HEADER SIGNALING PROTEIN 11-MAY-19 6K1Q TITLE HUMAN ENDOTHELIN RECEPTOR TYPE-B IN COMPLEX WITH INVERSE AGONIST TITLE 2 IRL2500 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENDOTHELIN B RECEPTOR,ENDOLYSIN,ENDOTHELIN B RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ET-BR,ENDOTHELIN RECEPTOR NON-SELECTIVE TYPE,LYSIS PROTEIN, COMPND 5 LYSOZYME,MURAMIDASE,ET-BR,ENDOTHELIN RECEPTOR NON-SELECTIVE TYPE; COMPND 6 EC: 3.2.1.17; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: EDNRB, ETRB; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PFASTBAC KEYWDS ALPHA HELICAL, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR C.NAGIRI,W.SHIHOYA,O.NUREKI REVDAT 1 17-JUL-19 6K1Q 0 JRNL AUTH C.NAGIRI,W.SHIHOYA,A.INOUE,F.M.N.KADJI,J.AOKI,O.NUREKI JRNL TITL CRYSTAL STRUCTURE OF HUMAN ENDOTHELIN ETBRECEPTOR IN COMPLEX JRNL TITL 2 WITH PEPTIDE INVERSE AGONIST IRL2500. JRNL REF COMMUN BIOL V. 2 236 2019 JRNL REFN ESSN 2399-3642 JRNL PMID 31263780 JRNL DOI 10.1038/S42003-019-0482-7 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.14_3260 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.47 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 25008 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.224 REMARK 3 R VALUE (WORKING SET) : 0.222 REMARK 3 FREE R VALUE : 0.265 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1251 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 48.4772 - 5.6138 1.00 2824 147 0.2224 0.2834 REMARK 3 2 5.6138 - 4.4569 1.00 2681 142 0.2022 0.2229 REMARK 3 3 4.4569 - 3.8938 1.00 2653 139 0.1937 0.2129 REMARK 3 4 3.8938 - 3.5379 1.00 2620 139 0.1964 0.2533 REMARK 3 5 3.5379 - 3.2844 1.00 2623 138 0.2349 0.2980 REMARK 3 6 3.2844 - 3.0908 1.00 2619 138 0.2414 0.2968 REMARK 3 7 3.0908 - 2.9360 1.00 2579 136 0.2649 0.3294 REMARK 3 8 2.9360 - 2.8082 0.99 2576 136 0.2893 0.3388 REMARK 3 9 2.8082 - 2.7001 0.99 2582 136 0.3255 0.3526 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL 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) : 0.410 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.360 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 70.14 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 83.77 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 203 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.8155 41.9249 31.9392 REMARK 3 T TENSOR REMARK 3 T11: 0.3813 T22: 0.3953 REMARK 3 T33: 0.5151 T12: -0.1236 REMARK 3 T13: 0.0144 T23: -0.0308 REMARK 3 L TENSOR REMARK 3 L11: 2.5150 L22: 4.0288 REMARK 3 L33: 3.4160 L12: -0.9008 REMARK 3 L13: 0.1077 L23: -1.1018 REMARK 3 S TENSOR REMARK 3 S11: 0.0327 S12: -0.1504 S13: 0.0281 REMARK 3 S21: -0.0979 S22: -0.2618 S23: -0.0870 REMARK 3 S31: 0.2647 S32: 0.0112 S33: 0.1998 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 48.9781 32.2077 28.7928 REMARK 3 T TENSOR REMARK 3 T11: 0.4155 T22: 0.3416 REMARK 3 T33: 0.4355 T12: -0.0617 REMARK 3 T13: 0.0670 T23: 0.0057 REMARK 3 L TENSOR REMARK 3 L11: 2.8307 L22: 1.3356 REMARK 3 L33: 0.6422 L12: -0.9310 REMARK 3 L13: 1.0909 L23: -0.1238 REMARK 3 S TENSOR REMARK 3 S11: 0.1414 S12: -0.3404 S13: -0.2632 REMARK 3 S21: -0.0656 S22: 0.1238 S23: 0.1693 REMARK 3 S31: 0.6095 S32: -0.1026 S33: -0.1156 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 248 THROUGH 312 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.8219 25.9253 31.2921 REMARK 3 T TENSOR REMARK 3 T11: 0.8711 T22: 0.5713 REMARK 3 T33: 0.5910 T12: -0.2188 REMARK 3 T13: -0.0023 T23: -0.0031 REMARK 3 L TENSOR REMARK 3 L11: 0.9463 L22: 0.5670 REMARK 3 L33: 2.2105 L12: -0.4818 REMARK 3 L13: -0.5102 L23: -0.1861 REMARK 3 S TENSOR REMARK 3 S11: -0.0592 S12: -0.2566 S13: -0.2530 REMARK 3 S21: 0.0421 S22: -0.2431 S23: 0.1256 REMARK 3 S31: 0.7212 S32: 0.1786 S33: 0.2817 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 313 THROUGH 403 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.4439 14.0336 65.1505 REMARK 3 T TENSOR REMARK 3 T11: 0.9038 T22: 0.9914 REMARK 3 T33: 0.8099 T12: -0.1603 REMARK 3 T13: 0.0948 T23: 0.0900 REMARK 3 L TENSOR REMARK 3 L11: 3.4486 L22: 5.2776 REMARK 3 L33: 5.5651 L12: 1.5103 REMARK 3 L13: 2.5568 L23: 1.2442 REMARK 3 S TENSOR REMARK 3 S11: -0.0415 S12: -0.8565 S13: -0.2758 REMARK 3 S21: -0.1089 S22: -0.6047 S23: 0.6505 REMARK 3 S31: 0.5911 S32: -0.8476 S33: 0.5342 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: NULL REMARK 3 ORIGIN FOR THE GROUP (A): 32.4449 29.9822 39.2598 REMARK 3 T TENSOR REMARK 3 T11: 0.6211 T22: 0.5464 REMARK 3 T33: 0.6117 T12: -0.1692 REMARK 3 T13: 0.0680 T23: 0.0141 REMARK 3 L TENSOR REMARK 3 L11: 2.7217 L22: 3.2779 REMARK 3 L33: 2.0741 L12: -0.1011 REMARK 3 L13: 0.3288 L23: -1.7070 REMARK 3 S TENSOR REMARK 3 S11: 0.0447 S12: -0.5075 S13: -0.0117 REMARK 3 S21: 0.4138 S22: -0.3392 S23: 0.0217 REMARK 3 S31: 0.5613 S32: -0.2129 S33: 0.3005 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: NULL REMARK 3 ORIGIN FOR THE GROUP (A): 28.9300 38.5663 31.3760 REMARK 3 T TENSOR REMARK 3 T11: 0.4350 T22: 0.5469 REMARK 3 T33: 0.6871 T12: -0.1251 REMARK 3 T13: 0.0926 T23: 0.0006 REMARK 3 L TENSOR REMARK 3 L11: 5.4209 L22: 4.4820 REMARK 3 L33: 6.5643 L12: -0.4717 REMARK 3 L13: 1.8872 L23: -1.1556 REMARK 3 S TENSOR REMARK 3 S11: 0.0204 S12: 0.4498 S13: -0.5152 REMARK 3 S21: -0.3560 S22: 0.4026 S23: 0.4474 REMARK 3 S31: 0.1249 S32: -0.2072 S33: -0.5082 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 6K1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-MAY-19. REMARK 100 THE DEPOSITION ID IS D_1300012038. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-OCT-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 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) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28018 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 48.469 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 19.28 REMARK 200 R MERGE (I) : 0.32200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.6700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 19.52 REMARK 200 R MERGE FOR SHELL (I) : 5.83500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.740 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 (%): 70.88 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG300, 150 MM NAH2PO4,10 MM TCEP, REMARK 280 100 MM BIS-TRIS, PH 7.5, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 54.95500 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 54.95500 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 145.79500 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 54.95500 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 54.95500 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 145.79500 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 54.95500 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 54.95500 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 145.79500 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 54.95500 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 54.95500 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 145.79500 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 54.95500 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 54.95500 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 145.79500 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 54.95500 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 54.95500 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 145.79500 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 54.95500 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 54.95500 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 145.79500 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 54.95500 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 54.95500 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 145.79500 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 220 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21230 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 63 REMARK 465 GLY A 64 REMARK 465 GLY A 65 REMARK 465 LEU A 66 REMARK 465 ALA A 67 REMARK 465 PRO A 68 REMARK 465 ALA A 69 REMARK 465 GLU A 70 REMARK 465 VAL A 71 REMARK 465 PRO A 72 REMARK 465 LYS A 73 REMARK 465 GLY A 74 REMARK 465 ASP A 75 REMARK 465 ARG A 76 REMARK 465 THR A 77 REMARK 465 ALA A 78 REMARK 465 GLY A 79 REMARK 465 SER A 80 REMARK 465 PRO A 81 REMARK 465 PRO A 82 REMARK 465 ARG A 83 REMARK 465 THR A 84 REMARK 465 ILE A 85 REMARK 465 SER A 86 REMARK 465 PRO A 87 REMARK 465 PRO A 88 REMARK 465 PRO A 89 REMARK 465 CYS A 90 REMARK 465 ARG A 208 REMARK 465 ILE A 209 REMARK 465 LYS A 210 REMARK 465 GLY A 211 REMARK 465 ILE A 212 REMARK 465 GLY A 213 REMARK 465 GLY A 1012A REMARK 465 GLY A 1012B REMARK 465 SER A 1012C REMARK 465 GLY A 1012D REMARK 465 GLY A 1012E REMARK 465 ASP A 1012F REMARK 465 GLU A 1012G REMARK 465 TRP A 404 REMARK 465 ALA A 405 REMARK 465 GLN A 406 REMARK 465 SER A 407 REMARK 465 PRO A 408 REMARK 465 SER A 409 REMARK 465 SER A 410 REMARK 465 GLU A 411 REMARK 465 ASN A 412 REMARK 465 LEU A 413 REMARK 465 TYR A 414 REMARK 465 PHE A 415 REMARK 465 GLN A 416 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 SER A 207 OG REMARK 470 LYS A 216 CD CE NZ REMARK 470 LYS A1015 CG CD CE NZ REMARK 470 LEU A1016 CG CD1 CD2 REMARK 470 ARG A1069 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 357 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 391 CD CE NZ 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 PHE A 282 -58.83 -139.12 REMARK 500 LEU A 401 -66.32 -102.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1206 REMARK 610 OLC A 1212 REMARK 610 OLC A 1213 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue D2U A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1213 DBREF 6K1Q A 66 303 UNP P24530 EDNRB_HUMAN 66 303 DBREF 6K1Q A 1012F 1111 UNP P00720 ENLYS_BPT4 61 161 DBREF 6K1Q A 311 407 UNP P24530 EDNRB_HUMAN 311 407 SEQADV 6K1Q GLY A 63 UNP P24530 EXPRESSION TAG SEQADV 6K1Q GLY A 64 UNP P24530 EXPRESSION TAG SEQADV 6K1Q GLY A 65 UNP P24530 EXPRESSION TAG SEQADV 6K1Q TYR A 124 UNP P24530 ARG 124 ENGINEERED MUTATION SEQADV 6K1Q ALA A 270 UNP P24530 LYS 270 ENGINEERED MUTATION SEQADV 6K1Q ASN A 1002 UNP P24530 LINKER SEQADV 6K1Q ILE A 1003 UNP P24530 LINKER SEQADV 6K1Q PHE A 1004 UNP P24530 LINKER SEQADV 6K1Q GLU A 1005 UNP P24530 LINKER SEQADV 6K1Q MET A 1006 UNP P24530 LINKER SEQADV 6K1Q LEU A 1007 UNP P24530 LINKER SEQADV 6K1Q ARG A 1008 UNP P24530 LINKER SEQADV 6K1Q ILE A 1009 UNP P24530 LINKER SEQADV 6K1Q ASP A 1010 UNP P24530 LINKER SEQADV 6K1Q GLU A 1011 UNP P24530 LINKER SEQADV 6K1Q GLY A 1012 UNP P24530 LINKER SEQADV 6K1Q GLY A 1012A UNP P24530 LINKER SEQADV 6K1Q GLY A 1012B UNP P24530 LINKER SEQADV 6K1Q SER A 1012C UNP P24530 LINKER SEQADV 6K1Q GLY A 1012D UNP P24530 LINKER SEQADV 6K1Q GLY A 1012E UNP P24530 LINKER SEQADV 6K1Q ALA A 1047 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 6K1Q ARG A 1087 UNP P00720 ILE 137 ENGINEERED MUTATION SEQADV 6K1Q ALA A 342 UNP P24530 SER 342 ENGINEERED MUTATION SEQADV 6K1Q ALA A 381 UNP P24530 ILE 381 ENGINEERED MUTATION SEQADV 6K1Q ALA A 396 UNP P24530 CYS 396 ENGINEERED MUTATION SEQADV 6K1Q ALA A 400 UNP P24530 CYS 400 ENGINEERED MUTATION SEQADV 6K1Q ALA A 405 UNP P24530 CYS 405 ENGINEERED MUTATION SEQADV 6K1Q PRO A 408 UNP P24530 EXPRESSION TAG SEQADV 6K1Q SER A 409 UNP P24530 EXPRESSION TAG SEQADV 6K1Q SER A 410 UNP P24530 EXPRESSION TAG SEQADV 6K1Q GLU A 411 UNP P24530 EXPRESSION TAG SEQADV 6K1Q ASN A 412 UNP P24530 EXPRESSION TAG SEQADV 6K1Q LEU A 413 UNP P24530 EXPRESSION TAG SEQADV 6K1Q TYR A 414 UNP P24530 EXPRESSION TAG SEQADV 6K1Q PHE A 415 UNP P24530 EXPRESSION TAG SEQADV 6K1Q GLN A 416 UNP P24530 EXPRESSION TAG SEQRES 1 A 464 GLY GLY GLY LEU ALA PRO ALA GLU VAL PRO LYS GLY ASP SEQRES 2 A 464 ARG THR ALA GLY SER PRO PRO ARG THR ILE SER PRO PRO SEQRES 3 A 464 PRO CYS GLN GLY PRO ILE GLU ILE LYS GLU THR PHE LYS SEQRES 4 A 464 TYR ILE ASN THR VAL VAL SER CYS LEU VAL PHE VAL LEU SEQRES 5 A 464 GLY ILE ILE GLY ASN SER THR LEU LEU TYR ILE ILE TYR SEQRES 6 A 464 LYS ASN LYS CYS MET ARG ASN GLY PRO ASN ILE LEU ILE SEQRES 7 A 464 ALA SER LEU ALA LEU GLY ASP LEU LEU HIS ILE VAL ILE SEQRES 8 A 464 ASP ILE PRO ILE ASN VAL TYR LYS LEU LEU ALA GLU ASP SEQRES 9 A 464 TRP PRO PHE GLY ALA GLU MET CYS LYS LEU VAL PRO PHE SEQRES 10 A 464 ILE GLN LYS ALA SER VAL GLY ILE THR VAL LEU SER LEU SEQRES 11 A 464 CYS ALA LEU SER ILE ASP ARG TYR ARG ALA VAL ALA SER SEQRES 12 A 464 TRP SER ARG ILE LYS GLY ILE GLY VAL PRO LYS TRP THR SEQRES 13 A 464 ALA VAL GLU ILE VAL LEU ILE TRP VAL VAL SER VAL VAL SEQRES 14 A 464 LEU ALA VAL PRO GLU ALA ILE GLY PHE ASP ILE ILE THR SEQRES 15 A 464 MET ASP TYR LYS GLY SER TYR LEU ARG ILE CYS LEU LEU SEQRES 16 A 464 HIS PRO VAL GLN LYS THR ALA PHE MET GLN PHE TYR ALA SEQRES 17 A 464 THR ALA LYS ASP TRP TRP LEU PHE SER PHE TYR PHE CYS SEQRES 18 A 464 LEU PRO LEU ALA ILE THR ALA PHE PHE TYR THR LEU MET SEQRES 19 A 464 THR CYS GLU MET LEU ARG LYS ASN ILE PHE GLU MET LEU SEQRES 20 A 464 ARG ILE ASP GLU GLY GLY GLY SER GLY GLY ASP GLU ALA SEQRES 21 A 464 GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG SEQRES 22 A 464 GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SEQRES 23 A 464 SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET SEQRES 24 A 464 VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR SEQRES 25 A 464 ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU SEQRES 26 A 464 ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN SEQRES 27 A 464 THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG SEQRES 28 A 464 THR GLY THR TRP ASP ALA TYR LEU ASN ASP HIS LEU LYS SEQRES 29 A 464 GLN ARG ARG GLU VAL ALA LYS THR VAL PHE CYS LEU VAL SEQRES 30 A 464 LEU VAL PHE ALA LEU CYS TRP LEU PRO LEU HIS LEU ALA SEQRES 31 A 464 ARG ILE LEU LYS LEU THR LEU TYR ASN GLN ASN ASP PRO SEQRES 32 A 464 ASN ARG CYS GLU LEU LEU SER PHE LEU LEU VAL LEU ASP SEQRES 33 A 464 TYR ILE GLY ILE ASN MET ALA SER LEU ASN SER CYS ALA SEQRES 34 A 464 ASN PRO ILE ALA LEU TYR LEU VAL SER LYS ARG PHE LYS SEQRES 35 A 464 ASN ALA PHE LYS SER ALA LEU CYS CYS TRP ALA GLN SER SEQRES 36 A 464 PRO SER SER GLU ASN LEU TYR PHE GLN HET D2U A1201 43 HET PO4 A1202 5 HET PO4 A1203 5 HET PO4 A1204 5 HET PO4 A1205 5 HET OLC A1206 21 HET OLC A1207 25 HET OLC A1208 25 HET OLC A1209 25 HET OLC A1210 25 HET OLC A1211 25 HET OLC A1212 20 HET OLC A1213 20 HETNAM D2U (2~{S})-2-[[(2~{R})-2-[(3,5-DIMETHYLPHENYL)CARBONYL- HETNAM 2 D2U METHYL-AMINO]-3-(4-PHENYLPHENYL)PROPANOYL]AMINO]-3- HETNAM 3 D2U (1~{H}-INDOL-3-YL)PROPANOIC ACID HETNAM PO4 PHOSPHATE ION HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 D2U C36 H35 N3 O4 FORMUL 3 PO4 4(O4 P 3-) FORMUL 7 OLC 8(C21 H40 O4) FORMUL 15 HOH *34(H2 O) HELIX 1 AA1 GLN A 91 ASN A 129 1 39 HELIX 2 AA2 LYS A 130 ARG A 133 5 4 HELIX 3 AA3 ASN A 134 ALA A 164 1 31 HELIX 4 AA4 PHE A 169 ALA A 204 1 36 HELIX 5 AA5 PRO A 215 GLY A 239 1 25 HELIX 6 AA6 THR A 263 PHE A 282 1 20 HELIX 7 AA7 PHE A 282 GLY A 1012 1 33 HELIX 8 AA8 LEU A 1016 ASN A 1031 1 16 HELIX 9 AA9 LEU A 1034 LEU A 1041 1 8 HELIX 10 AB1 ASP A 1042 GLY A 1063 1 22 HELIX 11 AB2 PHE A 1064 GLN A 1073 1 10 HELIX 12 AB3 ARG A 1075 LYS A 1085 1 11 HELIX 13 AB4 SER A 1086 THR A 1092 1 7 HELIX 14 AB5 THR A 1092 GLY A 1106 1 15 HELIX 15 AB6 ASN A 312 TYR A 350 1 39 HELIX 16 AB7 ASN A 353 SER A 390 1 38 HELIX 17 AB8 SER A 390 LEU A 401 1 12 SHEET 1 AA1 2 PHE A 240 TYR A 247 0 SHEET 2 AA1 2 SER A 250 LEU A 257 -1 O ILE A 254 N ILE A 243 SSBOND 1 CYS A 174 CYS A 255 1555 1555 2.00 SITE 1 AC1 20 ASP A 147 HIS A 150 ASN A 158 LYS A 161 SITE 2 AC1 20 VAL A 177 PRO A 178 GLN A 181 LYS A 182 SITE 3 AC1 20 SER A 184 VAL A 185 THR A 188 PHE A 240 SITE 4 AC1 20 TYR A 281 TRP A 336 LEU A 339 ARG A 343 SITE 5 AC1 20 ALA A 375 ASN A 378 SER A 379 HOH A1311 SITE 1 AC2 5 ILE A1003 TYR A1038 ALA A1043 ARG A1046 SITE 2 AC2 5 ILE A1050 SITE 1 AC3 4 CYS A 131 ARG A 392 ASN A 395 HOH A1313 SITE 1 AC4 6 ASN A 312 ASP A 313 ASP A1010 ARG A1095 SITE 2 AC4 6 ARG A1098 HOH A1301 SITE 1 AC5 1 LYS A 398 SITE 1 AC6 8 GLU A 98 LYS A 101 TYR A 102 LEU A 163 SITE 2 AC6 8 LEU A 232 THR A 263 PHE A 265 TYR A 269 SITE 1 AC7 3 TRP A 275 SER A 279 OLC A1208 SITE 1 AC8 4 TYR A 102 ALA A 264 PHE A 268 OLC A1207 SITE 1 AC9 3 ILE A 117 LEU A 145 TRP A 226 SITE 1 AD1 7 LYS A 323 VAL A 331 ALA A 381 LEU A 388 SITE 2 AD1 7 VAL A 389 LYS A 391 OLC A1211 SITE 1 AD2 6 ALA A 290 PHE A 326 LEU A 330 VAL A 331 SITE 2 AD2 6 LEU A 334 OLC A1210 SITE 1 AD3 3 ILE A 96 MET A 374 LEU A 377 SITE 1 AD4 5 PHE A 112 LEU A 149 VAL A 159 ALA A 183 SITE 2 AD4 5 VAL A 230 CRYST1 109.910 109.910 291.590 90.00 90.00 90.00 I 4 2 2 16 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 0.009098 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009098 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003429 0.00000 ATOM 1 N GLN A 91 17.764 44.396 7.662 1.00152.26 N ANISOU 1 N GLN A 91 19475 19985 18391 -644 -6161 -1536 N ATOM 2 CA GLN A 91 17.909 42.972 7.932 1.00152.36 C ANISOU 2 CA GLN A 91 19603 19844 18441 -957 -6085 -1711 C ATOM 3 C GLN A 91 18.380 42.757 9.366 1.00146.77 C ANISOU 3 C GLN A 91 18648 19058 18061 -1114 -5736 -1704 C ATOM 4 O GLN A 91 19.002 43.640 9.955 1.00142.61 O ANISOU 4 O GLN A 91 18036 18549 17600 -922 -5330 -1553 O ATOM 5 CB GLN A 91 18.889 42.339 6.943 1.00153.49 C ANISOU 5 CB GLN A 91 20427 19796 18097 -860 -6072 -1841 C ATOM 6 CG GLN A 91 18.596 40.886 6.609 1.00158.65 C ANISOU 6 CG GLN A 91 21250 20322 18709 -1130 -6183 -2030 C ATOM 7 CD GLN A 91 19.480 40.362 5.493 1.00160.05 C ANISOU 7 CD GLN A 91 22108 20325 18380 -972 -6178 -2152 C ATOM 8 OE1 GLN A 91 19.714 41.047 4.498 1.00161.73 O ANISOU 8 OE1 GLN A 91 22624 20594 18232 -686 -6276 -2095 O ATOM 9 NE2 GLN A 91 19.982 39.144 5.658 1.00158.11 N ANISOU 9 NE2 GLN A 91 22112 19864 18100 -1136 -6039 -2306 N ATOM 10 N GLY A 92 18.068 41.589 9.922 1.00143.23 N ANISOU 10 N GLY A 92 18073 18532 17815 -1435 -5671 -1801 N ATOM 11 CA GLY A 92 18.474 41.230 11.263 1.00133.53 C ANISOU 11 CA GLY A 92 16638 17224 16875 -1604 -5336 -1791 C ATOM 12 C GLY A 92 19.937 41.494 11.579 1.00123.88 C ANISOU 12 C GLY A 92 15730 15862 15475 -1414 -4892 -1749 C ATOM 13 O GLY A 92 20.264 42.182 12.553 1.00127.11 O ANISOU 13 O GLY A 92 15889 16325 16082 -1334 -4526 -1616 O ATOM 14 N PRO A 93 20.850 40.937 10.773 1.00112.76 N ANISOU 14 N PRO A 93 14876 14279 13690 -1329 -4872 -1852 N ATOM 15 CA PRO A 93 22.283 41.136 11.064 1.00104.45 C ANISOU 15 CA PRO A 93 14088 13109 12488 -1143 -4396 -1782 C ATOM 16 C PRO A 93 22.705 42.594 11.156 1.00103.58 C ANISOU 16 C PRO A 93 13871 13115 12369 -853 -4144 -1581 C ATOM 17 O PRO A 93 23.438 42.957 12.084 1.00 97.32 O ANISOU 17 O PRO A 93 12959 12296 11723 -815 -3748 -1482 O ATOM 18 CB PRO A 93 22.971 40.415 9.899 1.00104.94 C ANISOU 18 CB PRO A 93 14758 13005 12108 -1045 -4491 -1917 C ATOM 19 CG PRO A 93 22.017 39.339 9.532 1.00110.96 C ANISOU 19 CG PRO A 93 15557 13707 12895 -1322 -4942 -2116 C ATOM 20 CD PRO A 93 20.646 39.927 9.717 1.00113.64 C ANISOU 20 CD PRO A 93 15381 14268 13528 -1432 -5246 -2049 C ATOM 21 N ILE A 94 22.263 43.444 10.227 1.00108.17 N ANISOU 21 N ILE A 94 14502 13811 12785 -653 -4376 -1513 N ATOM 22 CA ILE A 94 22.680 44.843 10.275 1.00109.01 C ANISOU 22 CA ILE A 94 14541 13990 12887 -378 -4138 -1312 C ATOM 23 C ILE A 94 21.950 45.605 11.379 1.00106.86 C ANISOU 23 C ILE A 94 13723 13849 13031 -426 -4060 -1213 C ATOM 24 O ILE A 94 22.518 46.528 11.978 1.00100.51 O ANISOU 24 O ILE A 94 12824 13038 12329 -286 -3732 -1079 O ATOM 25 CB ILE A 94 22.489 45.514 8.903 1.00115.96 C ANISOU 25 CB ILE A 94 15692 14935 13434 -123 -4393 -1249 C ATOM 26 CG1 ILE A 94 21.095 45.226 8.341 1.00121.05 C ANISOU 26 CG1 ILE A 94 16183 15708 14104 -232 -4935 -1343 C ATOM 27 CG2 ILE A 94 23.567 45.056 7.929 1.00120.49 C ANISOU 27 CG2 ILE A 94 16851 15371 13559 18 -4291 -1290 C ATOM 28 CD1 ILE A 94 20.906 45.675 6.903 1.00122.16 C ANISOU 28 CD1 ILE A 94 16660 15907 13850 8 -5247 -1307 C ATOM 29 N GLU A 95 20.700 45.238 11.675 1.00112.73 N ANISOU 29 N GLU A 95 14102 14708 14024 -621 -4350 -1277 N ATOM 30 CA GLU A 95 19.983 45.869 12.780 1.00117.63 C ANISOU 30 CA GLU A 95 14196 15459 15038 -654 -4238 -1186 C ATOM 31 C GLU A 95 20.579 45.473 14.125 1.00112.30 C ANISOU 31 C GLU A 95 13399 14703 14568 -806 -3843 -1199 C ATOM 32 O GLU A 95 20.711 46.312 15.024 1.00113.54 O ANISOU 32 O GLU A 95 13330 14899 14911 -710 -3564 -1098 O ATOM 33 CB GLU A 95 18.502 45.493 12.730 1.00127.62 C ANISOU 33 CB GLU A 95 15077 16882 16530 -833 -4637 -1233 C ATOM 34 CG GLU A 95 17.740 46.034 11.532 1.00138.89 C ANISOU 34 CG GLU A 95 16529 18436 17808 -668 -5064 -1196 C ATOM 35 CD GLU A 95 16.559 45.156 11.161 1.00151.07 C ANISOU 35 CD GLU A 95 17862 20072 19464 -926 -5546 -1305 C ATOM 36 OE1 GLU A 95 16.520 43.993 11.616 1.00154.01 O ANISOU 36 OE1 GLU A 95 18208 20357 19953 -1240 -5552 -1431 O ATOM 37 OE2 GLU A 95 15.671 45.623 10.418 1.00156.79 O ANISOU 37 OE2 GLU A 95 18449 20952 20173 -823 -5932 -1258 O ATOM 38 N ILE A 96 20.942 44.197 14.279 1.00 99.43 N ANISOU 38 N ILE A 96 11937 12948 12895 -1035 -3827 -1324 N ATOM 39 CA ILE A 96 21.468 43.707 15.551 1.00 87.37 C ANISOU 39 CA ILE A 96 10303 11345 11549 -1187 -3484 -1329 C ATOM 40 C ILE A 96 22.829 44.326 15.846 1.00 85.47 C ANISOU 40 C ILE A 96 10282 11011 11182 -994 -3099 -1247 C ATOM 41 O ILE A 96 23.088 44.793 16.962 1.00 86.71 O ANISOU 41 O ILE A 96 10230 11188 11526 -985 -2812 -1178 O ATOM 42 CB ILE A 96 21.543 42.170 15.538 1.00 80.33 C ANISOU 42 CB ILE A 96 9580 10314 10627 -1460 -3580 -1472 C ATOM 43 CG1 ILE A 96 20.146 41.564 15.682 1.00 85.06 C ANISOU 43 CG1 ILE A 96 9829 11007 11482 -1728 -3898 -1526 C ATOM 44 CG2 ILE A 96 22.478 41.666 16.632 1.00 72.15 C ANISOU 44 CG2 ILE A 96 8590 9158 9664 -1543 -3194 -1460 C ATOM 45 CD1 ILE A 96 20.072 40.111 15.270 1.00 87.85 C ANISOU 45 CD1 ILE A 96 10421 11194 11764 -1993 -4122 -1685 C ATOM 46 N LYS A 97 23.724 44.328 14.854 1.00 80.01 N ANISOU 46 N LYS A 97 10015 10217 10169 -839 -3088 -1250 N ATOM 47 CA LYS A 97 25.066 44.853 15.081 1.00 72.50 C ANISOU 47 CA LYS A 97 9252 9176 9118 -678 -2727 -1154 C ATOM 48 C LYS A 97 25.040 46.344 15.395 1.00 67.85 C ANISOU 48 C LYS A 97 8470 8664 8645 -491 -2596 -1009 C ATOM 49 O LYS A 97 25.867 46.823 16.179 1.00 70.57 O ANISOU 49 O LYS A 97 8781 8957 9074 -451 -2288 -936 O ATOM 50 CB LYS A 97 25.958 44.562 13.870 1.00 75.99 C ANISOU 50 CB LYS A 97 10171 9510 9190 -533 -2731 -1166 C ATOM 51 CG LYS A 97 26.446 43.113 13.801 1.00 83.63 C ANISOU 51 CG LYS A 97 11397 10337 10041 -677 -2714 -1302 C ATOM 52 CD LYS A 97 26.513 42.584 12.373 1.00 95.29 C ANISOU 52 CD LYS A 97 13307 11747 11150 -582 -2939 -1394 C ATOM 53 CE LYS A 97 27.580 43.284 11.544 1.00 99.53 C ANISOU 53 CE LYS A 97 14164 12257 11394 -288 -2734 -1268 C ATOM 54 NZ LYS A 97 27.483 42.906 10.102 1.00102.36 N ANISOU 54 NZ LYS A 97 14951 12582 11358 -162 -2975 -1352 N ATOM 55 N GLU A 98 24.092 47.088 14.818 1.00 63.99 N ANISOU 55 N GLU A 98 7856 8288 8171 -376 -2840 -966 N ATOM 56 CA GLU A 98 23.973 48.508 15.138 1.00 68.02 C ANISOU 56 CA GLU A 98 8188 8845 8811 -187 -2725 -831 C ATOM 57 C GLU A 98 23.490 48.713 16.568 1.00 71.84 C ANISOU 57 C GLU A 98 8279 9391 9627 -289 -2571 -841 C ATOM 58 O GLU A 98 24.007 49.579 17.285 1.00 70.52 O ANISOU 58 O GLU A 98 8059 9177 9559 -194 -2315 -769 O ATOM 59 CB GLU A 98 23.036 49.196 14.148 1.00 70.43 C ANISOU 59 CB GLU A 98 8458 9255 9046 -17 -3039 -773 C ATOM 60 CG GLU A 98 23.760 49.964 13.053 1.00 77.34 C ANISOU 60 CG GLU A 98 9691 10059 9637 231 -3012 -649 C ATOM 61 CD GLU A 98 24.390 51.245 13.562 1.00 82.24 C ANISOU 61 CD GLU A 98 10276 10603 10369 393 -2715 -499 C ATOM 62 OE1 GLU A 98 23.704 51.996 14.287 1.00 83.74 O ANISOU 62 OE1 GLU A 98 10154 10848 10815 438 -2700 -467 O ATOM 63 OE2 GLU A 98 25.573 51.498 13.244 1.00 83.59 O ANISOU 63 OE2 GLU A 98 10731 10652 10378 473 -2493 -412 O ATOM 64 N THR A 99 22.502 47.926 17.001 1.00 74.51 N ANISOU 64 N THR A 99 8348 9828 10136 -484 -2722 -927 N ATOM 65 CA THR A 99 22.031 48.011 18.380 1.00 70.71 C ANISOU 65 CA THR A 99 7504 9416 9945 -578 -2545 -929 C ATOM 66 C THR A 99 23.167 47.748 19.362 1.00 65.81 C ANISOU 66 C THR A 99 7000 8679 9325 -654 -2204 -941 C ATOM 67 O THR A 99 23.405 48.535 20.286 1.00 69.79 O ANISOU 67 O THR A 99 7390 9180 9948 -574 -1972 -897 O ATOM 68 CB THR A 99 20.889 47.018 18.612 1.00 76.62 C ANISOU 68 CB THR A 99 7967 10278 10868 -814 -2746 -1000 C ATOM 69 OG1 THR A 99 19.940 47.113 17.542 1.00 82.99 O ANISOU 69 OG1 THR A 99 8704 11186 11642 -768 -3125 -998 O ATOM 70 CG2 THR A 99 20.190 47.313 19.932 1.00 73.84 C ANISOU 70 CG2 THR A 99 7199 10041 10814 -852 -2563 -965 C ATOM 71 N PHE A 100 23.889 46.644 19.167 1.00 58.08 N ANISOU 71 N PHE A 100 6264 7598 8207 -798 -2182 -1004 N ATOM 72 CA PHE A 100 24.949 46.276 20.095 1.00 57.05 C ANISOU 72 CA PHE A 100 6225 7369 8082 -873 -1888 -1006 C ATOM 73 C PHE A 100 26.179 47.158 19.965 1.00 59.11 C ANISOU 73 C PHE A 100 6699 7534 8225 -693 -1688 -923 C ATOM 74 O PHE A 100 27.081 47.056 20.803 1.00 62.82 O ANISOU 74 O PHE A 100 7207 7938 8723 -737 -1454 -908 O ATOM 75 CB PHE A 100 25.324 44.807 19.909 1.00 50.49 C ANISOU 75 CB PHE A 100 5587 6445 7151 -1058 -1927 -1088 C ATOM 76 CG PHE A 100 24.433 43.865 20.662 1.00 66.64 C ANISOU 76 CG PHE A 100 7390 8541 9390 -1301 -1984 -1146 C ATOM 77 CD1 PHE A 100 24.553 43.737 22.036 1.00 61.84 C ANISOU 77 CD1 PHE A 100 6604 7952 8940 -1392 -1743 -1120 C ATOM 78 CD2 PHE A 100 23.471 43.117 20.004 1.00 66.05 C ANISOU 78 CD2 PHE A 100 7266 8493 9336 -1446 -2285 -1218 C ATOM 79 CE1 PHE A 100 23.738 42.874 22.740 1.00 63.78 C ANISOU 79 CE1 PHE A 100 6625 8244 9363 -1616 -1764 -1142 C ATOM 80 CE2 PHE A 100 22.652 42.252 20.702 1.00 67.40 C ANISOU 80 CE2 PHE A 100 7191 8701 9717 -1696 -2328 -1247 C ATOM 81 CZ PHE A 100 22.785 42.130 22.073 1.00 67.95 C ANISOU 81 CZ PHE A 100 7082 8791 9946 -1777 -2049 -1198 C ATOM 82 N LYS A 101 26.246 48.011 18.941 1.00 65.18 N ANISOU 82 N LYS A 101 7603 8293 8869 -502 -1782 -854 N ATOM 83 CA LYS A 101 27.266 49.053 18.932 1.00 64.54 C ANISOU 83 CA LYS A 101 7655 8123 8744 -345 -1583 -745 C ATOM 84 C LYS A 101 27.101 49.962 20.141 1.00 58.73 C ANISOU 84 C LYS A 101 6684 7401 8229 -322 -1429 -727 C ATOM 85 O LYS A 101 28.076 50.293 20.823 1.00 55.48 O ANISOU 85 O LYS A 101 6325 6903 7850 -331 -1215 -695 O ATOM 86 CB LYS A 101 27.192 49.871 17.641 1.00 72.26 C ANISOU 86 CB LYS A 101 8801 9090 9565 -138 -1715 -651 C ATOM 87 CG LYS A 101 27.868 49.238 16.439 1.00 77.15 C ANISOU 87 CG LYS A 101 9765 9651 9896 -96 -1762 -637 C ATOM 88 CD LYS A 101 28.063 50.265 15.332 1.00 79.70 C ANISOU 88 CD LYS A 101 10278 9948 10056 134 -1800 -496 C ATOM 89 CE LYS A 101 28.503 49.617 14.029 1.00 83.32 C ANISOU 89 CE LYS A 101 11096 10379 10184 207 -1877 -491 C ATOM 90 NZ LYS A 101 28.901 50.647 13.029 1.00 86.60 N ANISOU 90 NZ LYS A 101 11723 10758 10424 439 -1841 -314 N ATOM 91 N TYR A 102 25.858 50.367 20.419 1.00 57.94 N ANISOU 91 N TYR A 102 6323 7411 8279 -287 -1544 -750 N ATOM 92 CA TYR A 102 25.566 51.203 21.579 1.00 55.81 C ANISOU 92 CA TYR A 102 5845 7159 8202 -237 -1393 -753 C ATOM 93 C TYR A 102 25.700 50.415 22.877 1.00 56.22 C ANISOU 93 C TYR A 102 5777 7239 8344 -421 -1231 -828 C ATOM 94 O TYR A 102 26.344 50.874 23.829 1.00 51.26 O ANISOU 94 O TYR A 102 5168 6547 7760 -415 -1034 -832 O ATOM 95 CB TYR A 102 24.160 51.786 21.447 1.00 54.55 C ANISOU 95 CB TYR A 102 5427 7125 8176 -116 -1548 -743 C ATOM 96 CG TYR A 102 23.989 52.719 20.271 1.00 59.20 C ANISOU 96 CG TYR A 102 6129 7684 8682 101 -1705 -648 C ATOM 97 CD1 TYR A 102 24.271 54.072 20.394 1.00 59.80 C ANISOU 97 CD1 TYR A 102 6263 7652 8806 298 -1595 -572 C ATOM 98 CD2 TYR A 102 23.539 52.252 19.040 1.00 64.21 C ANISOU 98 CD2 TYR A 102 6834 8383 9181 112 -1975 -632 C ATOM 99 CE1 TYR A 102 24.117 54.936 19.329 1.00 66.76 C ANISOU 99 CE1 TYR A 102 7262 8491 9611 505 -1728 -459 C ATOM 100 CE2 TYR A 102 23.381 53.112 17.965 1.00 65.64 C ANISOU 100 CE2 TYR A 102 7139 8544 9259 328 -2122 -528 C ATOM 101 CZ TYR A 102 23.672 54.454 18.117 1.00 70.89 C ANISOU 101 CZ TYR A 102 7851 9102 9983 527 -1988 -430 C ATOM 102 OH TYR A 102 23.519 55.322 17.057 1.00 80.32 O ANISOU 102 OH TYR A 102 9182 10261 11075 750 -2124 -302 O ATOM 103 N ILE A 103 25.093 49.225 22.932 1.00 56.81 N ANISOU 103 N ILE A 103 5743 7401 8442 -593 -1325 -885 N ATOM 104 CA ILE A 103 25.092 48.430 24.159 1.00 51.51 C ANISOU 104 CA ILE A 103 4951 6762 7857 -767 -1172 -933 C ATOM 105 C ILE A 103 26.515 48.067 24.567 1.00 58.14 C ANISOU 105 C ILE A 103 6023 7477 8589 -828 -1000 -928 C ATOM 106 O ILE A 103 26.913 48.254 25.723 1.00 69.84 O ANISOU 106 O ILE A 103 7465 8950 10120 -851 -815 -936 O ATOM 107 CB ILE A 103 24.222 47.173 23.985 1.00 53.59 C ANISOU 107 CB ILE A 103 5081 7107 8174 -963 -1324 -975 C ATOM 108 CG1 ILE A 103 22.790 47.556 23.606 1.00 50.82 C ANISOU 108 CG1 ILE A 103 4444 6904 7963 -909 -1515 -963 C ATOM 109 CG2 ILE A 103 24.228 46.346 25.262 1.00 51.39 C ANISOU 109 CG2 ILE A 103 4692 6851 7982 -1141 -1144 -994 C ATOM 110 CD1 ILE A 103 21.874 46.366 23.452 1.00 52.85 C ANISOU 110 CD1 ILE A 103 4528 7239 8314 -1134 -1691 -995 C ATOM 111 N ASN A 104 27.304 47.537 23.627 1.00 55.04 N ANISOU 111 N ASN A 104 5878 6995 8040 -842 -1059 -913 N ATOM 112 CA ASN A 104 28.655 47.109 23.979 1.00 52.75 C ANISOU 112 CA ASN A 104 5773 6602 7667 -889 -896 -890 C ATOM 113 C ASN A 104 29.547 48.283 24.349 1.00 53.02 C ANISOU 113 C ASN A 104 5857 6571 7716 -773 -753 -830 C ATOM 114 O ASN A 104 30.458 48.126 25.166 1.00 60.93 O ANISOU 114 O ASN A 104 6899 7528 8725 -829 -606 -817 O ATOM 115 CB ASN A 104 29.293 46.317 22.840 1.00 55.04 C ANISOU 115 CB ASN A 104 6320 6812 7781 -890 -965 -881 C ATOM 116 CG ASN A 104 28.654 44.960 22.648 1.00 60.32 C ANISOU 116 CG ASN A 104 6994 7490 8433 -1048 -1095 -960 C ATOM 117 OD1 ASN A 104 27.433 44.823 22.723 1.00 65.95 O ANISOU 117 OD1 ASN A 104 7512 8293 9253 -1125 -1237 -1006 O ATOM 118 ND2 ASN A 104 29.474 43.946 22.410 1.00 53.65 N ANISOU 118 ND2 ASN A 104 6367 6544 7474 -1098 -1045 -972 N ATOM 119 N THR A 105 29.315 49.460 23.765 1.00 51.86 N ANISOU 119 N THR A 105 5715 6408 7582 -618 -807 -785 N ATOM 120 CA THR A 105 30.146 50.608 24.116 1.00 53.46 C ANISOU 120 CA THR A 105 5975 6515 7824 -532 -685 -727 C ATOM 121 C THR A 105 29.902 51.036 25.556 1.00 55.00 C ANISOU 121 C THR A 105 6022 6732 8145 -564 -582 -793 C ATOM 122 O THR A 105 30.848 51.370 26.279 1.00 54.35 O ANISOU 122 O THR A 105 5998 6572 8079 -597 -469 -784 O ATOM 123 CB THR A 105 29.885 51.772 23.161 1.00 51.34 C ANISOU 123 CB THR A 105 5762 6198 7548 -355 -767 -653 C ATOM 124 OG1 THR A 105 30.029 51.326 21.806 1.00 56.24 O ANISOU 124 OG1 THR A 105 6545 6815 8008 -311 -868 -595 O ATOM 125 CG2 THR A 105 30.878 52.893 23.427 1.00 45.17 C ANISOU 125 CG2 THR A 105 5071 5274 6817 -300 -644 -578 C ATOM 126 N VAL A 106 28.640 51.021 25.988 1.00 57.31 N ANISOU 126 N VAL A 106 6119 7135 8520 -550 -622 -857 N ATOM 127 CA VAL A 106 28.308 51.388 27.361 1.00 57.49 C ANISOU 127 CA VAL A 106 6017 7196 8632 -551 -499 -924 C ATOM 128 C VAL A 106 28.790 50.314 28.330 1.00 55.86 C ANISOU 128 C VAL A 106 5815 7024 8387 -722 -395 -955 C ATOM 129 O VAL A 106 29.392 50.617 29.367 1.00 53.21 O ANISOU 129 O VAL A 106 5524 6651 8044 -739 -282 -984 O ATOM 130 CB VAL A 106 26.796 51.635 27.498 1.00 55.64 C ANISOU 130 CB VAL A 106 5545 7091 8504 -467 -542 -958 C ATOM 131 CG1 VAL A 106 26.404 51.758 28.965 1.00 55.01 C ANISOU 131 CG1 VAL A 106 5342 7076 8482 -469 -376 -1026 C ATOM 132 CG2 VAL A 106 26.398 52.880 26.721 1.00 51.56 C ANISOU 132 CG2 VAL A 106 5037 6522 8032 -259 -630 -918 C ATOM 133 N VAL A 107 28.523 49.044 28.014 1.00 52.14 N ANISOU 133 N VAL A 107 5312 6613 7884 -849 -448 -949 N ATOM 134 CA VAL A 107 28.993 47.950 28.865 1.00 47.71 C ANISOU 134 CA VAL A 107 4777 6065 7285 -1003 -352 -956 C ATOM 135 C VAL A 107 30.511 47.998 29.005 1.00 54.76 C ANISOU 135 C VAL A 107 5858 6848 8099 -1013 -288 -917 C ATOM 136 O VAL A 107 31.057 47.882 30.109 1.00 63.97 O ANISOU 136 O VAL A 107 7041 8015 9249 -1064 -186 -926 O ATOM 137 CB VAL A 107 28.524 46.593 28.309 1.00 47.03 C ANISOU 137 CB VAL A 107 4671 6010 7187 -1139 -441 -953 C ATOM 138 CG1 VAL A 107 29.304 45.464 28.961 1.00 41.90 C ANISOU 138 CG1 VAL A 107 4121 5319 6480 -1273 -346 -934 C ATOM 139 CG2 VAL A 107 27.034 46.409 28.542 1.00 47.78 C ANISOU 139 CG2 VAL A 107 4515 6237 7403 -1183 -482 -978 C ATOM 140 N SER A 108 31.216 48.181 27.884 1.00 58.31 N ANISOU 140 N SER A 108 6446 7213 8497 -958 -347 -860 N ATOM 141 CA SER A 108 32.677 48.189 27.923 1.00 59.32 C ANISOU 141 CA SER A 108 6710 7251 8578 -967 -278 -794 C ATOM 142 C SER A 108 33.218 49.412 28.648 1.00 54.11 C ANISOU 142 C SER A 108 6045 6537 7977 -924 -227 -795 C ATOM 143 O SER A 108 34.268 49.334 29.294 1.00 50.19 O ANISOU 143 O SER A 108 5591 6004 7475 -980 -171 -766 O ATOM 144 CB SER A 108 33.245 48.119 26.508 1.00 61.63 C ANISOU 144 CB SER A 108 7144 7477 8795 -899 -320 -716 C ATOM 145 OG SER A 108 33.135 46.806 25.989 1.00 75.02 O ANISOU 145 OG SER A 108 8913 9185 10407 -955 -354 -727 O ATOM 146 N CYS A 109 32.523 50.545 28.551 1.00 55.04 N ANISOU 146 N CYS A 109 6117 6639 8158 -823 -261 -829 N ATOM 147 CA CYS A 109 32.907 51.704 29.346 1.00 57.06 C ANISOU 147 CA CYS A 109 6393 6815 8473 -788 -225 -861 C ATOM 148 C CYS A 109 32.635 51.461 30.823 1.00 57.30 C ANISOU 148 C CYS A 109 6368 6916 8488 -844 -158 -958 C ATOM 149 O CYS A 109 33.418 51.881 31.683 1.00 53.53 O ANISOU 149 O CYS A 109 5955 6379 8005 -881 -135 -985 O ATOM 150 CB CYS A 109 32.164 52.944 28.858 1.00 59.06 C ANISOU 150 CB CYS A 109 6635 7011 8796 -640 -271 -874 C ATOM 151 SG CYS A 109 32.786 53.613 27.308 1.00 63.24 S ANISOU 151 SG CYS A 109 7287 7414 9329 -559 -327 -731 S ATOM 152 N LEU A 110 31.537 50.771 31.134 1.00 58.96 N ANISOU 152 N LEU A 110 6459 7255 8687 -855 -131 -1004 N ATOM 153 CA LEU A 110 31.251 50.412 32.519 1.00 58.76 C ANISOU 153 CA LEU A 110 6390 7314 8622 -903 -35 -1070 C ATOM 154 C LEU A 110 32.311 49.464 33.065 1.00 57.32 C ANISOU 154 C LEU A 110 6288 7131 8359 -1032 -8 -1026 C ATOM 155 O LEU A 110 32.842 49.672 34.163 1.00 56.04 O ANISOU 155 O LEU A 110 6188 6963 8141 -1054 30 -1064 O ATOM 156 CB LEU A 110 29.863 49.785 32.614 1.00 57.19 C ANISOU 156 CB LEU A 110 6017 7258 8455 -906 4 -1086 C ATOM 157 CG LEU A 110 29.420 49.342 34.001 1.00 59.08 C ANISOU 157 CG LEU A 110 6196 7605 8645 -946 142 -1125 C ATOM 158 CD1 LEU A 110 29.539 50.488 34.994 1.00 60.06 C ANISOU 158 CD1 LEU A 110 6400 7694 8727 -829 213 -1217 C ATOM 159 CD2 LEU A 110 27.992 48.854 33.906 1.00 61.01 C ANISOU 159 CD2 LEU A 110 6222 7988 8972 -951 181 -1111 C ATOM 160 N VAL A 111 32.633 48.414 32.304 1.00 53.90 N ANISOU 160 N VAL A 111 5870 6698 7911 -1104 -39 -949 N ATOM 161 CA VAL A 111 33.637 47.446 32.739 1.00 48.05 C ANISOU 161 CA VAL A 111 5202 5949 7105 -1199 -10 -890 C ATOM 162 C VAL A 111 34.986 48.123 32.927 1.00 53.47 C ANISOU 162 C VAL A 111 5972 6552 7794 -1190 -37 -855 C ATOM 163 O VAL A 111 35.713 47.839 33.886 1.00 60.28 O ANISOU 163 O VAL A 111 6867 7429 8606 -1244 -22 -842 O ATOM 164 CB VAL A 111 33.731 46.285 31.734 1.00 41.18 C ANISOU 164 CB VAL A 111 4366 5061 6221 -1243 -37 -824 C ATOM 165 CG1 VAL A 111 34.956 45.436 32.024 1.00 34.55 C ANISOU 165 CG1 VAL A 111 3616 4185 5328 -1293 -3 -745 C ATOM 166 CG2 VAL A 111 32.470 45.440 31.781 1.00 38.12 C ANISOU 166 CG2 VAL A 111 3889 4748 5848 -1310 -30 -856 C ATOM 167 N PHE A 112 35.343 49.027 32.014 1.00 53.43 N ANISOU 167 N PHE A 112 5992 6458 7852 -1129 -85 -825 N ATOM 168 CA PHE A 112 36.615 49.728 32.126 1.00 49.69 C ANISOU 168 CA PHE A 112 5565 5894 7421 -1146 -114 -772 C ATOM 169 C PHE A 112 36.697 50.515 33.432 1.00 57.68 C ANISOU 169 C PHE A 112 6598 6890 8427 -1169 -139 -870 C ATOM 170 O PHE A 112 37.696 50.434 34.156 1.00 62.34 O ANISOU 170 O PHE A 112 7213 7471 9003 -1241 -175 -847 O ATOM 171 CB PHE A 112 36.803 50.644 30.918 1.00 42.16 C ANISOU 171 CB PHE A 112 4636 4839 6545 -1077 -141 -709 C ATOM 172 CG PHE A 112 38.166 51.263 30.822 1.00 35.73 C ANISOU 172 CG PHE A 112 3840 3925 5809 -1119 -158 -610 C ATOM 173 CD1 PHE A 112 39.246 50.527 30.365 1.00 38.90 C ANISOU 173 CD1 PHE A 112 4230 4339 6210 -1148 -119 -474 C ATOM 174 CD2 PHE A 112 38.365 52.590 31.166 1.00 36.70 C ANISOU 174 CD2 PHE A 112 3989 3933 6024 -1128 -211 -647 C ATOM 175 CE1 PHE A 112 40.508 51.101 30.267 1.00 35.98 C ANISOU 175 CE1 PHE A 112 3829 3895 5948 -1196 -126 -357 C ATOM 176 CE2 PHE A 112 39.621 53.171 31.070 1.00 37.34 C ANISOU 176 CE2 PHE A 112 4063 3913 6212 -1201 -241 -542 C ATOM 177 CZ PHE A 112 40.692 52.427 30.617 1.00 37.00 C ANISOU 177 CZ PHE A 112 3963 3910 6185 -1240 -196 -387 C ATOM 178 N VAL A 113 35.645 51.267 33.766 1.00 56.77 N ANISOU 178 N VAL A 113 6481 6775 8314 -1095 -127 -984 N ATOM 179 CA VAL A 113 35.687 52.101 34.966 1.00 54.69 C ANISOU 179 CA VAL A 113 6287 6473 8019 -1088 -146 -1102 C ATOM 180 C VAL A 113 35.556 51.244 36.222 1.00 50.38 C ANISOU 180 C VAL A 113 5754 6055 7335 -1134 -94 -1147 C ATOM 181 O VAL A 113 36.372 51.344 37.144 1.00 49.84 O ANISOU 181 O VAL A 113 5765 5971 7201 -1193 -152 -1173 O ATOM 182 CB VAL A 113 34.605 53.192 34.912 1.00 55.58 C ANISOU 182 CB VAL A 113 6410 6535 8173 -954 -123 -1207 C ATOM 183 CG1 VAL A 113 34.399 53.793 36.288 1.00 58.28 C ANISOU 183 CG1 VAL A 113 6850 6865 8428 -916 -105 -1359 C ATOM 184 CG2 VAL A 113 35.002 54.275 33.921 1.00 57.45 C ANISOU 184 CG2 VAL A 113 6688 6601 8538 -915 -193 -1158 C ATOM 185 N LEU A 114 34.518 50.405 36.283 1.00 46.74 N ANISOU 185 N LEU A 114 5213 5718 6828 -1112 5 -1146 N ATOM 186 CA LEU A 114 34.352 49.506 37.421 1.00 51.60 C ANISOU 186 CA LEU A 114 5843 6453 7311 -1158 81 -1152 C ATOM 187 C LEU A 114 35.575 48.619 37.602 1.00 57.67 C ANISOU 187 C LEU A 114 6654 7222 8035 -1260 27 -1049 C ATOM 188 O LEU A 114 36.077 48.444 38.719 1.00 66.59 O ANISOU 188 O LEU A 114 7864 8392 9047 -1291 11 -1063 O ATOM 189 CB LEU A 114 33.108 48.641 37.234 1.00 55.25 C ANISOU 189 CB LEU A 114 6182 7030 7782 -1155 193 -1124 C ATOM 190 CG LEU A 114 31.765 49.177 37.717 1.00 52.80 C ANISOU 190 CG LEU A 114 5795 6798 7467 -1050 304 -1212 C ATOM 191 CD1 LEU A 114 30.684 48.122 37.517 1.00 52.04 C ANISOU 191 CD1 LEU A 114 5536 6823 7415 -1100 398 -1145 C ATOM 192 CD2 LEU A 114 31.859 49.589 39.174 1.00 49.65 C ANISOU 192 CD2 LEU A 114 5518 6435 6912 -1001 375 -1301 C ATOM 193 N GLY A 115 36.067 48.046 36.503 1.00 54.88 N ANISOU 193 N GLY A 115 6257 6829 7764 -1293 -1 -940 N ATOM 194 CA GLY A 115 37.170 47.110 36.600 1.00 54.41 C ANISOU 194 CA GLY A 115 6222 6774 7677 -1356 -28 -826 C ATOM 195 C GLY A 115 38.472 47.758 37.007 1.00 54.67 C ANISOU 195 C GLY A 115 6289 6755 7728 -1385 -138 -806 C ATOM 196 O GLY A 115 39.270 47.146 37.723 1.00 56.46 O ANISOU 196 O GLY A 115 6537 7024 7890 -1427 -176 -743 O ATOM 197 N ILE A 116 38.713 48.991 36.561 1.00 52.79 N ANISOU 197 N ILE A 116 6050 6419 7589 -1371 -205 -846 N ATOM 198 CA ILE A 116 39.930 49.686 36.966 1.00 53.45 C ANISOU 198 CA ILE A 116 6149 6438 7723 -1433 -333 -827 C ATOM 199 C ILE A 116 39.872 50.041 38.445 1.00 51.90 C ANISOU 199 C ILE A 116 6053 6273 7393 -1456 -405 -954 C ATOM 200 O ILE A 116 40.834 49.816 39.187 1.00 52.10 O ANISOU 200 O ILE A 116 6093 6327 7374 -1523 -514 -916 O ATOM 201 CB ILE A 116 40.163 50.928 36.090 1.00 51.48 C ANISOU 201 CB ILE A 116 5885 6045 7630 -1429 -379 -824 C ATOM 202 CG1 ILE A 116 40.807 50.523 34.765 1.00 54.21 C ANISOU 202 CG1 ILE A 116 6145 6368 8083 -1421 -331 -651 C ATOM 203 CG2 ILE A 116 41.031 51.959 36.816 1.00 51.84 C ANISOU 203 CG2 ILE A 116 5973 5994 7729 -1516 -534 -874 C ATOM 204 CD1 ILE A 116 41.227 51.697 33.922 1.00 60.85 C ANISOU 204 CD1 ILE A 116 6972 7070 9080 -1428 -362 -598 C ATOM 205 N ILE A 117 38.741 50.591 38.897 1.00 53.01 N ANISOU 205 N ILE A 117 6268 6416 7456 -1386 -344 -1103 N ATOM 206 CA ILE A 117 38.589 50.909 40.315 1.00 59.78 C ANISOU 206 CA ILE A 117 7264 7310 8140 -1374 -382 -1237 C ATOM 207 C ILE A 117 38.594 49.632 41.144 1.00 51.37 C ANISOU 207 C ILE A 117 6214 6398 6905 -1389 -326 -1171 C ATOM 208 O ILE A 117 39.346 49.508 42.116 1.00 56.49 O ANISOU 208 O ILE A 117 6949 7083 7433 -1433 -439 -1176 O ATOM 209 CB ILE A 117 37.305 51.723 40.561 1.00 60.01 C ANISOU 209 CB ILE A 117 7363 7318 8121 -1254 -281 -1398 C ATOM 210 CG1 ILE A 117 37.351 53.061 39.823 1.00 54.38 C ANISOU 210 CG1 ILE A 117 6669 6422 7571 -1227 -351 -1458 C ATOM 211 CG2 ILE A 117 37.105 51.956 42.050 1.00 56.59 C ANISOU 211 CG2 ILE A 117 7105 6934 7461 -1212 -284 -1540 C ATOM 212 CD1 ILE A 117 36.078 53.870 39.961 1.00 43.54 C ANISOU 212 CD1 ILE A 117 5352 5018 6174 -1071 -243 -1601 C ATOM 213 N GLY A 118 37.762 48.660 40.759 1.00 41.80 N ANISOU 213 N GLY A 118 4924 5270 5688 -1360 -165 -1100 N ATOM 214 CA GLY A 118 37.570 47.482 41.592 1.00 43.64 C ANISOU 214 CA GLY A 118 5190 5628 5763 -1371 -81 -1033 C ATOM 215 C GLY A 118 38.826 46.646 41.748 1.00 51.65 C ANISOU 215 C GLY A 118 6204 6658 6764 -1435 -183 -892 C ATOM 216 O GLY A 118 39.169 46.219 42.853 1.00 65.94 O ANISOU 216 O GLY A 118 8109 8544 8403 -1441 -219 -869 O ATOM 217 N ASN A 119 39.519 46.381 40.641 1.00 50.21 N ANISOU 217 N ASN A 119 5918 6410 6750 -1463 -223 -783 N ATOM 218 CA ASN A 119 40.696 45.523 40.700 1.00 48.48 C ANISOU 218 CA ASN A 119 5670 6209 6540 -1491 -293 -629 C ATOM 219 C ASN A 119 41.907 46.250 41.272 1.00 50.03 C ANISOU 219 C ASN A 119 5871 6394 6746 -1535 -497 -634 C ATOM 220 O ASN A 119 42.778 45.611 41.876 1.00 51.40 O ANISOU 220 O ASN A 119 6043 6627 6861 -1547 -586 -528 O ATOM 221 CB ASN A 119 41.007 44.964 39.308 1.00 52.77 C ANISOU 221 CB ASN A 119 6114 6691 7246 -1477 -236 -512 C ATOM 222 CG ASN A 119 39.924 44.023 38.805 1.00 56.34 C ANISOU 222 CG ASN A 119 6577 7147 7682 -1459 -81 -500 C ATOM 223 OD1 ASN A 119 39.866 42.860 39.202 1.00 57.82 O ANISOU 223 OD1 ASN A 119 6807 7366 7796 -1464 -21 -417 O ATOM 224 ND2 ASN A 119 39.063 44.522 37.924 1.00 53.23 N ANISOU 224 ND2 ASN A 119 6147 6713 7366 -1445 -32 -576 N ATOM 225 N SER A 120 41.984 47.571 41.099 1.00 50.53 N ANISOU 225 N SER A 120 5936 6371 6891 -1565 -589 -747 N ATOM 226 CA SER A 120 43.044 48.333 41.750 1.00 52.63 C ANISOU 226 CA SER A 120 6218 6608 7170 -1641 -814 -775 C ATOM 227 C SER A 120 42.857 48.327 43.259 1.00 60.87 C ANISOU 227 C SER A 120 7437 7732 7957 -1633 -896 -884 C ATOM 228 O SER A 120 43.812 48.111 44.014 1.00 69.17 O ANISOU 228 O SER A 120 8501 8838 8941 -1679 -1076 -830 O ATOM 229 CB SER A 120 43.075 49.767 41.222 1.00 51.97 C ANISOU 229 CB SER A 120 6129 6377 7241 -1685 -887 -877 C ATOM 230 OG SER A 120 43.309 49.797 39.827 1.00 55.78 O ANISOU 230 OG SER A 120 6466 6792 7935 -1683 -807 -756 O ATOM 231 N THR A 121 41.625 48.567 43.717 1.00 63.24 N ANISOU 231 N THR A 121 7873 8052 8105 -1561 -763 -1028 N ATOM 232 CA THR A 121 41.340 48.486 45.145 1.00 65.74 C ANISOU 232 CA THR A 121 8385 8460 8135 -1522 -788 -1123 C ATOM 233 C THR A 121 41.580 47.076 45.662 1.00 60.55 C ANISOU 233 C THR A 121 7726 7937 7343 -1506 -741 -954 C ATOM 234 O THR A 121 42.102 46.892 46.767 1.00 64.54 O ANISOU 234 O THR A 121 8358 8519 7646 -1507 -877 -952 O ATOM 235 CB THR A 121 39.903 48.927 45.425 1.00 68.01 C ANISOU 235 CB THR A 121 8783 8756 8303 -1419 -591 -1277 C ATOM 236 OG1 THR A 121 39.701 50.247 44.905 1.00 69.10 O ANISOU 236 OG1 THR A 121 8931 8745 8577 -1412 -638 -1423 O ATOM 237 CG2 THR A 121 39.623 48.931 46.924 1.00 68.04 C ANISOU 237 CG2 THR A 121 9019 8857 7977 -1355 -591 -1379 C ATOM 238 N LEU A 122 41.227 46.068 44.861 1.00 51.97 N ANISOU 238 N LEU A 122 6517 6867 6363 -1489 -566 -811 N ATOM 239 CA LEU A 122 41.457 44.684 45.259 1.00 51.73 C ANISOU 239 CA LEU A 122 6497 6923 6235 -1472 -512 -636 C ATOM 240 C LEU A 122 42.943 44.403 45.455 1.00 55.40 C ANISOU 240 C LEU A 122 6908 7405 6736 -1501 -731 -509 C ATOM 241 O LEU A 122 43.332 43.726 46.412 1.00 67.42 O ANISOU 241 O LEU A 122 8522 9018 8078 -1474 -796 -421 O ATOM 242 CB LEU A 122 40.863 43.740 44.216 1.00 42.82 C ANISOU 242 CB LEU A 122 5259 5760 5249 -1464 -313 -528 C ATOM 243 CG LEU A 122 40.972 42.247 44.513 1.00 50.35 C ANISOU 243 CG LEU A 122 6244 6757 6131 -1447 -229 -346 C ATOM 244 CD1 LEU A 122 40.516 41.954 45.934 1.00 55.24 C ANISOU 244 CD1 LEU A 122 7031 7484 6472 -1419 -179 -346 C ATOM 245 CD2 LEU A 122 40.150 41.457 43.512 1.00 41.62 C ANISOU 245 CD2 LEU A 122 5070 5587 5158 -1460 -42 -293 C ATOM 246 N LEU A 123 43.791 44.909 44.560 1.00 56.02 N ANISOU 246 N LEU A 123 6828 7406 7050 -1549 -844 -477 N ATOM 247 CA LEU A 123 45.226 44.732 44.751 1.00 54.67 C ANISOU 247 CA LEU A 123 6557 7267 6949 -1579 -1057 -344 C ATOM 248 C LEU A 123 45.742 45.568 45.911 1.00 56.84 C ANISOU 248 C LEU A 123 6937 7580 7081 -1638 -1324 -457 C ATOM 249 O LEU A 123 46.732 45.193 46.550 1.00 58.76 O ANISOU 249 O LEU A 123 7150 7902 7273 -1647 -1522 -348 O ATOM 250 CB LEU A 123 45.981 45.092 43.473 1.00 56.18 C ANISOU 250 CB LEU A 123 6530 7373 7442 -1615 -1076 -261 C ATOM 251 CG LEU A 123 45.822 44.137 42.295 1.00 54.39 C ANISOU 251 CG LEU A 123 6210 7112 7344 -1540 -859 -123 C ATOM 252 CD1 LEU A 123 46.348 44.823 41.062 1.00 58.08 C ANISOU 252 CD1 LEU A 123 6511 7493 8062 -1569 -853 -86 C ATOM 253 CD2 LEU A 123 46.582 42.850 42.558 1.00 49.77 C ANISOU 253 CD2 LEU A 123 5586 6594 6731 -1465 -863 78 C ATOM 254 N TYR A 124 45.079 46.688 46.206 1.00 58.52 N ANISOU 254 N TYR A 124 7285 7732 7219 -1668 -1346 -678 N ATOM 255 CA TYR A 124 45.529 47.556 47.289 1.00 62.86 C ANISOU 255 CA TYR A 124 7984 8284 7615 -1726 -1617 -825 C ATOM 256 C TYR A 124 45.275 46.919 48.650 1.00 62.60 C ANISOU 256 C TYR A 124 8175 8390 7220 -1649 -1636 -834 C ATOM 257 O TYR A 124 46.155 46.921 49.518 1.00 65.79 O ANISOU 257 O TYR A 124 8639 8861 7498 -1683 -1909 -816 O ATOM 258 CB TYR A 124 44.830 48.914 47.189 1.00 65.21 C ANISOU 258 CB TYR A 124 8403 8446 7926 -1750 -1606 -1067 C ATOM 259 CG TYR A 124 45.200 49.910 48.272 1.00 69.00 C ANISOU 259 CG TYR A 124 9094 8884 8237 -1810 -1888 -1266 C ATOM 260 CD1 TYR A 124 44.544 49.912 49.500 1.00 74.97 C ANISOU 260 CD1 TYR A 124 10145 9715 8624 -1715 -1867 -1414 C ATOM 261 CD2 TYR A 124 46.191 50.860 48.060 1.00 70.95 C ANISOU 261 CD2 TYR A 124 9259 9007 8691 -1965 -2172 -1306 C ATOM 262 CE1 TYR A 124 44.874 50.821 50.488 1.00 80.62 C ANISOU 262 CE1 TYR A 124 11102 10380 9151 -1758 -2138 -1620 C ATOM 263 CE2 TYR A 124 46.528 51.776 49.044 1.00 78.12 C ANISOU 263 CE2 TYR A 124 10386 9850 9447 -2040 -2464 -1509 C ATOM 264 CZ TYR A 124 45.865 51.752 50.256 1.00 85.20 C ANISOU 264 CZ TYR A 124 11609 10818 9946 -1928 -2453 -1678 C ATOM 265 OH TYR A 124 46.195 52.660 51.237 1.00 96.30 O ANISOU 265 OH TYR A 124 13279 12146 11166 -1990 -2755 -1904 O ATOM 266 N ILE A 125 44.071 46.375 48.858 1.00 58.26 N ANISOU 266 N ILE A 125 7746 7891 6500 -1546 -1353 -851 N ATOM 267 CA ILE A 125 43.720 45.839 50.169 1.00 63.95 C ANISOU 267 CA ILE A 125 8703 8742 6854 -1463 -1326 -852 C ATOM 268 C ILE A 125 44.495 44.565 50.463 1.00 71.18 C ANISOU 268 C ILE A 125 9563 9760 7724 -1439 -1390 -602 C ATOM 269 O ILE A 125 44.743 44.236 51.629 1.00 79.54 O ANISOU 269 O ILE A 125 10807 10927 8486 -1390 -1506 -573 O ATOM 270 CB ILE A 125 42.201 45.610 50.279 1.00 54.17 C ANISOU 270 CB ILE A 125 7568 7533 5481 -1369 -976 -906 C ATOM 271 CG1 ILE A 125 41.751 44.449 49.395 1.00 51.77 C ANISOU 271 CG1 ILE A 125 7084 7229 5356 -1362 -729 -711 C ATOM 272 CG2 ILE A 125 41.449 46.873 49.912 1.00 53.84 C ANISOU 272 CG2 ILE A 125 7557 7387 5514 -1361 -910 -1137 C ATOM 273 CD1 ILE A 125 40.266 44.169 49.486 1.00 54.08 C ANISOU 273 CD1 ILE A 125 7428 7560 5561 -1301 -402 -737 C ATOM 274 N ILE A 126 44.898 43.831 49.428 1.00 66.63 N ANISOU 274 N ILE A 126 8752 9143 7420 -1453 -1316 -418 N ATOM 275 CA ILE A 126 45.723 42.654 49.664 1.00 66.67 C ANISOU 275 CA ILE A 126 8702 9223 7408 -1406 -1384 -176 C ATOM 276 C ILE A 126 47.164 43.059 49.945 1.00 70.81 C ANISOU 276 C ILE A 126 9119 9784 8000 -1459 -1751 -132 C ATOM 277 O ILE A 126 47.868 42.379 50.701 1.00 75.07 O ANISOU 277 O ILE A 126 9694 10427 8402 -1406 -1909 17 O ATOM 278 CB ILE A 126 45.617 41.685 48.474 1.00 51.47 C ANISOU 278 CB ILE A 126 6599 7226 5730 -1376 -1161 -6 C ATOM 279 CG1 ILE A 126 44.161 41.257 48.279 1.00 50.12 C ANISOU 279 CG1 ILE A 126 6524 7024 5495 -1353 -839 -47 C ATOM 280 CG2 ILE A 126 46.499 40.465 48.687 1.00 52.44 C ANISOU 280 CG2 ILE A 126 6676 7399 5850 -1298 -1221 247 C ATOM 281 CD1 ILE A 126 43.984 40.092 47.345 1.00 49.31 C ANISOU 281 CD1 ILE A 126 6323 6845 5566 -1326 -642 117 C ATOM 282 N TYR A 127 47.617 44.179 49.380 1.00 75.14 N ANISOU 282 N TYR A 127 9533 10249 8767 -1569 -1903 -249 N ATOM 283 CA TYR A 127 48.971 44.653 49.647 1.00 85.69 C ANISOU 283 CA TYR A 127 10735 11617 10208 -1656 -2270 -208 C ATOM 284 C TYR A 127 49.061 45.356 50.997 1.00 89.62 C ANISOU 284 C TYR A 127 11485 12168 10400 -1698 -2557 -387 C ATOM 285 O TYR A 127 49.989 45.103 51.772 1.00 91.72 O ANISOU 285 O TYR A 127 11745 12541 10564 -1705 -2853 -296 O ATOM 286 CB TYR A 127 49.430 45.586 48.523 1.00 91.77 C ANISOU 286 CB TYR A 127 11264 12260 11343 -1778 -2315 -243 C ATOM 287 CG TYR A 127 50.740 46.294 48.798 1.00101.73 C ANISOU 287 CG TYR A 127 12367 13533 12751 -1917 -2704 -223 C ATOM 288 CD1 TYR A 127 51.953 45.630 48.668 1.00106.15 C ANISOU 288 CD1 TYR A 127 12659 14190 13482 -1904 -2847 30 C ATOM 289 CD2 TYR A 127 50.763 47.631 49.181 1.00105.19 C ANISOU 289 CD2 TYR A 127 12917 13876 13176 -2063 -2933 -454 C ATOM 290 CE1 TYR A 127 53.154 46.276 48.919 1.00109.76 C ANISOU 290 CE1 TYR A 127 12924 14671 14108 -2050 -3218 66 C ATOM 291 CE2 TYR A 127 51.958 48.284 49.433 1.00107.58 C ANISOU 291 CE2 TYR A 127 13064 14173 13639 -2227 -3317 -436 C ATOM 292 CZ TYR A 127 53.149 47.602 49.299 1.00112.16 C ANISOU 292 CZ TYR A 127 13339 14873 14404 -2229 -3462 -169 C ATOM 293 OH TYR A 127 54.339 48.246 49.547 1.00120.80 O ANISOU 293 OH TYR A 127 14233 15975 15691 -2409 -3857 -133 O ATOM 294 N LYS A 128 48.104 46.239 51.300 1.00 88.07 N ANISOU 294 N LYS A 128 11522 11899 10042 -1711 -2481 -644 N ATOM 295 CA LYS A 128 48.222 47.053 52.506 1.00 91.69 C ANISOU 295 CA LYS A 128 12255 12375 10208 -1748 -2765 -855 C ATOM 296 C LYS A 128 47.873 46.258 53.758 1.00 91.96 C ANISOU 296 C LYS A 128 12570 12569 9801 -1610 -2739 -816 C ATOM 297 O LYS A 128 48.528 46.410 54.798 1.00 95.58 O ANISOU 297 O LYS A 128 13187 13110 10020 -1625 -3071 -856 O ATOM 298 CB LYS A 128 47.334 48.294 52.406 1.00 96.22 C ANISOU 298 CB LYS A 128 13008 12799 10754 -1776 -2677 -1147 C ATOM 299 CG LYS A 128 47.625 49.315 53.494 1.00107.39 C ANISOU 299 CG LYS A 128 14708 14175 11920 -1836 -3018 -1398 C ATOM 300 CD LYS A 128 46.549 50.383 53.595 1.00109.61 C ANISOU 300 CD LYS A 128 15248 14314 12083 -1790 -2867 -1692 C ATOM 301 CE LYS A 128 46.904 51.404 54.669 1.00115.52 C ANISOU 301 CE LYS A 128 16325 14993 12576 -1847 -3228 -1963 C ATOM 302 NZ LYS A 128 45.852 52.443 54.846 1.00119.47 N ANISOU 302 NZ LYS A 128 17118 15341 12933 -1761 -3069 -2262 N ATOM 303 N ASN A 129 46.847 45.417 53.687 1.00 84.95 N ANISOU 303 N ASN A 129 11753 11726 8799 -1482 -2357 -732 N ATOM 304 CA ASN A 129 46.376 44.670 54.848 1.00 80.67 C ANISOU 304 CA ASN A 129 11491 11325 7835 -1347 -2266 -675 C ATOM 305 C ASN A 129 47.182 43.383 54.972 1.00 84.59 C ANISOU 305 C ASN A 129 11867 11927 8348 -1297 -2341 -366 C ATOM 306 O ASN A 129 46.987 42.438 54.200 1.00 80.56 O ANISOU 306 O ASN A 129 11179 11391 8041 -1260 -2092 -168 O ATOM 307 CB ASN A 129 44.882 44.384 54.733 1.00 72.71 C ANISOU 307 CB ASN A 129 10590 10310 