997 -10.092 4.395 1.00 38.96 C ANISOU 2444 CG LYS A 384 3232 7013 4557 -682 -1130 -267 C ATOM 2445 CD LYS A 384 -27.012 -11.034 3.725 1.00 52.48 C ANISOU 2445 CD LYS A 384 4679 8917 6345 -559 -1079 -322 C ATOM 2446 CE LYS A 384 -27.705 -11.849 2.641 1.00 55.49 C ANISOU 2446 CE LYS A 384 5033 9336 6714 -445 -978 -431 C ATOM 2447 NZ LYS A 384 -26.772 -12.803 1.979 1.00 63.09 N ANISOU 2447 NZ LYS A 384 5744 10472 7756 -300 -906 -501 N ATOM 2448 N VAL A 385 -29.107 -9.597 8.089 1.00 37.15 N ANISOU 2448 N VAL A 385 3468 6318 4329 -717 -1416 -135 N ATOM 2449 CA VAL A 385 -30.121 -10.309 8.862 1.00 28.72 C ANISOU 2449 CA VAL A 385 2552 5086 3275 -614 -1468 -147 C ATOM 2450 C VAL A 385 -31.338 -9.419 9.073 1.00 27.12 C ANISOU 2450 C VAL A 385 2590 4724 2990 -693 -1419 -138 C ATOM 2451 O VAL A 385 -32.483 -9.855 8.904 1.00 25.77 O ANISOU 2451 O VAL A 385 2528 4453 2812 -625 -1388 -167 O ATOM 2452 CB VAL A 385 -29.539 -10.792 10.202 1.00 29.64 C ANISOU 2452 CB VAL A 385 2657 5169 3436 -561 -1596 -113 C ATOM 2453 CG1 VAL A 385 -30.600 -11.530 11.010 1.00 28.44 C ANISOU 2453 CG1 VAL A 385 2666 4858 3280 -459 -1639 -127 C ATOM 2454 CG2 VAL A 385 -28.321 -11.665 9.971 1.00 31.43 C ANISOU 2454 CG2 VAL A 385 2630 5553 3760 -468 -1641 -108 C ATOM 2455 N THR A 386 -31.108 -8.149 9.432 1.00 27.42 N ANISOU 2455 N THR A 386 2711 4741 2967 -838 -1406 -93 N ATOM 2456 CA THR A 386 -32.230 -7.220 9.564 1.00 26.07 C ANISOU 2456 CA THR A 386 2754 4427 2725 -909 -1343 -73 C ATOM 2457 C THR A 386 -32.979 -7.066 8.244 1.00 25.16 C ANISOU 2457 C THR A 386 2647 4326 2586 -908 -1245 -99 C ATOM 2458 O THR A 386 -34.215 -6.997 8.229 1.00 23.83 O ANISOU 2458 O THR A 386 2625 4033 2396 -878 -1203 -102 O ATOM 2459 CB THR A 386 -31.749 -5.857 10.061 1.00 26.79 C ANISOU 2459 CB THR A 386 2921 4506 2752 -1074 -1341 -15 C ATOM 2460 OG1 THR A 386 -30.890 -5.261 9.081 1.00 51.78 O ANISOU 2460 OG1 THR A 386 5955 7818 5899 -1174 -1302 -5 O ATOM 2461 CG2 THR A 386 -30.999 -6.001 11.372 1.00 32.43 C ANISOU 2461 CG2 THR A 386 3629 5215 3476 -1087 -1440 11 C ATOM 2462 N ARG A 387 -32.247 -7.007 7.124 1.00 40.63 N ANISOU 2462 N ARG A 387 4446 6446 4546 -945 -1202 -114 N ATOM 2463 CA ARG A 387 -32.902 -6.955 5.817 1.00 25.30 C ANISOU 2463 CA ARG A 387 2501 4541 2571 -944 -1108 -142 C ATOM 2464 C ARG A 387 -33.817 -8.157 5.606 1.00 24.76 C ANISOU 2464 C ARG A 387 2449 4420 2539 -798 -1106 -198 C ATOM 2465 O ARG A 387 -34.943 -8.015 5.109 1.00 23.18 O ANISOU 2465 O ARG A 387 2360 4143 2305 -789 -1052 -205 O ATOM 2466 CB ARG A 387 -31.853 -6.880 4.707 1.00 29.68 C ANISOU 2466 CB ARG A 387 2859 5303 3116 -996 -1057 -160 C ATOM 2467 CG ARG A 387 -31.559 -5.475 4.209 1.00 44.53 C ANISOU 2467 CG ARG A 387 4776 7226 4916 -1168 -1002 -109 C ATOM 2468 CD ARG A 387 -30.468 -5.499 3.146 1.00 61.49 C ANISOU 2468 CD ARG A 387 6716 9594 7053 -1218 -946 -131 C ATOM 2469 NE ARG A 387 -30.348 -4.232 2.429 1.00 72.01 N ANISOU 2469 NE ARG A 387 8094 10973 8294 -1384 -880 -87 N ATOM 2470 CZ ARG A 387 -30.878 -3.996 1.233 1.00 76.61 C ANISOU 2470 CZ ARG A 387 8695 11600 8812 -1417 -794 -101 C ATOM 2471 NH1 ARG A 387 -31.568 -4.944 0.611 1.00 74.10 N ANISOU 2471 NH1 ARG A 387 8353 11292 8509 -1298 -762 -167 N ATOM 2472 NH2 ARG A 387 -30.714 -2.813 0.654 1.00 77.56 N ANISOU 2472 NH2 ARG A 387 8865 11760 8846 -1576 -745 -50 N ATOM 2473 N THR A 388 -33.353 -9.351 5.990 1.00 27.04 N ANISOU 2473 N THR A 388 2629 4749 2897 -683 -1168 -233 N ATOM 2474 CA THR A 388 -34.183 -10.544 5.852 1.00 26.80 C ANISOU 2474 CA THR A 388 2618 4668 2896 -549 -1170 -288 C ATOM 2475 C THR A 388 -35.423 -10.462 6.736 1.00 25.40 C ANISOU 2475 C THR A 388 2656 4289 2706 -532 -1197 -262 C ATOM 2476 O THR A 388 -36.537 -10.772 6.289 1.00 21.64 O ANISOU 2476 O THR A 388 2262 3747 2214 -492 -1153 -288 O ATOM 2477 CB THR A 388 -33.368 -11.793 6.190 1.00 29.27 C ANISOU 2477 CB THR A 388 2771 5062 3286 -420 -1233 -324 C ATOM 2478 OG1 THR A 388 -32.242 -11.884 5.309 1.00 26.49 O ANISOU 2478 OG1 THR A 388 2201 4911 2954 -418 -1185 -358 O ATOM 2479 CG2 THR A 388 -34.226 -13.042 6.042 1.00 28.08 C ANISOU 2479 CG2 THR A 388 2661 4837 3170 -268 -1219 -394 C ATOM 2480 N ILE A 389 -35.248 -10.047 7.994 1.00 22.76 N ANISOU 2480 N ILE A 389 2408 3868 2374 -561 -1258 -216 N ATOM 2481 CA ILE A 389 -36.389 -9.878 8.891 1.00 34.18 C ANISOU 2481 CA ILE A 389 4047 5144 3797 -548 -1251 -194 C ATOM 2482 C ILE A 389 -37.424 -8.953 8.261 1.00 20.67 C ANISOU 2482 C ILE A 389 2449 3368 2035 -610 -1157 -174 C ATOM 2483 O ILE A 389 -38.624 -9.258 8.231 1.00 19.64 O ANISOU 2483 O ILE A 389 2416 3142 1905 -559 -1123 -180 O ATOM 2484 CB ILE A 389 -35.924 -9.355 10.263 1.00 26.32 C ANISOU 2484 CB ILE A 389 3121 4093 2785 -601 -1299 -144 C ATOM 2485 CG1 ILE A 389 -34.851 -10.270 10.860 1.00 23.32 C ANISOU 2485 CG1 ILE A 389 2614 3792 2455 -536 -1400 -152 C ATOM 2486 CG2 ILE A 389 -37.102 -9.244 11.218 1.00 21.12 C ANISOU 2486 CG2 ILE A 389 2658 3264 2104 -592 -1272 -113 C ATOM 2487 CD1 ILE A 389 -35.297 -11.698 11.060 1.00 23.01 C ANISOU 2487 CD1 ILE A 389 2563 3721 2457 -399 -1437 -179 C ATOM 2488 N LEU A 390 -36.970 -7.811 7.734 1.00 21.10 N ANISOU 2488 N LEU A 390 2489 3480 2049 -724 -1118 -142 N ATOM 2489 CA LEU A 390 -37.888 -6.900 7.060 1.00 20.39 C ANISOU 2489 CA LEU A 390 2497 3340 1910 -782 -1039 -112 C ATOM 2490 C LEU A 390 -38.594 -7.589 5.900 1.00 22.89 C ANISOU 2490 C LEU A 390 2770 3696 2233 -714 -996 -156 C ATOM 2491 O LEU A 390 -39.790 -7.367 5.677 1.00 18.95 O ANISOU 2491 O LEU A 390 2372 3110 1716 -701 -953 -137 O ATOM 2492 CB LEU A 390 -37.147 -5.660 6.565 1.00 21.19 C ANISOU 2492 CB LEU A 390 2574 3517 1959 -921 -1009 -71 C ATOM 2493 CG LEU A 390 -38.046 -4.651 5.841 1.00 20.64 C ANISOU 2493 CG LEU A 390 2610 3400 1834 -988 -938 -27 C ATOM 2494 CD1 LEU A 390 -39.053 -4.023 6.796 1.00 19.95 C ANISOU 2494 CD1 LEU A 390 2713 3135 1730 -999 -932 22 C ATOM 2495 CD2 LEU A 390 -37.225 -3.582 5.133 1.00 22.46 C ANISOU 2495 CD2 LEU A 390 2797 3730 2005 -1130 -908 8 C ATOM 2496 N ALA A 391 -37.875 -8.432 5.152 1.00 30.86 N ANISOU 2496 N ALA A 391 3623 4839 3262 -675 -1004 -212 N ATOM 2497 CA ALA A 391 -38.501 -9.145 4.039 1.00 20.11 C ANISOU 2497 CA ALA A 391 2223 3523 1894 -620 -957 -264 C ATOM 2498 C ALA A 391 -39.647 -10.028 4.524 1.00 30.48 C ANISOU 2498 C ALA A 391 3631 4712 3238 -523 -978 -285 C ATOM 2499 O ALA A 391 -40.741 -10.024 3.941 1.00 24.52 O ANISOU 2499 O ALA A 391 2941 3912 2463 -512 -933 -284 O ATOM 2500 CB ALA A 391 -37.458 -9.977 3.293 1.00 21.16 C ANISOU 2500 CB ALA A 391 2166 3832 2042 -584 -950 -336 C ATOM 2501 N ILE A 392 -39.417 -10.785 5.601 1.00 28.30 N ANISOU 2501 N ILE A 392 3363 4383 3009 -457 -1051 -296 N ATOM 2502 CA ILE A 392 -40.449 -11.687 6.115 1.00 24.96 C ANISOU 2502 CA ILE A 392 3030 3842 2609 -376 -1074 -313 C ATOM 2503 C ILE A 392 -41.649 -10.894 6.622 1.00 21.46 C ANISOU 2503 C ILE A 392 2743 3262 2150 -403 -1024 -252 C ATOM 2504 O ILE A 392 -42.806 -11.181 6.274 1.00 20.55 O ANISOU 2504 O ILE A 392 2687 3088 2036 -375 -988 -255 O ATOM 2505 CB ILE A 392 -39.865 -12.588 7.218 1.00 20.98 C ANISOU 2505 CB ILE A 392 2514 3298 2162 -299 -1158 -322 C ATOM 2506 CG1 ILE A 392 -38.613 -13.302 6.713 1.00 31.66 C ANISOU 2506 CG1 ILE A 392 3686 4784 3559 -234 -1164 -377 C ATOM 2507 CG2 ILE A 392 -40.893 -13.599 7.686 1.00 24.08 C ANISOU 2507 CG2 ILE A 392 3009 3547 2594 -204 -1159 -340 C ATOM 2508 CD1 ILE A 392 -37.894 -14.085 7.787 1.00 37.92 C ANISOU 2508 CD1 ILE A 392 4447 5548 4413 -153 -1253 -369 C ATOM 2509 N LEU A 393 -41.387 -9.878 7.451 1.00 17.60 N ANISOU 2509 N LEU A 393 2319 2724 1645 -466 -1023 -194 N ATOM 2510 CA LEU A 393 -42.471 -9.104 8.048 1.00 17.30 C ANISOU 2510 CA LEU A 393 2432 2553 1590 -495 -982 -133 C ATOM 2511 C LEU A 393 -43.295 -8.384 6.986 1.00 20.02 C ANISOU 2511 C LEU A 393 2798 2908 1901 -531 -921 -107 C ATOM 2512 O LEU A 393 -44.531 -8.372 7.053 1.00 15.86 O ANISOU 2512 O LEU A 393 2356 2293 1376 -507 -893 -80 O ATOM 2513 CB LEU A 393 -41.901 -8.110 9.059 1.00 17.31 C ANISOU 2513 CB LEU A 393 2504 2506 1566 -573 -997 -82 C ATOM 2514 CG LEU A 393 -41.227 -8.747 10.274 1.00 17.76 C ANISOU 2514 CG LEU A 393 2562 2538 1648 -544 -1061 -89 C ATOM 2515 CD1 LEU A 393 -40.573 -7.693 11.152 1.00 18.38 C ANISOU 2515 CD1 LEU A 393 2706 2587 1690 -642 -1078 -42 C ATOM 2516 CD2 LEU A 393 -42.232 -9.564 11.068 1.00 17.12 C ANISOU 2516 CD2 LEU A 393 2581 2330 1595 -470 -1061 -85 C ATOM 2517 N LEU A 394 -42.632 -7.781 5.996 1.00 25.00 N ANISOU 2517 N LEU A 394 3352 3649 2498 -594 -904 -108 N ATOM 2518 CA LEU A 394 -43.363 -7.120 4.919 1.00 16.80 C ANISOU 2518 CA LEU A 394 2331 2632 1419 -631 -852 -75 C ATOM 2519 C LEU A 394 -44.159 -8.122 4.098 1.00 25.72 C ANISOU 2519 C LEU A 394 