HEADER MEMBRANE PROTEIN/INHIBITOR 23-MAR-18 5ZK3 TITLE CRYSTAL STRUCTURE OF RATIONALLY THERMOSTABILIZED M2 MUSCARINIC TITLE 2 ACETYLCHOLINE RECEPTOR BOUND WITH QNB 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 5ZK3 1 REMARK REVDAT 2 28-NOV-18 5ZK3 1 JRNL REVDAT 1 21-NOV-18 5ZK3 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. 2.60 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.91 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 14817 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.244 REMARK 3 R VALUE (WORKING SET) : 0.241 REMARK 3 FREE R VALUE : 0.291 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870 REMARK 3 FREE R VALUE TEST SET COUNT : 721 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 45.9151 - 4.4447 1.00 2862 162 0.2287 0.2871 REMARK 3 2 4.4447 - 3.5283 1.00 2844 139 0.2253 0.2763 REMARK 3 3 3.5283 - 3.0824 1.00 2786 140 0.2631 0.3003 REMARK 3 4 3.0824 - 2.8006 1.00 2830 137 0.2636 0.3171 REMARK 3 5 2.8006 - 2.5999 1.00 2774 143 0.2834 0.3053 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) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.820 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 3122 REMARK 3 ANGLE : 0.418 4260 REMARK 3 CHIRALITY : 0.035 504 REMARK 3 PLANARITY : 0.004 527 REMARK 3 DIHEDRAL : 10.330 1855 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 1023 THROUGH 1055 ) REMARK 3 ORIGIN FOR THE GROUP (A): 171.7126 11.5788 574.0858 REMARK 3 T TENSOR REMARK 3 T11: 1.1696 T22: 1.5581 REMARK 3 T33: 1.1299 T12: 0.1701 REMARK 3 T13: -0.2618 T23: 0.1099 REMARK 3 L TENSOR REMARK 3 L11: 4.8969 L22: 2.5312 REMARK 3 L33: 6.1395 L12: 0.8486 REMARK 3 L13: -5.4065 L23: -0.2987 REMARK 3 S TENSOR REMARK 3 S11: -0.0806 S12: -0.7154 S13: -0.6069 REMARK 3 S21: -0.9014 S22: 0.1560 S23: -0.6107 REMARK 3 S31: 0.6365 S32: 0.1704 S33: -0.0912 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 1056 THROUGH 1106 ) OR (RESID REMARK 3 382 THROUGH 382)) REMARK 3 ORIGIN FOR THE GROUP (A): 163.8961 17.5529 576.6252 REMARK 3 T TENSOR REMARK 3 T11: 1.2123 T22: 2.3336 REMARK 3 T33: 1.0654 T12: -0.1796 REMARK 3 T13: -0.2685 T23: 0.3578 REMARK 3 L TENSOR REMARK 3 L11: 3.6709 L22: 2.3153 REMARK 3 L33: 3.3391 L12: 1.8076 REMARK 3 L13: 3.2483 L23: 2.2758 REMARK 3 S TENSOR REMARK 3 S11: 0.3569 S12: -2.0750 S13: -0.5492 REMARK 3 S21: -0.1326 S22: 0.1884 S23: -0.0259 REMARK 3 S31: 0.3459 S32: -2.0008 S33: -0.4687 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 458 ) REMARK 3 ORIGIN FOR THE GROUP (A): 172.8287 25.6327 536.2715 REMARK 3 T TENSOR REMARK 3 T11: 0.2378 T22: 0.4722 REMARK 3 T33: 0.3657 T12: -0.0590 REMARK 3 T13: -0.0326 T23: 0.0646 REMARK 3 L TENSOR REMARK 3 L11: 3.0153 L22: 3.5573 REMARK 3 L33: 2.8161 L12: -0.7276 REMARK 3 L13: -0.4700 L23: 1.9634 REMARK 3 S TENSOR REMARK 3 S11: 0.0152 S12: -0.4794 S13: 0.0312 REMARK 3 S21: 0.0975 S22: 0.0226 S23: 0.1724 REMARK 3 S31: -0.1711 S32: 0.1629 S33: -0.1869 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 195 ) REMARK 3 ORIGIN FOR THE GROUP (A): 180.4899 33.7205 533.1282 REMARK 3 T TENSOR REMARK 3 T11: 0.2882 T22: 0.5293 REMARK 3 T33: 0.3238 T12: 0.0120 REMARK 3 T13: -0.0172 T23: -0.0382 REMARK 3 L TENSOR REMARK 3 L11: 2.4313 L22: 1.8643 REMARK 3 L33: 1.6629 L12: -0.1640 REMARK 3 L13: -0.6964 L23: -0.1900 REMARK 3 S TENSOR REMARK 3 S11: -0.1222 S12: -0.1210 S13: 0.0592 REMARK 3 S21: 0.1823 S22: 0.0725 S23: -0.1182 REMARK 3 S31: -0.0748 S32: 0.2569 S33: 0.0752 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 196 THROUGH 214) OR (RESID REMARK 3 1001 THROUGH 1022 )) REMARK 3 ORIGIN FOR THE GROUP (A): 175.7225 15.8688 555.2003 REMARK 3 T TENSOR REMARK 3 T11: 0.6867 T22: 1.5675 REMARK 3 T33: 0.5470 T12: 0.1467 REMARK 3 T13: -0.0131 T23: 0.1763 REMARK 3 L TENSOR REMARK 3 L11: 4.7478 L22: 0.2139 REMARK 3 L33: 3.6132 L12: -0.4789 REMARK 3 L13: -4.1635 L23: 0.3225 REMARK 3 S TENSOR REMARK 3 S11: -0.6892 S12: -1.9955 S13: -0.6477 REMARK 3 S21: 0.5240 S22: 0.4100 S23: -0.0814 REMARK 3 S31: 0.9635 S32: -0.0164 S33: 0.1464 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 5ZK3 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_1300007220. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-JUL-16 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 : 14817 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 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 (%) : 99.9 REMARK 200 DATA REDUNDANCY : 12.70 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.2800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76 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 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 (%): 51.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES-NAOH PH 6.2-7.0, 26-32% REMARK 280 PEG300, 300~500MM AMMONIUM FLUORIDE, 1% 1,2,3-HEPTANETRIOL, REMARK 280 0.5MM QNB AND 5% DMSO, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 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 29.40000 REMARK 290 SMTRY3 2 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 PRO A 17 REMARK 465 SER A 215 REMARK 465 ARG A 216 REMARK 465 ILE A 217 REMARK 465 PRO A 377 REMARK 465 PRO A 378 REMARK 465 PRO A 379 REMARK 465 SER A 380 REMARK 465 ARG A 381 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A1057 CG CD OE1 OE2 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 PRO A1046 76.59 -68.44 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 QNB A 501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5XBA RELATED DB: PDB REMARK 900 RELATED ID: 5XBB RELATED DB: PDB DBREF 5ZK3 A 10 217 UNP P08172 ACM2_HUMAN 10 217 DBREF 5ZK3 A 1001 1106 PDB 5ZK3 5ZK3 1001 1106 DBREF 5ZK3 A 377 466 UNP P08172 ACM2_HUMAN 377 466 SEQADV 5ZK3 GLY A -1 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 PRO A 0 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 MET A 1 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 ASP A 2 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 ASP A 3 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 SER A 4 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 THR A 5 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 ASP A 6 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 SER A 7 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 SER A 8 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 ASP A 9 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 ARG A 110 UNP P08172 SER 110 ENGINEERED MUTATION SEQADV 5ZK3 LEU A 467 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 GLU A 468 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 VAL A 469 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 LEU A 470 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 PHE A 471 UNP P08172 EXPRESSION TAG SEQADV 5ZK3 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 QNB A 501 25 HETNAM QNB (3R)-1-AZABICYCLO[2.2.2]OCT-3-YL HYDROXY(DIPHENYL) HETNAM 2 QNB ACETATE FORMUL 2 QNB C21 H23 N O3 FORMUL 3 HOH *5(H2 O) HELIX 1 AA1 TYR A 18 ASN A 51 1 34 HELIX 2 AA2 ARG A 52 GLN A 55 5 4 HELIX 3 AA3 THR A 56 PHE A 75 1 20 HELIX 4 AA4 PHE A 75 GLY A 87 1 13 HELIX 5 AA5 GLY A 92 LYS A 127 1 36 HELIX 6 AA6 TYR A 131 ARG A 135 5 5 HELIX 7 AA7 THR A 136 GLY A 167 1 32 HELIX 8 AA8 ILE A 178 SER A 182 5 5 HELIX 9 AA9 ASN A 183 PHE A 195 1 13 HELIX 10 AB1 PHE A 195 LYS A 214 1 20 HELIX 11 AB2 ASP A 1002 LYS A 1019 1 18 HELIX 12 AB3 ASN A 1022 ALA A 1043 1 22 HELIX 13 AB4 LYS A 1047 LYS A 1051 5 5 HELIX 14 AB5 SER A 1055 GLU A 1081 1 27 HELIX 15 AB6 LYS A 1083 TYR A 1101 1 19 HELIX 16 AB7 LYS A 383 THR A 411 1 29 HELIX 17 AB8 PRO A 418 ALA A 441 1 24 HELIX 18 AB9 ASN A 444 MET A 456 1 13 SSBOND 1 CYS A 96 CYS A 176 1555 1555 2.03 SSBOND 2 CYS A 413 CYS A 416 1555 1555 2.03 SITE 1 AC1 11 ASP A 103 TYR A 104 SER A 107 ASN A 108 SITE 2 AC1 11 PHE A 181 THR A 187 ALA A 191 PHE A 195 SITE 3 AC1 11 TRP A 400 TYR A 403 ASN A 404 CRYST1 46.480 58.800 89.320 90.00 99.00 90.00 P 1 21 1 2 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 0.021515 0.000000 0.003407 0.00000 SCALE2 0.000000 0.017007 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011335 0.00000 ATOM 1 N TYR A 18 152.379 28.088 512.507 1.00117.49 N ANISOU 1 N TYR A 18 11614 18774 14254 -1100 -2005 -938 N ATOM 2 CA TYR A 18 152.950 27.656 513.777 1.00114.15 C ANISOU 2 CA TYR A 18 11224 18148 14000 -1120 -1814 -994 C ATOM 3 C TYR A 18 154.264 28.371 514.080 1.00109.87 C ANISOU 3 C TYR A 18 10908 17481 13357 -980 -1692 -873 C ATOM 4 O TYR A 18 154.621 28.553 515.243 1.00109.11 O ANISOU 4 O TYR A 18 10886 17157 13413 -899 -1519 -798 O ATOM 5 CB TYR A 18 153.174 26.141 513.780 1.00116.03 C ANISOU 5 CB TYR A 18 11511 18283 14291 -1318 -1747 -1270 C ATOM 6 CG TYR A 18 151.914 25.322 513.958 1.00120.03 C ANISOU 6 CG TYR A 18 11845 18753 15008 -1449 -1770 -1371 C ATOM 7 CD1 TYR A 18 150.720 25.919 514.342 1.00119.22 C ANISOU 7 CD1 TYR A 18 11545 18689 15064 -1379 -1819 -1214 C ATOM 8 CD2 TYR A 18 151.923 23.948 513.751 1.00123.95 C ANISOU 8 CD2 TYR A 18 12374 19165 15558 -1640 -1734 -1622 C ATOM 9 CE1 TYR A 18 149.569 25.172 514.508 1.00120.55 C ANISOU 9 CE1 TYR A 18 11544 18825 15435 -1504 -1836 -1299 C ATOM 10 CE2 TYR A 18 150.777 23.193 513.915 1.00125.88 C ANISOU 10 CE2 TYR A 18 12457 19363 16007 -1770 -1751 -1710 C ATOM 11 CZ TYR A 18 149.603 23.809 514.294 1.00123.40 C ANISOU 11 CZ TYR A 18 11941 19102 15845 -1704 -1804 -1545 C ATOM 12 OH TYR A 18 148.460 23.061 514.458 1.00124.73 O ANISOU 12 OH TYR A 18 11938 19229 16225 -1838 -1818 -1625 O ATOM 13 N LYS A 19 154.976 28.777 513.025 1.00106.27 N ANISOU 13 N LYS A 19 10562 17177 12641 -953 -1780 -852 N ATOM 14 CA LYS A 19 156.293 29.382 513.204 1.00100.10 C ANISOU 14 CA LYS A 19 9995 16276 11763 -842 -1662 -754 C ATOM 15 C LYS A 19 156.208 30.681 513.997 1.00 93.48 C ANISOU 15 C LYS A 19 9145 15343 11031 -660 -1604 -502 C ATOM 16 O LYS A 19 157.055 30.949 514.859 1.00 94.20 O ANISOU 16 O LYS A 19 9376 15225 11190 -588 -1444 -451 O ATOM 17 CB LYS A 19 156.947 29.623 511.844 1.00106.92 C ANISOU 17 CB LYS A 19 10954 17345 12324 -850 -1770 -763 C ATOM 18 CG LYS A 19 157.133 28.362 511.015 1.00114.46 C ANISOU 18 CG LYS A 19 11947 18393 13151 -1026 -1815 -1034 C ATOM 19 CD LYS A 19 157.739 28.674 509.656 1.00120.71 C ANISOU 19 CD LYS A 19 12848 19388 13629 -1015 -1905 -1025 C ATOM 20 CE LYS A 19 157.884 27.417 508.812 1.00124.77 C ANISOU 20 CE LYS A 19 13436 19939 14030 -1174 -1917 -1299 C ATOM 21 NZ LYS A 19 158.451 27.712 507.466 1.00125.58 N ANISOU 21 NZ LYS A 19 13667 20216 13830 -1150 -1975 -1282 N ATOM 22 N THR A 20 155.193 31.503 513.717 1.00 86.91 N ANISOU 22 N THR A 20 8145 14661 10216 -581 -1732 -348 N ATOM 23 CA THR A 20 155.008 32.736 514.476 1.00 83.75 C ANISOU 23 CA THR A 20 7725 14155 9939 -404 -1667 -119 C ATOM 24 C THR A 20 154.782 32.436 515.953 1.00 78.84 C ANISOU 24 C THR A 20 7090 13293 9574 -393 -1495 -148 C ATOM 25 O THR A 20 155.384 33.071 516.829 1.00 79.04 O ANISOU 25 O THR A 20 7233 13131 9669 -286 -1355 -54 O ATOM 26 CB THR A 20 153.837 33.536 513.903 1.00 83.06 C ANISOU 26 CB THR A 20 7434 14277 9850 -321 -1836 44 C ATOM 27 OG1 THR A 20 152.645 32.741 513.945 1.00 86.88 O ANISOU 27 OG1 THR A 20 7701 14853 10455 -428 -1917 -68 O ATOM 28 CG2 THR A 20 154.122 33.940 512.463 1.00 79.90 C ANISOU 28 CG2 THR A 20 7065 14124 9169 -311 -2002 107 C ATOM 29 N PHE A 21 153.922 31.457 516.248 1.00 73.97 N ANISOU 29 N PHE A 21 6331 12679 9095 -508 -1500 -281 N ATOM 30 CA PHE A 21 153.704 31.059 517.635 1.00 73.85 C ANISOU 30 CA PHE A 21 6307 12443 9309 -506 -1324 -309 C ATOM 31 C PHE A 21 154.971 30.494 518.261 1.00 71.86 C ANISOU 31 C PHE A 21 6279 11985 9039 -535 -1160 -402 C ATOM 32 O PHE A 21 155.173 30.624 519.473 1.00 72.71 O ANISOU 32 O PHE A 21 6449 11900 9279 -468 -1001 -357 O ATOM 33 CB PHE A 21 152.570 30.038 517.725 1.00 73.69 C ANISOU 33 CB PHE A 21 6089 12470 9440 -645 -1357 -437 C ATOM 34 CG PHE A 21 152.334 29.520 519.116 1.00 80.65 C ANISOU 34 CG PHE A 21 6963 13129 10550 -654 -1162 -462 C ATOM 35 CD1 PHE A 21 151.563 30.239 520.014 1.00 86.36 C ANISOU 35 CD1 PHE A 21 7576 13795 11443 -533 -1086 -316 C ATOM 36 CD2 PHE A 21 152.885 28.317 519.526 1.00 83.32 C ANISOU 36 CD2 PHE A 21 7410 13316 10930 -776 -1044 -626 C ATOM 37 CE1 PHE A 21 151.346 29.768 521.296 1.00 88.26 C ANISOU 37 CE1 PHE A 21 7818 13846 11872 -537 -897 -333 C ATOM 38 CE2 PHE A 21 152.673 27.841 520.806 1.00 86.01 C ANISOU 38 CE2 PHE A 21 7751 13461 11468 -777 -860 -628 C ATOM 39 CZ PHE A 21 151.902 28.568 521.692 1.00 87.76 C ANISOU 39 CZ PHE A 21 7866 13642 11837 -659 -787 -481 C ATOM 40 N GLU A 22 155.830 29.855 517.463 1.00 67.60 N ANISOU 40 N GLU A 22 5859 11491 8335 -629 -1195 -533 N ATOM 41 CA GLU A 22 157.092 29.362 518.003 1.00 69.07 C ANISOU 41 CA GLU A 22 6247 11494 8503 -640 -1046 -606 C ATOM 42 C GLU A 22 158.019 30.515 518.366 1.00 68.60 C ANISOU 42 C GLU A 22 6326 11356 8382 -493 -983 -450 C ATOM 43 O GLU A 22 158.712 30.463 519.390 1.00 65.04 O ANISOU 43 O GLU A 22 5989 10718 8004 -450 -838 -442 O ATOM 44 CB GLU A 22 157.765 28.419 517.004 1.00 74.64 C ANISOU 44 CB GLU A 22 7037 12271 9053 -767 -1091 -787 C ATOM 45 CG GLU A 22 156.990 27.136 516.744 1.00 82.71 C ANISOU 45 CG GLU A 22 7948 13324 10155 -936 -1126 -981 C ATOM 46 CD GLU A 22 157.754 26.156 515.874 1.00 89.82 C ANISOU 46 CD GLU A 22 8959 14254 10915 -1057 -1137 -1183 C ATOM 47 OE1 GLU A 22 158.770 25.604 516.346 1.00 91.76 O ANISOU 47 OE1 GLU A 22 9359 14324 11183 -1055 -991 -1243 O ATOM 48 OE2 GLU A 22 157.343 25.943 514.714 1.00 93.49 O ANISOU 48 OE2 GLU A 22 9356 14923 11243 -1148 -1290 -1282 O ATOM 49 N VAL A 23 158.036 31.570 517.548 1.00 69.61 N ANISOU 49 N VAL A 23 6443 11625 8380 -417 -1093 -321 N ATOM 50 CA VAL A 23 158.859 32.735 517.862 1.00 65.77 C ANISOU 50 CA VAL A 23 6079 11053 7858 -287 -1032 -169 C ATOM 51 C VAL A 23 158.341 33.430 519.116 1.00 64.51 C ANISOU 51 C VAL A 23 5878 10746 7886 -177 -937 -59 C ATOM 52 O VAL A 23 159.113 33.766 520.024 1.00 67.20 O ANISOU 52 O VAL A 23 6344 10918 8271 -118 -813 -32 O ATOM 53 CB VAL A 23 158.911 33.697 516.662 1.00 66.65 C ANISOU 53 CB VAL A 23 6181 11343 7798 -230 -1163 -38 C ATOM 54 CG1 VAL A 23 159.640 34.977 517.040 1.00 59.47 C ANISOU 54 CG1 VAL A 23 5382 10322 6894 -100 -1091 129 C ATOM 55 CG2 VAL A 23 159.584 33.027 515.475 1.00 71.74 C ANISOU 55 CG2 VAL A 23 6897 12130 8230 -333 -1231 -155 C ATOM 56 N VAL A 24 157.025 33.652 519.188 1.00 62.40 N ANISOU 56 N VAL A 24 5431 10549 7729 -147 -995 1 N ATOM 57 CA VAL A 24 156.444 34.293 520.367 1.00 55.65 C ANISOU 57 CA VAL A 24 4529 9560 7055 -36 -891 97 C ATOM 58 C VAL A 24 156.709 33.458 521.614 1.00 54.73 C ANISOU 58 C VAL A 24 4480 9263 7050 -79 -730 -9 C ATOM 59 O VAL A 24 157.064 33.989 522.674 1.00 60.23 O ANISOU 59 O VAL A 24 5267 9804 7813 9 -604 42 O ATOM 60 CB VAL A 24 154.937 34.534 520.159 1.00 54.43 C ANISOU 60 CB VAL A 24 4142 9530 7009 -4 -979 170 C ATOM 61 CG1 VAL A 24 154.325 35.171 521.399 1.00 51.54 C ANISOU 61 CG1 VAL A 24 3727 9021 6835 117 -849 261 C ATOM 62 CG2 VAL A 24 154.698 35.405 518.936 1.00 51.07 C ANISOU 62 CG2 VAL A 24 3651 9292 6460 58 -1145 302 C ATOM 63 N PHE A 25 156.553 32.137 521.501 1.00 49.86 N ANISOU 63 N PHE A 25 3827 8664 6452 -216 -729 -158 N ATOM 64 CA PHE A 25 156.794 31.254 522.638 1.00 57.45 C ANISOU 64 CA PHE A 25 4853 9456 7518 -256 -573 -243 C ATOM 65 C PHE A 25 158.247 31.325 523.095 1.00 59.62 C ANISOU 65 C PHE A 25 5342 9605 7708 -223 -483 -256 C ATOM 66 O PHE A 25 158.523 31.417 524.297 1.00 60.89 O ANISOU 66 O PHE A 25 5578 9619 7938 -163 -351 -231 O ATOM 67 CB PHE A 25 156.408 29.821 522.263 1.00 61.49 C ANISOU 67 CB PHE A 25 5291 10002 8069 -418 -593 -400 C ATOM 68 CG PHE A 25 156.562 28.832 523.384 1.00 65.63 C ANISOU 68 CG PHE A 25 5871 10349 8715 -461 -428 -470 C ATOM 69 CD1 PHE A 25 155.591 28.720 524.366 1.00 62.29 C ANISOU 69 CD1 PHE A 25 5340 9857 8470 -440 -329 -426 C ATOM 70 CD2 PHE A 25 157.670 28.002 523.446 1.00 69.31 C ANISOU 70 CD2 PHE A 25 6493 10721 9122 -514 -363 -567 C ATOM 71 CE1 PHE A 25 155.727 27.807 525.395 1.00 59.28 C ANISOU 71 CE1 PHE A 25 5015 9317 8191 -474 -168 -470 C ATOM 72 CE2 PHE A 25 157.811 27.087 524.472 1.00 67.03 C ANISOU 72 CE2 PHE A 25 6256 10269 8945 -541 -210 -608 C ATOM 73 CZ PHE A 25 156.838 26.989 525.448 1.00 60.62 C ANISOU 73 CZ PHE A 25 5345 9391 8297 -522 -112 -555 C ATOM 74 N ILE A 26 159.188 31.297 522.146 1.00 57.58 N ANISOU 74 N ILE A 26 5175 9412 7290 -260 -554 -294 N ATOM 75 CA ILE A 26 160.605 31.366 522.495 1.00 58.61 C ANISOU 75 CA ILE A 26 5486 9440 7344 -232 -478 -305 C ATOM 76 C ILE A 26 160.927 32.690 523.177 1.00 56.18 C ANISOU 76 C ILE A 26 5241 9055 7049 -104 -433 -175 C ATOM 77 O ILE A 26 161.667 32.729 524.169 1.00 59.99 O ANISOU 77 O ILE A 26 5833 9407 7554 -65 -329 -179 O ATOM 78 CB ILE A 26 161.474 31.145 521.242 1.00 63.82 C ANISOU 78 CB ILE A 26 6211 10204 7832 -293 -557 -364 C ATOM 79 CG1 ILE A 26 161.442 29.673 520.825 1.00 66.13 C ANISOU 79 CG1 ILE A 26 6489 10514 8122 -424 -556 -534 C ATOM 80 CG2 ILE A 26 162.905 31.601 521.489 1.00 64.19 C ANISOU 80 CG2 ILE A 26 6415 10170 7803 -243 -495 -333 C ATOM 81 CD1 ILE A 26 161.901 28.722 521.909 1.00 66.16 C ANISOU 81 CD1 ILE A 26 6567 10342 8230 -442 -412 -604 C ATOM 82 N VAL A 27 160.376 33.793 522.666 1.00 52.32 N ANISOU 82 N VAL A 27 4684 8644 6550 -34 -512 -58 N ATOM 83 CA VAL A 27 160.637 35.096 523.275 1.00 53.57 C ANISOU 83 CA VAL A 27 4905 8710 6740 85 -462 58 C ATOM 84 C VAL A 27 160.068 35.151 524.688 1.00 58.91 C ANISOU 84 C VAL A 27 5564 9257 7560 145 -342 62 C ATOM 85 O VAL A 27 160.709 35.669 525.613 1.00 62.20 O ANISOU 85 O VAL A 27 6095 9549 7990 204 -252 75 O ATOM 86 CB VAL A 27 160.073 36.223 522.388 1.00 55.69 C ANISOU 86 CB VAL A 27 5095 9079 6984 156 -565 196 C ATOM 87 CG1 VAL A 27 160.136 37.558 523.113 1.00 51.32 C ANISOU 87 CG1 VAL A 27 4592 8398 6508 283 -495 309 C ATOM 88 CG2 VAL A 27 160.842 36.295 521.079 1.00 60.52 C ANISOU 88 CG2 VAL A 27 5758 9811 7425 109 -661 208 C ATOM 89 N LEU A 28 158.865 34.604 524.884 1.00 58.25 N ANISOU 89 N LEU A 28 5338 9210 7582 126 -336 46 N ATOM 90 CA LEU A 28 158.236 34.651 526.201 1.00 53.50 C ANISOU 90 CA LEU A 28 4713 8501 7115 187 -207 59 C ATOM 91 C LEU A 28 159.006 33.813 527.216 1.00 51.51 C ANISOU 91 C LEU A 28 4587 8133 6853 151 -89 -26 C ATOM 92 O LEU A 28 159.341 34.296 528.306 1.00 52.45 O ANISOU 92 O LEU A 28 4801 8143 6987 227 13 -7 O ATOM 93 CB LEU A 28 156.782 34.184 526.108 1.00 52.72 C ANISOU 93 CB LEU A 28 4414 8477 7140 161 -223 64 C ATOM 94 CG LEU A 28 155.800 35.145 525.434 1.00 51.76 C ANISOU 94 CG LEU A 28 4139 8461 7065 238 -319 179 C ATOM 95 CD1 LEU A 28 154.379 34.609 525.520 1.00 60.04 C ANISOU 95 CD1 LEU A 28 4972 9581 8259 208 -320 176 C ATOM 96 CD2 LEU A 28 155.892 36.532 526.052 1.00 51.36 C ANISOU 96 CD2 LEU A 28 4153 8309 7053 391 -249 286 C ATOM 97 N VAL A 29 159.294 32.552 526.881 1.00 49.42 N ANISOU 97 N VAL A 29 4327 7890 6561 39 -101 -122 N ATOM 98 CA VAL A 29 160.006 31.700 527.830 1.00 55.73 C ANISOU 98 CA VAL A 29 5237 8578 7358 17 13 -182 C ATOM 99 C VAL A 29 161.421 32.216 528.062 1.00 58.77 C ANISOU 99 C VAL A 29 5787 8911 7631 60 20 -178 C ATOM 100 O VAL A 29 161.970 32.069 529.162 1.00 64.95 O ANISOU 100 O VAL A 29 6669 9601 8409 98 117 -185 O ATOM 101 CB VAL A 29 160.006 30.234 527.354 1.00 60.58 C ANISOU 101 CB VAL A 29 5822 9210 7988 -109 6 -285 C ATOM 102 CG1 VAL A 29 158.581 29.740 527.154 1.00 62.95 C ANISOU 102 CG1 VAL A 29 5943 9561 8416 -169 -4 -298 C ATOM 103 CG2 VAL A 29 160.818 30.074 526.078 1.00 66.70 C ANISOU 103 CG2 VAL A 29 6638 10068 8639 -173 -105 -342 C ATOM 104 N ALA A 30 162.025 32.843 527.052 1.00 55.10 N ANISOU 104 N ALA A 30 5349 8513 7072 54 -80 -160 N ATOM 105 CA ALA A 30 163.378 33.366 527.206 1.00 52.22 C ANISOU 105 CA ALA A 30 5121 8104 6617 82 -74 -155 C ATOM 106 C ALA A 30 163.396 34.568 528.141 1.00 54.51 C ANISOU 106 C ALA A 30 5463 8311 6936 181 -23 -92 C ATOM 107 O ALA A 30 164.235 34.651 529.048 1.00 55.18 O ANISOU 107 O ALA A 30 5655 8320 6992 206 37 -115 O ATOM 108 CB ALA A 30 163.950 33.732 525.838 1.00 44.41 C ANISOU 108 CB ALA A 30 4137 7210 5526 46 -180 -143 C ATOM 109 N GLY A 31 162.475 35.514 527.934 1.00 50.89 N ANISOU 109 N GLY A 31 4929 7870 6537 241 -47 -16 N ATOM 110 CA GLY A 31 162.369 36.636 528.851 1.00 49.03 C ANISOU 110 CA GLY A 31 4742 7538 6348 339 20 28 C ATOM 111 C GLY A 31 162.024 36.199 530.262 1.00 45.54 C ANISOU 111 C GLY A 31 4326 7020 5955 373 143 -11 C ATOM 112 O GLY A 31 162.494 36.789 531.239 1.00 37.37 O ANISOU 112 O GLY A 31 3395 5902 4903 427 209 -26 O ATOM 113 N SER A 32 161.205 35.152 530.386 1.00 45.48 N ANISOU 113 N SER A 32 4228 7046 6005 336 177 -31 N ATOM 114 CA SER A 32 160.872 34.623 531.705 1.00 51.58 C ANISOU 114 CA SER A 32 5027 7754 6818 365 309 -53 C ATOM 115 C SER A 32 162.107 34.051 532.393 1.00 52.26 C ANISOU 115 C SER A 32 5256 7795 6808 344 345 -105 C ATOM 116 O SER A 32 162.355 34.320 533.575 1.00 55.63 O ANISOU 116 O SER A 32 5772 8161 7204 404 431 -112 O ATOM 117 CB SER A 32 159.780 33.561 531.581 1.00 57.69 C ANISOU 117 CB SER A 32 5664 8567 7690 310 340 -57 C ATOM 118 OG SER A 32 158.620 34.097 530.970 1.00 61.44 O ANISOU 118 OG SER A 32 5986 9103 8257 334 295 -5 O ATOM 119 N LEU A 33 162.896 33.258 531.662 1.00 51.46 N ANISOU 119 N LEU A 33 5172 7728 6651 264 281 -144 N ATOM 120 CA LEU A 33 164.117 32.691 532.230 1.00 52.36 C ANISOU 120 CA LEU A 33 5404 7807 6682 254 307 -181 C ATOM 121 C LEU A 33 165.090 33.787 532.648 1.00 49.39 C ANISOU 121 C LEU A 33 5133 7404 6227 303 285 -182 C ATOM 122 O LEU A 33 165.635 33.760 533.759 1.00 46.05 O ANISOU 122 O LEU A 33 4801 6943 5753 342 340 -197 O ATOM 123 CB LEU A 33 164.772 31.744 531.226 1.00 51.62 C ANISOU 123 CB LEU A 33 5300 7754 6557 168 245 -224 C ATOM 124 CG LEU A 33 164.042 30.424 530.973 1.00 56.72 C ANISOU 124 CG LEU A 33 5868 8402 7282 101 282 -254 C ATOM 125 CD1 LEU A 33 164.698 29.653 529.838 1.00 59.98 C ANISOU 125 CD1 LEU A 33 6279 8853 7656 18 217 -317 C ATOM 126 CD2 LEU A 33 163.999 29.588 532.243 1.00 55.29 C ANISOU 126 CD2 LEU A 33 5733 8142 7131 130 407 -242 C ATOM 127 N SER A 34 165.316 34.765 531.767 1.00 49.14 N ANISOU 127 N SER A 34 5090 7395 6186 297 203 -163 N ATOM 128 CA SER A 34 166.219 35.865 532.093 1.00 50.14 C ANISOU 128 CA SER A 34 5308 7480 6262 327 184 -168 C ATOM 129 C SER A 34 165.751 36.608 533.339 1.00 50.85 C ANISOU 129 C SER A 34 5447 7500 6374 406 266 -174 C ATOM 130 O SER A 34 166.543 36.883 534.249 1.00 53.44 O ANISOU 130 O SER A 34 5873 7793 6637 424 288 -218 O ATOM 131 CB SER A 34 166.329 36.817 530.902 1.00 51.72 C ANISOU 131 CB SER A 34 5477 7702 6470 311 102 -124 C ATOM 132 OG SER A 34 167.126 37.946 531.217 1.00 57.13 O ANISOU 132 OG SER A 34 6245 8326 7136 330 95 -129 O ATOM 133 N LEU A 35 164.456 36.928 533.402 1.00 53.55 N ANISOU 133 N LEU A 35 5714 7827 6804 456 312 -136 N ATOM 134 CA LEU A 35 163.931 37.677 534.539 1.00 53.34 C ANISOU 134 CA LEU A 35 5732 7731 6803 541 408 -147 C ATOM 135 C LEU A 35 164.079 36.890 535.837 1.00 53.63 C ANISOU 135 C LEU A 35 5838 7763 6776 559 499 -187 C ATOM 136 O LEU A 35 164.501 37.441 536.862 1.00 53.80 O ANISOU 136 O LEU A 35 5965 7745 6733 602 544 -235 O ATOM 137 CB LEU A 35 162.468 38.040 534.289 1.00 57.14 C ANISOU 137 CB LEU A 35 6095 8210 7406 597 449 -88 C ATOM 138 CG LEU A 35 161.830 39.018 535.274 1.00 64.97 C ANISOU 138 CG LEU A 35 7120 9119 8445 701 557 -95 C ATOM 139 CD1 LEU A 35 162.630 40.308 535.336 1.00 67.51 C ANISOU 139 CD1 LEU A 35 7550 9359 8742 723 530 -127 C ATOM 140 CD2 LEU A 35 160.389 39.295 534.877 1.00 67.94 C ANISOU 140 CD2 LEU A 35 7348 9507 8959 761 590 -21 C ATOM 141 N VAL A 36 163.742 35.597 535.811 1.00 51.38 N ANISOU 141 N VAL A 36 5498 7519 6504 524 528 -169 N ATOM 142 CA VAL A 36 163.877 34.771 537.009 1.00 49.84 C ANISOU 142 CA VAL A 36 5369 7320 6248 546 622 -180 C ATOM 143 C VAL A 36 165.331 34.719 537.463 1.00 47.82 C ANISOU 143 C VAL A 36 5234 7073 5862 535 573 -222 C ATOM 144 O VAL A 36 165.630 34.852 538.658 1.00 50.36 O ANISOU 144 O VAL A 36 5650 7389 6094 586 629 -246 O ATOM 145 CB VAL A 36 163.311 33.361 536.754 1.00 48.26 C ANISOU 145 CB VAL A 36 5085 7141 6112 498 662 -146 C ATOM 146 CG1 VAL A 36 163.710 32.413 537.877 1.00 49.88 C ANISOU 146 CG1 VAL A 36 5372 7336 6244 519 750 -135 C ATOM 147 CG2 VAL A 36 161.797 33.418 536.617 1.00 43.00 C ANISOU 147 CG2 VAL A 36 4289 6472 5575 514 728 -107 C ATOM 148 N THR A 37 166.256 34.533 536.518 1.00 46.82 N ANISOU 148 N THR A 37 5098 6974 5718 471 467 -232 N ATOM 149 CA THR A 37 167.677 34.508 536.857 1.00 52.31 C ANISOU 149 CA THR A 37 5880 7688 6307 458 412 -268 C ATOM 150 C THR A 37 168.101 35.806 537.537 1.00 54.86 C ANISOU 150 C THR A 37 6286 7984 6573 491 399 -320 C ATOM 151 O THR A 37 168.703 35.790 538.622 1.00 67.14 O ANISOU 151 O THR A 37 7928 9556 8026 520 413 -356 O ATOM 152 CB THR A 37 168.505 34.266 535.592 1.00 55.79 C ANISOU 152 CB THR A 37 6282 8160 6757 386 314 -270 C ATOM 153 OG1 THR A 37 167.994 33.123 534.895 1.00 55.16 O ANISOU 153 OG1 THR A 37 6127 8097 6736 349 330 -245 O ATOM 154 CG2 THR A 37 169.967 34.028 535.942 1.00 54.01 C ANISOU 154 CG2 THR A 37 6118 7964 6438 375 265 -297 C ATOM 155 N ILE A 38 167.775 36.943 536.914 1.00 47.05 N ANISOU 155 N ILE A 38 5274 6952 5652 487 371 -325 N ATOM 156 CA ILE A 38 168.156 38.244 537.461 1.00 43.61 C ANISOU 156 CA ILE A 38 4918 6462 5191 507 365 -386 C ATOM 157 C ILE A 38 167.605 38.415 538.872 1.00 47.58 C ANISOU 157 C ILE A 38 5494 6944 5642 581 467 -428 C ATOM 158 O ILE A 38 168.340 38.754 539.809 1.00 45.23 O ANISOU 158 O ILE A 38 5293 6653 5239 588 459 -503 O ATOM 159 CB ILE A 38 167.678 39.372 536.530 1.00 40.01 C ANISOU 159 CB ILE A 38 4418 5942 4844 506 343 -358 C ATOM 160 CG1 ILE A 38 168.404 39.303 535.185 1.00 42.43 C ANISOU 160 CG1 ILE A 38 4674 6281 5167 431 243 -318 C ATOM 161 CG2 ILE A 38 167.880 40.730 537.180 1.00 38.83 C ANISOU 161 CG2 ILE A 38 4355 5700 4697 533 367 -427 C ATOM 162 CD1 ILE A 38 167.905 40.312 534.170 1.00 43.71 C ANISOU 162 CD1 ILE A 38 4787 6396 5425 438 220 -259 C ATOM 163 N ILE A 39 166.304 38.168 539.046 1.00 51.96 N ANISOU 163 N ILE A 39 5996 7484 6262 637 566 -384 N ATOM 164 CA ILE A 39 165.666 38.404 540.340 1.00 48.60 C ANISOU 164 CA ILE A 39 5636 7040 5791 716 687 -419 C ATOM 165 C ILE A 39 166.284 37.513 541.411 1.00 47.11 C ANISOU 165 C ILE A 39 5529 6921 5450 726 710 -434 C ATOM 166 O ILE A 39 166.628 37.976 542.506 1.00 43.91 O ANISOU 166 O ILE A 39 5233 6524 4925 762 739 -508 O ATOM 167 CB ILE A 39 164.146 38.190 540.237 1.00 44.24 C ANISOU 167 CB ILE A 39 4984 6469 5355 770 796 -353 C ATOM 168 CG1 ILE A 39 163.520 39.243 539.319 1.00 42.92 C ANISOU 168 CG1 ILE A 39 4742 6239 5328 786 773 -331 C ATOM 169 CG2 ILE A 39 163.507 38.236 541.616 1.00 43.21 C ANISOU 169 CG2 ILE A 39 4919 6333 5164 854 945 -380 C ATOM 170 CD1 ILE A 39 162.026 39.086 539.144 1.00 43.87 C ANISOU 170 CD1 ILE A 39 4735 6356 5578 841 863 -261 C ATOM 171 N GLY A 40 166.440 36.223 541.109 1.00 45.05 N ANISOU 171 N GLY A 40 5218 6712 5188 695 696 -365 N ATOM 172 CA GLY A 40 166.989 35.308 542.098 1.00 49.40 C ANISOU 172 CA GLY A 40 5840 7325 5605 719 723 -349 C ATOM 173 C GLY A 40 168.396 35.683 542.523 1.00 51.17 C ANISOU 173 C GLY A 40 6152 7596 5693 700 618 -417 C ATOM 174 O GLY A 40 168.690 35.803 543.718 1.00 53.42 O ANISOU 174 O GLY A 40 6536 7928 5832 747 645 -457 O ATOM 175 N ASN A 41 169.285 35.892 541.548 1.00 53.25 N ANISOU 175 N ASN A 41 6377 7858 5998 630 496 -435 N ATOM 176 CA ASN A 41 170.675 36.175 541.894 1.00 50.02 C ANISOU 176 CA ASN A 41 6023 7502 5478 601 390 -495 C ATOM 177 C ASN A 41 170.814 37.521 542.597 1.00 50.43 C ANISOU 177 C ASN A 41 6161 7528 5472 605 381 -610 C ATOM 178 O ASN A 41 171.643 37.668 543.506 1.00 50.97 O ANISOU 178 O ASN A 41 6304 7663 5400 608 331 -676 O ATOM 179 CB ASN A 41 171.547 36.109 540.644 1.00 45.17 C ANISOU 179 CB ASN A 41 5336 6889 4936 522 283 -483 C ATOM 180 CG ASN A 41 171.667 34.701 540.105 1.00 47.00 C ANISOU 180 CG ASN A 41 5505 7154 5199 518 289 -396 C ATOM 181 OD1 ASN A 41 172.344 33.858 540.691 1.00 52.00 O ANISOU 181 OD1 ASN A 41 6162 7848 5748 545 277 -367 O ATOM 182 ND2 ASN A 41 171.001 34.434 538.990 1.00 47.33 N ANISOU 182 ND2 ASN A 41 5468 7156 5361 486 306 -357 N ATOM 183 N ILE A 42 170.006 38.510 542.206 1.00 44.09 N ANISOU 183 N ILE A 42 5348 6628 4777 609 427 -640 N ATOM 184 CA ILE A 42 170.024 39.785 542.917 1.00 46.62 C ANISOU 184 CA ILE A 42 5760 6895 5059 620 444 -760 C ATOM 185 C ILE A 42 169.556 39.597 544.356 1.00 51.28 C ANISOU 185 C ILE A 42 6445 7533 5506 700 543 -801 C ATOM 186 O ILE A 42 170.111 40.193 545.288 1.00 55.56 O ANISOU 186 O ILE A 42 7089 8102 5919 699 518 -918 O ATOM 187 CB ILE A 42 169.177 40.832 542.170 1.00 51.70 C ANISOU 187 CB ILE A 42 6367 7408 5867 627 491 -761 C ATOM 188 CG1 ILE A 42 169.889 41.276 540.892 1.00 55.60 C ANISOU 188 CG1 ILE A 42 6799 7863 6463 542 384 -738 C ATOM 189 CG2 ILE A 42 168.908 42.034 543.056 1.00 52.53 C ANISOU 189 CG2 ILE A 42 6576 7435 5948 664 556 -886 C ATOM 190 CD1 ILE A 42 169.175 42.385 540.151 1.00 62.64 C ANISOU 190 CD1 ILE A 42 7663 8628 7511 556 420 -722 C ATOM 191 N LEU A 43 168.539 38.755 544.564 1.00 50.13 N ANISOU 191 N LEU A 43 6267 7404 5375 766 657 -707 N ATOM 192 CA LEU A 43 168.089 38.471 545.925 1.00 49.45 C ANISOU 192 CA LEU A 43 6271 7376 5142 847 769 -722 C ATOM 193 C LEU A 43 169.197 37.826 546.749 1.00 52.32 C ANISOU 193 C LEU A 43 6706 7869 5305 844 691 -730 C ATOM 194 O LEU A 43 169.356 38.133 547.938 1.00 40.80 O ANISOU 194 O LEU A 43 5360 6473 3668 886 718 -810 O ATOM 195 CB LEU A 43 166.850 37.576 545.899 1.00 49.47 C ANISOU 195 CB LEU A 43 6205 7371 5219 903 909 -600 C ATOM 196 CG LEU A 43 165.523 38.260 545.564 1.00 51.20 C ANISOU 196 CG LEU A 43 6366 7492 5596 944 1023 -598 C ATOM 197 CD1 LEU A 43 164.398 37.242 545.470 1.00 47.18 C ANISOU 197 CD1 LEU A 43 5760 6990 5174 977 1145 -473 C ATOM 198 CD2 LEU A 43 165.198 39.323 546.599 1.00 53.25 C ANISOU 198 CD2 LEU A 43 6739 7721 5773 1010 1117 -718 C ATOM 199 N VAL A 44 169.979 36.935 546.135 1.00 47.07 N ANISOU 199 N VAL A 44 5974 7251 4659 801 595 -648 N ATOM 200 CA VAL A 44 171.090 36.311 546.854 1.00 44.28 C ANISOU 200 CA VAL A 44 5668 7025 4130 810 510 -637 C ATOM 201 C VAL A 44 172.133 37.356 547.235 1.00 46.58 C ANISOU 201 C VAL A 44 6021 7356 4321 758 383 -788 C ATOM 202 O VAL A 44 172.523 37.475 548.405 1.00 50.10 O ANISOU 202 O VAL A 44 6562 7904 4568 792 363 -851 O ATOM 203 CB VAL A 44 171.708 35.180 546.014 1.00 42.51 C ANISOU 203 CB VAL A 44 5349 6823 3980 781 443 -522 C ATOM 204 CG1 VAL A 44 172.954 34.638 546.698 1.00 47.46 C ANISOU 204 CG1 VAL A 44 6008 7582 4441 798 341 -505 C ATOM 205 CG2 VAL A 44 170.692 34.071 545.790 1.00 39.54 C ANISOU 205 CG2 VAL A 44 4924 6407 3694 822 573 -389 C ATOM 206 N MET A 45 172.594 38.134 546.251 1.00 46.08 N ANISOU 206 N MET A 45 5901 7215 4391 671 297 -847 N ATOM 207 CA MET A 45 173.645 39.118 546.506 1.00 50.31 C ANISOU 207 CA MET A 45 6477 7773 4866 598 175 -991 C ATOM 208 C MET A 45 173.219 40.123 547.572 1.00 54.66 C ANISOU 208 C MET A 45 7153 8303 5312 623 233 -1141 C ATOM 209 O MET A 45 173.957 40.379 548.533 1.00 61.84 O ANISOU 209 O MET A 45 8138 9315 6043 610 158 -1248 O ATOM 210 CB MET A 45 174.012 39.833 545.205 1.00 54.97 C ANISOU 210 CB MET A 45 6986 8255 5644 503 111 -1010 C ATOM 211 CG MET A 45 174.610 38.922 544.143 1.00 54.88 C ANISOU 211 CG MET A 45 6858 8276 5715 469 46 -889 C ATOM 212 SD MET A 45 174.528 39.630 542.485 0.66 54.21 S ANISOU 212 SD MET A 45 6684 8059 5853 388 31 -866 S ATOM 213 CE MET A 45 175.324 41.212 542.750 1.00 54.94 C ANISOU 213 CE MET A 45 6829 8091 5953 297 -43 -1031 C ATOM 214 N VAL A 46 172.024 40.699 547.421 1.00 54.56 N ANISOU 214 N VAL A 46 7160 8164 5405 663 368 -1155 N ATOM 215 CA VAL A 46 171.541 41.675 548.394 1.00 56.08 C ANISOU 215 CA VAL A 46 7476 8317 5515 697 450 -1306 C ATOM 216 C VAL A 46 171.377 41.027 549.763 1.00 61.85 C ANISOU 216 C VAL A 46 8303 9194 6002 782 507 -1307 C ATOM 217 O VAL A 46 171.700 41.631 550.795 1.00 67.37 O ANISOU 217 O VAL A 46 9120 9950 6526 782 491 -1462 O ATOM 218 CB VAL A 46 170.226 42.310 547.902 1.00 55.79 C ANISOU 218 CB VAL A 46 7421 8117 5662 745 597 -1292 C ATOM 219 CG1 VAL A 46 169.631 43.215 548.972 1.00 52.24 C ANISOU 219 CG1 VAL A 46 7101 7621 5126 803 714 -1444 C ATOM 220 CG2 VAL A 46 170.465 43.090 546.619 1.00 56.37 C ANISOU 220 CG2 VAL A 46 7416 8053 5950 666 533 -1291 C ATOM 221 N SER A 47 170.888 39.784 549.795 1.00 63.56 N ANISOU 221 N SER A 47 8477 9476 6199 852 578 -1136 N ATOM 222 CA SER A 47 170.715 39.094 551.070 1.00 64.34 C ANISOU 222 CA SER A 47 8666 9714 6065 940 647 -1102 C ATOM 223 C SER A 47 172.043 38.924 551.793 1.00 66.62 C ANISOU 223 C SER A 47 9009 10172 6133 913 485 -1157 C ATOM 224 O SER A 47 172.112 39.060 553.021 1.00 65.74 O ANISOU 224 O SER A 47 9019 10177 5784 961 504 -1235 O ATOM 225 CB SER A 47 170.048 37.738 550.849 1.00 65.16 C ANISOU 225 CB SER A 47 8700 9835 6224 1004 748 -891 C ATOM 226 OG SER A 47 168.704 37.907 550.442 1.00 70.04 O ANISOU 226 OG SER A 47 9273 10329 7011 1039 909 -852 O ATOM 227 N ILE A 48 173.113 38.630 551.052 1.00 64.32 N ANISOU 227 N ILE A 48 8623 9906 5909 839 325 -1119 N ATOM 228 CA ILE A 48 174.421 38.532 551.689 1.00 60.73 C ANISOU 228 CA ILE A 48 8192 9619 5264 810 155 -1173 C ATOM 229 C ILE A 48 174.921 39.908 552.111 1.00 63.25 C ANISOU 229 C ILE A 48 8585 9929 5517 727 71 -1413 C ATOM 230 O ILE A 48 175.583 40.044 553.148 1.00 69.25 O ANISOU 230 O ILE A 48 9422 10847 6043 727 -21 -1512 O ATOM 231 CB ILE A 48 175.419 37.825 550.754 1.00 60.31 C ANISOU 231 CB ILE A 48 8002 9592 5321 760 22 -1063 C ATOM 232 CG1 ILE A 48 174.905 36.432 550.392 1.00 62.72 C ANISOU 232 CG1 ILE A 48 8248 9890 5692 840 117 -844 C ATOM 233 CG2 ILE A 48 176.788 37.723 551.408 1.00 58.04 C ANISOU 233 CG2 ILE A 48 7714 9490 4849 736 -161 -1109 C ATOM 234 CD1 ILE A 48 175.771 35.703 549.397 1.00 42.28 C ANISOU 234 CD1 ILE A 48 5530 7304 3230 801 17 -741 C ATOM 235 N LYS A 49 174.604 40.951 551.339 1.00 61.53 N ANISOU 235 N LYS A 49 8347 9528 5502 655 101 -1511 N ATOM 236 CA LYS A 49 175.141 42.273 551.652 1.00 64.41 C ANISOU 236 CA LYS A 49 8778 9852 5843 560 24 -1743 C ATOM 237 C LYS A 49 174.450 42.920 552.849 1.00 69.28 C ANISOU 237 C LYS A 49 9558 10477 6289 616 135 -1901 C ATOM 238 O LYS A 49 175.066 43.736 553.543 1.00 71.62 O ANISOU 238 O LYS A 49 9937 10817 6459 549 50 -2110 O ATOM 239 CB LYS A 49 175.038 43.187 550.431 1.00 66.73 C ANISOU 239 CB LYS A 49 9004 9932 6419 473 34 -1778 C ATOM 240 CG LYS A 49 175.957 42.807 549.277 1.00 74.45 C ANISOU 240 CG LYS A 49 9833 10910 7542 391 -92 -1674 C ATOM 241 CD LYS A 49 177.189 43.703 549.199 1.00 82.80 C ANISOU 241 CD LYS A 49 10871 11967 8623 248 -247 -1831 C ATOM 242 CE LYS A 49 178.216 43.362 550.267 1.00 90.23 C ANISOU 242 CE LYS A 49 11835 13129 9318 230 -394 -1908 C ATOM 243 NZ LYS A 49 179.438 44.203 550.152 1.00 92.74 N ANISOU 243 NZ LYS A 49 12107 13452 9678 75 -552 -2064 N ATOM 244 N VAL A 50 173.186 42.579 553.115 1.00 67.55 N ANISOU 244 N VAL A 50 9383 10217 6065 734 327 -1817 N ATOM 245 CA VAL A 50 172.431 43.252 554.173 1.00 68.63 C ANISOU 245 CA VAL A 50 9673 10343 6062 796 464 -1969 C ATOM 246 C VAL A 50 172.348 42.447 555.464 1.00 72.25 C ANISOU 246 C VAL A 50 10229 11018 6205 895 502 -1928 C ATOM 247 O VAL A 50 171.964 43.008 556.503 1.00 71.33 O ANISOU 247 O VAL A 50 10258 10939 5904 938 590 -2084 O ATOM 248 CB VAL A 50 171.004 43.612 553.703 1.00 68.72 C ANISOU 248 CB VAL A 50 9672 10161 6279 868 677 -1924 C ATOM 249 CG1 VAL A 50 171.053 44.380 552.387 1.00 67.07 C ANISOU 249 CG1 VAL A 50 9364 9745 6373 784 640 -1933 C ATOM 250 CG2 VAL A 50 170.149 42.358 553.579 1.00 69.94 C ANISOU 250 CG2 VAL A 50 9759 10364 6452 972 799 -1686 C ATOM 251 N ASN A 51 172.690 41.162 555.440 1.00 72.82 N ANISOU 251 N ASN A 51 10234 11231 6205 938 449 -1723 N ATOM 252 CA ASN A 51 172.625 40.306 556.620 1.00 69.79 C ANISOU 252 CA ASN A 51 9939 11053 5527 1043 490 -1640 C ATOM 253 C ASN A 51 174.045 39.896 556.986 1.00 68.44 C ANISOU 253 C ASN A 51 9749 11087 5169 1001 259 -1639 C ATOM 254 O ASN A 51 174.679 39.120 556.262 1.00 63.49 O ANISOU 254 O ASN A 51 8993 10479 4651 979 155 -1484 O ATOM 255 CB ASN A 51 171.745 39.084 556.364 1.00 68.07 C ANISOU 255 CB ASN A 51 9659 10816 5390 1144 646 -1378 C ATOM 256 CG ASN A 51 171.387 38.340 557.639 1.00 66.40 C ANISOU 256 CG ASN A 51 9559 10780 4889 1267 753 -1287 C ATOM 257 OD1 ASN A 51 172.048 38.489 558.667 1.00 70.22 O ANISOU 257 OD1 ASN A 51 10151 11450 5079 1281 662 -1381 O ATOM 258 ND2 ASN A 51 170.336 37.531 557.577 1.00 66.50 N ANISOU 258 ND2 ASN A 51 9544 10741 4982 1353 949 -1099 N ATOM 259 N ARG A 52 174.542 40.414 558.113 1.00 74.03 N ANISOU 259 N ARG A 52 10581 11955 5592 991 179 -1817 N ATOM 260 CA ARG A 52 175.894 40.077 558.542 1.00 78.87 C ANISOU 260 CA ARG A 52 11167 12791 6011 954 -56 -1824 C ATOM 261 C ARG A 52 176.006 38.615 558.953 1.00 76.25 C ANISOU 261 C ARG A 52 10811 12634 5526 1080 -51 -1554 C ATOM 262 O ARG A 52 177.098 38.039 558.892 1.00 77.65 O ANISOU 262 O ARG A 52 10901 12954 5649 1067 -237 -1469 O ATOM 263 CB ARG A 52 176.328 40.989 559.689 1.00 91.82 C ANISOU 263 CB ARG A 52 12949 14574 7364 911 -145 -2094 C ATOM 264 CG ARG A 52 175.955 42.449 559.491 1.00100.94 C ANISOU 264 CG ARG A 52 14170 15527 8655 813 -85 -2369 C ATOM 265 CD ARG A 52 176.949 43.383 560.166 1.00108.85 C ANISOU 265 CD ARG A 52 15238 16645 9475 692 -276 -2658 C ATOM 266 NE ARG A 52 178.012 43.796 559.254 1.00114.84 N ANISOU 266 NE ARG A 52 15849 17332 10451 535 -469 -2715 N ATOM 267 CZ ARG A 52 179.183 43.178 559.133 1.00120.18 C ANISOU 267 CZ ARG A 52 16400 18185 11076 495 -684 -2622 C ATOM 268 NH1 ARG A 52 179.454 42.110 559.872 1.00123.76 N ANISOU 268 NH1 ARG A 52 16861 18894 11267 608 -743 -2460 N ATOM 269 NH2 ARG A 52 180.086 43.630 558.273 1.00119.58 N ANISOU 269 NH2 ARG A 52 16187 18028 11219 349 -832 -2681 N ATOM 270 N HIS A 53 174.897 38.000 559.373 1.00 73.39 N ANISOU 270 N HIS A 53 10520 12258 5106 1205 166 -1411 N ATOM 271 CA HIS A 53 174.906 36.573 559.673 1.00 71.55 C ANISOU 271 CA HIS A 53 10263 12148 4774 1325 203 -1129 C ATOM 272 C HIS A 53 175.165 35.728 558.432 1.00 66.64 C ANISOU 272 C HIS A 53 9467 11405 4446 1304 170 -935 C ATOM 273 O HIS A 53 175.570 34.568 558.558 1.00 66.85 O ANISOU 273 O HIS A 53 9450 11533 4417 1381 138 -717 O ATOM 274 CB HIS A 53 173.582 36.159 560.319 1.00 74.37 C ANISOU 274 CB HIS A 53 10726 12486 5045 1448 470 -1021 C ATOM 275 CG HIS A 53 173.334 36.792 561.653 1.00 82.31 C ANISOU 275 CG HIS A 53 11916 13644 5713 1495 523 -1184 C ATOM 276 ND1 HIS A 53 173.859 36.289 562.824 1.00 85.33 N ANISOU 276 ND1 HIS A 53 12377 14230 5816 1540 448 -1102 N ATOM 277 CD2 HIS A 53 172.614 37.884 562.003 1.00 84.18 C ANISOU 277 CD2 HIS A 53 12263 13803 5919 1477 645 -1408 C ATOM 278 CE1 HIS A 53 173.474 37.045 563.837 1.00 86.73 C ANISOU 278 CE1 HIS A 53 12700 14429 5823 1522 516 -1268 C ATOM 279 NE2 HIS A 53 172.719 38.020 563.366 1.00 86.04 N ANISOU 279 NE2 HIS A 53 12636 14168 5886 1484 641 -1458 N ATOM 280 N LEU A 54 174.937 36.281 557.242 1.00 63.25 N ANISOU 280 N LEU A 54 8945 10762 4325 1206 182 -1005 N ATOM 281 CA LEU A 54 175.222 35.601 555.986 1.00 63.32 C ANISOU 281 CA LEU A 54 8794 10658 4606 1171 143 -858 C ATOM 282 C LEU A 54 176.551 36.027 555.380 1.00 63.02 C ANISOU 282 C LEU A 54 8654 10651 4639 1060 -86 -953 C ATOM 283 O LEU A 54 176.832 35.683 554.229 1.00 63.59 O ANISOU 283 O LEU A 54 8596 10618 4948 1013 -120 -872 O ATOM 284 CB LEU A 54 174.095 35.849 554.980 1.00 66.89 C ANISOU 284 CB LEU A 54 9196 10872 5349 1140 305 -849 C ATOM 285 CG LEU A 54 172.800 35.057 555.156 1.00 66.88 C ANISOU 285 CG LEU A 54 9217 10808 5386 1239 535 -685 C ATOM 286 CD1 LEU A 54 171.745 35.523 554.162 1.00 64.27 C ANISOU 286 CD1 LEU A 54 8821 10261 5337 1195 660 -714 C ATOM 287 CD2 LEU A 54 173.062 33.567 554.999 1.00 64.92 C ANISOU 287 CD2 LEU A 54 8903 10603 5162 1302 541 -440 C ATOM 288 N GLN A 55 177.367 36.772 556.119 1.00 65.13 N ANISOU 288 N GLN A 55 8976 11064 4708 1010 -241 -1129 N ATOM 289 CA GLN A 55 178.646 37.254 555.603 1.00 63.85 C ANISOU 289 CA GLN A 55 8706 10936 4617 890 -457 -1233 C ATOM 290 C GLN A 55 179.771 36.312 556.033 1.00 67.52 C ANISOU 290 C GLN A 55 9103 11627 4925 947 -620 -1098 C ATOM 291 O GLN A 55 180.669 36.658 556.801 1.00 72.14 O ANISOU 291 O GLN A 55 9702 12407 5300 918 -795 -1207 O ATOM 292 CB GLN A 55 178.896 38.688 556.061 1.00 63.46 C ANISOU 292 CB GLN A 55 8736 10892 4484 780 -536 -1525 C ATOM 293 CG GLN A 55 177.919 39.697 555.473 1.00 63.58 C ANISOU 293 CG GLN A 55 8795 10657 4705 722 -386 -1653 C ATOM 294 CD GLN A 55 178.220 41.120 555.901 1.00 70.06 C ANISOU 294 CD GLN A 55 9697 11453 5469 608 -456 -1948 C ATOM 295 OE1 GLN A 55 179.219 41.379 556.571 1.00 78.52 O ANISOU 295 OE1 GLN A 55 10778 12699 6356 550 -636 -2074 O ATOM 296 NE2 GLN A 55 177.354 42.051 555.516 1.00 70.75 N ANISOU 296 NE2 GLN A 55 9837 11320 5723 576 -316 -2062 N ATOM 297 N THR A 56 179.698 35.093 555.511 1.00 67.08 N ANISOU 297 N THR A 56 8966 11539 4983 1030 -560 -855 N ATOM 298 CA THR A 56 180.704 34.065 555.728 1.00 67.98 C ANISOU 298 CA THR A 56 8995 11825 5010 1105 -687 -684 C ATOM 299 C THR A 56 181.489 33.832 554.443 1.00 69.93 C ANISOU 299 C THR A 56 9063 11981 5525 1035 -769 -636 C ATOM 300 O THR A 56 181.118 34.302 553.364 1.00 67.44 O ANISOU 300 O THR A 56 8701 11467 5455 944 -704 -700 O ATOM 301 CB THR A 56 180.057 32.759 556.205 1.00 68.95 C ANISOU 301 CB THR A 56 9172 11974 5051 1270 -536 -430 C ATOM 302 OG1 THR A 56 179.159 32.272 555.198 1.00 65.48 O ANISOU 302 OG1 THR A 56 8693 11302 4884 1271 -355 -326 O ATOM 303 CG2 THR A 56 179.285 32.989 557.492 1.00 56.44 C ANISOU 303 CG2 THR A 56 7767 10493 3186 1344 -438 -468 C ATOM 304 N VAL A 57 182.592 33.091 554.574 1.00 74.56 N ANISOU 304 N VAL A 57 9548 12726 6057 1089 -910 -516 N ATOM 305 CA VAL A 57 183.454 32.823 553.425 1.00 77.16 C ANISOU 305 CA VAL A 57 9701 12995 6623 1035 -987 -469 C ATOM 306 C VAL A 57 182.701 32.030 552.362 1.00 75.83 C ANISOU 306 C VAL A 57 9501 12610 6700 1069 -805 -323 C ATOM 307 O VAL A 57 182.788 32.329 551.160 1.00 89.84 O ANISOU 307 O VAL A 57 11187 14238 8711 973 -792 -373 O ATOM 308 CB VAL A 57 184.733 32.098 553.884 1.00 82.95 C ANISOU 308 CB VAL A 57 10327 13950 7239 1113 -1160 -348 C ATOM 309 CG1 VAL A 57 185.702 33.088 554.506 1.00 87.49 C ANISOU 309 CG1 VAL A 57 10869 14719 7655 1016 -1383 -543 C ATOM 310 CG2 VAL A 57 184.392 31.008 554.888 1.00 82.52 C ANISOU 310 CG2 VAL A 57 10361 14013 6979 1297 -1095 -139 C ATOM 311 N ASN A 58 181.949 31.010 552.788 1.00 65.12 N ANISOU 311 N ASN A 58 8219 11234 5290 1200 -661 -144 N ATOM 312 CA ASN A 58 181.133 30.238 551.858 1.00 60.21 C ANISOU 312 CA ASN A 58 7575 10407 4896 1222 -483 -22 C ATOM 313 C ASN A 58 180.223 31.151 551.047 1.00 55.95 C ANISOU 313 C ASN A 58 7056 9681 4521 1105 -392 -170 C ATOM 314 O ASN A 58 180.119 31.017 549.824 1.00 54.04 O ANISOU 314 O ASN A 58 6730 9291 4510 1047 -351 -161 O ATOM 315 CB ASN A 58 180.307 29.198 552.617 1.00 60.03 C ANISOU 315 CB ASN A 58 7649 10384 4775 1362 -325 166 C ATOM 316 CG ASN A 58 181.165 28.164 553.314 1.00 67.63 C ANISOU 316 CG ASN A 58 8586 11507 5602 1499 -397 356 C ATOM 317 OD1 ASN A 58 182.325 27.960 552.959 1.00 74.15 O ANISOU 317 OD1 ASN A 58 9291 12407 6477 1500 -540 380 O ATOM 318 ND2 ASN A 58 180.594 27.497 554.310 1.00 70.76 N ANISOU 318 ND2 ASN A 58 9092 11962 5832 1623 -290 507 N ATOM 319 N ASN A 59 179.569 32.101 551.716 1.00 53.58 N ANISOU 319 N ASN A 59 6869 9391 4097 1075 -361 -307 N ATOM 320 CA ASN A 59 178.689 33.039 551.034 1.00 52.82 C ANISOU 320 CA ASN A 59 6793 9122 4152 981 -274 -440 C ATOM 321 C ASN A 59 179.446 34.136 550.295 1.00 55.80 C ANISOU 321 C ASN A 59 7097 9465 4639 843 -407 -606 C ATOM 322 O ASN A 59 178.833 34.861 549.507 1.00 58.34 O ANISOU 322 O ASN A 59 7413 9629 5123 767 -343 -688 O ATOM 323 CB ASN A 59 177.710 33.662 552.030 1.00 52.26 C ANISOU 323 CB ASN A 59 6869 9062 3924 1012 -173 -526 C ATOM 324 CG ASN A 59 176.806 32.630 552.678 1.00 52.56 C ANISOU 324 CG ASN A 59 6979 9111 3882 1139 -5 -353 C ATOM 325 OD1 ASN A 59 176.595 31.544 552.136 1.00 51.35 O ANISOU 325 OD1 ASN A 59 6763 8885 3862 1183 71 -183 O ATOM 326 ND2 ASN A 59 176.264 32.965 553.844 1.00 51.36 N ANISOU 326 ND2 ASN A 59 6959 9042 3512 1195 62 -400 N ATOM 327 N TYR A 60 180.749 34.292 550.538 1.00 57.08 N ANISOU 327 N TYR A 60 7196 9772 4720 810 -586 -651 N ATOM 328 CA TYR A 60 181.563 35.107 549.641 1.00 54.71 C ANISOU 328 CA TYR A 60 6792 9425 4571 675 -697 -767 C ATOM 329 C TYR A 60 181.743 34.400 548.304 1.00 51.72 C ANISOU 329 C TYR A 60 6290 8942 4418 667 -658 -645 C ATOM 330 O TYR A 60 181.539 34.995 547.235 1.00 52.40 O ANISOU 330 O TYR A 60 6335 8887 4689 575 -625 -702 O ATOM 331 CB TYR A 60 182.919 35.409 550.282 1.00 64.72 C ANISOU 331 CB TYR A 60 8004 10888 5698 