6727 -1252 -1815 -707 C ATOM 308 CG ASN A 129 44.053 45.650 54.687 1.00 73.50 C ANISOU 308 CG ASN A 129 10818 10316 6793 -1257 -1730 -1003 C ATOM 309 OD1 ASN A 129 44.204 46.536 55.530 1.00 80.41 O ANISOU 309 OD1 ASN A 129 11944 11187 7422 -1250 -1941 -1215 O ATOM 310 ND2 ASN A 129 43.177 45.750 53.693 1.00 66.82 N ANISOU 310 ND2 ASN A 129 9813 9383 6191 -1260 -1434 -1023 N ATOM 311 N LYS A 130 48.088 43.350 55.953 1.00 92.58 N ANISOU 311 N LYS A 130 12990 13048 9138 -1287 -2700 -328 N ATOM 312 CA LYS A 130 48.930 42.178 56.158 1.00 97.91 C ANISOU 312 CA LYS A 130 13556 13828 9817 -1214 -2810 -26 C ATOM 313 C LYS A 130 48.122 40.975 56.628 1.00 92.46 C ANISOU 313 C LYS A 130 13056 13202 8871 -1061 -2483 153 C ATOM 314 O LYS A 130 48.539 39.829 56.417 1.00 90.21 O ANISOU 314 O LYS A 130 12648 12939 8687 -986 -2427 430 O ATOM 315 CB LYS A 130 50.035 42.508 57.159 1.00109.49 C ANISOU 315 CB LYS A 130 15107 15410 11086 -1238 -3308 -39 C ATOM 316 CG LYS A 130 50.897 43.683 56.737 1.00116.20 C ANISOU 316 CG LYS A 130 15749 16183 12217 -1425 -3662 -196 C ATOM 317 CD LYS A 130 51.063 44.690 57.866 1.00122.28 C ANISOU 317 CD LYS A 130 16830 16982 12650 -1489 -4035 -459 C ATOM 318 CE LYS A 130 49.755 45.414 58.172 1.00120.06 C ANISOU 318 CE LYS A 130 16898 16617 12101 -1450 -3776 -751 C ATOM 319 NZ LYS A 130 49.288 46.265 57.039 1.00114.15 N ANISOU 319 NZ LYS A 130 15977 15677 11717 -1558 -3585 -906 N ATOM 320 N CYS A 131 46.979 41.208 57.273 1.00 89.62 N ANISOU 320 N CYS A 131 12996 12866 8190 -1006 -2254 12 N ATOM 321 CA CYS A 131 46.103 40.103 57.633 1.00 85.35 C ANISOU 321 CA CYS A 131 12606 12372 7453 -889 -1893 196 C ATOM 322 C CYS A 131 45.443 39.476 56.414 1.00 80.84 C ANISOU 322 C CYS A 131 11800 11675 7242 -924 -1529 301 C ATOM 323 O CYS A 131 45.023 38.317 56.482 1.00 78.50 O ANISOU 323 O CYS A 131 11543 11378 6906 -860 -1283 525 O ATOM 324 CB CYS A 131 45.031 40.573 58.615 1.00 91.40 C ANISOU 324 CB CYS A 131 13725 13207 7795 -816 -1711 27 C ATOM 325 SG CYS A 131 43.924 41.838 57.948 1.00 95.71 S ANISOU 325 SG CYS A 131 14233 13637 8494 -882 -1482 -301 S ATOM 326 N MET A 132 45.346 40.211 55.305 1.00 80.91 N ANISOU 326 N MET A 132 11582 11566 7596 -1028 -1503 148 N ATOM 327 CA MET A 132 44.707 39.712 54.094 1.00 74.92 C ANISOU 327 CA MET A 132 10618 10686 7161 -1065 -1194 215 C ATOM 328 C MET A 132 45.632 38.863 53.236 1.00 69.35 C ANISOU 328 C MET A 132 9669 9916 6763 -1063 -1259 433 C ATOM 329 O MET A 132 45.158 38.232 52.287 1.00 71.12 O ANISOU 329 O MET A 132 9771 10034 7217 -1076 -1013 513 O ATOM 330 CB MET A 132 44.173 40.880 53.261 1.00 70.69 C ANISOU 330 CB MET A 132 9968 10056 6836 -1153 -1134 -34 C ATOM 331 CG MET A 132 42.956 41.575 53.854 1.00 72.00 C ANISOU 331 CG MET A 132 10342 10255 6761 -1121 -943 -235 C ATOM 332 SD MET A 132 41.379 40.846 53.371 1.00 81.29 S ANISOU 332 SD MET A 132 11470 11403 8013 -1105 -460 -158 S ATOM 333 CE MET A 132 41.205 39.543 54.581 1.00 89.18 C ANISOU 333 CE MET A 132 12696 12523 8667 -1013 -323 94 C ATOM 334 N ARG A 133 46.926 38.829 53.539 1.00 72.02 N ANISOU 334 N ARG A 133 9938 10316 7110 -1040 -1587 530 N ATOM 335 CA ARG A 133 47.892 38.068 52.753 1.00 61.74 C ANISOU 335 CA ARG A 133 8390 8965 6102 -1003 -1645 745 C ATOM 336 C ARG A 133 47.801 36.597 53.131 1.00 71.24 C ANISOU 336 C ARG A 133 9710 10171 7188 -876 -1492 1013 C ATOM 337 O ARG A 133 48.308 36.175 54.171 1.00 81.22 O ANISOU 337 O ARG A 133 11114 11545 8201 -786 -1665 1148 O ATOM 338 CB ARG A 133 49.304 38.592 52.980 1.00 76.35 C ANISOU 338 CB ARG A 133 10084 10897 8027 -1022 -2054 770 C ATOM 339 CG ARG A 133 49.484 40.069 52.685 1.00 82.43 C ANISOU 339 CG ARG A 133 10756 11641 8923 -1170 -2239 519 C ATOM 340 CD ARG A 133 50.865 40.320 52.098 1.00 96.88 C ANISOU 340 CD ARG A 133 12255 13478 11077 -1217 -2504 622 C ATOM 341 NE ARG A 133 51.379 41.652 52.402 1.00107.43 N ANISOU 341 NE ARG A 133 13553 14829 12436 -1367 -2838 430 N ATOM 342 CZ ARG A 133 52.485 42.158 51.865 1.00113.13 C ANISOU 342 CZ ARG A 133 13964 15545 13474 -1462 -3071 485 C ATOM 343 NH1 ARG A 133 53.178 41.443 50.991 1.00116.11 N ANISOU 343 NH1 ARG A 133 14044 15921 14152 -1391 -2978 725 N ATOM 344 NH2 ARG A 133 52.895 43.376 52.193 1.00115.10 N ANISOU 344 NH2 ARG A 133 14204 15781 13746 -1627 -3386 303 N ATOM 345 N ASN A 134 47.157 35.807 52.282 1.00 65.59 N ANISOU 345 N ASN A 134 8952 9320 6651 -870 -1182 1091 N ATOM 346 CA ASN A 134 47.204 34.358 52.399 1.00 69.12 C ANISOU 346 CA ASN A 134 9480 9706 7077 -759 -1042 1359 C ATOM 347 C ASN A 134 47.110 33.763 51.003 1.00 68.94 C ANISOU 347 C ASN A 134 9295 9500 7399 -764 -843 1407 C ATOM 348 O ASN A 134 46.846 34.464 50.023 1.00 78.10 O ANISOU 348 O ASN A 134 10304 10600 8770 -854 -787 1235 O ATOM 349 CB ASN A 134 46.097 33.818 53.312 1.00 62.77 C ANISOU 349 CB ASN A 134 8958 8922 5970 -753 -818 1413 C ATOM 350 CG ASN A 134 44.778 34.522 53.105 1.00 71.33 C ANISOU 350 CG ASN A 134 10077 9990 7036 -873 -593 1190 C ATOM 351 OD1 ASN A 134 44.595 35.651 53.557 1.00 68.85 O ANISOU 351 OD1 ASN A 134 9809 9778 6573 -911 -695 982 O ATOM 352 ND2 ASN A 134 43.845 33.860 52.425 1.00 71.22 N ANISOU 352 ND2 ASN A 134 10041 9840 7178 -928 -294 1231 N ATOM 353 N GLY A 135 47.339 32.454 50.932 1.00 69.09 N ANISOU 353 N GLY A 135 9373 9420 7459 -653 -741 1644 N ATOM 354 CA GLY A 135 47.377 31.722 49.687 1.00 66.97 C ANISOU 354 CA GLY A 135 9006 8958 7480 -622 -572 1706 C ATOM 355 C GLY A 135 46.265 32.075 48.722 1.00 63.19 C ANISOU 355 C GLY A 135 8496 8370 7145 -765 -356 1509 C ATOM 356 O GLY A 135 46.510 32.583 47.624 1.00 61.05 O ANISOU 356 O GLY A 135 8047 8049 7101 -789 -365 1398 O ATOM 357 N PRO A 136 45.014 31.805 49.109 1.00 65.97 N ANISOU 357 N PRO A 136 9010 8688 7368 -859 -157 1478 N ATOM 358 CA PRO A 136 43.895 32.122 48.202 1.00 58.24 C ANISOU 358 CA PRO A 136 7975 7616 6536 -997 29 1301 C ATOM 359 C PRO A 136 43.811 33.592 47.830 1.00 59.83 C ANISOU 359 C PRO A 136 8026 7917 6789 -1069 -70 1058 C ATOM 360 O PRO A 136 43.484 33.918 46.684 1.00 71.59 O ANISOU 360 O PRO A 136 9398 9319 8485 -1127 -5 935 O ATOM 361 CB PRO A 136 42.662 31.672 48.999 1.00 59.68 C ANISOU 361 CB PRO A 136 8330 7804 6543 -1079 233 1345 C ATOM 362 CG PRO A 136 43.182 30.682 49.992 1.00 61.52 C ANISOU 362 CG PRO A 136 8739 8042 6595 -969 210 1600 C ATOM 363 CD PRO A 136 44.561 31.140 50.342 1.00 57.90 C ANISOU 363 CD PRO A 136 8215 7710 6076 -838 -78 1631 C ATOM 364 N ASN A 137 44.089 34.494 48.773 1.00 59.60 N ANISOU 364 N ASN A 137 8024 8055 6568 -1064 -235 982 N ATOM 365 CA ASN A 137 44.007 35.920 48.473 1.00 54.44 C ANISOU 365 CA ASN A 137 7258 7461 5965 -1134 -335 748 C ATOM 366 C ASN A 137 45.076 36.341 47.477 1.00 51.32 C ANISOU 366 C ASN A 137 6653 7024 5823 -1115 -487 736 C ATOM 367 O ASN A 137 44.810 37.148 46.577 1.00 58.66 O ANISOU 367 O ASN A 137 7463 7907 6917 -1180 -462 584 O ATOM 368 CB ASN A 137 44.126 36.738 49.757 1.00 62.74 C ANISOU 368 CB ASN A 137 8430 8673 6734 -1127 -498 662 C ATOM 369 CG ASN A 137 42.820 36.830 50.505 1.00 64.04 C ANISOU 369 CG ASN A 137 8768 8892 6672 -1155 -294 589 C ATOM 370 OD1 ASN A 137 41.819 36.239 50.100 1.00 61.57 O ANISOU 370 OD1 ASN A 137 8454 8505 6436 -1198 -38 624 O ATOM 371 ND2 ASN A 137 42.818 37.572 51.602 1.00 66.45 N ANISOU 371 ND2 ASN A 137 9224 9328 6697 -1129 -406 486 N ATOM 372 N ILE A 138 46.288 35.807 47.618 1.00 51.40 N ANISOU 372 N ILE A 138 6605 7055 5871 -1016 -635 914 N ATOM 373 CA ILE A 138 47.357 36.146 46.685 1.00 60.77 C ANISOU 373 CA ILE A 138 7562 8217 7312 -985 -749 941 C ATOM 374 C ILE A 138 47.019 35.646 45.286 1.00 61.04 C ANISOU 374 C ILE A 138 7537 8091 7565 -968 -531 946 C ATOM 375 O ILE A 138 47.285 36.327 44.289 1.00 65.56 O ANISOU 375 O ILE A 138 7952 8630 8328 -993 -536 868 O ATOM 376 CB ILE A 138 48.699 35.591 47.196 1.00 62.52 C ANISOU 376 CB ILE A 138 7709 8512 7532 -860 -941 1159 C ATOM 377 CG1 ILE A 138 49.228 36.460 48.331 1.00 67.08 C ANISOU 377 CG1 ILE A 138 8290 9255 7942 -908 -1241 1105 C ATOM 378 CG2 ILE A 138 49.729 35.522 46.083 1.00 65.95 C ANISOU 378 CG2 ILE A 138 7896 8899 8262 -783 -955 1258 C ATOM 379 CD1 ILE A 138 50.520 35.955 48.909 1.00 82.19 C ANISOU 379 CD1 ILE A 138 10111 11268 9848 -790 -1475 1324 C ATOM 380 N LEU A 139 46.413 34.458 45.188 1.00 58.12 N ANISOU 380 N LEU A 139 7313 7608 7161 -929 -343 1036 N ATOM 381 CA LEU A 139 45.931 33.977 43.897 1.00 56.54 C ANISOU 381 CA LEU A 139 7110 7239 7132 -931 -155 1003 C ATOM 382 C LEU A 139 44.846 34.893 43.342 1.00 57.95 C ANISOU 382 C LEU A 139 7261 7410 7346 -1070 -84 782 C ATOM 383 O LEU A 139 44.771 35.119 42.128 1.00 62.55 O ANISOU 383 O LEU A 139 7767 7909 8089 -1074 -24 709 O ATOM 384 CB LEU A 139 45.410 32.545 44.029 1.00 55.80 C ANISOU 384 CB LEU A 139 7206 7003 6991 -898 6 1129 C ATOM 385 CG LEU A 139 46.457 31.455 44.268 1.00 61.54 C ANISOU 385 CG LEU A 139 7978 7676 7729 -719 -24 1365 C ATOM 386 CD1 LEU A 139 45.797 30.120 44.552 1.00 62.25 C ANISOU 386 CD1 LEU A 139 8295 7601 7756 -716 133 1483 C ATOM 387 CD2 LEU A 139 47.372 31.337 43.069 1.00 66.76 C ANISOU 387 CD2 LEU A 139 8509 8258 8599 -587 -10 1400 C ATOM 388 N ILE A 140 43.999 35.434 44.219 1.00 54.92 N ANISOU 388 N ILE A 140 6946 7118 6802 -1163 -83 680 N ATOM 389 CA ILE A 140 42.991 36.394 43.782 1.00 54.66 C ANISOU 389 CA ILE A 140 6870 7093 6806 -1267 -25 478 C ATOM 390 C ILE A 140 43.648 37.686 43.315 1.00 55.14 C ANISOU 390 C ILE A 140 6783 7198 6971 -1273 -172 369 C ATOM 391 O ILE A 140 43.120 38.377 42.436 1.00 47.57 O ANISOU 391 O ILE A 140 5756 6194 6124 -1320 -126 239 O ATOM 392 CB ILE A 140 41.979 36.638 44.918 1.00 51.54 C ANISOU 392 CB ILE A 140 6585 6794 6203 -1328 38 413 C ATOM 393 CG1 ILE A 140 41.154 35.377 45.169 1.00 54.61 C ANISOU 393 CG1 ILE A 140 7091 7114 6543 -1358 226 532 C ATOM 394 CG2 ILE A 140 41.052 37.803 44.601 1.00 44.81 C ANISOU 394 CG2 ILE A 140 5670 5973 5384 -1398 77 204 C ATOM 395 CD1 ILE A 140 40.295 35.445 46.420 1.00 55.29 C ANISOU 395 CD1 ILE A 140 7291 7314 6403 -1392 323 531 C ATOM 396 N ALA A 141 44.811 38.026 43.874 1.00 58.67 N ANISOU 396 N ALA A 141 7173 7726 7394 -1233 -362 434 N ATOM 397 CA ALA A 141 45.497 39.252 43.478 1.00 55.03 C ANISOU 397 CA ALA A 141 6560 7288 7059 -1268 -514 352 C ATOM 398 C ALA A 141 46.034 39.147 42.055 1.00 63.21 C ANISOU 398 C ALA A 141 7451 8234 8331 -1223 -448 415 C ATOM 399 O ALA A 141 45.783 40.027 41.223 1.00 64.71 O ANISOU 399 O ALA A 141 7568 8380 8637 -1271 -425 306 O ATOM 400 CB ALA A 141 46.626 39.566 44.461 1.00 48.02 C ANISOU 400 CB ALA A 141 5631 6510 6103 -1259 -762 418 C ATOM 401 N SER A 142 46.778 38.074 41.758 1.00 64.09 N ANISOU 401 N SER A 142 7535 8313 8505 -1110 -404 597 N ATOM 402 CA SER A 142 47.247 37.847 40.394 1.00 62.54 C ANISOU 402 CA SER A 142 7239 8028 8495 -1030 -298 661 C ATOM 403 C SER A 142 46.079 37.805 39.421 1.00 59.20 C ANISOU 403 C SER A 142 6912 7495 8088 -1068 -131 531 C ATOM 404 O SER A 142 46.146 38.373 38.325 1.00 67.18 O ANISOU 404 O SER A 142 7846 8461 9217 -1062 -86 486 O ATOM 405 CB SER A 142 48.046 36.547 40.317 1.00 60.59 C ANISOU 405 CB SER A 142 7002 7742 8277 -869 -242 866 C ATOM 406 OG SER A 142 47.198 35.423 40.138 1.00 57.80 O ANISOU 406 OG SER A 142 6849 7264 7849 -840 -81 864 O ATOM 407 N LEU A 143 44.994 37.143 39.812 1.00 53.66 N ANISOU 407 N LEU A 143 6369 6752 7267 -1114 -45 481 N ATOM 408 CA LEU A 143 43.794 37.142 38.988 1.00 44.99 C ANISOU 408 CA LEU A 143 5336 5567 6190 -1176 74 352 C ATOM 409 C LEU A 143 43.274 38.561 38.773 1.00 48.00 C ANISOU 409 C LEU A 143 5635 6001 6601 -1259 23 190 C ATOM 410 O LEU A 143 42.831 38.907 37.674 1.00 55.30 O ANISOU 410 O LEU A 143 6541 6865 7607 -1264 75 114 O ATOM 411 CB LEU A 143 42.746 36.249 39.646 1.00 48.89 C ANISOU 411 CB LEU A 143 5973 6028 6574 -1240 160 351 C ATOM 412 CG LEU A 143 41.481 35.800 38.930 1.00 60.16 C ANISOU 412 CG LEU A 143 7471 7352 8035 -1319 273 263 C ATOM 413 CD1 LEU A 143 41.021 34.514 39.580 1.00 61.49 C ANISOU 413 CD1 LEU A 143 7777 7449 8137 -1355 357 363 C ATOM 414 CD2 LEU A 143 40.428 36.866 39.077 1.00 72.04 C ANISOU 414 CD2 LEU A 143 8905 8942 9524 -1419 267 107 C ATOM 415 N ALA A 144 43.330 39.407 39.803 1.00 55.91 N ANISOU 415 N ALA A 144 6610 7106 7526 -1310 -86 135 N ATOM 416 CA ALA A 144 42.911 40.794 39.625 1.00 50.06 C ANISOU 416 CA ALA A 144 5814 6386 6822 -1370 -138 -19 C ATOM 417 C ALA A 144 43.903 41.579 38.776 1.00 49.18 C ANISOU 417 C ALA A 144 5572 6244 6872 -1350 -210 14 C ATOM 418 O ALA A 144 43.501 42.487 38.040 1.00 47.46 O ANISOU 418 O ALA A 144 5318 5983 6732 -1374 -197 -79 O ATOM 419 CB ALA A 144 42.724 41.475 40.980 1.00 44.54 C ANISOU 419 CB ALA A 144 5167 5780 5976 -1417 -235 -105 C ATOM 420 N LEU A 145 45.193 41.251 38.862 1.00 45.88 N ANISOU 420 N LEU A 145 5068 5850 6514 -1299 -278 166 N ATOM 421 CA LEU A 145 46.178 41.900 38.007 1.00 47.22 C ANISOU 421 CA LEU A 145 5082 5998 6863 -1281 -312 239 C ATOM 422 C LEU A 145 45.997 41.486 36.553 1.00 49.83 C ANISOU 422 C LEU A 145 5425 6241 7269 -1197 -141 275 C ATOM 423 O LEU A 145 46.109 42.318 35.645 1.00 50.38 O ANISOU 423 O LEU A 145 5426 6272 7443 -1202 -117 261 O ATOM 424 CB LEU A 145 47.584 41.563 38.490 1.00 40.78 C ANISOU 424 CB LEU A 145 4134 5251 6109 -1238 -419 415 C ATOM 425 CG LEU A 145 48.721 42.216 37.714 1.00 52.08 C ANISOU 425 CG LEU A 145 5352 6681 7754 -1230 -446 532 C ATOM 426 CD1 LEU A 145 48.568 43.729 37.721 1.00 46.61 C ANISOU 426 CD1 LEU A 145 4612 5961 7136 -1371 -560 409 C ATOM 427 CD2 LEU A 145 50.055 41.808 38.301 1.00 53.62 C ANISOU 427 CD2 LEU A 145 5381 6969 8024 -1185 -567 719 C ATOM 428 N GLY A 146 45.700 40.206 36.318 1.00 50.11 N ANISOU 428 N GLY A 146 5571 6231 7239 -1117 -26 319 N ATOM 429 CA GLY A 146 45.448 39.752 34.962 1.00 45.38 C ANISOU 429 CA GLY A 146 5038 5534 6670 -1034 117 323 C ATOM 430 C GLY A 146 44.238 40.423 34.346 1.00 54.44 C ANISOU 430 C GLY A 146 6245 6644 7797 -1104 135 160 C ATOM 431 O GLY A 146 44.262 40.835 33.183 1.00 70.41 O ANISOU 431 O GLY A 146 8263 8620 9870 -1057 190 155 O ATOM 432 N ASP A 147 43.157 40.543 35.119 1.00 48.63 N ANISOU 432 N ASP A 147 5561 5935 6980 -1204 97 39 N ATOM 433 CA ASP A 147 41.982 41.234 34.603 1.00 44.42 C ANISOU 433 CA ASP A 147 5048 5384 6446 -1256 103 -104 C ATOM 434 C ASP A 147 42.262 42.713 34.389 1.00 48.65 C ANISOU 434 C ASP A 147 5488 5935 7061 -1274 36 -142 C ATOM 435 O ASP A 147 41.697 43.324 33.476 1.00 52.68 O ANISOU 435 O ASP A 147 6005 6405 7605 -1261 54 -203 O ATOM 436 CB ASP A 147 40.791 41.049 35.543 1.00 39.13 C ANISOU 436 CB ASP A 147 4421 4758 5689 -1343 104 -202 C ATOM 437 CG ASP A 147 40.423 39.594 35.728 1.00 52.97 C ANISOU 437 CG ASP A 147 6273 6468 7386 -1355 176 -152 C ATOM 438 OD1 ASP A 147 39.402 39.309 36.386 1.00 55.21 O ANISOU 438 OD1 ASP A 147 6580 6782 7615 -1433 208 -202 O ATOM 439 OD2 ASP A 147 41.168 38.728 35.223 1.00 59.12 O ANISOU 439 OD2 ASP A 147 7108 7174 8182 -1280 212 -52 O ATOM 440 N LEU A 148 43.132 43.302 35.206 1.00 47.73 N ANISOU 440 N LEU A 148 5293 5866 6978 -1307 -58 -102 N ATOM 441 CA LEU A 148 43.472 44.705 35.017 1.00 49.80 C ANISOU 441 CA LEU A 148 5477 6106 7340 -1346 -134 -131 C ATOM 442 C LEU A 148 44.266 44.909 33.733 1.00 55.34 C ANISOU 442 C LEU A 148 6108 6755 8163 -1283 -70 -6 C ATOM 443 O LEU A 148 44.091 45.920 33.045 1.00 58.85 O ANISOU 443 O LEU A 148 6536 7144 8679 -1292 -70 -32 O ATOM 444 CB LEU A 148 44.257 45.213 36.221 1.00 47.06 C ANISOU 444 CB LEU A 148 5072 5807 7001 -1418 -283 -124 C ATOM 445 CG LEU A 148 44.275 46.724 36.435 1.00 45.98 C ANISOU 445 CG LEU A 148 4914 5621 6937 -1498 -397 -221 C ATOM 446 CD1 LEU A 148 42.858 47.279 36.526 1.00 45.35 C ANISOU 446 CD1 LEU A 148 4941 5513 6777 -1492 -360 -401 C ATOM 447 CD2 LEU A 148 45.059 47.058 37.691 1.00 51.91 C ANISOU 447 CD2 LEU A 148 5640 6416 7668 -1580 -580 -230 C ATOM 448 N LEU A 149 45.133 43.952 33.387 1.00 55.17 N ANISOU 448 N LEU A 149 6055 6746 8160 -1200 3 142 N ATOM 449 CA LEU A 149 45.910 44.059 32.155 1.00 46.99 C ANISOU 449 CA LEU A 149 4960 5675 7220 -1109 109 279 C ATOM 450 C LEU A 149 45.006 44.020 30.930 1.00 51.20 C ANISOU 450 C LEU A 149 5628 6143 7683 -1042 208 211 C ATOM 451 O LEU A 149 45.185 44.799 29.987 1.00 52.66 O ANISOU 451 O LEU A 149 5792 6291 7927 -1010 256 259 O ATOM 452 CB LEU A 149 46.951 42.941 32.092 1.00 44.84 C ANISOU 452 CB LEU A 149 4640 5434 6965 -995 190 445 C ATOM 453 CG LEU A 149 48.133 43.115 33.045 1.00 49.58 C ANISOU 453 CG LEU A 149 5049 6113 7675 -1041 78 568 C ATOM 454 CD1 LEU A 149 49.023 41.884 33.053 1.00 50.09 C ANISOU 454 CD1 LEU A 149 5072 6212 7747 -895 161 733 C ATOM 455 CD2 LEU A 149 48.930 44.348 32.658 1.00 52.85 C ANISOU 455 CD2 LEU A 149 5279 6527 8273 -1106 44 660 C ATOM 456 N HIS A 150 44.027 43.114 30.921 1.00 44.22 N ANISOU 456 N HIS A 150 4886 5241 6675 -1027 229 109 N ATOM 457 CA HIS A 150 43.088 43.078 29.807 1.00 40.21 C ANISOU 457 CA HIS A 150 4504 4677 6096 -982 272 27 C ATOM 458 C HIS A 150 42.277 44.364 29.726 1.00 47.44 C ANISOU 458 C HIS A 150 5390 5592 7043 -1046 195 -72 C ATOM 459 O HIS A 150 41.992 44.858 28.629 1.00 59.63 O ANISOU 459 O HIS A 150 6985 7097 8576 -987 221 -70 O ATOM 460 CB HIS A 150 42.158 41.873 29.929 1.00 36.13 C ANISOU 460 CB HIS A 150 4121 4133 5473 -996 274 -66 C ATOM 461 CG HIS A 150 40.883 42.023 29.158 1.00 46.13 C ANISOU 461 CG HIS A 150 5476 5368 6682 -1014 238 -192 C ATOM 462 ND1 HIS A 150 40.844 42.059 27.780 1.00 50.44 N ANISOU 462 ND1 HIS A 150 6128 5862 7174 -915 274 -184 N ATOM 463 CD2 HIS A 150 39.602 42.161 29.572 1.00 51.31 C ANISOU 463 CD2 HIS A 150 6117 6051 7327 -1111 164 -318 C ATOM 464 CE1 HIS A 150 39.595 42.205 27.380 1.00 52.85 C ANISOU 464 CE1 HIS A 150 6481 6163 7438 -959 191 -305 C ATOM 465 NE2 HIS A 150 38.820 42.268 28.448 1.00 50.67 N ANISOU 465 NE2 HIS A 150 6112 5937 7204 -1078 130 -383 N ATOM 466 N ILE A 151 41.910 44.930 30.876 1.00 46.40 N ANISOU 466 N ILE A 151 5194 5498 6937 -1146 105 -155 N ATOM 467 CA ILE A 151 41.023 46.090 30.890 1.00 45.28 C ANISOU 467 CA ILE A 151 5042 5342 6821 -1181 43 -266 C ATOM 468 C ILE A 151 41.718 47.318 30.305 1.00 45.71 C ANISOU 468 C ILE A 151 5047 5336 6986 -1167 35 -187 C ATOM 469 O ILE A 151 41.140 48.047 29.491 1.00 48.71 O ANISOU 469 O ILE A 151 5464 5667 7375 -1123 35 -211 O ATOM 470 CB ILE A 151 40.525 46.355 32.320 1.00 46.81 C ANISOU 470 CB ILE A 151 5210 5585 6992 -1264 -27 -377 C ATOM 471 CG1 ILE A 151 39.440 45.348 32.709 1.00 43.59 C ANISOU 471 CG1 ILE A 151 4847 5228 6487 -1283 5 -453 C ATOM 472 CG2 ILE A 151 39.997 47.768 32.453 1.00 45.49 C ANISOU 472 CG2 ILE A 151 5030 5379 6877 -1275 -85 -472 C ATOM 473 CD1 ILE A 151 39.142 45.322 34.192 1.00 44.77 C ANISOU 473 CD1 ILE A 151 4988 5446 6577 -1344 -17 -520 C ATOM 474 N VAL A 152 42.961 47.574 30.715 1.00 42.90 N ANISOU 474 N VAL A 152 4596 4978 6725 -1209 19 -78 N ATOM 475 CA VAL A 152 43.610 48.809 30.283 1.00 44.93 C ANISOU 475 CA VAL A 152 4788 5161 7121 -1236 3 6 C ATOM 476 C VAL A 152 44.183 48.675 28.874 1.00 51.14 C ANISOU 476 C VAL A 152 5578 5923 7929 -1133 141 173 C ATOM 477 O VAL A 152 44.299 49.672 28.152 1.00 46.28 O ANISOU 477 O VAL A 152 4960 5233 7391 -1124 165 241 O ATOM 478 CB VAL A 152 44.692 49.236 31.293 1.00 46.81 C ANISOU 478 CB VAL A 152 4902 5404 7480 -1353 -99 57 C ATOM 479 CG1 VAL A 152 44.158 49.143 32.721 1.00 52.14 C ANISOU 479 CG1 VAL A 152 5619 6122 8068 -1424 -221 -108 C ATOM 480 CG2 VAL A 152 45.956 48.395 31.134 1.00 37.87 C ANISOU 480 CG2 VAL A 152 3651 4336 6402 -1320 -33 245 C ATOM 481 N ILE A 153 44.522 47.462 28.448 1.00 51.62 N ANISOU 481 N ILE A 153 5670 6035 7909 -1039 245 243 N ATOM 482 CA ILE A 153 45.171 47.273 27.156 1.00 48.81 C ANISOU 482 CA ILE A 153 5338 5663 7543 -911 404 406 C ATOM 483 C ILE A 153 44.154 47.002 26.057 1.00 48.30 C ANISOU 483 C ILE A 153 5468 5571 7313 -802 446 328 C ATOM 484 O ILE A 153 44.257 47.556 24.960 1.00 49.36 O ANISOU 484 O ILE A 153 5660 5668 7428 -719 527 419 O ATOM 485 CB ILE A 153 46.210 46.136 27.245 1.00 47.13 C ANISOU 485 CB ILE A 153 5067 5507 7333 -833 506 532 C ATOM 486 CG1 ILE A 153 47.327 46.501 28.221 1.00 38.83 C ANISOU 486 CG1 ILE A 153 3790 4499 6465 -939 439 641 C ATOM 487 CG2 ILE A 153 46.790 45.818 25.872 1.00 44.32 C ANISOU 487 CG2 ILE A 153 4774 5141 6925 -657 710 686 C ATOM 488 CD1 ILE A 153 48.272 45.351 28.510 1.00 39.55 C ANISOU 488 CD1 ILE A 153 3801 4660 6568 -852 510 762 C ATOM 489 N ASP A 154 43.157 46.165 26.330 1.00 40.92 N ANISOU 489 N ASP A 154 4637 4653 6257 -808 383 170 N ATOM 490 CA ASP A 154 42.280 45.653 25.288 1.00 36.16 C ANISOU 490 CA ASP A 154 4217 4027 5494 -715 393 96 C ATOM 491 C ASP A 154 40.969 46.420 25.161 1.00 45.82 C ANISOU 491 C ASP A 154 5468 5242 6698 -755 268 -33 C ATOM 492 O ASP A 154 40.469 46.605 24.047 1.00 54.47 O ANISOU 492 O ASP A 154 6684 6316 7696 -665 262 -37 O ATOM 493 CB ASP A 154 41.979 44.174 25.550 1.00 35.89 C ANISOU 493 CB ASP A 154 4280 3997 5361 -709 392 15 C ATOM 494 CG ASP A 154 43.233 43.347 25.713 1.00 46.31 C ANISOU 494 CG ASP A 154 5577 5318 6699 -637 517 145 C ATOM 495 OD1 ASP A 154 44.310 43.795 25.261 1.00 40.72 O ANISOU 495 OD1 ASP A 154 4796 4620 6054 -557 631 309 O ATOM 496 OD2 ASP A 154 43.143 42.245 26.291 1.00 39.23 O ANISOU 496 OD2 ASP A 154 4727 4412 5768 -654 507 99 O ATOM 497 N ILE A 155 40.392 46.867 26.270 1.00 41.21 N ANISOU 497 N ILE A 155 4781 4681 6195 -867 170 -135 N ATOM 498 CA ILE A 155 39.030 47.402 26.266 1.00 45.28 C ANISOU 498 CA ILE A 155 5302 5206 6698 -884 64 -265 C ATOM 499 C ILE A 155 38.917 48.670 25.422 1.00 48.45 C ANISOU 499 C ILE A 155 5726 5552 7129 -810 50 -209 C ATOM 500 O ILE A 155 38.032 48.731 24.554 1.00 50.92 O ANISOU 500 O ILE A 155 6118 5869 7359 -737 -6 -248 O ATOM 501 CB ILE A 155 38.524 47.653 27.695 1.00 46.44 C ANISOU 501 CB ILE A 155 5342 5391 6913 -989 3 -374 C ATOM 502 CG1 ILE A 155 38.331 46.322 28.427 1.00 47.91 C ANISOU 502 CG1 ILE A 155 5530 5632 7043 -1054 15 -424 C ATOM 503 CG2 ILE A 155 37.243 48.484 27.665 1.00 46.40 C ANISOU 503 CG2 ILE A 155 5308 5393 6927 -968 -76 -479 C ATOM 504 CD1 ILE A 155 36.886 45.921 28.640 1.00 49.93 C ANISOU 504 CD1 ILE A 155 5769 5937 7266 -1095 -42 -549 C ATOM 505 N PRO A 156 39.756 49.702 25.612 1.00 40.43 N ANISOU 505 N PRO A 156 4649 4476 6235 -832 84 -111 N ATOM 506 CA PRO A 156 39.593 50.902 24.769 1.00 42.88 C ANISOU 506 CA PRO A 156 5005 4709 6579 -760 78 -40 C ATOM 507 C PRO A 156 39.684 50.602 23.283 1.00 51.25 C ANISOU 507 C PRO A 156 6202 5769 7500 -625 147 67 C ATOM 508 O PRO A 156 38.923 51.169 22.489 1.00 50.21 O ANISOU 508 O PRO A 156 6155 5616 7308 -536 91 65 O ATOM 509 CB PRO A 156 40.733 51.818 25.239 1.00 39.39 C ANISOU 509 CB PRO A 156 4474 4184 6307 -841 117 74 C ATOM 510 CG PRO A 156 41.067 51.350 26.601 1.00 42.35 C ANISOU 510 CG PRO A 156 4750 4607 6735 -961 74 -9 C ATOM 511 CD PRO A 156 40.870 49.868 26.567 1.00 45.62 C ANISOU 511 CD PRO A 156 5197 5122 7014 -930 109 -51 C ATOM 512 N ILE A 157 40.589 49.708 22.889 1.00 52.04 N ANISOU 512 N ILE A 157 6343 5897 7533 -588 267 161 N ATOM 513 CA ILE A 157 40.720 49.342 21.484 1.00 46.47 C ANISOU 513 CA ILE A 157 5811 5193 6652 -435 352 251 C ATOM 514 C ILE A 157 39.504 48.547 21.024 1.00 52.56 C ANISOU 514 C ILE A 157 6721 6005 7246 -389 226 89 C ATOM 515 O ILE A 157 38.940 48.806 19.953 1.00 59.56 O ANISOU 515 O ILE A 157 7752 6885 7994 -279 177 98 O ATOM 516 CB ILE A 157 42.028 48.563 21.262 1.00 46.75 C ANISOU 516 CB ILE A 157 5851 5246 6666 -382 537 389 C ATOM 517 CG1 ILE A 157 43.205 49.534 21.179 1.00 49.17 C ANISOU 517 CG1 ILE A 157 6033 5514 7137 -396 671 609 C ATOM 518 CG2 ILE A 157 41.941 47.684 20.025 1.00 51.16 C ANISOU 518 CG2 ILE A 157 6644 5817 6978 -212 611 395 C ATOM 519 CD1 ILE A 157 44.538 48.863 21.024 1.00 49.51 C ANISOU 519 CD1 ILE A 157 6015 5594 7201 -336 867 775 C ATOM 520 N ASN A 158 39.078 47.571 21.830 1.00 51.81 N ANISOU 520 N ASN A 158 6583 5948 7156 -482 160 -53 N ATOM 521 CA ASN A 158 37.918 46.763 21.470 1.00 46.29 C ANISOU 521 CA ASN A 158 5986 5274 6328 -482 23 -204 C ATOM 522 C ASN A 158 36.662 47.615 21.329 1.00 46.45 C ANISOU 522 C ASN A 158 5955 5320 6375 -484 -140 -278 C ATOM 523 O ASN A 158 35.764 47.270 20.552 1.00 50.39 O ANISOU 523 O ASN A 158 6555 5841 6749 -442 -272 -352 O ATOM 524 CB ASN A 158 37.714 45.658 22.505 1.00 44.69 C ANISOU 524 CB ASN A 158 5719 5092 6169 -608 -2 -312 C ATOM 525 CG ASN A 158 38.758 44.555 22.395 1.00 52.68 C ANISOU 525 CG ASN A 158 6834 6068 7113 -563 133 -254 C ATOM 526 OD1 ASN A 158 39.648 44.615 21.547 1.00 60.39 O ANISOU 526 OD1 ASN A 158 7917 7018 8010 -429 261 -133 O ATOM 527 ND2 ASN A 158 38.654 43.543 23.253 1.00 48.60 N ANISOU 527 ND2 ASN A 158 6289 5549 6628 -658 121 -324 N ATOM 528 N VAL A 159 36.580 48.722 22.069 1.00 44.63 N ANISOU 528 N VAL A 159 5572 5081 6305 -525 -144 -261 N ATOM 529 CA VAL A 159 35.468 49.650 21.896 1.00 46.27 C ANISOU 529 CA VAL A 159 5731 5300 6550 -482 -273 -307 C ATOM 530 C VAL A 159 35.524 50.281 20.513 1.00 53.51 C ANISOU 530 C VAL A 159 6802 6179 7349 -328 -285 -192 C ATOM 531 O VAL A 159 34.524 50.313 19.784 1.00 58.41 O ANISOU 531 O VAL A 159 7478 6839 7875 -254 -433 -238 O ATOM 532 CB VAL A 159 35.484 50.719 23.003 1.00 50.83 C ANISOU 532 CB VAL A 159 6157 5843 7313 -534 -253 -320 C ATOM 533 CG1 VAL A 159 34.469 51.809 22.709 1.00 47.16 C ANISOU 533 CG1 VAL A 159 5663 5364 6893 -440 -356 -338 C ATOM 534 CG2 VAL A 159 35.206 50.094 24.352 1.00 51.26 C ANISOU 534 CG2 VAL A 159 6083 5957 7437 -663 -255 -443 C ATOM 535 N TYR A 160 36.699 50.780 20.126 1.00 53.34 N ANISOU 535 N TYR A 160 6846 6088 7333 -278 -132 -26 N ATOM 536 CA TYR A 160 36.835 51.398 18.813 1.00 55.33 C ANISOU 536 CA TYR A 160 7263 6303 7458 -123 -106 118 C ATOM 537 C TYR A 160 36.672 50.368 17.705 1.00 49.60 C ANISOU 537 C TYR A 160 6749 5628 6468 -24 -137 93 C ATOM 538 O TYR A 160 35.988 50.622 16.708 1.00 50.16 O ANISOU 538 O TYR A 160 6961 5716 6383 97 -254 103 O ATOM 539 CB TYR A 160 38.184 52.104 18.683 1.00 59.97 C ANISOU 539 CB TYR A 160 7849 6806 8132 -112 95 328 C ATOM 540 CG TYR A 160 38.288 52.889 17.399 1.00 64.75 C ANISOU 540 CG TYR A 160 8621 7363 8619 47 144 507 C ATOM 541 CD1 TYR A 160 37.716 54.148 17.292 1.00 68.16 C ANISOU 541 CD1 TYR A 160 9042 7718 9137 90 62 556 C ATOM 542 CD2 TYR A 160 38.931 52.361 16.284 1.00 69.80 C ANISOU 542 CD2 TYR A 160 9451 8028 9043 176 282 632 C ATOM 543 CE1 TYR A 160 37.793 54.869 16.117 1.00 72.89 C ANISOU 543 CE1 TYR A 160 9810 8266 9618 243 108 742 C ATOM 544 CE2 TYR A 160 39.014 53.075 15.107 1.00 71.50 C ANISOU 544 CE2 TYR A 160 9840 8207 9119 334 342 813 C ATOM 545 CZ TYR A 160 38.443 54.327 15.031 1.00 77.97 C ANISOU 545 CZ TYR A 160 10641 8950 10034 360 249 875 C ATOM 546 OH TYR A 160 38.520 55.039 13.861 1.00 90.86 O ANISOU 546 OH TYR A 160 12463 10540 11520 525 310 1077 O ATOM 547 N LYS A 161 37.303 49.200 17.862 1.00 49.29 N ANISOU 547 N LYS A 161 6756 5604 6368 -61 -44 57 N ATOM 548 CA LYS A 161 37.209 48.143 16.858 1.00 48.41 C ANISOU 548 CA LYS A 161 6889 5510 5994 36 -68 7 C ATOM 549 C LYS A 161 35.755 47.839 16.505 1.00 47.89 C ANISOU 549 C LYS A 161 6876 5490 5831 21 -344 -161 C ATOM 550 O LYS A 161 35.400 47.710 15.328 1.00 56.38 O ANISOU 550 O LYS A 161 8177 6574 6670 148 -439 -165 O ATOM 551 CB LYS A 161 37.922 46.891 17.374 1.00 46.50 C ANISOU 551 CB LYS A 161 6657 5257 5754 -21 46 -42 C ATOM 552 CG LYS A 161 37.964 45.730 16.402 1.00 49.56 C ANISOU 552 CG LYS A 161 7335 5623 5873 89 46 -107 C ATOM 553 CD LYS A 161 38.621 44.538 17.078 1.00 51.76 C ANISOU 553 CD LYS A 161 7603 5867 6196 34 156 -154 C ATOM 554 CE LYS A 161 38.054 43.214 16.599 1.00 58.17 C ANISOU 554 CE LYS A 161 8659 6627 6816 41 32 -331 C ATOM 555 NZ LYS A 161 38.876 42.616 15.515 1.00 61.41 N ANISOU 555 NZ LYS A 161 9380 6983 6970 255 197 -279 N ATOM 556 N LEU A 162 34.890 47.755 17.516 1.00 57.14 N ANISOU 556 N LEU A 162 7831 6698 7181 -130 -477 -291 N ATOM 557 CA LEU A 162 33.485 47.456 17.262 1.00 59.50 C ANISOU 557 CA LEU A 162 8113 7057 7439 -168 -741 -434 C ATOM 558 C LEU A 162 32.803 48.567 16.478 1.00 63.06 C ANISOU 558 C LEU A 162 8582 7538 7841 -35 -876 -369 C ATOM 559 O LEU A 162 31.836 48.313 15.751 1.00 67.90 O ANISOU 559 O LEU A 162 9267 8203 8330 -3 -1110 -446 O ATOM 560 CB LEU A 162 32.753 47.234 18.585 1.00 58.14 C ANISOU 560 CB LEU A 162 7667 6931 7493 -347 -803 -548 C ATOM 561 CG LEU A 162 31.320 46.708 18.511 1.00 63.94 C ANISOU 561 CG LEU A 162 8314 7738 8243 -434 -1056 -688 C ATOM 562 CD1 LEU A 162 31.303 45.186 18.526 1.00 70.16 C ANISOU 562 CD1 LEU A 162 9210 8489 8958 -561 -1102 -802 C ATOM 563 CD2 LEU A 162 30.479 47.273 19.641 1.00 64.61 C ANISOU 563 CD2 LEU A 162 8085 7896 8569 -518 -1083 -723 C ATOM 564 N LEU A 163 33.279 49.800 16.617 1.00 60.17 N ANISOU 564 N LEU A 163 8155 7131 7576 38 -751 -224 N ATOM 565 CA LEU A 163 32.568 50.942 16.066 1.00 53.48 C ANISOU 565 CA LEU A 163 7300 6293 6728 166 -875 -152 C ATOM 566 C LEU A 163 33.060 51.345 14.687 1.00 58.37 C ANISOU 566 C LEU A 163 8194 6877 7106 355 -833 8 C ATOM 567 O LEU A 163 32.321 52.015 13.956 1.00 60.76 O ANISOU 567 O LEU A 163 8555 7204 7327 485 -993 57 O ATOM 568 CB LEU A 163 32.680 52.132 17.021 1.00 46.97 C ANISOU 568 CB LEU A 163 6276 5410 6161 142 -780 -93 C ATOM 569 CG LEU A 163 31.885 52.000 18.323 1.00 49.23 C ANISOU 569 CG LEU A 163 6296 5750 6658 10 -844 -246 C ATOM 570 CD1 LEU A 163 32.227 53.137 19.265 1.00 44.20 C ANISOU 570 CD1 LEU A 163 5535 5025 6233 -1 -724 -201 C ATOM 571 CD2 LEU A 163 30.389 51.970 18.034 1.00 46.47 C ANISOU 571 CD2 LEU A 163 5845 5506 6307 53 -1091 -334 C ATOM 572 N ALA A 164 34.266 50.935 14.308 1.00 61.27 N ANISOU 572 N ALA A 164 8730 7198 7350 389 -616 102 N ATOM 573 CA ALA A 164 34.867 51.306 13.037 1.00 57.69 C ANISOU 573 CA ALA A 164 8547 6717 6657 580 -510 283 C ATOM 574 C ALA A 164 35.328 50.052 12.312 1.00 64.49 C ANISOU 574 C ALA A 164 9667 7599 7238 638 -456 226 C ATOM 575 O ALA A 164 35.864 49.130 12.932 1.00 67.10 O ANISOU 575 O ALA A 164 9947 7917 7631 535 -350 143 O ATOM 576 CB ALA A 164 36.047 52.259 13.242 1.00 50.67 C ANISOU 576 CB ALA A 164 7601 5737 5916 595 -230 511 C ATOM 577 N GLU A 165 35.116 50.020 10.995 1.00 77.93 N ANISOU 577 N GLU A 165 11671 9324 8615 821 -533 270 N ATOM 578 CA GLU A 165 35.509 48.859 10.207 1.00 81.70 C ANISOU 578 CA GLU A 165 12459 9804 8779 912 -488 197 C ATOM 579 C GLU A 165 37.018 48.764 10.034 1.00 74.37 C ANISOU 579 C GLU A 165 11621 8831 7804 1008 -98 379 C ATOM 580 O GLU A 165 37.536 47.666 9.805 1.00 73.45 O ANISOU 580 O GLU A 165 11683 8699 7525 1054 7 303 O ATOM 581 CB GLU A 165 34.830 48.898 8.835 1.00 97.46 C ANISOU 581 CB GLU A 165 14783 11843 10404 1094 -701 185 C ATOM 582 CG GLU A 165 33.317 49.081 8.892 1.00110.30 C ANISOU 582 CG GLU A 165 16290 13534 12085 1019 -1109 39 C ATOM 583 CD GLU A 165 32.607 47.937 9.594 1.00121.61 C ANISOU 583 CD GLU A 165 17591 14981 13636 804 -1321 -227 C ATOM 584 OE1 GLU A 165 32.332 46.913 8.934 1.00123.77 O ANISOU 584 OE1 GLU A 165 18129 15247 13652 816 -1487 -385 O ATOM 585 OE2 GLU A 165 32.330 48.058 10.808 1.00126.64 O ANISOU 585 OE2 GLU A 165 17878 15623 14616 622 -1318 -275 O ATOM 586 N ASP A 166 37.727 49.879 10.149 1.00 65.17 N ANISOU 586 N ASP A 166 10329 7638 6796 1038 118 623 N ATOM 587 CA ASP A 166 39.159 49.914 9.916 1.00 61.05 C ANISOU 587 CA ASP A 166 9848 7090 6260 1129 495 842 C ATOM 588 C ASP A 166 39.932 49.726 11.216 1.00 64.35 C ANISOU 588 C ASP A 166 9943 7482 7026 943 643 844 C ATOM 589 O ASP A 166 39.501 50.151 12.291 1.00 70.93 O ANISOU 589 O ASP A 166 10503 8297 8149 756 509 766 O ATOM 590 CB ASP A 166 39.550 51.236 9.258 1.00 66.49 C ANISOU 590 CB ASP A 166 10576 7750 6936 1247 650 1137 C ATOM 591 CG ASP A 166 41.015 51.305 8.925 1.00 69.93 C ANISOU 591 CG ASP A 166 11032 8174 7366 1342 1056 1399 C ATOM 592 OD1 ASP A 166 41.474 50.509 8.081 1.00 67.60 O ANISOU 592 OD1 ASP A 166 11009 7919 6758 1529 1216 1417 O ATOM 593 OD2 ASP A 166 41.703 52.167 9.503 1.00 72.65 O ANISOU 593 OD2 ASP A 166 11119 8463 8021 1231 1216 1590 O ATOM 594 N TRP A 167 41.093 49.082 11.101 1.00 63.53 N ANISOU 594 N TRP A 167 9879 7380 6878 1017 925 940 N ATOM 595 CA TRP A 167 41.986 48.914 12.235 1.00 52.55 C ANISOU 595 CA TRP A 167 8189 5979 5800 869 1076 984 C ATOM 596 C TRP A 167 43.128 49.909 12.118 1.00 62.29 C ANISOU 596 C TRP A 167 9275 7193 7198 891 1358 1301 C ATOM 597 O TRP A 167 44.012 49.719 11.269 1.00 55.81 O ANISOU 597 O TRP A 167 8593 6398 6216 1075 1639 1490 O ATOM 598 CB TRP A 167 42.528 47.489 12.294 1.00 54.26 C ANISOU 598 CB TRP A 167 8503 6209 5906 933 1191 888 C ATOM 599 CG TRP A 167 43.437 47.240 13.475 1.00 58.02 C ANISOU 599 CG TRP A 167 8667 6686 6691 797 1320 939 C ATOM 600 CD1 TRP A 167 44.775 47.508 13.555 1.00 55.10 C ANISOU 600 CD1 TRP A 167 8130 6335 6471 839 1614 1188 C ATOM 601 CD2 TRP A 167 43.069 46.676 14.739 1.00 56.22 C ANISOU 601 CD2 TRP A 167 8253 6450 6658 601 1149 750 C ATOM 602 NE1 TRP A 167 45.262 47.140 14.784 1.00 51.12 N ANISOU 602 NE1 TRP A 167 7351 5838 6235 683 1606 1156 N ATOM 603 CE2 TRP A 167 44.234 46.630 15.532 1.00 51.75 C ANISOU 603 CE2 TRP A 167 7431 5899 6331 542 1332 890 C ATOM 604 CE3 TRP A 167 41.868 46.207 15.278 1.00 54.27 C ANISOU 604 CE3 TRP A 167 8018 6193 6408 468 865 494 C ATOM 605 CZ2 TRP A 167 44.231 46.136 16.836 1.00 46.26 C ANISOU 605 CZ2 TRP A 167 6531 5207 5838 371 1229 775 C ATOM 606 CZ3 TRP A 167 41.869 45.712 16.570 1.00 56.36 C ANISOU 606 CZ3 TRP A 167 8074 6457 6883 295 799 393 C ATOM 607 CH2 TRP A 167 43.043 45.677 17.333 1.00 50.85 C ANISOU 607 CH2 TRP A 167 7161 5772 6386 256 976 530 C ATOM 608 N PRO A 168 43.161 50.963 12.927 1.00 56.53 N ANISOU 608 N PRO A 168 8278 6414 6788 712 1303 1373 N ATOM 609 CA PRO A 168 44.245 51.959 12.844 1.00 59.44 C ANISOU 609 CA PRO A 168 8491 6738 7357 689 1547 1682 C ATOM 610 C PRO A 168 45.398 51.752 13.818 1.00 68.60 C ANISOU 610 C PRO A 168 9341 7908 8817 545 1692 1766 C ATOM 611 O PRO A 168 46.350 52.538 13.773 1.00 75.62 O ANISOU 611 O PRO A 168 10066 8761 9906 498 1884 2031 O ATOM 612 CB PRO A 168 43.499 53.250 13.182 1.00 55.76 C ANISOU 612 CB PRO A 168 7946 6177 7064 569 1352 1678 C ATOM 613 CG PRO A 168 42.501 52.804 14.231 1.00 52.29 C ANISOU 613 CG PRO A 168 7410 5754 6705 430 1061 1363 C ATOM 614 CD PRO A 168 42.097 51.387 13.855 1.00 56.93 C ANISOU 614 CD PRO A 168 8186 6432 7014 535 1007 1176 C ATOM 615 N PHE A 169 45.346 50.746 14.684 1.00 65.03 N ANISOU 615 N PHE A 169 8798 7499 8413 469 1597 1565 N ATOM 616 CA PHE A 169 46.313 50.622 15.766 1.00 64.36 C ANISOU 616 CA PHE A 169 8400 7427 8626 315 1663 1626 C ATOM 617 C PHE A 169 47.587 49.893 15.365 1.00 71.67 C ANISOU 617 C PHE A 169 9281 8424 9525 458 1970 1818 C ATOM 618 O PHE A 169 48.496 49.778 16.192 1.00 70.63 O ANISOU 618 O PHE A 169 8866 8320 9649 348 2030 1904 O ATOM 619 CB PHE A 169 45.673 49.918 16.962 1.00 59.12 C ANISOU 619 CB PHE A 169 7655 6778 8030 172 1424 1346 C ATOM 620 CG PHE A 169 44.375 50.530 17.394 1.00 55.32 C ANISOU 620 CG PHE A 169 7201 6248 7571 59 1149 1151 C ATOM 621 CD1 PHE A 169 44.332 51.833 17.867 1.00 49.37 C ANISOU 621 CD1 PHE A 169 6304 5413 7043 -78 1075 1213 C ATOM 622 CD2 PHE A 169 43.196 49.804 17.332 1.00 56.92 C ANISOU 622 CD2 PHE A 169 7567 6477 7584 92 965 910 C ATOM 623 CE1 PHE A 169 43.134 52.400 18.265 1.00 45.09 C ANISOU 623 CE1 PHE A 169 5787 4825 6521 -144 846 1038 C ATOM 624 CE2 PHE A 169 41.997 50.365 17.730 1.00 60.59 C ANISOU 624 CE2 PHE A 169 8016 6916 8089 6 732 753 C ATOM 625 CZ PHE A 169 41.965 51.663 18.199 1.00 44.09 C ANISOU 625 CZ PHE A 169 5788 4754 6210 -94 683 816 C ATOM 626 N GLY A 170 47.680 49.397 14.136 1.00 53.94 N ANISOU 626 N GLY A 170 7309 6213 6972 712 2160 1887 N ATOM 627 CA GLY A 170 48.907 48.807 13.647 1.00 56.14 C ANISOU 627 CA GLY A 170 7556 6561 7215 895 2502 2098 C ATOM 628 C GLY A 170 48.993 47.308 13.878 1.00 57.34 C ANISOU 628 C GLY A 170 7808 6748 7232 1011 2516 1924 C ATOM 629 O GLY A 170 48.167 46.690 14.556 1.00 56.01 O ANISOU 629 O GLY A 170 7695 6549 7039 909 2255 1648 O ATOM 630 N ALA A 171 50.037 46.717 13.291 1.00 62.12 N ANISOU 630 N ALA A 171 8435 7412 7756 1240 2850 2107 N ATOM 631 CA ALA A 171 50.230 45.275 13.406 1.00 58.08 C ANISOU 631 CA ALA A 171 8052 6908 7108 1398 2907 1968 C ATOM 632 C ALA A 171 50.570 44.872 14.835 1.00 75.22 C ANISOU 632 C ALA A 171 9895 9091 9594 1208 2773 1909 C ATOM 633 O ALA A 171 50.163 43.800 15.298 1.00 73.14 O ANISOU 633 O ALA A 171 9752 8788 9249 1219 2641 1688 O ATOM 634 CB ALA A 171 51.326 44.810 12.445 1.00 61.58 C ANISOU 634 CB ALA A 171 8585 7412 7400 1724 3331 2200 C ATOM 635 N GLU A 172 51.322 45.716 15.546 1.00 72.84 N ANISOU 635 N GLU A 172 9191 8836 9649 1027 2794 2111 N ATOM 636 CA GLU A 172 51.741 45.373 16.903 1.00 70.13 C ANISOU 636 CA GLU A 172 8538 8519 9588 858 2659 2077 C ATOM 637 C GLU A 172 50.540 45.230 17.830 1.00 58.17 C ANISOU 637 C GLU A 172 7098 6941 8063 648 2290 1763 C ATOM 638 O GLU A 172 50.384 44.209 18.510 1.00 61.07 O ANISOU 638 O GLU A 172 7494 7299 8409 648 2193 1610 O ATOM 639 CB GLU A 172 52.715 46.426 17.434 1.00 79.66 C ANISOU 639 CB GLU A 172 9317 9779 11173 676 2704 2341 C ATOM 640 CG GLU A 172 54.179 46.180 17.092 1.00 96.36 C ANISOU 640 CG GLU A 172 11188 11997 13426 846 3048 2665 C ATOM 641 CD GLU A 172 54.992 47.455 17.163 1.00106.22 C ANISOU 641 CD GLU A 172 12077 13275 15008 665 3123 2961 C ATOM 642 OE1 GLU A 172 54.581 48.443 16.518 1.00107.01 O ANISOU 642 OE1 GLU A 172 12291 13309 15060 608 3140 3020 O ATOM 643 OE2 GLU A 172 56.018 47.482 17.878 1.00109.24 O ANISOU 643 OE2 GLU A 172 12063 13735 15710 569 3142 3138 O ATOM 644 N MET A 173 49.666 46.239 17.855 1.00 54.23 N ANISOU 644 N MET A 173 6634 6392 7578 482 2099 1677 N ATOM 645 CA MET A 173 48.545 46.212 18.786 1.00 47.46 C ANISOU 645 CA MET A 173 5802 5491 6739 287 1778 1407 C ATOM 646 C MET A 173 47.629 45.024 18.540 1.00 55.09 C ANISOU 646 C MET A 173 7072 6423 7437 386 1689 1164 C ATOM 647 O MET A 173 47.012 44.512 19.481 1.00 64.54 O ANISOU 647 O MET A 173 8246 7603 8672 254 1491 974 O ATOM 648 CB MET A 173 47.762 47.523 18.708 1.00 46.82 C ANISOU 648 CB MET A 173 5725 5357 6706 146 1623 1373 C ATOM 649 CG MET A 173 48.390 48.658 19.512 1.00 74.34 C ANISOU 649 CG MET A 173 8897 8829 10520 -61 1577 1510 C ATOM 650 SD MET A 173 49.107 48.082 21.068 1.00 65.43 S ANISOU 650 SD MET A 173 7479 7757 9625 -214 1475 1478 S ATOM 651 CE MET A 173 47.663 47.487 21.943 1.00 43.18 C ANISOU 651 CE MET A 173 4815 4917 6676 -306 1198 1129 C ATOM 652 N CYS A 174 47.526 44.562 17.300 1.00 62.00 N ANISOU 652 N CYS A 174 8243 7280 8035 610 1828 1167 N ATOM 653 CA CYS A 174 46.637 43.440 17.038 1.00 70.69 C ANISOU 653 CA CYS A 174 9650 8320 8888 678 1709 921 C ATOM 654 C CYS A 174 47.291 42.074 17.197 1.00 56.37 C ANISOU 654 C CYS A 174 7910 6482 7026 821 1845 908 C ATOM 655 O CYS A 174 46.576 41.065 17.267 1.00 48.45 O ANISOU 655 O CYS A 174 7128 5399 5882 820 1714 693 O ATOM 656 CB CYS A 174 46.037 43.545 15.645 1.00 95.34 C ANISOU 656 CB CYS A 174 13116 11414 11694 841 1724 876 C ATOM 657 SG CYS A 174 45.032 42.115 15.254 1.00104.47 S ANISOU 657 SG CYS A 174 14665 12474 12554 907 1553 570 S ATOM 658 N LYS A 175 48.615 42.005 17.271 1.00 50.19 N ANISOU 658 N LYS A 175 6939 5757 6373 940 2099 1139 N ATOM 659 CA LYS A 175 49.197 40.807 17.857 1.00 50.48 C ANISOU 659 CA LYS A 175 6950 5773 6457 1025 2169 1128 C ATOM 660 C LYS A 175 49.084 40.838 19.378 1.00 53.76 C ANISOU 660 C LYS A 175 7085 6211 7132 773 1955 1076 C ATOM 661 O LYS A 175 48.939 39.786 20.017 1.00 66.72 O ANISOU 661 O LYS A 175 8789 7798 8764 769 1883 964 O ATOM 662 CB LYS A 175 50.641 40.664 17.389 1.00 53.12 C ANISOU 662 CB LYS A 175 7164 6177 6842 1272 2521 1404 C ATOM 663 CG LYS A 175 50.726 40.504 15.868 1.00 62.39 C ANISOU 663 CG LYS A 175 8679 7327 7701 1563 2764 1443 C ATOM 664 CD LYS A 175 52.139 40.365 15.349 1.00 61.16 C ANISOU 664 CD LYS A 175 8400 7253 7586 1839 3161 1736 C ATOM 665 CE LYS A 175 52.095 39.760 13.959 1.00 61.58 C ANISOU 665 CE LYS A 175 8905 7248 7243 2177 3392 1694 C ATOM 666 NZ LYS A 175 51.380 38.457 13.963 1.00 61.32 N ANISOU 666 NZ LYS A 175 9257 7059 6981 2251 3244 1390 N ATOM 667 N LEU A 176 49.083 42.040 19.959 1.00 47.07 N ANISOU 667 N LEU A 176 5964 5427 6493 563 1843 1145 N ATOM 668 CA LEU A 176 49.076 42.184 21.409 1.00 56.34 C ANISOU 668 CA LEU A 176 6883 6634 7891 338 1649 1107 C ATOM 669 C LEU A 176 47.688 41.940 21.994 1.00 53.22 C ANISOU 669 C LEU A 176 6627 6179 7414 172 1390 839 C ATOM 670 O LEU A 176 47.536 41.157 22.937 1.00 57.02 O ANISOU 670 O LEU A 176 7088 6647 7931 104 1292 753 O ATOM 671 CB LEU A 176 49.587 43.571 21.791 1.00 58.44 C ANISOU 671 CB LEU A 176 6843 6962 8400 176 1616 1261 C ATOM 672 CG LEU A 176 49.715 43.758 23.301 1.00 53.77 C ANISOU 672 CG LEU A 176 6004 6407 8018 -41 1412 1225 C ATOM 673 CD1 LEU A 176 50.765 42.812 23.873 1.00 49.34 C ANISOU 673 CD1 LEU A 176 5292 5904 7550 54 1494 1349 C ATOM 674 CD2 LEU A 176 50.020 45.200 23.658 1.00 55.09 C ANISOU 674 CD2 LEU A 176 5933 6592 8405 -230 1327 1321 C ATOM 675 N VAL A 177 46.659 42.594 21.447 1.00 46.06 N ANISOU 675 N VAL A 177 5854 5243 6404 111 1282 722 N ATOM 676 CA VAL A 177 45.324 42.510 22.054 1.00 46.67 C ANISOU 676 CA VAL A 177 5994 5290 6450 -59 1041 494 C ATOM 677 C VAL A 177 44.828 41.072 22.181 1.00 47.05 C ANISOU 677 C VAL A 177 6240 5267 6368 -29 998 345 C ATOM 678 O VAL A 177 44.470 40.668 23.299 1.00 56.36 O ANISOU 678 O VAL A 177 7336 6448 7632 -170 880 264 O ATOM 679 CB VAL A 177 44.341 43.437 21.307 1.00 40.72 C ANISOU 679 CB VAL A 177 5339 4524 5609 -88 942 418 C ATOM 680 CG1 VAL A 177 42.905 43.173 21.752 1.00 45.22 C ANISOU 680 CG1 VAL A 177 5976 5072 6133 -226 716 191 C ATOM 681 CG2 VAL A 177 44.701 44.900 21.586 1.00 40.51 C ANISOU 681 CG2 VAL A 177 5092 4532 5769 -181 936 543 C ATOM 682 N PRO A 178 44.829 40.236 21.130 1.00 50.90 N ANISOU 682 N PRO A 178 7007 5680 6653 151 1094 309 N ATOM 683 CA PRO A 178 44.388 38.840 21.324 1.00 51.86 C ANISOU 683 CA PRO A 178 7331 5695 6680 157 1039 164 C ATOM 684 C PRO A 178 45.284 38.045 22.251 1.00 49.88 C ANISOU 684 C PRO A 178 6967 5435 6549 191 1131 260 C ATOM 685 O PRO A 178 44.802 37.134 22.937 1.00 51.64 O ANISOU 685 O PRO A 178 7259 5582 6778 102 1035 157 O ATOM 686 CB PRO A 178 44.420 38.246 19.907 1.00 57.25 C ANISOU 686 CB PRO A 178 8360 6287 7107 376 1142 120 C ATOM 687 CG PRO A 178 44.581 39.359 18.999 1.00 56.67 C ANISOU 687 CG PRO A 178 8275 6289 6969 459 1214 218 C ATOM 688 CD PRO A 178 45.252 40.461 19.743 1.00 56.14 C ANISOU 688 CD PRO A 178 7845 6337 7149 364 1263 398 C ATOM 689 N PHE A 179 46.586 38.333 22.254 1.00 46.29 N ANISOU 689 N PHE A 179 6339 5055 6193 324 1316 473 N ATOM 690 CA PHE A 179 47.491 37.681 23.190 1.00 51.71 C ANISOU 690 CA PHE A 179 6872 5760 7016 363 1379 591 C ATOM 691 C PHE A 179 47.125 38.025 24.630 1.00 53.13 C ANISOU 691 C PHE A 179 6831 6002 7354 117 1181 554 C ATOM 692 O PHE A 179 46.989 37.134 25.476 1.00 52.37 O ANISOU 692 O PHE A 179 6767 5860 7272 75 1121 515 O ATOM 693 CB PHE A 179 48.933 38.081 22.876 1.00 55.53 C ANISOU 693 CB PHE A 179 7151 6339 7608 537 1600 846 C ATOM 694 CG PHE A 179 49.887 37.794 23.987 1.00 52.77 C ANISOU 694 CG PHE A 179 6533 6061 7456 532 1605 997 C ATOM 695 CD1 PHE A 179 50.338 36.505 24.210 1.00 54.53 C ANISOU 695 CD1 PHE A 179 6858 6212 7648 702 1692 1029 C ATOM 696 CD2 PHE A 179 50.327 38.811 24.819 1.00 52.12 C ANISOU 696 CD2 PHE A 179 6112 6105 7587 360 1503 1105 C ATOM 697 CE1 PHE A 179 51.215 36.233 25.241 1.00 57.18 C ANISOU 697 CE1 PHE A 179 6942 6623 8159 713 1675 1183 C ATOM 698 CE2 PHE A 179 51.201 38.550 25.848 1.00 52.57 C ANISOU 698 CE2 PHE A 179 5925 6237 7811 351 1467 1241 C ATOM 699 CZ PHE A 179 51.648 37.259 26.061 1.00 52.99 C ANISOU 699 CZ PHE A 179 6063 6242 7830 534 1552 1289 C ATOM 700 N ILE A 180 46.941 39.316 24.923 1.00 45.02 N ANISOU 700 N ILE A 180 5608 5068 6431 -39 1085 566 N ATOM 701 CA ILE A 180 46.533 39.723 26.265 1.00 44.77 C ANISOU 701 CA ILE A 180 5407 5091 6511 -255 902 508 C ATOM 702 C ILE A 180 45.180 39.119 26.619 1.00 47.17 C ANISOU 702 C ILE A 180 5881 5328 6715 -374 770 307 C ATOM 703 O ILE A 180 44.948 38.707 27.763 1.00 60.55 O ANISOU 703 O ILE A 180 7525 7036 8447 -482 683 275 O ATOM 704 CB ILE A 180 46.510 41.259 26.383 1.00 38.85 C ANISOU 704 CB ILE A 180 4472 4415 5876 -383 827 533 C ATOM 705 CG1 ILE A 180 47.907 41.842 26.164 1.00 45.76 C ANISOU 705 CG1 ILE A 180 5134 5354 6900 -310 947 760 C ATOM 706 CG2 ILE A 180 45.975 41.684 27.741 1.00 37.63 C ANISOU 706 CG2 ILE A 180 4202 4304 5793 -584 641 436 C ATOM 707 CD1 ILE A 180 48.956 41.333 27.124 1.00 43.86 C ANISOU 707 CD1 ILE A 180 4704 5177 6785 -297 944 892 C ATOM 708 N GLN A 181 44.266 39.053 25.649 1.00 42.22 N ANISOU 708 N GLN A 181 5450 4633 5958 -360 748 180 N ATOM 709 CA GLN A 181 42.932 38.540 25.944 1.00 42.11 C ANISOU 709 CA GLN A 181 5551 4564 5885 -500 609 2 C ATOM 710 C GLN A 181 42.981 37.080 26.370 1.00 45.58 C ANISOU 710 C GLN A 181 6128 4899 6290 -481 635 -12 C ATOM 711 O GLN A 181 42.330 36.689 27.344 1.00 47.07 O ANISOU 711 O GLN A 181 6285 5083 6517 -632 547 -69 O ATOM 712 CB GLN A 181 42.012 38.715 24.736 1.00 44.44 C ANISOU 712 CB GLN A 181 6022 4809 6053 -482 552 -120 C ATOM 713 CG GLN A 181 41.578 40.155 24.496 1.00 45.92 C ANISOU 713 CG GLN A 181 6082 5085 6282 -536 482 -130 C ATOM 714 CD GLN A 181 40.627 40.293 23.324 1.00 49.30 C ANISOU 714 CD GLN A 181 6683 5477 6573 -507 395 -240 C ATOM 715 OE1 GLN A 181 39.860 41.251 23.245 1.00 48.34 O ANISOU 715 OE1 GLN A 181 6476 5409 6481 -575 288 -288 O ATOM 716 NE2 GLN A 181 40.677 39.337 22.403 1.00 52.87 N ANISOU 716 NE2 GLN A 181 7394 5830 6864 -393 430 -285 N ATOM 717 N LYS A 182 43.756 36.260 25.663 1.00 47.99 N ANISOU 717 N LYS A 182 6600 5113 6522 -285 771 49 N ATOM 718 CA LYS A 182 43.859 34.849 26.011 1.00 51.90 C ANISOU 718 CA LYS A 182 7260 5471 6989 -242 804 43 C ATOM 719 C LYS A 182 44.789 34.615 27.193 1.00 49.80 C ANISOU 719 C LYS A 182 6813 5267 6841 -217 851 203 C ATOM 720 O LYS A 182 44.572 33.678 27.969 1.00 46.15 O ANISOU 720 O LYS A 182 6423 4724 6389 -271 819 199 O ATOM 721 CB LYS A 182 44.336 34.045 24.804 1.00 55.74 C ANISOU 721 CB LYS A 182 8028 5815 7337 -8 940 36 C ATOM 722 CG LYS A 182 43.393 34.104 23.607 1.00 56.87 C ANISOU 722 CG LYS A 182 8410 5879 7319 -24 860 -139 C ATOM 723 CD LYS A 182 41.970 33.763 23.999 1.00 62.86 C ANISOU 723 CD LYS A 182 9223 6570 8090 -278 650 -310 C ATOM 724 CE LYS A 182 41.022 33.925 22.825 1.00 67.83 C ANISOU 724 CE LYS A 182 10049 7150 8575 -307 523 -477 C ATOM 725 NZ LYS A 182 40.963 35.330 22.327 1.00 66.53 N ANISOU 725 NZ LYS A 182 9731 7150 8397 -286 508 -443 N ATOM 726 N ALA A 183 45.818 35.450 27.353 1.00 50.63 N ANISOU 726 N ALA A 183 6683 5512 7041 -146 911 355 N ATOM 727 CA ALA A 183 46.678 35.330 28.525 1.00 50.31 C ANISOU 727 CA ALA A 183 6445 5555 7117 -142 902 505 C ATOM 728 C ALA A 183 45.910 35.658 29.799 1.00 48.37 C ANISOU 728 C ALA A 183 6100 5376 6902 -374 734 434 C ATOM 729 O ALA A 183 46.022 34.947 30.803 1.00 57.25 O ANISOU 729 O ALA A 183 7228 6489 8034 -397 701 486 O ATOM 730 CB ALA A 183 47.902 36.235 28.383 1.00 41.64 C ANISOU 730 CB ALA A 183 5088 4595 6138 -52 972 680 C ATOM 731 N SER A 184 45.116 36.732 29.774 1.00 45.32 N ANISOU 731 N SER A 184 5641 5058 6522 -528 639 323 N ATOM 732 CA SER A 184 44.381 37.135 30.970 1.00 47.71 C ANISOU 732 CA SER A 184 5855 5433 6839 -719 508 253 C ATOM 733 C SER A 184 43.336 36.092 31.349 1.00 49.05 C ANISOU 733 C SER A 184 6191 5507 6938 -809 487 164 C ATOM 734 O SER A 184 43.276 35.650 32.502 1.00 62.06 O ANISOU 734 O SER A 184 7820 7180 8581 -874 455 205 O ATOM 735 CB SER A 184 43.731 38.503 30.757 1.00 46.68 C ANISOU 735 CB SER A 184 5629 5374 6734 -828 433 152 C ATOM 736 OG SER A 184 42.696 38.434 29.794 1.00 55.06 O ANISOU 736 OG SER A 184 6827 6363 7729 -845 430 25 O ATOM 737 N VAL A 185 42.502 35.684 30.387 1.00 48.58 N ANISOU 737 N VAL A 185 6300 5336 6824 -822 495 49 N ATOM 738 CA VAL A 185 41.493 34.663 30.667 1.00 48.21 C ANISOU 738 CA VAL A 185 6398 5177 6743 -938 465 -27 C ATOM 739 C VAL A 185 42.155 33.374 31.134 1.00 53.29 C ANISOU 739 C VAL A 185 7166 5704 7376 -851 537 85 C ATOM 740 O VAL A 185 41.641 32.677 32.018 1.00 57.67 O ANISOU 740 O VAL A 185 7765 6214 7934 -963 520 101 O ATOM 741 CB VAL A 185 40.606 34.422 29.429 1.00 46.05 C ANISOU 741 CB VAL A 185 6291 4790 6417 -964 427 -170 C ATOM 742 CG1 VAL A 185 39.596 33.326 29.706 1.00 39.88 C ANISOU 742 CG1 VAL A 185 5643 3874 5637 -1116 380 -238 C ATOM 743 CG2 VAL A 185 39.887 35.689 29.024 1.00 39.14 C ANISOU 743 CG2 VAL A 185 5286 4032 5553 -1036 345 -263 C ATOM 744 N GLY A 186 43.307 33.037 30.551 1.00 55.73 N ANISOU 744 N GLY A 186 7534 5963 7678 -637 633 181 N ATOM 745 CA GLY A 186 44.024 31.851 30.989 1.00 53.94 C ANISOU 745 CA GLY A 186 7418 5624 7452 -513 707 305 C ATOM 746 C GLY A 186 44.508 31.963 32.421 1.00 54.95 C ANISOU 746 C GLY A 186 7375 5881 7624 -547 668 442 C ATOM 747 O GLY A 186 44.495 30.980 33.167 1.00 59.60 O ANISOU 747 O GLY A 186 8066 6381 8200 -548 679 518 O ATOM 748 N ILE A 187 44.951 33.158 32.822 1.00 54.10 N ANISOU 748 N ILE A 187 7024 5971 7560 -574 610 478 N ATOM 749 CA ILE A 187 45.339 33.382 34.213 1.00 53.42 C ANISOU 749 CA ILE A 187 6792 6019 7485 -624 530 579 C ATOM 750 C ILE A 187 44.152 33.139 35.135 1.00 53.51 C ANISOU 750 C ILE A 187 6877 6025 7431 -814 480 506 C ATOM 751 O ILE A 187 44.265 32.449 36.154 1.00 57.19 O ANISOU 751 O ILE A 187 7391 6485 7855 -817 472 608 O ATOM 752 CB ILE A 187 45.913 34.798 34.393 1.00 45.87 C ANISOU 752 CB ILE A 187 5591 5248 6591 -654 449 593 C ATOM 753 CG1 ILE A 187 47.275 34.903 33.711 1.00 47.65 C ANISOU 753 CG1 ILE A 187 5697 5498 6910 -463 517 735 C ATOM 754 CG2 ILE A 187 46.015 35.160 35.872 1.00 41.08 C ANISOU 754 CG2 ILE A 187 4880 4776 5954 -750 322 633 C ATOM 755 CD1 ILE A 187 47.740 36.320 33.509 1.00 40.56 C ANISOU 755 CD1 ILE A 187 4575 4731 6104 -515 458 740 C ATOM 756 N THR A 188 42.993 33.699 34.784 1.00 43.92 N ANISOU 756 N THR A 188 5663 4818 6206 -963 456 346 N ATOM 757 CA THR A 188 41.773 33.457 35.550 1.00 45.55 C ANISOU 757 CA THR A 188 5911 5024 6371 -1140 442 286 C ATOM 758 C THR A 188 41.428 31.970 35.585 1.00 51.83 C ANISOU 758 C THR A 188 6909 5627 7156 -1158 506 339 C ATOM 759 O THR A 188 41.109 31.414 36.644 1.00 61.59 O ANISOU 759 O THR A 188 8186 6862 8353 -1232 525 419 O ATOM 760 CB THR A 188 40.622 34.266 34.947 1.00 44.23 C ANISOU 760 CB THR A 188 5687 4892 6226 -1265 410 117 C ATOM 761 OG1 THR A 188 40.736 35.639 35.343 1.00 53.93 O ANISOU 761 OG1 THR A 188 6745 6290 7457 -1282 350 75 O ATOM 762 CG2 THR A 188 39.272 33.712 35.387 1.00 40.57 C ANISOU 762 CG2 THR A 188 5271 4387 5758 -1439 427 68 C ATOM 763 N VAL A 189 41.495 31.313 34.426 1.00 53.61 N ANISOU 763 N VAL A 189 7289 5674 7407 -1086 543 296 N ATOM 764 CA VAL A 189 41.134 29.900 34.331 1.00 53.35 C ANISOU 764 CA VAL A 189 7487 5407 7378 -1114 588 321 C ATOM 765 C VAL A 189 42.009 29.061 35.255 1.00 57.36 C ANISOU 765 C VAL A 189 8061 5868 7865 -994 640 515 C ATOM 766 O VAL A 189 41.515 28.213 36.009 1.00 54.81 O ANISOU 766 O VAL A 189 7845 5446 7535 -1093 666 588 O ATOM 767 CB VAL A 189 41.238 29.428 32.869 1.00 50.08 C ANISOU 767 CB VAL A 189 7262 4803 6964 -1015 607 223 C ATOM 768 CG1 VAL A 189 41.313 27.913 32.793 1.00 46.21 C ANISOU 768 CG1 VAL A 189 7050 4032 6475 -971 660 272 C ATOM 769 CG2 VAL A 189 40.057 29.946 32.061 1.00 43.39 C ANISOU 769 CG2 VAL A 189 6399 3961 6125 -1178 523 37 C ATOM 770 N LEU A 190 43.325 29.288 35.214 1.00 55.95 N ANISOU 770 N LEU A 190 7807 