HEADER SIGNALING PROTEIN 28-SEP-16 5TGZ TITLE CRYSTAL STRUCTURE OF THE HUMAN CANNABINOID RECEPTOR CB1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CANNABINOID RECEPTOR 1,FLAVODOXIN,CANNABINOID RECEPTOR 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 99-306,UNP RESIDUES 2-148,UNP RESIDUES 332- COMPND 5 414; COMPND 6 SYNONYM: CB1,CANN6,CB1,CANN6; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 OTHER_DETAILS: THE FUSION PROTEIN OF CANNABINOID RECEPTOR 1 (RESIDUES COMPND 10 99-306), FLAVODOXIN (RESIDUES 1002-1148), AND CANNABINOID RECEPTOR 1 COMPND 11 (RESIDUES 332-414) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, DESULFOVIBRIO VULGARIS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 882; SOURCE 5 STRAIN: HILDENBOROUGH / ATCC 29579 / NCIMB 8303; SOURCE 6 GENE: CNR1, CNR, DVU_2680; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: FREESTYLE 293-F (HEK-293F); SOURCE 10 EXPRESSION_SYSTEM_CELL: HEK293F; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PTT5 KEYWDS MEMBRANE PROTEIN, G PROTEIN-COUPLED RECEPTOR, HUMAN CANNABINOID KEYWDS 2 RECEPTOR CB1, MARIJUANA, STABILIZING ANTAGONIST AM6538, LIPIDIC KEYWDS 3 CUBIC PHASE, CB1-FLAVODOXIN CHIMERA, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.HUA,K.VEMURI,M.PU,L.QU,G.W.HAN,Y.WU,S.ZHAO,W.SHUI,S.LI,A.KORDE, AUTHOR 2 R.B.LAPRAIRIE,E.L.STAHL,J.H.HO,N.ZVONOK,H.ZHOU,I.KUFAREVA,B.WU, AUTHOR 3 Q.ZHAO,M.A.HANSON,L.M.BOHN,A.MAKRIYANNIS,R.C.STEVENS,Z.J.LIU REVDAT 2 19-FEB-20 5TGZ 1 AUTHOR REMARK REVDAT 1 02-NOV-16 5TGZ 0 JRNL AUTH T.HUA,K.VEMURI,M.PU,L.QU,G.W.HAN,Y.WU,S.ZHAO,W.SHUI,S.LI, JRNL AUTH 2 A.KORDE,R.B.LAPRAIRIE,E.L.STAHL,J.H.HO,N.ZVONOK,H.ZHOU, JRNL AUTH 3 I.KUFAREVA,B.WU,Q.ZHAO,M.A.HANSON,L.M.BOHN,A.MAKRIYANNIS, JRNL AUTH 4 R.C.STEVENS,Z.J.LIU JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN CANNABINOID RECEPTOR CB1. JRNL REF CELL V. 167 750 2016 JRNL REFN ISSN 1097-4172 JRNL PMID 27768894 JRNL DOI 10.1016/J.CELL.2016.10.004 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX DEV_2289 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.05 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 19827 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970 REMARK 3 FREE R VALUE TEST SET COUNT : 985 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 47.0517 - 5.3540 0.99 2823 153 0.1929 0.2207 REMARK 3 2 5.3540 - 4.2505 0.99 2765 138 0.1804 0.2233 REMARK 3 3 4.2505 - 3.7135 0.99 2744 152 0.2016 0.2243 REMARK 3 4 3.7135 - 3.3741 0.98 2677 150 0.2179 0.2562 REMARK 3 5 3.3741 - 3.1323 0.97 2671 128 0.2344 0.2490 REMARK 3 6 3.1323 - 2.9476 0.95 2603 136 0.2671 0.3161 REMARK 3 7 2.9476 - 2.8000 0.94 2559 128 0.2944 0.3116 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) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.730 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 3620 REMARK 3 ANGLE : 0.638 4904 REMARK 3 CHIRALITY : 0.040 558 REMARK 3 PLANARITY : 0.005 602 REMARK 3 DIHEDRAL : 20.316 1282 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 99:306) OR (RESID 1002:1148) REMARK 3 OR (RESID 332:412)) REMARK 3 ORIGIN FOR THE GROUP (A): 37.2354 23.2794 296.3046 REMARK 3 T TENSOR REMARK 3 T11: 0.5212 T22: 0.4552 REMARK 3 T33: 0.4798 T12: -0.0054 REMARK 3 T13: -0.0327 T23: 0.1377 REMARK 3 L TENSOR REMARK 3 L11: 0.9032 L22: 1.2386 REMARK 3 L33: 2.4083 L12: 0.2467 REMARK 3 L13: 0.5829 L23: 1.2853 REMARK 3 S TENSOR REMARK 3 S11: -0.1308 S12: -0.1669 S13: -0.0700 REMARK 3 S21: 0.2979 S22: 0.0936 S23: -0.0950 REMARK 3 S31: 0.0103 S32: 0.2053 S33: -0.0095 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2001:2001) REMARK 3 ORIGIN FOR THE GROUP (A): 43.8976 27.5518 318.1843 REMARK 3 T TENSOR REMARK 3 T11: 1.7067 T22: 1.2873 REMARK 3 T33: 1.2054 T12: -0.0933 REMARK 3 T13: -0.0136 T23: -0.1009 REMARK 3 L TENSOR REMARK 3 L11: 2.6694 L22: 8.3108 REMARK 3 L33: 0.4176 L12: -4.4787 REMARK 3 L13: 1.0441 L23: -1.6650 REMARK 3 S TENSOR REMARK 3 S11: 0.0276 S12: 0.0361 S13: 0.0855 REMARK 3 S21: -0.0615 S22: 0.0091 S23: -0.2088 REMARK 3 S31: 0.0674 S32: 0.0866 S33: -0.0252 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 5TGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-OCT-16. REMARK 100 THE DEPOSITION ID IS D_1000224224. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-MAY-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0-7.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : KB MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19837 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 47.050 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 8.100 REMARK 200 R MERGE (I) : 0.12600 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1 REMARK 200 DATA REDUNDANCY IN SHELL : 4.60 REMARK 200 R MERGE FOR SHELL (I) : 0.52000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100 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: 4Z34, 1I1O REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.0-7.4, 100MM REMARK 280 (NH4)2HPO4, 25%-32% PEG 400, 2-20 MM ETHYLENEDIAMINETETRAACETIC REMARK 280 ACID DISODIUM SALT DEHYDRATE (EDTA), LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 58.28000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.31500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.28000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.31500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -3 REMARK 465 PRO A 413 REMARK 465 SER A 414 REMARK 465 HIS A 415 REMARK 465 HIS A 416 REMARK 465 HIS A 417 REMARK 465 HIS A 418 REMARK 465 HIS A 419 REMARK 465 HIS A 420 REMARK 465 HIS A 421 REMARK 465 HIS A 422 REMARK 465 HIS A 423 REMARK 465 HIS A 424 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 MET A 109 CG SD CE REMARK 470 GLN A 115 CG CD OE1 NE2 REMARK 470 LEU A 117 CG CD1 CD2 REMARK 470 GLN A 261 CG CD OE1 NE2 REMARK 470 LYS A 370 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 185 -162.56 -73.98 REMARK 500 HIS A 270 -0.63 69.00 REMARK 500 ALA A1002 59.62 -116.45 REMARK 500 SER A1064 -141.37 -103.55 REMARK 500 REMARK 500 REMARK: NULL REMARK 600 REMARK 600 HETEROGEN REMARK 600 REMARK 600 THE NITRATE GROUP OF LIGAND ZDG BOUND TO THE CB1 STRUCTURE HAS NOT REMARK 600 BEEN MODELED DUE TO LACK OF ELECTRON DENSITY ON THE NITRATE GROUP. 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 ZDG A 2001 REMARK 610 OLC A 2003 REMARK 610 OLA A 2004 REMARK 610 OLA A 2005 REMARK 610 OLA A 2006 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZDG A 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue FMN A 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2006 DBREF 5TGZ A 99 306 UNP P21554 CNR1_HUMAN 99 306 DBREF 5TGZ A 1002 1148 UNP P00323 FLAV_DESVH 2 148 DBREF 5TGZ A 332 414 UNP P21554 CNR1_HUMAN 332 414 SEQADV 5TGZ GLY A -3 UNP P21554 EXPRESSION TAG SEQADV 5TGZ GLY A -2 UNP P21554 EXPRESSION TAG SEQADV 5TGZ GLY A -1 UNP P21554 EXPRESSION TAG SEQADV 5TGZ ARG A 0 UNP P21554 EXPRESSION TAG SEQADV 5TGZ ALA A 210 UNP P21554 THR 210 ENGINEERED MUTATION SEQADV 5TGZ LYS A 273 UNP P21554 GLU 273 ENGINEERED MUTATION SEQADV 5TGZ VAL A 283 UNP P21554 THR 283 ENGINEERED MUTATION SEQADV 5TGZ ALA A 1002 UNP P00323 PRO 2 ENGINEERED MUTATION SEQADV 5TGZ TRP A 1098 UNP P00323 TYR 98 ENGINEERED MUTATION SEQADV 5TGZ GLU A 340 UNP P21554 ARG 340 ENGINEERED MUTATION SEQADV 5TGZ HIS A 415 UNP P21554 EXPRESSION TAG SEQADV 5TGZ HIS A 416 UNP P21554 EXPRESSION TAG SEQADV 5TGZ HIS A 417 UNP P21554 EXPRESSION TAG SEQADV 5TGZ HIS A 418 UNP P21554 EXPRESSION TAG SEQADV 5TGZ HIS A 419 UNP P21554 EXPRESSION TAG SEQADV 5TGZ HIS A 420 UNP P21554 EXPRESSION TAG SEQADV 5TGZ HIS A 421 UNP P21554 EXPRESSION TAG SEQADV 5TGZ HIS A 422 UNP P21554 EXPRESSION TAG SEQADV 5TGZ HIS A 423 UNP P21554 EXPRESSION TAG SEQADV 5TGZ HIS A 424 UNP P21554 EXPRESSION TAG SEQRES 1 A 452 GLY GLY GLY ARG GLY GLU ASN PHE MET ASP ILE GLU CYS SEQRES 2 A 452 PHE MET VAL LEU ASN PRO SER GLN GLN LEU ALA ILE ALA SEQRES 3 A 452 VAL LEU SER LEU THR LEU GLY THR PHE THR VAL LEU GLU SEQRES 4 A 452 ASN LEU LEU VAL LEU CYS VAL ILE LEU HIS SER ARG SER SEQRES 5 A 452 LEU ARG CYS ARG PRO SER TYR HIS PHE ILE GLY SER LEU SEQRES 6 A 452 ALA VAL ALA ASP LEU LEU GLY SER VAL ILE PHE VAL TYR SEQRES 7 A 452 SER PHE ILE ASP PHE HIS VAL PHE HIS ARG LYS ASP SER SEQRES 8 A 452 ARG ASN VAL PHE LEU PHE LYS LEU GLY GLY VAL THR ALA SEQRES 9 A 452 SER PHE THR ALA SER VAL GLY SER LEU PHE LEU ALA ALA SEQRES 10 A 452 ILE ASP ARG TYR ILE SER ILE HIS ARG PRO LEU ALA TYR SEQRES 11 A 452 LYS ARG ILE VAL THR ARG PRO LYS ALA VAL VAL ALA PHE SEQRES 12 A 452 CYS LEU MET TRP THR ILE ALA ILE VAL ILE ALA VAL LEU SEQRES 13 A 452 PRO LEU LEU GLY TRP ASN CYS GLU LYS LEU GLN SER VAL SEQRES 14 A 452 CYS SER ASP ILE PHE PRO HIS ILE ASP LYS THR TYR LEU SEQRES 15 A 452 MET PHE TRP ILE GLY VAL VAL SER VAL LEU LEU LEU PHE SEQRES 16 A 452 ILE VAL TYR ALA TYR MET TYR ILE LEU TRP LYS ALA HIS SEQRES 17 A 452 SER HIS ALA VAL ALA LYS ALA LEU ILE VAL TYR GLY SER SEQRES 18 A 452 THR THR GLY ASN THR GLU TYR THR ALA GLU THR ILE ALA SEQRES 19 A 452 ARG GLU LEU ALA ASP ALA GLY TYR GLU VAL ASP SER ARG SEQRES 20 A 452 ASP ALA ALA SER VAL GLU ALA GLY GLY LEU PHE GLU GLY SEQRES 21 A 452 PHE ASP LEU VAL LEU LEU GLY CYS SER THR TRP GLY ASP SEQRES 22 A 452 ASP SER ILE GLU LEU GLN ASP ASP PHE ILE PRO LEU PHE SEQRES 23 A 452 ASP SER LEU GLU GLU THR GLY ALA GLN GLY ARG LYS VAL SEQRES 24 A 452 ALA CYS PHE GLY CYS GLY ASP SER SER TRP GLU TYR PHE SEQRES 25 A 452 CYS GLY ALA VAL ASP ALA ILE GLU GLU LYS LEU LYS ASN SEQRES 26 A 452 LEU GLY ALA GLU ILE VAL GLN ASP GLY LEU ARG ILE ASP SEQRES 27 A 452 GLY ASP PRO ARG ALA ALA ARG ASP ASP ILE VAL GLY TRP SEQRES 28 A 452 ALA HIS ASP VAL ARG GLY ALA ILE PRO ASP GLN ALA ARG SEQRES 29 A 452 MET ASP ILE GLU LEU ALA LYS THR LEU VAL LEU ILE LEU SEQRES 30 A 452 VAL VAL LEU ILE ILE CYS TRP GLY PRO LEU LEU ALA ILE SEQRES 31 A 452 MET VAL TYR ASP VAL PHE GLY LYS MET ASN LYS LEU ILE SEQRES 32 A 452 LYS THR VAL PHE ALA PHE CYS SER MET LEU CYS LEU LEU SEQRES 33 A 452 ASN SER THR VAL ASN PRO ILE ILE TYR ALA LEU ARG SER SEQRES 34 A 452 LYS ASP LEU ARG HIS ALA PHE ARG SER MET PHE PRO SER SEQRES 35 A 452 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HET ZDG A2001 33 HET FMN A2002 31 HET OLC A2003 19 HET OLA A2004 14 HET OLA A2005 9 HET OLA A2006 13 HET PEG A2007 7 HETNAM ZDG 4-[4-[2-(2,4-DICHLOROPHENYL)-4-METHYL-5-(PIPERIDIN-1- HETNAM 2 ZDG YLCARBAMOYL)PYRAZOL-3-YL]PHENYL]BUT-3-YNYL NITRATE HETNAM FMN FLAVIN MONONUCLEOTIDE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN FMN RIBOFLAVIN MONOPHOSPHATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 ZDG C26 H25 CL2 N5 O4 FORMUL 3 FMN C17 H21 N4 O9 P FORMUL 4 OLC C21 H40 O4 FORMUL 5 OLA 3(C18 H34 O2) FORMUL 8 PEG C4 H10 O3 FORMUL 9 HOH *9(H2 O) HELIX 1 AA1 PRO A 113 SER A 144 1 32 HELIX 2 AA2 SER A 144 CYS A 149 1 6 HELIX 3 AA3 SER A 152 HIS A 178 1 27 HELIX 4 AA4 SER A 185 ARG A 220 1 36 HELIX 5 AA5 ALA A 223 VAL A 228 1 6 HELIX 6 AA6 THR A 229 GLY A 254 1 26 HELIX 7 AA7 ASP A 272 ALA A 305 1 34 HELIX 8 AA8 GLY A 1013 ALA A 1029 1 17 HELIX 9 AA9 ALA A 1039 VAL A 1041 5 3 HELIX 10 AB1 PHE A 1071 SER A 1077 1 7 HELIX 11 AB2 LEU A 1078 THR A 1081 5 4 HELIX 12 AB3 CYS A 1102 LEU A 1115 1 14 HELIX 13 AB4 ASP A 1129 ALA A 1132 5 4 HELIX 14 AB5 ALA A 1133 GLY A 1146 1 14 HELIX 15 AB6 PRO A 332 PHE A 368 1 37 HELIX 16 AB7 ASN A 372 SER A 401 1 30 HELIX 17 AB8 SER A 401 MET A 411 1 11 SHEET 1 AA1 5 GLU A1032 ASP A1037 0 SHEET 2 AA1 5 LYS A1003 GLY A1009 1 N ILE A1006 O ARG A1036 SHEET 3 AA1 5 LEU A1052 CYS A1057 1 O LEU A1054 N LEU A1005 SHEET 4 AA1 5 LYS A1087 GLY A1094 1 O PHE A1091 N LEU A1055 SHEET 5 AA1 5 GLU A1118 ILE A1119 1 O GLU A1118 N VAL A1088 SHEET 1 AA2 5 GLU A1032 ASP A1037 0 SHEET 2 AA2 5 LYS A1003 GLY A1009 1 N ILE A1006 O ARG A1036 SHEET 3 AA2 5 LEU A1052 CYS A1057 1 O LEU A1054 N LEU A1005 SHEET 4 AA2 5 LYS A1087 GLY A1094 1 O PHE A1091 N LEU A1055 SHEET 5 AA2 5 LEU A1124 ASP A1127 1 O ILE A1126 N GLY A1094 SSBOND 1 CYS A 257 CYS A 264 1555 1555 2.04 CISPEP 1 GLY A -2 GLY A -1 0 9.86 CISPEP 2 ASN A 112 PRO A 113 0 -6.64 SITE 1 AC1 15 PHE A 102 MET A 103 ILE A 105 GLY A 166 SITE 2 AC1 15 PHE A 170 PHE A 174 LEU A 193 VAL A 196 SITE 3 AC1 15 THR A 197 LEU A 359 MET A 363 ALA A 380 SITE 4 AC1 15 SER A 383 CYS A 386 LEU A 387 SITE 1 AC2 17 SER A1010 THR A1011 THR A1012 GLY A1013 SITE 2 AC2 17 ASN A1014 THR A1015 SER A1058 THR A1059 SITE 3 AC2 17 TRP A1060 GLY A1061 CYS A1093 GLY A1094 SITE 4 AC2 17 ASP A1095 TRP A1098 TYR A1100 PHE A1101 SITE 5 AC2 17 CYS A1102 SITE 1 AC3 4 ARG A 226 TYR A1008 GLU A1016 ASP A1037 SITE 1 AC4 7 PRO A 151 SER A 152 ILE A 156 LEU A 209 SITE 2 AC4 7 ASP A 213 PHE A 237 LEU A 341 SITE 1 AC5 1 LEU A 209 CRYST1 116.560 52.630 143.630 90.00 111.14 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008579 0.000000 0.003317 0.00000 SCALE2 0.000000 0.019001 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007465 0.00000 ATOM 1 N GLY A -2 48.716 37.454 337.216 1.00131.71 N ANISOU 1 N GLY A -2 19357 18355 12331 1477 -3074 -119 N ATOM 2 CA GLY A -2 49.211 36.102 337.397 1.00138.20 C ANISOU 2 CA GLY A -2 20297 19162 13052 1584 -3159 19 C ATOM 3 C GLY A -2 50.725 36.062 337.484 1.00131.50 C ANISOU 3 C GLY A -2 19351 18374 12238 1695 -3401 -62 C ATOM 4 O GLY A -2 51.376 36.907 336.873 1.00140.64 O ANISOU 4 O GLY A -2 20297 19559 13582 1649 -3459 -194 O ATOM 5 N GLY A -1 51.313 35.092 338.190 1.00125.45 N ANISOU 5 N GLY A -1 18736 17630 11300 1837 -3550 7 N ATOM 6 CA GLY A -1 50.641 33.922 338.739 1.00124.67 C ANISOU 6 CA GLY A -1 18907 17470 10991 1879 -3489 188 C ATOM 7 C GLY A -1 51.108 32.685 337.995 1.00129.13 C ANISOU 7 C GLY A -1 19481 17947 11634 1963 -3549 310 C ATOM 8 O GLY A -1 52.284 32.575 337.650 1.00124.71 O ANISOU 8 O GLY A -1 18780 17423 11180 2066 -3732 235 O ATOM 9 N ARG A 0 50.194 31.742 337.753 1.00133.03 N ANISOU 9 N ARG A 0 20139 18333 12073 1919 -3397 485 N ATOM 10 CA ARG A 0 50.481 30.678 336.798 1.00124.49 C ANISOU 10 CA ARG A 0 19034 17150 11118 1971 -3416 592 C ATOM 11 C ARG A 0 50.650 31.227 335.392 1.00116.85 C ANISOU 11 C ARG A 0 17764 16173 10462 1890 -3345 515 C ATOM 12 O ARG A 0 51.224 30.548 334.535 1.00117.36 O ANISOU 12 O ARG A 0 17738 16190 10666 1950 -3406 546 O ATOM 13 CB ARG A 0 49.361 29.636 336.795 1.00122.81 C ANISOU 13 CB ARG A 0 19058 16818 10787 1907 -3244 789 C ATOM 14 CG ARG A 0 48.343 29.834 335.664 1.00109.02 C ANISOU 14 CG ARG A 0 17176 15011 9236 1743 -2996 823 C ATOM 15 CD ARG A 0 47.073 29.053 335.907 1.00115.44 C ANISOU 15 CD ARG A 0 18221 15746 9895 1643 -2800 981 C ATOM 16 NE ARG A 0 47.316 27.615 335.971 1.00134.26 N ANISOU 16 NE ARG A 0 20824 18015 12171 1730 -2878 1143 N ATOM 17 CZ ARG A 0 46.498 26.741 336.552 1.00145.06 C ANISOU 17 CZ ARG A 0 22483 19313 13319 1669 -2775 1294 C ATOM 18 NH1 ARG A 0 46.805 25.449 336.566 1.00139.76 N ANISOU 18 NH1 ARG A 0 22027 18516 12559 1755 -2871 1439 N ATOM 19 NH2 ARG A 0 45.376 27.154 337.130 1.00151.87 N ANISOU 19 NH2 ARG A 0 23429 20231 14043 1518 -2579 1294 N ATOM 20 N GLY A 99 50.139 32.428 335.132 1.00103.38 N ANISOU 20 N GLY A 99 15914 14505 8860 1755 -3220 415 N ATOM 21 CA GLY A 99 50.247 33.045 333.827 1.00102.33 C ANISOU 21 CA GLY A 99 15523 14355 9004 1660 -3151 344 C ATOM 22 C GLY A 99 49.003 32.889 332.981 1.00109.38 C ANISOU 22 C GLY A 99 16417 15149 9993 1534 -2914 443 C ATOM 23 O GLY A 99 48.447 31.793 332.869 1.00128.14 O ANISOU 23 O GLY A 99 18936 17444 12306 1545 -2834 594 O ATOM 24 N GLU A 100 48.549 33.990 332.391 1.00 86.45 N ANISOU 24 N GLU A 100 13364 12247 7238 1413 -2807 352 N ATOM 25 CA GLU A 100 47.502 33.960 331.375 1.00 97.16 C ANISOU 25 CA GLU A 100 14671 13516 8731 1301 -2606 415 C ATOM 26 C GLU A 100 48.200 33.788 330.031 1.00106.78 C ANISOU 26 C GLU A 100 15699 14692 10181 1287 -2639 412 C ATOM 27 O GLU A 100 48.749 34.744 329.478 1.00109.96 O ANISOU 27 O GLU A 100 15927 15122 10732 1230 -2684 291 O ATOM 28 CB GLU A 100 46.664 35.231 331.429 1.00 87.43 C ANISOU 28 CB GLU A 100 13391 12298 7532 1198 -2497 311 C ATOM 29 CG GLU A 100 45.830 35.369 332.697 1.00 83.62 C ANISOU 29 CG GLU A 100 13083 11869 6818 1201 -2434 305 C ATOM 30 CD GLU A 100 45.496 36.806 333.017 1.00 94.28 C ANISOU 30 CD GLU A 100 14371 13266 8186 1150 -2421 143 C ATOM 31 OE1 GLU A 100 46.344 37.687 332.759 1.00 96.37 O ANISOU 31 OE1 GLU A 100 14505 13544 8565 1145 -2541 26 O ATOM 32 OE2 GLU A 100 44.384 37.056 333.528 1.00 98.31 O ANISOU 32 OE2 GLU A 100 14963 13800 8591 1111 -2290 124 O ATOM 33 N ASN A 101 48.189 32.566 329.502 1.00 97.80 N ANISOU 33 N ASN A 101 14604 13488 9068 1329 -2615 540 N ATOM 34 CA ASN A 101 49.019 32.218 328.358 1.00105.27 C ANISOU 34 CA ASN A 101 15379 14415 10203 1345 -2673 531 C ATOM 35 C ASN A 101 48.183 31.616 327.240 1.00104.15 C ANISOU 35 C ASN A 101 15219 14168 10183 1273 -2504 642 C ATOM 36 O ASN A 101 47.215 30.891 327.491 1.00104.40 O ANISOU 36 O ASN A 101 15415 14137 10116 1264 -2388 764 O ATOM 37 CB ASN A 101 50.120 31.233 328.755 1.00113.03 C ANISOU 37 CB ASN A 101 16407 15429 11110 1507 -2863 551 C ATOM 38 CG ASN A 101 50.952 31.733 329.911 1.00115.84 C ANISOU 38 CG ASN A 101 16788 15894 11330 1593 -3044 440 C ATOM 39 OD1 ASN A 101 51.743 32.664 329.768 1.00117.33 O ANISOU 39 OD1 ASN A 101 16799 16171 11611 1564 -3131 288 O ATOM 40 ND2 ASN A 101 50.778 31.114 331.068 1.00115.20 N ANISOU 40 ND2 ASN A 101 16940 15810 11021 1691 -3103 515 N ATOM 41 N PHE A 102 48.581 31.918 326.006 1.00 98.65 N ANISOU 41 N PHE A 102 14325 13459 9696 1213 -2490 594 N ATOM 42 CA PHE A 102 47.901 31.390 324.833 1.00 88.85 C ANISOU 42 CA PHE A 102 13045 12126 8588 1147 -2345 685 C ATOM 43 C PHE A 102 48.098 29.882 324.751 1.00100.14 C ANISOU 43 C PHE A 102 14570 13504 9976 1252 -2379 806 C ATOM 44 O PHE A 102 49.193 29.369 324.994 1.00110.51 O ANISOU 44 O PHE A 102 15867 14859 11262 1373 -2547 779 O ATOM 45 CB PHE A 102 48.434 32.069 323.565 1.00 90.38 C ANISOU 45 CB PHE A 102 13015 12329 8998 1059 -2343 598 C ATOM 46 CG PHE A 102 47.513 31.965 322.373 1.00 91.64 C ANISOU 46 CG PHE A 102 13130 12395 9293 959 -2174 665 C ATOM 47 CD1 PHE A 102 46.158 32.216 322.502 1.00 89.75 C ANISOU 47 CD1 PHE A 102 12986 12100 9016 898 -2023 710 C ATOM 48 CD2 PHE A 102 48.010 31.639 321.118 1.00 91.52 C ANISOU 48 CD2 PHE A 102 12969 12361 9442 929 -2168 666 C ATOM 49 CE1 PHE A 102 45.311 32.128 321.412 1.00 87.70 C ANISOU 49 CE1 PHE A 102 12679 11762 8879 817 -1880 759 C ATOM 50 CE2 PHE A 102 47.165 31.550 320.019 1.00 88.15 C ANISOU 50 CE2 PHE A 102 12507 11851 9134 841 -2020 725 C ATOM 51 CZ PHE A 102 45.814 31.797 320.170 1.00 91.01 C ANISOU 51 CZ PHE A 102 12969 12153 9458 789 -1881 772 C ATOM 52 N MET A 103 47.020 29.172 324.420 1.00112.39 N ANISOU 52 N MET A 103 16223 14960 11518 1207 -2224 931 N ATOM 53 CA MET A 103 46.988 27.713 324.364 1.00120.19 C ANISOU 53 CA MET A 103 17346 15869 12453 1287 -2234 1062 C ATOM 54 C MET A 103 47.109 27.069 325.740 1.00119.22 C ANISOU 54 C MET A 103 17464 15746 12088 1391 -2332 1125 C ATOM 55 O MET A 103 47.543 25.918 325.848 1.00129.50 O ANISOU 55 O MET A 103 18885 16988 13331 1502 -2427 1206 O ATOM 56 CB MET A 103 48.083 27.157 323.444 1.00125.19 C ANISOU 56 CB MET A 103 17832 16502 13232 1366 -2349 1035 C ATOM 57 CG MET A 103 47.967 27.585 321.989 1.00136.02 C ANISOU 57 CG MET A 103 18990 17862 14828 1257 -2246 994 C ATOM 58 SD MET A 103 49.294 26.863 321.003 1.00141.12 S ANISOU 58 SD MET A 103 19463 18535 15622 1354 -2380 943 S ATOM 59 CE MET A 103 48.412 26.466 319.493 1.00133.88 C ANISOU 59 CE MET A 103 18476 17518 14876 1240 -2187 1023 C ATOM 60 N ASP A 104 46.734 27.782 326.802 1.00108.68 N ANISOU 60 N ASP A 104 16219 14471 10605 1361 -2317 1088 N ATOM 61 CA ASP A 104 46.699 27.216 328.147 1.00101.35 C ANISOU 61 CA ASP A 104 15546 13541 9420 1436 -2387 1155 C ATOM 62 C ASP A 104 45.239 26.927 328.486 1.00113.00 C ANISOU 62 C ASP A 104 17195 14969 10773 1314 -2177 1257 C ATOM 63 O ASP A 104 44.558 27.704 329.153 1.00119.73 O ANISOU 63 O ASP A 104 18077 15887 11529 1238 -2089 1206 O ATOM 64 CB ASP A 104 47.341 28.167 329.147 1.00102.25 C ANISOU 64 CB ASP A 104 15642 13772 9435 1486 -2521 1032 C ATOM 65 CG ASP A 104 47.592 27.514 330.484 1.00111.74 C ANISOU 65 CG ASP A 104 17105 14978 10375 1594 -2644 1095 C ATOM 66 OD1 ASP A 104 47.894 26.304 330.506 1.00119.56 O ANISOU 66 OD1 ASP A 104 18245 15882 11300 1691 -2725 1204 O ATOM 67 OD2 ASP A 104 47.484 28.213 331.512 1.00120.46 O ANISOU 67 OD2 ASP A 104 18276 16163 11330 1585 -2665 1034 O ATOM 68 N ILE A 105 44.762 25.776 328.016 1.00124.33 N ANISOU 68 N ILE A 105 18739 16292 12208 1293 -2096 1391 N ATOM 69 CA ILE A 105 43.349 25.426 328.126 1.00129.91 C ANISOU 69 CA ILE A 105 19577 16957 12827 1152 -1875 1478 C ATOM 70 C ILE A 105 43.158 24.553 329.362 1.00133.53 C ANISOU 70 C ILE A 105 20358 17379 12997 1170 -1901 1593 C ATOM 71 O ILE A 105 44.110 24.284 330.101 1.00144.52 O ANISOU 71 O ILE A 105 21869 18773 14267 1306 -2100 1601 O ATOM 72 CB ILE A 105 42.844 24.728 326.844 1.00132.56 C ANISOU 72 CB ILE A 105 19841 17193 13332 1088 -1753 1551 C ATOM 73 CG1 ILE A 105 43.563 25.275 325.607 1.00128.71 C ANISOU 73 CG1 ILE A 105 19072 16720 13112 1125 -1814 1459 C ATOM 74 CG2 ILE A 105 41.341 24.960 326.620 1.00135.73 C ANISOU 74 CG2 ILE A 105 20229 17604 13736 917 -1502 1558 C ATOM 75 CD1 ILE A 105 44.704 24.410 325.120 1.00135.78 C ANISOU 75 CD1 ILE A 105 19953 17557 14081 1262 -1983 1491 C ATOM 76 N GLU A 106 41.920 24.119 329.600 1.00120.28 N ANISOU 76 N GLU A 106 18828 15672 11200 1026 -1701 1674 N ATOM 77 CA GLU A 106 41.572 23.380 330.808 1.00130.68 C ANISOU 77 CA GLU A 106 20472 16962 12217 995 -1688 1783 C ATOM 78 C GLU A 106 42.124 21.956 330.813 1.00147.13 C ANISOU 78 C GLU A 106 22793 18890 14222 1085 -1814 1936 C ATOM 79 O GLU A 106 42.268 21.368 331.891 1.00128.08 O ANISOU 79 O GLU A 106 20676 16439 11551 1116 -1894 2023 O ATOM 80 CB GLU A 106 40.051 23.373 330.959 1.00124.91 C ANISOU 80 CB GLU A 106 19798 16266 11396 788 -1416 1804 C ATOM 81 CG GLU A 106 39.524 24.312 332.037 1.00128.65 C ANISOU 81 CG GLU A 106 20292 16890 11700 721 -1342 1704 C ATOM 82 CD GLU A 106 39.664 25.778 331.668 1.00119.61 C ANISOU 82 CD GLU A 106 18846 15858 10741 754 -1358 1521 C ATOM 83 OE1 GLU A 106 40.249 26.076 330.607 1.00120.35 O ANISOU 83 OE1 GLU A 106 18727 15916 11086 823 -1434 1478 O ATOM 84 OE2 GLU A 106 39.184 26.632 332.442 1.00117.60 O ANISOU 84 OE2 GLU A 106 18578 15728 10376 706 -1295 1418 O ATOM 85 N CYS A 107 42.426 21.398 329.644 1.00165.75 N ANISOU 85 N CYS A 107 25040 21151 16786 1130 -1839 1968 N ATOM 86 CA CYS A 107 43.149 20.132 329.497 1.00174.54 C ANISOU 86 CA CYS A 107 26334 22112 17870 1260 -2002 2081 C ATOM 87 C CYS A 107 42.698 19.081 330.515 1.00182.95 C ANISOU 87 C CYS A 107 27810 23068 18633 1211 -1990 2241 C ATOM 88 O CYS A 107 43.445 18.667 331.402 1.00195.90 O ANISOU 88 O CYS A 107 29637 24671 20124 1336 -2175 2272 O ATOM 89 CB CYS A 107 44.656 20.370 329.600 1.00172.29 C ANISOU 89 CB CYS A 107 25953 21865 17644 1488 -2284 1994 C ATOM 90 SG CYS A 107 45.214 21.024 331.202 1.00172.07 S ANISOU 90 SG CYS A 107 26063 21952 17365 1575 -2444 1935 S ATOM 91 N PHE A 108 41.450 18.641 330.370 1.00177.37 N ANISOU 91 N PHE A 108 27208 22315 17870 1006 -1750 2325 N ATOM 92 CA PHE A 108 40.979 17.476 331.113 1.00166.70 C ANISOU 92 CA PHE A 108 26198 20839 16301 913 -1698 2472 C ATOM 93 C PHE A 108 41.626 16.230 330.515 1.00159.46 C ANISOU 93 C PHE A 108 25329 19737 15521 1023 -1822 2543 C ATOM 94 O PHE A 108 41.443 15.944 329.327 1.00146.30 O ANISOU 94 O PHE A 108 23548 18006 14033 1010 -1768 2559 O ATOM 95 CB PHE A 108 39.455 17.362 331.052 1.00154.47 C ANISOU 95 CB PHE A 108 24723 19308 14659 645 -1397 2522 C ATOM 96 CG PHE A 108 38.704 18.484 331.742 1.00145.56 C ANISOU 96 CG PHE A 108 23519 18375 13413 518 -1243 2421 C ATOM 97 CD1 PHE A 108 39.273 19.732 331.958 1.00137.48 C ANISOU 97 CD1 PHE A 108 22266 17500 12469 630 -1340 2269 C ATOM 98 CD2 PHE A 108 37.406 18.274 332.175 1.00151.30 C ANISOU 98 CD2 PHE A 108 24375 19143 13967 274 -990 2456 C ATOM 99 CE1 PHE A 108 38.559 20.736 332.591 1.00141.86 C ANISOU 99 CE1 PHE A 108 22736 18229 12937 519 -1198 2158 C ATOM 100 CE2 PHE A 108 36.692 19.276 332.806 1.00153.62 C ANISOU 100 CE2 PHE A 108 24564 19631 14173 163 -842 2335 C ATOM 101 CZ PHE A 108 37.271 20.507 333.012 1.00148.07 C ANISOU 101 CZ PHE A 108 23642 19062 13555 295 -952 2186 C ATOM 102 N MET A 109 42.382 15.485 331.322 1.00158.88 N ANISOU 102 N MET A 109 25427 19576 15363 1138 -1993 2578 N ATOM 103 CA MET A 109 43.256 14.428 330.816 1.00152.23 C ANISOU 103 CA MET A 109 24612 18575 14654 1302 -2168 2605 C ATOM 104 C MET A 109 42.694 13.057 331.174 1.00154.09 C ANISOU 104 C MET A 109 25136 18626 14784 1187 -2091 2737 C ATOM 105 O MET A 109 42.676 12.675 332.348 1.00139.16 O ANISOU 105 O MET A 109 23483 16698 12692 1157 -2121 2786 O ATOM 106 CB MET A 109 44.670 14.590 331.372 1.00138.29 C ANISOU 106 CB MET A 109 22812 16841 12889 1551 -2453 2520 C ATOM 107 N VAL A 110 42.255 12.311 330.157 1.00171.55 N ANISOU 107 N VAL A 110 27333 20718 17128 1120 -1997 2790 N ATOM 108 CA VAL A 110 41.882 10.915 330.366 1.00175.25 C ANISOU 108 CA VAL A 110 28071 20990 17527 1036 -1959 2903 C ATOM 109 C VAL A 110 43.127 10.055 330.555 1.00191.11 C ANISOU 109 C VAL A 110 30187 22858 19567 1279 -2237 2895 C ATOM 110 O VAL A 110 43.159 9.174 331.423 1.00198.36 O ANISOU 110 O VAL A 110 31395 23645 20329 1266 -2293 2967 O ATOM 111 CB VAL A 110 41.016 10.409 329.196 1.00156.15 C ANISOU 111 CB VAL A 110 25591 18493 15245 887 -1773 2949 C ATOM 112 CG1 VAL A 110 40.785 8.901 329.294 1.00161.21 C ANISOU 112 CG1 VAL A 110 26501 18911 15839 826 -1770 3051 C ATOM 113 CG2 VAL A 110 39.676 11.121 329.175 1.00140.68 C ANISOU 113 CG2 VAL A 110 23569 16665 13218 628 -1487 2954 C ATOM 114 N LEU A 111 44.166 10.289 329.751 1.00192.54 N ANISOU 114 N LEU A 111 30143 23068 19946 1503 -2416 2798 N ATOM 115 CA LEU A 111 45.381 9.485 329.797 1.00190.72 C ANISOU 115 CA LEU A 111 29976 22721 19768 1751 -2683 2760 C ATOM 116 C LEU A 111 46.607 10.385 329.745 1.00187.88 C ANISOU 116 C LEU A 111 29366 22517 19503 1982 -2891 2612 C ATOM 117 O LEU A 111 46.605 11.416 329.067 1.00186.46 O ANISOU 117 O LEU A 111 28909 22493 19446 1975 -2838 2535 O ATOM 118 CB LEU A 111 45.441 8.484 328.634 1.00181.89 C ANISOU 118 CB LEU A 111 28836 21447 18826 1794 -2695 2778 C ATOM 119 CG LEU A 111 44.209 7.603 328.428 1.00170.27 C ANISOU 119 CG LEU A 111 27564 19828 17304 1554 -2479 2908 C ATOM 120 CD1 LEU A 111 44.284 6.856 327.106 1.00155.07 C ANISOU 120 CD1 LEU A 111 25548 17788 15585 1603 -2484 2901 C ATOM 121 CD2 LEU A 111 44.034 6.624 329.587 1.00177.11 C ANISOU 121 CD2 LEU A 111 28810 20534 17951 1498 -2514 3003 C ATOM 122 N ASN A 112 47.652 9.978 330.461 1.00185.73 N ANISOU 122 N ASN A 112 29197 22200 19172 2185 -3130 2564 N ATOM 123 CA ASN A 112 48.942 10.661 330.443 1.00180.96 C ANISOU 123 CA ASN A 112 28360 21736 18660 2421 -3352 2404 C ATOM 124 C ASN A 112 50.038 9.609 330.610 1.00180.72 C ANISOU 124 C ASN A 112 28441 21573 18650 2662 -3608 2354 C ATOM 125 O ASN A 112 49.769 8.522 331.116 1.00179.41 O ANISOU 125 O ASN A 112 28588 21215 18364 2635 -3622 2456 O ATOM 126 CB ASN A 112 49.034 11.705 331.561 1.00177.46 C ANISOU 126 CB ASN A 112 27913 21453 18061 2401 -3371 2364 C ATOM 127 CG ASN A 112 47.828 12.625 331.606 1.00173.68 C ANISOU 127 CG ASN A 112 27393 21084 17513 2153 -3113 2419 C ATOM 128 OD1 ASN A 112 46.740 12.220 332.015 1.00175.31 O ANISOU 128 OD1 ASN A 112 27821 21211 17578 1949 -2928 2546 O ATOM 129 ND2 ASN A 112 48.020 13.875 331.201 1.00167.35 N ANISOU 129 ND2 ASN A 112 26310 20471 16805 2168 -3103 2312 N ATOM 130 N PRO A 113 51.275 9.910 330.178 1.00181.69 N ANISOU 130 N PRO A 113 28313 21798 18922 2895 -3814 2187 N ATOM 131 CA PRO A 113 51.749 11.076 329.430 1.00178.81 C ANISOU 131 CA PRO A 113 27566 21652 18723 2943 -3825 2047 C ATOM 132 C PRO A 113 51.793 10.811 327.928 1.00179.43 C ANISOU 132 C PRO A 113 27433 21714 19030 2966 -3786 2008 C ATOM 133 O PRO A 113 52.214 11.679 327.162 1.00181.25 O ANISOU 133 O PRO A 113 27342 22113 19411 3005 -3800 1888 O ATOM 134 CB PRO A 113 53.152 11.285 329.989 1.00181.84 C ANISOU 134 CB PRO A 113 27847 22133 19109 3192 -4095 1881 C ATOM 135 CG PRO A 113 53.630 9.894 330.237 1.00184.31 C ANISOU 135 CG PRO A 113 28398 22246 19387 3346 -4254 1900 C ATOM 136 CD PRO A 113 52.407 9.078 330.626 1.00181.83 C ANISOU 136 CD PRO A 113 28442 21726 18921 3145 -4081 2110 C ATOM 137 N SER A 114 51.376 9.609 327.519 1.00178.68 N ANISOU 137 N SER A 114 27522 21416 18953 2939 -3742 2104 N ATOM 138 CA SER A 114 51.312 9.291 326.097 1.00173.93 C ANISOU 138 CA SER A 114 26742 20786 18557 2946 -3689 2079 C ATOM 139 C SER A 114 50.519 10.352 325.352 1.00180.29 C ANISOU 139 C SER A 114 27334 21723 19444 2761 -3478 2100 C ATOM 140 O SER A 114 50.961 10.870 324.321 1.00191.77 O ANISOU 140 O SER A 114 28489 23296 21079 2822 -3501 1992 O ATOM 141 CB SER A 114 50.677 7.917 325.889 1.00165.96 C ANISOU 141 CB SER A 114 26005 19531 17522 2880 -3623 2208 C ATOM 142 OG SER A 114 49.263 8.024 325.848 1.00154.59 O ANISOU 142 OG SER A 114 24682 18044 16012 2602 -3355 2362 O ATOM 143 N GLN A 115 49.331 10.680 325.862 1.00176.12 N ANISOU 143 N GLN A 115 26961 21178 18778 2530 -3269 2232 N ATOM 144 CA GLN A 115 48.565 11.787 325.308 1.00176.31 C ANISOU 144 CA GLN A 115 26803 21334 18854 2362 -3077 2240 C ATOM 145 C GLN A 115 49.426 13.040 325.230 1.00164.32 C ANISOU 145 C GLN A 115 24995 20033 17404 2472 -3195 2083 C ATOM 146 O GLN A 115 49.619 13.614 324.153 1.00161.00 O ANISOU 146 O GLN A 115 24309 19711 17155 2487 -3181 2004 O ATOM 147 CB GLN A 115 47.317 12.036 326.158 1.00180.41 C ANISOU 147 CB GLN A 115 27534 21837 19178 2126 -2868 2368 C ATOM 148 N GLN A 116 49.982 13.459 326.368 1.00153.91 N ANISOU 148 N GLN A 116 23729 18794 15956 2549 -3320 2030 N ATOM 149 CA GLN A 116 50.800 14.666 326.392 1.00150.48 C ANISOU 149 CA GLN A 116 23029 18573 15576 2638 -3434 1871 C ATOM 150 C GLN A 116 51.944 14.571 325.390 1.00147.49 