636 -901 -845 C ATOM 332 CG TYR A 60 182.976 36.712 551.049 1.00 74.24 C ANISOU 332 CG TYR A 60 9297 12136 6776 546 -976 -1072 C ATOM 333 CD1 TYR A 60 182.265 36.879 552.230 1.00 78.31 C ANISOU 333 CD1 TYR A 60 9968 12716 7069 611 -922 -1127 C ATOM 334 CD2 TYR A 60 183.754 37.770 550.599 1.00 77.56 C ANISOU 334 CD2 TYR A 60 9645 12527 7298 392 -1090 -1235 C ATOM 335 CE1 TYR A 60 182.319 38.066 552.936 1.00 82.68 C ANISOU 335 CE1 TYR A 60 10612 13302 7502 527 -983 -1356 C ATOM 336 CE2 TYR A 60 183.815 38.962 551.298 1.00 81.84 C ANISOU 336 CE2 TYR A 60 10271 13087 7738 299 -1153 -1460 C ATOM 337 CZ TYR A 60 183.095 39.103 552.466 1.00 83.77 C ANISOU 337 CZ TYR A 60 10678 13395 7757 368 -1100 -1528 C ATOM 338 OH TYR A 60 183.152 40.287 553.166 1.00 89.02 O ANISOU 338 OH TYR A 60 11436 14070 8316 274 -1155 -1772 O ATOM 339 N PHE A 61 182.114 33.117 548.350 1.00 47.58 N ANISOU 339 N PHE A 61 5713 8486 3879 769 -654 -474 N ATOM 340 CA PHE A 61 182.197 32.331 547.122 1.00 50.05 C ANISOU 340 CA PHE A 61 5926 8693 4398 773 -594 -365 C ATOM 341 C PHE A 61 180.851 32.299 546.405 1.00 50.08 C ANISOU 341 C PHE A 61 5978 8511 4537 758 -428 -352 C ATOM 342 O PHE A 61 180.774 32.501 545.186 1.00 48.21 O ANISOU 342 O PHE A 61 5677 8162 4478 684 -402 -374 O ATOM 343 CB PHE A 61 182.674 30.913 547.442 1.00 53.70 C ANISOU 343 CB PHE A 61 6347 9237 4819 904 -590 -181 C ATOM 344 CG PHE A 61 184.002 30.861 548.145 1.00 53.00 C ANISOU 344 CG PHE A 61 6189 9351 4597 937 -763 -170 C ATOM 345 CD1 PHE A 61 184.961 31.834 547.920 1.00 53.35 C ANISOU 345 CD1 PHE A 61 6146 9465 4658 822 -912 -310 C ATOM 346 CD2 PHE A 61 184.289 29.837 549.032 1.00 55.99 C ANISOU 346 CD2 PHE A 61 6580 9854 4839 1082 -776 -12 C ATOM 347 CE1 PHE A 61 186.182 31.786 548.564 1.00 57.82 C ANISOU 347 CE1 PHE A 61 6628 10233 5109 844 -1083 -304 C ATOM 348 CE2 PHE A 61 185.509 29.783 549.681 1.00 60.67 C ANISOU 348 CE2 PHE A 61 7094 10653 5303 1121 -950 8 C ATOM 349 CZ PHE A 61 186.457 30.760 549.447 1.00 61.11 C ANISOU 349 CZ PHE A 61 7051 10790 5379 998 -1110 -144 C ATOM 350 N LEU A 62 179.772 32.061 547.157 1.00 50.70 N ANISOU 350 N LEU A 62 6167 8569 4528 828 -315 -314 N ATOM 351 CA LEU A 62 178.437 32.069 546.571 1.00 50.99 C ANISOU 351 CA LEU A 62 6236 8446 4693 814 -163 -304 C ATOM 352 C LEU A 62 178.053 33.453 546.069 1.00 52.94 C ANISOU 352 C LEU A 62 6495 8606 5015 710 -173 -457 C ATOM 353 O LEU A 62 177.234 33.574 545.153 1.00 48.82 O ANISOU 353 O LEU A 62 5949 7953 4647 674 -89 -452 O ATOM 354 CB LEU A 62 177.411 31.572 547.592 1.00 47.24 C ANISOU 354 CB LEU A 62 5866 7980 4105 911 -33 -230 C ATOM 355 CG LEU A 62 177.581 30.135 548.093 1.00 43.08 C ANISOU 355 CG LEU A 62 5341 7506 3523 1025 15 -47 C ATOM 356 CD1 LEU A 62 176.489 29.780 549.089 1.00 41.49 C ANISOU 356 CD1 LEU A 62 5248 7305 3213 1109 162 26 C ATOM 357 CD2 LEU A 62 177.596 29.153 546.932 1.00 41.14 C ANISOU 357 CD2 LEU A 62 5001 7145 3484 1017 68 47 C ATOM 358 N PHE A 63 178.619 34.507 546.660 1.00 55.26 N ANISOU 358 N PHE A 63 6824 8967 5204 660 -275 -592 N ATOM 359 CA PHE A 63 178.369 35.855 546.161 1.00 53.62 C ANISOU 359 CA PHE A 63 6628 8657 5089 560 -282 -733 C ATOM 360 C PHE A 63 178.992 36.043 544.785 1.00 51.63 C ANISOU 360 C PHE A 63 6260 8339 5018 470 -335 -729 C ATOM 361 O PHE A 63 178.354 36.579 543.870 1.00 44.80 O ANISOU 361 O PHE A 63 5381 7344 4297 422 -276 -745 O ATOM 362 CB PHE A 63 178.908 36.892 547.149 1.00 50.69 C ANISOU 362 CB PHE A 63 6324 8366 4570 517 -378 -894 C ATOM 363 CG PHE A 63 178.591 38.314 546.774 1.00 48.40 C ANISOU 363 CG PHE A 63 6066 7944 4380 422 -365 -1043 C ATOM 364 CD1 PHE A 63 179.423 39.026 545.923 1.00 48.56 C ANISOU 364 CD1 PHE A 63 6004 7916 4530 305 -455 -1105 C ATOM 365 CD2 PHE A 63 177.466 38.944 547.281 1.00 48.23 C ANISOU 365 CD2 PHE A 63 6153 7840 4331 454 -251 -1114 C ATOM 366 CE1 PHE A 63 179.135 40.333 545.579 1.00 48.38 C ANISOU 366 CE1 PHE A 63 6015 7753 4614 222 -432 -1226 C ATOM 367 CE2 PHE A 63 177.173 40.251 546.941 1.00 49.94 C ANISOU 367 CE2 PHE A 63 6400 7917 4657 380 -229 -1242 C ATOM 368 CZ PHE A 63 178.009 40.947 546.089 1.00 49.49 C ANISOU 368 CZ PHE A 63 6268 7802 4734 264 -320 -1295 C ATOM 369 N SER A 64 180.245 35.609 544.620 1.00 54.90 N ANISOU 369 N SER A 64 6585 8851 5421 453 -445 -698 N ATOM 370 CA SER A 64 180.868 35.670 543.301 1.00 48.51 C ANISOU 370 CA SER A 64 5663 7992 4775 377 -477 -680 C ATOM 371 C SER A 64 180.094 34.832 542.288 1.00 43.90 C ANISOU 371 C SER A 64 5051 7313 4316 411 -363 -571 C ATOM 372 O SER A 64 179.856 35.272 541.152 1.00 46.74 O ANISOU 372 O SER A 64 5372 7578 4808 345 -336 -582 O ATOM 373 CB SER A 64 182.322 35.205 543.390 1.00 46.86 C ANISOU 373 CB SER A 64 5353 7919 4534 374 -598 -653 C ATOM 374 OG SER A 64 182.926 35.158 542.110 1.00 53.24 O ANISOU 374 OG SER A 64 6049 8685 5494 312 -606 -625 O ATOM 375 N LEU A 65 179.680 33.626 542.689 1.00 39.32 N ANISOU 375 N LEU A 65 4491 6756 3691 511 -296 -465 N ATOM 376 CA LEU A 65 178.910 32.768 541.793 1.00 41.95 C ANISOU 376 CA LEU A 65 4799 6996 4144 533 -189 -379 C ATOM 377 C LEU A 65 177.601 33.435 541.380 1.00 47.13 C ANISOU 377 C LEU A 65 5496 7539 4873 500 -105 -417 C ATOM 378 O LEU A 65 177.210 33.387 540.206 1.00 46.05 O ANISOU 378 O LEU A 65 5308 7327 4860 456 -71 -402 O ATOM 379 CB LEU A 65 178.645 31.423 542.469 1.00 38.02 C ANISOU 379 CB LEU A 65 4328 6526 3591 642 -120 -262 C ATOM 380 CG LEU A 65 178.279 30.245 541.568 1.00 42.99 C ANISOU 380 CG LEU A 65 4910 7074 4349 661 -30 -174 C ATOM 381 CD1 LEU A 65 179.407 29.956 540.591 1.00 46.13 C ANISOU 381 CD1 LEU A 65 5210 7491 4826 628 -91 -171 C ATOM 382 CD2 LEU A 65 177.964 29.014 542.403 1.00 44.44 C ANISOU 382 CD2 LEU A 65 5136 7265 4485 768 53 -55 C ATOM 383 N ALA A 66 176.916 34.075 542.333 1.00 48.13 N ANISOU 383 N ALA A 66 5709 7660 4916 525 -73 -468 N ATOM 384 CA ALA A 66 175.678 34.779 542.021 1.00 47.60 C ANISOU 384 CA ALA A 66 5672 7488 4926 508 10 -501 C ATOM 385 C ALA A 66 175.928 35.981 541.121 1.00 52.96 C ANISOU 385 C ALA A 66 6318 8104 5701 417 -45 -576 C ATOM 386 O ALA A 66 175.059 36.344 540.321 1.00 53.65 O ANISOU 386 O ALA A 66 6385 8102 5897 398 9 -563 O ATOM 387 CB ALA A 66 174.979 35.216 543.308 1.00 42.94 C ANISOU 387 CB ALA A 66 5185 6910 4220 565 69 -547 C ATOM 388 N ACYS A 67 177.099 36.611 541.240 0.46 50.48 N ANISOU 388 N ACYS A 67 5993 7836 5351 359 -150 -646 N ATOM 389 N BCYS A 67 177.097 36.616 541.238 0.54 50.41 N ANISOU 389 N BCYS A 67 5985 7827 5342 359 -150 -646 N ATOM 390 CA ACYS A 67 177.440 37.711 540.344 0.46 52.47 C ANISOU 390 CA ACYS A 67 6210 8018 5708 265 -192 -700 C ATOM 391 CA BCYS A 67 177.431 37.713 540.335 0.54 52.42 C ANISOU 391 CA BCYS A 67 6204 8011 5703 265 -191 -699 C ATOM 392 C ACYS A 67 177.606 37.213 538.913 0.46 47.63 C ANISOU 392 C ACYS A 67 5505 7385 5206 232 -188 -619 C ATOM 393 C BCYS A 67 177.598 37.208 538.908 0.54 47.75 C ANISOU 393 C BCYS A 67 5520 7401 5222 233 -187 -619 C ATOM 394 O ACYS A 67 177.095 37.825 537.966 0.46 50.99 O ANISOU 394 O ACYS A 67 5912 7728 5732 194 -160 -608 O ATOM 395 O BCYS A 67 177.087 37.815 537.958 0.54 50.92 O ANISOU 395 O BCYS A 67 5904 7720 5724 195 -159 -607 O ATOM 396 CB ACYS A 67 178.714 38.403 540.832 0.46 53.60 C ANISOU 396 CB ACYS A 67 6348 8220 5796 198 -304 -794 C ATOM 397 CB BCYS A 67 178.701 38.420 540.808 0.54 53.55 C ANISOU 397 CB BCYS A 67 6342 8211 5794 197 -303 -794 C ATOM 398 SG ACYS A 67 179.173 39.886 539.906 0.46 58.48 S ANISOU 398 SG ACYS A 67 6936 8731 6553 72 -340 -864 S ATOM 399 SG BCYS A 67 178.488 39.435 542.284 0.54 59.00 S ANISOU 399 SG BCYS A 67 7154 8901 6364 201 -315 -941 S ATOM 400 N ALA A 68 178.315 36.093 538.739 1.00 50.45 N ANISOU 400 N ALA A 68 5806 7822 5542 253 -212 -560 N ATOM 401 CA ALA A 68 178.464 35.512 537.408 1.00 46.52 C ANISOU 401 CA ALA A 68 5231 7312 5135 228 -195 -498 C ATOM 402 C ALA A 68 177.113 35.102 536.830 1.00 45.45 C ANISOU 402 C ALA A 68 5104 7109 5057 255 -107 -451 C ATOM 403 O ALA A 68 176.826 35.358 535.651 1.00 39.26 O ANISOU 403 O ALA A 68 4280 6287 4350 210 -97 -434 O ATOM 404 CB ALA A 68 179.410 34.314 537.465 1.00 31.59 C ANISOU 404 CB ALA A 68 3285 5504 3214 265 -218 -450 C ATOM 405 N ASP A 69 176.263 34.476 537.650 1.00 42.77 N ANISOU 405 N ASP A 69 4810 6763 4678 325 -43 -427 N ATOM 406 CA ASP A 69 174.935 34.096 537.180 1.00 43.47 C ANISOU 406 CA ASP A 69 4890 6792 4834 342 39 -388 C ATOM 407 C ASP A 69 174.110 35.321 536.805 1.00 47.79 C ANISOU 407 C ASP A 69 5445 7273 5438 316 49 -415 C ATOM 408 O ASP A 69 173.318 35.280 535.856 1.00 52.51 O ANISOU 408 O ASP A 69 5998 7840 6115 299 74 -383 O ATOM 409 CB ASP A 69 174.217 33.271 538.245 1.00 43.79 C ANISOU 409 CB ASP A 69 4975 6835 4829 418 118 -351 C ATOM 410 CG ASP A 69 174.875 31.930 538.483 1.00 42.16 C ANISOU 410 CG ASP A 69 4755 6670 4592 457 127 -294 C ATOM 411 OD1 ASP A 69 175.461 31.381 537.528 1.00 38.22 O ANISOU 411 OD1 ASP A 69 4198 6176 4148 425 103 -281 O ATOM 412 OD2 ASP A 69 174.805 31.424 539.623 1.00 38.16 O ANISOU 412 OD2 ASP A 69 4300 6192 4007 526 165 -258 O ATOM 413 N LEU A 70 174.282 36.423 537.539 1.00 47.58 N ANISOU 413 N LEU A 70 5477 7227 5375 315 28 -477 N ATOM 414 CA LEU A 70 173.568 37.650 537.205 1.00 44.26 C ANISOU 414 CA LEU A 70 5069 6724 5026 301 47 -499 C ATOM 415 C LEU A 70 174.040 38.213 535.871 1.00 45.34 C ANISOU 415 C LEU A 70 5150 6839 5238 231 -4 -477 C ATOM 416 O LEU A 70 173.221 38.641 535.047 1.00 49.66 O ANISOU 416 O LEU A 70 5667 7337 5862 231 19 -434 O ATOM 417 CB LEU A 70 173.747 38.684 538.316 1.00 43.26 C ANISOU 417 CB LEU A 70 5026 6565 4845 310 44 -590 C ATOM 418 CG LEU A 70 173.099 40.047 538.065 1.00 45.36 C ANISOU 418 CG LEU A 70 5316 6718 5200 305 75 -620 C ATOM 419 CD1 LEU A 70 171.590 39.908 537.942 1.00 47.89 C ANISOU 419 CD1 LEU A 70 5617 6996 5584 375 168 -564 C ATOM 420 CD2 LEU A 70 173.466 41.036 539.161 1.00 42.31 C ANISOU 420 CD2 LEU A 70 5022 6294 4760 298 69 -739 C ATOM 421 N ILE A 71 175.356 38.219 535.638 1.00 49.10 N ANISOU 421 N ILE A 71 5606 7360 5691 174 -72 -496 N ATOM 422 CA ILE A 71 175.871 38.681 534.351 1.00 49.35 C ANISOU 422 CA ILE A 71 5585 7380 5785 107 -105 -462 C ATOM 423 C ILE A 71 175.332 37.813 533.222 1.00 49.30 C ANISOU 423 C ILE A 71 5520 7407 5803 113 -82 -391 C ATOM 424 O ILE A 71 174.982 38.314 532.146 1.00 47.23 O ANISOU 424 O ILE A 71 5230 7124 5591 88 -83 -345 O ATOM 425 CB ILE A 71 177.410 38.707 534.362 1.00 50.20 C ANISOU 425 CB ILE A 71 5664 7543 5867 46 -169 -494 C ATOM 426 CG1 ILE A 71 177.921 39.680 535.427 1.00 53.12 C ANISOU 426 CG1 ILE A 71 6085 7883 6215 19 -206 -584 C ATOM 427 CG2 ILE A 71 177.945 39.096 532.993 1.00 45.44 C ANISOU 427 CG2 ILE A 71 5003 6937 5324 -22 -182 -446 C ATOM 428 CD1 ILE A 71 179.428 39.769 535.499 1.00 54.03 C ANISOU 428 CD1 ILE A 71 6151 8061 6316 -50 -280 -621 C ATOM 429 N ILE A 72 175.245 36.499 533.450 1.00 51.80 N ANISOU 429 N ILE A 72 5822 7775 6083 148 -61 -382 N ATOM 430 CA ILE A 72 174.679 35.612 532.436 1.00 51.77 C ANISOU 430 CA ILE A 72 5768 7796 6106 144 -38 -341 C ATOM 431 C ILE A 72 173.216 35.956 532.181 1.00 53.64 C ANISOU 431 C ILE A 72 5996 7992 6392 166 -6 -313 C ATOM 432 O ILE A 72 172.763 35.998 531.030 1.00 54.90 O ANISOU 432 O ILE A 72 6109 8170 6581 140 -20 -279 O ATOM 433 CB ILE A 72 174.851 34.140 532.855 1.00 50.94 C ANISOU 433 CB ILE A 72 5657 7724 5973 177 -6 -342 C ATOM 434 CG1 ILE A 72 176.323 33.737 532.786 1.00 46.89 C ANISOU 434 CG1 ILE A 72 5125 7263 5428 162 -41 -353 C ATOM 435 CG2 ILE A 72 174.000 33.227 531.982 1.00 51.31 C ANISOU 435 CG2 ILE A 72 5662 7774 6060 167 29 -324 C ATOM 436 CD1 ILE A 72 176.943 33.941 531.426 1.00 44.05 C ANISOU 436 CD1 ILE A 72 4717 6934 5088 101 -64 -346 C ATOM 437 N GLY A 73 172.458 36.217 533.246 1.00 52.01 N ANISOU 437 N GLY A 73 5828 7742 6192 218 36 -326 N ATOM 438 CA GLY A 73 171.045 36.510 533.084 1.00 51.18 C ANISOU 438 CA GLY A 73 5696 7602 6148 250 75 -295 C ATOM 439 C GLY A 73 170.772 37.842 532.416 1.00 51.18 C ANISOU 439 C GLY A 73 5686 7559 6200 243 50 -265 C ATOM 440 O GLY A 73 169.733 38.013 531.770 1.00 52.93 O ANISOU 440 O GLY A 73 5853 7781 6478 261 55 -215 O ATOM 441 N VAL A 74 171.688 38.800 532.552 1.00 47.44 N ANISOU 441 N VAL A 74 5260 7048 5718 218 21 -290 N ATOM 442 CA VAL A 74 171.474 40.134 532.001 1.00 46.64 C ANISOU 442 CA VAL A 74 5161 6877 5682 215 12 -252 C ATOM 443 C VAL A 74 171.953 40.205 530.556 1.00 50.49 C ANISOU 443 C VAL A 74 5601 7412 6171 160 -37 -187 C ATOM 444 O VAL A 74 171.186 40.557 529.654 1.00 53.39 O ANISOU 444 O VAL A 74 5926 7785 6577 177 -45 -109 O ATOM 445 CB VAL A 74 172.170 41.207 532.859 1.00 47.17 C ANISOU 445 CB VAL A 74 5305 6858 5757 202 17 -319 C ATOM 446 CG1 VAL A 74 172.108 42.560 532.168 1.00 46.31 C ANISOU 446 CG1 VAL A 74 5202 6657 5737 190 16 -269 C ATOM 447 CG2 VAL A 74 171.526 41.283 534.234 1.00 50.31 C ANISOU 447 CG2 VAL A 74 5761 7214 6141 268 76 -384 C ATOM 448 N PHE A 75 173.222 39.869 530.324 1.00 50.74 N ANISOU 448 N PHE A 75 5635 7489 6154 99 -68 -211 N ATOM 449 CA PHE A 75 173.840 40.100 529.023 1.00 53.21 C ANISOU 449 CA PHE A 75 5914 7842 6460 44 -98 -152 C ATOM 450 C PHE A 75 173.706 38.908 528.080 1.00 58.34 C ANISOU 450 C PHE A 75 6511 8602 7054 31 -112 -135 C ATOM 451 O PHE A 75 173.210 39.057 526.959 1.00 64.60 O ANISOU 451 O PHE A 75 7268 9437 7838 26 -129 -68 O ATOM 452 CB PHE A 75 175.320 40.458 529.204 1.00 52.30 C ANISOU 452 CB PHE A 75 5815 7719 6337 -19 -114 -188 C ATOM 453 CG PHE A 75 175.545 41.795 529.852 1.00 50.31 C ANISOU 453 CG PHE A 75 5614 7352 6151 -34 -107 -213 C ATOM 454 CD1 PHE A 75 175.569 41.917 531.232 1.00 49.58 C ANISOU 454 CD1 PHE A 75 5571 7213 6052 -14 -102 -306 C ATOM 455 CD2 PHE A 75 175.733 42.929 529.080 1.00 47.32 C ANISOU 455 CD2 PHE A 75 5237 6905 5837 -70 -99 -143 C ATOM 456 CE1 PHE A 75 175.775 43.147 531.830 1.00 49.61 C ANISOU 456 CE1 PHE A 75 5629 7104 6116 -37 -93 -354 C ATOM 457 CE2 PHE A 75 175.941 44.161 529.672 1.00 50.04 C ANISOU 457 CE2 PHE A 75 5633 7119 6263 -92 -82 -177 C ATOM 458 CZ PHE A 75 175.961 44.270 531.049 1.00 50.54 C ANISOU 458 CZ PHE A 75 5747 7134 6321 -79 -80 -295 C ATOM 459 N SER A 76 174.142 37.724 528.515 1.00 58.50 N ANISOU 459 N SER A 76 6527 8668 7034 28 -103 -194 N ATOM 460 CA SER A 76 174.263 36.593 527.598 1.00 57.53 C ANISOU 460 CA SER A 76 6364 8631 6865 4 -106 -200 C ATOM 461 C SER A 76 172.902 36.128 527.092 1.00 53.59 C ANISOU 461 C SER A 76 5828 8161 6373 21 -108 -184 C ATOM 462 O SER A 76 172.718 35.916 525.886 1.00 52.70 O ANISOU 462 O SER A 76 5681 8121 6222 -9 -133 -162 O ATOM 463 CB SER A 76 175.007 35.445 528.282 1.00 55.08 C ANISOU 463 CB SER A 76 6059 8336 6531 12 -84 -261 C ATOM 464 OG SER A 76 176.362 35.787 528.516 1.00 57.63 O ANISOU 464 OG SER A 76 6387 8666 6843 -12 -97 -273 O ATOM 465 N MET A 77 171.936 35.964 527.999 1.00 54.62 N ANISOU 465 N MET A 77 5960 8245 6549 66 -83 -196 N ATOM 466 CA MET A 77 170.635 35.429 527.609 1.00 52.87 C ANISOU 466 CA MET A 77 5683 8054 6353 74 -84 -188 C ATOM 467 C MET A 77 169.948 36.327 526.586 1.00 48.02 C ANISOU 467 C MET A 77 5025 7477 5743 75 -133 -113 C ATOM 468 O MET A 77 169.552 35.867 525.510 1.00 51.14 O ANISOU 468 O MET A 77 5369 7961 6102 42 -173 -107 O ATOM 469 CB MET A 77 169.752 35.243 528.843 1.00 54.14 C ANISOU 469 CB MET A 77 5847 8154 6571 126 -31 -201 C ATOM 470 CG MET A 77 170.093 34.016 529.675 1.00 52.28 C ANISOU 470 CG MET A 77 5637 7902 6326 128 20 -253 C ATOM 471 SD MET A 77 168.952 33.783 531.053 0.94 51.58 S ANISOU 471 SD MET A 77 5552 7754 6294 190 101 -249 S ATOM 472 CE MET A 77 169.435 32.159 531.630 1.00 46.45 C ANISOU 472 CE MET A 77 4925 7095 5630 183 158 -281 C ATOM 473 N ASN A 78 169.813 37.618 526.899 1.00 44.83 N ANISOU 473 N ASN A 78 4644 7006 5383 116 -130 -57 N ATOM 474 CA ASN A 78 169.067 38.521 526.027 1.00 47.72 C ANISOU 474 CA ASN A 78 4967 7395 5770 141 -169 39 C ATOM 475 C ASN A 78 169.723 38.644 524.656 1.00 50.95 C ANISOU 475 C ASN A 78 5370 7892 6096 92 -217 87 C ATOM 476 O ASN A 78 169.047 38.563 523.623 1.00 53.08 O ANISOU 476 O ASN A 78 5582 8259 6327 90 -270 139 O ATOM 477 CB ASN A 78 168.932 39.893 526.689 1.00 49.66 C ANISOU 477 CB ASN A 78 5253 7520 6094 199 -137 86 C ATOM 478 CG ASN A 78 168.063 39.855 527.930 1.00 49.32 C ANISOU 478 CG ASN A 78 5210 7407 6122 260 -80 46 C ATOM 479 OD1 ASN A 78 167.153 39.034 528.038 1.00 46.30 O ANISOU 479 OD1 ASN A 78 4765 7072 5755 273 -73 31 O ATOM 480 ND2 ASN A 78 168.340 40.747 528.874 1.00 51.08 N ANISOU 480 ND2 ASN A 78 5503 7515 6390 294 -33 24 N ATOM 481 N LEU A 79 171.045 38.839 524.624 1.00 45.77 N ANISOU 481 N LEU A 79 4768 7215 5406 52 -200 71 N ATOM 482 CA LEU A 79 171.731 38.981 523.344 1.00 40.81 C ANISOU 482 CA LEU A 79 4138 6672 4696 7 -225 123 C ATOM 483 C LEU A 79 171.661 37.693 522.532 1.00 40.40 C ANISOU 483 C LEU A 79 4051 6747 4550 -34 -248 63 C ATOM 484 O LEU A 79 171.549 37.733 521.299 1.00 42.37 O ANISOU 484 O LEU A 79 4280 7106 4714 -54 -286 112 O ATOM 485 CB LEU A 79 173.183 39.405 523.564 1.00 44.35 C ANISOU 485 CB LEU A 79 4635 7071 5147 -33 -190 112 C ATOM 486 CG LEU A 79 173.378 40.837 524.069 1.00 47.62 C ANISOU 486 CG LEU A 79 5086 7356 5649 -17 -169 171 C ATOM 487 CD1 LEU A 79 174.850 41.216 524.092 1.00 46.25 C ANISOU 487 CD1 LEU A 79 4939 7154 5481 -80 -143 159 C ATOM 488 CD2 LEU A 79 172.585 41.818 523.220 1.00 49.21 C ANISOU 488 CD2 LEU A 79 5273 7555 5868 22 -188 308 C ATOM 489 N TYR A 80 171.714 36.539 523.201 1.00 39.34 N ANISOU 489 N TYR A 80 3916 6601 4430 -46 -222 -44 N ATOM 490 CA TYR A 80 171.572 35.282 522.473 1.00 44.19 C ANISOU 490 CA TYR A 80 4502 7309 4977 -88 -233 -118 C ATOM 491 C TYR A 80 170.166 35.134 521.902 1.00 45.15 C ANISOU 491 C TYR A 80 4558 7503 5092 -87 -292 -103 C ATOM 492 O TYR A 80 169.993 34.622 520.788 1.00 44.04 O ANISOU 492 O TYR A 80 4391 7480 4860 -130 -333 -131 O ATOM 493 CB TYR A 80 171.919 34.100 523.377 1.00 45.03 C ANISOU 493 CB TYR A 80 4625 7360 5124 -93 -180 -220 C ATOM 494 CG TYR A 80 172.158 32.818 522.613 1.00 48.24 C ANISOU 494 CG TYR A 80 5023 7834 5473 -142 -168 -311 C ATOM 495 CD1 TYR A 80 173.325 32.631 521.884 1.00 46.68 C ANISOU 495 CD1 TYR A 80 4850 7687 5201 -169 -145 -332 C ATOM 496 CD2 TYR A 80 171.217 31.798 522.614 1.00 49.19 C ANISOU 496 CD2 TYR A 80 5108 7960 5623 -164 -168 -383 C ATOM 497 CE1 TYR A 80 173.550 31.466 521.180 1.00 39.90 C ANISOU 497 CE1 TYR A 80 3990 6879 4291 -207 -119 -430 C ATOM 498 CE2 TYR A 80 171.434 30.627 521.912 1.00 49.58 C ANISOU 498 CE2 TYR A 80 5156 8051 5630 -216 -149 -485 C ATOM 499 CZ TYR A 80 172.604 30.467 521.198 1.00 46.00 C ANISOU 499 CZ TYR A 80 4738 7643 5095 -232 -123 -512 C ATOM 500 OH TYR A 80 172.828 29.305 520.496 1.00 51.24 O ANISOU 500 OH TYR A 80 5410 8339 5719 -277 -91 -627 O ATOM 501 N THR A 81 169.149 35.582 522.646 1.00 49.75 N ANISOU 501 N THR A 81 5108 8028 5768 -37 -296 -64 N ATOM 502 CA THR A 81 167.787 35.566 522.122 1.00 56.76 C ANISOU 502 CA THR A 81 5908 8993 6666 -29 -359 -33 C ATOM 503 C THR A 81 167.661 36.465 520.903 1.00 53.86 C ANISOU 503 C THR A 81 5520 8728 6216 -18 -431 77 C ATOM 504 O THR A 81 167.037 36.087 519.906 1.00 53.59 O ANISOU 504 O THR A 81 5425 8832 6106 -48 -506 73 O ATOM 505 CB THR A 81 166.791 36.005 523.194 1.00 68.99 C ANISOU 505 CB THR A 81 7420 10453 8342 36 -332 1 C ATOM 506 OG1 THR A 81 167.124 37.322 523.649 1.00 84.28 O ANISOU 506 OG1 THR A 81 9406 12298 10319 99 -306 88 O ATOM 507 CG2 THR A 81 166.817 35.055 524.360 1.00 69.31 C ANISOU 507 CG2 THR A 81 7480 10410 8446 27 -257 -92 C ATOM 508 N LEU A 82 168.231 37.669 520.971 1.00 49.92 N ANISOU 508 N LEU A 82 5072 8166 5731 25 -411 179 N ATOM 509 CA LEU A 82 168.232 38.556 519.813 1.00 54.47 C ANISOU 509 CA LEU A 82 5640 8826 6227 42 -463 310 C ATOM 510 C LEU A 82 168.882 37.878 518.614 1.00 55.81 C ANISOU 510 C LEU A 82 5828 9143 6236 -28 -490 269 C ATOM 511 O LEU A 82 168.343 37.901 517.499 1.00 51.13 O ANISOU 511 O LEU A 82 5192 8701 5535 -32 -567 321 O ATOM 512 CB LEU A 82 168.958 39.856 520.162 1.00 56.06 C ANISOU 512 CB LEU A 82 5908 8902 6489 79 -410 409 C ATOM 513 CG LEU A 82 168.931 40.967 519.116 1.00 60.50 C ANISOU 513 CG LEU A 82 6472 9512 7003 114 -442 581 C ATOM 514 CD1 LEU A 82 167.504 41.435 518.894 1.00 61.23 C ANISOU 514 CD1 LEU A 82 6482 9645 7138 195 -507 684 C ATOM 515 CD2 LEU A 82 169.824 42.123 519.542 1.00 59.07 C ANISOU 515 CD2 LEU A 82 6365 9175 6904 125 -369 652 C ATOM 516 N TYR A 83 170.040 37.250 518.838 1.00 57.77 N ANISOU 516 N TYR A 83 6134 9356 6459 -78 -426 173 N ATOM 517 CA TYR A 83 170.751 36.544 517.777 1.00 55.90 C ANISOU 517 CA TYR A 83 5919 9243 6076 -139 -425 115 C ATOM 518 C TYR A 83 169.865 35.483 517.131 1.00 52.80 C ANISOU 518 C TYR A 83 5473 8979 5608 -180 -490 17 C ATOM 519 O TYR A 83 169.666 35.476 515.910 1.00 48.94 O ANISOU 519 O TYR A 83 4972 8650 4972 -202 -551 40 O ATOM 520 CB TYR A 83 172.021 35.914 518.354 1.00 55.20 C ANISOU 520 CB TYR A 83 5882 9077 6014 -170 -337 16 C ATOM 521 CG TYR A 83 173.045 35.464 517.336 1.00 54.35 C ANISOU 521 CG TYR A 83 5807 9070 5775 -217 -301 -22 C ATOM 522 CD1 TYR A 83 172.958 35.850 516.005 1.00 51.87 C ANISOU 522 CD1 TYR A 83 5495 8901 5311 -228 -338 52 C ATOM 523 CD2 TYR A 83 174.104 34.647 517.712 1.00 56.37 C ANISOU 523 CD2 TYR A 83 6089 9279 6051 -240 -225 -124 C ATOM 524 CE1 TYR A 83 173.900 35.436 515.079 1.00 55.54 C ANISOU 524 CE1 TYR A 83 5995 9464 5646 -267 -289 13 C ATOM 525 CE2 TYR A 83 175.048 34.228 516.795 1.00 54.97 C ANISOU 525 CE2 TYR A 83 5935 9190 5763 -273 -175 -163 C ATOM 526 CZ TYR A 83 174.942 34.625 515.481 1.00 57.03 C ANISOU 526 CZ TYR A 83 6204 9595 5871 -290 -202 -99 C ATOM 527 OH TYR A 83 175.882 34.207 514.567 1.00 65.66 O ANISOU 527 OH TYR A 83 7325 10781 6841 -319 -136 -141 O ATOM 528 N THR A 84 169.317 34.578 517.945 1.00 52.95 N ANISOU 528 N THR A 84 5462 8934 5724 -195 -479 -95 N ATOM 529 CA THR A 84 168.541 33.465 517.405 1.00 58.79 C ANISOU 529 CA THR A 84 6147 9772 6417 -256 -530 -215 C ATOM 530 C THR A 84 167.265 33.946 516.721 1.00 57.93 C ANISOU 530 C THR A 84 5950 9795 6268 -243 -648 -139 C ATOM 531 O THR A 84 166.919 33.468 515.634 1.00 57.80 O ANISOU 531 O THR A 84 5903 9941 6119 -297 -724 -194 O ATOM 532 CB THR A 84 168.208 32.473 518.520 1.00 68.88 C ANISOU 532 CB THR A 84 7408 10928 7836 -274 -476 -326 C ATOM 533 OG1 THR A 84 169.422 31.971 519.093 1.00 75.49 O ANISOU 533 OG1 THR A 84 8322 11662 8699 -276 -377 -386 O ATOM 534 CG2 THR A 84 167.390 31.310 517.978 1.00 73.80 C ANISOU 534 CG2 THR A 84 7971 11630 8437 -353 -521 -460 C ATOM 535 N VAL A 85 166.558 34.894 517.338 1.00 56.85 N ANISOU 535 N VAL A 85 5766 9596 6239 -168 -666 -14 N ATOM 536 CA VAL A 85 165.266 35.324 516.810 1.00 55.15 C ANISOU 536 CA VAL A 85 5441 9499 6014 -139 -777 68 C ATOM 537 C VAL A 85 165.443 36.100 515.510 1.00 54.54 C ANISOU 537 C VAL A 85 5376 9580 5768 -117 -853 194 C ATOM 538 O VAL A 85 164.692 35.898 514.548 1.00 54.05 O ANISOU 538 O VAL A 85 5240 9703 5594 -140 -968 197 O ATOM 539 CB VAL A 85 164.507 36.147 517.868 1.00 50.88 C ANISOU 539 CB VAL A 85 4849 8834 5649 -48 -753 170 C ATOM 540 CG1 VAL A 85 163.289 36.815 517.253 1.00 53.26 C ANISOU 540 CG1 VAL A 85 5032 9260 5946 8 -865 296 C ATOM 541 CG2 VAL A 85 164.090 35.256 519.027 1.00 50.09 C ANISOU 541 CG2 VAL A 85 4720 8622 5691 -75 -688 50 C ATOM 542 N ILE A 86 166.432 36.994 515.453 1.00 53.98 N ANISOU 542 N ILE A 86 5394 9444 5671 -76 -791 303 N ATOM 543 CA ILE A 86 166.618 37.775 514.234 1.00 54.39 C ANISOU 543 CA ILE A 86 5464 9637 5563 -49 -845 449 C ATOM 544 C ILE A 86 167.200 36.913 513.118 1.00 56.33 C ANISOU 544 C ILE A 86 5751 10052 5599 -133 -864 342 C ATOM 545 O ILE A 86 166.853 37.089 511.943 1.00 61.88 O ANISOU 545 O ILE A 86 6433 10954 6126 -132 -956 409 O ATOM 546 CB ILE A 86 167.483 39.016 514.528 1.00 52.87 C ANISOU 546 CB ILE A 86 5351 9308 5431 11 -759 602 C ATOM 547 CG1 ILE A 86 166.651 40.071 515.261 1.00 58.72 C ANISOU 547 CG1 ILE A 86 6043 9927 6342 111 -765 737 C ATOM 548 CG2 ILE A 86 168.062 39.597 513.251 1.00 51.55 C ANISOU 548 CG2 ILE A 86 5231 9272 5083 16 -772 734 C ATOM 549 CD1 ILE A 86 167.284 41.446 515.285 1.00 62.78 C ANISOU 549 CD1 ILE A 86 6625 10322 6908 172 -699 912 C ATOM 550 N GLY A 87 168.059 35.954 513.457 1.00 54.51 N ANISOU 550 N GLY A 87 5581 9754 5378 -201 -778 175 N ATOM 551 CA GLY A 87 168.664 35.072 512.484 1.00 54.55 C ANISOU 551 CA GLY A 87 5633 9893 5201 -276 -770 49 C ATOM 552 C GLY A 87 170.102 35.401 512.143 1.00 57.32 C ANISOU 552 C GLY A 87 6080 10223 5475 -276 -663 92 C ATOM 553 O GLY A 87 170.791 34.563 511.551 1.00 64.44 O ANISOU 553 O GLY A 87 7030 11197 6259 -333 -616 -37 O ATOM 554 N TYR A 88 170.567 36.596 512.497 1.00 53.70 N ANISOU 554 N TYR A 88 5648 9665 5093 -216 -616 264 N ATOM 555 CA TYR A 88 171.946 37.003 512.280 1.00 49.94 C ANISOU 555 CA TYR A 88 5245 9151 4579 -223 -507 317 C ATOM 556 C TYR A 88 172.329 37.958 513.402 1.00 51.86 C ANISOU 556 C TYR A 88 5498 9187 5022 -180 -447 415 C ATOM 557 O TYR A 88 171.510 38.286 514.264 1.00 54.50 O ANISOU 557 O TYR A 88 5792 9418 5497 -138 -485 439 O ATOM 558 CB TYR A 88 172.125 37.640 510.898 1.00 49.12 C ANISOU 558 CB TYR A 88 5170 9224 4268 -212 -526 460 C ATOM 559 CG TYR A 88 171.269 38.865 510.661 1.00 50.91 C ANISOU 559 CG TYR A 88 5364 9475 4505 -136 -605 680 C ATOM 560 CD1 TYR A 88 169.972 38.748 510.179 1.00 55.80 C ANISOU 560 CD1 TYR A 88 5915 10242 5046 -112 -744 700 C ATOM 561 CD2 TYR A 88 171.760 40.140 510.911 1.00 52.25 C ANISOU 561 CD2 TYR A 88 5563 9517 4773 -88 -539 869 C ATOM 562 CE1 TYR A 88 169.187 39.865 509.958 1.00 58.08 C ANISOU 562 CE1 TYR A 88 6162 10553 5352 -25 -814 917 C ATOM 563 CE2 TYR A 88 170.983 41.262 510.695 1.00 53.70 C ANISOU 563 CE2 TYR A 88 5721 9702 4983 -6 -597 1079 C ATOM 564 CZ TYR A 88 169.698 41.119 510.219 1.00 59.19 C ANISOU 564 CZ TYR A 88 6343 10548 5596 34 -735 1109 C ATOM 565 OH TYR A 88 168.920 42.233 510.000 1.00 64.24 O ANISOU 565 OH TYR A 88 6947 11191 6272 132 -793 1334 O ATOM 566 N TRP A 89 173.588 38.401 513.396 1.00 52.10 N ANISOU 566 N TRP A 89 5577 9157 5063 -195 -348 462 N ATOM 567 CA TRP A 89 174.069 39.325 514.414 1.00 47.40 C ANISOU 567 CA TRP A 89 4993 8368 4648 -173 -292 535 C ATOM 568 C TRP A 89 173.828 40.755 513.948 1.00 47.86 C ANISOU 568 C TRP A 89 5062 8410 4713 -127 -301 754 C ATOM 569 O TRP A 89 174.516 41.217 513.025 1.00 47.94 O ANISOU 569 O TRP A 89 5103 8491 4620 -142 -254 863 O ATOM 570 CB TRP A 89 175.546 39.100 514.701 1.00 47.32 C ANISOU 570 CB TRP A 89 5010 8296 4671 -221 -187 473 C ATOM 571 CG TRP A 89 176.042 39.950 515.828 1.00 46.01 C ANISOU 571 CG TRP A 89 4850 7942 4690 -215 -145 512 C ATOM 572 CD1 TRP A 89 176.808 41.074 515.734 1.00 45.99 C ANISOU 572 CD1 TRP A 89 4867 7864 4743 -230 -86 637 C ATOM 573 CD2 TRP A 89 175.777 39.760 517.223 1.00 40.92 C ANISOU 573 CD2 TRP A 89 4196 7160 4193 -199 -159 420 C ATOM 574 NE1 TRP A 89 177.048 41.589 516.985 1.00 45.48 N ANISOU 574 NE1 TRP A 89 4802 7624 4853 -232 -71 609 N ATOM 575 CE2 TRP A 89 176.425 40.800 517.917 1.00 42.92 C ANISOU 575 CE2 TRP A 89 4465 7269 4575 -207 -116 479 C ATOM 576 CE3 TRP A 89 175.059 38.807 517.953 1.00 40.70 C ANISOU 576 CE3 TRP A 89 4147 7118 4199 -182 -197 295 C ATOM 577 CZ2 TRP A 89 176.378 40.915 519.305 1.00 43.36 C ANISOU 577 CZ2 TRP A 89 4524 7184 4768 -195 -118 406 C ATOM 578 CZ3 TRP A 89 175.014 38.922 519.331 1.00 43.43 C ANISOU 578 CZ3 TRP A 89 4496 7322 4682 -163 -188 244 C ATOM 579 CH2 TRP A 89 175.670 39.968 519.993 1.00 41.64 C ANISOU 579 CH2 TRP A 89 4292 6970 4558 -167 -153 294 C ATOM 580 N PRO A 90 172.878 41.485 514.540 1.00 44.89 N ANISOU 580 N PRO A 90 4660 7936 4458 -64 -349 833 N ATOM 581 CA PRO A 90 172.545 42.826 514.047 1.00 47.44 C ANISOU 581 CA PRO A 90 4993 8235 4799 -4 -355 1055 C ATOM 582 C PRO A 90 173.296 43.972 514.707 1.00 49.50 C ANISOU 582 C PRO A 90 5295 8284 5228 -5 -263 1139 C ATOM 583 O PRO A 90 173.265 45.090 514.172 1.00 50.72 O ANISOU 583 O PRO A 90 5471 8403 5398 34 -241 1334 O ATOM 584 CB PRO A 90 171.048 42.920 514.368 1.00 43.23 C ANISOU 584 CB PRO A 90 4396 7704 4325 73 -450 1080 C ATOM 585 CG PRO A 90 170.929 42.158 515.657 1.00 41.51 C ANISOU 585 CG PRO A 90 4162 7378 4231 50 -438 890 C ATOM 586 CD PRO A 90 171.972 41.060 515.621 1.00 41.87 C ANISOU 586 CD PRO A 90 4237 7472 4198 -37 -392 729 C ATOM 587 N LEU A 91 173.962 43.738 515.837 1.00 51.06 N ANISOU 587 N LEU A 91 5506 8343 5552 -49 -212 1001 N ATOM 588 CA LEU A 91 174.522 44.842 516.611 1.00 55.99 C ANISOU 588 CA LEU A 91 6163 8758 6351 -57 -142 1050 C ATOM 589 C LEU A 91 175.812 45.366 515.991 1.00 62.87 C ANISOU 589 C LEU A 91 7064 9620 7204 -124 -55 1134 C ATOM 590 O LEU A 91 175.923 46.556 515.678 1.00 73.49 O ANISOU 590 O LEU A 91 8436 10870 8619 -111 -9 1301 O ATOM 591 CB LEU A 91 174.748 44.401 518.059 1.00 51.18 C ANISOU 591 CB LEU A 91 5554 8028 5863 -81 -132 869 C ATOM 592 CG LEU A 91 173.463 43.976 518.771 1.00 47.57 C ANISOU 592 CG LEU A 91 5068 7560 5446 -14 -195 799 C ATOM 593 CD1 LEU A 91 173.706 43.728 520.251 1.00 46.30 C ANISOU 593 CD1 LEU A 91 4923 7272 5399 -28 -171 648 C ATOM 594 CD2 LEU A 91 172.376 45.020 518.566 1.00 38.51 C ANISOU 594 CD2 LEU A 91 3911 6355 4364 76 -217 954 C ATOM 595 N GLY A 92 176.800 44.495 515.813 1.00 59.75 N ANISOU 595 N GLY A 92 6660 9315 6729 -193 -21 1026 N ATOM 596 CA GLY A 92 178.044 44.889 515.198 1.00 58.97 C ANISOU 596 CA GLY A 92 6570 9225 6609 -260 72 1099 C ATOM 597 C GLY A 92 179.209 44.020 515.622 1.00 54.83 C ANISOU 597 C GLY A 92 6018 8724 6092 -330 116 939 C ATOM 598 O GLY A 92 179.093 43.168 516.508 1.00 57.21 O ANISOU 598 O GLY A 92 6301 9011 6425 -326 75 776 O ATOM 599 N PRO A 93 180.368 44.227 514.990 1.00 49.72 N ANISOU 599 N PRO A 93 5360 8113 5417 -392 208 997 N ATOM 600 CA PRO A 93 181.540 43.412 515.351 1.00 50.97 C ANISOU 600 CA PRO A 93 5473 8302 5592 -450 256 857 C ATOM 601 C PRO A 93 182.091 43.729 516.730 1.00 46.07 C ANISOU 601 C PRO A 93 4825 7518 5163 -490 249 766 C ATOM 602 O PRO A 93 182.496 42.809 517.454 1.00 45.90 O ANISOU 602 O PRO A 93 4768 7515 5158 -495 229 614 O ATOM 603 CB PRO A 93 182.545 43.744 514.239 1.00 45.42 C ANISOU 603 CB PRO A 93 4759 7680 4819 -500 368 974 C ATOM 604 CG PRO A 93 182.164 45.116 513.794 1.00 45.54 C ANISOU 604 CG PRO A 93 4814 7611 4878 -493 390 1179 C ATOM 605 CD PRO A 93 180.666 45.196 513.921 1.00 49.05 C ANISOU 605 CD PRO A 93 5298 8047 5291 -406 282 1203 C ATOM 606 N VAL A 94 182.115 45.007 517.116 1.00 43.66 N ANISOU 606 N VAL A 94 4537 7051 5002 -518 266 853 N ATOM 607 CA VAL A 94 182.639 45.387 518.427 1.00 45.44 C ANISOU 607 CA VAL A 94 4741 7126 5398 -568 252 750 C ATOM 608 C VAL A 94 181.789 44.782 519.536 1.00 49.24 C ANISOU 608 C VAL A 94 5241 7578 5890 -506 162 612 C ATOM 609 O VAL A 94 182.304 44.138 520.459 1.00 47.12 O ANISOU 609 O VAL A 94 4940 7312 5652 -523 135 472 O ATOM 610 CB VAL A 94 182.716 46.920 518.548 1.00 47.32 C ANISOU 610 CB VAL A 94 5008 7180 5792 -612 295 863 C ATOM 611 CG1 VAL A 94 183.178 47.321 519.939 1.00 40.38 C ANISOU 611 CG1 VAL A 94 4115 6151 5077 -670 269 729 C ATOM 612 CG2 VAL A 94 183.642 47.490 517.486 1.00 50.80 C ANISOU 612 CG2 VAL A 94 5424 7645 6233 -682 402 1010 C ATOM 613 N VAL A 95 180.470 44.982 519.462 1.00 49.21 N ANISOU 613 N VAL A 95 5285 7552 5862 -428 117 661 N ATOM 614 CA VAL A 95 179.570 44.442 520.478 1.00 41.67 C ANISOU 614 CA VAL A 95 4344 6568 4920 -368 48 546 C ATOM 615 C VAL A 95 179.619 42.920 520.487 1.00 45.44 C ANISOU 615 C VAL A 95 4792 7187 5287 -350 20 431 C ATOM 616 O VAL A 95 179.470 42.291 521.542 1.00 53.25 O ANISOU 616 O VAL A 95 5777 8151 6303 -329 -14 309 O ATOM 617 CB VAL A 95 178.140 44.970 520.251 1.00 42.23 C ANISOU 617 CB VAL A 95 4450 6601 4994 -285 15 640 C ATOM 618 CG1 VAL A 95 177.177 44.392 521.278 1.00 35.75 C ANISOU 618 CG1 VAL A 95 3635 5757 4192 -223 -40 526 C ATOM 619 CG2 VAL A 95 178.127 46.491 520.307 1.00 38.15 C ANISOU 619 CG2 VAL A 95 3970 5914 4613 -293 58 755 C ATOM 620 N CYS A 96 179.840 42.303 519.325 1.00 48.26 N ANISOU 620 N CYS A 96 5131 7688 5516 -356 44 467 N ATOM 621 CA CYS A 96 180.004 40.853 519.280 1.00 46.88 C ANISOU 621 CA CYS A 96 4932 7627 5252 -345 36 348 C ATOM 622 C CYS A 96 181.245 40.421 520.050 1.00 43.48 C ANISOU 622 C CYS A 96 4461 7175 4887 -383 65 252 C ATOM 623 O CYS A 96 181.197 39.478 520.851 1.00 48.07 O ANISOU 623 O CYS A 96 5031 7758 5476 -355 39 140 O ATOM 624 CB CYS A 96 180.079 40.374 517.830 1.00 44.80 C ANISOU 624 CB CYS A 96 4668 7520 4834 -350 68 394 C ATOM 625 SG CYS A 96 180.649 38.670 517.672 1.00 51.03 S ANISOU 625 SG CYS A 96 5429 8422 5537 -350 97 238 S ATOM 626 N ASP A 97 182.371 41.102 519.818 1.00 40.86 N ANISOU 626 N ASP A 97 4096 6823 4605 -447 120 305 N ATOM 627 CA ASP A 97 183.599 40.763 520.530 1.00 46.21 C ANISOU 627 CA ASP A 97 4711 7495 5352 -485 137 223 C ATOM 628 C ASP A 97 183.439 40.959 522.033 1.00 41.78 C ANISOU 628 C ASP A 97 4158 6827 4889 -477 71 139 C ATOM 629 O ASP A 97 183.858 40.106 522.826 1.00 42.20 O ANISOU 629 O ASP A 97 4178 6907 4948 -457 46 42 O ATOM 630 CB ASP A 97 184.763 41.600 519.999 1.00 55.27 C ANISOU 630 CB ASP A 97 5808 8635 6556 -568 209 304 C ATOM 631 CG ASP A 97 185.086 41.296 518.548 1.00 62.74 C ANISOU 631 CG ASP A 97 6744 9708 7386 -572 293 380 C ATOM 632 OD1 ASP A 97 184.770 40.178 518.089 1.00 63.52 O ANISOU 632 OD1 ASP A 97 6854 9914 7365 -520 295 323 O ATOM 633 OD2 ASP A 97 185.661 42.173 517.868 1.00 65.92 O ANISOU 633 OD2 ASP A 97 7131 10101 7814 -631 364 494 O ATOM 634 N LEU A 98 182.822 42.070 522.444 1.00 44.50 N ANISOU 634 N LEU A 98 4552 7051 5306 -486 46 178 N ATOM 635 CA LEU A 98 182.618 42.319 523.868 1.00 43.32 C ANISOU 635 CA LEU A 98 4423 6804 5231 -477 -9 87 C ATOM 636 C LEU A 98 181.693 41.277 524.487 1.00 47.23 C ANISOU 636 C LEU A 98 4948 7333 5665 -392 -51 13 C ATOM 637 O LEU A 98 181.892 40.864 525.636 1.00 53.33 O ANISOU 637 O LEU A 98 5717 8093 6452 -376 -88 -80 O ATOM 638 CB LEU A 98 182.058 43.725 524.080 1.00 43.01 C ANISOU 638 CB LEU A 98 4441 6616 5286 -495 -6 140 C ATOM 639 CG LEU A 98 182.928 44.894 523.615 1.00 46.38 C ANISOU 639 CG LEU A 98 4846 6966 5809 -590 45 215 C ATOM 640 CD1 LEU A 98 182.213 46.218 523.843 1.00 45.48 C ANISOU 640 CD1 LEU A 98 4802 6679 5800 -589 57 266 C ATOM 641 CD2 LEU A 98 184.277 44.880 524.320 1.00 44.44 C ANISOU 641 CD2 LEU A 98 4530 6726 5630 -677 33 122 C ATOM 642 N TRP A 99 180.676 40.837 523.741 1.00 34.96 N ANISOU 642 N TRP A 99 3419 5827 4037 -340 -48 57 N ATOM 643 CA TRP A 99 179.749 39.841 524.270 1.00 37.60 C ANISOU 643 CA TRP A 99 3772 6185 4330 -272 -77 -9 C ATOM 644 C TRP A 99 180.428 38.485 524.425 1.00 39.22 C ANISOU 644 C TRP A 99 3939 6472 4490 -261 -67 -85 C ATOM 645 O TRP A 99 180.272 37.815 525.454 1.00 38.86 O ANISOU 645 O TRP A 99 3901 6410 4454 -222 -87 -155 O ATOM 646 CB TRP A 99 178.521 39.730 523.366 1.00 46.83 C ANISOU 646 CB TRP A 99 4957 7394 5441 -235 -85 52 C ATOM 647 CG TRP A 99 177.555 38.676 523.809 1.00 48.97 C ANISOU 647 CG TRP A 99 5232 7688 5684 -181 -107 -15 C ATOM 648 CD1 TRP A 99 176.888 38.628 524.997 1.00 53.85 C ANISOU 648 CD1 TRP A 99 5873 8235 6354 -139 -122 -62 C ATOM 649 CD2 TRP A 99 177.144 37.519 523.070 1.00 50.15 C ANISOU 649 CD2 TRP A 99 5364 7936 5755 -172 -106 -46 C ATOM 650 NE1 TRP A 99 176.087 37.514 525.045 1.00 54.90 N ANISOU 650 NE1 TRP A 99 5996 8410 6455 -106 -125 -105 N ATOM 651 CE2 TRP A 99 176.226 36.815 523.875 1.00 50.82 C ANISOU 651 CE2 TRP A 99 5454 7992 5865 -130 -120 -104 C ATOM 652 CE3 TRP A 99 177.462 37.010 521.807 1.00 55.91 C ANISOU 652 CE3 TRP A 99 6077 8774 6393 -199 -88 -38 C ATOM 653 CZ2 TRP A 99 175.624 35.630 523.460 1.00 51.39 C ANISOU 653 CZ2 TRP A 99 5509 8124 5893 -125 -120 -157 C ATOM 654 CZ3 TRP A 99 176.863 35.832 521.397 1.00 57.15 C ANISOU 654 CZ3 TRP A 99 6225 8997 6490 -190 -93 -105 C ATOM 655 CH2 TRP A 99 175.955 35.155 522.220 1.00 54.00 C ANISOU 655 CH2 TRP A 99 5827 8554 6139 -159 -111 -165 C ATOM 656 N LEU A 100 181.187 38.064 523.410 1.00 40.22 N ANISOU 656 N LEU A 100 4027 6685 4569 -289 -26 -66 N ATOM 657 CA LEU A 100 181.915 36.801 523.506 1.00 41.86 C ANISOU 657 CA LEU A 100 4195 6958 4752 -269 -1 -135 C ATOM 658 C LEU A 100 182.917 36.831 524.654 1.00 43.39 C ANISOU 658 C LEU A 100 4349 7125 5013 -274 -22 -177 C ATOM 659 O LEU A 100 182.975 35.902 525.471 1.00 45.91 O ANISOU 659 O LEU A 100 4662 7449 5333 -222 -35 -234 O ATOM 660 CB LEU A 100 182.621 36.505 522.184 1.00 38.99 C ANISOU 660 CB LEU A 100 3799 6689 4328 -297 63 -109 C ATOM 661 CG LEU A 100 181.739 36.237 520.964 1.00 41.54 C ANISOU 661 CG LEU A 100 4158 7077 4547 -291 77 -86 C ATOM 662 CD1 LEU A 100 182.567 36.331 519.694 1.00 42.44 C ANISOU 662 CD1 LEU A 100 4249 7286 4592 -327 148 -42 C ATOM 663 CD2 LEU A 100 181.072 34.873 521.072 1.00 32.82 C ANISOU 663 CD2 LEU A 100 3070 5993 3406 -246 73 -179 C ATOM 664 N ALA A 101 183.712 37.903 524.735 1.00 42.03 N ANISOU 664 N ALA A 101 4144 6926 4898 -338 -26 -146 N ATOM 665 CA ALA A 101 184.712 38.008 525.793 1.00 46.82 C ANISOU 665 CA ALA A 101 4698 7528 5564 -357 -63 -193 C ATOM 666 C ALA A 101 184.062 38.011 527.171 1.00 46.29 C ANISOU 666 C ALA A 101 4684 7403 5502 -315 -128 -250 C ATOM 667 O ALA A 101 184.533 37.328 528.087 1.00 43.57 O ANISOU 667 O ALA A 101 4311 7094 5149 -277 -161 -299 O ATOM 668 CB ALA A 101 185.556 39.267 525.593 1.00 49.23 C ANISOU 668 CB ALA A 101 4960 7800 5946 -454 -57 -158 C ATOM 669 N LEU A 102 182.972 38.764 527.333 1.00 48.67 N ANISOU 669 N LEU A 102 5062 7620 5811 -312 -140 -238 N ATOM 670 CA LEU A 102 182.278 38.796 528.616 1.00 44.87 C ANISOU 670 CA LEU A 102 4638 7087 5325 -267 -181 -294 C ATOM 671 C LEU A 102 181.739 37.420 528.987 1.00 47.48 C ANISOU 671 C LEU A 102 4982 7460 5598 -182 -174 -315 C ATOM 672 O LEU A 102 181.886 36.972 530.132 1.00 54.91 O ANISOU 672 O LEU A 102 5932 8412 6519 -141 -204 -360 O ATOM 673 CB LEU A 102 181.146 39.822 528.571 1.00 43.28 C ANISOU 673 CB LEU A 102 4507 6784 5154 -266 -174 -267 C ATOM 674 CG LEU A 102 180.227 39.896 529.793 1.00 44.08 C ANISOU 674 CG LEU A 102 4675 6827 5247 -210 -193 -321 C ATOM 675 CD1 LEU A 102 181.018 40.242 531.041 1.00 43.92 C ANISOU 675 CD1 LEU A 102 4660 6797 5230 -236 -240 -406 C ATOM 676 CD2 LEU A 102 179.113 40.908 529.563 1.00 46.22 C ANISOU 676 CD2 LEU A 102 5000 6996 5565 -197 -170 -282 C ATOM 677 N ASP A 103 181.123 36.727 528.026 1.00 42.51 N ANISOU 677 N ASP A 103 4354 6858 4939 -159 -133 -284 N ATOM 678 CA ASP A 103 180.528 35.427 528.319 1.00 41.58 C ANISOU 678 CA ASP A 103 4251 6757 4790 -92 -114 -308 C ATOM 679 C ASP A 103 181.588 34.396 528.693 1.00 38.81 C ANISOU 679 C ASP A 103 3854 6461 4433 -60 -106 -331 C ATOM 680 O ASP A 103 181.404 33.625 529.643 1.00 34.85 O ANISOU 680 O ASP A 103 3370 5951 3921 2 -108 -348 O ATOM 681 CB ASP A 103 179.706 34.953 527.120 1.00 43.01 C ANISOU 681 CB ASP A 103 4437 6960 4945 -93 -79 -288 C ATOM 682 CG ASP A 103 178.936 33.681 527.408 1.00 49.73 C ANISOU 682 CG ASP A 103 5303 7804 5786 -42 -54 -321 C ATOM 683 OD1 ASP A 103 178.323 33.586 528.492 1.00 54.36 O ANISOU 683 OD1 ASP A 103 5923 8344 6389 -1 -61 -330 O ATOM 684 OD2 ASP A 103 178.930 32.783 526.543 1.00 52.61 O ANISOU 684 OD2 ASP A 103 5652 8207 6131 -46 -19 -341 O ATOM 685 N TYR A 104 182.710 34.370 527.969 1.00 40.44 N ANISOU 685 N TYR A 104 3994 6721 4649 -94 -89 -321 N ATOM 686 CA TYR A 104 183.726 33.361 528.252 1.00 41.18 C ANISOU 686 CA TYR A 104 4028 6867 4750 -49 -74 -334 C ATOM 687 C TYR A 104 184.521 33.689 529.511 1.00 42.91 C ANISOU 687 C TYR A 104 4214 7107 4983 -39 -142 -344 C ATOM 688 O TYR A 104 184.907 32.781 530.257 1.00 42.24 O ANISOU 688 O TYR A 104 4107 7052 4892 34 -150 -344 O ATOM 689 CB TYR A 104 184.651 33.197 527.046 1.00 44.42 C ANISOU 689 CB TYR A 104 4370 7337 5170 -80 -19 -321 C ATOM 690 CG TYR A 104 184.070 32.289 525.984 1.00 43.33 C ANISOU 690 CG TYR A 104 4261 7205 4997 -61 52 -337 C ATOM 691 CD1 TYR A 104 183.108 32.753 525.098 1.00 43.27 C ANISOU 691 CD1 TYR A 104 4303 7189 4947 -103 59 -327 C ATOM 692 CD2 TYR A 104 184.473 30.964 525.880 1.00 42.78 C ANISOU 692 CD2 TYR A 104 4168 7149 4939 2 110 -366 C ATOM 693 CE1 TYR A 104 182.569 31.925 524.132 1.00 44.91 C ANISOU 693 CE1 TYR A 104 4535 7419 5109 -96 109 -359 C ATOM 694 CE2 TYR A 104 183.940 30.128 524.917 1.00 41.87 C ANISOU 694 CE2 TYR A 104 4084 7031 4793 7 176 -406 C ATOM 695 CZ TYR A 104 182.990 30.615 524.044 1.00 44.18 C ANISOU 695 CZ TYR A 104 4426 7332 5028 -48 169 -410 C ATOM 696 OH TYR A 104 182.457 29.787 523.083 1.00 46.66 O ANISOU 696 OH TYR A 104 4770 7660 5299 -53 221 -467 O ATOM 697 N VAL A 105 184.769 34.975 529.771 1.00 43.60 N ANISOU 697 N VAL A 105 4298 7179 5090 -110 -193 -353 N ATOM 698 CA VAL A 105 185.426 35.358 531.018 1.00 43.48 C ANISOU 698 CA VAL A 105 4258 7191 5073 -115 -273 -387 C ATOM 699 C VAL A 105 184.545 35.006 532.208 1.00 47.28 C ANISOU 699 C VAL A 105 4823 7645 5496 -43 -298 -407 C ATOM 700 O VAL A 105 185.026 34.483 533.222 1.00 48.11 O ANISOU 700 O VAL A 105 4909 7808 5563 12 -344 -413 O ATOM 701 CB VAL A 105 185.788 36.855 531.002 1.00 44.06 C ANISOU 701 CB VAL A 105 4319 7229 5192 -223 -312 -411 C ATOM 702 CG1 VAL A 105 186.107 37.342 532.406 1.00 42.68 C ANISOU 702 CG1 VAL A 105 4153 7068 4997 -235 -404 -477 C ATOM 703 CG2 VAL A 105 186.970 37.103 530.082 1.00 44.22 C ANISOU 703 CG2 VAL A 105 4230 7298 5275 -293 -288 -384 C ATOM 704 N VAL A 106 183.240 35.273 532.102 1.00 47.47 N ANISOU 704 N VAL A 106 4935 7591 5509 -36 -265 -407 N ATOM 705 CA VAL A 106 182.331 34.949 533.197 1.00 42.72 C ANISOU 705 CA VAL A 106 4412 6964 4857 32 -268 -420 C ATOM 706 C VAL A 106 182.233 33.439 533.385 1.00 41.10 C ANISOU 706 C VAL A 106 4200 6786 4629 121 -226 -383 C ATOM 707 O VAL A 106 182.190 32.943 534.519 1.00 44.40 O ANISOU 707 O VAL A 106 4647 7227 4995 189 -242 -375 O ATOM 708 CB VAL A 106 180.953 35.592 532.953 1.00 48.53 C ANISOU 708 CB VAL A 106 5220 7611 5606 21 -232 -421 C ATOM 709 CG1 VAL A 106 179.897 34.961 533.847 1.00 47.16 C ANISOU 709 CG1 VAL A 106 5113 7414 5392 99 -199 -418 C ATOM 710 CG2 VAL A 106 181.025 37.090 533.205 1.00 50.68 C ANISOU 710 CG2 VAL A 106 5519 7832 5903 -45 -269 -462 C ATOM 711 N SER A 107 182.215 32.683 532.285 1.00 40.28 N ANISOU 711 N SER A 107 4064 6678 4562 124 -167 -359 N ATOM 712 CA SER A 107 182.162 31.226 532.389 1.00 43.17 C ANISOU 712 CA SER A 107 4427 7045 4933 203 -113 -331 C ATOM 713 C SER A 107 183.405 30.679 533.081 1.00 46.42 C ANISOU 713 C SER A 107 4778 7526 5334 262 -147 -306 C ATOM 714 O SER A 107 183.312 29.842 533.990 1.00 50.38 O ANISOU 714 O SER A 107 5303 8029 5810 348 -137 -269 O ATOM 715 CB SER A 107 182.004 30.611 530.998 1.00 43.10 C ANISOU 715 CB SER A 107 4396 7018 4964 181 -45 -337 C ATOM 716 OG SER A 107 180.884 31.157 530.329 1.00 48.19 O ANISOU 716 OG SER A 107 5081 7622 5607 129 -32 -351 O ATOM 717 N ASN A 108 184.585 31.147 532.662 1.00 44.28 N ANISOU 717 N ASN A 108 4421 7318 5086 218 -185 -315 N ATOM 718 CA ASN A 108 185.824 30.691 533.284 1.00 43.95 C ANISOU 718 CA ASN A 108 4294 7361 5044 274 -229 -287 C ATOM 719 C ASN A 108 185.871 31.072 534.758 1.00 42.94 C ANISOU 719 C ASN A 108 4196 7281 4840 302 -322 -290 C ATOM 720 O ASN A 108 186.268 30.261 535.606 1.00 45.68 O ANISOU 720 O ASN A 108 4525 7680 5152 398 -343 -239 O ATOM 721 CB ASN A 108 187.024 31.271 532.538 1.00 44.18 C ANISOU 721 CB ASN A 108 4211 7453 5124 205 -251 -300 C ATOM 722 CG ASN A 108 188.306 30.515 532.819 1.00 47.05 C ANISOU 722 CG ASN A 108 4457 7905 5516 278 -268 -260 C ATOM 723 OD1 ASN A 108 188.656 29.579 532.099 1.00 45.94 O ANISOU 723 OD1 ASN A 108 4272 7757 5427 332 -185 -233 O ATOM 724 ND2 ASN A 108 189.014 30.918 533.868 1.00 48.17 N ANISOU 724 ND2 ASN A 108 4544 8134 5625 282 -379 -259 N ATOM 725 N ALA A 109 185.463 32.302 535.083 1.00 41.64 N ANISOU 725 N ALA A 109 4080 7098 4643 223 -373 -347 N ATOM 726 CA ALA A 109 185.422 32.729 536.477 1.00 46.73 C ANISOU 726 CA ALA A 109 4770 7789 5197 242 -455 -374 C ATOM 727 C ALA A 109 184.487 31.846 537.293 1.00 46.58 C ANISOU 727 C ALA A 109 4843 7745 5111 347 -408 -327 C ATOM 728 O ALA A 109 184.757 31.558 538.466 1.00 47.41 O ANISOU 728 O ALA A 109 4963 7926 5123 415 -461 -304 O ATOM 729 CB ALA A 109 184.995 34.194 536.565 1.00 33.78 C ANISOU 729 CB ALA A 109 3183 6098 3552 140 -490 -458 C ATOM 730 N ARG A 110 183.381 31.408 536.688 1.00 42.41 N ANISOU 730 N ARG A 110 4372 7116 4624 359 -307 -307 N ATOM 731 CA ARG A 110 182.503 30.449 537.349 1.00 39.35 C ANISOU 731 CA ARG A 110 4057 6692 4201 451 -240 -250 C ATOM 732 C ARG A 110 183.232 29.141 537.626 1.00 38.66 C ANISOU 732 C ARG A 110 3924 6646 4119 553 -222 -165 C ATOM 733 O ARG A 110 183.195 28.618 538.748 1.00 44.07 O ANISOU 733 O ARG A 110 4647 7371 4727 642 -230 -105 O ATOM 734 CB ARG A 110 181.266 30.198 536.489 1.00 42.75 C ANISOU 734 CB ARG A 110 4529 7013 4701 425 -141 -253 C ATOM 735 CG ARG A 110 180.538 28.906 536.813 1.00 46.11 C ANISOU 735 CG ARG A 110 4995 7384 5141 506 -48 -187 C ATOM 736 CD ARG A 110 179.551 28.553 