HEADER MEMBRANE PROTEIN/INHIBITOR 23-MAR-18 5ZK8 TITLE CRYSTAL STRUCTURE OF M2 MUSCARINIC ACETYLCHOLINE RECEPTOR BOUND WITH TITLE 2 NMS COMPND MOL_ID: 1; COMPND 2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M2,REDESIGNED APO- COMPND 3 CYTOCHROME B562,MUSCARINIC ACETYLCHOLINE RECEPTOR M2; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: UNP RESIDUES 10-217,UNP RESIDUES 377-466; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CHRM2; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR CRYSTALLOGRAPHY, MEMBRANE 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 4 23-MAR-22 5ZK8 1 REMARK REVDAT 3 12-DEC-18 5ZK8 1 REMARK DBREF SEQADV HELIX REVDAT 3 2 1 SSBOND SITE ATOM REVDAT 2 28-NOV-18 5ZK8 1 JRNL REVDAT 1 21-NOV-18 5ZK8 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. 3.00 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.34 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 9702 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.233 REMARK 3 R VALUE (WORKING SET) : 0.231 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.380 REMARK 3 FREE R VALUE TEST SET COUNT : 522 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 38.3400 - 4.7601 1.00 2352 129 0.2336 0.2542 REMARK 3 2 4.7601 - 3.7793 1.00 2279 130 0.2095 0.2687 REMARK 3 3 3.7793 - 3.3019 1.00 2267 133 0.2419 0.2826 REMARK 3 4 3.3019 - 3.0001 1.00 2282 130 0.2609 0.3026 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) : 0.340 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.750 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 3023 REMARK 3 ANGLE : 0.475 4127 REMARK 3 CHIRALITY : 0.036 496 REMARK 3 PLANARITY : 0.003 494 REMARK 3 DIHEDRAL : 11.276 1801 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 184.7394 31.7294 532.5604 REMARK 3 T TENSOR REMARK 3 T11: 0.1938 T22: 0.3308 REMARK 3 T33: 0.2782 T12: -0.0131 REMARK 3 T13: 0.0264 T23: -0.0557 REMARK 3 L TENSOR REMARK 3 L11: 2.0323 L22: 2.6027 REMARK 3 L33: 2.1712 L12: -0.5177 REMARK 3 L13: -0.1352 L23: -0.0718 REMARK 3 S TENSOR REMARK 3 S11: -0.0602 S12: -0.1751 S13: 0.0300 REMARK 3 S21: 0.2913 S22: 0.0155 S23: -0.1316 REMARK 3 S31: -0.0889 S32: 0.2399 S33: 0.0241 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 214 THROUGH 214 ) OR (RESID REMARK 3 1001 THROUGH 1079 )) REMARK 3 ORIGIN FOR THE GROUP (A): 169.8288 13.3744 569.8650 REMARK 3 T TENSOR REMARK 3 T11: 1.2061 T22: 2.0531 REMARK 3 T33: 0.8823 T12: 0.0426 REMARK 3 T13: -0.3042 T23: 0.1827 REMARK 3 L TENSOR REMARK 3 L11: 3.9525 L22: 3.6953 REMARK 3 L33: 2.0536 L12: -1.8749 REMARK 3 L13: 1.3920 L23: 0.1889 REMARK 3 S TENSOR REMARK 3 S11: 0.8617 S12: -1.3281 S13: -0.3724 REMARK 3 S21: -0.6987 S22: -0.0530 S23: -0.4173 REMARK 3 S31: 1.1284 S32: -0.5363 S33: -0.7615 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 1080 THROUFH 1106 ) OR (RESID REMARK 3 384 THROUGH 459 )) REMARK 3 ORIGIN FOR THE GROUP (A): 176.545 25.580 534.766 REMARK 3 T TENSOR REMARK 3 T11: 0.4528 T22: 0.5023 REMARK 3 T33: 0.3518 T12: 0.0206 REMARK 3 T13: 0.0327 T23: 0.0523 REMARK 3 L TENSOR REMARK 3 L11: 1.5154 L22: 1.9580 REMARK 3 L33: 2.4640 L12: 0.3133 REMARK 3 L13: -0.1837 L23: 0.0640 REMARK 3 S TENSOR REMARK 3 S11: 0.0631 S12: -0.7242 S13: -0.0119 REMARK 3 S21: 0.4356 S22: 0.0266 S23: 0.1428 REMARK 3 S31: -0.4279 S32: 0.1345 S33: -0.0573 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 5ZK8 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_1300007223. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-DEC-14 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 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 : 9702 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 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 : 116.6 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.18 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 (%): 51.81 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 NMS 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 29.60500 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 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 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 GLU A 382 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 PRO A1056 CG CD 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 GLN A 55 78.64 -115.59 REMARK 500 THR A 130 -41.31 -135.21 REMARK 500 PHE A 195 -59.65 -136.66 REMARK 500 ASN A1022 -153.15 -112.17 REMARK 500 TYR A 440 -34.04 -133.90 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 3C0 A 501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5XB9 RELATED DB: PDB REMARK 900 RELATED ID: 5XBA RELATED DB: PDB REMARK 900 RELATED ID: 5XBB RELATED DB: PDB DBREF 5ZK8 A 10 217 UNP P08172 ACM2_HUMAN 10 217 DBREF 5ZK8 A 1001 1106 PDB 5ZK8 5ZK8 1001 1106 DBREF 5ZK8 A 377 466 UNP P08172 ACM2_HUMAN 377 466 SEQADV 5ZK8 GLY A -1 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 PRO A 0 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 MET A 1 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 ASP A 2 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 ASP A 3 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 SER A 4 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 THR A 5 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 ASP A 6 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 SER A 7 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 SER A 8 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 ASP A 9 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 LEU A 467 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 GLU A 468 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 VAL A 469 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 LEU A 470 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 PHE A 471 UNP P08172 EXPRESSION TAG SEQADV 5ZK8 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 SER 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 3C0 A 501 23 HETNAM 3C0 N-METHYL SCOPOLAMINE HETSYN 3C0 (1R,2R,4S,5S,7S)-7-{[(2S)-3-HYDROXY-2- HETSYN 2 3C0 PHENYLPROPANOYL]OXY}-9,9-DIMETHYL-3-OXA-9- HETSYN 3 3C0 AZONIATRICYCLO[3.3.1.0~2,4~]NONANE FORMUL 2 3C0 C18 H24 N O4 1+ FORMUL 3 HOH *4(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 THR A 130 ARG A 135 1 6 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 ALA A 1020 1 19 HELIX 12 AB3 ALA A 1023 ALA A 1043 1 21 HELIX 13 AB4 GLU A 1057 ASN A 1080 1 24 HELIX 14 AB5 LYS A 1083 ALA A 1090 1 8 HELIX 15 AB6 ALA A 1090 LEU A 1106 1 17 HELIX 16 AB7 LYS A 384 CYS A 413 1 30 HELIX 17 AB8 PRO A 418 ASN A 436 1 19 HELIX 18 AB9 TYR A 440 CYS A 443 5 4 HELIX 19 AC1 ASN A 444 LEU A 455 1 12 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 12 ASP A 103 TYR A 104 SER A 107 TRP A 155 SITE 2 AC1 12 ALA A 191 ALA A 194 TRP A 400 TYR A 403 SITE 3 AC1 12 ASN A 404 TYR A 426 CYS A 429 TYR A 430 CRYST1 46.280 59.210 88.960 90.00 98.54 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 0.021608 0.000000 0.003245 0.00000 SCALE2 0.000000 0.016889 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011367 0.00000 ATOM 1 N TYR A 18 157.146 27.227 510.877 1.00180.32 N ANISOU 1 N TYR A 18 20064 24279 24170 -67 -2431 -1679 N ATOM 2 CA TYR A 18 157.514 27.166 512.287 1.00176.13 C ANISOU 2 CA TYR A 18 19478 23645 23797 -123 -2156 -1613 C ATOM 3 C TYR A 18 158.764 27.999 512.556 1.00170.91 C ANISOU 3 C TYR A 18 18984 22976 22979 2 -2036 -1551 C ATOM 4 O TYR A 18 159.062 28.337 513.701 1.00172.75 O ANISOU 4 O TYR A 18 19176 23151 23311 7 -1818 -1470 O ATOM 5 CB TYR A 18 157.736 25.714 512.721 1.00183.08 C ANISOU 5 CB TYR A 18 20376 24394 24792 -327 -2060 -1709 C ATOM 6 CG TYR A 18 158.025 25.547 514.197 1.00189.23 C ANISOU 6 CG TYR A 18 21101 25066 25730 -393 -1776 -1630 C ATOM 7 CD1 TYR A 18 156.995 25.533 515.128 1.00193.49 C ANISOU 7 CD1 TYR A 18 21428 25596 26494 -447 -1658 -1548 C ATOM 8 CD2 TYR A 18 159.327 25.400 514.659 1.00187.86 C ANISOU 8 CD2 TYR A 18 21095 24813 25471 -395 -1624 -1634 C ATOM 9 CE1 TYR A 18 157.253 25.382 516.478 1.00192.53 C ANISOU 9 CE1 TYR A 18 21284 25382 26486 -497 -1394 -1468 C ATOM 10 CE2 TYR A 18 159.595 25.249 516.007 1.00186.20 C ANISOU 10 CE2 TYR A 18 20851 24511 25387 -449 -1371 -1555 C ATOM 11 CZ TYR A 18 158.554 25.240 516.911 1.00187.35 C ANISOU 11 CZ TYR A 18 20807 24644 25734 -497 -1256 -1470 C ATOM 12 OH TYR A 18 158.816 25.088 518.254 1.00183.00 O ANISOU 12 OH TYR A 18 20247 24008 25275 -540 -1000 -1385 O ATOM 13 N LYS A 19 159.486 28.335 511.485 1.00151.33 N ANISOU 13 N LYS A 19 16699 20562 20240 103 -2178 -1588 N ATOM 14 CA LYS A 19 160.735 29.077 511.636 1.00129.60 C ANISOU 14 CA LYS A 19 14122 17806 17315 212 -2067 -1525 C ATOM 15 C LYS A 19 160.491 30.460 512.226 1.00108.79 C ANISOU 15 C LYS A 19 11428 15187 14720 359 -1969 -1357 C ATOM 16 O LYS A 19 161.288 30.946 513.037 1.00106.86 O ANISOU 16 O LYS A 19 11294 14858 14450 380 -1739 -1255 O ATOM 17 CB LYS A 19 161.453 29.187 510.289 1.00133.06 C ANISOU 17 CB LYS A 19 14818 18304 17434 296 -2205 -1556 C ATOM 18 CG LYS A 19 161.976 27.863 509.737 1.00133.54 C ANISOU 18 CG LYS A 19 15003 18325 17411 171 -2255 -1724 C ATOM 19 CD LYS A 19 160.895 27.090 508.992 1.00130.84 C ANISOU 19 CD LYS A 19 14567 18015 17131 92 -2474 -1844 C ATOM 20 CE LYS A 19 161.344 25.675 508.672 1.00122.70 C ANISOU 20 CE LYS A 19 13654 16893 16072 -52 -2477 -2008 C ATOM 21 NZ LYS A 19 160.245 24.876 508.064 1.00119.53 N ANISOU 21 NZ LYS A 19 13165 16492 15757 -154 -2656 -2105 N ATOM 22 N THR A 20 159.395 31.113 511.830 1.00 98.72 N ANISOU 22 N THR A 20 9999 14006 13503 463 -2134 -1321 N ATOM 23 CA THR A 20 159.064 32.411 512.410 1.00 94.21 C ANISOU 23 CA THR A 20 9349 13445 13002 620 -2055 -1182 C ATOM 24 C THR A 20 158.716 32.276 513.887 1.00 94.56 C ANISOU 24 C THR A 20 9230 13402 13294 538 -1811 -1145 C ATOM 25 O THR A 20 159.054 33.149 514.695 1.00 87.95 O ANISOU 25 O THR A 20 8429 12513 12475 626 -1635 -1045 O ATOM 26 CB THR A 20 157.908 33.056 511.643 1.00 93.95 C ANISOU 26 CB THR A 20 9219 13507 12970 742 -2254 -1125 C ATOM 27 OG1 THR A 20 156.740 32.232 511.744 1.00 93.61 O ANISOU 27 OG1 THR A 20 8968 13479 13120 610 -2304 -1182 O ATOM 28 CG2 THR A 20 158.272 33.231 510.176 1.00 97.00 C ANISOU 28 CG2 THR A 20 9802 13981 13074 835 -2485 -1144 C ATOM 29 N PHE A 21 158.041 31.185 514.255 1.00 96.86 N ANISOU 29 N PHE A 21 9387 13662 13753 366 -1777 -1206 N ATOM 30 CA PHE A 21 157.743 30.930 515.660 1.00 92.78 C ANISOU 30 CA PHE A 21 8747 13065 13438 281 -1532 -1162 C ATOM 31 C PHE A 21 159.017 30.648 516.445 1.00 85.76 C ANISOU 31 C PHE A 21 8004 12081 12503 221 -1331 -1170 C ATOM 32 O PHE A 21 159.137 31.044 517.612 1.00 86.38 O ANISOU 32 O PHE A 21 8058 12104 12659 240 -1114 -1096 O ATOM 33 CB PHE A 21 156.764 29.760 515.773 1.00 97.69 C ANISOU 33 CB PHE A 21 9209 13676 14232 107 -1553 -1217 C ATOM 34 CG PHE A 21 156.323 29.460 517.178 1.00 97.11 C ANISOU 34 CG PHE A 21 9009 13536 14351 24 -1305 -1156 C ATOM 35 CD1 PHE A 21 155.207 30.080 517.716 1.00103.81 C ANISOU 35 CD1 PHE A 21 9665 14438 15339 94 -1243 -1070 C ATOM 36 CD2 PHE A 21 157.013 28.544 517.956 1.00 88.71 C ANISOU 36 CD2 PHE A 21 8027 12362 13318 -116 -1130 -1180 C ATOM 37 CE1 PHE A 21 154.793 29.799 519.008 1.00101.83 C ANISOU 37 CE1 PHE A 21 9314 14139 15236 26 -1005 -1011 C ATOM 38 CE2 PHE A 21 156.607 28.261 519.247 1.00 90.50 C ANISOU 38 CE2 PHE A 21 8162 12534 13692 -183 -901 -1111 C ATOM 39 CZ PHE A 21 155.495 28.888 519.773 1.00 95.48 C ANISOU 39 CZ PHE A 21 8609 13226 14443 -114 -836 -1029 C ATOM 40 N GLU A 22 159.984 29.974 515.814 1.00 87.96 N ANISOU 40 N GLU A 22 8438 12342 12640 157 -1401 -1261 N ATOM 41 CA GLU A 22 161.214 29.608 516.506 1.00 86.68 C ANISOU 41 CA GLU A 22 8472 12068 12396 90 -1189 -1234 C ATOM 42 C GLU A 22 162.068 30.825 516.824 1.00 81.39 C ANISOU 42 C GLU A 22 7982 11371 11572 221 -1060 -1109 C ATOM 43 O GLU A 22 162.787 30.826 517.826 1.00 80.28 O ANISOU 43 O GLU A 22 7924 11147 11431 187 -854 -1060 O ATOM 44 CB GLU A 22 162.020 28.611 515.673 1.00102.93 C ANISOU 44 CB GLU A 22 10701 14097 14309 4 -1272 -1337 C ATOM 45 CG GLU A 22 163.256 28.082 516.392 1.00109.62 C ANISOU 45 CG GLU A 22 11721 14831 15098 -65 -1064 -1315 C ATOM 46 CD GLU A 22 164.142 27.241 515.498 1.00107.88 C ANISOU 46 CD GLU A 22 11687 14587 14716 -110 -1134 -1409 C ATOM 47 OE1 GLU A 22 163.713 26.914 514.373 1.00104.50 O ANISOU 47 OE1 GLU A 22 11252 14221 14231 -112 -1344 -1512 O ATOM 48 OE2 GLU A 22 165.270 26.910 515.921 1.00104.90 O ANISOU 48 OE2 GLU A 22 11463 14131 14263 -135 -982 -1385 O ATOM 49 N VAL A 23 162.017 31.861 515.988 1.00 66.66 N ANISOU 49 N VAL A 23 6185 9569 9574 368 -1184 -1057 N ATOM 50 CA VAL A 23 162.753 33.085 516.289 1.00 65.89 C ANISOU 50 CA VAL A 23 6250 9426 9358 483 -1064 -935 C ATOM 51 C VAL A 23 162.247 33.694 517.591 1.00 79.47 C ANISOU 51 C VAL A 23 7848 11102 11246 521 -896 -874 C ATOM 52 O VAL A 23 163.031 34.012 518.494 1.00 80.37 O ANISOU 52 O VAL A 23 8077 11133 11329 510 -708 -823 O ATOM 53 CB VAL A 23 162.646 34.073 515.117 1.00 74.43 C ANISOU 53 CB VAL A 23 7421 10575 10285 637 -1232 -877 C ATOM 54 CG1 VAL A 23 163.372 35.367 515.441 1.00 71.67 C ANISOU 54 CG1 VAL A 23 7240 10153 9840 743 -1103 -747 C ATOM 55 CG2 VAL A 23 163.212 33.437 513.866 1.00 81.48 C ANISOU 55 CG2 VAL A 23 8460 11517 10980 603 -1374 -942 C ATOM 56 N VAL A 24 160.924 33.840 517.711 1.00 78.67 N ANISOU 56 N VAL A 24 7506 11062 11323 569 -964 -884 N ATOM 57 CA VAL A 24 160.328 34.392 518.927 1.00 61.45 C ANISOU 57 CA VAL A 24 5192 8850 9305 621 -795 -835 C ATOM 58 C VAL A 24 160.620 33.495 520.126 1.00 58.31 C ANISOU 58 C VAL A 24 4772 8387 8995 473 -589 -861 C ATOM 59 O VAL A 24 161.007 33.977 521.198 1.00 76.73 O ANISOU 59 O VAL A 24 7178 10653 11323 500 -394 -809 O ATOM 60 CB VAL A 24 158.813 34.594 518.738 1.00 49.12 C ANISOU 60 CB VAL A 24 3343 7386 7936 699 -912 -847 C ATOM 61 CG1 VAL A 24 158.195 35.266 519.965 1.00 50.80 C ANISOU 61 CG1 VAL A 24 3452 7563 8286 775 -709 -781 C ATOM 62 CG2 VAL A 24 158.535 35.401 517.485 1.00 47.74 C ANISOU 62 CG2 VAL A 24 3201 7281 7655 853 -1143 -815 C ATOM 63 N PHE A 25 160.426 32.180 519.971 1.00 44.60 N ANISOU 63 N PHE A 25 2945 6663 7340 318 -634 -943 N ATOM 64 CA PHE A 25 160.651 31.269 521.092 1.00 48.98 C ANISOU 64 CA PHE A 25 3481 7147 7984 181 -440 -952 C ATOM 65 C PHE A 25 162.102 31.315 521.557 1.00 54.28 C ANISOU 65 C PHE A 25 4416 7731 8477 164 -309 -915 C ATOM 66 O PHE A 25 162.377 31.312 522.763 1.00 57.51 O ANISOU 66 O PHE A 25 4857 8083 8909 143 -112 -873 O ATOM 67 CB PHE A 25 160.253 29.843 520.703 1.00 41.84 C ANISOU 67 CB PHE A 25 2503 6232 7163 13 -522 -1026 C ATOM 68 CG PHE A 25 160.421 28.833 521.813 1.00 56.46 C ANISOU 68 CG PHE A 25 4371 7989 9091 -126 -324 -1006 C ATOM 69 CD1 PHE A 25 159.466 28.709 522.812 1.00 70.30 C ANISOU 69 CD1 PHE A 25 6003 9732 10977 -155 -175 -935 C ATOM 70 CD2 PHE A 25 161.526 27.997 521.847 1.00 50.33 C ANISOU 70 CD2 PHE A 25 3733 7141 8248 -218 -287 -1053 C ATOM 71 CE1 PHE A 25 159.617 27.777 523.829 1.00 65.61 C ANISOU 71 CE1 PHE A 25 5438 9054 10437 -273 4 -903 C ATOM 72 CE2 PHE A 25 161.682 27.064 522.859 1.00 48.58 C ANISOU 72 CE2 PHE A 25 3538 6827 8095 -331 -113 -1021 C ATOM 73 CZ PHE A 25 160.727 26.954 523.850 1.00 58.04 C ANISOU 73 CZ PHE A 25 4626 8013 9415 -359 30 -942 C ATOM 74 N ILE A 26 163.042 31.379 520.615 1.00 49.25 N ANISOU 74 N ILE A 26 3965 7090 7656 178 -415 -929 N ATOM 75 CA ILE A 26 164.457 31.420 520.967 1.00 39.08 C ANISOU 75 CA ILE A 26 2902 5732 6213 160 -304 -896 C ATOM 76 C ILE A 26 164.808 32.746 521.630 1.00 47.37 C ANISOU 76 C ILE A 26 4043 6753 7204 270 -195 -812 C ATOM 77 O ILE A 26 165.606 32.788 522.574 1.00 62.00 O ANISOU 77 O ILE A 26 6001 8544 9011 243 -47 -782 O ATOM 78 CB ILE A 26 165.323 31.151 519.722 1.00 44.66 C ANISOU 78 CB ILE A 26 3765 6455 6748 152 -434 -933 C ATOM 79 CG1 ILE A 26 165.235 29.676 519.328 1.00 56.47 C ANISOU 79 CG1 ILE A 26 5219 7941 8295 26 -499 -1033 C ATOM 80 CG2 ILE A 26 166.775 31.545 519.964 1.00 34.66 C ANISOU 80 CG2 ILE A 26 2710 5136 5323 166 -328 -879 C ATOM 81 CD1 ILE A 26 165.651 28.727 520.428 1.00 51.14 C ANISOU 81 CD1 ILE A 26 4554 7180 7698 -83 -334 -1034 C ATOM 82 N VAL A 27 164.222 33.851 521.156 1.00 47.90 N ANISOU 82 N VAL A 27 4075 6856 7270 399 -275 -776 N ATOM 83 CA VAL A 27 164.484 35.143 521.788 1.00 46.36 C ANISOU 83 CA VAL A 27 3972 6607 7036 505 -173 -707 C ATOM 84 C VAL A 27 163.962 35.147 523.222 1.00 51.88 C ANISOU 84 C VAL A 27 4575 7278 7859 502 5 -703 C ATOM 85 O VAL A 27 164.637 35.624 524.143 1.00 52.68 O ANISOU 85 O VAL A 27 4803 7313 7902 512 142 -678 O ATOM 86 CB VAL A 27 163.876 36.291 520.955 1.00 42.81 C ANISOU 86 CB VAL A 27 3505 6187 6573 658 -299 -662 C ATOM 87 CG1 VAL A 27 163.841 37.577 521.762 1.00 31.61 C ANISOU 87 CG1 VAL A 27 2145 4694 5171 774 -181 -605 C ATOM 88 CG2 VAL A 27 164.675 36.517 519.678 1.00 42.17 C ANISOU 88 CG2 VAL A 27 3590 6117 6314 675 -429 -637 C ATOM 89 N LEU A 28 162.767 34.590 523.438 1.00 49.67 N ANISOU 89 N LEU A 28 4070 7052 7750 483 7 -732 N ATOM 90 CA LEU A 28 162.188 34.579 524.778 1.00 43.06 C ANISOU 90 CA LEU A 28 3132 6200 7028 487 198 -720 C ATOM 91 C LEU A 28 162.967 33.664 525.719 1.00 37.65 C ANISOU 91 C LEU A 28 2542 5465 6300 360 343 -723 C ATOM 92 O LEU A 28 163.234 34.031 526.870 1.00 44.81 O ANISOU 92 O LEU A 28 3527 6330 7171 388 509 -698 O ATOM 93 CB LEU A 28 160.719 34.159 524.709 1.00 40.11 C ANISOU 93 CB LEU A 28 2470 5905 6865 485 171 -742 C ATOM 94 CG LEU A 28 159.773 35.084 523.939 1.00 40.55 C ANISOU 94 CG LEU A 28 2394 6025 6989 637 32 -730 C ATOM 95 CD1 LEU A 28 158.352 34.545 523.979 1.00 38.25 C ANISOU 95 CD1 LEU A 28 1894 5799 6841 594 16 -708 C ATOM 96 CD2 LEU A 28 159.833 36.500 524.494 1.00 41.01 C ANISOU 96 CD2 LEU A 28 2547 6032 7003 809 131 -682 C ATOM 97 N VAL A 29 163.341 32.471 525.251 1.00 30.50 N ANISOU 97 N VAL A 29 1643 4558 5390 230 278 -757 N ATOM 98 CA VAL A 29 164.092 31.552 526.102 1.00 44.77 C ANISOU 98 CA VAL A 29 3543 6308 7159 123 405 -749 C ATOM 99 C VAL A 29 165.473 32.116 526.417 1.00 60.00 C ANISOU 99 C VAL A 29 5707 8188 8903 154 445 -723 C ATOM 100 O VAL A 29 165.928 32.075 527.568 1.00 71.45 O ANISOU 100 O VAL A 29 7240 9601 10308 142 588 -695 O ATOM 101 CB VAL A 29 164.181 30.163 525.442 1.00 37.58 C ANISOU 101 CB VAL A 29 2595 5388 6295 -11 318 -798 C ATOM 102 CG1 VAL A 29 165.182 29.289 526.181 1.00 38.86 C ANISOU 102 CG1 VAL A 29 2895 5478 6390 -95 428 -778 C ATOM 103 CG2 VAL A 29 162.812 29.499 525.419 1.00 36.88 C ANISOU 103 CG2 VAL A 29 2259 5332 6420 -76 308 -824 C ATOM 104 N ALA A 30 166.156 32.663 525.409 1.00 45.51 N ANISOU 104 N ALA A 30 3979 6355 6957 192 317 -729 N ATOM 105 CA ALA A 30 167.496 33.201 525.622 1.00 40.20 C ANISOU 105 CA ALA A 30 3505 5638 6130 205 347 -704 C ATOM 106 C ALA A 30 167.466 34.401 526.563 1.00 48.08 C ANISOU 106 C ALA A 30 4562 6602 7105 291 448 -675 C ATOM 107 O ALA A 30 168.268 34.489 527.503 1.00 56.40 O ANISOU 107 O ALA A 30 5730 7615 8083 270 542 -666 O ATOM 108 CB ALA A 30 168.124 33.577 524.279 1.00 38.16 C ANISOU 108 CB ALA A 30 3334 5395 5772 227 206 -704 C ATOM 109 N GLY A 31 166.543 35.336 526.327 1.00 33.26 N ANISOU 109 N GLY A 31 2610 4737 5291 397 422 -668 N ATOM 110 CA GLY A 31 166.419 36.475 527.222 1.00 29.58 C ANISOU 110 CA GLY A 31 2203 4221 4813 493 524 -656 C ATOM 111 C GLY A 31 166.051 36.067 528.635 1.00 31.81 C ANISOU 111 C GLY A 31 2448 4504 5133 476 696 -665 C ATOM 112 O GLY A 31 166.529 36.658 529.609 1.00 40.54 O ANISOU 112 O GLY A 31 3682 5562 6160 507 794 -670 O ATOM 113 N SER A 32 165.202 35.045 528.767 1.00 31.91 N ANISOU 113 N SER A 32 2292 4570 5264 423 735 -667 N ATOM 114 CA SER A 32 164.846 34.542 530.090 1.00 39.58 C ANISOU 114 CA SER A 32 3229 5544 6264 399 917 -657 C ATOM 115 C SER A 32 166.067 33.978 530.807 1.00 53.25 C ANISOU 115 C SER A 32 5135 7239 7860 318 970 -646 C ATOM 116 O SER A 32 166.302 34.273 531.985 1.00 72.65 O ANISOU 116 O SER A 32 7691 9676 10236 349 1099 -640 O ATOM 117 CB SER A 32 163.753 33.480 529.968 1.00 36.28 C ANISOU 117 CB SER A 32 2588 5179 6018 330 943 -650 C ATOM 118 OG SER A 32 162.634 33.980 529.257 1.00 48.41 O ANISOU 118 OG SER A 32 3939 6766 7689 407 868 -663 O ATOM 119 N LEU A 33 166.862 33.165 530.104 1.00 37.79 N ANISOU 119 N LEU A 33 3218 5274 5866 224 867 -646 N ATOM 120 CA LEU A 33 168.065 32.602 530.709 1.00 38.88 C ANISOU 120 CA LEU A 33 3506 5381 5885 162 900 -631 C ATOM 121 C LEU A 33 169.041 33.696 531.122 1.00 38.68 C ANISOU 121 C LEU A 33 3652 5326 5720 214 893 -641 C ATOM 122 O LEU A 33 169.621 33.643 532.215 1.00 45.21 O ANISOU 122 O LEU A 33 4588 6139 6452 209 973 -633 O ATOM 123 CB LEU A 33 168.730 31.626 529.739 1.00 43.74 C ANISOU 123 CB LEU A 33 4127 5993 6498 76 786 -639 C ATOM 124 CG LEU A 33 167.953 30.342 529.445 1.00 57.25 C ANISOU 124 CG LEU A 33 5699 7708 8344 -6 789 -641 C ATOM 125 CD1 LEU A 33 168.478 29.671 528.187 1.00 60.20 C ANISOU 125 CD1 LEU A 33 6084 8076 8712 -61 645 -678 C ATOM 126 CD2 LEU A 33 168.024 29.393 530.632 1.00 44.84 C ANISOU 126 CD2 LEU A 33 4154 6105 6778 -61 932 -595 C ATOM 127 N SER A 34 169.232 34.700 530.262 1.00 33.75 N ANISOU 127 N SER A 34 3058 4686 5080 262 793 -657 N ATOM 128 CA SER A 34 170.115 35.811 530.604 1.00 29.87 C ANISOU 128 CA SER A 34 2722 4145 4482 297 783 -671 C ATOM 129 C SER A 34 169.627 36.533 531.854 1.00 36.07 C ANISOU 129 C SER A 34 3554 4905 5246 373 907 -693 C ATOM 130 O SER A 34 170.409 36.812 532.772 1.00 48.28 O ANISOU 130 O SER A 34 5236 6424 6682 363 943 -714 O ATOM 131 CB SER A 34 170.216 36.780 529.426 1.00 41.84 C ANISOU 131 CB SER A 34 4256 5634 6007 338 672 -667 C ATOM 132 OG SER A 34 170.983 37.921 529.767 1.00 53.48 O ANISOU 132 OG SER A 34 5876 7039 7405 360 671 -679 O ATOM 133 N LEU A 35 168.326 36.831 531.913 1.00 38.78 N ANISOU 133 N LEU A 35 3780 5263 5690 455 970 -696 N ATOM 134 CA LEU A 35 167.783 37.544 533.064 1.00 40.96 C ANISOU 134 CA LEU A 35 4099 5518 5944 548 1107 -725 C ATOM 135 C LEU A 35 167.943 36.735 534.346 1.00 46.32 C ANISOU 135 C LEU A 35 4826 6228 6545 507 1238 -717 C ATOM 136 O LEU A 35 168.305 37.284 535.395 1.00 53.98 O ANISOU 136 O LEU A 35 5941 7171 7397 549 1310 -753 O ATOM 137 CB LEU A 35 166.313 37.884 532.821 1.00 45.39 C ANISOU 137 CB LEU A 35 4490 6106 6651 651 1158 -722 C ATOM 138 CG LEU A 35 165.639 38.752 533.883 1.00 63.73 C ANISOU 138 CG LEU A 35 6846 8404 8964 780 1311 -759 C ATOM 139 CD1 LEU A 35 166.360 40.084 534.019 1.00 56.34 C ANISOU 139 CD1 LEU A 35 6111 7365 7932 843 1267 -810 C ATOM 140 CD2 LEU A 35 164.172 38.962 533.543 1.00 78.36 C ANISOU 140 CD2 LEU A 35 8486 10300 10988 885 1358 -747 C ATOM 141 N VAL A 36 167.686 35.425 534.281 1.00 51.24 N ANISOU 141 N VAL A 36 5342 6901 7227 426 1266 -670 N ATOM 142 CA VAL A 36 167.840 34.577 535.461 1.00 44.87 C ANISOU 142 CA VAL A 36 4590 6116 6342 389 1394 -637 C ATOM 143 C VAL A 36 169.293 34.559 535.921 1.00 36.99 C ANISOU 143 C VAL A 36 3784 5096 5175 348 1330 -647 C ATOM 144 O VAL A 36 169.581 34.659 537.121 1.00 33.61 O ANISOU 144 O VAL A 36 3484 4673 4615 378 1416 -653 O ATOM 145 CB VAL A 36 167.319 33.157 535.171 1.00 43.04 C ANISOU 145 CB VAL A 36 4210 5914 6229 297 1425 -578 C ATOM 146 CG1 VAL A 36 167.689 32.211 536.303 1.00 37.46 C ANISOU 146 CG1 VAL A 36 3593 5212 5429 252 1541 -522 C ATOM 147 CG2 VAL A 36 165.813 33.180 534.969 1.00 48.08 C ANISOU 147 CG2 VAL A 36 4638 6587 7042 333 1507 -571 C ATOM 148 N THR A 37 170.230 34.437 534.976 1.00 37.85 N ANISOU 148 N THR A 37 3913 5188 5281 286 1176 -650 N ATOM 149 CA THR A 37 171.649 34.460 535.324 1.00 24.87 C ANISOU 149 CA THR A 37 2417 3532 3501 247 1102 -659 C ATOM 150 C THR A 37 172.019 35.761 536.028 1.00 41.80 C ANISOU 150 C THR A 37 4703 5641 5539 305 1103 -724 C ATOM 151 O THR A 37 172.631 35.750 537.106 1.00 57.27 O ANISOU 151 O THR A 37 6789 7610 7362 307 1126 -740 O ATOM 152 CB THR A 37 172.498 34.272 534.065 1.00 23.62 C ANISOU 152 CB THR A 37 2232 3365 3376 184 955 -654 C ATOM 153 OG1 THR A 37 172.193 33.009 533.460 1.00 27.60 O ANISOU 153 OG1 THR A 37 2629 3891 3968 131 950 -613 O ATOM 154 CG2 THR A 37 173.979 34.321 534.405 1.00 23.04 C ANISOU 154 CG2 THR A 37 2279 3290 3186 144 880 -662 C ATOM 155 N ILE A 38 171.639 36.895 535.432 1.00 35.93 N ANISOU 155 N ILE A 38 3947 4850 4854 356 1070 -764 N ATOM 156 CA ILE A 38 171.979 38.198 536.000 1.00 34.81 C ANISOU 156 CA ILE A 38 3949 4644 4633 406 1063 -837 C ATOM 157 C ILE A 38 171.403 38.338 537.404 1.00 48.84 C ANISOU 157 C ILE A 38 5803 6434 6319 484 1209 -874 C ATOM 158 O ILE A 38 172.109 38.714 538.349 1.00 60.07 O ANISOU 158 O ILE A 38 7384 7842 7598 484 1200 -929 O ATOM 159 CB ILE A 38 171.491 39.328 535.075 1.00 34.18 C ANISOU 159 CB ILE A 38 3839 4494 4653 464 1020 -856 C ATOM 160 CG1 ILE A 38 172.198 39.256 533.720 1.00 36.46 C ANISOU 160 CG1 ILE A 38 4087 4774 4993 389 883 -815 C ATOM 161 CG2 ILE A 38 171.716 40.684 535.720 1.00 27.56 C ANISOU 161 CG2 ILE A 38 3159 3560 3750 522 1030 -939 C ATOM 162 CD1 ILE A 38 171.718 40.291 532.727 1.00 33.29 C ANISOU 162 CD1 ILE A 38 3664 4306 4678 452 835 -809 C ATOM 163 N ILE A 39 170.114 38.028 537.564 1.00 28.54 N ANISOU 163 N ILE A 39 3117 3899 3827 550 1344 -846 N ATOM 164 CA ILE A 39 169.463 38.202 538.862 1.00 49.32 C ANISOU 164 CA ILE A 39 5816 6551 6372 639 1515 -875 C ATOM 165 C ILE A 39 170.117 37.312 539.912 1.00 39.32 C ANISOU 165 C ILE A 39 4657 5339 4945 591 1554 -845 C ATOM 166 O ILE A 39 170.415 37.754 541.029 1.00 46.84 O ANISOU 166 O ILE A 39 5779 6290 5728 640 1602 -903 O ATOM 167 CB ILE A 39 167.953 37.926 538.748 1.00 43.63 C ANISOU 167 CB ILE A 39 4910 5873 5796 707 1663 -834 C ATOM 168 CG1 ILE A 39 167.280 38.994 537.883 1.00 38.94 C ANISOU 168 CG1 ILE A 39 4234 5225 5337 794 1622 -870 C ATOM 169 CG2 ILE A 39 167.315 37.879 540.126 1.00 39.74 C ANISOU 169 CG2 ILE A 39 4477 5420 5203 790 1874 -843 C ATOM 170 CD1 ILE A 39 165.801 38.763 537.674 1.00 32.72 C ANISOU 170 CD1 ILE A 39 3226 4489 4715 864 1741 -832 C ATOM 171 N GLY A 40 170.362 36.047 539.566 1.00 29.36 N ANISOU 171 N GLY A 40 3310 4121 3725 501 1527 -757 N ATOM 172 CA GLY A 40 170.954 35.132 540.531 1.00 38.20 C ANISOU 172 CA GLY A 40 4530 5285 4699 469 1563 -707 C ATOM 173 C GLY A 40 172.337 35.564 540.977 1.00 42.31 C ANISOU 173 C GLY A 40 5227 5796 5054 447 1424 -764 C ATOM 174 O GLY A 40 172.618 35.663 542.177 1.00 43.68 O ANISOU 174 O GLY A 40 5557 5996 5043 490 1469 -788 O ATOM 175 N ASN A 41 173.222 35.841 540.014 1.00 42.26 N ANISOU 175 N ASN A 41 5194 5755 5107 381 1253 -787 N ATOM 176 CA ASN A 41 174.593 36.192 540.375 1.00 34.27 C ANISOU 176 CA ASN A 41 4312 4740 3969 341 1110 -836 C ATOM 177 C ASN A 41 174.657 37.534 541.097 1.00 34.14 C ANISOU 177 C ASN A 41 4447 4677 3848 395 1105 -955 C ATOM 178 O ASN A 41 175.475 37.713 542.009 1.00 34.15 O ANISOU 178 O ASN A 41 4592 4697 3685 390 1040 -1007 O ATOM 179 CB ASN A 41 175.477 36.196 539.131 1.00 26.93 C ANISOU 179 CB ASN A 41 3300 3787 3145 255 956 -825 C ATOM 180 CG ASN A 41 175.701 34.804 538.582 1.00 36.75 C ANISOU 180 CG ASN A 41 4438 5073 4451 205 941 -728 C ATOM 181 OD1 ASN A 41 176.529 34.051 539.093 1.00 50.09 O ANISOU 181 OD1 ASN A 41 6173 6804 6054 184 897 -691 O ATOM 182 ND2 ASN A 41 174.957 34.450 537.542 1.00 42.80 N ANISOU 182 ND2 ASN A 41 5067 5826 5368 193 971 -692 N ATOM 183 N ILE A 42 173.801 38.485 540.714 1.00 33.78 N ANISOU 183 N ILE A 42 4376 4566 3894 454 1164 -1006 N ATOM 184 CA ILE A 42 173.751 39.757 541.429 1.00 30.91 C ANISOU 184 CA ILE A 42 4170 4135 3439 520 1178 -1129 C ATOM 185 C ILE A 42 173.303 39.538 542.869 1.00 69.01 C ANISOU 185 C ILE A 42 9121 9018 8082 606 1318 -1155 C ATOM 186 O ILE A 42 173.865 40.121 543.806 1.00 71.29 O ANISOU 186 O ILE A 42 9595 9293 8199 625 1274 -1256 O ATOM 187 CB ILE A 42 172.839 40.756 540.693 1.00 31.14 C ANISOU 187 CB ILE A 42 4140 4075 3618 589 1225 -1163 C ATOM 188 CG1 ILE A 42 173.538 41.295 539.445 1.00 35.13 C ANISOU 188 CG1 ILE A 42 4599 4505 4245 506 1069 -1157 C ATOM 189 CG2 ILE A 42 172.443 41.901 541.611 1.00 44.03 C ANISOU 189 CG2 ILE A 42 5936 5635 5156 696 1302 -1288 C ATOM 190 CD1 ILE A 42 172.764 42.384 538.737 1.00 40.90 C ANISOU 190 CD1 ILE A 42 5303 5131 5105 583 1093 -1183 C ATOM 191 N LEU A 43 172.292 38.687 543.070 1.00 56.10 N ANISOU 191 N LEU A 43 7390 7448 6477 655 1489 -1065 N ATOM 192 CA LEU A 43 171.859 38.366 544.427 1.00 40.68 C ANISOU 192 CA LEU A 43 5556 5561 4341 736 1649 -1063 C ATOM 193 C LEU A 43 172.992 37.750 545.239 1.00 47.51 C ANISOU 193 C LEU A 43 6564 6487 5003 689 1551 -1046 C ATOM 194 O LEU A 43 173.173 38.083 546.418 1.00 52.13 O ANISOU 194 O LEU A 43 7342 7098 5365 753 1582 -1116 O ATOM 195 CB LEU A 43 170.654 37.427 544.387 1.00 35.27 C ANISOU 195 CB LEU A 43 4712 4934 3756 765 1849 -943 C ATOM 196 CG LEU A 43 169.311 38.062 544.026 1.00 41.86 C ANISOU 196 CG LEU A 43 5419 5739 4746 857 1995 -968 C ATOM 197 CD1 LEU A 43 168.216 37.009 543.960 1.00 45.11 C ANISOU 197 CD1 LEU A 43 5643 6218 5281 853 2174 -842 C ATOM 198 CD2 LEU A 43 168.956 39.147 545.028 1.00 46.96 C ANISOU 198 CD2 LEU A 43 6237 6361 5245 992 2107 -1089 C ATOM 199 N VAL A 44 173.771 36.855 544.626 1.00 46.96 N ANISOU 199 N VAL A 44 6404 6441 4996 589 1425 -958 N ATOM 200 CA VAL A 44 174.887 36.235 545.339 1.00 40.37 C ANISOU 200 CA VAL A 44 5685 5667 3985 557 1314 -930 C ATOM 201 C VAL A 44 175.918 37.286 545.736 1.00 37.09 C ANISOU 201 C VAL A 44 5420 5226 3445 540 1137 -1074 C ATOM 202 O VAL A 44 176.325 37.375 546.902 1.00 35.88 O ANISOU 202 O VAL A 44 5448 5122 3063 584 1111 -1124 O ATOM 203 CB VAL A 44 175.518 35.119 544.487 1.00 34.55 C ANISOU 203 CB VAL A 44 4808 4948 3371 466 1217 -816 C ATOM 204 CG1 VAL A 44 176.773 34.586 545.160 1.00 32.36 C ANISOU 204 CG1 VAL A 44 4636 4731 2927 447 1075 -792 C ATOM 205 CG2 VAL A 44 174.517 33.997 544.258 1.00 32.70 C ANISOU 205 CG2 VAL A 44 4451 4730 3246 471 1387 -683 C ATOM 206 N MET A 45 176.351 38.103 544.771 1.00 39.33 N ANISOU 206 N MET A 45 5637 5431 3878 472 1011 -1142 N ATOM 207 CA MET A 45 177.397 39.088 545.040 1.00 39.89 C ANISOU 207 CA MET A 45 5826 5459 3872 425 832 -1275 C ATOM 208 C MET A 45 176.960 40.088 546.105 1.00 48.85 C ANISOU 208 C MET A 45 7163 6556 4842 514 895 -1418 C ATOM 209 O MET A 45 177.687 40.338 547.075 1.00 51.76 O ANISOU 209 O MET A 45 7698 6956 5012 514 790 -1509 O ATOM 210 CB MET A 45 177.775 39.813 543.748 1.00 33.28 C ANISOU 210 CB MET A 45 4875 4525 3243 336 727 -1302 C ATOM 211 CG MET A 45 178.401 38.920 542.692 1.00 32.95 C ANISOU 211 CG MET A 45 4658 4524 3339 247 647 -1185 C ATOM 212 SD MET A 45 178.528 39.744 541.095 0.57 30.48 S ANISOU 212 SD MET A 45 4218 4103 3258 170 587 -1189 S ATOM 213 CE MET A 45 179.389 41.245 541.559 1.00 30.92 C ANISOU 213 CE MET A 45 4426 4061 3262 112 450 -1349 C ATOM 214 N VAL A 46 175.771 40.674 545.936 1.00 50.98 N ANISOU 214 N VAL A 46 7421 6761 5188 600 1062 -1447 N ATOM 215 CA VAL A 46 175.279 41.645 546.910 1.00 53.10 C ANISOU 215 CA VAL A 46 7885 6983 5309 706 1146 -1592 C ATOM 216 C VAL A 46 175.134 40.997 548.280 1.00 55.48 C ANISOU 216 C VAL A 46 8336 7402 5341 789 1244 -1579 C ATOM 217 O VAL A 46 175.483 41.596 549.306 1.00 46.22 O ANISOU 217 O VAL A 46 7383 6228 3950 833 1198 -1716 O ATOM 218 CB VAL A 46 173.954 42.264 546.427 1.00 50.07 C ANISOU 218 CB VAL A 46 7427 6519 5077 805 1327 -1603 C ATOM 219 CG1 VAL A 46 173.371 43.178 547.494 1.00 53.08 C ANISOU 219 CG1 VAL A 46 8014 6858 5298 942 1448 -1752 C ATOM 220 CG2 VAL A 46 174.171 43.031 545.133 1.00 37.48 C ANISOU 220 CG2 VAL A 46 5727 4799 3714 735 1213 -1619 C ATOM 221 N SER A 47 174.635 39.758 548.320 1.00 58.46 N ANISOU 221 N SER A 47 8611 7878 5725 808 1376 -1413 N ATOM 222 CA SER A 47 174.504 39.056 549.593 1.00 48.92 C ANISOU 222 CA SER A 47 7550 6781 4258 886 1483 -1366 C ATOM 223 C SER A 47 175.854 38.893 550.279 1.00 52.00 C ANISOU 223 C SER A 47 8092 7229 4438 839 1261 -1408 C ATOM 224 O SER A 47 175.961 39.051 551.501 1.00 57.24 O ANISOU 224 O SER A 47 8976 7950 4821 919 1277 -1478 O ATOM 225 CB SER A 47 173.846 37.695 549.377 1.00 40.70 C ANISOU 225 CB SER A 47 6354 5808 3300 885 1645 -1163 C ATOM 226 OG SER A 47 172.484 37.849 549.028 1.00 48.16 O ANISOU 226 OG SER A 47 7175 6725 4399 947 1870 -1135 O ATOM 227 N ILE A 48 176.899 38.579 549.510 1.00 56.04 N ANISOU 227 N ILE A 48 8485 7736 5074 717 1049 -1369 N ATOM 228 CA ILE A 48 178.222 38.425 550.105 1.00 52.68 C ANISOU 228 CA ILE A 48 8165 7374 4476 672 819 -1407 C ATOM 229 C ILE A 48 178.770 39.770 550.570 1.00 56.27 C ANISOU 229 C ILE A 48 8784 7768 4827 655 667 -1627 C ATOM 230 O ILE A 48 179.472 39.843 551.587 1.00 66.69 O ANISOU 230 O ILE A 48 10281 9156 5902 674 534 -1706 O ATOM 231 CB ILE A 48 179.170 37.732 549.109 1.00 42.03 C ANISOU 231 CB ILE A 48 6620 6038 3313 555 653 -1305 C ATOM 232 CG1 ILE A 48 178.675 36.316 548.810 1.00 43.83 C ANISOU 232 CG1 ILE A 48 6724 6317 3612 577 794 -1100 C ATOM 233 CG2 ILE A 48 180.592 37.690 549.648 1.00 40.15 C ANISOU 233 CG2 ILE A 48 6455 5868 2932 507 394 -1355 C ATOM 234 CD1 ILE A 48 179.493 35.587 547.772 1.00 50.53 C ANISOU 234 CD1 ILE A 48 7383 7168 4648 482 661 -1005 C ATOM 235 N LYS A 49 178.450 40.854 549.861 1.00 51.15 N ANISOU 235 N LYS A 49 8093 6985 4357 623 680 -1732 N ATOM 236 CA LYS A 49 179.024 42.150 550.212 1.00 47.24 C ANISOU 236 CA LYS A 49 7753 6398 3799 586 526 -1945 C ATOM 237 C LYS A 49 178.314 42.817 551.386 1.00 55.44 C ANISOU 237 C LYS A 49 9043 7421 4599 723 651 -2091 C ATOM 238 O LYS A 49 178.945 43.586 552.120 1.00 55.81 O ANISOU 238 O LYS A 49 9283 7440 4484 708 498 -2273 O ATOM 239 CB LYS A 49 179.011 43.081 548.999 1.00 51.44 C ANISOU 239 CB LYS A 49 8162 6769 4614 500 489 -1992 C ATOM 240 CG LYS A 49 180.167 42.852 548.041 1.00 61.07 C ANISOU 240 CG LYS A 49 9204 7988 6012 337 289 -1930 C ATOM 241 CD LYS A 49 181.500 42.970 548.766 1.00 65.52 C ANISOU 241 CD LYS A 49 9860 8607 6429 254 39 -2030 C ATOM 242 CE LYS A 49 182.666 42.645 547.847 1.00 75.93 C ANISOU 242 CE LYS A 49 10973 9947 7930 102 -140 -1954 C ATOM 243 NZ LYS A 49 183.963 42.635 548.580 1.00 88.21 N ANISOU 243 NZ LYS A 49 12581 11583 9353 27 -390 -2037 N ATOM 244 N VAL A 50 177.021 42.552 551.586 1.00 65.48 N ANISOU 244 N VAL A 50 10317 8713 5849 857 927 -2023 N ATOM 245 CA VAL A 50 176.260 43.248 552.620 1.00 65.08 C ANISOU 245 CA VAL A 50 10441 8648 5638 976 1068 -2138 C ATOM 246 C VAL A 50 176.179 42.468 553.923 1.00 67.61 C ANISOU 246 C VAL A 50 10870 9129 5691 1038 1132 -2064 C ATOM 247 O VAL A 50 175.640 42.989 554.909 1.00 70.03 O ANISOU 247 O VAL A 50 11294 9447 5867 1112 1227 -2141 O ATOM 248 CB VAL A 50 174.840 43.598 552.132 1.00 61.07 C ANISOU 248 CB VAL A 50 9808 8070 5324 1067 1321 -2099 C ATOM 249 CG1 VAL A 50 174.903 44.356 550.815 1.00 64.09 C ANISOU 249 CG1 VAL A 50 10095 8287 5967 1016 1260 -2153 C ATOM 250 CG2 VAL A 50 173.991 42.342 552.007 1.00 51.73 C ANISOU 250 CG2 VAL A 50 8472 7002 4181 1117 1535 -1884 C ATOM 251 N ASN A 51 176.701 41.244 553.967 1.00 68.35 N ANISOU 251 N ASN A 51 10934 9342 5693 1017 1083 -1913 N ATOM 252 CA ASN A 51 176.627 40.404 555.158 1.00 69.09 C ANISOU 252 CA ASN A 51 11134 9579 5538 1080 1148 -1809 C ATOM 253 C ASN A 51 178.027 39.935 555.528 1.00 72.50 C ANISOU 253 C ASN A 51 11654 10098 5796 1022 871 -1809 C ATOM 254 O ASN A 51 178.693 39.275 554.725 1.00 64.36 O ANISOU 254 O ASN A 51 10515 9085 4853 969 754 -1727 O ATOM 255 CB ASN A 51 175.701 39.205 554.930 1.00 63.78 C ANISOU 255 CB ASN A 51 10326 8969 4940 1129 1399 -1578 C ATOM 256 CG ASN A 51 175.476 38.393 556.192 1.00 66.60 C ANISOU 256 CG ASN A 51 10801 9451 5052 1197 1502 -1457 C ATOM 257 OD1 ASN A 51 175.755 38.852 557.300 1.00 70.88 O ANISOU 257 OD1 ASN A 51 11531 10038 5364 1233 1432 -1557 O ATOM 258 ND2 ASN A 51 174.961 37.181 556.030 1.00 65.02 N ANISOU 258 ND2 ASN A 51 10496 9301 4907 1211 1670 -1238 N ATOM 259 N ARG A 52 178.465 40.267 556.747 1.00 73.54 N ANISOU 259 N ARG A 52 11971 10291 5682 1040 761 -1902 N ATOM 260 CA ARG A 52 179.787 39.843 557.200 1.00 69.21 C ANISOU 260 CA ARG A 52 11492 9838 4966 992 479 -1901 C ATOM 261 C ARG A 52 179.847 38.341 557.445 1.00 65.42 C ANISOU 261 C ARG A 52 10994 9487 4376 1051 537 -1660 C ATOM 262 O ARG A 52 180.906 37.728 557.266 1.00 65.00 O ANISOU 262 O ARG A 52 10905 9500 4291 1014 316 -1602 O ATOM 263 CB ARG A 52 180.186 40.594 558.472 1.00 80.68 C ANISOU 263 CB ARG A 52 13146 11326 6182 999 350 -2063 C ATOM 264 CG ARG A 52 180.405 42.090 558.296 1.00 90.57 C ANISOU 264 CG ARG A 52 14434 12442 7536 919 235 -2314 C ATOM 265 CD ARG A 52 179.116 42.872 558.492 1.00 98.98 C ANISOU 265 CD ARG A 52 15547 13417 8643 1003 501 -2389 C ATOM 266 NE ARG A 52 179.373 44.235 558.945 1.00103.18 N ANISOU 266 NE ARG A 52 16206 13854 9145 962 387 -2635 N ATOM 267 CZ ARG A 52 179.515 44.579 560.221 1.00107.05 C ANISOU 267 CZ ARG A 52 16888 14408 9379 1002 341 -2743 C ATOM 268 NH1 ARG A 52 179.427 43.657 561.171 1.00101.58 N ANISOU 268 NH1 ARG A 52 16286 13877 8431 1087 398 -2615 N ATOM 269 NH2 ARG A 52 179.748 45.842 560.550 1.00115.48 N ANISOU 269 NH2 ARG A 52 18064 15372 10442 956 239 -2976 N ATOM 270 N HIS A 53 178.731 37.734 557.858 1.00 56.50 N ANISOU 270 N HIS A 53 9877 8388 3202 1142 828 -1512 N ATOM 271 CA HIS A 53 178.702 36.291 558.063 1.00 56.33 C ANISOU 271 CA HIS A 53 9840 8459 3104 1190 911 -1266 C ATOM 272 C HIS A 53 178.933 35.524 556.768 1.00 61.05 C ANISOU 272 C HIS A 53 10245 9027 3922 1144 899 -1143 C ATOM 273 O HIS A 53 179.343 34.359 556.814 1.00 52.84 O ANISOU 273 O HIS A 53 9195 8056 2826 1168 869 -962 O ATOM 274 CB HIS A 53 177.370 35.873 558.688 1.00 58.36 C ANISOU 274 CB HIS A 53 10123 8733 3318 1272 1244 -1138 C ATOM 275 CG HIS A 53 177.170 36.382 560.082 1.00 78.49 C ANISOU 275 CG HIS A 53 12879 11342 5603 1340 1271 -1224 C ATOM 276 ND1 HIS A 53 177.630 35.709 561.193 1.00 83.37 N ANISOU 276 ND1 HIS A 53 13661 12073 5943 1395 1207 -1127 N ATOM 277 CD2 HIS A 53 176.559 37.498 560.545 1.00 83.40 C ANISOU 277 CD2 HIS A 53 13574 11925 6190 1371 1357 -1398 C ATOM 278 CE1 HIS A 53 177.312 36.388 562.281 1.00 87.58 C ANISOU 278 CE1 HIS A 53 14364 12641 6272 1453 1254 -1243 C ATOM 279 NE2 HIS A 53 176.662 37.478 561.915 1.00 87.70 N ANISOU 279 NE2 HIS A 53 14328 12565 6431 1440 1348 -1411 N ATOM 280 N LEU A 54 178.679 36.150 555.618 1.00 60.38 N ANISOU 280 N LEU A 54 10016 8838 4086 1086 922 -1236 N ATOM 281 CA LEU A 54 178.947 35.557 554.315 1.00 63.52 C ANISOU 281 CA LEU A 54 10133 9180 4821 972 867 -1118 C ATOM 282 C LEU A 54 180.267 36.040 553.723 1.00 64.16 C ANISOU 282 C LEU A 54 10121 9238 5018 854 545 -1226 C ATOM 283 O LEU A 54 180.430 36.055 552.499 1.00 77.50 O ANISOU 283 O LEU A 54 11587 10853 7007 751 503 -1203 O ATOM 284 CB LEU A 54 177.797 35.852 553.352 1.00 72.73 C ANISOU 284 CB LEU A 54 11124 10241 6270 946 1086 -1108 C ATOM 285 CG LEU A 54 176.476 35.130 553.615 1.00 75.18 C ANISOU 285 CG LEU A 54 11420 10569 6575 1026 1415 -956 C ATOM 286 CD1 LEU A 54 175.385 35.656 552.697 1.00 80.16 C ANISOU 286 CD1 LEU A 54 11873 11104 7481 1007 1588 -989 C ATOM 287 CD2 LEU A 54 176.651 33.630 553.438 1.00 73.19 C ANISOU 287 CD2 LEU A 54 11074 10356 6380 1000 1442 -725 C ATOM 288 N GLN A 55 181.214 36.439 554.569 1.00 64.76 N ANISOU 288 N GLN A 55 10362 9383 4860 865 316 -1344 N ATOM 289 CA GLN A 55 182.518 36.938 554.132 1.00 66.57 C ANISOU 289 CA GLN A 55 10498 9602 5192 745 2 -1455 C ATOM 290 C GLN A 55 183.590 35.971 554.624 1.00 65.02 C ANISOU 290 C GLN A 55 10310 9540 4857 767 -200 -1345 C ATOM 291 O GLN A 55 184.272 36.222 555.620 1.00 63.92 O ANISOU 291 O GLN A 55 10342 9489 4453 805 -394 -1441 O ATOM 292 CB GLN A 55 182.757 38.364 554.638 1.00 66.30 C ANISOU 292 CB GLN A 55 10628 9519 5042 718 -127 -1717 C ATOM 293 CG GLN A 55 181.843 39.401 554.008 1.00 58.71 C ANISOU 293 CG GLN A 55 9640 8404 4265 694 40 -1829 C ATOM 294 CD GLN A 55 182.129 40.805 554.499 1.00 67.79 C ANISOU 294 CD GLN A 55 10967 9477 5315 665 -94 -2094 C ATOM 295 OE1 GLN A 55 182.944 41.007 555.399 1.00 77.09 O ANISOU 295 OE1 GLN A 55 12269 10724 6299 644 -301 -2187 O ATOM 296 NE2 GLN A 55 181.458 41.787 553.908 1.00 71.51 N ANISOU 296 NE2 GLN A 55 11416 9792 5963 644 22 -2196 N ATOM 297 N THR A 56 183.732 34.855 553.915 1.00 59.49 N ANISOU 297 N THR A 56 9422 8848 4334 753 -163 -1148 N ATOM 298 CA THR A 56 184.755 33.856 554.188 1.00 50.33 C ANISOU 298 CA THR A 56 8228 7794 3099 784 -346 -1021 C ATOM 299 C THR A 56 185.531 33.588 552.904 1.00 65.14 C ANISOU 299 C THR A 56 9818 9631 5302 671 -464 -977 C ATOM 300 O THR A 56 185.238 34.154 551.847 1.00 76.52 O ANISOU 300 O THR A 56 11109 10968 6999 572 -397 -1035 O ATOM 301 CB THR A 56 184.140 32.563 554.739 1.00 55.44 C ANISOU 301 CB THR A 56 8969 8488 3606 911 -154 -795 C ATOM 302 OG1 THR A 56 183.175 32.056 553.809 1.00 62.19 O ANISOU 302 OG1 THR A 56 9674 9242 4714 880 102 -676 O ATOM 303 CG2 THR A 56 183.464 32.819 556.078 1.00 51.49 C ANISOU 303 CG2 THR A 56 8767 8049 2750 1031 -33 -831 C ATOM 304 N VAL A 57 186.532 32.711 553.001 1.00 67.04 N ANISOU 304 N VAL A 57 9987 9959 5524 701 -637 -867 N ATOM 305 CA VAL A 57 187.351 32.384 551.835 1.00 69.40 C ANISOU 305 CA VAL A 57 10017 10237 6116 614 -743 -822 C ATOM 306 C VAL A 57 186.502 31.709 550.764 1.00 67.79 C ANISOU 306 C VAL A 57 9678 9930 6150 599 -497 -691 C ATOM 307 O VAL A 57 186.550 32.075 549.580 1.00 73.76 O ANISOU 307 O VAL A 57 10249 10610 7167 495 -479 -732 O ATOM 308 CB VAL A 57 188.543 31.503 552.252 1.00 67.50 C ANISOU 308 CB VAL A 57 9734 10117 5795 682 -964 -721 C ATOM 309 CG1 VAL A 57 189.449 31.238 551.064 1.00 69.49 C ANISOU 309 CG1 VAL A 57 9700 10355 6347 601 -1067 -690 C ATOM 310 CG2 VAL A 57 189.316 32.160 553.385 1.00 67.68 C ANISOU 310 CG2 VAL A 57 9901 10256 5560 701 -1225 -858 C ATOM 311 N ASN A 58 185.707 30.713 551.169 1.00 65.09 N ANISOU 311 N ASN A 58 9433 9582 5716 699 -306 -529 N ATOM 312 CA ASN A 58 184.814 30.039 550.232 1.00 68.97 C ANISOU 312 CA ASN A 58 9807 9972 6428 677 -77 -415 C ATOM 313 C ASN A 58 183.894 31.033 549.538 1.00 79.02 C ANISOU 313 C ASN A 58 11026 11152 7846 594 62 -533 C ATOM 314 O ASN A 58 183.680 30.947 548.324 1.00 97.38 O ANISOU 314 O ASN A 58 13172 13402 10427 521 122 -519 O ATOM 315 CB ASN A 58 183.993 28.973 550.960 1.00 70.61 C ANISOU 315 CB ASN A 58 10155 10178 6496 783 121 -238 C ATOM 316 CG ASN A 58 184.855 27.891 551.578 1.00 65.24 C ANISOU 316 CG ASN A 58 9533 9569 5685 882 -5 -90 C ATOM 317 OD1 ASN A 58 185.930 27.572 551.072 1.00 76.28 O ANISOU 317 OD1 ASN A 58 10792 10992 7200 869 -191 -77 O ATOM 318 ND2 ASN A 58 184.384 27.318 552.680 1.00 60.94 N ANISOU 318 ND2 ASN A 58 9197 9060 4897 991 105 30 N ATOM 319 N ASN A 59 183.350 31.993 550.288 1.00 72.24 N ANISOU 319 N ASN A 59 10329 10300 6821 615 111 -655 N ATOM 320 CA ASN A 59 182.464 32.983 549.691 1.00 65.11 C ANISOU 320 CA ASN A 59 9385 9303 6052 559 240 -766 C ATOM 321 C ASN A 59 183.221 34.023 548.874 1.00 67.55 C ANISOU 321 C ASN A 59 9576 9568 6523 445 65 -911 C ATOM 322 O ASN A 59 182.602 34.730 548.072 1.00 77.30 O ANISOU 322 O ASN A 59 10736 10710 7926 391 156 -973 O ATOM 323 CB ASN A 59 181.633 33.663 550.778 1.00 57.84 C ANISOU 323 CB ASN A 59 8682 8394 4900 638 364 -852 C ATOM 324 CG ASN A 59 180.703 32.696 551.485 1.00 55.46 C ANISOU 324 CG ASN A 59 8482 8125 4465 741 595 -694 C ATOM 325 OD1 ASN A 59 180.254 31.711 