C ANISOU 150 C GLN A 116 22370 18263 15405 2823 -3598 1716 C ATOM 151 O GLN A 116 52.221 15.525 324.654 1.00156.70 O ANISOU 151 O GLN A 116 23253 19590 16697 2816 -3596 1608 O ATOM 152 CB GLN A 116 51.341 14.904 327.799 1.00146.90 C ANISOU 152 CB GLN A 116 22692 18172 14951 2718 -3569 1831 C ATOM 153 CG GLN A 116 50.277 14.842 328.889 1.00155.11 C ANISOU 153 CG GLN A 116 24030 19141 15764 2545 -3420 1978 C ATOM 154 CD GLN A 116 50.335 16.011 329.857 1.00161.17 C ANISOU 154 CD GLN A 116 24765 20071 16402 2513 -3434 1918 C ATOM 155 OE1 GLN A 116 49.306 16.461 330.358 1.00161.57 O ANISOU 155 OE1 GLN A 116 24935 20140 16315 2330 -3256 2000 O ATOM 156 NE2 GLN A 116 51.540 16.500 330.136 1.00160.50 N ANISOU 156 NE2 GLN A 116 24513 20112 16356 2689 -3645 1761 N ATOM 157 N LEU A 117 52.620 13.422 325.343 1.00131.84 N ANISOU 157 N LEU A 117 20465 16169 13460 2987 -3744 1692 N ATOM 158 CA LEU A 117 53.730 13.255 324.412 1.00123.19 C ANISOU 158 CA LEU A 117 19098 15151 12557 3170 -3900 1524 C ATOM 159 C LEU A 117 53.229 13.101 322.979 1.00133.02 C ANISOU 159 C LEU A 117 20206 16365 13970 3091 -3768 1553 C ATOM 160 O LEU A 117 53.668 13.822 322.076 1.00133.06 O ANISOU 160 O LEU A 117 19901 16530 14126 3110 -3784 1428 O ATOM 161 CB LEU A 117 54.578 12.049 324.818 1.00 84.97 C ANISOU 161 CB LEU A 117 14396 10192 7695 3381 -4100 1477 C ATOM 162 N ALA A 118 52.297 12.172 322.755 1.00135.26 N ANISOU 162 N ALA A 118 20718 16447 14228 2989 -3633 1715 N ATOM 163 CA ALA A 118 51.880 11.850 321.394 1.00138.59 C ANISOU 163 CA ALA A 118 21026 16818 14812 2935 -3524 1739 C ATOM 164 C ALA A 118 51.057 12.976 320.776 1.00135.71 C ANISOU 164 C ALA A 118 20512 16558 14492 2746 -3334 1774 C ATOM 165 O ALA A 118 51.229 13.295 319.593 1.00127.49 O ANISOU 165 O ALA A 118 19187 15603 13649 2721 -3277 1685 O ATOM 166 CB ALA A 118 51.095 10.539 321.383 1.00137.81 C ANISOU 166 CB ALA A 118 21221 16474 14665 2866 -3431 1895 C ATOM 167 N ILE A 119 50.151 13.582 321.547 1.00127.90 N ANISOU 167 N ILE A 119 19670 15573 13353 2576 -3192 1877 N ATOM 168 CA ILE A 119 49.384 14.708 321.022 1.00108.80 C ANISOU 168 CA ILE A 119 17029 13272 11038 2347 -2948 1855 C ATOM 169 C ILE A 119 50.311 15.873 320.711 1.00104.32 C ANISOU 169 C ILE A 119 16098 12927 10611 2382 -3011 1658 C ATOM 170 O ILE A 119 50.101 16.611 319.741 1.00101.10 O ANISOU 170 O ILE A 119 15416 12615 10384 2245 -2859 1587 O ATOM 171 CB ILE A 119 48.271 15.120 322.006 1.00102.67 C ANISOU 171 CB ILE A 119 16466 12473 10071 2167 -2786 1974 C ATOM 172 CG1 ILE A 119 47.175 14.048 322.034 1.00 99.69 C ANISOU 172 CG1 ILE A 119 16395 11893 9590 2057 -2654 2158 C ATOM 173 CG2 ILE A 119 47.688 16.490 321.629 1.00102.56 C ANISOU 173 CG2 ILE A 119 16186 12614 10168 1969 -2579 1900 C ATOM 174 CD1 ILE A 119 46.017 14.345 322.974 1.00103.04 C ANISOU 174 CD1 ILE A 119 17031 12304 9815 1861 -2476 2267 C ATOM 175 N ALA A 120 51.351 16.059 321.525 1.00107.82 N ANISOU 175 N ALA A 120 16545 13456 10967 2558 -3239 1564 N ATOM 176 CA ALA A 120 52.257 17.181 321.314 1.00106.02 C ANISOU 176 CA ALA A 120 15980 13446 10855 2573 -3301 1368 C ATOM 177 C ALA A 120 52.989 17.047 319.985 1.00120.19 C ANISOU 177 C ALA A 120 17470 15316 12881 2622 -3328 1233 C ATOM 178 O ALA A 120 52.978 17.969 319.159 1.00129.56 O ANISOU 178 O ALA A 120 18374 16627 14227 2473 -3195 1142 O ATOM 179 CB ALA A 120 53.251 17.281 322.470 1.00 93.42 C ANISOU 179 CB ALA A 120 14456 11927 9113 2766 -3557 1286 C ATOM 180 N VAL A 121 53.632 15.899 319.758 1.00134.04 N ANISOU 180 N VAL A 121 19288 16994 14648 2831 -3504 1215 N ATOM 181 CA VAL A 121 54.322 15.675 318.489 1.00136.06 C ANISOU 181 CA VAL A 121 19256 17327 15115 2886 -3529 1077 C ATOM 182 C VAL A 121 53.322 15.700 317.341 1.00138.17 C ANISOU 182 C VAL A 121 19451 17529 15519 2674 -3266 1160 C ATOM 183 O VAL A 121 53.565 16.319 316.297 1.00132.95 O ANISOU 183 O VAL A 121 18483 16997 15034 2572 -3171 1046 O ATOM 184 CB VAL A 121 55.117 14.352 318.532 1.00134.29 C ANISOU 184 CB VAL A 121 19148 17012 14865 3172 -3779 1042 C ATOM 185 CG1 VAL A 121 54.204 13.154 318.808 1.00134.96 C ANISOU 185 CG1 VAL A 121 19629 16822 14828 3191 -3752 1262 C ATOM 186 CG2 VAL A 121 55.905 14.146 317.236 1.00127.53 C ANISOU 186 CG2 VAL A 121 17966 16266 14224 3238 -3811 867 C ATOM 187 N LEU A 122 52.171 15.054 317.527 1.00135.89 N ANISOU 187 N LEU A 122 19447 17044 15143 2592 -3143 1356 N ATOM 188 CA LEU A 122 51.154 15.020 316.482 1.00121.76 C ANISOU 188 CA LEU A 122 17602 15189 13473 2398 -2899 1434 C ATOM 189 C LEU A 122 50.706 16.427 316.107 1.00111.88 C ANISOU 189 C LEU A 122 16125 14076 12307 2177 -2708 1386 C ATOM 190 O LEU A 122 50.705 16.798 314.927 1.00120.38 O ANISOU 190 O LEU A 122 16958 15221 13559 2079 -2600 1316 O ATOM 191 CB LEU A 122 49.973 14.169 316.955 1.00121.74 C ANISOU 191 CB LEU A 122 17956 14970 13331 2330 -2800 1643 C ATOM 192 CG LEU A 122 48.628 14.258 316.230 1.00125.61 C ANISOU 192 CG LEU A 122 18444 15392 13889 2095 -2524 1746 C ATOM 193 CD1 LEU A 122 47.922 12.918 316.340 1.00118.67 C ANISOU 193 CD1 LEU A 122 17882 14288 12920 2101 -2499 1907 C ATOM 194 CD2 LEU A 122 47.739 15.359 316.808 1.00128.13 C ANISOU 194 CD2 LEU A 122 18770 15780 14134 1901 -2353 1784 C ATOM 195 N SER A 123 50.330 17.233 317.102 1.00103.86 N ANISOU 195 N SER A 123 15198 13100 11164 2099 -2673 1417 N ATOM 196 CA SER A 123 49.820 18.569 316.813 1.00105.01 C ANISOU 196 CA SER A 123 15168 13352 11379 1898 -2501 1375 C ATOM 197 C SER A 123 50.907 19.459 316.227 1.00106.88 C ANISOU 197 C SER A 123 15083 13773 11754 1904 -2572 1187 C ATOM 198 O SER A 123 50.642 20.255 315.319 1.00 97.91 O ANISOU 198 O SER A 123 13752 12699 10751 1745 -2431 1140 O ATOM 199 CB SER A 123 49.236 19.193 318.080 1.00100.58 C ANISOU 199 CB SER A 123 14780 12794 10640 1835 -2467 1434 C ATOM 200 OG SER A 123 48.102 18.468 318.524 1.00110.54 O ANISOU 200 OG SER A 123 16322 13904 11776 1776 -2357 1602 O ATOM 201 N LEU A 124 52.138 19.337 316.726 1.00 99.35 N ANISOU 201 N LEU A 124 14073 12911 10764 2080 -2791 1071 N ATOM 202 CA LEU A 124 53.230 20.137 316.183 1.00111.26 C ANISOU 202 CA LEU A 124 15265 14614 12396 2071 -2857 874 C ATOM 203 C LEU A 124 53.516 19.758 314.735 1.00124.04 C ANISOU 203 C LEU A 124 16675 16259 14197 2048 -2803 809 C ATOM 204 O LEU A 124 53.728 20.634 313.888 1.00111.60 O ANISOU 204 O LEU A 124 14858 14800 12747 1899 -2711 710 O ATOM 205 CB LEU A 124 54.484 19.963 317.038 1.00105.15 C ANISOU 205 CB LEU A 124 14470 13941 11539 2282 -3115 749 C ATOM 206 CG LEU A 124 55.708 20.764 316.589 1.00106.68 C ANISOU 206 CG LEU A 124 14328 14361 11846 2272 -3196 520 C ATOM 207 CD1 LEU A 124 55.437 22.259 316.663 1.00111.58 C ANISOU 207 CD1 LEU A 124 14842 15072 12483 2051 -3070 482 C ATOM 208 CD2 LEU A 124 56.925 20.400 317.420 1.00109.33 C ANISOU 208 CD2 LEU A 124 14645 14795 12100 2512 -3468 386 C ATOM 209 N THR A 125 53.525 18.457 314.433 1.00137.62 N ANISOU 209 N THR A 125 18497 17865 15927 2188 -2862 863 N ATOM 210 CA THR A 125 53.764 18.015 313.062 1.00124.51 C ANISOU 210 CA THR A 125 16648 16227 14434 2175 -2811 799 C ATOM 211 C THR A 125 52.652 18.484 312.133 1.00117.61 C ANISOU 211 C THR A 125 15737 15298 13651 1940 -2559 889 C ATOM 212 O THR A 125 52.918 18.927 311.010 1.00133.27 O ANISOU 212 O THR A 125 17481 17381 15776 1833 -2478 795 O ATOM 213 CB THR A 125 53.894 16.493 313.009 1.00122.01 C ANISOU 213 CB THR A 125 16489 15772 14098 2381 -2931 849 C ATOM 214 OG1 THR A 125 52.749 15.884 313.618 1.00131.25 O ANISOU 214 OG1 THR A 125 17995 16730 15145 2357 -2860 1060 O ATOM 215 CG2 THR A 125 55.158 16.046 313.724 1.00118.01 C ANISOU 215 CG2 THR A 125 15971 15340 13526 2641 -3209 718 C ATOM 216 N LEU A 126 51.399 18.388 312.581 1.00100.86 N ANISOU 216 N LEU A 126 13851 13027 11444 1854 -2434 1063 N ATOM 217 CA LEU A 126 50.290 18.899 311.784 1.00 93.94 C ANISOU 217 CA LEU A 126 12940 12108 10647 1643 -2206 1135 C ATOM 218 C LEU A 126 50.461 20.383 311.493 1.00 89.08 C ANISOU 218 C LEU A 126 12122 11632 10091 1484 -2138 1036 C ATOM 219 O LEU A 126 50.219 20.836 310.369 1.00100.33 O ANISOU 219 O LEU A 126 13394 13086 11640 1345 -2014 1008 O ATOM 220 CB LEU A 126 48.965 18.652 312.504 1.00 99.35 C ANISOU 220 CB LEU A 126 13897 12642 11209 1579 -2094 1308 C ATOM 221 CG LEU A 126 47.738 19.288 311.846 1.00 83.60 C ANISOU 221 CG LEU A 126 11868 10616 9279 1371 -1869 1367 C ATOM 222 CD1 LEU A 126 47.596 18.811 310.415 1.00 81.17 C ANISOU 222 CD1 LEU A 126 11433 10279 9127 1328 -1785 1359 C ATOM 223 CD2 LEU A 126 46.485 18.976 312.638 1.00 92.93 C ANISOU 223 CD2 LEU A 126 13304 11677 10329 1314 -1764 1512 C ATOM 224 N GLY A 127 50.873 21.157 312.497 1.00 99.61 N ANISOU 224 N GLY A 127 13468 13047 11333 1499 -2223 984 N ATOM 225 CA GLY A 127 51.018 22.590 312.300 1.00103.65 C ANISOU 225 CA GLY A 127 13820 13673 11891 1343 -2167 892 C ATOM 226 C GLY A 127 52.110 22.931 311.303 1.00102.22 C ANISOU 226 C GLY A 127 13361 13639 11840 1306 -2205 731 C ATOM 227 O GLY A 127 51.903 23.730 310.385 1.00115.36 O ANISOU 227 O GLY A 127 14897 15337 13599 1130 -2086 699 O ATOM 228 N THR A 128 53.290 22.328 311.469 1.00110.01 N ANISOU 228 N THR A 128 14254 14719 12826 1469 -2376 619 N ATOM 229 CA THR A 128 54.406 22.626 310.575 1.00123.84 C ANISOU 229 CA THR A 128 15720 16644 14691 1431 -2414 437 C ATOM 230 C THR A 128 54.123 22.157 309.153 1.00122.93 C ANISOU 230 C THR A 128 15508 16497 14704 1358 -2291 453 C ATOM 231 O THR A 128 54.606 22.767 308.192 1.00127.24 O ANISOU 231 O THR A 128 15838 17164 15345 1218 -2232 341 O ATOM 232 CB THR A 128 55.696 21.986 311.101 1.00120.75 C ANISOU 232 CB THR A 128 15243 16369 14268 1651 -2636 295 C ATOM 233 OG1 THR A 128 56.787 22.302 310.227 1.00126.49 O ANISOU 233 OG1 THR A 128 15666 17292 15101 1597 -2660 95 O ATOM 234 CG2 THR A 128 55.558 20.475 311.202 1.00103.49 C ANISOU 234 CG2 THR A 128 13211 14054 12057 1867 -2721 375 C ATOM 235 N PHE A 129 53.351 21.080 308.998 1.00105.07 N ANISOU 235 N PHE A 129 13408 14075 12439 1441 -2251 589 N ATOM 236 CA PHE A 129 52.939 20.654 307.665 1.00 99.82 C ANISOU 236 CA PHE A 129 12671 13367 11891 1364 -2124 615 C ATOM 237 C PHE A 129 52.101 21.730 306.990 1.00102.60 C ANISOU 237 C PHE A 129 12993 13698 12291 1122 -1938 665 C ATOM 238 O PHE A 129 52.266 22.003 305.795 1.00106.33 O ANISOU 238 O PHE A 129 13302 14233 12866 1000 -1854 604 O ATOM 239 CB PHE A 129 52.155 19.345 307.755 1.00 96.78 C ANISOU 239 CB PHE A 129 12498 12795 11480 1483 -2113 761 C ATOM 240 CG PHE A 129 51.589 18.881 306.441 1.00 99.31 C ANISOU 240 CG PHE A 129 12766 13054 11912 1403 -1977 801 C ATOM 241 CD1 PHE A 129 52.358 18.910 305.290 1.00104.58 C ANISOU 241 CD1 PHE A 129 13188 13851 12695 1368 -1969 663 C ATOM 242 CD2 PHE A 129 50.291 18.402 306.361 1.00107.95 C ANISOU 242 CD2 PHE A 129 14052 13972 12991 1356 -1854 967 C ATOM 243 CE1 PHE A 129 51.839 18.480 304.079 1.00113.93 C ANISOU 243 CE1 PHE A 129 14330 14983 13977 1296 -1847 697 C ATOM 244 CE2 PHE A 129 49.765 17.969 305.153 1.00102.64 C ANISOU 244 CE2 PHE A 129 13329 13246 12421 1285 -1734 996 C ATOM 245 CZ PHE A 129 50.541 18.008 304.012 1.00102.76 C ANISOU 245 CZ PHE A 129 13111 13384 12550 1260 -1734 865 C ATOM 246 N THR A 130 51.203 22.360 307.749 1.00106.37 N ANISOU 246 N THR A 130 13635 14091 12689 1055 -1879 769 N ATOM 247 CA THR A 130 50.341 23.401 307.198 1.00103.97 C ANISOU 247 CA THR A 130 13329 13752 12423 852 -1724 812 C ATOM 248 C THR A 130 51.157 24.605 306.752 1.00 97.47 C ANISOU 248 C THR A 130 12318 13072 11644 709 -1732 674 C ATOM 249 O THR A 130 50.950 25.143 305.658 1.00 78.23 O ANISOU 249 O THR A 130 9795 10643 9287 550 -1627 660 O ATOM 250 CB THR A 130 49.310 23.832 308.240 1.00103.95 C ANISOU 250 CB THR A 130 13529 13652 12316 835 -1682 919 C ATOM 251 OG1 THR A 130 48.836 22.688 308.962 1.00103.85 O ANISOU 251 OG1 THR A 130 13702 13534 12223 975 -1710 1027 O ATOM 252 CG2 THR A 130 48.137 24.538 307.571 1.00 95.82 C ANISOU 252 CG2 THR A 130 12530 12546 11333 672 -1520 983 C ATOM 253 N VAL A 131 52.079 25.055 307.605 1.00 96.74 N ANISOU 253 N VAL A 131 12174 13092 11493 754 -1859 572 N ATOM 254 CA VAL A 131 52.900 26.217 307.278 1.00102.37 C ANISOU 254 CA VAL A 131 12717 13944 12235 601 -1869 433 C ATOM 255 C VAL A 131 53.650 25.987 305.973 1.00114.49 C ANISOU 255 C VAL A 131 14037 15590 13875 529 -1839 326 C ATOM 256 O VAL A 131 53.746 26.884 305.127 1.00125.95 O ANISOU 256 O VAL A 131 15396 17086 15372 324 -1754 278 O ATOM 257 CB VAL A 131 53.865 26.531 308.437 1.00 98.05 C ANISOU 257 CB VAL A 131 12133 13515 11608 687 -2027 323 C ATOM 258 CG1 VAL A 131 54.754 27.725 308.091 1.00 88.16 C ANISOU 258 CG1 VAL A 131 10699 12413 10384 505 -2034 167 C ATOM 259 CG2 VAL A 131 53.088 26.799 309.722 1.00 97.87 C ANISOU 259 CG2 VAL A 131 12329 13388 11471 746 -2048 428 C ATOM 260 N LEU A 132 54.193 24.784 305.788 1.00105.59 N ANISOU 260 N LEU A 132 12837 14505 12776 694 -1911 283 N ATOM 261 CA LEU A 132 54.957 24.499 304.580 1.00 98.12 C ANISOU 261 CA LEU A 132 11670 13687 11924 640 -1885 160 C ATOM 262 C LEU A 132 54.048 24.370 303.365 1.00101.56 C ANISOU 262 C LEU A 132 12138 14017 12431 520 -1723 260 C ATOM 263 O LEU A 132 54.370 24.886 302.288 1.00125.71 O ANISOU 263 O LEU A 132 15054 17163 15547 343 -1641 185 O ATOM 264 CB LEU A 132 55.785 23.230 304.776 1.00110.59 C ANISOU 264 CB LEU A 132 13167 15338 13514 880 -2028 70 C ATOM 265 CG LEU A 132 56.929 23.350 305.786 1.00110.12 C ANISOU 265 CG LEU A 132 13016 15429 13395 1005 -2209 -80 C ATOM 266 CD1 LEU A 132 57.575 21.994 306.014 1.00109.48 C ANISOU 266 CD1 LEU A 132 12901 15377 13318 1281 -2368 -150 C ATOM 267 CD2 LEU A 132 57.963 24.367 305.316 1.00 95.93 C ANISOU 267 CD2 LEU A 132 10964 13855 11630 819 -2198 -277 C ATOM 268 N GLU A 133 52.906 23.697 303.513 1.00 86.27 N ANISOU 268 N GLU A 133 10394 11898 10485 602 -1672 426 N ATOM 269 CA GLU A 133 52.047 23.481 302.356 1.00 81.90 C ANISOU 269 CA GLU A 133 9864 11252 10003 506 -1529 510 C ATOM 270 C GLU A 133 51.353 24.770 301.932 1.00 97.73 C ANISOU 270 C GLU A 133 11914 13211 12009 286 -1413 557 C ATOM 271 O GLU A 133 51.101 24.969 300.738 1.00116.07 O ANISOU 271 O GLU A 133 14181 15528 14393 151 -1311 560 O ATOM 272 CB GLU A 133 51.032 22.373 302.650 1.00 71.70 C ANISOU 272 CB GLU A 133 8759 9787 8698 646 -1508 660 C ATOM 273 CG GLU A 133 49.748 22.825 303.318 1.00 92.02 C ANISOU 273 CG GLU A 133 11539 12214 11209 602 -1437 805 C ATOM 274 CD GLU A 133 48.778 21.679 303.545 1.00104.93 C ANISOU 274 CD GLU A 133 13347 13695 12826 710 -1401 939 C ATOM 275 OE1 GLU A 133 48.346 21.475 304.697 1.00116.45 O ANISOU 275 OE1 GLU A 133 14975 15081 14191 791 -1439 1016 O ATOM 276 OE2 GLU A 133 48.451 20.975 302.568 1.00104.17 O ANISOU 276 OE2 GLU A 133 13223 13553 12805 703 -1333 965 O ATOM 277 N ASN A 134 51.047 25.661 302.879 1.00 92.10 N ANISOU 277 N ASN A 134 11310 12461 11225 252 -1436 589 N ATOM 278 CA ASN A 134 50.536 26.975 302.508 1.00 83.10 C ANISOU 278 CA ASN A 134 10211 11279 10082 55 -1356 608 C ATOM 279 C ASN A 134 51.655 27.886 302.027 1.00107.71 C ANISOU 279 C ASN A 134 13167 14545 13211 -111 -1376 464 C ATOM 280 O ASN A 134 51.414 28.775 301.203 1.00128.75 O ANISOU 280 O ASN A 134 15839 17184 15895 -304 -1297 467 O ATOM 281 CB ASN A 134 49.798 27.623 303.681 1.00 92.36 C ANISOU 281 CB ASN A 134 11557 12361 11175 80 -1376 678 C ATOM 282 CG ASN A 134 48.328 27.255 303.715 1.00 93.43 C ANISOU 282 CG ASN A 134 11856 12336 11306 123 -1287 820 C ATOM 283 OD1 ASN A 134 47.531 27.767 302.927 1.00 86.31 O ANISOU 283 OD1 ASN A 134 10992 11359 10443 11 -1194 863 O ATOM 284 ND2 ASN A 134 47.959 26.367 304.629 1.00 87.36 N ANISOU 284 ND2 ASN A 134 11191 11517 10483 281 -1318 888 N ATOM 285 N LEU A 135 52.877 27.681 302.521 1.00115.38 N ANISOU 285 N LEU A 135 13999 15674 14165 -45 -1484 333 N ATOM 286 CA LEU A 135 54.027 28.363 301.940 1.00113.07 C ANISOU 286 CA LEU A 135 13516 15555 13889 -214 -1490 173 C ATOM 287 C LEU A 135 54.284 27.876 300.521 1.00105.73 C ANISOU 287 C LEU A 135 12449 14690 13033 -295 -1406 129 C ATOM 288 O LEU A 135 54.765 28.640 299.676 1.00 97.73 O ANISOU 288 O LEU A 135 11340 13764 12030 -517 -1344 48 O ATOM 289 CB LEU A 135 55.262 28.144 302.820 1.00101.64 C ANISOU 289 CB LEU A 135 11930 14280 12409 -100 -1633 22 C ATOM 290 CG LEU A 135 56.550 28.912 302.505 1.00100.56 C ANISOU 290 CG LEU A 135 11581 14354 12272 -274 -1656 -175 C ATOM 291 CD1 LEU A 135 56.279 30.390 302.265 1.00105.68 C ANISOU 291 CD1 LEU A 135 12312 14951 12892 -542 -1581 -155 C ATOM 292 CD2 LEU A 135 57.542 28.742 303.651 1.00100.26 C ANISOU 292 CD2 LEU A 135 11445 14459 12190 -125 -1817 -308 C ATOM 293 N LEU A 136 53.959 26.612 300.241 1.00 87.81 N ANISOU 293 N LEU A 136 10182 12375 10808 -129 -1400 181 N ATOM 294 CA LEU A 136 54.107 26.082 298.891 1.00 88.91 C ANISOU 294 CA LEU A 136 10199 12566 11016 -191 -1318 144 C ATOM 295 C LEU A 136 53.125 26.744 297.932 1.00107.47 C ANISOU 295 C LEU A 136 12661 14791 13381 -381 -1181 253 C ATOM 296 O LEU A 136 53.480 27.058 296.789 1.00116.66 O ANISOU 296 O LEU A 136 13722 16035 14569 -558 -1104 190 O ATOM 297 CB LEU A 136 53.905 24.566 298.910 1.00 94.65 C ANISOU 297 CB LEU A 136 10934 13245 11784 45 -1355 181 C ATOM 298 CG LEU A 136 54.142 23.795 297.609 1.00 89.95 C ANISOU 298 CG LEU A 136 10200 12714 11263 31 -1292 123 C ATOM 299 CD1 LEU A 136 55.595 23.895 297.177 1.00 88.49 C ANISOU 299 CD1 LEU A 136 9748 12782 11094 -29 -1331 -100 C ATOM 300 CD2 LEU A 136 53.736 22.337 297.775 1.00 78.28 C ANISOU 300 CD2 LEU A 136 8790 11133 9818 272 -1337 189 C ATOM 301 N VAL A 137 51.886 26.964 298.377 1.00105.25 N ANISOU 301 N VAL A 137 12590 14321 13080 -345 -1153 408 N ATOM 302 CA VAL A 137 50.902 27.647 297.541 1.00 89.42 C ANISOU 302 CA VAL A 137 10701 12191 11085 -501 -1046 503 C ATOM 303 C VAL A 137 51.352 29.075 297.264 1.00 90.17 C ANISOU 303 C VAL A 137 10791 12330 11140 -737 -1033 441 C ATOM 304 O VAL A 137 51.289 29.557 296.127 1.00 87.27 O ANISOU 304 O VAL A 137 10419 11957 10782 -920 -955 438 O ATOM 305 CB VAL A 137 49.514 27.609 298.210 1.00 89.51 C ANISOU 305 CB VAL A 137 10919 12014 11078 -399 -1032 653 C ATOM 306 CG1 VAL A 137 48.477 28.333 297.360 1.00 93.53 C ANISOU 306 CG1 VAL A 137 11543 12397 11599 -535 -941 733 C ATOM 307 CG2 VAL A 137 49.079 26.169 298.450 1.00 83.76 C ANISOU 307 CG2 VAL A 137 10212 11235 10379 -196 -1035 716 C ATOM 308 N LEU A 138 51.818 29.773 298.304 1.00108.17 N ANISOU 308 N LEU A 138 13086 14647 13366 -743 -1113 391 N ATOM 309 CA LEU A 138 52.335 31.125 298.123 1.00116.26 C ANISOU 309 CA LEU A 138 14114 15713 14348 -976 -1111 321 C ATOM 310 C LEU A 138 53.481 31.161 297.120 1.00129.12 C ANISOU 310 C LEU A 138 15547 17525 15989 -1152 -1071 184 C ATOM 311 O LEU A 138 53.685 32.180 296.449 1.00128.17 O ANISOU 311 O LEU A 138 15456 17406 15835 -1400 -1021 157 O ATOM 312 CB LEU A 138 52.809 31.693 299.462 1.00119.07 C ANISOU 312 CB LEU A 138 14484 16109 14647 -933 -1214 264 C ATOM 313 CG LEU A 138 51.857 32.593 300.255 1.00115.65 C ANISOU 313 CG LEU A 138 14267 15507 14167 -926 -1237 357 C ATOM 314 CD1 LEU A 138 51.670 33.935 299.561 1.00114.58 C ANISOU 314 CD1 LEU A 138 14238 15291 14008 -1173 -1195 362 C ATOM 315 CD2 LEU A 138 50.516 31.916 300.489 1.00108.07 C ANISOU 315 CD2 LEU A 138 13445 14391 13225 -749 -1206 501 C ATOM 316 N CYS A 139 54.242 30.071 297.007 1.00138.44 N ANISOU 316 N CYS A 139 16532 18861 17209 -1032 -1094 89 N ATOM 317 CA CYS A 139 55.424 30.076 296.151 1.00140.15 C ANISOU 317 CA CYS A 139 16527 19291 17433 -1191 -1058 -77 C ATOM 318 C CYS A 139 55.039 30.007 294.678 1.00128.63 C ANISOU 318 C CYS A 139 15078 17800 15996 -1340 -934 -34 C ATOM 319 O CYS A 139 55.455 30.851 293.875 1.00132.23 O ANISOU 319 O CYS A 139 15512 18318 16413 -1610 -865 -90 O ATOM 320 CB CYS A 139 56.338 28.906 296.520 1.00145.37 C ANISOU 320 CB CYS A 139 16972 20131 18132 -983 -1139 -210 C ATOM 321 SG CYS A 139 58.110 29.265 296.390 1.00151.84 S ANISOU 321 SG CYS A 139 17489 21274 18930 -1136 -1170 -486 S ATOM 322 N VAL A 140 54.238 29.006 294.304 1.00109.80 N ANISOU 322 N VAL A 140 12738 15315 13666 -1178 -903 66 N ATOM 323 CA VAL A 140 53.914 28.787 292.897 1.00110.53 C ANISOU 323 CA VAL A 140 12822 15394 13782 -1293 -793 94 C ATOM 324 C VAL A 140 53.185 29.985 292.305 1.00111.32 C ANISOU 324 C VAL A 140 13119 15346 13833 -1516 -728 196 C ATOM 325 O VAL A 140 53.283 30.247 291.099 1.00114.71 O ANISOU 325 O VAL A 140 13535 15806 14245 -1711 -640 180 O ATOM 326 CB VAL A 140 53.091 27.493 292.739 1.00109.17 C ANISOU 326 CB VAL A 140 12681 15120 13677 -1064 -784 188 C ATOM 327 CG1 VAL A 140 53.925 26.289 293.140 1.00111.22 C ANISOU 327 CG1 VAL A 140 12753 15524 13981 -856 -858 72 C ATOM 328 CG2 VAL A 140 51.811 27.561 293.563 1.00109.05 C ANISOU 328 CG2 VAL A 140 12892 14883 13661 -929 -812 357 C ATOM 329 N ILE A 141 52.451 30.734 293.128 1.00107.90 N ANISOU 329 N ILE A 141 12879 14748 13369 -1489 -774 295 N ATOM 330 CA ILE A 141 51.720 31.893 292.621 1.00103.73 C ANISOU 330 CA ILE A 141 12559 14059 12794 -1672 -738 386 C ATOM 331 C ILE A 141 52.684 33.038 292.329 1.00 99.55 C ANISOU 331 C ILE A 141 12009 13623 12192 -1959 -727 286 C ATOM 332 O ILE A 141 52.733 33.563 291.212 1.00100.03 O ANISOU 332 O ILE A 141 12122 13672 12211 -2185 -656 290 O ATOM 333 CB ILE A 141 50.621 32.316 293.611 1.00 94.76 C ANISOU 333 CB ILE A 141 11627 12727 11651 -1536 -797 503 C ATOM 334 CG1 ILE A 141 49.575 31.203 293.711 1.00 80.86 C ANISOU 334 CG1 ILE A 141 9899 10873 9953 -1301 -782 603 C ATOM 335 CG2 ILE A 141 49.977 33.635 293.175 1.00 99.32 C ANISOU 335 CG2 ILE A 141 12424 13140 12175 -1714 -789 570 C ATOM 336 CD1 ILE A 141 48.418 31.493 294.637 1.00 70.12 C ANISOU 336 CD1 ILE A 141 8717 9343 8583 -1167 -822 705 C ATOM 337 N LEU A 142 53.460 33.446 293.335 1.00116.64 N ANISOU 337 N LEU A 142 14108 15881 14331 -1964 -798 194 N ATOM 338 CA LEU A 142 54.442 34.505 293.121 1.00119.35 C ANISOU 338 CA LEU A 142 14417 16328 14602 -2253 -786 83 C ATOM 339 C LEU A 142 55.502 34.088 292.110 1.00138.60 C ANISOU 339 C LEU A 142 16628 18997 17036 -2415 -704 -57 C ATOM 340 O LEU A 142 56.079 34.944 291.429 1.00132.81 O ANISOU 340 O LEU A 142 15906 18325 16232 -2720 -645 -120 O ATOM 341 CB LEU A 142 55.112 34.887 294.441 1.00108.66 C ANISOU 341 CB LEU A 142 13004 15054 13229 -2204 -884 -8 C ATOM 342 CG LEU A 142 54.215 35.368 295.583 1.00118.56 C ANISOU 342 CG LEU A 142 14462 16113 14474 -2055 -969 100 C ATOM 343 CD1 LEU A 142 55.059 35.818 296.769 1.00120.29 C ANISOU 343 CD1 LEU A 142 14606 16440 14660 -2050 -1060 -14 C ATOM 344 CD2 LEU A 142 53.292 36.492 295.135 1.00127.99 C ANISOU 344 CD2 LEU A 142 15931 17077 15623 -2203 -950 216 C ATOM 345 N HIS A 143 55.778 32.787 292.006 1.00160.82 N ANISOU 345 N HIS A 143 19242 21944 19920 -2222 -699 -115 N ATOM 346 CA HIS A 143 56.810 32.312 291.089 1.00178.60 C ANISOU 346 CA HIS A 143 21248 24440 22172 -2348 -626 -275 C ATOM 347 C HIS A 143 56.411 32.528 289.634 1.00176.67 C ANISOU 347 C HIS A 143 21093 24141 21893 -2557 -506 -213 C ATOM 348 O HIS A 143 57.216 33.020 288.833 1.00186.57 O ANISOU 348 O HIS A 143 22260 25545 23082 -2843 -426 -324 O ATOM 349 CB HIS A 143 57.099 30.832 291.348 1.00192.98 C ANISOU 349 CB HIS A 143 22860 26384 24079 -2054 -670 -348 C ATOM 350 CG HIS A 143 57.630 30.099 290.153 1.00205.73 C ANISOU 350 CG HIS A 143 24279 28175 25715 -2117 -582 -458 C ATOM 351 ND1 HIS A 143 58.949 30.174 289.757 1.00210.65 N ANISOU 351 ND1 HIS A 143 24646 29083 26310 -2286 -546 -680 N ATOM 352 CD2 HIS A 143 57.019 29.274 289.269 1.00206.60 C ANISOU 352 CD2 HIS A 143 24404 28226 25870 -2036 -521 -388 C ATOM 353 CE1 HIS A 143 59.127 29.428 288.681 1.00210.86 C ANISOU 353 CE1 HIS A 143 24537 29221 26360 -2301 -465 -744 C ATOM 354 NE2 HIS A 143 57.972 28.871 288.365 1.00207.59 N ANISOU 354 NE2 HIS A 143 24288 28595 25991 -2149 -452 -566 N ATOM 355 N SER A 144 55.182 32.171 289.273 1.00166.52 N ANISOU 355 N SER A 144 19978 22649 20642 -2429 -491 -45 N ATOM 356 CA SER A 144 54.750 32.179 287.883 1.00161.22 C ANISOU 356 CA SER A 144 19382 21928 19945 -2579 -390 14 C ATOM 357 C SER A 144 53.933 33.430 287.590 1.00158.20 C ANISOU 357 C SER A 144 19307 21314 19487 -2756 -386 154 C ATOM 358 O SER A 144 53.098 33.849 288.398 1.00160.01 O ANISOU 358 O SER A 144 19719 21348 19728 -2630 -463 265 O ATOM 359 CB SER A 144 53.930 30.927 287.555 1.00147.11 C ANISOU 359 CB SER A 144 17577 20073 18246 -2326 -378 93 C ATOM 360 OG SER A 144 52.570 31.086 287.924 1.00129.46 O ANISOU 360 OG SER A 144 15577 17578 16032 -2185 -418 272 O ATOM 361 N ARG A 145 54.182 34.018 286.419 1.00151.41 N ANISOU 361 N ARG A 145 18509 20479 18543 -3048 -299 142 N ATOM 362 CA ARG A 145 53.513 35.246 286.012 1.00138.12 C ANISOU 362 CA ARG A 145 17137 18573 16770 -3240 -306 264 C ATOM 363 C ARG A 145 52.138 34.976 285.416 1.00128.51 C ANISOU 363 C ARG A 145 16107 17138 15580 -3102 -309 425 C ATOM 364 O ARG A 145 51.264 35.849 285.457 1.00138.18 O ANISOU 364 O ARG A 145 17607 18130 16766 -3124 -364 544 O ATOM 365 CB ARG A 145 54.396 35.983 285.011 1.00135.85 C ANISOU 365 CB ARG A 145 16856 18399 16360 -3629 -215 184 C ATOM 366 CG ARG A 145 53.930 37.368 284.598 1.00139.87 C ANISOU 366 CG ARG A 145 17709 18682 16752 -3874 -233 293 C ATOM 367 CD ARG A 145 54.853 37.923 283.518 1.00141.05 C ANISOU 367 CD ARG A 145 17857 18968 16769 -4278 -122 210 C ATOM 368 NE ARG A 145 56.263 37.701 283.843 1.00141.85 N ANISOU 368 NE ARG A 145 17649 19380 16869 -4402 -68 4 N ATOM 369 CZ ARG A 145 56.980 36.648 283.449 1.00137.48 C ANISOU 369 CZ ARG A 145 16775 19102 16360 -4360 12 -139 C ATOM 370 NH1 ARG A 145 58.252 36.543 283.808 1.00128.51 N ANISOU 370 NH1 ARG A 145 15359 18250 15220 -4466 43 -344 N ATOM 371 NH2 ARG A 145 56.436 35.696 282.701 1.00138.02 N ANISOU 371 NH2 ARG A 145 16796 19168 16480 -4208 54 -91 N ATOM 372 N SER A 146 51.930 33.782 284.861 1.00109.37 N ANISOU 372 N SER A 146 13539 14791 13226 -2954 -257 420 N ATOM 373 CA SER A 146 50.632 33.422 284.310 1.00110.19 C ANISOU 373 CA SER A 146 13793 14711 13365 -2813 -258 556 C ATOM 374 C SER A 146 49.539 33.362 285.370 1.00125.06 C ANISOU 374 C SER A 146 15792 16407 15317 -2544 -352 659 C ATOM 375 O SER A 146 48.359 33.282 285.012 1.00119.69 O ANISOU 375 O SER A 146 15261 15556 14658 -2439 -365 768 O ATOM 376 CB SER A 146 50.735 32.072 283.598 1.00114.77 C ANISOU 376 CB SER A 146 14168 15427 14011 -2704 -186 509 C ATOM 377 OG SER A 146 51.144 31.058 284.499 1.00124.34 O ANISOU 377 OG SER A 146 15161 16762 15319 -2474 -216 434 O ATOM 378 N LEU A 147 49.895 33.401 286.652 1.00127.76 N ANISOU 378 N LEU A 147 16065 16788 15690 -2434 -415 617 N ATOM 379 CA LEU A 147 48.928 33.327 287.741 1.00118.43 C ANISOU 379 CA LEU A 147 14980 15455 14561 -2190 -494 700 C ATOM 380 C LEU A 147 48.833 34.609 288.550 1.00112.47 C ANISOU 380 C LEU A 147 14401 14583 13749 -2260 -574 719 C ATOM 381 O LEU A 147 47.736 34.986 288.965 1.00112.17 O ANISOU 381 O LEU A 147 14539 14359 13720 -2139 -631 808 O ATOM 382 CB LEU A 147 49.281 32.166 288.679 1.00117.69 C ANISOU 382 CB LEU A 147 14681 15486 14549 -1958 -513 646 C ATOM 383 CG LEU A 147 49.426 30.782 288.040 1.00106.19 C ANISOU 383 CG LEU A 147 13044 14142 13160 -1851 -453 613 C ATOM 384 CD1 LEU A 147 49.808 29.763 289.098 1.00106.77 C ANISOU 384 CD1 LEU A 147 12961 14309 13298 -1621 -500 563 C ATOM 385 CD2 LEU A 147 48.151 30.360 287.331 1.00 94.74 C ANISOU 385 CD2 LEU A 147 11710 12542 11746 -1763 -418 726 C ATOM 386 N ARG A 148 49.952 35.300 288.786 1.00114.79 N ANISOU 386 N ARG A 148 14647 14986 13984 -2455 -582 625 N ATOM 387 CA ARG A 148 49.908 36.552 289.536 1.00126.90 C ANISOU 387 CA ARG A 148 16356 16401 15459 -2536 -661 636 C ATOM 388 C ARG A 148 49.322 37.701 288.727 1.00137.13 C ANISOU 388 C ARG A 148 17935 17496 16673 -2720 -676 715 C ATOM 389 O ARG A 148 49.197 38.809 289.261 1.00129.04 O ANISOU 389 O ARG A 148 17093 16341 15597 -2789 -753 728 O ATOM 390 CB ARG A 148 51.306 36.928 290.043 1.00128.14 C ANISOU 390 CB ARG A 148 16369 16742 15576 -2698 -666 499 C ATOM 391 CG ARG A 148 52.371 37.070 288.967 1.00134.86 C ANISOU 391 CG ARG A 148 17117 17759 16364 -2994 -575 406 C ATOM 392 CD ARG A 148 53.772 37.208 289.578 1.00151.59 C ANISOU 392 CD ARG A 148 19027 20108 18463 -3112 -577 239 C ATOM 393 NE ARG A 148 54.846 36.955 288.614 1.00152.53 N ANISOU 393 NE ARG A 148 18954 20457 18543 -3342 -474 113 N ATOM 394 CZ ARG A 148 55.633 37.884 288.071 1.00137.79 C ANISOU 394 CZ ARG A 148 17124 18657 16571 -3695 -421 39 C ATOM 395 NH1 ARG A 148 55.493 39.164 288.383 1.00134.48 N ANISOU 395 NH1 ARG A 148 16947 18073 16075 -3865 -473 86 N ATOM 396 NH2 ARG A 148 56.576 37.525 287.210 1.00129.84 N ANISOU 396 NH2 ARG A 148 15914 17888 15531 -3888 -315 -90 N ATOM 397 N CYS A 149 48.966 37.470 287.462 1.00150.46 N ANISOU 397 N CYS A 149 19676 19150 18343 -2797 -616 765 N ATOM 398 CA CYS A 149 48.199 38.427 286.682 1.00151.03 C ANISOU 398 CA CYS A 149 20044 19001 18340 -2914 -651 857 C ATOM 399 C CYS A 149 46.715 38.091 286.654 1.00139.19 C ANISOU 399 C CYS A 149 18655 17329 16902 -2658 -697 957 C ATOM 400 O CYS A 149 45.912 38.932 286.236 1.00146.25 O ANISOU 400 O CYS A 149 19809 18015 17744 -2688 -763 1027 O ATOM 401 CB CYS A 149 48.735 38.499 285.245 1.00155.81 C ANISOU 401 CB CYS A 149 20668 19672 18863 -3184 -561 846 C ATOM 402 SG CYS A 149 50.434 39.114 285.106 1.00165.69 S ANISOU 402 SG CYS A 149 21821 21123 20012 -3557 -495 715 S ATOM 403 N ARG A 150 46.334 36.891 287.095 1.00118.88 N ANISOU 403 N ARG A 150 15898 14837 14435 -2409 -669 956 N ATOM 404 CA ARG A 150 44.934 36.498 287.155 1.00112.69 C ANISOU 404 CA ARG A 150 15189 13917 13713 -2172 -700 1033 C ATOM 405 C ARG A 150 44.284 37.077 288.413 1.00109.03 C ANISOU 405 C ARG A 150 14830 13334 13264 -2016 -797 1045 C ATOM 406 O ARG A 150 44.880 37.031 289.492 1.00 94.58 O ANISOU 406 O ARG A 150 12897 11592 11446 -1976 -813 995 O ATOM 407 CB ARG A 150 44.811 34.976 287.172 1.00102.30 C ANISOU 407 CB ARG A 150 13645 12729 12494 -1990 -628 1025 C ATOM 408 CG ARG A 150 45.459 