5765 7688 -779 656 620 N ATOM 771 CA LEU A 190 44.242 28.482 36.013 1.00 57.59 C ANISOU 771 CA LEU A 190 8064 5935 7883 -628 688 820 C ATOM 772 C LEU A 190 44.197 28.875 37.487 1.00 64.14 C ANISOU 772 C LEU A 190 8764 6953 8653 -719 618 916 C ATOM 773 O LEU A 190 44.290 28.009 38.366 1.00 47.77 O ANISOU 773 O LEU A 190 6800 4814 6538 -697 638 1062 O ATOM 774 CB LEU A 190 45.659 28.602 35.452 1.00 54.91 C ANISOU 774 CB LEU A 190 7644 5633 7585 -361 727 916 C ATOM 775 CG LEU A 190 45.837 28.014 34.046 1.00 50.00 C ANISOU 775 CG LEU A 190 7212 4806 6980 -207 834 846 C ATOM 776 CD1 LEU A 190 47.215 28.318 33.469 1.00 48.05 C ANISOU 776 CD1 LEU A 190 6833 4643 6779 63 909 954 C ATOM 777 CD2 LEU A 190 45.579 26.516 34.066 1.00 49.60 C ANISOU 777 CD2 LEU A 190 7470 4460 6914 -164 898 879 C ATOM 778 N SER A 191 44.052 30.171 37.779 1.00 56.23 N ANISOU 778 N SER A 191 7558 6172 7633 -811 537 836 N ATOM 779 CA SER A 191 43.911 30.598 39.169 1.00 53.55 C ANISOU 779 CA SER A 191 7140 6006 7199 -896 467 892 C ATOM 780 C SER A 191 42.670 29.982 39.805 1.00 52.13 C ANISOU 780 C SER A 191 7093 5755 6959 -1067 533 885 C ATOM 781 O SER A 191 42.723 29.469 40.929 1.00 58.35 O ANISOU 781 O SER A 191 7952 6568 7652 -1065 541 1026 O ATOM 782 CB SER A 191 43.867 32.126 39.257 1.00 53.48 C ANISOU 782 CB SER A 191 6931 6204 7185 -969 373 770 C ATOM 783 OG SER A 191 45.135 32.694 38.967 1.00 56.72 O ANISOU 783 OG SER A 191 7191 6700 7661 -834 301 829 O ATOM 784 N LEU A 192 41.540 30.020 39.095 1.00 50.83 N ANISOU 784 N LEU A 192 6955 5507 6852 -1216 578 739 N ATOM 785 CA LEU A 192 40.323 29.392 39.602 1.00 49.56 C ANISOU 785 CA LEU A 192 6882 5271 6678 -1399 652 750 C ATOM 786 C LEU A 192 40.528 27.903 39.848 1.00 56.51 C ANISOU 786 C LEU A 192 7980 5925 7565 -1362 721 915 C ATOM 787 O LEU A 192 39.990 27.346 40.811 1.00 58.91 O ANISOU 787 O LEU A 192 8356 6212 7817 -1461 787 1032 O ATOM 788 CB LEU A 192 39.177 29.610 38.620 1.00 53.64 C ANISOU 788 CB LEU A 192 7367 5722 7292 -1557 656 573 C ATOM 789 CG LEU A 192 38.090 30.604 39.023 1.00 61.93 C ANISOU 789 CG LEU A 192 8244 6958 8329 -1709 657 471 C ATOM 790 CD1 LEU A 192 38.634 31.673 39.957 1.00 67.59 C ANISOU 790 CD1 LEU A 192 8843 7910 8930 -1627 620 485 C ATOM 791 CD2 LEU A 192 37.514 31.232 37.772 1.00 54.15 C ANISOU 791 CD2 LEU A 192 7176 5961 7438 -1759 598 287 C ATOM 792 N CYS A 193 41.286 27.234 38.977 1.00 62.23 N ANISOU 792 N CYS A 193 8828 6463 8352 -1209 724 933 N ATOM 793 CA CYS A 193 41.607 25.830 39.214 1.00 60.75 C ANISOU 793 CA CYS A 193 8872 6035 8175 -1133 789 1095 C ATOM 794 C CYS A 193 42.514 25.672 40.427 1.00 62.28 C ANISOU 794 C CYS A 193 9053 6344 8268 -984 776 1312 C ATOM 795 O CYS A 193 42.343 24.740 41.220 1.00 61.26 O ANISOU 795 O CYS A 193 9080 6098 8098 -1005 834 1479 O ATOM 796 CB CYS A 193 42.261 25.219 37.974 1.00 56.95 C ANISOU 796 CB CYS A 193 8542 5329 7766 -958 808 1049 C ATOM 797 SG CYS A 193 41.182 25.052 36.536 1.00 59.08 S ANISOU 797 SG CYS A 193 8932 5394 8120 -1125 796 805 S ATOM 798 N ALA A 194 43.489 26.568 40.585 1.00 59.00 N ANISOU 798 N ALA A 194 8454 6152 7812 -839 688 1324 N ATOM 799 CA ALA A 194 44.379 26.490 41.737 1.00 58.84 C ANISOU 799 CA ALA A 194 8403 6266 7689 -702 627 1522 C ATOM 800 C ALA A 194 43.637 26.822 43.024 1.00 63.85 C ANISOU 800 C ALA A 194 9030 7059 8172 -859 617 1558 C ATOM 801 O ALA A 194 43.907 26.230 44.075 1.00 54.42 O ANISOU 801 O ALA A 194 7940 5877 6861 -797 616 1753 O ATOM 802 CB ALA A 194 45.568 27.424 41.536 1.00 51.18 C ANISOU 802 CB ALA A 194 7209 5494 6742 -545 509 1517 C ATOM 803 N LEU A 195 42.685 27.754 42.953 1.00 58.65 N ANISOU 803 N LEU A 195 8262 6523 7501 -1043 623 1379 N ATOM 804 CA LEU A 195 41.862 28.081 44.110 1.00 55.51 C ANISOU 804 CA LEU A 195 7868 6273 6952 -1177 658 1398 C ATOM 805 C LEU A 195 41.072 26.867 44.586 1.00 58.77 C ANISOU 805 C LEU A 195 8471 6509 7349 -1279 806 1547 C ATOM 806 O LEU A 195 41.037 26.565 45.784 1.00 69.94 O ANISOU 806 O LEU A 195 9978 7997 8599 -1267 843 1713 O ATOM 807 CB LEU A 195 40.916 29.229 43.757 1.00 56.18 C ANISOU 807 CB LEU A 195 7798 6484 7065 -1332 665 1174 C ATOM 808 CG LEU A 195 41.164 30.638 44.303 1.00 56.60 C ANISOU 808 CG LEU A 195 7707 6796 7004 -1311 554 1067 C ATOM 809 CD1 LEU A 195 42.412 30.705 45.164 1.00 58.64 C ANISOU 809 CD1 LEU A 195 7981 7169 7130 -1155 414 1199 C ATOM 810 CD2 LEU A 195 41.224 31.659 43.173 1.00 47.47 C ANISOU 810 CD2 LEU A 195 6388 5665 5985 -1322 486 869 C ATOM 811 N SER A 196 40.433 26.151 43.656 1.00 58.55 N ANISOU 811 N SER A 196 8520 6239 7489 -1386 887 1495 N ATOM 812 CA SER A 196 39.596 25.019 44.044 1.00 60.76 C ANISOU 812 CA SER A 196 8968 6321 7797 -1530 1024 1634 C ATOM 813 C SER A 196 40.426 23.830 44.511 1.00 63.24 C ANISOU 813 C SER A 196 9503 6454 8072 -1370 1044 1877 C ATOM 814 O SER A 196 39.969 23.053 45.356 1.00 67.48 O ANISOU 814 O SER A 196 10182 6905 8552 -1447 1152 2068 O ATOM 815 CB SER A 196 38.701 24.601 42.880 1.00 65.81 C ANISOU 815 CB SER A 196 9632 6734 8640 -1710 1059 1493 C ATOM 816 OG SER A 196 39.472 24.039 41.834 1.00 73.84 O ANISOU 816 OG SER A 196 10772 7528 9754 -1567 1003 1451 O ATOM 817 N ILE A 197 41.631 23.657 43.968 1.00 64.00 N ANISOU 817 N ILE A 197 9627 6485 8206 -1138 956 1891 N ATOM 818 CA ILE A 197 42.490 22.578 44.440 1.00 68.93 C ANISOU 818 CA ILE A 197 10444 6952 8796 -941 967 2136 C ATOM 819 C ILE A 197 43.022 22.900 45.831 1.00 71.63 C ANISOU 819 C ILE A 197 10750 7545 8920 -837 905 2315 C ATOM 820 O ILE A 197 43.118 22.018 46.693 1.00 69.61 O ANISOU 820 O ILE A 197 10678 7197 8572 -781 958 2556 O ATOM 821 CB ILE A 197 43.625 22.316 43.433 1.00 67.05 C ANISOU 821 CB ILE A 197 10221 6586 8668 -693 912 2107 C ATOM 822 CG1 ILE A 197 43.055 21.832 42.099 1.00 70.52 C ANISOU 822 CG1 ILE A 197 10779 6738 9276 -786 976 1934 C ATOM 823 CG2 ILE A 197 44.589 21.273 43.974 1.00 62.82 C ANISOU 823 CG2 ILE A 197 9857 5913 8099 -445 919 2374 C ATOM 824 CD1 ILE A 197 44.073 21.793 40.987 1.00 71.05 C ANISOU 824 CD1 ILE A 197 10848 6721 9425 -537 951 1863 C ATOM 825 N ASP A 198 43.351 24.171 46.082 1.00 69.43 N ANISOU 825 N ASP A 198 10257 7578 8546 -813 781 2199 N ATOM 826 CA ASP A 198 43.827 24.568 47.403 1.00 73.58 C ANISOU 826 CA ASP A 198 10768 8352 8837 -727 683 2332 C ATOM 827 C ASP A 198 42.747 24.415 48.465 1.00 77.43 C ANISOU 827 C ASP A 198 11376 8894 9151 -890 815 2417 C ATOM 828 O ASP A 198 43.056 24.093 49.619 1.00 81.73 O ANISOU 828 O ASP A 198 12046 9523 9484 -797 794 2625 O ATOM 829 CB ASP A 198 44.341 26.005 47.366 1.00 79.30 C ANISOU 829 CB ASP A 198 11253 9359 9517 -701 509 2157 C ATOM 830 CG ASP A 198 45.664 26.123 46.644 1.00 93.86 C ANISOU 830 CG ASP A 198 12961 11203 11498 -501 373 2164 C ATOM 831 OD1 ASP A 198 46.088 25.120 46.028 1.00 98.79 O ANISOU 831 OD1 ASP A 198 13680 11601 12255 -370 440 2270 O ATOM 832 OD2 ASP A 198 46.285 27.208 46.702 1.00 97.78 O ANISOU 832 OD2 ASP A 198 13260 11918 11975 -470 208 2072 O ATOM 833 N ARG A 199 41.484 24.644 48.105 1.00 71.72 N ANISOU 833 N ARG A 199 10608 8134 8507 -1121 954 2275 N ATOM 834 CA ARG A 199 40.409 24.428 49.065 1.00 67.64 C ANISOU 834 CA ARG A 199 10182 7663 7854 -1274 1126 2383 C ATOM 835 C ARG A 199 40.269 22.952 49.403 1.00 71.78 C ANISOU 835 C ARG A 199 10948 7920 8406 -1284 1260 2657 C ATOM 836 O ARG A 199 39.979 22.598 50.552 1.00 81.42 O ANISOU 836 O ARG A 199 12305 9202 9429 -1292 1365 2868 O ATOM 837 CB ARG A 199 39.091 24.980 48.529 1.00 61.77 C ANISOU 837 CB ARG A 199 9290 6943 7236 -1513 1244 2185 C ATOM 838 CG ARG A 199 39.038 26.492 48.403 1.00 59.36 C ANISOU 838 CG ARG A 199 8775 6906 6874 -1509 1146 1937 C ATOM 839 CD ARG A 199 39.213 27.164 49.753 1.00 71.06 C ANISOU 839 CD ARG A 199 10297 8661 8042 -1423 1121 1988 C ATOM 840 NE ARG A 199 40.614 27.407 50.087 1.00 73.45 N ANISOU 840 NE ARG A 199 10629 9059 8220 -1214 895 2029 N ATOM 841 CZ ARG A 199 41.083 27.456 51.330 1.00 70.68 C ANISOU 841 CZ ARG A 199 10407 8868 7580 -1098 828 2166 C ATOM 842 NH1 ARG A 199 42.367 27.690 51.547 1.00 71.73 N ANISOU 842 NH1 ARG A 199 10528 9090 7638 -925 585 2199 N ATOM 843 NH2 ARG A 199 40.267 27.258 52.355 1.00 66.38 N ANISOU 843 NH2 ARG A 199 9999 8402 6820 -1152 1005 2282 N ATOM 844 N TYR A 200 40.480 22.071 48.423 1.00 75.42 N ANISOU 844 N TYR A 200 11491 8068 9097 -1275 1264 2663 N ATOM 845 CA TYR A 200 40.430 20.644 48.720 1.00 83.86 C ANISOU 845 CA TYR A 200 12821 8836 10207 -1271 1378 2925 C ATOM 846 C TYR A 200 41.609 20.229 49.591 1.00 83.36 C ANISOU 846 C TYR A 200 12898 8819 9957 -990 1289 3173 C ATOM 847 O TYR A 200 41.439 19.506 50.579 1.00 82.09 O ANISOU 847 O TYR A 200 12930 8602 9657 -982 1390 3443 O ATOM 848 CB TYR A 200 40.398 19.820 47.432 1.00 69.20 C ANISOU 848 CB TYR A 200 11057 6606 8628 -1312 1388 2842 C ATOM 849 CG TYR A 200 40.554 18.343 47.698 1.00 78.65 C ANISOU 849 CG TYR A 200 12557 7448 9877 -1264 1479 3108 C ATOM 850 CD1 TYR A 200 39.507 17.601 48.228 1.00 75.35 C ANISOU 850 CD1 TYR A 200 12273 6861 9494 -1503 1655 3276 C ATOM 851 CD2 TYR A 200 41.756 17.696 47.445 1.00 79.30 C ANISOU 851 CD2 TYR A 200 12785 7362 9983 -971 1399 3211 C ATOM 852 CE1 TYR A 200 39.651 16.248 48.487 1.00 79.13 C ANISOU 852 CE1 TYR A 200 13051 6984 10031 -1467 1739 3535 C ATOM 853 CE2 TYR A 200 41.909 16.349 47.699 1.00 80.67 C ANISOU 853 CE2 TYR A 200 13258 7187 10206 -904 1484 3460 C ATOM 854 CZ TYR A 200 40.855 15.630 48.219 1.00 84.74 C ANISOU 854 CZ TYR A 200 13930 7513 10755 -1159 1648 3619 C ATOM 855 OH TYR A 200 41.010 14.287 48.472 1.00 94.31 O ANISOU 855 OH TYR A 200 15460 8345 12027 -1099 1733 3879 O ATOM 856 N ARG A 201 42.819 20.678 49.242 1.00 85.03 N ANISOU 856 N ARG A 201 13002 9140 10166 -755 1098 3105 N ATOM 857 CA ARG A 201 43.989 20.323 50.040 1.00 89.71 C ANISOU 857 CA ARG A 201 13683 9802 10600 -476 977 3345 C ATOM 858 C ARG A 201 43.888 20.867 51.459 1.00 93.70 C ANISOU 858 C ARG A 201 14205 10616 10780 -474 934 3456 C ATOM 859 O ARG A 201 44.456 20.282 52.390 1.00 98.31 O ANISOU 859 O ARG A 201 14954 11216 11185 -301 888 3727 O ATOM 860 CB ARG A 201 45.267 20.829 49.368 1.00 87.66 C ANISOU 860 CB ARG A 201 13235 9642 10430 -248 779 3245 C ATOM 861 CG ARG A 201 45.486 20.287 47.967 1.00 95.84 C ANISOU 861 CG ARG A 201 14286 10386 11744 -193 834 3142 C ATOM 862 CD ARG A 201 46.851 20.674 47.412 1.00102.33 C ANISOU 862 CD ARG A 201 14921 11315 12646 75 678 3114 C ATOM 863 NE ARG A 201 47.348 21.926 47.978 1.00104.83 N ANISOU 863 NE ARG A 201 14988 12017 12827 89 487 3050 N ATOM 864 CZ ARG A 201 48.458 22.027 48.701 1.00109.53 C ANISOU 864 CZ ARG A 201 15501 12796 13318 305 304 3224 C ATOM 865 NH1 ARG A 201 48.836 23.204 49.181 1.00110.53 N ANISOU 865 NH1 ARG A 201 15416 13250 13332 276 107 3135 N ATOM 866 NH2 ARG A 201 49.197 20.951 48.934 1.00111.65 N ANISOU 866 NH2 ARG A 201 15905 12912 13605 553 303 3487 N ATOM 867 N ALA A 202 43.170 21.977 51.647 1.00 88.03 N ANISOU 867 N ALA A 202 13340 10140 9966 -644 947 3252 N ATOM 868 CA ALA A 202 43.035 22.561 52.977 1.00 82.87 C ANISOU 868 CA ALA A 202 12736 9779 8970 -628 916 3322 C ATOM 869 C ALA A 202 42.316 21.608 53.921 1.00 91.04 C ANISOU 869 C ALA A 202 14029 10711 9850 -687 1135 3606 C ATOM 870 O ALA A 202 42.731 21.423 55.071 1.00 99.48 O ANISOU 870 O ALA A 202 15263 11912 10623 -542 1082 3823 O ATOM 871 CB ALA A 202 42.295 23.895 52.889 1.00 76.38 C ANISOU 871 CB ALA A 202 11730 9189 8103 -792 929 3032 C ATOM 872 N VAL A 203 41.235 20.982 53.445 1.00 90.48 N ANISOU 872 N VAL A 203 13998 10401 9979 -907 1377 3621 N ATOM 873 CA VAL A 203 40.486 20.027 54.253 1.00 90.42 C ANISOU 873 CA VAL A 203 14217 10260 9879 -1001 1617 3913 C ATOM 874 C VAL A 203 40.935 18.589 54.024 1.00 96.83 C ANISOU 874 C VAL A 203 15251 10695 10844 -916 1648 4168 C ATOM 875 O VAL A 203 40.406 17.677 54.673 1.00101.95 O ANISOU 875 O VAL A 203 16115 11182 11439 -988 1843 4450 O ATOM 876 CB VAL A 203 38.974 20.156 53.970 1.00 90.21 C ANISOU 876 CB VAL A 203 14086 10192 9998 -1318 1868 3816 C ATOM 877 CG1 VAL A 203 38.574 21.623 53.935 1.00 76.95 C ANISOU 877 CG1 VAL A 203 12166 8844 8229 -1374 1826 3520 C ATOM 878 CG2 VAL A 203 38.615 19.471 52.659 1.00 89.90 C ANISOU 878 CG2 VAL A 203 14007 9792 10358 -1484 1905 3723 C ATOM 879 N ALA A 204 41.899 18.359 53.133 1.00103.12 N ANISOU 879 N ALA A 204 12048 15583 11551 -1129 1165 5628 N ATOM 880 CA ALA A 204 42.289 17.001 52.774 1.00114.04 C ANISOU 880 CA ALA A 204 13563 16561 13206 -1249 978 5837 C ATOM 881 C ALA A 204 42.809 16.237 53.985 1.00131.24 C ANISOU 881 C ALA A 204 15741 18895 15231 -1155 960 6090 C ATOM 882 O ALA A 204 43.525 16.783 54.829 1.00139.29 O ANISOU 882 O ALA A 204 16764 20238 15923 -956 1038 6010 O ATOM 883 CB ALA A 204 43.356 17.028 51.678 1.00115.27 C ANISOU 883 CB ALA A 204 13933 16368 13496 -1246 843 5623 C ATOM 884 N SER A 205 42.447 14.952 54.054 1.00150.63 N ANISOU 884 N SER A 205 18188 21111 17935 -1297 844 6388 N ATOM 885 CA SER A 205 42.878 14.085 55.145 1.00162.96 C ANISOU 885 CA SER A 205 19744 22774 19399 -1236 810 6665 C ATOM 886 C SER A 205 44.379 13.825 55.134 1.00168.49 C ANISOU 886 C SER A 205 20651 23331 20035 -1117 690 6579 C ATOM 887 O SER A 205 44.948 13.492 56.180 1.00173.28 O ANISOU 887 O SER A 205 21261 24135 20442 -996 697 6726 O ATOM 888 CB SER A 205 42.133 12.752 55.065 1.00168.24 C ANISOU 888 CB SER A 205 20351 23170 20403 -1431 693 6990 C ATOM 889 OG SER A 205 40.806 12.925 54.593 1.00167.67 O ANISOU 889 OG SER A 205 20132 23073 20501 -1575 745 7012 O ATOM 890 N TRP A 206 45.028 13.968 53.977 1.00165.10 N ANISOU 890 N TRP A 206 20391 22566 19772 -1141 574 6345 N ATOM 891 CA TRP A 206 46.447 13.645 53.870 1.00165.11 C ANISOU 891 CA TRP A 206 20593 22387 19756 -1032 436 6268 C ATOM 892 C TRP A 206 47.298 14.623 54.670 1.00165.55 C ANISOU 892 C TRP A 206 20659 22846 19395 -786 553 6104 C ATOM 893 O TRP A 206 48.321 14.235 55.245 1.00162.82 O ANISOU 893 O TRP A 206 20413 22519 18932 -656 476 6152 O ATOM 894 CB TRP A 206 46.858 13.625 52.396 1.00160.94 C ANISOU 894 CB TRP A 206 20226 21416 19507 -1110 289 6046 C ATOM 895 CG TRP A 206 45.921 12.790 51.565 1.00159.71 C ANISOU 895 CG TRP A 206 20043 20889 19749 -1333 173 6147 C ATOM 896 CD1 TRP A 206 45.259 11.668 51.968 1.00163.25 C ANISOU 896 CD1 TRP A 206 20406 21233 20387 -1455 103 6444 C ATOM 897 CD2 TRP A 206 45.516 13.027 50.208 1.00154.15 C ANISOU 897 CD2 TRP A 206 19384 19889 19298 -1451 110 5944 C ATOM 898 NE1 TRP A 206 44.479 11.184 50.948 1.00162.39 N ANISOU 898 NE1 TRP A 206 20285 20781 20636 -1633 -8 6426 N ATOM 899 CE2 TRP A 206 44.618 11.999 49.856 1.00155.36 C ANISOU 899 CE2 TRP A 206 19479 19767 19784 -1631 -8 6115 C ATOM 900 CE3 TRP A 206 45.830 14.003 49.256 1.00150.24 C ANISOU 900 CE3 TRP A 206 18966 19337 18780 -1417 136 5636 C ATOM 901 CZ2 TRP A 206 44.031 11.917 48.596 1.00152.07 C ANISOU 901 CZ2 TRP A 206 19087 19030 19664 -1764 -106 5966 C ATOM 902 CZ3 TRP A 206 45.244 13.919 48.002 1.00148.71 C ANISOU 902 CZ3 TRP A 206 18800 18820 18884 -1560 46 5504 C ATOM 903 CH2 TRP A 206 44.355 12.883 47.685 1.00149.96 C ANISOU 903 CH2 TRP A 206 18907 18715 19357 -1724 -77 5658 C ATOM 904 N SER A 207 46.897 15.891 54.713 1.00166.59 N ANISOU 904 N SER A 207 20685 23300 19310 -708 725 5892 N ATOM 905 CA SER A 207 47.549 16.890 55.560 1.00162.92 C ANISOU 905 CA SER A 207 20192 23267 18444 -458 840 5707 C ATOM 906 C SER A 207 46.672 18.131 55.688 1.00162.15 C ANISOU 906 C SER A 207 19919 23520 18171 -416 1030 5521 C ATOM 907 O SER A 207 46.136 18.631 54.697 1.00163.30 O ANISOU 907 O SER A 207 20047 23521 18478 -528 1056 5372 O ATOM 908 CB SER A 207 48.925 17.271 55.007 1.00161.27 C ANISOU 908 CB SER A 207 20165 22924 18187 -319 747 5454 C ATOM 909 N VAL A 214 54.274 24.491 51.676 1.00117.98 N ANISOU 909 N VAL A 214 14915 17238 12674 671 684 2261 N ATOM 910 CA VAL A 214 52.957 24.948 51.235 1.00124.05 C ANISOU 910 CA VAL A 214 15568 18072 13494 517 798 2311 C ATOM 911 C VAL A 214 52.864 26.483 51.063 1.00124.76 C ANISOU 911 C VAL A 214 15526 18330 13546 619 875 1942 C ATOM 912 O VAL A 214 52.169 26.945 50.160 1.00126.54 O ANISOU 912 O VAL A 214 15708 18440 13930 491 920 1859 O ATOM 913 CB VAL A 214 51.846 24.424 52.183 1.00130.26 C ANISOU 913 CB VAL A 214 16249 19146 14096 442 892 2708 C ATOM 914 CG1 VAL A 214 50.472 24.884 51.709 1.00129.17 C ANISOU 914 CG1 VAL A 214 15982 19069 14028 281 1007 2759 C ATOM 915 CG2 VAL A 214 51.881 22.901 52.252 1.00132.47 C ANISOU 915 CG2 VAL A 214 16648 19214 14472 316 800 3094 C ATOM 916 N PRO A 215 53.541 27.288 51.896 1.00123.58 N ANISOU 916 N PRO A 215 15308 18442 13205 850 877 1716 N ATOM 917 CA PRO A 215 53.643 28.716 51.548 1.00119.55 C ANISOU 917 CA PRO A 215 14688 17995 12742 943 907 1332 C ATOM 918 C PRO A 215 54.462 28.954 50.293 1.00116.84 C ANISOU 918 C PRO A 215 14442 17273 12680 911 828 1087 C ATOM 919 O PRO A 215 54.162 29.886 49.535 1.00115.33 O ANISOU 919 O PRO A 215 14175 17019 12626 872 863 877 O ATOM 920 CB PRO A 215 54.298 29.343 52.786 1.00123.56 C ANISOU 920 CB PRO A 215 15114 18839 12995 1210 891 1159 C ATOM 921 CG PRO A 215 54.998 28.214 53.454 1.00129.12 C ANISOU 921 CG PRO A 215 15944 19531 13586 1265 816 1381 C ATOM 922 CD PRO A 215 54.089 27.037 53.242 1.00129.75 C ANISOU 922 CD PRO A 215 16080 19508 13710 1039 855 1799 C ATOM 923 N LYS A 216 55.493 28.141 50.055 1.00114.93 N ANISOU 923 N LYS A 216 14356 16786 12525 932 721 1114 N ATOM 924 CA LYS A 216 56.176 28.154 48.768 1.00105.81 C ANISOU 924 CA LYS A 216 13302 15265 11636 880 656 940 C ATOM 925 C LYS A 216 55.301 27.609 47.649 1.00104.35 C ANISOU 925 C LYS A 216 13177 14835 11637 648 675 1096 C ATOM 926 O LYS A 216 55.565 27.890 46.476 1.00105.28 O ANISOU 926 O LYS A 216 13338 14706 11956 597 653 929 O ATOM 927 CB LYS A 216 57.458 27.331 48.851 1.00102.91 C ANISOU 927 CB LYS A 216 13082 14714 11304 969 536 944 C ATOM 928 CG LYS A 216 58.394 27.735 49.986 1.00102.01 C ANISOU 928 CG LYS A 216 12924 14824 11011 1206 493 802 C ATOM 929 N TRP A 217 54.267 26.836 47.988 1.00101.97 N ANISOU 929 N TRP A 217 12872 14600 11273 510 711 1417 N ATOM 930 CA TRP A 217 53.432 26.222 46.962 1.00 94.63 C ANISOU 930 CA TRP A 217 12000 13419 10536 290 703 1572 C ATOM 931 C TRP A 217 52.619 27.267 46.209 1.00 91.03 C ANISOU 931 C TRP A 217 11435 12985 10166 214 787 1411 C ATOM 932 O TRP A 217 52.415 27.148 44.995 1.00 92.21 O ANISOU 932 O TRP A 217 11649 12866 10519 93 756 1365 O ATOM 933 CB TRP A 217 52.513 25.176 47.593 1.00 96.82 C ANISOU 933 CB TRP A 217 12273 13770 10745 162 717 1972 C ATOM 934 CG TRP A 217 51.659 24.446 46.606 1.00106.81 C ANISOU 934 CG TRP A 217 13593 14759 12230 -62 682 2145 C ATOM 935 CD1 TRP A 217 50.294 24.396 46.576 1.00111.18 C ANISOU 935 CD1 TRP A 217 14046 15391 12805 -225 756 2347 C ATOM 936 CD2 TRP A 217 52.115 23.665 45.497 1.00117.29 C ANISOU 936 CD2 TRP A 217 15083 15688 13794 -138 552 2116 C ATOM 937 NE1 TRP A 217 49.873 23.625 45.517 1.00116.63 N ANISOU 937 NE1 TRP A 217 14829 15742 13742 -401 670 2445 N ATOM 938 CE2 TRP A 217 50.972 23.167 44.838 1.00120.26 C ANISOU 938 CE2 TRP A 217 15453 15910 14330 -345 542 2298 C ATOM 939 CE3 TRP A 217 53.378 23.338 44.995 1.00118.70 C ANISOU 939 CE3 TRP A 217 15405 15631 14065 -41 440 1945 C ATOM 940 CZ2 TRP A 217 51.058 22.359 43.705 1.00121.67 C ANISOU 940 CZ2 TRP A 217 15770 15709 14751 -447 411 2298 C ATOM 941 CZ3 TRP A 217 53.460 22.537 43.871 1.00115.78 C ANISOU 941 CZ3 TRP A 217 15168 14899 13923 -140 325 1950 C ATOM 942 CH2 TRP A 217 52.308 22.057 43.239 1.00117.79 C ANISOU 942 CH2 TRP A 217 15419 15009 14327 -336 305 2118 C ATOM 943 N THR A 218 52.141 28.298 46.912 1.00 87.09 N ANISOU 943 N THR A 218 10769 12809 9514 292 886 1318 N ATOM 944 CA THR A 218 51.392 29.349 46.235 1.00 83.91 C ANISOU 944 CA THR A 218 10252 12428 9202 230 956 1154 C ATOM 945 C THR A 218 52.293 30.172 45.325 1.00 75.13 C ANISOU 945 C THR A 218 9164 11135 8247 304 913 829 C ATOM 946 O THR A 218 51.816 30.744 44.341 1.00 74.90 O ANISOU 946 O THR A 218 9101 10989 8369 213 938 726 O ATOM 947 CB THR A 218 50.686 30.250 47.254 1.00 88.19 C ANISOU 947 CB THR A 218 10599 13366 9543 314 1059 1118 C ATOM 948 OG1 THR A 218 49.800 31.143 46.570 1.00 91.07 O ANISOU 948 OG1 THR A 218 10854 13733 10017 226 1120 1001 O ATOM 949 CG2 THR A 218 51.684 31.073 48.049 1.00 86.68 C ANISOU 949 CG2 THR A 218 10347 13369 9220 557 1036 859 C ATOM 950 N ALA A 219 53.594 30.229 45.621 1.00 68.51 N ANISOU 950 N ALA A 219 8377 10269 7384 468 849 679 N ATOM 951 CA ALA A 219 54.516 30.941 44.744 1.00 55.35 C ANISOU 951 CA ALA A 219 6725 8422 5885 535 810 401 C ATOM 952 C ALA A 219 54.795 30.140 43.479 1.00 60.71 C ANISOU 952 C ALA A 219 7565 8753 6750 422 753 452 C ATOM 953 O ALA A 219 54.936 30.713 42.392 1.00 63.78 O ANISOU 953 O ALA A 219 7947 8988 7297 392 758 296 O ATOM 954 CB ALA A 219 55.816 31.253 45.488 1.00 47.91 C ANISOU 954 CB ALA A 219 5771 7562 4871 749 754 226 C ATOM 955 N VAL A 220 54.882 28.813 43.602 1.00 60.45 N ANISOU 955 N VAL A 220 7670 8597 6700 366 690 671 N ATOM 956 CA VAL A 220 55.002 27.963 42.423 1.00 57.51 C ANISOU 956 CA VAL A 220 7449 7902 6502 260 620 721 C ATOM 957 C VAL A 220 53.740 28.059 41.575 1.00 60.66 C ANISOU 957 C VAL A 220 7820 8229 6999 79 661 795 C ATOM 958 O VAL A 220 53.809 28.164 40.344 1.00 62.02 O ANISOU 958 O VAL A 220 8047 8197 7322 30 638 689 O ATOM 959 CB VAL A 220 55.312 26.513 42.844 1.00 59.16 C ANISOU 959 CB VAL A 220 7798 7994 6688 243 524 944 C ATOM 960 CG1 VAL A 220 54.955 25.540 41.736 1.00 57.84 C ANISOU 960 CG1 VAL A 220 7761 7520 6697 97 445 1048 C ATOM 961 CG2 VAL A 220 56.784 26.377 43.221 1.00 61.32 C ANISOU 961 CG2 VAL A 220 8134 8235 6931 422 456 814 C ATOM 962 N GLU A 221 52.569 28.050 42.217 1.00 57.46 N ANISOU 962 N GLU A 221 7321 8005 6505 -14 723 977 N ATOM 963 CA GLU A 221 51.320 28.193 41.476 1.00 51.90 C ANISOU 963 CA GLU A 221 6574 7246 5900 -184 760 1045 C ATOM 964 C GLU A 221 51.308 29.481 40.661 1.00 54.64 C ANISOU 964 C GLU A 221 6838 7595 6329 -160 811 788 C ATOM 965 O GLU A 221 51.011 29.467 39.461 1.00 55.85 O ANISOU 965 O GLU A 221 7042 7548 6629 -254 786 746 O ATOM 966 CB GLU A 221 50.122 28.162 42.427 1.00 52.41 C ANISOU 966 CB GLU A 221 6513 7559 5842 -262 839 1263 C ATOM 967 CG GLU A 221 49.777 26.786 42.979 1.00 66.19 C ANISOU 967 CG GLU A 221 8328 9260 7563 -353 790 1594 C ATOM 968 CD GLU A 221 48.681 26.849 44.033 1.00 77.94 C ANISOU 968 CD GLU A 221 9665 11048 8900 -405 891 1818 C ATOM 969 OE1 GLU A 221 47.759 26.005 43.996 1.00 83.22 O ANISOU 969 OE1 GLU A 221 10334 11647 9640 -570 877 2098 O ATOM 970 OE2 GLU A 221 48.743 27.750 44.897 1.00 78.41 O ANISOU 970 OE2 GLU A 221 9596 11420 8777 -275 979 1711 O ATOM 971 N ILE A 222 51.638 30.609 41.302 1.00 53.87 N ANISOU 971 N ILE A 222 6607 7720 6142 -28 871 613 N ATOM 972 CA ILE A 222 51.596 31.903 40.620 1.00 57.65 C ANISOU 972 CA ILE A 222 6981 8206 6717 -6 912 384 C ATOM 973 C ILE A 222 52.472 31.876 39.374 1.00 58.28 C ANISOU 973 C ILE A 222 7168 8023 6954 11 859 252 C ATOM 974 O ILE A 222 52.065 32.327 38.296 1.00 61.17 O ANISOU 974 O ILE A 222 7521 8277 7443 -67 872 189 O ATOM 975 CB ILE A 222 52.021 33.034 41.572 1.00 53.80 C ANISOU 975 CB ILE A 222 6337 7970 6134 161 950 199 C ATOM 976 CG1 ILE A 222 50.953 33.272 42.629 1.00 57.99 C ANISOU 976 CG1 ILE A 222 6732 8794 6506 147 1020 300 C ATOM 977 CG2 ILE A 222 52.274 34.314 40.795 1.00 49.30 C ANISOU 977 CG2 ILE A 222 5671 7349 5713 199 962 -43 C ATOM 978 CD1 ILE A 222 49.679 33.845 42.068 1.00 61.13 C ANISOU 978 CD1 ILE A 222 7029 9214 6982 12 1078 313 C ATOM 979 N VAL A 223 53.689 31.344 39.503 1.00 51.08 N ANISOU 979 N VAL A 223 6357 7019 6032 119 799 212 N ATOM 980 CA VAL A 223 54.582 31.260 38.351 1.00 47.88 C ANISOU 980 CA VAL A 223 6048 6387 5759 152 756 93 C ATOM 981 C VAL A 223 53.970 30.375 37.272 1.00 49.65 C ANISOU 981 C VAL A 223 6401 6395 6070 10 712 210 C ATOM 982 O VAL A 223 53.902 30.758 36.098 1.00 58.10 O ANISOU 982 O VAL A 223 7482 7348 7246 -25 719 120 O ATOM 983 CB VAL A 223 55.974 30.763 38.783 1.00 47.43 C ANISOU 983 CB VAL A 223 6070 6281 5671 299 696 38 C ATOM 984 CG1 VAL A 223 56.870 30.573 37.568 1.00 50.84 C ANISOU 984 CG1 VAL A 223 6598 6490 6230 336 659 -70 C ATOM 985 CG2 VAL A 223 56.591 31.757 39.755 1.00 40.31 C ANISOU 985 CG2 VAL A 223 5027 5582 4706 451 724 -113 C ATOM 986 N LEU A 224 53.485 29.191 37.656 1.00 47.06 N ANISOU 986 N LEU A 224 6165 6013 5703 -73 658 417 N ATOM 987 CA LEU A 224 52.907 28.281 36.671 1.00 45.44 C ANISOU 987 CA LEU A 224 6081 5582 5603 -202 585 519 C ATOM 988 C LEU A 224 51.698 28.896 35.973 1.00 50.41 C ANISOU 988 C LEU A 224 6632 6224 6296 -331 633 522 C ATOM 989 O LEU A 224 51.530 28.737 34.758 1.00 57.86 O ANISOU 989 O LEU A 224 7649 6991 7343 -382 589 473 O ATOM 990 CB LEU A 224 52.520 26.959 37.331 1.00 49.58 C ANISOU 990 CB LEU A 224 6686 6049 6104 -277 510 765 C ATOM 991 CG LEU A 224 53.658 25.984 37.631 1.00 57.31 C ANISOU 991 CG LEU A 224 7795 6905 7074 -177 413 784 C ATOM 992 CD1 LEU A 224 53.081 24.599 37.843 1.00 61.32 C ANISOU 992 CD1 LEU A 224 8395 7270 7635 -294 308 1038 C ATOM 993 CD2 LEU A 224 54.692 25.977 36.513 1.00 52.50 C ANISOU 993 CD2 LEU A 224 7284 6111 6553 -82 363 578 C ATOM 994 N ILE A 225 50.844 29.601 36.721 1.00 47.67 N ANISOU 994 N ILE A 225 6135 6094 5882 -376 718 571 N ATOM 995 CA ILE A 225 49.642 30.191 36.132 1.00 47.37 C ANISOU 995 CA ILE A 225 6012 6077 5910 -501 760 579 C ATOM 996 C ILE A 225 50.015 31.194 35.046 1.00 50.39 C ANISOU 996 C ILE A 225 6368 6401 6378 -454 783 368 C ATOM 997 O ILE A 225 49.481 31.160 33.932 1.00 53.76 O ANISOU 997 O ILE A 225 6837 6690 6899 -541 755 359 O ATOM 998 CB ILE A 225 48.771 30.843 37.222 1.00 53.06 C ANISOU 998 CB ILE A 225 6559 7071 6532 -526 853 645 C ATOM 999 CG1 ILE A 225 48.266 29.792 38.209 1.00 53.54 C ANISOU 999 CG1 ILE A 225 6636 7198 6509 -590 840 903 C ATOM 1000 CG2 ILE A 225 47.599 31.578 36.601 1.00 51.72 C ANISOU 1000 CG2 ILE A 225 6286 6924 6441 -640 896 624 C ATOM 1001 CD1 ILE A 225 47.761 30.373 39.508 1.00 46.04 C ANISOU 1001 CD1 ILE A 225 5519 6572 5402 -551 939 956 C ATOM 1002 N TRP A 226 50.943 32.102 35.352 1.00 49.05 N ANISOU 1002 N TRP A 226 6120 6336 6181 -315 828 202 N ATOM 1003 CA TRP A 226 51.291 33.149 34.395 1.00 45.48 C ANISOU 1003 CA TRP A 226 5611 5845 5824 -274 857 29 C ATOM 1004 C TRP A 226 52.118 32.599 33.239 1.00 47.71 C ANISOU 1004 C TRP A 226 6041 5917 6170 -235 802 -22 C ATOM 1005 O TRP A 226 51.883 32.949 32.076 1.00 56.74 O ANISOU 1005 O TRP A 226 7194 6972 7391 -274 805 -71 O ATOM 1006 CB TRP A 226 52.027 34.283 35.109 1.00 44.62 C ANISOU 1006 CB TRP A 226 5356 5898 5701 -138 907 -126 C ATOM 1007 CG TRP A 226 51.097 35.128 35.910 1.00 44.89 C ANISOU 1007 CG TRP A 226 5218 6140 5697 -166 961 -133 C ATOM 1008 CD1 TRP A 226 50.489 34.789 37.081 1.00 47.51 C ANISOU 1008 CD1 TRP A 226 5507 6643 5900 -182 980 -24 C ATOM 1009 CD2 TRP A 226 50.651 36.453 35.594 1.00 43.93 C ANISOU 1009 CD2 TRP A 226 4936 6087 5667 -175 1001 -253 C ATOM 1010 NE1 TRP A 226 49.694 35.821 37.516 1.00 54.88 N ANISOU 1010 NE1 TRP A 226 6263 7760 6827 -190 1033 -86 N ATOM 1011 CE2 TRP A 226 49.776 36.855 36.622 1.00 47.41 C ANISOU 1011 CE2 TRP A 226 5243 6742 6027 -188 1039 -232 C ATOM 1012 CE3 TRP A 226 50.907 37.338 34.541 1.00 42.52 C ANISOU 1012 CE3 TRP A 226 4707 5814 5634 -169 1006 -366 C ATOM 1013 CZ2 TRP A 226 49.157 38.102 36.631 1.00 45.64 C ANISOU 1013 CZ2 TRP A 226 4840 6627 5874 -191 1070 -344 C ATOM 1014 CZ3 TRP A 226 50.292 38.576 34.551 1.00 43.66 C ANISOU 1014 CZ3 TRP A 226 4674 6055 5859 -184 1035 -455 C ATOM 1015 CH2 TRP A 226 49.427 38.948 35.590 1.00 45.40 C ANISOU 1015 CH2 TRP A 226 4766 6475 6008 -193 1060 -455 C ATOM 1016 N VAL A 227 53.089 31.733 33.535 1.00 41.57 N ANISOU 1016 N VAL A 227 5375 5066 5352 -150 751 -12 N ATOM 1017 CA VAL A 227 53.904 31.144 32.474 1.00 40.38 C ANISOU 1017 CA VAL A 227 5362 4730 5250 -94 695 -71 C ATOM 1018 C VAL A 227 53.032 30.346 31.510 1.00 47.24 C ANISOU 1018 C VAL A 227 6346 5439 6164 -213 625 11 C ATOM 1019 O VAL A 227 53.111 30.517 30.287 1.00 61.10 O ANISOU 1019 O VAL A 227 8142 7105 7969 -203 617 -67 O ATOM 1020 CB VAL A 227 55.026 30.275 33.069 1.00 40.21 C ANISOU 1020 CB VAL A 227 5437 4658 5183 16 639 -69 C ATOM 1021 CG1 VAL A 227 55.686 29.442 31.976 1.00 37.34 C ANISOU 1021 CG1 VAL A 227 5228 4094 4864 65 564 -117 C ATOM 1022 CG2 VAL A 227 56.051 31.152 33.770 1.00 38.38 C ANISOU 1022 CG2 VAL A 227 5092 4558 4932 155 694 -192 C ATOM 1023 N VAL A 228 52.175 29.473 32.044 1.00 49.82 N ANISOU 1023 N VAL A 228 6718 5734 6478 -322 570 174 N ATOM 1024 CA VAL A 228 51.368 28.615 31.179 1.00 49.68 C ANISOU 1024 CA VAL A 228 6808 5537 6531 -432 474 249 C ATOM 1025 C VAL A 228 50.326 29.433 30.420 1.00 55.68 C ANISOU 1025 C VAL A 228 7487 6329 7339 -529 516 226 C ATOM 1026 O VAL A 228 50.073 29.189 29.235 1.00 55.48 O ANISOU 1026 O VAL A 228 7543 6168 7370 -553 454 182 O ATOM 1027 CB VAL A 228 50.723 27.481 31.995 1.00 45.11 C ANISOU 1027 CB VAL A 228 6276 4905 5958 -533 398 455 C ATOM 1028 CG1 VAL A 228 49.661 26.774 31.185 1.00 43.64 C ANISOU 1028 CG1 VAL A 228 6158 4545 5879 -669 296 539 C ATOM 1029 CG2 VAL A 228 51.786 26.487 32.444 1.00 41.30 C ANISOU 1029 CG2 VAL A 228 5909 4329 5455 -436 319 475 C ATOM 1030 N SER A 229 49.709 30.415 31.080 1.00 55.02 N ANISOU 1030 N SER A 229 7243 6430 7233 -575 613 246 N ATOM 1031 CA SER A 229 48.716 31.237 30.395 1.00 48.17 C ANISOU 1031 CA SER A 229 6288 5592 6421 -665 648 222 C ATOM 1032 C SER A 229 49.349 32.031 29.260 1.00 49.04 C ANISOU 1032 C SER A 229 6397 5673 6563 -582 675 64 C ATOM 1033 O SER A 229 48.754 32.179 28.186 1.00 54.69 O ANISOU 1033 O SER A 229 7136 6313 7330 -638 647 46 O ATOM 1034 CB SER A 229 48.033 32.180 31.385 1.00 44.21 C ANISOU 1034 CB SER A 229 5602 5307 5890 -706 744 250 C ATOM 1035 OG SER A 229 47.459 31.459 32.458 1.00 52.76 O ANISOU 1035 OG SER A 229 6673 6451 6922 -774 736 417 O ATOM 1036 N VAL A 230 50.564 32.537 29.475 1.00 45.82 N ANISOU 1036 N VAL A 230 5956 5325 6129 -444 726 -41 N ATOM 1037 CA VAL A 230 51.228 33.330 28.448 1.00 46.45 C ANISOU 1037 CA VAL A 230 6009 5392 6246 -362 764 -162 C ATOM 1038 C VAL A 230 51.674 32.442 27.290 1.00 50.56 C ANISOU 1038 C VAL A 230 6700 5752 6758 -316 690 -189 C ATOM 1039 O VAL A 230 51.505 32.800 26.117 1.00 52.25 O ANISOU 1039 O VAL A 230 6925 5932 6994 -315 692 -232 O ATOM 1040 CB VAL A 230 52.398 34.117 29.068 1.00 47.60 C ANISOU 1040 CB VAL A 230 6051 5643 6393 -231 833 -257 C ATOM 1041 CG1 VAL A 230 53.310 34.671 27.990 1.00 49.20 C ANISOU 1041 CG1 VAL A 230 6242 5810 6642 -134 866 -351 C ATOM 1042 CG2 VAL A 230 51.861 35.248 29.934 1.00 45.19 C ANISOU 1042 CG2 VAL A 230 5555 5501 6115 -262 895 -274 C ATOM 1043 N VAL A 231 52.219 31.261 27.596 1.00 48.31 N ANISOU 1043 N VAL A 231 6547 5371 6438 -270 615 -167 N ATOM 1044 CA VAL A 231 52.646 30.331 26.551 1.00 46.65 C ANISOU 1044 CA VAL A 231 6500 5006 6220 -209 525 -214 C ATOM 1045 C VAL A 231 51.469 29.953 25.658 1.00 48.20 C ANISOU 1045 C VAL A 231 6761 5102 6452 -317 443 -177 C ATOM 1046 O VAL A 231 51.560 30.000 24.425 1.00 58.33 O ANISOU 1046 O VAL A 231 8101 6338 7724 -267 418 -255 O ATOM 1047 CB VAL A 231 53.308 29.088 27.175 1.00 44.09 C ANISOU 1047 CB VAL A 231 6296 4581 5876 -154 437 -187 C ATOM 1048 CG1 VAL A 231 53.404 27.959 26.155 1.00 35.77 C ANISOU 1048 CG1 VAL A 231 5414 3342 4835 -116 304 -231 C ATOM 1049 CG2 VAL A 231 54.689 29.440 27.712 1.00 45.28 C ANISOU 1049 CG2 VAL A 231 6403 4810 5993 -9 504 -264 C ATOM 1050 N LEU A 232 50.340 29.584 26.268 1.00 44.67 N ANISOU 1050 N LEU A 232 6297 4630 6044 -463 398 -54 N ATOM 1051 CA LEU A 232 49.162 29.179 25.506 1.00 45.86 C ANISOU 1051 CA LEU A 232 6499 4671 6253 -576 304 -12 C ATOM 1052 C LEU A 232 48.529 30.333 24.735 1.00 45.47 C ANISOU 1052 C LEU A 232 6354 4707 6217 -616 371 -55 C ATOM 1053 O LEU A 232 47.724 30.086 23.831 1.00 47.27 O ANISOU 1053 O LEU A 232 6636 4843 6483 -676 287 -58 O ATOM 1054 CB LEU A 232 48.125 28.548 26.440 1.00 44.65 C ANISOU 1054 CB LEU A 232 6324 4483 6158 -728 253 155 C ATOM 1055 CG LEU A 232 48.561 27.266 27.154 1.00 45.87 C ANISOU 1055 CG LEU A 232 6578 4524 6326 -714 158 239 C ATOM 1056 CD1 LEU A 232 47.461 26.738 28.048 1.00 43.67 C ANISOU 1056 CD1 LEU A 232 6249 4233 6111 -875 124 441 C ATOM 1057 CD2 LEU A 232 48.980 26.206 26.153 1.00 51.82 C ANISOU 1057 CD2 LEU A 232 7506 5065 7119 -644 1 156 C ATOM 1058 N ALA A 233 48.863 31.577 25.068 1.00 40.74 N ANISOU 1058 N ALA A 233 5610 4270 5600 -582 504 -90 N ATOM 1059 CA ALA A 233 48.354 32.731 24.340 1.00 42.74 C ANISOU 1059 CA ALA A 233 5761 4598 5882 -612 563 -125 C ATOM 1060 C ALA A 233 49.273 33.172 23.208 1.00 48.11 C ANISOU 1060 C ALA A 233 6468 5286 6524 -480 596 -224 C ATOM 1061 O ALA A 233 48.872 34.017 22.402 1.00 46.56 O ANISOU 1061 O ALA A 233 6207 5134 6349 -499 628 -239 O ATOM 1062 CB ALA A 233 48.128 33.903 25.301 1.00 31.69 C ANISOU 1062 CB ALA A 233 4168 3361 4511 -650 673 -108 C ATOM 1063 N VAL A 234 50.484 32.612 23.127 1.00 49.45 N ANISOU 1063 N VAL A 234 6725 5423 6640 -347 589 -282 N ATOM 1064 CA VAL A 234 51.432 33.045 22.097 1.00 49.72 C ANISOU 1064 CA VAL A 234 6766 5496 6631 -210 639 -363 C ATOM 1065 C VAL A 234 50.897 32.833 20.689 1.00 53.82 C ANISOU 1065 C VAL A 234 7374 5963 7111 -204 573 -389 C ATOM 1066 O VAL A 234 51.046 33.741 19.855 1.00 44.94 O ANISOU 1066 O VAL A 234 6178 4924 5972 -160 643 -402 O ATOM 1067 CB VAL A 234 52.800 32.384 22.331 1.00 46.42 C ANISOU 1067 CB VAL A 234 6422 5051 6164 -65 639 -422 C ATOM 1068 CG1 VAL A 234 53.672 32.513 21.089 1.00 47.72 C ANISOU 1068 CG1 VAL A 234 6623 5244 6264 83 671 -498 C ATOM 1069 CG2 VAL A 234 53.484 33.013 23.533 1.00 37.62 C ANISOU 1069 CG2 VAL A 234 5178 4029 5087 -41 728 -415 C ATOM 1070 N PRO A 235 50.277 31.693 20.336 1.00 55.43 N ANISOU 1070 N PRO A 235 7726 6030 7304 -239 430 -397 N ATOM 1071 CA PRO A 235 49.751 31.546 18.965 1.00 48.17 C ANISOU 1071 CA PRO A 235 6888 5073 6341 -217 353 -443 C ATOM 1072 C PRO A 235 48.828 32.671 18.521 1.00 53.49 C ANISOU 1072 C PRO A 235 7446 5828 7050 -310 404 -396 C ATOM 1073 O PRO A 235 48.712 32.926 17.315 1.00 57.89 O ANISOU 1073 O PRO A 235 8034 6415 7547 -252 388 -433 O ATOM 1074 CB PRO A 235 49.014 30.203 19.025 1.00 48.68 C ANISOU 1074 CB PRO A 235 7093 4955 6448 -283 172 -443 C ATOM 1075 CG PRO A 235 49.779 29.422 20.027 1.00 50.38 C ANISOU 1075 CG PRO A 235 7352 5113 6677 -249 157 -432 C ATOM 1076 CD PRO A 235 50.183 30.422 21.082 1.00 57.30 C ANISOU 1076 CD PRO A 235 8070 6133 7568 -275 318 -372 C ATOM 1077 N GLU A 236 48.167 33.357 19.453 1.00 57.57 N ANISOU 1077 N GLU A 236 7826 6389 7658 -443 462 -317 N ATOM 1078 CA GLU A 236 47.397 34.541 19.088 1.00 52.49 C ANISOU 1078 CA GLU A 236 7052 5828 7064 -520 516 -279 C ATOM 1079 C GLU A 236 48.299 35.615 18.488 1.00 46.15 C ANISOU 1079 C GLU A 236 6155 5146 6232 -410 633 -297 C ATOM 1080 O GLU A 236 47.993 36.183 17.435 1.00 43.51 O ANISOU 1080 O GLU A 236 5802 4852 5876 -396 637 -289 O ATOM 1081 CB GLU A 236 46.656 35.080 20.310 1.00 48.85 C ANISOU 1081 CB GLU A 236 6448 5410 6702 -658 561 -211 C ATOM 1082 CG GLU A 236 45.518 34.203 20.784 1.00 43.94 C ANISOU 1082 CG GLU A 236 5879 4689 6129 -793 457 -153 C ATOM 1083 CD GLU A 236 44.389 34.119 19.780 1.00 49.93 C ANISOU 1083 CD GLU A 236 6678 5375 6917 -869 359 -149 C ATOM 1084 OE1 GLU A 236 44.455 33.239 18.898 1.00 59.23 O ANISOU 1084 OE1 GLU A 236 8011 6445 8050 -813 244 -198 O ATOM 1085 OE2 GLU A 236 43.442 34.935 19.863 1.00 50.02 O ANISOU 1085 OE2 GLU A 236 6567 5438 7001 -973 385 -108 O ATOM 1086 N ALA A 237 49.419 35.910 19.152 1.00 42.39 N ANISOU 1086 N ALA A 237 5613 4731 5764 -331 725 -310 N ATOM 1087 CA ALA A 237 50.360 36.892 18.626 1.00 43.43 C ANISOU 1087 CA ALA A 237 5639 4966 5896 -227 835 -309 C ATOM 1088 C ALA A 237 51.025 36.423 17.341 1.00 46.14 C ANISOU 1088 C ALA A 237 6098 5322 6111 -85 824 -345 C ATOM 1089 O ALA A 237 51.555 37.255 16.597 1.00 52.80 O ANISOU 1089 O ALA A 237 6854 6264 6945 -11 910 -312 O ATOM 1090 CB ALA A 237 51.425 37.222 19.675 1.00 28.51 C ANISOU 1090 CB ALA A 237 3650 3121 4060 -171 917 -325 C ATOM 1091 N ILE A 238 50.991 35.120 17.055 1.00 49.07 N ANISOU 1091 N ILE A 238 6654 5600 6390 -40 716 -409 N ATOM 1092 CA ILE A 238 51.619 34.610 15.842 1.00 53.69 C ANISOU 1092 CA ILE A 238 7354 6212 6835 120 694 -471 C ATOM 1093 C ILE A 238 50.675 34.732 14.655 1.00 53.36 C ANISOU 1093 C ILE A 238 7360 6183 6733 101 627 -466 C ATOM 1094 O ILE A 238 51.035 35.290 13.613 1.00 53.26 O ANISOU 1094 O ILE A 238 7315 6288 6632 201 689 -448 O ATOM 1095 CB ILE A 238 52.081 33.153 16.040 1.00 53.55 C ANISOU 1095 CB ILE A 238 7509 6082 6757 200 587 -566 C ATOM 1096 CG1 ILE A 238 53.086 33.068 17.189 1.00 55.66 C ANISOU 1096 CG1 ILE A 238 7726 6347 7074 231 654 -567 C ATOM 1097 CG2 ILE A 238 52.683 32.603 14.748 1.00 48.07 C ANISOU 1097 CG2 ILE A 238 6932 5428 5906 385 552 -658 C ATOM 1098 CD1 ILE A 238 54.187 34.120 17.118 1.00 60.54 C ANISOU 1098 CD1 ILE A 238 8193 7107 7703 323 815 -538 C ATOM 1099 N GLY A 239 49.447 34.233 14.803 1.00 53.62 N ANISOU 1099 N GLY A 239 7459 6100 6814 -26 499 -471 N ATOM 1100 CA GLY A 239 48.554 34.143 13.661 1.00 57.40 C ANISOU 1100 CA GLY A 239 8010 6568 7233 -30 400 -492 C ATOM 1101 C GLY A 239 47.949 35.472 13.251 1.00 59.69 C ANISOU 1101 C GLY A 239 8155 6957 7566 -103 475 -399 C ATOM 1102 O GLY A 239 47.692 35.704 12.067 1.00 71.91 O ANISOU 1102 O GLY A 239 9735 8569 9019 -40 448 -403 O ATOM 1103 N PHE A 240 47.692 36.351 14.214 1.00 53.95 N ANISOU 1103 N PHE A 240 7267 6248 6982 -229 559 -321 N ATOM 1104 CA PHE A 240 46.980 37.584 13.907 1.00 50.01 C ANISOU 1104 CA PHE A 240 6627 5816 6560 -315 603 -239 C ATOM 1105 C PHE A 240 47.902 38.559 13.192 1.00 53.10 C ANISOU 1105 C PHE A 240 6916 6351 6910 -202 729 -179 C ATOM 1106 O PHE A 240 49.027 38.803 13.635 1.00 55.59 O ANISOU 1106 O PHE A 240 7163 6718 7242 -128 833 -169 O ATOM 1107 CB PHE A 240 46.425 38.219 15.182 1.00 41.91 C ANISOU 1107 CB PHE A 240 5450 4768 5704 -469 642 -193 C ATOM 1108 CG PHE A 240 45.035 37.764 15.529 1.00 46.30 C ANISOU 1108 CG PHE A 240 6040 5224 6326 -619 529 -194 C ATOM 1109 CD1 PHE A 240 43.931 38.378 14.958 1.00 41.72 C ANISOU 1109 CD1 PHE A 240 5406 4646 5799 -707 485 -158 C ATOM 1110 CD2 PHE A 240 44.830 36.726 16.425 1.00 42.48 C ANISOU 1110 CD2 PHE A 240 5634 4643 5862 -674 467 -217 C ATOM 1111 CE1 PHE A 240 42.647 37.964 15.269 1.00 35.53 C ANISOU 1111 CE1 PHE A 240 4638 3770 5090 -847 383 -154 C ATOM 1112 CE2 PHE A 240 43.547 36.306 16.740 1.00 40.99 C ANISOU 1112 CE2 PHE A 240 5458 4365 5750 -818 369 -194 C ATOM 1113 CZ PHE A 240 42.453 36.928 16.161 1.00 37.32 C ANISOU 1113 CZ PHE A 240 4932 3904 5342 -904 328 -166 C ATOM 1114 N ASP A 241 47.431 39.107 12.075 1.00 51.58 N ANISOU 1114 N ASP A 241 6708 6222 6667 -186 716 -129 N ATOM 1115 CA ASP A 241 48.150 40.182 11.413 1.00 46.17 C ANISOU 1115 CA ASP A 241 5892 5677 5972 -105 839 -26 C ATOM 1116 C ASP A 241 47.149 41.039 10.657 1.00 39.67 C ANISOU 1116 C ASP A 241 5001 4888 5185 -178 806 58 C ATOM 1117 O ASP A 241 45.972 40.695 10.530 1.00 41.49 O ANISOU 1117 O ASP A 241 5305 5038 5422 -269 685 18 O ATOM 1118 CB ASP A 241 49.248 39.646 10.489 1.00 42.10 C ANISOU 1118 CB ASP A 241 5473 5265 5257 97 882 -49 C ATOM 1119 CG ASP A 241 50.532 40.441 10.599 1.00 47.81 C ANISOU 1119 CG ASP A 241 6040 6098 6027 178 1044 42 C ATOM 1120 OD1 ASP A 241 50.460 41.687 10.678 1.00 42.61 O ANISOU 1120 OD1 ASP A 241 5192 5480 5518 109 1117 165 O ATOM 1121 OD2 ASP A 241 51.614 39.819 10.627 1.00 51.13 O ANISOU 1121 OD2 ASP A 241 6517 6554 6355 311 1090 -11 O ATOM 1122 N ILE A 242 47.627 42.177 10.181 1.00 37.92 N ANISOU 1122 N ILE A 242 4624 4776 5007 -142 911 186 N ATOM 1123 CA ILE A 242 46.793 43.105 9.429 1.00 43.05 C ANISOU 1123 CA ILE A 242 5190 5465 5702 -202 887 291 C ATOM 1124 C ILE A 242 46.687 42.633 7.987 1.00 46.04 C ANISOU 1124 C ILE A 242 5711 5939 5843 -74 838 295 C ATOM 1125 O ILE A 242 47.682 42.219 7.379 1.00 43.67 O ANISOU 1125 O ILE A 242 5474 5749 5368 93 900 294 O ATOM 1126 CB ILE A 242 47.375 44.528 9.502 1.00 43.87 C ANISOU 1126 CB ILE A 242 5056 5638 5974 -215 1007 445 C ATOM 1127 CG1 ILE A 242 47.400 45.023 10.950 1.00 43.55 C ANISOU 1127 CG1 ILE A 242 4871 5504 6171 -329 1030 409 C ATOM 1128 CG2 ILE A 242 46.587 45.468 8.608 1.00 37.30 C ANISOU 1128 CG2 ILE A 242 4140 4851 5181 -262 978 572 C ATOM 1129 CD1 ILE A 242 46.045 45.265 11.516 1.00 38.25 C ANISOU 1129 CD1 ILE A 242 4165 4736 5631 -489 934 364 C ATOM 1130 N ILE A 243 45.481 42.693 7.430 1.00 47.18 N ANISOU 1130 N ILE A 243 5902 6050 5973 -142 723 293 N ATOM 1131 CA ILE A 243 45.282 42.551 5.995 1.00 48.68 C ANISOU 1131 CA ILE A 243 6190 6354 5951 -22 673 319 C ATOM 1132 C ILE A 243 44.800 43.897 5.466 1.00 51.32 C ANISOU 1132 C ILE A 243 6361 6754 6383 -85 704 494 C ATOM 1133 O ILE A 243 43.822 44.466 5.970 1.00 47.13 O ANISOU 1133 O ILE A 243 5742 6119 6048 -249 646 509 O ATOM 1134 CB ILE A 243 44.323 41.395 5.650 1.00 48.61 C ANISOU 1134 CB ILE A 243 6387 6249 5832 -21 485 158 C ATOM 1135 CG1 ILE A 243 44.402 41.063 4.162 1.00 60.90 C ANISOU 1135 CG1 ILE A 243 8069 7952 7120 163 433 145 C ATOM 1136 CG2 ILE A 243 42.880 41.697 6.027 1.00 47.30 C ANISOU 1136 CG2 ILE A 243 6180 5948 5843 -213 371 153 C ATOM 1137 CD1 ILE A 243 43.539 39.912 3.773 1.00 67.29 C ANISOU 1137 CD1 ILE A 243 9076 8658 7832 185 227 -32 C ATOM 1138 N THR A 244 45.536 44.441 4.504 1.00 51.67 N ANISOU 1138 N THR A 244 6348 6978 6305 47 802 638 N ATOM 1139 CA THR A 244 45.197 45.707 3.875 1.00 50.43 C ANISOU 1139 CA THR A 244 6034 6897 6229 6 833 836 C ATOM 1140 C THR A 244 44.576 45.436 2.511 1.00 55.11 C ANISOU 1140 C THR A 244 6757 7600 6581 106 738 846 C ATOM 1141 O THR A 244 45.157 44.721 1.688 1.00 53.71 O ANISOU 1141 O THR A 244 6713 7566 6129 295 752 806 O ATOM 1142 CB THR A 244 46.436 46.597 3.730 1.00 49.87 C ANISOU 1142 CB THR A 244 5780 6958 6211 78 1011 1033 C ATOM 1143 OG1 THR A 244 47.132 46.664 4.983 1.00 50.27 O ANISOU 1143 OG1 THR A 244 5735 6911 6455 18 1084 986 O ATOM 1144 CG2 THR A 244 46.043 48.004 3.304 1.00 39.00 C ANISOU 1144 CG2 THR A 244 4206 5614 5000 -1 1030 1256 C ATOM 1145 N MET A 245 43.396 46.003 2.283 1.00 55.12 N ANISOU 1145 N MET A 245 6719 7539 6684 -10 634 889 N ATOM 1146 CA MET A 245 42.685 45.894 1.021 1.00 49.05 C ANISOU 1146 CA MET A 245 6055 6866 5715 71 526 906 C ATOM 1147 C MET A 245 42.594 47.277 0.406 1.00 54.72 C ANISOU 1147 C MET A 245 6590 7686 6517 44 585 1162 C ATOM 1148 O MET A 245 42.336 48.255 1.113 1.00 58.32 O ANISOU 1148 O MET A 245 6859 8034 7267 -115 611 1254 O ATOM 1149 CB MET A 245 41.271 45.340 1.212 1.00 61.10 C ANISOU 1149 CB MET A 245 7695 8220 7301 -45 326 740 C ATOM 1150 CG MET A 245 41.179 44.100 2.063 1.00 81.23 C ANISOU 1150 CG MET A 245 10383 10615 9866 -79 253 517 C ATOM 1151 SD MET A 245 40.759 42.664 1.056 1.00 96.09 S ANISOU 1151 SD MET A 245 12539 12513 11458 81 62 314 S ATOM 1152 CE MET A 245 40.403 41.454 2.328 1.00 98.94 C ANISOU 1152 CE MET A 245 12998 12625 11971 -40 -38 105 C ATOM 1153 N ASP A 246 42.802 47.359 -0.906 1.00 55.97 N ANISOU 1153 N ASP A 246 6795 8054 6417 208 599 1275 N ATOM 1154 CA ASP A 246 42.664 48.612 -1.636 1.00 53.55 C ANISOU 1154 CA ASP A 246 6326 7859 6163 196 642 1544 C ATOM 1155 C ASP A 246 41.939 48.326 -2.938 1.00 66.20 C ANISOU 1155 C ASP A 246 8072 9592 7489 314 517 1538 C ATOM 1156 O ASP A 246 42.417 47.534 -3.757 1.00 67.51 O ANISOU 1156 O ASP A 246 8390 9940 7322 523 524 1475 O ATOM 1157 CB ASP A 246 44.030 49.253 -1.895 1.00 59.89 C ANISOU 1157 CB ASP A 246 6972 8841 6943 296 848 1779 C ATOM 1158 CG ASP A 246 43.928 50.592 -2.591 1.00 68.55 C ANISOU 1158 CG ASP A 246 7875 10036 8135 269 893 2093 C ATOM 1159 OD1 ASP A 246 43.671 50.621 -3.814 1.00 74.06 O ANISOU 1159 OD1 ASP A 246 8639 10922 8579 394 861 2198 O ATOM 1160 OD2 ASP A 246 44.099 51.621 -1.904 1.00 71.97 O ANISOU 1160 OD2 ASP A 246 8085 10355 8905 127 949 2233 O ATOM 1161 N TYR A 247 40.789 48.960 -3.125 1.00 47.17 N ANISOU 1161 N TYR A 247 5612 7095 5214 192 394 1590 N ATOM 1162 CA TYR A 247 40.049 48.802 -4.365 1.00 56.04 C ANISOU 1162 CA TYR A 247 6858 8341 6094 300 262 1597 C ATOM 1163 C TYR A 247 39.271 50.081 -4.628 1.00 60.62 C ANISOU 1163 C TYR A 247 7272 8887 6875 173 218 1809 C ATOM 1164 O TYR A 247 38.445 50.480 -3.802 1.00 50.69 O ANISOU 1164 O TYR A 247 5929 7404 5926 -29 138 1754 O ATOM 1165 CB TYR A 247 39.121 47.586 -4.298 1.00 50.11 C ANISOU 1165 CB TYR A 247 6330 7456 5255 299 58 1289 C ATOM 1166 CG TYR A 247 38.413 47.309 -5.599 1.00 51.09 C ANISOU 1166 CG TYR A 247 6596 7710 5107 439 -99 1257 C ATOM 1167 CD1 TYR A 247 39.130 46.990 -6.750 1.00 67.45 C ANISOU 1167 CD1 TYR A 247 8762 10068 6799 699 -49 1305 C ATOM 1168 CD2 TYR A 247 37.032 47.372 -5.682 1.00 50.92 C ANISOU 1168 CD2 TYR A 247 6609 7537 5203 322 -298 1176 C ATOM 1169 CE1 TYR A 247 38.484 46.743 -7.946 1.00 55.71 C ANISOU 1169 CE1 TYR A 247 7406 8717 5044 846 -203 1264 C ATOM 1170 CE2 TYR A 247 36.380 47.127 -6.863 1.00 57.59 C ANISOU 1170 CE2 TYR A 247 7582 8495 5805 455 -457 1137 C ATOM 1171 CZ TYR A 247 37.109 46.813 -7.994 1.00 60.89 C ANISOU 1171 CZ TYR A 247 8098 9202 5834 722 -413 1177 C ATOM 1172 OH TYR A 247 36.449 46.570 -9.173 1.00 69.67 O ANISOU 1172 OH TYR A 247 9341 10444 6688 872 -583 1125 O ATOM 1173 N LYS A 248 39.572 50.729 -5.759 1.00 50.60 N ANISOU 1173 N LYS A 248 7394 6315 5516 1656 -63 -45 N ATOM 1174 CA LYS A 248 38.825 51.890 -6.252 1.00 51.23 C ANISOU 1174 CA LYS A 248 7492 6413 5561 1791 -6 -41 C ATOM 1175 C LYS A 248 38.868 53.062 -5.271 1.00 51.09 C ANISOU 1175 C LYS A 248 7485 6289 5638 1642 66 4 C ATOM 1176 O LYS A 248 37.838 53.611 -4.877 1.00 56.88 O ANISOU 1176 O LYS A 248 8221 7025 6365 1626 59 -85 O ATOM 1177 CB LYS A 248 37.379 51.510 -6.589 1.00 58.54 C ANISOU 1177 CB LYS A 248 8399 7449 6395 1879 -91 -215 C ATOM 1178 CG LYS A 248 37.263 50.504 -7.722 1.00 51.89 C ANISOU 1178 CG LYS A 248 7560 6714 5441 2050 -155 -267 C ATOM 1179 CD LYS A 248 35.900 50.566 -8.385 1.00 52.57 C ANISOU 1179 CD LYS A 248 7624 6933 5416 2199 -207 -400 C ATOM 1180 CE LYS A 248 35.878 49.818 -9.713 1.00 55.29 C ANISOU 1180 CE LYS A 248 7983 7389 5636 2408 -251 -431 C ATOM 1181 NZ LYS A 248 34.967 50.460 -10.711 1.00 54.33 N ANISOU 1181 NZ LYS A 248 7849 7399 5396 2646 -242 -463 N ATOM 1182 N GLY A 249 40.081 53.446 -4.878 1.00 51.02 N ANISOU 1182 N GLY A 249 7482 6192 5712 1533 135 142 N ATOM 1183 CA GLY A 249 40.261 54.602 -4.023 1.00 51.10 C ANISOU 1183 CA GLY A 249 7516 6090 5810 1388 212 193 C ATOM 1184 C GLY A 249 39.841 54.427 -2.580 1.00 57.18 C ANISOU 1184 C GLY A 249 8263 6817 6645 1147 151 83 C ATOM 1185 O GLY A 249 39.734 55.423 -1.861 1.00 50.48 O ANISOU 1185 O GLY A 249 7446 5880 5854 1040 207 93 O ATOM 1186 N SER A 250 39.597 53.196 -2.134 1.00 49.60 N ANISOU 1186 N SER A 250 7258 5911 5675 1061 44 -21 N ATOM 1187 CA SER A 250 39.207 52.912 -0.761 1.00 48.88 C ANISOU 1187 CA SER A 250 7144 5790 5640 837 -14 -123 C ATOM 1188 C SER A 250 40.106 51.823 -0.209 1.00 51.85 C ANISOU 1188 C SER A 250 7483 6166 6050 701 -66 -99 C ATOM 1189 O SER A 250 40.201 50.738 -0.790 1.00 60.07 O ANISOU 1189 O SER A 250 8515 7269 7038 784 -120 -120 O ATOM 1190 CB SER A 250 37.745 52.469 -0.660 1.00 48.71 C ANISOU 1190 CB SER A 250 7105 5841 5563 864 -94 -294 C ATOM 1191 OG SER A 250 36.888 53.584 -0.539 1.00 49.13 O ANISOU 1191 OG SER A 250 7183 5878 5607 909 -47 -327 O ATOM 1192 N TYR A 251 40.756 52.106 0.910 1.00 52.17 N ANISOU 1192 N TYR A 251 7509 6143 6172 498 -50 -58 N ATOM 1193 CA TYR A 251 41.539 51.094 1.594 1.00 51.17 C ANISOU 1193 CA TYR A 251 7344 6028 6072 364 -100 -40 C ATOM 1194 C TYR A 251 40.907 50.748 2.939 1.00 55.12 C ANISOU 1194 C TYR A 251 7828 6509 6605 169 -163 -159 C ATOM 1195 O TYR A 251 40.246 51.577 3.573 1.00 59.19 O ANISOU 1195 O TYR A 251 8356 6983 7149 90 -146 -216 O ATOM 1196 CB TYR A 251 43.000 51.531 1.770 1.00 50.04 C ANISOU 1196 CB TYR A 251 7175 5856 5981 291 -36 120 C ATOM 1197 CG TYR A 251 43.225 52.907 2.363 1.00 63.56 C ANISOU 1197 CG TYR A 251 8901 7488 7760 167 38 166 C ATOM 1198 CD1 TYR A 251 43.058 54.060 1.599 1.00 66.85 C ANISOU 1198 CD1 TYR A 251 9368 7859 8173 282 126 219 C ATOM 1199 CD2 TYR A 251 43.650 53.051 3.676 1.00 66.56 C ANISOU 1199 CD2 TYR A 251 9253 7835 8203 -62 24 159 C ATOM 1200 CE1 TYR A 251 43.278 55.310 2.138 1.00 66.90 C ANISOU 1200 CE1 TYR A 251 9408 7771 8239 163 200 258 C ATOM 1201 CE2 TYR A 251 43.874 54.297 4.222 1.00 66.72 C ANISOU 1201 CE2 TYR A 251 9297 7773 8279 -186 89 190 C ATOM 1202 CZ TYR A 251 43.688 55.421 3.449 1.00 63.32 C ANISOU 1202 CZ TYR A 251 8929 7281 7848 -77 180 238 C ATOM 1203 OH TYR A 251 43.911 56.664 3.992 1.00 61.04 O ANISOU 1203 OH TYR A 251 8685 6891 7616 -206 253 266 O ATOM 1204 N LEU A 252 41.099 49.495 3.347 1.00 58.65 N ANISOU 1204 N LEU A 252 8256 6986 7043 105 -230 -192 N ATOM 1205 CA LEU A 252 40.545 48.949 4.578 1.00 56.02 C ANISOU 1205 CA LEU A 252 7909 6644 6733 -69 -290 -297 C ATOM 1206 C LEU A 252 41.614 48.109 5.257 1.00 57.82 C ANISOU 1206 C LEU A 252 8113 6875 6982 -176 -311 -229 C ATOM 1207 O LEU A 252 42.268 47.294 4.602 1.00 58.91 O ANISOU 1207 O LEU A 252 8256 7043 7084 -75 -318 -167 O ATOM 1208 CB LEU A 252 39.303 48.093 4.290 1.00 53.87 C ANISOU 1208 CB LEU A 252 7649 6413 6406 -16 -358 -442 C ATOM 1209 CG LEU A 252 38.566 47.503 5.484 1.00 60.62 C ANISOU 1209 CG LEU A 252 8491 7264 7279 -188 -416 -557 C ATOM 1210 CD1 LEU A 252 38.054 48.628 6.360 1.00 55.89 C ANISOU 1210 CD1 LEU A 252 7879 6634 6722 -293 -388 -591 C ATOM 1211 CD2 LEU A 252 37.423 46.656 4.974 1.00 66.19 C ANISOU 1211 CD2 LEU A 252 9204 8020 7925 -127 -476 -690 C ATOM 1212 N ARG A 253 41.803 48.310 6.558 1.00 59.90 N ANISOU 1212 N ARG A 253 8351 7114 7295 -366 -319 -236 N ATOM 1213 CA ARG A 253 42.742 47.509 7.333 1.00 55.89 C ANISOU 1213 CA ARG A 253 7814 6624 6797 -469 -342 -177 C ATOM 1214 C ARG A 253 41.961 46.662 8.328 1.00 57.03 C ANISOU 1214 C ARG A 253 7969 6763 6938 -586 -403 -292 C ATOM 1215 O ARG A 253 41.313 47.192 9.240 1.00 66.47 O ANISOU 1215 O ARG A 253 9157 7936 8163 -713 -410 -366 O ATOM 1216 CB ARG A 253 43.779 48.388 8.026 1.00 51.26 C ANISOU 1216 CB ARG A 253 7183 6034 6261 -595 -299 -76 C ATOM 1217 CG ARG A 253 44.886 48.863 7.090 1.00 53.79 C ANISOU 1217 CG ARG A 253 7479 6376 6581 -494 -238 71 C ATOM 1218 CD ARG A 253 45.550 50.103 7.645 1.00 56.92 C ANISOU 1218 CD ARG A 253 7844 6749 7034 -632 -186 137 C ATOM 1219 NE ARG A 253 44.561 51.013 8.213 1.00 58.97 N ANISOU 1219 NE ARG A 253 8145 6936 7324 -720 -179 31 N ATOM 1220 CZ ARG A 253 44.863 52.090 8.930 1.00 64.57 C ANISOU 1220 CZ ARG A 253 8852 7600 8081 -870 -142 45 C ATOM 1221 NH1 ARG A 253 43.897 52.860 9.413 1.00 61.58 N ANISOU 1221 NH1 ARG A 253 8526 7151 7720 -926 -133 -56 N ATOM 1222 NH2 ARG A 253 46.131 52.397 9.168 1.00 73.66 N ANISOU 1222 NH2 ARG A 253 9948 8782 9259 -966 -114 157 N ATOM 1223 N ILE A 254 42.003 45.350 8.119 1.00 56.68 N ANISOU 1223 N ILE A 254 7949 6733 6853 -536 -441 -306 N ATOM 1224 CA ILE A 254 41.375 44.368 8.987 1.00 53.51 C ANISOU 1224 CA ILE A 254 7568 6320 6444 -641 -490 -399 C ATOM 1225 C ILE A 254 42.491 43.587 9.641 1.00 63.02 C ANISOU 1225 C ILE A 254 8764 7538 7643 -691 -492 -303 C ATOM 1226 O ILE A 254 43.473 43.221 8.986 1.00 73.18 O ANISOU 1226 O ILE A 254 10053 8850 8902 -579 -473 -196 O ATOM 1227 CB ILE A 254 40.447 43.421 8.205 1.00 58.84 C ANISOU 1227 CB ILE A 254 8297 6990 7071 -548 -528 -503 C ATOM 1228 CG1 ILE A 254 39.315 44.210 7.547 1.00 69.69 C ANISOU 1228 CG1 ILE A 254 9663 8379 8436 -485 -529 -597 C ATOM 1229 CG2 ILE A 254 39.938 42.305 