550.900 1.00 47.68 O ANISOU 325 OD1 ASN A 59 7373 7105 3639 729 724 -539 O ATOM 326 ND2 ASN A 59 180.413 32.972 552.750 1.00 64.79 N ANISOU 326 ND2 ASN A 59 9896 9369 5351 838 652 -734 N ATOM 327 N TYR A 60 184.537 34.139 549.060 1.00 58.74 N ANISOU 327 N TYR A 60 8438 8516 5366 406 -183 -959 N ATOM 328 CA TYR A 60 185.333 34.971 548.163 1.00 56.85 C ANISOU 328 CA TYR A 60 8049 8231 5319 278 -333 -1063 C ATOM 329 C TYR A 60 185.525 34.281 546.818 1.00 48.45 C ANISOU 329 C TYR A 60 6756 7136 4515 228 -294 -949 C ATOM 330 O TYR A 60 185.346 34.897 545.758 1.00 46.79 O ANISOU 330 O TYR A 60 6432 6842 4503 144 -254 -992 O ATOM 331 CB TYR A 60 186.682 35.298 548.805 1.00 54.56 C ANISOU 331 CB TYR A 60 7782 8029 4919 243 -611 -1152 C ATOM 332 CG TYR A 60 186.722 36.646 549.490 1.00 68.24 C ANISOU 332 CG TYR A 60 9672 9728 6527 202 -705 -1357 C ATOM 333 CD1 TYR A 60 185.993 36.880 550.649 1.00 71.25 C ANISOU 333 CD1 TYR A 60 10301 10127 6644 303 -627 -1418 C ATOM 334 CD2 TYR A 60 187.492 37.683 548.981 1.00 78.83 C ANISOU 334 CD2 TYR A 60 10921 11013 8016 60 -864 -1493 C ATOM 335 CE1 TYR A 60 186.026 38.109 551.278 1.00 80.82 C ANISOU 335 CE1 TYR A 60 11676 11297 7736 273 -713 -1624 C ATOM 336 CE2 TYR A 60 187.532 38.916 549.604 1.00 89.37 C ANISOU 336 CE2 TYR A 60 12412 12293 9251 14 -955 -1692 C ATOM 337 CZ TYR A 60 186.797 39.123 550.752 1.00 95.36 C ANISOU 337 CZ TYR A 60 13427 13066 9740 125 -884 -1765 C ATOM 338 OH TYR A 60 186.834 40.349 551.377 1.00107.77 O ANISOU 338 OH TYR A 60 15172 14572 11204 88 -974 -1981 O ATOM 339 N PHE A 61 185.883 32.994 546.844 1.00 41.85 N ANISOU 339 N PHE A 61 5866 6363 3673 288 -303 -803 N ATOM 340 CA PHE A 61 185.977 32.229 545.604 1.00 40.90 C ANISOU 340 CA PHE A 61 5553 6206 3780 259 -246 -700 C ATOM 341 C PHE A 61 184.637 32.209 544.876 1.00 47.32 C ANISOU 341 C PHE A 61 6343 6921 4714 250 -22 -671 C ATOM 342 O PHE A 61 184.566 32.461 543.666 1.00 66.28 O ANISOU 342 O PHE A 61 8605 9265 7315 180 7 -686 O ATOM 343 CB PHE A 61 186.451 30.807 545.901 1.00 50.74 C ANISOU 343 CB PHE A 61 6783 7513 4981 348 -273 -549 C ATOM 344 CG PHE A 61 187.815 30.737 546.529 1.00 51.56 C ANISOU 344 CG PHE A 61 6877 7728 4987 371 -513 -563 C ATOM 345 CD1 PHE A 61 188.745 31.742 546.318 1.00 41.40 C ANISOU 345 CD1 PHE A 61 5502 6472 3757 274 -693 -694 C ATOM 346 CD2 PHE A 61 188.168 29.663 547.330 1.00 54.84 C ANISOU 346 CD2 PHE A 61 7364 8212 5259 490 -562 -439 C ATOM 347 CE1 PHE A 61 190.000 31.677 546.895 1.00 43.68 C ANISOU 347 CE1 PHE A 61 5753 6873 3972 288 -928 -712 C ATOM 348 CE2 PHE A 61 189.421 29.592 547.909 1.00 54.23 C ANISOU 348 CE2 PHE A 61 7264 8249 5093 524 -801 -450 C ATOM 349 CZ PHE A 61 190.338 30.601 547.692 1.00 49.22 C ANISOU 349 CZ PHE A 61 6519 7657 4525 420 -990 -592 C ATOM 350 N LEU A 62 183.557 31.920 545.607 1.00 44.35 N ANISOU 350 N LEU A 62 6098 6534 4217 324 139 -628 N ATOM 351 CA LEU A 62 182.226 31.947 545.011 1.00 46.53 C ANISOU 351 CA LEU A 62 6337 6730 4613 317 346 -608 C ATOM 352 C LEU A 62 181.839 33.351 544.571 1.00 48.30 C ANISOU 352 C LEU A 62 6552 6893 4907 263 353 -746 C ATOM 353 O LEU A 62 181.021 33.511 543.659 1.00 56.56 O ANISOU 353 O LEU A 62 7504 7871 6114 237 464 -740 O ATOM 354 CB LEU A 62 181.196 31.397 545.999 1.00 41.22 C ANISOU 354 CB LEU A 62 5800 6070 3794 404 526 -531 C ATOM 355 CG LEU A 62 181.376 29.942 546.436 1.00 35.56 C ANISOU 355 CG LEU A 62 5110 5383 3017 463 558 -365 C ATOM 356 CD1 LEU A 62 180.302 29.547 547.436 1.00 35.18 C ANISOU 356 CD1 LEU A 62 5204 5341 2821 538 762 -286 C ATOM 357 CD2 LEU A 62 181.370 29.009 545.234 1.00 43.07 C ANISOU 357 CD2 LEU A 62 5889 6274 4203 419 588 -278 C ATOM 358 N PHE A 63 182.406 34.379 545.207 1.00 37.53 N ANISOU 358 N PHE A 63 5291 5544 3425 247 229 -873 N ATOM 359 CA PHE A 63 182.161 35.746 544.761 1.00 39.87 C ANISOU 359 CA PHE A 63 5590 5756 3803 192 222 -1005 C ATOM 360 C PHE A 63 182.766 35.981 543.384 1.00 47.46 C ANISOU 360 C PHE A 63 6374 6673 4987 90 144 -1001 C ATOM 361 O PHE A 63 182.103 36.510 542.484 1.00 58.97 O ANISOU 361 O PHE A 63 7769 8049 6588 65 227 -1014 O ATOM 362 CB PHE A 63 182.721 36.742 545.778 1.00 35.19 C ANISOU 362 CB PHE A 63 5158 5174 3038 186 91 -1153 C ATOM 363 CG PHE A 63 182.428 38.180 545.448 1.00 37.55 C ANISOU 363 CG PHE A 63 5495 5360 3414 138 93 -1294 C ATOM 364 CD1 PHE A 63 181.278 38.791 545.920 1.00 45.13 C ANISOU 364 CD1 PHE A 63 6582 6262 4304 218 247 -1359 C ATOM 365 CD2 PHE A 63 183.303 38.922 544.669 1.00 38.90 C ANISOU 365 CD2 PHE A 63 5573 5473 3733 17 -49 -1355 C ATOM 366 CE1 PHE A 63 181.005 40.112 545.619 1.00 62.13 C ANISOU 366 CE1 PHE A 63 8781 8292 6535 190 250 -1486 C ATOM 367 CE2 PHE A 63 183.035 40.243 544.365 1.00 46.34 C ANISOU 367 CE2 PHE A 63 6565 6287 4753 -27 -42 -1472 C ATOM 368 CZ PHE A 63 181.884 40.839 544.840 1.00 64.73 C ANISOU 368 CZ PHE A 63 9033 8549 7013 65 102 -1539 C ATOM 369 N SER A 64 184.031 35.591 543.200 1.00 45.09 N ANISOU 369 N SER A 64 5988 6432 4712 40 -13 -976 N ATOM 370 CA SER A 64 184.657 35.729 541.888 1.00 37.33 C ANISOU 370 CA SER A 64 4834 5421 3929 -50 -65 -958 C ATOM 371 C SER A 64 183.927 34.896 540.840 1.00 38.36 C ANISOU 371 C SER A 64 4856 5526 4194 -26 74 -852 C ATOM 372 O SER A 64 183.711 35.354 539.709 1.00 44.43 O ANISOU 372 O SER A 64 5538 6234 5108 -77 109 -858 O ATOM 373 CB SER A 64 186.129 35.327 541.965 1.00 41.76 C ANISOU 373 CB SER A 64 5305 6068 4492 -90 -241 -941 C ATOM 374 OG SER A 64 186.746 35.404 540.692 1.00 52.50 O ANISOU 374 OG SER A 64 6495 7413 6041 -169 -265 -915 O ATOM 375 N LEU A 65 183.535 33.671 541.202 1.00 40.36 N ANISOU 375 N LEU A 65 5121 5819 4394 49 149 -754 N ATOM 376 CA LEU A 65 182.775 32.834 540.278 1.00 36.89 C ANISOU 376 CA LEU A 65 4590 5346 4083 63 274 -669 C ATOM 377 C LEU A 65 181.466 33.507 539.880 1.00 40.11 C ANISOU 377 C LEU A 65 5006 5682 4554 65 402 -705 C ATOM 378 O LEU A 65 181.080 33.489 538.703 1.00 34.74 O ANISOU 378 O LEU A 65 4222 4961 4017 35 441 -688 O ATOM 379 CB LEU A 65 182.514 31.468 540.913 1.00 28.20 C ANISOU 379 CB LEU A 65 3526 4276 2912 136 341 -561 C ATOM 380 CG LEU A 65 182.031 30.341 539.999 1.00 40.50 C ANISOU 380 CG LEU A 65 4983 5795 4609 138 432 -472 C ATOM 381 CD1 LEU A 65 183.041 30.078 538.894 1.00 48.92 C ANISOU 381 CD1 LEU A 65 5921 6871 5794 99 337 -467 C ATOM 382 CD2 LEU A 65 181.777 29.078 540.807 1.00 41.71 C ANISOU 382 CD2 LEU A 65 5203 5956 4688 204 503 -362 C ATOM 383 N ALA A 66 180.778 34.121 540.847 1.00 43.00 N ANISOU 383 N ALA A 66 5497 6036 4806 109 465 -757 N ATOM 384 CA ALA A 66 179.548 34.844 540.545 1.00 36.44 C ANISOU 384 CA ALA A 66 4667 5141 4039 131 584 -797 C ATOM 385 C ALA A 66 179.812 36.058 539.666 1.00 44.36 C ANISOU 385 C ALA A 66 5635 6077 5144 73 513 -873 C ATOM 386 O ALA A 66 178.948 36.443 538.869 1.00 62.10 O ANISOU 386 O ALA A 66 7822 8268 7503 84 585 -872 O ATOM 387 CB ALA A 66 178.853 35.267 541.839 1.00 39.22 C ANISOU 387 CB ALA A 66 5169 5498 4233 206 676 -845 C ATOM 388 N ACYS A 67 180.988 36.676 539.796 0.45 45.81 N ANISOU 388 N ACYS A 67 5849 6260 5295 12 371 -933 N ATOM 389 N BCYS A 67 180.987 36.679 539.797 0.55 45.85 N ANISOU 389 N BCYS A 67 5855 6266 5300 12 371 -934 N ATOM 390 CA ACYS A 67 181.331 37.794 538.923 0.45 40.56 C ANISOU 390 CA ACYS A 67 5151 5519 4740 -59 311 -987 C ATOM 391 CA BCYS A 67 181.334 37.793 538.921 0.55 39.29 C ANISOU 391 CA BCYS A 67 4990 5358 4580 -59 310 -987 C ATOM 392 C ACYS A 67 181.524 37.326 537.486 0.45 46.11 C ANISOU 392 C ACYS A 67 5703 6225 5591 -101 311 -906 C ATOM 393 C BCYS A 67 181.519 37.322 537.485 0.55 46.26 C ANISOU 393 C BCYS A 67 5722 6244 5610 -101 311 -906 C ATOM 394 O ACYS A 67 181.020 37.955 536.547 0.45 41.27 O ANISOU 394 O ACYS A 67 5056 5545 5079 -110 347 -905 O ATOM 395 O BCYS A 67 181.012 37.946 536.544 0.55 41.26 O ANISOU 395 O BCYS A 67 5055 5544 5079 -110 348 -904 O ATOM 396 CB ACYS A 67 182.590 38.493 539.437 0.45 40.77 C ANISOU 396 CB ACYS A 67 5231 5546 4714 -136 157 -1069 C ATOM 397 CB BCYS A 67 182.599 38.487 539.427 0.55 40.16 C ANISOU 397 CB BCYS A 67 5153 5469 4638 -136 157 -1068 C ATOM 398 SG ACYS A 67 183.120 39.913 538.453 0.45 38.37 S ANISOU 398 SG ACYS A 67 4899 5125 4555 -246 91 -1124 S ATOM 399 SG BCYS A 67 182.412 39.329 541.011 0.55 43.90 S ANISOU 399 SG BCYS A 67 5836 5918 4926 -94 131 -1204 S ATOM 400 N ALA A 68 182.246 36.217 537.297 1.00 43.71 N ANISOU 400 N ALA A 68 5318 5998 5292 -115 271 -839 N ATOM 401 CA ALA A 68 182.444 35.680 535.954 1.00 37.06 C ANISOU 401 CA ALA A 68 4347 5164 4569 -142 279 -773 C ATOM 402 C ALA A 68 181.116 35.265 535.330 1.00 35.39 C ANISOU 402 C ALA A 68 4103 4926 4419 -92 392 -735 C ATOM 403 O ALA A 68 180.826 35.599 534.174 1.00 21.96 O ANISOU 403 O ALA A 68 2345 3191 2809 -108 405 -723 O ATOM 404 CB ALA A 68 183.415 34.499 536.003 1.00 24.03 C ANISOU 404 CB ALA A 68 2629 3595 2905 -141 227 -717 C ATOM 405 N ASP A 69 180.288 34.542 536.090 1.00 34.49 N ANISOU 405 N ASP A 69 4021 4828 4254 -32 473 -712 N ATOM 406 CA ASP A 69 178.975 34.154 535.584 1.00 38.95 C ANISOU 406 CA ASP A 69 4533 5370 4895 4 575 -681 C ATOM 407 C ASP A 69 178.110 35.370 535.280 1.00 44.26 C ANISOU 407 C ASP A 69 5221 5983 5612 26 610 -730 C ATOM 408 O ASP A 69 177.304 35.340 534.342 1.00 51.40 O ANISOU 408 O ASP A 69 6047 6870 6614 39 641 -711 O ATOM 409 CB ASP A 69 178.276 33.238 536.588 1.00 51.87 C ANISOU 409 CB ASP A 69 6202 7030 6477 52 672 -641 C ATOM 410 CG ASP A 69 179.017 31.932 536.801 1.00 71.26 C ANISOU 410 CG ASP A 69 8646 9524 8905 46 645 -574 C ATOM 411 OD1 ASP A 69 179.724 31.490 535.870 1.00 70.42 O ANISOU 411 OD1 ASP A 69 8467 9424 8866 13 580 -557 O ATOM 412 OD2 ASP A 69 178.892 31.347 537.897 1.00 75.64 O ANISOU 412 OD2 ASP A 69 9273 10100 9367 84 696 -535 O ATOM 413 N LEU A 70 178.263 36.447 536.055 1.00 42.23 N ANISOU 413 N LEU A 70 5068 5691 5285 37 596 -797 N ATOM 414 CA LEU A 70 177.531 37.675 535.764 1.00 48.02 C ANISOU 414 CA LEU A 70 5830 6347 6067 71 625 -845 C ATOM 415 C LEU A 70 177.986 38.287 534.445 1.00 59.69 C ANISOU 415 C LEU A 70 7260 7780 7637 20 553 -830 C ATOM 416 O LEU A 70 177.155 38.725 533.639 1.00 60.95 O ANISOU 416 O LEU A 70 7380 7899 7878 59 581 -815 O ATOM 417 CB LEU A 70 177.705 38.674 536.908 1.00 44.43 C ANISOU 417 CB LEU A 70 5522 5848 5512 92 620 -936 C ATOM 418 CG LEU A 70 177.054 40.045 536.709 1.00 47.30 C ANISOU 418 CG LEU A 70 5942 6104 5926 137 648 -996 C ATOM 419 CD1 LEU A 70 175.549 39.908 536.538 1.00 57.83 C ANISOU 419 CD1 LEU A 70 7210 7440 7323 238 773 -969 C ATOM 420 CD2 LEU A 70 177.384 40.973 537.867 1.00 40.23 C ANISOU 420 CD2 LEU A 70 5211 5153 4920 148 629 -1107 C ATOM 421 N ILE A 71 179.300 38.322 534.206 1.00 60.92 N ANISOU 421 N ILE A 71 7414 7949 7782 -62 462 -827 N ATOM 422 CA ILE A 71 179.804 38.852 532.941 1.00 50.71 C ANISOU 422 CA ILE A 71 6078 6621 6568 -116 415 -796 C ATOM 423 C ILE A 71 179.315 38.003 531.773 1.00 47.51 C ANISOU 423 C ILE A 71 5569 6261 6221 -93 441 -728 C ATOM 424 O ILE A 71 178.998 38.525 530.697 1.00 38.25 O ANISOU 424 O ILE A 71 4377 5052 5103 -85 437 -700 O ATOM 425 CB ILE A 71 181.341 38.947 532.972 1.00 43.18 C ANISOU 425 CB ILE A 71 5115 5689 5602 -214 328 -801 C ATOM 426 CG1 ILE A 71 181.792 39.911 534.071 1.00 42.20 C ANISOU 426 CG1 ILE A 71 5098 5508 5426 -249 278 -888 C ATOM 427 CG2 ILE A 71 181.878 39.401 531.624 1.00 38.33 C ANISOU 427 CG2 ILE A 71 4449 5048 5066 -272 310 -750 C ATOM 428 CD1 ILE A 71 183.294 40.065 534.169 1.00 49.05 C ANISOU 428 CD1 ILE A 71 5934 6401 6299 -358 176 -902 C ATOM 429 N ILE A 72 179.235 36.684 531.967 1.00 52.95 N ANISOU 429 N ILE A 72 6202 7022 6893 -80 462 -703 N ATOM 430 CA ILE A 72 178.701 35.816 530.921 1.00 41.60 C ANISOU 430 CA ILE A 72 4677 5619 5512 -62 478 -660 C ATOM 431 C ILE A 72 177.222 36.107 530.688 1.00 42.61 C ANISOU 431 C ILE A 72 4781 5717 5691 1 525 -665 C ATOM 432 O ILE A 72 176.744 36.093 529.547 1.00 49.95 O ANISOU 432 O ILE A 72 5656 6650 6671 15 505 -644 O ATOM 433 CB ILE A 72 178.941 34.337 531.278 1.00 31.47 C ANISOU 433 CB ILE A 72 3354 4392 4213 -65 493 -637 C ATOM 434 CG1 ILE A 72 180.435 34.018 531.254 1.00 26.43 C ANISOU 434 CG1 ILE A 72 2709 3791 3542 -110 435 -625 C ATOM 435 CG2 ILE A 72 178.191 33.419 530.325 1.00 23.86 C ANISOU 435 CG2 ILE A 72 2312 3442 3313 -51 511 -616 C ATOM 436 CD1 ILE A 72 181.078 34.226 529.902 1.00 28.84 C ANISOU 436 CD1 ILE A 72 2967 4107 3883 -142 403 -606 C ATOM 437 N GLY A 73 176.479 36.388 531.759 1.00 40.11 N ANISOU 437 N GLY A 73 4501 5381 5358 47 588 -694 N ATOM 438 CA GLY A 73 175.054 36.634 531.609 1.00 48.51 C ANISOU 438 CA GLY A 73 5514 6429 6488 116 643 -697 C ATOM 439 C GLY A 73 174.745 37.960 530.938 1.00 39.66 C ANISOU 439 C GLY A 73 4421 5244 5405 158 612 -706 C ATOM 440 O GLY A 73 173.780 38.068 530.177 1.00 28.37 O ANISOU 440 O GLY A 73 2917 3816 4047 211 608 -687 O ATOM 441 N VAL A 74 175.557 38.983 531.204 1.00 39.34 N ANISOU 441 N VAL A 74 4486 5138 5322 134 582 -731 N ATOM 442 CA VAL A 74 175.265 40.313 530.676 1.00 33.46 C ANISOU 442 CA VAL A 74 3793 4302 4619 178 564 -733 C ATOM 443 C VAL A 74 175.723 40.440 529.228 1.00 37.17 C ANISOU 443 C VAL A 74 4237 4771 5116 142 495 -669 C ATOM 444 O VAL A 74 174.960 40.870 528.355 1.00 39.09 O ANISOU 444 O VAL A 74 4454 4992 5406 208 479 -634 O ATOM 445 CB VAL A 74 175.905 41.395 531.565 1.00 28.96 C ANISOU 445 CB VAL A 74 3360 3639 4006 156 562 -795 C ATOM 446 CG1 VAL A 74 175.703 42.772 530.951 1.00 25.07 C ANISOU 446 CG1 VAL A 74 2936 3021 3570 193 543 -786 C ATOM 447 CG2 VAL A 74 175.321 41.346 532.967 1.00 24.90 C ANISOU 447 CG2 VAL A 74 2892 3129 3440 216 639 -863 C ATOM 448 N PHE A 75 176.971 40.068 528.946 1.00 39.65 N ANISOU 448 N PHE A 75 4555 5116 5393 48 457 -651 N ATOM 449 CA PHE A 75 177.582 40.321 527.646 1.00 38.43 C ANISOU 449 CA PHE A 75 4399 4958 5245 9 415 -588 C ATOM 450 C PHE A 75 177.484 39.137 526.691 1.00 41.03 C ANISOU 450 C PHE A 75 4638 5388 5563 12 397 -554 C ATOM 451 O PHE A 75 177.034 39.298 525.553 1.00 50.99 O ANISOU 451 O PHE A 75 5887 6657 6830 52 370 -511 O ATOM 452 CB PHE A 75 179.054 40.714 527.828 1.00 39.38 C ANISOU 452 CB PHE A 75 4565 5054 5346 -97 395 -587 C ATOM 453 CG PHE A 75 179.252 42.019 528.549 1.00 46.21 C ANISOU 453 CG PHE A 75 5534 5795 6229 -119 393 -628 C ATOM 454 CD1 PHE A 75 179.315 42.061 529.932 1.00 46.91 C ANISOU 454 CD1 PHE A 75 5668 5870 6286 -125 397 -712 C ATOM 455 CD2 PHE A 75 179.381 43.203 527.841 1.00 46.09 C ANISOU 455 CD2 PHE A 75 5588 5670 6255 -133 387 -584 C ATOM 456 CE1 PHE A 75 179.499 43.261 530.597 1.00 41.95 C ANISOU 456 CE1 PHE A 75 5153 5120 5668 -146 386 -771 C ATOM 457 CE2 PHE A 75 179.565 44.405 528.499 1.00 46.25 C ANISOU 457 CE2 PHE A 75 5717 5550 6304 -159 383 -631 C ATOM 458 CZ PHE A 75 179.624 44.434 529.879 1.00 44.31 C ANISOU 458 CZ PHE A 75 5516 5291 6028 -167 379 -736 C ATOM 459 N SER A 76 177.897 37.947 527.131 1.00 38.75 N ANISOU 459 N SER A 76 4299 5171 5254 -24 407 -576 N ATOM 460 CA SER A 76 178.070 36.831 526.205 1.00 40.74 C ANISOU 460 CA SER A 76 4487 5499 5493 -33 389 -556 C ATOM 461 C SER A 76 176.732 36.320 525.680 1.00 42.20 C ANISOU 461 C SER A 76 4611 5709 5714 28 375 -564 C ATOM 462 O SER A 76 176.565 36.122 524.470 1.00 48.56 O ANISOU 462 O SER A 76 5399 6547 6505 45 333 -546 O ATOM 463 CB SER A 76 178.847 35.708 526.889 1.00 40.13 C ANISOU 463 CB SER A 76 4380 5470 5398 -74 403 -575 C ATOM 464 OG SER A 76 180.091 36.182 527.371 1.00 24.97 O ANISOU 464 OG SER A 76 2494 3542 3454 -131 396 -572 O ATOM 465 N MET A 77 175.768 36.097 526.576 1.00 47.11 N ANISOU 465 N MET A 77 5197 6323 6381 60 410 -594 N ATOM 466 CA MET A 77 174.492 35.519 526.162 1.00 47.02 C ANISOU 466 CA MET A 77 5095 6342 6430 101 395 -606 C ATOM 467 C MET A 77 173.761 36.422 525.177 1.00 39.78 C ANISOU 467 C MET A 77 4170 5413 5530 168 338 -584 C ATOM 468 O MET A 77 173.221 35.945 524.171 1.00 52.09 O ANISOU 468 O MET A 77 5672 7019 7101 185 273 -585 O ATOM 469 CB MET A 77 173.615 35.248 527.384 1.00 51.94 C ANISOU 469 CB MET A 77 5672 6957 7107 121 470 -629 C ATOM 470 CG MET A 77 174.101 34.109 528.262 1.00 48.12 C ANISOU 470 CG MET A 77 5189 6489 6604 68 521 -635 C ATOM 471 SD MET A 77 172.952 33.752 529.603 0.82 50.16 S ANISOU 471 SD MET A 77 5397 6745 6916 94 634 -641 S ATOM 472 CE MET A 77 173.731 32.322 530.345 1.00 56.22 C ANISOU 472 CE MET A 77 6192 7523 7645 31 674 -621 C ATOM 473 N ASN A 78 173.733 37.729 525.445 1.00 36.81 N ANISOU 473 N ASN A 78 3862 4971 5154 211 353 -565 N ATOM 474 CA ASN A 78 172.992 38.644 524.582 1.00 44.08 C ANISOU 474 CA ASN A 78 4785 5868 6096 296 299 -529 C ATOM 475 C ASN A 78 173.654 38.782 523.216 1.00 44.66 C ANISOU 475 C ASN A 78 4912 5961 6095 281 233 -477 C ATOM 476 O ASN A 78 172.972 38.749 522.184 1.00 51.32 O ANISOU 476 O ASN A 78 5723 6846 6931 339 157 -455 O ATOM 477 CB ASN A 78 172.857 40.007 525.259 1.00 39.19 C ANISOU 477 CB ASN A 78 4245 5145 5499 350 341 -524 C ATOM 478 CG ASN A 78 172.019 39.949 526.521 1.00 47.96 C ANISOU 478 CG ASN A 78 5307 6247 6669 395 419 -577 C ATOM 479 OD1 ASN A 78 171.042 39.203 526.599 1.00 47.45 O ANISOU 479 OD1 ASN A 78 5118 6247 6663 423 429 -594 O ATOM 480 ND2 ASN A 78 172.398 40.737 527.520 1.00 50.84 N ANISOU 480 ND2 ASN A 78 5771 6530 7016 397 478 -607 N ATOM 481 N LEU A 79 174.980 38.936 523.187 1.00 32.49 N ANISOU 481 N LEU A 79 3451 4399 4496 206 262 -454 N ATOM 482 CA LEU A 79 175.677 39.071 521.913 1.00 30.80 C ANISOU 482 CA LEU A 79 3291 4209 4204 191 230 -395 C ATOM 483 C LEU A 79 175.574 37.794 521.088 1.00 43.32 C ANISOU 483 C LEU A 79 4817 5897 5744 186 186 -423 C ATOM 484 O LEU A 79 175.410 37.849 519.863 1.00 60.78 O ANISOU 484 O LEU A 79 7057 8150 7887 227 129 -389 O ATOM 485 CB LEU A 79 177.141 39.443 522.150 1.00 32.35 C ANISOU 485 CB LEU A 79 3552 4369 4370 100 285 -368 C ATOM 486 CG LEU A 79 177.393 40.838 522.728 1.00 47.11 C ANISOU 486 CG LEU A 79 5505 6115 6278 87 314 -342 C ATOM 487 CD1 LEU A 79 178.883 41.092 522.896 1.00 45.90 C ANISOU 487 CD1 LEU A 79 5387 5940 6113 -26 354 -322 C ATOM 488 CD2 LEU A 79 176.761 41.906 521.851 1.00 24.50 C ANISOU 488 CD2 LEU A 79 2711 3187 3411 169 284 -266 C ATOM 489 N TYR A 80 175.664 36.633 521.740 1.00 38.37 N ANISOU 489 N TYR A 80 4124 5308 5148 140 209 -487 N ATOM 490 CA TYR A 80 175.517 35.378 521.009 1.00 35.42 C ANISOU 490 CA TYR A 80 3705 5007 4747 133 166 -530 C ATOM 491 C TYR A 80 174.088 35.197 520.510 1.00 36.11 C ANISOU 491 C TYR A 80 3722 5124 4875 192 80 -558 C ATOM 492 O TYR A 80 173.869 34.645 519.423 1.00 23.33 O ANISOU 492 O TYR A 80 2101 3562 3202 208 4 -582 O ATOM 493 CB TYR A 80 175.938 34.204 521.892 1.00 41.81 C ANISOU 493 CB TYR A 80 4470 5822 5595 74 216 -581 C ATOM 494 CG TYR A 80 176.122 32.910 521.135 1.00 41.73 C ANISOU 494 CG TYR A 80 4442 5859 5554 59 186 -629 C ATOM 495 CD1 TYR A 80 177.224 32.716 520.313 1.00 44.22 C ANISOU 495 CD1 TYR A 80 4814 6209 5778 52 201 -616 C ATOM 496 CD2 TYR A 80 175.197 31.880 521.245 1.00 35.23 C ANISOU 496 CD2 TYR A 80 3545 5040 4801 49 153 -690 C ATOM 497 CE1 TYR A 80 177.399 31.536 519.619 1.00 36.59 C ANISOU 497 CE1 TYR A 80 3848 5277 4777 52 181 -675 C ATOM 498 CE2 TYR A 80 175.365 30.695 520.555 1.00 42.51 C ANISOU 498 CE2 TYR A 80 4468 5983 5702 32 122 -750 C ATOM 499 CZ TYR A 80 176.467 30.529 519.744 1.00 41.53 C ANISOU 499 CZ TYR A 80 4417 5889 5472 42 135 -747 C ATOM 500 OH TYR A 80 176.639 29.351 519.053 1.00 51.19 O ANISOU 500 OH TYR A 80 5657 7125 6668 38 110 -820 O ATOM 501 N THR A 81 173.103 35.658 521.287 1.00 39.05 N ANISOU 501 N THR A 81 4032 5463 5341 228 89 -562 N ATOM 502 CA THR A 81 171.717 35.605 520.835 1.00 39.96 C ANISOU 502 CA THR A 81 4050 5614 5517 289 3 -582 C ATOM 503 C THR A 81 171.510 36.479 519.605 1.00 46.00 C ANISOU 503 C THR A 81 4874 6399 6206 372 -92 -527 C ATOM 504 O THR A 81 170.854 36.065 518.642 1.00 56.63 O ANISOU 504 O THR A 81 6176 7813 7529 405 -206 -552 O ATOM 505 CB THR A 81 170.776 36.039 521.958 1.00 41.16 C ANISOU 505 CB THR A 81 4120 5731 5789 326 58 -588 C ATOM 506 OG1 THR A 81 170.979 35.206 523.104 1.00 51.55 O ANISOU 506 OG1 THR A 81 5401 7033 7152 254 153 -625 O ATOM 507 CG2 THR A 81 169.326 35.927 521.511 1.00 52.92 C ANISOU 507 CG2 THR A 81 5470 7271 7367 388 -31 -609 C ATOM 508 N LEU A 82 172.061 37.695 519.621 1.00 43.36 N ANISOU 508 N LEU A 82 4646 6000 5827 405 -51 -451 N ATOM 509 CA LEU A 82 171.993 38.552 518.442 1.00 44.42 C ANISOU 509 CA LEU A 82 4865 6139 5874 484 -125 -373 C ATOM 510 C LEU A 82 172.674 37.893 517.249 1.00 46.04 C ANISOU 510 C LEU A 82 5134 6421 5939 455 -168 -372 C ATOM 511 O LEU A 82 172.145 37.912 516.129 1.00 39.60 O ANISOU 511 O LEU A 82 4335 5667 5043 525 -279 -355 O ATOM 512 CB LEU A 82 172.636 39.905 518.749 1.00 35.62 C ANISOU 512 CB LEU A 82 3869 4915 4751 497 -51 -288 C ATOM 513 CG LEU A 82 172.443 41.028 517.731 1.00 37.75 C ANISOU 513 CG LEU A 82 4240 5149 4953 594 -108 -180 C ATOM 514 CD1 LEU A 82 170.978 41.418 517.651 1.00 46.15 C ANISOU 514 CD1 LEU A 82 5222 6222 6092 726 -202 -178 C ATOM 515 CD2 LEU A 82 173.303 42.228 518.094 1.00 34.33 C ANISOU 515 CD2 LEU A 82 3934 4583 4526 566 -15 -103 C ATOM 516 N TYR A 83 173.842 37.288 517.481 1.00 47.24 N ANISOU 516 N TYR A 83 5321 6575 6054 363 -82 -393 N ATOM 517 CA TYR A 83 174.589 36.635 516.410 1.00 40.49 C ANISOU 517 CA TYR A 83 4530 5791 5065 345 -93 -399 C ATOM 518 C TYR A 83 173.770 35.525 515.761 1.00 48.12 C ANISOU 518 C TYR A 83 5434 6839 6010 364 -207 -493 C ATOM 519 O TYR A 83 173.617 35.488 514.534 1.00 42.65 O ANISOU 519 O TYR A 83 4804 6212 5189 418 -293 -487 O ATOM 520 CB TYR A 83 175.902 36.082 516.968 1.00 33.94 C ANISOU 520 CB TYR A 83 3711 4950 4236 253 23 -418 C ATOM 521 CG TYR A 83 176.840 35.494 515.936 1.00 38.03 C ANISOU 521 CG TYR A 83 4295 5535 4619 243 49 -419 C ATOM 522 CD1 TYR A 83 176.838 35.945 514.623 1.00 29.68 C ANISOU 522 CD1 TYR A 83 3335 4526 3417 305 11 -360 C ATOM 523 CD2 TYR A 83 177.729 34.483 516.278 1.00 51.02 C ANISOU 523 CD2 TYR A 83 5912 7198 6276 186 117 -476 C ATOM 524 CE1 TYR A 83 177.697 35.407 513.682 1.00 38.91 C ANISOU 524 CE1 TYR A 83 4573 5764 4448 307 55 -365 C ATOM 525 CE2 TYR A 83 178.590 33.939 515.344 1.00 46.66 C ANISOU 525 CE2 TYR A 83 5416 6707 5604 194 157 -484 C ATOM 526 CZ TYR A 83 178.570 34.404 514.048 1.00 43.74 C ANISOU 526 CZ TYR A 83 5145 6391 5083 253 133 -432 C ATOM 527 OH TYR A 83 179.426 33.865 513.116 1.00 51.03 O ANISOU 527 OH TYR A 83 6133 7383 5872 270 192 -443 O ATOM 528 N THR A 84 173.229 34.612 516.571 1.00 54.16 N ANISOU 528 N THR A 84 6083 7597 6900 316 -212 -583 N ATOM 529 CA THR A 84 172.514 33.468 516.011 1.00 48.68 C ANISOU 529 CA THR A 84 5324 6960 6211 307 -319 -685 C ATOM 530 C THR A 84 171.175 33.881 515.411 1.00 42.51 C ANISOU 530 C THR A 84 4479 6225 5448 383 -470 -688 C ATOM 531 O THR A 84 170.780 33.369 514.357 1.00 29.00 O ANISOU 531 O THR A 84 2779 4585 3656 406 -600 -747 O ATOM 532 CB THR A 84 172.308 32.398 517.083 1.00 57.84 C ANISOU 532 CB THR A 84 6379 8081 7515 224 -268 -762 C ATOM 533 OG1 THR A 84 171.535 32.942 518.160 1.00 77.99 O ANISOU 533 OG1 THR A 84 8835 10593 10205 231 -232 -733 O ATOM 534 CG2 THR A 84 173.648 31.915 517.618 1.00 47.93 C ANISOU 534 CG2 THR A 84 5186 6790 6235 166 -141 -758 C ATOM 535 N VAL A 85 170.465 34.805 516.062 1.00 50.92 N ANISOU 535 N VAL A 85 5477 7254 6616 432 -461 -632 N ATOM 536 CA VAL A 85 169.136 35.190 515.591 1.00 41.71 C ANISOU 536 CA VAL A 85 4217 6136 5496 519 -606 -632 C ATOM 537 C VAL A 85 169.232 35.963 514.281 1.00 39.81 C ANISOU 537 C VAL A 85 4102 5943 5082 621 -709 -558 C ATOM 538 O VAL A 85 168.478 35.705 513.334 1.00 50.48 O ANISOU 538 O VAL A 85 5421 7379 6380 674 -878 -596 O ATOM 539 CB VAL A 85 168.394 35.995 516.673 1.00 44.83 C ANISOU 539 CB VAL A 85 4510 6475 6049 564 -547 -591 C ATOM 540 CG1 VAL A 85 167.197 36.714 516.074 1.00 36.52 C ANISOU 540 CG1 VAL A 85 3381 5468 5026 692 -691 -557 C ATOM 541 CG2 VAL A 85 167.946 35.073 517.797 1.00 55.81 C ANISOU 541 CG2 VAL A 85 5752 7849 7603 475 -475 -668 C ATOM 542 N ILE A 86 170.159 36.922 514.200 1.00 44.54 N ANISOU 542 N ILE A 86 4850 6487 5588 648 -612 -448 N ATOM 543 CA ILE A 86 170.292 37.688 512.964 1.00 46.77 C ANISOU 543 CA ILE A 86 5271 6803 5695 745 -687 -353 C ATOM 544 C ILE A 86 170.843 36.816 511.840 1.00 56.09 C ANISOU 544 C ILE A 86 6545 8077 6691 722 -737 -405 C ATOM 545 O ILE A 86 170.449 36.966 510.676 1.00 67.04 O ANISOU 545 O ILE A 86 8000 9543 7929 811 -874 -384 O ATOM 546 CB ILE A 86 171.158 38.940 513.206 1.00 48.07 C ANISOU 546 CB ILE A 86 5568 6865 5830 760 -554 -215 C ATOM 547 CG1 ILE A 86 170.374 39.969 514.023 1.00 53.05 C ANISOU 547 CG1 ILE A 86 6137 7405 6613 831 -547 -166 C ATOM 548 CG2 ILE A 86 171.628 39.550 511.893 1.00 48.17 C ANISOU 548 CG2 ILE A 86 5757 6909 5636 830 -584 -102 C ATOM 549 CD1 ILE A 86 170.986 41.351 514.021 1.00 65.08 C ANISOU 549 CD1 ILE A 86 7811 8812 8106 869 -460 -26 C ATOM 550 N GLY A 87 171.734 35.880 512.163 1.00 45.50 N ANISOU 550 N GLY A 87 5212 6729 5349 617 -633 -479 N ATOM 551 CA GLY A 87 172.326 34.998 511.181 1.00 31.49 C ANISOU 551 CA GLY A 87 3530 5029 3405 602 -654 -544 C ATOM 552 C GLY A 87 173.756 35.332 510.817 1.00 39.62 C ANISOU 552 C GLY A 87 4709 6050 4296 588 -500 -458 C ATOM 553 O GLY A 87 174.388 34.563 510.082 1.00 51.91 O ANISOU 553 O GLY A 87 6343 7667 5714 579 -480 -516 O ATOM 554 N TYR A 88 174.279 36.450 511.310 1.00 39.01 N ANISOU 554 N TYR A 88 4667 5895 4259 584 -387 -329 N ATOM 555 CA TYR A 88 175.648 36.866 511.041 1.00 35.96 C ANISOU 555 CA TYR A 88 4395 5494 3777 552 -229 -235 C ATOM 556 C TYR A 88 176.022 37.926 512.066 1.00 33.07 C ANISOU 556 C TYR A 88 4008 5009 3549 506 -124 -140 C ATOM 557 O TYR A 88 175.176 38.412 512.820 1.00 29.35 O ANISOU 557 O TYR A 88 3465 4473 3212 526 -175 -142 O ATOM 558 CB TYR A 88 175.803 37.394 509.611 1.00 32.45 C ANISOU 558 CB TYR A 88 4111 5115 3103 641 -255 -136 C ATOM 559 CG TYR A 88 174.841 38.508 509.274 1.00 33.72 C ANISOU 559 CG TYR A 88 4315 5251 3247 744 -367 -30 C ATOM 560 CD1 TYR A 88 173.568 38.229 508.792 1.00 56.45 C ANISOU 560 CD1 TYR A 88 7152 8200 6097 832 -569 -93 C ATOM 561 CD2 TYR A 88 175.202 39.837 509.441 1.00 34.03 C ANISOU 561 CD2 TYR A 88 4429 5189 3313 755 -277 132 C ATOM 562 CE1 TYR A 88 172.683 39.243 508.486 1.00 59.80 C ANISOU 562 CE1 TYR A 88 7603 8605 6512 947 -680 9 C ATOM 563 CE2 TYR A 88 174.325 40.857 509.138 1.00 37.05 C ANISOU 563 CE2 TYR A 88 4859 5531 3687 867 -377 235 C ATOM 564 CZ TYR A 88 173.066 40.555 508.661 1.00 54.41 C ANISOU 564 CZ TYR A 88 7010 7813 5852 972 -580 177 C ATOM 565 OH TYR A 88 172.188 41.569 508.355 1.00 62.72 O ANISOU 565 OH TYR A 88 8098 8831 6901 1104 -688 285 O ATOM 566 N TRP A 89 177.300 38.281 512.085 1.00 43.61 N ANISOU 566 N TRP A 89 5403 6315 4853 444 25 -66 N ATOM 567 CA TRP A 89 177.784 39.260 513.049 1.00 43.87 C ANISOU 567 CA TRP A 89 5423 6228 5017 381 119 7 C ATOM 568 C TRP A 89 177.501 40.670 512.546 1.00 44.49 C ANISOU 568 C TRP A 89 5615 6232 5057 444 109 155 C ATOM 569 O TRP A 89 178.013 41.053 511.487 1.00 52.69 O ANISOU 569 O TRP A 89 6773 7300 5947 469 155 263 O ATOM 570 CB TRP A 89 179.273 39.079 513.301 1.00 28.29 C ANISOU 570 CB TRP A 89 3444 4254 3052 277 269 25 C ATOM 571 CG TRP A 89 179.771 39.956 514.395 1.00 27.72 C ANISOU 571 CG TRP A 89 3345 4062 3125 194 340 66 C ATOM 572 CD1 TRP A 89 180.519 41.086 514.262 1.00 34.90 C ANISOU 572 CD1 TRP A 89 4326 4890 4044 143 430 190 C ATOM 573 CD2 TRP A 89 179.534 39.792 515.798 1.00 35.07 C ANISOU 573 CD2 TRP A 89 4180 4936 4209 147 323 -20 C ATOM 574 NE1 TRP A 89 180.775 41.632 515.497 1.00 41.22 N ANISOU 574 NE1 TRP A 89 5081 5582 4998 63 455 168 N ATOM 575 CE2 TRP A 89 180.180 40.856 516.457 1.00 35.00 C ANISOU 575 CE2 TRP A 89 4197 4816 4287 73 392 41 C ATOM 576 CE3 TRP A 89 178.843 38.846 516.561 1.00 32.47 C ANISOU 576 CE3 TRP A 89 3753 4635 3948 158 263 -140 C ATOM 577 CZ2 TRP A 89 180.156 41.000 517.843 1.00 30.49 C ANISOU 577 CZ2 TRP A 89 3568 4173 3845 21 390 -26 C ATOM 578 CZ3 TRP A 89 178.820 38.990 517.935 1.00 34.72 C ANISOU 578 CZ3 TRP A 89 3980 4851 4360 109 280 -186 C ATOM 579 CH2 TRP A 89 179.473 40.059 518.562 1.00 41.95 C ANISOU 579 CH2 TRP A 89 4934 5668 5338 48 338 -136 C ATOM 580 N PRO A 90 176.706 41.468 513.261 1.00 44.96 N ANISOU 580 N PRO A 90 5651 6191 5242 479 61 171 N ATOM 581 CA PRO A 90 176.330 42.791 512.748 1.00 43.40 C ANISOU 581 CA PRO A 90 5570 5905 5013 562 39 313 C ATOM 582 C PRO A 90 177.162 43.935 513.309 1.00 45.92 C ANISOU 582 C PRO A 90 5956 6067 5423 482 164 407 C ATOM 583 O PRO A 90 177.163 45.035 512.747 1.00 44.78 O ANISOU 583 O PRO A 90 5941 5833 5242 529 181 551 O ATOM 584 CB PRO A 90 174.860 42.921 513.180 1.00 39.73 C ANISOU 584 CB PRO A 90 5025 5424 4645 668 -94 260 C ATOM 585 CG PRO A 90 174.611 41.774 514.181 1.00 35.39 C ANISOU 585 CG PRO A 90 4314 4927 4206 603 -104 94 C ATOM 586 CD PRO A 90 175.929 41.119 514.458 1.00 38.08 C ANISOU 586 CD PRO A 90 4649 5290 4529 472 14 58 C ATOM 587 N LEU A 91 177.871 43.695 514.411 1.00 55.25 N ANISOU 587 N LEU A 91 7059 7209 6724 359 242 329 N ATOM 588 CA LEU A 91 178.518 44.768 515.153 1.00 55.21 C ANISOU 588 CA LEU A 91 7099 7043 6835 273 328 380 C ATOM 589 C LEU A 91 179.909 45.119 514.639 1.00 57.77 C ANISOU 589 C LEU A 91 7485 7349 7118 160 456 484 C ATOM 590 O LEU A 91 180.434 46.177 515.003 1.00 70.79 O ANISOU 590 O LEU A 91 9194 8847 8857 84 522 552 O ATOM 591 CB LEU A 91 178.597 44.400 516.638 1.00 46.66 C ANISOU 591 CB LEU A 91 5907 5931 5891 199 336 243 C ATOM 592 CG LEU A 91 177.243 44.115 517.293 1.00 42.13 C ANISOU 592 CG LEU A 91 5260 5367 5380 299 243 147 C ATOM 593 CD1 LEU A 91 177.405 43.821 518.774 1.00 42.17 C ANISOU 593 CD1 LEU A 91 5185 5340 5496 227 273 29 C ATOM 594 CD2 LEU A 91 176.286 45.277 517.074 1.00 43.28 C ANISOU 594 CD2 LEU A 91 5487 5399 5557 421 195 222 C ATOM 595 N GLY A 92 180.519 44.273 513.813 1.00 49.85 N ANISOU 595 N GLY A 92 6465 6487 5987 145 499 493 N ATOM 596 CA GLY A 92 181.802 44.585 513.232 1.00 53.54 C ANISOU 596 CA GLY A 92 6975 6955 6411 49 640 602 C ATOM 597 C GLY A 92 182.936 43.751 513.795 1.00 60.29 C ANISOU 597 C GLY A 92 7698 7886 7323 -71 718 517 C ATOM 598 O GLY A 92 182.759 42.961 514.727 1.00 55.68 O ANISOU 598 O GLY A 92 7004 7339 6813 -83 661 377 O ATOM 599 N PRO A 93 184.137 43.927 513.237 1.00 57.10 N ANISOU 599 N PRO A 93 7299 7506 6889 -156 857 612 N ATOM 600 CA PRO A 93 185.262 43.077 513.665 1.00 53.73 C ANISOU 600 CA PRO A 93 6728 7172 6513 -250 932 538 C ATOM 601 C PRO A 93 185.773 43.403 515.058 1.00 46.58 C ANISOU 601 C PRO A 93 5721 6174 5802 -376 919 472 C ATOM 602 O PRO A 93 186.116 42.483 515.814 1.00 58.29 O ANISOU 602 O PRO A 93 7080 7731 7337 -401 893 355 O ATOM 603 CB PRO A 93 186.322 43.345 512.588 1.00 51.82 C ANISOU 603 CB PRO A 93 6521 6980 6189 -296 1098 680 C ATOM 604 CG PRO A 93 186.017 44.724 512.104 1.00 45.04 C ANISOU 604 CG PRO A 93 5814 5979 5321 -300 1123 840 C ATOM 605 CD PRO A 93 184.521 44.868 512.171 1.00 44.82 C ANISOU 605 CD PRO A 93 5875 5903 5251 -164 962 800 C ATOM 606 N VAL A 94 185.835 44.687 515.419 1.00 32.02 N ANISOU 606 N VAL A 94 3940 4164 4062 -452 930 541 N ATOM 607 CA VAL A 94 186.381 45.076 516.718 1.00 39.89 C ANISOU 607 CA VAL A 94 4858 5068 5231 -581 908 468 C ATOM 608 C VAL A 94 185.537 44.497 517.846 1.00 39.83 C ANISOU 608 C VAL A 94 4809 5069 5257 -519 782 311 C ATOM 609 O VAL A 94 186.055 43.854 518.769 1.00 54.67 O ANISOU 609 O VAL A 94 6572 7002 7197 -574 757 209 O ATOM 610 CB VAL A 94 186.482 46.608 516.821 1.00 48.13 C ANISOU 610 CB VAL A 94 6007 5905 6376 -668 937 562 C ATOM 611 CG1 VAL A 94 187.038 47.013 518.178 1.00 33.15 C ANISOU 611 CG1 VAL A 94 4039 3910 4646 -805 895 462 C ATOM 612 CG2 VAL A 94 187.344 47.161 515.697 1.00 49.88 C ANISOU 612 CG2 VAL A 94 6268 6115 6568 -741 1084 738 C ATOM 613 N VAL A 95 184.221 44.714 517.788 1.00 32.94 N ANISOU 613 N VAL A 95 4026 4146 4344 -396 705 299 N ATOM 614 CA VAL A 95 183.331 44.195 518.822 1.00 33.30 C ANISOU 614 CA VAL A 95 4030 4201 4423 -333 607 164 C ATOM 615 C VAL A 95 183.355 42.672 518.839 1.00 30.59 C ANISOU 615 C VAL A 95 3579 4024 4019 -295 588 80 C ATOM 616 O VAL A 95 183.183 42.052 519.895 1.00 40.48 O ANISOU 616 O VAL A 95 4761 5300 5318 -298 542 -29 O ATOM 617 CB VAL A 95 181.904 44.740 518.616 1.00 42.83 C ANISOU 617 CB VAL A 95 5331 5333 5608 -200 541 182 C ATOM 618 CG1 VAL A 95 181.011 44.364 519.789 1.00 43.75 C ANISOU 618 CG1 VAL A 95 5398 5444 5781 -147 468 51 C ATOM 619 CG2 VAL A 95 181.937 46.249 518.428 1.00 42.89 C ANISOU 619 CG2 VAL A 95 5467 5158 5672 -223 571 285 C ATOM 620 N CYS A 96 183.575 42.046 517.681 1.00 30.13 N ANISOU 620 N CYS A 96 3520 4078 3851 -254 627 128 N ATOM 621 CA CYS A 96 183.697 40.592 517.637 1.00 39.42 C ANISOU 621 CA CYS A 96 4609 5393 4978 -220 617 43 C ATOM 622 C CYS A 96 184.920 40.123 518.416 1.00 46.57 C ANISOU 622 C CYS A 96 5400 6335 5959 -318 662 0 C ATOM 623 O CYS A 96 184.831 39.209 519.246 1.00 51.01 O ANISOU 623 O CYS A 96 5889 6939 6553 -306 618 -97 O ATOM 624 CB CYS A 96 183.769 40.115 516.186 1.00 43.72 C ANISOU 624 CB CYS A 96 5198 6039 5376 -154 657 96 C ATOM 625 SG CYS A 96 184.356 38.416 516.007 0.78 46.82 S ANISOU 625 SG CYS A 96 5494 6579 5716 -131 685 0 S ATOM 626 N ASP A 97 186.075 40.744 518.161 1.00 49.58 N ANISOU 626 N ASP A 97 5761 6702 6375 -415 750 79 N ATOM 627 CA ASP A 97 187.291 40.365 518.872 1.00 47.68 C ANISOU 627 CA ASP A 97 5389 6507 6220 -507 780 43 C ATOM 628 C ASP A 97 187.162 40.630 520.368 1.00 47.45 C ANISOU 628 C ASP A 97 5333 6403 6294 -560 691 -42 C ATOM 629 O ASP A 97 187.591 39.810 521.190 1.00 47.35 O ANISOU 629 O ASP A 97 5223 6453 6313 -568 656 -118 O ATOM 630 CB ASP A 97 188.491 41.113 518.291 1.00 54.53 C ANISOU 630 CB ASP A 97 6224 7367 7127 -616 893 152 C ATOM 631 CG ASP A 97 188.708 40.813 516.819 1.00 69.24 C ANISOU 631 CG ASP A 97 8123 9321 8864 -557 1004 240 C ATOM 632 OD1 ASP A 97 188.365 39.695 516.382 1.00 74.88 O ANISOU 632 OD1 ASP A 97 8835 10138 9476 -447 994 184 O ATOM 633 OD2 ASP A 97 189.223 41.695 516.099 1.00 73.41 O ANISOU 633 OD2 ASP A 97 8691 9811 9392 -620 1107 365 O ATOM 634 N LEU A 98 186.564 41.766 520.740 1.00 48.63 N ANISOU 634 N LEU A 98 5577 6414 6485 -583 655 -31 N ATOM 635 CA LEU A 98 186.373 42.069 522.155 1.00 42.79 C ANISOU 635 CA LEU A 98 4837 5601 5819 -620 575 -124 C ATOM 636 C LEU A 98 185.428 41.070 522.813 1.00 40.66 C ANISOU 636 C LEU A 98 4558 5386 5506 -516 513 -216 C ATOM 637 O LEU A 98 185.599 40.721 523.987 1.00 56.00 O ANISOU 637 O LEU A 98 6460 7341 7477 -536 464 -297 O ATOM 638 CB LEU A 98 185.844 43.494 522.321 1.00 37.57 C ANISOU 638 CB LEU A 98 4301 4767 5208 -645 561 -99 C ATOM 639 CG LEU A 98 186.761 44.628 521.858 1.00 40.93 C ANISOU 639 CG LEU A 98 4751 5094 5707 -775 623 -6 C ATOM 640 CD1 LEU A 98 186.083 45.978 522.046 1.00 40.48 C ANISOU 640 CD1 LEU A 98 4841 4839 5701 -775 604 12 C ATOM 641 CD2 LEU A 98 188.091 44.584 522.596 1.00 37.11 C ANISOU 641 CD2 LEU A 98 4145 4638 5316 -922 612 -50 C ATOM 642 N TRP A 99 184.425 40.598 522.070 1.00 27.95 N ANISOU 642 N TRP A 99 2984 3811 3825 -407 512 -203 N ATOM 643 CA TRP A 99 183.487 39.622 522.615 1.00 28.58 C ANISOU 643 CA TRP A 99 3042 3936 3882 -323 464 -282 C ATOM 644 C TRP A 99 184.162 38.271 522.826 1.00 30.78 C ANISOU 644 C TRP A 99 3224 4324 4146 -326 471 -322 C ATOM 645 O TRP A 99 184.064 37.678 523.910 1.00 23.63 O ANISOU 645 O TRP A 99 2286 3432 3261 -320 438 -386 O ATOM 646 CB TRP A 99 182.277 39.498 521.686 1.00 30.18 C ANISOU 646 CB TRP A 99 3291 4149 4029 -220 447 -260 C ATOM 647 CG TRP A 99 181.369 38.344 521.987 1.00 30.00 C ANISOU 647 CG TRP A 99 3220 4183 3994 -151 408 -333 C ATOM 648 CD1 TRP A 99 180.690 38.115 523.147 1.00 38.44 C ANISOU 648 CD1 TRP A 99 4270 5227 5108 -133 384 -397 C ATOM 649 CD2 TRP A 99 181.023 37.273 521.101 1.00 30.70 C ANISOU 649 CD2 TRP A 99 3283 4357 4025 -97 394 -348 C ATOM 650 NE1 TRP A 99 179.952 36.960 523.043 1.00 39.08 N ANISOU 650 NE1 TRP A 99 4302 5367 5181 -83 364 -440 N ATOM 651 CE2 TRP A 99 180.139 36.425 521.796 1.00 31.31 C ANISOU 651 CE2 TRP A 99 3313 4445 4137 -63 360 -419 C ATOM 652 CE3 TRP A 99 181.381 36.945 519.789 1.00 41.93 C ANISOU 652 CE3 TRP A 99 4724 5845 5364 -75 413 -312 C ATOM 653 CZ2 TRP A 99 179.606 35.271 521.224 1.00 36.83 C ANISOU 653 CZ2 TRP A 99 3979 5203 4812 -23 332 -462 C ATOM 654 CZ3 TRP A 99 180.851 35.799 519.223 1.00 45.71 C ANISOU 654 CZ3 TRP A 99 5182 6389 5796 -22 378 -367 C ATOM 655 CH2 TRP A 99 179.974 34.976 519.940 1.00 45.13 C ANISOU 655 CH2 TRP A 99 5057 6311 5780 -3 332 -444 C ATOM 656 N LEU A 100 184.864 37.776 521.801 1.00 29.14 N ANISOU 656 N LEU A 100 2981 4195 3898 -324 522 -280 N ATOM 657 CA LEU A 100 185.557 36.495 521.917 1.00 34.49 C ANISOU 657 CA LEU A 100 3570 4965 4568 -309 537 -317 C ATOM 658 C LEU A 100 186.596 36.528 523.033 1.00 50.26 C ANISOU 658 C LEU A 100 5490 6971 6635 -380 521 -336 C ATOM 659 O LEU A 100 186.652 35.624 523.876 1.00 49.41 O ANISOU 659 O LEU A 100 5340 6895 6537 -352 485 -388 O ATOM 660 CB LEU A 100 186.213 36.135 520.583 1.00 31.51 C ANISOU 660 CB LEU A 100 3177 4664 4131 -288 613 -269 C ATOM 661 CG LEU A 100 185.285 35.946 519.383 1.00 33.07 C ANISOU 661 CG LEU A 100 3458 4878 4230 -208 613 -260 C ATOM 662 CD1 LEU A 100 186.092 35.805 518.103 1.00 28.74 C ANISOU 662 CD1 LEU A 100 2914 4406 3600 -192 706 -205 C ATOM 663 CD2 LEU A 100 184.386 34.737 519.589 1.00 33.20 C ANISOU 663 CD2 LEU A 100 3470 4912 4231 -136 554 -348 C ATOM 664 N ALA A 101 187.433 37.569 523.050 1.00 58.42 N ANISOU 664 N ALA A 101 6505 7973 7719 -476 540 -293 N ATOM 665 CA ALA A 101 188.419 37.695 524.118 1.00 50.36 C ANISOU 665 CA ALA A 101 5402 6964 6769 -555 497 -322 C ATOM 666 C ALA A 101 187.744 37.800 525.479 1.00 39.51 C ANISOU 666 C ALA A 101 4083 5533 5394 -545 410 -396 C ATOM 667 O ALA A 101 188.239 37.252 526.471 1.00 32.44 O ANISOU 667 O ALA A 101 3133 4684 4509 -548 355 -440 O ATOM 668 CB ALA A 101 189.316 38.908 523.866 1.00 38.68 C ANISOU 668 CB ALA A 101 3895 5439 5361 -682 528 -267 C ATOM 669 N LEU A 102 186.597 38.481 525.539 1.00 38.85 N ANISOU 669 N LEU A 102 4111 5358 5293 -519 401 -408 N ATOM 670 CA LEU A 102 185.907 38.673 526.810 1.00 31.15 C ANISOU 670 CA LEU A 102 3199 4329 4309 -500 344 -479 C ATOM 671 C LEU A 102 185.416 37.346 527.378 1.00 31.52 C ANISOU 671 C LEU A 102 3222 4442 4311 -416 332 -514 C ATOM 672 O LEU A 102 185.786 36.958 528.492 1.00 47.29 O ANISOU 672 O LEU A 102 5204 6468 6295 -421 286 -554 O ATOM 673 CB LEU A 102 184.744 39.650 526.637 1.00 39.89 C ANISOU 673 CB LEU A 102 4416 5326 5416 -467 355 -478 C ATOM 674 CG LEU A 102 183.937 39.923 527.909 1.00 39.38 C ANISOU 674 CG LEU A 102 4424 5203 5336 -431 321 -554 C ATOM 675 CD1 LEU A 102 184.838 40.466 529.008 1.00 36.08 C ANISOU 675 CD1 LEU A 102 4019 4757 4933 -519 264 -613 C ATOM 676 CD2 LEU A 102 182.789 40.882 527.629 1.00 42.09 C ANISOU 676 CD2 LEU A 102 4860 5439 5693 -377 342 -549 C ATOM 677 N ASP A 103 184.577 36.629 526.624 1.00 40.57 N ANISOU 677 N ASP A 103 4372 5611 5432 -340 367 -498 N ATOM 678 CA ASP A 103 184.008 35.403 527.180 1.00 42.25 C ANISOU 678 CA ASP A 103 4571 5860 5622 -274 364 -528 C ATOM 679 C ASP A 103 185.052 34.298 527.300 1.00 42.92 C ANISOU 679 C ASP A 103 4579 6022 5706 -269 359 -521 C ATOM 680 O ASP A 103 184.922 33.420 528.162 1.00 56.38 O ANISOU 680 O ASP A 103 6282 7744 7397 -231 344 -538 O ATOM 681 CB ASP A 103 182.810 34.934 526.350 1.00 47.56 C ANISOU 681 CB ASP A 103 5258 6527 6287 -210 388 -525 C ATOM 682 CG ASP A 103 183.206 34.395 524.993 1.00 59.08 C ANISOU 682 CG ASP A 103 6683 8036 7729 -196 411 -498 C ATOM 683 OD1 ASP A 103 184.154 34.930 524.393 1.00 68.05 O ANISOU 683 OD1 ASP A 103 7804 9191 8861 -237 431 -460 O ATOM 684 OD2 ASP A 103 182.559 33.437 524.522 1.00 60.19 O ANISOU 684 OD2 ASP A 103 6815 8196 7859 -147 413 -518 O ATOM 685 N TYR A 104 186.098 34.326 526.469 1.00 34.04 N ANISOU 685 N TYR A 104 3391 4944 4598 -298 380 -488 N ATOM 686 CA TYR A 104 187.162 33.336 526.612 1.00 27.74 C ANISOU 686 CA TYR A 104 2505 4222 3813 -278 378 -481 C ATOM 687 C TYR A 104 187.980 33.585 527.876 1.00 36.45 C ANISOU 687 C TYR A 104 3571 5345 4932 -320 307 -495 C ATOM 688 O TYR A 104 188.250 32.653 528.647 1.00 38.12 O ANISOU 688 O TYR A 104 3759 5593 5131 -269 273 -502 O ATOM 689 CB TYR A 104 188.054 33.337 525.371 1.00 23.55 C ANISOU 689 CB TYR A 104 1905 3746 3297 -289 438 -442 C ATOM 690 CG TYR A 104 187.657 32.298 524.344 1.00 26.01 C ANISOU 690 CG TYR A 104 2231 4080 3572 -206 491 -449 C ATOM 691 CD1 TYR A 104 186.602 32.523 523.471 1.00 32.04 C ANISOU 691 CD1 TYR A 104 3074 4808 4291 -187 509 -453 C ATOM 692 CD2 TYR A 104 188.336 31.090 524.253 1.00 37.23 C ANISOU 692 CD2 TYR A 104 3590 5554 5003 -142 513 -458 C ATOM 693 CE1 TYR A 104 186.235 31.575 522.532 1.00 39.32 C ANISOU 693 CE1 TYR A 104 4018 5751 5172 -118 538 -478 C ATOM 694 CE2 TYR A 104 187.976 30.136 523.319 1.00 40.23 C ANISOU 694 CE2 TYR A 104 4001 5939 5348 -68 557 -483 C ATOM 695 CZ TYR A 104 186.925 30.383 522.462 1.00 43.38 C ANISOU 695 CZ TYR A 104 4483 6306 5695 -63 565 -499 C ATOM 696 OH TYR A 104 186.566 29.436 521.531 1.00 47.86 O ANISOU 696 OH TYR A 104 5088 6878 6220 4 590 -542 O ATOM 697 N VAL A 105 188.377 34.839 528.110 1.00 32.25 N ANISOU 697 N VAL A 105 3043 4783 4428 -411 276 -501 N ATOM 698 CA VAL A 105 189.108 35.173 529.331 1.00 23.21 C ANISOU 698 CA VAL A 105 1873 3656 3291 -461 184 -534 C ATOM 699 C VAL A 105 188.261 34.872 530.562 1.00 33.36 C ANISOU 699 C VAL A 105 3259 4914 4503 -407 141 -577 C ATOM 700 O VAL A 105 188.745 34.288 531.540 1.00 34.38 O ANISOU 700 O VAL A 105 3369 5095 4598 -378 74 -588 O ATOM 701 CB VAL A 105 189.556 36.647 529.302 1.00 24.16 C ANISOU 701 CB VAL A 105 1996 3718 3463 -585 158 -547 C ATOM 702 CG1 VAL A 105 189.907 37.128 530.702 1.00 25.02 C ANISOU 702 CG1 VAL A 105 2132 3817 3556 -635 43 -614 C ATOM 703 CG2 VAL A 105 190.746 36.822 528.374 1.00 40.13 C ANISOU 703 CG2 VAL A 105 3885 5795 5567 -654 199 -493 C ATOM 704 N VAL A 106 186.983 35.256 530.528 1.00 40.51 N ANISOU 704 N VAL A 106 4268 5742 5379 -383 183 -593 N ATOM 705 CA VAL A 106 186.103 35.035 531.674 1.00 37.21 C ANISOU 705 CA VAL A 106 3945 5301 4893 -330 172 -628 C ATOM 706 C VAL A 106 185.939 33.545 531.946 1.00 36.48 C ANISOU 706 C VAL A 106 3832 5258 4771 -247 192 -596 C ATOM 707 O VAL A 106 186.015 33.095 533.098 1.00 44.54 O ANISOU 707 O VAL A 106 4893 6304 5728 -213 156 -601 O ATOM 708 CB VAL A 106 184.746 35.726 531.443 1.00 33.53 C ANISOU 708 CB VAL A 106 3565 4751 4426 -310 230 -646 C ATOM 709 CG1 VAL A 106 183.707 35.206 532.421 1.00 31.43 C ANISOU 709 CG1 VAL A 106 3367 4476 4098 -239 261 -663 C ATOM 710 CG2 VAL A 106 184.895 37.235 531.576 1.00 28.20 C ANISOU 710 CG2 VAL A 106 2946 3999 3769 -379 200 -686 C ATOM 711 N SER A 107 185.719 32.754 530.893 1.00 28.38 N ANISOU 711 N SER A 107 2758 4240 3784 -213 250 -562 N ATOM 712 CA SER A 107 185.563 31.315 531.077 1.00 32.03 C ANISOU 712 CA SER A 107 3211 4721 4238 -141 273 -534 C ATOM 713 C SER A 107 186.833 30.687 531.638 1.00 34.80 C ANISOU 713 C SER A 107 3505 5139 4580 -117 213 -511 C ATOM 714 O SER A 107 186.771 29.834 532.533 1.00 45.85 O ANISOU 714 O SER A 107 4940 6543 5937 -58 199 -486 O ATOM 715 CB SER A 107 185.181 30.659 529.753 1.00 39.84 C ANISOU 715 CB SER A 107 4166 5698 