3418 3791 2565 -560 -839 -118 C ATOM 2520 O LEU A 394 -45.271 -7.817 3.648 1.00 28.09 O ANISOU 2520 O LEU A 394 3768 4056 2847 -561 -810 -78 O ATOM 2521 CB LEU A 394 -42.403 -6.342 4.022 1.00 17.57 C ANISOU 2521 CB LEU A 394 2355 2849 1470 -723 -832 -65 C ATOM 2522 CG LEU A 394 -41.818 -5.076 4.635 1.00 18.03 C ANISOU 2522 CG LEU A 394 2482 2874 1496 -828 -836 -6 C ATOM 2523 CD1 LEU A 394 -41.116 -4.257 3.570 1.00 33.26 C ANISOU 2523 CD1 LEU A 394 4350 4918 3367 -933 -806 15 C ATOM 2524 CD2 LEU A 394 -42.901 -4.267 5.327 1.00 17.51 C ANISOU 2524 CD2 LEU A 394 2586 2655 1413 -846 -823 61 C ATOM 2525 N ALA A 395 -43.604 -9.319 3.883 1.00 16.70 N ANISOU 2525 N ALA A 395 2183 2712 1449 -503 -865 -197 N ATOM 2526 CA ALA A 395 -44.361 -10.362 3.200 1.00 16.46 C ANISOU 2526 CA ALA A 395 2131 2694 1428 -446 -857 -247 C ATOM 2527 C ALA A 395 -45.677 -10.629 3.920 1.00 15.70 C ANISOU 2527 C ALA A 395 2137 2467 1361 -404 -859 -216 C ATOM 2528 O ALA A 395 -46.760 -10.534 3.324 1.00 20.51 O ANISOU 2528 O ALA A 395 2770 3065 1957 -408 -831 -190 O ATOM 2529 CB ALA A 395 -43.525 -11.638 3.099 1.00 17.01 C ANISOU 2529 CB ALA A 395 2108 2834 1520 -392 -891 -340 C ATOM 2530 N PHE A 396 -45.603 -10.926 5.221 1.00 15.50 N ANISOU 2530 N PHE A 396 2171 2345 1374 -370 -890 -208 N ATOM 2531 CA PHE A 396 -46.813 -11.232 5.980 1.00 14.90 C ANISOU 2531 CA PHE A 396 2195 2140 1328 -333 -885 -177 C ATOM 2532 C PHE A 396 -47.789 -10.061 5.979 1.00 14.56 C ANISOU 2532 C PHE A 396 2232 2043 1256 -377 -850 -94 C ATOM 2533 O PHE A 396 -48.985 -10.233 5.709 1.00 14.25 O ANISOU 2533 O PHE A 396 2222 1970 1221 -361 -838 -70 O ATOM 2534 CB PHE A 396 -46.455 -11.616 7.414 1.00 14.91 C ANISOU 2534 CB PHE A 396 2257 2045 1363 -301 -919 -174 C ATOM 2535 CG PHE A 396 -47.647 -11.722 8.320 1.00 14.40 C ANISOU 2535 CG PHE A 396 2314 1842 1317 -279 -908 -133 C ATOM 2536 CD1 PHE A 396 -47.965 -10.694 9.191 1.00 14.26 C ANISOU 2536 CD1 PHE A 396 2407 1737 1275 -318 -892 -69 C ATOM 2537 CD2 PHE A 396 -48.456 -12.848 8.291 1.00 19.63 C ANISOU 2537 CD2 PHE A 396 2988 2457 2012 -227 -913 -164 C ATOM 2538 CE1 PHE A 396 -49.065 -10.788 10.021 1.00 13.93 C ANISOU 2538 CE1 PHE A 396 2484 1573 1238 -299 -881 -36 C ATOM 2539 CE2 PHE A 396 -49.560 -12.949 9.119 1.00 13.86 C ANISOU 2539 CE2 PHE A 396 2366 1607 1291 -215 -904 -127 C ATOM 2540 CZ PHE A 396 -49.865 -11.918 9.986 1.00 16.89 C ANISOU 2540 CZ PHE A 396 2857 1913 1646 -248 -888 -64 C ATOM 2541 N ILE A 397 -47.299 -8.860 6.296 1.00 14.74 N ANISOU 2541 N ILE A 397 2299 2056 1247 -437 -842 -45 N ATOM 2542 CA ILE A 397 -48.185 -7.707 6.444 1.00 14.58 C ANISOU 2542 CA ILE A 397 2385 1962 1193 -475 -818 38 C ATOM 2543 C ILE A 397 -48.887 -7.398 5.128 1.00 26.62 C ANISOU 2543 C ILE A 397 3863 3560 2690 -488 -796 70 C ATOM 2544 O ILE A 397 -50.117 -7.273 5.076 1.00 34.58 O ANISOU 2544 O ILE A 397 4905 4515 3720 -452 -764 121 O ATOM 2545 CB ILE A 397 -47.401 -6.489 6.965 1.00 19.45 C ANISOU 2545 CB ILE A 397 3069 2550 1771 -550 -814 76 C ATOM 2546 CG1 ILE A 397 -46.934 -6.729 8.404 1.00 22.21 C ANISOU 2546 CG1 ILE A 397 3487 2811 2141 -542 -837 61 C ATOM 2547 CG2 ILE A 397 -48.249 -5.230 6.877 1.00 15.02 C ANISOU 2547 CG2 ILE A 397 2621 1917 1169 -584 -777 161 C ATOM 2548 CD1 ILE A 397 -46.087 -5.607 8.974 1.00 18.51 C ANISOU 2548 CD1 ILE A 397 3084 2316 1632 -631 -840 90 C ATOM 2549 N ILE A 398 -48.117 -7.283 4.041 1.00 15.01 N ANISOU 2549 N ILE A 398 2294 2215 1194 -525 -787 44 N ATOM 2550 CA ILE A 398 -48.706 -6.926 2.752 1.00 15.19 C ANISOU 2550 CA ILE A 398 2277 2316 1180 -548 -767 80 C ATOM 2551 C ILE A 398 -49.685 -7.999 2.292 1.00 15.97 C ANISOU 2551 C ILE A 398 2331 2432 1305 -494 -773 52 C ATOM 2552 O ILE A 398 -50.767 -7.691 1.776 1.00 14.98 O ANISOU 2552 O ILE A 398 2214 2309 1167 -494 -766 116 O ATOM 2553 CB ILE A 398 -47.607 -6.682 1.701 1.00 15.79 C ANISOU 2553 CB ILE A 398 2263 2520 1215 -601 -750 48 C ATOM 2554 CG1 ILE A 398 -46.730 -5.495 2.098 1.00 35.49 C ANISOU 2554 CG1 ILE A 398 4805 5001 3678 -679 -746 90 C ATOM 2555 CG2 ILE A 398 -48.223 -6.440 0.335 1.00 16.07 C ANISOU 2555 CG2 ILE A 398 2261 2636 1209 -624 -728 82 C ATOM 2556 CD1 ILE A 398 -45.554 -5.278 1.168 1.00 16.87 C ANISOU 2556 CD1 ILE A 398 2355 2774 1280 -744 -729 60 C ATOM 2557 N THR A 399 -49.335 -9.274 2.480 1.00 18.91 N ANISOU 2557 N THR A 399 2658 2813 1714 -449 -787 -39 N ATOM 2558 CA THR A 399 -50.200 -10.334 1.969 1.00 19.99 C ANISOU 2558 CA THR A 399 2762 2966 1868 -417 -793 -75 C ATOM 2559 C THR A 399 -51.449 -10.541 2.817 1.00 18.94 C ANISOU 2559 C THR A 399 2696 2721 1777 -383 -800 -28 C ATOM 2560 O THR A 399 -52.453 -11.056 2.311 1.00 15.73 O ANISOU 2560 O THR A 399 2264 2332 1380 -377 -800 -21 O ATOM 2561 CB THR A 399 -49.430 -11.647 1.876 1.00 20.03 C ANISOU 2561 CB THR A 399 2716 3003 1892 -381 -807 -188 C ATOM 2562 OG1 THR A 399 -48.707 -11.855 3.096 1.00 28.70 O ANISOU 2562 OG1 THR A 399 3849 4029 3027 -349 -832 -207 O ATOM 2563 CG2 THR A 399 -48.463 -11.620 0.701 1.00 15.75 C ANISOU 2563 CG2 THR A 399 2092 2586 1306 -409 -788 -240 C ATOM 2564 N TRP A 400 -51.414 -10.163 4.094 1.00 17.43 N ANISOU 2564 N TRP A 400 2587 2418 1617 -359 -792 4 N ATOM 2565 CA TRP A 400 -52.535 -10.419 4.989 1.00 13.81 C ANISOU 2565 CA TRP A 400 2190 1847 1209 -317 -772 41 C ATOM 2566 C TRP A 400 -53.392 -9.190 5.266 1.00 13.82 C ANISOU 2566 C TRP A 400 2249 1790 1214 -313 -726 147 C ATOM 2567 O TRP A 400 -54.472 -9.331 5.848 1.00 13.74 O ANISOU 2567 O TRP A 400 2271 1704 1246 -275 -694 188 O ATOM 2568 CB TRP A 400 -52.028 -10.998 6.315 1.00 15.32 C ANISOU 2568 CB TRP A 400 2450 1940 1429 -287 -788 1 C ATOM 2569 CG TRP A 400 -51.705 -12.460 6.241 1.00 18.99 C ANISOU 2569 CG TRP A 400 2877 2419 1919 -258 -824 -87 C ATOM 2570 CD1 TRP A 400 -50.658 -13.035 5.583 1.00 22.63 C ANISOU 2570 CD1 TRP A 400 3267 2965 2365 -258 -853 -164 C ATOM 2571 CD2 TRP A 400 -52.429 -13.532 6.857 1.00 13.58 C ANISOU 2571 CD2 TRP A 400 2230 1652 1279 -222 -824 -107 C ATOM 2572 NE1 TRP A 400 -50.689 -14.399 5.743 1.00 14.11 N ANISOU 2572 NE1 TRP A 400 2188 1852 1323 -215 -873 -232 N ATOM 2573 CE2 TRP A 400 -51.765 -14.729 6.523 1.00 13.85 C ANISOU 2573 CE2 TRP A 400 2225 1715 1324 -200 -859 -197 C ATOM 2574 CE3 TRP A 400 -53.574 -13.597 7.656 1.00 13.42 C ANISOU 2574 CE3 TRP A 400 2273 1535 1290 -208 -792 -57 C ATOM 2575 CZ2 TRP A 400 -52.208 -15.975 6.958 1.00 13.95 C ANISOU 2575 CZ2 TRP A 400 2274 1651 1375 -169 -869 -236 C ATOM 2576 CZ3 TRP A 400 -54.013 -14.833 8.086 1.00 13.48 C ANISOU 2576 CZ3 TRP A 400 2307 1482 1334 -187 -801 -94 C ATOM 2577 CH2 TRP A 400 -53.332 -16.007 7.735 1.00 13.74 C ANISOU 2577 CH2 TRP A 400 2313 1534 1374 -171 -843 -182 C ATOM 2578 N ALA A 401 -52.947 -7.998 4.868 1.00 17.57 N ANISOU 2578 N ALA A 401 2737 2292 1645 -350 -714 195 N ATOM 2579 CA ALA A 401 -53.754 -6.800 5.092 1.00 14.25 C ANISOU 2579 CA ALA A 401 2382 1801 1232 -335 -663 298 C ATOM 2580 C ALA A 401 -55.090 -6.823 4.353 1.00 17.71 C ANISOU 2580 C ALA A 401 2755 2278 1697 -303 -648 365 C ATOM 2581 O ALA A 401 -56.121 -6.529 4.986 1.00 28.31 O ANISOU 2581 O ALA A 401 4136 3534 3086 -250 -600 429 O ATOM 2582 CB ALA A 401 -52.935 -5.556 4.730 1.00 14.60 C ANISOU 2582 CB ALA A 401 2464 1863 1220 -391 -658 333 C ATOM 2583 N PRO A 402 -55.160 -7.149 3.050 1.00 21.66 N ANISOU 2583 N PRO A 402 3156 2908 2166 -334 -686 357 N ATOM 2584 CA PRO A 402 -56.466 -7.082 2.363 1.00 21.70 C ANISOU 2584 CA PRO A 402 3095 2958 2191 -313 -685 437 C ATOM 2585 C PRO A 402 -57.536 -7.956 2.989 1.00 18.15 C ANISOU 2585 C PRO A 402 2625 2462 1810 -270 -673 435 C ATOM 2586 O PRO A 402 -58.682 -7.512 3.120 1.00 15.38 O ANISOU 2586 O PRO A 402 2256 2084 1502 -226 -640 530 O ATOM 2587 CB PRO A 402 -56.133 -7.538 0.935 1.00 15.41 C ANISOU 2587 CB PRO A 402 2210 2314 1332 -376 -739 399 C ATOM 2588 CG PRO A 402 -54.698 -7.234 0.771 1.00 15.32 C ANISOU 2588 CG PRO A 402 2226 2331 1265 -421 -744 340 C ATOM 2589 CD PRO A 402 -54.081 -7.500 2.109 1.00 26.15 C ANISOU 2589 CD PRO A 402 3668 3594 2674 -394 -727 284 C ATOM 2590 N TYR A 403 -57.197 -9.185 3.383 1.00 19.99 N ANISOU 2590 N TYR A 403 2857 2684 2054 -280 -695 335 N ATOM 2591 CA TYR A 403 -58.185 -10.073 3.990 1.00 15.22 C ANISOU 2591 CA TYR A 403 2242 2032 1508 -255 -682 332 C ATOM 2592 C TYR A 403 -58.752 -9.475 5.273 1.00 21.87 C ANISOU 2592 C TYR A 403 3163 2745 2402 -196 -611 394 C ATOM 2593 O TYR A 403 -59.971 -9.474 5.485 1.00 33.75 O ANISOU 2593 O TYR A 403 4633 4233 3958 -165 -574 461 O ATOM 2594 CB TYR A 403 -57.557 -11.441 4.256 1.00 16.55 C ANISOU 2594 CB TYR A 403 2424 2189 1676 -273 -715 213 C ATOM 2595 CG TYR A 403 -58.399 -12.363 5.108 1.00 19.52 C ANISOU 2595 CG TYR A 403 2821 2489 2109 -256 -697 204 C ATOM 2596 CD1 TYR A 