HEADER MEMBRANE PROTEIN 13-DEC-19 6TPG TITLE CRYSTAL STRUCTURE OF THE OREXIN-2 RECEPTOR IN COMPLEX WITH EMPA AT TITLE 2 2.74 A RESOLUTION CAVEAT 6TPG YCM A 1004 HAS WRONG CHIRALITY AT ATOM CA COMPND MOL_ID: 1; COMPND 2 MOLECULE: OREXIN RECEPTOR TYPE 2,GLGA GLYCOGEN SYNTHASE,HYPOCRETIN COMPND 3 RECEPTOR-2; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: OX2R,HYPOCRETIN RECEPTOR TYPE 2,GLYCOGEN SYNTHASE,CDNA, COMPND 6 FLJ95033,HOMO SAPIENS HYPOCRETIN (OREXIN) RECEPTOR 2 (HCRTR2),MRNA; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI GE5; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 272844; SOURCE 5 GENE: HCRTR2, PAB2292; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS 7TM, GPCR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.RAPPAS,A.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,M.CONGREVE, AUTHOR 2 R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,A.JAZAYERI, AUTHOR 3 F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,B.G.TEHAN,M.WEIR, AUTHOR 4 J.A.CHRISTOPHER REVDAT 3 11-MAR-20 6TPG 1 JRNL REVDAT 2 29-JAN-20 6TPG 1 JRNL REVDAT 1 01-JAN-20 6TPG 0 JRNL AUTH M.RAPPAS,A.A.E.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL, JRNL AUTH 2 M.CONGREVE,R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY, JRNL AUTH 3 A.JAZAYERI,F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL, JRNL AUTH 4 B.G.TEHAN,M.WEIR,J.A.CHRISTOPHER JRNL TITL COMPARISON OF OREXIN 1 AND OREXIN 2 LIGAND BINDING MODES JRNL TITL 2 USING X-RAY CRYSTALLOGRAPHY AND COMPUTATIONAL ANALYSIS. JRNL REF J.MED.CHEM. V. 63 1528 2020 JRNL REFN ISSN 0022-2623 JRNL PMID 31860301 JRNL DOI 10.1021/ACS.JMEDCHEM.9B01787 REMARK 2 REMARK 2 RESOLUTION. 2.74 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.55 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 68.6 REMARK 3 NUMBER OF REFLECTIONS : 11345 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.220 REMARK 3 R VALUE (WORKING SET) : 0.218 REMARK 3 FREE R VALUE : 0.275 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400 REMARK 3 FREE R VALUE TEST SET COUNT : 499 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 45.5458 - 4.3496 0.98 3998 181 0.2035 0.2680 REMARK 3 2 4.3496 - 3.4527 0.98 3876 174 0.2129 0.2499 REMARK 3 3 3.4527 - 3.0164 0.62 2432 109 0.2570 0.3244 REMARK 3 4 3.0164 - 2.7410 0.14 540 35 0.2963 0.4037 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.710 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.96 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 : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESID 37:388) REMARK 3 ORIGIN FOR THE GROUP (A): 92.6198 213.3954 0.3373 REMARK 3 T TENSOR REMARK 3 T11: 0.2126 T22: -0.0971 REMARK 3 T33: 0.5363 T12: -0.0204 REMARK 3 T13: -0.0087 T23: -0.0095 REMARK 3 L TENSOR REMARK 3 L11: 1.5133 L22: 1.2648 REMARK 3 L33: 0.8984 L12: -0.5774 REMARK 3 L13: -0.1694 L23: 0.5430 REMARK 3 S TENSOR REMARK 3 S11: -0.0496 S12: 0.0051 S13: 0.0389 REMARK 3 S21: -0.1740 S22: 0.0955 S23: -0.0611 REMARK 3 S31: -0.1246 S32: 0.0211 S33: -0.0083 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 1001:1196) REMARK 3 ORIGIN FOR THE GROUP (A): 117.1252 170.1043 -17.8166 REMARK 3 T TENSOR REMARK 3 T11: 0.3541 T22: 0.1258 REMARK 3 T33: 0.5613 T12: -0.0371 REMARK 3 T13: 0.0254 T23: -0.1120 REMARK 3 L TENSOR REMARK 3 L11: 1.4376 L22: 3.2923 REMARK 3 L33: 1.4208 L12: -0.7281 REMARK 3 L13: -0.4343 L23: -0.0424 REMARK 3 S TENSOR REMARK 3 S11: 0.0290 S12: 0.2233 S13: -0.2476 REMARK 3 S21: -0.3832 S22: -0.1836 S23: 0.3130 REMARK 3 S31: 0.0648 S32: -0.1226 S33: 0.1493 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 6TPG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-DEC-19. REMARK 100 THE DEPOSITION ID IS D_1292105847. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-SEP-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0-6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.96861 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11345 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740 REMARK 200 RESOLUTION RANGE LOW (A) : 45.550 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.1 REMARK 200 DATA REDUNDANCY : 8.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 5WQC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRISODIUM CITRATE BUFFER 150 REMARK 280 -300 MM SODIUM CHLORIDE 28-43 % (V/V) POLYETHYLENE GLYCOL 400, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z 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 38.90500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.90500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 45.54850 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 86.45700 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.54850 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 86.45700 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 38.90500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.54850 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 86.45700 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 38.90500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.54850 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 86.45700 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 860 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 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 GLN A -10 REMARK 465 ASP A -9 REMARK 465 LEU A -8 REMARK 465 ASP A -7 REMARK 465 TYR A -6 REMARK 465 LYS A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 LYS A 0 REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 GLY A 3 REMARK 465 THR A 4 REMARK 465 LYS A 5 REMARK 465 LEU A 6 REMARK 465 GLU A 7 REMARK 465 ASP A 8 REMARK 465 SER A 9 REMARK 465 PRO A 10 REMARK 465 PRO A 11 REMARK 465 CYS A 12 REMARK 465 ARG A 13 REMARK 465 ASP A 14 REMARK 465 TRP A 15 REMARK 465 SER A 16 REMARK 465 SER A 17 REMARK 465 ALA A 18 REMARK 465 SER A 19 REMARK 465 GLU A 20 REMARK 465 LEU A 21 REMARK 465 ASP A 22 REMARK 465 GLU A 23 REMARK 465 THR A 24 REMARK 465 GLN A 25 REMARK 465 GLU A 26 REMARK 465 PRO A 27 REMARK 465 LEU A 28 REMARK 465 LEU A 29 REMARK 465 ASP A 30 REMARK 465 PRO A 31 REMARK 465 THR A 32 REMARK 465 ASP A 33 REMARK 465 TYR A 34 REMARK 465 ASP A 35 REMARK 465 ASP A 36 REMARK 465 GLY A 199 REMARK 465 LEU A 200 REMARK 465 ALA A 201 REMARK 465 ASP A 202 REMARK 465 LYS A 203 REMARK 465 HIS A 389 REMARK 465 HIS A 390 REMARK 465 HIS A 391 REMARK 465 HIS A 392 REMARK 465 HIS A 393 REMARK 465 HIS A 394 REMARK 465 HIS A 395 REMARK 465 HIS A 396 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 TYR A 232 -69.43 -125.51 REMARK 500 GLN A1045 -89.91 -110.04 REMARK 500 ASP A1076 117.68 -29.41 REMARK 500 GLU A1122 83.95 -152.64 REMARK 500 PHE A 333 -11.27 82.25 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 OLA A 1203 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 7MA A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1203 DBREF 6TPG A 1 254 UNP O43614 OX2R_HUMAN 1 254 DBREF 6TPG A 1001 1196 UNP Q9V2J8 Q9V2J8_PYRAB 218 413 DBREF 6TPG A 294 388 UNP Q548Y0 Q548Y0_HUMAN 294 388 SEQADV 6TPG GLN A -10 UNP O43614 EXPRESSION TAG SEQADV 6TPG ASP A -9 UNP O43614 EXPRESSION TAG SEQADV 6TPG LEU A -8 UNP O43614 EXPRESSION TAG SEQADV 6TPG ASP A -7 UNP O43614 EXPRESSION TAG SEQADV 6TPG TYR A -6 UNP O43614 EXPRESSION TAG SEQADV 6TPG LYS A -5 UNP O43614 EXPRESSION TAG SEQADV 6TPG ASP A -4 UNP O43614 EXPRESSION TAG SEQADV 6TPG ASP A -3 UNP O43614 EXPRESSION TAG SEQADV 6TPG ASP A -2 UNP O43614 EXPRESSION TAG SEQADV 6TPG ASP A -1 UNP O43614 EXPRESSION TAG SEQADV 6TPG LYS A 0 UNP O43614 EXPRESSION TAG SEQADV 6TPG ASP A 14 UNP O43614 ASN 14 ENGINEERED MUTATION SEQADV 6TPG ASP A 22 UNP O43614 ASN 22 ENGINEERED MUTATION SEQADV 6TPG LEU A 28 UNP O43614 PHE 28 ENGINEERED MUTATION SEQADV 6TPG ASP A 30 UNP O43614 ASN 30 ENGINEERED MUTATION SEQADV 6TPG ALA A 54 UNP O43614 GLU 54 ENGINEERED MUTATION SEQADV 6TPG LEU A 91 UNP O43614 TYR 91 ENGINEERED MUTATION SEQADV 6TPG ALA A 100 UNP O43614 ASP 100 ENGINEERED MUTATION SEQADV 6TPG ALA A 142 UNP O43614 VAL 142 ENGINEERED MUTATION SEQADV 6TPG LEU A 170 UNP O43614 ARG 170 ENGINEERED MUTATION SEQADV 6TPG ASP A 202 UNP O43614 ASN 202 ENGINEERED MUTATION SEQADV 6TPG ALA A 206 UNP O43614 LEU 206 ENGINEERED MUTATION SEQADV 6TPG ALA A 219 UNP O43614 TYR 219 ENGINEERED MUTATION SEQADV 6TPG ALA A 233 UNP O43614 MET 233 ENGINEERED MUTATION SEQADV 6TPG LEU A 242 UNP O43614 ALA 242 ENGINEERED MUTATION SEQADV 6TPG VAL A 310 UNP Q548Y0 LEU 310 ENGINEERED MUTATION SEQADV 6TPG ALA A 318 UNP Q548Y0 LEU 318 ENGINEERED MUTATION SEQADV 6TPG ALA A 347 UNP Q548Y0 THR 347 ENGINEERED MUTATION SEQADV 6TPG TRP A 381 UNP Q548Y0 CYS 381 ENGINEERED MUTATION SEQADV 6TPG TRP A 382 UNP Q548Y0 CYS 382 ENGINEERED MUTATION SEQADV 6TPG TRP A 383 UNP Q548Y0 CYS 383 ENGINEERED MUTATION SEQADV 6TPG HIS A 389 UNP Q548Y0 EXPRESSION TAG SEQADV 6TPG HIS A 390 UNP Q548Y0 EXPRESSION TAG SEQADV 6TPG HIS A 391 UNP Q548Y0 EXPRESSION TAG SEQADV 6TPG HIS A 392 UNP Q548Y0 EXPRESSION TAG SEQADV 6TPG HIS A 393 UNP Q548Y0 EXPRESSION TAG SEQADV 6TPG HIS A 394 UNP Q548Y0 EXPRESSION TAG SEQADV 6TPG HIS A 395 UNP Q548Y0 EXPRESSION TAG SEQADV 6TPG HIS A 396 UNP Q548Y0 EXPRESSION TAG SEQRES 1 A 564 GLN ASP LEU ASP TYR LYS ASP ASP ASP ASP LYS MET SER SEQRES 2 A 564 GLY THR LYS LEU GLU ASP SER PRO PRO CYS ARG ASP TRP SEQRES 3 A 564 SER SER ALA SER GLU LEU ASP GLU THR GLN GLU PRO LEU SEQRES 4 A 564 LEU ASP PRO THR ASP TYR ASP ASP GLU GLU PHE LEU ARG SEQRES 5 A 564 TYR LEU TRP ARG GLU TYR LEU HIS PRO LYS GLU TYR ALA SEQRES 6 A 564 TRP VAL LEU ILE ALA GLY TYR ILE ILE VAL PHE VAL VAL SEQRES 7 A 564 ALA LEU ILE GLY ASN VAL LEU VAL CYS VAL ALA VAL TRP SEQRES 8 A 564 LYS ASN HIS HIS MET ARG THR VAL THR ASN LEU PHE ILE SEQRES 9 A 564 VAL ASN LEU SER LEU ALA ALA VAL LEU VAL THR ILE THR SEQRES 10 A 564 CYS LEU PRO ALA THR LEU VAL VAL ASP ILE THR GLU THR SEQRES 11 A 564 TRP PHE PHE GLY GLN SER LEU CYS LYS VAL ILE PRO TYR SEQRES 12 A 564 LEU GLN THR VAL SER VAL SER VAL SER ALA LEU THR LEU SEQRES 13 A 564 SER CYS ILE ALA LEU ASP ARG TRP TYR ALA ILE CYS HIS SEQRES 14 A 564 PRO LEU MET PHE LYS SER THR ALA LYS ARG ALA LEU ASN SEQRES 15 A 564 SER ILE VAL ILE ILE TRP ILE VAL SER CYS ILE ILE MET SEQRES 16 A 564 ILE PRO GLN ALA ILE VAL MET GLU CYS SER THR VAL PHE SEQRES 17 A 564 PRO GLY LEU ALA ASP LYS THR THR ALA PHE THR VAL CYS SEQRES 18 A 564 ASP GLU ARG TRP GLY GLY GLU ILE ALA PRO LYS MET TYR SEQRES 19 A 564 HIS ILE CYS PHE PHE LEU VAL THR TYR ALA ALA PRO LEU SEQRES 20 A 564 CYS LEU MET VAL LEU LEU TYR LEU GLN ILE PHE ARG LYS SEQRES 21 A 564 LEU TRP CYS ARG GLN GLY ILE ASP YCM SER PHE TRP ASN SEQRES 22 A 564 GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG LYS LYS SEQRES 23 A 564 SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY VAL THR SEQRES 24 A 564 PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN LYS GLY SEQRES 25 A 564 VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU SER SER SEQRES 26 A 564 LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE ILE GLY SEQRES 27 A 564 LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG SER LEU SEQRES 28 A 564 GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR GLU MET SEQRES 29 A 564 LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY SER VAL SEQRES 30 A 564 ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO PHE GLY SEQRES 31 A 564 LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA ILE PRO SEQRES 32 A 564 ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE ILE THR SEQRES 33 A 564 ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP PRO GLY SEQRES 34 A 564 GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU LEU SER SEQRES 35 A 564 ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS LYS LYS SEQRES 36 A 564 ARG ALA MET SER PHE SER LYS GLN ILE ARG ALA ARG ARG SEQRES 37 A 564 LYS THR ALA ARG MET LEU MET VAL VAL VAL LEU VAL PHE SEQRES 38 A 564 ALA ILE CYS TYR ALA PRO ILE SER ILE LEU ASN VAL LEU SEQRES 39 A 564 LYS ARG VAL PHE GLY MET PHE ALA HIS THR GLU ASP ARG SEQRES 40 A 564 GLU THR VAL TYR ALA TRP PHE ALA PHE SER HIS TRP LEU SEQRES 41 A 564 VAL TYR ALA ASN SER ALA ALA ASN PRO ILE ILE TYR ASN SEQRES 42 A 564 PHE LEU SER GLY LYS PHE ARG GLU GLU PHE LYS ALA ALA SEQRES 43 A 564 PHE SER TRP TRP TRP LEU GLY VAL HIS HIS HIS HIS HIS SEQRES 44 A 564 HIS HIS HIS HIS HIS MODRES 6TPG YCM A 1004 CYS MODIFIED RESIDUE HET YCM A1004 10 HET 7MA A1201 58 HET PG4 A1202 13 HET OLA A1203 11 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM 7MA N-ETHYL-2-[(6-METHOXYPYRIDIN-3-YL)-(2-METHYLPHENYL) HETNAM 2 7MA SULFONYL-AMINO]-N-(PYRIDIN-3-YLMETHYL)ETHANAMIDE HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM OLA OLEIC ACID HETSYN YCM CYSTEINE-S-ACETAMIDE FORMUL 1 YCM C5 H10 N2 O3 S FORMUL 2 7MA C23 H26 N4 O4 S FORMUL 3 PG4 C8 H18 O5 FORMUL 4 OLA C18 H34 O2 FORMUL 5 HOH *56(H2 O) HELIX 1 AA1 GLU A 37 GLU A 46 1 10 HELIX 2 AA2 TYR A 53 ASN A 82 1 30 HELIX 3 AA3 HIS A 83 ARG A 86 5 4 HELIX 4 AA4 THR A 87 CYS A 107 1 21 HELIX 5 AA5 CYS A 107 GLU A 118 1 12 HELIX 6 AA6 GLY A 123 CYS A 157 1 35 HELIX 7 AA7 THR A 165 MET A 184 1 20 HELIX 8 AA8 MET A 184 VAL A 190 1 7 HELIX 9 AA9 ILE A 218 TYR A 232 1 15 HELIX 10 AB1 TYR A 232 CYS A 252 1 21 HELIX 11 AB2 ASN A 1008 LEU A 1012 5 5 HELIX 12 AB3 SER A 1015 PHE A 1027 1 13 HELIX 13 AB4 GLY A 1047 SER A 1059 1 13 HELIX 14 AB5 SER A 1060 GLN A 1065 5 6 HELIX 15 AB6 ASP A 1076 HIS A 1090 1 15 HELIX 16 AB7 SER A 1101 GLY A 1110 1 10 HELIX 17 AB8 GLY A 1125 LEU A 1134 1 10 HELIX 18 AB9 VAL A 1143 ILE A 1150 1 8 HELIX 19 AC1 ASP A 1162 ARG A 1178 1 17 HELIX 20 AC2 LEU A 1181 VAL A 329 1 52 HELIX 21 AC3 ASP A 338 SER A 368 1 31 HELIX 22 AC4 SER A 368 LEU A 384 1 17 SHEET 1 AA1 2 MET A 191 SER A 194 0 SHEET 2 AA1 2 VAL A 209 GLU A 212 -1 O ASP A 211 N GLU A 192 SHEET 1 AA2 6 VAL A1093 ILE A1096 0 SHEET 2 AA2 6 MET A1067 ILE A1072 1 N ILE A1071 O LYS A1094 SHEET 3 AA2 6 VAL A1033 ILE A1038 1 N PHE A1037 O ILE A1072 SHEET 4 AA2 6 PHE A1114 ILE A1117 1 O ILE A1116 N MET A1036 SHEET 5 AA2 6 ILE A1137 SER A1141 1 O ILE A1139 N VAL A1115 SHEET 6 AA2 6 ILE A1156 VAL A1158 1 O ILE A1156 N PRO A1138 SSBOND 1 CYS A 127 CYS A 210 1555 1555 2.03 LINK C ASP A1003 N YCM A1004 1555 1555 1.33 LINK C YCM A1004 N SER A1005 1555 1555 1.33 SITE 1 AC1 10 GLN A 134 VAL A 138 PHE A 227 ILE A 320 SITE 2 AC1 10 SER A 321 ASN A 324 HIS A 350 TYR A 354 SITE 3 AC1 10 HOH A1312 HOH A1323 SITE 1 AC2 3 LYS A 327 PHE A 346 HOH A1313 SITE 1 AC3 1 ILE A 175 CRYST1 91.097 172.914 77.810 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010977 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005783 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012852 0.00000 ATOM 1 N GLU A 37 75.067 239.640 12.816 1.00 75.73 N ANISOU 1 N GLU A 37 9399 7414 11960 763 -575 -660 N ATOM 2 CA GLU A 37 75.038 238.419 12.019 1.00 74.58 C ANISOU 2 CA GLU A 37 9255 7321 11760 721 -562 -583 C ATOM 3 C GLU A 37 76.008 238.496 10.842 1.00 72.42 C ANISOU 3 C GLU A 37 9044 6993 11479 664 -548 -516 C ATOM 4 O GLU A 37 75.990 239.459 10.078 1.00 73.59 O ANISOU 4 O GLU A 37 9256 7049 11654 680 -554 -491 O ATOM 5 CB GLU A 37 73.622 238.148 11.510 1.00 78.00 C ANISOU 5 CB GLU A 37 9683 7770 12182 769 -584 -555 C ATOM 6 CG GLU A 37 73.466 236.809 10.809 1.00 80.77 C ANISOU 6 CG GLU A 37 10023 8182 12486 730 -576 -491 C ATOM 7 CD GLU A 37 72.044 236.564 10.350 1.00 85.52 C ANISOU 7 CD GLU A 37 10606 8798 13089 780 -603 -477 C ATOM 8 OE1 GLU A 37 71.786 236.657 9.129 1.00 87.41 O ANISOU 8 OE1 GLU A 37 10893 8999 13319 786 -625 -424 O ATOM 9 OE2 GLU A 37 71.181 236.291 11.215 1.00 86.90 O ANISOU 9 OE2 GLU A 37 10721 9023 13274 820 -601 -522 O ATOM 10 N GLU A 38 76.866 237.479 10.711 1.00 67.38 N ANISOU 10 N GLU A 38 8391 6408 10802 601 -523 -486 N ATOM 11 CA GLU A 38 77.834 237.455 9.615 1.00 62.85 C ANISOU 11 CA GLU A 38 7873 5791 10215 547 -501 -425 C ATOM 12 C GLU A 38 77.148 237.307 8.265 1.00 58.92 C ANISOU 12 C GLU A 38 7434 5266 9686 562 -510 -350 C ATOM 13 O GLU A 38 77.571 237.922 7.278 1.00 59.04 O ANISOU 13 O GLU A 38 7529 5200 9703 555 -497 -305 O ATOM 14 CB GLU A 38 78.831 236.312 9.819 1.00 60.77 C ANISOU 14 CB GLU A 38 7572 5601 9918 486 -474 -415 C ATOM 15 CG GLU A 38 79.890 236.182 8.723 1.00 59.64 C ANISOU 15 CG GLU A 38 7480 5423 9759 430 -445 -357 C ATOM 16 CD GLU A 38 80.858 237.353 8.708 1.00 60.03 C ANISOU 16 CD GLU A 38 7563 5382 9862 413 -427 -381 C ATOM 17 OE1 GLU A 38 80.870 238.124 9.692 1.00 60.46 O ANISOU 17 OE1 GLU A 38 7588 5415 9968 436 -441 -452 O ATOM 18 OE2 GLU A 38 81.603 237.510 7.716 1.00 60.03 O ANISOU 18 OE2 GLU A 38 7623 5329 9856 376 -397 -331 O ATOM 19 N PHE A 39 76.088 236.494 8.207 1.00 54.94 N ANISOU 19 N PHE A 39 6895 4825 9155 587 -531 -339 N ATOM 20 CA PHE A 39 75.441 236.188 6.933 1.00 51.10 C ANISOU 20 CA PHE A 39 6454 4324 8636 603 -546 -277 C ATOM 21 C PHE A 39 74.758 237.405 6.318 1.00 52.61 C ANISOU 21 C PHE A 39 6716 4422 8853 670 -571 -263 C ATOM 22 O PHE A 39 74.688 237.519 5.088 1.00 52.66 O ANISOU 22 O PHE A 39 6800 4380 8831 682 -573 -201 O ATOM 23 CB PHE A 39 74.434 235.052 7.112 1.00 46.23 C ANISOU 23 CB PHE A 39 5770 3792 8002 614 -566 -282 C ATOM 24 CG PHE A 39 73.740 234.661 5.837 1.00 42.58 C ANISOU 24 CG PHE A 39 5344 3322 7513 634 -591 -230 C ATOM 25 CD1 PHE A 39 74.440 234.050 4.812 1.00 40.43 C ANISOU 25 CD1 PHE A 39 5117 3049 7196 590 -574 -176 C ATOM 26 CD2 PHE A 39 72.389 234.912 5.662 1.00 41.87 C ANISOU 26 CD2 PHE A 39 5241 3225 7444 702 -633 -243 C ATOM 27 CE1 PHE A 39 73.812 233.699 3.635 1.00 39.63 C ANISOU 27 CE1 PHE A 39 5053 2938 7067 615 -600 -135 C ATOM 28 CE2 PHE A 39 71.751 234.562 4.482 1.00 41.17 C ANISOU 28 CE2 PHE A 39 5183 3128 7331 728 -664 -202 C ATOM 29 CZ PHE A 39 72.465 233.953 3.468 1.00 40.20 C ANISOU 29 CZ PHE A 39 5111 3003 7161 685 -648 -148 C ATOM 30 N LEU A 40 74.237 238.312 7.148 1.00 53.70 N ANISOU 30 N LEU A 40 6832 4532 9041 719 -588 -319 N ATOM 31 CA LEU A 40 73.662 239.543 6.623 1.00 33.92 C ANISOU 31 CA LEU A 40 4395 1927 6565 787 -609 -307 C ATOM 32 C LEU A 40 74.721 240.390 5.937 1.00 34.69 C ANISOU 32 C LEU A 40 4591 1920 6671 763 -574 -265 C ATOM 33 O LEU A 40 74.470 240.975 4.878 1.00 35.62 O ANISOU 33 O LEU A 40 4802 1953 6778 803 -575 -206 O ATOM 34 CB LEU A 40 73.005 240.332 7.752 1.00 36.68 C ANISOU 34 CB LEU A 40 4695 2269 6971 843 -631 -386 C ATOM 35 CG LEU A 40 71.715 239.773 8.341 1.00 34.29 C ANISOU 35 CG LEU A 40 4311 2048 6670 890 -661 -426 C ATOM 36 CD1 LEU A 40 71.114 240.774 9.322 1.00 35.27 C ANISOU 36 CD1 LEU A 40 4406 2146 6851 955 -679 -503 C ATOM 37 CD2 LEU A 40 70.747 239.450 7.221 1.00 34.47 C ANISOU 37 CD2 LEU A 40 4358 2070 6670 932 -694 -374 C ATOM 38 N ARG A 41 75.923 240.443 6.514 1.00 34.42 N ANISOU 38 N ARG A 41 4538 1884 6654 699 -541 -293 N ATOM 39 CA ARG A 41 76.997 241.192 5.877 1.00 35.21 C ANISOU 39 CA ARG A 41 4725 1882 6770 666 -500 -257 C ATOM 40 C ARG A 41 77.342 240.591 4.525 1.00 34.91 C ANISOU 40 C ARG A 41 4764 1834 6665 640 -475 -168 C ATOM 41 O ARG A 41 77.739 241.315 3.607 1.00 35.92 O ANISOU 41 O ARG A 41 5002 1855 6790 646 -445 -112 O ATOM 42 CB ARG A 41 78.236 241.231 6.781 1.00 48.10 C ANISOU 42 CB ARG A 41 6305 3529 8441 600 -474 -313 C ATOM 43 CG ARG A 41 77.992 241.708 8.215 1.00 47.48 C ANISOU 43 CG ARG A 41 6147 3473 8421 626 -499 -412 C ATOM 44 CD ARG A 41 79.291 242.100 8.926 1.00 46.65 C ANISOU 44 CD ARG A 41 6010 3345 8368 573 -475 -469 C ATOM 45 NE ARG A 41 79.850 243.356 8.428 1.00 47.28 N ANISOU 45 NE ARG A 41 6167 3286 8510 566 -451 -458 N ATOM 46 CZ ARG A 41 79.761 244.524 9.062 1.00 47.83 C ANISOU 46 CZ ARG A 41 6233 3278 8660 597 -463 -524 C ATOM 47 NH1 ARG A 41 79.134 244.612 10.229 1.00 47.06 N ANISOU 47 NH1 ARG A 41 6060 3236 8585 642 -501 -610 N ATOM 48 NH2 ARG A 41 80.307 245.611 8.529 1.00 49.41 N ANISOU 48 NH2 ARG A 41 6510 3342 8921 585 -435 -507 N ATOM 49 N TYR A 42 77.176 239.274 4.381 1.00 39.91 N ANISOU 49 N TYR A 42 5348 2573 7245 615 -484 -155 N ATOM 50 CA TYR A 42 77.434 238.625 3.101 1.00 39.93 C ANISOU 50 CA TYR A 42 5418 2573 7181 596 -464 -79 C ATOM 51 C TYR A 42 76.351 238.952 2.078 1.00 43.96 C ANISOU 51 C TYR A 42 6006 3033 7665 676 -491 -27 C ATOM 52 O TYR A 42 76.646 239.113 0.887 1.00 45.90 O ANISOU 52 O TYR A 42 6361 3211 7867 686 -463 44 O ATOM 53 CB TYR A 42 77.554 237.115 3.293 1.00 37.45 C ANISOU 53 CB TYR A 42 5021 2381 6827 548 -469 -88 C ATOM 54 CG TYR A 42 77.593 236.360 1.990 1.00 35.63 C ANISOU 54 CG TYR A 42 4850 2156 6529 540 -459 -21 C ATOM 55 CD1 TYR A 42 78.718 236.392 1.184 1.00 35.84 C ANISOU 55 CD1 TYR A 42 4957 2135 6525 497 -409 25 C ATOM 56 CD2 TYR A 42 76.498 235.625 1.559 1.00 35.29 C ANISOU 56 CD2 TYR A 42 4785 2164 6458 578 -501 -10 C ATOM 57 CE1 TYR A 42 78.757 235.710 -0.010 1.00 35.68 C ANISOU 57 CE1 TYR A 42 4999 2118 6439 496 -398 81 C ATOM 58 CE2 TYR A 42 76.525 234.944 0.367 1.00 35.11 C ANISOU 58 CE2 TYR A 42 4817 2145 6378 577 -496 43 C ATOM 59 CZ TYR A 42 77.658 234.989 -0.416 1.00 35.69 C ANISOU 59 CZ TYR A 42 4977 2172 6413 538 -443 89 C ATOM 60 OH TYR A 42 77.697 234.311 -1.614 1.00 36.39 O ANISOU 60 OH TYR A 42 5126 2260 6439 542 -435 139 O ATOM 61 N LEU A 43 75.089 239.043 2.514 1.00 45.63 N ANISOU 61 N LEU A 43 6163 3275 7900 739 -543 -61 N ATOM 62 CA LEU A 43 74.030 239.471 1.604 1.00 47.43 C ANISOU 62 CA LEU A 43 6457 3452 8114 829 -575 -18 C ATOM 63 C LEU A 43 74.268 240.894 1.136 1.00 49.62 C ANISOU 63 C LEU A 43 6852 3588 8414 875 -548 21 C ATOM 64 O LEU A 43 74.025 241.230 -0.028 1.00 49.99 O ANISOU 64 O LEU A 43 7006 3564 8426 932 -540 96 O ATOM 65 CB LEU A 43 72.674 239.376 2.291 1.00 35.22 C ANISOU 65 CB LEU A 43 4817 1963 6601 888 -635 -75 C ATOM 66 CG LEU A 43 72.199 238.019 2.785 1.00 33.88 C ANISOU 66 CG LEU A 43 4532 1920 6419 854 -661 -114 C ATOM 67 CD1 LEU A 43 70.856 238.198 3.466 1.00 34.22 C ANISOU 67 CD1 LEU A 43 4499 1997 6507 921 -711 -171 C ATOM 68 CD2 LEU A 43 72.105 237.043 1.626 1.00 33.40 C ANISOU 68 CD2 LEU A 43 4499 1891 6300 846 -669 -61 C ATOM 69 N TRP A 44 74.748 241.747 2.041 1.00 52.92 N ANISOU 69 N TRP A 44 7254 3959 8894 856 -532 -27 N ATOM 70 CA TRP A 44 75.068 243.123 1.693 1.00 56.33 C ANISOU 70 CA TRP A 44 7797 4244 9362 890 -501 4 C ATOM 71 C TRP A 44 76.244 243.205 0.735 1.00 57.98 C ANISOU 71 C TRP A 44 8122 4376 9532 840 -434 77 C ATOM 72 O TRP A 44 76.346 244.180 -0.012 1.00 60.05 O ANISOU 72 O TRP A 44 8514 4505 9796 883 -402 138 O ATOM 73 CB TRP A 44 75.358 243.944 2.953 1.00 57.77 C ANISOU 73 CB TRP A 44 7921 4399 9630 873 -503 -79 C ATOM 74 CG TRP A 44 74.129 244.403 3.673 1.00 59.00 C ANISOU 74 CG TRP A 44 8015 4571 9833 952 -558 -137 C ATOM 75 CD1 TRP A 44 72.968 243.711 3.829 1.00 57.75 C ANISOU 75 CD1 TRP A 44 7782 4509 9653 998 -609 -157 C ATOM 76 CD2 TRP A 44 73.935 245.668 4.321 1.00 61.88 C ANISOU 76 CD2 TRP A 44 8388 4847 10278 997 -565 -186 C ATOM 77 NE1 TRP A 44 72.062 244.459 4.540 1.00 59.14 N ANISOU 77 NE1 TRP A 44 7916 4666 9887 1069 -648 -216 N ATOM 78 CE2 TRP A 44 72.631 245.666 4.852 1.00 61.45 C ANISOU 78 CE2 TRP A 44 8259 4847 10241 1072 -622 -236 C ATOM 79 CE3 TRP A 44 74.741 246.801 4.506 1.00 64.17 C ANISOU 79 CE3 TRP A 44 8735 5013 10632 979 -530 -199 C ATOM 80 CZ2 TRP A 44 72.112 246.748 5.558 1.00 64.46 C ANISOU 80 CZ2 TRP A 44 8625 5168 10698 1133 -645 -297 C ATOM 81 CZ3 TRP A 44 74.222 247.876 5.207 1.00 66.30 C ANISOU 81 CZ3 TRP A 44 8990 5219 10981 1038 -554 -261 C ATOM 82 CH2 TRP A 44 72.922 247.839 5.727 1.00 66.12 C ANISOU 82 CH2 TRP A 44 8896 5258 10970 1116 -611 -309 C ATOM 83 N ARG A 45 77.137 242.216 0.745 1.00 57.07 N ANISOU 83 N ARG A 45 7967 4336 9380 752 -410 74 N ATOM 84 CA ARG A 45 78.259 242.193 -0.178 1.00 57.98 C ANISOU 84 CA ARG A 45 8188 4387 9454 702 -348 138 C ATOM 85 C ARG A 45 78.014 241.355 -1.422 1.00 59.35 C ANISOU 85 C ARG A 45 8428 4588 9535 724 -340 213 C ATOM 86 O ARG A 45 78.814 241.427 -2.357 1.00 60.34 O ANISOU 86 O ARG A 45 8669 4644 9614 700 -286 277 O ATOM 87 CB ARG A 45 79.507 241.652 0.515 1.00 55.90 C ANISOU 87 CB ARG A 45 7843 4184 9213 595 -322 89 C ATOM 88 CG ARG A 45 79.960 242.424 1.721 1.00 56.30 C ANISOU 88 CG ARG A 45 7824 4209 9357 567 -323 11 C ATOM 89 CD ARG A 45 81.301 241.896 2.188 1.00 55.70 C ANISOU 89 CD ARG A 45 7681 4182 9299 471 -291 -25 C ATOM 90 NE ARG A 45 81.194 241.008 3.342 1.00 54.15 N ANISOU 90 NE ARG A 45 7337 4124 9112 451 -325 -98 N ATOM 91 CZ ARG A 45 81.237 239.681 3.286 1.00 51.87 C ANISOU 91 CZ ARG A 45 6992 3950 8766 423 -331 -91 C ATOM 92 NH1 ARG A 45 81.376 239.064 2.119 1.00 51.16 N ANISOU 92 NH1 ARG A 45 6972 3861 8606 412 -310 -21 N ATOM 93 NH2 ARG A 45 81.134 238.974 4.406 1.00 50.34 N ANISOU 93 NH2 ARG A 45 6678 3866 8585 411 -358 -154 N ATOM 94 N GLU A 46 76.931 240.576 -1.462 1.00 60.88 N ANISOU 94 N GLU A 46 8553 4875 9703 770 -394 203 N ATOM 95 CA GLU A 46 76.802 239.515 -2.454 1.00 62.86 C ANISOU 95 CA GLU A 46 8828 5179 9876 774 -394 250 C ATOM 96 C GLU A 46 76.799 240.070 -3.874 1.00 64.89 C ANISOU 96 C GLU A 46 9251 5324 10079 842 -352 352 C ATOM 97 O GLU A 46 77.159 239.356 -4.816 1.00 64.55 O ANISOU 97 O GLU A 46 9263 5295 9967 831 -323 402 O ATOM 98 CB GLU A 46 75.534 238.699 -2.176 1.00 65.21 C ANISOU 98 CB GLU A 46 9014 5586 10176 815 -470 211 C ATOM 99 CG GLU A 46 75.349 237.494 -3.089 1.00 68.18 C ANISOU 99 CG GLU A 46 9390 6028 10486 814 -482 243 C ATOM 100 CD GLU A 46 73.941 236.912 -3.036 1.00 71.53 C ANISOU 100 CD GLU A 46 9727 6529 10921 873 -563 212 C ATOM 101 OE1 GLU A 46 72.977 237.680 -2.808 1.00 73.33 O ANISOU 101 OE1 GLU A 46 9945 6728 11188 950 -605 199 O ATOM 102 OE2 GLU A 46 73.802 235.681 -3.225 1.00 71.88 O ANISOU 102 OE2 GLU A 46 9711 6661 10940 841 -587 195 O ATOM 103 N TYR A 47 76.416 241.339 -4.048 1.00 67.27 N ANISOU 103 N TYR A 47 9639 5510 10410 918 -342 387 N ATOM 104 CA TYR A 47 76.389 241.932 -5.382 1.00 69.98 C ANISOU 104 CA TYR A 47 10149 5738 10703 997 -290 498 C ATOM 105 C TYR A 47 77.783 242.069 -5.996 1.00 71.56 C ANISOU 105 C TYR A 47 10482 5853 10854 929 -206 549 C ATOM 106 O TYR A 47 77.915 242.033 -7.226 1.00 72.51 O ANISOU 106 O TYR A 47 10732 5915 10903 977 -152 645 O ATOM 107 CB TYR A 47 75.702 243.301 -5.334 1.00 72.32 C ANISOU 107 CB TYR A 47 10505 5921 11052 1095 -295 525 C ATOM 108 CG TYR A 47 76.453 244.329 -4.512 1.00 73.85 C ANISOU 108 CG TYR A 47 10727 6022 11311 1040 -269 483 C ATOM 109 CD1 TYR A 47 76.209 244.478 -3.154 1.00 73.71 C ANISOU 109 CD1 TYR A 47 10571 6060 11374 1007 -321 378 C ATOM 110 CD2 TYR A 47 77.416 245.145 -5.093 1.00 75.60 C ANISOU 110 CD2 TYR A 47 11113 6097 11516 1020 -197 546 C ATOM 111 CE1 TYR A 47 76.903 245.405 -2.397 1.00 74.70 C ANISOU 111 CE1 TYR A 47 10705 6104 11574 959 -300 334 C ATOM 112 CE2 TYR A 47 78.116 246.079 -4.339 1.00 76.72 C ANISOU 112 CE2 TYR A 47 11265 6151 11734 961 -187 499 C ATOM 113 CZ TYR A 47 77.854 246.202 -2.988 1.00 76.24 C ANISOU 113 CZ TYR A 47 11048 6154 11765 933 -236 392 C ATOM 114 OH TYR A 47 78.533 247.122 -2.215 1.00 77.18 O ANISOU 114 OH TYR A 47 11158 6190 11975 880 -224 339 O ATOM 115 N LEU A 48 78.825 242.229 -5.168 1.00 72.11 N ANISOU 115 N LEU A 48 10515 5917 10967 821 -194 489 N ATOM 116 CA LEU A 48 80.176 242.496 -5.667 1.00 73.49 C ANISOU 116 CA LEU A 48 10808 6002 11112 745 -137 526 C ATOM 117 C LEU A 48 80.835 241.297 -6.349 1.00 72.31 C ANISOU 117 C LEU A 48 10670 5923 10881 689 -115 547 C ATOM 118 O LEU A 48 81.609 241.486 -7.293 1.00 73.02 O ANISOU 118 O LEU A 48 10908 5926 10908 667 -78 613 O ATOM 119 CB LEU A 48 81.068 242.993 -4.526 1.00 73.96 C ANISOU 119 CB LEU A 48 10782 6048 11270 647 -139 448 C ATOM 120 CG LEU A 48 80.824 244.439 -4.084 1.00 75.92 C ANISOU 120 CG LEU A 48 11074 6171 11600 687 -141 439 C ATOM 121 CD1 LEU A 48 81.394 244.704 -2.694 1.00 75.68 C ANISOU 121 CD1 LEU A 48 10896 6174 11684 609 -153 336 C ATOM 122 CD2 LEU A 48 81.384 245.432 -5.103 1.00 78.10 C ANISOU 122 CD2 LEU A 48 11557 6266 11850 697 -101 530 C ATOM 123 N HIS A 49 80.580 240.071 -5.898 1.00 70.82 N ANISOU 123 N HIS A 49 10332 5885 10691 659 -149 491 N ATOM 124 CA HIS A 49 81.162 238.878 -6.515 1.00 70.21 C ANISOU 124 CA HIS A 49 10256 5877 10543 609 -130 505 C ATOM 125 C HIS A 49 80.078 237.829 -6.702 1.00 69.70 C ANISOU 125 C HIS A 49 10105 5925 10453 665 -173 496 C ATOM 126 O HIS A 49 80.048 236.815 -5.996 1.00 68.50 O ANISOU 126 O HIS A 49 9808 5897 10323 611 -212 429 O ATOM 127 CB HIS A 49 82.320 238.322 -5.684 1.00 69.65 C ANISOU 127 CB HIS A 49 10072 5876 10514 486 -127 437 C ATOM 128 CG HIS A 49 83.488 239.253 -5.575 1.00 70.18 C ANISOU 128 CG HIS A 49 10198 5839 10626 419 -91 443 C ATOM 129 ND1 HIS A 49 84.720 238.982 -6.133 1.00 70.69 N ANISOU 129 ND1 HIS A 49 10312 5879 10668 339 -57 467 N ATOM 130 CD2 HIS A 49 83.608 240.456 -4.966 1.00 71.69 C ANISOU 130 CD2 HIS A 49 10394 5944 10901 416 -88 424 C ATOM 131 CE1 HIS A 49 85.547 239.979 -5.873 1.00 72.02 C ANISOU 131 CE1 HIS A 49 10500 5952 10912 286 -34 465 C ATOM 132 NE2 HIS A 49 84.897 240.887 -5.168 1.00 72.46 N ANISOU 132 NE2 HIS A 49 10535 5966 11032 333 -51 437 N ATOM 133 N PRO A 50 79.174 238.035 -7.662 1.00 70.91 N ANISOU 133 N PRO A 50 10335 6038 10570 776 -168 567 N ATOM 134 CA PRO A 50 78.126 237.036 -7.910 1.00 70.31 C ANISOU 134 CA PRO A 50 10162 6068 10486 825 -228 555 C ATOM 135 C PRO A 50 78.662 235.912 -8.786 1.00 70.29 C ANISOU 135 C PRO A 50 10183 6107 10415 796 -196 582 C ATOM 136 O PRO A 50 79.266 236.158 -9.832 1.00 71.44 O ANISOU 136 O PRO A 50 10464 6173 10505 817 -116 664 O ATOM 137 CB PRO A 50 77.029 237.839 -8.622 1.00 71.39 C ANISOU 137 CB PRO A 50 10355 6140 10632 962 -239 628 C ATOM 138 CG PRO A 50 77.734 239.061 -9.195 1.00 72.83 C ANISOU 138 CG PRO A 50 10708 6169 10796 988 -142 716 C ATOM 139 CD PRO A 50 79.153 239.110 -8.667 1.00 72.54 C ANISOU 139 CD PRO A 50 10711 6108 10741 857 -107 670 C ATOM 140 N LYS A 51 78.445 234.674 -8.350 1.00 68.81 N ANISOU 140 N LYS A 51 9864 6044 10236 747 -254 513 N ATOM 141 CA LYS A 51 78.928 233.495 -9.064 1.00 67.96 C ANISOU 141 CA LYS A 51 9762 5985 10075 713 -234 522 C ATOM 142 C LYS A 51 77.726 232.737 -9.616 1.00 66.75 C ANISOU 142 C LYS A 51 9545 5896 9921 786 -309 520 C ATOM 143 O LYS A 51 76.931 232.180 -8.853 1.00 65.14 O ANISOU 143 O LYS A 51 9213 5779 9757 774 -394 446 O ATOM 144 CB LYS A 51 79.778 232.618 -8.146 1.00 67.03 C ANISOU 144 CB LYS A 51 9544 5952 9974 593 -240 444 C ATOM 145 CG LYS A 51 81.048 233.304 -7.651 1.00 68.03 C ANISOU 145 CG LYS A 51 9714 6023 10111 517 -185 440 C ATOM 146 CD LYS A 51 81.859 232.415 -6.717 1.00 67.26 C ANISOU 146 CD LYS A 51 9487 6023 10046 414 -194 370 C ATOM 147 CE LYS A 51 82.420 233.208 -5.536 1.00 67.65 C ANISOU 147 CE LYS A 51 9476 6061 10168 366 -189 329 C ATOM 148 NZ LYS A 51 83.135 234.439 -5.967 1.00 69.14 N ANISOU 148 NZ LYS A 51 9798 6120 10352 361 -140 375 N ATOM 149 N GLU A 52 77.584 232.737 -10.941 1.00 67.99 N ANISOU 149 N GLU A 52 9784 6009 10038 864 -280 605 N ATOM 150 CA GLU A 52 76.483 232.035 -11.587 1.00 69.25 C ANISOU 150 CA GLU A 52 9882 6224 10208 937 -389 600 C ATOM 151 C GLU A 52 76.772 230.553 -11.769 1.00 67.49 C ANISOU 151 C GLU A 52 9598 6075 9969 874 -425 546 C ATOM 152 O GLU A 52 75.875 229.806 -12.174 1.00 67.77 O ANISOU 152 O GLU A 52 9569 6154 10025 916 -555 511 O ATOM 153 CB GLU A 52 76.162 232.675 -12.945 1.00 73.65 C ANISOU 153 CB GLU A 52 10524 6693 10767 1052 -417 716 C ATOM 154 CG GLU A 52 76.310 234.192 -12.966 1.00 77.56 C ANISOU 154 CG GLU A 52 11105 7081 11282 1102 -328 804 C ATOM 155 CD GLU A 52 75.185 234.925 -12.248 1.00 79.91 C ANISOU 155 CD GLU A 52 11356 7389 11618 1162 -403 764 C ATOM 156 OE1 GLU A 52 74.020 234.832 -12.695 1.00 81.35 O ANISOU 156 OE1 GLU A 52 11498 7597 11814 1254 -547 761 O ATOM 157 OE2 GLU A 52 75.473 235.609 -11.240 1.00 80.17 O ANISOU 157 OE2 GLU A 52 11397 7399 11664 1117 -340 727 O ATOM 158 N TYR A 53 77.994 230.116 -11.475 1.00 65.56 N ANISOU 158 N TYR A 53 9377 5845 9688 776 -323 530 N ATOM 159 CA TYR A 53 78.345 228.706 -11.496 1.00 63.60 C ANISOU 159 CA TYR A 53 9065 5670 9431 708 -346 473 C ATOM 160 C TYR A 53 78.169 228.038 -10.141 1.00 61.30 C ANISOU 160 C TYR A 53 8634 5475 9183 627 -394 376 C ATOM 161 O TYR A 53 78.632 226.910 -9.952 1.00 60.54 O ANISOU 161 O TYR A 53 8478 5439 9086 557 -395 331 O ATOM 162 CB TYR A 53 79.785 228.518 -12.010 1.00 64.07 C ANISOU 162 CB TYR A 53 9218 5688 9436 651 -231 511 C ATOM 163 CG TYR A 53 80.915 229.009 -11.110 1.00 64.39 C ANISOU 163 CG TYR A 53 9281 5709 9473 558 -172 489 C ATOM 164 CD1 TYR A 53 81.683 228.111 -10.371 1.00 63.29 C ANISOU 164 CD1 TYR A 53 9058 5644 9346 455 -180 422 C ATOM 165 CD2 TYR A 53 81.247 230.362 -11.040 1.00 66.34 C ANISOU 165 CD2 TYR A 53 9628 5863 9716 575 -120 537 C ATOM 166 CE1 TYR A 53 82.736 228.546 -9.566 1.00 63.21 C ANISOU 166 CE1 TYR A 53 9039 5626 9352 375 -149 402 C ATOM 167 CE2 TYR A 53 82.299 230.807 -10.236 1.00 65.91 C ANISOU 167 CE2 TYR A 53 9582 5790 9670 484 -98 507 C ATOM 168 CZ TYR A 53 83.041 229.894 -9.500 1.00 64.70 C ANISOU 168 CZ TYR A 53 9320 5722 9540 387 -115 440 C ATOM 169 OH TYR A 53 84.083 230.321 -8.700 1.00 63.86 O ANISOU 169 OH TYR A 53 9184 5611 9471 306 -99 413 O ATOM 170 N ALA A 54 77.519 228.715 -9.191 1.00 59.78 N ANISOU 170 N ALA A 54 8382 5292 9041 638 -435 348 N ATOM 171 CA ALA A 54 77.411 228.171 -7.842 1.00 56.81 C ANISOU 171 CA ALA A 54 7864 4998 8722 566 -470 272 C ATOM 172 C ALA A 54 76.645 226.858 -7.826 1.00 53.56 C ANISOU 172 C ALA A 54 7349 4668 8334 557 -539 217 C ATOM 173 O ALA A 54 76.966 225.960 -7.038 1.00 52.13 O ANISOU 173 O ALA A 54 7068 4554 8183 482 -537 171 O ATOM 174 CB ALA A 54 76.753 229.186 -6.910 1.00 56.88 C ANISOU 174 CB ALA A 54 7834 4995 8782 594 -498 255 C ATOM 175 N TRP A 55 75.654 226.710 -8.701 1.00 52.35 N ANISOU 175 N TRP A 55 7214 4506 8172 637 -600 223 N ATOM 176 CA TRP A 55 74.890 225.472 -8.694 1.00 49.41 C ANISOU 176 CA TRP A 55 6730 4193 7850 625 -688 158 C ATOM 177 C TRP A 55 75.763 224.286 -9.093 1.00 45.72 C ANISOU 177 C TRP A 55 6261 3751 7358 561 -654 148 C ATOM 178 O TRP A 55 75.606 223.191 -8.539 1.00 44.91 O ANISOU 178 O TRP A 55 6052 3713 7297 505 -673 93 O ATOM 179 CB TRP A 55 73.657 225.606 -9.599 1.00 51.05 C ANISOU 179 CB TRP A 55 6936 4365 8097 729 -824 149 C ATOM 180 CG TRP A 55 73.939 225.742 -11.073 1.00 51.65 C ANISOU 180 CG TRP A 55 7128 4374 8123 798 -855 204 C ATOM 181 CD1 TRP A 55 74.145 226.899 -11.771 1.00 52.32 C ANISOU 181 CD1 TRP A 55 7338 4383 8159 873 -827 291 C ATOM 182 CD2 TRP A 55 74.019 224.677 -12.030 1.00 52.15 C ANISOU 182 CD2 TRP A 55 7194 4437 8183 805 -924 179 C ATOM 183 NE1 TRP A 55 74.361 226.616 -13.101 1.00 53.20 N ANISOU 183 NE1 TRP A 55 7533 4452 8230 930 -876 330 N ATOM 184 CE2 TRP A 55 74.288 225.258 -13.283 1.00 53.30 C ANISOU 184 CE2 TRP A 55 7475 4511 8266 891 -942 255 C ATOM 185 CE3 TRP A 55 73.899 223.284 -11.943 1.00 51.81 C ANISOU 185 CE3 TRP A 55 7053 4445 8188 750 -972 100 C ATOM 186 CZ2 TRP A 55 74.436 224.495 -14.439 1.00 55.24 C ANISOU 186 CZ2 TRP A 55 7768 4737 8482 929 -1020 247 C ATOM 187 CZ3 TRP A 55 74.049 222.530 -13.087 1.00 52.65 C ANISOU 187 CZ3 TRP A 55 7200 4527 8279 782 -1043 84 C ATOM 188 CH2 TRP A 55 74.314 223.134 -14.319 1.00 54.26 C ANISOU 188 CH2 TRP A 55 7547 4663 8407 874 -1073 153 C ATOM 189 N VAL A 56 76.724 224.500 -9.998 1.00 42.73 N ANISOU 189 N VAL A 56 6000 3318 6919 567 -594 204 N ATOM 190 CA VAL A 56 77.551 223.401 -10.495 1.00 40.61 C ANISOU 190 CA VAL A 56 5737 3065 6629 514 -566 192 C ATOM 191 C VAL A 56 78.481 222.901 -9.397 1.00 37.57 C ANISOU 191 C VAL A 56 5291 2743 6240 413 -492 166 C ATOM 192 O VAL A 56 78.599 221.695 -9.153 1.00 36.32 O ANISOU 192 O VAL A 56 5050 2641 6108 363 -506 121 O ATOM 193 CB VAL A 56 78.346 223.848 -11.735 1.00 41.39 C ANISOU 193 CB VAL A 56 5978 3077 6672 551 -519 264 C ATOM 194 CG1 VAL A 56 78.912 222.646 -12.483 1.00 28.53 C ANISOU 194 CG1 VAL A 56 4351 1452 5037 521 -528 243 C ATOM 195 CG2 VAL A 56 77.485 224.710 -12.639 1.00 43.34 C ANISOU 195 CG2 VAL A 56 6291 3253 6924 668 -602 314 C ATOM 196 N LEU A 57 79.166 223.827 -8.723 1.00 36.23 N ANISOU 196 N LEU A 57 5144 2553 6068 387 -440 191 N ATOM 197 CA LEU A 57 80.032 223.458 -7.613 1.00 33.50 C ANISOU 197 CA LEU A 57 4714 2261 5752 305 -407 164 C ATOM 198 C LEU A 57 79.227 222.820 -6.494 1.00 32.17 C ANISOU 198 C LEU A 57 4397 2170 5655 286 -459 113 C ATOM 199 O LEU A 57 79.694 221.877 -5.843 1.00 31.13 O ANISOU 199 O LEU A 57 4178 2100 5551 231 -445 86 O ATOM 200 CB LEU A 57 80.769 224.695 -7.113 1.00 31.93 C ANISOU 200 CB LEU A 57 4564 2020 5550 292 -357 192 C ATOM 201 CG LEU A 57 81.972 224.501 -6.205 1.00 29.13 C ANISOU 201 CG LEU A 57 4149 1705 5215 219 -312 174 C ATOM 202 CD1 LEU A 57 83.081 223.825 -6.979 1.00 28.36 C ANISOU 202 CD1 LEU A 57 4106 1599 5072 181 -264 186 C ATOM 203 CD2 LEU A 57 82.428 225.826 -5.646 1.00 28.89 C ANISOU 203 CD2 LEU A 57 4151 1626 5199 217 -283 188 C ATOM 204 N ILE A 58 77.995 223.289 -6.290 1.00 31.63 N ANISOU 204 N ILE A 58 4301 2096 5620 337 -515 101 N ATOM 205 CA ILE A 58 77.150 222.706 -5.255 1.00 30.89 C ANISOU 205 CA ILE A 58 4074 2066 5598 321 -556 54 C ATOM 206 C ILE A 58 76.744 221.288 -5.634 1.00 30.44 C ANISOU 206 C ILE A 58 3954 2047 5563 304 -588 20 C ATOM 207 O ILE A 58 76.857 220.358 -4.827 1.00 29.79 O ANISOU 207 O ILE A 58 3771 2021 5526 255 -575 -5 O ATOM 208 CB ILE A 58 75.919 223.589 -4.995 1.00 25.54 C ANISOU 208 CB ILE A 58 3385 1367 4952 382 -608 44 C ATOM 209 CG1 ILE A 58 76.362 224.922 -4.380 1.00 25.86 C ANISOU 209 CG1 ILE A 58 3468 1373 4987 390 -572 68 C ATOM 210 CG2 ILE A 58 74.912 222.823 -4.118 1.00 25.13 C ANISOU 210 CG2 ILE A 58 3198 1374 4977 369 -647 -7 C ATOM 211 CD1 ILE A 58 75.239 225.929 -4.202 1.00 26.61 C ANISOU 211 CD1 ILE A 58 3567 1436 5108 459 -618 63 C ATOM 212 N ALA A 59 76.251 221.097 -6.859 1.00 25.09 N ANISOU 212 N ALA A 59 3337 1336 4861 350 -629 19 N ATOM 213 CA ALA A 59 75.856 219.752 -7.251 1.00 25.52 C ANISOU 213 CA ALA A 59 3331 1420 4946 334 -665 -25 C ATOM 214 C ALA A 59 77.055 218.822 -7.252 1.00 25.92 C ANISOU 214 C ALA A 59 3375 1496 4978 269 -608 -21 C ATOM 215 O ALA A 59 76.946 217.655 -6.860 1.00 26.23 O ANISOU 215 O ALA A 59 3319 1579 5069 229 -612 -55 O ATOM 216 CB ALA A 59 75.191 219.773 -8.622 1.00 26.66 C ANISOU 216 CB ALA A 59 3516 1500 5112 403 -765 -38 C ATOM 217 N GLY A 60 78.225 219.343 -7.621 1.00 25.52 N ANISOU 217 N GLY A 60 3421 1415 4861 259 -548 21 N ATOM 218 CA GLY A 60 79.416 218.517 -7.624 1.00 23.76 C ANISOU 218 CA GLY A 60 3192 1216 4620 202 -494 22 C ATOM 219 C GLY A 60 79.835 218.128 -6.227 1.00 23.81 C ANISOU 219 C GLY A 60 3087 1286 4676 152 -466 12 C ATOM 220 O GLY A 60 80.287 217.003 -6.001 1.00 23.68 O ANISOU 220 O GLY A 60 3008 1308 4680 115 -448 -6 O ATOM 221 N TYR A 61 79.657 219.037 -5.264 1.00 23.63 N ANISOU 221 N TYR A 61 3036 1269 4672 158 -461 22 N ATOM 222 CA TYR A 61 79.942 218.711 -3.872 1.00 22.79 C ANISOU 222 CA TYR A 61 2827 1221 4612 125 -436 12 C ATOM 223 C TYR A 61 78.884 217.788 -3.282 1.00 22.86 C ANISOU 223 C TYR A 61 2726 1268 4690 123 -467 -18 C ATOM 224 O TYR A 61 79.207 216.899 -2.488 1.00 22.46 O ANISOU 224 O TYR A 61 2596 1263 4674 93 -439 -25 O ATOM 225 CB TYR A 61 80.069 219.991 -3.046 1.00 22.96 C ANISOU 225 CB TYR A 61 2859 1230 4635 137 -422 25 C ATOM 226 CG TYR A 61 81.494 220.515 -2.943 1.00 22.86 C ANISOU 226 CG TYR A 61 2894 1204 4587 112 -367 44 C ATOM 227 CD1 TYR A 61 82.052 221.290 -3.953 1.00 23.09 C ANISOU 227 CD1 TYR A 61 3041 1170 4563 121 -346 72 C ATOM 228 CD2 TYR A 61 82.279 220.231 -1.828 1.00 22.49 C ANISOU 228 CD2 TYR A 61 2777 1204 4565 84 -334 34 C ATOM 229 CE1 TYR A 61 83.349 221.761 -3.858 1.00 23.15 C ANISOU 229 CE1 TYR A 61 3085 1160 4551 93 -294 85 C ATOM 230 CE2 TYR A 61 83.572 220.703 -1.723 1.00 22.45 C ANISOU 230 CE2 TYR A 61 2803 1186 4540 63 -291 43 C ATOM 231 CZ TYR A 61 84.105 221.465 -2.738 1.00 23.18 C ANISOU 231 CZ TYR A 61 3003 1215 4589 63 -271 66 C ATOM 232 OH TYR A 61 85.404 221.932 -2.627 1.00 23.82 O ANISOU 232 OH TYR A 61 3109 1278 4664 37 -224 70 O ATOM 233 N ILE A 62 77.616 217.966 -3.649 1.00 23.54 N ANISOU 233 N ILE A 62 2806 1334 4804 157 -523 -37 N ATOM 234 CA ILE A 62 76.606 217.054 -3.117 1.00 24.60 C ANISOU 234 CA ILE A 62 2831 1497 5017 149 -546 -69 C ATOM 235 C ILE A 62 76.862 215.642 -3.615 1.00 25.04 C ANISOU 235 C ILE A 62 2854 1568 5091 121 -540 -86 C ATOM 236 O ILE A 62 76.761 214.666 -2.860 1.00 24.83 O ANISOU 236 O ILE A 62 2736 1576 5123 94 -515 -95 O ATOM 237 CB ILE A 62 75.185 217.520 -3.483 1.00 25.15 C ANISOU 237 CB ILE A 62 2894 1539 5121 195 -613 -96 C ATOM 238 CG1 ILE A 62 74.915 218.905 -2.893 1.00 26.44 C ANISOU 238 CG1 ILE A 62 3086 1687 5274 227 -615 -81 C ATOM 239 CG2 ILE A 62 74.171 216.481 -3.008 1.00 24.22 C ANISOU 239 CG2 ILE A 62 2658 1445 5099 181 -630 -135 C ATOM 240 CD1 ILE A 62 73.553 219.468 -3.233 1.00 27.75 C ANISOU 240 CD1 ILE A 62 3249 1823 5471 283 -683 -107 C ATOM 241 N ILE A 63 77.236 215.519 -4.888 1.00 26.32 N ANISOU 241 N ILE A 63 3098 1700 5203 130 -557 -88 N ATOM 242 CA ILE A 63 77.505 214.212 -5.479 1.00 26.42 C ANISOU 242 CA ILE A 63 3089 1719 5231 107 -556 -112 C ATOM 243 C ILE A 63 78.714 213.566 -4.810 1.00 26.98 C ANISOU 243 C ILE A 63 3129 1827 5295 66 -489 -92 C ATOM 244 O ILE A 63 78.664 212.406 -4.376 1.00 27.29 O ANISOU 244 O ILE A 63 3086 1892 5391 44 -472 -107 O ATOM 245 CB ILE A 63 77.712 214.362 -6.999 1.00 26.28 C ANISOU 245 CB ILE A 63 3184 1653 5149 132 -583 -120 C ATOM 246 CG1 ILE A 63 76.407 214.757 -7.696 1.00 26.77 C ANISOU 246 CG1 ILE A 63 3255 1676 5242 186 -669 -152 C ATOM 247 CG2 ILE A 63 78.323 213.110 -7.608 1.00 25.86 C ANISOU 247 CG2 ILE A 63 3127 1604 5095 104 -568 -143 C ATOM 248 CD1 ILE A 63 76.562 214.945 -9.196 1.00 27.53 C ANISOU 248 CD1 ILE A 63 3443 1704 5314 229 -728 -162 C ATOM 249 N VAL A 64 79.816 214.317 -4.697 1.00 26.95 N ANISOU 249 N VAL A 64 3191 1822 5229 61 -448 -59 N ATOM 250 CA VAL A 64 81.013 213.767 -4.066 1.00 26.49 C ANISOU 250 CA VAL A 64 3103 1798 5165 30 -391 -46 C ATOM 251 C VAL A 64 80.765 213.448 -2.604 1.00 26.03 C ANISOU 251 C VAL A 64 2945 1782 5165 23 -370 -42 C ATOM 252 O VAL A 64 81.305 212.468 -2.084 1.00 25.26 O ANISOU 252 O VAL A 64 2795 1711 5091 6 -336 -41 O ATOM 253 CB VAL A 64 82.207 214.726 -4.220 1.00 26.50 C ANISOU 253 CB VAL A 64 3186 1782 5099 26 -354 -19 C ATOM 254 CG1 VAL A 64 83.296 214.368 -3.230 1.00 25.76 C ANISOU 254 CG1 VAL A 64 3041 1729 5016 4 -306 -12 C ATOM 255 CG2 VAL A 64 82.746 214.670 -5.638 1.00 27.30 C ANISOU 255 CG2 VAL A 64 3389 1841 5143 26 -350 -19 C ATOM 256 N PHE A 65 79.949 214.248 -1.916 1.00 27.28 N ANISOU 256 N PHE A 65 3081 1940 5345 40 -386 -39 N ATOM 257 CA PHE A 65 79.712 213.997 -0.500 1.00 28.24 C ANISOU 257 CA PHE A 65 3121 2094 5514 36 -358 -34 C ATOM 258 C PHE A 65 78.986 212.676 -0.289 1.00 30.74 C ANISOU 258 C PHE A 65 3356 2421 5903 25 -354 -48 C ATOM 259 O PHE A 65 79.336 211.898 0.607 1.00 32.95 O ANISOU 259 O PHE A 65 3585 2723 6210 14 -310 -36 O ATOM 260 CB PHE A 65 78.913 215.138 0.117 1.00 27.66 C ANISOU 260 CB PHE A 65 3045 2012 5451 58 -377 -35 C ATOM 261 CG PHE A 65 78.551 214.905 1.551 1.00 26.47 C ANISOU 261 CG PHE A 65 2823 1887 5347 56 -346 -31 C ATOM 262 CD1 PHE A 65 77.423 214.173 1.885 1.00 26.05 C ANISOU 262 CD1 PHE A 65 2697 1834 5365 55 -347 -43 C ATOM 263 CD2 PHE A 65 79.340 215.415 2.571 1.00 25.90 C ANISOU 263 CD2 PHE A 65 2758 1832 5250 57 -312 -19 C ATOM 264 CE1 PHE A 65 77.087 213.955 3.208 1.00 25.41 C ANISOU 264 CE1 PHE A 65 2564 1768 5324 55 -306 -35 C ATOM 265 CE2 PHE A 65 79.008 215.202 3.897 1.00 25.16 C ANISOU 265 CE2 PHE A 65 2614 1755 5191 60 -280 -15 C ATOM 266 CZ PHE A 65 77.879 214.470 4.214 1.00 24.86 C ANISOU 266 CZ PHE A 65 2514 1714 5216 60 -273 -19 C ATOM 267 N VAL A 66 77.972 212.400 -1.108 1.00 30.57 N ANISOU 267 N VAL A 66 3322 2375 5917 32 -399 -75 N ATOM 268 CA VAL A 66 77.214 211.168 -0.929 1.00 30.27 C ANISOU 268 CA VAL A 66 3199 2337 5965 21 -394 -94 C ATOM 269 C VAL A 66 78.068 209.965 -1.317 1.00 28.16 C ANISOU 269 C VAL A 66 2928 2074 5696 1 -367 -95 C ATOM 270 O VAL A 66 78.170 208.983 -0.570 1.00 27.96 O ANISOU 270 O VAL A 66 2843 2060 5721 -11 -321 -85 O ATOM 271 CB VAL A 66 75.894 211.237 -1.724 1.00 31.87 C ANISOU 271 CB VAL A 66 3383 2510 6216 36 -458 -135 C ATOM 272 CG1 VAL A 66 75.152 209.907 -1.682 1.00 22.44 C ANISOU 272 CG1 VAL A 66 2096 1306 5123 21 -451 -165 C ATOM 273 CG2 VAL A 66 75.019 212.346 -1.162 1.00 32.46 C ANISOU 273 CG2 VAL A 66 3450 2580 6304 58 -478 -135 C ATOM 274 N VAL A 67 78.755 210.056 -2.458 1.00 26.51 N ANISOU 274 N VAL A 67 2792 1852 5427 1 -388 -105 N ATOM 275 CA VAL A 67 79.554 208.933 -2.944 1.00 24.68 C ANISOU 275 CA VAL A 67 2562 1619 5196 -16 -367 -113 C ATOM 276 C VAL A 67 80.766 208.693 -2.048 1.00 24.05 C ANISOU 276 C VAL A 67 2476 1569 5093 -26 -307 -81 C ATOM 277 O VAL A 67 81.119 207.544 -1.755 1.00 24.49 O ANISOU 277 O VAL A 67 2489 1629 5187 -37 -274 -80 O ATOM 278 CB VAL A 67 79.975 209.179 -4.402 1.00 23.56 C ANISOU 278 CB VAL A 67 2511 1450 4990 -13 -401 -134 C ATOM 279 CG1 VAL A 67 80.909 208.066 -4.892 1.00 23.09 C ANISOU 279 CG1 VAL A 67 2458 1388 4926 -30 -374 -146 C ATOM 280 CG2 VAL A 67 78.746 209.303 -5.286 1.00 23.49 C ANISOU 280 CG2 VAL A 67 2508 1408 5008 4 -468 -174 C ATOM 281 N ALA A 68 81.426 209.765 -1.598 1.00 23.10 N ANISOU 281 N ALA A 68 2399 1464 4915 -20 -293 -56 N ATOM 282 CA ALA A 68 82.576 209.582 -0.720 1.00 22.71 C ANISOU 282 CA ALA A 68 2341 1440 4849 -26 -245 -34 C ATOM 283 C ALA A 68 82.151 208.975 0.612 1.00 23.21 C ANISOU 283 C ALA A 68 2331 1518 4968 -24 -213 -18 C ATOM 284 O ALA A 68 82.763 208.011 1.088 1.00 23.44 O ANISOU 284 O ALA A 68 2335 1555 5017 -30 -177 -8 O ATOM 285 CB ALA A 68 83.296 210.911 -0.507 1.00 22.19 C ANISOU 285 CB ALA A 68 2330 1381 4722 -20 -241 -20 C ATOM 286 N LEU A 69 81.081 209.504 1.214 1.00 23.35 N ANISOU 286 N LEU A 69 2321 1535 5015 -15 -222 -15 N ATOM 287 CA LEU A 69 80.630 208.990 2.504 1.00 23.52 C ANISOU 287 CA LEU A 69 2285 1563 5087 -13 -182 4 C ATOM 288 C LEU A 69 80.099 207.571 2.380 1.00 24.92 C ANISOU 288 C LEU A 69 2407 1721 5339 -23 -162 0 C ATOM 289 O LEU A 69 80.356 206.732 3.255 1.00 25.31 O ANISOU 289 O LEU A 69 2429 1769 5417 -26 -112 25 O ATOM 290 CB LEU A 69 79.564 209.902 3.090 1.00 22.66 C ANISOU 290 CB LEU A 69 2162 1452 4997 -1 -194 4 C ATOM 291 CG LEU A 69 79.013 209.516 4.460 1.00 21.91 C ANISOU 291 CG LEU A 69 2020 1356 4948 2 -144 26 C ATOM 292 CD1 LEU A 69 80.105 209.597 5.499 1.00 21.36 C ANISOU 292 CD1 LEU A 69 1979 1304 4832 8 -106 52 C ATOM 293 CD2 LEU A 69 77.864 210.418 4.830 1.00 21.95 C ANISOU 293 CD2 LEU A 69 2010 1354 4977 15 -160 17 C ATOM 294 N ILE A 70 79.374 207.276 1.296 1.00 26.28 N ANISOU 294 N ILE A 70 2565 1872 5547 -28 -201 -32 N ATOM 295 CA ILE A 70 78.773 205.952 1.159 1.00 27.83 C ANISOU 295 CA ILE A 70 2701 2042 5832 -38 -183 -46 C ATOM 296 C ILE A 70 79.834 204.915 0.820 1.00 28.89 C ANISOU 296 C ILE A 70 2848 2172 5958 -48 -161 -45 C ATOM 297 O ILE A 70 79.902 203.843 1.438 1.00 30.05 O ANISOU 297 O ILE A 70 2955 2303 6158 -53 -112 -27 O ATOM 298 CB ILE A 70 77.658 205.973 0.103 1.00 27.88 C ANISOU 298 CB ILE A 70 2686 2023 5886 -39 -240 -93 C ATOM 299 CG1 ILE A 70 76.533 206.911 0.537 1.00 28.47 C ANISOU 299 CG1 ILE A 70 2736 2097 5983 -27 -260 -96 C ATOM 300 CG2 ILE A 70 77.112 204.569 -0.125 1.00 28.20 C ANISOU 300 CG2 ILE A 70 2659 2030 6027 -51 -223 -118 C ATOM 301 CD1 ILE A 70 75.445 206.221 1.339 1.00 29.33 C ANISOU 301 CD1 ILE A 70 2758 2185 6202 -32 -219 -96 C ATOM 302 N GLY A 71 80.695 205.228 -0.149 1.00 27.95 N ANISOU 302 N GLY A 71 2788 2061 5772 -49 -191 -61 N ATOM 303 CA GLY A 71 81.671 204.247 -0.581 1.00 28.20 C ANISOU 303 CA GLY A 71 2830 2083 5799 -57 -174 -68 C ATOM 304 C GLY A 71 82.688 203.915 0.492 1.00 28.05 C ANISOU 304 C GLY A 71 2811 2082 5766 -55 -122 -31 C ATOM 305 O GLY A 71 83.127 202.767 0.609 1.00 27.89 O ANISOU 305 O GLY A 71 2769 2044 5782 -60 -92 -28 O ATOM 306 N ASN A 72 83.081 204.909 1.288 1.00 29.30 N ANISOU 306 N ASN A 72 2994 2268 5871 -46 -114 -5 N ATOM 307 CA ASN A 72 84.108 204.678 2.298 1.00 28.67 C ANISOU 307 CA ASN A 72 2921 2202 5771 -40 -74 24 C ATOM 308 C ASN A 72 83.552 203.985 3.530 1.00 28.35 C ANISOU 308 C ASN A 72 2840 2148 5785 -36 -29 58 C ATOM 309 O ASN A 72 84.288 203.274 4.227 1.00 29.02 O ANISOU 309 O ASN A 72 2928 2226 5873 -32 7 82 O ATOM 310 CB ASN A 72 84.777 205.993 2.673 1.00 27.32 C ANISOU 310 CB ASN A 72 2791 2058 5530 -32 -85 30 C ATOM 311 CG ASN A 72 85.729 206.460 1.605 1.00 27.68 C ANISOU 311 CG ASN A 72 2884 2109 5523 -37 -107 8 C ATOM 312 OD1 ASN A 72 86.772 205.846 1.388 1.00 27.11 O ANISOU 312 OD1 ASN A 72 2820 2036 5444 -41 -92 3 O ATOM 313 ND2 ASN A 72 85.367 207.533 0.908 1.00 27.50 N ANISOU 313 ND2 ASN A 72 2897 2085 5466 -37 -139 -4 N ATOM 314 N VAL A 73 82.267 204.172 3.819 1.00 28.53 N ANISOU 314 N VAL A 73 2829 2160 5852 -36 -26 61 N ATOM 315 CA VAL A 73 81.672 203.412 4.908 1.00 28.58 C ANISOU 315 CA VAL A 73 2800 2142 5918 -34 29 96 C ATOM 316 C VAL A 73 81.636 201.927 4.563 1.00 27.33 C ANISOU 316 C VAL A 73 2609 1944 5831 -44 56 95 C ATOM 317 O VAL A 73 81.961 201.074 5.396 1.00 26.96 O ANISOU 317 O VAL A 73 2560 1874 5807 -41 108 133 O ATOM 318 CB VAL A 73 80.278 203.969 5.228 1.00 29.11 C ANISOU 318 CB VAL A 73 2834 2203 6025 -32 30 95 C ATOM 319 CG1 VAL A 73 79.490 202.973 6.043 1.00 30.21 C ANISOU 319 CG1 VAL A 73 2927 2302 6249 -35 95 127 C ATOM 320 CG2 VAL A 73 80.424 205.271 5.991 1.00 28.91 C ANISOU 320 CG2 VAL A 73 2845 2207 5934 -18 22 107 C ATOM 321 N LEU A 74 81.316 201.598 3.312 1.00 26.67 N ANISOU 321 N LEU A 74 2506 1847 5781 -56 19 50 N ATOM 322 CA LEU A 74 81.318 200.199 2.901 1.00 26.14 C ANISOU 322 CA LEU A 74 2408 1737 5788 -67 40 39 C ATOM 323 C LEU A 74 82.714 199.592 2.944 1.00 25.14 C ANISOU 323 C LEU A 74 2314 1611 5625 -64 55 51 C ATOM 324 O LEU A 74 82.858 198.405 3.262 1.00 25.12 O ANISOU 324 O LEU A 74 2294 1569 5683 -68 97 69 O ATOM 325 CB LEU A 74 80.745 200.070 1.494 1.00 26.13 C ANISOU 325 CB LEU A 74 2387 1720 5820 -77 -12 -22 C ATOM 326 CG LEU A 74 79.342 200.619 1.287 1.00 25.30 C ANISOU 326 CG LEU A 74 2245 1610 5760 -78 -40 -46 C ATOM 327 CD1 LEU A 74 79.027 200.614 -0.193 1.00 25.12 C ANISOU 327 CD1 LEU A 74 2224 1575 5746 -84 -106 -111 C ATOM 328 CD2 LEU A 74 78.324 199.795 2.061 1.00 25.46 C ANISOU 328 CD2 LEU A 74 2196 1585 5892 -85 17 -30 C ATOM 329 N VAL A 75 83.754 200.378 2.634 1.00 24.05 N ANISOU 329 N VAL A 75 2226 1512 5399 -58 25 42 N ATOM 330 CA VAL A 75 85.108 199.828 2.674 1.00 22.33 C ANISOU 330 CA VAL A 75 2035 1294 5155 -54 38 49 C ATOM 331 C VAL A 75 85.458 199.411 4.089 1.00 39.95 C ANISOU 331 C VAL A 75 4273 3515 7393 -43 87 103 C ATOM 332 O VAL A 75 86.046 198.347 4.315 1.00 39.68 O ANISOU 332 O VAL A 75 4239 3449 7389 -40 115 118 O ATOM 333 CB VAL A 75 86.135 200.836 2.126 1.00 21.67 C ANISOU 333 CB VAL A 75 1999 1250 4984 -51 3 28 C ATOM 334 CG1 VAL A 75 87.543 200.267 2.225 1.00 21.64 C ANISOU 334 CG1 VAL A 75 2015 1244 4964 -46 18 31 C ATOM 335 CG2 VAL A 75 85.810 201.201 0.691 1.00 25.12 C ANISOU 335 CG2 VAL A 75 2450 1688 5408 -61 -41 -18 C ATOM 336 N CYS A 76 85.086 200.232 5.069 1.00 39.86 N ANISOU 336 N CYS A 76 4272 3523 7351 -32 98 133 N ATOM 337 CA CYS A 76 85.282 199.834 6.454 1.00 38.95 C ANISOU 337 CA CYS A 76 4173 3389 7236 -17 147 188 C ATOM 338 C CYS A 76 84.441 198.613 6.781 1.00 39.35 C ANISOU 338 C CYS A 76 4190 3384 7377 -23 201 219 C ATOM 339 O CYS A 76 84.944 197.630 7.342 1.00 38.19 O ANISOU 339 O CYS A 76 4059 3200 7252 -14 240 256 O ATOM 340 CB CYS A 76 84.928 200.984 7.384 1.00 39.44 C ANISOU 340 CB CYS A 76 4257 3478 7250 -4 148 208 C ATOM 341 SG CYS A 76 85.932 202.454 7.092 1.00 37.94 S ANISOU 341 SG CYS A 76 4107 3343 6968 2 92 172 S ATOM 342 N VAL A 77 83.168 198.632 6.385 1.00 38.88 N ANISOU 342 N VAL A 77 4083 3311 7379 -36 202 201 N ATOM 343 CA VAL A 77 82.294 197.527 6.740 1.00 41.32 C ANISOU 343 CA VAL A 77 4352 3561 7788 -44 261 229 C ATOM 344 C VAL A 77 82.750 196.250 6.075 1.00 43.41 C ANISOU 344 C VAL A 77 4602 3781 8111 -55 268 212 C ATOM 345 O VAL A 77 82.604 195.167 6.646 1.00 43.55 O ANISOU 345 O VAL A 77 4611 3741 8196 -55 327 254 O ATOM 346 CB VAL A 77 80.840 197.846 6.375 1.00 24.82 C ANISOU 346 CB VAL A 77 2206 1463 5763 -57 256 201 C ATOM 347 CG1 VAL A 77 79.981 196.637 6.627 1.00 25.96 C ANISOU 347 CG1 VAL A 77 2300 1536 6026 -69 320 221 C ATOM 348 CG2 VAL A 77 80.345 199.051 7.171 1.00 24.34 C ANISOU 348 CG2 VAL A 77 2160 1437 5652 -45 258 222 C ATOM 349 N ALA A 78 83.315 196.343 4.872 1.00 46.12 N ANISOU 349 N ALA A 78 4946 4145 8432 -62 211 155 N ATOM 350 CA ALA A 78 83.711 195.130 4.167 1.00 48.53 C ANISOU 350 CA ALA A 78 5236 4406 8798 -72 214 130 C ATOM 351 C ALA A 78 84.913 194.470 4.829 1.00 51.30 C ANISOU 351 C ALA A 78 5627 4738 9125 -58 244 172 C ATOM 352 O ALA A 78 84.966 193.241 4.946 1.00 51.17 O ANISOU 352 O ALA A 78 5599 4660 9185 -62 282 188 O ATOM 353 CB ALA A 78 84.012 195.445 2.703 1.00 47.93 C ANISOU 353 CB ALA A 78 5161 4355 8695 -81 148 58 C ATOM 354 N VAL A 79 85.885 195.266 5.274 1.00 53.44 N ANISOU 354 N VAL A 79 5948 5057 9300 -41 225 187 N ATOM 355 CA VAL A 79 87.062 194.685 5.906 1.00 58.52 C ANISOU 355 CA VAL A 79 6633 5682 9921 -22 244 222 C ATOM 356 C VAL A 79 86.745 194.226 7.319 1.00 59.55 C ANISOU 356 C VAL A 79 6787 5771 10068 -4 306 301 C ATOM 357 O VAL A 79 87.286 193.220 7.787 1.00 60.22 O ANISOU 357 O VAL A 79 6896 5804 10180 11 339 340 O ATOM 358 CB VAL A 79 88.236 195.682 5.874 1.00 60.31 C ANISOU 358 CB VAL A 79 6900 5966 10049 -9 200 203 C ATOM 359 CG1 VAL A 79 89.429 195.133 6.644 1.00 61.78 C ANISOU 359 CG1 VAL A 79 7130 6130 10213 16 215 237 C ATOM 360 CG2 VAL A 79 88.629 195.974 4.433 1.00 61.59 C ANISOU 360 CG2 VAL A 79 7047 6156 10198 -25 152 134 C ATOM 361 N TRP A 80 85.872 194.950 8.020 1.00 61.18 N ANISOU 361 N TRP A 80 6992 5995 10258 0 325 329 N ATOM 362 CA TRP A 80 85.503 194.581 9.381 1.00 62.28 C ANISOU 362 CA TRP A 80 7163 6095 10406 22 390 409 C ATOM 363 C TRP A 80 84.527 193.416 9.445 1.00 61.42 C ANISOU 363 C TRP A 80 7014 5912 10412 7 456 440 C ATOM 364 O TRP A 80 84.440 192.753 10.484 1.00 62.25 O ANISOU 364 O TRP A 80 7153 5965 10536 27 521 517 O ATOM 365 CB TRP A 80 84.909 195.789 10.110 1.00 65.14 C ANISOU 365 CB TRP A 80 7540 6499 10711 32 391 426 C ATOM 366 CG TRP A 80 85.904 196.880 10.370 1.00 67.22 C ANISOU 366 CG TRP A 80 7854 6820 10867 53 340 409 C ATOM 367 CD1 TRP A 80 87.264 196.759 10.389 1.00 67.25 C ANISOU 367 CD1 TRP A 80 7900 6831 10822 72 310 401 C ATOM 368 CD2 TRP A 80 85.620 198.260 10.645 1.00 69.61 C ANISOU 368 CD2 TRP A 80 8166 7173 11108 58 312 391 C ATOM 369 NE1 TRP A 80 87.844 197.973 10.662 1.00 66.98 N ANISOU 369 NE1 TRP A 80 7898 6848 10704 86 267 379 N ATOM 370 CE2 TRP A 80 86.859 198.911 10.823 1.00 68.41 C ANISOU 370 CE2 TRP A 80 8062 7056 10876 78 267 373 C ATOM 371 CE3 TRP A 80 84.441 199.006 10.759 1.00 71.03 C ANISOU 371 CE3 TRP A 80 8318 7369 11301 49 319 386 C ATOM 372 CZ2 TRP A 80 86.954 200.272 11.108 1.00 69.99 C ANISOU 372 CZ2 TRP A 80 8283 7301 11010 87 232 350 C ATOM 373 CZ3 TRP A 80 84.536 200.360 11.041 1.00 71.97 C ANISOU 373 CZ3 TRP A 80 8462 7535 11350 59 283 366 C ATOM 374 CH2 TRP A 80 85.785 200.978 11.211 1.00 71.12 C ANISOU 374 CH2 TRP A 80 8402 7457 11164 77 240 347 C ATOM 375 N LYS A 81 83.798 193.143 8.368 1.00 60.70 N ANISOU 375 N LYS A 81 6854 5808 10401 -25 441 382 N ATOM 376 CA LYS A 81 82.889 192.004 8.376 1.00 61.01 C ANISOU 376 CA LYS A 81 6847 5768 10566 -43 503 401 C ATOM 377 C LYS A 81 83.594 190.703 8.012 1.00 61.04 C ANISOU 377 C LYS A 81 6855 5709 10627 -46 515 400 C ATOM 378 O LYS A 81 83.448 189.703 8.718 1.00 62.28 O ANISOU 378 O LYS A 81 7024 5791 10848 -40 586 464 O ATOM 379 CB LYS A 81 81.718 192.250 7.420 1.00 60.81 C ANISOU 379 CB LYS A 81 6746 5748 10613 -72 478 332 C ATOM 380 CG LYS A 81 80.356 191.826 7.969 1.00 61.99 C ANISOU 380 CG LYS A 81 6847 5839 10869 -85 552 365 C ATOM 381 CD LYS A 81 79.769 192.895 8.887 1.00 61.80 C ANISOU 381 CD LYS A 81 6838 5856 10788 -71 573 403 C ATOM 382 CE LYS A 81 78.347 192.551 9.295 1.00 63.07 C ANISOU 382 CE LYS A 81 6941 5961 11062 -87 646 424 C ATOM 383 NZ LYS A 81 77.635 193.708 9.911 1.00 62.74 N ANISOU 383 NZ LYS A 81 6899 5963 10975 -77 652 438 N ATOM 384 N ASN A 82 84.394 190.720 6.949 1.00 59.85 N ANISOU 384 N ASN A 82 6701 5586 10453 -52 450 333 N ATOM 385 CA ASN A 82 85.034 189.528 6.402 1.00 60.31 C ANISOU 385 CA ASN A 82 6755 5586 10573 -57 453 315 C ATOM 386 C ASN A 82 86.458 189.408 6.932 1.00 59.69 C ANISOU 386 C ASN A 82 6747 5514 10417 -26 445 351 C ATOM 387 O ASN A 82 87.253 190.344 6.800 1.00 59.25 O ANISOU 387 O ASN A 82 6721 5529 10261 -13 392 328 O ATOM 388 CB ASN A 82 85.032 189.588 4.870 1.00 60.32 C ANISOU 388 CB ASN A 82 6713 5609 10597 -80 389 215 C ATOM 389 CG ASN A 82 85.602 188.332 4.222 1.00 61.57 C ANISOU 389 CG ASN A 82 6861 5702 10829 -87 391 185 C ATOM 390 OD1 ASN A 82 85.833 187.315 4.884 1.00 63.13 O ANISOU 390 OD1 ASN A 82 7076 5828 11084 -79 445 239 O ATOM 391 ND2 ASN A 82 85.819 188.398 2.909 1.00 61.18 N ANISOU 391 ND2 ASN A 82 6790 5675 10781 -100 332 99 N ATOM 392 N HIS A 83 86.775 188.257 7.537 1.00 59.81 N ANISOU 392 N HIS A 83 6790 5450 10485 -11 496 409 N ATOM 393 CA HIS A 83 88.103 188.066 8.117 1.00 58.64 C ANISOU 393 CA HIS A 83 6714 5296 10269 28 487 447 C ATOM 394 C HIS A 83 89.159 187.712 7.078 1.00 57.66 C ANISOU 394 C HIS A 83 6583 5177 10149 24 434 378 C ATOM 395 O HIS A 83 90.350 187.944 7.314 1.00 56.99 O ANISOU 395 O HIS A 83 6548 5117 9991 54 403 382 O ATOM 396 CB HIS A 83 88.058 186.988 9.195 1.00 60.01 C ANISOU 396 CB HIS A 83 6932 5377 10490 56 560 544 C ATOM 397 CG HIS A 83 87.032 187.247 10.248 1.00 60.07 C ANISOU 397 CG HIS A 83 6951 5373 10498 63 624 620 C ATOM 398 ND1 HIS A 83 87.272 188.057 11.338 1.00 59.80 N ANISOU 398 ND1 HIS A 83 6983 5382 10356 104 626 678 N ATOM 399 CD2 HIS A 83 85.752 186.823 10.367 1.00 61.17 C ANISOU 399 CD2 HIS A 83 7042 5463 10736 35 690 643 C ATOM 400 CE1 HIS A 83 86.187 188.113 12.088 1.00 60.21 C ANISOU 400 CE1 HIS A 83 7030 5413 10435 102 693 738 C ATOM 401 NE2 HIS A 83 85.250 187.374 11.520 1.00 61.27 N ANISOU 401 NE2 HIS A 83 7092 5490 10697 59 735 719 N ATOM 402 N HIS A 84 88.755 187.157 5.932 1.00 57.15 N ANISOU 402 N HIS A 84 6458 5086 10169 -9 423 311 N ATOM 403 CA HIS A 84 89.686 186.923 4.832 1.00 56.41 C ANISOU 403 CA HIS A 84 6356 5003 10075 -14 373 236 C ATOM 404 C HIS A 84 90.047 188.204 4.100 1.00 52.50 C ANISOU 404 C HIS A 84 5857 4607 9484 -20 310 176 C ATOM 405 O HIS A 84 90.986 188.199 3.296 1.00 51.68 O ANISOU 405 O HIS A 84 5758 4522 9357 -18 271 122 O ATOM 406 CB HIS A 84 89.101 185.921 3.838 1.00 59.70 C ANISOU 406 CB HIS A 84 6716 5356 10613 -43 380 180 C ATOM 407 CG HIS A 84 89.057 184.517 4.355 1.00 64.91 C ANISOU 407 CG HIS A 84 7381 5903 11377 -37 439 228 C ATOM 408 ND1 HIS A 84 88.207 184.123 5.367 1.00 66.36 N ANISOU 408 ND1 HIS A 84 7569 6030 11615 -36 509 308 N ATOM 409 CD2 HIS A 84 89.765 183.416 4.006 1.00 66.32 C ANISOU 409 CD2 HIS A 84 7566 6011 11619 -30 442 210 C ATOM 410 CE1 HIS A 84 88.390 182.839 5.617 1.00 67.57 C ANISOU 410 CE1 HIS A 84 7734 6079 11861 -30 554 343 C ATOM 411 NE2 HIS A 84 89.330 182.386 4.805 1.00 67.79 N ANISOU 411 NE2 HIS A 84 7764 6096 11898 -25 512 283 N ATOM 412 N MET A 85 89.280 189.274 4.323 1.00 50.25 N ANISOU 412 N MET A 85 5564 4378 9152 -28 302 183 N ATOM 413 CA MET A 85 89.585 190.621 3.865 1.00 46.92 C ANISOU 413 CA MET A 85 5149 4045 8632 -29 250 144 C ATOM 414 C MET A 85 90.643 191.325 4.705 1.00 45.02 C ANISOU 414 C MET A 85 4962 3846 8298 -1 240 178 C ATOM 415 O MET A 85 91.212 192.319 4.243 1.00 44.53 O ANISOU 415 O MET A 85 4909 3846 8165 -2 198 140 O ATOM 416 CB MET A 85 88.308 191.468 3.875 1.00 46.25 C ANISOU 416 CB MET A 85 5037 3994 8541 -44 248 143 C ATOM 417 CG MET A 85 87.315 191.147 2.777 1.00 46.62 C ANISOU 417 CG MET A 85 5031 4019 8663 -70 233 84 C ATOM 418 SD MET A 85 87.894 191.747 1.184 1.00 46.44 S ANISOU 418 SD MET A 85 5014 4046 8583 -78 163 -4 S ATOM 419 CE MET A 85 87.692 193.516 1.387 1.00 45.90 C ANISOU 419 CE MET A 85 4971 4063 8405 -72 131 6 C ATOM 420 N ARG A 86 90.927 190.847 5.915 1.00 43.88 N ANISOU 420 N ARG A 86 4858 3662 8153 27 276 248 N ATOM 421 CA ARG A 86 91.811 191.571 6.824 1.00 41.87 C ANISOU 421 CA ARG A 86 4658 3443 7809 59 261 278 C ATOM 422 C ARG A 86 93.280 191.317 6.482 1.00 41.32 C ANISOU 422 C ARG A 86 4608 3372 7719 77 230 246 C ATOM 423 O ARG A 86 94.048 190.785 7.280 1.00 42.57 O ANISOU 423 O ARG A 86 4815 3493 7868 117 239 287 O ATOM 424 CB ARG A 86 91.524 191.176 8.265 1.00 41.91 C ANISOU 424 CB ARG A 86 4711 3402 7809 94 309 368 C ATOM 425 CG ARG A 86 90.094 191.334 8.721 1.00 41.92 C ANISOU 425 CG ARG A 86 4693 3396 7840 79 352 406 C ATOM 426 