5273 -116 331 -524 C ATOM 716 OG SER A 107 183.965 31.187 529.251 1.00 50.31 O ANISOU 716 OG SER A 107 5534 6974 6608 -127 366 -542 O ATOM 717 N ASN A 108 187.997 31.098 531.125 1.00 35.92 N ANISOU 717 N ASN A 108 3551 5332 4764 -157 179 -509 N ATOM 718 CA ASN A 108 189.256 30.587 531.658 1.00 45.75 C ANISOU 718 CA ASN A 108 4713 6654 6017 -130 108 -488 C ATOM 719 C ASN A 108 189.404 30.930 533.136 1.00 52.78 C ANISOU 719 C ASN A 108 5659 7562 6833 -138 9 -507 C ATOM 720 O ASN A 108 189.803 30.081 533.945 1.00 55.90 O ANISOU 720 O ASN A 108 6055 7999 7186 -65 -44 -476 O ATOM 721 CB ASN A 108 190.429 31.147 530.853 1.00 44.98 C ANISOU 721 CB ASN A 108 4481 6613 5994 -190 101 -484 C ATOM 722 CG ASN A 108 191.721 30.400 531.108 1.00 41.41 C ANISOU 722 CG ASN A 108 3901 6253 5579 -137 47 -455 C ATOM 723 OD1 ASN A 108 192.078 29.484 530.366 1.00 34.89 O ANISOU 723 OD1 ASN A 108 3011 5453 4793 -62 108 -426 O ATOM 724 ND2 ASN A 108 192.431 30.786 532.162 1.00 45.88 N ANISOU 724 ND2 ASN A 108 4429 6871 6131 -168 -75 -469 N ATOM 725 N ALA A 109 189.071 32.170 533.507 1.00 23.84 N ANISOU 725 N ALA A 109 2056 3862 3141 -217 -19 -559 N ATOM 726 CA ALA A 109 189.146 32.574 534.907 1.00 28.09 C ANISOU 726 CA ALA A 109 2674 4414 3585 -223 -115 -599 C ATOM 727 C ALA A 109 188.190 31.769 535.776 1.00 34.49 C ANISOU 727 C ALA A 109 3606 5203 4293 -131 -74 -573 C ATOM 728 O ALA A 109 188.495 31.495 536.942 1.00 49.58 O ANISOU 728 O ALA A 109 5572 7160 6105 -89 -152 -570 O ATOM 729 CB ALA A 109 188.856 34.069 535.038 1.00 25.02 C ANISOU 729 CB ALA A 109 2350 3963 3194 -319 -135 -673 C ATOM 730 N SER A 110 187.033 31.382 535.234 1.00 41.08 N ANISOU 730 N SER A 110 4483 5975 5151 -102 46 -551 N ATOM 731 CA SER A 110 186.113 30.548 536.001 1.00 40.14 C ANISOU 731 CA SER A 110 4461 5831 4959 -28 107 -513 C ATOM 732 C SER A 110 186.670 29.142 536.185 1.00 47.85 C ANISOU 732 C SER A 110 5407 6839 5935 51 93 -437 C ATOM 733 O SER A 110 186.539 28.551 537.266 1.00 60.80 O ANISOU 733 O SER A 110 7132 8490 7479 113 85 -393 O ATOM 734 CB SER A 110 184.747 30.503 535.319 1.00 32.32 C ANISOU 734 CB SER A 110 3492 4767 4022 -30 229 -513 C ATOM 735 OG SER A 110 184.834 29.900 534.040 1.00 50.62 O ANISOU 735 OG SER A 110 5722 7072 6439 -31 263 -492 O ATOM 736 N VAL A 111 187.300 28.591 535.143 1.00 46.19 N ANISOU 736 N VAL A 111 5087 6640 5823 60 98 -417 N ATOM 737 CA VAL A 111 187.895 27.260 535.255 1.00 43.22 C ANISOU 737 CA VAL A 111 4682 6279 5462 150 87 -349 C ATOM 738 C VAL A 111 188.993 27.257 536.312 1.00 51.70 C ANISOU 738 C VAL A 111 5742 7438 6462 191 -44 -328 C ATOM 739 O VAL A 111 188.998 26.426 537.230 1.00 59.46 O ANISOU 739 O VAL A 111 6799 8424 7371 276 -65 -263 O ATOM 740 CB VAL A 111 188.424 26.790 533.889 1.00 36.72 C ANISOU 740 CB VAL A 111 3745 5455 4753 161 122 -351 C ATOM 741 CG1 VAL A 111 189.213 25.499 534.042 1.00 29.33 C ANISOU 741 CG1 VAL A 111 2772 4531 3840 270 101 -289 C ATOM 742 CG2 VAL A 111 187.272 26.599 532.915 1.00 45.43 C ANISOU 742 CG2 VAL A 111 4879 6476 5907 135 231 -373 C ATOM 743 N MET A 112 189.939 28.195 536.204 1.00 45.31 N ANISOU 743 N MET A 112 4839 6701 5675 128 -140 -378 N ATOM 744 CA MET A 112 190.992 28.276 537.209 1.00 36.09 C ANISOU 744 CA MET A 112 3642 5627 4443 155 -293 -373 C ATOM 745 C MET A 112 190.448 28.644 538.584 1.00 40.00 C ANISOU 745 C MET A 112 4299 6124 4775 163 -344 -390 C ATOM 746 O MET A 112 191.092 28.335 539.592 1.00 41.24 O ANISOU 746 O MET A 112 4480 6354 4836 226 -465 -363 O ATOM 747 CB MET A 112 192.067 29.273 536.774 1.00 27.99 C ANISOU 747 CB MET A 112 2466 4670 3499 58 -382 -432 C ATOM 748 CG MET A 112 192.909 28.782 535.605 1.00 38.06 C ANISOU 748 CG MET A 112 3565 5979 4915 78 -341 -401 C ATOM 749 SD MET A 112 194.523 29.578 535.494 0.55 44.32 S ANISOU 749 SD MET A 112 4142 6893 5806 -5 -472 -433 S ATOM 750 CE MET A 112 194.042 31.278 535.217 1.00 41.16 C ANISOU 750 CE MET A 112 3792 6427 5419 -188 -455 -521 C ATOM 751 N ASN A 113 189.280 29.287 538.649 1.00 34.79 N ANISOU 751 N ASN A 113 3752 5393 4074 113 -253 -434 N ATOM 752 CA ASN A 113 188.632 29.509 539.937 1.00 37.36 C ANISOU 752 CA ASN A 113 4247 5716 4231 142 -260 -445 C ATOM 753 C ASN A 113 188.170 28.190 540.545 1.00 34.39 C ANISOU 753 C ASN A 113 3961 5324 3780 256 -194 -334 C ATOM 754 O ASN A 113 188.373 27.944 541.741 1.00 40.11 O ANISOU 754 O ASN A 113 4792 6100 4349 323 -263 -300 O ATOM 755 CB ASN A 113 187.456 30.472 539.772 1.00 49.91 C ANISOU 755 CB ASN A 113 5917 7230 5817 79 -156 -514 C ATOM 756 CG ASN A 113 186.974 31.046 541.092 1.00 68.29 C ANISOU 756 CG ASN A 113 8413 9567 7966 98 -175 -562 C ATOM 757 OD1 ASN A 113 187.205 30.476 542.159 1.00 74.90 O ANISOU 757 OD1 ASN A 113 9340 10461 8659 175 -226 -517 O ATOM 758 ND2 ASN A 113 186.296 32.184 541.024 1.00 75.09 N ANISOU 758 ND2 ASN A 113 9330 10373 8827 41 -128 -652 N ATOM 759 N LEU A 114 187.551 27.327 539.733 1.00 34.52 N ANISOU 759 N LEU A 114 3948 5264 3903 276 -62 -275 N ATOM 760 CA LEU A 114 187.183 25.998 540.213 1.00 36.31 C ANISOU 760 CA LEU A 114 4252 5450 4092 371 7 -161 C ATOM 761 C LEU A 114 188.413 25.219 540.661 1.00 38.98 C ANISOU 761 C LEU A 114 4560 5853 4399 468 -120 -90 C ATOM 762 O LEU A 114 188.374 24.510 541.676 1.00 43.80 O ANISOU 762 O LEU A 114 5285 6468 4887 559 -129 3 O ATOM 763 CB LEU A 114 186.431 25.237 539.122 1.00 35.20 C ANISOU 763 CB LEU A 114 4066 5206 4101 357 145 -133 C ATOM 764 CG LEU A 114 185.124 25.868 538.644 1.00 36.90 C ANISOU 764 CG LEU A 114 4297 5361 4362 276 264 -190 C ATOM 765 CD1 LEU A 114 184.480 25.014 537.564 1.00 36.54 C ANISOU 765 CD1 LEU A 114 4198 5224 4462 262 367 -170 C ATOM 766 CD2 LEU A 114 184.177 26.069 539.814 1.00 27.72 C ANISOU 766 CD2 LEU A 114 3273 4191 3070 290 339 -166 C ATOM 767 N LEU A 115 189.517 25.342 539.919 1.00 34.60 N ANISOU 767 N LEU A 115 3844 5351 3949 458 -212 -123 N ATOM 768 CA LEU A 115 190.767 24.726 540.354 1.00 44.84 C ANISOU 768 CA LEU A 115 5080 6729 5229 559 -350 -64 C ATOM 769 C LEU A 115 191.210 25.276 541.704 1.00 42.15 C ANISOU 769 C LEU A 115 4817 6490 4707 579 -506 -77 C ATOM 770 O LEU A 115 191.680 24.524 542.567 1.00 48.56 O ANISOU 770 O LEU A 115 5686 7345 5419 698 -591 14 O ATOM 771 CB LEU A 115 191.855 24.945 539.302 1.00 49.77 C ANISOU 771 CB LEU A 115 5494 7408 6008 531 -407 -110 C ATOM 772 CG LEU A 115 191.660 24.256 537.950 1.00 48.29 C ANISOU 772 CG LEU A 115 5231 7139 5979 542 -272 -99 C ATOM 773 CD1 LEU A 115 192.713 24.720 536.955 1.00 44.72 C ANISOU 773 CD1 LEU A 115 4578 6759 5653 502 -311 -153 C ATOM 774 CD2 LEU A 115 191.703 22.746 538.109 1.00 34.23 C ANISOU 774 CD2 LEU A 115 3499 5293 4214 684 -234 8 C ATOM 775 N ILE A 116 191.060 26.589 541.908 1.00 32.80 N ANISOU 775 N ILE A 116 3652 5339 3472 469 -552 -190 N ATOM 776 CA ILE A 116 191.446 27.201 543.177 1.00 33.92 C ANISOU 776 CA ILE A 116 3885 5573 3430 477 -711 -232 C ATOM 777 C ILE A 116 190.615 26.633 544.320 1.00 41.70 C ANISOU 777 C ILE A 116 5093 6536 4214 572 -647 -151 C ATOM 778 O ILE A 116 191.143 26.323 545.396 1.00 42.10 O ANISOU 778 O ILE A 116 5227 6670 4099 665 -780 -103 O ATOM 779 CB ILE A 116 191.321 28.734 543.091 1.00 33.59 C ANISOU 779 CB ILE A 116 3841 5533 3389 334 -749 -384 C ATOM 780 CG1 ILE A 116 192.461 29.319 542.256 1.00 39.11 C ANISOU 780 CG1 ILE A 116 4320 6283 4259 242 -857 -448 C ATOM 781 CG2 ILE A 116 191.307 29.353 544.479 1.00 35.34 C ANISOU 781 CG2 ILE A 116 4227 5816 3386 346 -870 -446 C ATOM 782 CD1 ILE A 116 192.384 30.822 542.087 1.00 36.66 C ANISOU 782 CD1 ILE A 116 4007 5946 3977 91 -889 -586 C ATOM 783 N ILE A 117 189.306 26.482 544.108 1.00 37.70 N ANISOU 783 N ILE A 117 4683 5925 3718 552 -443 -128 N ATOM 784 CA ILE A 117 188.446 25.924 545.151 1.00 36.72 C ANISOU 784 CA ILE A 117 4761 5774 3416 633 -343 -36 C ATOM 785 C ILE A 117 188.845 24.484 545.453 1.00 49.41 C ANISOU 785 C ILE A 117 6395 7371 5006 764 -352 128 C ATOM 786 O ILE A 117 188.982 24.087 546.618 1.00 62.42 O ANISOU 786 O ILE A 117 8193 9071 6455 866 -407 213 O ATOM 787 CB ILE A 117 186.967 26.023 544.739 1.00 36.63 C ANISOU 787 CB ILE A 117 4801 5653 3466 575 -114 -41 C ATOM 788 CG1 ILE A 117 186.579 27.480 544.484 1.00 35.48 C ANISOU 788 CG1 ILE A 117 4640 5509 3333 468 -110 -197 C ATOM 789 CG2 ILE A 117 186.074 25.409 545.808 1.00 34.38 C ANISOU 789 CG2 ILE A 117 4708 5342 3012 651 18 68 C ATOM 790 CD1 ILE A 117 185.139 27.663 544.058 1.00 31.17 C ANISOU 790 CD1 ILE A 117 4118 4868 2856 422 99 -208 C ATOM 791 N SER A 118 189.047 23.683 544.403 1.00 50.95 N ANISOU 791 N SER A 118 6460 7495 5403 774 -299 177 N ATOM 792 CA SER A 118 189.374 22.272 544.592 1.00 44.60 C ANISOU 792 CA SER A 118 5689 6647 4612 905 -291 332 C ATOM 793 C SER A 118 190.684 22.105 545.354 1.00 49.67 C ANISOU 793 C SER A 118 6314 7415 5144 1019 -514 374 C ATOM 794 O SER A 118 190.762 21.331 546.317 1.00 55.52 O ANISOU 794 O SER A 118 7195 8161 5737 1146 -541 508 O ATOM 795 CB SER A 118 189.441 21.566 543.238 1.00 42.90 C ANISOU 795 CB SER A 118 5331 6331 4638 892 -208 339 C ATOM 796 OG SER A 118 188.211 21.682 542.542 1.00 37.52 O ANISOU 796 OG SER A 118 4662 5541 4053 789 -25 299 O ATOM 797 N PHE A 119 191.729 22.827 544.939 1.00 54.86 N ANISOU 797 N PHE A 119 6794 8175 5874 976 -678 268 N ATOM 798 CA PHE A 119 193.006 22.732 545.639 1.00 63.87 C ANISOU 798 CA PHE A 119 7884 9455 6930 1076 -914 295 C ATOM 799 C PHE A 119 192.921 23.300 547.051 1.00 61.08 C ANISOU 799 C PHE A 119 7710 9198 6301 1098 -1033 279 C ATOM 800 O PHE A 119 193.616 22.817 547.953 1.00 59.57 O ANISOU 800 O PHE A 119 7573 9096 5966 1231 -1194 363 O ATOM 801 CB PHE A 119 194.100 23.446 544.847 1.00 39.45 C ANISOU 801 CB PHE A 119 4536 6452 4000 1000 -1048 179 C ATOM 802 CG PHE A 119 194.688 22.616 543.744 1.00 42.89 C ANISOU 802 CG PHE A 119 4790 6847 4658 1058 -999 228 C ATOM 803 CD1 PHE A 119 195.586 21.600 544.030 1.00 44.92 C ANISOU 803 CD1 PHE A 119 4994 7145 4928 1231 -1102 342 C ATOM 804 CD2 PHE A 119 194.352 22.853 542.422 1.00 36.87 C ANISOU 804 CD2 PHE A 119 3919 6007 4081 954 -851 159 C ATOM 805 CE1 PHE A 119 196.133 20.833 543.019 1.00 42.37 C ANISOU 805 CE1 PHE A 119 4511 6780 4808 1301 -1045 376 C ATOM 806 CE2 PHE A 119 194.895 22.090 541.407 1.00 45.24 C ANISOU 806 CE2 PHE A 119 4830 7034 5325 1018 -797 192 C ATOM 807 CZ PHE A 119 195.787 21.079 541.706 1.00 45.20 C ANISOU 807 CZ PHE A 119 4771 7063 5339 1192 -887 296 C ATOM 808 N ASP A 120 192.083 24.317 547.260 1.00 55.72 N ANISOU 808 N ASP A 120 7130 8503 5536 981 -961 168 N ATOM 809 CA ASP A 120 191.916 24.878 548.597 1.00 56.26 C ANISOU 809 CA ASP A 120 7396 8656 5322 1007 -1053 135 C ATOM 810 C ASP A 120 191.310 23.851 549.546 1.00 51.90 C ANISOU 810 C ASP A 120 7072 8072 4576 1149 -953 311 C ATOM 811 O ASP A 120 191.795 23.661 550.669 1.00 46.39 O ANISOU 811 O ASP A 120 6503 7478 3647 1262 -1106 368 O ATOM 812 CB ASP A 120 191.047 26.135 548.531 1.00 63.83 C ANISOU 812 CB ASP A 120 8421 9580 6253 867 -958 -20 C ATOM 813 CG ASP A 120 190.805 26.750 549.897 1.00 68.51 C ANISOU 813 CG ASP A 120 9239 10250 6542 898 -1032 -76 C ATOM 814 OD1 ASP A 120 191.750 27.341 550.459 1.00 71.08 O ANISOU 814 OD1 ASP A 120 9549 10695 6764 894 -1279 -169 O ATOM 815 OD2 ASP A 120 189.670 26.642 550.406 1.00 64.22 O ANISOU 815 OD2 ASP A 120 8886 9652 5864 927 -842 -31 O ATOM 816 N ARG A 121 190.247 23.172 549.107 1.00 55.04 N ANISOU 816 N ARG A 121 7522 8325 5064 1142 -698 405 N ATOM 817 CA ARG A 121 189.644 22.137 549.941 1.00 55.17 C ANISOU 817 CA ARG A 121 7747 8289 4927 1261 -573 592 C ATOM 818 C ARG A 121 190.592 20.959 550.132 1.00 63.14 C ANISOU 818 C ARG A 121 8738 9310 5944 1420 -695 753 C ATOM 819 O ARG A 121 190.672 20.388 551.228 1.00 68.37 O ANISOU 819 O ARG A 121 9588 10010 6381 1556 -735 893 O ATOM 820 CB ARG A 121 188.325 21.675 549.324 1.00 54.40 C ANISOU 820 CB ARG A 121 7671 8026 4973 1193 -280 647 C ATOM 821 CG ARG A 121 187.572 20.653 550.153 1.00 64.48 C ANISOU 821 CG ARG A 121 9158 9226 6115 1286 -111 846 C ATOM 822 CD ARG A 121 187.119 21.233 551.479 1.00 80.41 C ANISOU 822 CD ARG A 121 11399 11338 7813 1323 -92 847 C ATOM 823 NE ARG A 121 186.332 20.271 552.242 1.00 83.98 N ANISOU 823 NE ARG A 121 12055 11715 8140 1402 106 1053 N ATOM 824 CZ ARG A 121 185.809 20.514 553.439 1.00 85.63 C ANISOU 824 CZ ARG A 121 12490 11990 8055 1456 182 1101 C ATOM 825 NH1 ARG A 121 185.106 19.576 554.058 1.00 92.82 N ANISOU 825 NH1 ARG A 121 13573 12822 8873 1520 386 1310 N ATOM 826 NH2 ARG A 121 185.988 21.694 554.016 1.00 86.66 N ANISOU 826 NH2 ARG A 121 12683 12260 7984 1445 63 940 N ATOM 827 N TYR A 122 191.322 20.585 549.076 1.00 59.90 N ANISOU 827 N TYR A 122 8108 8867 5782 1419 -750 738 N ATOM 828 CA TYR A 122 192.282 19.491 549.182 1.00 54.53 C ANISOU 828 CA TYR A 122 7388 8194 5135 1586 -868 880 C ATOM 829 C TYR A 122 193.352 19.793 550.224 1.00 59.63 C ANISOU 829 C TYR A 122 8059 9029 5570 1694 -1153 883 C ATOM 830 O TYR A 122 193.698 18.930 551.040 1.00 51.12 O ANISOU 830 O TYR A 122 7107 7969 4348 1868 -1228 1051 O ATOM 831 CB TYR A 122 192.917 19.223 547.816 1.00 51.30 C ANISOU 831 CB TYR A 122 6724 7738 5029 1562 -874 828 C ATOM 832 CG TYR A 122 194.011 18.178 547.829 1.00 57.67 C ANISOU 832 CG TYR A 122 7454 8558 5899 1747 -1003 953 C ATOM 833 CD1 TYR A 122 193.706 16.824 547.882 1.00 66.94 C ANISOU 833 CD1 TYR A 122 8747 9576 7111 1874 -879 1134 C ATOM 834 CD2 TYR A 122 195.349 18.546 547.773 1.00 52.55 C ANISOU 834 CD2 TYR A 122 6606 8070 5292 1794 -1244 890 C ATOM 835 CE1 TYR A 122 194.703 15.867 547.889 1.00 66.81 C ANISOU 835 CE1 TYR A 122 8666 9557 7160 2063 -993 1249 C ATOM 836 CE2 TYR A 122 196.352 17.596 547.780 1.00 59.79 C ANISOU 836 CE2 TYR A 122 7433 9005 6278 1982 -1361 1004 C ATOM 837 CZ TYR A 122 196.024 16.258 547.838 1.00 68.29 C ANISOU 837 CZ TYR A 122 8646 9920 7383 2126 -1234 1184 C ATOM 838 OH TYR A 122 197.020 15.308 547.844 1.00 81.98 O ANISOU 838 OH TYR A 122 10298 11659 9193 2332 -1347 1301 O ATOM 839 N PHE A 123 193.884 21.018 550.218 1.00 58.88 N ANISOU 839 N PHE A 123 7849 9069 5453 1591 -1323 699 N ATOM 840 CA PHE A 123 194.859 21.406 551.229 1.00 57.93 C ANISOU 840 CA PHE A 123 7748 9136 5129 1669 -1617 673 C ATOM 841 C PHE A 123 194.227 21.584 552.603 1.00 64.14 C ANISOU 841 C PHE A 123 8841 9969 5562 1723 -1616 715 C ATOM 842 O PHE A 123 194.929 21.473 553.613 1.00 72.18 O ANISOU 842 O PHE A 123 9944 11124 6356 1850 -1844 762 O ATOM 843 CB PHE A 123 195.573 22.691 550.807 1.00 65.77 C ANISOU 843 CB PHE A 123 8529 10239 6220 1518 -1792 454 C ATOM 844 CG PHE A 123 196.498 22.512 549.636 1.00 69.88 C ANISOU 844 CG PHE A 123 8737 10765 7049 1495 -1842 428 C ATOM 845 CD1 PHE A 123 197.175 21.318 549.447 1.00 67.60 C ANISOU 845 CD1 PHE A 123 8359 10469 6859 1667 -1880 580 C ATOM 846 CD2 PHE A 123 196.685 23.535 548.721 1.00 67.04 C ANISOU 846 CD2 PHE A 123 8180 10412 6879 1312 -1837 256 C ATOM 847 CE1 PHE A 123 198.026 21.149 548.371 1.00 66.26 C ANISOU 847 CE1 PHE A 123 7900 10309 6965 1661 -1905 552 C ATOM 848 CE2 PHE A 123 197.534 23.372 547.642 1.00 70.45 C ANISOU 848 CE2 PHE A 123 8329 10858 7581 1295 -1859 240 C ATOM 849 CZ PHE A 123 198.205 22.178 547.467 1.00 71.57 C ANISOU 849 CZ PHE A 123 8376 11003 7813 1472 -1889 383 C ATOM 850 N CYS A 124 192.921 21.856 552.665 1.00 65.50 N ANISOU 850 N CYS A 124 9176 10041 5672 1638 -1366 698 N ATOM 851 CA CYS A 124 192.252 21.926 553.959 1.00 67.88 C ANISOU 851 CA CYS A 124 9780 10382 5630 1706 -1318 757 C ATOM 852 C CYS A 124 192.111 20.544 554.587 1.00 75.09 C ANISOU 852 C CYS A 124 10869 11241 6421 1890 -1241 1022 C ATOM 853 O CYS A 124 192.236 20.398 555.808 1.00 78.87 O ANISOU 853 O CYS A 124 11569 11818 6580 2019 -1338 1109 O ATOM 854 CB CYS A 124 190.883 22.592 553.813 1.00 70.54 C ANISOU 854 CB CYS A 124 10216 10628 5960 1572 -1051 670 C ATOM 855 SG CYS A 124 190.923 24.402 553.785 1.00 84.73 S ANISOU 855 SG CYS A 124 11965 12511 7719 1405 -1167 370 S ATOM 856 N VAL A 125 191.854 19.517 553.771 1.00 75.24 N ANISOU 856 N VAL A 125 10807 11096 6683 1908 -1069 1154 N ATOM 857 CA VAL A 125 191.659 18.173 554.308 1.00 68.50 C ANISOU 857 CA VAL A 125 10130 10151 5745 2071 -971 1415 C ATOM 858 C VAL A 125 192.962 17.390 554.444 1.00 69.83 C ANISOU 858 C VAL A 125 10223 10380 5932 2256 -1215 1531 C ATOM 859 O VAL A 125 193.027 16.451 555.249 1.00 72.19 O ANISOU 859 O VAL A 125 10713 10654 6062 2431 -1219 1750 O ATOM 860 CB VAL A 125 190.669 17.365 553.448 1.00 63.66 C ANISOU 860 CB VAL A 125 9499 9308 5382 2002 -659 1508 C ATOM 861 CG1 VAL A 125 189.301 18.045 553.417 1.00 69.38 C ANISOU 861 CG1 VAL A 125 10301 9979 6080 1842 -410 1422 C ATOM 862 CG2 VAL A 125 191.217 17.167 552.047 1.00 62.69 C ANISOU 862 CG2 VAL A 125 9095 9112 5613 1948 -691 1425 C ATOM 863 N THR A 126 194.000 17.743 553.686 1.00 66.44 N ANISOU 863 N THR A 126 9514 10026 5703 2229 -1412 1400 N ATOM 864 CA THR A 126 195.264 17.021 553.759 1.00 66.82 C ANISOU 864 CA THR A 126 9451 10140 5797 2413 -1643 1501 C ATOM 865 C THR A 126 196.287 17.687 554.666 1.00 74.46 C ANISOU 865 C THR A 126 10401 11352 6540 2485 -1991 1430 C ATOM 866 O THR A 126 197.197 17.003 555.148 1.00 79.95 O ANISOU 866 O THR A 126 11085 12123 7168 2684 -2195 1563 O ATOM 867 CB THR A 126 195.877 16.854 552.362 1.00 69.54 C ANISOU 867 CB THR A 126 9480 10427 6515 2368 -1641 1422 C ATOM 868 OG1 THR A 126 196.035 18.139 551.749 1.00 70.55 O ANISOU 868 OG1 THR A 126 9413 10647 6748 2172 -1699 1179 O ATOM 869 CG2 THR A 126 194.995 15.970 551.489 1.00 78.76 C ANISOU 869 CG2 THR A 126 10676 11348 7900 2334 -1334 1508 C ATOM 870 N LYS A 127 196.165 18.990 554.909 1.00 74.91 N ANISOU 870 N LYS A 127 10453 11526 6483 2332 -2073 1222 N ATOM 871 CA LYS A 127 197.094 19.733 555.760 1.00 73.86 C ANISOU 871 CA LYS A 127 10304 11621 6140 2367 -2419 1116 C ATOM 872 C LYS A 127 196.304 20.528 556.793 1.00 80.23 C ANISOU 872 C LYS A 127 11397 12485 6601 2312 -2389 1038 C ATOM 873 O LYS A 127 196.202 21.757 556.706 1.00 81.17 O ANISOU 873 O LYS A 127 11469 12661 6712 2142 -2439 810 O ATOM 874 CB LYS A 127 197.984 20.653 554.924 1.00 64.68 C ANISOU 874 CB LYS A 127 8801 10549 5226 2219 -2595 897 C ATOM 875 CG LYS A 127 198.748 19.944 553.817 1.00 63.22 C ANISOU 875 CG LYS A 127 8317 10313 5389 2268 -2593 955 C ATOM 876 CD LYS A 127 199.556 20.925 552.982 1.00 70.03 C ANISOU 876 CD LYS A 127 8847 11266 6494 2102 -2728 744 C ATOM 877 CE LYS A 127 200.300 20.211 551.865 1.00 77.90 C ANISOU 877 CE LYS A 127 9552 12221 7825 2164 -2696 803 C ATOM 878 NZ LYS A 127 201.072 21.155 551.010 1.00 73.69 N ANISOU 878 NZ LYS A 127 8690 11775 7535 1995 -2794 615 N ATOM 879 N PRO A 128 195.731 19.852 557.795 1.00 78.76 N ANISOU 879 N PRO A 128 11512 12261 6151 2435 -2280 1221 N ATOM 880 CA PRO A 128 194.915 20.571 558.786 1.00 82.65 C ANISOU 880 CA PRO A 128 12271 12781 6351 2362 -2190 1142 C ATOM 881 C PRO A 128 195.730 21.393 559.767 1.00 81.88 C ANISOU 881 C PRO A 128 12187 12843 6081 2314 -2483 986 C ATOM 882 O PRO A 128 195.187 22.335 560.358 1.00 78.97 O ANISOU 882 O PRO A 128 11973 12509 5524 2214 -2445 835 O ATOM 883 CB PRO A 128 194.156 19.444 559.508 1.00 83.71 C ANISOU 883 CB PRO A 128 12678 12804 6325 2490 -1958 1407 C ATOM 884 CG PRO A 128 194.382 18.202 558.677 1.00 78.76 C ANISOU 884 CG PRO A 128 11933 12051 5942 2605 -1885 1609 C ATOM 885 CD PRO A 128 195.708 18.399 558.023 1.00 75.15 C ANISOU 885 CD PRO A 128 11158 11692 5702 2613 -2179 1502 C ATOM 886 N LEU A 129 197.008 21.073 559.962 1.00 84.65 N ANISOU 886 N LEU A 129 12377 13286 6500 2380 -2767 1016 N ATOM 887 CA LEU A 129 197.839 21.738 560.955 1.00 82.29 C ANISOU 887 CA LEU A 129 12090 13139 6036 2340 -3058 894 C ATOM 888 C LEU A 129 198.684 22.864 560.374 1.00 78.14 C ANISOU 888 C LEU A 129 11281 12703 5705 2168 -3288 642 C ATOM 889 O LEU A 129 199.420 23.515 561.123 1.00 82.36 O ANISOU 889 O LEU A 129 11801 13359 6133 2105 -3541 521 O ATOM 890 CB LEU A 129 198.751 20.716 561.641 1.00 89.37 C ANISOU 890 CB LEU A 129 12987 14092 6876 2513 -3242 1089 C ATOM 891 CG LEU A 129 198.065 19.489 562.247 1.00 91.52 C ANISOU 891 CG LEU A 129 13529 14263 6981 2686 -3032 1366 C ATOM 892 CD1 LEU A 129 199.094 18.514 562.799 1.00 93.49 C ANISOU 892 CD1 LEU A 129 13742 14564 7215 2857 -3241 1548 C ATOM 893 CD2 LEU A 129 197.081 19.903 563.329 1.00 90.45 C ANISOU 893 CD2 LEU A 129 13726 14136 6503 2656 -2883 1347 C ATOM 894 N THR A 130 198.599 23.112 559.076 1.00 83.10 N ANISOU 894 N THR A 130 11687 13272 6616 2084 -3203 563 N ATOM 895 CA THR A 130 199.448 24.113 558.437 1.00 87.30 C ANISOU 895 CA THR A 130 11923 13872 7376 1910 -3400 346 C ATOM 896 C THR A 130 198.691 25.017 557.477 1.00 89.82 C ANISOU 896 C THR A 130 12186 14115 7826 1748 -3231 172 C ATOM 897 O THR A 130 198.933 26.226 557.462 1.00 88.31 O ANISOU 897 O THR A 130 11925 13957 7674 1565 -3345 -50 O ATOM 898 CB THR A 130 200.603 23.416 557.693 1.00 87.35 C ANISOU 898 CB THR A 130 11598 13912 7679 1978 -3536 435 C ATOM 899 OG1 THR A 130 201.381 22.652 558.622 1.00103.17 O ANISOU 899 OG1 THR A 130 13644 15992 9565 2127 -3719 585 O ATOM 900 CG2 THR A 130 201.501 24.435 557.012 1.00 75.75 C ANISOU 900 CG2 THR A 130 9803 12507 6469 1782 -3710 228 C ATOM 901 N TYR A 131 197.774 24.466 556.678 1.00 88.34 N ANISOU 901 N TYR A 131 12033 13821 7713 1806 -2962 272 N ATOM 902 CA TYR A 131 197.111 25.277 555.660 1.00 80.23 C ANISOU 902 CA TYR A 131 10910 12690 6885 1621 -2773 121 C ATOM 903 C TYR A 131 196.107 26.269 556.241 1.00 74.39 C ANISOU 903 C TYR A 131 10425 11918 5922 1523 -2662 -27 C ATOM 904 O TYR A 131 196.115 27.436 555.814 1.00 81.98 O ANISOU 904 O TYR A 131 11290 12859 7000 1338 -2691 -240 O ATOM 905 CB TYR A 131 196.463 24.368 554.612 1.00 89.40 C ANISOU 905 CB TYR A 131 11997 13673 8299 1634 -2456 275 C ATOM 906 CG TYR A 131 195.822 25.120 553.468 1.00 85.00 C ANISOU 906 CG TYR A 131 11314 12985 7996 1430 -2244 139 C ATOM 907 CD1 TYR A 131 196.596 25.702 552.474 1.00 76.08 C ANISOU 907 CD1 TYR A 131 9883 11873 7153 1296 -2338 14 C ATOM 908 CD2 TYR A 131 194.442 25.245 553.381 1.00 77.25 C ANISOU 908 CD2 TYR A 131 10513 11869 6971 1376 -1946 145 C ATOM 909 CE1 TYR A 131 196.015 26.391 551.426 1.00 70.09 C ANISOU 909 CE1 TYR A 131 9027 10995 6609 1121 -2147 -95 C ATOM 910 CE2 TYR A 131 193.851 25.931 552.337 1.00 69.16 C ANISOU 910 CE2 TYR A 131 9374 10731 6172 1206 -1770 29 C ATOM 911 CZ TYR A 131 194.642 26.502 551.362 1.00 71.74 C ANISOU 911 CZ TYR A 131 9424 11073 6761 1082 -1874 -88 C ATOM 912 OH TYR A 131 194.058 27.186 550.320 1.00 79.23 O ANISOU 912 OH TYR A 131 10276 11909 7917 924 -1701 -189 O ATOM 913 N PRO A 132 195.224 25.897 557.179 1.00 70.11 N ANISOU 913 N PRO A 132 10207 11362 5071 1639 -2520 77 N ATOM 914 CA PRO A 132 194.199 26.860 557.626 1.00 62.13 C ANISOU 914 CA PRO A 132 9420 10309 3876 1551 -2371 -71 C ATOM 915 C PRO A 132 194.750 28.132 558.253 1.00 64.11 C ANISOU 915 C PRO A 132 9685 10629 4046 1416 -2598 -313 C ATOM 916 O PRO A 132 194.027 29.135 558.299 1.00 63.43 O ANISOU 916 O PRO A 132 9709 10483 3908 1308 -2487 -484 O ATOM 917 CB PRO A 132 193.379 26.051 558.641 1.00 64.59 C ANISOU 917 CB PRO A 132 10042 10599 3899 1703 -2180 123 C ATOM 918 CG PRO A 132 193.563 24.643 558.226 1.00 65.24 C ANISOU 918 CG PRO A 132 10052 10645 4093 1845 -2119 381 C ATOM 919 CD PRO A 132 194.982 24.562 557.756 1.00 69.60 C ANISOU 919 CD PRO A 132 10316 11287 4844 1846 -2427 346 C ATOM 920 N VAL A 133 195.993 28.136 558.737 1.00 68.46 N ANISOU 920 N VAL A 133 10122 11286 4604 1409 -2899 -331 N ATOM 921 CA VAL A 133 196.518 29.356 559.344 1.00 68.90 C ANISOU 921 CA VAL A 133 10189 11391 4598 1258 -3106 -558 C ATOM 922 C VAL A 133 196.900 30.377 558.275 1.00 76.29 C ANISOU 922 C VAL A 133 10871 12281 5835 1055 -3175 -758 C ATOM 923 O VAL A 133 196.876 31.586 558.532 1.00 77.02 O ANISOU 923 O VAL A 133 11015 12345 5905 900 -3235 -970 O ATOM 924 CB VAL A 133 197.703 29.036 560.275 1.00 72.76 C ANISOU 924 CB VAL A 133 10644 12018 4982 1310 -3405 -508 C ATOM 925 CG1 VAL A 133 198.943 28.666 559.478 1.00 80.08 C ANISOU 925 CG1 VAL A 133 11213 13001 6213 1290 -3605 -463 C ATOM 926 CG2 VAL A 133 197.986 30.212 561.202 1.00 75.64 C ANISOU 926 CG2 VAL A 133 11120 12435 5184 1179 -3577 -723 C ATOM 927 N LYS A 134 197.244 29.924 557.071 1.00 81.70 N ANISOU 927 N LYS A 134 11284 12950 6810 1052 -3156 -692 N ATOM 928 CA LYS A 134 197.533 30.813 555.954 1.00 83.88 C ANISOU 928 CA LYS A 134 11309 13172 7388 861 -3179 -855 C ATOM 929 C LYS A 134 196.309 31.086 555.092 1.00 85.90 C ANISOU 929 C LYS A 134 11618 13285 7735 813 -2872 -885 C ATOM 930 O LYS A 134 196.409 31.835 554.115 1.00 93.01 O ANISOU 930 O LYS A 134 12328 14097 8913 637 -2824 -995 O ATOM 931 CB LYS A 134 198.650 30.226 555.085 1.00 89.28 C ANISOU 931 CB LYS A 134 11635 13917 8371 864 -3304 -767 C ATOM 932 CG LYS A 134 199.964 30.012 555.815 1.00108.91 C ANISOU 932 CG LYS A 134 14009 16525 10845 881 -3591 -729 C ATOM 933 CD LYS A 134 200.986 29.335 554.916 1.00117.67 C ANISOU 933 CD LYS A 134 14762 17685 12261 910 -3665 -622 C ATOM 934 CE LYS A 134 200.465 28.004 554.401 1.00117.62 C ANISOU 934 CE LYS A 134 14769 17650 12269 1120 -3474 -412 C ATOM 935 NZ LYS A 134 200.065 27.103 555.514 1.00124.00 N ANISOU 935 NZ LYS A 134 15866 18481 12767 1324 -3458 -246 N ATOM 936 N ARG A 135 195.163 30.497 555.430 1.00 81.19 N ANISOU 936 N ARG A 135 11259 12622 6968 930 -2611 -759 N ATOM 937 CA ARG A 135 193.936 30.639 554.649 1.00 72.80 C ANISOU 937 CA ARG A 135 10225 11385 6049 865 -2261 -741 C ATOM 938 C ARG A 135 193.209 31.886 555.135 1.00 76.24 C ANISOU 938 C ARG A 135 10866 11770 6332 781 -2210 -945 C ATOM 939 O ARG A 135 192.331 31.826 555.996 1.00 81.11 O ANISOU 939 O ARG A 135 11761 12386 6672 878 -2076 -927 O ATOM 940 CB ARG A 135 193.079 29.386 554.784 1.00 66.97 C ANISOU 940 CB ARG A 135 9618 10599 5228 1020 -2008 -506 C ATOM 941 CG ARG A 135 191.881 29.324 553.856 1.00 64.83 C ANISOU 941 CG ARG A 135 9321 10159 5152 957 -1663 -463 C ATOM 942 CD ARG A 135 191.221 27.957 553.945 1.00 62.65 C ANISOU 942 CD ARG A 135 9133 9835 4838 1094 -1448 -221 C ATOM 943 NE ARG A 135 190.069 27.833 553.058 1.00 61.13 N ANISOU 943 NE ARG A 135 8898 9487 4840 1029 -1136 -181 N ATOM 944 CZ ARG A 135 188.810 28.018 553.440 1.00 61.64 C ANISOU 944 CZ ARG A 135 9145 9490 4785 1038 -897 -177 C ATOM 945 NH1 ARG A 135 188.534 28.336 554.697 1.00 54.85 N ANISOU 945 NH1 ARG A 135 8541 8706 3594 1115 -915 -209 N ATOM 946 NH2 ARG A 135 187.825 27.882 552.564 1.00 74.03 N ANISOU 946 NH2 ARG A 135 10638 10929 6561 974 -641 -143 N ATOM 947 N THR A 136 193.583 33.031 554.575 1.00 78.00 N ANISOU 947 N THR A 136 10954 11944 6740 602 -2306 -1139 N ATOM 948 CA THR A 136 193.032 34.322 554.963 1.00 83.44 C ANISOU 948 CA THR A 136 11820 12562 7320 512 -2286 -1358 C ATOM 949 C THR A 136 192.350 34.977 553.761 1.00 81.64 C ANISOU 949 C THR A 136 11476 12158 7386 377 -2058 -1407 C ATOM 950 O THR A 136 192.238 34.389 552.682 1.00 87.43 O ANISOU 950 O THR A 136 12012 12834 8372 358 -1910 -1271 O ATOM 951 CB THR A 136 194.127 35.222 555.542 1.00 86.79 C ANISOU 951 CB THR A 136 12224 13063 7687 408 -2630 -1557 C ATOM 952 OG1 THR A 136 195.174 35.384 554.578 1.00 82.17 O ANISOU 952 OG1 THR A 136 11311 12492 7419 274 -2790 -1583 O ATOM 953 CG2 THR A 136 194.701 34.613 556.814 1.00 90.65 C ANISOU 953 CG2 THR A 136 12830 13687 7925 516 -2792 -1467 C ATOM 954 N THR A 137 191.892 36.215 553.961 1.00 80.42 N ANISOU 954 N THR A 137 11457 11913 7187 290 -2037 -1608 N ATOM 955 CA THR A 137 191.206 36.948 552.903 1.00 83.89 C ANISOU 955 CA THR A 137 11815 12180 7880 176 -1834 -1660 C ATOM 956 C THR A 137 192.185 37.489 551.867 1.00 86.79 C ANISOU 956 C THR A 137 11905 12506 8566 -6 -1974 -1717 C ATOM 957 O THR A 137 191.939 37.382 550.659 1.00 88.86 O ANISOU 957 O THR A 137 11990 12679 9093 -64 -1811 -1632 O ATOM 958 CB THR A 137 190.384 38.089 553.507 1.00 82.79 C ANISOU 958 CB THR A 137 11928 11945 7583 165 -1759 -1852 C ATOM 959 OG1 THR A 137 189.298 37.547 554.270 1.00 77.88 O ANISOU 959 OG1 THR A 137 11536 11348 6705 335 -1549 -1770 O ATOM 960 CG2 THR A 137 189.831 38.994 552.417 1.00 88.26 C ANISOU 960 CG2 THR A 137 12530 12453 8550 44 -1599 -1919 C ATOM 961 N LYS A 138 193.298 38.069 552.323 1.00 81.35 N ANISOU 961 N LYS A 138 11172 11885 7853 -100 -2275 -1860 N ATOM 962 CA LYS A 138 194.285 38.620 551.399 1.00 74.11 C ANISOU 962 CA LYS A 138 9980 10935 7244 -287 -2406 -1912 C ATOM 963 C LYS A 138 194.844 37.543 550.477 1.00 76.25 C ANISOU 963 C LYS A 138 9969 11276 7726 -259 -2366 -1709 C ATOM 964 O LYS A 138 195.040 37.781 549.279 1.00 71.79 O ANISOU 964 O LYS A 138 9194 10633 7449 -374 -2278 -1677 O ATOM 965 CB LYS A 138 195.406 39.297 552.190 1.00 66.60 C ANISOU 965 CB LYS A 138 9022 10066 6217 -387 -2756 -2095 C ATOM 966 CG LYS A 138 196.614 39.704 551.367 1.00 74.30 C ANISOU 966 CG LYS A 138 9677 11033 7519 -585 -2897 -2106 C ATOM 967 CD LYS A 138 197.603 40.492 552.213 1.00 92.73 C ANISOU 967 CD LYS A 138 12025 13384 9825 -729 -3136 -2214 C ATOM 968 CE LYS A 138 198.937 40.655 551.506 1.00104.16 C ANISOU 968 CE LYS A 138 13129 14866 11580 -902 -3278 -2178 C ATOM 969 NZ LYS A 138 199.633 39.349 551.339 1.00109.46 N ANISOU 969 NZ LYS A 138 13581 15719 12290 -775 -3350 -1998 N ATOM 970 N MET A 139 195.094 36.348 551.016 1.00 72.99 N ANISOU 970 N MET A 139 9563 11005 7166 -97 -2422 -1567 N ATOM 971 CA MET A 139 195.609 35.256 550.196 1.00 69.37 C ANISOU 971 CA MET A 139 8858 10603 6895 -45 -2379 -1379 C ATOM 972 C MET A 139 194.607 34.850 549.120 1.00 66.69 C ANISOU 972 C MET A 139 8493 10136 6710 -24 -2055 -1258 C ATOM 973 O MET A 139 194.977 34.657 547.955 1.00 66.77 O ANISOU 973 O MET A 139 8270 10117 6982 -87 -1987 -1192 O ATOM 974 CB MET A 139 195.968 34.067 551.090 1.00 73.54 C ANISOU 974 CB MET A 139 9444 11285 7211 146 -2497 -1248 C ATOM 975 CG MET A 139 196.246 32.765 550.357 1.00 84.58 C ANISOU 975 CG MET A 139 10657 12716 8766 250 -2403 -1036 C ATOM 976 SD MET A 139 194.806 31.679 550.330 0.53 90.02 S ANISOU 976 SD MET A 139 11546 13310 9346 412 -2072 -852 S ATOM 977 CE MET A 139 195.552 30.142 549.795 1.00 97.46 C ANISOU 977 CE MET A 139 12283 14315 10432 548 -2082 -636 C ATOM 978 N ALA A 140 193.330 34.724 549.491 1.00 62.17 N ANISOU 978 N ALA A 140 8153 9491 5976 63 -1852 -1231 N ATOM 979 CA ALA A 140 192.305 34.380 548.512 1.00 51.19 C ANISOU 979 CA ALA A 140 6737 7983 4730 76 -1561 -1131 C ATOM 980 C ALA A 140 192.183 35.457 547.441 1.00 49.83 C ANISOU 980 C ALA A 140 6454 7686 4792 -88 -1491 -1228 C ATOM 981 O ALA A 140 192.010 35.149 546.255 1.00 51.43 O ANISOU 981 O ALA A 140 6505 7831 5206 -116 -1347 -1142 O ATOM 982 CB ALA A 140 190.965 34.161 549.214 1.00 43.04 C ANISOU 982 CB ALA A 140 5962 6906 3485 188 -1366 -1099 C ATOM 983 N GLY A 141 192.275 36.727 547.841 1.00 46.27 N ANISOU 983 N GLY A 141 6094 7187 4302 -193 -1593 -1409 N ATOM 984 CA GLY A 141 192.232 37.801 546.862 1.00 50.79 C ANISOU 984 CA GLY A 141 6575 7626 5097 -350 -1538 -1493 C ATOM 985 C GLY A 141 193.406 37.762 545.903 1.00 65.38 C ANISOU 985 C GLY A 141 8135 9510 7195 -466 -1634 -1453 C ATOM 986 O GLY A 141 193.249 38.003 544.703 1.00 59.87 O ANISOU 986 O GLY A 141 7314 8724 6709 -540 -1497 -1410 O ATOM 987 N MET A 142 194.600 37.454 546.418 1.00 73.39 N ANISOU 987 N MET A 142 9036 10663 8185 -474 -1868 -1463 N ATOM 988 CA MET A 142 195.768 37.345 545.548 1.00 62.40 C ANISOU 988 CA MET A 142 7345 9327 7037 -571 -1949 -1417 C ATOM 989 C MET A 142 195.634 36.169 544.588 1.00 50.76 C ANISOU 989 C MET A 142 5732 7876 5677 -470 -1773 -1232 C ATOM 990 O MET A 142 196.052 36.260 543.427 1.00 52.68 O ANISOU 990 O MET A 142 5773 8094 6148 -553 -1699 -1187 O ATOM 991 CB MET A 142 197.040 37.217 546.386 1.00 64.00 C ANISOU 991 CB MET A 142 7444 9689 7185 -583 -2250 -1467 C ATOM 992 CG MET A 142 197.391 38.469 547.174 1.00 74.89 C ANISOU 992 CG MET A 142 8916 11040 8499 -725 -2459 -1677 C ATOM 993 SD MET A 142 198.988 38.359 548.006 0.52 78.44 S ANISOU 993 SD MET A 142 9185 11690 8929 -765 -2846 -1744 S ATOM 994 CE MET A 142 198.719 36.953 549.082 1.00 69.39 C ANISOU 994 CE MET A 142 8200 10699 7465 -487 -2894 -1618 C ATOM 995 N MET A 143 195.051 35.059 545.050 1.00 51.92 N ANISOU 995 N MET A 143 5995 8066 5666 -292 -1698 -1123 N ATOM 996 CA MET A 143 194.825 33.928 544.154 1.00 55.04 C ANISOU 996 CA MET A 143 6288 8457 6169 -197 -1525 -963 C ATOM 997 C MET A 143 193.820 34.276 543.061 1.00 64.35 C ANISOU 997 C MET A 143 7489 9493 7468 -251 -1286 -951 C ATOM 998 O MET A 143 194.034 33.948 541.887 1.00 69.78 O ANISOU 998 O MET A 143 8012 10164 8338 -272 -1186 -881 O ATOM 999 CB MET A 143 194.354 32.710 544.947 1.00 59.38 C ANISOU 999 CB MET A 143 6981 9055 6527 -9 -1492 -850 C ATOM 1000 CG MET A 143 195.479 31.816 545.442 1.00 68.00 C ANISOU 1000 CG MET A 143 7959 10291 7586 94 -1678 -773 C ATOM 1001 SD MET A 143 194.867 30.307 546.218 1.00 82.05 S ANISOU 1001 SD MET A 143 9919 12091 9165 319 -1600 -603 S ATOM 1002 CE MET A 143 196.372 29.343 546.321 1.00 86.46 C ANISOU 1002 CE MET A 143 10264 12799 9788 431 -1809 -505 C ATOM 1003 N ILE A 144 192.721 34.941 543.426 1.00 67.92 N ANISOU 1003 N ILE A 144 8145 9847 7815 -263 -1194 -1021 N ATOM 1004 CA ILE A 144 191.709 35.309 542.437 1.00 66.36 C ANISOU 1004 CA ILE A 144 7969 9519 7725 -300 -984 -1010 C ATOM 1005 C ILE A 144 192.292 36.274 541.411 1.00 66.58 C ANISOU 1005 C ILE A 144 7848 9492 7958 -456 -999 -1060 C ATOM 1006 O ILE A 144 192.138 36.089 540.196 1.00 70.88 O ANISOU 1006 O ILE A 144 8283 9995 8652 -475 -867 -989 O ATOM 1007 CB ILE A 144 190.472 35.903 543.134 1.00 68.33 C ANISOU 1007 CB ILE A 144 8454 9684 7823 -269 -895 -1082 C ATOM 1008 CG1 ILE A 144 189.745 34.825 543.943 1.00 74.03 C ANISOU 1008 CG1 ILE A 144 9311 10452 8365 -113 -815 -995 C ATOM 1009 CG2 ILE A 144 189.541 36.544 542.116 1.00 65.90 C ANISOU 1009 CG2 ILE A 144 8150 9244 7646 -319 -720 -1092 C ATOM 1010 CD1 ILE A 144 188.558 35.343 544.724 1.00 81.94 C ANISOU 1010 CD1 ILE A 144 10535 11392 9205 -67 -711 -1060 C ATOM 1011 N ALA A 145 192.973 37.320 541.889 1.00 58.81 N ANISOU 1011 N ALA A 145 6864 8502 6979 -575 -1160 -1183 N ATOM 1012 CA ALA A 145 193.584 38.284 540.979 1.00 39.24 C ANISOU 1012 CA ALA A 145 4246 5960 4705 -742 -1171 -1222 C ATOM 1013 C ALA A 145 194.605 37.613 540.070 1.00 36.04 C ANISOU 1013 C ALA A 145 3579 5647 4466 -761 -1173 -1119 C ATOM 1014 O ALA A 145 194.674 37.914 538.872 1.00 51.36 O ANISOU 1014 O ALA A 145 5412 7531 6570 -834 -1056 -1073 O ATOM 1015 CB ALA A 145 194.231 39.418 541.772 1.00 38.63 C ANISOU 1015 CB ALA A 145 4208 5859 4609 -876 -1368 -1379 C ATOM 1016 N ALA A 146 195.404 36.694 540.620 1.00 42.17 N ANISOU 1016 N ALA A 146 4257 6569 5195 -681 -1300 -1077 N ATOM 1017 CA ALA A 146 196.359 35.961 539.797 1.00 46.85 C ANISOU 1017 CA ALA A 146 4599 7257 5944 -667 -1289 -978 C ATOM 1018 C ALA A 146 195.648 35.145 538.726 1.00 50.91 C ANISOU 1018 C ALA A 146 5110 7728 6504 -572 -1064 -864 C ATOM 1019 O ALA A 146 196.127 35.044 537.589 1.00 47.88 O ANISOU 1019 O ALA A 146 4557 7355 6279 -610 -975 -807 O ATOM 1020 CB ALA A 146 197.227 35.060 540.674 1.00 38.62 C ANISOU 1020 CB ALA A 146 3473 6372 4827 -562 -1469 -948 C ATOM 1021 N ALA A 147 194.496 34.561 539.067 1.00 53.84 N ANISOU 1021 N ALA A 147 5669 8052 6736 -453 -968 -833 N ATOM 1022 CA ALA A 147 193.739 33.789 538.087 1.00 39.60 C ANISOU 1022 CA ALA A 147 3872 6198 4976 -374 -773 -742 C ATOM 1023 C ALA A 147 193.234 34.678 536.957 1.00 44.29 C ANISOU 1023 C ALA A 147 4463 6686 5678 -477 -641 -761 C ATOM 1024 O ALA A 147 193.397 34.353 535.775 1.00 56.58 O ANISOU 1024 O ALA A 147 5908 8243 7346 -477 -534 -699 O ATOM 1025 CB ALA A 147 192.576 33.070 538.772 1.00 38.94 C ANISOU 1025 CB ALA A 147 3982 6079 4736 -250 -702 -710 C ATOM 1026 N TRP A 148 192.619 35.814 537.302 1.00 43.22 N ANISOU 1026 N TRP A 148 4462 6456 5502 -556 -647 -845 N ATOM 1027 CA TRP A 148 192.091 36.702 536.269 1.00 40.56 C ANISOU 1027 CA TRP A 148 4143 6008 5261 -638 -529 -851 C ATOM 1028 C TRP A 148 193.203 37.252 535.382 1.00 53.08 C ANISOU 1028 C TRP A 148 5547 7611 7011 -765 -544 -835 C ATOM 1029 O TRP A 148 193.066 37.290 534.152 1.00 48.20 O ANISOU 1029 O TRP A 148 4872 6959 6481 -781 -414 -773 O ATOM 1030 CB TRP A 148 191.296 37.841 536.907 1.00 32.07 C ANISOU 1030 CB TRP A 148 3249 4819 4117 -684 -542 -950 C ATOM 1031 CG TRP A 148 189.916 37.438 537.340 1.00 41.80 C ANISOU 1031 CG TRP A 148 4648 6011 5225 -564 -446 -945 C ATOM 1032 CD1 TRP A 148 189.537 37.008 538.579 1.00 42.46 C ANISOU 1032 CD1 TRP A 148 4853 6132 5147 -477 -488 -973 C ATOM 1033 CD2 TRP A 148 188.733 37.426 536.532 1.00 43.94 C ANISOU 1033 CD2 TRP A 148 4969 6202 5525 -518 -288 -903 C ATOM 1034 NE1 TRP A 148 188.191 36.730 538.592 1.00 35.25 N ANISOU 1034 NE1 TRP A 148 4053 5166 4176 -388 -348 -948 N ATOM 1035 CE2 TRP A 148 187.674 36.979 537.348 1.00 44.29 C ANISOU 1035 CE2 TRP A 148 5146 6241 5443 -413 -234 -910 C ATOM 1036 CE3 TRP A 148 188.466 37.751 535.199 1.00 48.16 C ANISOU 1036 CE3 TRP A 148 5447 6677 6174 -553 -189 -856 C ATOM 1037 CZ2 TRP A 148 186.370 36.849 536.874 1.00 55.42 C ANISOU 1037 CZ2 TRP A 148 6607 7588 6861 -351 -93 -879 C ATOM 1038 CZ3 TRP A 148 187.170 37.622 534.730 1.00 48.08 C ANISOU 1038 CZ3 TRP A 148 5506 6609 6154 -481 -68 -828 C ATOM 1039 CH2 TRP A 148 186.139 37.175 535.565 1.00 49.92 C ANISOU 1039 CH2 TRP A 148 5845 6839 6284 -385 -25 -843 C ATOM 1040 N VAL A 149 194.317 37.675 535.987 1.00 67.19 N ANISOU 1040 N VAL A 149 7236 9455 8839 -857 -701 -889 N ATOM 1041 CA VAL A 149 195.425 38.215 535.202 1.00 56.78 C ANISOU 1041 CA VAL A 149 5720 8157 7696 -994 -707 -869 C ATOM 1042 C VAL A 149 196.009 37.142 534.291 1.00 48.48 C ANISOU 1042 C VAL A 149 4486 7215 6719 -917 -618 -760 C ATOM 1043 O VAL A 149 196.289 37.394 533.112 1.00 44.29 O ANISOU 1043 O VAL A 149 3856 6668 6304 -975 -496 -701 O ATOM 1044 CB VAL A 149 196.495 38.821 536.130 1.00 40.80 C ANISOU 1044 CB VAL A 149 3610 6183 5711 -1114 -916 -960 C ATOM 1045 CG1 VAL A 149 197.735 39.203 535.337 1.00 37.11 C ANISOU 1045 CG1 VAL A 149 2892 5760 5448 -1256 -914 -922 C ATOM 1046 CG2 VAL A 149 195.936 40.035 536.854 1.00 36.42 C ANISOU 1046 CG2 VAL A 149 3250 5491 5098 -1207 -985 -1084 C ATOM 1047 N LEU A 150 196.191 35.927 534.816 1.00 45.41 N ANISOU 1047 N LEU A 150 4065 6931 6258 -774 -670 -729 N ATOM 1048 CA LEU A 150 196.721 34.843 533.994 1.00 49.09 C ANISOU 1048 CA LEU A 150 4373 7486 6791 -678 -582 -637 C ATOM 1049 C LEU A 150 195.794 34.525 532.828 1.00 57.20 C ANISOU 1049 C LEU A 150 5482 8439 7811 -622 -383 -583 C ATOM 1050 O LEU A 150 196.257 34.271 531.710 1.00 60.13 O ANISOU 1050 O LEU A 150 5729 8845 8272 -617 -271 -526 O ATOM 1051 CB LEU A 150 196.956 33.597 534.848 1.00 61.79 C ANISOU 1051 CB LEU A 150 5972 9190 8316 -519 -676 -611 C ATOM 1052 CG LEU A 150 198.329 33.493 535.513 1.00 72.86 C ANISOU 1052 CG LEU A 150 7178 10728 9777 -533 -857 -622 C ATOM 1053 CD1 LEU A 150 198.415 32.247 536.379 1.00 72.33 C ANISOU 1053 CD1 LEU A 150 7141 10737 9603 -351 -947 -580 C ATOM 1054 CD2 LEU A 150 199.427 33.494 534.461 1.00 73.10 C ANISOU 1054 CD2 LEU A 150 6945 10834 9994 -581 -790 -574 C ATOM 1055 N SER A 151 194.480 34.536 533.065 1.00 52.80 N ANISOU 1055 N SER A 151 5130 7786 7144 -575 -338 -603 N ATOM 1056 CA SER A 151 193.536 34.287 531.980 1.00 37.49 C ANISOU 1056 CA SER A 151 3265 5780 5199 -529 -176 -563 C ATOM 1057 C SER A 151 193.623 35.379 530.919 1.00 43.10 C ANISOU 1057 C SER A 151 3947 6434 5994 -648 -93 -551 C ATOM 1058 O SER A 151 193.668 35.092 529.715 1.00 50.75 O ANISOU 1058 O SER A 151 4866 7416 7002 -625 29 -495 O ATOM 1059 CB SER A 151 192.116 34.183 532.535 1.00 37.25 C ANISOU 1059 CB SER A 151 3434 5666 5055 -469 -155 -589 C ATOM 1060 OG SER A 151 192.002 33.101 533.441 1.00 40.04 O ANISOU 1060 OG SER A 151 3824 6064 5326 -356 -204 -577 O ATOM 1061 N PHE A 152 193.656 36.643 531.354 1.00 41.18 N ANISOU 1061 N PHE A 152 3751 6122 5776 -774 -157 -602 N ATOM 1062 CA PHE A 152 193.749 37.751 530.407 1.00 46.46 C ANISOU 1062 CA PHE A 152 4409 6712 6530 -894 -77 -578 C ATOM 1063 C PHE A 152 195.016 37.658 529.567 1.00 46.40 C ANISOU 1063 C PHE A 152 4193 6794 6643 -953 -25 -514 C ATOM 1064 O PHE A 152 194.975 37.853 528.346 1.00 52.20 O ANISOU 1064 O PHE A 152 4912 7509 7411 -969 113 -445 O ATOM 1065 CB PHE A 152 193.698 39.085 531.152 1.00 53.93 C ANISOU 1065 CB PHE A 152 5440 7552 7497 -1023 -170 -654 C ATOM 1066 CG PHE A 152 193.832 40.285 530.257 1.00 53.67 C ANISOU 1066 CG PHE A 152 5411 7415 7567 -1155 -92 -619 C ATOM 1067 CD1 PHE A 152 192.723 40.816 529.620 1.00 51.18 C ANISOU 1067 CD1 PHE A 152 5251 6980 7216 -1125 6 -592 C ATOM 1068 CD2 PHE A 152 195.065 40.884 530.054 1.00 53.99 C ANISOU 1068 CD2 PHE A 152 5294 7474 7747 -1308 -116 -604 C ATOM 1069 CE1 PHE A 152 192.841 41.920 528.795 1.00 40.46 C ANISOU 1069 CE1 PHE A 152 3914 5513 5944 -1235 79 -542 C ATOM 1070 CE2 PHE A 152 195.190 41.987 529.230 1.00 56.53 C ANISOU 1070 CE2 PHE A 152 5628 7684 8166 -1437 -29 -554 C ATOM 1071 CZ PHE A 152 194.076 42.505 528.600 1.00 47.37 C ANISOU 1071 CZ PHE A 152 4648 6396 6956 -1395 69 -518 C ATOM 1072 N ILE A 153 196.153 37.365 530.203 1.00 44.17 N ANISOU 1072 N ILE A 153 3745 6617 6421 -981 -132 -532 N ATOM 1073 CA ILE A 153 197.405 37.249 529.462 1.00 48.49 C ANISOU 1073 CA ILE A 153 4061 7264 7099 -1032 -74 -471 C ATOM 1074 C ILE A 153 197.369 36.050 528.524 1.00 49.72 C ANISOU 1074 C ILE A 153 4171 7497 7224 -878 63 -403 C ATOM 1075 O ILE A 153 197.930 36.097 527.421 1.00 44.58 O ANISOU 1075 O ILE A 153 3408 6888 6643 -902 200 -336 O ATOM 1076 CB ILE A 153 198.594 37.171 530.439 1.00 49.77 C ANISOU 1076 CB ILE A 153 4039 7533 7340 -1083 -244 -513 C ATOM 1077 CG1 ILE A 153 198.697 38.459 531.258 1.00 53.80 C ANISOU 1077 CG1 ILE A 153 4597 7955 7888 -1258 -383 -598 C ATOM 1078 CG2 ILE A 153 199.895 36.916 529.695 1.00 46.29 C ANISOU 1078 CG2 ILE A 153 3324 7216 7048 -1113 -174 -445 C ATOM 1079 CD1 ILE A 153 199.841 38.458 532.248 1.00 55.70 C ANISOU 1079 CD1 ILE A 153 4659 8303 8200 -1322 -583 -656 C ATOM 1080 N LEU A 154 196.700 34.969 528.926 1.00 49.74 N ANISOU 1080 N LEU A 154 4269 7511 7118 -722 39 -419 N ATOM 1081 CA LEU A 154 196.664 33.775 528.089 1.00 48.96 C ANISOU 1081 CA LEU A 154 4141 7466 6994 -576 157 -374 C ATOM 1082 C LEU A 154 195.818 33.990 526.839 1.00 54.90 C ANISOU 1082 C LEU A 154 5014 8148 7697 -568 310 -343 C ATOM 1083 O LEU A 154 196.233 33.620 525.734 1.00 43.61 O ANISOU 1083 O LEU A 154 3510 6771 6288 -527 441 -297 O ATOM 1084 CB LEU A 154 196.138 32.582 528.888 1.00 50.67 C ANISOU 1084 CB LEU A 154 4444 7688 7122 -425 88 -396 C ATOM 1085 CG LEU A 154 197.118 31.854 529.812 1.00 58.28 C ANISOU 1085 CG LEU A 154 5269 8756 8118 -356 -34 -395 C ATOM 1086 CD1 LEU A 154 196.449 30.647 530.452 1.00 43.72 C ANISOU 1086 CD1 LEU A 154 3548 6887 6176 -200 -68 -393 C ATOM 1087 CD2 LEU A 154 198.372 31.440 529.057 1.00 61.70 C ANISOU 1087 CD2 LEU A 154 5473 9303 8668 -322 35 -349 C ATOM 1088 N TRP A 155 194.636 34.590 526.984 1.00 59.14 N ANISOU 1088 N TRP A 155 5734 8572 8164 -598 297 -369 N ATOM 1089 CA TRP A 155 193.660 34.613 525.898 1.00 33.34 C ANISOU 1089 CA TRP A 155 2594 5245 4830 -558 410 -345 C ATOM 1090 C TRP A 155 193.537 35.946 525.178 1.00 30.30 C ANISOU 1090 C TRP A 155 2254 4789 4471 -674 472 -306 C ATOM 1091 O TRP A 155 193.308 35.958 523.968 1.00 33.97 O