403 -59.517 -13.001 4.584 1.00 14.92 C ANISOU 2596 CD1 TYR A 403 2163 1960 1548 -283 -710 224 C ATOM 2597 CD2 TYR A 403 -58.066 -12.606 6.436 1.00 25.16 C ANISOU 2597 CD2 TYR A 403 3631 3082 2846 -225 -671 178 C ATOM 2598 CE1 TYR A 403 -60.286 -13.850 5.362 1.00 21.31 C ANISOU 2598 CE1 TYR A 403 2990 2701 2406 -281 -689 218 C ATOM 2599 CE2 TYR A 403 -58.825 -13.452 7.222 1.00 25.14 C ANISOU 2599 CE2 TYR A 403 3656 3007 2888 -217 -650 173 C ATOM 2600 CZ TYR A 403 -59.934 -14.071 6.681 1.00 30.30 C ANISOU 2600 CZ TYR A 403 4231 3713 3567 -246 -655 193 C ATOM 2601 OH TYR A 403 -60.690 -14.914 7.464 1.00 23.92 O ANISOU 2601 OH TYR A 403 3450 2836 2801 -252 -630 191 O ATOM 2602 N ASN A 404 -57.881 -8.951 6.141 1.00 14.25 N ANISOU 2602 N ASN A 404 2304 1691 1421 -186 -587 373 N ATOM 2603 CA ASN A 404 -58.349 -8.364 7.393 1.00 14.32 C ANISOU 2603 CA ASN A 404 2413 1567 1461 -139 -511 421 C ATOM 2604 C ASN A 404 -59.212 -7.136 7.140 1.00 14.89 C ANISOU 2604 C ASN A 404 2478 1624 1555 -94 -452 535 C ATOM 2605 O ASN A 404 -60.208 -6.911 7.842 1.00 16.38 O ANISOU 2605 O ASN A 404 2690 1738 1795 -37 -377 592 O ATOM 2606 CB ASN A 404 -57.159 -8.014 8.282 1.00 17.16 C ANISOU 2606 CB ASN A 404 2894 1846 1782 -157 -513 373 C ATOM 2607 CG ASN A 404 -56.403 -9.243 8.743 1.00 13.66 C ANISOU 2607 CG ASN A 404 2461 1398 1330 -179 -567 276 C ATOM 2608 OD1 ASN A 404 -56.737 -9.844 9.764 1.00 13.59 O ANISOU 2608 OD1 ASN A 404 2513 1305 1346 -160 -546 261 O ATOM 2609 ND2 ASN A 404 -55.383 -9.627 7.988 1.00 13.53 N ANISOU 2609 ND2 ASN A 404 2386 1472 1281 -215 -634 213 N ATOM 2610 N VAL A 405 -58.844 -6.324 6.144 1.00 19.72 N ANISOU 2610 N VAL A 405 3060 2304 2129 -114 -478 573 N ATOM 2611 CA VAL A 405 -59.689 -5.193 5.766 1.00 19.24 C ANISOU 2611 CA VAL A 405 2985 2232 2092 -62 -430 694 C ATOM 2612 C VAL A 405 -61.061 -5.681 5.320 1.00 21.70 C ANISOU 2612 C VAL A 405 3168 2613 2463 -26 -431 757 C ATOM 2613 O VAL A 405 -62.094 -5.099 5.680 1.00 16.93 O ANISOU 2613 O VAL A 405 2556 1957 1918 51 -360 850 O ATOM 2614 CB VAL A 405 -59.004 -4.356 4.671 1.00 16.06 C ANISOU 2614 CB VAL A 405 2573 1900 1628 -105 -472 724 C ATOM 2615 CG1 VAL A 405 -59.943 -3.273 4.164 1.00 16.94 C ANISOU 2615 CG1 VAL A 405 2663 2007 1769 -43 -435 861 C ATOM 2616 CG2 VAL A 405 -57.722 -3.747 5.209 1.00 22.26 C ANISOU 2616 CG2 VAL A 405 3485 2612 2360 -149 -463 675 C ATOM 2617 N MET A 406 -61.094 -6.764 4.538 1.00 16.13 N ANISOU 2617 N MET A 406 2359 2027 1742 -82 -508 706 N ATOM 2618 CA MET A 406 -62.367 -7.325 4.102 1.00 16.68 C ANISOU 2618 CA MET A 406 2302 2175 1860 -73 -523 761 C ATOM 2619 C MET A 406 -63.185 -7.834 5.279 1.00 28.36 C ANISOU 2619 C MET A 406 3796 3569 3411 -30 -454 763 C ATOM 2620 O MET A 406 -64.420 -7.779 5.246 1.00 31.84 O ANISOU 2620 O MET A 406 4145 4038 3914 10 -424 850 O ATOM 2621 CB MET A 406 -62.131 -8.447 3.095 1.00 16.56 C ANISOU 2621 CB MET A 406 2204 2290 1799 -160 -617 686 C ATOM 2622 CG MET A 406 -61.472 -7.987 1.814 1.00 16.74 C ANISOU 2622 CG MET A 406 2199 2417 1743 -209 -679 691 C ATOM 2623 SD MET A 406 -60.937 -9.367 0.794 1.00 18.85 S ANISOU 2623 SD MET A 406 2411 2809 1941 -312 -767 568 S ATOM 2624 CE MET A 406 -59.818 -8.526 -0.317 1.00 18.25 C ANISOU 2624 CE MET A 406 2352 2815 1768 -356 -798 566 C ATOM 2625 N VAL A 407 -62.522 -8.333 6.323 1.00 16.07 N ANISOU 2625 N VAL A 407 2348 1913 1845 -40 -430 673 N ATOM 2626 CA VAL A 407 -63.240 -8.744 7.526 1.00 28.45 C ANISOU 2626 CA VAL A 407 3954 3389 3469 -5 -354 677 C ATOM 2627 C VAL A 407 -63.865 -7.532 8.208 1.00 16.77 C ANISOU 2627 C VAL A 407 2526 1815 2031 85 -243 771 C ATOM 2628 O VAL A 407 -65.056 -7.535 8.555 1.00 34.78 O ANISOU 2628 O VAL A 407 4745 4088 4380 136 -174 841 O ATOM 2629 CB VAL A 407 -62.299 -9.506 8.477 1.00 31.90 C ANISOU 2629 CB VAL A 407 4509 3738 3873 -38 -363 567 C ATOM 2630 CG1 VAL A 407 -62.995 -9.788 9.799 1.00 34.31 C ANISOU 2630 CG1 VAL A 407 4879 3935 4220 -6 -274 578 C ATOM 2631 CG2 VAL A 407 -61.826 -10.799 7.834 1.00 15.11 C ANISOU 2631 CG2 VAL A 407 2329 1691 1720 -109 -457 476 C ATOM 2632 N LEU A 408 -63.070 -6.474 8.399 1.00 16.64 N ANISOU 2632 N LEU A 408 2623 1725 1975 105 -218 775 N ATOM 2633 CA LEU A 408 -63.580 -5.268 9.047 1.00 17.33 C ANISOU 2633 CA LEU A 408 2790 1700 2094 192 -104 855 C ATOM 2634 C LEU A 408 -64.773 -4.696 8.292 1.00 22.73 C ANISOU 2634 C LEU A 408 3340 2452 2845 266 -78 983 C ATOM 2635 O LEU A 408 -65.798 -4.357 8.895 1.00 23.89 O ANISOU 2635 O LEU A 408 3473 2543 3061 352 27 1053 O ATOM 2636 CB LEU A 408 -62.470 -4.223 9.167 1.00 24.33 C ANISOU 2636 CB LEU A 408 3820 2507 2916 178 -100 837 C ATOM 2637 CG LEU A 408 -61.322 -4.524 10.129 1.00 16.46 C ANISOU 2637 CG LEU A 408 2971 1426 1857 117 -112 731 C ATOM 2638 CD1 LEU A 408 -60.422 -3.309 10.260 1.00 16.61 C ANISOU 2638 CD1 LEU A 408 3128 1364 1817 98 -96 734 C ATOM 2639 CD2 LEU A 408 -61.852 -4.958 11.488 1.00 28.51 C ANISOU 2639 CD2 LEU A 408 4579 2846 3407 146 -27 709 C ATOM 2640 N ILE A 409 -64.659 -4.576 6.967 1.00 24.79 N ANISOU 2640 N ILE A 409 3497 2838 3083 235 -172 1020 N ATOM 2641 CA ILE A 409 -65.777 -4.060 6.182 1.00 31.61 C ANISOU 2641 CA ILE A 409 4224 3782 4006 301 -169 1154 C ATOM 2642 C ILE A 409 -66.965 -5.009 6.265 1.00 33.76 C ANISOU 2642 C ILE A 409 4345 4133 4348 305 -166 1181 C ATOM 2643 O ILE A 409 -68.121 -4.576 6.348 1.00 33.52 O ANISOU 2643 O ILE A 409 4224 4112 4400 395 -101 1294 O ATOM 2644 CB ILE A 409 -65.343 -3.812 4.726 1.00 19.59 C ANISOU 2644 CB ILE A 409 2633 2384 2425 247 -282 1184 C ATOM 2645 CG1 ILE A 409 -64.277 -2.720 4.674 1.00 19.39 C ANISOU 2645 CG1 ILE A 409 2754 2276 2338 244 -269 1178 C ATOM 2646 CG2 ILE A 409 -66.536 -3.425 3.866 1.00 20.83 C ANISOU 2646 CG2 ILE A 409 2632 2645 2638 306 -303 1330 C ATOM 2647 CD1 ILE A 409 -63.837 -2.364 3.270 1.00 27.23 C ANISOU 2647 CD1 ILE A 409 3695 3386 3267 189 -366 1216 C ATOM 2648 N ASN A 410 -66.699 -6.318 6.272 1.00 31.49 N ANISOU 2648 N ASN A 410 4032 3900 4032 208 -230 1080 N ATOM 2649 CA ASN A 410 -67.769 -7.305 6.354 1.00 27.74 C ANISOU 2649 CA ASN A 410 3426 3498 3614 185 -233 1097 C ATOM 2650 C ASN A 410 -68.502 -7.261 7.688 1.00 25.57 C ANISOU 2650 C ASN A 410 3191 3115 3411 256 -97 1119 C ATOM 2651 O ASN A 410 -69.620 -7.780 7.779 1.00 21.83 O ANISOU 2651 O ASN A 410 2588 2703 3003 258 -72 1171 O ATOM 2652 CB ASN A 410 -67.215 -8.713 6.119 1.00 32.10 C ANISOU 2652 CB ASN A 410 3979 4103 4113 64 -326 973 C ATOM 2653 CG ASN A 410 -68.311 -9.743 5.912 1.00 32.54 C ANISOU 2653 CG ASN A 410 3892 4257 4215 9 -354 994 C ATOM 2654 OD1 ASN A 410 -69.365 -9.438 5.354 1.00 47.01 O ANISOU 2654 OD1 ASN A 410 5575 6188 6098 34 -362 1108 O ATOM 2655 ND2 ASN A 410 -68.071 -10.968 6.366 1.00 21.29 N ANISOU 2655 ND2 ASN A 410 2513 2803 2773 -68 -372 891 N ATOM 2656 N THR A 411 -67.909 -6.661 8.724 1.00 30.17 N ANISOU 2656 N THR A 411 3948 3541 3974 304 -5 1082 N ATOM 2657 CA THR A 411 -68.619 -6.568 9.998 1.00 37.81 C ANISOU 2657 CA THR A 411 4967 4401 4996 371 138 1101 C ATOM 2658 C THR A 411 -69.897 -5.742 9.882 1.00 47.52 C ANISOU 2658 C THR A 411 6077 5655 6323 490 231 1243 C ATOM 2659 O THR A 411 -70.839 -5.952 10.654 1.00 55.52 O ANISOU 2659 O THR A 411 7048 6645 7403 535 340 1278 O ATOM 2660 CB THR A 411 -67.713 -5.977 11.079 1.00 36.38 C ANISOU 2660 CB THR A 411 5012 4048 4761 391 214 1036 C ATOM 2661 OG1 THR A 411 -67.265 -4.676 10.677 1.00 43.47 O ANISOU 2661 OG1 THR A 411 5976 4901 5639 447 225 1082 O ATOM 2662 CG2 THR A 411 -66.511 -6.876 11.320 1.00 31.71 C ANISOU 2662 CG2 THR A 411 4522 3439 4087 283 124 906 C ATOM 2663 N PHE A 412 -69.959 -4.809 8.930 1.00 41.78 N ANISOU 2663 N PHE A 412 5290 4977 5607 545 194 1333 N ATOM 2664 CA PHE A 412 -71.116 -3.926 8.813 1.00 44.75 C ANISOU 2664 CA PHE A 412 5556 5366 6081 681 281 1479 C ATOM 2665 C PHE A 412 -71.692 -3.796 7.407 1.00 41.90 C ANISOU 2665 C PHE A 412 4992 5177 5750 685 168 1593 C ATOM 2666 O PHE A 412 -72.845 -3.371 7.280 1.00 35.08 O ANISOU 2666 O PHE A 412 3980 4363 4984 788 222 1725 O ATOM 2667 CB PHE A 412 -70.774 -2.523 9.337 1.00 39.88 C ANISOU 2667 CB PHE A 412 5111 4579 5462 795 397 1509 C ATOM 2668 CG PHE A 412 -69.596 -1.892 8.658 1.00 30.68 C ANISOU 2668 CG PHE A 412 4059 3388 4210 751 308 1480 C ATOM 2669 CD1 PHE A 412 -68.315 -2.085 9.147 1.00 29.12 C ANISOU 2669 CD1 PHE A 412 4044 3105 3915 659 283 1349 C ATOM 2670 CD2 PHE A 412 -69.770 -1.103 7.535 1.00 27.15 C ANISOU 2670 CD2 PHE A 412 3531 3008 3776 798 248 1591 C ATOM 2671 CE1 PHE A 412 -67.227 -1.505 8.526 1.00 26.02 C ANISOU 2671 CE1 PHE A 412 3741 2700 3443 610 207 1325 C ATOM 2672 CE2 PHE A 412 -68.687 -0.520 6.910 1.00 39.30 C ANISOU 2672 CE2 PHE A 412 5176 4527 5228 744 173 1561 C ATOM 2673 CZ PHE A 412 -67.413 -0.722 