CD ARG A 86 90.005 190.852 10.154 1.00 42.81 C ANISOU 426 CD ARG A 86 4869 3457 7941 123 405 503 C ATOM 427 NE ARG A 86 88.662 190.942 10.706 1.00 43.21 N ANISOU 427 NE ARG A 86 4902 3493 8024 112 460 549 N ATOM 428 CZ ARG A 86 88.217 191.974 11.413 1.00 42.58 C ANISOU 428 CZ ARG A 86 4841 3457 7879 124 461 570 C ATOM 429 NH1 ARG A 86 89.010 193.016 11.647 1.00 41.55 N ANISOU 429 NH1 ARG A 86 4749 3388 7650 147 408 547 N ATOM 430 NH2 ARG A 86 86.977 191.964 11.886 1.00 42.92 N ANISOU 430 NH2 ARG A 86 4864 3481 7963 114 518 611 N ATOM 431 N THR A 87 93.670 191.721 5.275 1.00 39.46 N ANISOU 431 N THR A 87 4340 3177 7476 53 193 173 N ATOM 432 CA THR A 87 95.072 191.700 4.884 1.00 37.65 C ANISOU 432 CA THR A 87 4122 2957 7225 67 165 134 C ATOM 433 C THR A 87 95.753 193.011 5.280 1.00 36.02 C ANISOU 433 C THR A 87 3937 2815 6935 78 136 125 C ATOM 434 O THR A 87 95.105 193.997 5.643 1.00 35.12 O ANISOU 434 O THR A 87 3825 2741 6777 70 132 139 O ATOM 435 CB THR A 87 95.229 191.453 3.383 1.00 36.82 C ANISOU 435 CB THR A 87 3980 2857 7153 39 148 61 C ATOM 436 OG1 THR A 87 94.696 192.561 2.649 1.00 24.84 O ANISOU 436 OG1 THR A 87 2445 1400 5593 15 127 26 O ATOM 437 CG2 THR A 87 94.520 190.185 2.978 1.00 26.56 C ANISOU 437 CG2 THR A 87 2657 1490 5946 27 173 60 C ATOM 438 N VAL A 88 97.089 193.006 5.225 1.00 35.67 N ANISOU 438 N VAL A 88 3905 2774 6876 97 114 98 N ATOM 439 CA VAL A 88 97.846 194.224 5.514 1.00 23.97 C ANISOU 439 CA VAL A 88 2432 1345 5330 105 86 78 C ATOM 440 C VAL A 88 97.406 195.347 4.589 1.00 26.16 C ANISOU 440 C VAL A 88 2680 1681 5579 68 74 37 C ATOM 441 O VAL A 88 97.162 196.480 5.022 1.00 22.66 O ANISOU 441 O VAL A 88 2244 1277 5087 66 63 43 O ATOM 442 CB VAL A 88 99.359 193.970 5.367 1.00 24.13 C ANISOU 442 CB VAL A 88 2454 1355 5358 128 66 40 C ATOM 443 CG1 VAL A 88 100.152 195.004 6.164 1.00 23.70 C ANISOU 443 CG1 VAL A 88 2419 1334 5252 152 39 33 C ATOM 444 CG2 VAL A 88 99.722 192.551 5.760 1.00 25.09 C ANISOU 444 CG2 VAL A 88 2601 1405 5527 164 79 68 C ATOM 445 N THR A 89 97.283 195.041 3.297 1.00 25.93 N ANISOU 445 N THR A 89 2624 1650 5577 43 76 -6 N ATOM 446 CA THR A 89 96.923 196.061 2.322 1.00 24.63 C ANISOU 446 CA THR A 89 2449 1530 5378 17 64 -41 C ATOM 447 C THR A 89 95.546 196.634 2.605 1.00 25.18 C ANISOU 447 C THR A 89 2519 1618 5429 7 65 -12 C ATOM 448 O THR A 89 95.329 197.844 2.469 1.00 25.16 O ANISOU 448 O THR A 89 2524 1656 5379 -1 51 -20 O ATOM 449 CB THR A 89 96.949 195.471 0.915 1.00 23.77 C ANISOU 449 CB THR A 89 2329 1405 5298 1 66 -89 C ATOM 450 OG1 THR A 89 98.296 195.147 0.556 1.00 23.41 O ANISOU 450 OG1 THR A 89 2281 1350 5264 9 67 -125 O ATOM 451 CG2 THR A 89 96.369 196.460 -0.082 1.00 23.00 C ANISOU 451 CG2 THR A 89 2240 1342 5158 -20 55 -116 C ATOM 452 N ASN A 90 94.593 195.776 2.984 1.00 25.61 N ANISOU 452 N ASN A 90 2565 1635 5529 8 84 21 N ATOM 453 CA ASN A 90 93.238 196.259 3.218 1.00 22.81 C ANISOU 453 CA ASN A 90 2203 1294 5170 -2 88 44 C ATOM 454 C ASN A 90 93.127 197.020 4.528 1.00 22.51 C ANISOU 454 C ASN A 90 2187 1276 5089 14 92 88 C ATOM 455 O ASN A 90 92.294 197.926 4.643 1.00 22.62 O ANISOU 455 O ASN A 90 2199 1319 5077 7 85 93 O ATOM 456 CB ASN A 90 92.250 195.097 3.176 1.00 26.36 C ANISOU 456 CB ASN A 90 2629 1691 5694 -10 113 61 C ATOM 457 CG ASN A 90 92.006 194.589 1.759 1.00 27.03 C ANISOU 457 CG ASN A 90 2692 1760 5819 -29 100 5 C ATOM 458 OD1 ASN A 90 92.419 195.215 0.779 1.00 26.54 O ANISOU 458 OD1 ASN A 90 2640 1729 5716 -37 74 -39 O ATOM 459 ND2 ASN A 90 91.318 193.452 1.647 1.00 28.29 N ANISOU 459 ND2 ASN A 90 2825 1864 6060 -36 120 8 N ATOM 460 N LEU A 91 93.938 196.672 5.528 1.00 22.72 N ANISOU 460 N LEU A 91 2241 1284 5108 40 100 117 N ATOM 461 CA LEU A 91 93.897 197.430 6.775 1.00 27.41 C ANISOU 461 CA LEU A 91 2868 1894 5654 62 99 152 C ATOM 462 C LEU A 91 94.421 198.845 6.571 1.00 26.08 C ANISOU 462 C LEU A 91 2699 1778 5432 56 66 114 C ATOM 463 O LEU A 91 93.879 199.802 7.139 1.00 25.54 O ANISOU 463 O LEU A 91 2642 1734 5328 59 60 125 O ATOM 464 CB LEU A 91 94.680 196.697 7.871 1.00 28.39 C ANISOU 464 CB LEU A 91 3035 1976 5775 104 110 192 C ATOM 465 CG LEU A 91 94.114 195.334 8.296 1.00 23.93 C ANISOU 465 CG LEU A 91 2482 1347 5262 117 152 247 C ATOM 466 CD1 LEU A 91 95.038 194.646 9.271 1.00 24.54 C ANISOU 466 CD1 LEU A 91 2618 1380 5326 172 156 286 C ATOM 467 CD2 LEU A 91 92.708 195.471 8.884 1.00 24.09 C ANISOU 467 CD2 LEU A 91 2503 1361 5290 112 186 293 C ATOM 468 N PHE A 92 95.449 199.009 5.735 1.00 25.84 N ANISOU 468 N PHE A 92 2656 1761 5399 47 48 67 N ATOM 469 CA PHE A 92 95.841 200.358 5.351 1.00 24.94 C ANISOU 469 CA PHE A 92 2539 1691 5247 36 26 31 C ATOM 470 C PHE A 92 94.738 201.040 4.557 1.00 25.15 C ANISOU 470 C PHE A 92 2557 1740 5261 13 23 23 C ATOM 471 O PHE A 92 94.474 202.230 4.753 1.00 25.18 O ANISOU 471 O PHE A 92 2568 1770 5229 11 10 19 O ATOM 472 CB PHE A 92 97.137 200.325 4.544 1.00 24.13 C ANISOU 472 CB PHE A 92 2424 1591 5154 31 19 -16 C ATOM 473 CG PHE A 92 98.358 200.079 5.378 1.00 23.45 C ANISOU 473 CG PHE A 92 2344 1490 5074 57 9 -21 C ATOM 474 CD1 PHE A 92 98.541 200.762 6.570 1.00 22.93 C ANISOU 474 CD1 PHE A 92 2300 1432 4980 80 -8 -9 C ATOM 475 CD2 PHE A 92 99.322 199.162 4.978 1.00 22.98 C ANISOU 475 CD2 PHE A 92 2275 1406 5051 64 12 -43 C ATOM 476 CE1 PHE A 92 99.666 200.540 7.344 1.00 22.58 C ANISOU 476 CE1 PHE A 92 2269 1370 4940 114 -25 -20 C ATOM 477 CE2 PHE A 92 100.441 198.937 5.748 1.00 22.66 C ANISOU 477 CE2 PHE A 92 2243 1349 5019 96 -3 -52 C ATOM 478 CZ PHE A 92 100.613 199.628 6.932 1.00 22.47 C ANISOU 478 CZ PHE A 92 2242 1332 4963 123 -24 -41 C ATOM 479 N ILE A 93 94.049 200.295 3.688 1.00 25.86 N ANISOU 479 N ILE A 93 2632 1812 5381 0 31 18 N ATOM 480 CA ILE A 93 92.985 200.903 2.896 1.00 26.61 C ANISOU 480 CA ILE A 93 2726 1921 5464 -16 21 8 C ATOM 481 C ILE A 93 91.851 201.363 3.794 1.00 27.57 C ANISOU 481 C ILE A 93 2845 2050 5581 -12 23 42 C ATOM 482 O ILE A 93 91.258 202.426 3.568 1.00 27.87 O ANISOU 482 O ILE A 93 2890 2111 5590 -17 7 35 O ATOM 483 CB ILE A 93 92.473 199.929 1.823 1.00 21.17 C ANISOU 483 CB ILE A 93 2024 1205 4816 -29 24 -12 C ATOM 484 CG1 ILE A 93 93.554 199.661 0.791 1.00 21.24 C ANISOU 484 CG1 ILE A 93 2042 1207 4820 -34 22 -52 C ATOM 485 CG2 ILE A 93 91.222 200.482 1.151 1.00 21.09 C ANISOU 485 CG2 ILE A 93 2014 1202 4798 -41 6 -21 C ATOM 486 CD1 ILE A 93 93.116 198.690 -0.266 1.00 22.18 C ANISOU 486 CD1 ILE A 93 2153 1295 4978 -46 21 -80 C ATOM 487 N VAL A 94 91.534 200.589 4.835 1.00 28.31 N ANISOU 487 N VAL A 94 2934 2120 5703 1 47 81 N ATOM 488 CA VAL A 94 90.510 201.060 5.757 1.00 28.43 C ANISOU 488 CA VAL A 94 2952 2139 5712 7 57 114 C ATOM 489 C VAL A 94 90.945 202.384 6.365 1.00 28.13 C ANISOU 489 C VAL A 94 2938 2133 5617 17 38 108 C ATOM 490 O VAL A 94 90.145 203.322 6.491 1.00 28.56 O ANISOU 490 O VAL A 94 2993 2205 5654 14 28 108 O ATOM 491 CB VAL A 94 90.214 200.004 6.838 1.00 28.75 C ANISOU 491 CB VAL A 94 2998 2138 5786 23 97 165 C ATOM 492 CG1 VAL A 94 89.429 200.626 7.979 1.00 21.53 C ANISOU 492 CG1 VAL A 94 2101 1229 4851 37 113 201 C ATOM 493 CG2 VAL A 94 89.432 198.855 6.234 1.00 29.17 C ANISOU 493 CG2 VAL A 94 3017 2154 5911 8 120 168 C ATOM 494 N ASN A 95 92.242 202.516 6.671 1.00 27.30 N ANISOU 494 N ASN A 95 2851 2033 5490 29 28 96 N ATOM 495 CA ASN A 95 92.729 203.765 7.240 1.00 25.51 C ANISOU 495 CA ASN A 95 2642 1829 5220 38 7 81 C ATOM 496 C ASN A 95 92.550 204.916 6.265 1.00 24.82 C ANISOU 496 C ASN A 95 2548 1769 5116 18 -13 48 C ATOM 497 O ASN A 95 92.312 206.052 6.686 1.00 25.00 O ANISOU 497 O ASN A 95 2581 1805 5112 22 -26 42 O ATOM 498 CB ASN A 95 94.194 203.620 7.651 1.00 25.34 C ANISOU 498 CB ASN A 95 2633 1802 5193 55 -3 64 C ATOM 499 CG ASN A 95 94.685 204.789 8.489 1.00 25.12 C ANISOU 499 CG ASN A 95 2624 1789 5133 71 -26 46 C ATOM 500 OD1 ASN A 95 94.244 204.977 9.620 1.00 25.40 O ANISOU 500 OD1 ASN A 95 2689 1815 5147 97 -24 71 O ATOM 501 ND2 ASN A 95 95.607 205.573 7.941 1.00 24.45 N ANISOU 501 ND2 ASN A 95 2523 1719 5047 58 -43 2 N ATOM 502 N LEU A 96 92.638 204.647 4.962 1.00 24.39 N ANISOU 502 N LEU A 96 2484 1713 5071 1 -14 27 N ATOM 503 CA LEU A 96 92.379 205.694 3.981 1.00 24.73 C ANISOU 503 CA LEU A 96 2538 1769 5088 -13 -29 5 C ATOM 504 C LEU A 96 90.914 206.110 3.987 1.00 25.53 C ANISOU 504 C LEU A 96 2639 1872 5188 -15 -38 20 C ATOM 505 O LEU A 96 90.599 207.306 3.957 1.00 25.40 O ANISOU 505 O LEU A 96 2638 1866 5146 -16 -54 14 O ATOM 506 CB LEU A 96 92.788 205.217 2.596 1.00 25.24 C ANISOU 506 CB LEU A 96 2609 1823 5157 -27 -26 -19 C ATOM 507 CG LEU A 96 94.282 205.003 2.434 1.00 26.44 C ANISOU 507 CG LEU A 96 2760 1972 5313 -26 -16 -41 C ATOM 508 CD1 LEU A 96 94.537 204.418 1.073 1.00 27.11 C ANISOU 508 CD1 LEU A 96 2857 2041 5403 -40 -7 -64 C ATOM 509 CD2 LEU A 96 95.001 206.325 2.606 1.00 26.73 C ANISOU 509 CD2 LEU A 96 2810 2021 5326 -28 -20 -57 C ATOM 510 N SER A 97 90.000 205.141 4.036 1.00 26.65 N ANISOU 510 N SER A 97 2760 2000 5367 -16 -28 37 N ATOM 511 CA SER A 97 88.586 205.492 4.089 1.00 25.99 C ANISOU 511 CA SER A 97 2666 1915 5294 -18 -35 48 C ATOM 512 C SER A 97 88.231 206.184 5.400 1.00 24.86 C ANISOU 512 C SER A 97 2527 1782 5139 -4 -29 68 C ATOM 513 O SER A 97 87.254 206.939 5.449 1.00 25.24 O ANISOU 513 O SER A 97 2573 1834 5184 -4 -41 69 O ATOM 514 CB SER A 97 87.724 204.251 3.875 1.00 26.41 C ANISOU 514 CB SER A 97 2687 1944 5404 -23 -20 57 C ATOM 515 OG SER A 97 87.932 203.706 2.585 1.00 26.93 O ANISOU 515 OG SER A 97 2755 1998 5481 -35 -32 29 O ATOM 516 N LEU A 98 89.004 205.945 6.467 1.00 24.73 N ANISOU 516 N LEU A 98 2520 1763 5112 10 -13 84 N ATOM 517 CA LEU A 98 88.737 206.627 7.732 1.00 24.89 C ANISOU 517 CA LEU A 98 2557 1786 5112 28 -9 99 C ATOM 518 C LEU A 98 89.086 208.107 7.647 1.00 24.28 C ANISOU 518 C LEU A 98 2497 1728 5001 28 -38 69 C ATOM 519 O LEU A 98 88.309 208.967 8.078 1.00 24.41 O ANISOU 519 O LEU A 98 2519 1747 5008 35 -46 69 O ATOM 520 CB LEU A 98 89.513 205.971 8.874 1.00 25.37 C ANISOU 520 CB LEU A 98 2641 1832 5166 50 11 122 C ATOM 521 CG LEU A 98 88.962 204.639 9.380 1.00 26.37 C ANISOU 521 CG LEU A 98 2765 1927 5326 59 52 168 C ATOM 522 CD1 LEU A 98 89.722 204.167 10.596 1.00 26.58 C ANISOU 522 CD1 LEU A 98 2837 1933 5330 95 67 198 C ATOM 523 CD2 LEU A 98 87.489 204.800 9.678 1.00 27.26 C ANISOU 523 CD2 LEU A 98 2863 2033 5461 57 73 190 C ATOM 524 N ALA A 99 90.270 208.424 7.127 1.00 23.91 N ANISOU 524 N ALA A 99 2457 1687 4939 22 -52 42 N ATOM 525 CA ALA A 99 90.597 209.819 6.875 1.00 23.39 C ANISOU 525 CA ALA A 99 2405 1629 4852 19 -73 14 C ATOM 526 C ALA A 99 89.694 210.401 5.800 1.00 22.55 C ANISOU 526 C ALA A 99 2304 1522 4740 5 -85 11 C ATOM 527 O ALA A 99 89.367 211.590 5.847 1.00 19.00 O ANISOU 527 O ALA A 99 1870 1070 4277 7 -101 1 O ATOM 528 CB ALA A 99 92.066 209.957 6.478 1.00 23.86 C ANISOU 528 CB ALA A 99 2466 1689 4909 13 -75 -13 C ATOM 529 N ALA A 100 89.265 209.581 4.837 1.00 22.18 N ANISOU 529 N ALA A 100 2250 1470 4706 -6 -82 18 N ATOM 530 CA ALA A 100 88.361 210.077 3.807 1.00 22.30 C ANISOU 530 CA ALA A 100 2281 1477 4715 -14 -101 13 C ATOM 531 C ALA A 100 87.023 210.477 4.409 1.00 23.44 C ANISOU 531 C ALA A 100 2411 1621 4873 -5 -110 25 C ATOM 532 O ALA A 100 86.525 211.576 4.143 1.00 24.61 O ANISOU 532 O ALA A 100 2580 1763 5006 -3 -132 17 O ATOM 533 CB ALA A 100 88.167 209.025 2.723 1.00 21.81 C ANISOU 533 CB ALA A 100 2215 1405 4669 -25 -100 10 C ATOM 534 N VAL A 101 86.438 209.616 5.249 1.00 23.05 N ANISOU 534 N VAL A 101 2330 1571 4855 1 -90 44 N ATOM 535 CA VAL A 101 85.166 209.963 5.880 1.00 22.29 C ANISOU 535 CA VAL A 101 2219 1472 4780 9 -90 54 C ATOM 536 C VAL A 101 85.333 211.160 6.807 1.00 21.64 C ANISOU 536 C VAL A 101 2158 1394 4669 24 -97 48 C ATOM 537 O VAL A 101 84.447 212.021 6.891 1.00 22.10 O ANISOU 537 O VAL A 101 2219 1448 4731 31 -113 42 O ATOM 538 CB VAL A 101 84.591 208.760 6.652 1.00 22.05 C ANISOU 538 CB VAL A 101 2155 1429 4792 12 -53 82 C ATOM 539 CG1 VAL A 101 83.418 209.197 7.497 1.00 21.98 C ANISOU 539 CG1 VAL A 101 2135 1414 4803 23 -42 93 C ATOM 540 CG2 VAL A 101 84.187 207.620 5.723 1.00 22.00 C ANISOU 540 CG2 VAL A 101 2119 1409 4830 -2 -49 80 C ATOM 541 N LEU A 102 86.473 211.244 7.508 1.00 20.54 N ANISOU 541 N LEU A 102 2036 1261 4509 32 -88 44 N ATOM 542 CA LEU A 102 86.619 212.247 8.561 1.00 20.13 C ANISOU 542 CA LEU A 102 2004 1208 4438 50 -95 32 C ATOM 543 C LEU A 102 86.587 213.663 7.997 1.00 20.18 C ANISOU 543 C LEU A 102 2026 1210 4430 47 -125 6 C ATOM 544 O LEU A 102 86.049 214.577 8.634 1.00 20.52 O ANISOU 544 O LEU A 102 2079 1247 4472 62 -135 -5 O ATOM 545 CB LEU A 102 87.923 212.036 9.321 1.00 19.09 C ANISOU 545 CB LEU A 102 1886 1078 4289 61 -89 25 C ATOM 546 CG LEU A 102 88.333 213.198 10.230 1.00 19.12 C ANISOU 546 CG LEU A 102 1914 1078 4275 82 -106 -4 C ATOM 547 CD1 LEU A 102 87.374 213.358 11.407 1.00 19.27 C ANISOU 547 CD1 LEU A 102 1949 1087 4287 112 -95 7 C ATOM 548 CD2 LEU A 102 89.762 212.996 10.706 1.00 19.13 C ANISOU 548 CD2 LEU A 102 1923 1078 4267 91 -111 -23 C ATOM 549 N VAL A 103 87.139 213.866 6.799 1.00 19.78 N ANISOU 549 N VAL A 103 1986 1157 4371 30 -135 -3 N ATOM 550 CA VAL A 103 87.095 215.180 6.166 1.00 19.28 C ANISOU 550 CA VAL A 103 1952 1077 4295 27 -156 -19 C ATOM 551 C VAL A 103 85.812 215.378 5.370 1.00 19.70 C ANISOU 551 C VAL A 103 2013 1119 4353 27 -175 -9 C ATOM 552 O VAL A 103 85.328 216.507 5.251 1.00 20.54 O ANISOU 552 O VAL A 103 2143 1206 4455 35 -194 -17 O ATOM 553 CB VAL A 103 88.334 215.377 5.278 1.00 19.33 C ANISOU 553 CB VAL A 103 1980 1075 4288 11 -150 -29 C ATOM 554 CG1 VAL A 103 89.606 215.284 6.117 1.00 19.26 C ANISOU 554 CG1 VAL A 103 1956 1075 4286 14 -138 -47 C ATOM 555 CG2 VAL A 103 88.357 214.333 4.179 1.00 19.28 C ANISOU 555 CG2 VAL A 103 1977 1072 4277 -3 -142 -16 C ATOM 556 N THR A 104 85.242 214.300 4.828 1.00 19.91 N ANISOU 556 N THR A 104 2020 1151 4394 20 -172 4 N ATOM 557 CA THR A 104 83.982 214.440 4.112 1.00 20.92 C ANISOU 557 CA THR A 104 2150 1265 4534 22 -197 6 C ATOM 558 C THR A 104 82.905 215.006 5.023 1.00 21.94 C ANISOU 558 C THR A 104 2259 1391 4686 39 -204 4 C ATOM 559 O THR A 104 82.056 215.785 4.577 1.00 22.72 O ANISOU 559 O THR A 104 2373 1470 4788 48 -233 -3 O ATOM 560 CB THR A 104 83.544 213.093 3.542 1.00 21.17 C ANISOU 560 CB THR A 104 2151 1299 4592 11 -193 12 C ATOM 561 OG1 THR A 104 84.485 212.660 2.551 1.00 22.11 O ANISOU 561 OG1 THR A 104 2298 1415 4688 -2 -189 9 O ATOM 562 CG2 THR A 104 82.147 213.189 2.921 1.00 21.01 C ANISOU 562 CG2 THR A 104 2122 1262 4600 16 -224 6 C ATOM 563 N ILE A 105 82.957 214.670 6.306 1.00 22.01 N ANISOU 563 N ILE A 105 2243 1413 4708 47 -177 10 N ATOM 564 CA ILE A 105 81.958 215.125 7.262 1.00 22.29 C ANISOU 564 CA ILE A 105 2264 1443 4763 65 -174 7 C ATOM 565 C ILE A 105 82.328 216.467 7.881 1.00 22.47 C ANISOU 565 C ILE A 105 2319 1457 4762 83 -187 -14 C ATOM 566 O ILE A 105 81.471 217.341 8.031 1.00 22.67 O ANISOU 566 O ILE A 105 2349 1466 4798 99 -205 -27 O ATOM 567 CB ILE A 105 81.762 214.037 8.334 1.00 22.54 C ANISOU 567 CB ILE A 105 2267 1481 4817 69 -130 29 C ATOM 568 CG1 ILE A 105 81.192 212.779 7.685 1.00 23.72 C ANISOU 568 CG1 ILE A 105 2377 1628 5007 52 -117 45 C ATOM 569 CG2 ILE A 105 80.864 214.518 9.453 1.00 22.14 C ANISOU 569 CG2 ILE A 105 2213 1419 4779 94 -116 27 C ATOM 570 CD1 ILE A 105 81.269 211.575 8.570 1.00 24.52 C ANISOU 570 CD1 ILE A 105 2460 1728 5130 53 -66 75 C ATOM 571 N THR A 106 83.597 216.672 8.231 1.00 22.28 N ANISOU 571 N THR A 106 2313 1438 4714 81 -180 -23 N ATOM 572 CA THR A 106 83.978 217.834 9.028 1.00 21.84 C ANISOU 572 CA THR A 106 2280 1371 4648 100 -191 -51 C ATOM 573 C THR A 106 84.546 218.994 8.218 1.00 22.61 C ANISOU 573 C THR A 106 2406 1446 4737 92 -213 -69 C ATOM 574 O THR A 106 84.561 220.125 8.721 1.00 22.84 O ANISOU 574 O THR A 106 2450 1456 4770 108 -227 -95 O ATOM 575 CB THR A 106 85.003 217.431 10.106 1.00 20.65 C ANISOU 575 CB THR A 106 2131 1231 4483 109 -173 -59 C ATOM 576 OG1 THR A 106 86.280 217.194 9.504 1.00 19.80 O ANISOU 576 OG1 THR A 106 2025 1130 4368 89 -172 -63 O ATOM 577 CG2 THR A 106 84.547 216.167 10.826 1.00 20.22 C ANISOU 577 CG2 THR A 106 2064 1187 4432 119 -140 -29 C ATOM 578 N CYS A 107 85.003 218.755 6.991 1.00 22.71 N ANISOU 578 N CYS A 107 2433 1456 4740 70 -214 -55 N ATOM 579 CA CYS A 107 85.748 219.754 6.233 1.00 23.14 C ANISOU 579 CA CYS A 107 2526 1480 4784 60 -219 -64 C ATOM 580 C CYS A 107 85.115 220.112 4.905 1.00 23.29 C ANISOU 580 C CYS A 107 2588 1471 4791 57 -235 -46 C ATOM 581 O CYS A 107 85.208 221.268 4.467 1.00 20.94 O ANISOU 581 O CYS A 107 2336 1133 4489 60 -242 -49 O ATOM 582 CB CYS A 107 87.168 219.254 5.974 1.00 23.55 C ANISOU 582 CB CYS A 107 2576 1542 4830 40 -197 -66 C ATOM 583 SG CYS A 107 88.135 219.011 7.465 1.00 23.50 S ANISOU 583 SG CYS A 107 2535 1557 4838 50 -189 -95 S ATOM 584 N LEU A 108 84.528 219.133 4.227 1.00 22.72 N ANISOU 584 N LEU A 108 2506 1413 4713 51 -239 -28 N ATOM 585 CA LEU A 108 83.913 219.398 2.931 1.00 21.73 C ANISOU 585 CA LEU A 108 2429 1257 4572 52 -260 -14 C ATOM 586 C LEU A 108 82.828 220.454 3.011 1.00 21.31 C ANISOU 586 C LEU A 108 2395 1173 4528 77 -290 -19 C ATOM 587 O LEU A 108 82.863 221.406 2.212 1.00 21.49 O ANISOU 587 O LEU A 108 2485 1149 4531 84 -300 -11 O ATOM 588 CB LEU A 108 83.358 218.094 2.359 1.00 20.94 C ANISOU 588 CB LEU A 108 2303 1177 4477 45 -266 -6 C ATOM 589 CG LEU A 108 82.648 218.226 1.013 1.00 20.81 C ANISOU 589 CG LEU A 108 2337 1126 4443 51 -296 2 C ATOM 590 CD1 LEU A 108 82.719 216.911 0.266 1.00 20.62 C ANISOU 590 CD1 LEU A 108 2300 1116 4418 35 -294 3 C ATOM 591 CD2 LEU A 108 81.209 218.651 1.190 1.00 21.02 C ANISOU 591 CD2 LEU A 108 2348 1142 4498 75 -333 -6 C ATOM 592 N PRO A 109 81.855 220.375 3.925 1.00 20.97 N ANISOU 592 N PRO A 109 2304 1147 4516 94 -301 -30 N ATOM 593 CA PRO A 109 80.813 221.409 3.924 1.00 21.42 C ANISOU 593 CA PRO A 109 2381 1172 4586 123 -332 -39 C ATOM 594 C PRO A 109 81.374 222.802 4.126 1.00 21.82 C ANISOU 594 C PRO A 109 2478 1184 4630 134 -331 -48 C ATOM 595 O PRO A 109 80.918 223.747 3.472 1.00 22.37 O ANISOU 595 O PRO A 109 2601 1205 4693 154 -353 -43 O ATOM 596 CB PRO A 109 79.907 220.990 5.095 1.00 21.26 C ANISOU 596 CB PRO A 109 2295 1179 4604 136 -330 -53 C ATOM 597 CG PRO A 109 80.161 219.540 5.288 1.00 20.81 C ANISOU 597 CG PRO A 109 2192 1161 4554 113 -303 -42 C ATOM 598 CD PRO A 109 81.610 219.341 4.947 1.00 20.59 C ANISOU 598 CD PRO A 109 2190 1140 4493 91 -283 -33 C ATOM 599 N ALA A 110 82.404 222.957 4.961 1.00 21.67 N ANISOU 599 N ALA A 110 2442 1177 4614 123 -306 -63 N ATOM 600 CA ALA A 110 82.922 224.298 5.193 1.00 22.16 C ANISOU 600 CA ALA A 110 2540 1196 4685 131 -305 -80 C ATOM 601 C ALA A 110 83.671 224.801 3.970 1.00 31.61 C ANISOU 601 C ALA A 110 3807 2344 5858 114 -292 -58 C ATOM 602 O ALA A 110 83.565 225.978 3.609 1.00 32.23 O ANISOU 602 O ALA A 110 3941 2362 5941 127 -298 -55 O ATOM 603 CB ALA A 110 83.815 224.313 6.431 1.00 21.97 C ANISOU 603 CB ALA A 110 2476 1194 4676 126 -288 -112 C ATOM 604 N THR A 111 84.407 223.912 3.301 1.00 31.41 N ANISOU 604 N THR A 111 3786 2338 5809 87 -271 -40 N ATOM 605 CA THR A 111 85.102 224.292 2.078 1.00 31.80 C ANISOU 605 CA THR A 111 3913 2339 5831 70 -250 -16 C ATOM 606 C THR A 111 84.109 224.736 1.003 1.00 23.13 C ANISOU 606 C THR A 111 2889 1192 4706 94 -273 11 C ATOM 607 O THR A 111 84.360 225.705 0.280 1.00 23.82 O ANISOU 607 O THR A 111 3062 1210 4779 98 -260 31 O ATOM 608 CB THR A 111 85.970 223.114 1.608 1.00 22.19 C ANISOU 608 CB THR A 111 2682 1156 4592 41 -224 -8 C ATOM 609 OG1 THR A 111 86.992 222.866 2.579 1.00 21.89 O ANISOU 609 OG1 THR A 111 2586 1151 4581 26 -204 -33 O ATOM 610 CG2 THR A 111 86.612 223.378 0.254 1.00 22.63 C ANISOU 610 CG2 THR A 111 2828 1159 4613 23 -198 19 C ATOM 611 N LEU A 112 82.948 224.079 0.921 1.00 22.88 N ANISOU 611 N LEU A 112 2828 1189 4674 113 -307 12 N ATOM 612 CA LEU A 112 81.953 224.480 -0.068 1.00 23.39 C ANISOU 612 CA LEU A 112 2959 1208 4720 145 -338 32 C ATOM 613 C LEU A 112 81.460 225.894 0.202 1.00 27.34 C ANISOU 613 C LEU A 112 3497 1653 5237 179 -352 30 C ATOM 614 O LEU A 112 81.334 226.701 -0.725 1.00 27.58 O ANISOU 614 O LEU A 112 3624 1613 5242 203 -353 58 O ATOM 615 CB LEU A 112 80.780 223.496 -0.077 1.00 23.05 C ANISOU 615 CB LEU A 112 2858 1207 4691 158 -376 21 C ATOM 616 CG LEU A 112 79.600 223.912 -0.961 1.00 23.63 C ANISOU 616 CG LEU A 112 2984 1238 4756 202 -421 31 C ATOM 617 CD1 LEU A 112 80.044 224.051 -2.415 1.00 24.07 C ANISOU 617 CD1 LEU A 112 3151 1239 4755 209 -410 64 C ATOM 618 CD2 LEU A 112 78.429 222.947 -0.845 1.00 23.36 C ANISOU 618 CD2 LEU A 112 2874 1244 4757 212 -461 9 C ATOM 619 N VAL A 113 81.220 226.231 1.472 1.00 27.82 N ANISOU 619 N VAL A 113 3491 1738 5340 187 -360 -2 N ATOM 620 CA VAL A 113 80.750 227.576 1.785 1.00 29.33 C ANISOU 620 CA VAL A 113 3714 1875 5555 222 -375 -11 C ATOM 621 C VAL A 113 81.825 228.606 1.464 1.00 31.66 C ANISOU 621 C VAL A 113 4082 2101 5846 208 -340 3 C ATOM 622 O VAL A 113 81.553 229.633 0.831 1.00 33.30 O ANISOU 622 O VAL A 113 4375 2231 6048 237 -342 25 O ATOM 623 CB VAL A 113 80.310 227.663 3.257 1.00 28.28 C ANISOU 623 CB VAL A 113 3497 1782 5467 234 -388 -54 C ATOM 624 CG1 VAL A 113 80.014 229.106 3.633 1.00 28.69 C ANISOU 624 CG1 VAL A 113 3582 1773 5548 269 -399 -71 C ATOM 625 CG2 VAL A 113 79.092 226.780 3.500 1.00 27.53 C ANISOU 625 CG2 VAL A 113 3341 1736 5384 250 -416 -63 C ATOM 626 N VAL A 114 83.070 228.337 1.857 1.00 31.75 N ANISOU 626 N VAL A 114 4066 2134 5865 166 -304 -10 N ATOM 627 CA VAL A 114 84.107 229.348 1.689 1.00 33.23 C ANISOU 627 CA VAL A 114 4307 2253 6067 147 -268 -7 C ATOM 628 C VAL A 114 84.328 229.640 0.215 1.00 35.11 C ANISOU 628 C VAL A 114 4663 2419 6260 145 -244 46 C ATOM 629 O VAL A 114 84.375 230.803 -0.197 1.00 36.05 O ANISOU 629 O VAL A 114 4866 2447 6385 159 -231 66 O ATOM 630 CB VAL A 114 85.413 228.930 2.394 1.00 25.26 C ANISOU 630 CB VAL A 114 3234 1284 5082 104 -238 -37 C ATOM 631 CG1 VAL A 114 86.479 229.999 2.195 1.00 26.12 C ANISOU 631 CG1 VAL A 114 3389 1314 5220 80 -201 -39 C ATOM 632 CG2 VAL A 114 85.170 228.710 3.879 1.00 29.58 C ANISOU 632 CG2 VAL A 114 3684 1891 5665 117 -261 -86 C ATOM 633 N ASP A 115 84.423 228.594 -0.608 1.00 36.62 N ANISOU 633 N ASP A 115 4870 2641 6403 131 -238 70 N ATOM 634 CA ASP A 115 84.678 228.783 -2.034 1.00 39.52 C ANISOU 634 CA ASP A 115 5361 2939 6716 132 -211 119 C ATOM 635 C ASP A 115 83.527 229.475 -2.747 1.00 39.34 C ANISOU 635 C ASP A 115 5428 2852 6668 192 -238 153 C ATOM 636 O ASP A 115 83.731 230.054 -3.820 1.00 38.08 O ANISOU 636 O ASP A 115 5396 2605 6466 207 -209 201 O ATOM 637 CB ASP A 115 84.974 227.440 -2.700 1.00 43.27 C ANISOU 637 CB ASP A 115 5829 3465 7148 109 -203 128 C ATOM 638 CG ASP A 115 86.296 226.823 -2.224 1.00 47.13 C ANISOU 638 CG ASP A 115 6251 4000 7656 55 -168 104 C ATOM 639 OD1 ASP A 115 87.045 227.478 -1.445 1.00 46.58 O ANISOU 639 OD1 ASP A 115 6145 3918 7633 35 -147 81 O ATOM 640 OD2 ASP A 115 86.588 225.672 -2.645 1.00 48.62 O ANISOU 640 OD2 ASP A 115 6422 4234 7818 37 -161 105 O ATOM 641 N ILE A 116 82.328 229.409 -2.185 1.00 39.87 N ANISOU 641 N ILE A 116 5433 2956 6760 232 -289 130 N ATOM 642 CA ILE A 116 81.169 230.062 -2.778 1.00 40.92 C ANISOU 642 CA ILE A 116 5634 3033 6879 300 -322 156 C ATOM 643 C ILE A 116 80.968 231.467 -2.228 1.00 43.02 C ANISOU 643 C ILE A 116 5925 3234 7188 329 -323 151 C ATOM 644 O ILE A 116 80.639 232.389 -2.976 1.00 45.30 O ANISOU 644 O ILE A 116 6323 3431 7458 379 -316 193 O ATOM 645 CB ILE A 116 79.908 229.195 -2.570 1.00 39.51 C ANISOU 645 CB ILE A 116 5372 2927 6712 329 -382 130 C ATOM 646 CG1 ILE A 116 79.941 227.967 -3.485 1.00 38.65 C ANISOU 646 CG1 ILE A 116 5273 2853 6560 316 -385 144 C ATOM 647 CG2 ILE A 116 78.633 230.019 -2.794 1.00 40.68 C ANISOU 647 CG2 ILE A 116 5555 3029 6872 407 -427 139 C ATOM 648 CD1 ILE A 116 78.659 227.152 -3.466 1.00 37.94 C ANISOU 648 CD1 ILE A 116 5111 2817 6489 345 -448 118 C ATOM 649 N THR A 117 81.150 231.665 -0.926 1.00 41.52 N ANISOU 649 N THR A 117 5640 3081 7055 307 -329 101 N ATOM 650 CA THR A 117 80.857 232.957 -0.325 1.00 42.10 C ANISOU 650 CA THR A 117 5726 3094 7177 338 -337 84 C ATOM 651 C THR A 117 82.102 233.786 -0.050 1.00 42.66 C ANISOU 651 C THR A 117 5825 3104 7280 297 -290 78 C ATOM 652 O THR A 117 81.984 234.989 0.202 1.00 43.16 O ANISOU 652 O THR A 117 5926 3089 7384 322 -288 72 O ATOM 653 CB THR A 117 80.071 232.759 0.972 1.00 28.56 C ANISOU 653 CB THR A 117 3893 1450 5509 353 -380 26 C ATOM 654 OG1 THR A 117 80.862 232.005 1.896 1.00 35.24 O ANISOU 654 OG1 THR A 117 4645 2373 6372 300 -364 -11 O ATOM 655 CG2 THR A 117 78.783 232.004 0.685 1.00 28.19 C ANISOU 655 CG2 THR A 117 3815 1454 5444 392 -428 28 C ATOM 656 N GLU A 118 83.284 233.178 -0.118 1.00 42.46 N ANISOU 656 N GLU A 118 5780 3107 7244 235 -252 76 N ATOM 657 CA GLU A 118 84.543 233.842 0.213 1.00 43.59 C ANISOU 657 CA GLU A 118 5926 3203 7433 189 -209 59 C ATOM 658 C GLU A 118 84.504 234.430 1.623 1.00 41.11 C ANISOU 658 C GLU A 118 5522 2904 7194 194 -230 -7 C ATOM 659 O GLU A 118 85.089 235.478 1.899 1.00 42.28 O ANISOU 659 O GLU A 118 5690 2977 7398 181 -208 -25 O ATOM 660 CB GLU A 118 84.887 234.916 -0.820 1.00 45.75 C ANISOU 660 CB GLU A 118 6342 3344 7696 192 -171 113 C ATOM 661 CG GLU A 118 85.101 234.346 -2.223 1.00 49.21 C ANISOU 661 CG GLU A 118 6884 3761 8052 186 -145 178 C ATOM 662 CD GLU A 118 85.433 235.408 -3.271 1.00 54.37 C ANISOU 662 CD GLU A 118 7699 4274 8686 194 -106 241 C ATOM 663 OE1 GLU A 118 85.820 236.534 -2.873 1.00 56.12 O ANISOU 663 OE1 GLU A 118 7937 4414 8972 181 -89 230 O ATOM 664 OE2 GLU A 118 85.310 235.115 -4.487 1.00 56.02 O ANISOU 664 OE2 GLU A 118 8023 4447 8814 213 -93 302 O ATOM 665 N THR A 119 83.825 233.732 2.538 1.00 39.20 N ANISOU 665 N THR A 119 5183 2756 6957 212 -270 -45 N ATOM 666 CA THR A 119 83.656 234.207 3.906 1.00 37.49 C ANISOU 666 CA THR A 119 4887 2557 6798 227 -293 -111 C ATOM 667 C THR A 119 83.695 233.039 4.881 1.00 35.75 C ANISOU 667 C THR A 119 4560 2451 6572 214 -308 -148 C ATOM 668 O THR A 119 83.272 231.926 4.557 1.00 35.33 O ANISOU 668 O THR A 119 4488 2462 6473 213 -317 -123 O ATOM 669 CB THR A 119 82.345 234.972 4.070 1.00 37.13 C ANISOU 669 CB THR A 119 4864 2476 6769 289 -331 -117 C ATOM 670 OG1 THR A 119 82.339 236.101 3.187 1.00 38.23 O ANISOU 670 OG1 THR A 119 5113 2498 6915 308 -314 -77 O ATOM 671 CG2 THR A 119 82.198 235.463 5.498 1.00 37.19 C ANISOU 671 CG2 THR A 119 4795 2501 6835 306 -353 -191 C ATOM 672 N TRP A 120 84.215 233.304 6.084 1.00 35.11 N ANISOU 672 N TRP A 120 4413 2388 6538 208 -310 -209 N ATOM 673 CA TRP A 120 84.327 232.299 7.142 1.00 33.60 C ANISOU 673 CA TRP A 120 4135 2292 6340 204 -320 -245 C ATOM 674 C TRP A 120 83.189 232.505 8.138 1.00 34.06 C ANISOU 674 C TRP A 120 4158 2373 6410 253 -356 -284 C ATOM 675 O TRP A 120 83.251 233.390 8.995 1.00 34.41 O ANISOU 675 O TRP A 120 4187 2388 6500 273 -367 -340 O ATOM 676 CB TRP A 120 85.691 232.366 7.827 1.00 32.20 C ANISOU 676 CB TRP A 120 3914 2121 6200 173 -301 -292 C ATOM 677 CG TRP A 120 85.896 231.246 8.793 1.00 30.72 C ANISOU 677 CG TRP A 120 3655 2023 5993 173 -309 -318 C ATOM 678 CD1 TRP A 120 85.887 231.325 10.153 1.00 30.67 C ANISOU 678 CD1 TRP A 120 3600 2046 6008 198 -329 -382 C ATOM 679 CD2 TRP A 120 86.106 229.863 8.476 1.00 29.93 C ANISOU 679 CD2 TRP A 120 3536 1989 5846 153 -296 -282 C ATOM 680 NE1 TRP A 120 86.089 230.081 10.707 1.00 29.61 N ANISOU 680 NE1 TRP A 120 3426 1987 5839 195 -326 -381 N ATOM 681 CE2 TRP A 120 86.223 229.166 9.697 1.00 29.31 C ANISOU 681 CE2 TRP A 120 3400 1971 5763 166 -306 -319 C ATOM 682 CE3 TRP A 120 86.216 229.148 7.280 1.00 29.88 C ANISOU 682 CE3 TRP A 120 3561 1991 5802 128 -276 -223 C ATOM 683 CZ2 TRP A 120 86.444 227.790 9.756 1.00 28.64 C ANISOU 683 CZ2 TRP A 120 3289 1950 5642 154 -295 -295 C ATOM 684 CZ3 TRP A 120 86.437 227.780 7.341 1.00 28.93 C ANISOU 684 CZ3 TRP A 120 3404 1940 5649 115 -268 -207 C ATOM 685 CH2 TRP A 120 86.549 227.117 8.570 1.00 28.29 C ANISOU 685 CH2 TRP A 120 3266 1914 5570 127 -276 -240 C ATOM 686 N PHE A 121 82.144 231.684 8.011 1.00 34.30 N ANISOU 686 N PHE A 121 4174 2452 6405 272 -372 -259 N ATOM 687 CA PHE A 121 80.966 231.783 8.861 1.00 35.12 C ANISOU 687 CA PHE A 121 4246 2578 6519 319 -398 -291 C ATOM 688 C PHE A 121 81.111 231.048 10.188 1.00 34.52 C ANISOU 688 C PHE A 121 4107 2570 6438 323 -393 -332 C ATOM 689 O PHE A 121 80.288 231.253 11.087 1.00 35.12 O ANISOU 689 O PHE A 121 4162 2659 6524 366 -406 -369 O ATOM 690 CB PHE A 121 79.740 231.253 8.110 1.00 25.94 C ANISOU 690 CB PHE A 121 3095 1431 5332 338 -416 -249 C ATOM 691 CG PHE A 121 79.334 232.111 6.958 1.00 26.73 C ANISOU 691 CG PHE A 121 3267 1456 5433 358 -430 -216 C ATOM 692 CD1 PHE A 121 78.614 233.270 7.174 1.00 28.09 C ANISOU 692 CD1 PHE A 121 3462 1572 5639 408 -453 -240 C ATOM 693 CD2 PHE A 121 79.690 231.776 5.665 1.00 26.67 C ANISOU 693 CD2 PHE A 121 3314 1430 5390 333 -418 -161 C ATOM 694 CE1 PHE A 121 78.246 234.075 6.122 1.00 28.46 C ANISOU 694 CE1 PHE A 121 3588 1542 5685 435 -464 -204 C ATOM 695 CE2 PHE A 121 79.328 232.581 4.606 1.00 27.51 C ANISOU 695 CE2 PHE A 121 3505 1459 5488 361 -426 -125 C ATOM 696 CZ PHE A 121 78.603 233.731 4.833 1.00 28.42 C ANISOU 696 CZ PHE A 121 3645 1515 5638 413 -449 -144 C ATOM 697 N PHE A 122 82.124 230.209 10.330 1.00 34.21 N ANISOU 697 N PHE A 122 4047 2571 6381 286 -372 -325 N ATOM 698 CA PHE A 122 82.352 229.425 11.532 1.00 34.07 C ANISOU 698 CA PHE A 122 3986 2611 6349 295 -363 -356 C ATOM 699 C PHE A 122 83.293 230.173 12.469 1.00 35.03 C ANISOU 699 C PHE A 122 4096 2713 6499 303 -369 -423 C ATOM 700 O PHE A 122 83.831 231.228 12.137 1.00 35.56 O ANISOU 700 O PHE A 122 4180 2724 6607 292 -374 -444 O ATOM 701 CB PHE A 122 82.883 228.053 11.142 1.00 32.65 C ANISOU 701 CB PHE A 122 3791 2480 6135 258 -341 -311 C ATOM 702 CG PHE A 122 82.248 227.533 9.896 1.00 31.97 C ANISOU 702 CG PHE A 122 3720 2395 6030 241 -340 -253 C ATOM 703 CD1 PHE A 122 81.036 226.872 9.947 1.00 31.54 C ANISOU 703 CD1 PHE A 122 3648 2368 5967 258 -344 -235 C ATOM 704 CD2 PHE A 122 82.829 227.769 8.663 1.00 32.26 C ANISOU 704 CD2 PHE A 122 3794 2399 6062 211 -335 -221 C ATOM 705 CE1 PHE A 122 80.435 226.425 8.804 1.00 31.16 C ANISOU 705 CE1 PHE A 122 3612 2319 5910 246 -352 -192 C ATOM 706 CE2 PHE A 122 82.235 227.328 7.510 1.00 31.95 C ANISOU 706 CE2 PHE A 122 3779 2358 6000 204 -339 -174 C ATOM 707 CZ PHE A 122 81.032 226.653 7.578 1.00 31.38 C ANISOU 707 CZ PHE A 122 3682 2317 5924 222 -352 -164 C ATOM 708 N GLY A 123 83.466 229.636 13.664 1.00 36.23 N ANISOU 708 N GLY A 123 4223 2909 6634 327 -366 -461 N ATOM 709 CA GLY A 123 84.154 230.377 14.695 1.00 37.79 C ANISOU 709 CA GLY A 123 4408 3093 6857 350 -382 -542 C ATOM 710 C GLY A 123 85.633 230.510 14.420 1.00 38.61 C ANISOU 710 C GLY A 123 4499 3182 6990 307 -379 -559 C ATOM 711 O GLY A 123 86.173 229.992 13.440 1.00 38.76 O ANISOU 711 O GLY A 123 4522 3203 7003 261 -360 -505 O ATOM 712 N GLN A 124 86.288 231.296 15.276 1.00 38.55 N ANISOU 712 N GLN A 124 4472 3156 7021 325 -399 -644 N ATOM 713 CA GLN A 124 87.744 231.299 15.284 1.00 38.70 C ANISOU 713 CA GLN A 124 4463 3168 7072 291 -399 -678 C ATOM 714 C GLN A 124 88.296 229.948 15.721 1.00 37.92 C ANISOU 714 C GLN A 124 4351 3134 6924 292 -392 -665 C ATOM 715 O GLN A 124 89.364 229.532 15.255 1.00 38.06 O ANISOU 715 O GLN A 124 4350 3156 6956 252 -381 -653 O ATOM 716 CB GLN A 124 88.260 232.403 16.204 1.00 40.54 C ANISOU 716 CB GLN A 124 4669 3371 7362 315 -429 -787 C ATOM 717 CG GLN A 124 89.709 232.222 16.622 1.00 42.62 C ANISOU 717 CG GLN A 124 4890 3648 7657 298 -439 -848 C ATOM 718 CD GLN A 124 90.692 232.826 15.637 1.00 46.00 C ANISOU 718 CD GLN A 124 5302 4017 8158 236 -417 -840 C ATOM 719 OE1 GLN A 124 90.657 234.034 15.369 1.00 49.34 O ANISOU 719 OE1 GLN A 124 5729 4370 8648 226 -416 -867 O ATOM 720 NE2 GLN A 124 91.579 231.994 15.096 1.00 44.78 N ANISOU 720 NE2 GLN A 124 5132 3886 7996 199 -394 -802 N ATOM 721 N SER A 125 87.573 229.237 16.590 1.00 37.57 N ANISOU 721 N SER A 125 4319 3134 6821 342 -393 -663 N ATOM 722 CA SER A 125 88.029 227.926 17.030 1.00 37.04 C ANISOU 722 CA SER A 125 4252 3117 6703 352 -381 -643 C ATOM 723 C SER A 125 88.009 226.929 15.881 1.00 35.22 C ANISOU 723 C SER A 125 4027 2901 6455 300 -351 -548 C ATOM 724 O SER A 125 88.967 226.174 15.686 1.00 33.99 O ANISOU 724 O SER A 125 3856 2762 6294 275 -344 -535 O ATOM 725 CB SER A 125 87.164 227.436 18.187 1.00 38.47 C ANISOU 725 CB SER A 125 4452 3331 6833 428 -377 -655 C ATOM 726 OG SER A 125 87.134 228.398 19.225 1.00 40.46 O ANISOU 726 OG SER A 125 4677 3569 7129 486 -417 -762 O ATOM 727 N LEU A 126 86.933 226.927 15.093 1.00 34.15 N ANISOU 727 N LEU A 126 3906 2756 6312 287 -338 -489 N ATOM 728 CA LEU A 126 86.876 226.053 13.927 1.00 32.72 C ANISOU 728 CA LEU A 126 3726 2589 6115 242 -315 -411 C ATOM 729 C LEU A 126 87.803 226.518 12.813 1.00 32.78 C ANISOU 729 C LEU A 126 3730 2567 6159 194 -309 -402 C ATOM 730 O LEU A 126 88.121 225.726 11.923 1.00 32.74 O ANISOU 730 O LEU A 126 3724 2577 6137 162 -289 -351 O ATOM 731 CB LEU A 126 85.442 225.952 13.406 1.00 31.52 C ANISOU 731 CB LEU A 126 3590 2437 5950 249 -308 -363 C ATOM 732 CG LEU A 126 84.463 225.204 14.309 1.00 29.93 C ANISOU 732 CG LEU A 126 3392 2267 5715 291 -295 -353 C ATOM 733 CD1 LEU A 126 83.167 224.896 13.580 1.00 29.15 C ANISOU 733 CD1 LEU A 126 3292 2169 5616 285 -288 -304 C ATOM 734 CD2 LEU A 126 85.095 223.934 14.811 1.00 28.84 C ANISOU 734 CD2 LEU A 126 3251 2164 5544 292 -275 -334 C ATOM 735 N CYS A 127 88.223 227.786 12.831 1.00 32.56 N ANISOU 735 N CYS A 127 3701 2490 6178 192 -321 -450 N ATOM 736 CA CYS A 127 89.208 228.243 11.859 1.00 33.17 C ANISOU 736 CA CYS A 127 3779 2530 6292 149 -304 -442 C ATOM 737 C CYS A 127 90.554 227.544 12.069 1.00 32.89 C ANISOU 737 C CYS A 127 3709 2522 6267 129 -295 -463 C ATOM 738 O CYS A 127 91.327 227.389 11.114 1.00 34.48 O ANISOU 738 O CYS A 127 3911 2709 6480 92 -268 -436 O ATOM 739 CB CYS A 127 89.327 229.775 11.936 1.00 35.38 C ANISOU 739 CB CYS A 127 4068 2742 6634 151 -313 -491 C ATOM 740 SG CYS A 127 90.637 230.549 10.942 1.00 36.73 S ANISOU 740 SG CYS A 127 4244 2845 6868 99 -280 -494 S ATOM 741 N LYS A 128 90.860 227.121 13.304 1.00 31.41 N ANISOU 741 N LYS A 128 3496 2369 6070 159 -318 -514 N ATOM 742 CA LYS A 128 92.028 226.283 13.563 1.00 23.34 C ANISOU 742 CA LYS A 128 2443 1377 5048 151 -316 -532 C ATOM 743 C LYS A 128 91.748 224.798 13.320 1.00 27.54 C ANISOU 743 C LYS A 128 2987 1955 5522 149 -299 -464 C ATOM 744 O LYS A 128 92.585 224.087 12.749 1.00 22.24 O ANISOU 744 O LYS A 128 2301 1297 4853 123 -282 -443 O ATOM 745 CB LYS A 128 92.508 226.484 15.004 1.00 23.69 C ANISOU 745 CB LYS A 128 2465 1433 5103 194 -354 -622 C ATOM 746 CG LYS A 128 92.702 227.919 15.405 1.00 24.74 C ANISOU 746 CG LYS A 128 2578 1523 5299 201 -378 -704 C ATOM 747 CD LYS A 128 94.072 228.414 14.996 1.00 25.22 C ANISOU 747 CD LYS A 128 2592 1554 5437 161 -371 -750 C ATOM 748 CE LYS A 128 94.749 229.153 16.129 1.00 26.06 C ANISOU 748 CE LYS A 128 2653 1654 5595 190 -416 -873 C ATOM 749 NZ LYS A 128 96.185 229.407 15.818 1.00 26.64 N ANISOU 749 NZ LYS A 128 2667 1707 5749 152 -408 -925 N ATOM 750 N VAL A 129 90.569 224.322 13.726 1.00 26.86 N ANISOU 750 N VAL A 129 2927 1890 5389 178 -299 -431 N ATOM 751 CA VAL A 129 90.327 222.887 13.788 1.00 25.69 C ANISOU 751 CA VAL A 129 2788 1780 5194 184 -282 -379 C ATOM 752 C VAL A 129 90.143 222.311 12.397 1.00 25.61 C ANISOU 752 C VAL A 129 2777 1775 5177 141 -256 -312 C ATOM 753 O VAL A 129 90.760 221.299 12.047 1.00 26.08 O ANISOU 753 O VAL A 129 2826 1855 5226 124 -241 -287 O ATOM 754 CB VAL A 129 89.109 222.588 14.679 1.00 25.39 C ANISOU 754 CB VAL A 129 2777 1754 5115 231 -279 -366 C ATOM 755 CG1 VAL A 129 88.693 221.140 14.522 1.00 25.12 C ANISOU 755 CG1 VAL A 129 2752 1747 5044 228 -251 -299 C ATOM 756 CG2 VAL A 129 89.414 222.887 16.141 1.00 25.33 C ANISOU 756 CG2 VAL A 129 2783 1749 5094 293 -300 -433 C ATOM 757 N ILE A 130 89.270 222.919 11.591 1.00 25.25 N ANISOU 757 N ILE A 130 2747 1710 5136 130 -253 -286 N ATOM 758 CA ILE A 130 89.009 222.388 10.249 1.00 24.45 C ANISOU 758 CA ILE A 130 2656 1614 5020 100 -234 -230 C ATOM 759 C ILE A 130 90.277 222.348 9.408 1.00 25.36 C ANISOU 759 C ILE A 130 2766 1719 5151 68 -216 -231 C ATOM 760 O ILE A 130 90.572 221.292 8.811 1.00 25.77 O ANISOU 760 O ILE A 130 2813 1794 5184 53 -199 -200 O ATOM 761 CB ILE A 130 87.902 223.205 9.569 1.00 23.80 C ANISOU 761 CB ILE A 130 2601 1503 4938 103 -242 -212 C ATOM 762 CG1 ILE A 130 86.539 222.771 10.099 1.00 23.79 C ANISOU 762 CG1 ILE A 130 2596 1522 4921 128 -249 -196 C ATOM 763 CG2 ILE A 130 87.968 223.064 8.047 1.00 23.26 C ANISOU 763 CG2 ILE A 130 2559 1420 4857 75 -227 -171 C ATOM 764 CD1 ILE A 130 85.404 223.626 9.601 1.00 24.06 C ANISOU 764 CD1 ILE A 130 2652 1526 4962 140 -265 -189 C ATOM 765 N PRO A 131 91.048 223.435 9.284 1.00 24.96 N ANISOU 765 N PRO A 131 2717 1629 5137 57 -215 -267 N ATOM 766 CA PRO A 131 92.302 223.350 8.513 1.00 21.84 C ANISOU 766 CA PRO A 131 2315 1220 4763 26 -188 -270 C ATOM 767 C PRO A 131 93.263 222.322 9.059 1.00 27.96 C ANISOU 767 C PRO A 131 3050 2032 5541 28 -188 -289 C ATOM 768 O PRO A 131 94.007 221.707 8.284 1.00 28.11 O ANISOU 768 O PRO A 131 3064 2057 5560 6 -163 -272 O ATOM 769 CB PRO A 131 92.862 224.780 8.632 1.00 22.65 C ANISOU 769 CB PRO A 131 2418 1267 4920 17 -187 -316 C ATOM 770 CG PRO A 131 91.638 225.635 8.805 1.00 22.89 C ANISOU 770 CG PRO A 131 2479 1273 4944 38 -208 -310 C ATOM 771 CD PRO A 131 90.688 224.815 9.643 1.00 22.27 C ANISOU 771 CD PRO A 131 2389 1246 4828 69 -231 -301 C ATOM 772 N TYR A 132 93.279 222.125 10.367 1.00 27.80 N ANISOU 772 N TYR A 132 3008 2032 5522 57 -215 -325 N ATOM 773 CA TYR A 132 94.096 221.071 10.946 1.00 27.55 C ANISOU 773 CA TYR A 132 2950 2030 5486 66 -221 -338 C ATOM 774 C TYR A 132 93.610 219.694 10.500 1.00 27.31 C ANISOU 774 C TYR A 132 2932 2031 5413 63 -203 -276 C ATOM 775 O TYR A 132 94.398 218.868 10.021 1.00 26.75 O ANISOU 775 O TYR A 132 2846 1972 5345 49 -188 -266 O ATOM 776 CB TYR A 132 94.071 221.196 12.465 1.00 27.53 C ANISOU 776 CB TYR A 132 2944 2035 5481 108 -256 -389 C ATOM 777 CG TYR A 132 94.913 220.178 13.157 1.00 21.09 C ANISOU 777 CG TYR A 132 2117 1241 4655 128 -267 -407 C ATOM 778 CD1 TYR A 132 96.286 220.338 13.255 1.00 21.44 C ANISOU 778 CD1 TYR A 132 2120 1279 4746 122 -280 -466 C ATOM 779 CD2 TYR A 132 94.341 219.047 13.707 1.00 27.49 C ANISOU 779 CD2 TYR A 132 2958 2073 5414 158 -263 -365 C ATOM 780 CE1 TYR A 132 97.064 219.405 13.891 1.00 27.64 C ANISOU 780 CE1 TYR A 132 2899 2082 5522 148 -297 -486 C ATOM 781 CE2 TYR A 132 95.111 218.100 14.345 1.00 27.23 C ANISOU 781 CE2 TYR A 132 2928 2051 5366 187 -273 -375 C ATOM 782 CZ TYR A 132 96.471 218.286 14.434 1.00 26.62 C ANISOU 782 CZ TYR A 132 2813 1970 5332 184 -294 -437 C ATOM 783 OH TYR A 132 97.239 217.345 15.071 1.00 27.32 O ANISOU 783 OH TYR A 132 2908 2067 5404 222 -310 -451 O ATOM 784 N LEU A 133 92.306 219.437 10.617 1.00 27.20 N ANISOU 784 N LEU A 133 2941 2028 5366 76 -204 -239 N ATOM 785 CA LEU A 133 91.793 218.129 10.230 1.00 27.65 C ANISOU 785 CA LEU A 133 3002 2110 5395 72 -186 -186 C ATOM 786 C LEU A 133 92.009 217.867 8.748 1.00 28.73 C ANISOU 786 C LEU A 133 3141 2245 5532 41 -166 -160 C ATOM 787 O LEU A 133 92.239 216.722 8.348 1.00 28.72 O ANISOU 787 O LEU A 133 3131 2261 5522 33 -151 -136 O ATOM 788 CB LEU A 133 90.312 218.018 10.581 1.00 27.48 C ANISOU 788 CB LEU A 133 2997 2094 5352 89 -187 -158 C ATOM 789 CG LEU A 133 90.039 218.230 12.070 1.00 27.86 C ANISOU 789 CG LEU A 133 3058 2138 5389 130 -199 -182 C ATOM 790 CD1 LEU A 133 88.565 218.469 12.297 1.00 27.94 C ANISOU 790 CD1 LEU A 133 3082 2145 5388 146 -196 -163 C ATOM 791 CD2 LEU A 133 90.548 217.050 12.905 1.00 27.51 C ANISOU 791 CD2 LEU A 133 3023 2106 5325 154 -190 -171 C ATOM 792 N GLN A 134 91.957 218.907 7.919 1.00 30.14 N ANISOU 792 N GLN A 134 3338 2396 5718 25 -162 -164 N ATOM 793 CA GLN A 134 92.136 218.696 6.490 1.00 31.07 C ANISOU 793 CA GLN A 134 3478 2503 5825 1 -140 -138 C ATOM 794 C GLN A 134 93.585 218.350 6.173 1.00 29.96 C ANISOU 794 C GLN A 134 3320 2361 5704 -15 -119 -157 C ATOM 795 O GLN A 134 93.859 217.375 5.466 1.00 32.37 O ANISOU 795 O GLN A 134 3625 2678 5995 -25 -102 -138 O ATOM 796 CB GLN A 134 91.672 219.933 5.717 1.00 34.16 C ANISOU 796 CB GLN A 134 3913 2853 6213 -8 -140 -131 C ATOM 797 CG GLN A 134 91.738 219.794 4.205 1.00 36.51 C ANISOU 797 CG GLN A 134 4257 3129 6486 -29 -118 -102 C ATOM 798 CD GLN A 134 90.868 218.664 3.670 1.00 38.16 C ANISOU 798 CD GLN A 134 4470 3365 6665 -25 -125 -71 C ATOM 799 OE1 GLN A 134 89.684 218.552 4.012 1.00 38.39 O ANISOU 799 OE1 GLN A 134 4492 3406 6688 -9 -148 -60 O ATOM 800 NE2 GLN A 134 91.455 217.818 2.820 1.00 38.67 N ANISOU 800 NE2 GLN A 134 4543 3434 6716 -40 -105 -63 N ATOM 801 N THR A 135 94.535 219.113 6.722 1.00 28.20 N ANISOU 801 N THR A 135 3076 2120 5519 -17 -120 -201 N ATOM 802 CA THR A 135 95.940 218.816 6.460 1.00 20.76 C ANISOU 802 CA THR A 135 2107 1173 4607 -32 -98 -227 C ATOM 803 C THR A 135 96.361 217.491 7.086 1.00 22.55 C ANISOU 803 C THR A 135 2300 1437 4832 -17 -109 -230 C ATOM 804 O THR A 135 97.086 216.709 6.464 1.00 20.32 O ANISOU 804 O THR A 135 2007 1159 4554 -28 -87 -226 O ATOM 805 CB THR A 135 96.819 219.956 6.965 1.00 21.33 C ANISOU 805 CB THR A 135 2155 1215 4736 -38 -99 -283 C ATOM 806 OG1 THR A 135 96.547 220.192 8.349 1.00 24.26 O ANISOU 806 OG1 THR A 135 2503 1599 5116 -10 -141 -317 O ATOM 807 CG2 THR A 135 96.528 221.226 6.169 1.00 22.15 C ANISOU 807 CG2 THR A 135 2302 1268 4847 -60 -78 -273 C ATOM 808 N VAL A 136 95.884 217.199 8.299 1.00 22.19 N ANISOU 808 N VAL A 136 2246 1409 4775 11 -139 -235 N ATOM 809 CA VAL A 136 96.218 215.924 8.927 1.00 21.65 C ANISOU 809 CA VAL A 136 2163 1363 4699 28 -148 -229 C ATOM 810 C VAL A 136 95.757 214.782 8.043 1.00 22.04 C ANISOU 810 C VAL A 136 2224 1427 4724 18 -125 -179 C ATOM 811 O VAL A 136 96.475 213.792 7.850 1.00 22.99 O ANISOU 811 O VAL A 136 2329 1554 4853 17 -115 -178 O ATOM 812 CB VAL A 136 95.581 215.825 10.327 1.00 21.02 C ANISOU 812 CB VAL A 136 2099 1290 4598 63 -175 -232 C ATOM 813 CG1 VAL A 136 95.646 214.392 10.836 1.00 20.33 C ANISOU 813 CG1 VAL A 136 2021 1215 4490 83 -173 -204 C ATOM 814 CG2 VAL A 136 96.266 216.771 11.288 1.00 21.45 C ANISOU 814 CG2 VAL A 136 2139 1331 4679 81 -205 -298 C ATOM 815 N SER A 137 94.555 214.912 7.476 1.00 21.19 N ANISOU 815 N SER A 137 2141 1321 4591 12 -119 -144 N ATOM 816 CA SER A 137 94.003 213.858 6.639 1.00 20.50 C ANISOU 816 CA SER A 137 2061 1244 4486 3 -104 -107 C ATOM 817 C SER A 137 94.774 213.713 5.338 1.00 20.84 C ANISOU 817 C SER A 137 2110 1276 4532 -19 -81 -112 C ATOM 818 O SER A 137 94.791 212.627 4.749 1.00 20.74 O ANISOU 818 O SER A 137 2095 1270 4515 -23 -69 -97 O ATOM 819 CB SER A 137 92.530 214.135 6.365 1.00 20.29 C ANISOU 819 CB SER A 137 2055 1217 4439 4 -111 -79 C ATOM 820 OG SER A 137 91.924 213.027 5.731 1.00 20.54 O ANISOU 820 OG SER A 137 2084 1257 4463 -1 -102 -52 O ATOM 821 N VAL A 138 95.375 214.800 4.852 1.00 21.27 N ANISOU 821 N VAL A 138 2178 1307 4597 -33 -70 -134 N ATOM 822 CA VAL A 138 96.219 214.703 3.667 1.00 21.95 C ANISOU 822 CA VAL A 138 2278 1375 4686 -56 -38 -140 C ATOM 823 C VAL A 138 97.509 213.977 3.997 1.00 21.80 C ANISOU 823 C VAL A 138 2217 1366 4702 -53 -28 -168 C ATOM 824 O VAL A 138 98.036 213.211 3.184 1.00 21.80 O ANISOU 824 O VAL A 138 2217 1362 4702 -64 -5 -168 O ATOM 825 CB VAL A 138 96.506 216.101 3.098 1.00 23.00 C ANISOU 825 CB VAL A 138 2444 1469 4825 -76 -19 -151 C ATOM 826 CG1 VAL A 138 97.633 216.031 2.082 1.00 23.03 C ANISOU 826 CG1 VAL A 138 2461 1449 4841 -101 24 -163 C ATOM 827 CG2 VAL A 138 95.241 216.699 2.488 1.00 23.94 C ANISOU 827 CG2 VAL A 138 2621 1572 4905 -78 -29 -118 C ATOM 828 N SER A 139 98.054 214.226 5.187 1.00 22.59 N ANISOU 828 N SER A 139 2279 1471 4832 -39 -49 -199 N ATOM 829 CA SER A 139 99.264 213.529 5.603 1.00 23.43 C ANISOU 829 CA SER A 139 2343 1583 4975 -32 -50 -232 C ATOM 830 C SER A 139 98.979 212.058 5.875 1.00 23.03 C ANISOU 830 C SER A 139 2290 1551 4908 -15 -60 -204 C ATOM 831 O SER A 139 99.686 211.175 5.373 1.00 23.35 O ANISOU 831 O SER A 139 2316 1591 4965 -19 -44 -210 O ATOM 832 CB SER A 139 99.851 214.208 6.838 1.00 24.22 C ANISOU 832 CB SER A 139 2411 1680 5111 -16 -80 -279 C ATOM 833 OG SER A 139 100.910 213.440 7.376 1.00 24.40 O ANISOU 833 OG SER A 139 2397 1709 5166 -2 -94 -312 O ATOM 834 N VAL A 140 97.914 211.771 6.625 1.00 22.36 N ANISOU 834 N VAL A 140 2221 1478 4795 2 -81 -173 N ATOM 835 CA VAL A 140 97.575 210.384 6.910 1.00 22.67 C ANISOU 835 CA VAL A 140 2265 1524 4825 16 -82 -142 C ATOM 836 C VAL A 140 97.361 209.630 5.614 1.00 22.99 C ANISOU 836 C VAL A 140 2310 1564 4861 -2 -56 -122 C ATOM 837 O VAL A 140 97.730 208.455 5.502 1.00 23.25 O ANISOU 837 O VAL A 140 2333 1593 4907 3 -49 -116 O ATOM 838 CB VAL A 140 96.336 210.333 7.828 1.00 19.27 C ANISOU 838 CB VAL A 140 1857 1099 4368 33 -94 -108 C ATOM 839 CG1 VAL A 140 95.838 208.912 7.994 1.00 26.31 C ANISOU 839 CG1 VAL A 140 2755 1987 5254 43 -82 -68 C ATOM 840 CG2 VAL A 140 96.664 210.951 9.189 1.00 19.38 C ANISOU 840 CG2 VAL A 140 1877 1107 4381 60 -121 -134 C ATOM 841 N SER A 141 96.837 210.311 4.594 1.00 24.85 N ANISOU 841 N SER A 141 2568 1796 5078 -20 -44 -117 N ATOM 842 CA SER A 141 96.614 209.677 3.297 1.00 23.04 C ANISOU 842 CA SER A 141 2356 1560 4838 -35 -25 -106 C ATOM 843 C SER A 141 97.930 209.352 2.598 1.00 23.00 C ANISOU 843 C SER A 141 2342 1544 4855 -45 -1 -135 C ATOM 844 O SER A 141 98.120 208.236 2.095 1.00 23.03 O ANISOU 844 O SER A 141 2340 1545 4867 -46 9 -134 O ATOM 845 CB SER A 141 95.755 210.580 2.408 1.00 22.16 C ANISOU 845 CB SER A 141 2287 1439 4695 -49 -24 -95 C ATOM 846 OG SER A 141 94.451 210.749 2.941 1.00 22.02 O ANISOU 846 OG SER A 141 2272 1431 4664 -38 -46 -71 O ATOM 847 N ALA A 142 98.853 210.315 2.548 1.00 22.89 N ANISOU 847 N ALA A 142 2322 1519 4856 -55 12 -165 N ATOM 848 CA ALA A 142 100.093 210.089 1.814 1.00 22.89 C ANISOU 848 CA ALA A 142 2311 1505 4883 -69 44 -196 C ATOM 849 C ALA A 142 100.960 209.044 2.505 1.00 23.10 C ANISOU 849 C ALA A 142 2289 1539 4949 -52 34 -216 C ATOM 850 O ALA A 142 101.442 208.103 1.864 1.00 23.60 O ANISOU 850 O ALA A 142 2346 1595 5025 -55 52 -225 O ATOM 851 CB ALA A 142 100.856 211.403 1.643 1.00 22.97 C ANISOU 851 CB ALA A 142 2321 1493 4912 -88 68 -224 C ATOM 852 N LEU A 143 101.151 209.172 3.821 1.00 22.97 N ANISOU 852 N LEU A 143 2245 1533 4952 -32 2 -226 N ATOM 853 CA LEU A 143 101.976 208.193 4.526 1.00 22.73 C ANISOU 853 CA LEU A 143 2181 1502 4955 -11 -15 -244 C ATOM 854 C LEU A 143 101.355 206.807 4.503 1.00 23.08 C ANISOU 854 C LEU A 143 2240 1544 4984 0 -19 -205 C ATOM 855 O LEU A 143 102.078 205.803 4.498 1.00 23.33 O ANISOU 855 O LEU A 143 2255 1565 5044 10 -18 -218 O ATOM 856 CB LEU A 143 102.203 208.618 5.973 1.00 22.08 C ANISOU 856 CB LEU A 143 2084 1422 4884 12 -56 -262 C ATOM 857 CG LEU A 143 102.897 209.962 6.068 1.00 21.37 C ANISOU 857 CG LEU A 143 1967 1327 4825 1 -55 -312 C ATOM 858 CD1 LEU A 143 103.009 210.391 7.517 1.00 21.01 C ANISOU 858 CD1 LEU A 143 1913 1283 4786 28 -104 -338 C ATOM 859 CD2 LEU A 143 104.245 209.847 5.403 1.00 21.02 C ANISOU 859 CD2 LEU A 143 1881 1272 4836 -13 -28 -361 C ATOM 860 N THR A 144 100.026 206.723 4.505 1.00 23.00 N ANISOU 860 N THR A 144 2259 1541 4938 0 -22 -163 N ATOM 861 CA THR A 144 99.411 205.408 4.404 1.00 23.54 C ANISOU 861 CA THR A 144 2336 1601 5005 6 -18 -130 C ATOM 862 C THR A 144 99.643 204.806 3.026 1.00 23.74 C ANISOU 862 C THR A 144 2362 1617 5040 -10 7 -144 C ATOM 863 O THR A 144 99.978 203.624 2.918 1.00 24.13 O ANISOU 863 O THR A 144 2401 1651 5115 -3 12 -145 O ATOM 864 CB THR A 144 97.917 205.477 4.729 1.00 23.95 C ANISOU 864 CB THR A 144 2409 1661 5029 8 -24 -89 C ATOM 865 OG1 THR A 144 97.742 205.842 6.105 1.00 24.52 O ANISOU 865 OG1 THR A 144 2490 1736 5092 28 -43 -76 O ATOM 866 CG2 THR A 144 97.256 204.124 4.491 1.00 23.88 C ANISOU 866 CG2 THR A 144 2402 1636 5034 10 -13 -61 C ATOM 867 N LEU A 145 99.511 205.599 1.961 1.00 20.01 N ANISOU 867 N LEU A 145 1910 1147 4546 -31 24 -156 N ATOM 868 CA LEU A 145 99.794 205.060 0.635 1.00 20.21 C ANISOU 868 CA LEU A 145 1949 1157 4573 -46 49 -173 C ATOM 869 C LEU A 145 101.251 204.661 0.495 1.00 30.47 C ANISOU 869 C LEU A 145 3219 2445 5912 -45 67 -213 C ATOM 870 O LEU A 145 101.574 203.701 -0.214 1.00 30.94 O ANISOU 870 O LEU A 145 3277 2489 5989 -48 81 -228 O ATOM 871 CB LEU A 145 99.449 206.079 -0.440 1.00 23.41 C ANISOU 871 CB LEU A 145 2401 1555 4938 -69 65 -176 C ATOM 872 CG LEU A 145 97.983 206.259 -0.743 1.00 20.06 C ANISOU 872 CG LEU A 145 2011 1133 4477 -72 47 -146 C ATOM 873 CD1 LEU A 145 97.901 207.424 -1.678 1.00 20.15 C ANISOU 873 CD1 LEU A 145 2079 1129 4448 -93 62 -148 C ATOM 874 CD2 LEU A 145 97.435 204.996 -1.372 1.00 20.20 C ANISOU 874 CD2 LEU A 145 2033 1139 4503 -71 44 -145 C ATOM 875 N SER A 146 102.146 205.408 1.133 1.00 29.80 N ANISOU 875 N SER A 146 3107 2366 5850 -42 65 -236 N ATOM 876 CA SER A 146 103.548 205.024 1.112 1.00 29.81 C ANISOU 876 CA SER A 146 3069 2356 5901 -39 78 -280 C ATOM 877 C SER A 146 103.774 203.733 1.889 1.00 30.54 C ANISOU 877 C SER A 146 3139 2442 6023 -13 51 -275 C ATOM 878 O SER A 146 104.600 202.903 1.492 1.00 31.06 O ANISOU 878 O SER A 146 3184 2492 6125 -9 63 -304 O ATOM 879 CB SER A 146 104.408 206.161 1.664 1.00 28.57 C ANISOU 879 CB SER A 146 2880 2203 5771 -43 78 -315 C ATOM 880 OG SER A 146 104.226 207.335 0.888 1.00 27.65 O ANISOU 880 OG SER A 146 2793 2080 5630 -69 111 -316 O ATOM 881 N CYS A 147 103.051 203.537 2.995 1.00 30.30 N ANISOU 881 N CYS A 147 3119 2417 5976 7 18 -238 N ATOM 882 CA CYS A 147 103.225 202.296 3.740 1.00 32.17 C ANISOU 882 CA CYS A 147 3355 2634 6235 34 -2 -223 C ATOM 883 C CYS A 147 102.685 201.101 2.979 1.00 32.86 C ANISOU 883 C CYS A 147 3454 2702 6328 30 16 -204 C ATOM 884 O CYS A 147 103.210 199.993 3.120 1.00 32.39 O ANISOU 884 O CYS A 147 3389 2616 6303 47 13 -209 O ATOM 885 CB CYS A 147 102.562 202.391 5.107 1.00 33.44 C ANISOU 885 CB CYS A 147 3541 2795 6370 58 -30 -184 C ATOM 886 SG CYS A 147 103.512 203.377 6.258 1.00 35.53 S ANISOU 886 SG CYS A 147 3792 3066 6642 80 -66 -223 S ATOM 887 N ILE A 148 101.636 201.290 2.185 1.00 33.03 N ANISOU 887 N ILE A 148 3496 2733 6322 9 31 -186 N ATOM 888 CA ILE A 148 101.148 200.179 1.381 1.00 33.59 C ANISOU 888 CA ILE A 148 3575 2783 6407 4 44 -182 C ATOM 889 C ILE A 148 102.194 199.784 0.354 1.00 34.19 C ANISOU 889 C ILE A 148 3637 2843 6509 -4 64 -231 C ATOM 890 O ILE A 148 102.391 198.597 0.065 1.00 34.79 O ANISOU 890 O ILE A 148 3707 2892 6621 4 69 -241 O ATOM 891 CB ILE A 148 99.817 200.550 0.713 1.00 32.96 C ANISOU 891 CB ILE A 148 3519 2712 6291 -14 47 -163 C ATOM 892 CG1 ILE A 148 98.712 200.649 1.759 1.00 20.91 C ANISOU 892 CG1 ILE A 148 1997 1193 4753 -5 31 -116 C ATOM 893 CG2 ILE A 148 99.480 199.544 -0.358 1.00 21.40 C ANISOU 893 CG2 ILE A 148 2061 1223 4847 -23 58 -179 C ATOM 894 CD1 ILE A 148 97.537 201.471 1.304 1.00 20.62 C ANISOU 894 CD1 ILE A 148 1980 1174 4680 -19 27 -104 C ATOM 895 N ALA A 149 102.900 200.774 -0.196 1.00 33.03 N ANISOU 895 N ALA A 149 3489 2711 6351 -19 82 -264 N ATOM 896 CA ALA A 149 103.925 200.481 -1.190 1.00 32.22 C ANISOU 896 CA ALA A 149 3375 2592 6273 -29 112 -314 C ATOM 897 C ALA A 149 105.120 199.777 -0.557 1.00 31.45 C ANISOU 897 C ALA A 149 3234 2481 6234 -7 103 -342 C ATOM 898 O ALA A 149 105.670 198.831 -1.134 1.00 31.30 O ANISOU 898 O ALA A 149 3205 2439 6250 -3 116 -373 O ATOM 899 CB ALA A 149 104.354 201.767 -1.896 1.00 31.64 C ANISOU 899 CB ALA A 149 3317 2529 6175 -53 144 -337 C ATOM 900 N LEU A 150 105.527 200.202 0.639 1.00 31.23 N ANISOU 900 N LEU A 150 3185 2463 6217 10 76 -337 N ATOM 901 CA LEU A 150 106.601 199.488 1.316 1.00 32.70 C ANISOU 901 CA LEU A 150 3340 2630 6455 38 55 -364 C ATOM 902 C LEU A 150 106.200 198.053 1.624 1.00 33.85 C ANISOU 902 C LEU A 150 3505 2743 6615 62 39 -333 C ATOM 903 O LEU A 150 106.989 197.127 1.413 1.00 34.34 O ANISOU 903 O LEU A 150 3551 2776 6722 79 40 -363 O ATOM 904 CB LEU A 150 106.980 200.208 2.598 1.00 33.32 C ANISOU 904 CB LEU A 150 3405 2721 6535 57 19 -366 C ATOM 905 CG LEU A 150 107.479 201.597 2.278 1.00 34.73 C ANISOU 905 CG LEU A 150 3555 2924 6718 31 39 -405 C ATOM 906 CD1 LEU A 150 107.699 202.330 3.571 1.00 35.96 C ANISOU 906 CD1 LEU A 150 3698 3088 6875 50 -3 -411 C ATOM 907 CD2 LEU A 150 108.749 201.458 1.495 1.00 35.59 C ANISOU 907 CD2 LEU A 150 3619 3022 6882 21 70 -471 C ATOM 908 N ASP A 151 104.980 197.845 2.122 1.00 35.60 N ANISOU 908 N ASP A 151 3761 2963 6804 66 29 -274 N ATOM 909 CA ASP A 151 104.597 196.499 2.525 1.00 38.07 C ANISOU 909 CA ASP A 151 4094 3233 7137 91 22 -239 C ATOM 910 C ASP A 151 104.510 195.572 1.323 1.00 36.56 C ANISOU 910 C ASP A 151 3895 3018 6978 76 46 -263 C ATOM 911 O ASP A 151 104.851 194.388 1.422 1.00 36.00 O ANISOU 911 O ASP A 151 3826 2903 6950 100 43 -266 O ATOM 912 CB ASP A 151 103.276 196.519 3.293 1.00 42.78 C ANISOU 912 CB ASP A 151 4725 3831 7701 95 17 -173 C ATOM 913 CG ASP A 151 102.593 195.149 3.321 1.00 47.54 C ANISOU 913 CG ASP A 151 5345 4386 8333 106 29 -137 C ATOM 914 OD1 ASP A 151 101.865 194.829 2.354 1.00 49.32 O ANISOU 914 OD1 ASP A 151 5562 4608 8570 78 47 -145 O ATOM 915 OD2 ASP A 151 102.800 194.383 4.290 1.00 49.07 O ANISOU 915 OD2 ASP A 151 5566 4538 8539 146 21 -103 O ATOM 916 N ARG A 152 104.063 196.089 0.173 1.00 35.48 N ANISOU 916 N ARG A 152 3759 2904 6819 43 67 -284 N ATOM 917 CA ARG A 152 104.088 195.277 -1.040 1.00 34.43 C ANISOU 917 CA ARG A 152 3625 2746 6710 32 87 -321 C ATOM 918 C ARG A 152 105.524 195.003 -1.486 1.00 34.16 C ANISOU 918 C ARG A 152 3565 2699 6716 40 99 -381 C ATOM 919 O ARG A 152 105.846 193.891 -1.922 1.00 35.12 O ANISOU 919 O ARG A 152 3679 2783 6881 50 104 -409 O ATOM 920 CB ARG A 152 103.304 195.961 -2.166 1.00 32.93 C ANISOU 920 CB ARG A 152 3459 2577 6475 1 104 -331 C ATOM 921 CG ARG A 152 101.838 196.262 -1.876 1.00 31.86 C ANISOU 921 CG ARG A 152 3345 2454 6306 -7 90 -282 C ATOM 922 CD ARG A 152 100.958 195.022 -1.832 1.00 32.13 C ANISOU 922 CD ARG A 152 3378 2451 6381 -2 84 -264 C ATOM 923 NE ARG A 152 101.156 194.268 -0.599 1.00 32.57 N ANISOU 923 NE ARG A 152 3423 2480 6474 24 76 -227 N ATOM 924 CZ ARG A 152 101.422 192.967 -0.535 1.00 33.21 C ANISOU 924 CZ ARG A 152 3495 2509 6613 39 79 -232 C ATOM 925 NH1 ARG A 152 101.506 192.238 -1.642 1.00 33.73 N ANISOU 925 NH1 ARG A 152 3555 2548 6713 30 88 -280 N ATOM 926 NH2 ARG A 152 101.587 192.390 0.648 1.00 33.40 N ANISOU 926 NH2 ARG A 152 3528 2503 6660 68 74 -188 N ATOM 927 N TRP A 153 106.406 196.004 -1.377 1.00 32.91 N ANISOU 927 N TRP A 153 3386 2569 6550 34 106 -408 N ATOM 928 CA TRP A 153 107.765 195.837 -1.880 1.00 32.50 C ANISOU 928 CA TRP A 153 3301 2507 6542 37 125 -474 C ATOM 929 C TRP A 153 108.545 194.838 -1.046 1.00 34.45 C ANISOU 929 C TRP A 153 3525 2721 6843 78 96 -484 C ATOM 930 O TRP A 153 109.294 194.019 -1.588 1.00 34.83 O ANISOU 930 O TRP A 153 3554 2741 6937 89 106 -532 O ATOM 931 CB TRP A 153 108.499 197.176 -1.904 1.00 30.88 C ANISOU 931 CB TRP A 153 3071 2334 6327 20 145 -503 C ATOM 932 CG TRP A 153 109.858 197.078 -2.545 1.00 30.50 C ANISOU 932 CG TRP A 153 2983 2277 6330 15 177 -578 C ATOM 933 CD1 TRP A 153 110.144 197.172 -3.880 1.00 30.21 C ANISOU 933 CD1 TRP A 153 2957 2235 6289 -11 230 -621 C ATOM 934 CD2 TRP A 153 111.110 196.848 -1.886 1.00 30.70 C ANISOU 934 CD2 TRP A 153 2952 2294 6418 40 158 -624 C ATOM 935 NE1 TRP A 153 111.493 197.020 -4.089 1.00 30.56 N ANISOU 935 NE1 TRP A 153 2948 2271 6393 -8 254 -692 N ATOM 936 CE2 TRP A 153 112.111 196.823 -2.882 1.00 30.87 C ANISOU 936 CE2 TRP A 153 2941 2309 6478 24 207 -697 C ATOM 937 CE3 TRP A 153 111.484 196.666 -0.554 1.00 31.17 C ANISOU 937 CE3 TRP A 153 2993 2348 6502 78 104 -615 C ATOM 938 CZ2 TRP A 153 113.457 196.626 -2.586 1.00 26.02 C ANISOU 938 CZ2 TRP A 153 2227 1676 5983 39 206 -776 C ATOM 939 CZ3 TRP A 153 112.832 196.468 -0.264 1.00 25.58 C ANISOU 939 CZ3 TRP A 153 2213 1624 5882 100 91 -688 C ATOM 940 CH2 TRP A 153 113.793 196.449 -1.275 1.00 26.20 C ANISOU 940 CH2 TRP A 153 2222 1693 6042 77 142 -772 C ATOM 941 N TYR A 154 108.400 194.900 0.274 1.00 35.85 N ANISOU 941 N TYR A 154 3712 2896 7012 106 58 -441 N ATOM 942 CA TYR A 154 109.102 193.936 1.110 1.00 38.00 C ANISOU 942 CA TYR A 154 3985 3128 7324 157 26 -443 C ATOM 943 C TYR A 154 108.537 192.536 0.941 1.00 40.16 C ANISOU 943 C TYR A 154 4287 3350 7621 175 29 -414 C ATOM 944 O TYR A 154 109.246 191.548 1.174 1.00 42.77 O ANISOU 944 O TYR A 154 4619 3637 7996 219 16 -431 O ATOM 945 CB TYR A 154 109.065 194.386 2.570 1.00 38.21 C ANISOU 945 CB TYR A 154 4034 3162 7323 193 -13 -403 C ATOM 946 CG TYR A 154 110.119 195.425 2.849 1.00 38.44 C ANISOU 946 CG TYR A 154 4020 3222 7364 194 -28 -460 C ATOM 947 CD1 TYR A 154 109.862 196.781 2.685 1.00 38.26 C ANISOU 947 CD1 TYR A 154 3979 3244 7314 151 -14 -466 C ATOM 948 CD2 TYR A 154 111.391 195.041 3.238 1.00 40.19 C ANISOU 948 CD2 TYR A 154 4214 3425 7630 241 -55 -514 C ATOM 949 CE1 TYR A 154 110.848 197.727 2.931 1.00 39.91 C ANISOU 949 CE1 TYR A 154 4140 3476 7549 148 -24 -525 C ATOM 950 CE2 TYR A 154 112.380 195.971 3.484 1.00 41.72 C ANISOU 950 CE2 TYR A 154 4336 3639 7876 238 -71 -584 C ATOM 951 CZ TYR A 154 112.108 197.309 3.329 1.00 42.70 C ANISOU 951 CZ TYR A 154 4438 3804 7981 187 -53 -590 C ATOM 952 OH TYR A 154 113.110 198.222 3.579 1.00 45.86 O ANISOU 952 OH TYR A 154 4747 4214 8465 179 -68 -672 O ATOM 953 N ALA A 155 107.275 192.429 0.532 1.00 41.95 N ANISOU 953 N ALA A 155 4537 3579 7824 145 46 -376 N ATOM 954 CA ALA A 155 106.672 191.116 0.366 1.00 45.06 C ANISOU 954 CA ALA A 155 4951 3919 8253 156 52 -354 C ATOM 955 C ALA A 155 106.913 190.544 -1.022 1.00 47.63 C ANISOU 955 C ALA A 155 5256 4228 8614 137 75 -417 C ATOM 956 O ALA A 155 107.024 189.322 -1.169 1.00 49.99 O ANISOU 956 O ALA A 155 5558 4471 8966 158 74 -428 O ATOM 957 CB ALA A 155 105.174 191.189 0.666 1.00 25.87 C ANISOU 957 CB ALA A 155 2546 1490 5792 137 57 -289 C ATOM 958 N ILE A 156 107.002 191.388 -2.044 1.00 26.04 N ANISOU 958 N ILE A 156 2508 1536 5850 101 97 -461 N ATOM 959 CA ILE A 156 107.140 190.915 -3.415 1.00 30.15 C ANISOU 959 CA ILE A 156 3024 2041 6390 84 122 -523 C ATOM 960 C ILE A 156 108.582 190.975 -3.899 1.00 30.08 C ANISOU 960 C ILE A 156 2983 2034 6409 92 139 -596 C ATOM 961 O ILE A 156 109.027 190.088 -4.627 1.00 30.98 O ANISOU 961 O ILE A 156 3090 2116 6567 101 150 -651 O ATOM 962 CB ILE A 156 106.214 191.698 -4.369 1.00 30.08 C ANISOU 962 CB ILE A 156 3042 2065 6323 45 140 -524 C ATOM 963 CG1 ILE A 156 104.743 191.369 -4.087 1.00 30.20 C ANISOU 963 CG1 ILE A 156 3078 2068 6329 38 124 -471 C ATOM 964 CG2 ILE A 156 106.567 191.377 -5.813 1.00 30.48 C ANISOU 964 CG2 ILE A 156 3100 2101 6379 31 167 -599 C ATOM 965 CD1 ILE A 156 103.749 192.088 -5.005 1.00 29.67 C ANISOU 965 CD1 ILE A 156 3042 2028 6206 6 131 -475 C ATOM 966 N CYS A 157 109.335 192.004 -3.514 1.00 29.43 N ANISOU 966 N CYS A 157 2879 1990 6312 89 142 -605 N ATOM 967 CA CYS A 157 110.647 192.224 -4.109 1.00 29.25 C ANISOU 967 CA CYS A 157 2818 1975 6320 87 170 -682 C ATOM 968 C CYS A 157 111.802 191.839 -3.206 1.00 30.43 C ANISOU 968 C CYS A 157 2927 2108 6525 130 141 -707 C ATOM 969 O CYS A 157 112.779 191.260 -3.688 1.00 30.43 O ANISOU 969 O CYS A 157 2897 2089 6577 146 154 -776 O ATOM 970 CB CYS A 157 110.796 193.686 -4.531 1.00 28.41 C ANISOU 970 CB CYS A 157 2710 1915 6171 49 206 -693 C ATOM 971 SG CYS A 157 109.968 194.055 -6.094 1.00 27.98 S ANISOU 971 SG CYS A 157 2713 1866 6053 7 253 -704 S ATOM 972 N HIS A 158 111.715 192.123 -1.915 1.00 32.32 N ANISOU 972 N HIS A 158 3172 2353 6754 154 100 -658 N ATOM 973 CA HIS A 158 112.845 191.836 -1.039 1.00 34.98 C ANISOU 973 CA HIS A 158 3480 2675 7136 205 65 -687 C ATOM 974 C HIS A 158 113.071 190.326 -0.959 1.00 39.69 C ANISOU 974 C HIS A 158 4092 3211 7777 258 46 -693 C ATOM 975 O HIS A 158 112.107 189.552 -0.883 1.00 40.04 O ANISOU 975 O HIS A 158 4181 3220 7813 263 43 -637 O ATOM 976 CB HIS A 158 112.613 192.402 0.360 1.00 33.57 C ANISOU 976 CB HIS A 158 3322 2510 6924 231 21 -633 C ATOM 977 CG HIS A 158 113.852 192.454 1.202 1.00 33.35 C ANISOU 977 CG HIS A 158 3238 2470 6963 283 -21 -686 C ATOM 978 ND1 HIS A 158 114.274 191.394 1.977 1.00 33.78 N ANISOU 978 ND1 HIS A 158 3315 2480 7042 365 -62 -677 N ATOM 979 CD2 HIS A 158 114.771 193.434 1.374 1.00 33.15 C ANISOU 979 CD2 HIS A 158 3127 2469 6999 270 -28 -757 C ATOM 980 CE1 HIS A 158 115.390 191.723 2.602 1.00 34.52 C ANISOU 980 CE1 HIS A 158 3343 