ANISOU 1091 O TRP A 155 2755 5254 4899 -647 589 -255 O ATOM 1092 CB TRP A 155 192.283 34.205 526.423 1.00 27.36 C ANISOU 1092 CB TRP A 155 2002 4415 3981 -481 366 -390 C ATOM 1093 CG TRP A 155 192.181 32.745 526.692 1.00 36.85 C ANISOU 1093 CG TRP A 155 3195 5660 5148 -351 356 -405 C ATOM 1094 CD1 TRP A 155 192.190 32.130 527.910 1.00 38.40 C ANISOU 1094 CD1 TRP A 155 3397 5867 5326 -302 262 -430 C ATOM 1095 CD2 TRP A 155 192.076 31.705 525.716 1.00 27.15 C ANISOU 1095 CD2 TRP A 155 1962 4458 3894 -249 447 -393 C ATOM 1096 NE1 TRP A 155 192.085 30.769 527.752 1.00 26.86 N ANISOU 1096 NE1 TRP A 155 1936 4425 3845 -180 293 -423 N ATOM 1097 CE2 TRP A 155 192.015 30.483 526.413 1.00 25.27 C ANISOU 1097 CE2 TRP A 155 1728 4229 3644 -147 403 -411 C ATOM 1098 CE3 TRP A 155 192.023 31.689 524.320 1.00 27.14 C ANISOU 1098 CE3 TRP A 155 1972 4470 3870 -230 559 -371 C ATOM 1099 CZ2 TRP A 155 191.903 29.259 525.761 1.00 26.03 C ANISOU 1099 CZ2 TRP A 155 1835 4329 3725 -35 467 -418 C ATOM 1100 CZ3 TRP A 155 191.913 30.476 523.675 1.00 32.74 C ANISOU 1100 CZ3 TRP A 155 2695 5200 4546 -114 617 -389 C ATOM 1101 CH2 TRP A 155 191.854 29.277 524.395 1.00 35.86 C ANISOU 1101 CH2 TRP A 155 3091 5586 4948 -22 570 -417 C ATOM 1102 N ALA A 156 193.667 37.073 525.876 1.00 29.81 N ANISOU 1102 N ALA A 156 2207 4657 4462 -799 397 -327 N ATOM 1103 CA ALA A 156 193.403 38.362 525.235 1.00 30.65 C ANISOU 1103 CA ALA A 156 2391 4659 4595 -902 456 -284 C ATOM 1104 C ALA A 156 194.387 38.696 524.120 1.00 44.35 C ANISOU 1104 C ALA A 156 4009 6442 6401 -974 584 -191 C ATOM 1105 O ALA A 156 193.932 39.016 523.006 1.00 48.51 O ANISOU 1105 O ALA A 156 4623 6931 6876 -957 696 -122 O ATOM 1106 CB ALA A 156 193.360 39.464 526.298 1.00 41.66 C ANISOU 1106 CB ALA A 156 3839 5949 6041 -1019 342 -343 C ATOM 1107 N PRO A 157 195.714 38.648 524.319 1.00 51.63 N ANISOU 1107 N PRO A 157 4730 7451 7434 -1052 579 -179 N ATOM 1108 CA PRO A 157 196.613 39.096 523.241 1.00 41.34 C ANISOU 1108 CA PRO A 157 3311 6186 6209 -1136 728 -78 C ATOM 1109 C PRO A 157 196.529 38.249 521.984 1.00 39.15 C ANISOU 1109 C PRO A 157 3041 5996 5838 -1003 886 -19 C ATOM 1110 O PRO A 157 196.606 38.790 520.874 1.00 53.99 O ANISOU 1110 O PRO A 157 4954 7859 7699 -1040 1032 75 O ATOM 1111 CB PRO A 157 198.005 39.013 523.886 1.00 40.48 C ANISOU 1111 CB PRO A 157 2955 6177 6249 -1226 668 -95 C ATOM 1112 CG PRO A 157 197.756 39.001 525.354 1.00 45.89 C ANISOU 1112 CG PRO A 157 3676 6829 6931 -1235 462 -205 C ATOM 1113 CD PRO A 157 196.476 38.253 525.518 1.00 44.21 C ANISOU 1113 CD PRO A 157 3654 6585 6561 -1071 438 -246 C ATOM 1114 N ALA A 158 196.380 36.931 522.124 1.00 36.58 N ANISOU 1114 N ALA A 158 2698 5756 5445 -847 863 -70 N ATOM 1115 CA ALA A 158 196.306 36.068 520.950 1.00 45.15 C ANISOU 1115 CA ALA A 158 3804 6917 6435 -715 1004 -38 C ATOM 1116 C ALA A 158 195.040 36.340 520.147 1.00 50.74 C ANISOU 1116 C ALA A 158 4735 7541 7005 -668 1044 -21 C ATOM 1117 O ALA A 158 195.093 36.511 518.923 1.00 57.57 O ANISOU 1117 O ALA A 158 5642 8431 7800 -649 1184 50 O ATOM 1118 CB ALA A 158 196.375 34.600 521.373 1.00 30.69 C ANISOU 1118 CB ALA A 158 1922 5162 4576 -562 956 -107 C ATOM 1119 N ILE A 159 193.891 36.393 520.825 1.00 36.93 N ANISOU 1119 N ILE A 159 3125 5699 5208 -643 920 -83 N ATOM 1120 CA ILE A 159 192.622 36.609 520.136 1.00 36.20 C ANISOU 1120 CA ILE A 159 3222 5535 4997 -587 933 -73 C ATOM 1121 C ILE A 159 192.585 37.991 519.496 1.00 47.56 C ANISOU 1121 C ILE A 159 4730 6895 6443 -688 998 21 C ATOM 1122 O ILE A 159 192.155 38.147 518.345 1.00 50.60 O ANISOU 1122 O ILE A 159 5219 7281 6724 -638 1082 82 O ATOM 1123 CB ILE A 159 191.449 36.406 521.113 1.00 30.21 C ANISOU 1123 CB ILE A 159 2563 4700 4214 -545 796 -156 C ATOM 1124 CG1 ILE A 159 191.385 34.952 521.583 1.00 29.93 C ANISOU 1124 CG1 ILE A 159 2486 4727 4158 -436 753 -229 C ATOM 1125 CG2 ILE A 159 190.132 36.813 520.469 1.00 44.57 C ANISOU 1125 CG2 ILE A 159 4551 6445 5941 -499 793 -143 C ATOM 1126 CD1 ILE A 159 190.266 34.680 522.578 1.00 24.21 C ANISOU 1126 CD1 ILE A 159 1849 3934 3414 -399 642 -297 C ATOM 1127 N LEU A 160 193.045 39.015 520.220 1.00 40.37 N ANISOU 1127 N LEU A 160 3775 5911 5653 -829 955 36 N ATOM 1128 CA LEU A 160 192.914 40.380 519.726 1.00 58.47 C ANISOU 1128 CA LEU A 160 6159 8088 7969 -929 1007 126 C ATOM 1129 C LEU A 160 193.958 40.728 518.672 1.00 54.77 C ANISOU 1129 C LEU A 160 5607 7674 7528 -1000 1177 248 C ATOM 1130 O LEU A 160 193.666 41.501 517.752 1.00 50.93 O ANISOU 1130 O LEU A 160 5240 7123 6990 -1017 1268 353 O ATOM 1131 CB LEU A 160 193.006 41.370 520.888 1.00 63.84 C ANISOU 1131 CB LEU A 160 6838 8645 8773 -1062 899 82 C ATOM 1132 CG LEU A 160 191.910 41.293 521.953 1.00 58.24 C ANISOU 1132 CG LEU A 160 6236 7861 8029 -1001 754 -26 C ATOM 1133 CD1 LEU A 160 192.145 42.341 523.030 1.00 56.22 C ANISOU 1133 CD1 LEU A 160 5992 7485 7886 -1136 660 -77 C ATOM 1134 CD2 LEU A 160 190.541 41.463 521.324 1.00 60.69 C ANISOU 1134 CD2 LEU A 160 6724 8105 8229 -893 765 -2 C ATOM 1135 N PHE A 161 195.167 40.177 518.776 1.00 45.18 N ANISOU 1135 N PHE A 161 4191 6580 6396 -1033 1229 245 N ATOM 1136 CA PHE A 161 196.287 40.640 517.969 1.00 43.55 C ANISOU 1136 CA PHE A 161 3866 6423 6258 -1131 1400 363 C ATOM 1137 C PHE A 161 196.884 39.580 517.053 1.00 39.40 C ANISOU 1137 C PHE A 161 3247 6067 5655 -1013 1549 390 C ATOM 1138 O PHE A 161 197.859 39.877 516.349 1.00 44.51 O ANISOU 1138 O PHE A 161 3779 6778 6354 -1082 1719 492 O ATOM 1139 CB PHE A 161 197.385 41.198 518.884 1.00 47.35 C ANISOU 1139 CB PHE A 161 4148 6892 6950 -1311 1348 350 C ATOM 1140 CG PHE A 161 196.901 42.258 519.831 1.00 45.97 C ANISOU 1140 CG PHE A 161 4070 6543 6854 -1431 1202 303 C ATOM 1141 CD1 PHE A 161 196.031 43.247 519.402 1.00 43.07 C ANISOU 1141 CD1 PHE A 161 3914 6015 6437 -1455 1224 364 C ATOM 1142 CD2 PHE A 161 197.310 42.259 521.154 1.00 53.34 C ANISOU 1142 CD2 PHE A 161 4894 7472 7903 -1508 1037 195 C ATOM 1143 CE1 PHE A 161 195.584 44.223 520.274 1.00 36.96 C ANISOU 1143 CE1 PHE A 161 3239 5068 5737 -1551 1099 311 C ATOM 1144 CE2 PHE A 161 196.867 43.232 522.030 1.00 58.70 C ANISOU 1144 CE2 PHE A 161 5679 7987 8638 -1610 906 134 C ATOM 1145 CZ PHE A 161 196.002 44.215 521.590 1.00 44.30 C ANISOU 1145 CZ PHE A 161 4065 5993 6774 -1631 944 189 C ATOM 1146 N TRP A 162 196.340 38.359 517.033 1.00 39.27 N ANISOU 1146 N TRP A 162 3278 6120 5521 -841 1501 300 N ATOM 1147 CA TRP A 162 196.888 37.333 516.151 1.00 45.35 C ANISOU 1147 CA TRP A 162 3982 7037 6214 -715 1644 307 C ATOM 1148 C TRP A 162 196.779 37.732 514.685 1.00 60.05 C ANISOU 1148 C TRP A 162 5966 8918 7933 -689 1827 420 C ATOM 1149 O TRP A 162 197.659 37.395 513.883 1.00 61.74 O ANISOU 1149 O TRP A 162 6083 9249 8124 -654 2010 476 O ATOM 1150 CB TRP A 162 196.186 35.997 516.391 1.00 44.01 C ANISOU 1150 CB TRP A 162 3877 6898 5945 -543 1548 183 C ATOM 1151 CG TRP A 162 196.710 34.890 515.533 1.00 40.47 C ANISOU 1151 CG TRP A 162 3380 6579 5416 -401 1686 167 C ATOM 1152 CD1 TRP A 162 196.048 34.245 514.530 1.00 45.39 C ANISOU 1152 CD1 TRP A 162 4165 7226 5854 -263 1742 137 C ATOM 1153 CD2 TRP A 162 198.016 34.304 515.593 1.00 44.90 C ANISOU 1153 CD2 TRP A 162 3716 7261 6081 -374 1782 171 C ATOM 1154 NE1 TRP A 162 196.858 33.289 513.966 1.00 54.54 N ANISOU 1154 NE1 TRP A 162 5232 8504 6986 -149 1876 114 N ATOM 1155 CE2 TRP A 162 198.072 33.306 514.601 1.00 52.91 C ANISOU 1155 CE2 TRP A 162 4782 8361 6961 -208 1909 140 C ATOM 1156 CE3 TRP A 162 199.142 34.526 516.392 1.00 44.34 C ANISOU 1156 CE3 TRP A 162 3409 7227 6210 -467 1759 192 C ATOM 1157 CZ2 TRP A 162 199.210 32.531 514.387 1.00 66.23 C ANISOU 1157 CZ2 TRP A 162 6339 10103 8724 -124 2005 120 C ATOM 1158 CZ3 TRP A 162 200.271 33.756 516.177 1.00 45.72 C ANISOU 1158 CZ3 TRP A 162 3451 7453 6467 -376 1841 183 C ATOM 1159 CH2 TRP A 162 200.296 32.771 515.183 1.00 60.95 C ANISOU 1159 CH2 TRP A 162 5459 9431 8267 -209 1969 141 C ATOM 1160 N GLN A 163 195.714 38.451 514.319 1.00 64.43 N ANISOU 1160 N GLN A 163 6734 9363 8383 -693 1785 460 N ATOM 1161 CA GLN A 163 195.570 38.924 512.946 1.00 47.30 C ANISOU 1161 CA GLN A 163 4706 7207 6059 -664 1943 583 C ATOM 1162 C GLN A 163 196.711 39.858 512.562 1.00 43.89 C ANISOU 1162 C GLN A 163 4160 6781 5735 -815 2126 736 C ATOM 1163 O GLN A 163 197.200 39.820 511.427 1.00 42.02 O ANISOU 1163 O GLN A 163 3939 6635 5393 -777 2330 836 O ATOM 1164 CB GLN A 163 194.221 39.622 512.774 1.00 49.21 C ANISOU 1164 CB GLN A 163 5182 7319 6198 -643 1835 605 C ATOM 1165 CG GLN A 163 193.892 40.611 513.881 1.00 58.17 C ANISOU 1165 CG GLN A 163 6318 8294 7492 -774 1697 598 C ATOM 1166 CD GLN A 163 192.576 41.326 513.654 1.00 58.32 C ANISOU 1166 CD GLN A 163 6558 8186 7417 -731 1606 628 C ATOM 1167 OE1 GLN A 163 192.173 41.560 512.516 1.00 59.12 O ANISOU 1167 OE1 GLN A 163 6807 8298 7356 -659 1682 722 O ATOM 1168 NE2 GLN A 163 191.896 41.673 514.741 1.00 58.82 N ANISOU 1168 NE2 GLN A 163 6644 8132 7572 -763 1443 549 N ATOM 1169 N PHE A 164 197.149 40.706 513.496 1.00 50.63 N ANISOU 1169 N PHE A 164 4901 7538 6800 -993 2061 752 N ATOM 1170 CA PHE A 164 198.291 41.571 513.224 1.00 43.83 C ANISOU 1170 CA PHE A 164 3898 6673 6083 -1166 2227 889 C ATOM 1171 C PHE A 164 199.598 40.792 513.256 1.00 48.28 C ANISOU 1171 C PHE A 164 4204 7407 6732 -1161 2313 854 C ATOM 1172 O PHE A 164 200.554 41.162 512.564 1.00 46.75 O ANISOU 1172 O PHE A 164 3948 7270 6546 -1233 2451 934 O ATOM 1173 CB PHE A 164 198.335 42.723 514.227 1.00 45.14 C ANISOU 1173 CB PHE A 164 4035 6667 6450 -1366 2104 892 C ATOM 1174 CG PHE A 164 197.076 43.541 514.267 1.00 47.27 C ANISOU 1174 CG PHE A 164 4565 6754 6641 -1357 1996 908 C ATOM 1175 CD1 PHE A 164 196.818 44.489 513.291 1.00 48.11 C ANISOU 1175 CD1 PHE A 164 4840 6766 6674 -1389 2125 1073 C ATOM 1176 CD2 PHE A 164 196.153 43.366 515.285 1.00 42.47 C ANISOU 1176 CD2 PHE A 164 4033 6071 6034 -1306 1775 765 C ATOM 1177 CE1 PHE A 164 195.662 45.244 513.326 1.00 45.32 C ANISOU 1177 CE1 PHE A 164 4719 6243 6257 -1361 2022 1092 C ATOM 1178 CE2 PHE A 164 194.995 44.118 515.326 1.00 47.31 C ANISOU 1178 CE2 PHE A 164 4866 6522 6587 -1282 1685 778 C ATOM 1179 CZ PHE A 164 194.749 45.059 514.345 1.00 49.89 C ANISOU 1179 CZ PHE A 164 5353 6754 6851 -1305 1802 940 C ATOM 1180 N ILE A 165 199.662 39.720 514.050 1.00 49.82 N ANISOU 1180 N ILE A 165 4282 7680 6965 -1067 2190 711 N ATOM 1181 CA ILE A 165 200.865 38.891 514.080 1.00 47.51 C ANISOU 1181 CA ILE A 165 3792 7537 6721 -1026 2219 639 C ATOM 1182 C ILE A 165 201.075 38.215 512.730 1.00 45.19 C ANISOU 1182 C ILE A 165 3575 7348 6247 -878 2409 657 C ATOM 1183 O ILE A 165 202.189 38.195 512.192 1.00 47.56 O ANISOU 1183 O ILE A 165 3756 7738 6576 -907 2539 682 O ATOM 1184 CB ILE A 165 200.783 37.861 515.221 1.00 60.16 C ANISOU 1184 CB ILE A 165 5291 9173 8395 -935 2043 490 C ATOM 1185 CG1 ILE A 165 200.814 38.566 516.578 1.00 63.00 C ANISOU 1185 CG1 ILE A 165 5555 9457 8926 -1089 1844 480 C ATOM 1186 CG2 ILE A 165 201.921 36.857 515.118 1.00 67.12 C ANISOU 1186 CG2 ILE A 165 6004 10175 9324 -842 2098 410 C ATOM 1187 CD1 ILE A 165 202.088 39.338 516.833 1.00 65.73 C ANISOU 1187 CD1 ILE A 165 5716 9833 9428 -1271 1842 522 C ATOM 1188 N VAL A 166 200.007 37.650 512.161 1.00 53.04 N ANISOU 1188 N VAL A 166 4768 8339 7045 -716 2424 638 N ATOM 1189 CA VAL A 166 200.125 37.019 510.850 1.00 52.81 C ANISOU 1189 CA VAL A 166 4847 8403 6816 -571 2588 641 C ATOM 1190 C VAL A 166 200.082 38.036 509.716 1.00 53.76 C ANISOU 1190 C VAL A 166 5112 8504 6813 -636 2747 802 C ATOM 1191 O VAL A 166 200.577 37.748 508.619 1.00 48.86 O ANISOU 1191 O VAL A 166 4534 7972 6057 -565 2909 826 O ATOM 1192 CB VAL A 166 199.029 35.961 510.644 1.00 58.25 C ANISOU 1192 CB VAL A 166 5700 9108 7325 -370 2523 542 C ATOM 1193 CG1 VAL A 166 199.188 34.832 511.649 1.00 41.65 C ANISOU 1193 CG1 VAL A 166 3465 7021 5337 -290 2389 393 C ATOM 1194 CG2 VAL A 166 197.650 36.590 510.755 1.00 66.32 C ANISOU 1194 CG2 VAL A 166 6914 10032 8254 -383 2415 585 C ATOM 1195 N GLY A 167 199.508 39.214 509.945 1.00 51.43 N ANISOU 1195 N GLY A 167 4901 8082 6557 -762 2707 915 N ATOM 1196 CA GLY A 167 199.461 40.254 508.939 1.00 50.79 C ANISOU 1196 CA GLY A 167 4970 7954 6373 -828 2849 1086 C ATOM 1197 C GLY A 167 198.227 40.267 508.067 1.00 52.78 C ANISOU 1197 C GLY A 167 5508 8185 6361 -686 2868 1140 C ATOM 1198 O GLY A 167 198.172 41.059 507.118 1.00 49.75 O ANISOU 1198 O GLY A 167 5277 7770 5854 -712 2986 1290 O ATOM 1199 N VAL A 168 197.238 39.425 508.352 1.00 50.22 N ANISOU 1199 N VAL A 168 5264 7879 5937 -536 2740 1023 N ATOM 1200 CA VAL A 168 196.022 39.361 507.549 1.00 47.83 C ANISOU 1200 CA VAL A 168 5244 7557 5372 -399 2669 1017 C ATOM 1201 C VAL A 168 194.884 38.880 508.437 1.00 47.35 C ANISOU 1201 C VAL A 168 5237 7418 5337 -344 2389 849 C ATOM 1202 O VAL A 168 195.071 38.012 509.295 1.00 46.51 O ANISOU 1202 O VAL A 168 4986 7340 5348 -325 2296 706 O ATOM 1203 CB VAL A 168 196.209 38.448 506.315 1.00 52.85 C ANISOU 1203 CB VAL A 168 5969 8359 5753 -222 2827 997 C ATOM 1204 CG1 VAL A 168 196.588 37.034 506.739 1.00 52.35 C ANISOU 1204 CG1 VAL A 168 5766 8385 5741 -125 2779 801 C ATOM 1205 CG2 VAL A 168 194.954 38.440 505.452 1.00 46.31 C ANISOU 1205 CG2 VAL A 168 5434 7518 4644 -88 2730 989 C ATOM 1206 N ARG A 169 193.704 39.463 508.240 1.00 56.80 N ANISOU 1206 N ARG A 169 6637 8515 6430 -316 2260 877 N ATOM 1207 CA ARG A 169 192.495 39.063 508.955 1.00 52.47 C ANISOU 1207 CA ARG A 169 6149 7897 5890 -257 2012 732 C ATOM 1208 C ARG A 169 191.691 38.146 508.040 1.00 59.03 C ANISOU 1208 C ARG A 169 7139 8817 6471 -77 1963 646 C ATOM 1209 O ARG A 169 191.053 38.603 507.088 1.00 75.81 O ANISOU 1209 O ARG A 169 9457 10943 8405 -10 1964 727 O ATOM 1210 CB ARG A 169 191.680 40.280 509.379 1.00 43.60 C ANISOU 1210 CB ARG A 169 5126 6607 4834 -332 1892 805 C ATOM 1211 CG ARG A 169 190.361 39.923 510.042 1.00 39.99 C ANISOU 1211 CG ARG A 169 4728 6088 4379 -261 1658 669 C ATOM 1212 CD ARG A 169 189.619 41.157 510.524 1.00 38.68 C ANISOU 1212 CD ARG A 169 4646 5754 4298 -323 1556 737 C ATOM 1213 NE ARG A 169 188.391 40.800 511.226 1.00 44.49 N ANISOU 1213 NE ARG A 169 5408 6441 5054 -254 1352 606 N ATOM 1214 CZ ARG A 169 188.332 40.491 512.517 1.00 55.10 C ANISOU 1214 CZ ARG A 169 6633 7742 6560 -306 1254 489 C ATOM 1215 NH1 ARG A 169 189.435 40.498 513.253 1.00 62.15 N ANISOU 1215 NH1 ARG A 169 7373 8636 7606 -421 1317 479 N ATOM 1216 NH2 ARG A 169 187.171 40.176 513.074 1.00 66.25 N ANISOU 1216 NH2 ARG A 169 8074 9116 7980 -239 1093 386 N ATOM 1217 N THR A 170 191.724 36.845 508.330 1.00 43.02 N ANISOU 1217 N THR A 170 5038 6861 4449 3 1912 479 N ATOM 1218 CA THR A 170 190.984 35.873 507.538 1.00 39.04 C ANISOU 1218 CA THR A 170 4676 6428 3730 161 1849 365 C ATOM 1219 C THR A 170 189.502 35.830 507.886 1.00 56.44 C ANISOU 1219 C THR A 170 6979 8550 5918 195 1608 280 C ATOM 1220 O THR A 170 188.734 35.176 507.172 1.00 67.98 O ANISOU 1220 O THR A 170 8570 10059 7201 310 1525 190 O ATOM 1221 CB THR A 170 191.590 34.478 507.711 1.00 42.60 C ANISOU 1221 CB THR A 170 5017 6960 4208 233 1893 218 C ATOM 1222 OG1 THR A 170 191.477 34.072 509.080 1.00 47.99 O ANISOU 1222 OG1 THR A 170 5556 7569 5108 178 1758 122 O ATOM 1223 CG2 THR A 170 193.058 34.485 507.310 1.00 50.98 C ANISOU 1223 CG2 THR A 170 5959 8121 5289 219 2144 301 C ATOM 1224 N VAL A 171 189.084 36.502 508.955 1.00 58.15 N ANISOU 1224 N VAL A 171 7132 8646 6315 100 1494 298 N ATOM 1225 CA VAL A 171 187.677 36.553 509.335 1.00 51.79 C ANISOU 1225 CA VAL A 171 6398 7765 5515 132 1284 229 C ATOM 1226 C VAL A 171 186.982 37.561 508.426 1.00 60.28 C ANISOU 1226 C VAL A 171 7648 8817 6439 173 1260 355 C ATOM 1227 O VAL A 171 187.215 38.768 508.527 1.00 65.37 O ANISOU 1227 O VAL A 171 8313 9380 7146 96 1316 501 O ATOM 1228 CB VAL A 171 187.505 36.925 510.812 1.00 49.99 C ANISOU 1228 CB VAL A 171 6051 7423 5520 31 1191 202 C ATOM 1229 CG1 VAL A 171 186.031 36.940 511.187 1.00 63.71 C ANISOU 1229 CG1 VAL A 171 7848 9094 7266 76 998 133 C ATOM 1230 CG2 VAL A 171 188.277 35.955 511.695 1.00 31.76 C ANISOU 1230 CG2 VAL A 171 3578 5145 3345 1 1214 100 C ATOM 1231 N GLU A 172 186.127 37.067 507.534 1.00 68.20 N ANISOU 1231 N GLU A 172 8783 9885 7245 294 1167 297 N ATOM 1232 CA GLU A 172 185.451 37.930 506.580 1.00 68.48 C ANISOU 1232 CA GLU A 172 8995 9917 7106 360 1127 418 C ATOM 1233 C GLU A 172 184.381 38.767 507.279 1.00 64.70 C ANISOU 1233 C GLU A 172 8517 9312 6753 341 964 447 C ATOM 1234 O GLU A 172 184.062 38.572 508.455 1.00 61.13 O ANISOU 1234 O GLU A 172 7940 8788 6498 285 878 354 O ATOM 1235 CB GLU A 172 184.830 37.101 505.457 1.00 64.36 C ANISOU 1235 CB GLU A 172 8610 9514 6332 500 1045 326 C ATOM 1236 CG GLU A 172 185.784 36.100 504.827 1.00 77.25 C ANISOU 1236 CG GLU A 172 10247 11267 7838 542 1196 254 C ATOM 1237 CD GLU A 172 185.145 35.314 503.700 1.00 95.83 C ANISOU 1237 CD GLU A 172 12759 13727 9924 680 1102 145 C ATOM 1238 OE1 GLU A 172 184.377 35.911 502.918 1.00103.98 O ANISOU 1238 OE1 GLU A 172 13947 14781 10779 752 1005 220 O ATOM 1239 OE2 GLU A 172 185.407 34.097 503.601 1.00101.82 O ANISOU 1239 OE2 GLU A 172 13493 14543 10651 721 1115 -20 O ATOM 1240 N ASP A 173 183.824 39.717 506.531 1.00 73.52 N ANISOU 1240 N ASP A 173 9786 10404 7746 402 929 583 N ATOM 1241 CA ASP A 173 182.779 40.576 507.069 1.00 72.30 C ANISOU 1241 CA ASP A 173 9645 10128 7698 413 783 621 C ATOM 1242 C ASP A 173 181.521 39.765 507.353 1.00 67.28 C ANISOU 1242 C ASP A 173 8960 9526 7078 488 568 452 C ATOM 1243 O ASP A 173 181.103 38.932 506.545 1.00 79.90 O ANISOU 1243 O ASP A 173 10615 11240 8505 577 487 365 O ATOM 1244 CB ASP A 173 182.467 41.710 506.093 1.00 79.80 C ANISOU 1244 CB ASP A 173 10779 11046 8493 487 790 816 C ATOM 1245 CG ASP A 173 181.542 42.755 506.688 1.00 85.52 C ANISOU 1245 CG ASP A 173 11518 11621 9355 503 671 877 C ATOM 1246 OD1 ASP A 173 181.369 42.766 507.925 1.00 86.68 O ANISOU 1246 OD1 ASP A 173 11530 11677 9726 430 628 787 O ATOM 1247 OD2 ASP A 173 180.985 43.565 505.916 1.00 88.16 O ANISOU 1247 OD2 ASP A 173 12005 11928 9564 601 622 1017 O ATOM 1248 N GLY A 174 180.917 40.014 508.514 1.00 47.45 N ANISOU 1248 N GLY A 174 6342 6911 4775 446 480 401 N ATOM 1249 CA GLY A 174 179.744 39.285 508.939 1.00 39.48 C ANISOU 1249 CA GLY A 174 5255 5923 3824 495 300 250 C ATOM 1250 C GLY A 174 180.027 38.019 509.717 1.00 38.91 C ANISOU 1250 C GLY A 174 5045 5882 3857 431 309 83 C ATOM 1251 O GLY A 174 179.105 37.474 510.338 1.00 40.46 O ANISOU 1251 O GLY A 174 5152 6065 4154 440 185 -32 O ATOM 1252 N GLU A 175 181.262 37.531 509.700 1.00 37.82 N ANISOU 1252 N GLU A 175 4883 5782 3705 372 457 74 N ATOM 1253 CA GLU A 175 181.661 36.364 510.470 1.00 48.39 C ANISOU 1253 CA GLU A 175 6099 7137 5149 321 477 -64 C ATOM 1254 C GLU A 175 182.316 36.796 511.777 1.00 46.58 C ANISOU 1254 C GLU A 175 5759 6818 5119 214 552 -37 C ATOM 1255 O GLU A 175 182.757 37.938 511.932 1.00 32.65 O ANISOU 1255 O GLU A 175 4018 4987 3399 163 621 85 O ATOM 1256 CB GLU A 175 182.624 35.486 509.667 1.00 60.20 C ANISOU 1256 CB GLU A 175 7627 8734 6510 345 588 -102 C ATOM 1257 CG GLU A 175 182.044 34.945 508.373 1.00 66.77 C ANISOU 1257 CG GLU A 175 8586 9662 7120 454 510 -159 C ATOM 1258 CD GLU A 175 183.056 34.152 507.569 1.00 88.21 C ANISOU 1258 CD GLU A 175 11351 12475 9691 491 645 -198 C ATOM 1259 OE1 GLU A 175 184.260 34.215 507.897 1.00 93.85 O ANISOU 1259 OE1 GLU A 175 11996 13189 10473 436 815 -145 O ATOM 1260 OE2 GLU A 175 182.647 33.464 506.610 1.00100.09 O ANISOU 1260 OE2 GLU A 175 12961 14057 11013 578 577 -289 O ATOM 1261 N CYS A 176 182.375 35.862 512.723 1.00 49.74 N ANISOU 1261 N CYS A 176 6049 7211 5638 179 531 -153 N ATOM 1262 CA CYS A 176 182.995 36.130 514.017 1.00 46.28 C ANISOU 1262 CA CYS A 176 5510 6706 5370 86 580 -145 C ATOM 1263 C CYS A 176 183.487 34.812 514.598 1.00 44.80 C ANISOU 1263 C CYS A 176 5228 6555 5239 74 598 -254 C ATOM 1264 O CYS A 176 182.684 34.004 515.073 1.00 47.07 O ANISOU 1264 O CYS A 176 5483 6828 5573 96 510 -353 O ATOM 1265 CB CYS A 176 182.019 36.817 514.967 1.00 44.23 C ANISOU 1265 CB CYS A 176 5233 6349 5225 71 489 -148 C ATOM 1266 SG CYS A 176 182.764 37.273 516.542 0.89 46.67 S ANISOU 1266 SG CYS A 176 5452 6575 5707 -38 535 -148 S ATOM 1267 N TYR A 177 184.801 34.604 514.561 1.00 46.15 N ANISOU 1267 N TYR A 177 5349 6769 5418 41 715 -228 N ATOM 1268 CA TYR A 177 185.407 33.403 515.117 1.00 39.30 C ANISOU 1268 CA TYR A 177 4391 5931 4611 45 739 -315 C ATOM 1269 C TYR A 177 186.878 33.681 515.380 1.00 41.63 C ANISOU 1269 C TYR A 177 4595 6257 4966 -14 859 -251 C ATOM 1270 O TYR A 177 187.459 34.622 514.833 1.00 44.02 O ANISOU 1270 O TYR A 177 4916 6573 5238 -54 945 -147 O ATOM 1271 CB TYR A 177 185.236 32.198 514.183 1.00 32.32 C ANISOU 1271 CB TYR A 177 3558 5110 3612 135 738 -405 C ATOM 1272 CG TYR A 177 185.867 32.374 512.817 1.00 40.31 C ANISOU 1272 CG TYR A 177 4646 6206 4463 183 845 -354 C ATOM 1273 CD1 TYR A 177 185.179 33.005 511.788 1.00 44.36 C ANISOU 1273 CD1 TYR A 177 5286 6740 4829 223 810 -307 C ATOM 1274 CD2 TYR A 177 187.146 31.899 512.555 1.00 48.98 C ANISOU 1274 CD2 TYR A 177 5690 7372 5550 200 985 -347 C ATOM 1275 CE1 TYR A 177 185.750 33.165 510.540 1.00 49.21 C ANISOU 1275 CE1 TYR A 177 5990 7439 5271 275 919 -250 C ATOM 1276 CE2 TYR A 177 187.725 32.055 511.309 1.00 58.26 C ANISOU 1276 CE2 TYR A 177 6937 8632 6567 250 1108 -296 C ATOM 1277 CZ TYR A 177 187.022 32.688 510.306 1.00 61.89 C ANISOU 1277 CZ TYR A 177 7541 9110 6863 285 1078 -246 C ATOM 1278 OH TYR A 177 187.594 32.845 509.064 1.00 67.77 O ANISOU 1278 OH TYR A 177 8377 9947 7426 342 1211 -185 O ATOM 1279 N ILE A 178 187.473 32.848 516.235 1.00 37.28 N ANISOU 1279 N ILE A 178 3939 5715 4509 -19 862 -308 N ATOM 1280 CA ILE A 178 188.890 32.982 516.548 1.00 40.05 C ANISOU 1280 CA ILE A 178 4171 6111 4936 -67 956 -260 C ATOM 1281 C ILE A 178 189.714 32.590 515.331 1.00 43.83 C ANISOU 1281 C ILE A 178 4650 6687 5318 -8 1094 -237 C ATOM 1282 O ILE A 178 189.518 31.517 514.745 1.00 44.40 O ANISOU 1282 O ILE A 178 4768 6795 5307 92 1104 -317 O ATOM 1283 CB ILE A 178 189.252 32.132 517.774 1.00 42.98 C ANISOU 1283 CB ILE A 178 4437 6474 5420 -64 905 -323 C ATOM 1284 CG1 ILE A 178 188.669 32.760 519.041 1.00 46.43 C ANISOU 1284 CG1 ILE A 178 4872 6827 5941 -135 799 -326 C ATOM 1285 CG2 ILE A 178 190.757 31.974 517.892 1.00 42.66 C ANISOU 1285 CG2 ILE A 178 4253 6508 5447 -79 996 -288 C ATOM 1286 CD1 ILE A 178 189.067 32.050 520.311 1.00 53.74 C ANISOU 1286 CD1 ILE A 178 5711 7750 6957 -133 746 -369 C ATOM 1287 N GLN A 179 190.647 33.463 514.944 1.00 46.25 N ANISOU 1287 N GLN A 179 4906 7030 5637 -72 1209 -131 N ATOM 1288 CA GLN A 179 191.387 33.261 513.702 1.00 60.16 C ANISOU 1288 CA GLN A 179 6679 8891 7288 -15 1369 -89 C ATOM 1289 C GLN A 179 192.315 32.055 513.797 1.00 66.62 C ANISOU 1289 C GLN A 179 7379 9786 8146 62 1440 -157 C ATOM 1290 O GLN A 179 192.260 31.152 512.952 1.00 70.34 O ANISOU 1290 O GLN A 179 7920 10310 8496 180 1495 -222 O ATOM 1291 CB GLN A 179 192.169 34.526 513.349 1.00 64.53 C ANISOU 1291 CB GLN A 179 7192 9455 7870 -120 1492 57 C ATOM 1292 CG GLN A 179 192.865 34.472 512.001 1.00 61.58 C ANISOU 1292 CG GLN A 179 6848 9187 7363 -65 1685 126 C ATOM 1293 CD GLN A 179 193.274 35.845 511.505 1.00 65.19 C ANISOU 1293 CD GLN A 179 7324 9624 7820 -173 1799 292 C ATOM 1294 OE1 GLN A 179 192.697 36.857 511.902 1.00 63.79 O ANISOU 1294 OE1 GLN A 179 7207 9337 7694 -260 1713 347 O ATOM 1295 NE2 GLN A 179 194.274 35.886 510.633 1.00 74.22 N ANISOU 1295 NE2 GLN A 179 8419 10867 8912 -164 2007 377 N ATOM 1296 N PHE A 180 193.167 32.011 514.824 1.00 60.76 N ANISOU 1296 N PHE A 180 6464 9052 7571 7 1430 -149 N ATOM 1297 CA PHE A 180 194.108 30.901 514.944 1.00 64.56 C ANISOU 1297 CA PHE A 180 6819 9607 8105 96 1495 -199 C ATOM 1298 C PHE A 180 193.429 29.573 515.255 1.00 60.21 C ANISOU 1298 C PHE A 180 6336 9011 7530 209 1399 -326 C ATOM 1299 O PHE A 180 194.117 28.548 515.311 1.00 63.30 O ANISOU 1299 O PHE A 180 6649 9443 7958 308 1449 -375 O ATOM 1300 CB PHE A 180 195.174 31.208 516.002 1.00 61.03 C ANISOU 1300 CB PHE A 180 6159 9186 7845 12 1481 -156 C ATOM 1301 CG PHE A 180 194.621 31.550 517.358 1.00 54.40 C ANISOU 1301 CG PHE A 180 5316 8254 7098 -70 1301 -179 C ATOM 1302 CD1 PHE A 180 194.318 30.554 518.272 1.00 50.10 C ANISOU 1302 CD1 PHE A 180 4767 7678 6593 0 1189 -261 C ATOM 1303 CD2 PHE A 180 194.432 32.872 517.728 1.00 52.76 C ANISOU 1303 CD2 PHE A 180 5121 7988 6937 -214 1256 -117 C ATOM 1304 CE1 PHE A 180 193.819 30.867 519.522 1.00 58.98 C ANISOU 1304 CE1 PHE A 180 5901 8729 7781 -67 1041 -278 C ATOM 1305 CE2 PHE A 180 193.935 33.192 518.978 1.00 63.23 C ANISOU 1305 CE2 PHE A 180 6458 9234 8333 -277 1101 -151 C ATOM 1306 CZ PHE A 180 193.629 32.188 519.876 1.00 72.23 C ANISOU 1306 CZ PHE A 180 7593 10359 9492 -202 998 -230 C ATOM 1307 N PHE A 181 192.113 29.561 515.458 1.00 44.34 N ANISOU 1307 N PHE A 181 4463 6911 5472 198 1269 -376 N ATOM 1308 CA PHE A 181 191.351 28.325 515.556 1.00 48.36 C ANISOU 1308 CA PHE A 181 5055 7366 5954 289 1191 -493 C ATOM 1309 C PHE A 181 190.903 27.807 514.196 1.00 66.13 C ANISOU 1309 C PHE A 181 7449 9640 8037 381 1240 -559 C ATOM 1310 O PHE A 181 190.051 26.914 514.137 1.00 68.23 O ANISOU 1310 O PHE A 181 7808 9843 8271 434 1157 -665 O ATOM 1311 CB PHE A 181 190.134 28.518 516.464 1.00 50.15 C ANISOU 1311 CB PHE A 181 5338 7492 6227 227 1033 -517 C ATOM 1312 CG PHE A 181 190.439 28.376 517.928 1.00 44.08 C ANISOU 1312 CG PHE A 181 4463 6686 5598 189 965 -506 C ATOM 1313 CD1 PHE A 181 191.676 27.917 518.350 1.00 45.93 C ANISOU 1313 CD1 PHE A 181 4563 6974 5915 225 1016 -489 C ATOM 1314 CD2 PHE A 181 189.486 28.691 518.881 1.00 42.72 C ANISOU 1314 CD2 PHE A 181 4327 6435 5469 129 849 -512 C ATOM 1315 CE1 PHE A 181 191.959 27.782 519.697 1.00 40.35 C ANISOU 1315 CE1 PHE A 181 3770 6244 5317 201 934 -477 C ATOM 1316 CE2 PHE A 181 189.763 28.557 520.229 1.00 56.26 C ANISOU 1316 CE2 PHE A 181 5967 8124 7284 103 787 -502 C ATOM 1317 CZ PHE A 181 191.001 28.102 520.637 1.00 39.28 C ANISOU 1317 CZ PHE A 181 3695 6030 5201 139 820 -484 C ATOM 1318 N SER A 182 191.451 28.350 513.104 1.00 78.09 N ANISOU 1318 N SER A 182 8989 11243 9439 397 1373 -500 N ATOM 1319 CA SER A 182 191.117 27.848 511.776 1.00 80.12 C ANISOU 1319 CA SER A 182 9398 11539 9505 498 1424 -568 C ATOM 1320 C SER A 182 191.556 26.403 511.583 1.00 82.19 C ANISOU 1320 C SER A 182 9660 11805 9763 628 1474 -691 C ATOM 1321 O SER A 182 191.002 25.707 510.725 1.00 89.19 O ANISOU 1321 O SER A 182 10695 12683 10509 712 1458 -801 O ATOM 1322 CB SER A 182 191.751 28.735 510.703 1.00 82.67 C ANISOU 1322 CB SER A 182 9747 11965 9701 495 1585 -459 C ATOM 1323 OG SER A 182 191.278 30.068 510.797 1.00 82.34 O ANISOU 1323 OG SER A 182 9734 11894 9658 384 1537 -345 O ATOM 1324 N ASN A 183 192.534 25.939 512.356 1.00 81.86 N ANISOU 1324 N ASN A 183 9460 11772 9873 652 1526 -679 N ATOM 1325 CA ASN A 183 192.980 24.554 512.324 1.00 76.59 C ANISOU 1325 CA ASN A 183 8785 11084 9232 787 1569 -787 C ATOM 1326 C ASN A 183 192.290 23.781 513.441 1.00 78.07 C ANISOU 1326 C ASN A 183 8978 11140 9547 774 1409 -851 C ATOM 1327 O ASN A 183 192.208 24.263 514.576 1.00 83.75 O ANISOU 1327 O ASN A 183 9602 11827 10390 681 1323 -781 O ATOM 1328 CB ASN A 183 194.500 24.467 512.470 1.00 76.53 C ANISOU 1328 CB ASN A 183 8589 11171 9319 844 1724 -724 C ATOM 1329 CG ASN A 183 195.008 23.041 512.446 1.00 77.46 C ANISOU 1329 CG ASN A 183 8698 11260 9475 1008 1775 -830 C ATOM 1330 OD1 ASN A 183 195.227 22.432 513.492 1.00 74.24 O ANISOU 1330 OD1 ASN A 183 8197 10789 9220 1032 1702 -837 O ATOM 1331 ND2 ASN A 183 195.197 22.498 511.249 1.00 82.00 N ANISOU 1331 ND2 ASN A 183 9401 11839 9917 1111 1885 -898 N ATOM 1332 N ALA A 184 191.796 22.584 513.115 1.00 75.72 N ANISOU 1332 N ALA A 184 8799 10760 9211 865 1376 -987 N ATOM 1333 CA ALA A 184 191.024 21.813 514.085 1.00 59.38 C ANISOU 1333 CA ALA A 184 6755 8550 7258 842 1237 -1042 C ATOM 1334 C ALA A 184 191.907 21.268 515.200 1.00 59.29 C ANISOU 1334 C ALA A 184 6603 8512 7412 890 1252 -996 C ATOM 1335 O ALA A 184 191.488 21.221 516.363 1.00 65.75 O ANISOU 1335 O ALA A 184 7387 9255 8340 826 1145 -959 O ATOM 1336 CB ALA A 184 190.286 20.675 513.380 1.00 54.99 C ANISOU 1336 CB ALA A 184 6366 7897 6631 913 1198 -1203 C ATOM 1337 N ALA A 185 193.131 20.849 514.868 1.00 58.94 N ANISOU 1337 N ALA A 185 6476 8536 7382 1011 1386 -994 N ATOM 1338 CA ALA A 185 194.018 20.289 515.883 1.00 57.20 C ANISOU 1338 CA ALA A 185 6114 8302 7318 1079 1388 -947 C ATOM 1339 C ALA A 185 194.401 21.326 516.930 1.00 60.90 C ANISOU 1339 C ALA A 185 6421 8838 7880 964 1330 -815 C ATOM 1340 O ALA A 185 194.612 20.979 518.098 1.00 64.01 O ANISOU 1340 O ALA A 185 6740 9188 8392 973 1249 -775 O ATOM 1341 CB ALA A 185 195.270 19.708 515.227 1.00 59.77 C ANISOU 1341 CB ALA A 185 6363 8704 7645 1245 1553 -971 C ATOM 1342 N VAL A 186 194.496 22.598 516.536 1.00 61.47 N ANISOU 1342 N VAL A 186 6450 9009 7897 856 1366 -746 N ATOM 1343 CA VAL A 186 194.768 23.655 517.505 1.00 64.38 C ANISOU 1343 CA VAL A 186 6688 9421 8353 728 1298 -639 C ATOM 1344 C VAL A 186 193.605 23.793 518.478 1.00 50.98 C ANISOU 1344 C VAL A 186 5079 7615 6678 637 1137 -644 C ATOM 1345 O VAL A 186 193.803 23.908 519.695 1.00 49.08 O ANISOU 1345 O VAL A 186 4757 7361 6531 599 1049 -596 O ATOM 1346 CB VAL A 186 195.062 24.981 516.780 1.00 73.49 C ANISOU 1346 CB VAL A 186 7802 10675 9447 628 1383 -566 C ATOM 1347 CG1 VAL A 186 195.380 26.079 517.783 1.00 71.39 C ANISOU 1347 CG1 VAL A 186 7407 10434 9285 487 1307 -472 C ATOM 1348 CG2 VAL A 186 196.206 24.803 515.793 1.00 74.08 C ANISOU 1348 CG2 VAL A 186 7786 10865 9495 722 1572 -553 C ATOM 1349 N THR A 187 192.374 23.777 517.960 1.00 47.94 N ANISOU 1349 N THR A 187 4855 7158 6201 604 1097 -704 N ATOM 1350 CA THR A 187 191.202 23.840 518.827 1.00 42.10 C ANISOU 1350 CA THR A 187 4189 6318 5490 527 965 -712 C ATOM 1351 C THR A 187 191.140 22.631 519.753 1.00 39.36 C ANISOU 1351 C THR A 187 3849 5877 5230 595 913 -738 C ATOM 1352 O THR A 187 190.720 22.746 520.911 1.00 49.60 O ANISOU 1352 O THR A 187 5139 7124 6584 539 825 -699 O ATOM 1353 CB THR A 187 189.930 23.936 517.983 1.00 40.47 C ANISOU 1353 CB THR A 187 4131 6064 5181 494 933 -778 C ATOM 1354 OG1 THR A 187 190.074 24.984 517.016 1.00 61.21 O ANISOU 1354 OG1 THR A 187 6769 8779 7708 457 992 -740 O ATOM 1355 CG2 THR A 187 188.723 24.233 518.861 1.00 32.63 C ANISOU 1355 CG2 THR A 187 3180 4989 4228 403 814 -770 C ATOM 1356 N PHE A 188 191.564 21.463 519.264 1.00 34.08 N ANISOU 1356 N PHE A 188 3206 5174 4568 723 974 -802 N ATOM 1357 CA PHE A 188 191.550 20.269 520.102 1.00 31.47 C ANISOU 1357 CA PHE A 188 2896 4733 4328 799 933 -815 C ATOM 1358 C PHE A 188 192.592 20.356 521.209 1.00 45.54 C ANISOU 1358 C PHE A 188 4532 6571 6198 833 910 -718 C ATOM 1359 O PHE A 188 192.314 19.995 522.358 1.00 58.20 O ANISOU 1359 O PHE A 188 6151 8105 7859 827 829 -677 O ATOM 1360 CB PHE A 188 191.777 19.023 519.250 1.00 33.33 C ANISOU 1360 CB PHE A 188 3208 4902 4553 937 1007 -915 C ATOM 1361 CG PHE A 188 191.655 17.738 520.015 1.00 44.65 C ANISOU 1361 CG PHE A 188 4694 6186 6085 1016 970 -928 C ATOM 1362 CD1 PHE A 188 190.561 17.507 520.833 1.00 44.31 C ANISOU 1362 CD1 PHE A 188 4730 6022 6084 929 878 -915 C ATOM 1363 CD2 PHE A 188 192.628 16.758 519.912 1.00 61.42 C ANISOU 1363 CD2 PHE A 188 6789 8283 8263 1183 1039 -946 C ATOM 1364 CE1 PHE A 188 190.443 16.326 521.539 1.00 48.51 C ANISOU 1364 CE1 PHE A 188 5322 6403 6708 996 857 -908 C ATOM 1365 CE2 PHE A 188 192.515 15.573 520.613 1.00 61.16 C ANISOU 1365 CE2 PHE A 188 6821 8092 8325 1263 1006 -945 C ATOM 1366 CZ PHE A 188 191.421 15.357 521.429 1.00 60.56 C ANISOU 1366 CZ PHE A 188 6835 7890 8287 1163 917 -920 C ATOM 1367 N GLY A 189 193.801 20.820 520.882 1.00 42.69 N ANISOU 1367 N GLY A 189 4027 6344 5851 870 980 -679 N ATOM 1368 CA GLY A 189 194.798 21.035 521.918 1.00 43.85 C ANISOU 1368 CA GLY A 189 4012 6565 6086 886 933 -593 C ATOM 1369 C GLY A 189 194.346 22.052 522.946 1.00 50.13 C ANISOU 1369 C GLY A 189 4794 7372 6880 740 818 -534 C ATOM 1370 O GLY A 189 194.614 21.905 524.143 1.00 47.06 O ANISOU 1370 O GLY A 189 4359 6981 6542 753 725 -482 O ATOM 1371 N THR A 190 193.647 23.096 522.493 1.00 47.14 N ANISOU 1371 N THR A 190 4470 7006 6437 611 822 -543 N ATOM 1372 CA THR A 190 193.048 24.048 523.422 1.00 46.13 C ANISOU 1372 CA THR A 190 4361 6864 6302 482 722 -506 C ATOM 1373 C THR A 190 192.023 23.368 524.322 1.00 55.14 C ANISOU 1373 C THR A 190 5623 7887 7441 491 646 -516 C ATOM 1374 O THR A 190 191.965 23.641 525.527 1.00 61.62 O ANISOU 1374 O THR A 190 6433 8704 8275 454 560 -473 O ATOM 1375 CB THR A 190 192.405 25.198 522.644 1.00 52.14 C ANISOU 1375 CB THR A 190 5176 7637 6996 368 751 -514 C ATOM 1376 OG1 THR A 190 193.427 26.075 522.153 1.00 66.54 O ANISOU 1376 OG1 THR A 190 6875 9569 8837 324 813 -470 O ATOM 1377 CG2 THR A 190 191.445 25.979 523.525 1.00 46.26 C ANISOU 1377 CG2 THR A 190 4499 6839 6238 262 657 -500 C ATOM 1378 N ALA A 191 191.213 22.469 523.757 1.00 53.74 N ANISOU 1378 N ALA A 191 5562 7611 7246 537 679 -576 N ATOM 1379 CA ALA A 191 190.223 21.761 524.561 1.00 40.91 C ANISOU 1379 CA ALA A 191 4042 5864 5638 534 627 -578 C ATOM 1380 C ALA A 191 190.880 20.830 525.571 1.00 43.06 C ANISOU 1380 C ALA A 191 4289 6105 5966 635 596 -524 C ATOM 1381 O ALA A 191 190.341 20.627 526.665 1.00 51.46 O ANISOU 1381 O ALA A 191 5409 7108 7034 615 541 -479 O ATOM 1382 CB ALA A 191 189.273 20.977 523.656 1.00 44.30 C ANISOU 1382 CB ALA A 191 4587 6189 6055 548 663 -663 C ATOM 1383 N ILE A 192 192.036 20.260 525.230 1.00 47.02 N ANISOU 1383 N ILE A 192 4708 6650 6507 754 636 -521 N ATOM 1384 CA ILE A 192 192.730 19.371 526.154 1.00 48.12 C ANISOU 1384 CA ILE A 192 4817 6763 6703 874 597 -460 C ATOM 1385 C ILE A 192 193.395 20.164 527.272 1.00 48.70 C ANISOU 1385 C ILE A 192 4782 6948 6772 840 501 -381 C ATOM 1386 O ILE A 192 193.339 19.773 528.443 1.00 61.06 O ANISOU 1386 O ILE A 192 6387 8479 8336 876 425 -317 O ATOM 1387 CB ILE A 192 193.750 18.507 525.391 1.00 43.94 C ANISOU 1387 CB ILE A 192 4223 6245 6227 1032 674 -488 C ATOM 1388 CG1 ILE A 192 193.035 17.568 524.417 1.00 39.03 C ANISOU 1388 CG1 ILE A 192 3744 5486 5602 1074 751 -583 C ATOM 1389 CG2 ILE A 192 194.618 17.714 526.359 1.00 37.01 C ANISOU 1389 CG2 ILE A 192 3287 5361 5414 1174 621 -409 C ATOM 1390 CD1 ILE A 192 193.974 16.654 523.656 1.00 36.58 C ANISOU 1390 CD1 ILE A 192 3398 5166 5334 1247 840 -628 C ATOM 1391 N ALA A 193 194.025 21.292 526.938 1.00 40.49 N ANISOU 1391 N ALA A 193 3615 6041 5727 765 500 -383 N ATOM 1392 CA ALA A 193 194.758 22.051 527.944 1.00 39.85 C ANISOU 1392 CA ALA A 193 3420 6066 5654 724 394 -328 C ATOM 1393 C ALA A 193 193.842 22.880 528.836 1.00 44.13 C ANISOU 1393 C ALA A 193 4060 6581 6127 597 316 -320 C ATOM 1394 O ALA A 193 194.152 23.079 530.016 1.00 53.99 O ANISOU 1394 O ALA A 193 5289 7869 7354 596 206 -277 O ATOM 1395 CB ALA A 193 195.788 22.958 527.269 1.00 50.63 C ANISOU 1395 CB ALA A 193 4605 7569 7062 673 428 -333 C ATOM 1396 N ALA A 194 192.720 23.363 528.307 1.00 43.53 N ANISOU 1396 N ALA A 194 4088 6442 6009 502 366 -364 N ATOM 1397 CA ALA A 194 191.865 24.298 529.026 1.00 39.99 C ANISOU 1397 CA ALA A 194 3718 5975 5503 387 312 -365 C ATOM 1398 C ALA A 194 190.597 23.663 529.582 1.00 51.75 C ANISOU 1398 C ALA A 194 5360 7348 6956 396 320 -359 C ATOM 1399 O ALA A 194 189.831 24.351 530.265 1.00 59.70 O ANISOU 1399 O ALA A 194 6435 8338 7912 321 290 -359 O ATOM 1400 CB ALA A 194 191.491 25.474 528.118 1.00 39.57 C ANISOU 1400 CB ALA A 194 3659 5940 5436 273 357 -406 C ATOM 1401 N PHE A 195 190.350 22.381 529.316 1.00 47.49 N ANISOU 1401 N PHE A 195 4875 6720 6449 485 369 -356 N ATOM 1402 CA PHE A 195 189.139 21.751 529.832 1.00 41.48 C ANISOU 1402 CA PHE A 195 4246 5839 5676 476 389 -343 C ATOM 1403 C PHE A 195 189.400 20.359 530.395 1.00 44.35 C ANISOU 1403 C PHE A 195 4659 6121 6073 594 391 -284 C ATOM 1404 O PHE A 195 189.143 20.109 531.577 1.00 44.71 O ANISOU 1404 O PHE A 195 4773 6137 6080 610 359 -213 O ATOM 1405 CB PHE A 195 188.065 21.672 528.745 1.00 30.44 C ANISOU 1405 CB PHE A 195 2900 4367 4298 419 456 -414 C ATOM 1406 CG PHE A 195 186.843 20.901 529.162 1.00 27.51 C ANISOU 1406 CG PHE A 195 2635 3867 3950 400 486 -404 C ATOM 1407 CD1 PHE A 195 185.929 21.452 530.044 1.00 28.16 C ANISOU 1407 CD1 PHE A 195 2764 3941 3996 328 479 -374 C ATOM 1408 CD2 PHE A 195 186.613 19.623 528.679 1.00 24.27 C ANISOU 1408 CD2 PHE A 195 2277 3338 3605 451 529 -427 C ATOM 1409 CE1 PHE A 195 184.809 20.745 530.436 1.00 23.30 C ANISOU 1409 CE1 PHE A 195 2225 3212 3414 302 525 -354 C ATOM 1410 CE2 PHE A 195 185.492 18.911 529.067 1.00 28.02 C ANISOU 1410 CE2 PHE A 195 2839 3685 4124 413 561 -412 C ATOM 1411 CZ PHE A 195 184.589 19.474 529.945 1.00 23.99 C ANISOU 1411 CZ PHE A 195 2354 3178 3582 335 564 -369 C ATOM 1412 N TYR A 196 189.905 19.447 529.560 1.00 29.54 N ANISOU 1412 N TYR A 196 2762 4202 4261 685 436 -311 N ATOM 1413 CA TYR A 196 189.997 18.047 529.964 1.00 34.82 C ANISOU 1413 CA TYR A 196 3503 4749 4977 800 452 -261 C ATOM 1414 C TYR A 196 190.956 17.864 531.135 1.00 41.30 C ANISOU 1414 C TYR A 196 4287 5630 5774 901 372 -159 C ATOM 1415 O TYR A 196 190.622 17.200 532.124 1.00 44.54 O ANISOU 1415 O TYR A 196 4799 5957 6166 943 357 -73 O ATOM 1416 CB TYR A 196 190.412 17.183 528.772 1.00 33.72 C ANISOU 1416 CB TYR A 196 3353 4549 4909 890 518 -330 C ATOM 1417 CG TYR A 196 189.282 16.942 527.796 1.00 50.53 C ANISOU 1417 CG TYR A 196 5569 6573 7057 810 579 -427 C ATOM 1418 CD1 TYR A 196 188.309 15.986 528.057 1.00 46.97 C ANISOU 1418 CD1 TYR A 196 5242 5947 6658 791 605 -422 C ATOM 1419 CD2 TYR A 196 189.182 17.675 526.621 1.00 55.03 C ANISOU 1419 CD2 TYR A 196 6095 7219 7596 750 605 -519 C ATOM 1420 CE1 TYR A 196 187.271 15.763 527.174 1.00 38.03 C ANISOU 1420 CE1 TYR A 196 4171 4724 5554 707 638 -521 C ATOM 1421 CE2 TYR A 196 188.146 17.459 525.731 1.00 46.76 C ANISOU 1421 CE2 TYR A 196 5126 6088 6553 683 635 -612 C ATOM 1422 CZ TYR A 196 187.194 16.501 526.013 1.00 41.43 C ANISOU 1422 CZ TYR A 196 4557 5245 5940 659 643 -620 C ATOM 1423 OH TYR A 196 186.161 16.280 525.132 1.00 49.71 O ANISOU 1423 OH TYR A 196 5667 6216 7006 582 651 -723 O ATOM 1424 N LEU A 197 192.151 18.448 531.046 1.00 36.76 N ANISOU 1424 N LEU A 197 3565 5204 5199 939 317 -160 N ATOM 1425 CA LEU A 197 193.094 18.351 532.161 1.00 41.58 C ANISOU 1425 CA LEU A 197 4120 5893 5784 1032 210 -70 C ATOM 1426 C LEU A 197 192.566 19.009 533.429 1.00 43.78 C ANISOU 1426 C LEU A 197 4476 6205 5954 954 131 -21 C ATOM 1427 O LEU A 197 192.684 18.397 534.507 1.00 46.00 O ANISOU 1427 O LEU A 197 4831 6460 6188 1043 75 74 O ATOM 1428 CB LEU A 197 194.453 18.925 531.746 1.00 47.51 C ANISOU 1428 CB LEU A 197 4667 6808 6579 1064 165 -92 C ATOM 1429 CG LEU A 197 195.238 18.127 530.703 1.00 53.43 C ANISOU 1429 CG LEU A 197 5328 7546 7429 1194 245 -121 C ATOM 1430 CD1 LEU A 197 196.608 18.746 530.475 1.00 47.23 C ANISOU 1430 CD1 LEU A 197 4312 6940 6693 1221 203 -123 C ATOM 1431 CD2 LEU A 197 195.366 16.671 531.126 1.00 54.19 C ANISOU 1431 CD2 LEU A 197 5509 7516 7565 1371 248 -54 C ATOM 1432 N PRO A 198 191.990 20.220 533.401 1.00 37.55 N ANISOU 1432 N PRO A 198 3688 5467 5112 805 127 -77 N ATOM 1433 CA PRO A 198 191.365 20.742 534.629 1.00 38.39 C ANISOU 1433 CA PRO A 198 3897 5585 5104 748 74 -40 C ATOM 1434 C PRO A 198 190.265 19.847 535.176 1.00 48.40 C ANISOU 1434 C PRO A 198 5334 6711 6345 770 148 24 C ATOM 1435 O PRO A 198 190.148 19.700 536.399 1.00 75.35 O ANISOU 1435 O PRO A 198 8841 10129 9659 807 103 104 O ATOM 1436 CB PRO A 198 190.823 22.108 534.189 1.00 31.67 C ANISOU 1436 CB PRO A 198 3023 4777 4233 594 91 -127 C ATOM 1437 CG PRO A 198 191.717 22.518 533.084 1.00 30.23 C ANISOU 1437 CG PRO A 198 2685 4669 4133 580 94 -182 C ATOM 1438 CD PRO A 198 192.049 21.253 532.347 1.00 30.66 C ANISOU 1438 CD PRO A 198 2719 4660 4270 697 160 -167 C ATOM 1439 N VAL A 199 189.454 19.241 534.305 1.00 36.26 N ANISOU 1439 N VAL A 199 3840 5048 4890 743 259 -10 N ATOM 1440 CA VAL A 199 188.392 18.353 534.773 1.00 37.64 C ANISOU 1440 CA VAL A 199 4158 5075 5070 742 340 52 C ATOM 1441 C VAL A 199 188.984 17.133 535.468 1.00 45.88 C ANISOU 1441 C VAL A 199 5265 6050 6117 890 319 168 C ATOM 1442 O VAL A 199 188.486 16.693 536.512 1.00 49.49 O ANISOU 1442 O VAL A 199 5847 6446 6510 911 340 272 O ATOM 1443 CB VAL A 199 187.470 17.953 533.605 1.00 40.84 C ANISOU 1443 CB VAL A 199 4576 5360 5580 673 440 -26 C ATOM 1444 CG1 VAL A 199 186.589 16.776 533.997 1.00 36.62 C ANISOU 1444 CG1 VAL A 199 4168 4650 5096 679 522 43 C ATOM 1445 CG2 VAL A 199 186.610 19.132 533.186 1.00 42.09 C ANISOU 1445 CG2 VAL A 199 4704 5573 5715 535 459 -108 C ATOM 1446 N ILE A 200 190.058 16.572 534.907 1.00 41.10 N ANISOU 1446 N ILE A 200 4579 5453 5584 1005 287 161 N ATOM 1447 CA ILE A 200 190.701 15.417 535.530 1.00 40.81 C ANISOU 1447 CA ILE A 200 4597 5348 5562 1172 259 276 C ATOM 1448 C ILE A 200 191.310 15.806 536.872 1.00 42.88 C ANISOU 1448 C ILE A 200 4867 5736 5689 1234 134 373 C ATOM 1449 O ILE A 200 191.216 15.059 537.855 1.00 34.87 O ANISOU 1449 O ILE A 200 3981 4653 4617 1323 124 504 O ATOM 1450 CB ILE A 200 191.755 14.816 534.581 1.00 42.39 C ANISOU 1450 CB ILE A 200 4689 5543 5875 1297 256 234 C ATOM 1451 CG1 ILE A 200 191.091 14.293 533.306 1.00 42.19 C ANISOU 1451 CG1 ILE A 200 4697 5374 5958 1248 376 132 C ATOM 1452 CG2 ILE A 200 192.526 13.704 535.272 1.00 43.37 C ANISOU 1452 CG2 ILE A 200 4857 5606 6016 1494 211 360 C ATOM 1453 CD1 ILE A 200 192.070 13.761 532.285 1.00 33.40 C ANISOU 1453 CD1 ILE A 200 3491 4259 4939 1373 397 69 C ATOM 1454 N ILE A 201 191.936 16.984 536.937 1.00 32.98 N ANISOU 1454 N ILE A 201 3487 4665 4380 1184 33 312 N ATOM 1455 CA ILE A 201 192.537 17.443 538.187 1.00 38.30 C ANISOU 1455 CA ILE A 201 4164 5471 4916 1230 -112 377 C ATOM 1456 C ILE A 201 191.469 17.610 539.261 1.00 55.44 C ANISOU 1456 C ILE A 201 6520 7601 6942 1172 -79 437 C ATOM 1457 O ILE A 201 191.634 17.162 540.401 1.00 35.66 O ANISOU 1457 O ILE A 201 4124 5104 4320 1272 -139 556 O ATOM 1458 CB ILE A 201 193.319 18.749 537.957 1.00 36.17 C ANISOU 1458 CB ILE A 201 3722 5385 4638 1152 -221 278 C ATOM 1459 CG1 ILE A 201 194.540 18.489 537.074 1.00 40.43 C ANISOU 1459 CG1 ILE A 201 4063 5985 5313 1236 -251 249 C ATOM 1460 CG2 ILE A 201 193.739 19.363 539.285 1.00 39.53 C ANISOU 1460 CG2 ILE A 201 4173 5940 4905 1164 -383 314 C ATOM 1461 CD1 ILE A 201 195.348 19.730 536.768 1.00 39.76 C ANISOU 1461 CD1 ILE A 201 3788 6068 5250 1143 -339 161 C ATOM 1462 N MET A 202 190.353 18.254 538.910 1.00 52.88 N ANISOU 1462 N MET A 202 6234 7239 6619 1021 23 362 N ATOM 1463 CA MET A 202 189.278 18.443 539.879 1.00 42.75 C ANISOU 1463 CA MET A 202 5111 5923 5209 967 85 413 C ATOM 1464 C MET A 202 188.621 17.123 540.258 1.00 42.13 C ANISOU 1464 C MET A 202 5180 5676 5150 1030 198 544 C ATOM 1465 O MET A 202 188.113 16.984 541.377 1.00 40.64 O ANISOU 1465 O MET A 202 5139 5476 4827 1049 230 645 O ATOM 1466 CB MET A 202 188.238 19.418 539.327 1.00 41.34 C ANISOU 1466 CB MET A 202 4914 5740 5054 805 172 300 C ATOM 1467 CG MET A 202 188.781 20.812 539.066 1.00 47.97 C ANISOU 1467 CG MET A 202 5639 6722 5867 731 72 183 C ATOM 1468 