9.102 1.00 53.10 C ANISOU 1229 CG2 ILE A 254 7599 6238 6337 -667 -568 -582 C ATOM 1230 CD1 ILE A 254 38.903 43.655 6.234 1.00 74.54 C ANISOU 1230 CD1 ILE A 254 10316 9016 8990 -323 -548 -642 C ATOM 1231 N CYS A 255 42.359 43.348 10.923 1.00 66.25 N ANISOU 1231 N CYS A 255 9160 7941 8070 -846 -513 -334 N ATOM 1232 CA CYS A 255 43.260 42.425 11.560 1.00 71.43 C ANISOU 1232 CA CYS A 255 9817 8618 8706 -876 -518 -254 C ATOM 1233 C CYS A 255 42.524 41.131 11.834 1.00 60.41 C ANISOU 1233 C CYS A 255 8492 7180 7280 -894 -550 -340 C ATOM 1234 O CYS A 255 41.417 41.135 12.382 1.00 61.67 O ANISOU 1234 O CYS A 255 8662 7314 7457 -995 -572 -457 O ATOM 1235 CB CYS A 255 43.849 43.015 12.828 1.00 89.16 C ANISOU 1235 CB CYS A 255 11997 10899 10980 -1030 -514 -206 C ATOM 1236 SG CYS A 255 45.228 42.053 13.267 1.00 91.06 S ANISOU 1236 SG CYS A 255 12219 11202 11179 -1007 -511 -69 S ATOM 1237 N LEU A 256 43.128 40.036 11.393 1.00 44.82 N ANISOU 1237 N LEU A 256 6572 5199 5260 -790 -546 -280 N ATOM 1238 CA LEU A 256 42.517 38.729 11.489 1.00 67.27 C ANISOU 1238 CA LEU A 256 9507 7982 8070 -794 -565 -355 C ATOM 1239 C LEU A 256 43.603 37.675 11.591 1.00 60.65 C ANISOU 1239 C LEU A 256 8718 7144 7183 -716 -546 -241 C ATOM 1240 O LEU A 256 44.765 37.902 11.242 1.00 53.44 O ANISOU 1240 O LEU A 256 7764 6289 6250 -618 -521 -110 O ATOM 1241 CB LEU A 256 41.612 38.432 10.286 1.00 67.18 C ANISOU 1241 CB LEU A 256 9557 7934 8036 -698 -583 -460 C ATOM 1242 CG LEU A 256 42.130 38.586 8.846 1.00 61.99 C ANISOU 1242 CG LEU A 256 8914 7297 7344 -505 -567 -405 C ATOM 1243 CD1 LEU A 256 42.990 37.416 8.368 1.00 61.06 C ANISOU 1243 CD1 LEU A 256 8880 7155 7165 -373 -551 -326 C ATOM 1244 CD2 LEU A 256 40.945 38.769 7.911 1.00 58.82 C ANISOU 1244 CD2 LEU A 256 8532 6887 6930 -457 -594 -538 C ATOM 1245 N LEU A 257 43.192 36.516 12.081 1.00 62.69 N ANISOU 1245 N LEU A 257 9065 7337 7416 -758 -553 -289 N ATOM 1246 CA LEU A 257 43.978 35.292 12.042 1.00 66.44 C ANISOU 1246 CA LEU A 257 9631 7783 7832 -658 -529 -204 C ATOM 1247 C LEU A 257 43.389 34.446 10.922 1.00 64.03 C ANISOU 1247 C LEU A 257 9447 7393 7489 -555 -534 -289 C ATOM 1248 O LEU A 257 42.298 33.886 11.068 1.00 67.23 O ANISOU 1248 O LEU A 257 9921 7721 7901 -645 -553 -418 O ATOM 1249 CB LEU A 257 43.932 34.570 13.384 1.00 66.36 C ANISOU 1249 CB LEU A 257 9655 7745 7815 -774 -522 -196 C ATOM 1250 CG LEU A 257 44.584 33.194 13.490 1.00 65.05 C ANISOU 1250 CG LEU A 257 9608 7528 7581 -675 -488 -117 C ATOM 1251 CD1 LEU A 257 45.325 33.097 14.804 1.00 68.48 C ANISOU 1251 CD1 LEU A 257 9994 8026 7999 -734 -472 -11 C ATOM 1252 CD2 LEU A 257 43.521 32.112 13.408 1.00 69.29 C ANISOU 1252 CD2 LEU A 257 10291 7929 8107 -722 -489 -241 C ATOM 1253 N HIS A 258 44.091 34.380 9.799 1.00 59.14 N ANISOU 1253 N HIS A 258 8849 6793 6827 -374 -518 -221 N ATOM 1254 CA HIS A 258 43.522 33.751 8.618 1.00 57.78 C ANISOU 1254 CA HIS A 258 8786 6554 6615 -269 -529 -312 C ATOM 1255 C HIS A 258 43.340 32.249 8.842 1.00 58.46 C ANISOU 1255 C HIS A 258 9033 6525 6654 -270 -518 -350 C ATOM 1256 O HIS A 258 44.160 31.615 9.518 1.00 55.27 O ANISOU 1256 O HIS A 258 8671 6109 6221 -245 -483 -242 O ATOM 1257 CB HIS A 258 44.417 34.005 7.401 1.00 66.07 C ANISOU 1257 CB HIS A 258 9826 7657 7621 -60 -507 -215 C ATOM 1258 CG HIS A 258 43.730 33.794 6.086 1.00 74.92 C ANISOU 1258 CG HIS A 258 11020 8742 8705 44 -529 -322 C ATOM 1259 ND1 HIS A 258 43.880 32.642 5.345 1.00 77.11 N ANISOU 1259 ND1 HIS A 258 11445 8947 8907 177 -519 -339 N ATOM 1260 CD2 HIS A 258 42.889 34.588 5.381 1.00 74.34 C ANISOU 1260 CD2 HIS A 258 10895 8701 8651 42 -559 -420 C ATOM 1261 CE1 HIS A 258 43.163 32.735 4.239 1.00 77.36 C ANISOU 1261 CE1 HIS A 258 11507 8973 8912 243 -549 -449 C ATOM 1262 NE2 HIS A 258 42.552 33.906 4.237 1.00 76.19 N ANISOU 1262 NE2 HIS A 258 11235 8894 8819 168 -574 -496 N ATOM 1263 N PRO A 259 42.271 31.653 8.302 1.00 59.60 N ANISOU 1263 N PRO A 259 9275 6585 6786 -302 -543 -502 N ATOM 1264 CA PRO A 259 42.113 30.193 8.417 1.00 60.83 C ANISOU 1264 CA PRO A 259 9609 6609 6894 -305 -524 -543 C ATOM 1265 C PRO A 259 43.256 29.419 7.790 1.00 65.59 C ANISOU 1265 C PRO A 259 10324 7180 7417 -91 -480 -426 C ATOM 1266 O PRO A 259 43.509 28.277 8.197 1.00 69.08 O ANISOU 1266 O PRO A 259 10910 7519 7817 -75 -443 -399 O ATOM 1267 CB PRO A 259 40.786 29.921 7.695 1.00 55.84 C ANISOU 1267 CB PRO A 259 9034 5922 6260 -371 -568 -735 C ATOM 1268 CG PRO A 259 40.036 31.207 7.781 1.00 52.47 C ANISOU 1268 CG PRO A 259 8441 5601 5896 -468 -609 -799 C ATOM 1269 CD PRO A 259 41.091 32.286 7.685 1.00 52.59 C ANISOU 1269 CD PRO A 259 8335 5722 5924 -358 -591 -650 C ATOM 1270 N VAL A 260 43.949 30.005 6.815 1.00 62.69 N ANISOU 1270 N VAL A 260 9901 6897 7023 81 -477 -352 N ATOM 1271 CA VAL A 260 45.132 29.416 6.201 1.00 61.02 C ANISOU 1271 CA VAL A 260 9769 6686 6730 304 -431 -221 C ATOM 1272 C VAL A 260 46.361 30.060 6.827 1.00 60.94 C ANISOU 1272 C VAL A 260 9621 6803 6730 348 -399 -33 C ATOM 1273 O VAL A 260 46.478 31.293 6.858 1.00 56.91 O ANISOU 1273 O VAL A 260 8945 6404 6274 302 -416 1 O ATOM 1274 CB VAL A 260 45.121 29.606 4.675 1.00 60.24 C ANISOU 1274 CB VAL A 260 9696 6609 6584 476 -443 -257 C ATOM 1275 CG1 VAL A 260 46.435 29.131 4.071 1.00 60.51 C ANISOU 1275 CG1 VAL A 260 9791 6668 6531 720 -390 -101 C ATOM 1276 CG2 VAL A 260 43.944 28.862 4.064 1.00 56.54 C ANISOU 1276 CG2 VAL A 260 9368 6023 6090 429 -479 -450 C ATOM 1277 N GLN A 261 47.272 29.232 7.334 1.00 61.29 N ANISOU 1277 N GLN A 261 9735 6833 6718 434 -352 90 N ATOM 1278 CA GLN A 261 48.440 29.702 8.063 1.00 67.68 C ANISOU 1278 CA GLN A 261 10410 7779 7526 461 -325 267 C ATOM 1279 C GLN A 261 49.710 29.129 7.448 1.00 74.99 C ANISOU 1279 C GLN A 261 11385 8753 8353 714 -271 424 C ATOM 1280 O GLN A 261 49.688 28.114 6.746 1.00 73.27 O ANISOU 1280 O GLN A 261 11346 8430 8063 858 -245 398 O ATOM 1281 CB GLN A 261 48.356 29.324 9.547 1.00 69.99 C ANISOU 1281 CB GLN A 261 10706 8050 7837 312 -318 283 C ATOM 1282 CG GLN A 261 47.261 30.048 10.317 1.00 50.40 C ANISOU 1282 CG GLN A 261 8141 5558 5450 65 -365 157 C ATOM 1283 CD GLN A 261 47.601 31.500 10.578 1.00 58.07 C ANISOU 1283 CD GLN A 261 8905 6678 6482 -9 -389 208 C ATOM 1284 OE1 GLN A 261 48.687 31.817 11.065 1.00 54.83 O ANISOU 1284 OE1 GLN A 261 8393 6388 6053 27 -370 352 O ATOM 1285 NE2 GLN A 261 46.675 32.395 10.250 1.00 48.77 N ANISOU 1285 NE2 GLN A 261 7665 5496 5371 -113 -428 89 N ATOM 1286 N LYS A 262 50.827 29.798 7.740 1.00 84.67 N ANISOU 1286 N LYS A 262 12450 10147 9575 762 -252 586 N ATOM 1287 CA LYS A 262 52.114 29.425 7.161 1.00 85.86 C ANISOU 1287 CA LYS A 262 12604 10388 9632 1005 -200 754 C ATOM 1288 C LYS A 262 52.519 28.009 7.560 1.00 84.70 C ANISOU 1288 C LYS A 262 12629 10163 9391 1128 -150 813 C ATOM 1289 O LYS A 262 52.683 27.131 6.706 1.00 87.54 O ANISOU 1289 O LYS A 262 13154 10440 9669 1322 -115 818 O ATOM 1290 CB LYS A 262 53.186 30.429 7.594 1.00 88.02 C ANISOU 1290 CB LYS A 262 12650 10872 9923 988 -192 912 C ATOM 1291 CG LYS A 262 53.094 31.796 6.932 1.00 85.61 C ANISOU 1291 CG LYS A 262 12194 10647 9688 934 -216 897 C ATOM 1292 CD LYS A 262 54.062 32.779 7.581 1.00 80.64 C ANISOU 1292 CD LYS A 262 11346 10207 9086 857 -211 1034 C ATOM 1293 CE LYS A 262 54.691 33.714 6.558 1.00 78.50 C ANISOU 1293 CE LYS A 262 10956 10049 8822 948 -188 1121 C ATOM 1294 NZ LYS A 262 53.681 34.548 5.847 1.00 72.72 N ANISOU 1294 NZ LYS A 262 10232 9234 8165 873 -216 987 N ATOM 1295 N THR A 263 52.691 27.771 8.857 1.00 78.50 N ANISOU 1295 N THR A 263 11815 9401 8610 1027 -144 861 N ATOM 1296 CA THR A 263 53.261 26.528 9.358 1.00 71.07 C ANISOU 1296 CA THR A 263 11017 8416 7572 1163 -86 956 C ATOM 1297 C THR A 263 52.171 25.511 9.690 1.00 62.08 C ANISOU 1297 C THR A 263 10101 7045 6440 1070 -80 812 C ATOM 1298 O THR A 263 50.981 25.829 9.762 1.00 62.42 O ANISOU 1298 O THR A 263 10154 6992 6569 870 -128 644 O ATOM 1299 CB THR A 263 54.132 26.798 10.590 1.00 78.10 C ANISOU 1299 CB THR A 263 11749 9479 8445 1123 -76 1103 C ATOM 1300 OG1 THR A 263 53.327 27.353 11.638 1.00 83.68 O ANISOU 1300 OG1 THR A 263 12379 10169 9246 857 -125 1005 O ATOM 1301 CG2 THR A 263 55.255 27.773 10.243 1.00 77.73 C ANISOU 1301 CG2 THR A 263 11476 9668 8388 1201 -79 1247 C ATOM 1302 N ALA A 264 52.602 24.264 9.896 1.00 61.57 N ANISOU 1302 N ALA A 264 10221 6894 6278 1223 -14 884 N ATOM 1303 CA ALA A 264 51.660 23.191 10.202 1.00 65.14 C ANISOU 1303 CA ALA A 264 10910 7111 6728 1143 8 762 C ATOM 1304 C ALA A 264 50.985 23.416 11.549 1.00 72.84 C ANISOU 1304 C ALA A 264 11821 8073 7780 892 -17 709 C ATOM 1305 O ALA A 264 49.770 23.237 11.684 1.00 79.43 O ANISOU 1305 O ALA A 264 12742 8758 8679 706 -42 543 O ATOM 1306 CB ALA A 264 52.374 21.838 10.185 1.00 61.61 C ANISOU 1306 CB ALA A 264 10683 6573 6154 1378 98 872 C ATOM 1307 N PHE A 265 51.763 23.795 12.565 1.00 71.79 N ANISOU 1307 N PHE A 265 11534 8109 7633 884 -11 848 N ATOM 1308 CA PHE A 265 51.186 24.014 13.887 1.00 68.83 C ANISOU 1308 CA PHE A 265 11098 7735 7319 661 -32 806 C ATOM 1309 C PHE A 265 50.193 25.167 13.870 1.00 65.15 C ANISOU 1309 C PHE A 265 10487 7290 6977 422 -112 656 C ATOM 1310 O PHE A 265 49.095 25.060 14.428 1.00 64.35 O ANISOU 1310 O PHE A 265 10436 7077 6937 226 -129 527 O ATOM 1311 CB PHE A 265 52.285 24.279 14.914 1.00 67.24 C ANISOU 1311 CB PHE A 265 10742 7739 7067 710 -19 984 C ATOM 1312 CG PHE A 265 51.766 24.796 16.223 1.00 69.20 C ANISOU 1312 CG PHE A 265 10880 8033 7379 476 -55 942 C ATOM 1313 CD1 PHE A 265 51.205 23.935 17.156 1.00 71.76 C ANISOU 1313 CD1 PHE A 265 11350 8226 7689 401 -17 914 C ATOM 1314 CD2 PHE A 265 51.825 26.148 16.517 1.00 66.78 C ANISOU 1314 CD2 PHE A 265 10335 7895 7145 331 -121 927 C ATOM 1315 CE1 PHE A 265 50.723 24.413 18.357 1.00 72.76 C ANISOU 1315 CE1 PHE A 265 11376 8402 7868 196 -47 876 C ATOM 1316 CE2 PHE A 265 51.342 26.633 17.719 1.00 63.93 C ANISOU 1316 CE2 PHE A 265 9881 7574 6834 124 -153 882 C ATOM 1317 CZ PHE A 265 50.791 25.762 18.640 1.00 69.38 C ANISOU 1317 CZ PHE A 265 10709 8146 7506 61 -118 858 C ATOM 1318 N MET A 266 50.573 26.289 13.250 1.00 62.92 N ANISOU 1318 N MET A 266 10024 7153 6729 438 -154 677 N ATOM 1319 CA MET A 266 49.680 27.442 13.194 1.00 57.68 C ANISOU 1319 CA MET A 266 9229 6512 6175 236 -221 544 C ATOM 1320 C MET A 266 48.417 27.126 12.403 1.00 61.62 C ANISOU 1320 C MET A 266 9863 6836 6712 173 -241 360 C ATOM 1321 O MET A 266 47.335 27.636 12.716 1.00 62.42 O ANISOU 1321 O MET A 266 9919 6903 6894 -26 -284 225 O ATOM 1322 CB MET A 266 50.406 28.648 12.597 1.00 55.90 C ANISOU 1322 CB MET A 266 8808 6461 5969 288 -247 616 C ATOM 1323 CG MET A 266 51.299 29.368 13.593 1.00 61.99 C ANISOU 1323 CG MET A 266 9389 7424 6742 234 -255 742 C ATOM 1324 SD MET A 266 50.448 29.749 15.138 1.00 61.70 S ANISOU 1324 SD MET A 266 9295 7375 6774 -39 -291 653 S ATOM 1325 CE MET A 266 49.074 30.732 14.552 1.00 54.72 C ANISOU 1325 CE MET A 266 8378 6410 6004 -208 -346 457 C ATOM 1326 N GLN A 267 48.536 26.295 11.366 1.00 64.72 N ANISOU 1326 N GLN A 267 10420 7129 7042 343 -211 351 N ATOM 1327 CA GLN A 267 47.351 25.826 10.659 1.00 61.52 C ANISOU 1327 CA GLN A 267 10160 6557 6658 278 -230 169 C ATOM 1328 C GLN A 267 46.462 25.009 11.584 1.00 59.29 C ANISOU 1328 C GLN A 267 10006 6126 6396 109 -214 80 C ATOM 1329 O GLN A 267 45.241 25.200 11.623 1.00 62.55 O ANISOU 1329 O GLN A 267 10416 6476 6876 -77 -255 -81 O ATOM 1330 CB GLN A 267 47.756 24.995 9.443 1.00 63.08 C ANISOU 1330 CB GLN A 267 10528 6671 6768 503 -195 183 C ATOM 1331 CG GLN A 267 46.600 24.689 8.519 1.00 62.47 C ANISOU 1331 CG GLN A 267 10572 6457 6706 443 -229 -13 C ATOM 1332 CD GLN A 267 45.823 25.937 8.165 1.00 66.24 C ANISOU 1332 CD GLN A 267 10873 7028 7269 312 -302 -120 C ATOM 1333 OE1 GLN A 267 46.318 26.805 7.450 1.00 70.33 O ANISOU 1333 OE1 GLN A 267 11266 7670 7787 417 -319 -65 O ATOM 1334 NE2 GLN A 267 44.604 26.042 8.681 1.00 63.46 N ANISOU 1334 NE2 GLN A 267 10508 6619 6985 86 -339 -267 N ATOM 1335 N PHE A 268 47.057 24.079 12.331 1.00 59.66 N ANISOU 1335 N PHE A 268 10166 6122 6380 179 -150 189 N ATOM 1336 CA PHE A 268 46.273 23.283 13.267 1.00 70.50 C ANISOU 1336 CA PHE A 268 11667 7350 7769 23 -122 123 C ATOM 1337 C PHE A 268 45.647 24.164 14.341 1.00 70.08 C ANISOU 1337 C PHE A 268 11439 7385 7803 -208 -166 78 C ATOM 1338 O PHE A 268 44.477 23.988 14.699 1.00 75.11 O ANISOU 1338 O PHE A 268 12119 7924 8495 -402 -179 -58 O ATOM 1339 CB PHE A 268 47.146 22.199 13.896 1.00 74.75 C ANISOU 1339 CB PHE A 268 12354 7833 8214 169 -36 273 C ATOM 1340 CG PHE A 268 46.484 21.485 15.029 1.00 78.02 C ANISOU 1340 CG PHE A 268 12879 8123 8643 13 4 240 C ATOM 1341 CD1 PHE A 268 45.507 20.534 14.791 1.00 79.01 C ANISOU 1341 CD1 PHE A 268 13221 8024 8777 -82 32 105 C ATOM 1342 CD2 PHE A 268 46.824 21.777 16.336 1.00 83.60 C ANISOU 1342 CD2 PHE A 268 13472 8941 9353 -48 14 341 C ATOM 1343 CE1 PHE A 268 44.890 19.878 15.841 1.00 84.34 C ANISOU 1343 CE1 PHE A 268 13998 8580 9467 -234 78 81 C ATOM 1344 CE2 PHE A 268 46.215 21.125 17.389 1.00 81.04 C ANISOU 1344 CE2 PHE A 268 13250 8505 9037 -184 57 319 C ATOM 1345 CZ PHE A 268 45.245 20.175 17.142 1.00 82.77 C ANISOU 1345 CZ PHE A 268 13686 8493 9269 -278 93 193 C ATOM 1346 N TYR A 269 46.414 25.123 14.865 1.00 64.20 N ANISOU 1346 N TYR A 269 10494 6830 7069 -193 -187 190 N ATOM 1347 CA TYR A 269 45.871 26.040 15.861 1.00 62.70 C ANISOU 1347 CA TYR A 269 10140 6728 6954 -400 -230 145 C ATOM 1348 C TYR A 269 44.670 26.808 15.313 1.00 66.22 C ANISOU 1348 C TYR A 269 10518 7157 7487 -551 -291 -30 C ATOM 1349 O TYR A 269 43.608 26.850 15.946 1.00 67.97 O ANISOU 1349 O TYR A 269 10736 7329 7761 -742 -306 -140 O ATOM 1350 CB TYR A 269 46.956 27.003 16.343 1.00 62.78 C ANISOU 1350 CB TYR A 269 9950 6948 6956 -355 -248 284 C ATOM 1351 CG TYR A 269 46.416 28.106 17.222 1.00 66.90 C ANISOU 1351 CG TYR A 269 10302 7561 7555 -561 -297 225 C ATOM 1352 CD1 TYR A 269 46.049 27.856 18.539 1.00 70.91 C ANISOU 1352 CD1 TYR A 269 10818 8058 8068 -694 -284 222 C ATOM 1353 CD2 TYR A 269 46.260 29.393 16.732 1.00 67.05 C ANISOU 1353 CD2 TYR A 269 10167 7673 7637 -615 -350 175 C ATOM 1354 CE1 TYR A 269 45.546 28.865 19.344 1.00 71.19 C ANISOU 1354 CE1 TYR A 269 10708 8176 8165 -873 -327 164 C ATOM 1355 CE2 TYR A 269 45.760 30.404 17.523 1.00 66.87 C ANISOU 1355 CE2 TYR A 269 10008 7721 7677 -793 -389 118 C ATOM 1356 CZ TYR A 269 45.404 30.136 18.830 1.00 70.57 C ANISOU 1356 CZ TYR A 269 10486 8182 8147 -921 -379 110 C ATOM 1357 OH TYR A 269 44.906 31.140 19.627 1.00 77.53 O ANISOU 1357 OH TYR A 269 11241 9134 9084 -1089 -416 51 O ATOM 1358 N ALA A 270 44.817 27.421 14.132 1.00 64.56 N ANISOU 1358 N ALA A 270 10251 6995 7284 -459 -324 -54 N ATOM 1359 CA ALA A 270 43.737 28.242 13.585 1.00 62.00 C ANISOU 1359 CA ALA A 270 9848 6679 7030 -576 -381 -207 C ATOM 1360 C ALA A 270 42.473 27.425 13.384 1.00 60.91 C ANISOU 1360 C ALA A 270 9850 6389 6905 -688 -384 -369 C ATOM 1361 O ALA A 270 41.362 27.905 13.639 1.00 62.92 O ANISOU 1361 O ALA A 270 10036 6650 7219 -860 -421 -495 O ATOM 1362 CB ALA A 270 44.171 28.886 12.270 1.00 63.44 C ANISOU 1362 CB ALA A 270 9973 6929 7202 -427 -403 -191 C ATOM 1363 N THR A 271 42.626 26.171 12.960 1.00 61.51 N ANISOU 1363 N THR A 271 10125 6327 6919 -595 -341 -367 N ATOM 1364 CA THR A 271 41.478 25.292 12.767 1.00 65.82 C ANISOU 1364 CA THR A 271 10820 6717 7472 -714 -339 -523 C ATOM 1365 C THR A 271 40.911 24.813 14.099 1.00 71.13 C ANISOU 1365 C THR A 271 11530 7324 8172 -898 -307 -538 C ATOM 1366 O THR A 271 39.692 24.772 14.288 1.00 72.85 O ANISOU 1366 O THR A 271 11743 7498 8438 -1088 -330 -680 O ATOM 1367 CB THR A 271 41.874 24.094 11.895 1.00 61.01 C ANISOU 1367 CB THR A 271 10434 5964 6782 -556 -296 -516 C ATOM 1368 OG1 THR A 271 42.249 24.550 10.590 1.00 61.69 O ANISOU 1368 OG1 THR A 271 10485 6113 6840 -392 -329 -521 O ATOM 1369 CG2 THR A 271 40.730 23.089 11.766 1.00 56.96 C ANISOU 1369 CG2 THR A 271 10096 5274 6274 -701 -287 -679 C ATOM 1370 N ALA A 272 41.770 24.425 15.034 1.00 70.27 N ANISOU 1370 N ALA A 272 11454 7218 8028 -841 -253 -389 N ATOM 1371 CA ALA A 272 41.254 23.881 16.283 1.00 64.25 C ANISOU 1371 CA ALA A 272 10746 6385 7281 -999 -213 -394 C ATOM 1372 C ALA A 272 40.889 24.957 17.298 1.00 57.07 C ANISOU 1372 C ALA A 272 9633 5616 6434 -1152 -251 -400 C ATOM 1373 O ALA A 272 40.402 24.613 18.377 1.00 61.35 O ANISOU 1373 O ALA A 272 10200 6119 6990 -1289 -220 -406 O ATOM 1374 CB ALA A 272 42.267 22.912 16.910 1.00 62.75 C ANISOU 1374 CB ALA A 272 10697 6134 7013 -864 -131 -232 C ATOM 1375 N LYS A 273 41.058 26.238 16.959 1.00 57.11 N ANISOU 1375 N LYS A 273 9451 5774 6474 -1134 -311 -403 N ATOM 1376 CA LYS A 273 41.038 27.294 17.970 1.00 53.81 C ANISOU 1376 CA LYS A 273 8852 5494 6098 -1239 -338 -376 C ATOM 1377 C LYS A 273 39.700 27.351 18.700 1.00 57.52 C ANISOU 1377 C LYS A 273 9299 5933 6622 -1459 -347 -501 C ATOM 1378 O LYS A 273 39.657 27.372 19.935 1.00 67.55 O ANISOU 1378 O LYS A 273 10537 7234 7896 -1551 -326 -458 O ATOM 1379 CB LYS A 273 41.357 28.642 17.327 1.00 49.72 C ANISOU 1379 CB LYS A 273 8165 5116 5612 -1186 -394 -374 C ATOM 1380 CG LYS A 273 41.432 29.787 18.325 1.00 48.85 C ANISOU 1380 CG LYS A 273 7882 5140 5539 -1288 -420 -346 C ATOM 1381 CD LYS A 273 41.381 31.131 17.619 1.00 47.93 C ANISOU 1381 CD LYS A 273 7624 5122 5467 -1274 -470 -385 C ATOM 1382 CE LYS A 273 41.485 32.266 18.630 1.00 47.23 C ANISOU 1382 CE LYS A 273 7385 5150 5411 -1378 -491 -362 C ATOM 1383 NZ LYS A 273 41.510 33.621 18.009 1.00 56.93 N ANISOU 1383 NZ LYS A 273 8490 6461 6681 -1364 -527 -387 N ATOM 1384 N ASP A 274 38.596 27.356 17.951 1.00 60.40 N ANISOU 1384 N ASP A 274 9677 6250 7022 -1541 -378 -655 N ATOM 1385 CA ASP A 274 37.277 27.514 18.560 1.00 60.29 C ANISOU 1385 CA ASP A 274 9613 6236 7057 -1748 -390 -777 C ATOM 1386 C ASP A 274 36.976 26.394 19.552 1.00 55.20 C ANISOU 1386 C ASP A 274 9098 5479 6398 -1853 -325 -759 C ATOM 1387 O ASP A 274 36.512 26.649 20.669 1.00 60.23 O ANISOU 1387 O ASP A 274 9667 6160 7058 -1985 -314 -761 O ATOM 1388 CB ASP A 274 36.209 27.574 17.469 1.00 67.52 C ANISOU 1388 CB ASP A 274 10526 7132 7997 -1800 -433 -941 C ATOM 1389 CG ASP A 274 36.308 28.827 16.633 1.00 74.71 C ANISOU 1389 CG ASP A 274 11293 8168 8926 -1714 -493 -964 C ATOM 1390 OD1 ASP A 274 36.394 29.924 17.226 1.00 76.89 O ANISOU 1390 OD1 ASP A 274 11424 8559 9232 -1743 -512 -932 O ATOM 1391 OD2 ASP A 274 36.318 28.715 15.390 1.00 79.90 O ANISOU 1391 OD2 ASP A 274 11991 8805 9564 -1615 -517 -1013 O ATOM 1392 N TRP A 275 37.216 25.141 19.159 1.00 57.01 N ANISOU 1392 N TRP A 275 9524 5553 6585 -1794 -275 -741 N ATOM 1393 CA TRP A 275 37.035 24.044 20.104 1.00 62.25 C ANISOU 1393 CA TRP A 275 10332 6092 7228 -1878 -198 -704 C ATOM 1394 C TRP A 275 38.059 24.115 21.226 1.00 69.13 C ANISOU 1394 C TRP A 275 11179 7027 8061 -1798 -159 -533 C ATOM 1395 O TRP A 275 37.752 23.788 22.380 1.00 67.13 O ANISOU 1395 O TRP A 275 10947 6754 7807 -1904 -114 -502 O ATOM 1396 CB TRP A 275 37.124 22.698 19.389 1.00 64.97 C ANISOU 1396 CB TRP A 275 10915 6240 7529 -1819 -146 -721 C ATOM 1397 CG TRP A 275 35.873 22.329 18.674 1.00 74.38 C ANISOU 1397 CG TRP A 275 12159 7347 8755 -1971 -167 -905 C ATOM 1398 CD1 TRP A 275 35.690 22.264 17.326 1.00 78.44 C ANISOU 1398 CD1 TRP A 275 12713 7831 9260 -1915 -211 -1006 C ATOM 1399 CD2 TRP A 275 34.616 21.984 19.268 1.00 81.08 C ANISOU 1399 CD2 TRP A 275 13014 8147 9646 -2210 -149 -1012 C ATOM 1400 NE1 TRP A 275 34.399 21.892 17.041 1.00 82.81 N ANISOU 1400 NE1 TRP A 275 13294 8326 9845 -2108 -226 -1175 N ATOM 1401 CE2 TRP A 275 33.718 21.715 18.217 1.00 81.69 C ANISOU 1401 CE2 TRP A 275 13128 8172 9737 -2296 -187 -1181 C ATOM 1402 CE3 TRP A 275 34.163 21.872 20.587 1.00 84.56 C ANISOU 1402 CE3 TRP A 275 13428 8592 10109 -2359 -102 -981 C ATOM 1403 CZ2 TRP A 275 32.394 21.343 18.443 1.00 81.48 C ANISOU 1403 CZ2 TRP A 275 13103 8106 9749 -2536 -181 -1318 C ATOM 1404 CZ3 TRP A 275 32.848 21.501 20.809 1.00 84.10 C ANISOU 1404 CZ3 TRP A 275 13377 8486 10091 -2590 -90 -1111 C ATOM 1405 CH2 TRP A 275 31.979 21.242 19.742 1.00 82.67 C ANISOU 1405 CH2 TRP A 275 13223 8261 9926 -2681 -130 -1278 C ATOM 1406 N TRP A 276 39.281 24.538 20.903 1.00 68.37 N ANISOU 1406 N TRP A 276 11032 7018 7926 -1610 -176 -417 N ATOM 1407 CA TRP A 276 40.306 24.705 21.926 1.00 63.16 C ANISOU 1407 CA TRP A 276 10320 6456 7221 -1531 -151 -257 C ATOM 1408 C TRP A 276 39.878 25.734 22.967 1.00 63.86 C ANISOU 1408 C TRP A 276 10228 6683 7352 -1676 -188 -280 C ATOM 1409 O TRP A 276 40.013 25.505 24.175 1.00 70.73 O ANISOU 1409 O TRP A 276 11102 7577 8194 -1718 -150 -208 O ATOM 1410 CB TRP A 276 41.631 25.104 21.275 1.00 58.15 C ANISOU 1410 CB TRP A 276 9632 5920 6543 -1321 -172 -143 C ATOM 1411 CG TRP A 276 42.585 25.778 22.210 1.00 59.66 C ANISOU 1411 CG TRP A 276 9681 6283 6703 -1276 -183 -12 C ATOM 1412 CD1 TRP A 276 42.917 27.102 22.227 1.00 52.28 C ANISOU 1412 CD1 TRP A 276 8547 5517 5800 -1292 -247 -7 C ATOM 1413 CD2 TRP A 276 43.329 25.164 23.269 1.00 53.16 C ANISOU 1413 CD2 TRP A 276 8906 5485 5806 -1211 -127 130 C ATOM 1414 NE1 TRP A 276 43.824 27.349 23.225 1.00 53.36 N ANISOU 1414 NE1 TRP A 276 8599 5786 5888 -1255 -240 121 N ATOM 1415 CE2 TRP A 276 44.093 26.177 23.881 1.00 55.56 C ANISOU 1415 CE2 TRP A 276 9020 5991 6098 -1198 -170 209 C ATOM 1416 CE3 TRP A 276 43.425 23.858 23.758 1.00 54.48 C ANISOU 1416 CE3 TRP A 276 9265 5524 5912 -1159 -42 200 C ATOM 1417 CZ2 TRP A 276 44.940 25.927 24.957 1.00 55.21 C ANISOU 1417 CZ2 TRP A 276 8957 6045 5977 -1134 -140 350 C ATOM 1418 CZ3 TRP A 276 44.268 23.611 24.825 1.00 55.04 C ANISOU 1418 CZ3 TRP A 276 9323 5684 5905 -1080 -4 351 C ATOM 1419 CH2 TRP A 276 45.014 24.640 25.413 1.00 58.08 C ANISOU 1419 CH2 TRP A 276 9501 6291 6274 -1066 -57 422 C ATOM 1420 N LEU A 277 39.351 26.876 22.515 1.00 58.12 N ANISOU 1420 N LEU A 277 9350 6048 6686 -1744 -258 -381 N ATOM 1421 CA LEU A 277 38.879 27.899 23.444 1.00 61.18 C ANISOU 1421 CA LEU A 277 9579 6556 7111 -1876 -290 -415 C ATOM 1422 C LEU A 277 37.781 27.359 24.349 1.00 64.01 C ANISOU 1422 C LEU A 277 9987 6848 7486 -2048 -251 -480 C ATOM 1423 O LEU A 277 37.757 27.642 25.553 1.00 65.88 O ANISOU 1423 O LEU A 277 10162 7156 7712 -2119 -239 -440 O ATOM 1424 CB LEU A 277 38.375 29.113 22.673 1.00 49.38 C ANISOU 1424 CB LEU A 277 7947 5141 5674 -1908 -359 -521 C ATOM 1425 CG LEU A 277 39.447 30.042 22.119 1.00 48.66 C ANISOU 1425 CG LEU A 277 7756 5158 5576 -1775 -398 -447 C ATOM 1426 CD1 LEU A 277 38.807 31.265 21.490 1.00 60.24 C ANISOU 1426 CD1 LEU A 277 9099 6689 7099 -1819 -453 -554 C ATOM 1427 CD2 LEU A 277 40.393 30.444 23.237 1.00 48.54 C ANISOU 1427 CD2 LEU A 277 7663 5254 5526 -1761 -393 -326 C ATOM 1428 N PHE A 278 36.868 26.572 23.785 1.00 68.26 N ANISOU 1428 N PHE A 278 10635 7255 8045 -2122 -230 -581 N ATOM 1429 CA PHE A 278 35.773 26.012 24.569 1.00 65.46 C ANISOU 1429 CA PHE A 278 10326 6836 7710 -2301 -187 -645 C ATOM 1430 C PHE A 278 36.282 24.997 25.586 1.00 73.10 C ANISOU 1430 C PHE A 278 11427 7724 8623 -2280 -103 -520 C ATOM 1431 O PHE A 278 35.837 24.980 26.740 1.00 77.86 O ANISOU 1431 O PHE A 278 12003 8356 9226 -2391 -71 -506 O ATOM 1432 CB PHE A 278 34.752 25.377 23.625 1.00 57.77 C ANISOU 1432 CB PHE A 278 9438 5744 6767 -2390 -187 -784 C ATOM 1433 CG PHE A 278 33.658 24.625 24.318 1.00 58.46 C ANISOU 1433 CG PHE A 278 9591 5748 6872 -2582 -132 -847 C ATOM 1434 CD1 PHE A 278 32.724 25.292 25.090 1.00 57.91 C ANISOU 1434 CD1 PHE A 278 9381 5784 6838 -2734 -146 -909 C ATOM 1435 CD2 PHE A 278 33.545 23.251 24.171 1.00 61.73 C ANISOU 1435 CD2 PHE A 278 10214 5974 7265 -2612 -61 -844 C ATOM 1436 CE1 PHE A 278 31.705 24.604 25.719 1.00 56.82 C ANISOU 1436 CE1 PHE A 278 9292 5581 6716 -2915 -91 -961 C ATOM 1437 CE2 PHE A 278 32.529 22.556 24.793 1.00 58.53 C ANISOU 1437 CE2 PHE A 278 9871 5488 6881 -2804 -3 -900 C ATOM 1438 CZ PHE A 278 31.606 23.233 25.569 1.00 56.28 C ANISOU 1438 CZ PHE A 278 9427 5324 6632 -2958 -19 -956 C ATOM 1439 N SER A 279 37.232 24.154 25.181 1.00 72.80 N ANISOU 1439 N SER A 279 11536 7593 8530 -2123 -63 -421 N ATOM 1440 CA SER A 279 37.662 23.043 26.025 1.00 63.56 C ANISOU 1440 CA SER A 279 10527 6324 7299 -2084 30 -302 C ATOM 1441 C SER A 279 38.522 23.526 27.190 1.00 63.21 C ANISOU 1441 C SER A 279 10383 6430 7204 -2015 33 -164 C ATOM 1442 O SER A 279 38.205 23.279 28.361 1.00 64.61 O ANISOU 1442 O SER A 279 10572 6612 7364 -2100 80 -128 O ATOM 1443 CB SER A 279 38.428 22.021 25.183 1.00 58.21 C ANISOU 1443 CB SER A 279 10045 5505 6568 -1914 76 -238 C ATOM 1444 OG SER A 279 37.718 21.680 24.006 1.00 67.87 O ANISOU 1444 OG SER A 279 11350 6607 7830 -1967 60 -375 O ATOM 1445 N PHE A 280 39.630 24.207 26.886 1.00 59.84 N ANISOU 1445 N PHE A 280 9855 6133 6747 -1863 -16 -86 N ATOM 1446 CA PHE A 280 40.585 24.588 27.921 1.00 56.89 C ANISOU 1446 CA PHE A 280 9391 5913 6311 -1787 -17 49 C ATOM 1447 C PHE A 280 40.105 25.763 28.764 1.00 53.81 C ANISOU 1447 C PHE A 280 8813 5673 5958 -1928 -72 -8 C ATOM 1448 O PHE A 280 40.411 25.820 29.959 1.00 53.62 O ANISOU 1448 O PHE A 280 8751 5739 5884 -1937 -53 70 O ATOM 1449 CB PHE A 280 41.941 24.936 27.299 1.00 53.78 C ANISOU 1449 CB PHE A 280 8940 5623 5871 -1591 -52 151 C ATOM 1450 CG PHE A 280 42.996 25.305 28.310 1.00 58.77 C ANISOU 1450 CG PHE A 280 9466 6434 6429 -1513 -59 289 C ATOM 1451 CD1 PHE A 280 43.168 26.623 28.710 1.00 54.37 C ANISOU 1451 CD1 PHE A 280 8704 6059 5896 -1581 -134 265 C ATOM 1452 CD2 PHE A 280 43.810 24.332 28.865 1.00 60.33 C ANISOU 1452 CD2 PHE A 280 9775 6621 6527 -1369 12 441 C ATOM 1453 CE1 PHE A 280 44.129 26.963 29.642 1.00 53.41 C ANISOU 1453 CE1 PHE A 280 8482 6113 5700 -1525 -147 380 C ATOM 1454 CE2 PHE A 280 44.774 24.666 29.796 1.00 62.30 C ANISOU 1454 CE2 PHE A 280 9915 7060 6697 -1295 0 565 C ATOM 1455 CZ PHE A 280 44.930 25.983 30.188 1.00 57.58 C ANISOU 1455 CZ PHE A 280 9103 6650 6124 -1382 -84 530 C ATOM 1456 N TYR A 281 39.386 26.714 28.174 1.00 52.11 N ANISOU 1456 N TYR A 281 8485 5494 5820 -2025 -138 -141 N ATOM 1457 CA TYR A 281 39.034 27.945 28.866 1.00 53.23 C ANISOU 1457 CA TYR A 281 8454 5780 5991 -2132 -191 -194 C ATOM 1458 C TYR A 281 37.616 27.942 29.410 1.00 53.97 C ANISOU 1458 C TYR A 281 8543 5835 6130 -2316 -173 -307 C ATOM 1459 O TYR A 281 37.174 28.959 29.958 1.00 53.05 O ANISOU 1459 O TYR A 281 8294 5827 6037 -2406 -212 -365 O ATOM 1460 CB TYR A 281 39.230 29.143 27.938 1.00 55.91 C ANISOU 1460 CB TYR A 281 8664 6203 6378 -2104 -269 -253 C ATOM 1461 CG TYR A 281 40.679 29.388 27.574 1.00 57.13 C ANISOU 1461 CG TYR A 281 8779 6442 6487 -1942 -290 -134 C ATOM 1462 CD1 TYR A 281 41.278 28.708 26.520 1.00 57.90 C ANISOU 1462 CD1 TYR A 281 8971 6464 6565 -1797 -273 -84 C ATOM 1463 CD2 TYR A 281 41.450 30.297 28.287 1.00 56.54 C ANISOU 1463 CD2 TYR A 281 8570 6530 6384 -1936 -328 -74 C ATOM 1464 CE1 TYR A 281 42.600 28.927 26.188 1.00 54.81 C ANISOU 1464 CE1 TYR A 281 8532 6166 6127 -1645 -288 32 C ATOM 1465 CE2 TYR A 281 42.772 30.524 27.962 1.00 54.07 C ANISOU 1465 CE2 TYR A 281 8204 6313 6028 -1802 -347 36 C ATOM 1466 CZ TYR A 281 43.343 29.836 26.911 1.00 55.66 C ANISOU 1466 CZ TYR A 281 8491 6446 6210 -1653 -326 93 C ATOM 1467 OH TYR A 281 44.662 30.053 26.578 1.00 57.17 O ANISOU 1467 OH TYR A 281 8619 6749 6354 -1514 -340 210 O ATOM 1468 N PHE A 282 36.889 26.837 29.268 1.00 52.70 N ANISOU 1468 N PHE A 282 8522 5521 5979 -2376 -112 -341 N ATOM 1469 CA PHE A 282 35.570 26.735 29.876 1.00 56.18 C ANISOU 1469 CA PHE A 282 8954 5936 6455 -2557 -85 -433 C ATOM 1470 C PHE A 282 35.362 25.350 30.474 1.00 59.91 C ANISOU 1470 C PHE A 282 9601 6269 6894 -2594 15 -373 C ATOM 1471 O PHE A 282 35.130 25.225 31.678 1.00 60.40 O ANISOU 1471 O PHE A 282 9656 6366 6927 -2659 59 -328 O ATOM 1472 CB PHE A 282 34.473 27.054 28.858 1.00 56.90 C ANISOU 1472 CB PHE A 282 9003 5998 6619 -2652 -125 -592 C ATOM 1473 CG PHE A 282 33.128 27.310 29.485 1.00 56.75 C ANISOU 1473 CG PHE A 282 8911 6016 6636 -2834 -114 -692 C ATOM 1474 CD1 PHE A 282 32.935 28.419 30.292 1.00 51.59 C ANISOU 1474 CD1 PHE A 282 8109 5511 5983 -2873 -147 -706 C ATOM 1475 CD2 PHE A 282 32.062 26.447 29.272 1.00 53.32 C ANISOU 1475 CD2 PHE A 282 8557 5473 6230 -2966 -70 -773 C ATOM 1476 CE1 PHE A 282 31.712 28.665 30.876 1.00 52.48 C ANISOU 1476 CE1 PHE A 282 8152 5670 6119 -3023 -133 -791 C ATOM 1477 CE2 PHE A 282 30.831 26.691 29.854 1.00 53.55 C ANISOU 1477 CE2 PHE A 282 8503 5558 6287 -3132 -58 -857 C ATOM 1478 CZ PHE A 282 30.658 27.803 30.655 1.00 58.00 C ANISOU 1478 CZ PHE A 282 8915 6276 6846 -3151 -88 -863 C ATOM 1479 N CYS A 283 35.459 24.306 29.649 1.00 60.37 N ANISOU 1479 N CYS A 283 9825 6162 6949 -2548 56 -369 N ATOM 1480 CA CYS A 283 35.225 22.954 30.144 1.00 59.86 C ANISOU 1480 CA CYS A 283 9953 5935 6855 -2589 162 -316 C ATOM 1481 C CYS A 283 36.278 22.531 31.165 1.00 66.03 C ANISOU 1481 C CYS A 283 10797 6743 7547 -2457 219 -138 C ATOM 1482 O CYS A 283 35.950 21.880 32.164 1.00 70.99 O ANISOU 1482 O CYS A 283 11507 7320 8147 -2521 301 -84 O ATOM 1483 CB CYS A 283 35.193 21.969 28.981 1.00 58.09 C ANISOU 1483 CB CYS A 283 9909 5521 6640 -2555 191 -355 C ATOM 1484 SG CYS A 283 33.701 22.057 27.985 1.00 70.16 S ANISOU 1484 SG CYS A 283 11406 6994 8259 -2752 151 -569 S ATOM 1485 N LEU A 284 37.550 22.861 30.923 1.00 62.87 N ANISOU 1485 N LEU A 284 10360 6432 7096 -2269 182 -40 N ATOM 1486 CA LEU A 284 38.592 22.471 31.873 1.00 62.83 C ANISOU 1486 CA LEU A 284 10397 6482 6992 -2129 231 132 C ATOM 1487 C LEU A 284 38.401 23.102 33.246 1.00 66.98 C ANISOU 1487 C LEU A 284 10794 7161 7495 -2209 223 157 C ATOM 1488 O LEU A 284 38.397 22.362 34.246 1.00 71.27 O ANISOU 1488 O LEU A 284 11434 7668 7979 -2205 307 249 O ATOM 1489 CB LEU A 284 39.981 22.792 31.305 1.00 61.61 C ANISOU 1489 CB LEU A 284 10197 6426 6787 -1920 184 227 C ATOM 1490 CG LEU A 284 41.143 22.411 32.229 1.00 61.55 C ANISOU 1490 CG LEU A 284 10213 6510 6663 -1756 228 411 C ATOM 1491 CD1 LEU A 284 41.416 20.918 32.143 1.00 67.98 C ANISOU 1491 CD1 LEU A 284 11279 7136 7415 -1639 342 511 C ATOM 1492 CD2 LEU A 284 42.399 23.213 31.922 1.00 57.39 C ANISOU 1492 CD2 LEU A 284 9538 6174 6095 -1606 152 483 C ATOM 1493 N PRO A 285 38.242 24.425 33.384 1.00 64.22 N ANISOU 1493 N PRO A 285 10241 6978 7180 -2275 132 83 N ATOM 1494 CA PRO A 285 38.052 24.985 34.733 1.00 63.45 C ANISOU 1494 CA PRO A 285 10038 7021 7051 -2347 128 102 C ATOM 1495 C PRO A 285 36.756 24.542 35.389 1.00 63.82 C ANISOU 1495 C PRO A 285 10138 6985 7127 -2517 194 42 C ATOM 1496 O PRO A 285 36.755 24.205 36.579 1.00 68.76 O ANISOU 1496 O PRO A 285 10791 7645 7691 -2527 252 122 O ATOM 1497 CB PRO A 285 38.086 26.500 34.485 1.00 62.88 C ANISOU 1497 CB PRO A 285 9763 7107 7020 -2384 19 13 C ATOM 1498 CG PRO A 285 37.690 26.661 33.068 1.00 60.26 C ANISOU 1498 CG PRO A 285 9437 6688 6772 -2401 -19 -92 C ATOM 1499 CD PRO A 285 38.245 25.477 32.353 1.00 57.51 C ANISOU 1499 CD PRO A 285 9261 6195 6396 -2279 35 -17 C ATOM 1500 N LEU A 286 35.648 24.521 34.642 1.00 62.75 N ANISOU 1500 N LEU A 286 10011 6752 7080 -2651 189 -94 N ATOM 1501 CA LEU A 286 34.378 24.103 35.225 1.00 58.59 C ANISOU 1501 CA LEU A 286 9518 6161 6583 -2827 253 -154 C ATOM 1502 C LEU A 286 34.448 22.667 35.727 1.00 65.06 C ANISOU 1502 C LEU A 286 10543 6821 7354 -2813 376 -47 C ATOM 1503 O LEU A 286 33.949 22.358 36.816 1.00 73.56 O ANISOU 1503 O LEU A 286 11641 7904 8403 -2894 445 -9 O ATOM 1504 CB LEU A 286 33.243 24.259 34.212 1.00 59.67 C ANISOU 1504 CB LEU A 286 9624 6233 6814 -2965 222 -317 C ATOM 1505 CG LEU A 286 32.842 25.675 33.793 1.00 60.95 C ANISOU 1505 CG LEU A 286 9588 6543 7028 -3004 118 -437 C ATOM 1506 CD1 LEU A 286 31.396 25.698 33.315 1.00 59.86 C ANISOU 1506 CD1 LEU A 286 9410 6373 6962 -3176 116 -586 C ATOM 1507 CD2 LEU A 286 33.066 26.677 34.913 1.00 58.60 C ANISOU 1507 CD2 LEU A 286 9153 6423 6691 -2996 87 -404 C ATOM 1508 N ALA A 287 35.074 21.776 34.956 1.00 63.64 N ANISOU 1508 N ALA A 287 10528 6495 7157 -2701 411 8 N ATOM 1509 CA ALA A 287 35.171 20.382 35.380 1.00 70.61 C ANISOU 1509 CA ALA A 287 11635 7203 7990 -2674 539 114 C ATOM 1510 C ALA A 287 36.052 20.245 36.616 1.00 70.05 C ANISOU 1510 C ALA A 287 11575 7229 7810 -2539 584 283 C ATOM 1511 O ALA A 287 35.680 19.574 37.585 1.00 72.18 O ANISOU 1511 O ALA A 287 11939 7442 8043 -2590 683 351 O ATOM 1512 CB ALA A 287 35.707 19.518 34.240 1.00 61.29 C ANISOU 1512 CB ALA A 287 10637 5845 6806 -2562 565 132 C ATOM 1513 N ILE A 288 37.224 20.886 36.603 1.00 67.12 N ANISOU 1513 N ILE A 288 11103 7018 7383 -2369 512 356 N ATOM 1514 CA ILE A 288 38.158 20.739 37.714 1.00 65.50 C ANISOU 1514 CA ILE A 288 10899 6929 7059 -2224 546 519 C ATOM 1515 C ILE A 288 37.605 21.390 38.977 1.00 67.54 C ANISOU 1515 C ILE A 288 11025 7335 7301 -2337 537 502 C ATOM 1516 O ILE A 288 37.658 20.805 40.066 1.00 74.42 O ANISOU 1516 O ILE A 288 11972 8211 8094 -2308 622 611 O ATOM 1517 CB ILE A 288 39.538 21.302 37.329 1.00 64.07 C ANISOU 1517 CB ILE A 288 10620 6902 6822 -2030 465 590 C ATOM 1518 CG1 ILE A 288 40.310 20.269 36.507 1.00 64.44 C ANISOU 1518 CG1 ILE A 288 10853 6803 6829 -1853 522 682 C ATOM 1519 CG2 ILE A 288 40.326 21.705 38.564 1.00 63.27 C ANISOU 1519 CG2 ILE A 288 10413 7017 6610 -1938 450 706 C ATOM 1520 CD1 ILE A 288 41.757 20.628 36.277 1.00 71.40 C ANISOU 1520 CD1 ILE A 288 11650 7849 7630 -1639 465 789 C ATOM 1521 N THR A 289 37.055 22.600 38.855 1.00 65.67 N ANISOU 1521 N THR A 289 10600 7221 7132 -2458 440 368 N ATOM 1522 CA THR A 289 36.513 23.266 40.035 1.00 64.05 C ANISOU 1522 CA THR A 289 10273 7157 6905 -2558 430 344 C ATOM 1523 C THR A 289 35.315 22.510 40.596 1.00 69.53 C ANISOU 1523 C THR A 289 11067 7727 7624 -2707 537 327 C ATOM 1524 O THR A 289 35.141 22.442 41.818 1.00 78.00 O ANISOU 1524 O THR A 289 12131 8874 8633 -2725 587 390 O ATOM 1525 CB THR A 289 36.133 24.711 39.714 1.00 60.67 C ANISOU 1525 CB THR A 289 9643 6864 6543 -2648 313 201 C ATOM 1526 OG1 THR A 289 35.225 24.737 38.608 1.00 61.16 O ANISOU 1526 OG1 THR A 289 9714 6808 6716 -2760 297 67 O ATOM 1527 CG2 THR A 289 37.372 25.527 39.366 1.00 56.76 C ANISOU 1527 CG2 THR A 289 9040 6512 6015 -2513 215 232 C ATOM 1528 N ALA A 290 34.477 21.935 39.730 1.00 66.92 N ANISOU 1528 N ALA A 290 10830 7215 7382 -2820 574 241 N ATOM 1529 CA ALA A 290 33.358 21.136 40.223 1.00 67.09 C ANISOU 1529 CA ALA A 290 10952 7112 7428 -2978 683 229 C ATOM 1530 C ALA A 290 33.853 19.861 40.891 1.00 74.91 C ANISOU 1530 C ALA A 290 12151 7978 8332 -2882 815 396 C ATOM 1531 O ALA A 290 33.358 19.470 41.955 1.00 84.24 O ANISOU 1531 O ALA A 290 13373 9157 9477 -2947 905 455 O ATOM 1532 CB ALA A 290 32.396 20.798 39.084 1.00 62.04 C ANISOU 1532 CB ALA A 290 10360 6315 6896 -3129 686 92 C ATOM 1533 N PHE A 291 34.832 19.196 40.272 1.00 71.85 N ANISOU 1533 N PHE A 291 11904 7489 7908 -2716 834 481 N ATOM 1534 CA PHE A 291 35.356 17.950 40.821 1.00 73.16 C ANISOU 1534 CA PHE A 291 12290 7524 7985 -2597 967 648 C ATOM 1535 C PHE A 291 35.929 18.161 42.218 1.00 73.79 C ANISOU 1535 C PHE A 291 12310 7781 7945 -2487 988 785 C ATOM 1536 O PHE A 291 35.616 17.409 43.150 1.00 77.64 O ANISOU 1536 O PHE A 291 12916 8202 8380 -2505 1109 879 O ATOM 1537 CB PHE A 291 36.414 17.370 39.881 1.00 73.75 C ANISOU 1537 CB PHE A 291 12502 7494 8027 -2404 969 716 C ATOM 1538 CG PHE A 291 37.117 16.163 40.432 1.00 71.97 C ANISOU 1538 CG PHE A 291 12502 7152 7690 -2233 1103 903 C ATOM 1539 CD1 PHE A 291 36.481 14.934 40.467 1.00 69.68 C ANISOU 1539 CD1 PHE A 291 12457 6602 7417 -2315 1248 929 C ATOM 1540 CD2 PHE A 291 38.415 16.256 40.906 1.00 71.73 C ANISOU 1540 CD2 PHE A 291 12442 7276 7535 -1990 1088 1055 C ATOM 1541 CE1 PHE A 291 37.124 13.823 40.969 1.00 71.50 C ANISOU 1541 CE1 PHE A 291 12915 6712 7541 -2144 1382 1108 C ATOM 1542 CE2 PHE A 291 39.062 15.150 41.408 1.00 75.41 C ANISOU 1542 CE2 PHE A 291 13117 7647 7888 -1811 1215 1236 C ATOM 1543 CZ PHE A 291 38.416 13.931 41.441 1.00 80.12 C ANISOU 1543 CZ PHE A 291 13973 7967 8502 -1881 1366 1265 C ATOM 1544 N PHE A 292 36.768 19.188 42.384 1.00 70.16 N ANISOU 1544 N PHE A 292 11666 7554 7437 -2376 873 795 N ATOM 1545 CA PHE A 292 37.350 19.478 43.690 1.00 68.33 C ANISOU 1545 CA PHE A 292 11359 7521 7084 -2274 875 909 C ATOM 1546 C PHE A 292 36.387 20.180 44.634 1.00 75.24 C ANISOU 1546 C PHE A 292 12099 8512 7975 -2439 862 834 C ATOM 1547 O PHE A 292 36.596 20.129 45.850 1.00 79.40 O ANISOU 1547 O PHE A 292 12615 9157 8398 -2381 903 933 O ATOM 1548 CB PHE A 292 38.622 20.305 43.526 1.00 64.29 C ANISOU 1548 CB PHE A 292 10698 7221 6510 -2110 755 942 C ATOM 1549 CG PHE A 292 39.793 19.501 43.045 1.00 72.67 C ANISOU 1549 CG PHE A 292 11890 8225 7496 -1887 792 1079 C ATOM 1550 CD1 PHE A 292 40.438 18.624 43.902 1.00 69.68 C ANISOU 1550 CD1 PHE A 292 11638 7857 6982 -1717 892 1262 C ATOM 1551 CD2 PHE A 292 40.243 19.610 41.738 1.00 72.44 C ANISOU 1551 CD2 PHE A 292 11862 8137 7523 -1833 733 1032 C ATOM 1552 CE1 PHE A 292 41.505 17.874 43.470 1.00 74.34 C ANISOU 1552 CE1 PHE A 292 12351 8402 7493 -1493 933 1395 C ATOM 1553 CE2 PHE A 292 41.313 18.861 41.297 1.00 71.61 C ANISOU 1553 CE2 PHE A 292 11880 7987 7343 -1614 772 1162 C ATOM 1554 CZ PHE A 292 41.947 17.991 42.164 1.00 74.03 C ANISOU 1554 CZ PHE A 292 12310 8306 7511 -1441 873 1345 C ATOM 1555 N TYR A 293 35.344 20.831 44.116 1.00 77.64 N ANISOU 1555 N TYR A 293 12303 8798 8397 -2629 809 665 N ATOM 1556 CA TYR A 293 34.285 21.303 45.000 1.00 77.70 C ANISOU 1556 CA TYR A 293 12215 8888 8419 -2786 825 602 C ATOM 1557 C TYR A 293 33.585 20.129 45.666 1.00 80.11 C ANISOU 1557 C TYR A 293 12691 9042 8707 -2856 984 684 C ATOM 1558 O TYR A 293 33.447 20.089 46.893 1.00 77.73 O ANISOU 1558 O TYR A 293 12377 8832 8323 -2848 1041 761 O ATOM 1559 CB TYR A 293 33.269 22.153 44.233 1.00 75.65 C ANISOU 1559 CB TYR A 293 11822 8635 8285 -2963 746 412 C ATOM 1560 CG TYR A 293 32.037 22.500 45.040 1.00 75.90 C ANISOU 1560 CG TYR A 293 11771 8730 8336 -3129 780 346 C ATOM 1561 CD1 TYR A 293 32.062 23.529 45.973 1.00 72.34 C ANISOU 1561 CD1 TYR A 293 11166 8493 7827 -3117 723 329 C ATOM 1562 CD2 TYR A 293 30.848 21.798 44.869 1.00 76.28 C ANISOU 1562 CD2 TYR A 293 11895 8631 8456 -3301 871 300 C ATOM 1563 CE1 TYR A 293 30.940 23.847 46.716 1.00 71.01 C ANISOU 1563 CE1 TYR A 293 10924 8389 7667 -3252 759 273 C ATOM 1564 CE2 TYR A 293 29.719 22.110 45.608 1.00 75.64 C ANISOU 1564 CE2 TYR A 293 11726 8626 8388 -3448 907 247 C ATOM 1565 CZ TYR A 293 29.774 23.135 46.528 1.00 74.55 C ANISOU 1565 CZ TYR A 293 11438 8702 8187 -3414 852 237 C ATOM 1566 OH TYR A 293 28.653 23.446 47.260 1.00 76.36 O ANISOU 1566 OH TYR A 293 11581 9011 8420 -3545 892 189 O ATOM 1567 N THR A 294 33.132 19.162 44.863 1.00 84.43 N ANISOU 1567 N THR A 294 13403 9351 9326 -2931 1061 666 N ATOM 1568 CA THR A 294 32.391 18.030 45.409 1.00 87.27 C ANISOU 1568 CA THR A 294 13936 9540 9682 -3029 1221 733 C ATOM 1569 C THR A 294 33.249 17.221 46.377 1.00 86.47 C ANISOU 1569 C THR A 294 13984 9427 9444 -2843 1326 938 C ATOM 1570 O THR A 294 32.771 16.806 47.440 1.00 92.34 O ANISOU 1570 O THR A 294 14779 10169 10138 -2888 1434 1017 O ATOM 1571 CB THR A 294 31.871 17.144 44.275 1.00 85.28 C ANISOU 1571 CB THR A 294 13846 9027 9529 -3141 1276 667 C ATOM 1572 OG1 THR A 294 32.969 16.688 43.475 1.00 93.21 O ANISOU 1572 OG1 THR A 294 14976 9934 10504 -2958 1261 728 O ATOM 1573 CG2 THR A 294 30.902 17.919 43.391 1.00 75.36 C ANISOU 1573 CG2 THR A 294 12432 7803 8397 -3330 1177 465 C ATOM 1574 N LEU A 295 34.517 16.984 46.029 1.00 83.26 N ANISOU 1574 N LEU A 295 13645 9022 8967 -2623 1302 1034 N ATOM 1575 CA LEU A 295 35.408 16.291 46.956 1.00 71.22 C ANISOU 1575 CA LEU A 295 12244 7523 7295 -2416 1393 1236 C ATOM 1576 C LEU A 295 35.586 17.082 48.243 1.00 81.28 C ANISOU 1576 C LEU A 295 13347 9066 8468 -2370 1351 1280 C ATOM 1577 O LEU A 295 35.656 16.505 49.335 1.00 84.98 O ANISOU 1577 O LEU A 295 13905 9551 8833 -2298 1460 1419 O ATOM 1578 CB LEU A 295 36.773 16.042 46.314 1.00 71.15 C ANISOU 1578 CB LEU A 295 12298 7514 7221 -2177 1357 1324 C ATOM 1579 CG LEU A 295 36.947 14.846 45.382 1.00 77.44 C ANISOU 1579 CG LEU A 295 13353 8026 8045 -2121 1453 1367 C ATOM 1580 CD1 LEU A 295 38.412 14.445 45.349 1.00 78.56 C ANISOU 1580 CD1 LEU A 295 13573 8220 8056 -1820 1462 1531 C ATOM 1581 CD2 LEU A 295 36.077 13.688 45.819 1.00 80.52 C ANISOU 1581 CD2 LEU A 295 13971 8174 8450 -2235 1632 1420 C ATOM 1582 N MET A 296 35.678 18.406 48.131 1.00 75.75 N ANISOU 1582 N MET A 296 12410 8577 7794 -2406 1196 1161 N ATOM 1583 CA MET A 296 35.892 19.239 49.307 1.00 75.38 C ANISOU 1583 CA MET A 296 12201 8791 7648 -2365 1142 1184 C ATOM 1584 C MET A 296 34.698 19.180 50.253 1.00 76.29 C ANISOU 1584 C MET A 296 12312 8904 7771 -2522 1227 1166 C ATOM 1585 O MET A 296 34.862 18.966 51.460 1.00 83.08 O ANISOU 1585 O MET A 296 13191 9865 8509 -2442 1291 1282 O ATOM 1586 CB MET A 296 36.163 20.678 48.877 1.00 66.97 C ANISOU 1586 CB MET A 296 10905 7916 6623 -2393 965 1044 C ATOM 1587 CG MET A 296 36.575 21.592 50.011 1.00 66.75 C ANISOU 1587 CG MET A 296 10716 8163 6483 -2337 893 1059 C ATOM 1588 SD MET A 296 36.120 23.305 49.684 1.00 69.01 S ANISOU 1588 SD MET A 296 10759 8605 6857 -2485 729 846 S ATOM 1589 CE MET A 296 34.329 23.175 49.695 1.00 65.83 C ANISOU 1589 CE MET A 296 10379 8063 6570 -2719 809 736 C ATOM 1590 N THR A 297 33.485 19.365 49.720 1.00 72.44 N ANISOU 1590 N THR A 297 11791 8315 7419 -2740 1229 1023 N ATOM 1591 CA THR A 297 32.302 19.388 50.577 1.00 74.81 C ANISOU 1591 CA THR A 297 12061 8635 7729 -2897 1305 998 C ATOM 1592 C THR A 297 32.105 18.056 51.287 1.00 77.39 C ANISOU 1592 C THR A 297 12600 8809 7996 -2878 1491 1159 C ATOM 1593 O THR A 297 31.717 18.025 52.461 1.00 79.26 O ANISOU 1593 O THR A 297 12821 9137 8158 -2890 1563 1225 O ATOM 1594 CB THR A 297 31.053 19.742 49.769 1.00 71.88 C ANISOU 1594 CB THR A 297 11614 8186 7510 -3129 1278 822 C ATOM 1595 OG1 THR A 297 30.756 18.686 48.847 1.00 88.64 O ANISOU 1595 OG1 THR A 297 13912 10048 9718 -3204 1358 821 O ATOM 1596 CG2 THR A 297 31.253 21.048 49.010 1.00 66.99 C ANISOU 1596 CG2 THR A 297 10803 7702 6949 -3134 1104 670 C ATOM 1597 N CYS A 298 32.348 16.944 50.587 1.00 77.40 N ANISOU 1597 N CYS A 298 12810 8570 8028 -2847 1577 1223 N ATOM 1598 CA CYS A 298 32.308 15.635 51.232 1.00 86.70 C ANISOU 1598 CA CYS A 298 14221 9581 9140 -2802 1764 1392 C ATOM 1599 C CYS A 298 33.309 15.565 52.377 1.00 91.61 C ANISOU 1599 C CYS A 298 14857 10368 9582 -2562 1790 1568 C ATOM 1600 O CYS A 298 32.990 15.090 53.473 1.00 91.34 O ANISOU 1600 O CYS A 298 14894 10344 9468 -2552 1913 1682 O ATOM 1601 CB CYS A 298 32.597 14.535 50.211 1.00 88.41 C ANISOU 1601 CB CYS A 298 14671 9514 9406 -2774 1838 1428 C ATOM 1602 SG CYS A 298 31.345 14.351 48.930 1.00 95.45 S ANISOU 1602 SG CYS A 298 15587 10186 10493 -3068 1836 1234 S ATOM 1603 N GLU A 299 34.530 16.042 52.137 1.00 92.95 N ANISOU 1603 N GLU A 299 14951 10683 9681 -2366 1674 1593 N ATOM 1604 CA GLU A 299 35.549 15.999 53.177 1.00 95.84 C ANISOU 1604 CA GLU A 299 15313 11237 9865 -2130 1685 1755 C ATOM 1605 C GLU A 299 35.249 17.003 54.284 1.00 96.70 C ANISOU 1605 C GLU A 299 15220 11614 9909 -2171 1619 1713 C ATOM 1606 O GLU A 299 35.458 16.707 55.465 1.00101.91 O ANISOU 1606 O GLU A 299 15916 12377 10428 -2058 1696 1849 O ATOM 1607 CB GLU A 299 36.927 16.247 52.568 1.00 98.82 C ANISOU 1607 CB GLU A 299 15647 11713 10187 -1924 1576 1788 C ATOM 1608 CG GLU A 299 38.072 15.970 53.529 1.00109.96 C ANISOU 1608 CG GLU A 299 17080 13302 11397 -1656 1602 1977 C ATOM 1609 CD GLU A 299 38.024 14.572 54.116 1.00120.66 C ANISOU 1609 CD GLU A 299 18698 14478 12668 -1550 1807 2169 C ATOM 1610 OE1 GLU A 299 37.791 13.611 53.354 1.00122.94 O ANISOU 1610 OE1 GLU A 299 19202 14478 13032 -1578 1912 2194 O ATOM 1611 OE2 GLU A 299 38.211 14.439 55.345 1.00121.53 O ANISOU 1611 OE2 GLU A 299 18810 14734 12633 -1439 1866 2295 O ATOM 1612 N MET A 300 34.749 18.191 53.931 1.00 93.05 N ANISOU 1612 N MET A 300 14553 11263 9539 -2321 1483 1528 N ATOM 1613 CA MET A 300 34.328 19.134 54.963 1.00 91.42 C ANISOU 1613 CA MET A 300 14175 11285 9275 -2374 1432 1474 C ATOM 1614 C MET A 300 33.177 18.564 55.779 1.00 92.84 C ANISOU 1614 C MET A 300 14435 11384 9457 -2496 1584 1518 C ATOM 1615 O MET A 300 33.059 18.836 56.980 1.00 95.44 O ANISOU 1615 O MET A 300 14706 11882 9673 -2456 1608 1570 O ATOM 1616 CB MET A 300 33.921 20.472 54.341 1.00 94.70 C ANISOU 1616 CB MET A 300 14383 11800 9798 -2515 1274 1265 C ATOM 1617 CG MET A 300 35.042 21.224 53.642 1.00101.84 C ANISOU 1617 CG MET A 300 15180 12818 10697 -2410 1116 1214 C ATOM 1618 SD MET A 300 34.751 23.002 53.555 1.00104.22 S ANISOU 1618 SD MET A 300 15226 13325 11048 -2524 938 1007 S ATOM 1619 CE MET A 300 33.009 23.052 53.140 1.00102.78 C ANISOU 1619 CE MET A 300 15037 12990 11024 -2773 995 869 C ATOM 1620 N LEU A 301 32.316 17.769 55.141 1.00 90.90 N ANISOU 1620 N LEU A 301 14321 10883 9333 -2650 1690 1498 N ATOM 1621 CA LEU A 301 31.179 17.188 55.844 1.00 86.70 C ANISOU 1621 CA LEU A 301 13864 10264 8815 -2790 1843 1540 C ATOM 1622 C LEU A 301 31.641 16.208 56.915 1.00 90.33 C ANISOU 1622 C LEU A 301 14496 10703 9124 -2626 1996 1761 C ATOM 1623 O LEU A 301 31.165 16.246 58.055 1.00 92.84 O ANISOU 1623 O LEU A 301 14786 11127 9361 -2638 2069 1821 O ATOM 1624 CB LEU A 301 30.248 16.502 54.846 1.00 83.95 C ANISOU 1624 CB LEU A 301 13623 9645 8628 -2999 1918 1467 C ATOM 1625 CG LEU A 301 28.952 15.920 55.402 1.00 86.03 C ANISOU 1625 CG LEU A 301 13946 9808 8932 -3194 2074 1488 C ATOM 1626 CD1 LEU A 301 28.077 17.023 55.975 1.00 87.70 C ANISOU 1626 CD1 LEU A 301 13928 10240 9153 -3313 2009 1374 C ATOM 1627 CD2 LEU A 301 28.221 15.164 54.309 1.00 80.15 C ANISOU 1627 CD2 LEU A 301 13323 8790 8339 -3393 2139 1416 C ATOM 1628 N ARG A 302 32.575 15.320 56.566 1.00 91.03 N ANISOU 1628 N ARG A 302 14766 10658 9164 -2457 2050 1889 N ATOM 1629 CA ARG A 302 33.102 14.378 57.548 1.00 94.08 C ANISOU 1629 CA ARG A 302 15326 11027 9393 -2267 2198 2111 C ATOM 1630 C ARG A 302 33.831 15.102 58.673 1.00 95.25 C ANISOU 1630 C ARG A 302 15326 11500 9365 -2082 2120 2173 C ATOM 1631 O ARG A 302 33.701 14.732 59.846 1.00100.57 O ANISOU 1631 O ARG A 302 16055 12241 9916 -2009 2231 2305 O ATOM 1632 CB ARG A 302 34.026 13.372 56.865 1.00 95.60 C ANISOU 1632 CB ARG A 302 15735 11026 9562 -2098 2259 2229 C ATOM 1633 CG ARG A 302 33.322 12.458 55.871 1.00103.35 C ANISOU 1633 CG ARG A 302 16914 11659 10695 -2270 2366 2188 C ATOM 1634 CD ARG A 302 34.302 11.474 55.251 1.00114.56 C ANISOU 1634 CD ARG A 302 18564 12892 12072 -2073 2431 2311 C ATOM 1635 NE ARG A 302 33.690 10.682 54.188 1.00125.45 N ANISOU 1635 NE ARG A 302 20129 13938 13597 -2242 2511 2246 N ATOM 1636 CZ ARG A 302 33.188 9.462 54.354 1.00131.63 C ANISOU 1636 CZ ARG A 302 21179 14443 14392 -2304 2714 2347 C ATOM 1637 NH1 ARG A 302 32.651 8.819 53.326 1.00133.88 N ANISOU 1637 NH1 ARG A 302 21623 14436 14811 -2474 2768 2264 N ATOM 1638 NH2 ARG A 302 33.223 8.883 55.545 1.00131.78 N ANISOU 1638 NH2 ARG A 302 21312 14473 14284 -2199 2864 2530 N ATOM 1639 N LYS A 303 34.602 16.142 58.340 1.00 91.00 N ANISOU 1639 N LYS A 303 14600 11168 8808 -2010 1930 2076 N ATOM 1640 CA LYS A 303 35.295 16.901 59.379 1.00 93.98 C ANISOU 1640 CA LYS A 303 14825 11866 9018 -1858 1840 2111 C ATOM 1641 C LYS A 303 34.303 17.551 60.335 1.00 94.96 C ANISOU 1641 C LYS A 303 14829 12124 9127 -1992 1847 2043 C ATOM 1642 O LYS A 303 34.561 17.648 61.541 1.00 96.23 O ANISOU 1642 O LYS A 303 14960 12480 9124 -1869 1871 2136 O ATOM 1643 CB LYS A 303 36.198 17.968 58.757 1.00100.01 C ANISOU 1643 CB LYS A 303 15403 12810 9788 -1804 1633 1995 C ATOM 1644 CG LYS A 303 37.302 17.445 57.849 1.00109.81 C ANISOU 1644 CG LYS A 303 16730 13968 11023 -1646 1611 2066 C ATOM 1645 CD LYS A 303 38.460 16.841 58.627 1.00117.13 C ANISOU 1645 CD LYS A 303 17731 15030 11743 -1361 1661 2274 C ATOM 1646 CE LYS A 303 39.546 16.341 57.683 1.00117.07 C ANISOU 1646 CE LYS A 303 17804 14951 11728 -1193 1640 2345 C ATOM 1647 NZ LYS A 303 40.696 15.748 58.419 1.00118.82 N ANISOU 1647 NZ LYS A 303 18087 15323 11736 -896 1690 2554 N ATOM 1648 N ASN A1002 33.160 18.001 59.815 1.00 92.57 N ANISOU 1648 N ASN A1002 14455 11733 8985 -2234 1827 1881 N ATOM 1649 CA ASN A1002 32.167 18.653 60.663 1.00 87.61 C ANISOU 1649 CA ASN A1002 13706 11235 8345 -2358 1835 1810 C ATOM 1650 C ASN A1002 31.466 17.647 61.566 1.00 86.93 C ANISOU 1650 C ASN A1002 13772 11052 8206 -2376 2042 1961 C ATOM 1651 O ASN A1002 31.283 17.896 62.764 1.00 81.66 O ANISOU 1651 O ASN A1002 13053 10562 7412 -2323 2076 2015 O ATOM 1652 CB ASN A1002 31.156 19.404 59.799 1.00 86.78 C ANISOU 1652 CB ASN A1002 13478 11075 8421 -2595 1758 1602 C ATOM 1653 CG ASN A1002 31.763 20.616 59.127 1.00 90.42 C ANISOU 1653 CG ASN A1002 13766 11673 8915 -2578 1553 1448 C ATOM 1654 OD1 ASN A1002 32.793 21.124 59.567 1.00 90.73 O ANISOU 1654 OD1 ASN A1002 13735 11907 8831 -2418 1458 1476 O ATOM 1655 ND2 ASN A1002 31.129 21.088 58.060 1.00 95.59 N ANISOU 1655 ND2 ASN A1002 14350 12235 9734 -2745 1487 1286 N ATOM 1656 N ILE A1003 31.056 16.506 61.005 1.00 84.59 N ANISOU 1656 N ILE A1003 13668 10469 8002 -2456 2186 2029 N ATOM 1657 CA ILE A1003 30.430 15.462 61.814 1.00 84.12 C ANISOU 1657 CA ILE A1003 13777 10287 7897 -2480 2400 2186 C ATOM 1658 C ILE A1003 31.390 14.993 62.898 1.00 95.51 C ANISOU 1658 C ILE A1003 15313 11850 9128 -2207 2467 2392 C ATOM 1659 O ILE A1003 31.006 14.807 64.060 1.00 87.08 O ANISOU 1659 O ILE A1003 14265 10871 7952 -2174 2575 2495 O ATOM 1660 CB ILE A1003 29.976 14.289 60.928 1.00 88.36 C ANISOU 1660 CB ILE A1003 14528 10475 8568 -2609 2537 2220 C ATOM 1661 CG1 ILE A1003 28.979 14.766 59.876 1.00 89.89 C ANISOU 1661 CG1 ILE A1003 14613 10578 8962 -2881 2466 2010 C ATOM 1662 CG2 ILE A1003 29.366 13.185 61.779 1.00 87.61 C ANISOU 1662 CG2 ILE A1003 14623 10239 8426 -2639 2771 2392 C ATOM 1663 CD1 ILE A1003 28.454 13.658 58.995 1.00 90.31 C ANISOU 1663 CD1 ILE A1003 14867 10299 9149 -3038 2592 2019 C ATOM 1664 N PHE A1004 32.655 14.793 62.529 1.00 91.86 N ANISOU 1664 N PHE A1004 14904 11403 8595 -2000 2407 2460 N ATOM 1665 CA PHE A1004 33.665 14.404 63.505 1.00 90.22 C ANISOU 1665 CA PHE A1004 14764 11345 8171 -1717 2453 2653 C ATOM 1666 C PHE A1004 33.776 15.441 64.618 1.00 92.45 C ANISOU 1666 C PHE A1004 14841 11973 8312 -1653 2351 2616 C ATOM 1667 O PHE A1004 33.787 15.097 65.805 1.00100.65 O ANISOU 1667 O PHE A1004 15931 13119 9193 -1531 2454 2760 O ATOM 1668 CB PHE A1004 35.008 14.207 62.801 1.00 92.42 C ANISOU 1668 CB PHE A1004 15085 11625 8405 -1515 2373 2701 C ATOM 1669 CG PHE A1004 36.117 13.775 63.713 1.00104.35 C ANISOU 1669 CG PHE A1004 16658 13305 9686 -1207 2415 2904 C ATOM 1670 CD1 PHE A1004 36.908 14.712 64.356 1.00109.80 C ANISOU 1670 CD1 PHE A1004 17145 14346 10228 -1068 2261 2879 C ATOM 1671 CD2 PHE A1004 36.379 12.431 63.917 1.00112.15 C ANISOU 1671 CD2 PHE A1004 17911 14102 10600 -1052 2610 3120 C ATOM 1672 CE1 PHE A1004 37.932 14.320 65.195 1.00113.52 C ANISOU 1672 CE1 PHE A1004 17657 15000 10474 -780 2293 3064 C ATOM 1673 CE2 PHE A1004 37.406 12.030 64.754 1.00115.68 C ANISOU 1673 CE2 PHE A1004 18412 14721 10822 -746 2652 3314 C ATOM 1674 CZ PHE A1004 38.183 12.975 65.395 1.00115.18 C ANISOU 1674 CZ PHE A1004 18126 15032 10607 -609 2489 3286 C ATOM 1675 N GLU A1005 33.852 16.722 64.249 1.00 89.34 N ANISOU 1675 N GLU A1005 14222 11752 7970 -1734 2151 2421 N ATOM 1676 CA GLU A1005 33.936 17.778 65.254 1.00 91.96 C ANISOU 1676 CA GLU A1005 14367 12401 8174 -1690 2045 2361 C ATOM 1677 C GLU A1005 32.684 17.814 66.120 1.00 91.45 C ANISOU 1677 C GLU A1005 14293 12347 8107 -1820 2156 