535.714 1.00 51.61 C ANISOU 736 CD ARG A 110 5696 7988 5926 460 34 -206 C ATOM 737 NE ARG A 110 178.751 29.710 535.325 1.00 48.52 N ANISOU 737 NE ARG A 110 5326 7574 5536 385 15 -259 N ATOM 738 CZ ARG A 110 177.672 30.122 535.980 1.00 50.60 C ANISOU 738 CZ ARG A 110 5647 7804 5775 394 39 -261 C ATOM 739 NH1 ARG A 110 177.261 29.470 537.059 1.00 49.83 N ANISOU 739 NH1 ARG A 110 5597 7698 5639 467 88 -213 N ATOM 740 NH2 ARG A 110 177.004 31.187 535.559 1.00 52.77 N ANISOU 740 NH2 ARG A 110 5930 8053 6067 338 25 -302 N ATOM 741 N VAL A 111 183.906 28.600 536.608 1.00 39.17 N ANISOU 741 N VAL A 111 3908 6702 4273 549 -192 -153 N ATOM 742 CA VAL A 111 184.586 27.315 536.763 1.00 47.55 C ANISOU 742 CA VAL A 111 4922 7779 5367 658 -156 -70 C ATOM 743 C VAL A 111 185.615 27.383 537.887 1.00 47.72 C ANISOU 743 C VAL A 111 4892 7933 5307 725 -262 -22 C ATOM 744 O VAL A 111 185.633 26.537 538.792 1.00 42.51 O ANISOU 744 O VAL A 111 4257 7294 4603 840 -251 71 O ATOM 745 CB VAL A 111 185.230 26.887 535.433 1.00 46.01 C ANISOU 745 CB VAL A 111 4645 7560 5279 637 -101 -87 C ATOM 746 CG1 VAL A 111 186.087 25.654 535.639 1.00 34.89 C ANISOU 746 CG1 VAL A 111 3173 6166 3917 761 -65 -3 C ATOM 747 CG2 VAL A 111 184.157 26.628 534.385 1.00 40.15 C ANISOU 747 CG2 VAL A 111 3959 6702 4593 582 -1 -133 C ATOM 748 N MET A 112 186.484 28.396 537.853 1.00 48.31 N ANISOU 748 N MET A 112 4891 8103 5363 651 -370 -81 N ATOM 749 CA MET A 112 187.491 28.515 538.900 1.00 49.50 C ANISOU 749 CA MET A 112 4975 8401 5432 700 -493 -51 C ATOM 750 C MET A 112 186.882 28.887 540.246 1.00 51.95 C ANISOU 750 C MET A 112 5391 8757 5591 724 -551 -57 C ATOM 751 O MET A 112 187.506 28.637 541.283 1.00 55.56 O ANISOU 751 O MET A 112 5820 9342 5948 802 -639 -4 O ATOM 752 CB MET A 112 188.560 29.531 538.496 1.00 42.06 C ANISOU 752 CB MET A 112 3914 7543 4523 593 -592 -127 C ATOM 753 CG MET A 112 189.408 29.070 537.320 1.00 38.92 C ANISOU 753 CG MET A 112 3392 7139 4258 593 -535 -103 C ATOM 754 SD MET A 112 190.988 29.926 537.207 0.49 38.81 S ANISOU 754 SD MET A 112 3192 7270 4285 510 -658 -144 S ATOM 755 CE MET A 112 190.439 31.625 537.174 1.00 38.21 C ANISOU 755 CE MET A 112 3190 7149 4179 330 -712 -275 C ATOM 756 N ASN A 113 185.681 29.469 540.257 1.00 53.15 N ANISOU 756 N ASN A 113 5659 8819 5718 665 -500 -118 N ATOM 757 CA ASN A 113 184.976 29.674 541.519 1.00 48.83 C ANISOU 757 CA ASN A 113 5225 8303 5027 706 -518 -118 C ATOM 758 C ASN A 113 184.560 28.340 542.128 1.00 49.27 C ANISOU 758 C ASN A 113 5331 8343 5047 847 -435 19 C ATOM 759 O ASN A 113 184.725 28.119 543.336 1.00 51.27 O ANISOU 759 O ASN A 113 5621 8701 5158 931 -486 77 O ATOM 760 CB ASN A 113 183.759 30.571 541.297 1.00 49.47 C ANISOU 760 CB ASN A 113 5404 8277 5116 621 -462 -208 C ATOM 761 CG ASN A 113 183.174 31.099 542.594 1.00 55.93 C ANISOU 761 CG ASN A 113 6331 9141 5779 643 -487 -245 C ATOM 762 OD1 ASN A 113 183.489 30.611 543.681 1.00 61.07 O ANISOU 762 OD1 ASN A 113 7004 9900 6298 733 -529 -185 O ATOM 763 ND2 ASN A 113 182.311 32.099 542.484 1.00 54.56 N ANISOU 763 ND2 ASN A 113 6228 8888 5614 568 -456 -340 N ATOM 764 N LEU A 114 184.018 27.438 541.306 1.00 49.75 N ANISOU 764 N LEU A 114 5397 8274 5233 872 -306 73 N ATOM 765 CA LEU A 114 183.694 26.103 541.796 1.00 51.81 C ANISOU 765 CA LEU A 114 5699 8492 5496 1000 -211 210 C ATOM 766 C LEU A 114 184.950 25.362 542.236 1.00 53.61 C ANISOU 766 C LEU A 114 5841 8825 5703 1114 -274 317 C ATOM 767 O LEU A 114 184.922 24.594 543.206 1.00 58.12 O ANISOU 767 O LEU A 114 6454 9433 6196 1239 -254 445 O ATOM 768 CB LEU A 114 182.951 25.316 540.717 1.00 52.54 C ANISOU 768 CB LEU A 114 5801 8414 5746 981 -67 218 C ATOM 769 CG LEU A 114 181.643 25.945 540.235 1.00 51.17 C ANISOU 769 CG LEU A 114 5693 8145 5604 878 -7 129 C ATOM 770 CD1 LEU A 114 181.016 25.110 539.131 1.00 55.43 C ANISOU 770 CD1 LEU A 114 6225 8541 6293 852 114 127 C ATOM 771 CD2 LEU A 114 180.678 26.117 541.395 1.00 44.18 C ANISOU 771 CD2 LEU A 114 4912 7266 4610 913 26 160 C ATOM 772 N LEU A 115 186.066 25.584 541.535 1.00 53.46 N ANISOU 772 N LEU A 115 5697 8862 5755 1081 -344 278 N ATOM 773 CA LEU A 115 187.335 25.014 541.975 1.00 55.39 C ANISOU 773 CA LEU A 115 5832 9229 5983 1191 -421 377 C ATOM 774 C LEU A 115 187.738 25.558 543.341 1.00 52.92 C ANISOU 774 C LEU A 115 5529 9103 5477 1224 -571 393 C ATOM 775 O LEU A 115 188.239 24.813 544.192 1.00 53.81 O ANISOU 775 O LEU A 115 5619 9312 5516 1365 -609 529 O ATOM 776 CB LEU A 115 188.426 25.298 540.942 1.00 55.25 C ANISOU 776 CB LEU A 115 5665 9244 6083 1133 -463 318 C ATOM 777 CG LEU A 115 188.325 24.534 539.621 1.00 52.64 C ANISOU 777 CG LEU A 115 5309 8764 5929 1133 -318 318 C ATOM 778 CD1 LEU A 115 189.327 25.068 538.608 1.00 49.32 C ANISOU 778 CD1 LEU A 115 4752 8392 5597 1054 -355 244 C ATOM 779 CD2 LEU A 115 188.540 23.048 539.856 1.00 54.73 C ANISOU 779 CD2 LEU A 115 5564 8974 6257 1301 -227 467 C ATOM 780 N ILE A 116 187.521 26.856 543.570 1.00 51.11 N ANISOU 780 N ILE A 116 5334 8926 5159 1099 -658 252 N ATOM 781 CA ILE A 116 187.863 27.454 544.858 1.00 53.94 C ANISOU 781 CA ILE A 116 5713 9464 5319 1112 -805 231 C ATOM 782 C ILE A 116 187.002 26.865 545.967 1.00 53.12 C ANISOU 782 C ILE A 116 5749 9366 5066 1226 -743 334 C ATOM 783 O ILE A 116 187.496 26.565 547.061 1.00 52.33 O ANISOU 783 O ILE A 116 5648 9429 4806 1329 -834 422 O ATOM 784 CB ILE A 116 187.731 28.987 544.791 1.00 52.92 C ANISOU 784 CB ILE A 116 5606 9349 5151 944 -886 39 C ATOM 785 CG1 ILE A 116 188.880 29.588 543.980 1.00 56.88 C ANISOU 785 CG1 ILE A 116 5947 9897 5769 842 -977 -39 C ATOM 786 CG2 ILE A 116 187.705 29.586 546.189 1.00 51.69 C ANISOU 786 CG2 ILE A 116 5525 9345 4769 951 -1001 -12 C ATOM 787 CD1 ILE A 116 188.846 31.099 543.902 1.00 59.28 C ANISOU 787 CD1 ILE A 116 6267 10198 6060 671 -1051 -220 C ATOM 788 N ILE A 117 185.704 26.688 545.707 1.00 50.45 N ANISOU 788 N ILE A 117 5530 8864 4776 1209 -588 332 N ATOM 789 CA ILE A 117 184.823 26.094 546.713 1.00 49.85 C ANISOU 789 CA ILE A 117 5584 8781 4577 1312 -501 440 C ATOM 790 C ILE A 117 185.260 24.667 547.022 1.00 47.68 C ANISOU 790 C ILE A 117 5278 8515 4322 1480 -453 650 C ATOM 791 O ILE A 117 185.371 24.267 548.189 1.00 49.72 O ANISOU 791 O ILE A 117 5586 8895 4410 1599 -484 772 O ATOM 792 CB ILE A 117 183.358 26.145 546.243 1.00 52.87 C ANISOU 792 CB ILE A 117 6067 8975 5045 1253 -336 399 C ATOM 793 CG1 ILE A 117 182.900 27.595 546.074 1.00 51.79 C ANISOU 793 CG1 ILE A 117 5968 8830 4878 1112 -381 211 C ATOM 794 CG2 ILE A 117 182.454 25.407 547.222 1.00 51.50 C ANISOU 794 CG2 ILE A 117 6013 8781 4773 1361 -218 531 C ATOM 795 CD1 ILE A 117 181.457 27.731 545.645 1.00 49.18 C ANISOU 795 CD1 ILE A 117 5719 8336 4631 1061 -233 173 C ATOM 796 N SER A 118 185.532 23.883 545.975 1.00 49.31 N ANISOU 796 N SER A 118 5406 8595 4736 1496 -373 697 N ATOM 797 CA SER A 118 185.899 22.484 546.165 1.00 52.07 C ANISOU 797 CA SER A 118 5729 8910 5145 1659 -300 895 C ATOM 798 C SER A 118 187.199 22.354 546.952 1.00 52.50 C ANISOU 798 C SER A 118 5688 9180 5081 1773 -459 994 C ATOM 799 O SER A 118 187.285 21.568 547.904 1.00 49.03 O ANISOU 799 O SER A 118 5286 8803 4541 1929 -448 1177 O ATOM 800 CB SER A 118 186.016 21.789 544.809 1.00 54.27 C ANISOU 800 CB SER A 118 5938 9010 5670 1640 -187 885 C ATOM 801 OG SER A 118 184.816 21.919 544.069 1.00 55.84 O ANISOU 801 OG SER A 118 6214 9033 5967 1530 -60 789 O ATOM 802 N PHE A 119 188.224 23.121 546.570 1.00 57.87 N ANISOU 802 N PHE A 119 6236 9981 5772 1699 -610 884 N ATOM 803 CA PHE A 119 189.498 23.047 547.281 1.00 67.73 C ANISOU 803 CA PHE A 119 7364 11454 6917 1796 -781 968 C ATOM 804 C PHE A 119 189.370 23.569 548.707 1.00 64.94 C ANISOU 804 C PHE A 119 7093 11298 6283 1822 -907 975 C ATOM 805 O PHE A 119 189.982 23.020 549.629 1.00 53.22 O ANISOU 805 O PHE A 119 5575 9979 4667 1971 -993 1133 O ATOM 806 CB PHE A 119 190.576 23.821 546.523 1.00 49.14 C ANISOU 806 CB PHE A 119 4838 9180 4653 1686 -907 834 C ATOM 807 CG PHE A 119 191.266 23.014 545.463 1.00 50.40 C ANISOU 807 CG PHE A 119 4865 9244 5040 1742 -827 898 C ATOM 808 CD1 PHE A 119 192.141 21.998 545.810 1.00 50.87 C ANISOU 808 CD1 PHE A 119 4821 9379 5129 1927 -847 1084 C ATOM 809 CD2 PHE A 119 191.049 23.275 544.119 1.00 48.59 C ANISOU 809 CD2 PHE A 119 4615 8856 4989 1620 -727 774 C ATOM 810 CE1 PHE A 119 192.782 21.252 544.839 1.00 50.86 C ANISOU 810 CE1 PHE A 119 4699 9282 5344 1988 -756 1134 C ATOM 811 CE2 PHE A 119 191.687 22.533 543.143 1.00 47.00 C ANISOU 811 CE2 PHE A 119 4301 8574 4983 1673 -642 819 C ATOM 812 CZ PHE A 119 192.555 21.521 543.504 1.00 48.92 C ANISOU 812 CZ PHE A 119 4443 8879 5266 1858 -650 992 C ATOM 813 N ASP A 120 188.583 24.629 548.905 1.00 57.81 N ANISOU 813 N ASP A 120 6300 10387 5279 1686 -918 808 N ATOM 814 CA ASP A 120 188.382 25.170 550.246 1.00 56.69 C ANISOU 814 CA ASP A 120 6257 10426 4858 1703 -1019 786 C ATOM 815 C ASP A 120 187.760 24.127 551.166 1.00 60.57 C ANISOU 815 C ASP A 120 6869 10916 5227 1875 -910 1000 C ATOM 816 O ASP A 120 188.223 23.919 552.296 1.00 63.50 O ANISOU 816 O ASP A 120 7251 11498 5379 1990 -1019 1109 O ATOM 817 CB ASP A 120 187.509 26.423 550.172 1.00 56.58 C ANISOU 817 CB ASP A 120 6350 10349 4798 1534 -1002 567 C ATOM 818 CG ASP A 120 187.117 26.945 551.539 1.00 66.74 C ANISOU 818 CG ASP A 120 7769 11794 5795 1554 -1066 528 C ATOM 819 OD1 ASP A 120 187.997 27.472 552.252 1.00 70.43 O ANISOU 819 OD1 ASP A 120 8183 12487 6091 1543 -1263 468 O ATOM 820 OD2 ASP A 120 185.927 26.831 551.898 1.00 69.24 O ANISOU 820 OD2 ASP A 120 8239 12015 6052 1577 -918 551 O ATOM 821 N ARG A 121 186.709 23.452 550.693 1.00 56.84 N ANISOU 821 N ARG A 121 6486 10213 4896 1893 -693 1068 N ATOM 822 CA ARG A 121 186.118 22.376 551.483 1.00 59.09 C ANISOU 822 CA ARG A 121 6878 10467 5105 2053 -562 1290 C ATOM 823 C ARG A 121 187.115 21.243 551.700 1.00 63.02 C ANISOU 823 C ARG A 121 7279 11031 5634 2236 -596 1519 C ATOM 824 O ARG A 121 187.167 20.648 552.785 1.00 65.85 O ANISOU 824 O ARG A 121 7696 11508 5816 2392 -601 1713 O ATOM 825 CB ARG A 121 184.853 21.861 550.798 1.00 57.63 C ANISOU 825 CB ARG A 121 6780 10006 5110 2014 -324 1303 C ATOM 826 CG ARG A 121 184.126 20.773 551.566 1.00 58.38 C ANISOU 826 CG ARG A 121 6989 10035 5157 2156 -158 1529 C ATOM 827 CD ARG A 121 183.628 21.281 552.906 1.00 64.73 C ANISOU 827 CD ARG A 121 7925 11008 5661 2188 -185 1544 C ATOM 828 NE ARG A 121 182.810 20.284 553.589 1.00 71.39 N ANISOU 828 NE ARG A 121 8885 11772 6470 2311 4 1763 N ATOM 829 CZ ARG A 121 182.207 20.483 554.756 1.00 71.47 C ANISOU 829 CZ ARG A 121 9028 11899 6229 2361 42 1819 C ATOM 830 NH1 ARG A 121 181.481 19.517 555.302 1.00 69.60 N ANISOU 830 NH1 ARG A 121 8887 11573 5986 2470 234 2037 N ATOM 831 NH2 ARG A 121 182.328 21.649 555.376 1.00 75.42 N ANISOU 831 NH2 ARG A 121 9568 12600 6487 2299 -103 1654 N ATOM 832 N TYR A 122 187.927 20.943 550.682 1.00 60.04 N ANISOU 832 N TYR A 122 6751 10585 5477 2228 -615 1507 N ATOM 833 CA TYR A 122 188.901 19.861 550.796 1.00 62.97 C ANISOU 833 CA TYR A 122 7014 11001 5913 2412 -634 1723 C ATOM 834 C TYR A 122 189.909 20.138 551.905 1.00 58.41 C ANISOU 834 C TYR A 122 6364 10742 5088 2507 -863 1797 C ATOM 835 O TYR A 122 190.202 19.263 552.728 1.00 60.72 O ANISOU 835 O TYR A 122 6665 11122 5283 2702 -866 2039 O ATOM 836 CB TYR A 122 189.609 19.649 549.458 1.00 58.49 C ANISOU 836 CB TYR A 122 6291 10314 5620 2372 -613 1658 C ATOM 837 CG TYR A 122 190.649 18.554 549.498 1.00 57.81 C ANISOU 837 CG TYR A 122 6078 10258 5630 2569 -621 1871 C ATOM 838 CD1 TYR A 122 190.275 17.217 549.518 1.00 61.04 C ANISOU 838 CD1 TYR A 122 6549 10480 6162 2723 -430 2080 C ATOM 839 CD2 TYR A 122 192.004 18.856 549.520 1.00 57.92 C ANISOU 839 CD2 TYR A 122 5901 10480 5624 2602 -813 1867 C ATOM 840 CE1 TYR A 122 191.222 16.212 549.559 1.00 66.22 C ANISOU 840 CE1 TYR A 122 7091 11148 6923 2918 -425 2283 C ATOM 841 CE2 TYR A 122 192.958 17.858 549.561 1.00 59.89 C ANISOU 841 CE2 TYR A 122 6020 10762 5973 2798 -816 2072 C ATOM 842 CZ TYR A 122 192.560 16.537 549.580 1.00 60.61 C ANISOU 842 CZ TYR A 122 6186 10655 6188 2963 -620 2282 C ATOM 843 OH TYR A 122 193.505 15.538 549.620 1.00 82.12 O ANISOU 843 OH TYR A 122 8783 13393 9027 3173 -611 2494 O ATOM 844 N PHE A 123 190.454 21.355 551.941 1.00 66.20 N ANISOU 844 N PHE A 123 7276 11905 5971 2370 -1058 1594 N ATOM 845 CA PHE A 123 191.400 21.709 552.991 1.00 68.11 C ANISOU 845 CA PHE A 123 7442 12469 5968 2433 -1298 1629 C ATOM 846 C PHE A 123 190.709 21.848 554.341 1.00 74.90 C ANISOU 846 C PHE A 123 8481 13467 6510 2488 -1314 1684 C ATOM 847 O PHE A 123 191.345 21.648 555.383 1.00 65.20 O ANISOU 847 O PHE A 123 7227 12478 5069 2606 -1458 1806 O ATOM 848 CB PHE A 123 192.129 23.000 552.623 1.00 65.02 C ANISOU 848 CB PHE A 123 6924 12206 5575 2245 -1491 1375 C ATOM 849 CG PHE A 123 192.934 22.899 551.359 1.00 63.38 C ANISOU 849 CG PHE A 123 6526 11901 5653 2198 -1483 1332 C ATOM 850 CD1 PHE A 123 193.677 21.763 551.085 1.00 63.63 C ANISOU 850 CD1 PHE A 123 6429 11916 5832 2373 -1446 1540 C ATOM 851 CD2 PHE A 123 192.937 23.935 550.439 1.00 60.05 C ANISOU 851 CD2 PHE A 123 6060 11399 5357 1986 -1497 1092 C ATOM 852 CE1 PHE A 123 194.416 21.665 549.921 1.00 60.79 C ANISOU 852 CE1 PHE A 123 5896 11471 5730 2335 -1421 1495 C ATOM 853 CE2 PHE A 123 193.673 23.842 549.273 1.00 56.51 C ANISOU 853 CE2 PHE A 123 5442 10871 5157 1945 -1475 1059 C ATOM 854 CZ PHE A 123 194.413 22.706 549.014 1.00 57.60 C ANISOU 854 CZ PHE A 123 5451 11002 5431 2118 -1435 1254 C ATOM 855 N CYS A 124 189.416 22.185 554.348 1.00 71.66 N ANISOU 855 N CYS A 124 8251 12903 6075 2398 -1159 1590 N ATOM 856 CA CYS A 124 188.683 22.217 555.609 1.00 70.36 C ANISOU 856 CA CYS A 124 8265 12853 5617 2465 -1133 1658 C ATOM 857 C CYS A 124 188.531 20.821 556.200 1.00 75.09 C ANISOU 857 C CYS A 124 8919 13429 6183 2693 -1008 1989 C ATOM 858 O CYS A 124 188.597 20.650 557.423 1.00 83.60 O ANISOU 858 O CYS A 124 10073 14696 6995 2800 -1065 2112 O ATOM 859 CB CYS A 124 187.314 22.865 555.412 1.00 72.94 C ANISOU 859 CB CYS A 124 8752 13003 5957 2324 -973 1490 C ATOM 860 SG CYS A 124 187.297 24.645 555.691 1.00 74.99 S ANISOU 860 SG CYS A 124 9047 13407 6037 2118 -1141 1147 S ATOM 861 N VAL A 125 188.329 19.808 555.355 1.00 74.40 N ANISOU 861 N VAL A 125 8800 13083 6386 2751 -823 2121 N ATOM 862 CA VAL A 125 188.123 18.456 555.866 1.00 73.98 C ANISOU 862 CA VAL A 125 8808 12961 6340 2962 -676 2440 C ATOM 863 C VAL A 125 189.415 17.656 556.005 1.00 75.59 C ANISOU 863 C VAL A 125 8856 13288 6577 3151 -791 2656 C ATOM 864 O VAL A 125 189.424 16.631 556.702 1.00 80.42 O ANISOU 864 O VAL A 125 9517 13887 7152 3329 -705 2923 O ATOM 865 CB VAL A 125 187.136 17.673 554.982 1.00 73.45 C ANISOU 865 CB VAL A 125 8806 12530 6573 2934 -394 2482 C ATOM 866 CG1 VAL A 125 185.842 18.456 554.804 1.00 67.82 C ANISOU 866 CG1 VAL A 125 8224 11701 5845 2755 -283 2278 C ATOM 867 CG2 VAL A 125 187.767 17.344 553.638 1.00 75.94 C ANISOU 867 CG2 VAL A 125 8965 12675 7214 2896 -377 2420 C ATOM 868 N THR A 126 190.505 18.087 555.369 1.00 73.12 N ANISOU 868 N THR A 126 8351 13064 6368 3095 -962 2533 N ATOM 869 CA THR A 126 191.757 17.343 555.440 1.00 75.81 C ANISOU 869 CA THR A 126 8527 13471 6805 3234 -1044 2694 C ATOM 870 C THR A 126 192.799 17.984 556.346 1.00 80.01 C ANISOU 870 C THR A 126 8975 14283 7142 3184 -1294 2607 C ATOM 871 O THR A 126 193.692 17.277 556.825 1.00 80.60 O ANISOU 871 O THR A 126 8961 14432 7232 3314 -1350 2777 O ATOM 872 CB THR A 126 192.359 17.169 554.039 1.00 74.40 C ANISOU 872 CB THR A 126 8169 13163 6936 3222 -1026 2642 C ATOM 873 OG1 THR A 126 192.474 18.446 553.400 1.00 75.29 O ANISOU 873 OG1 THR A 126 8222 13317 7069 2986 -1137 2327 O ATOM 874 CG2 THR A 126 191.484 16.255 553.196 1.00 72.87 C ANISOU 874 CG2 THR A 126 8069 12596 7023 3231 -731 2699 C ATOM 875 N LYS A 127 192.711 19.289 556.592 1.00 83.83 N ANISOU 875 N LYS A 127 9485 14911 7456 2999 -1442 2348 N ATOM 876 CA LYS A 127 193.661 20.006 557.443 1.00 84.80 C ANISOU 876 CA LYS A 127 9536 15286 7399 2925 -1684 2235 C ATOM 877 C LYS A 127 192.894 20.856 558.448 1.00 73.74 C ANISOU 877 C LYS A 127 8321 13994 5703 2826 -1722 2095 C ATOM 878 O LYS A 127 192.882 22.089 558.358 1.00 72.83 O ANISOU 878 O LYS A 127 8208 13945 5520 2636 -1836 1822 O ATOM 879 CB LYS A 127 194.603 20.867 556.600 1.00 81.27 C ANISOU 879 CB LYS A 127 8892 14892 7095 2767 -1844 2016 C ATOM 880 CG LYS A 127 195.378 20.091 555.546 1.00 71.68 C ANISOU 880 CG LYS A 127 7486 13567 6180 2857 -1794 2132 C ATOM 881 CD LYS A 127 196.226 21.013 554.688 1.00 70.65 C ANISOU 881 CD LYS A 127 7167 13482 6193 2684 -1930 1907 C ATOM 882 CE LYS A 127 196.993 20.230 553.635 1.00 82.40 C ANISOU 882 CE LYS A 127 8468 14860 7981 2778 -1860 2017 C ATOM 883 NZ LYS A 127 197.792 21.122 552.750 1.00 83.83 N ANISOU 883 NZ LYS A 127 8463 15076 8312 2605 -1966 1806 N ATOM 884 N PRO A 128 192.242 20.224 559.430 1.00 77.59 N ANISOU 884 N PRO A 128 8970 14490 6019 2950 -1615 2274 N ATOM 885 CA PRO A 128 191.458 21.003 560.403 1.00 77.70 C ANISOU 885 CA PRO A 128 9170 14601 5753 2865 -1625 2141 C ATOM 886 C PRO A 128 192.310 21.817 561.361 1.00 84.99 C ANISOU 886 C PRO A 128 10057 15778 6458 2779 -1875 1994 C ATOM 887 O PRO A 128 191.797 22.775 561.953 1.00 87.48 O ANISOU 887 O PRO A 128 10500 16166 6573 2656 -1915 1795 O ATOM 888 CB PRO A 128 190.656 19.929 561.156 1.00 77.51 C ANISOU 888 CB PRO A 128 9303 14511 5636 3042 -1428 2415 C ATOM 889 CG PRO A 128 190.799 18.669 560.340 1.00 76.74 C ANISOU 889 CG PRO A 128 9121 14223 5815 3194 -1281 2661 C ATOM 890 CD PRO A 128 192.129 18.778 559.674 1.00 76.82 C ANISOU 890 CD PRO A 128 8902 14296 5991 3171 -1456 2604 C ATOM 891 N LEU A 129 193.584 21.471 561.536 1.00 89.86 N ANISOU 891 N LEU A 129 10503 16526 7112 2839 -2039 2081 N ATOM 892 CA LEU A 129 194.442 22.145 562.502 1.00 96.68 C ANISOU 892 CA LEU A 129 11326 17640 7766 2768 -2285 1965 C ATOM 893 C LEU A 129 195.174 23.350 561.925 1.00 95.31 C ANISOU 893 C LEU A 129 11014 17519 7680 2554 -2470 1670 C ATOM 894 O LEU A 129 195.761 24.120 562.693 1.00 99.60 O ANISOU 894 O LEU A 129 11543 18252 8050 2454 -2671 1519 O ATOM 895 CB LEU A 129 195.469 21.160 563.072 1.00102.79 C ANISOU 895 CB LEU A 129 11982 18547 8526 2946 -2378 2219 C ATOM 896 CG LEU A 129 194.914 19.929 563.791 1.00 89.49 C ANISOU 896 CG LEU A 129 10424 16829 6749 3166 -2212 2535 C ATOM 897 CD1 LEU A 129 196.040 18.984 564.181 1.00 92.81 C ANISOU 897 CD1 LEU A 129 10699 17363 7200 3340 -2310 2781 C ATOM 898 CD2 LEU A 129 194.108 20.341 565.011 1.00 95.84 C ANISOU 898 CD2 LEU A 129 11446 17744 7223 3141 -2198 2487 C ATOM 899 N THR A 130 195.162 23.533 560.614 1.00 91.66 N ANISOU 899 N THR A 130 10451 16894 7481 2480 -2405 1586 N ATOM 900 CA THR A 130 195.926 24.618 560.007 1.00 93.86 C ANISOU 900 CA THR A 130 10581 17208 7873 2279 -2567 1329 C ATOM 901 C THR A 130 195.087 25.531 559.127 1.00 91.92 C ANISOU 901 C THR A 130 10404 16800 7722 2110 -2473 1100 C ATOM 902 O THR A 130 195.284 26.748 559.151 1.00 91.71 O ANISOU 902 O THR A 130 10369 16817 7659 1913 -2594 835 O ATOM 903 CB THR A 130 197.090 24.035 559.184 1.00100.04 C ANISOU 903 CB THR A 130 11115 17980 8916 2338 -2620 1441 C ATOM 904 OG1 THR A 130 197.879 23.172 560.014 1.00111.24 O ANISOU 904 OG1 THR A 130 12466 19548 10251 2506 -2708 1663 O ATOM 905 CG2 THR A 130 197.973 25.146 558.635 1.00101.41 C ANISOU 905 CG2 THR A 130 11122 18201 9208 2127 -2789 1191 C ATOM 906 N TYR A 131 194.152 24.981 558.358 1.00 89.46 N ANISOU 906 N TYR A 131 10161 16297 7534 2181 -2260 1196 N ATOM 907 CA TYR A 131 193.428 25.764 557.363 1.00 85.78 C ANISOU 907 CA TYR A 131 9730 15674 7190 2033 -2173 998 C ATOM 908 C TYR A 131 192.303 26.622 557.945 1.00 86.09 C ANISOU 908 C TYR A 131 9987 15696 7028 1936 -2119 824 C ATOM 909 O TYR A 131 192.156 27.777 557.525 1.00 68.18 O ANISOU 909 O TYR A 131 7724 13384 4798 1749 -2161 567 O ATOM 910 CB TYR A 131 192.872 24.848 556.271 1.00 78.37 C ANISOU 910 CB TYR A 131 8773 14541 6465 2145 -1974 1163 C ATOM 911 CG TYR A 131 192.306 25.605 555.093 1.00 75.57 C ANISOU 911 CG TYR A 131 8412 14040 6261 1996 -1908 972 C ATOM 912 CD1 TYR A 131 193.136 26.319 554.240 1.00 75.71 C ANISOU 912 CD1 TYR A 131 8253 14058 6453 1847 -2017 806 C ATOM 913 CD2 TYR A 131 190.942 25.608 554.835 1.00 61.94 C ANISOU 913 CD2 TYR A 131 6857 12153 4525 1992 -1721 958 C ATOM 914 CE1 TYR A 131 192.624 27.016 553.163 1.00 74.82 C ANISOU 914 CE1 TYR A 131 8144 13788 6498 1700 -1941 636 C ATOM 915 CE2 TYR A 131 190.423 26.300 553.760 1.00 74.67 C ANISOU 915 CE2 TYR A 131 8482 13538 6350 1817 -1619 767 C ATOM 916 CZ TYR A 131 191.268 27.003 552.927 1.00 71.36 C ANISOU 916 CZ TYR A 131 7897 13121 6094 1675 -1729 612 C ATOM 917 OH TYR A 131 190.753 27.695 551.856 1.00 76.12 O ANISOU 917 OH TYR A 131 8518 13507 6898 1509 -1626 443 O ATOM 918 N PRO A 132 191.478 26.120 558.877 1.00 85.60 N ANISOU 918 N PRO A 132 10107 15652 6766 2054 -2010 953 N ATOM 919 CA PRO A 132 190.381 26.963 559.389 1.00 85.52 C ANISOU 919 CA PRO A 132 10300 15614 6580 1962 -1937 778 C ATOM 920 C PRO A 132 190.832 28.286 559.989 1.00 87.75 C ANISOU 920 C PRO A 132 10598 16017 6727 1780 -2119 495 C ATOM 921 O PRO A 132 190.084 29.269 559.912 1.00 89.38 O ANISOU 921 O PRO A 132 10919 16146 6896 1651 -2068 275 O ATOM 922 CB PRO A 132 189.719 26.066 560.443 1.00 88.14 C ANISOU 922 CB PRO A 132 10790 15983 6715 2136 -1812 1002 C ATOM 923 CG PRO A 132 189.972 24.696 559.958 1.00 88.69 C ANISOU 923 CG PRO A 132 10766 15983 6950 2315 -1723 1298 C ATOM 924 CD PRO A 132 191.356 24.737 559.377 1.00 87.43 C ANISOU 924 CD PRO A 132 10375 15890 6956 2278 -1905 1272 C ATOM 925 N VAL A 133 192.026 28.350 560.582 1.00 88.49 N ANISOU 925 N VAL A 133 10580 16288 6754 1767 -2325 493 N ATOM 926 CA VAL A 133 192.479 29.614 561.156 1.00 90.41 C ANISOU 926 CA VAL A 133 10838 16636 6876 1584 -2501 218 C ATOM 927 C VAL A 133 192.911 30.581 560.059 1.00 90.27 C ANISOU 927 C VAL A 133 10689 16518 7091 1390 -2566 -6 C ATOM 928 O VAL A 133 192.841 31.803 560.236 1.00 94.68 O ANISOU 928 O VAL A 133 11307 17065 7603 1211 -2632 -274 O ATOM 929 CB VAL A 133 193.605 29.369 562.180 1.00 93.48 C ANISOU 929 CB VAL A 133 11151 17259 7109 1630 -2709 290 C ATOM 930 CG1 VAL A 133 194.878 28.900 561.490 1.00 93.27 C ANISOU 930 CG1 VAL A 133 10866 17270 7300 1653 -2829 394 C ATOM 931 CG2 VAL A 133 193.862 30.623 563.003 1.00 97.92 C ANISOU 931 CG2 VAL A 133 11782 17933 7488 1454 -2871 11 C ATOM 932 N LYS A 134 193.347 30.063 558.913 1.00 85.00 N ANISOU 932 N LYS A 134 9850 15767 6681 1420 -2537 100 N ATOM 933 CA LYS A 134 193.725 30.883 557.770 1.00 84.07 C ANISOU 933 CA LYS A 134 9601 15542 6802 1246 -2572 -82 C ATOM 934 C LYS A 134 192.539 31.228 556.881 1.00 79.51 C ANISOU 934 C LYS A 134 9124 14761 6325 1196 -2388 -167 C ATOM 935 O LYS A 134 192.723 31.879 555.848 1.00 77.37 O ANISOU 935 O LYS A 134 8755 14384 6257 1058 -2392 -303 O ATOM 936 CB LYS A 134 194.793 30.164 556.940 1.00 87.56 C ANISOU 936 CB LYS A 134 9801 15995 7472 1303 -2621 71 C ATOM 937 CG LYS A 134 195.962 29.640 557.753 1.00 95.40 C ANISOU 937 CG LYS A 134 10676 17187 8384 1387 -2790 197 C ATOM 938 CD LYS A 134 196.835 28.710 556.929 1.00100.89 C ANISOU 938 CD LYS A 134 11153 17869 9310 1493 -2784 391 C ATOM 939 CE LYS A 134 197.421 29.422 555.722 1.00102.63 C ANISOU 939 CE LYS A 134 11201 18000 9794 1324 -2813 236 C ATOM 940 NZ LYS A 134 198.317 28.528 554.937 1.00104.40 N ANISOU 940 NZ LYS A 134 11208 18215 10243 1430 -2798 417 N ATOM 941 N ARG A 135 191.332 30.814 557.264 1.00 77.50 N ANISOU 941 N ARG A 135 9059 14453 5936 1305 -2225 -84 N ATOM 942 CA ARG A 135 190.148 30.920 556.415 1.00 72.51 C ANISOU 942 CA ARG A 135 8516 13635 5399 1294 -2036 -117 C ATOM 943 C ARG A 135 189.352 32.155 556.830 1.00 73.47 C ANISOU 943 C ARG A 135 8806 13704 5404 1157 -2006 -374 C ATOM 944 O ARG A 135 188.347 32.079 557.538 1.00 78.31 O ANISOU 944 O ARG A 135 9606 14305 5843 1225 -1885 -357 O ATOM 945 CB ARG A 135 189.322 29.642 556.521 1.00 62.62 C ANISOU 945 CB ARG A 135 7353 12339 4100 1502 -1857 150 C ATOM 946 CG ARG A 135 188.188 29.513 555.528 1.00 59.50 C ANISOU 946 CG ARG A 135 7028 11677 3904 1484 -1629 160 C ATOM 947 CD ARG A 135 187.666 28.088 555.539 1.00 80.45 C ANISOU 947 CD ARG A 135 9725 14243 6601 1671 -1453 447 C ATOM 948 NE ARG A 135 186.616 27.859 554.553 1.00 73.54 N ANISOU 948 NE ARG A 135 8901 13066 5974 1633 -1222 459 N ATOM 949 CZ ARG A 135 185.328 27.732 554.850 1.00 71.51 C ANISOU 949 CZ ARG A 135 8807 12691 5671 1661 -1033 487 C ATOM 950 NH1 ARG A 135 184.927 27.811 556.112 1.00 69.43 N ANISOU 950 NH1 ARG A 135 8684 12580 5117 1734 -1032 510 N ATOM 951 NH2 ARG A 135 184.441 27.526 553.886 1.00 65.33 N ANISOU 951 NH2 ARG A 135 8043 11651 5130 1616 -846 491 N ATOM 952 N THR A 136 189.816 33.313 556.372 1.00 72.72 N ANISOU 952 N THR A 136 8641 13566 5421 963 -2105 -613 N ATOM 953 CA THR A 136 189.182 34.589 556.669 1.00 77.32 C ANISOU 953 CA THR A 136 9368 14075 5934 820 -2081 -878 C ATOM 954 C THR A 136 188.504 35.144 555.423 1.00 75.24 C ANISOU 954 C THR A 136 9099 13609 5879 729 -1963 -985 C ATOM 955 O THR A 136 188.631 34.606 554.320 1.00 76.63 O ANISOU 955 O THR A 136 9162 13643 6313 743 -1886 -854 O ATOM 956 CB THR A 136 190.202 35.599 557.206 1.00 88.90 C ANISOU 956 CB THR A 136 10781 15629 7370 653 -2281 -1086 C ATOM 957 OG1 THR A 136 189.522 36.789 557.623 1.00 92.93 O ANISOU 957 OG1 THR A 136 11456 16055 7797 532 -2241 -1340 O ATOM 958 CG2 THR A 136 191.208 35.956 556.125 1.00 88.90 C ANISOU 958 CG2 THR A 136 10563 15583 7634 522 -2381 -1140 C ATOM 959 N THR A 137 187.776 36.246 555.617 1.00 75.01 N ANISOU 959 N THR A 137 9212 13468 5820 620 -1900 -1207 N ATOM 960 CA THR A 137 187.089 36.881 554.497 1.00 70.92 C ANISOU 960 CA THR A 137 8711 12653 5582 516 -1743 -1285 C ATOM 961 C THR A 137 188.068 37.549 553.540 1.00 69.99 C ANISOU 961 C THR A 137 8419 12474 5699 349 -1852 -1388 C ATOM 962 O THR A 137 187.782 37.661 552.342 1.00 67.01 O ANISOU 962 O THR A 137 7994 11879 5589 298 -1736 -1353 O ATOM 963 CB THR A 137 186.072 37.901 555.010 1.00 69.51 C ANISOU 963 CB THR A 137 8727 12369 5313 460 -1642 -1488 C ATOM 964 OG1 THR A 137 186.745 38.906 555.778 1.00 72.44 O ANISOU 964 OG1 THR A 137 9116 12881 5528 336 -1819 -1737 O ATOM 965 CG2 THR A 137 185.027 37.218 555.881 1.00 67.93 C ANISOU 965 CG2 THR A 137 8695 12217 4900 627 -1500 -1372 C ATOM 966 N LYS A 138 189.220 37.996 554.044 1.00 67.34 N ANISOU 966 N LYS A 138 7982 12337 5268 259 -2074 -1512 N ATOM 967 CA LYS A 138 190.212 38.630 553.181 1.00 66.25 C ANISOU 967 CA LYS A 138 7662 12152 5359 92 -2175 -1604 C ATOM 968 C LYS A 138 190.822 37.624 552.213 1.00 65.16 C ANISOU 968 C LYS A 138 7338 12007 5411 164 -2160 -1376 C ATOM 969 O LYS A 138 190.943 37.897 551.012 1.00 62.85 O ANISOU 969 O LYS A 138 6957 11537 5385 76 -2086 -1372 O ATOM 970 CB LYS A 138 191.298 39.293 554.029 1.00 67.48 C ANISOU 970 CB LYS A 138 7764 12447 5430 -28 -2377 -1753 C ATOM 971 CG LYS A 138 192.588 39.574 553.276 1.00 67.10 C ANISOU 971 CG LYS A 138 7484 12403 5609 -162 -2496 -1768 C ATOM 972 CD LYS A 138 193.585 40.315 554.148 1.00 75.62 C ANISOU 972 CD LYS A 138 8527 13580 6626 -295 -2679 -1921 C ATOM 973 CE LYS A 138 194.980 40.276 553.548 1.00 80.66 C ANISOU 973 CE LYS A 138 8910 14273 7466 -383 -2803 -1873 C ATOM 974 NZ LYS A 138 195.513 38.886 553.489 1.00 80.14 N ANISOU 974 NZ LYS A 138 8711 14356 7382 -199 -2831 -1604 N ATOM 975 N MET A 139 191.215 36.451 552.720 1.00 65.61 N ANISOU 975 N MET A 139 7338 12258 5333 332 -2221 -1181 N ATOM 976 CA MET A 139 191.773 35.420 551.850 1.00 67.84 C ANISOU 976 CA MET A 139 7453 12526 5795 421 -2189 -964 C ATOM 977 C MET A 139 190.773 35.007 550.779 1.00 66.15 C ANISOU 977 C MET A 139 7311 12041 5782 464 -1948 -858 C ATOM 978 O MET A 139 191.134 34.850 549.606 1.00 62.16 O ANISOU 978 O MET A 139 6680 11422 5515 424 -1894 -804 O ATOM 979 CB MET A 139 192.199 34.207 552.677 1.00 69.03 C ANISOU 979 CB MET A 139 7564 12902 5762 619 -2268 -757 C ATOM 980 CG MET A 139 192.867 33.112 551.858 1.00 71.03 C ANISOU 980 CG MET A 139 7638 13151 6200 726 -2240 -538 C ATOM 981 SD MET A 139 192.864 31.507 552.678 0.38 70.55 S ANISOU 981 SD MET A 139 7601 13233 5972 1001 -2223 -239 S ATOM 982 CE MET A 139 191.110 31.147 552.704 1.00 69.31 C ANISOU 982 CE MET A 139 7704 12855 5776 1079 -1962 -179 C ATOM 983 N ALA A 140 189.507 34.829 551.166 1.00 65.08 N ANISOU 983 N ALA A 140 7371 11809 5548 541 -1801 -831 N ATOM 984 CA ALA A 140 188.473 34.498 550.192 1.00 57.81 C ANISOU 984 CA ALA A 140 6515 10641 4810 568 -1584 -749 C ATOM 985 C ALA A 140 188.318 35.604 549.157 1.00 54.25 C ANISOU 985 C ALA A 140 6045 9999 4570 395 -1537 -900 C ATOM 986 O ALA A 140 188.199 35.330 547.956 1.00 56.62 O ANISOU 986 O ALA A 140 6282 10149 5082 381 -1434 -825 O ATOM 987 CB ALA A 140 187.146 34.240 550.907 1.00 55.66 C ANISOU 987 CB ALA A 140 6443 10317 4388 666 -1444 -712 C ATOM 988 N GLY A 141 188.325 36.863 549.603 1.00 54.81 N ANISOU 988 N GLY A 141 6173 10070 4582 263 -1608 -1114 N ATOM 989 CA GLY A 141 188.195 37.970 548.670 1.00 58.06 C ANISOU 989 CA GLY A 141 6573 10289 5198 103 -1559 -1247 C ATOM 990 C GLY A 141 189.328 38.026 547.663 1.00 62.63 C ANISOU 990 C GLY A 141 6952 10871 5976 11 -1626 -1221 C ATOM 991 O GLY A 141 189.101 38.244 546.470 1.00 65.80 O ANISOU 991 O GLY A 141 7320 11096 6584 -45 -1519 -1193 O ATOM 992 N MET A 142 190.564 37.824 548.126 1.00 64.68 N ANISOU 992 N MET A 142 7067 11340 6169 -1 -1802 -1224 N ATOM 993 CA MET A 142 191.696 37.856 547.206 1.00 68.29 C ANISOU 993 CA MET A 142 7314 11814 6820 -84 -1859 -1195 C ATOM 994 C MET A 142 191.711 36.640 546.289 1.00 58.84 C ANISOU 994 C MET A 142 6040 10574 5744 44 -1747 -979 C ATOM 995 O MET A 142 192.168 36.737 545.145 1.00 53.55 O ANISOU 995 O MET A 142 5251 9820 5276 -24 -1698 -950 O ATOM 996 CB MET A 142 193.008 37.961 547.983 1.00 78.49 C ANISOU 996 CB MET A 142 8452 13357 8015 -129 -2084 -1256 C ATOM 997 CG MET A 142 193.120 39.222 548.827 1.00 84.97 C ANISOU 997 CG MET A 142 9336 14221 8730 -285 -2208 -1504 C ATOM 998 SD MET A 142 192.633 40.713 547.931 0.09 82.20 S ANISOU 998 SD MET A 142 9054 13575 8603 -493 -2092 -1682 S ATOM 999 CE MET A 142 193.846 40.748 546.613 1.00 79.23 C ANISOU 999 CE MET A 142 8418 13177 8509 -601 -2106 -1610 C ATOM 1000 N MET A 143 191.217 35.492 546.762 1.00 58.58 N ANISOU 1000 N MET A 143 6076 10591 5593 225 -1695 -828 N ATOM 1001 CA MET A 143 191.102 34.333 545.882 1.00 62.17 C ANISOU 1001 CA MET A 143 6480 10968 6172 341 -1567 -643 C ATOM 1002 C MET A 143 190.070 34.574 544.785 1.00 59.73 C ANISOU 1002 C MET A 143 6262 10418 6014 294 -1385 -652 C ATOM 1003 O MET A 143 190.305 34.235 543.618 1.00 58.18 O ANISOU 1003 O MET A 143 5978 10138 5989 284 -1306 -586 O ATOM 1004 CB MET A 143 190.743 33.087 546.691 1.00 65.02 C ANISOU 1004 CB MET A 143 6908 11413 6384 538 -1540 -481 C ATOM 1005 CG MET A 143 191.935 32.218 547.059 1.00 64.84 C ANISOU 1005 CG MET A 143 6723 11589 6326 648 -1659 -352 C ATOM 1006 SD MET A 143 191.438 30.694 547.884 0.80 71.11 S ANISOU 1006 SD MET A 143 7607 12436 6975 892 -1590 -124 S ATOM 1007 CE MET A 143 192.996 29.814 547.943 1.00 78.64 C ANISOU 1007 CE MET A 143 8323 13587 7968 1008 -1721 28 C ATOM 1008 N ILE A 144 188.925 35.162 545.139 1.00 58.12 N ANISOU 1008 N ILE A 144 6230 10111 5743 269 -1318 -733 N ATOM 1009 CA ILE A 144 187.899 35.461 544.142 1.00 59.31 C ANISOU 1009 CA ILE A 144 6458 10048 6029 227 -1161 -740 C ATOM 1010 C ILE A 144 188.418 36.483 543.137 1.00 61.02 C ANISOU 1010 C ILE A 144 6589 10181 6415 67 -1175 -830 C ATOM 1011 O ILE A 144 188.297 36.303 541.917 1.00 63.24 O ANISOU 1011 O ILE A 144 6827 10355 6848 50 -1078 -768 O ATOM 1012 CB ILE A 144 186.611 35.948 544.830 1.00 61.54 C ANISOU 1012 CB ILE A 144 6925 10251 6206 241 -1092 -810 C ATOM 1013 CG1 ILE A 144 185.966 34.809 545.623 1.00 61.86 C ANISOU 1013 CG1 ILE A 144 7051 10347 6108 404 -1033 -686 C ATOM 1014 CG2 ILE A 144 185.641 36.521 543.809 1.00 59.90 C ANISOU 1014 CG2 ILE A 144 6775 9837 6149 179 -959 -836 C ATOM 1015 CD1 ILE A 144 184.734 35.222 546.396 1.00 63.63 C ANISOU 1015 CD1 ILE A 144 7446 10514 6215 429 -954 -746 C ATOM 1016 N ALA A 145 189.006 37.573 543.639 1.00 62.44 N ANISOU 1016 N ALA A 145 6746 10411 6568 -55 -1292 -978 N ATOM 1017 CA ALA A 145 189.566 38.590 542.754 1.00 59.59 C ANISOU 1017 CA ALA A 145 6299 9964 6377 -217 -1300 -1057 C ATOM 1018 C ALA A 145 190.616 37.995 541.825 1.00 54.50 C ANISOU 1018 C ALA A 145 5469 9378 5861 -219 -1307 -954 C ATOM 1019 O ALA A 145 190.639 38.301 540.627 1.00 55.85 O ANISOU 1019 O ALA A 145 5597 9434 6191 -287 -1219 -928 O ATOM 1020 CB ALA A 145 190.161 39.731 543.578 1.00 64.68 C ANISOU 1020 CB ALA A 145 6935 10668 6973 -352 -1438 -1240 C ATOM 1021 N ALA A 146 191.487 37.134 542.357 1.00 49.88 N ANISOU 1021 N ALA A 146 4770 8975 5205 -136 -1404 -887 N ATOM 1022 CA ALA A 146 192.486 36.482 541.517 1.00 51.28 C ANISOU 1022 CA ALA A 146 4765 9212 5508 -115 -1396 -783 C ATOM 1023 C ALA A 146 191.828 35.598 540.467 1.00 50.05 C ANISOU 1023 C ALA A 146 4649 8934 5433 -21 -1225 -657 C ATOM 1024 O ALA A 146 192.315 35.499 539.334 1.00 51.77 O ANISOU 1024 O ALA A 146 4764 9113 5794 -56 -1157 -613 O ATOM 1025 CB ALA A 146 193.450 35.667 542.379 1.00 52.38 C ANISOU 1025 CB ALA A 146 4780 9571 5552 -15 -1530 -719 C ATOM 1026 N ALA A 147 190.716 34.950 540.821 1.00 46.74 N ANISOU 1026 N ALA A 147 4379 8457 4923 93 -1149 -603 N ATOM 1027 CA ALA A 147 189.997 34.135 539.848 1.00 47.25 C ANISOU 1027 CA ALA A 147 4488 8399 5064 166 -992 -506 C ATOM 1028 C ALA A 147 189.469 34.991 538.702 1.00 45.42 C ANISOU 1028 C ALA A 147 4295 8016 4947 49 -902 -557 C ATOM 1029 O ALA A 147 189.632 34.646 537.525 1.00 47.06 O ANISOU 1029 O ALA A 147 4443 8174 5262 44 -815 -503 O ATOM 1030 CB ALA A 147 188.857 33.380 540.533 1.00 42.22 C ANISOU 1030 CB ALA A 147 3999 7725 4317 289 -929 -450 C ATOM 1031 N TRP A 148 188.845 36.126 539.028 1.00 41.98 N ANISOU 1031 N TRP A 148 3959 7507 4486 -39 -918 -659 N ATOM 1032 CA TRP A 148 188.295 36.978 537.979 1.00 48.73 C ANISOU 1032 CA TRP A 148 4853 8213 5448 -135 -833 -686 C ATOM 1033 C TRP A 148 189.395 37.582 537.110 1.00 52.35 C ANISOU 1033 C TRP A 148 5173 8683 6033 -253 -851 -699 C ATOM 1034 O TRP A 148 189.283 37.591 535.878 1.00 48.26 O ANISOU 1034 O TRP A 148 4634 8093 5609 -280 -755 -645 O ATOM 1035 CB TRP A 148 187.422 38.071 538.595 1.00 52.09 C ANISOU 1035 CB TRP A 148 5413 8547 5833 -190 -840 -789 C ATOM 1036 CG TRP A 148 186.065 37.577 539.006 1.00 51.38 C ANISOU 1036 CG TRP A 148 5461 8400 5662 -85 -765 -758 C ATOM 1037 CD1 TRP A 148 185.710 37.066 540.221 1.00 54.33 C ANISOU 1037 CD1 TRP A 148 5906 8843 5892 8 -793 -762 C ATOM 1038 CD2 TRP A 148 184.883 37.541 538.196 1.00 48.60 C ANISOU 1038 CD2 TRP A 148 5181 7917 5366 -62 -646 -711 C ATOM 1039 NE1 TRP A 148 184.380 36.718 540.219 1.00 51.24 N ANISOU 1039 NE1 TRP A 148 5624 8364 5481 81 -687 -721 N ATOM 1040 CE2 TRP A 148 183.850 37.000 538.988 1.00 49.27 C ANISOU 1040 CE2 TRP A 148 5370 7994 5356 38 -603 -694 C ATOM 1041 CE3 TRP A 148 184.597 37.916 536.879 1.00 50.51 C ANISOU 1041 CE3 TRP A 148 5405 8062 5724 -117 -574 -677 C ATOM 1042 CZ2 TRP A 148 182.553 36.824 538.505 1.00 49.23 C ANISOU 1042 CZ2 TRP A 148 5435 7885 5386 77 -496 -652 C ATOM 1043 CZ3 TRP A 148 183.308 37.741 536.402 1.00 45.44 C ANISOU 1043 CZ3 TRP A 148 4839 7328 5099 -71 -481 -633 C ATOM 1044 CH2 TRP A 148 182.303 37.200 537.214 1.00 44.36 C ANISOU 1044 CH2 TRP A 148 4789 7183 4883 21 -445 -625 C ATOM 1045 N VAL A 149 190.467 38.083 537.730 1.00 60.04 N ANISOU 1045 N VAL A 149 6048 9756 7008 -328 -971 -767 N ATOM 1046 CA VAL A 149 191.563 38.670 536.960 1.00 60.58 C ANISOU 1046 CA VAL A 149 5967 9839 7211 -451 -982 -777 C ATOM 1047 C VAL A 149 192.208 37.622 536.060 1.00 55.66 C ANISOU 1047 C VAL A 149 5218 9281 6649 -380 -917 -661 C ATOM 1048 O VAL A 149 192.509 37.887 534.889 1.00 59.42 O ANISOU 1048 O VAL A 149 5634 9707 7236 -444 -832 -623 O ATOM 1049 CB VAL A 149 192.593 39.319 537.903 1.00 61.77 C ANISOU 1049 CB VAL A 149 6017 10102 7350 -549 -1138 -883 C ATOM 1050 CG1 VAL A 149 193.796 39.812 537.115 1.00 64.69 C ANISOU 1050 CG1 VAL A 149 6205 10498 7877 -676 -1142 -880 C ATOM 1051 CG2 VAL A 149 191.959 40.465 538.672 1.00 64.06 C ANISOU 1051 CG2 VAL A 149 6442 10302 7594 -636 -1182 -1024 C ATOM 1052 N LEU A 150 192.422 36.415 536.588 1.00 49.06 N ANISOU 1052 N LEU A 150 4348 8554 5740 -239 -946 -597 N ATOM 1053 CA LEU A 150 193.030 35.355 535.790 1.00 45.74 C ANISOU 1053 CA LEU A 150 3815 8182 5384 -155 -873 -495 C ATOM 1054 C LEU A 150 192.132 34.955 534.625 1.00 53.13 C ANISOU 1054 C LEU A 150 4845 8990 6352 -122 -715 -444 C ATOM 1055 O LEU A 150 192.617 34.713 533.514 1.00 55.82 O ANISOU 1055 O LEU A 150 5104 9328 6778 -134 -627 -401 O ATOM 1056 CB LEU A 150 193.337 34.146 536.673 1.00 45.22 C ANISOU 1056 CB LEU A 150 3710 8234 5238 3 -929 -428 C ATOM 1057 CG LEU A 150 194.749 33.566 536.569 1.00 52.73 C ANISOU 1057 CG LEU A 150 4448 9327 6259 48 -969 -369 C ATOM 1058 CD1 LEU A 150 194.924 32.403 537.533 1.00 54.08 C ANISOU 1058 CD1 LEU A 150 4601 9602 6343 222 -1026 -285 C ATOM 1059 CD2 LEU A 150 195.057 33.137 535.143 1.00 53.40 C ANISOU 1059 CD2 LEU A 150 4463 9358 6470 55 -820 -313 C ATOM 1060 N SER A 151 190.819 34.878 534.859 1.00 51.70 N ANISOU 1060 N SER A 151 4832 8713 6098 -81 -678 -453 N ATOM 1061 CA SER A 151 189.898 34.560 533.771 1.00 45.02 C ANISOU 1061 CA SER A 151 4069 7758 5277 -63 -547 -416 C ATOM 1062 C SER A 151 189.935 35.637 532.693 1.00 43.73 C ANISOU 1062 C SER A 151 3896 7530 5191 -191 -500 -434 C ATOM 1063 O SER A 151 190.005 35.335 531.493 1.00 42.73 O ANISOU 1063 O SER A 151 3741 7385 5108 -194 -403 -390 O ATOM 1064 CB SER A 151 188.480 34.392 534.317 1.00 45.08 C ANISOU 1064 CB SER A 151 4238 7685 5204 -7 -527 -425 C ATOM 1065 OG SER A 151 188.415 33.327 535.249 1.00 47.20 O ANISOU 1065 OG SER A 151 4524 8008 5403 116 -549 -386 O ATOM 1066 N PHE A 152 189.900 36.907 533.108 1.00 42.60 N ANISOU 1066 N PHE A 152 3778 7346 5062 -298 -561 -498 N ATOM 1067 CA PHE A 152 189.942 38.007 532.149 1.00 46.86 C ANISOU 1067 CA PHE A 152 4312 7806 5687 -419 -511 -498 C ATOM 1068 C PHE A 152 191.232 37.988 531.339 1.00 53.44 C ANISOU 1068 C PHE A 152 4985 8711 6609 -475 -480 -460 C ATOM 1069 O PHE A 152 191.217 38.243 530.129 1.00 53.43 O ANISOU 1069 O PHE A 152 4977 8670 6655 -518 -382 -409 O ATOM 1070 CB PHE A 152 189.784 39.341 532.879 1.00 48.24 C ANISOU 1070 CB PHE A 152 4539 7911 5881 -522 -581 -584 C ATOM 1071 CG PHE A 152 189.889 40.542 531.982 1.00 54.20 C ANISOU 1071 CG PHE A 152 5287 8564 6742 -649 -525 -573 C ATOM 1072 CD1 PHE A 152 191.103 41.187 531.800 1.00 58.55 C ANISOU 1072 CD1 PHE A 152 5707 9146 7395 -770 -549 -590 C ATOM 1073 CD2 PHE A 152 188.773 41.028 531.323 1.00 54.78 C ANISOU 1073 CD2 PHE A 152 5478 8514 6822 -645 -448 -534 C ATOM 1074 CE1 PHE A 152 191.202 42.291 530.975 1.00 61.55 C ANISOU 1074 CE1 PHE A 152 6085 9419 7883 -887 -483 -563 C ATOM 1075 CE2 PHE A 152 188.864 42.134 530.497 1.00 59.37 C ANISOU 1075 CE2 PHE A 152 6058 8998 7502 -750 -391 -500 C ATOM 1076 CZ PHE A 152 190.080 42.765 530.323 1.00 64.09 C ANISOU 1076 CZ PHE A 152 6536 9611 8202 -872 -402 -511 C ATOM 1077 N ILE A 153 192.361 37.693 531.987 1.00 57.61 N ANISOU 1077 N ILE A 153 5377 9356 7155 -472 -560 -479 N ATOM 1078 CA ILE A 153 193.633 37.659 531.273 1.00 52.01 C ANISOU 1078 CA ILE A 153 4492 8726 6544 -522 -525 -442 C ATOM 1079 C ILE A 153 193.680 36.475 530.315 1.00 49.50 C ANISOU 1079 C ILE A 153 4149 8439 6219 -413 -407 -364 C ATOM 1080 O ILE A 153 194.207 36.580 529.200 1.00 51.90 O ANISOU 1080 O ILE A 153 4379 8752 6588 -457 -307 -320 O ATOM 1081 CB ILE A 153 194.802 37.632 532.275 1.00 52.60 C ANISOU 1081 CB ILE A 153 4409 8933 6643 -540 -656 -482 C ATOM 1082 CG1 ILE A 153 194.908 38.975 533.002 1.00 56.31 C ANISOU 1082 CG1 ILE A 153 4890 9365 7141 -689 -760 -583 C ATOM 1083 CG2 ILE A 153 196.112 37.301 531.575 1.00 53.44 C ANISOU 1083 CG2 ILE A 153 4310 9140 6854 -553 -609 -427 C ATOM 1084 CD1 ILE A 153 196.065 39.056 533.976 1.00 60.53 C ANISOU 1084 CD1 ILE A 153 5259 10046 7693 -731 -910 -641 C ATOM 1085 N LEU A 154 193.118 35.335 530.720 1.00 46.17 N ANISOU 1085 N LEU A 154 3796 8028 5720 -273 -404 -348 N ATOM 1086 CA LEU A 154 193.177 34.148 529.874 1.00 45.81 C ANISOU 1086 CA LEU A 154 3732 7998 5677 -170 -289 -295 C ATOM 1087 C LEU A 154 192.280 34.282 528.649 1.00 51.73 C ANISOU 1087 C LEU A 154 4594 8659 6404 -199 -173 -283 C ATOM 1088 O LEU A 154 192.639 33.818 527.560 1.00 50.66 O ANISOU 1088 O LEU A 154 4414 8545 6288 -182 -63 -254 O ATOM 1089 CB LEU A 154 192.791 32.907 530.679 1.00 45.30 C ANISOU 1089 CB LEU A 154 3715 7946 5553 -20 -311 -279 C ATOM 1090 CG LEU A 154 193.843 32.340 531.631 1.00 47.08 C ANISOU 1090 CG LEU A 154 3803 8290 5796 59 -397 -253 C ATOM 1091 CD1 LEU A 154 193.255 31.194 532.438 1.00 53.46 C ANISOU 1091 CD1 LEU A 154 4693 9084 6536 208 -407 -218 C ATOM 1092 CD2 LEU A 154 195.068 31.879 530.861 1.00 42.97 C ANISOU 1092 CD2 LEU A 154 3108 7846 5373 84 -325 -212 C ATOM 1093 N TRP A 155 191.114 34.909 528.797 1.00 52.42 N ANISOU 1093 N TRP A 155 4822 8655 6442 -236 -197 -305 N ATOM 1094 CA TRP A 155 190.107 34.892 527.740 1.00 45.47 C ANISOU 1094 CA TRP A 155 4049 7706 5520 -240 -108 -287 C ATOM 1095 C TRP A 155 189.968 36.196 526.971 1.00 46.40 C ANISOU 1095 C TRP A 155 4190 7777 5665 -358 -82 -264 C ATOM 1096 O TRP A 155 189.793 36.161 525.751 1.00 45.67 O ANISOU 1096 O TRP A 155 4116 7687 5551 -371 9 -225 O ATOM 1097 CB TRP A 155 188.744 34.514 528.324 1.00 43.28 C ANISOU 1097 CB TRP A 155 3909 7360 5175 -177 -135 -308 C ATOM 1098 CG TRP A 155 188.568 33.047 528.504 1.00 39.82 C ANISOU 1098 CG TRP A 155 3482 6937 4710 -59 -99 -307 C ATOM 1099 CD1 TRP A 155 188.569 32.357 529.680 1.00 42.25 C ANISOU 1099 CD1 TRP A 155 3795 7257 5001 27 -151 -309 C ATOM 1100 CD2 TRP A 155 188.372 32.079 527.470 1.00 35.72 C ANISOU 1100 CD2 TRP A 155 2977 6414 4180 -14 5 -303 C ATOM 1101 NE1 TRP A 155 188.378 31.017 529.442 1.00 39.16 N ANISOU 1101 NE1 TRP A 155 3418 6853 4609 124 -78 -296 N ATOM 1102 CE2 TRP A 155 188.255 30.821 528.092 1.00 34.28 C ANISOU 1102 CE2 TRP A 155 2807 6221 3998 96 18 -305 C ATOM 1103 CE3 TRP A 155 188.281 32.154 526.077 1.00 33.66 C ANISOU 1103 CE3 TRP A 155 2726 6162 3903 -56 92 -300 C ATOM 1104 CZ2 TRP A 155 188.053 29.648 527.370 1.00 33.35 C ANISOU 1104 CZ2 TRP A 155 2709 6078 3883 156 117 -320 C ATOM 1105 CZ3 TRP A 155 188.081 30.990 525.363 1.00 34.76 C ANISOU 1105 CZ3 TRP A 155 2887 6299 4022 4 181 -325 C ATOM 1106 CH2 TRP A 155 187.967 29.755 526.010 1.00 34.39 C ANISOU 1106 CH2 TRP A 155 2851 6221 3994 105 195 -342 C ATOM 1107 N ALA A 156 190.034 37.345 527.641 1.00 47.10 N ANISOU 1107 N ALA A 156 4282 7819 5796 -441 -156 -287 N ATOM 1108 CA ALA A 156 189.707 38.607 526.975 1.00 46.93 C ANISOU 1108 CA ALA A 156 4305 7715 5809 -541 -123 -254 C ATOM 1109 C ALA A 156 190.642 38.945 525.818 1.00 52.11 C ANISOU 1109 C ALA A 156 4867 8413 6521 -613 -33 -190 C ATOM 1110 O ALA A 156 190.139 39.195 524.707 1.00 54.91 O ANISOU 1110 O ALA A 156 5280 8744 6842 -625 48 -125 O ATOM 1111 CB ALA A 156 189.664 39.736 528.011 1.00 45.38 C ANISOU 1111 CB ALA A 156 4133 7444 5665 -617 -212 -309 C ATOM 1112 N PRO A 157 191.974 38.975 525.981 1.00 52.53 N ANISOU 1112 N PRO A 157 4770 8538 6652 -661 -39 -197 N ATOM 1113 CA PRO A 157 192.819 39.416 524.855 1.00 49.49 C ANISOU 1113 CA PRO A 157 4293 8183 6328 -740 66 -127 C ATOM 1114 C PRO A 157 192.731 38.513 523.638 1.00 49.54 C ANISOU 1114 C PRO A 157 4312 8256 6255 -665 188 -77 C ATOM 1115 O PRO A 157 192.723 39.008 522.504 1.00 51.13 O ANISOU 1115 O PRO A 157 4531 8453 6442 -714 287 -2 O ATOM 1116 CB PRO A 157 194.233 39.418 525.458 1.00 50.18 C ANISOU 1116 CB PRO A 157 4195 8351 6518 -789 22 -158 C ATOM 1117 CG PRO A 157 194.030 39.436 526.937 1.00 51.11 C ANISOU 1117 CG PRO A 157 4334 8457 6629 -772 -128 -246 C ATOM 1118 CD PRO A 157 192.790 38.641 527.162 1.00 49.39 C ANISOU 1118 CD PRO A 157 4267 8208 6291 -648 -140 -260 C ATOM 1119 N ALA A 158 192.663 37.196 523.842 1.00 46.15 N ANISOU 1119 N ALA A 158 3880 7886 5769 -547 187 -116 N ATOM 1120 CA ALA A 158 192.577 36.278 522.712 1.00 44.21 C ANISOU 1120 CA ALA A 158 3654 7696 5448 -479 306 -97 C ATOM 1121 C ALA A 158 191.277 36.455 521.937 1.00 54.70 C ANISOU 1121 C ALA A 158 5139 8977 6669 -476 333 -75 C ATOM 1122 O ALA A 158 191.256 36.267 520.717 1.00 65.35 O ANISOU 1122 O ALA A 158 6509 10374 7947 -474 438 -40 O ATOM 1123 CB ALA A 158 192.716 34.835 523.194 1.00 42.61 C ANISOU 1123 CB ALA A 158 3426 7535 5230 -353 301 -151 C ATOM 1124 N ILE A 159 190.189 36.816 522.617 1.00 49.13 N ANISOU 1124 N ILE A 159 4538 8186 5942 -471 242 -95 N ATOM 1125 CA ILE A 159 188.917 36.990 521.924 1.00 43.33 C ANISOU 1125 CA ILE A 159 3932 7417 5116 -462 254 -68 C ATOM 1126 C ILE A 159 188.852 38.352 