SD MET A 202 187.553 21.936 538.378 0.85 59.94 S ANISOU 1468 SD MET A 202 7142 8214 7417 567 172 66 S ATOM 1469 CE MET A 202 187.028 21.030 536.926 1.00 66.30 C ANISOU 1469 CE MET A 202 7897 8886 8407 548 290 43 C ATOM 1470 N THR A 203 188.621 16.146 539.349 1.00 45.15 N ANISOU 1470 N THR A 203 5538 5922 5696 1061 268 545 N ATOM 1471 CA THR A 203 188.058 14.838 539.670 1.00 41.50 C ANISOU 1471 CA THR A 203 5217 5271 5279 1113 374 671 C ATOM 1472 C THR A 203 188.942 14.088 540.658 1.00 49.94 C ANISOU 1472 C THR A 203 6368 6344 6261 1294 288 826 C ATOM 1473 O THR A 203 188.439 13.469 541.604 1.00 50.70 O ANISOU 1473 O THR A 203 6631 6353 6278 1332 350 973 O ATOM 1474 CB THR A 203 187.863 14.019 538.394 1.00 36.18 C ANISOU 1474 CB THR A 203 4503 4439 4806 1097 456 605 C ATOM 1475 OG1 THR A 203 186.969 14.709 537.512 1.00 32.63 O ANISOU 1475 OG1 THR A 203 3987 3991 4419 934 522 470 O ATOM 1476 CG2 THR A 203 187.287 12.649 538.720 1.00 39.90 C ANISOU 1476 CG2 THR A 203 5127 4686 5348 1136 564 731 C ATOM 1477 N VAL A 204 190.261 14.132 540.458 1.00 50.41 N ANISOU 1477 N VAL A 204 6309 6509 6335 1413 147 806 N ATOM 1478 CA VAL A 204 191.174 13.486 541.396 1.00 42.77 C ANISOU 1478 CA VAL A 204 5399 5570 5283 1603 35 953 C ATOM 1479 C VAL A 204 191.137 14.191 542.747 1.00 44.08 C ANISOU 1479 C VAL A 204 5655 5880 5213 1603 -57 1017 C ATOM 1480 O VAL A 204 191.094 13.543 543.802 1.00 44.23 O ANISOU 1480 O VAL A 204 5839 5857 5108 1712 -66 1182 O ATOM 1481 CB VAL A 204 192.597 13.449 540.812 1.00 43.65 C ANISOU 1481 CB VAL A 204 5321 5781 5484 1726 -97 903 C ATOM 1482 CG1 VAL A 204 193.565 12.837 541.808 1.00 42.82 C ANISOU 1482 CG1 VAL A 204 5254 5724 5290 1937 -239 1055 C ATOM 1483 CG2 VAL A 204 192.612 12.674 539.505 1.00 55.13 C ANISOU 1483 CG2 VAL A 204 6717 7083 7147 1747 11 837 C ATOM 1484 N LEU A 205 191.149 15.526 542.737 1.00 42.66 N ANISOU 1484 N LEU A 205 5386 5864 4960 1486 -125 887 N ATOM 1485 CA LEU A 205 191.096 16.281 543.985 1.00 43.97 C ANISOU 1485 CA LEU A 205 5649 6166 4892 1480 -216 915 C ATOM 1486 C LEU A 205 189.811 15.988 544.748 1.00 44.76 C ANISOU 1486 C LEU A 205 5965 6162 4879 1438 -53 1015 C ATOM 1487 O LEU A 205 189.840 15.734 545.957 1.00 56.23 O ANISOU 1487 O LEU A 205 7580 7648 6136 1532 -90 1146 O ATOM 1488 CB LEU A 205 191.228 17.778 543.703 1.00 44.22 C ANISOU 1488 CB LEU A 205 5553 6351 4899 1342 -294 739 C ATOM 1489 CG LEU A 205 192.619 18.261 543.290 1.00 47.67 C ANISOU 1489 CG LEU A 205 5778 6934 5400 1377 -481 657 C ATOM 1490 CD1 LEU A 205 192.620 19.763 543.062 1.00 40.04 C ANISOU 1490 CD1 LEU A 205 4715 6086 4414 1217 -537 494 C ATOM 1491 CD2 LEU A 205 193.650 17.875 544.337 1.00 41.38 C ANISOU 1491 CD2 LEU A 205 5003 6244 4474 1546 -674 763 C ATOM 1492 N TYR A 206 188.669 16.010 544.054 1.00 49.39 N ANISOU 1492 N TYR A 206 6553 6628 5586 1299 130 959 N ATOM 1493 CA TYR A 206 187.419 15.655 544.716 1.00 52.76 C ANISOU 1493 CA TYR A 206 7155 6949 5942 1252 309 1062 C ATOM 1494 C TYR A 206 187.437 14.212 545.198 1.00 54.56 C ANISOU 1494 C TYR A 206 7529 7022 6180 1375 373 1264 C ATOM 1495 O TYR A 206 186.809 13.890 546.212 1.00 53.93 O ANISOU 1495 O TYR A 206 7630 6903 5959 1396 471 1406 O ATOM 1496 CB TYR A 206 186.224 15.878 543.789 1.00 37.59 C ANISOU 1496 CB TYR A 206 5171 4928 4183 1082 478 962 C ATOM 1497 CG TYR A 206 184.932 15.406 544.413 1.00 38.45 C ANISOU 1497 CG TYR A 206 5428 4920 4259 1027 679 1076 C ATOM 1498 CD1 TYR A 206 184.273 16.183 545.355 1.00 38.81 C ANISOU 1498 CD1 TYR A 206 5566 5061 4118 989 738 1086 C ATOM 1499 CD2 TYR A 206 184.387 14.170 544.086 1.00 39.17 C ANISOU 1499 CD2 TYR A 206 5569 4803 4511 1014 816 1174 C ATOM 1500 CE1 TYR A 206 183.103 15.751 545.944 1.00 64.19 C ANISOU 1500 CE1 TYR A 206 8902 8181 7307 942 943 1201 C ATOM 1501 CE2 TYR A 206 183.216 13.729 544.671 1.00 60.07 C ANISOU 1501 CE2 TYR A 206 8335 7343 7148 950 1011 1290 C ATOM 1502 CZ TYR A 206 182.578 14.525 545.598 1.00 67.07 C ANISOU 1502 CZ TYR A 206 9295 8342 7847 915 1081 1308 C ATOM 1503 OH TYR A 206 181.411 14.094 546.185 1.00 79.81 O ANISOU 1503 OH TYR A 206 11011 9859 9454 852 1297 1431 O ATOM 1504 N TRP A 207 188.133 13.329 544.482 1.00 48.11 N ANISOU 1504 N TRP A 207 6644 6105 5530 1463 333 1283 N ATOM 1505 CA TRP A 207 188.241 11.944 544.926 1.00 45.67 C ANISOU 1505 CA TRP A 207 6482 5626 5243 1597 384 1478 C ATOM 1506 C TRP A 207 188.977 11.857 546.257 1.00 54.64 C ANISOU 1506 C TRP A 207 7744 6878 6139 1768 248 1632 C ATOM 1507 O TRP A 207 188.540 11.151 547.175 1.00 50.89 O ANISOU 1507 O TRP A 207 7473 6308 5555 1830 338 1824 O ATOM 1508 CB TRP A 207 188.950 11.110 543.859 1.00 46.16 C ANISOU 1508 CB TRP A 207 6441 5570 5530 1677 353 1442 C ATOM 1509 CG TRP A 207 188.810 9.631 544.035 1.00 62.07 C ANISOU 1509 CG TRP A 207 8608 7340 7634 1779 449 1616 C ATOM 1510 CD1 TRP A 207 187.957 8.980 544.876 1.00 73.32 C ANISOU 1510 CD1 TRP A 207 10238 8622 8997 1764 591 1794 C ATOM 1511 CD2 TRP A 207 189.549 8.616 543.346 1.00 76.90 C ANISOU 1511 CD2 TRP A 207 10453 9075 9690 1914 422 1630 C ATOM 1512 NE1 TRP A 207 188.117 7.621 544.753 1.00 80.93 N ANISOU 1512 NE1 TRP A 207 11306 9348 10098 1872 648 1924 N ATOM 1513 CE2 TRP A 207 189.090 7.372 543.821 1.00 84.72 C ANISOU 1513 CE2 TRP A 207 11645 9820 10724 1973 542 1819 C ATOM 1514 CE3 TRP A 207 190.554 8.638 542.374 1.00 72.58 C ANISOU 1514 CE3 TRP A 207 9727 8579 9269 1996 320 1502 C ATOM 1515 CZ2 TRP A 207 189.601 6.162 543.358 1.00 90.59 C ANISOU 1515 CZ2 TRP A 207 12428 10355 11638 2115 553 1875 C ATOM 1516 CZ3 TRP A 207 191.060 7.435 541.915 1.00 75.68 C ANISOU 1516 CZ3 TRP A 207 10151 8782 9822 2146 339 1554 C ATOM 1517 CH2 TRP A 207 190.583 6.215 542.407 1.00 87.32 C ANISOU 1517 CH2 TRP A 207 11839 9999 11340 2206 449 1734 C ATOM 1518 N HIS A 208 190.089 12.586 546.389 1.00 60.74 N ANISOU 1518 N HIS A 208 8397 7859 6823 1842 30 1553 N ATOM 1519 CA HIS A 208 190.832 12.572 547.644 1.00 56.73 C ANISOU 1519 CA HIS A 208 7996 7484 6073 2005 -137 1681 C ATOM 1520 C HIS A 208 190.077 13.283 548.760 1.00 51.11 C ANISOU 1520 C HIS A 208 7454 6870 5096 1942 -94 1709 C ATOM 1521 O HIS A 208 190.210 12.907 549.930 1.00 56.69 O ANISOU 1521 O HIS A 208 8350 7610 5580 2072 -137 1878 O ATOM 1522 CB HIS A 208 192.208 13.207 547.449 1.00 58.88 C ANISOU 1522 CB HIS A 208 8067 7961 6345 2079 -393 1570 C ATOM 1523 CG HIS A 208 193.081 12.466 546.485 1.00 62.22 C ANISOU 1523 CG HIS A 208 8328 8312 7003 2183 -437 1560 C ATOM 1524 ND1 HIS A 208 193.380 11.129 546.631 1.00 66.01 N ANISOU 1524 ND1 HIS A 208 8903 8635 7544 2365 -414 1735 N ATOM 1525 CD2 HIS A 208 193.722 12.876 545.366 1.00 62.89 C ANISOU 1525 CD2 HIS A 208 8169 8456 7272 2141 -489 1398 C ATOM 1526 CE1 HIS A 208 194.165 10.746 545.640 1.00 65.45 C ANISOU 1526 CE1 HIS A 208 8650 8530 7686 2438 -451 1669 C ATOM 1527 NE2 HIS A 208 194.390 11.788 544.860 1.00 64.49 N ANISOU 1527 NE2 HIS A 208 8320 8546 7637 2303 -492 1468 N ATOM 1528 N ILE A 209 189.288 14.305 548.427 1.00 48.61 N ANISOU 1528 N ILE A 209 7081 6601 4789 1757 -6 1550 N ATOM 1529 CA ILE A 209 188.521 15.014 549.448 1.00 50.23 C ANISOU 1529 CA ILE A 209 7446 6893 4748 1703 58 1561 C ATOM 1530 C ILE A 209 187.387 14.136 549.966 1.00 54.88 C ANISOU 1530 C ILE A 209 8236 7313 5303 1696 307 1747 C ATOM 1531 O ILE A 209 187.160 14.035 551.178 1.00 59.06 O ANISOU 1531 O ILE A 209 8975 7889 5575 1774 338 1886 O ATOM 1532 CB ILE A 209 187.995 16.349 548.892 1.00 57.20 C ANISOU 1532 CB ILE A 209 8204 7857 5674 1522 88 1338 C ATOM 1533 CG1 ILE A 209 189.160 17.295 548.594 1.00 45.97 C ANISOU 1533 CG1 ILE A 209 6607 6610 4249 1524 -162 1174 C ATOM 1534 CG2 ILE A 209 187.020 16.991 549.868 1.00 74.30 C ANISOU 1534 CG2 ILE A 209 10541 10079 7612 1470 207 1346 C ATOM 1535 CD1 ILE A 209 188.805 18.419 547.649 1.00 42.04 C ANISOU 1535 CD1 ILE A 209 5948 6140 3886 1348 -130 964 C ATOM 1536 N SER A 210 186.661 13.486 549.054 1.00 65.39 N ANISOU 1536 N SER A 210 9509 8445 6891 1598 490 1752 N ATOM 1537 CA SER A 210 185.567 12.610 549.462 1.00 64.24 C ANISOU 1537 CA SER A 210 9528 8119 6762 1565 737 1928 C ATOM 1538 C SER A 210 186.088 11.386 550.202 1.00 67.78 C ANISOU 1538 C SER A 210 10158 8467 7130 1748 717 2175 C ATOM 1539 O SER A 210 185.451 10.910 551.149 1.00 66.09 O ANISOU 1539 O SER A 210 10151 8189 6769 1774 870 2367 O ATOM 1540 CB SER A 210 184.744 12.194 548.243 1.00 64.20 C ANISOU 1540 CB SER A 210 9399 7922 7072 1408 901 1854 C ATOM 1541 OG SER A 210 185.541 11.498 547.300 1.00 77.30 O ANISOU 1541 OG SER A 210 10952 9479 8938 1468 804 1822 O ATOM 1542 N ARG A 211 187.243 10.858 549.787 1.00 80.88 N ANISOU 1542 N ARG A 211 11741 10107 8882 1884 539 2184 N ATOM 1543 CA ARG A 211 187.855 9.773 550.545 1.00 87.15 C ANISOU 1543 CA ARG A 211 12708 10824 9583 2090 487 2422 C ATOM 1544 C ARG A 211 188.443 10.257 551.864 1.00 90.86 C ANISOU 1544 C ARG A 211 13315 11512 9697 2234 320 2506 C ATOM 1545 O ARG A 211 188.656 9.443 552.769 1.00 93.20 O ANISOU 1545 O ARG A 211 13817 11756 9839 2398 316 2741 O ATOM 1546 CB ARG A 211 188.930 9.076 549.710 1.00 94.70 C ANISOU 1546 CB ARG A 211 13532 11700 10751 2215 347 2401 C ATOM 1547 CG ARG A 211 188.378 7.993 548.794 1.00 97.19 C ANISOU 1547 CG ARG A 211 13845 11718 11366 2153 531 2433 C ATOM 1548 CD ARG A 211 189.480 7.114 548.220 1.00102.95 C ANISOU 1548 CD ARG A 211 14507 12348 12260 2334 409 2460 C ATOM 1549 NE ARG A 211 190.064 7.673 547.005 1.00106.51 N ANISOU 1549 NE ARG A 211 14698 12887 12885 2287 307 2218 N ATOM 1550 CZ ARG A 211 191.190 8.377 546.967 1.00108.00 C ANISOU 1550 CZ ARG A 211 14724 13306 13005 2379 84 2121 C ATOM 1551 NH1 ARG A 211 191.868 8.613 548.083 1.00113.51 N ANISOU 1551 NH1 ARG A 211 15490 14176 13462 2524 -86 2230 N ATOM 1552 NH2 ARG A 211 191.641 8.842 545.810 1.00 98.73 N ANISOU 1552 NH2 ARG A 211 13319 12193 12001 2321 32 1917 N ATOM 1553 N ALA A 212 188.702 11.559 551.995 1.00 92.70 N ANISOU 1553 N ALA A 212 13450 11981 9791 2177 178 2319 N ATOM 1554 CA ALA A 212 189.165 12.104 553.267 1.00 87.85 C ANISOU 1554 CA ALA A 212 12979 11580 8821 2293 15 2368 C ATOM 1555 C ALA A 212 188.012 12.273 554.247 1.00 92.39 C ANISOU 1555 C ALA A 212 13791 12152 9159 2240 229 2469 C ATOM 1556 O ALA A 212 188.164 11.995 555.442 1.00104.57 O ANISOU 1556 O ALA A 212 15565 13760 10406 2386 192 2646 O ATOM 1557 CB ALA A 212 189.877 13.437 553.042 1.00 82.95 C ANISOU 1557 CB ALA A 212 12171 11192 8154 2240 -218 2119 C ATOM 1558 N SER A 213 186.854 12.729 553.762 1.00 90.58 N ANISOU 1558 N SER A 213 13506 11858 9050 2042 455 2364 N ATOM 1559 CA SER A 213 185.672 12.810 554.612 1.00 92.45 C ANISOU 1559 CA SER A 213 13944 12079 9105 1989 703 2468 C ATOM 1560 C SER A 213 185.129 11.433 554.970 1.00 88.12 C ANISOU 1560 C SER A 213 13576 11310 8595 2038 921 2753 C ATOM 1561 O SER A 213 184.373 11.310 555.940 1.00 84.70 O ANISOU 1561 O SER A 213 13357 10877 7950 2049 1111 2908 O ATOM 1562 CB SER A 213 184.583 13.635 553.924 1.00 98.90 C ANISOU 1562 CB SER A 213 14620 12880 10077 1772 883 2280 C ATOM 1563 OG SER A 213 185.035 14.950 553.647 1.00107.70 O ANISOU 1563 OG SER A 213 15594 14181 11148 1724 698 2029 O ATOM 1564 N LYS A 214 185.496 10.403 554.214 1.00162.26 N ANISOU 1564 N LYS A 214 23511 20609 17532 7478 1573 -66 N ATOM 1565 CA LYS A 214 185.060 9.039 554.489 1.00151.86 C ANISOU 1565 CA LYS A 214 22540 19154 16008 7385 809 -55 C ATOM 1566 C LYS A 214 185.959 8.377 555.528 1.00147.60 C ANISOU 1566 C LYS A 214 21616 18631 15833 7272 554 -108 C ATOM 1567 O LYS A 214 185.478 7.801 556.504 1.00147.29 O ANISOU 1567 O LYS A 214 21468 18697 15797 6880 -39 -27 O ATOM 1568 CB LYS A 214 185.047 8.215 553.200 1.00149.48 C ANISOU 1568 CB LYS A 214 22953 18500 15342 7896 729 -121 C ATOM 1569 CG LYS A 214 184.853 6.722 553.411 1.00148.29 C ANISOU 1569 CG LYS A 214 23155 18120 15070 7882 -38 -142 C ATOM 1570 CD LYS A 214 184.965 5.966 552.097 1.00151.29 C ANISOU 1570 CD LYS A 214 24225 18142 15116 8458 -83 -263 C ATOM 1571 CE LYS A 214 184.914 4.463 552.315 1.00150.86 C ANISOU 1571 CE LYS A 214 24494 17806 15019 8475 -849 -310 C ATOM 1572 NZ LYS A 214 183.640 4.035 552.955 1.00146.84 N ANISOU 1572 NZ LYS A 214 24063 17339 14389 7947 -1565 -153 N ATOM 1573 N ALA A1001 185.889 12.371 564.598 1.00173.81 N ANISOU 1573 N ALA A1001 20792 24485 20762 4568 -84 -198 N ATOM 1574 CA ALA A1001 185.357 11.984 563.296 1.00174.80 C ANISOU 1574 CA ALA A1001 21528 24301 20586 4764 0 -84 C ATOM 1575 C ALA A1001 183.985 11.333 563.440 1.00176.69 C ANISOU 1575 C ALA A1001 22133 24649 20351 4468 -528 139 C ATOM 1576 O ALA A1001 183.040 11.696 562.741 1.00177.38 O ANISOU 1576 O ALA A1001 22500 24720 20175 4433 -435 210 O ATOM 1577 CB ALA A1001 186.320 11.043 562.589 1.00174.63 C ANISOU 1577 CB ALA A1001 21812 23874 20664 5163 28 -119 C ATOM 1578 N ASP A1002 183.885 10.366 564.354 1.00174.57 N ANISOU 1578 N ASP A1002 21851 24484 19993 4256 -1089 262 N ATOM 1579 CA ASP A1002 182.615 9.685 564.585 1.00173.88 C ANISOU 1579 CA ASP A1002 22057 24498 19509 3940 -1610 509 C ATOM 1580 C ASP A1002 181.660 10.561 565.389 1.00169.19 C ANISOU 1580 C ASP A1002 21106 24391 18787 3553 -1622 557 C ATOM 1581 O ASP A1002 180.504 10.757 564.995 1.00172.77 O ANISOU 1581 O ASP A1002 21772 24911 18962 3395 -1681 668 O ATOM 1582 CB ASP A1002 182.862 8.353 565.297 1.00179.75 C ANISOU 1582 CB ASP A1002 22901 25173 20223 3843 -2189 664 C ATOM 1583 CG ASP A1002 181.719 7.370 565.118 1.00185.65 C ANISOU 1583 CG ASP A1002 24106 25814 20621 3627 -2718 937 C ATOM 1584 OD1 ASP A1002 180.547 7.801 565.124 1.00187.22 O ANISOU 1584 OD1 ASP A1002 24318 26235 20582 3357 -2759 1050 O ATOM 1585 OD2 ASP A1002 181.995 6.162 564.969 1.00188.77 O ANISOU 1585 OD2 ASP A1002 24833 25885 21005 3729 -3107 1034 O ATOM 1586 N LEU A1003 182.132 11.097 566.519 1.00154.73 N ANISOU 1586 N LEU A1003 18725 22908 17159 3418 -1580 452 N ATOM 1587 CA LEU A1003 181.307 11.999 567.316 1.00144.60 C ANISOU 1587 CA LEU A1003 17068 22113 15761 3098 -1565 448 C ATOM 1588 C LEU A1003 180.900 13.232 566.520 1.00148.63 C ANISOU 1588 C LEU A1003 17550 22614 16307 3181 -1076 311 C ATOM 1589 O LEU A1003 179.827 13.800 566.758 1.00146.95 O ANISOU 1589 O LEU A1003 17246 22707 15883 2935 -1113 362 O ATOM 1590 CB LEU A1003 182.055 12.407 568.586 1.00136.28 C ANISOU 1590 CB LEU A1003 15437 21396 14948 3027 -1582 294 C ATOM 1591 CG LEU A1003 181.257 13.161 569.652 1.00128.35 C ANISOU 1591 CG LEU A1003 14025 20958 13785 2705 -1669 283 C ATOM 1592 CD1 LEU A1003 180.247 12.240 570.322 1.00129.34 C ANISOU 1592 CD1 LEU A1003 14312 21338 13495 2374 -2198 612 C ATOM 1593 CD2 LEU A1003 182.189 13.783 570.680 1.00118.48 C ANISOU 1593 CD2 LEU A1003 12204 19967 12844 2747 -1588 27 C ATOM 1594 N GLU A1004 181.742 13.659 565.575 1.00149.27 N ANISOU 1594 N GLU A1004 17704 22354 16658 3533 -610 150 N ATOM 1595 CA GLU A1004 181.367 14.751 564.682 1.00152.64 C ANISOU 1595 CA GLU A1004 18183 22708 17105 3644 -141 67 C ATOM 1596 C GLU A1004 180.136 14.387 563.862 1.00153.84 C ANISOU 1596 C GLU A1004 18860 22756 16835 3588 -319 252 C ATOM 1597 O GLU A1004 179.226 15.208 563.695 1.00151.76 O ANISOU 1597 O GLU A1004 18559 22666 16437 3461 -199 251 O ATOM 1598 CB GLU A1004 182.539 15.099 563.763 1.00154.60 C ANISOU 1598 CB GLU A1004 18462 22581 17697 4051 389 -76 C ATOM 1599 CG GLU A1004 183.829 15.440 564.493 1.00148.00 C ANISOU 1599 CG GLU A1004 17088 21797 17348 4127 568 -275 C ATOM 1600 CD GLU A1004 183.786 16.805 565.151 1.00141.81 C ANISOU 1600 CD GLU A1004 15740 21314 16829 3969 814 -454 C ATOM 1601 OE1 GLU A1004 183.067 17.690 564.642 1.00140.18 O ANISOU 1601 OE1 GLU A1004 15584 21141 16538 3934 1072 -451 O ATOM 1602 OE2 GLU A1004 184.470 16.992 566.179 1.00140.81 O ANISOU 1602 OE2 GLU A1004 15123 21381 16998 3895 726 -612 O ATOM 1603 N ASP A1005 180.090 13.157 563.344 1.00156.07 N ANISOU 1603 N ASP A1005 19633 22743 16925 3692 -635 395 N ATOM 1604 CA ASP A1005 178.922 12.714 562.591 1.00155.37 C ANISOU 1604 CA ASP A1005 20046 22529 16458 3638 -884 555 C ATOM 1605 C ASP A1005 177.708 12.537 563.493 1.00148.84 C ANISOU 1605 C ASP A1005 19079 22083 15390 3183 -1333 726 C ATOM 1606 O ASP A1005 176.576 12.789 563.061 1.00148.06 O ANISOU 1606 O ASP A1005 19166 22041 15050 3065 -1404 802 O ATOM 1607 CB ASP A1005 179.232 11.410 561.855 1.00161.45 C ANISOU 1607 CB ASP A1005 21359 22864 17121 3878 -1153 633 C ATOM 1608 CG ASP A1005 180.416 11.537 560.916 1.00162.08 C ANISOU 1608 CG ASP A1005 21591 22588 17403 4362 -687 471 C ATOM 1609 OD1 ASP A1005 180.691 12.663 560.451 1.00159.78 O ANISOU 1609 OD1 ASP A1005 21141 22316 17254 4525 -133 350 O ATOM 1610 OD2 ASP A1005 181.071 10.510 560.640 1.00163.75 O ANISOU 1610 OD2 ASP A1005 22075 22501 17643 4584 -871 473 O ATOM 1611 N ASN A1006 177.918 12.104 564.738 1.00143.65 N ANISOU 1611 N ASN A1006 18093 21699 14787 2936 -1635 798 N ATOM 1612 CA ASN A1006 176.808 11.979 565.679 1.00133.65 C ANISOU 1612 CA ASN A1006 16640 20852 13287 2507 -2011 985 C ATOM 1613 C ASN A1006 176.172 13.337 565.955 1.00126.24 C ANISOU 1613 C ASN A1006 15329 20305 12330 2371 -1716 861 C ATOM 1614 O ASN A1006 174.962 13.523 565.771 1.00121.61 O ANISOU 1614 O ASN A1006 14838 19864 11504 2180 -1834 965 O ATOM 1615 CB ASN A1006 177.292 11.334 566.979 1.00124.97 C ANISOU 1615 CB ASN A1006 15246 19992 12243 2321 -2334 1083 C ATOM 1616 CG ASN A1006 177.517 9.842 566.844 1.00121.64 C ANISOU 1616 CG ASN A1006 15220 19230 11770 2345 -2782 1290 C ATOM 1617 OD1 ASN A1006 178.624 9.393 566.549 1.00121.47 O ANISOU 1617 OD1 ASN A1006 15318 18882 11955 2635 -2723 1189 O ATOM 1618 ND2 ASN A1006 176.465 9.063 567.066 1.00120.13 N ANISOU 1618 ND2 ASN A1006 15216 19101 11326 2040 -3241 1583 N ATOM 1619 N TRP A1007 176.981 14.303 566.400 1.00121.13 N ANISOU 1619 N TRP A1007 14243 19818 11964 2473 -1349 622 N ATOM 1620 CA TRP A1007 176.456 15.637 566.673 1.00119.03 C ANISOU 1620 CA TRP A1007 13608 19892 11726 2374 -1075 467 C ATOM 1621 C TRP A1007 175.871 16.263 565.414 1.00122.95 C ANISOU 1621 C TRP A1007 14414 20146 12153 2530 -788 433 C ATOM 1622 O TRP A1007 174.863 16.979 565.479 1.00126.10 O ANISOU 1622 O TRP A1007 14699 20804 12409 2371 -763 421 O ATOM 1623 CB TRP A1007 177.553 16.525 567.261 1.00119.23 C ANISOU 1623 CB TRP A1007 13133 20032 12137 2498 -746 191 C ATOM 1624 CG TRP A1007 177.025 17.774 567.891 1.00125.44 C ANISOU 1624 CG TRP A1007 13464 21239 12956 2349 -592 20 C ATOM 1625 CD1 TRP A1007 177.178 19.052 567.439 1.00130.70 C ANISOU 1625 CD1 TRP A1007 13948 21838 13876 2496 -147 -203 C ATOM 1626 CD2 TRP A1007 176.245 17.864 569.089 1.00128.54 C ANISOU 1626 CD2 TRP A1007 13530 22188 13120 2039 -887 58 C ATOM 1627 NE1 TRP A1007 176.547 19.933 568.285 1.00135.77 N ANISOU 1627 NE1 TRP A1007 14171 22941 14476 2303 -174 -336 N ATOM 1628 CE2 TRP A1007 175.965 19.227 569.305 1.00132.59 C ANISOU 1628 CE2 TRP A1007 13671 22948 13759 2033 -613 -186 C ATOM 1629 CE3 TRP A1007 175.759 16.923 570.001 1.00120.90 C ANISOU 1629 CE3 TRP A1007 12549 21536 11853 1775 -1347 290 C ATOM 1630 CZ2 TRP A1007 175.221 19.672 570.395 1.00125.00 C ANISOU 1630 CZ2 TRP A1007 12328 22557 12611 1797 -787 -239 C ATOM 1631 CZ3 TRP A1007 175.017 17.365 571.079 1.00119.03 C ANISOU 1631 CZ3 TRP A1007 11929 21880 11416 1530 -1488 274 C ATOM 1632 CH2 TRP A1007 174.757 18.727 571.269 1.00118.30 C ANISOU 1632 CH2 TRP A1007 11471 22043 11432 1555 -1209 -5 C ATOM 1633 N GLU A1008 176.489 15.998 564.259 1.00120.06 N ANISOU 1633 N GLU A1008 14448 19297 11873 2864 -571 415 N ATOM 1634 CA GLU A1008 175.921 16.431 562.985 1.00122.70 C ANISOU 1634 CA GLU A1008 15169 19377 12074 3050 -343 418 C ATOM 1635 C GLU A1008 174.499 15.911 562.816 1.00125.47 C ANISOU 1635 C GLU A1008 15814 19815 12044 2823 -767 606 C ATOM 1636 O GLU A1008 173.577 16.673 562.503 1.00130.76 O ANISOU 1636 O GLU A1008 16482 20610 12589 2761 -676 584 O ATOM 1637 CB GLU A1008 176.807 15.958 561.833 1.00122.81 C ANISOU 1637 CB GLU A1008 15619 18881 12162 3460 -121 404 C ATOM 1638 CG GLU A1008 176.104 15.920 560.486 1.00117.41 C ANISOU 1638 CG GLU A1008 15499 17907 11204 3665 -71 468 C ATOM 1639 CD GLU A1008 176.874 15.126 559.450 1.00122.79 C ANISOU 1639 CD GLU A1008 16673 18123 11858 4063 11 477 C ATOM 1640 OE1 GLU A1008 178.116 15.053 559.557 1.00123.33 O ANISOU 1640 OE1 GLU A1008 16581 18067 12211 4258 266 390 O ATOM 1641 OE2 GLU A1008 176.236 14.568 558.532 1.00129.63 O ANISOU 1641 OE2 GLU A1008 18080 18751 12422 4195 -194 555 O ATOM 1642 N THR A1009 174.306 14.606 563.026 1.00123.27 N ANISOU 1642 N THR A1009 15775 19455 11607 2694 -1249 795 N ATOM 1643 CA THR A1009 172.969 14.026 562.949 1.00120.29 C ANISOU 1643 CA THR A1009 15629 19150 10926 2438 -1695 993 C ATOM 1644 C THR A1009 172.023 14.697 563.938 1.00121.72 C ANISOU 1644 C THR A1009 15345 19880 11023 2069 -1772 1024 C ATOM 1645 O THR A1009 170.846 14.931 563.627 1.00130.25 O ANISOU 1645 O THR A1009 16517 21061 11911 1935 -1892 1086 O ATOM 1646 CB THR A1009 173.042 12.520 563.209 1.00117.45 C ANISOU 1646 CB THR A1009 15514 18619 10492 2323 -2210 1204 C ATOM 1647 OG1 THR A1009 174.045 11.938 562.366 1.00123.46 O ANISOU 1647 OG1 THR A1009 16663 18894 11352 2705 -2118 1131 O ATOM 1648 CG2 THR A1009 171.706 11.856 562.921 1.00114.38 C ANISOU 1648 CG2 THR A1009 15418 18193 9848 2092 -2675 1413 C ATOM 1649 N LEU A1010 172.528 15.034 565.129 1.00116.87 N ANISOU 1649 N LEU A1010 14223 19635 10548 1928 -1704 961 N ATOM 1650 CA LEU A1010 171.682 15.658 566.143 1.00112.44 C ANISOU 1650 CA LEU A1010 13202 19639 9880 1611 -1772 969 C ATOM 1651 C LEU A1010 171.187 17.025 565.684 1.00116.51 C ANISOU 1651 C LEU A1010 13586 20253 10429 1703 -1410 766 C ATOM 1652 O LEU A1010 169.979 17.291 565.685 1.00123.34 O ANISOU 1652 O LEU A1010 14418 21349 11096 1516 -1541 831 O ATOM 1653 CB LEU A1010 172.440 15.774 567.467 1.00115.08 C ANISOU 1653 CB LEU A1010 13046 20332 10346 1513 -1766 898 C ATOM 1654 CG LEU A1010 172.957 14.475 568.093 1.00121.59 C ANISOU 1654 CG LEU A1010 13946 21111 11140 1413 -2140 1108 C ATOM 1655 CD1 LEU A1010 173.200 14.649 569.585 1.00123.48 C ANISOU 1655 CD1 LEU A1010 13667 21878 11373 1225 -2230 1090 C ATOM 1656 CD2 LEU A1010 172.005 13.323 567.836 1.00120.72 C ANISOU 1656 CD2 LEU A1010 14205 20881 10781 1195 -2594 1441 C ATOM 1657 N ASN A1011 172.107 17.910 565.282 1.00129.72 N ANISOU 1657 N ASN A1011 15170 21742 12377 1992 -953 528 N ATOM 1658 CA ASN A1011 171.682 19.233 564.836 1.00132.74 C ANISOU 1658 CA ASN A1011 15433 22177 12826 2088 -608 350 C ATOM 1659 C ASN A1011 170.919 19.181 563.519 1.00132.54 C ANISOU 1659 C ASN A1011 15920 21827 12610 2227 -605 434 C ATOM 1660 O ASN A1011 170.220 20.143 563.186 1.00139.26 O ANISOU 1660 O ASN A1011 16713 22769 13431 2248 -439 343 O ATOM 1661 CB ASN A1011 172.879 20.186 564.718 1.00139.78 C ANISOU 1661 CB ASN A1011 16090 22911 14110 2349 -117 106 C ATOM 1662 CG ASN A1011 173.913 19.726 563.703 1.00142.98 C ANISOU 1662 CG ASN A1011 16884 22782 14659 2682 108 131 C ATOM 1663 OD1 ASN A1011 174.998 19.280 564.072 1.00142.13 O ANISOU 1663 OD1 ASN A1011 16663 22582 14757 2760 135 97 O ATOM 1664 ND2 ASN A1011 173.594 19.859 562.420 1.00145.67 N ANISOU 1664 ND2 ASN A1011 17679 22782 14887 2906 277 180 N ATOM 1665 N ASP A1012 171.038 18.090 562.760 1.00124.82 N ANISOU 1665 N ASP A1012 15452 20470 11504 2345 -805 588 N ATOM 1666 CA ASP A1012 170.221 17.941 561.560 1.00113.19 C ANISOU 1666 CA ASP A1012 14486 18713 9807 2476 -892 660 C ATOM 1667 C ASP A1012 168.777 17.618 561.924 1.00111.32 C ANISOU 1667 C ASP A1012 14212 18766 9320 2134 -1335 804 C ATOM 1668 O ASP A1012 167.853 18.373 561.593 1.00111.85 O ANISOU 1668 O ASP A1012 14257 18949 9290 2112 -1282 751 O ATOM 1669 CB ASP A1012 170.806 16.856 560.653 1.00111.50 C ANISOU 1669 CB ASP A1012 14828 18004 9531 2737 -1001 744 C ATOM 1670 CG ASP A1012 172.090 17.293 559.976 1.00114.02 C ANISOU 1670 CG ASP A1012 15253 18003 10068 3143 -490 606 C ATOM 1671 OD1 ASP A1012 172.262 18.510 559.753 1.00104.70 O ANISOU 1671 OD1 ASP A1012 13881 16864 9037 3271 -42 474 O ATOM 1672 OD2 ASP A1012 172.927 16.418 559.667 1.00106.92 O ANISOU 1672 OD2 ASP A1012 14614 16803 9206 3334 -535 638 O ATOM 1673 N ASN A1013 168.564 16.499 562.623 1.00111.63 N ANISOU 1673 N ASN A1013 14222 18921 9270 1859 -1775 1001 N ATOM 1674 CA ASN A1013 167.201 16.077 562.933 1.00113.59 C ANISOU 1674 CA ASN A1013 14433 19414 9311 1518 -2202 1184 C ATOM 1675 C ASN A1013 166.502 17.048 563.878 1.00112.87 C ANISOU 1675 C ASN A1013 13781 19903 9201 1270 -2103 1118 C ATOM 1676 O ASN A1013 165.271 17.175 563.832 1.00103.59 O ANISOU 1676 O ASN A1013 12562 18922 7875 1082 -2300 1189 O ATOM 1677 CB ASN A1013 167.211 14.668 563.525 1.00110.29 C ANISOU 1677 CB ASN A1013 14082 18979 8844 1269 -2671 1446 C ATOM 1678 CG ASN A1013 167.665 13.623 562.526 1.00111.79 C ANISOU 1678 CG ASN A1013 14867 18582 9027 1507 -2867 1504 C ATOM 1679 OD1 ASN A1013 166.848 12.956 561.891 1.00112.02 O ANISOU 1679 OD1 ASN A1013 15253 18381 8928 1456 -3233 1623 O ATOM 1680 ND2 ASN A1013 168.975 13.481 562.376 1.00107.95 N ANISOU 1680 ND2 ASN A1013 14478 17844 8692 1784 -2637 1400 N ATOM 1681 N LEU A1014 167.260 17.745 564.730 1.00112.06 N ANISOU 1681 N LEU A1014 13237 20081 9259 1282 -1814 962 N ATOM 1682 CA LEU A1014 166.641 18.693 565.652 1.00114.60 C ANISOU 1682 CA LEU A1014 13023 20965 9555 1089 -1726 856 C ATOM 1683 C LEU A1014 165.987 19.846 564.900 1.00121.53 C ANISOU 1683 C LEU A1014 13930 21806 10439 1239 -1485 675 C ATOM 1684 O LEU A1014 164.929 20.341 565.306 1.00118.73 O ANISOU 1684 O LEU A1014 13302 21844 9967 1051 -1571 658 O ATOM 1685 CB LEU A1014 167.677 19.212 566.649 1.00103.04 C ANISOU 1685 CB LEU A1014 11113 19753 8285 1124 -1490 679 C ATOM 1686 CG LEU A1014 167.117 20.003 567.832 1.00101.07 C ANISOU 1686 CG LEU A1014 10283 20145 7973 919 -1474 566 C ATOM 1687 CD1 LEU A1014 165.997 19.228 568.508 1.00102.24 C ANISOU 1687 CD1 LEU A1014 10331 20689 7825 556 -1875 850 C ATOM 1688 CD2 LEU A1014 168.220 20.320 568.827 1.00115.24 C ANISOU 1688 CD2 LEU A1014 11685 22150 9952 971 -1326 390 C ATOM 1689 N LYS A1015 166.600 20.287 563.799 1.00125.00 N ANISOU 1689 N LYS A1015 14699 21785 11011 1589 -1175 548 N ATOM 1690 CA LYS A1015 165.959 21.280 562.944 1.00132.16 C ANISOU 1690 CA LYS A1015 15727 22588 11901 1757 -976 422 C ATOM 1691 C LYS A1015 164.920 20.646 562.029 1.00137.70 C ANISOU 1691 C LYS A1015 16890 23075 12356 1745 -1302 581 C ATOM 1692 O LYS A1015 163.961 21.318 561.628 1.00142.12 O ANISOU 1692 O LYS A1015 17456 23714 12831 1758 -1306 518 O ATOM 1693 CB LYS A1015 167.004 22.027 562.111 1.00137.66 C ANISOU 1693 CB LYS A1015 16596 22882 12828 2142 -494 264 C ATOM 1694 CG LYS A1015 167.672 23.202 562.821 1.00136.41 C ANISOU 1694 CG LYS A1015 15921 22936 12974 2177 -124 30 C ATOM 1695 CD LYS A1015 168.646 22.739 563.891 1.00134.84 C ANISOU 1695 CD LYS A1015 15394 22910 12927 2063 -159 9 C ATOM 1696 CE LYS A1015 169.539 23.872 564.361 1.00132.53 C ANISOU 1696 CE LYS A1015 14665 22684 13008 2178 227 -252 C ATOM 1697 NZ LYS A1015 170.639 23.373 565.231 1.00131.61 N ANISOU 1697 NZ LYS A1015 14294 22646 13065 2134 197 -286 N ATOM 1698 N VAL A1016 165.092 19.364 561.688 1.00130.53 N ANISOU 1698 N VAL A1016 16365 21879 11350 1733 -1602 767 N ATOM 1699 CA VAL A1016 164.062 18.654 560.935 1.00129.37 C ANISOU 1699 CA VAL A1016 16622 21538 10995 1686 -2001 908 C ATOM 1700 C VAL A1016 162.752 18.629 561.713 1.00115.06 C ANISOU 1700 C VAL A1016 14446 20196 9076 1289 -2322 1012 C ATOM 1701 O VAL A1016 161.666 18.674 561.120 1.00112.69 O ANISOU 1701 O VAL A1016 14312 19852 8654 1262 -2538 1035 O ATOM 1702 CB VAL A1016 164.544 17.233 560.576 1.00104.58 C ANISOU 1702 CB VAL A1016 13913 18011 7812 1726 -2307 1074 C ATOM 1703 CG1 VAL A1016 163.406 16.398 560.008 1.00106.23 C ANISOU 1703 CG1 VAL A1016 14460 18054 7847 1604 -2818 1224 C ATOM 1704 CG2 VAL A1016 165.688 17.301 559.579 1.00104.79 C ANISOU 1704 CG2 VAL A1016 14357 17557 7902 2179 -1976 958 C ATOM 1705 N ILE A1017 162.828 18.577 563.046 1.00107.67 N ANISOU 1705 N ILE A1017 12999 19731 8178 993 -2352 1073 N ATOM 1706 CA ILE A1017 161.617 18.642 563.862 1.00105.75 C ANISOU 1706 CA ILE A1017 12349 20006 7824 631 -2587 1176 C ATOM 1707 C ILE A1017 160.873 19.948 563.613 1.00106.76 C ANISOU 1707 C ILE A1017 12284 20336 7944 725 -2375 957 C ATOM 1708 O ILE A1017 159.641 19.966 563.490 1.00114.93 O ANISOU 1708 O ILE A1017 13262 21535 8871 566 -2612 1019 O ATOM 1709 CB ILE A1017 161.963 18.463 565.352 1.00109.05 C ANISOU 1709 CB ILE A1017 12259 20926 8250 363 -2590 1260 C ATOM 1710 CG1 ILE A1017 162.456 17.041 565.621 1.00109.37 C ANISOU 1710 CG1 ILE A1017 12499 20777 8279 218 -2899 1536 C ATOM 1711 CG2 ILE A1017 160.760 18.788 566.227 1.00104.28 C ANISOU 1711 CG2 ILE A1017 11171 20936 7516 45 -2716 1325 C ATOM 1712 CD1 ILE A1017 162.653 16.735 567.090 1.00105.79 C ANISOU 1712 CD1 ILE A1017 11583 20834 7781 -63 -2967 1681 C ATOM 1713 N GLU A1018 161.605 21.062 563.525 1.00112.86 N ANISOU 1713 N GLU A1018 12942 21080 8860 986 -1937 700 N ATOM 1714 CA GLU A1018 160.957 22.348 563.290 1.00135.41 C ANISOU 1714 CA GLU A1018 15618 24092 11740 1097 -1735 484 C ATOM 1715 C GLU A1018 160.441 22.458 561.861 1.00150.89 C ANISOU 1715 C GLU A1018 18099 25605 13628 1339 -1785 473 C ATOM 1716 O GLU A1018 159.342 22.977 561.631 1.00148.29 O ANISOU 1716 O GLU A1018 17696 25426 13222 1306 -1890 417 O ATOM 1717 CB GLU A1018 161.924 23.491 563.602 1.00137.83 C ANISOU 1717 CB GLU A1018 15652 24444 12272 1300 -1275 222 C ATOM 1718 CG GLU A1018 161.345 24.875 563.345 1.00135.56 C ANISOU 1718 CG GLU A1018 15189 24264 12055 1439 -1060 -12 C ATOM 1719 CD GLU A1018 162.292 25.990 563.740 1.00130.85 C ANISOU 1719 CD GLU A1018 14277 23702 11739 1608 -644 -271 C ATOM 1720 OE1 GLU A1018 163.227 25.728 564.526 1.00124.53 O ANISOU 1720 OE1 GLU A1018 13251 23010 11053 1548 -570 -291 O ATOM 1721 OE2 GLU A1018 162.102 27.130 563.264 1.00127.88 O ANISOU 1721 OE2 GLU A1018 13875 23226 11488 1804 -412 -455 O ATOM 1722 N LYS A1019 161.211 21.970 560.886 1.00165.64 N ANISOU 1722 N LYS A1019 20498 26934 15503 1608 -1718 518 N ATOM 1723 CA LYS A1019 160.787 22.046 559.492 1.00169.55 C ANISOU 1723 CA LYS A1019 21536 27001 15883 1891 -1767 503 C ATOM 1724 C LYS A1019 159.694 21.043 559.143 1.00173.24 C ANISOU 1724 C LYS A1019 22253 27404 16167 1716 -2309 670 C ATOM 1725 O LYS A1019 159.200 21.070 558.009 1.00181.00 O ANISOU 1725 O LYS A1019 23684 28059 17028 1946 -2426 641 O ATOM 1726 CB LYS A1019 161.983 21.828 558.562 1.00172.04 C ANISOU 1726 CB LYS A1019 22342 26790 16236 2267 -1504 495 C ATOM 1727 CG LYS A1019 162.293 20.362 558.304 1.00174.68 C ANISOU 1727 CG LYS A1019 23062 26837 16472 2242 -1838 669 C ATOM 1728 CD LYS A1019 163.366 20.184 557.244 1.00173.92 C ANISOU 1728 CD LYS A1019 23487 26225 16369 2673 -1574 639 C ATOM 1729 CE LYS A1019 164.710 20.701 557.723 1.00172.36 C ANISOU 1729 CE LYS A1019 23016 26054 16419 2777 -1086 556 C ATOM 1730 NZ LYS A1019 165.784 20.443 556.725 1.00173.57 N ANISOU 1730 NZ LYS A1019 23646 25728 16575 3190 -813 552 N ATOM 1731 N ALA A1020 159.302 20.177 560.075 1.00152.36 N ANISOU 1731 N ALA A1020 19331 25052 13507 1325 -2646 848 N ATOM 1732 CA ALA A1020 158.368 19.102 559.765 1.00138.84 C ANISOU 1732 CA ALA A1020 17845 23219 11689 1132 -3183 1036 C ATOM 1733 C ALA A1020 156.995 19.649 559.389 1.00134.13 C ANISOU 1733 C ALA A1020 17178 22764 11021 1087 -3366 972 C ATOM 1734 O ALA A1020 156.468 20.557 560.040 1.00129.46 O ANISOU 1734 O ALA A1020 16102 22626 10460 963 -3210 876 O ATOM 1735 CB ALA A1020 158.246 18.152 560.954 1.00140.70 C ANISOU 1735 CB ALA A1020 17727 23776 11956 693 -3460 1279 C ATOM 1736 N ASP A1021 156.419 19.082 558.327 1.00140.90 N ANISOU 1736 N ASP A1021 18523 23226 11788 1210 -3720 1004 N ATOM 1737 CA ASP A1021 155.101 19.460 557.832 1.00141.89 C ANISOU 1737 CA ASP A1021 18648 23410 11853 1195 -3972 941 C ATOM 1738 C ASP A1021 153.991 18.562 558.358 1.00147.45 C ANISOU 1738 C ASP A1021 19100 24327 12598 751 -4494 1150 C ATOM 1739 O ASP A1021 152.909 19.055 558.692 1.00146.85 O ANISOU 1739 O ASP A1021 18638 24619 12542 563 -4593 1128 O ATOM 1740 CB ASP A1021 155.084 19.435 556.300 1.00142.20 C ANISOU 1740 CB ASP A1021 19383 22886 11760 1631 -4074 828 C ATOM 1741 CG ASP A1021 156.158 20.312 555.687 1.00141.15 C ANISOU 1741 CG ASP A1021 19522 22522 11588 2082 -3532 668 C ATOM 1742 OD1 ASP A1021 156.528 21.328 556.309 1.00136.78 O ANISOU 1742 OD1 ASP A1021 18565 22269 11138 2073 -3100 574 O ATOM 1743 OD2 ASP A1021 156.637 19.983 554.581 1.00142.98 O ANISOU 1743 OD2 ASP A1021 20366 22267 11692 2454 -3538 636 O ATOM 1744 N ASN A1022 154.230 17.254 558.436 1.00152.95 N ANISOU 1744 N ASN A1022 19992 24792 13331 581 -4832 1361 N ATOM 1745 CA ASN A1022 153.274 16.285 558.935 1.00152.76 C ANISOU 1745 CA ASN A1022 19741 24907 13395 136 -5335 1613 C ATOM 1746 C ASN A1022 153.787 15.711 560.260 1.00150.98 C ANISOU 1746 C ASN A1022 19106 25019 13241 -226 -5268 1860 C ATOM 1747 O ASN A1022 154.547 16.387 560.977 1.00148.13 O ANISOU 1747 O ASN A1022 18457 24969 12855 -179 -4820 1783 O ATOM 1748 CB ASN A1022 153.028 15.232 557.857 1.00156.95 C ANISOU 1748 CB ASN A1022 20865 24836 13932 248 -5850 1653 C ATOM 1749 CG ASN A1022 154.295 14.503 557.456 1.00161.57 C ANISOU 1749 CG ASN A1022 21943 24957 14487 494 -5809 1662 C ATOM 1750 OD1 ASN A1022 155.392 15.054 557.529 1.00164.65 O ANISOU 1750 OD1 ASN A1022 22380 25357 14821 745 -5326 1549 O ATOM 1751 ND2 ASN A1022 154.147 13.254 557.029 1.00162.81 N ANISOU 1751 ND2 ASN A1022 22457 24695 14708 427 -6328 1787 N ATOM 1752 N ALA A1023 153.382 14.485 560.583 1.00146.37 N ANISOU 1752 N ALA A1023 18498 24362 12754 -577 -5723 2154 N ATOM 1753 CA ALA A1023 153.711 13.877 561.865 1.00139.19 C ANISOU 1753 CA ALA A1023 17213 23701 11971 -921 -5647 2401 C ATOM 1754 C ALA A1023 154.817 12.836 561.783 1.00135.93 C ANISOU 1754 C ALA A1023 17172 22918 11557 -867 -5801 2547 C ATOM 1755 O ALA A1023 155.519 12.622 562.775 1.00134.17 O ANISOU 1755 O ALA A1023 16699 22920 11362 -1008 -5609 2678 O ATOM 1756 CB ALA A1023 152.465 13.231 562.480 1.00143.96 C ANISOU 1756 CB ALA A1023 17462 24422 12814 -1358 -5905 2631 C ATOM 1757 N ALA A1024 154.994 12.179 560.634 1.00147.61 N ANISOU 1757 N ALA A1024 19259 23790 13034 -633 -6127 2494 N ATOM 1758 CA ALA A1024 156.005 11.130 560.538 1.00158.41 C ANISOU 1758 CA ALA A1024 20997 24734 14457 -552 -6277 2597 C ATOM 1759 C ALA A1024 157.419 11.689 560.651 1.00176.33 C ANISOU 1759 C ALA A1024 23338 27009 16651 -219 -5751 2415 C ATOM 1760 O ALA A1024 158.316 11.006 561.163 1.00159.55 O ANISOU 1760 O ALA A1024 21239 24802 14583 -267 -5756 2548 O ATOM 1761 CB ALA A1024 155.844 10.361 559.227 1.00147.86 C ANISOU 1761 CB ALA A1024 20314 22719 13147 -308 -6723 2509 C ATOM 1762 N GLN A1025 157.633 12.923 560.190 1.00192.34 N ANISOU 1762 N GLN A1025 25382 29119 18578 113 -5306 2122 N ATOM 1763 CA GLN A1025 158.975 13.496 560.203 1.00193.40 C ANISOU 1763 CA GLN A1025 25579 29211 18693 439 -4801 1944 C ATOM 1764 C GLN A1025 159.474 13.717 561.625 1.00190.91 C ANISOU 1764 C GLN A1025 24698 29408 18432 181 -4551 2047 C ATOM 1765 O GLN A1025 160.664 13.526 561.906 1.00192.63 O ANISOU 1765 O GLN A1025 24961 29530 18702 313 -4350 2027 O ATOM 1766 CB GLN A1025 158.993 14.806 559.414 1.00195.42 C ANISOU 1766 CB GLN A1025 25944 29442 18866 817 -4391 1645 C ATOM 1767 CG GLN A1025 158.586 14.654 557.957 1.00201.25 C ANISOU 1767 CG GLN A1025 27287 29679 19498 1145 -4608 1524 C ATOM 1768 CD GLN A1025 158.679 15.954 557.182 1.00202.03 C ANISOU 1768 CD GLN A1025 27517 29743 19503 1537 -4175 1268 C ATOM 1769 OE1 GLN A1025 159.360 16.891 557.599 1.00202.09 O ANISOU 1769 OE1 GLN A1025 27249 29973 19563 1632 -3672 1162 O ATOM 1770 NE2 GLN A1025 157.991 16.018 556.048 1.00201.47 N ANISOU 1770 NE2 GLN A1025 27870 29375 19304 1773 -4388 1170 N ATOM 1771 N VAL A1026 158.585 14.114 562.540 1.00182.58 N ANISOU 1771 N VAL A1026 23104 28912 17357 -167 -4567 2149 N ATOM 1772 CA VAL A1026 159.022 14.333 563.915 1.00169.20 C ANISOU 1772 CA VAL A1026 20880 27741 15665 -383 -4348 2234 C ATOM 1773 C VAL A1026 159.360 13.007 564.588 1.00161.50 C ANISOU 1773 C VAL A1026 19918 26709 14737 -653 -4672 2564 C ATOM 1774 O VAL A1026 160.277 12.943 565.413 1.00156.56 O ANISOU 1774 O VAL A1026 19098 26263 14123 -665 -4496 2596 O ATOM 1775 CB VAL A1026 157.968 15.129 564.715 1.00161.09 C ANISOU 1775 CB VAL A1026 19274 27365 14570 -645 -4263 2240 C ATOM 1776 CG1 VAL A1026 157.486 16.329 563.919 1.00156.48 C ANISOU 1776 CG1 VAL A1026 18738 26758 13961 -381 -4036 1933 C ATOM 1777 CG2 VAL A1026 156.795 14.252 565.132 1.00161.79 C ANISOU 1777 CG2 VAL A1026 19210 27521 14740 -1064 -4645 2543 C ATOM 1778 N LYS A1027 158.657 11.927 564.235 1.00157.99 N ANISOU 1778 N LYS A1027 19706 25983 14340 -861 -5170 2809 N ATOM 1779 CA LYS A1027 158.955 10.633 564.841 1.00153.67 C ANISOU 1779 CA LYS A1027 19196 25302 13889 -1114 -5489 3135 C ATOM 1780 C LYS A1027 160.251 10.052 564.291 1.00153.27 C ANISOU 1780 C LYS A1027 19623 24731 13884 -794 -5508 3052 C ATOM 1781 O LYS A1027 161.070 9.521 565.050 1.00153.13 O ANISOU 1781 O LYS A1027 19513 24767 13903 -867 -5507 3197 O ATOM 1782 CB LYS A1027 157.794 9.663 564.624 1.00158.86 C ANISOU 1782 CB LYS A1027 19949 25671 14739 -1398 -5930 3348 C ATOM 1783 CG LYS A1027 156.656 9.816 565.623 1.00160.51 C ANISOU 1783 CG LYS A1027 19601 26342 15043 -1798 -5849 3520 C ATOM 1784 CD LYS A1027 155.398 10.344 564.957 1.00158.53 C ANISOU 1784 CD LYS A1027 19307 26112 14816 -1818 -5935 3397 C ATOM 1785 CE LYS A1027 154.948 9.434 563.826 1.00156.53 C ANISOU 1785 CE LYS A1027 19536 25246 14694 -1777 -6444 3432 C ATOM 1786 NZ LYS A1027 153.742 9.963 563.133 1.00160.91 N ANISOU 1786 NZ LYS A1027 20060 25808 15273 -1763 -6557 3286 N ATOM 1787 N ASP A1028 160.456 10.142 562.974 1.00152.32 N ANISOU 1787 N ASP A1028 20017 24092 13766 -409 -5506 2805 N ATOM 1788 CA ASP A1028 161.695 9.640 562.387 1.00149.76 C ANISOU 1788 CA ASP A1028 20147 23264 13489 -49 -5464 2686 C ATOM 1789 C ASP A1028 162.896 10.438 562.882 1.00143.00 C ANISOU 1789 C ASP A1028 19065 22633 12637 166 -4922 2503 C ATOM 1790 O ASP A1028 163.890 9.866 563.352 1.00143.12 O ANISOU 1790 O ASP A1028 19092 22559 12729 198 -4921 2572 O ATOM 1791 CB ASP A1028 161.606 9.684 560.862 1.00153.27 C ANISOU 1791 CB ASP A1028 21178 23175 13884 355 -5528 2448 C ATOM 1792 CG ASP A1028 162.814 9.064 560.189 1.00156.28 C ANISOU 1792 CG ASP A1028 22053 23030 14296 747 -5513 2332 C ATOM 1793 OD1 ASP A1028 162.910 7.819 560.170 1.00160.17 O ANISOU 1793 OD1 ASP A1028 22794 23185 14877 654 -5970 2501 O ATOM 1794 OD2 ASP A1028 163.668 9.820 559.681 1.00154.61 O ANISOU 1794 OD2 ASP A1028 21970 22737 14037 1151 -5041 2078 O ATOM 1795 N ALA A1029 162.815 11.769 562.790 1.00137.89 N ANISOU 1795 N ALA A1029 18195 22263 11932 316 -4477 2263 N ATOM 1796 CA ALA A1029 163.905 12.617 563.263 1.00127.40 C ANISOU 1796 CA ALA A1029 16606 21140 10659 507 -3973 2070 C ATOM 1797 C ALA A1029 164.158 12.409 564.750 1.00125.47 C ANISOU 1797 C ALA A1029 15864 21372 10438 188 -3998 2246 C ATOM 1798 O ALA A1029 165.313 12.399 565.196 1.00132.51 O ANISOU 1798 O ALA A1029 16667 22260 11420 319 -3801 2177 O ATOM 1799 CB ALA A1029 163.594 14.084 562.971 1.00124.77 C ANISOU 1799 CB ALA A1029 16085 21031 10293 668 -3553 1809 C ATOM 1800 N LEU A1030 163.090 12.238 565.533 1.00137.21 N ANISOU 1800 N LEU A1030 17014 23282 11838 -219 -4237 2478 N ATOM 1801 CA LEU A1030 163.249 11.935 566.951 1.00112.48 C ANISOU 1801 CA LEU A1030 13443 20622 8672 -522 -4295 2694 C ATOM 1802 C LEU A1030 164.035 10.644 567.145 1.00130.88 C ANISOU 1802 C LEU A1030 16023 22622 11084 -553 -4589 2916 C ATOM 1803 O LEU A1030 165.125 10.649 567.724 1.00136.84 O ANISOU 1803 O LEU A1030 16662 23440 11890 -437 -4425 2854 O ATOM 1804 CB LEU A1030 161.881 11.844 567.632 1.00113.98 C ANISOU 1804 CB LEU A1030 13276 21288 8742 -949 -4517 2957 C ATOM 1805 CG LEU A1030 161.330 13.109 568.299 1.00112.64 C ANISOU 1805 CG LEU A1030 12583 21734 8482 -1009 -4176 2783 C ATOM 1806 CD1 LEU A1030 159.942 12.852 568.866 1.00114.74 C ANISOU 1806 CD1 LEU A1030 12592 22181 8822 -1381 -4281 2982 C ATOM 1807 CD2 LEU A1030 162.267 13.606 569.382 1.00112.46 C ANISOU 1807 CD2 LEU A1030 12188 22114 8426 -948 -3889 2670 C ATOM 1808 N THR A1031 163.505 9.528 566.635 1.00123.30 N ANISOU 1808 N THR A1031 15413 21273 10161 -692 -5049 3156 N ATOM 1809 CA THR A1031 164.110 8.222 566.892 1.00126.45 C ANISOU 1809 CA THR A1031 16033 21359 10653 -767 -5399 3407 C ATOM 1810 C THR A1031 165.561 8.169 566.422 1.00128.91 C ANISOU 1810 C THR A1031 16639 21271 11069 -339 -5199 3157 C ATOM 1811 O THR A1031 166.456 7.775 567.181 1.00132.85 O ANISOU 1811 O THR A1031 17021 21838 11620 -342 -5200 3236 O ATOM 1812 CB THR A1031 163.288 7.121 566.220 1.00131.98 C ANISOU 1812 CB THR A1031 17105 21615 11426 -936 -5938 3640 C ATOM 1813 OG1 THR A1031 163.104 7.437 564.835 1.00132.35 O ANISOU 1813 OG1 THR A1031 17573 21233 11480 -611 -5904 3354 O ATOM 1814 CG2 THR A1031 161.930 6.985 566.894 1.00132.71 C ANISOU 1814 CG2 THR A1031 16839 22028 11557 -1380 -6064 3891 C ATOM 1815 N LYS A1032 165.815 8.562 565.170 1.00134.76 N ANISOU 1815 N LYS A1032 17761 21604 11837 46 -5021 2860 N ATOM 1816 CA LYS A1032 167.184 8.522 564.663 1.00133.57 C ANISOU 1816 CA LYS A1032 17878 21081 11791 470 -4792 2630 C ATOM 1817 C LYS A1032 168.088 9.467 565.447 1.00131.43 C ANISOU 1817 C LYS A1032 17171 21195 11570 569 -4317 2450 C ATOM 1818 O LYS A1032 169.239 9.129 565.757 1.00130.28 O ANISOU 1818 O LYS A1032 17025 20929 11546 724 -4254 2408 O ATOM 1819 CB LYS A1032 167.205 8.858 563.172 1.00127.81 C ANISOU 1819 CB LYS A1032 17621 19904 11038 875 -4641 2367 C ATOM 1820 CG LYS A1032 168.589 8.808 562.544 1.00123.63 C ANISOU 1820 CG LYS A1032 17379 18986 10607 1341 -4369 2142 C ATOM 1821 CD LYS A1032 168.509 8.630 561.036 1.00124.17 C ANISOU 1821 CD LYS A1032 18047 18529 10603 1722 -4405 1981 C ATOM 1822 CE LYS A1032 167.693 9.732 560.383 1.00120.05 C ANISOU 1822 CE LYS A1032 17528 18138 9949 1801 -4151 1835 C ATOM 1823 NZ LYS A1032 167.583 9.534 558.912 1.00116.09 N ANISOU 1823 NZ LYS A1032 17640 17141 9328 2196 -4212 1688 N ATOM 1824 N MET A1033 167.572 10.649 565.797 1.00136.88 N ANISOU 1824 N MET A1033 17472 22346 12190 484 -4010 2329 N ATOM 1825 CA MET A1033 168.346 11.589 566.600 1.00150.77 C ANISOU 1825 CA MET A1033 18782 24484 14021 560 -3605 2136 C ATOM 1826 C MET A1033 168.677 11.016 567.972 1.00162.59 C ANISOU 1826 C MET A1033 19948 26328 15501 304 -3804 2347 C ATOM 1827 O MET A1033 169.683 11.399 568.578 1.00153.04 O ANISOU 1827 O MET A1033 18483 25269 14398 436 -3575 2190 O ATOM 1828 CB MET A1033 167.581 12.904 566.752 1.00151.24 C ANISOU 1828 CB MET A1033 18489 24971 14003 495 -3314 1974 C ATOM 1829 CG MET A1033 168.434 14.070 567.223 1.00151.72 C ANISOU 1829 CG MET A1033 18167 25283 14197 678 -2850 1674 C ATOM 1830 SD MET A1033 167.454 15.423 567.899 1.00147.25 S ANISOU 1830 SD MET A1033 17064 25362 13524 502 -2641 1535 S ATOM 1831 CE MET A1033 165.982 15.313 566.887 1.00146.36 C ANISOU 1831 CE MET A1033 17270 25088 13253 405 -2845 1655 C ATOM 1832 N ARG A1034 167.852 10.101 568.478 1.00181.57 N ANISOU 1832 N ARG A1034 22348 28857 17783 -57 -4234 2711 N ATOM 1833 CA ARG A1034 168.098 9.537 569.798 1.00184.67 C ANISOU 1833 CA ARG A1034 22444 29604 18119 -304 -4428 2963 C ATOM 1834 C ARG A1034 169.032 8.341 569.745 1.00183.05 C ANISOU 1834 