2358 C ATOM 1678 O GLU A1005 32.766 18.021 67.337 1.00 88.33 O ANISOU 1678 O GLU A1005 13857 12163 7543 -1709 2176 2426 O ATOM 1679 CB GLU A1005 34.159 19.130 64.576 1.00 99.09 C ANISOU 1679 CB GLU A1005 15056 13439 9156 -1779 1824 2142 C ATOM 1680 CG GLU A1005 34.328 20.299 65.536 1.00106.83 C ANISOU 1680 CG GLU A1005 15849 14737 10004 -1739 1700 2059 C ATOM 1681 CD GLU A1005 35.630 20.242 66.317 1.00113.94 C ANISOU 1681 CD GLU A1005 16733 15875 10683 -1485 1653 2182 C ATOM 1682 OE1 GLU A1005 36.554 19.519 65.888 1.00116.97 O ANISOU 1682 OE1 GLU A1005 17211 16199 11032 -1336 1673 2302 O ATOM 1683 OE2 GLU A1005 35.728 20.921 67.362 1.00113.88 O ANISOU 1683 OE2 GLU A1005 16617 16125 10528 -1430 1595 2157 O ATOM 1684 N MET A1006 31.515 17.608 65.509 1.00 88.65 N ANISOU 1684 N MET A1006 13971 11778 7933 -2053 2229 2280 N ATOM 1685 CA MET A1006 30.266 17.584 66.265 1.00 86.71 C ANISOU 1685 CA MET A1006 13712 11538 7696 -2189 2346 2283 C ATOM 1686 C MET A1006 30.273 16.472 67.309 1.00 89.46 C ANISOU 1686 C MET A1006 14240 11845 7906 -2061 2551 2518 C ATOM 1687 O MET A1006 29.955 16.700 68.481 1.00 89.14 O ANISOU 1687 O MET A1006 14152 11982 7735 -2010 2599 2570 O ATOM 1688 CB MET A1006 29.086 17.419 65.309 1.00 85.04 C ANISOU 1688 CB MET A1006 13510 11097 7704 -2461 2394 2170 C ATOM 1689 CG MET A1006 27.752 17.232 66.007 1.00 86.24 C ANISOU 1689 CG MET A1006 13657 11237 7875 -2616 2538 2191 C ATOM 1690 SD MET A1006 26.458 16.607 64.919 1.00 92.09 S ANISOU 1690 SD MET A1006 14459 11677 8854 -2926 2641 2115 S ATOM 1691 CE MET A1006 27.209 15.083 64.351 1.00 97.86 C ANISOU 1691 CE MET A1006 15482 12099 9602 -2841 2772 2286 C ATOM 1692 N LEU A1007 30.638 15.255 66.899 1.00 92.70 N ANISOU 1692 N LEU A1007 14870 12016 8336 -1999 2680 2665 N ATOM 1693 CA LEU A1007 30.708 14.144 67.842 1.00 95.40 C ANISOU 1693 CA LEU A1007 15409 12295 8543 -1860 2888 2903 C ATOM 1694 C LEU A1007 31.798 14.354 68.883 1.00 94.98 C ANISOU 1694 C LEU A1007 15320 12522 8245 -1565 2840 3021 C ATOM 1695 O LEU A1007 31.648 13.925 70.031 1.00 96.03 O ANISOU 1695 O LEU A1007 15524 12733 8230 -1457 2974 3177 O ATOM 1696 CB LEU A1007 30.946 12.833 67.097 1.00100.88 C ANISOU 1696 CB LEU A1007 16362 12659 9309 -1844 3029 3027 C ATOM 1697 CG LEU A1007 29.849 12.391 66.134 1.00109.45 C ANISOU 1697 CG LEU A1007 17523 13442 10620 -2139 3109 2934 C ATOM 1698 CD1 LEU A1007 30.072 10.949 65.699 1.00116.24 C ANISOU 1698 CD1 LEU A1007 18686 13971 11509 -2100 3292 3093 C ATOM 1699 CD2 LEU A1007 28.486 12.558 66.785 1.00112.32 C ANISOU 1699 CD2 LEU A1007 17815 13835 11026 -2347 3204 2903 C ATOM 1700 N ARG A1008 32.897 15.009 68.511 1.00 94.27 N ANISOU 1700 N ARG A1008 15116 12598 8104 -1434 2652 2951 N ATOM 1701 CA ARG A1008 33.957 15.261 69.479 1.00 98.64 C ANISOU 1701 CA ARG A1008 15611 13448 8419 -1164 2589 3049 C ATOM 1702 C ARG A1008 33.464 16.177 70.591 1.00102.13 C ANISOU 1702 C ARG A1008 15887 14162 8755 -1190 2538 2979 C ATOM 1703 O ARG A1008 33.743 15.946 71.773 1.00102.50 O ANISOU 1703 O ARG A1008 15964 14384 8598 -1007 2606 3122 O ATOM 1704 CB ARG A1008 35.175 15.865 68.782 1.00 95.26 C ANISOU 1704 CB ARG A1008 15068 13152 7973 -1057 2387 2966 C ATOM 1705 CG ARG A1008 36.480 15.726 69.559 1.00 98.02 C ANISOU 1705 CG ARG A1008 15410 13757 8075 -747 2353 3115 C ATOM 1706 CD ARG A1008 37.514 16.732 69.066 1.00104.81 C ANISOU 1706 CD ARG A1008 16071 14838 8913 -697 2115 2980 C ATOM 1707 NE ARG A1008 37.068 18.108 69.280 1.00112.77 N ANISOU 1707 NE ARG A1008 16859 16034 9954 -859 1955 2764 N ATOM 1708 CZ ARG A1008 37.281 18.797 70.398 1.00119.40 C ANISOU 1708 CZ ARG A1008 17571 17181 10614 -777 1882 2744 C ATOM 1709 NH1 ARG A1008 37.939 18.240 71.405 1.00117.18 N ANISOU 1709 NH1 ARG A1008 17348 17070 10105 -532 1950 2931 N ATOM 1710 NH2 ARG A1008 36.838 20.043 70.510 1.00120.28 N ANISOU 1710 NH2 ARG A1008 17505 17430 10767 -931 1743 2538 N ATOM 1711 N ILE A1009 32.719 17.223 70.225 1.00105.20 N ANISOU 1711 N ILE A1009 16106 14591 9274 -1406 2420 2761 N ATOM 1712 CA ILE A1009 32.176 18.142 71.222 1.00103.39 C ANISOU 1712 CA ILE A1009 15726 14604 8952 -1438 2372 2678 C ATOM 1713 C ILE A1009 31.142 17.435 72.090 1.00102.51 C ANISOU 1713 C ILE A1009 15725 14419 8807 -1479 2589 2810 C ATOM 1714 O ILE A1009 31.162 17.537 73.322 1.00110.63 O ANISOU 1714 O ILE A1009 16732 15654 9647 -1349 2631 2893 O ATOM 1715 CB ILE A1009 31.581 19.384 70.535 1.00105.33 C ANISOU 1715 CB ILE A1009 15786 14881 9353 -1653 2211 2418 C ATOM 1716 CG1 ILE A1009 32.698 20.304 70.040 1.00106.98 C ANISOU 1716 CG1 ILE A1009 15859 15250 9537 -1582 1986 2293 C ATOM 1717 CG2 ILE A1009 30.637 20.120 71.472 1.00108.11 C ANISOU 1717 CG2 ILE A1009 16028 15399 9649 -1728 2221 2343 C ATOM 1718 CD1 ILE A1009 32.414 20.932 68.695 1.00112.02 C ANISOU 1718 CD1 ILE A1009 16414 15753 10394 -1775 1868 2098 C ATOM 1719 N ASP A1010 30.230 16.695 71.459 1.00 99.42 N ANISOU 1719 N ASP A1010 15449 13735 8592 -1665 2731 2832 N ATOM 1720 CA ASP A1010 29.118 16.104 72.196 1.00101.81 C ANISOU 1720 CA ASP A1010 15834 13961 8889 -1752 2936 2937 C ATOM 1721 C ASP A1010 29.531 14.834 72.929 1.00104.99 C ANISOU 1721 C ASP A1010 16458 14284 9148 -1560 3137 3207 C ATOM 1722 O ASP A1010 29.286 14.702 74.131 1.00101.11 O ANISOU 1722 O ASP A1010 15984 13934 8499 -1461 3241 3326 O ATOM 1723 CB ASP A1010 27.948 15.829 71.253 1.00100.31 C ANISOU 1723 CB ASP A1010 15669 13505 8941 -2046 3009 2847 C ATOM 1724 CG ASP A1010 27.109 17.065 71.003 1.00 98.74 C ANISOU 1724 CG ASP A1010 15245 13431 8841 -2234 2876 2618 C ATOM 1725 OD1 ASP A1010 27.438 18.121 71.580 1.00 91.12 O ANISOU 1725 OD1 ASP A1010 14124 12738 7759 -2138 2735 2528 O ATOM 1726 OD2 ASP A1010 26.127 16.986 70.238 1.00 99.97 O ANISOU 1726 OD2 ASP A1010 15383 13417 9185 -2473 2913 2524 O ATOM 1727 N GLU A1011 30.146 13.879 72.226 1.00 87.73 N ANISOU 1727 N GLU A1011 11624 12161 9550 -1141 744 3512 N ATOM 1728 CA GLU A1011 30.574 12.651 72.892 1.00 97.90 C ANISOU 1728 CA GLU A1011 13076 13293 10828 -1192 696 3828 C ATOM 1729 C GLU A1011 31.707 12.922 73.875 1.00103.85 C ANISOU 1729 C GLU A1011 13804 14127 11527 -1149 479 4081 C ATOM 1730 O GLU A1011 31.680 12.435 75.011 1.00116.80 O ANISOU 1730 O GLU A1011 15602 15806 12972 -1327 385 4285 O ATOM 1731 CB GLU A1011 31.006 11.600 71.865 1.00103.21 C ANISOU 1731 CB GLU A1011 13824 13622 11769 -993 746 3914 C ATOM 1732 CG GLU A1011 29.908 11.112 70.932 1.00105.95 C ANISOU 1732 CG GLU A1011 14258 13838 12162 -1061 921 3702 C ATOM 1733 CD GLU A1011 28.798 10.387 71.665 1.00115.41 C ANISOU 1733 CD GLU A1011 15617 15061 13173 -1389 981 3733 C ATOM 1734 OE1 GLU A1011 27.758 11.015 71.942 1.00118.55 O ANISOU 1734 OE1 GLU A1011 15917 15724 13402 -1592 1071 3510 O ATOM 1735 OE2 GLU A1011 28.967 9.189 71.974 1.00123.60 O ANISOU 1735 OE2 GLU A1011 16877 15853 14234 -1451 930 3974 O ATOM 1736 N GLY A1012 32.707 13.692 73.459 1.00103.06 N ANISOU 1736 N GLY A1012 13518 14057 11584 -947 381 4081 N ATOM 1737 CA GLY A1012 33.847 13.988 74.305 1.00111.45 C ANISOU 1737 CA GLY A1012 14513 15196 12637 -901 142 4311 C ATOM 1738 C GLY A1012 34.998 13.034 74.061 1.00120.38 C ANISOU 1738 C GLY A1012 15604 16091 14045 -668 39 4567 C ATOM 1739 O GLY A1012 34.916 12.166 73.192 1.00124.34 O ANISOU 1739 O GLY A1012 16149 16359 14736 -526 173 4541 O ATOM 1740 N ALA A1013 39.586 10.662 72.615 1.00116.02 N ANISOU 1740 N ALA A1013 14372 14950 14760 512 -296 5049 N ATOM 1741 CA ALA A1013 40.578 10.506 71.558 1.00116.30 C ANISOU 1741 CA ALA A1013 14070 14976 15142 838 -160 4936 C ATOM 1742 C ALA A1013 40.336 9.221 70.777 1.00125.14 C ANISOU 1742 C ALA A1013 15358 15750 16438 1081 -15 4839 C ATOM 1743 O ALA A1013 41.054 8.235 70.950 1.00122.19 O ANISOU 1743 O ALA A1013 14950 15143 16335 1381 -193 4947 O ATOM 1744 CB ALA A1013 41.983 10.517 72.143 1.00119.76 C ANISOU 1744 CB ALA A1013 14170 15497 15836 1040 -452 5123 C ATOM 1745 N GLU A1014 39.321 9.237 69.915 1.00148.38 N ANISOU 1745 N GLU A1014 18496 18640 19240 963 274 4621 N ATOM 1746 CA GLU A1014 38.929 8.066 69.141 1.00152.96 C ANISOU 1746 CA GLU A1014 19301 18878 19940 1140 410 4501 C ATOM 1747 C GLU A1014 38.987 8.394 67.657 1.00151.01 C ANISOU 1747 C GLU A1014 18911 18716 19750 1248 763 4198 C ATOM 1748 O GLU A1014 38.288 9.298 67.188 1.00147.51 O ANISOU 1748 O GLU A1014 18503 18458 19086 1004 931 4056 O ATOM 1749 CB GLU A1014 37.528 7.590 69.532 1.00155.03 C ANISOU 1749 CB GLU A1014 19998 18956 19950 847 393 4536 C ATOM 1750 CG GLU A1014 37.276 7.520 71.035 1.00157.13 C ANISOU 1750 CG GLU A1014 20444 19236 20022 604 103 4825 C ATOM 1751 CD GLU A1014 38.054 6.415 71.740 1.00164.73 C ANISOU 1751 CD GLU A1014 21516 19889 21183 820 -228 5093 C ATOM 1752 OE1 GLU A1014 39.029 5.877 71.171 1.00167.38 O ANISOU 1752 OE1 GLU A1014 21669 20060 21866 1225 -263 5045 O ATOM 1753 OE2 GLU A1014 37.681 6.079 72.882 1.00167.31 O ANISOU 1753 OE2 GLU A1014 22124 20139 21309 582 -466 5346 O ATOM 1754 N LYS A1015 39.811 7.650 66.925 1.00152.39 N ANISOU 1754 N LYS A1015 18943 18748 20210 1618 859 4086 N ATOM 1755 CA LYS A1015 39.926 7.782 65.480 1.00153.76 C ANISOU 1755 CA LYS A1015 19023 18988 20410 1733 1217 3787 C ATOM 1756 C LYS A1015 38.954 6.883 64.728 1.00162.63 C ANISOU 1756 C LYS A1015 20549 19771 21471 1750 1348 3608 C ATOM 1757 O LYS A1015 38.944 6.900 63.493 1.00165.94 O ANISOU 1757 O LYS A1015 20972 20209 21868 1832 1637 3346 O ATOM 1758 CB LYS A1015 41.361 7.475 65.039 1.00156.40 C ANISOU 1758 CB LYS A1015 18945 19403 21076 2132 1302 3700 C ATOM 1759 N LEU A1016 38.149 6.097 65.441 1.00175.79 N ANISOU 1759 N LEU A1016 22571 21134 23088 1643 1138 3750 N ATOM 1760 CA LEU A1016 37.158 5.216 64.838 1.00179.18 C ANISOU 1760 CA LEU A1016 23401 21220 23458 1599 1211 3609 C ATOM 1761 C LEU A1016 35.840 5.920 64.552 1.00175.46 C ANISOU 1761 C LEU A1016 23105 20883 22680 1201 1328 3512 C ATOM 1762 O LEU A1016 34.861 5.250 64.208 1.00180.15 O ANISOU 1762 O LEU A1016 24028 21218 23204 1082 1345 3423 O ATOM 1763 CB LEU A1016 36.911 4.011 65.748 1.00183.15 C ANISOU 1763 CB LEU A1016 24218 21319 24050 1617 909 3831 C ATOM 1764 N PHE A1017 35.796 7.247 64.686 1.00165.04 N ANISOU 1764 N PHE A1017 21568 19943 21195 1002 1378 3516 N ATOM 1765 CA PHE A1017 34.540 7.972 64.520 1.00154.99 C ANISOU 1765 CA PHE A1017 20431 18793 19665 663 1428 3411 C ATOM 1766 C PHE A1017 33.997 7.837 63.103 1.00144.94 C ANISOU 1766 C PHE A1017 19327 17405 18339 679 1632 3129 C ATOM 1767 O PHE A1017 32.780 7.742 62.906 1.00139.81 O ANISOU 1767 O PHE A1017 18900 16665 17557 459 1621 3030 O ATOM 1768 CB PHE A1017 34.739 9.444 64.880 1.00151.83 C ANISOU 1768 CB PHE A1017 19781 18776 19133 506 1401 3446 C ATOM 1769 CG PHE A1017 34.522 9.751 66.335 1.00150.84 C ANISOU 1769 CG PHE A1017 19628 18777 18909 319 1185 3659 C ATOM 1770 CD1 PHE A1017 33.459 9.192 67.024 1.00150.41 C ANISOU 1770 CD1 PHE A1017 19810 18607 18732 106 1104 3716 C ATOM 1771 CD2 PHE A1017 35.381 10.598 67.013 1.00150.07 C ANISOU 1771 CD2 PHE A1017 19274 18929 18815 325 1068 3796 C ATOM 1772 CE1 PHE A1017 33.256 9.477 68.363 1.00148.94 C ANISOU 1772 CE1 PHE A1017 19619 18573 18400 -94 941 3895 C ATOM 1773 CE2 PHE A1017 35.186 10.887 68.349 1.00147.98 C ANISOU 1773 CE2 PHE A1017 19022 18785 18419 147 867 3973 C ATOM 1774 CZ PHE A1017 34.122 10.326 69.026 1.00147.74 C ANISOU 1774 CZ PHE A1017 19242 18657 18235 -61 818 4017 C ATOM 1775 N ASN A1018 34.881 7.813 62.104 1.00138.48 N ANISOU 1775 N ASN A1018 18398 16605 17613 924 1820 2986 N ATOM 1776 CA ASN A1018 34.417 7.824 60.720 1.00134.52 C ANISOU 1776 CA ASN A1018 18083 16034 16996 908 2015 2715 C ATOM 1777 C ASN A1018 33.723 6.516 60.354 1.00134.12 C ANISOU 1777 C ASN A1018 18384 15579 16998 965 1997 2607 C ATOM 1778 O ASN A1018 32.622 6.526 59.792 1.00132.30 O ANISOU 1778 O ASN A1018 18398 15253 16618 764 1997 2465 O ATOM 1779 CB ASN A1018 35.580 8.110 59.771 1.00134.77 C ANISOU 1779 CB ASN A1018 17911 16229 17067 1121 2261 2583 C ATOM 1780 CG ASN A1018 35.106 8.514 58.389 1.00132.07 C ANISOU 1780 CG ASN A1018 17769 15913 16500 1006 2450 2336 C ATOM 1781 OD1 ASN A1018 35.730 8.185 57.380 1.00137.19 O ANISOU 1781 OD1 ASN A1018 18427 16555 17144 1187 2693 2148 O ATOM 1782 ND2 ASN A1018 33.983 9.222 58.338 1.00124.98 N ANISOU 1782 ND2 ASN A1018 17037 15046 15403 707 2326 2319 N ATOM 1783 N GLN A1019 34.348 5.377 60.660 1.00134.31 N ANISOU 1783 N GLN A1019 18449 15336 17248 1239 1942 2668 N ATOM 1784 CA GLN A1019 33.677 4.104 60.411 1.00133.73 C ANISOU 1784 CA GLN A1019 18758 14822 17232 1266 1869 2590 C ATOM 1785 C GLN A1019 32.456 3.933 61.308 1.00133.07 C ANISOU 1785 C GLN A1019 18867 14646 17046 896 1661 2762 C ATOM 1786 O GLN A1019 31.480 3.288 60.908 1.00131.83 O ANISOU 1786 O GLN A1019 19023 14230 16838 738 1626 2659 O ATOM 1787 CB GLN A1019 34.647 2.938 60.600 1.00137.84 C ANISOU 1787 CB GLN A1019 19301 15032 18040 1667 1798 2619 C ATOM 1788 CG GLN A1019 35.141 2.748 62.023 1.00139.67 C ANISOU 1788 CG GLN A1019 19402 15248 18419 1701 1534 2953 C ATOM 1789 CD GLN A1019 35.744 1.377 62.248 1.00145.10 C ANISOU 1789 CD GLN A1019 20258 15479 19395 2057 1347 2993 C ATOM 1790 OE1 GLN A1019 35.101 0.355 62.005 1.00146.74 O ANISOU 1790 OE1 GLN A1019 20873 15256 19626 2032 1250 2935 O ATOM 1791 NE2 GLN A1019 36.987 1.346 62.710 1.00148.19 N ANISOU 1791 NE2 GLN A1019 20340 15942 20025 2395 1260 3086 N ATOM 1792 N ASP A1020 32.490 4.508 62.514 1.00134.12 N ANISOU 1792 N ASP A1020 18814 15010 17137 733 1530 3010 N ATOM 1793 CA ASP A1020 31.321 4.483 63.387 1.00133.59 C ANISOU 1793 CA ASP A1020 18877 14956 16924 343 1393 3144 C ATOM 1794 C ASP A1020 30.161 5.253 62.770 1.00126.00 C ANISOU 1794 C ASP A1020 17922 14178 15775 73 1484 2932 C ATOM 1795 O ASP A1020 29.007 4.812 62.837 1.00124.13 O ANISOU 1795 O ASP A1020 17873 13823 15469 -200 1431 2895 O ATOM 1796 CB ASP A1020 31.674 5.067 64.755 1.00139.13 C ANISOU 1796 CB ASP A1020 19371 15920 17573 239 1264 3410 C ATOM 1797 CG ASP A1020 32.326 4.055 65.681 1.00145.47 C ANISOU 1797 CG ASP A1020 20296 16457 18518 360 1053 3686 C ATOM 1798 OD1 ASP A1020 31.988 4.048 66.885 1.00147.60 O ANISOU 1798 OD1 ASP A1020 20621 16801 18661 101 901 3924 O ATOM 1799 OD2 ASP A1020 33.171 3.265 65.211 1.00149.40 O ANISOU 1799 OD2 ASP A1020 20848 16672 19246 718 1028 3654 O ATOM 1800 N VAL A1021 30.448 6.417 62.180 1.00112.94 N ANISOU 1800 N VAL A1021 16059 12808 14044 130 1594 2798 N ATOM 1801 CA VAL A1021 29.407 7.195 61.510 1.00101.31 C ANISOU 1801 CA VAL A1021 14610 11470 12414 -78 1620 2586 C ATOM 1802 C VAL A1021 28.839 6.414 60.334 1.00106.71 C ANISOU 1802 C VAL A1021 15588 11855 13103 -66 1667 2372 C ATOM 1803 O VAL A1021 27.619 6.298 60.177 1.00107.45 O ANISOU 1803 O VAL A1021 15803 11893 13131 -311 1592 2264 O ATOM 1804 CB VAL A1021 29.952 8.563 61.060 1.00 83.53 C ANISOU 1804 CB VAL A1021 12145 9516 10075 -17 1683 2515 C ATOM 1805 CG1 VAL A1021 28.970 9.238 60.107 1.00 76.17 C ANISOU 1805 CG1 VAL A1021 11317 8624 9001 -170 1663 2278 C ATOM 1806 CG2 VAL A1021 30.219 9.456 62.262 1.00 77.31 C ANISOU 1806 CG2 VAL A1021 11101 9022 9253 -102 1585 2691 C ATOM 1807 N ASP A1022 29.717 5.876 59.484 1.00105.82 N ANISOU 1807 N ASP A1022 15579 11562 13067 220 1791 2283 N ATOM 1808 CA ASP A1022 29.253 5.111 58.331 1.00110.39 C ANISOU 1808 CA ASP A1022 16479 11839 13624 250 1834 2053 C ATOM 1809 C ASP A1022 28.375 3.942 58.761 1.00110.84 C ANISOU 1809 C ASP A1022 16791 11565 13758 80 1682 2106 C ATOM 1810 O ASP A1022 27.322 3.696 58.161 1.00117.98 O ANISOU 1810 O ASP A1022 17903 12333 14592 -122 1621 1946 O ATOM 1811 CB ASP A1022 30.443 4.620 57.506 1.00118.91 C ANISOU 1811 CB ASP A1022 17610 12791 14779 619 2019 1932 C ATOM 1812 CG ASP A1022 31.004 5.692 56.587 1.00120.34 C ANISOU 1812 CG ASP A1022 17657 13267 14799 676 2209 1795 C ATOM 1813 OD1 ASP A1022 30.212 6.469 56.012 1.00119.43 O ANISOU 1813 OD1 ASP A1022 17626 13263 14488 449 2168 1688 O ATOM 1814 OD2 ASP A1022 32.241 5.749 56.431 1.00121.58 O ANISOU 1814 OD2 ASP A1022 17626 13542 15028 936 2385 1793 O ATOM 1815 N ALA A1023 28.779 3.214 59.806 1.00106.63 N ANISOU 1815 N ALA A1023 16261 10891 13363 127 1590 2344 N ATOM 1816 CA ALA A1023 27.930 2.136 60.304 1.00107.33 C ANISOU 1816 CA ALA A1023 16621 10666 13494 -114 1428 2443 C ATOM 1817 C ALA A1023 26.608 2.681 60.828 1.00105.62 C ANISOU 1817 C ALA A1023 16301 10693 13135 -561 1367 2467 C ATOM 1818 O ALA A1023 25.564 2.032 60.693 1.00105.84 O ANISOU 1818 O ALA A1023 16532 10532 13149 -842 1283 2414 O ATOM 1819 CB ALA A1023 28.651 1.339 61.390 1.00111.49 C ANISOU 1819 CB ALA A1023 17201 10994 14165 -4 1297 2734 C ATOM 1820 N ALA A1024 26.628 3.883 61.408 1.00104.35 N ANISOU 1820 N ALA A1024 15810 10961 12879 -630 1406 2519 N ATOM 1821 CA ALA A1024 25.407 4.462 61.958 1.00100.57 C ANISOU 1821 CA ALA A1024 15175 10757 12281 -1003 1364 2491 C ATOM 1822 C ALA A1024 24.394 4.790 60.865 1.00102.54 C ANISOU 1822 C ALA A1024 15460 11015 12486 -1119 1349 2193 C ATOM 1823 O ALA A1024 23.196 4.519 61.024 1.00100.89 O ANISOU 1823 O ALA A1024 15258 10818 12258 -1444 1282 2127 O ATOM 1824 CB ALA A1024 25.746 5.708 62.773 1.00 95.31 C ANISOU 1824 CB ALA A1024 14171 10514 11528 -990 1390 2569 C ATOM 1825 N VAL A1025 24.846 5.377 59.752 1.00107.05 N ANISOU 1825 N VAL A1025 16052 11594 13030 -883 1399 2013 N ATOM 1826 CA VAL A1025 23.900 5.688 58.682 1.00109.25 C ANISOU 1826 CA VAL A1025 16413 11850 13247 -993 1328 1744 C ATOM 1827 C VAL A1025 23.413 4.407 58.023 1.00113.90 C ANISOU 1827 C VAL A1025 17350 12037 13890 -1076 1273 1654 C ATOM 1828 O VAL A1025 22.277 4.352 57.540 1.00115.32 O ANISOU 1828 O VAL A1025 17585 12180 14052 -1304 1151 1482 O ATOM 1829 CB VAL A1025 24.501 6.660 57.645 1.00105.92 C ANISOU 1829 CB VAL A1025 15992 11529 12725 -774 1377 1601 C ATOM 1830 CG1 VAL A1025 25.572 7.526 58.275 1.00101.91 C ANISOU 1830 CG1 VAL A1025 15233 11287 12202 -610 1467 1762 C ATOM 1831 CG2 VAL A1025 25.038 5.922 56.428 1.00110.17 C ANISOU 1831 CG2 VAL A1025 16863 11758 13239 -583 1463 1474 C ATOM 1832 N ARG A1026 24.242 3.357 57.998 1.00112.18 N ANISOU 1832 N ARG A1026 17369 11499 13757 -886 1329 1752 N ATOM 1833 CA ARG A1026 23.769 2.067 57.514 1.00111.68 C ANISOU 1833 CA ARG A1026 17675 11001 13756 -981 1239 1679 C ATOM 1834 C ARG A1026 22.554 1.621 58.314 1.00111.10 C ANISOU 1834 C ARG A1026 17573 10930 13711 -1426 1106 1778 C ATOM 1835 O ARG A1026 21.506 1.292 57.750 1.00113.26 O ANISOU 1835 O ARG A1026 17972 11082 13978 -1677 991 1617 O ATOM 1836 CB ARG A1026 24.885 1.021 57.592 1.00113.78 C ANISOU 1836 CB ARG A1026 18176 10909 14145 -676 1281 1783 C ATOM 1837 CG ARG A1026 26.049 1.251 56.633 1.00113.84 C ANISOU 1837 CG ARG A1026 18219 10900 14134 -243 1453 1617 C ATOM 1838 CD ARG A1026 26.756 -0.056 56.284 1.00118.24 C ANISOU 1838 CD ARG A1026 19109 10986 14832 51 1451 1560 C ATOM 1839 NE ARG A1026 26.976 -0.911 57.449 1.00124.34 N ANISOU 1839 NE ARG A1026 19938 11528 15778 32 1306 1840 N ATOM 1840 CZ ARG A1026 28.082 -0.910 58.186 1.00126.02 C ANISOU 1840 CZ ARG A1026 19970 11795 16117 310 1332 2026 C ATOM 1841 NH1 ARG A1026 29.084 -0.094 57.887 1.00126.04 N ANISOU 1841 NH1 ARG A1026 19677 12104 16108 616 1529 1953 N ATOM 1842 NH2 ARG A1026 28.186 -1.729 59.226 1.00124.86 N ANISOU 1842 NH2 ARG A1026 19948 11391 16102 255 1138 2297 N ATOM 1843 N GLY A1027 22.664 1.659 59.641 1.00109.67 N ANISOU 1843 N GLY A1027 17206 10923 13539 -1560 1124 2040 N ATOM 1844 CA GLY A1027 21.551 1.239 60.475 1.00111.64 C ANISOU 1844 CA GLY A1027 17412 11234 13774 -2033 1049 2147 C ATOM 1845 C GLY A1027 20.346 2.153 60.362 1.00109.83 C ANISOU 1845 C GLY A1027 16855 11390 13485 -2294 1038 1938 C ATOM 1846 O GLY A1027 19.202 1.690 60.415 1.00114.98 O ANISOU 1846 O GLY A1027 17504 12027 14155 -2682 962 1878 O ATOM 1847 N ILE A1028 20.578 3.462 60.224 1.00104.22 N ANISOU 1847 N ILE A1028 15853 11026 12721 -2089 1092 1819 N ATOM 1848 CA ILE A1028 19.469 4.389 60.010 1.00102.41 C ANISOU 1848 CA ILE A1028 15320 11120 12472 -2253 1027 1576 C ATOM 1849 C ILE A1028 18.741 4.047 58.717 1.00102.36 C ANISOU 1849 C ILE A1028 15511 10870 12510 -2312 875 1328 C ATOM 1850 O ILE A1028 17.505 4.081 58.653 1.00101.00 O ANISOU 1850 O ILE A1028 15171 10820 12385 -2606 764 1166 O ATOM 1851 CB ILE A1028 19.974 5.844 60.011 1.00 97.96 C ANISOU 1851 CB ILE A1028 14496 10876 11847 -1985 1056 1503 C ATOM 1852 CG1 ILE A1028 20.572 6.205 61.371 1.00 94.69 C ANISOU 1852 CG1 ILE A1028 13876 10724 11377 -1975 1173 1730 C ATOM 1853 CG2 ILE A1028 18.846 6.809 59.674 1.00 95.39 C ANISOU 1853 CG2 ILE A1028 13894 10814 11535 -2086 921 1217 C ATOM 1854 CD1 ILE A1028 21.234 7.567 61.403 1.00 92.15 C ANISOU 1854 CD1 ILE A1028 13354 10658 11000 -1711 1182 1689 C ATOM 1855 N LEU A1029 19.493 3.699 57.669 1.00102.05 N ANISOU 1855 N LEU A1029 15822 10499 12452 -2039 867 1277 N ATOM 1856 CA LEU A1029 18.864 3.258 56.429 1.00102.44 C ANISOU 1856 CA LEU A1029 16142 10275 12506 -2104 710 1047 C ATOM 1857 C LEU A1029 18.173 1.911 56.601 1.00113.82 C ANISOU 1857 C LEU A1029 17798 11412 14035 -2436 624 1098 C ATOM 1858 O LEU A1029 17.232 1.600 55.862 1.00117.39 O ANISOU 1858 O LEU A1029 18357 11728 14516 -2643 444 905 O ATOM 1859 CB LEU A1029 19.901 3.194 55.307 1.00 96.06 C ANISOU 1859 CB LEU A1029 15676 9213 11608 -1739 769 965 C ATOM 1860 CG LEU A1029 20.613 4.508 54.963 1.00 94.00 C ANISOU 1860 CG LEU A1029 15264 9223 11230 -1468 846 922 C ATOM 1861 CD1 LEU A1029 21.749 4.276 53.976 1.00 92.13 C ANISOU 1861 CD1 LEU A1029 15349 8772 10885 -1152 983 864 C ATOM 1862 CD2 LEU A1029 19.636 5.545 54.430 1.00 81.89 C ANISOU 1862 CD2 LEU A1029 13577 7892 9645 -1585 637 716 C ATOM 1863 N ARG A1030 18.616 1.104 57.571 1.00119.56 N ANISOU 1863 N ARG A1030 18612 12013 14804 -2515 712 1367 N ATOM 1864 CA ARG A1030 17.958 -0.173 57.834 1.00127.47 C ANISOU 1864 CA ARG A1030 19851 12706 15875 -2892 605 1461 C ATOM 1865 C ARG A1030 16.592 0.029 58.479 1.00133.35 C ANISOU 1865 C ARG A1030 20234 13793 16639 -3395 565 1436 C ATOM 1866 O ARG A1030 15.618 -0.635 58.105 1.00137.54 O ANISOU 1866 O ARG A1030 20866 14161 17231 -3747 414 1338 O ATOM 1867 CB ARG A1030 18.836 -1.049 58.730 1.00129.72 C ANISOU 1867 CB ARG A1030 20365 12738 16186 -2842 663 1783 C ATOM 1868 CG ARG A1030 19.634 -2.133 58.011 1.00133.20 C ANISOU 1868 CG ARG A1030 21328 12588 16694 -2562 586 1771 C ATOM 1869 CD ARG A1030 20.658 -1.530 57.069 1.00131.81 C ANISOU 1869 CD ARG A1030 21178 12421 16483 -2023 699 1583 C ATOM 1870 NE ARG A1030 21.703 -2.470 56.672 1.00135.50 N ANISOU 1870 NE ARG A1030 22042 12415 17026 -1659 698 1584 N ATOM 1871 CZ ARG A1030 22.739 -2.805 57.435 1.00136.83 C ANISOU 1871 CZ ARG A1030 22229 12482 17280 -1413 743 1810 C ATOM 1872 NH1 ARG A1030 22.867 -2.291 58.651 1.00133.59 N ANISOU 1872 NH1 ARG A1030 21503 12404 16852 -1531 792 2078 N ATOM 1873 NH2 ARG A1030 23.644 -3.661 56.983 1.00140.97 N ANISOU 1873 NH2 ARG A1030 23088 12567 17909 -1036 720 1747 N ATOM 1874 N ASN A1031 16.500 0.934 59.451 1.00134.78 N ANISOU 1874 N ASN A1031 19978 14462 16770 -3442 700 1501 N ATOM 1875 CA ASN A1031 15.253 1.124 60.178 1.00137.46 C ANISOU 1875 CA ASN A1031 19918 15191 17120 -3908 720 1451 C ATOM 1876 C ASN A1031 14.205 1.795 59.302 1.00134.85 C ANISOU 1876 C ASN A1031 19315 15046 16875 -3950 566 1088 C ATOM 1877 O ASN A1031 14.452 2.852 58.711 1.00134.51 O ANISOU 1877 O ASN A1031 19146 15138 16825 -3593 516 903 O ATOM 1878 CB ASN A1031 15.495 1.953 61.436 1.00136.92 C ANISOU 1878 CB ASN A1031 19474 15599 16950 -3899 915 1573 C ATOM 1879 CG ASN A1031 16.036 1.125 62.577 1.00140.26 C ANISOU 1879 CG ASN A1031 20106 15910 17275 -4095 1021 1951 C ATOM 1880 OD1 ASN A1031 16.826 0.206 62.368 1.00143.16 O ANISOU 1880 OD1 ASN A1031 20929 15799 17668 -3967 949 2147 O ATOM 1881 ND2 ASN A1031 15.599 1.433 63.792 1.00141.03 N ANISOU 1881 ND2 ASN A1031 19889 16443 17253 -4407 1174 2044 N ATOM 1882 N ALA A1032 13.024 1.174 59.231 1.00131.70 N ANISOU 1882 N ALA A1032 18833 14645 16561 -4409 461 997 N ATOM 1883 CA ALA A1032 11.903 1.752 58.499 1.00124.54 C ANISOU 1883 CA ALA A1032 17608 13938 15774 -4491 269 648 C ATOM 1884 C ALA A1032 11.345 3.002 59.170 1.00116.02 C ANISOU 1884 C ALA A1032 15892 13468 14724 -4464 354 470 C ATOM 1885 O ALA A1032 10.691 3.807 58.500 1.00112.01 O ANISOU 1885 O ALA A1032 15116 13119 14324 -4335 155 158 O ATOM 1886 CB ALA A1032 10.800 0.708 58.333 1.00131.57 C ANISOU 1886 CB ALA A1032 18534 14688 16769 -5031 133 607 C ATOM 1887 N LYS A1033 11.597 3.190 60.468 1.00115.42 N ANISOU 1887 N LYS A1033 15593 13716 14546 -4565 618 647 N ATOM 1888 CA LYS A1033 11.161 4.406 61.147 1.00112.61 C ANISOU 1888 CA LYS A1033 14661 13930 14197 -4488 716 446 C ATOM 1889 C LYS A1033 12.127 5.563 60.930 1.00111.84 C ANISOU 1889 C LYS A1033 14600 13853 14042 -3933 690 412 C ATOM 1890 O LYS A1033 11.700 6.720 60.897 1.00111.07 O ANISOU 1890 O LYS A1033 14117 14073 14012 -3742 607 136 O ATOM 1891 CB LYS A1033 11.003 4.144 62.644 1.00111.96 C ANISOU 1891 CB LYS A1033 14350 14211 13977 -4861 1018 632 C ATOM 1892 CG LYS A1033 9.868 3.189 63.007 1.00114.60 C ANISOU 1892 CG LYS A1033 14526 14668 14350 -5507 1078 639 C ATOM 1893 CD LYS A1033 10.257 2.260 64.149 1.00115.60 C ANISOU 1893 CD LYS A1033 14906 14755 14261 -5906 1309 1047 C ATOM 1894 CE LYS A1033 9.093 1.346 64.506 1.00123.17 C ANISOU 1894 CE LYS A1033 15710 15856 15232 -6624 1375 1067 C ATOM 1895 NZ LYS A1033 9.461 0.307 65.510 1.00127.17 N ANISOU 1895 NZ LYS A1033 16590 16221 15507 -7074 1533 1514 N ATOM 1896 N LEU A1034 13.419 5.276 60.773 1.00112.67 N ANISOU 1896 N LEU A1034 15153 13618 14038 -3674 742 675 N ATOM 1897 CA LEU A1034 14.425 6.324 60.647 1.00114.71 C ANISOU 1897 CA LEU A1034 15444 13914 14227 -3212 746 685 C ATOM 1898 C LEU A1034 14.782 6.644 59.204 1.00115.25 C ANISOU 1898 C LEU A1034 15797 13670 14322 -2892 532 552 C ATOM 1899 O LEU A1034 15.215 7.766 58.921 1.00114.38 O ANISOU 1899 O LEU A1034 15620 13661 14177 -2578 463 463 O ATOM 1900 CB LEU A1034 15.698 5.925 61.399 1.00113.61 C ANISOU 1900 CB LEU A1034 15553 13657 13956 -3110 941 1042 C ATOM 1901 CG LEU A1034 15.551 5.744 62.910 1.00113.01 C ANISOU 1901 CG LEU A1034 15266 13897 13777 -3403 1146 1220 C ATOM 1902 CD1 LEU A1034 16.867 5.310 63.531 1.00112.35 C ANISOU 1902 CD1 LEU A1034 15483 13625 13581 -3267 1252 1584 C ATOM 1903 CD2 LEU A1034 15.055 7.028 63.545 1.00110.03 C ANISOU 1903 CD2 LEU A1034 14394 14038 13374 -3353 1195 992 C ATOM 1904 N LYS A1035 14.619 5.687 58.290 1.00114.75 N ANISOU 1904 N LYS A1035 16084 13224 14293 -2989 420 540 N ATOM 1905 CA LYS A1035 15.003 5.916 56.897 1.00111.33 C ANISOU 1905 CA LYS A1035 15986 12494 13821 -2714 243 417 C ATOM 1906 C LYS A1035 14.233 7.054 56.234 1.00108.43 C ANISOU 1906 C LYS A1035 15389 12302 13508 -2618 -28 116 C ATOM 1907 O LYS A1035 14.873 7.899 55.584 1.00109.36 O ANISOU 1907 O LYS A1035 15658 12366 13526 -2315 -109 82 O ATOM 1908 CB LYS A1035 14.856 4.612 56.105 1.00114.53 C ANISOU 1908 CB LYS A1035 16820 12456 14240 -2869 162 424 C ATOM 1909 CG LYS A1035 15.819 4.482 54.935 1.00112.18 C ANISOU 1909 CG LYS A1035 17007 11800 13818 -2552 139 409 C ATOM 1910 CD LYS A1035 15.100 4.489 53.597 1.00114.15 C ANISOU 1910 CD LYS A1035 17469 11853 14051 -2595 -153 146 C ATOM 1911 CE LYS A1035 16.079 4.259 52.454 1.00115.53 C ANISOU 1911 CE LYS A1035 18164 11690 14044 -2319 -120 121 C ATOM 1912 NZ LYS A1035 15.427 4.383 51.121 1.00117.55 N ANISOU 1912 NZ LYS A1035 18676 11768 14218 -2360 -425 -132 N ATOM 1913 N PRO A1036 12.898 7.149 56.339 1.00104.85 N ANISOU 1913 N PRO A1036 14576 12051 13211 -2860 -197 -108 N ATOM 1914 CA PRO A1036 12.196 8.207 55.584 1.00103.14 C ANISOU 1914 CA PRO A1036 14185 11927 13075 -2712 -540 -409 C ATOM 1915 C PRO A1036 12.603 9.616 55.978 1.00104.43 C ANISOU 1915 C PRO A1036 14126 12346 13208 -2406 -553 -454 C ATOM 1916 O PRO A1036 12.856 10.451 55.100 1.00105.25 O ANISOU 1916 O PRO A1036 14423 12319 13250 -2158 -798 -541 O ATOM 1917 CB PRO A1036 10.717 7.931 55.893 1.00106.52 C ANISOU 1917 CB PRO A1036 14160 12590 13723 -3047 -664 -635 C ATOM 1918 CG PRO A1036 10.669 6.511 56.302 1.00109.18 C ANISOU 1918 CG PRO A1036 14647 12790 14048 -3418 -454 -437 C ATOM 1919 CD PRO A1036 11.943 6.276 57.042 1.00106.68 C ANISOU 1919 CD PRO A1036 14557 12416 13560 -3296 -121 -109 C ATOM 1920 N VAL A1037 12.663 9.913 57.277 1.00105.47 N ANISOU 1920 N VAL A1037 13888 12827 13358 -2442 -316 -396 N ATOM 1921 CA VAL A1037 13.047 11.256 57.702 1.00101.14 C ANISOU 1921 CA VAL A1037 13146 12500 12781 -2156 -350 -455 C ATOM 1922 C VAL A1037 14.496 11.540 57.325 1.00100.78 C ANISOU 1922 C VAL A1037 13525 12226 12541 -1905 -270 -208 C ATOM 1923 O VAL A1037 14.843 12.662 56.938 1.00 99.21 O ANISOU 1923 O VAL A1037 13383 12017 12296 -1659 -454 -271 O ATOM 1924 CB VAL A1037 12.801 11.433 59.213 1.00 98.44 C ANISOU 1924 CB VAL A1037 12349 12592 12463 -2275 -91 -461 C ATOM 1925 CG1 VAL A1037 13.521 10.354 60.013 1.00101.55 C ANISOU 1925 CG1 VAL A1037 12919 12945 12720 -2482 268 -113 C ATOM 1926 CG2 VAL A1037 13.236 12.819 59.666 1.00 92.25 C ANISOU 1926 CG2 VAL A1037 11406 12001 11642 -1969 -147 -539 C ATOM 1927 N TYR A1038 15.358 10.523 57.407 1.00104.23 N ANISOU 1927 N TYR A1038 14263 12468 12871 -1970 -13 68 N ATOM 1928 CA TYR A1038 16.768 10.709 57.079 1.00104.03 C ANISOU 1928 CA TYR A1038 14571 12270 12685 -1737 103 283 C ATOM 1929 C TYR A1038 16.942 11.109 55.620 1.00101.94 C ANISOU 1929 C TYR A1038 14654 11750 12329 -1591 -125 182 C ATOM 1930 O TYR A1038 17.748 11.989 55.297 1.00 98.97 O ANISOU 1930 O TYR A1038 14405 11369 11830 -1397 -153 242 O ATOM 1931 CB TYR A1038 17.545 9.429 57.383 1.00106.15 C ANISOU 1931 CB TYR A1038 15075 12352 12907 -1808 378 546 C ATOM 1932 CG TYR A1038 19.040 9.532 57.164 1.00106.55 C ANISOU 1932 CG TYR A1038 15375 12277 12831 -1557 536 751 C ATOM 1933 CD1 TYR A1038 19.874 10.024 58.160 1.00105.14 C ANISOU 1933 CD1 TYR A1038 15023 12306 12621 -1453 689 934 C ATOM 1934 CD2 TYR A1038 19.620 9.122 55.969 1.00108.07 C ANISOU 1934 CD2 TYR A1038 15962 12167 12932 -1437 540 742 C ATOM 1935 CE1 TYR A1038 21.239 10.112 57.970 1.00103.94 C ANISOU 1935 CE1 TYR A1038 15035 12072 12386 -1239 828 1110 C ATOM 1936 CE2 TYR A1038 20.986 9.209 55.771 1.00107.12 C ANISOU 1936 CE2 TYR A1038 16001 11988 12710 -1216 722 897 C ATOM 1937 CZ TYR A1038 21.789 9.706 56.775 1.00104.08 C ANISOU 1937 CZ TYR A1038 15391 11823 12333 -1121 859 1084 C ATOM 1938 OH TYR A1038 23.149 9.797 56.588 1.00101.98 O ANISOU 1938 OH TYR A1038 15222 11531 11995 -914 1032 1228 O ATOM 1939 N ASP A1039 16.194 10.464 54.720 1.00107.93 N ANISOU 1939 N ASP A1039 15595 12293 13119 -1720 -299 37 N ATOM 1940 CA ASP A1039 16.266 10.825 53.308 1.00107.25 C ANISOU 1940 CA ASP A1039 15885 11965 12899 -1621 -544 -70 C ATOM 1941 C ASP A1039 15.821 12.264 53.084 1.00114.84 C ANISOU 1941 C ASP A1039 16698 13054 13881 -1499 -884 -231 C ATOM 1942 O ASP A1039 16.414 12.987 52.276 1.00114.39 O ANISOU 1942 O ASP A1039 16948 12874 13641 -1368 -1008 -197 O ATOM 1943 CB ASP A1039 15.415 9.866 52.473 1.00105.24 C ANISOU 1943 CB ASP A1039 15838 11464 12685 -1808 -718 -218 C ATOM 1944 CG ASP A1039 15.871 8.423 52.593 1.00101.59 C ANISOU 1944 CG ASP A1039 15608 10791 12202 -1914 -439 -72 C ATOM 1945 OD1 ASP A1039 17.026 8.190 53.011 1.00 99.28 O ANISOU 1945 OD1 ASP A1039 15410 10485 11828 -1777 -133 139 O ATOM 1946 OD2 ASP A1039 15.078 7.518 52.257 1.00100.40 O ANISOU 1946 OD2 ASP A1039 15551 10466 12131 -2129 -559 -174 O ATOM 1947 N SER A1040 14.780 12.700 53.798 1.00132.99 N ANISOU 1947 N SER A1040 18533 15599 16399 -1545 -1042 -415 N ATOM 1948 CA SER A1040 14.271 14.055 53.618 1.00138.32 C ANISOU 1948 CA SER A1040 19052 16359 17143 -1386 -1423 -613 C ATOM 1949 C SER A1040 15.294 15.103 54.033 1.00136.76 C ANISOU 1949 C SER A1040 18892 16245 16824 -1191 -1344 -464 C ATOM 1950 O SER A1040 15.337 16.193 53.451 1.00139.60 O ANISOU 1950 O SER A1040 19408 16507 17126 -1051 -1676 -530 O ATOM 1951 CB SER A1040 12.984 14.236 54.422 1.00147.52 C ANISOU 1951 CB SER A1040 19637 17820 18595 -1446 -1547 -884 C ATOM 1952 OG SER A1040 12.213 13.047 54.431 1.00152.76 O ANISOU 1952 OG SER A1040 20184 18486 19372 -1715 -1466 -945 O ATOM 1953 N LEU A1041 16.126 14.790 55.021 1.00124.46 N ANISOU 1953 N LEU A1041 17222 14846 15223 -1199 -946 -252 N ATOM 1954 CA LEU A1041 17.029 15.777 55.590 1.00107.53 C ANISOU 1954 CA LEU A1041 15040 12821 12995 -1046 -881 -122 C ATOM 1955 C LEU A1041 18.202 16.072 54.661 1.00 96.99 C ANISOU 1955 C LEU A1041 14162 11269 11421 -979 -861 78 C ATOM 1956 O LEU A1041 18.596 15.251 53.829 1.00 95.04 O ANISOU 1956 O LEU A1041 14242 10824 11046 -1040 -733 166 O ATOM 1957 CB LEU A1041 17.558 15.297 56.939 1.00101.57 C ANISOU 1957 CB LEU A1041 14035 12300 12257 -1095 -490 52 C ATOM 1958 CG LEU A1041 16.540 15.156 58.063 1.00 96.09 C ANISOU 1958 CG LEU A1041 12869 11908 11733 -1199 -437 -123 C ATOM 1959 CD1 LEU A1041 17.225 14.645 59.316 1.00 92.71 C ANISOU 1959 CD1 LEU A1041 12316 11667 11241 -1280 -63 111 C ATOM 1960 CD2 LEU A1041 15.853 16.487 58.322 1.00 94.72 C ANISOU 1960 CD2 LEU A1041 12413 11905 11673 -1042 -742 -408 C ATOM 1961 N ASP A1042 18.755 17.269 54.817 1.00 87.92 N ANISOU 1961 N ASP A1042 13032 10169 10204 -866 -985 133 N ATOM 1962 CA ASP A1042 20.009 17.633 54.186 1.00 84.92 C ANISOU 1962 CA ASP A1042 13005 9674 9588 -853 -893 358 C ATOM 1963 C ASP A1042 21.177 17.043 54.974 1.00 87.70 C ANISOU 1963 C ASP A1042 13249 10167 9906 -849 -444 608 C ATOM 1964 O ASP A1042 21.005 16.452 56.043 1.00 92.53 O ANISOU 1964 O ASP A1042 13562 10940 10654 -860 -251 626 O ATOM 1965 CB ASP A1042 20.128 19.150 54.090 1.00 87.53 C ANISOU 1965 CB ASP A1042 13408 9981 9867 -780 -1238 337 C ATOM 1966 CG ASP A1042 19.680 19.841 55.355 1.00 94.79 C ANISOU 1966 CG ASP A1042 13914 11117 10985 -673 -1339 209 C ATOM 1967 OD1 ASP A1042 20.535 20.425 56.055 1.00 97.52 O ANISOU 1967 OD1 ASP A1042 14192 11579 11284 -640 -1231 359 O ATOM 1968 OD2 ASP A1042 18.469 19.779 55.655 1.00 98.68 O ANISOU 1968 OD2 ASP A1042 14135 11681 11679 -630 -1517 -61 O ATOM 1969 N ALA A1043 22.385 17.218 54.432 1.00 89.16 N ANISOU 1969 N ALA A1043 13680 10298 9898 -847 -289 803 N ATOM 1970 CA ALA A1043 23.560 16.585 55.024 1.00 84.96 C ANISOU 1970 CA ALA A1043 13046 9877 9358 -814 110 1026 C ATOM 1971 C ALA A1043 23.764 17.023 56.469 1.00 87.08 C ANISOU 1971 C ALA A1043 12956 10378 9751 -771 148 1108 C ATOM 1972 O ALA A1043 24.108 16.204 57.329 1.00 88.11 O ANISOU 1972 O ALA A1043 12909 10604 9966 -755 398 1224 O ATOM 1973 CB ALA A1043 24.804 16.894 54.190 1.00 80.89 C ANISOU 1973 CB ALA A1043 12784 9327 8625 -829 257 1184 C ATOM 1974 N VAL A1044 23.548 18.306 56.761 1.00 87.59 N ANISOU 1974 N VAL A1044 12949 10514 9818 -753 -127 1044 N ATOM 1975 CA VAL A1044 23.785 18.806 58.113 1.00 84.38 C ANISOU 1975 CA VAL A1044 12243 10326 9491 -714 -104 1097 C ATOM 1976 C VAL A1044 22.807 18.174 59.099 1.00 74.82 C ANISOU 1976 C VAL A1044 10741 9261 8428 -725 -41 959 C ATOM 1977 O VAL A1044 23.207 17.653 60.145 1.00 73.31 O ANISOU 1977 O VAL A1044 10368 9225 8260 -746 186 1095 O ATOM 1978 CB VAL A1044 23.700 20.343 58.140 1.00 84.62 C ANISOU 1978 CB VAL A1044 12308 10352 9492 -680 -456 1016 C ATOM 1979 CG1 VAL A1044 23.966 20.866 59.550 1.00 78.39 C ANISOU 1979 CG1 VAL A1044 11239 9785 8762 -637 -438 1044 C ATOM 1980 CG2 VAL A1044 24.682 20.936 57.150 1.00 86.86 C ANISOU 1980 CG2 VAL A1044 12911 10500 9592 -751 -504 1191 C ATOM 1981 N ARG A1045 21.512 18.207 58.779 1.00 75.19 N ANISOU 1981 N ARG A1045 10735 9268 8567 -736 -251 690 N ATOM 1982 CA ARG A1045 20.516 17.656 59.693 1.00 77.55 C ANISOU 1982 CA ARG A1045 10716 9755 8994 -799 -171 536 C ATOM 1983 C ARG A1045 20.609 16.138 59.794 1.00 81.94 C ANISOU 1983 C ARG A1045 11308 10269 9557 -930 132 685 C ATOM 1984 O ARG A1045 20.253 15.567 60.831 1.00 84.64 O ANISOU 1984 O ARG A1045 11425 10794 9940 -1040 301 700 O ATOM 1985 CB ARG A1045 19.118 18.083 59.259 1.00 76.21 C ANISOU 1985 CB ARG A1045 10429 9571 8955 -774 -487 188 C ATOM 1986 CG ARG A1045 18.919 19.583 59.299 1.00 77.03 C ANISOU 1986 CG ARG A1045 10486 9689 9091 -610 -842 5 C ATOM 1987 CD ARG A1045 17.475 19.944 59.050 1.00 84.93 C ANISOU 1987 CD ARG A1045 11281 10709 10281 -541 -1167 -379 C ATOM 1988 NE ARG A1045 17.239 21.378 59.179 1.00 90.93 N ANISOU 1988 NE ARG A1045 11990 11453 11107 -338 -1548 -590 N ATOM 1989 CZ ARG A1045 17.370 22.247 58.183 1.00 95.55 C ANISOU 1989 CZ ARG A1045 12907 11743 11654 -242 -1954 -598 C ATOM 1990 NH1 ARG A1045 17.739 21.828 56.980 1.00 95.47 N ANISOU 1990 NH1 ARG A1045 13291 11474 11508 -348 -1988 -413 N ATOM 1991 NH2 ARG A1045 17.134 23.535 58.389 1.00 98.99 N ANISOU 1991 NH2 ARG A1045 13313 12129 12171 -50 -2337 -795 N ATOM 1992 N ARG A1046 21.072 15.464 58.739 1.00 82.07 N ANISOU 1992 N ARG A1046 11632 10035 9515 -933 198 789 N ATOM 1993 CA ARG A1046 21.348 14.036 58.860 1.00 84.95 C ANISOU 1993 CA ARG A1046 12082 10303 9894 -1015 462 943 C ATOM 1994 C ARG A1046 22.397 13.779 59.933 1.00 82.11 C ANISOU 1994 C ARG A1046 11626 10063 9509 -983 693 1207 C ATOM 1995 O ARG A1046 22.307 12.800 60.682 1.00 84.68 O ANISOU 1995 O ARG A1046 11895 10406 9875 -1088 849 1318 O ATOM 1996 CB ARG A1046 21.804 13.467 57.516 1.00 87.79 C ANISOU 1996 CB ARG A1046 12807 10373 10175 -973 496 972 C ATOM 1997 CG ARG A1046 20.715 13.391 56.460 1.00 91.59 C ANISOU 1997 CG ARG A1046 13439 10692 10670 -1044 259 733 C ATOM 1998 CD ARG A1046 21.276 12.880 55.145 1.00 97.47 C ANISOU 1998 CD ARG A1046 14594 11167 11274 -1005 315 756 C ATOM 1999 NE ARG A1046 20.337 13.054 54.042 1.00100.75 N ANISOU 1999 NE ARG A1046 15209 11422 11651 -1069 20 536 N ATOM 2000 CZ ARG A1046 20.563 12.647 52.797 1.00104.49 C ANISOU 2000 CZ ARG A1046 16080 11660 11963 -1073 13 496 C ATOM 2001 NH1 ARG A1046 21.700 12.036 52.491 1.00107.68 N ANISOU 2001 NH1 ARG A1046 16687 11980 12248 -993 320 630 N ATOM 2002 NH2 ARG A1046 19.650 12.850 51.858 1.00107.94 N ANISOU 2002 NH2 ARG A1046 16705 11951 12356 -1147 -311 302 N ATOM 2003 N ALA A1047 23.395 14.661 60.032 1.00 76.48 N ANISOU 2003 N ALA A1047 10909 9423 8727 -863 683 1323 N ATOM 2004 CA ALA A1047 24.408 14.521 61.071 1.00 76.64 C ANISOU 2004 CA ALA A1047 10814 9568 8736 -827 844 1567 C ATOM 2005 C ALA A1047 23.809 14.730 62.456 1.00 75.76 C ANISOU 2005 C ALA A1047 10444 9708 8632 -929 829 1536 C ATOM 2006 O ALA A1047 24.231 14.090 63.426 1.00 76.29 O ANISOU 2006 O ALA A1047 10455 9845 8687 -981 969 1731 O ATOM 2007 CB ALA A1047 25.547 15.504 60.822 1.00 74.30 C ANISOU 2007 CB ALA A1047 10545 9314 8370 -718 808 1678 C ATOM 2008 N ALA A1048 22.822 15.623 62.568 1.00 72.25 N ANISOU 2008 N ALA A1048 9850 9402 8200 -952 650 1277 N ATOM 2009 CA ALA A1048 22.131 15.801 63.839 1.00 73.00 C ANISOU 2009 CA ALA A1048 9678 9779 8281 -1055 678 1177 C ATOM 2010 C ALA A1048 21.332 14.558 64.206 1.00 82.47 C ANISOU 2010 C ALA A1048 10823 11005 9505 -1269 841 1179 C ATOM 2011 O ALA A1048 21.256 14.186 65.382 1.00 82.16 O ANISOU 2011 O ALA A1048 10665 11163 9389 -1419 985 1275 O ATOM 2012 CB ALA A1048 21.224 17.028 63.779 1.00 68.28 C ANISOU 2012 CB ALA A1048 8908 9311 7725 -982 437 836 C ATOM 2013 N LEU A1049 20.736 13.900 63.210 1.00 85.70 N ANISOU 2013 N LEU A1049 11351 11212 10000 -1320 809 1086 N ATOM 2014 CA LEU A1049 20.049 12.638 63.461 1.00 81.72 C ANISOU 2014 CA LEU A1049 10846 10677 9525 -1565 944 1121 C ATOM 2015 C LEU A1049 21.044 11.552 63.856 1.00 80.03 C ANISOU 2015 C LEU A1049 10852 10293 9263 -1601 1114 1473 C ATOM 2016 O LEU A1049 20.799 10.776 64.788 1.00 87.05 O ANISOU 2016 O LEU A1049 11713 11261 10102 -1828 1237 1609 O ATOM 2017 CB LEU A1049 19.247 12.224 62.225 1.00 80.45 C ANISOU 2017 CB LEU A1049 10797 10300 9471 -1605 820 936 C ATOM 2018 CG LEU A1049 18.297 11.042 62.418 1.00 80.46 C ANISOU 2018 CG LEU A1049 10763 10283 9526 -1912 905 915 C ATOM 2019 CD1 LEU A1049 17.380 11.309 63.595 1.00 84.27 C ANISOU 2019 CD1 LEU A1049 10857 11173 9990 -2127 990 779 C ATOM 2020 CD2 LEU A1049 17.488 10.792 61.157 1.00 78.14 C ANISOU 2020 CD2 LEU A1049 10567 9782 9341 -1942 722 700 C ATOM 2021 N ILE A1050 22.179 11.488 63.153 1.00 75.42 N ANISOU 2021 N ILE A1050 10490 9477 8691 -1382 1113 1620 N ATOM 2022 CA ILE A1050 23.248 10.564 63.526 1.00 76.96 C ANISOU 2022 CA ILE A1050 10853 9505 8883 -1332 1233 1925 C ATOM 2023 C ILE A1050 23.712 10.838 64.950 1.00 79.80 C ANISOU 2023 C ILE A1050 11064 10104 9153 -1383 1275 2113 C ATOM 2024 O ILE A1050 23.998 9.909 65.717 1.00 79.27 O ANISOU 2024 O ILE A1050 11093 9965 9061 -1490 1338 2349 O ATOM 2025 CB ILE A1050 24.414 10.669 62.524 1.00 78.27 C ANISOU 2025 CB ILE A1050 11186 9471 9082 -1058 1247 1984 C ATOM 2026 CG1 ILE A1050 23.997 10.148 61.149 1.00 76.83 C ANISOU 2026 CG1 ILE A1050 11232 9019 8939 -1036 1226 1818 C ATOM 2027 CG2 ILE A1050 25.638 9.918 63.033 1.00 79.27 C ANISOU 2027 CG2 ILE A1050 11391 9481 9248 -935 1341 2269 C ATOM 2028 CD1 ILE A1050 24.961 10.527 60.054 1.00 73.53 C ANISOU 2028 CD1 ILE A1050 10955 8494 8490 -810 1260 1800 C ATOM 2029 N ASN A1051 23.792 12.118 65.324 1.00 80.10 N ANISOU 2029 N ASN A1051 10905 10402 9129 -1313 1206 2014 N ATOM 2030 CA ASN A1051 24.182 12.495 66.679 1.00 77.87 C ANISOU 2030 CA ASN A1051 10496 10365 8727 -1370 1223 2154 C ATOM 2031 C ASN A1051 23.265 11.853 67.713 1.00 83.59 C ANISOU 2031 C ASN A1051 11161 11256 9345 -1678 1321 2166 C ATOM 2032 O ASN A1051 23.728 11.295 68.714 1.00 72.81 O ANISOU 2032 O ASN A1051 9873 9919 7872 -1794 1369 2427 O ATOM 2033 CB ASN A1051 24.167 14.021 66.807 1.00 76.40 C ANISOU 2033 CB ASN A1051 10129 10404 8494 -1262 1101 1963 C ATOM 2034 CG ASN A1051 24.704 14.509 68.140 1.00 80.98 C ANISOU 2034 CG ASN A1051 10614 11221 8935 -1296 1091 2093 C ATOM 2035 OD1 ASN A1051 24.204 14.140 69.202 1.00 90.96 O ANISOU 2035 OD1 ASN A1051 11821 12672 10066 -1502 1179 2120 O ATOM 2036 ND2 ASN A1051 25.731 15.349 68.088 1.00 76.69 N ANISOU 2036 ND2 ASN A1051 10067 10678 8395 -1128 982 2176 N ATOM 2037 N MET A1052 21.954 11.928 67.483 1.00 80.84 N ANISOU 2037 N MET A1052 10670 11029 9015 -1836 1342 1888 N ATOM 2038 CA MET A1052 21.010 11.293 68.394 1.00 79.81 C ANISOU 2038 CA MET A1052 10451 11101 8772 -2191 1477 1881 C ATOM 2039 C MET A1052 21.164 9.779 68.382 1.00 85.61 C ANISOU 2039 C MET A1052 11468 11541 9520 -2382 1537 2168 C ATOM 2040 O MET A1052 20.994 9.121 69.415 1.00 86.02 O ANISOU 2040 O MET A1052 11580 11690 9412 -2682 1631 2360 O ATOM 2041 CB MET A1052 19.585 11.694 68.025 1.00 79.95 C ANISOU 2041 CB MET A1052 10196 11320 8861 -2300 1476 1488 C ATOM 2042 CG MET A1052 19.275 13.144 68.326 1.00 84.66 C ANISOU 2042 CG MET A1052 10501 12232 9434 -2137 1402 1177 C ATOM 2043 SD MET A1052 17.699 13.691 67.652 1.00 89.51 S ANISOU 2043 SD MET A1052 10772 13013 10223 -2142 1307 672 S ATOM 2044 CE MET A1052 16.565 12.675 68.592 1.00 85.49 C ANISOU 2044 CE MET A1052 10052 12821 9608 -2634 1585 642 C ATOM 2045 N VAL A1053 21.481 9.207 67.219 1.00 91.36 N ANISOU 2045 N VAL A1053 12406 11891 10414 -2225 1468 2197 N ATOM 2046 CA VAL A1053 21.628 7.759 67.121 1.00 96.07 C ANISOU 2046 CA VAL A1053 13310 12140 11052 -2365 1481 2434 C ATOM 2047 C VAL A1053 22.858 7.292 67.890 1.00 96.68 C ANISOU 2047 C VAL A1053 13581 12079 11075 -2270 1456 2798 C ATOM 2048 O VAL A1053 22.850 6.220 68.506 1.00 96.09 O ANISOU 2048 O VAL A1053 13729 11838 10942 -2499 1450 3049 O ATOM 2049 CB VAL A1053 21.678 7.333 65.642 1.00 93.43 C ANISOU 2049 CB VAL A1053 13162 11441 10897 -2181 1411 2317 C ATOM 2050 CG1 VAL A1053 22.090 5.874 65.515 1.00 97.31 C ANISOU 2050 CG1 VAL A1053 14018 11503 11452 -2227 1389 2555 C ATOM 2051 CG2 VAL A1053 20.322 7.558 64.988 1.00 91.96 C ANISOU 2051 CG2 VAL A1053 12819 11357 10764 -2350 1382 1993 C ATOM 2052 N PHE A1054 23.929 8.088 67.873 1.00 96.25 N ANISOU 2052 N PHE A1054 13451 12078 11041 -1949 1408 2841 N ATOM 2053 CA PHE A1054 25.114 7.755 68.657 1.00 99.90 C ANISOU 2053 CA PHE A1054 14034 12450 11475 -1840 1344 3168 C ATOM 2054 C PHE A1054 24.795 7.708 70.146 1.00105.45 C ANISOU 2054 C PHE A1054 14723 13407 11936 -2163 1361 3337 C ATOM 2055 O PHE A1054 25.272 6.823 70.867 1.00110.57 O ANISOU 2055 O PHE A1054 15606 13877 12527 -2263 1283 3655 O ATOM 2056 CB PHE A1054 26.219 8.776 68.384 1.00101.39 C ANISOU 2056 CB PHE A1054 14070 12727 11727 -1493 1294 3148 C ATOM 2057 CG PHE A1054 27.275 8.293 67.435 1.00106.28 C ANISOU 2057 CG PHE A1054 14807 13026 12549 -1165 1270 3215 C ATOM 2058 CD1 PHE A1054 27.005 8.159 66.083 1.00103.01 C ANISOU 2058 CD1 PHE A1054 14462 12431 12245 -1050 1327 3001 C ATOM 2059 CD2 PHE A1054 28.545 7.987 67.895 1.00111.06 C ANISOU 2059 CD2 PHE A1054 15440 13528 13229 -964 1187 3469 C ATOM 2060 CE1 PHE A1054 27.982 7.717 65.207 1.00103.77 C ANISOU 2060 CE1 PHE A1054 14658 12273 12496 -749 1350 3020 C ATOM 2061 CE2 PHE A1054 29.525 7.547 67.030 1.00112.17 C ANISOU 2061 CE2 PHE A1054 15628 13419 13573 -638 1195 3481 C ATOM 2062 CZ PHE A1054 29.245 7.412 65.682 1.00108.57 C ANISOU 2062 CZ PHE A1054 15244 12809 13199 -532 1302 3246 C ATOM 2063 N GLN A1055 23.981 8.649 70.620 1.00102.90 N ANISOU 2063 N GLN A1055 14146 13493 11457 -2328 1448 3113 N ATOM 2064 CA GLN A1055 23.737 8.788 72.049 1.00 93.91 C ANISOU 2064 CA GLN A1055 12977 12671 10035 -2621 1500 3224 C ATOM 2065 C GLN A1055 22.699 7.792 72.551 1.00 95.87 C ANISOU 2065 C GLN A1055 13342 12950 10134 -3094 1619 3297 C ATOM 2066 O GLN A1055 22.848 7.241 73.648 1.00 96.88 O ANISOU 2066 O GLN A1055 13663 13118 10030 -3372 1615 3583 O ATOM 2067 CB GLN A1055 23.291 10.218 72.350 1.00 89.79 C ANISOU 2067 CB GLN A1055 12128 12581 9407 -2577 1555 2902 C ATOM 2068 CG GLN A1055 22.962 10.501 73.805 1.00 95.29 C ANISOU 2068 CG GLN A1055 12769 13667 9769 -2870 1647 2930 C ATOM 2069 CD GLN A1055 22.308 11.854 73.979 1.00 97.02 C ANISOU 2069 CD GLN A1055 12653 14292 9920 -2804 1710 2514 C ATOM 2070 OE1 GLN A1055 21.841 12.455 73.011 1.00102.11 O ANISOU 2070 OE1 GLN A1055 13106 14919 10771 -2607 1681 2203 O ATOM 2071 NE2 GLN A1055 22.275 12.345 75.212 1.00 99.81 N ANISOU 2071 NE2 GLN A1055 12959 14991 9972 -2959 1770 2496 N ATOM 2072 N MET A1056 21.652 7.545 71.762 1.00 95.12 N ANISOU 2072 N MET A1056 13150 12834 10157 -3222 1705 3058 N ATOM 2073 CA MET A1056 20.492 6.791 72.213 1.00 98.26 C ANISOU 2073 CA MET A1056 13560 13360 10414 -3731 1847 3059 C ATOM 2074 C MET A1056 20.282 5.479 71.472 1.00 97.74 C ANISOU 2074 C MET A1056 13788 12837 10510 -3867 1777 3200 C ATOM 2075 O MET A1056 19.494 4.648 71.938 1.00100.28 O ANISOU 2075 O MET A1056 14213 13187 10700 -4352 1859 3307 O ATOM 2076 CB MET A1056 19.223 7.646 72.069 1.00102.94 C ANISOU 2076 CB MET A1056 13711 14398 11003 -3845 2004 2607 C ATOM 2077 CG MET A1056 19.419 9.122 72.377 1.00104.43 C ANISOU 2077 CG MET A1056 13602 14941 11137 -3562 2009 2349 C ATOM 2078 SD MET A1056 17.948 10.106 72.032 1.00105.00 S ANISOU 2078 SD MET A1056 13152 15447 11298 -3581 2115 1765 S ATOM 2079 CE MET A1056 16.763 9.326 73.129 1.00113.67 C ANISOU 2079 CE MET A1056 14120 16947 12123 -4240 2414 1769 C ATOM 2080 N GLY A1057 20.945 5.268 70.339 1.00 97.38 N ANISOU 2080 N GLY A1057 13890 12382 10727 -3480 1634 3190 N ATOM 2081 CA GLY A1057 20.675 4.116 69.507 1.00101.97 C ANISOU 2081 CA GLY A1057 14748 12523 11474 -3568 1559 3238 C ATOM 2082 C GLY A1057 19.460 4.332 68.625 1.00103.58 C ANISOU 2082 C GLY A1057 14723 12844 11789 -3693 1617 2874 C ATOM 2083 O GLY A1057 18.680 5.271 68.791 1.00102.16 O ANISOU 2083 O GLY A1057 14151 13108 11557 -3769 1723 2590 O ATOM 2084 N GLU A1058 19.296 3.423 67.663 1.00106.90 N ANISOU 2084 N GLU A1058 15400 12838 12379 -3699 1516 2865 N ATOM 2085 CA GLU A1058 18.239 3.589 66.671 1.00112.22 C ANISOU 2085 CA GLU A1058 15897 13557 13186 -3776 1505 2522 C ATOM 2086 C GLU A1058 16.856 3.443 67.295 1.00114.62 C ANISOU 2086 C GLU A1058 15940 14220 13391 -4331 1628 2422 C ATOM 2087 O GLU A1058 15.929 4.179 66.938 1.00114.40 O ANISOU 2087 O GLU A1058 15521 14515 13432 -4362 1661 2071 O ATOM 2088 CB GLU A1058 18.430 2.585 65.540 1.00119.75 C ANISOU 2088 CB GLU A1058 17238 13950 14313 -3673 1355 2540 C ATOM 2089 CG GLU A1058 19.741 2.752 64.804 1.00122.85 C ANISOU 2089 CG GLU A1058 17827 14045 14805 -3121 1284 2566 C ATOM 2090 CD GLU A1058 20.091 1.543 63.972 1.00129.55 C ANISOU 2090 CD GLU A1058 19125 14313 15784 -3026 1159 2629 C ATOM 2091 OE1 GLU A1058 19.201 0.696 63.751 1.00133.66 O ANISOU 2091 OE1 GLU A1058 19807 14642 16336 -3381 1092 2603 O ATOM 2092 OE2 GLU A1058 21.260 1.433 63.549 1.00129.92 O ANISOU 2092 OE2 GLU A1058 19355 14102 15907 -2600 1129 2686 O ATOM 2093 N THR A1059 16.699 2.503 68.231 1.00119.71 N ANISOU 2093 N THR A1059 16790 14821 13874 -4783 1686 2724 N ATOM 2094 CA THR A1059 15.403 2.310 68.875 1.00124.01 C ANISOU 2094 CA THR A1059 17074 15755 14290 -5384 1851 2646 C ATOM 2095 C THR A1059 14.995 3.536 69.684 1.00121.59 C ANISOU 2095 C THR A1059 16255 16115 13830 -5394 2062 2412 C ATOM 2096 O THR A1059 13.820 3.925 69.689 1.00122.36 O ANISOU 2096 O THR A1059 15908 16631 13954 -5637 2188 2089 O ATOM 2097 CB THR A1059 15.441 1.070 69.768 1.00131.63 C ANISOU 2097 CB THR A1059 18438 16518 15057 -5901 1861 3073 C ATOM 2098 OG1 THR A1059 16.512 1.195 70.713 1.00137.30 O ANISOU 2098 OG1 THR A1059 19363 17224 15579 -5750 1857 3382 O ATOM 2099 CG2 THR A1059 15.659 -0.180 68.933 1.00131.23 C ANISOU 2099 CG2 THR A1059 18891 15783 15186 -5919 1624 3244 C ATOM 2100 N GLY A1060 15.950 4.155 70.380 1.00117.93 N ANISOU 2100 N GLY A1060 15832 15759 13216 -5121 2087 2546 N ATOM 2101 CA GLY A1060 15.633 5.347 71.151 1.00117.30 C ANISOU 2101 CA GLY A1060 15314 16275 12981 -5090 2264 2300 C ATOM 2102 C GLY A1060 15.278 6.533 70.275 1.00114.98 C ANISOU 2102 C GLY A1060 14624 16148 12916 -4677 2197 1841 C ATOM 2103 O GLY A1060 14.354 7.290 70.586 1.00117.89 O ANISOU 2103 O GLY A1060 14526 17005 13262 -4768 2329 1485 O ATOM 2104 N VAL A1061 16.003 6.713 69.169 1.00109.70 N ANISOU 2104 N VAL A1061 14143 15076 12463 -4219 1982 1833 N ATOM 2105 CA VAL A1061 15.708 7.821 68.265 1.00107.86 C ANISOU 2105 CA VAL A1061 13622 14934 12425 -3846 1861 1440 C ATOM 2106 C VAL A1061 14.346 7.626 67.610 1.00110.67 C ANISOU 2106 C VAL A1061 13709 15387 12952 -4070 1832 1127 C ATOM 2107 O VAL A1061 13.611 8.592 67.368 1.00110.02 O ANISOU 2107 O VAL A1061 13219 15602 12983 -3931 1784 732 O ATOM 2108 CB VAL A1061 16.830 7.969 67.222 1.00105.32 C ANISOU 2108 CB VAL A1061 13611 14165 12239 -3380 1664 1540 C ATOM 2109 CG1 VAL A1061 16.493 9.055 66.226 1.00102.16 C ANISOU 2109 CG1 VAL A1061 12998 13812 12008 -3058 1500 1174 C ATOM 2110 CG2 VAL A1061 18.143 8.281 67.913 1.00106.49 C ANISOU 2110 CG2 VAL A1061 13921 14287 12252 -3159 1682 1811 C ATOM 2111 N ALA A1062 13.979 6.373 67.326 1.00109.33 N ANISOU 2111 N ALA A1062 13765 14954 12820 -4420 1826 1290 N ATOM 2112 CA ALA A1062 12.691 6.104 66.694 1.00108.61 C ANISOU 2112 CA ALA A1062 13420 14942 12904 -4678 1771 1010 C ATOM 2113 C ALA A1062 11.525 6.513 67.585 1.00113.00 C ANISOU 2113 C ALA A1062 13410 16130 13395 -5024 1987 742 C ATOM 2114 O ALA A1062 10.438 6.816 67.082 1.00118.31 O ANISOU 2114 O ALA A1062 13675 17013 14264 -5083 1918 371 O ATOM 2115 CB ALA A1062 12.580 4.625 66.328 1.00111.48 C ANISOU 2115 CB ALA A1062 14183 14878 13298 -5037 1714 1268 C ATOM 2116 N GLY A1063 11.727 6.539 68.903 1.00113.88 N ANISOU 2116 N GLY A1063 13474 16568 13228 -5250 2244 903 N ATOM 2117 CA GLY A1063 10.658 6.917 69.808 1.00113.28 C ANISOU 2117 CA GLY A1063 12854 17146 13043 -5593 2511 624 C ATOM 2118 C GLY A1063 10.142 8.324 69.612 1.00112.65 C ANISOU 2118 C GLY A1063 12232 17442 13126 -5193 2460 99 C ATOM 2119 O GLY A1063 9.058 8.650 70.106 1.00113.80 O ANISOU 2119 O GLY A1063 11826 18134 13277 -5422 2650 -254 O ATOM 2120 N PHE A1064 10.885 9.168 68.896 1.00112.65 N ANISOU 2120 N PHE A1064 12373 17164 13263 -4608 2199 