7.407 1.00 40.29 C ANISOU 2673 CZ PHE A 412 5475 4572 5262 650 157 1432 C ATOM 2674 N CYS A 413 -70.947 -4.130 6.355 1.00 37.17 N ANISOU 2674 N CYS A 413 4379 4675 5071 579 16 1552 N ATOM 2675 CA CYS A 413 -71.469 -4.126 4.987 1.00 33.25 C ANISOU 2675 CA CYS A 413 3700 4355 4581 556 -107 1652 C ATOM 2676 C CYS A 413 -71.045 -5.424 4.311 1.00 33.30 C ANISOU 2676 C CYS A 413 3656 4486 4510 390 -248 1551 C ATOM 2677 O CYS A 413 -69.926 -5.514 3.792 1.00 43.02 O ANISOU 2677 O CYS A 413 4983 5719 5645 312 -326 1466 O ATOM 2678 CB CYS A 413 -70.968 -2.919 4.193 1.00 44.18 C ANISOU 2678 CB CYS A 413 5138 5721 5926 608 -143 1725 C ATOM 2679 SG CYS A 413 -71.640 -2.876 2.514 1.00 50.88 S ANISOU 2679 SG CYS A 413 5771 6790 6769 578 -302 1862 S ATOM 2680 N ALA A 414 -71.935 -6.426 4.313 1.00 33.52 N ANISOU 2680 N ALA A 414 3539 4616 4581 332 -273 1559 N ATOM 2681 CA ALA A 414 -71.602 -7.682 3.646 1.00 29.27 C ANISOU 2681 CA ALA A 414 2966 4185 3970 172 -401 1461 C ATOM 2682 C ALA A 414 -71.602 -7.546 2.129 1.00 28.39 C ANISOU 2682 C ALA A 414 2753 4233 3801 111 -544 1518 C ATOM 2683 O ALA A 414 -70.670 -8.059 1.488 1.00 36.05 O ANISOU 2683 O ALA A 414 3792 5236 4670 6 -633 1414 O ATOM 2684 CB ALA A 414 -72.546 -8.792 4.108 1.00 30.98 C ANISOU 2684 CB ALA A 414 3075 4455 4243 110 -385 1451 C ATOM 2685 N PRO A 415 -72.584 -6.884 1.495 1.00 32.71 N ANISOU 2685 N PRO A 415 3141 4884 4402 174 -572 1681 N ATOM 2686 CA PRO A 415 -72.547 -6.779 0.027 1.00 35.44 C ANISOU 2686 CA PRO A 415 3405 5387 4674 102 -720 1737 C ATOM 2687 C PRO A 415 -71.415 -5.924 -0.502 1.00 39.49 C ANISOU 2687 C PRO A 415 4058 5848 5101 119 -742 1719 C ATOM 2688 O PRO A 415 -71.223 -5.900 -1.722 1.00 30.30 O ANISOU 2688 O PRO A 415 2860 4799 3852 39 -852 1730 O ATOM 2689 CB PRO A 415 -73.907 -6.157 -0.320 1.00 31.93 C ANISOU 2689 CB PRO A 415 2758 5049 4324 192 -731 1936 C ATOM 2690 CG PRO A 415 -74.749 -6.404 0.855 1.00 32.57 C ANISOU 2690 CG PRO A 415 2780 5072 4525 262 -606 1954 C ATOM 2691 CD PRO A 415 -73.849 -6.347 2.028 1.00 27.14 C ANISOU 2691 CD PRO A 415 2304 4183 3827 301 -479 1825 C ATOM 2692 N CYS A 416 -70.672 -5.217 0.357 1.00 41.71 N ANISOU 2692 N CYS A 416 4502 5954 5391 205 -632 1676 N ATOM 2693 CA CYS A 416 -69.550 -4.404 -0.109 1.00 41.44 C ANISOU 2693 CA CYS A 416 4604 5868 5272 204 -650 1656 C ATOM 2694 C CYS A 416 -68.382 -5.245 -0.615 1.00 32.14 C ANISOU 2694 C CYS A 416 3504 4733 3976 59 -730 1499 C ATOM 2695 O CYS A 416 -67.549 -4.738 -1.376 1.00 29.86 O ANISOU 2695 O CYS A 416 3279 4465 3600 22 -777 1492 O ATOM 2696 CB CYS A 416 -69.064 -3.478 1.011 1.00 41.76 C ANISOU 2696 CB CYS A 416 4807 5708 5350 314 -513 1644 C ATOM 2697 SG CYS A 416 -70.151 -2.079 1.384 1.00 43.70 S ANISOU 2697 SG CYS A 416 5012 5874 5717 511 -404 1836 S ATOM 2698 N ILE A 417 -68.297 -6.505 -0.213 1.00 26.98 N ANISOU 2698 N ILE A 417 2847 4087 3316 -21 -739 1377 N ATOM 2699 CA ILE A 417 -67.181 -7.375 -0.553 1.00 32.96 C ANISOU 2699 CA ILE A 417 3685 4864 3976 -137 -794 1219 C ATOM 2700 C ILE A 417 -67.716 -8.543 -1.374 1.00 31.65 C ANISOU 2700 C ILE A 417 3406 4846 3774 -256 -896 1188 C ATOM 2701 O ILE A 417 -68.304 -9.481 -0.832 1.00 21.91 O ANISOU 2701 O ILE A 417 2130 3607 2588 -287 -883 1149 O ATOM 2702 CB ILE A 417 -66.445 -7.868 0.707 1.00 38.93 C ANISOU 2702 CB ILE A 417 4570 5472 4750 -125 -714 1090 C ATOM 2703 CG1 ILE A 417 -66.116 -6.689 1.628 1.00 41.05 C ANISOU 2703 CG1 ILE A 417 4951 5589 5056 -14 -609 1131 C ATOM 2704 CG2 ILE A 417 -65.164 -8.586 0.327 1.00 19.23 C ANISOU 2704 CG2 ILE A 417 2156 2990 2161 -218 -766 940 C ATOM 2705 CD1 ILE A 417 -65.141 -5.694 1.028 1.00 19.74 C ANISOU 2705 CD1 ILE A 417 2333 2881 2286 -16 -628 1144 C ATOM 2706 N PRO A 418 -67.543 -8.510 -2.695 1.00 25.07 N ANISOU 2706 N PRO A 418 2532 4145 2847 -336 -997 1205 N ATOM 2707 CA PRO A 418 -67.939 -9.651 -3.530 1.00 29.71 C ANISOU 2707 CA PRO A 418 3061 4837 3390 -463 -1060 1127 C ATOM 2708 C PRO A 418 -67.102 -10.886 -3.230 1.00 36.34 C ANISOU 2708 C PRO A 418 3990 5635 4182 -543 -1065 952 C ATOM 2709 O PRO A 418 -66.089 -10.844 -2.531 1.00 35.31 O ANISOU 2709 O PRO A 418 3968 5403 4045 -507 -1022 875 O ATOM 2710 CB PRO A 418 -67.699 -9.150 -4.958 1.00 32.65 C ANISOU 2710 CB PRO A 418 3442 5281 3681 -506 -1090 1129 C ATOM 2711 CG PRO A 418 -67.731 -7.665 -4.855 1.00 23.96 C ANISOU 2711 CG PRO A 418 2345 4144 2616 -395 -1057 1263 C ATOM 2712 CD PRO A 418 -67.186 -7.331 -3.501 1.00 23.34 C ANISOU 2712 CD PRO A 418 2344 3936 2587 -303 -993 1264 C ATOM 2713 N ASN A 419 -67.543 -12.012 -3.794 1.00 35.49 N ANISOU 2713 N ASN A 419 3850 5586 4047 -647 -1102 877 N ATOM 2714 CA ASN A 419 -66.844 -13.271 -3.569 1.00 31.36 C ANISOU 2714 CA ASN A 419 3417 5010 3487 -716 -1099 709 C ATOM 2715 C ASN A 419 -65.510 -13.318 -4.303 1.00 31.51 C ANISOU 2715 C ASN A 419 3544 5011 3419 -730 -1080 586 C ATOM 2716 O ASN A 419 -64.583 -14.009 -3.859 1.00 41.72 O ANISOU 2716 O ASN A 419 4926 6228 4696 -733 -1057 458 O ATOM 2717 CB ASN A 419 -67.734 -14.437 -3.989 1.00 34.29 C ANISOU 2717 CB ASN A 419 3740 5435 3854 -821 -1135 672 C ATOM 2718 CG ASN A 419 -68.941 -14.589 -3.090 1.00 47.27 C ANISOU 2718 CG ASN A 419 5274 7093 5594 -818 -1143 774 C ATOM 2719 OD1 ASN A 419 -68.850 -14.386 -1.880 1.00 49.75 O ANISOU 2719 OD1 ASN A 419 5606 7317 5981 -745 -1094 797 O ATOM 2720 ND2 ASN A 419 -70.081 -14.939 -3.676 1.00 57.87 N ANISOU 2720 ND2 ASN A 419 6516 8527 6945 -888 -1179 829 N ATOM 2721 N THR A 420 -65.388 -12.588 -5.412 1.00 24.80 N ANISOU 2721 N THR A 420 2680 4226 2515 -735 -1089 627 N ATOM 2722 CA THR A 420 -64.131 -12.576 -6.152 1.00 31.86 C ANISOU 2722 CA THR A 420 3661 5116 3330 -751 -1065 523 C ATOM 2723 C THR A 420 -63.005 -11.985 -5.309 1.00 32.83 C ANISOU 2723 C THR A 420 3853 5154 3465 -679 -1020 497 C ATOM 2724 O THR A 420 -61.919 -12.570 -5.201 1.00 36.01 O ANISOU 2724 O THR A 420 4329 5512 3841 -683 -991 367 O ATOM 2725 CB THR A 420 -64.300 -11.796 -7.457 1.00 32.47 C ANISOU 2725 CB THR A 420 3707 5283 3347 -778 -1087 595 C ATOM 2726 OG1 THR A 420 -65.363 -12.371 -8.227 1.00 28.12 O ANISOU 2726 OG1 THR A 420 3094 4813 2779 -853 -1137 622 O ATOM 2727 CG2 THR A 420 -63.014 -11.836 -8.270 1.00 31.33 C ANISOU 2727 CG2 THR A 420 3642 5144 3118 -804 -1058 491 C ATOM 2728 N VAL A 421 -63.251 -10.831 -4.687 1.00 20.29 N ANISOU 2728 N VAL A 421 2247 3541 1921 -608 -1013 623 N ATOM 2729 CA VAL A 421 -62.203 -10.194 -3.897 1.00 42.07 C ANISOU 2729 CA VAL A 421 5085 6217 4682 -551 -974 608 C ATOM 2730 C VAL A 421 -61.924 -10.978 -2.616 1.00 27.59 C ANISOU 2730 C VAL A 421 3300 4293 2890 -533 -964 536 C ATOM 2731 O VAL A 421 -60.780 -11.012 -2.143 1.00 33.63 O ANISOU 2731 O VAL A 421 4146 4989 3642 -514 -931 450 O ATOM 2732 CB VAL A 421 -62.569 -8.725 -3.615 1.00 32.97 C ANISOU 2732 CB VAL A 421 3923 5043 3560 -477 -962 769 C ATOM 2733 CG1 VAL A 421 -62.512 -7.919 -4.903 1.00 30.19 C ANISOU 2733 CG1 VAL A 421 3554 4766 3153 -501 -972 821 C ATOM 2734 CG2 VAL A 421 -63.942 -8.630 -3.010 1.00 22.89 C ANISOU 2734 CG2 VAL A 421 2564 3762 2369 -424 -973 896 C ATOM 2735 N TRP A 422 -62.948 -11.613 -2.034 1.00 18.62 N ANISOU 2735 N TRP A 422 2121 3131 1823 -529 -964 557 N ATOM 2736 CA TRP A 422 -62.708 -12.564 -0.952 1.00 17.96 C ANISOU 2736 CA TRP A 422 2100 2934 1790 -513 -923 458 C ATOM 2737 C TRP A 422 -61.712 -13.630 -1.388 1.00 27.81 C ANISOU 2737 C TRP A 422 3402 4194 2972 -575 -951 303 C ATOM 2738 O TRP A 422 -60.707 -13.881 -0.706 1.00 28.50 O ANISOU 2738 O TRP A 422 3570 4190 3068 -537 -916 217 O ATOM 2739 CB TRP A 422 -64.021 -13.219 -0.517 1.00 18.47 C ANISOU 2739 CB TRP A 422 2100 2994 1923 -529 -925 500 C ATOM 2740 CG TRP A 422 -64.828 -12.441 0.487 1.00 27.07 C ANISOU 2740 CG TRP A 422 3167 4011 3107 -437 -855 615 C ATOM 2741 CD1 TRP A 422 -66.088 -11.943 0.316 1.00 28.21 C ANISOU 2741 CD1 TRP A 422 3196 4219 3302 -416 -857 751 C ATOM 2742 CD2 TRP A 422 -64.439 -12.095 1.823 1.00 27.84 C ANISOU 2742 CD2 TRP A 422 3361 3960 3258 -353 -768 604 C ATOM 2743 NE1 TRP A 422 -66.505 -11.302 1.460 1.00 28.70 N ANISOU 2743 NE1 TRP A 422 3279 4176 3450 -314 -763 820 N ATOM 2744 CE2 TRP A 422 -65.511 -11.381 2.399 1.00 29.39 C ANISOU 2744 CE2 TRP A 422 3504 4129 3533 -281 -707 728 C ATOM 2745 CE3 TRP A 422 -63.289 -12.317 2.586 1.00 24.67 C ANISOU 2745 CE3 TRP A 422 3082 3450 2841 -332 -738 503 C ATOM 2746 CZ2 TRP A 422 -65.464 -10.884 3.703 1.00 28.13 C ANISOU 2746 CZ2 TRP A 422 3431 3831 3428 -196 -609 744 C ATOM 2747 CZ3 TRP A 422 -63.245 -11.823 3.880 1.00 28.02 C ANISOU 2747 CZ3 TRP A 422 3587 3744 3316 -257 -657 527 C ATOM 2748 CH2 TRP A 422 -64.326 -11.114 4.424 1.00 16.97 C ANISOU 2748 CH2 TRP A 422 2151 2313 1985 -193 -589 642 C ATOM 2749 N THR A 423 -61.978 -14.260 -2.539 