34.275 285.986 1.00 87.10 C ANISOU 408 CG ARG A 150 11588 10942 10566 -2114 -532 994 C ATOM 409 CD ARG A 150 44.434 33.899 284.928 1.00 84.35 C ANISOU 409 CD ARG A 150 11318 10497 10234 -2060 -507 1062 C ATOM 410 NE ARG A 150 43.490 32.893 285.407 1.00 93.73 N ANISOU 410 NE ARG A 150 12431 11661 11523 -1797 -504 1093 N ATOM 411 CZ ARG A 150 43.674 31.579 285.318 1.00101.82 C ANISOU 411 CZ ARG A 150 13260 12806 12620 -1692 -438 1068 C ATOM 412 NH1 ARG A 150 44.775 31.088 284.765 1.00103.24 N ANISOU 412 NH1 ARG A 150 13281 13154 12793 -1805 -374 999 N ATOM 413 NH2 ARG A 150 42.752 30.749 285.784 1.00 98.60 N ANISOU 413 NH2 ARG A 150 12819 12354 12291 -1476 -437 1103 N ATOM 414 N PRO A 151 43.068 37.629 288.317 1.00115.60 N ANISOU 414 N PRO A 151 15858 13975 14090 -1918 -867 1100 N ATOM 415 CA PRO A 151 42.379 38.069 289.542 1.00110.25 C ANISOU 415 CA PRO A 151 15252 13206 13431 -1746 -951 1094 C ATOM 416 C PRO A 151 41.889 36.917 290.399 1.00111.40 C ANISOU 416 C PRO A 151 15222 13440 13664 -1508 -910 1091 C ATOM 417 O PRO A 151 41.641 37.118 291.594 1.00115.86 O ANISOU 417 O PRO A 151 15793 13992 14236 -1387 -956 1069 O ATOM 418 CB PRO A 151 41.203 38.908 289.012 1.00115.36 C ANISOU 418 CB PRO A 151 16144 13638 14049 -1703 -1038 1134 C ATOM 419 CG PRO A 151 41.468 39.104 287.538 1.00123.26 C ANISOU 419 CG PRO A 151 17240 14602 14991 -1897 -1013 1170 C ATOM 420 CD PRO A 151 42.266 37.919 287.117 1.00125.68 C ANISOU 420 CD PRO A 151 17303 15114 15337 -1953 -885 1156 C ATOM 421 N SER A 152 41.746 35.718 289.829 1.00106.29 N ANISOU 421 N SER A 152 14430 12879 13075 -1446 -825 1111 N ATOM 422 CA SER A 152 41.269 34.575 290.600 1.00 84.49 C ANISOU 422 CA SER A 152 11529 10187 10387 -1238 -783 1116 C ATOM 423 C SER A 152 42.336 34.049 291.551 1.00 84.99 C ANISOU 423 C SER A 152 11435 10399 10459 -1223 -767 1073 C ATOM 424 O SER A 152 42.003 33.455 292.583 1.00 73.15 O ANISOU 424 O SER A 152 9879 8927 8988 -1059 -767 1076 O ATOM 425 CB SER A 152 40.812 33.467 289.652 1.00 64.32 C ANISOU 425 CB SER A 152 8885 7663 7889 -1187 -705 1147 C ATOM 426 OG SER A 152 41.852 33.116 288.763 1.00105.21 O ANISOU 426 OG SER A 152 13967 12949 13059 -1337 -649 1128 O ATOM 427 N TYR A 153 43.613 34.252 291.230 1.00 86.21 N ANISOU 427 N TYR A 153 11520 10656 10580 -1393 -756 1027 N ATOM 428 CA TYR A 153 44.696 33.815 292.101 1.00 95.54 C ANISOU 428 CA TYR A 153 12545 11990 11766 -1374 -759 965 C ATOM 429 C TYR A 153 45.108 34.873 293.115 1.00101.62 C ANISOU 429 C TYR A 153 13390 12740 12481 -1421 -838 925 C ATOM 430 O TYR A 153 45.871 34.561 294.036 1.00 90.05 O ANISOU 430 O TYR A 153 11810 11390 11015 -1372 -859 873 O ATOM 431 CB TYR A 153 45.905 33.387 291.264 1.00 91.80 C ANISOU 431 CB TYR A 153 11915 11675 11291 -1521 -703 905 C ATOM 432 CG TYR A 153 45.636 32.101 290.525 1.00 99.47 C ANISOU 432 CG TYR A 153 12772 12695 12327 -1431 -630 926 C ATOM 433 CD1 TYR A 153 45.046 32.112 289.273 1.00109.02 C ANISOU 433 CD1 TYR A 153 14050 13836 13538 -1500 -584 970 C ATOM 434 CD2 TYR A 153 45.935 30.873 291.098 1.00 93.76 C ANISOU 434 CD2 TYR A 153 11890 12075 11658 -1267 -619 903 C ATOM 435 CE1 TYR A 153 44.777 30.939 288.599 1.00108.00 C ANISOU 435 CE1 TYR A 153 13817 13748 13468 -1417 -519 984 C ATOM 436 CE2 TYR A 153 45.672 29.690 290.433 1.00 87.92 C ANISOU 436 CE2 TYR A 153 11061 11364 10979 -1182 -559 919 C ATOM 437 CZ TYR A 153 45.089 29.730 289.183 1.00111.54 C ANISOU 437 CZ TYR A 153 14108 14294 13976 -1260 -506 958 C ATOM 438 OH TYR A 153 44.820 28.563 288.504 1.00138.74 O ANISOU 438 OH TYR A 153 17466 17768 17482 -1180 -448 968 O ATOM 439 N HIS A 154 44.634 36.110 292.970 1.00 98.57 N ANISOU 439 N HIS A 154 13201 12205 12045 -1508 -893 943 N ATOM 440 CA HIS A 154 44.662 37.038 294.091 1.00 91.70 C ANISOU 440 CA HIS A 154 12427 11281 11133 -1492 -977 913 C ATOM 441 C HIS A 154 43.691 36.627 295.186 1.00 95.50 C ANISOU 441 C HIS A 154 12916 11724 11644 -1252 -999 937 C ATOM 442 O HIS A 154 43.784 37.144 296.305 1.00 98.96 O ANISOU 442 O HIS A 154 13392 12156 12051 -1205 -1060 902 O ATOM 443 CB HIS A 154 44.336 38.453 293.619 1.00 80.16 C ANISOU 443 CB HIS A 154 11199 9648 9611 -1633 -1043 924 C ATOM 444 CG HIS A 154 45.449 39.100 292.861 1.00 89.52 C ANISOU 444 CG HIS A 154 12408 10871 10735 -1911 -1031 889 C ATOM 445 ND1 HIS A 154 45.682 38.853 291.526 1.00 99.30 N ANISOU 445 ND1 HIS A 154 13632 12134 11962 -2056 -963 911 N ATOM 446 CD2 HIS A 154 46.405 39.973 293.255 1.00 97.21 C ANISOU 446 CD2 HIS A 154 13413 11874 11649 -2085 -1071 825 C ATOM 447 CE1 HIS A 154 46.729 39.554 291.127 1.00103.13 C ANISOU 447 CE1 HIS A 154 14143 12664 12377 -2318 -956 863 C ATOM 448 NE2 HIS A 154 47.187 40.241 292.158 1.00105.10 N ANISOU 448 NE2 HIS A 154 14418 12916 12598 -2344 -1021 809 N ATOM 449 N PHE A 155 42.767 35.715 294.883 1.00 81.41 N ANISOU 449 N PHE A 155 11098 9922 9914 -1114 -945 988 N ATOM 450 CA PHE A 155 41.844 35.166 295.865 1.00 70.42 C ANISOU 450 CA PHE A 155 9697 8516 8543 -908 -941 1007 C ATOM 451 C PHE A 155 42.434 33.953 296.575 1.00 78.32 C ANISOU 451 C PHE A 155 10538 9657 9565 -813 -903 1004 C ATOM 452 O PHE A 155 42.335 33.846 297.802 1.00 98.72 O ANISOU 452 O PHE A 155 13123 12264 12123 -704 -931 993 O ATOM 453 CB PHE A 155 40.522 34.796 295.185 1.00 70.49 C ANISOU 453 CB PHE A 155 9752 8438 8594 -821 -900 1053 C ATOM 454 CG PHE A 155 39.619 33.955 296.037 1.00 74.46 C ANISOU 454 CG PHE A 155 10212 8959 9121 -637 -862 1070 C ATOM 455 CD1 PHE A 155 38.887 34.520 297.066 1.00 83.05 C ANISOU 455 CD1 PHE A 155 11381 10000 10177 -541 -905 1042 C ATOM 456 CD2 PHE A 155 39.507 32.595 295.810 1.00 66.49 C ANISOU 456 CD2 PHE A 155 9088 8016 8160 -571 -781 1107 C ATOM 457 CE1 PHE A 155 38.057 33.739 297.856 1.00 92.30 C ANISOU 457 CE1 PHE A 155 12513 11201 11354 -398 -856 1052 C ATOM 458 CE2 PHE A 155 38.685 31.807 296.589 1.00 70.50 C ANISOU 458 CE2 PHE A 155 9574 8535 8676 -431 -738 1125 C ATOM 459 CZ PHE A 155 37.957 32.377 297.615 1.00 85.36 C ANISOU 459 CZ PHE A 155 11533 10382 10517 -352 -769 1099 C ATOM 460 N ILE A 156 43.064 33.042 295.830 1.00 74.39 N ANISOU 460 N ILE A 156 9911 9249 9105 -849 -848 1008 N ATOM 461 CA ILE A 156 43.713 31.891 296.453 1.00 79.55 C ANISOU 461 CA ILE A 156 10425 10024 9776 -748 -835 996 C ATOM 462 C ILE A 156 44.904 32.346 297.287 1.00 85.18 C ANISOU 462 C ILE A 156 11087 10835 10443 -792 -904 924 C ATOM 463 O ILE A 156 45.055 31.954 298.450 1.00 83.86 O ANISOU 463 O ILE A 156 10899 10710 10253 -669 -941 916 O ATOM 464 CB ILE A 156 44.133 30.860 295.385 1.00 85.68 C ANISOU 464 CB ILE A 156 11075 10873 10607 -771 -772 998 C ATOM 465 CG1 ILE A 156 42.974 29.915 295.059 1.00 76.25 C ANISOU 465 CG1 ILE A 156 9900 9609 9462 -653 -708 1068 C ATOM 466 CG2 ILE A 156 45.331 30.030 295.843 1.00 95.91 C ANISOU 466 CG2 ILE A 156 12216 12317 11909 -721 -794 941 C ATOM 467 CD1 ILE A 156 41.939 30.521 294.172 1.00 70.59 C ANISOU 467 CD1 ILE A 156 9288 8777 8755 -709 -682 1103 C ATOM 468 N GLY A 157 45.771 33.174 296.703 1.00 87.58 N ANISOU 468 N GLY A 157 11373 11177 10725 -977 -921 866 N ATOM 469 CA GLY A 157 46.926 33.655 297.443 1.00 75.75 C ANISOU 469 CA GLY A 157 9813 9784 9184 -1038 -985 780 C ATOM 470 C GLY A 157 46.536 34.363 298.725 1.00 74.46 C ANISOU 470 C GLY A 157 9763 9556 8971 -965 -1055 780 C ATOM 471 O GLY A 157 47.201 34.216 299.754 1.00 69.90 O ANISOU 471 O GLY A 157 9122 9070 8365 -900 -1110 729 O ATOM 472 N SER A 158 45.453 35.141 298.679 1.00 79.81 N ANISOU 472 N SER A 158 10608 10079 9635 -964 -1062 826 N ATOM 473 CA SER A 158 44.939 35.782 299.887 1.00 79.96 C ANISOU 473 CA SER A 158 10735 10036 9609 -877 -1125 817 C ATOM 474 C SER A 158 44.535 34.742 300.927 1.00 78.75 C ANISOU 474 C SER A 158 10537 9930 9453 -674 -1113 847 C ATOM 475 O SER A 158 44.885 34.860 302.108 1.00 68.24 O ANISOU 475 O SER A 158 9205 8649 8072 -610 -1169 812 O ATOM 476 CB SER A 158 43.753 36.684 299.538 1.00 74.18 C ANISOU 476 CB SER A 158 10179 9134 8871 -885 -1137 847 C ATOM 477 OG SER A 158 43.153 37.215 300.707 1.00 80.22 O ANISOU 477 OG SER A 158 11036 9849 9596 -779 -1191 827 O ATOM 478 N LEU A 159 43.792 33.714 300.507 1.00 63.69 N ANISOU 478 N LEU A 159 8604 8003 7590 -581 -1040 913 N ATOM 479 CA LEU A 159 43.408 32.657 301.438 1.00 67.01 C ANISOU 479 CA LEU A 159 9005 8459 7998 -413 -1021 951 C ATOM 480 C LEU A 159 44.629 31.922 301.977 1.00 74.74 C ANISOU 480 C LEU A 159 9869 9566 8961 -370 -1063 918 C ATOM 481 O LEU A 159 44.711 31.634 303.178 1.00 69.94 O ANISOU 481 O LEU A 159 9284 8992 8298 -261 -1105 917 O ATOM 482 CB LEU A 159 42.448 31.674 300.762 1.00 54.20 C ANISOU 482 CB LEU A 159 7376 6788 6429 -349 -932 1022 C ATOM 483 CG LEU A 159 40.964 32.046 300.705 1.00 70.82 C ANISOU 483 CG LEU A 159 9586 8786 8536 -311 -893 1049 C ATOM 484 CD1 LEU A 159 40.140 30.857 300.221 1.00 75.64 C ANISOU 484 CD1 LEU A 159 10166 9379 9194 -243 -802 1109 C ATOM 485 CD2 LEU A 159 40.440 32.531 302.056 1.00 67.59 C ANISOU 485 CD2 LEU A 159 9261 8365 8056 -230 -926 1026 C ATOM 486 N ALA A 160 45.595 31.617 301.110 1.00 90.60 N ANISOU 486 N ALA A 160 11756 11655 11013 -450 -1058 881 N ATOM 487 CA ALA A 160 46.730 30.813 301.545 1.00 99.16 C ANISOU 487 CA ALA A 160 12714 12871 12091 -382 -1108 831 C ATOM 488 C ALA A 160 47.637 31.586 302.493 1.00 91.07 C ANISOU 488 C ALA A 160 11671 11926 11006 -410 -1203 745 C ATOM 489 O ALA A 160 48.226 30.991 303.403 1.00101.43 O ANISOU 489 O ALA A 160 12938 13318 12284 -290 -1270 717 O ATOM 490 CB ALA A 160 47.518 30.316 300.334 1.00100.32 C ANISOU 490 CB ALA A 160 12714 13103 12300 -460 -1075 788 C ATOM 491 N VAL A 161 47.763 32.902 302.308 1.00 84.18 N ANISOU 491 N VAL A 161 10845 11024 10114 -565 -1219 701 N ATOM 492 CA VAL A 161 48.532 33.696 303.262 1.00 93.00 C ANISOU 492 CA VAL A 161 11959 12207 11171 -598 -1310 617 C ATOM 493 C VAL A 161 47.738 33.934 304.538 1.00 93.65 C ANISOU 493 C VAL A 161 12176 12217 11191 -472 -1346 654 C ATOM 494 O VAL A 161 48.333 34.169 305.597 1.00 85.83 O ANISOU 494 O VAL A 161 11174 11295 10141 -428 -1428 596 O ATOM 495 CB VAL A 161 48.987 35.033 302.647 1.00 89.29 C ANISOU 495 CB VAL A 161 11510 11722 10694 -825 -1318 552 C ATOM 496 CG1 VAL A 161 47.840 36.036 302.559 1.00 95.36 C ANISOU 496 CG1 VAL A 161 12473 12313 11447 -868 -1306 608 C ATOM 497 CG2 VAL A 161 50.155 35.618 303.436 1.00 86.71 C ANISOU 497 CG2 VAL A 161 11113 11514 10318 -884 -1407 434 C ATOM 498 N ALA A 162 46.405 33.875 304.466 1.00 90.79 N ANISOU 498 N ALA A 162 11931 11730 10835 -414 -1286 740 N ATOM 499 CA ALA A 162 45.599 33.882 305.681 1.00 76.07 C ANISOU 499 CA ALA A 162 10175 9822 8905 -285 -1302 769 C ATOM 500 C ALA A 162 45.737 32.561 306.425 1.00 82.14 C ANISOU 500 C ALA A 162 10911 10655 9642 -127 -1307 810 C ATOM 501 O ALA A 162 45.940 32.547 307.644 1.00 94.93 O ANISOU 501 O ALA A 162 12570 12316 11182 -42 -1370 792 O ATOM 502 CB ALA A 162 44.135 34.161 305.338 1.00 64.87 C ANISOU 502 CB ALA A 162 8869 8275 7503 -271 -1232 826 C ATOM 503 N ASP A 163 45.643 31.440 305.705 1.00 78.08 N ANISOU 503 N ASP A 163 10341 10142 9184 -87 -1250 865 N ATOM 504 CA ASP A 163 45.873 30.139 306.325 1.00 77.47 C ANISOU 504 CA ASP A 163 10252 10108 9076 59 -1270 904 C ATOM 505 C ASP A 163 47.274 30.057 306.917 1.00 90.18 C ANISOU 505 C ASP A 163 11771 11842 10652 98 -1387 819 C ATOM 506 O ASP A 163 47.474 29.461 307.982 1.00 95.48 O ANISOU 506 O ASP A 163 12489 12541 11248 230 -1451 832 O ATOM 507 CB ASP A 163 45.659 29.028 305.296 1.00 78.11 C ANISOU 507 CB ASP A 163 10280 10165 9234 79 -1199 959 C ATOM 508 CG ASP A 163 44.198 28.859 304.914 1.00 98.84 C ANISOU 508 CG ASP A 163 12997 12677 11881 75 -1089 1043 C ATOM 509 OD1 ASP A 163 43.325 29.136 305.765 1.00 95.78 O ANISOU 509 OD1 ASP A 163 12721 12244 11429 112 -1070 1071 O ATOM 510 OD2 ASP A 163 43.921 28.448 303.764 1.00 94.56 O ANISOU 510 OD2 ASP A 163 12407 12104 11418 33 -1021 1070 O ATOM 511 N LEU A 164 48.255 30.666 306.246 1.00 90.05 N ANISOU 511 N LEU A 164 11628 11905 10680 -22 -1418 724 N ATOM 512 CA LEU A 164 49.629 30.612 306.732 1.00 96.83 C ANISOU 512 CA LEU A 164 12368 12907 11514 7 -1529 616 C ATOM 513 C LEU A 164 49.805 31.470 307.979 1.00 96.25 C ANISOU 513 C LEU A 164 12364 12855 11351 19 -1612 569 C ATOM 514 O LEU A 164 50.471 31.054 308.936 1.00 96.49 O ANISOU 514 O LEU A 164 12374 12967 11320 140 -1714 527 O ATOM 515 CB LEU A 164 50.596 31.056 305.635 1.00 98.54 C ANISOU 515 CB LEU A 164 12421 13222 11798 -154 -1521 513 C ATOM 516 CG LEU A 164 52.070 30.962 306.042 1.00100.72 C ANISOU 516 CG LEU A 164 12535 13678 12057 -130 -1633 370 C ATOM 517 CD1 LEU A 164 52.852 30.126 305.042 1.00101.10 C ANISOU 517 CD1 LEU A 164 12400 13835 12178 -130 -1619 304 C ATOM 518 CD2 LEU A 164 52.682 32.347 306.192 1.00 92.78 C ANISOU 518 CD2 LEU A 164 11496 12731 11024 -308 -1667 264 C ATOM 519 N LEU A 165 49.219 32.673 307.983 1.00 91.26 N ANISOU 519 N LEU A 165 11821 12148 10707 -97 -1581 569 N ATOM 520 CA LEU A 165 49.327 33.557 309.140 1.00 78.49 C ANISOU 520 CA LEU A 165 10275 10542 9005 -92 -1658 517 C ATOM 521 C LEU A 165 48.867 32.857 310.409 1.00 92.56 C ANISOU 521 C LEU A 165 12160 12314 10695 91 -1691 576 C ATOM 522 O LEU A 165 49.454 33.043 311.481 1.00 98.32 O ANISOU 522 O LEU A 165 12896 13115 11344 153 -1791 517 O ATOM 523 CB LEU A 165 48.505 34.828 308.907 1.00 85.78 C ANISOU 523 CB LEU A 165 11311 11350 9932 -214 -1615 524 C ATOM 524 CG LEU A 165 48.224 35.717 310.125 1.00 90.27 C ANISOU 524 CG LEU A 165 11992 11895 10413 -185 -1676 487 C ATOM 525 CD1 LEU A 165 49.511 36.333 310.663 1.00 71.43 C ANISOU 525 CD1 LEU A 165 9527 9623 7991 -245 -1786 363 C ATOM 526 CD2 LEU A 165 47.211 36.793 309.766 1.00 97.00 C ANISOU 526 CD2 LEU A 165 12967 12608 11279 -270 -1632 500 C ATOM 527 N GLY A 166 47.813 32.051 310.307 1.00 90.47 N ANISOU 527 N GLY A 166 11981 11962 10431 169 -1607 689 N ATOM 528 CA GLY A 166 47.296 31.331 311.452 1.00 96.62 C ANISOU 528 CA GLY A 166 12879 12722 11108 315 -1619 755 C ATOM 529 C GLY A 166 48.114 30.102 311.791 1.00 87.94 C ANISOU 529 C GLY A 166 11743 11689 9981 450 -1698 765 C ATOM 530 O GLY A 166 48.404 29.850 312.964 1.00 85.83 O ANISOU 530 O GLY A 166 11546 11459 9606 559 -1786 760 O ATOM 531 N SER A 167 48.497 29.326 310.774 1.00 89.32 N ANISOU 531 N SER A 167 11814 11876 10247 453 -1677 773 N ATOM 532 CA SER A 167 49.290 28.127 311.023 1.00 88.56 C ANISOU 532 CA SER A 167 11684 11833 10132 600 -1769 769 C ATOM 533 C SER A 167 50.674 28.471 311.558 1.00 87.51 C ANISOU 533 C SER A 167 11437 11843 9970 638 -1920 633 C ATOM 534 O SER A 167 51.272 27.669 312.284 1.00 78.06 O ANISOU 534 O SER A 167 10262 10689 8709 798 -2037 620 O ATOM 535 CB SER A 167 49.413 27.298 309.745 1.00 90.92 C ANISOU 535 CB SER A 167 11882 12121 10544 592 -1715 785 C ATOM 536 OG SER A 167 50.113 28.021 308.753 1.00 96.59 O ANISOU 536 OG SER A 167 12425 12922 11353 455 -1704 682 O ATOM 537 N VAL A 168 51.205 29.644 311.204 1.00 85.85 N ANISOU 537 N VAL A 168 11112 11706 9802 491 -1925 526 N ATOM 538 CA VAL A 168 52.473 30.088 311.775 1.00 91.65 C ANISOU 538 CA VAL A 168 11732 12588 10503 504 -2062 380 C ATOM 539 C VAL A 168 52.295 30.438 313.246 1.00 97.46 C ANISOU 539 C VAL A 168 12608 13316 11108 588 -2141 389 C ATOM 540 O VAL A 168 53.115 30.061 314.092 1.00 91.76 O ANISOU 540 O VAL A 168 11865 12685 10316 720 -2282 325 O ATOM 541 CB VAL A 168 53.036 31.275 310.969 1.00 81.58 C ANISOU 541 CB VAL A 168 10315 11384 9300 289 -2031 266 C ATOM 542 CG1 VAL A 168 54.183 31.967 311.717 1.00 75.57 C ANISOU 542 CG1 VAL A 168 9456 10768 8489 270 -2161 110 C ATOM 543 CG2 VAL A 168 53.516 30.801 309.609 1.00 93.97 C ANISOU 543 CG2 VAL A 168 11719 13008 10978 221 -1978 228 C ATOM 544 N ILE A 169 51.225 31.163 313.577 1.00100.74 N ANISOU 544 N ILE A 169 13165 13629 11483 519 -2060 457 N ATOM 545 CA ILE A 169 50.969 31.511 314.971 1.00100.96 C ANISOU 545 CA ILE A 169 13330 13653 11379 592 -2122 462 C ATOM 546 C ILE A 169 50.728 30.254 315.793 1.00 95.85 C ANISOU 546 C ILE A 169 12814 12976 10630 778 -2164 557 C ATOM 547 O ILE A 169 51.118 30.176 316.964 1.00100.59 O ANISOU 547 O ILE A 169 13484 13625 11109 885 -2279 531 O ATOM 548 CB ILE A 169 49.782 32.492 315.068 1.00 94.74 C ANISOU 548 CB ILE A 169 12659 12764 10575 489 -2017 505 C ATOM 549 CG1 ILE A 169 50.164 33.869 314.508 1.00 88.30 C ANISOU 549 CG1 ILE A 169 11756 11967 9827 313 -2018 399 C ATOM 550 CG2 ILE A 169 49.279 32.624 316.506 1.00 91.59 C ANISOU 550 CG2 ILE A 169 12420 12354 10027 579 -2053 529 C ATOM 551 CD1 ILE A 169 51.327 34.552 315.214 1.00 89.69 C ANISOU 551 CD1 ILE A 169 11856 12264 9956 295 -2153 259 C ATOM 552 N PHE A 170 50.087 29.249 315.197 1.00 73.11 N ANISOU 552 N PHE A 170 9984 10008 7788 815 -2078 669 N ATOM 553 CA PHE A 170 49.859 28.002 315.914 1.00 90.06 C ANISOU 553 CA PHE A 170 12281 12105 9832 974 -2118 768 C ATOM 554 C PHE A 170 51.180 27.366 316.323 1.00 87.68 C ANISOU 554 C PHE A 170 11916 11899 9498 1127 -2302 690 C ATOM 555 O PHE A 170 51.422 27.103 317.506 1.00102.85 O ANISOU 555 O PHE A 170 13960 13837 11282 1250 -2416 696 O ATOM 556 CB PHE A 170 49.050 27.039 315.049 1.00 87.69 C ANISOU 556 CB PHE A 170 12026 11696 9598 969 -1996 885 C ATOM 557 CG PHE A 170 48.774 25.721 315.714 1.00 93.95 C ANISOU 557 CG PHE A 170 13001 12413 10283 1110 -2030 996 C ATOM 558 CD1 PHE A 170 49.707 24.696 315.674 1.00 84.91 C ANISOU 558 CD1 PHE A 170 11834 11287 9140 1259 -2164 978 C ATOM 559 CD2 PHE A 170 47.581 25.507 316.380 1.00104.87 C ANISOU 559 CD2 PHE A 170 14585 13706 11556 1091 -1932 1111 C ATOM 560 CE1 PHE A 170 49.451 23.486 316.286 1.00 86.38 C ANISOU 560 CE1 PHE A 170 12224 11378 9218 1387 -2208 1087 C ATOM 561 CE2 PHE A 170 47.320 24.298 316.993 1.00 96.35 C ANISOU 561 CE2 PHE A 170 13700 12546 10362 1195 -1957 1220 C ATOM 562 CZ PHE A 170 48.255 23.287 316.945 1.00 91.14 C ANISOU 562 CZ PHE A 170 13046 11881 9703 1344 -2100 1216 C ATOM 563 N VAL A 171 52.051 27.109 315.347 1.00 76.59 N ANISOU 563 N VAL A 171 10320 10566 8216 1126 -2339 605 N ATOM 564 CA VAL A 171 53.315 26.438 315.635 1.00 90.86 C ANISOU 564 CA VAL A 171 12041 12477 10006 1290 -2522 507 C ATOM 565 C VAL A 171 54.165 27.285 316.570 1.00 89.69 C ANISOU 565 C VAL A 171 11835 12459 9784 1308 -2657 374 C ATOM 566 O VAL A 171 54.828 26.763 317.474 1.00 83.38 O ANISOU 566 O VAL A 171 11085 11709 8887 1484 -2826 335 O ATOM 567 CB VAL A 171 54.059 26.114 314.326 1.00 91.15 C ANISOU 567 CB VAL A 171 11849 12590 10195 1264 -2517 413 C ATOM 568 CG1 VAL A 171 55.458 25.565 314.610 1.00 81.67 C ANISOU 568 CG1 VAL A 171 10516 11531 8985 1436 -2719 264 C ATOM 569 CG2 VAL A 171 53.259 25.116 313.512 1.00 82.66 C ANISOU 569 CG2 VAL A 171 10849 11381 9178 1280 -2407 543 C ATOM 570 N TYR A 172 54.164 28.604 316.371 1.00 91.57 N ANISOU 570 N TYR A 172 11980 12748 10063 1127 -2595 300 N ATOM 571 CA TYR A 172 54.947 29.482 317.233 1.00104.08 C ANISOU 571 CA TYR A 172 13509 14455 11583 1122 -2716 166 C ATOM 572 C TYR A 172 54.474 29.385 318.679 1.00112.95 C ANISOU 572 C TYR A 172 14857 15526 12534 1239 -2780 240 C ATOM 573 O TYR A 172 55.261 29.103 319.589 1.00 95.81 O ANISOU 573 O TYR A 172 12697 13437 10267 1388 -2952 171 O ATOM 574 CB TYR A 172 54.862 30.925 316.732 1.00 91.43 C ANISOU 574 CB TYR A 172 11812 12877 10049 888 -2624 94 C ATOM 575 CG TYR A 172 55.618 31.907 317.601 1.00108.09 C ANISOU 575 CG TYR A 172 13871 15104 12096 858 -2739 -48 C ATOM 576 CD1 TYR A 172 57.008 31.926 317.614 1.00115.35 C ANISOU 576 CD1 TYR A 172 14588 16203 13038 887 -2877 -226 C ATOM 577 CD2 TYR A 172 54.945 32.811 318.412 1.00115.48 C ANISOU 577 CD2 TYR A 172 14952 15979 12947 803 -2713 -18 C ATOM 578 CE1 TYR A 172 57.708 32.820 318.412 1.00119.66 C ANISOU 578 CE1 TYR A 172 15079 16861 13524 853 -2984 -366 C ATOM 579 CE2 TYR A 172 55.635 33.710 319.213 1.00113.19 C ANISOU 579 CE2 TYR A 172 14619 15791 12597 774 -2822 -153 C ATOM 580 CZ TYR A 172 57.015 33.710 319.209 1.00119.92 C ANISOU 580 CZ TYR A 172 15273 16818 13475 795 -2957 -324 C ATOM 581 OH TYR A 172 57.701 34.604 320.004 1.00124.24 O ANISOU 581 OH TYR A 172 15771 17471 13962 758 -3065 -467 O ATOM 582 N SER A 173 53.180 29.615 318.906 1.00128.08 N ANISOU 582 N SER A 173 16951 17314 14401 1173 -2645 373 N ATOM 583 CA SER A 173 52.636 29.574 320.257 1.00127.03 C ANISOU 583 CA SER A 173 17035 17139 14093 1256 -2679 441 C ATOM 584 C SER A 173 52.659 28.173 320.852 1.00116.29 C ANISOU 584 C SER A 173 15837 15727 12621 1449 -2765 539 C ATOM 585 O SER A 173 52.669 28.035 322.079 1.00113.94 O ANISOU 585 O SER A 173 15700 15435 12157 1550 -2858 561 O ATOM 586 CB SER A 173 51.208 30.114 320.248 1.00131.20 C ANISOU 586 CB SER A 173 17689 17557 14604 1133 -2500 539 C ATOM 587 OG SER A 173 50.363 29.318 319.436 1.00137.49 O ANISOU 587 OG SER A 173 18534 18244 15463 1112 -2366 664 O ATOM 588 N PHE A 174 52.660 27.134 320.017 1.00114.15 N ANISOU 588 N PHE A 174 15544 15398 12430 1500 -2740 600 N ATOM 589 CA PHE A 174 52.728 25.775 320.538 1.00116.26 C ANISOU 589 CA PHE A 174 15987 15594 12592 1686 -2839 693 C ATOM 590 C PHE A 174 54.133 25.437 321.020 1.00122.53 C ANISOU 590 C PHE A 174 16704 16503 13349 1870 -3080 564 C ATOM 591 O PHE A 174 54.297 24.843 322.090 1.00125.30 O ANISOU 591 O PHE A 174 17245 16826 13537 2029 -3217 606 O ATOM 592 CB PHE A 174 52.281 24.776 319.472 1.00104.73 C ANISOU 592 CB PHE A 174 14532 14026 11233 1684 -2742 789 C ATOM 593 CG PHE A 174 52.074 23.387 319.999 1.00117.48 C ANISOU 593 CG PHE A 174 16387 15520 12729 1844 -2813 915 C ATOM 594 CD1 PHE A 174 53.119 22.480 320.033 1.00115.67 C ANISOU 594 CD1 PHE A 174 16139 15313 12496 2044 -3010 859 C ATOM 595 CD2 PHE A 174 50.834 22.991 320.469 1.00124.48 C ANISOU 595 CD2 PHE A 174 17525 16271 13501 1791 -2687 1082 C ATOM 596 CE1 PHE A 174 52.928 21.202 320.522 1.00117.70 C ANISOU 596 CE1 PHE A 174 16652 15433 12635 2194 -3091 981 C ATOM 597 CE2 PHE A 174 50.637 21.716 320.957 1.00124.10 C ANISOU 597 CE2 PHE A 174 17726 16097 13329 1913 -2749 1206 C ATOM 598 CZ PHE A 174 51.685 20.821 320.984 1.00125.74 C ANISOU 598 CZ PHE A 174 17941 16303 13532 2118 -2957 1162 C ATOM 599 N ILE A 175 55.156 25.808 320.246 1.00131.36 N ANISOU 599 N ILE A 175 17545 17758 14609 1849 -3137 399 N ATOM 600 CA ILE A 175 56.531 25.567 320.665 1.00136.27 C ANISOU 600 CA ILE A 175 18049 18520 15206 2022 -3370 239 C ATOM 601 C ILE A 175 56.986 26.578 321.709 1.00130.44 C ANISOU 601 C ILE A 175 17294 17897 14370 2008 -3467 132 C ATOM 602 O ILE A 175 57.936 26.305 322.453 1.00138.59 O ANISOU 602 O ILE A 175 18311 19025 15322 2185 -3680 27 O ATOM 603 CB ILE A 175 57.478 25.591 319.452 1.00135.16 C ANISOU 603 CB ILE A 175 17596 18511 15247 1989 -3385 77 C ATOM 604 CG1 ILE A 175 58.821 24.941 319.809 1.00143.45 C ANISOU 604 CG1 ILE A 175 18538 19694 16274 2223 -3637 -83 C ATOM 605 CG2 ILE A 175 57.668 27.025 318.937 1.00134.33 C ANISOU 605 CG2 ILE A 175 17279 18520 15239 1749 -3281 -41 C ATOM 606 CD1 ILE A 175 59.802 24.854 318.649 1.00146.90 C ANISOU 606 CD1 ILE A 175 18652 20285 16878 2206 -3659 -266 C ATOM 607 N ASP A 176 56.332 27.738 321.790 1.00110.04 N ANISOU 607 N ASP A 176 14717 15303 11789 1813 -3326 147 N ATOM 608 CA ASP A 176 56.714 28.750 322.765 1.00 96.72 C ANISOU 608 CA ASP A 176 13020 13717 10013 1788 -3411 42 C ATOM 609 C ASP A 176 56.147 28.474 324.151 1.00114.55 C ANISOU 609 C ASP A 176 15564 15901 12058 1899 -3466 152 C ATOM 610 O ASP A 176 56.620 29.069 325.126 1.00118.73 O ANISOU 610 O ASP A 176 16106 16523 12485 1938 -3585 59 O ATOM 611 CB ASP A 176 56.254 30.132 322.296 1.00 84.03 C ANISOU 611 CB ASP A 176 11321 12118 8491 1540 -3252 5 C ATOM 612 CG ASP A 176 56.836 31.255 323.130 1.00 93.33 C ANISOU 612 CG ASP A 176 12443 13414 9606 1497 -3349 -140 C ATOM 613 OD1 ASP A 176 58.014 31.149 323.527 1.00112.18 O ANISOU 613 OD1 ASP A 176 14709 15946 11970 1606 -3533 -288 O ATOM 614 OD2 ASP A 176 56.118 32.242 323.391 1.00 92.97 O ANISOU 614 OD2 ASP A 176 12470 13318 9534 1360 -3248 -118 O ATOM 615 N PHE A 177 55.162 27.586 324.267 1.00130.35 N ANISOU 615 N PHE A 177 17797 17744 13985 1941 -3381 341 N ATOM 616 CA PHE A 177 54.524 27.301 325.548 1.00131.58 C ANISOU 616 CA PHE A 177 18245 17827 13923 2013 -3405 457 C ATOM 617 C PHE A 177 54.590 25.835 325.945 1.00126.44 C ANISOU 617 C PHE A 177 17810 17078 13154 2209 -3518 572 C ATOM 618 O PHE A 177 54.824 25.532 327.117 1.00140.46 O ANISOU 618 O PHE A 177 19775 18855 14739 2344 -3665 590 O ATOM 619 CB PHE A 177 53.056 27.756 325.515 1.00129.32 C ANISOU 619 CB PHE A 177 18083 17438 13614 1838 -3169 581 C ATOM 620 CG PHE A 177 52.342 27.587 326.827 1.00141.17 C ANISOU 620 CG PHE A 177 19868 18888 14884 1875 -3164 683 C ATOM 621 CD1 PHE A 177 52.594 28.449 327.884 1.00141.43 C ANISOU 621 CD1 PHE A 177 19927 19014 14795 1882 -3245 594 C ATOM 622 CD2 PHE A 177 51.419 26.568 327.005 1.00141.59 C ANISOU 622 CD2 PHE A 177 20162 18804 14832 1889 -3074 861 C ATOM 623 CE1 PHE A 177 51.941 28.297 329.095 1.00135.18 C ANISOU 623 CE1 PHE A 177 19396 18188 13777 1907 -3234 681 C ATOM 624 CE2 PHE A 177 50.763 26.411 328.215 1.00134.73 C ANISOU 624 CE2 PHE A 177 19558 17899 13732 1899 -3057 951 C ATOM 625 CZ PHE A 177 51.024 27.277 329.259 1.00130.74 C ANISOU 625 CZ PHE A 177 19075 17497 13104 1910 -3136 860 C ATOM 626 N HIS A 178 54.391 24.911 325.006 1.00111.07 N ANISOU 626 N HIS A 178 15857 15036 11309 2229 -3461 650 N ATOM 627 CA HIS A 178 54.443 23.491 325.331 1.00111.69 C ANISOU 627 CA HIS A 178 16164 14996 11279 2412 -3575 762 C ATOM 628 C HIS A 178 55.859 22.935 325.341 1.00124.46 C ANISOU 628 C HIS A 178 17670 16699 12920 2641 -3840 623 C ATOM 629 O HIS A 178 56.050 21.787 325.756 1.00129.97 O ANISOU 629 O HIS A 178 18578 17297 13507 2832 -3988 697 O ATOM 630 CB HIS A 178 53.589 22.688 324.345 1.00126.13 C ANISOU 630 CB HIS A 178 18049 16674 13199 2340 -3406 902 C ATOM 631 CG HIS A 178 52.119 22.768 324.616 1.00128.65 C ANISOU 631 CG HIS A 178 18574 16878 13429 2177 -3187 1067 C ATOM 632 ND1 HIS A 178 51.465 23.962 324.835 1.00128.31 N ANISOU 632 ND1 HIS A 178 18476 16895 13382 2005 -3040 1042 N ATOM 633 CD2 HIS A 178 51.176 21.800 324.708 1.00129.56 C ANISOU 633 CD2 HIS A 178 18944 16829 13451 2157 -3090 1246 C ATOM 634 CE1 HIS A 178 50.183 23.726 325.049 1.00129.78 C ANISOU 634 CE1 HIS A 178 18856 16975 13480 1895 -2862 1186 C ATOM 635 NE2 HIS A 178 49.981 22.423 324.977 1.00128.37 N ANISOU 635 NE2 HIS A 178 18867 16662 13244 1972 -2882 1314 N ATOM 636 N VAL A 179 56.847 23.708 324.900 1.00130.85 N ANISOU 636 N VAL A 179 18162 17691 13865 2627 -3908 418 N ATOM 637 CA VAL A 179 58.244 23.294 324.914 1.00139.07 C ANISOU 637 CA VAL A 179 19049 18857 14936 2840 -4161 243 C ATOM 638 C VAL A 179 59.065 24.156 325.865 1.00139.43 C ANISOU 638 C VAL A 179 19008 19072 14897 2887 -4320 80 C ATOM 639 O VAL A 179 59.780 23.639 326.724 1.00151.67 O ANISOU 639 O VAL A 179 20656 20654 16318 3114 -4562 26 O ATOM 640 CB VAL A 179 58.839 23.320 323.487 1.00133.10 C ANISOU 640 CB VAL A 179 17960 18198 14416 2787 -4114 108 C ATOM 641 CG1 VAL A 179 60.342 23.044 323.510 1.00132.18 C ANISOU 641 CG1 VAL A 179 17629 18257 14337 2995 -4371 -121 C ATOM 642 CG2 VAL A 179 58.124 22.306 322.598 1.00121.31 C ANISOU 642 CG2 VAL A 179 16565 16533 12994 2782 -3994 260 C ATOM 643 N PHE A 180 58.962 25.478 325.734 1.00130.48 N ANISOU 643 N PHE A 180 17704 18041 13830 2675 -4195 -2 N ATOM 644 CA PHE A 180 59.727 26.392 326.569 1.00142.74 C ANISOU 644 CA PHE A 180 19156 19760 15317 2690 -4330 -169 C ATOM 645 C PHE A 180 58.960 26.877 327.791 1.00143.30 C ANISOU 645 C PHE A 180 19486 19769 15194 2650 -4297 -63 C ATOM 646 O PHE A 180 59.579 27.412 328.718 1.00148.92 O ANISOU 646 O PHE A 180 20182 20596 15804 2713 -4448 -182 O ATOM 647 CB PHE A 180 60.177 27.607 325.747 1.00141.16 C ANISOU 647 CB PHE A 180 18623 19714 15296 2476 -4232 -342 C ATOM 648 CG PHE A 180 61.129 27.271 324.626 1.00137.67 C ANISOU 648 CG PHE A 180 17885 19391 15032 2502 -4279 -497 C ATOM 649 CD1 PHE A 180 62.066 26.259 324.764 1.00137.84 C ANISOU 649 CD1 PHE A 180 17863 19476 15033 2764 -4506 -591 C ATOM 650 CD2 PHE A 180 61.087 27.976 323.435 1.00133.59 C ANISOU 650 CD2 PHE A 180 17140 18925 14695 2268 -4101 -556 C ATOM 651 CE1 PHE A 180 62.941 25.957 323.736 1.00138.08 C ANISOU 651 CE1 PHE A 180 17602 19636 15225 2791 -4546 -756 C ATOM 652 CE2 PHE A 180 61.960 27.678 322.404 1.00135.26 C ANISOU 652 CE2 PHE A 180 17074 19262 15058 2275 -4132 -707 C ATOM 653 CZ PHE A 180 62.886 26.668 322.555 1.00141.53 C ANISOU 653 CZ PHE A 180 17803 20137 15835 2537 -4349 -814 C ATOM 654 N HIS A 181 57.639 26.703 327.817 1.00129.49 N ANISOU 654 N HIS A 181 17963 17851 13388 2544 -4103 142 N ATOM 655 CA HIS A 181 56.819 27.091 328.963 1.00125.90 C ANISOU 655 CA HIS A 181 17757 17342 12736 2499 -4052 241 C ATOM 656 C HIS A 181 57.015 28.562 329.323 1.00128.54 C ANISOU 656 C HIS A 181 17944 17808 13086 2366 -4032 97 C ATOM 657 O HIS A 181 56.962 28.939 330.496 1.00139.20 O ANISOU 657 O HIS A 181 19436 19192 14261 2404 -4105 85 O ATOM 658 CB HIS A 181 57.113 26.207 330.179 1.00134.94 C ANISOU 658 CB HIS A 181 19175 18449 13648 2726 -4262 300 C ATOM 659 CG HIS A 181 56.940 24.742 329.922 1.00137.55 C ANISOU 659 CG HIS A 181 19695 18625 13941 2865 -4305 445 C ATOM 660 ND1 HIS A 181 57.908 23.972 329.314 1.00138.39 N ANISOU 660 ND1 HIS A 181 19669 18758 14154 3037 -4469 359 N ATOM 661 CD2 HIS A 181 55.914 23.903 330.200 1.00137.27 C ANISOU 661 CD2 HIS A 181 19977 18408 13773 2852 -4207 662 C ATOM 662 CE1 HIS A 181 57.485 22.724 329.223 1.00135.67 C ANISOU 662 CE1 HIS A 181 19536 18228 13784 3098 -4430 518 C ATOM 663 NE2 HIS A 181 56.277 22.655 329.753 1.00137.10 N ANISOU 663 NE2 HIS A 181 19997 18280 13814 2983 -4276 707 N ATOM 664 N ARG A 182 57.246 29.403 328.319 1.00123.71 N ANISOU 664 N ARG A 182 17060 17268 12676 2203 -3935 -15 N ATOM 665 CA ARG A 182 57.405 30.827 328.557 1.00123.88 C ANISOU 665 CA ARG A 182 16954 17392 12725 2055 -3909 -151 C ATOM 666 C ARG A 182 56.049 31.468 328.837 1.00116.84 C ANISOU 666 C ARG A 182 16227 16393 11773 