29 N ATOM 2121 CA PHE A1064 10.444 10.532 68.617 1.00119.57 C ANISOU 2121 CA PHE A1064 12819 18296 14318 -4193 2060 -452 C ATOM 2122 C PHE A1064 9.601 10.560 67.350 1.00126.55 C ANISOU 2122 C PHE A1064 13518 19021 15545 -4092 1776 -744 C ATOM 2123 O PHE A1064 9.843 11.377 66.457 1.00125.29 O ANISOU 2123 O PHE A1064 13416 18627 15562 -3630 1460 -908 O ATOM 2124 CB PHE A1064 11.638 11.471 68.477 1.00114.03 C ANISOU 2124 CB PHE A1064 12387 17364 13575 -3669 1887 -366 C ATOM 2125 CG PHE A1064 12.552 11.496 69.673 1.00112.78 C ANISOU 2125 CG PHE A1064 12430 17326 13094 -3732 2099 -75 C ATOM 2126 CD1 PHE A1064 13.501 10.503 69.851 1.00112.39 C ANISOU 2126 CD1 PHE A1064 12875 16939 12890 -3893 2147 431 C ATOM 2127 CD2 PHE A1064 12.493 12.531 70.594 1.00111.30 C ANISOU 2127 CD2 PHE A1064 11960 17560 12768 -3598 2206 -321 C ATOM 2128 CE1 PHE A1064 14.353 10.526 70.925 1.00110.67 C ANISOU 2128 CE1 PHE A1064 12854 16808 12387 -3940 2279 709 C ATOM 2129 CE2 PHE A1064 13.352 12.564 71.677 1.00109.77 C ANISOU 2129 CE2 PHE A1064 11986 17462 12259 -3663 2361 -50 C ATOM 2130 CZ PHE A1064 14.284 11.556 71.842 1.00108.44 C ANISOU 2130 CZ PHE A1064 12302 16959 11942 -3842 2386 480 C ATOM 2131 N THR A1065 8.605 9.675 67.276 1.00133.69 N ANISOU 2131 N THR A1065 14217 20050 16529 -4556 1865 -799 N ATOM 2132 CA THR A1065 7.806 9.535 66.062 1.00136.86 C ANISOU 2132 CA THR A1065 14485 20266 17249 -4522 1562 -1036 C ATOM 2133 C THR A1065 7.174 10.860 65.657 1.00137.62 C ANISOU 2133 C THR A1065 14102 20588 17599 -4085 1314 -1559 C ATOM 2134 O THR A1065 7.207 11.246 64.483 1.00139.12 O ANISOU 2134 O THR A1065 14438 20426 17996 -3747 920 -1671 O ATOM 2135 CB THR A1065 6.722 8.475 66.266 1.00142.96 C ANISOU 2135 CB THR A1065 14999 21255 18064 -5154 1726 -1056 C ATOM 2136 OG1 THR A1065 5.798 8.921 67.269 1.00148.49 O ANISOU 2136 OG1 THR A1065 15028 22657 18734 -5372 2018 -1395 O ATOM 2137 CG2 THR A1065 7.332 7.154 66.704 1.00142.65 C ANISOU 2137 CG2 THR A1065 15491 20937 17771 -5601 1920 -523 C ATOM 2138 N ASN A1066 6.579 11.564 66.621 1.00138.19 N ANISOU 2138 N ASN A1066 13616 21241 17649 -4089 1527 -1898 N ATOM 2139 CA ASN A1066 5.970 12.855 66.325 1.00136.23 C ANISOU 2139 CA ASN A1066 12899 21197 17666 -3629 1264 -2432 C ATOM 2140 C ASN A1066 7.017 13.854 65.846 1.00128.10 C ANISOU 2140 C ASN A1066 12277 19776 16620 -3054 959 -2360 C ATOM 2141 O ASN A1066 6.828 14.528 64.827 1.00127.24 O ANISOU 2141 O ASN A1066 12179 19409 16758 -2680 520 -2575 O ATOM 2142 CB ASN A1066 5.238 13.380 67.562 1.00139.97 C ANISOU 2142 CB ASN A1066 12722 22382 18079 -3728 1605 -2821 C ATOM 2143 CG ASN A1066 4.464 14.654 67.286 1.00142.53 C ANISOU 2143 CG ASN A1066 12493 22929 18732 -3241 1313 -3445 C ATOM 2144 OD1 ASN A1066 4.258 15.474 68.182 1.00144.38 O ANISOU 2144 OD1 ASN A1066 12344 23606 18908 -3066 1491 -3787 O ATOM 2145 ND2 ASN A1066 4.036 14.830 66.041 1.00143.54 N ANISOU 2145 ND2 ASN A1066 12604 22732 19204 -3004 833 -3606 N ATOM 2146 N SER A1067 8.138 13.952 66.566 1.00121.24 N ANISOU 2146 N SER A1067 11764 18850 15451 -3007 1163 -2038 N ATOM 2147 CA SER A1067 9.186 14.894 66.184 1.00112.64 C ANISOU 2147 CA SER A1067 11047 17421 14329 -2524 902 -1944 C ATOM 2148 C SER A1067 9.813 14.515 64.848 1.00105.06 C ANISOU 2148 C SER A1067 10618 15862 13437 -2407 606 -1662 C ATOM 2149 O SER A1067 10.125 15.390 64.031 1.00100.13 O ANISOU 2149 O SER A1067 10165 14961 12918 -2017 244 -1755 O ATOM 2150 CB SER A1067 10.255 14.957 67.274 1.00111.36 C ANISOU 2150 CB SER A1067 11133 17345 13835 -2558 1187 -1639 C ATOM 2151 OG SER A1067 9.669 15.121 68.553 1.00116.84 O ANISOU 2151 OG SER A1067 11391 18612 14390 -2755 1520 -1870 O ATOM 2152 N LEU A1068 10.012 13.215 64.613 1.00106.92 N ANISOU 2152 N LEU A1068 11148 15884 13594 -2754 750 -1321 N ATOM 2153 CA LEU A1068 10.576 12.768 63.343 1.00104.78 C ANISOU 2153 CA LEU A1068 11381 15066 13363 -2654 509 -1095 C ATOM 2154 C LEU A1068 9.650 13.100 62.181 1.00112.08 C ANISOU 2154 C LEU A1068 12158 15869 14559 -2523 110 -1430 C ATOM 2155 O LEU A1068 10.110 13.511 61.110 1.00107.89 O ANISOU 2155 O LEU A1068 11979 14957 14056 -2244 -206 -1395 O ATOM 2156 CB LEU A1068 10.855 11.265 63.384 1.00100.29 C ANISOU 2156 CB LEU A1068 11136 14291 12680 -3047 725 -723 C ATOM 2157 CG LEU A1068 12.043 10.796 64.224 1.00 96.57 C ANISOU 2157 CG LEU A1068 10997 13745 11949 -3115 1003 -298 C ATOM 2158 CD1 LEU A1068 12.259 9.298 64.058 1.00 89.05 C ANISOU 2158 CD1 LEU A1068 10417 12478 10939 -3449 1107 38 C ATOM 2159 CD2 LEU A1068 13.298 11.572 63.857 1.00 83.81 C ANISOU 2159 CD2 LEU A1068 9700 11880 10263 -2683 876 -159 C ATOM 2160 N ARG A1069 8.341 12.914 62.370 1.00126.64 N ANISOU 2160 N ARG A1069 13482 18043 16594 -2746 111 -1752 N ATOM 2161 CA ARG A1069 7.387 13.280 61.330 1.00130.02 C ANISOU 2161 CA ARG A1069 13705 18383 17313 -2607 -322 -2102 C ATOM 2162 C ARG A1069 7.518 14.757 60.978 1.00132.42 C ANISOU 2162 C ARG A1069 13969 18624 17719 -2085 -690 -2358 C ATOM 2163 O ARG A1069 7.669 15.121 59.808 1.00135.10 O ANISOU 2163 O ARG A1069 14638 18569 18126 -1853 -1109 -2366 O ATOM 2164 CB ARG A1069 5.962 12.950 61.783 1.00135.54 C ANISOU 2164 CB ARG A1069 13725 19550 18225 -2922 -228 -2448 C ATOM 2165 N MET A1070 7.512 15.619 61.996 1.00130.68 N ANISOU 2165 N MET A1070 13405 18767 17479 -1911 -547 -2555 N ATOM 2166 CA MET A1070 7.589 17.057 61.761 1.00127.88 C ANISOU 2166 CA MET A1070 13012 18338 17237 -1418 -925 -2823 C ATOM 2167 C MET A1070 8.902 17.465 61.103 1.00122.12 C ANISOU 2167 C MET A1070 12961 17123 16315 -1193 -1103 -2470 C ATOM 2168 O MET A1070 8.931 18.442 60.347 1.00122.08 O ANISOU 2168 O MET A1070 13114 16859 16411 -857 -1563 -2611 O ATOM 2169 CB MET A1070 7.391 17.799 63.077 1.00128.91 C ANISOU 2169 CB MET A1070 12680 18951 17348 -1302 -689 -3102 C ATOM 2170 CG MET A1070 6.089 17.436 63.779 1.00134.06 C ANISOU 2170 CG MET A1070 12604 20167 18165 -1548 -449 -3487 C ATOM 2171 SD MET A1070 5.859 18.395 65.283 1.00135.00 S ANISOU 2171 SD MET A1070 12197 20876 18222 -1370 -160 -3887 S ATOM 2172 CE MET A1070 7.459 18.132 66.044 1.00127.49 C ANISOU 2172 CE MET A1070 11866 19775 16801 -1504 202 -3301 C ATOM 2173 N LEU A1071 9.994 16.746 61.371 1.00117.65 N ANISOU 2173 N LEU A1071 12796 16430 15475 -1381 -762 -2017 N ATOM 2174 CA LEU A1071 11.231 16.996 60.635 1.00111.59 C ANISOU 2174 CA LEU A1071 12633 15231 14536 -1213 -895 -1688 C ATOM 2175 C LEU A1071 11.055 16.661 59.163 1.00115.13 C ANISOU 2175 C LEU A1071 13422 15279 15044 -1214 -1224 -1655 C ATOM 2176 O LEU A1071 11.499 17.407 58.282 1.00117.81 O ANISOU 2176 O LEU A1071 14112 15309 15342 -984 -1562 -1623 O ATOM 2177 CB LEU A1071 12.382 16.179 61.221 1.00105.95 C ANISOU 2177 CB LEU A1071 12213 14481 13563 -1402 -468 -1243 C ATOM 2178 CG LEU A1071 13.215 16.782 62.350 1.00103.59 C ANISOU 2178 CG LEU A1071 11880 14379 13100 -1303 -258 -1125 C ATOM 2179 CD1 LEU A1071 14.406 15.888 62.672 1.00 99.33 C ANISOU 2179 CD1 LEU A1071 11689 13711 12342 -1463 64 -660 C ATOM 2180 CD2 LEU A1071 13.680 18.178 61.980 1.00102.98 C ANISOU 2180 CD2 LEU A1071 11946 14146 13034 -947 -598 -1221 C ATOM 2181 N GLN A1072 10.424 15.520 58.880 1.00115.75 N ANISOU 2181 N GLN A1072 13441 15350 15190 -1509 -1134 -1648 N ATOM 2182 CA GLN A1072 10.159 15.136 57.499 1.00111.31 C ANISOU 2182 CA GLN A1072 13203 14419 14670 -1538 -1459 -1652 C ATOM 2183 C GLN A1072 9.271 16.163 56.807 1.00115.90 C ANISOU 2183 C GLN A1072 13608 14954 15476 -1287 -2012 -2025 C ATOM 2184 O GLN A1072 9.468 16.470 55.625 1.00116.60 O ANISOU 2184 O GLN A1072 14125 14669 15507 -1161 -2389 -1986 O ATOM 2185 CB GLN A1072 9.521 13.749 57.466 1.00109.69 C ANISOU 2185 CB GLN A1072 12911 14241 14525 -1927 -1285 -1617 C ATOM 2186 CG GLN A1072 9.308 13.194 56.078 1.00110.10 C ANISOU 2186 CG GLN A1072 13355 13896 14583 -1996 -1591 -1604 C ATOM 2187 CD GLN A1072 8.713 11.802 56.105 1.00112.80 C ANISOU 2187 CD GLN A1072 13640 14235 14985 -2408 -1431 -1560 C ATOM 2188 OE1 GLN A1072 8.410 11.266 57.171 1.00114.23 O ANISOU 2188 OE1 GLN A1072 13473 14729 15202 -2671 -1094 -1530 O ATOM 2189 NE2 GLN A1072 8.543 11.208 54.930 1.00112.67 N ANISOU 2189 NE2 GLN A1072 14002 13856 14953 -2496 -1685 -1551 N ATOM 2190 N GLN A1073 8.297 16.720 57.532 1.00121.38 N ANISOU 2190 N GLN A1073 13679 16023 16416 -1204 -2081 -2401 N ATOM 2191 CA GLN A1073 7.487 17.817 57.010 1.00127.35 C ANISOU 2191 CA GLN A1073 14223 16736 17430 -886 -2647 -2791 C ATOM 2192 C GLN A1073 8.273 19.117 56.885 1.00125.15 C ANISOU 2192 C GLN A1073 14260 16244 17048 -520 -2908 -2746 C ATOM 2193 O GLN A1073 7.698 20.124 56.454 1.00128.50 O ANISOU 2193 O GLN A1073 14588 16561 17676 -219 -3440 -3048 O ATOM 2194 CB GLN A1073 6.265 18.058 57.903 1.00132.44 C ANISOU 2194 CB GLN A1073 14052 17884 18384 -862 -2606 -3254 C ATOM 2195 CG GLN A1073 5.562 16.811 58.419 1.00134.98 C ANISOU 2195 CG GLN A1073 13972 18547 18768 -1309 -2208 -3275 C ATOM 2196 CD GLN A1073 4.491 16.289 57.484 1.00140.90 C ANISOU 2196 CD GLN A1073 14562 19203 19771 -1457 -2568 -3472 C ATOM 2197 OE1 GLN A1073 4.593 16.419 56.265 1.00142.61 O ANISOU 2197 OE1 GLN A1073 15224 18977 19986 -1336 -3027 -3409 O ATOM 2198 NE2 GLN A1073 3.451 15.693 58.055 1.00144.91 N ANISOU 2198 NE2 GLN A1073 14435 20146 20480 -1753 -2362 -3712 N ATOM 2199 N LYS A1074 9.555 19.118 57.261 1.00120.18 N ANISOU 2199 N LYS A1074 13996 15542 16126 -546 -2577 -2381 N ATOM 2200 CA LYS A1074 10.416 20.302 57.216 1.00118.92 C ANISOU 2200 CA LYS A1074 14153 15192 15841 -273 -2778 -2288 C ATOM 2201 C LYS A1074 9.873 21.438 58.077 1.00125.50 C ANISOU 2201 C LYS A1074 14530 16275 16881 20 -2951 -2675 C ATOM 2202 O LYS A1074 10.036 22.616 57.748 1.00128.14 O ANISOU 2202 O LYS A1074 15061 16377 17250 310 -3393 -2770 O ATOM 2203 CB LYS A1074 10.648 20.774 55.778 1.00119.09 C ANISOU 2203 CB LYS A1074 14733 14733 15782 -170 -3287 -2192 C ATOM 2204 CG LYS A1074 11.362 19.746 54.925 1.00117.79 C ANISOU 2204 CG LYS A1074 15079 14320 15356 -426 -3079 -1824 C ATOM 2205 CD LYS A1074 12.016 20.376 53.710 1.00117.02 C ANISOU 2205 CD LYS A1074 15623 13800 15041 -353 -3445 -1644 C ATOM 2206 CE LYS A1074 12.877 19.364 52.970 1.00114.83 C ANISOU 2206 CE LYS A1074 15833 13332 14464 -586 -3138 -1303 C ATOM 2207 NZ LYS A1074 13.913 18.764 53.862 1.00110.17 N ANISOU 2207 NZ LYS A1074 15194 12930 13737 -686 -2530 -1030 N ATOM 2208 N ARG A1075 9.229 21.088 59.192 1.00129.87 N ANISOU 2208 N ARG A1075 14492 17298 17553 -66 -2602 -2907 N ATOM 2209 CA ARG A1075 8.782 22.060 60.188 1.00132.86 C ANISOU 2209 CA ARG A1075 14406 17992 18084 200 -2642 -3302 C ATOM 2210 C ARG A1075 9.839 22.098 61.289 1.00127.18 C ANISOU 2210 C ARG A1075 13798 17443 17082 121 -2181 -3044 C ATOM 2211 O ARG A1075 9.702 21.485 62.348 1.00127.02 O ANISOU 2211 O ARG A1075 13444 17835 16982 -95 -1693 -3056 O ATOM 2212 CB ARG A1075 7.401 21.688 60.728 1.00136.63 C ANISOU 2212 CB ARG A1075 14138 18936 18839 133 -2520 -3754 C ATOM 2213 CG ARG A1075 6.317 21.614 59.664 1.00140.10 C ANISOU 2213 CG ARG A1075 14410 19227 19594 201 -3009 -4023 C ATOM 2214 CD ARG A1075 5.997 22.991 59.113 1.00144.14 C ANISOU 2214 CD ARG A1075 14966 19462 20339 689 -3704 -4347 C ATOM 2215 NE ARG A1075 5.240 23.792 60.070 1.00150.23 N ANISOU 2215 NE ARG A1075 15086 20628 21367 993 -3725 -4896 N ATOM 2216 CZ ARG A1075 4.812 25.030 59.843 1.00154.92 C ANISOU 2216 CZ ARG A1075 15589 21045 22228 1474 -4321 -5288 C ATOM 2217 NH1 ARG A1075 5.065 25.626 58.686 1.00155.11 N ANISOU 2217 NH1 ARG A1075 16169 20491 22276 1666 -4968 -5151 N ATOM 2218 NH2 ARG A1075 4.128 25.674 60.779 1.00159.35 N ANISOU 2218 NH2 ARG A1075 15522 22002 23021 1761 -4278 -5830 N ATOM 2219 N TRP A1076 10.914 22.845 61.022 1.00123.08 N ANISOU 2219 N TRP A1076 13773 16597 16394 272 -2363 -2795 N ATOM 2220 CA TRP A1076 12.073 22.819 61.912 1.00121.62 C ANISOU 2220 CA TRP A1076 13766 16511 15932 173 -1976 -2481 C ATOM 2221 C TRP A1076 11.733 23.393 63.282 1.00123.53 C ANISOU 2221 C TRP A1076 13564 17170 16202 296 -1802 -2810 C ATOM 2222 O TRP A1076 12.054 22.796 64.316 1.00121.45 O ANISOU 2222 O TRP A1076 13168 17226 15752 74 -1315 -2670 O ATOM 2223 CB TRP A1076 13.241 23.593 61.296 1.00118.30 C ANISOU 2223 CB TRP A1076 13921 15674 15353 291 -2245 -2180 C ATOM 2224 CG TRP A1076 13.417 23.410 59.817 1.00114.01 C ANISOU 2224 CG TRP A1076 13826 14709 14785 246 -2543 -1979 C ATOM 2225 CD1 TRP A1076 13.357 24.382 58.862 1.00114.77 C ANISOU 2225 CD1 TRP A1076 14238 14434 14937 442 -3112 -2050 C ATOM 2226 CD2 TRP A1076 13.689 22.185 59.124 1.00110.27 C ANISOU 2226 CD2 TRP A1076 13578 14128 14193 -21 -2303 -1681 C ATOM 2227 NE1 TRP A1076 13.573 23.840 57.619 1.00113.90 N ANISOU 2227 NE1 TRP A1076 14537 14024 14716 290 -3214 -1810 N ATOM 2228 CE2 TRP A1076 13.778 22.493 57.752 1.00111.13 C ANISOU 2228 CE2 TRP A1076 14128 13831 14266 23 -2716 -1603 C ATOM 2229 CE3 TRP A1076 13.863 20.858 59.530 1.00108.03 C ANISOU 2229 CE3 TRP A1076 13201 14025 13819 -296 -1803 -1477 C ATOM 2230 CZ2 TRP A1076 14.034 21.524 56.785 1.00109.64 C ANISOU 2230 CZ2 TRP A1076 14268 13446 13946 -182 -2610 -1364 C ATOM 2231 CZ3 TRP A1076 14.113 19.898 58.568 1.00107.68 C ANISOU 2231 CZ3 TRP A1076 13483 13746 13683 -475 -1733 -1242 C ATOM 2232 CH2 TRP A1076 14.199 20.236 57.212 1.00107.61 C ANISOU 2232 CH2 TRP A1076 13890 13364 13631 -410 -2116 -1204 C ATOM 2233 N ASP A1077 11.089 24.562 63.308 1.00125.70 N ANISOU 2233 N ASP A1077 13634 17432 16696 657 -2217 -3262 N ATOM 2234 CA ASP A1077 10.789 25.215 64.578 1.00126.44 C ANISOU 2234 CA ASP A1077 13333 17907 16803 823 -2073 -3636 C ATOM 2235 C ASP A1077 9.824 24.386 65.419 1.00125.78 C ANISOU 2235 C ASP A1077 12634 18396 16762 610 -1605 -3903 C ATOM 2236 O ASP A1077 9.976 24.302 66.644 1.00129.05 O ANISOU 2236 O ASP A1077 12848 19203 16982 496 -1187 -3954 O ATOM 2237 CB ASP A1077 10.233 26.616 64.327 1.00130.97 C ANISOU 2237 CB ASP A1077 13821 18295 17647 1299 -2673 -4112 C ATOM 2238 CG ASP A1077 11.281 27.567 63.779 1.00129.67 C ANISOU 2238 CG ASP A1077 14287 17607 17375 1454 -3098 -3838 C ATOM 2239 OD1 ASP A1077 11.734 27.363 62.632 1.00129.07 O ANISOU 2239 OD1 ASP A1077 14666 17128 17248 1346 -3325 -3481 O ATOM 2240 OD2 ASP A1077 11.654 28.518 64.497 1.00130.51 O ANISOU 2240 OD2 ASP A1077 14445 17714 17427 1657 -3200 -3984 O ATOM 2241 N GLU A1078 8.824 23.769 64.785 1.00123.87 N ANISOU 2241 N GLU A1078 12097 18218 16751 517 -1673 -4069 N ATOM 2242 CA GLU A1078 7.952 22.856 65.516 1.00124.67 C ANISOU 2242 CA GLU A1078 11636 18864 16868 208 -1196 -4254 C ATOM 2243 C GLU A1078 8.712 21.618 65.967 1.00124.48 C ANISOU 2243 C GLU A1078 11873 18921 16503 -277 -661 -3714 C ATOM 2244 O GLU A1078 8.445 21.074 67.044 1.00125.27 O ANISOU 2244 O GLU A1078 11658 19495 16445 -561 -175 -3760 O ATOM 2245 CB GLU A1078 6.762 22.454 64.654 1.00124.88 C ANISOU 2245 CB GLU A1078 11311 18903 17235 184 -1438 -4520 C ATOM 2246 CG GLU A1078 6.011 23.617 64.066 1.00127.28 C ANISOU 2246 CG GLU A1078 11396 19048 17916 687 -2066 -5028 C ATOM 2247 CD GLU A1078 4.770 23.167 63.341 1.00131.83 C ANISOU 2247 CD GLU A1078 11537 19708 18846 641 -2294 -5320 C ATOM 2248 OE1 GLU A1078 4.380 21.992 63.504 1.00133.86 O ANISOU 2248 OE1 GLU A1078 11558 20250 19053 194 -1887 -5200 O ATOM 2249 OE2 GLU A1078 4.184 23.984 62.605 1.00135.51 O ANISOU 2249 OE2 GLU A1078 11912 19934 19643 1039 -2913 -5662 O ATOM 2250 N ALA A1079 9.655 21.151 65.149 1.00125.48 N ANISOU 2250 N ALA A1079 12583 18588 16504 -379 -752 -3207 N ATOM 2251 CA ALA A1079 10.484 20.022 65.554 1.00122.54 C ANISOU 2251 CA ALA A1079 12499 18224 15838 -767 -309 -2696 C ATOM 2252 C ALA A1079 11.382 20.405 66.721 1.00116.25 C ANISOU 2252 C ALA A1079 11815 17594 14760 -757 -53 -2547 C ATOM 2253 O ALA A1079 11.618 19.596 67.626 1.00116.98 O ANISOU 2253 O ALA A1079 11884 17943 14620 -1087 381 -2326 O ATOM 2254 CB ALA A1079 11.319 19.530 64.374 1.00122.41 C ANISOU 2254 CB ALA A1079 13055 17681 15773 -807 -480 -2257 C ATOM 2255 N ALA A1080 11.873 21.647 66.726 1.00109.54 N ANISOU 2255 N ALA A1080 11115 16585 13922 -399 -354 -2663 N ATOM 2256 CA ALA A1080 12.726 22.109 67.814 1.00104.89 C ANISOU 2256 CA ALA A1080 10644 16134 13074 -376 -173 -2548 C ATOM 2257 C ALA A1080 11.954 22.181 69.123 1.00112.95 C ANISOU 2257 C ALA A1080 11174 17732 14010 -459 157 -2927 C ATOM 2258 O ALA A1080 12.453 21.762 70.174 1.00114.12 O ANISOU 2258 O ALA A1080 11379 18127 13855 -706 531 -2716 O ATOM 2259 CB ALA A1080 13.330 23.469 67.467 1.00101.17 C ANISOU 2259 CB ALA A1080 10444 15338 12657 4 -622 -2620 C ATOM 2260 N VAL A1081 10.727 22.706 69.084 1.00116.72 N ANISOU 2260 N VAL A1081 11157 18447 14744 -260 24 -3503 N ATOM 2261 CA VAL A1081 9.975 22.858 70.325 1.00119.49 C ANISOU 2261 CA VAL A1081 10998 19400 15001 -320 371 -3934 C ATOM 2262 C VAL A1081 9.600 21.489 70.889 1.00122.46 C ANISOU 2262 C VAL A1081 11181 20163 15186 -868 911 -3736 C ATOM 2263 O VAL A1081 9.846 21.206 72.066 1.00128.68 O ANISOU 2263 O VAL A1081 11950 21310 15633 -1130 1323 -3647 O ATOM 2264 CB VAL A1081 8.749 23.777 70.126 1.00120.06 C ANISOU 2264 CB VAL A1081 10531 19647 15438 75 84 -4651 C ATOM 2265 CG1 VAL A1081 9.196 25.151 69.633 1.00115.12 C ANISOU 2265 CG1 VAL A1081 10195 18574 14972 597 -499 -4804 C ATOM 2266 CG2 VAL A1081 7.721 23.188 69.172 1.00123.06 C ANISOU 2266 CG2 VAL A1081 10593 20013 16151 0 -49 -4795 C ATOM 2267 N ASN A1082 9.068 20.593 70.051 1.00121.15 N ANISOU 2267 N ASN A1082 10940 19889 15203 -1084 892 -3620 N ATOM 2268 CA ASN A1082 8.659 19.285 70.559 1.00123.38 C ANISOU 2268 CA ASN A1082 11062 20501 15315 -1645 1366 -3429 C ATOM 2269 C ASN A1082 9.858 18.490 71.062 1.00121.13 C ANISOU 2269 C ASN A1082 11319 20052 14652 -1960 1618 -2793 C ATOM 2270 O ASN A1082 9.750 17.744 72.043 1.00123.94 O ANISOU 2270 O ASN A1082 11605 20767 14721 -2394 2049 -2652 O ATOM 2271 CB ASN A1082 7.903 18.502 69.486 1.00121.59 C ANISOU 2271 CB ASN A1082 10705 20120 15375 -1810 1227 -3419 C ATOM 2272 CG ASN A1082 7.226 17.251 70.035 1.00123.51 C ANISOU 2272 CG ASN A1082 10684 20756 15490 -2415 1686 -3325 C ATOM 2273 OD1 ASN A1082 6.206 17.334 70.722 1.00128.83 O ANISOU 2273 OD1 ASN A1082 10755 22007 16186 -2566 1952 -3753 O ATOM 2274 ND2 ASN A1082 7.787 16.086 69.726 1.00119.89 N ANISOU 2274 ND2 ASN A1082 10675 19982 14895 -2771 1776 -2777 N ATOM 2275 N LEU A1083 11.015 18.640 70.410 1.00117.13 N ANISOU 2275 N LEU A1083 11354 19012 14138 -1756 1344 -2406 N ATOM 2276 CA LEU A1083 12.230 18.003 70.910 1.00118.56 C ANISOU 2276 CA LEU A1083 12011 19032 14004 -1973 1530 -1843 C ATOM 2277 C LEU A1083 12.679 18.618 72.230 1.00126.32 C ANISOU 2277 C LEU A1083 12986 20328 14683 -1952 1711 -1898 C ATOM 2278 O LEU A1083 13.218 17.918 73.096 1.00127.92 O ANISOU 2278 O LEU A1083 13394 20645 14566 -2279 1993 -1545 O ATOM 2279 CB LEU A1083 13.350 18.112 69.877 1.00112.83 C ANISOU 2279 CB LEU A1083 11786 17718 13365 -1733 1207 -1482 C ATOM 2280 CG LEU A1083 13.391 17.054 68.778 1.00109.05 C ANISOU 2280 CG LEU A1083 11542 16873 13018 -1886 1145 -1196 C ATOM 2281 CD1 LEU A1083 14.666 17.182 67.959 1.00101.31 C ANISOU 2281 CD1 LEU A1083 11058 15395 12039 -1669 920 -837 C ATOM 2282 CD2 LEU A1083 13.283 15.674 69.391 1.00110.13 C ANISOU 2282 CD2 LEU A1083 11723 17147 12974 -2369 1508 -903 C ATOM 2283 N ALA A1084 12.477 19.928 72.395 1.00135.32 N ANISOU 2283 N ALA A1084 13929 21576 15911 -1566 1512 -2339 N ATOM 2284 CA ALA A1084 12.950 20.612 73.595 1.00139.19 C ANISOU 2284 CA ALA A1084 14459 22319 16107 -1509 1632 -2424 C ATOM 2285 C ALA A1084 12.197 20.163 74.835 1.00146.91 C ANISOU 2285 C ALA A1084 15098 23921 16801 -1878 2114 -2624 C ATOM 2286 O ALA A1084 12.754 20.182 75.940 1.00151.48 O ANISOU 2286 O ALA A1084 15848 24705 17001 -2039 2323 -2480 O ATOM 2287 CB ALA A1084 12.818 22.123 73.422 1.00139.15 C ANISOU 2287 CB ALA A1084 14336 22244 16291 -995 1266 -2897 C ATOM 2288 N LYS A1085 10.935 19.768 74.679 1.00148.39 N ANISOU 2288 N LYS A1085 14803 24433 17146 -2041 2294 -2958 N ATOM 2289 CA LYS A1085 10.131 19.287 75.798 1.00155.98 C ANISOU 2289 CA LYS A1085 15399 26042 17825 -2465 2800 -3160 C ATOM 2290 C LYS A1085 10.204 17.762 75.778 1.00150.80 C ANISOU 2290 C LYS A1085 14955 25328 17013 -3048 3053 -2623 C ATOM 2291 O LYS A1085 9.262 17.071 75.398 1.00156.92 O ANISOU 2291 O LYS A1085 15414 26259 17950 -3323 3185 -2725 O ATOM 2292 CB LYS A1085 8.688 19.805 75.711 1.00164.69 C ANISOU 2292 CB LYS A1085 15778 27593 19203 -2313 2861 -3888 C ATOM 2293 CG LYS A1085 8.440 20.978 74.747 1.00165.39 C ANISOU 2293 CG LYS A1085 15706 27377 19758 -1664 2334 -4319 C ATOM 2294 CD LYS A1085 9.158 22.262 75.154 1.00166.11 C ANISOU 2294 CD LYS A1085 16023 27327 19764 -1205 2085 -4493 C ATOM 2295 CE LYS A1085 8.892 23.383 74.159 1.00165.67 C ANISOU 2295 CE LYS A1085 15872 26907 20168 -599 1509 -4881 C ATOM 2296 NZ LYS A1085 10.143 24.094 73.770 1.00159.63 N ANISOU 2296 NZ LYS A1085 15710 25561 19380 -305 1087 -4556 N ATOM 2297 N SER A1086 11.348 17.231 76.205 1.00138.46 N ANISOU 2297 N SER A1086 13944 23519 15145 -3239 3089 -2047 N ATOM 2298 CA SER A1086 11.572 15.794 76.141 1.00132.66 C ANISOU 2298 CA SER A1086 13515 22606 14283 -3733 3238 -1497 C ATOM 2299 C SER A1086 12.431 15.360 77.317 1.00126.68 C ANISOU 2299 C SER A1086 13169 21924 13038 -4047 3433 -1065 C ATOM 2300 O SER A1086 13.074 16.178 77.982 1.00124.70 O ANISOU 2300 O SER A1086 13046 21748 12588 -3825 3379 -1119 O ATOM 2301 CB SER A1086 12.233 15.390 74.817 1.00127.52 C ANISOU 2301 CB SER A1086 13221 21283 13947 -3523 2875 -1144 C ATOM 2302 OG SER A1086 12.817 14.103 74.900 1.00126.28 O ANISOU 2302 OG SER A1086 13495 20858 13626 -3904 2960 -563 O ATOM 2303 N ARG A1087 12.428 14.050 77.569 1.00121.75 N ANISOU 2303 N ARG A1087 12780 21255 12223 -4581 3624 -627 N ATOM 2304 CA ARG A1087 13.282 13.494 78.611 1.00122.50 C ANISOU 2304 CA ARG A1087 13343 21334 11866 -4902 3734 -140 C ATOM 2305 C ARG A1087 14.740 13.460 78.175 1.00122.76 C ANISOU 2305 C ARG A1087 13891 20753 11998 -4570 3364 319 C ATOM 2306 O ARG A1087 15.640 13.561 79.015 1.00126.88 O ANISOU 2306 O ARG A1087 14738 21257 12213 -4594 3329 592 O ATOM 2307 CB ARG A1087 12.794 12.098 78.989 1.00125.72 C ANISOU 2307 CB ARG A1087 13880 21838 12051 -5592 4001 194 C ATOM 2308 CG ARG A1087 11.371 12.095 79.532 1.00136.66 C ANISOU 2308 CG ARG A1087 14720 23912 13291 -6007 4425 -247 C ATOM 2309 CD ARG A1087 10.731 10.719 79.503 1.00144.52 C ANISOU 2309 CD ARG A1087 15850 24751 14310 -6512 4482 30 C ATOM 2310 NE ARG A1087 9.311 10.804 79.836 1.00150.23 N ANISOU 2310 NE ARG A1087 16020 26007 15052 -6736 4756 -453 N ATOM 2311 CZ ARG A1087 8.494 9.760 79.917 1.00155.33 C ANISOU 2311 CZ ARG A1087 16651 26674 15694 -7213 4861 -337 C ATOM 2312 NH1 ARG A1087 7.216 9.938 80.226 1.00160.92 N ANISOU 2312 NH1 ARG A1087 16808 27911 16424 -7390 5115 -806 N ATOM 2313 NH2 ARG A1087 8.953 8.537 79.691 1.00156.01 N ANISOU 2313 NH2 ARG A1087 17270 26245 15761 -7503 4698 235 N ATOM 2314 N TRP A1088 14.990 13.319 76.872 1.00118.80 N ANISOU 2314 N TRP A1088 13459 19768 11913 -4269 3088 395 N ATOM 2315 CA TRP A1088 16.350 13.430 76.355 1.00110.92 C ANISOU 2315 CA TRP A1088 12856 18244 11044 -3906 2764 743 C ATOM 2316 C TRP A1088 16.903 14.831 76.583 1.00105.25 C ANISOU 2316 C TRP A1088 12068 17606 10315 -3477 2598 506 C ATOM 2317 O TRP A1088 18.062 15.002 76.981 1.00 97.29 O ANISOU 2317 O TRP A1088 11370 16420 9175 -3359 2452 809 O ATOM 2318 CB TRP A1088 16.367 13.073 74.868 1.00104.72 C ANISOU 2318 CB TRP A1088 12119 16996 10673 -3688 2550 787 C ATOM 2319 CG TRP A1088 17.539 13.626 74.110 1.00101.33 C ANISOU 2319 CG TRP A1088 11918 16143 10440 -3216 2237 928 C ATOM 2320 CD1 TRP A1088 18.858 13.351 74.323 1.00 97.67 C ANISOU 2320 CD1 TRP A1088 11826 15391 9892 -3129 2115 1358 C ATOM 2321 CD2 TRP A1088 17.493 14.533 73.000 1.00 98.70 C ANISOU 2321 CD2 TRP A1088 11450 15637 10416 -2796 2000 643 C ATOM 2322 NE1 TRP A1088 19.637 14.040 73.424 1.00 90.07 N ANISOU 2322 NE1 TRP A1088 10929 14132 9162 -2704 1864 1346 N ATOM 2323 CE2 TRP A1088 18.823 14.771 72.600 1.00 93.86 C ANISOU 2323 CE2 TRP A1088 11138 14663 9861 -2512 1787 928 C ATOM 2324 CE3 TRP A1088 16.457 15.171 72.310 1.00 99.24 C ANISOU 2324 CE3 TRP A1088 11173 15819 10714 -2642 1926 178 C ATOM 2325 CZ2 TRP A1088 19.143 15.617 71.540 1.00 97.15 C ANISOU 2325 CZ2 TRP A1088 11557 14841 10514 -2136 1533 786 C ATOM 2326 CZ3 TRP A1088 16.778 16.012 71.260 1.00 98.85 C ANISOU 2326 CZ3 TRP A1088 11164 15487 10909 -2236 1620 46 C ATOM 2327 CH2 TRP A1088 18.109 16.227 70.885 1.00 97.81 C ANISOU 2327 CH2 TRP A1088 11370 15007 10785 -2012 1442 359 C ATOM 2328 N TYR A1089 16.078 15.851 76.334 1.00107.58 N ANISOU 2328 N TYR A1089 11956 18151 10767 -3236 2585 -46 N ATOM 2329 CA TYR A1089 16.471 17.221 76.644 1.00104.94 C ANISOU 2329 CA TYR A1089 11564 17902 10406 -2859 2417 -322 C ATOM 2330 C TYR A1089 16.724 17.394 78.138 1.00107.11 C ANISOU 2330 C TYR A1089 11926 18552 10218 -3078 2613 -292 C ATOM 2331 O TYR A1089 17.678 18.070 78.537 1.00107.11 O ANISOU 2331 O TYR A1089 12148 18447 10103 -2876 2424 -189 O ATOM 2332 CB TYR A1089 15.389 18.188 76.157 1.00106.21 C ANISOU 2332 CB TYR A1089 11265 18261 10830 -2573 2351 -956 C ATOM 2333 CG TYR A1089 15.712 19.663 76.300 1.00108.84 C ANISOU 2333 CG TYR A1089 11561 18590 11203 -2135 2098 -1287 C ATOM 2334 CD1 TYR A1089 15.628 20.301 77.533 1.00113.25 C ANISOU 2334 CD1 TYR A1089 12031 19553 11444 -2161 2249 -1548 C ATOM 2335 CD2 TYR A1089 16.066 20.426 75.194 1.00107.42 C ANISOU 2335 CD2 TYR A1089 11462 17995 11359 -1719 1697 -1352 C ATOM 2336 CE1 TYR A1089 15.913 21.648 77.665 1.00111.84 C ANISOU 2336 CE1 TYR A1089 11854 19330 11310 -1761 1983 -1868 C ATOM 2337 CE2 TYR A1089 16.347 21.777 75.316 1.00108.54 C ANISOU 2337 CE2 TYR A1089 11614 18087 11541 -1351 1424 -1640 C ATOM 2338 CZ TYR A1089 16.269 22.381 76.555 1.00108.45 C ANISOU 2338 CZ TYR A1089 11517 18449 11239 -1361 1557 -1904 C ATOM 2339 OH TYR A1089 16.549 23.722 76.686 1.00107.14 O ANISOU 2339 OH TYR A1089 11397 18194 11117 -995 1253 -2204 O ATOM 2340 N ASN A1090 15.883 16.786 78.979 1.00111.89 N ANISOU 2340 N ASN A1090 12374 19609 10532 -3526 2990 -374 N ATOM 2341 CA ASN A1090 16.000 17.008 80.417 1.00115.54 C ANISOU 2341 CA ASN A1090 12918 20488 10494 -3763 3205 -406 C ATOM 2342 C ASN A1090 17.309 16.451 80.966 1.00115.43 C ANISOU 2342 C ASN A1090 13453 20189 10218 -3913 3066 219 C ATOM 2343 O ASN A1090 17.980 17.105 81.772 1.00115.46 O ANISOU 2343 O ASN A1090 13633 20281 9957 -3823 2974 230 O ATOM 2344 CB ASN A1090 14.804 16.397 81.145 1.00121.74 C ANISOU 2344 CB ASN A1090 13424 21839 10992 -4282 3674 -602 C ATOM 2345 CG ASN A1090 14.977 16.404 82.651 1.00130.14 C ANISOU 2345 CG ASN A1090 14673 23326 11447 -4636 3929 -541 C ATOM 2346 OD1 ASN A1090 14.988 15.355 83.293 1.00135.16 O ANISOU 2346 OD1 ASN A1090 15566 24061 11726 -5185 4138 -142 O ATOM 2347 ND2 ASN A1090 15.132 17.594 83.221 1.00131.06 N ANISOU 2347 ND2 ASN A1090 14708 23666 11423 -4333 3882 -929 N ATOM 2348 N GLN A1091 17.700 15.254 80.528 1.00116.44 N ANISOU 2348 N GLN A1091 13857 19952 10433 -4121 3012 728 N ATOM 2349 CA GLN A1091 18.900 14.624 81.069 1.00119.96 C ANISOU 2349 CA GLN A1091 14801 20118 10659 -4256 2852 1317 C ATOM 2350 C GLN A1091 20.172 15.217 80.472 1.00111.73 C ANISOU 2350 C GLN A1091 13927 18636 9890 -3770 2455 1485 C ATOM 2351 O GLN A1091 21.191 15.321 81.163 1.00108.02 O ANISOU 2351 O GLN A1091 13746 18083 9214 -3757 2285 1777 O ATOM 2352 CB GLN A1091 18.850 13.114 80.834 1.00129.74 C ANISOU 2352 CB GLN A1091 16290 21094 11913 -4630 2906 1774 C ATOM 2353 CG GLN A1091 19.836 12.321 81.678 1.00137.34 C ANISOU 2353 CG GLN A1091 17765 21857 12561 -4881 2777 2358 C ATOM 2354 CD GLN A1091 19.509 10.840 81.722 1.00143.47 C ANISOU 2354 CD GLN A1091 18797 22431 13284 -5325 2851 2727 C ATOM 2355 OE1 GLN A1091 18.386 10.431 81.426 1.00145.58 O ANISOU 2355 OE1 GLN A1091 18832 22849 13631 -5566 3080 2514 O ATOM 2356 NE2 GLN A1091 20.492 10.027 82.094 1.00145.61 N ANISOU 2356 NE2 GLN A1091 19529 22263 13533 -5326 2569 3219 N ATOM 2357 N THR A1092 20.143 15.604 79.197 1.00113.58 N ANISOU 2357 N THR A1092 13987 18595 10573 -3396 2296 1314 N ATOM 2358 CA THR A1092 21.297 16.205 78.523 1.00109.77 C ANISOU 2358 CA THR A1092 13630 17728 10350 -2976 1954 1451 C ATOM 2359 C THR A1092 20.859 17.462 77.779 1.00107.50 C ANISOU 2359 C THR A1092 13051 17468 10325 -2602 1836 961 C ATOM 2360 O THR A1092 20.750 17.461 76.548 1.00103.33 O ANISOU 2360 O THR A1092 12453 16662 10147 -2394 1721 907 O ATOM 2361 CB THR A1092 21.956 15.217 77.555 1.00101.58 C ANISOU 2361 CB THR A1092 12797 16206 9592 -2914 1829 1857 C ATOM 2362 OG1 THR A1092 21.052 14.912 76.485 1.00 99.60 O ANISOU 2362 OG1 THR A1092 12360 15868 9617 -2890 1912 1645 O ATOM 2363 CG2 THR A1092 22.339 13.919 78.261 1.00100.29 C ANISOU 2363 CG2 THR A1092 12952 15948 9205 -3263 1887 2336 C ATOM 2364 N PRO A1093 20.619 18.566 78.497 1.00106.34 N ANISOU 2364 N PRO A1093 12769 17628 10006 -2502 1828 594 N ATOM 2365 CA PRO A1093 20.141 19.778 77.806 1.00 98.68 C ANISOU 2365 CA PRO A1093 11551 16641 9301 -2130 1659 108 C ATOM 2366 C PRO A1093 21.175 20.425 76.899 1.00 90.19 C ANISOU 2366 C PRO A1093 10644 15128 8496 -1794 1290 267 C ATOM 2367 O PRO A1093 20.820 20.859 75.797 1.00 92.35 O ANISOU 2367 O PRO A1093 10804 15203 9081 -1557 1135 62 O ATOM 2368 CB PRO A1093 19.736 20.704 78.964 1.00103.92 C ANISOU 2368 CB PRO A1093 12087 17728 9669 -2122 1741 -303 C ATOM 2369 CG PRO A1093 20.502 20.204 80.143 1.00105.83 C ANISOU 2369 CG PRO A1093 12626 18090 9496 -2419 1828 77 C ATOM 2370 CD PRO A1093 20.581 18.716 79.962 1.00107.35 C ANISOU 2370 CD PRO A1093 12963 18152 9674 -2744 1987 546 C ATOM 2371 N ASN A1094 22.438 20.516 77.326 1.00 89.91 N ANISOU 2371 N ASN A1094 10873 14948 8341 -1790 1132 626 N ATOM 2372 CA ASN A1094 23.458 21.176 76.510 1.00 90.56 C ANISOU 2372 CA ASN A1094 11084 14668 8658 -1524 808 774 C ATOM 2373 C ASN A1094 23.582 20.522 75.141 1.00 89.12 C ANISOU 2373 C ASN A1094 10926 14151 8785 -1451 789 967 C ATOM 2374 O ASN A1094 23.635 21.206 74.113 1.00 89.01 O ANISOU 2374 O ASN A1094 10898 13915 9008 -1226 589 839 O ATOM 2375 CB ASN A1094 24.807 21.151 77.226 1.00 96.83 C ANISOU 2375 CB ASN A1094 12109 15396 9287 -1587 671 1171 C ATOM 2376 CG ASN A1094 25.011 22.346 78.125 1.00105.40 C ANISOU 2376 CG ASN A1094 13226 16651 10169 -1519 501 939 C ATOM 2377 OD1 ASN A1094 26.140 22.771 78.359 1.00110.34 O ANISOU 2377 OD1 ASN A1094 14007 17147 10771 -1478 262 1171 O ATOM 2378 ND2 ASN A1094 23.915 22.905 78.626 1.00108.36 N ANISOU 2378 ND2 ASN A1094 13438 17324 10408 -1502 617 453 N ATOM 2379 N ARG A1095 23.652 19.193 75.112 1.00 87.28 N ANISOU 2379 N ARG A1095 10773 13858 8533 -1650 977 1281 N ATOM 2380 CA ARG A1095 23.747 18.491 73.839 1.00 79.26 C ANISOU 2380 CA ARG A1095 9807 12525 7785 -1583 976 1435 C ATOM 2381 C ARG A1095 22.430 18.555 73.078 1.00 77.80 C ANISOU 2381 C ARG A1095 9425 12380 7756 -1554 1038 1061 C ATOM 2382 O ARG A1095 22.423 18.670 71.847 1.00 75.25 O ANISOU 2382 O ARG A1095 9127 11796 7669 -1391 915 1019 O ATOM 2383 CB ARG A1095 24.167 17.045 74.079 1.00 78.83 C ANISOU 2383 CB ARG A1095 9921 12357 7672 -1786 1119 1848 C ATOM 2384 CG ARG A1095 24.239 16.204 72.824 1.00 72.50 C ANISOU 2384 CG ARG A1095 9199 11225 7124 -1720 1137 1980 C ATOM 2385 CD ARG A1095 24.768 14.830 73.159 1.00 77.81 C ANISOU 2385 CD ARG A1095 10076 11737 7751 -1879 1218 2383 C ATOM 2386 NE ARG A1095 24.958 14.008 71.972 1.00 84.30 N ANISOU 2386 NE ARG A1095 11006 12213 8812 -1779 1224 2494 N ATOM 2387 CZ ARG A1095 25.511 12.803 71.993 1.00 91.32 C ANISOU 2387 CZ ARG A1095 12099 12859 9741 -1829 1241 2819 C ATOM 2388 NH1 ARG A1095 25.929 12.288 73.141 1.00 95.27 N ANISOU 2388 NH1 ARG A1095 12730 13412 10058 -1991 1224 3098 N ATOM 2389 NH2 ARG A1095 25.652 12.112 70.870 1.00 92.20 N ANISOU 2389 NH2 ARG A1095 12312 12654 10065 -1708 1250 2857 N ATOM 2390 N ALA A1096 21.305 18.484 73.792 1.00 81.13 N ANISOU 2390 N ALA A1096 9640 13144 8040 -1725 1226 778 N ATOM 2391 CA ALA A1096 20.012 18.617 73.132 1.00 81.10 C ANISOU 2391 CA ALA A1096 9377 13222 8216 -1686 1256 378 C ATOM 2392 C ALA A1096 19.869 19.995 72.503 1.00 86.10 C ANISOU 2392 C ALA A1096 9920 13761 9034 -1338 959 28 C ATOM 2393 O ALA A1096 19.440 20.120 71.351 1.00 86.71 O ANISOU 2393 O ALA A1096 9960 13627 9357 -1195 807 -109 O ATOM 2394 CB ALA A1096 18.881 18.350 74.123 1.00 81.19 C ANISOU 2394 CB ALA A1096 9123 13693 8034 -1951 1543 113 C ATOM 2395 N LYS A1097 20.247 21.042 73.242 1.00 88.11 N ANISOU 2395 N LYS A1097 10183 14136 9160 -1209 836 -108 N ATOM 2396 CA LYS A1097 20.214 22.398 72.701 1.00 91.69 C ANISOU 2396 CA LYS A1097 10623 14437 9779 -886 492 -408 C ATOM 2397 C LYS A1097 20.994 22.500 71.394 1.00 93.27 C ANISOU 2397 C LYS A1097 11068 14194 10176 -758 249 -145 C ATOM 2398 O LYS A1097 20.522 23.096 70.421 1.00 96.34 O ANISOU 2398 O LYS A1097 11442 14392 10771 -569 5 -370 O ATOM 2399 CB LYS A1097 20.769 23.390 73.725 1.00 94.22 C ANISOU 2399 CB LYS A1097 11012 14884 9904 -805 375 -498 C ATOM 2400 CG LYS A1097 19.846 23.697 74.894 1.00102.93 C ANISOU 2400 CG LYS A1097 11857 16436 10814 -844 560 -930 C ATOM 2401 CD LYS A1097 20.497 24.694 75.839 1.00104.05 C ANISOU 2401 CD LYS A1097 12138 16648 10748 -753 403 -1012 C ATOM 2402 CE LYS A1097 19.638 24.965 77.062 1.00108.75 C ANISOU 2402 CE LYS A1097 12502 17726 11092 -802 631 -1460 C ATOM 2403 NZ LYS A1097 20.264 25.988 77.946 1.00113.80 N ANISOU 2403 NZ LYS A1097 13317 18402 11521 -696 441 -1578 N ATOM 2404 N ARG A1098 22.200 21.926 71.352 1.00 89.08 N ANISOU 2404 N ARG A1098 10764 13507 9577 -860 305 325 N ATOM 2405 CA ARG A1098 23.009 22.031 70.141 1.00 83.98 C ANISOU 2405 CA ARG A1098 10328 12500 9082 -762 130 559 C ATOM 2406 C ARG A1098 22.401 21.231 68.997 1.00 86.36 C ANISOU 2406 C ARG A1098 10633 12636 9544 -781 199 549 C ATOM 2407 O ARG A1098 22.373 21.699 67.852 1.00 89.28 O ANISOU 2407 O ARG A1098 11114 12758 10049 -655 -14 484 O ATOM 2408 CB ARG A1098 24.440 21.573 70.412 1.00 81.21 C ANISOU 2408 CB ARG A1098 10144 12067 8644 -846 195 1019 C ATOM 2409 CG ARG A1098 25.254 22.546 71.245 1.00 83.52 C ANISOU 2409 CG ARG A1098 10487 12433 8814 -814 21 1064 C ATOM 2410 CD ARG A1098 26.726 22.163 71.259 1.00 79.57 C ANISOU 2410 CD ARG A1098 10110 11821 8303 -869 27 1511 C ATOM 2411 NE ARG A1098 26.957 20.875 71.904 1.00 74.19 N ANISOU 2411 NE ARG A1098 9421 11232 7536 -1008 263 1776 N ATOM 2412 CZ ARG A1098 27.158 20.724 73.208 1.00 76.98 C ANISOU 2412 CZ ARG A1098 9773 11791 7683 -1127 302 1867 C ATOM 2413 NH1 ARG A1098 27.367 19.518 73.717 1.00 79.53 N ANISOU 2413 NH1 ARG A1098 10146 12141 7929 -1267 468 2141 N ATOM 2414 NH2 ARG A1098 27.146 21.783 74.005 1.00 83.14 N ANISOU 2414 NH2 ARG A1098 10541 12730 8320 -1112 147 1682 N ATOM 2415 N VAL A1099 21.906 20.025 69.283 1.00 84.18 N ANISOU 2415 N VAL A1099 10273 12478 9235 -966 471 619 N ATOM 2416 CA VAL A1099 21.325 19.203 68.226 1.00 77.97 C ANISOU 2416 CA VAL A1099 9511 11519 8595 -1009 521 607 C ATOM 2417 C VAL A1099 20.039 19.831 67.699 1.00 83.01 C ANISOU 2417 C VAL A1099 9957 12201 9383 -902 347 163 C ATOM 2418 O VAL A1099 19.835 19.920 66.483 1.00 84.96 O ANISOU 2418 O VAL A1099 10314 12194 9773 -807 167 106 O ATOM 2419 CB VAL A1099 21.096 17.762 68.720 1.00 76.32 C ANISOU 2419 CB VAL A1099 9288 11396 8313 -1269 818 800 C ATOM 2420 CG1 VAL A1099 20.254 16.977 67.720 1.00 75.85 C ANISOU 2420 CG1 VAL A1099 9225 11187 8407 -1340 845 706 C ATOM 2421 CG2 VAL A1099 22.427 17.065 68.935 1.00 68.80 C ANISOU 2421 CG2 VAL A1099 8567 10288 7286 -1306 904 1248 C ATOM 2422 N ILE A1100 19.155 20.286 68.592 1.00 87.29 N ANISOU 2422 N ILE A1100 10206 13069 9890 -906 386 -178 N ATOM 2423 CA ILE A1100 17.915 20.897 68.118 1.00 91.52 C ANISOU 2423 CA ILE A1100 10497 13659 10617 -758 192 -643 C ATOM 2424 C ILE A1100 18.201 22.210 67.400 1.00 89.79 C ANISOU 2424 C ILE A1100 10435 13172 10509 -461 -231 -777 C ATOM 2425 O ILE A1100 17.487 22.576 66.459 1.00 93.66 O ANISOU 2425 O ILE A1100 10895 13497 11193 -317 -505 -1016 O ATOM 2426 CB ILE A1100 16.911 21.089 69.270 1.00100.21 C ANISOU 2426 CB ILE A1100 11196 15219 11660 -814 367 -1027 C ATOM 2427 CG1 ILE A1100 17.398 22.158 70.249 1.00108.95 C ANISOU 2427 CG1 ILE A1100 12310 16470 12615 -668 294 -1145 C ATOM 2428 CG2 ILE A1100 16.646 19.757 69.976 1.00 99.56 C ANISOU 2428 CG2 ILE A1100 11015 15393 11422 -1191 784 -841 C ATOM 2429 CD1 ILE A1100 16.421 22.456 71.363 1.00115.88 C ANISOU 2429 CD1 ILE A1100 12797 17825 13408 -689 478 -1589 C ATOM 2430 N THR A1101 19.241 22.938 67.816 1.00 89.68 N ANISOU 2430 N THR A1101 10613 13090 10373 -388 -329 -614 N ATOM 2431 CA THR A1101 19.634 24.131 67.074 1.00 90.15 C ANISOU 2431 CA THR A1101 10897 12842 10513 -175 -745 -663 C ATOM 2432 C THR A1101 20.167 23.758 65.697 1.00 91.23 C ANISOU 2432 C THR A1101 11339 12630 10696 -221 -835 -371 C ATOM 2433 O THR A1101 19.874 24.439 64.709 1.00 91.93 O ANISOU 2433 O THR A1101 11577 12459 10895 -89 -1187 -502 O ATOM 2434 CB THR A1101 20.673 24.937 67.861 1.00 86.49 C ANISOU 2434 CB THR A1101 10573 12391 9899 -148 -822 -528 C ATOM 2435 OG1 THR A1101 20.036 25.592 68.968 1.00 91.61 O ANISOU 2435 OG1 THR A1101 10983 13315 10509 -38 -843 -917 O ATOM 2436 CG2 THR A1101 21.350 25.982 66.974 1.00 77.09 C ANISOU 2436 CG2 THR A1101 9704 10830 8756 -36 -1224 -432 C ATOM 2437 N THR A1102 20.935 22.669 65.611 1.00 89.56 N ANISOU 2437 N THR A1102 11237 12401 10391 -402 -533 10 N ATOM 2438 CA THR A1102 21.436 22.206 64.319 1.00 86.94 C ANISOU 2438 CA THR A1102 11179 11777 10076 -445 -553 248 C ATOM 2439 C THR A1102 20.291 21.827 63.386 1.00 89.95 C ANISOU 2439 C THR A1102 11530 12053 10594 -428 -659 21 C ATOM 2440 O THR A1102 20.294 22.185 62.202 1.00 91.99 O ANISOU 2440 O THR A1102 12031 12038 10882 -374 -911 17 O ATOM 2441 CB THR A1102 22.380 21.020 64.520 1.00 84.98 C ANISOU 2441 CB THR A1102 11001 11550 9736 -595 -199 630 C ATOM 2442 OG1 THR A1102 23.564 21.462 65.194 1.00 90.24 O ANISOU 2442 OG1 THR A1102 11716 12272 10299 -599 -176 862 O ATOM 2443 CG2 THR A1102 22.756 20.400 63.180 1.00 75.94 C ANISOU 2443 CG2 THR A1102 10109 10139 8607 -623 -166 800 C ATOM 2444 N PHE A1103 19.308 21.085 63.901 1.00 90.48 N ANISOU 2444 N PHE A1103 11310 12340 10728 -510 -477 -159 N ATOM 2445 CA PHE A1103 18.108 20.787 63.127 1.00 87.34 C ANISOU 2445 CA PHE A1103 10811 11883 10491 -505 -614 -420 C ATOM 2446 C PHE A1103 17.456 22.069 62.626 1.00 92.82 C ANISOU 2446 C PHE A1103 11484 12460 11323 -269 -1079 -760 C ATOM 2447 O PHE A1103 17.284 22.272 61.418 1.00100.87 O ANISOU 2447 O PHE A1103 12738 13188 12399 -211 -1373 -780 O ATOM 2448 CB PHE A1103 17.115 20.000 63.985 1.00 86.69 C ANISOU 2448 CB PHE A1103 10346 12135 10459 -660 -350 -600 C ATOM 2449 CG PHE A1103 17.383 18.523 64.044 1.00 85.13 C ANISOU 2449 CG PHE A1103 10236 11926 10183 -921 -8 -300 C ATOM 2450 CD1 PHE A1103 17.666 17.802 62.896 1.00 82.36 C ANISOU 2450 CD1 PHE A1103 10182 11260 9851 -968 -34 -117 C ATOM 2451 CD2 PHE A1103 17.336 17.854 65.254 1.00 88.35 C ANISOU 2451 CD2 PHE A1103 10465 12622 10483 -1127 322 -211 C ATOM 2452 CE1 PHE A1103 17.901 16.438 62.959 1.00 80.59 C ANISOU 2452 CE1 PHE A1103 10065 10978 9576 -1178 243 131 C ATOM 2453 CE2 PHE A1103 17.571 16.495 65.323 1.00 89.39 C ANISOU 2453 CE2 PHE A1103 10726 12687 10552 -1369 579 76 C ATOM 2454 CZ PHE A1103 17.855 15.786 64.174 1.00 86.37 C ANISOU 2454 CZ PHE A1103 10631 11958 10227 -1376 529 237 C ATOM 2455 N ARG A1104 17.093 22.951 63.559 1.00 98.52 N ANISOU 2455 N ARG A1104 11952 13393 12088 -122 -1172 -1041 N ATOM 2456 CA ARG A1104 16.382 24.176 63.213 1.00107.04 C ANISOU 2456 CA ARG A1104 12977 14352 13340 151 -1652 -1422 C ATOM 2457 C ARG A1104 17.191 25.032 62.249 1.00105.44 C ANISOU 2457 C ARG A1104 13252 13731 13078 235 -2032 -1223 C ATOM 2458 O ARG A1104 16.663 25.544 61.256 1.00103.90 O ANISOU 2458 O ARG A1104 13211 13265 13003 361 -2462 -1374 O ATOM 2459 CB ARG A1104 16.064 24.962 64.485 1.00111.83 C ANISOU 2459 CB ARG A1104 13270 15254 13968 307 -1644 -1749 C ATOM 2460 CG ARG A1104 15.343 26.274 64.250 1.00119.10 C ANISOU 2460 CG ARG A1104 14122 16033 15097 649 -2169 -2191 C ATOM 2461 CD ARG A1104 15.229 27.063 65.542 1.00124.00 C ANISOU 2461 CD ARG A1104 14495 16926 15695 815 -2132 -2506 C ATOM 2462 NE ARG A1104 16.540 27.383 66.098 1.00122.52 N ANISOU 2462 NE ARG A1104 14613 16677 15263 720 -2034 -2164 N ATOM 2463 CZ ARG A1104 17.311 28.375 65.665 1.00122.11 C ANISOU 2463 CZ ARG A1104 14957 16259 15181 819 -2422 -2023 C ATOM 2464 NH1 ARG A1104 18.491 28.597 66.227 1.00118.49 N ANISOU 2464 NH1 ARG A1104 14717 15791 14514 696 -2312 -1715 N ATOM 2465 NH2 ARG A1104 16.903 29.144 64.664 1.00124.50 N ANISOU 2465 NH2 ARG A1104 15451 16195 15659 1016 -2947 -2178 N ATOM 2466 N THR A1105 18.485 25.191 62.522 1.00101.17 N ANISOU 2466 N THR A1105 12958 13139 12342 138 -1894 -872 N ATOM 2467 CA THR A1105 19.289 26.099 61.714 1.00100.10 C ANISOU 2467 CA THR A1105 13255 12653 12124 160 -2234 -680 C ATOM 2468 C THR A1105 19.605 25.499 60.350 1.00 96.46 C ANISOU 2468 C THR A1105 13128 11943 11580 13 -2228 -421 C ATOM 2469 O THR A1105 19.491 26.180 59.323 1.00104.28 O ANISOU 2469 O THR A1105 14437 12619 12564 54 -2639 -440 O ATOM 2470 CB THR A1105 20.577 26.456 62.454 1.00102.22 C ANISOU 2470 CB THR A1105 13630 12984 12224 72 -2081 -397 C ATOM 2471 OG1 THR A1105 20.255 27.102 63.693 1.00103.87 O ANISOU 2471 OG1 THR A1105 13585 13404 12478 215 -2129 -672 O ATOM 2472 CG2 THR A1105 21.442 27.381 61.609 1.00103.89 C ANISOU 2472 CG2 THR A1105 14282 12858 12335 21 -2408 -174 C ATOM 2473 N GLY A1106 19.995 24.226 60.318 1.00 93.47 N ANISOU 2473 N GLY A1106 12712 11681 11121 -160 -1785 -189 N ATOM 2474 CA GLY A1106 20.492 23.608 59.107 1.00 87.84 C ANISOU 2474 CA GLY A1106 12331 10757 10287 -297 -1708 59 C ATOM 2475 C GLY A1106 21.955 23.855 58.809 1.00 94.65 C ANISOU 2475 C GLY A1106 13484 11530 10948 -416 -1592 423 C ATOM 2476 O GLY A1106 22.426 23.452 57.739 1.00 92.94 O ANISOU 2476 O GLY A1106 13559 11155 10598 -530 -1518 602 O ATOM 2477 N THR A1107 22.684 24.516 59.702 1.00103.15 N ANISOU 2477 N THR A1107 14482 12718 11992 -406 -1573 521 N ATOM 2478 CA THR A1107 24.117 24.757 59.559 1.00101.00 C ANISOU 2478 CA THR A1107 14399 12420 11558 -544 -1447 865 C ATOM 2479 C THR A1107 24.851 24.166 60.759 1.00 98.37 C ANISOU 2479 C THR A1107 13791 12358 11229 -568 -1079 1028 C ATOM 2480 O THR A1107 24.251 23.550 61.640 1.00104.04 O ANISOU 2480 O THR A1107 14233 13265 12032 -510 -916 899 O ATOM 2481 CB THR A1107 24.432 26.254 59.419 1.00101.72 C ANISOU 2481 CB THR A1107 14721 12333 11594 -555 -1869 870 C ATOM 2482 OG1 THR A1107 24.443 26.870 60.714 1.00103.08 O ANISOU 2482 OG1 THR A1107 14670 12655 11841 -458 -1947 760 O ATOM 2483 CG2 THR A1107 23.409 26.950 58.534 1.00102.20 C ANISOU 2483 CG2 THR A1107 15018 12111 11703 -467 -2355 632 C ATOM 2484 N TRP A1108 26.167 24.377 60.793 1.00 91.13 N ANISOU 2484 N TRP A1108 12951 11465 10208 -679 -967 1320 N ATOM 2485 CA TRP A1108 27.028 23.828 61.830 1.00 80.49 C ANISOU 2485 CA TRP A1108 11375 10343 8865 -704 -671 1517 C ATOM 2486 C TRP A1108 27.386 24.847 62.904 1.00 89.25 C ANISOU 2486 C TRP A1108 12397 11550 9965 -699 -864 1511 C ATOM 2487 O TRP A1108 28.409 24.684 63.575 1.00 94.23 O ANISOU 2487 O TRP A1108 12915 12323 10567 -762 -711 1739 O ATOM 2488 CB TRP A1108 28.310 23.268 61.215 1.00 76.22 C ANISOU 2488 CB TRP A1108 10903 9804 8254 -810 -399 1826 C ATOM 2489 CG TRP A1108 28.087 22.115 60.303 1.00 82.21 C ANISOU 2489 CG TRP A1108 11745 10481 9011 -795 -159 1825 C ATOM 2490 CD1 TRP A1108 27.864 22.167 58.960 1.00 82.20 C ANISOU 2490 CD1 TRP A1108 12021 10295 8915 -849 -220 1777 C ATOM 2491 CD2 TRP A1108 28.074 20.729 60.661 1.00 87.56 C ANISOU 2491 CD2 TRP A1108 12273 11230 9766 -734 153 1872 C ATOM 2492 NE1 TRP A1108 27.711 20.898 58.457 1.00 85.30 N ANISOU 2492 NE1 TRP A1108 12436 10651 9325 -812 48 1767 N ATOM 2493 CE2 TRP A1108 27.835 19.997 59.482 1.00 87.76 C ANISOU 2493 CE2 TRP A1108 12489 11099 9755 -737 270 1826 C ATOM 2494 CE3 TRP A1108 28.241 20.035 61.864 1.00 88.31 C ANISOU 2494 CE3 TRP A1108 12135 11481 9937 -692 315 1957 C ATOM 2495 CZ2 TRP A1108 27.758 18.607 59.470 1.00 89.76 C ANISOU 2495 CZ2 TRP A1108 12704 11326 10076 -684 533 1847 C ATOM 2496 CZ3 TRP A1108 28.164 18.655 61.849 1.00 89.45 C ANISOU 2496 CZ3 TRP A1108 12254 11591 10142 -656 563 2007 C ATOM 2497 CH2 TRP A1108 27.926 17.957 60.659 1.00 90.38 C ANISOU 2497 CH2 TRP A1108 12560 11529 10250 -644 666 1945 C ATOM 2498 N ASP A1109 26.563 25.884 63.088 1.00 92.56 N ANISOU 2498 N ASP A1109 12866 11885 10416 -608 -1224 1237 N ATOM 2499 CA ASP A1109 26.917 26.966 64.005 1.00 95.64 C ANISOU 2499 CA ASP A1109 13242 12315 10783 -598 -1459 1200 C ATOM 2500 C ASP A1109 27.196 26.452 65.412 1.00 96.24 C ANISOU 2500 C ASP A1109 13050 12680 10837 -591 -1219 1245 C ATOM 2501 O ASP A1109 28.153 26.888 66.062 1.00 95.84 O ANISOU 2501 O ASP A1109 12992 12697 10725 -673 -1262 1421 O ATOM 2502 CB ASP A1109 25.803 28.008 64.037 1.00100.97 C ANISOU 2502 CB ASP A1109 13984 12847 11532 -430 -1877 815 C ATOM 2503 CG ASP A1109 25.734 28.816 62.767 1.00105.70 C ANISOU 2503 CG ASP A1109 14939 13102 12122 -466 -2248 823 C ATOM 2504 OD1 ASP A1109 26.774 28.949 62.087 1.00106.40 O ANISOU 2504 OD1 ASP A1109 15245 13088 12093 -677 -2218 1147 O ATOM 2505 OD2 ASP A1109 24.639 29.324 62.450 1.00109.11 O ANISOU 2505 OD2 ASP A1109 15429 13372 12656 -294 -2579 503 O ATOM 2506 N ALA A1110 26.374 25.522 65.898 1.00 94.76 N ANISOU 2506 N ALA A1110 12658 12664 10683 -527 -984 1103 N ATOM 2507 CA ALA A1110 26.514 25.059 67.271 1.00 89.23 C ANISOU 2507 CA ALA A1110 11755 12234 9913 -554 -785 1138 C ATOM 2508 C ALA A1110 27.758 24.208 67.480 1.00 87.88 C ANISOU 2508 C ALA A1110 11562 12127 9702 -670 -539 1543 C ATOM 2509 O ALA A1110 28.167 24.012 68.630 1.00 90.04 O ANISOU 2509 O ALA A1110 11733 12584 9893 -715 -463 1644 O ATOM 2510 CB ALA A1110 25.271 24.277 67.690 1.00 87.61 C ANISOU 2510 CB ALA A1110 11354 12203 9730 -519 -592 893 C ATOM 2511 N TYR A1111 28.376 23.712 66.405 1.00 82.60 N ANISOU 2511 N TYR A1111 10987 11314 9083 -708 -428 1758 N ATOM 2512 CA TYR A1111 29.504 22.804 66.522 1.00 81.20 C ANISOU 2512 CA TYR A1111 10742 11192 8917 -761 -189 2091 C ATOM 2513 C TYR A1111 30.761 23.268 65.805 1.00 86.28 C ANISOU 2513 C TYR A1111 11452 11759 9571 -832 -230 2320 C ATOM 2514 O TYR A1111 31.805 22.626 65.958 1.00 94.06 O ANISOU 2514 O TYR A1111 12322 12819 10599 -847 -58 2574 O ATOM 2515 CB TYR A1111 29.127 21.413 65.990 1.00 78.99 C ANISOU 2515 CB TYR A1111 10457 10856 8698 -730 86 2124 C ATOM 2516 CG TYR A1111 28.021 20.732 66.761 1.00 77.44 C ANISOU 2516 CG TYR A1111 10168 10771 8485 -735 186 1967 C ATOM 2517 CD1 TYR A1111 28.275 20.131 67.987 1.00 74.84 C ANISOU 2517 CD1 TYR A1111 9739 10604 8094 -789 297 2110 C ATOM 2518 CD2 TYR A1111 26.724 20.681 66.262 1.00 73.82 C ANISOU 2518 CD2 TYR A1111 9722 10263 8062 -715 158 1684 C ATOM 2519 CE1 TYR A1111 27.271 19.505 68.695 1.00 74.70 C ANISOU 2519 CE1 TYR A1111 9653 10713 8017 -862 415 1986 C ATOM 2520 CE2 TYR A1111 25.716 20.056 66.965 1.00 69.39 C ANISOU 2520 CE2 TYR A1111 9034 9848 7484 -770 278 1538 C ATOM 2521 CZ TYR A1111 25.996 19.470 68.178 1.00 73.52 C ANISOU 2521 CZ TYR A1111 9476 10547 7912 -863 425 1696 C ATOM 2522 OH TYR A1111 24.999 18.845 68.886 1.00 76.72 O ANISOU 2522 OH TYR A1111 9772 11122 8256 -984 570 1571 O ATOM 2523 N LEU A 311 30.706 24.347 65.033 1.00 84.12 N ANISOU 2523 N LEU A 311 11354 11345 9264 -887 -462 2241 N ATOM 2524 CA LEU A 311 31.833 24.744 64.198 1.00 78.08 C ANISOU 2524 CA LEU A 311 10668 10526 8474 -1024 -458 2462 C ATOM 2525 C LEU A 311 32.756 25.657 64.997 1.00 76.18 C ANISOU 2525 C LEU A 311 10359 10375 8211 -1140 -653 2603 C ATOM 2526 O LEU A 311 32.318 26.691 65.513 1.00 77.91 O ANISOU 2526 O LEU A 311 10679 10535 8389 -1147 -970 2449 O ATOM 2527 CB LEU A 311 31.346 25.439 62.927 1.00 77.27 C ANISOU 2527 CB LEU A 311 10855 10202 8302 -1091 -637 2351 C ATOM 2528 CG LEU A 311 32.005 25.057 61.600 1.00 72.68 C ANISOU 2528 CG LEU A 311 10389 9570 7656 -1206 -424 2509 C ATOM 2529 CD1 LEU A 311 32.065 23.549 61.432 1.00 65.83 C ANISOU 2529 CD1 LEU A 311 9375 8778 6858 -1080 -35 2541 C ATOM 2530 CD2 LEU A 311 31.224 25.687 60.463 1.00 68.59 C ANISOU 2530 CD2 LEU A 311 10219 8808 7034 -1266 -660 2367 C ATOM 2531 N ASN A 312 34.026 25.273 65.103 1.00 65.82 N ANISOU 2531 N ASN A 312 8866 9201 6943 -1216 -483 2873 N ATOM 2532 CA ASN A 312 34.996 26.093 65.810 1.00 67.08 C ANISOU 2532 CA ASN A 312 8936 9455 7097 -1360 -679 3031 C ATOM 2533 C ASN A 312 35.435 27.266 64.928 1.00 74.89 C ANISOU 2533 C ASN A 312 10122 10322 8012 -1597 -879 3095 C ATOM 2534 O ASN A 312 35.007 27.412 63.779 1.00 82.52 O ANISOU 2534 O ASN A 312 11308 11133 8911 -1645 -864 3029 O ATOM 2535 CB ASN A 312 36.173 25.231 66.285 1.00 67.94 C ANISOU 2535 CB ASN A 312 8734 9766 7315 -1342 -462 3284 C ATOM 2536 CG ASN A 312 37.008 24.661 65.148 1.00 69.02 C ANISOU 2536 CG ASN A 312 8760 9947 7516 -1383 -166 3430 C ATOM 2537 OD1 ASN A 312 36.873 25.060 63.997 1.00 85.60 O ANISOU 2537 OD1 ASN A 312 11044 11948 9531 -1499 -129 3387 O ATOM 2538 ND2 ASN A 312 37.893 23.721 65.480 1.00 73.81 N ANISOU 2538 ND2 ASN A 312 9072 10707 8267 -1281 37 3591 N ATOM 2539 N ASP A 313 36.303 28.120 65.475 1.00101.11 N ANISOU 2539 N ASP A 313 16739 15410 6269 -3457 -379 1231 N ATOM 2540 CA ASP A 313 36.752 29.287 64.721 1.00107.82 C ANISOU 2540 CA ASP A 313 17467 16076 7425 -3371 -579 938 C ATOM 2541 C ASP A 313 37.577 28.876 63.513 1.00107.37 C ANISOU 2541 C ASP A 313 17112 15751 7931 -3312 -757 1172 C ATOM 2542 O ASP A 313 37.461 29.475 62.436 1.00 91.62 O ANISOU 2542 O ASP A 313 14901 13576 6333 -3207 -716 979 O ATOM 2543 CB ASP A 313 37.552 30.220 65.624 1.00101.93 C ANISOU 2543 CB ASP A 313 16979 15412 6339 -3437 -952 782 C ATOM 2544 CG ASP A 313 36.680 30.912 66.640 1.00110.41 C ANISOU 2544 CG ASP A 313 18355 16711 6885 -3449 -750 434 C ATOM 2545 OD1 ASP A 313 35.570 31.340 66.268 1.00112.65 O ANISOU 2545 OD1 ASP A 313 18562 16996 7243 -3349 -381 147 O ATOM 2546 OD2 ASP A 313 37.082 31.012 67.817 1.00118.65 O ANISOU 2546 OD2 ASP A 313 19715 17935 7430 -3551 -949 454 O ATOM 2547 N HIS A 314 38.407 27.847 63.676 1.00115.66 N ANISOU 2547 N HIS A 314 18150 16776 9020 -3368 -941 1600 N ATOM 2548 CA HIS A 314 39.218 27.348 62.571 1.00110.09 C ANISOU 2548 CA HIS A 314 17177 15820 8832 -3291 -1077 1853 C ATOM 2549 C HIS A 314 38.348 26.842 61.424 1.00104.36 C ANISOU 2549 C HIS A 314 16236 14947 8469 -3197 -724 1817 C ATOM 2550 O HIS A 314 38.629 27.123 60.252 1.00107.53 O ANISOU 2550 O HIS A 314 16414 15141 9303 -3087 -756 1760 O ATOM 2551 CB HIS A 314 40.146 26.245 63.076 1.00123.13 C ANISOU 2551 CB HIS A 314 18873 17484 10428 -3358 -1291 2334 C ATOM 2552 CG HIS A 314 40.870 25.516 61.990 1.00128.24 C ANISOU 2552 CG HIS A 314 19263 17877 11587 -3256 -1353 2630 C ATOM 2553 ND1 HIS A 314 41.115 24.160 62.043 1.00131.01 N ANISOU 2553 ND1 HIS A 314 19594 18172 12010 -3267 -1309 3042 N ATOM 2554 CD2 HIS A 314 41.406 25.952 60.826 1.00127.19 C ANISOU 2554 CD2 HIS A 314 18890 17526 11912 -3129 -1441 2576 C ATOM 2555 CE1 HIS A 314 41.768 23.792 60.956 1.00129.09 C ANISOU 2555 CE1 HIS A 314 19124 17682 12243 -3139 -1358 3211 C ATOM 2556 NE2 HIS A 314 41.957 24.860 60.201 1.00126.05 N ANISOU 2556 NE2 HIS A 314 18599 17206 12088 -3054 -1433 2940 N ATOM 2557 N LEU A 315 37.288 26.094 61.738 1.00 94.64 N ANISOU 2557 N LEU A 315 15070 13824 7064 -3247 -392 1862 N ATOM 2558 CA LEU A 315 36.422 25.568 60.687 1.00 87.34 C ANISOU 2558 CA LEU A 315 13954 12759 6473 -3188 -83 1839 C ATOM 2559 C LEU A 315 35.465 26.620 60.147 1.00 91.64 C ANISOU 2559 C LEU A 315 14404 13308 7107 -3120 121 1416 