2577 7197 408 -102 -742 C ATOM 981 NE2 HIS A 158 115.713 192.957 2.255 1.00 34.15 N ANISOU 981 NE2 HIS A 158 3224 2570 7181 345 -83 -797 N ATOM 982 N PRO A 159 114.327 189.878 -0.976 1.00 43.90 N ANISOU 982 N PRO A 159 4568 3721 8389 296 36 -767 N ATOM 983 CA PRO A 159 114.592 188.429 -0.976 1.00 45.80 C ANISOU 983 CA PRO A 159 4829 3901 8671 354 21 -775 C ATOM 984 C PRO A 159 114.010 187.691 0.213 1.00 45.64 C ANISOU 984 C PRO A 159 4884 3839 8615 418 -18 -684 C ATOM 985 O PRO A 159 113.629 186.526 0.072 1.00 45.69 O ANISOU 985 O PRO A 159 4923 3787 8651 442 -15 -662 O ATOM 986 CB PRO A 159 116.131 188.370 -0.974 1.00 47.35 C ANISOU 986 CB PRO A 159 4933 4091 8967 392 7 -878 C ATOM 987 CG PRO A 159 116.562 189.683 -1.552 1.00 47.15 C ANISOU 987 CG PRO A 159 4831 4118 8966 323 44 -941 C ATOM 988 CD PRO A 159 115.559 190.682 -1.076 1.00 45.68 C ANISOU 988 CD PRO A 159 4694 3971 8692 285 42 -859 C ATOM 989 N LEU A 160 113.945 188.328 1.376 1.00 46.22 N ANISOU 989 N LEU A 160 4980 3935 8646 447 -50 -637 N ATOM 990 CA LEU A 160 113.317 187.702 2.531 1.00 48.68 C ANISOU 990 CA LEU A 160 5366 4203 8928 511 -75 -545 C ATOM 991 C LEU A 160 111.792 187.617 2.411 1.00 49.86 C ANISOU 991 C LEU A 160 5557 4339 9047 456 -49 -468 C ATOM 992 O LEU A 160 111.176 186.766 3.070 1.00 50.56 O ANISOU 992 O LEU A 160 5705 4373 9133 498 -51 -395 O ATOM 993 CB LEU A 160 113.704 188.438 3.826 1.00 48.16 C ANISOU 993 CB LEU A 160 5316 4169 8814 571 -117 -522 C ATOM 994 CG LEU A 160 114.951 187.915 4.551 1.00 48.73 C ANISOU 994 CG LEU A 160 5365 4217 8933 685 -164 -561 C ATOM 995 CD1 LEU A 160 116.222 188.083 3.723 1.00 48.53 C ANISOU 995 CD1 LEU A 160 5228 4207 9005 665 -168 -688 C ATOM 996 CD2 LEU A 160 115.096 188.588 5.911 1.00 48.87 C ANISOU 996 CD2 LEU A 160 5401 4263 8904 757 -211 -531 C ATOM 997 N MET A 161 111.172 188.464 1.592 1.00 50.69 N ANISOU 997 N MET A 161 5635 4494 9132 369 -20 -481 N ATOM 998 CA MET A 161 109.728 188.439 1.358 1.00 51.56 C ANISOU 998 CA MET A 161 5772 4601 9216 320 3 -423 C ATOM 999 C MET A 161 108.958 188.326 2.679 1.00 52.29 C ANISOU 999 C MET A 161 5926 4673 9271 357 -12 -329 C ATOM 1000 O MET A 161 108.308 187.322 2.990 1.00 52.98 O ANISOU 1000 O MET A 161 6052 4699 9378 379 -2 -275 O ATOM 1001 CB MET A 161 109.360 187.312 0.391 1.00 52.32 C ANISOU 1001 CB MET A 161 5865 4649 9366 304 27 -444 C ATOM 1002 CG MET A 161 110.038 187.432 -0.963 1.00 53.07 C ANISOU 1002 CG MET A 161 5911 4765 9486 272 48 -538 C ATOM 1003 SD MET A 161 109.404 186.255 -2.168 1.00 54.77 S ANISOU 1003 SD MET A 161 6128 4929 9753 250 72 -571 S ATOM 1004 CE MET A 161 107.814 186.986 -2.547 1.00 54.42 C ANISOU 1004 CE MET A 161 6100 4925 9653 187 88 -527 C ATOM 1005 N PHE A 162 109.067 189.405 3.454 1.00 52.28 N ANISOU 1005 N PHE A 162 5929 4718 9216 364 -31 -313 N ATOM 1006 CA PHE A 162 108.407 189.476 4.751 1.00 52.42 C ANISOU 1006 CA PHE A 162 6009 4724 9183 406 -43 -229 C ATOM 1007 C PHE A 162 106.892 189.434 4.590 1.00 52.33 C ANISOU 1007 C PHE A 162 6015 4711 9158 353 -12 -170 C ATOM 1008 O PHE A 162 106.322 190.094 3.716 1.00 51.71 O ANISOU 1008 O PHE A 162 5899 4676 9072 282 6 -195 O ATOM 1009 CB PHE A 162 108.807 190.762 5.482 1.00 51.53 C ANISOU 1009 CB PHE A 162 5892 4669 9019 419 -72 -240 C ATOM 1010 CG PHE A 162 110.285 191.047 5.472 1.00 51.25 C ANISOU 1010 CG PHE A 162 5814 4652 9008 456 -102 -319 C ATOM 1011 CD1 PHE A 162 111.075 190.736 6.570 1.00 51.64 C ANISOU 1011 CD1 PHE A 162 5895 4685 9042 564 -141 -313 C ATOM 1012 CD2 PHE A 162 110.883 191.653 4.377 1.00 50.61 C ANISOU 1012 CD2 PHE A 162 5659 4607 8963 392 -87 -401 C ATOM 1013 CE1 PHE A 162 112.434 191.011 6.570 1.00 51.77 C ANISOU 1013 CE1 PHE A 162 5855 4723 9094 602 -173 -397 C ATOM 1014 CE2 PHE A 162 112.247 191.928 4.373 1.00 50.64 C ANISOU 1014 CE2 PHE A 162 5613 4627 9001 421 -110 -481 C ATOM 1015 CZ PHE A 162 113.019 191.605 5.472 1.00 51.35 C ANISOU 1015 CZ PHE A 162 5710 4697 9105 521 -158 -486 C ATOM 1016 N LYS A 163 106.237 188.661 5.453 1.00 52.62 N ANISOU 1016 N LYS A 163 6111 4693 9189 395 -3 -92 N ATOM 1017 CA LYS A 163 104.782 188.645 5.555 1.00 52.11 C ANISOU 1017 CA LYS A 163 6062 4625 9114 354 27 -32 C ATOM 1018 C LYS A 163 104.399 189.471 6.777 1.00 50.92 C ANISOU 1018 C LYS A 163 5956 4503 8890 384 17 24 C ATOM 1019 O LYS A 163 104.565 189.016 7.913 1.00 51.32 O ANISOU 1019 O LYS A 163 6072 4513 8914 466 10 83 O ATOM 1020 CB LYS A 163 104.251 187.218 5.678 1.00 53.71 C ANISOU 1020 CB LYS A 163 6295 4740 9372 376 54 17 C ATOM 1021 CG LYS A 163 105.099 186.168 4.990 1.00 55.66 C ANISOU 1021 CG LYS A 163 6525 4934 9689 397 50 -32 C ATOM 1022 CD LYS A 163 104.816 184.787 5.579 1.00 57.61 C ANISOU 1022 CD LYS A 163 6826 5081 9983 451 71 34 C ATOM 1023 CE LYS A 163 105.871 183.766 5.172 1.00 58.94 C ANISOU 1023 CE LYS A 163 6992 5191 10213 499 58 -11 C ATOM 1024 NZ LYS A 163 105.869 182.570 6.065 1.00 59.88 N ANISOU 1024 NZ LYS A 163 7184 5210 10358 583 69 66 N ATOM 1025 N SER A 164 103.909 190.685 6.552 1.00 49.63 N ANISOU 1025 N SER A 164 5763 4407 8688 329 16 8 N ATOM 1026 CA SER A 164 103.515 191.528 7.669 1.00 49.67 C ANISOU 1026 CA SER A 164 5808 4440 8625 356 6 53 C ATOM 1027 C SER A 164 102.271 190.970 8.353 1.00 50.38 C ANISOU 1027 C SER A 164 5945 4491 8708 367 40 139 C ATOM 1028 O SER A 164 101.438 190.305 7.731 1.00 50.95 O ANISOU 1028 O SER A 164 5995 4535 8830 322 73 151 O ATOM 1029 CB SER A 164 103.249 192.953 7.202 1.00 48.73 C ANISOU 1029 CB SER A 164 5644 4395 8475 293 -1 12 C ATOM 1030 OG SER A 164 103.066 193.808 8.317 1.00 48.79 O ANISOU 1030 OG SER A 164 5690 4427 8421 327 -18 42 O ATOM 1031 N THR A 165 102.163 191.224 9.654 1.00 51.30 N ANISOU 1031 N THR A 165 6126 4602 8763 434 33 195 N ATOM 1032 CA THR A 165 100.996 190.840 10.435 1.00 51.75 C ANISOU 1032 CA THR A 165 6232 4626 8805 450 70 282 C ATOM 1033 C THR A 165 100.079 192.043 10.651 1.00 50.47 C ANISOU 1033 C THR A 165 6057 4522 8598 408 76 287 C ATOM 1034 O THR A 165 100.455 193.191 10.403 1.00 47.26 O ANISOU 1034 O THR A 165 5619 4177 8161 383 45 231 O ATOM 1035 CB THR A 165 101.414 190.244 11.781 1.00 54.13 C ANISOU 1035 CB THR A 165 6628 4880 9060 572 62 352 C ATOM 1036 OG1 THR A 165 102.081 191.240 12.564 1.00 53.98 O ANISOU 1036 OG1 THR A 165 6639 4911 8959 640 16 333 O ATOM 1037 CG2 THR A 165 102.351 189.064 11.562 1.00 55.58 C ANISOU 1037 CG2 THR A 165 6826 5003 9289 625 52 346 C ATOM 1038 N ALA A 166 98.842 191.759 11.081 1.00 51.33 N ANISOU 1038 N ALA A 166 6185 4608 8712 397 118 353 N ATOM 1039 CA ALA A 166 97.876 192.827 11.329 1.00 51.38 C ANISOU 1039 CA ALA A 166 6179 4663 8679 363 127 361 C ATOM 1040 C ALA A 166 98.269 193.700 12.513 1.00 52.43 C ANISOU 1040 C ALA A 166 6373 4824 8723 436 97 376 C ATOM 1041 O ALA A 166 97.924 194.887 12.546 1.00 54.26 O ANISOU 1041 O ALA A 166 6587 5110 8920 408 83 348 O ATOM 1042 CB ALA A 166 96.489 192.240 11.553 1.00 50.77 C ANISOU 1042 CB ALA A 166 6103 4550 8639 341 184 426 C ATOM 1043 N LYS A 167 98.969 193.139 13.502 1.00 51.36 N ANISOU 1043 N LYS A 167 6315 4652 8547 543 82 418 N ATOM 1044 CA LYS A 167 99.431 193.971 14.607 1.00 48.59 C ANISOU 1044 CA LYS A 167 6021 4335 8104 636 42 420 C ATOM 1045 C LYS A 167 100.514 194.937 14.143 1.00 45.30 C ANISOU 1045 C LYS A 167 5559 3973 7681 623 -10 324 C ATOM 1046 O LYS A 167 100.569 196.085 14.600 1.00 44.22 O ANISOU 1046 O LYS A 167 5425 3884 7494 641 -36 295 O ATOM 1047 CB LYS A 167 99.936 193.102 15.762 1.00 50.34 C ANISOU 1047 CB LYS A 167 6338 4513 8274 780 29 487 C ATOM 1048 CG LYS A 167 99.063 191.882 16.097 1.00 52.37 C ANISOU 1048 CG LYS A 167 6637 4697 8565 788 85 586 C ATOM 1049 CD LYS A 167 97.597 192.248 16.325 1.00 53.76 C ANISOU 1049 CD LYS A 167 6802 4878 8746 727 138 634 C ATOM 1050 CE LYS A 167 96.735 191.002 16.571 1.00 57.68 C ANISOU 1050 CE LYS A 167 7320 5297 9299 720 207 730 C ATOM 1051 NZ LYS A 167 96.722 190.029 15.434 1.00 59.45 N ANISOU 1051 NZ LYS A 167 7482 5473 9632 640 238 707 N ATOM 1052 N ARG A 168 101.379 194.494 13.227 1.00 43.83 N ANISOU 1052 N ARG A 168 5324 3777 7552 589 -22 272 N ATOM 1053 CA ARG A 168 102.374 195.401 12.668 1.00 42.62 C ANISOU 1053 CA ARG A 168 5112 3671 7411 559 -62 180 C ATOM 1054 C ARG A 168 101.707 196.513 11.868 1.00 40.94 C ANISOU 1054 C ARG A 168 4836 3506 7215 449 -54 140 C ATOM 1055 O ARG A 168 102.090 197.683 11.975 1.00 40.48 O ANISOU 1055 O ARG A 168 4755 3490 7135 441 -83 89 O ATOM 1056 CB ARG A 168 103.354 194.627 11.793 1.00 43.70 C ANISOU 1056 CB ARG A 168 5208 3785 7612 545 -70 135 C ATOM 1057 CG ARG A 168 104.296 195.522 11.009 1.00 44.13 C ANISOU 1057 CG ARG A 168 5186 3883 7696 493 -100 39 C ATOM 1058 CD ARG A 168 105.743 195.214 11.364 1.00 45.40 C ANISOU 1058 CD ARG A 168 5348 4037 7863 578 -140 -4 C ATOM 1059 NE ARG A 168 106.666 196.209 10.830 1.00 44.07 N ANISOU 1059 NE ARG A 168 5106 3912 7727 535 -168 -99 N ATOM 1060 CZ ARG A 168 107.960 196.238 11.118 1.00 44.31 C ANISOU 1060 CZ ARG A 168 5110 3950 7775 599 -208 -159 C ATOM 1061 NH1 ARG A 168 108.473 195.328 11.934 1.00 46.63 N ANISOU 1061 NH1 ARG A 168 5442 4214 8060 721 -230 -130 N ATOM 1062 NH2 ARG A 168 108.739 197.173 10.599 1.00 43.50 N ANISOU 1062 NH2 ARG A 168 4918 3875 7734 544 -231 -251 N ATOM 1063 N ALA A 169 100.675 196.168 11.092 1.00 40.36 N ANISOU 1063 N ALA A 169 4732 3425 7178 374 -14 162 N ATOM 1064 CA ALA A 169 99.951 197.163 10.310 1.00 38.54 C ANISOU 1064 CA ALA A 169 4447 3244 6954 291 -7 131 C ATOM 1065 C ALA A 169 99.200 198.149 11.199 1.00 37.13 C ANISOU 1065 C ALA A 169 4299 3089 6719 306 -10 155 C ATOM 1066 O ALA A 169 99.038 199.317 10.825 1.00 36.77 O ANISOU 1066 O ALA A 169 4218 3088 6664 263 -23 115 O ATOM 1067 CB ALA A 169 98.982 196.466 9.356 1.00 38.18 C ANISOU 1067 CB ALA A 169 4365 3185 6955 233 30 148 C ATOM 1068 N LEU A 170 98.714 197.698 12.362 1.00 36.28 N ANISOU 1068 N LEU A 170 4260 2951 6574 373 6 223 N ATOM 1069 CA LEU A 170 97.975 198.587 13.255 1.00 34.17 C ANISOU 1069 CA LEU A 170 4028 2706 6251 399 6 246 C ATOM 1070 C LEU A 170 98.910 199.558 13.964 1.00 33.25 C ANISOU 1070 C LEU A 170 3934 2617 6084 461 -43 200 C ATOM 1071 O LEU A 170 98.571 200.733 14.148 1.00 33.00 O ANISOU 1071 O LEU A 170 3891 2619 6027 444 -57 172 O ATOM 1072 CB LEU A 170 97.183 197.765 14.268 1.00 34.03 C ANISOU 1072 CB LEU A 170 4079 2646 6207 462 43 336 C ATOM 1073 CG LEU A 170 96.001 197.000 13.660 1.00 33.52 C ANISOU 1073 CG LEU A 170 3978 2555 6203 393 98 377 C ATOM 1074 CD1 LEU A 170 95.753 195.653 14.337 1.00 34.65 C ANISOU 1074 CD1 LEU A 170 4176 2632 6358 448 138 462 C ATOM 1075 CD2 LEU A 170 94.738 197.846 13.696 1.00 32.63 C ANISOU 1075 CD2 LEU A 170 3842 2472 6083 350 119 384 C ATOM 1076 N ASN A 171 100.095 199.091 14.368 1.00 32.42 N ANISOU 1076 N ASN A 171 3854 2499 5966 539 -73 186 N ATOM 1077 CA ASN A 171 101.050 199.983 15.014 1.00 31.21 C ANISOU 1077 CA ASN A 171 3705 2379 5775 607 -122 129 C ATOM 1078 C ASN A 171 101.538 201.064 14.062 1.00 29.67 C ANISOU 1078 C ASN A 171 3426 2216 5632 509 -144 40 C ATOM 1079 O ASN A 171 101.776 202.201 14.480 1.00 29.44 O ANISOU 1079 O ASN A 171 3386 2218 5584 523 -174 -9 O ATOM 1080 CB ASN A 171 102.223 199.183 15.551 1.00 32.04 C ANISOU 1080 CB ASN A 171 3831 2466 5876 719 -151 128 C ATOM 1081 CG ASN A 171 101.803 198.216 16.619 1.00 33.44 C ANISOU 1081 CG ASN A 171 4093 2611 6003 840 -135 224 C ATOM 1082 OD1 ASN A 171 100.764 198.409 17.262 1.00 33.94 O ANISOU 1082 OD1 ASN A 171 4199 2673 6025 861 -113 280 O ATOM 1083 ND2 ASN A 171 102.598 197.166 16.824 1.00 34.19 N ANISOU 1083 ND2 ASN A 171 4211 2678 6102 924 -147 245 N ATOM 1084 N SER A 172 101.702 200.727 12.780 1.00 28.82 N ANISOU 1084 N SER A 172 3258 2103 5588 419 -128 18 N ATOM 1085 CA SER A 172 102.069 201.739 11.795 1.00 27.48 C ANISOU 1085 CA SER A 172 3014 1967 5461 334 -139 -53 C ATOM 1086 C SER A 172 100.942 202.742 11.591 1.00 26.84 C ANISOU 1086 C SER A 172 2922 1913 5364 281 -125 -43 C ATOM 1087 O SER A 172 101.198 203.914 11.293 1.00 26.46 O ANISOU 1087 O SER A 172 2834 1892 5327 245 -141 -96 O ATOM 1088 CB SER A 172 102.427 201.080 10.469 1.00 26.97 C ANISOU 1088 CB SER A 172 2897 1896 5454 275 -119 -70 C ATOM 1089 OG SER A 172 103.252 199.944 10.655 1.00 27.36 O ANISOU 1089 OG SER A 172 2964 1911 5521 327 -126 -66 O ATOM 1090 N ILE A 173 99.691 202.294 11.720 1.00 26.87 N ANISOU 1090 N ILE A 173 2956 1907 5347 275 -92 21 N ATOM 1091 CA ILE A 173 98.559 203.202 11.576 1.00 26.74 C ANISOU 1091 CA ILE A 173 2929 1915 5314 235 -80 30 C ATOM 1092 C ILE A 173 98.490 204.154 12.758 1.00 26.38 C ANISOU 1092 C ILE A 173 2923 1878 5223 286 -104 20 C ATOM 1093 O ILE A 173 98.238 205.354 12.599 1.00 26.34 O ANISOU 1093 O ILE A 173 2894 1898 5216 255 -117 -15 O ATOM 1094 CB ILE A 173 97.257 202.396 11.419 1.00 27.42 C ANISOU 1094 CB ILE A 173 3027 1987 5404 219 -38 94 C ATOM 1095 CG1 ILE A 173 97.269 201.642 10.083 1.00 27.62 C ANISOU 1095 CG1 ILE A 173 3004 2011 5479 169 -20 85 C ATOM 1096 CG2 ILE A 173 96.041 203.311 11.537 1.00 27.13 C ANISOU 1096 CG2 ILE A 173 2988 1973 5348 198 -29 104 C ATOM 1097 CD1 ILE A 173 96.162 200.621 9.947 1.00 28.09 C ANISOU 1097 CD1 ILE A 173 3066 2045 5560 160 18 138 C ATOM 1098 N VAL A 174 98.717 203.638 13.963 1.00 26.48 N ANISOU 1098 N VAL A 174 3000 1870 5192 380 -111 50 N ATOM 1099 CA VAL A 174 98.771 204.507 15.131 1.00 26.15 C ANISOU 1099 CA VAL A 174 2999 1842 5096 457 -138 32 C ATOM 1100 C VAL A 174 99.931 205.486 15.009 1.00 26.30 C ANISOU 1100 C VAL A 174 2965 1879 5147 447 -186 -61 C ATOM 1101 O VAL A 174 99.809 206.663 15.372 1.00 27.45 O ANISOU 1101 O VAL A 174 3091 2039 5302 447 -211 -106 O ATOM 1102 CB VAL A 174 98.881 203.667 16.418 1.00 26.81 C ANISOU 1102 CB VAL A 174 3148 1902 5136 590 -139 87 C ATOM 1103 CG1 VAL A 174 99.244 204.561 17.601 1.00 27.10 C ANISOU 1103 CG1 VAL A 174 3180 1954 5162 693 -185 49 C ATOM 1104 CG2 VAL A 174 97.576 202.932 16.670 1.00 26.95 C ANISOU 1104 CG2 VAL A 174 3220 1901 5120 596 -87 178 C ATOM 1105 N ILE A 175 101.070 205.032 14.486 1.00 25.52 N ANISOU 1105 N ILE A 175 2829 1775 5093 436 -202 -98 N ATOM 1106 CA ILE A 175 102.194 205.949 14.345 1.00 22.10 C ANISOU 1106 CA ILE A 175 2320 1350 4726 418 -249 -195 C ATOM 1107 C ILE A 175 101.876 207.013 13.305 1.00 28.70 C ANISOU 1107 C ILE A 175 3118 2212 5574 314 -231 -224 C ATOM 1108 O ILE A 175 102.198 208.196 13.491 1.00 29.10 O ANISOU 1108 O ILE A 175 3124 2270 5661 301 -261 -289 O ATOM 1109 CB ILE A 175 103.479 205.176 14.002 1.00 22.55 C ANISOU 1109 CB ILE A 175 2339 1393 4838 431 -268 -231 C ATOM 1110 CG1 ILE A 175 103.848 204.226 15.141 1.00 23.56 C ANISOU 1110 CG1 ILE A 175 2508 1503 4941 563 -292 -202 C ATOM 1111 CG2 ILE A 175 104.618 206.131 13.744 1.00 22.76 C ANISOU 1111 CG2 ILE A 175 2271 1427 4950 399 -311 -341 C ATOM 1112 CD1 ILE A 175 104.944 203.250 14.790 1.00 24.06 C ANISOU 1112 CD1 ILE A 175 2546 1550 5046 587 -305 -221 C ATOM 1113 N ILE A 176 101.193 206.621 12.219 1.00 27.13 N ANISOU 1113 N ILE A 176 2903 2015 5390 246 -191 -180 N ATOM 1114 CA ILE A 176 100.899 207.551 11.128 1.00 25.06 C ANISOU 1114 CA ILE A 176 2591 1774 5157 173 -174 -199 C ATOM 1115 C ILE A 176 100.013 208.687 11.615 1.00 24.35 C ANISOU 1115 C ILE A 176 2517 1694 5038 172 -181 -199 C ATOM 1116 O ILE A 176 100.226 209.855 11.270 1.00 24.23 O ANISOU 1116 O ILE A 176 2468 1690 5048 143 -188 -242 O ATOM 1117 CB ILE A 176 100.245 206.794 9.959 1.00 23.84 C ANISOU 1117 CB ILE A 176 2428 1624 5008 131 -133 -152 C ATOM 1118 CG1 ILE A 176 101.299 205.991 9.182 1.00 24.66 C ANISOU 1118 CG1 ILE A 176 2498 1719 5151 121 -125 -174 C ATOM 1119 CG2 ILE A 176 99.494 207.751 9.050 1.00 22.43 C ANISOU 1119 CG2 ILE A 176 2230 1466 4825 87 -115 -151 C ATOM 1120 CD1 ILE A 176 100.713 205.155 8.064 1.00 25.06 C ANISOU 1120 CD1 ILE A 176 2544 1770 5207 92 -89 -139 C ATOM 1121 N TRP A 177 99.011 208.370 12.434 1.00 23.46 N ANISOU 1121 N TRP A 177 2460 1576 4879 209 -174 -149 N ATOM 1122 CA TRP A 177 98.181 209.433 12.982 1.00 22.81 C ANISOU 1122 CA TRP A 177 2396 1501 4770 216 -182 -154 C ATOM 1123 C TRP A 177 98.989 210.316 13.925 1.00 23.01 C ANISOU 1123 C TRP A 177 2422 1526 4797 262 -225 -224 C ATOM 1124 O TRP A 177 98.934 211.545 13.822 1.00 22.76 O ANISOU 1124 O TRP A 177 2363 1501 4784 236 -239 -269 O ATOM 1125 CB TRP A 177 96.945 208.835 13.663 1.00 22.23 C ANISOU 1125 CB TRP A 177 2379 1418 4649 253 -157 -86 C ATOM 1126 CG TRP A 177 95.912 208.403 12.648 1.00 21.67 C ANISOU 1126 CG TRP A 177 2287 1354 4593 196 -121 -39 C ATOM 1127 CD1 TRP A 177 95.807 207.180 12.049 1.00 21.54 C ANISOU 1127 CD1 TRP A 177 2263 1330 4593 179 -94 0 C ATOM 1128 CD2 TRP A 177 94.878 209.215 12.078 1.00 21.87 C ANISOU 1128 CD2 TRP A 177 2293 1396 4621 157 -112 -36 C ATOM 1129 NE1 TRP A 177 94.769 207.176 11.153 1.00 21.54 N ANISOU 1129 NE1 TRP A 177 2236 1342 4605 136 -72 21 N ATOM 1130 CE2 TRP A 177 94.177 208.411 11.155 1.00 21.74 C ANISOU 1130 CE2 TRP A 177 2258 1383 4620 124 -83 2 C ATOM 1131 CE3 TRP A 177 94.472 210.544 12.262 1.00 22.06 C ANISOU 1131 CE3 TRP A 177 2316 1428 4639 153 -128 -65 C ATOM 1132 CZ2 TRP A 177 93.087 208.887 10.422 1.00 21.89 C ANISOU 1132 CZ2 TRP A 177 2258 1415 4644 95 -74 11 C ATOM 1133 CZ3 TRP A 177 93.391 211.017 11.533 1.00 21.92 C ANISOU 1133 CZ3 TRP A 177 2283 1421 4625 121 -116 -50 C ATOM 1134 CH2 TRP A 177 92.712 210.190 10.622 1.00 21.80 C ANISOU 1134 CH2 TRP A 177 2251 1411 4621 95 -91 -13 C ATOM 1135 N ILE A 178 99.809 209.709 14.794 1.00 24.10 N ANISOU 1135 N ILE A 178 2572 1650 4936 335 -253 -243 N ATOM 1136 CA ILE A 178 100.584 210.492 15.757 1.00 24.76 C ANISOU 1136 CA ILE A 178 2614 1725 5070 392 -315 -332 C ATOM 1137 C ILE A 178 101.538 211.434 15.032 1.00 26.03 C ANISOU 1137 C ILE A 178 2692 1889 5308 323 -337 -418 C ATOM 1138 O ILE A 178 101.610 212.633 15.334 1.00 25.74 O ANISOU 1138 O ILE A 178 2618 1853 5308 316 -367 -486 O ATOM 1139 CB ILE A 178 101.352 209.567 16.717 1.00 25.42 C ANISOU 1139 CB ILE A 178 2707 1798 5154 502 -351 -340 C ATOM 1140 CG1 ILE A 178 100.422 208.947 17.760 1.00 25.40 C ANISOU 1140 CG1 ILE A 178 2783 1796 5072 607 -330 -258 C ATOM 1141 CG2 ILE A 178 102.484 210.335 17.395 1.00 26.23 C ANISOU 1141 CG2 ILE A 178 2738 1908 5321 551 -431 -467 C ATOM 1142 CD1 ILE A 178 101.137 207.999 18.727 1.00 26.13 C ANISOU 1142 CD1 ILE A 178 2894 1894 5139 748 -358 -243 C ATOM 1143 N VAL A 179 102.291 210.902 14.066 1.00 27.10 N ANISOU 1143 N VAL A 179 2796 2028 5474 276 -317 -417 N ATOM 1144 CA VAL A 179 103.209 211.741 13.304 1.00 28.96 C ANISOU 1144 CA VAL A 179 2952 2268 5784 218 -319 -488 C ATOM 1145 C VAL A 179 102.442 212.793 12.508 1.00 29.15 C ANISOU 1145 C VAL A 179 2994 2309 5773 160 -276 -460 C ATOM 1146 O VAL A 179 102.854 213.957 12.434 1.00 29.25 O ANISOU 1146 O VAL A 179 2958 2317 5837 139 -285 -521 O ATOM 1147 CB VAL A 179 104.090 210.870 12.389 1.00 28.94 C ANISOU 1147 CB VAL A 179 2919 2265 5813 192 -295 -484 C ATOM 1148 CG1 VAL A 179 104.975 211.750 11.512 1.00 28.93 C ANISOU 1148 CG1 VAL A 179 2840 2267 5884 138 -276 -545 C ATOM 1149 CG2 VAL A 179 104.922 209.905 13.221 1.00 29.72 C ANISOU 1149 CG2 VAL A 179 3000 2342 5948 261 -345 -519 C ATOM 1150 N SER A 180 101.300 212.417 11.926 1.00 29.96 N ANISOU 1150 N SER A 180 3133 2417 5835 138 -240 -380 N ATOM 1151 CA SER A 180 100.543 213.386 11.141 1.00 29.10 C ANISOU 1151 CA SER A 180 3019 2311 5727 97 -212 -361 C ATOM 1152 C SER A 180 99.971 214.482 12.025 1.00 29.73 C ANISOU 1152 C SER A 180 3115 2386 5795 116 -239 -388 C ATOM 1153 O SER A 180 99.961 215.656 11.640 1.00 30.17 O ANISOU 1153 O SER A 180 3149 2434 5881 90 -233 -416 O ATOM 1154 CB SER A 180 99.424 212.696 10.371 1.00 29.25 C ANISOU 1154 CB SER A 180 3070 2339 5706 79 -177 -283 C ATOM 1155 OG SER A 180 99.942 211.900 9.323 1.00 29.46 O ANISOU 1155 OG SER A 180 3077 2367 5749 57 -149 -269 O ATOM 1156 N CYS A 181 99.490 214.121 13.214 1.00 29.54 N ANISOU 1156 N CYS A 181 3137 2362 5724 169 -264 -380 N ATOM 1157 CA CYS A 181 98.970 215.139 14.117 1.00 29.53 C ANISOU 1157 CA CYS A 181 3154 2357 5707 199 -289 -415 C ATOM 1158 C CYS A 181 100.072 216.055 14.624 1.00 29.89 C ANISOU 1158 C CYS A 181 3133 2390 5834 210 -337 -524 C ATOM 1159 O CYS A 181 99.794 217.197 15.006 1.00 29.89 O ANISOU 1159 O CYS A 181 3120 2382 5856 213 -357 -571 O ATOM 1160 CB CYS A 181 98.241 214.484 15.288 1.00 29.92 C ANISOU 1160 CB CYS A 181 3258 2402 5707 272 -300 -385 C ATOM 1161 SG CYS A 181 96.692 213.688 14.819 1.00 29.54 S ANISOU 1161 SG CYS A 181 3268 2364 5593 255 -244 -273 S ATOM 1162 N ILE A 182 101.320 215.581 14.649 1.00 30.22 N ANISOU 1162 N ILE A 182 3118 2427 5939 217 -363 -576 N ATOM 1163 CA ILE A 182 102.377 216.401 15.226 1.00 31.25 C ANISOU 1163 CA ILE A 182 3160 2544 6169 232 -421 -703 C ATOM 1164 C ILE A 182 102.930 217.378 14.203 1.00 31.52 C ANISOU 1164 C ILE A 182 3144 2574 6258 164 -382 -727 C ATOM 1165 O ILE A 182 103.138 218.556 14.509 1.00 32.82 O ANISOU 1165 O ILE A 182 3264 2727 6481 159 -403 -803 O ATOM 1166 CB ILE A 182 103.480 215.513 15.815 1.00 23.60 C ANISOU 1166 CB ILE A 182 2146 1573 5247 284 -476 -767 C ATOM 1167 CG1 ILE A 182 102.953 214.804 17.064 1.00 23.91 C ANISOU 1167 CG1 ILE A 182 2250 1617 5218 389 -516 -751 C ATOM 1168 CG2 ILE A 182 104.704 216.352 16.136 1.00 24.61 C ANISOU 1168 CG2 ILE A 182 2160 1698 5493 285 -536 -915 C ATOM 1169 CD1 ILE A 182 103.896 213.774 17.642 1.00 24.60 C ANISOU 1169 CD1 ILE A 182 2323 1711 5314 469 -564 -788 C ATOM 1170 N ILE A 183 103.160 216.917 12.974 1.00 30.04 N ANISOU 1170 N ILE A 183 2973 2394 6047 118 -320 -664 N ATOM 1171 CA ILE A 183 103.716 217.796 11.954 1.00 29.20 C ANISOU 1171 CA ILE A 183 2835 2274 5986 67 -270 -679 C ATOM 1172 C ILE A 183 102.727 218.899 11.560 1.00 28.50 C ANISOU 1172 C ILE A 183 2778 2166 5885 44 -244 -646 C ATOM 1173 O ILE A 183 103.137 219.992 11.147 1.00 29.14 O ANISOU 1173 O ILE A 183 2828 2217 6026 15 -218 -684 O ATOM 1174 CB ILE A 183 104.152 216.963 10.732 1.00 28.81 C ANISOU 1174 CB ILE A 183 2778 2224 5943 36 -217 -632 C ATOM 1175 CG1 ILE A 183 102.958 216.212 10.149 1.00 28.00 C ANISOU 1175 CG1 ILE A 183 2742 2133 5761 32 -191 -530 C ATOM 1176 CG2 ILE A 183 105.250 216.008 11.141 1.00 28.86 C ANISOU 1176 CG2 ILE A 183 2738 2241 5985 60 -247 -681 C ATOM 1177 CD1 ILE A 183 103.256 215.418 8.903 1.00 27.72 C ANISOU 1177 CD1 ILE A 183 2709 2099 5725 6 -141 -489 C ATOM 1178 N MET A 184 101.419 218.658 11.689 1.00 27.40 N ANISOU 1178 N MET A 184 2701 2037 5673 56 -246 -578 N ATOM 1179 CA MET A 184 100.421 219.663 11.332 1.00 27.30 C ANISOU 1179 CA MET A 184 2720 2005 5646 40 -228 -548 C ATOM 1180 C MET A 184 100.111 220.633 12.462 1.00 28.40 C ANISOU 1180 C MET A 184 2857 2136 5798 68 -272 -608 C ATOM 1181 O MET A 184 99.243 221.500 12.294 1.00 27.98 O ANISOU 1181 O MET A 184 2831 2064 5736 60 -264 -589 O ATOM 1182 CB MET A 184 99.132 219.000 10.857 1.00 26.02 C ANISOU 1182 CB MET A 184 2616 1860 5412 40 -210 -456 C ATOM 1183 CG MET A 184 99.323 218.234 9.578 1.00 26.05 C ANISOU 1183 CG MET A 184 2626 1868 5404 12 -165 -405 C ATOM 1184 SD MET A 184 100.294 219.177 8.384 1.00 27.39 S ANISOU 1184 SD MET A 184 2776 1997 5634 -31 -115 -430 S ATOM 1185 CE MET A 184 100.813 217.860 7.275 1.00 27.50 C ANISOU 1185 CE MET A 184 2793 2026 5630 -46 -75 -392 C ATOM 1186 N ILE A 185 100.754 220.488 13.623 1.00 30.34 N ANISOU 1186 N ILE A 185 3076 2395 6056 106 -324 -684 N ATOM 1187 CA ILE A 185 100.581 221.483 14.674 1.00 31.71 C ANISOU 1187 CA ILE A 185 3230 2557 6262 138 -372 -765 C ATOM 1188 C ILE A 185 100.943 222.878 14.183 1.00 34.39 C ANISOU 1188 C ILE A 185 3537 2861 6667 99 -349 -808 C ATOM 1189 O ILE A 185 100.136 223.798 14.366 1.00 33.13 O ANISOU 1189 O ILE A 185 3401 2682 6504 102 -353 -810 O ATOM 1190 CB ILE A 185 101.377 221.073 15.932 1.00 31.16 C ANISOU 1190 CB ILE A 185 3087 2494 6259 197 -455 -877 C ATOM 1191 CG1 ILE A 185 100.726 219.874 16.609 1.00 30.35 C ANISOU 1191 CG1 ILE A 185 3043 2409 6079 254 -475 -827 C ATOM 1192 CG2 ILE A 185 101.444 222.238 16.900 1.00 31.86 C ANISOU 1192 CG2 ILE A 185 3123 2571 6410 229 -515 -998 C ATOM 1193 CD1 ILE A 185 101.528 219.373 17.780 1.00 30.90 C ANISOU 1193 CD1 ILE A 185 3067 2489 6185 332 -558 -931 C ATOM 1194 N PRO A 186 102.090 223.096 13.545 1.00 37.11 N ANISOU 1194 N PRO A 186 3825 3187 7089 63 -321 -844 N ATOM 1195 CA PRO A 186 102.412 224.467 13.105 1.00 25.49 C ANISOU 1195 CA PRO A 186 2321 1664 5700 27 -291 -886 C ATOM 1196 C PRO A 186 101.347 225.040 12.192 1.00 28.69 C ANISOU 1196 C PRO A 186 2792 2035 6073 -1 -244 -798 C ATOM 1197 O PRO A 186 101.127 226.249 12.200 1.00 26.02 O ANISOU 1197 O PRO A 186 2455 1651 5779 -13 -238 -826 O ATOM 1198 CB PRO A 186 103.769 224.297 12.386 1.00 25.96 C ANISOU 1198 CB PRO A 186 2321 1710 5834 -8 -249 -916 C ATOM 1199 CG PRO A 186 103.831 222.853 12.020 1.00 39.43 C ANISOU 1199 CG PRO A 186 4048 3454 7479 0 -241 -852 C ATOM 1200 CD PRO A 186 103.147 222.142 13.148 1.00 38.57 C ANISOU 1200 CD PRO A 186 3972 3388 7294 54 -308 -848 C ATOM 1201 N GLN A 187 100.677 224.189 11.412 1.00 27.82 N ANISOU 1201 N GLN A 187 2738 1944 5890 -8 -215 -698 N ATOM 1202 CA GLN A 187 99.600 224.662 10.558 1.00 27.17 C ANISOU 1202 CA GLN A 187 2720 1834 5769 -26 -182 -622 C ATOM 1203 C GLN A 187 98.422 225.184 11.367 1.00 27.09 C ANISOU 1203 C GLN A 187 2740 1827 5727 6 -223 -625 C ATOM 1204 O GLN A 187 97.809 226.191 10.998 1.00 27.99 O ANISOU 1204 O GLN A 187 2885 1897 5852 -6 -209 -611 O ATOM 1205 CB GLN A 187 99.125 223.543 9.628 1.00 26.01 C ANISOU 1205 CB GLN A 187 2618 1715 5551 -34 -153 -531 C ATOM 1206 CG GLN A 187 98.001 223.946 8.700 1.00 25.75 C ANISOU 1206 CG GLN A 187 2654 1659 5473 -47 -128 -459 C ATOM 1207 CD GLN A 187 98.499 224.659 7.459 1.00 26.12 C ANISOU 1207 CD GLN A 187 2727 1647 5550 -90 -72 -442 C ATOM 1208 OE1 GLN A 187 99.505 224.255 6.869 1.00 26.80 O ANISOU 1208 OE1 GLN A 187 2794 1729 5659 -114 -35 -448 O ATOM 1209 NE2 GLN A 187 97.803 225.727 7.056 1.00 26.13 N ANISOU 1209 NE2 GLN A 187 2779 1598 5552 -99 -62 -421 N ATOM 1210 N ALA A 188 98.067 224.511 12.459 1.00 26.36 N ANISOU 1210 N ALA A 188 2646 1779 5592 49 -269 -642 N ATOM 1211 CA ALA A 188 97.013 225.063 13.301 1.00 23.84 C ANISOU 1211 CA ALA A 188 2353 1459 5245 83 -303 -657 C ATOM 1212 C ALA A 188 97.476 226.332 14.006 1.00 24.80 C ANISOU 1212 C ALA A 188 2437 1547 5438 91 -332 -757 C ATOM 1213 O ALA A 188 96.665 227.221 14.278 1.00 25.12 O ANISOU 1213 O ALA A 188 2499 1564 5482 104 -343 -769 O ATOM 1214 CB ALA A 188 96.529 224.021 14.305 1.00 23.23 C ANISOU 1214 CB ALA A 188 2300 1430 5098 131 -335 -649 C ATOM 1215 N ILE A 189 98.778 226.449 14.280 1.00 31.47 N ANISOU 1215 N ILE A 189 3219 2389 6349 84 -344 -837 N ATOM 1216 CA ILE A 189 99.288 227.610 15.010 1.00 32.79 C ANISOU 1216 CA ILE A 189 3335 2529 6595 93 -376 -949 C ATOM 1217 C ILE A 189 99.079 228.896 14.213 1.00 34.12 C ANISOU 1217 C ILE A 189 3514 2625 6826 52 -334 -937 C ATOM 1218 O ILE A 189 98.780 229.955 14.782 1.00 34.82 O ANISOU 1218 O ILE A 189 3593 2682 6953 66 -359 -999 O ATOM 1219 CB ILE A 189 100.780 227.415 15.358 1.00 26.96 C ANISOU 1219 CB ILE A 189 2516 1803 5923 91 -396 -1042 C ATOM 1220 CG1 ILE A 189 100.974 226.304 16.396 1.00 26.81 C ANISOU 1220 CG1 ILE A 189 2454 1837 5897 150 -467 -1094 C ATOM 1221 CG2 ILE A 189 101.384 228.717 15.842 1.00 28.33 C ANISOU 1221 CG2 ILE A 189 2615 1937 6214 87 -419 -1166 C ATOM 1222 CD1 ILE A 189 102.421 226.110 16.831 1.00 27.71 C ANISOU 1222 CD1 ILE A 189 2451 1960 6116 163 -512 -1217 C ATOM 1223 N VAL A 190 99.218 228.822 12.886 1.00 35.59 N ANISOU 1223 N VAL A 190 3726 2779 7016 4 -270 -858 N ATOM 1224 CA VAL A 190 99.213 230.018 12.045 1.00 35.94 C ANISOU 1224 CA VAL A 190 3791 2742 7121 -37 -222 -845 C ATOM 1225 C VAL A 190 97.842 230.404 11.492 1.00 36.57 C ANISOU 1225 C VAL A 190 3954 2796 7144 -33 -210 -762 C ATOM 1226 O VAL A 190 97.688 231.523 10.976 1.00 28.57 O ANISOU 1226 O VAL A 190 2970 1708 6179 -57 -183 -756 O ATOM 1227 CB VAL A 190 100.199 229.837 10.878 1.00 28.25 C ANISOU 1227 CB VAL A 190 2811 1738 6184 -89 -153 -813 C ATOM 1228 CG1 VAL A 190 101.591 229.512 11.401 1.00 31.81 C ANISOU 1228 CG1 VAL A 190 3170 2212 6705 -92 -164 -905 C ATOM 1229 CG2 VAL A 190 99.713 228.746 9.962 1.00 27.21 C ANISOU 1229 CG2 VAL A 190 2738 1642 5958 -93 -126 -707 C ATOM 1230 N MET A 191 96.856 229.504 11.531 1.00 34.46 N ANISOU 1230 N MET A 191 3727 2583 6782 -5 -228 -697 N ATOM 1231 CA MET A 191 95.511 229.877 11.101 1.00 35.49 C ANISOU 1231 CA MET A 191 3925 2693 6864 5 -226 -632 C ATOM 1232 C MET A 191 94.946 230.929 12.037 1.00 38.03 C ANISOU 1232 C MET A 191 4240 2988 7220 35 -265 -696 C ATOM 1233 O MET A 191 94.967 230.759 13.260 1.00 37.58 O ANISOU 1233 O MET A 191 4146 2971 7161 73 -311 -765 O ATOM 1234 CB MET A 191 94.578 228.667 11.077 1.00 33.67 C ANISOU 1234 CB MET A 191 3724 2529 6539 30 -238 -565 C ATOM 1235 CG MET A 191 95.010 227.566 10.161 1.00 31.95 C ANISOU 1235 CG MET A 191 3514 2340 6284 5 -204 -505 C ATOM 1236 SD MET A 191 95.373 228.211 8.542 1.00 31.91 S ANISOU 1236 SD MET A 191 3560 2264 6300 -44 -143 -455 S ATOM 1237 CE MET A 191 93.750 228.728 8.029 1.00 32.23 C ANISOU 1237 CE MET A 191 3678 2279 6290 -27 -153 -394 C ATOM 1238 N GLU A 192 94.363 231.973 11.458 1.00 39.21 N ANISOU 1238 N GLU A 192 4437 3069 7393 25 -248 -672 N ATOM 1239 CA GLU A 192 93.842 233.086 12.237 1.00 41.63 C ANISOU 1239 CA GLU A 192 4739 3337 7743 53 -281 -735 C ATOM 1240 C GLU A 192 92.715 233.748 11.470 1.00 42.61 C ANISOU 1240 C GLU A 192 4938 3406 7847 56 -268 -670 C ATOM 1241 O GLU A 192 92.883 234.132 10.308 1.00 41.98 O ANISOU 1241 O GLU A 192 4907 3264 7779 20 -224 -613 O ATOM 1242 CB GLU A 192 94.926 234.128 12.554 1.00 44.23 C ANISOU 1242 CB GLU A 192 5017 3605 8185 29 -277 -828 C ATOM 1243 CG GLU A 192 96.015 233.681 13.527 1.00 45.93 C ANISOU 1243 CG GLU A 192 5147 3870 8433 38 -307 -923 C ATOM 1244 CD GLU A 192 95.494 233.319 14.910 1.00 47.86 C ANISOU 1244 CD GLU A 192 5371 4183 8631 100 -373 -986 C ATOM 1245 OE1 GLU A 192 94.266 233.380 15.137 1.00 48.62 O ANISOU 1245 OE1 GLU A 192 5514 4290 8672 135 -389 -954 O ATOM 1246 OE2 GLU A 192 96.327 232.962 15.771 1.00 48.96 O ANISOU 1246 OE2 GLU A 192 5450 4366 8788 118 -408 -1070 O ATOM 1247 N CYS A 193 91.579 233.887 12.140 1.00 44.83 N ANISOU 1247 N CYS A 193 5230 3707 8096 103 -306 -681 N ATOM 1248 CA CYS A 193 90.409 234.558 11.598 1.00 45.43 C ANISOU 1248 CA CYS A 193 5370 3734 8159 120 -305 -634 C ATOM 1249 C CYS A 193 90.546 236.061 11.814 1.00 46.74 C ANISOU 1249 C CYS A 193 5538 3807 8413 120 -309 -695 C ATOM 1250 O CYS A 193 90.793 236.511 12.939 1.00 46.67 O ANISOU 1250 O CYS A 193 5477 3804 8452 143 -342 -791 O ATOM 1251 CB CYS A 193 89.153 234.016 12.280 1.00 46.30 C ANISOU 1251 CB CYS A 193 5481 3907 8203 171 -340 -628 C ATOM 1252 SG CYS A 193 87.663 234.097 11.294 1.00 47.84 S ANISOU 1252 SG CYS A 193 5748 4080 8350 189 -336 -540 S ATOM 1253 N SER A 194 90.355 236.833 10.742 1.00 48.72 N ANISOU 1253 N SER A 194 5857 3969 8686 99 -277 -640 N ATOM 1254 CA SER A 194 90.569 238.276 10.750 1.00 51.37 C ANISOU 1254 CA SER A 194 6207 4195 9115 91 -269 -684 C ATOM 1255 C SER A 194 89.483 238.976 9.948 1.00 52.90 C ANISOU 1255 C SER A 194 6495 4315 9291 113 -263 -617 C ATOM 1256 O SER A 194 88.846 238.380 9.079 1.00 52.42 O ANISOU 1256 O SER A 194 6492 4275 9152 118 -253 -530 O ATOM 1257 CB SER A 194 91.923 238.648 10.150 1.00 52.09 C ANISOU 1257 CB SER A 194 6293 4221 9278 29 -217 -689 C ATOM 1258 OG SER A 194 91.869 238.556 8.737 1.00 51.97 O ANISOU 1258 OG SER A 194 6366 4159 9223 -1 -168 -585 O ATOM 1259 N THR A 195 89.298 240.264 10.236 1.00 55.13 N ANISOU 1259 N THR A 195 6791 4506 9651 127 -271 -665 N ATOM 1260 CA THR A 195 88.303 241.097 9.568 1.00 56.71 C ANISOU 1260 CA THR A 195 7081 4618 9848 156 -270 -612 C ATOM 1261 C THR A 195 88.942 241.854 8.405 1.00 59.37 C ANISOU 1261 C THR A 195 7499 4830 10228 109 -212 -556 C ATOM 1262 O THR A 195 89.894 242.612 8.609 1.00 60.06 O ANISOU 1262 O THR A 195 7561 4846 10415 71 -187 -610 O ATOM 1263 CB THR A 195 87.681 242.076 10.562 1.00 57.22 C ANISOU 1263 CB THR A 195 7120 4647 9973 205 -312 -697 C ATOM 1264 OG1 THR A 195 87.027 241.348 11.610 1.00 55.71 O ANISOU 1264 OG1 THR A 195 6867 4571 9731 251 -360 -743 O ATOM 1265 CG2 THR A 195 86.679 242.963 9.862 1.00 58.46 C ANISOU 1265 CG2 THR A 195 7372 4706 10133 241 -311 -643 C ATOM 1266 N VAL A 196 88.411 241.655 7.193 1.00 61.70 N ANISOU 1266 N VAL A 196 7895 5095 10451 114 -191 -452 N ATOM 1267 CA VAL A 196 88.880 242.342 5.991 1.00 64.98 C ANISOU 1267 CA VAL A 196 8415 5386 10888 78 -134 -383 C ATOM 1268 C VAL A 196 87.900 243.452 5.637 1.00 67.73 C ANISOU 1268 C VAL A 196 8861 5621 11251 128 -146 -352 C ATOM 1269 O VAL A 196 86.697 243.346 5.901 1.00 66.96 O ANISOU 1269 O VAL A 196 8769 5564 11109 192 -192 -349 O ATOM 1270 CB VAL A 196 89.051 241.381 4.795 1.00 64.29 C ANISOU 1270 CB VAL A 196 8391 5332 10703 54 -102 -288 C ATOM 1271 CG1 VAL A 196 89.737 242.088 3.635 1.00 65.16 C ANISOU 1271 CG1 VAL A 196 8608 5311 10839 10 -39 -224 C ATOM 1272 CG2 VAL A 196 89.828 240.135 5.209 1.00 63.16 C ANISOU 1272 CG2 VAL A 196 8148 5314 10535 20 -100 -318 C ATOM 1273 N PHE A 197 88.417 244.507 4.997 1.00 71.12 N ANISOU 1273 N PHE A 197 9372 5906 11747 98 -100 -324 N ATOM 1274 CA PHE A 197 87.631 245.680 4.604 1.00 75.71 C ANISOU 1274 CA PHE A 197 10060 6354 12354 145 -103 -290 C ATOM 1275 C PHE A 197 87.800 245.927 3.108 1.00 79.64 C ANISOU 1275 C PHE A 197 10710 6743 12805 129 -53 -173 C ATOM 1276 O PHE A 197 88.715 246.658 2.695 1.00 80.20 O ANISOU 1276 O PHE A 197 10824 6697 12952 74 1 -159 O ATOM 1277 CB PHE A 197 88.037 246.920 5.408 1.00 77.48 C ANISOU 1277 CB PHE A 197 10241 6478 12718 134 -101 -378 C ATOM 1278 CG PHE A 197 87.920 246.760 6.912 1.00 77.19 C ANISOU 1278 CG PHE A 197 10062 6540 12727 155 -155 -502 C ATOM 1279 CD1 PHE A 197 86.717 246.992 7.561 1.00 77.01 C ANISOU 1279 CD1 PHE A 197 10026 6544 12689 232 -212 -537 C ATOM 1280 CD2 PHE A 197 89.024 246.406 7.674 1.00 76.84 C ANISOU 1280 CD2 PHE A 197 9900 6557 12739 102 -148 -586 C ATOM 1281 CE1 PHE A 197 86.614 246.859 8.941 1.00 76.80 C ANISOU 1281 CE1 PHE A 197 9879 6605 12697 253 -262 -652 C ATOM 1282 CE2 PHE A 197 88.927 246.273 9.050 1.00 76.60 C ANISOU 1282 CE2 PHE A 197 9752 6612 12739 129 -202 -701 C ATOM 1283 CZ PHE A 197 87.721 246.499 9.685 1.00 76.60 C ANISOU 1283 CZ PHE A 197 9749 6639 12718 204 -258 -733 C ATOM 1284 N PRO A 198 86.940 245.337 2.249 1.00 82.67 N ANISOU 1284 N PRO A 198 11183 7159 13070 176 -68 -88 N ATOM 1285 CA PRO A 198 87.020 245.551 0.794 1.00 85.14 C ANISOU 1285 CA PRO A 198 11658 7369 13322 174 -29 26 C ATOM 1286 C PRO A 198 86.688 246.978 0.349 1.00 89.10 C ANISOU 1286 C PRO A 198 12291 7689 13875 210 -17 69 C ATOM 1287 O PRO A 198 86.514 247.869 1.181 1.00 91.08 O ANISOU 1287 O PRO A 198 12497 7885 14223 227 -31 2 O ATOM 1288 CB PRO A 198 85.980 244.571 0.237 1.00 82.48 C ANISOU 1288 CB PRO A 198 11361 7126 12853 236 -65 80 C ATOM 1289 CG PRO A 198 85.001 244.410 1.336 1.00 81.01 C ANISOU 1289 CG PRO A 198 11067 7030 12681 292 -124 7 C ATOM 1290 CD PRO A 198 85.809 244.462 2.608 1.00 81.08 C ANISOU 1290 CD PRO A 198 10931 7087 12787 238 -125 -98 C ATOM 1291 N THR A 204 81.838 249.672 2.664 1.00 82.29 N ANISOU 1291 N THR A 204 11408 6730 13128 581 -211 -75 N ATOM 1292 CA THR A 204 82.400 249.652 4.012 1.00 81.38 C ANISOU 1292 CA THR A 204 11138 6683 13102 529 -228 -198 C ATOM 1293 C THR A 204 81.931 248.446 4.825 1.00 76.86 C ANISOU 1293 C THR A 204 10425 6302 12474 536 -276 -255 C ATOM 1294 O THR A 204 82.123 248.399 6.043 1.00 75.51 O ANISOU 1294 O THR A 204 10130 6198 12361 520 -302 -360 O ATOM 1295 CB THR A 204 82.034 250.921 4.792 1.00 84.62 C ANISOU 1295 CB THR A 204 11532 6992 13626 572 -249 -273 C ATOM 1296 OG1 THR A 204 80.609 251.010 4.910 1.00 85.30 O ANISOU 1296 OG1 THR A 204 11626 7105 13677 677 -299 -271 O ATOM 1297 CG2 THR A 204 82.567 252.161 4.087 1.00 87.18 C ANISOU 1297 CG2 THR A 204 11990 7112 14023 558 -199 -223 C ATOM 1298 N THR A 205 81.289 247.493 4.149 1.00 74.30 N ANISOU 1298 N THR A 205 10128 6061 12040 565 -288 -187 N ATOM 1299 CA THR A 205 80.896 246.223 4.751 1.00 74.47 C ANISOU 1299 CA THR A 205 10032 6259 12005 562 -326 -224 C ATOM 1300 C THR A 205 82.054 245.234 4.675 1.00 72.76 C ANISOU 1300 C THR A 205 9769 6121 11757 473 -294 -219 C ATOM 1301 O THR A 205 82.692 245.100 3.626 1.00 72.72 O ANISOU 1301 O THR A 205 9851 6065 11714 435 -249 -144 O ATOM 1302 CB THR A 205 79.665 245.651 4.046 1.00 74.60 C ANISOU 1302 CB THR A 205 10089 6323 11933 633 -355 -160 C ATOM 1303 OG1 THR A 205 79.762 245.921 2.640 1.00 75.97 O ANISOU 1303 OG1 THR A 205 10413 6396 12057 649 -317 -54 O ATOM 1304 CG2 THR A 205 78.382 246.265 4.598 1.00 74.44 C ANISOU 1304 CG2 THR A 205 10044 6293 11948 724 -406 -201 C ATOM 1305 N ALA A 206 82.287 244.510 5.768 1.00 70.67 N ANISOU 1305 N ALA A 206 9371 5978 11502 446 -318 -297 N ATOM 1306 CA ALA A 206 83.536 243.797 5.988 1.00 69.15 C ANISOU 1306 CA ALA A 206 9116 5847 11311 366 -289 -318 C ATOM 1307 C ALA A 206 83.344 242.284 6.039 1.00 66.73 C ANISOU 1307 C ALA A 206 8748 5690 10917 356 -305 -302 C ATOM 1308 O ALA A 206 82.302 241.780 6.469 1.00 66.18 O ANISOU 1308 O ALA A 206 8634 5700 10810 404 -348 -316 O ATOM 1309 CB ALA A 206 84.196 244.267 7.286 1.00 68.65 C ANISOU 1309 CB ALA A 206 8952 5790 11343 344 -300 -430 C ATOM 1310 N PHE A 207 84.384 241.569 5.603 1.00 64.60 N ANISOU 1310 N PHE A 207 8472 5452 10621 292 -268 -275 N ATOM 1311 CA PHE A 207 84.506 240.123 5.696 1.00 60.99 C ANISOU 1311 CA PHE A 207 7950 5127 10095 270 -275 -267 C ATOM 1312 C PHE A 207 84.899 239.688 7.100 1.00 58.24 C ANISOU 1312 C PHE A 207 7477 4870 9781 258 -297 -357 C ATOM 1313 O PHE A 207 85.299 240.485 7.949 1.00 58.47 O ANISOU 1313 O PHE A 207 7466 4862 9888 257 -303 -431 O ATOM 1314 CB PHE A 207 85.598 239.585 4.775 1.00 60.67 C ANISOU 1314 CB PHE A 207 7946 5080 10024 208 -224 -215 C ATOM 1315 CG PHE A 207 85.325 239.741 3.324 1.00 60.79 C ANISOU 1315 CG PHE A 207 8093 5021 9983 217 -199 -122 C ATOM 1316 CD1 PHE A 207 84.567 238.807 2.651 1.00 60.01 C ANISOU 1316 CD1 PHE A 207 8022 4985 9795 244 -216 -69 C ATOM 1317 CD2 PHE A 207 85.878 240.794 2.619 1.00 62.44 C ANISOU 1317 CD2 PHE A 207 8402 5093 10229 198 -156 -87 C ATOM 1318 CE1 PHE A 207 84.334 238.933 1.305 1.00 60.86 C ANISOU 1318 CE1 PHE A 207 8258 5023 9842 260 -195 13 C ATOM 1319 CE2 PHE A 207 85.649 240.930 1.276 1.00 63.30 C ANISOU 1319 CE2 PHE A 207 8649 5128 10274 213 -133 4 C ATOM 1320 CZ PHE A 207 84.874 239.998 0.613 1.00 62.53 C ANISOU 1320 CZ PHE A 207 8582 5097 10079 248 -154 53 C ATOM 1321 N THR A 208 84.804 238.383 7.322 1.00 54.75 N ANISOU 1321 N THR A 208 6980 4545 9278 252 -309 -350 N ATOM 1322 CA THR A 208 85.653 237.684 8.276 1.00 52.28 C ANISOU 1322 CA THR A 208 6573 4313 8977 223 -310 -408 C ATOM 1323 C THR A 208 86.192 236.468 7.543 1.00 50.37 C ANISOU 1323 C THR A 208 6333 4132 8673 184 -283 -351 C ATOM 1324 O THR A 208 85.413 235.665 7.019 1.00 49.92 O ANISOU 1324 O THR A 208 6295 4122 8549 199 -293 -299 O ATOM 1325 CB THR A 208 84.898 237.295 9.556 1.00 50.78 C ANISOU 1325 CB THR A 208 6312 4206 8777 267 -354 -467 C ATOM 1326 OG1 THR A 208 83.791 236.447 9.234 1.00 50.00 O ANISOU 1326 OG1 THR A 208 6222 4167 8609 294 -370 -417 O ATOM 1327 CG2 THR A 208 84.389 238.547 10.276 1.00 51.24 C ANISOU 1327 CG2 THR A 208 6368 4202 8899 310 -380 -532 C ATOM 1328 N VAL A 209 87.512 236.360 7.453 1.00 49.24 N ANISOU 1328 N VAL A 209 6169 3981 8559 134 -249 -364 N ATOM 1329 CA VAL A 209 88.140 235.312 6.663 1.00 47.48 C ANISOU 1329 CA VAL A 209 5954 3801 8285 96 -218 -313 C ATOM 1330 C VAL A 209 89.072 234.505 7.548 1.00 45.27 C ANISOU 1330 C VAL A 209 5581 3600 8019 76 -220 -366 C ATOM 1331 O VAL A 209 89.590 234.992 8.557 1.00 46.22 O ANISOU 1331 O VAL A 209 5643 3716 8202 78 -233 -443 O ATOM 1332 CB VAL A 209 88.915 235.871 5.452 1.00 48.66 C ANISOU 1332 CB VAL A 209 6184 3856 8449 54 -165 -266 C ATOM 1333 CG1 VAL A 209 87.969 236.575 4.498 1.00 49.84 C ANISOU 1333 CG1 VAL A 209 6445 3924 8570 82 -165 -204 C ATOM 1334 CG2 VAL A 209 90.014 236.804 5.920 1.00 49.69 C ANISOU 1334 CG2 VAL A 209 6282 3921 8679 20 -141 -326 C ATOM 1335 N CYS A 210 89.283 233.259 7.150 1.00 42.31 N ANISOU 1335 N CYS A 210 5194 3295 7585 61 -209 -328 N ATOM 1336 CA CYS A 210 90.182 232.342 7.832 1.00 40.34 C ANISOU 1336 CA CYS A 210 4868 3119 7339 46 -208 -366 C ATOM 1337 C CYS A 210 91.358 232.067 6.906 1.00 40.18 C ANISOU 1337 C CYS A 210 4862 3078 7326 -3 -159 -339 C ATOM 1338 O CYS A 210 91.161 231.667 5.755 1.00 39.97 O ANISOU 1338 O CYS A 210 4896 3043 7247 -16 -135 -272 O ATOM 1339 CB CYS A 210 89.443 231.053 8.194 1.00 38.57 C ANISOU 1339 CB CYS A 210 4616 2989 7048 71 -233 -345 C ATOM 1340 SG CYS A 210 90.421 229.807 9.062 1.00 36.82 S ANISOU 1340 SG CYS A 210 4317 2852 6820 63 -236 -381 S ATOM 1341 N ASP A 211 92.573 232.301 7.395 1.00 40.82 N ANISOU 1341 N ASP A 211 4888 3148 7472 -28 -144 -398 N ATOM 1342 CA ASP A 211 93.758 232.169 6.556 1.00 41.19 C ANISOU 1342 CA ASP A 211 4942 3166 7541 -76 -90 -383 C ATOM 1343 C ASP A 211 94.982 232.038 7.452 1.00 42.22 C ANISOU 1343 C ASP A 211 4980 3322 7741 -89 -92 -464 C ATOM 1344 O ASP A 211 94.931 232.334 8.648 1.00 43.02 O ANISOU 1344 O ASP A 211 5024 3442 7879 -63 -134 -536 O ATOM 1345 CB ASP A 211 93.895 233.367 5.605 1.00 41.98 C ANISOU 1345 CB ASP A 211 5120 3151 7678 -106 -47 -353 C ATOM 1346 CG ASP A 211 94.810 233.090 4.406 1.00 41.51 C ANISOU 1346 CG ASP A 211 5102 3060 7611 -155 16 -308 C ATOM 1347 OD1 ASP A 211 95.122 231.910 4.125 1.00 40.77 O ANISOU 1347 OD1 ASP A 211 4988 3035 7467 -160 23 -289 O ATOM 1348 OD2 ASP A 211 95.214 234.070 3.738 1.00 42.12 O ANISOU 1348 OD2 ASP A 211 5234 3035 7734 -189 61 -291 O ATOM 1349 N GLU A 212 96.078 231.566 6.860 1.00 42.42 N ANISOU 1349 N GLU A 212 4988 3348 7780 -127 -48 -458 N ATOM 1350 CA GLU A 212 97.364 231.546 7.549 1.00 43.01 C ANISOU 1350 CA GLU A 212 4975 3434 7934 -142 -43 -541 C ATOM 1351 C GLU A 212 97.865 232.962 7.800 1.00 43.68 C ANISOU 1351 C GLU A 212 5040 3429 8127 -166 -28 -603 C ATOM 1352 O GLU A 212 97.713 233.848 6.955 1.00 43.15 O ANISOU 1352 O GLU A 212 5041 3273 8081 -194 14 -563 O ATOM 1353 CB GLU A 212 98.396 230.785 6.726 1.00 44.22 C ANISOU 1353 CB GLU A 212 5118 3599 8085 -178 8 -519 C ATOM 1354 CG GLU A 212 97.969 229.392 6.322 1.00 44.46 C ANISOU 1354 CG GLU A 212 5171 3705 8017 -161 -1 -457 C ATOM 1355 CD GLU A 212 98.965 228.723 5.383 1.00 45.71 C ANISOU 1355 CD GLU A 212 5329 3864 8173 -197 54 -436 C ATOM 1356 OE1 GLU A 212 100.141 229.151 5.340 1.00 46.68 O ANISOU 1356 OE1 GLU A 212 5408 3949 8379 -230 93 -485 O ATOM 1357 OE2 GLU A 212 98.562 227.770 4.679 1.00 45.33 O ANISOU 1357 OE2 GLU A 212 5323 3855 8047 -191 60 -375 O ATOM 1358 N ARG A 213 98.491 233.166 8.957 1.00 45.72 N ANISOU 1358 N ARG A 213 5209 3707 8456 -153 -62 -706 N ATOM 1359 CA ARG A 213 99.032 234.467 9.344 1.00 49.21 C ANISOU 1359 CA ARG A 213 5613 4069 9016 -174 -54 -787 C ATOM 1360 C ARG A 213 100.476 234.281 9.799 1.00 47.79 C ANISOU 1360 C ARG A 213 5329 3904 8923 -195 -46 -880 C ATOM 1361 O ARG A 213 100.730 233.826 10.919 1.00 47.29 O ANISOU 1361 O ARG A 213 5193 3910 8865 -158 -105 -959 O ATOM 1362 CB ARG A 213 98.193 235.098 10.437 1.00 54.42 C ANISOU 1362 CB ARG A 213 6260 4731 9685 -128 -119 -843 C ATOM 1363 CG ARG A 213 96.729 235.243 10.072 1.00 58.03 C ANISOU 1363 CG ARG A 213 6809 5180 10062 -100 -132 -761 C ATOM 1364 CD ARG A 213 96.466 236.438 9.149 1.00 61.94 C ANISOU 1364 CD ARG A 213 7380 5556 10598 -131 -86 -717 C ATOM 1365 NE ARG A 213 95.046 236.532 8.805 1.00 64.44 N ANISOU 1365 NE ARG A 213 7782 5867 10837 -96 -106 -644 N ATOM 1366 CZ ARG A 213 94.539 236.281 7.601 1.00 66.07 C ANISOU 1366 CZ ARG A 213 8079 6052 10971 -106 -74 -541 C ATOM 1367 NH1 ARG A 213 95.333 235.937 6.594 1.00 66.41 N ANISOU 1367 NH1 ARG A 213 8149 6075 11008 -151 -17 -494 N ATOM 1368 NH2 ARG A 213 93.232 236.386 7.401 1.00 66.48 N ANISOU 1368 NH2 ARG A 213 8196 6102 10960 -67 -101 -491 N ATOM 1369 N TRP A 214 101.422 234.636 8.930 1.00 47.16 N ANISOU 1369 N TRP A 214 5247 3758 8912 -253 28 -874 N ATOM 1370 CA TRP A 214 102.843 234.476 9.202 1.00 46.58 C ANISOU 1370 CA TRP A 214 5073 3694 8933 -278 48 -962 C ATOM 1371 C TRP A 214 103.468 235.811 9.575 1.00 49.31 C ANISOU 1371 C TRP A 214 5360 3951 9424 -309 64 -1061 C ATOM 1372 O TRP A 214 103.187 236.839 8.950 1.00 50.66 O ANISOU 1372 O TRP A 214 5592 4021 9637 -344 111 -1023 O ATOM 1373 CB TRP A 214 103.563 233.904 7.986 1.00 44.98 C ANISOU 1373 CB TRP A 214 4894 3477 8717 -324 128 -899 C ATOM 1374 CG TRP A 214 103.038 232.590 7.530 1.00 43.43 C ANISOU 1374 CG TRP A 214 4750 3361 8390 -299 117 -810 C ATOM 1375 CD1 TRP A 214 102.016 232.373 6.648 1.00 42.72 C ANISOU 1375 CD1 TRP A 214 4769 3265 8197 -295 130 -698 C ATOM 1376 CD2 TRP A 214 103.511 231.299 7.923 1.00 42.59 C ANISOU 1376 CD2 TRP A 214 4588 3348 8247 -272 87 -832 C ATOM 1377 NE1 TRP A 214 101.822 231.021 6.475 1.00 41.62 N ANISOU 1377 NE1 TRP A 214 4639 3211 7964 -271 113 -652 N ATOM 1378 CE2 TRP A 214 102.727 230.342 7.248 1.00 41.75 C ANISOU 1378 CE2 TRP A 214 4558 3285 8018 -257 88 -729 C ATOM 1379 CE3 TRP A 214 104.517 230.859 8.785 1.00 43.36 C ANISOU 1379 CE3 TRP A 214 4578 3492 8405 -256 55 -932 C ATOM 1380 CZ2 TRP A 214 102.922 228.973 7.406 1.00 41.45 C ANISOU 1380 CZ2 TRP A 214 4494 3332 7924 -231 65 -719 C ATOM 1381 CZ3 TRP A 214 104.709 229.501 8.941 1.00 42.86 C ANISOU 1381 CZ3 TRP A 214 4495 3512 8279 -227 29 -918 C ATOM 1382 CH2 TRP A 214 103.917 228.572 8.255 1.00 41.95 C ANISOU 1382 CH2 TRP A 214 4459 3433 8046 -216 36 -810 C ATOM 1383 N GLY A 215 104.318 235.787 10.597 1.00 50.71 N ANISOU 1383 N GLY A 215 5421 4165 9683 -294 22 -1190 N ATOM 1384 CA GLY A 215 105.164 236.928 10.888 1.00 53.11 C ANISOU 1384 CA GLY A 215 5646 4388 10144 -330 45 -1301 C ATOM 1385 C GLY A 215 106.459 236.854 10.100 1.00 54.94 C ANISOU 1385 C GLY A 215 5833 4580 10463 -392 132 -1314 C ATOM 1386 O GLY A 215 107.375 236.117 10.478 1.00 54.49 O ANISOU 1386 O GLY A 215 5686 4588 10431 -381 116 -1385 O ATOM 1387 N GLY A 216 106.538 237.583 8.999 1.00 56.84 N ANISOU 1387 N GLY A 216 6138 4713 10746 -456 226 -1246 N ATOM 1388 CA GLY A 216 107.689 237.568 8.119 1.00 59.03 C ANISOU 1388 CA GLY A 216 6387 4940 11101 -522 325 -1245 C ATOM 1389 C GLY A 216 107.441 236.735 6.870 1.00 58.61 C ANISOU 1389 C GLY A 216 6438 4903 10928 -538 382 -1105 C ATOM 1390 O GLY A 216 106.707 235.738 6.885 1.00 57.78 O ANISOU 1390 O GLY A 216 6382 4885 10685 -489 331 -1039 O ATOM 1391 N GLU A 217 108.092 237.136 5.777 1.00 60.16 N ANISOU 1391 N GLU A 217 6665 5011 11182 -608 490 -1064 N ATOM 1392 CA GLU A 217 107.877 236.579 4.444 1.00 59.53 C ANISOU 1392 CA GLU A 217 6696 4923 11000 -632 555 -932 C ATOM 1393 C GLU A 217 108.761 235.379 4.126 1.00 57.82 C ANISOU 1393 C GLU A 217 6428 4782 10760 -636 582 -944 C ATOM 1394 O GLU A 217 108.644 234.821 3.029 1.00 57.27 O ANISOU 1394 O GLU A 217 6444 4714 10604 -654 634 -845 O ATOM 1395 CB GLU A 217 108.081 237.674 3.391 1.00 61.91 C ANISOU 1395 CB GLU A 217 7071 5082 11369 -705 661 -874 C ATOM 1396 CG GLU A 217 107.077 238.808 3.532 1.00 63.77 C ANISOU 1396 CG GLU A 217 7385 5235 11612 -697 635 -840 C ATOM 1397 CD GLU A 217 107.246 239.886 2.481 1.00 66.80 C ANISOU 1397 CD GLU A 217 7853 5467 12060 -767 739 -772 C ATOM 1398 OE1 GLU A 217 108.377 240.392 2.314 1.00 69.20 O ANISOU 1398 OE1 GLU A 217 8087 5700 12505 -831 823 -830 O ATOM 1399 OE2 GLU A 217 106.240 240.228 1.820 1.00 67.60 O ANISOU 1399 OE2 GLU A 217 8092 5517 12073 -756 737 -660 O ATOM 1400 N ILE A 218 109.641 234.980 5.040 1.00 57.08 N ANISOU 1400 N ILE A 218 6198 4747 10741 -618 547 -1067 N ATOM 1401 CA ILE A 218 110.492 233.813 4.831 1.00 55.96 C ANISOU 1401 CA ILE A 218 6001 4677 10584 -614 564 -1088 C ATOM 1402 C ILE A 218 109.807 232.534 5.284 1.00 52.99 C ANISOU 1402 C ILE A 218 5643 4420 10069 -541 473 -1053 C ATOM 1403 O ILE A 218 109.794 231.537 4.559 1.00 52.16 O ANISOU 1403 O ILE A 218 5585 4358 9877 -537 496 -983 O ATOM 1404 CB ILE A 218 111.843 233.993 5.557 1.00 58.05 C ANISOU 1404 CB ILE A 218 6108 4943 11006 -627 570 -1244 C ATOM 1405 CG1 ILE A 218 111.601 234.218 7.059 1.00 60.55 C ANISOU 1405 CG1 ILE A 218 6343 5309 11356 -568 454 -1352 C ATOM 1406 CG2 ILE A 218 112.665 235.108 4.904 1.00 59.03 C ANISOU 1406 CG2 ILE A 218 6210 4944 11275 -712 686 -1273 C ATOM 1407 CD1 ILE A 218 112.851 234.169 7.930 1.00 62.27 C ANISOU 1407 CD1 ILE A 218 6399 5556 11706 -558 428 -1519 C ATOM 1408 N ALA A 219 109.231 232.518 6.485 1.00 51.61 N ANISOU 1408 N ALA A 219 5435 4299 9875 -482 370 -1102 N ATOM 1409 CA ALA A 219 108.737 231.250 7.020 1.00 49.05 C ANISOU 1409 CA ALA A 219 5113 4086 9437 -416 288 -1080 C ATOM 1410 C ALA A 219 107.718 230.589 6.105 1.00 47.16 C ANISOU 1410 C ALA A 219 4999 3866 9053 -409 301 -939 C ATOM 1411 O ALA A 219 107.907 229.409 5.768 1.00 46.73 O ANISOU 1411 O ALA A 219 4949 3872 8935 -394 303 -906 O ATOM 1412 CB ALA A 219 108.181 231.458 8.430 1.00 48.17 C ANISOU 1412 CB ALA A 219 4961 4019 9324 -358 181 -1148 C ATOM 1413 N PRO A 220 106.673 231.274 5.627 1.00 46.59 N ANISOU 1413 N PRO A 220 5030 3743 8930 -418 312 -857 N ATOM 1414 CA PRO A 220 105.678 230.569 4.794 1.00 45.00 C ANISOU 1414 CA PRO A 220 4939 3569 8588 -404 313 -736 C ATOM 1415 C PRO A 220 106.277 229.930 3.557 1.00 45.16 C ANISOU 1415 C PRO A 220 4995 3583 8583 -441 390 -684 C ATOM 1416 O PRO A 220 105.845 228.845 3.151 1.00 43.93 O ANISOU 1416 O PRO A 220 4881 3487 8324 -417 374 -624 O ATOM 1417 CB PRO A 220 104.682 231.682 4.418 1.00 45.38 C ANISOU 1417 CB PRO A 220 5083 3541 8618 -415 321 -676 C ATOM 1418 CG PRO A 220 105.481 232.942 4.513 1.00 47.49 C ANISOU 1418 CG PRO A 220 5305 3713 9025 -464 370 -743 C ATOM 1419 CD PRO A 220 106.399 232.726 5.688 1.00 47.72 C ANISOU 1419 CD PRO A 220 5194 3792 9145 -445 330 -872 C ATOM 1420 N LYS A 221 107.287 230.571 2.962 1.00 46.77 N ANISOU 1420 N LYS A 221 5177 3711 8882 -501 476 -711 N ATOM 1421 CA LYS A 221 107.891 230.032 1.755 1.00 46.64 C ANISOU 1421 CA LYS A 221 5196 3681 8843 -541 557 -664 C ATOM 1422 C LYS A 221 108.648 228.749 2.055 1.00 45.16 C ANISOU 1422 C LYS A 221 4926 3579 8654 -516 540 -714 C ATOM 1423 O LYS A 221 108.543 227.771 1.307 1.00 44.54 O ANISOU 1423 O LYS A 221 4895 3538 8492 -511 556 -657 O ATOM 1424 CB LYS A 221 108.818 231.076 1.134 1.00 35.73 C ANISOU 1424 CB LYS A 221 3805 2194 7578 -614 660 -686 C ATOM 1425 CG LYS A 221 108.110 232.352 0.688 1.00 36.69 C ANISOU 1425 CG LYS A 221 4023 2213 7703 -643 687 -624 C ATOM 1426 CD LYS A 221 109.037 233.196 -0.174 1.00 43.45 C ANISOU 1426 CD LYS A 221 4888 2960 8661 -723 807 -621 C ATOM 1427 CE LYS A 221 108.355 234.430 -0.732 1.00 39.60 C ANISOU 1427 CE LYS A 221 4512 2359 8176 -752 840 -544 C ATOM 1428 NZ LYS A 221 109.242 235.109 -1.713 1.00 41.41 N ANISOU 1428 NZ LYS A 221 4762 2480 8490 -833 968 -521 N ATOM 1429 N MET A 222 109.404 228.729 3.156 1.00 45.50 N ANISOU 1429 N MET A 222 4846 3652 8790 -497 502 -826 N ATOM 1430 CA MET A 222 110.113 227.517 3.554 1.00 44.57 C ANISOU 1430 CA MET A 222 4647 3612 8673 -465 473 -879 C ATOM 1431 C MET A 222 109.163 226.441 4.054 1.00 41.80 C ANISOU 1431 C MET A 222 4329 3350 8205 -399 384 -832 C ATOM 1432 O MET A 222 109.397 225.250 3.816 1.00 41.06 O ANISOU 1432 O MET A 222 4228 3309 8065 -380 379 -817 O ATOM 1433 CB MET A 222 111.133 227.850 4.632 1.00 45.87 C ANISOU 1433 CB MET A 222 4675 3783 8970 -456 445 -1017 C ATOM 1434 CG MET A 222 112.247 228.715 4.115 1.00 47.91 C ANISOU 1434 CG MET A 222 4883 3961 9361 -524 543 -1077 C ATOM 1435 SD MET A 222 113.427 229.167 5.384 1.00 48.63 S ANISOU 1435 SD MET A 222 4802 4057 9617 -513 504 -1258 S ATOM 1436 CE MET A 222 114.520 230.218 4.418 1.00 51.57 C ANISOU 1436 CE MET A 222 5144 4314 10135 -610 649 -1294 C ATOM 1437 N TYR A 223 108.091 226.838 4.744 1.00 40.76 N ANISOU 1437 N TYR A 223 4230 3229 8028 -366 316 -811 N ATOM 1438 CA TYR A 223 107.146 225.858 5.258 1.00 29.17 C ANISOU 1438 CA TYR A 223 2790 1838 6454 -309 239 -767 C ATOM 1439 C TYR A 223 106.445 225.135 4.124 1.00 32.23 C ANISOU 1439 C TYR A 223 3276 2236 6732 -315 269 -660 C ATOM 1440 O TYR A 223 106.420 223.902 4.080 1.00 27.50 O ANISOU 1440 O TYR A 223 2674 1696 6079 -288 247 -639 O ATOM 1441 CB TYR A 223 106.119 226.537 6.159 1.00 35.22 C ANISOU 1441 CB TYR A 223 3576 2606 7201 -278 173 -769 C ATOM 1442 CG TYR A 223 104.957 225.633 6.529 1.00 34.30 C ANISOU 1442 CG TYR A 223 3506 2557 6971 -229 109 -707 C ATOM 1443 CD1 TYR A 223 105.062 224.740 7.585 1.00 33.69 C ANISOU 1443 CD1 TYR A 223 3375 2548 6879 -182 40 -747 C ATOM 1444 CD2 TYR A 223 103.756 225.670 5.819 1.00 33.99 C ANISOU 1444 CD2 TYR A 223 3566 2508 6842 -230 118 -612 C ATOM 1445 CE1 TYR A 223 104.014 223.909 7.928 1.00 32.81 C ANISOU 1445 CE1 TYR A 223 3307 2489 6671 -143 -9 -690 C ATOM 1446 CE2 TYR A 223 102.700 224.835 6.154 1.00 32.94 C ANISOU 1446 CE2 TYR A 223 3465 2433 6616 -189 66 -563 C ATOM 1447 CZ TYR A 223 102.836 223.955 7.212 1.00 32.37 C ANISOU 1447 CZ TYR A 223 3338 2424 6536 -148 7 -600 C ATOM 1448 OH TYR A 223 101.796 223.118 7.568 1.00 31.28 O ANISOU 1448 OH TYR A 223 3233 2337 6314 -113 -36 -550 O ATOM 1449 N HIS A 224 105.879 225.883 3.183 1.00 33.06 N ANISOU 1449 N HIS A 224 3473 2282 6808 -349 315 -593 N ATOM 1450 CA HIS A 224 105.134 225.219 2.126 1.00 33.33 C ANISOU 1450 CA HIS A 224 3603 2327 6733 -349 331 -500 C ATOM 1451 C HIS A 224 106.036 224.417 1.202 1.00 34.18 C ANISOU 1451 C HIS A 224 3706 2439 6842 -375 392 -496 C ATOM 1452 O HIS A 224 105.557 223.480 0.555 1.00 33.54 O ANISOU 1452 O HIS A 224 3678 2391 6674 -363 388 -440 O ATOM 1453 CB HIS A 224 104.300 226.235 1.354 1.00 33.47 C ANISOU 1453 CB HIS A 224 3727 2276 6716 -374 356 -433 C ATOM 1454 CG HIS A 224 103.168 226.788 2.160 1.00 32.81 C ANISOU 1454 CG HIS A 224 3660 2198 6608 -338 290 -426 C ATOM 1455 ND1 HIS A 224 102.052 226.044 2.477 1.00 31.44 N ANISOU 1455 ND1 HIS A 224 3511 2088 6346 -292 227 -388 N ATOM 1456 CD2 HIS A 224 103.002 227.992 2.757 1.00 33.28 C ANISOU 1456 CD2 HIS A 224 3708 2209 6728 -342 278 -458 C ATOM 1457 CE1 HIS A 224 101.235 226.778 3.212 1.00 31.64 C ANISOU 1457 CE1 HIS A 224 3543 2105 6375 -269 182 -395 C ATOM 1458 NE2 HIS A 224 101.786 227.965 3.394 1.00 32.53 N ANISOU 1458 NE2 HIS A 224 3635 2149 6576 -297 209 -438 N ATOM 1459 N ILE A 225 107.328 224.744 1.125 1.00 35.26 N ANISOU 1459 N ILE A 225 3776 2542 7078 -412 450 -560 N ATOM 1460 CA ILE A 225 108.246 223.832 0.449 1.00 34.74 C ANISOU 1460 CA ILE A 225 3686 2493 7022 -428 500 -572 C ATOM 1461 C ILE A 225 108.306 222.501 1.184 1.00 33.99 C ANISOU 1461 C ILE A 225 3530 2482 6901 -374 434 -599 C ATOM 1462 O ILE A 225 108.339 221.429 0.566 1.00 33.82 O ANISOU 1462 O ILE A 225 3532 2492 6827 -367 445 -569 O ATOM 1463 CB ILE A 225 109.643 224.461 0.319 1.00 35.19 C ANISOU 1463 CB ILE A 225 3668 2497 7204 -477 577 -647 C ATOM 1464 CG1 ILE A 225 109.619 225.596 -0.703 1.00 36.28 C ANISOU 1464 CG1 ILE A 225 3886 2542 7358 -540 662 -599 C ATOM 1465 CG2 ILE A 225 110.655 223.395 -0.078 1.00 34.64 C ANISOU 1465 CG2 ILE A 225 3546 2459 7156 -481 614 -683 C ATOM 1466 CD1 ILE A 225 110.985 226.123 -1.050 1.00 37.67 C ANISOU 1466 CD1 ILE A 225 3998 2660 7657 -599 759 -662 C ATOM 1467 N CYS A 226 108.306 222.547 2.512 1.00 33.69 N ANISOU 1467 N CYS A 226 3420 2479 6901 -335 362 -656 N ATOM 1468 CA CYS A 226 108.321 221.323 3.300 1.00 33.25 C ANISOU 1468 CA CYS A 226 3315 2496 6821 -283 294 -676 C ATOM 1469 C CYS A 226 106.972 220.624 3.298 1.00 31.34 C ANISOU 1469 C CYS A 226 3147 2296 6465 -249 244 -593 C ATOM 1470 O CYS A 226 106.915 219.390 3.317 1.00 30.75 O ANISOU 1470 O CYS A 226 3067 2267 6349 -222 220 -576 O ATOM 1471 CB CYS A 226 108.784 221.646 4.714 1.00 34.73 C ANISOU 1471 CB CYS A 226 3409 2703 7085 -253 230 -767 C ATOM 1472 SG CYS A 226 110.493 222.210 4.716 1.00 37.19 S ANISOU 1472 SG CYS A 226 3610 2975 7544 -289 285 -885 S ATOM 1473 N PHE A 227 105.886 221.390 3.258 1.00 30.51 N ANISOU 1473 N PHE A 227 3107 2170 6313 -251 231 -545 N ATOM 1474 CA PHE A 227 104.568 220.782 3.119 1.00 28.79 C ANISOU 1474 CA PHE A 227 2958 1987 5993 -224 193 -470 C ATOM 1475 C PHE A 227 104.433 220.087 1.782 1.00 27.80 C ANISOU 1475 C PHE A 227 2898 1858 5808 -243 238 -414 C ATOM 1476 O PHE A 227 103.803 219.028 1.690 1.00 26.61 O ANISOU 1476 O PHE A 227 2767 1749 5593 -217 209 -377 O ATOM 1477 CB PHE A 227 103.479 221.841 3.283 1.00 29.01 C ANISOU 1477 CB PHE A 227 3041 1988 5994 -223 173 -439 C ATOM 1478 CG PHE A 227 102.080 221.289 3.375 1.00 27.89 C ANISOU 1478 CG PHE A 227 2950 1885 5762 -191 127 -378 C ATOM 1479 CD1 PHE A 227 101.503 221.032 4.610 1.00 27.12 C ANISOU 1479 CD1 PHE A 227 2819 1831 5655 -151 62 -393 C ATOM 1480 CD2 PHE A 227 101.330 221.058 2.231 1.00 27.64 C ANISOU 1480 CD2 PHE A 227 3002 1843 5659 -203 148 -312 C ATOM 1481 CE1 PHE A 227 100.216 220.531 4.702 1.00 26.36 C ANISOU 1481 CE1 PHE A 227 2763 1766 5485 -126 28 -341 C ATOM 1482 CE2 PHE A 227 100.034 220.556 2.324 1.00 26.80 C ANISOU 1482 CE2 PHE A 227 2931 1770 5481 -174 106 -266 C ATOM 1483 CZ PHE A 227 99.481 220.297 3.560 1.00 25.99 C ANISOU 1483 CZ PHE A 227 2787 1711 5378 -138 50 -280 C ATOM 1484 N PHE A 228 105.057 220.648 0.744 1.00 28.29 N ANISOU 1484 N PHE A 228 2991 1865 5894 -290 311 -411 N ATOM 1485 CA PHE A 228 104.973 220.046 -0.580 1.00 28.22 C ANISOU 1485 CA PHE A 228 3052 1845 5825 -310 355 -363 C ATOM 1486 C PHE A 228 105.727 218.729 -0.625 1.00 27.93 C ANISOU 1486 C PHE A 228 2961 1851 5801 -297 359 -392 C ATOM 1487 O PHE A 228 105.213 217.725 -1.130 1.00 27.26 O ANISOU 1487 O PHE A 228 2914 1793 5650 -282 346 -355 O ATOM 1488 CB PHE A 228 105.522 221.010 -1.631 1.00 29.74 C ANISOU 1488 CB PHE A 228 3295 1962 6044 -367 436 -352 C ATOM 1489 CG PHE A 228 105.463 220.480 -3.039 1.00 30.38 C ANISOU 1489 CG PHE A 228 3459 2025 6060 -392 482 -304 C ATOM 1490 CD1 PHE A 228 104.241 220.302 -3.676 1.00 30.28 C ANISOU 1490 CD1 PHE A 228 3545 2011 5948 -379 451 -236 C ATOM 1491 CD2 PHE A 228 106.627 220.170 -3.734 1.00 30.67 C ANISOU 1491 CD2 PHE A 228 3474 2042 6138 -427 555 -331 C ATOM 1492 CE1 PHE A 228 104.188 219.815 -4.972 1.00 30.00 C ANISOU 1492 CE1 PHE A 228 3590 1956 5853 -400 486 -198 C ATOM 1493 CE2 PHE A 228 106.571 219.691 -5.033 1.00 30.67 C ANISOU 1493 CE2 PHE A 228 3554 2023 6076 -450 596 -289 C ATOM 1494 CZ PHE A 228 105.353 219.510 -5.645 1.00 30.31 C ANISOU 1494 CZ PHE A 228 3611 1977 5930 -435 558 -223 C ATOM 1495 N LEU A 229 106.945 218.710 -0.085 1.00 28.39 N ANISOU 1495 N LEU A 229 2928 1911 5949 -301 375 -464 N ATOM 1496 CA LEU A 229 107.728 217.480 -0.095 1.00 27.77 C ANISOU 1496 CA LEU A 229 2793 1867 5891 -286 377 -497 C ATOM 1497 C LEU A 229 107.090 216.414 0.786 1.00 26.13 C ANISOU 1497 C LEU A 229 2565 1720 5645 -232 297 -484 C ATOM 1498 O LEU A 229 107.037 215.241 0.406 1.00 25.68 O ANISOU 1498 O LEU A 229 2516 1687 5554 -218 293 -466 O ATOM 1499 CB LEU A 229 109.165 217.773 0.350 1.00 28.57 C ANISOU 1499 CB LEU A 229 2795 1955 6106 -299 406 -586 C ATOM 1500 CG LEU A 229 109.873 218.894 -0.431 1.00 29.68 C ANISOU 1500 CG LEU A 229 2945 2028 6304 -359 496 -605 C ATOM 1501 CD1 LEU A 229 111.054 219.471 0.334 1.00 30.10 C ANISOU 1501 CD1 LEU A 229 2887 2066 6481 -368 508 -704 C ATOM 1502 CD2 LEU A 229 110.310 218.412 -1.806 1.00 30.33 C ANISOU 1502 CD2 LEU A 229 3074 2089 6363 -396 576 -583 C ATOM 1503 N VAL A 230 106.660 216.772 1.981 1.00 23.91 N ANISOU 1503 N VAL A 230 2260 1457 5367 -204 235 -491 N ATOM 1504 CA VAL A 230 106.106 215.755 2.920 1.00 24.54 C ANISOU 1504 CA VAL A 230 2317 1588 5420 -157 164 -483 C ATOM 1505 C VAL A 230 104.796 215.126 2.437 1.00 23.47 C ANISOU 1505 C VAL A 230 2255 1471 5193 -147 149 -407 C ATOM 1506 O VAL A 230 104.632 213.928 2.598 1.00 21.98 O ANISOU 1506 O VAL A 230 2059 1313 4980 -123 123 -390 O ATOM 1507 CB VAL A 230 105.930 216.380 4.309 1.00 24.91 C ANISOU 1507 CB VAL A 230 2323 1647 5496 -132 103 -519 C ATOM 1508 CG1 VAL A 230 105.834 215.325 5.385 1.00 22.46 C ANISOU 1508 CG1 VAL A 230 2005 1380 5149 -89 37 -502 C ATOM 1509 CG2 VAL A 230 107.062 217.339 4.612 1.00 26.16 C ANISOU 1509 CG2 VAL A 230 2398 1788 5754 -139 110 -610 C ATOM 1510 N THR A 231 103.883 215.911 1.888 1.00 23.31 N ANISOU 1510 N THR A 231 2303 1428 5126 -164 165 -363 N ATOM 1511 CA THR A 231 102.541 215.388 1.540 1.00 22.39 C ANISOU 1511 CA THR A 231 2246 1330 4930 -151 140 -303 C ATOM 1512 C THR A 231 102.673 214.676 0.199 1.00 21.97 C ANISOU 1512 C THR A 231 2254 1262 4833 -172 179 -271 C ATOM 1513 O THR A 231 102.072 213.635 0.066 1.00 21.55 O ANISOU 1513 O THR A 231 2241 1224 4722 -160 156 -232 O ATOM 1514 CB THR A 231 101.498 216.471 1.818 1.00 22.78 C ANISOU 1514 CB THR A 231 2336 1365 4953 -151 120 -277 C ATOM 1515 OG1 THR A 231 101.837 217.606 1.027 1.00 23.69 O ANISOU 1515 OG1 THR A 231 2505 1427 5068 -187 167 -268 O ATOM 1516 CG2 THR A 231 101.477 216.888 3.267 1.00 22.73 C ANISOU 1516 CG2 THR A 231 2275 1370 4991 -131 80 -315 C ATOM 1517 N TYR A 232 103.392 215.240 -0.762 1.00 22.55 N ANISOU 1517 N TYR A 232 2335 1300 4932 -205 238 -292 N ATOM 1518 CA TYR A 232 103.245 214.874 -2.189 1.00 22.98 C ANISOU 1518 CA TYR A 232 2467 1329 4935 -231 276 -262 C ATOM 1519 C TYR A 232 104.568 214.463 -2.825 1.00 23.46 C ANISOU 1519 C TYR A 232 2505 1372 5036 -255 335 -299 C ATOM 1520 O TYR A 232 104.745 213.307 -3.167 1.00 23.34 O ANISOU 1520 O TYR A 232 2484 1376 5009 -245 335 -303 O ATOM 1521 CB TYR A 232 102.759 216.102 -2.950 1.00 24.09 C ANISOU 1521 CB TYR A 232 2693 1420 5040 -258 296 -226 C ATOM 1522 CG TYR A 232 102.126 215.836 -4.286 1.00 24.85 C ANISOU 1522 CG TYR A 232 2889 1489 5064 -276 313 -185 C ATOM 1523 CD1 TYR A 232 100.832 215.382 -4.378 1.00 24.83 C ANISOU 1523 CD1 TYR A 232 2932 1505 4997 -252 264 -151 C ATOM 1524 CD2 TYR A 232 102.814 216.068 -5.455 1.00 25.55 C ANISOU 1524 CD2 TYR A 232 3026 1530 5153 -317 378 -186 C ATOM 1525 CE1 TYR A 232 100.243 215.147 -5.601 1.00 25.64 C ANISOU 1525 CE1 TYR A 232 3129 1578 5036 -266 270 -122 C ATOM 1526 CE2 TYR A 232 102.240 215.840 -6.687 1.00 26.33 C ANISOU 1526 CE2 TYR A 232 3224 1598 5181 -332 388 -150 C ATOM 1527 CZ TYR A 232 100.947 215.384 -6.758 1.00 26.76 C ANISOU 1527 CZ TYR A 232 3326 1670 5170 -304 329 -120 C ATOM 1528 OH TYR A 232 100.370 215.174 -7.967 1.00 28.23 O ANISOU 1528 OH TYR A 232 3616 1821 5288 -315 329 -92 O ATOM 1529 N ALA A 233 105.479 215.401 -3.010 1.00 24.61 N ANISOU 1529 N ALA A 233 2634 1480 5238 -288 388 -328 N ATOM 1530 CA ALA A 233 106.662 215.021 -3.805 1.00 25.61 C ANISOU 1530 CA ALA A 233 2736 1586 5409 -318 456 -367 C ATOM 1531 C ALA A 233 107.450 213.872 -3.186 1.00 25.38 C ANISOU 1531 C ALA A 233 2626 1601 5416 -286 433 -409 C ATOM 1532 O ALA A 233 107.689 212.929 -3.904 1.00 25.21 O ANISOU 1532 O ALA A 233 2628 1587 5363 -282 440 -402 O ATOM 1533 CB ALA A 233 107.532 216.226 -4.032 1.00 26.68 C ANISOU 1533 CB ALA A 233 2830 1681 5625 -353 511 -407 C ATOM 1534 N ALA A 234 107.768 213.899 -1.899 1.00 25.75 N ANISOU 1534 N ALA A 234 2581 1670 5531 -262 400 -456 N ATOM 1535 CA ALA A 234 108.605 212.797 -1.375 1.00 26.01 C ANISOU 1535 CA ALA A 234 2536 1734 5611 -233 379 -501 C ATOM 1536 C ALA A 234 107.867 211.459 -1.411 1.00 25.96 C ANISOU 1536 C ALA A 234 2555 1761 5548 -200 331 -462 C ATOM 1537 O ALA A 234 108.437 210.508 -1.931 1.00 25.86 O ANISOU 1537 O ALA A 234 2532 1749 5543 -199 351 -479 O ATOM 1538 CB ALA A 234 109.077 213.131 0.011 1.00 25.70 C ANISOU 1538 CB ALA A 234 2408 1712 5645 -208 334 -554 C ATOM 1539 N PRO A 235 106.620 211.352 -0.910 1.00 25.84 N ANISOU 1539 N PRO A 235 2572 1768 5479 -176 274 -414 N ATOM 1540 CA PRO A 235 105.864 210.092 -0.979 1.00 25.41 C ANISOU 1540 CA PRO A 235 2537 1736 5380 -151 240 -381 C ATOM 1541 C PRO A 235 105.601 209.634 -2.392 1.00 26.42 C ANISOU 1541 C PRO A 235 2731 1846 5463 -173 278 -362 C ATOM 1542 O PRO A 235 105.634 208.427 -2.664 1.00 26.60 O ANISOU 1542 O PRO A 235 2745 1876 5484 -160 271 -367 O ATOM 1543 CB PRO A 235 104.557 210.427 -0.251 1.00 24.80 C ANISOU 1543 CB PRO A 235 2488 1679 5257 -132 188 -335 C ATOM 1544 CG PRO A 235 104.924 211.512 0.687 1.00 24.91 C ANISOU 1544 CG PRO A 235 2465 1691 5311 -131 175 -361 C ATOM 1545 CD PRO A 235 105.961 212.332 -0.034 1.00 25.62 C ANISOU 1545 CD PRO A 235 2547 1745 5442 -167 238 -399 C ATOM 1546 N LEU A 236 105.346 210.556 -3.316 1.00 27.75 N ANISOU 1546 N LEU A 236 2968 1983 5593 -206 317 -343 N ATOM 1547 CA LEU A 236 105.019 210.113 -4.668 1.00 29.09 C ANISOU 1547 CA LEU A 236 3213 2130 5711 -226 344 -326 C ATOM 1548 C LEU A 236 106.258 209.601 -5.399 1.00 31.56 C ANISOU 1548 C LEU A 236 3504 2424 6062 -246 402 -373 C ATOM 1549 O LEU A 236 106.169 208.655 -6.189 1.00 32.22 O ANISOU 1549 O LEU A 236 3617 2503 6123 -247 409 -377 O ATOM 1550 CB LEU A 236 104.344 211.225 -5.462 1.00 29.15 C ANISOU 1550 CB LEU A 236 3315 2102 5659 -256 362 -287 C ATOM 1551 CG LEU A 236 103.414 210.712 -6.571 1.00 29.07 C ANISOU 1551 CG LEU A 236 3396 2076 5574 -260 350 -257 C ATOM 1552 CD1 LEU A 236 102.084 210.229 -6.005 1.00 28.45 C ANISOU 1552 CD1 LEU A 236 3316 2030 5464 -226 281 -229 C ATOM 1553 CD2 LEU A 236 103.188 211.789 -7.622 1.00 29.92 C ANISOU 1553 CD2 LEU A 236 3607 2129 5630 -298 383 -226 C ATOM 1554 N CYS A 237 107.430 210.183 -5.137 1.00 33.44 N ANISOU 1554 N CYS A 237 3686 2651 6368 -264 445 -415 N ATOM 1555 CA CYS A 237 108.646 209.618 -5.714 1.00 35.49 C ANISOU 1555 CA CYS A 237 3907 2897 6678 -280 502 -468 C ATOM 1556 C CYS A 237 108.914 208.231 -5.159 1.00 35.18 C ANISOU 1556 C CYS A 237 3802 2890 6674 -240 460 -497 C ATOM 1557 O CYS A 237 109.244 207.303 -5.908 1.00 33.74 O ANISOU 1557 O CYS A 237 3626 2700 6493 -242 483 -519 O ATOM 1558 CB CYS A 237 109.838 210.529 -5.447 1.00 37.69 C ANISOU 1558 CB CYS A 237 4126 3159 7038 -306 555 -516 C ATOM 1559 SG CYS A 237 109.794 211.999 -6.464 1.00 40.34 S ANISOU 1559 SG CYS A 237 4548 3437 7344 -369 632 -485 S ATOM 1560 N LEU A 238 108.744 208.064 -3.849 1.00 36.93 N ANISOU 1560 N LEU A 238 3965 3142 6923 -202 397 -495 N ATOM 1561 CA LEU A 238 109.033 206.777 -3.236 1.00 36.27 C ANISOU 1561 CA LEU A 238 3824 3080 6876 -166 355 -516 C ATOM 1562 C LEU A 238 108.125 205.700 -3.804 1.00 35.71 C ANISOU 1562 C LEU A 238 3806 3010 6751 -154 334 -481 C ATOM 1563 O LEU A 238 108.570 204.579 -4.088 1.00 35.92 O ANISOU 1563 O LEU A 238 3811 3033 6806 -143 337 -508 O ATOM 1564 CB LEU A 238 108.870 206.880 -1.718 1.00 35.53 C ANISOU 1564 CB LEU A 238 3681 3013 6807 -132 287 -509 C ATOM 1565 CG LEU A 238 108.968 205.592 -0.900 1.00 35.37 C ANISOU 1565 CG LEU A 238 3620 3006 6812 -93 231 -513 C ATOM 1566 CD1 LEU A 238 110.295 204.888 -1.158 1.00 35.31 C ANISOU 1566 CD1 LEU A 238 3552 2987 6875 -90 253 -579 C ATOM 1567 CD2 LEU A 238 108.792 205.896 0.579 1.00 34.67 C ANISOU 1567 CD2 LEU A 238 3502 2936 6735 -66 168 -505 C ATOM 1568 N MET A 239 106.859 206.037 -4.032 1.00 33.73 N ANISOU 1568 N MET A 239 3624 2762 6430 -158 314 -427 N ATOM 1569 CA MET A 239 105.947 205.050 -4.587 1.00 31.55 C ANISOU 1569 CA MET A 239 3392 2485 6112 -149 293 -404 C ATOM 1570 C MET A 239 106.275 204.742 -6.040 1.00 30.62 C ANISOU 1570 C MET A 239 3324 2337 5975 -176 342 -430 C ATOM 1571 O MET A 239 106.181 203.587 -6.464 1.00 30.64 O ANISOU 1571 O MET A 239 3328 2332 5981 -165 333 -445 O ATOM 1572 CB MET A 239 104.510 205.528 -4.424 1.00 30.82 C ANISOU 1572 CB MET A 239 3351 2402 5958 -146 256 -349 C ATOM 1573 CG MET A 239 104.022 205.398 -2.994 1.00 30.75 C ANISOU 1573 CG MET A 239 3295 2422 5965 -115 203 -324 C ATOM 1574 SD MET A 239 102.319 205.916 -2.757 1.00 31.52 S ANISOU 1574 SD MET A 239 3442 2533 6002 -111 165 -268 S ATOM 1575 CE MET A 239 102.512 207.681 -2.549 1.00 32.15 C ANISOU 1575 CE MET A 239 3538 2609 6069 -129 181 -265 C ATOM 1576 N VAL A 240 106.697 205.740 -6.815 1.00 29.94 N ANISOU 1576 N VAL A 240 3280 2225 5870 -212 397 -437 N ATOM 1577 CA VAL A 240 107.035 205.451 -8.207 1.00 29.87 C ANISOU 1577 CA VAL A 240 3329 2184 5838 -240 447 -462 C ATOM 1578 C VAL A 240 108.209 204.482 -8.281 1.00 29.46 C ANISOU 1578 C VAL A 240 3209 2131 5855 -233 475 -525 C ATOM 1579 O VAL A 240 108.203 203.538 -9.081 1.00 28.95 O ANISOU 1579 O VAL A 240 3169 2052 5780 -231 481 -550 O ATOM 1580 CB VAL A 240 107.324 206.747 -8.986 1.00 30.14 C ANISOU 1580 CB VAL A 240 3426 2184 5844 -287 508 -451 C ATOM 1581 CG1 VAL A 240 107.739 206.413 -10.416 1.00 29.98 C ANISOU 1581 CG1 VAL A 240 3469 2124 5798 -317 563 -478 C ATOM 1582 CG2 VAL A 240 106.097 207.630 -8.993 1.00 29.89 C ANISOU 1582 CG2 VAL A 240 3470 2146 5743 -291 472 -390 C ATOM 1583 N LEU A 241 109.223 204.678 -7.433 1.00 30.22 N ANISOU 1583 N LEU A 241 3216 2242 6026 -225 486 -557 N ATOM 1584 CA LEU A 241 110.372 203.778 -7.468 1.00 30.69 C ANISOU 1584 CA LEU A 241 3205 2300 6158 -215 508 -621 C ATOM 1585 C LEU A 241 109.991 202.375 -7.023 1.00 30.56 C ANISOU 1585 C LEU A 241 3162 2294 6154 -173 447 -620 C ATOM 1586 O LEU A 241 110.536 201.387 -7.532 1.00 24.56 O ANISOU 1586 O LEU A 241 2384 1521 5426 -166 462 -666 O ATOM 1587 CB LEU A 241 111.497 204.322 -6.591 1.00 30.80 C ANISOU 1587 CB LEU A 241 3119 2321 6262 -214 524 -664 C ATOM 1588 CG LEU A 241 112.311 205.488 -7.146 1.00 31.63 C ANISOU 1588 CG LEU A 241 3200 2395 6424 -261 620 -701 C ATOM 1589 CD1 LEU A 241 113.406 205.870 -6.160 1.00 31.92 C ANISOU 1589 CD1 LEU A 241 3110 2437 6580 -252 627 -763 C ATOM 1590 CD2 LEU A 241 112.893 205.143 -8.511 1.00 26.42 C ANISOU 1590 CD2 LEU A 241 2538 1691 5808 -295 720 -754 C ATOM 1591 N LEU A 242 109.054 202.270 -6.079 1.00 30.19 N ANISOU 1591 N LEU A 242 3114 2268 6088 -146 381 -568 N ATOM 1592 CA LEU A 242 108.686 200.973 -5.524 1.00 30.32 C ANISOU 1592 CA LEU A 242 3107 2289 6125 -111 328 -559 C ATOM 1593 C LEU A 242 107.796 200.196 -6.488 1.00 29.93 C ANISOU 1593 C LEU A 242 3119 2222 6032 -114 324 -550 C ATOM 1594 O LEU A 242 108.070 199.031 -6.792 1.00 30.13 O ANISOU 1594 O LEU A 242 3129 2229 6090 -100 320 -583 O ATOM 1595 CB LEU A 242 108.012 201.165 -4.160 1.00 29.96 C ANISOU 1595 CB LEU A 242 3042 2266 6074 -86 269 -509 C ATOM 1596 CG LEU A 242 108.911 201.627 -3.007 1.00 23.09 C ANISOU 1596 CG LEU A 242 2105 1411 5259 -72 251 -528 C ATOM 1597 CD1 LEU A 242 108.172 201.487 -1.683 1.00 23.88 C ANISOU 1597 CD1 LEU A 242 2200 1525 5346 -44 188 -480 C ATOM 1598 CD2 LEU A 242 110.229 200.854 -2.976 1.00 23.63 C ANISOU 1598 CD2 LEU A 242 2110 1465 5402 -59 259 -592 C ATOM 1599 N TYR A 243 106.753 200.833 -7.020 1.00 29.80 N ANISOU 1599 N TYR A 243 3174 2204 5944 -132 322 -513 N ATOM 1600 CA TYR A 243 105.888 200.118 -7.948 1.00 30.70 C ANISOU 1600 CA TYR A 243 3347 2298 6020 -135 310 -515 C ATOM 1601 C TYR A 243 106.577 199.839 -9.281 1.00 32.54 C ANISOU 1601 C TYR A 243 3616 2501 6247 -155 359 -573 C ATOM 1602 O TYR A 243 106.190 198.890 -9.970 1.00 33.62 O ANISOU 1602 O TYR A 243 3780 2617 6378 -149 347 -599 O ATOM 1603 CB TYR A 243 104.560 200.869 -8.148 1.00 30.02 C ANISOU 1603 CB TYR A 243 3328 2216 5862 -147 286 -465 C ATOM 1604 CG TYR A 243 103.649 200.772 -6.936 1.00 29.13 C ANISOU 1604 CG TYR A 243 3180 2130 5758 -123 234 -416 C ATOM 1605 CD1 TYR A 243 102.976 199.592 -6.631 1.00 29.05 C ANISOU 1605 CD1 TYR A 243 3147 2114 5775 -103 199 -410 C ATOM 1606 CD2 TYR A 243 103.492 201.852 -6.076 1.00 28.71 C ANISOU 1606 CD2 TYR A 243 3116 2101 5692 -123 225 -379 C ATOM 1607 CE1 TYR A 243 102.164 199.494 -5.490 1.00 28.58 C ANISOU 1607 CE1 TYR A 243 3058 2074 5727 -85 161 -363 C ATOM 1608 CE2 TYR A 243 102.687 201.765 -4.941 1.00 28.24 C ANISOU 1608 CE2 TYR A 243 3027 2064 5639 -102 182 -338 C ATOM 1609 CZ TYR A 243 102.029 200.586 -4.652 1.00 28.17 C ANISOU 1609 CZ TYR A 243 3000 2050 5654 -84 153 -328 C ATOM 1610 OH TYR A 243 101.233 200.501 -3.529 1.00 27.70 O ANISOU 1610 OH TYR A 243 2917 2007 5602 -68 120 -286 O ATOM 1611 N LEU A 244 107.599 200.615 -9.662 1.00 32.74 N ANISOU 1611 N LEU A 244 3642 2520 6279 -180 418 -599 N ATOM 1612 CA LEU A 244 108.320 200.274 -10.889 1.00 33.59 C ANISOU 1612 CA LEU A 244 3770 2593 6398 -199 477 -663 C ATOM 1613 C LEU A 244 109.092 198.965 -10.745 1.00 34.83 C ANISOU 1613 C LEU A 244 3846 2743 6643 -173 478 -725 C ATOM 1614 O LEU A 244 109.172 198.179 -11.697 1.00 35.34 O ANISOU 1614 O LEU A 244 3921 2776 6732 -172 501 -783 O ATOM 1615 CB LEU A 244 109.255 201.409 -11.302 1.00 33.72 C ANISOU 1615 CB LEU A 244 3767 2588 6458 -239 568 -688 C ATOM 1616 CG LEU A 244 108.599 202.377 -12.290 1.00 33.80 C ANISOU 1616 CG LEU A 244 3881 2563 6398 -275 602 -659 C ATOM 1617 CD1 LEU A 244 109.495 203.580 -12.564 1.00 33.88 C ANISOU 1617 CD1 LEU A 244 3874 2546 6454 -320 703 -670 C ATOM 1618 CD2 LEU A 244 108.244 201.651 -13.582 1.00 33.22 C ANISOU 1618 CD2 LEU A 244 3864 2445 6314 -278 622 -706 C ATOM 1619 N GLN A 245 109.666 198.706 -9.567 1.00 35.65 N ANISOU 1619 N GLN A 245 3872 2873 6801 -148 450 -720 N ATOM 1620 CA GLN A 245 110.297 197.409 -9.352 1.00 37.41 C ANISOU 1620 CA GLN A 245 4026 3083 7105 -117 437 -769 C ATOM 1621 C GLN A 245 109.255 196.305 -9.241 1.00 39.68 C ANISOU 1621 C GLN A 245 4349 3364 7364 -92 375 -741 C ATOM 1622 O GLN A 245 109.481 195.184 -9.712 1.00 41.28 O ANISOU 1622 O GLN A 245 4544 3542 7600 -76 373 -788 O ATOM 1623 CB GLN A 245 111.183 197.444 -8.107 1.00 36.47 C ANISOU 1623 CB GLN A 245 3814 2980 7061 -96 419 -775 C ATOM 1624 CG GLN A 245 112.307 198.470 -8.184 1.00 36.66 C ANISOU 1624 CG GLN A 245 3769 3003 7158 -124 489 -825 C ATOM 1625 CD GLN A 245 113.362 198.282 -7.101 1.00 37.17 C ANISOU 1625 CD GLN A 245 3720 3073 7329 -100 468 -864 C ATOM 1626 OE1 GLN A 245 113.417 197.238 -6.440 1.00 37.00 O ANISOU 1626 OE1 GLN A 245 3675 3048 7336 -61 408 -862 O ATOM 1627 NE2 GLN A 245 114.208 199.295 -6.918 1.00 37.72 N ANISOU 1627 NE2 GLN A 245 3720 3146 7465 -123 517 -903 N ATOM 1628 N ILE A 246 108.099 196.605 -8.639 1.00 40.22 N ANISOU 1628 N ILE A 246 4439 3446 7395 -89 332 -673 N ATOM 1629 CA ILE A 246 107.063 195.586 -8.481 1.00 25.02 C ANISOU 1629 CA ILE A 246 2523 1506 5475 -70 285 -651 C ATOM 1630 C ILE A 246 106.460 195.234 -9.829 1.00 39.37 C ANISOU 1630 C ILE A 246 4408 3299 7253 -85 293 -686 C ATOM 1631 O ILE A 246 106.222 194.059 -10.133 1.00 39.84 O ANISOU 1631 O ILE A 246 4461 3331 7347 -70 275 -718 O ATOM 1632 CB ILE A 246 105.979 196.049 -7.488 1.00 24.41 C ANISOU 1632 CB ILE A 246 2449 1453 5373 -66 244 -575 C ATOM 1633 CG1 ILE A 246 106.537 196.095 -6.063 1.00 24.23 C ANISOU 1633 CG1 ILE A 246 2366 1446 5395 -43 224 -547 C ATOM 1634 CG2 ILE A 246 104.782 195.127 -7.546 1.00 24.54 C ANISOU 1634 CG2 ILE A 246 2481 1450 5395 -58 208 -557 C ATOM 1635 CD1 ILE A 246 105.655 196.842 -5.071 1.00 23.64 C ANISOU 1635 CD1 ILE A 246 2296 1398 5286 -41 194 -480 C ATOM 1636 N PHE A 247 106.212 196.242 -10.664 1.00 38.70 N ANISOU 1636 N PHE A 247 4393 3217 7095 -113 319 -685 N ATOM 1637 CA PHE A 247 105.656 195.982 -11.984 1.00 38.49 C ANISOU 1637 CA PHE A 247 4444 3162 7019 -125 320 -724 C ATOM 1638 C PHE A 247 106.609 195.144 -12.823 1.00 39.47 C ANISOU 1638 C PHE A 247 4552 3256 7187 -119 357 -812 C ATOM 1639 O PHE A 247 106.220 194.113 -13.382 1.00 40.04 O ANISOU 1639 O PHE A 247 4633 3302 7278 -105 336 -859 O ATOM 1640 CB PHE A 247 105.343 197.304 -12.680 1.00 37.65 C ANISOU 1640 CB PHE A 247 4426 3054 6825 -156 342 -702 C ATOM 1641 CG PHE A 247 105.069 197.156 -14.140 1.00 37.69 C ANISOU 1641 CG PHE A 247 4495 3012 6813 -167 363 -765 C ATOM 1642 CD1 PHE A 247 103.797 196.845 -14.588 1.00 37.02 C ANISOU 1642 CD1 PHE A 247 4470 2913 6682 -161 308 -763 C ATOM 1643 CD2 PHE A 247 106.083 197.316 -15.071 1.00 38.06 C ANISOU 1643 CD2 PHE A 247 4533 3022 6907 -183 445 -841 C ATOM 1644 CE1 PHE A 247 103.539 196.696 -15.929 1.00 37.46 C ANISOU 1644 CE1 PHE A 247 4580 2919 6735 -165 322 -839 C ATOM 1645 CE2 PHE A 247 105.828 197.169 -16.418 1.00 38.42 C ANISOU 1645 CE2 PHE A 247 4639 3018 6942 -189 472 -915 C ATOM 1646 CZ PHE A 247 104.556 196.857 -16.845 1.00 38.27 C ANISOU 1646 CZ PHE A 247 4682 2985 6873 -176 404 -916 C ATOM 1647 N ARG A 248 107.875 195.549 -12.893 1.00 40.31 N ANISOU 1647 N ARG A 248 4606 3360 7351 -129 422 -852 N ATOM 1648 CA ARG A 248 108.808 194.834 -13.753 1.00 42.47 C ANISOU 1648 CA ARG A 248 4837 3598 7700 -125 477 -957 C ATOM 1649 C ARG A 248 108.947 193.383 -13.325 1.00 39.93 C ANISOU 1649 C ARG A 248 4465 3269 7438 -88 432 -983 C ATOM 1650 O ARG A 248 109.132 192.505 -14.174 1.00 40.33 O ANISOU 1650 O ARG A 248 4510 3288 7526 -77 445 -1067 O ATOM 1651 CB ARG A 248 110.168 195.535 -13.762 1.00 47.65 C ANISOU 1651 CB ARG A 248 5428 4254 8423 -146 563 -998 C ATOM 1652 CG ARG A 248 111.096 195.078 -14.882 1.00 53.18 C ANISOU 1652 CG ARG A 248 6096 4919 9191 -154 648 -1119 C ATOM 1653 CD ARG A 248 112.237 196.061 -15.122 1.00 57.31 C ANISOU 1653 CD ARG A 248 6570 5436 9770 -193 762 -1160 C ATOM 1654 NE ARG A 248 113.151 196.175 -13.985 1.00 61.28 N ANISOU 1654 NE ARG A 248 6967 5964 10351 -185 756 -1149 N ATOM 1655 CZ ARG A 248 113.212 197.226 -13.168 1.00 63.46 C ANISOU 1655 CZ ARG A 248 7229 6264 10618 -201 754 -1084 C ATOM 1656 NH1 ARG A 248 112.407 198.267 -13.361 1.00 63.33 N ANISOU 1656 NH1 ARG A 248 7300 6249 10514 -228 757 -1014 N ATOM 1657 NH2 ARG A 248 114.086 197.241 -12.162 1.00 63.89 N ANISOU 1657 NH2 ARG A 248 7180 6340 10755 -188 743 -1095 N ATOM 1658 N LYS A 249 108.821 193.101 -12.027 1.00 38.47 N ANISOU 1658 N LYS A 249 4248 3108 7260 -66 379 -914 N ATOM 1659 CA LYS A 249 108.924 191.716 -11.577 1.00 38.64 C ANISOU 1659 CA LYS A 249 4232 3109 7341 -32 341 -929 C ATOM 1660 C LYS A 249 107.635 190.947 -11.826 1.00 40.41 C ANISOU 1660 C LYS A 249 4495 3311 7549 -27 295 -916 C ATOM 1661 O LYS A 249 107.658 189.844 -12.382 1.00 41.73 O ANISOU 1661 O LYS A 249 4658 3442 7756 -11 287 -977 O ATOM 1662 CB LYS A 249 109.284 191.648 -10.090 1.00 37.52 C ANISOU 1662 CB LYS A 249 4029 2982 7245 -10 311 -873 C ATOM 1663 CG LYS A 249 109.602 190.227 -9.627 1.00 38.48 C ANISOU 1663 CG LYS A 249 4106 3065 7451 27 281 -895 C ATOM 1664 CD LYS A 249 109.519 190.043 -8.112 1.00 39.89 C ANISOU 1664 CD LYS A 249 4247 3242 7666 51 240 -824 C ATOM 1665 CE LYS A 249 109.874 188.591 -7.721 1.00 42.14 C ANISOU 1665 CE LYS A 249 4504 3474 8034 90 214 -844 C ATOM 1666 NZ LYS A 249 109.636 188.255 -6.281 1.00 43.04 N ANISOU 1666 NZ LYS A 249 4608 3571 8176 118 173 -770 N ATOM 1667 N LEU A 250 106.498 191.513 -11.423 1.00 40.23 N ANISOU 1667 N LEU A 250 4497 3304 7485 -41 267 -847 N ATOM 1668 CA LEU A 250 105.240 190.783 -11.537 1.00 40.56 C ANISOU 1668 CA LEU A 250 4553 3322 7538 -39 226 -839 C ATOM 1669 C LEU A 250 104.796 190.637 -12.983 1.00 40.53 C ANISOU 1669 C LEU A 250 4614 3297 7488 -50 228 -909 C ATOM 1670 O LEU A 250 104.182 189.629 -13.351 1.00 40.86 O ANISOU 1670 O LEU A 250 4652 3305 7569 -42 200 -948 O ATOM 1671 CB LEU A 250 104.160 191.474 -10.713 1.00 26.86 C ANISOU 1671 CB LEU A 250 2822 1612 5773 -49 198 -753 C ATOM 1672 CG LEU A 250 104.233 191.203 -9.218 1.00 29.97 C ANISOU 1672 CG LEU A 250 3156 2012 6222 -30 180 -689 C ATOM 1673 CD1 LEU A 250 103.087 191.927 -8.575 1.00 29.25 C ANISOU 1673 CD1 LEU A 250 3076 1947 6092 -40 158 -617 C ATOM 1674 CD2 LEU A 250 104.170 189.706 -8.933 1.00 27.43 C ANISOU 1674 CD2 LEU A 250 2796 1639 5988 -8 163 -706 C ATOM 1675 N TRP A 251 105.080 191.635 -13.813 1.00 39.86 N ANISOU 1675 N TRP A 251 4596 3228 7322 -69 259 -928 N ATOM 1676 CA TRP A 251 104.566 191.653 -15.176 1.00 40.28 C ANISOU 1676 CA TRP A 251 4711 3253 7341 -78 261 -1000 C ATOM 1677 C TRP A 251 105.529 191.089 -16.208 1.00 41.80 C ANISOU 1677 C TRP A 251 4881 3413 7590 -68 309 -1121 C ATOM 1678 O TRP A 251 105.082 190.510 -17.201 1.00 42.75 O ANISOU 1678 O TRP A 251 5027 3502 7713 -60 295 -1207 O ATOM 1679 CB TRP A 251 104.165 193.078 -15.568 1.00 39.38 C ANISOU 1679 CB TRP A 251 4666 3150 7147 -104 276 -966 C ATOM 1680 CG TRP A 251 102.743 193.377 -15.215 1.00 38.29 C ANISOU 1680 CG TRP A 251 4572 3027 6950 -110 216 -898 C ATOM 1681 CD1 TRP A 251 101.647 193.168 -15.998 1.00 38.63 C ANISOU 1681 CD1 TRP A 251 4661 3045 6973 -111 177 -937 C ATOM 1682 CD2 TRP A 251 102.257 193.911 -13.980 1.00 37.04 C ANISOU 1682 CD2 TRP A 251 4379 2903 6792 -113 196 -802 C ATOM 1683 NE1 TRP A 251 100.509 193.544 -15.331 1.00 37.82 N ANISOU 1683 NE1 TRP A 251 4567 2965 6838 -117 133 -861 N ATOM 1684 CE2 TRP A 251 100.857 194.003 -14.088 1.00 37.03 C ANISOU 1684 CE2 TRP A 251 4406 2898 6768 -118 149 -783 C ATOM 1685 CE3 TRP A 251 102.869 194.315 -12.791 1.00 36.38 C ANISOU 1685 CE3 TRP A 251 4231 2849 6741 -110 214 -743 C ATOM 1686 CZ2 TRP A 251 100.059 194.492 -13.055 1.00 36.96 C ANISOU 1686 CZ2 TRP A 251 4363 2915 6766 -120 125 -705 C ATOM 1687 CZ3 TRP A 251 102.076 194.799 -11.767 1.00 36.00 C ANISOU 1687 CZ3 TRP A 251 4158 2828 6694 -110 186 -668 C ATOM 1688 CH2 TRP A 251 100.686 194.886 -11.906 1.00 36.38 C ANISOU 1688 CH2 TRP A 251 4234 2873 6718 -115 145 -648 C ATOM 1689 N CYS A 252 106.830 191.220 -15.998 1.00 41.70 N ANISOU 1689 N CYS A 252 4814 3406 7624 -66 364 -1142 N ATOM 1690 CA CYS A 252 107.802 190.821 -17.001 1.00 43.15 C ANISOU 1690 CA CYS A 252 4972 3565 7857 -58 425 -1266 C ATOM 1691 C CYS A 252 108.667 189.664 -16.520 1.00 43.75 C ANISOU 1691 C CYS A 252 4964 3632 8026 -29 421 -1303 C ATOM 1692 O CYS A 252 108.634 188.585 -17.117 1.00 44.17 O ANISOU 1692 O CYS A 252 5007 3656 8118 -6 407 -1387 O ATOM 1693 CB CYS A 252 108.665 192.026 -17.393 1.00 43.78 C ANISOU 1693 CB CYS A 252 5057 3652 7927 -86 516 -1284 C ATOM 1694 SG CYS A 252 107.696 193.496 -17.859 1.00 43.71 S ANISOU 1694 SG CYS A 252 5157 3640 7813 -121 524 -1225 S ATOM 1695 N ARG A 253 109.418 189.856 -15.430 1.00 43.85 N ANISOU 1695 N ARG A 253 4917 3666 8079 -25 427 -1246 N ATOM 1696 CA ARG A 253 110.372 188.857 -14.955 1.00 45.08 C ANISOU 1696 CA ARG A 253 4993 3806 8328 7 425 -1285 C ATOM 1697 C ARG A 253 109.712 187.580 -14.444 1.00 45.40 C ANISOU 1697 C ARG A 253 5034 3819 8397 36 355 -1258 C ATOM 1698 O ARG A 253 110.375 186.538 -14.391 1.00 46.29 O ANISOU 1698 O ARG A 253 5097 3902 8589 66 351 -1313 O ATOM 1699 CB ARG A 253 111.243 189.460 -13.856 1.00 45.51 C ANISOU 1699 CB ARG A 253 4987 3888 8416 6 439 -1232 C ATOM 1700 CG ARG A 253 111.977 190.721 -14.270 1.00 46.79 C ANISOU 1700 CG ARG A 253 5134 4071 8574 -29 520 -1260 C ATOM 1701 CD ARG A 253 113.050 190.462 -15.326 1.00 49.82 C ANISOU 1701 CD ARG A 253 5472 4436 9021 -30 602 -1395 C ATOM 1702 NE ARG A 253 113.541 191.721 -15.883 1.00 52.48 N ANISOU 1702 NE ARG A 253 5811 4783 9346 -75 700 -1421 N ATOM 1703 CZ ARG A 253 113.135 192.239 -17.039 1.00 55.45 C ANISOU 1703 CZ ARG A 253 6262 5145 9662 -101 758 -1461 C ATOM 1704 NH1 ARG A 253 112.243 191.595 -17.783 1.00 57.00 N ANISOU 1704 NH1 ARG A 253 6529 5323 9806 -82 717 -1491 N ATOM 1705 NH2 ARG A 253 113.626 193.398 -17.456 1.00 56.36 N ANISOU 1705 NH2 ARG A 253 6382 5258 9774 -146 863 -1476 N ATOM 1706 N GLN A 254 108.447 187.638 -14.029 1.00 44.61 N ANISOU 1706 N GLN A 254 4985 3725 8241 26 305 -1175 N ATOM 1707 CA GLN A 254 107.710 186.445 -13.644 1.00 44.99 C ANISOU 1707 CA GLN A 254 5034 3737 8323 44 253 -1156 C ATOM 1708 C GLN A 254 106.448 186.243 -14.460 1.00 46.33 C ANISOU 1708 C GLN A 254 5251 3890 8460 29 227 -1182 C ATOM 1709 O GLN A 254 105.741 185.253 -14.240 1.00 48.14 O ANISOU 1709 O GLN A 254 5455 4078 8759 36 193 -1185 O ATOM 1710 CB GLN A 254 107.342 186.487 -12.156 1.00 43.82 C ANISOU 1710 CB GLN A 254 4845 3591 8214 48 225 -1051 C ATOM 1711 CG GLN A 254 108.508 186.208 -11.226 1.00 43.94 C ANISOU 1711 CG GLN A 254 4806 3600 8289 76 230 -1037 C ATOM 1712 CD GLN A 254 108.095 186.079 -9.771 1.00 43.66 C ANISOU 1712 CD GLN A 254 4747 3556 8288 87 198 -940 C ATOM 1713 OE1 GLN A 254 106.946 186.326 -9.411 1.00 43.02 O ANISOU 1713 OE1 GLN A 254 4683 3481 8183 70 180 -879 O ATOM 1714 NE2 GLN A 254 109.037 185.687 -8.927 1.00 44.47 N ANISOU 1714 NE2 GLN A 254 4812 3641 8442 121 192 -930 N ATOM 1715 N GLY A1001 106.150 187.133 -15.400 1.00 49.18 N ANISOU 1715 N GLY A1001 5999 3878 8809 546 -137 -850 N ATOM 1716 CA GLY A1001 104.920 187.031 -16.157 1.00 51.07 C ANISOU 1716 CA GLY A1001 6086 4129 9191 658 -296 -894 C ATOM 1717 C GLY A1001 104.989 185.970 -17.232 1.00 51.38 C ANISOU 1717 C GLY A1001 6092 4244 9186 633 -465 -943 C ATOM 1718 O GLY A1001 105.292 186.277 -18.389 1.00 52.14 O ANISOU 1718 O GLY A1001 6313 4362 9137 703 -600 -915 O ATOM 1719 N ILE A1002 104.743 184.711 -16.846 1.00 50.97 N ANISOU 1719 N ILE A1002 5894 4224 9249 534 -446 -1015 N ATOM 1720 CA ILE A1002 104.773 183.598 -17.787 1.00 50.47 C ANISOU 1720 CA ILE A1002 5797 4220 9161 498 -601 -1082 C ATOM 1721 C ILE A1002 103.510 183.601 -18.639 1.00 53.53 C ANISOU 1721 C ILE A1002 6034 4635 9671 605 -820 -1142 C ATOM 1722 O ILE A1002 102.431 184.015 -18.194 1.00 54.48 O ANISOU 1722 O ILE A1002 5981 4732 9988 666 -816 -1152 O ATOM 1723 CB ILE A1002 104.933 182.260 -17.045 1.00 48.48 C ANISOU 1723 CB ILE A1002 5443 3972 9007 355 -497 -1137 C ATOM 1724 CG1 ILE A1002 105.021 181.112 -18.061 1.00 49.25 C ANISOU 1724 CG1 ILE A1002 5528 4115 9071 317 -656 -1215 C ATOM 1725 CG2 ILE A1002 103.781 182.073 -16.066 1.00 48.23 C ANISOU 1725 CG2 ILE A1002 5184 3906 9233 343 -407 -1171 C ATOM 1726 CD1 ILE A1002 105.217 179.731 -17.455 1.00 49.17 C ANISOU 1726 CD1 ILE A1002 5431 4095 9154 180 -561 -1267 C ATOM 1727 N ASP A1003 103.634 183.107 -19.867 1.00 54.88 N ANISOU 1727 N ASP A1003 6268 4854 9730 632 -1017 -1187 N ATOM 1728 CA ASP A1003 102.505 183.066 -20.790 1.00 58.35 C ANISOU 1728 CA ASP A1003 6583 5325 10260 737 -1274 -1255 C ATOM 1729 C ASP A1003 101.684 181.796 -20.571 1.00 59.22 C ANISOU 1729 C ASP A1003 6440 5446 10614 643 -1336 -1378 C ATOM 1730 O ASP A1003 102.071 180.708 -21.006 1.00 58.95 O ANISOU 1730 O ASP A1003 6438 5433 10528 556 -1396 -1450 O ATOM 1731 CB ASP A1003 102.999 183.165 -22.241 1.00 59.98 C ANISOU 1731 CB ASP A1003 7009 5573 10209 824 -1468 -1251 C ATOM 1732 CG ASP A1003 101.876 183.431 -23.231 1.00 63.85 C ANISOU 1732 CG ASP A1003 7419 6096 10746 972 -1760 -1302 C ATOM 1733 OD1 ASP A1003 100.695 183.351 -22.834 1.00 65.83 O ANISOU 1733 OD1 ASP A1003 7403 6343 11268 988 -1828 -1359 O ATOM 1734 OD2 ASP A1003 102.175 183.722 -24.408 1.00 65.44 O ANISOU 1734 OD2 ASP A1003 7825 6325 10715 1080 -1922 -1283 O HETATM 1735 N YCM A1004 100.566 181.953 -19.864 1.00 61.02 N ANISOU 1735 N YCM A1004 6418 5648 11120 658 -1300 -1397 N HETATM 1736 CA YCM A1004 99.593 180.856 -19.589 1.00 63.35 C ANISOU 1736 CA YCM A1004 6423 5933 11713 571 -1343 -1508 C HETATM 1737 CB YCM A1004 100.120 179.939 -18.505 1.00 62.73 C ANISOU 1737 CB YCM A1004 6325 5816 11695 406 -1089 -1507 C HETATM 1738 SG YCM A1004 99.867 180.532 -16.816 1.00 63.13 S ANISOU 1738 SG YCM A1004 6290 5801 11897 390 -757 -1419 S HETATM 1739 CD YCM A1004 100.394 179.078 -15.868 1.00 63.21 C ANISOU 1739 CD YCM A1004 6277 5772 11968 199 -541 -1442 C HETATM 1740 CE YCM A1004 99.513 177.887 -16.165 1.00 66.64 C ANISOU 1740 CE YCM A1004 6467 6190 12663 122 -643 -1555 C HETATM 1741 OZ1 YCM A1004 99.999 176.848 -16.598 1.00 66.73 O ANISOU 1741 OZ1 YCM A1004 6529 6206 12619 30 -706 -1614 O HETATM 1742 NZ2 YCM A1004 98.229 178.052 -15.940 1.00 69.88 N ANISOU 1742 NZ2 YCM A1004 6609 6573 13368 159 -656 -1586 N HETATM 1743 C YCM A1004 99.266 180.085 -20.870 1.00 65.31 C ANISOU 1743 C YCM A1004 6641 6226 11946 580 -1650 -1627 C HETATM 1744 O YCM A1004 99.397 178.848 -20.867 1.00 64.99 O ANISOU 1744 O YCM A1004 6547 6176 11972 449 -1652 -1714 O ATOM 1745 N SER A1005 98.886 180.811 -21.911 1.00 67.48 N ANISOU 1745 N SER A1005 6973 6542 12126 735 -1899 -1628 N ATOM 1746 CA SER A1005 98.340 180.236 -23.130 1.00 70.48 C ANISOU 1746 CA SER A1005 7310 6964 12507 776 -2236 -1751 C ATOM 1747 C SER A1005 99.368 179.510 -23.988 1.00 69.41 C ANISOU 1747 C SER A1005 7437 6853 12082 729 -2309 -1795 C ATOM 1748 O SER A1005 99.032 178.537 -24.664 1.00 70.72 O ANISOU 1748 O SER A1005 7545 7031 12294 684 -2516 -1932 O ATOM 1749 CB SER A1005 97.688 181.345 -23.946 1.00 73.24 C ANISOU 1749 CB SER A1005 7678 7347 12803 982 -2474 -1718 C ATOM 1750 OG SER A1005 96.926 182.188 -23.099 1.00 74.39 O ANISOU 1750 OG SER A1005 7625 7459 13179 1045 -2354 -1650 O ATOM 1751 N PHE A1006 100.610 179.993 -23.980 1.00 67.72 N ANISOU 1751 N PHE A1006 7510 6640 11581 742 -2139 -1683 N ATOM 1752 CA PHE A1006 101.639 179.362 -24.801 1.00 67.25 C ANISOU 1752 CA PHE A1006 7706 6599 11246 712 -2176 -1711 C ATOM 1753 C PHE A1006 102.251 178.136 -24.125 1.00 66.49 C ANISOU 1753 C PHE A1006 7573 6470 11219 528 -1989 -1757 C ATOM 1754 O PHE A1006 102.397 177.083 -24.759 1.00 67.17 O ANISOU 1754 O PHE A1006 7703 6559 11261 473 -2103 -1867 O ATOM 1755 CB PHE A1006 102.743 180.368 -25.141 1.00 65.81 C ANISOU 1755 CB PHE A1006 7834 6424 10749 802 -2064 -1567 C ATOM 1756 CG PHE A1006 103.848 179.788 -25.978 1.00 64.97 C ANISOU 1756 CG PHE A1006 7994 6329 10361 784 -2063 -1580 C ATOM 1757 CD1 PHE A1006 104.952 179.199 -25.384 1.00 62.30 C ANISOU 1757 CD1 PHE A1006 7726 5968 9978 653 -1820 -1548 C ATOM 1758 CD2 PHE A1006 103.771 179.809 -27.362 1.00 67.05 C ANISOU 1758 CD2 PHE A1006 8442 6627 10405 909 -2305 -1624 C ATOM 1759 CE1 PHE A1006 105.966 178.661 -26.153 1.00 62.08 C ANISOU 1759 CE1 PHE A1006 7931 5947 9711 645 -1801 -1556 C ATOM 1760 CE2 PHE A1006 104.783 179.273 -28.135 1.00 67.09 C ANISOU 1760 CE2 PHE A1006 8706 6638 10148 904 -2277 -1635 C ATOM 1761 CZ PHE A1006 105.882 178.700 -27.528 1.00 65.07 C ANISOU 1761 CZ PHE A1006 8500 6354 9870 770 -2016 -1600 C ATOM 1762 N TRP A1007 102.626 178.250 -22.847 1.00 64.75 N ANISOU 1762 N TRP A1007 7291 6214 11098 439 -1707 -1674 N ATOM 1763 CA TRP A1007 103.304 177.149 -22.162 1.00 64.05 C ANISOU 1763 CA TRP A1007 7195 6091 11051 281 -1518 -1694 C ATOM 1764 C TRP A1007 102.258 176.211 -21.564 1.00 68.01 C ANISOU 1764 C TRP A1007 7401 6552 11887 178 -1526 -1795 C ATOM 1765 O TRP A1007 102.013 176.167 -20.357 1.00 66.97 O ANISOU 1765 O TRP A1007 7122 6379 11943 109 -1319 -1752 O ATOM 1766 CB TRP A1007 104.272 177.683 -21.120 1.00 60.11 C ANISOU 1766 CB TRP A1007 6796 5573 10471 242 -1234 -1560 C ATOM 1767 CG TRP A1007 105.322 178.550 -21.727 1.00 58.87 C ANISOU 1767 CG TRP A1007 6908 5440 10020 325 -1216 -1464 C ATOM 1768 CD1 TRP A1007 105.299 179.910 -21.824 1.00 59.52 C ANISOU 1768 CD1 TRP A1007 7072 5527 10016 438 -1217 -1370 C ATOM 1769 CD2 TRP A1007 106.547 178.125 -22.342 1.00 57.45 C ANISOU 1769 CD2 TRP A1007 6947 5271 9610 304 -1180 -1447 C ATOM 1770 NE1 TRP A1007 106.437 180.361 -22.449 1.00 58.72 N ANISOU 1770 NE1 TRP A1007 7225 5433 9652 479 -1176 -1293 N ATOM 1771 CE2 TRP A1007 107.219 179.285 -22.779 1.00 57.36 C ANISOU 1771 CE2 TRP A1007 7136 5270 9390 400 -1149 -1337 C ATOM 1772 CE3 TRP A1007 107.143 176.881 -22.559 1.00 56.42 C ANISOU 1772 CE3 TRP A1007 6862 5134 9442 217 -1155 -1511 C ATOM 1773 CZ2 TRP A1007 108.452 179.236 -23.424 1.00 55.73 C ANISOU 1773 CZ2 TRP A1007 7158 5068 8950 409 -1086 -1287 C ATOM 1774 CZ3 TRP A1007 108.372 176.835 -23.197 1.00 55.23 C ANISOU 1774 CZ3 TRP A1007 6943 4992 9050 235 -1097 -1464 C ATOM 1775 CH2 TRP A1007 109.010 178.004 -23.622 1.00 54.93 C ANISOU 1775 CH2 TRP A1007 7087 4966 8818 329 -1059 -1352 C ATOM 1776 N ASN A1008 101.632 175.459 -22.461 1.00 73.85 N ANISOU 1776 N ASN A1008 8066 7297 12698 172 -1771 -1936 N ATOM 1777 CA ASN A1008 100.620 174.466 -22.139 1.00 79.20 C ANISOU 1777 CA ASN A1008 8459 7924 13709 65 -1821 -2056 C ATOM 1778 C ASN A1008 101.048 173.107 -22.672 1.00 82.96 C ANISOU 1778 C ASN A1008 9010 8368 14143 -37 -1885 -2173 C ATOM 1779 O ASN A1008 101.694 173.006 -23.718 1.00 82.29 O ANISOU 1779 O ASN A1008 9161 8316 13789 18 -2022 -2209 O ATOM 1780 CB ASN A1008 99.259 174.825 -22.745 1.00 82.89 C ANISOU 1780 CB ASN A1008 8714 8413 14368 150 -2105 -2143 C ATOM 1781 CG ASN A1008 98.392 175.616 -21.800 1.00 84.03 C ANISOU 1781 CG ASN A1008 8620 8542 14764 185 -1983 -2070 C ATOM 1782 OD1 ASN A1008 98.800 175.935 -20.684 1.00 83.36 O ANISOU 1782 OD1 ASN A1008 8554 8429 14689 149 -1687 -1956 O ATOM 1783 ND2 ASN A1008 97.184 175.944 -22.243 1.00 86.95 N ANISOU 1783 ND2 ASN A1008 8770 8928 15339 264 -2217 -2137 N ATOM 1784 N GLU A1009 100.653 172.058 -21.956 1.00 88.35 N ANISOU 1784 N GLU A1009 9517 9041 15010 -144 -1726 -2166 N ATOM 1785 CA GLU A1009 100.890 170.699 -22.417 1.00 90.81 C ANISOU 1785 CA GLU A1009 9889 9369 15244 -209 -1737 -2219 C ATOM 1786 C GLU A1009 99.955 170.293 -23.555 1.00 93.55 C ANISOU 1786 C GLU A1009 10153 9719 15673 -179 -2065 -2380 C ATOM 1787 O GLU A1009 100.206 169.274 -24.208 1.00 94.18 O ANISOU 1787 O GLU A1009 10335 9803 15645 -216 -2128 -2449 O ATOM 1788 CB GLU A1009 100.759 169.723 -21.243 1.00 92.88 C ANISOU 1788 CB GLU A1009 10017 9613 15662 -315 -1450 -2145 C ATOM 1789 CG GLU A1009 99.385 169.716 -20.562 1.00 97.07 C ANISOU 1789 CG GLU A1009 10234 10098 16551 -335 -1417 -2164 C ATOM 1790 CD GLU A1009 99.143 170.914 -19.647 1.00 98.39 C ANISOU 1790 CD GLU A1009 10305 10247 16832 -294 -1287 -2077 C ATOM 1791 OE1 GLU A1009 99.605 172.033 -19.967 1.00 98.15 O ANISOU 1791 OE1 GLU A1009 10399 10231 16662 -221 -1374 -2059 O ATOM 1792 OE2 GLU A1009 98.482 170.730 -18.603 1.00 99.66 O ANISOU 1792 OE2 GLU A1009 10279 10364 17223 -330 -1086 -2029 O ATOM 1793 N SER A1010 98.895 171.067 -23.810 1.00 96.21 N ANISOU 1793 N SER A1010 10310 10054 16191 -108 -2280 -2440 N ATOM 1794 CA SER A1010 97.954 170.732 -24.875 1.00100.10 C ANISOU 1794 CA SER A1010 10718 10561 16754 -65 -2612 -2585 C ATOM 1795 C SER A1010 98.609 170.786 -26.251 1.00100.24 C ANISOU 1795 C SER A1010 11037 10619 16431 19 -2869 -2667 C ATOM 1796 O SER A1010 98.173 170.090 -27.174 1.00103.30 O ANISOU 1796 O SER A1010 11445 11016 16788 30 -3093 -2787 O ATOM 1797 CB SER A1010 96.754 171.676 -24.825 1.00102.64 C ANISOU 1797 CB SER A1010 10789 10887 17322 18 -2784 -2606 C ATOM 1798 OG SER A1010 96.334 171.911 -23.492 1.00102.42 O ANISOU 1798 OG SER A1010 10535 10816 17563 -36 -2504 -2508 O ATOM 1799 N TYR A1011 99.643 171.609 -26.408 1.00 97.49 N ANISOU 1799 N TYR A1011 10943 10282 15818 85 -2831 -2606 N ATOM 1800 CA TYR A1011 100.350 171.762 -27.674 1.00 97.10 C ANISOU 1800 CA TYR A1011 11225 10258 15411 186 -3034 -2668 C ATOM 1801 C TYR A1011 101.151 170.523 -28.057 1.00 95.71 C ANISOU 1801 C TYR A1011 11235 10075 15054 116 -2926 -2695 C ATOM 1802 O TYR A1011 101.551 170.401 -29.220 1.00 96.78 O ANISOU 1802 O TYR A1011 11633 10228 14911 198 -3107 -2773 O ATOM 1803 CB TYR A1011 101.268 172.988 -27.609 1.00 95.86 C ANISOU 1803 CB TYR A1011 11302 10144 14977 303 -2882 -2494 C ATOM 1804 CG TYR A1011 100.511 174.301 -27.540 1.00 97.90 C ANISOU 1804 CG TYR A1011 11451 10453 15292 437 -2978 -2408 C ATOM 1805 CD1 TYR A1011 99.550 174.514 -26.561 1.00 99.28 C ANISOU 1805 CD1 TYR A1011 11289 10606 15827 386 -2916 -2392 C ATOM 1806 CD2 TYR A1011 100.748 175.320 -28.454 1.00 98.96 C ANISOU 1806 CD2 TYR A1011 11828 10648 15125 622 -3114 -2338 C ATOM 1807 CE1 TYR A1011 98.849 175.695 -26.493 1.00101.03 C ANISOU 1807 CE1 TYR A1011 11407 10865 16114 517 -2993 -2316 C ATOM 1808 CE2 TYR A1011 100.056 176.517 -28.387 1.00100.61 C ANISOU 1808 CE2 TYR A1011 11944 10892 15392 754 -3196 -2255 C ATOM 1809 CZ TYR A1011 99.103 176.696 -27.404 1.00102.04 C ANISOU 1809 CZ TYR A1011 11777 11051 15942 702 -3139 -2248 C ATOM 1810 OH TYR A1011 98.394 177.872 -27.317 1.00103.23 O ANISOU 1810 OH TYR A1011 11826 11227 16169 841 -3210 -2166 O ATOM 1811 N LEU A1012 101.419 169.629 -27.106 1.00 93.17 N ANISOU 1811 N LEU A1012 10805 9729 14866 -21 -2630 -2627 N ATOM 1812 CA LEU A1012 102.094 168.363 -27.364 1.00 92.14 C ANISOU 1812 CA LEU A1012 10814 9585 14611 -97 -2519 -2651 C ATOM 1813 C LEU A1012 101.136 167.346 -27.982 1.00 93.91 C ANISOU 1813 C LEU A1012 10923 9795 14965 -137 -2721 -2796 C ATOM 1814 O LEU A1012 99.914 167.430 -27.818 1.00 95.66 O ANISOU 1814 O LEU A1012 10882 10011 15454 -145 -2854 -2846 O ATOM 1815 CB LEU A1012 102.689 167.806 -26.066 1.00 89.80 C ANISOU 1815 CB LEU A1012 10445 9270 14405 -213 -2146 -2514 C ATOM 1816 CG LEU A1012 103.460 168.846 -25.252 1.00 87.25 C ANISOU 1816 CG LEU A1012 10181 8961 14011 -185 -1938 -2363 C ATOM 1817 CD1 LEU A1012 103.681 168.378 -23.819 1.00 85.63 C ANISOU 1817 CD1 LEU A1012 9845 8749 13941 -286 -1612 -2230 C ATOM 1818 CD2 LEU A1012 104.778 169.161 -25.941 1.00 86.08 C ANISOU 1818 CD2 LEU A1012 10357 8819 13530 -116 -1912 -2334 C ATOM 1819 N THR A1013 101.708 166.385 -28.717 1.00 93.42 N ANISOU 1819 N THR A1013 11063 9718 14716 -161 -2739 -2865 N ATOM 1820 CA THR A1013 100.962 165.285 -29.315 1.00 95.06 C ANISOU 1820 CA THR A1013 11202 9895 15022 -214 -2905 -3007 C ATOM 1821 C THR A1013 101.651 163.957 -29.027 1.00 93.10 C ANISOU 1821 C THR A1013 11031 9595 14748 -332 -2672 -2993 C ATOM 1822 O THR A1013 102.876 163.886 -28.888 1.00 91.09 O ANISOU 1822 O THR A1013 10983 9340 14287 -330 -2467 -2909 O ATOM 1823 CB THR A1013 100.809 165.436 -30.843 1.00 97.53 C ANISOU 1823 CB THR A1013 11729 10233 15094 -96 -3255 -3151 C ATOM 1824 OG1 THR A1013 102.102 165.516 -31.457 1.00 96.40 O ANISOU 1824 OG1 THR A1013 11944 10098 14584 -29 -3183 -3130 O ATOM 1825 CG2 THR A1013 99.988 166.674 -31.198 1.00 98.71 C ANISOU 1825 CG2 THR A1013 11796 10432 15277 34 -3530 -3173 C ATOM 1826 N GLY A1014 100.845 162.897 -28.949 1.00 93.28 N ANISOU 1826 N GLY A1014 10884 9567 14993 -430 -2708 -3075 N ATOM 1827 CA GLY A1014 101.360 161.582 -28.635 1.00 91.76 C ANISOU 1827 CA GLY A1014 10745 9310 14810 -543 -2501 -3067 C ATOM 1828 C GLY A1014 101.684 161.449 -27.157 1.00 87.33 C ANISOU 1828 C GLY A1014 10051 8734 14396 -618 -2156 -2897 C ATOM 1829 O GLY A1014 101.372 162.312 -26.329 1.00 86.92 O ANISOU 1829 O GLY A1014 9838 8716 14473 -596 -2073 -2798 O ATOM 1830 N SER A1015 102.318 160.324 -26.828 1.00 84.98 N ANISOU 1830 N SER A1015 9836 8380 14071 -700 -1957 -2865 N ATOM 1831 CA SER A1015 102.822 160.048 -25.489 1.00 79.95 C ANISOU 1831 CA SER A1015 9137 7730 13510 -755 -1631 -2700 C ATOM 1832 C SER A1015 104.209 160.658 -25.303 1.00 74.78 C ANISOU 1832 C SER A1015 8697 7124 12591 -693 -1471 -2573 C ATOM 1833 O SER A1015 104.953 160.875 -26.262 1.00 74.43 O ANISOU 1833 O SER A1015 8888 7094 12297 -629 -1560 -2622 O ATOM 1834 CB SER A1015 102.881 158.541 -25.225 1.00 80.95 C ANISOU 1834 CB SER A1015 9264 7766 13728 -859 -1503 -2720 C ATOM 1835 OG SER A1015 103.943 157.936 -25.946 1.00 80.72 O ANISOU 1835 OG SER A1015 9510 7709 13451 -849 -1487 -2756 O ATOM 1836 N ARG A1016 104.553 160.926 -24.040 1.00 70.70 N ANISOU 1836 N ARG A1016 8102 6629 12131 -707 -1227 -2410 N ATOM 1837 CA ARG A1016 105.862 161.501 -23.744 1.00 66.30 C ANISOU 1837 CA ARG A1016 7723 6117 11352 -655 -1068 -2281 C ATOM 1838 C ARG A1016 106.991 160.560 -24.150 1.00 64.70 C ANISOU 1838 C ARG A1016 7745 5872 10968 -665 -977 -2282 C ATOM 1839 O ARG A1016 108.070 161.017 -24.543 1.00 62.58 O ANISOU 1839 O ARG A1016 7674 5625 10477 -601 -937 -2242 O ATOM 1840 CB ARG A1016 105.960 161.849 -22.258 1.00 64.14 C ANISOU 1840 CB ARG A1016 7322 5871 11176 -671 -836 -2115 C ATOM 1841 CG ARG A1016 107.125 162.758 -21.897 1.00 62.09 C ANISOU 1841 CG ARG A1016 7202 5670 10719 -610 -713 -1984 C ATOM 1842 CD ARG A1016 107.142 163.090 -20.414 1.00 61.20 C ANISOU 1842 CD ARG A1016 6972 5587 10694 -624 -507 -1834 C ATOM 1843 NE ARG A1016 108.160 164.087 -20.093 1.00 59.38 N ANISOU 1843 NE ARG A1016 6860 5414 10288 -568 -422 -1721 N ATOM 1844 CZ ARG A1016 107.929 165.394 -20.034 1.00 58.54 C ANISOU 1844 CZ ARG A1016 6720 5346 10175 -519 -474 -1699 C ATOM 1845 NH1 ARG A1016 106.713 165.868 -20.271 1.00 39.59 N ANISOU 1845 NH1 ARG A1016 4168 2935 7940 -511 -616 -1782 N ATOM 1846 NH2 ARG A1016 108.912 166.228 -19.732 1.00 56.37 N ANISOU 1846 NH2 ARG A1016 6560 5113 9744 -477 -387 -1595 N ATOM 1847 N ASP A1017 106.759 159.244 -24.078 1.00 66.62 N ANISOU 1847 N ASP A1017 7960 6040 11313 -741 -936 -2330 N ATOM 1848 CA ASP A1017 107.777 158.292 -24.513 1.00 67.10 C ANISOU 1848 CA ASP A1017 8235 6043 11217 -745 -857 -2343 C ATOM 1849 C ASP A1017 108.070 158.455 -26.000 1.00 66.77 C ANISOU 1849 C ASP A1017 8409 5991 10970 -685 -1040 -2483 C ATOM 1850 O ASP A1017 109.235 158.438 -26.417 1.00 65.69 O ANISOU 1850 O ASP A1017 8496 5843 10622 -629 -956 -2457 O ATOM 1851 CB ASP A1017 107.329 156.857 -24.217 1.00 71.27 C ANISOU 1851 CB ASP A1017 8690 6477 11913 -838 -802 -2386 C ATOM 1852 CG ASP A1017 106.959 156.631 -22.747 1.00 73.05 C ANISOU 1852 CG ASP A1017 8713 6702 12342 -887 -613 -2255 C ATOM 1853 OD1 ASP A1017 107.401 157.422 -21.880 1.00 70.62 O ANISOU 1853 OD1 ASP A1017 8376 6465 11994 -845 -483 -2112 O ATOM 1854 OD2 ASP A1017 106.231 155.651 -22.460 1.00 74.65 O ANISOU 1854 OD2 ASP A1017 8797 6826 12741 -965 -591 -2300 O ATOM 1855 N GLU A1018 107.021 158.637 -26.813 1.00 68.29 N ANISOU 1855 N GLU A1018 8541 6188 11220 -684 -1293 -2634 N ATOM 1856 CA GLU A1018 107.200 158.780 -28.256 1.00 68.30 C ANISOU 1856 CA GLU A1018 8761 6184 11007 -613 -1493 -2779 C ATOM 1857 C GLU A1018 107.935 160.070 -28.597 1.00 65.16 C ANISOU 1857 C GLU A1018 8511 5855 10392 -494 -1499 -2721 C ATOM 1858 O GLU A1018 108.761 160.097 -29.519 1.00 65.08 O ANISOU 1858 O GLU A1018 8764 5829 10135 -417 -1509 -2769 O ATOM 1859 CB GLU A1018 105.843 158.738 -28.959 1.00 70.84 C ANISOU 1859 CB GLU A1018 8962 6505 11449 -628 -1792 -2945 C ATOM 1860 CG GLU A1018 105.163 157.367 -28.949 1.00 73.24 C ANISOU 1860 CG GLU A1018 9169 6718 11939 -742 -1819 -3044 C ATOM 1861 CD GLU A1018 103.731 157.403 -29.472 1.00 76.69 C ANISOU 1861 CD GLU A1018 9428 7158 12553 -762 -2112 -3193 C ATOM 1862 OE1 GLU A1018 103.083 158.474 -29.381 1.00 76.89 O ANISOU 1862 OE1 GLU A1018 9308 7255 12650 -706 -2243 -3176 O ATOM 1863 OE2 GLU A1018 103.256 156.356 -29.971 1.00 79.32 O ANISOU 1863 OE2 GLU A1018 9765 7414 12960 -832 -2216 -3329 O ATOM 1864 N ARG A1019 107.663 161.146 -27.852 1.00 62.75 N ANISOU 1864 N ARG A1019 8050 5616 10176 -474 -1476 -2615 N ATOM 1865 CA ARG A1019 108.339 162.411 -28.117 1.00 60.11 C ANISOU 1865 CA ARG A1019 7851 5333 9655 -365 -1475 -2554 C ATOM 1866 C ARG A1019 109.805 162.335 -27.723 1.00 57.70 C ANISOU 1866 C ARG A1019 7699 5013 9210 -349 -1207 -2425 C ATOM 1867 O ARG A1019 110.684 162.756 -28.484 1.00 56.99 O ANISOU 1867 O ARG A1019 7841 4918 8896 -256 -1193 -2434 O ATOM 1868 CB ARG A1019 107.650 163.553 -27.370 1.00 58.32 C ANISOU 1868 CB ARG A1019 7417 5166 9578 -354 -1510 -2478 C ATOM 1869 CG ARG A1019 106.172 163.709 -27.678 1.00 59.36 C ANISOU 1869 CG ARG A1019 7361 5309 9886 -358 -1773 -2595 C ATOM 1870 CD ARG A1019 105.641 165.028 -27.136 1.00 57.10 C ANISOU 1870 CD ARG A1019 6921 5070 9704 -311 -1817 -2526 C ATOM 1871 NE ARG A1019 104.348 164.860 -26.481 1.00 56.64 N ANISOU 1871 NE ARG A1019 6558 5007 9956 -375 -1864 -2546 N ATOM 1872 CZ ARG A1019 104.186 164.806 -25.164 1.00 53.69 C ANISOU 1872 CZ ARG A1019 5997 4631 9771 -443 -1641 -2428 C ATOM 1873 NH1 ARG A1019 105.238 164.921 -24.364 1.00 50.53 N ANISOU 1873 NH1 ARG A1019 5684 4244 9269 -455 -1383 -2281 N ATOM 1874 NH2 ARG A1019 102.973 164.647 -24.650 1.00 54.64 N ANISOU 1874 NH2 ARG A1019 5851 4733 10178 -488 -1676 -2456 N ATOM 1875 N LYS A1020 110.087 161.795 -26.535 1.00 56.23 N ANISOU 1875 N LYS A1020 7390 4819 9156 -427 -994 -2301 N ATOM 1876 CA LYS A1020 111.471 161.683 -26.093 1.00 54.39 C ANISOU 1876 CA LYS A1020 7278 4577 8812 -406 -760 -2173 C ATOM 1877 C LYS A1020 112.267 160.759 -27.002 1.00 55.40 C ANISOU 1877 C LYS A1020 7635 4628 8785 -378 -725 -2252 C ATOM 1878 O LYS A1020 113.446 161.014 -27.273 1.00 54.92 O ANISOU 1878 O LYS A1020 7747 4553 8566 -305 -602 -2199 O ATOM 1879 CB LYS A1020 111.526 161.183 -24.651 1.00 52.84 C ANISOU 1879 CB LYS A1020 6911 4391 8774 -480 -578 -2035 C ATOM 1880 CG LYS A1020 112.930 161.028 -24.095 1.00 51.29 C ANISOU 1880 CG LYS A1020 6809 4195 8486 -452 -367 -1897 C ATOM 1881 CD LYS A1020 112.898 160.720 -22.610 1.00 38.66 C ANISOU 1881 CD LYS A1020 5041 2625 7024 -505 -221 -1760 C ATOM 1882 CE LYS A1020 112.510 159.277 -22.341 1.00 44.46 C ANISOU 1882 CE LYS A1020 5724 3291 7879 -571 -185 -1797 C ATOM 1883 NZ LYS A1020 113.684 158.368 -22.465 1.00 44.07 N ANISOU 1883 NZ LYS A1020 5820 3186 7741 -543 -70 -1766 N ATOM 1884 N LYS A1021 111.640 159.686 -27.494 1.00 57.00 N ANISOU 1884 N LYS A1021 7845 4772 9041 -430 -823 -2382 N ATOM 1885 CA LYS A1021 112.346 158.791 -28.404 1.00 57.69 C ANISOU 1885 CA LYS A1021 8169 4775 8974 -399 -788 -2472 C ATOM 1886 C LYS A1021 112.642 159.490 -29.727 1.00 58.59 C ANISOU 1886 C LYS A1021 8511 4900 8850 -284 -903 -2576 C ATOM 1887 O LYS A1021 113.766 159.416 -30.241 1.00 58.32 O ANISOU 1887 O LYS A1021 8694 4826 8638 -204 -768 -2566 O ATOM 1888 CB LYS A1021 111.535 157.512 -28.625 1.00 60.72 C ANISOU 1888 CB LYS A1021 8509 5087 9476 -488 -878 -2597 C ATOM 1889 CG LYS A1021 111.421 156.615 -27.388 1.00 61.49 C ANISOU 1889 CG LYS A1021 8433 5150 9782 -583 -729 -2494 C ATOM 1890 CD LYS A1021 110.625 155.324 -27.655 1.00 65.66 C ANISOU 1890 CD LYS A1021 8926 5585 10438 -673 -812 -2623 C ATOM 1891 CE LYS A1021 109.328 155.279 -26.835 1.00 68.44 C ANISOU 1891 CE LYS A1021 8983 5960 11063 -766 -873 -2612 C ATOM 1892 NZ LYS A1021 108.827 153.896 -26.567 1.00 71.39 N ANISOU 1892 NZ LYS A1021 9285 6227 11611 -865 -842 -2664 N ATOM 1893 N SER A1022 111.659 160.204 -30.281 1.00 59.78 N ANISOU 1893 N SER A1022 8617 5106 8991 -256 -1150 -2668 N ATOM 1894 CA SER A1022 111.922 160.998 -31.474 1.00 61.12 C ANISOU 1894 CA SER A1022 9016 5300 8905 -117 -1277 -2742 C ATOM 1895 C SER A1022 112.938 162.093 -31.192 1.00 58.90 C ANISOU 1895 C SER A1022 8811 5048 8519 -30 -1113 -2599 C ATOM 1896 O SER A1022 113.724 162.454 -32.075 1.00 59.46 O ANISOU 1896 O SER A1022 9136 5106 8348 96 -1079 -2616 O ATOM 1897 CB SER A1022 110.625 161.609 -31.993 1.00 63.17 C ANISOU 1897 CB SER A1022 9198 5617 9186 -90 -1600 -2846 C ATOM 1898 OG SER A1022 109.662 160.615 -32.289 1.00 65.90 O ANISOU 1898 OG SER A1022 9458 5930 9650 -171 -1765 -2985 O ATOM 1899 N LEU A1023 112.942 162.630 -29.970 1.00 56.94 N ANISOU 1899 N LEU A1023 8354 4838 8443 -88 -1003 -2452 N ATOM 1900 CA LEU A1023 113.872 163.705 -29.646 1.00 55.57 C ANISOU 1900 CA LEU A1023 8234 4686 8195 -17 -856 -2317 C ATOM 1901 C LEU A1023 115.308 163.207 -29.683 1.00 54.99 C ANISOU 1901 C LEU A1023 8312 4553 8028 18 -603 -2253 C ATOM 1902 O LEU A1023 116.173 163.808 -30.333 1.00 55.00 O ANISOU 1902 O LEU A1023 8510 4537 7850 136 -531 -2234 O ATOM 1903 CB LEU A1023 113.546 164.279 -28.271 1.00 53.96 C ANISOU 1903 CB LEU A1023 7770 4535 8195 -95 -790 -2178 C ATOM 1904 CG LEU A1023 114.242 165.596 -27.939 1.00 52.85 C ANISOU 1904 CG LEU A1023 7657 4422 8001 -30 -694 -2051 C ATOM 1905 CD1 LEU A1023 113.310 166.760 -28.224 1.00 53.51 C ANISOU 1905 CD1 LEU A1023 7705 4545 8080 25 -904 -2088 C ATOM 1906 CD2 LEU A1023 114.707 165.607 -26.492 1.00 51.26 C ANISOU 1906 CD2 LEU A1023 7279 4252 7945 -112 -493 -1883 C ATOM 1907 N LEU A1024 115.575 162.088 -29.002 1.00 54.83 N ANISOU 1907 N LEU A1024 8211 4496 8127 -69 -469 -2213 N ATOM 1908 CA LEU A1024 116.924 161.537 -28.964 1.00 54.13 C ANISOU 1908 CA LEU A1024 8247 4345 7975 -26 -244 -2145 C ATOM 1909 C LEU A1024 117.355 161.027 -30.333 1.00 56.47 C ANISOU 1909 C LEU A1024 8811 4569 8077 63 -231 -2286 C ATOM 1910 O LEU A1024 118.536 161.121 -30.686 1.00 56.19 O ANISOU 1910 O LEU A1024 8921 4490 7939 157 -45 -2247 O ATOM 1911 CB LEU A1024 116.990 160.425 -27.911 1.00 53.05 C ANISOU 1911 CB LEU A1024 7963 4192 8000 -117 -156 -2065 C ATOM 1912 CG LEU A1024 116.870 160.903 -26.454 1.00 50.25 C ANISOU 1912 CG LEU A1024 7361 3923 7810 -183 -102 -1902 C ATOM 1913 CD1 LEU A1024 116.639 159.751 -25.479 1.00 49.82 C ANISOU 1913 CD1 LEU A1024 7161 3858 7911 -267 -48 -1852 C ATOM 1914 CD2 LEU A1024 118.110 161.698 -26.049 1.00 48.21 C ANISOU 1914 CD2 LEU A1024 7110 3697 7510 -119 50 -1758 C ATOM 1915 N SER A1025 116.413 160.521 -31.133 1.00 58.94 N ANISOU 1915 N SER A1025 9176 4875 8344 44 -426 -2451 N ATOM 1916 CA SER A1025 116.764 160.046 -32.467 1.00 61.68 C ANISOU 1916 CA SER A1025 9777 5177 8482 139 -437 -2591 C ATOM 1917 C SER A1025 117.247 161.183 -33.361 1.00 62.53 C ANISOU 1917 C SER A1025 10090 5330 8339 306 -461 -2571 C ATOM 1918 O SER A1025 118.149 160.986 -34.183 1.00 63.31 O ANISOU 1918 O SER A1025 10411 5400 8245 423 -334 -2580 O ATOM 1919 CB SER A1025 115.562 159.349 -33.103 1.00 64.35 C ANISOU 1919 CB SER A1025 10126 5509 8816 83 -687 -2766 C ATOM 1920 OG SER A1025 115.857 158.920 -34.422 1.00 67.27 O ANISOU 1920 OG SER A1025 10760 5847 8953 185 -723 -2900 O ATOM 1921 N LYS A1026 116.676 162.382 -33.201 1.00 62.80 N ANISOU 1921 N LYS A1026 10070 5434 8358 330 -609 -2520 N ATOM 1922 CA LYS A1026 117.104 163.523 -34.008 1.00 64.28 C ANISOU 1922 CA LYS A1026 10496 5653 8276 494 -619 -2467 C ATOM 1923 C LYS A1026 118.544 163.904 -33.710 1.00 63.39 C ANISOU 1923 C LYS A1026 10449 5510 8126 556 -306 -2300 C ATOM 1924 O LYS A1026 119.297 164.279 -34.618 1.00 64.74 O ANISOU 1924 O LYS A1026 10887 5676 8037 696 -187 -2251 O ATOM 1925 CB LYS A1026 116.191 164.722 -33.753 1.00 64.28 C ANISOU 1925 CB LYS A1026 10401 5717 8307 500 -828 -2438 C ATOM 1926 CG LYS A1026 114.735 164.550 -34.173 1.00 66.42 C ANISOU 1926 CG LYS A1026 10607 6028 8601 468 -1164 -2589 C ATOM 1927 CD LYS A1026 113.905 165.772 -33.776 1.00 65.57 C ANISOU 1927 CD LYS A1026 10366 5978 8569 481 -1342 -2544 C ATOM 1928 CE LYS A1026 112.468 165.688 -34.265 1.00 67.40 C ANISOU 1928 CE LYS A1026 10527 6253 8830 473 -1691 -2689 C ATOM 1929 NZ LYS A1026 111.702 166.879 -33.798 1.00 66.42 N ANISOU 1929 NZ LYS A1026 10250 6175 8811 492 -1842 -2638 N ATOM 1930 N PHE A1027 118.947 163.792 -32.452 1.00 61.31 N ANISOU 1930 N PHE A1027 9946 5231 8118 453 -156 -2199 N ATOM 1931 CA PHE A1027 120.291 164.135 -32.017 1.00 59.90 C ANISOU 1931 CA PHE A1027 9772 5034 7954 487 133 -2024 C ATOM 1932 C PHE A1027 121.269 162.980 -32.163 1.00 60.94 C ANISOU 1932 C PHE A1027 9926 5122 8107 504 334 -2023 C ATOM 1933 O PHE A1027 122.434 163.124 -31.778 1.00 60.18 O ANISOU 1933 O PHE A1027 9781 5030 8055 525 574 -1866 O ATOM 1934 CB PHE A1027 120.271 164.613 -30.565 1.00 57.26 C ANISOU 1934 CB PHE A1027 9130 4746 7879 368 177 -1892 C ATOM 1935 CG PHE A1027 119.426 165.837 -30.341 1.00 56.85 C ANISOU 1935 CG PHE A1027 8989 4780 7831 352 13 -1848 C ATOM 1936 CD1 PHE A1027 119.886 167.090 -30.705 1.00 56.78 C ANISOU 1936 CD1 PHE A1027 9070 4831 7672 432 84 -1710 C ATOM 1937 CD2 PHE A1027 118.179 165.737 -29.744 1.00 56.91 C ANISOU 1937 CD2 PHE A1027 8818 4797 8010 259 -195 -1937 C ATOM 1938 CE1 PHE A1027 119.116 168.221 -30.490 1.00 56.60 C ANISOU 1938 CE1 PHE A1027 8972 4875 7657 426 -59 -1666 C ATOM 1939 CE2 PHE A1027 117.403 166.863 -29.525 1.00 56.80 C ANISOU 1939 CE2 PHE A1027 8716 4856 8011 256 -334 -1893 C ATOM 1940 CZ PHE A1027 117.873 168.108 -29.899 1.00 56.49 C ANISOU 1940 CZ PHE A1027 8780 4875 7810 343 -270 -1759 C ATOM 1941 N GLY A1028 120.822 161.845 -32.697 1.00 63.07 N ANISOU 1941 N GLY A1028 10246 5355 8362 492 235 -2187 N ATOM 1942 CA GLY A1028 121.675 160.682 -32.872 1.00 64.14 C ANISOU 1942 CA GLY A1028 10409 5441 8519 522 395 -2196 C ATOM 1943 C GLY A1028 121.965 159.925 -31.596 1.00 63.30 C ANISOU 1943 C GLY A1028 10049 5316 8685 434 450 -2121 C ATOM 1944 O GLY A1028 123.125 159.570 -31.345 1.00 62.70 O ANISOU 1944 O GLY A1028 9951 5237 8633 472 666 -1994 O ATOM 1945 N MET A1029 120.954 159.700 -30.758 1.00 63.24 N ANISOU 1945 N MET A1029 9882 5303 8844 328 257 -2157 N ATOM 1946 CA MET A1029 121.163 159.070 -29.462 1.00 62.63 C ANISOU 1946 CA MET A1029 9624 5238 8936 237 330 -2011 C ATOM 1947 C MET A1029 120.117 157.989 -29.195 1.00 63.09 C ANISOU 1947 C MET A1029 9666 5243 9062 132 199 -2090 C ATOM 1948 O MET A1029 118.986 158.038 -29.690 1.00 63.58 O ANISOU 1948 O MET A1029 9803 5285 9068 66 57 -2212 O ATOM 1949 CB MET A1029 121.131 160.107 -28.325 1.00 61.75 C ANISOU 1949 CB MET A1029 9310 5219 8932 164 365 -1848 C ATOM 1950 CG MET A1029 122.255 161.131 -28.376 1.00 61.94 C ANISOU 1950 CG MET A1029 9336 5286 8911 233 544 -1723 C ATOM 1951 SD MET A1029 122.264 162.253 -26.968 1.00 60.33 S ANISOU 1951 SD MET A1029 8894 5182 8848 145 564 -1546 S ATOM 1952 CE MET A1029 120.748 163.172 -27.226 1.00 61.23 C ANISOU 1952 CE MET A1029 9029 5311 8925 108 335 -1650 C ATOM 1953 N ASP A1030 120.523 157.014 -28.384 1.00 63.26 N ANISOU 1953 N ASP A1030 9563 5253 9222 91 298 -2009 N ATOM 1954 CA ASP A1030 119.661 155.940 -27.916 1.00 65.14 C ANISOU 1954 CA ASP A1030 9732 5446 9573 -18 229 -2049 C ATOM 1955 C ASP A1030 118.692 156.452 -26.855 1.00 62.64 C ANISOU 1955 C ASP A1030 9188 5215 9398 -140 166 -1976 C ATOM 1956 O ASP A1030 118.943 157.456 -26.184 1.00 61.45 O ANISOU 1956 O ASP A1030 8916 5156 9276 -139 209 -1856 O ATOM 1957 CB ASP A1030 120.496 154.804 -27.324 1.00 67.89 C ANISOU 1957 CB ASP A1030 10018 5753 10023 -3 377 -1971 C ATOM 1958 CG ASP A1030 121.587 154.313 -28.265 1.00 71.99 C ANISOU 1958 CG ASP A1030 10708 6208 10439 130 479 -2024 C ATOM 1959 OD1 ASP A1030 121.274 154.055 -29.446 1.00 74.28 O ANISOU 1959 OD1 ASP A1030 11200 6424 10598 186 376 -2194 O ATOM 1960 OD2 ASP A1030 122.754 154.177 -27.826 1.00 71.23 O ANISOU 1960 OD2 ASP A1030 10539 6134 10389 179 668 -1899 O ATOM 1961 N GLU A1031 117.569 155.748 -26.702 1.00 62.33 N ANISOU 1961 N GLU A1031 9082 5144 9459 -243 67 -2052 N ATOM 1962 CA GLU A1031 116.632 156.093 -25.641 1.00 60.00 C ANISOU 1962 CA GLU A1031 8548 4926 9325 -343 26 -1984 C ATOM 1963 C GLU A1031 117.314 155.974 -24.286 1.00 56.75 C ANISOU 1963 C GLU A1031 7987 4563 9015 -347 184 -1805 C ATOM 1964 O GLU A1031 118.086 155.043 -24.044 1.00 56.44 O ANISOU 1964 O GLU A1031 7977 4469 8997 -320 297 -1763 O ATOM 1965 CB GLU A1031 115.393 155.193 -25.691 1.00 62.03 C ANISOU 1965 CB GLU A1031 8735 5126 9707 -446 -81 -2096 C ATOM 1966 CG GLU A1031 114.563 155.363 -26.943 1.00 64.91 C ANISOU 1966 CG GLU A1031 9205 5463 9993 -458 -269 -2283 C ATOM 1967 CD GLU A1031 114.510 154.103 -27.777 1.00 68.74 C ANISOU 1967 CD GLU A1031 9855 5823 10440 -473 -302 -2427 C ATOM 1968 OE1 GLU A1031 115.582 153.587 -28.167 1.00 69.44 O ANISOU 1968 OE1 GLU A1031 10135 5840 10408 -393 -190 -2420 O ATOM 1969 OE2 GLU A1031 113.387 153.624 -28.036 1.00 71.11 O ANISOU 1969 OE2 GLU A1031 10085 6091 10842 -561 -443 -2550 O ATOM 1970 N GLY A1032 117.033 156.934 -23.410 1.00 54.26 N ANISOU 1970 N GLY A1032 7515 4346 8753 -375 189 -1704 N ATOM 1971 CA GLY A1032 117.598 156.960 -22.071 1.00 51.32 C ANISOU 1971 CA GLY A1032 7012 4031 8457 -380 323 -1542 C ATOM 1972 C GLY A1032 116.975 158.088 -21.277 1.00 48.93 C ANISOU 1972 C GLY A1032 6565 3827 8198 -414 291 -1474 C ATOM 1973 O GLY A1032 116.116 158.826 -21.770 1.00 49.14 O ANISOU 1973 O GLY A1032 6579 3878 8215 -432 170 -1547 O ATOM 1974 N VAL A1033 117.410 158.204 -20.021 1.00 46.10 N ANISOU 1974 N VAL A1033 6105 3522 7889 -417 399 -1337 N ATOM 1975 CA VAL A1033 116.952 159.289 -19.155 1.00 43.36 C ANISOU 1975 CA VAL A1033 5642 3264 7570 -437 390 -1263 C ATOM 1976 C VAL A1033 117.634 160.581 -19.592 1.00 42.03 C ANISOU 1976 C VAL A1033 5533 3149 7289 -385 368 -1234 C ATOM 1977 O VAL A1033 118.866 160.684 -19.564 1.00 41.45 O ANISOU 1977 O VAL A1033 5510 3081 7158 -335 450 -1167 O ATOM 1978 CB VAL A1033 117.241 158.970 -17.682 1.00 41.70 C ANISOU 1978 CB VAL A1033 5339 3079 7425 -448 510 -1138 C ATOM 1979 CG1 VAL A1033 118.679 158.508 -17.513 1.00 41.10 C ANISOU 1979 CG1 VAL A1033 5326 2986 7303 -394 610 -1064 C ATOM 1980 CG2 VAL A1033 116.958 160.185 -16.806 1.00 40.03 C ANISOU 1980 CG2 VAL A1033 5044 2953 7211 -452 508 -1063 C ATOM 1981 N THR A1034 116.834 161.576 -19.981 1.00 41.68 N ANISOU 1981 N THR A1034 5471 3137 7230 -394 264 -1284 N ATOM 1982 CA THR A1034 117.324 162.781 -20.643 1.00 32.53 C ANISOU 1982 CA THR A1034 4393 2002 5964 -342 230 -1282 C ATOM 1983 C THR A1034 117.340 163.969 -19.686 1.00 34.69 C ANISOU 1983 C THR A1034 4575 2355 6249 -348 255 -1178 C ATOM 1984 O THR A1034 116.332 164.264 -19.035 1.00 34.41 O ANISOU 1984 O THR A1034 4430 2353 6292 -386 219 -1174 O ATOM 1985 CB THR A1034 116.457 163.101 -21.862 1.00 33.79 C ANISOU 1985 CB THR A1034 4625 2127 6087 -332 83 -1422 C ATOM 1986 OG1 THR A1034 116.538 162.018 -22.797 1.00 35.29 O ANISOU 1986 OG1 THR A1034 4933 2236 6240 -322 57 -1530 O ATOM 1987 CG2 THR A1034 116.903 164.396 -22.543 1.00 33.40 C ANISOU 1987 CG2 THR A1034 4674 2088 5928 -268 56 -1420 C ATOM 1988 N PHE A1035 118.479 164.654 -19.620 1.00 30.21 N ANISOU 1988 N PHE A1035 4053 1810 5615 -308 321 -1099 N ATOM 1989 CA PHE A1035 118.637 165.889 -18.867 1.00 29.05 C ANISOU 1989 CA PHE A1035 3850 1727 5460 -310 335 -1012 C ATOM 1990 C PHE A1035 118.892 167.036 -19.837 1.00 31.30 C ANISOU 1990 C PHE A1035 4228 1996 5668 -267 296 -1035 C ATOM 1991 O PHE A1035 119.508 166.850 -20.892 1.00 31.83 O ANISOU 1991 O PHE A1035 4413 2007 5673 -220 315 -1079 O ATOM 1992 CB PHE A1035 119.797 165.796 -17.866 1.00 31.33 C ANISOU 1992 CB PHE A1035 4101 2047 5757 -306 441 -897 C ATOM 1993 CG PHE A1035 119.685 164.649 -16.902 1.00 31.49 C ANISOU 1993 CG PHE A1035 4057 2064 5844 -331 493 -867 C ATOM 1994 CD1 PHE A1035 120.153 163.388 -17.241 1.00 31.64 C ANISOU 1994 CD1 PHE A1035 4112 2028 5883 -318 542 -889 C ATOM 1995 CD2 PHE A1035 119.127 164.832 -15.645 1.00 31.33 C ANISOU 1995 CD2 PHE A1035 3955 2083 5866 -360 506 -816 C ATOM 1996 CE1 PHE A1035 120.055 162.331 -16.349 1.00 31.87 C ANISOU 1996 CE1 PHE A1035 4092 2038 5977 -336 599 -855 C ATOM 1997 CE2 PHE A1035 119.029 163.776 -14.751 1.00 31.48 C ANISOU 1997 CE2 PHE A1035 3936 2082 5945 -374 570 -785 C ATOM 1998 CZ PHE A1035 119.496 162.528 -15.104 1.00 31.79 C ANISOU 1998 CZ PHE A1035 4007 2064 6008 -364 614 -802 C ATOM 1999 N MET A1036 118.442 168.233 -19.471 1.00 31.03 N ANISOU 1999 N MET A1036 4154 1999 5636 -273 256 -1005 N ATOM 2000 CA MET A1036 118.546 169.367 -20.378 1.00 31.39 C ANISOU 2000 CA MET A1036 4293 2014 5618 -227 217 -1027 C ATOM 2001 C MET A1036 118.915 170.631 -19.613 1.00 31.15 C ANISOU 2001 C MET A1036 4223 2027 5587 -235 253 -927 C ATOM 2002 O MET A1036 118.383 170.896 -18.530 1.00 30.81 O ANISOU 2002 O MET A1036 4081 2037 5589 -270 244 -888 O ATOM 2003 CB MET A1036 117.232 169.560 -21.148 1.00 31.58 C ANISOU 2003 CB MET A1036 4337 2010 5652 -212 76 -1145 C ATOM 2004 CG MET A1036 117.054 170.923 -21.760 1.00 31.09 C ANISOU 2004 CG MET A1036 4347 1921 5547 -158 17 -1156 C ATOM 2005 SD MET A1036 115.313 171.253 -22.089 1.00 31.97 S ANISOU 2005 SD MET A1036 4391 2028 5729 -146 -176 -1271 S ATOM 2006 CE MET A1036 115.378 173.023 -22.363 1.00 31.60 C ANISOU 2006 CE MET A1036 4414 1951 5640 -74 -207 -1226 C ATOM 2007 N PHE A1037 119.837 171.402 -20.189 1.00 31.73 N ANISOU 2007 N PHE A1037 4380 2065 5610 -200 306 -889 N ATOM 2008 CA PHE A1037 120.252 172.700 -19.676 1.00 31.69 C ANISOU 2008 CA PHE A1037 4357 2080 5603 -209 336 -803 C ATOM 2009 C PHE A1037 120.004 173.729 -20.763 1.00 33.07 C ANISOU 2009 C PHE A1037 4648 2184 5732 -152 305 -834 C ATOM 2010 O PHE A1037 120.488 173.573 -21.888 1.00 33.15 O ANISOU 2010 O PHE A1037 4783 2121 5691 -98 352 -865 O ATOM 2011 CB PHE A1037 121.736 172.698 -19.274 1.00 31.92 C ANISOU 2011 CB PHE A1037 4362 2119 5646 -225 450 -711 C ATOM 2012 CG PHE A1037 122.301 174.072 -18.995 1.00 32.54 C ANISOU 2012 CG PHE A1037 4439 2198 5726 -237 480 -633 C ATOM 2013 CD1 PHE A1037 122.769 174.874 -20.028 1.00 33.76 C ANISOU 2013 CD1 PHE A1037 4696 2279 5853 -199 539 -613 C ATOM 2014 CD2 PHE A1037 122.384 174.555 -17.696 1.00 32.52 C ANISOU 2014 CD2 PHE A1037 4349 2257 5748 -284 460 -580 C ATOM 2015 CE1 PHE A1037 123.282 176.141 -19.772 1.00 33.66 C ANISOU 2015 CE1 PHE A1037 4678 2256 5853 -220 574 -537 C ATOM 2016 CE2 PHE A1037 122.902 175.814 -17.439 1.00 32.53 C ANISOU 2016 CE2 PHE A1037 4354 2252 5754 -302 477 -522 C ATOM 2017 CZ PHE A1037 123.346 176.605 -18.478 1.00 26.31 C ANISOU 2017 CZ PHE A1037 3648 1393 4955 -277 532 -497 C ATOM 2018 N ILE A1038 119.249 174.774 -20.436 1.00 34.87 N ANISOU 2018 N ILE A1038 4854 2422 5974 -151 241 -825 N ATOM 2019 CA ILE A1038 119.042 175.890 -21.352 1.00 36.72 C ANISOU 2019 CA ILE A1038 5203 2577 6174 -85 215 -835 C ATOM 2020 C ILE A1038 119.430 177.169 -20.630 1.00 36.90 C ANISOU 2020 C ILE A1038 5199 2614 6208 -112 263 -733 C ATOM 2021 O ILE A1038 118.924 177.449 -19.536 1.00 36.44 O ANISOU 2021 O ILE A1038 5040 2619 6185 -154 228 -714 O ATOM 2022 CB ILE A1038 117.596 175.975 -21.875 1.00 37.57 C ANISOU 2022 CB ILE A1038 5318 2680 6278 -33 53 -933 C ATOM 2023 CG1 ILE A1038 117.499 177.083 -22.932 1.00 38.97 C ANISOU 2023 CG1 ILE A1038 5642 2861 6305 67 9 -889 C ATOM 2024 CG2 ILE A1038 116.628 176.228 -20.732 1.00 36.80 C ANISOU 2024 CG2 ILE A1038 5071 2630 6281 -80 2 -934 C ATOM 2025 CD1 ILE A1038 116.597 176.765 -24.119 1.00 40.73 C ANISOU 2025 CD1 ILE A1038 5957 3099 6420 158 -153 -982 C ATOM 2026 N GLY A1039 120.320 177.935 -21.236 1.00 38.38 N ANISOU 2026 N GLY A1039 5485 2742 6356 -86 356 -664 N ATOM 2027 CA GLY A1039 120.761 179.180 -20.650 1.00 39.37 C ANISOU 2027 CA GLY A1039 5593 2862 6501 -118 401 -573 C ATOM 2028 C GLY A1039 122.078 179.617 -21.237 1.00 41.54 C ANISOU 2028 C GLY A1039 5942 3083 6759 -117 546 -483 C ATOM 2029 O GLY A1039 122.753 178.876 -21.951 1.00 42.11 O ANISOU 2029 O GLY A1039 6060 3158 6782 -91 622 -475 O ATOM 2030 N ARG A1040 122.439 180.853 -20.906 1.00 42.73 N ANISOU 2030 N ARG A1040 6094 3213 6928 -144 580 -406 N ATOM 2031 CA ARG A1040 123.690 181.437 -21.366 1.00 44.71 C ANISOU 2031 CA ARG A1040 6388 3410 7189 -159 727 -307 C ATOM 2032 C ARG A1040 124.880 180.770 -20.681 1.00 45.96 C ANISOU 2032 C ARG A1040 6404 3631 7426 -237 782 -279 C ATOM 2033 O ARG A1040 124.765 180.223 -19.578 1.00 45.30 O ANISOU 2033 O ARG A1040 6200 3636 7376 -287 696 -316 O ATOM 2034 CB ARG A1040 123.685 182.936 -21.083 1.00 45.42 C ANISOU 2034 CB ARG A1040 6498 3468 7292 -179 728 -243 C ATOM 2035 CG ARG A1040 124.784 183.745 -21.735 1.00 47.21 C ANISOU 2035 CG ARG A1040 6788 3619 7532 -187 886 -133 C ATOM 2036 CD ARG A1040 124.567 185.211 -21.407 1.00 48.92 C ANISOU 2036 CD ARG A1040 7027 3800 7758 -206 861 -88 C ATOM 2037 NE ARG A1040 125.770 186.022 -21.559 1.00 51.87 N ANISOU 2037 NE ARG A1040 7385 4130 8194 -262 992 10 N ATOM 2038 CZ ARG A1040 126.033 187.101 -20.826 1.00 53.95 C ANISOU 2038 CZ ARG A1040 7592 4392 8517 -332 963 31 C ATOM 2039 NH1 ARG A1040 125.176 187.483 -19.883 1.00 53.63 N ANISOU 2039 NH1 ARG A1040 7526 4390 8463 -345 820 -33 N ATOM 2040 NH2 ARG A1040 127.153 187.795 -21.027 1.00 56.17 N ANISOU 2040 NH2 ARG A1040 7845 4625 8872 -387 1083 111 N ATOM 2041 N PHE A1041 126.031 180.798 -21.356 1.00 47.46 N ANISOU 2041 N PHE A1041 6620 3767 7647 -235 939 -206 N ATOM 2042 CA PHE A1041 127.275 180.271 -20.789 1.00 48.28 C ANISOU 2042 CA PHE A1041 6576 3909 7858 -299 1002 -170 C ATOM 2043 C PHE A1041 127.998 181.406 -20.062 1.00 49.55 C ANISOU 2043 C PHE A1041 6644 4080 8105 -379 1001 -110 C ATOM 2044 O PHE A1041 128.641 182.250 -20.688 1.00 50.06 O ANISOU 2044 O PHE A1041 6746 4075 8200 -384 1123 -32 O ATOM 2045 CB PHE A1041 128.139 179.640 -21.876 1.00 49.01 C ANISOU 2045 CB PHE A1041 6728 3935 7961 -249 1186 -126 C ATOM 2046 CG PHE A1041 127.554 178.373 -22.463 1.00 48.80 C ANISOU 2046 CG PHE A1041 6785 3918 7838 -172 1167 -207 C ATOM 2047 CD1 PHE A1041 126.325 177.893 -22.033 1.00 47.62 C ANISOU 2047 CD1 PHE A1041 6639 3812 7644 -166 1001 -309 C ATOM 2048 CD2 PHE A1041 128.237 177.660 -23.437 1.00 49.70 C ANISOU 2048 CD2 PHE A1041 6967 4019 7898 -104 1310 -183 C ATOM 2049 CE1 PHE A1041 125.784 176.736 -22.567 1.00 47.67 C ANISOU 2049 CE1 PHE A1041 6707 3843 7564 -106 962 -393 C ATOM 2050 CE2 PHE A1041 127.697 176.498 -23.974 1.00 49.76 C ANISOU 2050 CE2 PHE A1041 7058 4054 7796 -34 1270 -271 C ATOM 2051 CZ PHE A1041 126.473 176.038 -23.538 1.00 48.86 C ANISOU 2051 CZ PHE A1041 6938 3977 7648 -41 1088 -379 C ATOM 2052 N ASP A1042 127.898 181.412 -18.729 1.00 50.89 N ANISOU 2052 N ASP A1042 6702 4329 8304 -438 869 -148 N ATOM 2053 CA ASP A1042 128.264 182.523 -17.855 1.00 52.95 C ANISOU 2053 CA ASP A1042 6906 4599 8612 -508 813 -128 C ATOM 2054 C ASP A1042 129.334 182.121 -16.847 1.00 54.28 C ANISOU 2054 C ASP A1042 6922 4813 8888 -572 780 -124 C ATOM 2055 O ASP A1042 129.565 180.939 -16.581 1.00 54.74 O ANISOU 2055 O ASP A1042 6915 4911 8971 -558 771 -143 O ATOM 2056 CB ASP A1042 127.042 183.031 -17.082 1.00 52.90 C ANISOU 2056 CB ASP A1042 6951 4629 8520 -503 677 -184 C ATOM 2057 CG ASP A1042 126.114 183.852 -17.933 1.00 54.35 C ANISOU 2057 CG ASP A1042 7269 4747 8633 -447 693 -177 C ATOM 2058 OD1 ASP A1042 126.596 184.788 -18.607 1.00 56.16 O ANISOU 2058 OD1 ASP A1042 7552 4900 8888 -451 783 -112 O ATOM 2059 OD2 ASP A1042 124.898 183.568 -17.920 1.00 54.02 O ANISOU 2059 OD2 ASP A1042 7278 4726 8522 -396 618 -232 O ATOM 2060 N ARG A1043 129.959 183.134 -16.239 1.00 56.06 N ANISOU 2060 N ARG A1043 7096 5023 9180 -640 748 -105 N ATOM 2061 CA ARG A1043 130.954 182.889 -15.199 1.00 56.52 C ANISOU 2061 CA ARG A1043 7017 5111 9347 -702 683 -111 C ATOM 2062 C ARG A1043 130.300 182.599 -13.853 1.00 55.79 C ANISOU 2062 C ARG A1043 6939 5079 9180 -710 529 -178 C ATOM 2063 O ARG A1043 130.470 181.512 -13.290 1.00 55.96 O ANISOU 2063 O ARG A1043 6902 5141 9221 -697 489 -195 O ATOM 2064 CB ARG A1043 131.891 184.087 -15.085 1.00 59.36 C ANISOU 2064 CB ARG A1043 7319 5416 9817 -778 700 -75 C ATOM 2065 CG ARG A1043 132.825 184.233 -16.262 1.00 61.31 C ANISOU 2065 CG ARG A1043 7516 5601 10178 -776 879 5 C ATOM 2066 CD ARG A1043 134.021 183.322 -16.114 1.00 64.08 C ANISOU 2066 CD ARG A1043 7694 5964 10688 -789 918 31 C ATOM 2067 NE ARG A1043 135.027 183.625 -17.123 1.00 68.08 N ANISOU 2067 NE ARG A1043 8136 6404 11328 -794 1107 114 N ATOM 2068 CZ ARG A1043 136.281 183.188 -17.089 1.00 72.23 C ANISOU 2068 CZ ARG A1043 8482 6918 12043 -815 1168 154 C ATOM 2069 NH1 ARG A1043 137.122 183.520 -18.058 1.00 74.60 N ANISOU 2069 NH1 ARG A1043 8733 7152 12460 -811 1368 236 N ATOM 2070 NH2 ARG A1043 136.698 182.427 -16.087 1.00 73.20 N ANISOU 2070 NH2 ARG A1043 8477 7089 12246 -832 1037 118 N ATOM 2071 N GLY A1044 129.549 183.559 -13.322 1.00 56.16 N ANISOU 2071 N GLY A1044 7073 5119 9144 -725 456 -210 N ATOM 2072 CA GLY A1044 128.873 183.369 -12.053 1.00 55.14 C ANISOU 2072 CA GLY A1044 6982 5032 8937 -726 340 -269 C ATOM 2073 C GLY A1044 127.369 183.208 -11.935 1.00 53.38 C ANISOU 2073 C GLY A1044 6876 4820 8585 -673 326 -301 C ATOM 2074 O GLY A1044 126.822 183.235 -10.829 1.00 54.36 O ANISOU 2074 O GLY A1044 7066 4932 8658 -688 265 -335 O ATOM 2075 N GLN A1045 126.684 183.040 -13.065 1.00 49.84 N ANISOU 2075 N GLN A1045 6454 4386 8097 -609 381 -296 N ATOM 2076 CA GLN A1045 125.249 183.251 -13.212 1.00 45.80 C ANISOU 2076 CA GLN A1045 6027 3881 7496 -555 361 -329 C ATOM 2077 C GLN A1045 124.517 181.927 -13.414 1.00 41.74 C ANISOU 2077 C GLN A1045 5496 3415 6948 -504 363 -357 C ATOM 2078 O GLN A1045 124.112 181.285 -12.438 1.00 40.79 O ANISOU 2078 O GLN A1045 5357 3338 6803 -503 321 -387 O ATOM 2079 CB GLN A1045 124.967 184.215 -14.369 1.00 45.33 C ANISOU 2079 CB GLN A1045 6039 3752 7431 -528 413 -299 C ATOM 2080 CG GLN A1045 125.367 185.673 -14.097 1.00 45.33 C ANISOU 2080 CG GLN A1045 6076 3693 7456 -574 409 -277 C ATOM 2081 CD GLN A1045 126.722 186.058 -14.689 1.00 44.42 C ANISOU 2081 CD GLN A1045 5915 3529 7435 -625 487 -217 C ATOM 2082 OE1 GLN A1045 127.743 185.401 -14.441 1.00 44.44 O ANISOU 2082 OE1 GLN A1045 5817 3558 7510 -665 498 -206 O ATOM 2083 NE2 GLN A1045 126.736 187.134 -15.471 1.00 44.07 N ANISOU 2083 NE2 GLN A1045 5939 3403 7402 -619 550 -172 N ATOM 2084 N LYS A1046 124.360 181.498 -14.669 1.00 39.20 N ANISOU 2084 N LYS A1046 5193 3072 6629 -462 416 -350 N ATOM 2085 CA LYS A1046 123.509 180.357 -15.008 1.00 36.02 C ANISOU 2085 CA LYS A1046 4791 2699 6197 -416 406 -392 C ATOM 2086 C LYS A1046 124.094 178.992 -14.638 1.00 35.22 C ANISOU 2086 C LYS A1046 4618 2640 6126 -426 421 -395 C ATOM 2087 O LYS A1046 123.342 178.012 -14.615 1.00 35.10 O ANISOU 2087 O LYS A1046 4594 2652 6090 -400 405 -434 O ATOM 2088 CB LYS A1046 123.175 180.374 -16.503 1.00 35.23 C ANISOU 2088 CB LYS A1046 4763 2539 6084 -364 446 -397 C ATOM 2089 CG LYS A1046 122.312 181.549 -16.933 1.00 35.24 C ANISOU 2089 CG LYS A1046 4848 2486 6057 -327 420 -401 C ATOM 2090 CD LYS A1046 121.173 181.750 -15.958 1.00 36.41 C ANISOU 2090 CD LYS A1046 4971 2675 6186 -323 345 -443 C ATOM 2091 CE LYS A1046 120.463 183.073 -16.168 1.00 39.26 C ANISOU 2091 CE LYS A1046 5403 2976 6539 -288 325 -438 C ATOM 2092 NZ LYS A1046 119.813 183.509 -14.899 1.00 41.30 N ANISOU 2092 NZ LYS A1046 5633 3267 6792 -302 289 -460 N ATOM 2093 N GLY A1047 125.391 178.883 -14.356 1.00 35.02 N ANISOU 2093 N GLY A1047 4533 2609 6163 -462 452 -355 N ATOM 2094 CA GLY A1047 125.914 177.644 -13.804 1.00 34.56 C ANISOU 2094 CA GLY A1047 4407 2579 6144 -465 455 -354 C ATOM 2095 C GLY A1047 126.271 176.525 -14.762 1.00 34.80 C ANISOU 2095 C GLY A1047 4422 2591 6208 -430 530 -353 C ATOM 2096 O GLY A1047 126.438 175.385 -14.315 1.00 34.63 O ANISOU 2096 O GLY A1047 4358 2587 6211 -420 532 -360 O ATOM 2097 N VAL A1048 126.425 176.800 -16.060 1.00 35.16 N ANISOU 2097 N VAL A1048 4518 2585 6255 -406 604 -344 N ATOM 2098 CA VAL A1048 126.877 175.739 -16.960 1.00 35.76 C ANISOU 2098 CA VAL A1048 4601 2625 6359 -368 695 -347 C ATOM 2099 C VAL A1048 128.253 175.226 -16.553 1.00 36.15 C ANISOU 2099 C VAL A1048 4543 2667 6525 -386 755 -296 C ATOM 2100 O VAL A1048 128.595 174.069 -16.828 1.00 36.58 O ANISOU 2100 O VAL A1048 4579 2705 6615 -352 813 -302 O ATOM 2101 CB VAL A1048 126.899 176.217 -18.424 1.00 36.66 C ANISOU 2101 CB VAL A1048 4821 2662 6445 -329 787 -339 C ATOM 2102 CG1 VAL A1048 128.137 177.061 -18.684 1.00 28.03 C ANISOU 2102 CG1 VAL A1048 3693 1521 5435 -356 894 -256 C ATOM 2103 CG2 VAL A1048 126.860 175.023 -19.371 1.00 27.64 C ANISOU 2103 CG2 VAL A1048 3743 1481 5278 -269 856 -380 C ATOM 2104 N ASP A1049 129.080 176.075 -15.932 1.00 35.48 N ANISOU 2104 N ASP A1049 4383 2583 6516 -436 740 -249 N ATOM 2105 CA ASP A1049 130.385 175.603 -15.482 1.00 35.59 C ANISOU 2105 CA ASP A1049 4269 2580 6672 -453 773 -203 C ATOM 2106 C ASP A1049 130.239 174.551 -14.392 1.00 33.59 C ANISOU 2106 C ASP A1049 3974 2363 6424 -443 693 -224 C ATOM 2107 O ASP A1049 131.062 173.628 -14.303 1.00 33.27 O ANISOU 2107 O ASP A1049 3855 2296 6492 -422 739 -196 O ATOM 2108 CB ASP A1049 131.241 176.780 -14.995 1.00 37.28 C ANISOU 2108 CB ASP A1049 4404 2784 6977 -518 744 -161 C ATOM 2109 CG ASP A1049 130.576 177.574 -13.894 1.00 38.22 C ANISOU 2109 CG ASP A1049 4561 2944 7016 -558 601 -197 C ATOM 2110 OD1 ASP A1049 129.331 177.566 -13.826 1.00 38.23 O ANISOU 2110 OD1 ASP A1049 4662 2976 6885 -533 557 -241 O ATOM 2111 OD2 ASP A1049 131.306 178.211 -13.099 1.00 39.65 O ANISOU 2111 OD2 ASP A1049 4671 3118 7276 -615 534 -183 O ATOM 2112 N VAL A1050 129.180 174.657 -13.578 1.00 32.09 N ANISOU 2112 N VAL A1050 3844 2220 6127 -451 591 -266 N ATOM 2113 CA VAL A1050 128.877 173.631 -12.585 1.00 31.18 C ANISOU 2113 CA VAL A1050 3720 2124 6001 -435 540 -280 C ATOM 2114 C VAL A1050 128.367 172.371 -13.256 1.00 31.24 C ANISOU 2114 C VAL A1050 3762 2128 5978 -384 603 -307 C ATOM 2115 O VAL A1050 128.683 171.257 -12.831 1.00 31.98 O ANISOU 2115 O VAL A1050 3823 2205 6123 -359 618 -294 O ATOM 2116 CB VAL A1050 127.843 174.147 -11.578 1.00 30.21 C ANISOU 2116 CB VAL A1050 3664 2039 5778 -455 448 -312 C ATOM 2117 CG1 VAL A1050 127.467 173.049 -10.600 1.00 29.73 C ANISOU 2117 CG1 VAL A1050 3613 1979 5705 -434 426 -318 C ATOM 2118 CG2 VAL A1050 128.355 175.370 -10.864 1.00 30.96 C ANISOU 2118 CG2 VAL A1050 3745 2124 5896 -507 379 -300 C ATOM 2119 N LEU A1051 127.518 172.519 -14.271 1.00 30.50 N ANISOU 2119 N LEU A1051 3744 2039 5804 -367 628 -348 N ATOM 2120 CA LEU A1051 127.028 171.333 -14.956 1.00 30.11 C ANISOU 2120 CA LEU A1051 3735 1977 5730 -326 671 -389 C ATOM 2121 C LEU A1051 128.164 170.605 -15.662 1.00 31.17 C ANISOU 2121 C LEU A1051 3839 2054 5951 -291 782 -362 C ATOM 2122 O LEU A1051 128.211 169.371 -15.649 1.00 32.34 O ANISOU 2122 O LEU A1051 3984 2184 6120 -259 815 -375 O ATOM 2123 CB LEU A1051 125.932 171.707 -15.946 1.00 29.64 C ANISOU 2123 CB LEU A1051 3765 1915 5581 -314 653 -447 C ATOM 2124 CG LEU A1051 125.392 170.568 -16.804 1.00 29.73 C ANISOU 2124 CG LEU A1051 3832 1899 5564 -277 676 -510 C ATOM 2125 CD1 LEU A1051 124.659 169.558 -15.941 1.00 25.84 C ANISOU 2125 CD1 LEU A1051 3308 1438 5071 -287 632 -533 C ATOM 2126 CD2 LEU A1051 124.481 171.117 -17.883 1.00 26.36 C ANISOU 2126 CD2 LEU A1051 3502 1449 5065 -259 641 -571 C ATOM 2127 N LEU A1052 129.111 171.347 -16.247 1.00 30.92 N ANISOU 2127 N LEU A1052 3781 1983 5982 -295 855 -318 N ATOM 2128 CA LEU A1052 130.227 170.698 -16.929 1.00 31.51 C ANISOU 2128 CA LEU A1052 3821 1994 6160 -253 993 -282 C ATOM 2129 C LEU A1052 131.142 170.002 -15.932 1.00 31.71 C ANISOU 2129 C LEU A1052 3719 2010 6318 -250 985 -232 C ATOM 2130 O LEU A1052 131.658 168.909 -16.207 1.00 32.15 O ANISOU 2130 O LEU A1052 3757 2022 6439 -196 1071 -221 O ATOM 2131 CB LEU A1052 131.011 171.717 -17.755 1.00 32.39 C ANISOU 2131 CB LEU A1052 3927 2056 6324 -260 1099 -231 C ATOM 2132 CG LEU A1052 130.266 172.395 -18.898 1.00 32.66 C ANISOU 2132 CG LEU A1052 4110 2065 6233 -242 1134 -265 C ATOM 2133 CD1 LEU A1052 131.193 173.370 -19.598 1.00 30.03 C ANISOU 2133 CD1 LEU A1052 3771 1671 5969 -247 1271 -189 C ATOM 2134 CD2 LEU A1052 129.731 171.349 -19.867 1.00 33.07 C ANISOU 2134 CD2 LEU A1052 4290 2082 6194 -170 1186 -334 C ATOM 2135 N LYS A1053 131.358 170.628 -14.770 1.00 31.22 N ANISOU 2135 N LYS A1053 3582 1979 6300 -300 877 -203 N ATOM 2136 CA LYS A1053 132.121 169.974 -13.717 1.00 28.70 C ANISOU 2136 CA LYS A1053 3160 1638 6106 -291 835 -158 C ATOM 2137 C LYS A1053 131.396 168.749 -13.204 1.00 28.29 C ANISOU 2137 C LYS A1053 3167 1594 5986 -253 809 -187 C ATOM 2138 O LYS A1053 132.036 167.756 -12.840 1.00 30.40 O ANISOU 2138 O LYS A1053 3381 1815 6355 -207 837 -148 O ATOM 2139 CB LYS A1053 132.383 170.940 -12.567 1.00 28.70 C ANISOU 2139 CB LYS A1053 3101 1660 6144 -355 701 -138 C ATOM 2140 CG LYS A1053 133.204 172.149 -12.936 1.00 33.06 C ANISOU 2140 CG LYS A1053 3573 2201 6788 -406 718 -106 C ATOM 2141 CD LYS A1053 133.654 172.884 -11.677 1.00 33.46 C ANISOU 2141 CD LYS A1053 3551 2257 6907 -469 564 -94 C ATOM 2142 CE LYS A1053 134.254 174.240 -12.014 1.00 34.10 C ANISOU 2142 CE LYS A1053 3569 2338 7048 -534 567 -77 C ATOM 2143 NZ LYS A1053 134.526 175.048 -10.794 1.00 34.51 N ANISOU 2143 NZ LYS A1053 3582 2397 7135 -603 395 -91 N ATOM 2144 N ALA A1054 130.065 168.796 -13.186 1.00 27.42 N ANISOU 2144 N ALA A1054 3161 1535 5721 -268 762 -247 N ATOM 2145 CA ALA A1054 129.300 167.633 -12.768 1.00 37.94 C ANISOU 2145 CA ALA A1054 4545 2871 7001 -242 755 -272 C ATOM 2146 C ALA A1054 129.438 166.508 -13.779 1.00 37.63 C ANISOU 2146 C ALA A1054 4530 2790 6976 -190 859 -294 C ATOM 2147 O ALA A1054 129.623 165.347 -13.401 1.00 38.85 O ANISOU 2147 O ALA A1054 4678 2910 7173 -152 889 -277 O ATOM 2148 CB ALA A1054 127.831 168.005 -12.568 1.00 26.40 C ANISOU 2148 CB ALA A1054 3160 1465 5404 -274 691 -328 C ATOM 2149 N ILE A1055 129.392 166.834 -15.072 1.00 36.81 N ANISOU 2149 N ILE A1055 4473 2678 6837 -182 920 -331 N ATOM 2150 CA ILE A1055 129.466 165.781 -16.078 1.00 37.51 C ANISOU 2150 CA ILE A1055 4618 2718 6918 -129 1016 -367 C ATOM 2151 C ILE A1055 130.839 165.113 -16.055 1.00 37.96 C ANISOU 2151 C ILE A1055 4595 2712 7115 -72 1123 -301 C ATOM 2152 O ILE A1055 130.956 163.918 -16.343 1.00 38.58 O ANISOU 2152 O ILE A1055 4705 2750 7204 -20 1189 -315 O ATOM 2153 CB ILE A1055 129.103 166.337 -17.472 1.00 37.69 C ANISOU 2153 CB ILE A1055 4740 2726 6856 -121 1056 -424 C ATOM 2154 CG1 ILE A1055 127.606 166.680 -17.526 1.00 36.82 C ANISOU 2154 CG1 ILE A1055 4701 2662 6626 -160 939 -498 C ATOM 2155 CG2 ILE A1055 129.462 165.340 -18.565 1.00 38.74 C ANISOU 2155 CG2 ILE A1055 4947 2792 6982 -53 1175 -459 C ATOM 2156 CD1 ILE A1055 127.135 167.250 -18.855 1.00 37.19 C ANISOU 2156 CD1 ILE A1055 4864 2683 6585 -142 949 -559 C ATOM 2157 N GLU A1056 131.894 165.851 -15.702 1.00 37.81 N ANISOU 2157 N GLU A1056 4466 2679 7221 -78 1138 -226 N ATOM 2158 CA GLU A1056 133.209 165.227 -15.574 1.00 38.60 C ANISOU 2158 CA GLU A1056 4458 2715 7495 -17 1227 -151 C ATOM 2159 C GLU A1056 133.232 164.218 -14.432 1.00 38.26 C ANISOU 2159 C GLU A1056 4382 2660 7495 12 1163 -120 C ATOM 2160 O GLU A1056 133.885 163.173 -14.530 1.00 39.30 O ANISOU 2160 O GLU A1056 4483 2739 7712 90 1246 -86 O ATOM 2161 CB GLU A1056 134.271 166.301 -15.360 1.00 39.17 C ANISOU 2161 CB GLU A1056 4391 2767 7725 -46 1230 -77 C ATOM 2162 CG GLU A1056 134.379 167.313 -16.495 1.00 39.56 C ANISOU 2162 CG GLU A1056 4476 2809 7747 -69 1327 -84 C ATOM 2163 CD GLU A1056 135.409 166.915 -17.530 1.00 41.45 C ANISOU 2163 CD GLU A1056 4682 2977 8092 10 1533 -40 C ATOM 2164 OE1 GLU A1056 135.876 165.757 -17.487 1.00 42.47 O ANISOU 2164 OE1 GLU A1056 4779 3069 8288 90 1598 -22 O ATOM 2165 OE2 GLU A1056 135.755 167.763 -18.380 1.00 42.30 O ANISOU 2165 OE2 GLU A1056 4798 3081 8192 0 1636 -16 O ATOM 2166 N ILE A1057 132.509 164.508 -13.347 1.00 37.05 N ANISOU 2166 N ILE A1057 4249 2549 7277 -39 1028 -128 N ATOM 2167 CA ILE A1057 132.449 163.598 -12.204 1.00 36.55 C ANISOU 2167 CA ILE A1057 4187 2461 7238 -7 977 -90 C ATOM 2168 C ILE A1057 131.718 162.318 -12.584 1.00 36.68 C ANISOU 2168 C ILE A1057 4301 2467 7169 24 1041 -136 C ATOM 2169 O ILE A1057 132.212 161.206 -12.360 1.00 37.59 O ANISOU 2169 O ILE A1057 4404 2526 7351 93 1093 -93 O ATOM 2170 CB ILE A1057 131.755 164.283 -11.011 1.00 35.51 C ANISOU 2170 CB ILE A1057 4087 2368 7036 -66 842 -91 C ATOM 2171 CG1 ILE A1057 132.556 165.480 -10.496 1.00 34.95 C ANISOU 2171 CG1 ILE A1057 3921 2293 7066 -104 753 -49 C ATOM 2172 CG2 ILE A1057 131.470 163.280 -9.905 1.00 36.37 C ANISOU 2172 CG2 ILE A1057 4244 2439 7134 -27 815 -53 C ATOM 2173 CD1 ILE A1057 131.831 166.301 -9.426 1.00 33.54 C ANISOU 2173 CD1 ILE A1057 3802 2151 6793 -166 626 -68 C ATOM 2174 N LEU A1058 130.525 162.461 -13.169 1.00 36.13 N ANISOU 2174 N LEU A1058 4324 2443 6960 -25 1029 -223 N ATOM 2175 CA LEU A1058 129.714 161.305 -13.533 1.00 36.56 C ANISOU 2175 CA LEU A1058 4463 2480 6950 -16 1065 -279 C ATOM 2176 C LEU A1058 130.352 160.479 -14.647 1.00 39.17 C ANISOU 2176 C LEU A1058 4815 2753 7316 46 1182 -298 C ATOM 2177 O LEU A1058 130.111 159.271 -14.727 1.00 40.36 O ANISOU 2177 O LEU A1058 5015 2859 7460 72 1223 -318 O ATOM 2178 CB LEU A1058 128.305 161.765 -13.939 1.00 35.06 C ANISOU 2178 CB LEU A1058 4341 2344 6635 -82 1002 -367 C ATOM 2179 CG LEU A1058 127.377 162.396 -12.886 1.00 33.53 C ANISOU 2179 CG LEU A1058 4146 2204 6390 -137 910 -361 C ATOM 2180 CD1 LEU A1058 126.125 163.050 -13.500 1.00 32.70 C ANISOU 2180 CD1 LEU A1058 4082 2151 6191 -187 853 -442 C ATOM 2181 CD2 LEU A1058 126.964 161.379 -11.826 1.00 33.67 C ANISOU 2181 CD2 LEU A1058 4181 2187 6424 -129 920 -329 C ATOM 2182 N SER A1059 131.183 161.090 -15.495 1.00 40.39 N ANISOU 2182 N SER A1059 4940 2898 7510 72 1250 -288 N ATOM 2183 CA SER A1059 131.622 160.402 -16.706 1.00 42.95 C ANISOU 2183 CA SER A1059 5320 3167 7831 134 1377 -322 C ATOM 2184 C SER A1059 132.451 159.166 -16.396 1.00 43.87 C ANISOU 2184 C SER A1059 5399 3221 8047 213 1459 -265 C ATOM 2185 O SER A1059 132.532 158.262 -17.241 1.00 44.04 O ANISOU 2185 O SER A1059 5499 3194 8040 262 1552 -309 O ATOM 2186 CB SER A1059 132.409 161.356 -17.613 1.00 44.77 C ANISOU 2186 CB SER A1059 5528 3390 8091 155 1467 -304 C ATOM 2187 OG SER A1059 133.421 162.038 -16.904 1.00 46.10 O ANISOU 2187 OG SER A1059 5547 3560 8410 160 1467 -205 O ATOM 2188 N SER A1060 133.069 159.112 -15.212 1.00 43.72 N ANISOU 2188 N SER A1060 5272 3197 8142 236 1420 -169 N ATOM 2189 CA SER A1060 133.895 157.982 -14.803 1.00 44.27 C ANISOU 2189 CA SER A1060 5298 3206 8318 326 1483 -97 C ATOM 2190 C SER A1060 133.083 156.820 -14.226 1.00 44.07 C ANISOU 2190 C SER A1060 5361 3153 8231 321 1453 -117 C ATOM 2191 O SER A1060 133.670 155.786 -13.886 1.00 44.45 O ANISOU 2191 O SER A1060 5395 3142 8352 400 1506 -58 O ATOM 2192 CB SER A1060 134.979 158.446 -13.810 1.00 43.99 C ANISOU 2192 CB SER A1060 5105 3164 8447 370 1435 22 C ATOM 2193 OG SER A1060 134.481 159.290 -12.786 1.00 42.86 O ANISOU 2193 OG SER A1060 4946 3060 8279 301 1289 35 O ATOM 2194 N LYS A1061 131.764 156.961 -14.096 1.00 44.11 N ANISOU 2194 N LYS A1061 5448 3194 8120 235 1377 -191 N ATOM 2195 CA LYS A1061 130.896 155.903 -13.593 1.00 46.04 C ANISOU 2195 CA LYS A1061 5766 3404 8324 218 1364 -211 C ATOM 2196 C LYS A1061 130.162 155.202 -14.734 1.00 47.13 C ANISOU 2196 C LYS A1061 6004 3512 8392 193 1404 -325 C ATOM 2197 O LYS A1061 129.858 155.804 -15.769 1.00 47.08 O ANISOU 2197 O LYS A1061 6035 3534 8318 164 1393 -406 O ATOM 2198 CB LYS A1061 129.901 156.473 -12.573 1.00 47.19 C ANISOU 2198 CB LYS A1061 5918 3599 8413 143 1261 -207 C ATOM 2199 CG LYS A1061 130.592 156.985 -11.307 1.00 49.39 C ANISOU 2199 CG LYS A1061 6132 3881 8754 176 1208 -97 C ATOM 2200 CD LYS A1061 129.786 158.016 -10.530 1.00 50.46 C ANISOU 2200 CD LYS A1061 6275 4076 8820 103 1109 -104 C ATOM 2201 CE LYS A1061 130.595 158.565 -9.346 1.00 53.35 C ANISOU 2201 CE LYS A1061 6592 4427 9251 143 1040 -2 C ATOM 2202 NZ LYS A1061 129.926 159.710 -8.655 1.00 54.69 N ANISOU 2202 NZ LYS A1061 6781 4648 9349 73 947 -16 N ATOM 2203 N LYS A1062 129.883 153.910 -14.529 1.00 48.67 N ANISOU 2203 N LYS A1062 6252 3636 8605 211 1444 -331 N ATOM 2204 CA LYS A1062 129.163 153.123 -15.528 1.00 49.79 C ANISOU 2204 CA LYS A1062 6491 3728 8698 185 1465 -445 C ATOM 2205 C LYS A1062 127.736 153.620 -15.729 1.00 48.48 C ANISOU 2205 C LYS A1062 6355 3608 8456 84 1362 -539 C ATOM 2206 O LYS A1062 127.183 153.483 -16.825 1.00 48.75 O ANISOU 2206 O LYS A1062 6464 3622 8437 60 1340 -651 O ATOM 2207 CB LYS A1062 129.140 151.649 -15.117 1.00 51.71 C ANISOU 2207 CB LYS A1062 6775 3875 8998 217 1528 -423 C ATOM 2208 CG LYS A1062 129.825 150.690 -16.083 1.00 54.19 C ANISOU 2208 CG LYS A1062 7154 4103 9332 291 1630 -459 C ATOM 2209 CD LYS A1062 129.776 149.260 -15.566 1.00 56.49 C ANISOU 2209 CD LYS A1062 7485 4292 9687 321 1690 -429 C ATOM 2210 CE LYS A1062 130.510 148.309 -16.505 1.00 58.95 C ANISOU 2210 CE LYS A1062 7866 4514 10020 403 1797 -464 C ATOM 2211 NZ LYS A1062 130.416 146.885 -16.058 1.00 60.82 N ANISOU 2211 NZ LYS A1062 8151 4637 10320 430 1857 -441 N ATOM 2212 N GLU A1063 127.125 154.190 -14.688 1.00 47.58 N ANISOU 2212 N GLU A1063 6188 3550 8340 31 1297 -496 N ATOM 2213 CA GLU A1063 125.754 154.677 -14.780 1.00 47.33 C ANISOU 2213 CA GLU A1063 6164 3564 8257 -57 1208 -571 C ATOM 2214 C GLU A1063 125.629 155.839 -15.758 1.00 46.54 C ANISOU 2214 C GLU A1063 6074 3527 8083 -75 1144 -637 C ATOM 2215 O GLU A1063 124.524 156.114 -16.241 1.00 46.35 O ANISOU 2215 O GLU A1063 6073 3521 8017 -132 1066 -724 O ATOM 2216 CB GLU A1063 125.257 155.084 -13.394 1.00 47.93 C ANISOU 2216 CB GLU A1063 6186 3681 8345 -91 1178 -498 C ATOM 2217 CG GLU A1063 125.223 153.945 -12.369 1.00 50.61 C ANISOU 2217 CG GLU A1063 6537 3945 8747 -71 1248 -429 C ATOM 2218 CD GLU A1063 126.606 153.551 -11.848 1.00 53.50 C ANISOU 2218 CD GLU A1063 6900 4269 9160 22 1309 -322 C ATOM 2219 OE1 GLU A1063 127.477 154.441 -11.704 1.00 54.18 O ANISOU 2219 OE1 GLU A1063 6942 4403 9243 58 1281 -271 O ATOM 2220 OE2 GLU A1063 126.821 152.345 -11.585 1.00 55.60 O ANISOU 2220 OE2 GLU A1063 7201 4447 9478 63 1383 -287 O ATOM 2221 N PHE A1064 126.742 156.519 -16.060 1.00 46.13 N ANISOU 2221 N PHE A1064 6002 3497 8026 -24 1180 -594 N ATOM 2222 CA PHE A1064 126.728 157.656 -16.976 1.00 45.19 C ANISOU 2222 CA PHE A1064 5905 3425 7840 -32 1141 -642 C ATOM 2223 C PHE A1064 126.256 157.264 -18.371 1.00 45.57 C ANISOU 2223 C PHE A1064 6067 3425 7822 -26 1132 -764 C ATOM 2224 O PHE A1064 125.758 158.116 -19.117 1.00 45.17 O ANISOU 2224 O PHE A1064 6062 3403 7697 -44 1066 -828 O ATOM 2225 CB PHE A1064 128.122 158.285 -17.046 1.00 45.13 C ANISOU 2225 CB PHE A1064 5849 3427 7872 26 1216 -563 C ATOM 2226 CG PHE A1064 128.220 159.454 -17.986 1.00 45.15 C ANISOU 2226 CG PHE A1064 5882 3460 7814 24 1208 -598 C ATOM 2227 CD1 PHE A1064 127.663 160.675 -17.650 1.00 43.97 C ANISOU 2227 CD1 PHE A1064 5699 3381 7626 -32 1117 -593 C ATOM 2228 CD2 PHE A1064 128.896 159.342 -19.196 1.00 46.51 C ANISOU 2228 CD2 PHE A1064 6126 3583 7962 87 1308 -629 C ATOM 2229 CE1 PHE A1064 127.756 161.759 -18.505 1.00 43.87 C ANISOU 2229 CE1 PHE A1064 5724 3384 7559 -29 1117 -617 C ATOM 2230 CE2 PHE A1064 128.991 160.425 -20.056 1.00 46.29 C ANISOU 2230 CE2 PHE A1064 6146 3571 7872 94 1322 -651 C ATOM 2231 CZ PHE A1064 128.421 161.634 -19.707 1.00 44.93 C ANISOU 2231 CZ PHE A1064 5939 3463 7669 34 1223 -643 C ATOM 2232 N GLN A1065 126.409 155.991 -18.746 1.00 46.76 N ANISOU 2232 N GLN A1065 6279 3493 7996 7 1190 -802 N ATOM 2233 CA GLN A1065 125.991 155.541 -20.066 1.00 48.35 C ANISOU 2233 CA GLN A1065 6612 3632 8128 21 1170 -932 C ATOM 2234 C GLN A1065 124.484 155.357 -20.169 1.00 47.89 C ANISOU 2234 C GLN A1065 6578 3566 8051 -59 1038 -1032 C ATOM 2235 O GLN A1065 123.981 155.138 -21.273 1.00 49.35 O ANISOU 2235 O GLN A1065 6878 3700 8172 -54 979 -1157 O ATOM 2236 CB GLN A1065 126.695 154.234 -20.452 1.00 51.81 C ANISOU 2236 CB GLN A1065 7115 3973 8597 88 1278 -945 C ATOM 2237 CG GLN A1065 128.201 154.360 -20.723 1.00 54.98 C ANISOU 2237 CG GLN A1065 7506 4365 9017 185 1425 -866 C ATOM 2238 CD GLN A1065 128.559 155.486 -21.688 1.00 57.55 C ANISOU 2238 CD GLN A1065 7884 4725 9257 218 1448 -890 C ATOM 2239 OE1 GLN A1065 127.827 155.776 -22.638 1.00 58.83 O ANISOU 2239 OE1 GLN A1065 8163 4877 9312 207 1374 -1004 O ATOM 2240 NE2 GLN A1065 129.695 156.129 -21.440 1.00 58.96 N ANISOU 2240 NE2 GLN A1065 7976 4935 9490 263 1551 -779 N ATOM 2241 N GLU A1066 123.756 155.417 -19.052 1.00 45.90 N ANISOU 2241 N GLU A1066 6226 3356 7859 -125 995 -983 N ATOM 2242 CA GLU A1066 122.301 155.417 -19.114 1.00 44.65 C ANISOU 2242 CA GLU A1066 6058 3199 7708 -203 882 -1066 C ATOM 2243 C GLU A1066 121.720 156.802 -19.390 1.00 42.82 C ANISOU 2243 C GLU A1066 5810 3047 7414 -229 782 -1091 C ATOM 2244 O GLU A1066 120.607 156.900 -19.919 1.00 43.50 O ANISOU 2244 O GLU A1066 5917 3122 7491 -274 675 -1191 O ATOM 2245 CB GLU A1066 121.731 154.845 -17.812 1.00 43.80 C ANISOU 2245 CB GLU A1066 5853 3089 7698 -255 911 -1001 C ATOM 2246 CG GLU A1066 121.994 153.354 -17.679 1.00 44.89 C ANISOU 2246 CG GLU A1066 6026 3123 7905 -240 994 -1002 C ATOM 2247 CD GLU A1066 121.553 152.776 -16.350 1.00 44.99 C ANISOU 2247 CD GLU A1066 5961 3121 8012 -276 1050 -923 C ATOM 2248 OE1 GLU A1066 122.394 152.676 -15.430 1.00 44.59 O ANISOU 2248 OE1 GLU A1066 5883 3079 7979 -230 1133 -807 O ATOM 2249 OE2 GLU A1066 120.362 152.418 -16.228 1.00 45.67 O ANISOU 2249 OE2 GLU A1066 6015 3177 8160 -347 1015 -978 O ATOM 2250 N MET A1067 122.463 157.863 -19.094 1.00 40.50 N ANISOU 2250 N MET A1067 5479 2823 7087 -200 811 -1008 N ATOM 2251 CA MET A1067 121.964 159.230 -19.154 1.00 38.08 C ANISOU 2251 CA MET A1067 5147 2590 6733 -222 729 -1011 C ATOM 2252 C MET A1067 122.207 159.872 -20.517 1.00 38.33 C ANISOU 2252 C MET A1067 5295 2602 6668 -177 698 -1085 C ATOM 2253 O MET A1067 123.115 159.491 -21.255 1.00 39.26 O ANISOU 2253 O MET A1067 5500 2667 6750 -113 777 -1101 O ATOM 2254 CB MET A1067 122.628 160.065 -18.062 1.00 35.62 C ANISOU 2254 CB MET A1067 4744 2351 6440 -219 774 -885 C ATOM 2255 CG MET A1067 122.652 159.353 -16.726 1.00 34.43 C ANISOU 2255 CG MET A1067 4516 2200 6365 -236 825 -807 C ATOM 2256 SD MET A1067 123.746 160.124 -15.526 1.00 32.77 S ANISOU 2256 SD MET A1067 4235 2045 6172 -212 872 -672 S ATOM 2257 CE MET A1067 123.436 159.085 -14.094 1.00 32.71 C ANISOU 2257 CE MET A1067 4189 2007 6233 -224 917 -609 C ATOM 2258 N ARG A1068 121.376 160.861 -20.841 1.00 37.93 N ANISOU 2258 N ARG A1068 5251 2586 6573 -200 594 -1131 N ATOM 2259 CA ARG A1068 121.558 161.696 -22.019 1.00 32.88 C ANISOU 2259 CA ARG A1068 4732 1928 5833 -148 564 -1190 C ATOM 2260 C ARG A1068 121.487 163.154 -21.596 1.00 31.68 C ANISOU 2260 C ARG A1068 4518 1847 5671 -162 538 -1122 C ATOM 2261 O ARG A1068 120.651 163.525 -20.770 1.00 30.99 O ANISOU 2261 O ARG A1068 4328 1815 5632 -218 474 -1098 O ATOM 2262 CB ARG A1068 120.500 161.405 -23.081 1.00 41.26 C ANISOU 2262 CB ARG A1068 5904 2934 6840 -151 435 -1346 C ATOM 2263 CG ARG A1068 120.163 159.931 -23.244 1.00 42.44 C ANISOU 2263 CG ARG A1068 6084 3013 7028 -172 423 -1422 C ATOM 2264 CD ARG A1068 121.238 159.186 -24.018 1.00 42.75 C ANISOU 2264 CD ARG A1068 6259 2978 7005 -91 524 -1450 C ATOM 2265 NE ARG A1068 120.918 157.769 -24.154 1.00 43.48 N ANISOU 2265 NE ARG A1068 6390 2993 7139 -111 512 -1525 N ATOM 2266 CZ ARG A1068 121.501 156.796 -23.462 1.00 43.01 C ANISOU 2266 CZ ARG A1068 6268 2910 7164 -114 621 -1454 C ATOM 2267 NH1 ARG A1068 122.449 157.086 -22.584 1.00 41.47 N ANISOU 2267 NH1 ARG A1068 5971 2770 7017 -96 741 -1310 N ATOM 2268 NH2 ARG A1068 121.142 155.529 -23.653 1.00 44.27 N ANISOU 2268 NH2 ARG A1068 6475 2983 7362 -134 607 -1530 N ATOM 2269 N PHE A1069 122.361 163.979 -22.163 1.00 31.59 N ANISOU 2269 N PHE A1069 4572 1827 5602 -108 605 -1091 N ATOM 2270 CA PHE A1069 122.488 165.371 -21.752 1.00 31.16 C ANISOU 2270 CA PHE A1069 4466 1827 5548 -120 601 -1014 C ATOM 2271 C PHE A1069 122.361 166.280 -22.966 1.00 31.81 C ANISOU 2271 C PHE A1069 4690 1864 5532 -65 577 -1075 C ATOM 2272 O PHE A1069 123.184 166.210 -23.887 1.00 32.10 O ANISOU 2272 O PHE A1069 4848 1843 5504 5 683 -1086 O ATOM 2273 CB PHE A1069 123.825 165.619 -21.048 1.00 30.95 C ANISOU 2273 CB PHE A1069 4360 1825 5576 -116 729 -887 C ATOM 2274 CG PHE A1069 123.956 164.941 -19.709 1.00 30.40 C ANISOU 2274 CG PHE A1069 4163 1798 5592 -157 740 -820 C ATOM 2275 CD1 PHE A1069 124.611 163.726 -19.592 1.00 29.76 C ANISOU 2275 CD1 PHE A1069 4073 1678 5555 -133 822 -807 C ATOM 2276 CD2 PHE A1069 123.449 165.535 -18.565 1.00 29.52 C ANISOU 2276 CD2 PHE A1069 3956 1754 5507 -207 681 -770 C ATOM 2277 CE1 PHE A1069 124.740 163.105 -18.365 1.00 29.35 C ANISOU 2277 CE1 PHE A1069 3925 1649 5576 -158 836 -744 C ATOM 2278 CE2 PHE A1069 123.578 164.920 -17.331 1.00 29.07 C ANISOU 2278 CE2 PHE A1069 3814 1722 5509 -229 701 -712 C ATOM 2279 CZ PHE A1069 124.224 163.702 -17.232 1.00 28.43 C ANISOU 2279 CZ PHE A1069 3730 1597 5475 -204 775 -698 C ATOM 2280 N ILE A1070 121.343 167.139 -22.957 1.00 31.49 N ANISOU 2280 N ILE A1070 4640 1846 5479 -86 456 -1110 N ATOM 2281 CA ILE A1070 121.208 168.221 -23.925 1.00 32.46 C ANISOU 2281 CA ILE A1070 4892 1925 5516 -28 432 -1149 C ATOM 2282 C ILE A1070 121.591 169.516 -23.222 1.00 31.66 C ANISOU 2282 C ILE A1070 4712 1866 5452 -52 477 -1027 C ATOM 2283 O ILE A1070 120.926 169.930 -22.263 1.00 30.58 O ANISOU 2283 O ILE A1070 4453 1793 5374 -108 399 -994 O ATOM 2284 CB ILE A1070 119.788 168.313 -24.502 1.00 33.49 C ANISOU 2284 CB ILE A1070 5070 2036 5618 -21 247 -1286 C ATOM 2285 CG1 ILE A1070 119.326 166.958 -25.037 1.00 34.91 C ANISOU 2285 CG1 ILE A1070 5304 2181 5779 -22 180 -1411 C ATOM 2286 CG2 ILE A1070 119.758 169.349 -25.618 1.00 34.24 C ANISOU 2286 CG2 ILE A1070 5331 2110 5569 71 215 -1308 C ATOM 2287 CD1 ILE A1070 120.111 166.477 -26.232 1.00 36.31 C ANISOU 2287 CD1 ILE A1070 5688 2276 5832 67 263 -1480 C ATOM 2288 N ILE A1071 122.655 170.160 -23.702 1.00 32.52 N ANISOU 2288 N ILE A1071 4899 1935 5522 -7 616 -956 N ATOM 2289 CA ILE A1071 123.152 171.415 -23.148 1.00 32.05 C ANISOU 2289 CA ILE A1071 4779 1899 5501 -33 668 -839 C ATOM 2290 C ILE A1071 122.946 172.494 -24.207 1.00 34.59 C ANISOU 2290 C ILE A1071 5252 2214 5677 39 655 -824 C ATOM 2291 O ILE A1071 123.593 172.471 -25.261 1.00 36.30 O ANISOU 2291 O ILE A1071 5613 2412 5768 116 756 -798 O ATOM 2292 CB ILE A1071 124.626 171.300 -22.738 1.00 30.74 C ANISOU 2292 CB ILE A1071 4540 1741 5401 -49 827 -727 C ATOM 2293 CG1 ILE A1071 124.804 170.107 -21.795 1.00 29.63 C ANISOU 2293 CG1 ILE A1071 4268 1654 5337 -91 809 -724 C ATOM 2294 CG2 ILE A1071 125.114 172.606 -22.103 1.00 29.95 C ANISOU 2294 CG2 ILE A1071 4362 1662 5354 -93 854 -619 C ATOM 2295 CD1 ILE A1071 126.243 169.716 -21.551 1.00 29.46 C ANISOU 2295 CD1 ILE A1071 4180 1620 5395 -84 958 -639 C ATOM 2296 N ILE A1072 122.056 173.448 -23.931 1.00 34.98 N ANISOU 2296 N ILE A1072 5277 2288 5727 26 537 -825 N ATOM 2297 CA ILE A1072 121.615 174.430 -24.920 1.00 36.79 C ANISOU 2297 CA ILE A1072 5654 2525 5800 109 482 -811 C ATOM 2298 C ILE A1072 122.050 175.825 -24.477 1.00 37.13 C ANISOU 2298 C ILE A1072 5665 2564 5877 86 547 -688 C ATOM 2299 O ILE A1072 121.546 176.352 -23.476 1.00 29.97 O ANISOU 2299 O ILE A1072 4638 1669 5080 25 481 -684 O ATOM 2300 CB ILE A1072 120.095 174.367 -25.128 1.00 31.82 C ANISOU 2300 CB ILE A1072 5030 1916 5144 133 269 -925 C ATOM 2301 CG1 ILE A1072 119.670 172.932 -25.423 1.00 32.37 C ANISOU 2301 CG1 ILE A1072 5104 1972 5223 129 198 -1059 C ATOM 2302 CG2 ILE A1072 119.673 175.257 -26.272 1.00 38.85 C ANISOU 2302 CG2 ILE A1072 6098 2813 5850 244 196 -912 C ATOM 2303 CD1 ILE A1072 118.180 172.739 -25.423 1.00 32.82 C ANISOU 2303 CD1 ILE A1072 5105 2043 5324 124 -15 -1181 C ATOM 2304 N GLY A1073 122.961 176.427 -25.229 1.00 38.93 N ANISOU 2304 N GLY A1073 6009 2767 6017 135 687 -592 N ATOM 2305 CA GLY A1073 123.375 177.785 -24.942 1.00 39.41 C ANISOU 2305 CA GLY A1073 6055 2804 6113 112 754 -479 C ATOM 2306 C GLY A1073 124.624 178.183 -25.703 1.00 40.85 C ANISOU 2306 C GLY A1073 6334 2942 6245 147 961 -366 C ATOM 2307 O GLY A1073 125.189 177.415 -26.483 1.00 41.35 O ANISOU 2307 O GLY A1073 6486 2996 6230 203 1064 -370 O ATOM 2308 N LYS A1074 125.035 179.425 -25.455 1.00 41.26 N ANISOU 2308 N LYS A1074 6370 2956 6353 114 1031 -263 N ATOM 2309 CA LYS A1074 126.265 179.984 -26.003 1.00 42.28 C ANISOU 2309 CA LYS A1074 6550 3026 6490 122 1249 -138 C ATOM 2310 C LYS A1074 126.701 181.144 -25.113 1.00 41.45 C ANISOU 2310 C LYS A1074 6323 2877 6550 21 1281 -60 C ATOM 2311 O LYS A1074 125.970 181.573 -24.215 1.00 40.88 O ANISOU 2311 O LYS A1074 6173 2820 6539 -32 1136 -104 O ATOM 2312 CB LYS A1074 126.089 180.427 -27.464 1.00 44.26 C ANISOU 2312 CB LYS A1074 7058 3243 6514 258 1318 -89 C ATOM 2313 CG LYS A1074 125.456 181.794 -27.673 1.00 44.56 C ANISOU 2313 CG LYS A1074 7199 3246 6487 296 1264 -32 C ATOM 2314 CD LYS A1074 125.502 182.179 -29.150 1.00 46.65 C ANISOU 2314 CD LYS A1074 7740 3470 6517 443 1366 41 C ATOM 2315 CE LYS A1074 124.988 183.595 -29.370 1.00 48.21 C ANISOU 2315 CE LYS A1074 8048 3614 6656 491 1337 123 C ATOM 2316 NZ LYS A1074 124.919 183.962 -30.811 1.00 50.79 N ANISOU 2316 NZ LYS A1074 8674 3901 6722 654 1417 197 N ATOM 2317 N GLY A1075 127.919 181.628 -25.356 1.00 40.90 N ANISOU 2317 N GLY A1075 6235 2744 6562 -9 1480 52 N ATOM 2318 CA GLY A1075 128.466 182.722 -24.582 1.00 34.34 C ANISOU 2318 CA GLY A1075 5287 1854 5905 -116 1518 120 C ATOM 2319 C GLY A1075 129.863 182.186 -24.375 1.00 35.06 C ANISOU 2319 C GLY A1075 5235 1904 6182 -193 1697 200 C ATOM 2320 O GLY A1075 130.436 181.563 -25.272 1.00 49.68 O ANISOU 2320 O GLY A1075 7168 3699 8009 -144 1906 294 O ATOM 2321 N ASP A1076 130.409 182.403 -23.182 1.00 34.14 N ANISOU 2321 N ASP A1076 4888 1873 6210 -296 1589 160 N ATOM 2322 CA ASP A1076 131.822 182.354 -22.863 1.00 34.93 C ANISOU 2322 CA ASP A1076 4801 1982 6489 -365 1695 219 C ATOM 2323 C ASP A1076 132.539 181.365 -23.786 1.00 41.71 C ANISOU 2323 C ASP A1076 5695 2792 7362 -296 1903 263 C ATOM 2324 O ASP A1076 132.224 180.159 -23.761 1.00 41.31 O ANISOU 2324 O ASP A1076 5662 2765 7269 -251 1862 195 O ATOM 2325 CB ASP A1076 131.978 181.940 -21.404 1.00 34.54 C ANISOU 2325 CB ASP A1076 4548 2033 6543 -447 1508 148 C ATOM 2326 CG ASP A1076 133.399 181.994 -20.921 1.00 36.51 C ANISOU 2326 CG ASP A1076 4589 2291 6992 -517 1566 196 C ATOM 2327 OD1 ASP A1076 134.293 181.451 -21.608 1.00 38.03 O ANISOU 2327 OD1 ASP A1076 4739 2442 7270 -485 1752 257 O ATOM 2328 OD2 ASP A1076 133.623 182.596 -19.856 1.00 36.75 O ANISOU 2328 OD2 ASP A1076 4504 2363 7097 -597 1425 172 O ATOM 2329 N PRO A1077 133.490 181.817 -24.604 1.00 43.17 N ANISOU 2329 N PRO A1077 5896 2904 7601 -280 2138 374 N ATOM 2330 CA PRO A1077 134.150 180.882 -25.531 1.00 44.52 C ANISOU 2330 CA PRO A1077 6127 3019 7770 -196 2366 422 C ATOM 2331 C PRO A1077 134.858 179.717 -24.861 1.00 44.20 C ANISOU 2331 C PRO A1077 5877 3027 7889 -225 2348 386 C ATOM 2332 O PRO A1077 134.878 178.618 -25.429 1.00 44.72 O ANISOU 2332 O PRO A1077 6014 3121 7855 -128 2415 355 O ATOM 2333 CB PRO A1077 135.144 181.789 -26.289 1.00 46.55 C ANISOU 2333 CB PRO A1077 6384 3207 8095 -195 2620 557 C ATOM 2334 CG PRO A1077 135.289 183.013 -25.444 1.00 46.22 C ANISOU 2334 CG PRO A1077 6190 3200 8172 -310 2489 559 C ATOM 2335 CD PRO A1077 133.964 183.199 -24.778 1.00 44.19 C ANISOU 2335 CD PRO A1077 6008 2992 7788 -326 2222 460 C ATOM 2336 N GLU A1078 135.447 179.908 -23.681 1.00 43.64 N ANISOU 2336 N GLU A1078 5547 3027 8006 -329 2217 372 N ATOM 2337 CA GLU A1078 136.129 178.783 -23.046 1.00 43.53 C ANISOU 2337 CA GLU A1078 5345 3052 8142 -339 2194 349 C ATOM 2338 C GLU A1078 135.140 177.760 -22.507 1.00 42.15 C ANISOU 2338 C GLU A1078 5229 2930 7857 -312 2009 239 C ATOM 2339 O GLU A1078 135.424 176.557 -22.511 1.00 42.95 O ANISOU 2339 O GLU A1078 5291 3033 7994 -263 2049 219 O ATOM 2340 CB GLU A1078 137.061 179.271 -21.933 1.00 43.88 C ANISOU 2340 CB GLU A1078 5118 3148 8405 -439 2085 362 C ATOM 2341 CG GLU A1078 138.277 180.050 -22.445 1.00 46.23 C ANISOU 2341 CG GLU A1078 5303 3392 8871 -460 2280 464 C ATOM 2342 CD GLU A1078 139.093 179.292 -23.497 1.00 49.15 C ANISOU 2342 CD GLU A1078 5672 3695 9306 -371 2575 544 C ATOM 2343 OE1 GLU A1078 138.931 178.054 -23.636 1.00 49.08 O ANISOU 2343 OE1 GLU A1078 5704 3684 9261 -306 2611 518 O ATOM 2344 OE2 GLU A1078 139.900 179.948 -24.190 1.00 51.00 O ANISOU 2344 OE2 GLU A1078 5875 3873 9628 -361 2782 632 O ATOM 2345 N LEU A1079 133.973 178.208 -22.054 1.00 40.55 N ANISOU 2345 N LEU A1079 5115 2775 7517 -335 1811 167 N ATOM 2346 CA LEU A1079 132.944 177.257 -21.663 1.00 33.23 C ANISOU 2346 CA LEU A1079 4251 1899 6477 -303 1656 63 C ATOM 2347 C LEU A1079 132.364 176.540 -22.870 1.00 43.33 C ANISOU 2347 C LEU A1079 5737 3151 7576 -188 1743 26 C ATOM 2348 O LEU A1079 132.052 175.349 -22.795 1.00 33.07 O ANISOU 2348 O LEU A1079 4450 1884 6231 -145 1695 -45 O ATOM 2349 CB LEU A1079 131.845 177.966 -20.892 1.00 31.95 C ANISOU 2349 CB LEU A1079 4118 1803 6220 -349 1440 1 C ATOM 2350 CG LEU A1079 132.239 178.422 -19.499 1.00 31.51 C ANISOU 2350 CG LEU A1079 3886 1817 6270 -439 1294 0 C ATOM 2351 CD1 LEU A1079 131.111 179.225 -18.911 1.00 30.52 C ANISOU 2351 CD1 LEU A1079 3832 1736 6028 -465 1128 -52 C ATOM 2352 CD2 LEU A1079 132.561 177.223 -18.630 1.00 31.02 C ANISOU 2352 CD2 LEU A1079 3702 1804 6280 -440 1223 -31 C ATOM 2353 N GLU A1080 132.219 177.240 -23.996 1.00 44.78 N ANISOU 2353 N GLU A1080 6093 3294 7627 -129 1857 69 N ATOM 2354 CA GLU A1080 131.747 176.572 -25.207 1.00 46.36 C ANISOU 2354 CA GLU A1080 6508 3495 7611 -4 1920 27 C ATOM 2355 C GLU A1080 132.740 175.518 -25.675 1.00 47.38 C ANISOU 2355 C GLU A1080 6608 3606 7790 57 2103 51 C ATOM 2356 O GLU A1080 132.344 174.457 -26.176 1.00 47.53 O ANISOU 2356 O GLU A1080 6742 3638 7681 138 2093 -29 O ATOM 2357 CB GLU A1080 131.516 177.586 -26.322 1.00 49.24 C ANISOU 2357 CB GLU A1080 7081 3814 7814 62 2017 88 C ATOM 2358 CG GLU A1080 130.361 178.532 -26.099 1.00 50.65 C ANISOU 2358 CG GLU A1080 7336 4006 7901 43 1836 56 C ATOM 2359 CD GLU A1080 130.186 179.488 -27.263 1.00 53.26 C ANISOU 2359 CD GLU A1080 7892 4284 8061 129 1941 130 C ATOM 2360 OE1 GLU A1080 129.469 180.500 -27.102 1.00 53.97 O ANISOU 2360 OE1 GLU A1080 8031 4362 8112 114 1835 140 O ATOM 2361 OE2 GLU A1080 130.773 179.223 -28.338 1.00 55.48 O ANISOU 2361 OE2 GLU A1080 8311 4528 8241 222 2139 185 O ATOM 2362 N GLY A1081 134.038 175.788 -25.510 1.00 48.20 N ANISOU 2362 N GLY A1081 6548 3671 8094 18 2273 157 N ATOM 2363 CA GLY A1081 135.041 174.807 -25.881 1.00 49.28 C ANISOU 2363 CA GLY A1081 6626 3786 8313 80 2460 189 C ATOM 2364 C GLY A1081 135.136 173.670 -24.889 1.00 37.41 C ANISOU 2364 C GLY A1081 4957 2325 6931 54 2336 126 C ATOM 2365 O GLY A1081 135.553 172.566 -25.245 1.00 38.09 O ANISOU 2365 O GLY A1081 5054 2398 7020 134 2442 110 O ATOM 2366 N TRP A1082 134.746 173.917 -23.638 1.00 35.91 N ANISOU 2366 N TRP A1082 4631 2179 6834 -47 2120 93 N ATOM 2367 CA TRP A1082 134.691 172.835 -22.667 1.00 54.57 C ANISOU 2367 CA TRP A1082 6875 4579 9280 -61 1992 37 C ATOM 2368 C TRP A1082 133.495 171.933 -22.932 1.00 53.70 C ANISOU 2368 C TRP A1082 6936 4487 8979 -5 1891 -82 C ATOM 2369 O TRP A1082 133.617 170.703 -22.900 1.00 54.56 O ANISOU 2369 O TRP A1082 7039 4588 9104 47 1913 -121 O ATOM 2370 CB TRP A1082 134.641 173.405 -21.251 1.00 33.90 C ANISOU 2370 CB TRP A1082 4089 1996 6795 -176 1801 40 C ATOM 2371 CG TRP A1082 134.800 172.355 -20.204 1.00 33.32 C ANISOU 2371 CG TRP A1082 3888 1953 6819 -181 1693 13 C ATOM 2372 CD1 TRP A1082 134.947 171.013 -20.410 1.00 33.60 C ANISOU 2372 CD1 TRP A1082 3938 1979 6848 -100 1752 -12 C ATOM 2373 CD2 TRP A1082 134.837 172.550 -18.787 1.00 33.45 C ANISOU 2373 CD2 TRP A1082 3761 2019 6930 -259 1507 10 C ATOM 2374 NE1 TRP A1082 135.069 170.362 -19.211 1.00 34.11 N ANISOU 2374 NE1 TRP A1082 3877 2069 7015 -123 1624 -18 N ATOM 2375 CE2 TRP A1082 135.004 171.282 -18.197 1.00 33.46 C ANISOU 2375 CE2 TRP A1082 3702 2022 6989 -218 1470 -5 C ATOM 2376 CE3 TRP A1082 134.743 173.668 -17.960 1.00 32.96 C ANISOU 2376 CE3 TRP A1082 3635 2012 6876 -345 1361 15 C ATOM 2377 CZ2 TRP A1082 135.076 171.102 -16.818 1.00 31.95 C ANISOU 2377 CZ2 TRP A1082 3399 1878 6863 -258 1298 -5 C ATOM 2378 CZ3 TRP A1082 134.815 173.486 -16.592 1.00 31.67 C ANISOU 2378 CZ3 TRP A1082 3366 1900 6767 -385 1186 1 C ATOM 2379 CH2 TRP A1082 134.981 172.212 -16.037 1.00 31.59 C ANISOU 2379 CH2 TRP A1082 3307 1883 6814 -341 1158 -4 C ATOM 2380 N ALA A1083 132.330 172.529 -23.197 1.00 51.91 N ANISOU 2380 N ALA A1083 6858 4277 8590 -15 1776 -141 N ATOM 2381 CA ALA A1083 131.153 171.740 -23.537 1.00 50.40 C ANISOU 2381 CA ALA A1083 6817 4096 8236 31 1670 -261 C ATOM 2382 C ALA A1083 131.307 171.051 -24.887 1.00 50.92 C ANISOU 2382 C ALA A1083 7066 4123 8159 147 1816 -291 C ATOM 2383 O ALA A1083 130.846 169.919 -25.065 1.00 50.24 O ANISOU 2383 O ALA A1083 7049 4024 8014 188 1775 -388 O ATOM 2384 CB ALA A1083 129.909 172.623 -23.527 1.00 32.16 C ANISOU 2384 CB ALA A1083 4599 1813 5808 1 1510 -310 C ATOM 2385 N ARG A1084 131.939 171.714 -25.857 1.00 53.62 N ANISOU 2385 N ARG A1084 7502 4434 8438 202 1994 -213 N ATOM 2386 CA ARG A1084 132.146 171.057 -27.144 1.00 55.69 C ANISOU 2386 CA ARG A1084 7965 4652 8543 327 2153 -239 C ATOM 2387 C ARG A1084 133.118 169.888 -27.016 1.00 55.37 C ANISOU 2387 C ARG A1084 7826 4579 8634 366 2298 -227 C ATOM 2388 O ARG A1084 133.005 168.902 -27.757 1.00 56.16 O ANISOU 2388 O ARG A1084 8081 4642 8614 458 2360 -303 O ATOM 2389 CB ARG A1084 132.632 172.065 -28.192 1.00 59.08 C ANISOU 2389 CB ARG A1084 8533 5047 8870 386 2341 -140 C ATOM 2390 CG ARG A1084 131.563 173.071 -28.636 1.00 60.64 C ANISOU 2390 CG ARG A1084 8902 5262 8875 394 2208 -162 C ATOM 2391 CD ARG A1084 130.386 172.395 -29.354 1.00 62.83 C ANISOU 2391 CD ARG A1084 9407 5553 8911 475 2057 -309 C ATOM 2392 NE ARG A1084 129.438 173.358 -29.922 1.00 65.90 N ANISOU 2392 NE ARG A1084 9972 5957 9110 510 1936 -320 N ATOM 2393 CZ ARG A1084 128.335 173.028 -30.594 1.00 69.33 C ANISOU 2393 CZ ARG A1084 10602 6407 9332 581 1768 -442 C ATOM 2394 NH1 ARG A1084 128.024 171.752 -30.787 1.00 70.61 N ANISOU 2394 NH1 ARG A1084 10817 6563 9447 611 1705 -574 N ATOM 2395 NH2 ARG A1084 127.537 173.975 -31.075 1.00 70.32 N ANISOU 2395 NH2 ARG A1084 10870 6548 9301 623 1654 -436 N ATOM 2396 N SER A1085 134.062 169.971 -26.072 1.00 55.07 N ANISOU 2396 N SER A1085 7534 4548 8842 302 2339 -137 N ATOM 2397 CA SER A1085 135.021 168.888 -25.887 1.00 55.21 C ANISOU 2397 CA SER A1085 7434 4534 9008 349 2468 -112 C ATOM 2398 C SER A1085 134.366 167.672 -25.247 1.00 53.49 C ANISOU 2398 C SER A1085 7208 4323 8795 345 2313 -219 C ATOM 2399 O SER A1085 134.689 166.533 -25.596 1.00 54.94 O ANISOU 2399 O SER A1085 7438 4458 8980 427 2416 -254 O ATOM 2400 CB SER A1085 136.205 169.370 -25.049 1.00 55.24 C ANISOU 2400 CB SER A1085 7156 4547 9285 285 2526 13 C ATOM 2401 OG SER A1085 137.356 168.582 -25.298 1.00 56.60 O ANISOU 2401 OG SER A1085 7235 4676 9597 365 2732 71 O ATOM 2402 N LEU A1086 133.451 167.888 -24.301 1.00 50.91 N ANISOU 2402 N LEU A1086 6826 4042 8475 252 2081 -269 N ATOM 2403 CA LEU A1086 132.705 166.762 -23.750 1.00 49.37 C ANISOU 2403 CA LEU A1086 6635 3863 8260 239 1937 -364 C ATOM 2404 C LEU A1086 131.766 166.150 -24.778 1.00 48.82 C ANISOU 2404 C LEU A1086 6796 3778 7975 295 1903 -490 C ATOM 2405 O LEU A1086 131.514 164.941 -24.742 1.00 35.70 O ANISOU 2405 O LEU A1086 5160 2117 6290 314 1863 -557 O ATOM 2406 CB LEU A1086 131.931 167.208 -22.516 1.00 33.27 C ANISOU 2406 CB LEU A1086 4485 1897 6257 130 1714 -374 C ATOM 2407 CG LEU A1086 132.828 167.610 -21.354 1.00 42.34 C ANISOU 2407 CG LEU A1086 5413 3066 7609 75 1702 -270 C ATOM 2408 CD1 LEU A1086 131.985 168.176 -20.243 1.00 40.53 C ANISOU 2408 CD1 LEU A1086 5125 2916 7359 -20 1491 -288 C ATOM 2409 CD2 LEU A1086 133.613 166.411 -20.864 1.00 33.45 C ANISOU 2409 CD2 LEU A1086 4178 1922 6609 120 1756 -239 C ATOM 2410 N GLU A1087 131.247 166.960 -25.699 1.00 48.16 N ANISOU 2410 N GLU A1087 6889 3672 7736 324 1911 -524 N ATOM 2411 CA GLU A1087 130.334 166.438 -26.710 1.00 47.67 C ANISOU 2411 CA GLU A1087 7059 3591 7463 383 1849 -657 C ATOM 2412 C GLU A1087 131.058 165.535 -27.702 1.00 48.34 C ANISOU 2412 C GLU A1087 7277 3623 7467 496 2036 -673 C ATOM 2413 O GLU A1087 130.495 164.533 -28.162 1.00 48.88 O ANISOU 2413 O GLU A1087 7467 3679 7427 527 1963 -792 O ATOM 2414 CB GLU A1087 129.653 167.601 -27.432 1.00 47.20 C ANISOU 2414 CB GLU A1087 7154 3546 7233 399 1789 -670 C ATOM 2415 CG GLU A1087 128.782 167.199 -28.603 1.00 47.19 C ANISOU 2415 CG GLU A1087 7416 3519 6994 479 1715 -807 C ATOM 2416 CD GLU A1087 128.315 168.398 -29.393 1.00 46.18 C ANISOU 2416 CD GLU A1087 7445 3423 6677 519 1669 -784 C ATOM 2417 OE1 GLU A1087 129.119 169.334 -29.576 1.00 45.80 O ANISOU 2417 OE1 GLU A1087 7386 3379 6636 538 1827 -646 O ATOM 2418 OE2 GLU A1087 127.142 168.412 -29.818 1.00 45.93 O ANISOU 2418 OE2 GLU A1087 7541 3406 6503 533 1472 -900 O ATOM 2419 N GLU A1088 132.301 165.891 -28.057 1.00 48.15 N ANISOU 2419 N GLU A1088 7228 3565 7503 556 2282 -554 N ATOM 2420 CA GLU A1088 133.113 165.066 -28.949 1.00 48.75 C ANISOU 2420 CA GLU A1088 7410 3597 7516 668 2491 -548 C ATOM 2421 C GLU A1088 133.527 163.760 -28.290 1.00 47.48 C ANISOU 2421 C GLU A1088 7103 3441 7495 657 2483 -555 C ATOM 2422 O GLU A1088 133.733 162.752 -28.977 1.00 48.45 O ANISOU 2422 O GLU A1088 7348 3530 7529 735 2565 -608 O ATOM 2423 CB GLU A1088 134.365 165.837 -29.391 1.00 50.40 C ANISOU 2423 CB GLU A1088 7586 3768 7796 728 2775 -399 C ATOM 2424 CG GLU A1088 134.085 167.043 -30.280 1.00 52.37 C ANISOU 2424 CG GLU A1088 8026 4010 7860 764 2829 -369 C ATOM 2425 CD GLU A1088 135.353 167.767 -30.740 1.00 55.27 C ANISOU 2425 CD GLU A1088 8346 4348 8307 810 3127 -204 C ATOM 2426 OE1 GLU A1088 135.243 168.964 -31.083 1.00 56.67 O ANISOU 2426 OE1 GLU A1088 8585 4541 8407 793 3148 -132 O ATOM 2427 OE2 GLU A1088 136.448 167.154 -30.766 1.00 56.76 O ANISOU 2427 OE2 GLU A1088 8430 4489 8647 866 3347 -143 O ATOM 2428 N LYS A1089 133.665 163.768 -26.967 1.00 45.34 N ANISOU 2428 N LYS A1089 6586 3207 7432 567 2383 -500 N ATOM 2429 CA LYS A1089 134.129 162.601 -26.236 1.00 44.63 C ANISOU 2429 CA LYS A1089 6355 3119 7483 566 2380 -483 C ATOM 2430 C LYS A1089 133.021 161.589 -26.021 1.00 45.21 C ANISOU 2430 C LYS A1089 6504 3201 7472 531 2188 -611 C ATOM 2431 O LYS A1089 133.275 160.379 -26.079 1.00 47.07 O ANISOU 2431 O LYS A1089 6755 3404 7724 573 2229 -638 O ATOM 2432 CB LYS A1089 134.698 163.037 -24.885 1.00 42.61 C ANISOU 2432 CB LYS A1089 5828 2897 7465 496 2336 -372 C ATOM 2433 CG LYS A1089 135.369 161.934 -24.109 1.00 42.56 C ANISOU 2433 CG LYS A1089 5671 2885 7616 517 2353 -327 C ATOM 2434 CD LYS A1089 136.040 162.470 -22.873 1.00 42.30 C ANISOU 2434 CD LYS A1089 5386 2877 7810 467 2307 -216 C ATOM 2435 CE LYS A1089 136.794 161.377 -22.153 1.00 44.19 C ANISOU 2435 CE LYS A1089 5485 3102 8203 513 2329 -159 C ATOM 2436 NZ LYS A1089 137.376 161.897 -20.886 1.00 44.69 N ANISOU 2436 NZ LYS A1089 5313 3187 8481 471 2241 -62 N ATOM 2437 N HIS A1090 131.799 162.063 -25.791 1.00 44.11 N ANISOU 2437 N HIS A1090 6406 3098 7256 454 1985 -688 N ATOM 2438 CA HIS A1090 130.691 161.234 -25.346 1.00 43.79 C ANISOU 2438 CA HIS A1090 6376 3070 7190 395 1790 -791 C ATOM 2439 C HIS A1090 129.579 161.251 -26.380 1.00 44.76 C ANISOU 2439 C HIS A1090 6713 3171 7123 410 1681 -939 C ATOM 2440 O HIS A1090 129.148 162.323 -26.819 1.00 44.90 O ANISOU 2440 O HIS A1090 6808 3204 7048 407 1639 -954 O ATOM 2441 CB HIS A1090 130.161 161.728 -24.001 1.00 35.72 C ANISOU 2441 CB HIS A1090 5181 2116 6273 288 1633 -746 C ATOM 2442 CG HIS A1090 131.183 161.710 -22.912 1.00 35.25 C ANISOU 2442 CG HIS A1090 4923 2076 6394 277 1700 -616 C ATOM 2443 ND1 HIS A1090 131.860 160.565 -22.548 1.00 35.92 N ANISOU 2443 ND1 HIS A1090 4947 2130 6572 319 1775 -580 N ATOM 2444 CD2 HIS A1090 131.642 162.691 -22.104 1.00 34.36 C ANISOU 2444 CD2 HIS A1090 4662 2004 6390 233 1689 -519 C ATOM 2445 CE1 HIS A1090 132.694 160.843 -21.563 1.00 35.51 C ANISOU 2445 CE1 HIS A1090 4715 2098 6680 309 1800 -465 C ATOM 2446 NE2 HIS A1090 132.579 162.126 -21.272 1.00 45.79 N ANISOU 2446 NE2 HIS A1090 5960 3443 7996 253 1743 -431 N ATOM 2447 N GLY A1091 129.076 160.067 -26.715 1.00 39.09 N ANISOU 2447 N GLY A1091 6084 2411 6357 424 1618 -1050 N ATOM 2448 CA GLY A1091 127.966 159.945 -27.623 1.00 39.94 C ANISOU 2448 CA GLY A1091 6377 2490 6308 433 1474 -1212 C ATOM 2449 C GLY A1091 126.621 160.197 -26.988 1.00 44.16 C ANISOU 2449 C GLY A1091 6838 3062 6881 330 1240 -1274 C ATOM 2450 O GLY A1091 125.594 160.117 -27.670 1.00 45.02 O ANISOU 2450 O GLY A1091 7073 3144 6889 329 1088 -1418 O ATOM 2451 N ASN A1092 126.597 160.489 -25.684 1.00 42.44 N ANISOU 2451 N ASN A1092 6415 2905 6805 246 1205 -1171 N ATOM 2452 CA ASN A1092 125.373 160.819 -24.963 1.00 41.39 C ANISOU 2452 CA ASN A1092 6195 2820 6713 150 1015 -1200 C ATOM 2453 C ASN A1092 125.339 162.278 -24.517 1.00 40.62 C ANISOU 2453 C ASN A1092 6017 2788 6627 117 993 -1118 C ATOM 2454 O ASN A1092 124.565 162.634 -23.622 1.00 39.81 O ANISOU 2454 O ASN A1092 5799 2742 6583 38 877 -1098 O ATOM 2455 CB ASN A1092 125.173 159.876 -23.769 1.00 35.37 C ANISOU 2455 CB ASN A1092 5287 2074 6079 83 987 -1155 C ATOM 2456 CG ASN A1092 126.394 159.780 -22.860 1.00 34.71 C ANISOU 2456 CG ASN A1092 5073 2015 6102 96 1128 -1009 C ATOM 2457 OD1 ASN A1092 127.526 160.015 -23.275 1.00 35.15 O ANISOU 2457 OD1 ASN A1092 5148 2052 6155 164 1274 -952 O ATOM 2458 ND2 ASN A1092 126.159 159.415 -21.609 1.00 33.88 N ANISOU 2458 ND2 ASN A1092 4836 1945 6092 38 1090 -947 N ATOM 2459 N VAL A1093 126.175 163.128 -25.107 1.00 40.83 N ANISOU 2459 N VAL A1093 6107 2804 6601 177 1120 -1064 N ATOM 2460 CA VAL A1093 126.132 164.565 -24.867 1.00 40.14 C ANISOU 2460 CA VAL A1093 5978 2759 6516 151 1104 -997 C ATOM 2461 C VAL A1093 125.949 165.269 -26.203 1.00 41.89 C ANISOU 2461 C VAL A1093 6412 2932 6573 229 1128 -1059 C ATOM 2462 O VAL A1093 126.474 164.825 -27.233 1.00 43.39 O ANISOU 2462 O VAL A1093 6765 3067 6652 320 1247 -1093 O ATOM 2463 CB VAL A1093 127.395 165.077 -24.147 1.00 33.32 C ANISOU 2463 CB VAL A1093 4973 1918 5767 142 1248 -843 C ATOM 2464 CG1 VAL A1093 127.387 166.587 -24.097 1.00 32.71 C ANISOU 2464 CG1 VAL A1093 4884 1862 5682 121 1242 -782 C ATOM 2465 CG2 VAL A1093 127.460 164.508 -22.748 1.00 32.48 C ANISOU 2465 CG2 VAL A1093 4683 1864 5795 75 1195 -787 C ATOM 2466 N LYS A1094 125.187 166.363 -26.177 1.00 41.59 N ANISOU 2466 N LYS A1094 6386 2914 6501 202 1020 -1069 N ATOM 2467 CA LYS A1094 124.852 167.121 -27.374 1.00 43.19 C ANISOU 2467 CA LYS A1094 6803 3089 6516 282 1006 -1116 C ATOM 2468 C LYS A1094 124.699 168.583 -26.993 1.00 42.70 C ANISOU 2468 C LYS A1094 6671 3091 6461 250 963 -1013 C ATOM 2469 O LYS A1094 123.864 168.930 -26.149 1.00 41.17 O ANISOU 2469 O LYS A1094 6347 2931 6364 172 820 -1030 O ATOM 2470 CB LYS A1094 123.559 166.616 -28.020 1.00 44.09 C ANISOU 2470 CB LYS A1094 7038 3186 6527 296 802 -1292 C ATOM 2471 CG LYS A1094 123.101 167.447 -29.211 1.00 45.43 C ANISOU 2471 CG LYS A1094 7417 3384 6459 388 717 -1319 C ATOM 2472 CD LYS A1094 123.938 167.141 -30.450 1.00 47.41 C ANISOU 2472 CD LYS A1094 7914 3591 6507 515 879 -1319 C ATOM 2473 CE LYS A1094 123.571 168.049 -31.627 1.00 48.97 C ANISOU 2473 CE LYS A1094 8351 3815 6440 625 813 -1320 C ATOM 2474 NZ LYS A1094 124.228 167.643 -32.913 1.00 51.22 N ANISOU 2474 NZ LYS A1094 8923 4048 6490 763 962 -1344 N ATOM 2475 N VAL A1095 125.504 169.432 -27.624 1.00 44.21 N ANISOU 2475 N VAL A1095 6955 3289 6555 313 1104 -905 N ATOM 2476 CA VAL A1095 125.509 170.867 -27.371 1.00 43.73 C ANISOU 2476 CA VAL A1095 6849 3267 6498 290 1096 -798 C ATOM 2477 C VAL A1095 124.836 171.567 -28.540 1.00 46.13 C ANISOU 2477 C VAL A1095 7375 3580 6574 383 1017 -826 C ATOM 2478 O VAL A1095 125.119 171.264 -29.708 1.00 47.15 O ANISOU 2478 O VAL A1095 7717 3678 6518 490 1098 -849 O ATOM 2479 CB VAL A1095 126.937 171.395 -27.158 1.00 43.22 C ANISOU 2479 CB VAL A1095 6708 3189 6525 281 1318 -642 C ATOM 2480 CG1 VAL A1095 126.914 172.896 -26.944 1.00 42.24 C ANISOU 2480 CG1 VAL A1095 6554 3085 6410 250 1308 -542 C ATOM 2481 CG2 VAL A1095 127.572 170.697 -25.970 1.00 42.55 C ANISOU 2481 CG2 VAL A1095 6403 3102 6661 201 1359 -616 C ATOM 2482 N ILE A1096 123.949 172.502 -28.220 1.00 47.35 N ANISOU 2482 N ILE A1096 7489 3771 6731 355 862 -822 N ATOM 2483 CA ILE A1096 123.242 173.315 -29.200 1.00 50.90 C ANISOU 2483 CA ILE A1096 8129 4231 6978 449 761 -832 C ATOM 2484 C ILE A1096 123.555 174.769 -28.880 1.00 52.67 C ANISOU 2484 C ILE A1096 8312 4460 7238 432 830 -687 C ATOM 2485 O ILE A1096 123.160 175.277 -27.821 1.00 52.01 O ANISOU 2485 O ILE A1096 8052 4399 7310 343 750 -670 O ATOM 2486 CB ILE A1096 121.729 173.058 -29.176 1.00 36.71 C ANISOU 2486 CB ILE A1096 6317 2465 5166 445 485 -976 C ATOM 2487 CG1 ILE A1096 121.424 171.589 -29.476 1.00 37.37 C ANISOU 2487 CG1 ILE A1096 6436 2526 5238 446 415 -1131 C ATOM 2488 CG2 ILE A1096 121.015 173.964 -30.162 1.00 42.51 C ANISOU 2488 CG2 ILE A1096 7242 3215 5694 556 360 -976 C ATOM 2489 CD1 ILE A1096 119.941 171.276 -29.455 1.00 37.70 C ANISOU 2489 CD1 ILE A1096 6433 2585 5304 427 141 -1282 C ATOM 2490 N THR A1097 124.286 175.430 -29.780 1.00 54.74 N ANISOU 2490 N THR A1097 8748 4691 7362 516 996 -581 N ATOM 2491 CA THR A1097 124.634 176.836 -29.631 1.00 55.46 C ANISOU 2491 CA THR A1097 8829 4762 7483 504 1083 -439 C ATOM 2492 C THR A1097 123.794 177.765 -30.504 1.00 56.70 C ANISOU 2492 C THR A1097 9192 4918 7435 615 974 -424 C ATOM 2493 O THR A1097 123.791 178.975 -30.265 1.00 56.11 O ANISOU 2493 O THR A1097 9100 4822 7398 601 999 -323 O ATOM 2494 CB THR A1097 126.123 177.048 -29.945 1.00 56.74 C ANISOU 2494 CB THR A1097 9014 4869 7675 511 1378 -304 C ATOM 2495 OG1 THR A1097 126.445 176.393 -31.178 1.00 58.91 O ANISOU 2495 OG1 THR A1097 9517 5119 7746 635 1490 -324 O ATOM 2496 CG2 THR A1097 127.003 176.479 -28.832 1.00 55.37 C ANISOU 2496 CG2 THR A1097 8583 4697 7756 390 1466 -286 C ATOM 2497 N GLU A1098 123.088 177.235 -31.499 1.00 58.72 N ANISOU 2497 N GLU A1098 9645 5189 7475 728 846 -525 N ATOM 2498 CA GLU A1098 122.234 178.037 -32.365 1.00 61.27 C ANISOU 2498 CA GLU A1098 10175 5518 7588 853 707 -518 C ATOM 2499 C GLU A1098 120.938 178.423 -31.657 1.00 60.46 C ANISOU 2499 C GLU A1098 9920 5460 7591 811 443 -587 C ATOM 2500 O GLU A1098 120.454 177.711 -30.772 1.00 58.85 O ANISOU 2500 O GLU A1098 9506 5289 7564 709 327 -691 O ATOM 2501 CB GLU A1098 121.924 177.278 -33.657 1.00 65.76 C ANISOU 2501 CB GLU A1098 11013 6089 7882 993 631 -618 C ATOM 2502 CG GLU A1098 121.547 178.173 -34.850 1.00 70.41 C ANISOU 2502 CG GLU A1098 11905 6663 8183 1165 584 -556 C ATOM 2503 CD GLU A1098 121.754 177.502 -36.207 1.00 75.32 C ANISOU 2503 CD GLU A1098 12852 7266 8499 1315 620 -611 C ATOM 2504 OE1 GLU A1098 122.391 176.426 -36.262 1.00 76.19 O ANISOU 2504 OE1 GLU A1098 12958 7361 8630 1286 742 -674 O ATOM 2505 OE2 GLU A1098 121.278 178.059 -37.222 1.00 78.27 O ANISOU 2505 OE2 GLU A1098 13501 7636 8601 1473 528 -590 O ATOM 2506 N MET A1099 120.386 179.574 -32.049 1.00 62.07 N ANISOU 2506 N MET A1099 10235 5657 7693 897 366 -519 N ATOM 2507 CA MET A1099 119.152 180.076 -31.452 1.00 61.45 C ANISOU 2507 CA MET A1099 10020 5613 7716 880 134 -570 C ATOM 2508 C MET A1099 117.978 179.142 -31.733 1.00 62.09 C ANISOU 2508 C MET A1099 10084 5748 7760 913 -142 -751 C ATOM 2509 O MET A1099 117.811 178.650 -32.853 1.00 64.28 O ANISOU 2509 O MET A1099 10576 6031 7816 1025 -225 -818 O ATOM 2510 CB MET A1099 118.833 181.476 -31.985 1.00 63.95 C ANISOU 2510 CB MET A1099 10492 5898 7906 995 114 -454 C ATOM 2511 CG MET A1099 117.488 182.023 -31.516 1.00 64.24 C ANISOU 2511 CG MET A1099 10408 5968 8034 1011 -132 -505 C ATOM 2512 SD MET A1099 117.632 183.313 -30.260 1.00 63.59 S ANISOU 2512 SD MET A1099 10141 5837 8181 912 -23 -388 S ATOM 2513 CE MET A1099 118.295 184.659 -31.246 1.00 65.57 C ANISOU 2513 CE MET A1099 10676 6001 8236 1039 149 -195 C ATOM 2514 N LEU A1100 117.141 178.935 -30.714 1.00 61.52 N ANISOU 2514 N LEU A1100 9760 5707 7907 816 -285 -833 N ATOM 2515 CA LEU A1100 115.973 178.064 -30.791 1.00 63.95 C ANISOU 2515 CA LEU A1100 9987 6055 8256 816 -542 -1007 C ATOM 2516 C LEU A1100 114.691 178.859 -30.549 1.00 65.84 C ANISOU 2516 C LEU A1100 10124 6320 8571 857 -756 -1024 C ATOM 2517 O LEU A1100 114.657 179.762 -29.708 1.00 65.79 O ANISOU 2517 O LEU A1100 9994 6302 8700 814 -685 -933 O ATOM 2518 CB LEU A1100 116.081 176.911 -29.779 1.00 39.01 C ANISOU 2518 CB LEU A1100 6603 2900 5321 661 -501 -1095 C ATOM 2519 CG LEU A1100 117.307 175.997 -29.903 1.00 38.66 C ANISOU 2519 CG LEU A1100 6622 2826 5241 620 -297 -1086 C ATOM 2520 CD1 LEU A1100 117.291 174.887 -28.863 1.00 37.23 C ANISOU 2520 CD1 LEU A1100 6220 2642 5286 481 -277 -1166 C ATOM 2521 CD2 LEU A1100 117.386 175.410 -31.290 1.00 42.37 C ANISOU 2521 CD2 LEU A1100 7352 3287 5460 737 -350 -1161 C ATOM 2522 N SER A1101 113.643 178.523 -31.305 1.00 67.05 N ANISOU 2522 N SER A1101 10331 6505 8641 945 -1022 -1146 N ATOM 2523 CA SER A1101 112.319 179.130 -31.212 1.00 65.90 C ANISOU 2523 CA SER A1101 10073 6387 8577 1003 -1261 -1183 C ATOM 2524 C SER A1101 111.562 178.622 -29.986 1.00 62.45 C ANISOU 2524 C SER A1101 9306 5963 8459 862 -1316 -1271 C ATOM 2525 O SER A1101 111.763 177.496 -29.527 1.00 60.85 O ANISOU 2525 O SER A1101 8993 5753 8374 744 -1267 -1358 O ATOM 2526 CB SER A1101 111.498 178.811 -32.454 1.00 68.32 C ANISOU 2526 CB SER A1101 10537 6723 8698 1140 -1549 -1301 C ATOM 2527 OG SER A1101 111.097 177.451 -32.432 1.00 68.41 O ANISOU 2527 OG SER A1101 10442 6745 8805 1057 -1677 -1483 O ATOM 2528 N ARG A1102 110.630 179.446 -29.492 1.00 60.01 N ANISOU 2528 N ARG A1102 8846 5664 8289 889 -1418 -1248 N ATOM 2529 CA ARG A1102 109.909 179.085 -28.272 1.00 57.43 C ANISOU 2529 CA ARG A1102 8213 5340 8268 765 -1430 -1311 C ATOM 2530 C ARG A1102 109.173 177.765 -28.430 1.00 56.04 C ANISOU 2530 C ARG A1102 7912 5177 8202 707 -1606 -1491 C ATOM 2531 O ARG A1102 109.090 176.977 -27.478 1.00 54.01 O ANISOU 2531 O ARG A1102 7457 4903 8161 568 -1523 -1543 O ATOM 2532 CB ARG A1102 108.910 180.178 -27.891 1.00 58.95 C ANISOU 2532 CB ARG A1102 8280 5538 8582 833 -1527 -1268 C ATOM 2533 CG ARG A1102 109.511 181.494 -27.439 1.00 58.74 C ANISOU 2533 CG ARG A1102 8324 5475 8517 860 -1339 -1101 C ATOM 2534 CD ARG A1102 108.547 182.237 -26.514 1.00 58.95 C ANISOU 2534 CD ARG A1102 8142 5493 8765 863 -1367 -1085 C ATOM 2535 NE ARG A1102 107.201 182.337 -27.075 1.00 60.88 N ANISOU 2535 NE ARG A1102 8300 5767 9063 976 -1640 -1163 N ATOM 2536 CZ ARG A1102 106.155 182.821 -26.414 1.00 60.63 C ANISOU 2536 CZ ARG A1102 8056 5731 9248 997 -1699 -1173 C ATOM 2537 NH1 ARG A1102 106.299 183.243 -25.163 1.00 59.36 N ANISOU 2537 NH1 ARG A1102 7776 5533 9246 914 -1496 -1114 N ATOM 2538 NH2 ARG A1102 104.966 182.880 -26.999 1.00 61.97 N ANISOU 2538 NH2 ARG A1102 8135 5931 9478 1106 -1964 -1245 N ATOM 2539 N GLU A1103 108.632 177.502 -29.621 1.00 57.45 N ANISOU 2539 N GLU A1103 8214 5378 8235 813 -1852 -1590 N ATOM 2540 CA GLU A1103 107.936 176.238 -29.837 1.00 58.36 C ANISOU 2540 CA GLU A1103 8218 5493 8463 751 -2039 -1779 C ATOM 2541 C GLU A1103 108.888 175.050 -29.753 1.00 56.77 C ANISOU 2541 C GLU A1103 8083 5256 8230 643 -1875 -1826 C ATOM 2542 O GLU A1103 108.489 173.961 -29.321 1.00 56.68 O ANISOU 2542 O GLU A1103 7901 5217 8417 525 -1911 -1949 O ATOM 2543 CB GLU A1103 107.221 176.240 -31.189 1.00 61.99 C ANISOU 2543 CB GLU A1103 8827 5983 8745 896 -2362 -1884 C ATOM 2544 CG GLU A1103 106.245 177.385 -31.395 1.00 64.38 C ANISOU 2544 CG GLU A1103 9074 6320 9068 1030 -2557 -1839 C ATOM 2545 CD GLU A1103 106.905 178.603 -32.012 1.00 67.30 C ANISOU 2545 CD GLU A1103 9726 6696 9149 1186 -2472 -1670 C ATOM 2546 OE1 GLU A1103 107.524 179.394 -31.267 1.00 66.41 O ANISOU 2546 OE1 GLU A1103 9596 6560 9076 1155 -2219 -1515 O ATOM 2547 OE2 GLU A1103 106.811 178.760 -33.250 1.00 70.55 O ANISOU 2547 OE2 GLU A1103 10388 7126 9290 1342 -2658 -1694 O ATOM 2548 N PHE A1104 110.140 175.229 -30.169 1.00 55.93 N ANISOU 2548 N PHE A1104 8219 5141 7892 684 -1686 -1726 N ATOM 2549 CA PHE A1104 111.090 174.135 -30.061 1.00 55.03 C ANISOU 2549 CA PHE A1104 8158 4989 7762 595 -1514 -1759 C ATOM 2550 C PHE A1104 111.439 173.870 -28.604 1.00 55.04 C ANISOU 2550 C PHE A1104 7932 4968 8014 443 -1302 -1700 C ATOM 2551 O PHE A1104 111.485 172.713 -28.168 1.00 54.57 O ANISOU 2551 O PHE A1104 7770 4873 8093 335 -1261 -1786 O ATOM 2552 CB PHE A1104 112.340 174.448 -30.875 1.00 54.49 C ANISOU 2552 CB PHE A1104 8389 4914 7403 688 -1348 -1657 C ATOM 2553 CG PHE A1104 113.366 173.364 -30.828 1.00 53.92 C ANISOU 2553 CG PHE A1104 8376 4800 7311 618 -1160 -1681 C ATOM 2554 CD1 PHE A1104 113.257 172.251 -31.645 1.00 55.52 C ANISOU 2554 CD1 PHE A1104 8704 4977 7415 637 -1271 -1838 C ATOM 2555 CD2 PHE A1104 114.431 173.445 -29.951 1.00 52.15 C