1904 -3710 -34 C ATOM 667 O ARG A 182 54.992 30.920 328.511 1.00112.39 O ANISOU 667 O ARG A 182 15805 15693 11203 1866 -3554 132 O ATOM 668 CB ARG A 182 58.072 31.503 327.359 1.00115.58 C ANISOU 668 CB ARG A 182 15586 16435 11895 1910 -3865 -300 C ATOM 669 CG ARG A 182 59.402 30.879 326.957 1.00123.08 C ANISOU 669 CG ARG A 182 16329 17516 12920 2046 -4042 -443 C ATOM 670 CD ARG A 182 60.545 31.885 327.019 1.00134.22 C ANISOU 670 CD ARG A 182 17483 19126 14388 1974 -4150 -688 C ATOM 671 NE ARG A 182 61.820 31.291 326.614 1.00138.24 N ANISOU 671 NE ARG A 182 17764 19789 14973 2103 -4315 -853 N ATOM 672 CZ ARG A 182 62.727 30.785 327.448 1.00138.64 C ANISOU 672 CZ ARG A 182 17806 19950 14920 2333 -4560 -963 C ATOM 673 NH1 ARG A 182 63.850 30.268 326.968 1.00137.94 N ANISOU 673 NH1 ARG A 182 17483 20010 14917 2448 -4701 -1133 N ATOM 674 NH2 ARG A 182 62.524 30.794 328.760 1.00135.97 N ANISOU 674 NH2 ARG A 182 17691 19582 14388 2454 -4670 -915 N ATOM 675 N LYS A 183 56.089 32.644 329.454 1.00112.87 N ANISOU 675 N LYS A 183 15698 15960 11226 1819 -3721 -139 N ATOM 676 CA LYS A 183 54.882 33.347 329.860 1.00103.93 C ANISOU 676 CA LYS A 183 14713 14752 10025 1699 -3561 -68 C ATOM 677 C LYS A 183 54.527 34.441 328.865 1.00109.01 C ANISOU 677 C LYS A 183 15197 15370 10851 1489 -3410 -125 C ATOM 678 O LYS A 183 55.398 35.047 328.236 1.00118.49 O ANISOU 678 O LYS A 183 16182 16651 12189 1411 -3461 -264 O ATOM 679 CB LYS A 183 55.048 33.955 331.255 1.00105.73 C ANISOU 679 CB LYS A 183 15046 15058 10068 1751 -3672 -146 C ATOM 680 CG LYS A 183 55.163 32.936 332.377 1.00117.42 C ANISOU 680 CG LYS A 183 16752 16538 11324 1947 -3807 -63 C ATOM 681 CD LYS A 183 53.906 32.081 332.511 1.00117.10 C ANISOU 681 CD LYS A 183 16962 16356 11175 1946 -3653 148 C ATOM 682 CE LYS A 183 54.159 30.843 333.352 1.00114.47 C ANISOU 682 CE LYS A 183 16861 15993 10640 2138 -3799 249 C ATOM 683 NZ LYS A 183 54.739 29.737 332.544 1.00115.73 N ANISOU 683 NZ LYS A 183 16965 16105 10901 2248 -3876 293 N ATOM 684 N ASP A 184 53.229 34.687 328.736 1.00101.88 N ANISOU 684 N ASP A 184 14411 14357 9940 1395 -3227 -22 N ATOM 685 CA ASP A 184 52.699 35.712 327.850 1.00102.92 C ANISOU 685 CA ASP A 184 14444 14437 10225 1211 -3086 -59 C ATOM 686 C ASP A 184 52.235 36.907 328.669 1.00113.28 C ANISOU 686 C ASP A 184 15827 15759 11453 1149 -3073 -139 C ATOM 687 O ASP A 184 51.472 36.751 329.627 1.00124.44 O ANISOU 687 O ASP A 184 17421 17157 12703 1206 -3039 -80 O ATOM 688 CB ASP A 184 51.536 35.169 327.020 1.00 94.32 C ANISOU 688 CB ASP A 184 13417 13219 9204 1160 -2897 92 C ATOM 689 CG ASP A 184 51.991 34.225 325.935 1.00107.61 C ANISOU 689 CG ASP A 184 14992 14882 11015 1183 -2893 146 C ATOM 690 OD1 ASP A 184 53.154 34.344 325.498 1.00116.27 O ANISOU 690 OD1 ASP A 184 15910 16065 12202 1182 -3002 36 O ATOM 691 OD2 ASP A 184 51.187 33.367 325.516 1.00106.23 O ANISOU 691 OD2 ASP A 184 14903 14613 10848 1198 -2779 286 O ATOM 692 N SER A 185 52.695 38.095 328.289 1.00103.08 N ANISOU 692 N SER A 185 14402 14493 10268 1023 -3098 -277 N ATOM 693 CA SER A 185 52.180 39.324 328.876 1.00 96.32 C ANISOU 693 CA SER A 185 13613 13622 9365 951 -3077 -360 C ATOM 694 C SER A 185 50.785 39.599 328.326 1.00 99.35 C ANISOU 694 C SER A 185 14073 13875 9801 873 -2893 -278 C ATOM 695 O SER A 185 50.139 38.694 327.788 1.00 85.59 O ANISOU 695 O SER A 185 12365 12069 8085 898 -2783 -143 O ATOM 696 CB SER A 185 53.132 40.484 328.588 1.00 89.65 C ANISOU 696 CB SER A 185 12618 12827 8619 828 -3167 -532 C ATOM 697 OG SER A 185 53.471 40.518 327.215 1.00 95.26 O ANISOU 697 OG SER A 185 13181 13501 9511 707 -3114 -531 O ATOM 698 N ARG A 186 50.301 40.835 328.462 1.00 98.75 N ANISOU 698 N ARG A 186 14025 13757 9740 787 -2865 -369 N ATOM 699 CA ARG A 186 49.009 41.186 327.883 1.00 84.31 C ANISOU 699 CA ARG A 186 12252 11809 7973 726 -2710 -319 C ATOM 700 C ARG A 186 49.125 41.392 326.378 1.00108.03 C ANISOU 700 C ARG A 186 15142 14726 11177 603 -2654 -301 C ATOM 701 O ARG A 186 48.307 40.876 325.608 1.00116.32 O ANISOU 701 O ARG A 186 16205 15698 12293 594 -2528 -195 O ATOM 702 CB ARG A 186 48.450 42.445 328.549 1.00 87.71 C ANISOU 702 CB ARG A 186 12759 12218 8349 697 -2718 -437 C ATOM 703 CG ARG A 186 47.000 42.732 328.188 1.00 89.65 C ANISOU 703 CG ARG A 186 13075 12363 8625 678 -2571 -405 C ATOM 704 CD ARG A 186 46.668 44.212 328.243 1.00106.68 C ANISOU 704 CD ARG A 186 15261 14453 10819 615 -2600 -546 C ATOM 705 NE ARG A 186 47.117 44.844 329.482 1.00118.43 N ANISOU 705 NE ARG A 186 16797 16024 12177 654 -2714 -669 N ATOM 706 CZ ARG A 186 48.228 45.565 329.610 1.00122.22 C ANISOU 706 CZ ARG A 186 17224 16530 12684 592 -2851 -779 C ATOM 707 NH1 ARG A 186 48.534 46.092 330.786 1.00127.64 N ANISOU 707 NH1 ARG A 186 17960 17295 13242 637 -2949 -891 N ATOM 708 NH2 ARG A 186 49.035 45.768 328.576 1.00115.22 N ANISOU 708 NH2 ARG A 186 16232 15600 11946 475 -2886 -785 N ATOM 709 N ASN A 187 50.141 42.139 325.942 1.00117.13 N ANISOU 709 N ASN A 187 16187 15898 12421 498 -2744 -408 N ATOM 710 CA ASN A 187 50.272 42.456 324.523 1.00116.66 C ANISOU 710 CA ASN A 187 16036 15755 12533 356 -2691 -399 C ATOM 711 C ASN A 187 50.711 41.240 323.717 1.00118.13 C ANISOU 711 C ASN A 187 16119 15977 12790 380 -2658 -302 C ATOM 712 O ASN A 187 50.176 40.983 322.631 1.00133.14 O ANISOU 712 O ASN A 187 18002 17790 14796 326 -2550 -220 O ATOM 713 CB ASN A 187 51.255 43.611 324.335 1.00112.37 C ANISOU 713 CB ASN A 187 15420 15229 12048 209 -2790 -547 C ATOM 714 CG ASN A 187 50.659 44.950 324.729 1.00121.40 C ANISOU 714 CG ASN A 187 16679 16279 13168 153 -2804 -636 C ATOM 715 OD1 ASN A 187 49.514 45.025 325.176 1.00124.37 O ANISOU 715 OD1 ASN A 187 17176 16596 13485 237 -2742 -602 O ATOM 716 ND2 ASN A 187 51.435 46.014 324.570 1.00124.47 N ANISOU 716 ND2 ASN A 187 17033 16658 13601 7 -2886 -762 N ATOM 717 N VAL A 188 51.682 40.478 324.226 1.00107.89 N ANISOU 717 N VAL A 188 14753 14806 11433 472 -2759 -319 N ATOM 718 CA VAL A 188 52.142 39.294 323.507 1.00109.67 C ANISOU 718 CA VAL A 188 14881 15067 11723 518 -2746 -244 C ATOM 719 C VAL A 188 51.010 38.289 323.349 1.00116.56 C ANISOU 719 C VAL A 188 15863 15855 12572 605 -2623 -78 C ATOM 720 O VAL A 188 50.951 37.555 322.354 1.00114.87 O ANISOU 720 O VAL A 188 15587 15604 12454 592 -2555 1 O ATOM 721 CB VAL A 188 53.354 38.674 324.228 1.00102.48 C ANISOU 721 CB VAL A 188 13895 14307 10736 636 -2904 -310 C ATOM 722 CG1 VAL A 188 53.784 37.374 323.558 1.00 92.61 C ANISOU 722 CG1 VAL A 188 12558 13088 9543 716 -2905 -239 C ATOM 723 CG2 VAL A 188 54.503 39.661 324.252 1.00117.54 C ANISOU 723 CG2 VAL A 188 15663 16313 12682 524 -3015 -491 C ATOM 724 N PHE A 189 50.095 38.235 324.318 1.00116.46 N ANISOU 724 N PHE A 189 16009 15815 12426 684 -2587 -31 N ATOM 725 CA PHE A 189 48.965 37.317 324.216 1.00105.24 C ANISOU 725 CA PHE A 189 14694 14322 10971 741 -2458 115 C ATOM 726 C PHE A 189 47.989 37.772 323.139 1.00105.04 C ANISOU 726 C PHE A 189 14655 14183 11073 633 -2316 148 C ATOM 727 O PHE A 189 47.600 36.987 322.267 1.00105.25 O ANISOU 727 O PHE A 189 14658 14155 11177 627 -2224 248 O ATOM 728 CB PHE A 189 48.256 37.198 325.568 1.00 88.87 C ANISOU 728 CB PHE A 189 12789 12270 8706 830 -2448 139 C ATOM 729 CG PHE A 189 47.031 36.329 325.528 1.00 88.74 C ANISOU 729 CG PHE A 189 12886 12191 8640 859 -2299 275 C ATOM 730 CD1 PHE A 189 47.126 34.963 325.737 1.00 85.83 C ANISOU 730 CD1 PHE A 189 12590 11825 8195 949 -2302 394 C ATOM 731 CD2 PHE A 189 45.786 36.877 325.265 1.00101.35 C ANISOU 731 CD2 PHE A 189 14519 13724 10267 793 -2162 273 C ATOM 732 CE1 PHE A 189 46.001 34.159 325.691 1.00 93.24 C ANISOU 732 CE1 PHE A 189 13640 12705 9083 950 -2158 515 C ATOM 733 CE2 PHE A 189 44.657 36.079 325.214 1.00106.55 C ANISOU 733 CE2 PHE A 189 15262 14342 10880 805 -2018 380 C ATOM 734 CZ PHE A 189 44.764 34.719 325.427 1.00105.58 C ANISOU 734 CZ PHE A 189 15215 14224 10678 871 -2009 505 C ATOM 735 N LEU A 190 47.583 39.044 323.185 1.00 91.83 N ANISOU 735 N LEU A 190 13003 12467 9420 554 -2307 58 N ATOM 736 CA LEU A 190 46.598 39.549 322.234 1.00 80.31 C ANISOU 736 CA LEU A 190 11553 10893 8070 472 -2194 77 C ATOM 737 C LEU A 190 47.138 39.547 320.811 1.00 90.17 C ANISOU 737 C LEU A 190 12684 12096 9482 365 -2181 93 C ATOM 738 O LEU A 190 46.372 39.354 319.859 1.00 99.24 O ANISOU 738 O LEU A 190 13832 13158 10718 329 -2075 161 O ATOM 739 CB LEU A 190 46.165 40.958 322.634 1.00 71.86 C ANISOU 739 CB LEU A 190 10545 9779 6981 427 -2221 -40 C ATOM 740 CG LEU A 190 45.535 41.069 324.022 1.00 78.82 C ANISOU 740 CG LEU A 190 11539 10713 7697 524 -2221 -76 C ATOM 741 CD1 LEU A 190 45.305 42.525 324.381 1.00 78.98 C ANISOU 741 CD1 LEU A 190 11607 10692 7711 485 -2275 -216 C ATOM 742 CD2 LEU A 190 44.233 40.289 324.094 1.00 76.62 C ANISOU 742 CD2 LEU A 190 11327 10418 7369 584 -2077 17 C ATOM 743 N PHE A 191 48.442 39.762 320.644 1.00 84.64 N ANISOU 743 N PHE A 191 11878 11463 8818 308 -2284 21 N ATOM 744 CA PHE A 191 49.037 39.691 319.314 1.00 85.94 C ANISOU 744 CA PHE A 191 11921 11611 9123 195 -2264 28 C ATOM 745 C PHE A 191 48.865 38.298 318.717 1.00 96.17 C ANISOU 745 C PHE A 191 13173 12910 10456 266 -2191 149 C ATOM 746 O PHE A 191 48.457 38.150 317.559 1.00 81.85 O ANISOU 746 O PHE A 191 11328 11022 8748 197 -2101 206 O ATOM 747 CB PHE A 191 50.514 40.078 319.386 1.00 88.88 C ANISOU 747 CB PHE A 191 12169 12092 9508 123 -2386 -92 C ATOM 748 CG PHE A 191 51.285 39.757 318.138 1.00105.14 C ANISOU 748 CG PHE A 191 14078 14183 11687 19 -2366 -96 C ATOM 749 CD1 PHE A 191 51.271 40.619 317.053 1.00100.06 C ANISOU 749 CD1 PHE A 191 13417 13459 11142 -168 -2319 -123 C ATOM 750 CD2 PHE A 191 52.027 38.589 318.050 1.00112.19 C ANISOU 750 CD2 PHE A 191 14857 15184 12586 109 -2399 -78 C ATOM 751 CE1 PHE A 191 51.983 40.318 315.902 1.00104.34 C ANISOU 751 CE1 PHE A 191 13821 14044 11781 -278 -2290 -132 C ATOM 752 CE2 PHE A 191 52.738 38.282 316.904 1.00 98.91 C ANISOU 752 CE2 PHE A 191 13021 13548 11011 17 -2376 -99 C ATOM 753 CZ PHE A 191 52.717 39.148 315.829 1.00102.82 C ANISOU 753 CZ PHE A 191 13491 13979 11598 -186 -2314 -126 C ATOM 754 N LYS A 192 49.174 37.260 319.497 1.00 98.07 N ANISOU 754 N LYS A 192 13427 13230 10606 406 -2237 190 N ATOM 755 CA LYS A 192 48.936 35.895 319.041 1.00 94.09 C ANISOU 755 CA LYS A 192 12916 12710 10124 485 -2175 309 C ATOM 756 C LYS A 192 47.467 35.684 318.698 1.00 97.02 C ANISOU 756 C LYS A 192 13387 12969 10508 479 -2026 412 C ATOM 757 O LYS A 192 47.132 35.219 317.603 1.00103.72 O ANISOU 757 O LYS A 192 14190 13760 11459 439 -1940 477 O ATOM 758 CB LYS A 192 49.375 34.896 320.111 1.00 95.42 C ANISOU 758 CB LYS A 192 13139 12954 10163 646 -2264 340 C ATOM 759 CG LYS A 192 50.870 34.836 320.366 1.00100.90 C ANISOU 759 CG LYS A 192 13711 13774 10852 686 -2423 234 C ATOM 760 CD LYS A 192 51.203 33.613 321.200 1.00107.10 C ANISOU 760 CD LYS A 192 14570 14604 11521 869 -2512 289 C ATOM 761 CE LYS A 192 52.701 33.444 321.407 1.00114.91 C ANISOU 761 CE LYS A 192 15420 15729 12510 939 -2687 168 C ATOM 762 NZ LYS A 192 53.216 34.326 322.487 1.00107.62 N ANISOU 762 NZ LYS A 192 14508 14892 11488 945 -2803 50 N ATOM 763 N LEU A 193 46.575 36.016 319.631 1.00 92.22 N ANISOU 763 N LEU A 193 12907 12342 9792 519 -1994 415 N ATOM 764 CA LEU A 193 45.149 35.819 319.397 1.00 94.16 C ANISOU 764 CA LEU A 193 13231 12506 10038 516 -1852 488 C ATOM 765 C LEU A 193 44.657 36.681 318.242 1.00 92.44 C ANISOU 765 C LEU A 193 12965 12201 9959 406 -1793 456 C ATOM 766 O LEU A 193 43.851 36.229 317.419 1.00 92.23 O ANISOU 766 O LEU A 193 12934 12109 10001 389 -1685 526 O ATOM 767 CB LEU A 193 44.369 36.129 320.674 1.00 93.52 C ANISOU 767 CB LEU A 193 13277 12450 9807 570 -1834 463 C ATOM 768 CG LEU A 193 42.845 36.044 320.590 1.00 86.34 C ANISOU 768 CG LEU A 193 12435 11489 8883 565 -1686 500 C ATOM 769 CD1 LEU A 193 42.390 34.695 320.067 1.00 88.36 C ANISOU 769 CD1 LEU A 193 12700 11715 9157 582 -1583 630 C ATOM 770 CD2 LEU A 193 42.251 36.309 321.958 1.00 77.82 C ANISOU 770 CD2 LEU A 193 11468 10468 7634 616 -1675 456 C ATOM 771 N GLY A 194 45.128 37.926 318.164 1.00 92.52 N ANISOU 771 N GLY A 194 12951 12199 10003 328 -1868 350 N ATOM 772 CA GLY A 194 44.743 38.783 317.056 1.00 88.76 C ANISOU 772 CA GLY A 194 12460 11621 9645 220 -1833 323 C ATOM 773 C GLY A 194 45.184 38.228 315.715 1.00 81.77 C ANISOU 773 C GLY A 194 11475 10714 8881 149 -1796 382 C ATOM 774 O GLY A 194 44.454 38.317 314.726 1.00 75.49 O ANISOU 774 O GLY A 194 10685 9828 8168 103 -1719 419 O ATOM 775 N GLY A 195 46.385 37.651 315.662 1.00 78.32 N ANISOU 775 N GLY A 195 10939 10366 8452 147 -1856 378 N ATOM 776 CA GLY A 195 46.834 37.021 314.432 1.00 71.40 C ANISOU 776 CA GLY A 195 9956 9491 7683 90 -1818 423 C ATOM 777 C GLY A 195 45.877 35.941 313.964 1.00 90.77 C ANISOU 777 C GLY A 195 12433 11892 10162 157 -1705 540 C ATOM 778 O GLY A 195 45.491 35.896 312.793 1.00100.18 O ANISOU 778 O GLY A 195 13595 13018 11452 88 -1632 578 O ATOM 779 N VAL A 196 45.476 35.055 314.879 1.00 85.84 N ANISOU 779 N VAL A 196 11875 11296 9443 283 -1688 600 N ATOM 780 CA VAL A 196 44.494 34.030 314.536 1.00 79.86 C ANISOU 780 CA VAL A 196 11158 10487 8697 332 -1574 708 C ATOM 781 C VAL A 196 43.172 34.679 314.155 1.00 82.82 C ANISOU 781 C VAL A 196 11588 10775 9104 287 -1479 707 C ATOM 782 O VAL A 196 42.519 34.272 313.186 1.00 95.75 O ANISOU 782 O VAL A 196 13204 12354 10823 261 -1388 761 O ATOM 783 CB VAL A 196 44.326 33.042 315.705 1.00 85.70 C ANISOU 783 CB VAL A 196 11992 11268 9304 453 -1579 768 C ATOM 784 CG1 VAL A 196 43.232 32.023 315.403 1.00 85.73 C ANISOU 784 CG1 VAL A 196 12053 11212 9308 477 -1449 876 C ATOM 785 CG2 VAL A 196 45.639 32.339 315.986 1.00 85.20 C ANISOU 785 CG2 VAL A 196 11876 11280 9216 522 -1694 763 C ATOM 786 N THR A 197 42.757 35.698 314.909 1.00 75.28 N ANISOU 786 N THR A 197 10702 9815 8086 289 -1506 632 N ATOM 787 CA THR A 197 41.534 36.416 314.571 1.00 74.18 C ANISOU 787 CA THR A 197 10609 9598 7979 267 -1440 602 C ATOM 788 C THR A 197 41.644 37.059 313.193 1.00 81.48 C ANISOU 788 C THR A 197 11488 10437 9034 166 -1446 586 C ATOM 789 O THR A 197 40.686 37.036 312.411 1.00 68.82 O ANISOU 789 O THR A 197 9891 8763 7493 158 -1370 609 O ATOM 790 CB THR A 197 41.234 37.465 315.644 1.00 63.56 C ANISOU 790 CB THR A 197 9340 8266 6542 295 -1493 502 C ATOM 791 OG1 THR A 197 40.898 36.804 316.870 1.00 76.45 O ANISOU 791 OG1 THR A 197 11031 9977 8039 381 -1461 525 O ATOM 792 CG2 THR A 197 40.077 38.378 315.234 1.00 57.02 C ANISOU 792 CG2 THR A 197 8554 7354 5759 285 -1457 439 C ATOM 793 N ALA A 198 42.808 37.627 312.872 1.00 80.11 N ANISOU 793 N ALA A 198 11268 10273 8897 81 -1535 542 N ATOM 794 CA ALA A 198 42.999 38.230 311.556 1.00 70.67 C ANISOU 794 CA ALA A 198 10048 8997 7807 -40 -1538 533 C ATOM 795 C ALA A 198 42.969 37.174 310.459 1.00 80.19 C ANISOU 795 C ALA A 198 11175 10200 9093 -55 -1457 621 C ATOM 796 O ALA A 198 42.450 37.422 309.364 1.00 87.78 O ANISOU 796 O ALA A 198 12146 11076 10130 -115 -1414 641 O ATOM 797 CB ALA A 198 44.317 39.003 311.518 1.00 62.32 C ANISOU 797 CB ALA A 198 8954 7970 6754 -153 -1639 459 C ATOM 798 N SER A 199 43.518 35.988 310.734 1.00 79.97 N ANISOU 798 N SER A 199 11078 10260 9046 5 -1444 672 N ATOM 799 CA SER A 199 43.548 34.934 309.724 1.00 78.54 C ANISOU 799 CA SER A 199 10822 10078 8942 -1 -1375 747 C ATOM 800 C SER A 199 42.140 34.562 309.280 1.00 81.62 C ANISOU 800 C SER A 199 11261 10390 9360 35 -1268 808 C ATOM 801 O SER A 199 41.874 34.419 308.080 1.00 82.22 O ANISOU 801 O SER A 199 11302 10415 9524 -20 -1216 838 O ATOM 802 CB SER A 199 44.283 33.709 310.270 1.00 86.71 C ANISOU 802 CB SER A 199 11803 11205 9936 90 -1398 784 C ATOM 803 OG SER A 199 44.169 32.608 309.384 1.00102.87 O ANISOU 803 OG SER A 199 13794 13240 12051 105 -1330 856 O ATOM 804 N PHE A 200 41.219 34.421 310.234 1.00 74.96 N ANISOU 804 N PHE A 200 10494 9548 8439 121 -1231 815 N ATOM 805 CA PHE A 200 39.847 34.071 309.891 1.00 67.61 C ANISOU 805 CA PHE A 200 9593 8567 7529 150 -1125 850 C ATOM 806 C PHE A 200 39.115 35.254 309.278 1.00 71.18 C ANISOU 806 C PHE A 200 10078 8934 8032 108 -1133 785 C ATOM 807 O PHE A 200 38.287 35.080 308.376 1.00 71.88 O ANISOU 807 O PHE A 200 10155 8968 8187 100 -1068 806 O ATOM 808 CB PHE A 200 39.111 33.586 311.134 1.00 50.97 C ANISOU 808 CB PHE A 200 7553 6506 5309 234 -1076 860 C ATOM 809 CG PHE A 200 37.705 33.154 310.868 1.00 66.20 C ANISOU 809 CG PHE A 200 9495 8410 7250 252 -955 879 C ATOM 810 CD1 PHE A 200 37.449 32.015 310.127 1.00 60.86 C ANISOU 810 CD1 PHE A 200 8780 7716 6627 243 -872 962 C ATOM 811 CD2 PHE A 200 36.641 33.883 311.362 1.00 68.09 C ANISOU 811 CD2 PHE A 200 9775 8650 7445 279 -928 799 C ATOM 812 CE1 PHE A 200 36.154 31.609 309.881 1.00 71.37 C ANISOU 812 CE1 PHE A 200 10114 9035 7969 248 -758 968 C ATOM 813 CE2 PHE A 200 35.341 33.484 311.124 1.00 67.32 C ANISOU 813 CE2 PHE A 200 9668 8553 7358 293 -815 794 C ATOM 814 CZ PHE A 200 35.096 32.343 310.381 1.00 69.31 C ANISOU 814 CZ PHE A 200 9881 8791 7665 270 -727 880 C ATOM 815 N THR A 201 39.403 36.463 309.759 1.00 74.91 N ANISOU 815 N THR A 201 10602 9389 8470 88 -1223 702 N ATOM 816 CA THR A 201 38.753 37.650 309.216 1.00 80.98 C ANISOU 816 CA THR A 201 11432 10057 9279 60 -1257 635 C ATOM 817 C THR A 201 39.063 37.799 307.734 1.00 72.93 C ANISOU 817 C THR A 201 10390 8960 8359 -40 -1262 669 C ATOM 818 O THR A 201 38.156 37.958 306.909 1.00 70.01 O ANISOU 818 O THR A 201 10045 8514 8043 -32 -1231 670 O ATOM 819 CB THR A 201 39.204 38.895 309.980 1.00 87.87 C ANISOU 819 CB THR A 201 12376 10913 10097 44 -1368 542 C ATOM 820 OG1 THR A 201 39.391 38.574 311.362 1.00 86.74 O ANISOU 820 OG1 THR A 201 12236 10871 9852 115 -1373 525 O ATOM 821 CG2 THR A 201 38.163 40.004 309.858 1.00 77.40 C ANISOU 821 CG2 THR A 201 11142 9485 8780 79 -1404 456 C ATOM 822 N ALA A 202 40.349 37.750 307.378 1.00 71.65 N ANISOU 822 N ALA A 202 10179 8829 8216 -137 -1302 687 N ATOM 823 CA ALA A 202 40.734 37.841 305.975 1.00 78.21 C ANISOU 823 CA ALA A 202 10985 9607 9126 -252 -1295 717 C ATOM 824 C ALA A 202 40.154 36.693 305.163 1.00 78.05 C ANISOU 824 C ALA A 202 10899 9592 9164 -217 -1194 794 C ATOM 825 O ALA A 202 39.812 36.874 303.988 1.00 71.28 O ANISOU 825 O ALA A 202 10057 8659 8367 -274 -1175 813 O ATOM 826 CB ALA A 202 42.257 37.863 305.849 1.00 75.74 C ANISOU 826 CB ALA A 202 10600 9367 8813 -365 -1341 704 C ATOM 827 N SER A 203 40.036 35.507 305.765 1.00 68.12 N ANISOU 827 N SER A 203 9583 8416 7884 -126 -1133 841 N ATOM 828 CA SER A 203 39.428 34.379 305.066 1.00 73.06 C ANISOU 828 CA SER A 203 10157 9040 8562 -93 -1035 910 C ATOM 829 C SER A 203 37.981 34.685 304.696 1.00 72.22 C ANISOU 829 C SER A 203 10102 8858 8479 -54 -989 894 C ATOM 830 O SER A 203 37.565 34.485 303.549 1.00 69.93 O ANISOU 830 O SER A 203 9792 8518 8259 -84 -950 920 O ATOM 831 CB SER A 203 39.516 33.120 305.928 1.00 54.62 C ANISOU 831 CB SER A 203 7789 6784 6179 -6 -990 961 C ATOM 832 OG SER A 203 40.862 32.705 306.081 1.00 70.31 O ANISOU 832 OG SER A 203 9714 8843 8159 -23 -1043 969 O ATOM 833 N VAL A 204 37.199 35.180 305.658 1.00 70.82 N ANISOU 833 N VAL A 204 9985 8682 8242 19 -998 838 N ATOM 834 CA VAL A 204 35.828 35.583 305.358 1.00 65.61 C ANISOU 834 CA VAL A 204 9359 7966 7604 70 -970 789 C ATOM 835 C VAL A 204 35.828 36.781 304.419 1.00 60.16 C ANISOU 835 C VAL A 204 8736 7161 6961 17 -1057 745 C ATOM 836 O VAL A 204 35.016 36.858 303.489 1.00 68.85 O ANISOU 836 O VAL A 204 9846 8198 8116 30 -1041 738 O ATOM 837 CB VAL A 204 35.058 35.879 306.660 1.00 66.59 C ANISOU 837 CB VAL A 204 9520 8138 7643 160 -961 715 C ATOM 838 CG1 VAL A 204 33.633 36.330 306.357 1.00 61.92 C ANISOU 838 CG1 VAL A 204 8942 7509 7076 226 -941 633 C ATOM 839 CG2 VAL A 204 35.040 34.647 307.564 1.00 54.99 C ANISOU 839 CG2 VAL A 204 8014 6771 6107 194 -871 771 C ATOM 840 N GLY A 205 36.738 37.733 304.639 1.00 54.30 N ANISOU 840 N GLY A 205 8054 6386 6191 -48 -1156 714 N ATOM 841 CA GLY A 205 36.831 38.877 303.749 1.00 64.10 C ANISOU 841 CA GLY A 205 9394 7500 7462 -123 -1245 684 C ATOM 842 C GLY A 205 37.167 38.489 302.322 1.00 71.38 C ANISOU 842 C GLY A 205 10287 8385 8449 -222 -1214 754 C ATOM 843 O GLY A 205 36.724 39.144 301.374 1.00 63.77 O ANISOU 843 O GLY A 205 9409 7306 7513 -252 -1258 743 O ATOM 844 N SER A 206 37.947 37.419 302.147 1.00 75.77 N ANISOU 844 N SER A 206 10728 9037 9024 -267 -1145 821 N ATOM 845 CA SER A 206 38.274 36.949 300.804 1.00 66.86 C ANISOU 845 CA SER A 206 9556 7895 7955 -358 -1104 879 C ATOM 846 C SER A 206 37.067 36.295 300.142 1.00 78.12 C ANISOU 846 C SER A 206 10958 9293 9431 -279 -1033 905 C ATOM 847 O SER A 206 36.812 36.512 298.950 1.00 90.64 O ANISOU 847 O SER A 206 12580 10804 11056 -332 -1039 920 O ATOM 848 CB SER A 206 39.452 35.975 300.866 1.00 64.07 C ANISOU 848 CB SER A 206 9075 7661 7609 -406 -1061 920 C ATOM 849 OG SER A 206 40.646 36.633 301.259 1.00 62.94 O ANISOU 849 OG SER A 206 8936 7552 7426 -501 -1131 881 O ATOM 850 N LEU A 207 36.311 35.489 300.895 1.00 67.76 N ANISOU 850 N LEU A 207 9591 8044 8112 -164 -964 906 N ATOM 851 CA LEU A 207 35.096 34.898 300.341 1.00 65.54 C ANISOU 851 CA LEU A 207 9280 7748 7875 -97 -893 911 C ATOM 852 C LEU A 207 34.072 35.969 300.003 1.00 67.49 C ANISOU 852 C LEU A 207 9619 7896 8127 -48 -960 835 C ATOM 853 O LEU A 207 33.236 35.772 299.114 1.00 78.39 O ANISOU 853 O LEU A 207 10989 9238 9556 -20 -936 830 O ATOM 854 CB LEU A 207 34.499 33.888 301.322 1.00 67.58 C ANISOU 854 CB LEU A 207 9474 8096 8105 -8 -801 919 C ATOM 855 CG LEU A 207 35.347 32.660 301.665 1.00 80.24 C ANISOU 855 CG LEU A 207 11006 9781 9699 -26 -743 996 C ATOM 856 CD1 LEU A 207 34.581 31.728 302.601 1.00 83.20 C ANISOU 856 CD1 LEU A 207 11363 10219 10031 49 -653 1008 C ATOM 857 CD2 LEU A 207 35.781 31.921 300.405 1.00 75.19 C ANISOU 857 CD2 LEU A 207 10304 9132 9134 -87 -706 1057 C ATOM 858 N PHE A 208 34.124 37.107 300.697 1.00 60.97 N ANISOU 858 N PHE A 208 8887 7026 7253 -28 -1055 767 N ATOM 859 CA PHE A 208 33.231 38.214 300.377 1.00 53.48 C ANISOU 859 CA PHE A 208 8047 5966 6308 34 -1147 683 C ATOM 860 C PHE A 208 33.601 38.842 299.039 1.00 59.09 C ANISOU 860 C PHE A 208 8858 6549 7045 -65 -1222 716 C ATOM 861 O PHE A 208 32.733 39.080 298.191 1.00 56.69 O ANISOU 861 O PHE A 208 8601 6166 6772 -16 -1255 690 O ATOM 862 CB PHE A 208 33.276 39.253 301.494 1.00 55.28 C ANISOU 862 CB PHE A 208 8359 6173 6473 80 -1237 597 C ATOM 863 CG PHE A 208 32.344 40.409 301.282 1.00 66.76 C ANISOU 863 CG PHE A 208 9932 7507 7927 170 -1351 492 C ATOM 864 CD1 PHE A 208 30.977 40.252 301.447 1.00 71.25 C ANISOU 864 CD1 PHE A 208 10450 8112 8511 316 -1325 401 C ATOM 865 CD2 PHE A 208 32.834 41.653 300.927 1.00 67.55 C ANISOU 865 CD2 PHE A 208 10199 7459 8007 109 -1489 473 C ATOM 866 CE1 PHE A 208 30.115 41.317 301.255 1.00 71.66 C ANISOU 866 CE1 PHE A 208 10605 8058 8565 425 -1448 283 C ATOM 867 CE2 PHE A 208 31.981 42.724 300.736 1.00 78.52 C ANISOU 867 CE2 PHE A 208 11721 8718 9393 210 -1616 372 C ATOM 868 CZ PHE A 208 30.616 42.556 300.901 1.00 75.17 C ANISOU 868 CZ PHE A 208 11235 8336 8990 382 -1603 272 C ATOM 869 N LEU A 209 34.891 39.121 298.832 1.00 62.98 N ANISOU 869 N LEU A 209 9386 7027 7517 -211 -1250 767 N ATOM 870 CA LEU A 209 35.331 39.689 297.563 1.00 63.51 C ANISOU 870 CA LEU A 209 9557 6982 7590 -341 -1306 805 C ATOM 871 C LEU A 209 35.071 38.736 296.407 1.00 76.94 C ANISOU 871 C LEU A 209 11179 8710 9346 -360 -1223 867 C ATOM 872 O LEU A 209 34.756 39.178 295.294 1.00 75.55 O ANISOU 872 O LEU A 209 11104 8425 9176 -398 -1272 878 O ATOM 873 CB LEU A 209 36.818 40.040 297.630 1.00 46.99 C ANISOU 873 CB LEU A 209 7485 4909 5461 -516 -1326 834 C ATOM 874 CG LEU A 209 37.216 41.193 298.550 1.00 65.47 C ANISOU 874 CG LEU A 209 9938 7194 7743 -538 -1430 772 C ATOM 875 CD1 LEU A 209 38.725 41.389 298.498 1.00 64.35 C ANISOU 875 CD1 LEU A 209 9782 7099 7570 -733 -1431 794 C ATOM 876 CD2 LEU A 209 36.492 42.486 298.176 1.00 69.51 C ANISOU 876 CD2 LEU A 209 10664 7515 8232 -510 -1562 720 C ATOM 877 N ALA A 210 35.195 37.431 296.645 1.00 64.29 N ANISOU 877 N ALA A 210 9410 7241 7777 -334 -1104 908 N ATOM 878 CA ALA A 210 34.898 36.469 295.591 1.00 68.25 C ANISOU 878 CA ALA A 210 9832 7768 8334 -343 -1024 958 C ATOM 879 C ALA A 210 33.433 36.543 295.187 1.00 59.08 C ANISOU 879 C ALA A 210 8698 6547 7201 -221 -1037 912 C ATOM 880 O ALA A 210 33.108 36.496 293.995 1.00 72.31 O ANISOU 880 O ALA A 210 10404 8167 8905 -246 -1045 932 O ATOM 881 CB ALA A 210 35.262 35.059 296.049 1.00 69.65 C ANISOU 881 CB ALA A 210 9845 8083 8537 -323 -907 1002 C ATOM 882 N ALA A 211 32.532 36.669 296.165 1.00 62.73 N ANISOU 882 N ALA A 211 9147 7034 7654 -86 -1042 839 N ATOM 883 CA ALA A 211 31.117 36.816 295.843 1.00 54.04 C ANISOU 883 CA ALA A 211 8055 5898 6581 39 -1063 763 C ATOM 884 C ALA A 211 30.885 38.023 294.944 1.00 69.78 C ANISOU 884 C ALA A 211 10220 7732 8562 37 -1207 731 C ATOM 885 O ALA A 211 30.095 37.957 293.994 1.00 74.31 O ANISOU 885 O ALA A 211 10808 8259 9169 86 -1229 712 O ATOM 886 CB ALA A 211 30.294 36.932 297.124 1.00 52.28 C ANISOU 886 CB ALA A 211 7791 5739 6333 169 -1052 666 C ATOM 887 N ILE A 212 31.578 39.133 295.217 1.00 72.94 N ANISOU 887 N ILE A 212 10764 8039 8910 -24 -1314 725 N ATOM 888 CA ILE A 212 31.425 40.330 294.396 1.00 64.28 C ANISOU 888 CA ILE A 212 9875 6764 7787 -40 -1464 704 C ATOM 889 C ILE A 212 31.887 40.057 292.973 1.00 74.28 C ANISOU 889 C ILE A 212 11181 7983 9060 -175 -1446 796 C ATOM 890 O ILE A 212 31.221 40.443 292.004 1.00 61.18 O ANISOU 890 O ILE A 212 9631 6214 7401 -135 -1527 781 O ATOM 891 CB ILE A 212 32.188 41.510 295.030 1.00 64.44 C ANISOU 891 CB ILE A 212 10049 6694 7744 -108 -1570 686 C ATOM 892 CG1 ILE A 212 31.484 41.942 296.319 1.00 72.91 C ANISOU 892 CG1 ILE A 212 11108 7792 8804 55 -1614 569 C ATOM 893 CG2 ILE A 212 32.283 42.693 294.071 1.00 63.58 C ANISOU 893 CG2 ILE A 212 10190 6378 7591 -178 -1722 694 C ATOM 894 CD1 ILE A 212 32.215 43.012 297.120 1.00 83.41 C ANISOU 894 CD1 ILE A 212 12567 9050 10074 1 -1710 540 C ATOM 895 N ASP A 213 33.034 39.391 292.822 1.00 69.19 N ANISOU 895 N ASP A 213 10449 7426 8415 -330 -1347 883 N ATOM 896 CA ASP A 213 33.524 39.059 291.489 1.00 68.45 C ANISOU 896 CA ASP A 213 10371 7314 8322 -467 -1313 960 C ATOM 897 C ASP A 213 32.504 38.235 290.720 1.00 76.75 C ANISOU 897 C ASP A 213 11338 8392 9431 -366 -1264 956 C ATOM 898 O ASP A 213 32.268 38.473 289.529 1.00 68.60 O ANISOU 898 O ASP A 213 10408 7271 8386 -405 -1312 979 O ATOM 899 CB ASP A 213 34.845 38.303 291.588 1.00 47.26 C ANISOU 899 CB ASP A 213 7554 4761 5641 -616 -1203 1023 C ATOM 900 CG ASP A 213 35.237 37.650 290.284 1.00 63.86 C ANISOU 900 CG ASP A 213 9613 6894 7757 -731 -1135 1085 C ATOM 901 OD1 ASP A 213 35.844 38.356 289.452 1.00 66.86 O ANISOU 901 OD1 ASP A 213 10131 7195 8080 -893 -1183 1115 O ATOM 902 OD2 ASP A 213 34.938 36.453 290.071 1.00 62.05 O ANISOU 902 OD2 ASP A 213 9224 6764 7588 -671 -1033 1102 O ATOM 903 N ARG A 214 31.892 37.255 291.386 1.00 68.96 N ANISOU 903 N ARG A 214 10175 7528 8500 -246 -1168 927 N ATOM 904 CA ARG A 214 30.885 36.433 290.727 1.00 73.65 C ANISOU 904 CA ARG A 214 10676 8158 9151 -157 -1113 911 C ATOM 905 C ARG A 214 29.625 37.230 290.429 1.00 69.94 C ANISOU 905 C ARG A 214 10311 7586 8679 -15 -1235 818 C ATOM 906 O ARG A 214 28.972 36.992 289.407 1.00 63.59 O ANISOU 906 O ARG A 214 9510 6753 7900 20 -1249 809 O ATOM 907 CB ARG A 214 30.560 35.214 291.591 1.00 56.73 C ANISOU 907 CB ARG A 214 8336 6164 7054 -87 -978 900 C ATOM 908 CG ARG A 214 31.677 34.184 291.650 1.00 40.08 C ANISOU 908 CG ARG A 214 6116 4153 4958 -197 -865 988 C ATOM 909 CD ARG A 214 31.912 33.550 290.284 1.00 62.85 C ANISOU 909 CD ARG A 214 8968 7038 7875 -278 -821 1043 C ATOM 910 NE ARG A 214 32.886 34.286 289.483 1.00 53.81 N ANISOU 910 NE ARG A 214 7937 5826 6684 -424 -882 1086 N ATOM 911 CZ ARG A 214 33.144 34.034 288.203 1.00 59.93 C ANISOU 911 CZ ARG A 214 8723 6587 7462 -515 -864 1126 C ATOM 912 NH1 ARG A 214 32.496 33.066 287.568 1.00 60.84 N ANISOU 912 NH1 ARG A 214 8741 6744 7633 -462 -795 1128 N ATOM 913 NH2 ARG A 214 34.051 34.752 287.555 1.00 69.55 N ANISOU 913 NH2 ARG A 214 10053 7752 8620 -672 -910 1160 N ATOM 914 N TYR A 215 29.272 38.182 291.293 1.00 57.27 N ANISOU 914 N TYR A 215 8790 5926 7043 77 -1333 737 N ATOM 915 CA TYR A 215 28.119 39.029 291.008 1.00 75.18 C ANISOU 915 CA TYR A 215 11167 8090 9307 231 -1475 629 C ATOM 916 C TYR A 215 28.358 39.881 289.769 1.00 78.78 C ANISOU 916 C TYR A 215 11847 8367 9718 163 -1611 673 C ATOM 917 O TYR A 215 27.434 40.110 288.980 1.00 71.85 O ANISOU 917 O TYR A 215 11032 7417 8849 271 -1702 618 O ATOM 918 CB TYR A 215 27.796 39.909 292.214 1.00 59.38 C ANISOU 918 CB TYR A 215 9217 6065 7278 342 -1559 524 C ATOM 919 CG TYR A 215 26.738 39.330 293.132 1.00 86.22 C ANISOU 919 CG TYR A 215 12431 9613 10717 496 -1481 409 C ATOM 920 CD1 TYR A 215 25.388 39.541 292.887 1.00100.41 C ANISOU 920 CD1 TYR A 215 14202 11407 12540 673 -1550 270 C ATOM 921 CD2 TYR A 215 27.090 38.576 294.243 1.00101.37 C ANISOU 921 CD2 TYR A 215 14203 11679 12635 460 -1340 430 C ATOM 922 CE1 TYR A 215 24.416 39.015 293.724 1.00104.62 C ANISOU 922 CE1 TYR A 215 14554 12097 13101 790 -1464 148 C ATOM 923 CE2 TYR A 215 26.127 38.047 295.086 1.00101.12 C ANISOU 923 CE2 TYR A 215 14016 11784 12619 573 -1257 327 C ATOM 924 CZ TYR A 215 24.792 38.270 294.823 1.00 96.62 C ANISOU 924 CZ TYR A 215 13409 11225 12077 728 -1311 182 C ATOM 925 OH TYR A 215 23.826 37.747 295.656 1.00 92.08 O ANISOU 925 OH TYR A 215 12668 10808 11511 818 -1215 63 O ATOM 926 N ILE A 216 29.593 40.351 289.571 1.00 72.95 N ANISOU 926 N ILE A 216 11237 7560 8923 -23 -1628 767 N ATOM 927 CA ILE A 216 29.910 41.107 288.362 1.00 72.54 C ANISOU 927 CA ILE A 216 11415 7340 8808 -130 -1739 824 C ATOM 928 C ILE A 216 29.882 40.195 287.141 1.00 71.82 C ANISOU 928 C ILE A 216 11249 7300 8740 -194 -1655 889 C ATOM 929 O ILE A 216 29.413 40.589 286.067 1.00 51.03 O ANISOU 