C ATOM 2560 O LEU A 315 35.053 26.531 58.985 1.00 82.09 O ANISOU 2560 O LEU A 315 12989 11930 6273 -3045 259 1351 O ATOM 2561 CB LEU A 315 35.630 24.363 61.193 1.00 88.68 C ANISOU 2561 CB LEU A 315 14201 13025 6468 -3284 180 2071 C ATOM 2562 CG LEU A 315 36.457 23.129 61.553 1.00 95.09 C ANISOU 2562 CG LEU A 315 15071 13785 7275 -3339 24 2533 C ATOM 2563 CD1 LEU A 315 35.559 21.937 61.846 1.00 91.57 C ANISOU 2563 CD1 LEU A 315 14663 13383 6745 -3431 311 2755 C ATOM 2564 CD2 LEU A 315 37.443 22.809 60.441 1.00 91.34 C ANISOU 2564 CD2 LEU A 315 14411 13020 7273 -3226 -163 2694 C ATOM 2565 N LYS A 316 35.091 27.612 60.960 1.00 91.44 N ANISOU 2565 N LYS A 316 14534 13466 6742 -3140 144 1127 N ATOM 2566 CA LYS A 316 34.285 28.703 60.426 1.00 92.02 C ANISOU 2566 CA LYS A 316 14506 13519 6940 -3054 313 729 C ATOM 2567 C LYS A 316 35.096 29.557 59.460 1.00 92.14 C ANISOU 2567 C LYS A 316 14357 13323 7328 -2956 57 604 C ATOM 2568 O LYS A 316 34.533 30.156 58.538 1.00 80.55 O ANISOU 2568 O LYS A 316 12708 11752 6145 -2866 190 379 O ATOM 2569 CB LYS A 316 33.716 29.559 61.561 1.00 93.22 C ANISOU 2569 CB LYS A 316 14888 13900 6631 -3078 414 443 C ATOM 2570 CG LYS A 316 32.354 30.171 61.228 1.00 98.05 C ANISOU 2570 CG LYS A 316 15396 14554 7304 -3002 781 126 C ATOM 2571 CD LYS A 316 32.060 31.431 62.035 1.00108.41 C ANISOU 2571 CD LYS A 316 16906 15999 8285 -2960 809 -254 C ATOM 2572 CE LYS A 316 31.727 31.119 63.484 1.00119.66 C ANISOU 2572 CE LYS A 316 18634 17704 9126 -3039 942 -210 C ATOM 2573 NZ LYS A 316 31.201 32.321 64.194 1.00127.34 N ANISOU 2573 NZ LYS A 316 19805 18802 9778 -2968 1064 -621 N ATOM 2574 N GLN A 317 36.417 29.613 59.653 1.00 92.42 N ANISOU 2574 N GLN A 317 14437 13299 7379 -2974 -312 773 N ATOM 2575 CA GLN A 317 37.289 30.314 58.716 1.00 93.28 C ANISOU 2575 CA GLN A 317 14363 13207 7874 -2886 -562 729 C ATOM 2576 C GLN A 317 37.354 29.593 57.372 1.00 90.14 C ANISOU 2576 C GLN A 317 13713 12608 7929 -2795 -465 910 C ATOM 2577 O GLN A 317 37.269 30.231 56.316 1.00 90.99 O ANISOU 2577 O GLN A 317 13629 12575 8367 -2695 -444 750 O ATOM 2578 CB GLN A 317 38.686 30.466 59.325 1.00108.22 C ANISOU 2578 CB GLN A 317 16348 15099 9672 -2944 -985 916 C ATOM 2579 CG GLN A 317 39.807 30.650 58.316 1.00118.02 C ANISOU 2579 CG GLN A 317 17353 16124 11366 -2859 -1239 1074 C ATOM 2580 CD GLN A 317 41.187 30.531 58.946 1.00127.91 C ANISOU 2580 CD GLN A 317 18664 17386 12550 -2929 -1647 1360 C ATOM 2581 OE1 GLN A 317 42.094 31.301 58.633 1.00136.13 O ANISOU 2581 OE1 GLN A 317 19594 18322 13809 -2907 -1943 1359 O ATOM 2582 NE2 GLN A 317 41.350 29.555 59.834 1.00123.15 N ANISOU 2582 NE2 GLN A 317 18222 16909 11661 -3021 -1674 1631 N ATOM 2583 N ARG A 318 37.486 28.264 57.388 1.00 87.83 N ANISOU 2583 N ARG A 318 13432 12292 7649 -2827 -401 1242 N ATOM 2584 CA ARG A 318 37.612 27.512 56.142 1.00 87.43 C ANISOU 2584 CA ARG A 318 13188 12031 8001 -2736 -319 1411 C ATOM 2585 C ARG A 318 36.322 27.507 55.328 1.00 82.88 C ANISOU 2585 C ARG A 318 12501 11414 7574 -2704 3 1201 C ATOM 2586 O ARG A 318 36.378 27.427 54.096 1.00 81.88 O ANISOU 2586 O ARG A 318 12201 11107 7801 -2606 39 1200 O ATOM 2587 CB ARG A 318 38.056 26.079 56.432 1.00 75.95 C ANISOU 2587 CB ARG A 318 11800 10540 6518 -2777 -333 1811 C ATOM 2588 CG ARG A 318 39.562 25.924 56.624 1.00 84.94 C ANISOU 2588 CG ARG A 318 12926 11613 7734 -2747 -670 2104 C ATOM 2589 CD ARG A 318 40.065 24.641 55.986 1.00 84.64 C ANISOU 2589 CD ARG A 318 12811 11384 7965 -2673 -636 2454 C ATOM 2590 NE ARG A 318 40.089 23.532 56.931 1.00 95.06 N ANISOU 2590 NE ARG A 318 14289 12780 9050 -2776 -622 2752 N ATOM 2591 CZ ARG A 318 41.176 23.135 57.582 1.00 99.09 C ANISOU 2591 CZ ARG A 318 14846 13309 9496 -2795 -877 3079 C ATOM 2592 NH1 ARG A 318 42.331 23.758 57.386 1.00105.72 N ANISOU 2592 NH1 ARG A 318 15573 14095 10500 -2724 -1167 3150 N ATOM 2593 NH2 ARG A 318 41.110 22.113 58.423 1.00 93.12 N ANISOU 2593 NH2 ARG A 318 14232 12623 8527 -2890 -849 3357 N ATOM 2594 N ARG A 319 35.156 27.586 55.977 1.00 86.93 N ANISOU 2594 N ARG A 319 13107 12098 7826 -2784 240 1038 N ATOM 2595 CA ARG A 319 33.916 27.587 55.205 1.00 87.48 C ANISOU 2595 CA ARG A 319 13042 12134 8063 -2765 529 866 C ATOM 2596 C ARG A 319 33.655 28.931 54.540 1.00 88.24 C ANISOU 2596 C ARG A 319 12998 12191 8337 -2669 522 534 C ATOM 2597 O ARG A 319 33.076 28.969 53.449 1.00 86.46 O ANISOU 2597 O ARG A 319 12597 11855 8400 -2613 650 448 O ATOM 2598 CB ARG A 319 32.719 27.199 56.079 1.00 94.17 C ANISOU 2598 CB ARG A 319 13991 13178 8610 -2874 810 839 C ATOM 2599 CG ARG A 319 32.481 28.097 57.281 1.00113.27 C ANISOU 2599 CG ARG A 319 16577 15826 10635 -2903 829 631 C ATOM 2600 CD ARG A 319 30.996 28.248 57.589 1.00125.02 C ANISOU 2600 CD ARG A 319 18044 17472 11985 -2933 1189 457 C ATOM 2601 NE ARG A 319 30.305 29.039 56.574 1.00129.80 N ANISOU 2601 NE ARG A 319 18433 17986 12899 -2841 1305 196 N ATOM 2602 CZ ARG A 319 30.311 30.369 56.533 1.00133.77 C ANISOU 2602 CZ ARG A 319 18917 18495 13415 -2749 1253 -115 C ATOM 2603 NH1 ARG A 319 30.978 31.058 57.450 1.00142.98 N ANISOU 2603 NH1 ARG A 319 20284 19747 14296 -2744 1076 -223 N ATOM 2604 NH2 ARG A 319 29.655 31.010 55.576 1.00126.08 N ANISOU 2604 NH2 ARG A 319 17730 17433 12743 -2667 1362 -312 N ATOM 2605 N GLU A 320 34.070 30.035 55.165 1.00 87.41 N ANISOU 2605 N GLU A 320 12975 12165 8073 -2653 362 348 N ATOM 2606 CA GLU A 320 33.899 31.333 54.521 1.00 91.23 C ANISOU 2606 CA GLU A 320 13324 12581 8760 -2557 334 49 C ATOM 2607 C GLU A 320 34.861 31.492 53.349 1.00 80.33 C ANISOU 2607 C GLU A 320 11763 10990 7767 -2461 126 151 C ATOM 2608 O GLU A 320 34.490 32.044 52.306 1.00 75.77 O ANISOU 2608 O GLU A 320 11002 10311 7477 -2375 191 7 O ATOM 2609 CB GLU A 320 34.085 32.461 55.538 1.00102.04 C ANISOU 2609 CB GLU A 320 14857 14062 9851 -2572 209 -188 C ATOM 2610 CG GLU A 320 34.435 33.805 54.910 1.00110.61 C ANISOU 2610 CG GLU A 320 15820 15019 11189 -2478 45 -422 C ATOM 2611 CD GLU A 320 33.588 34.954 55.429 1.00117.94 C ANISOU 2611 CD GLU A 320 16824 16030 11959 -2450 178 -799 C ATOM 2612 OE1 GLU A 320 32.394 34.735 55.720 1.00122.04 O ANISOU 2612 OE1 GLU A 320 17364 16676 12330 -2455 502 -900 O ATOM 2613 OE2 GLU A 320 34.123 36.079 55.545 1.00116.78 O ANISOU 2613 OE2 GLU A 320 16711 15812 11849 -2418 -39 -986 O ATOM 2614 N VAL A 321 36.094 31.001 53.501 1.00 77.67 N ANISOU 2614 N VAL A 321 11469 10595 7447 -2468 -118 421 N ATOM 2615 CA VAL A 321 37.068 31.049 52.413 1.00 68.85 C ANISOU 2615 CA VAL A 321 10174 9289 6695 -2361 -289 566 C ATOM 2616 C VAL A 321 36.612 30.180 51.245 1.00 67.53 C ANISOU 2616 C VAL A 321 9883 8998 6779 -2298 -88 665 C ATOM 2617 O VAL A 321 36.664 30.600 50.083 1.00 71.18 O ANISOU 2617 O VAL A 321 10170 9335 7540 -2192 -82 601 O ATOM 2618 CB VAL A 321 38.458 30.625 52.922 1.00 67.12 C ANISOU 2618 CB VAL A 321 10016 9049 6436 -2380 -574 871 C ATOM 2619 CG1 VAL A 321 39.419 30.468 51.763 1.00 69.18 C ANISOU 2619 CG1 VAL A 321 10080 9121 7084 -2249 -688 1074 C ATOM 2620 CG2 VAL A 321 38.986 31.637 53.929 1.00 69.43 C ANISOU 2620 CG2 VAL A 321 10424 9438 6518 -2449 -833 751 C ATOM 2621 N ALA A 322 36.175 28.951 51.528 1.00 64.86 N ANISOU 2621 N ALA A 322 9642 8683 6318 -2367 68 830 N ATOM 2622 CA ALA A 322 35.686 28.095 50.452 1.00 65.31 C ANISOU 2622 CA ALA A 322 9615 8602 6596 -2327 243 902 C ATOM 2623 C ALA A 322 34.461 28.705 49.784 1.00 66.18 C ANISOU 2623 C ALA A 322 9607 8729 6809 -2320 434 622 C ATOM 2624 O ALA A 322 34.297 28.613 48.562 1.00 66.68 O ANISOU 2624 O ALA A 322 9544 8656 7135 -2244 485 602 O ATOM 2625 CB ALA A 322 35.373 26.695 50.981 1.00 68.24 C ANISOU 2625 CB ALA A 322 10126 8985 6816 -2426 365 1124 C ATOM 2626 N LYS A 323 33.593 29.345 50.571 1.00 66.69 N ANISOU 2626 N LYS A 323 9713 8963 6665 -2392 544 410 N ATOM 2627 CA LYS A 323 32.431 30.015 49.996 1.00 66.79 C ANISOU 2627 CA LYS A 323 9586 8998 6793 -2375 722 156 C ATOM 2628 C LYS A 323 32.855 31.144 49.065 1.00 70.00 C ANISOU 2628 C LYS A 323 9829 9302 7465 -2248 590 10 C ATOM 2629 O LYS A 323 32.252 31.346 48.004 1.00 69.35 O ANISOU 2629 O LYS A 323 9590 9148 7613 -2200 681 -81 O ATOM 2630 CB LYS A 323 31.536 30.542 51.115 1.00 68.76 C ANISOU 2630 CB LYS A 323 9915 9450 6759 -2445 874 -32 C ATOM 2631 CG LYS A 323 30.257 31.201 50.647 1.00 75.53 C ANISOU 2631 CG LYS A 323 10614 10347 7736 -2424 1085 -271 C ATOM 2632 CD LYS A 323 29.573 31.872 51.822 1.00 89.69 C ANISOU 2632 CD LYS A 323 12501 12336 9240 -2450 1230 -466 C ATOM 2633 CE LYS A 323 28.286 32.562 51.422 1.00 96.32 C ANISOU 2633 CE LYS A 323 13163 13219 10215 -2411 1459 -688 C ATOM 2634 NZ LYS A 323 27.725 33.297 52.589 1.00102.61 N ANISOU 2634 NZ LYS A 323 14070 14195 10723 -2399 1612 -894 N ATOM 2635 N THR A 324 33.899 31.884 49.447 1.00 70.61 N ANISOU 2635 N THR A 324 9938 9372 7519 -2205 359 3 N ATOM 2636 CA THR A 324 34.419 32.955 48.603 1.00 69.11 C ANISOU 2636 CA THR A 324 9586 9075 7598 -2092 211 -94 C ATOM 2637 C THR A 324 34.979 32.405 47.295 1.00 68.90 C ANISOU 2637 C THR A 324 9435 8887 7858 -1997 175 95 C ATOM 2638 O THR A 324 34.685 32.921 46.210 1.00 65.96 O ANISOU 2638 O THR A 324 8899 8440 7724 -1916 212 2 O ATOM 2639 CB THR A 324 35.501 33.727 49.360 1.00 70.63 C ANISOU 2639 CB THR A 324 9849 9281 7708 -2094 -59 -95 C ATOM 2640 OG1 THR A 324 34.923 34.379 50.498 1.00 79.59 O ANISOU 2640 OG1 THR A 324 11123 10554 8562 -2164 -17 -326 O ATOM 2641 CG2 THR A 324 36.153 34.757 48.466 1.00 71.07 C ANISOU 2641 CG2 THR A 324 9720 9208 8074 -1987 -230 -138 C ATOM 2642 N VAL A 325 35.795 31.352 47.386 1.00 68.98 N ANISOU 2642 N VAL A 325 9528 8842 7841 -1996 108 369 N ATOM 2643 CA VAL A 325 36.472 30.814 46.209 1.00 65.61 C ANISOU 2643 CA VAL A 325 9010 8254 7664 -1878 80 558 C ATOM 2644 C VAL A 325 35.457 30.339 45.176 1.00 64.08 C ANISOU 2644 C VAL A 325 8767 7998 7584 -1867 285 480 C ATOM 2645 O VAL A 325 35.540 30.684 43.991 1.00 69.08 O ANISOU 2645 O VAL A 325 9268 8539 8442 -1759 285 451 O ATOM 2646 CB VAL A 325 37.430 29.679 46.614 1.00 67.93 C ANISOU 2646 CB VAL A 325 9418 8495 7896 -1874 4 870 C ATOM 2647 CG1 VAL A 325 37.790 28.830 45.405 1.00 68.12 C ANISOU 2647 CG1 VAL A 325 9399 8346 8137 -1750 73 1038 C ATOM 2648 CG2 VAL A 325 38.682 30.249 47.269 1.00 66.03 C ANISOU 2648 CG2 VAL A 325 9163 8281 7643 -1856 -260 995 C ATOM 2649 N PHE A 326 34.491 29.530 45.603 1.00 63.99 N ANISOU 2649 N PHE A 326 8859 8039 7416 -1985 452 461 N ATOM 2650 CA PHE A 326 33.543 28.976 44.646 1.00 62.03 C ANISOU 2650 CA PHE A 326 8572 7719 7279 -2003 613 411 C ATOM 2651 C PHE A 326 32.434 29.945 44.274 1.00 61.09 C ANISOU 2651 C PHE A 326 8306 7675 7231 -2022 702 155 C ATOM 2652 O PHE A 326 31.638 29.635 43.383 1.00 63.03 O ANISOU 2652 O PHE A 326 8490 7865 7592 -2041 801 108 O ATOM 2653 CB PHE A 326 32.956 27.671 45.180 1.00 62.28 C ANISOU 2653 CB PHE A 326 8751 7751 7160 -2135 741 527 C ATOM 2654 CG PHE A 326 33.946 26.548 45.213 1.00 66.50 C ANISOU 2654 CG PHE A 326 9418 8155 7695 -2095 676 797 C ATOM 2655 CD1 PHE A 326 34.349 25.930 44.039 1.00 67.98 C ANISOU 2655 CD1 PHE A 326 9611 8148 8072 -1987 676 889 C ATOM 2656 CD2 PHE A 326 34.489 26.123 46.412 1.00 61.08 C ANISOU 2656 CD2 PHE A 326 8856 7538 6815 -2152 617 962 C ATOM 2657 CE1 PHE A 326 35.267 24.905 44.059 1.00 70.16 C ANISOU 2657 CE1 PHE A 326 10005 8285 8368 -1923 637 1138 C ATOM 2658 CE2 PHE A 326 35.409 25.092 46.442 1.00 64.92 C ANISOU 2658 CE2 PHE A 326 9445 7894 7329 -2103 556 1233 C ATOM 2659 CZ PHE A 326 35.799 24.481 45.262 1.00 71.99 C ANISOU 2659 CZ PHE A 326 10335 8579 8438 -1980 575 1320 C ATOM 2660 N CYS A 327 32.363 31.101 44.933 1.00 61.83 N ANISOU 2660 N CYS A 327 8346 7882 7263 -2019 661 -8 N ATOM 2661 CA CYS A 327 31.562 32.199 44.409 1.00 58.68 C ANISOU 2661 CA CYS A 327 7776 7516 7003 -1985 714 -233 C ATOM 2662 C CYS A 327 32.198 32.765 43.145 1.00 55.93 C ANISOU 2662 C CYS A 327 7286 7045 6919 -1848 593 -214 C ATOM 2663 O CYS A 327 31.517 32.982 42.137 1.00 55.39 O ANISOU 2663 O CYS A 327 7089 6942 7014 -1821 657 -290 O ATOM 2664 CB CYS A 327 31.405 33.286 45.474 1.00 59.17 C ANISOU 2664 CB CYS A 327 7850 7702 6931 -2000 700 -420 C ATOM 2665 SG CYS A 327 30.594 34.803 44.907 1.00 67.08 S ANISOU 2665 SG CYS A 327 8636 8714 8138 -1925 744 -692 S ATOM 2666 N LEU A 328 33.515 32.997 43.181 1.00 50.60 N ANISOU 2666 N LEU A 328 6625 6310 6290 -1763 415 -89 N ATOM 2667 CA LEU A 328 34.226 33.445 41.990 1.00 50.83 C ANISOU 2667 CA LEU A 328 6518 6229 6566 -1624 316 -20 C ATOM 2668 C LEU A 328 34.141 32.402 40.881 1.00 57.79 C ANISOU 2668 C LEU A 328 7425 7009 7524 -1580 403 104 C ATOM 2669 O LEU A 328 33.981 32.745 39.701 1.00 61.21 O ANISOU 2669 O LEU A 328 7741 7388 8128 -1497 414 74 O ATOM 2670 CB LEU A 328 35.685 33.746 42.330 1.00 48.48 C ANISOU 2670 CB LEU A 328 6221 5892 6307 -1555 113 141 C ATOM 2671 CG LEU A 328 35.927 34.800 43.410 1.00 57.87 C ANISOU 2671 CG LEU A 328 7417 7154 7418 -1606 -26 18 C ATOM 2672 CD1 LEU A 328 37.418 35.027 43.621 1.00 53.90 C ANISOU 2672 CD1 LEU A 328 6891 6596 6991 -1553 -262 218 C ATOM 2673 CD2 LEU A 328 35.230 36.101 43.054 1.00 57.32 C ANISOU 2673 CD2 LEU A 328 7199 7093 7487 -1581 -12 -223 C ATOM 2674 N VAL A 329 34.253 31.120 41.240 1.00 57.61 N ANISOU 2674 N VAL A 329 7570 6952 7369 -1633 459 244 N ATOM 2675 CA VAL A 329 34.116 30.057 40.248 1.00 56.44 C ANISOU 2675 CA VAL A 329 7491 6678 7274 -1601 543 335 C ATOM 2676 C VAL A 329 32.736 30.111 39.608 1.00 58.86 C ANISOU 2676 C VAL A 329 7740 7007 7617 -1683 654 163 C ATOM 2677 O VAL A 329 32.599 30.100 38.379 1.00 58.59 O ANISOU 2677 O VAL A 329 7659 6895 7707 -1613 662 147 O ATOM 2678 CB VAL A 329 34.384 28.682 40.886 1.00 54.40 C ANISOU 2678 CB VAL A 329 7432 6363 6874 -1661 584 508 C ATOM 2679 CG1 VAL A 329 34.009 27.562 39.920 1.00 50.46 C ANISOU 2679 CG1 VAL A 329 7038 5714 6419 -1656 679 552 C ATOM 2680 CG2 VAL A 329 35.839 28.567 41.303 1.00 54.41 C ANISOU 2680 CG2 VAL A 329 7466 6325 6884 -1556 459 723 C ATOM 2681 N LEU A 330 31.693 30.179 40.438 1.00 63.44 N ANISOU 2681 N LEU A 330 8317 7703 8086 -1831 740 44 N ATOM 2682 CA LEU A 330 30.335 30.273 39.916 1.00 62.97 C ANISOU 2682 CA LEU A 330 8163 7679 8084 -1920 839 -95 C ATOM 2683 C LEU A 330 30.161 31.515 39.049 1.00 62.02 C ANISOU 2683 C LEU A 330 7841 7578 8147 -1825 789 -221 C ATOM 2684 O LEU A 330 29.559 31.453 37.971 1.00 60.00 O ANISOU 2684 O LEU A 330 7517 7279 8002 -1827 803 -257 O ATOM 2685 CB LEU A 330 29.343 30.283 41.075 1.00 61.71 C ANISOU 2685 CB LEU A 330 8001 7663 7784 -2069 959 -178 C ATOM 2686 CG LEU A 330 28.191 29.284 41.011 1.00 68.18 C ANISOU 2686 CG LEU A 330 8856 8478 8572 -2232 1083 -154 C ATOM 2687 CD1 LEU A 330 27.213 29.608 42.114 1.00 76.21 C ANISOU 2687 CD1 LEU A 330 9810 9671 9476 -2343 1224 -241 C ATOM 2688 CD2 LEU A 330 27.509 29.313 39.650 1.00 68.17 C ANISOU 2688 CD2 LEU A 330 8745 8404 8751 -2238 1069 -212 C ATOM 2689 N VAL A 331 30.692 32.653 39.505 1.00 60.71 N ANISOU 2689 N VAL A 331 7584 7467 8015 -1748 713 -283 N ATOM 2690 CA VAL A 331 30.586 33.895 38.741 1.00 60.04 C ANISOU 2690 CA VAL A 331 7301 7386 8125 -1655 655 -385 C ATOM 2691 C VAL A 331 31.247 33.743 37.375 1.00 59.50 C ANISOU 2691 C VAL A 331 7207 7207 8193 -1532 585 -267 C ATOM 2692 O VAL A 331 30.719 34.206 36.355 1.00 62.85 O ANISOU 2692 O VAL A 331 7501 7624 8754 -1499 583 -321 O ATOM 2693 CB VAL A 331 31.192 35.061 39.546 1.00 62.60 C ANISOU 2693 CB VAL A 331 7569 7752 8464 -1601 561 -457 C ATOM 2694 CG1 VAL A 331 31.644 36.180 38.624 1.00 64.44 C ANISOU 2694 CG1 VAL A 331 7623 7930 8932 -1472 449 -467 C ATOM 2695 CG2 VAL A 331 30.182 35.588 40.547 1.00 60.06 C ANISOU 2695 CG2 VAL A 331 7224 7547 8050 -1688 665 -648 C ATOM 2696 N PHE A 332 32.405 33.081 37.334 1.00 57.61 N ANISOU 2696 N PHE A 332 7090 6885 7913 -1456 533 -92 N ATOM 2697 CA PHE A 332 33.084 32.839 36.068 1.00 50.20 C ANISOU 2697 CA PHE A 332 6152 5845 7076 -1316 503 33 C ATOM 2698 C PHE A 332 32.230 31.984 35.139 1.00 55.04 C ANISOU 2698 C PHE A 332 6849 6405 7660 -1367 585 0 C ATOM 2699 O PHE A 332 32.124 32.270 33.940 1.00 55.60 O ANISOU 2699 O PHE A 332 6854 6448 7825 -1290 569 -7 O ATOM 2700 CB PHE A 332 34.431 32.172 36.334 1.00 46.54 C ANISOU 2700 CB PHE A 332 5806 5303 6573 -1221 463 241 C ATOM 2701 CG PHE A 332 35.120 31.670 35.100 1.00 56.19 C ANISOU 2701 CG PHE A 332 7073 6415 7863 -1061 485 383 C ATOM 2702 CD1 PHE A 332 35.956 32.498 34.368 1.00 58.99 C ANISOU 2702 CD1 PHE A 332 7276 6761 8375 -898 422 477 C ATOM 2703 CD2 PHE A 332 34.939 30.365 34.676 1.00 55.65 C ANISOU 2703 CD2 PHE A 332 7205 6241 7699 -1068 576 425 C ATOM 2704 CE1 PHE A 332 36.591 32.033 33.232 1.00 57.38 C ANISOU 2704 CE1 PHE A 332 7121 6470 8211 -731 474 614 C ATOM 2705 CE2 PHE A 332 35.567 29.896 33.543 1.00 53.82 C ANISOU 2705 CE2 PHE A 332 7046 5900 7503 -901 616 535 C ATOM 2706 CZ PHE A 332 36.396 30.731 32.818 1.00 54.09 C ANISOU 2706 CZ PHE A 332 6929 5950 7673 -724 578 631 C ATOM 2707 N ALA A 333 31.617 30.927 35.674 1.00 56.75 N ANISOU 2707 N ALA A 333 7216 6605 7743 -1507 660 -11 N ATOM 2708 CA ALA A 333 30.840 30.021 34.834 1.00 53.66 C ANISOU 2708 CA ALA A 333 6929 6135 7326 -1582 707 -36 C ATOM 2709 C ALA A 333 29.660 30.740 34.194 1.00 53.31 C ANISOU 2709 C ALA A 333 6712 6168 7377 -1653 700 -179 C ATOM 2710 O ALA A 333 29.423 30.616 32.989 1.00 58.30 O ANISOU 2710 O ALA A 333 7355 6744 8051 -1622 669 -189 O ATOM 2711 CB ALA A 333 30.355 28.827 35.657 1.00 54.86 C ANISOU 2711 CB ALA A 333 7249 6252 7344 -1744 778 -7 C ATOM 2712 N LEU A 334 28.897 31.488 34.992 1.00 56.49 N ANISOU 2712 N LEU A 334 6957 6699 7807 -1743 731 -284 N ATOM 2713 CA LEU A 334 27.718 32.166 34.468 1.00 60.14 C ANISOU 2713 CA LEU A 334 7227 7238 8386 -1809 734 -399 C ATOM 2714 C LEU A 334 28.088 33.291 33.511 1.00 60.99 C ANISOU 2714 C LEU A 334 7174 7353 8648 -1658 649 -411 C ATOM 2715 O LEU A 334 27.359 33.545 32.545 1.00 62.53 O ANISOU 2715 O LEU A 334 7264 7561 8933 -1681 615 -446 O ATOM 2716 CB LEU A 334 26.872 32.703 35.621 1.00 63.11 C ANISOU 2716 CB LEU A 334 7476 7746 8757 -1908 822 -501 C ATOM 2717 CG LEU A 334 26.345 31.627 36.571 1.00 68.76 C ANISOU 2717 CG LEU A 334 8322 8481 9322 -2072 926 -470 C ATOM 2718 CD1 LEU A 334 25.569 32.264 37.704 1.00 72.97 C ANISOU 2718 CD1 LEU A 334 8727 9164 9833 -2136 1042 -568 C ATOM 2719 CD2 LEU A 334 25.479 30.625 35.819 1.00 64.89 C ANISOU 2719 CD2 LEU A 334 7883 7925 8849 -2215 927 -434 C ATOM 2720 N CYS A 335 29.215 33.963 33.749 1.00 59.64 N ANISOU 2720 N CYS A 335 6973 7172 8515 -1515 599 -362 N ATOM 2721 CA CYS A 335 29.638 35.029 32.848 1.00 61.31 C ANISOU 2721 CA CYS A 335 7022 7382 8890 -1374 517 -340 C ATOM 2722 C CYS A 335 30.086 34.473 31.503 1.00 61.60 C ANISOU 2722 C CYS A 335 7154 7340 8910 -1281 488 -232 C ATOM 2723 O CYS A 335 29.803 35.062 30.456 1.00 63.46 O ANISOU 2723 O CYS A 335 7271 7595 9246 -1229 442 -232 O ATOM 2724 CB CYS A 335 30.761 35.841 33.485 1.00 59.34 C ANISOU 2724 CB CYS A 335 6716 7130 8702 -1264 455 -293 C ATOM 2725 SG CYS A 335 30.249 36.962 34.804 1.00 63.83 S ANISOU 2725 SG CYS A 335 7152 7782 9317 -1328 460 -464 S ATOM 2726 N TRP A 336 30.788 33.345 31.504 1.00 58.17 N ANISOU 2726 N TRP A 336 6943 6814 8344 -1249 521 -135 N ATOM 2727 CA TRP A 336 31.321 32.786 30.269 1.00 53.65 C ANISOU 2727 CA TRP A 336 6499 6154 7731 -1128 521 -40 C ATOM 2728 C TRP A 336 30.404 31.751 29.630 1.00 59.98 C ANISOU 2728 C TRP A 336 7473 6896 8421 -1249 539 -108 C ATOM 2729 O TRP A 336 30.724 31.243 28.549 1.00 60.68 O ANISOU 2729 O TRP A 336 7709 6904 8444 -1156 539 -63 O ATOM 2730 CB TRP A 336 32.700 32.179 30.528 1.00 50.33 C ANISOU 2730 CB TRP A 336 6222 5645 7257 -988 553 118 C ATOM 2731 CG TRP A 336 33.753 33.224 30.654 1.00 52.36 C ANISOU 2731 CG TRP A 336 6300 5941 7652 -840 500 229 C ATOM 2732 CD1 TRP A 336 34.174 33.832 31.797 1.00 55.01 C ANISOU 2732 CD1 TRP A 336 6532 6322 8047 -866 448 241 C ATOM 2733 CD2 TRP A 336 34.505 33.806 29.588 1.00 57.76 C ANISOU 2733 CD2 TRP A 336 6889 6622 8437 -654 483 353 C ATOM 2734 NE1 TRP A 336 35.154 34.752 31.512 1.00 55.81 N ANISOU 2734 NE1 TRP A 336 6471 6431 8302 -721 378 367 N ATOM 2735 CE2 TRP A 336 35.375 34.755 30.160 1.00 58.23 C ANISOU 2735 CE2 TRP A 336 6766 6714 8644 -585 410 451 C ATOM 2736 CE3 TRP A 336 34.532 33.613 28.203 1.00 51.42 C ANISOU 2736 CE3 TRP A 336 6145 5793 7600 -542 520 398 C ATOM 2737 CZ2 TRP A 336 36.261 35.508 29.396 1.00 55.31 C ANISOU 2737 CZ2 TRP A 336 6245 6351 8421 -414 379 614 C ATOM 2738 CZ3 TRP A 336 35.409 34.362 27.449 1.00 46.97 C ANISOU 2738 CZ3 TRP A 336 5443 5254 7151 -356 509 556 C ATOM 2739 CH2 TRP A 336 36.262 35.297 28.045 1.00 50.62 C ANISOU 2739 CH2 TRP A 336 5697 5746 7791 -295 442 673 C ATOM 2740 N LEU A 337 29.271 31.436 30.265 1.00 63.23 N ANISOU 2740 N LEU A 337 7872 7343 8810 -1454 553 -210 N ATOM 2741 CA LEU A 337 28.354 30.454 29.687 1.00 61.78 C ANISOU 2741 CA LEU A 337 7838 7091 8546 -1601 539 -262 C ATOM 2742 C LEU A 337 27.713 30.937 28.391 1.00 63.70 C ANISOU 2742 C LEU A 337 7994 7370 8839 -1604 452 -307 C ATOM 2743 O LEU A 337 27.729 30.179 27.405 1.00 66.10 O ANISOU 2743 O LEU A 337 8504 7573 9038 -1596 415 -305 O ATOM 2744 CB LEU A 337 27.297 30.057 30.721 1.00 57.26 C ANISOU 2744 CB LEU A 337 7229 6562 7964 -1826 580 -323 C ATOM 2745 CG LEU A 337 26.194 29.130 30.207 1.00 61.19 C ANISOU 2745 CG LEU A 337 7831 6995 8425 -2024 539 -366 C ATOM 2746 CD1 LEU A 337 26.756 27.769 29.821 1.00 61.64 C ANISOU 2746 CD1 LEU A 337 8223 6854 8345 -2009 539 -320 C ATOM 2747 CD2 LEU A 337 25.080 28.989 31.234 1.00 65.74 C ANISOU 2747 CD2 LEU A 337 8285 7655 9038 -2238 593 -397 C ATOM 2748 N PRO A 338 27.136 32.146 28.305 1.00 61.77 N ANISOU 2748 N PRO A 338 7469 7257 8744 -1614 410 -346 N ATOM 2749 CA PRO A 338 26.447 32.515 27.055 1.00 63.90 C ANISOU 2749 CA PRO A 338 7660 7564 9056 -1637 308 -366 C ATOM 2750 C PRO A 338 27.363 32.563 25.843 1.00 69.12 C ANISOU 2750 C PRO A 338 8441 8177 9644 -1446 275 -290 C ATOM 2751 O PRO A 338 26.979 32.086 24.767 1.00 76.37 O ANISOU 2751 O PRO A 338 9497 9058 10461 -1483 202 -307 O ATOM 2752 CB PRO A 338 25.855 33.896 27.375 1.00 61.63 C ANISOU 2752 CB PRO A 338 7029 7415 8974 -1643 292 -397 C ATOM 2753 CG PRO A 338 25.815 33.968 28.858 1.00 60.26 C ANISOU 2753 CG PRO A 338 6798 7271 8826 -1696 392 -442 C ATOM 2754 CD PRO A 338 27.015 33.212 29.316 1.00 58.66 C ANISOU 2754 CD PRO A 338 6830 6973 8484 -1609 445 -380 C ATOM 2755 N LEU A 339 28.570 33.117 25.984 1.00 64.49 N ANISOU 2755 N LEU A 339 7810 7594 9099 -1244 326 -197 N ATOM 2756 CA LEU A 339 29.470 33.221 24.839 1.00 59.50 C ANISOU 2756 CA LEU A 339 7263 6937 8408 -1042 325 -94 C ATOM 2757 C LEU A 339 29.908 31.844 24.357 1.00 61.96 C ANISOU 2757 C LEU A 339 7931 7105 8505 -999 378 -88 C ATOM 2758 O LEU A 339 29.850 31.546 23.157 1.00 69.93 O ANISOU 2758 O LEU A 339 9095 8086 9388 -946 348 -90 O ATOM 2759 CB LEU A 339 30.688 34.071 25.197 1.00 55.57 C ANISOU 2759 CB LEU A 339 6615 6467 8033 -849 367 34 C ATOM 2760 CG LEU A 339 31.711 34.211 24.072 1.00 56.24 C ANISOU 2760 CG LEU A 339 6755 6540 8075 -621 398 183 C ATOM 2761 CD1 LEU A 339 31.070 34.791 22.819 1.00 54.83 C ANISOU 2761 CD1 LEU A 339 6497 6441 7894 -618 318 181 C ATOM 2762 CD2 LEU A 339 32.852 35.079 24.540 1.00 56.69 C ANISOU 2762 CD2 LEU A 339 6620 6621 8297 -467 419 332 C ATOM 2763 N HIS A 340 30.361 30.991 25.279 1.00 58.40 N ANISOU 2763 N HIS A 340 7630 6556 8004 -1014 457 -79 N ATOM 2764 CA HIS A 340 30.769 29.647 24.890 1.00 61.33 C ANISOU 2764 CA HIS A 340 8349 6759 8196 -966 517 -76 C ATOM 2765 C HIS A 340 29.599 28.847 24.342 1.00 65.22 C ANISOU 2765 C HIS A 340 9023 7182 8575 -1169 432 -212 C ATOM 2766 O HIS A 340 29.783 28.015 23.448 1.00 61.66 O ANISOU 2766 O HIS A 340 8866 6603 7960 -1110 438 -240 O ATOM 2767 CB HIS A 340 31.407 28.923 26.073 1.00 56.47 C ANISOU 2767 CB HIS A 340 7828 6052 7575 -960 604 -20 C ATOM 2768 CG HIS A 340 32.823 29.334 26.329 1.00 57.79 C ANISOU 2768 CG HIS A 340 7918 6230 7809 -726 679 147 C ATOM 2769 ND1 HIS A 340 33.891 28.769 25.667 1.00 60.28 N ANISOU 2769 ND1 HIS A 340 8417 6439 8049 -498 776 259 N ATOM 2770 CD2 HIS A 340 33.346 30.264 27.163 1.00 57.26 C ANISOU 2770 CD2 HIS A 340 7605 6264 7888 -686 666 227 C ATOM 2771 CE1 HIS A 340 35.012 29.328 26.087 1.00 59.62 C ANISOU 2771 CE1 HIS A 340 8173 6399 8080 -333 817 428 C ATOM 2772 NE2 HIS A 340 34.709 30.238 26.995 1.00 59.61 N ANISOU 2772 NE2 HIS A 340 7919 6518 8211 -455 734 406 N ATOM 2773 N LEU A 341 28.395 29.084 24.862 1.00 65.03 N ANISOU 2773 N LEU A 341 8833 7236 8640 -1407 352 -293 N ATOM 2774 CA LEU A 341 27.210 28.462 24.287 1.00 64.25 C ANISOU 2774 CA LEU A 341 8850 7089 8474 -1624 235 -396 C ATOM 2775 C LEU A 341 26.990 28.939 22.856 1.00 71.44 C ANISOU 2775 C LEU A 341 9768 8053 9322 -1567 128 -412 C ATOM 2776 O LEU A 341 26.758 28.133 21.948 1.00 74.16 O ANISOU 2776 O LEU A 341 10393 8285 9499 -1612 55 -476 O ATOM 2777 CB LEU A 341 25.994 28.768 25.159 1.00 57.75 C ANISOU 2777 CB LEU A 341 7778 6367 7796 -1868 190 -439 C ATOM 2778 CG LEU A 341 24.659 28.133 24.778 1.00 60.52 C ANISOU 2778 CG LEU A 341 8182 6679 8132 -2139 56 -513 C ATOM 2779 CD1 LEU A 341 24.694 26.620 24.952 1.00 64.76 C ANISOU 2779 CD1 LEU A 341 9062 7002 8541 -2247 64 -542 C ATOM 2780 CD2 LEU A 341 23.545 28.748 25.604 1.00 57.29 C ANISOU 2780 CD2 LEU A 341 7437 6419 7910 -2322 48 -516 C ATOM 2781 N ALA A 342 27.097 30.251 22.632 1.00 68.56 N ANISOU 2781 N ALA A 342 9113 7852 9083 -1464 113 -351 N ATOM 2782 CA ALA A 342 26.868 30.801 21.298 1.00 63.41 C ANISOU 2782 CA ALA A 342 8438 7276 8378 -1411 7 -337 C ATOM 2783 C ALA A 342 27.882 30.261 20.294 1.00 65.64 C ANISOU 2783 C ALA A 342 9036 7466 8440 -1194 70 -303 C ATOM 2784 O ALA A 342 27.515 29.832 19.194 1.00 74.41 O ANISOU 2784 O ALA A 342 10364 8539 9368 -1228 -26 -360 O ATOM 2785 CB ALA A 342 26.917 32.329 21.347 1.00 54.05 C ANISOU 2785 CB ALA A 342 6874 6264 7400 -1322 -4 -251 C ATOM 2786 N ARG A 343 29.168 30.271 20.661 1.00 62.08 N ANISOU 2786 N ARG A 343 8616 6976 7997 -966 232 -204 N ATOM 2787 CA ARG A 343 30.210 29.810 19.749 1.00 57.91 C ANISOU 2787 CA ARG A 343 8357 6368 7279 -718 337 -146 C ATOM 2788 C ARG A 343 30.045 28.335 19.404 1.00 67.37 C ANISOU 2788 C ARG A 343 9986 7361 8251 -776 341 -271 C ATOM 2789 O ARG A 343 30.305 27.925 18.267 1.00 73.66 O ANISOU 2789 O ARG A 343 11060 8099 8827 -654 356 -300 O ATOM 2790 CB ARG A 343 31.592 30.046 20.358 1.00 48.08 C ANISOU 2790 CB ARG A 343 7024 5114 6131 -481 507 11 C ATOM 2791 CG ARG A 343 31.942 31.493 20.613 1.00 46.36 C ANISOU 2791 CG ARG A 343 6415 5064 6136 -401 497 145 C ATOM 2792 CD ARG A 343 31.829 32.299 19.344 1.00 46.86 C ANISOU 2792 CD ARG A 343 6395 5248 6160 -310 442 207 C ATOM 2793 NE ARG A 343 32.032 33.731 19.549 1.00 54.44 N ANISOU 2793 NE ARG A 343 6971 6350 7363 -259 408 333 N ATOM 2794 CZ ARG A 343 33.224 34.314 19.623 1.00 54.73 C ANISOU 2794 CZ ARG A 343 6867 6415 7514 -47 503 520 C ATOM 2795 NH1 ARG A 343 33.315 35.627 19.791 1.00 43.77 N ANISOU 2795 NH1 ARG A 343 5137 5132 6362 -29 443 623 N ATOM 2796 NH2 ARG A 343 34.328 33.583 19.540 1.00 49.06 N ANISOU 2796 NH2 ARG A 343 6340 5608 6691 147 657 616 N ATOM 2797 N ILE A 344 29.642 27.515 20.376 1.00 69.37 N ANISOU 2797 N ILE A 344 10317 7493 8547 -955 334 -344 N ATOM 2798 CA ILE A 344 29.518 26.081 20.123 1.00 76.71 C ANISOU 2798 CA ILE A 344 11661 8190 9294 -1017 332 -456 C ATOM 2799 C ILE A 344 28.274 25.785 19.295 1.00 78.37 C ANISOU 2799 C ILE A 344 12007 8379 9390 -1256 123 -602 C ATOM 2800 O ILE A 344 28.273 24.878 18.453 1.00 84.39 O ANISOU 2800 O ILE A 344 13159 8974 9933 -1242 89 -706 O ATOM 2801 CB ILE A 344 29.517 25.305 21.453 1.00 78.57 C ANISOU 2801 CB ILE A 344 11922 8301 9629 -1136 389 -453 C ATOM 2802 CG1 ILE A 344 30.919 25.310 22.066 1.00 76.97 C ANISOU 2802 CG1 ILE A 344 11693 8070 9481 -873 584 -304 C ATOM 2803 CG2 ILE A 344 29.039 23.876 21.256 1.00 81.09 C ANISOU 2803 CG2 ILE A 344 12628 8371 9811 -1286 333 -581 C ATOM 2804 CD1 ILE A 344 32.010 24.924 21.098 1.00 77.49 C ANISOU 2804 CD1 ILE A 344 12022 8032 9389 -567 719 -257 C ATOM 2805 N LEU A 345 27.192 26.532 19.527 1.00 76.27 N ANISOU 2805 N LEU A 345 11429 8274 9277 -1478 -27 -609 N ATOM 2806 CA LEU A 345 25.991 26.367 18.718 1.00 75.84 C ANISOU 2806 CA LEU A 345 11446 8225 9144 -1714 -255 -711 C ATOM 2807 C LEU A 345 26.250 26.764 17.266 1.00 79.17 C ANISOU 2807 C LEU A 345 12002 8714 9364 -1559 -311 -713 C ATOM 2808 O LEU A 345 25.837 26.057 16.339 1.00 86.64 O ANISOU 2808 O LEU A 345 13277 9551 10091 -1649 -448 -828 O ATOM 2809 CB LEU A 345 24.841 27.175 19.323 1.00 72.53 C ANISOU 2809 CB LEU A 345 10609 7981 8969 -1950 -373 -681 C ATOM 2810 CG LEU A 345 24.284 26.701 20.673 1.00 70.92 C ANISOU 2810 CG LEU A 345 10289 7727 8931 -2158 -341 -688 C ATOM 2811 CD1 LEU A 345 22.931 27.346 20.969 1.00 68.51 C ANISOU 2811 CD1 LEU A 345 9623 7579 8827 -2408 -477 -673 C ATOM 2812 CD2 LEU A 345 24.183 25.182 20.724 1.00 70.58 C ANISOU 2812 CD2 LEU A 345 10636 7427 8756 -2289 -370 -776 C ATOM 2813 N LYS A 346 26.944 27.883 17.046 1.00 72.26 N ANISOU 2813 N LYS A 346 10892 8013 8551 -1330 -214 -582 N ATOM 2814 CA LYS A 346 27.347 28.229 15.686 1.00 72.97 C ANISOU 2814 CA LYS A 346 11124 8173 8429 -1146 -227 -551 C ATOM 2815 C LYS A 346 28.279 27.171 15.106 1.00 80.17 C ANISOU 2815 C LYS A 346 12508 8893 9059 -935 -82 -612 C ATOM 2816 O LYS A 346 28.139 26.777 13.942 1.00 90.53 O ANISOU 2816 O LYS A 346 14142 10163 10092 -912 -160 -699 O ATOM 2817 CB LYS A 346 28.010 29.605 15.659 1.00 68.97 C ANISOU 2817 CB LYS A 346 10258 7872 8077 -933 -129 -366 C ATOM 2818 CG LYS A 346 28.934 29.798 14.469 1.00 75.26 C ANISOU 2818 CG LYS A 346 11232 8713 8649 -644 -26 -281 C ATOM 2819 CD LYS A 346 29.392 31.233 14.302 1.00 80.23 C ANISOU 2819 CD LYS A 346 11479 9553 9451 -483 19 -78 C ATOM 2820 CE LYS A 346 28.392 32.038 13.495 1.00 85.24 C ANISOU 2820 CE LYS A 346 11946 10354 10088 -625 -201 -58 C ATOM 2821 NZ LYS A 346 28.984 33.318 13.018 1.00 85.79 N ANISOU 2821 NZ LYS A 346 11731 10603 10262 -423 -145 158 N ATOM 2822 N LEU A 347 29.220 26.677 15.914 1.00 81.77 N ANISOU 2822 N LEU A 347 12771 8972 9326 -780 127 -569 N ATOM 2823 CA LEU A 347 30.176 25.684 15.431 1.00 89.09 C ANISOU 2823 CA LEU A 347 14124 9704 10024 -542 301 -607 C ATOM 2824 C LEU A 347 29.494 24.376 15.049 1.00 92.82 C ANISOU 2824 C LEU A 347 15044 9935 10289 -726 174 -824 C ATOM 2825 O LEU A 347 29.939 23.693 14.120 1.00100.05 O ANISOU 2825 O LEU A 347 16379 10712 10924 -560 241 -912 O ATOM 2826 CB LEU A 347 31.241 25.435 16.496 1.00 92.76 C ANISOU 2826 CB LEU A 347 14510 10085 10648 -367 525 -489 C ATOM 2827 CG LEU A 347 32.645 25.038 16.058 1.00 96.77 C ANISOU 2827 CG LEU A 347 15240 10500 11027 10 785 -396 C ATOM 2828 CD1 LEU A 347 33.156 25.975 14.978 1.00 98.31 C ANISOU 2828 CD1 LEU A 347 15344 10890 11118 243 853 -277 C ATOM 2829 CD2 LEU A 347 33.559 25.078 17.263 1.00 97.70 C ANISOU 2829 CD2 LEU A 347 15143 10597 11381 128 946 -232 C ATOM 2830 N THR A 348 28.410 24.018 15.739 1.00 89.84 N ANISOU 2830 N THR A 348 14592 9498 10046 -1067 -9 -908 N ATOM 2831 CA THR A 348 27.753 22.733 15.534 1.00 93.64 C ANISOU 2831 CA THR A 348 15473 9720 10386 -1279 -149 -1096 C ATOM 2832 C THR A 348 26.540 22.796 14.615 1.00 97.20 C ANISOU 2832 C THR A 348 16007 10216 10708 -1546 -453 -1215 C ATOM 2833 O THR A 348 26.254 21.808 13.933 1.00103.79 O ANISOU 2833 O THR A 348 17285 10834 11316 -1635 -571 -1386 O ATOM 2834 CB THR A 348 27.315 22.133 16.878 1.00 95.16 C ANISOU 2834 CB THR A 348 15557 9792 10809 -1507 -163 -1091 C ATOM 2835 OG1 THR A 348 26.769 23.164 17.713 1.00 97.82 O ANISOU 2835 OG1 THR A 348 15386 10370 11412 -1648 -208 -976 O ATOM 2836 CG2 THR A 348 28.488 21.471 17.588 1.00 92.56 C ANISOU 2836 CG2 THR A 348 15366 9292 10512 -1273 95 -1027 C ATOM 2837 N LEU A 349 25.814 23.915 14.574 1.00144.92 N ANISOU 2837 N LEU A 349 20864 16493 17707 -2246 -4177 -6050 N ATOM 2838 CA LEU A 349 24.499 23.949 13.939 1.00146.04 C ANISOU 2838 CA LEU A 349 21002 16681 17804 -2704 -4719 -5950 C ATOM 2839 C LEU A 349 24.456 24.809 12.684 1.00159.34 C ANISOU 2839 C LEU A 349 22755 19052 18736 -2637 -4692 -6053 C ATOM 2840 O LEU A 349 23.369 25.180 12.230 1.00160.63 O ANISOU 2840 O LEU A 349 22792 19411 18829 -2997 -5065 -5814 O ATOM 2841 CB LEU A 349 23.441 24.445 14.923 1.00131.62 C ANISOU 2841 CB LEU A 349 18664 14817 16529 -3122 -4778 -5206 C ATOM 2842 CG LEU A 349 23.269 23.671 16.224 1.00120.95 C ANISOU 2842 CG LEU A 349 17187 12847 15921 -3284 -4829 -4963 C ATOM 2843 CD1 LEU A 349 21.981 24.102 16.904 1.00109.93 C ANISOU 2843 CD1 LEU A 349 15296 11511 14960 -3750 -4985 -4283 C ATOM 2844 CD2 LEU A 349 23.281 22.172 15.973 1.00118.60 C ANISOU 2844 CD2 LEU A 349 17285 11994 15785 -3298 -5085 -5342 C ATOM 2845 N TYR A 350 25.603 25.139 12.104 1.00181.94 N ANISOU 2845 N TYR A 350 25790 22314 21024 -2192 -4266 -6371 N ATOM 2846 CA TYR A 350 25.598 26.002 10.928 1.00193.52 C ANISOU 2846 CA TYR A 350 27321 24471 21737 -2141 -4204 -6400 C ATOM 2847 C TYR A 350 25.540 25.131 9.681 1.00203.62 C ANISOU 2847 C TYR A 350 29130 25711 22526 -2083 -4592 -7072 C ATOM 2848 O TYR A 350 26.560 24.695 9.146 1.00209.16 O ANISOU 2848 O TYR A 350 30133 26505 22835 -1680 -4277 -7508 O ATOM 2849 CB TYR A 350 26.805 26.926 10.924 1.00199.79 C ANISOU 2849 CB TYR A 350 27969 25804 22139 -1760 -3505 -6277 C ATOM 2850 CG TYR A 350 26.471 28.260 10.312 1.00206.19 C ANISOU 2850 CG TYR A 350 28591 27270 22481 -1886 -3388 -5835 C ATOM 2851 CD1 TYR A 350 25.181 28.531 9.864 1.00211.96 C ANISOU 2851 CD1 TYR A 350 29275 28075 23187 -2261 -3886 -5591 C ATOM 2852 CD2 TYR A 350 27.434 29.245 10.176 1.00206.11 C ANISOU 2852 CD2 TYR A 350 28444 27795 22074 -1643 -2809 -5638 C ATOM 2853 CE1 TYR A 350 24.861 29.749 9.301 1.00213.45 C ANISOU 2853 CE1 TYR A 350 29311 28829 22960 -2345 -3812 -5164 C ATOM 2854 CE2 TYR A 350 27.127 30.465 9.614 1.00207.09 C ANISOU 2854 CE2 TYR A 350 28436 28459 21789 -1771 -2730 -5199 C ATOM 2855 CZ TYR A 350 25.841 30.709 9.178 1.00211.21 C ANISOU 2855 CZ TYR A 350 28943 29018 22288 -2099 -3234 -4967 C ATOM 2856 OH TYR A 350 25.534 31.929 8.616 1.00213.06 O ANISOU 2856 OH TYR A 350 29065 29764 22125 -2193 -3181 -4508 O ATOM 2857 N ASN A 351 24.317 24.890 9.206 1.00204.44 N ANISOU 2857 N ASN A 351 29254 25730 22692 -2511 -5117 -6957 N ATOM 2858 CA ASN A 351 24.076 24.032 8.053 1.00210.04 C ANISOU 2858 CA ASN A 351 30363 26406 23036 -2556 -5390 -7403 C ATOM 2859 C ASN A 351 24.328 24.735 6.726 1.00211.39 C ANISOU 2859 C ASN A 351 30740 27298 22280 -2407 -5299 -7560 C ATOM 2860 O ASN A 351 24.513 24.056 5.709 1.00217.83 O ANISOU 2860 O ASN A 351 31957 28154 22654 -2306 -5374 -8024 O ATOM 2861 CB ASN A 351 22.636 23.516 8.096 1.00212.52 C ANISOU 2861 CB ASN A 351 30524 26410 23813 -3082 -5974 -7203 C ATOM 2862 CG ASN A 351 21.622 24.643 8.223 1.00206.42 C ANISOU 2862 CG ASN A 351 29298 26027 23104 -3407 -6190 -6611 C ATOM 2863 OD1 ASN A 351 21.985 25.785 8.510 1.00199.78 O ANISOU 2863 OD1 ASN A 351 28264 25562 22081 -3270 -5920 -6302 O ATOM 2864 ND2 ASN A 351 20.350 24.327 8.016 1.00208.04 N ANISOU 2864 ND2 ASN A 351 29324 26141 23581 -3820 -6679 -6432 N ATOM 2865 N GLN A 352 24.328 26.069 6.724 1.00207.17 N ANISOU 2865 N GLN A 352 29948 27323 21444 -2395 -5144 -7162 N ATOM 2866 CA GLN A 352 24.531 26.959 5.577 1.00209.05 C ANISOU 2866 CA GLN A 352 30321 28303 20804 -2280 -5025 -7130 C ATOM 2867 C GLN A 352 23.362 26.963 4.601 1.00210.86 C ANISOU 2867 C GLN A 352 30621 28748 20750 -2650 -5579 -7077 C ATOM 2868 O GLN A 352 23.499 27.520 3.501 1.00212.59 O ANISOU 2868 O GLN A 352 31054 29537 20184 -2578 -5536 -7082 O ATOM 2869 CB GLN A 352 25.821 26.639 4.815 1.00212.63 C ANISOU 2869 CB GLN A 352 31161 28989 20638 -1814 -4544 -7580 C ATOM 2870 CG GLN A 352 27.085 26.801 5.650 1.00207.10 C ANISOU 2870 CG GLN A 352 30276 28288 20125 -1401 -3911 -7599 C ATOM 2871 CD GLN A 352 27.358 28.244 6.032 1.00200.70 C ANISOU 2871 CD GLN A 352 29023 28072 19161 -1389 -3527 -7101 C ATOM 2872 OE1 GLN A 352 28.160 28.925 5.396 1.00202.48 O ANISOU 2872 OE1 GLN A 352 29264 28904 18764 -1160 -3067 -7023 O ATOM 2873 NE2 GLN A 352 26.695 28.714 7.075 1.00193.53 N ANISOU 2873 NE2 GLN A 352 27703 26887 18941 -1683 -3594 -6518 N ATOM 2874 N ASN A 353 22.221 26.381 4.957 1.00207.68 N ANISOU 2874 N ASN A 353 30008 27937 20965 -3027 -6078 -6985 N ATOM 2875 CA ASN A 353 21.015 26.571 4.162 1.00209.84 C ANISOU 2875 CA ASN A 353 30158 28497 21073 -3338 -6604 -6840 C ATOM 2876 C ASN A 353 20.452 27.961 4.425 1.00212.39 C ANISOU 2876 C ASN A 353 30070 29217 21410 -3423 -6667 -6157 C ATOM 2877 O ASN A 353 20.215 28.330 5.579 1.00210.61 O ANISOU 2877 O ASN A 353 29499 28718 21805 -3551 -6599 -5695 O ATOM 2878 CB ASN A 353 19.973 25.509 4.504 1.00205.44 C ANISOU 2878 CB ASN A 353 29473 27363 21220 -3702 -7086 -6889 C ATOM 2879 CG ASN A 353 20.456 24.107 4.224 1.00201.43 C ANISOU 2879 CG ASN A 353 29425 26383 20727 -3620 -7090 -7528 C ATOM 2880 OD1 ASN A 353 21.608 23.900 3.842 1.00198.54 O ANISOU 2880 OD1 ASN A 353 29453 26089 19894 -3250 -6699 -7935 O ATOM 2881 ND2 ASN A 353 19.579 23.132 4.419 1.00201.56 N ANISOU 2881 ND2 ASN A 353 29393 25896 21293 -3949 -7524 -7589 N ATOM 2882 N ASP A 354 20.247 28.732 3.356 1.00224.95 N ANISOU 2882 N ASP A 354 31728 31432 22312 -3353 -6783 -6047 N ATOM 2883 CA ASP A 354 19.729 30.095 3.489 1.00226.47 C ANISOU 2883 CA ASP A 354 31616 31971 22462 -3441 -6821 -5307 C ATOM 2884 C ASP A 354 18.461 30.186 4.333 1.00225.17 C ANISOU 2884 C ASP A 354 30934 31505 23114 -3814 -7174 -4783 C ATOM 2885 O ASP A 354 18.413 31.045 5.229 1.00220.28 O ANISOU 2885 O ASP A 354 29984 30902 22810 -3893 -6947 -4210 O ATOM 2886 CB ASP A 354 19.495 30.700 2.097 1.00236.63 C ANISOU 2886 CB ASP A 354 33086 33877 22945 -3322 -7011 -5263 C ATOM 2887 CG ASP A 354 19.436 32.224 2.119 1.00234.90 C ANISOU 2887 CG ASP A 354 32663 34108 22480 -3337 -6797 -4505 C ATOM 2888 OD1 ASP A 354 19.946 32.855 1.168 1.00239.24 O ANISOU 2888 OD1 ASP A 354 33474 35164 22263 -3119 -6601 -4454 O ATOM 2889 OD2 ASP A 354 18.897 32.796 3.090 1.00229.65 O ANISOU 2889 OD2 ASP A 354 31560 33303 22394 -3556 -6792 -3944 O ATOM 2890 N PRO A 355 17.417 29.369 4.121 1.00225.31 N ANISOU 2890 N PRO A 355 30819 31297 23491 -4067 -7673 -4919 N ATOM 2891 CA PRO A 355 16.195 29.556 4.928 1.00219.33 C ANISOU 2891 CA PRO A 355 29494 30350 23492 -4390 -7938 -4346 C ATOM 2892 C PRO A 355 16.416 29.372 6.420 1.00205.21 C ANISOU 2892 C PRO A 355 27439 28084 22448 -4468 -7635 -4119 C ATOM 2893 O PRO A 355 15.957 30.199 7.219 1.00201.21 O ANISOU 2893 O PRO A 355 26476 27653 22323 -4555 -7535 -3496 O ATOM 2894 CB PRO A 355 15.235 28.501 4.357 1.00229.53 C ANISOU 2894 CB PRO A 355 30783 31470 24958 -4655 -8467 -4650 C ATOM 2895 CG PRO A 355 15.741 28.219 2.994 1.00237.54 C ANISOU 2895 CG PRO A 355 32313 32800 25140 -4466 -8560 -5230 C ATOM 2896 CD PRO A 355 17.231 28.315 3.106 1.00233.87 C ANISOU 2896 CD PRO A 355 32224 32359 24278 -4109 -8001 -5541 C ATOM 2897 N ASN A 356 17.109 28.303 6.822 1.00194.48 N ANISOU 2897 N ASN A 356 26345 26244 21306 -4415 -7472 -4599 N ATOM 2898 CA ASN A 356 17.360 28.092 8.243 1.00180.25 C ANISOU 2898 CA ASN A 356 24311 23981 20195 -4463 -7184 -4381 C ATOM 2899 C ASN A 356 18.364 29.098 8.791 1.00166.16 C ANISOU 2899 C ASN A 356 22530 22389 18214 -4208 -6660 -4152 C ATOM 2900 O ASN A 356 18.311 29.439 9.978 1.00159.01 O ANISOU 2900 O ASN A 356 21217 21317 17882 -4197 -6314 -3702 O ATOM 2901 CB ASN A 356 17.871 26.672 8.501 1.00178.47 C ANISOU 2901 CB ASN A 356 24399 23170 20242 -4439 -7142 -4924 C ATOM 2902 CG ASN A 356 17.065 25.604 7.775 1.00179.71 C ANISOU 2902 CG ASN A 356 24684 23145 20452 -4689 -7615 -5238 C ATOM 2903 OD1 ASN A 356 17.586 24.531 7.464 1.00180.42 O ANISOU 2903 OD1 ASN A 356 25200 22894 20459 -4612 -7626 -5796 O ATOM 2904 ND2 ASN A 356 15.795 25.889 7.505 1.00181.48 N ANISOU 2904 ND2 ASN A 356 24544 23590 20819 -4982 -8009 -4874 N ATOM 2905 N ARG A 357 19.271 29.589 7.942 1.00160.16 N ANISOU 2905 N ARG A 357 22106 22039 16710 -3881 -6360 -4386 N ATOM 2906 CA ARG A 357 20.389 30.395 8.422 1.00151.86 C ANISOU 2906 CA ARG A 357 20983 21170 15548 -3514 -5605 -4190 C ATOM 2907 C ARG A 357 19.916 31.713 9.023 1.00148.09 C ANISOU 2907 C ARG A 357 20012 20935 15320 -3532 -5368 -3421 C ATOM 2908 O ARG A 357 20.343 32.092 10.118 1.00136.41 O ANISOU 2908 O ARG A 357 18277 19291 14261 -3404 -4895 -3132 O ATOM 2909 CB ARG A 357 21.373 30.652 7.281 1.00150.06 C ANISOU 2909 CB ARG A 357 21182 21404 14431 -3215 -5368 -4559 C ATOM 2910 N CYS A 358 19.014 32.411 8.327 1.00152.78 N ANISOU 2910 N CYS A 358 20483 21906 15660 -3673 -5723 -3095 N ATOM 2911 CA CYS A 358 18.683 33.793 8.671 1.00151.74 C ANISOU 2911 CA CYS A 358 19980 22054 15622 -3595 -5488 -2408 C ATOM 2912 C CYS A 358 18.227 33.924 10.121 1.00142.93 C ANISOU 2912 C CYS A 358 18376 20603 15328 -3648 -5304 -1995 C ATOM 2913 O CYS A 358 18.816 34.676 10.906 1.00132.84 O ANISOU 2913 O CYS A 358 16954 19304 14216 -3433 -4768 -1709 O ATOM 2914 CB CYS A 358 17.608 34.320 7.719 1.00161.53 C ANISOU 2914 CB CYS A 358 21142 23685 16547 -3752 -6027 -2140 C ATOM 2915 SG CYS A 358 16.012 33.489 7.856 1.00174.82 S ANISOU 2915 SG CYS A 358 22488 25159 18778 -4185 -6805 -2091 S ATOM 2916 N GLU A 359 17.173 33.196 10.497 1.00143.92 N ANISOU 2916 N GLU A 359 18240 20481 15961 -3950 -5751 -1954 N ATOM 2917 CA GLU A 359 16.641 33.336 11.849 1.00140.03 C ANISOU 2917 CA GLU A 359 17250 19754 16202 -4005 -5573 -1520 C ATOM 2918 C GLU A 359 17.594 32.753 12.887 1.00132.51 C ANISOU 2918 C GLU A 359 16388 18383 15576 -3888 -5114 -1725 C ATOM 2919 O GLU A 359 17.735 33.308 13.984 1.00122.94 O ANISOU 2919 O GLU A 359 14891 17095 14725 -3747 -4690 -1368 O ATOM 2920 CB GLU A 359 15.263 32.681 11.945 1.00147.22 C ANISOU 2920 CB GLU A 359 17814 20564 17557 -4401 -6168 -1384 C ATOM 2921 CG GLU A 359 14.553 32.944 13.264 1.00146.06 C ANISOU 2921 CG GLU A 359 17077 20311 18107 -4452 -5984 -856 C ATOM 2922 CD GLU A 359 13.092 32.540 13.231 1.00154.45 C ANISOU 2922 CD GLU A 359 17688 21440 19556 -4843 -6566 -604 C ATOM 2923 OE1 GLU A 359 12.261 33.261 13.823 1.00154.58 O ANISOU 2923 OE1 GLU A 359 17153 21675 19906 -4797 -6492 -59 O ATOM 2924 OE2 GLU A 359 12.774 31.506 12.607 1.00161.68 O ANISOU 2924 OE2 GLU A 359 18809 22178 20445 -5070 -6950 -969 O ATOM 2925 N LEU A 360 18.255 31.635 12.567 1.00133.45 N ANISOU 2925 N LEU A 360 16917 18224 15565 -3917 -5208 -2306 N ATOM 2926 CA LEU A 360 19.232 31.069 13.494 1.00125.62 C ANISOU 2926 CA LEU A 360 16032 16844 14854 -3760 -4792 -2508 C ATOM 2927 C LEU A 360 20.414 32.009 13.680 1.00125.16 C ANISOU 2927 C LEU A 360 16046 17010 14499 -3384 -4160 -2430 C ATOM 2928 O LEU A 360 20.961 32.129 14.782 1.00123.40 O ANISOU 2928 O LEU A 360 15678 16592 14617 -3246 -3741 -2279 O ATOM 2929 CB LEU A 360 19.713 29.707 12.991 1.00125.48 C ANISOU 2929 CB LEU A 360 16477 16479 14719 -3806 -5054 -3180 C ATOM 2930 CG LEU A 360 20.852 29.052 13.780 1.00118.20 C ANISOU 2930 CG LEU A 360 15733 15164 14015 -3574 -4658 -3457 C ATOM 2931 CD1 LEU A 360 20.399 28.672 15.182 1.00110.99 C ANISOU 2931 CD1 LEU A 360 14476 13842 13852 -3751 -4610 -3101 C ATOM 2932 CD2 LEU A 360 21.405 27.841 13.042 1.00121.70 C ANISOU 2932 CD2 LEU A 360 16705 15322 14214 -3512 -4914 -4183 C ATOM 2933 N LEU A 361 20.814 32.690 12.608 1.00128.39 N ANISOU 2933 N LEU A 361 16675 17845 14262 -3242 -4103 -2508 N ATOM 2934 CA LEU A 361 21.930 33.624 12.683 1.00125.87 C ANISOU 2934 CA LEU A 361 16413 17770 13640 -2948 -3532 -2397 C ATOM 2935 C LEU A 361 21.608 34.804 13.587 1.00113.37 C ANISOU 2935 C LEU A 361 14449 16241 12385 -2903 -3262 -1779 C ATOM 2936 O LEU A 361 22.412 35.179 14.447 1.00107.75 O ANISOU 2936 O LEU A 361 13664 15428 11847 -2733 -2795 -1672 O ATOM 2937 CB LEU A 361 22.284 34.107 11.283 1.00133.85 C ANISOU 2937 CB LEU A 361 17724 19261 13870 -2865 -3571 -2539 C ATOM 2938 CG LEU A 361 23.497 33.410 10.687 1.00138.83 C ANISOU 2938 CG LEU A 361 18750 19953 14046 -2663 -3365 -3135 C ATOM 2939 CD1 LEU A 361 24.502 34.486 10.407 1.00137.98 C ANISOU 2939 CD1 LEU A 361 18671 20265 13490 -2458 -2852 -2935 C ATOM 2940 CD2 LEU A 361 24.078 32.368 11.639 1.00140.75 C ANISOU 2940 CD2 LEU A 361 19005 19704 14769 -2573 -3206 -3458 C ATOM 2941 N SER A 362 20.438 35.413 13.391 1.00112.00 N ANISOU 2941 N SER A 362 14035 16232 12288 -3032 -3568 -1384 N ATOM 2942 CA SER A 362 20.059 36.566 14.197 1.00108.84 C ANISOU 2942 CA SER A 362 13297 15876 12181 -2932 -3337 -825 C ATOM 2943 C SER A 362 20.036 36.213 15.677 1.00107.81 C ANISOU 2943 C SER A 362 12901 15385 12677 -2920 -3099 -721 C ATOM 2944 O SER A 362 20.530 36.978 16.514 1.00105.68 O ANISOU 2944 O SER A 362 12536 15069 12549 -2736 -2679 -489 O ATOM 2945 CB SER A 362 18.700 37.090 13.744 1.00112.68 C ANISOU 2945 CB SER A 362 13532 16584 12697 -3044 -3766 -455 C ATOM 2946 OG SER A 362 17.672 36.166 14.047 1.00117.21 O ANISOU 2946 OG SER A 362 13850 16987 13698 -3295 -4164 -485 O ATOM 2947 N PHE A 363 19.486 35.045 16.017 1.00106.60 N ANISOU 2947 N PHE A 363 12652 14964 12887 -3134 -3379 -887 N ATOM 2948 CA PHE A 363 19.489 34.605 17.408 1.00 98.64 C ANISOU 2948 CA PHE A 363 11419 13625 12434 -3145 -3159 -776 C ATOM 2949 C PHE A 363 20.910 34.370 17.908 1.00 93.43 C ANISOU 2949 C PHE A 363 11007 12776 11717 -2943 -2724 -1048 C ATOM 2950 O PHE A 363 21.301 34.883 18.963 1.00 95.85 O ANISOU 2950 O PHE A 363 11168 13007 12242 -2789 -2338 -825 O ATOM 2951 CB PHE A 363 18.650 33.337 17.567 1.00105.38 C ANISOU 2951 CB PHE A 363 12157 14214 13669 -3471 -3584 -881 C ATOM 2952 CG PHE A 363 18.957 32.568 18.819 1.00110.99 C ANISOU 2952 CG PHE A 363 12792 14531 14849 -3500 -3373 -887 C ATOM 2953 CD1 PHE A 363 18.566 33.049 20.059 1.00109.64 C ANISOU 2953 CD1 PHE A 363 12241 14356 15062 -3444 -3096 -445 C ATOM 2954 CD2 PHE A 363 19.647 31.368 18.759 1.00113.58 C ANISOU 2954 CD2 PHE A 363 13451 14496 15209 -3553 -3456 -1337 C ATOM 2955 CE1 PHE A 363 18.855 32.345 21.217 1.00104.29 C ANISOU 2955 CE1 PHE A 363 11510 13348 14766 -3475 -2906 -418 C ATOM 2956 CE2 PHE A 363 19.937 30.659 19.911 1.00110.61 C ANISOU 2956 CE2 PHE A 363 13024 13742 15259 -3572 -3287 -1302 C ATOM 2957 CZ PHE A 363 19.541 31.148 21.142 1.00105.40 C ANISOU 2957 CZ PHE A 363 11981 13112 14954 -3551 -3013 -825 C ATOM 2958 N LEU A 364 21.701 33.589 17.166 1.00 95.12 N ANISOU 2958 N LEU A 364 11588 12926 11626 -2921 -2791 -1546 N ATOM 2959 CA LEU A 364 23.070 33.317 17.596 1.00 80.64 C ANISOU 2959 CA LEU A 364 9945 10950 9743 -2698 -2393 -1814 C ATOM 2960 C LEU A 364 23.898 34.589 17.674 1.00 81.63 C ANISOU 2960 C LEU A 364 10054 11362 9601 -2478 -1945 -1608 C ATOM 2961 O LEU A 364 24.802 34.690 18.510 1.00 84.35 O ANISOU 2961 O LEU A 364 10373 11594 10082 -2322 -1574 -1609 O ATOM 2962 CB LEU A 364 23.742 32.321 16.652 1.00 89.56 C ANISOU 2962 CB LEU A 364 11468 12024 10538 -2649 -2543 -2408 C ATOM 2963 CG LEU A 364 23.408 30.848 16.892 1.00 87.56 C ANISOU 2963 CG LEU A 364 11329 11297 10644 -2806 -2890 -2716 C ATOM 2964 CD1 LEU A 364 24.173 29.965 15.922 1.00 91.91 C ANISOU 2964 CD1 LEU A 364 12322 11790 10809 -2666 -3006 -3359 C ATOM 2965 CD2 LEU A 364 23.705 30.459 18.332 1.00 85.60 C ANISOU 2965 CD2 LEU A 364 10916 10676 10934 -2762 -2654 -2555 C ATOM 2966 N LEU A 365 23.614 35.565 16.813 1.00 79.14 N ANISOU 2966 N LEU A 365 9760 11402 8907 -2482 -2001 -1415 N ATOM 2967 CA LEU A 365 24.357 36.819 16.852 1.00 79.22 C ANISOU 2967 CA LEU A 365 9776 11642 8683 -2327 -1616 -1174 C ATOM 2968 C LEU A 365 24.031 37.601 18.117 1.00 71.73 C ANISOU 2968 C LEU A 365 8549 10541 8166 -2274 -1415 -750 C ATOM 2969 O LEU A 365 24.933 38.107 18.795 1.00 70.88 O ANISOU 2969 O LEU A 365 8440 10388 8105 -2147 -1042 -687 O ATOM 2970 CB LEU A 365 24.049 37.645 15.604 1.00 82.94 C ANISOU 2970 CB LEU A 365 10365 12496 8651 -2363 -1772 -1022 C ATOM 2971 CG LEU A 365 24.934 38.866 15.367 1.00 82.54 C ANISOU 2971 CG LEU A 365 10402 12695 8265 -2256 -1412 -798 C ATOM 2972 CD1 LEU A 365 26.391 38.460 15.176 1.00 77.86 C ANISOU 2972 CD1 LEU A 365 9983 12205 7395 -2154 -1070 -1157 C ATOM 2973 CD2 LEU A 365 24.423 39.630 14.162 1.00 90.18 C ANISOU 2973 CD2 LEU A 365 11487 14009 8770 -2316 -1638 -575 C ATOM 2974 N VAL A 366 22.741 37.708 18.449 1.00 72.27 N ANISOU 2974 N VAL A 366 8368 10551 8542 -2363 -1665 -465 N ATOM 2975 CA VAL A 366 22.337 38.345 19.702 1.00 81.36 C ANISOU 2975 CA VAL A 366 9248 11570 10096 -2271 -1472 -103 C ATOM 2976 C VAL A 366 22.970 37.627 20.887 1.00 66.13 C ANISOU 2976 C VAL A 366 7284 9355 8486 -2232 -1228 -248 C ATOM 2977 O VAL A 366 23.492 38.259 21.812 1.00 65.54 O ANISOU 2977 O VAL A 366 7166 9210 8528 -2087 -903 -104 O ATOM 2978 CB VAL A 366 20.802 38.379 19.820 1.00 79.24 C ANISOU 2978 CB VAL A 366 8659 11342 10106 -2362 -1787 194 C ATOM 2979 CG1 VAL A 366 20.381 38.844 21.209 1.00 68.42 C ANISOU 2979 CG1 VAL A 366 6995 9852 9149 -2232 -1552 510 C ATOM 2980 CG2 VAL A 366 20.213 39.284 18.753 1.00 73.98 C ANISOU 2980 CG2 VAL A 366 8010 10967 9132 -2342 -2016 406 C ATOM 2981 N LEU A 367 22.942 36.292 20.872 1.00 67.72 N ANISOU 2981 N LEU A 367 7533 9367 8829 -2362 -1413 -535 N ATOM 2982 CA LEU A 367 23.553 35.530 21.955 1.00 65.53 C ANISOU 2982 CA LEU A 367 7251 8798 8851 -2319 -1222 -655 C ATOM 2983 C LEU A 367 25.057 35.775 22.026 1.00 70.36 C ANISOU 2983 C LEU A 367 8061 9438 9236 -2128 -875 -864 C ATOM 2984 O LEU A 367 25.621 35.904 23.118 1.00 60.30 O ANISOU 2984 O LEU A 367 6720 8035 8158 -2018 -606 -782 O ATOM 2985 CB LEU A 367 23.257 34.043 21.779 1.00 72.12 C ANISOU 2985 CB LEU A 367 8161 9373 9870 -2501 -1539 -929 C ATOM 2986 CG LEU A 367 23.731 33.126 22.905 1.00 70.65 C ANISOU 2986 CG LEU A 367 7974 8832 10038 -2478 -1416 -1001 C ATOM 2987 CD1 LEU A 367 23.149 33.561 24.240 1.00 64.67 C ANISOU 2987 CD1 LEU A 367 6903 8042 9627 -2479 -1238 -561 C ATOM 2988 CD2 LEU A 367 23.352 31.695 22.593 1.00 73.66 C ANISOU 2988 CD2 LEU A 367 8479 8899 10608 -2688 -1800 -1257 C ATOM 2989 N ASP A 368 25.722 35.852 20.869 1.00 69.24 N ANISOU 2989 N ASP A 368 8143 9504 8660 -2090 -878 -1123 N ATOM 2990 CA ASP A 368 27.163 36.100 20.861 1.00 69.57 C ANISOU 2990 CA ASP A 368 8307 9651 8475 -1925 -537 -1298 C ATOM 2991 C ASP A 368 27.492 37.463 21.457 1.00 65.66 C ANISOU 2991 C ASP A 368 7706 9263 7977 -1861 -246 -951 C ATOM 2992 O ASP A 368 28.463 37.600 22.210 1.00 63.83 O ANISOU 2992 O ASP A 368 7450 8975 7828 -1760 29 -976 O ATOM 2993 CB ASP A 368 27.711 35.998 19.437 1.00 67.24 C ANISOU 2993 CB ASP A 368 8240 9648 7661 -1899 -572 -1598 C ATOM 2994 CG ASP A 368 29.219 35.786 19.402 1.00 70.87 C ANISOU 2994 CG ASP A 368 8784 10215 7930 -1718 -248 -1880 C ATOM 2995 OD1 ASP A 368 29.659 34.626 19.539 1.00 68.33 O ANISOU 2995 OD1 ASP A 368 8545 9698 7721 -1610 -286 -2246 O ATOM 2996 OD2 ASP A 368 29.965 36.775 19.238 1.00 66.21 O ANISOU 2996 OD2 ASP A 368 8166 9898 7094 -1685 33 -1724 O ATOM 2997 N TYR A 369 26.696 38.484 21.129 1.00 63.80 N ANISOU 2997 N TYR A 369 7421 9163 7657 -1915 -333 -629 N ATOM 2998 CA TYR A 369 26.949 39.822 21.655 1.00 59.29 C ANISOU 2998 CA TYR A 369 6807 8624 7095 -1850 -104 -311 C ATOM 2999 C TYR A 369 26.725 39.878 23.160 1.00 58.82 C ANISOU 2999 C TYR A 369 6584 8311 7455 -1771 18 -160 C ATOM 3000 O TYR A 369 27.546 40.436 23.899 1.00 53.55 O ANISOU 3000 O TYR A 369 5933 7585 6827 -1697 269 -113 O ATOM 3001 CB TYR A 369 26.061 40.838 20.945 1.00 61.98 C ANISOU 3001 CB TYR A 369 7156 9118 7276 -1882 -272 -1 C ATOM 3002 CG TYR A 369 26.670 41.372 19.679 1.00 68.07 C ANISOU 3002 CG TYR A 369 8130 10180 7555 -1937 -247 -15 C ATOM 3003 CD1 TYR A 369 27.873 42.061 19.712 1.00 68.99 C ANISOU 3003 CD1 TYR A 