521.243 1.00 43.55 C ANISOU 1126 C ILE A 159 3981 7407 5160 -552 283 25 C ATOM 1127 O ILE A 159 188.321 38.479 520.133 1.00 39.34 O ANISOU 1127 O ILE A 159 3507 6902 4538 -551 339 86 O ATOM 1128 CB ILE A 159 187.747 36.787 522.905 1.00 42.79 C ANISOU 1128 CB ILE A 159 3954 7276 5029 -411 160 -117 C ATOM 1129 CG1 ILE A 159 187.721 35.344 523.416 1.00 42.41 C ANISOU 1129 CG1 ILE A 159 3898 7257 4958 -315 155 -187 C ATOM 1130 CG2 ILE A 159 186.418 37.139 522.248 1.00 37.93 C ANISOU 1130 CG2 ILE A 159 3447 6626 4339 -408 159 -80 C ATOM 1131 CD1 ILE A 159 186.691 35.103 524.500 1.00 45.99 C ANISOU 1131 CD1 ILE A 159 4427 7643 5402 -266 76 -228 C ATOM 1132 N LEU A 160 189.416 39.382 521.875 1.00 45.91 N ANISOU 1132 N LEU A 160 4230 7642 5572 -632 247 40 N ATOM 1133 CA LEU A 160 189.280 40.746 521.376 1.00 46.23 C ANISOU 1133 CA LEU A 160 4301 7606 5657 -718 277 133 C ATOM 1134 C LEU A 160 190.302 41.111 520.306 1.00 47.22 C ANISOU 1134 C LEU A 160 4347 7790 5806 -786 394 222 C ATOM 1135 O LEU A 160 189.983 41.894 519.403 1.00 50.95 O ANISOU 1135 O LEU A 160 4871 8234 6253 -822 457 333 O ATOM 1136 CB LEU A 160 189.393 41.742 522.534 1.00 46.23 C ANISOU 1136 CB LEU A 160 4294 7489 5781 -787 196 94 C ATOM 1137 CG LEU A 160 188.348 41.619 523.643 1.00 46.30 C ANISOU 1137 CG LEU A 160 4395 7429 5769 -726 94 14 C ATOM 1138 CD1 LEU A 160 188.599 42.649 524.737 1.00 47.55 C ANISOU 1138 CD1 LEU A 160 4547 7480 6041 -804 26 -43 C ATOM 1139 CD2 LEU A 160 186.946 41.763 523.072 1.00 46.30 C ANISOU 1139 CD2 LEU A 160 4514 7385 5691 -670 105 72 C ATOM 1140 N PHE A 161 191.521 40.574 520.374 1.00 48.20 N ANISOU 1140 N PHE A 161 4339 7997 5978 -799 433 189 N ATOM 1141 CA PHE A 161 192.618 41.077 519.556 1.00 47.53 C ANISOU 1141 CA PHE A 161 4152 7955 5952 -882 549 272 C ATOM 1142 C PHE A 161 193.266 40.032 518.657 1.00 44.76 C ANISOU 1142 C PHE A 161 3737 7746 5524 -824 664 276 C ATOM 1143 O PHE A 161 194.244 40.355 517.966 1.00 43.68 O ANISOU 1143 O PHE A 161 3503 7662 5434 -885 779 345 O ATOM 1144 CB PHE A 161 193.685 41.711 520.457 1.00 50.89 C ANISOU 1144 CB PHE A 161 4442 8342 6554 -983 504 238 C ATOM 1145 CG PHE A 161 193.142 42.758 521.388 1.00 51.08 C ANISOU 1145 CG PHE A 161 4530 8218 6660 -1048 400 208 C ATOM 1146 CD1 PHE A 161 192.255 43.719 520.928 1.00 48.98 C ANISOU 1146 CD1 PHE A 161 4388 7838 6385 -1076 425 292 C ATOM 1147 CD2 PHE A 161 193.502 42.771 522.725 1.00 56.78 C ANISOU 1147 CD2 PHE A 161 5192 8920 7463 -1073 278 96 C ATOM 1148 CE1 PHE A 161 191.746 44.679 521.781 1.00 51.81 C ANISOU 1148 CE1 PHE A 161 4810 8045 6829 -1127 346 256 C ATOM 1149 CE2 PHE A 161 192.996 43.729 523.585 1.00 56.18 C ANISOU 1149 CE2 PHE A 161 5186 8708 7452 -1133 192 48 C ATOM 1150 CZ PHE A 161 192.116 44.684 523.111 1.00 54.01 C ANISOU 1150 CZ PHE A 161 5037 8301 7184 -1159 233 123 C ATOM 1151 N TRP A 162 192.757 38.797 518.637 1.00 41.43 N ANISOU 1151 N TRP A 162 3367 7381 4993 -712 649 200 N ATOM 1152 CA TRP A 162 193.309 37.788 517.737 1.00 54.66 C ANISOU 1152 CA TRP A 162 5000 9177 6593 -651 772 187 C ATOM 1153 C TRP A 162 193.193 38.224 516.282 1.00 57.54 C ANISOU 1153 C TRP A 162 5420 9597 6844 -683 899 287 C ATOM 1154 O TRP A 162 194.090 37.957 515.472 1.00 65.61 O ANISOU 1154 O TRP A 162 6365 10714 7848 -686 1038 316 O ATOM 1155 CB TRP A 162 192.602 36.450 517.953 1.00 57.72 C ANISOU 1155 CB TRP A 162 5460 9581 6890 -534 735 82 C ATOM 1156 CG TRP A 162 193.074 35.355 517.050 1.00 57.28 C ANISOU 1156 CG TRP A 162 5380 9627 6757 -466 866 43 C ATOM 1157 CD1 TRP A 162 192.380 34.783 516.024 1.00 55.20 C ANISOU 1157 CD1 TRP A 162 5226 9415 6333 -425 930 16 C ATOM 1158 CD2 TRP A 162 194.345 34.697 517.090 1.00 60.11 C ANISOU 1158 CD2 TRP A 162 5592 10050 7198 -428 953 18 C ATOM 1159 NE1 TRP A 162 193.139 33.807 515.425 1.00 62.12 N ANISOU 1159 NE1 TRP A 162 6048 10373 7183 -367 1060 -38 N ATOM 1160 CE2 TRP A 162 194.351 33.736 516.061 1.00 64.86 C ANISOU 1160 CE2 TRP A 162 6234 10726 7685 -359 1082 -30 C ATOM 1161 CE3 TRP A 162 195.479 34.827 517.897 1.00 60.66 C ANISOU 1161 CE3 TRP A 162 5493 10128 7428 -443 930 26 C ATOM 1162 CZ2 TRP A 162 195.446 32.909 515.817 1.00 69.23 C ANISOU 1162 CZ2 TRP A 162 6669 11345 8289 -296 1206 -65 C ATOM 1163 CZ3 TRP A 162 196.565 34.007 517.654 1.00 64.76 C ANISOU 1163 CZ3 TRP A 162 5880 10728 8000 -379 1040 5 C ATOM 1164 CH2 TRP A 162 196.541 33.061 516.622 1.00 68.48 C ANISOU 1164 CH2 TRP A 162 6399 11256 8365 -301 1184 -38 C ATOM 1165 N GLN A 163 192.092 38.898 515.934 1.00 53.81 N ANISOU 1165 N GLN A 163 5078 9076 6290 -700 858 350 N ATOM 1166 CA GLN A 163 191.933 39.435 514.586 1.00 49.26 C ANISOU 1166 CA GLN A 163 4562 8561 5594 -727 964 471 C ATOM 1167 C GLN A 163 193.069 40.387 514.233 1.00 53.63 C ANISOU 1167 C GLN A 163 5011 9110 6256 -827 1076 588 C ATOM 1168 O GLN A 163 193.533 40.414 513.086 1.00 56.79 O ANISOU 1168 O GLN A 163 5400 9610 6566 -837 1222 669 O ATOM 1169 CB GLN A 163 190.583 40.142 514.468 1.00 46.96 C ANISOU 1169 CB GLN A 163 4407 8203 5233 -725 879 538 C ATOM 1170 CG GLN A 163 190.321 41.146 515.583 1.00 51.62 C ANISOU 1170 CG GLN A 163 4996 8631 5987 -777 774 556 C ATOM 1171 CD GLN A 163 188.895 41.656 515.595 1.00 55.66 C ANISOU 1171 CD GLN A 163 5635 9073 6440 -745 686 602 C ATOM 1172 OE1 GLN A 163 188.279 41.837 514.545 1.00 56.22 O ANISOU 1172 OE1 GLN A 163 5782 9207 6372 -721 721 698 O ATOM 1173 NE2 GLN A 163 188.359 41.883 516.789 1.00 59.02 N ANISOU 1173 NE2 GLN A 163 6080 9379 6966 -738 571 535 N ATOM 1174 N PHE A 164 193.532 41.176 515.205 1.00 50.14 N ANISOU 1174 N PHE A 164 4489 8556 6006 -907 1015 593 N ATOM 1175 CA PHE A 164 194.667 42.055 514.955 1.00 48.76 C ANISOU 1175 CA PHE A 164 4193 8366 5967 -1019 1120 690 C ATOM 1176 C PHE A 164 195.977 41.279 514.920 1.00 53.00 C ANISOU 1176 C PHE A 164 4561 9014 6562 -1012 1208 636 C ATOM 1177 O PHE A 164 196.914 41.684 514.223 1.00 49.85 O ANISOU 1177 O PHE A 164 4064 8663 6212 -1079 1354 729 O ATOM 1178 CB PHE A 164 194.729 43.155 516.014 1.00 49.53 C ANISOU 1178 CB PHE A 164 4260 8302 6258 -1121 1021 689 C ATOM 1179 CG PHE A 164 193.468 43.964 516.121 1.00 53.53 C ANISOU 1179 CG PHE A 164 4924 8681 6735 -1118 945 742 C ATOM 1180 CD1 PHE A 164 193.159 44.919 515.167 1.00 56.15 C ANISOU 1180 CD1 PHE A 164 5328 8970 7036 -1157 1036 912 C ATOM 1181 CD2 PHE A 164 192.593 43.770 517.177 1.00 51.56 C ANISOU 1181 CD2 PHE A 164 4744 8356 6490 -1068 791 633 C ATOM 1182 CE1 PHE A 164 191.998 45.665 515.262 1.00 57.62 C ANISOU 1182 CE1 PHE A 164 5648 9036 7208 -1138 969 973 C ATOM 1183 CE2 PHE A 164 191.431 44.513 517.279 1.00 53.76 C ANISOU 1183 CE2 PHE A 164 5155 8517 6754 -1055 732 683 C ATOM 1184 CZ PHE A 164 191.132 45.462 516.320 1.00 54.94 C ANISOU 1184 CZ PHE A 164 5369 8621 6885 -1086 818 853 C ATOM 1185 N ILE A 165 196.061 40.168 515.655 1.00 56.32 N ANISOU 1185 N ILE A 165 4940 9474 6986 -925 1131 498 N ATOM 1186 CA ILE A 165 197.275 39.357 515.628 1.00 58.68 C ANISOU 1186 CA ILE A 165 5071 9877 7346 -893 1216 453 C ATOM 1187 C ILE A 165 197.466 38.728 514.253 1.00 57.58 C ANISOU 1187 C ILE A 165 4959 9863 7055 -834 1398 487 C ATOM 1188 O ILE A 165 198.548 38.808 513.660 1.00 63.81 O ANISOU 1188 O ILE A 165 5618 10730 7897 -868 1550 543 O ATOM 1189 CB ILE A 165 197.238 38.288 516.734 1.00 61.63 C ANISOU 1189 CB ILE A 165 5409 10255 7753 -796 1093 316 C ATOM 1190 CG1 ILE A 165 197.136 38.947 518.110 1.00 61.21 C ANISOU 1190 CG1 ILE A 165 5326 10099 7830 -859 918 279 C ATOM 1191 CG2 ILE A 165 198.472 37.403 516.655 1.00 60.24 C ANISOU 1191 CG2 ILE A 165 5056 10187 7645 -739 1188 283 C ATOM 1192 CD1 ILE A 165 198.270 39.893 518.417 1.00 61.41 C ANISOU 1192 CD1 ILE A 165 5178 10114 8040 -992 929 323 C ATOM 1193 N VAL A 166 196.418 38.089 513.723 1.00 54.41 N ANISOU 1193 N VAL A 166 4723 9489 6461 -749 1388 445 N ATOM 1194 CA VAL A 166 196.516 37.472 512.400 1.00 59.22 C ANISOU 1194 CA VAL A 166 5380 10226 6897 -694 1554 452 C ATOM 1195 C VAL A 166 196.386 38.478 511.269 1.00 55.07 C ANISOU 1195 C VAL A 166 4920 9736 6267 -766 1660 610 C ATOM 1196 O VAL A 166 196.691 38.141 510.118 1.00 52.82 O ANISOU 1196 O VAL A 166 4654 9576 5838 -738 1823 638 O ATOM 1197 CB VAL A 166 195.455 36.373 512.211 1.00 66.78 C ANISOU 1197 CB VAL A 166 6485 11207 7682 -588 1501 331 C ATOM 1198 CG1 VAL A 166 195.722 35.213 513.155 1.00 66.44 C ANISOU 1198 CG1 VAL A 166 6374 11136 7735 -501 1445 191 C ATOM 1199 CG2 VAL A 166 194.062 36.936 512.430 1.00 68.72 C ANISOU 1199 CG2 VAL A 166 6882 11374 7855 -608 1352 357 C ATOM 1200 N GLY A 167 195.947 39.700 511.559 1.00 52.77 N ANISOU 1200 N GLY A 167 4669 9339 6043 -852 1582 717 N ATOM 1201 CA GLY A 167 195.847 40.726 510.544 1.00 54.07 C ANISOU 1201 CA GLY A 167 4894 9521 6131 -916 1686 896 C ATOM 1202 C GLY A 167 194.624 40.647 509.661 1.00 57.75 C ANISOU 1202 C GLY A 167 5547 10048 6347 -856 1665 936 C ATOM 1203 O GLY A 167 194.567 41.351 508.647 1.00 53.03 O ANISOU 1203 O GLY A 167 5006 9502 5640 -886 1768 1096 O ATOM 1204 N VAL A 168 193.644 39.818 510.008 1.00 57.03 N ANISOU 1204 N VAL A 168 5548 9958 6161 -775 1534 802 N ATOM 1205 CA VAL A 168 192.417 39.717 509.229 1.00 57.29 C ANISOU 1205 CA VAL A 168 5743 10059 5964 -724 1487 825 C ATOM 1206 C VAL A 168 191.314 39.227 510.155 1.00 55.66 C ANISOU 1206 C VAL A 168 5599 9771 5778 -675 1298 699 C ATOM 1207 O VAL A 168 191.558 38.441 511.075 1.00 46.33 O ANISOU 1207 O VAL A 168 4356 8541 4705 -645 1245 555 O ATOM 1208 CB VAL A 168 192.604 38.792 508.001 1.00 65.52 C ANISOU 1208 CB VAL A 168 6830 11292 6774 -668 1620 773 C ATOM 1209 CG1 VAL A 168 192.814 37.344 508.430 1.00 63.11 C ANISOU 1209 CG1 VAL A 168 6489 11008 6483 -598 1612 556 C ATOM 1210 CG2 VAL A 168 191.431 38.925 507.037 1.00 51.44 C ANISOU 1210 CG2 VAL A 168 5204 9609 4734 -638 1576 831 C ATOM 1211 N ARG A 169 190.103 39.725 509.928 1.00 53.10 N ANISOU 1211 N ARG A 169 5388 9431 5355 -662 1200 767 N ATOM 1212 CA ARG A 169 188.929 39.318 510.691 1.00 47.34 C ANISOU 1212 CA ARG A 169 4720 8635 4632 -615 1032 664 C ATOM 1213 C ARG A 169 188.084 38.409 509.808 1.00 49.63 C ANISOU 1213 C ARG A 169 5104 9068 4684 -556 1013 586 C ATOM 1214 O ARG A 169 187.440 38.875 508.863 1.00 51.99 O ANISOU 1214 O ARG A 169 5483 9458 4814 -551 1009 695 O ATOM 1215 CB ARG A 169 188.126 40.530 511.157 1.00 45.01 C ANISOU 1215 CB ARG A 169 4468 8211 4423 -639 930 786 C ATOM 1216 CG ARG A 169 186.822 40.164 511.844 1.00 45.46 C ANISOU 1216 CG ARG A 169 4585 8214 4473 -586 771 696 C ATOM 1217 CD ARG A 169 185.987 41.390 512.157 1.00 43.30 C ANISOU 1217 CD ARG A 169 4357 7821 4272 -594 691 828 C ATOM 1218 NE ARG A 169 184.738 41.027 512.817 1.00 46.54 N ANISOU 1218 NE ARG A 169 4812 8187 4683 -539 552 743 N ATOM 1219 CZ ARG A 169 184.595 40.915 514.133 1.00 44.97 C ANISOU 1219 CZ ARG A 169 4589 7860 4638 -536 477 644 C ATOM 1220 NH1 ARG A 169 185.625 41.145 514.936 1.00 50.91 N ANISOU 1220 NH1 ARG A 169 5271 8524 5550 -585 510 610 N ATOM 1221 NH2 ARG A 169 183.423 40.574 514.647 1.00 39.35 N ANISOU 1221 NH2 ARG A 169 3916 7119 3917 -485 369 580 N ATOM 1222 N THR A 170 188.095 37.113 510.111 1.00 48.95 N ANISOU 1222 N THR A 170 5009 9003 4587 -512 1002 398 N ATOM 1223 CA THR A 170 187.328 36.145 509.339 1.00 54.79 C ANISOU 1223 CA THR A 170 5834 9865 5121 -471 984 286 C ATOM 1224 C THR A 170 185.877 36.044 509.787 1.00 59.38 C ANISOU 1224 C THR A 170 6477 10400 5686 -451 814 243 C ATOM 1225 O THR A 170 185.119 35.264 509.201 1.00 65.36 O ANISOU 1225 O THR A 170 7298 11254 6284 -430 777 140 O ATOM 1226 CB THR A 170 187.987 34.765 509.414 1.00 55.73 C ANISOU 1226 CB THR A 170 5918 10006 5251 -434 1067 99 C ATOM 1227 OG1 THR A 170 188.061 34.341 510.782 1.00 61.35 O ANISOU 1227 OG1 THR A 170 6571 10572 6169 -413 996 16 O ATOM 1228 CG2 THR A 170 189.386 34.813 508.824 1.00 46.62 C ANISOU 1228 CG2 THR A 170 4694 8923 4095 -443 1252 140 C ATOM 1229 N VAL A 171 185.473 36.803 510.804 1.00 59.20 N ANISOU 1229 N VAL A 171 6433 10234 5826 -460 715 311 N ATOM 1230 CA VAL A 171 184.081 36.843 511.247 1.00 56.27 C ANISOU 1230 CA VAL A 171 6108 9816 5454 -437 566 293 C ATOM 1231 C VAL A 171 183.339 37.789 510.307 1.00 57.91 C ANISOU 1231 C VAL A 171 6373 10110 5522 -439 530 457 C ATOM 1232 O VAL A 171 183.411 39.010 510.452 1.00 60.12 O ANISOU 1232 O VAL A 171 6646 10313 5884 -454 531 622 O ATOM 1233 CB VAL A 171 183.956 37.282 512.708 1.00 54.68 C ANISOU 1233 CB VAL A 171 5869 9435 5474 -438 490 295 C ATOM 1234 CG1 VAL A 171 182.495 37.287 513.136 1.00 51.46 C ANISOU 1234 CG1 VAL A 171 5501 8985 5065 -407 356 276 C ATOM 1235 CG2 VAL A 171 184.778 36.373 513.608 1.00 39.21 C ANISOU 1235 CG2 VAL A 171 3849 7413 3637 -427 524 158 C ATOM 1236 N GLU A 172 182.627 37.225 509.335 1.00 58.69 N ANISOU 1236 N GLU A 172 6526 10366 5408 -422 498 411 N ATOM 1237 CA GLU A 172 181.936 38.032 508.343 1.00 64.86 C ANISOU 1237 CA GLU A 172 7357 11265 6023 -412 457 574 C ATOM 1238 C GLU A 172 180.739 38.746 508.970 1.00 61.51 C ANISOU 1238 C GLU A 172 6932 10746 5694 -383 315 660 C ATOM 1239 O GLU A 172 180.298 38.432 510.079 1.00 60.55 O ANISOU 1239 O GLU A 172 6782 10495 5730 -374 245 561 O ATOM 1240 CB GLU A 172 181.496 37.163 507.166 1.00 73.43 C ANISOU 1240 CB GLU A 172 8497 12565 6840 -406 445 477 C ATOM 1241 CG GLU A 172 182.656 36.521 506.419 1.00 81.60 C ANISOU 1241 CG GLU A 172 9543 13703 7758 -423 605 399 C ATOM 1242 CD GLU A 172 182.204 35.496 505.401 1.00 90.28 C ANISOU 1242 CD GLU A 172 10703 14997 8602 -423 592 243 C ATOM 1243 OE1 GLU A 172 180.981 35.276 505.276 1.00 93.97 O ANISOU 1243 OE1 GLU A 172 11194 15525 8986 -419 444 197 O ATOM 1244 OE2 GLU A 172 183.073 34.905 504.726 1.00 95.42 O ANISOU 1244 OE2 GLU A 172 11374 15741 9139 -430 731 159 O ATOM 1245 N ASP A 173 180.218 39.729 508.236 1.00 63.05 N ANISOU 1245 N ASP A 173 7157 11008 5790 -360 284 857 N ATOM 1246 CA ASP A 173 179.107 40.534 508.725 1.00 62.50 C ANISOU 1246 CA ASP A 173 7080 10850 5815 -318 166 967 C ATOM 1247 C ASP A 173 177.890 39.660 509.002 1.00 60.56 C ANISOU 1247 C ASP A 173 6821 10653 5538 -295 29 818 C ATOM 1248 O ASP A 173 177.546 38.772 508.217 1.00 61.78 O ANISOU 1248 O ASP A 173 6992 10983 5499 -305 -7 712 O ATOM 1249 CB ASP A 173 178.757 41.620 507.705 1.00 69.30 C ANISOU 1249 CB ASP A 173 7978 11806 6548 -283 161 1217 C ATOM 1250 CG ASP A 173 177.723 42.602 508.223 1.00 75.75 C ANISOU 1250 CG ASP A 173 8781 12504 7496 -225 64 1359 C ATOM 1251 OD1 ASP A 173 177.484 42.633 509.449 1.00 77.52 O ANISOU 1251 OD1 ASP A 173 8974 12547 7934 -223 30 1276 O ATOM 1252 OD2 ASP A 173 177.144 43.343 507.400 1.00 79.77 O ANISOU 1252 OD2 ASP A 173 9313 13105 7890 -173 26 1559 O ATOM 1253 N GLY A 174 177.236 39.918 510.133 1.00 54.32 N ANISOU 1253 N GLY A 174 5998 9702 4940 -271 -41 804 N ATOM 1254 CA GLY A 174 176.090 39.140 510.549 1.00 51.40 C ANISOU 1254 CA GLY A 174 5599 9350 4582 -255 -156 672 C ATOM 1255 C GLY A 174 176.416 37.894 511.341 1.00 51.07 C ANISOU 1255 C GLY A 174 5542 9242 4620 -289 -130 446 C ATOM 1256 O GLY A 174 175.490 37.206 511.789 1.00 44.95 O ANISOU 1256 O GLY A 174 4740 8459 3881 -284 -210 333 O ATOM 1257 N GLU A 175 177.694 37.580 511.524 1.00 55.84 N ANISOU 1257 N GLU A 175 6155 9799 5263 -321 -17 385 N ATOM 1258 CA GLU A 175 178.130 36.430 512.298 1.00 60.24 C ANISOU 1258 CA GLU A 175 6695 10284 5908 -338 20 195 C ATOM 1259 C GLU A 175 178.734 36.893 513.617 1.00 60.88 C ANISOU 1259 C GLU A 175 6751 10178 6203 -332 52 214 C ATOM 1260 O GLU A 175 179.219 38.020 513.743 1.00 65.31 O ANISOU 1260 O GLU A 175 7310 10674 6833 -337 84 350 O ATOM 1261 CB GLU A 175 179.158 35.602 511.520 1.00 68.36 C ANISOU 1261 CB GLU A 175 7742 11413 6819 -366 126 100 C ATOM 1262 CG GLU A 175 178.674 35.118 510.165 1.00 77.04 C ANISOU 1262 CG GLU A 175 8881 12715 7678 -379 103 57 C ATOM 1263 CD GLU A 175 179.789 34.515 509.333 1.00 87.55 C ANISOU 1263 CD GLU A 175 10238 14144 8884 -399 234 -17 C ATOM 1264 OE1 GLU A 175 180.972 34.730 509.674 1.00 90.46 O ANISOU 1264 OE1 GLU A 175 10581 14437 9351 -399 344 17 O ATOM 1265 OE2 GLU A 175 179.483 33.825 508.338 1.00 94.27 O ANISOU 1265 OE2 GLU A 175 11128 15152 9538 -415 228 -117 O ATOM 1266 N CYS A 176 178.700 36.004 514.608 1.00 59.01 N ANISOU 1266 N CYS A 176 6496 9854 6071 -326 45 75 N ATOM 1267 CA CYS A 176 179.307 36.299 515.904 1.00 56.71 C ANISOU 1267 CA CYS A 176 6180 9410 5956 -319 66 72 C ATOM 1268 C CYS A 176 179.840 35.002 516.494 1.00 55.32 C ANISOU 1268 C CYS A 176 5987 9204 5826 -313 107 -80 C ATOM 1269 O CYS A 176 179.061 34.158 516.948 1.00 56.89 O ANISOU 1269 O CYS A 176 6191 9376 6047 -295 67 -175 O ATOM 1270 CB CYS A 176 178.311 36.963 516.848 1.00 51.93 C ANISOU 1270 CB CYS A 176 5575 8695 5460 -290 -13 117 C ATOM 1271 SG CYS A 176 179.092 37.555 518.357 0.91 52.47 S ANISOU 1271 SG CYS A 176 5629 8596 5712 -291 8 117 S ATOM 1272 N TYR A 177 181.162 34.852 516.493 1.00 50.33 N ANISOU 1272 N TYR A 177 5328 8573 5220 -324 191 -93 N ATOM 1273 CA TYR A 177 181.810 33.670 517.043 1.00 50.35 C ANISOU 1273 CA TYR A 177 5306 8545 5279 -301 240 -214 C ATOM 1274 C TYR A 177 183.279 33.985 517.278 1.00 46.64 C ANISOU 1274 C TYR A 177 4779 8062 4880 -310 311 -179 C ATOM 1275 O TYR A 177 183.827 34.937 516.716 1.00 45.58 O ANISOU 1275 O TYR A 177 4630 7964 4725 -348 346 -78 O ATOM 1276 CB TYR A 177 181.653 32.457 516.117 1.00 53.80 C ANISOU 1276 CB TYR A 177 5768 9070 5602 -299 286 -330 C ATOM 1277 CG TYR A 177 182.216 32.657 514.726 1.00 60.46 C ANISOU 1277 CG TYR A 177 6625 10048 6300 -325 359 -300 C ATOM 1278 CD1 TYR A 177 181.471 33.291 513.739 1.00 61.73 C ANISOU 1278 CD1 TYR A 177 6824 10312 6317 -349 314 -227 C ATOM 1279 CD2 TYR A 177 183.487 32.204 514.398 1.00 59.78 C ANISOU 1279 CD2 TYR A 177 6507 9995 6213 -317 477 -336 C ATOM 1280 CE1 TYR A 177 181.979 33.474 512.468 1.00 63.15 C ANISOU 1280 CE1 TYR A 177 7025 10629 6340 -368 387 -190 C ATOM 1281 CE2 TYR A 177 184.002 32.382 513.128 1.00 62.43 C ANISOU 1281 CE2 TYR A 177 6857 10461 6404 -338 561 -307 C ATOM 1282 CZ TYR A 177 183.244 33.017 512.167 1.00 65.62 C ANISOU 1282 CZ TYR A 177 7313 10970 6650 -365 517 -234 C ATOM 1283 OH TYR A 177 183.753 33.198 510.901 1.00 71.71 O ANISOU 1283 OH TYR A 177 8107 11884 7254 -381 606 -194 O ATOM 1284 N ILE A 178 183.906 33.176 518.130 1.00 49.11 N ANISOU 1284 N ILE A 178 5052 8323 5284 -276 334 -253 N ATOM 1285 CA ILE A 178 185.320 33.352 518.441 1.00 47.34 C ANISOU 1285 CA ILE A 178 4749 8099 5140 -279 390 -229 C ATOM 1286 C ILE A 178 186.146 32.978 517.217 1.00 43.79 C ANISOU 1286 C ILE A 178 4275 7754 4608 -286 508 -240 C ATOM 1287 O ILE A 178 186.046 31.859 516.701 1.00 45.37 O ANISOU 1287 O ILE A 178 4501 7992 4746 -252 563 -336 O ATOM 1288 CB ILE A 178 185.719 32.517 519.664 1.00 44.01 C ANISOU 1288 CB ILE A 178 4285 7611 4824 -223 374 -294 C ATOM 1289 CG1 ILE A 178 185.125 33.126 520.936 1.00 42.35 C ANISOU 1289 CG1 ILE A 178 4094 7312 4687 -222 270 -269 C ATOM 1290 CG2 ILE A 178 187.227 32.411 519.766 1.00 43.07 C ANISOU 1290 CG2 ILE A 178 4064 7527 4774 -214 440 -283 C ATOM 1291 CD1 ILE A 178 185.519 32.400 522.202 1.00 44.19 C ANISOU 1291 CD1 ILE A 178 4292 7497 5003 -163 246 -312 C ATOM 1292 N GLN A 179 186.974 33.917 516.752 1.00 44.95 N ANISOU 1292 N GLN A 179 4376 7943 4761 -334 558 -144 N ATOM 1293 CA GLN A 179 187.674 33.735 515.483 1.00 50.29 C ANISOU 1293 CA GLN A 179 5038 8732 5338 -345 683 -134 C ATOM 1294 C GLN A 179 188.657 32.571 515.546 1.00 60.63 C ANISOU 1294 C GLN A 179 6281 10063 6692 -290 779 -228 C ATOM 1295 O GLN A 179 188.664 31.707 514.660 1.00 63.84 O ANISOU 1295 O GLN A 179 6724 10539 6995 -262 866 -308 O ATOM 1296 CB GLN A 179 188.387 35.027 515.085 1.00 48.34 C ANISOU 1296 CB GLN A 179 4745 8508 5114 -412 729 5 C ATOM 1297 CG GLN A 179 189.181 34.912 513.795 1.00 55.23 C ANISOU 1297 CG GLN A 179 5598 9506 5883 -423 878 34 C ATOM 1298 CD GLN A 179 189.488 36.260 513.176 1.00 59.60 C ANISOU 1298 CD GLN A 179 6142 10082 6420 -495 923 198 C ATOM 1299 OE1 GLN A 179 188.764 37.232 513.389 1.00 61.35 O ANISOU 1299 OE1 GLN A 179 6412 10240 6660 -527 838 288 O ATOM 1300 NE2 GLN A 179 190.567 36.326 512.403 1.00 59.57 N ANISOU 1300 NE2 GLN A 179 6076 10164 6394 -515 1069 244 N ATOM 1301 N PHE A 180 189.490 32.518 516.589 1.00 63.10 N ANISOU 1301 N PHE A 180 6496 10320 7158 -270 764 -225 N ATOM 1302 CA PHE A 180 190.456 31.426 516.654 1.00 65.91 C ANISOU 1302 CA PHE A 180 6774 10696 7570 -201 858 -295 C ATOM 1303 C PHE A 180 189.806 30.077 516.934 1.00 67.11 C ANISOU 1303 C PHE A 180 6991 10795 7713 -123 850 -414 C ATOM 1304 O PHE A 180 190.517 29.066 516.978 1.00 66.88 O ANISOU 1304 O PHE A 180 6909 10762 7738 -50 937 -475 O ATOM 1305 CB PHE A 180 191.546 31.721 517.694 1.00 64.15 C ANISOU 1305 CB PHE A 180 6414 10449 7512 -195 830 -250 C ATOM 1306 CG PHE A 180 191.039 31.897 519.100 1.00 59.84 C ANISOU 1306 CG PHE A 180 5879 9813 7046 -185 682 -251 C ATOM 1307 CD1 PHE A 180 190.838 30.800 519.924 1.00 58.73 C ANISOU 1307 CD1 PHE A 180 5746 9620 6948 -95 651 -316 C ATOM 1308 CD2 PHE A 180 190.804 33.162 519.612 1.00 57.82 C ANISOU 1308 CD2 PHE A 180 5627 9519 6824 -264 587 -184 C ATOM 1309 CE1 PHE A 180 190.385 30.961 521.222 1.00 56.35 C ANISOU 1309 CE1 PHE A 180 5461 9250 6701 -82 526 -310 C ATOM 1310 CE2 PHE A 180 190.355 33.329 520.911 1.00 53.40 C ANISOU 1310 CE2 PHE A 180 5083 8883 6321 -252 463 -197 C ATOM 1311 CZ PHE A 180 190.145 32.227 521.716 1.00 53.09 C ANISOU 1311 CZ PHE A 180 5055 8813 6304 -161 432 -258 C ATOM 1312 N PHE A 181 188.486 30.031 517.118 1.00 66.08 N ANISOU 1312 N PHE A 181 6962 10615 7528 -137 758 -444 N ATOM 1313 CA PHE A 181 187.741 28.782 517.151 1.00 64.94 C ANISOU 1313 CA PHE A 181 6888 10421 7365 -87 766 -562 C ATOM 1314 C PHE A 181 187.289 28.338 515.765 1.00 67.04 C ANISOU 1314 C PHE A 181 7232 10764 7476 -111 838 -645 C ATOM 1315 O PHE A 181 186.392 27.494 515.655 1.00 68.86 O ANISOU 1315 O PHE A 181 7535 10956 7672 -104 823 -750 O ATOM 1316 CB PHE A 181 186.533 28.905 518.084 1.00 60.34 C ANISOU 1316 CB PHE A 181 6362 9751 6814 -95 637 -557 C ATOM 1317 CG PHE A 181 186.870 28.738 519.539 1.00 59.27 C ANISOU 1317 CG PHE A 181 6174 9530 6815 -42 585 -529 C ATOM 1318 CD1 PHE A 181 188.110 28.254 519.926 1.00 57.50 C ANISOU 1318 CD1 PHE A 181 5857 9310 6681 20 645 -523 C ATOM 1319 CD2 PHE A 181 185.945 29.056 520.519 1.00 57.59 C ANISOU 1319 CD2 PHE A 181 6001 9248 6633 -47 477 -505 C ATOM 1320 CE1 PHE A 181 188.422 28.096 521.264 1.00 56.83 C ANISOU 1320 CE1 PHE A 181 5722 9170 6701 75 583 -488 C ATOM 1321 CE2 PHE A 181 186.251 28.900 521.859 1.00 57.96 C ANISOU 1321 CE2 PHE A 181 6009 9235 6777 5 429 -478 C ATOM 1322 CZ PHE A 181 187.492 28.420 522.231 1.00 60.13 C ANISOU 1322 CZ PHE A 181 6195 9525 7127 65 475 -468 C ATOM 1323 N SER A 182 187.881 28.899 514.706 1.00 67.71 N ANISOU 1323 N SER A 182 7304 10962 7461 -146 917 -602 N ATOM 1324 CA SER A 182 187.582 28.430 513.356 1.00 62.39 C ANISOU 1324 CA SER A 182 6706 10386 6614 -162 994 -690 C ATOM 1325 C SER A 182 187.965 26.968 513.179 1.00 64.71 C ANISOU 1325 C SER A 182 7008 10643 6936 -97 1110 -847 C ATOM 1326 O SER A 182 187.312 26.242 512.420 1.00 67.67 O ANISOU 1326 O SER A 182 7470 11045 7195 -111 1136 -979 O ATOM 1327 CB SER A 182 188.304 29.297 512.325 1.00 54.66 C ANISOU 1327 CB SER A 182 5705 9538 5524 -200 1080 -596 C ATOM 1328 OG SER A 182 187.879 30.645 512.406 1.00 53.20 O ANISOU 1328 OG SER A 182 5526 9370 5319 -259 984 -448 O ATOM 1329 N ASN A 183 189.014 26.520 513.865 1.00 62.10 N ANISOU 1329 N ASN A 183 6584 10249 6761 -26 1179 -838 N ATOM 1330 CA ASN A 183 189.422 25.124 513.843 1.00 60.68 C ANISOU 1330 CA ASN A 183 6405 10003 6648 56 1297 -969 C ATOM 1331 C ASN A 183 188.688 24.364 514.942 1.00 60.07 C ANISOU 1331 C ASN A 183 6356 9774 6693 94 1215 -1013 C ATOM 1332 O ASN A 183 188.588 24.843 516.076 1.00 59.28 O ANISOU 1332 O ASN A 183 6211 9619 6693 101 1106 -912 O ATOM 1333 CB ASN A 183 190.935 25.005 514.026 1.00 60.51 C ANISOU 1333 CB ASN A 183 6252 9994 6743 131 1415 -919 C ATOM 1334 CG ASN A 183 191.435 23.588 513.846 1.00 68.65 C ANISOU 1334 CG ASN A 183 7282 10959 7844 232 1565 -1049 C ATOM 1335 OD1 ASN A 183 191.510 22.819 514.803 1.00 71.88 O ANISOU 1335 OD1 ASN A 183 7662 11243 8408 312 1552 -1060 O ATOM 1336 ND2 ASN A 183 191.784 23.234 512.614 1.00 78.41 N ANISOU 1336 ND2 ASN A 183 8554 12274 8963 234 1717 -1146 N ATOM 1337 N ALA A 184 188.174 23.180 514.600 1.00 55.87 N ANISOU 1337 N ALA A 184 5903 9174 6151 113 1276 -1168 N ATOM 1338 CA ALA A 184 187.411 22.400 515.569 1.00 51.64 C ANISOU 1338 CA ALA A 184 5402 8485 5735 140 1218 -1207 C ATOM 1339 C ALA A 184 188.312 21.812 516.649 1.00 51.72 C ANISOU 1339 C ALA A 184 5327 8389 5935 258 1266 -1147 C ATOM 1340 O ALA A 184 187.937 21.778 517.828 1.00 53.71 O ANISOU 1340 O ALA A 184 5568 8553 6288 284 1175 -1077 O ATOM 1341 CB ALA A 184 186.633 21.295 514.855 1.00 50.39 C ANISOU 1341 CB ALA A 184 5348 8271 5528 113 1279 -1397 C ATOM 1342 N ALA A 185 189.503 21.342 516.267 1.00 51.48 N ANISOU 1342 N ALA A 185 5232 8375 5953 337 1409 -1168 N ATOM 1343 CA ALA A 185 190.413 20.752 517.244 1.00 54.86 C ANISOU 1343 CA ALA A 185 5563 8718 6563 465 1453 -1100 C ATOM 1344 C ALA A 185 190.887 21.780 518.264 1.00 53.95 C ANISOU 1344 C ALA A 185 5340 8659 6499 467 1326 -929 C ATOM 1345 O ALA A 185 191.088 21.440 519.436 1.00 55.01 O ANISOU 1345 O ALA A 185 5425 8718 6757 547 1278 -855 O ATOM 1346 CB ALA A 185 191.606 20.112 516.534 1.00 54.87 C ANISOU 1346 CB ALA A 185 5502 8739 6606 553 1641 -1155 C ATOM 1347 N VAL A 186 191.074 23.032 517.840 1.00 52.64 N ANISOU 1347 N VAL A 186 5140 8623 6237 379 1273 -865 N ATOM 1348 CA VAL A 186 191.414 24.096 518.782 1.00 55.66 C ANISOU 1348 CA VAL A 186 5434 9048 6666 355 1144 -726 C ATOM 1349 C VAL A 186 190.299 24.268 519.804 1.00 53.53 C ANISOU 1349 C VAL A 186 5236 8699 6404 330 997 -699 C ATOM 1350 O VAL A 186 190.544 24.352 521.015 1.00 57.52 O ANISOU 1350 O VAL A 186 5685 9173 6998 378 915 -620 O ATOM 1351 CB VAL A 186 191.695 25.408 518.029 1.00 53.54 C ANISOU 1351 CB VAL A 186 5135 8908 6301 251 1131 -670 C ATOM 1352 CG1 VAL A 186 191.849 26.564 519.008 1.00 53.31 C ANISOU 1352 CG1 VAL A 186 5037 8896 6321 203 989 -551 C ATOM 1353 CG2 VAL A 186 192.936 25.267 517.162 1.00 50.05 C ANISOU 1353 CG2 VAL A 186 4598 8551 5867 283 1289 -675 C ATOM 1354 N THR A 187 189.053 24.312 519.327 1.00 50.98 N ANISOU 1354 N THR A 187 5033 8353 5982 257 964 -764 N ATOM 1355 CA THR A 187 187.915 24.467 520.224 1.00 44.13 C ANISOU 1355 CA THR A 187 4230 7413 5125 233 842 -742 C ATOM 1356 C THR A 187 187.825 23.307 521.207 1.00 41.03 C ANISOU 1356 C THR A 187 3845 6894 4851 331 862 -751 C ATOM 1357 O THR A 187 187.563 23.511 522.398 1.00 38.38 O ANISOU 1357 O THR A 187 3502 6519 4563 356 770 -675 O ATOM 1358 CB THR A 187 186.624 24.585 519.414 1.00 45.00 C ANISOU 1358 CB THR A 187 4448 7531 5119 144 815 -817 C ATOM 1359 OG1 THR A 187 186.786 25.583 518.398 1.00 46.37 O ANISOU 1359 OG1 THR A 187 4618 7828 5172 70 813 -793 O ATOM 1360 CG2 THR A 187 185.460 24.972 520.315 1.00 35.48 C ANISOU 1360 CG2 THR A 187 3288 6268 3926 113 690 -777 C ATOM 1361 N PHE A 188 188.054 22.080 520.731 1.00 44.41 N ANISOU 1361 N PHE A 188 4293 7255 5327 393 992 -840 N ATOM 1362 CA PHE A 188 187.958 20.926 521.621 1.00 47.25 C ANISOU 1362 CA PHE A 188 4666 7473 5813 493 1029 -835 C ATOM 1363 C PHE A 188 189.080 20.918 522.650 1.00 45.06 C ANISOU 1363 C PHE A 188 4275 7210 5636 605 1011 -710 C ATOM 1364 O PHE A 188 188.843 20.618 523.825 1.00 40.85 O ANISOU 1364 O PHE A 188 3745 6609 5165 667 956 -634 O ATOM 1365 CB PHE A 188 187.966 19.628 520.818 1.00 51.80 C ANISOU 1365 CB PHE A 188 5295 7955 6434 531 1186 -970 C ATOM 1366 CG PHE A 188 187.937 18.393 521.672 1.00 51.41 C ANISOU 1366 CG PHE A 188 5259 7735 6537 642 1249 -953 C ATOM 1367 CD1 PHE A 188 186.956 18.226 522.636 1.00 50.54 C ANISOU 1367 CD1 PHE A 188 5204 7533 6464 631 1175 -905 C ATOM 1368 CD2 PHE A 188 188.887 17.398 521.511 1.00 54.37 C ANISOU 1368 CD2 PHE A 188 5594 8040 7026 764 1394 -975 C ATOM 1369 CE1 PHE A 188 186.926 17.094 523.427 1.00 50.28 C ANISOU 1369 CE1 PHE A 188 5191 7341 6574 735 1245 -869 C ATOM 1370 CE2 PHE A 188 188.860 16.262 522.298 1.00 54.24 C ANISOU 1370 CE2 PHE A 188 5595 7854 7160 876 1461 -939 C ATOM 1371 CZ PHE A 188 187.880 16.111 523.257 1.00 50.93 C ANISOU 1371 CZ PHE A 188 5235 7343 6771 859 1386 -881 C ATOM 1372 N GLY A 189 190.308 21.226 522.229 1.00 47.82 N ANISOU 1372 N GLY A 189 4516 7657 5996 636 1058 -684 N ATOM 1373 CA GLY A 189 191.400 21.311 523.187 1.00 48.44 C ANISOU 1373 CA GLY A 189 4462 7779 6165 733 1018 -564 C ATOM 1374 C GLY A 189 191.146 22.361 524.250 1.00 48.07 C ANISOU 1374 C GLY A 189 4396 7788 6080 682 844 -470 C ATOM 1375 O GLY A 189 191.352 22.124 525.446 1.00 47.83 O ANISOU 1375 O GLY A 189 4328 7741 6105 764 777 -383 O ATOM 1376 N THR A 190 190.680 23.538 523.826 1.00 42.85 N ANISOU 1376 N THR A 190 3767 7194 5318 550 773 -485 N ATOM 1377 CA THR A 190 190.312 24.572 524.787 1.00 47.43 C ANISOU 1377 CA THR A 190 4350 7808 5862 494 619 -419 C ATOM 1378 C THR A 190 189.205 24.090 525.717 1.00 53.39 C ANISOU 1378 C THR A 190 5207 8462 6616 525 569 -411 C ATOM 1379 O THR A 190 189.182 24.440 526.903 1.00 58.47 O ANISOU 1379 O THR A 190 5836 9119 7260 548 467 -342 O ATOM 1380 CB THR A 190 189.888 25.840 524.050 1.00 47.46 C ANISOU 1380 CB THR A 190 4387 7871 5773 356 576 -438 C ATOM 1381 OG1 THR A 190 190.935 26.243 523.159 1.00 52.15 O ANISOU 1381 OG1 THR A 190 4888 8557 6371 328 644 -434 O ATOM 1382 CG2 THR A 190 189.625 26.958 525.033 1.00 45.61 C ANISOU 1382 CG2 THR A 190 4151 7658 5519 301 433 -381 C ATOM 1383 N ALA A 191 188.281 23.274 525.199 1.00 58.73 N ANISOU 1383 N ALA A 191 5984 9041 7289 521 646 -485 N ATOM 1384 CA ALA A 191 187.241 22.706 526.050 1.00 60.87 C ANISOU 1384 CA ALA A 191 6341 9206 7579 549 623 -472 C ATOM 1385 C ALA A 191 187.812 21.690 527.031 1.00 59.87 C ANISOU 1385 C ALA A 191 6180 9020 7550 692 657 -397 C ATOM 1386 O ALA A 191 187.247 21.489 528.111 1.00 64.03 O ANISOU 1386 O ALA A 191 6750 9496 8083 731 611 -334 O ATOM 1387 CB ALA A 191 186.148 22.064 525.195 1.00 54.78 C ANISOU 1387 CB ALA A 191 5670 8347 6796 495 697 -580 C ATOM 1388 N ILE A 192 188.921 21.040 526.674 1.00 52.33 N ANISOU 1388 N ILE A 192 5143 8071 6668 780 745 -392 N ATOM 1389 CA ILE A 192 189.577 20.127 527.603 1.00 53.58 C ANISOU 1389 CA ILE A 192 5251 8184 6925 934 772 -295 C ATOM 1390 C ILE A 192 190.251 20.909 528.722 1.00 53.68 C ANISOU 1390 C ILE A 192 5171 8322 6904 966 630 -181 C ATOM 1391 O ILE A 192 190.139 20.559 529.902 1.00 53.89 O ANISOU 1391 O ILE A 192 5209 8328 6938 1051 579 -85 O ATOM 1392 CB ILE A 192 190.582 19.230 526.859 1.00 54.43 C ANISOU 1392 CB ILE A 192 5287 8262 7132 1029 915 -323 C ATOM 1393 CG1 ILE A 192 189.856 18.295 525.891 1.00 59.72 C ANISOU 1393 CG1 ILE A 192 6066 8787 7837 1004 1060 -454 C ATOM 1394 CG2 ILE A 192 191.422 18.433 527.846 1.00 52.00 C ANISOU 1394 CG2 ILE A 192 4897 7932 6930 1206 928 -193 C ATOM 1395 CD1 ILE A 192 190.783 17.371 525.130 1.00 59.64 C ANISOU 1395 CD1 ILE A 192 6005 8729 7927 1102 1223 -504 C ATOM 1396 N ALA A 193 190.954 21.987 528.368 1.00 50.70 N ANISOU 1396 N ALA A 193 4701 8078 6483 892 564 -191 N ATOM 1397 CA ALA A 193 191.633 22.782 529.385 1.00 50.96 C ANISOU 1397 CA ALA A 193 4638 8236 6488 900 420 -108 C ATOM 1398 C ALA A 193 190.650 23.537 530.272 1.00 53.06 C ANISOU 1398 C ALA A 193 4999 8503 6657 830 300 -99 C ATOM 1399 O ALA A 193 190.939 23.773 531.450 1.00 54.52 O ANISOU 1399 O ALA A 193 5149 8755 6809 875 190 -27 O ATOM 1400 CB ALA A 193 192.606 23.758 528.724 1.00 53.13 C ANISOU 1400 CB ALA A 193 4788 8636 6762 818 394 -131 C ATOM 1401 N ALA A 194 189.490 23.914 529.737 1.00 49.40 N ANISOU 1401 N ALA A 194 4653 7974 6142 727 318 -173 N ATOM 1402 CA ALA A 194 188.566 24.786 530.451 1.00 45.93 C ANISOU 1402 CA ALA A 194 4294 7538 5619 655 217 -173 C ATOM 1403 C ALA A 194 187.428 24.049 531.142 1.00 47.94 C ANISOU 1403 C ALA A 194 4663 7687 5864 705 245 -150 C ATOM 1404 O ALA A 194 186.927 24.535 532.162 1.00 50.41 O ANISOU 1404 O ALA A 194 5023 8019 6114 700 163 -117 O ATOM 1405 CB ALA A 194 187.974 25.827 529.494 1.00 40.82 C ANISOU 1405 CB ALA A 194 3689 6897 4925 514 208 -249 C ATOM 1406 N PHE A 195 186.994 22.902 530.623 1.00 45.48 N ANISOU 1406 N PHE A 195 4400 7262 5619 747 366 -172 N ATOM 1407 CA PHE A 195 185.847 22.207 531.194 1.00 42.62 C ANISOU 1407 CA PHE A 195 4141 6785 5268 774 408 -152 C ATOM 1408 C PHE A 195 186.180 20.825 531.733 1.00 45.68 C ANISOU 1408 C PHE A 195 4527 7085 5744 916 494 -73 C ATOM 1409 O PHE A 195 185.892 20.539 532.901 1.00 47.17 O ANISOU 1409 O PHE A 195 4752 7255 5915 988 472 24 O ATOM 1410 CB PHE A 195 184.720 22.098 530.153 1.00 38.49 C ANISOU 1410 CB PHE A 195 3693 6178 4754 672 473 -258 C ATOM 1411 CG PHE A 195 183.496 21.397 530.666 1.00 39.14 C ANISOU 1411 CG PHE A 195 3865 6140 4868 680 524 -245 C ATOM 1412 CD1 PHE A 195 182.643 22.031 531.554 1.00 40.62 C ANISOU 1412 CD1 PHE A 195 4099 6341 4993 654 458 -206 C ATOM 1413 CD2 PHE A 195 183.203 20.102 530.272 1.00 39.60 C ANISOU 1413 CD2 PHE A 195 3957 6062 5028 712 649 -277 C ATOM 1414 CE1 PHE A 195 181.519 21.388 532.037 1.00 39.82 C ANISOU 1414 CE1 PHE A 195 4068 6133 4930 660 518 -186 C ATOM 1415 CE2 PHE A 195 182.079 19.454 530.750 1.00 39.22 C ANISOU 1415 CE2 PHE A 195 3981 5894 5028 706 704 -262 C ATOM 1416 CZ PHE A 195 181.236 20.099 531.633 1.00 38.01 C ANISOU 1416 CZ PHE A 195 3864 5767 4810 680 640 -210 C ATOM 1417 N TYR A 196 186.784 19.955 530.920 1.00 33.04 N ANISOU 1417 N TYR A 196 3088 3184 6282 140 -786 -1300 N ATOM 1418 CA TYR A 196 186.900 18.549 531.298 1.00 44.04 C ANISOU 1418 CA TYR A 196 4644 4412 7679 -93 -786 -1166 C ATOM 1419 C TYR A 196 187.823 18.362 532.499 1.00 53.16 C ANISOU 1419 C TYR A 196 5861 5427 8912 43 -932 -1197 C ATOM 1420 O TYR A 196 187.435 17.744 533.499 1.00 60.53 O ANISOU 1420 O TYR A 196 6812 6484 9703 -10 -919 -1065 O ATOM 1421 CB TYR A 196 187.380 17.725 530.103 1.00 45.34 C ANISOU 1421 CB TYR A 196 4987 4486 7752 -200 -639 -968 C ATOM 1422 CG TYR A 196 186.308 17.524 529.055 1.00 50.86 C ANISOU 1422 CG TYR A 196 5656 5317 8353 -410 -517 -967 C ATOM 1423 CD1 TYR A 196 186.109 18.457 528.045 1.00 50.90 C ANISOU 1423 CD1 TYR A 196 5552 5456 8334 -265 -492 -1021 C ATOM 1424 CD2 TYR A 196 185.484 16.406 529.084 1.00 49.76 C ANISOU 1424 CD2 TYR A 196 5566 5193 8146 -768 -415 -910 C ATOM 1425 CE1 TYR A 196 185.125 18.280 527.090 1.00 44.67 C ANISOU 1425 CE1 TYR A 196 4709 4832 7430 -460 -406 -1034 C ATOM 1426 CE2 TYR A 196 184.498 16.220 528.134 1.00 47.86 C ANISOU 1426 CE2 TYR A 196 5258 5174 7752 -990 -324 -918 C ATOM 1427 CZ TYR A 196 184.323 17.159 527.140 1.00 48.27 C ANISOU 1427 CZ TYR A 196 5199 5385 7756 -831 -339 -980 C ATOM 1428 OH TYR A 196 183.341 16.975 526.193 1.00 53.39 O ANISOU 1428 OH TYR A 196 5744 6296 8245 -1039 -277 -977 O ATOM 1429 N LEU A 197 189.047 18.885 532.418 1.00 52.20 N ANISOU 1429 N LEU A 197 5751 5353 8728 243 -963 -1172 N ATOM 1430 CA LEU A 197 189.970 18.778 533.546 1.00 56.57 C ANISOU 1430 CA LEU A 197 6344 5853 9299 396 -1105 -1233 C ATOM 1431 C LEU A 197 189.404 19.386 534.825 1.00 57.90 C ANISOU 1431 C LEU A 197 6369 6261 9369 580 -1196 -1428 C ATOM 1432 O LEU A 197 189.500 18.737 535.883 1.00 67.00 O ANISOU 1432 O LEU A 197 7545 7608 10304 637 -1203 -1232 O ATOM 1433 CB LEU A 197 191.320 19.402 533.171 1.00 56.12 C ANISOU 1433 CB LEU A 197 6275 5944 9106 434 -1101 -1198 C ATOM 1434 CG LEU A 197 192.014 18.834 531.931 1.00 58.89 C ANISOU 1434 CG LEU A 197 6747 6263 9367 314 -959 -970 C ATOM 1435 CD1 LEU A 197 193.282 19.614 531.618 1.00 62.07 C ANISOU 1435 CD1 LEU A 197 6983 6781 9820 361 -1078 -1051 C ATOM 1436 CD2 LEU A 197 192.318 17.356 532.110 1.00 59.43 C ANISOU 1436 CD2 LEU A 197 7012 6080 9489 259 -912 -816 C ATOM 1437 N PRO A 198 188.814 20.591 534.819 1.00 54.39 N ANISOU 1437 N PRO A 198 5753 6025 8886 656 -1179 -1656 N ATOM 1438 CA PRO A 198 188.187 21.083 536.059 1.00 53.72 C ANISOU 1438 CA PRO A 198 5516 6396 8499 756 -1170 -1687 C ATOM 1439 C PRO A 198 187.087 20.178 536.585 1.00 52.63 C ANISOU 1439 C PRO A 198 5392 6501 8106 595 -1095 -1381 C ATOM 1440 O PRO A 198 186.976 19.998 537.803 1.00 62.29 O ANISOU 1440 O PRO A 198 6565 8040 9064 682 -1116 -1288 O ATOM 1441 CB PRO A 198 187.643 22.457 535.649 1.00 47.18 C ANISOU 1441 CB PRO A 198 4592 5642 7693 795 -1068 -1915 C ATOM 1442 CG PRO A 198 188.520 22.886 534.539 1.00 45.38 C ANISOU 1442 CG PRO A 198 4507 5179 7556 616 -1056 -1865 C ATOM 1443 CD PRO A 198 188.824 21.633 533.775 1.00 48.72 C ANISOU 1443 CD PRO A 198 4994 5381 8136 531 -1088 -1648 C ATOM 1444 N VAL A 199 186.267 19.603 535.704 1.00 43.27 N ANISOU 1444 N VAL A 199 4255 5206 6980 353 -993 -1238 N ATOM 1445 CA VAL A 199 185.196 18.723 536.164 1.00 43.60 C ANISOU 1445 CA VAL A 199 4306 5462 6797 159 -882 -981 C ATOM 1446 C VAL A 199 185.775 17.475 536.818 1.00 43.91 C ANISOU 1446 C VAL A 199 4519 5372 6791 144 -848 -711 C ATOM 1447 O VAL A 199 185.266 17.001 537.842 1.00 45.59 O ANISOU 1447 O VAL A 199 4721 5847 6755 152 -785 -512 O ATOM 1448 CB VAL A 199 184.250 18.377 534.998 1.00 43.00 C ANISOU 1448 CB VAL A 199 4210 5334 6793 -134 -760 -947 C ATOM 1449 CG1 VAL A 199 183.387 17.173 535.341 1.00 40.79 C ANISOU 1449 CG1 VAL A 199 3990 5154 6353 -406 -601 -699 C ATOM 1450 CG2 VAL A 199 183.373 19.574 534.669 1.00 42.60 C ANISOU 1450 CG2 VAL A 199 3937 5582 6666 -61 -749 -1111 C ATOM 1451 N ILE A 200 186.855 16.931 536.252 1.00 46.84 N ANISOU 1451 N ILE A 200 5054 5342 7402 148 -866 -676 N ATOM 1452 CA ILE A 200 187.507 15.777 536.865 1.00 49.93 C ANISOU 1452 CA ILE A 200 5611 5596 7764 200 -795 -378 C ATOM 1453 C ILE A 200 188.075 16.149 538.231 1.00 46.53 C ANISOU 1453 C ILE A 200 5078 5521 7079 526 -919 -354 C ATOM 1454 O ILE A 200 187.919 15.406 539.211 1.00 39.77 O ANISOU 1454 O ILE A 200 4252 4855 6005 599 -827 -59 O ATOM 1455 CB ILE A 200 188.594 15.217 535.929 1.00 53.04 C ANISOU 1455 CB ILE A 200 6188 5485 8478 164 -783 -358 C ATOM 1456 CG1 ILE A 200 187.971 14.744 534.615 1.00 51.09 C ANISOU 1456 CG1 ILE A 200 6021 4945 8444 -197 -635 -391 C ATOM 1457 CG2 ILE A 200 189.349 14.081 536.602 1.00 58.14 C ANISOU 1457 CG2 ILE A 200 6998 5996 9094 287 -677 -12 C ATOM 1458 CD1 ILE A 200 188.974 14.191 533.627 1.00 50.70 C ANISOU 1458 CD1 ILE A 200 6153 4388 8721 -265 -605 -391 C ATOM 1459 N ILE A 201 188.727 17.310 538.320 1.00 42.67 N ANISOU 1459 N ILE A 201 4450 5155 6608 722 -1100 -676 N ATOM 1460 CA ILE A 201 189.318 17.744 539.585 1.00 48.32 C ANISOU 1460 CA ILE A 201 5019 6279 7063 1001 -1218 -737 C ATOM 1461 C ILE A 201 188.241 17.901 540.652 1.00 53.50 C ANISOU 1461 C ILE A 201 5540 7411 7378 1012 -1173 -658 C ATOM 1462 O ILE A 201 188.399 17.445 541.792 1.00 57.21 O ANISOU 1462 O ILE A 201 5962 8211 7565 1174 -1173 -449 O ATOM 1463 CB ILE A 201 190.112 19.048 539.384 1.00 47.71 C ANISOU 1463 CB ILE A 201 4803 6224 7100 1137 -1364 -1185 C ATOM 1464 CG1 ILE A 201 191.343 18.792 538.512 1.00 46.73 C ANISOU 1464 CG1 ILE A 201 4810 5669 7277 1167 -1422 -1231 C ATOM 1465 CG2 ILE A 201 190.516 19.644 540.725 1.00 53.27 C ANISOU 1465 CG2 ILE A 201 5293 7457 7491 1362 -1461 -1346 C ATOM 1466 CD1 ILE A 201 192.143 20.038 538.203 1.00 48.19 C ANISOU 1466 CD1 ILE A 201 4877 5809 7623 1272 -1523 -1686 C ATOM 1467 N MET A 202 187.125 18.543 540.298 1.00 52.04 N ANISOU 1467 N MET A 202 5278 7295 7201 860 -1124 -803 N ATOM 1468 CA MET A 202 186.038 18.717 541.256 1.00 55.95 C ANISOU 1468 CA MET A 202 5646 8230 7385 857 -1074 -733 C ATOM 1469 C MET A 202 185.410 17.384 541.640 1.00 58.20 C ANISOU 1469 C MET A 202 6055 8526 7532 737 -921 -308 C ATOM 1470 O MET A 202 184.986 17.209 542.789 1.00 60.41 O ANISOU 1470 O MET A 202 6257 9190 7506 834 -894 -151 O ATOM 1471 CB MET A 202 184.977 19.658 540.688 1.00 55.17 C ANISOU 1471 CB MET A 202 5436 8189 7337 737 -1027 -946 C ATOM 1472 CG MET A 202 185.488 21.050 540.365 1.00 53.61 C ANISOU 1472 CG MET A 202 5117 7959 7291 875 -1092 -1354 C ATOM 1473 SD MET A 202 184.199 22.121 539.701 0.55 55.08 S ANISOU 1473 SD MET A 202 5172 8228 7530 804 -968 -1510 S ATOM 1474 CE MET A 202 183.512 21.073 538.425 1.00 50.27 C ANISOU 1474 CE MET A 202 4691 7357 7054 517 -888 -1244 C ATOM 1475 N THR A 203 185.340 16.439 540.700 1.00 52.68 N ANISOU 1475 N THR A 203 5546 7407 7062 518 -788 -132 N ATOM 1476 CA THR A 203 184.793 15.124 541.017 1.00 54.24 C ANISOU 1476 CA THR A 203 5885 7540 7184 377 -564 252 C ATOM 1477 C THR A 203 185.669 14.392 542.026 1.00 61.29 C ANISOU 1477 C THR A 203 6846 8509 7933 647 -533 560 C ATOM 1478 O THR A 203 185.158 13.806 542.989 1.00 69.20 O ANISOU 1478 O THR A 203 7847 9754 8693 704 -398 849 O ATOM 1479 CB THR A 203 184.635 14.298 539.741 1.00 52.77 C ANISOU 1479 CB THR A 203 5881 6868 7303 55 -389 309 C ATOM 1480 OG1 THR A 203 183.641 14.900 538.902 1.00 49.90 O ANISOU 1480 OG1 THR A 203 5402 6573 6984 -186 -394 73 O ATOM 1481 CG2 THR A 203 184.216 12.871 540.072 1.00 54.21 C ANISOU 1481 CG2 THR A 203 6236 6901 7461 -103 -79 687 C ATOM 1482 N VAL A 204 186.989 14.421 541.831 1.00 58.98 N ANISOU 1482 N VAL A 204 6595 8044 7769 839 -646 521 N ATOM 1483 CA VAL A 204 187.886 13.761 542.776 1.00 60.16 C ANISOU 1483 CA VAL A 204 6769 8345 7746 1150 -619 837 C ATOM 1484 C VAL A 204 187.848 14.463 544.129 1.00 64.27 C ANISOU 1484 C VAL A 204 7036 9529 7857 1415 -772 767 C ATOM 1485 O VAL A 204 187.783 13.812 545.183 1.00 54.68 O ANISOU 1485 O VAL A 204 5798 8616 6362 1607 -666 1122 O ATOM 1486 CB VAL A 204 189.313 13.705 542.203 1.00 57.67 C ANISOU 1486 CB VAL A 204 6524 7739 7649 1293 -719 780 C ATOM 1487 CG1 VAL A 204 190.252 13.000 543.175 1.00 51.62 C ANISOU 1487 CG1 VAL A 204 5750 7198 6667 1655 -677 1149 C ATOM 1488 CG2 VAL A 204 189.309 13.008 540.852 1.00 52.12 C ANISOU 1488 CG2 VAL A 204 6068 6386 7348 1007 -553 830 C ATOM 1489 N LEU A 205 187.886 15.798 544.123 1.00 60.00 N ANISOU 1489 N LEU A 205 6294 9226 7277 1433 -988 309 N ATOM 1490 CA LEU A 205 187.823 16.549 545.373 1.00 58.31 C ANISOU 1490 CA LEU A 205 5820 9650 6685 1637 -1111 161 C ATOM 1491 C LEU A 205 186.562 16.205 546.155 1.00 61.29 C ANISOU 1491 C LEU A 205 6172 10313 6803 1577 -977 402 C ATOM 1492 O LEU A 205 186.626 15.912 547.355 1.00 63.57 O ANISOU 1492 O LEU A 205 6349 11066 6739 1800 -967 619 O ATOM 1493 CB LEU A 205 187.897 18.050 545.094 1.00 50.52 C ANISOU 1493 CB LEU A 205 4657 8762 5776 1597 -1270 -401 C ATOM 1494 CG LEU A 205 189.289 18.605 544.784 1.00 51.31 C ANISOU 1494 CG LEU A 205 4691 8792 6014 1730 -1421 -710 C ATOM 1495 CD1 LEU A 205 189.239 20.109 544.573 1.00 46.04 C ANISOU 1495 CD1 LEU A 205 3857 8195 5442 1678 -1489 -1269 C ATOM 1496 CD2 LEU A 205 190.263 18.253 545.898 1.00 51.19 C ANISOU 1496 CD2 LEU A 205 4526 9259 5666 2028 -1505 -580 C ATOM 1497 N TYR A 206 185.404 16.210 545.485 1.00 60.82 N ANISOU 1497 N TYR A 206 6198 10016 6894 1283 -865 376 N ATOM 1498 CA TYR A 206 184.176 15.843 546.180 1.00 53.72 C ANISOU 1498 CA TYR A 206 5278 9372 5762 1201 -722 600 C ATOM 1499 C TYR A 206 184.209 14.394 546.640 1.00 60.78 C ANISOU 1499 C TYR A 206 6341 10170 6584 1261 -492 1127 C ATOM 1500 O TYR A 206 183.646 14.068 547.690 1.00 62.51 O ANISOU 1500 O TYR A 206 6499 10749 6503 1363 -398 1371 O ATOM 1501 CB TYR A 206 182.943 16.074 545.305 1.00 60.04 C ANISOU 1501 CB TYR A 206 6113 9974 6724 865 -633 472 C ATOM 1502 CG TYR A 206 181.683 15.648 546.025 1.00 58.63 C ANISOU 1502 CG TYR A 206 5909 10065 6304 766 -476 699 C ATOM 1503 CD1 TYR A 206 181.088 16.480 546.963 1.00 62.90 C ANISOU 1503 CD1 TYR A 206 6242 11112 6547 874 -563 564 C ATOM 1504 CD2 TYR A 206 181.117 14.397 545.805 1.00 55.51 C ANISOU 1504 CD2 TYR A 206 5698 9411 5983 559 -209 1037 C ATOM 1505 CE1 TYR A 206 179.953 16.090 547.645 1.00 66.69 C ANISOU 1505 CE1 TYR A 206 6696 11844 6800 793 -423 777 C ATOM 1506 CE2 TYR A 206 179.983 13.998 546.486 1.00 65.78 C ANISOU 1506 CE2 TYR A 206 6973 10951 7068 462 -43 1234 C ATOM 1507 CZ TYR A 206 179.404 14.850 547.403 1.00 58.32 C ANISOU 1507 CZ TYR A 206 5819 10523 5818 588 -168 1114 C ATOM 1508 OH TYR A 206 178.274 14.462 548.084 1.00 85.30 O ANISOU 1508 OH TYR A 206 9210 14182 9019 495 -6 1311 O ATOM 1509 N TRP A 207 184.835 13.509 545.863 1.00 56.58 N ANISOU 1509 N TRP A 207 6028 9135 6335 1202 -359 1318 N ATOM 1510 CA TRP A 207 185.002 12.130 546.308 1.00 60.01 C ANISOU 1510 CA TRP A 207 6638 9425 6736 1305 -72 1843 C ATOM 1511 C TRP A 207 185.697 12.090 547.663 1.00 70.01 C ANISOU 1511 C TRP A 207 7749 11229 7621 1750 -146 2078 C ATOM 1512 O TRP A 207 185.260 11.389 548.587 1.00 66.80 O ANISOU 1512 O TRP A 207 7355 11047 6979 1886 59 2474 O ATOM 1513 CB TRP A 207 185.792 11.340 545.262 1.00 59.18 C ANISOU 1513 CB TRP A 207 6774 8700 7010 1217 70 1961 C ATOM 1514 CG TRP A 207 185.687 9.851 545.397 1.00 62.54 C ANISOU 1514 CG TRP A 207 7443 8793 7528 1201 493 2476 C ATOM 1515 CD1 TRP A 207 184.974 9.156 546.330 1.00 66.19 C ANISOU 1515 CD1 TRP A 207 7932 9441 7777 1264 761 2849 C ATOM 1516 