C ARG A1034 22555 28951 18043 -206 -4707 3100 C ATOM 1835 O ARG A1034 169.810 8.130 570.684 1.00184.96 O ANISOU 1835 O ARG A1034 22581 29392 18304 -215 -4724 3150 O ATOM 1836 CB ARG A1034 166.781 9.139 570.472 1.00190.92 C ANISOU 1836 CB ARG A1034 23028 30789 18725 -759 -4725 3341 C ATOM 1837 CG ARG A1034 165.780 10.280 570.620 1.00195.96 C ANISOU 1837 CG ARG A1034 23312 31920 19225 -869 -4478 3217 C ATOM 1838 CD ARG A1034 166.469 11.637 570.725 1.00200.32 C ANISOU 1838 CD ARG A1034 23597 32695 19822 -576 -3989 2782 C ATOM 1839 NE ARG A1034 165.536 12.756 570.616 1.00207.93 N ANISOU 1839 NE ARG A1034 24305 34006 20694 -615 -3761 2610 N ATOM 1840 CZ ARG A1034 165.909 14.030 570.539 1.00212.70 C ANISOU 1840 CZ ARG A1034 24697 34752 21366 -374 -3354 2226 C ATOM 1841 NH1 ARG A1034 165.000 14.990 570.447 1.00215.56 N ANISOU 1841 NH1 ARG A1034 24839 35415 21651 -414 -3191 2085 N ATOM 1842 NH2 ARG A1034 167.197 14.346 570.558 1.00212.65 N ANISOU 1842 NH2 ARG A1034 24685 34573 21537 -92 -3119 1981 N ATOM 1843 N ALA A1035 168.977 7.553 568.670 1.00165.68 N ANISOU 1843 N ALA A1035 20869 26152 15931 -89 -4948 3142 N ATOM 1844 CA ALA A1035 170.014 6.551 568.452 1.00156.13 C ANISOU 1844 CA ALA A1035 19988 24459 14875 109 -5156 3172 C ATOM 1845 C ALA A1035 171.377 7.219 568.329 1.00147.06 C ANISOU 1845 C ALA A1035 18763 23241 13872 512 -4729 2807 C ATOM 1846 O ALA A1035 172.343 6.825 568.997 1.00151.76 O ANISOU 1846 O ALA A1035 19247 23850 14565 576 -4781 2828 O ATOM 1847 CB ALA A1035 169.695 5.728 567.205 1.00158.46 C ANISOU 1847 CB ALA A1035 20859 24121 15229 228 -5461 3202 C ATOM 1848 N ALA A1036 171.466 8.257 567.490 1.00143.30 N ANISOU 1848 N ALA A1036 18323 22694 13430 782 -4303 2482 N ATOM 1849 CA ALA A1036 172.699 9.026 567.390 1.00141.97 C ANISOU 1849 CA ALA A1036 18010 22489 13442 1134 -3848 2149 C ATOM 1850 C ALA A1036 173.043 9.737 568.692 1.00143.04 C ANISOU 1850 C ALA A1036 17563 23189 13596 1002 -3669 2084 C ATOM 1851 O ALA A1036 174.220 10.020 568.937 1.00134.35 O ANISOU 1851 O ALA A1036 16297 22056 12695 1233 -3445 1877 O ATOM 1852 CB ALA A1036 172.597 10.045 566.253 1.00112.80 C ANISOU 1852 CB ALA A1036 14456 18628 9773 1413 -3420 1868 C ATOM 1853 N ALA A1037 172.050 10.024 569.536 1.00139.87 N ANISOU 1853 N ALA A1037 16840 23309 12996 653 -3773 2245 N ATOM 1854 CA ALA A1037 172.330 10.684 570.806 1.00140.20 C ANISOU 1854 CA ALA A1037 16341 23920 13009 554 -3636 2167 C ATOM 1855 C ALA A1037 172.940 9.719 571.816 1.00143.36 C ANISOU 1855 C ALA A1037 16664 24412 13395 451 -3961 2388 C ATOM 1856 O ALA A1037 173.852 10.093 572.562 1.00145.82 O ANISOU 1856 O ALA A1037 16665 24934 13806 573 -3829 2212 O ATOM 1857 CB ALA A1037 171.052 11.309 571.361 1.00144.23 C ANISOU 1857 CB ALA A1037 16536 24986 13279 251 -3626 2257 C ATOM 1858 N LEU A1038 172.448 8.478 571.859 1.00148.37 N ANISOU 1858 N LEU A1038 17575 24876 13925 229 -4407 2775 N ATOM 1859 CA LEU A1038 173.037 7.485 572.752 1.00142.74 C ANISOU 1859 CA LEU A1038 16840 24187 13206 144 -4743 3022 C ATOM 1860 C LEU A1038 174.410 7.049 572.256 1.00148.02 C ANISOU 1860 C LEU A1038 17752 24339 14150 510 -4725 2829 C ATOM 1861 O LEU A1038 175.356 6.934 573.048 1.00161.31 O ANISOU 1861 O LEU A1038 19230 26147 15913 607 -4754 2775 O ATOM 1862 CB LEU A1038 172.106 6.282 572.891 1.00139.06 C ANISOU 1862 CB LEU A1038 16602 23634 12599 -207 -5230 3515 C ATOM 1863 CG LEU A1038 170.723 6.558 573.485 1.00144.16 C ANISOU 1863 CG LEU A1038 16973 24820 12982 -604 -5280 3776 C ATOM 1864 CD1 LEU A1038 169.906 5.278 573.560 1.00126.35 C ANISOU 1864 CD1 LEU A1038 14960 22337 10710 -938 -5730 4251 C ATOM 1865 CD2 LEU A1038 170.844 7.203 574.857 1.00123.48 C ANISOU 1865 CD2 LEU A1038 13829 22918 10172 -695 -5127 3763 C ATOM 1866 N ASP A1039 174.540 6.804 570.948 1.00154.55 N ANISOU 1866 N ASP A1039 19012 24596 15114 739 -4679 2711 N ATOM 1867 CA ASP A1039 175.853 6.497 570.390 1.00159.74 C ANISOU 1867 CA ASP A1039 19879 24783 16033 1132 -4590 2489 C ATOM 1868 C ASP A1039 176.821 7.658 570.578 1.00157.40 C ANISOU 1868 C ASP A1039 19206 24674 15924 1392 -4102 2099 C ATOM 1869 O ASP A1039 178.032 7.443 570.703 1.00158.39 O ANISOU 1869 O ASP A1039 19289 24616 16276 1643 -4058 1950 O ATOM 1870 CB ASP A1039 175.724 6.134 568.910 1.00162.30 C ANISOU 1870 CB ASP A1039 20734 24518 16415 1360 -4587 2413 C ATOM 1871 CG ASP A1039 175.108 4.763 568.700 1.00163.94 C ANISOU 1871 CG ASP A1039 21352 24392 16546 1176 -5152 2756 C ATOM 1872 OD1 ASP A1039 173.962 4.547 569.147 1.00161.88 O ANISOU 1872 OD1 ASP A1039 21019 24382 16106 784 -5413 3057 O ATOM 1873 OD2 ASP A1039 175.771 3.900 568.088 1.00166.35 O ANISOU 1873 OD2 ASP A1039 22038 24177 16990 1428 -5340 2722 O ATOM 1874 N ALA A1040 176.310 8.891 570.602 1.00155.43 N ANISOU 1874 N ALA A1040 18667 24772 15617 1338 -3749 1924 N ATOM 1875 CA ALA A1040 177.132 10.037 570.962 1.00150.01 C ANISOU 1875 CA ALA A1040 17553 24310 15135 1525 -3334 1573 C ATOM 1876 C ALA A1040 177.398 10.109 572.459 1.00144.16 C ANISOU 1876 C ALA A1040 16360 24081 14333 1365 -3492 1606 C ATOM 1877 O ALA A1040 178.355 10.771 572.874 1.00144.67 O ANISOU 1877 O ALA A1040 16085 24254 14628 1553 -3266 1313 O ATOM 1878 CB ALA A1040 176.469 11.334 570.495 1.00151.10 C ANISOU 1878 CB ALA A1040 17541 24623 15245 1526 -2938 1374 C ATOM 1879 N GLN A1041 176.575 9.445 573.272 1.00144.28 N ANISOU 1879 N GLN A1041 16357 24414 14048 1031 -3876 1961 N ATOM 1880 CA GLN A1041 176.810 9.408 574.711 1.00146.19 C ANISOU 1880 CA GLN A1041 16217 25161 14167 901 -4053 2033 C ATOM 1881 C GLN A1041 177.918 8.427 575.067 1.00148.21 C ANISOU 1881 C GLN A1041 16582 25160 14572 1045 -4330 2107 C ATOM 1882 O GLN A1041 178.749 8.714 575.936 1.00145.24 O ANISOU 1882 O GLN A1041 15872 25030 14283 1159 -4319 1935 O ATOM 1883 CB GLN A1041 175.517 9.046 575.446 1.00144.47 C ANISOU 1883 CB GLN A1041 15937 25397 13559 497 -4330 2429 C ATOM 1884 CG GLN A1041 175.691 8.686 576.919 1.00146.26 C ANISOU 1884 CG GLN A1041 15876 26120 13577 355 -4593 2625 C ATOM 1885 CD GLN A1041 175.962 9.890 577.804 1.00147.95 C ANISOU 1885 CD GLN A1041 15568 26897 13748 444 -4342 2284 C ATOM 1886 OE1 GLN A1041 176.932 10.621 577.605 1.00155.70 O ANISOU 1886 OE1 GLN A1041 16386 27741 15033 737 -4082 1862 O ATOM 1887 NE2 GLN A1041 175.100 10.100 578.794 1.00141.28 N ANISOU 1887 NE2 GLN A1041 14448 26694 12538 198 -4422 2465 N ATOM 1888 N LYS A1042 177.948 7.267 574.405 1.00147.78 N ANISOU 1888 N LYS A1042 16993 24599 14560 1060 -4606 2342 N ATOM 1889 CA LYS A1042 178.999 6.294 574.686 1.00145.42 C ANISOU 1889 CA LYS A1042 16821 24012 14420 1219 -4892 2407 C ATOM 1890 C LYS A1042 180.367 6.792 574.235 1.00151.80 C ANISOU 1890 C LYS A1042 17528 24538 15613 1635 -4572 1972 C ATOM 1891 O LYS A1042 181.383 6.448 574.849 1.00152.72 O ANISOU 1891 O LYS A1042 17505 24635 15885 1786 -4716 1903 O ATOM 1892 CB LYS A1042 178.666 4.959 574.022 1.00139.67 C ANISOU 1892 CB LYS A1042 16625 22773 13671 1151 -5277 2733 C ATOM 1893 CG LYS A1042 177.361 4.348 574.505 1.00141.33 C ANISOU 1893 CG LYS A1042 16914 23218 13565 714 -5632 3211 C ATOM 1894 CD LYS A1042 177.013 3.090 573.731 1.00144.68 C ANISOU 1894 CD LYS A1042 17867 23067 14039 655 -6022 3492 C ATOM 1895 CE LYS A1042 175.672 2.531 574.174 1.00141.43 C ANISOU 1895 CE LYS A1042 17493 22871 13373 192 -6356 3980 C ATOM 1896 NZ LYS A1042 175.278 1.338 573.376 1.00136.34 N ANISOU 1896 NZ LYS A1042 17354 21625 12825 124 -6768 4231 N ATOM 1897 N ALA A1043 180.417 7.600 573.178 1.00167.90 N ANISOU 1897 N ALA A1043 19618 26357 17817 1825 -4138 1691 N ATOM 1898 CA ALA A1043 181.668 8.167 572.697 1.00170.76 C ANISOU 1898 CA ALA A1043 19845 26463 18571 2206 -3766 1300 C ATOM 1899 C ALA A1043 181.966 9.472 573.423 1.00170.56 C ANISOU 1899 C ALA A1043 19252 26884 18667 2217 -3457 997 C ATOM 1900 O ALA A1043 181.060 10.259 573.709 1.00168.96 O ANISOU 1900 O ALA A1043 18855 27075 18265 2009 -3339 994 O ATOM 1901 CB ALA A1043 181.608 8.408 571.188 1.00171.33 C ANISOU 1901 CB ALA A1043 20260 26079 18759 2426 -3426 1173 C ATOM 1902 N THR A1044 183.248 9.697 573.722 1.00166.55 N ANISOU 1902 N THR A1044 18467 26302 18511 2472 -3346 722 N ATOM 1903 CA THR A1044 183.663 10.874 574.470 1.00159.22 C ANISOU 1903 CA THR A1044 16980 25754 17763 2506 -3117 399 C ATOM 1904 C THR A1044 185.068 11.278 574.042 1.00151.24 C ANISOU 1904 C THR A1044 15772 24406 17287 2863 -2802 47 C ATOM 1905 O THR A1044 185.953 10.410 573.973 1.00150.71 O ANISOU 1905 O THR A1044 15835 24034 17393 3050 -2980 70 O ATOM 1906 CB THR A1044 183.638 10.619 575.979 1.00161.41 C ANISOU 1906 CB THR A1044 16971 26534 17823 2340 -3515 491 C ATOM 1907 OG1 THR A1044 182.376 10.052 576.353 1.00163.89 O ANISOU 1907 OG1 THR A1044 17494 27129 17650 2006 -3817 891 O ATOM 1908 CG2 THR A1044 183.847 11.917 576.745 1.00159.90 C ANISOU 1908 CG2 THR A1044 16217 26778 17760 2363 -3307 133 C ATOM 1909 N PRO A1045 185.308 12.566 573.749 1.00144.94 N ANISOU 1909 N PRO A1045 14647 23642 16782 2964 -2341 -271 N ATOM 1910 CA PRO A1045 186.652 13.043 573.404 1.00139.68 C ANISOU 1910 CA PRO A1045 13713 22679 16681 3278 -2012 -598 C ATOM 1911 C PRO A1045 187.600 13.033 574.600 1.00144.00 C ANISOU 1911 C PRO A1045 13811 23446 17458 3345 -2261 -799 C ATOM 1912 O PRO A1045 187.129 12.941 575.734 1.00147.26 O ANISOU 1912 O PRO A1045 14071 24317 17563 3146 -2619 -726 O ATOM 1913 CB PRO A1045 186.402 14.474 572.920 1.00134.87 C ANISOU 1913 CB PRO A1045 12857 22111 16274 3287 -1506 -826 C ATOM 1914 CG PRO A1045 185.148 14.885 573.610 1.00136.15 C ANISOU 1914 CG PRO A1045 12943 22773 16016 2978 -1680 -733 C ATOM 1915 CD PRO A1045 184.307 13.644 573.676 1.00141.35 C ANISOU 1915 CD PRO A1045 14058 23475 16172 2788 -2100 -329 C ATOM 1916 N PRO A1056 185.027 15.964 588.019 1.00140.32 N ANISOU 1916 N PRO A1056 10785 28483 14049 2595 -4772 -1616 N ATOM 1917 CA PRO A1056 184.917 14.961 586.966 1.00138.47 C ANISOU 1917 CA PRO A1056 10801 28002 13811 2508 -4838 -1209 C ATOM 1918 C PRO A1056 184.050 15.456 585.810 1.00137.39 C ANISOU 1918 C PRO A1056 10678 27825 13700 2372 -4510 -1163 C ATOM 1919 O PRO A1056 182.821 15.421 585.881 1.00133.78 O ANISOU 1919 O PRO A1056 10426 27589 12816 2116 -4400 -867 O ATOM 1920 CB PRO A1056 184.358 13.665 587.528 1.00140.47 C ANISOU 1920 CB PRO A1056 11471 28364 13538 2304 -5109 -612 C ATOM 1921 N GLU A1057 184.706 15.915 584.741 1.00141.99 N ANISOU 1921 N GLU A1057 11105 27998 14845 2533 -4283 -1443 N ATOM 1922 CA GLU A1057 183.984 16.388 583.567 1.00144.86 C ANISOU 1922 CA GLU A1057 11635 28082 15325 2400 -3868 -1387 C ATOM 1923 C GLU A1057 183.301 15.251 582.819 1.00156.10 C ANISOU 1923 C GLU A1057 13599 29243 16469 2190 -3899 -830 C ATOM 1924 O GLU A1057 182.311 15.491 582.118 1.00148.11 O ANISOU 1924 O GLU A1057 12764 28196 15313 2016 -3668 -677 O ATOM 1925 CB GLU A1057 184.934 17.135 582.629 1.00127.99 C ANISOU 1925 CB GLU A1057 9334 25374 13922 2604 -3505 -1777 C ATOM 1926 N MET A1058 183.803 14.021 582.958 1.00172.79 N ANISOU 1926 N MET A1058 15975 31157 18520 2212 -4207 -536 N ATOM 1927 CA MET A1058 183.171 12.884 582.299 1.00175.20 C ANISOU 1927 CA MET A1058 16794 31188 18586 2016 -4301 -15 C ATOM 1928 C MET A1058 181.767 12.640 582.832 1.00174.32 C ANISOU 1928 C MET A1058 16782 31597 17855 1702 -4440 377 C ATOM 1929 O MET A1058 180.894 12.176 582.090 1.00174.34 O ANISOU 1929 O MET A1058 17127 31412 17702 1493 -4385 717 O ATOM 1930 CB MET A1058 184.029 11.632 582.475 1.00189.04 C ANISOU 1930 CB MET A1058 18774 32643 20409 2119 -4654 198 C ATOM 1931 CG MET A1058 185.400 11.715 581.828 1.00196.02 C ANISOU 1931 CG MET A1058 19594 32967 21920 2429 -4508 -139 C ATOM 1932 SD MET A1058 185.326 11.657 580.029 1.00189.27 S ANISOU 1932 SD MET A1058 19115 31406 21393 2467 -4094 -99 S ATOM 1933 CE MET A1058 184.614 10.033 579.776 1.00186.29 C ANISOU 1933 CE MET A1058 19342 30832 20609 2256 -4471 522 C ATOM 1934 N LYS A1059 181.531 12.946 584.110 1.00169.04 N ANISOU 1934 N LYS A1059 15808 31590 16830 1676 -4622 330 N ATOM 1935 CA LYS A1059 180.205 12.748 584.683 1.00152.19 C ANISOU 1935 CA LYS A1059 13867 29724 14235 1351 -4578 691 C ATOM 1936 C LYS A1059 179.208 13.774 584.161 1.00147.71 C ANISOU 1936 C LYS A1059 13181 29317 13626 1240 -4223 541 C ATOM 1937 O LYS A1059 178.018 13.467 584.035 1.00146.81 O ANISOU 1937 O LYS A1059 13292 29255 13235 959 -4151 895 O ATOM 1938 CB LYS A1059 180.277 12.801 586.208 1.00146.41 C ANISOU 1938 CB LYS A1059 13033 29316 13278 1358 -4668 650 C ATOM 1939 CG LYS A1059 181.098 11.681 586.826 1.00145.69 C ANISOU 1939 CG LYS A1059 13114 29081 13160 1432 -5049 876 C ATOM 1940 CD LYS A1059 181.071 11.747 588.343 1.00153.93 C ANISOU 1940 CD LYS A1059 14077 30489 13920 1449 -5132 859 C ATOM 1941 CE LYS A1059 181.841 10.591 588.958 1.00161.97 C ANISOU 1941 CE LYS A1059 15294 31354 14892 1519 -5533 1116 C ATOM 1942 NZ LYS A1059 181.280 9.274 588.549 1.00159.37 N ANISOU 1942 NZ LYS A1059 15389 30755 14409 1268 -5706 1725 N ATOM 1943 N ASP A1060 179.667 14.989 583.855 1.00152.98 N ANISOU 1943 N ASP A1060 13484 30034 14606 1456 -4003 16 N ATOM 1944 CA ASP A1060 178.780 15.986 583.265 1.00151.32 C ANISOU 1944 CA ASP A1060 13165 29932 14398 1378 -3681 -142 C ATOM 1945 C ASP A1060 178.542 15.703 581.786 1.00149.37 C ANISOU 1945 C ASP A1060 13253 29146 14356 1319 -3508 28 C ATOM 1946 O ASP A1060 177.410 15.828 581.301 1.00151.50 O ANISOU 1946 O ASP A1060 13659 29488 14416 1122 -3386 214 O ATOM 1947 CB ASP A1060 179.360 17.387 583.458 1.00151.81 C ANISOU 1947 CB ASP A1060 12787 30079 14816 1616 -3466 -759 C ATOM 1948 CG ASP A1060 178.347 18.481 583.180 1.00158.46 C ANISOU 1948 CG ASP A1060 13518 31084 15605 1527 -3151 -928 C ATOM 1949 OD1 ASP A1060 177.151 18.160 583.020 1.00161.31 O ANISOU 1949 OD1 ASP A1060 14114 31564 15610 1279 -3104 -575 O ATOM 1950 OD2 ASP A1060 178.747 19.662 583.121 1.00160.99 O ANISOU 1950 OD2 ASP A1060 13520 31369 16279 1705 -2950 -1416 O ATOM 1951 N PHE A1061 179.602 15.331 581.061 1.00140.79 N ANISOU 1951 N PHE A1061 12344 27444 13705 1498 -3457 -50 N ATOM 1952 CA PHE A1061 179.448 14.863 579.687 1.00128.42 C ANISOU 1952 CA PHE A1061 11211 25271 12311 1469 -3298 144 C ATOM 1953 C PHE A1061 178.420 13.742 579.616 1.00124.53 C ANISOU 1953 C PHE A1061 11098 24832 11388 1182 -3559 692 C ATOM 1954 O PHE A1061 177.538 13.739 578.750 1.00127.05 O ANISOU 1954 O PHE A1061 11666 24977 11630 1046 -3431 851 O ATOM 1955 CB PHE A1061 180.802 14.393 579.146 1.00125.23 C ANISOU 1955 CB PHE A1061 10938 24282 12360 1721 -3281 29 C ATOM 1956 CG PHE A1061 180.781 13.991 577.695 1.00126.76 C ANISOU 1956 CG PHE A1061 11571 23847 12746 1768 -3087 160 C ATOM 1957 CD1 PHE A1061 180.359 12.726 577.313 1.00129.42 C ANISOU 1957 CD1 PHE A1061 12372 23947 12855 1634 -3350 590 C ATOM 1958 CD2 PHE A1061 181.206 14.872 576.714 1.00125.02 C ANISOU 1958 CD2 PHE A1061 11304 23262 12937 1963 -2652 -146 C ATOM 1959 CE1 PHE A1061 180.343 12.356 575.982 1.00125.49 C ANISOU 1959 CE1 PHE A1061 12291 22881 12507 1716 -3201 672 C ATOM 1960 CE2 PHE A1061 181.197 14.504 575.382 1.00117.83 C ANISOU 1960 CE2 PHE A1061 10815 21804 12150 2045 -2467 -29 C ATOM 1961 CZ PHE A1061 180.766 13.244 575.016 1.00116.95 C ANISOU 1961 CZ PHE A1061 11174 21479 11782 1935 -2752 361 C ATOM 1962 N ARG A1062 178.520 12.778 580.533 1.00123.31 N ANISOU 1962 N ARG A1062 10985 24906 10962 1087 -3945 994 N ATOM 1963 CA ARG A1062 177.541 11.703 580.601 1.00124.43 C ANISOU 1963 CA ARG A1062 11437 25121 10720 785 -4219 1549 C ATOM 1964 C ARG A1062 176.195 12.187 581.121 1.00124.80 C ANISOU 1964 C ARG A1062 11306 25745 10368 524 -4153 1684 C ATOM 1965 O ARG A1062 175.179 11.526 580.881 1.00127.91 O ANISOU 1965 O ARG A1062 11995 26002 10605 243 -4207 2078 O ATOM 1966 CB ARG A1062 178.075 10.574 581.484 1.00133.08 C ANISOU 1966 CB ARG A1062 12614 26289 11662 765 -4638 1851 C ATOM 1967 CG ARG A1062 177.428 9.220 581.246 1.00135.43 C ANISOU 1967 CG ARG A1062 13335 26362 11760 503 -4949 2435 C ATOM 1968 CD ARG A1062 178.474 8.143 580.972 1.00138.69 C ANISOU 1968 CD ARG A1062 14053 26213 12430 662 -5213 2537 C ATOM 1969 NE ARG A1062 179.473 8.047 582.035 1.00140.91 N ANISOU 1969 NE ARG A1062 14101 26726 12712 843 -5406 2420 N ATOM 1970 CZ ARG A1062 180.702 8.548 581.957 1.00136.98 C ANISOU 1970 CZ ARG A1062 13420 26033 12594 1176 -5279 1959 C ATOM 1971 NH1 ARG A1062 181.094 9.186 580.862 1.00141.02 N ANISOU 1971 NH1 ARG A1062 13954 26119 13510 1358 -4923 1601 N ATOM 1972 NH2 ARG A1062 181.542 8.413 582.974 1.00135.21 N ANISOU 1972 NH2 ARG A1062 12982 26040 12351 1333 -5510 1865 N ATOM 1973 N HIS A1063 176.161 13.323 581.817 1.00132.82 N ANISOU 1973 N HIS A1063 11943 27143 11380 607 -3922 1310 N ATOM 1974 CA HIS A1063 174.924 13.862 582.362 1.00134.22 C ANISOU 1974 CA HIS A1063 12027 27648 11324 395 -3706 1352 C ATOM 1975 C HIS A1063 174.300 14.927 581.468 1.00130.31 C ANISOU 1975 C HIS A1063 11410 27193 10910 415 -3423 1102 C ATOM 1976 O HIS A1063 173.380 15.627 581.903 1.00133.17 O ANISOU 1976 O HIS A1063 11612 27861 11126 309 -3212 1023 O ATOM 1977 CB HIS A1063 175.156 14.427 583.766 1.00137.57 C ANISOU 1977 CB HIS A1063 12146 28486 11637 487 -3644 1114 C ATOM 1978 CG HIS A1063 173.908 14.514 584.588 1.00128.36 C ANISOU 1978 CG HIS A1063 10938 27691 10144 259 -3507 1317 C ATOM 1979 ND1 HIS A1063 173.274 13.401 585.097 1.00131.00 N ANISOU 1979 ND1 HIS A1063 11489 28045 10238 4 -3655 1834 N ATOM 1980 CD2 HIS A1063 173.166 15.579 584.975 1.00128.07 C ANISOU 1980 CD2 HIS A1063 10640 28029 9993 260 -3232 1075 C ATOM 1981 CE1 HIS A1063 172.201 13.776 585.768 1.00132.32 C ANISOU 1981 CE1 HIS A1063 11498 28626 10154 -140 -3462 1909 C ATOM 1982 NE2 HIS A1063 172.111 15.092 585.709 1.00130.54 N ANISOU 1982 NE2 HIS A1063 10991 28623 9987 19 -3207 1448 N ATOM 1983 N GLY A1064 174.781 15.074 580.238 1.00126.14 N ANISOU 1983 N GLY A1064 10971 26326 10630 570 -3384 970 N ATOM 1984 CA GLY A1064 174.076 15.892 579.271 1.00130.93 C ANISOU 1984 CA GLY A1064 11621 26772 11353 558 -3081 816 C ATOM 1985 C GLY A1064 173.039 15.081 578.520 1.00150.88 C ANISOU 1985 C GLY A1064 14540 29090 13699 308 -3189 1251 C ATOM 1986 O GLY A1064 171.893 15.512 578.341 1.00151.38 O ANISOU 1986 O GLY A1064 14547 29395 13577 149 -3101 1308 O ATOM 1987 N PHE A1065 173.435 13.881 578.090 1.00164.01 N ANISOU 1987 N PHE A1065 16593 30291 15431 280 -3411 1549 N ATOM 1988 CA PHE A1065 172.537 13.034 577.315 1.00169.80 C ANISOU 1988 CA PHE A1065 17725 30739 16053 61 -3567 1940 C ATOM 1989 C PHE A1065 171.445 12.398 578.165 1.00171.95 C ANISOU 1989 C PHE A1065 17977 31335 16021 -294 -3755 2350 C ATOM 1990 O PHE A1065 170.401 12.028 577.621 1.00174.04 O ANISOU 1990 O PHE A1065 18462 31424 16240 -511 -3797 2594 O ATOM 1991 CB PHE A1065 173.329 11.945 576.592 1.00179.03 C ANISOU 1991 CB PHE A1065 19339 31237 17446 170 -3743 2087 C ATOM 1992 CG PHE A1065 174.142 12.452 575.437 1.00182.08 C ANISOU 1992 CG PHE A1065 19899 31065 18218 493 -3437 1731 C ATOM 1993 CD1 PHE A1065 173.534 12.780 574.236 1.00182.88 C ANISOU 1993 CD1 PHE A1065 20257 30849 18381 523 -3252 1682 C ATOM 1994 CD2 PHE A1065 175.514 12.597 575.548 1.00181.77 C ANISOU 1994 CD2 PHE A1065 19760 30824 18479 777 -3333 1458 C ATOM 1995 CE1 PHE A1065 174.279 13.246 573.169 1.00180.11 C ANISOU 1995 CE1 PHE A1065 20076 30007 18351 835 -2941 1392 C ATOM 1996 CE2 PHE A1065 176.263 13.057 574.485 1.00180.70 C ANISOU 1996 CE2 PHE A1065 19761 30191 18705 1071 -3014 1167 C ATOM 1997 CZ PHE A1065 175.646 13.385 573.295 1.00179.34 C ANISOU 1997 CZ PHE A1065 19860 29723 18557 1103 -2804 1146 C ATOM 1998 N ASP A1066 171.653 12.252 579.476 1.00167.35 N ANISOU 1998 N ASP A1066 17197 31039 15350 -345 -3779 2391 N ATOM 1999 CA ASP A1066 170.598 11.674 580.303 1.00155.50 C ANISOU 1999 CA ASP A1066 15709 29707 13666 -661 -3816 2755 C ATOM 2000 C ASP A1066 169.505 12.695 580.601 1.00139.51 C ANISOU 2000 C ASP A1066 13389 28099 11518 -757 -3509 2607 C ATOM 2001 O ASP A1066 168.314 12.374 580.514 1.00131.78 O ANISOU 2001 O ASP A1066 12469 27146 10457 -1023 -3501 2888 O ATOM 2002 CB ASP A1066 171.184 11.098 581.597 1.00157.02 C ANISOU 2002 CB ASP A1066 15824 30085 13754 -659 -3957 2891 C ATOM 2003 CG ASP A1066 171.908 12.135 582.439 1.00158.19 C ANISOU 2003 CG ASP A1066 15596 30635 13874 -409 -3781 2458 C ATOM 2004 OD1 ASP A1066 171.805 13.342 582.141 1.00157.09 O ANISOU 2004 OD1 ASP A1066 15217 30676 13793 -274 -3524 2066 O ATOM 2005 OD2 ASP A1066 172.586 11.737 583.408 1.00163.14 O ANISOU 2005 OD2 ASP A1066 16173 31381 14431 -336 -3920 2500 O ATOM 2006 N ILE A1067 169.889 13.927 580.949 1.00133.11 N ANISOU 2006 N ILE A1067 12244 27615 10719 -536 -3270 2157 N ATOM 2007 CA ILE A1067 168.907 14.993 581.090 1.00130.90 C ANISOU 2007 CA ILE A1067 11695 27690 10351 -576 -2983 1960 C ATOM 2008 C ILE A1067 168.295 15.342 579.742 1.00121.46 C ANISOU 2008 C ILE A1067 10647 26234 9267 -600 -2915 1911 C ATOM 2009 O ILE A1067 167.178 15.869 579.686 1.00121.90 O ANISOU 2009 O ILE A1067 10581 26489 9245 -720 -2750 1900 O ATOM 2010 CB ILE A1067 169.539 16.233 581.758 1.00135.58 C ANISOU 2010 CB ILE A1067 11915 28633 10966 -305 -2779 1454 C ATOM 2011 CG1 ILE A1067 168.459 17.235 582.175 1.00142.21 C ANISOU 2011 CG1 ILE A1067 12473 29894 11666 -350 -2505 1285 C ATOM 2012 CG2 ILE A1067 170.543 16.898 580.832 1.00126.89 C ANISOU 2012 CG2 ILE A1067 10787 27288 10138 -25 -2746 1065 C ATOM 2013 CD1 ILE A1067 169.008 18.515 582.768 1.00140.50 C ANISOU 2013 CD1 ILE A1067 11915 29971 11496 -72 -2320 749 C ATOM 2014 N LEU A1068 168.995 15.047 578.644 1.00123.32 N ANISOU 2014 N LEU A1068 11147 26045 9664 -468 -3047 1886 N ATOM 2015 CA LEU A1068 168.393 15.202 577.325 1.00126.53 C ANISOU 2015 CA LEU A1068 11772 26175 10128 -485 -3027 1898 C ATOM 2016 C LEU A1068 167.317 14.145 577.089 1.00129.44 C ANISOU 2016 C LEU A1068 12426 26320 10433 -803 -3218 2353 C ATOM 2017 O LEU A1068 166.173 14.473 576.753 1.00119.70 O ANISOU 2017 O LEU A1068 11167 25151 9165 -944 -3129 2389 O ATOM 2018 CB LEU A1068 169.477 15.129 576.248 1.00125.22 C ANISOU 2018 CB LEU A1068 11831 25619 10127 -216 -3090 1757 C ATOM 2019 CG LEU A1068 169.152 15.709 574.870 1.00121.15 C ANISOU 2019 CG LEU A1068 11564 24652 9814 -88 -2861 1572 C ATOM 2020 CD1 LEU A1068 168.932 17.212 574.951 1.00109.02 C ANISOU 2020 CD1 LEU A1068 9670 23412 8340 46 -2527 1162 C ATOM 2021 CD2 LEU A1068 170.251 15.375 573.872 1.00109.66 C ANISOU 2021 CD2 LEU A1068 10493 22489 8684 178 -2780 1465 C ATOM 2022 N VAL A1069 167.662 12.870 577.293 1.00147.41 N ANISOU 2022 N VAL A1069 14953 28336 12719 -918 -3501 2696 N ATOM 2023 CA VAL A1069 166.755 11.774 576.960 1.00159.01 C ANISOU 2023 CA VAL A1069 16710 29515 14192 -1206 -3739 3121 C ATOM 2024 C VAL A1069 165.546 11.760 577.890 1.00176.47 C ANISOU 2024 C VAL A1069 18655 32127 16267 -1502 -3645 3338 C ATOM 2025 O VAL A1069 164.421 11.467 577.461 1.00164.87 O ANISOU 2025 O VAL A1069 17262 30571 14810 -1727 -3711 3549 O ATOM 2026 CB VAL A1069 167.516 10.434 576.986 1.00154.16 C ANISOU 2026 CB VAL A1069 16415 28512 13645 -1228 -4081 3413 C ATOM 2027 CG1 VAL A1069 166.552 9.260 576.982 1.00156.58 C ANISOU 2027 CG1 VAL A1069 16930 28595 13968 -1565 -4339 3876 C ATOM 2028 CG2 VAL A1069 168.457 10.340 575.795 1.00141.06 C ANISOU 2028 CG2 VAL A1069 15070 26419 12107 -953 -4197 3258 C ATOM 2029 N GLY A1070 165.753 12.084 579.171 1.00199.53 N ANISOU 2029 N GLY A1070 21247 35519 19047 -1490 -3495 3288 N ATOM 2030 CA GLY A1070 164.651 12.062 580.124 1.00216.03 C ANISOU 2030 CA GLY A1070 23056 38070 20956 -1746 -3384 3518 C ATOM 2031 C GLY A1070 163.473 12.911 579.690 1.00227.48 C ANISOU 2031 C GLY A1070 24326 39719 22386 -1817 -3179 3389 C ATOM 2032 O GLY A1070 162.316 12.552 579.921 1.00230.98 O ANISOU 2032 O GLY A1070 24664 40347 22751 -2100 -3192 3695 O ATOM 2033 N GLN A1071 163.750 14.047 579.054 1.00235.16 N ANISOU 2033 N GLN A1071 25243 40670 23436 -1563 -2995 2943 N ATOM 2034 CA GLN A1071 162.709 14.862 578.444 1.00234.61 C ANISOU 2034 CA GLN A1071 25065 40697 23380 -1590 -2836 2792 C ATOM 2035 C GLN A1071 162.407 14.441 577.011 1.00231.57 C ANISOU 2035 C GLN A1071 25062 39771 23151 -1626 -3035 2880 C ATOM 2036 O GLN A1071 161.291 14.674 576.529 1.00231.70 O ANISOU 2036 O GLN A1071 25049 39811 23176 -1750 -3014 2919 O ATOM 2037 CB GLN A1071 163.116 16.340 578.492 1.00238.13 C ANISOU 2037 CB GLN A1071 25250 41395 23832 -1290 -2546 2267 C ATOM 2038 CG GLN A1071 162.174 17.293 577.777 1.00240.80 C ANISOU 2038 CG GLN A1071 25496 41793 24205 -1258 -2387 2055 C ATOM 2039 CD GLN A1071 162.690 17.691 576.410 1.00238.42 C ANISOU 2039 CD GLN A1071 25458 41063 24068 -1041 -2422 1822 C ATOM 2040 OE1 GLN A1071 163.889 17.901 576.227 1.00238.77 O ANISOU 2040 OE1 GLN A1071 25557 40975 24190 -808 -2414 1613 O ATOM 2041 NE2 GLN A1071 161.788 17.794 575.441 1.00235.69 N ANISOU 2041 NE2 GLN A1071 25263 40524 23764 -1104 -2467 1862 N ATOM 2042 N ILE A1072 163.369 13.811 576.332 1.00208.20 N ANISOU 2042 N ILE A1072 22464 36340 20304 -1504 -3244 2911 N ATOM 2043 CA ILE A1072 163.136 13.324 574.973 1.00175.13 C ANISOU 2043 CA ILE A1072 18687 31625 16229 -1504 -3463 2999 C ATOM 2044 C ILE A1072 161.967 12.349 574.948 1.00160.15 C ANISOU 2044 C ILE A1072 16888 29609 14350 -1853 -3696 3410 C ATOM 2045 O ILE A1072 161.056 12.467 574.120 1.00153.82 O ANISOU 2045 O ILE A1072 16192 28655 13599 -1921 -3759 3415 O ATOM 2046 CB ILE A1072 164.414 12.681 574.409 1.00164.22 C ANISOU 2046 CB ILE A1072 17663 29805 14927 -1308 -3659 3002 C ATOM 2047 CG1 ILE A1072 165.352 13.755 573.858 1.00158.40 C ANISOU 2047 CG1 ILE A1072 16878 29107 14201 -941 -3442 2579 C ATOM 2048 CG2 ILE A1072 164.064 11.649 573.354 1.00158.31 C ANISOU 2048 CG2 ILE A1072 17381 28501 14266 -1397 -3996 3252 C ATOM 2049 CD1 ILE A1072 166.787 13.306 573.744 1.00157.31 C ANISOU 2049 CD1 ILE A1072 16903 28758 14108 -719 -3554 2547 C ATOM 2050 N ASP A1073 161.976 11.365 575.852 1.00154.23 N ANISOU 2050 N ASP A1073 16097 28937 13569 -2079 -3843 3770 N ATOM 2051 CA ASP A1073 160.865 10.420 575.905 1.00157.74 C ANISOU 2051 CA ASP A1073 16573 29314 14047 -2442 -4068 4201 C ATOM 2052 C ASP A1073 159.562 11.114 576.277 1.00159.36 C ANISOU 2052 C ASP A1073 16386 30009 14153 -2621 -3855 4210 C ATOM 2053 O ASP A1073 158.480 10.640 575.912 1.00159.43 O ANISOU 2053 O ASP A1073 16415 29931 14229 -2879 -4025 4465 O ATOM 2054 CB ASP A1073 161.173 9.290 576.886 1.00161.31 C ANISOU 2054 CB ASP A1073 17017 29808 14466 -2647 -4241 4607 C ATOM 2055 CG ASP A1073 162.245 8.351 576.371 1.00156.99 C ANISOU 2055 CG ASP A1073 16909 28684 14057 -2519 -4545 4673 C ATOM 2056 OD1 ASP A1073 163.439 8.698 576.475 1.00150.30 O ANISOU 2056 OD1 ASP A1073 16107 27814 13186 -2230 -4457 4414 O ATOM 2057 OD2 ASP A1073 161.894 7.269 575.855 1.00159.26 O ANISOU 2057 OD2 ASP A1073 17483 28541 14487 -2702 -4888 4977 O ATOM 2058 N ASP A1074 159.642 12.235 576.997 1.00156.34 N ANISOU 2058 N ASP A1074 15635 30144 13623 -2478 -3502 3926 N ATOM 2059 CA ASP A1074 158.455 13.041 577.250 1.00160.70 C ANISOU 2059 CA ASP A1074 15821 31159 14077 -2579 -3281 3860 C ATOM 2060 C ASP A1074 157.980 13.765 575.997 1.00157.65 C ANISOU 2060 C ASP A1074 15574 30517 13810 -2439 -3270 3571 C ATOM 2061 O ASP A1074 156.796 14.104 575.904 1.00154.04 O ANISOU 2061 O ASP A1074 14915 30282 13329 -2581 -3215 3608 O ATOM 2062 CB ASP A1074 158.727 14.050 578.368 1.00160.36 C ANISOU 2062 CB ASP A1074 15369 31719 13842 -2422 -2927 3597 C ATOM 2063 CG ASP A1074 159.210 13.390 579.645 1.00157.08 C ANISOU 2063 CG ASP A1074 14818 31594 13271 -2521 -2938 3863 C ATOM 2064 OD1 ASP A1074 158.901 12.198 579.853 1.00158.13 O ANISOU 2064 OD1 ASP A1074 15049 31624 13410 -2810 -3170 4340 O ATOM 2065 OD2 ASP A1074 159.896 14.064 580.442 1.00153.74 O ANISOU 2065 OD2 ASP A1074 14192 31496 12725 -2306 -2731 3595 O ATOM 2066 N ALA A1075 158.876 14.009 575.036 1.00156.00 N ANISOU 2066 N ALA A1075 15695 29869 13708 -2157 -3322 3299 N ATOM 2067 CA ALA A1075 158.465 14.608 573.771 1.00150.03 C ANISOU 2067 CA ALA A1075 15127 28839 13038 -2008 -3342 3062 C ATOM 2068 C ALA A1075 157.876 13.566 572.826 1.00147.70 C ANISOU 2068 C ALA A1075 15204 28050 12864 -2177 -3723 3338 C ATOM 2069 O ALA A1075 156.838 13.809 572.198 1.00146.52 O ANISOU 2069 O ALA A1075 15057 27857 12758 -2243 -3788 3316 O ATOM 2070 CB ALA A1075 159.650 15.317 573.114 1.00145.48 C ANISOU 2070 CB ALA A1075 14735 28054 12488 -1630 -3227 2689 C ATOM 2071 N LEU A1076 158.525 12.404 572.712 1.00146.62 N ANISOU 2071 N LEU A1076 15386 27526 12797 -2233 -4000 3581 N ATOM 2072 CA LEU A1076 157.965 11.322 571.908 1.00136.75 C ANISOU 2072 CA LEU A1076 14482 25794 11684 -2403 -4405 3849 C ATOM 2073 C LEU A1076 156.658 10.815 572.502 1.00136.76 C ANISOU 2073 C LEU A1076 14194 26056 11711 -2814 -4509 4212 C ATOM 2074 O LEU A1076 155.803 10.298 571.773 1.00129.35 O ANISOU 2074 O LEU A1076 13416 24827 10903 -2968 -4801 4357 O ATOM 2075 CB LEU A1076 158.980 10.185 571.777 1.00133.42 C ANISOU 2075 CB LEU A1076 14435 24922 11336 -2365 -4679 4027 C ATOM 2076 CG LEU A1076 158.666 9.047 570.802 1.00135.06 C ANISOU 2076 CG LEU A1076 15090 24518 11709 -2453 -5139 4232 C ATOM 2077 CD1 LEU A1076 159.930 8.600 570.087 1.00134.55 C ANISOU 2077 CD1 LEU A1076 15495 23955 11672 -2151 -5297 4118 C ATOM 2078 CD2 LEU A1076 158.022 7.869 571.520 1.00129.31 C ANISOU 2078 CD2 LEU A1076 14244 23802 11086 -2875 -5398 4716 C ATOM 2079 N LYS A1077 156.487 10.949 573.820 1.00151.42 N ANISOU 2079 N LYS A1077 15618 28479 13437 -2991 -4283 4371 N ATOM 2080 CA LYS A1077 155.199 10.648 574.435 1.00157.07 C ANISOU 2080 CA LYS A1077 15979 29573 14127 -3374 -4308 4723 C ATOM 2081 C LYS A1077 154.108 11.558 573.885 1.00160.48 C ANISOU 2081 C LYS A1077 16236 30173 14567 -3349 -4202 4506 C ATOM 2082 O LYS A1077 152.972 11.120 573.670 1.00162.58 O ANISOU 2082 O LYS A1077 16409 30438 14925 -3630 -4401 4762 O ATOM 2083 CB LYS A1077 155.302 10.783 575.954 1.00153.79 C ANISOU 2083 CB LYS A1077 15130 29807 13497 -3494 -4031 4888 C ATOM 2084 CG LYS A1077 153.981 10.639 576.691 1.00158.63 C ANISOU 2084 CG LYS A1077 15300 30959 14013 -3867 -3975 5254 C ATOM 2085 CD LYS A1077 154.167 10.813 578.190 1.00162.90 C ANISOU 2085 CD LYS A1077 15436 32177 14282 -3927 -3685 5396 C ATOM 2086 CE LYS A1077 152.836 10.782 578.922 1.00168.03 C ANISOU 2086 CE LYS A1077 15602 33459 14782 -4271 -3581 5757 C ATOM 2087 NZ LYS A1077 151.942 11.893 578.494 1.00168.37 N ANISOU 2087 NZ LYS A1077 15429 33743 14799 -4164 -3385 5429 N ATOM 2088 N LEU A1078 154.438 12.829 573.646 1.00158.04 N ANISOU 2088 N LEU A1078 15869 29998 14181 -3016 -3908 4039 N ATOM 2089 CA LEU A1078 153.496 13.753 573.031 1.00160.05 C ANISOU 2089 CA LEU A1078 16004 30353 14454 -2937 -3821 3790 C ATOM 2090 C LEU A1078 153.410 13.577 571.521 1.00163.25 C ANISOU 2090 C LEU A1078 16877 30130 15022 -2794 -4122 3657 C ATOM 2091 O LEU A1078 152.454 14.062 570.907 1.00188.60 O ANISOU 2091 O LEU A1078 20037 33340 18280 -2784 -4166 3535 O ATOM 2092 CB LEU A1078 153.882 15.198 573.356 1.00152.93 C ANISOU 2092 CB LEU A1078 14863 29821 13424 -2632 -3408 3347 C ATOM 2093 CG LEU A1078 154.047 15.557 574.834 1.00157.12 C ANISOU 2093 CG LEU A1078 14947 30993 13760 -2683 -3091 3375 C ATOM 2094 CD1 LEU A1078 154.372 17.035 574.993 1.00138.96 C ANISOU 2094 CD1 LEU A1078 12440 28977 11382 -2355 -2738 2883 C ATOM 2095 CD2 LEU A1078 152.804 15.189 575.628 1.00128.47 C ANISOU 2095 CD2 LEU A1078 10934 27851 10030 -3038 -3078 3737 C ATOM 2096 N ALA A1079 154.385 12.900 570.911 1.00169.64 N ANISOU 2096 N ALA A1079 18143 30416 15897 -2658 -4337 3670 N ATOM 2097 CA ALA A1079 154.346 12.673 569.471 1.00174.70 C ANISOU 2097 CA ALA A1079 19268 30467 16642 -2487 -4636 3549 C ATOM 2098 C ALA A1079 153.352 11.585 569.087 1.00184.81 C ANISOU 2098 C ALA A1079 20664 31460 18093 -2791 -5070 3872 C ATOM 2099 O ALA A1079 152.827 11.599 567.968 1.00186.61 O ANISOU 2099 O ALA A1079 21168 31331 18404 -2689 -5314 3746 O ATOM 2100 CB ALA A1079 155.740 12.313 568.957 1.00175.67 C ANISOU 2100 CB ALA A1079 19839 30159 16749 -2215 -4710 3454 C ATOM 2101 N ASN A1080 153.081 10.643 569.988 1.00160.57 N ANISOU 2101 N ASN A1080 20508 23977 16524 -836 4582 2986 N ATOM 2102 CA ASN A1080 152.172 9.539 569.716 1.00167.54 C ANISOU 2102 CA ASN A1080 21245 24792 17620 -975 4674 3144 C ATOM 2103 C ASN A1080 150.813 9.710 570.384 1.00183.35 C ANISOU 2103 C ASN A1080 23139 26935 19590 -1061 5011 3055 C ATOM 2104 O ASN A1080 149.961 8.825 570.260 1.00187.82 O ANISOU 2104 O ASN A1080 23581 27467 20315 -1200 5118 3171 O ATOM 2105 CB ASN A1080 152.806 8.215 570.162 1.00160.84 C ANISOU 2105 CB ASN A1080 20611 23842 16659 -1106 4541 3413 C ATOM 2106 CG ASN A1080 152.183 7.009 569.484 1.00156.32 C ANISOU 2106 CG ASN A1080 19894 23128 16374 -1229 4536 3584 C ATOM 2107 OD1 ASN A1080 151.679 7.103 568.364 1.00155.32 O ANISOU 2107 OD1 ASN A1080 19511 22935 16567 -1190 4513 3526 O ATOM 2108 ND2 ASN A1080 152.211 5.867 570.162 1.00153.95 N ANISOU 2108 ND2 ASN A1080 19767 22771 15956 -1383 4555 3794 N ATOM 2109 N GLU A1081 150.586 10.823 571.082 1.00191.96 N ANISOU 2109 N GLU A1081 24275 28181 20482 -989 5184 2844 N ATOM 2110 CA GLU A1081 149.316 11.049 571.758 1.00204.20 C ANISOU 2110 CA GLU A1081 25720 29874 21992 -1060 5517 2740 C ATOM 2111 C GLU A1081 148.252 11.648 570.849 1.00211.74 C ANISOU 2111 C GLU A1081 26320 30855 23278 -965 5630 2573 C ATOM 2112 O GLU A1081 147.059 11.518 571.148 1.00215.29 O ANISOU 2112 O GLU A1081 26604 31400 23796 -1049 5883 2534 O ATOM 2113 CB GLU A1081 149.512 11.965 572.971 1.00207.01 C ANISOU 2113 CB GLU A1081 26296 30380 21977 -1026 5669 2576 C ATOM 2114 CG GLU A1081 149.822 13.409 572.615 1.00207.62 C ANISOU 2114 CG GLU A1081 26337 30493 22057 -822 5631 2309 C ATOM 2115 CD GLU A1081 149.932 14.302 573.834 1.00212.64 C ANISOU 2115 CD GLU A1081 27197 31269 22327 -807 5799 2128 C ATOM 2116 OE1 GLU A1081 149.813 13.784 574.964 1.00216.34 O ANISOU 2116 OE1 GLU A1081 27859 31811 22529 -954 5938 2221 O ATOM 2117 OE2 GLU A1081 150.138 15.522 573.663 1.00212.45 O ANISOU 2117 OE2 GLU A1081 27171 31272 22279 -651 5795 1890 O ATOM 2118 N GLY A1082 148.650 12.300 569.754 1.00214.23 N ANISOU 2118 N GLY A1082 26511 31087 23798 -793 5449 2474 N ATOM 2119 CA GLY A1082 147.728 12.923 568.818 1.00212.87 C ANISOU 2119 CA GLY A1082 26014 30923 23945 -674 5519 2318 C ATOM 2120 C GLY A1082 147.993 14.400 568.597 1.00211.47 C ANISOU 2120 C GLY A1082 25832 30775 23742 -450 5511 2062 C ATOM 2121 O GLY A1082 147.697 14.922 567.517 1.00209.58 O ANISOU 2121 O GLY A1082 25373 30473 23785 -307 5445 1964 O ATOM 2122 N LYS A1083 148.541 15.083 569.599 1.00194.50 N ANISOU 2122 N LYS A1083 23935 28711 21256 -420 5574 1949 N ATOM 2123 CA LYS A1083 148.852 16.508 569.509 1.00168.43 C ANISOU 2123 CA LYS A1083 20678 25427 17892 -221 5574 1692 C ATOM 2124 C LYS A1083 150.355 16.657 569.298 1.00155.61 C ANISOU 2124 C LYS A1083 19292 23707 16126 -176 5295 1733 C ATOM 2125 O LYS A1083 151.144 16.501 570.234 1.00161.00 O ANISOU 2125 O LYS A1083 20254 24434 16484 -260 5253 1783 O ATOM 2126 CB LYS A1083 148.384 17.249 570.757 1.00159.69 C ANISOU 2126 CB LYS A1083 19684 24482 16508 -224 5845 1502 C ATOM 2127 CG LYS A1083 146.873 17.362 570.881 1.00155.86 C ANISOU 2127 CG LYS A1083 18928 24106 16185 -226 6131 1406 C ATOM 2128 CD LYS A1083 146.481 18.324 571.991 1.00150.89 C ANISOU 2128 CD LYS A1083 18404 23629 15298 -187 6389 1168 C ATOM 2129 CE LYS A1083 144.979 18.555 572.016 1.00148.52 C ANISOU 2129 CE LYS A1083 17799 23444 15188 -155 6666 1046 C ATOM 2130 NZ LYS A1083 144.590 19.570 573.034 1.00150.35 N ANISOU 2130 NZ LYS A1083 18118 23823 15185 -95 6917 789 N ATOM 2131 N VAL A1084 150.748 16.966 568.059 1.00137.90 N ANISOU 2131 N VAL A1084 16934 21335 14127 -45 5101 1710 N ATOM 2132 CA VAL A1084 152.160 17.121 567.719 1.00136.59 C ANISOU 2132 CA VAL A1084 16957 21078 13862 1 4832 1742 C ATOM 2133 C VAL A1084 152.668 18.537 567.955 1.00140.91 C ANISOU 2133 C VAL A1084 17655 21651 14235 144 4840 1480 C ATOM 2134 O VAL A1084 153.890 18.754 567.965 1.00140.03 O ANISOU 2134 O VAL A1084 17745 21501 13959 156 4640 1480 O ATOM 2135 CB VAL A1084 152.402 16.714 566.250 1.00134.60 C ANISOU 2135 CB VAL A1084 16526 20667 13947 54 4618 1851 C ATOM 2136 CG1 VAL A1084 153.861 16.341 566.022 1.00129.92 C ANISOU 2136 CG1 VAL A1084 16124 19992 13249 29 4335 1978 C ATOM 2137 CG2 VAL A1084 151.484 15.565 565.861 1.00137.63 C ANISOU 2137 CG2 VAL A1084 16692 21022 14581 -65 4669 2033 C ATOM 2138 N LYS A1085 151.772 19.507 568.159 1.00144.86 N ANISOU 2138 N LYS A1085 18065 22210 14764 251 5061 1251 N ATOM 2139 CA LYS A1085 152.202 20.890 568.341 1.00145.77 C ANISOU 2139 CA LYS A1085 18333 22321 14733 392 5074 983 C ATOM 2140 C LYS A1085 153.024 21.056 569.614 1.00146.19 C ANISOU 2140 C LYS A1085 18716 22469 14359 286 5071 942 C ATOM 2141 O LYS A1085 153.972 21.850 569.646 1.00146.82 O ANISOU 2141 O LYS A1085 18992 22513 14281 342 4943 805 O ATOM 2142 CB LYS A1085 150.988 21.817 568.356 1.00153.50 C ANISOU 2142 CB LYS A1085 19141 23338 15843 531 5322 752 C ATOM 2143 CG LYS A1085 150.173 21.778 567.073 1.00153.32 C ANISOU 2143 CG LYS A1085 18791 23219 16243 653 5306 773 C ATOM 2144 CD LYS A1085 148.969 22.702 567.143 1.00154.42 C ANISOU 2144 CD LYS A1085 18758 23403 16511 805 5539 546 C ATOM 2145 CE LYS A1085 148.167 22.659 565.852 1.00149.26 C ANISOU 2145 CE LYS A1085 17775 22657 16278 927 5495 572 C ATOM 2146 NZ LYS A1085 146.975 23.551 565.909 1.00148.52 N ANISOU 2146 NZ LYS A1085 17496 22609 16325 1090 5705 357 N ATOM 2147 N GLU A1086 152.680 20.319 570.673 1.00146.08 N ANISOU 2147 N GLU A1086 18778 22575 14153 124 5206 1056 N ATOM 2148 CA GLU A1086 153.472 20.378 571.899 1.00136.65 C ANISOU 2148 CA GLU A1086 17910 21467 12544 11 5187 1042 C ATOM 2149 C GLU A1086 154.800 19.650 571.731 1.00125.25 C ANISOU 2149 C GLU A1086 16623 19960 11007 -62 4877 1250 C ATOM 2150 O GLU A1086 155.841 20.121 572.211 1.00117.53 O ANISOU 2150 O GLU A1086 15896 18997 9762 -75 4741 1175 O ATOM 2151 CB GLU A1086 152.682 19.788 573.068 1.00138.68 C ANISOU 2151 CB GLU A1086 18212 21858 12621 -139 5433 1111 C ATOM 2152 CG GLU A1086 151.440 20.574 573.469 1.00143.61 C ANISOU 2152 CG GLU A1086 18709 22585 13273 -79 5754 880 C ATOM 2153 CD GLU A1086 150.223 20.239 572.624 1.00143.80 C ANISOU 2153 CD GLU A1086 18364 22588 13687 -21 5872 924 C ATOM 2154 OE1 GLU A1086 150.394 19.724 571.499 1.00138.13 O ANISOU 2154 OE1 GLU A1086 17484 21747 13252 17 5686 1070 O ATOM 2155 OE2 GLU A1086 149.092 20.488 573.091 1.00145.68 O ANISOU 2155 OE2 GLU A1086 18470 22937 13945 -20 6148 809 O ATOM 2156 N ALA A1087 154.782 18.497 571.054 1.00123.54 N ANISOU 2156 N ALA A1087 16257 19670 11012 -113 4757 1506 N ATOM 2157 CA ALA A1087 156.016 17.761 570.805 1.00123.55 C ANISOU 2157 CA ALA A1087 16376 19603 10965 -166 4455 1706 C ATOM 2158 C ALA A1087 157.008 18.605 570.017 1.00123.93 C ANISOU 2158 C ALA A1087 16458 19577 11053 -44 4238 1575 C ATOM 2159 O ALA A1087 158.215 18.569 570.283 1.00123.91 O ANISOU 2159 O ALA A1087 16649 19580 10852 -79 4019 1615 O ATOM 2160 CB ALA A1087 155.712 16.457 570.069 1.00119.79 C ANISOU 2160 CB ALA A1087 15711 19035 10770 -227 4380 1972 C ATOM 2161 N GLN A1088 156.518 19.373 569.041 1.00125.06 N ANISOU 2161 N GLN A1088 16415 19648 11455 100 4291 1418 N ATOM 2162 CA GLN A1088 157.385 20.321 568.350 1.00125.73 C ANISOU 2162 CA GLN A1088 16556 19658 11558 216 4123 1259 C ATOM 2163 C GLN A1088 157.696 21.529 569.223 1.00127.11 C ANISOU 2163 C GLN A1088 16963 19903 11429 239 4197 992 C ATOM 2164 O GLN A1088 158.728 22.182 569.029 1.00120.31 O ANISOU 2164 O GLN A1088 16245 19006 10460 270 4019 882 O ATOM 2165 CB GLN A1088 156.743 20.765 567.036 1.00130.10 C ANISOU 2165 CB GLN A1088 16860 20091 12480 372 4158 1180 C ATOM 2166 CG GLN A1088 156.675 19.678 565.977 1.00132.56 C ANISOU 2166 CG GLN A1088 16964 20305 13099 348 4027 1422 C ATOM 2167 CD GLN A1088 156.079 20.174 564.674 1.00131.69 C ANISOU 2167 CD GLN A1088 16622 20074 13339 501 4048 1336 C ATOM 2168 OE1 GLN A1088 154.866 20.349 564.560 1.00137.04 O ANISOU 2168 OE1 GLN A1088 17116 20763 14191 556 4243 1271 O ATOM 2169 NE2 GLN A1088 156.933 20.409 563.684 1.00123.67 N ANISOU 2169 NE2 GLN A1088 15614 18946 12429 570 3842 1335 N ATOM 2170 N ALA A1089 156.822 21.843 570.183 1.00136.91 N ANISOU 2170 N ALA A1089 18247 21242 12530 212 4460 877 N ATOM 2171 CA ALA A1089 157.087 22.948 571.096 1.00136.93 C ANISOU 2171 CA ALA A1089 18489 21308 12230 213 4543 618 C ATOM 2172 C ALA A1089 158.209 22.629 572.074 1.00136.31 C ANISOU 2172 C ALA A1089 18703 21302 11784 69 4384 696 C ATOM 2173 O ALA A1089 158.797 23.553 572.646 1.00134.31 O ANISOU 2173 O ALA A1089 18681 21071 11280 60 4359 489 O ATOM 2174 CB ALA A1089 155.816 23.323 571.859 1.00136.48 C ANISOU 2174 CB ALA A1089 18382 21346 12127 219 4876 475 C ATOM 2175 N ALA A1090 158.519 21.350 572.278 1.00126.21 N ANISOU 2175 N ALA A1090 17428 20049 10476 -39 4267 988 N ATOM 2176 CA ALA A1090 159.644 20.962 573.121 1.00106.99 C ANISOU 2176 CA ALA A1090 15256 17670 7726 -147 4073 1094 C ATOM 2177 C ALA A1090 160.995 21.131 572.432 1.00109.57 C ANISOU 2177 C ALA A1090 15621 17937 8072 -117 3740 1103 C ATOM 2178 O ALA A1090 162.027 20.847 573.052 1.00118.69 O ANISOU 2178 O ALA A1090 16967 19142 8987 -190 3537 1185 O ATOM 2179 CB ALA A1090 159.480 19.511 573.580 1.00 93.58 C ANISOU 2179 CB ALA A1090 13548 16005 6003 -259 4062 1407 C ATOM 2180 N ALA A1091 161.016 21.590 571.178 1.00 86.44 N ANISOU 2180 N ALA A1091 12514 14907 5424 -8 3675 1020 N ATOM 2181 CA ALA A1091 162.272 21.689 570.440 1.00118.64 C ANISOU 2181 CA ALA A1091 16604 18932 9543 8 3366 1038 C ATOM 2182 C ALA A1091 163.160 22.796 570.997 1.00144.51 C ANISOU 2182 C ALA A1091 20126 22245 12537 -13 3271 797 C ATOM 2183 O ALA A1091 164.364 22.597 571.193 1.00115.89 O ANISOU 2183 O ALA A1091 16614 18657 8763 -81 3006 860 O ATOM 2184 CB ALA A1091 161.990 21.917 568.955 1.00104.85 C ANISOU 2184 CB ALA A1091 14621 17056 8162 135 3348 1009 C ATOM 2185 N GLU A1092 162.584 23.975 571.248 1.00170.34 N ANISOU 2185 N GLU A1092 23478 25499 15744 44 3479 514 N ATOM 2186 CA GLU A1092 163.369 25.073 571.806 1.00170.88 C ANISOU 2186 CA GLU A1092 23806 25575 15547 19 3405 268 C ATOM 2187 C GLU A1092 163.916 24.726 573.184 1.00172.28 C ANISOU 2187 C GLU A1092 24230 25870 15360 -83 3342 345 C ATOM 2188 O GLU A1092 165.018 25.158 573.541 1.00175.28 O ANISOU 2188 O GLU A1092 24781 26282 15536 -120 3125 265 O ATOM 2189 CB GLU A1092 162.526 26.347 571.873 1.00176.47 C ANISOU 2189 CB GLU A1092 24565 26219 16268 104 3669 -47 C ATOM 2190 CG GLU A1092 162.801 27.340 570.754 1.00180.81 C ANISOU 2190 CG GLU A1092 25055 26633 17011 203 3592 -253 C ATOM 2191 CD GLU A1092 164.228 27.855 570.771 1.00183.08 C ANISOU 2191 CD GLU A1092 25541 26899 17123 141 3313 -345 C ATOM 2192 OE1 GLU A1092 164.867 27.880 569.698 1.00180.53 O ANISOU 2192 OE1 GLU A1092 25103 26512 16979 154 3114 -327 O ATOM 2193 OE2 GLU A1092 164.712 28.228 571.860 1.00184.86 O ANISOU 2193 OE2 GLU A1092 26009 27191 17037 109 3277 -426 O ATOM 2194 N GLN A1093 163.165 23.952 573.970 1.00158.73 N ANISOU 2194 N GLN A1093 22524 24226 13561 -125 3519 500 N ATOM 2195 CA GLN A1093 163.681 23.488 575.253 1.00145.59 C ANISOU 2195 CA GLN A1093 21086 22675 11555 -201 3446 613 C ATOM 2196 C GLN A1093 164.807 22.481 575.057 1.00133.32 C ANISOU 2196 C GLN A1093 19493 21157 10007 -271 3104 866 C ATOM 2197 O GLN A1093 165.807 22.506 575.785 1.00140.63 