1.00 18.49 N ANISOU 2749 N THR A 423 2182 3105 1739 -650 -985 259 N ATOM 2750 CA THR A 423 -61.054 -15.246 -3.093 1.00 21.10 C ANISOU 2750 CA THR A 423 2569 3422 2025 -674 -967 106 C ATOM 2751 C THR A 423 -59.653 -14.668 -3.237 1.00 23.13 C ANISOU 2751 C THR A 423 2871 3667 2249 -628 -929 58 C ATOM 2752 O THR A 423 -58.656 -15.350 -2.962 1.00 27.37 O ANISOU 2752 O THR A 423 3463 4153 2785 -607 -908 -56 O ATOM 2753 CB THR A 423 -61.563 -15.737 -4.449 1.00 25.98 C ANISOU 2753 CB THR A 423 3152 4128 2593 -746 -986 84 C ATOM 2754 OG1 THR A 423 -62.932 -16.144 -4.332 1.00 23.55 O ANISOU 2754 OG1 THR A 423 2785 3846 2316 -798 -1024 147 O ATOM 2755 CG2 THR A 423 -60.733 -16.911 -4.937 1.00 34.17 C ANISOU 2755 CG2 THR A 423 4255 5138 3590 -768 -968 -72 C ATOM 2756 N ILE A 424 -59.562 -13.401 -3.654 1.00 18.08 N ANISOU 2756 N ILE A 424 2207 3076 1587 -614 -923 149 N ATOM 2757 CA ILE A 424 -58.260 -12.751 -3.779 1.00 22.02 C ANISOU 2757 CA ILE A 424 2742 3570 2054 -587 -888 117 C ATOM 2758 C ILE A 424 -57.558 -12.684 -2.427 1.00 22.71 C ANISOU 2758 C ILE A 424 2885 3561 2183 -535 -873 92 C ATOM 2759 O ILE A 424 -56.353 -12.937 -2.329 1.00 35.41 O ANISOU 2759 O ILE A 424 4524 5150 3780 -517 -849 1 O ATOM 2760 CB ILE A 424 -58.417 -11.355 -4.409 1.00 18.06 C ANISOU 2760 CB ILE A 424 2216 3127 1521 -591 -889 235 C ATOM 2761 CG1 ILE A 424 -58.980 -11.469 -5.827 1.00 19.10 C ANISOU 2761 CG1 ILE A 424 2302 3355 1599 -650 -909 253 C ATOM 2762 CG2 ILE A 424 -57.081 -10.627 -4.429 1.00 17.74 C ANISOU 2762 CG2 ILE A 424 2215 3078 1447 -579 -852 210 C ATOM 2763 CD1 ILE A 424 -59.272 -10.136 -6.479 1.00 19.64 C ANISOU 2763 CD1 ILE A 424 2346 3477 1638 -656 -918 382 C ATOM 2764 N GLY A 425 -58.296 -12.355 -1.363 1.00 17.00 N ANISOU 2764 N GLY A 425 2175 2775 1508 -510 -891 177 N ATOM 2765 CA GLY A 425 -57.676 -12.285 -0.045 1.00 21.55 C ANISOU 2765 CA GLY A 425 2823 3225 2140 -446 -849 150 C ATOM 2766 C GLY A 425 -57.178 -13.635 0.441 1.00 37.05 C ANISOU 2766 C GLY A 425 4824 5131 4124 -441 -853 26 C ATOM 2767 O GLY A 425 -56.026 -13.772 0.884 1.00 42.59 O ANISOU 2767 O GLY A 425 5567 5792 4824 -414 -842 -42 O ATOM 2768 N TYR A 426 -58.044 -14.651 0.366 1.00 15.83 N ANISOU 2768 N TYR A 426 2120 2439 1456 -470 -872 2 N ATOM 2769 CA TYR A 426 -57.649 -16.016 0.703 1.00 15.84 C ANISOU 2769 CA TYR A 426 2167 2378 1472 -469 -877 -115 C ATOM 2770 C TYR A 426 -56.362 -16.407 -0.020 1.00 31.72 C ANISOU 2770 C TYR A 426 4183 4440 3428 -474 -881 -225 C ATOM 2771 O TYR A 426 -55.345 -16.753 0.605 1.00 36.60 O ANISOU 2771 O TYR A 426 4845 4995 4067 -423 -871 -290 O ATOM 2772 CB TYR A 426 -58.781 -16.984 0.338 1.00 16.44 C ANISOU 2772 CB TYR A 426 2221 2473 1553 -533 -904 -126 C ATOM 2773 CG TYR A 426 -59.971 -16.999 1.280 1.00 16.38 C ANISOU 2773 CG TYR A 426 2210 2396 1619 -522 -885 -44 C ATOM 2774 CD1 TYR A 426 -60.595 -15.822 1.675 1.00 37.73 C ANISOU 2774 CD1 TYR A 426 4877 5102 4357 -484 -857 82 C ATOM 2775 CD2 TYR A 426 -60.488 -18.199 1.750 1.00 16.65 C ANISOU 2775 CD2 TYR A 426 2280 2360 1686 -551 -888 -91 C ATOM 2776 CE1 TYR A 426 -61.685 -15.838 2.528 1.00 16.32 C ANISOU 2776 CE1 TYR A 426 2154 2333 1714 -468 -825 155 C ATOM 2777 CE2 TYR A 426 -61.580 -18.225 2.599 1.00 16.72 C ANISOU 2777 CE2 TYR A 426 2279 2316 1759 -550 -862 -15 C ATOM 2778 CZ TYR A 426 -62.173 -17.043 2.985 1.00 32.79 C ANISOU 2778 CZ TYR A 426 4266 4363 3830 -506 -827 107 C ATOM 2779 OH TYR A 426 -63.257 -17.067 3.831 1.00 44.50 O ANISOU 2779 OH TYR A 426 5732 5797 5377 -498 -785 180 O ATOM 2780 N TRP A 427 -56.388 -16.337 -1.353 1.00 16.62 N ANISOU 2780 N TRP A 427 2217 2632 1464 -509 -871 -241 N ATOM 2781 CA TRP A 427 -55.216 -16.735 -2.119 1.00 24.55 C ANISOU 2781 CA TRP A 427 3222 3677 2429 -498 -850 -344 C ATOM 2782 C TRP A 427 -54.020 -15.833 -1.857 1.00 16.60 C ANISOU 2782 C TRP A 427 2209 2682 1415 -459 -830 -333 C ATOM 2783 O TRP A 427 -52.889 -16.242 -2.127 1.00 19.06 O ANISOU 2783 O TRP A 427 2522 3012 1708 -441 -816 -420 O ATOM 2784 CB TRP A 427 -55.542 -16.770 -3.614 1.00 17.83 C ANISOU 2784 CB TRP A 427 2338 2919 1517 -553 -846 -349 C ATOM 2785 CG TRP A 427 -56.276 -18.009 -4.008 1.00 18.50 C ANISOU 2785 CG TRP A 427 2443 2990 1595 -598 -864 -411 C ATOM 2786 CD1 TRP A 427 -57.570 -18.097 -4.422 1.00 18.97 C ANISOU 2786 CD1 TRP A 427 2476 3084 1650 -659 -891 -352 C ATOM 2787 CD2 TRP A 427 -55.765 -19.348 -3.997 1.00 20.71 C ANISOU 2787 CD2 TRP A 427 2781 3214 1873 -590 -858 -542 C ATOM 2788 NE1 TRP A 427 -57.896 -19.408 -4.682 1.00 19.66 N ANISOU 2788 NE1 TRP A 427 2601 3139 1728 -699 -901 -440 N ATOM 2789 CE2 TRP A 427 -56.804 -20.195 -4.429 1.00 19.64 C ANISOU 2789 CE2 TRP A 427 2659 3074 1728 -655 -878 -559 C ATOM 2790 CE3 TRP A 427 -54.528 -19.913 -3.671 1.00 19.90 C ANISOU 2790 CE3 TRP A 427 2721 3065 1775 -536 -840 -644 C ATOM 2791 CZ2 TRP A 427 -56.645 -21.574 -4.543 1.00 24.56 C ANISOU 2791 CZ2 TRP A 427 3353 3634 2345 -668 -874 -679 C ATOM 2792 CZ3 TRP A 427 -54.372 -21.283 -3.784 1.00 19.60 C ANISOU 2792 CZ3 TRP A 427 2752 2965 1732 -540 -836 -762 C ATOM 2793 CH2 TRP A 427 -55.424 -22.098 -4.215 1.00 20.29 C ANISOU 2793 CH2 TRP A 427 2864 3035 1809 -603 -851 -781 C ATOM 2794 N LEU A 428 -54.234 -14.627 -1.330 1.00 16.10 N ANISOU 2794 N LEU A 428 2144 2610 1365 -453 -828 -227 N ATOM 2795 CA LEU A 428 -53.101 -13.762 -1.015 1.00 15.83 C ANISOU 2795 CA LEU A 428 2113 2580 1323 -432 -810 -216 C ATOM 2796 C LEU A 428 -52.387 -14.218 0.252 1.00 28.29 C ANISOU 2796 C LEU A 428 3735 4068 2945 -385 -823 -261 C ATOM 2797 O LEU A 428 -51.150 -14.222 0.300 1.00 32.77 O ANISOU 2797 O LEU A 428 4287 4660 3505 -368 -817 -314 O ATOM 2798 CB LEU A 428 -53.559 -12.309 -0.890 1.00 15.62 C ANISOU 2798 CB LEU A 428 2092 2557 1286 -449 -806 -88 C ATOM 2799 CG LEU A 428 -53.574 -11.518 -2.202 1.00 16.17 C ANISOU 2799 CG LEU A 428 2121 2726 1297 -493 -790 -43 C ATOM 2800 CD1 LEU A 428 -54.174 -10.134 -2.005 1.00 16.09 C ANISOU 2800 CD1 LEU A 428 2129 2704 1280 -503 -795 94 C ATOM 2801 CD2 LEU A 428 -52.174 -11.424 -2.790 1.00 16.48 C ANISOU 2801 CD2 LEU A 428 2141 2824 1298 -507 -762 -110 C ATOM 2802 N CYS A 429 -53.140 -14.616 1.283 1.00 25.40 N ANISOU 2802 N CYS A 429 3425 3597 2631 -363 -841 -236 N ATOM 2803 CA CYS A 429 -52.505 -15.207 2.462 1.00 25.29 C ANISOU 2803 CA CYS A 429 3462 3479 2670 -304 -846 -279 C ATOM 2804 C CYS A 429 -51.782 -16.505 2.104 1.00 29.02 C ANISOU 2804 C CYS A 429 3921 3960 3144 -278 -855 -399 C ATOM 2805 O CYS A 429 -50.611 -16.721 2.476 1.00 35.26 O ANISOU 2805 O CYS A 429 4706 4743 3950 -233 -861 -447 O ATOM 2806 CB CYS A 429 -53.552 -15.461 3.547 1.00 20.29 C ANISOU 2806 CB CYS A 429 2891 2725 2091 -283 -841 -229 C ATOM 2807 SG CYS A 429 -54.510 -14.012 4.054 1.00 20.41 S ANISOU 2807 SG CYS A 429 2930 2709 2117 -290 -809 -92 S ATOM 2808 N TYR A 430 -52.473 -17.392 1.381 1.00 31.32 N ANISOU 2808 N TYR A 430 4211 4268 3422 -307 -857 -447 N ATOM 2809 CA TYR A 430 -51.826 -18.625 0.944 1.00 20.56 C ANISOU 2809 CA TYR A 430 2852 2903 2056 -280 -853 -568 C ATOM 2810 C TYR A 430 -50.570 -18.326 0.127 1.00 18.79 C ANISOU 2810 C TYR A 430 2563 2789 1786 -273 -832 -623 C ATOM 2811 O TYR A 430 -49.531 -18.982 0.296 1.00 17.25 O ANISOU 2811 O TYR A 430 2360 2576 1617 -208 -822 -700 O ATOM 2812 CB TYR A 430 -52.822 -19.471 0.151 1.00 25.88 C ANISOU 2812 CB TYR A 430 3544 3588 2703 -339 -857 -609 C ATOM 2813 CG TYR A 430 -54.006 -19.943 0.973 1.00 25.34 C ANISOU 2813 CG TYR A 430 3530 3413 2684 -352 -873 -564 C ATOM 2814 CD1 TYR A 430 -53.909 -20.071 2.355 1.00 17.37 C ANISOU 2814 CD1 TYR A 430 2576 2282 1743 -291 -875 -533 C ATOM 2815 CD2 TYR A 430 -55.219 -20.264 0.369 1.00 28.32 C ANISOU 2815 CD2 TYR A 430 3901 3822 3039 -432 -883 -548 C ATOM 2816 CE1 TYR A 430 -54.982 -20.506 3.114 1.00 16.05 C ANISOU 2816 CE1 TYR A 430 2460 2021 1617 -308 -879 -491 C ATOM 2817 CE2 TYR A 430 -56.301 -20.699 1.120 1.00 16.92 C ANISOU 2817 CE2 TYR A 430 2495 2290 1641 -453 -895 -505 C ATOM 2818 CZ TYR A 430 -56.175 -20.818 2.493 1.00 34.75 C ANISOU 2818 CZ TYR A 430 4811 4425 3968 -389 -885 -478 C ATOM 2819 OH TYR A 430 -57.242 -21.248 3.249 1.00 16.44 O ANISOU 2819 OH TYR A 430 2531 2023 1692 -415 -882 -433 O ATOM 2820 N ILE A 431 -50.634 -17.307 -0.733 1.00 22.24 N ANISOU 2820 N ILE A 431 2952 3341 2158 -337 -822 -576 N ATOM 2821 CA ILE A 431 -49.472 -16.904 -1.518 1.00 17.31 C ANISOU 2821 CA ILE A 431 2267 2819 1491 -342 -787 -608 C ATOM 2822 C ILE A 431 -48.341 -16.437 -0.610 1.00 17.08 C ANISOU 2822 C ILE A 431 2210 2783 1498 -293 -796 -600 C ATOM 2823 O ILE A 431 -47.164 -16.667 -0.913 1.00 25.32 O ANISOU 2823 O ILE A 431 3196 3888 2536 -263 -773 -667 O ATOM 2824 CB ILE A 431 -49.877 -15.832 -2.553 1.00 17.40 C ANISOU 2824 CB ILE A 431 2253 