929 O ILE A 216 8766 4547 6074 -176 -1756 893 O ATOM 930 CB ILE A 216 31.273 41.808 288.513 1.00 66.49 C ANISOU 930 CB ILE A 216 10787 6508 7967 -343 -1757 898 C ATOM 931 CG1 ILE A 216 31.221 42.807 289.672 1.00 65.67 C ANISOU 931 CG1 ILE A 216 10783 6332 7837 -269 -1862 823 C ATOM 932 CG2 ILE A 216 31.661 42.514 287.213 1.00 55.05 C ANISOU 932 CG2 ILE A 216 9587 4893 6435 -497 -1850 968 C ATOM 933 CD1 ILE A 216 32.546 43.499 289.979 1.00 55.28 C ANISOU 933 CD1 ILE A 216 9586 4967 6452 -480 -1877 877 C ATOM 934 N SER A 217 30.398 38.971 287.280 1.00 67.11 N ANISOU 934 N SER A 217 10431 6875 8195 -266 -1479 940 N ATOM 935 CA SER A 217 30.365 38.023 286.171 1.00 50.78 C ANISOU 935 CA SER A 217 8273 4866 6154 -318 -1392 990 C ATOM 936 C SER A 217 28.931 37.712 285.760 1.00 65.96 C ANISOU 936 C SER A 217 10146 6787 8127 -131 -1428 911 C ATOM 937 O SER A 217 28.634 37.575 284.568 1.00 74.91 O ANISOU 937 O SER A 217 11334 7877 9252 -145 -1456 931 O ATOM 938 CB SER A 217 31.102 36.740 286.556 1.00 60.58 C ANISOU 938 CB SER A 217 9283 6288 7449 -394 -1211 1038 C ATOM 939 OG SER A 217 31.079 35.810 285.489 1.00 72.97 O ANISOU 939 OG SER A 217 10765 7913 9048 -440 -1129 1078 O ATOM 940 N ILE A 218 28.026 37.607 286.733 1.00 54.56 N ANISOU 940 N ILE A 218 8596 5401 6732 42 -1427 811 N ATOM 941 CA ILE A 218 26.635 37.284 286.432 1.00 51.23 C ANISOU 941 CA ILE A 218 8094 5008 6361 219 -1451 708 C ATOM 942 C ILE A 218 25.939 38.475 285.784 1.00 51.66 C ANISOU 942 C ILE A 218 8369 4891 6370 327 -1662 642 C ATOM 943 O ILE A 218 25.316 38.349 284.724 1.00 71.04 O ANISOU 943 O ILE A 218 10856 7308 8830 379 -1716 623 O ATOM 944 CB ILE A 218 25.915 36.826 287.714 1.00 53.51 C ANISOU 944 CB ILE A 218 8198 5431 6704 348 -1374 608 C ATOM 945 CG1 ILE A 218 26.509 35.494 288.189 1.00 47.95 C ANISOU 945 CG1 ILE A 218 7298 4881 6040 248 -1174 683 C ATOM 946 CG2 ILE A 218 24.416 36.682 287.487 1.00 47.28 C ANISOU 946 CG2 ILE A 218 7325 4680 5961 532 -1414 467 C ATOM 947 CD1 ILE A 218 26.118 35.090 289.605 1.00 45.33 C ANISOU 947 CD1 ILE A 218 6825 4670 5728 321 -1087 617 C ATOM 948 N HIS A 219 26.048 39.653 286.402 1.00 69.20 N ANISOU 948 N HIS A 219 10757 6995 8540 367 -1795 603 N ATOM 949 CA HIS A 219 25.297 40.817 285.942 1.00 73.02 C ANISOU 949 CA HIS A 219 11463 7302 8980 507 -2018 520 C ATOM 950 C HIS A 219 25.925 41.489 284.725 1.00 75.40 C ANISOU 950 C HIS A 219 12040 7417 9191 368 -2129 629 C ATOM 951 O HIS A 219 25.204 42.082 283.915 1.00 71.16 O ANISOU 951 O HIS A 219 11673 6743 8620 480 -2299 581 O ATOM 952 CB HIS A 219 25.167 41.836 287.075 1.00 70.50 C ANISOU 952 CB HIS A 219 11233 6916 8637 609 -2128 430 C ATOM 953 CG HIS A 219 24.150 41.466 288.108 1.00 81.31 C ANISOU 953 CG HIS A 219 12382 8438 10075 800 -2080 274 C ATOM 954 ND1 HIS A 219 24.495 41.022 289.367 1.00 96.24 N ANISOU 954 ND1 HIS A 219 14108 10471 11987 765 -1940 269 N ATOM 955 CD2 HIS A 219 22.797 41.480 288.072 1.00 95.07 C ANISOU 955 CD2 HIS A 219 14041 10223 11860 1022 -2152 107 C ATOM 956 CE1 HIS A 219 23.398 40.775 290.061 1.00101.57 C ANISOU 956 CE1 HIS A 219 14615 11269 12708 941 -1917 113 C ATOM 957 NE2 HIS A 219 22.354 41.046 289.298 1.00 98.38 N ANISOU 957 NE2 HIS A 219 14243 10815 12320 1098 -2041 5 N ATOM 958 N ARG A 220 27.248 41.428 284.585 1.00 80.93 N ANISOU 958 N ARG A 220 12793 8113 9844 126 -2042 764 N ATOM 959 CA ARG A 220 27.962 42.083 283.487 1.00 67.17 C ANISOU 959 CA ARG A 220 11318 6207 7997 -53 -2124 870 C ATOM 960 C ARG A 220 28.843 41.071 282.763 1.00 71.49 C ANISOU 960 C ARG A 220 11739 6878 8545 -262 -1945 983 C ATOM 961 O ARG A 220 30.060 41.248 282.658 1.00 87.53 O ANISOU 961 O ARG A 220 13838 8903 10516 -491 -1887 1075 O ATOM 962 CB ARG A 220 28.799 43.249 284.011 1.00 49.30 C ANISOU 962 CB ARG A 220 9280 3801 5650 -174 -2214 904 C ATOM 963 CG ARG A 220 28.012 44.307 284.753 1.00 70.02 C ANISOU 963 CG ARG A 220 12044 6291 8268 32 -2402 785 C ATOM 964 CD ARG A 220 27.000 45.004 283.858 1.00 75.00 C ANISOU 964 CD ARG A 220 12904 6737 8857 195 -2618 728 C ATOM 965 NE ARG A 220 27.609 45.529 282.635 1.00 79.81 N ANISOU 965 NE ARG A 220 13807 7171 9348 2 -2695 849 N ATOM 966 CZ ARG A 220 28.339 46.638 282.575 1.00 81.04 C ANISOU 966 CZ ARG A 220 14273 7128 9393 -153 -2806 912 C ATOM 967 NH1 ARG A 220 28.565 47.352 283.669 1.00 73.41 N ANISOU 967 NH1 ARG A 220 13358 6108 8426 -127 -2861 861 N ATOM 968 NH2 ARG A 220 28.854 47.034 281.421 1.00 55.66 N ANISOU 968 NH2 ARG A 220 11323 3766 6057 -348 -2859 1024 N ATOM 969 N PRO A 221 28.257 39.995 282.235 1.00 64.62 N ANISOU 969 N PRO A 221 10680 6130 7744 -191 -1854 967 N ATOM 970 CA PRO A 221 29.094 38.986 281.567 1.00 66.88 C ANISOU 970 CA PRO A 221 10835 6538 8036 -375 -1686 1060 C ATOM 971 C PRO A 221 29.916 39.553 280.423 1.00 52.76 C ANISOU 971 C PRO A 221 9280 4637 6128 -592 -1730 1158 C ATOM 972 O PRO A 221 31.050 39.107 280.209 1.00 65.82 O ANISOU 972 O PRO A 221 10865 6385 7761 -802 -1598 1232 O ATOM 973 CB PRO A 221 28.074 37.950 281.071 1.00 44.20 C ANISOU 973 CB PRO A 221 7780 3767 5247 -231 -1631 1006 C ATOM 974 CG PRO A 221 26.813 38.711 280.908 1.00 50.68 C ANISOU 974 CG PRO A 221 8733 4463 6059 -20 -1819 906 C ATOM 975 CD PRO A 221 26.822 39.763 281.997 1.00 60.13 C ANISOU 975 CD PRO A 221 10045 5570 7233 46 -1926 856 C ATOM 976 N LEU A 222 29.392 40.533 279.687 1.00 59.06 N ANISOU 976 N LEU A 222 10362 5239 6840 -551 -1916 1154 N ATOM 977 CA LEU A 222 30.096 41.000 278.497 1.00 64.83 C ANISOU 977 CA LEU A 222 11331 5861 7439 -772 -1950 1253 C ATOM 978 C LEU A 222 31.362 41.765 278.864 1.00 75.04 C ANISOU 978 C LEU A 222 12769 7100 8644 -1013 -1935 1320 C ATOM 979 O LEU A 222 32.429 41.534 278.284 1.00 90.82 O ANISOU 979 O LEU A 222 14767 9163 10578 -1268 -1823 1397 O ATOM 980 CB LEU A 222 29.171 41.871 277.642 1.00 74.43 C ANISOU 980 CB LEU A 222 12845 6862 8573 -654 -2173 1234 C ATOM 981 CG LEU A 222 29.667 42.229 276.237 1.00 66.85 C ANISOU 981 CG LEU A 222 12148 5789 7464 -863 -2215 1336 C ATOM 982 CD1 LEU A 222 30.115 40.996 275.471 1.00 50.15 C ANISOU 982 CD1 LEU A 222 9812 3868 5374 -993 -2019 1381 C ATOM 983 CD2 LEU A 222 28.563 42.941 275.486 1.00 62.76 C ANISOU 983 CD2 LEU A 222 11899 5067 6881 -684 -2451 1300 C ATOM 984 N ALA A 223 31.263 42.690 279.816 1.00 63.06 N ANISOU 984 N ALA A 223 11370 5470 7119 -942 -2048 1278 N ATOM 985 CA ALA A 223 32.373 43.558 280.181 1.00 65.66 C ANISOU 985 CA ALA A 223 11867 5722 7358 -1166 -2060 1328 C ATOM 986 C ALA A 223 33.081 43.113 281.456 1.00 68.04 C ANISOU 986 C ALA A 223 11914 6197 7741 -1196 -1922 1302 C ATOM 987 O ALA A 223 33.869 43.882 282.014 1.00 76.98 O ANISOU 987 O ALA A 223 13161 7272 8818 -1337 -1947 1314 O ATOM 988 CB ALA A 223 31.873 44.996 280.337 1.00 61.74 C ANISOU 988 CB ALA A 223 11720 4956 6781 -1085 -2298 1301 C ATOM 989 N TYR A 224 32.828 41.889 281.923 1.00 74.74 N ANISOU 989 N TYR A 224 12432 7251 8713 -1073 -1782 1265 N ATOM 990 CA TYR A 224 33.426 41.428 283.174 1.00 68.96 C ANISOU 990 CA TYR A 224 11473 6677 8053 -1075 -1667 1239 C ATOM 991 C TYR A 224 34.949 41.502 283.130 1.00 59.43 C ANISOU 991 C TYR A 224 10258 5540 6784 -1360 -1571 1297 C ATOM 992 O TYR A 224 35.584 41.938 284.097 1.00 61.19 O ANISOU 992 O TYR A 224 10472 5777 6999 -1415 -1572 1277 O ATOM 993 CB TYR A 224 32.974 39.997 283.473 1.00 64.35 C ANISOU 993 CB TYR A 224 10567 6290 7592 -931 -1526 1209 C ATOM 994 CG TYR A 224 33.832 39.297 284.497 1.00 60.89 C ANISOU 994 CG TYR A 224 9898 6028 7208 -980 -1387 1208 C ATOM 995 CD1 TYR A 224 33.661 39.530 285.855 1.00 53.84 C ANISOU 995 CD1 TYR A 224 8951 5154 6350 -863 -1410 1153 C ATOM 996 CD2 TYR A 224 34.817 38.401 284.106 1.00 82.33 C ANISOU 996 CD2 TYR A 224 12452 8895 9935 -1133 -1242 1253 C ATOM 997 CE1 TYR A 224 34.450 38.890 286.791 1.00 74.07 C ANISOU 997 CE1 TYR A 224 11320 7872 8952 -900 -1297 1155 C ATOM 998 CE2 TYR A 224 35.606 37.760 285.033 1.00 78.18 C ANISOU 998 CE2 TYR A 224 11725 8524 9455 -1157 -1137 1244 C ATOM 999 CZ TYR A 224 35.421 38.007 286.368 1.00 64.28 C ANISOU 999 CZ TYR A 224 9931 6770 7723 -1041 -1168 1200 C ATOM 1000 OH TYR A 224 36.218 37.355 287.271 1.00 77.01 O ANISOU 1000 OH TYR A 224 11358 8532 9371 -1060 -1075 1194 O ATOM 1001 N LYS A 225 35.551 41.076 282.018 1.00 74.49 N ANISOU 1001 N LYS A 225 12156 7505 8644 -1545 -1486 1354 N ATOM 1002 CA LYS A 225 37.007 41.003 281.940 1.00 64.44 C ANISOU 1002 CA LYS A 225 10821 6345 7319 -1817 -1374 1383 C ATOM 1003 C LYS A 225 37.647 42.374 282.125 1.00 69.45 C ANISOU 1003 C LYS A 225 11721 6829 7836 -2005 -1472 1398 C ATOM 1004 O LYS A 225 38.719 42.487 282.733 1.00 60.97 O ANISOU 1004 O LYS A 225 10565 5853 6750 -2160 -1406 1381 O ATOM 1005 CB LYS A 225 37.428 40.382 280.606 1.00 60.18 C ANISOU 1005 CB LYS A 225 10244 5888 6735 -1979 -1275 1427 C ATOM 1006 CG LYS A 225 37.816 38.909 280.710 1.00 74.09 C ANISOU 1006 CG LYS A 225 11657 7894 8601 -1941 -1105 1404 C ATOM 1007 CD LYS A 225 37.644 38.172 279.386 1.00 94.96 C ANISOU 1007 CD LYS A 225 14260 10590 11231 -1984 -1038 1431 C ATOM 1008 CE LYS A 225 36.184 37.785 279.135 1.00100.89 C ANISOU 1008 CE LYS A 225 15016 11267 12051 -1729 -1102 1423 C ATOM 1009 NZ LYS A 225 36.004 36.993 277.871 1.00 88.86 N ANISOU 1009 NZ LYS A 225 13436 9805 10521 -1761 -1035 1441 N ATOM 1010 N ARG A 226 37.008 43.429 281.621 1.00 60.66 N ANISOU 1010 N ARG A 226 10936 5476 6637 -1992 -1637 1421 N ATOM 1011 CA ARG A 226 37.570 44.768 281.740 1.00 70.89 C ANISOU 1011 CA ARG A 226 12526 6597 7813 -2181 -1742 1440 C ATOM 1012 C ARG A 226 37.200 45.463 283.043 1.00 74.93 C ANISOU 1012 C ARG A 226 13087 7015 8367 -2015 -1856 1378 C ATOM 1013 O ARG A 226 37.809 46.488 283.369 1.00 96.56 O ANISOU 1013 O ARG A 226 16026 9638 11023 -2177 -1925 1380 O ATOM 1014 CB ARG A 226 37.129 45.643 280.559 1.00 72.79 C ANISOU 1014 CB ARG A 226 13145 6593 7918 -2260 -1885 1500 C ATOM 1015 CG ARG A 226 35.654 46.054 280.570 1.00 88.00 C ANISOU 1015 CG ARG A 226 15233 8327 9875 -1950 -2077 1468 C ATOM 1016 CD ARG A 226 35.431 47.301 279.732 1.00 90.67 C ANISOU 1016 CD ARG A 226 15944 8444 10063 -2012 -2243 1473 C ATOM 1017 NE ARG A 226 34.019 47.652 279.605 1.00 92.02 N ANISOU 1017 NE ARG A 226 16241 8462 10260 -1701 -2430 1415 N ATOM 1018 CZ ARG A 226 33.324 48.339 280.508 1.00 86.92 C ANISOU 1018 CZ ARG A 226 15689 7681 9655 -1483 -2589 1341 C ATOM 1019 NH1 ARG A 226 33.895 48.756 281.631 1.00 78.38 N ANISOU 1019 NH1 ARG A 226 14605 6584 8593 -1541 -2587 1327 N ATOM 1020 NH2 ARG A 226 32.047 48.608 280.290 1.00 78.88 N ANISOU 1020 NH2 ARG A 226 14761 6550 8659 -1201 -2756 1267 N ATOM 1021 N ILE A 227 36.224 44.951 283.787 1.00 63.66 N ANISOU 1021 N ILE A 227 11489 5639 7060 -1712 -1874 1316 N ATOM 1022 CA ILE A 227 35.852 45.544 285.070 1.00 72.00 C ANISOU 1022 CA ILE A 227 12565 6634 8156 -1546 -1969 1243 C ATOM 1023 C ILE A 227 36.740 45.028 286.193 1.00 80.20 C ANISOU 1023 C ILE A 227 13344 7877 9253 -1599 -1838 1214 C ATOM 1024 O ILE A 227 37.340 45.811 286.933 1.00 66.68 O ANISOU 1024 O ILE A 227 11721 6114 7500 -1690 -1885 1190 O ATOM 1025 CB ILE A 227 34.358 45.279 285.361 1.00 60.81 C ANISOU 1025 CB ILE A 227 11087 5191 6828 -1206 -2048 1172 C ATOM 1026 CG1 ILE A 227 33.484 46.036 284.355 1.00 60.01 C ANISOU 1026 CG1 ILE A 227 11287 4856 6657 -1132 -2229 1180 C ATOM 1027 CG2 ILE A 227 34.000 45.699 286.784 1.00 51.32 C ANISOU 1027 CG2 ILE A 227 9842 3983 5675 -1030 -2112 1080 C ATOM 1028 CD1 ILE A 227 31.984 45.798 284.513 1.00 67.27 C ANISOU 1028 CD1 ILE A 227 12137 5762 7659 -798 -2316 1088 C ATOM 1029 N VAL A 228 36.833 43.707 286.334 1.00 74.22 N ANISOU 1029 N VAL A 228 12272 7342 8587 -1537 -1681 1212 N ATOM 1030 CA VAL A 228 37.639 43.079 287.375 1.00 74.66 C ANISOU 1030 CA VAL A 228 12075 7595 8697 -1559 -1565 1185 C ATOM 1031 C VAL A 228 39.020 42.832 286.777 1.00 78.27 C ANISOU 1031 C VAL A 228 12467 8169 9102 -1846 -1454 1223 C ATOM 1032 O VAL A 228 39.229 41.865 286.044 1.00 86.82 O ANISOU 1032 O VAL A 228 13394 9380 10212 -1888 -1340 1250 O ATOM 1033 CB VAL A 228 37.002 41.785 287.881 1.00 75.76 C ANISOU 1033 CB VAL A 228 11935 7898 8953 -1338 -1468 1160 C ATOM 1034 CG1 VAL A 228 37.840 41.177 288.996 1.00 80.55 C ANISOU 1034 CG1 VAL A 228 12316 8688 9601 -1349 -1370 1135 C ATOM 1035 CG2 VAL A 228 35.582 42.042 288.351 1.00 70.16 C ANISOU 1035 CG2 VAL A 228 11281 7092 8285 -1074 -1568 1104 C ATOM 1036 N THR A 229 39.964 43.711 287.094 1.00 74.69 N ANISOU 1036 N THR A 229 12127 7678 8573 -2047 -1485 1211 N ATOM 1037 CA THR A 229 41.311 43.657 286.549 1.00 64.32 C ANISOU 1037 CA THR A 229 10764 6479 7195 -2348 -1387 1224 C ATOM 1038 C THR A 229 42.315 43.419 287.669 1.00 79.98 C ANISOU 1038 C THR A 229 12537 8640 9212 -2392 -1324 1161 C ATOM 1039 O THR A 229 41.980 43.435 288.856 1.00 81.14 O ANISOU 1039 O THR A 229 12622 8793 9414 -2207 -1368 1121 O ATOM 1040 CB THR A 229 41.653 44.955 285.808 1.00 64.72 C ANISOU 1040 CB THR A 229 11152 6334 7104 -2604 -1474 1259 C ATOM 1041 OG1 THR A 229 41.683 46.041 286.741 1.00 70.22 O ANISOU 1041 OG1 THR A 229 12018 6893 7770 -2600 -1594 1223 O ATOM 1042 CG2 THR A 229 40.620 45.250 284.734 1.00 69.39 C ANISOU 1042 CG2 THR A 229 11984 6729 7651 -2539 -1565 1320 C ATOM 1043 N ARG A 230 43.569 43.207 287.271 1.00 87.24 N ANISOU 1043 N ARG A 230 13344 9714 10089 -2641 -1222 1143 N ATOM 1044 CA ARG A 230 44.630 42.979 288.249 1.00 90.91 C ANISOU 1044 CA ARG A 230 13598 10364 10578 -2694 -1169 1069 C ATOM 1045 C ARG A 230 44.821 44.167 289.180 1.00 87.81 C ANISOU 1045 C ARG A 230 13373 9854 10139 -2744 -1278 1032 C ATOM 1046 O ARG A 230 44.940 43.954 290.399 1.00 90.72 O ANISOU 1046 O ARG A 230 13601 10307 10563 -2602 -1292 979 O ATOM 1047 CB ARG A 230 45.925 42.626 287.511 1.00101.43 C ANISOU 1047 CB ARG A 230 14786 11889 11865 -2969 -1047 1034 C ATOM 1048 CG ARG A 230 46.829 41.668 288.262 1.00107.88 C ANISOU 1048 CG ARG A 230 15265 12971 12753 -2918 -962 951 C ATOM 1049 CD ARG A 230 47.876 42.390 289.084 1.00118.11 C ANISOU 1049 CD ARG A 230 16541 14333 14003 -3079 -987 867 C ATOM 1050 NE ARG A 230 48.907 42.994 288.245 1.00126.08 N ANISOU 1050 NE ARG A 230 17606 15394 14904 -3442 -932 831 N ATOM 1051 CZ ARG A 230 50.047 43.502 288.704 1.00132.52 C ANISOU 1051 CZ ARG A 230 18357 16322 15671 -3651 -920 736 C ATOM 1052 NH1 ARG A 230 50.315 43.481 290.005 1.00118.15 N ANISOU 1052 NH1 ARG A 230 16417 14572 13903 -3518 -970 671 N ATOM 1053 NH2 ARG A 230 50.924 44.031 287.862 1.00141.96 N ANISOU 1053 NH2 ARG A 230 19608 17571 16759 -4004 -856 701 N ATOM 1054 N PRO A 231 44.861 45.417 288.704 1.00 87.24 N ANISOU 1054 N PRO A 231 13607 9581 9959 -2939 -1364 1056 N ATOM 1055 CA PRO A 231 44.957 46.535 289.653 1.00 83.44 C ANISOU 1055 CA PRO A 231 13293 8970 9440 -2960 -1480 1015 C ATOM 1056 C PRO A 231 43.711 46.700 290.503 1.00 88.01 C ANISOU 1056 C PRO A 231 13943 9415 10084 -2635 -1595 1011 C ATOM 1057 O PRO A 231 43.819 47.106 291.666 1.00 91.88 O ANISOU 1057 O PRO A 231 14419 9903 10588 -2560 -1653 952 O ATOM 1058 CB PRO A 231 45.194 47.748 288.744 1.00 73.93 C ANISOU 1058 CB PRO A 231 12435 7558 8099 -3248 -1546 1055 C ATOM 1059 CG PRO A 231 44.650 47.348 287.432 1.00 83.45 C ANISOU 1059 CG PRO A 231 13714 8712 9282 -3256 -1514 1134 C ATOM 1060 CD PRO A 231 44.914 45.885 287.308 1.00 86.97 C ANISOU 1060 CD PRO A 231 13794 9431 9820 -3168 -1360 1118 C ATOM 1061 N LYS A 232 42.529 46.398 289.964 1.00 75.25 N ANISOU 1061 N LYS A 232 12391 7699 8503 -2441 -1629 1060 N ATOM 1062 CA LYS A 232 41.316 46.469 290.770 1.00 80.66 C ANISOU 1062 CA LYS A 232 13103 8293 9252 -2128 -1723 1033 C ATOM 1063 C LYS A 232 41.334 45.426 291.879 1.00 88.10 C ANISOU 1063 C LYS A 232 13732 9450 10291 -1939 -1637 989 C ATOM 1064 O LYS A 232 40.971 45.720 293.024 1.00 93.20 O ANISOU 1064 O LYS A 232 14374 10077 10959 -1782 -1700 934 O ATOM 1065 CB LYS A 232 40.089 46.274 289.884 1.00 75.73 C ANISOU 1065 CB LYS A 232 12580 7549 8646 -1970 -1767 1078 C ATOM 1066 CG LYS A 232 39.830 47.403 288.909 1.00 78.91 C ANISOU 1066 CG LYS A 232 13345 7692 8944 -2095 -1897 1120 C ATOM 1067 CD LYS A 232 39.167 48.594 289.584 1.00 73.84 C ANISOU 1067 CD LYS A 232 12955 6826 8277 -1966 -2084 1069 C ATOM 1068 CE LYS A 232 38.503 49.514 288.567 1.00 89.33 C ANISOU 1068 CE LYS A 232 15281 8507 10153 -1982 -2242 1110 C ATOM 1069 NZ LYS A 232 37.434 48.832 287.785 1.00 72.18 N ANISOU 1069 NZ LYS A 232 13062 6335 8029 -1788 -2242 1133 N ATOM 1070 N ALA A 233 41.755 44.202 291.559 1.00 77.97 N ANISOU 1070 N ALA A 233 12198 8369 9058 -1952 -1498 1010 N ATOM 1071 CA ALA A 233 41.719 43.126 292.542 1.00 72.21 C ANISOU 1071 CA ALA A 233 11201 7824 8412 -1766 -1423 981 C ATOM 1072 C ALA A 233 42.716 43.371 293.667 1.00 79.17 C ANISOU 1072 C ALA A 233 11996 8810 9276 -1831 -1429 919 C ATOM 1073 O ALA A 233 42.425 43.085 294.835 1.00 95.05 O ANISOU 1073 O ALA A 233 13911 10879 11323 -1649 -1441 883 O ATOM 1074 CB ALA A 233 41.992 41.787 291.856 1.00 71.33 C ANISOU 1074 CB ALA A 233 10868 7882 8353 -1773 -1289 1015 C ATOM 1075 N VAL A 234 43.894 43.907 293.340 1.00 81.61 N ANISOU 1075 N VAL A 234 12337 9150 9521 -2097 -1418 898 N ATOM 1076 CA VAL A 234 44.897 44.179 294.366 1.00 82.45 C ANISOU 1076 CA VAL A 234 12355 9366 9608 -2173 -1429 824 C ATOM 1077 C VAL A 234 44.374 45.208 295.358 1.00 78.40 C ANISOU 1077 C VAL A 234 12018 8699 9070 -2076 -1557 787 C ATOM 1078 O VAL A 234 44.544 45.063 296.575 1.00 79.36 O ANISOU 1078 O VAL A 234 12032 8911 9211 -1961 -1573 733 O ATOM 1079 CB VAL A 234 46.215 44.638 293.715 1.00 79.96 C ANISOU 1079 CB VAL A 234 12047 9113 9222 -2506 -1391 795 C ATOM 1080 CG1 VAL A 234 47.145 45.272 294.743 1.00 68.76 C ANISOU 1080 CG1 VAL A 234 10601 7757 7767 -2608 -1435 705 C ATOM 1081 CG2 VAL A 234 46.900 43.462 293.042 1.00 71.60 C ANISOU 1081 CG2 VAL A 234 10736 8272 8197 -2567 -1258 792 C ATOM 1082 N VAL A 235 43.738 46.268 294.857 1.00 91.40 N ANISOU 1082 N VAL A 235 13950 10109 10667 -2117 -1658 810 N ATOM 1083 CA VAL A 235 43.223 47.308 295.744 1.00 93.50 C ANISOU 1083 CA VAL A 235 14401 10215 10909 -2019 -1793 761 C ATOM 1084 C VAL A 235 42.151 46.736 296.661 1.00 88.06 C ANISOU 1084 C VAL A 235 13605 9565 10289 -1696 -1802 738 C ATOM 1085 O VAL A 235 42.131 47.015 297.866 1.00102.94 O ANISOU 1085 O VAL A 235 15466 11474 12172 -1593 -1850 673 O ATOM 1086 CB VAL A 235 42.697 48.501 294.922 1.00 92.63 C ANISOU 1086 CB VAL A 235 14636 9826 10731 -2105 -1916 790 C ATOM 1087 CG1 VAL A 235 42.018 49.532 295.826 1.00 84.94 C ANISOU 1087 CG1 VAL A 235 13856 8676 9742 -1957 -2071 726 C ATOM 1088 CG2 VAL A 235 43.835 49.154 294.149 1.00 85.95 C ANISOU 1088 CG2 VAL A 235 13920 8942 9795 -2465 -1902 808 C ATOM 1089 N ALA A 236 41.249 45.920 296.113 1.00 81.69 N ANISOU 1089 N ALA A 236 12729 8773 9537 -1543 -1751 785 N ATOM 1090 CA ALA A 236 40.175 45.361 296.928 1.00 83.09 C ANISOU 1090 CA ALA A 236 12805 8994 9770 -1260 -1746 757 C ATOM 1091 C ALA A 236 40.726 44.473 298.035 1.00 89.44 C ANISOU 1091 C ALA A 236 13369 10013 10601 -1196 -1662 734 C ATOM 1092 O ALA A 236 40.243 44.514 299.172 1.00 93.64 O ANISOU 1092 O ALA A 236 13874 10571 11136 -1030 -1691 681 O ATOM 1093 CB ALA A 236 39.203 44.572 296.053 1.00 77.33 C ANISOU 1093 CB ALA A 236 12028 8259 9093 -1142 -1693 808 C ATOM 1094 N PHE A 237 41.734 43.659 297.722 1.00 84.68 N ANISOU 1094 N PHE A 237 12595 9569 10011 -1318 -1563 765 N ATOM 1095 CA PHE A 237 42.279 42.749 298.723 1.00 90.59 C ANISOU 1095 CA PHE A 237 13126 10512 10780 -1241 -1500 744 C ATOM 1096 C PHE A 237 43.150 43.485 299.735 1.00 97.28 C ANISOU 1096 C PHE A 237 13993 11393 11577 -1316 -1566 672 C ATOM 1097 O PHE A 237 43.123 43.167 300.930 1.00 97.54 O ANISOU 1097 O PHE A 237 13939 11515 11606 -1180 -1571 636 O ATOM 1098 CB PHE A 237 43.062 41.636 298.036 1.00 72.07 C ANISOU 1098 CB PHE A 237 10592 8323 8469 -1324 -1391 783 C ATOM 1099 CG PHE A 237 42.203 40.495 297.594 1.00 76.80 C ANISOU 1099 CG PHE A 237 11098 8953 9130 -1176 -1311 841 C ATOM 1100 CD1 PHE A 237 41.801 39.532 298.503 1.00 80.25 C ANISOU 1100 CD1 PHE A 237 11407 9487 9596 -987 -1267 845 C ATOM 1101 CD2 PHE A 237 41.783 40.391 296.281 1.00 77.42 C ANISOU 1101 CD2 PHE A 237 11229 8959 9228 -1232 -1280 892 C ATOM 1102 CE1 PHE A 237 41.004 38.477 298.111 1.00 77.36 C ANISOU 1102 CE1 PHE A 237 10965 9145 9283 -868 -1190 895 C ATOM 1103 CE2 PHE A 237 40.985 39.337 295.878 1.00 81.74 C ANISOU 1103 CE2 PHE A 237 11687 9536 9834 -1100 -1207 937 C ATOM 1104 CZ PHE A 237 40.593 38.377 296.797 1.00 66.72 C ANISOU 1104 CZ PHE A 237 9655 7730 7966 -922 -1160 937 C ATOM 1105 N CYS A 238 43.929 44.469 299.283 1.00 93.68 N ANISOU 1105 N CYS A 238 13657 10866 11073 -1542 -1616 648 N ATOM 1106 CA CYS A 238 44.729 45.254 300.214 1.00 83.25 C ANISOU 1106 CA CYS A 238 12366 9565 9702 -1627 -1685 569 C ATOM 1107 C CYS A 238 43.837 45.982 301.211 1.00 85.78 C ANISOU 1107 C CYS A 238 12824 9765 10003 -1456 -1784 524 C ATOM 1108 O CYS A 238 44.101 45.977 302.419 1.00 98.48 O ANISOU 1108 O CYS A 238 14361 11461 11594 -1376 -1810 465 O ATOM 1109 CB CYS A 238 45.607 46.241 299.445 1.00 86.37 C ANISOU 1109 CB CYS A 238 12895 9881 10039 -1925 -1717 553 C ATOM 1110 SG CYS A 238 47.048 45.478 298.662 1.00 97.95 S ANISOU 1110 SG CYS A 238 14140 11568 11509 -2158 -1598 546 S ATOM 1111 N LEU A 239 42.764 46.606 300.722 1.00 75.59 N ANISOU 1111 N LEU A 239 11728 8279 8713 -1389 -1848 541 N ATOM 1112 CA LEU A 239 41.804 47.239 301.620 1.00 75.11 C ANISOU 1112 CA LEU A 239 11781 8115 8640 -1199 -1942 480 C ATOM 1113 C LEU A 239 41.229 46.226 302.594 1.00 82.05 C ANISOU 1113 C LEU A 239 12474 9150 9550 -970 -1875 468 C ATOM 1114 O LEU A 239 41.140 46.478 303.801 1.00102.97 O ANISOU 1114 O LEU A 239 15114 11839 12171 -868 -1916 399 O ATOM 1115 CB LEU A 239 40.666 47.870 300.825 1.00 69.24 C ANISOU 1115 CB LEU A 239 11246 7158 7902 -1128 -2020 492 C ATOM 1116 CG LEU A 239 40.938 49.076 299.926 1.00 92.88 C ANISOU 1116 CG LEU A 239 14512 9933 10846 -1322 -2124 502 C ATOM 1117 CD1 LEU A 239 39.609 49.775 299.678 1.00 92.77 C ANISOU 1117 CD1 LEU A 239 14706 9708 10834 -1147 -2247 473 C ATOM 1118 CD2 LEU A 239 41.983 50.033 300.511 1.00 86.90 C ANISOU 1118 CD2 LEU A 239 13850 9141 10026 -1506 -2193 445 C ATOM 1119 N MET A 240 40.822 45.069 302.075 1.00 79.56 N ANISOU 1119 N MET A 240 12021 8921 9286 -896 -1769 536 N ATOM 1120 CA MET A 240 40.129 44.089 302.899 1.00 84.60 C ANISOU 1120 CA MET A 240 12515 9683 9945 -692 -1699 534 C ATOM 1121 C MET A 240 41.022 43.601 304.031 1.00 82.45 C ANISOU 1121 C MET A 240 12107 9578 9642 -689 -1673 513 C ATOM 1122 O MET A 240 40.553 43.383 305.154 1.00 86.66 O ANISOU 1122 O MET A 240 12604 10174 10147 -539 -1670 475 O ATOM 1123 CB MET A 240 39.664 42.921 302.028 1.00 78.57 C ANISOU 1123 CB MET A 240 11640 8973 9241 -650 -1591 614 C ATOM 1124 CG MET A 240 38.905 41.825 302.776 1.00 67.29 C ANISOU 1124 CG MET A 240 10076 7663 7828 -465 -1505 621 C ATOM 1125 SD MET A 240 39.984 40.627 303.586 1.00 75.00 S ANISOU 1125 SD MET A 240 10865 8843 8790 -473 -1428 656 S ATOM 1126 CE MET A 240 40.770 39.868 302.164 1.00 66.14 C ANISOU 1126 CE MET A 240 9648 7758 7726 -615 -1359 734 C ATOM 1127 N TRP A 241 42.316 43.430 303.759 1.00 65.54 N ANISOU 1127 N TRP A 241 9888 7519 7496 -853 -1656 527 N ATOM 1128 CA TRP A 241 43.229 42.957 304.792 1.00 82.10 C ANISOU 1128 CA TRP A 241 11852 9780 9563 -840 -1649 496 C ATOM 1129 C TRP A 241 43.446 44.012 305.866 1.00 87.20 C ANISOU 1129 C TRP A 241 12593 10393 10147 -840 -1751 406 C ATOM 1130 O TRP A 241 43.525 43.685 307.055 1.00 86.53 O ANISOU 1130 O TRP A 241 12442 10410 10024 -727 -1758 372 O ATOM 1131 CB TRP A 241 44.560 42.557 304.165 1.00 81.79 C ANISOU 1131 CB TRP A 241 11688 9849 9538 -1012 -1614 507 C ATOM 1132 CG TRP A 241 44.580 41.148 303.693 1.00 81.30 C ANISOU 1132 CG TRP A 241 11467 9898 9526 -949 -1514 574 C ATOM 1133 CD1 TRP A 241 44.158 40.679 302.483 1.00 74.87 C ANISOU 1133 CD1 TRP A 241 10643 9040 8763 -977 -1446 640 C ATOM 1134 CD2 TRP A 241 45.045 40.011 304.425 1.00 79.16 C ANISOU 1134 CD2 TRP A 241 11035 9789 9253 -840 -1481 579 C ATOM 1135 NE1 TRP A 241 44.334 39.319 302.417 1.00 81.79 N ANISOU 1135 NE1 TRP A 241 11358 10043 9677 -896 -1369 682 N ATOM 1136 CE2 TRP A 241 44.878 38.885 303.598 1.00 71.26 C ANISOU 1136 CE2 TRP A 241 9938 8829 8309 -808 -1393 648 C ATOM 1137 CE3 TRP A 241 45.588 39.837 305.701 1.00 89.03 C ANISOU 1137 CE3 TRP A 241 12228 11146 10453 -762 -1527 531 C ATOM 1138 CZ2 TRP A 241 45.235 37.603 304.005 1.00 74.34 C ANISOU 1138 CZ2 TRP A 241 10188 9350 8709 -699 -1356 671 C ATOM 1139 CZ3 TRP A 241 45.942 38.564 306.103 1.00 88.56 C ANISOU 1139 CZ3 TRP A 241 12033 11218 10397 -651 -1494 557 C ATOM 1140 CH2 TRP A 241 45.765 37.462 305.258 1.00 77.58 C ANISOU 1140 CH2 TRP A 241 10559 9851 9064 -620 -1411 627 C ATOM 1141 N THR A 242 43.557 45.281 305.469 1.00 92.51 N ANISOU 1141 N THR A 242 13432 10915 10802 -971 -1835 365 N ATOM 1142 CA THR A 242 43.710 46.339 306.461 1.00100.76 C ANISOU 1142 CA THR A 242 14584 11909 11790 -970 -1940 272 C ATOM 1143 C THR A 242 42.478 46.428 307.351 1.00 96.51 C ANISOU 1143 C THR A 242 14099 11335 11235 -743 -1964 234 C ATOM 1144 O THR A 242 42.593 46.678 308.556 1.00 95.82 O ANISOU 1144 O THR A 242 14005 11306 11096 -670 -2009 163 O ATOM 1145 CB THR A 242 43.979 47.677 305.771 1.00 91.84 C ANISOU 1145 CB THR A 242 13659 10595 10643 -1160 -2030 242 C ATOM 1146 OG1 THR A 242 42.981 47.913 304.773 1.00 89.13 O ANISOU 1146 OG1 THR A 242 13453 10084 10329 -1126 -2039 291 O ATOM 1147 CG2 THR A 242 45.350 47.674 305.120 1.00 78.79 C ANISOU 1147 CG2 THR A 242 11940 9014 8984 -1417 -2001 250 C ATOM 1148 N ILE A 243 41.291 46.214 306.782 1.00 76.43 N ANISOU 1148 N ILE A 243 11598 8713 8730 -630 -1934 269 N ATOM 1149 CA ILE A 243 40.091 46.137 307.607 1.00 81.46 C ANISOU 1149 CA ILE A 243 12243 9358 9351 -415 -1933 219 C ATOM 1150 C ILE A 243 40.144 44.898 308.490 1.00 89.14 C ANISOU 1150 C ILE A 243 13039 10527 10302 -313 -1834 248 C ATOM 1151 O ILE A 243 39.754 44.937 309.661 1.00 94.83 O ANISOU 1151 O ILE A 243 13754 11311 10967 -191 -1844 186 O ATOM 1152 CB ILE A 243 38.828 46.154 306.728 1.00 72.40 C ANISOU 1152 CB ILE A 243 11160 8096 8251 -323 -1924 234 C ATOM 1153 CG1 ILE A 243 38.760 47.455 305.923 1.00 69.79 C ANISOU 1153 CG1 ILE A 243 11045 7545 7924 -411 -2049 203 C ATOM 1154 CG2 ILE A 243 37.575 46.003 307.597 1.00 61.26 C ANISOU 1154 CG2 ILE A 243 9723 6730 6822 -107 -1907 160 C ATOM 1155 CD1 ILE A 243 37.658 47.476 304.852 1.00 78.33 C ANISOU 1155 CD1 ILE A 243 12202 8507 9055 -334 -2058 224 C ATOM 1156 N ALA A 244 40.627 43.780 307.945 1.00 84.00 N ANISOU 1156 N ALA A 244 12257 9973 9688 -360 -1741 340 N ATOM 1157 CA ALA A 244 40.746 42.562 308.738 1.00 71.39 C ANISOU 1157 CA ALA A 244 10521 8541 8064 -268 -1661 378 C ATOM 1158 C ALA A 244 41.782 42.720 309.844 1.00 83.00 C ANISOU 1158 C ALA A 244 11960 10111 9466 -290 -1718 329 C ATOM 1159 O ALA A 244 41.540 42.325 310.992 1.00 79.22 O ANISOU 1159 O ALA A 244 11456 9722 8921 -173 -1704 310 O ATOM 1160 CB ALA A 244 41.101 41.385 307.831 1.00 50.99 C ANISOU 1160 CB ALA A 244 7818 6018 5538 -313 -1570 477 C ATOM 1161 N ILE A 245 42.944 43.292 309.520 1.00 84.61 N ANISOU 1161 N ILE A 245 12164 10307 9676 -448 -1780 304 N ATOM 1162 CA ILE A 245 43.979 43.494 310.531 1.00 81.99 C ANISOU 1162 CA ILE A 245 11792 10078 9283 -475 -1844 240 C ATOM 1163 C ILE A 245 43.489 44.435 311.622 1.00 91.92 C ANISOU 1163 C ILE A 245 13164 11289 10473 -398 -1921 149 C ATOM 1164 O ILE A 245 43.777 44.239 312.809 1.00 92.64 O ANISOU 1164 O ILE A 245 13220 11487 10492 -321 -1946 109 O ATOM 1165 CB ILE A 245 45.271 44.023 309.878 1.00 77.24 C ANISOU 1165 CB ILE A 245 11165 9481 8704 -686 -1890 210 C ATOM 1166 CG1 ILE A 245 45.979 42.888 309.128 1.00 74.42 C ANISOU 1166 CG1 ILE A 245 10644 9237 8394 -735 -1815 274 C ATOM 1167 CG2 ILE A 245 46.181 44.704 310.925 1.00 56.07 C ANISOU 1167 CG2 ILE A 245 8485 6864 5957 -732 -1986 107 C ATOM 1168 CD1 ILE A 245 47.497 42.814 309.331 1.00 81.93 C ANISOU 1168 CD1 ILE A 245 11466 10333 9330 -848 -1855 210 C ATOM 1169 N VAL A 246 42.766 45.487 311.236 1.00 80.54 N ANISOU 1169 N VAL A 246 11869 9685 9049 -412 -1971 106 N ATOM 1170 CA VAL A 246 42.358 46.495 312.210 1.00 75.42 C ANISOU 1170 CA VAL A 246 11335 8980 8340 -342 -2059 -2 C ATOM 1171 C VAL A 246 41.561 45.856 313.337 1.00 87.13 C ANISOU 1171 C VAL A 246 12770 10573 9762 -151 -2008 -18 C ATOM 1172 O VAL A 246 41.693 46.246 314.504 1.00 96.70 O ANISOU 1172 O VAL A 246 14007 11839 10896 -96 -2062 -99 O ATOM 1173 CB VAL A 246 41.565 47.624 311.524 1.00 87.25 C ANISOU 1173 CB VAL A 246 13009 10271 9872 -354 -2128 -45 C ATOM 1174 CG1 VAL A 246 40.601 48.316 312.506 1.00 94.24 C ANISOU 1174 CG1 VAL A 246 13986 11115 10706 -192 -2189 -157 C ATOM 1175 CG2 VAL A 246 42.519 48.660 310.945 1.00 64.98 C ANISOU 1175 CG2 VAL A 246 10298 7333 7060 -563 -2220 -71 C ATOM 1176 N ILE A 247 40.726 44.867 313.018 1.00 83.94 N ANISOU 1176 N ILE A 247 12302 10209 9384 -61 -1900 55 N ATOM 1177 CA ILE A 247 39.875 44.278 314.046 1.00 95.58 C ANISOU 1177 CA ILE A 247 13744 11783 10787 95 -1837 37 C ATOM 1178 C ILE A 247 40.716 43.510 315.053 1.00103.94 C ANISOU 1178 C ILE A 247 14728 12998 11766 110 -1825 66 C ATOM 1179 O ILE A 247 40.458 43.555 316.260 1.00110.80 O ANISOU 1179 O ILE A 247 15619 13944 12537 198 -1833 9 O ATOM 1180 CB ILE A 247 38.799 43.376 313.422 1.00 86.14 C ANISOU 1180 CB ILE A 247 12498 10594 9636 164 -1718 105 C ATOM 1181 CG1 ILE A 247 38.195 44.017 312.170 1.00 80.33 C ANISOU 1181 CG1 ILE A 247 11827 9702 8992 135 -1744 95 C ATOM 1182 CG2 ILE A 247 37.717 43.125 314.431 1.00 87.27 C ANISOU 1182 CG2 ILE A 247 12639 10819 9701 301 -1659 48 C ATOM 1183 CD1 ILE A 247 37.881 45.517 312.271 1.00 76.13 C ANISOU 1183 CD1 ILE A 247 11439 9033 8454 149 -1872 -27 C ATOM 1184 N ALA A 248 41.728 42.786 314.578 1.00 98.14 N ANISOU 1184 N ALA A 248 13905 12317 11065 31 -1810 145 N ATOM 1185 CA ALA A 248 42.629 42.094 315.492 1.00115.68 C ANISOU 1185 CA ALA A 248 16062 14678 13212 58 -1828 161 