ANISOU 2555 CD2 PHE A1104 8080 4558 7177 536 -884 -1555 C ATOM 2556 CE1 PHE A1104 114.192 171.246 -31.594 1.00 55.48 C ANISOU 2556 CE1 PHE A1104 8755 4923 7403 583 -1088 -1859 C ATOM 2557 CE2 PHE A1104 115.374 172.442 -29.893 1.00 52.20 C ANISOU 2557 CE2 PHE A1104 8127 4526 7182 484 -716 -1571 C ATOM 2558 CZ PHE A1104 115.255 171.339 -30.717 1.00 53.71 C ANISOU 2558 CZ PHE A1104 8444 4685 7276 510 -807 -1720 C ATOM 2559 N VAL A1105 111.674 174.934 -27.833 1.00 56.81 N ANISOU 2559 N VAL A1105 8087 5204 8295 436 -1170 -1557 N ATOM 2560 CA VAL A1105 111.991 174.779 -26.417 1.00 57.88 C ANISOU 2560 CA VAL A1105 8030 5320 8641 306 -983 -1499 C ATOM 2561 C VAL A1105 110.800 174.192 -25.672 1.00 60.43 C ANISOU 2561 C VAL A1105 8100 5633 9228 222 -1089 -1603 C ATOM 2562 O VAL A1105 110.958 173.394 -24.740 1.00 61.00 O ANISOU 2562 O VAL A1105 8039 5674 9466 106 -970 -1618 O ATOM 2563 CB VAL A1105 112.423 176.136 -25.829 1.00 36.02 C ANISOU 2563 CB VAL A1105 5266 2560 5861 327 -849 -1340 C ATOM 2564 CG1 VAL A1105 112.715 176.012 -24.350 1.00 34.14 C ANISOU 2564 CG1 VAL A1105 4851 2303 5817 203 -681 -1290 C ATOM 2565 CG2 VAL A1105 113.635 176.667 -26.570 1.00 36.05 C ANISOU 2565 CG2 VAL A1105 5504 2559 5636 396 -720 -1232 C ATOM 2566 N ARG A1106 109.588 174.560 -26.085 1.00 62.16 N ANISOU 2566 N ARG A1106 8247 5873 9497 284 -1312 -1673 N ATOM 2567 CA ARG A1106 108.398 173.967 -25.487 1.00 61.28 C ANISOU 2567 CA ARG A1106 7878 5744 9663 205 -1415 -1780 C ATOM 2568 C ARG A1106 108.307 172.483 -25.810 1.00 60.23 C ANISOU 2568 C ARG A1106 7725 5569 9590 126 -1479 -1928 C ATOM 2569 O ARG A1106 107.903 171.681 -24.962 1.00 59.82 O ANISOU 2569 O ARG A1106 7475 5490 9764 8 -1408 -1961 O ATOM 2570 CB ARG A1106 107.155 174.708 -25.976 1.00 41.39 C ANISOU 2570 CB ARG A1106 5279 3258 7191 304 -1658 -1824 C ATOM 2571 CG ARG A1106 105.842 174.212 -25.405 1.00 42.38 C ANISOU 2571 CG ARG A1106 5106 3362 7636 230 -1766 -1929 C ATOM 2572 CD ARG A1106 104.677 174.974 -26.002 1.00 50.25 C ANISOU 2572 CD ARG A1106 6023 4395 8674 347 -2027 -1969 C ATOM 2573 NE ARG A1106 104.573 174.768 -27.446 1.00 52.49 N ANISOU 2573 NE ARG A1106 6488 4705 8749 448 -2290 -2068 N ATOM 2574 CZ ARG A1106 103.870 175.550 -28.259 1.00 54.39 C ANISOU 2574 CZ ARG A1106 6768 4989 8908 595 -2536 -2081 C ATOM 2575 NH1 ARG A1106 103.212 176.593 -27.768 1.00 54.44 N ANISOU 2575 NH1 ARG A1106 6630 5012 9043 658 -2540 -1998 N ATOM 2576 NH2 ARG A1106 103.831 175.299 -29.561 1.00 50.54 N ANISOU 2576 NH2 ARG A1106 6479 4524 8201 691 -2776 -2174 N ATOM 2577 N GLU A1107 108.691 172.098 -27.029 1.00 59.63 N ANISOU 2577 N GLU A1107 7867 5497 9294 194 -1588 -1998 N ATOM 2578 CA GLU A1107 108.724 170.681 -27.368 1.00 60.67 C ANISOU 2578 CA GLU A1107 8015 5573 9463 121 -1634 -2144 C ATOM 2579 C GLU A1107 109.737 169.942 -26.500 1.00 57.72 C ANISOU 2579 C GLU A1107 7618 5199 9113 17 -1330 -2035 C ATOM 2580 O GLU A1107 109.457 168.848 -25.998 1.00 58.22 O ANISOU 2580 O GLU A1107 7542 5271 9307 -87 -1262 -2048 O ATOM 2581 CB GLU A1107 109.042 170.511 -28.855 1.00 63.92 C ANISOU 2581 CB GLU A1107 8710 5996 9582 235 -1783 -2223 C ATOM 2582 CG GLU A1107 109.051 169.077 -29.340 1.00 67.52 C ANISOU 2582 CG GLU A1107 9208 6415 10033 174 -1828 -2361 C ATOM 2583 CD GLU A1107 109.639 168.935 -30.735 1.00 72.55 C ANISOU 2583 CD GLU A1107 10187 7032 10346 298 -1924 -2443 C ATOM 2584 OE1 GLU A1107 110.497 168.044 -30.930 1.00 72.83 O ANISOU 2584 OE1 GLU A1107 10344 7040 10288 268 -1760 -2443 O ATOM 2585 OE2 GLU A1107 109.249 169.718 -31.631 1.00 75.81 O ANISOU 2585 OE2 GLU A1107 10742 7492 10572 434 -2122 -2457 O ATOM 2586 N LEU A1108 110.897 170.561 -26.253 1.00 53.97 N ANISOU 2586 N LEU A1108 7272 4715 8522 50 -1144 -1913 N ATOM 2587 CA LEU A1108 111.914 169.939 -25.409 1.00 50.25 C ANISOU 2587 CA LEU A1108 6776 4254 8064 -35 -877 -1798 C ATOM 2588 C LEU A1108 111.445 169.805 -23.966 1.00 47.86 C ANISOU 2588 C LEU A1108 6230 3996 7957 -136 -760 -1707 C ATOM 2589 O LEU A1108 111.706 168.788 -23.313 1.00 46.78 O ANISOU 2589 O LEU A1108 6029 3873 7872 -214 -630 -1667 O ATOM 2590 CB LEU A1108 113.199 170.753 -25.453 1.00 48.75 C ANISOU 2590 CB LEU A1108 6744 4042 7736 25 -725 -1689 C ATOM 2591 CG LEU A1108 113.967 170.822 -26.763 1.00 37.04 C ANISOU 2591 CG LEU A1108 5525 2559 5989 133 -730 -1695 C ATOM 2592 CD1 LEU A1108 115.134 171.788 -26.620 1.00 35.85 C ANISOU 2592 CD1 LEU A1108 5467 2432 5723 173 -536 -1521 C ATOM 2593 CD2 LEU A1108 114.464 169.444 -27.131 1.00 39.30 C ANISOU 2593 CD2 LEU A1108 5890 2788 6256 104 -680 -1788 C ATOM 2594 N TYR A1109 110.753 170.821 -23.444 1.00 48.05 N ANISOU 2594 N TYR A1109 6139 4037 8081 -120 -803 -1673 N ATOM 2595 CA TYR A1109 110.241 170.712 -22.082 1.00 47.84 C ANISOU 2595 CA TYR A1109 5905 4048 8224 -197 -687 -1595 C ATOM 2596 C TYR A1109 109.252 169.563 -21.968 1.00 50.01 C ANISOU 2596 C TYR A1109 6022 4318 8662 -263 -745 -1680 C ATOM 2597 O TYR A1109 109.157 168.927 -20.912 1.00 50.71 O ANISOU 2597 O TYR A1109 5994 4423 8849 -332 -597 -1614 O ATOM 2598 CB TYR A1109 109.587 172.020 -21.642 1.00 46.53 C ANISOU 2598 CB TYR A1109 5652 3883 8145 -156 -726 -1562 C ATOM 2599 CG TYR A1109 110.552 173.131 -21.320 1.00 44.75 C ANISOU 2599 CG TYR A1109 5543 3662 7797 -117 -608 -1441 C ATOM 2600 CD1 TYR A1109 111.869 172.859 -20.973 1.00 32.01 C ANISOU 2600 CD1 TYR A1109 4030 2073 6060 -149 -436 -1343 C ATOM 2601 CD2 TYR A1109 110.148 174.456 -21.364 1.00 45.18 C ANISOU 2601 CD2 TYR A1109 5601 3690 7875 -46 -674 -1426 C ATOM 2602 CE1 TYR A1109 112.760 173.885 -20.671 1.00 30.90 C ANISOU 2602 CE1 TYR A1109 3977 1934 5829 -124 -336 -1236 C ATOM 2603 CE2 TYR A1109 111.029 175.483 -21.069 1.00 43.89 C ANISOU 2603 CE2 TYR A1109 5545 3523 7608 -17 -560 -1313 C ATOM 2604 CZ TYR A1109 112.332 175.189 -20.724 1.00 31.07 C ANISOU 2604 CZ TYR A1109 4007 1928 5869 -64 -393 -1221 C ATOM 2605 OH TYR A1109 113.213 176.207 -20.437 1.00 30.15 O ANISOU 2605 OH TYR A1109 3979 1806 5672 -48 -291 -1115 O ATOM 2606 N GLY A1110 108.542 169.255 -23.051 1.00 51.34 N ANISOU 2606 N GLY A1110 6198 4458 8850 -237 -963 -1828 N ATOM 2607 CA GLY A1110 107.565 168.191 -23.077 1.00 52.41 C ANISOU 2607 CA GLY A1110 6180 4580 9155 -300 -1041 -1922 C ATOM 2608 C GLY A1110 108.117 166.812 -23.343 1.00 52.35 C ANISOU 2608 C GLY A1110 6261 4550 9081 -354 -974 -1950 C ATOM 2609 O GLY A1110 107.357 165.840 -23.324 1.00 54.12 O ANISOU 2609 O GLY A1110 6364 4748 9450 -415 -1018 -2023 O ATOM 2610 N SER A1111 109.423 166.685 -23.568 1.00 49.90 N ANISOU 2610 N SER A1111 6151 4237 8574 -332 -857 -1894 N ATOM 2611 CA SER A1111 110.028 165.423 -23.989 1.00 49.46 C ANISOU 2611 CA SER A1111 6210 4143 8441 -363 -804 -1933 C ATOM 2612 C SER A1111 111.185 164.974 -23.113 1.00 46.63 C ANISOU 2612 C SER A1111 5896 3791 8031 -391 -561 -1792 C ATOM 2613 O SER A1111 111.310 163.779 -22.834 1.00 46.74 O ANISOU 2613 O SER A1111 5895 3773 8091 -444 -482 -1792 O ATOM 2614 CB SER A1111 110.515 165.533 -25.440 1.00 50.79 C ANISOU 2614 CB SER A1111 6614 4281 8403 -281 -933 -2040 C ATOM 2615 OG SER A1111 109.425 165.615 -26.338 1.00 53.32 O ANISOU 2615 OG SER A1111 6910 4595 8753 -252 -1199 -2193 O ATOM 2616 N VAL A1112 112.045 165.896 -22.678 1.00 44.73 N ANISOU 2616 N VAL A1112 5710 3584 7701 -352 -452 -1674 N ATOM 2617 CA VAL A1112 113.143 165.532 -21.792 1.00 42.78 C ANISOU 2617 CA VAL A1112 5485 3354 7416 -370 -253 -1540 C ATOM 2618 C VAL A1112 112.604 165.105 -20.428 1.00 41.22 C ANISOU 2618 C VAL A1112 5110 3185 7366 -432 -161 -1465 C ATOM 2619 O VAL A1112 111.522 165.517 -19.995 1.00 41.97 O ANISOU 2619 O VAL A1112 5060 3296 7590 -452 -209 -1481 O ATOM 2620 CB VAL A1112 114.148 166.689 -21.649 1.00 41.45 C ANISOU 2620 CB VAL A1112 5400 3216 7134 -317 -178 -1438 C ATOM 2621 CG1 VAL A1112 114.730 167.067 -23.003 1.00 42.19 C ANISOU 2621 CG1 VAL A1112 5687 3261 7081 -241 -237 -1509 C ATOM 2622 CG2 VAL A1112 113.489 167.892 -20.966 1.00 41.04 C ANISOU 2622 CG2 VAL A1112 5235 3210 7149 -316 -203 -1388 C ATOM 2623 N ASP A1113 113.370 164.257 -19.748 1.00 39.45 N ANISOU 2623 N ASP A1113 4902 2958 7130 -451 -23 -1387 N ATOM 2624 CA ASP A1113 112.944 163.746 -18.455 1.00 38.25 C ANISOU 2624 CA ASP A1113 4616 2818 7100 -496 78 -1318 C ATOM 2625 C ASP A1113 113.169 164.766 -17.347 1.00 36.20 C ANISOU 2625 C ASP A1113 4311 2622 6823 -479 158 -1203 C ATOM 2626 O ASP A1113 112.306 164.943 -16.476 1.00 36.59 O ANISOU 2626 O ASP A1113 4237 2680 6984 -501 194 -1182 O ATOM 2627 CB ASP A1113 113.671 162.437 -18.165 1.00 38.34 C ANISOU 2627 CB ASP A1113 4674 2790 7102 -510 181 -1285 C ATOM 2628 CG ASP A1113 113.187 161.319 -19.054 1.00 40.14 C ANISOU 2628 CG ASP A1113 4927 2941 7382 -542 111 -1407 C ATOM 2629 OD1 ASP A1113 111.987 161.352 -19.402 1.00 41.33 O ANISOU 2629 OD1 ASP A1113 4988 3075 7641 -575 4 -1502 O ATOM 2630 OD2 ASP A1113 113.986 160.428 -19.422 1.00 40.25 O ANISOU 2630 OD2 ASP A1113 5046 2908 7338 -530 154 -1415 O ATOM 2631 N PHE A1114 114.299 165.469 -17.385 1.00 34.39 N ANISOU 2631 N PHE A1114 4179 2426 6463 -439 189 -1134 N ATOM 2632 CA PHE A1114 114.641 166.452 -16.371 1.00 32.97 C ANISOU 2632 CA PHE A1114 3976 2299 6250 -425 252 -1032 C ATOM 2633 C PHE A1114 115.254 167.671 -17.038 1.00 32.63 C ANISOU 2633 C PHE A1114 4020 2274 6103 -385 204 -1022 C ATOM 2634 O PHE A1114 115.825 167.582 -18.129 1.00 33.54 O ANISOU 2634 O PHE A1114 4238 2359 6148 -358 168 -1065 O ATOM 2635 CB PHE A1114 115.635 165.902 -15.344 1.00 32.18 C ANISOU 2635 CB PHE A1114 3893 2214 6119 -425 370 -934 C ATOM 2636 CG PHE A1114 115.179 164.651 -14.670 1.00 33.42 C ANISOU 2636 CG PHE A1114 3991 2336 6371 -457 438 -932 C ATOM 2637 CD1 PHE A1114 115.456 163.407 -15.221 1.00 34.81 C ANISOU 2637 CD1 PHE A1114 4203 2461 6563 -466 448 -972 C ATOM 2638 CD2 PHE A1114 114.486 164.709 -13.472 1.00 33.46 C ANISOU 2638 CD2 PHE A1114 3916 2345 6452 -474 508 -891 C ATOM 2639 CE1 PHE A1114 115.040 162.252 -14.596 1.00 36.21 C ANISOU 2639 CE1 PHE A1114 4330 2591 6837 -496 520 -967 C ATOM 2640 CE2 PHE A1114 114.076 163.555 -12.841 1.00 30.11 C ANISOU 2640 CE2 PHE A1114 3445 1872 6124 -501 591 -884 C ATOM 2641 CZ PHE A1114 114.353 162.328 -13.403 1.00 36.61 C ANISOU 2641 CZ PHE A1114 4298 2645 6968 -514 595 -920 C ATOM 2642 N VAL A1115 115.129 168.813 -16.368 1.00 31.69 N ANISOU 2642 N VAL A1115 3871 2192 5976 -376 216 -967 N ATOM 2643 CA VAL A1115 115.782 170.049 -16.778 1.00 30.61 C ANISOU 2643 CA VAL A1115 3814 2065 5752 -342 194 -936 C ATOM 2644 C VAL A1115 116.671 170.505 -15.630 1.00 29.66 C ANISOU 2644 C VAL A1115 3694 1986 5588 -348 278 -830 C ATOM 2645 O VAL A1115 116.228 170.552 -14.474 1.00 29.40 O ANISOU 2645 O VAL A1115 3600 1976 5596 -365 319 -796 O ATOM 2646 CB VAL A1115 114.762 171.135 -17.177 1.00 30.52 C ANISOU 2646 CB VAL A1115 3778 2042 5778 -320 104 -985 C ATOM 2647 CG1 VAL A1115 113.880 171.520 -16.000 1.00 27.76 C ANISOU 2647 CG1 VAL A1115 3317 1715 5516 -338 138 -958 C ATOM 2648 CG2 VAL A1115 115.472 172.355 -17.762 1.00 27.57 C ANISOU 2648 CG2 VAL A1115 3508 1654 5312 -279 89 -955 C ATOM 2649 N ILE A1116 117.932 170.801 -15.947 1.00 29.50 N ANISOU 2649 N ILE A1116 3745 1965 5498 -332 306 -786 N ATOM 2650 CA ILE A1116 118.925 171.210 -14.964 1.00 25.30 C ANISOU 2650 CA ILE A1116 3210 1464 4938 -341 362 -699 C ATOM 2651 C ILE A1116 119.003 172.724 -14.968 1.00 28.38 C ANISOU 2651 C ILE A1116 3629 1860 5292 -333 337 -674 C ATOM 2652 O ILE A1116 119.079 173.351 -16.031 1.00 29.10 O ANISOU 2652 O ILE A1116 3779 1919 5360 -310 309 -696 O ATOM 2653 CB ILE A1116 120.299 170.590 -15.260 1.00 25.28 C ANISOU 2653 CB ILE A1116 3237 1447 4922 -332 415 -666 C ATOM 2654 CG1 ILE A1116 120.219 169.071 -15.222 1.00 25.68 C ANISOU 2654 CG1 ILE A1116 3267 1479 5010 -335 446 -690 C ATOM 2655 CG2 ILE A1116 121.321 171.053 -14.240 1.00 24.78 C ANISOU 2655 CG2 ILE A1116 3154 1407 4856 -344 449 -588 C ATOM 2656 CD1 ILE A1116 121.539 168.438 -15.519 1.00 25.82 C ANISOU 2656 CD1 ILE A1116 3307 1470 5032 -316 509 -659 C ATOM 2657 N ILE A1117 118.971 173.314 -13.783 1.00 27.64 N ANISOU 2657 N ILE A1117 3513 1793 5195 -348 351 -631 N ATOM 2658 CA ILE A1117 119.066 174.762 -13.649 1.00 27.33 C ANISOU 2658 CA ILE A1117 3508 1752 5125 -346 331 -607 C ATOM 2659 C ILE A1117 120.078 175.067 -12.554 1.00 26.90 C ANISOU 2659 C ILE A1117 3458 1713 5049 -369 355 -549 C ATOM 2660 O ILE A1117 119.692 175.394 -11.424 1.00 26.84 O ANISOU 2660 O ILE A1117 3451 1713 5036 -378 357 -541 O ATOM 2661 CB ILE A1117 117.699 175.387 -13.344 1.00 24.65 C ANISOU 2661 CB ILE A1117 3144 1407 4814 -334 304 -641 C ATOM 2662 CG1 ILE A1117 116.664 174.899 -14.358 1.00 26.75 C ANISOU 2662 CG1 ILE A1117 3380 1649 5133 -314 259 -713 C ATOM 2663 CG2 ILE A1117 117.805 176.891 -13.359 1.00 24.62 C ANISOU 2663 CG2 ILE A1117 3191 1386 4779 -324 286 -620 C ATOM 2664 CD1 ILE A1117 115.248 175.057 -13.879 1.00 27.12 C ANISOU 2664 CD1 ILE A1117 3351 1688 5264 -308 248 -751 C ATOM 2665 N PRO A1118 121.354 174.961 -12.826 1.00 24.10 N ANISOU 2665 N PRO A1118 3110 1352 4696 -379 373 -515 N ATOM 2666 CA PRO A1118 122.371 175.169 -11.793 1.00 24.05 C ANISOU 2666 CA PRO A1118 3094 1348 4696 -405 375 -470 C ATOM 2667 C PRO A1118 122.800 176.629 -11.662 1.00 26.89 C ANISOU 2667 C PRO A1118 3483 1694 5040 -427 348 -451 C ATOM 2668 O PRO A1118 123.992 176.948 -11.659 1.00 24.43 O ANISOU 2668 O PRO A1118 3153 1366 4762 -453 351 -417 O ATOM 2669 CB PRO A1118 123.520 174.279 -12.276 1.00 24.24 C ANISOU 2669 CB PRO A1118 3085 1360 4767 -402 413 -447 C ATOM 2670 CG PRO A1118 123.425 174.398 -13.783 1.00 24.45 C ANISOU 2670 CG PRO A1118 3137 1363 4788 -380 437 -468 C ATOM 2671 CD PRO A1118 121.945 174.520 -14.103 1.00 24.37 C ANISOU 2671 CD PRO A1118 3157 1361 4743 -363 399 -521 C ATOM 2672 N SER A1119 121.822 177.529 -11.545 1.00 26.64 N ANISOU 2672 N SER A1119 3489 1658 4975 -419 326 -472 N ATOM 2673 CA SER A1119 122.112 178.952 -11.410 1.00 26.87 C ANISOU 2673 CA SER A1119 3560 1661 4989 -439 304 -458 C ATOM 2674 C SER A1119 122.786 179.272 -10.080 1.00 28.29 C ANISOU 2674 C SER A1119 3751 1831 5165 -478 275 -447 C ATOM 2675 O SER A1119 122.511 178.642 -9.055 1.00 28.85 O ANISOU 2675 O SER A1119 3828 1907 5225 -476 270 -458 O ATOM 2676 CB SER A1119 120.830 179.783 -11.529 1.00 26.18 C ANISOU 2676 CB SER A1119 3511 1558 4877 -409 292 -487 C ATOM 2677 OG SER A1119 120.203 179.641 -12.789 1.00 26.06 O ANISOU 2677 OG SER A1119 3497 1531 4875 -372 295 -507 O ATOM 2678 N TYR A1120 123.684 180.261 -10.106 1.00 28.94 N ANISOU 2678 N TYR A1120 3846 1885 5266 -516 255 -428 N ATOM 2679 CA TYR A1120 124.159 180.884 -8.874 1.00 29.43 C ANISOU 2679 CA TYR A1120 3943 1918 5323 -559 202 -438 C ATOM 2680 C TYR A1120 123.149 181.890 -8.341 1.00 30.55 C ANISOU 2680 C TYR A1120 4170 2032 5406 -547 190 -470 C ATOM 2681 O TYR A1120 123.066 182.115 -7.125 1.00 30.72 O ANISOU 2681 O TYR A1120 4251 2022 5399 -562 157 -498 O ATOM 2682 CB TYR A1120 125.503 181.584 -9.112 1.00 28.64 C ANISOU 2682 CB TYR A1120 3807 1787 5288 -616 182 -412 C ATOM 2683 CG TYR A1120 126.685 180.649 -9.343 1.00 28.17 C ANISOU 2683 CG TYR A1120 3647 1738 5319 -632 193 -381 C ATOM 2684 CD1 TYR A1120 127.033 180.237 -10.624 1.00 28.32 C ANISOU 2684 CD1 TYR A1120 3612 1765 5384 -610 267 -347 C ATOM 2685 CD2 TYR A1120 127.461 180.190 -8.281 1.00 28.05 C ANISOU 2685 CD2 TYR A1120 3597 1707 5355 -663 129 -386 C ATOM 2686 CE1 TYR A1120 128.114 179.386 -10.842 1.00 28.72 C ANISOU 2686 CE1 TYR A1120 3566 1812 5534 -616 294 -316 C ATOM 2687 CE2 TYR A1120 128.538 179.341 -8.489 1.00 28.48 C ANISOU 2687 CE2 TYR A1120 3542 1759 5518 -669 136 -353 C ATOM 2688 CZ TYR A1120 128.863 178.945 -9.772 1.00 28.89 C ANISOU 2688 CZ TYR A1120 3533 1825 5621 -644 227 -316 C ATOM 2689 OH TYR A1120 129.935 178.104 -9.995 1.00 29.55 O ANISOU 2689 OH TYR A1120 3504 1895 5829 -642 253 -280 O ATOM 2690 N PHE A1121 122.366 182.477 -9.241 1.00 31.81 N ANISOU 2690 N PHE A1121 4344 2189 5555 -512 217 -470 N ATOM 2691 CA PHE A1121 121.554 183.645 -8.927 1.00 33.72 C ANISOU 2691 CA PHE A1121 4659 2388 5766 -496 211 -493 C ATOM 2692 C PHE A1121 120.343 183.635 -9.839 1.00 34.47 C ANISOU 2692 C PHE A1121 4742 2489 5867 -433 243 -500 C ATOM 2693 O PHE A1121 120.480 183.702 -11.069 1.00 34.62 O ANISOU 2693 O PHE A1121 4747 2502 5906 -418 255 -479 O ATOM 2694 CB PHE A1121 122.362 184.937 -9.090 1.00 34.73 C ANISOU 2694 CB PHE A1121 4828 2461 5906 -540 190 -479 C ATOM 2695 CG PHE A1121 121.574 186.186 -8.845 1.00 34.89 C ANISOU 2695 CG PHE A1121 4933 2423 5900 -518 188 -501 C ATOM 2696 CD1 PHE A1121 121.132 186.505 -7.570 1.00 34.95 C ANISOU 2696 CD1 PHE A1121 5011 2399 5869 -516 168 -545 C ATOM 2697 CD2 PHE A1121 121.288 187.047 -9.888 1.00 34.62 C ANISOU 2697 CD2 PHE A1121 4922 2349 5883 -491 213 -477 C ATOM 2698 CE1 PHE A1121 120.409 187.654 -7.343 1.00 34.95 C ANISOU 2698 CE1 PHE A1121 5090 2335 5853 -487 175 -568 C ATOM 2699 CE2 PHE A1121 120.565 188.205 -9.667 1.00 34.68 C ANISOU 2699 CE2 PHE A1121 5008 2292 5877 -461 214 -495 C ATOM 2700 CZ PHE A1121 120.125 188.507 -8.395 1.00 34.86 C ANISOU 2700 CZ PHE A1121 5088 2290 5866 -458 197 -542 C ATOM 2701 N GLU A1122 119.165 183.520 -9.239 1.00 34.88 N ANISOU 2701 N GLU A1122 4799 2539 5914 -395 260 -533 N ATOM 2702 CA GLU A1122 117.929 183.378 -10.003 1.00 35.40 C ANISOU 2702 CA GLU A1122 4827 2607 6018 -337 280 -551 C ATOM 2703 C GLU A1122 116.772 183.932 -9.188 1.00 36.78 C ANISOU 2703 C GLU A1122 5022 2746 6208 -299 309 -584 C ATOM 2704 O GLU A1122 116.076 183.201 -8.479 1.00 36.25 O ANISOU 2704 O GLU A1122 4915 2692 6166 -287 349 -606 O ATOM 2705 CB GLU A1122 117.677 181.917 -10.362 1.00 35.50 C ANISOU 2705 CB GLU A1122 4759 2670 6060 -331 291 -560 C ATOM 2706 CG GLU A1122 116.490 181.757 -11.243 1.00 37.49 C ANISOU 2706 CG GLU A1122 4963 2911 6371 -282 286 -592 C ATOM 2707 CD GLU A1122 116.654 182.546 -12.529 1.00 40.01 C ANISOU 2707 CD GLU A1122 5328 3188 6688 -254 254 -581 C ATOM 2708 OE1 GLU A1122 117.374 182.057 -13.432 1.00 41.41 O ANISOU 2708 OE1 GLU A1122 5512 3370 6850 -264 245 -567 O ATOM 2709 OE2 GLU A1122 116.087 183.660 -12.633 1.00 41.14 O ANISOU 2709 OE2 GLU A1122 5511 3277 6844 -215 247 -584 O ATOM 2710 N PRO A1123 116.556 185.240 -9.242 1.00 38.61 N ANISOU 2710 N PRO A1123 5317 2919 6433 -277 304 -586 N ATOM 2711 CA PRO A1123 115.447 185.855 -8.466 1.00 40.39 C ANISOU 2711 CA PRO A1123 5566 3098 6682 -229 346 -619 C ATOM 2712 C PRO A1123 114.049 185.346 -8.798 1.00 42.08 C ANISOU 2712 C PRO A1123 5683 3316 6992 -169 383 -644 C ATOM 2713 O PRO A1123 113.168 185.350 -7.928 1.00 44.10 O ANISOU 2713 O PRO A1123 5922 3547 7289 -139 449 -671 O ATOM 2714 CB PRO A1123 115.576 187.354 -8.790 1.00 40.84 C ANISOU 2714 CB PRO A1123 5709 3084 6723 -210 328 -609 C ATOM 2715 CG PRO A1123 117.010 187.518 -9.294 1.00 40.32 C ANISOU 2715 CG PRO A1123 5677 3027 6616 -276 283 -571 C ATOM 2716 CD PRO A1123 117.408 186.230 -9.928 1.00 39.40 C ANISOU 2716 CD PRO A1123 5478 2982 6510 -297 274 -554 C ATOM 2717 N PHE A1124 113.808 184.945 -10.038 1.00 41.65 N ANISOU 2717 N PHE A1124 5562 3276 6986 -149 343 -643 N ATOM 2718 CA PHE A1124 112.454 184.712 -10.516 1.00 42.21 C ANISOU 2718 CA PHE A1124 5532 3327 7178 -88 345 -679 C ATOM 2719 C PHE A1124 112.167 183.279 -10.906 1.00 41.00 C ANISOU 2719 C PHE A1124 5268 3222 7089 -109 330 -704 C ATOM 2720 O PHE A1124 111.041 182.820 -10.724 1.00 41.62 O ANISOU 2720 O PHE A1124 5235 3288 7291 -84 356 -742 O ATOM 2721 CB PHE A1124 112.175 185.614 -11.710 1.00 28.34 C ANISOU 2721 CB PHE A1124 3805 1514 5449 -22 284 -674 C ATOM 2722 CG PHE A1124 112.850 186.932 -11.598 1.00 35.99 C ANISOU 2722 CG PHE A1124 4905 2434 6336 -21 292 -636 C ATOM 2723 CD1 PHE A1124 112.317 187.928 -10.793 1.00 29.17 C ANISOU 2723 CD1 PHE A1124 4085 1517 5483 17 338 -644 C ATOM 2724 CD2 PHE A1124 114.031 187.178 -12.273 1.00 35.66 C ANISOU 2724 CD2 PHE A1124 4941 2389 6218 -59 264 -594 C ATOM 2725 CE1 PHE A1124 112.940 189.145 -10.685 1.00 29.49 C ANISOU 2725 CE1 PHE A1124 4248 1503 5455 12 339 -616 C ATOM 2726 CE2 PHE A1124 114.657 188.390 -12.165 1.00 28.55 C ANISOU 2726 CE2 PHE A1124 4148 1433 5266 -69 274 -561 C ATOM 2727 CZ PHE A1124 114.112 189.375 -11.371 1.00 29.19 C ANISOU 2727 CZ PHE A1124 4275 1461 5354 -37 303 -574 C ATOM 2728 N GLY A1125 113.137 182.568 -11.468 1.00 40.61 N ANISOU 2728 N GLY A1125 5238 3218 6975 -152 293 -685 N ATOM 2729 CA GLY A1125 112.956 181.159 -11.779 1.00 40.11 C ANISOU 2729 CA GLY A1125 5086 3194 6960 -176 283 -711 C ATOM 2730 C GLY A1125 112.001 180.876 -12.919 1.00 40.17 C ANISOU 2730 C GLY A1125 5012 3174 7077 -133 208 -768 C ATOM 2731 O GLY A1125 111.255 179.892 -12.865 1.00 40.67 O ANISOU 2731 O GLY A1125 4962 3245 7244 -145 208 -813 O ATOM 2732 N LEU A1126 111.991 181.726 -13.947 1.00 39.44 N ANISOU 2732 N LEU A1126 4978 3033 6975 -79 136 -772 N ATOM 2733 CA LEU A1126 110.988 181.587 -14.996 1.00 39.38 C ANISOU 2733 CA LEU A1126 4901 2981 7082 -15 29 -840 C ATOM 2734 C LEU A1126 111.147 180.282 -15.776 1.00 38.78 C ANISOU 2734 C LEU A1126 4793 2931 7012 -45 -33 -890 C ATOM 2735 O LEU A1126 110.150 179.699 -16.224 1.00 39.26 O ANISOU 2735 O LEU A1126 4743 2971 7202 -24 -120 -971 O ATOM 2736 CB LEU A1126 111.049 182.791 -15.924 1.00 39.73 C ANISOU 2736 CB LEU A1126 5050 2954 7093 69 -39 -823 C ATOM 2737 CG LEU A1126 110.038 182.726 -17.060 1.00 41.55 C ANISOU 2737 CG LEU A1126 5227 3127 7432 164 -196 -900 C ATOM 2738 CD1 LEU A1126 108.615 182.806 -16.528 1.00 42.01 C ANISOU 2738 CD1 LEU A1126 5118 3165 7680 205 -219 -951 C ATOM 2739 CD2 LEU A1126 110.329 183.840 -18.037 1.00 42.97 C ANISOU 2739 CD2 LEU A1126 5556 3249 7523 263 -260 -855 C ATOM 2740 N VAL A1127 112.381 179.800 -15.948 1.00 38.19 N ANISOU 2740 N VAL A1127 4807 2893 6813 -92 5 -850 N ATOM 2741 CA VAL A1127 112.575 178.543 -16.675 1.00 38.14 C ANISOU 2741 CA VAL A1127 4787 2902 6802 -115 -39 -898 C ATOM 2742 C VAL A1127 112.003 177.357 -15.899 1.00 28.15 C ANISOU 2742 C VAL A1127 3391 1679 5625 -169 0 -926 C ATOM 2743 O VAL A1127 111.562 176.371 -16.499 1.00 28.78 O ANISOU 2743 O VAL A1127 3416 1753 5767 -179 -64 -998 O ATOM 2744 CB VAL A1127 114.067 178.354 -17.020 1.00 37.05 C ANISOU 2744 CB VAL A1127 4767 2779 6529 -142 14 -843 C ATOM 2745 CG1 VAL A1127 114.433 176.881 -17.110 1.00 27.27 C ANISOU 2745 CG1 VAL A1127 3500 1577 5283 -186 31 -867 C ATOM 2746 CG2 VAL A1127 114.390 179.070 -18.332 1.00 37.29 C ANISOU 2746 CG2 VAL A1127 4925 2735 6508 -74 -45 -851 C ATOM 2747 N ALA A1128 111.984 177.428 -14.563 1.00 27.64 N ANISOU 2747 N ALA A1128 3287 1644 5570 -201 106 -876 N ATOM 2748 CA ALA A1128 111.395 176.345 -13.777 1.00 27.85 C ANISOU 2748 CA ALA A1128 3201 1688 5691 -241 167 -893 C ATOM 2749 C ALA A1128 109.880 176.291 -13.944 1.00 29.10 C ANISOU 2749 C ALA A1128 3209 1800 6046 -221 120 -971 C ATOM 2750 O ALA A1128 109.295 175.203 -14.027 1.00 29.76 O ANISOU 2750 O ALA A1128 3187 1878 6242 -253 113 -1022 O ATOM 2751 CB ALA A1128 111.764 176.501 -12.300 1.00 27.24 C ANISOU 2751 CB ALA A1128 3149 1633 5565 -264 289 -824 C ATOM 2752 N LEU A1129 109.228 177.453 -13.989 1.00 29.60 N ANISOU 2752 N LEU A1129 3253 1822 6174 -167 88 -983 N ATOM 2753 CA LEU A1129 107.788 177.467 -14.203 1.00 36.16 C ANISOU 2753 CA LEU A1129 3916 2596 7228 -136 26 -1064 C ATOM 2754 C LEU A1129 107.436 176.945 -15.590 1.00 38.45 C ANISOU 2754 C LEU A1129 4168 2864 7579 -119 -158 -1161 C ATOM 2755 O LEU A1129 106.456 176.206 -15.753 1.00 40.75 O ANISOU 2755 O LEU A1129 4295 3128 8059 -139 -216 -1244 O ATOM 2756 CB LEU A1129 107.240 178.882 -14.012 1.00 35.67 C ANISOU 2756 CB LEU A1129 3852 2483 7217 -60 24 -1051 C ATOM 2757 CG LEU A1129 107.210 179.445 -12.590 1.00 31.12 C ANISOU 2757 CG LEU A1129 3295 1906 6624 -66 198 -985 C ATOM 2758 CD1 LEU A1129 106.716 180.877 -12.594 1.00 31.71 C ANISOU 2758 CD1 LEU A1129 3389 1926 6732 22 185 -976 C ATOM 2759 CD2 LEU A1129 106.340 178.580 -11.695 1.00 31.85 C ANISOU 2759 CD2 LEU A1129 3229 1979 6892 -107 315 -1007 C ATOM 2760 N GLU A1130 108.238 177.291 -16.599 1.00 37.58 N ANISOU 2760 N GLU A1130 4211 2756 7312 -83 -252 -1160 N ATOM 2761 CA GLU A1130 107.922 176.847 -17.951 1.00 37.95 C ANISOU 2761 CA GLU A1130 4261 2772 7385 -50 -446 -1266 C ATOM 2762 C GLU A1130 108.158 175.349 -18.111 1.00 37.99 C ANISOU 2762 C GLU A1130 4241 2813 7379 -128 -435 -1305 C ATOM 2763 O GLU A1130 107.346 174.648 -18.727 1.00 39.04 O ANISOU 2763 O GLU A1130 4274 2925 7636 -135 -571 -1415 O ATOM 2764 CB GLU A1130 108.738 177.642 -18.966 1.00 37.03 C ANISOU 2764 CB GLU A1130 4345 2630 7093 26 -524 -1248 C ATOM 2765 CG GLU A1130 108.364 179.111 -19.002 1.00 37.28 C ANISOU 2765 CG GLU A1130 4408 2640 7116 124 -557 -1199 C ATOM 2766 CD GLU A1130 109.264 179.914 -19.914 1.00 37.56 C ANISOU 2766 CD GLU A1130 4657 2689 6924 197 -584 -1128 C ATOM 2767 OE1 GLU A1130 110.259 179.342 -20.411 1.00 37.98 O ANISOU 2767 OE1 GLU A1130 4830 2754 6849 165 -554 -1121 O ATOM 2768 OE2 GLU A1130 108.981 181.115 -20.127 1.00 37.69 O ANISOU 2768 OE2 GLU A1130 4724 2697 6900 290 -618 -1074 O ATOM 2769 N ALA A1131 109.253 174.833 -17.548 1.00 37.02 N ANISOU 2769 N ALA A1131 4204 2742 7120 -182 -284 -1219 N ATOM 2770 CA ALA A1131 109.515 173.404 -17.654 1.00 37.65 C ANISOU 2770 CA ALA A1131 4272 2843 7189 -241 -260 -1244 C ATOM 2771 C ALA A1131 108.453 172.602 -16.914 1.00 39.29 C ANISOU 2771 C ALA A1131 4290 3043 7594 -291 -216 -1276 C ATOM 2772 O ALA A1131 107.902 171.638 -17.454 1.00 41.35 O ANISOU 2772 O ALA A1131 4478 3284 7949 -318 -297 -1365 O ATOM 2773 CB ALA A1131 110.910 173.087 -17.118 1.00 30.08 C ANISOU 2773 CB ALA A1131 3433 1930 6067 -272 -117 -1140 C ATOM 2774 N MET A1132 108.123 173.009 -15.687 1.00 38.43 N ANISOU 2774 N MET A1132 4107 2938 7558 -300 -83 -1211 N ATOM 2775 CA MET A1132 107.153 172.261 -14.892 1.00 39.07 C ANISOU 2775 CA MET A1132 4015 2994 7836 -342 1 -1230 C ATOM 2776 C MET A1132 105.750 172.319 -15.479 1.00 41.48 C ANISOU 2776 C MET A1132 4133 3242 8384 -329 -135 -1345 C ATOM 2777 O MET A1132 104.944 171.415 -15.235 1.00 42.41 O ANISOU 2777 O MET A1132 4097 3330 8686 -372 -105 -1390 O ATOM 2778 CB MET A1132 107.152 172.786 -13.462 1.00 37.63 C ANISOU 2778 CB MET A1132 3825 2814 7659 -341 182 -1139 C ATOM 2779 CG MET A1132 108.480 172.612 -12.757 1.00 36.46 C ANISOU 2779 CG MET A1132 3839 2718 7297 -355 292 -1037 C ATOM 2780 SD MET A1132 108.606 173.517 -11.209 1.00 36.49 S ANISOU 2780 SD MET A1132 3889 2720 7255 -339 452 -948 S ATOM 2781 CE MET A1132 107.386 172.702 -10.204 1.00 38.37 C ANISOU 2781 CE MET A1132 3963 2896 7721 -369 608 -961 C ATOM 2782 N CYS A1133 105.424 173.381 -16.217 1.00 43.19 N ANISOU 2782 N CYS A1133 4354 3435 8621 -265 -288 -1394 N ATOM 2783 CA CYS A1133 104.143 173.432 -16.911 1.00 46.27 C ANISOU 2783 CA CYS A1133 4564 3770 9245 -242 -474 -1519 C ATOM 2784 C CYS A1133 104.052 172.416 -18.038 1.00 46.50 C ANISOU 2784 C CYS A1133 4595 3805 9266 -266 -653 -1627 C ATOM 2785 O CYS A1133 102.945 172.019 -18.412 1.00 49.51 O ANISOU 2785 O CYS A1133 4792 4153 9866 -277 -788 -1733 O ATOM 2786 CB CYS A1133 103.887 174.835 -17.462 1.00 48.20 C ANISOU 2786 CB CYS A1133 4841 3975 9497 -145 -618 -1545 C ATOM 2787 SG CYS A1133 103.329 176.033 -16.221 1.00 48.76 S ANISOU 2787 SG CYS A1133 4824 3999 9705 -101 -448 -1467 S ATOM 2788 N LEU A1134 105.184 171.997 -18.595 1.00 44.03 N ANISOU 2788 N LEU A1134 4486 3531 8712 -273 -657 -1607 N ATOM 2789 CA LEU A1134 105.216 170.974 -19.632 1.00 44.01 C ANISOU 2789 CA LEU A1134 4526 3528 8669 -294 -800 -1708 C ATOM 2790 C LEU A1134 105.688 169.620 -19.111 1.00 45.10 C ANISOU 2790 C LEU A1134 4678 3679 8779 -375 -636 -1665 C ATOM 2791 O LEU A1134 105.990 168.724 -19.909 1.00 38.66 O ANISOU 2791 O LEU A1134 3945 2858 7887 -395 -712 -1731 O ATOM 2792 CB LEU A1134 106.082 171.440 -20.803 1.00 38.15 C ANISOU 2792 CB LEU A1134 4015 2791 7688 -227 -933 -1737 C ATOM 2793 CG LEU A1134 105.368 172.497 -21.641 1.00 39.44 C ANISOU 2793 CG LEU A1134 4170 2921 7895 -131 -1179 -1827 C ATOM 2794 CD1 LEU A1134 106.240 173.714 -21.863 1.00 38.21 C ANISOU 2794 CD1 LEU A1134 4217 2755 7547 -44 -1155 -1751 C ATOM 2795 CD2 LEU A1134 104.924 171.901 -22.957 1.00 41.51 C ANISOU 2795 CD2 LEU A1134 4466 3174 8133 -104 -1449 -1984 C ATOM 2796 N GLY A1135 105.762 169.457 -17.792 1.00 45.76 N ANISOU 2796 N GLY A1135 4700 3772 8916 -411 -416 -1560 N ATOM 2797 CA GLY A1135 106.057 168.185 -17.172 1.00 45.73 C ANISOU 2797 CA GLY A1135 4694 3765 8917 -474 -266 -1519 C ATOM 2798 C GLY A1135 107.522 167.856 -16.945 1.00 43.97 C ANISOU 2798 C GLY A1135 4667 3581 8461 -478 -150 -1423 C ATOM 2799 O GLY A1135 107.813 166.812 -16.346 1.00 44.55 O ANISOU 2799 O GLY A1135 4743 3644 8539 -519 -25 -1381 O ATOM 2800 N ALA A1136 108.458 168.689 -17.392 1.00 42.89 N ANISOU 2800 N ALA A1136 4684 3476 8134 -432 -185 -1386 N ATOM 2801 CA ALA A1136 109.861 168.396 -17.128 1.00 40.76 C ANISOU 2801 CA ALA A1136 4570 3238 7678 -433 -74 -1294 C ATOM 2802 C ALA A1136 110.140 168.525 -15.636 1.00 39.31 C ANISOU 2802 C ALA A1136 4361 3082 7494 -445 100 -1176 C ATOM 2803 O ALA A1136 109.539 169.356 -14.948 1.00 39.72 O ANISOU 2803 O ALA A1136 4336 3136 7619 -432 136 -1151 O ATOM 2804 CB ALA A1136 110.771 169.328 -17.923 1.00 39.54 C ANISOU 2804 CB ALA A1136 4573 3099 7350 -381 -135 -1280 C ATOM 2805 N ILE A1137 111.025 167.678 -15.124 1.00 37.57 N ANISOU 2805 N ILE A1137 4207 2872 7197 -464 204 -1112 N ATOM 2806 CA ILE A1137 111.334 167.632 -13.696 1.00 35.97 C ANISOU 2806 CA ILE A1137 3998 2685 6983 -469 352 -1011 C ATOM 2807 C ILE A1137 112.582 168.470 -13.454 1.00 33.61 C ANISOU 2807 C ILE A1137 3823 2434 6514 -438 369 -930 C ATOM 2808 O ILE A1137 113.654 168.129 -13.983 1.00 33.55 O ANISOU 2808 O ILE A1137 3909 2436 6403 -429 353 -914 O ATOM 2809 CB ILE A1137 111.544 166.197 -13.194 1.00 30.58 C ANISOU 2809 CB ILE A1137 3312 1972 6337 -500 446 -989 C ATOM 2810 CG1 ILE A1137 110.254 165.384 -13.287 1.00 32.21 C ANISOU 2810 CG1 ILE A1137 3380 2118 6739 -540 449 -1066 C ATOM 2811 CG2 ILE A1137 112.040 166.227 -11.760 1.00 29.89 C ANISOU 2811 CG2 ILE A1137 3257 1894 6206 -493 583 -885 C ATOM 2812 CD1 ILE A1137 110.441 163.914 -12.964 1.00 32.85 C ANISOU 2812 CD1 ILE A1137 3467 2151 6863 -573 536 -1053 C ATOM 2813 N PRO A1138 112.503 169.536 -12.658 1.00 31.81 N ANISOU 2813 N PRO A1138 3595 2226 6266 -421 406 -881 N ATOM 2814 CA PRO A1138 113.656 170.430 -12.485 1.00 29.59 C ANISOU 2814 CA PRO A1138 3422 1982 5840 -397 403 -816 C ATOM 2815 C PRO A1138 114.645 169.929 -11.445 1.00 27.98 C ANISOU 2815 C PRO A1138 3273 1790 5570 -403 488 -738 C ATOM 2816 O PRO A1138 114.265 169.488 -10.359 1.00 28.07 O ANISOU 2816 O PRO A1138 3256 1780 5630 -414 576 -711 O ATOM 2817 CB PRO A1138 113.008 171.744 -12.034 1.00 29.51 C ANISOU 2817 CB PRO A1138 3389 1971 5853 -379 402 -812 C ATOM 2818 CG PRO A1138 111.794 171.295 -11.279 1.00 30.73 C ANISOU 2818 CG PRO A1138 3430 2090 6157 -395 477 -833 C ATOM 2819 CD PRO A1138 111.307 170.022 -11.952 1.00 31.92 C ANISOU 2819 CD PRO A1138 3505 2215 6407 -422 451 -894 C ATOM 2820 N ILE A1139 115.925 170.003 -11.791 1.00 26.98 N ANISOU 2820 N ILE A1139 3224 1684 5345 -393 465 -704 N ATOM 2821 CA ILE A1139 117.025 169.796 -10.854 1.00 26.42 C ANISOU 2821 CA ILE A1139 3202 1619 5218 -391 515 -633 C ATOM 2822 C ILE A1139 117.728 171.141 -10.739 1.00 26.14 C ANISOU 2822 C ILE A1139 3219 1606 5106 -382 478 -602 C ATOM 2823 O ILE A1139 118.528 171.513 -11.607 1.00 26.53 O ANISOU 2823 O ILE A1139 3299 1665 5115 -374 438 -600 O ATOM 2824 CB ILE A1139 117.990 168.699 -11.314 1.00 26.04 C ANISOU 2824 CB ILE A1139 3175 1558 5159 -388 528 -622 C ATOM 2825 CG1 ILE A1139 117.272 167.365 -11.477 1.00 26.89 C ANISOU 2825 CG1 ILE A1139 3240 1631 5346 -402 563 -660 C ATOM 2826 CG2 ILE A1139 119.089 168.514 -10.303 1.00 25.29 C ANISOU 2826 CG2 ILE A1139 3118 1457 5035 -380 567 -551 C ATOM 2827 CD1 ILE A1139 118.152 166.307 -12.104 1.00 26.87 C ANISOU 2827 CD1 ILE A1139 3267 1604 5337 -393 574 -662 C ATOM 2828 N ALA A1140 117.436 171.887 -9.679 1.00 25.39 N ANISOU 2828 N ALA A1140 3141 1507 4999 -383 499 -580 N ATOM 2829 CA ALA A1140 117.810 173.290 -9.637 1.00 24.53 C ANISOU 2829 CA ALA A1140 3078 1408 4833 -379 456 -568 C ATOM 2830 C ALA A1140 118.578 173.620 -8.365 1.00 28.82 C ANISOU 2830 C ALA A1140 3683 1936 5333 -387 470 -524 C ATOM 2831 O ALA A1140 118.480 172.924 -7.350 1.00 29.32 O ANISOU 2831 O ALA A1140 3761 1969 5408 -388 523 -506 O ATOM 2832 CB ALA A1140 116.573 174.185 -9.753 1.00 24.79 C ANISOU 2832 CB ALA A1140 3086 1432 4900 -367 449 -605 C ATOM 2833 N SER A1141 119.376 174.686 -8.457 1.00 27.54 N ANISOU 2833 N SER A1141 3562 1778 5124 -396 420 -511 N ATOM 2834 CA SER A1141 119.991 175.288 -7.279 1.00 26.71 C ANISOU 2834 CA SER A1141 3523 1642 4983 -410 405 -490 C ATOM 2835 C SER A1141 118.916 175.783 -6.323 1.00 27.31 C ANISOU 2835 C SER A1141 3642 1685 5050 -398 446 -510 C ATOM 2836 O SER A1141 117.915 176.369 -6.745 1.00 27.75 O ANISOU 2836 O SER A1141 3671 1747 5125 -382 459 -538 O ATOM 2837 CB SER A1141 120.873 176.478 -7.671 1.00 25.20 C ANISOU 2837 CB SER A1141 3356 1454 4765 -431 344 -483 C ATOM 2838 OG SER A1141 121.942 176.123 -8.522 1.00 24.24 O ANISOU 2838 OG SER A1141 3192 1348 4670 -441 330 -460 O ATOM 2839 N ALA A1142 119.133 175.583 -5.026 1.00 26.98 N ANISOU 2839 N ALA A1142 3673 1591 4987 -399 471 -498 N ATOM 2840 CA ALA A1142 118.180 176.073 -4.034 1.00 25.88 C ANISOU 2840 CA ALA A1142 3597 1401 4836 -381 536 -518 C ATOM 2841 C ALA A1142 118.490 177.534 -3.692 1.00 32.71 C ANISOU 2841 C ALA A1142 4546 2238 5644 -388 476 -541 C ATOM 2842 O ALA A1142 118.967 177.865 -2.608 1.00 26.69 O ANISOU 2842 O ALA A1142 3896 1410 4833 -393 460 -550 O ATOM 2843 CB ALA A1142 118.201 175.185 -2.797 1.00 26.56 C ANISOU 2843 CB ALA A1142 3758 1420 4915 -368 611 -494 C ATOM 2844 N VAL A1143 118.195 178.421 -4.646 1.00 32.13 N ANISOU 2844 N VAL A1143 4428 2201 5579 -387 442 -556 N ATOM 2845 CA VAL A1143 118.371 179.863 -4.447 1.00 32.82 C ANISOU 2845 CA VAL A1143 4591 2256 5624 -392 396 -577 C ATOM 2846 C VAL A1143 117.255 180.622 -5.160 1.00 33.43 C ANISOU 2846 C VAL A1143 4626 2342 5735 -359 424 -596 C ATOM 2847 O VAL A1143 116.766 180.198 -6.211 1.00 32.32 O ANISOU 2847 O VAL A1143 4390 2243 5647 -346 430 -592 O ATOM 2848 CB VAL A1143 119.753 180.359 -4.939 1.00 32.55 C ANISOU 2848 CB VAL A1143 4562 2235 5571 -438 301 -561 C ATOM 2849 CG1 VAL A1143 120.886 179.712 -4.140 1.00 33.39 C ANISOU 2849 CG1 VAL A1143 4703 2313 5671 -471 260 -550 C ATOM 2850 CG2 VAL A1143 119.919 180.119 -6.431 1.00 31.53 C ANISOU 2850 CG2 VAL A1143 4336 2166 5476 -438 293 -537 C ATOM 2851 N GLY A1144 116.870 181.764 -4.580 1.00 34.64 N ANISOU 2851 N GLY A1144 4859 2441 5862 -340 435 -623 N ATOM 2852 CA GLY A1144 116.015 182.724 -5.279 1.00 35.12 C ANISOU 2852 CA GLY A1144 4893 2491 5958 -304 445 -637 C ATOM 2853 C GLY A1144 114.636 182.197 -5.612 1.00 35.39 C ANISOU 2853 C GLY A1144 4824 2534 6088 -262 522 -650 C ATOM 2854 O GLY A1144 113.933 181.632 -4.768 1.00 35.18 O ANISOU 2854 O GLY A1144 4787 2483 6098 -245 616 -661 O ATOM 2855 N GLY A1145 114.225 182.418 -6.861 1.00 36.18 N ANISOU 2855 N GLY A1145 4849 2653 6243 -242 485 -652 N ATOM 2856 CA GLY A1145 112.922 181.950 -7.290 1.00 37.90 C ANISOU 2856 CA GLY A1145 4949 2868 6584 -207 529 -677 C ATOM 2857 C GLY A1145 112.838 180.444 -7.447 1.00 39.20 C ANISOU 2857 C GLY A1145 5022 3073 6799 -234 547 -677 C ATOM 2858 O GLY A1145 111.751 179.869 -7.333 1.00 40.06 O ANISOU 2858 O GLY A1145 5029 3164 7029 -220 611 -702 O ATOM 2859 N LEU A1146 113.968 179.777 -7.702 1.00 39.65 N ANISOU 2859 N LEU A1146 5106 3176 6785 -274 498 -650 N ATOM 2860 CA LEU A1146 113.953 178.315 -7.725 1.00 40.56 C ANISOU 2860 CA LEU A1146 5153 3318 6939 -296 525 -647 C ATOM 2861 C LEU A1146 113.653 177.748 -6.342 1.00 42.52 C ANISOU 2861 C LEU A1146 5421 3533 7201 -301 633 -637 C ATOM 2862 O LEU A1146 112.905 176.772 -6.207 1.00 43.13 O ANISOU 2862 O LEU A1146 5416 3600 7373 -305 705 -646 O ATOM 2863 CB LEU A1146 115.286 177.774 -8.238 1.00 39.28 C ANISOU 2863 CB LEU A1146 5022 3199 6702 -326 464 -618 C ATOM 2864 CG LEU A1146 115.831 178.306 -9.566 1.00 38.71 C ANISOU 2864 CG LEU A1146 4961 3145 6602 -322 386 -617 C ATOM 2865 CD1 LEU A1146 117.273 177.847 -9.766 1.00 38.41 C ANISOU 2865 CD1 LEU A1146 4956 3134 6504 -352 362 -580 C ATOM 2866 CD2 LEU A1146 114.962 177.874 -10.738 1.00 38.86 C ANISOU 2866 CD2 LEU A1146 4904 3162 6699 -301 357 -659 C ATOM 2867 N ARG A1147 114.211 178.364 -5.297 1.00 44.23 N ANISOU 2867 N ARG A1147 5757 3717 7329 -300 649 -622 N ATOM 2868 CA ARG A1147 113.902 177.933 -3.940 1.00 46.91 C ANISOU 2868 CA ARG A1147 6155 4002 7667 -292 764 -614 C ATOM 2869 C ARG A1147 112.445 178.206 -3.593 1.00 48.23 C ANISOU 2869 C ARG A1147 6267 4120 7938 -257 888 -638 C ATOM 2870 O ARG A1147 111.851 177.471 -2.797 1.00 48.80 O ANISOU 2870 O ARG A1147 6330 4147 8063 -251 1025 -627 O ATOM 2871 CB ARG A1147 114.837 178.626 -2.946 1.00 49.35 C ANISOU 2871 CB ARG A1147 6626 4270 7855 -294 732 -609 C ATOM 2872 CG ARG A1147 114.799 178.083 -1.525 1.00 52.65 C ANISOU 2872 CG ARG A1147 7154 4616 8235 -279 841 -596 C ATOM 2873 CD ARG A1147 115.510 179.032 -0.554 1.00 56.63 C ANISOU 2873 CD ARG A1147 7836 5058 8622 -272 798 -619 C ATOM 2874 NE ARG A1147 116.970 178.949 -0.649 1.00 60.14 N ANISOU 2874 NE ARG A1147 8323 5515 9014 -314 656 -611 N ATOM 2875 CZ ARG A1147 117.823 179.584 0.159 1.00 64.37 C ANISOU 2875 CZ ARG A1147 9004 5987 9466 -325 583 -640 C ATOM 2876 NH1 ARG A1147 119.132 179.434 -0.017 1.00 64.94 N ANISOU 2876 NH1 ARG A1147 9077 6065 9534 -372 455 -633 N ATOM 2877 NH2 ARG A1147 117.379 180.367 1.143 1.00 66.85 N ANISOU 2877 NH2 ARG A1147 9466 6226 9709 -290 639 -684 N ATOM 2878 N ASP A1148 111.853 179.250 -4.181 1.00 49.43 N ANISOU 2878 N ASP A1148 6380 4268 8132 -229 856 -667 N ATOM 2879 CA ASP A1148 110.435 179.523 -3.965 1.00 51.41 C ANISOU 2879 CA ASP A1148 6549 4467 8519 -190 973 -692 C ATOM 2880 C ASP A1148 109.568 178.529 -4.724 1.00 49.70 C ANISOU 2880 C ASP A1148 6143 4261 8478 -205 991 -710 C ATOM 2881 O ASP A1148 108.624 177.955 -4.167 1.00 50.98 O ANISOU 2881 O ASP A1148 6223 4373 8772 -202 1135 -713 O ATOM 2882 CB ASP A1148 110.090 180.953 -4.403 1.00 54.74 C ANISOU 2882 CB ASP A1148 6984 4868 8944 -145 923 -716 C ATOM 2883 CG ASP A1148 110.806 182.023 -3.584 1.00 58.00 C ANISOU 2883 CG ASP A1148 7582 5251 9206 -131 912 -713 C ATOM 2884 OD1 ASP A1148 111.125 181.775 -2.402 1.00 59.30 O ANISOU 2884 OD1 ASP A1148 7860 5381 9291 -135 988 -706 O ATOM 2885 OD2 ASP A1148 111.037 183.128 -4.129 1.00 58.21 O ANISOU 2885 OD2 ASP A1148 7647 5274 9194 -114 827 -721 O ATOM 2886 N ILE A1149 109.885 178.304 -5.999 1.00 48.60 N ANISOU 2886 N ILE A1149 5940 4178 8348 -223 851 -725 N ATOM 2887 CA ILE A1149 108.993 177.540 -6.864 1.00 48.25 C ANISOU 2887 CA ILE A1149 5721 4132 8481 -233 830 -765 C ATOM 2888 C ILE A1149 109.046 176.060 -6.518 1.00 46.86 C ANISOU 2888 C ILE A1149 5500 3961 8346 -278 900 -752 C ATOM 2889 O ILE A1149 108.013 175.421 -6.289 1.00 47.59 O ANISOU 2889 O ILE A1149 5460 4005 8617 -288 1000 -773 O ATOM 2890 CB ILE A1149 109.348 177.797 -8.340 1.00 47.69 C ANISOU 2890 CB ILE A1149 5634 4103 8383 -228 658 -791 C ATOM 2891 CG1 ILE A1149 108.955 179.225 -8.715 1.00 49.08 C ANISOU 2891 CG1 ILE A1149 5828 4246 8573 -171 610 -807 C ATOM 2892 CG2 ILE A1149 108.674 176.797 -9.254 1.00 47.45 C ANISOU 2892 CG2 ILE A1149 5453 4071 8505 -246 603 -845 C ATOM 2893 CD1 ILE A1149 109.365 179.618 -10.096 1.00 49.47 C ANISOU 2893 CD1 ILE A1149 5903 4316 8577 -153 459 -822 C ATOM 2894 N ILE A1150 110.249 175.506 -6.440 1.00 45.03 N ANISOU 2894 N ILE A1150 5370 3775 7965 -303 859 -714 N ATOM 2895 CA ILE A1150 110.417 174.061 -6.377 1.00 43.94 C ANISOU 2895 CA ILE A1150 5195 3642 7858 -338 897 -701 C ATOM 2896 C ILE A1150 110.285 173.589 -4.939 1.00 45.20 C ANISOU 2896 C ILE A1150 5410 3744 8019 -340 1067 -656 C ATOM 2897 O ILE A1150 110.950 174.101 -4.030 1.00 44.67 O ANISOU 2897 O ILE A1150 5490 3663 7820 -323 1096 -619 O ATOM 2898 CB ILE A1150 111.766 173.648 -6.977 1.00 41.38 C ANISOU 2898 CB ILE A1150 4950 3380 7395 -354 787 -678 C ATOM 2899 CG1 ILE A1150 111.834 174.093 -8.436 1.00 40.41 C ANISOU 2899 CG1 ILE A1150 4792 3294 7269 -346 647 -719 C ATOM 2900 CG2 ILE A1150 111.959 172.151 -6.849 1.00 41.05 C ANISOU 2900 CG2 ILE A1150 4883 3331 7384 -380 835 -662 C ATOM 2901 CD1 ILE A1150 113.227 174.172 -8.963 1.00 26.39 C ANISOU 2901 CD1 ILE A1150 3113 1565 5349 -350 564 -689 C ATOM 2902 N THR A1151 109.446 172.594 -4.742 1.00 47.37 N ANISOU 2902 N THR A1151 5577 3975 8446 -359 1180 -663 N ATOM 2903 CA THR A1151 109.201 172.003 -3.447 1.00 49.87 C ANISOU 2903 CA THR A1151 5945 4219 8783 -357 1374 -613 C ATOM 2904 C THR A1151 109.793 170.599 -3.411 1.00 50.79 C ANISOU 2904 C THR A1151 6082 4338 8876 -384 1386 -580 C ATOM 2905 O THR A1151 110.337 170.092 -4.398 1.00 50.47 O ANISOU 2905 O THR A1151 6008 4355 8813 -403 1251 -601 O ATOM 2906 CB THR A1151 107.703 171.992 -3.150 1.00 51.77 C ANISOU 2906 CB THR A1151 6040 4383 9247 -355 1538 -637 C ATOM 2907 OG1 THR A1151 107.006 171.355 -4.226 1.00 52.19 O ANISOU 2907 OG1 THR A1151 5896 4445 9487 -387 1467 -698 O ATOM 2908 CG2 THR A1151 107.196 173.415 -2.994 1.00 52.39 C ANISOU 2908 CG2 THR A1151 6126 4443 9337 -314 1550 -659 C ATOM 2909 N ASN A1152 109.698 169.976 -2.239 1.00 52.12 N ANISOU 2909 N ASN A1152 6324 4433 9044 -377 1564 -521 N ATOM 2910 CA ASN A1152 110.268 168.650 -2.071 1.00 54.06 C ANISOU 2910 CA ASN A1152 6609 4664 9267 -392 1593 -478 C ATOM 2911 C ASN A1152 109.596 167.636 -2.982 1.00 54.88 C ANISOU 2911 C ASN A1152 6538 4770 9546 -431 1581 -525 C ATOM 2912 O ASN A1152 110.239 166.675 -3.421 1.00 54.92 O ANISOU 2912 O ASN A1152 6555 4793 9519 -446 1519 -518 O ATOM 2913 CB ASN A1152 110.143 168.222 -0.613 1.00 56.42 C ANISOU 2913 CB ASN A1152 7033 4865 9538 -366 1810 -399 C ATOM 2914 CG ASN A1152 110.869 166.939 -0.332 1.00 57.93 C ANISOU 2914 CG ASN A1152 7297 5030 9683 -367 1837 -339 C ATOM 2915 OD1 ASN A1152 111.861 166.617 -0.987 1.00 57.33 O ANISOU 2915 OD1 ASN A1152 7236 5012 9534 -375 1676 -345 O ATOM 2916 ND2 ASN A1152 110.374 166.185 0.641 1.00 59.77 N ANISOU 2916 ND2 ASN A1152 7579 5167 9966 -352 2056 -276 N ATOM 2917 N GLU A1153 108.312 167.833 -3.278 1.00 54.49 N ANISOU 2917 N GLU A1153 6323 4689 9691 -444 1637 -579 N ATOM 2918 CA GLU A1153 107.535 166.895 -4.077 1.00 53.51 C ANISOU 2918 CA GLU A1153 6025 4545 9762 -482 1622 -639 C ATOM 2919 C GLU A1153 107.576 167.176 -5.574 1.00 51.04 C ANISOU 2919 C GLU A1153 5628 4303 9462 -495 1395 -725 C ATOM 2920 O GLU A1153 107.064 166.366 -6.351 1.00 51.18 O ANISOU 2920 O GLU A1153 5527 4304 9617 -526 1344 -786 O ATOM 2921 CB GLU A1153 106.083 166.891 -3.594 1.00 54.87 C ANISOU 2921 CB GLU A1153 6044 4625 10180 -487 1805 -658 C ATOM 2922 CG GLU A1153 105.909 166.302 -2.209 1.00 55.82 C ANISOU 2922 CG GLU A1153 6244 4651 10314 -473 2068 -571 C ATOM 2923 CD GLU A1153 104.454 166.030 -1.872 1.00 58.35 C ANISOU 2923 CD GLU A1153 6385 4866 10918 -480 2268 -592 C ATOM 2924 OE1 GLU A1153 103.643 166.984 -1.885 1.00 58.88 O ANISOU 2924 OE1 GLU A1153 6349 4914 11110 -463 2303 -627 O ATOM 2925 OE2 GLU A1153 104.119 164.853 -1.600 1.00 59.93 O ANISOU 2925 OE2 GLU A1153 6543 4994 11232 -498 2395 -573 O ATOM 2926 N THR A1154 108.181 168.283 -6.000 1.00 48.91 N ANISOU 2926 N THR A1154 5431 4103 9050 -470 1259 -731 N ATOM 2927 CA THR A1154 108.092 168.718 -7.388 1.00 47.64 C ANISOU 2927 CA THR A1154 5204 3993 8904 -471 1067 -807 C ATOM 2928 C THR A1154 109.453 169.104 -7.948 1.00 45.65 C ANISOU 2928 C THR A1154 5098 3820 8429 -455 930 -784 C ATOM 2929 O THR A1154 109.557 170.028 -8.760 1.00 45.31 O ANISOU 2929 O THR A1154 5061 3814 8339 -436 804 -817 O ATOM 2930 CB THR A1154 107.122 169.887 -7.526 1.00 48.06 C ANISOU 2930 CB THR A1154 5156 4028 9076 -449 1051 -851 C ATOM 2931 OG1 THR A1154 107.704 171.054 -6.935 1.00 47.13 O ANISOU 2931 OG1 THR A1154 5170 3935 8803 -414 1065 -801 O ATOM 2932 CG2 THR A1154 105.820 169.564 -6.816 1.00 49.63 C ANISOU 2932 CG2 THR A1154 5202 4135 9520 -461 1224 -863 C ATOM 2933 N GLY A1155 110.499 168.419 -7.519 1.00 44.52 N ANISOU 2933 N GLY A1155 5066 3687 8162 -458 961 -725 N ATOM 2934 CA GLY A1155 111.825 168.673 -8.039 1.00 28.94 C ANISOU 2934 CA GLY A1155 3206 1775 6015 -443 849 -702 C ATOM 2935 C GLY A1155 112.879 168.310 -7.018 1.00 31.26 C ANISOU 2935 C GLY A1155 3620 2060 6197 -434 915 -622 C ATOM 2936 O GLY A1155 112.582 167.854 -5.915 1.00 29.23 O ANISOU 2936 O GLY A1155 3381 1747 5978 -434 1048 -581 O ATOM 2937 N ILE A1156 114.128 168.538 -7.421 1.00 30.06 N ANISOU 2937 N ILE A1156 3550 1953 5919 -421 824 -600 N ATOM 2938 CA ILE A1156 115.311 168.231 -6.623 1.00 29.81 C ANISOU 2938 CA ILE A1156 3622 1910 5795 -408 847 -533 C ATOM 2939 C ILE A1156 116.149 169.496 -6.505 1.00 29.44 C ANISOU 2939 C ILE A1156 3650 1898 5640 -394 769 -516 C ATOM 2940 O ILE A1156 116.677 169.985 -7.512 1.00 28.80 O ANISOU 2940 O ILE A1156 3561 1862 5519 -393 676 -536 O ATOM 2941 CB ILE A1156 116.148 167.105 -7.251 1.00 29.57 C ANISOU 2941 CB ILE A1156 3597 1881 5757 -409 821 -525 C ATOM 2942 CG1 ILE A1156 115.294 165.855 -7.483 1.00 30.25 C ANISOU 2942 CG1 ILE A1156 3611 1925 5958 -430 887 -554 C ATOM 2943 CG2 ILE A1156 117.376 166.807 -6.396 1.00 29.49 C ANISOU 2943 CG2 ILE A1156 3679 1845 5679 -389 839 -453 C ATOM 2944 CD1 ILE A1156 115.970 164.818 -8.358 1.00 30.27 C ANISOU 2944 CD1 ILE A1156 3618 1923 5960 -432 852 -569 C ATOM 2945 N LEU A1157 116.269 170.027 -5.290 1.00 29.80 N ANISOU 2945 N LEU A1157 3776 1906 5640 -383 815 -480 N ATOM 2946 CA LEU A1157 117.132 171.171 -5.026 1.00 29.49 C ANISOU 2946 CA LEU A1157 3817 1881 5509 -377 738 -469 C ATOM 2947 C LEU A1157 118.529 170.712 -4.632 1.00 30.13 C ANISOU 2947 C LEU A1157 3964 1940 5543 -372 701 -423 C ATOM 2948 O LEU A1157 118.707 169.637 -4.052 1.00 31.58 O ANISOU 2948 O LEU A1157 4176 2076 5748 -361 764 -385 O ATOM 2949 CB LEU A1157 116.549 172.058 -3.928 1.00 29.70 C ANISOU 2949 CB LEU A1157 3915 1860 5511 -365 795 -471 C ATOM 2950 CG LEU A1157 115.246 172.759 -4.313 1.00 29.94 C ANISOU 2950 CG LEU A1157 3870 1902 5605 -362 826 -516 C ATOM 2951 CD1 LEU A1157 114.717 173.569 -3.143 1.00 30.68 C ANISOU 2951 CD1 LEU A1157 4049 1934 5675 -340 911 -516 C ATOM 2952 CD2 LEU A1157 115.450 173.645 -5.533 1.00 29.06 C ANISOU 2952 CD2 LEU A1157 3716 1851 5474 -365 708 -549 C ATOM 2953 N VAL A1158 119.520 171.549 -4.951 1.00 28.98 N ANISOU 2953 N VAL A1158 3840 1821 5352 -380 604 -424 N ATOM 2954 CA VAL A1158 120.929 171.283 -4.681 1.00 28.65 C ANISOU 2954 CA VAL A1158 3832 1753 5301 -380 553 -387 C ATOM 2955 C VAL A1158 121.603 172.597 -4.314 1.00 25.76 C ANISOU 2955 C VAL A1158 3519 1375 4894 -399 469 -398 C ATOM 2956 O VAL A1158 121.162 173.678 -4.720 1.00 25.45 O ANISOU 2956 O VAL A1158 3472 1370 4827 -411 443 -430 O ATOM 2957 CB VAL A1158 121.655 170.636 -5.888 1.00 25.38 C ANISOU 2957 CB VAL A1158 3337 1380 4926 -380 529 -383 C ATOM 2958 CG1 VAL A1158 120.918 169.401 -6.380 1.00 25.50 C ANISOU 2958 CG1 VAL A1158 3304 1400 4983 -369 599 -392 C ATOM 2959 CG2 VAL A1158 121.822 171.655 -7.015 1.00 31.00 C ANISOU 2959 CG2 VAL A1158 4008 2149 5621 -395 472 -412 C ATOM 2960 N LYS A1159 122.679 172.501 -3.532 1.00 26.30 N ANISOU 2960 N LYS A1159 3640 1381 4972 -401 421 -371 N ATOM 2961 CA LYS A1159 123.400 173.705 -3.138 1.00 28.99 C ANISOU 2961 CA LYS A1159 4024 1695 5295 -431 324 -393 C ATOM 2962 C LYS A1159 124.009 174.366 -4.366 1.00 28.99 C ANISOU 2962 C LYS A1159 3926 1767 5321 -462 273 -400 C ATOM 2963 O LYS A1159 124.645 173.703 -5.196 1.00 29.09 O ANISOU 2963 O LYS A1159 3852 1810 5393 -456 282 -375 O ATOM 2964 CB LYS A1159 124.497 173.381 -2.132 1.00 27.52 C ANISOU 2964 CB LYS A1159 3894 1412 5151 -427 254 -370 C ATOM 2965 CG LYS A1159 125.100 174.638 -1.541 1.00 28.14 C ANISOU 2965 CG LYS A1159 4027 1444 5221 -468 132 -415 C ATOM 2966 CD LYS A1159 126.514 174.450 -1.042 1.00 29.11 C ANISOU 2966 CD LYS A1159 4122 1579 5359 -463 -18 -382 C ATOM 2967 CE LYS A1159 127.134 175.811 -0.742 1.00 34.93 C ANISOU 2967 CE LYS A1159 4874 2317 6082 -521 -163 -437 C ATOM 2968 NZ LYS A1159 128.599 175.715 -0.499 1.00 35.74 N ANISOU 2968 NZ LYS A1159 4890 2449 6241 -531 -330 -410 N ATOM 2969 N ALA A1160 123.852 175.684 -4.468 1.00 28.89 N ANISOU 2969 N ALA A1160 3940 1767 5270 -488 233 -432 N ATOM 2970 CA ALA A1160 124.321 176.367 -5.664 1.00 25.60 C ANISOU 2970 CA ALA A1160 3449 1402 4875 -510 212 -429 C ATOM 2971 C ALA A1160 125.839 176.276 -5.769 1.00 40.19 C ANISOU 2971 C ALA A1160 5227 3232 6812 -541 155 -403 C ATOM 2972 O ALA A1160 126.560 176.280 -4.765 1.00 26.87 O ANISOU 2972 O ALA A1160 3560 1485 5166 -563 79 -406 O ATOM 2973 CB ALA A1160 123.876 177.829 -5.664 1.00 31.70 C ANISOU 2973 CB ALA A1160 4276 2173 5596 -529 187 -460 C ATOM 2974 N GLY A1161 126.320 176.144 -7.002 1.00 39.82 N ANISOU 2974 N GLY A1161 5093 3224 6814 -539 190 -380 N ATOM 2975 CA GLY A1161 127.738 176.181 -7.271 1.00 40.40 C ANISOU 2975 CA GLY A1161 5071 3277 7001 -568 158 -350 C ATOM 2976 C GLY A1161 128.508 174.939 -6.884 1.00 40.39 C ANISOU 2976 C GLY A1161 5007 3241 7097 -546 149 -317 C ATOM 2977 O GLY A1161 129.745 174.963 -6.917 1.00 41.29 O ANISOU 2977 O GLY A1161 5021 3326 7342 -570 105 -288 O ATOM 2978 N ASP A1162 127.825 173.842 -6.561 1.00 40.51 N ANISOU 2978 N ASP A1162 5069 3251 7072 -500 194 -313 N ATOM 2979 CA ASP A1162 128.491 172.657 -6.029 1.00 41.38 C ANISOU 2979 CA ASP A1162 5145 3305 7273 -468 185 -273 C ATOM 2980 C ASP A1162 128.359 171.530 -7.034 1.00 44.14 C ANISOU 2980 C ASP A1162 5451 3680 7639 -422 292 -255 C ATOM 2981 O ASP A1162 127.290 170.908 -7.134 1.00 41.64 O ANISOU 2981 O ASP A1162 5193 3386 7241 -396 355 -273 O ATOM 2982 CB ASP A1162 127.888 172.251 -4.681 1.00 40.94 C ANISOU 2982 CB ASP A1162 5203 3189 7163 -447 160 -275 C ATOM 2983 CG ASP A1162 128.734 171.235 -3.942 1.00 41.09 C ANISOU 2983 CG ASP A1162 5205 3138 7268 -401 114 -217 C ATOM 2984 OD1 ASP A1162 129.324 170.362 -4.605 1.00 41.59 O ANISOU 2984 OD1 ASP A1162 5179 3200 7424 -369 162 -176 O ATOM 2985 OD2 ASP A1162 128.807 171.318 -2.700 1.00 42.30 O ANISOU 2985 OD2 ASP A1162 5451 3295 7326 -375 23 -203 O ATOM 2986 N PRO A1163 129.388 171.269 -7.837 1.00 48.67 N ANISOU 2986 N PRO A1163 5922 4246 8326 -414 320 -225 N ATOM 2987 CA PRO A1163 129.301 170.173 -8.814 1.00 50.53 C ANISOU 2987 CA PRO A1163 6138 4488 8574 -366 427 -219 C ATOM 2988 C PRO A1163 129.063 168.804 -8.206 1.00 52.56 C ANISOU 2988 C PRO A1163 6429 4704 8838 -316 457 -196 C ATOM 2989 O PRO A1163 128.366 167.979 -8.822 1.00 54.12 O ANISOU 2989 O PRO A1163 6659 4921 8985 -290 533 -220 O ATOM 2990 CB PRO A1163 130.651 170.267 -9.554 1.00 27.65 C ANISOU 2990 CB PRO A1163 3120 1560 5825 -364 459 -180 C ATOM 2991 CG PRO A1163 131.138 171.671 -9.306 1.00 51.23 C ANISOU 2991 CG PRO A1163 6065 4555 8844 -428 379 -181 C ATOM 2992 CD PRO A1163 130.669 171.992 -7.923 1.00 50.31 C ANISOU 2992 CD PRO A1163 6021 4428 8666 -452 264 -199 C ATOM 2993 N GLY A1164 129.595 168.551 -7.013 1.00 50.60 N ANISOU 2993 N GLY A1164 6183 4388 8654 -301 390 -151 N ATOM 2994 CA GLY A1164 129.437 167.244 -6.407 1.00 48.57 C ANISOU 2994 CA GLY A1164 5973 4074 8406 -241 430 -110 C ATOM 2995 C GLY A1164 128.052 167.019 -5.839 1.00 47.49 C ANISOU 2995 C GLY A1164 5956 3951 8136 -246 468 -138 C ATOM 2996 O GLY A1164 127.565 165.881 -5.790 1.00 46.00 O ANISOU 2996 O GLY A1164 5805 3742 7930 -210 547 -123 O ATOM 2997 N GLU A1165 127.396 168.096 -5.415 1.00 47.41 N ANISOU 2997 N GLU A1165 6000 3971 8044 -292 423 -177 N ATOM 2998 CA GLU A1165 125.988 168.018 -5.060 1.00 48.52 C ANISOU 2998 CA GLU A1165 6226 4131 8079 -299 479 -207 C ATOM 2999 C GLU A1165 125.139 167.739 -6.289 1.00 45.57 C ANISOU 2999 C GLU A1165 5809 3833 7673 -310 541 -256 C ATOM 3000 O GLU A1165 124.203 166.933 -6.235 1.00 44.66 O ANISOU 3000 O GLU A1165 5715 3713 7540 -301 608 -265 O ATOM 3001 CB GLU A1165 125.547 169.326 -4.410 1.00 52.32 C ANISOU 3001 CB GLU A1165 6769 4618 8492 -336 421 -240 C ATOM 3002 CG GLU A1165 124.446 169.180 -3.394 1.00 57.05 C ANISOU 3002 CG GLU A1165 7478 5176 9022 -323 480 -240 C ATOM 3003 CD GLU A1165 124.996 168.984 -2.002 1.00 63.59 C ANISOU 3003 CD GLU A1165 8418 5884 9859 -287 451 -190 C ATOM 3004 OE1 GLU A1165 126.186 168.607 -1.892 1.00 66.26 O ANISOU 3004 OE1 GLU A1165 8719 6203 10253 -257 373 -142 O ATOM 3005 OE2 GLU A1165 124.249 169.224 -1.025 1.00 65.97 O ANISOU 3005 OE2 GLU A1165 8846 6132 10089 -274 498 -192 O ATOM 3006 N LEU A1166 125.460 168.391 -7.412 1.00 46.20 N ANISOU 3006 N LEU A1166 5829 3967 7758 -328 517 -286 N ATOM 3007 CA LEU A1166 124.666 168.221 -8.624 1.00 47.31 C ANISOU 3007 CA LEU A1166 5950 4157 7868 -332 554 -337 C ATOM 3008 C LEU A1166 124.859 166.838 -9.235 1.00 50.41 C ANISOU 3008 C LEU A1166 6322 4522 8308 -301 617 -336 C ATOM 3009 O LEU A1166 123.915 166.272 -9.797 1.00 52.45 O ANISOU 3009 O LEU A1166 6587 4792 8549 -305 647 -381 O ATOM 3010 CB LEU A1166 125.007 169.316 -9.633 1.00 45.89 C ANISOU 3010 CB LEU A1166 5744 4016 7675 -349 522 -359 C ATOM 3011 CG LEU A1166 124.325 169.323 -11.006 1.00 24.96 C ANISOU 3011 CG LEU A1166 3095 1393 4994 -345 541 -412 C ATOM 3012 CD1 LEU A1166 122.809 169.366 -10.917 1.00 24.76 C ANISOU 3012 CD1 LEU A1166 3091 1391 4924 -355 529 -456 C ATOM 3013 CD2 LEU A1166 124.848 170.506 -11.804 1.00 24.84 C ANISOU 3013 CD2 LEU A1166 3076 1390 4971 -357 522 -412 C ATOM 3014 N ALA A1167 126.066 166.275 -9.143 1.00 50.98 N ANISOU 3014 N ALA A1167 6366 4549 8456 -270 635 -288 N ATOM 3015 CA ALA A1167 126.255 164.915 -9.633 1.00 26.93 C ANISOU 3015 CA ALA A1167 3312 1463 5455 -233 706 -286 C ATOM 3016 C ALA A1167 125.419 163.928 -8.827 1.00 38.07 C ANISOU 3016 C ALA A1167 4770 2840 6853 -227 744 -275 C ATOM 3017 O ALA A1167 124.778 163.036 -9.394 1.00 38.24 O ANISOU 3017 O ALA A1167 4799 2853 6877 -228 792 -314 O ATOM 3018 CB ALA A1167 127.730 164.520 -9.578 1.00 27.60 C ANISOU 3018 CB ALA A1167 3347 1493 5646 -187 726 -224 C ATOM 3019 N ASN A1168 125.382 164.090 -7.500 1.00 37.90 N ANISOU 3019 N ASN A1168 4790 2787 6823 -222 727 -225 N ATOM 3020 CA ASN A1168 124.573 163.192 -6.684 1.00 37.55 C ANISOU 3020 CA ASN A1168 4801 2696 6769 -213 790 -203 C ATOM 3021 C ASN A1168 123.095 163.312 -7.043 1.00 36.63 C ANISOU 3021 C ASN A1168 4676 2624 6618 -260 813 -270 C ATOM 3022 O ASN A1168 122.380 162.306 -7.096 1.00 37.68 O ANISOU 3022 O ASN A1168 4808 2726 6781 -264 881 -282 O ATOM 3023 CB ASN A1168 124.782 163.485 -5.194 1.00 37.91 C ANISOU 3023 CB ASN A1168 4924 2683 6797 -192 773 -134 C ATOM 3024 CG ASN A1168 126.194 163.141 -4.700 1.00 38.22 C ANISOU 3024 CG ASN A1168 4969 2649 6903 -129 739 -53 C ATOM 3025 OD1 ASN A1168 126.907 162.329 -5.301 1.00 37.72 O ANISOU 3025 OD1 ASN A1168 4857 2568 6909 -90 766 -33 O ATOM 3026 ND2 ASN A1168 126.589 163.751 -3.587 1.00 39.30 N ANISOU 3026 ND2 ASN A1168 5170 2732 7031 -109 674 -5 N ATOM 3027 N ALA A1169 122.625 164.532 -7.328 1.00 34.79 N ANISOU 3027 N ALA A1169 4426 2455 6339 -293 757 -314 N ATOM 3028 CA ALA A1169 121.223 164.715 -7.692 1.00 26.85 C ANISOU 3028 CA ALA A1169 3394 1482 5326 -326 769 -374 C ATOM 3029 C ALA A1169 120.910 164.051 -9.022 1.00 26.97 C ANISOU 3029 C ALA A1169 3367 1508 5373 -335 769 -436 C ATOM 3030 O ALA A1169 119.838 163.462 -9.196 1.00 27.44 O ANISOU 3030 O ALA A1169 3400 1551 5476 -357 801 -476 O ATOM 3031 CB ALA A1169 120.887 166.204 -7.753 1.00 26.20 C ANISOU 3031 CB ALA A1169 3308 1455 5192 -346 706 -400 C ATOM 3032 N ILE A1170 121.827 164.154 -9.982 1.00 26.74 N ANISOU 3032 N ILE A1170 3334 1492 5333 -319 737 -448 N ATOM 3033 CA ILE A1170 121.609 163.523 -11.274 1.00 27.06 C ANISOU 3033 CA ILE A1170 3367 1523 5391 -321 736 -513 C ATOM 3034 C ILE A1170 121.634 162.014 -11.143 1.00 31.23 C ANISOU 3034 C ILE A1170 3904 1985 5977 -310 805 -507 C ATOM 3035 O ILE A1170 120.948 161.303 -11.887 1.00 28.49 O ANISOU 3035 O ILE A1170 3554 1611 5659 -329 808 -573 O ATOM 3036 CB ILE A1170 122.658 164.022 -12.275 1.00 26.82 C ANISOU 3036 CB ILE A1170 3347 1504 5337 -298 715 -520 C ATOM 3037 CG1 ILE A1170 122.356 165.473 -12.650 1.00 26.34 C ANISOU 3037 CG1 ILE A1170 3287 1497 5223 -315 650 -541 C ATOM 3038 CG2 ILE A1170 122.699 163.112 -13.479 1.00 27.46 C ANISOU 3038 CG2 ILE A1170 3456 1545 5434 -285 738 -579 C ATOM 3039 CD1 ILE A1170 123.491 166.155 -13.342 1.00 26.64 C ANISOU 3039 CD1 ILE A1170 3333 1537 5251 -296 651 -523 C ATOM 3040 N LEU A1171 122.448 161.499 -10.222 1.00 31.92 N ANISOU 3040 N LEU A1171 4008 2033 6088 -278 854 -429 N ATOM 3041 CA LEU A1171 122.408 160.081 -9.897 1.00 32.79 C ANISOU 3041 CA LEU A1171 4136 2068 6254 -263 931 -408 C ATOM 3042 C LEU A1171 121.095 159.709 -9.228 1.00 34.35 C ANISOU 3042 C LEU A1171 4325 2243 6482 -301 972 -418 C ATOM 3043 O LEU A1171 120.535 158.641 -9.499 1.00 36.61 O ANISOU 3043 O LEU A1171 4606 2477 6829 -318 1021 -451 O ATOM 3044 CB LEU A1171 123.594 159.728 -9.003 1.00 32.34 C ANISOU 3044 CB LEU A1171 4107 1964 6218 -208 965 -311 C ATOM 3045 CG LEU A1171 124.897 159.484 -9.756 1.00 31.73 C ANISOU 3045 CG LEU A1171 4016 1870 6171 -159 971 -299 C ATOM 3046 CD1 LEU A1171 126.092 159.440 -8.817 1.00 31.68 C ANISOU 3046 CD1 LEU A1171 4011 1820 6205 -99 975 -197 C ATOM 3047 CD2 LEU A1171 124.770 158.185 -10.521 1.00 32.31 C ANISOU 3047 CD2 LEU A1171 4107 1886 6283 -148 1033 -340 C ATOM 3048 N LYS A1172 120.569 160.590 -8.376 1.00 33.21 N ANISOU 3048 N LYS A1172 4179 2129 6310 -317 964 -394 N ATOM 3049 CA LYS A1172 119.275 160.314 -7.761 1.00 33.30 C ANISOU 3049 CA LYS A1172 4170 2112 6370 -350 1028 -403 C ATOM 3050 C LYS A1172 118.159 160.326 -8.798 1.00 29.97 C ANISOU 3050 C LYS A1172 3677 1712 6000 -397 992 -503 C ATOM 3051 O LYS A1172 117.290 159.448 -8.789 1.00 30.99 O ANISOU 3051 O LYS A1172 3768 1786 6219 -427 1051 -532 O ATOM 3052 CB LYS A1172 118.989 161.328 -6.653 1.00 29.47 C ANISOU 3052 CB LYS A1172 3711 1644 5841 -348 1038 -360 C ATOM 3053 CG LYS A1172 119.774 161.078 -5.367 1.00 33.95 C ANISOU 3053 CG LYS A1172 4372 2152 6377 -303 1090 -258 C ATOM 3054 CD LYS A1172 119.543 162.177 -4.334 1.00 29.68 C ANISOU 3054 CD LYS A1172 3885 1616 5778 -300 1090 -228 C ATOM 3055 CE LYS A1172 119.944 161.733 -2.935 1.00 32.32 C ANISOU 3055 CE LYS A1172 4340 1856 6084 -251 1168 -127 C ATOM 3056 NZ LYS A1172 119.184 160.527 -2.458 1.00 33.53 N ANISOU 3056 NZ LYS A1172 4507 1932 6299 -250 1316 -91 N ATOM 3057 N ALA A1173 118.181 161.290 -9.721 1.00 29.21 N ANISOU 3057 N ALA A1173 3562 1682 5855 -403 893 -557 N ATOM 3058 CA ALA A1173 117.116 161.360 -10.715 1.00 37.20 C ANISOU 3058 CA ALA A1173 4517 2701 6915 -439 838 -653 C ATOM 3059 C ALA A1173 117.097 160.112 -11.589 1.00 38.38 C ANISOU 3059 C ALA A1173 4673 2791 7117 -452 840 -711 C ATOM 3060 O ALA A1173 116.024 159.629 -11.970 1.00 31.50 O ANISOU 3060 O ALA A1173 3748 1883 6338 -494 830 -782 O ATOM 3061 CB ALA A1173 117.284 162.611 -11.575 1.00 28.74 C ANISOU 3061 CB ALA A1173 3453 1696 5770 -430 734 -689 C ATOM 3062 N LEU A1174 118.276 159.557 -11.893 1.00 38.23 N ANISOU 3062 N LEU A1174 4717 2751 7057 -417 855 -685 N ATOM 3063 CA LEU A1174 118.338 158.309 -12.650 1.00 39.04 C ANISOU 3063 CA LEU A1174 4846 2781 7206 -423 871 -739 C ATOM 3064 C LEU A1174 117.699 157.154 -11.880 1.00 39.59 C ANISOU 3064 C LEU A1174 4888 2774 7381 -451 965 -721 C ATOM 3065 O LEU A1174 116.973 156.335 -12.458 1.00 40.24 O ANISOU 3065 O LEU A1174 4952 2795 7544 -491 958 -799 O ATOM 3066 CB LEU A1174 119.795 157.988 -12.988 1.00 38.48 C ANISOU 3066 CB LEU A1174 4841 2695 7082 -368 895 -702 C ATOM 3067 CG LEU A1174 120.090 156.545 -13.411 1.00 38.94 C ANISOU 3067 CG LEU A1174 4943 2660 7191 -357 950 -729 C ATOM 3068 CD1 LEU A1174 119.420 156.238 -14.735 1.00 39.43 C ANISOU 3068 CD1 LEU A1174 5031 2688 7262 -389 879 -857 C ATOM 3069 CD2 LEU A1174 121.594 156.277 -13.482 1.00 38.71 C ANISOU 3069 CD2 LEU A1174 4961 2613 7133 -288 1000 -669 C ATOM 3070 N GLU A1175 117.957 157.070 -10.570 1.00 39.37 N ANISOU 3070 N GLU A1175 4867 2734 7357 -430 1054 -621 N ATOM 3071 CA GLU A1175 117.325 156.026 -9.774 1.00 40.70 C ANISOU 3071 CA GLU A1175 5021 2818 7627 -451 1166 -592 C ATOM 3072 C GLU A1175 115.817 156.190 -9.754 1.00 41.40 C ANISOU 3072 C GLU A1175 5016 2897 7815 -513 1172 -653 C ATOM 3073 O GLU A1175 115.090 155.194 -9.767 1.00 42.94 O ANISOU 3073 O GLU A1175 5173 3010 8131 -552 1233 -687 O ATOM 3074 CB GLU A1175 117.897 156.029 -8.356 1.00 41.77 C ANISOU 3074 CB GLU A1175 5208 2934 7728 -407 1257 -468 C ATOM 3075 CG GLU A1175 117.249 155.026 -7.441 1.00 46.20 C ANISOU 3075 CG GLU A1175 5771 3398 8384 -421 1397 -422 C ATOM 3076 CD GLU A1175 117.269 153.631 -8.030 1.00 51.46 C ANISOU 3076 CD GLU A1175 6445 3974 9133 -435 1437 -459 C ATOM 3077 OE1 GLU A1175 118.316 153.248 -8.602 1.00 52.96 O ANISOU 3077 OE1 GLU A1175 6688 4157 9278 -395 1400 -457 O ATOM 3078 OE2 GLU A1175 116.237 152.922 -7.940 