2909 1449 -407 -765 -526 C ATOM 2825 CG1 ILE A 431 -50.344 -16.499 -3.850 1.00 18.18 C ANISOU 2825 CG1 ILE A 431 2354 3060 1494 -451 -745 -576 C ATOM 2826 CG2 ILE A 431 -48.733 -14.871 -2.836 1.00 17.58 C ANISOU 2826 CG2 ILE A 431 2224 3015 1442 -422 -736 -507 C ATOM 2827 CD1 ILE A 431 -50.977 -15.541 -4.846 1.00 18.37 C ANISOU 2827 CD1 ILE A 431 2358 3154 1468 -511 -735 -488 C ATOM 2828 N ASN A 432 -48.663 -15.791 0.516 1.00 16.35 N ANISOU 2828 N ASN A 432 2159 2606 1447 -284 -823 -512 N ATOM 2829 CA ASN A 432 -47.634 -15.516 1.519 1.00 16.26 C ANISOU 2829 CA ASN A 432 2141 2561 1475 -242 -841 -500 C ATOM 2830 C ASN A 432 -46.915 -16.797 1.909 1.00 18.97 C ANISOU 2830 C ASN A 432 2475 2859 1873 -155 -850 -589 C ATOM 2831 O ASN A 432 -45.671 -16.860 1.917 1.00 22.03 O ANISOU 2831 O ASN A 432 2795 3304 2273 -120 -849 -626 O ATOM 2832 CB ASN A 432 -48.248 -14.864 2.760 1.00 15.52 C ANISOU 2832 CB ASN A 432 2125 2358 1413 -244 -865 -407 C ATOM 2833 CG ASN A 432 -47.277 -14.804 3.930 1.00 19.97 C ANISOU 2833 CG ASN A 432 2703 2871 2014 -206 -898 -401 C ATOM 2834 OD1 ASN A 432 -46.097 -14.498 3.759 1.00 24.58 O ANISOU 2834 OD1 ASN A 432 3218 3537 2585 -213 -904 -420 O ATOM 2835 ND2 ASN A 432 -47.769 -15.108 5.125 1.00 15.84 N ANISOU 2835 ND2 ASN A 432 2265 2221 1532 -173 -921 -371 N ATOM 2836 N SER A 433 -47.694 -17.840 2.225 1.00 38.59 N ANISOU 2836 N SER A 433 5026 5241 4394 -119 -859 -619 N ATOM 2837 CA SER A 433 -47.073 -19.133 2.512 1.00 17.35 C ANISOU 2837 CA SER A 433 2344 2492 1757 -30 -865 -702 C ATOM 2838 C SER A 433 -46.239 -19.636 1.338 1.00 18.34 C ANISOU 2838 C SER A 433 2394 2718 1855 -7 -819 -804 C ATOM 2839 O SER A 433 -45.286 -20.397 1.539 1.00 19.10 O ANISOU 2839 O SER A 433 2460 2798 1998 84 -816 -865 O ATOM 2840 CB SER A 433 -48.133 -20.166 2.889 1.00 17.26 C ANISOU 2840 CB SER A 433 2429 2352 1776 -16 -875 -719 C ATOM 2841 OG SER A 433 -48.780 -19.809 4.098 1.00 42.43 O ANISOU 2841 OG SER A 433 5686 5442 4994 -23 -906 -632 O ATOM 2842 N THR A 434 -46.564 -19.218 0.110 1.00 41.83 N ANISOU 2842 N THR A 434 5339 5799 4754 -84 -782 -819 N ATOM 2843 CA THR A 434 -45.744 -19.621 -1.034 1.00 31.53 C ANISOU 2843 CA THR A 434 3970 4598 3410 -70 -724 -918 C ATOM 2844 C THR A 434 -44.422 -18.858 -1.081 1.00 33.69 C ANISOU 2844 C THR A 434 4135 4986 3682 -59 -707 -905 C ATOM 2845 O THR A 434 -43.386 -19.424 -1.450 1.00 33.05 O ANISOU 2845 O THR A 434 3984 4956 3617 8 -665 -986 O ATOM 2846 CB THR A 434 -46.510 -19.414 -2.343 1.00 30.56 C ANISOU 2846 CB THR A 434 3860 4560 3191 -170 -694 -936 C ATOM 2847 OG1 THR A 434 -47.739 -20.145 -2.304 1.00 35.31 O ANISOU 2847 OG1 THR A 434 4552 5069 3796 -194 -716 -946 O ATOM 2848 CG2 THR A 434 -45.683 -19.895 -3.532 1.00 30.15 C ANISOU 2848 CG2 THR A 434 3759 4610 3085 -161 -621 -1050 C ATOM 2849 N ILE A 435 -44.430 -17.576 -0.709 1.00 28.98 N ANISOU 2849 N ILE A 435 3520 4426 3066 -124 -736 -803 N ATOM 2850 CA ILE A 435 -43.295 -16.699 -0.985 1.00 24.42 C ANISOU 2850 CA ILE A 435 2840 3976 2462 -155 -716 -785 C ATOM 2851 C ILE A 435 -42.311 -16.579 0.171 1.00 27.15 C ANISOU 2851 C ILE A 435 3139 4298 2878 -100 -761 -754 C ATOM 2852 O ILE A 435 -41.214 -16.033 -0.034 1.00 20.38 O ANISOU 2852 O ILE A 435 2178 3556 2009 -122 -745 -750 O ATOM 2853 CB ILE A 435 -43.760 -15.285 -1.394 1.00 26.41 C ANISOU 2853 CB ILE A 435 3105 4291 2639 -275 -717 -693 C ATOM 2854 CG1 ILE A 435 -44.421 -14.576 -0.207 1.00 28.63 C ANISOU 2854 CG1 ILE A 435 3465 4461 2953 -292 -774 -588 C ATOM 2855 CG2 ILE A 435 -44.695 -15.356 -2.594 1.00 20.18 C ANISOU 2855 CG2 ILE A 435 2350 3545 1772 -335 -685 -711 C ATOM 2856 CD1 ILE A 435 -44.761 -13.130 -0.469 1.00 19.58 C ANISOU 2856 CD1 ILE A 435 2343 3344 1754 -387 -767 -486 C ATOM 2857 N ASN A 436 -42.663 -17.037 1.376 1.00 19.25 N ANISOU 2857 N ASN A 436 2211 3161 1942 -43 -819 -726 N ATOM 2858 CA ASN A 436 -41.703 -16.994 2.483 1.00 19.54 C ANISOU 2858 CA ASN A 436 2206 3180 2037 6 -874 -694 C ATOM 2859 C ASN A 436 -40.323 -17.566 2.148 1.00 20.87 C ANISOU 2859 C ASN A 436 2238 3447 2244 85 -851 -761 C ATOM 2860 O ASN A 436 -39.314 -16.901 2.452 1.00 22.96 O ANISOU 2860 O ASN A 436 2407 3802 2513 59 -876 -722 O ATOM 2861 CB ASN A 436 -42.300 -17.708 3.703 1.00 20.58 C ANISOU 2861 CB ASN A 436 2447 3146 2228 71 -932 -671 C ATOM 2862 CG ASN A 436 -42.963 -16.751 4.664 1.00 28.04 C ANISOU 2862 CG ASN A 436 3484 4016 3152 -1 -976 -572 C ATOM 2863 OD1 ASN A 436 -42.583 -15.583 4.751 1.00 34.21 O ANISOU 2863 OD1 ASN A 436 4241 4862 3895 -80 -985 -515 O ATOM 2864 ND2 ASN A 436 -43.958 -17.240 5.397 1.00 34.79 N ANISOU 2864 ND2 ASN A 436 4455 4732 4030 22 -996 -551 N ATOM 2865 N PRO A 437 -40.194 -18.761 1.547 1.00 21.67 N ANISOU 2865 N PRO A 437 2322 3538 2375 180 -802 -859 N ATOM 2866 CA PRO A 437 -38.841 -19.284 1.278 1.00 23.41 C ANISOU 2866 CA PRO A 437 2401 3851 2643 275 -770 -918 C ATOM 2867 C PRO A 437 -37.999 -18.359 0.421 1.00 23.74 C ANISOU 2867 C PRO A 437 2308 4080 2630 196 -716 -917 C ATOM 2868 O PRO A 437 -36.795 -18.221 0.666 1.00 24.71 O ANISOU 2868 O PRO A 437 2294 4300 2795 231 -725 -906 O ATOM 2869 CB PRO A 437 -39.117 -20.620 0.571 1.00 23.85 C ANISOU 2869 CB PRO A 437 2499 3847 2716 370 -702 -1032 C ATOM 2870 CG PRO A 437 -40.476 -21.010 1.016 1.00 22.78 C ANISOU 2870 CG PRO A 437 2529 3551 2576 349 -740 -1014 C ATOM 2871 CD PRO A 437 -41.231 -19.722 1.126 1.00 29.98 C ANISOU 2871 CD PRO A 437 3481 4488 3421 209 -771 -922 C ATOM 2872 N ALA A 438 -38.601 -17.716 -0.581 1.00 23.29 N ANISOU 2872 N ALA A 438 2286 4085 2480 86 -662 -922 N ATOM 2873 CA ALA A 438 -37.866 -16.725 -1.356 1.00 23.84 C ANISOU 2873 CA ALA A 438 2247 4326 2485 -10 -613 -907 C ATOM 2874 C ALA A 438 -37.452 -15.547 -0.488 1.00 46.87 C ANISOU 2874 C ALA A 438 5136 7270 5404 -95 -686 -798 C ATOM 2875 O ALA A 438 -36.432 -14.903 -0.761 1.00 41.11 O ANISOU 2875 O ALA A 438 4281 6683 4657 -150 -664 -782 O ATOM 2876 CB ALA A 438 -38.707 -16.246 -2.540 1.00 23.45 C ANISOU 2876 CB ALA A 438 2263 4320 2327 -117 -556 -917 C ATOM 2877 N CYS A 439 -38.216 -15.259 0.567 1.00 38.58 N ANISOU 2877 N CYS A 439 4204 6086 4370 -114 -767 -725 N ATOM 2878 CA CYS A 439 -37.858 -14.158 1.451 1.00 30.98 C ANISOU 2878 CA CYS A 439 3242 5131 3400 -200 -835 -629 C ATOM 2879 C CYS A 439 -36.613 -14.487 2.265 1.00 26.11 C ANISOU 2879 C CYS A 439 2506 4558 2855 -138 -891 -623 C ATOM 2880 O CYS A 439 -35.691 -13.667 2.352 1.00 36.35 O ANISOU 2880 O CYS A 439 3707 5970 4135 -220 -908 -581 O ATOM 2881 CB CYS A 439 -39.029 -13.806 2.369 1.00 28.19 C ANISOU 2881 CB CYS A 439 3055 4615 3040 -229 -893 -560 C ATOM 2882 SG CYS A 439 -40.303 -12.801 1.582 1.00 34.58 S ANISOU 2882 SG CYS A 439 3974 5405 3759 -341 -849 -513 S ATOM 2883 N TYR A 440 -36.550 -15.680 2.864 1.00 24.35 N ANISOU 2883 N TYR A 440 2288 4251 2714 2 -924 -658 N ATOM 2884 CA TYR A 440 -35.407 -15.953 3.735 1.00 26.22 C ANISOU 2884 CA TYR A 440 2413 4528 3021 64 -996 -632 C ATOM 2885 C TYR A 440 -34.381 -16.930 3.170 1.00 37.18 C ANISOU 2885 C TYR A 440 3635 6015 4479 197 -945 -708 C ATOM 2886 O TYR A 440 -33.194 -16.792 3.476 1.00 27.13 O ANISOU 2886 O TYR A 440 2204 4857 3247 212 -980 -681 O ATOM 2887 CB TYR A 440 -35.875 -16.456 5.111 1.00 23.76 C ANISOU 2887 CB TYR A 440 2222 4050 2755 125 -1096 -587 C ATOM 2888 CG TYR A 440 -36.784 -17.663 5.095 1.00 35.36 C ANISOU 2888 CG TYR A 440 3802 5371 4261 239 -1073 -643 C ATOM 2889 CD1 TYR A 440 -38.163 -17.519 5.186 1.00 32.90 C ANISOU 2889 CD1 TYR A 440 3660 4934 3908 188 -1063 -630 C ATOM 2890 CD2 TYR A 440 -36.264 -18.948 5.012 1.00 27.59 C ANISOU 2890 CD2 TYR A 440 2754 4370 3358 398 -1060 -705 C ATOM 2891 CE1 TYR A 440 -38.995 -18.617 5.176 1.00 38.07 C ANISOU 2891 CE1 TYR A 440 4414 5459 4594 273 -1045 -678 C ATOM 2892 CE2 TYR A 440 -37.089 -20.051 5.001 1.00 30.45 C ANISOU 2892 CE2 TYR A 440 3234 4585 3750 488 -1039 -757 C ATOM 2893 CZ TYR A 440 -38.454 -19.880 5.084 1.00 44.64 C ANISOU 2893 CZ TYR A 440 5196 6268 5498 416 -1034 -743 C ATOM 2894 OH TYR A 440 -39.288 -20.974 5.075 1.00 60.54 O ANISOU 2894 OH TYR A 440 7325 8140 7538 487 -1015 -792 O ATOM 2895 N ALA A 441 -34.785 -17.894 2.345 1.00 38.24 N ANISOU 2895 N ALA A 441 3795 6109 4624 292 -859 -802 N ATOM 2896 CA ALA A 441 -33.891 -18.973 1.935 1.00 36.55 C ANISOU 2896 CA ALA A 441 3451 5950 4488 449 -803 -881 C ATOM 2897 C ALA A 441 -33.195 -18.721 0.604 1.00 39.88 C ANISOU 2897 C ALA A 441 3731 6551 4870 420 -679 -947 C ATOM 2898 O ALA A 441 -32.020 -19.067 0.454 1.00 30.49 O ANISOU 2898 O ALA A 441 2362 5478 3744 509 -646 -972 O ATOM 2899 CB ALA A 441 -34.659 -20.297 1.863 1.00 42.05 C ANISOU 2899 CB ALA A 441 4273 6480 5222 577 -775 -957 C ATOM 2900 N LEU A 442 -33.887 -18.136 -0.373 1.00 44.42 N ANISOU 2900 