CD2 TRP A 207 186.315 8.871 544.561 1.00 69.58 C ANISOU 1516 CD2 TRP A 207 8595 9070 8772 1113 748 2673 C ATOM 1517 NE1 TRP A 207 185.122 7.804 546.129 1.00 68.92 N ANISOU 1517 NE1 TRP A 207 8546 9301 8338 1227 1201 3273 N ATOM 1518 CE2 TRP A 207 185.940 7.603 545.049 1.00 76.59 C ANISOU 1518 CE2 TRP A 207 9666 9775 9661 1128 1205 3167 C ATOM 1519 CE3 TRP A 207 187.159 8.944 543.448 1.00 64.78 C ANISOU 1519 CE3 TRP A 207 8088 8034 8492 1025 660 2481 C ATOM 1520 CZ2 TRP A 207 186.380 6.418 544.462 1.00 79.17 C ANISOU 1520 CZ2 TRP A 207 10277 9485 10318 1049 1605 3463 C ATOM 1521 CZ3 TRP A 207 187.595 7.767 542.867 1.00 61.62 C ANISOU 1521 CZ3 TRP A 207 7962 7053 8400 944 1016 2770 C ATOM 1522 CH2 TRP A 207 187.205 6.521 543.375 1.00 75.95 C ANISOU 1522 CH2 TRP A 207 9959 8676 10221 953 1497 3251 C ATOM 1523 N HIS A 208 186.768 12.876 547.810 1.00 67.13 N ANISOU 1523 N HIS A 208 7211 11124 7172 1981 -428 1817 N ATOM 1524 CA HIS A 208 187.451 12.951 549.097 1.00 65.76 C ANISOU 1524 CA HIS A 208 6815 11593 6576 2395 -528 1967 C ATOM 1525 C HIS A 208 186.590 13.623 550.162 1.00 67.10 C ANISOU 1525 C HIS A 208 6751 12380 6365 2430 -614 1837 C ATOM 1526 O HIS A 208 186.715 13.298 551.347 1.00 70.91 O ANISOU 1526 O HIS A 208 7090 13398 6456 2735 -577 2130 O ATOM 1527 CB HIS A 208 188.780 13.687 548.944 1.00 64.62 C ANISOU 1527 CB HIS A 208 6508 11613 6432 2574 -801 1633 C ATOM 1528 CG HIS A 208 189.735 13.010 548.012 1.00 63.64 C ANISOU 1528 CG HIS A 208 6597 10941 6644 2593 -727 1791 C ATOM 1529 ND1 HIS A 208 190.100 11.689 548.154 1.00 66.57 N ANISOU 1529 ND1 HIS A 208 7151 11108 7036 2782 -453 2375 N ATOM 1530 CD2 HIS A 208 190.398 13.469 546.925 1.00 60.23 C ANISOU 1530 CD2 HIS A 208 6229 10106 6551 2457 -861 1453 C ATOM 1531 CE1 HIS A 208 190.947 11.363 547.194 1.00 64.94 C ANISOU 1531 CE1 HIS A 208 7113 10397 7166 2750 -431 2378 C ATOM 1532 NE2 HIS A 208 191.145 12.426 546.435 1.00 61.01 N ANISOU 1532 NE2 HIS A 208 6543 9780 6859 2550 -692 1820 N ATOM 1533 N ILE A 209 185.718 14.555 549.769 1.00 71.96 N ANISOU 1533 N ILE A 209 7311 12955 7075 2146 -712 1423 N ATOM 1534 CA ILE A 209 184.830 15.196 550.738 1.00 72.87 C ANISOU 1534 CA ILE A 209 7219 13614 6854 2159 -765 1297 C ATOM 1535 C ILE A 209 183.854 14.179 551.317 1.00 76.78 C ANISOU 1535 C ILE A 209 7828 14142 7202 2144 -500 1788 C ATOM 1536 O ILE A 209 183.760 14.004 552.537 1.00 79.94 O ANISOU 1536 O ILE A 209 8080 15084 7208 2394 -476 2014 O ATOM 1537 CB ILE A 209 184.079 16.376 550.096 1.00 72.63 C ANISOU 1537 CB ILE A 209 7128 13475 6994 1877 -869 796 C ATOM 1538 CG1 ILE A 209 185.059 17.394 549.522 1.00 69.31 C ANISOU 1538 CG1 ILE A 209 6608 12976 6751 1900 -1071 313 C ATOM 1539 CG2 ILE A 209 183.181 17.047 551.120 1.00 75.86 C ANISOU 1539 CG2 ILE A 209 7324 14435 7062 1901 -901 669 C ATOM 1540 CD1 ILE A 209 186.058 17.877 550.518 1.00 73.24 C ANISOU 1540 CD1 ILE A 209 6845 14052 6931 2188 -1232 137 C ATOM 1541 N SER A 210 183.108 13.499 550.443 1.00 79.43 N ANISOU 1541 N SER A 210 8413 13920 7846 1838 -277 1939 N ATOM 1542 CA SER A 210 182.108 12.542 550.899 1.00 83.14 C ANISOU 1542 CA SER A 210 9004 14360 8227 1759 25 2352 C ATOM 1543 C SER A 210 182.745 11.362 551.616 1.00 88.13 C ANISOU 1543 C SER A 210 9730 15030 8725 2085 259 2924 C ATOM 1544 O SER A 210 182.150 10.812 552.549 1.00 91.72 O ANISOU 1544 O SER A 210 10174 15747 8930 2206 458 3281 O ATOM 1545 CB SER A 210 181.267 12.056 549.719 1.00 76.72 C ANISOU 1545 CB SER A 210 8412 12953 7785 1319 238 2325 C ATOM 1546 OG SER A 210 182.066 11.361 548.778 1.00 78.62 O ANISOU 1546 OG SER A 210 8866 12634 8370 1256 356 2426 O ATOM 1547 N ARG A 211 183.948 10.951 551.201 1.00 91.49 N ANISOU 1547 N ARG A 211 10248 15203 9312 2256 265 3046 N ATOM 1548 CA ARG A 211 184.628 9.899 551.949 1.00101.69 C ANISOU 1548 CA ARG A 211 11595 16604 10439 2650 501 3629 C ATOM 1549 C ARG A 211 185.119 10.407 553.299 1.00109.43 C ANISOU 1549 C ARG A 211 12245 18445 10889 3088 285 3676 C ATOM 1550 O ARG A 211 185.207 9.631 554.258 1.00109.58 O ANISOU 1550 O ARG A 211 12239 18769 10627 3433 502 4203 O ATOM 1551 CB ARG A 211 185.788 9.325 551.135 1.00107.40 C ANISOU 1551 CB ARG A 211 12495 16842 11469 2733 579 3764 C ATOM 1552 CG ARG A 211 186.408 8.090 551.772 1.00119.78 C ANISOU 1552 CG ARG A 211 14168 18413 12930 3142 926 4451 C ATOM 1553 CD ARG A 211 187.373 7.380 550.841 1.00125.37 C ANISOU 1553 CD ARG A 211 15113 18506 14018 3163 1097 4621 C ATOM 1554 NE ARG A 211 187.925 6.181 551.468 1.00135.05 N ANISOU 1554 NE ARG A 211 16444 19720 15147 3593 1495 5333 N ATOM 1555 CZ ARG A 211 188.747 5.330 550.864 1.00137.71 C ANISOU 1555 CZ ARG A 211 17008 19530 15784 3698 1765 5642 C ATOM 1556 NH1 ARG A 211 189.118 5.540 549.609 1.00134.88 N ANISOU 1556 NH1 ARG A 211 16792 18622 15835 3380 1651 5275 N ATOM 1557 NH2 ARG A 211 189.198 4.266 551.516 1.00142.44 N ANISOU 1557 NH2 ARG A 211 17691 20156 16275 4143 2174 6339 N ATOM 1558 N ALA A 212 185.429 11.702 553.399 1.00117.64 N ANISOU 1558 N ALA A 212 13015 19902 11780 3079 -108 3126 N ATOM 1559 CA ALA A 212 185.845 12.265 554.680 1.00127.02 C ANISOU 1559 CA ALA A 212 13845 21973 12442 3432 -310 3071 C ATOM 1560 C ALA A 212 184.673 12.356 555.649 1.00130.62 C ANISOU 1560 C ALA A 212 14197 22849 12585 3418 -236 3170 C ATOM 1561 O ALA A 212 184.813 12.033 556.834 1.00133.12 O ANISOU 1561 O ALA A 212 14332 23785 12461 3780 -185 3507 O ATOM 1562 CB ALA A 212 186.477 13.640 554.470 1.00124.35 C ANISOU 1562 CB ALA A 212 13258 21909 12080 3365 -685 2390 C ATOM 1563 N SER A 213 183.508 12.794 555.164 1.00135.14 N ANISOU 1563 N SER A 213 14862 23129 13357 3023 -226 2895 N ATOM 1564 CA SER A 213 182.324 12.855 556.012 1.00144.19 C ANISOU 1564 CA SER A 213 15929 24622 14236 2981 -141 2991 C ATOM 1565 C SER A 213 181.811 11.471 556.386 1.00147.56 C ANISOU 1565 C SER A 213 16567 24857 14643 3076 261 3658 C ATOM 1566 O SER A 213 181.112 11.334 557.396 1.00154.79 O ANISOU 1566 O SER A 213 17381 26200 15231 3196 355 3876 O ATOM 1567 CB SER A 213 181.217 13.649 555.316 1.00148.30 C ANISOU 1567 CB SER A 213 16490 24873 14984 2545 -209 2552 C ATOM 1568 OG SER A 213 181.637 14.973 555.032 1.00151.52 O ANISOU 1568 OG SER A 213 16706 25443 15420 2482 -512 1953 O ATOM 1569 N LYS A 214 182.140 10.451 555.601 1.00133.48 N ANISOU 1569 N LYS A 214 15077 22424 13214 3021 532 3977 N ATOM 1570 CA LYS A 214 181.718 9.085 555.886 1.00129.54 C ANISOU 1570 CA LYS A 214 14810 21644 12764 3099 1006 4608 C ATOM 1571 C LYS A 214 182.703 8.389 556.820 1.00133.62 C ANISOU 1571 C LYS A 214 15247 22550 12975 3674 1141 5165 C ATOM 1572 O LYS A 214 182.415 8.182 557.999 1.00138.19 O ANISOU 1572 O LYS A 214 15677 23682 13147 3976 1235 5496 O ATOM 1573 CB LYS A 214 181.572 8.291 554.587 1.00123.31 C ANISOU 1573 CB LYS A 214 14376 19954 12523 2737 1304 4666 C ATOM 1574 CG LYS A 214 181.396 6.796 554.784 1.00124.29 C ANISOU 1574 CG LYS A 214 14771 19679 12774 2832 1880 5317 C ATOM 1575 CD LYS A 214 181.304 6.075 553.449 1.00117.60 C ANISOU 1575 CD LYS A 214 14254 17951 12480 2421 2183 5278 C ATOM 1576 CE LYS A 214 181.315 4.567 553.633 1.00116.99 C ANISOU 1576 CE LYS A 214 14461 17415 12575 2540 2828 5922 C ATOM 1577 NZ LYS A 214 180.202 4.104 554.505 1.00115.98 N ANISOU 1577 NZ LYS A 214 14348 17457 12262 2527 3152 6215 N ATOM 1578 N ALA A1001 182.241 13.025 565.610 1.00167.95 N ANISOU 1578 N ALA A1001 16976 32112 14725 4748 157 3580 N ATOM 1579 CA ALA A1001 181.822 12.083 564.579 1.00166.59 C ANISOU 1579 CA ALA A1001 17227 31222 14849 4676 304 4032 C ATOM 1580 C ALA A1001 180.401 11.589 564.834 1.00168.92 C ANISOU 1580 C ALA A1001 17686 31333 15164 4579 482 4354 C ATOM 1581 O ALA A1001 179.451 12.047 564.199 1.00164.87 O ANISOU 1581 O ALA A1001 17339 30513 14790 4218 405 4130 O ATOM 1582 CB ALA A1001 182.789 10.910 564.509 1.00168.62 C ANISOU 1582 CB ALA A1001 17570 31348 15148 5039 527 4584 C ATOM 1583 N ASP A1002 180.265 10.648 565.771 1.00177.51 N ANISOU 1583 N ASP A1002 18715 32619 16111 4908 743 4880 N ATOM 1584 CA ASP A1002 178.954 10.097 566.100 1.00184.89 C ANISOU 1584 CA ASP A1002 19812 33368 17070 4832 955 5205 C ATOM 1585 C ASP A1002 178.131 11.068 566.939 1.00192.77 C ANISOU 1585 C ASP A1002 20542 34851 17849 4693 772 4805 C ATOM 1586 O ASP A1002 176.908 11.161 566.768 1.00194.08 O ANISOU 1586 O ASP A1002 20868 34783 18091 4416 807 4778 O ATOM 1587 CB ASP A1002 179.123 8.764 566.831 1.00189.94 C ANISOU 1587 CB ASP A1002 20482 34014 17672 5256 1328 5896 C ATOM 1588 CG ASP A1002 177.800 8.143 567.230 1.00192.16 C ANISOU 1588 CG ASP A1002 20941 34075 17996 5181 1589 6227 C ATOM 1589 OD1 ASP A1002 177.034 7.742 566.329 1.00189.95 O ANISOU 1589 OD1 ASP A1002 21042 33138 17991 4851 1765 6330 O ATOM 1590 OD2 ASP A1002 177.528 8.050 568.446 1.00196.92 O ANISOU 1590 OD2 ASP A1002 21294 35172 18356 5436 1641 6371 O ATOM 1591 N LEU A1003 178.786 11.796 567.848 1.00201.50 N ANISOU 1591 N LEU A1003 21238 36635 18689 4864 608 4480 N ATOM 1592 CA LEU A1003 178.077 12.748 568.698 1.00199.97 C ANISOU 1592 CA LEU A1003 20775 36902 18305 4736 472 4084 C ATOM 1593 C LEU A1003 177.389 13.824 567.870 1.00194.41 C ANISOU 1593 C LEU A1003 20190 35895 17782 4274 275 3539 C ATOM 1594 O LEU A1003 176.248 14.207 568.158 1.00197.42 O ANISOU 1594 O LEU A1003 20568 36296 18148 4083 264 3422 O ATOM 1595 CB LEU A1003 179.049 13.383 569.693 1.00206.44 C ANISOU 1595 CB LEU A1003 21135 38479 18823 4955 373 3774 C ATOM 1596 CG LEU A1003 179.868 12.426 570.560 1.00214.94 C ANISOU 1596 CG LEU A1003 22006 39988 19673 5455 565 4273 C ATOM 1597 CD1 LEU A1003 180.872 13.191 571.408 1.00217.15 C ANISOU 1597 CD1 LEU A1003 21810 41060 19636 5601 459 3869 C ATOM 1598 CD2 LEU A1003 178.951 11.593 571.434 1.00221.16 C ANISOU 1598 CD2 LEU A1003 22796 40874 20362 5671 781 4796 C ATOM 1599 N GLU A1004 178.068 14.322 566.834 1.00179.13 N ANISOU 1599 N GLU A1004 18355 33677 16030 4105 132 3210 N ATOM 1600 CA GLU A1004 177.474 15.347 565.982 1.00165.84 C ANISOU 1600 CA GLU A1004 16775 31693 14545 3705 -26 2708 C ATOM 1601 C GLU A1004 176.267 14.803 565.227 1.00156.59 C ANISOU 1601 C GLU A1004 15940 30004 13554 3475 82 2991 C ATOM 1602 O GLU A1004 175.286 15.525 565.010 1.00152.37 O ANISOU 1602 O GLU A1004 15419 29387 13086 3192 21 2695 O ATOM 1603 CB GLU A1004 178.521 15.889 565.010 1.00161.16 C ANISOU 1603 CB GLU A1004 16227 30879 14126 3610 -177 2343 C ATOM 1604 CG GLU A1004 179.887 16.128 565.638 1.00161.17 C ANISOU 1604 CG GLU A1004 15944 31349 13946 3853 -223 2164 C ATOM 1605 CD GLU A1004 179.842 17.109 566.795 1.00161.95 C ANISOU 1605 CD GLU A1004 15662 32069 13801 3858 -261 1733 C ATOM 1606 OE1 GLU A1004 179.038 18.064 566.741 1.00159.49 O ANISOU 1606 OE1 GLU A1004 15325 31705 13568 3592 -319 1333 O ATOM 1607 OE2 GLU A1004 180.610 16.922 567.762 1.00166.09 O ANISOU 1607 OE2 GLU A1004 15897 33157 14052 4134 -211 1802 O ATOM 1608 N ASP A1005 176.320 13.531 564.824 1.00151.93 N ANISOU 1608 N ASP A1005 15617 29058 13049 3583 289 3562 N ATOM 1609 CA ASP A1005 175.180 12.926 564.143 1.00145.30 C ANISOU 1609 CA ASP A1005 15100 27738 12369 3326 477 3835 C ATOM 1610 C ASP A1005 173.994 12.768 565.087 1.00145.36 C ANISOU 1610 C ASP A1005 15045 27948 12236 3311 601 3984 C ATOM 1611 O ASP A1005 172.851 13.052 564.707 1.00148.41 O ANISOU 1611 O ASP A1005 15533 28155 12700 2991 621 3850 O ATOM 1612 CB ASP A1005 175.578 11.575 563.548 1.00143.30 C ANISOU 1612 CB ASP A1005 15160 27007 12280 3429 769 4402 C ATOM 1613 CG ASP A1005 176.677 11.695 562.511 1.00137.82 C ANISOU 1613 CG ASP A1005 14559 26054 11752 3419 649 4275 C ATOM 1614 OD1 ASP A1005 177.250 12.797 562.375 1.00134.96 O ANISOU 1614 OD1 ASP A1005 13992 25928 11359 3380 334 3747 O ATOM 1615 OD2 ASP A1005 176.966 10.689 561.830 1.00136.91 O ANISOU 1615 OD2 ASP A1005 14731 25456 11834 3435 906 4686 O ATOM 1616 N ASN A1006 174.243 12.321 566.320 1.00146.11 N ANISOU 1616 N ASN A1006 14953 28440 12121 3660 690 4259 N ATOM 1617 CA ASN A1006 173.153 12.162 567.279 1.00150.19 C ANISOU 1617 CA ASN A1006 15399 29167 12499 3674 799 4410 C ATOM 1618 C ASN A1006 172.523 13.506 567.627 1.00150.20 C ANISOU 1618 C ASN A1006 15162 29497 12411 3463 557 3845 C ATOM 1619 O ASN A1006 171.295 13.657 567.600 1.00151.59 O ANISOU 1619 O ASN A1006 15420 29555 12624 3222 601 3803 O ATOM 1620 CB ASN A1006 173.660 11.462 568.541 1.00155.71 C ANISOU 1620 CB ASN A1006 15903 30280 12979 4133 937 4809 C ATOM 1621 CG ASN A1006 174.028 10.013 568.297 1.00159.11 C ANISOU 1621 CG ASN A1006 16606 30305 13546 4357 1281 5448 C ATOM 1622 OD1 ASN A1006 175.168 9.606 568.514 1.00163.88 O ANISOU 1622 OD1 ASN A1006 17105 31063 14097 4703 1324 5652 O ATOM 1623 ND2 ASN A1006 173.060 9.225 567.844 1.00157.15 N ANISOU 1623 ND2 ASN A1006 16703 29516 13492 4145 1573 5751 N ATOM 1624 N TRP A1007 173.354 14.500 567.953 1.00149.13 N ANISOU 1624 N TRP A1007 14731 29756 12177 3539 339 3395 N ATOM 1625 CA TRP A1007 172.829 15.807 568.336 1.00144.85 C ANISOU 1625 CA TRP A1007 13961 29491 11583 3351 179 2851 C ATOM 1626 C TRP A1007 172.105 16.475 567.173 1.00145.94 C ANISOU 1626 C TRP A1007 14290 29193 11968 2964 108 2536 C ATOM 1627 O TRP A1007 171.012 17.032 567.348 1.00149.05 O ANISOU 1627 O TRP A1007 14649 29612 12372 2774 102 2363 O ATOM 1628 CB TRP A1007 173.966 16.691 568.849 1.00139.59 C ANISOU 1628 CB TRP A1007 12964 29286 10789 3481 39 2417 C ATOM 1629 CG TRP A1007 173.503 17.963 569.484 1.00138.19 C ANISOU 1629 CG TRP A1007 12522 29450 10535 3338 -48 1901 C ATOM 1630 CD1 TRP A1007 173.649 19.226 568.992 1.00136.72 C ANISOU 1630 CD1 TRP A1007 12268 29194 10484 3109 -155 1312 C ATOM 1631 CD2 TRP A1007 172.811 18.095 570.731 1.00140.07 C ANISOU 1631 CD2 TRP A1007 12531 30134 10556 3423 -6 1939 C ATOM 1632 NE1 TRP A1007 173.094 20.138 569.857 1.00138.92 N ANISOU 1632 NE1 TRP A1007 12292 29842 10650 3044 -165 986 N ATOM 1633 CE2 TRP A1007 172.572 19.468 570.933 1.00139.10 C ANISOU 1633 CE2 TRP A1007 12208 30195 10450 3226 -90 1354 C ATOM 1634 CE3 TRP A1007 172.371 17.185 571.697 1.00141.68 C ANISOU 1634 CE3 TRP A1007 12681 30589 10563 3657 113 2417 C ATOM 1635 CZ2 TRP A1007 171.913 19.954 572.060 1.00138.03 C ANISOU 1635 CZ2 TRP A1007 11817 30495 10134 3241 -75 1230 C ATOM 1636 CZ3 TRP A1007 171.717 17.668 572.815 1.00143.28 C ANISOU 1636 CZ3 TRP A1007 12626 31233 10580 3677 112 2289 C ATOM 1637 CH2 TRP A1007 171.495 19.040 572.988 1.00141.24 C ANISOU 1637 CH2 TRP A1007 12169 31159 10336 3463 11 1697 C ATOM 1638 N GLU A1008 172.697 16.426 565.977 1.00147.09 N ANISOU 1638 N GLU A1008 14624 28953 12311 2860 63 2469 N ATOM 1639 CA GLU A1008 172.044 16.990 564.800 1.00139.65 C ANISOU 1639 CA GLU A1008 13847 27617 11599 2519 15 2207 C ATOM 1640 C GLU A1008 170.712 16.303 564.528 1.00131.57 C ANISOU 1640 C GLU A1008 13033 26337 10619 2324 185 2530 C ATOM 1641 O GLU A1008 169.725 16.960 564.175 1.00128.89 O ANISOU 1641 O GLU A1008 12690 25916 10364 2072 163 2289 O ATOM 1642 CB GLU A1008 172.967 16.876 563.586 1.00144.02 C ANISOU 1642 CB GLU A1008 14568 27812 12342 2472 -48 2151 C ATOM 1643 CG GLU A1008 172.384 17.434 562.299 1.00146.80 C ANISOU 1643 CG GLU A1008 15065 27784 12926 2146 -91 1891 C ATOM 1644 CD GLU A1008 173.306 17.238 561.112 1.00147.83 C ANISOU 1644 CD GLU A1008 15361 27567 13240 2112 -155 1868 C ATOM 1645 OE1 GLU A1008 174.347 16.567 561.270 1.00151.99 O ANISOU 1645 OE1 GLU A1008 15919 28109 13722 2339 -148 2105 O ATOM 1646 OE2 GLU A1008 172.991 17.756 560.020 1.00146.84 O ANISOU 1646 OE2 GLU A1008 15321 27165 13308 1876 -207 1624 O ATOM 1647 N THR A1009 170.665 14.978 564.690 1.00125.04 N ANISOU 1647 N THR A1009 12387 25372 9751 2436 398 3076 N ATOM 1648 CA THR A1009 169.413 14.249 564.517 1.00120.07 C ANISOU 1648 CA THR A1009 11958 24490 9173 2225 630 3370 C ATOM 1649 C THR A1009 168.363 14.721 565.517 1.00120.07 C ANISOU 1649 C THR A1009 11780 24811 9031 2206 604 3266 C ATOM 1650 O THR A1009 167.208 14.977 565.152 1.00120.24 O ANISOU 1650 O THR A1009 11853 24704 9129 1920 644 3151 O ATOM 1651 CB THR A1009 169.663 12.747 564.662 1.00123.28 C ANISOU 1651 CB THR A1009 12587 24659 9594 2383 942 3971 C ATOM 1652 OG1 THR A1009 170.499 12.293 563.589 1.00128.22 O ANISOU 1652 OG1 THR A1009 13412 24903 10401 2344 1011 4074 O ATOM 1653 CG2 THR A1009 168.353 11.978 564.638 1.00119.44 C ANISOU 1653 CG2 THR A1009 12291 23911 9178 2146 1245 4236 C ATOM 1654 N LEU A1010 168.755 14.854 566.787 1.00122.83 N ANISOU 1654 N LEU A1010 11894 25606 9169 2508 542 3297 N ATOM 1655 CA LEU A1010 167.815 15.282 567.819 1.00123.16 C ANISOU 1655 CA LEU A1010 11754 25977 9064 2511 525 3213 C ATOM 1656 C LEU A1010 167.257 16.668 567.517 1.00118.35 C ANISOU 1656 C LEU A1010 11007 25424 8535 2271 355 2674 C ATOM 1657 O LEU A1010 166.037 16.877 567.534 1.00121.25 O ANISOU 1657 O LEU A1010 11398 25741 8931 2074 399 2635 O ATOM 1658 CB LEU A1010 168.499 15.256 569.188 1.00126.34 C ANISOU 1658 CB LEU A1010 11881 26903 9217 2882 488 3296 C ATOM 1659 CG LEU A1010 167.681 15.628 570.429 1.00111.92 C ANISOU 1659 CG LEU A1010 9833 25490 7203 2941 479 3244 C ATOM 1660 CD1 LEU A1010 168.098 14.764 571.604 1.00122.75 C ANISOU 1660 CD1 LEU A1010 11081 27212 8348 3326 596 3666 C ATOM 1661 CD2 LEU A1010 167.844 17.100 570.782 1.00110.80 C ANISOU 1661 CD2 LEU A1010 9388 25694 7015 2876 281 2659 C ATOM 1662 N ASN A1011 168.139 17.632 567.237 1.00115.92 N ANISOU 1662 N ASN A1011 10557 25207 8279 2291 189 2256 N ATOM 1663 CA ASN A1011 167.677 18.993 566.976 1.00116.56 C ANISOU 1663 CA ASN A1011 10512 25314 8462 2101 88 1756 C ATOM 1664 C ASN A1011 166.811 19.055 565.723 1.00115.72 C ANISOU 1664 C ASN A1011 10610 24785 8573 1804 130 1729 C ATOM 1665 O ASN A1011 165.761 19.712 565.718 1.00114.83 O ANISOU 1665 O ASN A1011 10437 24687 8505 1648 139 1562 O ATOM 1666 CB ASN A1011 168.871 19.939 566.856 1.00120.19 C ANISOU 1666 CB ASN A1011 10809 25898 8959 2174 -37 1320 C ATOM 1667 CG ASN A1011 169.658 20.051 568.149 1.00126.70 C ANISOU 1667 CG ASN A1011 11356 27240 9545 2432 -67 1259 C ATOM 1668 OD1 ASN A1011 169.690 19.119 568.952 1.00128.62 O ANISOU 1668 OD1 ASN A1011 11572 27694 9603 2635 -2 1655 O ATOM 1669 ND2 ASN A1011 170.294 21.198 568.358 1.00128.05 N ANISOU 1669 ND2 ASN A1011 11302 27635 9715 2428 -140 759 N ATOM 1670 N ASP A1012 167.228 18.370 564.655 1.00115.86 N ANISOU 1670 N ASP A1012 10851 24450 8721 1725 168 1899 N ATOM 1671 CA ASP A1012 166.447 18.369 563.421 1.00110.88 C ANISOU 1671 CA ASP A1012 10382 23467 8281 1428 226 1869 C ATOM 1672 C ASP A1012 165.050 17.809 563.655 1.00112.87 C ANISOU 1672 C ASP A1012 10697 23693 8493 1264 378 2111 C ATOM 1673 O ASP A1012 164.055 18.379 563.192 1.00109.64 O ANISOU 1673 O ASP A1012 10250 23227 8179 1056 381 1936 O ATOM 1674 CB ASP A1012 167.172 17.571 562.337 1.00110.17 C ANISOU 1674 CB ASP A1012 10516 23034 8310 1368 278 2051 C ATOM 1675 CG ASP A1012 168.378 18.303 561.783 1.00112.91 C ANISOU 1675 CG ASP A1012 10813 23333 8756 1456 109 1727 C ATOM 1676 OD1 ASP A1012 168.413 19.548 561.877 1.00113.94 O ANISOU 1676 OD1 ASP A1012 10765 23592 8933 1464 -2 1305 O ATOM 1677 OD2 ASP A1012 169.288 17.633 561.250 1.00114.68 O ANISOU 1677 OD2 ASP A1012 11182 23367 9025 1514 118 1898 O ATOM 1678 N ASN A1013 164.954 16.691 564.380 1.00117.71 N ANISOU 1678 N ASN A1013 11402 24348 8975 1368 525 2521 N ATOM 1679 CA ASN A1013 163.639 16.128 564.668 1.00117.37 C ANISOU 1679 CA ASN A1013 11427 24269 8900 1206 696 2734 C ATOM 1680 C ASN A1013 162.823 17.042 565.574 1.00116.60 C ANISOU 1680 C ASN A1013 11105 24499 8699 1242 592 2522 C ATOM 1681 O ASN A1013 161.591 17.071 565.470 1.00114.66 O ANISOU 1681 O ASN A1013 10869 24211 8484 1037 664 2520 O ATOM 1682 CB ASN A1013 163.781 14.740 565.290 1.00120.46 C ANISOU 1682 CB ASN A1013 11978 24595 9196 1342 930 3230 C ATOM 1683 CG ASN A1013 164.222 13.697 564.283 1.00117.26 C ANISOU 1683 CG ASN A1013 11841 23758 8955 1211 1151 3482 C ATOM 1684 OD1 ASN A1013 163.397 13.004 563.687 1.00113.24 O ANISOU 1684 OD1 ASN A1013 11500 22949 8575 908 1398 3604 O ATOM 1685 ND2 ASN A1013 165.528 13.586 564.080 1.00119.64 N ANISOU 1685 ND2 ASN A1013 12169 24019 9269 1419 1085 3534 N ATOM 1686 N LEU A1014 163.482 17.794 566.459 1.00119.92 N ANISOU 1686 N LEU A1014 11310 25254 8999 1486 444 2329 N ATOM 1687 CA LEU A1014 162.772 18.797 567.247 1.00121.67 C ANISOU 1687 CA LEU A1014 11311 25770 9149 1497 369 2076 C ATOM 1688 C LEU A1014 162.144 19.848 566.339 1.00123.93 C ANISOU 1688 C LEU A1014 11561 25906 9621 1281 319 1737 C ATOM 1689 O LEU A1014 160.970 20.210 566.501 1.00124.34 O ANISOU 1689 O LEU A1014 11556 26009 9679 1164 349 1695 O ATOM 1690 CB LEU A1014 163.726 19.440 568.257 1.00121.98 C ANISOU 1690 CB LEU A1014 11108 26197 9040 1756 257 1872 C ATOM 1691 CG LEU A1014 163.154 20.358 569.344 1.00124.05 C ANISOU 1691 CG LEU A1014 11120 26835 9179 1805 215 1643 C ATOM 1692 CD1 LEU A1014 164.010 20.279 570.598 1.00125.32 C ANISOU 1692 CD1 LEU A1014 11066 27441 9109 2081 178 1661 C ATOM 1693 CD2 LEU A1014 163.060 21.802 568.867 1.00123.13 C ANISOU 1693 CD2 LEU A1014 10887 26693 9203 1686 145 1164 C ATOM 1694 N LYS A1015 162.915 20.346 565.367 1.00130.24 N ANISOU 1694 N LYS A1015 12389 26524 10574 1248 252 1508 N ATOM 1695 CA LYS A1015 162.365 21.303 564.412 1.00133.15 C ANISOU 1695 CA LYS A1015 12727 26736 11128 1084 233 1232 C ATOM 1696 C LYS A1015 161.242 20.687 563.588 1.00130.55 C ANISOU 1696 C LYS A1015 12528 26184 10890 835 332 1428 C ATOM 1697 O LYS A1015 160.295 21.386 563.210 1.00129.48 O ANISOU 1697 O LYS A1015 12314 26043 10840 723 338 1290 O ATOM 1698 CB LYS A1015 163.469 21.828 563.492 1.00138.86 C ANISOU 1698 CB LYS A1015 13475 27287 11999 1110 164 985 C ATOM 1699 CG LYS A1015 164.725 22.287 564.215 1.00146.92 C ANISOU 1699 CG LYS A1015 14370 28521 12931 1326 79 772 C ATOM 1700 CD LYS A1015 164.416 23.319 565.286 1.00152.27 C ANISOU 1700 CD LYS A1015 14813 29539 13505 1410 63 508 C ATOM 1701 CE LYS A1015 165.669 23.689 566.063 1.00155.92 C ANISOU 1701 CE LYS A1015 15110 30277 13855 1591 -4 275 C ATOM 1702 NZ LYS A1015 166.288 22.501 566.714 1.00158.25 N ANISOU 1702 NZ LYS A1015 15437 30716 13976 1747 -14 615 N ATOM 1703 N VAL A1016 161.329 19.386 563.299 1.00117.72 N ANISOU 1703 N VAL A1016 11094 24386 9249 743 433 1745 N ATOM 1704 CA VAL A1016 160.255 18.715 562.573 1.00113.03 C ANISOU 1704 CA VAL A1016 10608 23606 8730 459 566 1895 C ATOM 1705 C VAL A1016 158.983 18.681 563.411 1.00119.24 C ANISOU 1705 C VAL A1016 11318 24578 9409 414 621 1980 C ATOM 1706 O VAL A1016 157.880 18.907 562.899 1.00120.24 O ANISOU 1706 O VAL A1016 11400 24679 9609 216 650 1910 O ATOM 1707 CB VAL A1016 160.696 17.300 562.153 1.00106.93 C ANISOU 1707 CB VAL A1016 10071 22584 7974 355 735 2203 C ATOM 1708 CG1 VAL A1016 159.518 16.516 561.596 1.00103.77 C ANISOU 1708 CG1 VAL A1016 9767 22021 7642 22 933 2327 C ATOM 1709 CG2 VAL A1016 161.814 17.379 561.127 1.00105.96 C ANISOU 1709 CG2 VAL A1016 10024 22253 7984 355 681 2101 C ATOM 1710 N ILE A1017 159.114 18.402 564.711 1.00126.16 N ANISOU 1710 N ILE A1017 12163 25668 10105 609 633 2135 N ATOM 1711 CA ILE A1017 157.946 18.406 565.589 1.00131.97 C ANISOU 1711 CA ILE A1017 12821 26594 10728 587 679 2212 C ATOM 1712 C ILE A1017 157.348 19.803 565.671 1.00138.86 C ANISOU 1712 C ILE A1017 13483 27636 11642 603 558 1898 C ATOM 1713 O ILE A1017 156.122 19.969 565.697 1.00141.64 O ANISOU 1713 O ILE A1017 13782 28037 11997 473 593 1897 O ATOM 1714 CB ILE A1017 158.319 17.869 566.984 1.00133.84 C ANISOU 1714 CB ILE A1017 13044 27054 10756 832 714 2442 C ATOM 1715 CG1 ILE A1017 158.817 16.428 566.887 1.00136.18 C ANISOU 1715 CG1 ILE A1017 13572 27141 11028 842 902 2820 C ATOM 1716 CG2 ILE A1017 157.125 17.943 567.922 1.00135.00 C ANISOU 1716 CG2 ILE A1017 13101 27409 10784 818 754 2505 C ATOM 1717 CD1 ILE A1017 159.306 15.865 568.200 1.00139.34 C ANISOU 1717 CD1 ILE A1017 13949 27767 11227 1147 950 3096 C ATOM 1718 N GLU A1018 158.200 20.831 565.707 1.00147.47 N ANISOU 1718 N GLU A1018 14454 28811 12767 763 439 1627 N ATOM 1719 CA GLU A1018 157.691 22.196 565.805 1.00153.99 C ANISOU 1719 CA GLU A1018 15102 29768 13639 796 380 1339 C ATOM 1720 C GLU A1018 156.903 22.601 564.564 1.00155.14 C ANISOU 1720 C GLU A1018 15260 29723 13963 619 398 1260 C ATOM 1721 O GLU A1018 155.924 23.349 564.672 1.00158.56 O ANISOU 1721 O GLU A1018 15583 30255 14407 605 400 1176 O ATOM 1722 CB GLU A1018 158.844 23.171 566.046 1.00158.88 C ANISOU 1722 CB GLU A1018 15611 30492 14263 977 297 1037 C ATOM 1723 CG GLU A1018 158.401 24.610 566.263 1.00162.43 C ANISOU 1723 CG GLU A1018 15901 31072 14743 1023 277 734 C ATOM 1724 CD GLU A1018 159.553 25.531 566.610 1.00165.53 C ANISOU 1724 CD GLU A1018 16186 31589 15119 1167 221 395 C ATOM 1725 OE1 GLU A1018 160.681 25.029 566.799 1.00166.94 O ANISOU 1725 OE1 GLU A1018 16378 31806 15245 1250 181 405 O ATOM 1726 OE2 GLU A1018 159.330 26.757 566.696 1.00166.64 O ANISOU 1726 OE2 GLU A1018 16236 31786 15294 1192 227 113 O ATOM 1727 N LYS A1019 157.300 22.117 563.386 1.00154.86 N ANISOU 1727 N LYS A1019 15347 29436 14058 495 413 1298 N ATOM 1728 CA LYS A1019 156.678 22.507 562.126 1.00149.28 C ANISOU 1728 CA LYS A1019 14622 28584 13514 350 419 1216 C ATOM 1729 C LYS A1019 155.860 21.379 561.502 1.00147.10 C ANISOU 1729 C LYS A1019 14441 28201 13250 80 504 1417 C ATOM 1730 O LYS A1019 155.673 21.344 560.284 1.00152.25 O ANISOU 1730 O LYS A1019 15104 28713 14031 -72 509 1368 O ATOM 1731 CB LYS A1019 157.737 22.991 561.136 1.00148.25 C ANISOU 1731 CB LYS A1019 14526 28269 13534 403 373 1040 C ATOM 1732 CG LYS A1019 158.508 24.218 561.589 1.00150.06 C ANISOU 1732 CG LYS A1019 14663 28584 13769 631 316 771 C ATOM 1733 CD LYS A1019 159.490 24.666 560.518 1.00150.26 C ANISOU 1733 CD LYS A1019 14740 28398 13955 668 289 594 C ATOM 1734 CE LYS A1019 160.234 25.925 560.933 1.00151.43 C ANISOU 1734 CE LYS A1019 14812 28611 14114 863 260 276 C ATOM 1735 NZ LYS A1019 161.165 26.390 559.867 1.00150.18 N ANISOU 1735 NZ LYS A1019 14721 28217 14122 901 248 90 N ATOM 1736 N ALA A1020 155.365 20.453 562.318 1.00143.87 N ANISOU 1736 N ALA A1020 14094 27865 12704 10 588 1627 N ATOM 1737 CA ALA A1020 154.606 19.326 561.799 1.00138.82 C ANISOU 1737 CA ALA A1020 13560 27115 12069 -278 721 1786 C ATOM 1738 C ALA A1020 153.202 19.753 561.385 1.00135.43 C ANISOU 1738 C ALA A1020 12990 26804 11664 -423 706 1704 C ATOM 1739 O ALA A1020 152.621 20.688 561.944 1.00135.57 O ANISOU 1739 O ALA A1020 12856 27014 11640 -279 632 1627 O ATOM 1740 CB ALA A1020 154.525 18.209 562.840 1.00137.45 C ANISOU 1740 CB ALA A1020 13519 26961 11745 -285 863 2050 C ATOM 1741 N ASP A1021 152.658 19.050 560.392 1.00132.81 N ANISOU 1741 N ASP A1021 12702 26368 11392 -713 789 1714 N ATOM 1742 CA ASP A1021 151.328 19.323 559.861 1.00131.37 C ANISOU 1742 CA ASP A1021 12370 26333 11210 -868 767 1636 C ATOM 1743 C ASP A1021 150.275 18.335 560.344 1.00128.66 C ANISOU 1743 C ASP A1021 12071 26058 10754 -1099 920 1756 C ATOM 1744 O ASP A1021 149.125 18.723 560.565 1.00126.01 O ANISOU 1744 O ASP A1021 11589 25939 10350 -1120 882 1728 O ATOM 1745 CB ASP A1021 151.357 19.315 558.329 1.00130.05 C ANISOU 1745 CB ASP A1021 12173 26071 11169 -1041 739 1508 C ATOM 1746 CG ASP A1021 152.295 20.358 557.756 1.00124.83 C ANISOU 1746 CG ASP A1021 11466 25333 10630 -809 607 1387 C ATOM 1747 OD1 ASP A1021 152.456 21.425 558.384 1.00123.71 O ANISOU 1747 OD1 ASP A1021 11242 25282 10481 -529 527 1342 O ATOM 1748 OD2 ASP A1021 152.872 20.111 556.676 1.00122.17 O ANISOU 1748 OD2 ASP A1021 11184 24835 10401 -915 608 1322 O ATOM 1749 N ASN A1022 150.640 17.063 560.511 1.00130.10 N ANISOU 1749 N ASN A1022 12461 26045 10924 -1267 1124 1896 N ATOM 1750 CA ASN A1022 149.681 16.046 560.928 1.00129.74 C ANISOU 1750 CA ASN A1022 12490 26007 10800 -1507 1341 2003 C ATOM 1751 C ASN A1022 150.184 15.284 562.148 1.00131.86 C ANISOU 1751 C ASN A1022 12946 26173 10982 -1381 1513 2260 C ATOM 1752 O ASN A1022 151.187 15.666 562.758 1.00129.82 O ANISOU 1752 O ASN A1022 12716 25922 10689 -1082 1410 2340 O ATOM 1753 CB ASN A1022 149.393 15.080 559.777 1.00132.20 C ANISOU 1753 CB ASN A1022 12875 26139 11214 -1905 1531 1914 C ATOM 1754 CG ASN A1022 150.623 14.310 559.338 1.00133.77 C ANISOU 1754 CG ASN A1022 13289 25995 11544 -1964 1688 1984 C ATOM 1755 OD1 ASN A1022 151.749 14.789 559.471 1.00135.29 O ANISOU 1755 OD1 ASN A1022 13515 26129 11758 -1700 1556 2032 O ATOM 1756 ND2 ASN A1022 150.413 13.110 558.810 1.00135.92 N ANISOU 1756 ND2 ASN A1022 13701 26026 11917 -2317 1994 1978 N ATOM 1757 N ALA A1023 149.490 14.207 562.510 1.00187.24 N ANISOU 1757 N ALA A1023 21077 33893 16173 -234 -5874 2514 N ATOM 1758 CA ALA A1023 149.824 13.417 563.686 1.00182.08 C ANISOU 1758 CA ALA A1023 20507 32788 15887 -515 -5879 2253 C ATOM 1759 C ALA A1023 150.885 12.357 563.419 1.00178.41 C ANISOU 1759 C ALA A1023 20441 32038 15311 -982 -5894 1839 C ATOM 1760 O ALA A1023 151.251 11.623 564.343 1.00177.25 O ANISOU 1760 O ALA A1023 20382 31531 15433 -1232 -5886 1636 O ATOM 1761 CB ALA A1023 148.564 12.748 564.246 1.00182.02 C ANISOU 1761 CB ALA A1023 20129 33119 15912 -878 -6000 2136 C ATOM 1762 N ALA A1024 151.386 12.254 562.189 1.00181.10 N ANISOU 1762 N ALA A1024 21029 32537 15244 -1113 -5894 1722 N ATOM 1763 CA ALA A1024 152.405 11.261 561.870 1.00184.94 C ANISOU 1763 CA ALA A1024 21930 32757 15583 -1592 -5860 1317 C ATOM 1764 C ALA A1024 153.819 11.801 562.047 1.00185.74 C ANISOU 1764 C ALA A1024 22376 32326 15871 -1205 -5710 1434 C ATOM 1765 O ALA A1024 154.679 11.110 562.604 1.00185.75 O ANISOU 1765 O ALA A1024 22654 31745 16177 -1408 -5571 1188 O ATOM 1766 CB ALA A1024 152.217 10.754 560.438 1.00192.57 C ANISOU 1766 CB ALA A1024 23019 34176 15973 -2041 -5902 1054 C ATOM 1767 N GLN A1025 154.073 13.029 561.589 1.00189.43 N ANISOU 1767 N GLN A1025 22866 32806 16302 -612 -5612 1789 N ATOM 1768 CA GLN A1025 155.416 13.593 561.676 1.00180.77 C ANISOU 1768 CA GLN A1025 22104 31171 15409 -239 -5388 1869 C ATOM 1769 C GLN A1025 155.840 13.828 563.121 1.00168.99 C ANISOU 1769 C GLN A1025 20559 29072 14577 23 -5238 1933 C ATOM 1770 O GLN A1025 157.026 13.691 563.446 1.00166.24 O ANISOU 1770 O GLN A1025 20538 27968 14659 83 -4958 1748 O ATOM 1771 CB GLN A1025 155.485 14.896 560.880 1.00184.80 C ANISOU 1771 CB GLN A1025 22632 31904 15678 336 -5285 2266 C ATOM 1772 CG GLN A1025 155.247 14.719 559.387 1.00192.46 C ANISOU 1772 CG GLN A1025 23731 33316 16078 123 -5343 2184 C ATOM 1773 CD GLN A1025 154.993 16.032 558.673 1.00195.94 C ANISOU 1773 CD GLN A1025 24114 33977 16357 726 -5210 2644 C ATOM 1774 OE1 GLN A1025 155.750 16.428 557.786 1.00198.72 O ANISOU 1774 OE1 GLN A1025 24791 34278 16435 917 -5057 2705 O ATOM 1775 NE2 GLN A1025 153.918 16.713 559.052 1.00196.36 N ANISOU 1775 NE2 GLN A1025 23766 34279 16564 1031 -5230 2981 N ATOM 1776 N VAL A1026 154.891 14.170 563.998 1.00165.28 N ANISOU 1776 N VAL A1026 19676 28908 14216 168 -5391 2175 N ATOM 1777 CA VAL A1026 155.227 14.439 565.394 1.00158.38 C ANISOU 1777 CA VAL A1026 18717 27590 13871 391 -5279 2252 C ATOM 1778 C VAL A1026 155.801 13.191 566.055 1.00155.30 C ANISOU 1778 C VAL A1026 18519 26666 13821 -36 -5219 1866 C ATOM 1779 O VAL A1026 156.857 13.238 566.696 1.00150.15 O ANISOU 1779 O VAL A1026 18065 25372 13613 118 -4979 1783 O ATOM 1780 CB VAL A1026 153.995 14.968 566.154 1.00155.65 C ANISOU 1780 CB VAL A1026 17982 27434 13724 569 -5308 2485 C ATOM 1781 CG1 VAL A1026 153.790 16.446 565.868 1.00155.08 C ANISOU 1781 CG1 VAL A1026 17833 27441 13648 1153 -5109 2884 C ATOM 1782 CG2 VAL A1026 152.750 14.184 565.774 1.00159.64 C ANISOU 1782 CG2 VAL A1026 18270 28397 13989 146 -5512 2346 C ATOM 1783 N LYS A1027 155.123 12.053 565.897 1.00163.63 N ANISOU 1783 N LYS A1027 19512 28002 14659 -580 -5402 1632 N ATOM 1784 CA LYS A1027 155.599 10.821 566.515 1.00169.98 C ANISOU 1784 CA LYS A1027 20523 28274 15786 -961 -5273 1308 C ATOM 1785 C LYS A1027 156.803 10.254 565.773 1.00176.25 C ANISOU 1785 C LYS A1027 21808 28505 16655 -1102 -4993 1019 C ATOM 1786 O LYS A1027 157.734 9.737 566.402 1.00175.98 O ANISOU 1786 O LYS A1027 21987 27823 17053 -1079 -4755 900 O ATOM 1787 CB LYS A1027 154.472 9.790 566.576 1.00176.74 C ANISOU 1787 CB LYS A1027 21192 29561 16399 -1533 -5467 1120 C ATOM 1788 CG LYS A1027 154.820 8.549 567.381 1.00179.01 C ANISOU 1788 CG LYS A1027 21677 29283 17055 -1874 -5274 856 C ATOM 1789 CD LYS A1027 153.615 7.638 567.552 1.00185.38 C ANISOU 1789 CD LYS A1027 22277 30512 17647 -2438 -5419 675 C ATOM 1790 CE LYS A1027 153.951 6.448 568.437 1.00185.84 C ANISOU 1790 CE LYS A1027 22558 29948 18107 -2708 -5154 472 C ATOM 1791 NZ LYS A1027 152.771 5.567 568.655 1.00190.03 N ANISOU 1791 NZ LYS A1027 22908 30841 18456 -3286 -5231 270 N ATOM 1792 N ASP A1028 156.800 10.342 564.438 1.00185.27 N ANISOU 1792 N ASP A1028 23117 29913 17366 -1230 -5005 927 N ATOM 1793 CA ASP A1028 157.937 9.855 563.662 1.00187.80 C ANISOU 1793 CA ASP A1028 23919 29692 17746 -1360 -4706 651 C ATOM 1794 C ASP A1028 159.221 10.574 564.051 1.00175.69 C ANISOU 1794 C ASP A1028 22551 27542 16663 -846 -4448 775 C ATOM 1795 O ASP A1028 160.299 9.967 564.076 1.00175.63 O ANISOU 1795 O ASP A1028 22862 26905 16964 -905 -4158 572 O ATOM 1796 CB ASP A1028 157.665 10.015 562.166 1.00197.25 C ANISOU 1796 CB ASP A1028 25237 31361 18348 -1543 -4779 572 C ATOM 1797 CG ASP A1028 156.656 9.011 561.646 1.00206.15 C ANISOU 1797 CG ASP A1028 26288 33029 19012 -2229 -4947 288 C ATOM 1798 OD1 ASP A1028 156.533 7.923 562.247 1.00208.26 O ANISOU 1798 OD1 ASP A1028 26616 33014 19499 -2642 -4845 30 O ATOM 1799 OD2 ASP A1028 155.987 9.308 560.633 1.00212.25 O ANISOU 1799 OD2 ASP A1028 26934 34532 19180 -2365 -5156 321 O ATOM 1800 N ALA A1029 159.130 11.869 564.358 1.00162.67 N ANISOU 1800 N ALA A1029 20680 26069 15057 -348 -4507 1104 N ATOM 1801 CA ALA A1029 160.300 12.583 564.854 1.00149.59 C ANISOU 1801 CA ALA A1029 19135 23873 13830 73 -4240 1175 C ATOM 1802 C ALA A1029 160.525 12.340 566.341 1.00135.16 C ANISOU 1802 C ALA A1029 17122 21766 12466 138 -4219 1202 C ATOM 1803 O ALA A1029 161.664 12.433 566.815 1.00126.84 O ANISOU 1803 O ALA A1029 16180 20228 11786 318 -3984 1143 O ATOM 1804 CB ALA A1029 160.162 14.080 564.575 1.00149.64 C ANISOU 1804 CB ALA A1029 19034 24112 13709 549 -4203 1482 C ATOM 1805 N LEU A1030 159.463 12.021 567.085 1.00132.17 N ANISOU 1805 N LEU A1030 16441 21731 12046 -15 -4460 1291 N ATOM 1806 CA LEU A1030 159.600 11.777 568.518 1.00125.59 C ANISOU 1806 CA LEU A1030 15428 20684 11606 41 -4450 1338 C ATOM 1807 C LEU A1030 160.410 10.515 568.793 1.00122.72 C ANISOU 1807 C LEU A1030 15300 19820 11509 -186 -4270 1117 C ATOM 1808 O LEU A1030 161.320 10.522 569.630 1.00119.27 O ANISOU 1808 O LEU A1030 14852 19028 11437 17 -4114 1146 O ATOM 1809 CB LEU A1030 158.220 11.679 569.171 1.00124.81 C ANISOU 1809 CB LEU A1030 14974 21069 11380 -93 -4728 1478 C ATOM 1810 CG LEU A1030 157.647 12.954 569.793 1.00111.08 C ANISOU 1810 CG LEU A1030 12908 19636 9663 276 -4807 1784 C ATOM 1811 CD1 LEU A1030 156.240 12.708 570.315 1.00112.65 C ANISOU 1811 CD1 LEU A1030 12757 20330 9716 100 -5075 1904 C ATOM 1812 CD2 LEU A1030 158.551 13.460 570.904 1.00107.37 C ANISOU 1812 CD2 LEU A1030 12412 18773 9611 549 -4609 1822 C ATOM 1813 N THR A1031 160.091 9.418 568.100 1.00125.25 N ANISOU 1813 N THR A1031 15825 20125 11639 -612 -4255 901 N ATOM 1814 CA THR A1031 160.766 8.154 568.385 1.00129.17 C ANISOU 1814 CA THR A1031 16569 20101 12409 -812 -4001 727 C ATOM 1815 C THR A1031 162.245 8.212 568.016 1.00134.18 C ANISOU 1815 C THR A1031 17482 20216 13285 -581 -3690 660 C ATOM 1816 O THR A1031 163.102 7.770 568.793 1.00132.69 O ANISOU 1816 O THR A1031 17312 19633 13469 -420 -3495 706 O ATOM 1817 CB THR A1031 160.066 7.002 567.657 1.00131.99 C ANISOU 1817 CB THR A1031 17126 20529 12495 -1379 -3966 460 C ATOM 1818 OG1 THR A1031 160.865 5.816 567.753 1.00136.24 O ANISOU 1818 OG1 THR A1031 17998 20448 13319 -1531 -3590 297 O ATOM 1819 CG2 THR A1031 159.829 7.338 566.188 1.00132.16 C ANISOU 1819 CG2 THR A1031 17297 20860 12056 -1560 -4029 314 C ATOM 1820 N LYS A1032 162.569 8.765 566.845 1.00144.00 N ANISOU 1820 N LYS A1032 18920 21487 14307 -543 -3633 573 N ATOM 1821 CA LYS A1032 163.968 8.861 566.441 1.00146.36 C ANISOU 1821 CA LYS A1032 19477 21301 14833 -335 -3319 493 C ATOM 1822 C LYS A1032 164.713 9.884 567.289 1.00140.42 C ANISOU 1822 C LYS A1032 18490 20488 14373 119 -3294 674 C ATOM 1823 O LYS A1032 165.894 9.695 567.604 1.00141.47 O ANISOU 1823 O LYS A1032 18684 20236 14832 294 -3052 649 O ATOM 1824 CB LYS A1032 164.066 9.218 564.959 1.00152.11 C ANISOU 1824 CB LYS A1032 20486 22090 15218 -427 -3253 351 C ATOM 1825 CG LYS A1032 165.420 8.915 564.340 1.00153.52 C ANISOU 1825 CG LYS A1032 21023 21706 15602 -364 -2871 185 C ATOM 1826 CD LYS A1032 165.749 9.887 563.220 1.00154.49 C ANISOU 1826 CD LYS A1032 21317 21903 15480 -216 -2811 160 C ATOM 1827 CE LYS A1032 164.635 9.960 562.192 1.00158.95 C ANISOU 1827 CE LYS A1032 21943 22980 15470 -502 -3029 115 C ATOM 1828 NZ LYS A1032 164.923 10.984 561.151 1.00161.45 N ANISOU 1828 NZ LYS A1032 22415 23404 15524 -284 -2962 166 N ATOM 1829 N MET A1033 164.038 10.973 567.666 1.00134.33 N ANISOU 1829 N MET A1033 17439 20117 13483 299 -3509 851 N ATOM 1830 CA MET A1033 164.663 11.962 568.538 1.00131.81 C ANISOU 1830 CA MET A1033 16899 19760 13421 648 -3438 971 C ATOM 1831 C MET A1033 164.987 11.366 569.902 1.00132.37 C ANISOU 1831 C MET A1033 16756 19729 13811 675 -3445 1031 C ATOM 1832 O MET A1033 166.020 11.689 570.500 1.00132.07 O ANISOU 1832 O MET A1033 16614 19533 14031 883 -3289 1034 O ATOM 1833 CB MET A1033 163.753 13.183 568.685 1.00129.79 C ANISOU 1833 CB MET A1033 16419 19917 12978 813 -3596 1157 C ATOM 1834 CG MET A1033 164.290 14.243 569.633 1.00128.28 C ANISOU 1834 CG MET A1033 16018 19691 13034 1097 -3464 1233 C ATOM 1835 SD MET A1033 163.193 15.663 569.803 1.00126.07 S ANISOU 1835 SD MET A1033 15525 19804 12573 1314 -3526 1474 S ATOM 1836 CE MET A1033 164.042 16.593 571.076 1.00121.69 C ANISOU 1836 CE MET A1033 14774 19101 12361 1499 -3276 1436 C ATOM 1837 N ARG A1034 164.117 10.488 570.409 1.00132.49 N ANISOU 1837 N ARG A1034 16685 19867 13786 456 -3613 1081 N ATOM 1838 CA ARG A1034 164.393 9.841 571.687 1.00132.69 C ANISOU 1838 CA ARG A1034 16532 19799 14086 503 -3599 1180 C ATOM 1839 C ARG A1034 165.494 8.796 571.550 1.00136.69 C ANISOU 1839 C ARG A1034 17257 19854 14825 517 -3315 1115 C ATOM 1840 O ARG A1034 166.331 8.648 572.448 1.00138.06 O ANISOU 1840 O ARG A1034 17265 19937 15255 734 -3216 1227 O ATOM 1841 CB ARG A1034 163.119 9.209 572.247 1.00133.03 C ANISOU 1841 CB ARG A1034 16449 20072 14026 265 -3808 1255 C ATOM 1842 CG ARG A1034 163.310 8.564 573.610 1.00134.80 C ANISOU 1842 CG ARG A1034 16495 20223 14501 336 -3787 1401 C ATOM 1843 CD ARG A1034 162.020 7.961 574.136 1.00137.92 C ANISOU 1843 CD ARG A1034 16789 20818 14797 81 -3958 1457 C ATOM 1844 NE ARG A1034 162.211 7.333 575.439 1.00138.12 N ANISOU 1844 NE ARG A1034 16671 20763 15046 175 -3909 1627 N ATOM 1845 CZ ARG A1034 161.250 6.724 576.125 1.00138.36 C ANISOU 1845 CZ ARG A1034 16614 20900 15056 -11 -3996 1700 C ATOM 1846 NH1 ARG A1034 161.517 6.180 577.305 1.00138.99 N ANISOU 1846 NH1 ARG A1034 16582 20902 15327 121 -3922 1889 N ATOM 1847 NH2 ARG A1034 160.020 6.658 575.632 1.00138.62 N ANISOU 1847 NH2 ARG A1034 16651 21160 14858 -328 -4152 1593 N ATOM 1848 N ALA A1035 165.506 8.058 570.436 1.00139.89 N ANISOU 1848 N ALA A1035 18021 20002 15127 290 -3159 945 N ATOM 1849 CA ALA A1035 166.576 7.093 570.201 1.00141.10 C ANISOU 1849 CA ALA A1035 18424 19665 15523 328 -2806 892 C ATOM 1850 C ALA A1035 167.934 7.784 570.166 1.00138.90 C ANISOU 1850 C ALA A1035 18080 19254 15441 666 -2643 904 C ATOM 1851 O ALA A1035 168.871 7.379 570.867 1.00140.32 O ANISOU 1851 O ALA A1035 18136 19275 15906 896 -2474 1030 O ATOM 1852 CB ALA A1035 166.320 6.332 568.899 1.00145.07 C ANISOU 1852 CB ALA A1035 19356 19923 15841 -29 -2627 650 C ATOM 1853 N ALA A1036 168.055 8.840 569.358 1.00132.41 N ANISOU 1853 N ALA A1036 17322 18530 14457 707 -2672 787 N ATOM 1854 CA ALA A1036 169.288 9.617 569.331 1.00127.88 C ANISOU 1854 CA ALA A1036 16673 17858 14058 982 -2496 756 C ATOM 1855 C ALA A1036 169.551 10.319 570.656 1.00123.16 C ANISOU 1855 C ALA A1036 15636 17556 13603 1197 -2614 895 C ATOM 1856 O ALA A1036 170.704 10.649 570.952 1.00126.27 O ANISOU 1856 O ALA A1036 15881 17903 14192 1393 -2445 874 O ATOM 1857 CB ALA A1036 169.243 10.641 568.196 1.00128.30 C ANISOU 1857 CB ALA A1036 16919 17941 13887 974 -2463 615 C ATOM 1858 N ALA A1037 168.509 10.555 571.457 1.00118.09 N ANISOU 1858 N ALA A1037 14769 17247 12851 1136 -2884 1015 N ATOM 1859 CA ALA A1037 168.703 11.170 572.765 1.00115.46 C ANISOU 1859 CA ALA A1037 14034 17213 12624 1284 -2978 1122 C ATOM 1860 C ALA A1037 169.380 10.204 573.729 1.00118.50 C ANISOU 1860 C ALA A1037 14231 17565 13227 1399 -2923 1274 C ATOM 1861 O ALA A1037 170.333 10.572 574.426 1.00116.03 O ANISOU 1861 O ALA A1037 13634 17408 13043 1571 -2852 1300 O ATOM 1862 CB ALA A1037 167.362 11.643 573.327 1.00113.46 C ANISOU 1862 CB ALA A1037 13616 17296 12197 1186 -3247 1218 C ATOM 1863 N LEU A1038 168.897 8.960 573.784 1.00123.71 N ANISOU 1863 N LEU A1038 15039 18052 13915 1302 -2925 1384 N ATOM 1864 CA LEU A1038 169.521 7.969 574.655 1.00125.75 C ANISOU 1864 CA LEU A1038 15156 18241 14381 1474 -2808 1600 C ATOM 1865 C LEU A1038 170.903 7.578 574.145 1.00129.55 C ANISOU 1865 C LEU A1038 15732 18425 15068 1676 -2488 1589 C ATOM 1866 O LEU A1038 171.838 7.412 574.938 1.00131.22 O ANISOU 1866 O LEU A1038 15642 18780 15435 1940 -2409 1767 O ATOM 1867 CB LEU A1038 168.622 6.739 574.781 1.00123.42 C ANISOU 1867 CB LEU A1038 15058 17756 14081 1307 -2794 1709 C ATOM 1868 CG LEU A1038 167.277 6.957 575.477 1.00117.08 C ANISOU 1868 CG LEU A1038 14102 17272 13111 1126 -3096 1763 C ATOM 1869 CD1 LEU A1038 166.488 5.659 575.550 1.00119.31 C ANISOU 1869 CD1 LEU A1038 14603 17322 13409 923 -3005 1830 C ATOM 1870 CD2 LEU A1038 167.482 7.541 576.866 1.00112.25 C ANISOU 1870 CD2 LEU A1038 13048 17071 12530 1322 -3262 1941 C ATOM 1871 N ASP A1039 171.053 7.430 572.825 1.00133.29 N ANISOU 1871 N ASP A1039 16597 18525 15522 1557 -2296 1390 N ATOM 1872 CA ASP A1039 172.372 7.145 572.270 1.00137.28 C ANISOU 1872 CA ASP A1039 17202 18727 16233 1746 -1960 1359 C ATOM 1873 C ASP A1039 173.346 8.288 572.524 1.00132.87 C ANISOU 1873 C ASP A1039 16313 18454 15718 1927 -1975 1287 C ATOM 1874 O ASP A1039 174.547 8.053 572.700 1.00137.49 O ANISOU 1874 O ASP A1039 16727 19009 16505 2168 -1765 1367 O ATOM 1875 CB ASP A1039 172.267 6.854 570.773 1.00145.80 C ANISOU 1875 CB ASP A1039 18791 19368 17239 1530 -1749 1121 C ATOM 1876 CG ASP A1039 172.003 5.388 570.482 1.00155.59 C ANISOU 1876 CG ASP A1039 20376 20173 18567 1402 -1484 1173 C ATOM 1877 OD1 ASP A1039 172.513 4.532 571.236 1.00159.32 O ANISOU 1877 OD1 ASP A1039 20731 20520 19282 1637 -1289 1433 O ATOM 1878 OD2 ASP A1039 171.290 5.092 569.501 1.00159.12 O ANISOU 1878 OD2 ASP A1039 21212 20420 18827 1060 -1437 957 O ATOM 1879 N ALA A1040 172.854 9.528 572.546 1.00123.32 N ANISOU 1879 N ALA A1040 15001 17529 14324 1812 -2179 1134 N ATOM 1880 CA ALA A1040 173.696 10.662 572.902 1.00118.96 C ANISOU 1880 CA ALA A1040 14137 17257 13804 1914 -2143 1020 C ATOM 1881 C ALA A1040 173.962 10.738 574.399 1.00114.88 C ANISOU 1881 C ALA A1040 13106 17220 13324 2027 -2289 1188 C ATOM 1882 O ALA A1040 174.963 11.335 574.809 1.00115.59 O ANISOU 1882 O ALA A1040 12868 17579 13471 2113 -2200 1107 O ATOM 1883 CB ALA A1040 173.057 11.968 572.425 1.00120.96 C ANISOU 1883 CB ALA A1040 14501 17594 13863 1766 -2212 818 C ATOM 1884 N GLN A1041 173.090 10.147 575.218 1.00113.32 N ANISOU 1884 N GLN A1041 12820 17168 13068 2002 -2501 1405 N ATOM 1885 CA GLN A1041 173.299 10.140 576.661 1.00111.82 C ANISOU 1885 CA GLN A1041 12153 17463 12868 2109 -2646 1593 C ATOM 1886 C GLN A1041 174.313 9.080 577.072 1.00117.43 C ANISOU 1886 C GLN A1041 12675 18188 13753 2402 -2495 1867 C ATOM 1887 O GLN A1041 175.090 9.293 578.010 1.00124.84 O ANISOU 1887 O GLN A1041 13140 19613 14680 2546 -2535 1970 O ATOM 1888 CB GLN A1041 171.972 9.909 577.383 1.00108.71 C ANISOU 1888 CB GLN A1041 11751 17207 12348 1985 -2902 1738 C ATOM 1889 CG GLN A1041 172.061 9.975 578.899 1.00108.32 C ANISOU 1889 CG GLN A1041 11232 17689 12237 2062 -3065 1924 C ATOM 1890 CD GLN A1041 170.795 9.486 579.575 1.00106.82 C ANISOU 1890 CD GLN A1041 11079 17549 11960 1968 -3266 2107 C ATOM 1891 OE1 GLN A1041 170.164 10.214 580.342 1.00102.66 O ANISOU 1891 OE1 GLN A1041 10352 17361 11293 1836 -3446 2065 O ATOM 1892 NE2 GLN A1041 170.417 8.245 579.294 1.00105.50 N ANISOU 1892 NE2 GLN A1041 11183 17018 11885 2012 -3188 2292 N ATOM 1893 N LYS A1042 174.318 7.934 576.387 1.00120.70 N ANISOU 1893 N LYS A1042 13445 18103 14315 2490 -2291 1996 N ATOM 1894 CA LYS A1042 175.250 6.868 576.741 1.00125.68 C ANISOU 1894 CA LYS A1042 13931 18680 15142 2834 -2064 2323 C ATOM 1895 C LYS A1042 176.691 7.265 576.450 1.00114.59 C ANISOU 1895 C LYS A1042 12283 17402 13854 3024 -1874 2246 C ATOM 1896 O LYS A1042 177.606 6.884 577.190 