O ANISOU 2197 O GLN A1093 20597 22164 10671 -318 2897 878 O ATOM 2198 CB GLN A1093 162.553 22.884 576.086 1.00148.13 C ANISOU 2198 CB GLN A1093 21430 23054 11800 -233 3736 722 C ATOM 2199 CG GLN A1093 162.998 22.387 577.448 1.00151.63 C ANISOU 2199 CG GLN A1093 22118 23616 11877 -293 3683 850 C ATOM 2200 CD GLN A1093 162.605 20.947 577.694 1.00152.95 C ANISOU 2200 CD GLN A1093 22212 23814 12088 -379 3714 1166 C ATOM 2201 OE1 GLN A1093 161.624 20.456 577.137 1.00150.09 O ANISOU 2201 OE1 GLN A1093 21639 23405 11985 -391 3890 1246 O ATOM 2202 NE2 GLN A1093 163.376 20.258 578.527 1.00155.54 N ANISOU 2202 NE2 GLN A1093 22708 24223 12167 -435 3532 1347 N ATOM 2203 N LEU A1094 164.662 21.585 574.075 1.00122.95 N ANISOU 2203 N LEU A1094 17938 19782 8997 -266 3035 1070 N ATOM 2204 CA LEU A1094 165.759 20.690 573.721 1.00117.05 C ANISOU 2204 CA LEU A1094 17135 19038 8302 -304 2708 1294 C ATOM 2205 C LEU A1094 167.001 21.467 573.302 1.00119.11 C ANISOU 2205 C LEU A1094 17434 19296 8525 -302 2439 1139 C ATOM 2206 O LEU A1094 168.126 20.991 573.494 1.00111.70 O ANISOU 2206 O LEU A1094 16536 18409 7494 -350 2155 1262 O ATOM 2207 CB LEU A1094 165.325 19.745 572.600 1.00110.41 C ANISOU 2207 CB LEU A1094 16025 18100 7826 -269 2702 1504 C ATOM 2208 CG LEU A1094 164.524 18.504 572.997 1.00107.82 C ANISOU 2208 CG LEU A1094 15650 17771 7545 -312 2837 1761 C ATOM 2209 CD1 LEU A1094 163.716 17.993 571.816 1.00105.33 C ANISOU 2209 CD1 LEU A1094 15060 17342 7619 -259 2927 1861 C ATOM 2210 CD2 LEU A1094 165.463 17.424 573.503 1.00 89.16 C ANISOU 2210 CD2 LEU A1094 13382 15439 5057 -371 2588 2015 C ATOM 2211 N LYS A1095 166.818 22.661 572.736 1.00125.24 N ANISOU 2211 N LYS A1095 18198 20010 9379 -250 2523 868 N ATOM 2212 CA LYS A1095 167.954 23.468 572.305 1.00132.25 C ANISOU 2212 CA LYS A1095 19126 20882 10240 -269 2283 698 C ATOM 2213 C LYS A1095 168.601 24.188 573.484 1.00147.98 C ANISOU 2213 C LYS A1095 21381 22968 11877 -329 2211 532 C ATOM 2214 O LYS A1095 169.830 24.175 573.630 1.00153.26 O ANISOU 2214 O LYS A1095 22095 23696 12439 -398 1919 544 O ATOM 2215 CB LYS A1095 167.507 24.470 571.238 1.00131.36 C ANISOU 2215 CB LYS A1095 18917 20647 10348 -190 2400 471 C ATOM 2216 CG LYS A1095 168.620 24.919 570.308 1.00134.70 C ANISOU 2216 CG LYS A1095 19283 21019 10876 -217 2135 384 C ATOM 2217 CD LYS A1095 169.257 23.727 569.613 1.00133.90 C ANISOU 2217 CD LYS A1095 18995 20928 10955 -230 1905 671 C ATOM 2218 CE LYS A1095 170.362 24.154 568.663 1.00127.38 C ANISOU 2218 CE LYS A1095 18100 20058 10240 -263 1654 587 C ATOM 2219 NZ LYS A1095 171.105 22.978 568.129 1.00122.61 N ANISOU 2219 NZ LYS A1095 17333 19470 9782 -269 1417 866 N ATOM 2220 N THR A1096 167.790 24.821 574.338 1.00161.14 N ANISOU 2220 N THR A1096 23209 24655 13363 -293 2470 375 N ATOM 2221 CA THR A1096 168.339 25.488 575.514 1.00166.17 C ANISOU 2221 CA THR A1096 24093 25392 13652 -329 2410 222 C ATOM 2222 C THR A1096 168.957 24.498 576.493 1.00169.71 C ANISOU 2222 C THR A1096 24631 25983 13870 -405 2239 455 C ATOM 2223 O THR A1096 169.789 24.897 577.315 1.00174.37 O ANISOU 2223 O THR A1096 25385 26674 14192 -458 2073 367 O ATOM 2224 CB THR A1096 167.262 26.325 576.213 1.00174.34 C ANISOU 2224 CB THR A1096 25264 26427 14552 -237 2742 18 C ATOM 2225 OG1 THR A1096 167.879 27.201 577.164 1.00179.70 O ANISOU 2225 OG1 THR A1096 26156 27198 14924 -260 2654 -185 O ATOM 2226 CG2 THR A1096 166.266 25.436 576.938 1.00178.64 C ANISOU 2226 CG2 THR A1096 25822 27030 15023 -221 2982 215 C ATOM 2227 N THR A1097 168.570 23.221 576.426 1.00154.17 N ANISOU 2227 N THR A1097 22556 24018 12004 -412 2271 749 N ATOM 2228 CA THR A1097 169.303 22.188 577.146 1.00136.28 C ANISOU 2228 CA THR A1097 20351 21858 9571 -473 2058 997 C ATOM 2229 C THR A1097 170.531 21.738 576.364 1.00135.81 C ANISOU 2229 C THR A1097 20146 21788 9669 -504 1703 1113 C ATOM 2230 O THR A1097 171.545 21.361 576.964 1.00131.02 O ANISOU 2230 O THR A1097 19613 21282 8888 -551 1447 1210 O ATOM 2231 CB THR A1097 168.391 20.992 577.433 1.00126.62 C ANISOU 2231 CB THR A1097 19090 20626 8394 -470 2238 1265 C ATOM 2232 OG1 THR A1097 167.184 21.449 578.057 1.00134.78 O ANISOU 2232 OG1 THR A1097 20227 21668 9316 -439 2594 1145 O ATOM 2233 CG2 THR A1097 169.080 19.997 578.357 1.00120.90 C ANISOU 2233 CG2 THR A1097 18481 20004 7450 -520 2044 1507 C ATOM 2234 N ARG A1098 170.459 21.787 575.031 1.00141.46 N ANISOU 2234 N ARG A1098 20650 22387 10712 -468 1686 1100 N ATOM 2235 CA ARG A1098 171.600 21.422 574.199 1.00145.21 C ANISOU 2235 CA ARG A1098 20971 22845 11355 -483 1370 1195 C ATOM 2236 C ARG A1098 172.778 22.364 574.412 1.00152.51 C ANISOU 2236 C ARG A1098 21986 23838 12123 -548 1138 983 C ATOM 2237 O ARG A1098 173.936 21.937 574.324 1.00153.50 O ANISOU 2237 O ARG A1098 22049 24021 12254 -584 839 1088 O ATOM 2238 CB ARG A1098 171.173 21.406 572.726 1.00143.35 C ANISOU 2238 CB ARG A1098 20506 22471 11488 -422 1434 1198 C ATOM 2239 CG ARG A1098 172.288 21.194 571.701 1.00144.47 C ANISOU 2239 CG ARG A1098 20480 22582 11830 -425 1141 1256 C ATOM 2240 CD ARG A1098 172.877 22.515 571.209 1.00148.77 C ANISOU 2240 CD ARG A1098 21047 23105 12375 -465 1062 957 C ATOM 2241 NE ARG A1098 172.005 23.645 571.517 1.00151.77 N ANISOU 2241 NE ARG A1098 21566 23446 12654 -454 1326 690 N ATOM 2242 CZ ARG A1098 172.371 24.920 571.428 1.00150.39 C ANISOU 2242 CZ ARG A1098 21491 23240 12412 -497 1304 395 C ATOM 2243 NH1 ARG A1098 173.600 25.235 571.042 1.00152.51 N ANISOU 2243 NH1 ARG A1098 21724 23522 12699 -574 1031 327 N ATOM 2244 NH2 ARG A1098 171.510 25.882 571.730 1.00147.14 N ANISOU 2244 NH2 ARG A1098 21209 22771 11925 -460 1559 164 N ATOM 2245 N ASN A1099 172.506 23.643 574.687 1.00162.70 N ANISOU 2245 N ASN A1099 23416 25117 13287 -563 1273 682 N ATOM 2246 CA ASN A1099 173.583 24.627 574.775 1.00169.27 C ANISOU 2246 CA ASN A1099 24322 25985 14006 -641 1063 455 C ATOM 2247 C ASN A1099 174.559 24.286 575.896 1.00178.01 C ANISOU 2247 C ASN A1099 25545 27259 14832 -712 825 536 C ATOM 2248 O ASN A1099 175.777 24.457 575.744 1.00179.08 O ANISOU 2248 O ASN A1099 25631 27448 14962 -784 536 500 O ATOM 2249 CB ASN A1099 172.997 26.026 574.972 1.00172.86 C ANISOU 2249 CB ASN A1099 24929 26377 14372 -631 1276 121 C ATOM 2250 CG ASN A1099 173.909 27.121 574.452 1.00171.69 C ANISOU 2250 CG ASN A1099 24789 26177 14268 -708 1101 -133 C ATOM 2251 OD1 ASN A1099 175.121 26.935 574.346 1.00170.18 O ANISOU 2251 OD1 ASN A1099 24537 26053 14071 -796 802 -86 O ATOM 2252 ND2 ASN A1099 173.329 28.270 574.122 1.00169.40 N ANISOU 2252 ND2 ASN A1099 24569 25759 14035 -675 1290 -405 N ATOM 2253 N ALA A1100 174.043 23.792 577.026 1.00209.09 N ANISOU 2253 N ALA A1100 29629 31281 18533 -693 943 651 N ATOM 2254 CA ALA A1100 174.910 23.446 578.147 1.00195.90 C ANISOU 2254 CA ALA A1100 28084 29775 16575 -749 725 736 C ATOM 2255 C ALA A1100 175.866 22.316 577.789 1.00202.20 C ANISOU 2255 C ALA A1100 28718 30610 17499 -751 428 1010 C ATOM 2256 O ALA A1100 177.004 22.292 578.270 1.00174.29 O ANISOU 2256 O ALA A1100 25206 27196 13820 -807 146 1020 O ATOM 2257 CB ALA A1100 174.069 23.067 579.366 1.00104.91 C ANISOU 2257 CB ALA A1100 16753 18325 4784 -719 936 825 C ATOM 2258 N TYR A1101 175.429 21.375 576.949 1.00204.32 N ANISOU 2258 N TYR A1101 28812 30777 18042 -684 483 1229 N ATOM 2259 CA TYR A1101 176.307 20.284 576.542 1.00200.86 C ANISOU 2259 CA TYR A1101 28211 30353 17755 -659 213 1486 C ATOM 2260 C TYR A1101 177.290 20.737 575.468 1.00194.94 C ANISOU 2260 C TYR A1101 27273 29573 17223 -683 -7 1379 C ATOM 2261 O TYR A1101 178.490 20.453 575.556 1.00197.89 O ANISOU 2261 O TYR A1101 27576 30035 17578 -706 -304 1447 O ATOM 2262 CB TYR A1101 175.480 19.097 576.047 1.00201.87 C ANISOU 2262 CB TYR A1101 28229 30368 18104 -578 354 1757 C ATOM 2263 CG TYR A1101 176.314 17.991 575.436 1.00206.66 C ANISOU 2263 CG TYR A1101 28652 30946 18924 -527 99 2009 C ATOM 2264 CD1 TYR A1101 176.562 17.957 574.070 1.00204.32 C ANISOU 2264 CD1 TYR A1101 28128 30543 18961 -488 32 2008 C ATOM 2265 CD2 TYR A1101 176.857 16.985 576.224 1.00213.07 C ANISOU 2265 CD2 TYR A1101 29524 31829 19604 -506 -72 2246 C ATOM 2266 CE1 TYR A1101 177.325 16.955 573.505 1.00206.46 C ANISOU 2266 CE1 TYR A1101 28232 30777 19436 -424 -188 2228 C ATOM 2267 CE2 TYR A1101 177.623 15.973 575.665 1.00214.65 C ANISOU 2267 CE2 TYR A1101 29559 31985 20014 -437 -297 2468 C ATOM 2268 CZ TYR A1101 177.852 15.966 574.303 1.00212.74 C ANISOU 2268 CZ TYR A1101 29087 31635 20111 -394 -350 2454 C ATOM 2269 OH TYR A1101 178.608 14.970 573.729 1.00215.70 O ANISOU 2269 OH TYR A1101 29298 31956 20704 -311 -560 2664 O ATOM 2270 N ILE A1102 176.797 21.440 574.444 1.00178.09 N ANISOU 2270 N ILE A1102 25051 27316 15298 -676 138 1212 N ATOM 2271 CA ILE A1102 177.666 21.894 573.365 1.00157.52 C ANISOU 2271 CA ILE A1102 22276 24672 12903 -706 -45 1106 C ATOM 2272 C ILE A1102 178.690 22.900 573.868 1.00162.57 C ANISOU 2272 C ILE A1102 23005 25414 13350 -822 -233 872 C ATOM 2273 O ILE A1102 179.706 23.133 573.204 1.00159.12 O ANISOU 2273 O ILE A1102 22426 24988 13045 -871 -451 817 O ATOM 2274 CB ILE A1102 176.830 22.483 572.207 1.00130.83 C ANISOU 2274 CB ILE A1102 18813 21133 9765 -673 170 969 C ATOM 2275 CG1 ILE A1102 177.643 22.495 570.910 1.00123.12 C ANISOU 2275 CG1 ILE A1102 17620 20097 9063 -678 -16 967 C ATOM 2276 CG2 ILE A1102 176.358 23.886 572.543 1.00120.77 C ANISOU 2276 CG2 ILE A1102 17718 19829 8339 -727 348 641 C ATOM 2277 CD1 ILE A1102 176.903 23.091 569.732 1.00124.07 C ANISOU 2277 CD1 ILE A1102 17664 20063 9412 -645 172 833 C ATOM 2278 N GLN A1103 178.449 23.505 575.034 1.00159.10 N ANISOU 2278 N GLN A1103 22794 25052 12603 -871 -150 730 N ATOM 2279 CA GLN A1103 179.457 24.370 575.636 1.00158.05 C ANISOU 2279 CA GLN A1103 22754 25028 12272 -988 -346 526 C ATOM 2280 C GLN A1103 180.720 23.583 575.965 1.00152.89 C ANISOU 2280 C GLN A1103 21997 24521 11574 -1009 -683 713 C ATOM 2281 O GLN A1103 181.837 24.048 575.711 1.00149.28 O ANISOU 2281 O GLN A1103 21447 24119 11153 -1097 -917 602 O ATOM 2282 CB GLN A1103 178.896 25.033 576.894 1.00165.33 C ANISOU 2282 CB GLN A1103 23948 26009 12861 -1017 -185 366 C ATOM 2283 CG GLN A1103 179.548 26.359 577.244 1.00168.70 C ANISOU 2283 CG GLN A1103 24492 26471 13137 -1142 -276 48 C ATOM 2284 CD GLN A1103 178.972 27.514 576.448 1.00164.20 C ANISOU 2284 CD GLN A1103 23945 25723 12721 -1152 -78 -227 C ATOM 2285 OE1 GLN A1103 177.765 27.581 576.216 1.00159.80 O ANISOU 2285 OE1 GLN A1103 23430 25054 12234 -1057 214 -243 O ATOM 2286 NE2 GLN A1103 179.835 28.430 576.023 1.00164.08 N ANISOU 2286 NE2 GLN A1103 23900 25676 12767 -1269 -233 -442 N ATOM 2287 N LYS A1104 180.560 22.384 576.524 1.00158.66 N ANISOU 2287 N LYS A1104 22738 25309 12237 -927 -708 999 N ATOM 2288 CA LYS A1104 181.688 21.531 576.868 1.00145.32 C ANISOU 2288 CA LYS A1104 20955 23746 10514 -915 -1017 1202 C ATOM 2289 C LYS A1104 182.059 20.555 575.760 1.00145.51 C ANISOU 2289 C LYS A1104 20717 23693 10878 -823 -1133 1423 C ATOM 2290 O LYS A1104 183.072 19.858 575.886 1.00132.43 O ANISOU 2290 O LYS A1104 18948 22125 9245 -793 -1398 1584 O ATOM 2291 CB LYS A1104 181.389 20.754 578.156 1.00130.15 C ANISOU 2291 CB LYS A1104 19215 21920 8315 -872 -998 1393 C ATOM 2292 CG LYS A1104 181.143 21.639 579.368 1.00123.35 C ANISOU 2292 CG LYS A1104 18619 21161 7086 -954 -911 1189 C ATOM 2293 CD LYS A1104 181.051 20.824 580.646 1.00124.26 C ANISOU 2293 CD LYS A1104 18908 21393 6911 -917 -940 1393 C ATOM 2294 CE LYS A1104 180.920 21.729 581.859 1.00130.47 C ANISOU 2294 CE LYS A1104 19955 22298 7319 -998 -877 1181 C ATOM 2295 NZ LYS A1104 180.918 20.957 583.132 1.00134.15 N ANISOU 2295 NZ LYS A1104 20599 22894 7477 -967 -925 1379 N ATOM 2296 N TYR A1105 181.267 20.483 574.687 1.00157.49 N ANISOU 2296 N TYR A1105 22134 25047 12659 -768 -941 1435 N ATOM 2297 CA TYR A1105 181.625 19.626 573.561 1.00163.27 C ANISOU 2297 CA TYR A1105 22617 25694 13722 -679 -1044 1623 C ATOM 2298 C TYR A1105 182.892 20.120 572.872 1.00168.64 C ANISOU 2298 C TYR A1105 23116 26423 14537 -738 -1290 1501 C ATOM 2299 O TYR A1105 183.732 19.315 572.452 1.00172.76 O ANISOU 2299 O TYR A1105 23449 26964 15228 -670 -1496 1674 O ATOM 2300 CB TYR A1105 180.462 19.551 572.572 1.00162.49 C ANISOU 2300 CB TYR A1105 22461 25417 13860 -618 -779 1637 C ATOM 2301 CG TYR A1105 180.844 19.037 571.202 1.00156.34 C ANISOU 2301 CG TYR A1105 21429 24536 13437 -547 -869 1742 C ATOM 2302 CD1 TYR A1105 181.069 17.684 570.983 1.00154.88 C ANISOU 2302 CD1 TYR A1105 21124 24309 13415 -432 -969 2037 C ATOM 2303 CD2 TYR A1105 180.968 19.905 570.125 1.00158.59 C ANISOU 2303 CD2 TYR A1105 21609 24753 13894 -592 -848 1542 C ATOM 2304 CE1 TYR A1105 181.415 17.212 569.731 1.00158.21 C ANISOU 2304 CE1 TYR A1105 21322 24626 14163 -357 -1042 2125 C ATOM 2305 CE2 TYR A1105 181.313 19.442 568.871 1.00161.18 C ANISOU 2305 CE2 TYR A1105 21714 24991 14536 -525 -924 1636 C ATOM 2306 CZ TYR A1105 181.535 18.096 568.679 1.00158.47 C ANISOU 2306 CZ TYR A1105 21249 24609 14351 -404 -1019 1925 C ATOM 2307 OH TYR A1105 181.878 17.634 567.430 1.00149.78 O ANISOU 2307 OH TYR A1105 19936 23407 13566 -328 -1086 2010 O ATOM 2308 N LEU A1106 183.047 21.435 572.748 1.00174.06 N ANISOU 2308 N LEU A1106 23856 27119 15159 -862 -1264 1200 N ATOM 2309 CA LEU A1106 184.255 22.021 572.178 1.00166.18 C ANISOU 2309 CA LEU A1106 22703 26172 14268 -952 -1485 1057 C ATOM 2310 C LEU A1106 184.839 23.077 573.110 1.00163.60 C ANISOU 2310 C LEU A1106 22525 25970 13666 -1105 -1583 816 C ATOM 2311 O LEU A1106 185.771 22.804 573.867 1.00157.87 O ANISOU 2311 O LEU A1106 21782 25404 12797 -1133 -1815 879 O ATOM 2312 CB LEU A1106 183.965 22.632 570.805 1.00155.78 C ANISOU 2312 CB LEU A1106 21276 24700 13213 -972 -1367 913 C ATOM 2313 CG LEU A1106 184.015 21.681 569.609 1.00148.44 C ANISOU 2313 CG LEU A1106 20110 23677 12612 -849 -1395 1122 C ATOM 2314 CD1 LEU A1106 183.647 22.410 568.326 1.00138.68 C ANISOU 2314 CD1 LEU A1106 18806 22294 11592 -881 -1263 956 C ATOM 2315 CD2 LEU A1106 185.391 21.045 569.491 1.00151.26 C ANISOU 2315 CD2 LEU A1106 20259 24144 13067 -827 -1695 1252 C ATOM 2316 N LYS A 383 179.958 15.771 554.120 1.00 72.40 N ANISOU 2316 N LYS A 383 8916 11599 6993 246 -539 1946 N ATOM 2317 CA LYS A 383 179.876 17.134 554.632 1.00 77.53 C ANISOU 2317 CA LYS A 383 9670 12342 7445 135 -499 1730 C ATOM 2318 C LYS A 383 179.203 18.047 553.609 1.00 85.44 C ANISOU 2318 C LYS A 383 10698 13150 8615 104 -365 1539 C ATOM 2319 O LYS A 383 179.193 17.753 552.414 1.00 88.30 O ANISOU 2319 O LYS A 383 10974 13343 9233 146 -356 1545 O ATOM 2320 CB LYS A 383 181.271 17.656 554.988 1.00 76.54 C ANISOU 2320 CB LYS A 383 9501 12404 7177 56 -685 1639 C ATOM 2321 CG LYS A 383 181.273 18.885 555.885 1.00 68.64 C ANISOU 2321 CG LYS A 383 8637 11543 5899 -70 -669 1450 C ATOM 2322 CD LYS A 383 182.686 19.286 556.266 1.00 67.18 C ANISOU 2322 CD LYS A 383 8393 11560 5572 -164 -873 1375 C ATOM 2323 CE LYS A 383 182.693 20.544 557.117 1.00 74.95 C ANISOU 2323 CE LYS A 383 9532 12666 6281 -308 -857 1165 C ATOM 2324 NZ LYS A 383 184.078 20.974 557.454 1.00 79.66 N ANISOU 2324 NZ LYS A 383 10059 13465 6742 -425 -1065 1079 N ATOM 2325 N LYS A 384 178.637 19.156 554.090 1.00 93.26 N ANISOU 2325 N LYS A 384 11818 14165 9453 36 -262 1369 N ATOM 2326 CA LYS A 384 177.915 20.069 553.209 1.00 94.14 C ANISOU 2326 CA LYS A 384 11972 14089 9709 24 -133 1197 C ATOM 2327 C LYS A 384 178.854 20.763 552.228 1.00 90.48 C ANISOU 2327 C LYS A 384 11462 13555 9362 -42 -223 1046 C ATOM 2328 O LYS A 384 178.493 20.983 551.066 1.00 89.54 O ANISOU 2328 O LYS A 384 11318 13244 9458 -20 -164 989 O ATOM 2329 CB LYS A 384 177.146 21.094 554.046 1.00107.08 C ANISOU 2329 CB LYS A 384 13768 15771 11145 -17 -1 1049 C ATOM 2330 CG LYS A 384 176.568 22.263 553.260 1.00114.14 C ANISOU 2330 CG LYS A 384 14731 16487 12152 -30 110 844 C ATOM 2331 CD LYS A 384 177.391 23.527 553.471 1.00119.10 C ANISOU 2331 CD LYS A 384 15460 17161 12632 -153 49 622 C ATOM 2332 CE LYS A 384 176.847 24.689 552.658 1.00119.22 C ANISOU 2332 CE LYS A 384 15561 16971 12764 -158 155 430 C ATOM 2333 NZ LYS A 384 177.671 25.916 552.835 1.00120.09 N ANISOU 2333 NZ LYS A 384 15787 17103 12738 -296 98 214 N ATOM 2334 N VAL A 385 180.062 21.113 552.676 1.00 90.85 N ANISOU 2334 N VAL A 385 11494 13763 9264 -134 -367 982 N ATOM 2335 CA VAL A 385 181.004 21.822 551.811 1.00 77.26 C ANISOU 2335 CA VAL A 385 9725 11993 7636 -223 -444 833 C ATOM 2336 C VAL A 385 181.397 20.949 550.625 1.00 74.82 C ANISOU 2336 C VAL A 385 9258 11576 7593 -152 -490 941 C ATOM 2337 O VAL A 385 181.354 21.383 549.466 1.00 86.72 O ANISOU 2337 O VAL A 385 10756 12915 9278 -170 -445 846 O ATOM 2338 CB VAL A 385 182.236 22.271 552.616 1.00 72.23 C ANISOU 2338 CB VAL A 385 9079 11582 6785 -346 -599 756 C ATOM 2339 CG1 VAL A 385 183.188 23.063 551.734 1.00 72.94 C ANISOU 2339 CG1 VAL A 385 9117 11626 6970 -464 -661 593 C ATOM 2340 CG2 VAL A 385 181.809 23.091 553.824 1.00 72.84 C ANISOU 2340 CG2 VAL A 385 9333 11763 6579 -419 -547 642 C ATOM 2341 N THR A 386 181.787 19.701 550.901 1.00 68.60 N ANISOU 2341 N THR A 386 8359 10878 6830 -65 -579 1141 N ATOM 2342 CA THR A 386 182.125 18.772 549.826 1.00 61.85 C ANISOU 2342 CA THR A 386 7365 9911 6224 19 -612 1247 C ATOM 2343 C THR A 386 180.936 18.551 548.899 1.00 55.83 C ANISOU 2343 C THR A 386 6641 8912 5661 85 -466 1267 C ATOM 2344 O THR A 386 181.103 18.395 547.682 1.00 50.06 O ANISOU 2344 O THR A 386 5847 8037 5138 104 -458 1243 O ATOM 2345 CB THR A 386 182.604 17.445 550.418 1.00 52.44 C ANISOU 2345 CB THR A 386 6076 8838 5010 120 -719 1471 C ATOM 2346 OG1 THR A 386 183.561 17.701 551.454 1.00 53.59 O ANISOU 2346 OG1 THR A 386 6199 9230 4932 60 -861 1460 O ATOM 2347 CG2 THR A 386 183.253 16.584 549.348 1.00 50.22 C ANISOU 2347 CG2 THR A 386 5646 8465 4972 201 -772 1549 C ATOM 2348 N ARG A 387 179.723 18.547 549.459 1.00 49.12 N ANISOU 2348 N ARG A 387 5890 8030 4745 117 -351 1305 N ATOM 2349 CA ARG A 387 178.519 18.418 548.646 1.00 49.65 C ANISOU 2349 CA ARG A 387 5980 7893 4990 171 -218 1315 C ATOM 2350 C ARG A 387 178.396 19.578 547.666 1.00 44.21 C ANISOU 2350 C ARG A 387 5341 7067 4390 113 -169 1118 C ATOM 2351 O ARG A 387 178.148 19.379 546.469 1.00 41.93 O ANISOU 2351 O ARG A 387 5015 6610 4308 144 -143 1116 O ATOM 2352 CB ARG A 387 177.290 18.346 549.554 1.00 64.48 C ANISOU 2352 CB ARG A 387 7942 9801 6758 201 -97 1374 C ATOM 2353 CG ARG A 387 176.124 17.601 548.948 1.00 86.70 C ANISOU 2353 CG ARG A 387 10725 12457 9762 275 7 1480 C ATOM 2354 CD ARG A 387 176.531 16.178 548.647 1.00 98.61 C ANISOU 2354 CD ARG A 387 12138 13932 11397 335 -69 1673 C ATOM 2355 NE ARG A 387 175.890 15.669 547.442 1.00105.68 N ANISOU 2355 NE ARG A 387 12987 14626 12541 375 -19 1703 N ATOM 2356 CZ ARG A 387 176.375 14.670 546.717 1.00 99.87 C ANISOU 2356 CZ ARG A 387 12177 13802 11968 419 -85 1802 C ATOM 2357 NH1 ARG A 387 177.508 14.084 547.075 1.00 86.80 N ANISOU 2357 NH1 ARG A 387 10472 12242 10266 446 -201 1886 N ATOM 2358 NH2 ARG A 387 175.734 14.265 545.632 1.00103.59 N ANISOU 2358 NH2 ARG A 387 12622 14091 12647 440 -37 1812 N ATOM 2359 N THR A 388 178.568 20.805 548.164 1.00 45.86 N ANISOU 2359 N THR A 388 5650 7338 4436 26 -157 950 N ATOM 2360 CA THR A 388 178.518 21.983 547.304 1.00 50.54 C ANISOU 2360 CA THR A 388 6315 7791 5095 -35 -114 764 C ATOM 2361 C THR A 388 179.579 21.912 546.212 1.00 61.09 C ANISOU 2361 C THR A 388 7565 9077 6570 -82 -201 735 C ATOM 2362 O THR A 388 179.298 22.172 545.033 1.00 53.47 O ANISOU 2362 O THR A 388 6613 7935 5768 -76 -158 684 O ATOM 2363 CB THR A 388 178.696 23.246 548.148 1.00 50.41 C ANISOU 2363 CB THR A 388 6434 7857 4863 -133 -100 592 C ATOM 2364 OG1 THR A 388 177.538 23.445 548.969 1.00 59.34 O ANISOU 2364 OG1 THR A 388 7660 8999 5889 -78 20 591 O ATOM 2365 CG2 THR A 388 178.909 24.460 547.261 1.00 45.24 C ANISOU 2365 CG2 THR A 388 5864 7055 4270 -215 -78 405 C ATOM 2366 N ILE A 389 180.810 21.552 546.590 1.00 55.03 N ANISOU 2366 N ILE A 389 6702 8472 5735 -126 -325 768 N ATOM 2367 CA ILE A 389 181.895 21.463 545.616 1.00 43.34 C ANISOU 2367 CA ILE A 389 5116 6971 4380 -171 -398 737 C ATOM 2368 C ILE A 389 181.543 20.469 544.517 1.00 41.99 C ANISOU 2368 C ILE A 389 4868 6646 4438 -66 -366 849 C ATOM 2369 O ILE A 389 181.705 20.754 543.323 1.00 54.79 O ANISOU 2369 O ILE A 389 6487 8133 6198 -95 -341 777 O ATOM 2370 CB ILE A 389 183.215 21.092 546.316 1.00 53.66 C ANISOU 2370 CB ILE A 389 6300 8507 5582 -210 -541 777 C ATOM 2371 CG1 ILE A 389 183.656 22.226 547.244 1.00 60.91 C ANISOU 2371 CG1 ILE A 389 7303 9568 6272 -351 -582 629 C ATOM 2372 CG2 ILE A 389 184.296 20.780 545.292 1.00 46.33 C ANISOU 2372 CG2 ILE A 389 5225 7568 4810 -227 -601 770 C ATOM 2373 CD1 ILE A 389 184.971 21.972 547.937 1.00 50.83 C ANISOU 2373 CD1 ILE A 389 5895 8537 4880 -407 -742 655 C ATOM 2374 N LEU A 390 181.040 19.291 544.900 1.00 41.06 N ANISOU 2374 N LEU A 390 4703 6539 4357 49 -364 1026 N ATOM 2375 CA LEU A 390 180.633 18.311 543.897 1.00 38.60 C ANISOU 2375 CA LEU A 390 4338 6070 4259 140 -331 1127 C ATOM 2376 C LEU A 390 179.530 18.861 543.003 1.00 42.86 C ANISOU 2376 C LEU A 390 4969 6413 4902 136 -226 1050 C ATOM 2377 O LEU A 390 179.518 18.604 541.794 1.00 45.63 O ANISOU 2377 O LEU A 390 5296 6621 5418 151 -212 1041 O ATOM 2378 CB LEU A 390 180.171 17.016 544.564 1.00 34.98 C ANISOU 2378 CB LEU A 390 3841 5641 3808 246 -337 1328 C ATOM 2379 CG LEU A 390 179.696 15.962 543.558 1.00 33.84 C ANISOU 2379 CG LEU A 390 3656 5318 3882 327 -302 1427 C ATOM 2380 CD1 LEU A 390 180.848 15.501 542.675 1.00 33.60 C ANISOU 2380 CD1 LEU A 390 3524 5266 3977 345 -369 1420 C ATOM 2381 CD2 LEU A 390 179.027 14.783 544.242 1.00 41.54 C ANISOU 2381 CD2 LEU A 390 4628 6294 4863 410 -284 1622 C ATOM 2382 N ALA A 391 178.592 19.618 543.577 1.00 44.77 N ANISOU 2382 N ALA A 391 5317 6649 5045 123 -152 993 N ATOM 2383 CA ALA A 391 177.519 20.195 542.773 1.00 34.52 C ANISOU 2383 CA ALA A 391 4096 5174 3845 137 -62 924 C ATOM 2384 C ALA A 391 178.076 21.132 541.707 1.00 36.53 C ANISOU 2384 C ALA A 391 4398 5328 4152 60 -74 777 C ATOM 2385 O ALA A 391 177.721 21.031 540.525 1.00 43.95 O ANISOU 2385 O ALA A 391 5344 6112 5243 80 -52 772 O ATOM 2386 CB ALA A 391 176.525 20.929 543.672 1.00 47.05 C ANISOU 2386 CB ALA A 391 5779 6790 5306 148 24 875 C ATOM 2387 N ILE A 392 178.966 22.044 542.107 1.00 44.38 N ANISOU 2387 N ILE A 392 5434 6411 5015 -41 -110 657 N ATOM 2388 CA ILE A 392 179.525 22.998 541.152 1.00 47.48 C ANISOU 2388 CA ILE A 392 5887 6708 5444 -138 -112 518 C ATOM 2389 C ILE A 392 180.342 22.276 540.086 1.00 47.39 C ANISOU 2389 C ILE A 392 5768 6665 5573 -144 -157 561 C ATOM 2390 O ILE A 392 180.230 22.573 538.888 1.00 45.86 O ANISOU 2390 O ILE A 392 5619 6319 5485 -164 -126 513 O ATOM 2391 CB ILE A 392 180.363 24.060 541.889 1.00 49.02 C ANISOU 2391 CB ILE A 392 6144 7016 5464 -268 -144 383 C ATOM 2392 CG1 ILE A 392 179.538 24.709 543.001 1.00 61.67 C ANISOU 2392 CG1 ILE A 392 7865 8651 6916 -252 -89 333 C ATOM 2393 CG2 ILE A 392 180.855 25.116 540.917 1.00 50.90 C ANISOU 2393 CG2 ILE A 392 6468 7135 5736 -385 -130 241 C ATOM 2394 CD1 ILE A 392 180.303 25.729 543.814 1.00 76.64 C ANISOU 2394 CD1 ILE A 392 9841 10657 8623 -388 -122 191 C ATOM 2395 N LEU A 393 181.168 21.311 540.502 1.00 41.05 N ANISOU 2395 N LEU A 393 4824 6003 4768 -118 -227 655 N ATOM 2396 CA LEU A 393 181.995 20.580 539.546 1.00 39.77 C ANISOU 2396 CA LEU A 393 4550 5819 4741 -106 -259 691 C ATOM 2397 C LEU A 393 181.137 19.825 538.537 1.00 42.99 C ANISOU 2397 C LEU A 393 4970 6048 5316 -16 -209 764 C ATOM 2398 O LEU A 393 181.400 19.863 537.329 1.00 44.33 O ANISOU 2398 O LEU A 393 5146 6109 5590 -42 -189 717 O ATOM 2399 CB LEU A 393 182.930 19.620 540.282 1.00 39.17 C ANISOU 2399 CB LEU A 393 4319 5925 4638 -60 -347 794 C ATOM 2400 CG LEU A 393 183.984 20.254 541.193 1.00 50.13 C ANISOU 2400 CG LEU A 393 5661 7521 5866 -160 -425 723 C ATOM 2401 CD1 LEU A 393 184.949 19.202 541.721 1.00 59.57 C ANISOU 2401 CD1 LEU A 393 6681 8888 7065 -90 -526 841 C ATOM 2402 CD2 LEU A 393 184.729 21.362 540.468 1.00 55.60 C ANISOU 2402 CD2 LEU A 393 6380 8193 6554 -313 -412 556 C ATOM 2403 N LEU A 394 180.099 19.134 539.015 1.00 36.46 N ANISOU 2403 N LEU A 394 4150 5192 4511 79 -187 877 N ATOM 2404 CA LEU A 394 179.235 18.380 538.112 1.00 35.03 C ANISOU 2404 CA LEU A 394 3976 4849 4486 150 -149 946 C ATOM 2405 C LEU A 394 178.475 19.305 537.171 1.00 35.81 C ANISOU 2405 C LEU A 394 4189 4792 4625 112 -98 845 C ATOM 2406 O LEU A 394 178.252 18.961 536.003 1.00 35.03 O ANISOU 2406 O LEU A 394 4101 4560 4650 125 -87 848 O ATOM 2407 CB LEU A 394 178.267 17.508 538.910 1.00 28.89 C ANISOU 2407 CB LEU A 394 3178 4084 3713 235 -131 1087 C ATOM 2408 CG LEU A 394 178.888 16.301 539.614 1.00 32.18 C ANISOU 2408 CG LEU A 394 3495 4604 4127 297 -185 1228 C ATOM 2409 CD1 LEU A 394 177.817 15.461 540.290 1.00 44.67 C ANISOU 2409 CD1 LEU A 394 5082 6170 5720 363 -150 1372 C ATOM 2410 CD2 LEU A 394 179.691 15.466 538.631 1.00 32.05 C ANISOU 2410 CD2 LEU A 394 3406 4519 4251 330 -216 1251 C ATOM 2411 N ALA A 395 178.065 20.479 537.657 1.00 33.20 N ANISOU 2411 N ALA A 395 3955 4472 4189 72 -68 757 N ATOM 2412 CA ALA A 395 177.445 21.459 536.770 1.00 36.34 C ANISOU 2412 CA ALA A 395 4471 4717 4618 46 -29 662 C ATOM 2413 C ALA A 395 178.407 21.868 535.660 1.00 34.55 C ANISOU 2413 C ALA A 395 4273 4429 4424 -42 -45 577 C ATOM 2414 O ALA A 395 178.037 21.902 534.480 1.00 34.05 O ANISOU 2414 O ALA A 395 4262 4221 4452 -38 -33 565 O ATOM 2415 CB ALA A 395 176.988 22.679 537.569 1.00 28.09 C ANISOU 2415 CB ALA A 395 3534 3691 3447 26 9 572 C ATOM 2416 N PHE A 396 179.658 22.162 536.025 1.00 42.00 N ANISOU 2416 N PHE A 396 5178 5491 5287 -129 -74 521 N ATOM 2417 CA PHE A 396 180.658 22.558 535.036 1.00 37.42 C ANISOU 2417 CA PHE A 396 4609 4877 4731 -230 -75 438 C ATOM 2418 C PHE A 396 180.882 21.459 534.001 1.00 36.75 C ANISOU 2418 C PHE A 396 4445 4736 4783 -182 -76 504 C ATOM 2419 O PHE A 396 180.839 21.710 532.789 1.00 37.09 O ANISOU 2419 O PHE A 396 4560 4650 4882 -219 -48 460 O ATOM 2420 CB PHE A 396 181.963 22.914 535.751 1.00 35.24 C ANISOU 2420 CB PHE A 396 4261 4775 4352 -332 -113 378 C ATOM 2421 CG PHE A 396 183.134 23.107 534.831 1.00 32.15 C ANISOU 2421 CG PHE A 396 3830 4392 3995 -440 -107 309 C ATOM 2422 CD1 PHE A 396 183.260 24.263 534.080 1.00 35.62 C ANISOU 2422 CD1 PHE A 396 4408 4720 4405 -563 -64 196 C ATOM 2423 CD2 PHE A 396 184.123 22.142 534.737 1.00 32.20 C ANISOU 2423 CD2 PHE A 396 3661 4516 4060 -415 -139 358 C ATOM 2424 CE1 PHE A 396 184.344 24.446 533.240 1.00 38.76 C ANISOU 2424 CE1 PHE A 396 4767 5135 4827 -678 -43 134 C ATOM 2425 CE2 PHE A 396 185.208 22.319 533.899 1.00 35.17 C ANISOU 2425 CE2 PHE A 396 3981 4914 4468 -514 -117 289 C ATOM 2426 CZ PHE A 396 185.319 23.472 533.149 1.00 32.39 C ANISOU 2426 CZ PHE A 396 3765 4461 4080 -654 -65 176 C ATOM 2427 N ILE A 397 181.107 20.227 534.465 1.00 35.44 N ANISOU 2427 N ILE A 397 4145 4657 4666 -97 -108 610 N ATOM 2428 CA ILE A 397 181.429 19.129 533.557 1.00 37.64 C ANISOU 2428 CA ILE A 397 4350 4879 5072 -45 -104 663 C ATOM 2429 C ILE A 397 180.250 18.822 532.642 1.00 33.70 C ANISOU 2429 C ILE A 397 3939 4199 4667 2 -77 693 C ATOM 2430 O ILE A 397 180.404 18.720 531.419 1.00 35.77 O ANISOU 2430 O ILE A 397 4240 4357 4994 -23 -54 654 O ATOM 2431 CB ILE A 397 181.858 17.885 534.356 1.00 45.07 C ANISOU 2431 CB ILE A 397 5147 5934 6044 51 -147 781 C ATOM 2432 CG1 ILE A 397 183.114 18.181 535.176 1.00 55.28 C ANISOU 2432 CG1 ILE A 397 6335 7426 7244 4 -194 750 C ATOM 2433 CG2 ILE A 397 182.090 16.706 533.422 1.00 40.44 C ANISOU 2433 CG2 ILE A 397 4505 5260 5600 121 -133 831 C ATOM 2434 CD1 ILE A 397 183.522 17.050 536.092 1.00 56.22 C ANISOU 2434 CD1 ILE A 397 6321 7667 7372 110 -254 879 C ATOM 2435 N ILE A 398 179.056 18.670 533.219 1.00 35.89 N ANISOU 2435 N ILE A 398 4243 4446 4946 66 -78 760 N ATOM 2436 CA ILE A 398 177.892 18.298 532.420 1.00 36.39 C ANISOU 2436 CA ILE A 398 4362 4359 5105 108 -66 796 C ATOM 2437 C ILE A 398 177.516 19.410 531.447 1.00 37.27 C ANISOU 2437 C ILE A 398 4606 4354 5200 49 -51 699 C ATOM 2438 O ILE A 398 177.048 19.139 530.334 1.00 28.41 O ANISOU 2438 O ILE A 398 3534 3108 4153 54 -54 700 O ATOM 2439 CB ILE A 398 176.717 17.923 533.343 1.00 30.92 C ANISOU 2439 CB ILE A 398 3645 3686 4418 179 -63 890 C ATOM 2440 CG1 ILE A 398 177.050 16.654 534.129 1.00 39.46 C ANISOU 2440 CG1 ILE A 398 4617 4850 5526 238 -79 1009 C ATOM 2441 CG2 ILE A 398 175.436 17.724 532.546 1.00 24.49 C ANISOU 2441 CG2 ILE A 398 2875 2733 3697 207 -58 914 C ATOM 2442 CD1 ILE A 398 175.939 16.192 535.045 1.00 53.08 C ANISOU 2442 CD1 ILE A 398 6319 6599 7251 292 -62 1114 C ATOM 2443 N THR A 399 177.728 20.672 531.827 1.00 37.42 N ANISOU 2443 N THR A 399 4699 4404 5115 -9 -39 615 N ATOM 2444 CA THR A 399 177.368 21.762 530.929 1.00 33.09 C ANISOU 2444 CA THR A 399 4298 3727 4549 -58 -26 535 C ATOM 2445 C THR A 399 178.413 21.999 529.845 1.00 36.15 C ANISOU 2445 C THR A 399 4730 4075 4932 -156 -13 466 C ATOM 2446 O THR A 399 178.074 22.514 528.774 1.00 34.58 O ANISOU 2446 O THR A 399 4653 3744 4741 -186 -8 431 O ATOM 2447 CB THR A 399 177.143 23.051 531.719 1.00 37.27 C ANISOU 2447 CB THR A 399 4916 4273 4972 -82 -9 467 C ATOM 2448 OG1 THR A 399 178.202 23.220 532.668 1.00 64.51 O ANISOU 2448 OG1 THR A 399 8307 7871 8331 -145 -9 431 O ATOM 2449 CG2 THR A 399 175.808 23.003 532.445 1.00 42.00 C ANISOU 2449 CG2 THR A 399 5504 4868 5584 24 -2 522 C ATOM 2450 N TRP A 400 179.674 21.635 530.087 1.00 40.09 N ANISOU 2450 N TRP A 400 5128 4690 5414 -204 -6 449 N ATOM 2451 CA TRP A 400 180.743 21.929 529.140 1.00 40.49 C ANISOU 2451 CA TRP A 400 5203 4727 5454 -310 26 375 C ATOM 2452 C TRP A 400 181.225 20.718 528.350 1.00 31.85 C ANISOU 2452 C TRP A 400 4021 3628 4454 -274 39 409 C ATOM 2453 O TRP A 400 182.062 20.878 527.456 1.00 29.67 O ANISOU 2453 O TRP A 400 3762 3338 4172 -355 83 346 O ATOM 2454 CB TRP A 400 181.931 22.568 529.865 1.00 26.21 C ANISOU 2454 CB TRP A 400 3339 3063 3558 -412 33 306 C ATOM 2455 CG TRP A 400 181.704 23.990 530.271 1.00 32.57 C ANISOU 2455 CG TRP A 400 4282 3833 4259 -495 40 229 C ATOM 2456 CD1 TRP A 400 180.536 24.546 530.704 1.00 26.40 C ANISOU 2456 CD1 TRP A 400 3609 2971 3451 -434 30 239 C ATOM 2457 CD2 TRP A 400 182.674 25.043 530.267 1.00 30.35 C ANISOU 2457 CD2 TRP A 400 4052 3588 3891 -655 64 124 C ATOM 2458 NE1 TRP A 400 180.720 25.880 530.978 1.00 27.68 N ANISOU 2458 NE1 TRP A 400 3901 3102 3515 -534 49 144 N ATOM 2459 CE2 TRP A 400 182.024 26.210 530.717 1.00 32.96 C ANISOU 2459 CE2 TRP A 400 4543 3837 4143 -682 67 73 C ATOM 2460 CE3 TRP A 400 184.029 25.113 529.928 1.00 28.33 C ANISOU 2460 CE3 TRP A 400 3715 3426 3621 -782 90 65 C ATOM 2461 CZ2 TRP A 400 182.684 27.430 530.838 1.00 46.52 C ANISOU 2461 CZ2 TRP A 400 6364 5547 5765 -842 91 -35 C ATOM 2462 CZ3 TRP A 400 184.681 26.325 530.050 1.00 29.34 C ANISOU 2462 CZ3 TRP A 400 3927 3566 3656 -952 113 -39 C ATOM 2463 CH2 TRP A 400 184.009 27.467 530.501 1.00 48.79 C ANISOU 2463 CH2 TRP A 400 6571 5929 6039 -986 111 -88 C ATOM 2464 N ALA A 401 180.723 19.514 528.645 1.00 28.94 N ANISOU 2464 N ALA A 401 3566 3261 4168 -159 14 503 N ATOM 2465 CA ALA A 401 181.191 18.331 527.923 1.00 34.13 C ANISOU 2465 CA ALA A 401 4155 3894 4919 -117 32 527 C ATOM 2466 C ALA A 401 180.724 18.291 526.470 1.00 48.39 C ANISOU 2466 C ALA A 401 6087 5542 6757 -144 54 493 C ATOM 2467 O ALA A 401 181.550 17.985 525.589 1.00 63.59 O ANISOU 2467 O ALA A 401 8005 7455 8701 -180 103 443 O ATOM 2468 CB ALA A 401 180.780 17.065 528.681 1.00 29.90 C ANISOU 2468 CB ALA A 401 3516 3384 4461 5 -1 642 C ATOM 2469 N PRO A 402 179.448 18.561 526.141 1.00 43.16 N ANISOU 2469 N PRO A 402 5534 4765 6099 -128 21 517 N ATOM 2470 CA PRO A 402 179.022 18.412 524.735 1.00 43.12 C ANISOU 2470 CA PRO A 402 5646 4621 6116 -153 24 491 C ATOM 2471 C PRO A 402 179.821 19.244 523.747 1.00 45.69 C ANISOU 2471 C PRO A 402 6077 4918 6365 -265 75 398 C ATOM 2472 O PRO A 402 180.174 18.738 522.676 1.00 40.99 O ANISOU 2472 O PRO A 402 5520 4268 5786 -290 111 365 O ATOM 2473 CB PRO A 402 177.549 18.843 524.775 1.00 44.18 C ANISOU 2473 CB PRO A 402 5862 4674 6253 -118 -36 532 C ATOM 2474 CG PRO A 402 177.116 18.552 526.157 1.00 39.01 C ANISOU 2474 CG PRO A 402 5094 4106 5624 -44 -55 602 C ATOM 2475 CD PRO A 402 178.301 18.877 527.014 1.00 37.78 C ANISOU 2475 CD PRO A 402 4862 4083 5410 -74 -22 572 C ATOM 2476 N TYR A 403 180.116 20.507 524.066 1.00 46.76 N ANISOU 2476 N TYR A 403 6271 5084 6412 -341 87 351 N ATOM 2477 CA TYR A 403 180.897 21.331 523.146 1.00 31.81 C ANISOU 2477 CA TYR A 403 4487 3159 4441 -468 146 269 C ATOM 2478 C TYR A 403 182.271 20.722 522.892 1.00 29.37 C ANISOU 2478 C TYR A 403 4060 2949 4152 -510 221 224 C ATOM 2479 O TYR A 403 182.746 20.689 521.749 1.00 29.53 O ANISOU 2479 O TYR A 403 4150 2922 4148 -578 283 174 O ATOM 2480 CB TYR A 403 181.032 22.751 523.697 1.00 25.19 C ANISOU 2480 CB TYR A 403 3729 2333 3511 -550 149 228 C ATOM 2481 CG TYR A 403 181.868 23.673 522.834 1.00 26.52 C ANISOU 2481 CG TYR A 403 4019 2464 3593 -705 217 149 C ATOM 2482 CD1 TYR A 403 181.287 24.423 521.820 1.00 32.13 C ANISOU 2482 CD1 TYR A 403 4943 3020 4245 -751 211 143 C ATOM 2483 CD2 TYR A 403 183.238 23.800 523.038 1.00 28.90 C ANISOU 2483 CD2 TYR A 403 4218 2893 3870 -810 284 88 C ATOM 2484 CE1 TYR A 403 182.045 25.268 521.031 1.00 34.24 C ANISOU 2484 CE1 TYR A 403 5339 3245 4424 -904 281 83 C ATOM 2485 CE2 TYR A 403 184.003 24.639 522.252 1.00 27.61 C ANISOU 2485 CE2 TYR A 403 4162 2701 3628 -971 359 18 C ATOM 2486 CZ TYR A 403 183.402 25.372 521.253 1.00 37.07 C ANISOU 2486 CZ TYR A 403 5593 3731 4762 -1022 363 18 C ATOM 2487 OH TYR A 403 184.163 26.210 520.472 1.00 54.04 O ANISOU 2487 OH TYR A 403 7866 5844 6823 -1194 445 -41 O ATOM 2488 N ASN A 404 182.920 20.222 523.944 1.00 37.88 N ANISOU 2488 N ASN A 404 4953 4169 5269 -464 218 244 N ATOM 2489 CA ASN A 404 184.273 19.700 523.790 1.00 39.43 C ANISOU 2489 CA ASN A 404 5009 4480 5494 -487 284 202 C ATOM 2490 C ASN A 404 184.282 18.380 523.028 1.00 44.42 C ANISOU 2490 C ASN A 404 5605 5055 6216 -397 314 220 C ATOM 2491 O ASN A 404 185.209 18.117 522.251 1.00 55.17 O ANISOU 2491 O ASN A 404 6933 6443 7586 -436 400 157 O ATOM 2492 CB ASN A 404 184.933 19.553 525.159 1.00 27.02 C ANISOU 2492 CB ASN A 404 3249 3083 3933 -452 251 227 C ATOM 2493 CG ASN A 404 185.165 20.892 525.833 1.00 30.68 C ANISOU 2493 CG ASN A 404 3752 3613 4294 -571 237 179 C ATOM 2494 OD1 ASN A 404 186.165 21.563 525.580 1.00 28.22 O ANISOU 2494 OD1 ASN A 404 3420 3371 3931 -704 290 100 O ATOM 2495 ND2 ASN A 404 184.234 21.291 526.691 1.00 37.31 N ANISOU 2495 ND2 ASN A 404 4649 4427 5100 -531 172 221 N ATOM 2496 N VAL A 405 183.262 17.536 523.222 1.00 28.31 N ANISOU 2496 N VAL A 405 3576 2935 4246 -284 254 297 N ATOM 2497 CA VAL A 405 183.203 16.335 522.392 1.00 31.23 C ANISOU 2497 CA VAL A 405 3952 3219 4695 -218 283 300 C ATOM 2498 C VAL A 405 182.861 16.706 520.952 1.00 42.99 C ANISOU 2498 C VAL A 405 5628 4580 6126 -303 317 237 C ATOM 2499 O VAL A 405 183.260 16.005 520.012 1.00 61.06 O ANISOU 2499 O VAL A 405 7940 6821 8439 -298 382 190 O ATOM 2500 CB VAL A 405 182.222 15.296 522.972 1.00 30.43 C ANISOU 2500 CB VAL A 405 3817 3058 4685 -96 212 400 C ATOM 2501 CG1 VAL A 405 182.495 15.072 524.454 1.00 30.96 C ANISOU 2501 CG1 VAL A 405 3727 3257 4780 -23 173 475 C ATOM 2502 CG2 VAL A 405 180.776 15.700 522.736 1.00 52.04 C ANISOU 2502 CG2 VAL A 405 6693 5683 7399 -116 144 432 C ATOM 2503 N MET A 406 182.144 17.817 520.748 1.00 40.11 N ANISOU 2503 N MET A 406 5408 4157 5676 -377 276 235 N ATOM 2504 CA MET A 406 181.954 18.328 519.395 1.00 35.43 C ANISOU 2504 CA MET A 406 5005 3457 5001 -470 303 181 C ATOM 2505 C MET A 406 183.270 18.792 518.788 1.00 40.76 C ANISOU 2505 C MET A 406 5684 4194 5610 -582 421 94 C ATOM 2506 O MET A 406 183.449 18.716 517.567 1.00 57.44 O ANISOU 2506 O MET A 406 7914 6239 7670 -642 482 41 O ATOM 2507 CB MET A 406 180.945 19.478 519.388 1.00 27.78 C ANISOU 2507 CB MET A 406 4185 2410 3959 -508 228 209 C ATOM 2508 CG MET A 406 179.520 19.078 519.718 1.00 24.73 C ANISOU 2508 CG MET A 406 3807 1956 3633 -409 119 288 C ATOM 2509 SD MET A 406 178.482 20.519 520.033 0.75 24.45 S ANISOU 2509 SD MET A 406 3895 1863 3531 -419 42 319 S ATOM 2510 CE MET A 406 177.314 19.843 521.210 1.00 23.79 C ANISOU 2510 CE MET A 406 3674 1809 3556 -284 -40 411 C ATOM 2511 N VAL A 407 184.194 19.286 519.614 1.00 40.31 N ANISOU 2511 N VAL A 407 5498 4272 5545 -622 456 74 N ATOM 2512 CA VAL A 407 185.521 19.633 519.114 1.00 49.83 C ANISOU 2512 CA VAL A 407 6664 5565 6706 -735 576 -10 C ATOM 2513 C VAL A 407 186.293 18.373 518.741 1.00 44.39 C ANISOU 2513 C VAL A 407 5838 4928 6102 -657 656 -42 C ATOM 2514 O VAL A 407 186.876 18.279 517.651 1.00 51.44 O ANISOU 2514 O VAL A 407 6785 5803 6955 -722 765 -114 O ATOM 2515 CB VAL A 407 186.282 20.476 520.154 1.00 50.14 C ANISOU 2515 CB VAL A 407 6585 5746 6718 -809 577 -27 C ATOM 2516 CG1 VAL A 407 187.707 20.735 519.689 1.00 58.89 C ANISOU 2516 CG1 VAL A 407 7608 6970 7797 -933 704 -113 C ATOM 2517 CG2 VAL A 407 185.553 21.787 520.411 1.00 35.36 C ANISOU 2517 CG2 VAL A 407 4884 3796 4757 -890 517 -13 C ATOM 2518 N LEU A 408 186.297 17.380 519.638 1.00 37.69 N ANISOU 2518 N LEU A 408 4820 4135 5366 -512 608 13 N ATOM 2519 CA LEU A 408 187.011 16.133 519.375 1.00 36.22 C ANISOU 2519 CA LEU A 408 4504 3981 5277 -408 679 -9 C ATOM 2520 C LEU A 408 186.515 15.465 518.098 1.00 42.06 C ANISOU 2520 C LEU A 408 5403 4565 6015 -393 722 -46 C ATOM 2521 O LEU A 408 187.320 15.002 517.279 1.00 30.98 O ANISOU 2521 O LEU A 408 3979 3174 4619 -396 842 -124 O ATOM 2522 CB LEU A 408 186.870 15.187 520.568 1.00 38.75 C ANISOU 2522 CB LEU A 408 4662 4350 5713 -245 598 81 C ATOM 2523 CG LEU A 408 187.304 13.729 520.383 1.00 52.83 C ANISOU 2523 CG LEU A 408 6344 6112 7619 -96 646 85 C ATOM 2524 CD1 LEU A 408 188.749 13.630 519.920 1.00 66.63 C ANISOU 2524 CD1 LEU A 408 7955 7979 9384 -107 776 -6 C ATOM 2525 CD2 LEU A 408 187.104 12.953 521.675 1.00 56.41 C ANISOU 2525 CD2 LEU A 408 6660 6605 8167 51 552 197 C ATOM 2526 N ILE A 409 185.195 15.405 517.907 1.00 46.62 N ANISOU 2526 N ILE A 409 6136 5000 6577 -379 627 5 N ATOM 2527 CA ILE A 409 184.660 14.850 516.666 1.00 45.33 C ANISOU 2527 CA ILE A 409 6141 4693 6391 -387 648 -35 C ATOM 2528 C ILE A 409 184.976 15.770 515.492 1.00 43.59 C ANISOU 2528 C ILE A 409 6084 4450 6026 -539 728 -115 C ATOM 2529 O ILE A 409 185.241 15.309 514.376 1.00 56.80 O ANISOU 2529 O ILE A 409 7851 6067 7662 -565 816 -189 O ATOM 2530 CB ILE A 409 183.148 14.597 516.802 1.00 49.87 C ANISOU 2530 CB ILE A 409 6817 5143 6988 -346 511 42 C ATOM 2531 CG1 ILE A 409 182.875 13.587 517.919 1.00 43.85 C ANISOU 2531 CG1 ILE A 409 5902 4394 6363 -207 452 125 C ATOM 2532 CG2 ILE A 409 182.564 14.105 515.487 1.00 49.35 C ANISOU 2532 CG2 ILE A 409 6935 4936 6881 -377 514 -6 C ATOM 2533 CD1 ILE A 409 181.409 13.306 518.138 1.00 37.82 C ANISOU 2533 CD1 ILE A 409 5209 3528 5634 -177 330 203 C ATOM 2534 N ASN A 410 184.970 17.084 515.730 1.00 37.72 N ANISOU 2534 N ASN A 410 5392 3746 5194 -647 706 -102 N ATOM 2535 CA ASN A 410 185.250 18.047 514.672 1.00 32.99 C ANISOU 2535 CA ASN A 410 4969 3115 4449 -803 779 -159 C ATOM 2536 C ASN A 410 186.674 17.932 514.144 1.00 47.87 C ANISOU 2536 C ASN A 410 6771 5103 6314 -869 954 -254 C ATOM 2537 O ASN A 410 186.938 18.357 513.013 1.00 60.71 O ANISOU 2537 O ASN A 410 8556 6692 7821 -989 1046 -312 O ATOM 2538 CB ASN A 410 184.989 19.466 515.183 1.00 43.19 C ANISOU 2538 CB ASN A 410 6329 4414 5666 -896 720 -121 C ATOM 2539 CG ASN A 410 185.276 20.529 514.139 1.00 52.33 C ANISOU 2539 CG ASN A 410 7690 5524 6669 -1065 794 -164 C ATOM 2540 OD1 ASN A 410 184.458 20.784 513.255 1.00 68.38 O ANISOU 2540 OD1 ASN A 410 9939 7427 8613 -1094 745 -145 O ATOM 2541 ND2 ASN A 410 186.441 21.159 514.240 1.00 41.09 N ANISOU 2541 ND2 ASN A 410 6196 4208 5209 -1185 908 -217 N ATOM 2542 N THR A 411 187.595 17.369 514.930 1.00 49.84 N ANISOU 2542 N THR A 411 6772 5490 6674 -792 1004 -267 N ATOM 2543 CA THR A 411 188.971 17.216 514.462 1.00 45.25 C ANISOU 2543 CA THR A 411 6074 5028 6093 -840 1175 -360 C ATOM 2544 C THR A 411 189.039 16.364 513.198 1.00 41.18 C ANISOU 2544 C THR A 411 5664 4426 5555 -814 1282 -434 C ATOM 2545 O THR A 411 189.690 16.740 512.216 1.00 51.69 O ANISOU 2545 O THR A 411 7073 5780 6785 -936 1426 -515 O ATOM 2546 CB THR A 411 189.839 16.605 515.563 1.00 46.70 C ANISOU 2546 CB THR A 411 5956 5372 6418 -723 1182 -348 C ATOM 2547 OG1 THR A 411 189.330 15.314 515.920 1.00 53.92 O ANISOU 2547 OG1 THR A 411 6815 6217 7454 -530 1115 -300 O ATOM 2548 CG2 THR A 411 189.841 17.496 516.785 1.00 47.34 C ANISOU 2548 CG2 THR A 411 5944 5549 6493 -770 1082 -290 C ATOM 2549 N PHE A 412 188.369 15.210 513.202 1.00 34.04 N ANISOU 2549 N PHE A 412 4775 3419 4738 -665 1220 -411 N ATOM 2550 CA PHE A 412 188.443 14.273 512.090 1.00 41.44 C ANISOU 2550 CA PHE A 412 5811 4268 5665 -627 1319 -494 C ATOM 2551 C PHE A 412 187.196 14.248 511.218 1.00 50.90 C ANISOU 2551 C PHE A 412 7285 5290 6764 -674 1231 -483 C ATOM 2552 O PHE A 412 187.192 13.548 510.200 1.00 51.33 O ANISOU 2552 O PHE A 412 7460 5263 6780 -667 1308 -563 O ATOM 2553 CB PHE A 412 188.724 12.851 512.603 1.00 45.91 C ANISOU 2553 CB PHE A 412 6205 4832 6406 -428 1331 -494 C ATOM 2554 CG PHE A 412 187.718 12.354 513.605 1.00 47.08 C ANISOU 2554 CG PHE A 412 6321 4908 6657 -315 1156 -380 C ATOM 2555 CD1 PHE A 412 186.585 11.671 513.192 1.00 47.17 C ANISOU 2555 CD1 PHE A 412 6498 4747 6676 -281 1071 -361 C ATOM 2556 CD2 PHE A 412 187.913 12.561 514.961 1.00 49.58 C ANISOU 2556 CD2 PHE A 412 6442 5339 7057 -254 1077 -293 C ATOM 2557 CE1 PHE A 412 185.661 11.212 514.111 1.00 52.29 C ANISOU 2557 CE1 PHE A 412 7109 5338 7421 -192 924 -254 C ATOM 2558 CE2 PHE A 412 186.992 12.103 515.886 1.00 53.38 C ANISOU 2558 CE2 PHE A 412 6900 5761 7621 -158 932 -185 C ATOM 2559 CZ PHE A 412 185.865 11.428 515.460 1.00 55.12 C ANISOU 2559 CZ PHE A 412 7278 5809 7857 -129 861 -164 C ATOM 2560 N CYS A 413 186.144 14.978 511.581 1.00 50.82 N ANISOU 2560 N CYS A 413 7373 5224 6711 -716 1073 -394 N ATOM 2561 CA CYS A 413 184.931 15.020 510.767 1.00 47.40 C ANISOU 2561 CA CYS A 413 7182 4642 6185 -758 970 -376 C ATOM 2562 C CYS A 413 184.244 16.356 511.000 1.00 49.57 C ANISOU 2562 C CYS A 413 7560 4903 6370 -847 857 -297 C ATOM 2563 O CYS A 413 183.730 16.609 512.094 1.00 54.03 O ANISOU 2563 O CYS A 413 8025 5489 7016 -787 745 -214 O ATOM 2564 CB CYS A 413 183.998 13.861 511.104 1.00 52.91 C ANISOU 2564 CB CYS A 413 7858 5243 7004 -630 856 -335 C ATOM 2565 SG CYS A 413 182.450 13.887 510.173 0.64 62.40 S ANISOU 2565 SG CYS A 413 9321 6286 8103 -689 702 -311 S ATOM 2566 N ALA A 414 184.229 17.201 509.974 1.00 55.47 N ANISOU 2566 N ALA A 414 8519 5610 6948 -983 891 -323 N ATOM 2567 CA ALA A 414 183.574 18.501 510.052 1.00 59.26 C ANISOU 2567 CA ALA A 414 9133 6049 7334 -1061 788 -250 C ATOM 2568 C ALA A 414 182.065 18.399 509.823 1.00 57.17 C ANISOU 2568 C ALA A 414 9004 5663 7056 -1012 602 -180 C ATOM 2569 O ALA A 414 181.300 19.011 510.579 1.00 54.74 O ANISOU 2569 O ALA A 414 8675 5338 6785 -972 477 -96 O ATOM 2570 CB ALA A 414 184.205 19.481 509.058 1.00 60.82 C ANISOU 2570 CB ALA A 414 9513 6245 