1.00 54.52 O ANISOU 3078 OE2 GLU A1175 6782 4290 9642 -486 1510 -493 O ATOM 3079 N LEU A1176 115.330 157.427 -9.750 1.00 40.57 N ANISOU 3079 N LEU A1176 4865 2868 7680 -520 1111 -671 N ATOM 3080 CA LEU A1176 113.892 157.642 -9.822 1.00 41.81 C ANISOU 3080 CA LEU A1176 4915 3015 7958 -571 1111 -736 C ATOM 3081 C LEU A1176 113.330 157.259 -11.178 1.00 42.58 C ANISOU 3081 C LEU A1176 4967 3090 8121 -613 1005 -860 C ATOM 3082 O LEU A1176 112.145 156.921 -11.283 1.00 43.87 O ANISOU 3082 O LEU A1176 5030 3205 8436 -663 1015 -924 O ATOM 3083 CB LEU A1176 113.567 159.099 -9.523 1.00 41.18 C ANISOU 3083 CB LEU A1176 4803 3013 7831 -559 1071 -725 C ATOM 3084 CG LEU A1176 113.568 159.475 -8.055 1.00 41.46 C ANISOU 3084 CG LEU A1176 4865 3041 7848 -536 1192 -628 C ATOM 3085 CD1 LEU A1176 113.380 160.972 -7.937 1.00 40.96 C ANISOU 3085 CD1 LEU A1176 4788 3052 7723 -522 1134 -630 C ATOM 3086 CD2 LEU A1176 112.465 158.719 -7.337 1.00 43.12 C ANISOU 3086 CD2 LEU A1176 5004 3161 8217 -568 1339 -621 C ATOM 3087 N SER A1177 114.154 157.325 -12.222 1.00 42.33 N ANISOU 3087 N SER A1177 5012 3086 7987 -591 905 -899 N ATOM 3088 CA SER A1177 113.671 157.106 -13.578 1.00 43.68 C ANISOU 3088 CA SER A1177 5174 3233 8190 -623 786 -1025 C ATOM 3089 C SER A1177 113.496 155.631 -13.910 1.00 46.50 C ANISOU 3089 C SER A1177 5545 3482 8640 -659 819 -1078 C ATOM 3090 O SER A1177 112.902 155.313 -14.946 1.00 47.16 O ANISOU 3090 O SER A1177 5618 3525 8774 -698 718 -1197 O ATOM 3091 CB SER A1177 114.602 157.782 -14.594 1.00 42.11 C ANISOU 3091 CB SER A1177 5073 3087 7838 -580 684 -1049 C ATOM 3092 OG SER A1177 115.940 157.318 -14.490 1.00 41.35 O ANISOU 3092 OG SER A1177 5071 2979 7659 -533 745 -985 O ATOM 3093 N ARG A1178 113.982 154.728 -13.059 1.00 49.11 N ANISOU 3093 N ARG A1178 5906 3758 8998 -647 952 -997 N ATOM 3094 CA ARG A1178 113.716 153.309 -13.251 1.00 53.20 C ANISOU 3094 CA ARG A1178 6430 4157 9625 -685 1002 -1042 C ATOM 3095 C ARG A1178 112.269 152.943 -12.941 1.00 58.38 C ANISOU 3095 C ARG A1178 6956 4752 10474 -758 1037 -1091 C ATOM 3096 O ARG A1178 111.846 151.827 -13.264 1.00 61.15 O ANISOU 3096 O ARG A1178 7295 4998 10942 -807 1054 -1155 O ATOM 3097 CB ARG A1178 114.671 152.477 -12.398 1.00 52.41 C ANISOU 3097 CB ARG A1178 6403 4007 9503 -641 1140 -932 C ATOM 3098 CG ARG A1178 116.115 152.852 -12.593 1.00 50.02 C ANISOU 3098 CG ARG A1178 6200 3759 9045 -565 1117 -876 C ATOM 3099 CD ARG A1178 117.036 151.882 -11.896 1.00 49.91 C ANISOU 3099 CD ARG A1178 6253 3677 9033 -518 1238 -782 C ATOM 3100 NE ARG A1178 118.407 152.382 -11.866 1.00 48.48 N ANISOU 3100 NE ARG A1178 6136 3553 8731 -440 1225 -713 N ATOM 3101 CZ ARG A1178 119.215 152.405 -12.920 1.00 48.22 C ANISOU 3101 CZ ARG A1178 6160 3528 8632 -406 1167 -761 C ATOM 3102 NH1 ARG A1178 118.789 151.962 -14.095 1.00 49.15 N ANISOU 3102 NH1 ARG A1178 6305 3598 8770 -439 1106 -882 N ATOM 3103 NH2 ARG A1178 120.448 152.877 -12.800 1.00 47.42 N ANISOU 3103 NH2 ARG A1178 6093 3472 8453 -336 1175 -690 N ATOM 3104 N SER A1179 111.514 153.840 -12.316 1.00 59.88 N ANISOU 3104 N SER A1179 7045 4995 10712 -765 1056 -1065 N ATOM 3105 CA SER A1179 110.097 153.652 -12.054 1.00 63.19 C ANISOU 3105 CA SER A1179 7314 5358 11337 -827 1093 -1116 C ATOM 3106 C SER A1179 109.301 154.721 -12.791 1.00 62.93 C ANISOU 3106 C SER A1179 7189 5391 11332 -842 940 -1207 C ATOM 3107 O SER A1179 109.863 155.614 -13.428 1.00 61.42 O ANISOU 3107 O SER A1179 7063 5286 10987 -804 821 -1221 O ATOM 3108 CB SER A1179 109.815 153.702 -10.551 1.00 64.58 C ANISOU 3108 CB SER A1179 7448 5513 11576 -812 1285 -1000 C ATOM 3109 OG SER A1179 110.665 152.806 -9.860 1.00 65.67 O ANISOU 3109 OG SER A1179 7693 5595 11664 -783 1413 -906 O ATOM 3110 N ASP A1180 107.976 154.611 -12.727 1.00 64.89 N ANISOU 3110 N ASP A1180 7278 5587 11792 -896 947 -1272 N ATOM 3111 CA ASP A1180 107.121 155.593 -13.383 1.00 66.08 C ANISOU 3111 CA ASP A1180 7319 5787 12002 -905 798 -1361 C ATOM 3112 C ASP A1180 107.286 156.953 -12.720 1.00 64.13 C ANISOU 3112 C ASP A1180 7068 5636 11662 -847 832 -1277 C ATOM 3113 O ASP A1180 107.359 157.059 -11.492 1.00 64.15 O ANISOU 3113 O ASP A1180 7069 5634 11672 -824 1002 -1171 O ATOM 3114 CB ASP A1180 105.656 155.156 -13.338 1.00 70.11 C ANISOU 3114 CB ASP A1180 7635 6210 12795 -971 811 -1443 C ATOM 3115 CG ASP A1180 104.771 155.997 -14.245 1.00 72.39 C ANISOU 3115 CG ASP A1180 7805 6535 13166 -980 614 -1561 C ATOM 3116 OD1 ASP A1180 105.253 157.038 -14.748 1.00 71.10 O ANISOU 3116 OD1 ASP A1180 7713 6467 12834 -930 495 -1561 O ATOM 3117 OD2 ASP A1180 103.599 155.611 -14.464 1.00 74.95 O ANISOU 3117 OD2 ASP A1180 7961 6785 13731 -1036 574 -1653 O ATOM 3118 N LEU A1181 107.366 158.000 -13.540 1.00 63.08 N ANISOU 3118 N LEU A1181 6951 5583 11435 -820 669 -1327 N ATOM 3119 CA LEU A1181 107.487 159.362 -13.040 1.00 60.82 C ANISOU 3119 CA LEU A1181 6663 5379 11066 -768 681 -1261 C ATOM 3120 C LEU A1181 106.213 160.177 -13.228 1.00 61.13 C ANISOU 3120 C LEU A1181 6533 5419 11275 -775 608 -1332 C ATOM 3121 O LEU A1181 106.213 161.378 -12.937 1.00 59.40 O ANISOU 3121 O LEU A1181 6307 5259 11003 -732 603 -1294 O ATOM 3122 CB LEU A1181 108.667 160.069 -13.710 1.00 59.16 C ANISOU 3122 CB LEU A1181 6609 5252 10616 -720 575 -1243 C ATOM 3123 CG LEU A1181 110.049 159.467 -13.478 1.00 58.50 C ANISOU 3123 CG LEU A1181 6683 5175 10370 -696 646 -1163 C ATOM 3124 CD1 LEU A1181 111.037 160.190 -14.354 1.00 57.26 C ANISOU 3124 CD1 LEU A1181 6650 5083 10023 -653 533 -1170 C ATOM 3125 CD2 LEU A1181 110.452 159.565 -12.018 1.00 57.62 C ANISOU 3125 CD2 LEU A1181 6592 5072 10228 -670 814 -1034 C ATOM 3126 N SER A1182 105.123 159.554 -13.686 1.00 63.70 N ANISOU 3126 N SER A1182 6714 5671 11817 -827 551 -1436 N ATOM 3127 CA SER A1182 103.952 160.325 -14.091 1.00 65.60 C ANISOU 3127 CA SER A1182 6783 5911 12231 -826 435 -1522 C ATOM 3128 C SER A1182 103.345 161.099 -12.929 1.00 64.37 C ANISOU 3128 C SER A1182 6516 5749 12191 -798 592 -1448 C ATOM 3129 O SER A1182 102.918 162.247 -13.101 1.00 63.83 O ANISOU 3129 O SER A1182 6380 5718 12155 -760 512 -1470 O ATOM 3130 CB SER A1182 102.907 159.401 -14.708 1.00 69.57 C ANISOU 3130 CB SER A1182 7141 6325 12967 -891 347 -1648 C ATOM 3131 OG SER A1182 103.320 158.948 -15.979 1.00 71.04 O ANISOU 3131 OG SER A1182 7430 6517 13043 -910 157 -1747 O ATOM 3132 N LYS A1183 103.306 160.505 -11.735 1.00 64.11 N ANISOU 3132 N LYS A1183 6476 5661 12221 -809 822 -1361 N ATOM 3133 CA LYS A1183 102.776 161.256 -10.603 1.00 63.60 C ANISOU 3133 CA LYS A1183 6335 5580 12249 -776 992 -1290 C ATOM 3134 C LYS A1183 103.692 162.419 -10.251 1.00 61.08 C ANISOU 3134 C LYS A1183 6161 5357 11692 -717 995 -1208 C ATOM 3135 O LYS A1183 103.218 163.484 -9.839 1.00 61.34 O ANISOU 3135 O LYS A1183 6129 5398 11779 -682 1032 -1193 O ATOM 3136 CB LYS A1183 102.560 160.337 -9.394 1.00 64.42 C ANISOU 3136 CB LYS A1183 6428 5592 12458 -796 1251 -1213 C ATOM 3137 CG LYS A1183 101.995 161.033 -8.142 1.00 64.05 C ANISOU 3137 CG LYS A1183 6325 5507 12504 -757 1465 -1137 C ATOM 3138 CD LYS A1183 100.597 161.634 -8.365 1.00 65.88 C ANISOU 3138 CD LYS A1183 6328 5686 13019 -756 1437 -1216 C ATOM 3139 CE LYS A1183 100.117 162.451 -7.151 1.00 66.41 C ANISOU 3139 CE LYS A1183 6362 5710 13161 -707 1662 -1139 C ATOM 3140 NZ LYS A1183 98.727 162.982 -7.319 1.00 68.78 N ANISOU 3140 NZ LYS A1183 6426 5938 13769 -699 1654 -1211 N ATOM 3141 N PHE A1184 105.000 162.254 -10.452 1.00 58.28 N ANISOU 3141 N PHE A1184 5995 5065 11085 -705 951 -1160 N ATOM 3142 CA PHE A1184 105.915 163.354 -10.180 1.00 55.63 C ANISOU 3142 CA PHE A1184 5794 4814 10530 -654 936 -1088 C ATOM 3143 C PHE A1184 105.723 164.480 -11.187 1.00 54.71 C ANISOU 3143 C PHE A1184 5647 4751 10389 -630 744 -1158 C ATOM 3144 O PHE A1184 105.722 165.658 -10.815 1.00 54.34 O ANISOU 3144 O PHE A1184 5611 4737 10298 -592 758 -1123 O ATOM 3145 CB PHE A1184 107.363 162.856 -10.183 1.00 54.70 C ANISOU 3145 CB PHE A1184 5866 4738 10180 -644 932 -1024 C ATOM 3146 CG PHE A1184 108.348 163.857 -9.644 1.00 54.99 C ANISOU 3146 CG PHE A1184 6037 4845 10012 -596 946 -937 C ATOM 3147 CD1 PHE A1184 108.874 163.731 -8.365 1.00 55.08 C ANISOU 3147 CD1 PHE A1184 6137 4843 9950 -579 1102 -835 C ATOM 3148 CD2 PHE A1184 108.746 164.931 -10.415 1.00 56.30 C ANISOU 3148 CD2 PHE A1184 6249 5080 10063 -569 801 -962 C ATOM 3149 CE1 PHE A1184 109.778 164.658 -7.874 1.00 55.22 C ANISOU 3149 CE1 PHE A1184 6278 4916 9787 -540 1093 -768 C ATOM 3150 CE2 PHE A1184 109.646 165.859 -9.922 1.00 56.59 C ANISOU 3150 CE2 PHE A1184 6404 5172 9927 -531 811 -888 C ATOM 3151 CZ PHE A1184 110.162 165.717 -8.655 1.00 55.81 C ANISOU 3151 CZ PHE A1184 6384 5061 9762 -520 948 -796 C ATOM 3152 N ARG A1185 105.532 164.139 -12.463 1.00 54.72 N ANISOU 3152 N ARG A1185 5619 4752 10421 -649 564 -1261 N ATOM 3153 CA ARG A1185 105.333 165.169 -13.478 1.00 53.83 C ANISOU 3153 CA ARG A1185 5490 4679 10284 -619 371 -1332 C ATOM 3154 C ARG A1185 104.015 165.912 -13.271 1.00 54.98 C ANISOU 3154 C ARG A1185 5438 4786 10665 -606 360 -1378 C ATOM 3155 O ARG A1185 103.945 167.130 -13.476 1.00 55.16 O ANISOU 3155 O ARG A1185 5460 4839 10657 -561 284 -1382 O ATOM 3156 CB ARG A1185 105.401 164.540 -14.872 1.00 54.11 C ANISOU 3156 CB ARG A1185 5556 4707 10294 -640 180 -1441 C ATOM 3157 CG ARG A1185 106.707 163.837 -15.145 1.00 52.98 C ANISOU 3157 CG ARG A1185 5605 4587 9937 -646 200 -1401 C ATOM 3158 CD ARG A1185 106.907 163.589 -16.621 1.00 54.10 C ANISOU 3158 CD ARG A1185 5825 4726 10005 -647 5 -1510 C ATOM 3159 NE ARG A1185 108.326 163.487 -16.955 1.00 54.01 N ANISOU 3159 NE ARG A1185 6017 4748 9757 -622 23 -1459 N ATOM 3160 CZ ARG A1185 108.962 162.341 -17.177 1.00 54.90 C ANISOU 3160 CZ ARG A1185 6221 4826 9813 -646 62 -1463 C ATOM 3161 NH1 ARG A1185 108.306 161.187 -17.106 1.00 57.14 N ANISOU 3161 NH1 ARG A1185 6422 5040 10248 -701 84 -1517 N ATOM 3162 NH2 ARG A1185 110.253 162.350 -17.475 1.00 53.54 N ANISOU 3162 NH2 ARG A1185 6217 4676 9448 -612 84 -1416 N ATOM 3163 N GLU A1186 102.961 165.202 -12.850 1.00 55.32 N ANISOU 3163 N GLU A1186 5309 4751 10959 -642 445 -1411 N ATOM 3164 CA GLU A1186 101.680 165.862 -12.614 1.00 54.29 C ANISOU 3164 CA GLU A1186 4970 4569 11089 -625 454 -1453 C ATOM 3165 C GLU A1186 101.754 166.794 -11.414 1.00 51.11 C ANISOU 3165 C GLU A1186 4589 4167 10663 -585 645 -1351 C ATOM 3166 O GLU A1186 101.034 167.797 -11.371 1.00 51.06 O ANISOU 3166 O GLU A1186 4466 4140 10794 -549 623 -1375 O ATOM 3167 CB GLU A1186 100.568 164.820 -12.436 1.00 56.16 C ANISOU 3167 CB GLU A1186 5018 4708 11613 -675 517 -1509 C ATOM 3168 CG GLU A1186 99.126 165.370 -12.362 1.00 57.27 C ANISOU 3168 CG GLU A1186 4909 4777 12073 -658 502 -1570 C ATOM 3169 CD GLU A1186 98.604 165.942 -13.687 1.00 56.84 C ANISOU 3169 CD GLU A1186 4760 4747 12090 -636 195 -1696 C ATOM 3170 OE1 GLU A1186 98.953 165.405 -14.765 1.00 56.31 O ANISOU 3170 OE1 GLU A1186 4767 4713 11917 -660 -5 -1773 O ATOM 3171 OE2 GLU A1186 97.841 166.938 -13.646 1.00 56.79 O ANISOU 3171 OE2 GLU A1186 4614 4719 12246 -589 153 -1717 O ATOM 3172 N ASN A1187 102.619 166.484 -10.440 1.00 48.59 N ANISOU 3172 N ASN A1187 4423 3866 10174 -589 827 -1242 N ATOM 3173 CA ASN A1187 102.834 167.388 -9.311 1.00 46.74 C ANISOU 3173 CA ASN A1187 4254 3635 9868 -551 995 -1149 C ATOM 3174 C ASN A1187 103.552 168.660 -9.741 1.00 44.11 C ANISOU 3174 C ASN A1187 4042 3381 9338 -509 864 -1136 C ATOM 3175 O ASN A1187 103.251 169.749 -9.237 1.00 43.47 O ANISOU 3175 O ASN A1187 3943 3287 9288 -473 924 -1112 O ATOM 3176 CB ASN A1187 103.632 166.692 -8.207 1.00 46.26 C ANISOU 3176 CB ASN A1187 4345 3571 9660 -562 1188 -1043 C ATOM 3177 CG ASN A1187 102.819 165.655 -7.455 1.00 48.70 C ANISOU 3177 CG ASN A1187 4547 3778 10180 -590 1386 -1031 C ATOM 3178 OD1 ASN A1187 101.596 165.772 -7.330 1.00 50.48 O ANISOU 3178 OD1 ASN A1187 4584 3924 10672 -590 1453 -1076 O ATOM 3179 ND2 ASN A1187 103.501 164.632 -6.940 1.00 48.26 N ANISOU 3179 ND2 ASN A1187 4610 3711 10018 -609 1486 -969 N ATOM 3180 N CYS A1188 104.506 168.551 -10.668 1.00 42.39 N ANISOU 3180 N CYS A1188 3954 3233 8920 -510 698 -1150 N ATOM 3181 CA CYS A1188 105.107 169.760 -11.215 1.00 40.79 C ANISOU 3181 CA CYS A1188 3857 3089 8553 -467 571 -1145 C ATOM 3182 C CYS A1188 104.050 170.618 -11.892 1.00 42.13 C ANISOU 3182 C CYS A1188 3874 3224 8911 -437 441 -1231 C ATOM 3183 O CYS A1188 103.897 171.802 -11.574 1.00 42.17 O ANISOU 3183 O CYS A1188 3885 3221 8918 -394 462 -1208 O ATOM 3184 CB CYS A1188 106.209 169.420 -12.218 1.00 39.76 C ANISOU 3184 CB CYS A1188 3877 3019 8213 -470 430 -1154 C ATOM 3185 SG CYS A1188 107.613 168.505 -11.573 1.00 38.51 S ANISOU 3185 SG CYS A1188 3894 2897 7842 -490 544 -1056 S ATOM 3186 N LYS A1189 103.280 170.026 -12.807 1.00 43.69 N ANISOU 3186 N LYS A1189 3932 3390 9277 -456 299 -1337 N ATOM 3187 CA LYS A1189 102.351 170.834 -13.582 1.00 45.48 C ANISOU 3187 CA LYS A1189 4016 3584 9678 -419 122 -1430 C ATOM 3188 C LYS A1189 101.402 171.585 -12.660 1.00 47.53 C ANISOU 3188 C LYS A1189 4119 3779 10162 -394 260 -1409 C ATOM 3189 O LYS A1189 101.212 172.796 -12.804 1.00 47.85 O ANISOU 3189 O LYS A1189 4151 3805 10225 -339 197 -1415 O ATOM 3190 CB LYS A1189 101.582 169.956 -14.569 1.00 47.15 C ANISOU 3190 CB LYS A1189 4089 3768 10058 -447 -55 -1554 C ATOM 3191 CG LYS A1189 102.465 169.352 -15.655 1.00 46.61 C ANISOU 3191 CG LYS A1189 4190 3750 9769 -461 -211 -1593 C ATOM 3192 CD LYS A1189 101.617 168.670 -16.717 1.00 48.89 C ANISOU 3192 CD LYS A1189 4354 4008 10215 -480 -425 -1735 C ATOM 3193 CE LYS A1189 101.702 167.156 -16.611 1.00 49.57 C ANISOU 3193 CE LYS A1189 4443 4071 10320 -553 -345 -1746 C ATOM 3194 NZ LYS A1189 103.062 166.645 -16.951 1.00 47.84 N ANISOU 3194 NZ LYS A1189 4465 3898 9813 -565 -326 -1704 N ATOM 3195 N LYS A1190 100.842 170.895 -11.665 1.00 49.05 N ANISOU 3195 N LYS A1190 4203 3916 10515 -427 472 -1377 N ATOM 3196 CA LYS A1190 99.929 171.563 -10.741 1.00 41.91 C ANISOU 3196 CA LYS A1190 3155 2933 9836 -401 644 -1352 C ATOM 3197 C LYS A1190 100.646 172.613 -9.906 1.00 42.99 C ANISOU 3197 C LYS A1190 3469 3094 9773 -364 778 -1254 C ATOM 3198 O LYS A1190 100.068 173.660 -9.595 1.00 44.01 O ANISOU 3198 O LYS A1190 3526 3168 10026 -317 828 -1252 O ATOM 3199 CB LYS A1190 99.258 170.532 -9.841 1.00 43.39 C ANISOU 3199 CB LYS A1190 3227 3044 10214 -438 869 -1330 C ATOM 3200 CG LYS A1190 98.359 169.595 -10.592 1.00 45.49 C ANISOU 3200 CG LYS A1190 3306 3266 10714 -471 742 -1431 C ATOM 3201 CD LYS A1190 97.793 168.533 -9.686 1.00 52.70 C ANISOU 3201 CD LYS A1190 4141 4090 11794 -507 979 -1398 C ATOM 3202 CE LYS A1190 96.904 167.607 -10.494 1.00 55.40 C ANISOU 3202 CE LYS A1190 4303 4381 12364 -549 832 -1506 C ATOM 3203 NZ LYS A1190 96.442 166.430 -9.717 1.00 57.45 N ANISOU 3203 NZ LYS A1190 4507 4547 12776 -595 1052 -1476 N ATOM 3204 N ARG A1191 101.905 172.356 -9.535 1.00 40.78 N ANISOU 3204 N ARG A1191 3424 2888 9184 -379 831 -1174 N ATOM 3205 CA ARG A1191 102.632 173.300 -8.692 1.00 39.26 C ANISOU 3205 CA ARG A1191 3418 2720 8778 -345 941 -1085 C ATOM 3206 C ARG A1191 103.013 174.555 -9.469 1.00 38.63 C ANISOU 3206 C ARG A1191 3426 2677 8575 -289 764 -1103 C ATOM 3207 O ARG A1191 102.937 175.668 -8.933 1.00 38.64 O ANISOU 3207 O ARG A1191 3485 2655 8539 -237 833 -1067 O ATOM 3208 CB ARG A1191 103.873 172.625 -8.098 1.00 37.83 C ANISOU 3208 CB ARG A1191 3444 2600 8329 -373 1017 -1004 C ATOM 3209 CG ARG A1191 104.874 173.565 -7.395 1.00 36.29 C ANISOU 3209 CG ARG A1191 3472 2447 7871 -340 1061 -925 C ATOM 3210 CD ARG A1191 104.241 174.388 -6.270 1.00 36.82 C ANISOU 3210 CD ARG A1191 3538 2443 8007 -303 1249 -891 C ATOM 3211 NE ARG A1191 105.181 175.334 -5.670 1.00 35.69 N ANISOU 3211 NE ARG A1191 3618 2335 7606 -268 1257 -835 N ATOM 3212 CZ ARG A1191 104.853 176.221 -4.733 1.00 36.90 C ANISOU 3212 CZ ARG A1191 3837 2438 7745 -223 1395 -807 C ATOM 3213 NH1 ARG A1191 103.606 176.283 -4.286 1.00 38.96 N ANISOU 3213 NH1 ARG A1191 3951 2610 8241 -204 1559 -820 N ATOM 3214 NH2 ARG A1191 105.768 177.050 -4.243 1.00 35.99 N ANISOU 3214 NH2 ARG A1191 3932 2354 7390 -194 1372 -770 N ATOM 3215 N ALA A1192 103.429 174.401 -10.731 1.00 38.10 N ANISOU 3215 N ALA A1192 3390 2658 8429 -290 544 -1155 N ATOM 3216 CA ALA A1192 103.698 175.571 -11.561 1.00 35.29 C ANISOU 3216 CA ALA A1192 3115 2316 7976 -226 379 -1173 C ATOM 3217 C ALA A1192 102.418 176.333 -11.886 1.00 41.86 C ANISOU 3217 C ALA A1192 3762 3063 9081 -167 308 -1244 C ATOM 3218 O ALA A1192 102.432 177.564 -11.983 1.00 41.65 O ANISOU 3218 O ALA A1192 3803 3019 9001 -85 272 -1225 O ATOM 3219 CB ALA A1192 104.409 175.155 -12.846 1.00 36.22 C ANISOU 3219 CB ALA A1192 3322 2487 7952 -235 182 -1214 C ATOM 3220 N MET A1193 101.295 175.625 -12.038 1.00 42.97 N ANISOU 3220 N MET A1193 3659 3141 9525 -198 285 -1323 N ATOM 3221 CA MET A1193 100.027 176.309 -12.277 1.00 44.07 C ANISOU 3221 CA MET A1193 3584 3183 9978 -137 215 -1395 C ATOM 3222 C MET A1193 99.587 177.079 -11.044 1.00 43.80 C ANISOU 3222 C MET A1193 3528 3094 10022 -86 463 -1321 C ATOM 3223 O MET A1193 99.230 178.258 -11.132 1.00 43.91 O ANISOU 3223 O MET A1193 3541 3096 10047 28 429 -1308 O ATOM 3224 CB MET A1193 98.947 175.311 -12.703 1.00 45.91 C ANISOU 3224 CB MET A1193 3536 3372 10537 -199 126 -1498 C ATOM 3225 CG MET A1193 99.226 174.612 -14.029 1.00 45.39 C ANISOU 3225 CG MET A1193 3498 3370 10377 -225 -149 -1586 C ATOM 3226 SD MET A1193 97.890 173.536 -14.585 1.00 47.61 S ANISOU 3226 SD MET A1193 3472 3627 10990 -267 -288 -1706 S ATOM 3227 CE MET A1193 98.437 173.189 -16.257 1.00 46.96 C ANISOU 3227 CE MET A1193 3529 3619 10696 -257 -646 -1809 C ATOM 3228 N SER A1194 99.642 176.441 -9.880 1.00 43.49 N ANISOU 3228 N SER A1194 3496 3048 9981 -151 718 -1256 N ATOM 3229 CA SER A1194 99.267 177.129 -8.653 1.00 44.66 C ANISOU 3229 CA SER A1194 3661 3148 10159 -104 971 -1184 C ATOM 3230 C SER A1194 100.190 178.299 -8.355 1.00 44.46 C ANISOU 3230 C SER A1194 3909 3189 9795 -37 976 -1110 C ATOM 3231 O SER A1194 99.752 179.303 -7.780 1.00 45.90 O ANISOU 3231 O SER A1194 4109 3343 9989 43 1086 -1074 O ATOM 3232 CB SER A1194 99.283 176.156 -7.487 1.00 44.70 C ANISOU 3232 CB SER A1194 3672 3128 10182 -180 1237 -1125 C ATOM 3233 OG SER A1194 100.617 175.972 -7.034 1.00 42.58 O ANISOU 3233 OG SER A1194 3681 2951 9548 -206 1270 -1051 O ATOM 3234 N PHE A1195 101.465 178.193 -8.732 1.00 42.93 N ANISOU 3234 N PHE A1195 3924 3085 9302 -69 864 -1084 N ATOM 3235 CA PHE A1195 102.388 179.298 -8.484 1.00 42.25 C ANISOU 3235 CA PHE A1195 4081 3049 8924 -20 858 -1022 C ATOM 3236 C PHE A1195 102.112 180.463 -9.427 1.00 43.40 C ANISOU 3236 C PHE A1195 4218 3182 9089 79 689 -1051 C ATOM 3237 O PHE A1195 102.134 181.629 -9.011 1.00 43.75 O ANISOU 3237 O PHE A1195 4366 3216 9041 151 745 -1009 O ATOM 3238 CB PHE A1195 103.840 178.833 -8.626 1.00 34.56 C ANISOU 3238 CB PHE A1195 3305 2165 7662 -81 794 -983 C ATOM 3239 CG PHE A1195 104.857 179.818 -8.100 1.00 33.38 C ANISOU 3239 CG PHE A1195 3392 2053 7240 -55 820 -918 C ATOM 3240 CD1 PHE A1195 105.191 180.962 -8.816 1.00 33.01 C ANISOU 3240 CD1 PHE A1195 3434 2014 7095 4 693 -917 C ATOM 3241 CD2 PHE A1195 105.490 179.588 -6.890 1.00 34.95 C ANISOU 3241 CD2 PHE A1195 3727 2265 7290 -87 963 -863 C ATOM 3242 CE1 PHE A1195 106.132 181.856 -8.327 1.00 32.13 C ANISOU 3242 CE1 PHE A1195 3526 1923 6759 14 714 -865 C ATOM 3243 CE2 PHE A1195 106.437 180.485 -6.398 1.00 34.17 C ANISOU 3243 CE2 PHE A1195 3834 2188 6962 -70 958 -822 C ATOM 3244 CZ PHE A1195 106.755 181.614 -7.119 1.00 31.65 C ANISOU 3244 CZ PHE A1195 3584 1877 6564 -26 836 -825 C ATOM 3245 N SER A1196 101.852 180.166 -10.702 1.00 44.61 N ANISOU 3245 N SER A1196 4264 3330 9354 91 474 -1124 N ATOM 3246 CA SER A1196 101.452 181.212 -11.634 1.00 46.15 C ANISOU 3246 CA SER A1196 4440 3502 9594 211 301 -1152 C ATOM 3247 C SER A1196 100.084 181.774 -11.286 1.00 49.69 C ANISOU 3247 C SER A1196 4683 3888 10310 306 366 -1166 C ATOM 3248 O SER A1196 99.814 182.950 -11.547 1.00 50.98 O ANISOU 3248 O SER A1196 4879 4046 10447 425 312 -1141 O ATOM 3249 CB SER A1196 101.457 180.666 -13.056 1.00 46.17 C ANISOU 3249 CB SER A1196 4390 3523 9630 211 40 -1231 C ATOM 3250 OG SER A1196 102.756 180.232 -13.412 1.00 44.40 O ANISOU 3250 OG SER A1196 4365 3350 9155 140 2 -1211 O ATOM 3251 N LYS A 294 99.210 180.955 -10.701 1.00 45.74 N ANISOU 3251 N LYS A 294 4952 3491 8934 -10 62 -959 N ATOM 3252 CA LYS A 294 97.938 181.467 -10.217 1.00 47.26 C ANISOU 3252 CA LYS A 294 5136 3702 9118 -33 55 -898 C ATOM 3253 C LYS A 294 98.150 182.500 -9.119 1.00 47.51 C ANISOU 3253 C LYS A 294 5186 3793 9073 -28 70 -789 C ATOM 3254 O LYS A 294 97.400 183.480 -9.032 1.00 47.03 O ANISOU 3254 O LYS A 294 5138 3785 8946 -44 60 -754 O ATOM 3255 CB LYS A 294 97.085 180.303 -9.719 1.00 49.60 C ANISOU 3255 CB LYS A 294 5385 3910 9551 -42 62 -885 C ATOM 3256 CG LYS A 294 95.793 180.693 -9.026 1.00 50.98 C ANISOU 3256 CG LYS A 294 5541 4092 9738 -63 66 -816 C ATOM 3257 CD LYS A 294 95.054 179.455 -8.550 1.00 53.43 C ANISOU 3257 CD LYS A 294 5803 4301 10196 -73 85 -806 C ATOM 3258 CE LYS A 294 93.825 179.817 -7.735 1.00 36.22 C ANISOU 3258 CE LYS A 294 3602 2124 8034 -92 100 -730 C ATOM 3259 NZ LYS A 294 93.254 178.607 -7.072 1.00 40.74 N ANISOU 3259 NZ LYS A 294 4134 2589 8755 -101 137 -701 N ATOM 3260 N GLN A 295 99.190 182.313 -8.298 1.00 48.22 N ANISOU 3260 N GLN A 295 5279 3874 9169 -3 89 -742 N ATOM 3261 CA GLN A 295 99.512 183.272 -7.242 1.00 48.25 C ANISOU 3261 CA GLN A 295 5300 3934 9101 5 99 -651 C ATOM 3262 C GLN A 295 100.109 184.557 -7.810 1.00 45.99 C ANISOU 3262 C GLN A 295 5044 3730 8700 1 94 -672 C ATOM 3263 O GLN A 295 99.854 185.651 -7.291 1.00 45.18 O ANISOU 3263 O GLN A 295 4956 3686 8526 -6 94 -614 O ATOM 3264 CB GLN A 295 100.473 182.637 -6.231 1.00 52.05 C ANISOU 3264 CB GLN A 295 5780 4373 9625 38 114 -605 C ATOM 3265 CG GLN A 295 99.829 181.636 -5.273 1.00 56.17 C ANISOU 3265 CG GLN A 295 6290 4813 10239 45 129 -543 C ATOM 3266 CD GLN A 295 98.823 182.282 -4.323 1.00 59.19 C ANISOU 3266 CD GLN A 295 6677 5224 10590 31 139 -454 C ATOM 3267 OE1 GLN A 295 97.638 181.936 -4.323 1.00 60.96 O ANISOU 3267 OE1 GLN A 295 6879 5414 10868 9 147 -445 O ATOM 3268 NE2 GLN A 295 99.296 183.220 -3.505 1.00 59.37 N ANISOU 3268 NE2 GLN A 295 6723 5305 10529 45 138 -394 N ATOM 3269 N ILE A 296 100.921 184.447 -8.863 1.00 45.98 N ANISOU 3269 N ILE A 296 5055 3732 8684 6 95 -756 N ATOM 3270 CA ILE A 296 101.486 185.641 -9.483 1.00 46.31 C ANISOU 3270 CA ILE A 296 5132 3840 8623 -1 101 -777 C ATOM 3271 C ILE A 296 100.390 186.466 -10.143 1.00 46.31 C ANISOU 3271 C ILE A 296 5165 3874 8556 -27 85 -783 C ATOM 3272 O ILE A 296 100.394 187.701 -10.077 1.00 45.86 O ANISOU 3272 O ILE A 296 5139 3874 8413 -37 90 -747 O ATOM 3273 CB ILE A 296 102.584 185.250 -10.488 1.00 30.74 C ANISOU 3273 CB ILE A 296 3170 1856 6655 11 114 -870 C ATOM 3274 CG1 ILE A 296 103.643 184.391 -9.803 1.00 31.32 C ANISOU 3274 CG1 ILE A 296 3208 1889 6801 42 124 -866 C ATOM 3275 CG2 ILE A 296 103.217 186.483 -11.101 1.00 29.99 C ANISOU 3275 CG2 ILE A 296 3116 1822 6459 2 134 -888 C ATOM 3276 CD1 ILE A 296 104.585 183.721 -10.761 1.00 32.13 C ANISOU 3276 CD1 ILE A 296 3309 1966 6933 59 135 -967 C ATOM 3277 N ARG A 297 99.425 185.796 -10.772 1.00 46.92 N ANISOU 3277 N ARG A 297 5235 3913 8678 -38 64 -831 N ATOM 3278 CA ARG A 297 98.332 186.513 -11.416 1.00 45.74 C ANISOU 3278 CA ARG A 297 5118 3789 8471 -59 40 -844 C ATOM 3279 C ARG A 297 97.469 187.241 -10.390 1.00 44.09 C ANISOU 3279 C ARG A 297 4897 3612 8244 -68 35 -750 C ATOM 3280 O ARG A 297 96.930 188.318 -10.680 1.00 42.72 O ANISOU 3280 O ARG A 297 4762 3480 7991 -80 22 -735 O ATOM 3281 CB ARG A 297 97.495 185.534 -12.245 1.00 46.04 C ANISOU 3281 CB ARG A 297 5139 3775 8578 -67 13 -927 C ATOM 3282 CG ARG A 297 96.281 186.145 -12.919 1.00 45.04 C ANISOU 3282 CG ARG A 297 5041 3666 8404 -85 -22 -951 C ATOM 3283 CD ARG A 297 95.662 185.187 -13.911 1.00 45.93 C ANISOU 3283 CD ARG A 297 5139 3730 8581 -90 -53 -1059 C ATOM 3284 NE ARG A 297 94.303 185.586 -14.266 1.00 46.81 N ANISOU 3284 NE ARG A 297 5254 3850 8681 -106 -94 -1076 N ATOM 3285 CZ ARG A 297 94.001 186.437 -15.242 1.00 47.71 C ANISOU 3285 CZ ARG A 297 5439 3996 8692 -109 -123 -1120 C ATOM 3286 NH1 ARG A 297 94.965 186.989 -15.976 1.00 47.83 N ANISOU 3286 NH1 ARG A 297 5532 4037 8606 -101 -107 -1149 N ATOM 3287 NH2 ARG A 297 92.730 186.740 -15.483 1.00 48.73 N ANISOU 3287 NH2 ARG A 297 5564 4129 8823 -120 -166 -1136 N ATOM 3288 N ALA A 298 97.349 186.683 -9.180 1.00 43.68 N ANISOU 3288 N ALA A 298 4799 3534 8262 -59 47 -686 N ATOM 3289 CA ALA A 298 96.598 187.337 -8.113 1.00 28.89 C ANISOU 3289 CA ALA A 298 2915 1690 6371 -64 49 -599 C ATOM 3290 C ALA A 298 97.363 188.522 -7.544 1.00 27.85 C ANISOU 3290 C ALA A 298 2809 1621 6150 -56 60 -546 C ATOM 3291 O ALA A 298 96.766 189.551 -7.199 1.00 27.12 O ANISOU 3291 O ALA A 298 2731 1573 6000 -63 53 -501 O ATOM 3292 CB ALA A 298 96.286 186.331 -7.010 1.00 29.53 C ANISOU 3292 CB ALA A 298 2952 1717 6551 -56 66 -548 C ATOM 3293 N ARG A 299 98.684 188.389 -7.417 1.00 27.84 N ANISOU 3293 N ARG A 299 2811 1621 6145 -40 77 -555 N ATOM 3294 CA ARG A 299 99.482 189.537 -7.007 1.00 40.66 C ANISOU 3294 CA ARG A 299 4454 3302 7694 -34 87 -521 C ATOM 3295 C ARG A 299 99.462 190.657 -8.045 1.00 40.10 C ANISOU 3295 C ARG A 299 4431 3271 7534 -52 86 -553 C ATOM 3296 O ARG A 299 99.491 191.834 -7.678 1.00 40.11 O ANISOU 3296 O ARG A 299 4451 3318 7472 -56 89 -512 O ATOM 3297 CB ARG A 299 100.913 189.096 -6.703 1.00 40.52 C ANISOU 3297 CB ARG A 299 4422 3271 7705 -13 104 -535 C ATOM 3298 CG ARG A 299 101.061 188.439 -5.356 1.00 40.73 C ANISOU 3298 CG ARG A 299 4421 3267 7786 9 104 -476 C ATOM 3299 CD ARG A 299 102.489 188.061 -5.068 1.00 41.81 C ANISOU 3299 CD ARG A 299 4547 3389 7949 35 112 -495 C ATOM 3300 NE ARG A 299 102.701 187.814 -3.643 1.00 43.22 N ANISOU 3300 NE ARG A 299 4722 3550 8149 61 107 -427 N ATOM 3301 CZ ARG A 299 103.857 187.425 -3.107 1.00 43.37 C ANISOU 3301 CZ ARG A 299 4736 3548 8195 93 105 -430 C ATOM 3302 NH1 ARG A 299 104.929 187.229 -3.877 1.00 43.59 N ANISOU 3302 NH1 ARG A 299 4751 3573 8239 101 110 -501 N ATOM 3303 NH2 ARG A 299 103.939 187.231 -1.793 1.00 43.35 N ANISOU 3303 NH2 ARG A 299 4747 3525 8200 122 97 -364 N ATOM 3304 N ARG A 300 99.379 190.330 -9.334 1.00 39.70 N ANISOU 3304 N ARG A 300 4409 3198 7477 -61 81 -627 N ATOM 3305 CA ARG A 300 99.332 191.386 -10.341 1.00 38.51 C ANISOU 3305 CA ARG A 300 4323 3074 7234 -77 82 -653 C ATOM 3306 C ARG A 300 98.093 192.257 -10.161 1.00 38.05 C ANISOU 3306 C ARG A 300 4287 3040 7130 -89 58 -608 C ATOM 3307 O ARG A 300 98.176 193.488 -10.229 1.00 38.42 O ANISOU 3307 O ARG A 300 4377 3122 7100 -97 64 -579 O ATOM 3308 CB ARG A 300 99.343 190.786 -11.753 1.00 38.58 C ANISOU 3308 CB ARG A 300 4370 3049 7241 -81 76 -746 C ATOM 3309 CG ARG A 300 100.634 190.957 -12.560 1.00 38.35 C ANISOU 3309 CG ARG A 300 4377 3020 7173 -79 111 -801 C ATOM 3310 CD ARG A 300 100.458 190.407 -13.975 1.00 39.50 C ANISOU 3310 CD ARG A 300 4571 3133 7304 -81 101 -899 C ATOM 3311 NE ARG A 300 100.581 188.950 -14.038 1.00 41.74 N ANISOU 3311 NE ARG A 300 4801 3374 7685 -66 92 -956 N ATOM 3312 CZ ARG A 300 101.539 188.308 -14.706 1.00 43.02 C ANISOU 3312 CZ ARG A 300 4967 3515 7865 -52 113 -1034 C ATOM 3313 NH1 ARG A 300 102.456 188.989 -15.389 1.00 43.85 N ANISOU 3313 NH1 ARG A 300 5125 3638 7896 -53 149 -1065 N ATOM 3314 NH2 ARG A 300 101.580 186.982 -14.703 1.00 43.56 N ANISOU 3314 NH2 ARG A 300 4983 3538 8028 -38 102 -1083 N ATOM 3315 N LYS A 301 96.936 191.634 -9.895 1.00 37.10 N ANISOU 3315 N LYS A 301 4132 2898 7065 -91 32 -601 N ATOM 3316 CA LYS A 301 95.685 192.385 -9.798 1.00 34.85 C ANISOU 3316 CA LYS A 301 3861 2632 6747 -101 5 -569 C ATOM 3317 C LYS A 301 95.684 193.311 -8.595 1.00 33.08 C ANISOU 3317 C LYS A 301 3624 2452 6494 -96 16 -487 C ATOM 3318 O LYS A 301 95.174 194.439 -8.668 1.00 32.17 O ANISOU 3318 O LYS A 301 3544 2366 6312 -103 4 -461 O ATOM 3319 CB LYS A 301 94.505 191.425 -9.709 1.00 35.28 C ANISOU 3319 CB LYS A 301 3867 2650 6888 -104 -19 -586 C ATOM 3320 CG LYS A 301 94.172 190.755 -11.015 1.00 36.59 C ANISOU 3320 CG LYS A 301 4052 2777 7073 -112 -44 -679 C ATOM 3321 CD LYS A 301 93.130 189.670 -10.841 1.00 38.75 C ANISOU 3321 CD LYS A 301 4261 3005 7457 -116 -62 -702 C ATOM 3322 CE LYS A 301 92.788 189.064 -12.186 1.00 41.65 C ANISOU 3322 CE LYS A 301 4645 3337 7843 -122 -94 -809 C ATOM 3323 NZ LYS A 301 94.014 188.797 -13.004 1.00 43.74 N ANISOU 3323 NZ LYS A 301 4953 3595 8072 -114 -79 -868 N ATOM 3324 N THR A 302 96.244 192.846 -7.476 1.00 32.87 N ANISOU 3324 N THR A 302 3550 2426 6515 -82 35 -447 N ATOM 3325 CA THR A 302 96.297 193.685 -6.288 1.00 32.42 C ANISOU 3325 CA THR A 302 3482 2408 6429 -74 42 -378 C ATOM 3326 C THR A 302 97.273 194.838 -6.478 1.00 33.66 C ANISOU 3326 C THR A 302 3676 2602 6512 -76 56 -377 C ATOM 3327 O THR A 302 96.977 195.980 -6.102 1.00 33.57 O ANISOU 3327 O THR A 302 3681 2625 6448 -79 52 -341 O ATOM 3328 CB THR A 302 96.684 192.853 -5.069 1.00 31.58 C ANISOU 3328 CB THR A 302 3330 2283 6387 -57 57 -341 C ATOM 3329 OG1 THR A 302 95.743 191.785 -4.899 1.00 32.21 O ANISOU 3329 OG1 THR A 302 3378 2317 6543 -60 54 -338 O ATOM 3330 CG2 THR A 302 96.682 193.720 -3.830 1.00 30.51 C ANISOU 3330 CG2 THR A 302 3190 2186 6217 -49 60 -277 C ATOM 3331 N ALA A 303 98.444 194.561 -7.056 1.00 34.53 N ANISOU 3331 N ALA A 303 3796 2701 6624 -74 76 -420 N ATOM 3332 CA ALA A 303 99.380 195.642 -7.336 1.00 34.25 C ANISOU 3332 CA ALA A 303 3792 2692 6529 -81 98 -424 C ATOM 3333 C ALA A 303 98.847 196.577 -8.415 1.00 35.45 C ANISOU 3333 C ALA A 303 4017 2847 6606 -101 94 -438 C ATOM 3334 O ALA A 303 99.085 197.788 -8.355 1.00 36.24 O ANISOU 3334 O ALA A 303 4148 2971 6651 -109 106 -414 O ATOM 3335 CB ALA A 303 100.737 195.071 -7.732 1.00 33.82 C ANISOU 3335 CB ALA A 303 3727 2620 6504 -75 126 -473 C ATOM 3336 N ARG A 304 98.101 196.051 -9.398 1.00 35.59 N ANISOU 3336 N ARG A 304 4066 2836 6621 -108 75 -478 N ATOM 3337 CA ARG A 304 97.546 196.932 -10.426 1.00 35.17 C ANISOU 3337 CA ARG A 304 4097 2778 6490 -125 64 -491 C ATOM 3338 C ARG A 304 96.531 197.898 -9.834 1.00 33.23 C ANISOU 3338 C ARG A 304 3856 2556 6212 -126 40 -434 C ATOM 3339 O ARG A 304 96.485 199.073 -10.217 1.00 33.00 O ANISOU 3339 O ARG A 304 3893 2534 6113 -137 44 -417 O ATOM 3340 CB ARG A 304 96.893 196.126 -11.549 1.00 37.28 C ANISOU 3340 CB ARG A 304 4395 3005 6763 -128 38 -555 C ATOM 3341 CG ARG A 304 96.170 197.014 -12.578 1.00 38.91 C ANISOU 3341 CG ARG A 304 4699 3199 6884 -141 16 -568 C ATOM 3342 CD ARG A 304 95.511 196.246 -13.720 1.00 42.22 C ANISOU 3342 CD ARG A 304 5154 3580 7307 -140 -18 -645 C ATOM 3343 NE ARG A 304 94.415 195.402 -13.249 1.00 46.01 N ANISOU 3343 NE ARG A 304 5558 4056 7870 -135 -57 -651 N ATOM 3344 CZ ARG A 304 93.369 195.035 -13.988 1.00 50.13 C ANISOU 3344 CZ ARG A 304 6094 4552 8400 -136 -102 -706 C ATOM 3345 NH1 ARG A 304 93.252 195.450 -15.246 1.00 51.11 N ANISOU 3345 NH1 ARG A 304 6320 4655 8444 -136 -119 -761 N ATOM 3346 NH2 ARG A 304 92.430 194.258 -13.457 1.00 52.09 N ANISOU 3346 NH2 ARG A 304 6257 4793 8741 -134 -129 -710 N ATOM 3347 N MET A 305 95.725 197.429 -8.881 1.00 31.47 N ANISOU 3347 N MET A 305 3569 2344 6045 -116 19 -405 N ATOM 3348 CA MET A 305 94.736 198.301 -8.261 1.00 29.09 C ANISOU 3348 CA MET A 305 3264 2067 5720 -115 -2 -356 C ATOM 3349 C MET A 305 95.404 199.379 -7.423 1.00 28.53 C ANISOU 3349 C MET A 305 3193 2032 5616 -111 19 -311 C ATOM 3350 O MET A 305 95.011 200.551 -7.476 1.00 28.59 O ANISOU 3350 O MET A 305 3240 2052 5569 -117 11 -287 O ATOM 3351 CB MET A 305 93.800 197.475 -7.401 1.00 27.95 C ANISOU 3351 CB MET A 305 3049 1919 5650 -106 -19 -338 C ATOM 3352 CG MET A 305 92.725 198.261 -6.713 1.00 26.74 C ANISOU 3352 CG MET A 305 2885 1790 5486 -104 -39 -294 C ATOM 3353 SD MET A 305 91.893 197.181 -5.538 1.00 26.84 S ANISOU 3353 SD MET A 305 2813 1791 5596 -95 -37 -267 S ATOM 3354 CE MET A 305 92.897 197.469 -4.082 1.00 26.47 C ANISOU 3354 CE MET A 305 2742 1774 5542 -80 -6 -213 C ATOM 3355 N LEU A 306 96.436 199.001 -6.661 1.00 28.18 N ANISOU 3355 N LEU A 306 3103 1998 5607 -101 43 -304 N ATOM 3356 CA LEU A 306 97.183 199.968 -5.866 1.00 21.90 C ANISOU 3356 CA LEU A 306 2298 1232 4790 -97 60 -275 C ATOM 3357 C LEU A 306 97.857 201.004 -6.750 1.00 22.77 C ANISOU 3357 C LEU A 306 2471 1338 4841 -115 84 -290 C ATOM 3358 O LEU A 306 97.970 202.175 -6.369 1.00 21.54 O ANISOU 3358 O LEU A 306 2330 1200 4654 -119 90 -264 O ATOM 3359 CB LEU A 306 98.221 199.248 -5.009 1.00 21.99 C ANISOU 3359 CB LEU A 306 2253 1246 4855 -82 76 -276 C ATOM 3360 CG LEU A 306 97.676 198.221 -4.011 1.00 24.93 C ANISOU 3360 CG LEU A 306 2575 1612 5286 -65 62 -251 C ATOM 3361 CD1 LEU A 306 98.792 197.476 -3.267 1.00 25.06 C ANISOU 3361 CD1 LEU A 306 2553 1619 5350 -49 74 -253 C ATOM 3362 CD2 LEU A 306 96.749 198.917 -3.033 1.00 24.51 C ANISOU 3362 CD2 LEU A 306 2514 1584 5216 -61 46 -202 C ATOM 3363 N MET A 307 98.321 200.595 -7.932 1.00 23.31 N ANISOU 3363 N MET A 307 2581 1377 4898 -127 100 -334 N ATOM 3364 CA MET A 307 98.944 201.550 -8.840 1.00 23.79 C ANISOU 3364 CA MET A 307 2714 1422 4901 -148 131 -345 C ATOM 3365 C MET A 307 97.930 202.529 -9.416 1.00 23.78 C ANISOU 3365 C MET A 307 2794 1410 4833 -159 110 -323 C ATOM 3366 O MET A 307 98.261 203.695 -9.647 1.00 23.38 O ANISOU 3366 O MET A 307 2796 1352 4738 -175 131 -304 O ATOM 3367 CB MET A 307 99.686 200.797 -9.935 1.00 24.53 C ANISOU 3367 CB MET A 307 2838 1484 4999 -156 156 -402 C ATOM 3368 CG MET A 307 100.917 200.042 -9.418 1.00 24.83 C ANISOU 3368 CG MET A 307 2802 1530 5104 -145 184 -427 C ATOM 3369 SD MET A 307 101.646 198.987 -10.689 1.00 25.59 S ANISOU 3369 SD MET A 307 2924 1587 5214 -150 209 -503 S ATOM 3370 CE MET A 307 102.501 197.771 -9.679 1.00 24.72 C ANISOU 3370 CE MET A 307 2704 1486 5202 -124 211 -519 C ATOM 3371 N VAL A 308 96.692 202.082 -9.636 1.00 24.64 N ANISOU 3371 N VAL A 308 2910 1510 4940 -153 67 -325 N ATOM 3372 CA VAL A 308 95.654 203.004 -10.091 1.00 25.28 C ANISOU 3372 CA VAL A 308 3064 1579 4964 -158 40 -304 C ATOM 3373 C VAL A 308 95.339 204.028 -9.006 1.00 25.00 C ANISOU 3373 C VAL A 308 2997 1575 4925 -152 34 -253 C ATOM 3374 O VAL A 308 95.105 205.210 -9.298 1.00 21.75 O ANISOU 3374 O VAL A 308 2652 1151 4460 -160 34 -229 O ATOM 3375 CB VAL A 308 94.393 202.227 -10.525 1.00 25.56 C ANISOU 3375 CB VAL A 308 3098 1598 5015 -150 -7 -330 C ATOM 3376 CG1 VAL A 308 93.297 203.183 -11.003 1.00 22.49 C ANISOU 3376 CG1 VAL A 308 2782 1193 4570 -150 -41 -313 C ATOM 3377 CG2 VAL A 308 94.742 201.225 -11.603 1.00 23.04 C ANISOU 3377 CG2 VAL A 308 2810 1245 4700 -154 -4 -392 C ATOM 3378 N VAL A 309 95.382 203.610 -7.740 1.00 24.75 N ANISOU 3378 N VAL A 309 2872 1580 4951 -136 31 -236 N ATOM 3379 CA VAL A 309 95.042 204.512 -6.645 1.00 21.11 C ANISOU 3379 CA VAL A 309 2381 1149 4490 -127 22 -196 C ATOM 3380 C VAL A 309 96.078 205.619 -6.526 1.00 32.38 C ANISOU 3380 C VAL A 309 3832 2579 5892 -138 56 -187 C ATOM 3381 O VAL A 309 95.733 206.795 -6.347 1.00 31.78 O ANISOU 3381 O VAL A 309 3786 2503 5785 -141 51 -161 O ATOM 3382 CB VAL A 309 94.908 203.728 -5.329 1.00 21.14 C ANISOU 3382 CB VAL A 309 2293 1182 4556 -108 14 -183 C ATOM 3383 CG1 VAL A 309 94.643 204.672 -4.174 1.00 20.55 C ANISOU 3383 CG1 VAL A 309 2194 1137 4477 -99 6 -148 C ATOM 3384 CG2 VAL A 309 93.815 202.674 -5.447 1.00 21.13 C ANISOU 3384 CG2 VAL A 309 2266 1171 4592 -103 -13 -191 C ATOM 3385 N VAL A 310 97.364 205.258 -6.614 1.00 31.41 N ANISOU 3385 N VAL A 310 3690 2453 5792 -143 92 -210 N ATOM 3386 CA VAL A 310 98.424 206.262 -6.534 1.00 30.66 C ANISOU 3386 CA VAL A 310 3606 2354 5690 -157 130 -210 C ATOM 3387 C VAL A 310 98.437 207.150 -7.771 1.00 30.10 C ANISOU 3387 C VAL A 310 3638 2241 5558 -184 151 -206 C ATOM 3388 O VAL A 310 98.782 208.336 -7.692 1.00 30.49 O ANISOU 3388 O VAL A 310 3714 2279 5592 -198 173 -189 O ATOM 3389 CB VAL A 310 99.796 205.599 -6.307 1.00 30.78 C ANISOU 3389 CB VAL A 310 3565 2374 5755 -155 163 -243 C ATOM 3390 CG1 VAL A 310 99.776 204.719 -5.051 1.00 30.29 C ANISOU 3390 CG1 VAL A 310 3417 2343 5749 -127 137 -239 C ATOM 3391 CG2 VAL A 310 100.216 204.792 -7.534 1.00 31.55 C ANISOU 3391 CG2 VAL A 310 3700 2441 5845 -168 185 -279 C ATOM 3392 N LEU A 311 98.078 206.601 -8.929 1.00 31.49 N ANISOU 3392 N LEU A 311 3880 2385 5700 -191 145 -223 N ATOM 3393 CA LEU A 311 97.985 207.432 -10.122 1.00 32.57 C ANISOU 3393 CA LEU A 311 4135 2471 5769 -214 158 -213 C ATOM 3394 C LEU A 311 96.865 208.455 -9.977 1.00 32.60 C ANISOU 3394 C LEU A 311 4187 2467 5733 -208 125 -172 C ATOM 3395 O LEU A 311 97.051 209.641 -10.280 1.00 32.69 O ANISOU 3395 O LEU A 311 4266 2446 5708 -223 145 -145 O ATOM 3396 CB LEU A 311 97.763 206.563 -11.360 1.00 32.86 C ANISOU 3396 CB LEU A 311 4239 2471 5775 -216 149 -247 C ATOM 3397 CG LEU A 311 97.149 207.281 -12.556 1.00 33.06 C ANISOU 3397 CG LEU A 311 4406 2438 5719 -224 136 -233 C ATOM 3398 CD1 LEU A 311 98.040 208.429 -12.981 1.00 23.32 C ANISOU 3398 CD1 LEU A 311 3239 1165 4456 -252 185 -205 C ATOM 3399 CD2 LEU A 311 96.951 206.297 -13.675 1.00 23.33 C ANISOU 3399 CD2 LEU A 311 3232 1170 4461 -219 120 -282 C ATOM 3400 N VAL A 312 95.691 208.015 -9.503 1.00 32.37 N ANISOU 3400 N VAL A 312 4119 2463 5716 -185 76 -168 N ATOM 3401 CA VAL A 312 94.583 208.944 -9.303 1.00 21.72 C ANISOU 3401 CA VAL A 312 2804 1110 4339 -175 42 -135 C ATOM 3402 C VAL A 312 94.877 209.914 -8.171 1.00 21.48 C ANISOU 3402 C VAL A 312 2723 1106 4332 -173 54 -109 C ATOM 3403 O VAL A 312 94.362 211.037 -8.162 1.00 21.57 O ANISOU 3403 O VAL A 312 2783 1099 4314 -172 45 -82 O ATOM 3404 CB VAL A 312 93.282 208.177 -9.032 1.00 21.94 C ANISOU 3404 CB VAL A 312 2786 1159 4392 -153 -9 -144 C ATOM 3405 CG1 VAL A 312 92.131 209.155 -8.857 1.00 21.49 C ANISOU 3405 CG1 VAL A 312 2757 1095 4311 -141 -43 -115 C ATOM 3406 CG2 VAL A 312 92.998 207.191 -10.162 1.00 22.12 C ANISOU 3406 CG2 VAL A 312 2853 1151 4402 -154 -24 -182 C ATOM 3407 N PHE A 313 95.662 209.486 -7.176 1.00 22.48 N ANISOU 3407 N PHE A 313 2754 1273 4514 -168 71 -121 N ATOM 3408 CA PHE A 313 96.067 210.379 -6.093 1.00 21.06 C ANISOU 3408 CA PHE A 313 2527 1114 4360 -165 81 -109 C ATOM 3409 C PHE A 313 96.990 211.477 -6.590 1.00 21.48 C ANISOU 3409 C PHE A 313 2636 1129 4397 -191 126 -104 C ATOM 3410 O PHE A 313 96.943 212.609 -6.096 1.00 21.56 O ANISOU 3410 O PHE A 313 2649 1131 4410 -194 128 -88 O ATOM 3411 CB PHE A 313 96.757 209.579 -4.994 1.00 20.77 C ANISOU 3411 CB PHE A 313 2388 1120 4385 -150 86 -127 C ATOM 3412 CG PHE A 313 97.417 210.433 -3.931 1.00 23.90 C ANISOU 3412 CG PHE A 313 2738 1531 4812 -147 97 -127 C ATOM 3413 CD1 PHE A 313 96.695 210.860 -2.830 1.00 23.68 C ANISOU 3413 CD1 PHE A 313 2674 1528 4794 -128 65 -111 C ATOM 3414 CD2 PHE A 313 98.762 210.778 -4.013 1.00 20.98 C ANISOU 3414 CD2 PHE A 313 2356 1148 4468 -163 140 -150 C ATOM 3415 CE1 PHE A 313 97.292 211.625 -1.842 1.00 20.39 C ANISOU 3415 CE1 PHE A 313 2218 1122 4409 -124 69 -120 C ATOM 3416 CE2 PHE A 313 99.364 211.546 -3.023 1.00 21.00 C ANISOU 3416 CE2 PHE A 313 2310 1159 4509 -160 145 -160 C ATOM 3417 CZ PHE A 313 98.624 211.965 -1.935 1.00 20.69 C ANISOU 3417 CZ PHE A 313 2242 1145 4476 -139 107 -146 C ATOM 3418 N ALA A 314 97.869 211.151 -7.535 1.00 21.84 N ANISOU 3418 N ALA A 314 2719 1145 4433 -214 165 -121 N ATOM 3419 CA ALA A 314 98.738 212.176 -8.091 1.00 22.38 C ANISOU 3419 CA ALA A 314 2842 1169 4493 -245 215 -114 C ATOM 3420 C ALA A 314 97.947 213.138 -8.955 1.00 22.76 C ANISOU 3420 C ALA A 314 3012 1162 4475 -255 204 -74 C ATOM 3421 O ALA A 314 98.245 214.336 -8.985 1.00 23.19 O ANISOU 3421 O ALA A 314 3102 1180 4529 -274 230 -51 O ATOM 3422 CB ALA A 314 99.869 211.529 -8.878 1.00 22.72 C ANISOU 3422 CB ALA A 314 2891 1194 4548 -268 264 -143 C ATOM 3423 N ILE A 315 96.897 212.639 -9.610 1.00 22.68 N ANISOU 3423 N ILE A 315 3062 1139 4414 -239 163 -67 N ATOM 3424 CA ILE A 315 96.084 213.488 -10.470 1.00 23.09 C ANISOU 3424 CA ILE A 315 3242 1131 4399 -238 144 -30 C ATOM 3425 C ILE A 315 95.237 214.432 -9.629 1.00 25.65 C ANISOU 3425 C ILE A 315 3549 1467 4730 -219 115 -5 C ATOM 3426 O ILE A 315 95.144 215.630 -9.921 1.00 26.55 O ANISOU 3426 O ILE A 315 3742 1530 4818 -226 123 30 O ATOM 3427 CB ILE A 315 95.219 212.630 -11.416 1.00 23.10 C ANISOU 3427 CB ILE A 315 3313 1113 4351 -220 105 -42 C ATOM 3428 CG1 ILE A 315 96.089 211.781 -12.335 1.00 23.37 C ANISOU 3428 CG1 ILE A 315 3377 1125 4376 -238 133 -72 C ATOM 3429 CG2 ILE A 315 94.357 213.491 -12.305 1.00 23.58 C ANISOU 3429 CG2 ILE A 315 3517 1104 4338 -205 80 -5 C ATOM 3430 CD1 ILE A 315 95.272 210.924 -13.278 1.00 24.43 C ANISOU 3430 CD1 ILE A 315 3583 1234 4467 -217 93 -97 C ATOM 3431 N CYS A 316 94.642 213.923 -8.546 1.00 24.42 N ANISOU 3431 N CYS A 316 3288 1375 4616 -195 81 -21 N ATOM 3432 CA CYS A 316 93.704 214.741 -7.780 1.00 23.78 C ANISOU 3432 CA CYS A 316 3190 1305 4542 -174 48 -1 C ATOM 3433 C CYS A 316 94.423 215.833 -6.998 1.00 23.68 C ANISOU 3433 C CYS A 316 3145 1288 4563 -187 77 5 C ATOM 3434 O CYS A 316 94.022 217.003 -7.036 1.00 23.48 O ANISOU 3434 O CYS A 316 3176 1223 4522 -185 73 31 O ATOM 3435 CB CYS A 316 92.877 213.853 -6.844 1.00 22.81 C ANISOU 3435 CB CYS A 316 2963 1245 4458 -149 6 -18 C ATOM 3436 SG CYS A 316 91.679 212.812 -7.715 1.00 22.83 S ANISOU 3436 SG CYS A 316 2996 1241 4436 -132 -38 -29 S ATOM 3437 N TYR A 317 95.500 215.473 -6.297 1.00 23.53 N ANISOU 3437 N TYR A 317 3039 1304 4597 -197 105 -22 N ATOM 3438 CA TYR A 317 96.243 216.408 -5.454 1.00 23.54 C ANISOU 3438 CA TYR A 317 2994 1304 4646 -206 129 -29 C ATOM 3439 C TYR A 317 97.261 217.255 -6.213 1.00 24.54 C ANISOU 3439 C TYR A 317 3181 1368 4774 -244 186 -22 C ATOM 3440 O TYR A 317 97.741 218.255 -5.664 1.00 25.08 O ANISOU 3440 O TYR A 317 3228 1418 4885 -256 207 -26 O ATOM 3441 CB TYR A 317 96.941 215.648 -4.319 1.00 22.58 C ANISOU 3441 CB TYR A 317 2754 1242 4586 -194 129 -65 C ATOM 3442 CG TYR A 317 95.982 215.131 -3.261 1.00 22.03 C ANISOU 3442 CG TYR A 317 2618 1224 4527 -160 78 -65 C ATOM 3443 CD1 TYR A 317 95.325 213.922 -3.427 1.00 22.16 C ANISOU 3443 CD1 TYR A 317 2620 1269 4530 -145 52 -64 C ATOM 3444 CD2 TYR A 317 95.729 215.854 -2.104 1.00 21.94 C ANISOU 3444 CD2 TYR A 317 2563 1229 4545 -145 57 -69 C ATOM 3445 CE1 TYR A 317 94.453 213.442 -2.471 1.00 22.27 C ANISOU 3445 CE1 TYR A 317 2576 1325 4562 -120 13 -60 C ATOM 3446 CE2 TYR A 317 94.848 215.383 -1.139 1.00 22.14 C ANISOU 3446 CE2 TYR A 317 2536 1298 4580 -118 16 -66 C ATOM 3447 CZ TYR A 317 94.215 214.172 -1.331 1.00 22.49 C ANISOU 3447 CZ TYR A 317 2566 1368 4612 -107 -3 -59 C ATOM 3448 OH TYR A 317 93.334 213.673 -0.391 1.00 22.59 O ANISOU 3448 OH TYR A 317 2528 1416 4640 -84 -35 -54 O ATOM 3449 N ALA A 318 97.573 216.906 -7.461 1.00 24.79 N ANISOU 3449 N ALA A 318 3291 1363 4766 -265 212 -10 N ATOM 3450 CA ALA A 318 98.527 217.709 -8.222 1.00 24.29 C ANISOU 3450 CA ALA A 318 3287 1235 4709 -306 272 4 C ATOM 3451 C ALA A 318 98.094 219.161 -8.338 1.00 28.94 C ANISOU 3451 C ALA A 318 3950 1762 5285 -313 273 45 C ATOM 3452 O ALA A 318 98.924 220.053 -8.086 1.00 25.53 O ANISOU 3452 O ALA A 318 3495 1298 4906 -342 319 42 O ATOM 3453 CB ALA A 318 98.753 217.088 -9.598 1.00 24.60 C ANISOU 3453 CB ALA A 318 3411 1239 4697 -324 292 16 C ATOM 3454 N PRO A 319 96.852 219.477 -8.721 1.00 28.85 N ANISOU 3454 N PRO A 319 4027 1724 5212 -288 225 81 N ATOM 3455 CA PRO A 319 96.491 220.901 -8.858 1.00 29.22 C ANISOU 3455 CA PRO A 319 4150 1700 5250 -291 226 123 C ATOM 3456 C PRO A 319 96.601 221.683 -7.561 1.00 29.06 C ANISOU 3456 C PRO A 319 4041 1701 5301 -287 227 99 C ATOM 3457 O PRO A 319 97.212 222.761 -7.542 1.00 30.34 O ANISOU 3457 O PRO A 319 4218 1807 5504 -315 267 110 O ATOM 3458 CB PRO A 319 95.047 220.848 -9.385 1.00 25.55 C ANISOU 3458 CB PRO A 319 3783 1218 4709 -250 165 154 C ATOM 3459 CG PRO A 319 94.913 219.497 -9.990 1.00 25.07 C ANISOU 3459 CG PRO A 319 3728 1188 4609 -242 149 136 C ATOM 3460 CD PRO A 319 95.750 218.593 -9.136 1.00 24.43 C ANISOU 3460 CD PRO A 319 3506 1186 4592 -255 171 85 C ATOM 3461 N ILE A 320 96.054 221.164 -6.461 1.00 27.28 N ANISOU 3461 N ILE A 320 3719 1550 5097 -255 184 66 N ATOM 3462 CA ILE A 320 96.110 221.921 -5.220 1.00 26.57 C ANISOU 3462 CA ILE A 320 3551 1475 5070 -247 176 42 C ATOM 3463 C ILE A 320 97.549 222.059 -4.747 1.00 27.59 C ANISOU 3463 C ILE A 320 3602 1606 5275 -278 227 3 C ATOM 3464 O ILE A 320 97.943 223.116 -4.241 1.00 29.24 O ANISOU 3464 O ILE A 320 3790 1779 5540 -292 246 -10 O ATOM 3465 CB ILE A 320 95.207 221.271 -4.155 1.00 25.03 C ANISOU 3465 CB ILE A 320 3273 1357 4880 -206 119 20 C ATOM 3466 CG1 ILE A 320 94.977 222.223 -2.990 1.00 23.93 C ANISOU 3466 CG1 ILE A 320 3083 1219 4792 -192 100 2 C ATOM 3467 CG2 ILE A 320 95.826 219.993 -3.643 1.00 23.18 C ANISOU 3467 CG2 ILE A 320 2943 1193 4671 -202 120 -15 C ATOM 3468 CD1 ILE A 320 93.988 221.712 -2.006 1.00 23.18 C ANISOU 3468 CD1 ILE A 320 2921 1188 4697 -154 45 -10 C ATOM 3469 N SER A 321 98.365 221.011 -4.917 1.00 26.54 N ANISOU 3469 N SER A 321 3422 1511 5152 -289 250 -22 N ATOM 3470 CA SER A 321 99.737 221.098 -4.418 1.00 26.11 C ANISOU 3470 CA SER A 321 3283 1462 5178 -312 297 -67 C ATOM 3471 C SER A 321 100.566 222.053 -5.259 1.00 27.15 C ANISOU 3471 C SER A 321 3471 1511 5335 -362 367 -51 C ATOM 3472 O SER A 321 101.420 222.769 -4.728 1.00 28.17 O ANISOU 3472 O SER A 321 3541 1616 5544 -384 403 -86 O ATOM 3473 CB SER A 321 100.414 219.723 -4.383 1.00 25.35 C ANISOU 3473 CB SER A 321 3120 1421 5090 -307 304 -99 C ATOM 3474 OG SER A 321 99.747 218.846 -3.489 1.00 24.44 O ANISOU 3474 OG SER A 321 2944 1376 4965 -264 245 -112 O ATOM 3475 N ILE A 322 100.325 222.087 -6.570 1.00 27.46 N ANISOU 3475 N ILE A 322 3623 1500 5311 -381 388 0 N ATOM 3476 CA ILE A 322 101.063 223.012 -7.421 1.00 27.80 C ANISOU 3476 CA ILE A 322 3727 1457 5378 -431 460 28 C ATOM 3477 C ILE A 322 100.598 224.437 -7.173 1.00 39.38 C ANISOU 3477 C ILE A 322 5238 2858 6866 -434 455 56 C ATOM 3478 O ILE A 322 101.413 225.361 -7.084 1.00 29.51 O ANISOU 3478 O ILE A 322 3967 1553 5691 -472 514 47 O ATOM 3479 CB ILE A 322 100.908 222.619 -8.900 1.00 28.10 C ANISOU 3479 CB ILE A 322 3881 1457 5338 -446 478 82 C ATOM 3480 CG1 ILE A 322 101.377 221.189 -9.132 1.00 27.43 C ANISOU 3480 CG1 ILE A 322 3749 1432 5240 -442 484 47 C ATOM 3481 CG2 ILE A 322 101.720 223.540 -9.789 1.00 29.47 C ANISOU 3481 CG2 ILE A 322 4114 1541 5542 -500 563 122 C ATOM 3482 CD1 ILE A 322 102.865 221.014 -8.970 1.00 27.83 C ANISOU 3482 CD1 ILE A 322 3709 1491 5375 -478 562 -2 C ATOM 3483 N LEU A 323 99.280 224.638 -7.054 1.00 38.36 N ANISOU 3483 N LEU A 323 5167 2730 6677 -394 387 86 N ATOM 3484 CA LEU A 323 98.736 225.968 -6.793 1.00 38.38 C ANISOU 3484 CA LEU A 323 5216 2669 6699 -389 374 111 C ATOM 3485 C LEU A 323 99.174 226.500 -5.432 1.00 37.29 C ANISOU 3485 C LEU A 323 4960 2552 6657 -389 376 48 C ATOM 3486 O LEU A 323 99.269 227.719 -5.239 1.00 37.83 O ANISOU 3486 O LEU A 323 5046 2550 6779 -406 396 53 O ATOM 3487 CB LEU A 323 97.214 225.927 -6.873 1.00 37.74 C ANISOU 3487 CB LEU A 323 5207 2595 6537 -339 299 144 C ATOM 3488 CG LEU A 323 96.548 225.916 -8.246 1.00 28.75 C ANISOU 3488 CG LEU A 323 4220 1398 5306 -329 283 214 C ATOM 3489 CD1 LEU A 323 95.059 225.702 -8.086 1.00 28.12 C ANISOU 3489 CD1 LEU A 323 4178 1343 5161 -270 208 223 C ATOM 3490 CD2 LEU A 323 96.819 227.225 -8.947 1.00 30.20 C ANISOU 3490 CD2 LEU A 323 4502 1466 5506 -357 322 273 C ATOM 3491 N ASN A 324 99.424 225.606 -4.472 1.00 35.50 N ANISOU 3491 N ASN A 324 4618 2416 6457 -368 350 -10 N ATOM 3492 CA ASN A 324 99.867 226.046 -3.155 1.00 35.08 C ANISOU 3492 CA ASN A 324 4455 2382 6492 -363 342 -73 C ATOM 3493 C ASN A 324 101.304 226.553 -3.183 1.00 35.53 C ANISOU 3493 C ASN A 324 4460 2394 6644 -412 415 -111 C ATOM 3494 O ASN A 324 101.638 227.514 -2.481 1.00 35.19 O ANISOU 3494 O ASN A 324 4372 2315 6685 -424 424 -149 O ATOM 3495 CB ASN A 324 99.728 224.914 -2.147 1.00 34.58 C ANISOU 3495 CB ASN A 324 4292 2422 6425 -323 290 -116 C ATOM 3496 CG ASN A 324 100.143 225.333 -0.756 1.00 35.66 C ANISOU 3496 CG ASN A 324 4324 2580 6646 -311 269 -182 C ATOM 3497 OD1 ASN A 324 99.485 226.168 -0.128 1.00 36.08 O ANISOU 3497 OD1 ASN A 324 4381 2614 6715 -294 236 -187 O ATOM 3498 ND2 ASN A 324 101.241 224.759 -0.262 1.00 35.86 N ANISOU 3498 ND2 ASN A 324 4257 2641 6728 -316 285 -237 N ATOM 3499 N VAL A 325 102.172 225.924 -3.981 1.00 35.85 N ANISOU 3499 N VAL A 325 4503 2436 6683 -443 471 -109 N ATOM 3500 CA VAL A 325 103.555 226.388 -4.041 1.00 37.80 C ANISOU 3500 CA VAL A 325 4694 2640 7030 -493 550 -150 C ATOM 3501 C VAL A 325 103.674 227.636 -4.904 1.00 39.92 C ANISOU 3501 C VAL A 325 5051 2796 7321 -541 615 -99 C ATOM 3502 O VAL A 325 104.459 228.536 -4.597 1.00 41.72 O ANISOU 3502 O VAL A 325 5230 2967 7653 -578 666 -136 O ATOM 3503 CB VAL A 325 104.504 225.274 -4.527 1.00 37.61 C ANISOU 3503 CB VAL A 325 4629 2656 7007 -508 594 -173 C ATOM 3504 CG1 VAL A 325 104.493 224.086 -3.563 1.00 36.38 C ANISOU 3504 CG1 VAL A 325 4377 2601 6846 -459 531 -224 C ATOM 3505 CG2 VAL A 325 104.152 224.839 -5.935 1.00 37.53 C ANISOU 3505 CG2 VAL A 325 4734 2623 6904 -522 618 -101 C ATOM 3506 N LEU A 326 102.918 227.717 -6.000 1.00 39.99 N ANISOU 3506 N LEU A 326 5191 2763 7238 -541 614 -15 N ATOM 3507 CA LEU A 326 102.978 228.935 -6.797 1.00 33.13 C ANISOU 3507 CA LEU A 326 4418 1780 6391 -582 671 45 C ATOM 3508 C LEU A 326 102.493 230.130 -5.991 1.00 34.88 C ANISOU 3508 C LEU A 326 4633 1952 6667 -571 642 33 C ATOM 3509 O LEU A 326 103.036 231.234 -6.124 1.00 36.19 O ANISOU 3509 O LEU A 326 4808 2026 6916 -615 705 39 O ATOM 3510 CB LEU A 326 102.141 228.782 -8.066 1.00 33.19 C ANISOU 3510 CB LEU A 326 4575 1753 6283 -572 656 141 C ATOM 3511 CG LEU A 326 102.470 227.604 -8.975 1.00 32.72 C ANISOU 3511 CG LEU A 326 4537 1735 6160 -579 678 158 C ATOM 3512 CD1 LEU A 326 101.506 227.590 -10.147 1.00 35.76 C ANISOU 3512 CD1 LEU A 326 5075 2078 6435 -560 644 250 C ATOM 3513 CD2 LEU A 326 103.904 227.710 -9.452 1.00 33.75 C ANISOU 3513 CD2 LEU A 326 4626 1831 6367 -642 793 143 C ATOM 3514 N LYS A 327 101.507 229.918 -5.120 1.00 33.94 N ANISOU 3514 N LYS A 327 4492 1893 6511 -515 552 12 N ATOM 3515 CA LYS A 327 100.960 231.014 -4.333 1.00 34.47 C ANISOU 3515 CA LYS A 327 4554 1916 6625 -499 519 -3 C ATOM 3516 C LYS A 327 101.853 231.351 -3.145 1.00 34.48 C ANISOU 3516 C LYS A 327 4417 1932 6752 -514 532 -99 C ATOM 3517 O LYS A 327 102.206 232.517 -2.936 1.00 34.57 O ANISOU 3517 O LYS A 327 4421 1859 6855 -544 567 -117 O ATOM 3518 CB LYS A 327 99.547 230.663 -3.855 1.00 33.54 C ANISOU 3518 CB LYS A 327 4462 1857 6425 -434 424 8 C ATOM 3519 CG LYS A 327 99.032 231.563 -2.728 1.00 33.98 C ANISOU 3519 CG LYS A 327 4476 1897 6539 -408 381 -32 C ATOM 3520 CD LYS A 327 97.749 231.041 -2.108 1.00 30.84 C ANISOU 3520 CD LYS A 327 4072 1576 6071 -345 296 -34 C ATOM 3521 CE LYS A 327 97.369 231.819 -0.866 1.00 30.97 C ANISOU 3521 CE LYS A 327 4026 1588 6152 -320 256 -87 C ATOM 3522 NZ LYS A 327 96.164 232.659 -1.075 1.00 31.38 N ANISOU 3522 NZ LYS A 327 4174 1581 6170 -289 223 -43 N ATOM 3523 N ARG A 328 102.242 230.339 -2.368 1.00 33.16 N ANISOU 3523 N ARG A 328 4141 1865 6592 -491 502 -163 N ATOM 3524 CA ARG A 328 102.948 230.572 -1.113 1.00 33.26 C ANISOU 3524 CA ARG A 328 4022 1901 6712 -490 491 -260 C ATOM 3525 C ARG A 328 104.463 230.591 -1.256 1.00 33.26 C ANISOU 3525 C ARG A 328 3945 1878 6814 -541 570 -315 C ATOM 3526 O ARG A 328 105.144 231.219 -0.439 1.00 33.99 O ANISOU 3526 O ARG A 328 3946 1948 7020 -555 578 -395 O ATOM 3527 CB ARG A 328 102.567 229.504 -0.081 1.00 30.88 C ANISOU 3527 CB ARG A 328 3644 1717 6373 -432 411 -301 C ATOM 3528 CG ARG A 328 101.095 229.434 0.278 1.00 30.47 C ANISOU 3528 CG ARG A 328 3640 1698 6237 -380 334 -264 C ATOM 3529 CD ARG A 328 100.685 230.502 1.283 1.00 31.08 C ANISOU 3529 CD ARG A 328 3689 1745 6376 -364 297 -306 C ATOM 3530 NE ARG A 328 99.313 230.317 1.761 1.00 30.08 N ANISOU 3530 NE ARG A 328 3590 1663 6177 -311 224 -282 N ATOM 3531 CZ ARG A 328 98.622 231.224 2.451 1.00 30.47 C ANISOU 3531 CZ ARG A 328 3642 1682 6254 -289 186 -301 C ATOM 3532 NH1 ARG A 328 99.164 232.399 2.750 1.00 31.37 N ANISOU 3532 NH1 ARG A 328 3735 1718 6468 -315 211 -345 N ATOM 3533 NH2 ARG A 328 97.381 230.956 2.839 1.00 29.34 N ANISOU 3533 NH2 ARG A 328 3519 1584 6044 -241 127 -279 N ATOM 3534 N VAL A 329 105.015 229.891 -2.236 1.00 38.56 N ANISOU 3534 N VAL A 329 4643 2556 7451 -568 626 -283 N ATOM 3535 CA VAL A 329 106.468 229.824 -2.334 1.00 40.34 C ANISOU 3535 CA VAL A 329 4784 2766 7777 -614 703 -344 C ATOM 3536 C VAL A 329 107.005 230.849 -3.322 1.00 42.61 C ANISOU 3536 C VAL A 329 5132 2938 8122 -683 808 -304 C ATOM 3537 O VAL A 329 108.031 231.483 -3.063 1.00 44.05 O ANISOU 3537 O VAL A 329 5234 3069 8432 -727 870 -369 O ATOM 3538 CB VAL A 329 106.922 228.397 -2.704 1.00 39.79 C ANISOU 3538 CB VAL A 329 4687 2776 7655 -602 710 -349 C ATOM 3539 CG1 VAL A 329 108.428 228.359 -2.866 1.00 40.60 C ANISOU 3539 CG1 VAL A 329 4703 2859 7866 -650 796 -415 C ATOM 3540 CG2 VAL A 329 106.473 227.401 -1.636 1.00 38.92 C ANISOU 3540 CG2 VAL A 329 4511 2773 7505 -535 612 -388 C ATOM 3541 N PHE A 330 106.319 231.038 -4.449 1.00 43.45 N ANISOU 3541 N PHE A 330 5377 2994 8139 -694 829 -200 N ATOM 3542 CA PHE A 330 106.806 231.908 -5.509 1.00 45.61 C ANISOU 3542 CA PHE A 330 5723 3154 8453 -759 934 -143 C ATOM 3543 C PHE A 330 106.048 233.225 -5.623 1.00 48.31 C ANISOU 3543 C PHE A 330 6157 3394 8806 -764 928 -85 C ATOM 3544 O PHE A 330 106.423 234.066 -6.448 1.00 49.55 O ANISOU 3544 O PHE A 330 6378 3443 9006 -818 1018 -31 O ATOM 3545 CB PHE A 330 106.766 231.172 -6.842 1.00 44.62 C ANISOU 3545 CB PHE A 330 5694 3035 8226 -771 975 -62 C ATOM 3546 CG PHE A 330 107.708 230.017 -6.902 1.00 43.76 C ANISOU 3546 CG PHE A 330 5498 3001 8126 -779 1006 -118 C ATOM 3547 CD1 PHE A 330 109.066 230.225 -7.069 1.00 45.03 C ANISOU 3547 CD1 PHE A 330 5583 3126 8401 -838 1112 -168 C ATOM 3548 CD2 PHE A 330 107.241 228.720 -6.784 1.00 42.18 C ANISOU 3548 CD2 PHE A 330 5292 2904 7832 -727 933 -124 C ATOM 3549 CE1 PHE A 330 109.939 229.162 -7.121 1.00 44.72 C ANISOU 3549 CE1 PHE A 330 5463 3154 8375 -841 1140 -225 C ATOM 3550 CE2 PHE A 330 108.108 227.653 -6.839 1.00 41.87 C ANISOU 3550 CE2 PHE A 330 5176 2927 7807 -731 960 -176 C ATOM 3551 CZ PHE A 330 109.460 227.874 -7.006 1.00 43.12 C ANISOU 3551 CZ PHE A 330 5259 3050 8073 -786 1062 -228 C ATOM 3552 N GLY A 331 105.001 233.427 -4.826 1.00 49.40 N ANISOU 3552 N GLY A 331 6303 3558 8908 -710 830 -94 N ATOM 3553 CA GLY A 331 104.323 234.708 -4.833 1.00 52.03 C ANISOU 3553 CA GLY A 331 6713 3789 9265 -711 821 -52 C ATOM 3554 C GLY A 331 103.410 234.938 -6.012 1.00 53.78 C ANISOU 3554 C GLY A 331 7104 3952 9378 -701 817 72 C ATOM 3555 O GLY A 331 103.011 236.075 -6.260 1.00 55.04 O ANISOU 3555 O GLY A 331 7344 4003 9565 -710 831 122 O ATOM 3556 N MET A 332 103.081 233.893 -6.761 1.00 54.39 N ANISOU 3556 N MET A 332 7238 4090 9336 -679 797 122 N ATOM 3557 CA MET A 332 102.207 234.058 -7.908 1.00 56.82 C ANISOU 3557 CA MET A 332 7707 4343 9538 -663 783 236 C ATOM 3558 C MET A 332 100.796 234.423 -7.471 1.00 58.83 C ANISOU 3558 C MET A 332 8024 4596 9734 -598 679 254 C ATOM 3559 O MET A 332 100.359 234.131 -6.350 1.00 58.46 O ANISOU 3559 O MET A 332 7895 4626 9692 -558 610 183 O ATOM 3560 CB MET A 332 102.169 232.787 -8.743 1.00 55.90 C ANISOU 3560 CB MET A 332 7626 4298 9314 -651 775 269 C ATOM 3561 CG MET A 332 103.325 232.669 -9.703 1.00 57.32 C ANISOU 3561 CG MET A 332 7813 4441 9526 -715 892 298 C ATOM 3562 SD MET A 332 102.858 231.699 -11.145 1.00 57.61 S ANISOU 3562 SD MET A 332 7973 4501 9417 -696 879 390 S ATOM 3563 CE MET A 332 101.491 232.672 -11.782 1.00 58.65 C ANISOU 3563 CE MET A 332 8275 4537 9475 -653 815 505 C ATOM 3564 N PHE A 333 100.079 235.087 -8.375 1.00 61.60 N ANISOU 3564 N PHE A 333 8520 4854 10029 -585 670 353 N ATOM 3565 CA PHE A 333 98.676 235.439 -8.213 1.00 62.84 C ANISOU 3565 CA PHE A 333 8761 4996 10118 -518 575 383 C ATOM 3566 C PHE A 333 98.495 236.708 -7.382 1.00 67.00 C ANISOU 3566 C PHE A 333 9269 5447 10740 -516 571 353 C ATOM 3567 O PHE A 333 97.380 237.234 -7.311 1.00 67.44 O ANISOU 3567 O PHE A 333 9405 5465 10755 -463 505 383 O ATOM 3568 CB PHE A 333 97.856 234.305 -7.569 1.00 59.42 C ANISOU 3568 CB PHE A 333 8278 4695 9602 -459 483 332 C ATOM 3569 CG PHE A 333 98.116 232.945 -8.153 1.00 57.40 C ANISOU 3569 CG PHE A 333 8012 4525 9272 -463 485 336 C ATOM 3570 CD1 PHE A 333 98.127 232.745 -9.520 1.00 57.58 C ANISOU 3570 CD1 PHE A 333 8149 4504 9227 -473 505 422 C ATOM 3571 CD2 PHE A 333 98.351 231.862 -7.317 1.00 55.99 C ANISOU 3571 CD2 PHE A 333 7708 4469 9097 -452 463 256 C ATOM 3572 CE1 PHE A 333 98.355 231.486 -10.051 1.00 56.85 C ANISOU 3572 CE1 PHE A 333 8045 4486 9070 -474 504 420 C ATOM 3573 CE2 PHE A 333 98.582 230.594 -7.843 1.00 55.21 C ANISOU 3573 CE2 PHE A 333 7600 4442 8936 -453 464 257 C ATOM 3574 CZ PHE A 333 98.583 230.406 -9.211 1.00 55.50 C ANISOU 3574 CZ PHE A 333 7751 4433 8905 -466 485 334 C ATOM 3575 N ALA A 334 99.545 237.202 -6.728 1.00 70.12 N ANISOU 3575 N ALA A 334 9556 5818 11268 -569 637 286 N ATOM 3576 CA ALA A 334 99.405 238.412 -5.929 1.00 73.10 C ANISOU 3576 CA ALA A 334 9911 6118 11748 -569 632 248 C ATOM 3577 C ALA A 334 98.986 239.586 -6.802 1.00 76.72 C ANISOU 3577 C ALA A 334 10517 6423 12209 -572 655 350 C ATOM 3578 O ALA A 334 97.988 240.260 -6.522 1.00 77.07 O ANISOU 3578 O ALA A 334 10625 6420 12239 -522 593 365 O ATOM 3579 CB ALA A 334 100.716 238.722 -5.203 1.00 73.66 C ANISOU 3579 CB ALA A 334 9840 6179 11969 -630 703 156 C ATOM 3580 N HIS A 335 99.722 239.823 -7.887 1.00 79.59 N ANISOU 3580 N HIS A 335 10942 6708 12591 -626 747 426 N ATOM 3581 CA HIS A 335 99.408 240.886 -8.843 1.00 83.04 C ANISOU 3581 CA HIS A 335 11527 6994 13030 -630 778 543 C ATOM 3582 C HIS A 335 98.525 240.281 -9.925 1.00 83.31 C ANISOU 3582 C HIS A 335 11697 7050 12908 -576 718 646 C ATOM 3583 O HIS A 335 99.002 239.816 -10.961 1.00 83.56 O ANISOU 3583 O HIS A 335 11772 7083 12895 -604 773 716 O ATOM 3584 CB HIS A 335 100.680 241.502 -9.417 1.00 84.31 C ANISOU 3584 CB HIS A 335 11676 7055 13302 -718 920 576 C ATOM 3585 CG HIS A 335 101.619 242.041 -8.379 1.00 85.83 C ANISOU 3585 CG HIS A 335 11725 7227 13661 -773 977 462 C ATOM 3586 ND1 HIS A 335 102.468 241.233 -7.653 1.00 83.27 N ANISOU 3586 ND1 HIS A 335 11244 7014 13383 -799 993 349 N ATOM 3587 CD2 HIS A 335 101.843 243.305 -7.947 1.00 86.03 C ANISOU 3587 CD2 HIS A 335 11737 7129 13823 -803 1017 440 C ATOM 3588 CE1 HIS A 335 103.175 241.975 -6.819 1.00 85.05 C ANISOU 3588 CE1 HIS A 335 11362 7189 13764 -841 1036 260 C ATOM 3589 NE2 HIS A 335 102.815 243.236 -6.977 1.00 85.94 N ANISOU 3589 NE2 HIS A 335 11556 7158 13937 -847 1053 310 N ATOM 3590 N THR A 336 97.216 240.296 -9.685 1.00 83.89 N ANISOU 3590 N THR A 336 11834 7140 12900 -496 604 653 N ATOM 3591 CA THR A 336 96.271 239.530 -10.488 1.00 84.62 C ANISOU 3591 CA THR A 336 12028 7280 12846 -432 521 719 C ATOM 3592 C THR A 336 95.843 240.305 -11.732 1.00 86.52 C ANISOU 3592 C THR A 336 12432 7390 13051 -409 518 861 C ATOM 3593 O THR A 336 95.500 241.490 -11.652 1.00 87.72 O ANISOU 3593 O THR A 336 12649 7423 13257 -392 514 898 O ATOM 3594 CB THR A 336 95.047 239.163 -9.646 1.00 84.48 C ANISOU 3594 CB THR A 336 11995 7341 12761 -352 408 655 C ATOM 3595 OG1 THR A 336 94.159 238.336 -10.410 1.00 84.83 O ANISOU 3595 OG1 THR A 336 12127 7434 12670 -292 328 704 O ATOM 3596 CG2 THR A 336 94.310 240.422 -9.191 1.00 85.80 C ANISOU 3596 CG2 THR A 336 12220 7407 12975 -311 373 660 C ATOM 3597 N GLU A 337 95.874 239.631 -12.884 1.00 87.06 N ANISOU 3597 N GLU A 337 12564 7479 13035 -403 520 944 N ATOM 3598 CA GLU A 337 95.239 240.136 -14.094 1.00 89.22 C ANISOU 3598 CA GLU A 337 12987 7658 13253 -355 487 1088 C ATOM 3599 C GLU A 337 93.784 239.695 -14.179 1.00 87.68 C ANISOU 3599 C GLU A 337 12855 7507 12951 -252 327 1093 C ATOM 3600 O GLU A 337 92.915 240.486 -14.568 1.00 89.04 O ANISOU 3600 O GLU A 337 13131 7588 13111 -186 257 1170 O ATOM 3601 CB GLU A 337 96.005 239.655 -15.334 1.00 90.98 C ANISOU 3601 CB GLU A 337 13240 7885 13444 -396 578 1182 C ATOM 3602 CG GLU A 337 95.412 240.112 -16.667 1.00 93.58 C ANISOU 3602 CG GLU A 337 13713 8130 13713 -340 558 1347 C ATOM 3603 CD GLU A 337 95.888 239.275 -17.849 1.00 94.55 C ANISOU 3603 CD GLU A 337 13861 8304 13761 -353 623 1427 C ATOM 3604 OE1 GLU A 337 95.934 238.030 -17.725 1.00 93.05 O ANISOU 3604 OE1 GLU A 337 13603 8233 13520 -351 592 1354 O ATOM 3605 OE2 GLU A 337 96.215 239.862 -18.903 1.00 97.00 O ANISOU 3605 OE2 GLU A 337 14264 8520 14071 -352 752 1568 O ATOM 3606 N ASP A 338 93.507 238.436 -13.769 1.00 84.74 N ANISOU 3606 N ASP A 338 12416 7272 12509 -233 269 1006 N ATOM 3607 CA ASP A 338 92.191 237.791 -13.865 1.00 82.68 C ANISOU 3607 CA ASP A 338 12204 7067 12143 -140 128 996 C ATOM 3608 C ASP A 338 91.980 237.000 -12.571 1.00 79.49 C ANISOU 3608 C ASP A 338 11698 6789 11718 -135 116 852 C ATOM 3609 O ASP A 338 92.216 235.790 -12.513 1.00 78.29 O ANISOU 3609 O ASP A 338 11479 6746 11523 -151 119 802 O ATOM 3610 CB ASP A 338 92.102 236.892 -15.099 1.00 82.87 C ANISOU 3610 CB ASP A 338 12260 7128 12100 -121 92 1073 C ATOM 3611 CG ASP A 338 90.697 236.358 -15.345 1.00 82.80 C ANISOU 3611 CG ASP A 338 12275 7182 12002 -16 -54 1066 C ATOM 3612 OD1 ASP A 338 90.038 235.905 -14.384 1.00 81.97 O ANISOU 3612 OD1 ASP A 338 12136 7170 11839 21 -94 950 O ATOM 3613 OD2 ASP A 338 90.250 236.390 -16.513 1.00 84.07 O ANISOU 3613 OD2 ASP A 338 12467 7320 12155 34 -103 1177 O ATOM 3614 N ARG A 339 91.547 237.703 -11.519 1.00 77.87 N ANISOU 3614 N ARG A 339 11468 6567 11552 -111 112 791 N ATOM 3615 CA ARG A 339 91.331 237.052 -10.230 1.00 74.31 C ANISOU 3615 CA ARG A 339 10892 6239 11105 -103 117 671 C ATOM 3616 C ARG A 339 90.205 236.025 -10.291 1.00 70.39 C ANISOU 3616 C ARG A 339 10419 5834 10492 -26 48 647 C ATOM 3617 O ARG A 339 90.240 235.027 -9.562 1.00 69.31 O ANISOU 3617 O ARG A 339 10160 5822 10352 -36 62 569 O ATOM 3618 CB ARG A 339 91.048 238.094 -9.146 1.00 75.45 C ANISOU 3618 CB ARG A 339 10995 6342 11332 -88 128 622 C ATOM 3619 CG ARG A 339 89.660 238.714 -9.217 1.00 76.77 C ANISOU 3619 CG ARG A 339 11274 6453 11442 13 60 649 C ATOM 3620 CD ARG A 339 89.294 239.485 -7.947 1.00 77.98 C ANISOU 3620 CD ARG A 339 11349 6601 11681 32 69 579 C ATOM 3621 NE ARG A 339 89.178 238.644 -6.753 1.00 77.51 N ANISOU 3621 NE ARG A 339 11117 6688 11645 27 70 477 N ATOM 3622 CZ ARG A 339 88.139 237.856 -6.480 1.00 77.80 C ANISOU 3622 CZ ARG A 339 11119 6824 11618 91 29 450 C ATOM 3623 NH1 ARG A 339 87.120 237.771 -7.327 1.00 78.35 N ANISOU 3623 NH1 ARG A 339 11315 6865 11588 172 -3 507 N ATOM 3624 NH2 ARG A 339 88.124 237.141 -5.360 1.00 76.93 N ANISOU 3624 NH2 ARG A 339 10841 6840 11549 75 21 368 N ATOM 3625 N GLU A 340 89.205 236.242 -11.149 1.00 67.88 N ANISOU 3625 N GLU A 340 10238 5469 10085 56 -22 711 N ATOM 3626 CA GLU A 340 88.097 235.295 -11.226 1.00 63.60 C ANISOU 3626 CA GLU A 340 9693 5039 9434 139 -53 678 C ATOM 3627 C GLU A 340 88.576 233.930 -11.703 1.00 60.52 C ANISOU 3627 C GLU A 340 9261 4736 8997 102 -53 664 C ATOM 3628 O GLU A 340 88.184 232.895 -11.148 1.00 59.33 O ANISOU 3628 O GLU A 340 9029 4688 8824 119 -34 598 O ATOM 3629 CB GLU A 340 87.002 235.834 -12.150 1.00 64.20 C ANISOU 3629 CB GLU A 340 9898 5078 9417 243 -116 743 C ATOM 3630 CG GLU A 340 86.012 236.791 -11.480 1.00 64.88 C ANISOU 3630 CG GLU A 340 10007 5125 9519 325 -96 729 C ATOM 3631 CD GLU A 340 86.191 238.248 -11.904 1.00 67.27 C ANISOU 3631 CD GLU A 340 10410 5282 9868 324 -144 803 C ATOM 3632 OE1 GLU A 340 87.207 238.564 -12.567 1.00 69.57 O ANISOU 3632 OE1 GLU A 340 10712 5495 10228 241 -170 873 O ATOM 3633 OE2 GLU A 340 85.309 239.075 -11.573 1.00 67.54 O ANISOU 3633 OE2 GLU A 340 10488 5275 9898 407 -136 803 O ATOM 3634 N THR A 341 89.461 233.910 -12.702 1.00 58.90 N ANISOU 3634 N THR A 341 9088 4484 8808 45 -67 733 N ATOM 3635 CA THR A 341 90.006 232.643 -13.178 1.00 55.50 C ANISOU 3635 CA THR A 341 8612 4126 8348 8 -62 721 C ATOM 3636 C THR A 341 90.847 231.959 -12.106 1.00 51.23 C ANISOU 3636 C THR A 341 7951 3647 7868 -62 12 634 C ATOM 3637 O THR A 341 90.791 230.733 -11.954 1.00 50.07 O ANISOU 3637 O THR A 341 7744 3599 7683 -61 14 581 O ATOM 3638 CB THR A 341 90.835 232.883 -14.443 1.00 57.11 C ANISOU 3638 CB THR A 341 8849 4253 8599 -39 -62 830 C ATOM 3639 OG1 THR A 341 89.960 233.198 -15.534 1.00 58.13 O ANISOU 3639 OG1 THR A 341 9033 4351 8705 35 -160 922 O ATOM 3640 CG2 THR A 341 91.671 231.656 -14.794 1.00 56.77 C ANISOU 3640 CG2 THR A 341 8748 4271 8551 -93 -23 811 C ATOM 3641 N VAL A 342 91.600 232.734 -11.324 1.00 48.55 N ANISOU 3641 N VAL A 342 7530 3287 7629 -116 77 610 N ATOM 3642 CA VAL A 342 92.452 232.125 -10.308 1.00 44.50 C ANISOU 3642 CA VAL A 342 6851 2873 7185 -172 137 524 C ATOM 3643 C VAL A 342 91.604 231.535 -9.188 1.00 41.26 C ANISOU 3643 C VAL A 342 6344 2567 6768 -127 106 447 C ATOM 3644 O VAL A 342 91.854 230.415 -8.720 1.00 39.45 O ANISOU 3644 O VAL A 342 6003 2444 6541 -142 112 391 O ATOM 3645 CB VAL A 342 93.472 233.148 -9.774 1.00 44.34 C ANISOU 3645 CB VAL A 342 6769 2796 7283 -234 209 514 C ATOM 3646 CG1 VAL A 342 94.302 232.525 -8.667 1.00 42.99 C ANISOU 3646 CG1 VAL A 342 6423 2726 7184 -275 251 420 C ATOM 3647 CG2 VAL A 342 94.371 233.636 -10.902 1.00 45.40 C ANISOU 3647 CG2 VAL A 342 6974 2834 7441 -286 267 596 C ATOM 3648 N TYR A 343 90.580 232.273 -8.747 1.00 40.71 N ANISOU 3648 N TYR A 343 6305 2468 6697 -69 74 446 N ATOM 3649 CA TYR A 343 89.686 231.760 -7.716 1.00 38.95 C ANISOU 3649 CA TYR A 343 5972 2344 6484 -27 44 384 C ATOM 3650 C TYR A 343 88.863 230.578 -8.218 1.00 38.84 C ANISOU 3650 C TYR A 343 5973 2397 6387 19 14 385 C ATOM 3651 O TYR A 343 88.484 229.705 -7.424 1.00 37.55 O ANISOU 3651 O TYR A 343 5679 2342 6247 24 -6 331 O ATOM 3652 CB TYR A 343 88.785 232.884 -7.203 1.00 38.21 C ANISOU 3652 CB TYR A 343 5903 2196 6420 26 22 387 C ATOM 3653 CG TYR A 343 89.375 233.600 -6.002 1.00 37.52 C ANISOU 3653 CG TYR A 343 5703 2110 6444 -13 41 334 C ATOM 3654 CD1 TYR A 343 90.267 234.659 -6.158 1.00 38.21 C ANISOU 3654 CD1 TYR A 343 5832 2093 6591 -59 82 355 C ATOM 3655 CD2 TYR A 343 89.054 233.202 -4.708 1.00 36.46 C ANISOU 3655 CD2 TYR A 343 5416 2075 6360 -5 15 263 C ATOM 3656 CE1 TYR A 343 90.815 235.306 -5.061 1.00 38.37 C ANISOU 3656 CE1 TYR A 343 5748 2111 6721 -91 102 298 C ATOM 3657 CE2 TYR A 343 89.595 233.842 -3.604 1.00 36.62 C ANISOU 3657 CE2 TYR A 343 5342 2095 6478 -32 26 210 C ATOM 3658 CZ TYR A 343 90.475 234.894 -3.785 1.00 37.92 C ANISOU 3658 CZ TYR A 343 5549 2155 6702 -74 71 223 C ATOM 3659 OH TYR A 343 91.020 235.525 -2.683 1.00 38.47 O ANISOU 3659 OH TYR A 343 5520 2221 6877 -98 83 160 O ATOM 3660 N ALA A 344 88.582 230.527 -9.524 1.00 39.85 N ANISOU 3660 N ALA A 344 6258 2459 6423 52 4 447 N ATOM 3661 CA ALA A 344 87.899 229.369 -10.087 1.00 39.73 C ANISOU 3661 CA ALA A 344 6258 2501 6338 96 -11 442 C ATOM 3662 C ALA A 344 88.796 228.137 -10.081 1.00 39.25 C ANISOU 3662 C ALA A 344 6111 2518 6283 33 2 405 C ATOM 3663 O ALA A 344 88.329 227.030 -9.794 1.00 39.04 O ANISOU 3663 O ALA A 344 5993 2583 6257 46 -12 363 O ATOM 3664 CB ALA A 344 87.425 229.684 -11.502 1.00 31.82 C ANISOU 3664 CB ALA A 344 5427 1433 5230 161 -21 514 C ATOM 3665 N TRP A 345 90.086 228.301 -10.397 1.00 39.59 N ANISOU 3665 N TRP A 345 6168 2527 6348 -37 29 422 N ATOM 3666 CA TRP A 345 90.991 227.154 -10.388 1.00 38.02 C ANISOU 3666 CA TRP A 345 5881 2401 6164 -91 52 386 C ATOM 3667 C TRP A 345 91.151 226.593 -8.986 1.00 35.42 C ANISOU 3667 C TRP A 345 5366 2181 5910 -108 61 312 C ATOM 3668 O TRP A 345 91.236 225.375 -8.803 1.00 34.09 O ANISOU 3668 O TRP A 345 5116 2097 5740 -115 56 274 O ATOM 3669 CB TRP A 345 92.360 227.544 -10.939 1.00 39.36 C ANISOU 3669 CB TRP A 345 6072 2514 6369 -160 96 420 C ATOM 3670 CG TRP A 345 92.552 227.261 -12.405 1.00 40.17 C ANISOU 3670 CG TRP A 345 6296 2559 6409 -163 74 484 C ATOM 3671 CD1 TRP A 345 92.428 228.151 -13.439 1.00 41.53 C ANISOU 3671 CD1 TRP A 345 6596 2621 6563 -150 41 576 C ATOM 3672 CD2 TRP A 345 92.927 226.011 -12.999 1.00 39.24 C ANISOU 3672 CD2 TRP A 345 6164 2487 6258 -177 73 468 C ATOM 3673 NE1 TRP A 345 92.697 227.529 -14.633 1.00 41.47 N ANISOU 3673 NE1 TRP A 345 6629 2601 6526 -155 17 623 N ATOM 3674 CE2 TRP A 345 93.003 226.216 -14.391 1.00 40.14 C ANISOU 3674 CE2 TRP A 345 6390 2519 6341 -172 36 553 C ATOM 3675 CE3 TRP A 345 93.201 224.738 -12.489 1.00 37.79 C ANISOU 3675 CE3 TRP A 345 5870 2405 6084 -191 93 397 C ATOM 3676 CZ2 TRP A 345 93.340 225.197 -15.279 1.00 39.95 C ANISOU 3676 CZ2 TRP A 345 6366 2507 6308 -179 36 562 C ATOM 3677 CZ3 TRP A 345 93.538 223.726 -13.377 1.00 37.51 C ANISOU 3677 CZ3 TRP A 345 5861 2379 6012 -201 85 398 C ATOM 3678 CH2 TRP A 345 93.605 223.963 -14.754 1.00 38.43 C ANISOU 3678 CH2 TRP A 345 6095 2412 6095 -196 50 475 C ATOM 3679 N PHE A 346 91.189 227.470 -7.981 1.00 35.03 N ANISOU 3679 N PHE A 346 5250 2129 5932 -113 67 292 N ATOM 3680 CA PHE A 346 91.308 227.009 -6.601 1.00 33.17 C ANISOU 3680 CA PHE A 346 4846 1990 5765 -121 59 227 C ATOM 3681 C PHE A 346 90.074 226.225 -6.173 1.00 31.61 C ANISOU 3681 C PHE A 346 4593 1870 5549 -73 6 206 C ATOM 3682 O PHE A 346 90.186 225.185 -5.513 1.00 30.05 O ANISOU 3682 O PHE A 346 4281 1764 5375 -80 -7 166 O ATOM 3683 CB PHE A 346 91.544 228.200 -5.673 1.00 32.91 C ANISOU 3683 CB PHE A 346 4770 1925 5810 -129 70 209 C ATOM 3684 CG PHE A 346 92.988 228.545 -5.488 1.00 33.15 C ANISOU 3684 CG PHE A 346 4756 1931 5906 -187 126 191 C ATOM 3685 CD1 PHE A 346 93.645 229.358 -6.393 1.00 34.33 C ANISOU 3685 CD1 PHE A 346 5005 1980 6060 -222 171 238 C ATOM 3686 CD2 PHE A 346 93.691 228.057 -4.400 1.00 32.47 C ANISOU 3686 CD2 PHE A 346 4528 1923 5886 -205 135 129 C ATOM 3687 CE1 PHE A 346 94.980 229.679 -6.212 1.00 34.71 C ANISOU 3687 CE1 PHE A 346 4996 2006 6186 -278 233 216 C ATOM 3688 CE2 PHE A 346 95.015 228.368 -4.216 1.00 32.85 C ANISOU 3688 CE2 PHE A 346 4527 1950 6005 -252 189 104 C ATOM 3689 CZ PHE A 346 95.665 229.180 -5.123 1.00 33.94 C ANISOU 3689 CZ PHE A 346 4752 1989 6156 -292 243 144 C ATOM 3690 N ALA A 347 88.887 226.701 -6.553 1.00 32.60 N ANISOU 3690 N ALA A 347 4795 1955 5637 -21 -26 234 N ATOM 3691 CA ALA A 347 87.673 225.974 -6.213 1.00 32.04 C ANISOU 3691 CA ALA A 347 4659 1952 5563 21 -77 213 C ATOM 3692 C ALA A 347 87.658 224.602 -6.866 1.00 32.07 C ANISOU 3692 C ALA A 347 4656 2002 5526 16 -83 207 C ATOM 3693 O ALA A 347 87.163 223.635 -6.274 1.00 31.91 O ANISOU 3693 O ALA A 347 4528 2065 5533 21 -117 173 O ATOM 3694 CB ALA A 347 86.441 226.778 -6.633 1.00 32.33 C ANISOU 3694 CB ALA A 347 4781 1929 5574 85 -105 245 C ATOM 3695 N PHE A 348 88.216 224.493 -8.073 1.00 30.86 N ANISOU 3695 N PHE A 348 4622 1792 5313 6 -51 239 N ATOM 3696 CA PHE A 348 88.252 223.207 -8.759 1.00 28.27 C ANISOU 3696 CA PHE A 348 4296 1498 4948 2 -54 228 C ATOM 3697 C PHE A 348 89.215 222.244 -8.081 1.00 26.98 C ANISOU 3697 C PHE A 348 4009 1413 4830 -48 -40 186 C ATOM 3698 O PHE A 348 88.875 221.080 -7.842 1.00 26.44 O ANISOU 3698 O PHE A 348 3857 1413 4775 -45 -65 155 O ATOM 3699 CB PHE A 348 88.635 223.404 -10.221 1.00 28.61 C ANISOU 3699 CB PHE A 348 4512 1449 4909 8 -25 275 C ATOM 3700 CG PHE A 348 88.877 222.128 -10.945 1.00 28.70 C ANISOU 3700 CG PHE A 348 4533 1487 4886 -1 -22 258 C ATOM 3701 CD1 PHE A 348 87.825 221.270 -11.226 1.00 28.57 C ANISOU 3701 CD1 PHE A 348 4492 1503 4860 43 -54 237 C ATOM 3702 CD2 PHE A 348 90.150 221.767 -11.339 1.00 29.24 C ANISOU 3702 CD2 PHE A 348 4619 1545 4945 -56 7 257 C ATOM 3703 CE1 PHE A 348 88.044 220.085 -11.883 1.00 28.69 C ANISOU 3703 CE1 PHE A 348 4513 1536 4853 35 -51 214 C ATOM 3704 CE2 PHE A 348 90.373 220.572 -12.000 1.00 29.32 C ANISOU 3704 CE2 PHE A 348 4638 1575 4926 -63 7 236 C ATOM 3705 CZ PHE A 348 89.316 219.735 -12.270 1.00 29.06 C ANISOU 3705 CZ PHE A 348 4594 1570 4879 -16 -19 212 C ATOM 3706 N SER A 349 90.421 222.709 -7.756 1.00 26.93 N ANISOU 3706 N SER A 349 3984 1394 4855 -92 2 184 N ATOM 3707 CA SER A 349 91.379 221.837 -7.092 1.00 26.16 C ANISOU 3707 CA SER A 349 3767 1367 4805 -126 21 144 C ATOM 3708 C SER A 349 90.845 221.355 -5.755 1.00 25.64 C ANISOU 3708 C SER A 349 3563 1387 4792 -107 -15 107 C ATOM 3709 O SER A 349 91.169 220.244 -5.320 1.00 25.27 O ANISOU 3709 O SER A 349 3428 1406 4767 -114 -17 79 O ATOM 3710 CB SER A 349 92.698 222.572 -6.890 1.00 27.11 C ANISOU 3710 CB SER A 349 3878 1455 4967 -168 73 142 C ATOM 3711 OG SER A 349 92.493 223.730 -6.103 1.00 28.08 O ANISOU 3711 OG SER A 349 3982 1555 5133 -160 68 142 O ATOM 3712 N HIS A 350 90.023 222.174 -5.092 1.00 26.32 N ANISOU 3712 N HIS A 350 3634 1467 4898 -81 -43 110 N ATOM 3713 CA HIS A 350 89.460 221.784 -3.804 1.00 25.55 C ANISOU 3713 CA HIS A 350 3416 1443 4848 -64 -79 80 C ATOM 3714 C HIS A 350 88.445 220.668 -3.970 1.00 25.37 C ANISOU 3714 C HIS A 350 3362 1466 4811 -43 -119 75 C ATOM 3715 O HIS A 350 88.522 219.634 -3.297 1.00 24.61 O ANISOU 3715 O HIS A 350 3172 1436 4743 -47 -128 52 O ATOM 3716 CB HIS A 350 88.808 222.991 -3.139 1.00 25.66 C ANISOU 3716 CB HIS A 350 3432 1432 4888 -42 -100 82 C ATOM 3717 CG HIS A 350 89.768 224.087 -2.817 1.00 26.19 C ANISOU 3717 CG HIS A 350 3511 1451 4987 -64 -64 77 C ATOM 3718 ND1 HIS A 350 89.363 225.360 -2.480 1.00 26.50 N ANISOU 3718 ND1 HIS A 350 3580 1439 5049 -48 -72 82 N ATOM 3719 CD2 HIS A 350 91.121 224.099 -2.785 1.00 26.08 C ANISOU 3719 CD2 HIS A 350 3480 1430 4998 -100 -19 64 C ATOM 3720 CE1 HIS A 350 90.426 226.108 -2.247 1.00 27.33 C ANISOU 3720 CE1 HIS A 350 3684 1505 5194 -77 -34 71 C ATOM 3721 NE2 HIS A 350 91.506 225.367 -2.427 1.00 26.79 N ANISOU 3721 NE2 HIS A 350 3585 1464 5129 -110 -1 59 N ATOM 3722 N TRP A 351 87.493 220.855 -4.880 1.00 25.89 N ANISOU 3722 N TRP A 351 3508 1492 4838 -18 -143 96 N ATOM 3723 CA TRP A 351 86.525 219.803 -5.141 1.00 25.54 C ANISOU 3723 CA TRP A 351 3430 1482 4791 -1 -184 85 C ATOM 3724 C TRP A 351 87.233 218.529 -5.566 1.00 26.06 C ANISOU 3724 C TRP A 351 3477 1577 4849 -26 -165 70 C ATOM 3725 O TRP A 351 86.905 217.435 -5.091 1.00 24.72 O ANISOU 3725 O TRP A 351 3217 1463 4712 -27 -185 48 O ATOM 3726 CB TRP A 351 85.546 220.278 -6.216 1.00 24.87 C ANISOU 3726 CB TRP A 351 3448 1338 4665 37 -209 107 C ATOM 3727 CG TRP A 351 84.640 219.220 -6.700 1.00 23.78 C ANISOU 3727 CG TRP A 351 3284 1222 4529 54 -252 89 C ATOM 3728 CD1 TRP A 351 83.401 218.917 -6.216 1.00 23.26 C ANISOU 3728 CD1 TRP A 351 3142 1189 4506 76 -306 70 C ATOM 3729 CD2 TRP A 351 84.887 218.312 -7.777 1.00 23.21 C ANISOU 3729 CD2 TRP A 351 3261 1136 4423 48 -245 83 C ATOM 3730 NE1 TRP A 351 82.862 217.874 -6.928 1.00 22.97 N ANISOU 3730 NE1 TRP A 351 3097 1159 4471 83 -337 49 N ATOM 3731 CE2 TRP A 351 83.757 217.481 -7.890 1.00 23.05 C ANISOU 3731 CE2 TRP A 351 3185 1141 4433 68 -301 55 C ATOM 3732 CE3 TRP A 351 85.959 218.116 -8.651 1.00 23.28 C ANISOU 3732 CE3 TRP A 351 3354 1108 4381 27 -197 93 C ATOM 3733 CZ2 TRP A 351 83.668 216.466 -8.843 1.00 22.99 C ANISOU 3733 CZ2 TRP A 351 3200 1125 4411 70 -313 33 C ATOM 3734 CZ3 TRP A 351 85.867 217.110 -9.595 1.00 23.31 C ANISOU 3734 CZ3 TRP A 351 3389 1104 4363 31 -204 75 C ATOM 3735 CH2 TRP A 351 84.732 216.299 -9.682 1.00 23.17 C ANISOU 3735 CH2 TRP A 351 3311 1112 4379 54 -263 43 C ATOM 3736 N LEU A 352 88.276 218.670 -6.384 1.00 28.50 N ANISOU 3736 N LEU A 352 3865 1844 5120 -48 -121 83 N ATOM 3737 CA LEU A 352 89.006 217.512 -6.875 1.00 26.73 C ANISOU 3737 CA LEU A 352 3631 1639 4887 -70 -101 66 C ATOM 3738 C LEU A 352 89.666 216.740 -5.744 1.00 25.68 C ANISOU 3738 C LEU A 352 3371 1576 4809 -86 -91 40 C ATOM 3739 O LEU A 352 89.869 215.527 -5.865 1.00 25.60 O ANISOU 3739 O LEU A 352 3320 1598 4811 -92 -91 21 O ATOM 3740 CB LEU A 352 90.049 217.963 -7.894 1.00 26.47 C ANISOU 3740 CB LEU A 352 3710 1540 4805 -93 -52 86 C ATOM 3741 CG LEU A 352 90.705 216.826 -8.652 1.00 25.84 C ANISOU 3741 CG LEU A 352 3645 1466 4707 -112 -34 68 C ATOM 3742 CD1 LEU A 352 89.644 215.854 -9.127 1.00 25.09 C ANISOU 3742 CD1 LEU A 352 3547 1384 4603 -87 -77 50 C ATOM 3743 CD2 LEU A 352 91.475 217.402 -9.812 1.00 26.48 C ANISOU 3743 CD2 LEU A 352 3863 1468 4732 -131 6 95 C ATOM 3744 N VAL A 353 90.017 217.418 -4.646 1.00 25.24 N ANISOU 3744 N VAL A 353 3260 1540 4791 -87 -82 37 N ATOM 3745 CA VAL A 353 90.600 216.717 -3.503 1.00 24.56 C ANISOU 3745 CA VAL A 353 3064 1514 4754 -91 -75 14 C ATOM 3746 C VAL A 353 89.561 215.820 -2.847 1.00 23.61 C ANISOU 3746 C VAL A 353 2869 1442 4659 -71 -113 7 C ATOM 3747 O VAL A 353 89.822 214.648 -2.547 1.00 22.38 O ANISOU 3747 O VAL A 353 2654 1323 4525 -73 -109 -6 O ATOM 3748 CB VAL A 353 91.192 217.720 -2.495 1.00 24.48 C ANISOU 3748 CB VAL A 353 3020 1504 4776 -93 -60 7 C ATOM 3749 CG1 VAL A 353 91.447 217.036 -1.163 1.00 23.76 C ANISOU 3749 CG1 VAL A 353 2824 1472 4730 -83 -68 -15 C ATOM 3750 CG2 VAL A 353 92.485 218.327 -3.040 1.00 25.17 C ANISOU 3750 CG2 VAL A 353 3154 1548 4861 -121 -12 6 C ATOM 3751 N TYR A 354 88.367 216.366 -2.599 1.00 24.72 N ANISOU 3751 N TYR A 354 3011 1578 4802 -51 -148 15 N ATOM 3752 CA TYR A 354 87.288 215.549 -2.055 1.00 25.02 C ANISOU 3752 CA TYR A 354 2981 1653 4872 -37 -181 9 C ATOM 3753 C TYR A 354 86.821 214.505 -3.056 1.00 24.61 C ANISOU 3753 C TYR A 354 2944 1594 4812 -39 -196 2 C ATOM 3754 O TYR A 354 86.441 213.400 -2.658 1.00 24.70 O ANISOU 3754 O TYR A 354 2887 1637 4861 -38 -204 -8 O ATOM 3755 CB TYR A 354 86.120 216.435 -1.610 1.00 25.51 C ANISOU 3755 CB TYR A 354 3041 1706 4945 -16 -213 14 C ATOM 3756 CG TYR A 354 86.510 217.435 -0.549 1.00 20.62 C ANISOU 3756 CG TYR A 354 2404 1091 4341 -12 -202 12 C ATOM 3757 CD1 TYR A 354 86.933 217.018 0.706 1.00 20.26 C ANISOU 3757 CD1 TYR A 354 2284 1086 4327 -12 -189 1 C ATOM 3758 CD2 TYR A 354 86.459 218.798 -0.804 1.00 21.07 C ANISOU 3758 CD2 TYR A 354 2523 1101 4381 -5 -204 21 C ATOM 3759 CE1 TYR A 354 87.296 217.931 1.679 1.00 20.31 C ANISOU 3759 CE1 TYR A 354 2277 1091 4348 -6 -184 -9 C ATOM 3760 CE2 TYR A 354 86.815 219.721 0.163 1.00 21.15 C ANISOU 3760 CE2 TYR A 354 2514 1108 4413 -1 -196 11 C ATOM 3761 CZ TYR A 354 87.235 219.284 1.400 1.00 20.75 C ANISOU 3761 CZ TYR A 354 2387 1103 4395 -2 -188 -7 C ATOM 3762 OH TYR A 354 87.598 220.213 2.350 1.00 20.89 O ANISOU 3762 OH TYR A 354 2389 1113 4435 4 -185 -25 O ATOM 3763 N ALA A 355 86.877 214.817 -4.351 1.00 24.43 N ANISOU 3763 N ALA A 355 3015 1524 4743 -42 -197 8 N ATOM 3764 CA ALA A 355 86.475 213.834 -5.350 1.00 24.65 C ANISOU 3764 CA ALA A 355 3064 1540 4763 -42 -215 -7 C ATOM 3765 C ALA A 355 87.360 212.597 -5.297 1.00 24.69 C ANISOU 3765 C ALA A 355 3024 1572 4787 -60 -188 -24 C ATOM 3766 O ALA A 355 86.890 211.487 -5.574 1.00 24.91 O ANISOU 3766 O ALA A 355 3017 1608 4841 -60 -207 -44 O ATOM 3767 CB ALA A 355 86.517 214.450 -6.743 1.00 21.58 C ANISOU 3767 CB ALA A 355 2803 1085 4309 -37 -213 3 C ATOM 3768 N ASN A 356 88.636 212.768 -4.932 1.00 25.30 N ANISOU 3768 N ASN A 356 3096 1658 4858 -75 -146 -20 N ATOM 3769 CA ASN A 356 89.549 211.634 -4.828 1.00 23.89 C ANISOU 3769 CA ASN A 356 2873 1502 4702 -87 -120 -37 C ATOM 3770 C ASN A 356 89.056 210.630 -3.795 1.00 22.83 C ANISOU 3770 C ASN A 356 2637 1411 4626 -76 -133 -43 C ATOM 3771 O ASN A 356 89.157 209.415 -4.001 1.00 22.75 O ANISOU 3771 O ASN A 356 2597 1407 4641 -80 -130 -58 O ATOM 3772 CB ASN A 356 90.943 212.136 -4.457 1.00 24.87 C ANISOU 3772 CB ASN A 356 2997 1629 4823 -99 -77 -35 C ATOM 3773 CG ASN A 356 91.891 211.018 -4.047 1.00 25.79 C ANISOU 3773 CG ASN A 356 3051 1775 4975 -103 -54 -53 C ATOM 3774 OD1 ASN A 356 92.553 210.404 -4.893 1.00 26.54 O ANISOU 3774 OD1 ASN A 356 3173 1852 5058 -116 -34 -68 O ATOM 3775 ND2 ASN A 356 91.980 210.767 -2.737 1.00 24.61 N ANISOU 3775 ND2 ASN A 356 2822 1663 4866 -91 -56 -52 N ATOM 3776 N SER A 357 88.500 211.119 -2.686 1.00 22.23 N ANISOU 3776 N SER A 357 2516 1358 4573 -64 -145 -30 N ATOM 3777 CA SER A 357 87.955 210.217 -1.685 1.00 22.21 C ANISOU 3777 CA SER A 357 2432 1385 4623 -55 -149 -28 C ATOM 3778 C SER A 357 86.716 209.502 -2.200 1.00 22.76 C ANISOU 3778 C SER A 357 2485 1443 4720 -53 -179 -38 C ATOM 3779 O SER A 357 86.467 208.349 -1.830 1.00 23.14 O ANISOU 3779 O SER A 357 2476 1500 4816 -54 -172 -42 O ATOM 3780 CB SER A 357 87.668 210.993 -0.407 1.00 22.76 C ANISOU 3780 CB SER A 357 2470 1475 4704 -43 -150 -14 C ATOM 3781 OG SER A 357 88.873 211.547 0.095 1.00 23.13 O ANISOU 3781 OG SER A 357 2523 1529 4737 -45 -127 -15 O ATOM 3782 N ALA A 358 85.929 210.154 -3.060 1.00 23.21 N ANISOU 3782 N ALA A 358 2592 1473 4752 -50 -211 -43 N ATOM 3783 CA ALA A 358 84.838 209.431 -3.711 1.00 23.95 C ANISOU 3783 CA ALA A 358 2671 1551 4879 -48 -245 -63 C ATOM 3784 C ALA A 358 85.361 208.429 -4.731 1.00 24.02 C ANISOU 3784 C ALA A 358 2703 1540 4883 -59 -241 -89 C ATOM 3785 O ALA A 358 84.725 207.395 -4.969 1.00 24.22 O ANISOU 3785 O ALA A 358 2686 1559 4960 -61 -257 -113 O ATOM 3786 CB ALA A 358 83.866 210.402 -4.378 1.00 24.30 C ANISOU 3786 CB ALA A 358 2767 1566 4899 -35 -289 -66 C ATOM 3787 N ALA A 359 86.520 208.706 -5.329 1.00 23.76 N ANISOU 3787 N ALA A 359 2735 1495 4796 -68 -215 -87 N ATOM 3788 CA ALA A 359 87.008 207.847 -6.396 1.00 24.09 C ANISOU 3788 CA ALA A 359 2812 1513 4826 -79 -210 -116 C ATOM 3789 C ALA A 359 87.528 206.518 -5.869 1.00 24.76 C ANISOU 3789 C ALA A 359 2822 1618 4967 -85 -186 -128 C ATOM 3790 O ALA A 359 87.292 205.481 -6.489 1.00 26.12 O ANISOU 3790 O ALA A 359 2983 1772 5169 -89 -197 -161 O ATOM 3791 CB ALA A 359 88.093 208.559 -7.198 1.00 24.01 C ANISOU 3791 CB ALA A 359 2900 1477 4745 -88 -181 -111 C ATOM 3792 N ASN A 360 88.229 206.512 -4.735 1.00 23.91 N ANISOU 3792 N ASN A 360 2667 1542 4876 -83 -154 -105 N ATOM 3793 CA ASN A 360 88.890 205.275 -4.322 1.00 23.76 C ANISOU 3793 CA ASN A 360 2594 1531 4902 -84 -128 -113 C ATOM 3794 C ASN A 360 87.926 204.113 -4.140 1.00 23.24 C ANISOU 3794 C ASN A 360 2467 1457 4908 -82 -142 -125 C ATOM 3795 O ASN A 360 88.201 203.025 -4.669 1.00 23.39 O ANISOU 3795 O ASN A 360 2475 1455 4957 -88 -136 -152 O ATOM 3796 CB ASN A 360 89.729 205.528 -3.066 1.00 24.97 C ANISOU 3796 CB ASN A 360 2712 1714 5061 -77 -99 -88 C ATOM 3797 CG ASN A 360 90.948 206.368 -3.354 1.00 26.65 C ANISOU 3797 CG ASN A 360 2973 1928 5226 -84 -77 -89 C ATOM 3798 OD1 ASN A 360 91.451 206.397 -4.483 1.00 27.02 O ANISOU 3798 OD1 ASN A 360 3075 1950 5240 -96 -70 -108 O ATOM 3799 ND2 ASN A 360 91.424 207.074 -2.339 1.00 28.28 N ANISOU 3799 ND2 ASN A 360 3159 2156 5429 -77 -66 -72 N ATOM 3800 N PRO A 361 86.818 204.240 -3.426 1.00 23.51 N ANISOU 3800 N PRO A 361 2456 1498 4978 -76 -155 -109 N ATOM 3801 CA PRO A 361 85.905 203.087 -3.337 1.00 23.89 C ANISOU 3801 CA PRO A 361 2444 1527 5107 -78 -160 -124 C ATOM 3802 C PRO A 361 85.455 202.571 -4.700 1.00 23.94 C ANISOU 3802 C PRO A 361 2472 1500 5126 -86 -194 -174 C ATOM 3803 O PRO A 361 85.276 201.357 -4.851 1.00 24.53 O ANISOU 3803 O PRO A 361 2503 1550 5267 -91 -189 -199 O ATOM 3804 CB PRO A 361 84.718 203.648 -2.509 1.00 24.17 C ANISOU 3804 CB PRO A 361 2441 1572 5169 -70 -170 -102 C ATOM 3805 CG PRO A 361 85.334 204.708 -1.666 1.00 23.96 C ANISOU 3805 CG PRO A 361 2437 1577 5089 -62 -154 -68 C ATOM 3806 CD PRO A 361 86.441 205.328 -2.490 1.00 23.88 C ANISOU 3806 CD PRO A 361 2497 1569 5008 -66 -157 -78 C ATOM 3807 N ILE A 362 85.276 203.451 -5.683 1.00 23.76 N ANISOU 3807 N ILE A 362 2518 1467 5043 -85 -228 -191 N ATOM 3808 CA ILE A 362 84.943 203.007 -7.025 1.00 24.32 C ANISOU 3808 CA ILE A 362 2625 1502 5112 -90 -264 -244 C ATOM 3809 C ILE A 362 86.103 202.236 -7.655 1.00 24.92 C ANISOU 3809 C ILE A 362 2731 1565 5173 -99 -239 -269 C ATOM 3810 O ILE A 362 85.891 201.304 -8.450 1.00 25.39 O ANISOU 3810 O ILE A 362 2785 1594 5268 -105 -257 -322 O ATOM 3811 CB ILE A 362 84.522 204.214 -7.881 1.00 24.08 C ANISOU 3811 CB ILE A 362 2681 1458 5011 -82 -303 -250 C ATOM 3812 CG1 ILE A 362 83.189 204.780 -7.356 1.00 24.80 C ANISOU 3812 CG1 ILE A 362 2729 1555 5138 -70 -338 -240 C ATOM 3813 CG2 ILE A 362 84.460 203.852 -9.363 1.00 23.82 C ANISOU 3813 CG2 ILE A 362 2715 1384 4952 -83 -335 -308 C ATOM 3814 CD1 ILE A 362 82.909 206.232 -7.735 1.00 25.09 C ANISOU 3814 CD1 ILE A 362 2845 1584 5103 -56 -365 -222 C ATOM 3815 N ILE A 363 87.342 202.602 -7.314 1.00 25.17 N ANISOU 3815 N ILE A 363 2790 1616 5159 -101 -198 -239 N ATOM 3816 CA ILE A 363 88.508 201.866 -7.798 1.00 25.72 C ANISOU 3816 CA ILE A 363 2878 1673 5222 -109 -170 -263 C ATOM 3817 C ILE A 363 88.529 200.459 -7.213 1.00 27.45 C ANISOU 3817 C ILE A 363 3013 1888 5530 -108 -154 -273 C ATOM 3818 O ILE A 363 88.838 199.487 -7.910 1.00 28.52 O ANISOU 3818 O ILE A 363 3149 1996 5693 -114 -153 -318 O ATOM 3819 CB ILE A 363 89.801 202.641 -7.463 1.00 24.01 C ANISOU 3819 CB ILE A 363 2696 1477 4949 -110 -130 -231 C ATOM 3820 CG1 ILE A 363 89.799 204.009 -8.146 1.00 23.15 C ANISOU 3820 CG1 ILE A 363 2682 1358 4757 -113 -138 -220 C ATOM 3821 CG2 ILE A 363 91.034 201.843 -7.858 1.00 23.82 C ANISOU 3821 CG2 ILE A 363 2679 1442 4931 -116 -98 -258 C ATOM 3822 CD1 ILE A 363 90.947 204.905 -7.723 1.00 22.48 C ANISOU 3822 CD1 ILE A 363 2621 1289 4631 -117 -98 -190 C ATOM 3823 N TYR A 364 88.196 200.327 -5.923 1.00 27.91 N ANISOU 3823 N TYR A 364 3004 1965 5635 -101 -138 -233 N ATOM 3824 CA TYR A 364 88.144 199.012 -5.293 1.00 29.19 C ANISOU 3824 CA TYR A 364 3096 2110 5884 -100 -116 -233 C ATOM 3825 C TYR A 364 87.016 198.169 -5.860 1.00 31.63 C ANISOU 3825 C TYR A 364 3370 2382 6267 -107 -143 -276 C ATOM 3826 O TYR A 364 87.089 196.935 -5.839 1.00 32.48 O ANISOU 3826 O TYR A 364 3435 2457 6449 -111 -127 -297 O ATOM 3827 CB TYR A 364 87.951 199.142 -3.784 1.00 28.39 C ANISOU 3827 CB TYR A 364 2948 2030 5808 -91 -90 -177 C ATOM 3828 CG TYR A 364 88.921 200.061 -3.081 1.00 27.49 C ANISOU 3828 CG TYR A 364 2861 1955 5631 -82 -72 -141 C ATOM 3829 CD1 TYR A 364 90.210 200.262 -3.560 1.00 27.39 C ANISOU 3829 CD1 TYR A 364 2887 1948 5572 -83 -61 -155 C ATOM 3830 CD2 TYR A 364 88.535 200.732 -1.932 1.00 27.72 C ANISOU 3830 CD2 TYR A 364 2872 2009 5653 -73 -64 -99 C ATOM 3831 CE1 TYR A 364 91.088 201.106 -2.911 1.00 27.88 C ANISOU 3831 CE1 TYR A 364 2964 2039 5590 -77 -46 -130 C ATOM 3832 CE2 TYR A 364 89.398 201.577 -1.278 1.00 28.15 C ANISOU 3832 CE2 TYR A 364 2947 2093 5657 -66 -53 -76 C ATOM 3833 CZ TYR A 364 90.676 201.765 -1.766 1.00 28.24 C ANISOU 3833 CZ TYR A 364 2990 2109 5630 -68 -45 -93 C ATOM 3834 OH TYR A 364 91.532 202.621 -1.097 1.00 28.42 O ANISOU 3834 OH TYR A 364 3024 2157 5616 -61 -34 -76 O ATOM 3835 N ASN A 365 85.945 198.806 -6.324 1.00 33.14 N ANISOU 3835 N ASN A 365 3572 2572 6449 -108 -183 -293 N ATOM 3836 CA ASN A 365 84.839 198.022 -6.849 1.00 35.06 C ANISOU 3836 CA ASN A 365 3770 2777 6772 -114 -214 -344 C ATOM 3837 C ASN A 365 85.199 197.393 -8.189 1.00 36.87 C ANISOU 3837 C ASN A 365 4037 2976 6996 -121 -238 -416 C ATOM 3838 O ASN A 365 84.816 196.251 -8.468 1.00 37.76 O ANISOU 3838 O ASN A 365 4100 3052 7197 -128 -243 -464 O ATOM 3839 CB ASN A 365 83.587 198.886 -6.977 1.00 34.02 C ANISOU 3839 CB ASN A 365 3637 2651 6637 -110 -257 -349 C ATOM 3840 CG ASN A 365 82.359 198.061 -7.249 1.00 33.66 C ANISOU 3840 CG ASN A 365 3522 2569 6698 -116 -285 -402 C ATOM 3841 OD1 ASN A 365 81.793 197.457 -6.337 1.00 33.81 O ANISOU 3841 OD1 ASN A 365 3464 2575 6808 -119 -253 -382 O ATOM 3842 ND2 ASN A 365 81.960 197.991 -8.513 1.00 33.56 N ANISOU 3842 ND2 ASN A 365 3539 2534 6680 -117 -341 -476 N ATOM 3843 N PHE A 366 85.961 198.108 -9.017 1.00 37.90 N ANISOU 3843 N PHE A 366 4257 3115 7026 -120 -247 -426 N ATOM 3844 CA PHE A 366 86.235 197.659 -10.375 1.00 37.65 C ANISOU 3844 CA PHE A 366 4278 3053 6974 -125 -272 -500 C ATOM 3845 C PHE A 366 87.524 196.850 -10.499 1.00 37.00 C ANISOU 3845 C PHE A 366 4203 2962 6895 -129 -231 -512 C ATOM 3846 O PHE A 366 87.652 196.064 -11.445 1.00 38.49 O ANISOU 3846 O PHE A 366 4405 3119 7102 -133 -246 -584 O ATOM 3847 CB PHE A 366 86.268 198.868 -11.325 1.00 38.22 C ANISOU 3847 CB PHE A 366 4461 3127 6934 -120 -300 -508 C ATOM 3848 CG PHE A 366 84.908 199.457 -11.608 1.00 39.22 C ANISOU 3848 CG PHE A 366 4589 3246 7065 -111 -358 -527 C ATOM 3849 CD1 PHE A 366 83.846 198.637 -11.964 1.00 41.15 C ANISOU 3849 CD1 PHE A 366 4772 3467 7396 -111 -404 -595 C ATOM 3850 CD2 PHE A 366 84.683 200.824 -11.514 1.00 39.02 C ANISOU 3850 CD2 PHE A 366 4624 3237 6967 -101 -368 -481 C ATOM 3851 CE1 PHE A 366 82.588 199.167 -12.222 1.00 41.89 C ANISOU 3851 CE1 PHE A 366 4858 3555 7503 -100 -463 -621 C ATOM 3852 CE2 PHE A 366 83.424 201.359 -11.772 1.00 40.06 C ANISOU 3852 CE2 PHE A 366 4755 3359 7108 -87 -426 -501 C ATOM 3853 CZ PHE A 366 82.378 200.526 -12.126 1.00 41.39 C ANISOU 3853 CZ PHE A 366 4857 3508 7363 -86 -476 -573 C ATOM 3854 N LEU A 367 88.473 196.996 -9.573 1.00 36.17 N ANISOU 3854 N LEU A 367 4084 2882 6776 -126 -183 -453 N ATOM 3855 CA LEU A 367 89.754 196.313 -9.689 1.00 35.76 C ANISOU 3855 CA LEU A 367 4038 2822 6728 -126 -147 -467 C ATOM 3856 C LEU A 367 89.991 195.244 -8.625 1.00 34.40 C ANISOU 3856 C LEU A 367 3782 2641 6647 -122 -115 -442 C ATOM 3857 O LEU A 367 91.063 194.623 -8.624 1.00 34.67 O ANISOU 3857 O LEU A 367 3814 2666 6694 -119 -88 -452 O ATOM 3858 CB LEU A 367 90.894 197.336 -9.664 1.00 35.74 C ANISOU 3858 CB LEU A 367 4098 2848 6633 -125 -118 -432 C ATOM 3859 CG LEU A 367 90.881 198.320 -10.839 1.00 36.87 C ANISOU 3859 CG LEU A 367 4346 2982 6680 -131 -137 -455 C ATOM 3860 CD1 LEU A 367 92.120 199.182 -10.837 1.00 23.51 C ANISOU 3860 CD1 LEU A 367 2710 1305 4916 -134 -96 -425 C ATOM 3861 CD2 LEU A 367 90.766 197.564 -12.140 1.00 38.33 C ANISOU 3861 CD2 LEU A 367 4570 3127 6868 -134 -159 -538 C ATOM 3862 N SER A 368 89.024 194.989 -7.743 1.00 32.76 N ANISOU 3862 N SER A 368 3511 2430 6507 -120 -116 -411 N ATOM 3863 CA SER A 368 89.159 193.963 -6.710 1.00 32.32 C ANISOU 3863 CA SER A 368 3390 2353 6538 -117 -80 -381 C ATOM 3864 C SER A 368 87.834 193.212 -6.614 1.00 32.81 C ANISOU 3864 C SER A 368 3390 2375 6702 -125 -90 -400 C ATOM 3865 O SER A 368 86.808 193.795 -6.233 1.00 33.16 O ANISOU 3865 O SER A 368 3415 2432 6751 -126 -103 -378 O ATOM 3866 CB SER A 368 89.538 194.579 -5.362 1.00 31.48 C ANISOU 3866 CB SER A 368 3276 2283 6401 -105 -50 -303 C ATOM 3867 OG SER A 368 89.419 193.641 -4.304 1.00 25.13 O ANISOU 3867 OG SER A 368 2420 1451 5678 -101 -16 -267 O ATOM 3868 N GLY A 369 87.853 191.913 -6.940 1.00 32.43 N ANISOU 3868 N GLY A 369 3306 2273 6743 -131 -83 -445 N ATOM 3869 CA GLY A 369 86.628 191.132 -6.873 1.00 32.83 C ANISOU 3869 CA GLY A 369 3290 2276 6908 -143 -87 -471 C ATOM 3870 C GLY A 369 86.142 190.891 -5.457 1.00 32.63 C ANISOU 3870 C GLY A 369 3216 2238 6945 -141 -40 -396 C ATOM 3871 O GLY A 369 84.945 190.688 -5.236 1.00 33.11 O ANISOU 3871 O GLY A 369 3226 2272 7084 -151 -38 -401 O ATOM 3872 N LYS A 370 87.057 190.904 -4.481 1.00 32.92 N ANISOU 3872 N LYS A 370 3269 2289 6950 -130 1 -329 N ATOM 3873 CA LYS A 370 86.653 190.736 -3.088 1.00 32.71 C ANISOU 3873 CA LYS A 370 3213 2249 6966 -126 49 -254 C ATOM 3874 C LYS A 370 85.923 191.970 -2.571 1.00 31.68 C ANISOU 3874 C LYS A 370 3088 2170 6779 -122 39 -216 C ATOM 3875 O LYS A 370 84.927 191.849 -1.851 1.00 27.34 O ANISOU 3875 O LYS A 370 2498 1599 6290 -127 65 -186 O ATOM 3876 CB LYS A 370 87.867 190.425 -2.222 1.00 32.31 C ANISOU 3876 CB LYS A 370 3188 2198 6891 -111 85 -199 C ATOM 3877 CG LYS A 370 88.225 188.952 -2.143 1.00 28.61 C ANISOU 3877 CG LYS A 370 2697 1653 6520 -113 117 -206 C ATOM 3878 CD LYS A 370 89.335 188.757 -1.137 1.00 31.95 C ANISOU 3878 CD LYS A 370 3151 2075 6913 -94 150 -143 C ATOM 3879 CE LYS A 370 89.766 187.314 -1.013 1.00 32.88 C ANISOU 3879 CE LYS A 370 3257 2110 7125 -92 181 -143 C ATOM 3880 NZ LYS A 370 90.877 187.222 -0.017 1.00 32.73 N ANISOU 3880 NZ LYS A 370 3280 2092 7066 -66 203 -80 N ATOM 3881 N PHE A 371 86.404 193.167 -2.917 1.00 31.09 N ANISOU 3881 N PHE A 371 3063 2157 6593 -114 6 -218 N ATOM 3882 CA PHE A 371 85.636 194.363 -2.588 1.00 31.36 C ANISOU 3882 CA PHE A 371 3102 2232 6580 -111 -11 -194 C ATOM 3883 C PHE A 371 84.337 194.413 -3.377 1.00 34.40 C ANISOU 3883 C PHE A 371 3457 2599 7013 -122 -48 -246 C ATOM 3884 O PHE A 371 83.295 194.801 -2.839 1.00 34.96 O ANISOU 3884 O PHE A 371 3496 2673 7115 -123 -45 -226 O ATOM 3885 CB PHE A 371 86.452 195.630 -2.843 1.00 29.14 C ANISOU 3885 CB PHE A 371 2884 2011 6178 -102 -35 -187 C ATOM 3886 CG PHE A 371 87.363 196.011 -1.709 1.00 27.45 C ANISOU 3886 CG PHE A 371 2688 1827 5916 -89 -3 -128 C ATOM 3887 CD1 PHE A 371 86.853 196.307 -0.453 1.00 26.65 C ANISOU 3887 CD1 PHE A 371 2569 1735 5823 -82 23 -74 C ATOM 3888 CD2 PHE A 371 88.730 196.098 -1.904 1.00 26.84 C ANISOU 3888 CD2 PHE A 371 2647 1766 5786 -83 -1 -133 C ATOM 3889 CE1 PHE A 371 87.692 196.661 0.581 1.00 25.71 C ANISOU 3889 CE1 PHE A 371 2471 1640 5657 -68 46 -28 C ATOM 3890 CE2 PHE A 371 89.573 196.456 -0.866 1.00 26.08 C ANISOU 3890 CE2 PHE A 371 2564 1694 5652 -69 21 -89 C ATOM 3891 CZ PHE A 371 89.050 196.735 0.374 1.00 25.55 C ANISOU 3891 CZ PHE A 371 2483 1635 5589 -62 41 -38 C ATOM 3892 N ARG A 372 84.371 194.008 -4.649 1.00 36.60 N ANISOU 3892 N ARG A 372 3746 2856 7305 -130 -86 -318 N ATOM 3893 CA ARG A 372 83.171 194.125 -5.473 1.00 38.67 C ANISOU 3893 CA ARG A 372 3984 3101 7607 -138 -134 -378 C ATOM 3894 C ARG A 372 82.056 193.232 -4.949 1.00 41.66 C ANISOU 3894 C ARG A 372 4278 3429 8124 -149 -108 -385 C ATOM 3895 O ARG A 372 80.884 193.621 -4.964 1.00 42.55 O ANISOU 3895 O ARG A 372 4354 3538 8273 -151 -130 -402 O ATOM 3896 CB ARG A 372 83.492 193.792 -6.931 1.00 38.42 C ANISOU 3896 CB ARG A 372 3987 3053 7559 -143 -180 -462 C ATOM 3897 CG ARG A 372 82.288 193.802 -7.865 1.00 38.43 C ANISOU 3897 CG ARG A 372 3964 3032 7605 -149 -240 -541 C ATOM 3898 CD ARG A 372 82.671 193.633 -9.333 1.00 38.34 C ANISOU 3898 CD ARG A 372 4006 3010 7551 -150 -290 -627 C ATOM 3899 NE ARG A 372 83.532 192.478 -9.570 1.00 38.96 N ANISOU 3899 NE ARG A 372 4076 3055 7671 -156 -262 -656 N ATOM 3900 CZ ARG A 372 84.828 192.559 -9.863 1.00 38.93 C ANISOU 3900 CZ ARG A 372 4136 3067 7586 -151 -245 -646 C ATOM 3901 NH1 ARG A 372 85.418 193.747 -9.967 1.00 37.77 N ANISOU 3901 NH1 ARG A 372 4068 2966 7315 -143 -249 -607 N ATOM 3902 NH2 ARG A 372 85.538 191.454 -10.064 1.00 39.86 N ANISOU 3902 NH2 ARG A 372 4239 3151 7755 -155 -222 -679 N ATOM 3903 N GLU A 373 82.406 192.052 -4.430 1.00 43.51 N ANISOU 3903 N GLU A 373 4479 3616 8438 -155 -55 -368 N ATOM 3904 CA GLU A 373 81.404 191.163 -3.850 1.00 46.08 C ANISOU 3904 CA GLU A 373 4727 3880 8902 -168 -14 -366 C ATOM 3905 C GLU A 373 80.914 191.671 -2.498 1.00 45.43 C ANISOU 3905 C GLU A 373 4630 3812 8817 -163 35 -283 C ATOM 3906 O GLU A 373 79.706 191.719 -2.249 1.00 45.38 O ANISOU 3906 O GLU A 373 4571 3785 8887 -170 44 -291 O ATOM 3907 CB GLU A 373 81.969 189.748 -3.728 1.00 49.34 C ANISOU 3907 CB GLU A 373 5119 4228 9401 -177 31 -369 C ATOM 3908 CG GLU A 373 82.188 189.050 -5.068 1.00 53.40 C ANISOU 3908 CG GLU A 373 5629 4711 9951 -186 -14 -468 C ATOM 3909 CD GLU A 373 80.884 188.761 -5.786 1.00 57.24 C ANISOU 3909 CD GLU A 373 6052 5160 10539 -201 -50 -554 C ATOM 3910 OE1 GLU A 373 80.020 188.071 -5.199 1.00 59.85 O ANISOU 3910 OE1 GLU A 373 6312 5431 10998 -216 -6 -547 O ATOM 3911 OE2 GLU A 373 80.719 189.241 -6.929 1.00 58.35 O ANISOU 3911 OE2 GLU A 373 6214 5326 10629 -199 -122 -629 O ATOM 3912 N GLU A 374 81.832 192.072 -1.618 1.00 45.48 N ANISOU 3912 N GLU A 374 4684 3855 8740 -148 67 -209 N ATOM 3913 CA GLU A 374 81.417 192.561 -0.307 1.00 45.72 C ANISOU 3913 CA GLU A 374 4710 3901 8762 -141 113 -134 C ATOM 3914 C GLU A 374 80.623 193.853 -0.406 1.00 44.95 C ANISOU 3914 C GLU A 374 4613 3853 8615 -136 73 -143 C ATOM 3915 O GLU A 374 79.799 194.141 0.470 1.00 44.30 O ANISOU 3915 O GLU A 374 4503 3767 8564 -135 108 -105 O ATOM 3916 CB GLU A 374 82.628 192.767 0.590 1.00 47.66 C ANISOU 3916 CB GLU A 374 5011 4176 8922 -125 144 -66 C ATOM 3917 CG GLU A 374 83.297 191.475 0.969 1.00 50.16 C ANISOU 3917 CG GLU A 374 5327 4435 9297 -126 192 -41 C ATOM 3918 CD GLU A 374 82.330 190.510 1.617 1.00 54.40 C ANISOU 3918 CD GLU A 374 5812 4896 9963 -139 257 -14 C ATOM 3919 OE1 GLU A 374 81.474 190.971 2.403 1.00 54.81 O ANISOU 3919 OE1 GLU A 374 5847 4952 10026 -138 288 26 O ATOM 3920 OE2 GLU A 374 82.411 189.298 1.323 1.00 56.99 O ANISOU 3920 OE2 GLU A 374 6115 5154 10385 -151 279 -34 O ATOM 3921 N PHE A 375 80.869 194.655 -1.441 1.00 44.98 N ANISOU 3921 N PHE A 375 4652 3897 8539 -131 4 -189 N ATOM 3922 CA PHE A 375 79.999 195.799 -1.674 1.00 45.21 C ANISOU 3922 CA PHE A 375 4681 3960 8537 -126 -40 -205 C ATOM 3923 C PHE A 375 78.595 195.354 -2.050 1.00 43.11 C ANISOU 3923 C PHE A 375 4342 3648 8389 -138 -54 -258 C ATOM 3924 O PHE A 375 77.611 195.884 -1.525 1.00 41.66 O ANISOU 3924 O PHE A 375 4125 3468 8236 -135 -47 -245 O ATOM 3925 CB PHE A 375 80.585 196.703 -2.755 1.00 48.43 C ANISOU 3925 CB PHE A 375 5156 4410 8835 -120 -107 -239 C ATOM 3926 CG PHE A 375 81.795 197.466 -2.305 1.00 51.43 C ANISOU 3926 CG PHE A 375 5600 4839 9102 -108 -95 -189 C ATOM 3927 CD1 PHE A 375 82.087 197.592 -0.955 1.00 53.68 C ANISOU 3927 CD1 PHE A 375 5881 5139 9375 -101 -43 -122 C ATOM 3928 CD2 PHE A 375 82.642 198.049 -3.228 1.00 24.24 C ANISOU 3928 CD2 PHE A 375 2224 1421 5566 -105 -133 -212 C ATOM 3929 CE1 PHE A 375 83.200 198.288 -0.540 1.00 23.69 C ANISOU 3929 CE1 PHE A 375 2136 1384 5482 -90 -36 -88 C ATOM 3930 CE2 PHE A 375 83.756 198.742 -2.819 1.00 23.52 C ANISOU 3930 CE2 PHE A 375 2183 1369 5384 -97 -118 -173 C ATOM 3931 CZ PHE A 375 84.036 198.864 -1.474 1.00 23.24 C ANISOU 3931 CZ PHE A 375 2135 1351 5345 -89 -73 -115 C ATOM 3932 N LYS A 376 78.478 194.359 -2.932 1.00 43.23 N ANISOU 3932 N LYS A 376 4329 3617 8480 -151 -71 -324 N ATOM 3933 CA LYS A 376 77.148 193.882 -3.289 1.00 43.23 C ANISOU 3933 CA LYS A 376 4250 3567 8606 -163 -85 -387 C ATOM 3934 C LYS A 376 76.423 193.296 -2.090 1.00 44.27 C ANISOU 3934 C LYS A 376 4316 3653 8849 -173 -2 -340 C ATOM 3935 O LYS A 376 75.208 193.463 -1.965 1.00 45.32 O ANISOU 3935 O LYS A 376 4390 3766 9062 -177 -2 -366 O ATOM 3936 CB LYS A 376 77.236 192.853 -4.419 1.00 43.19 C ANISOU 3936 CB LYS A 376 4226 3518 8668 -176 -117 -475 C ATOM 3937 CG LYS A 376 77.686 193.423 -5.770 1.00 43.23 C ANISOU 3937 CG LYS A 376 4294 3558 8574 -167 -204 -538 C ATOM 3938 CD LYS A 376 78.015 192.299 -6.754 1.00 45.34 C ANISOU 3938 CD LYS A 376 4550 3781 8897 -179 -223 -619 C ATOM 3939 CE LYS A 376 78.753 192.849 -7.973 1.00 46.64 C ANISOU 3939 CE LYS A 376 4800 3981 8939 -168 -291 -665 C ATOM 3940 NZ LYS A 376 79.328 191.786 -8.853 1.00 48.72 N ANISOU 3940 NZ LYS A 376 5067 4208 9237 -177 -302 -739 N ATOM 3941 N ALA A 377 77.136 192.640 -1.185 1.00 45.27 N ANISOU 3941 N ALA A 377 4458 3761 8983 -175 72 -271 N ATOM 3942 CA ALA A 377 76.446 192.104 -0.018 1.00 47.30 C ANISOU 3942 CA ALA A 377 4667 3968 9338 -184 160 -218 C ATOM 3943 C ALA A 377 75.968 193.205 0.914 1.00 49.21 C ANISOU 3943 C ALA A 377 4918 4254 9527 -171 179 -162 C ATOM 3944 O ALA A 377 74.933 193.052 1.571 1.00 50.70 O ANISOU 3944 O ALA A 377 5053 4404 9808 -179 231 -147 O ATOM 3945 CB ALA A 377 77.339 191.132 0.730 1.00 46.14 C ANISOU 3945 CB ALA A 377 4544 3783 9206 -187 233 -154 C ATOM 3946 N ALA A 378 76.691 194.320 0.983 1.00 49.81 N ANISOU 3946 N ALA A 378 5060 4404 9461 -151 140 -134 N ATOM 3947 CA ALA A 378 76.264 195.389 1.878 1.00 50.04 C ANISOU 3947 CA ALA A 378 5100 4473 9440 -139 156 -87 C ATOM 3948 C ALA A 378 75.013 196.094 1.363 1.00 48.78 C ANISOU 3948 C ALA A 378 4893 4318 9322 -139 106 -143 C ATOM 3949 O ALA A 378 74.202 196.579 2.158 1.00 45.88 O ANISOU 3949 O ALA A 378 4499 3951 8983 -135 140 -116 O ATOM 3950 CB ALA A 378 77.402 196.382 2.095 1.00 49.46 C ANISOU 3950 CB ALA A 378 5108 4471 9215 -120 128 -49 C ATOM 3951 N PHE A 379 74.848 196.188 0.041 1.00 51.36 N ANISOU 3951 N PHE A 379 5215 4649 9652 -141 24 -223 N ATOM 3952 CA PHE A 379 73.650 196.830 -0.500 1.00 53.83 C ANISOU 3952 CA PHE A 379 5484 4962 10007 -137 -33 -284 C ATOM 3953 C PHE A 379 72.413 195.959 -0.315 1.00 57.80 C ANISOU 3953 C PHE A 379 5888 5395 10679 -154 9 -322 C ATOM 3954 O PHE A 379 71.317 196.475 -0.064 1.00 57.70 O ANISOU 3954 O PHE A 379 5827 5377 10721 -151 6 -340 O ATOM 3955 CB PHE A 379 73.845 197.162 -1.983 1.00 53.78 C ANISOU 3955 CB PHE A 379 5509 4975 9948 -132 -135 -360 C ATOM 3956 CG PHE A 379 74.819 198.282 -2.234 1.00 52.98 C ANISOU 3956 CG PHE A 379 5504 4938 9688 -116 -179 -328 C ATOM 3957 CD1 PHE A 379 74.836 199.411 -1.428 1.00 51.90 C ANISOU 3957 CD1 PHE A 379 5397 4844 9480 -103 -168 -271 C ATOM 3958 CD2 PHE A 379 75.733 198.195 -3.264 1.00 52.79 C ANISOU 3958 CD2 PHE A 379 5541 4926 9591 -116 -224 -357 C ATOM 3959 CE1 PHE A 379 75.741 200.435 -1.663 1.00 51.51 C ANISOU 3959 CE1 PHE A 379 5432 4844 9295 -91 -203 -246 C ATOM 3960 CE2 PHE A 379 76.634 199.214 -3.499 1.00 52.32 C ANISOU 3960 CE2 PHE A 379 5570 4915 9393 -104 -253 -328 C ATOM 3961 CZ PHE A 379 76.639 200.332 -2.700 1.00 52.46 C ANISOU 3961 CZ PHE A 379 5613 4972 9347 -92 -242 -273 C ATOM 3962 N SER A 380 72.565 194.639 -0.444 1.00 60.45 N ANISOU 3962 N SER A 380 6191 5670 11105 -174 51 -339 N ATOM 3963 CA SER A 380 71.414 193.753 -0.321 1.00 64.29 C ANISOU 3963 CA SER A 380 6582 6079 11765 -195 97 -382 C ATOM 3964 C SER A 380 70.916 193.707 1.115 1.00 64.68 C ANISOU 3964 C SER A 380 6608 6103 11865 -200 203 -301 C ATOM 3965 O SER A 380 69.706 193.780 1.364 1.00 65.08 O ANISOU 3965 O SER A 380 6589 6120 12020 -208 226 -330 O ATOM 3966 CB SER A 380 71.774 192.360 -0.836 1.00 67.32 C ANISOU 3966 CB SER A 380 6943 6401 12235 -217 115 -421 C ATOM 3967 OG SER A 380 72.254 192.439 -2.169 1.00 68.33 O ANISOU 3967 OG SER A 380 7100 6555 12307 -210 18 -497 O ATOM 3968 N TRP A 381 71.834 193.607 2.075 1.00 64.66 N ANISOU 3968 N TRP A 381 6666 6114 11788 -194 268 -203 N ATOM 3969 CA TRP A 381 71.428 193.622 3.474 1.00 66.02 C ANISOU 3969 CA TRP A 381 6831 6265 11989 -195 370 -120 C ATOM 3970 C TRP A 381 70.775 194.952 3.837 1.00 63.94 C ANISOU 3970 C TRP A 381 6566 6052 11675 -178 346 -116 C ATOM 3971 O TRP A 381 69.787 194.987 4.582 1.00 65.02 O ANISOU 3971 O TRP A 381 6654 6155 11897 -184 411 -99 O ATOM 3972 CB TRP A 381 72.638 193.340 4.370 1.00 69.07 C ANISOU 3972 CB TRP A 381 7293 6663 12285 -186 428 -22 C ATOM 3973 CG TRP A 381 72.367 193.543 5.833 1.00 72.49 C ANISOU 3973 CG TRP A 381 7744 7089 12711 -179 523 70 C ATOM 3974 CD1 TRP A 381 71.992 192.589 6.740 1.00 74.36 C ANISOU 3974 CD1 TRP A 381 7960 7248 13045 -194 637 131 C ATOM 3975 CD2 TRP A 381 72.443 194.778 6.560 1.00 74.08 C ANISOU 3975 CD2 TRP A 381 7989 7356 12803 -156 517 114 C ATOM 3976 NE1 TRP A 381 71.831 193.153 7.984 1.00 74.86 N ANISOU 3976 NE1 TRP A 381 8057 7329 13057 -179 703 212 N ATOM 3977 CE2 TRP A 381 72.100 194.494 7.901 1.00 74.62 C ANISOU 3977 CE2 TRP A 381 8064 7387 12902 -156 629 199 C ATOM 3978 CE3 TRP A 381 72.764 196.094 6.209 1.00 73.33 C ANISOU 3978 CE3 TRP A 381 7932 7344 12588 -137 431 90 C ATOM 3979 CZ2 TRP A 381 72.070 195.476 8.889 1.00 75.56 C ANISOU 3979 CZ2 TRP A 381 8224 7550 12935 -135 653 254 C ATOM 3980 CZ3 TRP A 381 72.731 197.068 7.193 1.00 74.03 C ANISOU 3980 CZ3 TRP A 381 8056 7472 12599 -119 455 142 C ATOM 3981 CH2 TRP A 381 72.386 196.753 8.517 1.00 74.71 C ANISOU 3981 CH2 TRP A 381 8147 7522 12718 -117 563 220 C ATOM 3982 N TRP A 382 71.273 196.046 3.264 1.00 60.22 N ANISOU 3982 N TRP A 382 6144 5657 11078 -158 253 -136 N ATOM 3983 CA TRP A 382 70.800 197.384 3.605 1.00 56.52 C ANISOU 3983 CA TRP A 382 5685 5238 10551 -140 225 -128 C ATOM 3984 C TRP A 382 69.452 197.695 2.963 1.00 54.72 C ANISOU 3984 C TRP A 382 5353 4977 10460 -137 178 -216 C ATOM 3985 O TRP A 382 68.585 198.298 3.604 1.00 54.49 O ANISOU 3985 O TRP A 382 5258 4931 10513 -125 209 -211 O ATOM 3986 CB TRP A 382 71.863 198.401 3.182 1.00 53.92 C ANISOU 3986 CB TRP A 382 5440 4987 10059 -120 147 -119 C ATOM 3987 CG TRP A 382 71.562 199.861 3.378 1.00 51.34 C ANISOU 3987 CG TRP A 382 5136 4713 9659 -102 103 -116 C ATOM 3988 CD1 TRP A 382 70.686 200.429 4.258 1.00 50.84 C ANISOU 3988 CD1 TRP A 382 5022 4637 9656 -94 144 -97 C ATOM 3989 CD2 TRP A 382 72.174 200.936 2.668 1.00 49.27 C ANISOU 3989 CD2 TRP A 382 4937 4509 9276 -88 14 -134 C ATOM 3990 NE1 TRP A 382 70.713 201.797 4.131 1.00 49.62 N ANISOU 3990 NE1 TRP A 382 4898 4533 9424 -77 79 -105 N ATOM 3991 CE2 TRP A 382 71.621 202.132 3.160 1.00 48.51 C ANISOU 3991 CE2 TRP A 382 4842 4439 9150 -75 0 -124 C ATOM 3992 CE3 TRP A 382 73.138 201.002 1.655 1.00 48.03 C ANISOU 3992 CE3 TRP A 382 4838 4377 9035 -86 -50 -155 C ATOM 3993 CZ2 TRP A 382 72.000 203.382 2.674 1.00 47.32 C ANISOU 3993 CZ2 TRP A 382 4751 4336 8891 -60 -77 -135 C ATOM 3994 CZ3 TRP A 382 73.512 202.241 1.174 1.00 46.80 C ANISOU 3994 CZ3 TRP A 382 4743 4268 8770 -72 -120 -162 C ATOM 3995 CH2 TRP A 382 72.944 203.415 1.682 1.00 46.37 C ANISOU 3995 CH2 TRP A 382 4692 4236 8692 -60 -134 -151 C ATOM 3996 N TRP A 383 69.252 197.292 1.707 1.00 53.61 N ANISOU 3996 N TRP A 383 5183 4819 10368 -143 104 -305 N ATOM 3997 CA TRP A 383 68.030 197.632 0.985 1.00 53.14 C ANISOU 3997 CA TRP A 383 5016 4725 10450 -132 39 -406 C ATOM 3998 C TRP A 383 67.007 196.509 0.943 1.00 57.04 C ANISOU 3998 C TRP A 383 5395 5125 11153 -153 91 -469 C ATOM 3999 O TRP A 383 65.837 196.770 0.639 1.00 59.17 O ANISOU 3999 O TRP A 383 5559 5355 11568 -142 59 -554 O ATOM 4000 CB TRP A 383 68.351 198.057 -0.452 1.00 49.34 C ANISOU 4000 CB TRP A 383 4570 4280 9898 -118 -92 -480 C ATOM 4001 CG TRP A 383 69.071 199.354 -0.518 1.00 45.03 C ANISOU 4001 CG TRP A 383 4121 3812 9177 -98 -150 -436 C ATOM 4002 CD1 TRP A 383 70.413 199.533 -0.623 1.00 42.76 C ANISOU 4002 CD1 TRP A 383 3962 3583 8703 -102 -155 -379 C ATOM 4003 CD2 TRP A 383 68.492 200.662 -0.468 1.00 43.38 C ANISOU 4003 CD2 TRP A 383 3887 3624 8970 -72 -207 -449 C ATOM 4004 NE1 TRP A 383 70.714 200.870 -0.645 1.00 41.26 N ANISOU 4004 NE1 TRP A 383 3834 3448 8396 -83 -206 -354 N ATOM 4005 CE2 TRP A 383 69.553 201.587 -0.552 1.00 41.66 C ANISOU 4005 CE2 TRP A 383 3795 3477 8557 -65 -242 -393 C ATOM 4006 CE3 TRP A 383 67.183 201.142 -0.354 1.00 42.47 C ANISOU 4006 CE3 TRP A 383 3655 3471 9010 -52 -232 -506 C ATOM 4007 CZ2 TRP A 383 69.350 202.960 -0.529 1.00 27.71 C ANISOU 4007 CZ2 TRP A 383 2046 1741 6741 -44 -299 -389 C ATOM 4008 CZ3 TRP A 383 66.982 202.511 -0.331 1.00 40.59 C ANISOU 4008 CZ3 TRP A 383 3428 3268 8727 -28 -297 -504 C ATOM 4009 CH2 TRP A 383 68.061 203.404 -0.421 1.00 38.12 C ANISOU 4009 CH2 TRP A 383 3249 3023 8213 -26 -330 -443 C ATOM 4010 N LEU A 384 67.407 195.278 1.258 1.00 58.41 N ANISOU 4010 N LEU A 384 5584 5258 11351 -182 171 -434 N ATOM 4011 CA LEU A 384 66.516 194.132 1.101 1.00 61.66 C ANISOU 4011 CA LEU A 384 5892 5573 11961 -211 220 -501 C ATOM 4012 C LEU A 384 66.412 193.257 2.345 1.00 65.93 C ANISOU 4012 C LEU A 384 6421 6051 12577 -238 368 -415 C ATOM 4013 O LEU A 384 65.343 192.704 2.631 1.00 68.21 O ANISOU 4013 O LEU A 384 6609 6256 13053 -260 437 -452 O ATOM 4014 CB LEU A 384 66.983 193.271 -0.071 1.00 60.16 C ANISOU 4014 CB LEU A 384 5716 5373 11769 -226 158 -573 C ATOM 4015 CG LEU A 384 67.151 193.948 -1.428 1.00 35.64 C ANISOU 4015 CG LEU A 384 2628 2320 8594 -200 13 -663 C ATOM 4016 CD1 LEU A 384 67.831 192.995 -2.378 1.00 35.92 C ANISOU 4016 CD1 LEU A 384 2695 2343 8608 -217 -23 -712 C ATOM 4017 CD2 LEU A 384 65.816 194.398 -1.990 1.00 36.72 C ANISOU 4017 CD2 LEU A 384 2647 2424 8880 -183 -55 -783 C ATOM 4018 N GLY A 385 67.503 193.138 3.096 1.00 67.97 N ANISOU 4018 N GLY A 385 6784 6345 12696 -237 419 -302 N ATOM 4019 CA GLY A 385 67.655 192.087 4.073 1.00 71.29 C ANISOU 4019 CA GLY A 385 7214 6702 13172 -261 546 -221 C ATOM 4020 C GLY A 385 68.240 190.804 3.526 1.00 74.37 C ANISOU 4020 C GLY A 385 7621 7048 13588 -287 549 -240 C ATOM 4021 O GLY A 385 68.426 189.852 4.293 1.00 74.69 O ANISOU 4021 O GLY A 385 7667 7022 13692 -306 654 -171 O ATOM 4022 N VAL A 386 68.538 190.743 2.226 1.00 77.92 N ANISOU 4022 N VAL A 386 8066 7518 14023 -284 443 -333 N ATOM 4023 CA VAL A 386 69.180 189.562 1.664 1.00 82.56 C ANISOU 4023 CA VAL A 386 8651 8055 14661 -301 446 -359 C ATOM 4024 C VAL A 386 70.584 189.416 2.262 1.00 84.52 C ANISOU 4024 C VAL A 386 8995 8332 14785 -286 479 -254 C ATOM 4025 O VAL A 386 71.243 190.405 2.614 1.00 83.43 O ANISOU 4025 O VAL A 386 8931 8277 14493 -257 452 -198 O ATOM 4026 CB VAL A 386 69.228 189.662 0.128 1.00 83.04 C ANISOU 4026 CB VAL A 386 8697 8143 14713 -296 319 -483 C ATOM 4027 CG1 VAL A 386 69.657 188.344 -0.490 1.00 84.59 C ANISOU 4027 CG1 VAL A 386 8871 8272 14997 -319 326 -531 C ATOM 4028 CG2 VAL A 386 67.866 190.074 -0.408 1.00 84.06 C ANISOU 4028 CG2 VAL A 386 8741 8262 14935 -301 268 -587 C ATOM 4029 N HIS A 387 71.031 188.162 2.414 1.00 88.31 N ANISOU 4029 N HIS A 387 9473 8738 15343 -305 541 -231 N ATOM 4030 CA HIS A 387 72.341 187.918 3.017 1.00 91.24 C ANISOU 4030 CA HIS A 387 9931 9126 15610 -289 575 -136 C ATOM 4031 C HIS A 387 73.471 188.411 2.115 1.00 91.15 C ANISOU 4031 C HIS A 387 9982 9194 15457 -267 471 -171 C ATOM 4032 O HIS A 387 74.386 189.102 2.582 1.00 90.08 O ANISOU 4032 O HIS A 387 9924 9127 15175 -242 460 -105 O ATOM 4033 CB HIS A 387 72.511 186.429 3.375 1.00 95.00 C ANISOU 4033 CB HIS A 387 10390 9494 16212 -315 666 -102 C ATOM 4034 CG HIS A 387 72.568 185.494 2.195 1.00 97.84 C ANISOU 4034 CG HIS A 387 10701 9800 16674 -336 621 -206 C ATOM 4035 ND1 HIS A 387 71.822 185.681 1.050 1.00 99.19 N ANISOU 4035 ND1 HIS A 387 10805 9977 16905 -347 539 -334 N ATOM 4036 CD2 HIS A 387 73.274 184.350 1.999 1.00 99.71 C ANISOU 4036 CD2 HIS A 387 10947 9971 16966 -348 645 -205 C ATOM 4037 CE1 HIS A 387 72.076 184.703 0.196 1.00100.13 C ANISOU 4037 CE1 HIS A 387 10895 10042 17109 -364 514 -410 C ATOM 4038 NE2 HIS A 387 72.953 183.882 0.747 1.00100.39 N ANISOU 4038 NE2 HIS A 387 10971 10028 17143 -366 578 -333 N ATOM 4039 N HIS A 388 73.411 188.112 0.819 1.00 92.69 N ANISOU 4039 N HIS A 388 10143 9380 15693 -276 393 -278 N ATOM 4040 CA HIS A 388 74.411 188.649 -0.101 1.00 92.69 C ANISOU 4040 CA HIS A 388 10205 9454 15558 -256 298 -313 C ATOM 4041 C HIS A 388 74.025 188.509 -1.572 1.00 93.34 C ANISOU 4041 C HIS A 388 10247 9531 15687 -264 206 -443 C ATOM 4042 O HIS A 388 74.675 189.096 -2.443 1.00 92.42 O ANISOU 4042 O HIS A 388 10182 9477 15457 -248 123 -480 O ATOM 4043 CB HIS A 388 75.772 187.973 0.135 1.00 93.61 C ANISOU 4043 CB HIS A 388 10383 9561 15625 -251 327 -260 C ATOM 4044 CG HIS A 388 75.837 186.551 -0.340 1.00 95.78 C ANISOU 4044 CG HIS A 388 10615 9743 16032 -275 350 -308 C ATOM 4045 ND1 HIS A 388 75.821 185.470 0.518 1.00 97.56 N ANISOU 4045 ND1 HIS A 388 10824 9880 16363 -291 450 -247 N ATOM 4046 CD2 HIS A 388 75.921 186.035 -1.589 1.00 96.81 C ANISOU 4046 CD2 HIS A 388 10720 9854 16210 -285 287 -414 C ATOM 4047 CE1 HIS A 388 75.886 184.351 -0.183 1.00 98.57 C ANISOU 4047 CE1 HIS A 388 10913 9933 16604 -312 447 -314 C ATOM 4048 NE2 HIS A 388 75.947 184.666 -1.464 1.00 98.30 N ANISOU 4048 NE2 HIS A 388 10871 9942 16537 -308 348 -420 N TER 4049 HIS A 388 HETATM 4050 C10 7MA A1201 98.174 221.051 -0.587 1.00 36.99 C HETATM 4051 C13 7MA A1201 94.820 225.402 2.198 1.00 41.22 C HETATM 4052 C15 7MA A1201 92.752 224.040 2.019 1.00 41.14 C HETATM 4053 C20 7MA A1201 91.791 224.711 1.255 1.00 40.86 C HETATM 4054 C22 7MA A1201 90.118 220.467 -0.023 1.00 39.56 C HETATM 4055 C26 7MA A1201 91.858 225.642 4.636 1.00 40.76 C HETATM 4056 C28 7MA A1201 90.662 227.716 4.749 1.00 40.57 C HETATM 4057 C32 7MA A1201 90.572 223.422 4.704 1.00 40.80 C HETATM 4058 C31 7MA A1201 90.660 224.922 4.717 1.00 40.88 C HETATM 4059 C30 7MA A1201 89.480 225.652 4.825 1.00 40.85 C HETATM 4060 C29 7MA A1201 89.480 227.027 4.841 1.00 40.68 C HETATM 4061 C27 7MA A1201 91.853 227.031 4.639 1.00 40.53 C HETATM 4062 S23 7MA A1201 93.406 224.819 4.460 0.13 40.66 S HETATM 4063 O24 7MA A1201 94.420 225.662 5.013 0.49 40.87 O HETATM 4064 O25 7MA A1201 93.265 223.478 4.932 0.76 40.40 O HETATM 4065 N14 7MA A1201 93.670 224.732 2.801 1.00 41.21 N HETATM 4066 C16 7MA A1201 92.751 222.650 1.998 1.00 41.24 C HETATM 4067 N17 7MA A1201 91.878 221.940 1.274 1.00 40.98 N HETATM 4068 C19 7MA A1201 90.905 223.993 0.518 1.00 40.55 C HETATM 4069 C18 7MA A1201 90.989 222.606 0.566 1.00 40.49 C HETATM 4070 O21 7MA A1201 90.101 221.894 -0.170 1.00 39.88 O HETATM 4071 C11 7MA A1201 95.465 224.642 1.044 1.00 40.96 C HETATM 4072 O12 7MA A1201 95.000 224.749 -0.088 1.00 41.27 O HETATM 4073 N03 7MA A1201 96.535 223.854 1.312 1.00 40.24 N HETATM 4074 C02 7MA A1201 96.964 223.517 2.679 1.00 40.70 C HETATM 4075 C01 7MA A1201 98.403 223.883 2.943 1.00 40.99 C HETATM 4076 C04 7MA A1201 97.335 223.283 0.221 1.00 39.16 C HETATM 4077 C05 7MA A1201 97.241 221.785 0.120 1.00 38.05 C HETATM 4078 C09 7MA A1201 98.058 219.682 -0.668 1.00 36.12 C HETATM 4079 C08 7MA A1201 96.995 219.074 -0.043 1.00 36.04 C HETATM 4080 N07 7MA A1201 96.064 219.744 0.645 1.00 36.54 N HETATM 4081 C06 7MA A1201 96.201 221.079 0.708 1.00 37.57 C HETATM 4082 H1 7MA A1201 98.891 221.490 -1.014 1.00 44.67 H HETATM 4083 H2 7MA A1201 95.499 225.548 2.890 1.00 49.75 H HETATM 4084 H3 7MA A1201 94.536 226.281 1.869 1.00 49.75 H HETATM 4085 H4 7MA A1201 91.773 225.643 1.261 1.00 49.32 H HETATM 4086 H5 7MA A1201 89.451 220.074 -0.610 1.00 47.76 H HETATM 4087 H6 7MA A1201 90.997 220.128 -0.260 1.00 47.76 H HETATM 4088 H7 7MA A1201 89.917 220.235 0.898 1.00 47.76 H HETATM 4089 H8 7MA A1201 90.661 228.656 4.761 1.00 48.97 H HETATM 4090 H9 7MA A1201 90.679 223.082 5.607 1.00 49.25 H HETATM 4091 H10 7MA A1201 91.273 223.060 4.138 1.00 49.25 H HETATM 4092 H11 7MA A1201 89.706 223.150 4.358 1.00 49.25 H HETATM 4093 H12 7MA A1201 88.661 225.188 4.889 1.00 49.31 H HETATM 4094 H13 7MA A1201 88.665 227.497 4.915 1.00 49.11 H HETATM 4095 H14 7MA A1201 92.663 227.502 4.567 1.00 48.92 H HETATM 4096 H15 7MA A1201 93.389 222.189 2.514 1.00 49.78 H HETATM 4097 H16 7MA A1201 90.251 224.418 -0.009 1.00 48.95 H HETATM 4098 H17 7MA A1201 96.845 222.554 2.823 1.00 49.12 H HETATM 4099 H18 7MA A1201 96.390 223.990 3.319 1.00 49.12 H HETATM 4100 H19 7MA A1201 98.624 223.683 3.867 1.00 49.48 H HETATM 4101 H20 7MA A1201 98.532 224.831 2.779 1.00 49.48 H HETATM 4102 H21 7MA A1201 98.981 223.371 2.355 1.00 49.48 H HETATM 4103 H22 7MA A1201 98.273 223.536 0.357 1.00 47.28 H HETATM 4104 H23 7MA A1201 97.036 223.679 -0.625 1.00 47.28 H HETATM 4105 H24 7MA A1201 98.693 219.173 -1.142 1.00 43.63 H HETATM 4106 H25 7MA A1201 96.916 218.137 -0.099 1.00 43.54 H HETATM 4107 H26 7MA A1201 95.551 221.565 1.182 1.00 45.37 H HETATM 4108 O1 PG4 A1202 92.808 232.019 1.003 1.00 51.71 O HETATM 4109 C1 PG4 A1202 92.813 232.378 -0.368 1.00 51.80 C HETATM 4110 C2 PG4 A1202 92.630 231.195 -1.268 1.00 51.78 C HETATM 4111 O2 PG4 A1202 92.670 231.609 -2.628 1.00 51.82 O HETATM 4112 C3 PG4 A1202 93.901 232.230 -2.977 1.00 52.24 C HETATM 4113 C4 PG4 A1202 93.854 232.695 -4.399 1.00 52.73 C HETATM 4114 O3 PG4 A1202 95.072 233.361 -4.717 1.00 53.12 O HETATM 4115 C5 PG4 A1202 95.250 234.571 -3.987 1.00 53.21 C HETATM 4116 C6 PG4 A1202 96.677 235.020 -4.066 1.00 53.10 C HETATM 4117 O4 PG4 A1202 96.877 236.120 -3.186 1.00 52.93 O HETATM 4118 C7 PG4 A1202 98.247 236.325 -2.857 1.00 52.62 C HETATM 4119 C8 PG4 A1202 98.760 235.171 -2.044 1.00 51.98 C HETATM 4120 O5 PG4 A1202 98.068 235.025 -0.817 1.00 51.39 O HETATM 4121 C8 OLA A1203 107.462 213.407 8.255 1.00 33.97 C HETATM 4122 C9 OLA A1203 108.007 212.012 8.305 1.00 33.88 C HETATM 4123 C10 OLA A1203 107.331 210.886 8.297 1.00 33.58 C HETATM 4124 C11 OLA A1203 107.942 209.519 8.370 1.00 33.50 C HETATM 4125 C12 OLA A1203 106.957 208.407 8.169 1.00 33.92 C HETATM 4126 C13 OLA A1203 106.471 207.708 9.433 1.00 34.42 C HETATM 4127 C14 OLA A1203 105.270 206.810 9.201 1.00 35.03 C HETATM 4128 C15 OLA A1203 105.054 205.722 10.234 1.00 35.21 C HETATM 4129 C16 OLA A1203 106.111 204.636 10.227 1.00 35.35 C HETATM 4130 C17 OLA A1203 105.810 203.431 11.093 1.00 35.16 C HETATM 4131 C18 OLA A1203 106.847 202.326 11.080 1.00 34.74 C HETATM 4132 O HOH A1301 132.326 175.381 -9.967 1.00 28.58 O HETATM 4133 O HOH A1302 112.466 179.143 -21.715 1.00 26.29 O HETATM 4134 O HOH A1303 81.551 246.802 0.877 1.00 27.40 O HETATM 4135 O HOH A1304 97.268 178.842 -13.576 1.00 28.40 O HETATM 4136 O HOH A1305 98.372 192.701 1.647 1.00 14.12 O HETATM 4137 O HOH A1306 94.302 189.600 -15.971 1.00 33.38 O HETATM 4138 O HOH A1307 96.680 242.193 -20.202 1.00 16.61 O HETATM 4139 O HOH A1308 136.463 172.632 -27.838 1.00 19.24 O HETATM 4140 O HOH A1309 92.235 213.729 2.134 1.00 33.12 O HETATM 4141 O HOH A1310 101.948 189.795 -0.377 1.00 21.05 O HETATM 4142 O HOH A1311 89.714 207.078 -0.138 1.00 0.94 O HETATM 4143 O HOH A1312 93.377 219.596 1.661 1.00 6.17 O HETATM 4144 O HOH A1313 90.981 233.885 2.045 1.00 36.37 O HETATM 4145 O HOH A1314 101.761 221.859 -2.074 1.00 15.57 O HETATM 4146 O HOH A1315 93.123 194.387 -10.702 1.00 20.72 O HETATM 4147 O HOH A1316 80.300 236.084 -3.226 1.00 21.19 O HETATM 4148 O HOH A1317 134.787 177.875 -11.424 1.00 12.19 O HETATM 4149 O HOH A1318 132.060 169.151 -4.503 1.00 27.98 O HETATM 4150 O HOH A1319 93.035 192.976 -5.369 1.00 21.87 O HETATM 4151 O HOH A1320 96.219 228.933 0.925 1.00 34.79 O HETATM 4152 O HOH A1321 97.062 173.909 -9.487 1.00 30.07 O HETATM 4153 O HOH A1322 99.419 183.978 -17.875 1.00 23.25 O HETATM 4154 O HOH A1323 93.777 227.502 -0.448 1.00 17.89 O HETATM 4155 O HOH A1324 131.712 173.822 -4.891 1.00 29.80 O HETATM 4156 O HOH A1325 90.870 209.045 1.454 1.00 6.29 O HETATM 4157 O HOH A1326 118.546 177.448 -16.494 1.00 19.20 O HETATM 4158 O HOH A1327 130.714 157.506 -26.170 1.00 26.60 O HETATM 4159 O HOH A1328 102.380 191.383 3.620 1.00 44.15 O HETATM 4160 O HOH A1329 111.767 183.521 3.068 1.00 1.62 O HETATM 4161 O HOH A1330 130.275 168.460 -1.859 1.00 23.18 O HETATM 4162 O HOH A1331 75.819 236.352 -5.791 1.00 14.09 O HETATM 4163 O HOH A1332 87.937 232.954 4.085 1.00 12.56 O HETATM 4164 O HOH A1333 94.560 228.648 3.433 1.00 45.61 O HETATM 4165 O HOH A1334 89.792 229.324 -2.356 1.00 25.39 O HETATM 4166 O HOH A1335 89.174 192.700 -10.847 1.00 30.04 O HETATM 4167 O HOH A1336 108.438 157.041 -16.734 1.00 15.71 O HETATM 4168 O HOH A1337 91.433 192.138 -1.858 1.00 18.91 O HETATM 4169 O HOH A1338 87.666 231.878 -1.131 1.00 33.67 O HETATM 4170 O HOH A1339 97.922 191.604 -1.869 1.00 21.04 O HETATM 4171 O HOH A1340 98.711 215.863 -1.589 0.69 24.58 O HETATM 4172 O HOH A1341 102.394 188.258 -19.679 1.00 17.22 O HETATM 4173 O HOH A1342 88.827 236.016 0.313 1.00 49.18 O HETATM 4174 O HOH A1343 95.758 177.864 -19.356 1.00 36.30 O HETATM 4175 O HOH A1344 97.286 182.252 -14.266 1.00 34.91 O HETATM 4176 O HOH A1345 92.704 244.199 -15.318 1.00 12.11 O HETATM 4177 O HOH A1346 130.572 161.184 -30.374 1.00 15.36 O HETATM 4178 O HOH A1347 119.294 182.543 -19.403 1.00 18.15 O HETATM 4179 O HOH A1348 101.107 187.210 -22.802 1.00 17.84 O HETATM 4180 O HOH A1349 135.953 159.540 -28.787 1.00 40.43 O HETATM 4181 O HOH A1350 92.650 236.993 2.614 1.00 21.49 O HETATM 4182 O HOH A1351 133.691 161.174 -7.892 1.00 30.57 O HETATM 4183 O HOH A1352 99.930 190.222 3.898 1.00 15.07 O HETATM 4184 O HOH A1353 95.198 180.597 -17.282 1.00 34.32 O HETATM 4185 O HOH A1354 119.143 180.139 -24.637 1.00 14.10 O HETATM 4186 O HOH A1355 90.540 228.399 1.569 1.00 29.30 O HETATM 4187 O HOH A1356 102.957 190.501 -21.065 1.00 19.80 O CONECT 740 1340 CONECT 1340 740 CONECT 1729 1735 CONECT 1735 1729 1736 CONECT 1736 1735 1737 1743 CONECT 1737 1736 1738 CONECT 1738 1737 1739 CONECT 1739 1738 1740 CONECT 1740 1739 1741 1742 CONECT 1741 1740 CONECT 1742 1740 CONECT 1743 1736 1744 1745 CONECT 1744 1743 CONECT 1745 1743 CONECT 4050 4077 4078 4082 CONECT 4051 4065 4071 4083 4084 CONECT 4052 4053 4065 4066 CONECT 4053 4052 4068 4085 CONECT 4054 4070 4086 4087 4088 CONECT 4055 4058 4061 4062 CONECT 4056 4060 4061 4089 CONECT 4057 4058 4090 4091 4092 CONECT 4058 4055 4057 4059 CONECT 4059 4058 4060 4093 CONECT 4060 4056 4059 4094 CONECT 4061 4055 4056 4095 CONECT 4062 4055 4063 4064 4065 CONECT 4063 4062 CONECT 4064 4062 CONECT 4065 4051 4052 4062 CONECT 4066 4052 4067 4096 CONECT 4067 4066 4069 CONECT 4068 4053 4069 4097 CONECT 4069 4067 4068 4070 CONECT 4070 4054 4069 CONECT 4071 4051 4072 4073 CONECT 4072 4071 CONECT 4073 4071 4074 4076 CONECT 4074 4073 4075 4098 4099 CONECT 4075 4074 4100 4101 4102 CONECT 4076 4073 4077 4103 4104 CONECT 4077 4050 4076 4081 CONECT 4078 4050 4079 4105 CONECT 4079 4078 4080 4106 CONECT 4080 4079 4081 CONECT 4081 4077 4080 4107 CONECT 4082 4050 CONECT 4083 4051 CONECT 4084 4051 CONECT 4085 4053 CONECT 4086 4054 CONECT 4087 4054 CONECT 4088 4054 CONECT 4089 4056 CONECT 4090 4057 CONECT 4091 4057 CONECT 4092 4057 CONECT 4093 4059 CONECT 4094 4060 CONECT 4095 4061 CONECT 4096 4066 CONECT 4097 4068 CONECT 4098 4074 CONECT 4099 4074 CONECT 4100 4075 CONECT 4101 4075 CONECT 4102 4075 CONECT 4103 4076 CONECT 4104 4076 CONECT 4105 4078 CONECT 4106 4079 CONECT 4107 4081 CONECT 4108 4109 CONECT 4109 4108 4110 CONECT 4110 4109 4111 CONECT 4111 4110 4112 CONECT 4112 4111 4113 CONECT 4113 4112 4114 CONECT 4114 4113 4115 CONECT 4115 4114 4116 CONECT 4116 4115 4117 CONECT 4117 4116 4118 CONECT 4118 4117 4119 CONECT 4119 4118 4120 CONECT 4120 4119 CONECT 4121 4122 CONECT 4122 4121 4123 CONECT 4123 4122 4124 CONECT 4124 4123 4125 CONECT 4125 4124 4126 CONECT 4126 4125 4127 CONECT 4127 4126 4128 CONECT 4128 4127 4129 CONECT 4129 4128 4130 CONECT 4130 4129 4131 CONECT 4131 4130 MASTER 351 0 4 22 8 0 5 6 4160 1 96 44 END