1.00117.42 O ANISOU 1896 O LYS A1042 12222 18102 14289 3339 -1808 2528 O ATOM 1897 CB LYS A1042 174.890 5.586 575.992 1.00125.51 C ANISOU 1897 CB LYS A1042 14418 18000 15269 2840 -1783 2430 C ATOM 1898 CG LYS A1042 173.542 4.995 576.371 1.00114.80 C ANISOU 1898 CG LYS A1042 13263 16539 13818 2650 -1914 2526 C ATOM 1899 CD LYS A1042 173.265 3.722 575.591 1.00117.44 C ANISOU 1899 CD LYS A1042 14118 16205 14297 2584 -1548 2563 C ATOM 1900 CE LYS A1042 171.919 3.119 575.961 1.00117.54 C ANISOU 1900 CE LYS A1042 14322 16128 14212 2337 -1642 2612 C ATOM 1901 NZ LYS A1042 171.645 1.875 575.189 1.00120.71 N ANISOU 1901 NZ LYS A1042 15256 15868 14741 2188 -1214 2579 N ATOM 1902 N ALA A1043 176.914 8.030 575.385 1.00113.00 N ANISOU 1902 N ALA A1043 12316 16969 13651 2848 -1775 1885 N ATOM 1903 CA ALA A1043 178.261 8.403 574.987 1.00126.66 C ANISOU 1903 CA ALA A1043 13859 18756 15508 2989 -1549 1767 C ATOM 1904 C ALA A1043 178.765 9.582 575.818 1.00124.84 C ANISOU 1904 C ALA A1043 13084 19209 15139 2916 -1716 1608 C ATOM 1905 O ALA A1043 178.018 10.226 576.559 1.00111.92 O ANISOU 1905 O ALA A1043 11293 17922 13307 2728 -1979 1542 O ATOM 1906 CB ALA A1043 178.305 8.736 573.497 1.00124.75 C ANISOU 1906 CB ALA A1043 14121 17968 15310 2819 -1331 1439 C ATOM 1907 N THR A1044 180.062 9.860 575.684 1.00123.81 N ANISOU 1907 N THR A1044 12658 19272 15112 3040 -1522 1521 N ATOM 1908 CA THR A1044 180.717 10.913 576.444 1.00124.28 C ANISOU 1908 CA THR A1044 12164 20019 15036 2923 -1607 1320 C ATOM 1909 C THR A1044 181.038 12.093 575.543 1.00128.45 C ANISOU 1909 C THR A1044 12889 20348 15570 2662 -1409 837 C ATOM 1910 O THR A1044 181.701 11.916 574.511 1.00127.49 O ANISOU 1910 O THR A1044 13008 19807 15627 2748 -1126 743 O ATOM 1911 CB THR A1044 182.006 10.393 577.093 1.00128.33 C ANISOU 1911 CB THR A1044 12080 21057 15623 3239 -1532 1581 C ATOM 1912 OG1 THR A1044 182.965 10.088 576.073 1.00133.18 O ANISOU 1912 OG1 THR A1044 12840 21282 16481 3409 -1186 1535 O ATOM 1913 CG2 THR A1044 181.722 9.135 577.902 1.00130.15 C ANISOU 1913 CG2 THR A1044 12174 21408 15867 3582 -1646 2136 C ATOM 1914 N PRO A1045 180.593 13.297 575.888 1.00137.26 N ANISOU 1914 N PRO A1045 13936 21712 16504 2351 -1495 533 N ATOM 1915 CA PRO A1045 180.922 14.476 575.083 1.00142.34 C ANISOU 1915 CA PRO A1045 14776 22150 17158 2121 -1227 90 C ATOM 1916 C PRO A1045 182.336 14.946 575.373 1.00150.13 C ANISOU 1916 C PRO A1045 15256 23601 18185 2077 -1027 -130 C ATOM 1917 O PRO A1045 182.996 14.424 576.285 1.00154.99 O ANISOU 1917 O PRO A1045 15308 24807 18773 2222 -1151 79 O ATOM 1918 CB PRO A1045 179.882 15.507 575.544 1.00133.93 C ANISOU 1918 CB PRO A1045 13786 21209 15893 1841 -1344 -89 C ATOM 1919 CG PRO A1045 179.615 15.133 576.955 1.00110.23 C ANISOU 1919 CG PRO A1045 10322 18805 12755 1856 -1650 141 C ATOM 1920 CD PRO A1045 179.706 13.629 577.016 1.00111.58 C ANISOU 1920 CD PRO A1045 10474 18883 13039 2200 -1785 590 C ATOM 1921 N PRO A1046 182.846 15.933 574.620 1.00152.72 N ANISOU 1921 N PRO A1046 15745 23719 18561 1879 -699 -542 N ATOM 1922 CA PRO A1046 184.192 16.449 574.910 1.00156.93 C ANISOU 1922 CA PRO A1046 15763 24743 19120 1762 -481 -818 C ATOM 1923 C PRO A1046 184.250 17.204 576.229 1.00156.25 C ANISOU 1923 C PRO A1046 15119 25452 18797 1461 -598 -1011 C ATOM 1924 O PRO A1046 184.279 18.438 576.251 1.00157.81 O ANISOU 1924 O PRO A1046 15348 25702 18912 1088 -353 -1462 O ATOM 1925 CB PRO A1046 184.479 17.376 573.721 1.00157.62 C ANISOU 1925 CB PRO A1046 16290 24288 19309 1586 -59 -1230 C ATOM 1926 CG PRO A1046 183.577 16.897 572.637 1.00158.22 C ANISOU 1926 CG PRO A1046 17072 23593 19453 1758 -81 -1038 C ATOM 1927 CD PRO A1046 182.335 16.435 573.333 1.00156.87 C ANISOU 1927 CD PRO A1046 16940 23528 19137 1807 -477 -729 C ATOM 1928 N LYS A1047 184.262 16.462 577.333 1.00156.11 N ANISOU 1928 N LYS A1047 14610 26048 18657 1612 -931 -670 N ATOM 1929 CA LYS A1047 184.321 17.070 578.653 1.00151.21 C ANISOU 1929 CA LYS A1047 13425 26269 17757 1312 -1072 -833 C ATOM 1930 C LYS A1047 185.673 17.732 578.889 1.00154.51 C ANISOU 1930 C LYS A1047 13273 27324 18110 1053 -834 -1229 C ATOM 1931 O LYS A1047 186.699 17.321 578.339 1.00153.59 O ANISOU 1931 O LYS A1047 12987 27209 18160 1254 -682 -1185 O ATOM 1932 CB LYS A1047 184.068 16.022 579.737 1.00143.66 C ANISOU 1932 CB LYS A1047 12077 25843 16664 1588 -1479 -315 C ATOM 1933 CG LYS A1047 182.663 15.452 579.747 1.00134.51 C ANISOU 1933 CG LYS A1047 11400 24187 15520 1742 -1715 17 C ATOM 1934 CD LYS A1047 181.638 16.525 580.067 1.00129.80 C ANISOU 1934 CD LYS A1047 11030 23524 14765 1351 -1721 -292 C ATOM 1935 CE LYS A1047 180.279 15.915 580.358 1.00127.53 C ANISOU 1935 CE LYS A1047 11045 22967 14442 1489 -2011 65 C ATOM 1936 NZ LYS A1047 179.237 16.956 580.561 1.00124.04 N ANISOU 1936 NZ LYS A1047 10851 22395 13882 1161 -1976 -198 N ATOM 1937 N LEU A1048 185.665 18.770 579.719 1.00158.80 N ANISOU 1937 N LEU A1048 13511 28421 18403 572 -771 -1642 N ATOM 1938 CA LEU A1048 186.898 19.424 580.121 1.00165.45 C ANISOU 1938 CA LEU A1048 13729 30023 19111 218 -558 -2076 C ATOM 1939 C LEU A1048 187.570 18.637 581.240 1.00182.23 C ANISOU 1939 C LEU A1048 15009 33228 21001 387 -918 -1739 C ATOM 1940 O LEU A1048 186.907 18.029 582.085 1.00183.72 O ANISOU 1940 O LEU A1048 15068 33716 21023 568 -1294 -1332 O ATOM 1941 CB LEU A1048 186.630 20.860 580.579 1.00155.55 C ANISOU 1941 CB LEU A1048 12502 28936 17663 -429 -270 -2701 C ATOM 1942 CG LEU A1048 186.447 21.943 579.509 1.00147.18 C ANISOU 1942 CG LEU A1048 12100 27018 16806 -677 272 -3165 C ATOM 1943 CD1 LEU A1048 185.134 21.783 578.752 1.00142.29 C ANISOU 1943 CD1 LEU A1048 12286 25424 16355 -378 218 -2863 C ATOM 1944 CD2 LEU A1048 186.541 23.329 580.132 1.00146.05 C ANISOU 1944 CD2 LEU A1048 11812 27219 16460 -1357 668 -3824 C ATOM 1945 N GLU A1049 188.903 18.639 581.222 1.00199.73 N ANISOU 1945 N GLU A1049 16636 36051 23200 352 -786 -1885 N ATOM 1946 CA GLU A1049 189.781 17.973 582.182 1.00206.71 C ANISOU 1946 CA GLU A1049 16606 38094 23840 536 -1070 -1571 C ATOM 1947 C GLU A1049 189.711 16.451 582.105 1.00208.96 C ANISOU 1947 C GLU A1049 16891 38215 24291 1305 -1346 -746 C ATOM 1948 O GLU A1049 190.395 15.780 582.890 1.00217.06 O ANISOU 1948 O GLU A1049 17173 40177 25125 1587 -1574 -349 O ATOM 1949 CB GLU A1049 189.506 18.406 583.631 1.00207.62 C ANISOU 1949 CB GLU A1049 16191 39220 23476 133 -1326 -1706 C ATOM 1950 CG GLU A1049 189.543 19.912 583.862 1.00206.44 C ANISOU 1950 CG GLU A1049 16031 39275 23132 -689 -988 -2548 C ATOM 1951 CD GLU A1049 190.876 20.535 583.495 1.00208.95 C ANISOU 1951 CD GLU A1049 15910 40027 23456 -1039 -622 -3080 C ATOM 1952 OE1 GLU A1049 191.074 20.874 582.308 1.00206.42 O ANISOU 1952 OE1 GLU A1049 16105 38834 23491 -1030 -227 -3324 O ATOM 1953 OE2 GLU A1049 191.731 20.683 584.393 1.00214.46 O ANISOU 1953 OE2 GLU A1049 15853 41857 23777 -1324 -711 -3236 O ATOM 1954 N ASP A1050 188.914 15.884 581.195 1.00205.34 N ANISOU 1954 N ASP A1050 17228 36629 24162 1646 -1299 -471 N ATOM 1955 CA ASP A1050 188.805 14.435 581.007 1.00203.56 C ANISOU 1955 CA ASP A1050 17122 36082 24140 2330 -1440 258 C ATOM 1956 C ASP A1050 188.397 13.742 582.309 1.00201.74 C ANISOU 1956 C ASP A1050 16467 36559 23625 2562 -1839 775 C ATOM 1957 O ASP A1050 189.139 12.944 582.887 1.00211.15 O ANISOU 1957 O ASP A1050 17036 38461 24730 2977 -1958 1259 O ATOM 1958 CB ASP A1050 190.111 13.854 580.453 1.00212.15 C ANISOU 1958 CB ASP A1050 17860 37298 25448 2707 -1223 452 C ATOM 1959 CG ASP A1050 190.520 14.489 579.138 1.00213.14 C ANISOU 1959 CG ASP A1050 18439 36684 25859 2494 -805 -42 C ATOM 1960 OD1 ASP A1050 189.626 14.942 578.392 1.00208.66 O ANISOU 1960 OD1 ASP A1050 18651 35218 25413 2285 -688 -304 O ATOM 1961 OD2 ASP A1050 191.734 14.535 578.848 1.00217.67 O ANISOU 1961 OD2 ASP A1050 18573 37607 26525 2549 -587 -147 O ATOM 1962 N LYS A1051 187.190 14.066 582.763 1.00183.09 N ANISOU 1962 N LYS A1051 14452 34000 21115 2312 -2023 692 N ATOM 1963 CA LYS A1051 186.707 13.602 584.054 1.00173.41 C ANISOU 1963 CA LYS A1051 12863 33446 19578 2425 -2384 1087 C ATOM 1964 C LYS A1051 186.202 12.163 583.968 1.00166.07 C ANISOU 1964 C LYS A1051 12232 32016 18849 3065 -2484 1824 C ATOM 1965 O LYS A1051 185.871 11.651 582.896 1.00163.63 O ANISOU 1965 O LYS A1051 12568 30699 18903 3291 -2291 1930 O ATOM 1966 CB LYS A1051 185.598 14.519 584.566 1.00166.29 C ANISOU 1966 CB LYS A1051 12234 32485 18464 1901 -2490 701 C ATOM 1967 CG LYS A1051 185.937 15.997 584.487 1.00163.35 C ANISOU 1967 CG LYS A1051 11765 32337 17962 1232 -2250 -79 C ATOM 1968 CD LYS A1051 184.825 16.852 585.065 1.00157.81 C ANISOU 1968 CD LYS A1051 11330 31565 17066 764 -2296 -399 C ATOM 1969 CE LYS A1051 185.073 18.325 584.794 1.00154.85 C ANISOU 1969 CE LYS A1051 11035 31153 16648 124 -1912 -1178 C ATOM 1970 NZ LYS A1051 186.423 18.757 585.255 1.00157.85 N ANISOU 1970 NZ LYS A1051 10640 32547 16787 -185 -1808 -1521 N ATOM 1971 N SER A1052 186.147 11.513 585.129 1.00161.32 N ANISOU 1971 N SER A1052 11298 31992 18003 3283 -2704 2292 N ATOM 1972 CA SER A1052 185.679 10.141 585.217 1.00154.52 C ANISOU 1972 CA SER A1052 10729 30671 17311 3854 -2725 2987 C ATOM 1973 C SER A1052 184.157 10.089 585.081 1.00154.05 C ANISOU 1973 C SER A1052 11238 29984 17311 3757 -2872 2989 C ATOM 1974 O SER A1052 183.476 11.105 585.237 1.00148.85 O ANISOU 1974 O SER A1052 10738 29321 16498 3232 -2972 2500 O ATOM 1975 CB SER A1052 186.121 9.523 586.542 1.00153.66 C ANISOU 1975 CB SER A1052 10346 31113 16924 4000 -2770 3397 C ATOM 1976 OG SER A1052 185.627 10.263 587.644 1.00152.19 O ANISOU 1976 OG SER A1052 10126 31342 16359 3485 -2939 3093 O ATOM 1977 N PRO A1053 183.598 8.914 584.774 1.00161.41 N ANISOU 1977 N PRO A1053 12620 30221 18489 4192 -2792 3488 N ATOM 1978 CA PRO A1053 182.132 8.813 584.657 1.00163.92 C ANISOU 1978 CA PRO A1053 13594 29825 18864 4008 -2876 3438 C ATOM 1979 C PRO A1053 181.384 9.097 585.951 1.00164.20 C ANISOU 1979 C PRO A1053 13465 30363 18561 3761 -3154 3454 C ATOM 1980 O PRO A1053 180.168 9.320 585.902 1.00161.86 O ANISOU 1980 O PRO A1053 13555 29690 18255 3538 -3281 3326 O ATOM 1981 CB PRO A1053 181.914 7.366 584.190 1.00136.13 C ANISOU 1981 CB PRO A1053 10494 25575 15655 4523 -2660 3987 C ATOM 1982 CG PRO A1053 183.174 6.647 584.553 1.00142.33 C ANISOU 1982 CG PRO A1053 10704 26919 16455 5068 -2533 4492 C ATOM 1983 CD PRO A1053 184.262 7.657 584.387 1.00143.56 C ANISOU 1983 CD PRO A1053 10358 27686 16503 4831 -2541 4064 C ATOM 1984 N ASP A1054 182.056 9.097 587.100 1.00168.64 N ANISOU 1984 N ASP A1054 13643 31566 18867 3703 -3156 3534 N ATOM 1985 CA ASP A1054 181.416 9.415 588.370 1.00171.94 C ANISOU 1985 CA ASP A1054 14072 32272 18983 3366 -3289 3445 C ATOM 1986 C ASP A1054 181.538 10.889 588.741 1.00170.46 C ANISOU 1986 C ASP A1054 13680 32557 18529 2744 -3334 2803 C ATOM 1987 O ASP A1054 181.173 11.265 589.859 1.00172.25 O ANISOU 1987 O ASP A1054 13852 33122 18474 2443 -3397 2694 O ATOM 1988 CB ASP A1054 182.000 8.552 589.493 1.00181.12 C ANISOU 1988 CB ASP A1054 14948 33911 19959 3668 -3246 3931 C ATOM 1989 CG ASP A1054 181.611 7.092 589.369 1.00185.44 C ANISOU 1989 CG ASP A1054 15769 33950 20740 4240 -3145 4581 C ATOM 1990 OD1 ASP A1054 181.143 6.690 588.283 1.00183.27 O ANISOU 1990 OD1 ASP A1054 15853 32990 20791 4445 -3080 4670 O ATOM 1991 OD2 ASP A1054 181.764 6.348 590.360 1.00190.75 O ANISOU 1991 OD2 ASP A1054 16301 34921 21255 4486 -3099 5010 O ATOM 1992 N SER A1055 182.031 11.725 587.835 1.00165.76 N ANISOU 1992 N SER A1055 12973 31991 18018 2548 -3260 2374 N ATOM 1993 CA SER A1055 182.214 13.138 588.117 1.00158.19 C ANISOU 1993 CA SER A1055 11815 31470 16822 1947 -3215 1736 C ATOM 1994 C SER A1055 180.881 13.878 588.069 1.00143.62 C ANISOU 1994 C SER A1055 10369 29227 14975 1591 -3270 1429 C ATOM 1995 O SER A1055 179.925 13.417 587.439 1.00139.27 O ANISOU 1995 O SER A1055 10239 28031 14645 1801 -3354 1631 O ATOM 1996 CB SER A1055 183.188 13.748 587.115 1.00157.17 C ANISOU 1996 CB SER A1055 11422 31484 16809 1864 -3061 1367 C ATOM 1997 OG SER A1055 182.688 13.643 585.793 1.00149.82 O ANISOU 1997 OG SER A1055 10877 29830 16219 2049 -3020 1347 O ATOM 1998 N PRO A1056 180.788 15.030 588.740 1.00133.84 N ANISOU 1998 N PRO A1056 14328 21744 14781 -1272 -4716 2559 N ATOM 1999 CA PRO A1056 179.542 15.812 588.670 1.00133.22 C ANISOU 1999 CA PRO A1056 14051 22446 14120 -1237 -4315 2666 C ATOM 2000 C PRO A1056 179.190 16.269 587.265 1.00131.26 C ANISOU 2000 C PRO A1056 13915 21911 14048 -1065 -3957 2338 C ATOM 2001 O PRO A1056 178.001 16.409 586.951 1.00128.63 O ANISOU 2001 O PRO A1056 13469 22054 13353 -1178 -3803 2572 O ATOM 2002 CB PRO A1056 179.826 17.004 589.595 1.00135.34 C ANISOU 2002 CB PRO A1056 14135 23236 14051 -883 -4022 2352 C ATOM 2003 CG PRO A1056 180.882 16.515 590.528 1.00127.36 C ANISOU 2003 CG PRO A1056 13179 21964 13247 -933 -4396 2399 C ATOM 2004 CD PRO A1056 181.739 15.594 589.713 1.00137.75 C ANISOU 2004 CD PRO A1056 14768 22297 15276 -1011 -4709 2277 C ATOM 2005 N GLU A1057 180.186 16.505 586.408 1.00133.39 N ANISOU 2005 N GLU A1057 14399 21435 14848 -817 -3827 1793 N ATOM 2006 CA GLU A1057 179.903 16.953 585.048 1.00136.66 C ANISOU 2006 CA GLU A1057 14955 21564 15407 -696 -3496 1481 C ATOM 2007 C GLU A1057 179.205 15.862 584.243 1.00142.77 C ANISOU 2007 C GLU A1057 15818 22113 16313 -1062 -3733 1866 C ATOM 2008 O GLU A1057 178.224 16.128 583.538 1.00140.17 O ANISOU 2008 O GLU A1057 15482 22011 15765 -1099 -3524 1953 O ATOM 2009 CB GLU A1057 181.197 17.389 584.360 1.00132.92 C ANISOU 2009 CB GLU A1057 14683 20378 15443 -422 -3316 812 C ATOM 2010 N MET A1058 179.701 14.626 584.335 1.00154.26 N ANISOU 2010 N MET A1058 17363 23100 18150 -1326 -4204 2087 N ATOM 2011 CA MET A1058 179.061 13.518 583.633 1.00158.59 C ANISOU 2011 CA MET A1058 17996 23412 18849 -1687 -4492 2471 C ATOM 2012 C MET A1058 177.669 13.243 584.190 1.00160.91 C ANISOU 2012 C MET A1058 18102 24468 18569 -2004 -4589 3137 C ATOM 2013 O MET A1058 176.737 12.950 583.431 1.00161.81 O ANISOU 2013 O MET A1058 18232 24654 18596 -2187 -4552 3357 O ATOM 2014 CB MET A1058 179.935 12.266 583.724 1.00163.94 C ANISOU 2014 CB MET A1058 18800 23410 20080 -1880 -5053 2544 C ATOM 2015 CG MET A1058 181.292 12.400 583.052 1.00165.47 C ANISOU 2015 CG MET A1058 19141 22841 20890 -1603 -4978 1834 C ATOM 2016 SD MET A1058 181.180 12.473 581.254 1.00164.29 S ANISOU 2016 SD MET A1058 19162 22212 21048 -1566 -4664 1412 S ATOM 2017 CE MET A1058 180.455 10.874 580.899 1.00167.64 C ANISOU 2017 CE MET A1058 19640 22389 21665 -2022 -5237 2000 C ATOM 2018 N LYS A1059 177.509 13.336 585.513 1.00159.40 N ANISOU 2018 N LYS A1059 17719 24880 17965 -2092 -4708 3447 N ATOM 2019 CA LYS A1059 176.200 13.114 586.118 1.00158.69 C ANISOU 2019 CA LYS A1059 17405 25620 17271 -2431 -4772 4045 C ATOM 2020 C LYS A1059 175.203 14.181 585.681 1.00154.18 C ANISOU 2020 C LYS A1059 16666 25627 16290 -2214 -4263 3862 C ATOM 2021 O LYS A1059 174.020 13.887 585.475 1.00156.75 O ANISOU 2021 O LYS A1059 16865 26391 16301 -2479 -4269 4237 O ATOM 2022 CB LYS A1059 176.321 13.084 587.642 1.00158.23 C ANISOU 2022 CB LYS A1059 17169 26131 16822 -2573 -4970 4346 C ATOM 2023 CG LYS A1059 177.128 11.913 588.181 1.00157.36 C ANISOU 2023 CG LYS A1059 17229 25503 17058 -2868 -5589 4653 C ATOM 2024 CD LYS A1059 177.155 11.916 589.702 1.00160.83 C ANISOU 2024 CD LYS A1059 17506 26573 17030 -3058 -5786 4996 C ATOM 2025 CE LYS A1059 177.962 10.748 590.245 1.00165.68 C ANISOU 2025 CE LYS A1059 18327 26621 18002 -3361 -6476 5320 C ATOM 2026 NZ LYS A1059 177.404 9.436 589.813 1.00169.10 N ANISOU 2026 NZ LYS A1059 18901 26756 18591 -3870 -6968 5880 N ATOM 2027 N ASP A1060 175.661 15.427 585.541 1.00149.19 N ANISOU 2027 N ASP A1060 16030 24991 15664 -1734 -3850 3279 N ATOM 2028 CA ASP A1060 174.789 16.472 585.014 1.00142.00 C ANISOU 2028 CA ASP A1060 15008 24498 14448 -1487 -3429 3044 C ATOM 2029 C ASP A1060 174.461 16.224 583.548 1.00137.84 C ANISOU 2029 C ASP A1060 14702 23450 14221 -1532 -3363 2963 C ATOM 2030 O ASP A1060 173.326 16.453 583.111 1.00139.40 O ANISOU 2030 O ASP A1060 14792 24040 14133 -1575 -3224 3089 O ATOM 2031 CB ASP A1060 175.440 17.844 585.193 1.00142.12 C ANISOU 2031 CB ASP A1060 15015 24537 14446 -978 -3072 2442 C ATOM 2032 CG ASP A1060 175.592 18.231 586.650 1.00152.78 C ANISOU 2032 CG ASP A1060 16102 26529 15418 -902 -3092 2496 C ATOM 2033 OD1 ASP A1060 174.768 17.783 587.474 1.00160.32 O ANISOU 2033 OD1 ASP A1060 16797 28194 15923 -1210 -3248 2970 O ATOM 2034 OD2 ASP A1060 176.535 18.984 586.972 1.00154.68 O ANISOU 2034 OD2 ASP A1060 16391 26586 15794 -558 -2950 2060 O ATOM 2035 N PHE A1061 175.443 15.751 582.775 1.00132.06 N ANISOU 2035 N PHE A1061 14262 21852 14063 -1523 -3468 2727 N ATOM 2036 CA PHE A1061 175.201 15.453 581.367 1.00126.20 C ANISOU 2036 CA PHE A1061 13737 20604 13610 -1596 -3417 2632 C ATOM 2037 C PHE A1061 174.143 14.368 581.208 1.00129.01 C ANISOU 2037 C PHE A1061 14024 21147 13846 -2027 -3708 3230 C ATOM 2038 O PHE A1061 173.272 14.465 580.336 1.00132.09 O ANISOU 2038 O PHE A1061 14443 21601 14142 -2071 -3575 3276 O ATOM 2039 CB PHE A1061 176.506 15.040 580.686 1.00120.05 C ANISOU 2039 CB PHE A1061 13228 18926 13459 -1547 -3507 2243 C ATOM 2040 CG PHE A1061 176.366 14.783 579.212 1.00116.81 C ANISOU 2040 CG PHE A1061 13043 17999 13342 -1620 -3427 2071 C ATOM 2041 CD1 PHE A1061 176.295 15.836 578.315 1.00112.95 C ANISOU 2041 CD1 PHE A1061 12690 17430 12795 -1380 -3017 1646 C ATOM 2042 CD2 PHE A1061 176.311 13.488 578.722 1.00117.97 C ANISOU 2042 CD2 PHE A1061 13277 17729 13817 -1943 -3792 2333 C ATOM 2043 CE1 PHE A1061 176.165 15.603 576.958 1.00110.95 C ANISOU 2043 CE1 PHE A1061 12658 16726 12773 -1482 -2946 1495 C ATOM 2044 CE2 PHE A1061 176.183 13.248 577.366 1.00114.96 C ANISOU 2044 CE2 PHE A1061 13091 16899 13691 -2013 -3714 2151 C ATOM 2045 CZ PHE A1061 176.112 14.307 576.483 1.00111.92 C ANISOU 2045 CZ PHE A1061 12840 16472 13212 -1792 -3277 1735 C ATOM 2046 N ARG A1062 174.198 13.329 582.044 1.00130.82 N ANISOU 2046 N ARG A1062 14176 21457 14072 -2367 -4134 3705 N ATOM 2047 CA ARG A1062 173.174 12.290 581.985 1.00134.82 C ANISOU 2047 CA ARG A1062 14615 22179 14431 -2828 -4442 4319 C ATOM 2048 C ARG A1062 171.839 12.800 582.515 1.00137.04 C ANISOU 2048 C ARG A1062 14578 23450 14042 -2910 -4246 4607 C ATOM 2049 O ARG A1062 170.777 12.432 581.997 1.00139.36 O ANISOU 2049 O ARG A1062 14811 23960 14180 -3144 -4273 4901 O ATOM 2050 CB ARG A1062 173.629 11.059 582.768 1.00141.04 C ANISOU 2050 CB ARG A1062 15439 22757 15391 -3202 -5007 4766 C ATOM 2051 CG ARG A1062 174.927 10.444 582.267 1.00140.13 C ANISOU 2051 CG ARG A1062 15596 21662 15985 -3122 -5278 4453 C ATOM 2052 CD ARG A1062 175.282 9.192 583.054 1.00143.49 C ANISOU 2052 CD ARG A1062 16069 21859 16591 -3501 -5931 4928 C ATOM 2053 NE ARG A1062 176.545 8.607 582.615 1.00143.71 N ANISOU 2053 NE ARG A1062 16317 20950 17334 -3384 -6234 4560 N ATOM 2054 CZ ARG A1062 177.725 8.878 583.165 1.00144.50 C ANISOU 2054 CZ ARG A1062 16449 20776 17681 -3133 -6287 4196 C ATOM 2055 NH1 ARG A1062 177.805 9.727 584.180 1.00145.01 N ANISOU 2055 NH1 ARG A1062 16358 21415 17323 -2975 -6057 4177 N ATOM 2056 NH2 ARG A1062 178.824 8.299 582.701 1.00145.22 N ANISOU 2056 NH2 ARG A1062 16702 20027 18446 -3031 -6579 3817 N ATOM 2057 N HIS A1063 171.874 13.651 583.543 1.00137.51 N ANISOU 2057 N HIS A1063 14409 24134 13705 -2712 -4051 4490 N ATOM 2058 CA HIS A1063 170.641 14.157 584.140 1.00139.57 C ANISOU 2058 CA HIS A1063 14304 25409 13318 -2775 -3869 4688 C ATOM 2059 C HIS A1063 169.857 15.018 583.156 1.00135.27 C ANISOU 2059 C HIS A1063 13729 24977 12689 -2489 -3510 4363 C ATOM 2060 O HIS A1063 168.624 14.926 583.085 1.00133.63 O ANISOU 2060 O HIS A1063 13293 25355 12125 -2678 -3482 4624 O ATOM 2061 CB HIS A1063 170.967 14.947 585.407 1.00130.83 C ANISOU 2061 CB HIS A1063 12961 24900 11849 -2571 -3731 4528 C ATOM 2062 CG HIS A1063 169.761 15.394 586.172 1.00133.93 C ANISOU 2062 CG HIS A1063 12918 26415 11555 -2666 -3575 4700 C ATOM 2063 ND1 HIS A1063 168.893 14.510 586.775 1.00138.44 N ANISOU 2063 ND1 HIS A1063 13269 27600 11730 -3223 -3820 5315 N ATOM 2064 CD2 HIS A1063 169.281 16.632 586.437 1.00133.56 C ANISOU 2064 CD2 HIS A1063 12593 27007 11148 -2284 -3215 4305 C ATOM 2065 CE1 HIS A1063 167.929 15.184 587.376 1.00140.73 C ANISOU 2065 CE1 HIS A1063 13137 28906 11427 -3187 -3581 5267 C ATOM 2066 NE2 HIS A1063 168.141 16.473 587.187 1.00142.13 N ANISOU 2066 NE2 HIS A1063 13264 29107 11633 -2597 -3227 4642 N ATOM 2067 N GLY A1064 170.556 15.862 582.392 1.00132.01 N ANISOU 2067 N GLY A1064 13548 24013 12596 -2053 -3254 3792 N ATOM 2068 CA GLY A1064 169.876 16.691 581.409 1.00121.33 C ANISOU 2068 CA GLY A1064 12231 22678 11191 -1793 -2972 3488 C ATOM 2069 C GLY A1064 169.094 15.872 580.401 1.00121.58 C ANISOU 2069 C GLY A1064 12368 22486 11342 -2097 -3109 3789 C ATOM 2070 O GLY A1064 167.941 16.180 580.087 1.00122.36 O ANISOU 2070 O GLY A1064 12298 23041 11151 -2093 -3005 3851 O ATOM 2071 N PHE A1065 169.710 14.806 579.886 1.00121.16 N ANISOU 2071 N PHE A1065 12579 21725 11732 -2354 -3366 3954 N ATOM 2072 CA PHE A1065 169.007 13.929 578.958 1.00132.77 C ANISOU 2072 CA PHE A1065 14151 22957 13340 -2665 -3537 4256 C ATOM 2073 C PHE A1065 167.950 13.083 579.655 1.00135.48 C ANISOU 2073 C PHE A1065 14206 23954 13315 -3117 -3793 4894 C ATOM 2074 O PHE A1065 167.003 12.639 578.998 1.00126.55 O ANISOU 2074 O PHE A1065 13053 22899 12131 -3335 -3859 5141 O ATOM 2075 CB PHE A1065 170.003 13.036 578.217 1.00129.77 C ANISOU 2075 CB PHE A1065 14112 21631 13562 -2789 -3764 4187 C ATOM 2076 CG PHE A1065 170.816 13.767 577.185 1.00123.49 C ANISOU 2076 CG PHE A1065 13611 20202 13108 -2447 -3486 3571 C ATOM 2077 CD1 PHE A1065 172.014 14.370 577.526 1.00114.93 C ANISOU 2077 CD1 PHE A1065 12614 18853 12200 -2164 -3349 3138 C ATOM 2078 CD2 PHE A1065 170.376 13.857 575.875 1.00114.85 C ANISOU 2078 CD2 PHE A1065 12708 18796 12134 -2439 -3365 3429 C ATOM 2079 CE1 PHE A1065 172.761 15.046 576.580 1.00120.05 C ANISOU 2079 CE1 PHE A1065 13530 18959 13124 -1911 -3088 2579 C ATOM 2080 CE2 PHE A1065 171.119 14.532 574.923 1.00111.81 C ANISOU 2080 CE2 PHE A1065 12608 17865 12009 -2194 -3113 2882 C ATOM 2081 CZ PHE A1065 172.313 15.126 575.277 1.00117.66 C ANISOU 2081 CZ PHE A1065 13428 18368 12908 -1945 -2968 2458 C ATOM 2082 N ASP A1066 168.084 12.851 580.964 1.00135.36 N ANISOU 2082 N ASP A1066 13976 24428 13027 -3292 -3944 5173 N ATOM 2083 CA ASP A1066 167.000 12.218 581.710 1.00142.67 C ANISOU 2083 CA ASP A1066 14589 26135 13483 -3754 -4133 5760 C ATOM 2084 C ASP A1066 165.756 13.098 581.704 1.00145.57 C ANISOU 2084 C ASP A1066 14614 27343 13353 -3605 -3812 5640 C ATOM 2085 O ASP A1066 164.653 12.637 581.380 1.00149.33 O ANISOU 2085 O ASP A1066 14944 28157 13638 -3900 -3882 5958 O ATOM 2086 CB ASP A1066 167.445 11.922 583.144 1.00150.91 C ANISOU 2086 CB ASP A1066 15483 27575 14280 -3974 -4337 6041 C ATOM 2087 CG ASP A1066 168.282 10.664 583.248 1.00154.75 C ANISOU 2087 CG ASP A1066 16250 27358 15192 -4316 -4834 6384 C ATOM 2088 OD1 ASP A1066 168.050 9.726 582.456 1.00155.69 O ANISOU 2088 OD1 ASP A1066 16550 26991 15613 -4591 -5102 6642 O ATOM 2089 OD2 ASP A1066 169.171 10.610 584.124 1.00156.52 O ANISOU 2089 OD2 ASP A1066 16510 27500 15459 -4301 -4987 6381 O ATOM 2090 N ILE A1067 165.917 14.376 582.058 1.00148.60 N ANISOU 2090 N ILE A1067 14855 28063 13544 -3135 -3480 5152 N ATOM 2091 CA ILE A1067 164.790 15.305 582.014 1.00145.98 C ANISOU 2091 CA ILE A1067 14191 28475 12800 -2912 -3207 4931 C ATOM 2092 C ILE A1067 164.257 15.427 580.592 1.00143.13 C ANISOU 2092 C ILE A1067 14031 27666 12686 -2786 -3136 4776 C ATOM 2093 O ILE A1067 163.040 15.494 580.369 1.00144.03 O ANISOU 2093 O ILE A1067 13890 28316 12518 -2871 -3096 4873 O ATOM 2094 CB ILE A1067 165.203 16.675 582.583 1.00147.89 C ANISOU 2094 CB ILE A1067 14297 29012 12881 -2381 -2919 4378 C ATOM 2095 CG1 ILE A1067 165.822 16.514 583.972 1.00151.53 C ANISOU 2095 CG1 ILE A1067 14594 29862 13120 -2513 -3004 4530 C ATOM 2096 CG2 ILE A1067 164.006 17.613 582.640 1.00152.41 C ANISOU 2096 CG2 ILE A1067 14478 30397 13035 -2137 -2703 4119 C ATOM 2097 CD1 ILE A1067 166.298 17.815 584.582 1.00149.81 C ANISOU 2097 CD1 ILE A1067 14245 29913 12764 -1996 -2744 3987 C ATOM 2098 N LEU A1068 165.160 15.446 579.607 1.00140.37 N ANISOU 2098 N LEU A1068 14130 26349 12855 -2602 -3125 4519 N ATOM 2099 CA LEU A1068 164.743 15.571 578.213 1.00136.00 C ANISOU 2099 CA LEU A1068 13813 25327 12533 -2503 -3062 4361 C ATOM 2100 C LEU A1068 163.872 14.394 577.790 1.00133.67 C ANISOU 2100 C LEU A1068 13477 25077 12236 -2980 -3307 4879 C ATOM 2101 O LEU A1068 162.822 14.578 577.166 1.00127.28 O ANISOU 2101 O LEU A1068 12571 24504 11287 -2970 -3251 4883 O ATOM 2102 CB LEU A1068 165.971 15.689 577.309 1.00130.98 C ANISOU 2102 CB LEU A1068 13655 23686 12425 -2308 -3012 4007 C ATOM 2103 CG LEU A1068 165.698 15.981 575.833 1.00118.40 C ANISOU 2103 CG LEU A1068 12361 21571 11053 -2185 -2915 3769 C ATOM 2104 CD1 LEU A1068 165.019 17.333 575.670 1.00117.96 C ANISOU 2104 CD1 LEU A1068 12197 21904 10719 -1785 -2683 3403 C ATOM 2105 CD2 LEU A1068 166.986 15.924 575.027 1.00118.44 C ANISOU 2105 CD2 LEU A1068 12806 20647 11550 -2103 -2875 3447 C ATOM 2106 N VAL A1069 164.294 13.172 578.125 1.00131.90 N ANISOU 2106 N VAL A1069 13331 24606 12180 -3402 -3615 5316 N ATOM 2107 CA VAL A1069 163.503 11.995 577.776 1.00131.47 C ANISOU 2107 CA VAL A1069 13250 24566 12135 -3891 -3897 5842 C ATOM 2108 C VAL A1069 162.183 11.993 578.538 1.00136.51 C ANISOU 2108 C VAL A1069 13411 26271 12184 -4143 -3884 6169 C ATOM 2109 O VAL A1069 161.146 11.573 578.009 1.00141.90 O ANISOU 2109 O VAL A1069 13994 27153 12769 -4378 -3955 6411 O ATOM 2110 CB VAL A1069 164.315 10.711 578.032 1.00132.04 C ANISOU 2110 CB VAL A1069 13527 24094 12546 -4275 -4299 6219 C ATOM 2111 CG1 VAL A1069 163.436 9.477 577.894 1.00135.15 C ANISOU 2111 CG1 VAL A1069 13856 24607 12888 -4834 -4645 6830 C ATOM 2112 CG2 VAL A1069 165.487 10.631 577.068 1.00128.17 C ANISOU 2112 CG2 VAL A1069 13469 22559 12671 -4045 -4313 5836 C ATOM 2113 N GLY A1070 162.193 12.475 579.783 1.00137.88 N ANISOU 2113 N GLY A1070 13264 27179 11945 -4104 -3784 6153 N ATOM 2114 CA GLY A1070 160.949 12.572 580.532 1.00141.18 C ANISOU 2114 CA GLY A1070 13173 28711 11759 -4334 -3725 6373 C ATOM 2115 C GLY A1070 159.935 13.476 579.857 1.00146.81 C ANISOU 2115 C GLY A1070 13691 29773 12319 -3995 -3468 6000 C ATOM 2116 O GLY A1070 158.780 13.091 579.644 1.00149.84 O ANISOU 2116 O GLY A1070 13832 30625 12476 -4275 -3524 6249 O ATOM 2117 N GLN A1071 160.356 14.693 579.500 1.00143.25 N ANISOU 2117 N GLN A1071 13353 29073 12001 -3394 -3215 5392 N ATOM 2118 CA GLN A1071 159.446 15.611 578.823 1.00142.05 C ANISOU 2118 CA GLN A1071 13063 29161 11749 -3033 -3036 5004 C ATOM 2119 C GLN A1071 159.063 15.106 577.436 1.00138.57 C ANISOU 2119 C GLN A1071 12931 28079 11639 -3137 -3146 5117 C ATOM 2120 O GLN A1071 157.951 15.378 576.967 1.00136.18 O ANISOU 2120 O GLN A1071 12429 28136 11177 -3078 -3114 5040 O ATOM 2121 CB GLN A1071 160.071 17.002 578.734 1.00139.34 C ANISOU 2121 CB GLN A1071 12842 28592 11508 -2395 -2808 4358 C ATOM 2122 CG GLN A1071 160.261 17.687 580.076 1.00135.83 C ANISOU 2122 CG GLN A1071 12024 28889 10694 -2214 -2676 4156 C ATOM 2123 CD GLN A1071 160.880 19.063 579.941 1.00133.05 C ANISOU 2123 CD GLN A1071 11818 28257 10477 -1583 -2488 3516 C ATOM 2124 OE1 GLN A1071 160.817 19.878 580.861 1.00134.72 O ANISOU 2124 OE1 GLN A1071 11691 29109 10387 -1314 -2366 3218 O ATOM 2125 NE2 GLN A1071 161.483 19.329 578.789 1.00129.06 N ANISOU 2125 NE2 GLN A1071 11820 26803 10415 -1366 -2474 3297 N ATOM 2126 N ILE A1072 159.963 14.379 576.768 1.00135.28 N ANISOU 2126 N ILE A1072 12984 26731 11687 -3282 -3288 5264 N ATOM 2127 CA ILE A1072 159.619 13.755 575.492 1.00133.78 C ANISOU 2127 CA ILE A1072 13076 25954 11802 -3444 -3418 5405 C ATOM 2128 C ILE A1072 158.485 12.757 575.681 1.00140.43 C ANISOU 2128 C ILE A1072 13621 27336 12400 -3959 -3620 5949 C ATOM 2129 O ILE A1072 157.536 12.711 574.887 1.00139.45 O ANISOU 2129 O ILE A1072 13456 27270 12259 -3990 -3637 5971 O ATOM 2130 CB ILE A1072 160.861 13.090 574.867 1.00128.73 C ANISOU 2130 CB ILE A1072 12935 24281 11697 -3526 -3548 5427 C ATOM 2131 CG1 ILE A1072 161.765 14.138 574.215 1.00124.10 C ANISOU 2131 CG1 ILE A1072 12692 23088 11372 -3036 -3317 4834 C ATOM 2132 CG2 ILE A1072 160.455 12.033 573.849 1.00128.20 C ANISOU 2132 CG2 ILE A1072 13069 23746 11896 -3868 -3774 5739 C ATOM 2133 CD1 ILE A1072 163.019 13.561 573.597 1.00121.52 C ANISOU 2133 CD1 ILE A1072 12804 21813 11557 -3103 -3406 4755 C ATOM 2134 N ASP A1073 158.558 11.949 576.742 1.00145.59 N ANISOU 2134 N ASP A1073 14069 28397 12850 -4394 -3794 6405 N ATOM 2135 CA ASP A1073 157.488 10.998 577.015 1.00142.37 C ANISOU 2135 CA ASP A1073 13370 28562 12161 -4955 -3998 6956 C ATOM 2136 C ASP A1073 156.200 11.701 577.420 1.00145.38 C ANISOU 2136 C ASP A1073 13214 29999 12024 -4874 -3786 6803 C ATOM 2137 O ASP A1073 155.108 11.197 577.134 1.00147.96 O ANISOU 2137 O ASP A1073 13356 30592 12270 -5166 -3806 7016 O ATOM 2138 CB ASP A1073 157.924 10.009 578.095 1.00145.50 C ANISOU 2138 CB ASP A1073 13733 29037 12514 -5452 -4199 7431 C ATOM 2139 CG ASP A1073 158.880 8.958 577.567 1.00143.84 C ANISOU 2139 CG ASP A1073 13995 27835 12822 -5672 -4566 7708 C ATOM 2140 OD1 ASP A1073 158.689 8.505 576.418 1.00142.23 O ANISOU 2140 OD1 ASP A1073 14032 27078 12929 -5718 -4710 7765 O ATOM 2141 OD2 ASP A1073 159.822 8.586 578.296 1.00148.16 O ANISOU 2141 OD2 ASP A1073 14668 28137 13490 -5785 -4718 7832 O ATOM 2142 N ASP A1074 156.298 12.860 578.078 1.00145.35 N ANISOU 2142 N ASP A1074 12955 30524 11746 -4455 -3537 6358 N ATOM 2143 CA ASP A1074 155.095 13.642 578.350 1.00148.18 C ANISOU 2143 CA ASP A1074 12800 31801 11700 -4274 -3324 6061 C ATOM 2144 C ASP A1074 154.459 14.137 577.056 1.00149.43 C ANISOU 2144 C ASP A1074 13078 31650 12050 -3943 -3315 5761 C ATOM 2145 O ASP A1074 153.232 14.089 576.899 1.00154.28 O ANISOU 2145 O ASP A1074 13336 32857 12428 -4062 -3320 5792 O ATOM 2146 CB ASP A1074 155.421 14.816 579.273 1.00148.49 C ANISOU 2146 CB ASP A1074 12568 32390 11462 -3838 -3099 5585 C ATOM 2147 CG ASP A1074 155.551 14.397 580.724 1.00152.43 C ANISOU 2147 CG ASP A1074 12782 33464 11669 -4211 -3001 5827 C ATOM 2148 OD1 ASP A1074 155.544 13.179 580.997 1.00154.61 O ANISOU 2148 OD1 ASP A1074 13142 33601 12003 -4809 -3148 6386 O ATOM 2149 OD2 ASP A1074 155.653 15.289 581.593 1.00153.60 O ANISOU 2149 OD2 ASP A1074 12629 34194 11539 -3914 -2798 5453 O ATOM 2150 N ALA A1075 155.280 14.612 576.114 1.00142.91 N ANISOU 2150 N ALA A1075 12768 29851 11679 -3543 -3278 5442 N ATOM 2151 CA ALA A1075 154.758 15.038 574.820 1.00139.40 C ANISOU 2151 CA ALA A1075 12534 28970 11460 -3266 -3279 5175 C ATOM 2152 C ALA A1075 154.149 13.873 574.052 1.00141.49 C ANISOU 2152 C ALA A1075 12906 28990 11865 -3728 -3489 5641 C ATOM 2153 O ALA A1075 153.170 14.056 573.319 1.00141.72 O ANISOU 2153 O ALA A1075 12847 29130 11871 -3649 -3516 5541 O ATOM 2154 CB ALA A1075 155.865 15.694 573.995 1.00134.51 C ANISOU 2154 CB ALA A1075 12485 27355 11267 -2848 -3205 4790 C ATOM 2155 N LEU A1076 154.717 12.675 574.199 1.00140.25 N ANISOU 2155 N LEU A1076 12943 28471 11874 -4199 -3672 6137 N ATOM 2156 CA LEU A1076 154.141 11.496 573.560 1.00141.45 C ANISOU 2156 CA LEU A1076 13178 28410 12158 -4672 -3913 6609 C ATOM 2157 C LEU A1076 152.797 11.138 574.186 1.00146.56 C ANISOU 2157 C LEU A1076 13255 30100 12332 -5049 -3957 6912 C ATOM 2158 O LEU A1076 151.845 10.790 573.474 1.00147.68 O ANISOU 2158 O LEU A1076 13335 30271 12506 -5194 -4027 7020 O ATOM 2159 CB LEU A1076 155.126 10.330 573.655 1.00140.78 C ANISOU 2159 CB LEU A1076 13428 27676 12388 -5061 -4155 7030 C ATOM 2160 CG LEU A1076 154.999 9.156 572.683 1.00142.60 C ANISOU 2160 CG LEU A1076 13956 27249 12977 -5425 -4440 7394 C ATOM 2161 CD1 LEU A1076 156.377 8.604 572.357 1.00139.13 C ANISOU 2161 CD1 LEU A1076 13998 25824 13039 -5434 -4591 7396 C ATOM 2162 CD2 LEU A1076 154.126 8.064 573.269 1.00145.28 C ANISOU 2162 CD2 LEU A1076 13995 28089 13114 -6038 -4623 7962 C ATOM 2163 N LYS A1077 152.701 11.227 575.516 1.00157.42 N ANISOU 2163 N LYS A1077 14245 32199 13368 -5189 -3793 6948 N ATOM 2164 CA LYS A1077 151.428 10.995 576.192 1.00155.32 C ANISOU 2164 CA LYS A1077 13435 32870 12712 -5521 -3664 7084 C ATOM 2165 C LYS A1077 150.365 11.970 575.704 1.00155.93 C ANISOU 2165 C LYS A1077 13189 33457 12599 -5114 -3534 6618 C ATOM 2166 O LYS A1077 149.286 11.559 575.262 1.00158.28 O ANISOU 2166 O LYS A1077 13303 33994 12843 -5340 -3573 6753 O ATOM 2167 CB LYS A1077 151.604 11.114 577.707 1.00161.87 C ANISOU 2167 CB LYS A1077 13909 34424 13170 -5690 -3484 7118 C ATOM 2168 CG LYS A1077 152.458 10.027 578.337 1.00162.47 C ANISOU 2168 CG LYS A1077 14234 34094 13403 -6188 -3656 7628 C ATOM 2169 CD LYS A1077 152.730 10.338 579.800 1.00165.47 C ANISOU 2169 CD LYS A1077 14294 35165 13412 -6275 -3477 7587 C ATOM 2170 CE LYS A1077 153.704 9.344 580.411 1.00163.27 C ANISOU 2170 CE LYS A1077 14313 34382 13339 -6706 -3701 8045 C ATOM 2171 NZ LYS A1077 154.037 9.697 581.819 1.00166.06 N ANISOU 2171 NZ LYS A1077 14386 35369 13339 -6771 -3540 7989 N ATOM 2172 N LEU A1078 150.656 13.273 575.774 1.00154.04 N ANISOU 2172 N LEU A1078 12881 33366 12280 -4501 -3405 6047 N ATOM 2173 CA LEU A1078 149.695 14.269 575.308 1.00161.79 C ANISOU 2173 CA LEU A1078 13575 34755 13144 -4053 -3340 5537 C ATOM 2174 C LEU A1078 149.381 14.097 573.828 1.00159.82 C ANISOU 2174 C LEU A1078 13675 33833 13216 -3973 -3555 5571 C ATOM 2175 O LEU A1078 148.281 14.442 573.383 1.00159.48 O ANISOU 2175 O LEU A1078 13368 34135 13094 -3827 -3565 5341 O ATOM 2176 CB LEU A1078 150.221 15.678 575.580 1.00159.11 C ANISOU 2176 CB LEU A1078 13191 34517 12746 -3392 -3230 4918 C ATOM 2177 CG LEU A1078 150.361 16.079 577.050 1.00159.61 C ANISOU 2177 CG LEU A1078 12826 35371 12449 -3371 -2992 4749 C ATOM 2178 CD1 LEU A1078 150.885 17.502 577.170 1.00156.40 C ANISOU 2178 CD1 LEU A1078 12422 34950 12053 -2670 -2924 4102 C ATOM 2179 CD2 LEU A1078 149.032 15.930 577.775 1.00164.55 C ANISOU 2179 CD2 LEU A1078 12797 37063 12661 -3632 -2822 4725 C ATOM 2180 N ALA A1079 150.329 13.567 573.052 1.00159.45 N ANISOU 2180 N ALA A1079 14258 32713 13611 -4046 -3656 5783 N ATOM 2181 CA ALA A1079 150.065 13.302 571.643 1.00159.67 C ANISOU 2181 CA ALA A1079 14679 31994 13995 -4017 -3793 5810 C ATOM 2182 C ALA A1079 149.115 12.125 571.462 1.00162.32 C ANISOU 2182 C ALA A1079 14810 32623 14242 -4589 -3978 6328 C ATOM 2183 O ALA A1079 148.349 12.094 570.492 1.00159.81 O ANISOU 2183 O ALA A1079 14551 32125 14044 -4539 -4071 6273 O ATOM 2184 CB ALA A1079 151.375 13.047 570.899 1.00153.50 C ANISOU 2184 CB ALA A1079 14585 30049 13690 -3959 -3832 5842 C ATOM 2185 N ASN A1080 149.145 11.154 572.379 1.00167.92 N ANISOU 2185 N ASN A1080 15329 33673 14801 -5131 -3989 6799 N ATOM 2186 CA ASN A1080 148.237 10.017 572.270 1.00172.39 C ANISOU 2186 CA ASN A1080 15749 34397 15355 -5693 -4082 7255 C ATOM 2187 C ASN A1080 146.825 10.357 572.731 1.00176.86 C ANISOU 2187 C ASN A1080 15687 36004 15508 -5733 -3915 7092 C ATOM 2188 O ASN A1080 145.857 9.791 572.211 1.00180.85 O ANISOU 2188 O ASN A1080 16080 36611 16023 -5999 -3998 7283 O ATOM 2189 CB ASN A1080 148.769 8.830 573.073 1.00175.30 C ANISOU 2189 CB ASN A1080 16195 34646 15765 -6285 -4158 7806 C ATOM 2190 CG ASN A1080 150.103 8.331 572.560 1.00171.27 C ANISOU 2190 CG ASN A1080 16285 33071 15717 -6279 -4369 7958 C ATOM 2191 OD1 ASN A1080 150.987 7.985 573.340 1.00169.75 O ANISOU 2191 OD1 ASN A1080 16195 32732 15570 -6442 -4399 8130 O ATOM 2192 ND2 ASN A1080 150.256 8.294 571.241 1.00168.70 N ANISOU 2192 ND2 ASN A1080 16354 32007 15736 -6094 -4528 7873 N ATOM 2193 N GLU A1081 146.682 11.267 573.698 1.00178.02 N ANISOU 2193 N GLU A1081 15408 36938 15295 -5469 -3679 6714 N ATOM 2194 CA GLU A1081 145.360 11.624 574.202 1.00181.97 C ANISOU 2194 CA GLU A1081 15268 38486 15385 -5489 -3500 6483 C ATOM 2195 C GLU A1081 144.563 12.476 573.223 1.00185.41 C ANISOU 2195 C GLU A1081 15621 38905 15923 -4973 -3561 5977 C ATOM 2196 O GLU A1081 143.370 12.698 573.454 1.00194.21 O ANISOU 2196 O GLU A1081 16221 40805 16763 -4977 -3453 5755 O ATOM 2197 CB GLU A1081 145.483 12.368 575.535 1.00181.01 C ANISOU 2197 CB GLU A1081 14712 39203 14859 -5335 -3232 6168 C ATOM 2198 CG GLU A1081 146.445 11.746 576.543 1.00181.70 C ANISOU 2198 CG GLU A1081 14922 39251 14864 -5740 -3190 6584 C ATOM 2199 CD GLU A1081 145.993 10.390 577.053 1.00183.21 C ANISOU 2199 CD GLU A1081 14992 39735 14885 -6571 -3229 7255 C ATOM 2200 OE1 GLU A1081 146.095 9.397 576.302 1.00179.17 O ANISOU 2200 OE1 GLU A1081 14856 38509 14710 -6907 -3472 7705 O ATOM 2201 OE2 GLU A1081 145.536 10.317 578.213 1.00187.13 O ANISOU 2201 OE2 GLU A1081 15018 41179 14904 -6906 -3025 7327 O ATOM 2202 N GLY A1082 145.184 12.952 572.145 1.00180.55 N ANISOU 2202 N GLY A1082 15500 37422 15681 -4549 -3740 5782 N ATOM 2203 CA GLY A1082 144.538 13.847 571.206 1.00179.95 C ANISOU 2203 CA GLY A1082 15411 37243 15719 -4033 -3849 5292 C ATOM 2204 C GLY A1082 144.990 15.287 571.299 1.00178.33 C ANISOU 2204 C GLY A1082 15216 37030 15512 -3337 -3813 4657 C ATOM 2205 O GLY A1082 144.529 16.114 570.504 1.00180.75 O ANISOU 2205 O GLY A1082 15577 37150 15951 -2869 -3947 4222 O ATOM 2206 N LYS A1083 145.871 15.615 572.241 1.00171.84 N ANISOU 2206 N LYS A1083 14368 36358 14565 -3252 -3655 4585 N ATOM 2207 CA LYS A1083 146.381 16.975 572.400 1.00166.39 C ANISOU 2207 CA LYS A1083 13720 35600 13899 -2595 -3604 3979 C ATOM 2208 C LYS A1083 147.716 17.110 571.667 1.00161.31 C ANISOU 2208 C LYS A1083 13878 33723 13690 -2412 -3613 4008 C ATOM 2209 O LYS A1083 148.792 17.178 572.262 1.00161.21 O ANISOU 2209 O LYS A1083 14042 33513 13697 -2400 -3492 4049 O ATOM 2210 CB LYS A1083 146.516 17.318 573.882 1.00169.02 C ANISOU 2210 CB LYS A1083 13571 36776 13875 -2581 -3354 3805 C ATOM 2211 CG LYS A1083 145.203 17.364 574.650 1.00177.79 C ANISOU 2211 CG LYS A1083 13967 38965 14621 -2690 -3174 3600 C ATOM 2212 CD LYS A1083 144.463 18.669 574.407 1.00167.65 C ANISOU 2212 CD LYS A1083 12403 37941 13354 -2013 -3220 2829 C ATOM 2213 CE LYS A1083 143.324 18.849 575.397 1.00174.30 C ANISOU 2213 CE LYS A1083 12501 39934 13791 -2067 -2984 2512 C ATOM 2214 NZ LYS A1083 142.700 20.196 575.286 1.00178.75 N ANISOU 2214 NZ LYS A1083 12794 40713 14410 -1347 -3045 1680 N ATOM 2215 N VAL A1084 147.622 17.146 570.336 1.00158.64 N ANISOU 2215 N VAL A1084 14018 32567 13692 -2286 -3761 3971 N ATOM 2216 CA VAL A1084 148.821 17.275 569.512 1.00143.21 C ANISOU 2216 CA VAL A1084 12815 29468 12129 -2153 -3763 3962 C ATOM 2217 C VAL A1084 149.403 18.680 569.631 1.00141.68 C ANISOU 2217 C VAL A1084 12777 29070 11983 -1551 -3696 3384 C ATOM 2218 O VAL A1084 150.627 18.865 569.625 1.00138.30 O ANISOU 2218 O VAL A1084 12779 28033 11736 -1473 -3597 3353 O ATOM 2219 CB VAL A1084 148.501 16.912 568.051 1.00147.03 C ANISOU 2219 CB VAL A1084 13749 29203 12911 -2233 -3940 4080 C ATOM 2220 CG1 VAL A1084 149.779 16.835 567.228 1.00142.13 C ANISOU 2220 CG1 VAL A1084 13873 27473 12659 -2226 -3916 4119 C ATOM 2221 CG2 VAL A1084 147.735 15.599 567.986 1.00143.71 C ANISOU 2221 CG2 VAL A1084 13089 29094 12420 -2798 -4038 4609 C ATOM 2222 N LYS A1085 148.536 19.690 569.739 1.00147.44 N ANISOU 2222 N LYS A1085 13154 30299 12569 -1115 -3773 2898 N ATOM 2223 CA LYS A1085 149.002 21.062 569.914 1.00143.60 C ANISOU 2223 CA LYS A1085 12779 29658 12125 -529 -3766 2330 C ATOM 2224 C LYS A1085 149.806 21.201 571.201 1.00154.62 C ANISOU 2224 C LYS A1085 13941 31475 13334 -519 -3548 2299 C ATOM 2225 O LYS A1085 150.893 21.795 571.213 1.00154.69 O ANISOU 2225 O LYS A1085 14345 30928 13501 -280 -3477 2115 O ATOM 2226 CB LYS A1085 147.811 22.023 569.913 1.00150.95 C ANISOU 2226 CB LYS A1085 13272 31148 12933 -74 -3946 1801 C ATOM 2227 CG LYS A1085 146.659 21.610 569.000 1.00149.19 C ANISOU 2227 CG LYS A1085 12992 30923 12770 -200 -4156 1904 C ATOM 2228 CD LYS A1085 145.592 20.827 569.762 1.00153.70 C ANISOU 2228 CD LYS A1085 12798 32596 13004 -558 -4093 2106 C ATOM 2229 CE LYS A1085 144.514 20.297 568.830 1.00155.19 C ANISOU 2229 CE LYS A1085 12954 32738 13272 -737 -4293 2260 C ATOM 2230 NZ LYS A1085 143.502 19.484 569.561 1.00159.77 N ANISOU 2230 NZ LYS A1085 12795 34401 13509 -1156 -4222 2486 N ATOM 2231 N GLU A1086 149.284 20.651 572.301 1.00153.88 N ANISOU 2231 N GLU A1086 13205 32381 12882 -807 -3444 2483 N ATOM 2232 CA GLU A1086 150.027 20.625 573.553 1.00151.85 C ANISOU 2232 CA GLU A1086 12728 32557 12412 -887 -3250 2532 C ATOM 2233 C GLU A1086 151.305 19.805 573.443 1.00148.19 C ANISOU 2233 C GLU A1086 12797 31335 12173 -1237 -3176 2991 C ATOM 2234 O GLU A1086 152.232 20.013 574.232 1.00147.96 O ANISOU 2234 O GLU A1086 12797 31322 12098 -1175 -3045 2944 O ATOM 2235 CB GLU A1086 149.147 20.076 574.680 1.00161.24 C ANISOU 2235 CB GLU A1086 13145 34991 13130 -1241 -3171 2704 C ATOM 2236 CG GLU A1086 148.081 21.043 575.185 1.00170.53 C ANISOU 2236 CG GLU A1086 13647 37126 14021 -832 -3186 2103 C ATOM 2237 CD GLU A1086 146.897 21.180 574.243 1.00177.44 C ANISOU 2237 CD GLU A1086 14420 37997 15000 -695 -3381 1918 C ATOM 2238 OE1 GLU A1086 146.877 20.499 573.196 1.00177.37 O ANISOU 2238 OE1 GLU A1086 14859 37283 15250 -944 -3500 2292 O ATOM 2239 OE2 GLU A1086 145.981 21.970 574.554 1.00183.81 O ANISOU 2239 OE2 GLU A1086 14769 39366 15703 -326 -3357 1359 O ATOM 2240 N ALA A1087 151.373 18.874 572.488 1.00147.00 N ANISOU 2240 N ALA A1087 13049 30528 12276 -1590 -3276 3403 N ATOM 2241 CA ALA A1087 152.625 18.169 572.242 1.00137.91 C ANISOU 2241 CA ALA A1087 12428 28562 11411 -1852 -3244 3731 C ATOM 2242 C ALA A1087 153.626 19.056 571.513 1.00146.23 C ANISOU 2242 C ALA A1087 14066 28707 12787 -1440 -3205 3350 C ATOM 2243 O ALA A1087 154.837 18.924 571.723 1.00139.52 O ANISOU 2243 O ALA A1087 13520 27392 12101 -1485 -3112 3400 O ATOM 2244 CB ALA A1087 152.367 16.888 571.450 1.00137.47 C ANISOU 2244 CB ALA A1087 12588 28110 11535 -2350 -3386 4244 C ATOM 2245 N GLN A1088 153.145 19.960 570.655 1.00151.67 N ANISOU 2245 N GLN A1088 14926 29132 13569 -1060 -3296 2968 N ATOM 2246 CA GLN A1088 154.041 20.924 570.022 1.00154.17 C ANISOU 2246 CA GLN A1088 15787 28659 14131 -691 -3277 2592 C ATOM 2247 C GLN A1088 154.561 21.935 571.039 1.00165.84 C ANISOU 2247 C GLN A1088 17068 30475 15471 -302 -3162 2203 C ATOM 2248 O GLN A1088 155.759 22.250 571.065 1.00162.47 O ANISOU 2248 O GLN A1088 17011 29510 15209 -210 -3055 2090 O ATOM 2249 CB GLN A1088 153.323 21.628 568.869 1.00146.67 C ANISOU 2249 CB GLN A1088 15085 27353 13290 -421 -3468 2317 C ATOM 2250 CG GLN A1088 152.982 20.710 567.705 1.00139.38 C ANISOU 2250 CG GLN A1088 14474 25938 12548 -782 -3579 2662 C ATOM 2251 CD GLN A1088 152.281 21.434 566.572 1.00137.37 C ANISOU 2251 CD GLN A1088 14489 25321 12385 -521 -3797 2395 C ATOM 2252 OE1 GLN A1088 151.627 22.455 566.783 1.00140.44 O ANISOU 2252 OE1 GLN A1088 14643 26061 12657 -98 -3925 1997 O ATOM 2253 NE2 GLN A1088 152.419 20.909 565.360 1.00127.78 N ANISOU 2253 NE2 GLN A1088 13772 23392 11386 -771 -3870 2593 N ATOM 2254 N ALA A1089 153.671 22.458 571.889 1.00185.21 N ANISOU 2254 N ALA A1089 18913 33841 17618 -69 -3183 1963 N ATOM 2255 CA ALA A1089 154.122 23.310 572.985 1.00184.91 C ANISOU 2255 CA ALA A1089 18608 34233 17418 270 -3073 1608 C ATOM 2256 C ALA A1089 155.092 22.560 573.890 1.00180.33 C ANISOU 2256 C ALA A1089 17991 33748 16776 -60 -2887 1943 C ATOM 2257 O ALA A1089 156.079 23.132 574.372 1.00180.42 O ANISOU 2257 O ALA A1089 18147 33561 16841 159 -2781 1725 O ATOM 2258 CB ALA A1089 152.923 23.822 573.783 1.00190.44 C ANISOU 2258 CB ALA A1089 18574 36013 17773 509 -3123 1297 C ATOM 2259 N ALA A1090 154.831 21.271 574.122 1.00179.78 N ANISOU 2259 N ALA A1090 17747 33954 16608 -598 -2880 2479 N ATOM 2260 CA ALA A1090 155.772 20.448 574.871 1.00176.48 C ANISOU 2260 CA ALA A1090 17370 33502 16183 -954 -2784 2847 C ATOM 2261 C ALA A1090 157.106 20.330 574.148 1.00168.45 C ANISOU 2261 C ALA A1090 17025 31394 15585 -957 -2757 2868 C ATOM 2262 O ALA A1090 158.149 20.190 574.794 1.00128.47 O ANISOU 2262 O ALA A1090 12050 26188 10574 -1008 -2669 2917 O ATOM 2263 CB ALA A1090 155.175 19.064 575.123 1.00173.27 C ANISOU 2263 CB ALA A1090 16709 33507 15621 -1561 -2861 3444 C ATOM 2264 N ALA A1091 157.095 20.379 572.813 1.00157.10 N ANISOU 2264 N ALA A1091 16050 29204 14437 -919 -2835 2813 N ATOM 2265 CA ALA A1091 158.351 20.431 572.073 1.00149.65 C ANISOU 2265 CA ALA A1091 15720 27279 13860 -899 -2782 2724 C ATOM 2266 C ALA A1091 159.070 21.752 572.312 1.00152.39 C ANISOU 2266 C ALA A1091 16217 27455 14230 -426 -2678 2217 C ATOM 2267 O ALA A1091 160.305 21.792 572.382 1.00149.94 O ANISOU 2267 O ALA A1091 16211 26646 14114 -425 -2571 2142 O ATOM 2268 CB ALA A1091 158.100 20.213 570.582 1.00145.84 C ANISOU 2268 CB ALA A1091 15679 26109 13623 -1000 -2886 2765 C ATOM 2269 N GLU A1092 158.314 22.848 572.438 