C ATOM 1186 C ALA A 248 43.321 43.084 316.419 1.00119.11 C ANISOU 1186 C ALA A 248 16541 15135 13579 33 -1945 51 C ATOM 1187 O ALA A 248 43.387 42.878 317.638 1.00132.19 O ANISOU 1187 O ALA A 248 18209 16887 15130 120 -1966 20 O ATOM 1188 CB ALA A 248 43.658 41.295 314.693 1.00116.97 C ANISOU 1188 CB ALA A 248 16115 14889 13438 -20 -1814 235 C ATOM 1189 N VAL A 249 43.819 44.185 315.857 1.00103.74 N ANISOU 1189 N VAL A 249 14637 13095 11684 -93 -2022 -11 N ATOM 1190 CA VAL A 249 44.594 45.134 316.640 1.00 96.57 C ANISOU 1190 CA VAL A 249 13768 12203 10721 -143 -2137 -120 C ATOM 1191 C VAL A 249 43.707 45.901 317.618 1.00 95.88 C ANISOU 1191 C VAL A 249 13793 12078 10560 -38 -2174 -212 C ATOM 1192 O VAL A 249 44.175 46.307 318.688 1.00103.76 O ANISOU 1192 O VAL A 249 14809 13141 11474 -16 -2249 -295 O ATOM 1193 CB VAL A 249 45.365 46.066 315.685 1.00 94.86 C ANISOU 1193 CB VAL A 249 13579 11887 10576 -337 -2199 -156 C ATOM 1194 CG1 VAL A 249 45.932 47.232 316.425 1.00111.36 C ANISOU 1194 CG1 VAL A 249 15742 13956 12613 -400 -2317 -281 C ATOM 1195 CG2 VAL A 249 46.478 45.301 314.994 1.00 76.18 C ANISOU 1195 CG2 VAL A 249 11070 9618 8258 -443 -2170 -103 C ATOM 1196 N LEU A 250 42.424 46.106 317.287 1.00 90.44 N ANISOU 1196 N LEU A 250 13172 11295 9897 36 -2127 -214 N ATOM 1197 CA LEU A 250 41.499 46.825 318.160 1.00 81.92 C ANISOU 1197 CA LEU A 250 12183 10191 8751 149 -2158 -323 C ATOM 1198 C LEU A 250 41.558 46.233 319.566 1.00 99.29 C ANISOU 1198 C LEU A 250 14346 12557 10824 249 -2136 -341 C ATOM 1199 O LEU A 250 41.959 46.933 320.504 1.00 77.92 O ANISOU 1199 O LEU A 250 11684 9879 8042 259 -2225 -441 O ATOM 1200 CB LEU A 250 40.072 46.779 317.604 1.00 80.26 C ANISOU 1200 CB LEU A 250 12003 9906 8585 238 -2088 -320 C ATOM 1201 CG LEU A 250 39.588 47.743 316.513 1.00 85.26 C ANISOU 1201 CG LEU A 250 12737 10345 9312 200 -2147 -356 C ATOM 1202 CD1 LEU A 250 38.271 48.347 316.927 1.00 82.92 C ANISOU 1202 CD1 LEU A 250 12509 10006 8990 349 -2164 -476 C ATOM 1203 CD2 LEU A 250 40.569 48.834 316.121 1.00 92.83 C ANISOU 1203 CD2 LEU A 250 13793 11178 10301 50 -2273 -394 C ATOM 1204 N PRO A 251 41.175 44.970 319.780 1.00113.26 N ANISOU 1204 N PRO A 251 16048 14433 12553 320 -2024 -247 N ATOM 1205 CA PRO A 251 41.468 44.361 321.085 1.00 77.34 C ANISOU 1205 CA PRO A 251 11485 10033 7866 391 -2019 -246 C ATOM 1206 C PRO A 251 42.874 44.575 321.597 1.00 96.41 C ANISOU 1206 C PRO A 251 13880 12508 10244 336 -2133 -276 C ATOM 1207 O PRO A 251 43.035 44.999 322.746 1.00103.17 O ANISOU 1207 O PRO A 251 14781 13429 10991 384 -2196 -363 O ATOM 1208 CB PRO A 251 41.187 42.892 320.820 1.00 77.17 C ANISOU 1208 CB PRO A 251 11404 10076 7840 423 -1898 -107 C ATOM 1209 CG PRO A 251 40.029 42.930 319.839 1.00106.19 C ANISOU 1209 CG PRO A 251 15079 13660 11609 428 -1810 -92 C ATOM 1210 CD PRO A 251 39.989 44.315 319.203 1.00126.34 C ANISOU 1210 CD PRO A 251 17684 16072 14249 377 -1902 -188 C ATOM 1211 N LEU A 252 43.904 44.251 320.814 1.00109.45 N ANISOU 1211 N LEU A 252 15454 14157 11976 241 -2159 -217 N ATOM 1212 CA LEU A 252 45.249 44.537 321.295 1.00109.19 C ANISOU 1212 CA LEU A 252 15382 14196 11910 185 -2273 -276 C ATOM 1213 C LEU A 252 45.351 45.981 321.750 1.00103.36 C ANISOU 1213 C LEU A 252 14725 13395 11150 139 -2376 -418 C ATOM 1214 O LEU A 252 45.968 46.276 322.779 1.00127.14 O ANISOU 1214 O LEU A 252 17744 16492 14072 160 -2462 -499 O ATOM 1215 CB LEU A 252 46.307 44.256 320.225 1.00106.84 C ANISOU 1215 CB LEU A 252 14978 13899 11718 62 -2289 -233 C ATOM 1216 CG LEU A 252 47.749 44.562 320.685 1.00107.61 C ANISOU 1216 CG LEU A 252 15005 14094 11786 -6 -2408 -319 C ATOM 1217 CD1 LEU A 252 48.785 43.696 319.955 1.00105.42 C ANISOU 1217 CD1 LEU A 252 14581 13901 11574 -62 -2403 -269 C ATOM 1218 CD2 LEU A 252 48.159 46.037 320.509 1.00105.64 C ANISOU 1218 CD2 LEU A 252 14809 13758 11571 -153 -2494 -440 C ATOM 1219 N LEU A 253 44.756 46.900 320.996 1.00 96.59 N ANISOU 1219 N LEU A 253 13942 12383 10373 81 -2378 -455 N ATOM 1220 CA LEU A 253 45.015 48.313 321.236 1.00 95.51 C ANISOU 1220 CA LEU A 253 13899 12156 10234 11 -2492 -587 C ATOM 1221 C LEU A 253 44.164 48.887 322.371 1.00103.79 C ANISOU 1221 C LEU A 253 15041 13211 11185 142 -2520 -692 C ATOM 1222 O LEU A 253 44.697 49.545 323.271 1.00108.97 O ANISOU 1222 O LEU A 253 15731 13904 11769 135 -2617 -800 O ATOM 1223 CB LEU A 253 44.808 49.103 319.938 1.00100.64 C ANISOU 1223 CB LEU A 253 14622 12618 11000 -110 -2505 -583 C ATOM 1224 CG LEU A 253 45.991 49.955 319.455 1.00102.93 C ANISOU 1224 CG LEU A 253 14930 12845 11333 -314 -2598 -636 C ATOM 1225 CD1 LEU A 253 47.347 49.245 319.596 1.00113.55 C ANISOU 1225 CD1 LEU A 253 16118 14360 12666 -392 -2604 -615 C ATOM 1226 CD2 LEU A 253 45.827 50.392 317.995 1.00 78.86 C ANISOU 1226 CD2 LEU A 253 11950 9623 8389 -449 -2583 -586 C ATOM 1227 N GLY A 254 42.851 48.658 322.356 1.00115.33 N ANISOU 1227 N GLY A 254 16534 14647 12638 258 -2436 -679 N ATOM 1228 CA GLY A 254 41.973 49.342 323.296 1.00113.52 C ANISOU 1228 CA GLY A 254 16388 14419 12327 374 -2462 -807 C ATOM 1229 C GLY A 254 41.017 48.461 324.076 1.00109.75 C ANISOU 1229 C GLY A 254 15877 14077 11746 513 -2346 -787 C ATOM 1230 O GLY A 254 41.098 48.392 325.308 1.00 77.97 O ANISOU 1230 O GLY A 254 11864 10174 7588 577 -2361 -844 O ATOM 1231 N TRP A 255 40.093 47.804 323.371 1.00116.32 N ANISOU 1231 N TRP A 255 16674 14891 12631 549 -2230 -711 N ATOM 1232 CA TRP A 255 39.132 46.894 323.990 1.00114.25 C ANISOU 1232 CA TRP A 255 16378 14758 12273 649 -2099 -685 C ATOM 1233 C TRP A 255 39.855 45.881 324.873 1.00134.37 C ANISOU 1233 C TRP A 255 18896 17458 14699 651 -2072 -600 C ATOM 1234 O TRP A 255 40.744 45.168 324.401 1.00149.33 O ANISOU 1234 O TRP A 255 20741 19361 16638 589 -2077 -482 O ATOM 1235 CB TRP A 255 38.359 46.166 322.888 1.00 89.24 C ANISOU 1235 CB TRP A 255 13157 11547 9202 646 -1982 -587 C ATOM 1236 CG TRP A 255 36.939 46.586 322.674 1.00 89.46 C ANISOU 1236 CG TRP A 255 13197 11540 9255 732 -1933 -686 C ATOM 1237 CD1 TRP A 255 35.941 46.591 323.598 1.00 99.56 C ANISOU 1237 CD1 TRP A 255 14474 12929 10425 830 -1868 -793 C ATOM 1238 CD2 TRP A 255 36.344 47.015 321.439 1.00 94.85 C ANISOU 1238 CD2 TRP A 255 13886 12077 10075 730 -1944 -698 C ATOM 1239 NE1 TRP A 255 34.766 47.014 323.026 1.00105.60 N ANISOU 1239 NE1 TRP A 255 15228 13637 11260 898 -1842 -886 N ATOM 1240 CE2 TRP A 255 34.987 47.280 321.701 1.00101.53 C ANISOU 1240 CE2 TRP A 255 14725 12957 10895 846 -1896 -825 C ATOM 1241 CE3 TRP A 255 36.830 47.211 320.140 1.00 88.33 C ANISOU 1241 CE3 TRP A 255 13075 11102 9383 640 -1993 -620 C ATOM 1242 CZ2 TRP A 255 34.110 47.731 320.718 1.00107.98 C ANISOU 1242 CZ2 TRP A 255 15549 13659 11820 894 -1911 -880 C ATOM 1243 CZ3 TRP A 255 35.950 47.661 319.163 1.00 97.03 C ANISOU 1243 CZ3 TRP A 255 14204 12080 10583 677 -2003 -659 C ATOM 1244 CH2 TRP A 255 34.609 47.914 319.459 1.00107.36 C ANISOU 1244 CH2 TRP A 255 15504 13419 11867 812 -1970 -789 C ATOM 1245 N ASN A 256 39.476 45.796 326.151 1.00124.86 N ANISOU 1245 N ASN A 256 17728 16377 13336 727 -2049 -665 N ATOM 1246 CA ASN A 256 40.180 44.907 327.069 1.00109.74 C ANISOU 1246 CA ASN A 256 15818 14593 11284 738 -2048 -590 C ATOM 1247 C ASN A 256 39.367 44.677 328.333 1.00113.29 C ANISOU 1247 C ASN A 256 16321 15176 11547 816 -1973 -647 C ATOM 1248 O ASN A 256 38.436 45.421 328.640 1.00118.11 O ANISOU 1248 O ASN A 256 16951 15792 12133 863 -1950 -784 O ATOM 1249 CB ASN A 256 41.546 45.483 327.452 1.00102.90 C ANISOU 1249 CB ASN A 256 14959 13730 10407 700 -2206 -637 C ATOM 1250 CG ASN A 256 42.659 44.969 326.582 1.00106.65 C ANISOU 1250 CG ASN A 256 15363 14172 10989 621 -2248 -528 C ATOM 1251 OD1 ASN A 256 42.598 43.851 326.072 1.00116.73 O ANISOU 1251 OD1 ASN A 256 16597 15463 12291 621 -2164 -393 O ATOM 1252 ND2 ASN A 256 43.689 45.778 326.405 1.00101.89 N ANISOU 1252 ND2 ASN A 256 14741 13528 10445 547 -2376 -597 N ATOM 1253 N CYS A 257 39.740 43.626 329.068 1.00108.37 N ANISOU 1253 N CYS A 257 15728 14663 10786 829 -1941 -547 N ATOM 1254 CA CYS A 257 39.352 43.532 330.472 1.00111.41 C ANISOU 1254 CA CYS A 257 16189 15184 10957 882 -1911 -607 C ATOM 1255 C CYS A 257 40.159 44.511 331.313 1.00118.43 C ANISOU 1255 C CYS A 257 17114 16100 11783 905 -2067 -734 C ATOM 1256 O CYS A 257 39.601 45.281 332.104 1.00114.70 O ANISOU 1256 O CYS A 257 16681 15680 11221 949 -2072 -883 O ATOM 1257 CB CYS A 257 39.567 42.114 330.999 1.00115.86 C ANISOU 1257 CB CYS A 257 16809 15835 11376 884 -1848 -451 C ATOM 1258 SG CYS A 257 38.696 40.791 330.152 1.00119.51 S ANISOU 1258 SG CYS A 257 17251 16272 11884 844 -1663 -291 S ATOM 1259 N GLU A 258 41.483 44.492 331.148 1.00128.41 N ANISOU 1259 N GLU A 258 18357 17337 13096 876 -2197 -690 N ATOM 1260 CA GLU A 258 42.354 45.307 331.985 1.00138.03 C ANISOU 1260 CA GLU A 258 19604 18596 14247 890 -2349 -807 C ATOM 1261 C GLU A 258 42.104 46.790 331.754 1.00136.37 C ANISOU 1261 C GLU A 258 19391 18292 14131 872 -2416 -976 C ATOM 1262 O GLU A 258 41.897 47.554 332.705 1.00158.03 O ANISOU 1262 O GLU A 258 22189 21086 16770 917 -2464 -1119 O ATOM 1263 CB GLU A 258 43.818 44.963 331.707 1.00138.60 C ANISOU 1263 CB GLU A 258 19624 18666 14371 853 -2471 -740 C ATOM 1264 CG GLU A 258 44.236 43.551 332.115 1.00140.42 C ANISOU 1264 CG GLU A 258 19881 18987 14487 900 -2454 -594 C ATOM 1265 CD GLU A 258 43.769 42.480 331.142 1.00140.84 C ANISOU 1265 CD GLU A 258 19903 18986 14625 880 -2327 -435 C ATOM 1266 OE1 GLU A 258 43.218 42.836 330.080 1.00145.99 O ANISOU 1266 OE1 GLU A 258 20496 19537 15435 827 -2259 -437 O ATOM 1267 OE2 GLU A 258 43.962 41.278 331.434 1.00138.13 O ANISOU 1267 OE2 GLU A 258 19606 18693 14186 921 -2305 -309 O ATOM 1268 N LYS A 259 42.112 47.215 330.490 1.00112.30 N ANISOU 1268 N LYS A 259 16295 15100 11275 807 -2424 -963 N ATOM 1269 CA LYS A 259 42.048 48.640 330.190 1.00103.55 C ANISOU 1269 CA LYS A 259 15215 13870 10261 779 -2517 -1111 C ATOM 1270 C LYS A 259 40.653 49.207 330.418 1.00108.15 C ANISOU 1270 C LYS A 259 15840 14435 10816 861 -2453 -1230 C ATOM 1271 O LYS A 259 40.519 50.375 330.798 1.00119.05 O ANISOU 1271 O LYS A 259 17277 15767 12192 888 -2545 -1394 O ATOM 1272 CB LYS A 259 42.493 48.882 328.749 1.00106.28 C ANISOU 1272 CB LYS A 259 15518 14061 10801 673 -2545 -1051 C ATOM 1273 CG LYS A 259 43.208 50.213 328.530 1.00104.62 C ANISOU 1273 CG LYS A 259 15350 13733 10667 588 -2694 -1170 C ATOM 1274 CD LYS A 259 44.114 50.196 327.301 1.00112.93 C ANISOU 1274 CD LYS A 259 16351 14689 11868 443 -2727 -1088 C ATOM 1275 CE LYS A 259 45.246 49.174 327.427 1.00114.27 C ANISOU 1275 CE LYS A 259 16420 14991 12008 409 -2732 -989 C ATOM 1276 NZ LYS A 259 46.166 49.177 326.256 1.00108.36 N ANISOU 1276 NZ LYS A 259 15600 14176 11396 260 -2759 -934 N ATOM 1277 N LEU A 260 39.610 48.409 330.199 1.00116.72 N ANISOU 1277 N LEU A 260 16897 15567 11886 903 -2301 -1164 N ATOM 1278 CA LEU A 260 38.239 48.878 330.346 1.00123.72 C ANISOU 1278 CA LEU A 260 17794 16460 12753 985 -2231 -1293 C ATOM 1279 C LEU A 260 37.579 48.432 331.644 1.00116.73 C ANISOU 1279 C LEU A 260 16926 15766 11660 1053 -2136 -1349 C ATOM 1280 O LEU A 260 36.487 48.918 331.960 1.00112.32 O ANISOU 1280 O LEU A 260 16365 15249 11064 1126 -2086 -1499 O ATOM 1281 CB LEU A 260 37.382 48.394 329.168 1.00124.96 C ANISOU 1281 CB LEU A 260 17895 16548 13036 979 -2120 -1215 C ATOM 1282 CG LEU A 260 37.417 49.204 327.870 1.00115.82 C ANISOU 1282 CG LEU A 260 16744 15186 12074 945 -2202 -1233 C ATOM 1283 CD1 LEU A 260 38.774 49.132 327.191 1.00112.61 C ANISOU 1283 CD1 LEU A 260 16335 14690 11760 827 -2288 -1114 C ATOM 1284 CD2 LEU A 260 36.322 48.720 326.931 1.00103.78 C ANISOU 1284 CD2 LEU A 260 15164 13630 10639 971 -2083 -1190 C ATOM 1285 N GLN A 261 38.201 47.522 332.395 1.00112.71 N ANISOU 1285 N GLN A 261 16439 15377 11010 1031 -2113 -1241 N ATOM 1286 CA GLN A 261 37.586 46.949 333.592 1.00121.27 C ANISOU 1286 CA GLN A 261 17562 16642 11874 1071 -2006 -1265 C ATOM 1287 C GLN A 261 36.224 46.347 333.269 1.00124.42 C ANISOU 1287 C GLN A 261 17916 17093 12265 1077 -1818 -1253 C ATOM 1288 O GLN A 261 35.306 46.370 334.094 1.00111.30 O ANISOU 1288 O GLN A 261 16263 15569 10456 1112 -1721 -1364 O ATOM 1289 CB GLN A 261 37.460 47.990 334.707 1.00123.20 C ANISOU 1289 CB GLN A 261 17854 16957 11998 1134 -2082 -1471 C ATOM 1290 N SER A 262 36.093 45.807 332.063 1.00132.38 N ANISOU 1290 N SER A 262 18867 18004 13428 1035 -1764 -1129 N ATOM 1291 CA SER A 262 34.842 45.255 331.574 1.00127.22 C ANISOU 1291 CA SER A 262 18154 17386 12798 1032 -1594 -1121 C ATOM 1292 C SER A 262 34.721 43.780 331.948 1.00124.29 C ANISOU 1292 C SER A 262 17814 17123 12286 972 -1449 -954 C ATOM 1293 O SER A 262 35.636 43.173 332.508 1.00131.14 O ANISOU 1293 O SER A 262 18758 18021 13049 948 -1495 -836 O ATOM 1294 CB SER A 262 34.747 45.428 330.058 1.00125.52 C ANISOU 1294 CB SER A 262 17871 17004 12816 1016 -1615 -1074 C ATOM 1295 OG SER A 262 33.696 44.642 329.526 1.00128.73 O ANISOU 1295 OG SER A 262 18215 17450 13246 1000 -1450 -1029 O ATOM 1296 N VAL A 263 33.559 43.205 331.632 1.00109.75 N ANISOU 1296 N VAL A 263 15921 15339 10441 949 -1279 -953 N ATOM 1297 CA VAL A 263 33.348 41.782 331.861 1.00 94.71 C ANISOU 1297 CA VAL A 263 14060 13513 8412 873 -1131 -790 C ATOM 1298 C VAL A 263 34.297 40.992 330.977 1.00104.45 C ANISOU 1298 C VAL A 263 15304 14616 9764 834 -1184 -579 C ATOM 1299 O VAL A 263 34.409 41.246 329.771 1.00106.48 O ANISOU 1299 O VAL A 263 15483 14745 10230 836 -1225 -557 O ATOM 1300 CB VAL A 263 31.883 41.405 331.593 1.00101.41 C ANISOU 1300 CB VAL A 263 14832 14447 9251 841 -935 -854 C ATOM 1301 CG1 VAL A 263 31.663 39.910 331.810 1.00102.88 C ANISOU 1301 CG1 VAL A 263 15086 14700 9305 737 -778 -679 C ATOM 1302 CG2 VAL A 263 30.956 42.219 332.486 1.00 92.96 C ANISOU 1302 CG2 VAL A 263 13730 13527 8061 889 -886 -1093 C ATOM 1303 N CYS A 264 34.991 40.033 331.576 1.00115.31 N ANISOU 1303 N CYS A 264 16785 16027 11002 803 -1189 -430 N ATOM 1304 CA CYS A 264 35.937 39.221 330.834 1.00123.59 C ANISOU 1304 CA CYS A 264 17843 16967 12147 782 -1249 -244 C ATOM 1305 C CYS A 264 35.217 38.083 330.111 1.00115.43 C ANISOU 1305 C CYS A 264 16794 15912 11151 717 -1089 -119 C ATOM 1306 O CYS A 264 34.048 37.780 330.367 1.00123.73 O ANISOU 1306 O CYS A 264 17845 17051 12115 673 -925 -161 O ATOM 1307 CB CYS A 264 37.013 38.671 331.771 1.00131.06 C ANISOU 1307 CB CYS A 264 18913 17951 12931 801 -1349 -150 C ATOM 1308 SG CYS A 264 38.731 39.278 331.514 1.00138.37 S ANISOU 1308 SG CYS A 264 19803 18794 13977 853 -1594 -150 S ATOM 1309 N SER A 265 35.933 37.459 329.180 1.00 98.76 N ANISOU 1309 N SER A 265 14660 13690 9174 706 -1138 24 N ATOM 1310 CA SER A 265 35.426 36.300 328.462 1.00100.66 C ANISOU 1310 CA SER A 265 14897 13893 9455 647 -1007 158 C ATOM 1311 C SER A 265 35.852 35.037 329.200 1.00109.46 C ANISOU 1311 C SER A 265 16169 15032 10387 625 -992 315 C ATOM 1312 O SER A 265 37.007 34.915 329.622 1.00 98.28 O ANISOU 1312 O SER A 265 14821 13599 8924 677 -1140 370 O ATOM 1313 CB SER A 265 35.938 36.281 327.020 1.00 96.03 C ANISOU 1313 CB SER A 265 14206 13173 9109 648 -1066 221 C ATOM 1314 OG SER A 265 37.333 36.041 326.966 1.00104.29 O ANISOU 1314 OG SER A 265 15278 14167 10182 680 -1216 307 O ATOM 1315 N ASP A 266 34.912 34.106 329.366 1.00109.89 N ANISOU 1315 N ASP A 266 16290 15129 10335 546 -820 380 N ATOM 1316 CA ASP A 266 35.204 32.865 330.071 1.00106.64 C ANISOU 1316 CA ASP A 266 16066 14721 9731 513 -800 537 C ATOM 1317 C ASP A 266 36.139 31.950 329.293 1.00101.60 C ANISOU 1317 C ASP A 266 15453 13951 9200 543 -891 702 C ATOM 1318 O ASP A 266 36.621 30.964 329.858 1.00111.22 O ANISOU 1318 O ASP A 266 16843 15144 10269 549 -929 834 O ATOM 1319 CB ASP A 266 33.900 32.131 330.381 1.00112.25 C ANISOU 1319 CB ASP A 266 16845 15505 10300 392 -578 557 C ATOM 1320 CG ASP A 266 33.060 32.853 331.410 1.00111.65 C ANISOU 1320 CG ASP A 266 16773 15592 10059 360 -487 394 C ATOM 1321 OD1 ASP A 266 32.528 33.935 331.085 1.00111.84 O ANISOU 1321 OD1 ASP A 266 16633 15660 10200 393 -473 219 O ATOM 1322 OD2 ASP A 266 32.930 32.339 332.541 1.00107.45 O ANISOU 1322 OD2 ASP A 266 16415 15139 9271 304 -433 436 O ATOM 1323 N ILE A 267 36.415 32.256 328.026 1.00104.87 N ANISOU 1323 N ILE A 267 15708 14279 9859 566 -934 692 N ATOM 1324 CA ILE A 267 37.284 31.424 327.200 1.00 96.61 C ANISOU 1324 CA ILE A 267 14658 13121 8928 596 -1014 826 C ATOM 1325 C ILE A 267 38.665 32.054 327.107 1.00 87.57 C ANISOU 1325 C ILE A 267 13449 11955 7869 687 -1220 787 C ATOM 1326 O ILE A 267 39.671 31.428 327.461 1.00 87.09 O ANISOU 1326 O ILE A 267 13472 11874 7743 751 -1345 867 O ATOM 1327 CB ILE A 267 36.686 31.217 325.796 1.00 99.70 C ANISOU 1327 CB ILE A 267 14917 13440 9523 546 -912 846 C ATOM 1328 CG1 ILE A 267 35.500 30.250 325.854 1.00 92.86 C ANISOU 1328 CG1 ILE A 267 14129 12588 8565 448 -717 913 C ATOM 1329 CG2 ILE A 267 37.747 30.712 324.811 1.00 94.17 C ANISOU 1329 CG2 ILE A 267 14162 12636 8982 591 -1023 937 C ATOM 1330 CD1 ILE A 267 35.883 28.808 326.130 1.00 79.22 C ANISOU 1330 CD1 ILE A 267 12582 10796 6720 434 -721 1089 C ATOM 1331 N PHE A 268 38.727 33.294 326.622 1.00 86.52 N ANISOU 1331 N PHE A 268 13169 11824 7880 693 -1263 657 N ATOM 1332 CA PHE A 268 40.005 33.927 326.333 1.00 88.81 C ANISOU 1332 CA PHE A 268 13376 12091 8276 744 -1441 611 C ATOM 1333 C PHE A 268 40.371 34.940 327.407 1.00 85.96 C ANISOU 1333 C PHE A 268 13045 11810 7807 782 -1542 488 C ATOM 1334 O PHE A 268 39.542 35.793 327.752 1.00 82.49 O ANISOU 1334 O PHE A 268 12595 11411 7336 761 -1479 376 O ATOM 1335 CB PHE A 268 39.969 34.620 324.971 1.00 86.84 C ANISOU 1335 CB PHE A 268 12965 11770 8262 706 -1436 560 C ATOM 1336 CG PHE A 268 39.918 33.670 323.812 1.00 94.88 C ANISOU 1336 CG PHE A 268 13934 12710 9406 679 -1374 674 C ATOM 1337 CD1 PHE A 268 41.016 32.886 323.490 1.00 90.51 C ANISOU 1337 CD1 PHE A 268 13373 12128 8890 717 -1469 759 C ATOM 1338 CD2 PHE A 268 38.774 33.565 323.039 1.00107.21 C ANISOU 1338 CD2 PHE A 268 15451 14234 11051 623 -1227 682 C ATOM 1339 CE1 PHE A 268 40.971 32.009 322.424 1.00110.41 C ANISOU 1339 CE1 PHE A 268 15847 14577 11525 697 -1415 854 C ATOM 1340 CE2 PHE A 268 38.720 32.694 321.968 1.00109.65 C ANISOU 1340 CE2 PHE A 268 15716 14472 11474 597 -1171 782 C ATOM 1341 CZ PHE A 268 39.820 31.915 321.657 1.00118.05 C ANISOU 1341 CZ PHE A 268 16779 15503 12574 632 -1263 870 C ATOM 1342 N PRO A 269 41.585 34.895 327.951 1.00 87.32 N ANISOU 1342 N PRO A 269 13247 12009 7922 845 -1704 490 N ATOM 1343 CA PRO A 269 42.018 35.962 328.858 1.00 91.80 C ANISOU 1343 CA PRO A 269 13822 12647 8410 876 -1813 357 C ATOM 1344 C PRO A 269 42.144 37.301 328.148 1.00 87.11 C ANISOU 1344 C PRO A 269 13090 12016 7992 837 -1855 226 C ATOM 1345 O PRO A 269 42.396 37.376 326.944 1.00 94.96 O ANISOU 1345 O PRO A 269 13974 12933 9172 797 -1857 245 O ATOM 1346 CB PRO A 269 43.384 35.471 329.357 1.00 85.61 C ANISOU 1346 CB PRO A 269 13076 11894 7557 955 -1987 394 C ATOM 1347 CG PRO A 269 43.341 34.002 329.205 1.00 86.21 C ANISOU 1347 CG PRO A 269 13245 11930 7583 980 -1945 557 C ATOM 1348 CD PRO A 269 42.502 33.742 327.988 1.00 91.75 C ANISOU 1348 CD PRO A 269 13867 12551 8443 904 -1792 610 C ATOM 1349 N HIS A 270 41.967 38.369 328.924 1.00 93.18 N ANISOU 1349 N HIS A 270 13880 12834 8689 846 -1894 90 N ATOM 1350 CA HIS A 270 42.152 39.756 328.504 1.00 88.50 C ANISOU 1350 CA HIS A 270 13202 12199 8227 814 -1963 -50 C ATOM 1351 C HIS A 270 41.106 40.240 327.506 1.00 88.35 C ANISOU 1351 C HIS A 270 13124 12095 8350 766 -1855 -81 C ATOM 1352 O HIS A 270 41.167 41.406 327.096 1.00 90.93 O ANISOU 1352 O HIS A 270 13407 12360 8782 739 -1915 -192 O ATOM 1353 CB HIS A 270 43.533 39.996 327.872 1.00 93.98 C ANISOU 1353 CB HIS A 270 13801 12858 9048 788 -2106 -57 C ATOM 1354 CG HIS A 270 44.676 39.403 328.638 1.00101.10 C ANISOU 1354 CG HIS A 270 14731 13843 9841 849 -2231 -28 C ATOM 1355 ND1 HIS A 270 45.332 40.080 329.644 1.00103.87 N ANISOU 1355 ND1 HIS A 270 15109 14267 10088 882 -2360 -138 N ATOM 1356 CD2 HIS A 270 45.301 38.208 328.522 1.00106.21 C ANISOU 1356 CD2 HIS A 270 15382 14506 10467 895 -2262 87 C ATOM 1357 CE1 HIS A 270 46.300 39.321 330.125 1.00104.97 C ANISOU 1357 CE1 HIS A 270 15266 14472 10146 949 -2466 -92 C ATOM 1358 NE2 HIS A 270 46.302 38.179 329.462 1.00103.07 N ANISOU 1358 NE2 HIS A 270 15015 14194 9953 964 -2414 43 N ATOM 1359 N ILE A 271 40.155 39.403 327.099 1.00 87.63 N ANISOU 1359 N ILE A 271 13039 11993 8264 755 -1706 6 N ATOM 1360 CA ILE A 271 39.260 39.710 325.986 1.00 90.41 C ANISOU 1360 CA ILE A 271 13321 12263 8769 718 -1616 -13 C ATOM 1361 C ILE A 271 37.960 40.294 326.519 1.00 96.55 C ANISOU 1361 C ILE A 271 14122 13088 9473 743 -1527 -135 C ATOM 1362 O ILE A 271 37.355 39.747 327.450 1.00105.63 O ANISOU 1362 O ILE A 271 15336 14342 10455 757 -1435 -128 O ATOM 1363 CB ILE A 271 38.997 38.457 325.129 1.00 87.26 C ANISOU 1363 CB ILE A 271 12895 11827 8433 689 -1509 139 C ATOM 1364 CG1 ILE A 271 40.233 38.105 324.291 1.00 87.55 C ANISOU 1364 CG1 ILE A 271 12871 11804 8591 666 -1603 223 C ATOM 1365 CG2 ILE A 271 37.782 38.637 324.221 1.00 74.79 C ANISOU 1365 CG2 ILE A 271 11259 10195 6964 663 -1390 111 C ATOM 1366 CD1 ILE A 271 40.736 39.229 323.380 1.00 82.95 C ANISOU 1366 CD1 ILE A 271 12207 11136 8173 618 -1692 143 C ATOM 1367 N ASP A 272 37.525 41.397 325.913 1.00 84.89 N ANISOU 1367 N ASP A 272 12598 11537 8118 745 -1556 -253 N ATOM 1368 CA ASP A 272 36.284 42.050 326.299 1.00 95.80 C ANISOU 1368 CA ASP A 272 13982 12962 9456 789 -1490 -400 C ATOM 1369 C ASP A 272 35.093 41.332 325.683 1.00 97.66 C ANISOU 1369 C ASP A 272 14166 13212 9728 776 -1326 -362 C ATOM 1370 O ASP A 272 35.107 40.975 324.501 1.00 97.59 O ANISOU 1370 O ASP A 272 14105 13111 9865 742 -1305 -276 O ATOM 1371 CB ASP A 272 36.288 43.511 325.851 1.00 95.70 C ANISOU 1371 CB ASP A 272 13958 12844 9562 813 -1608 -545 C ATOM 1372 CG ASP A 272 35.212 44.334 326.533 1.00113.46 C ANISOU 1372 CG ASP A 272 16218 15152 11738 888 -1585 -736 C ATOM 1373 OD1 ASP A 272 34.372 43.751 327.252 1.00122.40 O ANISOU 1373 OD1 ASP A 272 17346 16422 12738 907 -1455 -759 O ATOM 1374 OD2 ASP A 272 35.197 45.568 326.340 1.00123.46 O ANISOU 1374 OD2 ASP A 272 17504 16328 13079 924 -1699 -870 O ATOM 1375 N LYS A 273 34.049 41.136 326.491 1.00101.39 N ANISOU 1375 N LYS A 273 14648 13811 10063 795 -1207 -439 N ATOM 1376 CA LYS A 273 32.862 40.439 326.006 1.00 91.95 C ANISOU 1376 CA LYS A 273 13394 12656 8887 770 -1039 -425 C ATOM 1377 C LYS A 273 32.170 41.230 324.906 1.00 97.64 C ANISOU 1377 C LYS A 273 14027 13284 9787 810 -1060 -530 C ATOM 1378 O LYS A 273 31.718 40.653 323.910 1.00115.09 O ANISOU 1378 O LYS A 273 16177 15448 12103 780 -984 -461 O ATOM 1379 CB LYS A 273 31.892 40.174 327.157 1.00109.40 C ANISOU 1379 CB LYS A 273 15626 15043 10900 766 -903 -516 C ATOM 1380 CG LYS A 273 32.011 38.789 327.772 1.00118.62 C ANISOU 1380 CG LYS A 273 16877 16289 11902 686 -789 -356 C ATOM 1381 CD LYS A 273 30.739 38.411 328.515 1.00122.23 C ANISOU 1381 CD LYS A 273 17330 16915 12195 641 -603 -445 C ATOM 1382 CE LYS A 273 30.934 37.173 329.374 1.00114.28 C ANISOU 1382 CE LYS A 273 16461 15983 10978 552 -509 -294 C ATOM 1383 NZ LYS A 273 31.442 36.007 328.597 1.00107.89 N ANISOU 1383 NZ LYS A 273 15692 15061 10241 498 -496 -76 N ATOM 1384 N THR A 274 32.074 42.552 325.062 1.00105.57 N ANISOU 1384 N THR A 274 15035 14252 10825 883 -1173 -700 N ATOM 1385 CA THR A 274 31.376 43.348 324.062 1.00105.98 C ANISOU 1385 CA THR A 274 15030 14203 11033 939 -1215 -809 C ATOM 1386 C THR A 274 32.167 43.453 322.766 1.00 99.44 C ANISOU 1386 C THR A 274 14210 13193 10379 897 -1310 -689 C ATOM 1387 O THR A 274 31.572 43.696 321.711 1.00 99.97 O ANISOU 1387 O THR A 274 14236 13172 10577 920 -1313 -718 O ATOM 1388 CB THR A 274 31.061 44.744 324.609 1.00102.98 C ANISOU 1388 CB THR A 274 14678 13817 10634 1039 -1326 -1029 C ATOM 1389 OG1 THR A 274 30.238 45.453 323.675 1.00107.64 O ANISOU 1389 OG1 THR A 274 15226 14312 11362 1114 -1369 -1147 O ATOM 1390 CG2 THR A 274 32.329 45.533 324.846 1.00101.98 C ANISOU 1390 CG2 THR A 274 14642 13588 10519 1026 -1499 -1015 C ATOM 1391 N TYR A 275 33.487 43.266 322.811 1.00 97.08 N ANISOU 1391 N TYR A 275 13959 12846 10080 834 -1387 -565 N ATOM 1392 CA TYR A 275 34.234 43.198 321.563 1.00 84.17 C ANISOU 1392 CA TYR A 275 12315 11069 8598 771 -1448 -448 C ATOM 1393 C TYR A 275 33.860 41.959 320.764 1.00 89.33 C ANISOU 1393 C TYR A 275 12903 11733 9303 729 -1317 -311 C ATOM 1394 O TYR A 275 33.785 42.020 319.533 1.00 87.23 O ANISOU 1394 O TYR A 275 12607 11358 9178 706 -1330 -271 O ATOM 1395 CB TYR A 275 35.740 43.207 321.812 1.00 66.83 C ANISOU 1395 CB TYR A 275 10157 8849 6384 711 -1553 -366 C ATOM 1396 CG TYR A 275 36.471 42.720 320.589 1.00 76.07 C ANISOU 1396 CG TYR A 275 11291 9928 7685 630 -1565 -227 C ATOM 1397 CD1 TYR A 275 36.538 43.507 319.452 1.00 81.47 C ANISOU 1397 CD1 TYR A 275 11982 10465 8509 595 -1637 -250 C ATOM 1398 CD2 TYR A 275 37.038 41.453 320.546 1.00 79.22 C ANISOU 1398 CD2 TYR A 275 11656 10382 8060 592 -1503 -77 C ATOM 1399 CE1 TYR A 275 37.186 43.070 318.311 1.00 98.19 C ANISOU 1399 CE1 TYR A 275 14063 12510 10736 511 -1638 -131 C ATOM 1400 CE2 TYR A 275 37.690 41.003 319.412 1.00 79.51 C ANISOU 1400 CE2 TYR A 275 11646 10347 8217 524 -1512 33 C ATOM 1401 CZ TYR A 275 37.761 41.811 318.291 1.00100.25 C ANISOU 1401 CZ TYR A 275 14268 12845 10978 478 -1572 4 C ATOM 1402 OH TYR A 275 38.413 41.341 317.172 1.00113.81 O ANISOU 1402 OH TYR A 275 15936 14507 12801 400 -1570 108 O ATOM 1403 N LEU A 276 33.616 40.832 321.437 1.00 77.50 N ANISOU 1403 N LEU A 276 11398 10361 7689 713 -1192 -238 N ATOM 1404 CA LEU A 276 33.261 39.617 320.712 1.00 73.40 C ANISOU 1404 CA LEU A 276 10831 9845 7215 666 -1067 -109 C ATOM 1405 C LEU A 276 31.916 39.767 320.019 1.00 87.92 C ANISOU 1405 C LEU A 276 12596 11679 9129 695 -984 -198 C ATOM 1406 O LEU A 276 31.755 39.338 318.871 1.00 98.45 O ANISOU 1406 O LEU A 276 13882 12940 10585 666 -951 -125 O ATOM 1407 CB LEU A 276 33.243 38.415 321.656 1.00 79.58 C ANISOU 1407 CB LEU A 276 11653 10746 7836 634 -957 -17 C ATOM 1408 CG LEU A 276 34.577 37.804 322.095 1.00 84.52 C ANISOU 1408 CG LEU A 276 12345 11369 8400 611 -1028 117 C ATOM 1409 CD1 LEU A 276 34.318 36.430 322.695 1.00 81.98 C ANISOU 1409 CD1 LEU A 276 12083 11127 7941 576 -905 231 C ATOM 1410 CD2 LEU A 276 35.586 37.707 320.954 1.00 85.12 C ANISOU 1410 CD2 LEU A 276 12381 11329 8633 581 -1115 212 C ATOM 1411 N MET A 277 30.934 40.365 320.696 1.00 86.31 N ANISOU 1411 N MET A 277 12377 11562 8854 758 -952 -370 N ATOM 1412 CA MET A 277 29.662 40.643 320.041 1.00 91.34 C ANISOU 1412 CA MET A 277 12931 12204 9569 809 -898 -492 C ATOM 1413 C MET A 277 29.893 41.341 318.707 1.00 91.33 C ANISOU 1413 C MET A 277 12928 12025 9747 833 -1020 -487 C ATOM 1414 O MET A 277 29.401 40.900 317.661 1.00 74.47 O ANISOU 1414 O MET A 277 10734 9846 7714 820 -968 -445 O ATOM 1415 CB MET A 277 28.780 41.499 320.949 1.00 88.92 C ANISOU 1415 CB MET A 277 12607 12005 9175 898 -899 -715 C ATOM 1416 CG MET A 277 28.320 40.791 322.208 1.00118.64 C ANISOU 1416 CG MET A 277 16365 15965 12747 859 -750 -739 C ATOM 1417 SD MET A 277 26.943 41.645 323.006 1.00146.90 S ANISOU 1417 SD MET A 277 19869 19706 16242 961 -707 -1037 S ATOM 1418 CE MET A 277 27.704 43.205 323.467 1.00150.18 C ANISOU 1418 CE MET A 277 20374 20018 16667 1065 -931 -1155 C ATOM 1419 N PHE A 278 30.663 42.430 318.731 1.00 91.13 N ANISOU 1419 N PHE A 278 12980 11891 9753 857 -1184 -527 N ATOM 1420 CA PHE A 278 31.002 43.140 317.502 1.00 94.64 C ANISOU 1420 CA PHE A 278 13460 12153 10347 854 -1307 -511 C ATOM 1421 C PHE A 278 31.691 42.210 316.509 1.00 82.42 C ANISOU 1421 C PHE A 278 11888 10547 8880 753 -1266 -316 C ATOM 1422 O PHE A 278 31.309 42.144 315.336 1.00 75.95 O ANISOU 1422 O PHE A 278 11041 9643 8173 748 -1262 -290 O ATOM 1423 CB PHE A 278 31.880 44.347 317.844 1.00103.66 C ANISOU 1423 CB PHE A 278 14706 13196 11482 858 -1477 -569 C ATOM 1424 CG PHE A 278 32.749 44.820 316.714 1.00112.89 C ANISOU 1424 CG PHE A 278 15938 14186 12769 783 -1590 -486 C ATOM 1425 CD1 PHE A 278 32.276 45.733 315.782 1.00114.69 C ANISOU 1425 CD1 PHE A 278 16223 14259 13093 825 -1689 -560 C ATOM 1426 CD2 PHE A 278 34.054 44.371 316.603 1.00114.37 C ANISOU 1426 CD2 PHE A 278 16132 14363 12960 669 -1604 -343 C ATOM 1427 CE1 PHE A 278 33.089 46.175 314.748 1.00108.60 C ANISOU 1427 CE1 PHE A 278 15530 13322 12411 731 -1785 -479 C ATOM 1428 CE2 PHE A 278 34.868 44.803 315.581 1.00110.66 C ANISOU 1428 CE2 PHE A 278 15710 13750 12586 578 -1693 -280 C ATOM 1429 CZ PHE A 278 34.390 45.708 314.649 1.00109.73 C ANISOU 1429 CZ PHE A 278 15664 13474 12553 597 -1778 -341 C ATOM 1430 N TRP A 279 32.697 41.465 316.968 1.00 72.24 N ANISOU 1430 N TRP A 279 10608 9307 7533 680 -1241 -187 N ATOM 1431 CA TRP A 279 33.406 40.552 316.077 1.00 79.30 C ANISOU 1431 CA TRP A 279 11472 10158 8502 596 -1209 -18 C ATOM 1432 C TRP A 279 32.475 39.468 315.546 1.00 90.78 C ANISOU 1432 C TRP A 279 12851 11658 9983 592 -1061 36 C ATOM 1433 O TRP A 279 32.412 39.227 314.335 1.00 96.33 O ANISOU 1433 O TRP A 279 13520 12280 10801 562 -1052 96 O ATOM 1434 CB TRP A 279 34.596 39.927 316.804 1.00 85.61 C ANISOU 1434 CB TRP A 279 12291 11017 9219 548 -1222 83 C ATOM 1435 CG TRP A 279 34.964 38.561 316.285 1.00 97.10 C ANISOU 1435 CG TRP A 279 13702 12489 10702 496 -1138 242 C ATOM 1436 CD1 TRP A 279 34.575 37.353 316.798 1.00106.98 C ANISOU 1436 CD1 TRP A 279 14947 13831 11869 497 -1017 315 C ATOM 1437 CD2 TRP A 279 35.792 38.266 315.154 1.00 89.81 C ANISOU 1437 CD2 TRP A 279 12745 11487 9893 431 -1173 341 C ATOM 1438 NE1 TRP A 279 35.109 36.327 316.054 1.00 85.52 N ANISOU 1438 NE1 TRP A 279 12199 11083 9214 451 -986 452 N ATOM 1439 CE2 TRP A 279 35.860 36.861 315.040 1.00 88.97 C ANISOU 1439 CE2 TRP A 279 12606 11426 9773 415 -1077 464 C ATOM 1440 CE3 TRP A 279 36.482 39.052 314.229 1.00 79.87 C ANISOU 1440 CE3 TRP A 279 11487 10123 