N LEU A 442 4378 7158 5342 301 -609 -971 N ATOM 2901 CA LEU A 442 -33.293 -17.987 -1.697 1.00 46.78 C ANISOU 2901 CA LEU A 442 4564 7621 5588 272 -481 -1041 C ATOM 2902 C LEU A 442 -32.240 -16.887 -1.749 1.00 51.50 C ANISOU 2902 C LEU A 442 4998 8403 6165 164 -483 -978 C ATOM 2903 O LEU A 442 -31.382 -16.912 -2.638 1.00 51.41 O ANISOU 2903 O LEU A 442 4841 8551 6142 171 -378 -1031 O ATOM 2904 CB LEU A 442 -34.382 -17.722 -2.740 1.00 43.32 C ANISOU 2904 CB LEU A 442 4263 7162 5035 170 -416 -1079 C ATOM 2905 CG LEU A 442 -35.233 -18.937 -3.120 1.00 35.07 C ANISOU 2905 CG LEU A 442 3347 5982 3994 265 -375 -1174 C ATOM 2906 CD1 LEU A 442 -36.274 -18.579 -4.174 1.00 29.61 C ANISOU 2906 CD1 LEU A 442 2774 5297 3179 143 -326 -1198 C ATOM 2907 CD2 LEU A 442 -34.354 -20.083 -3.601 1.00 32.70 C ANISOU 2907 CD2 LEU A 442 2950 5719 3756 423 -278 -1288 C ATOM 2908 N CYS A 443 -32.275 -15.933 -0.823 1.00 60.01 N ANISOU 2908 N CYS A 443 6102 9466 7235 58 -592 -869 N ATOM 2909 CA CYS A 443 -31.280 -14.869 -0.779 1.00 67.06 C ANISOU 2909 CA CYS A 443 6851 10524 8105 -65 -606 -804 C ATOM 2910 C CYS A 443 -30.086 -15.210 0.105 1.00 57.47 C ANISOU 2910 C CYS A 443 5461 9378 6996 19 -677 -771 C ATOM 2911 O CYS A 443 -29.214 -14.357 0.298 1.00 60.48 O ANISOU 2911 O CYS A 443 5715 9898 7367 -91 -709 -708 O ATOM 2912 CB CYS A 443 -31.923 -13.563 -0.294 1.00 76.14 C ANISOU 2912 CB CYS A 443 8134 11619 9177 -243 -682 -704 C ATOM 2913 SG CYS A 443 -32.359 -13.528 1.464 1.00 77.35 S ANISOU 2913 SG CYS A 443 8410 11597 9383 -226 -845 -618 S ATOM 2914 N ASN A 444 -30.021 -16.428 0.636 1.00 56.09 N ANISOU 2914 N ASN A 444 5279 9112 6923 206 -706 -805 N ATOM 2915 CA ASN A 444 -28.970 -16.832 1.559 1.00 46.79 C ANISOU 2915 CA ASN A 444 3944 7984 5852 305 -793 -760 C ATOM 2916 C ASN A 444 -27.980 -17.754 0.860 1.00 41.47 C ANISOU 2916 C ASN A 444 3069 7428 5261 470 -687 -839 C ATOM 2917 O ASN A 444 -28.374 -18.662 0.124 1.00 35.24 O ANISOU 2917 O ASN A 444 2337 6572 4481 589 -581 -941 O ATOM 2918 CB ASN A 444 -29.563 -17.530 2.785 1.00 32.22 C ANISOU 2918 CB ASN A 444 2237 5940 4064 405 -913 -724 C ATOM 2919 CG ASN A 444 -28.505 -17.946 3.787 1.00 37.49 C ANISOU 2919 CG ASN A 444 2752 6657 4837 506 -1022 -663 C ATOM 2920 OD1 ASN A 444 -27.960 -19.047 3.711 1.00 40.10 O ANISOU 2920 OD1 ASN A 444 2978 6990 5267 698 -992 -706 O ATOM 2921 ND2 ASN A 444 -28.206 -17.063 4.733 1.00 42.94 N ANISOU 2921 ND2 ASN A 444 3432 7383 5501 375 -1150 -559 N ATOM 2922 N ALA A 445 -26.689 -17.519 1.106 1.00 45.10 N ANISOU 2922 N ALA A 445 3293 8064 5779 475 -714 -792 N ATOM 2923 CA ALA A 445 -25.649 -18.285 0.423 1.00 50.43 C ANISOU 2923 CA ALA A 445 3747 8877 6539 632 -600 -860 C ATOM 2924 C ALA A 445 -25.610 -19.731 0.905 1.00 59.42 C ANISOU 2924 C ALA A 445 4893 9882 7802 887 -619 -896 C ATOM 2925 O ALA A 445 -25.450 -20.654 0.097 1.00 74.55 O ANISOU 2925 O ALA A 445 6772 11793 9760 1045 -481 -1002 O ATOM 2926 CB ALA A 445 -24.289 -17.618 0.623 1.00 51.80 C ANISOU 2926 CB ALA A 445 3647 9285 6749 562 -634 -785 C ATOM 2927 N THR A 446 -25.750 -19.947 2.215 1.00 50.93 N ANISOU 2927 N THR A 446 3879 8691 6781 929 -784 -810 N ATOM 2928 CA THR A 446 -25.716 -21.304 2.752 1.00 46.54 C ANISOU 2928 CA THR A 446 3345 7995 6342 1169 -816 -829 C ATOM 2929 C THR A 446 -26.924 -22.110 2.287 1.00 52.85 C ANISOU 2929 C THR A 446 4388 8582 7109 1237 -736 -930 C ATOM 2930 O THR A 446 -26.789 -23.268 1.868 1.00 65.04 O ANISOU 2930 O THR A 446 5925 10059 8726 1433 -645 -1016 O ATOM 2931 CB THR A 446 -25.656 -21.263 4.278 1.00 42.71 C ANISOU 2931 CB THR A 446 2893 7435 5899 1169 -1020 -704 C ATOM 2932 OG1 THR A 446 -24.724 -20.258 4.693 1.00 51.03 O ANISOU 2932 OG1 THR A 446 3759 8686 6944 1033 -1108 -606 O ATOM 2933 CG2 THR A 446 -25.216 -22.611 4.827 1.00 42.25 C ANISOU 2933 CG2 THR A 446 2782 7289 5982 1429 -1059 -700 C ATOM 2934 N PHE A 447 -28.119 -21.515 2.359 1.00 42.21 N ANISOU 2934 N PHE A 447 3260 7125 5654 1076 -768 -920 N ATOM 2935 CA PHE A 447 -29.310 -22.188 1.855 1.00 35.58 C ANISOU 2935 CA PHE A 447 2642 6106 4773 1110 -695 -1010 C ATOM 2936 C PHE A 447 -29.174 -22.509 0.373 1.00 42.67 C ANISOU 2936 C PHE A 447 3495 7082 5637 1143 -509 -1139 C ATOM 2937 O PHE A 447 -29.644 -23.555 -0.087 1.00 44.47 O ANISOU 2937 O PHE A 447 3833 7182 5880 1261 -429 -1238 O ATOM 2938 CB PHE A 447 -30.552 -21.331 2.096 1.00 37.02 C ANISOU 2938 CB PHE A 447 3026 6196 4842 918 -754 -966 C ATOM 2939 CG PHE A 447 -31.206 -21.562 3.428 1.00 36.04 C ANISOU 2939 CG PHE A 447 3056 5894 4745 933 -895 -890 C ATOM 2940 CD1 PHE A 447 -31.855 -22.756 3.697 1.00 36.16 C ANISOU 2940 CD1 PHE A 447 3215 5716 4807 1067 -897 -933 C ATOM 2941 CD2 PHE A 447 -31.194 -20.577 4.402 1.00 31.34 C ANISOU 2941 CD2 PHE A 447 2474 5317 4115 802 -1021 -777 C ATOM 2942 CE1 PHE A 447 -32.465 -22.969 4.921 1.00 39.79 C ANISOU 2942 CE1 PHE A 447 3822 6015 5284 1071 -1020 -860 C ATOM 2943 CE2 PHE A 447 -31.802 -20.784 5.627 1.00 30.46 C ANISOU 2943 CE2 PHE A 447 2514 5043 4015 809 -1141 -709 C ATOM 2944 CZ PHE A 447 -32.438 -21.982 5.887 1.00 31.24 C ANISOU 2944 CZ PHE A 447 2748 4960 4164 944 -1140 -748 C ATOM 2945 N LYS A 448 -28.537 -21.621 -0.394 1.00 39.06 N ANISOU 2945 N LYS A 448 2885 6831 5123 1031 -435 -1142 N ATOM 2946 CA LYS A 448 -28.354 -21.880 -1.818 1.00 42.97 C ANISOU 2946 CA LYS A 448 3339 7416 5572 1051 -251 -1264 C ATOM 2947 C LYS A 448 -27.375 -23.024 -2.052 1.00 43.77 C ANISOU 2947 C LYS A 448 3289 7546 5794 1287 -156 -1338 C ATOM 2948 O LYS A 448 -27.584 -23.855 -2.945 1.00 50.53 O ANISOU 2948 O LYS A 448 4215 8347 6638 1382 -16 -1465 O ATOM 2949 CB LYS A 448 -27.889 -20.609 -2.531 1.00 45.24 C ANISOU 2949 CB LYS A 448 3504 7919 5766 863 -196 -1237 C ATOM 2950 CG LYS A 448 -29.027 -19.663 -2.896 1.00 48.01 C ANISOU 2950 CG LYS A 448 4041 8228 5973 651 -214 -1214 C ATOM 2951 CD LYS A 448 -28.546 -18.464 -3.706 1.00 48.65 C ANISOU 2951 CD LYS A 448 4016 8513 5956 470 -146 -1191 C ATOM 2952 CE LYS A 448 -27.819 -17.451 -2.837 1.00 57.83 C ANISOU 2952 CE LYS A 448 5047 9782 7144 363 -260 -1064 C ATOM 2953 NZ LYS A 448 -27.473 -16.212 -3.592 1.00 59.33 N ANISOU 2953 NZ LYS A 448 5167 10147 7227 161 -202 -1033 N ATOM 2954 N LYS A 449 -26.304 -23.089 -1.259 1.00 42.34 N ANISOU 2954 N LYS A 449 2905 7451 5730 1386 -231 -1259 N ATOM 2955 CA LYS A 449 -25.369 -24.204 -1.376 1.00 53.61 C ANISOU 2955 CA LYS A 449 4180 8896 7291 1638 -150 -1314 C ATOM 2956 C LYS A 449 -26.055 -25.527 -1.052 1.00 54.60 C ANISOU 2956 C LYS A 449 4504 8765 7478 1817 -158 -1372 C ATOM 2957 O LYS A 449 -25.899 -26.516 -1.780 1.00 58.79 O ANISOU 2957 O LYS A 449 5050 9242 8047 1981 -11 -1493 O ATOM 2958 CB LYS A 449 -24.163 -23.977 -0.463 1.00 59.36 C ANISOU 2958 CB LYS A 449 4651 9766 8136 1700 -261 -1194 C ATOM 2959 CG LYS A 449 -23.289 -22.802 -0.876 1.00 57.54 C ANISOU 2959 CG LYS A 449 4191 9809 7862 1538 -230 -1147 C ATOM 2960 CD LYS A 449 -22.175 -22.563 0.123 1.00 60.77 C ANISOU 2960 CD LYS A 449 4389 10326 8375 1558 -364 -1005 C ATOM 2961 CE LYS A 449 -21.361 -21.332 -0.244 1.00 69.66 C ANISOU 2961 CE LYS A 449 5354 11672 9442 1344 -338 -936 C ATOM 2962 NZ LYS A 449 -20.334 -21.019 0.789 1.00 78.07 N ANISOU 2962 NZ LYS A 449 6279 12792 10593 1310 -481 -776 N ATOM 2963 N THR A 450 -26.831 -25.561 0.037 1.00 53.63 N ANISOU 2963 N THR A 450 4547 8474 7358 1783 -322 -1291 N ATOM 2964 CA THR A 450 -27.533 -26.791 0.394 1.00 42.49 C ANISOU 2964 CA THR A 450 3337 6810 5997 1932 -336 -1337 C ATOM 2965 C THR A 450 -28.585 -27.152 -0.644 1.00 48.77 C ANISOU 2965 C THR A 450 4347 7492 6689 1875 -209 -1471 C ATOM 2966 O THR A 450 -28.811 -28.339 -0.909 1.00 46.37 O ANISOU 2966 O THR A 450 4158 7030 6429 2029 -133 -1566 O ATOM 2967 CB THR A 450 -28.180 -26.660 1.773 1.00 47.90 C ANISOU 2967 CB THR A 450 4158 7351 6689 1879 -533 -1217 C ATOM 2968 OG1 THR A 450 -27.249 -26.070 2.687 1.00 51.92 O ANISOU 2968 OG1 THR A 450 4474 7995 7257 1872 -664 -1086 O ATOM 2969 CG2 THR A 450 -28.587 -28.025 2.301 1.00 41.40 C ANISOU 2969 CG2 THR A 450 3495 6285 5949 2066 -558 -1242 C ATOM 2970 N PHE A 451 -29.230 -26.149 -1.245 1.00 42.90 N ANISOU 2970 N PHE A 451 3667 6827 5808 1652 -188 -1477 N ATOM 2971 CA PHE A 451 -30.193 -26.416 -2.310 1.00 41.72 C ANISOU 2971 CA PHE A 451 3703 6602 5549 1580 -75 -1597 C ATOM 2972 C PHE A 451 -29.512 -27.059 -3.512 1.00 60.56 C ANISOU 2972 C PHE A 451 6010 9062 7940 1696 122 -1737 C ATOM 2973 O PHE A 451 -29.971 -28.088 -4.025 1.00 67.57 O ANISOU 2973 O PHE A 451 7052 9802 8819 1784 212 -1855 O ATOM 2974 CB PHE A 451 -30.900 -25.126 -2.726 1.00 40.58 C ANISOU 2974 CB PHE A 451 3610 6549 5258 1326 -97 -1557 C ATOM 2975 CG PHE A 451 -31.939 -24.653 -1.748 1.00 46.48 C ANISOU 2975 CG PHE A 451 4509 7173 