1.00160.09 N ANISOU 2269 N GLU A1092 16972 28830 15026 -15 -2731 1843 N ATOM 2270 CA GLU A1092 158.931 24.106 572.847 1.00163.77 C ANISOU 2270 CA GLU A1092 17509 29228 15487 441 -2670 1366 C ATOM 2271 C GLU A1092 159.573 23.970 574.224 1.00166.04 C ANISOU 2271 C GLU A1092 17468 30001 15618 424 -2522 1403 C ATOM 2272 O GLU A1092 160.660 24.511 574.469 1.00165.76 O ANISOU 2272 O GLU A1092 17668 29607 15707 605 -2422 1177 O ATOM 2273 CB GLU A1092 157.896 25.233 572.835 1.00170.33 C ANISOU 2273 CB GLU A1092 18088 30470 16161 894 -2821 947 C ATOM 2274 CG GLU A1092 158.488 26.640 572.794 1.00173.11 C ANISOU 2274 CG GLU A1092 18702 30464 16608 1381 -2858 427 C ATOM 2275 CD GLU A1092 159.012 27.106 574.140 1.00177.16 C ANISOU 2275 CD GLU A1092 18861 31495 16957 1608 -2725 211 C ATOM 2276 OE1 GLU A1092 158.464 26.673 575.176 1.00181.42 O ANISOU 2276 OE1 GLU A1092 18803 32919 17211 1519 -2663 329 O ATOM 2277 OE2 GLU A1092 159.975 27.901 574.162 1.00176.77 O ANISOU 2277 OE2 GLU A1092 19133 30984 17048 1847 -2685 -73 O ATOM 2278 N GLN A1093 158.919 23.242 575.135 1.00167.42 N ANISOU 2278 N GLN A1093 17106 31001 15506 177 -2513 1696 N ATOM 2279 CA GLN A1093 159.537 22.954 576.427 1.00167.19 C ANISOU 2279 CA GLN A1093 16799 31421 15306 67 -2398 1814 C ATOM 2280 C GLN A1093 160.819 22.145 576.253 1.00161.26 C ANISOU 2280 C GLN A1093 16476 29942 14855 -233 -2356 2094 C ATOM 2281 O GLN A1093 161.810 22.375 576.959 1.00161.63 O ANISOU 2281 O GLN A1093 16562 29916 14935 -135 -2262 1980 O ATOM 2282 CB GLN A1093 158.551 22.208 577.329 1.00174.93 C ANISOU 2282 CB GLN A1093 17167 33409 15891 -257 -2421 2143 C ATOM 2283 CG GLN A1093 157.157 22.820 577.392 1.00181.73 C ANISOU 2283 CG GLN A1093 17546 35033 16469 -24 -2477 1868 C ATOM 2284 CD GLN A1093 157.118 24.142 578.135 1.00185.68 C ANISOU 2284 CD GLN A1093 17738 36020 16793 520 -2423 1277 C ATOM 2285 OE1 GLN A1093 158.065 24.507 578.832 1.00186.32 O ANISOU 2285 OE1 GLN A1093 17875 36042 16876 663 -2319 1139 O ATOM 2286 NE2 GLN A1093 156.015 24.867 577.992 1.00188.43 N ANISOU 2286 NE2 GLN A1093 17746 36847 17003 842 -2520 898 N ATOM 2287 N LEU A1094 160.813 21.189 575.318 1.00158.21 N ANISOU 2287 N LEU A1094 16394 29015 14705 -589 -2441 2430 N ATOM 2288 CA LEU A1094 162.028 20.441 575.006 1.00155.60 C ANISOU 2288 CA LEU A1094 16474 27930 14718 -838 -2433 2608 C ATOM 2289 C LEU A1094 163.148 21.376 574.575 1.00147.36 C ANISOU 2289 C LEU A1094 15856 26208 13926 -507 -2310 2157 C ATOM 2290 O LEU A1094 164.309 21.186 574.957 1.00147.61 O ANISOU 2290 O LEU A1094 16034 25921 14129 -549 -2245 2128 O ATOM 2291 CB LEU A1094 161.750 19.412 573.911 1.00155.51 C ANISOU 2291 CB LEU A1094 16724 27426 14937 -1207 -2561 2937 C ATOM 2292 CG LEU A1094 160.704 18.333 574.189 1.00122.68 C ANISOU 2292 CG LEU A1094 12215 23817 10582 -1617 -2714 3440 C ATOM 2293 CD1 LEU A1094 160.494 17.463 572.960 1.00121.57 C ANISOU 2293 CD1 LEU A1094 12393 23078 10719 -1913 -2846 3683 C ATOM 2294 CD2 LEU A1094 161.125 17.492 575.375 1.00124.44 C ANISOU 2294 CD2 LEU A1094 12198 24393 10693 -1934 -2776 3802 C ATOM 2295 N LYS A1095 162.820 22.388 573.769 1.00141.40 N ANISOU 2295 N LYS A1095 15312 25215 13199 -196 -2301 1803 N ATOM 2296 CA LYS A1095 163.817 23.386 573.400 1.00142.25 C ANISOU 2296 CA LYS A1095 15819 24738 13492 94 -2199 1374 C ATOM 2297 C LYS A1095 164.295 24.157 574.624 1.00144.26 C ANISOU 2297 C LYS A1095 15812 25409 13591 408 -2107 1112 C ATOM 2298 O LYS A1095 165.486 24.477 574.742 1.00142.99 O ANISOU 2298 O LYS A1095 15902 24821 13608 492 -1998 908 O ATOM 2299 CB LYS A1095 163.236 24.335 572.351 1.00145.36 C ANISOU 2299 CB LYS A1095 16487 24842 13902 336 -2279 1090 C ATOM 2300 CG LYS A1095 164.271 25.096 571.542 1.00146.43 C ANISOU 2300 CG LYS A1095 17193 24174 14271 446 -2207 757 C ATOM 2301 CD LYS A1095 163.605 25.911 570.444 1.00148.71 C ANISOU 2301 CD LYS A1095 17794 24152 14555 602 -2353 559 C ATOM 2302 CE LYS A1095 164.631 26.561 569.531 1.00147.30 C ANISOU 2302 CE LYS A1095 18233 23159 14576 590 -2290 290 C ATOM 2303 NZ LYS A1095 165.460 25.550 568.820 1.00144.89 N ANISOU 2303 NZ LYS A1095 18237 22311 14503 155 -2158 471 N ATOM 2304 N THR A1096 163.381 24.451 575.553 1.00149.57 N ANISOU 2304 N THR A1096 15958 26949 13925 574 -2146 1092 N ATOM 2305 CA THR A1096 163.748 25.185 576.762 1.00151.55 C ANISOU 2305 CA THR A1096 15911 27678 13992 877 -2066 824 C ATOM 2306 C THR A1096 164.776 24.417 577.587 1.00148.77 C ANISOU 2306 C THR A1096 15527 27303 13696 630 -1982 1057 C ATOM 2307 O THR A1096 165.841 24.949 577.920 1.00147.50 O ANISOU 2307 O THR A1096 15532 26850 13661 822 -1888 798 O ATOM 2308 CB THR A1096 162.502 25.478 577.600 1.00159.69 C ANISOU 2308 CB THR A1096 16320 29733 14621 1033 -2120 764 C ATOM 2309 OG1 THR A1096 161.655 26.396 576.897 1.00163.30 O ANISOU 2309 OG1 THR A1096 16809 30166 15071 1369 -2239 428 O ATOM 2310 CG2 THR A1096 162.891 26.078 578.945 1.00164.02 C ANISOU 2310 CG2 THR A1096 16513 30858 14949 1289 -2030 517 C ATOM 2311 N THR A1097 164.471 23.163 577.931 1.00144.22 N ANISOU 2311 N THR A1097 14745 27018 13033 194 -2048 1550 N ATOM 2312 CA THR A1097 165.409 22.384 578.737 1.00140.96 C ANISOU 2312 CA THR A1097 14314 26563 12683 -56 -2046 1798 C ATOM 2313 C THR A1097 166.685 22.076 577.962 1.00140.58 C ANISOU 2313 C THR A1097 14792 25522 13098 -140 -2022 1735 C ATOM 2314 O THR A1097 167.781 22.058 578.540 1.00141.21 O ANISOU 2314 O THR A1097 14945 25399 13309 -106 -1979 1646 O ATOM 2315 CB THR A1097 164.750 21.092 579.219 1.00142.27 C ANISOU 2315 CB THR A1097 14183 27217 12655 -547 -2188 2370 C ATOM 2316 OG1 THR A1097 164.195 20.388 578.101 1.00146.20 O ANISOU 2316 OG1 THR A1097 14881 27342 13325 -808 -2292 2618 O ATOM 2317 CG2 THR A1097 163.649 21.401 580.221 1.00143.06 C ANISOU 2317 CG2 THR A1097 13691 28425 12240 -504 -2172 2392 C ATOM 2318 N ARG A1098 166.564 21.834 576.654 1.00141.06 N ANISOU 2318 N ARG A1098 15207 24982 13405 -255 -2051 1752 N ATOM 2319 CA ARG A1098 167.740 21.569 575.832 1.00141.00 C ANISOU 2319 CA ARG A1098 15673 24080 13820 -352 -2009 1625 C ATOM 2320 C ARG A1098 168.717 22.736 575.884 1.00147.74 C ANISOU 2320 C ARG A1098 16739 24623 14771 7 -1843 1122 C ATOM 2321 O ARG A1098 169.916 22.548 576.119 1.00146.32 O ANISOU 2321 O ARG A1098 16703 24066 14824 -27 -1788 1008 O ATOM 2322 CB ARG A1098 167.325 21.285 574.389 1.00137.71 C ANISOU 2322 CB ARG A1098 15582 23162 13581 -514 -2049 1670 C ATOM 2323 CG ARG A1098 168.496 20.991 573.465 1.00132.75 C ANISOU 2323 CG ARG A1098 15412 21666 13361 -649 -1988 1493 C ATOM 2324 CD ARG A1098 168.213 21.465 572.051 1.00128.26 C ANISOU 2324 CD ARG A1098 15225 20634 12872 -636 -1942 1300 C ATOM 2325 NE ARG A1098 168.009 22.910 571.998 1.00124.61 N ANISOU 2325 NE ARG A1098 14846 20269 12231 -260 -1859 941 N ATOM 2326 CZ ARG A1098 167.763 23.590 570.884 1.00121.87 C ANISOU 2326 CZ ARG A1098 14856 19549 11901 -202 -1852 739 C ATOM 2327 NH1 ARG A1098 167.691 22.958 569.721 1.00121.09 N ANISOU 2327 NH1 ARG A1098 15051 18993 11965 -499 -1883 849 N ATOM 2328 NH2 ARG A1098 167.591 24.904 570.931 1.00120.18 N ANISOU 2328 NH2 ARG A1098 14716 19408 11538 146 -1845 424 N ATOM 2329 N ASN A1099 168.220 23.958 575.668 1.00162.69 N ANISOU 2329 N ASN A1099 18654 26657 16503 353 -1791 804 N ATOM 2330 CA ASN A1099 169.081 25.126 575.803 1.00168.27 C ANISOU 2330 CA ASN A1099 19548 27112 17275 691 -1668 341 C ATOM 2331 C ASN A1099 169.495 25.371 577.247 1.00173.88 C ANISOU 2331 C ASN A1099 19907 28330 17829 878 -1626 270 C ATOM 2332 O ASN A1099 170.519 26.022 577.483 1.00175.18 O ANISOU 2332 O ASN A1099 20231 28210 18121 1072 -1523 -53 O ATOM 2333 CB ASN A1099 168.390 26.367 575.239 1.00173.22 C ANISOU 2333 CB ASN A1099 20294 27742 17778 1016 -1704 32 C ATOM 2334 CG ASN A1099 168.687 26.578 573.769 1.00176.91 C ANISOU 2334 CG ASN A1099 21318 27426 18473 894 -1692 -96 C ATOM 2335 OD1 ASN A1099 167.941 26.127 572.901 1.00179.07 O ANISOU 2335 OD1 ASN A1099 21699 27584 18754 702 -1781 102 O ATOM 2336 ND2 ASN A1099 169.789 27.263 573.482 1.00176.75 N ANISOU 2336 ND2 ASN A1099 21654 26880 18621 976 -1579 -429 N ATOM 2337 N ALA A1100 168.727 24.868 578.216 1.00171.68 N ANISOU 2337 N ALA A1100 19156 28817 17259 798 -1703 563 N ATOM 2338 CA ALA A1100 169.143 24.974 579.609 1.00168.41 C ANISOU 2338 CA ALA A1100 18411 28909 16667 907 -1672 538 C ATOM 2339 C ALA A1100 170.349 24.091 579.899 1.00161.60 C ANISOU 2339 C ALA A1100 17699 27630 16070 650 -1683 704 C ATOM 2340 O ALA A1100 171.153 24.413 580.781 1.00162.00 O ANISOU 2340 O ALA A1100 17668 27770 16115 805 -1632 538 O ATOM 2341 CB ALA A1100 167.983 24.616 580.537 1.00170.52 C ANISOU 2341 CB ALA A1100 18133 30152 16507 808 -1750 821 C ATOM 2342 N TYR A1101 170.495 22.985 579.173 1.00155.76 N ANISOU 2342 N TYR A1101 17173 26425 15585 277 -1774 1001 N ATOM 2343 CA TYR A1101 171.619 22.070 579.336 1.00150.63 C ANISOU 2343 CA TYR A1101 16670 25309 15252 38 -1848 1124 C ATOM 2344 C TYR A1101 172.369 21.883 578.022 1.00148.46 C ANISOU 2344 C TYR A1101 16854 24145 15411 -56 -1795 922 C ATOM 2345 O TYR A1101 172.721 20.765 577.639 1.00148.86 O ANISOU 2345 O TYR A1101 17022 23800 15738 -372 -1931 1136 O ATOM 2346 CB TYR A1101 171.145 20.725 579.883 1.00151.94 C ANISOU 2346 CB TYR A1101 16606 25801 15324 -373 -2082 1691 C ATOM 2347 CG TYR A1101 170.339 20.834 581.158 1.00156.49 C ANISOU 2347 CG TYR A1101 16711 27339 15410 -374 -2124 1916 C ATOM 2348 CD1 TYR A1101 170.769 21.632 582.210 1.00159.24 C ANISOU 2348 CD1 TYR A1101 16867 28072 15567 -87 -2025 1663 C ATOM 2349 CD2 TYR A1101 169.141 20.149 581.303 1.00159.11 C ANISOU 2349 CD2 TYR A1101 16775 28228 15451 -680 -2255 2359 C ATOM 2350 CE1 TYR A1101 170.032 21.736 583.376 1.00162.36 C ANISOU 2350 CE1 TYR A1101 16805 29405 15478 -109 -2047 1830 C ATOM 2351 CE2 TYR A1101 168.397 20.247 582.464 1.00162.36 C ANISOU 2351 CE2 TYR A1101 16726 29591 15372 -729 -2270 2535 C ATOM 2352 CZ TYR A1101 168.847 21.042 583.496 1.00162.38 C ANISOU 2352 CZ TYR A1101 16535 29987 15176 -444 -2161 2260 C ATOM 2353 OH TYR A1101 168.108 21.142 584.653 1.00162.60 O ANISOU 2353 OH TYR A1101 16081 31017 14684 -514 -2161 2400 O ATOM 2354 N ILE A1102 172.626 22.985 577.311 1.00146.36 N ANISOU 2354 N ILE A1102 16850 23561 15200 201 -1616 491 N ATOM 2355 CA ILE A1102 173.300 22.927 576.016 1.00142.66 C ANISOU 2355 CA ILE A1102 16816 22316 15071 78 -1532 262 C ATOM 2356 C ILE A1102 174.788 23.244 576.110 1.00137.58 C ANISOU 2356 C ILE A1102 16361 21205 14707 164 -1402 -134 C ATOM 2357 O ILE A1102 175.522 23.002 575.138 1.00136.20 O ANISOU 2357 O ILE A1102 16499 20415 14837 -5 -1329 -341 O ATOM 2358 CB ILE A1102 172.626 23.874 574.997 1.00142.12 C ANISOU 2358 CB ILE A1102 16988 22131 14883 210 -1450 70 C ATOM 2359 CG1 ILE A1102 172.886 23.404 573.563 1.00140.95 C ANISOU 2359 CG1 ILE A1102 17232 21323 14999 -75 -1421 24 C ATOM 2360 CG2 ILE A1102 173.109 25.304 575.192 1.00140.56 C ANISOU 2360 CG2 ILE A1102 16909 21887 14612 570 -1312 -376 C ATOM 2361 CD1 ILE A1102 172.241 24.275 572.509 1.00140.05 C ANISOU 2361 CD1 ILE A1102 17406 21046 14761 0 -1383 -127 C ATOM 2362 N GLN A1103 175.260 23.766 577.245 1.00134.01 N ANISOU 2362 N GLN A1103 15711 21051 14156 408 -1368 -268 N ATOM 2363 CA GLN A1103 176.670 24.117 577.377 1.00127.42 C ANISOU 2363 CA GLN A1103 15033 19799 13584 504 -1245 -666 C ATOM 2364 C GLN A1103 177.581 22.897 577.353 1.00119.76 C ANISOU 2364 C GLN A1103 14088 18423 12992 235 -1355 -603 C ATOM 2365 O GLN A1103 178.794 23.050 577.172 1.00114.66 O ANISOU 2365 O GLN A1103 13602 17327 12637 258 -1249 -985 O ATOM 2366 CB GLN A1103 176.900 24.909 578.667 1.00130.92 C ANISOU 2366 CB GLN A1103 15229 20691 13823 834 -1212 -802 C ATOM 2367 CG GLN A1103 176.325 26.321 578.659 1.00133.94 C ANISOU 2367 CG GLN A1103 15626 21338 13927 1177 -1111 -1046 C ATOM 2368 CD GLN A1103 174.815 26.350 578.820 1.00139.20 C ANISOU 2368 CD GLN A1103 16035 22615 14238 1224 -1220 -755 C ATOM 2369 OE1 GLN A1103 174.182 25.318 579.046 1.00141.47 O ANISOU 2369 OE1 GLN A1103 16110 23198 14442 979 -1350 -335 O ATOM 2370 NE2 GLN A1103 174.232 27.537 578.704 1.00141.01 N ANISOU 2370 NE2 GLN A1103 16278 23034 14266 1534 -1191 -995 N ATOM 2371 N LYS A1104 177.031 21.694 577.529 1.00121.47 N ANISOU 2371 N LYS A1104 14145 18782 13225 -22 -1589 -151 N ATOM 2372 CA LYS A1104 177.847 20.487 577.483 1.00121.74 C ANISOU 2372 CA LYS A1104 14210 18388 13659 -267 -1776 -95 C ATOM 2373 C LYS A1104 178.261 20.122 576.063 1.00119.28 C ANISOU 2373 C LYS A1104 14201 17431 13687 -463 -1706 -339 C ATOM 2374 O LYS A1104 179.225 19.369 575.887 1.00119.03 O ANISOU 2374 O LYS A1104 14221 16943 14060 -593 -1808 -514 O ATOM 2375 CB LYS A1104 177.095 19.318 578.120 1.00122.53 C ANISOU 2375 CB LYS A1104 14070 18825 13661 -514 -2103 494 C ATOM 2376 CG LYS A1104 176.612 19.578 579.538 1.00106.90 C ANISOU 2376 CG LYS A1104 11763 17571 11283 -401 -2176 768 C ATOM 2377 CD LYS A1104 177.767 19.905 580.469 1.00109.86 C ANISOU 2377 CD LYS A1104 12082 17885 11774 -205 -2166 500 C ATOM 2378 CE LYS A1104 177.307 19.982 581.916 1.00112.57 C ANISOU 2378 CE LYS A1104 12091 18967 11713 -161 -2278 811 C ATOM 2379 NZ LYS A1104 176.268 21.029 582.116 1.00112.58 N ANISOU 2379 NZ LYS A1104 11917 19619 11238 59 -2072 787 N ATOM 2380 N TYR A1105 177.562 20.633 575.055 1.00119.58 N ANISOU 2380 N TYR A1105 14430 17431 13572 -488 -1554 -380 N ATOM 2381 CA TYR A1105 177.848 20.350 573.657 1.00121.20 C ANISOU 2381 CA TYR A1105 14931 17091 14027 -705 -1469 -604 C ATOM 2382 C TYR A1105 178.300 21.622 572.945 1.00121.99 C ANISOU 2382 C TYR A1105 15323 16971 14057 -584 -1161 -1075 C ATOM 2383 O TYR A1105 178.339 22.712 573.524 1.00122.85 O ANISOU 2383 O TYR A1105 15407 17322 13948 -311 -1044 -1213 O ATOM 2384 CB TYR A1105 176.624 19.745 572.966 1.00125.25 C ANISOU 2384 CB TYR A1105 15466 17699 14422 -915 -1599 -210 C ATOM 2385 CG TYR A1105 176.717 18.252 572.747 1.00130.55 C ANISOU 2385 CG TYR A1105 16080 18110 15415 -1210 -1868 17 C ATOM 2386 CD1 TYR A1105 177.524 17.728 571.745 1.00131.85 C ANISOU 2386 CD1 TYR A1105 16444 17691 15964 -1394 -1840 -318 C ATOM 2387 CD2 TYR A1105 175.991 17.368 573.533 1.00134.75 C ANISOU 2387 CD2 TYR A1105 16351 18987 15859 -1323 -2169 552 C ATOM 2388 CE1 TYR A1105 177.611 16.364 571.538 1.00134.13 C ANISOU 2388 CE1 TYR A1105 16670 17710 16583 -1634 -2134 -152 C ATOM 2389 CE2 TYR A1105 176.071 16.003 573.332 1.00137.05 C ANISOU 2389 CE2 TYR A1105 16615 18993 16465 -1601 -2477 773 C ATOM 2390 CZ TYR A1105 176.882 15.507 572.334 1.00136.33 C ANISOU 2390 CZ TYR A1105 16720 18283 16794 -1731 -2472 408 C ATOM 2391 OH TYR A1105 176.965 14.148 572.131 1.00137.61 O ANISOU 2391 OH TYR A1105 16846 18135 17305 -1978 -2823 588 O ATOM 2392 N LEU A1106 178.640 21.470 571.669 1.00122.38 N ANISOU 2392 N LEU A1106 15656 16560 14284 -814 -1048 -1324 N ATOM 2393 CA LEU A1106 179.092 22.588 570.850 1.00122.73 C ANISOU 2393 CA LEU A1106 16031 16351 14248 -809 -776 -1746 C ATOM 2394 C LEU A1106 177.910 23.324 570.227 1.00122.64 C ANISOU 2394 C LEU A1106 16212 16494 13892 -782 -763 -1561 C ATOM 2395 O LEU A1106 177.138 22.743 569.464 1.00123.57 O ANISOU 2395 O LEU A1106 16404 16560 13986 -980 -855 -1325 O ATOM 2396 CB LEU A1106 180.044 22.100 569.757 1.00123.93 C ANISOU 2396 CB LEU A1106 16391 15981 14714 -1116 -650 -2137 C ATOM 2397 CG LEU A1106 181.317 21.394 570.230 1.00123.22 C ANISOU 2397 CG LEU A1106 16119 15671 15029 -1136 -680 -2437 C ATOM 2398 CD1 LEU A1106 182.123 20.886 569.045 1.00124.63 C ANISOU 2398 CD1 LEU A1106 16461 15392 15499 -1451 -558 -2869 C ATOM 2399 CD2 LEU A1106 182.156 22.322 571.095 1.00119.49 C ANISOU 2399 CD2 LEU A1106 15591 15284 14527 -881 -541 -2728 C ATOM 2400 N GLU A 382 177.614 20.135 559.025 1.00110.14 N ANISOU 2400 N GLU A 382 16802 12457 12589 -3738 -250 -2576 N ATOM 2401 CA GLU A 382 178.592 19.964 557.957 1.00111.68 C ANISOU 2401 CA GLU A 382 17171 12407 12857 -4145 -6 -3120 C ATOM 2402 C GLU A 382 178.041 19.091 556.835 1.00112.04 C ANISOU 2402 C GLU A 382 17310 12326 12934 -4443 -92 -3060 C ATOM 2403 O GLU A 382 178.518 19.146 555.701 1.00114.83 O ANISOU 2403 O GLU A 382 17908 12527 13194 -4840 109 -3440 O ATOM 2404 CB GLU A 382 179.886 19.360 558.506 1.00112.96 C ANISOU 2404 CB GLU A 382 16996 12500 13424 -4101 82 -3576 C ATOM 2405 CG GLU A 382 180.661 20.275 559.446 1.00114.00 C ANISOU 2405 CG GLU A 382 17071 12719 13523 -3877 226 -3761 C ATOM 2406 CD GLU A 382 181.247 21.487 558.742 1.00116.98 C ANISOU 2406 CD GLU A 382 17843 13023 13581 -4151 537 -4116 C ATOM 2407 OE1 GLU A 382 180.490 22.437 558.448 1.00117.06 O ANISOU 2407 OE1 GLU A 382 18201 13068 13207 -4168 514 -3833 O ATOM 2408 OE2 GLU A 382 182.468 21.487 558.479 1.00119.12 O ANISOU 2408 OE2 GLU A 382 18075 13199 13987 -4366 783 -4689 O ATOM 2409 N LYS A 383 177.033 18.278 557.162 1.00 78.35 N ANISOU 2409 N LYS A 383 10781 13827 5163 1435 -541 2177 N ATOM 2410 CA LYS A 383 176.400 17.440 556.150 1.00 80.21 C ANISOU 2410 CA LYS A 383 11008 13766 5701 1318 -347 2445 C ATOM 2411 C LYS A 383 175.687 18.283 555.100 1.00 76.22 C ANISOU 2411 C LYS A 383 10209 13186 5566 1044 -200 2261 C ATOM 2412 O LYS A 383 175.805 18.018 553.897 1.00 74.53 O ANISOU 2412 O LYS A 383 9819 12748 5750 949 -240 2251 O ATOM 2413 CB LYS A 383 175.422 16.468 556.812 1.00 90.17 C ANISOU 2413 CB LYS A 383 12606 14812 6843 1289 -24 2781 C ATOM 2414 CG LYS A 383 176.070 15.237 557.429 1.00 96.94 C ANISOU 2414 CG LYS A 383 13766 15527 7542 1504 -151 3014 C ATOM 2415 CD LYS A 383 176.433 14.214 556.365 1.00 94.62 C ANISOU 2415 CD LYS A 383 13420 14953 7579 1536 -228 3183 C ATOM 2416 CE LYS A 383 176.858 12.894 556.988 1.00 98.80 C ANISOU 2416 CE LYS A 383 14281 15289 7970 1724 -294 3451 C ATOM 2417 NZ LYS A 383 177.069 11.836 555.962 1.00 97.25 N ANISOU 2417 NZ LYS A 383 14050 14783 8116 1740 -324 3617 N ATOM 2418 N LYS A 384 174.946 19.306 555.534 1.00 73.92 N ANISOU 2418 N LYS A 384 9864 13016 5204 907 -35 2069 N ATOM 2419 CA LYS A 384 174.221 20.148 554.588 1.00 72.26 C ANISOU 2419 CA LYS A 384 9393 12662 5402 653 95 1856 C ATOM 2420 C LYS A 384 175.162 20.982 553.730 1.00 69.51 C ANISOU 2420 C LYS A 384 8767 12353 5289 624 -178 1554 C ATOM 2421 O LYS A 384 174.807 21.351 552.605 1.00 67.25 O ANISOU 2421 O LYS A 384 8290 11872 5392 451 -127 1454 O ATOM 2422 CB LYS A 384 173.239 21.052 555.332 1.00 77.46 C ANISOU 2422 CB LYS A 384 10064 13446 5919 545 326 1707 C ATOM 2423 CG LYS A 384 171.855 20.449 555.504 1.00 82.67 C ANISOU 2423 CG LYS A 384 10848 13931 6632 418 715 1929 C ATOM 2424 CD LYS A 384 171.190 20.216 554.156 1.00 82.34 C ANISOU 2424 CD LYS A 384 10611 13570 7106 232 818 1945 C ATOM 2425 CE LYS A 384 169.783 19.665 554.314 1.00 89.31 C ANISOU 2425 CE LYS A 384 11561 14285 8088 85 1208 2108 C ATOM 2426 NZ LYS A 384 169.115 19.471 552.996 1.00 89.30 N ANISOU 2426 NZ LYS A 384 11345 13996 8590 -83 1277 2078 N ATOM 2427 N VAL A 385 176.355 21.296 554.238 1.00 70.61 N ANISOU 2427 N VAL A 385 8884 12745 5200 788 -463 1396 N ATOM 2428 CA VAL A 385 177.339 22.008 553.428 1.00 68.46 C ANISOU 2428 CA VAL A 385 8344 12502 5167 745 -699 1109 C ATOM 2429 C VAL A 385 177.815 21.124 552.282 1.00 61.70 C ANISOU 2429 C VAL A 385 7411 11424 4607 752 -781 1253 C ATOM 2430 O VAL A 385 177.875 21.555 551.123 1.00 63.00 O ANISOU 2430 O VAL A 385 7377 11433 5126 595 -779 1120 O ATOM 2431 CB VAL A 385 178.512 22.482 554.305 1.00 70.21 C ANISOU 2431 CB VAL A 385 8532 13061 5083 922 -986 878 C ATOM 2432 CG1 VAL A 385 179.524 23.253 553.469 1.00 66.65 C ANISOU 2432 CG1 VAL A 385 7782 12630 4913 839 -1188 556 C ATOM 2433 CG2 VAL A 385 178.003 23.335 555.455 1.00 72.33 C ANISOU 2433 CG2 VAL A 385 8887 13554 5040 920 -899 721 C ATOM 2434 N THR A 386 178.152 19.869 552.591 1.00 60.64 N ANISOU 2434 N THR A 386 7456 11264 4321 943 -847 1529 N ATOM 2435 CA THR A 386 178.567 18.932 551.552 1.00 64.47 C ANISOU 2435 CA THR A 386 7883 11529 5082 967 -914 1667 C ATOM 2436 C THR A 386 177.436 18.668 550.564 1.00 66.67 C ANISOU 2436 C THR A 386 8137 11491 5705 753 -654 1789 C ATOM 2437 O THR A 386 177.668 18.595 549.351 1.00 73.36 O ANISOU 2437 O THR A 386 8817 12174 6882 664 -694 1726 O ATOM 2438 CB THR A 386 179.047 17.627 552.190 1.00 69.93 C ANISOU 2438 CB THR A 386 8809 12230 5530 1235 -1022 1955 C ATOM 2439 OG1 THR A 386 180.128 17.903 553.089 1.00 60.50 O ANISOU 2439 OG1 THR A 386 7621 11350 4016 1462 -1307 1805 O ATOM 2440 CG2 THR A 386 179.521 16.651 551.126 1.00 66.44 C ANISOU 2440 CG2 THR A 386 8299 11557 5389 1275 -1101 2069 C ATOM 2441 N ARG A 387 176.204 18.526 551.065 1.00 65.98 N ANISOU 2441 N ARG A 387 8204 11325 5542 670 -383 1945 N ATOM 2442 CA ARG A 387 175.053 18.362 550.180 1.00 62.95 C ANISOU 2442 CA ARG A 387 7759 10667 5494 465 -144 2009 C ATOM 2443 C ARG A 387 174.910 19.550 549.238 1.00 54.81 C ANISOU 2443 C ARG A 387 6480 9610 4737 293 -167 1719 C ATOM 2444 O ARG A 387 174.676 19.382 548.035 1.00 52.43 O ANISOU 2444 O ARG A 387 6059 9098 4762 189 -146 1709 O ATOM 2445 CB ARG A 387 173.773 18.190 550.999 1.00 72.65 C ANISOU 2445 CB ARG A 387 9153 11862 6588 394 162 2159 C ATOM 2446 CG ARG A 387 173.554 16.813 551.594 1.00 85.25 C ANISOU 2446 CG ARG A 387 11021 13341 8030 494 294 2515 C ATOM 2447 CD ARG A 387 172.136 16.715 552.141 1.00 96.24 C ANISOU 2447 CD ARG A 387 12519 14654 9395 347 665 2625 C ATOM 2448 NE ARG A 387 171.880 15.464 552.848 1.00108.65 N ANISOU 2448 NE ARG A 387 14393 16106 10783 422 845 2980 N ATOM 2449 CZ ARG A 387 170.722 15.162 553.426 1.00115.68 C ANISOU 2449 CZ ARG A 387 15416 16913 11625 297 1208 3122 C ATOM 2450 NH1 ARG A 387 169.712 16.021 553.377 1.00118.01 N ANISOU 2450 NH1 ARG A 387 15540 17249 12051 106 1407 2917 N ATOM 2451 NH2 ARG A 387 170.570 14.003 554.052 1.00116.78 N ANISOU 2451 NH2 ARG A 387 15861 16915 11594 362 1384 3466 N ATOM 2452 N THR A 388 175.036 20.764 549.776 1.00 52.38 N ANISOU 2452 N THR A 388 6108 9505 4289 269 -209 1480 N ATOM 2453 CA THR A 388 174.888 21.965 548.960 1.00 54.01 C ANISOU 2453 CA THR A 388 6118 9663 4740 114 -219 1217 C ATOM 2454 C THR A 388 175.967 22.035 547.886 1.00 55.65 C ANISOU 2454 C THR A 388 6177 9818 5150 107 -414 1111 C ATOM 2455 O THR A 388 175.679 22.302 546.710 1.00 58.52 O ANISOU 2455 O THR A 388 6435 9996 5806 -16 -377 1056 O ATOM 2456 CB THR A 388 174.932 23.205 549.855 1.00 52.17 C ANISOU 2456 CB THR A 388 5863 9653 4307 105 -234 973 C ATOM 2457 OG1 THR A 388 173.891 23.123 550.836 1.00 50.71 O ANISOU 2457 OG1 THR A 388 5816 9525 3927 106 -22 1064 O ATOM 2458 CG2 THR A 388 174.748 24.464 549.032 1.00 51.75 C ANISOU 2458 CG2 THR A 388 5640 9507 4514 -50 -229 718 C ATOM 2459 N ILE A 389 177.221 21.791 548.276 1.00 51.71 N ANISOU 2459 N ILE A 389 5667 9491 4491 249 -624 1071 N ATOM 2460 CA ILE A 389 178.317 21.791 547.309 1.00 54.60 C ANISOU 2460 CA ILE A 389 5872 9826 5047 243 -790 954 C ATOM 2461 C ILE A 389 178.055 20.766 546.212 1.00 49.85 C ANISOU 2461 C ILE A 389 5278 8973 4690 222 -734 1146 C ATOM 2462 O ILE A 389 178.217 21.051 545.019 1.00 46.62 O ANISOU 2462 O ILE A 389 4744 8433 4534 111 -736 1050 O ATOM 2463 CB ILE A 389 179.658 21.533 548.018 1.00 55.43 C ANISOU 2463 CB ILE A 389 5948 10174 4937 432 -1032 878 C ATOM 2464 CG1 ILE A 389 180.006 22.705 548.939 1.00 59.00 C ANISOU 2464 CG1 ILE A 389 6345 10881 5192 428 -1110 607 C ATOM 2465 CG2 ILE A 389 180.766 21.297 547.002 1.00 52.13 C ANISOU 2465 CG2 ILE A 389 5353 9715 4739 436 -1176 777 C ATOM 2466 CD1 ILE A 389 181.334 22.551 549.648 1.00 66.19 C ANISOU 2466 CD1 ILE A 389 7191 12062 5895 622 -1381 472 C ATOM 2467 N LEU A 390 177.627 19.562 546.601 1.00 43.14 N ANISOU 2467 N LEU A 390 4589 8043 3761 325 -672 1417 N ATOM 2468 CA LEU A 390 177.323 18.534 545.610 1.00 51.44 C ANISOU 2468 CA LEU A 390 5649 8842 5056 303 -613 1582 C ATOM 2469 C LEU A 390 176.216 18.983 544.667 1.00 51.27 C ANISOU 2469 C LEU A 390 5559 8628 5293 108 -448 1534 C ATOM 2470 O LEU A 390 176.273 18.719 543.461 1.00 55.17 O ANISOU 2470 O LEU A 390 5968 8962 6030 51 -464 1514 O ATOM 2471 CB LEU A 390 176.931 17.229 546.300 1.00 54.21 C ANISOU 2471 CB LEU A 390 6207 9106 5283 425 -535 1883 C ATOM 2472 CG LEU A 390 176.472 16.127 545.341 1.00 52.40 C ANISOU 2472 CG LEU A 390 5992 8587 5330 384 -447 2042 C ATOM 2473 CD1 LEU A 390 177.611 15.703 544.423 1.00 54.30 C ANISOU 2473 CD1 LEU A 390 6114 8794 5722 464 -639 1970 C ATOM 2474 CD2 LEU A 390 175.901 14.933 546.093 1.00 52.45 C ANISOU 2474 CD2 LEU A 390 6229 8465 5235 462 -308 2344 C ATOM 2475 N ALA A 391 175.198 19.667 545.196 1.00 53.57 N ANISOU 2475 N ALA A 391 5884 8944 5528 21 -297 1500 N ATOM 2476 CA ALA A 391 174.105 20.129 544.348 1.00 46.97 C ANISOU 2476 CA ALA A 391 4972 7939 4935 -131 -167 1434 C ATOM 2477 C ALA A 391 174.591 21.155 543.334 1.00 43.55 C ANISOU 2477 C ALA A 391 4406 7489 4650 -208 -268 1219 C ATOM 2478 O ALA A 391 174.210 21.106 542.158 1.00 49.77 O ANISOU 2478 O ALA A 391 5139 8105 5667 -278 -251 1202 O ATOM 2479 CB ALA A 391 172.981 20.710 545.205 1.00 47.39 C ANISOU 2479 CB ALA A 391 5067 8043 4894 -189 8 1409 C ATOM 2480 N ILE A 392 175.437 22.091 543.769 1.00 43.27 N ANISOU 2480 N ILE A 392 4330 7630 4483 -199 -367 1047 N ATOM 2481 CA ILE A 392 175.966 23.096 542.848 1.00 41.74 C ANISOU 2481 CA ILE A 392 4032 7400 4429 -292 -430 849 C ATOM 2482 C ILE A 392 176.816 22.432 541.769 1.00 47.62 C ANISOU 2482 C ILE A 392 4719 8064 5311 -278 -518 878 C ATOM 2483 O ILE A 392 176.657 22.701 540.568 1.00 47.59 O ANISOU 2483 O ILE A 392 4682 7910 5491 -362 -494 835 O ATOM 2484 CB ILE A 392 176.762 24.162 543.623 1.00 42.24 C ANISOU 2484 CB ILE A 392 4047 7661 4340 -298 -506 638 C ATOM 2485 CG1 ILE A 392 175.858 24.857 544.643 1.00 45.60 C ANISOU 2485 CG1 ILE A 392 4530 8162 4632 -311 -406 585 C ATOM 2486 CG2 ILE A 392 177.371 25.174 542.668 1.00 39.41 C ANISOU 2486 CG2 ILE A 392 3597 7235 4143 -418 -535 443 C ATOM 2487 CD1 ILE A 392 176.571 25.879 545.498 1.00 50.77 C ANISOU 2487 CD1 ILE A 392 5141 9018 5129 -313 -483 353 C ATOM 2488 N LEU A 393 177.724 21.543 542.184 1.00 50.29 N ANISOU 2488 N LEU A 393 5052 8505 5548 -155 -625 947 N ATOM 2489 CA LEU A 393 178.592 20.859 541.229 1.00 50.08 C ANISOU 2489 CA LEU A 393 4954 8420 5653 -125 -708 952 C ATOM 2490 C LEU A 393 177.778 20.067 540.213 1.00 47.62 C ANISOU 2490 C LEU A 393 4683 7878 5533 -156 -626 1089 C ATOM 2491 O LEU A 393 178.038 20.132 539.005 1.00 43.39 O ANISOU 2491 O LEU A 393 4089 7244 5154 -216 -632 1021 O ATOM 2492 CB LEU A 393 179.567 19.943 541.970 1.00 47.65 C ANISOU 2492 CB LEU A 393 4647 8254 5206 55 -849 1016 C ATOM 2493 CG LEU A 393 180.603 20.617 542.872 1.00 49.69 C ANISOU 2493 CG LEU A 393 4824 8771 5285 114 -985 832 C ATOM 2494 CD1 LEU A 393 181.452 19.577 543.590 1.00 48.94 C ANISOU 2494 CD1 LEU A 393 4749 8806 5042 342 -1153 919 C ATOM 2495 CD2 LEU A 393 181.479 21.567 542.073 1.00 49.51 C ANISOU 2495 CD2 LEU A 393 4625 8783 5403 -15 -1014 571 C ATOM 2496 N LEU A 394 176.776 19.321 540.685 1.00 47.40 N ANISOU 2496 N LEU A 394 4754 7764 5492 -122 -537 1268 N ATOM 2497 CA LEU A 394 175.964 18.514 539.780 1.00 44.57 C ANISOU 2497 CA LEU A 394 4411 7188 5336 -156 -464 1367 C ATOM 2498 C LEU A 394 175.150 19.387 538.835 1.00 44.70 C ANISOU 2498 C LEU A 394 4385 7102 5497 -281 -406 1252 C ATOM 2499 O LEU A 394 174.992 19.050 537.656 1.00 42.46 O ANISOU 2499 O LEU A 394 4072 6682 5380 -308 -417 1236 O ATOM 2500 CB LEU A 394 175.049 17.589 540.576 1.00 41.77 C ANISOU 2500 CB LEU A 394 4162 6757 4952 -121 -349 1565 C ATOM 2501 CG LEU A 394 175.761 16.413 541.239 1.00 48.39 C ANISOU 2501 CG LEU A 394 5090 7611 5684 30 -408 1735 C ATOM 2502 CD1 LEU A 394 174.765 15.520 541.952 1.00 50.88 C ANISOU 2502 CD1 LEU A 394 5543 7804 5985 35 -244 1949 C ATOM 2503 CD2 LEU A 394 176.552 15.629 540.205 1.00 47.59 C ANISOU 2503 CD2 LEU A 394 4927 7410 5744 86 -514 1721 C ATOM 2504 N ALA A 395 174.616 20.504 539.332 1.00 43.99 N ANISOU 2504 N ALA A 395 4300 7075 5339 -339 -353 1165 N ATOM 2505 CA ALA A 395 173.921 21.436 538.451 1.00 43.33 C ANISOU 2505 CA ALA A 395 4193 6889 5380 -423 -325 1052 C ATOM 2506 C ALA A 395 174.838 21.901 537.327 1.00 47.21 C ANISOU 2506 C ALA A 395 4660 7354 5924 -457 -402 949 C ATOM 2507 O ALA A 395 174.472 21.850 536.144 1.00 48.47 O ANISOU 2507 O ALA A 395 4827 7379 6212 -480 -408 934 O ATOM 2508 CB ALA A 395 173.400 22.628 539.255 1.00 35.52 C ANISOU 2508 CB ALA A 395 3215 5977 4303 -460 -269 954 C ATOM 2509 N PHE A 396 176.051 22.333 537.684 1.00 47.61 N ANISOU 2509 N PHE A 396 4678 7541 5871 -461 -455 866 N ATOM 2510 CA PHE A 396 176.996 22.817 536.682 1.00 45.62 C ANISOU 2510 CA PHE A 396 4393 7269 5670 -521 -485 755 C ATOM 2511 C PHE A 396 177.339 21.731 535.666 1.00 45.91 C ANISOU 2511 C PHE A 396 4411 7227 5805 -482 -516 816 C ATOM 2512 O PHE A 396 177.279 21.959 534.452 1.00 47.35 O ANISOU 2512 O PHE A 396 4622 7301 6069 -531 -496 778 O ATOM 2513 CB PHE A 396 178.258 23.332 537.374 1.00 44.18 C ANISOU 2513 CB PHE A 396 4136 7265 5387 -536 -532 626 C ATOM 2514 CG PHE A 396 179.396 23.608 536.437 1.00 44.61 C ANISOU 2514 CG PHE A 396 4124 7318 5508 -607 -536 507 C ATOM 2515 CD1 PHE A 396 179.408 24.754 535.660 1.00 44.29 C ANISOU 2515 CD1 PHE A 396 4129 7177 5522 -737 -455 407 C ATOM 2516 CD2 PHE A 396 180.459 22.724 536.339 1.00 44.58 C ANISOU 2516 CD2 PHE A 396 4018 7405 5513 -541 -606 492 C ATOM 2517 CE1 PHE A 396 180.455 25.012 534.798 1.00 47.80 C ANISOU 2517 CE1 PHE A 396 4526 7615 6023 -825 -413 301 C ATOM 2518 CE2 PHE A 396 181.509 22.976 535.479 1.00 44.07 C ANISOU 2518 CE2 PHE A 396 3871 7352 5521 -619 -580 359 C ATOM 2519 CZ PHE A 396 181.508 24.121 534.708 1.00 47.86 C ANISOU 2519 CZ PHE A 396 4403 7734 6047 -775 -468 266 C ATOM 2520 N ILE A 397 177.693 20.538 536.148 1.00 45.45 N ANISOU 2520 N ILE A 397 4322 7217 5731 -382 -565 911 N ATOM 2521 CA ILE A 397 178.136 19.470 535.255 1.00 44.87 C ANISOU 2521 CA ILE A 397 4219 7071 5761 -333 -600 944 C ATOM 2522 C ILE A 397 177.005 19.027 534.335 1.00 46.63 C ANISOU 2522 C ILE A 397 4493 7110 6115 -351 -559 1001 C ATOM 2523 O ILE A 397 177.208 18.832 533.131 1.00 49.39 O ANISOU 2523 O ILE A 397 4836 7385 6544 -367 -568 948 O ATOM 2524 CB ILE A 397 178.690 18.291 536.075 1.00 46.67 C ANISOU 2524 CB ILE A 397 4425 7361 5948 -196 -670 1045 C ATOM 2525 CG1 ILE A 397 179.907 18.731 536.889 1.00 51.31 C ANISOU 2525 CG1 ILE A 397 4934 8157 6403 -152 -753 945 C ATOM 2526 CG2 ILE A 397 179.049 17.129 535.164 1.00 44.78 C ANISOU 2526 CG2 ILE A 397 4157 7017 5842 -133 -703 1071 C ATOM 2527 CD1 ILE A 397 180.372 17.699 537.894 1.00 55.13 C ANISOU 2527 CD1 ILE A 397 5432 8720 6796 23 -850 1058 C ATOM 2528 N ILE A 398 175.800 18.862 534.883 1.00 44.25 N ANISOU 2528 N ILE A 398 4232 6745 5836 -349 -511 1087 N ATOM 2529 CA ILE A 398 174.688 18.353 534.088 1.00 41.99 C ANISOU 2529 CA ILE A 398 3956 6296 5702 -362 -487 1109 C ATOM 2530 C ILE A 398 174.235 19.390 533.066 1.00 43.61 C ANISOU 2530 C ILE A 398 4188 6450 5931 -416 -496 998 C ATOM 2531 O ILE A 398 173.862 19.046 531.938 1.00 41.82 O ANISOU 2531 O ILE A 398 3968 6122 5800 -407 -528 961 O ATOM 2532 CB ILE A 398 173.537 17.910 535.010 1.00 41.66 C ANISOU 2532 CB ILE A 398 3925 6206 5698 -362 -406 1209 C ATOM 2533 CG1 ILE A 398 173.969 16.704 535.845 1.00 41.95 C ANISOU 2533 CG1 ILE A 398 3987 6244 5709 -291 -390 1356 C ATOM 2534 CG2 ILE A 398 172.291 17.569 534.201 1.00 40.91 C ANISOU 2534 CG2 ILE A 398 3797 5957 5788 -392 -383 1174 C ATOM 2535 CD1 ILE A 398 173.023 16.371 536.969 1.00 46.09 C ANISOU 2535 CD1 ILE A 398 4556 6744 6214 -305 -269 1476 C ATOM 2536 N THR A 399 174.267 20.673 533.432 1.00 43.51 N ANISOU 2536 N THR A 399 4206 6500 5824 -461 -476 938 N ATOM 2537 CA THR A 399 173.850 21.704 532.489 1.00 44.83 C ANISOU 2537 CA THR A 399 4439 6591 6002 -492 -486 856 C ATOM 2538 C THR A 399 174.920 22.032 531.455 1.00 52.46 C ANISOU 2538 C THR A 399 5454 7556 6924 -525 -495 799 C ATOM 2539 O THR A 399 174.583 22.517 530.370 1.00 52.44 O ANISOU 2539 O THR A 399 5541 7460 6925 -525 -509 763 O ATOM 2540 CB THR A 399 173.461 22.980 533.234 1.00 45.15 C ANISOU 2540 CB THR A 399 4511 6663 5982 -525 -449 808 C ATOM 2541 OG1 THR A 399 174.496 23.317 534.164 1.00 51.51 O ANISOU 2541 OG1 THR A 399 5289 7604 6679 -562 -427 785 O ATOM 2542 CG2 THR A 399 172.154 22.778 533.979 1.00 46.27 C ANISOU 2542 CG2 THR A 399 4609 6788 6186 -496 -418 835 C ATOM 2543 N TRP A 400 176.191 21.770 531.754 1.00 48.04 N ANISOU 2543 N TRP A 400 4835 7100 6316 -545 -485 782 N ATOM 2544 CA TRP A 400 177.273 22.151 530.860 1.00 43.84 C ANISOU 2544 CA TRP A 400 4324 6581 5751 -604 -453 704 C ATOM 2545 C TRP A 400 177.859 20.988 530.070 1.00 46.76 C ANISOU 2545 C TRP A 400 4645 6950 6171 -558 -475 702 C ATOM 2546 O TRP A 400 178.661 21.228 529.163 1.00 43.41 O ANISOU 2546 O TRP A 400 4242 6531 5721 -608 -426 629 O ATOM 2547 CB TRP A 400 178.390 22.842 531.653 1.00 35.58 C ANISOU 2547 CB TRP A 400 3210 5665 4642 -674 -417 621 C ATOM 2548 CG TRP A 400 178.041 24.232 532.074 1.00 32.59 C ANISOU 2548 CG TRP A 400 2901 5261 4221 -749 -370 573 C ATOM 2549 CD1 TRP A 400 176.938 24.623 532.776 1.00 36.88 C ANISOU 2549 CD1 TRP A 400 3483 5772 4758 -717 -386 610 C ATOM 2550 CD2 TRP A 400 178.800 25.421 531.826 1.00 28.48 C ANISOU 2550 CD2 TRP A 400 2417 4729 3676 -873 -285 463 C ATOM 2551 NE1 TRP A 400 176.961 25.981 532.977 1.00 35.53 N ANISOU 2551 NE1 TRP A 400 3373 5567 4558 -795 -333 527 N ATOM 2552 CE2 TRP A 400 178.094 26.495 532.405 1.00 31.60 C ANISOU 2552 CE2 TRP A 400 2884 5069 4055 -899 -267 442 C ATOM 2553 CE3 TRP A 400 180.007 25.682 531.172 1.00 32.53 C ANISOU 2553 CE3 TRP A 400 2902 5262 4195 -976 -201 368 C ATOM 2554 CZ2 TRP A 400 178.554 27.808 532.349 1.00 37.75 C ANISOU 2554 CZ2 TRP A 400 3724 5789 4830 -1023 -177 339 C ATOM 2555 CZ3 TRP A 400 180.463 26.987 531.119 1.00 38.64 C ANISOU 2555 CZ3 TRP A 400 3730 5984 4966 -1118 -92 268 C ATOM 2556 CH2 TRP A 400 179.738 28.033 531.703 1.00 40.10 C ANISOU 2556 CH2 TRP A 400 4004 6092 5142 -1139 -85 258 C ATOM 2557 N ALA A 401 177.490 19.741 530.387 1.00 48.31 N ANISOU 2557 N ALA A 401 4783 7127 6444 -470 -531 773 N ATOM 2558 CA ALA A 401 178.051 18.607 529.651 1.00 47.19 C ANISOU 2558 CA ALA A 401 4594 6967 6371 -416 -556 753 C ATOM 2559 C ALA A 401 177.571 18.541 528.205 1.00 54.19 C ANISOU 2559 C ALA A 401 5560 7751 7279 -418 -556 706 C ATOM 2560 O ALA A 401 178.411 18.324 527.311 1.00 59.53 O ANISOU 2560 O ALA A 401 6230 8450 7938 -425 -529 629 O ATOM 2561 CB ALA A 401 177.763 17.302 530.399 1.00 40.85 C ANISOU 2561 CB ALA A 401 3734 6132 5658 -322 -604 851 C ATOM 2562 N PRO A 402 176.274 18.720 527.889 1.00 51.67 N ANISOU 2562 N PRO A 402 5310 7332 6989 -403 -590 728 N ATOM 2563 CA PRO A 402 175.853 18.549 526.484 1.00 50.99 C ANISOU 2563 CA PRO A 402 5301 7170 6903 -371 -626 665 C ATOM 2564 C PRO A 402 176.583 19.444 525.496 1.00 48.89 C ANISOU 2564 C PRO A 402 5157 6930 6491 -421 -565 609 C ATOM 2565 O PRO A 402 176.982 18.966 524.429 1.00 49.07 O ANISOU 2565 O PRO A 402 5211 6950 6485 -398 -558 544 O ATOM 2566 CB PRO A 402 174.351 18.864 526.530 1.00 48.68 C ANISOU 2566 CB PRO A 402 5042 6795 6659 -340 -689 677 C ATOM 2567 CG PRO A 402 173.949 18.523 527.899 1.00 48.14 C ANISOU 2567 CG PRO A 402 4875 6737 6680 -349 -668 752 C ATOM 2568 CD PRO A 402 175.104 18.947 528.761 1.00 50.63 C ANISOU 2568 CD PRO A 402 5173 7164 6902 -396 -605 789 C ATOM 2569 N TYR A 403 176.770 20.729 525.809 1.00 44.03 N ANISOU 2569 N TYR A 403 4620 6328 5782 -493 -501 626 N ATOM 2570 CA TYR A 403 177.466 21.608 524.872 1.00 43.27 C ANISOU 2570 CA TYR A 403 4666 6223 5551 -562 -402 589 C ATOM 2571 C TYR A 403 178.885 21.121 524.605 1.00 48.02 C ANISOU 2571 C TYR A 403 5175 6921 6151 -619 -307 516 C ATOM 2572 O TYR A 403 179.357 21.144 523.461 1.00 48.96 O ANISOU 2572 O TYR A 403 5388 7033 6183 -641 -231 466 O ATOM 2573 CB TYR A 403 177.487 23.040 525.407 1.00 38.84 C ANISOU 2573 CB TYR A 403 4193 5634 4932 -647 -332 614 C ATOM 2574 CG TYR A 403 178.111 24.028 524.452 1.00 39.44 C ANISOU 2574 CG TYR A 403 4455 5654 4876 -735 -198 598 C ATOM 2575 CD1 TYR A 403 177.353 24.632 523.461 1.00 45.40 C ANISOU 2575 CD1 TYR A 403 5448 6285 5517 -675 -223 646 C ATOM 2576 CD2 TYR A 403 179.459 24.353 524.537 1.00 45.05 C ANISOU 2576 CD2 TYR A 403 5107 6433 5576 -875 -42 530 C ATOM 2577 CE1 TYR A 403 177.917 25.532 522.581 1.00 50.91 C ANISOU 2577 CE1 TYR A 403 6364 6908 6072 -755 -76 663 C ATOM 2578 CE2 TYR A 403 180.033 25.253 523.659 1.00 48.04 C ANISOU 2578 CE2 TYR A 403 5668 6741 5845 -985 127 521 C ATOM 2579 CZ TYR A 403 179.256 25.841 522.684 1.00 49.65 C ANISOU 2579 CZ TYR A 403 6151 6801 5914 -926 119 605 C ATOM 2580 OH TYR A 403 179.818 26.740 521.807 1.00 51.84 O ANISOU 2580 OH TYR A 403 6656 6985 6058 -1033 309 626 O ATOM 2581 N ASN A 404 179.579 20.663 525.649 1.00 49.98 N ANISOU 2581 N ASN A 404 5239 7266 6485 -630 -311 498 N ATOM 2582 CA ASN A 404 180.964 20.242 525.481 1.00 50.47 C ANISOU 2582 CA ASN A 404 5173 7434 6568 -667 -237 397 C ATOM 2583 C ASN A 404 181.069 18.897 524.772 1.00 48.15 C ANISOU 2583 C ASN A 404 4823 7135 6337 -568 -286 357 C ATOM 2584 O ASN A 404 182.062 18.643 524.080 1.00 44.24 O ANISOU 2584 O ASN A 404 4276 6701 5832 -595 -199 249 O ATOM 2585 CB ASN A 404 181.663 20.204 526.839 1.00 44.23 C ANISOU 2585 CB ASN A 404 4205 6761 5838 -674 -265 374 C ATOM 2586 CG ASN A 404 181.813 21.585 527.449 1.00 41.74 C ANISOU 2586 CG ASN A 404 3924 6468 5467 -795 -196 355 C ATOM 2587 OD1 ASN A 404 182.749 22.318 527.127 1.00 37.97 O ANISOU 2587 OD1 ASN A 404 3429 6031 4968 -922 -65 249 O ATOM 2588 ND2 ASN A 404 180.886 21.950 528.327 1.00 28.87 N ANISOU 2588 ND2 ASN A 404 2338 4804 3828 -766 -265 439 N ATOM 2589 N VAL A 405 180.068 18.024 524.918 1.00 44.33 N ANISOU 2589 N VAL A 405 4337 6572 5934 -461 -408 422 N ATOM 2590 CA VAL A 405 180.100 16.808 524.112 1.00 48.93 C ANISOU 2590 CA VAL A 405 4884 7120 6588 -376 -449 360 C ATOM 2591 C VAL A 405 179.727 17.120 522.668 1.00 51.92 C ANISOU 2591 C VAL A 405 5425 7454 6847 -384 -418 303 C ATOM 2592 O VAL A 405 180.143 16.406 521.748 1.00 50.24 O ANISOU 2592 O VAL A 405 5200 7254 6633 -345 -400 201 O ATOM 2593 CB VAL A 405 179.206 15.707 524.714 1.00 43.00 C ANISOU 2593 CB VAL A 405 4073 6276 5991 -279 -567 429 C ATOM 2594 CG1 VAL A 405 179.506 15.529 526.194 1.00 42.18 C ANISOU 2594 CG1 VAL A 405 3867 6215 5944 -259 -590 519 C ATOM 2595 CG2 VAL A 405 177.737 15.998 524.482 1.00 50.85 C ANISOU 2595 CG2 VAL A 405 5168 7169 6984 -273 -628 473 C ATOM 2596 N MET A 406 178.967 18.195 522.437 1.00 51.97 N ANISOU 2596 N MET A 406 5597 7410 6737 -419 -417 362 N ATOM 2597 CA MET A 406 178.785 18.677 521.071 1.00 49.42 C ANISOU 2597 CA MET A 406 5475 7060 6243 -415 -381 324 C ATOM 2598 C MET A 406 180.096 19.204 520.505 1.00 52.52 C ANISOU 2598 C MET A 406 5914 7526 6516 -523 -187 267 C ATOM 2599 O MET A 406 180.373 19.046 519.311 1.00 57.67 O ANISOU 2599 O MET A 406 6676 8193 7042 -511 -121 198 O ATOM 2600 CB MET A 406 177.713 19.765 521.025 1.00 42.97 C ANISOU 2600 CB MET A 406 4837 6158 5331 -401 -435 410 C ATOM 2601 CG MET A 406 176.325 19.300 521.421 1.00 36.21 C ANISOU 2601 CG MET A 406 3923 5237 4600 -300 -611 429 C ATOM 2602 SD MET A 406 175.197 20.688 521.630 0.82 37.30 S ANISOU 2602 SD MET A 406 4219 5292 4662 -274 -672 509 S ATOM 2603 CE MET A 406 173.957 19.960 522.697 1.00 30.73 C ANISOU 2603 CE MET A 406 3184 4429 4063 -218 -803 510 C ATOM 2604 N VAL A 407 180.915 19.835 521.351 1.00 50.85 N ANISOU 2604 N VAL A 407 5613 7368 6340 -635 -82 276 N ATOM 2605 CA VAL A 407 182.242 20.262 520.920 1.00 44.93 C ANISOU 2605 CA VAL A 407 4846 6696 5530 -764 125 185 C ATOM 2606 C VAL A 407 183.108 19.052 520.584 1.00 44.36 C ANISOU 2606 C VAL A 407 4590 6721 5545 -716 142 47 C ATOM 2607 O VAL A 407 183.858 19.061 519.600 1.00 45.58 O ANISOU 2607 O VAL A 407 4785 6924 5610 -772 302 -53 O ATOM 2608 CB VAL A 407 182.890 21.149 522.000 1.00 43.85 C ANISOU 2608 CB VAL A 407 4607 6602 5452 -893 205 182 C ATOM 2609 CG1 VAL A 407 184.343 21.434 521.662 1.00 47.21 C ANISOU 2609 CG1 VAL A 407 4936 7123 5878 -1039 423 41 C ATOM 2610 CG2 VAL A 407 182.116 22.450 522.147 1.00 42.10 C ANISOU 2610 CG2 VAL A 407 4596 6261 5138 -948 221 295 C ATOM 2611 N LEU A 408 183.009 17.988 521.386 1.00 41.53 N ANISOU 2611 N LEU A 408 4039 6383 5359 -606 -10 41 N ATOM 2612 CA LEU A 408 183.769 16.774 521.102 1.00 44.19 C ANISOU 2612 CA LEU A 408 4204 6782 5802 -528 -17 -89 C ATOM 2613 C LEU A 408 183.329 16.133 519.788 1.00 51.19 C ANISOU 2613 C LEU A 408 5210 7622 6618 -456 -27 -152 C ATOM 2614 O LEU A 408 184.168 15.713 518.983 1.00 52.34 O ANISOU 2614 O LEU A 408 5307 7838 6743 -459 82 -298 O ATOM 2615 CB LEU A 408 183.625 15.786 522.261 1.00 45.38 C ANISOU 2615 CB LEU A 408 4181 6920 6141 -405 -186 -45 C ATOM 2616 CG LEU A 408 184.047 14.329 522.040 1.00 49.10 C ANISOU 2616 CG LEU A 408 4511 7387 6760 -270 -251 -144 C ATOM 2617 CD1 LEU A 408 185.497 14.226 521.599 1.00 53.95 C ANISOU 2617 CD1 LEU A 408 4971 8135 7391 -297 -123 -332 C ATOM 2618 CD2 LEU A 408 183.820 13.521 523.308 1.00 50.35 C ANISOU 2618 CD2 LEU A 408 4561 7495 7076 -153 -405 -44 C ATOM 2619 N ILE A 409 182.016 16.054 519.552 1.00 49.41 N ANISOU 2619 N ILE A 409 5127 7288 6357 -387 -159 -68 N ATOM 2620 CA ILE A 409 181.515 15.427 518.332 1.00 51.25 C ANISOU 2620 CA ILE A 409 5465 7486 6520 -302 -206 -155 C ATOM 2621 C ILE A 409 181.816 16.292 517.113 1.00 55.92 C ANISOU 2621 C ILE A 409 6279 8124 6845 -370 -50 -188 C ATOM 2622 O ILE A 409 182.010 15.775 516.006 1.00 56.38 O ANISOU 2622 O ILE A 409 6397 8219 6805 -322 -12 -313 O ATOM 2623 CB ILE A 409 180.007 15.140 518.475 1.00 49.60 C ANISOU 2623 CB ILE A 409 5313 7162 6371 -212 -403 -88 C ATOM 2624 CG1 ILE A 409 179.768 14.119 519.589 1.00 50.65 C ANISOU 2624 CG1 ILE A 409 5247 7231 6768 -156 -512 -54 C ATOM 2625 CG2 ILE A 409 179.411 14.641 517.164 1.00 47.73 C ANISOU 2625 CG2 ILE A 409 5191 6903 6039 -121 -477 -206 C ATOM 2626 CD1 ILE A 409 178.306 13.908 519.923 1.00 52.54 C ANISOU 2626 CD1 ILE A 409 5505 7355 7104 -108 -661 8 C ATOM 2627 N ASN A 410 181.885 17.613 517.293 1.00 56.96 N ANISOU 2627 N ASN A 410 6551 8244 6846 -481 58 -79 N ATOM 2628 CA ASN A 410 182.118 18.517 516.173 1.00 53.47 C ANISOU 2628 CA ASN A 410 6375 7807 6132 -550 229 -69 C ATOM 2629 C ASN A 410 183.505 18.352 515.558 1.00 56.71 C ANISOU 2629 C ASN A 410 6722 8331 6496 -649 475 -210 C ATOM 2630 O ASN A 410 183.735 18.835 514.444 1.00 59.59 O ANISOU 2630 O ASN A 410 7318 8708 6616 -694 642 -222 O ATOM 2631 CB ASN A 410 181.908 19.963 516.632 1.00 50.19 C ANISOU 2631 CB ASN A 410 6120 7316 5635 -654 300 84 C ATOM 2632 CG ASN A 410 181.897 20.949 515.483 1.00 55.41 C ANISOU 2632 CG ASN A 410 7130 7926 5997 -699 455 148 C ATOM 2633 OD1 ASN A 410 180.919 21.048 514.743 1.00 60.34 O ANISOU 2633 OD1 ASN A 410 7985 8491 6450 -566 323 202 O ATOM 2634 ND2 ASN A 410 182.986 21.691 515.332 1.00 59.79 N ANISOU 2634 ND2 ASN A 410 7729 8500 6487 -883 740 136 N ATOM 2635 N THR A 411 184.429 17.673 516.245 1.00 55.46 N ANISOU 2635 N THR A 411 6258 8257 6557 -672 503 -323 N ATOM 2636 CA THR A 411 185.784 17.537 515.718 1.00 54.01 C ANISOU 2636 CA THR A 411 5963 8195 6363 -768 744 -493 C ATOM 2637 C THR A 411 185.842 16.592 514.525 1.00 51.25 C ANISOU 2637 C THR A 411 5657 7893 5924 -666 759 -640 C ATOM 2638 O THR A 411 186.689 16.766 513.643 1.00 56.66 O ANISOU 2638 O THR A 411 6390 8665 6474 -754 1007 -756 O ATOM 2639 CB THR A 411 186.736 17.053 516.814 1.00 51.98 C ANISOU 2639 CB THR A 411 5348 8025 6377 -781 727 -597 C ATOM 2640 OG1 THR A 411 186.309 15.772 517.296 1.00 57.59 O ANISOU 2640 OG1 THR A 411 5902 8708 7272 -596 484 -616 O ATOM 2641 CG2 THR A 411 186.753 18.036 517.963 1.00 44.30 C ANISOU 2641 CG2 THR A 411 4334 7031 5467 -887 720 -486 C ATOM 2642 N PHE A 412 184.963 15.592 514.478 1.00 50.44 N ANISOU 2642 N PHE A 412 5532 7734 5900 -492 515 -653 N ATOM 2643 CA PHE A 412 184.962 14.627 513.389 1.00 57.50 C ANISOU 2643 CA PHE A 412 6451 8668 6731 -384 503 -824 C ATOM 2644 C PHE A 412 183.695 14.646 512.547 1.00 60.15 C ANISOU 2644 C PHE A 412 7054 8936 6865 -276 348 -778 C ATOM 2645 O PHE A 412 183.700 14.077 511.449 1.00 62.17 O ANISOU 2645 O PHE A 412 7392 9244 6985 -199 364 -930 O ATOM 2646 CB PHE A 412 185.182 13.204 513.931 1.00 58.28 C ANISOU 2646 CB PHE A 412 6254 8755 7136 -259 355 -954 C ATOM 2647 CG PHE A 412 184.194 12.794 514.986 1.00 56.10 C ANISOU 2647 CG PHE A 412 5905 8347 7064 -174 101 -821 C ATOM 2648 CD1 PHE A 412 182.999 12.188 514.636 1.00 55.85 C ANISOU 2648 CD1 PHE A 412 5958 8212 7050 -61 -94 -826 C ATOM 2649 CD2 PHE A 412 184.464 13.007 516.328 1.00 56.44 C ANISOU 2649 CD2 PHE A 412 5790 8375 7279 -210 65 -710 C ATOM 2650 CE1 PHE A 412 182.089 11.809 515.601 1.00 56.33 C ANISOU 2650 CE1 PHE A 412 5945 8146 7311 -9 -284 -713 C ATOM 2651 CE2 PHE A 412 183.559 12.629 517.299 1.00 56.14 C ANISOU 2651 CE2 PHE A 412 5707 8219 7403 -141 -133 -580 C ATOM 2652 CZ PHE A 412 182.369 12.030 516.935 1.00 57.05 C ANISOU 2652 CZ PHE A 412 5906 8221 7551 -51 -291 -577 C ATOM 2653 N CYS A 413 182.615 15.271 513.018 1.00 60.71 