8737 376 -1273 333 C ATOM 1441 CZ2 TRP A 279 36.593 36.228 314.038 1.00 74.40 C ANISOU 1441 CZ2 TRP A 279 10713 9533 8021 363 -1082 566 C ATOM 1442 CZ3 TRP A 279 37.206 38.423 313.236 1.00 94.93 C ANISOU 1442 CZ3 TRP A 279 13344 11997 10729 307 -1265 436 C ATOM 1443 CH2 TRP A 279 37.258 37.025 313.147 1.00 95.62 C ANISOU 1443 CH2 TRP A 279 13383 12139 10808 310 -1172 546 C ATOM 1444 N ILE A 280 31.749 38.797 316.441 1.00 80.29 N ANISOU 1444 N ILE A 280 11501 10462 8542 611 -940 13 N ATOM 1445 CA ILE A 280 30.865 37.712 316.021 1.00 69.10 C ANISOU 1445 CA ILE A 280 10018 9098 7140 585 -788 61 C ATOM 1446 C ILE A 280 29.814 38.234 315.050 1.00 80.03 C ANISOU 1446 C ILE A 280 11337 10436 8635 634 -787 -45 C ATOM 1447 O ILE A 280 29.553 37.631 314.002 1.00 83.38 O ANISOU 1447 O ILE A 280 11711 10816 9155 603 -736 23 O ATOM 1448 CB ILE A 280 30.217 37.042 317.247 1.00 80.03 C ANISOU 1448 CB ILE A 280 11407 10639 8361 576 -656 33 C ATOM 1449 CG1 ILE A 280 31.269 36.302 318.082 1.00 84.04 C ANISOU 1449 CG1 ILE A 280 11998 11176 8756 530 -662 167 C ATOM 1450 CG2 ILE A 280 29.095 36.082 316.830 1.00 76.16 C ANISOU 1450 CG2 ILE A 280 10844 10212 7882 537 -491 42 C ATOM 1451 CD1 ILE A 280 31.926 35.124 317.371 1.00 91.06 C ANISOU 1451 CD1 ILE A 280 12892 12006 9702 470 -634 349 C ATOM 1452 N GLY A 281 29.193 39.364 315.385 1.00 78.14 N ANISOU 1452 N GLY A 281 11102 10204 8384 722 -853 -222 N ATOM 1453 CA GLY A 281 28.152 39.900 314.525 1.00 77.30 C ANISOU 1453 CA GLY A 281 10940 10054 8375 795 -874 -344 C ATOM 1454 C GLY A 281 28.659 40.246 313.138 1.00 79.62 C ANISOU 1454 C GLY A 281 11269 10173 8811 778 -979 -268 C ATOM 1455 O GLY A 281 27.967 40.027 312.141 1.00 79.41 O ANISOU 1455 O GLY A 281 11186 10113 8872 796 -952 -278 O ATOM 1456 N VAL A 282 29.879 40.781 313.054 1.00 71.09 N ANISOU 1456 N VAL A 282 10279 8985 7745 733 -1098 -196 N ATOM 1457 CA VAL A 282 30.433 41.182 311.763 1.00 75.54 C ANISOU 1457 CA VAL A 282 10891 9386 8425 691 -1196 -127 C ATOM 1458 C VAL A 282 30.645 39.965 310.870 1.00 89.31 C ANISOU 1458 C VAL A 282 12569 11134 10230 610 -1095 28 C ATOM 1459 O VAL A 282 30.259 39.963 309.695 1.00 94.90 O ANISOU 1459 O VAL A 282 13262 11763 11033 610 -1105 41 O ATOM 1460 CB VAL A 282 31.738 41.974 311.967 1.00 81.01 C ANISOU 1460 CB VAL A 282 11686 9988 9105 632 -1327 -93 C ATOM 1461 CG1 VAL A 282 32.551 42.054 310.668 1.00 81.56 C ANISOU 1461 CG1 VAL A 282 11794 9924 9273 533 -1386 17 C ATOM 1462 CG2 VAL A 282 31.422 43.376 312.474 1.00 73.64 C ANISOU 1462 CG2 VAL A 282 10841 8994 8144 718 -1458 -258 C ATOM 1463 N VAL A 283 31.268 38.914 311.407 1.00 89.66 N ANISOU 1463 N VAL A 283 12583 11265 10218 546 -1008 142 N ATOM 1464 CA VAL A 283 31.540 37.739 310.583 1.00 84.87 C ANISOU 1464 CA VAL A 283 11923 10655 9670 476 -924 284 C ATOM 1465 C VAL A 283 30.270 36.931 310.348 1.00 90.41 C ANISOU 1465 C VAL A 283 12544 11427 10383 501 -788 260 C ATOM 1466 O VAL A 283 30.120 36.298 309.296 1.00 88.23 O ANISOU 1466 O VAL A 283 12221 11112 10190 466 -742 329 O ATOM 1467 CB VAL A 283 32.641 36.871 311.215 1.00 76.58 C ANISOU 1467 CB VAL A 283 10881 9661 8556 417 -896 406 C ATOM 1468 CG1 VAL A 283 33.944 37.654 311.305 1.00 72.67 C ANISOU 1468 CG1 VAL A 283 10441 9108 8063 380 -1030 417 C ATOM 1469 CG2 VAL A 283 32.213 36.362 312.583 1.00 89.09 C ANISOU 1469 CG2 VAL A 283 12474 11373 10005 446 -812 381 C ATOM 1470 N SER A 284 29.339 36.937 311.306 1.00 90.47 N ANISOU 1470 N SER A 284 12525 11547 10303 552 -718 152 N ATOM 1471 CA SER A 284 28.082 36.222 311.115 1.00 81.43 C ANISOU 1471 CA SER A 284 11289 10487 9162 560 -582 103 C ATOM 1472 C SER A 284 27.264 36.837 309.987 1.00 86.49 C ANISOU 1472 C SER A 284 11885 11060 9917 624 -635 5 C ATOM 1473 O SER A 284 26.711 36.116 309.149 1.00 88.09 O ANISOU 1473 O SER A 284 12018 11269 10186 601 -557 35 O ATOM 1474 CB SER A 284 27.279 36.218 312.413 1.00 75.94 C ANISOU 1474 CB SER A 284 10573 9945 8337 587 -496 -16 C ATOM 1475 OG SER A 284 27.918 35.432 313.399 1.00 74.47 O ANISOU 1475 OG SER A 284 10441 9822 8032 519 -431 91 O ATOM 1476 N VAL A 285 27.168 38.168 309.954 1.00 88.80 N ANISOU 1476 N VAL A 285 12227 11281 10230 711 -776 -116 N ATOM 1477 CA VAL A 285 26.464 38.835 308.861 1.00 84.46 C ANISOU 1477 CA VAL A 285 11668 10642 9782 789 -860 -208 C ATOM 1478 C VAL A 285 27.142 38.520 307.536 1.00 75.19 C ANISOU 1478 C VAL A 285 10524 9339 8705 715 -894 -59 C ATOM 1479 O VAL A 285 26.491 38.137 306.557 1.00 77.40 O ANISOU 1479 O VAL A 285 10745 9603 9059 727 -861 -62 O ATOM 1480 CB VAL A 285 26.394 40.353 309.112 1.00 75.69 C ANISOU 1480 CB VAL A 285 10647 9447 8665 895 -1031 -352 C ATOM 1481 CG1 VAL A 285 25.969 41.115 307.843 1.00 73.01 C ANISOU 1481 CG1 VAL A 285 10355 8959 8428 969 -1162 -408 C ATOM 1482 CG2 VAL A 285 25.431 40.651 310.245 1.00 76.74 C ANISOU 1482 CG2 VAL A 285 10717 9727 8714 992 -990 -542 C ATOM 1483 N LEU A 286 28.465 38.683 307.485 1.00 69.60 N ANISOU 1483 N LEU A 286 9900 8549 7995 635 -959 63 N ATOM 1484 CA LEU A 286 29.192 38.423 306.249 1.00 78.87 C ANISOU 1484 CA LEU A 286 11099 9617 9251 552 -987 192 C ATOM 1485 C LEU A 286 28.993 36.987 305.784 1.00 74.98 C ANISOU 1485 C LEU A 286 10505 9194 8790 497 -841 292 C ATOM 1486 O LEU A 286 28.750 36.741 304.597 1.00 77.70 O ANISOU 1486 O LEU A 286 10826 9480 9216 482 -838 325 O ATOM 1487 CB LEU A 286 30.677 38.726 306.444 1.00 73.37 C ANISOU 1487 CB LEU A 286 10480 8865 8532 461 -1059 286 C ATOM 1488 CG LEU A 286 31.070 40.203 306.389 1.00 66.22 C ANISOU 1488 CG LEU A 286 9703 7832 7624 472 -1224 217 C ATOM 1489 CD1 LEU A 286 32.481 40.391 306.918 1.00 62.22 C ANISOU 1489 CD1 LEU A 286 9244 7323 7074 377 -1269 284 C ATOM 1490 CD2 LEU A 286 30.961 40.730 304.969 1.00 53.07 C ANISOU 1490 CD2 LEU A 286 8107 6019 6039 451 -1307 231 C ATOM 1491 N LEU A 287 29.082 36.025 306.703 1.00 54.54 N ANISOU 1491 N LEU A 287 7870 6721 6132 466 -725 340 N ATOM 1492 CA LEU A 287 28.909 34.626 306.322 1.00 66.99 C ANISOU 1492 CA LEU A 287 9374 8348 7731 410 -592 436 C ATOM 1493 C LEU A 287 27.480 34.343 305.874 1.00 74.41 C ANISOU 1493 C LEU A 287 10227 9338 8708 452 -511 342 C ATOM 1494 O LEU A 287 27.263 33.590 304.917 1.00 76.33 O ANISOU 1494 O LEU A 287 10419 9562 9022 416 -454 399 O ATOM 1495 CB LEU A 287 29.297 33.712 307.486 1.00 51.05 C ANISOU 1495 CB LEU A 287 7362 6424 5610 369 -501 506 C ATOM 1496 CG LEU A 287 30.766 33.289 307.544 1.00 55.00 C ANISOU 1496 CG LEU A 287 7908 6888 6102 311 -543 643 C ATOM 1497 CD1 LEU A 287 31.056 32.533 308.823 1.00 58.73 C ANISOU 1497 CD1 LEU A 287 8414 7446 6455 298 -482 693 C ATOM 1498 CD2 LEU A 287 31.142 32.435 306.346 1.00 57.58 C ANISOU 1498 CD2 LEU A 287 8193 7162 6522 257 -513 750 C ATOM 1499 N LEU A 288 26.493 34.925 306.557 1.00 71.92 N ANISOU 1499 N LEU A 288 9883 9097 8345 530 -506 183 N ATOM 1500 CA LEU A 288 25.108 34.751 306.133 1.00 93.29 C ANISOU 1500 CA LEU A 288 12486 11870 11088 579 -440 60 C ATOM 1501 C LEU A 288 24.910 35.239 304.704 1.00 94.81 C ANISOU 1501 C LEU A 288 12682 11946 11397 626 -541 42 C ATOM 1502 O LEU A 288 24.210 34.599 303.910 1.00 87.14 O ANISOU 1502 O LEU A 288 11626 10998 10484 618 -474 31 O ATOM 1503 CB LEU A 288 24.173 35.489 307.088 1.00 93.40 C ANISOU 1503 CB LEU A 288 12465 11990 11035 672 -444 -138 C ATOM 1504 CG LEU A 288 23.682 34.636 308.254 1.00 82.03 C ANISOU 1504 CG LEU A 288 10965 10722 9480 611 -272 -162 C ATOM 1505 CD1 LEU A 288 23.279 35.522 309.415 1.00 81.96 C ANISOU 1505 CD1 LEU A 288 10959 10804 9377 688 -302 -327 C ATOM 1506 CD2 LEU A 288 22.518 33.764 307.798 1.00 80.16 C ANISOU 1506 CD2 LEU A 288 10598 10587 9273 578 -131 -224 C ATOM 1507 N PHE A 289 25.527 36.370 304.357 1.00 75.86 N ANISOU 1507 N PHE A 289 10390 9413 9021 665 -705 39 N ATOM 1508 CA PHE A 289 25.449 36.856 302.987 1.00 69.18 C ANISOU 1508 CA PHE A 289 9585 8435 8264 693 -812 42 C ATOM 1509 C PHE A 289 26.209 35.942 302.034 1.00 73.55 C ANISOU 1509 C PHE A 289 10133 8941 8872 578 -759 216 C ATOM 1510 O PHE A 289 25.712 35.619 300.949 1.00 70.07 O ANISOU 1510 O PHE A 289 9652 8472 8501 584 -749 217 O ATOM 1511 CB PHE A 289 25.994 38.277 302.901 1.00 69.87 C ANISOU 1511 CB PHE A 289 9821 8379 8346 736 -997 9 C ATOM 1512 CG PHE A 289 26.310 38.704 301.502 1.00 86.40 C ANISOU 1512 CG PHE A 289 12007 10314 10508 713 -1105 69 C ATOM 1513 CD1 PHE A 289 25.301 39.115 300.649 1.00 90.94 C ANISOU 1513 CD1 PHE A 289 12584 10836 11132 819 -1181 -35 C ATOM 1514 CD2 PHE A 289 27.612 38.671 301.031 1.00 79.86 C ANISOU 1514 CD2 PHE A 289 11259 9399 9686 583 -1131 221 C ATOM 1515 CE1 PHE A 289 25.586 39.499 299.355 1.00 81.55 C ANISOU 1515 CE1 PHE A 289 11502 9496 9989 791 -1283 27 C ATOM 1516 CE2 PHE A 289 27.903 39.052 299.740 1.00 75.51 C ANISOU 1516 CE2 PHE A 289 10800 8711 9180 540 -1218 276 C ATOM 1517 CZ PHE A 289 26.889 39.467 298.899 1.00 78.85 C ANISOU 1517 CZ PHE A 289 11249 9068 9643 642 -1295 187 C ATOM 1518 N ILE A 290 27.419 35.522 302.415 1.00 68.71 N ANISOU 1518 N ILE A 290 9555 8324 8227 480 -731 350 N ATOM 1519 CA ILE A 290 28.224 34.680 301.533 1.00 64.32 C ANISOU 1519 CA ILE A 290 8986 7731 7721 380 -690 498 C ATOM 1520 C ILE A 290 27.495 33.378 301.233 1.00 75.10 C ANISOU 1520 C ILE A 290 10241 9177 9118 363 -546 520 C ATOM 1521 O ILE A 290 27.515 32.885 300.097 1.00 70.09 O ANISOU 1521 O ILE A 290 9578 8501 8553 327 -529 576 O ATOM 1522 CB ILE A 290 29.611 34.422 302.152 1.00 59.40 C ANISOU 1522 CB ILE A 290 8401 7117 7053 301 -690 608 C ATOM 1523 CG1 ILE A 290 30.454 35.695 302.111 1.00 61.18 C ANISOU 1523 CG1 ILE A 290 8736 7246 7266 282 -836 596 C ATOM 1524 CG2 ILE A 290 30.343 33.288 301.413 1.00 59.98 C ANISOU 1524 CG2 ILE A 290 8428 7189 7172 214 -624 740 C ATOM 1525 CD1 ILE A 290 31.721 35.612 302.953 1.00 65.49 C ANISOU 1525 CD1 ILE A 290 9305 7824 7755 222 -849 660 C ATOM 1526 N VAL A 291 26.840 32.800 302.242 1.00 74.58 N ANISOU 1526 N VAL A 291 10117 9228 8993 377 -437 474 N ATOM 1527 CA VAL A 291 26.097 31.564 302.023 1.00 71.53 C ANISOU 1527 CA VAL A 291 9636 8917 8626 340 -293 487 C ATOM 1528 C VAL A 291 24.999 31.798 300.994 1.00 72.08 C ANISOU 1528 C VAL A 291 9637 8977 8772 397 -309 382 C ATOM 1529 O VAL A 291 24.869 31.053 300.016 1.00 77.82 O ANISOU 1529 O VAL A 291 10319 9685 9566 357 -263 434 O ATOM 1530 CB VAL A 291 25.537 31.030 303.354 1.00 66.07 C ANISOU 1530 CB VAL A 291 8913 8354 7835 325 -173 443 C ATOM 1531 CG1 VAL A 291 24.469 29.962 303.120 1.00 44.18 C ANISOU 1531 CG1 VAL A 291 6043 5667 5078 282 -23 411 C ATOM 1532 CG2 VAL A 291 26.668 30.451 304.198 1.00 54.18 C ANISOU 1532 CG2 VAL A 291 7483 6848 6256 262 -150 578 C ATOM 1533 N TYR A 292 24.211 32.856 301.185 1.00 70.85 N ANISOU 1533 N TYR A 292 9477 8834 8608 502 -388 224 N ATOM 1534 CA TYR A 292 23.176 33.196 300.215 1.00 65.93 C ANISOU 1534 CA TYR A 292 8797 8199 8055 583 -436 105 C ATOM 1535 C TYR A 292 23.782 33.445 298.841 1.00 66.40 C ANISOU 1535 C TYR A 292 8930 8113 8187 567 -539 196 C ATOM 1536 O TYR A 292 23.294 32.931 297.829 1.00 78.03 O ANISOU 1536 O TYR A 292 10344 9581 9723 563 -512 195 O ATOM 1537 CB TYR A 292 22.400 34.426 300.689 1.00 65.83 C ANISOU 1537 CB TYR A 292 8792 8205 8017 722 -541 -87 C ATOM 1538 CG TYR A 292 21.424 34.951 299.663 1.00 74.64 C ANISOU 1538 CG TYR A 292 9872 9286 9202 838 -638 -221 C ATOM 1539 CD1 TYR A 292 21.821 35.881 298.712 1.00 81.88 C ANISOU 1539 CD1 TYR A 292 10921 10033 10159 890 -815 -196 C ATOM 1540 CD2 TYR A 292 20.108 34.514 299.639 1.00 74.06 C ANISOU 1540 CD2 TYR A 292 9640 9352 9147 889 -555 -377 C ATOM 1541 CE1 TYR A 292 20.936 36.362 297.765 1.00 86.62 C ANISOU 1541 CE1 TYR A 292 11511 10589 10813 1009 -922 -315 C ATOM 1542 CE2 TYR A 292 19.213 34.990 298.698 1.00 90.40 C ANISOU 1542 CE2 TYR A 292 11672 11397 11280 1013 -659 -514 C ATOM 1543 CZ TYR A 292 19.631 35.913 297.763 1.00 96.21 C ANISOU 1543 CZ TYR A 292 12556 11949 12052 1081 -850 -478 C ATOM 1544 OH TYR A 292 18.741 36.385 296.825 1.00102.95 O ANISOU 1544 OH TYR A 292 13392 12766 12958 1216 -971 -612 O ATOM 1545 N ALA A 293 24.854 34.237 298.787 1.00 69.91 N ANISOU 1545 N ALA A 293 9504 8443 8615 547 -654 271 N ATOM 1546 CA ALA A 293 25.447 34.599 297.506 1.00 71.49 C ANISOU 1546 CA ALA A 293 9791 8507 8864 513 -752 349 C ATOM 1547 C ALA A 293 25.960 33.369 296.771 1.00 69.54 C ANISOU 1547 C ALA A 293 9487 8275 8661 405 -647 483 C ATOM 1548 O ALA A 293 25.694 33.188 295.578 1.00 68.86 O ANISOU 1548 O ALA A 293 9391 8143 8630 400 -665 495 O ATOM 1549 CB ALA A 293 26.576 35.607 297.723 1.00 73.62 C ANISOU 1549 CB ALA A 293 10208 8671 9095 475 -872 402 C ATOM 1550 N TYR A 294 26.704 32.508 297.470 1.00 70.52 N ANISOU 1550 N TYR A 294 9578 8459 8755 325 -547 580 N ATOM 1551 CA TYR A 294 27.283 31.338 296.817 1.00 65.97 C ANISOU 1551 CA TYR A 294 8956 7889 8220 235 -462 701 C ATOM 1552 C TYR A 294 26.209 30.399 296.276 1.00 71.30 C ANISOU 1552 C TYR A 294 9526 8620 8944 247 -361 663 C ATOM 1553 O TYR A 294 26.431 29.726 295.264 1.00 69.99 O ANISOU 1553 O TYR A 294 9333 8427 8833 197 -331 729 O ATOM 1554 CB TYR A 294 28.204 30.596 297.786 1.00 63.47 C ANISOU 1554 CB TYR A 294 8636 7624 7855 176 -392 794 C ATOM 1555 CG TYR A 294 29.580 31.224 297.936 1.00 67.25 C ANISOU 1555 CG TYR A 294 9194 8050 8306 130 -483 858 C ATOM 1556 CD1 TYR A 294 29.816 32.544 297.562 1.00 65.86 C ANISOU 1556 CD1 TYR A 294 9108 7789 8127 137 -612 819 C ATOM 1557 CD2 TYR A 294 30.644 30.488 298.437 1.00 62.84 C ANISOU 1557 CD2 TYR A 294 8626 7526 7723 77 -445 951 C ATOM 1558 CE1 TYR A 294 31.071 33.115 297.693 1.00 65.68 C ANISOU 1558 CE1 TYR A 294 9153 7727 8076 71 -685 868 C ATOM 1559 CE2 TYR A 294 31.905 31.051 298.576 1.00 70.65 C ANISOU 1559 CE2 TYR A 294 9666 8490 8689 31 -526 988 C ATOM 1560 CZ TYR A 294 32.114 32.366 298.199 1.00 69.28 C ANISOU 1560 CZ TYR A 294 9571 8242 8512 17 -638 946 C ATOM 1561 OH TYR A 294 33.364 32.937 298.333 1.00 69.33 O ANISOU 1561 OH TYR A 294 9622 8230 8491 -52 -710 974 O ATOM 1562 N MET A 295 25.048 30.333 296.930 1.00 68.05 N ANISOU 1562 N MET A 295 9047 8297 8512 304 -304 547 N ATOM 1563 CA MET A 295 23.940 29.561 296.378 1.00 68.11 C ANISOU 1563 CA MET A 295 8945 8366 8568 310 -214 483 C ATOM 1564 C MET A 295 23.406 30.209 295.107 1.00 74.21 C ANISOU 1564 C MET A 295 9720 9075 9403 378 -321 413 C ATOM 1565 O MET A 295 23.166 29.528 294.102 1.00 82.85 O ANISOU 1565 O MET A 295 10763 10161 10556 349 -283 437 O ATOM 1566 CB MET A 295 22.828 29.426 297.416 1.00 80.25 C ANISOU 1566 CB MET A 295 10400 10034 10057 341 -125 353 C ATOM 1567 CG MET A 295 23.192 28.579 298.633 1.00103.93 C ANISOU 1567 CG MET A 295 13407 13101 12979 258 0 426 C ATOM 1568 SD MET A 295 23.762 26.913 298.223 1.00108.84 S ANISOU 1568 SD MET A 295 14024 13702 13627 134 123 591 S ATOM 1569 CE MET A 295 25.525 27.073 298.508 1.00 94.76 C ANISOU 1569 CE MET A 295 12361 11828 11817 111 38 750 C ATOM 1570 N TYR A 296 23.206 31.529 295.137 1.00 70.61 N ANISOU 1570 N TYR A 296 9336 8563 8930 474 -463 323 N ATOM 1571 CA TYR A 296 22.743 32.243 293.952 1.00 62.13 C ANISOU 1571 CA TYR A 296 8303 7404 7900 551 -593 260 C ATOM 1572 C TYR A 296 23.753 32.119 292.816 1.00 66.54 C ANISOU 1572 C TYR A 296 8946 7851 8484 463 -634 406 C ATOM 1573 O TYR A 296 23.378 31.876 291.663 1.00 69.50 O ANISOU 1573 O TYR A 296 9304 8198 8905 470 -652 401 O ATOM 1574 CB TYR A 296 22.484 33.708 294.316 1.00 51.16 C ANISOU 1574 CB TYR A 296 7012 5951 6475 672 -755 148 C ATOM 1575 CG TYR A 296 22.113 34.619 293.166 1.00 61.96 C ANISOU 1575 CG TYR A 296 8478 7196 7868 763 -927 91 C ATOM 1576 CD1 TYR A 296 20.789 34.792 292.787 1.00 61.33 C ANISOU 1576 CD1 TYR A 296 8321 7161 7821 900 -977 -80 C ATOM 1577 CD2 TYR A 296 23.088 35.332 292.480 1.00 74.12 C ANISOU 1577 CD2 TYR A 296 10196 8576 9390 709 -1046 200 C ATOM 1578 CE1 TYR A 296 20.448 35.637 291.743 1.00 84.07 C ANISOU 1578 CE1 TYR A 296 11313 9915 10714 1000 -1156 -133 C ATOM 1579 CE2 TYR A 296 22.759 36.177 291.435 1.00 73.19 C ANISOU 1579 CE2 TYR A 296 10204 8327 9276 784 -1212 158 C ATOM 1580 CZ TYR A 296 21.437 36.326 291.071 1.00 79.72 C ANISOU 1580 CZ TYR A 296 10967 9187 10135 939 -1274 -5 C ATOM 1581 OH TYR A 296 21.099 37.166 290.033 1.00 74.80 O ANISOU 1581 OH TYR A 296 10489 8424 9508 1030 -1458 -47 O ATOM 1582 N ILE A 297 25.044 32.248 293.132 1.00 59.89 N ANISOU 1582 N ILE A 297 8187 6960 7607 374 -642 528 N ATOM 1583 CA ILE A 297 26.087 32.129 292.115 1.00 55.31 C ANISOU 1583 CA ILE A 297 7672 6300 7042 272 -667 653 C ATOM 1584 C ILE A 297 26.025 30.758 291.455 1.00 70.88 C ANISOU 1584 C ILE A 297 9534 8330 9068 214 -543 710 C ATOM 1585 O ILE A 297 26.039 30.639 290.223 1.00 67.91 O ANISOU 1585 O ILE A 297 9172 7906 8725 188 -569 736 O ATOM 1586 CB ILE A 297 27.469 32.394 292.740 1.00 57.74 C ANISOU 1586 CB ILE A 297 8050 6586 7304 184 -679 748 C ATOM 1587 CG1 ILE A 297 27.573 33.859 293.164 1.00 61.74 C ANISOU 1587 CG1 ILE A 297 8692 7007 7759 229 -821 693 C ATOM 1588 CG2 ILE A 297 28.602 32.046 291.768 1.00 56.62 C ANISOU 1588 CG2 ILE A 297 7933 6405 7176 61 -671 864 C ATOM 1589 CD1 ILE A 297 28.566 34.102 294.270 1.00 59.12 C ANISOU 1589 CD1 ILE A 297 8391 6695 7376 178 -819 735 C ATOM 1590 N LEU A 298 25.952 29.702 292.268 1.00 69.85 N ANISOU 1590 N LEU A 298 9305 8295 8939 189 -410 730 N ATOM 1591 CA LEU A 298 25.897 28.349 291.726 1.00 68.85 C ANISOU 1591 CA LEU A 298 9088 8211 8862 133 -294 782 C ATOM 1592 C LEU A 298 24.609 28.119 290.945 1.00 76.91 C ANISOU 1592 C LEU A 298 10033 9256 9932 186 -279 684 C ATOM 1593 O LEU A 298 24.618 27.428 289.919 1.00 81.29 O ANISOU 1593 O LEU A 298 10551 9800 10535 146 -246 720 O ATOM 1594 CB LEU A 298 26.026 27.330 292.857 1.00 74.30 C ANISOU 1594 CB LEU A 298 9726 8978 9528 96 -169 822 C ATOM 1595 CG LEU A 298 26.059 25.857 292.436 1.00 70.71 C ANISOU 1595 CG LEU A 298 9202 8549 9116 34 -53 884 C ATOM 1596 CD1 LEU A 298 27.416 25.479 291.848 1.00 68.49 C ANISOU 1596 CD1 LEU A 298 8952 8220 8853 -28 -73 999 C ATOM 1597 CD2 LEU A 298 25.714 24.959 293.611 1.00 54.73 C ANISOU 1597 CD2 LEU A 298 7149 6593 7052 10 66 890 C ATOM 1598 N TRP A 299 23.491 28.682 291.416 1.00 76.82 N ANISOU 1598 N TRP A 299 9990 9290 9910 279 -306 547 N ATOM 1599 CA TRP A 299 22.227 28.533 290.699 1.00 76.55 C ANISOU 1599 CA TRP A 299 9868 9296 9923 343 -305 426 C ATOM 1600 C TRP A 299 22.271 29.252 289.357 1.00 71.05 C ANISOU 1600 C TRP A 299 9251 8496 9248 386 -446 422 C ATOM 1601 O TRP A 299 21.799 28.722 288.346 1.00 71.62 O ANISOU 1601 O TRP A 299 9268 8576 9368 384 -430 403 O ATOM 1602 CB TRP A 299 21.068 29.055 291.554 1.00 64.80 C ANISOU 1602 CB TRP A 299 8313 7895 8411 444 -312 254 C ATOM 1603 CG TRP A 299 19.753 29.101 290.826 1.00 75.50 C ANISOU 1603 CG TRP A 299 9570 9302 9813 534 -342 95 C ATOM 1604 CD1 TRP A 299 18.976 28.037 290.469 1.00 76.91 C ANISOU 1604 CD1 TRP A 299 9610 9575 10038 494 -224 44 C ATOM 1605 CD2 TRP A 299 19.062 30.273 290.371 1.00 93.04 C ANISOU 1605 CD2 TRP A 299 11828 11483 12039 685 -512 -44 C ATOM 1606 NE1 TRP A 299 17.846 28.472 289.817 1.00 84.62 N ANISOU 1606 NE1 TRP A 299 10515 10588 11049 611 -306 -126 N ATOM 1607 CE2 TRP A 299 17.875 29.841 289.745 1.00 90.43 C ANISOU 1607 CE2 TRP A 299 11361 11239 11759 740 -490 -183 C ATOM 1608 CE3 TRP A 299 19.331 31.644 290.431 1.00 98.73 C ANISOU 1608 CE3 TRP A 299 12694 12095 12723 781 -689 -69 C ATOM 1609 CZ2 TRP A 299 16.961 30.732 289.182 1.00 99.80 C ANISOU 1609 CZ2 TRP A 299 12545 12412 12961 905 -648 -351 C ATOM 1610 CZ3 TRP A 299 18.419 32.529 289.873 1.00 91.72 C ANISOU 1610 CZ3 TRP A 299 11825 11176 11847 943 -848 -226 C ATOM 1611 CH2 TRP A 299 17.250 32.068 289.257 1.00 97.10 C ANISOU 1611 CH2 TRP A 299 12363 11952 12581 1012 -832 -368 C ATOM 1612 N LYS A 300 22.838 30.458 289.326 1.00 73.14 N ANISOU 1612 N LYS A 300 9660 8657 9471 416 -586 443 N ATOM 1613 CA LYS A 300 22.977 31.173 288.065 1.00 65.71 C ANISOU 1613 CA LYS A 300 8837 7600 8529 434 -724 458 C ATOM 1614 C LYS A 300 23.956 30.471 287.135 1.00 62.87 C ANISOU 1614 C LYS A 300 8496 7209 8184 302 -670 599 C ATOM 1615 O LYS A 300 23.820 30.561 285.910 1.00 75.31 O ANISOU 1615 O LYS A 300 10115 8729 9769 301 -731 605 O ATOM 1616 CB LYS A 300 23.416 32.615 288.329 1.00 54.90 C ANISOU 1616 CB LYS A 300 7644 6115 7099 472 -882 455 C ATOM 1617 CG LYS A 300 22.279 33.548 288.724 1.00 65.90 C ANISOU 1617 CG LYS A 300 9054 7502 8483 643 -1000 283 C ATOM 1618 CD LYS A 300 21.329 33.778 287.556 1.00 90.53 C ANISOU 1618 CD LYS A 300 12187 10581 11630 748 -1107 191 C ATOM 1619 CE LYS A 300 20.311 34.871 287.854 1.00 94.37 C ANISOU 1619 CE LYS A 300 12715 11039 12101 941 -1267 10 C ATOM 1620 NZ LYS A 300 19.572 35.309 286.629 1.00 87.88 N ANISOU 1620 NZ LYS A 300 11964 10137 11289 1055 -1422 -68 N ATOM 1621 N ALA A 301 24.935 29.755 287.690 1.00 54.51 N ANISOU 1621 N ALA A 301 7400 6190 7121 199 -563 704 N ATOM 1622 CA ALA A 301 25.888 29.040 286.854 1.00 62.17 C ANISOU 1622 CA ALA A 301 8366 7148 8107 85 -510 816 C ATOM 1623 C ALA A 301 25.254 27.848 286.154 1.00 71.38 C ANISOU 1623 C ALA A 301 9411 8373 9337 81 -415 798 C ATOM 1624 O ALA A 301 25.752 27.424 285.106 1.00 80.85 O ANISOU 1624 O ALA A 301 10615 9552 10552 14 -403 856 O ATOM 1625 CB ALA A 301 27.080 28.577 287.690 1.00 66.37 C ANISOU 1625 CB ALA A 301 8882 7714 8621 1 -437 909 C ATOM 1626 N HIS A 302 24.173 27.303 286.702 1.00 66.47 N ANISOU 1626 N HIS A 302 8680 7829 8747 141 -344 710 N ATOM 1627 CA HIS A 302 23.467 26.203 286.063 1.00 77.18 C ANISOU 1627 CA HIS A 302 9922 9240 10162 131 -255 677 C ATOM 1628 C HIS A 302 22.321 26.664 285.173 1.00 77.85 C ANISOU 1628 C HIS A 302 9991 9320 10270 222 -339 557 C ATOM 1629 O HIS A 302 21.727 25.834 284.479 1.00 82.82 O ANISOU 1629 O HIS A 302 10527 9991 10948 213 -281 520 O ATOM 1630 CB HIS A 302 22.920 25.241 287.118 1.00 74.87 C ANISOU 1630 CB HIS A 302 9520 9042 9884 116 -115 645 C ATOM 1631 CG HIS A 302 23.979 24.481 287.853 1.00 88.87 C ANISOU 1631 CG HIS A 302 11308 10817 11640 32 -28 765 C ATOM 1632 ND1 HIS A 302 25.231 24.241 287.326 1.00 92.83 N ANISOU 1632 ND1 HIS A 302 11857 11269 12144 -31 -42 878 N ATOM 1633 CD2 HIS A 302 23.969 23.904 289.076 1.00 89.89 C ANISOU 1633 CD2 HIS A 302 11416 10997 11743 6 66 782 C ATOM 1634 CE1 HIS A 302 25.946 23.549 288.196 1.00 82.01 C ANISOU 1634 CE1 HIS A 302 10487 9915 10757 -74 27 952 C ATOM 1635 NE2 HIS A 302 25.203 23.332 289.266 1.00 87.90 N ANISOU 1635 NE2 HIS A 302 11205 10713 11481 -55 91 905 N ATOM 1636 N SER A 303 21.991 27.956 285.178 1.00 67.71 N ANISOU 1636 N SER A 303 8799 7980 8948 317 -484 489 N ATOM 1637 CA SER A 303 20.876 28.432 284.367 1.00 73.29 C ANISOU 1637 CA SER A 303 9498 8678 9671 431 -590 361 C ATOM 1638 C SER A 303 21.194 28.346 282.880 1.00 84.29 C ANISOU 1638 C SER A 303 10959 10000 11067 393 -647 421 C ATOM 1639 O SER A 303 20.330 27.979 282.076 1.00 94.46 O ANISOU 1639 O SER A 303 12176 11322 12393 444 -658 337 O ATOM 1640 CB SER A 303 20.520 29.868 284.749 1.00 78.49 C ANISOU 1640 CB SER A 303 10266 9274 10284 556 -754 274 C ATOM 1641 OG SER A 303 21.561 30.764 284.403 1.00 78.11 O ANISOU 1641 OG SER A 303 10413 9088 10176 510 -864 383 O ATOM 1642 N HIS A 304 22.422 28.694 282.493 1.00107.65 N ANISOU 1642 N HIS A 304 14053 12870 13980 298 -681 554 N ATOM 1643 CA HIS A 304 22.825 28.579 281.095 1.00114.06 C ANISOU 1643 CA HIS A 304 14933 13627 14778 236 -718 617 C ATOM 1644 C HIS A 304 23.113 27.127 280.740 1.00 96.65 C ANISOU 1644 C HIS A 304 12590 11502 12630 144 -561 666 C ATOM 1645 O HIS A 304 22.510 26.564 279.820 1.00104.21 O ANISOU 1645 O HIS A 304 13487 12486 13623 161 -550 622 O ATOM 1646 CB HIS A 304 24.063 29.438 280.814 1.00125.55 C ANISOU 1646 CB HIS A 304 16572 14976 16154 139 -793 731 C ATOM 1647 CG HIS A 304 24.049 30.771 281.495 1.00125.42 C ANISOU 1647 CG HIS A 304 16697 14874 16081 201 -922 704 C ATOM 1648 ND1 HIS A 304 24.379 30.931 282.824 1.00120.29 N ANISOU 1648 ND1 HIS A 304 16019 14256 15431 201 -880 708 N ATOM 1649 CD2 HIS A 304 23.760 32.009 281.028 1.00119.40 C ANISOU 1649 CD2 HIS A 304 16123 13987 15257 268 -1102 671 C ATOM 1650 CE1 HIS A 304 24.286 32.207 283.149 1.00116.59 C ANISOU 1650 CE1 HIS A 304 15700 13690 14908 264 -1023 673 C ATOM 1651 NE2 HIS A 304 23.912 32.883 282.077 1.00123.04 N ANISOU 1651 NE2 HIS A 304 16657 14404 15687 307 -1163 651 N ATOM 1652 N ALA A 305 24.037 26.509 281.467 1.00 83.29 N ANISOU 1652 N ALA A 305 10855 9845 10947 54 -450 753 N ATOM 1653 CA ALA A 305 24.441 25.142 281.196 1.00 74.22 C ANISOU 1653 CA ALA A 305 9598 8755 9849 -25 -316 804 C ATOM 1654 C ALA A 305 24.791 24.460 282.507 1.00 73.11 C ANISOU 1654 C ALA A 305 9388 8666 9726 -51 -206 838 C ATOM 1655 O ALA A 305 25.266 25.099 283.448 1.00100.00 O ANISOU 1655 O ALA A 305 12850 12055 13090 -48 -234 865 O ATOM 1656 CB ALA A 305 25.645 25.090 280.249 1.00 72.25 C ANISOU 1656 CB ALA A 305 9411 8471 9568 -131 -323 899 C ATOM 1657 N VAL A 306 24.516 23.168 282.571 1.00 65.67 N ANISOU 1657 N VAL A 306 8336 7778 8839 -76 -87 834 N ATOM 1658 CA VAL A 306 25.197 22.299 283.513 1.00 66.89 C ANISOU 1658 CA VAL A 306 8457 7956 9000 -126 12 903 C ATOM 1659 C VAL A 306 26.416 21.734 282.798 1.00 82.86 C ANISOU 1659 C VAL A 306 10487 9963 11032 -198 30 987 C ATOM 1660 O VAL A 306 26.481 21.707 281.568 1.00106.34 O ANISOU 1660 O VAL A 306 13461 12926 14017 -220 4 981 O ATOM 1661 CB VAL A 306 24.286 21.176 284.045 1.00 47.81 C ANISOU 1661 CB VAL A 306 5945 5592 6627 -127 130 856 C ATOM 1662 CG1 VAL A 306 22.973 21.756 284.534 1.00 58.50 C ANISOU 1662 CG1 VAL A 306 7263 6992 7974 -60 115 737 C ATOM 1663 CG2 VAL A 306 24.033 20.095 282.974 1.00 50.86 C ANISOU 1663 CG2 VAL A 306 6264 5986 7075 -163 188 845 C ATOM 1664 N ALA A1002 27.407 21.291 283.564 1.00 48.43 N ANISOU 1664 N ALA A1002 6131 5610 6661 -230 69 1057 N ATOM 1665 CA ALA A1002 28.617 20.775 282.935 1.00 66.51 C ANISOU 1665 CA ALA A1002 8409 7903 8959 -285 80 1114 C ATOM 1666 C ALA A1002 28.801 19.301 283.257 1.00 69.01 C ANISOU 1666 C ALA A1002 8666 8232 9322 -289 171 1138 C ATOM 1667 O ALA A1002 29.818 18.909 283.838 1.00 75.57 O ANISOU 1667 O ALA A1002 9503 9069 10142 -295 178 1187 O ATOM 1668 CB ALA A1002 29.837 21.583 283.379 1.00 92.79 C ANISOU 1668 CB ALA A1002 11794 11231 12231 -317 21 1161 C ATOM 1669 N LYS A1003 27.828 18.475 282.875 1.00 67.22 N ANISOU 1669 N LYS A1003 8390 8005 9146 -283 233 1097 N ATOM 1670 CA LYS A1003 27.839 17.050 283.183 1.00 66.83 C ANISOU 1670 CA LYS A1003 8311 7944 9137 -293 318 1117 C ATOM 1671 C LYS A1003 27.870 16.243 281.895 1.00 55.94 C ANISOU 1671 C LYS A1003 6878 6563 7814 -314 342 1094 C ATOM 1672 O LYS A1003 26.993 16.399 281.037 1.00 53.80 O ANISOU 1672 O LYS A1003 6572 6303 7566 -317 341 1035 O ATOM 1673 CB LYS A1003 26.614 16.649 284.004 1.00 60.92 C ANISOU 1673 CB LYS A1003 7556 7199 8393 -291 389 1082 C ATOM 1674 CG LYS A1003 26.490 17.371 285.334 1.00 65.07 C ANISOU 1674 CG LYS A1003 8130 7737 8857 -271 377 1092 C ATOM 1675 CD LYS A1003 25.247 16.931 286.098 1.00 66.06 C ANISOU 1675 CD LYS A1003 8237 7887 8977 -290 465 1041 C ATOM 1676 CE LYS A1003 25.264 15.437 286.396 1.00 72.95 C ANISOU 1676 CE LYS A1003 9128 8722 9867 -343 559 1083 C ATOM 1677 NZ LYS A1003 24.090 15.011 287.211 1.00 90.65 N ANISOU 1677 NZ LYS A1003 11365 10995 12085 -396 659 1036 N ATOM 1678 N ALA A1004 28.861 15.369 281.772 1.00 35.60 N ANISOU 1678 N ALA A1004 4292 3976 5258 -319 357 1131 N ATOM 1679 CA ALA A1004 28.962 14.487 280.622 1.00 48.93 C ANISOU 1679 CA ALA A1004 5928 5664 7000 -334 382 1102 C ATOM 1680 C ALA A1004 28.588 13.072 281.035 1.00 51.30 C ANISOU 1680 C ALA A1004 6233 5913 7346 -331 454 1107 C ATOM 1681 O ALA A1004 28.928 12.625 282.136 1.00 44.34 O ANISOU 1681 O ALA A1004 5408 4995 6445 -313 466 1156 O ATOM 1682 CB ALA A1004 30.371 14.510 280.021 1.00 33.87 C ANISOU 1682 CB ALA A1004 3997 3790 5084 -340 341 1115 C ATOM 1683 N LEU A1005 27.874 12.378 280.154 1.00 51.82 N ANISOU 1683 N LEU A1005 6255 5970 7464 -353 497 1057 N ATOM 1684 CA LEU A1005 27.523 10.981 280.361 1.00 43.91 C ANISOU 1684 CA LEU A1005 5270 4907 6507 -368 565 1056 C ATOM 1685 C LEU A1005 28.221 10.150 279.300 1.00 39.42 C ANISOU 1685 C LEU A1005 4663 4327 5987 -355 555 1034 C ATOM 1686 O LEU A1005 28.274 10.539 278.129 1.00 59.41 O ANISOU 1686 O LEU A1005 7132 6911 8531 -362 532 988 O ATOM 1687 CB LEU A1005 26.005 10.759 280.301 1.00 43.65 C ANISOU 1687 CB LEU A1005 5210 4877 6497 -417 634 996 C ATOM 1688 CG LEU A1005 25.540 9.301 280.365 1.00 40.65 C ANISOU 1688 CG LEU A1005 4855 4429 6163 -463 712 986 C ATOM 1689 CD1 LEU A1005 26.028 8.621 281.635 1.00 45.93 C ANISOU 1689 CD1 LEU A1005 5638 5018 6797 -465 731 1067 C ATOM 1690 CD2 LEU A1005 24.031 9.231 280.285 1.00 36.28 C ANISOU 1690 CD2 LEU A1005 4251 3907 5626 -528 784 907 C ATOM 1691 N ILE A1006 28.786 9.025 279.721 1.00 35.51 N ANISOU 1691 N ILE A1006 4216 3763 5514 -330 565 1062 N ATOM 1692 CA ILE A1006 29.447 8.095 278.817 1.00 52.60 C ANISOU 1692 CA ILE A1006 6346 5910 7729 -302 552 1027 C ATOM 1693 C ILE A1006 28.868 6.713 279.077 1.00 45.30 C ANISOU 1693 C ILE A1006 5489 4878 6847 -319 605 1027 C ATOM 1694 O ILE A1006 28.945 6.204 280.202 1.00 44.20 O ANISOU 1694 O ILE A1006 5456 4656 6682 -310 611 1085 O ATOM 1695 CB ILE A1006 30.976 8.094 278.993 1.00 50.67 C ANISOU 1695 CB ILE A1006 6097 5689 7468 -231 482 1043 C ATOM 1696 CG1 ILE A1006 31.530 9.482 278.670 1.00 39.06 C ANISOU 1696 CG1 ILE A1006 4566 4327 5948 -246 440 1038 C ATOM 1697 CG2 ILE A1006 31.622 7.034 278.090 1.00 44.77 C ANISOU 1697 CG2 ILE A1006 5306 4929 6776 -188 468 984 C ATOM 1698 CD1 ILE A1006 33.037 9.608 278.828 1.00 55.32 C ANISOU 1698 CD1 ILE A1006 6594 6440 7986 -195 377 1034 C ATOM 1699 N VAL A1007 28.273 6.120 278.046 1.00 57.04 N ANISOU 1699 N VAL A1007 6926 6358 8389 -352 642 962 N ATOM 1700 CA VAL A1007 27.713 4.775 278.109 1.00 52.88 C ANISOU 1700 CA VAL A1007 6464 5723 7906 -386 693 949 C ATOM 1701 C VAL A1007 28.448 3.938 277.078 1.00 45.08 C ANISOU 1701 C VAL A1007 5438 4715 6974 -333 659 895 C ATOM 1702 O VAL A1007 28.451 4.275 275.888 1.00 50.74 O ANISOU 1702 O