5977 1211 -254 -1454 C ATOM 2976 CD1 PHE A 451 -32.369 -25.472 -0.716 1.00 49.95 C ANISOU 2976 CD1 PHE A 451 5066 7417 6496 1315 -351 -1422 C ATOM 2977 CD2 PHE A 451 -32.493 -23.389 -1.868 1.00 45.50 C ANISOU 2977 CD2 PHE A 451 4416 7125 5746 1001 -297 -1387 C ATOM 2978 CE1 PHE A 451 -33.331 -25.033 0.182 1.00 46.73 C ANISOU 2978 CE1 PHE A 451 4798 6901 6058 1207 -480 -1331 C ATOM 2979 CE2 PHE A 451 -33.453 -22.947 -0.975 1.00 45.23 C ANISOU 2979 CE2 PHE A 451 4521 6975 5689 905 -425 -1296 C ATOM 2980 CZ PHE A 451 -33.872 -23.769 0.051 1.00 44.53 C ANISOU 2980 CZ PHE A 451 4541 6702 5676 1007 -512 -1271 C ATOM 2981 N LYS A 452 -28.406 -26.466 -3.972 1.00 63.86 N ANISOU 2981 N LYS A 452 6192 9706 8366 1691 197 -1730 N ATOM 2982 CA LYS A 452 -27.681 -27.039 -5.103 1.00 61.66 C ANISOU 2982 CA LYS A 452 5823 9513 8093 1807 401 -1863 C ATOM 2983 C LYS A 452 -27.187 -28.443 -4.782 1.00 60.99 C ANISOU 2983 C LYS A 452 5730 9289 8156 2088 447 -1921 C ATOM 2984 O LYS A 452 -27.174 -29.318 -5.655 1.00 70.04 O ANISOU 2984 O LYS A 452 6953 10369 9291 2196 612 -2067 O ATOM 2985 CB LYS A 452 -26.512 -26.135 -5.497 1.00 63.35 C ANISOU 2985 CB LYS A 452 5759 10005 8306 1754 463 -1825 C ATOM 2986 CG LYS A 452 -25.741 -26.624 -6.718 1.00 69.89 C ANISOU 2986 CG LYS A 452 6482 10945 9127 1859 695 -1963 C ATOM 2987 CD LYS A 452 -24.501 -25.784 -6.980 1.00 69.92 C ANISOU 2987 CD LYS A 452 6184 11232 9151 1818 753 -1912 C ATOM 2988 CE LYS A 452 -23.707 -26.328 -8.160 1.00 70.04 C ANISOU 2988 CE LYS A 452 6098 11349 9165 1933 996 -2046 C ATOM 2989 NZ LYS A 452 -22.433 -25.584 -8.376 1.00 71.40 N ANISOU 2989 NZ LYS A 452 6006 11757 9368 1872 1044 -1957 N ATOM 2990 N HIS A 453 -26.784 -28.680 -3.532 1.00 59.53 N ANISOU 2990 N HIS A 453 5464 9048 8106 2209 302 -1808 N ATOM 2991 CA HIS A 453 -26.344 -30.016 -3.143 1.00 56.61 C ANISOU 2991 CA HIS A 453 5097 8527 7884 2486 330 -1844 C ATOM 2992 C HIS A 453 -27.498 -31.013 -3.175 1.00 56.22 C ANISOU 2992 C HIS A 453 5361 8196 7803 2518 338 -1929 C ATOM 2993 O HIS A 453 -27.325 -32.157 -3.610 1.00 50.45 O ANISOU 2993 O HIS A 453 4701 7340 7128 2706 464 -2045 O ATOM 2994 CB HIS A 453 -25.706 -29.969 -1.755 1.00 49.59 C ANISOU 2994 CB HIS A 453 4060 7649 7132 2586 149 -1684 C ATOM 2995 CG HIS A 453 -25.421 -31.318 -1.173 1.00 55.38 C ANISOU 2995 CG HIS A 453 4850 8183 8009 2839 138 -1675 C ATOM 2996 ND1 HIS A 453 -26.236 -31.909 -0.232 1.00 53.87 N ANISOU 2996 ND1 HIS A 453 4866 7757 7845 2880 3 -1634 N ATOM 2997 CD2 HIS A 453 -24.409 -32.190 -1.396 1.00 60.10 C ANISOU 2997 CD2 HIS A 453 5358 8755 8722 3022 251 -1668 C ATOM 2998 CE1 HIS A 453 -25.741 -33.088 0.098 1.00 59.41 C ANISOU 2998 CE1 HIS A 453 5607 8300 8667 3071 31 -1601 C ATOM 2999 NE2 HIS A 453 -24.632 -33.283 -0.593 1.00 61.05 N ANISOU 2999 NE2 HIS A 453 5633 8629 8935 3169 181 -1621 N ATOM 3000 N LEU A 454 -28.686 -30.595 -2.730 1.00 55.66 N ANISOU 3000 N LEU A 454 5482 8023 7642 2333 210 -1876 N ATOM 3001 CA LEU A 454 -29.818 -31.514 -2.655 1.00 45.38 C ANISOU 3001 CA LEU A 454 4469 6460 6313 2343 200 -1941 C ATOM 3002 C LEU A 454 -30.408 -31.804 -4.030 1.00 60.61 C ANISOU 3002 C LEU A 454 6549 8364 8116 2265 366 -2107 C ATOM 3003 O LEU A 454 -30.834 -32.933 -4.299 1.00 57.49 O ANISOU 3003 O LEU A 454 6342 7771 7730 2359 437 -2214 O ATOM 3004 CB LEU A 454 -30.893 -30.949 -1.725 1.00 42.74 C ANISOU 3004 CB LEU A 454 4272 6039 5926 2171 17 -1826 C ATOM 3005 CG LEU A 454 -30.594 -30.986 -0.226 1.00 42.50 C ANISOU 3005 CG LEU A 454 4190 5948 6008 2253 -159 -1676 C ATOM 3006 CD1 LEU A 454 -31.689 -30.275 0.560 1.00 39.88 C ANISOU 3006 CD1 LEU A 454 3997 5556 5601 2056 -311 -1575 C ATOM 3007 CD2 LEU A 454 -30.435 -32.420 0.250 1.00 44.15 C ANISOU 3007 CD2 LEU A 454 4494 5941 6340 2489 -156 -1705 C ATOM 3008 N LEU A 455 -30.438 -30.806 -4.913 1.00 56.75 N ANISOU 3008 N LEU A 455 5990 8069 7502 2085 429 -2128 N ATOM 3009 CA LEU A 455 -31.064 -30.996 -6.216 1.00 59.24 C ANISOU 3009 CA LEU A 455 6460 8374 7675 1982 569 -2274 C ATOM 3010 C LEU A 455 -30.133 -31.680 -7.211 1.00 75.24 C ANISOU 3010 C LEU A 455 8413 10454 9722 2141 783 -2421 C ATOM 3011 O LEU A 455 -30.607 -32.374 -8.119 1.00 81.04 O ANISOU 3011 O LEU A 455 9328 11091 10372 2132 908 -2569 O ATOM 3012 CB LEU A 455 -31.535 -29.652 -6.772 1.00 47.27 C ANISOU 3012 CB LEU A 455 4919 7035 6006 1721 544 -2229 C ATOM 3013 CG LEU A 455 -32.508 -28.881 -5.875 1.00 41.48 C ANISOU 3013 CG LEU A 455 4263 6254 5242 1558 352 -2090 C ATOM 3014 CD1 LEU A 455 -32.878 -27.537 -6.487 1.00 39.35 C ANISOU 3014 CD1 LEU A 455 3961 6159 4831 1323 342 -2043 C ATOM 3015 CD2 LEU A 455 -33.750 -29.709 -5.590 1.00 44.74 C ANISOU 3015 CD2 LEU A 455 4935 6427 5638 1541 295 -2123 C ATOM 3016 N MET A 456 -28.824 -31.505 -7.063 1.00 81.13 N ANISOU 3016 N MET A 456 8896 11354 10575 2283 831 -2384 N ATOM 3017 CA MET A 456 -27.863 -32.137 -7.961 1.00 82.50 C ANISOU 3017 CA MET A 456 8992 11573 10780 2425 1040 -2484 C ATOM 3018 C MET A 456 -27.336 -33.442 -7.372 1.00 74.16 C ANISOU 3018 C MET A 456 7975 10309 9893 2667 1056 -2456 C ATOM 3019 O MET A 456 -28.070 -34.181 -6.715 1.00 65.85 O ANISOU 3019 O MET A 456 7119 9024 8878 2712 964 -2446 O ATOM 3020 CB MET A 456 -26.697 -31.189 -8.261 1.00 86.86 C ANISOU 3020 CB MET A 456 9242 12415 11347 2401 1099 -2427 C ATOM 3021 CG MET A 456 -27.093 -29.909 -8.987 1.00 91.04 C ANISOU 3021 CG MET A 456 9736 13154 11701 2150 1113 -2446 C ATOM 3022 SD MET A 456 -27.740 -30.203 -10.646 1.00100.87 S ANISOU 3022 SD MET A 456 11215 14367 12745 2013 1305 -2614 S ATOM 3023 CE MET A 456 -28.063 -28.527 -11.194 1.00 92.24 C ANISOU 3023 CE MET A 456 10047 13529 11473 1712 1267 -2556 C TER 3024 MET A 456 HETATM 3025 C4 82F A1201 -60.758 -12.798 12.588 1.00 10.00 C HETATM 3026 C5 82F A1201 -58.813 -13.642 11.741 1.00 11.76 C HETATM 3027 C6 82F A1201 -56.729 -14.838 12.173 1.00 37.39 C HETATM 3028 N1 82F A1201 -59.997 -13.870 12.321 1.00 8.68 N HETATM 3029 C7 82F A1201 -56.490 -15.835 13.115 1.00 34.15 C HETATM 3030 C8 82F A1201 -55.269 -15.881 13.765 1.00 25.47 C HETATM 3031 N2 82F A1201 -57.994 -14.776 11.503 1.00 16.69 N HETATM 3032 C9 82F A1201 -54.292 -14.948 13.485 1.00 28.05 C HETATM 3033 C10 82F A1201 -54.520 -13.951 12.552 1.00 30.53 C HETATM 3034 C11 82F A1201 -55.742 -13.882 11.885 1.00 29.67 C HETATM 3035 C12 82F A1201 -58.398 -15.793 10.590 1.00 10.05 C HETATM 3036 N3 82F A1201 -57.457 -16.700 10.313 1.00 1.00 N HETATM 3037 C13 82F A1201 -57.775 -17.792 9.406 1.00 1.75 C HETATM 3038 C14 82F A1201 -57.364 -17.472 7.984 1.00 6.47 C HETATM 3039 C15 82F A1201 -56.380 -18.752 6.171 1.00 11.00 C HETATM 3040 N4 82F A1201 -57.626 -18.352 6.839 1.00 9.18 N HETATM 3041 N 82F A1201 -57.100 -12.154 10.777 1.00 22.79 N HETATM 3042 C 82F A1201 -55.909 -12.768 10.907 1.00 19.08 C HETATM 3043 O 82F A1201 -54.957 -12.431 10.208 1.00 21.45 O HETATM 3044 C1 82F A1201 -58.352 -12.363 11.404 1.00 15.53 C HETATM 3045 C16 82F A1201 -55.764 -17.606 5.405 1.00 10.11 C HETATM 3046 C17 82F A1201 -56.739 -17.052 4.392 1.00 5.84 C HETATM 3047 C18 82F A1201 -58.050 -16.657 5.059 1.00 6.04 C HETATM 3048 C19 82F A1201 -58.610 -17.812 5.877 1.00 7.95 C HETATM 3049 C2 82F A1201 -59.165 -11.273 11.695 1.00 16.31 C HETATM 3050 C20 82F A1201 -59.248 -18.934 5.053 1.00 13.40 C HETATM 3051 C21 82F A1201 -61.341 -18.646 6.284 1.00 21.74 C HETATM 3052 C22 82F A1201 -61.719 -18.581 7.749 1.00 23.06 C HETATM 3053 C23 82F A1201 -62.906 -17.684 7.980 1.00 36.72 C HETATM 3054 C24 82F A1201 -60.632 -20.869 5.598 1.00 11.94 C HETATM 3055 C25 82F A1201 -60.659 -21.864 6.733 1.00 16.30 C HETATM 3056 C26 82F A1201 -61.109 -23.205 6.276 1.00 13.49 C HETATM 3057 C3 82F A1201 -60.389 -11.502 12.299 1.00 11.09 C HETATM 3058 N5 82F A1201 -60.200 -19.526 6.000 1.00 17.85 N HETATM 3059 O1 82F A1201 -59.526 -15.785 10.119 1.00 25.74 O CONECT 626 1272 CONECT 1272 626 CONECT 2679 2697 CONECT 2697 2679 CONECT 3025 3028 3057 CONECT 3026 3028 3031 3044 CONECT 3027 3029 3031 3034 CONECT 3028 3025 3026 CONECT 3029 3027 3030 CONECT 3030 3029 3032 CONECT 3031 3026 3027 3035 CONECT 3032 3030 3033 CONECT 3033 3032 3034 CONECT 3034 3027 3033 3042 CONECT 3035 3031 3036 3059 CONECT 3036 3035 3037 CONECT 3037 3036 3038 CONECT 3038 3037 3040 CONECT 3039 3040 3045 CONECT 3040 3038 3039 3048 CONECT 3041 3042 3044 CONECT 3042 3034 3041 3043 CONECT 3043 3042 CONECT 3044 3026 3041 3049 CONECT 3045 3039 3046 CONECT 3046 3045 3047 CONECT 3047 3046 3048 CONECT 3048 3040 3047 3050 CONECT 3049 3044 3057 CONECT 3050 3048 3058 CONECT 3051 3052 3058 CONECT 3052 3051 3053 CONECT 3053 3052 CONECT 3054 3055 3058 CONECT 3055 3054 3056 CONECT 3056 3055 CONECT 3057 3025 3049 CONECT 3058 3050 3051 3054 CONECT 3059 3035 MASTER 358 0 1 16 0 0 4 6 3058 1 39 33 END