N ANISOU 2653 N CYS A 413 7248 8905 6912 -255 191 -600 N ATOM 2654 CA CYS A 413 181.384 15.355 512.234 1.00 61.36 C ANISOU 2654 CA CYS A 413 7565 8939 6811 -133 16 -579 C ATOM 2655 C CYS A 413 180.660 16.638 512.633 1.00 59.66 C ANISOU 2655 C CYS A 413 7543 8641 6484 -167 -24 -364 C ATOM 2656 O CYS A 413 179.942 16.661 513.637 1.00 57.99 O ANISOU 2656 O CYS A 413 7217 8350 6468 -147 -183 -275 O ATOM 2657 CB CYS A 413 180.506 14.131 512.451 1.00 61.72 C ANISOU 2657 CB CYS A 413 7442 8921 7087 7 -244 -680 C ATOM 2658 SG CYS A 413 178.936 14.207 511.565 0.74 63.13 S ANISOU 2658 SG CYS A 413 7841 9058 7088 166 -500 -710 S ATOM 2659 N ALA A 414 180.847 17.688 511.842 1.00 62.02 N ANISOU 2659 N ALA A 414 8147 8949 6469 -215 131 -283 N ATOM 2660 CA ALA A 414 180.142 18.948 512.048 1.00 60.82 C ANISOU 2660 CA ALA A 414 8228 8694 6186 -221 91 -85 C ATOM 2661 C ALA A 414 178.656 18.836 511.702 1.00 63.42 C ANISOU 2661 C ALA A 414 8677 8969 6450 -20 -216 -76 C ATOM 2662 O ALA A 414 177.824 19.389 512.433 1.00 63.78 O ANISOU 2662 O ALA A 414 8719 8922 6592 10 -356 37 O ATOM 2663 CB ALA A 414 180.798 20.070 511.240 1.00 61.34 C ANISOU 2663 CB ALA A 414 8622 8753 5931 -325 366 10 C ATOM 2664 N PRO A 415 178.265 18.155 510.615 1.00 63.35 N ANISOU 2664 N PRO A 415 8760 9022 6286 126 -336 -218 N ATOM 2665 CA PRO A 415 176.824 17.995 510.350 1.00 63.51 C ANISOU 2665 CA PRO A 415 8836 9006 6290 323 -660 -257 C ATOM 2666 C PRO A 415 176.085 17.197 511.411 1.00 59.38 C ANISOU 2666 C PRO A 415 7972 8427 6161 342 -857 -319 C ATOM 2667 O PRO A 415 174.848 17.239 511.441 1.00 60.24 O ANISOU 2667 O PRO A 415 8080 8492 6316 470 -1104 -341 O ATOM 2668 CB PRO A 415 176.792 17.278 508.993 1.00 66.57 C ANISOU 2668 CB PRO A 415 9344 9499 6449 455 -723 -449 C ATOM 2669 CG PRO A 415 178.075 17.633 508.353 1.00 66.48 C ANISOU 2669 CG PRO A 415 9510 9560 6190 337 -396 -420 C ATOM 2670 CD PRO A 415 179.066 17.674 509.472 1.00 64.81 C ANISOU 2670 CD PRO A 415 9044 9323 6257 128 -180 -358 C ATOM 2671 N CYS A 416 176.791 16.470 512.279 1.00 54.33 N ANISOU 2671 N CYS A 416 7049 7789 5806 226 -754 -349 N ATOM 2672 CA CYS A 416 176.128 15.674 513.305 1.00 53.15 C ANISOU 2672 CA CYS A 416 6613 7568 6014 236 -905 -382 C ATOM 2673 C CYS A 416 175.498 16.522 514.403 1.00 51.27 C ANISOU 2673 C CYS A 416 6351 7251 5880 196 -949 -210 C ATOM 2674 O CYS A 416 174.755 15.977 515.226 1.00 49.78 O ANISOU 2674 O CYS A 416 5959 6999 5956 208 -1070 -224 O ATOM 2675 CB CYS A 416 177.116 14.687 513.927 1.00 55.38 C ANISOU 2675 CB CYS A 416 6642 7862 6537 151 -785 -439 C ATOM 2676 SG CYS A 416 177.620 13.336 512.839 0.85 60.71 S ANISOU 2676 SG CYS A 416 7252 8598 7217 225 -784 -699 S ATOM 2677 N ILE A 417 175.774 17.822 514.442 1.00 49.58 N ANISOU 2677 N ILE A 417 6339 7027 5471 141 -836 -56 N ATOM 2678 CA ILE A 417 175.172 18.709 515.434 1.00 47.83 C ANISOU 2678 CA ILE A 417 6111 6728 5333 113 -876 87 C ATOM 2679 C ILE A 417 174.490 19.866 514.714 1.00 52.54 C ANISOU 2679 C ILE A 417 7016 7280 5669 217 -953 163 C ATOM 2680 O ILE A 417 175.162 20.825 514.305 1.00 55.95 O ANISOU 2680 O ILE A 417 7691 7695 5870 157 -784 270 O ATOM 2681 CB ILE A 417 176.215 19.222 516.439 1.00 45.18 C ANISOU 2681 CB ILE A 417 5697 6397 5072 -60 -664 198 C ATOM 2682 CG1 ILE A 417 176.931 18.052 517.114 1.00 46.12 C ANISOU 2682 CG1 ILE A 417 5532 6566 5426 -119 -616 125 C ATOM 2683 CG2 ILE A 417 175.547 20.094 517.491 1.00 41.76 C ANISOU 2683 CG2 ILE A 417 5249 5891 4729 -81 -712 318 C ATOM 2684 CD1 ILE A 417 176.022 17.194 517.969 1.00 44.29 C ANISOU 2684 CD1 ILE A 417 5088 6281 5461 -66 -777 106 C ATOM 2685 N PRO A 418 173.173 19.819 514.530 1.00 47.99 N ANISOU 2685 N PRO A 418 6439 6672 5124 377 -1202 105 N ATOM 2686 CA PRO A 418 172.471 20.929 513.874 1.00 43.17 C ANISOU 2686 CA PRO A 418 6127 6011 4266 520 -1316 176 C ATOM 2687 C PRO A 418 172.512 22.195 514.718 1.00 45.33 C ANISOU 2687 C PRO A 418 6487 6183 4552 445 -1215 356 C ATOM 2688 O PRO A 418 172.858 22.188 515.902 1.00 47.24 O ANISOU 2688 O PRO A 418 6525 6411 5013 298 -1104 401 O ATOM 2689 CB PRO A 418 171.038 20.408 513.721 1.00 42.04 C ANISOU 2689 CB PRO A 418 5849 5875 4250 703 -1626 20 C ATOM 2690 CG PRO A 418 171.155 18.916 513.829 1.00 44.77 C ANISOU 2690 CG PRO A 418 5904 6278 4828 651 -1644 -153 C ATOM 2691 CD PRO A 418 172.285 18.671 514.779 1.00 43.23 C ANISOU 2691 CD PRO A 418 5566 6076 4782 444 -1394 -57 C ATOM 2692 N ASN A 419 172.139 23.304 514.075 1.00 46.31 N ANISOU 2692 N ASN A 419 6940 6231 4425 564 -1267 455 N ATOM 2693 CA ASN A 419 172.146 24.601 514.746 1.00 52.08 C ANISOU 2693 CA ASN A 419 7799 6833 5156 509 -1174 616 C ATOM 2694 C ASN A 419 171.202 24.615 515.944 1.00 54.78 C ANISOU 2694 C ASN A 419 7872 7147 5796 531 -1312 577 C ATOM 2695 O ASN A 419 171.532 25.172 516.999 1.00 57.80 O ANISOU 2695 O ASN A 419 8172 7478 6310 392 -1174 655 O ATOM 2696 CB ASN A 419 171.771 25.699 513.750 1.00 59.21 C ANISOU 2696 CB ASN A 419 9131 7631 5735 681 -1240 728 C ATOM 2697 CG ASN A 419 171.686 27.071 514.390 1.00 72.66 C ANISOU 2697 CG ASN A 419 10989 9163 7454 645 -1159 885 C ATOM 2698 OD1 ASN A 419 172.352 27.349 515.387 1.00 77.27 O ANISOU 2698 OD1 ASN A 419 11430 9717 8210 433 -959 928 O ATOM 2699 ND2 ASN A 419 170.863 27.940 513.814 1.00 81.94 N ANISOU 2699 ND2 ASN A 419 12460 10222 8450 869 -1330 957 N ATOM 2700 N THR A 420 170.023 24.005 515.798 1.00 56.68 N ANISOU 2700 N THR A 420 7959 7427 6147 700 -1574 436 N ATOM 2701 CA THR A 420 169.055 23.981 516.890 1.00 59.16 C ANISOU 2701 CA THR A 420 8007 7722 6750 716 -1682 379 C ATOM 2702 C THR A 420 169.632 23.299 518.125 1.00 55.99 C ANISOU 2702 C THR A 420 7311 7363 6599 501 -1509 384 C ATOM 2703 O THR A 420 169.432 23.767 519.253 1.00 60.82 O ANISOU 2703 O THR A 420 7810 7940 7360 431 -1451 432 O ATOM 2704 CB THR A 420 167.772 23.280 516.437 1.00 66.40 C ANISOU 2704 CB THR A 420 8769 8689 7770 906 -1969 183 C ATOM 2705 OG1 THR A 420 167.262 23.927 515.264 1.00 66.86 O ANISOU 2705 OG1 THR A 420 9121 8725 7559 1143 -2165 174 O ATOM 2706 CG2 THR A 420 166.716 23.331 517.530 1.00 74.76 C ANISOU 2706 CG2 THR A 420 9551 9726 9129 915 -2052 111 C ATOM 2707 N VAL A 421 170.366 22.202 517.929 1.00 51.01 N ANISOU 2707 N VAL A 421 6567 6808 6004 411 -1429 332 N ATOM 2708 CA VAL A 421 170.965 21.495 519.057 1.00 48.10 C ANISOU 2708 CA VAL A 421 5948 6476 5851 242 -1285 348 C ATOM 2709 C VAL A 421 172.038 22.353 519.721 1.00 50.11 C ANISOU 2709 C VAL A 421 6283 6719 6039 91 -1072 483 C ATOM 2710 O VAL A 421 172.181 22.350 520.952 1.00 55.41 O ANISOU 2710 O VAL A 421 6787 7401 6865 -7 -997 521 O ATOM 2711 CB VAL A 421 171.518 20.137 518.590 1.00 43.51 C ANISOU 2711 CB VAL A 421 5250 5959 5322 214 -1266 251 C ATOM 2712 CG1 VAL A 421 172.049 19.343 519.767 1.00 38.15 C ANISOU 2712 CG1 VAL A 421 4329 5299 4867 81 -1151 277 C ATOM 2713 CG2 VAL A 421 170.437 19.353 517.864 1.00 42.23 C ANISOU 2713 CG2 VAL A 421 5012 5801 5232 357 -1484 81 C ATOM 2714 N TRP A 422 172.808 23.100 518.923 1.00 47.06 N ANISOU 2714 N TRP A 422 6154 6310 5417 67 -963 548 N ATOM 2715 CA TRP A 422 173.744 24.066 519.491 1.00 49.54 C ANISOU 2715 CA TRP A 422 6546 6590 5685 -87 -758 648 C ATOM 2716 C TRP A 422 173.016 25.068 520.377 1.00 46.73 C ANISOU 2716 C TRP A 422 6200 6149 5406 -69 -800 702 C ATOM 2717 O TRP A 422 173.451 25.359 521.500 1.00 42.44 O ANISOU 2717 O TRP A 422 5529 5620 4974 -195 -694 724 O ATOM 2718 CB TRP A 422 174.500 24.795 518.376 1.00 53.59 C ANISOU 2718 CB TRP A 422 7371 7058 5933 -117 -617 709 C ATOM 2719 CG TRP A 422 175.608 24.004 517.746 1.00 54.38 C ANISOU 2719 CG TRP A 422 7437 7257 5966 -202 -478 651 C ATOM 2720 CD1 TRP A 422 175.656 23.533 516.466 1.00 54.17 C ANISOU 2720 CD1 TRP A 422 7559 7269 5754 -114 -504 602 C ATOM 2721 CD2 TRP A 422 176.835 23.601 518.367 1.00 54.41 C ANISOU 2721 CD2 TRP A 422 7239 7348 6087 -375 -297 611 C ATOM 2722 NE1 TRP A 422 176.835 22.861 516.252 1.00 56.39 N ANISOU 2722 NE1 TRP A 422 7736 7648 6041 -232 -331 532 N ATOM 2723 CE2 TRP A 422 177.576 22.888 517.404 1.00 55.48 C ANISOU 2723 CE2 TRP A 422 7397 7563 6119 -387 -211 535 C ATOM 2724 CE3 TRP A 422 177.379 23.773 519.644 1.00 51.44 C ANISOU 2724 CE3 TRP A 422 6659 7001 5884 -505 -215 616 C ATOM 2725 CZ2 TRP A 422 178.830 22.345 517.678 1.00 52.35 C ANISOU 2725 CZ2 TRP A 422 6808 7268 5814 -519 -47 457 C ATOM 2726 CZ3 TRP A 422 178.623 23.235 519.914 1.00 47.56 C ANISOU 2726 CZ3 TRP A 422 5987 6617 5466 -626 -73 543 C ATOM 2727 CH2 TRP A 422 179.335 22.529 518.937 1.00 50.99 C ANISOU 2727 CH2 TRP A 422 6430 7123 5821 -630 9 463 C ATOM 2728 N THR A 423 171.898 25.608 519.881 1.00 47.09 N ANISOU 2728 N THR A 423 6392 6111 5389 104 -969 704 N ATOM 2729 CA THR A 423 171.088 26.517 520.687 1.00 51.16 C ANISOU 2729 CA THR A 423 6898 6543 5998 151 -1028 725 C ATOM 2730 C THR A 423 170.650 25.855 521.989 1.00 48.16 C ANISOU 2730 C THR A 423 6185 6242 5871 98 -1049 660 C ATOM 2731 O THR A 423 170.651 26.492 523.051 1.00 51.41 O ANISOU 2731 O THR A 423 6535 6633 6367 26 -975 683 O ATOM 2732 CB THR A 423 169.873 26.985 519.883 1.00 57.03 C ANISOU 2732 CB THR A 423 7806 7205 6657 390 -1253 702 C ATOM 2733 OG1 THR A 423 170.314 27.643 518.688 1.00 58.04 O ANISOU 2733 OG1 THR A 423 8299 7248 6505 449 -1219 796 O ATOM 2734 CG2 THR A 423 169.023 27.949 520.696 1.00 60.71 C ANISOU 2734 CG2 THR A 423 8251 7580 7237 458 -1315 703 C ATOM 2735 N ILE A 424 170.294 24.569 521.930 1.00 45.13 N ANISOU 2735 N ILE A 424 5599 5943 5607 126 -1134 576 N ATOM 2736 CA ILE A 424 169.875 23.859 523.136 1.00 47.62 C ANISOU 2736 CA ILE A 424 5630 6314 6150 68 -1123 537 C ATOM 2737 C ILE A 424 171.021 23.775 524.137 1.00 48.76 C ANISOU 2737 C ILE A 424 5695 6518 6313 -102 -940 606 C ATOM 2738 O ILE A 424 170.829 23.999 525.338 1.00 52.95 O ANISOU 2738 O ILE A 424 6109 7070 6938 -156 -889 622 O ATOM 2739 CB ILE A 424 169.330 22.464 522.775 1.00 51.34 C ANISOU 2739 CB ILE A 424 5926 6826 6756 117 -1227 435 C ATOM 2740 CG1 ILE A 424 168.114 22.590 521.857 1.00 60.99 C ANISOU 2740 CG1 ILE A 424 7188 8012 7974 300 -1442 321 C ATOM 2741 CG2 ILE A 424 168.955 21.697 524.032 1.00 52.52 C ANISOU 2741 CG2 ILE A 424 5819 7006 7132 38 -1172 423 C ATOM 2742 CD1 ILE A 424 167.626 21.270 521.301 1.00 68.92 C ANISOU 2742 CD1 ILE A 424 8032 9048 9105 345 -1554 180 C ATOM 2743 N GLY A 425 172.231 23.460 523.665 1.00 45.51 N ANISOU 2743 N GLY A 425 5338 6146 5806 -179 -843 630 N ATOM 2744 CA GLY A 425 173.368 23.385 524.574 1.00 41.98 C ANISOU 2744 CA GLY A 425 4794 5773 5381 -319 -697 664 C ATOM 2745 C GLY A 425 173.688 24.723 525.217 1.00 46.78 C ANISOU 2745 C GLY A 425 5488 6352 5937 -397 -604 698 C ATOM 2746 O GLY A 425 173.885 24.816 526.438 1.00 51.48 O ANISOU 2746 O GLY A 425 5953 7006 6600 -463 -556 700 O ATOM 2747 N TYR A 426 173.750 25.778 524.397 1.00 43.22 N ANISOU 2747 N TYR A 426 5271 5798 5353 -388 -574 723 N ATOM 2748 CA TYR A 426 173.881 27.135 524.921 1.00 43.21 C ANISOU 2748 CA TYR A 426 5376 5716 5325 -453 -491 745 C ATOM 2749 C TYR A 426 172.857 27.402 526.017 1.00 46.53 C ANISOU 2749 C TYR A 426 5679 6134 5865 -397 -570 720 C ATOM 2750 O TYR A 426 173.186 27.941 527.082 1.00 47.25 O ANISOU 2750 O TYR A 426 5700 6255 5997 -487 -492 699 O ATOM 2751 CB TYR A 426 173.712 28.150 523.788 1.00 39.59 C ANISOU 2751 CB TYR A 426 5230 5097 4715 -398 -481 799 C ATOM 2752 CG TYR A 426 175.001 28.685 523.215 1.00 40.66 C ANISOU 2752 CG TYR A 426 5526 5192 4732 -550 -278 830 C ATOM 2753 CD1 TYR A 426 175.602 28.080 522.119 1.00 44.37 C ANISOU 2753 CD1 TYR A 426 6076 5702 5082 -560 -225 838 C ATOM 2754 CD2 TYR A 426 175.611 29.807 523.760 1.00 40.06 C ANISOU 2754 CD2 TYR A 426 5514 5033 4673 -694 -123 829 C ATOM 2755 CE1 TYR A 426 176.779 28.572 521.588 1.00 48.17 C ANISOU 2755 CE1 TYR A 426 6691 6148 5462 -717 -1 853 C ATOM 2756 CE2 TYR A 426 176.788 30.306 523.238 1.00 44.92 C ANISOU 2756 CE2 TYR A 426 6258 5601 5210 -861 94 837 C ATOM 2757 CZ TYR A 426 177.368 29.685 522.152 1.00 51.32 C ANISOU 2757 CZ TYR A 426 7141 6458 5900 -876 165 854 C ATOM 2758 OH TYR A 426 178.541 30.178 521.628 1.00 59.15 O ANISOU 2758 OH TYR A 426 8248 7406 6821 -1061 417 849 O ATOM 2759 N TRP A 427 171.604 27.008 525.775 1.00 45.35 N ANISOU 2759 N TRP A 427 5491 5963 5778 -250 -723 698 N ATOM 2760 CA TRP A 427 170.544 27.351 526.713 1.00 42.81 C ANISOU 2760 CA TRP A 427 5060 5632 5573 -192 -778 655 C ATOM 2761 C TRP A 427 170.593 26.509 527.979 1.00 39.11 C ANISOU 2761 C TRP A 427 4348 5296 5215 -268 -724 640 C ATOM 2762 O TRP A 427 170.145 26.969 529.030 1.00 38.17 O ANISOU 2762 O TRP A 427 4152 5197 5153 -280 -694 609 O ATOM 2763 CB TRP A 427 169.183 27.234 526.035 1.00 37.39 C ANISOU 2763 CB TRP A 427 4381 4887 4938 -11 -956 602 C ATOM 2764 CG TRP A 427 168.815 28.511 525.383 1.00 39.06 C ANISOU 2764 CG TRP A 427 4836 4950 5056 102 -1020 617 C ATOM 2765 CD1 TRP A 427 168.807 28.780 524.050 1.00 43.80 C ANISOU 2765 CD1 TRP A 427 5676 5462 5506 214 -1105 657 C ATOM 2766 CD2 TRP A 427 168.448 29.725 526.043 1.00 39.55 C ANISOU 2766 CD2 TRP A 427 4956 4919 5151 125 -997 601 C ATOM 2767 NE1 TRP A 427 168.435 30.084 523.834 1.00 50.80 N ANISOU 2767 NE1 TRP A 427 6784 6188 6329 316 -1142 687 N ATOM 2768 CE2 TRP A 427 168.210 30.686 525.045 1.00 44.23 C ANISOU 2768 CE2 TRP A 427 5835 5344 5627 261 -1077 645 C ATOM 2769 CE3 TRP A 427 168.287 30.090 527.383 1.00 44.55 C ANISOU 2769 CE3 TRP A 427 5441 5593 5894 55 -917 549 C ATOM 2770 CZ2 TRP A 427 167.819 31.985 525.341 1.00 46.59 C ANISOU 2770 CZ2 TRP A 427 6270 5490 5942 330 -1083 638 C ATOM 2771 CZ3 TRP A 427 167.899 31.382 527.676 1.00 46.18 C ANISOU 2771 CZ3 TRP A 427 5762 5670 6116 114 -919 518 C ATOM 2772 CH2 TRP A 427 167.669 32.315 526.659 1.00 48.27 C ANISOU 2772 CH2 TRP A 427 6306 5743 6290 251 -1003 563 C ATOM 2773 N LEU A 428 171.116 25.286 527.911 1.00 36.71 N ANISOU 2773 N LEU A 428 3939 5076 4934 -308 -709 661 N ATOM 2774 CA LEU A 428 171.362 24.541 529.140 1.00 42.83 C ANISOU 2774 CA LEU A 428 4538 5961 5775 -374 -645 681 C ATOM 2775 C LEU A 428 172.443 25.224 529.970 1.00 48.11 C ANISOU 2775 C LEU A 428 5220 6699 6360 -477 -543 688 C ATOM 2776 O LEU A 428 172.282 25.426 531.186 1.00 48.25 O ANISOU 2776 O LEU A 428 5158 6785 6389 -503 -503 679 O ATOM 2777 CB LEU A 428 171.752 23.100 528.812 1.00 42.76 C ANISOU 2777 CB LEU A 428 4441 5993 5814 -374 -659 707 C ATOM 2778 CG LEU A 428 170.661 22.253 528.159 1.00 50.53 C ANISOU 2778 CG LEU A 428 5364 6917 6920 -290 -755 666 C ATOM 2779 CD1 LEU A 428 171.177 20.856 527.870 1.00 52.92 C ANISOU 2779 CD1 LEU A 428 5589 7236 7281 -301 -754 681 C ATOM 2780 CD2 LEU A 428 169.425 22.199 529.046 1.00 57.44 C ANISOU 2780 CD2 LEU A 428 6113 7785 7926 -273 -752 640 C ATOM 2781 N CYS A 429 173.550 25.605 529.318 1.00 43.40 N ANISOU 2781 N CYS A 429 4720 6092 5678 -542 -494 684 N ATOM 2782 CA CYS A 429 174.594 26.351 530.013 1.00 48.07 C ANISOU 2782 CA CYS A 429 5304 6743 6216 -655 -399 646 C ATOM 2783 C CYS A 429 174.029 27.586 530.701 1.00 48.91 C ANISOU 2783 C CYS A 429 5462 6794 6325 -664 -379 603 C ATOM 2784 O CYS A 429 174.352 27.864 531.862 1.00 54.65 O ANISOU 2784 O CYS A 429 6101 7619 7044 -717 -341 553 O ATOM 2785 CB CYS A 429 175.704 26.743 529.038 1.00 49.06 C ANISOU 2785 CB CYS A 429 5535 6831 6275 -741 -318 628 C ATOM 2786 SG CYS A 429 176.747 25.368 528.516 0.95 55.93 S ANISOU 2786 SG CYS A 429 6293 7811 7148 -752 -309 627 S ATOM 2787 N TYR A 430 173.170 28.336 530.006 1.00 48.59 N ANISOU 2787 N TYR A 430 5570 6601 6291 -594 -418 608 N ATOM 2788 CA TYR A 430 172.563 29.507 530.630 1.00 50.40 C ANISOU 2788 CA TYR A 430 5848 6756 6545 -580 -407 553 C ATOM 2789 C TYR A 430 171.584 29.118 531.732 1.00 51.34 C ANISOU 2789 C TYR A 430 5805 6967 6736 -518 -443 522 C ATOM 2790 O TYR A 430 171.451 29.845 532.723 1.00 47.82 O ANISOU 2790 O TYR A 430 5328 6547 6295 -545 -399 450 O ATOM 2791 CB TYR A 430 171.870 30.363 529.572 1.00 55.13 C ANISOU 2791 CB TYR A 430 6660 7155 7131 -482 -461 574 C ATOM 2792 CG TYR A 430 172.831 31.023 528.611 1.00 63.02 C ANISOU 2792 CG TYR A 430 7873 8034 8038 -564 -373 616 C ATOM 2793 CD1 TYR A 430 174.143 31.284 528.984 1.00 67.04 C ANISOU 2793 CD1 TYR A 430 8352 8595 8527 -743 -230 577 C ATOM 2794 CD2 TYR A 430 172.430 31.383 527.332 1.00 67.72 C ANISOU 2794 CD2 TYR A 430 8702 8469 8559 -461 -426 684 C ATOM 2795 CE1 TYR A 430 175.028 31.887 528.113 1.00 71.10 C ANISOU 2795 CE1 TYR A 430 9050 8992 8974 -848 -105 603 C ATOM 2796 CE2 TYR A 430 173.309 31.987 526.451 1.00 70.99 C ANISOU 2796 CE2 TYR A 430 9343 8763 8867 -549 -305 740 C ATOM 2797 CZ TYR A 430 174.607 32.236 526.848 1.00 73.85 C ANISOU 2797 CZ TYR A 430 9659 9167 9235 -758 -126 699 C ATOM 2798 OH TYR A 430 175.488 32.836 525.977 1.00 78.15 O ANISOU 2798 OH TYR A 430 10416 9584 9691 -874 36 743 O ATOM 2799 N ILE A 431 170.901 27.979 531.583 1.00 51.67 N ANISOU 2799 N ILE A 431 5743 7055 6836 -448 -505 560 N ATOM 2800 CA ILE A 431 169.942 27.527 532.588 1.00 53.87 C ANISOU 2800 CA ILE A 431 5867 7408 7191 -412 -497 536 C ATOM 2801 C ILE A 431 170.644 27.234 533.905 1.00 54.24 C ANISOU 2801 C ILE A 431 5825 7613 7170 -494 -410 547 C ATOM 2802 O ILE A 431 170.054 27.402 534.983 1.00 58.82 O ANISOU 2802 O ILE A 431 6333 8261 7754 -488 -359 508 O ATOM 2803 CB ILE A 431 169.159 26.302 532.062 1.00 55.76 C ANISOU 2803 CB ILE A 431 6012 7640 7533 -348 -559 566 C ATOM 2804 CG1 ILE A 431 167.987 26.757 531.192 1.00 58.51 C ANISOU 2804 CG1 ILE A 431 6395 7870 7967 -225 -670 496 C ATOM 2805 CG2 ILE A 431 168.653 25.423 533.199 1.00 54.67 C ANISOU 2805 CG2 ILE A 431 5714 7601 7457 -374 -484 584 C ATOM 2806 CD1 ILE A 431 167.130 27.808 531.840 1.00 62.69 C ANISOU 2806 CD1 ILE A 431 6907 8369 8545 -172 -661 404 C ATOM 2807 N ASN A 432 171.912 26.812 533.846 1.00 49.67 N ANISOU 2807 N ASN A 432 5250 7106 6517 -559 -394 588 N ATOM 2808 CA ASN A 432 172.690 26.639 535.073 1.00 42.71 C ANISOU 2808 CA ASN A 432 4296 6387 5545 -609 -348 580 C ATOM 2809 C ASN A 432 172.580 27.855 535.990 1.00 40.85 C ANISOU 2809 C ASN A 432 4075 6185 5263 -640 -305 470 C ATOM 2810 O ASN A 432 172.412 27.713 537.208 1.00 38.11 O ANISOU 2810 O ASN A 432 3663 5969 4848 -631 -270 454 O ATOM 2811 CB ASN A 432 174.156 26.372 534.734 1.00 46.70 C ANISOU 2811 CB ASN A 432 4795 6953 5995 -666 -356 581 C ATOM 2812 CG ASN A 432 174.996 26.096 535.967 1.00 46.77 C ANISOU 2812 CG ASN A 432 4715 7149 5904 -680 -354 559 C ATOM 2813 OD1 ASN A 432 174.526 25.492 536.931 1.00 48.66 O ANISOU 2813 OD1 ASN A 432 4914 7477 6100 -626 -349 617 O ATOM 2814 ND2 ASN A 432 176.246 26.544 535.944 1.00 45.62 N ANISOU 2814 ND2 ASN A 432 4544 7070 5720 -751 -352 466 N ATOM 2815 N SER A 433 172.656 29.061 535.418 1.00 35.60 N ANISOU 2815 N SER A 433 3511 5391 4624 -671 -298 392 N ATOM 2816 CA SER A 433 172.572 30.273 536.227 1.00 34.80 C ANISOU 2816 CA SER A 433 3429 5289 4504 -704 -255 263 C ATOM 2817 C SER A 433 171.200 30.436 536.868 1.00 46.30 C ANISOU 2817 C SER A 433 4843 6743 6004 -619 -245 229 C ATOM 2818 O SER A 433 171.096 30.973 537.977 1.00 49.47 O ANISOU 2818 O SER A 433 5205 7236 6356 -633 -198 126 O ATOM 2819 CB SER A 433 172.905 31.498 535.376 1.00 34.76 C ANISOU 2819 CB SER A 433 3573 5093 4543 -755 -235 207 C ATOM 2820 OG SER A 433 174.258 31.476 534.957 1.00 41.42 O ANISOU 2820 OG SER A 433 4430 5955 5351 -868 -199 199 O ATOM 2821 N THR A 434 170.139 29.992 536.190 1.00 45.36 N ANISOU 2821 N THR A 434 4719 6534 5983 -531 -286 286 N ATOM 2822 CA THR A 434 168.807 30.070 536.777 1.00 43.36 C ANISOU 2822 CA THR A 434 4382 6291 5802 -457 -262 227 C ATOM 2823 C THR A 434 168.631 29.047 537.892 1.00 46.40 C ANISOU 2823 C THR A 434 4646 6857 6128 -479 -181 275 C ATOM 2824 O THR A 434 167.951 29.324 538.887 1.00 49.82 O ANISOU 2824 O THR A 434 5016 7366 6547 -466 -101 197 O ATOM 2825 CB THR A 434 167.741 29.863 535.699 1.00 42.01 C ANISOU 2825 CB THR A 434 4209 5982 5771 -353 -346 240 C ATOM 2826 OG1 THR A 434 168.022 30.706 534.574 1.00 38.87 O ANISOU 2826 OG1 THR A 434 3978 5412 5380 -316 -426 239 O ATOM 2827 CG2 THR A 434 166.362 30.206 536.240 1.00 44.87 C ANISOU 2827 CG2 THR A 434 4464 6342 6243 -272 -323 124 C ATOM 2828 N ILE A 435 169.244 27.872 537.752 1.00 50.51 N ANISOU 2828 N ILE A 435 5148 7440 6606 -507 -190 404 N ATOM 2829 CA ILE A 435 169.071 26.820 538.748 1.00 53.52 C ANISOU 2829 CA ILE A 435 5457 7954 6923 -516 -106 488 C ATOM 2830 C ILE A 435 169.942 27.066 539.979 1.00 51.97 C ANISOU 2830 C ILE A 435 5283 7936 6528 -545 -69 467 C ATOM 2831 O ILE A 435 169.576 26.657 541.088 1.00 47.74 O ANISOU 2831 O ILE A 435 4724 7521 5893 -536 25 499 O ATOM 2832 CB ILE A 435 169.360 25.449 538.111 1.00 57.42 C ANISOU 2832 CB ILE A 435 5937 8415 7464 -514 -139 632 C ATOM 2833 CG1 ILE A 435 168.461 25.236 536.894 1.00 62.67 C ANISOU 2833 CG1 ILE A 435 6570 8924 8318 -477 -196 613 C ATOM 2834 CG2 ILE A 435 169.151 24.322 539.111 1.00 61.84 C ANISOU 2834 CG2 ILE A 435 6462 9067 7967 -520 -37 748 C ATOM 2835 CD1 ILE A 435 166.982 25.329 537.205 1.00 65.84 C ANISOU 2835 CD1 ILE A 435 6870 9297 8850 -451 -130 535 C ATOM 2836 N ASN A 436 171.082 27.741 539.816 1.00 50.87 N ANISOU 2836 N ASN A 436 5189 7819 6322 -581 -135 400 N ATOM 2837 CA ASN A 436 172.033 27.913 540.917 1.00 50.81 C ANISOU 2837 CA ASN A 436 5176 7999 6128 -599 -138 348 C ATOM 2838 C ASN A 436 171.424 28.488 542.193 1.00 55.99 C ANISOU 2838 C ASN A 436 5823 8773 6676 -583 -57 246 C ATOM 2839 O ASN A 436 171.662 27.913 543.267 1.00 53.81 O ANISOU 2839 O ASN A 436 5550 8678 6217 -551 -29 296 O ATOM 2840 CB ASN A 436 173.214 28.774 540.448 1.00 51.36 C ANISOU 2840 CB ASN A 436 5263 8047 6204 -666 -202 229 C ATOM 2841 CG ASN A 436 174.364 27.944 539.918 1.00 56.78 C ANISOU 2841 CG ASN A 436 5925 8773 6876 -676 -271 307 C ATOM 2842 OD1 ASN A 436 174.413 26.730 540.118 1.00 57.41 O ANISOU 2842 OD1 ASN A 436 5984 8921 6909 -615 -290 446 O ATOM 2843 ND2 ASN A 436 175.306 28.598 539.249 1.00 58.96 N ANISOU 2843 ND2 ASN A 436 6203 8998 7201 -756 -294 211 N ATOM 2844 N PRO A 437 170.661 29.590 542.170 1.00 57.93 N ANISOU 2844 N PRO A 437 6069 8931 7009 -589 -17 103 N ATOM 2845 CA PRO A 437 170.134 30.118 543.441 1.00 56.03 C ANISOU 2845 CA PRO A 437 5811 8824 6654 -572 72 -19 C ATOM 2846 C PRO A 437 169.255 29.134 544.189 1.00 56.84 C ANISOU 2846 C PRO A 437 5887 9025 6683 -535 194 97 C ATOM 2847 O PRO A 437 169.254 29.135 545.425 1.00 59.97 O ANISOU 2847 O PRO A 437 6300 9608 6878 -519 269 60 O ATOM 2848 CB PRO A 437 169.346 31.362 543.005 1.00 57.56 C ANISOU 2848 CB PRO A 437 6005 8848 7018 -564 86 -180 C ATOM 2849 CG PRO A 437 169.942 31.749 541.700 1.00 59.88 C ANISOU 2849 CG PRO A 437 6359 8952 7441 -595 -12 -160 C ATOM 2850 CD PRO A 437 170.284 30.453 541.036 1.00 59.69 C ANISOU 2850 CD PRO A 437 6327 8932 7420 -595 -54 38 C ATOM 2851 N ALA A 438 168.511 28.283 543.481 1.00 58.04 N ANISOU 2851 N ALA A 438 6004 9059 6990 -527 226 228 N ATOM 2852 CA ALA A 438 167.676 27.289 544.144 1.00 56.07 C ANISOU 2852 CA ALA A 438 5729 8872 6705 -524 378 342 C ATOM 2853 C ALA A 438 168.485 26.162 544.773 1.00 60.80 C ANISOU 2853 C ALA A 438 6408 9595 7099 -512 386 532 C ATOM 2854 O ALA A 438 167.925 25.384 545.553 1.00 65.47 O ANISOU 2854 O ALA A 438 7025 10249 7601 -513 541 644 O ATOM 2855 CB ALA A 438 166.662 26.713 543.155 1.00 46.64 C ANISOU 2855 CB ALA A 438 4449 7501 5772 -530 402 391 C ATOM 2856 N CYS A 439 169.778 26.060 544.462 1.00 62.57 N ANISOU 2856 N CYS A 439 6675 9850 7248 -495 232 567 N ATOM 2857 CA CYS A 439 170.615 24.995 544.996 1.00 67.44 C ANISOU 2857 CA CYS A 439 7366 10577 7681 -445 199 737 C ATOM 2858 C CYS A 439 171.186 25.319 546.370 1.00 66.72 C ANISOU 2858 C CYS A 439 7343 10727 7281 -392 193 683 C ATOM 2859 O CYS A 439 171.469 24.398 547.146 1.00 66.62 O ANISOU 2859 O CYS A 439 7427 10822 7065 -322 216 847 O ATOM 2860 CB CYS A 439 171.765 24.690 544.031 1.00 70.33 C ANISOU 2860 CB CYS A 439 7717 10883 8120 -435 30 771 C ATOM 2861 SG CYS A 439 171.243 24.132 542.393 1.00 72.59 S ANISOU 2861 SG CYS A 439 7952 10915 8715 -474 15 842 S ATOM 2862 N TYR A 440 171.369 26.599 546.692 1.00 63.57 N ANISOU 2862 N TYR A 440 6909 10410 6836 -413 157 454 N ATOM 2863 CA TYR A 440 171.938 26.985 547.978 1.00 62.80 C ANISOU 2863 CA TYR A 440 6862 10560 6439 -358 128 353 C ATOM 2864 C TYR A 440 171.137 28.030 548.741 1.00 65.24 C ANISOU 2864 C TYR A 440 7159 10942 6688 -381 247 156 C ATOM 2865 O TYR A 440 171.287 28.106 549.967 1.00 69.33 O ANISOU 2865 O TYR A 440 7745 11682 6915 -323 275 107 O ATOM 2866 CB TYR A 440 173.376 27.500 547.805 1.00 59.13 C ANISOU 2866 CB TYR A 440 6350 10180 5938 -352 -76 206 C ATOM 2867 CG TYR A 440 173.529 28.675 546.864 1.00 55.24 C ANISOU 2867 CG TYR A 440 5770 9530 5687 -455 -116 8 C ATOM 2868 CD1 TYR A 440 173.400 29.980 547.322 1.00 53.97 C ANISOU 2868 CD1 TYR A 440 5584 9406 5518 -498 -95 -245 C ATOM 2869 CD2 TYR A 440 173.824 28.478 545.521 1.00 53.52 C ANISOU 2869 CD2 TYR A 440 5517 9120 5699 -506 -167 74 C ATOM 2870 CE1 TYR A 440 173.547 31.056 546.467 1.00 55.64 C ANISOU 2870 CE1 TYR A 440 5753 9436 5952 -591 -117 -404 C ATOM 2871 CE2 TYR A 440 173.973 29.548 544.658 1.00 53.23 C ANISOU 2871 CE2 TYR A 440 5446 8924 5854 -597 -184 -77 C ATOM 2872 CZ TYR A 440 173.833 30.834 545.136 1.00 54.19 C ANISOU 2872 CZ TYR A 440 5560 9056 5974 -640 -156 -305 C ATOM 2873 OH TYR A 440 173.982 31.903 544.281 1.00 50.57 O ANISOU 2873 OH TYR A 440 5103 8401 5710 -729 -158 -435 O ATOM 2874 N ALA A 441 170.304 28.832 548.080 1.00 61.72 N ANISOU 2874 N ALA A 441 6637 10324 6490 -444 308 33 N ATOM 2875 CA ALA A 441 169.547 29.861 548.783 1.00 64.35 C ANISOU 2875 CA ALA A 441 6944 10713 6791 -451 416 -181 C ATOM 2876 C ALA A 441 168.184 29.366 549.252 1.00 71.37 C ANISOU 2876 C ALA A 441 7827 11609 7681 -449 641 -104 C ATOM 2877 O ALA A 441 167.750 29.710 550.357 1.00 76.78 O ANISOU 2877 O ALA A 441 8536 12459 8177 -429 770 -212 O ATOM 2878 CB ALA A 441 169.376 31.096 547.895 1.00 62.84 C ANISOU 2878 CB ALA A 441 6685 10324 6868 -497 358 -377 C ATOM 2879 N LEU A 442 167.498 28.565 548.439 1.00 75.27 N ANISOU 2879 N LEU A 442 8278 11933 8387 -475 701 59 N ATOM 2880 CA LEU A 442 166.196 28.025 548.813 1.00 83.36 C ANISOU 2880 CA LEU A 442 9263 12949 9462 -500 935 115 C ATOM 2881 C LEU A 442 166.297 26.835 549.759 1.00 88.60 C ANISOU 2881 C LEU A 442 10055 13749 9860 -491 1076 343 C ATOM 2882 O LEU A 442 165.275 26.201 550.045 1.00 84.55 O ANISOU 2882 O LEU A 442 9521 13207 9396 -539 1308 426 O ATOM 2883 CB LEU A 442 165.409 27.627 547.561 1.00 79.87 C ANISOU 2883 CB LEU A 442 8706 12271 9371 -534 934 166 C ATOM 2884 CG LEU A 442 165.026 28.763 546.611 1.00 72.51 C ANISOU 2884 CG LEU A 442 7670 11180 8700 -515 818 -38 C ATOM 2885 CD1 LEU A 442 164.148 28.246 545.482 1.00 67.37 C ANISOU 2885 CD1 LEU A 442 6907 10336 8356 -523 811 6 C ATOM 2886 CD2 LEU A 442 164.330 29.883 547.369 1.00 71.06 C ANISOU 2886 CD2 LEU A 442 7429 11071 8498 -492 920 -285 C ATOM 2887 N CYS A 443 167.497 26.517 550.244 1.00 99.19 N ANISOU 2887 N CYS A 443 11528 15229 10930 -428 947 440 N ATOM 2888 CA CYS A 443 167.698 25.429 551.192 1.00109.74 C ANISOU 2888 CA CYS A 443 13037 16693 11968 -381 1052 674 C ATOM 2889 C CYS A 443 168.284 25.914 552.512 1.00102.52 C ANISOU 2889 C CYS A 443 12244 16062 10645 -294 1025 581 C ATOM 2890 O CYS A 443 168.604 25.090 553.378 1.00104.10 O ANISOU 2890 O CYS A 443 12629 16395 10528 -217 1074 778 O ATOM 2891 CB CYS A 443 168.602 24.353 550.583 1.00123.98 C ANISOU 2891 CB CYS A 443 14907 18404 13796 -337 896 907 C ATOM 2892 SG CYS A 443 168.038 23.715 548.988 1.00131.30 S ANISOU 2892 SG CYS A 443 15699 19013 15175 -426 895 996 S ATOM 2893 N ASN A 444 168.432 27.225 552.690 1.00 90.73 N ANISOU 2893 N ASN A 444 10666 14659 9145 -295 944 284 N ATOM 2894 CA ASN A 444 169.036 27.805 553.880 1.00 83.72 C ANISOU 2894 CA ASN A 444 9868 14051 7890 -212 885 130 C ATOM 2895 C ASN A 444 168.012 28.665 554.608 1.00 75.29 C ANISOU 2895 C ASN A 444 8762 13073 6773 -246 1096 -90 C ATOM 2896 O ASN A 444 167.299 29.458 553.986 1.00 66.87 O ANISOU 2896 O ASN A 444 7538 11850 6017 -317 1143 -271 O ATOM 2897 CB ASN A 444 170.265 28.645 553.515 1.00 81.74 C ANISOU 2897 CB ASN A 444 9539 13839 7680 -190 596 -81 C ATOM 2898 CG ASN A 444 171.034 29.112 554.732 1.00 82.13 C ANISOU 2898 CG ASN A 444 9666 14196 7345 -93 489 -254 C ATOM 2899 OD1 ASN A 444 170.716 30.142 555.325 1.00 81.23 O ANISOU 2899 OD1 ASN A 444 9514 14186 7164 -108 544 -526 O ATOM 2900 ND2 ASN A 444 172.057 28.355 555.109 1.00 86.65 N ANISOU 2900 ND2 ASN A 444 10342 14919 7663 24 322 -116 N ATOM 2901 N ALA A 445 167.951 28.510 555.934 1.00 74.61 N ANISOU 2901 N ALA A 445 8828 13241 6279 -178 1218 -80 N ATOM 2902 CA ALA A 445 166.948 29.224 556.719 1.00 75.30 C ANISOU 2902 CA ALA A 445 8887 13439 6286 -207 1456 -289 C ATOM 2903 C ALA A 445 167.248 30.717 556.788 1.00 71.99 C ANISOU 2903 C ALA A 445 8347 13075 5929 -199 1311 -683 C ATOM 2904 O ALA A 445 166.331 31.545 556.707 1.00 74.33 O ANISOU 2904 O ALA A 445 8515 13299 6429 -250 1446 -905 O ATOM 2905 CB ALA A 445 166.862 28.630 558.125 1.00 64.65 C ANISOU 2905 CB ALA A 445 7769 12358 4438 -131 1635 -161 C ATOM 2906 N THR A 446 168.523 31.081 556.944 1.00 68.97 N ANISOU 2906 N THR A 446 7995 12816 5395 -135 1037 -792 N ATOM 2907 CA THR A 446 168.885 32.494 556.994 1.00 68.04 C ANISOU 2907 CA THR A 446 7763 12723 5364 -149 905 -1179 C ATOM 2908 C THR A 446 168.612 33.176 555.659 1.00 65.90 C ANISOU 2908 C THR A 446 7325 12122 5592 -246 852 -1270 C ATOM 2909 O THR A 446 168.130 34.316 555.624 1.00 64.20 O ANISOU 2909 O THR A 446 7015 11827 5550 -276 894 -1552 O ATOM 2910 CB THR A 446 170.355 32.648 557.385 1.00 68.54 C ANISOU 2910 CB THR A 446 7866 12982 5194 -76 621 -1287 C ATOM 2911 OG1 THR A 446 170.683 31.692 558.400 1.00 74.12 O ANISOU 2911 OG1 THR A 446 8765 13960 5436 51 625 -1094 O ATOM 2912 CG2 THR A 446 170.616 34.048 557.920 1.00 71.35 C ANISOU 2912 CG2 THR A 446 8143 13447 5521 -84 547 -1723 C ATOM 2913 N PHE A 447 168.912 32.491 554.551 1.00 65.12 N ANISOU 2913 N PHE A 447 7204 11824 5717 -281 759 -1033 N ATOM 2914 CA PHE A 447 168.601 33.037 553.234 1.00 62.77 C ANISOU 2914 CA PHE A 447 6784 11212 5852 -355 715 -1079 C ATOM 2915 C PHE A 447 167.101 33.241 553.060 1.00 63.32 C ANISOU 2915 C PHE A 447 6777 11151 6129 -373 929 -1116 C ATOM 2916 O PHE A 447 166.670 34.236 552.468 1.00 64.74 O ANISOU 2916 O PHE A 447 6866 11144 6590 -390 907 -1307 O ATOM 2917 CB PHE A 447 169.142 32.121 552.135 1.00 59.61 C ANISOU 2917 CB PHE A 447 6389 10654 5604 -378 598 -808 C ATOM 2918 CG PHE A 447 170.516 32.493 551.650 1.00 55.47 C ANISOU 2918 CG PHE A 447 5846 10111 5121 -400 364 -887 C ATOM 2919 CD1 PHE A 447 170.751 33.734 551.078 1.00 50.99 C ANISOU 2919 CD1 PHE A 447 5208 9383 4783 -465 291 -1126 C ATOM 2920 CD2 PHE A 447 171.567 31.596 551.747 1.00 53.51 C ANISOU 2920 CD2 PHE A 447 5646 9987 4697 -356 230 -727 C ATOM 2921 CE1 PHE A 447 172.012 34.077 550.626 1.00 49.00 C ANISOU 2921 CE1 PHE A 447 4926 9103 4590 -515 118 -1212 C ATOM 2922 CE2 PHE A 447 172.831 31.933 551.295 1.00 49.14 C ANISOU 2922 CE2 PHE A 447 5037 9427 4208 -385 32 -833 C ATOM 2923 CZ PHE A 447 173.053 33.175 550.734 1.00 48.46 C ANISOU 2923 CZ PHE A 447 4871 9186 4357 -480 -10 -1078 C ATOM 2924 N LYS A 448 166.290 32.309 553.567 1.00 63.92 N ANISOU 2924 N LYS A 448 6888 11315 6082 -367 1140 -941 N ATOM 2925 CA LYS A 448 164.841 32.449 553.450 1.00 67.79 C ANISOU 2925 CA LYS A 448 7264 11706 6787 -390 1359 -1009 C ATOM 2926 C LYS A 448 164.335 33.628 554.271 1.00 68.95 C ANISOU 2926 C LYS A 448 7359 11961 6876 -360 1458 -1349 C ATOM 2927 O LYS A 448 163.548 34.447 553.780 1.00 69.84 O ANISOU 2927 O LYS A 448 7337 11908 7290 -353 1482 -1545 O ATOM 2928 CB LYS A 448 164.145 31.159 553.886 1.00 74.63 C ANISOU 2928 CB LYS A 448 8176 12644 7534 -420 1602 -759 C ATOM 2929 CG LYS A 448 164.350 29.981 552.954 1.00 79.31 C ANISOU 2929 CG LYS A 448 8787 13071 8276 -456 1540 -450 C ATOM 2930 CD LYS A 448 163.548 28.779 553.426 1.00 86.58 C ANISOU 2930 CD LYS A 448 9752 14025 9119 -507 1823 -230 C ATOM 2931 CE LYS A 448 163.925 27.525 552.660 1.00 91.71 C ANISOU 2931 CE LYS A 448 10455 14524 9867 -534 1753 80 C ATOM 2932 NZ LYS A 448 165.350 27.157 552.883 1.00 94.58 N ANISOU 2932 NZ LYS A 448 10994 14988 9953 -459 1541 231 N ATOM 2933 N LYS A 449 164.774 33.726 555.529 1.00 70.87 N ANISOU 2933 N LYS A 449 7714 12487 6727 -325 1505 -1434 N ATOM 2934 CA LYS A 449 164.330 34.823 556.384 1.00 69.10 C ANISOU 2934 CA LYS A 449 7447 12389 6420 -292 1606 -1782 C ATOM 2935 C LYS A 449 164.745 36.172 555.807 1.00 68.02 C ANISOU 2935 C LYS A 449 7228 12076 6540 -286 1402 -2067 C ATOM 2936 O LYS A 449 163.955 37.126 555.806 1.00 69.13 O ANISOU 2936 O LYS A 449 7262 12121 6881 -264 1480 -2332 O ATOM 2937 CB LYS A 449 164.885 34.640 557.797 1.00 72.59 C ANISOU 2937 CB LYS A 449 8049 13183 6348 -241 1652 -1818 C ATOM 2938 CG LYS A 449 164.296 35.583 558.835 1.00 77.30 C ANISOU 2938 CG LYS A 449 8617 13959 6797 -205 1814 -2169 C ATOM 2939 CD LYS A 449 165.273 36.684 559.212 1.00 76.99 C ANISOU 2939 CD LYS A 449 8588 14010 6654 -166 1588 -2491 C ATOM 2940 CE LYS A 449 164.707 37.567 560.312 1.00 80.79 C ANISOU 2940 CE LYS A 449 9050 14687 6958 -122 1751 -2857 C ATOM 2941 NZ LYS A 449 165.672 38.617 560.738 1.00 82.99 N ANISOU 2941 NZ LYS A 449 9334 15061 7137 -92 1532 -3202 N ATOM 2942 N THR A 450 165.977 36.267 555.302 1.00 67.45 N ANISOU 2942 N THR A 450 7205 11944 6480 -305 1153 -2022 N ATOM 2943 CA THR A 450 166.421 37.511 554.681 1.00 67.47 C ANISOU 2943 CA THR A 450 7151 11736 6746 -327 988 -2265 C ATOM 2944 C THR A 450 165.626 37.807 553.414 1.00 64.66 C ANISOU 2944 C THR A 450 6712 11036 6822 -333 989 -2218 C ATOM 2945 O THR A 450 165.312 38.969 553.129 1.00 64.08 O ANISOU 2945 O THR A 450 6591 10775 6983 -313 963 -2461 O ATOM 2946 CB THR A 450 167.918 37.443 554.378 1.00 65.43 C ANISOU 2946 CB THR A 450 6946 11492 6422 -370 755 -2218 C ATOM 2947 OG1 THR A 450 168.621 36.986 555.540 1.00 65.58 O ANISOU 2947 OG1 THR A 450 7043 11856 6017 -328 724 -2232 O ATOM 2948 CG2 THR A 450 168.444 38.816 553.990 1.00 65.89 C ANISOU 2948 CG2 THR A 450 6964 11361 6710 -419 632 -2513 C ATOM 2949 N PHE A 451 165.290 36.768 552.644 1.00 65.38 N ANISOU 2949 N PHE A 451 6791 11033 7018 -345 1007 -1917 N ATOM 2950 CA PHE A 451 164.446 36.954 551.466 1.00 66.21 C ANISOU 2950 CA PHE A 451 6812 10844 7500 -324 994 -1878 C ATOM 2951 C PHE A 451 163.106 37.565 551.850 1.00 70.12 C ANISOU 2951 C PHE A 451 7188 11323 8130 -258 1159 -2106 C ATOM 2952 O PHE A 451 162.690 38.585 551.288 1.00 72.03 O ANISOU 2952 O PHE A 451 7383 11340 8645 -199 1092 -2289 O ATOM 2953 CB PHE A 451 164.230 35.620 550.748 1.00 65.03 C ANISOU 2953 CB PHE A 451 6653 10648 7409 -349 1007 -1550 C ATOM 2954 CG PHE A 451 165.401 35.168 549.922 1.00 63.52 C ANISOU 2954 CG PHE A 451 6545 10370 7218 -394 817 -1348 C ATOM 2955 CD1 PHE A 451 166.428 36.038 549.606 1.00 65.99 C ANISOU 2955 CD1 PHE A 451 6914 10595 7564 -421 655 -1465 C ATOM 2956 CD2 PHE A 451 165.465 33.866 549.452 1.00 63.46 C ANISOU 2956 CD2 PHE A 451 6552 10360 7199 -418 818 -1057 C ATOM 2957 CE1 PHE A 451 167.503 35.615 548.842 1.00 64.34 C ANISOU 2957 CE1 PHE A 451 6761 10319 7366 -472 508 -1300 C ATOM 2958 CE2 PHE A 451 166.534 33.439 548.689 1.00 63.04 C ANISOU 2958 CE2 PHE A 451 6562 10236 7153 -451 653 -893 C ATOM 2959 CZ PHE A 451 167.555 34.315 548.384 1.00 64.41 C ANISOU 2959 CZ PHE A 451 6778 10343 7351 -478 502 -1016 C ATOM 2960 N LYS A 452 162.415 36.949 552.813 1.00 71.25 N ANISOU 2960 N LYS A 452 7289 11697 8084 -260 1385 -2099 N ATOM 2961 CA LYS A 452 161.109 37.455 553.220 1.00 72.98 C ANISOU 2961 CA LYS A 452 7364 11928 8437 -204 1573 -2336 C ATOM 2962 C LYS A 452 161.207 38.851 553.819 1.00 72.58 C ANISOU 2962 C LYS A 452 7313 11888 8375 -148 1550 -2700 C ATOM 2963 O LYS A 452 160.270 39.646 553.687 1.00 76.10 O ANISOU 2963 O LYS A 452 7634 12209 9072 -67 1600 -2938 O ATOM 2964 CB LYS A 452 160.453 36.490 554.207 1.00 81.85 C ANISOU 2964 CB LYS A 452 8463 13312 9326 -247 1864 -2251 C ATOM 2965 CG LYS A 452 159.803 35.292 553.535 1.00 91.02 C ANISOU 2965 CG LYS A 452 9545 14387 10651 -297 1953 -1987 C ATOM 2966 CD LYS A 452 158.810 35.746 552.473 1.00 97.46 C ANISOU 2966 CD LYS A 452 10162 14950 11918 -233 1891 -2115 C ATOM 2967 CE LYS A 452 158.222 34.569 551.713 1.00100.29 C ANISOU 2967 CE LYS A 452 10422 15216 12466 -286 1942 -1889 C ATOM 2968 NZ LYS A 452 157.283 35.016 550.646 1.00 99.85 N ANISOU 2968 NZ LYS A 452 10168 14934 12835 -194 1835 -2034 N ATOM 2969 N HIS A 453 162.326 39.173 554.472 1.00 73.75 N ANISOU 2969 N HIS A 453 7589 12180 8254 -180 1463 -2772 N ATOM 2970 CA HIS A 453 162.515 40.545 554.932 1.00 77.45 C ANISOU 2970 CA HIS A 453 8056 12619 8754 -140 1417 -3141 C ATOM 2971 C HIS A 453 162.663 41.502 553.755 1.00 77.26 C ANISOU 2971 C HIS A 453 8030 12211 9115 -114 1227 -3212 C ATOM 2972 O HIS A 453 162.168 42.634 553.801 1.00 80.60 O ANISOU 2972 O HIS A 453 8405 12482 9737 -41 1235 -3504 O ATOM 2973 CB HIS A 453 163.731 40.636 555.853 1.00 77.80 C ANISOU 2973 CB HIS A 453 8218 12910 8434 -185 1343 -3224 C ATOM 2974 CG HIS A 453 163.955 42.004 556.419 1.00 79.35 C ANISOU 2974 CG HIS A 453 8405 13093 8652 -160 1305 -3637 C ATOM 2975 ND1 HIS A 453 165.207 42.572 556.521 1.00 80.16 N ANISOU 2975 ND1 HIS A 453 8575 13194 8687 -216 1121 -3773 N ATOM 2976 CD2 HIS A 453 163.086 42.917 556.914 1.00 83.70 C ANISOU 2976 CD2 HIS A 453 8874 13624 9306 -89 1431 -3968 C ATOM 2977 CE1 HIS A 453 165.099 43.776 557.053 1.00 84.78 C ANISOU 2977 CE1 HIS A 453 9129 13747 9336 -189 1137 -4168 C ATOM 2978 NE2 HIS A 453 163.823 44.010 557.301 1.00 85.07 N ANISOU 2978 NE2 HIS A 453 9083 13770 9471 -103 1320 -4290 N ATOM 2979 N LEU A 454 163.335 41.062 552.688 1.00 75.01 N ANISOU 2979 N LEU A 454 7813 11754 8933 -165 1065 -2945 N ATOM 2980 CA LEU A 454 163.519 41.921 551.523 1.00 75.08 C ANISOU 2980 CA LEU A 454 7867 11391 9270 -144 904 -2971 C ATOM 2981 C LEU A 454 162.225 42.108 550.743 1.00 79.96 C ANISOU 2981 C LEU A 454 8394 11783 10205 -19 921 -2972 C ATOM 2982 O LEU A 454 162.019 43.164 550.134 1.00 80.51 O ANISOU 2982 O LEU A 454 8498 11555 10537 60 830 -3111 O ATOM 2983 CB LEU A 454 164.603 41.347 550.610 1.00 65.35 C ANISOU 2983 CB LEU A 454 6734 10064 8030 -236 751 -2689 C ATOM 2984 CG LEU A 454 166.050 41.456 551.094 1.00 58.13 C ANISOU 2984 CG LEU A 454 5895 9286 6904 -348 668 -2740 C ATOM 2985 CD1 LEU A 454 166.983 40.703 550.159 1.00 53.93 C ANISOU 2985 CD1 LEU A 454 5425 8686 6379 -428 546 -2450 C ATOM 2986 CD2 LEU A 454 166.464 42.914 551.206 1.00 57.34 C ANISOU 2986 CD2 LEU A 454 5833 9007 6946 -372 620 -3059 C ATOM 2987 N LEU A 455 161.345 41.107 550.747 1.00 82.94 N ANISOU 2987 N LEU A 455 8654 12286 10572 6 1034 -2830 N ATOM 2988 CA LEU A 455 160.133 41.166 549.941 1.00 84.17 C ANISOU 2988 CA LEU A 455 8688 12252 11041 129 1022 -2842 C ATOM 2989 C LEU A 455 158.943 41.766 550.678 1.00 94.48 C ANISOU 2989 C LEU A 455 9827 13624 12449 237 1179 -3160 C ATOM 2990 O LEU A 455 157.984 42.192 550.024 1.00 97.02 O ANISOU 2990 O LEU A 455 10040 13749 13075 381 1124 -3264 O ATOM 2991 CB LEU A 455 159.766 39.766 549.439 1.00 76.18 C ANISOU 2991 CB LEU A 455 7603 11313 10029 88 1057 -2555 C ATOM 2992 CG LEU A 455 160.804 39.098 548.535 1.00 69.22 C ANISOU 2992 CG LEU A 455 6862 10343 9095 6 896 -2244 C ATOM 2993 CD1 LEU A 455 160.304 37.748 548.046 1.00 67.76 C ANISOU 2993 CD1 LEU A 455 6588 10208 8949 -23 939 -2005 C ATOM 2994 CD2 LEU A 455 161.158 40.003 547.363 1.00 66.01 C ANISOU 2994 CD2 LEU A 455 6572 9603 8905 73 682 -2246 C ATOM 2995 N MET A 456 158.974 41.812 552.007 1.00103.83 N ANISOU 2995 N MET A 456 10985 15087 13380 187 1366 -3330 N ATOM 2996 CA MET A 456 157.858 42.380 552.750 1.00109.82 C ANISOU 2996 CA MET A 456 11575 15928 14223 284 1544 -3657 C ATOM 2997 C MET A 456 157.862 43.901 552.644 1.00113.21 C ANISOU 2997 C MET A 456 12038 16115 14860 404 1426 -3967 C ATOM 2998 O MET A 456 158.915 44.542 552.577 1.00113.45 O ANISOU 2998 O MET A 456 12240 16030 14834 357 1290 -3989 O ATOM 2999 CB MET A 456 157.910 41.954 554.219 1.00113.96 C ANISOU 2999 CB MET A 456 12093 16836 14370 196 1797 -3740 C ATOM 3000 CG MET A 456 159.105 42.487 554.992 1.00117.35 C ANISOU 3000 CG MET A 456 12696 17388 14505 137 1735 -3846 C ATOM 3001 SD MET A 456 158.976 42.178 556.765 1.00118.57 S ANISOU 3001 SD MET A 456 12853 18001 14195 93 2026 -4009 S ATOM 3002 CE MET A 456 157.499 43.110 557.164 1.00119.00 C ANISOU 3002 CE MET A 456 12685 18024 14504 225 2222 -4435 C ATOM 3003 N CYS A 457 156.664 44.478 552.622 1.00115.20 N ANISOU 3003 N CYS A 457 12116 16278 15377 562 1484 -4221 N ATOM 3004 CA CYS A 457 156.512 45.922 552.506 1.00116.58 C ANISOU 3004 CA CYS A 457 12319 16187 15789 709 1378 -4525 C ATOM 3005 C CYS A 457 156.757 46.572 553.863 1.00115.25 C ANISOU 3005 C CYS A 457 12158 16223 15409 672 1534 -4853 C ATOM 3006 O CYS A 457 156.077 46.251 554.844 1.00119.65 O ANISOU 3006 O CYS A 457 12562 17079 15821 666 1775 -5016 O ATOM 3007 CB CYS A 457 155.120 46.272 551.983 1.00121.95 C ANISOU 3007 CB CYS A 457 12794 16704 16837 926 1360 -4694 C ATOM 3008 SG CYS A 457 154.748 45.613 550.339 1.00122.28 S ANISOU 3008 SG CYS A 457 12821 16506 17135 1014 1135 -4368 S ATOM 3009 N HIS A 458 157.726 47.480 553.918 1.00109.05 N ANISOU 3009 N HIS A 458 11549 15279 14606 637 1408 -4962 N ATOM 3010 CA HIS A 458 158.031 48.200 555.149 1.00109.24 C ANISOU 3010 CA HIS A 458 11585 15474 14446 608 1518 -5315 C ATOM 3011 C HIS A 458 157.100 49.395 555.329 1.00114.29 C ANISOU 3011 C HIS A 458 12117 15926 15382 799 1553 -5720 C ATOM 3012 O HIS A 458 157.037 50.280 554.476 1.00115.34 O ANISOU 3012 O HIS A 458 12324 15650 15851 916 1382 -5768 O ATOM 3013 CB HIS A 458 159.490 48.664 555.156 1.00104.64 C ANISOU 3013 CB HIS A 458 11207 14803 13748 474 1371 -5305 C ATOM 3014 CG HIS A 458 160.463 47.598 555.555 1.00 98.56 C ANISOU 3014 CG HIS A 458 10509 14352 12586 301 1380 -5055 C ATOM 3015 ND1 HIS A 458 160.609 46.421 554.854 1.00 94.30 N ANISOU 3015 ND1 HIS A 458 9991 13850 11991 241 1338 -4641 N ATOM 3016 CD2 HIS A 458 161.340 47.534 556.585 1.00 98.76 C ANISOU 3016 CD2 HIS A 458 10593 14674 12259 197 1409 -5175 C ATOM 3017 CE1 HIS A 458 161.533 45.676 555.434 1.00 93.78 C ANISOU 3017 CE1 HIS A 458 9997 14073 11563 114 1344 -4504 C ATOM 3018 NE2 HIS A 458 161.992 46.329 556.487 1.00 96.06 N ANISOU 3018 NE2 HIS A 458 10310 14532 11657 92 1377 -4821 N TER 3019 HIS A 458 HETATM 3020 C1 QNB A 501 183.275 25.800 527.685 1.00 49.95 C HETATM 3021 C2 QNB A 501 183.907 26.845 528.614 1.00 47.67 C HETATM 3022 C3 QNB A 501 184.198 28.125 528.157 1.00 42.85 C HETATM 3023 C4 QNB A 501 184.771 29.063 529.000 1.00 43.33 C HETATM 3024 C5 QNB A 501 185.060 28.737 530.306 1.00 45.41 C HETATM 3025 C6 QNB A 501 184.779 27.472 530.773 1.00 46.68 C HETATM 3026 C7 QNB A 501 184.205 26.531 529.934 1.00 49.07 C HETATM 3027 C8 QNB A 501 183.887 25.869 526.281 1.00 56.32 C HETATM 3028 C9 QNB A 501 185.249 25.665 526.091 1.00 57.72 C HETATM 3029 C10 QNB A 501 185.804 25.728 524.825 1.00 56.54 C HETATM 3030 C11 QNB A 501 185.010 25.995 523.732 1.00 56.78 C HETATM 3031 C12 QNB A 501 183.659 26.200 523.904 1.00 58.91 C HETATM 3032 C13 QNB A 501 183.100 26.137 525.168 1.00 59.48 C HETATM 3033 C14 QNB A 501 181.745 25.989 527.636 1.00 45.61 C HETATM 3034 O15 QNB A 501 183.546 24.502 528.221 1.00 55.21 O HETATM 3035 O16 QNB A 501 180.970 25.079 527.732 1.00 44.66 O HETATM 3036 O17 QNB A 501 181.385 27.272 527.499 1.00 39.64 O HETATM 3037 C18 QNB A 501 179.965 27.588 527.592 1.00 38.38 C HETATM 3038 C19 QNB A 501 179.813 28.967 528.197 1.00 36.21 C HETATM 3039 N20 QNB A 501 179.342 29.940 527.210 1.00 42.64 N HETATM 3040 C21 QNB A 501 180.253 29.967 526.062 1.00 43.83 C HETATM 3041 C22 QNB A 501 180.301 28.609 525.371 1.00 43.83 C HETATM 3042 C23 QNB A 501 179.440 27.631 526.165 1.00 45.71 C HETATM 3043 C24 QNB A 501 178.001 28.142 526.197 1.00 47.21 C HETATM 3044 C25 QNB A 501 178.003 29.564 526.745 1.00 43.24 C HETATM 3045 O HOH A 601 180.460 31.326 521.770 1.00 49.04 O HETATM 3046 O HOH A 602 173.837 31.988 541.652 1.00 37.26 O HETATM 3047 O HOH A 603 185.009 20.841 518.151 1.00 50.14 O HETATM 3048 O HOH A 604 174.793 22.410 527.394 1.00 36.65 O HETATM 3049 O HOH A 605 176.952 26.177 539.209 1.00 38.81 O CONECT 625 1271 CONECT 1271 625 CONECT 2658 2676 CONECT 2676 2658 CONECT 3020 3021 3027 3033 3034 CONECT 3021 3020 3022 3026 CONECT 3022 3021 3023 CONECT 3023 3022 3024 CONECT 3024 3023 3025 CONECT 3025 3024 3026 CONECT 3026 3021 3025 CONECT 3027 3020 3028 3032 CONECT 3028 3027 3029 CONECT 3029 3028 3030 CONECT 3030 3029 3031 CONECT 3031 3030 3032 CONECT 3032 3027 3031 CONECT 3033 3020 3035 3036 CONECT 3034 3020 CONECT 3035 3033 CONECT 3036 3033 3037 CONECT 3037 3036 3038 3042 CONECT 3038 3037 3039 CONECT 3039 3038 3040 3044 CONECT 3040 3039 3041 CONECT 3041 3040 3042 CONECT 3042 3037 3041 3043 CONECT 3043 3042 3044 CONECT 3044 3039 3043 MASTER 343 0 1 18 0 0 3 6 3042 1 29 33 END