7351 -1231 902 -291 C ATOM 2571 N PRO A 415 181.581 17.660 508.813 1.00 59.64 N ANISOU 2571 N PRO A 415 9452 5894 7315 -1014 577 -217 N ATOM 2572 CA PRO A 415 180.122 17.562 508.628 1.00 60.31 C ANISOU 2572 CA PRO A 415 9638 5883 7395 -974 384 -149 C ATOM 2573 C PRO A 415 179.408 16.781 509.720 1.00 61.67 C ANISOU 2573 C PRO A 415 9621 6059 7751 -843 279 -94 C ATOM 2574 O PRO A 415 178.170 16.762 509.725 1.00 65.76 O ANISOU 2574 O PRO A 415 10182 6518 8286 -811 118 -31 O ATOM 2575 CB PRO A 415 179.982 16.856 507.271 1.00 65.40 C ANISOU 2575 CB PRO A 415 10462 6457 7929 -1028 401 -225 C ATOM 2576 CG PRO A 415 181.291 17.043 506.597 1.00 67.08 C ANISOU 2576 CG PRO A 415 10731 6719 8035 -1121 606 -317 C ATOM 2577 CD PRO A 415 182.293 17.006 507.699 1.00 66.30 C ANISOU 2577 CD PRO A 415 10385 6730 8076 -1069 719 -326 C ATOM 2578 N CYS A 416 180.133 16.138 510.638 1.00 62.22 N ANISOU 2578 N CYS A 416 9481 6202 7959 -769 364 -109 N ATOM 2579 CA CYS A 416 179.481 15.370 511.692 1.00 54.10 C ANISOU 2579 CA CYS A 416 8287 5173 7094 -652 274 -46 C ATOM 2580 C CYS A 416 178.771 16.254 512.708 1.00 50.66 C ANISOU 2580 C CYS A 416 7786 4770 6693 -618 166 54 C ATOM 2581 O CYS A 416 177.925 15.755 513.458 1.00 59.71 O ANISOU 2581 O CYS A 416 8832 5906 7949 -537 71 119 O ATOM 2582 CB CYS A 416 180.498 14.480 512.410 1.00 64.26 C ANISOU 2582 CB CYS A 416 9380 6529 8507 -572 389 -76 C ATOM 2583 SG CYS A 416 181.096 13.071 511.445 1.00 70.20 S ANISOU 2583 SG CYS A 416 10177 7216 9280 -552 506 -189 S ATOM 2584 N ILE A 417 179.090 17.541 512.757 1.00 38.40 N ANISOU 2584 N ILE A 417 6294 3249 5048 -681 187 63 N ATOM 2585 CA ILE A 417 178.495 18.472 513.704 1.00 41.11 C ANISOU 2585 CA ILE A 417 6593 3612 5413 -647 102 140 C ATOM 2586 C ILE A 417 177.867 19.619 512.922 1.00 46.37 C ANISOU 2586 C ILE A 417 7473 4200 5947 -711 30 164 C ATOM 2587 O ILE A 417 178.568 20.495 512.413 1.00 49.70 O ANISOU 2587 O ILE A 417 8017 4615 6252 -809 105 132 O ATOM 2588 CB ILE A 417 179.533 18.995 514.714 1.00 36.74 C ANISOU 2588 CB ILE A 417 5906 3168 4885 -655 194 128 C ATOM 2589 CG1 ILE A 417 180.369 17.844 515.278 1.00 36.98 C ANISOU 2589 CG1 ILE A 417 5742 3282 5027 -593 275 101 C ATOM 2590 CG2 ILE A 417 178.839 19.734 515.847 1.00 46.73 C ANISOU 2590 CG2 ILE A 417 7114 4453 6188 -600 108 200 C ATOM 2591 CD1 ILE A 417 179.580 16.874 516.130 1.00 47.65 C ANISOU 2591 CD1 ILE A 417 6963 4629 6512 -472 191 168 C ATOM 2592 N PRO A 418 176.543 19.643 512.796 1.00 34.18 N ANISOU 2592 N PRO A 418 5976 2592 4418 -658 -119 227 N ATOM 2593 CA PRO A 418 175.875 20.787 512.165 1.00 30.13 C ANISOU 2593 CA PRO A 418 5654 2004 3791 -688 -208 268 C ATOM 2594 C PRO A 418 176.030 22.049 513.003 1.00 42.54 C ANISOU 2594 C PRO A 418 7223 3587 5354 -678 -192 300 C ATOM 2595 O PRO A 418 176.477 22.027 514.151 1.00 59.06 O ANISOU 2595 O PRO A 418 9153 5757 7530 -643 -134 295 O ATOM 2596 CB PRO A 418 174.410 20.349 512.083 1.00 35.01 C ANISOU 2596 CB PRO A 418 6249 2583 4470 -608 -377 330 C ATOM 2597 CG PRO A 418 174.450 18.855 512.167 1.00 27.75 C ANISOU 2597 CG PRO A 418 5202 1690 3651 -589 -357 296 C ATOM 2598 CD PRO A 418 175.610 18.534 513.059 1.00 27.12 C ANISOU 2598 CD PRO A 418 4974 1689 3642 -577 -212 259 C ATOM 2599 N ASN A 419 175.637 23.174 512.399 1.00 47.15 N ANISOU 2599 N ASN A 419 8004 4084 5826 -709 -249 335 N ATOM 2600 CA ASN A 419 175.765 24.463 513.075 1.00 48.03 C ANISOU 2600 CA ASN A 419 8160 4173 5918 -708 -230 358 C ATOM 2601 C ASN A 419 174.826 24.562 514.272 1.00 48.32 C ANISOU 2601 C ASN A 419 8049 4234 6078 -569 -313 409 C ATOM 2602 O ASN A 419 175.195 25.120 515.313 1.00 63.38 O ANISOU 2602 O ASN A 419 9885 6178 8018 -557 -258 398 O ATOM 2603 CB ASN A 419 175.497 25.599 512.088 1.00 60.86 C ANISOU 2603 CB ASN A 419 10029 5699 7396 -752 -276 388 C ATOM 2604 CG ASN A 419 175.477 26.960 512.756 1.00 76.92 C ANISOU 2604 CG ASN A 419 12097 7713 9416 -727 -265 405 C ATOM 2605 OD1 ASN A 419 176.522 27.570 512.979 1.00 82.31 O ANISOU 2605 OD1 ASN A 419 12817 8407 10049 -832 -146 359 O ATOM 2606 ND2 ASN A 419 174.282 27.446 513.074 1.00 78.56 N ANISOU 2606 ND2 ASN A 419 12292 7886 9670 -592 -387 466 N ATOM 2607 N THR A 420 173.609 24.029 514.140 1.00 47.05 N ANISOU 2607 N THR A 420 7837 4059 5981 -472 -443 462 N ATOM 2608 CA THR A 420 172.658 24.068 515.248 1.00 54.49 C ANISOU 2608 CA THR A 420 8625 5037 7042 -341 -509 511 C ATOM 2609 C THR A 420 173.214 23.353 516.473 1.00 54.11 C ANISOU 2609 C THR A 420 8362 5101 7094 -323 -419 485 C ATOM 2610 O THR A 420 173.025 23.807 517.608 1.00 62.97 O ANISOU 2610 O THR A 420 9397 6264 8267 -258 -404 500 O ATOM 2611 CB THR A 420 171.329 23.444 514.819 1.00 56.02 C ANISOU 2611 CB THR A 420 8772 5219 7295 -265 -655 567 C ATOM 2612 OG1 THR A 420 170.887 24.049 513.597 1.00 56.80 O ANISOU 2612 OG1 THR A 420 9076 5223 7284 -286 -752 594 O ATOM 2613 CG2 THR A 420 170.268 23.652 515.890 1.00 53.38 C ANISOU 2613 CG2 THR A 420 8285 4921 7074 -129 -715 621 C ATOM 2614 N VAL A 421 173.917 22.239 516.260 1.00 44.28 N ANISOU 2614 N VAL A 421 7042 3907 5874 -375 -358 447 N ATOM 2615 CA VAL A 421 174.516 21.508 517.371 1.00 48.41 C ANISOU 2615 CA VAL A 421 7370 4534 6487 -350 -281 434 C ATOM 2616 C VAL A 421 175.594 22.349 518.046 1.00 46.20 C ANISOU 2616 C VAL A 421 7089 4305 6159 -401 -182 392 C ATOM 2617 O VAL A 421 175.698 22.376 519.280 1.00 54.23 O ANISOU 2617 O VAL A 421 7973 5402 7228 -354 -159 403 O ATOM 2618 CB VAL A 421 175.066 20.158 516.876 1.00 42.37 C ANISOU 2618 CB VAL A 421 6549 3790 5760 -382 -236 400 C ATOM 2619 CG1 VAL A 421 175.676 19.372 518.022 1.00 43.06 C ANISOU 2619 CG1 VAL A 421 6440 3979 5944 -338 -169 403 C ATOM 2620 CG2 VAL A 421 173.960 19.355 516.208 1.00 31.80 C ANISOU 2620 CG2 VAL A 421 5225 2393 4463 -353 -343 432 C ATOM 2621 N TRP A 422 176.409 23.054 517.253 1.00 35.44 N ANISOU 2621 N TRP A 422 5879 2902 4686 -511 -121 343 N ATOM 2622 CA TRP A 422 177.397 23.962 517.827 1.00 41.25 C ANISOU 2622 CA TRP A 422 6626 3679 5370 -588 -34 298 C ATOM 2623 C TRP A 422 176.727 25.036 518.675 1.00 48.17 C ANISOU 2623 C TRP A 422 7539 4521 6244 -532 -81 326 C ATOM 2624 O TRP A 422 177.185 25.339 519.785 1.00 52.96 O ANISOU 2624 O TRP A 422 8053 5205 6865 -535 -38 302 O ATOM 2625 CB TRP A 422 178.233 24.606 516.721 1.00 37.01 C ANISOU 2625 CB TRP A 422 6268 3085 4709 -731 39 250 C ATOM 2626 CG TRP A 422 179.258 23.695 516.112 1.00 46.19 C ANISOU 2626 CG TRP A 422 7369 4313 5867 -800 136 194 C ATOM 2627 CD1 TRP A 422 179.240 23.166 514.855 1.00 38.93 C ANISOU 2627 CD1 TRP A 422 6553 3341 4896 -837 145 179 C ATOM 2628 CD2 TRP A 422 180.455 23.211 516.734 1.00 55.20 C ANISOU 2628 CD2 TRP A 422 8330 5589 7055 -832 237 143 C ATOM 2629 NE1 TRP A 422 180.352 22.384 514.654 1.00 35.47 N ANISOU 2629 NE1 TRP A 422 6013 2988 4476 -883 263 114 N ATOM 2630 CE2 TRP A 422 181.113 22.393 515.793 1.00 50.13 C ANISOU 2630 CE2 TRP A 422 7685 4962 6399 -875 316 96 C ATOM 2631 CE3 TRP A 422 181.034 23.389 517.995 1.00 44.56 C ANISOU 2631 CE3 TRP A 422 6822 4354 5753 -825 265 131 C ATOM 2632 CZ2 TRP A 422 182.319 21.754 516.073 1.00 48.25 C ANISOU 2632 CZ2 TRP A 422 7275 4849 6208 -895 424 41 C ATOM 2633 CZ3 TRP A 422 182.232 22.754 518.271 1.00 43.08 C ANISOU 2633 CZ3 TRP A 422 6464 4298 5605 -854 355 83 C ATOM 2634 CH2 TRP A 422 182.861 21.947 517.314 1.00 45.19 C ANISOU 2634 CH2 TRP A 422 6718 4578 5875 -881 435 41 C ATOM 2635 N THR A 423 175.636 25.618 518.169 1.00 49.40 N ANISOU 2635 N THR A 423 7830 4562 6377 -474 -172 373 N ATOM 2636 CA THR A 423 174.896 26.609 518.944 1.00 51.75 C ANISOU 2636 CA THR A 423 8164 4815 6684 -392 -213 396 C ATOM 2637 C THR A 423 174.387 26.015 520.252 1.00 50.78 C ANISOU 2637 C THR A 423 7830 4798 6668 -281 -225 418 C ATOM 2638 O THR A 423 174.428 26.672 521.301 1.00 57.41 O ANISOU 2638 O THR A 423 8644 5664 7504 -255 -194 398 O ATOM 2639 CB THR A 423 173.734 27.163 518.118 1.00 52.28 C ANISOU 2639 CB THR A 423 8385 4752 6729 -319 -323 455 C ATOM 2640 OG1 THR A 423 174.232 27.699 516.885 1.00 43.22 O ANISOU 2640 OG1 THR A 423 7455 3505 5463 -429 -310 445 O ATOM 2641 CG2 THR A 423 173.008 28.261 518.882 1.00 63.57 C ANISOU 2641 CG2 THR A 423 9862 6119 8172 -217 -351 472 C ATOM 2642 N ILE A 424 173.919 24.765 520.213 1.00 40.79 N ANISOU 2642 N ILE A 424 6421 3590 5488 -225 -265 457 N ATOM 2643 CA ILE A 424 173.395 24.124 521.418 1.00 41.44 C ANISOU 2643 CA ILE A 424 6310 3770 5666 -130 -271 492 C ATOM 2644 C ILE A 424 174.503 23.938 522.449 1.00 42.48 C ANISOU 2644 C ILE A 424 6333 4017 5790 -175 -183 453 C ATOM 2645 O ILE A 424 174.334 24.260 523.631 1.00 43.21 O ANISOU 2645 O ILE A 424 6355 4172 5890 -126 -165 455 O ATOM 2646 CB ILE A 424 172.718 22.788 521.064 1.00 36.99 C ANISOU 2646 CB ILE A 424 5635 3226 5195 -87 -328 543 C ATOM 2647 CG1 ILE A 424 171.438 23.036 520.264 1.00 31.40 C ANISOU 2647 CG1 ILE A 424 4999 2431 4501 -30 -439 587 C ATOM 2648 CG2 ILE A 424 172.416 21.992 522.324 1.00 41.46 C ANISOU 2648 CG2 ILE A 424 6003 3899 5851 -18 -310 583 C ATOM 2649 CD1 ILE A 424 170.752 21.770 519.799 1.00 44.58 C ANISOU 2649 CD1 ILE A 424 6575 4111 6252 -16 -506 627 C ATOM 2650 N GLY A 425 175.654 23.415 522.017 1.00 41.21 N ANISOU 2650 N GLY A 425 6154 3895 5609 -266 -127 415 N ATOM 2651 CA GLY A 425 176.753 23.211 522.951 1.00 45.65 C ANISOU 2651 CA GLY A 425 6596 4583 6166 -304 -58 383 C ATOM 2652 C GLY A 425 177.253 24.512 523.551 1.00 40.72 C ANISOU 2652 C GLY A 425 6046 3970 5457 -368 -21 327 C ATOM 2653 O GLY A 425 177.454 24.618 524.768 1.00 45.92 O ANISOU 2653 O GLY A 425 6610 4727 6113 -348 -7 320 O ATOM 2654 N TYR A 426 177.463 25.520 522.700 1.00 29.08 N ANISOU 2654 N TYR A 426 4758 2389 3904 -455 -6 287 N ATOM 2655 CA TYR A 426 177.830 26.850 523.178 1.00 33.52 C ANISOU 2655 CA TYR A 426 5430 2922 4385 -527 27 231 C ATOM 2656 C TYR A 426 176.845 27.340 524.235 1.00 50.85 C ANISOU 2656 C TYR A 426 7618 5106 6598 -413 -9 250 C ATOM 2657 O TYR A 426 177.238 27.796 525.319 1.00 54.49 O ANISOU 2657 O TYR A 426 8043 5638 7023 -438 22 205 O ATOM 2658 CB TYR A 426 177.877 27.819 521.995 1.00 26.86 C ANISOU 2658 CB TYR A 426 4821 1923 3463 -613 36 212 C ATOM 2659 CG TYR A 426 179.083 28.727 521.968 1.00 27.48 C ANISOU 2659 CG TYR A 426 4990 2001 3450 -788 117 134 C ATOM 2660 CD1 TYR A 426 180.258 28.332 521.344 1.00 27.73 C ANISOU 2660 CD1 TYR A 426 4978 2101 3456 -919 189 96 C ATOM 2661 CD2 TYR A 426 179.042 29.985 522.553 1.00 28.25 C ANISOU 2661 CD2 TYR A 426 5217 2027 3491 -828 128 93 C ATOM 2662 CE1 TYR A 426 181.363 29.160 521.311 1.00 28.72 C ANISOU 2662 CE1 TYR A 426 5169 2240 3504 -1098 268 25 C ATOM 2663 CE2 TYR A 426 180.142 30.821 522.526 1.00 30.18 C ANISOU 2663 CE2 TYR A 426 5547 2266 3653 -1012 202 19 C ATOM 2664 CZ TYR A 426 181.299 30.403 521.904 1.00 29.75 C ANISOU 2664 CZ TYR A 426 5430 2295 3577 -1153 271 -13 C ATOM 2665 OH TYR A 426 182.397 31.232 521.874 1.00 45.76 O ANISOU 2665 OH TYR A 426 7526 4331 5529 -1355 349 -87 O ATOM 2666 N TRP A 427 175.548 27.224 523.939 1.00 57.54 N ANISOU 2666 N TRP A 427 8490 5875 7497 -287 -75 311 N ATOM 2667 CA TRP A 427 174.538 27.720 524.864 1.00 44.02 C ANISOU 2667 CA TRP A 427 6767 4151 5807 -167 -96 326 C ATOM 2668 C TRP A 427 174.517 26.933 526.166 1.00 35.54 C ANISOU 2668 C TRP A 427 5492 3236 4774 -112 -76 343 C ATOM 2669 O TRP A 427 174.193 27.500 527.212 1.00 34.04 O ANISOU 2669 O TRP A 427 5299 3075 4560 -63 -54 319 O ATOM 2670 CB TRP A 427 173.162 27.705 524.203 1.00 27.38 C ANISOU 2670 CB TRP A 427 4698 1946 3759 -42 -175 393 C ATOM 2671 CG TRP A 427 172.725 29.069 523.794 1.00 31.35 C ANISOU 2671 CG TRP A 427 5411 2290 4210 -15 -194 376 C ATOM 2672 CD1 TRP A 427 172.639 29.559 522.524 1.00 54.44 C ANISOU 2672 CD1 TRP A 427 8515 5077 7095 -47 -238 395 C ATOM 2673 CD2 TRP A 427 172.341 30.138 524.664 1.00 33.77 C ANISOU 2673 CD2 TRP A 427 5789 2548 4494 52 -165 337 C ATOM 2674 NE1 TRP A 427 172.210 30.864 522.549 1.00 62.48 N ANISOU 2674 NE1 TRP A 427 9711 5954 8074 5 -246 381 N ATOM 2675 CE2 TRP A 427 172.022 31.244 523.852 1.00 42.50 C ANISOU 2675 CE2 TRP A 427 7119 3471 5559 69 -197 339 C ATOM 2676 CE3 TRP A 427 172.230 30.266 526.052 1.00 35.17 C ANISOU 2676 CE3 TRP A 427 5874 2814 4674 103 -113 300 C ATOM 2677 CZ2 TRP A 427 171.599 32.460 524.381 1.00 39.07 C ANISOU 2677 CZ2 TRP A 427 6819 2925 5100 144 -175 302 C ATOM 2678 CZ3 TRP A 427 171.811 31.474 526.576 1.00 40.14 C ANISOU 2678 CZ3 TRP A 427 6636 3346 5270 168 -86 252 C ATOM 2679 CH2 TRP A 427 171.500 32.555 525.742 1.00 50.28 C ANISOU 2679 CH2 TRP A 427 8143 4433 6528 193 -116 251 C ATOM 2680 N LEU A 428 174.849 25.640 526.134 1.00 24.80 N ANISOU 2680 N LEU A 428 3979 1973 3470 -118 -81 385 N ATOM 2681 CA LEU A 428 174.964 24.882 527.377 1.00 39.70 C ANISOU 2681 CA LEU A 428 5693 4009 5383 -77 -62 413 C ATOM 2682 C LEU A 428 176.134 25.386 528.213 1.00 40.48 C ANISOU 2682 C LEU A 428 5783 4203 5393 -169 -15 343 C ATOM 2683 O LEU A 428 176.003 25.602 529.431 1.00 33.18 O ANISOU 2683 O LEU A 428 4812 3364 4433 -136 0 335 O ATOM 2684 CB LEU A 428 175.120 23.392 527.075 1.00 34.39 C ANISOU 2684 CB LEU A 428 4883 3390 4792 -62 -78 476 C ATOM 2685 CG LEU A 428 173.878 22.666 526.557 1.00 45.25 C ANISOU 2685 CG LEU A 428 6223 4706 6262 23 -131 550 C ATOM 2686 CD1 LEU A 428 174.180 21.196 526.314 1.00 48.93 C ANISOU 2686 CD1 LEU A 428 6576 5210 6804 20 -137 599 C ATOM 2687 CD2 LEU A 428 172.725 22.826 527.535 1.00 51.72 C ANISOU 2687 CD2 LEU A 428 6980 5560 7109 125 -137 592 C ATOM 2688 N CYS A 429 177.291 25.582 527.569 1.00 28.68 N ANISOU 2688 N CYS A 429 4332 2706 3859 -293 9 290 N ATOM 2689 CA CYS A 429 178.416 26.212 528.251 1.00 25.80 C ANISOU 2689 CA CYS A 429 3964 2429 3408 -405 45 212 C ATOM 2690 C CYS A 429 178.008 27.537 528.879 1.00 26.53 C ANISOU 2690 C CYS A 429 4197 2459 3423 -415 58 152 C ATOM 2691 O CYS A 429 178.539 27.917 529.929 1.00 44.10 O ANISOU 2691 O CYS A 429 6393 4784 5578 -466 73 99 O ATOM 2692 CB CYS A 429 179.577 26.422 527.279 1.00 27.62 C ANISOU 2692 CB CYS A 429 4241 2643 3609 -550 81 158 C ATOM 2693 SG CYS A 429 180.375 24.907 526.698 1.00 58.40 S ANISOU 2693 SG CYS A 429 7963 6639 7588 -545 91 199 S ATOM 2694 N TYR A 430 177.064 28.250 528.258 1.00 36.73 N ANISOU 2694 N TYR A 430 5646 3584 4724 -361 47 156 N ATOM 2695 CA TYR A 430 176.498 29.424 528.916 1.00 37.05 C ANISOU 2695 CA TYR A 430 5818 3549 4709 -327 63 104 C ATOM 2696 C TYR A 430 175.584 29.037 530.076 1.00 31.11 C ANISOU 2696 C TYR A 430 4954 2883 3983 -186 61 140 C ATOM 2697 O TYR A 430 175.536 29.748 531.086 1.00 36.10 O ANISOU 2697 O TYR A 430 5634 3539 4545 -183 93 77 O ATOM 2698 CB TYR A 430 175.739 30.282 527.905 1.00 42.17 C ANISOU 2698 CB TYR A 430 6664 3989 5368 -286 46 110 C ATOM 2699 CG TYR A 430 176.633 31.069 526.975 1.00 39.61 C ANISOU 2699 CG TYR A 430 6514 3556 4978 -445 69 58 C ATOM 2700 CD1 TYR A 430 177.943 31.364 527.327 1.00 42.26 C ANISOU 2700 CD1 TYR A 430 6845 3971 5242 -620 117 -20 C ATOM 2701 CD2 TYR A 430 176.166 31.522 525.749 1.00 48.04 C ANISOU 2701 CD2 TYR A 430 7749 4451 6052 -430 42 93 C ATOM 2702 CE1 TYR A 430 178.765 32.086 526.483 1.00 46.04 C ANISOU 2702 CE1 TYR A 430 7476 4356 5660 -785 152 -67 C ATOM 2703 CE2 TYR A 430 176.980 32.246 524.897 1.00 56.28 C ANISOU 2703 CE2 TYR A 430 8967 5394 7024 -588 75 54 C ATOM 2704 CZ TYR A 430 178.278 32.524 525.270 1.00 53.08 C ANISOU 2704 CZ TYR A 430 8549 5066 6553 -770 137 -27 C ATOM 2705 OH TYR A 430 179.091 33.244 524.426 1.00 56.04 O ANISOU 2705 OH TYR A 430 9090 5345 6856 -945 183 -64 O ATOM 2706 N ILE A 431 174.866 27.915 529.956 1.00 29.62 N ANISOU 2706 N ILE A 431 4624 2742 3887 -80 30 236 N ATOM 2707 CA ILE A 431 173.903 27.516 530.980 1.00 38.94 C ANISOU 2707 CA ILE A 431 5696 4002 5096 47 40 282 C ATOM 2708 C ILE A 431 174.612 27.193 532.287 1.00 46.21 C ANISOU 2708 C ILE A 431 6518 5096 5944 4 67 264 C ATOM 2709 O ILE A 431 174.027 27.334 533.372 1.00 53.33 O ANISOU 2709 O ILE A 431 7391 6062 6809 75 100 261 O ATOM 2710 CB ILE A 431 173.050 26.330 530.481 1.00 38.56 C ANISOU 2710 CB ILE A 431 5519 3963 5168 137 0 391 C ATOM 2711 CG1 ILE A 431 172.152 26.766 529.324 1.00 34.53 C ANISOU 2711 CG1 ILE A 431 5109 3295 4716 196 -43 408 C ATOM 2712 CG2 ILE A 431 172.193 25.746 531.597 1.00 26.09 C ANISOU 2712 CG2 ILE A 431 3803 2491 3617 240 24 449 C ATOM 2713 CD1 ILE A 431 171.361 28.019 529.607 1.00 27.00 C ANISOU 2713 CD1 ILE A 431 4274 2247 3736 281 -24 363 C ATOM 2714 N ASN A 432 175.878 26.768 532.213 1.00 48.61 N ANISOU 2714 N ASN A 432 6764 5486 6219 -109 56 251 N ATOM 2715 CA ASN A 432 176.667 26.578 533.431 1.00 46.20 C ANISOU 2715 CA ASN A 432 6372 5353 5829 -158 62 231 C ATOM 2716 C ASN A 432 176.559 27.786 534.358 1.00 43.67 C ANISOU 2716 C ASN A 432 6172 5030 5391 -183 98 131 C ATOM 2717 O ASN A 432 176.318 27.645 535.563 1.00 47.11 O ANISOU 2717 O ASN A 432 6555 5582 5762 -140 114 137 O ATOM 2718 CB ASN A 432 178.130 26.315 533.076 1.00 46.78 C ANISOU 2718 CB ASN A 432 6389 5502 5883 -288 43 203 C ATOM 2719 CG ASN A 432 178.984 26.046 534.301 1.00 36.65 C ANISOU 2719 CG ASN A 432 4995 4415 4514 -334 26 193 C ATOM 2720 OD1 ASN A 432 178.502 25.519 535.304 1.00 40.02 O ANISOU 2720 OD1 ASN A 432 5347 4940 4920 -250 21 253 O ATOM 2721 ND2 ASN A 432 180.258 26.413 534.227 1.00 29.37 N ANISOU 2721 ND2 ASN A 432 4060 3561 3537 -474 16 120 N ATOM 2722 N SER A 433 176.722 28.989 533.801 1.00 40.90 N ANISOU 2722 N SER A 433 5999 4537 5004 -255 116 37 N ATOM 2723 CA SER A 433 176.618 30.202 534.605 1.00 35.11 C ANISOU 2723 CA SER A 433 5412 3766 4162 -282 155 -72 C ATOM 2724 C SER A 433 175.208 30.401 535.146 1.00 53.14 C ANISOU 2724 C SER A 433 7723 6002 6465 -112 194 -54 C ATOM 2725 O SER A 433 175.030 31.016 536.204 1.00 51.41 O ANISOU 2725 O SER A 433 7566 5818 6150 -100 238 -129 O ATOM 2726 CB SER A 433 177.043 31.414 533.776 1.00 33.09 C ANISOU 2726 CB SER A 433 5361 3333 3879 -394 169 -164 C ATOM 2727 OG SER A 433 178.398 31.310 533.379 1.00 43.40 O ANISOU 2727 OG SER A 433 6631 4704 5156 -570 151 -194 O ATOM 2728 N THR A 434 174.198 29.893 534.439 1.00 62.92 N ANISOU 2728 N THR A 434 8911 7170 7825 16 181 38 N ATOM 2729 CA THR A 434 172.823 30.049 534.899 1.00 46.97 C ANISOU 2729 CA THR A 434 6884 5120 5841 182 221 60 C ATOM 2730 C THR A 434 172.546 29.166 536.110 1.00 44.52 C ANISOU 2730 C THR A 434 6413 5001 5503 233 250 114 C ATOM 2731 O THR A 434 171.976 29.624 537.107 1.00 41.04 O ANISOU 2731 O THR A 434 6000 4597 4995 300 315 68 O ATOM 2732 CB THR A 434 171.848 29.726 533.766 1.00 40.23 C ANISOU 2732 CB THR A 434 6003 4155 5127 289 184 145 C ATOM 2733 OG1 THR A 434 172.130 30.564 532.638 1.00 50.26 O ANISOU 2733 OG1 THR A 434 7444 5248 6404 239 154 105 O ATOM 2734 CG2 THR A 434 170.412 29.954 534.213 1.00 30.61 C ANISOU 2734 CG2 THR A 434 4755 2916 3958 464 226 163 C ATOM 2735 N ILE A 435 172.947 27.891 536.044 1.00 52.76 N ANISOU 2735 N ILE A 435 7295 6161 6590 204 208 214 N ATOM 2736 CA ILE A 435 172.675 26.962 537.138 1.00 51.93 C ANISOU 2736 CA ILE A 435 7046 6225 6459 250 231 290 C ATOM 2737 C ILE A 435 173.725 27.019 538.237 1.00 52.35 C ANISOU 2737 C ILE A 435 7098 6430 6361 153 230 243 C ATOM 2738 O ILE A 435 173.569 26.342 539.263 1.00 50.29 O ANISOU 2738 O ILE A 435 6744 6317 6046 184 249 305 O ATOM 2739 CB ILE A 435 172.559 25.512 536.625 1.00 45.95 C ANISOU 2739 CB ILE A 435 6131 5508 5822 272 187 428 C ATOM 2740 CG1 ILE A 435 173.890 25.045 536.032 1.00 42.20 C ANISOU 2740 CG1 ILE A 435 5629 5053 5351 163 125 433 C ATOM 2741 CG2 ILE A 435 171.439 25.396 535.602 1.00 47.05 C ANISOU 2741 CG2 ILE A 435 6259 5518 6102 360 176 475 C ATOM 2742 CD1 ILE A 435 173.885 23.596 535.598 1.00 51.98 C ANISOU 2742 CD1 ILE A 435 6729 6320 6700 187 88 558 C ATOM 2743 N ASN A 436 174.790 27.802 538.063 1.00 61.12 N ANISOU 2743 N ASN A 436 8310 7517 7396 28 205 139 N ATOM 2744 CA ASN A 436 175.832 27.866 539.086 1.00 61.25 C ANISOU 2744 CA ASN A 436 8312 7694 7265 -78 185 89 C ATOM 2745 C ASN A 436 175.330 28.404 540.425 1.00 60.30 C ANISOU 2745 C ASN A 436 8257 7649 7005 -43 246 28 C ATOM 2746 O ASN A 436 175.605 27.770 541.456 1.00 57.03 O ANISOU 2746 O ASN A 436 7756 7417 6498 -51 232 77 O ATOM 2747 CB ASN A 436 177.020 28.681 538.562 1.00 64.48 C ANISOU 2747 CB ASN A 436 8813 8057 7630 -238 151 -21 C ATOM 2748 CG ASN A 436 178.347 27.973 538.762 1.00 57.82 C ANISOU 2748 CG ASN A 436 7833 7384 6752 -343 80 9 C ATOM 2749 OD1 ASN A 436 178.470 27.089 539.609 1.00 54.34 O ANISOU 2749 OD1 ASN A 436 7264 7109 6272 -304 51 91 O ATOM 2750 ND2 ASN A 436 179.348 28.359 537.980 1.00 55.13 N ANISOU 2750 ND2 ASN A 436 7516 7005 6426 -474 53 -51 N ATOM 2751 N PRO A 437 174.612 29.536 540.495 1.00 61.93 N ANISOU 2751 N PRO A 437 8620 7726 7185 2 316 -76 N ATOM 2752 CA PRO A 437 174.184 30.027 541.819 1.00 52.93 C ANISOU 2752 CA PRO A 437 7548 6666 5897 35 389 -149 C ATOM 2753 C PRO A 437 173.226 29.097 542.542 1.00 51.40 C ANISOU 2753 C PRO A 437 7224 6592 5715 162 440 -34 C ATOM 2754 O PRO A 437 173.171 29.123 543.778 1.00 37.17 O ANISOU 2754 O PRO A 437 5436 4927 3761 160 485 -61 O ATOM 2755 CB PRO A 437 173.519 31.374 541.495 1.00 42.22 C ANISOU 2755 CB PRO A 437 6385 5104 4553 88 459 -275 C ATOM 2756 CG PRO A 437 174.080 31.772 540.178 1.00 40.54 C ANISOU 2756 CG PRO A 437 6241 4731 4433 11 401 -293 C ATOM 2757 CD PRO A 437 174.253 30.490 539.432 1.00 51.47 C ANISOU 2757 CD PRO A 437 7438 6175 5941 20 333 -142 C ATOM 2758 N ALA A 438 172.468 28.274 541.815 1.00 59.30 N ANISOU 2758 N ALA A 438 8103 7547 6881 260 438 94 N ATOM 2759 CA ALA A 438 171.532 27.357 542.454 1.00 51.53 C ANISOU 2759 CA ALA A 438 6989 6671 5919 361 494 211 C ATOM 2760 C ALA A 438 172.224 26.190 543.146 1.00 59.38 C ANISOU 2760 C ALA A 438 7866 7851 6846 303 443 324 C ATOM 2761 O ALA A 438 171.569 25.469 543.907 1.00 51.13 O ANISOU 2761 O ALA A 438 6738 6913 5776 362 498 420 O ATOM 2762 CB ALA A 438 170.534 26.826 541.424 1.00 46.58 C ANISOU 2762 CB ALA A 438 6266 5937 5495 462 494 308 C ATOM 2763 N CYS A 439 173.519 25.989 542.907 1.00 67.91 N ANISOU 2763 N CYS A 439 8934 8972 7897 193 344 321 N ATOM 2764 CA CYS A 439 174.234 24.867 543.499 1.00 70.66 C ANISOU 2764 CA CYS A 439 9167 9489 8194 157 280 438 C ATOM 2765 C CYS A 439 174.793 25.167 544.882 1.00 80.08 C ANISOU 2765 C CYS A 439 10409 10857 9160 95 276 387 C ATOM 2766 O CYS A 439 175.131 24.227 545.610 1.00 90.33 O ANISOU 2766 O CYS A 439 11620 12310 10392 95 236 504 O ATOM 2767 CB CYS A 439 175.380 24.424 542.587 1.00 74.10 C ANISOU 2767 CB CYS A 439 9538 9902 8714 85 175 464 C ATOM 2768 SG CYS A 439 174.855 23.817 540.972 1.00 67.74 S ANISOU 2768 SG CYS A 439 8671 8914 8151 145 165 539 S ATOM 2769 N TYR A 440 174.906 26.439 545.263 1.00 77.74 N ANISOU 2769 N TYR A 440 10261 10536 8739 42 312 219 N ATOM 2770 CA TYR A 440 175.465 26.775 546.567 1.00 64.66 C ANISOU 2770 CA TYR A 440 8668 9051 6850 -35 299 153 C ATOM 2771 C TYR A 440 174.622 27.818 547.286 1.00 68.86 C ANISOU 2771 C TYR A 440 9355 9547 7263 2 423 18 C ATOM 2772 O TYR A 440 174.500 27.786 548.516 1.00 97.26 O ANISOU 2772 O TYR A 440 12988 13294 10672 -3 463 9 O ATOM 2773 CB TYR A 440 176.913 27.260 546.422 1.00 65.37 C ANISOU 2773 CB TYR A 440 8784 9185 6870 -191 187 57 C ATOM 2774 CG TYR A 440 177.124 28.425 545.476 1.00 66.65 C ANISOU 2774 CG TYR A 440 9068 9158 7100 -260 199 -94 C ATOM 2775 CD1 TYR A 440 177.037 29.738 545.925 1.00 65.87 C ANISOU 2775 CD1 TYR A 440 9159 8996 6873 -320 255 -275 C ATOM 2776 CD2 TYR A 440 177.440 28.211 544.140 1.00 59.84 C ANISOU 2776 CD2 TYR A 440 8147 8172 6418 -271 158 -56 C ATOM 2777 CE1 TYR A 440 177.241 30.803 545.065 1.00 59.98 C ANISOU 2777 CE1 TYR A 440 8545 8058 6186 -388 267 -402 C ATOM 2778 CE2 TYR A 440 177.646 29.269 543.275 1.00 52.95 C ANISOU 2778 CE2 TYR A 440 7401 7124 5593 -342 171 -180 C ATOM 2779 CZ TYR A 440 177.546 30.563 543.742 1.00 53.52 C ANISOU 2779 CZ TYR A 440 7666 7126 5544 -401 224 -347 C ATOM 2780 OH TYR A 440 177.749 31.621 542.886 1.00 48.05 O ANISOU 2780 OH TYR A 440 7120 6239 4897 -476 239 -460 O ATOM 2781 N ALA A 441 174.028 28.737 546.525 1.00 60.82 N ANISOU 2781 N ALA A 441 8436 8328 6346 47 488 -84 N ATOM 2782 CA ALA A 441 173.268 29.823 547.134 1.00 66.76 C ANISOU 2782 CA ALA A 441 9347 9018 6998 97 611 -230 C ATOM 2783 C ALA A 441 171.929 29.328 547.666 1.00 68.27 C ANISOU 2783 C ALA A 441 9470 9259 7211 250 736 -146 C ATOM 2784 O ALA A 441 171.551 29.630 548.804 1.00 79.77 O ANISOU 2784 O ALA A 441 10998 10814 8496 271 831 -209 O ATOM 2785 CB ALA A 441 173.063 30.953 546.125 1.00 76.12 C ANISOU 2785 CB ALA A 441 10666 9959 8296 113 635 -352 C ATOM 2786 N LEU A 442 171.202 28.556 546.862 1.00 66.86 N ANISOU 2786 N LEU A 442 9149 9020 7234 348 743 -9 N ATOM 2787 CA LEU A 442 169.886 28.061 547.243 1.00 76.13 C ANISOU 2787 CA LEU A 442 10231 10237 8457 481 863 76 C ATOM 2788 C LEU A 442 169.945 26.894 548.223 1.00 91.85 C ANISOU 2788 C LEU A 442 12117 12439 10343 456 869 221 C ATOM 2789 O LEU A 442 168.898 26.317 548.536 1.00 92.88 O ANISOU 2789 O LEU A 442 12152 12621 10518 543 970 316 O ATOM 2790 CB LEU A 442 169.101 27.647 545.996 1.00 71.38 C ANISOU 2790 CB LEU A 442 9512 9498 8109 574 852 169 C ATOM 2791 CG LEU A 442 168.835 28.760 544.980 1.00 69.90 C ANISOU 2791 CG LEU A 442 9430 9095 8036 626 850 53 C ATOM 2792 CD1 LEU A 442 167.972 28.254 543.835 1.00 73.98 C ANISOU 2792 CD1 LEU A 442 9817 9508 8783 720 829 159 C ATOM 2793 CD2 LEU A 442 168.191 29.960 545.656 1.00 62.16 C ANISOU 2793 CD2 LEU A 442 8590 8068 6959 709 981 -104 C ATOM 2794 N CYS A 443 171.134 26.533 548.708 1.00 99.53 N ANISOU 2794 N CYS A 443 13101 13536 11178 340 762 247 N ATOM 2795 CA CYS A 443 171.287 25.448 549.666 1.00 99.39 C ANISOU 2795 CA CYS A 443 13006 13714 11043 318 751 396 C ATOM 2796 C CYS A 443 171.923 25.893 550.976 1.00 97.69 C ANISOU 2796 C CYS A 443 12911 13667 10541 236 747 310 C ATOM 2797 O CYS A 443 172.176 25.046 551.841 1.00 99.88 O ANISOU 2797 O CYS A 443 13146 14119 10686 209 719 435 O ATOM 2798 CB CYS A 443 172.118 24.311 549.055 1.00105.07 C ANISOU 2798 CB CYS A 443 13598 14451 11873 276 605 552 C ATOM 2799 SG CYS A 443 171.440 23.639 547.521 1.00110.54 S ANISOU 2799 SG CYS A 443 14160 14958 12884 353 596 656 S ATOM 2800 N ASN A 444 172.184 27.185 551.149 1.00 83.92 N ANISOU 2800 N ASN A 444 11326 11871 8689 190 769 104 N ATOM 2801 CA ASN A 444 172.792 27.718 552.360 1.00 82.76 C ANISOU 2801 CA ASN A 444 11313 11874 8257 94 759 -7 C ATOM 2802 C ASN A 444 171.780 28.596 553.084 1.00 76.68 C ANISOU 2802 C ASN A 444 10680 11083 7371 165 945 -148 C ATOM 2803 O ASN A 444 171.144 29.454 552.463 1.00 74.68 O ANISOU 2803 O ASN A 444 10490 10644 7240 240 1031 -265 O ATOM 2804 CB ASN A 444 174.055 28.516 552.031 1.00 81.04 C ANISOU 2804 CB ASN A 444 11182 11618 7992 -48 627 -149 C ATOM 2805 CG ASN A 444 174.802 28.965 553.270 1.00 77.40 C ANISOU 2805 CG ASN A 444 10843 11334 7230 -172 583 -256 C ATOM 2806 OD1 ASN A 444 174.528 30.029 553.823 1.00 77.72 O ANISOU 2806 OD1 ASN A 444 11062 11339 7127 -194 676 -443 O ATOM 2807 ND2 ASN A 444 175.756 28.153 553.712 1.00 80.16 N ANISOU 2807 ND2 ASN A 444 11101 11875 7481 -251 437 -141 N ATOM 2808 N ALA A 445 171.639 28.382 554.394 1.00 69.56 N ANISOU 2808 N ALA A 445 9829 10373 6227 147 1009 -136 N ATOM 2809 CA ALA A 445 170.626 29.103 555.160 1.00 67.24 C ANISOU 2809 CA ALA A 445 9654 10080 5812 226 1210 -264 C ATOM 2810 C ALA A 445 170.933 30.593 555.233 1.00 68.04 C ANISOU 2810 C ALA A 445 9971 10066 5817 177 1235 -529 C ATOM 2811 O ALA A 445 170.021 31.426 555.141 1.00 74.76 O ANISOU 2811 O ALA A 445 10906 10780 6718 288 1393 -659 O ATOM 2812 CB ALA A 445 170.508 28.509 556.563 1.00 53.70 C ANISOU 2812 CB ALA A 445 7962 8609 3832 198 1270 -188 C ATOM 2813 N THR A 446 172.208 30.951 555.404 1.00 58.02 N ANISOU 2813 N THR A 446 8790 8844 4411 13 1081 -613 N ATOM 2814 CA THR A 446 172.573 32.362 555.468 1.00 63.56 C ANISOU 2814 CA THR A 446 9710 9422 5017 -64 1096 -868 C ATOM 2815 C THR A 446 172.303 33.058 554.140 1.00 64.94 C ANISOU 2815 C THR A 446 9904 9316 5456 0 1110 -934 C ATOM 2816 O THR A 446 171.869 34.217 554.115 1.00 63.56 O ANISOU 2816 O THR A 446 9907 8971 5271 44 1220 -1122 O ATOM 2817 CB THR A 446 174.043 32.509 555.863 1.00 65.04 C ANISOU 2817 CB THR A 446 9957 9736 5020 -277 910 -929 C ATOM 2818 OG1 THR A 446 174.352 31.579 556.908 1.00 70.02 O ANISOU 2818 OG1 THR A 446 10520 10639 5443 -321 852 -799 O ATOM 2819 CG2 THR A 446 174.319 33.919 556.361 1.00 63.92 C ANISOU 2819 CG2 THR A 446 10076 9517 4695 -379 953 -1206 C ATOM 2820 N PHE A 447 172.546 32.365 553.025 1.00 64.00 N ANISOU 2820 N PHE A 447 9614 9137 5568 12 1003 -779 N ATOM 2821 CA PHE A 447 172.212 32.924 551.719 1.00 59.10 C ANISOU 2821 CA PHE A 447 9005 8257 5193 82 1014 -814 C ATOM 2822 C PHE A 447 170.707 33.093 551.560 1.00 60.13 C ANISOU 2822 C PHE A 447 9118 8279 5450 293 1189 -808 C ATOM 2823 O PHE A 447 170.250 34.060 550.941 1.00 70.61 O ANISOU 2823 O PHE A 447 10556 9387 6887 371 1250 -923 O ATOM 2824 CB PHE A 447 172.770 32.040 550.604 1.00 61.70 C ANISOU 2824 CB PHE A 447 9151 8568 5722 49 869 -645 C ATOM 2825 CG PHE A 447 174.172 32.389 550.193 1.00 64.22 C ANISOU 2825 CG PHE A 447 9516 8874 6013 -137 716 -711 C ATOM 2826 CD1 PHE A 447 174.435 33.567 549.512 1.00 63.00 C ANISOU 2826 CD1 PHE A 447 9523 8507 5909 -196 717 -869 C ATOM 2827 CD2 PHE A 447 175.224 31.531 550.468 1.00 61.44 C ANISOU 2827 CD2 PHE A 447 9039 8717 5588 -252 573 -609 C ATOM 2828 CE1 PHE A 447 175.723 33.889 549.125 1.00 55.84 C ANISOU 2828 CE1 PHE A 447 8645 7594 4977 -386 588 -929 C ATOM 2829 CE2 PHE A 447 176.514 31.847 550.082 1.00 58.92 C ANISOU 2829 CE2 PHE A 447 8730 8403 5252 -424 439 -671 C ATOM 2830 CZ PHE A 447 176.763 33.027 549.410 1.00 52.06 C ANISOU 2830 CZ PHE A 447 8017 7332 4431 -501 451 -834 C ATOM 2831 N LYS A 448 169.920 32.163 552.106 1.00 55.85 N ANISOU 2831 N LYS A 448 8433 7888 4899 388 1272 -670 N ATOM 2832 CA LYS A 448 168.468 32.285 552.027 1.00 67.32 C ANISOU 2832 CA LYS A 448 9837 9271 6472 584 1445 -663 C ATOM 2833 C LYS A 448 167.976 33.492 552.816 1.00 84.35 C ANISOU 2833 C LYS A 448 12198 11374 8478 646 1609 -882 C ATOM 2834 O LYS A 448 167.197 34.307 552.305 1.00 99.87 O ANISOU 2834 O LYS A 448 14221 13149 10577 789 1703 -976 O ATOM 2835 CB LYS A 448 167.803 31.005 552.535 1.00 74.75 C ANISOU 2835 CB LYS A 448 10583 10404 7416 638 1506 -469 C ATOM 2836 CG LYS A 448 168.093 29.769 551.701 1.00 71.53 C ANISOU 2836 CG LYS A 448 9975 10018 7186 605 1368 -251 C ATOM 2837 CD LYS A 448 167.515 28.523 552.353 1.00 75.97 C ANISOU 2837 CD LYS A 448 10380 10765 7719 632 1432 -64 C ATOM 2838 CE LYS A 448 167.892 27.269 551.584 1.00 78.11 C ANISOU 2838 CE LYS A 448 10479 11045 8155 590 1291 144 C ATOM 2839 NZ LYS A 448 167.386 27.303 550.184 1.00 79.32 N ANISOU 2839 NZ LYS A 448 10539 11008 8591 669 1260 171 N ATOM 2840 N LYS A 449 168.425 33.621 554.068 1.00 80.21 N ANISOU 2840 N LYS A 449 11793 11013 7669 547 1641 -968 N ATOM 2841 CA LYS A 449 168.014 34.759 554.885 1.00 84.40 C ANISOU 2841 CA LYS A 449 12542 11496 8032 595 1803 -1194 C ATOM 2842 C LYS A 449 168.477 36.074 554.271 1.00 82.06 C ANISOU 2842 C LYS A 449 12456 10943 7780 559 1762 -1391 C ATOM 2843 O LYS A 449 167.758 37.079 554.322 1.00 83.87 O ANISOU 2843 O LYS A 449 12830 11008 8030 689 1909 -1551 O ATOM 2844 CB LYS A 449 168.559 34.613 556.306 1.00 99.20 C ANISOU 2844 CB LYS A 449 14520 13604 9569 463 1816 -1249 C ATOM 2845 CG LYS A 449 168.173 35.757 557.231 1.00108.19 C ANISOU 2845 CG LYS A 449 15903 14703 10502 499 1991 -1499 C ATOM 2846 CD LYS A 449 168.891 35.667 558.566 1.00112.99 C ANISOU 2846 CD LYS A 449 16640 15540 10751 333 1966 -1565 C ATOM 2847 CE LYS A 449 168.505 36.825 559.473 1.00122.45 C ANISOU 2847 CE LYS A 449 18102 16688 11734 365 2149 -1834 C ATOM 2848 NZ LYS A 449 168.787 38.143 558.839 1.00123.89 N ANISOU 2848 NZ LYS A 449 18488 16582 12003 352 2132 -2049 N ATOM 2849 N THR A 450 169.675 36.087 553.680 1.00 81.28 N ANISOU 2849 N THR A 450 12379 10803 7700 384 1569 -1378 N ATOM 2850 CA THR A 450 170.169 37.312 553.062 1.00 69.56 C ANISOU 2850 CA THR A 450 11102 9071 6258 321 1529 -1553 C ATOM 2851 C THR A 450 169.367 37.661 551.813 1.00 61.10 C ANISOU 2851 C THR A 450 9996 7747 5473 497 1566 -1516 C ATOM 2852 O THR A 450 169.081 38.838 551.564 1.00 56.51 O ANISOU 2852 O THR A 450 9616 6931 4926 563 1640 -1678 O ATOM 2853 CB THR A 450 171.653 37.176 552.727 1.00 64.35 C ANISOU 2853 CB THR A 450 10445 8454 5552 80 1322 -1538 C ATOM 2854 OG1 THR A 450 172.334 36.546 553.820 1.00 62.52 O ANISOU 2854 OG1 THR A 450 10173 8501 5080 -58 1257 -1509 O ATOM 2855 CG2 THR A 450 172.265 38.547 552.493 1.00 56.61 C ANISOU 2855 CG2 THR A 450 9729 7257 4525 -41 1304 -1758 C ATOM 2856 N PHE A 451 168.994 36.654 551.018 1.00 53.03 N ANISOU 2856 N PHE A 451 8729 6763 4655 576 1511 -1303 N ATOM 2857 CA PHE A 451 168.138 36.897 549.860 1.00 52.10 C ANISOU 2857 CA PHE A 451 8559 6434 4801 752 1537 -1252 C ATOM 2858 C PHE A 451 166.796 37.475 550.291 1.00 70.06 C ANISOU 2858 C PHE A 451 10874 8643 7101 981 1738 -1339 C ATOM 2859 O PHE A 451 166.343 38.493 549.754 1.00 79.30 O ANISOU 2859 O PHE A 451 12183 9572 8376 1103 1789 -1444 O ATOM 2860 CB PHE A 451 167.930 35.602 549.072 1.00 55.16 C ANISOU 2860 CB PHE A 451 8671 6909 5376 783 1446 -1013 C ATOM 2861 CG PHE A 451 169.153 35.124 548.341 1.00 61.33 C ANISOU 2861 CG PHE A 451 9408 7700 6193 600 1257 -930 C ATOM 2862 CD1 PHE A 451 170.194 35.990 548.052 1.00 65.44 C ANISOU 2862 CD1 PHE A 451 10117 8098 6651 445 1176 -1059 C ATOM 2863 CD2 PHE A 451 169.258 33.802 547.937 1.00 61.17 C ANISOU 2863 CD2 PHE A 451 9158 7810 6275 581 1168 -727 C ATOM 2864 CE1 PHE A 451 171.318 35.545 547.377 1.00 55.00 C ANISOU 2864 CE1 PHE A 451 8732 6799 5366 279 1017 -986 C ATOM 2865 CE2 PHE A 451 170.378 33.353 547.264 1.00 62.60 C ANISOU 2865 CE2 PHE A 451 9291 8001 6493 431 1009 -659 C ATOM 2866 CZ PHE A 451 171.409 34.226 546.984 1.00 60.00 C ANISOU 2866 CZ PHE A 451 9129 7566 6101 282 936 -788 C ATOM 2867 N LYS A 452 166.146 36.830 551.264 1.00 62.87 N ANISOU 2867 N LYS A 452 9844 7947 6096 1048 1859 -1292 N ATOM 2868 CA LYS A 452 164.880 37.343 551.781 1.00 70.31 C ANISOU 2868 CA LYS A 452 10805 8861 7049 1265 2072 -1382 C ATOM 2869 C LYS A 452 165.031 38.772 552.288 1.00 74.78 C ANISOU 2869 C LYS A 452 11681 9259 7473 1278 2168 -1643 C ATOM 2870 O LYS A 452 164.143 39.609 552.086 1.00 74.51 O ANISOU 2870 O LYS A 452 11721 9046 7544 1483 2296 -1743 O ATOM 2871 CB LYS A 452 164.364 36.432 552.894 1.00 74.13 C ANISOU 2871 CB LYS A 452 11140 9626 7399 1282 2194 -1303 C ATOM 2872 CG LYS A 452 163.092 36.923 553.562 1.00 88.39 C ANISOU 2872 CG LYS A 452 12953 11442 9189 1495 2441 -1406 C ATOM 2873 CD LYS A 452 163.016 36.451 555.004 1.00 97.85 C ANISOU 2873 CD LYS A 452 14154 12905 10121 1434 2573 -1421 C ATOM 2874 CE LYS A 452 164.179 37.000 555.818 1.00 95.12 C ANISOU 2874 CE LYS A 452 14075 12588 9480 1237 2518 -1583 C ATOM 2875 NZ LYS A 452 164.129 36.561 557.240 1.00 81.50 N ANISOU 2875 NZ LYS A 452 12374 11127 7466 1173 2637 -1597 N ATOM 2876 N HIS A 453 166.155 39.070 552.943 1.00 79.20 N ANISOU 2876 N HIS A 453 12426 9870 7797 1062 2104 -1758 N ATOM 2877 CA HIS A 453 166.396 40.426 553.422 1.00 78.57 C ANISOU 2877 CA HIS A 453 12665 9619 7571 1037 2183 -2019 C ATOM 2878 C HIS A 453 166.602 41.402 552.270 1.00 73.01 C ANISOU 2878 C HIS A 453 12115 8583 7041 1060 2112 -2086 C ATOM 2879 O HIS A 453 166.290 42.591 552.403 1.00 71.20 O ANISOU 2879 O HIS A 453 12128 8133 6791 1152 2223 -2279 O ATOM 2880 CB HIS A 453 167.608 40.439 554.354 1.00 73.77 C ANISOU 2880 CB HIS A 453 12199 9164 6667 770 2103 -2116 C ATOM 2881 CG HIS A 453 167.886 41.775 554.967 1.00 72.47 C ANISOU 2881 CG HIS A 453 12373 8843 6321 714 2185 -2398 C ATOM 2882 ND1 HIS A 453 169.161 42.202 555.274 1.00 79.78 N ANISOU 2882 ND1 HIS A 453 13482 9774 7057 444 2058 -2520 N ATOM 2883 CD2 HIS A 453 167.055 42.778 555.336 1.00 79.43 C ANISOU 2883 CD2 HIS A 453 13445 9553 7182 890 2383 -2588 C ATOM 2884 CE1 HIS A 453 169.103 43.411 555.802 1.00 88.31 C ANISOU 2884 CE1 HIS A 453 14865 10684 8003 442 2172 -2777 C ATOM 2885 NE2 HIS A 453 167.837 43.783 555.852 1.00 83.18 N ANISOU 2885 NE2 HIS A 453 14234 9919 7454 719 2374 -2824 N ATOM 2886 N LEU A 454 167.118 40.925 551.135 1.00 71.81 N ANISOU 2886 N LEU A 454 11843 8386 7058 981 1935 -1928 N ATOM 2887 CA LEU A 454 167.356 41.810 550.001 1.00 78.23 C ANISOU 2887 CA LEU A 454 12811 8891 8024 984 1863 -1973 C ATOM 2888 C LEU A 454 166.090 42.073 549.196 1.00 75.70 C ANISOU 2888 C LEU A 454 12422 8391 7949 1274 1939 -1913 C ATOM 2889 O LEU A 454 165.932 43.169 548.646 1.00 73.84 O ANISOU 2889 O LEU A 454 12398 7865 7794 1357 1960 -2016 O ATOM 2890 CB LEU A 454 168.439 41.228 549.091 1.00 72.82 C ANISOU 2890 CB LEU A 454 12032 8231 7406 778 1654 -1837 C ATOM 2891 CG LEU A 454 169.874 41.244 549.621 1.00 63.29 C ANISOU 2891 CG LEU A 454 10921 7138 5988 476 1545 -1915 C ATOM 2892 CD1 LEU A 454 170.829 40.655 548.594 1.00 54.44 C ANISOU 2892 CD1 LEU A 454 9676 6035 4974 313 1358 -1772 C ATOM 2893 CD2 LEU A 454 170.296 42.655 550.003 1.00 59.44 C ANISOU 2893 CD2 LEU A 454 10777 6445 5363 380 1597 -2167 C ATOM 2894 N LEU A 455 165.186 41.100 549.111 1.00 72.21 N ANISOU 2894 N LEU A 455 11693 8114 7629 1427 1974 -1746 N ATOM 2895 CA LEU A 455 163.971 41.250 548.320 1.00 69.79 C ANISOU 2895 CA LEU A 455 11278 7675 7566 1698 2024 -1673 C ATOM 2896 C LEU A 455 162.787 41.774 549.127 1.00 75.00 C ANISOU 2896 C LEU A 455 11957 8331 8210 1944 2248 -1791 C ATOM 2897 O LEU A 455 161.668 41.803 548.605 1.00 77.42 O ANISOU 2897 O LEU A 455 12122 8577 8718 2190 2302 -1724 O ATOM 2898 CB LEU A 455 163.596 39.919 547.660 1.00 59.00 C ANISOU 2898 CB LEU A 455 9576 6475 6365 1722 1932 -1428 C ATOM 2899 CG LEU A 455 164.340 39.543 546.376 1.00 56.65 C ANISOU 2899 CG LEU A 455 9239 6095 6191 1590 1724 -1295 C ATOM 2900 CD1 LEU A 455 165.670 38.872 546.679 1.00 57.81 C ANISOU 2900 CD1 LEU A 455 9377 6402 6185 1308 1610 -1261 C ATOM 2901 CD2 LEU A 455 163.476 38.658 545.488 1.00 52.02 C ANISOU 2901 CD2 LEU A 455 8372 5560 5832 1724 1670 -1094 C ATOM 2902 N MET A 456 162.999 42.191 550.371 1.00 79.69 N ANISOU 2902 N MET A 456 12715 8995 8568 1888 2379 -1968 N ATOM 2903 CA MET A 456 161.926 42.733 551.187 1.00 84.13 C ANISOU 2903 CA MET A 456 13315 9555 9096 2120 2614 -2102 C ATOM 2904 C MET A 456 161.981 44.260 551.164 1.00 97.52 C ANISOU 2904 C MET A 456 15360 10926 10768 2202 2685 -2331 C ATOM 2905 O MET A 456 162.674 44.869 550.343 1.00 93.40 O ANISOU 2905 O MET A 456 15020 10166 10302 2107 2549 -2352 O ATOM 2906 CB MET A 456 162.006 42.176 552.612 1.00 94.33 C ANISOU 2906 CB MET A 456 14569 11140 10131 2023 2736 -2151 C ATOM 2907 CG MET A 456 163.231 42.610 553.398 1.00109.74 C ANISOU 2907 CG MET A 456 16795 13106 11796 1763 2693 -2314 C ATOM 2908 SD MET A 456 163.179 42.048 555.112 1.00106.49 S ANISOU 2908 SD MET A 456 16365 13035 11062 1682 2849 -2377 S ATOM 2909 CE MET A 456 161.678 42.840 555.683 1.00 80.93 C ANISOU 2909 CE MET A 456 13174 9717 7859 2017 3162 -2541 C ATOM 2910 N CYS A 457 161.237 44.893 552.075 1.00123.10 N ANISOU 2910 N CYS A 457 18693 14152 13926 2373 2901 -2501 N ATOM 2911 CA CYS A 457 161.168 46.351 552.090 1.00126.96 C ANISOU 2911 CA CYS A 457 19405 14374 14460 2413 2901 -2666 C ATOM 2912 C CYS A 457 162.487 46.969 552.542 1.00128.64 C ANISOU 2912 C CYS A 457 19910 14515 14454 2112 2812 -2818 C ATOM 2913 O CYS A 457 162.892 48.020 552.033 1.00136.02 O ANISOU 2913 O CYS A 457 21049 15179 15455 2057 2723 -2890 O ATOM 2914 CB CYS A 457 160.024 46.811 552.993 1.00132.62 C ANISOU 2914 CB CYS A 457 20053 15154 15183 2626 3100 -2776 C ATOM 2915 SG CYS A 457 158.400 46.181 552.512 1.00137.91 S ANISOU 2915 SG CYS A 457 20340 15930 16129 2970 3201 -2607 S ATOM 2916 N HIS A 458 163.167 46.336 553.492 1.00122.11 N ANISOU 2916 N HIS A 458 19095 13936 13365 1906 2827 -2858 N ATOM 2917 CA HIS A 458 164.432 46.854 553.999 1.00110.60 C ANISOU 2917 CA HIS A 458 17875 12457 11692 1603 2726 -2997 C ATOM 2918 C HIS A 458 165.614 46.126 553.367 1.00113.86 C ANISOU 2918 C HIS A 458 18279 12925 12057 1355 2542 -2888 C ATOM 2919 O HIS A 458 166.205 46.604 552.399 1.00112.64 O ANISOU 2919 O HIS A 458 18228 12551 12019 1263 2405 -2867 O ATOM 2920 CB HIS A 458 164.488 46.731 555.523 1.00100.20 C ANISOU 2920 CB HIS A 458 16586 11388 10097 1517 2834 -3124 C ATOM 2921 CG HIS A 458 165.747 47.267 556.129 1.00 97.18 C ANISOU 2921 CG HIS A 458 16423 11012 9490 1209 2720 -3269 C ATOM 2922 ND1 HIS A 458 166.900 46.519 556.236 1.00 76.90 N ANISOU 2922 ND1 HIS A 458 13837 8628 6755 935 2571 -3209 N ATOM 2923 CD2 HIS A 458 166.033 48.476 556.669 1.00 97.04 C ANISOU 2923 CD2 HIS A 458 16631 10847 9392 1133 2726 -3468 C ATOM 2924 CE1 HIS A 458 167.842 47.244 556.811 1.00 91.60 C ANISOU 2924 CE1 HIS A 458 15888 10467 8450 701 2482 -3362 C ATOM 2925 NE2 HIS A 458 167.342 48.436 557.084 1.00 93.63 N ANISOU 2925 NE2 HIS A 458 16303 10519 8754 813 2578 -3522 N TER 2926 HIS A 458 HETATM 2927 C10 3C0 A 501 187.885 24.340 525.974 1.00 37.45 C HETATM 2928 C13 3C0 A 501 183.918 26.952 524.854 1.00 43.91 C HETATM 2929 C15 3C0 A 501 183.412 29.472 524.621 1.00 41.85 C HETATM 2930 C17 3C0 A 501 184.674 29.179 526.642 1.00 42.24 C HETATM 2931 C20 3C0 A 501 182.141 30.804 526.283 1.00 47.88 C HETATM 2932 C21 3C0 A 501 181.148 28.921 525.374 1.00 56.87 C HETATM 2933 C22 3C0 A 501 183.227 28.618 526.686 1.00 44.48 C HETATM 2934 N19 3C0 A 501 182.466 29.465 525.749 1.00 47.53 N HETATM 2935 C14 3C0 A 501 183.459 28.093 523.919 1.00 47.67 C HETATM 2936 C16 3C0 A 501 184.796 29.771 525.261 1.00 43.54 C HETATM 2937 O18 3C0 A 501 184.918 30.608 526.458 1.00 57.54 O HETATM 2938 C23 3C0 A 501 183.255 27.146 526.237 1.00 38.87 C HETATM 2939 O12 3C0 A 501 185.370 26.858 524.900 1.00 43.59 O HETATM 2940 C02 3C0 A 501 185.871 25.746 525.504 1.00 31.52 C HETATM 2941 O01 3C0 A 501 185.203 24.792 525.901 1.00 33.77 O HETATM 2942 C03 3C0 A 501 187.395 25.748 525.637 1.00 27.63 C HETATM 2943 O11 3C0 A 501 187.385 23.423 524.996 1.00 38.53 O HETATM 2944 C04 3C0 A 501 187.780 26.646 526.627 1.00 30.87 C HETATM 2945 C05 3C0 A 501 188.343 27.866 526.268 1.00 28.17 C HETATM 2946 C06 3C0 A 501 188.729 28.771 527.250 1.00 32.41 C HETATM 2947 C07 3C0 A 501 188.552 28.456 528.593 1.00 30.84 C HETATM 2948 C08 3C0 A 501 187.988 27.237 528.952 1.00 37.08 C HETATM 2949 C09 3C0 A 501 187.601 26.331 527.970 1.00 41.19 C HETATM 2950 O HOH A 601 181.924 33.442 522.358 1.00 56.17 O HETATM 2951 O HOH A 602 196.704 13.303 549.184 1.00 41.60 O HETATM 2952 O HOH A 603 177.740 31.752 540.377 1.00 55.10 O HETATM 2953 O HOH A 604 177.996 22.059 525.840 1.00 28.67 O CONECT 625 1266 CONECT 1266 625 CONECT 2565 2583 CONECT 2583 2565 CONECT 2927 2942 2943 CONECT 2928 2935 2938 2939 CONECT 2929 2934 2935 2936 CONECT 2930 2933 2936 2937 CONECT 2931 2934 CONECT 2932 2934 CONECT 2933 2930 2934 2938 CONECT 2934 2929 2931 2932 2933 CONECT 2935 2928 2929 CONECT 2936 2929 2930 2937 CONECT 2937 2930 2936 CONECT 2938 2928 2933 CONECT 2939 2928 2940 CONECT 2940 2939 2941 2942 CONECT 2941 2940 CONECT 2942 2927 2940 2944 CONECT 2943 2927 CONECT 2944 2942 2945 2949 CONECT 2945 2944 2946 CONECT 2946 2945 2947 CONECT 2947 2946 2948 CONECT 2948 2947 2949 CONECT 2949 2944 2948 MASTER 329 0 1 19 0 0 3 6 2946 1 27 33 END