369 8340 10382 7492 -1934 53 21 C ATOM 3004 CD2 TYR A 369 26.046 41.193 18.453 1.00 69.10 C ANISOU 3004 CD2 TYR A 369 8347 10528 7381 -2016 -532 -42 C ATOM 3005 CE1 TYR A 369 28.441 42.553 18.561 1.00 69.68 C ANISOU 3005 CE1 TYR A 369 8587 10778 7109 -2013 107 61 C ATOM 3006 CE2 TYR A 369 26.606 41.684 17.295 1.00 71.95 C ANISOU 3006 CE2 TYR A 369 8903 11200 7233 -2066 -490 -26 C ATOM 3007 CZ TYR A 369 27.803 42.363 17.356 1.00 72.99 C ANISOU 3007 CZ TYR A 369 9111 11428 7194 -2067 -152 42 C ATOM 3008 OH TYR A 369 28.373 42.856 16.209 1.00 78.20 O ANISOU 3008 OH TYR A 369 9942 12441 7331 -2145 -80 108 O ATOM 3009 N ILE A 370 25.599 39.332 23.627 1.00 59.85 N ANISOU 3009 N ILE A 370 6544 8317 7881 -1800 -165 -66 N ATOM 3010 CA ILE A 370 25.404 39.157 25.062 1.00 62.38 C ANISOU 3010 CA ILE A 370 6706 8438 8557 -1729 -33 54 C ATOM 3011 C ILE A 370 26.588 38.414 25.655 1.00 59.04 C ANISOU 3011 C ILE A 370 6368 7879 8187 -1691 137 -196 C ATOM 3012 O ILE A 370 27.121 38.796 26.701 1.00 50.67 O ANISOU 3012 O ILE A 370 5287 6736 7230 -1590 354 -121 O ATOM 3013 CB ILE A 370 24.082 38.417 25.336 1.00 62.18 C ANISOU 3013 CB ILE A 370 6456 8348 8823 -1825 -262 179 C ATOM 3014 CG1 ILE A 370 22.893 39.264 24.889 1.00 57.26 C ANISOU 3014 CG1 ILE A 370 5679 7897 8182 -1809 -417 469 C ATOM 3015 CG2 ILE A 370 23.966 38.054 26.804 1.00 53.99 C ANISOU 3015 CG2 ILE A 370 5267 7142 8106 -1770 -102 300 C ATOM 3016 CD1 ILE A 370 21.580 38.529 24.960 1.00 59.75 C ANISOU 3016 CD1 ILE A 370 5713 8225 8764 -1951 -679 605 C ATOM 3017 N GLY A 371 27.045 37.367 24.964 1.00 59.31 N ANISOU 3017 N GLY A 371 6513 7892 8129 -1748 23 -512 N ATOM 3018 CA GLY A 371 28.139 36.561 25.479 1.00 59.53 C ANISOU 3018 CA GLY A 371 6605 7781 8231 -1664 152 -759 C ATOM 3019 C GLY A 371 29.405 37.359 25.725 1.00 57.90 C ANISOU 3019 C GLY A 371 6438 7704 7859 -1555 442 -777 C ATOM 3020 O GLY A 371 30.037 37.233 26.777 1.00 61.88 O ANISOU 3020 O GLY A 371 6895 8091 8527 -1469 588 -770 O ATOM 3021 N ILE A 372 29.800 38.191 24.759 1.00 52.30 N ANISOU 3021 N ILE A 372 5807 7249 6814 -1583 510 -776 N ATOM 3022 CA ILE A 372 31.039 38.939 24.942 1.00 58.48 C ANISOU 3022 CA ILE A 372 6597 8168 7453 -1543 769 -768 C ATOM 3023 C ILE A 372 30.855 40.064 25.946 1.00 58.95 C ANISOU 3023 C ILE A 372 6613 8126 7660 -1542 869 -464 C ATOM 3024 O ILE A 372 31.842 40.573 26.491 1.00 59.09 O ANISOU 3024 O ILE A 372 6619 8165 7667 -1530 1046 -450 O ATOM 3025 CB ILE A 372 31.580 39.494 23.611 1.00 65.29 C ANISOU 3025 CB ILE A 372 7553 9357 7896 -1609 834 -814 C ATOM 3026 CG1 ILE A 372 30.825 40.757 23.203 1.00 70.96 C ANISOU 3026 CG1 ILE A 372 8325 10141 8494 -1711 770 -476 C ATOM 3027 CG2 ILE A 372 31.504 38.446 22.517 1.00 62.94 C ANISOU 3027 CG2 ILE A 372 7347 9176 7392 -1585 696 -1135 C ATOM 3028 CD1 ILE A 372 31.520 41.525 22.110 1.00 81.68 C ANISOU 3028 CD1 ILE A 372 9777 11814 9442 -1809 882 -414 C ATOM 3029 N ASN A 373 29.609 40.464 26.204 1.00 58.55 N ANISOU 3029 N ASN A 373 6529 7973 7743 -1544 748 -232 N ATOM 3030 CA ASN A 373 29.339 41.438 27.253 1.00 55.33 C ANISOU 3030 CA ASN A 373 6100 7439 7482 -1474 841 7 C ATOM 3031 C ASN A 373 29.487 40.809 28.634 1.00 61.08 C ANISOU 3031 C ASN A 373 6745 7999 8463 -1385 917 -33 C ATOM 3032 O ASN A 373 30.115 41.392 29.524 1.00 65.73 O ANISOU 3032 O ASN A 373 7369 8526 9081 -1331 1054 4 O ATOM 3033 CB ASN A 373 27.941 42.028 27.069 1.00 51.91 C ANISOU 3033 CB ASN A 373 5623 6994 7105 -1440 703 256 C ATOM 3034 CG ASN A 373 27.900 43.103 26.003 1.00 55.67 C ANISOU 3034 CG ASN A 373 6228 7595 7330 -1492 652 398 C ATOM 3035 OD1 ASN A 373 28.821 43.913 25.886 1.00 49.49 O ANISOU 3035 OD1 ASN A 373 5576 6830 6397 -1542 776 428 O ATOM 3036 ND2 ASN A 373 26.831 43.117 25.218 1.00 55.19 N ANISOU 3036 ND2 ASN A 373 6122 7623 7225 -1504 446 516 N ATOM 3037 N MET A 374 28.929 39.608 28.826 1.00 62.34 N ANISOU 3037 N MET A 374 6812 8075 8800 -1389 805 -98 N ATOM 3038 CA MET A 374 29.089 38.918 30.104 1.00 56.88 C ANISOU 3038 CA MET A 374 6056 7228 8327 -1320 867 -96 C ATOM 3039 C MET A 374 30.556 38.615 30.380 1.00 58.19 C ANISOU 3039 C MET A 374 6280 7390 8440 -1275 975 -302 C ATOM 3040 O MET A 374 31.018 38.729 31.520 1.00 69.28 O ANISOU 3040 O MET A 374 7674 8727 9924 -1198 1075 -253 O ATOM 3041 CB MET A 374 28.282 37.619 30.124 1.00 60.12 C ANISOU 3041 CB MET A 374 6377 7519 8947 -1389 695 -104 C ATOM 3042 CG MET A 374 26.932 37.682 29.460 1.00 70.20 C ANISOU 3042 CG MET A 374 7552 8858 10262 -1488 519 43 C ATOM 3043 SD MET A 374 25.590 38.160 30.556 1.00 78.91 S ANISOU 3043 SD MET A 374 8429 9986 11569 -1427 580 419 S ATOM 3044 CE MET A 374 25.351 36.640 31.472 1.00 82.03 C ANISOU 3044 CE MET A 374 8718 10195 12255 -1530 522 467 C ATOM 3045 N ALA A 375 31.304 38.227 29.346 1.00 53.61 N ANISOU 3045 N ALA A 375 5747 6918 7704 -1304 956 -535 N ATOM 3046 CA ALA A 375 32.731 37.984 29.518 1.00 52.31 C ANISOU 3046 CA ALA A 375 5573 6818 7484 -1233 1073 -724 C ATOM 3047 C ALA A 375 33.467 39.258 29.923 1.00 52.84 C ANISOU 3047 C ALA A 375 5638 6997 7442 -1266 1226 -608 C ATOM 3048 O ALA A 375 34.339 39.217 30.796 1.00 60.94 O ANISOU 3048 O ALA A 375 6614 8005 8535 -1209 1296 -641 O ATOM 3049 CB ALA A 375 33.322 37.393 28.238 1.00 58.54 C ANISOU 3049 CB ALA A 375 6394 7765 8082 -1220 1057 -1004 C ATOM 3050 N SER A 376 33.130 40.401 29.315 1.00 51.72 N ANISOU 3050 N SER A 376 5563 6949 7141 -1370 1245 -460 N ATOM 3051 CA SER A 376 33.723 41.659 29.765 1.00 56.51 C ANISOU 3051 CA SER A 376 6213 7572 7686 -1436 1343 -328 C ATOM 3052 C SER A 376 33.363 41.938 31.219 1.00 59.77 C ANISOU 3052 C SER A 376 6652 7780 8277 -1342 1343 -218 C ATOM 3053 O SER A 376 34.196 42.428 31.988 1.00 42.06 O ANISOU 3053 O SER A 376 4426 5516 6038 -1360 1396 -224 O ATOM 3054 CB SER A 376 33.275 42.827 28.881 1.00 62.09 C ANISOU 3054 CB SER A 376 7032 8336 8222 -1553 1325 -146 C ATOM 3055 OG SER A 376 33.793 42.733 27.567 1.00 82.86 O ANISOU 3055 OG SER A 376 9655 11220 10609 -1659 1358 -222 O ATOM 3056 N LEU A 377 32.127 41.616 31.615 1.00 47.35 N ANISOU 3056 N LEU A 377 5069 6086 6834 -1249 1280 -115 N ATOM 3057 CA LEU A 377 31.703 41.855 32.989 1.00 48.60 C ANISOU 3057 CA LEU A 377 5246 6111 7107 -1128 1316 -5 C ATOM 3058 C LEU A 377 32.496 40.994 33.962 1.00 54.25 C ANISOU 3058 C LEU A 377 5909 6796 7906 -1073 1339 -108 C ATOM 3059 O LEU A 377 32.797 41.426 35.082 1.00 54.37 O ANISOU 3059 O LEU A 377 5983 6761 7916 -1007 1381 -73 O ATOM 3060 CB LEU A 377 30.205 41.589 33.129 1.00 52.47 C ANISOU 3060 CB LEU A 377 5664 6560 7713 -1047 1272 154 C ATOM 3061 CG LEU A 377 29.309 42.585 32.392 1.00 58.27 C ANISOU 3061 CG LEU A 377 6436 7319 8384 -1037 1231 299 C ATOM 3062 CD1 LEU A 377 27.878 42.084 32.322 1.00 61.26 C ANISOU 3062 CD1 LEU A 377 6648 7730 8897 -986 1158 447 C ATOM 3063 CD2 LEU A 377 29.369 43.949 33.065 1.00 56.41 C ANISOU 3063 CD2 LEU A 377 6358 6984 8092 -928 1304 380 C ATOM 3064 N ASN A 378 32.866 39.781 33.546 1.00 53.26 N ANISOU 3064 N ASN A 378 5699 6692 7846 -1080 1289 -245 N ATOM 3065 CA ASN A 378 33.629 38.913 34.430 1.00 54.18 C ANISOU 3065 CA ASN A 378 5770 6757 8060 -996 1280 -321 C ATOM 3066 C ASN A 378 34.990 39.507 34.765 1.00 54.52 C ANISOU 3066 C ASN A 378 5803 6905 8006 -1010 1330 -409 C ATOM 3067 O ASN A 378 35.547 39.212 35.827 1.00 63.52 O ANISOU 3067 O ASN A 378 6926 8013 9196 -931 1311 -408 O ATOM 3068 CB ASN A 378 33.796 37.526 33.803 1.00 57.18 C ANISOU 3068 CB ASN A 378 6096 7088 8542 -967 1192 -480 C ATOM 3069 CG ASN A 378 34.429 36.529 34.753 1.00 61.74 C ANISOU 3069 CG ASN A 378 6644 7554 9261 -844 1146 -514 C ATOM 3070 OD1 ASN A 378 33.805 36.083 35.717 1.00 71.18 O ANISOU 3070 OD1 ASN A 378 7856 8610 10580 -812 1110 -340 O ATOM 3071 ND2 ASN A 378 35.679 36.175 34.485 1.00 57.54 N ANISOU 3071 ND2 ASN A 378 6050 7109 8704 -763 1152 -715 N ATOM 3072 N SER A 379 35.541 40.342 33.887 1.00 48.28 N ANISOU 3072 N SER A 379 5014 6256 7074 -1134 1378 -458 N ATOM 3073 CA SER A 379 36.818 40.984 34.174 1.00 50.02 C ANISOU 3073 CA SER A 379 5187 6597 7223 -1214 1410 -504 C ATOM 3074 C SER A 379 36.706 42.108 35.198 1.00 48.42 C ANISOU 3074 C SER A 379 5128 6276 6993 -1255 1388 -388 C ATOM 3075 O SER A 379 37.735 42.669 35.591 1.00 53.71 O ANISOU 3075 O SER A 379 5774 7012 7623 -1358 1365 -420 O ATOM 3076 CB SER A 379 37.439 41.529 32.883 1.00 50.55 C ANISOU 3076 CB SER A 379 5194 6877 7137 -1378 1481 -545 C ATOM 3077 OG SER A 379 36.814 42.738 32.483 1.00 48.36 O ANISOU 3077 OG SER A 379 5074 6534 6766 -1515 1484 -384 O ATOM 3078 N CYS A 380 35.490 42.454 35.629 1.00 47.58 N ANISOU 3078 N CYS A 380 5164 6012 6904 -1171 1386 -267 N ATOM 3079 CA CYS A 380 35.285 43.441 36.681 1.00 53.43 C ANISOU 3079 CA CYS A 380 6082 6623 7596 -1131 1370 -206 C ATOM 3080 C CYS A 380 34.351 42.927 37.768 1.00 57.04 C ANISOU 3080 C CYS A 380 6571 7008 8094 -925 1394 -129 C ATOM 3081 O CYS A 380 33.987 43.689 38.669 1.00 54.11 O ANISOU 3081 O CYS A 380 6362 6551 7645 -826 1407 -96 O ATOM 3082 CB CYS A 380 34.725 44.746 36.108 1.00 52.02 C ANISOU 3082 CB CYS A 380 6074 6338 7352 -1198 1372 -117 C ATOM 3083 SG CYS A 380 32.975 44.696 35.659 1.00 54.03 S ANISOU 3083 SG CYS A 380 6339 6536 7654 -1035 1409 31 S ATOM 3084 N ALA A 381 33.960 41.660 37.712 1.00 57.55 N ANISOU 3084 N ALA A 381 6495 7103 8267 -860 1400 -98 N ATOM 3085 CA ALA A 381 32.908 41.192 38.597 1.00 55.15 C ANISOU 3085 CA ALA A 381 6189 6762 8005 -714 1445 49 C ATOM 3086 C ALA A 381 33.452 40.740 39.946 1.00 58.30 C ANISOU 3086 C ALA A 381 6619 7173 8360 -623 1427 60 C ATOM 3087 O ALA A 381 32.749 40.848 40.958 1.00 64.96 O ANISOU 3087 O ALA A 381 7525 8029 9128 -492 1497 184 O ATOM 3088 CB ALA A 381 32.125 40.064 37.919 1.00 52.46 C ANISOU 3088 CB ALA A 381 5699 6410 7822 -742 1423 123 C ATOM 3089 N ASN A 382 34.694 40.260 39.988 1.00 52.40 N ANISOU 3089 N ASN A 382 5818 6458 7635 -669 1339 -57 N ATOM 3090 CA ASN A 382 35.220 39.695 41.227 1.00 50.17 C ANISOU 3090 CA ASN A 382 5553 6196 7314 -573 1280 -19 C ATOM 3091 C ASN A 382 35.354 40.706 42.361 1.00 55.34 C ANISOU 3091 C ASN A 382 6390 6880 7755 -516 1277 -30 C ATOM 3092 O ASN A 382 35.001 40.351 43.500 1.00 56.25 O ANISOU 3092 O ASN A 382 6572 7028 7772 -386 1296 90 O ATOM 3093 CB ASN A 382 36.555 39.000 40.955 1.00 46.04 C ANISOU 3093 CB ASN A 382 4896 5721 6878 -598 1166 -148 C ATOM 3094 CG ASN A 382 36.390 37.743 40.131 1.00 51.03 C ANISOU 3094 CG ASN A 382 5405 6280 7705 -573 1146 -161 C ATOM 3095 OD1 ASN A 382 37.365 37.178 39.650 1.00 59.34 O ANISOU 3095 OD1 ASN A 382 6337 7373 8835 -545 1083 -302 O ATOM 3096 ND2 ASN A 382 35.149 37.296 39.964 1.00 48.44 N ANISOU 3096 ND2 ASN A 382 5100 5847 7459 -575 1190 -24 N ATOM 3097 N PRO A 383 35.846 41.935 42.156 1.00 52.75 N ANISOU 3097 N PRO A 383 6174 6535 7333 -612 1241 -162 N ATOM 3098 CA PRO A 383 35.808 42.902 43.266 1.00 48.67 C ANISOU 3098 CA PRO A 383 5898 5990 6605 -536 1214 -207 C ATOM 3099 C PRO A 383 34.421 43.078 43.859 1.00 55.47 C ANISOU 3099 C PRO A 383 6874 6840 7361 -325 1371 -89 C ATOM 3100 O PRO A 383 34.286 43.147 45.088 1.00 66.87 O ANISOU 3100 O PRO A 383 8459 8346 8603 -172 1385 -74 O ATOM 3101 CB PRO A 383 36.327 44.191 42.619 1.00 48.31 C ANISOU 3101 CB PRO A 383 5963 5846 6545 -716 1145 -340 C ATOM 3102 CG PRO A 383 37.228 43.721 41.536 1.00 53.12 C ANISOU 3102 CG PRO A 383 6331 6544 7308 -909 1105 -370 C ATOM 3103 CD PRO A 383 36.591 42.468 40.999 1.00 52.02 C ANISOU 3103 CD PRO A 383 6010 6451 7304 -809 1203 -274 C ATOM 3104 N ILE A 384 33.381 43.145 43.025 1.00 50.27 N ANISOU 3104 N ILE A 384 6139 6147 6816 -300 1490 3 N ATOM 3105 CA ILE A 384 32.021 43.242 43.551 1.00 53.18 C ANISOU 3105 CA ILE A 384 6526 6570 7111 -84 1659 144 C ATOM 3106 C ILE A 384 31.628 41.943 44.241 1.00 61.71 C ANISOU 3106 C ILE A 384 7451 7787 8209 -29 1726 349 C ATOM 3107 O ILE A 384 31.053 41.951 45.337 1.00 71.90 O ANISOU 3107 O ILE A 384 8802 9202 9313 152 1847 455 O ATOM 3108 CB ILE A 384 31.026 43.606 42.434 1.00 49.22 C ANISOU 3108 CB ILE A 384 5928 6024 6749 -83 1730 216 C ATOM 3109 CG1 ILE A 384 31.133 45.087 42.077 1.00 51.43 C ANISOU 3109 CG1 ILE A 384 6438 6143 6961 -58 1686 76 C ATOM 3110 CG2 ILE A 384 29.600 43.259 42.850 1.00 47.10 C ANISOU 3110 CG2 ILE A 384 5518 5895 6483 107 1907 428 C ATOM 3111 CD1 ILE A 384 32.090 45.373 40.949 1.00 56.24 C ANISOU 3111 CD1 ILE A 384 7050 6652 7667 -328 1548 -15 C ATOM 3112 N ALA A 385 31.941 40.807 43.614 1.00 57.12 N ANISOU 3112 N ALA A 385 6687 7177 7840 -180 1647 413 N ATOM 3113 CA ALA A 385 31.576 39.516 44.187 1.00 56.15 C ANISOU 3113 CA ALA A 385 6442 7107 7785 -168 1670 640 C ATOM 3114 C ALA A 385 32.226 39.311 45.552 1.00 64.09 C ANISOU 3114 C ALA A 385 7577 8195 8579 -71 1631 675 C ATOM 3115 O ALA A 385 31.574 38.853 46.498 1.00 71.43 O ANISOU 3115 O ALA A 385 8500 9247 9392 23 1738 907 O ATOM 3116 CB ALA A 385 31.965 38.389 43.228 1.00 49.07 C ANISOU 3116 CB ALA A 385 5397 6087 7161 -327 1540 632 C ATOM 3117 N LEU A 386 33.518 39.635 45.666 1.00 60.23 N ANISOU 3117 N LEU A 386 7187 7674 8024 -107 1469 469 N ATOM 3118 CA LEU A 386 34.214 39.488 46.941 1.00 61.79 C ANISOU 3118 CA LEU A 386 7512 7967 8000 -21 1376 487 C ATOM 3119 C LEU A 386 33.590 40.374 48.013 1.00 62.23 C ANISOU 3119 C LEU A 386 7780 8153 7713 155 1505 489 C ATOM 3120 O LEU A 386 33.436 39.955 49.167 1.00 60.37 O ANISOU 3120 O LEU A 386 7619 8067 7251 273 1540 649 O ATOM 3121 CB LEU A 386 35.700 39.815 46.770 1.00 48.02 C ANISOU 3121 CB LEU A 386 5785 6194 6265 -117 1157 255 C ATOM 3122 CG LEU A 386 36.519 38.926 45.831 1.00 54.20 C ANISOU 3122 CG LEU A 386 6348 6909 7335 -219 1039 215 C ATOM 3123 CD1 LEU A 386 37.957 39.414 45.716 1.00 53.58 C ANISOU 3123 CD1 LEU A 386 6227 6889 7243 -311 857 5 C ATOM 3124 CD2 LEU A 386 36.486 37.489 46.296 1.00 48.04 C ANISOU 3124 CD2 LEU A 386 5493 6101 6660 -137 983 431 C ATOM 3125 N TYR A 387 33.219 41.602 47.646 1.00 67.17 N ANISOU 3125 N TYR A 387 8523 8721 8276 196 1576 313 N ATOM 3126 CA TYR A 387 32.535 42.490 48.579 1.00 52.32 C ANISOU 3126 CA TYR A 387 6865 6941 6075 429 1715 264 C ATOM 3127 C TYR A 387 31.246 41.861 49.104 1.00 60.81 C ANISOU 3127 C TYR A 387 7806 8226 7074 591 1976 564 C ATOM 3128 O TYR A 387 30.951 41.941 50.302 1.00 78.09 O ANISOU 3128 O TYR A 387 10130 10619 8923 788 2088 625 O ATOM 3129 CB TYR A 387 32.256 43.827 47.889 1.00 53.23 C ANISOU 3129 CB TYR A 387 7116 6887 6223 461 1734 50 C ATOM 3130 CG TYR A 387 31.601 44.875 48.757 1.00 55.06 C ANISOU 3130 CG TYR A 387 7624 7160 6138 758 1858 -77 C ATOM 3131 CD1 TYR A 387 30.224 44.897 48.928 1.00 60.04 C ANISOU 3131 CD1 TYR A 387 8154 7950 6710 1014 2138 80 C ATOM 3132 CD2 TYR A 387 32.356 45.856 49.387 1.00 56.90 C ANISOU 3132 CD2 TYR A 387 8210 7275 6135 793 1685 -368 C ATOM 3133 CE1 TYR A 387 29.617 45.849 49.715 1.00 66.74 C ANISOU 3133 CE1 TYR A 387 9247 8859 7251 1357 2278 -66 C ATOM 3134 CE2 TYR A 387 31.754 46.821 50.179 1.00 61.58 C ANISOU 3134 CE2 TYR A 387 9108 7872 6418 1110 1787 -540 C ATOM 3135 CZ TYR A 387 30.382 46.809 50.338 1.00 70.19 C ANISOU 3135 CZ TYR A 387 10093 9140 7437 1422 2102 -396 C ATOM 3136 OH TYR A 387 29.757 47.755 51.119 1.00 80.26 O ANISOU 3136 OH TYR A 387 11658 10447 8390 1809 2235 -590 O ATOM 3137 N LEU A 388 30.470 41.221 48.230 1.00 54.01 N ANISOU 3137 N LEU A 388 6668 7345 6508 495 2070 763 N ATOM 3138 CA LEU A 388 29.153 40.739 48.637 1.00 56.96 C ANISOU 3138 CA LEU A 388 6857 7939 6846 604 2321 1074 C ATOM 3139 C LEU A 388 29.209 39.408 49.377 1.00 61.68 C ANISOU 3139 C LEU A 388 7357 8652 7425 516 2319 1394 C ATOM 3140 O LEU A 388 28.358 39.155 50.237 1.00 70.58 O ANISOU 3140 O LEU A 388 8415 10046 8355 635 2540 1661 O ATOM 3141 CB LEU A 388 28.240 40.604 47.419 1.00 53.07 C ANISOU 3141 CB LEU A 388 6095 7387 6683 502 2379 1177 C ATOM 3142 CG LEU A 388 27.835 41.898 46.714 1.00 52.55 C ANISOU 3142 CG LEU A 388 6093 7242 6632 632 2419 968 C ATOM 3143 CD1 LEU A 388 27.329 41.607 45.314 1.00 62.57 C ANISOU 3143 CD1 LEU A 388 7118 8409 8245 452 2358 1042 C ATOM 3144 CD2 LEU A 388 26.783 42.660 47.508 1.00 55.75 C ANISOU 3144 CD2 LEU A 388 6520 7879 6785 977 2682 1012 C ATOM 3145 N VAL A 389 30.191 38.553 49.070 1.00 60.49 N ANISOU 3145 N VAL A 389 7197 8317 7470 326 2081 1391 N ATOM 3146 CA VAL A 389 30.210 37.185 49.586 1.00 64.20 C ANISOU 3146 CA VAL A 389 7579 8801 8012 226 2034 1728 C ATOM 3147 C VAL A 389 31.157 36.994 50.765 1.00 64.77 C ANISOU 3147 C VAL A 389 7861 8959 7789 317 1909 1743 C ATOM 3148 O VAL A 389 31.040 35.982 51.476 1.00 60.12 O ANISOU 3148 O VAL A 389 7249 8433 7162 284 1903 2087 O ATOM 3149 CB VAL A 389 30.571 36.182 48.465 1.00 54.03 C ANISOU 3149 CB VAL A 389 6145 7221 7163 3 1835 1738 C ATOM 3150 CG1 VAL A 389 32.082 36.049 48.318 1.00 52.78 C ANISOU 3150 CG1 VAL A 389 6100 6905 7049 -6 1574 1494 C ATOM 3151 CG2 VAL A 389 29.915 34.833 48.700 1.00 56.22 C ANISOU 3151 CG2 VAL A 389 6282 7457 7622 -136 1844 2154 C ATOM 3152 N SER A 390 32.071 37.931 51.011 1.00 58.02 N ANISOU 3152 N SER A 390 7215 8106 6723 409 1786 1409 N ATOM 3153 CA SER A 390 33.130 37.755 51.999 1.00 61.36 C ANISOU 3153 CA SER A 390 7818 8600 6895 465 1585 1385 C ATOM 3154 C SER A 390 33.107 38.922 52.973 1.00 67.25 C ANISOU 3154 C SER A 390 8838 9552 7162 660 1651 1187 C ATOM 3155 O SER A 390 33.332 40.070 52.572 1.00 65.93 O ANISOU 3155 O SER A 390 8790 9292 6970 681 1615 841 O ATOM 3156 CB SER A 390 34.499 37.642 51.319 1.00 57.16 C ANISOU 3156 CB SER A 390 7247 7863 6608 344 1282 1148 C ATOM 3157 OG SER A 390 35.552 37.820 52.248 1.00 60.18 O ANISOU 3157 OG SER A 390 7795 8351 6721 407 1059 1054 O ATOM 3158 N LYS A 391 32.832 38.626 54.249 1.00 72.76 N ANISOU 3158 N LYS A 391 9663 10518 7464 802 1738 1409 N ATOM 3159 CA LYS A 391 32.803 39.669 55.271 1.00 76.07 C ANISOU 3159 CA LYS A 391 10392 11155 7358 1028 1795 1192 C ATOM 3160 C LYS A 391 34.166 40.329 55.427 1.00 75.63 C ANISOU 3160 C LYS A 391 10556 10979 7201 978 1436 820 C ATOM 3161 O LYS A 391 34.254 41.540 55.667 1.00 68.74 O ANISOU 3161 O LYS A 391 9943 10093 6083 1084 1408 468 O ATOM 3162 CB LYS A 391 32.343 39.089 56.609 1.00 83.82 C ANISOU 3162 CB LYS A 391 11461 12495 7891 1177 1947 1533 C ATOM 3163 CG LYS A 391 30.890 39.376 56.948 1.00 90.49 C ANISOU 3163 CG LYS A 391 12244 13631 8507 1377 2384 1695 C ATOM 3164 N ARG A 392 35.241 39.547 55.304 1.00 71.93 N ANISOU 3164 N ARG A 392 9982 10417 6933 820 1140 896 N ATOM 3165 CA ARG A 392 36.582 40.117 55.366 1.00 77.50 C ANISOU 3165 CA ARG A 392 10800 11044 7602 729 780 578 C ATOM 3166 C ARG A 392 36.828 41.069 54.199 1.00 73.44 C ANISOU 3166 C ARG A 392 10233 10280 7389 581 744 247 C ATOM 3167 O ARG A 392 37.316 42.187 54.394 1.00 81.53 O ANISOU 3167 O ARG A 392 11483 11253 8242 552 588 -80 O ATOM 3168 CB ARG A 392 37.630 39.004 55.390 1.00 82.31 C ANISOU 3168 CB ARG A 392 11229 11634 8412 633 494 760 C ATOM 3169 CG ARG A 392 37.558 38.114 56.628 1.00 95.78 C ANISOU 3169 CG ARG A 392 13037 13568 9788 766 454 1112 C ATOM 3170 CD ARG A 392 38.942 37.625 57.047 1.00110.67 C ANISOU 3170 CD ARG A 392 14888 15488 11675 737 34 1126 C ATOM 3171 NE ARG A 392 39.822 38.729 57.428 1.00122.69 N ANISOU 3171 NE ARG A 392 16582 17088 12946 695 -237 742 N ATOM 3172 CZ ARG A 392 41.026 38.580 57.976 1.00130.69 C ANISOU 3172 CZ ARG A 392 17588 18209 13858 670 -638 703 C ATOM 3173 NH1 ARG A 392 41.505 37.368 58.221 1.00133.81 N ANISOU 3173 NH1 ARG A 392 17823 18641 14377 734 -807 1030 N ATOM 3174 NH2 ARG A 392 41.751 39.647 58.282 1.00133.99 N ANISOU 3174 NH2 ARG A 392 18161 18682 14067 578 -899 345 N ATOM 3175 N PHE A 393 36.492 40.651 52.975 1.00 66.18 N ANISOU 3175 N PHE A 393 9043 9194 6907 469 869 335 N ATOM 3176 CA PHE A 393 36.731 41.521 51.827 1.00 65.13 C ANISOU 3176 CA PHE A 393 8860 8853 7032 316 840 72 C ATOM 3177 C PHE A 393 35.874 42.777 51.895 1.00 68.59 C ANISOU 3177 C PHE A 393 9543 9239 7280 437 1012 -113 C ATOM 3178 O PHE A 393 36.353 43.877 51.601 1.00 67.45 O ANISOU 3178 O PHE A 393 9558 8935 7136 340 873 -397 O ATOM 3179 CB PHE A 393 36.485 40.768 50.521 1.00 61.18 C ANISOU 3179 CB PHE A 393 8047 8222 6977 197 939 204 C ATOM 3180 CG PHE A 393 37.708 40.082 49.987 1.00 54.20 C ANISOU 3180 CG PHE A 393 6945 7294 6356 55 711 180 C ATOM 3181 CD1 PHE A 393 38.742 40.820 49.435 1.00 53.80 C ANISOU 3181 CD1 PHE A 393 6849 7197 6395 -115 536 -68 C ATOM 3182 CD2 PHE A 393 37.828 38.705 50.039 1.00 55.35 C ANISOU 3182 CD2 PHE A 393 6922 7443 6664 99 672 417 C ATOM 3183 CE1 PHE A 393 39.870 40.197 48.951 1.00 53.60 C ANISOU 3183 CE1 PHE A 393 6567 7202 6598 -206 360 -88 C ATOM 3184 CE2 PHE A 393 38.958 38.079 49.552 1.00 54.17 C ANISOU 3184 CE2 PHE A 393 6566 7261 6755 42 471 367 C ATOM 3185 CZ PHE A 393 39.976 38.826 49.008 1.00 53.79 C ANISOU 3185 CZ PHE A 393 6426 7236 6775 -95 333 110 C ATOM 3186 N LYS A 394 34.606 42.633 52.291 1.00 59.97 N ANISOU 3186 N LYS A 394 8476 8277 6033 653 1308 58 N ATOM 3187 CA LYS A 394 33.736 43.797 52.422 1.00 71.21 C ANISOU 3187 CA LYS A 394 10120 9674 7263 857 1488 -121 C ATOM 3188 C LYS A 394 34.308 44.815 53.400 1.00 74.15 C ANISOU 3188 C LYS A 394 10903 10038 7234 960 1306 -446 C ATOM 3189 O LYS A 394 34.278 46.022 53.136 1.00 76.12 O ANISOU 3189 O LYS A 394 11388 10067 7466 993 1253 -739 O ATOM 3190 CB LYS A 394 32.339 43.359 52.860 1.00 73.09 C ANISOU 3190 CB LYS A 394 10254 10158 7359 1100 1849 152 C ATOM 3191 CG LYS A 394 31.467 44.481 53.408 1.00 81.35 C ANISOU 3191 CG LYS A 394 11553 11282 8074 1437 2058 -38 C ATOM 3192 CD LYS A 394 29.987 44.145 53.282 1.00 87.34 C ANISOU 3192 CD LYS A 394 12048 12262 8877 1627 2443 247 C ATOM 3193 CE LYS A 394 29.691 42.747 53.801 1.00 94.79 C ANISOU 3193 CE LYS A 394 12737 13492 9786 1550 2569 688 C ATOM 3194 NZ LYS A 394 28.372 42.246 53.327 1.00101.76 N ANISOU 3194 NZ LYS A 394 13247 14534 10885 1575 2871 1022 N ATOM 3195 N ASN A 395 34.828 44.352 54.538 1.00 74.03 N ANISOU 3195 N ASN A 395 11006 10238 6884 1009 1179 -398 N ATOM 3196 CA ASN A 395 35.375 45.285 55.515 1.00 78.79 C ANISOU 3196 CA ASN A 395 12027 10846 7062 1098 963 -732 C ATOM 3197 C ASN A 395 36.661 45.923 55.005 1.00 78.71 C ANISOU 3197 C ASN A 395 12075 10567 7266 781 566 -1002 C ATOM 3198 O ASN A 395 36.925 47.103 55.270 1.00 80.42 O ANISOU 3198 O ASN A 395 12647 10599 7309 781 389 -1353 O ATOM 3199 CB ASN A 395 35.613 44.570 56.845 1.00 88.93 C ANISOU 3199 CB ASN A 395 13414 12471 7905 1220 903 -578 C ATOM 3200 CG ASN A 395 34.325 44.126 57.501 1.00 91.71 C ANISOU 3200 CG ASN A 395 13752 13140 7954 1530 1316 -312 C ATOM 3201 OD1 ASN A 395 33.266 44.703 57.262 1.00 90.83 O ANISOU 3201 OD1 ASN A 395 13665 13021 7824 1741 1621 -375 O ATOM 3202 ND2 ASN A 395 34.406 43.087 58.326 1.00 90.36 N ANISOU 3202 ND2 ASN A 395 13516 13267 7550 1559 1326 18 N ATOM 3203 N ALA A 396 37.470 45.154 54.271 1.00 80.77 N ANISOU 3203 N ALA A 396 11983 10801 7905 507 421 -841 N ATOM 3204 CA ALA A 396 38.705 45.689 53.708 1.00 67.13 C ANISOU 3204 CA ALA A 396 10208 8892 6406 179 83 -1039 C ATOM 3205 C ALA A 396 38.413 46.735 52.641 1.00 76.06 C ANISOU 3205 C ALA A 396 11400 9708 7790 59 149 -1204 C ATOM 3206 O ALA A 396 39.111 47.754 52.554 1.00 76.70 O ANISOU 3206 O ALA A 396 11676 9584 7884 -151 -114 -1456 O ATOM 3207 CB ALA A 396 39.553 44.550 53.137 1.00 64.84 C ANISOU 3207 CB ALA A 396 9484 8703 6451 -8 -24 -818 C ATOM 3208 N PHE A 397 37.385 46.499 51.820 1.00 72.40 N ANISOU 3208 N PHE A 397 10775 9196 7537 167 471 -1041 N ATOM 3209 CA PHE A 397 36.991 47.477 50.810 1.00 68.95 C ANISOU 3209 CA PHE A 397 10412 8471 7316 93 538 -1152 C ATOM 3210 C PHE A 397 36.518 48.771 51.462 1.00 73.96 C ANISOU 3210 C PHE A 397 11527 8912 7664 296 510 -1436 C ATOM 3211 O PHE A 397 36.908 49.868 51.047 1.00 77.39 O ANISOU 3211 O PHE A 397 12181 9027 8196 122 319 -1642 O ATOM 3212 CB PHE A 397 35.891 46.902 49.909 1.00 65.10 C ANISOU 3212 CB PHE A 397 9654 8017 7064 205 864 -909 C ATOM 3213 CG PHE A 397 36.402 46.054 48.768 1.00 62.46 C ANISOU 3213 CG PHE A 397 8924 7708 7100 -50 848 -738 C ATOM 3214 CD1 PHE A 397 37.179 46.605 47.764 1.00 59.23 C ANISOU 3214 CD1 PHE A 397 8447 7138 6921 -346 701 -827 C ATOM 3215 CD2 PHE A 397 36.078 44.711 48.692 1.00 55.80 C ANISOU 3215 CD2 PHE A 397 7793 7048 6362 10 984 -488 C ATOM 3216 CE1 PHE A 397 37.642 45.828 46.717 1.00 52.03 C ANISOU 3216 CE1 PHE A 397 7179 6298 6293 -532 717 -701 C ATOM 3217 CE2 PHE A 397 36.534 43.927 47.650 1.00 51.27 C ANISOU 3217 CE2 PHE A 397 6902 6474 6104 -175 961 -387 C ATOM 3218 CZ PHE A 397 37.319 44.486 46.659 1.00 50.41 C ANISOU 3218 CZ PHE A 397 6720 6253 6179 -423 843 -509 C ATOM 3219 N LYS A 398 35.668 48.659 52.488 1.00 76.85 N ANISOU 3219 N LYS A 398 12072 9463 7665 674 702 -1447 N ATOM 3220 CA LYS A 398 35.150 49.849 53.158 1.00 79.38 C ANISOU 3220 CA LYS A 398 12873 9618 7671 960 705 -1760 C ATOM 3221 C LYS A 398 36.266 50.648 53.817 1.00 85.62 C ANISOU 3221 C LYS A 398 14046 10223 8261 773 281 -2100 C ATOM 3222 O LYS A 398 36.273 51.883 53.759 1.00 93.01 O ANISOU 3222 O LYS A 398 15375 10787 9177 783 125 -2401 O ATOM 3223 CB LYS A 398 34.105 49.456 54.199 1.00 77.10 C ANISOU 3223 CB LYS A 398 12652 9671 6971 1412 1023 -1689 C ATOM 3224 CG LYS A 398 32.841 48.866 53.624 1.00 79.87 C ANISOU 3224 CG LYS A 398 12650 10192 7505 1607 1435 -1373 C ATOM 3225 CD LYS A 398 31.857 48.600 54.738 1.00 94.47 C ANISOU 3225 CD LYS A 398 14562 12424 8910 2037 1756 -1298 C ATOM 3226 CE LYS A 398 30.557 48.054 54.204 1.00100.99 C ANISOU 3226 CE LYS A 398 14992 13450 9930 2204 2154 -963 C ATOM 3227 NZ LYS A 398 29.554 47.981 55.302 1.00109.53 N ANISOU 3227 NZ LYS A 398 16125 14941 10551 2646 2504 -900 N ATOM 3228 N SER A 399 37.207 49.960 54.470 1.00 89.17 N ANISOU 3228 N SER A 399 14401 10911 8567 602 60 -2053 N ATOM 3229 CA SER A 399 38.339 50.650 55.078 1.00 95.93 C ANISOU 3229 CA SER A 399 15564 11630 9255 367 -399 -2355 C ATOM 3230 C SER A 399 39.165 51.381 54.031 1.00 98.56 C ANISOU 3230 C SER A 399 15837 11601 10012 -86 -665 -2431 C ATOM 3231 O SER A 399 39.662 52.486 54.280 1.00103.38 O ANISOU 3231 O SER A 399 16836 11894 10551 -252 -995 -2742 O ATOM 3232 CB SER A 399 39.217 49.655 55.835 1.00 99.54 C ANISOU 3232 CB SER A 399 15829 12453 9540 257 -600 -2219 C ATOM 3233 OG SER A 399 40.541 50.149 55.960 1.00108.66 O ANISOU 3233 OG SER A 399 17055 13489 10743 -128 -1087 -2412 O ATOM 3234 N ALA A 400 39.331 50.772 52.855 1.00 98.85 N ANISOU 3234 N ALA A 400 15397 11682 10478 -305 -536 -2143 N ATOM 3235 CA ALA A 400 40.186 51.364 51.834 1.00 97.39 C ANISOU 3235 CA ALA A 400 15090 11247 10667 -763 -755 -2152 C ATOM 3236 C ALA A 400 39.478 52.501 51.112 1.00101.86 C ANISOU 3236 C ALA A 400 15940 11383 11378 -732 -670 -2250 C ATOM 3237 O ALA A 400 40.114 53.491 50.729 1.00108.42 O ANISOU 3237 O ALA A 400 16953 11877 12364 -1078 -951 -2375 O ATOM 3238 CB ALA A 400 40.630 50.292 50.836 1.00 83.51 C ANISOU 3238 CB ALA A 400 12739 9732 9260 -963 -629 -1835 C ATOM 3239 N LEU A 401 38.165 52.382 50.924 1.00 99.64 N ANISOU 3239 N LEU A 401 15689 11107 11062 -332 -303 -2168 N ATOM 3240 CA LEU A 401 37.434 53.324 50.088 1.00100.38 C ANISOU 3240 CA LEU A 401 15971 10824 11343 -263 -205 -2191 C ATOM 3241 C LEU A 401 36.646 54.340 50.910 1.00118.41 C ANISOU 3241 C LEU A 401 18822 12836 13334 146 -207 -2507 C ATOM 3242 O LEU A 401 36.960 55.536 50.891 1.00124.36 O ANISOU 3242 O LEU A 401 20003 13129 14121 14 -488 -2748 O ATOM 3243 CB LEU A 401 36.501 52.565 49.141 1.00 88.61 C ANISOU 3243 CB LEU A 401 14083 9516 10067 -105 174 -1878 C ATOM 3244 CG LEU A 401 37.172 51.783 48.007 1.00 79.67 C ANISOU 3244 CG LEU A 401 12458 8546 9266 -484 185 -1610 C ATOM 3245 CD1 LEU A 401 36.123 51.165 47.095 1.00 70.82 C ANISOU 3245 CD1 LEU A 401 11041 7547 8321 -307 516 -1358 C ATOM 3246 CD2 LEU A 401 38.113 52.678 47.214 1.00 80.74 C ANISOU 3246 CD2 LEU A 401 12662 8389 9626 -942 -82 -1644 C ATOM 3247 N CYS A 402 35.629 53.872 51.640 1.00130.30 N ANISOU 3247 N CYS A 402 20339 14620 14548 645 103 -2505 N ATOM 3248 CA CYS A 402 34.703 54.787 52.305 1.00141.17 C ANISOU 3248 CA CYS A 402 22196 15798 15644 1140 195 -2795 C ATOM 3249 C CYS A 402 35.433 55.726 53.259 1.00159.06 C ANISOU 3249 C CYS A 402 25043 17771 17621 1085 -201 -3232 C ATOM 3250 O CYS A 402 35.311 56.952 53.156 1.00166.42 O ANISOU 3250 O CYS A 402 26449 18189 18595 1154 -382 -3507 O ATOM 3251 CB CYS A 402 33.622 53.997 53.044 1.00143.22 C ANISOU 3251 CB CYS A 402 22294 16536 15588 1645 612 -2684 C ATOM 3252 SG CYS A 402 32.620 52.929 51.981 1.00140.59 S ANISOU 3252 SG CYS A 402 21307 16515 15595 1707 1040 -2190 S ATOM 3253 N CYS A 403 36.202 55.170 54.189 1.00171.35 N ANISOU 3253 N CYS A 403 26594 19623 18889 956 -374 -3301 N ATOM 3254 CA CYS A 403 36.975 55.985 55.118 1.00185.55 C ANISOU 3254 CA CYS A 403 28928 21179 20392 851 -811 -3721 C ATOM 3255 C CYS A 403 38.396 55.450 55.256 1.00186.84 C ANISOU 3255 C CYS A 403 28847 21520 20622 304 -1181 -3634 C ATOM 3256 O CYS A 403 39.202 55.559 54.332 1.00187.38 O ANISOU 3256 O CYS A 403 28665 21416 21114 -202 -1382 -3482 O ATOM 3257 CB CYS A 403 36.294 56.032 56.485 1.00193.55 C ANISOU 3257 CB CYS A 403 30326 22426 20790 1420 -665 -4004 C ATOM 3258 SG CYS A 403 36.062 54.411 57.245 1.00191.91 S ANISOU 3258 SG CYS A 403 29660 23011 20246 1611 -333 -3657 S TER 3259 CYS A 403 HETATM 3260 C1 D2U A1201 36.238 33.144 23.856 1.00 48.72 C HETATM 3261 C2 D2U A1201 36.489 34.489 23.650 1.00 44.68 C HETATM 3262 C3 D2U A1201 37.517 35.130 24.331 1.00 42.97 C HETATM 3263 C4 D2U A1201 38.310 34.404 25.201 1.00 47.48 C HETATM 3264 C5 D2U A1201 38.058 33.055 25.407 1.00 48.52 C HETATM 3265 C6 D2U A1201 37.024 32.423 24.735 1.00 47.65 C HETATM 3266 C7 D2U A1201 35.095 32.469 23.108 1.00 48.25 C HETATM 3267 C8 D2U A1201 38.924 32.260 26.371 1.00 48.34 C HETATM 3268 C9 D2U A1201 37.800 36.621 24.088 1.00 43.67 C HETATM 3269 N10 D2U A1201 36.813 37.679 24.295 1.00 43.08 N HETATM 3270 C11 D2U A1201 37.175 39.054 23.998 1.00 54.22 C HETATM 3271 C12 D2U A1201 36.804 40.101 25.054 1.00 60.91 C HETATM 3272 C13 D2U A1201 37.248 39.700 26.469 1.00 61.32 C HETATM 3273 C14 D2U A1201 38.499 39.140 26.682 1.00 62.48 C HETATM 3274 C15 D2U A1201 38.874 38.782 27.967 1.00 67.12 C HETATM 3275 C16 D2U A1201 38.002 38.980 29.029 1.00 63.27 C HETATM 3276 C17 D2U A1201 36.753 39.534 28.808 1.00 62.91 C HETATM 3277 C18 D2U A1201 36.376 39.892 27.525 1.00 63.94 C HETATM 3278 C19 D2U A1201 38.405 38.576 30.454 1.00 57.10 C HETATM 3279 C20 D2U A1201 37.433 38.128 31.335 1.00 53.19 C HETATM 3280 C21 D2U A1201 37.780 37.755 32.623 1.00 49.54 C HETATM 3281 C22 D2U A1201 39.101 37.828 33.031 1.00 50.30 C HETATM 3282 C23 D2U A1201 40.074 38.274 32.156 1.00 57.66 C HETATM 3283 C24 D2U A1201 39.729 38.649 30.864 1.00 58.14 C HETATM 3284 C25 D2U A1201 35.459 37.411 24.744 1.00 36.65 C HETATM 3285 O26 D2U A1201 38.881 36.928 23.707 1.00 48.54 O HETATM 3286 C27 D2U A1201 36.694 39.393 22.586 1.00 58.89 C HETATM 3287 O28 D2U A1201 35.990 40.328 22.385 1.00 65.96 O HETATM 3288 N29 D2U A1201 37.128 38.508 21.514 1.00 51.33 N HETATM 3289 C30 D2U A1201 36.708 38.714 20.135 1.00 47.88 C HETATM 3290 C31 D2U A1201 35.795 37.542 19.772 1.00 53.69 C HETATM 3291 C32 D2U A1201 37.915 38.831 19.196 1.00 40.00 C HETATM 3292 C33 D2U A1201 38.637 40.175 19.355 1.00 44.05 C HETATM 3293 C34 D2U A1201 38.251 41.269 20.125 1.00 48.39 C HETATM 3294 N35 D2U A1201 39.154 42.225 19.993 1.00 49.96 N HETATM 3295 C36 D2U A1201 40.134 41.823 19.172 1.00 49.67 C HETATM 3296 C37 D2U A1201 39.851 40.539 18.747 1.00 43.08 C HETATM 3297 C38 D2U A1201 41.299 42.464 18.720 1.00 49.89 C HETATM 3298 C39 D2U A1201 42.163 41.806 17.854 1.00 47.88 C HETATM 3299 C40 D2U A1201 41.869 40.512 17.428 1.00 46.34 C HETATM 3300 C41 D2U A1201 40.719 39.870 17.873 1.00 42.49 C HETATM 3301 O42 D2U A1201 34.800 37.750 19.032 1.00 56.03 O HETATM 3302 O43 D2U A1201 36.028 36.386 20.218 1.00 46.66 O HETATM 3303 P PO4 A1202 25.677 12.558 56.223 1.00149.70 P HETATM 3304 O1 PO4 A1202 25.313 12.603 54.757 1.00152.66 O HETATM 3305 O2 PO4 A1202 27.138 12.211 56.374 1.00146.74 O HETATM 3306 O3 PO4 A1202 24.835 11.514 56.918 1.00151.29 O HETATM 3307 O4 PO4 A1202 25.423 13.907 56.845 1.00147.39 O HETATM 3308 P PO4 A1203 39.607 42.899 57.593 1.00156.69 P HETATM 3309 O1 PO4 A1203 39.124 42.199 56.350 1.00156.85 O HETATM 3310 O2 PO4 A1203 40.174 44.247 57.220 1.00152.10 O HETATM 3311 O3 PO4 A1203 40.681 42.064 58.248 1.00159.68 O HETATM 3312 O4 PO4 A1203 38.455 43.083 58.552 1.00158.95 O HETATM 3313 P PO4 A1204 27.454 16.467 76.373 1.00109.68 P HETATM 3314 O1 PO4 A1204 27.506 16.950 74.943 1.00117.24 O HETATM 3315 O2 PO4 A1204 28.397 17.301 77.199 1.00108.97 O HETATM 3316 O3 PO4 A1204 27.877 15.021 76.452 1.00108.40 O HETATM 3317 O4 PO4 A1204 26.050 16.596 76.907 1.00104.01 O HETATM 3318 P PO4 A1205 26.300 47.472 53.856 1.00219.61 P HETATM 3319 O1 PO4 A1205 25.844 47.935 52.494 1.00220.41 O HETATM 3320 O2 PO4 A1205 27.482 48.298 54.301 1.00219.38 O HETATM 3321 O3 PO4 A1205 26.689 46.015 53.778 1.00219.21 O HETATM 3322 O4 PO4 A1205 25.174 47.632 54.848 1.00220.44 O HETATM 3323 C10 OLC A1206 48.078 25.646 22.464 1.00 51.45 C HETATM 3324 C9 OLC A1206 49.264 25.954 21.952 1.00 56.43 C HETATM 3325 C11 OLC A1206 46.922 25.385 21.529 1.00 52.21 C HETATM 3326 C8 OLC A1206 50.437 26.219 22.861 1.00 59.19 C HETATM 3327 C24 OLC A1206 56.188 28.415 13.938 1.00 82.77 C HETATM 3328 C12 OLC A1206 46.836 23.890 21.247 1.00 56.83 C HETATM 3329 C7 OLC A1206 51.533 25.196 22.589 1.00 63.71 C HETATM 3330 C13 OLC A1206 45.473 23.511 20.682 1.00 59.96 C HETATM 3331 C6 OLC A1206 52.900 25.805 22.873 1.00 65.65 C HETATM 3332 C14 OLC A1206 45.083 24.425 19.524 1.00 62.70 C HETATM 3333 C5 OLC A1206 53.023 27.127 22.127 1.00 68.90 C HETATM 3334 C4 OLC A1206 54.468 27.603 22.069 1.00 74.12 C HETATM 3335 C3 OLC A1206 54.677 28.498 20.853 1.00 77.18 C HETATM 3336 C2 OLC A1206 55.294 27.721 19.693 1.00 83.04 C HETATM 3337 C21 OLC A1206 54.717 28.484 15.947 1.00 94.56 C HETATM 3338 C1 OLC A1206 54.726 28.251 18.397 1.00 91.62 C HETATM 3339 C22 OLC A1206 55.032 27.732 14.658 1.00 87.89 C HETATM 3340 O19 OLC A1206 53.810 29.056 18.413 1.00 97.70 O HETATM 3341 O25 OLC A1206 56.003 29.835 13.952 1.00 76.64 O HETATM 3342 O23 OLC A1206 55.392 26.380 14.958 1.00 88.08 O HETATM 3343 O20 OLC A1206 55.241 27.829 17.104 1.00 94.17 O HETATM 3344 C18 OLC A1207 47.710 18.657 31.864 1.00110.02 C HETATM 3345 C10 OLC A1207 42.812 19.992 25.182 1.00101.26 C HETATM 3346 C9 OLC A1207 42.374 19.704 23.958 1.00104.08 C HETATM 3347 C17 OLC A1207 46.512 18.514 30.950 1.00111.57 C HETATM 3348 C11 OLC A1207 41.855 20.068 26.348 1.00101.13 C HETATM 3349 C8 OLC A1207 40.906 19.458 23.702 1.00104.11 C HETATM 3350 C24 OLC A1207 35.718 21.901 13.673 1.00121.88 C HETATM 3351 C16 OLC A1207 45.610 19.742 31.016 1.00110.87 C HETATM 3352 C12 OLC A1207 42.659 20.170 27.639 1.00105.24 C HETATM 3353 C7 OLC A1207 40.405 20.409 22.620 1.00100.87 C HETATM 3354 C15 OLC A1207 44.432 19.607 30.057 1.00110.12 C HETATM 3355 C13 OLC A1207 43.796 19.154 27.649 1.00109.77 C HETATM 3356 C6 OLC A1207 41.243 20.297 21.354 1.00 99.44 C HETATM 3357 C14 OLC A1207 44.913 19.543 28.612 1.00110.71 C HETATM 3358 C5 OLC A1207 40.436 20.733 20.139 1.00100.01 C HETATM 3359 C4 OLC A1207 40.764 19.836 18.953 1.00100.08 C HETATM 3360 C3 OLC A1207 39.753 20.023 17.832 1.00104.26 C HETATM 3361 C2 OLC A1207 40.119 19.136 16.649 1.00108.68 C HETATM 3362 C21 OLC A1207 37.929 20.784 13.921 1.00118.69 C HETATM 3363 C1 OLC A1207 39.731 19.835 15.371 1.00109.63 C HETATM 3364 C22 OLC A1207 36.448 20.564 13.641 1.00122.45 C HETATM 3365 O19 OLC A1207 40.586 20.332 14.657 1.00107.50 O HETATM 3366 O25 OLC A1207 34.325 21.676 13.918 1.00121.82 O HETATM 3367 O23 OLC A1207 36.294 19.970 12.347 1.00125.99 O HETATM 3368 O20 OLC A1207 38.332 19.922 14.983 1.00114.09 O HETATM 3369 C18 OLC A1208 49.362 23.204 34.414 1.00 97.69 C HETATM 3370 C10 OLC A1208 49.020 22.246 25.491 1.00 85.03 C HETATM 3371 C9 OLC A1208 49.610 21.773 24.395 1.00 86.31 C HETATM 3372 C17 OLC A1208 49.841 22.973 32.996 1.00102.17 C HETATM 3373 C11 OLC A1208 47.608 21.868 25.867 1.00 86.50 C HETATM 3374 C8 OLC A1208 48.911 20.842 23.431 1.00 90.35 C HETATM 3375 C24 OLC A1208 54.465 19.987 14.263 1.00116.28 C HETATM 3376 C16 OLC A1208 48.673 22.921 32.017 1.00101.29 C HETATM 3377 C12 OLC A1208 47.583 21.526 27.353 1.00 89.33 C HETATM 3378 C7 OLC A1208 49.593 21.006 22.076 1.00 93.00 C HETATM 3379 C15 OLC A1208 49.160 22.825 30.574 1.00 98.07 C HETATM 3380 C13 OLC A1208 48.415 22.509 28.174 1.00 91.85 C HETATM 3381 C6 OLC A1208 48.958 20.177 20.964 1.00 89.43 C HETATM 3382 C14 OLC A1208 48.007 22.465 29.643 1.00 95.52 C HETATM 3383 C5 OLC A1208 49.880 20.232 19.751 1.00 90.65 C HETATM 3384 C4 OLC A1208 49.261 19.677 18.473 1.00 94.71 C HETATM 3385 C3 OLC A1208 49.837 20.441 17.286 1.00 98.88 C HETATM 3386 C2 OLC A1208 49.678 19.715 15.954 1.00104.54 C HETATM 3387 C21 OLC A1208 52.408 18.916 13.391 1.00117.53 C HETATM 3388 C1 OLC A1208 51.060 19.609 15.360 1.00111.80 C HETATM 3389 C22 OLC A1208 53.533 19.890 13.057 1.00117.46 C HETATM 3390 O19 OLC A1208 52.025 19.531 16.101 1.00116.84 O HETATM 3391 O25 OLC A1208 55.124 21.258 14.318 1.00113.20 O HETATM 3392 O23 OLC A1208 54.256 19.386 11.928 1.00114.83 O HETATM 3393 O20 OLC A1208 51.279 19.608 13.923 1.00114.64 O HETATM 3394 C18 OLC A1209 50.503 39.749 43.227 1.00 83.81 C HETATM 3395 C10 OLC A1209 55.031 38.782 35.599 1.00 71.68 C HETATM 3396 C9 OLC A1209 54.651 39.552 34.579 1.00 80.49 C HETATM 3397 C17 OLC A1209 50.831 38.408 42.606 1.00 84.70 C HETATM 3398 C11 OLC A1209 54.387 38.958 36.954 1.00 69.84 C HETATM 3399 C8 OLC A1209 53.581 40.607 34.756 1.00 84.75 C HETATM 3400 C24 OLC A1209 56.113 42.491 44.038 1.00106.71 C HETATM 3401 C16 OLC A1209 51.869 38.539 41.493 1.00 80.15 C HETATM 3402 C12 OLC A1209 53.551 37.724 37.277 1.00 71.62 C HETATM 3403 C7 OLC A1209 53.868 41.807 33.856 1.00 84.19 C HETATM 3404 C15 OLC A1209 51.207 38.712 40.132 1.00 74.29 C HETATM 3405 C13 OLC A1209 53.051 37.728 38.719 1.00 74.05 C HETATM 3406 C6 OLC A1209 53.091 43.045 34.299 1.00 83.45 C HETATM 3407 C14 OLC A1209 52.229 38.973 39.027 1.00 74.26 C HETATM 3408 C5 OLC A1209 53.798 43.782 35.433 1.00 81.94 C HETATM 3409 C4 OLC A1209 53.199 43.443 36.792 1.00 80.56 C HETATM 3410 C3 OLC A1209 54.263 43.549 37.877 1.00 81.44 C HETATM 3411 C2 OLC A1209 53.991 42.584 39.026 1.00 87.74 C HETATM 3412 C21 OLC A1209 56.440 41.495 41.777 1.00104.83 C HETATM 3413 C1 OLC A1209 55.167 42.622 39.973 1.00 94.98 C HETATM 3414 C22 OLC A1209 56.285 41.187 43.263 1.00107.68 C HETATM 3415 O19 OLC A1209 56.135 43.323 39.728 1.00 95.40 O HETATM 3416 O25 OLC A1209 56.611 42.337 45.373 1.00101.03 O HETATM 3417 O23 OLC A1209 55.144 40.345 43.469 1.00108.22 O HETATM 3418 O20 OLC A1209 55.182 41.823 41.188 1.00100.61 O HETATM 3419 C18 OLC A1210 28.335 44.585 36.954 1.00 69.84 C HETATM 3420 C10 OLC A1210 27.442 39.063 42.856 1.00 89.74 C HETATM 3421 C9 OLC A1210 27.008 38.364 43.904 1.00 95.33 C HETATM 3422 C17 OLC A1210 29.106 43.629 37.838 1.00 75.45 C HETATM 3423 C11 OLC A1210 28.348 38.442 41.819 1.00 85.37 C HETATM 3424 C8 OLC A1210 27.425 36.929 44.121 1.00 97.50 C HETATM 3425 C24 OLC A1210 27.382 37.543 55.290 1.00119.42 C HETATM 3426 C16 OLC A1210 28.901 42.182 37.407 1.00 81.19 C HETATM 3427 C12 OLC A1210 28.397 39.312 40.561 1.00 85.51 C HETATM 3428 C7 OLC A1210 26.774 36.394 45.394 1.00100.18 C HETATM 3429 C15 OLC A1210 28.867 41.262 38.623 1.00 85.40 C HETATM 3430 C13 OLC A1210 27.581 40.597 40.691 1.00 85.66 C HETATM 3431 C6 OLC A1210 26.820 37.400 46.535 1.00102.65 C HETATM 3432 C14 OLC A1210 27.549 41.381 39.381 1.00 86.84 C HETATM 3433 C5 OLC A1210 25.758 37.070 47.578 1.00106.69 C HETATM 3434 C4 OLC A1210 26.196 35.960 48.528 1.00110.42 C HETATM 3435 C3 OLC A1210 25.137 35.752 49.609 1.00113.08 C HETATM 3436 C2 OLC A1210 25.709 35.128 50.879 1.00114.42 C HETATM 3437 C21 OLC A1210 28.366 36.606 53.172 1.00115.78 C HETATM 3438 C1 OLC A1210 26.418 36.201 51.672 1.00116.85 C HETATM 3439 C22 OLC A1210 28.043 37.877 53.955 1.00115.38 C HETATM 3440 O19 OLC A1210 26.376 37.361 51.296 1.00118.59 O HETATM 3441 O25 OLC A1210 28.353 37.084 56.236 1.00118.48 O HETATM 3442 O23 OLC A1210 29.235 38.641 54.173 1.00110.56 O HETATM 3443 O20 OLC A1210 27.166 35.886 52.882 1.00117.04 O HETATM 3444 C18 OLC A1211 26.446 36.767 37.647 1.00 97.76 C HETATM 3445 C10 OLC A1211 27.919 32.174 46.183 1.00102.71 C HETATM 3446 C9 OLC A1211 28.129 31.186 47.051 1.00101.70 C HETATM 3447 C17 OLC A1211 27.006 35.625 38.467 1.00 97.99 C HETATM 3448 C11 OLC A1211 27.260 31.862 44.860 1.00103.42 C HETATM 3449 C8 OLC A1211 27.690 29.782 46.699 1.00102.89 C HETATM 3450 C24 OLC A1211 30.251 23.074 36.329 1.00103.97 C HETATM 3451 C16 OLC A1211 26.233 35.456 39.770 1.00 96.24 C HETATM 3452 C12 OLC A1211 26.624 33.096 44.233 1.00100.95 C HETATM 3453 C7 OLC A1211 28.865 28.923 46.239 1.00103.20 C HETATM 3454 C15 OLC A1211 26.770 34.261 40.548 1.00 94.36 C HETATM 3455 C13 OLC A1211 27.079 33.214 42.783 1.00 98.09 C HETATM 3456 C6 OLC A1211 28.357 27.743 45.413 1.00100.48 C HETATM 3457 C14 OLC A1211 26.264 34.225 41.985 1.00 95.38 C HETATM 3458 C5 OLC A1211 29.496 27.023 44.699 1.00 97.13 C HETATM 3459 C4 OLC A1211 28.991 25.874 43.831 1.00 95.11 C HETATM 3460 C3 OLC A1211 30.138 25.172 43.107 1.00 94.78 C HETATM 3461 C2 OLC A1211 30.567 25.930 41.854 1.00 98.43 C HETATM 3462 C21 OLC A1211 30.933 23.981 38.565 1.00 98.83 C HETATM 3463 C1 OLC A1211 31.142 24.959 40.847 1.00103.22 C HETATM 3464 C22 OLC A1211 30.347 24.324 37.200 1.00102.37 C HETATM 3465 O19 OLC A1211 31.839 24.025 41.206 1.00107.44 O HETATM 3466 O25 OLC A1211 29.009 22.398 36.564 1.00102.82 O HETATM 3467 O23 OLC A1211 29.042 24.884 37.378 1.00102.62 O HETATM 3468 O20 OLC A1211 30.843 25.112 39.430 1.00 99.64 O HETATM 3469 C18 OLC A1212 24.347 41.093 35.140 1.00 97.09 C HETATM 3470 C10 OLC A1212 22.391 43.480 28.054 1.00 93.39 C HETATM 3471 C9 OLC A1212 21.321 43.882 27.369 1.00 94.22 C HETATM 3472 C17 OLC A1212 24.788 40.906 33.705 1.00 97.06 C HETATM 3473 C11 OLC A1212 23.475 42.642 27.418 1.00 89.86 C HETATM 3474 C8 OLC A1212 21.126 43.497 25.922 1.00 95.62 C HETATM 3475 C16 OLC A1212 23.629 41.039 32.723 1.00 96.09 C HETATM 3476 C12 OLC A1212 24.362 42.014 28.493 1.00 87.48 C HETATM 3477 C7 OLC A1212 19.716 42.943 25.746 1.00 94.29 C HETATM 3478 C15 OLC A1212 24.154 41.264 31.307 1.00 99.38 C HETATM 3479 C13 OLC A1212 24.792 43.002 29.575 1.00 88.72 C HETATM 3480 C6 OLC A1212 19.517 42.340 24.360 1.00 90.45 C HETATM 3481 C14 OLC A1212 24.095 42.736 30.910 1.00 96.05 C HETATM 3482 C5 OLC A1212 18.892 43.324 23.377 1.00 89.46 C HETATM 3483 C4 OLC A1212 18.764 42.649 22.016 1.00 94.56 C HETATM 3484 C3 OLC A1212 18.197 43.558 20.932 1.00 94.28 C HETATM 3485 C2 OLC A1212 18.272 42.826 19.596 1.00 97.41 C HETATM 3486 C1 OLC A1212 17.614 43.618 18.491 1.00105.11 C HETATM 3487 O19 OLC A1212 17.087 44.696 18.715 1.00110.96 O HETATM 3488 O20 OLC A1212 17.603 43.092 17.136 1.00104.79 O HETATM 3489 C18 OLC A1213 48.070 39.247 30.795 1.00 58.44 C HETATM 3490 C10 OLC A1213 56.537 37.855 27.524 1.00 72.92 C HETATM 3491 C9 OLC A1213 56.616 36.748 26.788 1.00 69.90 C HETATM 3492 C17 OLC A1213 49.434 38.625 30.582 1.00 57.98 C HETATM 3493 C11 OLC A1213 55.393 38.820 27.309 1.00 78.01 C HETATM 3494 C8 OLC A1213 55.542 36.440 25.769 1.00 69.68 C HETATM 3495 C16 OLC A1213 50.534 39.678 30.618 1.00 60.10 C HETATM 3496 C12 OLC A1213 54.482 38.909 28.525 1.00 76.73 C HETATM 3497 C7 OLC A1213 55.916 36.939 24.380 1.00 73.31 C HETATM 3498 C15 OLC A1213 51.810 39.173 29.956 1.00 66.77 C HETATM 3499 C13 OLC A1213 53.529 40.087 28.354 1.00 73.46 C HETATM 3500 C6 OLC A1213 54.839 37.905 23.896 1.00 73.92 C HETATM 3501 C14 OLC A1213 52.720 40.347 29.619 1.00 74.06 C HETATM 3502 C5 OLC A1213 54.584 37.747 22.406 1.00 73.95 C HETATM 3503 C4 OLC A1213 54.500 39.107 21.721 1.00 80.99 C HETATM 3504 C3 OLC A1213 53.215 39.845 22.079 1.00 84.00 C HETATM 3505 C2 OLC A1213 52.614 40.528 20.852 1.00 84.49 C HETATM 3506 C1 OLC A1213 53.536 41.594 20.301 1.00 85.86 C HETATM 3507 O19 OLC A1213 54.331 41.336 19.413 1.00 88.99 O HETATM 3508 O20 OLC A1213 53.473 42.957 20.806 1.00 85.86 O HETATM 3509 O HOH A1301 28.375 12.779 76.330 1.00 68.29 O HETATM 3510 O HOH A1302 41.693 37.025 20.900 1.00 69.36 O HETATM 3511 O HOH A1303 46.096 31.906 27.954 1.00 37.87 O HETATM 3512 O HOH A1304 53.213 48.573 14.613 1.00 68.36 O HETATM 3513 O HOH A1305 38.815 37.004 36.290 1.00 52.41 O HETATM 3514 O HOH A1306 45.487 29.294 23.634 1.00 41.63 O HETATM 3515 O HOH A1307 35.061 31.260 19.527 1.00 50.37 O HETATM 3516 O HOH A1308 36.438 31.085 28.954 1.00 51.00 O HETATM 3517 O HOH A1309 29.471 34.986 28.001 1.00 61.99 O HETATM 3518 O HOH A1310 42.207 57.847 5.380 1.00 47.52 O HETATM 3519 O HOH A1311 38.093 34.909 20.330 1.00 47.29 O HETATM 3520 O HOH A1312 36.550 42.988 27.516 1.00 62.67 O HETATM 3521 O HOH A1313 36.266 41.569 59.210 1.00 74.55 O HETATM 3522 O HOH A1314 50.212 41.849 7.543 1.00 40.40 O HETATM 3523 O HOH A1315 31.324 44.602 25.963 1.00 44.81 O HETATM 3524 O HOH A1316 35.126 28.775 21.395 1.00 56.39 O HETATM 3525 O HOH A1317 40.178 35.839 18.619 1.00 49.96 O HETATM 3526 O HOH A1318 43.861 48.934 56.625 1.00 72.41 O HETATM 3527 O HOH A1319 46.701 49.830 11.187 1.00 62.41 O HETATM 3528 O HOH A1320 35.348 45.838 39.796 1.00 52.30 O HETATM 3529 O HOH A1321 44.437 49.081 -6.010 1.00 67.80 O HETATM 3530 O HOH A1322 29.115 33.504 10.199 1.00 84.85 O HETATM 3531 O HOH A1323 32.618 28.020 22.851 1.00 57.88 O HETATM 3532 O HOH A1324 28.117 34.734 15.393 1.00 77.90 O HETATM 3533 O HOH A1325 37.290 40.493 38.145 1.00 70.29 O HETATM 3534 O HOH A1326 35.969 44.096 24.632 1.00 58.26 O HETATM 3535 O HOH A1327 37.200 32.488 18.939 1.00 62.24 O HETATM 3536 O HOH A1328 40.540 53.342 6.834 1.00 72.63 O HETATM 3537 O HOH A1329 52.059 48.785 11.992 1.00 74.06 O HETATM 3538 O HOH A1330 51.140 47.668 10.199 1.00 86.28 O HETATM 3539 O HOH A1331 32.433 33.551 15.815 1.00 73.10 O HETATM 3540 O HOH A1332 30.672 35.169 15.891 1.00 58.50 O HETATM 3541 O HOH A1333 48.742 49.047 9.617 1.00 69.26 O HETATM 3542 O HOH A1334 50.719 45.827 8.442 1.00 73.71 O CONECT 657 1236 CONECT 1236 657 CONECT 3260 3261 3265 3266 CONECT 3261 3260 3262 CONECT 3262 3261 3263 3268 CONECT 3263 3262 3264 CONECT 3264 3263 3265 3267 CONECT 3265 3260 3264 CONECT 3266 3260 CONECT 3267 3264 CONECT 3268 3262 3269 3285 CONECT 3269 3268 3270 3284 CONECT 3270 3269 3271 3286 CONECT 3271 3270 3272 CONECT 3272 3271 3273 3277 CONECT 3273 3272 3274 CONECT 3274 3273 3275 CONECT 3275 3274 3276 3278 CONECT 3276 3275 3277 CONECT 3277 3272 3276 CONECT 3278 3275 3279 3283 CONECT 3279 3278 3280 CONECT 3280 3279 3281 CONECT 3281 3280 3282 CONECT 3282 3281 3283 CONECT 3283 3278 3282 CONECT 3284 3269 CONECT 3285 3268 CONECT 3286 3270 3287 3288 CONECT 3287 3286 CONECT 3288 3286 3289 CONECT 3289 3288 3290 3291 CONECT 3290 3289 3301 3302 CONECT 3291 3289 3292 CONECT 3292 3291 3293 3296 CONECT 3293 3292 3294 CONECT 3294 3293 3295 CONECT 3295 3294 3296 3297 CONECT 3296 3292 3295 3300 CONECT 3297 3295 3298 CONECT 3298 3297 3299 CONECT 3299 3298 3300 CONECT 3300 3296 3299 CONECT 3301 3290 CONECT 3302 3290 CONECT 3303 3304 3305 3306 3307 CONECT 3304 3303 CONECT 3305 3303 CONECT 3306 3303 CONECT 3307 3303 CONECT 3308 3309 3310 3311 3312 CONECT 3309 3308 CONECT 3310 3308 CONECT 3311 3308 CONECT 3312 3308 CONECT 3313 3314 3315 3316 3317 CONECT 3314 3313 CONECT 3315 3313 CONECT 3316 3313 CONECT 3317 3313 CONECT 3318 3319 3320 3321 3322 CONECT 3319 3318 CONECT 3320 3318 CONECT 3321 3318 CONECT 3322 3318 CONECT 3323 3324 3325 CONECT 3324 3323 3326 CONECT 3325 3323 3328 CONECT 3326 3324 3329 CONECT 3327 3339 3341 CONECT 3328 3325 3330 CONECT 3329 3326 3331 CONECT 3330 3328 3332 CONECT 3331 3329 3333 CONECT 3332 3330 CONECT 3333 3331 3334 CONECT 3334 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3338 CONECT 3337 3339 3343 CONECT 3338 3336 3340 3343 CONECT 3339 3327 3337 3342 CONECT 3340 3338 CONECT 3341 3327 CONECT 3342 3339 CONECT 3343 3337 3338 CONECT 3344 3347 CONECT 3345 3346 3348 CONECT 3346 3345 3349 CONECT 3347 3344 3351 CONECT 3348 3345 3352 CONECT 3349 3346 3353 CONECT 3350 3364 3366 CONECT 3351 3347 3354 CONECT 3352 3348 3355 CONECT 3353 3349 3356 CONECT 3354 3351 3357 CONECT 3355 3352 3357 CONECT 3356 3353 3358 CONECT 3357 3354 3355 CONECT 3358 3356 3359 CONECT 3359 3358 3360 CONECT 3360 3359 3361 CONECT 3361 3360 3363 CONECT 3362 3364 3368 CONECT 3363 3361 3365 3368 CONECT 3364 3350 3362 3367 CONECT 3365 3363 CONECT 3366 3350 CONECT 3367 3364 CONECT 3368 3362 3363 CONECT 3369 3372 CONECT 3370 3371 3373 CONECT 3371 3370 3374 CONECT 3372 3369 3376 CONECT 3373 3370 3377 CONECT 3374 3371 3378 CONECT 3375 3389 3391 CONECT 3376 3372 3379 CONECT 3377 3373 3380 CONECT 3378 3374 3381 CONECT 3379 3376 3382 CONECT 3380 3377 3382 CONECT 3381 3378 3383 CONECT 3382 3379 3380 CONECT 3383 3381 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3388 CONECT 3387 3389 3393 CONECT 3388 3386 3390 3393 CONECT 3389 3375 3387 3392 CONECT 3390 3388 CONECT 3391 3375 CONECT 3392 3389 CONECT 3393 3387 3388 CONECT 3394 3397 CONECT 3395 3396 3398 CONECT 3396 3395 3399 CONECT 3397 3394 3401 CONECT 3398 3395 3402 CONECT 3399 3396 3403 CONECT 3400 3414 3416 CONECT 3401 3397 3404 CONECT 3402 3398 3405 CONECT 3403 3399 3406 CONECT 3404 3401 3407 CONECT 3405 3402 3407 CONECT 3406 3403 3408 CONECT 3407 3404 3405 CONECT 3408 3406 3409 CONECT 3409 3408 3410 CONECT 3410 3409 3411 CONECT 3411 3410 3413 CONECT 3412 3414 3418 CONECT 3413 3411 3415 3418 CONECT 3414 3400 3412 3417 CONECT 3415 3413 CONECT 3416 3400 CONECT 3417 3414 CONECT 3418 3412 3413 CONECT 3419 3422 CONECT 3420 3421 3423 CONECT 3421 3420 3424 CONECT 3422 3419 3426 CONECT 3423 3420 3427 CONECT 3424 3421 3428 CONECT 3425 3439 3441 CONECT 3426 3422 3429 CONECT 3427 3423 3430 CONECT 3428 3424 3431 CONECT 3429 3426 3432 CONECT 3430 3427 3432 CONECT 3431 3428 3433 CONECT 3432 3429 3430 CONECT 3433 3431 3434 CONECT 3434 3433 3435 CONECT 3435 3434 3436 CONECT 3436 3435 3438 CONECT 3437 3439 3443 CONECT 3438 3436 3440 3443 CONECT 3439 3425 3437 3442 CONECT 3440 3438 CONECT 3441 3425 CONECT 3442 3439 CONECT 3443 3437 3438 CONECT 3444 3447 CONECT 3445 3446 3448 CONECT 3446 3445 3449 CONECT 3447 3444 3451 CONECT 3448 3445 3452 CONECT 3449 3446 3453 CONECT 3450 3464 3466 CONECT 3451 3447 3454 CONECT 3452 3448 3455 CONECT 3453 3449 3456 CONECT 3454 3451 3457 CONECT 3455 3452 3457 CONECT 3456 3453 3458 CONECT 3457 3454 3455 CONECT 3458 3456 3459 CONECT 3459 3458 3460 CONECT 3460 3459 3461 CONECT 3461 3460 3463 CONECT 3462 3464 3468 CONECT 3463 3461 3465 3468 CONECT 3464 3450 3462 3467 CONECT 3465 3463 CONECT 3466 3450 CONECT 3467 3464 CONECT 3468 3462 3463 CONECT 3469 3472 CONECT 3470 3471 3473 CONECT 3471 3470 3474 CONECT 3472 3469 3475 CONECT 3473 3470 3476 CONECT 3474 3471 3477 CONECT 3475 3472 3478 CONECT 3476 3473 3479 CONECT 3477 3474 3480 CONECT 3478 3475 3481 CONECT 3479 3476 3481 CONECT 3480 3477 3482 CONECT 3481 3478 3479 CONECT 3482 3480 3483 CONECT 3483 3482 3484 CONECT 3484 3483 3485 CONECT 3485 3484 3486 CONECT 3486 3485 3487 3488 CONECT 3487 3486 CONECT 3488 3486 CONECT 3489 3492 CONECT 3490 3491 3493 CONECT 3491 3490 3494 CONECT 3492 3489 3495 CONECT 3493 3490 3496 CONECT 3494 3491 3497 CONECT 3495 3492 3498 CONECT 3496 3493 3499 CONECT 3497 3494 3500 CONECT 3498 3495 3501 CONECT 3499 3496 3501 CONECT 3500 3497 3502 CONECT 3501 3498 3499 CONECT 3502 3500 3503 CONECT 3503 3502 3504 CONECT 3504 3503 3505 CONECT 3505 3504 3506 CONECT 3506 3505 3507 3508 CONECT 3507 3506 CONECT 3508 3506 MASTER 493 0 13 17 2 0 23 6 3541 1 251 36 END