VAL A1007 6049 5517 7713 -335 653 829 O ATOM 1703 CB VAL A1007 26.199 4.764 277.844 1.00 43.08 C ANISOU 1703 CB VAL A1007 5187 4497 6684 -484 775 898 C ATOM 1704 CG1 VAL A1007 25.632 3.374 278.102 1.00 48.11 C ANISOU 1704 CG1 VAL A1007 5913 5012 7353 -548 838 894 C ATOM 1705 CG2 VAL A1007 25.501 5.801 278.712 1.00 40.55 C ANISOU 1705 CG2 VAL A1007 4866 4235 6308 -521 800 921 C ATOM 1706 N TYR A1008 29.070 2.855 277.529 1.00 52.49 N ANISOU 1706 N TYR A1008 6474 5541 7928 -279 630 918 N ATOM 1707 CA TYR A1008 29.889 2.018 276.670 1.00 54.69 C ANISOU 1707 CA TYR A1008 6721 5799 8259 -204 582 855 C ATOM 1708 C TYR A1008 29.411 0.575 276.727 1.00 53.00 C ANISOU 1708 C TYR A1008 6620 5426 8091 -224 606 844 C ATOM 1709 O TYR A1008 28.923 0.101 277.758 1.00 48.14 O ANISOU 1709 O TYR A1008 6150 4692 7449 -270 634 912 O ATOM 1710 CB TYR A1008 31.371 2.089 277.073 1.00 52.13 C ANISOU 1710 CB TYR A1008 6400 5494 7913 -83 488 867 C ATOM 1711 CG TYR A1008 31.640 1.686 278.509 1.00 68.68 C ANISOU 1711 CG TYR A1008 8655 7471 9969 -40 450 953 C ATOM 1712 CD1 TYR A1008 31.865 0.356 278.849 1.00 63.98 C ANISOU 1712 CD1 TYR A1008 8198 6715 9397 19 410 960 C ATOM 1713 CD2 TYR A1008 31.670 2.636 279.527 1.00 66.04 C ANISOU 1713 CD2 TYR A1008 8350 7178 9566 -55 447 1028 C ATOM 1714 CE1 TYR A1008 32.110 -0.017 280.162 1.00 52.60 C ANISOU 1714 CE1 TYR A1008 6930 5153 7903 59 364 1046 C ATOM 1715 CE2 TYR A1008 31.916 2.272 280.842 1.00 59.29 C ANISOU 1715 CE2 TYR A1008 7649 6217 8661 -17 409 1108 C ATOM 1716 CZ TYR A1008 32.134 0.945 281.152 1.00 71.94 C ANISOU 1716 CZ TYR A1008 9398 7657 10279 39 367 1120 C ATOM 1717 OH TYR A1008 32.378 0.577 282.455 1.00 85.00 O ANISOU 1717 OH TYR A1008 11232 9195 11869 77 320 1206 O ATOM 1718 N GLY A1009 29.556 -0.115 275.601 1.00 43.55 N ANISOU 1718 N GLY A1009 5366 4226 6956 -198 597 756 N ATOM 1719 CA GLY A1009 29.360 -1.547 275.549 1.00 48.97 C ANISOU 1719 CA GLY A1009 6167 4750 7691 -195 596 734 C ATOM 1720 C GLY A1009 30.632 -2.218 275.075 1.00 58.33 C ANISOU 1720 C GLY A1009 7337 5914 8912 -48 498 670 C ATOM 1721 O GLY A1009 31.107 -1.936 273.970 1.00 54.96 O ANISOU 1721 O GLY A1009 6757 5614 8510 -9 484 580 O ATOM 1722 N SER A1010 31.202 -3.096 275.902 1.00 60.84 N ANISOU 1722 N SER A1010 7816 6077 9225 38 426 708 N ATOM 1723 CA SER A1010 32.494 -3.700 275.602 1.00 59.04 C ANISOU 1723 CA SER A1010 7571 5834 9027 209 311 633 C ATOM 1724 C SER A1010 32.568 -5.082 276.233 1.00 68.66 C ANISOU 1724 C SER A1010 9017 6811 10259 271 244 658 C ATOM 1725 O SER A1010 32.205 -5.247 277.401 1.00 77.65 O ANISOU 1725 O SER A1010 10342 7819 11344 227 248 770 O ATOM 1726 CB SER A1010 33.637 -2.817 276.123 1.00 65.19 C ANISOU 1726 CB SER A1010 8275 6736 9757 309 240 648 C ATOM 1727 OG SER A1010 34.898 -3.244 275.635 1.00 62.83 O ANISOU 1727 OG SER A1010 7897 6484 9491 469 138 537 O ATOM 1728 N THR A1011 33.037 -6.069 275.466 1.00 70.39 N ANISOU 1728 N THR A1011 9236 6967 10544 372 180 552 N ATOM 1729 CA THR A1011 33.270 -7.408 275.997 1.00 82.11 C ANISOU 1729 CA THR A1011 10952 8205 12040 462 84 562 C ATOM 1730 C THR A1011 34.725 -7.616 276.395 1.00 62.53 C ANISOU 1730 C THR A1011 8484 5722 9553 690 -78 517 C ATOM 1731 O THR A1011 35.006 -8.037 277.520 1.00 84.25 O ANISOU 1731 O THR A1011 11445 8311 12256 759 -165 599 O ATOM 1732 CB THR A1011 32.872 -8.497 274.983 1.00 94.91 C ANISOU 1732 CB THR A1011 12595 9726 13740 450 93 463 C ATOM 1733 OG1 THR A1011 33.953 -8.745 274.077 1.00104.85 O ANISOU 1733 OG1 THR A1011 13707 11078 15053 624 1 312 O ATOM 1734 CG2 THR A1011 31.640 -8.118 274.196 1.00 48.98 C ANISOU 1734 CG2 THR A1011 6667 3998 7946 256 243 449 C ATOM 1735 N THR A1012 35.658 -7.334 275.483 1.00 58.45 N ANISOU 1735 N THR A1012 7744 5388 9076 805 -122 377 N ATOM 1736 CA THR A1012 37.075 -7.510 275.775 1.00 70.62 C ANISOU 1736 CA THR A1012 9253 6963 10616 1027 -277 297 C ATOM 1737 C THR A1012 37.626 -6.367 276.618 1.00 78.06 C ANISOU 1737 C THR A1012 10127 8043 11487 1038 -290 364 C ATOM 1738 O THR A1012 38.557 -6.574 277.405 1.00 81.57 O ANISOU 1738 O THR A1012 10639 8447 11907 1203 -426 355 O ATOM 1739 CB THR A1012 37.866 -7.627 274.470 1.00 58.99 C ANISOU 1739 CB THR A1012 7548 5662 9206 1128 -305 101 C ATOM 1740 OG1 THR A1012 37.366 -8.730 273.708 1.00 73.07 O ANISOU 1740 OG1 THR A1012 9402 7306 11055 1128 -302 33 O ATOM 1741 CG2 THR A1012 39.358 -7.832 274.741 1.00 94.49 C ANISOU 1741 CG2 THR A1012 11980 10219 13704 1367 -468 -16 C ATOM 1742 N GLY A1013 37.070 -5.170 276.474 1.00 61.23 N ANISOU 1742 N GLY A1013 7871 6071 9323 873 -163 424 N ATOM 1743 CA GLY A1013 37.538 -4.007 277.203 1.00 51.99 C ANISOU 1743 CA GLY A1013 6631 5036 8086 865 -167 482 C ATOM 1744 C GLY A1013 38.119 -2.921 276.328 1.00 64.92 C ANISOU 1744 C GLY A1013 7999 6945 9721 834 -123 390 C ATOM 1745 O GLY A1013 38.544 -1.886 276.860 1.00 62.62 O ANISOU 1745 O GLY A1013 7641 6776 9374 815 -125 429 O ATOM 1746 N ASN A1014 38.170 -3.100 275.007 1.00 51.91 N ANISOU 1746 N ASN A1014 6203 5397 8123 818 -84 268 N ATOM 1747 CA ASN A1014 38.763 -2.078 274.155 1.00 57.48 C ANISOU 1747 CA ASN A1014 6672 6360 8807 770 -39 182 C ATOM 1748 C ASN A1014 37.930 -0.804 274.179 1.00 57.55 C ANISOU 1748 C ASN A1014 6657 6448 8762 584 73 292 C ATOM 1749 O ASN A1014 38.469 0.305 274.285 1.00 73.92 O ANISOU 1749 O ASN A1014 8625 8680 10781 544 82 297 O ATOM 1750 CB ASN A1014 38.923 -2.621 272.736 1.00 53.40 C ANISOU 1750 CB ASN A1014 6025 5924 8342 785 -18 29 C ATOM 1751 CG ASN A1014 40.011 -3.676 272.648 1.00 72.04 C ANISOU 1751 CG ASN A1014 8359 8263 10751 994 -145 -121 C ATOM 1752 OD1 ASN A1014 40.848 -3.794 273.546 1.00 69.28 O ANISOU 1752 OD1 ASN A1014 8044 7893 10387 1132 -255 -129 O ATOM 1753 ND2 ASN A1014 40.008 -4.448 271.574 1.00 72.87 N ANISOU 1753 ND2 ASN A1014 8401 8376 10910 1029 -140 -249 N ATOM 1754 N THR A1015 36.607 -0.940 274.110 1.00 54.99 N ANISOU 1754 N THR A1015 6432 6011 8450 471 153 375 N ATOM 1755 CA THR A1015 35.758 0.241 274.183 1.00 57.79 C ANISOU 1755 CA THR A1015 6771 6431 8756 318 242 467 C ATOM 1756 C THR A1015 35.657 0.776 275.608 1.00 47.67 C ANISOU 1756 C THR A1015 5601 5090 7421 311 224 592 C ATOM 1757 O THR A1015 35.413 1.972 275.792 1.00 58.07 O ANISOU 1757 O THR A1015 6877 6501 8687 224 266 647 O ATOM 1758 CB THR A1015 34.373 -0.078 273.615 1.00 59.30 C ANISOU 1758 CB THR A1015 7006 6546 8980 207 329 486 C ATOM 1759 OG1 THR A1015 34.518 -0.624 272.297 1.00 44.76 O ANISOU 1759 OG1 THR A1015 5065 4758 7185 222 338 364 O ATOM 1760 CG2 THR A1015 33.502 1.177 273.546 1.00 39.99 C ANISOU 1760 CG2 THR A1015 4524 4184 6487 71 405 552 C ATOM 1761 N GLU A1016 35.852 -0.073 276.623 1.00 61.95 N ANISOU 1761 N GLU A1016 7565 6742 9234 404 157 636 N ATOM 1762 CA GLU A1016 35.930 0.433 277.991 1.00 67.32 C ANISOU 1762 CA GLU A1016 8347 7381 9850 411 128 745 C ATOM 1763 C GLU A1016 37.183 1.272 278.190 1.00 61.07 C ANISOU 1763 C GLU A1016 7433 6749 9021 481 62 703 C ATOM 1764 O GLU A1016 37.129 2.345 278.804 1.00 59.12 O ANISOU 1764 O GLU A1016 7177 6569 8717 422 81 772 O ATOM 1765 CB GLU A1016 35.908 -0.719 278.996 1.00 67.01 C ANISOU 1765 CB GLU A1016 8525 7128 9808 494 60 802 C ATOM 1766 CG GLU A1016 36.080 -0.256 280.440 1.00 74.86 C ANISOU 1766 CG GLU A1016 9637 8083 10723 512 20 910 C ATOM 1767 CD GLU A1016 36.243 -1.398 281.411 1.00 81.28 C ANISOU 1767 CD GLU A1016 10683 8683 11515 609 -70 963 C ATOM 1768 OE1 GLU A1016 35.684 -1.301 282.524 1.00 76.04 O ANISOU 1768 OE1 GLU A1016 10185 7924 10783 547 -47 1082 O ATOM 1769 OE2 GLU A1016 36.925 -2.389 281.062 1.00 74.24 O ANISOU 1769 OE2 GLU A1016 9819 7719 10670 748 -168 883 O ATOM 1770 N TYR A1017 38.324 0.792 277.692 1.00 65.98 N ANISOU 1770 N TYR A1017 7956 7439 9676 608 -19 579 N ATOM 1771 CA TYR A1017 39.553 1.572 277.776 1.00 73.56 C ANISOU 1771 CA TYR A1017 8770 8579 10602 659 -73 511 C ATOM 1772 C TYR A1017 39.424 2.874 277.002 1.00 75.23 C ANISOU 1772 C TYR A1017 8833 8973 10779 507 19 501 C ATOM 1773 O TYR A1017 39.927 3.917 277.438 1.00 61.16 O ANISOU 1773 O TYR A1017 6996 7302 8941 470 10 520 O ATOM 1774 CB TYR A1017 40.728 0.756 277.244 1.00 78.55 C ANISOU 1774 CB TYR A1017 9296 9271 11278 818 -167 347 C ATOM 1775 CG TYR A1017 41.960 1.591 276.984 1.00 85.21 C ANISOU 1775 CG TYR A1017 9933 10354 12091 833 -194 236 C ATOM 1776 CD1 TYR A1017 42.808 1.948 278.024 1.00 90.34 C ANISOU 1776 CD1 TYR A1017 10582 11044 12700 919 -284 238 C ATOM 1777 CD2 TYR A1017 42.273 2.028 275.702 1.00 90.64 C ANISOU 1777 CD2 TYR A1017 10429 11232 12780 747 -125 123 C ATOM 1778 CE1 TYR A1017 43.937 2.715 277.797 1.00 94.63 C ANISOU 1778 CE1 TYR A1017 10926 11816 13213 914 -302 123 C ATOM 1779 CE2 TYR A1017 43.402 2.797 275.462 1.00 99.47 C ANISOU 1779 CE2 TYR A1017 11359 12578 13858 730 -135 14 C ATOM 1780 CZ TYR A1017 44.229 3.138 276.515 1.00 95.43 C ANISOU 1780 CZ TYR A1017 10838 12107 13313 810 -222 11 C ATOM 1781 OH TYR A1017 45.351 3.902 276.285 1.00 84.68 O ANISOU 1781 OH TYR A1017 9281 10982 11910 776 -227 -109 O ATOM 1782 N THR A1018 38.756 2.827 275.845 1.00 65.18 N ANISOU 1782 N THR A1018 7507 7726 9533 415 100 469 N ATOM 1783 CA THR A1018 38.538 4.035 275.055 1.00 56.03 C ANISOU 1783 CA THR A1018 6245 6715 8329 268 178 468 C ATOM 1784 C THR A1018 37.687 5.039 275.819 1.00 67.80 C ANISOU 1784 C THR A1018 7828 8162 9770 170 216 603 C ATOM 1785 O THR A1018 37.987 6.238 275.827 1.00 64.60 O ANISOU 1785 O THR A1018 7369 7871 9305 94 227 619 O ATOM 1786 CB THR A1018 37.879 3.676 273.721 1.00 53.69 C ANISOU 1786 CB THR A1018 5901 6431 8067 204 244 413 C ATOM 1787 OG1 THR A1018 38.804 2.941 272.911 1.00 54.08 O ANISOU 1787 OG1 THR A1018 5834 6563 8150 285 212 266 O ATOM 1788 CG2 THR A1018 37.437 4.929 272.961 1.00 42.29 C ANISOU 1788 CG2 THR A1018 4402 5103 6565 49 315 436 C ATOM 1789 N ALA A1019 36.621 4.570 276.468 1.00 55.06 N ANISOU 1789 N ALA A1019 6356 6388 8175 165 239 693 N ATOM 1790 CA ALA A1019 35.758 5.476 277.216 1.00 46.28 C ANISOU 1790 CA ALA A1019 5323 5245 7018 81 277 801 C ATOM 1791 C ALA A1019 36.477 6.044 278.435 1.00 69.06 C ANISOU 1791 C ALA A1019 8243 8146 9849 126 218 852 C ATOM 1792 O ALA A1019 36.340 7.233 278.745 1.00 70.24 O ANISOU 1792 O ALA A1019 8385 8359 9946 56 232 898 O ATOM 1793 CB ALA A1019 34.482 4.752 277.631 1.00 60.11 C ANISOU 1793 CB ALA A1019 7202 6840 8796 53 325 864 C ATOM 1794 N GLU A1020 37.251 5.211 279.138 1.00 76.89 N ANISOU 1794 N GLU A1020 9284 9079 10853 251 140 840 N ATOM 1795 CA GLU A1020 37.992 5.698 280.297 1.00 90.24 C ANISOU 1795 CA GLU A1020 11006 10791 12490 308 71 877 C ATOM 1796 C GLU A1020 39.032 6.736 279.896 1.00 83.50 C ANISOU 1796 C GLU A1020 9995 10126 11604 282 49 807 C ATOM 1797 O GLU A1020 39.309 7.665 280.663 1.00 81.96 O ANISOU 1797 O GLU A1020 9810 9979 11354 257 28 850 O ATOM 1798 CB GLU A1020 38.655 4.528 281.027 1.00 98.79 C ANISOU 1798 CB GLU A1020 12179 11769 13589 466 -29 863 C ATOM 1799 CG GLU A1020 37.678 3.690 281.843 1.00114.73 C ANISOU 1799 CG GLU A1020 14407 13583 15603 467 -14 966 C ATOM 1800 CD GLU A1020 38.334 2.500 282.522 1.00119.87 C ANISOU 1800 CD GLU A1020 15185 14103 16259 627 -130 959 C ATOM 1801 OE1 GLU A1020 39.194 1.847 281.892 1.00123.47 O ANISOU 1801 OE1 GLU A1020 15561 14589 16764 743 -203 846 O ATOM 1802 OE2 GLU A1020 37.989 2.219 283.690 1.00115.89 O ANISOU 1802 OE2 GLU A1020 14867 13464 15701 639 -154 1061 O ATOM 1803 N THR A1021 39.614 6.601 278.704 1.00 64.73 N ANISOU 1803 N THR A1021 7477 7864 9255 274 59 693 N ATOM 1804 CA THR A1021 40.563 7.602 278.229 1.00 62.46 C ANISOU 1804 CA THR A1021 7042 7767 8924 211 58 620 C ATOM 1805 C THR A1021 39.857 8.919 277.936 1.00 75.65 C ANISOU 1805 C THR A1021 8729 9475 10541 48 128 690 C ATOM 1806 O THR A1021 40.336 9.990 278.325 1.00 75.13 O ANISOU 1806 O THR A1021 8640 9490 10415 -11 114 704 O ATOM 1807 CB THR A1021 41.287 7.088 276.983 1.00 54.43 C ANISOU 1807 CB THR A1021 5872 6871 7938 226 65 473 C ATOM 1808 OG1 THR A1021 42.071 5.933 277.319 1.00 69.74 O ANISOU 1808 OG1 THR A1021 7790 8783 9926 402 -24 387 O ATOM 1809 CG2 THR A1021 42.208 8.157 276.394 1.00 44.95 C ANISOU 1809 CG2 THR A1021 4521 5881 6677 118 87 392 C ATOM 1810 N ILE A1022 38.715 8.855 277.248 1.00 76.22 N ANISOU 1810 N ILE A1022 8845 9482 10631 -20 195 726 N ATOM 1811 CA ILE A1022 37.920 10.052 276.991 1.00 60.52 C ANISOU 1811 CA ILE A1022 6895 7506 8594 -147 241 789 C ATOM 1812 C ILE A1022 37.426 10.647 278.300 1.00 59.21 C ANISOU 1812 C ILE A1022 6838 7261 8396 -142 223 891 C ATOM 1813 O ILE A1022 37.265 11.867 278.417 1.00 55.24 O ANISOU 1813 O ILE A1022 6357 6795 7837 -223 225 928 O ATOM 1814 CB ILE A1022 36.747 9.713 276.045 1.00 56.67 C ANISOU 1814 CB ILE A1022 6431 6963 8141 -193 300 792 C ATOM 1815 CG1 ILE A1022 37.276 9.146 274.725 1.00 56.43 C ANISOU 1815 CG1 ILE A1022 6290 7019 8133 -200 318 684 C ATOM 1816 CG2 ILE A1022 35.891 10.945 275.774 1.00 54.73 C ANISOU 1816 CG2 ILE A1022 6232 6722 7843 -299 326 845 C ATOM 1817 CD1 ILE A1022 36.213 8.530 273.853 1.00 43.59 C ANISOU 1817 CD1 ILE A1022 4681 5330 6551 -218 366 671 C ATOM 1818 N ALA A1023 37.189 9.802 279.305 1.00 57.83 N ANISOU 1818 N ALA A1023 6747 6976 8250 -49 201 934 N ATOM 1819 CA ALA A1023 36.639 10.279 280.569 1.00 62.57 C ANISOU 1819 CA ALA A1023 7456 7505 8812 -49 194 1026 C ATOM 1820 C ALA A1023 37.609 11.211 281.287 1.00 65.78 C ANISOU 1820 C ALA A1023 7840 7992 9160 -46 137 1030 C ATOM 1821 O ALA A1023 37.189 12.214 281.876 1.00 68.10 O ANISOU 1821 O ALA A1023 8187 8281 9406 -97 141 1086 O ATOM 1822 CB ALA A1023 36.280 9.090 281.460 1.00 63.99 C ANISOU 1822 CB ALA A1023 7746 7549 9018 36 185 1070 C ATOM 1823 N ARG A1024 38.909 10.902 281.253 1.00 77.89 N ANISOU 1823 N ARG A1024 9290 9607 10698 17 80 958 N ATOM 1824 CA ARG A1024 39.867 11.717 281.992 1.00 95.42 C ANISOU 1824 CA ARG A1024 11480 11912 12865 20 22 949 C ATOM 1825 C ARG A1024 40.183 13.022 281.270 1.00 90.68 C ANISOU 1825 C ARG A1024 10805 11433 12217 -118 47 918 C ATOM 1826 O ARG A1024 40.463 14.031 281.928 1.00103.48 O ANISOU 1826 O ARG A1024 12448 13087 13782 -162 21 945 O ATOM 1827 CB ARG A1024 41.155 10.925 282.260 1.00106.32 C ANISOU 1827 CB ARG A1024 12785 13349 14264 145 -58 862 C ATOM 1828 CG ARG A1024 42.076 10.716 281.057 1.00125.48 C ANISOU 1828 CG ARG A1024 15042 15919 16715 130 -54 727 C ATOM 1829 CD ARG A1024 43.419 10.125 281.497 1.00135.01 C ANISOU 1829 CD ARG A1024 16157 17208 17933 268 -151 620 C ATOM 1830 NE ARG A1024 43.542 8.696 281.207 1.00140.15 N ANISOU 1830 NE ARG A1024 16804 17795 18651 410 -190 559 N ATOM 1831 CZ ARG A1024 44.153 8.184 280.139 1.00142.18 C ANISOU 1831 CZ ARG A1024 16917 18158 18946 431 -184 423 C ATOM 1832 NH1 ARG A1024 44.711 8.974 279.230 1.00136.27 N ANISOU 1832 NH1 ARG A1024 16014 17596 18168 303 -130 335 N ATOM 1833 NH2 ARG A1024 44.205 6.869 279.976 1.00143.26 N ANISOU 1833 NH2 ARG A1024 17074 18212 19144 576 -233 371 N ATOM 1834 N GLU A1025 40.141 13.035 279.936 1.00 68.91 N ANISOU 1834 N GLU A1025 7976 8736 9472 -194 96 864 N ATOM 1835 CA GLU A1025 40.361 14.283 279.209 1.00 62.30 C ANISOU 1835 CA GLU A1025 7107 7994 8572 -345 121 848 C ATOM 1836 C GLU A1025 39.233 15.275 279.458 1.00 63.37 C ANISOU 1836 C GLU A1025 7369 8039 8671 -412 135 945 C ATOM 1837 O GLU A1025 39.474 16.483 279.554 1.00 68.28 O ANISOU 1837 O GLU A1025 8019 8697 9226 -506 119 961 O ATOM 1838 CB GLU A1025 40.498 14.012 277.713 1.00 60.53 C ANISOU 1838 CB GLU A1025 6797 7847 8355 -414 171 773 C ATOM 1839 CG GLU A1025 41.672 13.133 277.328 1.00 84.84 C ANISOU 1839 CG GLU A1025 9728 11045 11465 -354 157 647 C ATOM 1840 CD GLU A1025 42.988 13.600 277.932 1.00 92.79 C ANISOU 1840 CD GLU A1025 10644 12180 12431 -360 110 581 C ATOM 1841 OE1 GLU A1025 43.513 12.908 278.834 1.00 94.38 O ANISOU 1841 OE1 GLU A1025 10822 12370 12670 -215 44 553 O ATOM 1842 OE2 GLU A1025 43.491 14.662 277.512 1.00 78.34 O ANISOU 1842 OE2 GLU A1025 8777 10461 10529 -513 134 554 O ATOM 1843 N LEU A1026 37.993 14.790 279.539 1.00 59.96 N ANISOU 1843 N LEU A1026 7013 7491 8280 -366 162 997 N ATOM 1844 CA LEU A1026 36.875 15.669 279.863 1.00 59.56 C ANISOU 1844 CA LEU A1026 7066 7364 8200 -404 167 1066 C ATOM 1845 C LEU A1026 36.860 16.038 281.339 1.00 67.02 C ANISOU 1845 C LEU A1026 8079 8266 9119 -355 130 1119 C ATOM 1846 O LEU A1026 36.415 17.135 281.695 1.00 60.46 O ANISOU 1846 O LEU A1026 7316 7413 8242 -399 113 1154 O ATOM 1847 CB LEU A1026 35.553 15.004 279.482 1.00 56.65 C ANISOU 1847 CB LEU A1026 6732 6910 7882 -376 213 1081 C ATOM 1848 CG LEU A1026 35.382 14.606 278.016 1.00 58.58 C ANISOU 1848 CG LEU A1026 6921 7186 8152 -418 247 1029 C ATOM 1849 CD1 LEU A1026 33.967 14.108 277.767 1.00 53.64 C ANISOU 1849 CD1 LEU A1026 6331 6478 7572 -396 286 1039 C ATOM 1850 CD2 LEU A1026 35.721 15.757 277.074 1.00 49.16 C ANISOU 1850 CD2 LEU A1026 5726 6064 6889 -531 234 1011 C ATOM 1851 N ALA A1027 37.322 15.136 282.209 1.00 66.07 N ANISOU 1851 N ALA A1027 7952 8127 9023 -259 111 1123 N ATOM 1852 CA ALA A1027 37.403 15.455 283.630 1.00 71.08 C ANISOU 1852 CA ALA A1027 8657 8731 9621 -213 72 1172 C ATOM 1853 C ALA A1027 38.379 16.597 283.879 1.00 78.48 C ANISOU 1853 C ALA A1027 9565 9756 10500 -267 22 1151 C ATOM 1854 O ALA A1027 38.109 17.487 284.695 1.00 86.80 O ANISOU 1854 O ALA A1027 10688 10785 11506 -284 -1 1191 O ATOM 1855 CB ALA A1027 37.810 14.214 284.424 1.00 69.39 C ANISOU 1855 CB ALA A1027 8459 8474 9432 -97 46 1178 C ATOM 1856 N ASP A1028 39.518 16.593 283.185 1.00 69.59 N ANISOU 1856 N ASP A1028 8331 8738 9371 -303 7 1078 N ATOM 1857 CA ASP A1028 40.460 17.701 283.306 1.00 73.10 C ANISOU 1857 CA ASP A1028 8741 9278 9756 -388 -29 1046 C ATOM 1858 C ASP A1028 39.868 18.997 282.768 1.00 69.33 C ANISOU 1858 C ASP A1028 8337 8778 9229 -518 -13 1077 C ATOM 1859 O ASP A1028 40.101 20.072 283.331 1.00 93.74 O ANISOU 1859 O ASP A1028 11478 11876 12264 -573 -50 1093 O ATOM 1860 CB ASP A1028 41.756 17.371 282.572 1.00 74.51 C ANISOU 1860 CB ASP A1028 8772 9600 9940 -417 -33 940 C ATOM 1861 CG ASP A1028 42.693 16.531 283.404 1.00109.08 C ANISOU 1861 CG ASP A1028 13080 14023 14342 -284 -93 888 C ATOM 1862 OD1 ASP A1028 43.444 17.113 284.217 1.00124.11 O ANISOU 1862 OD1 ASP A1028 14966 15986 16205 -286 -147 868 O ATOM 1863 OD2 ASP A1028 42.676 15.291 283.251 1.00116.19 O ANISOU 1863 OD2 ASP A1028 13952 14893 15300 -171 -97 864 O ATOM 1864 N ALA A1029 39.101 18.915 281.687 1.00 64.46 N ANISOU 1864 N ALA A1029 7737 8127 8627 -561 31 1083 N ATOM 1865 CA ALA A1029 38.605 20.094 280.991 1.00 56.69 C ANISOU 1865 CA ALA A1029 6833 7116 7588 -677 29 1104 C ATOM 1866 C ALA A1029 37.365 20.704 281.635 1.00 56.56 C ANISOU 1866 C ALA A1029 6940 6985 7564 -636 7 1166 C ATOM 1867 O ALA A1029 36.760 21.601 281.038 1.00 56.27 O ANISOU 1867 O ALA A1029 6988 6904 7489 -700 -10 1180 O ATOM 1868 CB ALA A1029 38.306 19.749 279.531 1.00 58.90 C ANISOU 1868 CB ALA A1029 7086 7414 7880 -731 74 1077 C ATOM 1869 N GLY A1030 36.968 20.250 282.818 1.00 52.53 N ANISOU 1869 N GLY A1030 6448 6429 7082 -530 3 1195 N ATOM 1870 CA GLY A1030 35.927 20.913 283.575 1.00 65.18 C ANISOU 1870 CA GLY A1030 8149 7951 8665 -496 -17 1232 C ATOM 1871 C GLY A1030 34.551 20.290 283.515 1.00 71.40 C ANISOU 1871 C GLY A1030 8955 8674 9501 -432 27 1241 C ATOM 1872 O GLY A1030 33.582 20.942 283.920 1.00 80.89 O ANISOU 1872 O GLY A1030 10223 9826 10685 -411 11 1247 O ATOM 1873 N TYR A1031 34.430 19.059 283.033 1.00 50.73 N ANISOU 1873 N TYR A1031 6275 6059 6940 -402 79 1230 N ATOM 1874 CA TYR A1031 33.152 18.365 283.010 1.00 60.54 C ANISOU 1874 CA TYR A1031 7526 7247 8228 -357 130 1229 C ATOM 1875 C TYR A1031 33.022 17.481 284.243 1.00 59.11 C ANISOU 1875 C TYR A1031 7364 7035 8061 -292 159 1260 C ATOM 1876 O TYR A1031 34.001 16.886 284.700 1.00 61.95 O ANISOU 1876 O TYR A1031 7707 7410 8420 -259 143 1273 O ATOM 1877 CB TYR A1031 33.022 17.499 281.757 1.00 54.40 C ANISOU 1877 CB TYR A1031 6686 6479 7503 -373 170 1198 C ATOM 1878 CG TYR A1031 32.710 18.227 280.467 1.00 54.60 C ANISOU 1878 CG TYR A1031 6717 6518 7512 -435 153 1170 C ATOM 1879 CD1 TYR A1031 31.399 18.493 280.099 1.00 61.86 C ANISOU 1879 CD1 TYR A1031 7666 7396 8441 -422 155 1150 C ATOM 1880 CD2 TYR A1031 33.724 18.609 279.597 1.00 55.31 C ANISOU 1880 CD2 TYR A1031 6783 6666 7567 -509 132 1154 C ATOM 1881 CE1 TYR A1031 31.106 19.139 278.911 1.00 55.10 C ANISOU 1881 CE1 TYR A1031 6834 6542 7560 -466 122 1126 C ATOM 1882 CE2 TYR A1031 33.441 19.258 278.408 1.00 61.03 C ANISOU 1882 CE2 TYR A1031 7538 7393 8256 -577 114 1137 C ATOM 1883 CZ TYR A1031 32.129 19.518 278.070 1.00 65.66 C ANISOU 1883 CZ TYR A1031 8174 7922 8852 -547 101 1128 C ATOM 1884 OH TYR A1031 31.827 20.162 276.890 1.00 61.12 O ANISOU 1884 OH TYR A1031 7651 7339 8234 -601 65 1112 O ATOM 1885 N GLU A1032 31.808 17.397 284.779 1.00 72.66 N ANISOU 1885 N GLU A1032 9118 8710 9780 -273 197 1263 N ATOM 1886 CA GLU A1032 31.484 16.400 285.796 1.00 64.35 C ANISOU 1886 CA GLU A1032 8101 7619 8730 -238 245 1293 C ATOM 1887 C GLU A1032 31.125 15.115 285.058 1.00 75.29 C ANISOU 1887 C GLU A1032 9455 8973 10180 -242 303 1279 C ATOM 1888 O GLU A1032 29.995 14.943 284.597 1.00 85.02 O ANISOU 1888 O GLU A1032 10668 10193 11441 -268 354 1245 O ATOM 1889 CB GLU A1032 30.345 16.889 286.682 1.00 65.99 C ANISOU 1889 CB GLU A1032 8353 7817 8903 -238 274 1286 C ATOM 1890 CG GLU A1032 29.968 15.945 287.813 1.00 93.48 C ANISOU 1890 CG GLU A1032 11893 11262 12362 -230 334 1321 C ATOM 1891 CD GLU A1032 28.850 16.500 288.678 1.00109.19 C ANISOU 1891 CD GLU A1032 13910 13270 14307 -243 372 1295 C ATOM 1892 OE1 GLU A1032 28.849 17.727 288.932 1.00117.79 O ANISOU 1892 OE1 GLU A1032 15001 14392 15361 -227 319 1272 O ATOM 1893 OE2 GLU A1032 27.969 15.713 289.095 1.00105.63 O ANISOU 1893 OE2 GLU A1032 13479 12804 13852 -277 458 1289 O ATOM 1894 N VAL A1033 32.095 14.213 284.931 1.00 55.31 N ANISOU 1894 N VAL A1033 6912 6430 7672 -211 288 1292 N ATOM 1895 CA VAL A1033 31.986 13.067 284.034 1.00 55.09 C ANISOU 1895 CA VAL A1033 6850 6374 7709 -210 324 1267 C ATOM 1896 C VAL A1033 31.376 11.886 284.778 1.00 62.18 C ANISOU 1896 C VAL A1033 7825 7184 8615 -200 377 1299 C ATOM 1897 O VAL A1033 31.822 11.529 285.874 1.00 69.28 O ANISOU 1897 O VAL A1033 8806 8043 9474 -161 355 1349 O ATOM 1898 CB VAL A1033 33.362 12.698 283.455 1.00 55.92 C ANISOU 1898 CB VAL A1033 6897 6517 7834 -174 273 1244 C ATOM 1899 CG1 VAL A1033 33.262 11.484 282.543 1.00 54.82 C ANISOU 1899 CG1 VAL A1033 6723 6344 7762 -161 305 1208 C ATOM 1900 CG2 VAL A1033 33.945 13.873 282.704 1.00 56.47 C ANISOU 1900 CG2 VAL A1033 6899 6676 7879 -219 236 1212 C ATOM 1901 N ASP A1034 30.370 11.263 284.165 1.00 64.15 N ANISOU 1901 N ASP A1034 8061 7403 8911 -242 445 1270 N ATOM 1902 CA ASP A1034 29.687 10.094 284.713 1.00 59.71 C ANISOU 1902 CA ASP A1034 7579 6753 8354 -266 510 1293 C ATOM 1903 C ASP A1034 29.785 8.970 283.688 1.00 60.19 C ANISOU 1903 C ASP A1034 7614 6768 8487 -262 524 1259 C ATOM 1904 O ASP A1034 29.176 9.048 282.616 1.00 60.54 O ANISOU 1904 O ASP A1034 7577 6847 8578 -299 556 1200 O ATOM 1905 CB ASP A1034 28.232 10.430 285.034 1.00 56.41 C ANISOU 1905 CB ASP A1034 7162 6353 7919 -341 590 1268 C ATOM 1906 CG ASP A1034 27.601 9.459 286.003 1.00 76.48 C ANISOU 1906 CG ASP A1034 9813 8817 10427 -395 664 1305 C ATOM 1907 OD1 ASP A1034 27.955 8.260 285.983 1.00 99.20 O ANISOU 1907 OD1 ASP A1034 12766 11601 13324 -389 667 1336 O ATOM 1908 OD2 ASP A1034 26.739 9.908 286.789 1.00 82.66 O ANISOU 1908 OD2 ASP A1034 10614 9635 11160 -447 719 1296 O ATOM 1909 N SER A1035 30.545 7.928 284.012 1.00 54.41 N ANISOU 1909 N SER A1035 6957 5955 7761 -207 490 1290 N ATOM 1910 CA SER A1035 30.847 6.850 283.078 1.00 65.21 C ANISOU 1910 CA SER A1035 8304 7275 9197 -180 482 1249 C ATOM 1911 C SER A1035 30.156 5.578 283.554 1.00 63.21 C ANISOU 1911 C SER A1035 8183 6885 8948 -219 535 1280 C ATOM 1912 O SER A1035 30.358 5.151 284.695 1.00 58.55 O ANISOU 1912 O SER A1035 7735 6211 8302 -201 516 1348 O ATOM 1913 CB SER A1035 32.357 6.649 282.969 1.00 41.40 C ANISOU 1913 CB SER A1035 5266 4276 6189 -70 383 1236 C ATOM 1914 OG SER A1035 32.682 5.740 281.937 1.00 64.59 O ANISOU 1914 OG SER A1035 8158 7191 9194 -34 371 1174 O ATOM 1915 N ARG A1036 29.342 4.978 282.685 1.00 46.87 N ANISOU 1915 N ARG A1036 6080 4792 6937 -282 598 1229 N ATOM 1916 CA ARG A1036 28.518 3.839 283.062 1.00 49.12 C ANISOU 1916 CA ARG A1036 6489 4952 7222 -358 666 1249 C ATOM 1917 C ARG A1036 28.572 2.769 281.981 1.00 57.64 C ANISOU 1917 C ARG A1036 7552 5968 8382 -346 663 1191 C ATOM 1918 O ARG A1036 28.577 3.081 280.788 1.00 53.21 O ANISOU 1918 O ARG A1036 6848 5493 7877 -335 661 1117 O ATOM 1919 CB ARG A1036 27.056 4.253 283.288 1.00 51.61 C ANISOU 1919 CB ARG A1036 6778 5316 7517 -490 777 1229 C ATOM 1920 CG ARG A1036 26.852 5.402 284.257 1.00 45.67 C ANISOU 1920 CG ARG A1036 6020 4643 6688 -503 786 1262 C ATOM 1921 CD ARG A1036 25.368 5.665 284.464 1.00 51.28 C ANISOU 1921 CD ARG A1036 6693 5409 7383 -626 897 1214 C ATOM 1922 NE ARG A1036 25.098 6.993 285.004 1.00 62.65 N ANISOU 1922 NE ARG A1036 8072 6960 8773 -617 893 1204 N ATOM 1923 CZ ARG A1036 23.879 7.465 285.250 1.00 68.98 C ANISOU 1923 CZ ARG A1036 8815 7840 9554 -697 971 1141 C ATOM 1924 NH1 ARG A1036 22.809 6.719 285.009 1.00 79.22 N ANISOU 1924 NH1 ARG A1036 10095 9129 10875 -807 1070 1081 N ATOM 1925 NH2 ARG A1036 23.726 8.687 285.739 1.00 45.81 N ANISOU 1925 NH2 ARG A1036 5833 4999 6576 -667 949 1125 N ATOM 1926 N ASP A1037 28.606 1.509 282.406 1.00 60.45 N ANISOU 1926 N ASP A1037 8069 6163 8734 -350 659 1226 N ATOM 1927 CA ASP A1037 28.469 0.397 281.477 1.00 57.50 C ANISOU 1927 CA ASP A1037 7705 5706 8435 -356 666 1168 C ATOM 1928 C ASP A1037 27.028 0.306 280.983 1.00 68.63 C ANISOU 1928 C ASP A1037 9062 7142 9872 -509 787 1117 C ATOM 1929 O ASP A1037 26.081 0.553 281.736 1.00 69.94 O ANISOU 1929 O ASP A1037 9270 7318 9987 -625 872 1145 O ATOM 1930 CB ASP A1037 28.884 -0.909 282.158 1.00 72.23 C ANISOU 1930 CB ASP A1037 9794 7371 10280 -319 614 1224 C ATOM 1931 CG ASP A1037 28.978 -2.079 281.190 1.00 81.95 C ANISOU 1931 CG ASP A1037 11045 8501 11591 -291 591 1157 C ATOM 1932 OD1 ASP A1037 28.200 -2.123 280.211 1.00 86.34 O ANISOU 1932 OD1 ASP A1037 11488 9110 12206 -374 666 1082 O ATOM 1933 OD2 ASP A1037 29.832 -2.962 281.416 1.00 75.96 O ANISOU 1933 OD2 ASP A1037 10420 7607 10836 -177 490 1171 O ATOM 1934 N ALA A1038 26.863 -0.055 279.706 1.00 58.09 N ANISOU 1934 N ALA A1038 7623 5830 8617 -508 794 1028 N ATOM 1935 CA ALA A1038 25.526 -0.130 279.123 1.00 58.48 C ANISOU 1935 CA ALA A1038 7599 5921 8700 -640 896 959 C ATOM 1936 C ALA A1038 24.666 -1.177 279.821 1.00 59.93 C ANISOU 1936 C ALA A1038 7944 5964 8861 -778 980 986 C ATOM 1937 O ALA A1038 23.438 -1.037 279.880 1.00 59.99 O ANISOU 1937 O ALA A1038 7905 6026 8861 -919 1084 942 O ATOM 1938 CB ALA A1038 25.620 -0.434 277.625 1.00 48.60 C ANISOU 1938 CB ALA A1038 6225 4708 7532 -604 876 859 C ATOM 1939 N ALA A1039 25.287 -2.228 280.358 1.00 56.51 N ANISOU 1939 N ALA A1039 7708 5352 8411 -745 931 1049 N ATOM 1940 CA ALA A1039 24.540 -3.309 280.989 1.00 51.97 C ANISOU 1940 CA ALA A1039 7327 4617 7802 -892 1005 1083 C ATOM 1941 C ALA A1039 23.865 -2.888 282.288 1.00 69.13 C ANISOU 1941 C ALA A1039 9587 6809 9872 -1019 1090 1153 C ATOM 1942 O ALA A1039 23.043 -3.649 282.810 1.00 79.12 O ANISOU 1942 O ALA A1039 10994 7975 11093 -1189 1183 1170 O ATOM 1943 CB ALA A1039 25.468 -4.493 281.265 1.00 56.39 C ANISOU 1943 CB ALA A1039 8107 4960 8357 -802 905 1140 C ATOM 1944 N SER A1040 24.187 -1.708 282.816 1.00 78.92 N ANISOU 1944 N SER A1040 10746 8175 11065 -952 1065 1186 N ATOM 1945 CA SER A1040 23.725 -1.288 284.134 1.00 80.74 C ANISOU 1945 CA SER A1040 11067 8424 11187 -1046 1130 1253 C ATOM 1946 C SER A1040 22.804 -0.074 284.088 1.00 77.41 C ANISOU 1946 C SER A1040 10445 8208 10759 -1109 1211 1181 C ATOM 1947 O SER A1040 22.539 0.523 285.139 1.00 75.80 O ANISOU 1947 O SER A1040 10276 8057 10467 -1156 1251 1221 O ATOM 1948 CB SER A1040 24.926 -0.977 285.034 1.00 83.43 C ANISOU 1948 CB SER A1040 11519 8719 11461 -906 1017 1356 C ATOM 1949 OG SER A1040 25.679 0.111 284.517 1.00 85.48 O ANISOU 1949 OG SER A1040 11596 9119 11762 -757 935 1325 O ATOM 1950 N VAL A1041 22.314 0.314 282.911 1.00 75.58 N ANISOU 1950 N VAL A1041 10012 8092 10613 -1103 1226 1070 N ATOM 1951 CA VAL A1041 21.506 1.517 282.771 1.00 64.44 C ANISOU 1951 CA VAL A1041 8413 6870 9201 -1125 1271 989 C ATOM 1952 C VAL A1041 20.120 1.140 282.267 1.00 63.80 C ANISOU 1952 C VAL A1041 8239 6847 9157 -1277 1385 870 C ATOM 1953 O VAL A1041 19.912 0.093 281.650 1.00 53.41 O ANISOU 1953 O VAL A1041 6959 5442 7892 -1339 1412 838 O ATOM 1954 CB VAL A1041 22.162 2.550 281.829 1.00 64.81 C ANISOU 1954 CB VAL A1041 8300 7023 9300 -968 1167 956 C ATOM 1955 CG1 VAL A1041 23.550 2.917 282.333 1.00 81.32 C ANISOU 1955 CG1 VAL A1041 10468 9075 11356 -834 1060 1057 C ATOM 1956 CG2 VAL A1041 22.230 2.025 280.402 1.00 61.82 C ANISOU 1956 CG2 VAL A1041 7839 6634 9016 -938 1140 884 C ATOM 1957 N GLU A1042 19.162 2.015 282.562 1.00 73.11 N ANISOU 1957 N GLU A1042 9291 8180 10307 -1333 1448 793 N ATOM 1958 CA GLU A1042 17.817 1.952 282.011 1.00 66.02 C ANISOU 1958 CA GLU A1042 8244 7392 9448 -1448 1540 644 C ATOM 1959 C GLU A1042 17.645 3.105 281.030 1.00 60.80 C ANISOU 1959 C GLU A1042 7377 6881 8843 -1321 1463 547 C ATOM 1960 O GLU A1042 18.049 4.237 281.313 1.00 59.21 O ANISOU 1960 O GLU A1042 7140 6748 8611 -1210 1393 576 O ATOM 1961 CB GLU A1042 16.764 2.024 283.123 1.00 74.42 C ANISOU 1961 CB GLU A1042 9315 8533 10430 -1614 1673 600 C ATOM 1962 CG GLU A1042 16.802 0.848 284.090 1.00 98.59 C ANISOU 1962 CG GLU A1042 12607 11439 13415 -1776 1761 695 C ATOM 1963 CD GLU A1042 16.350 -0.451 283.448 1.00120.92 C ANISOU 1963 CD GLU A1042 15484 14166 16293 -1912 1824 651 C ATOM 1964 OE1 GLU A1042 15.268 -0.458 282.821 1.00127.66 O ANISOU 1964 OE1 GLU A1042 16168 15141 17197 -2005 1899 498 O ATOM 1965 OE2 GLU A1042 17.079 -1.461 283.563 1.00127.96 O ANISOU 1965 OE2 GLU A1042 16586 14856 17177 -1918 1791 761 O ATOM 1966 N ALA A1043 17.058 2.809 279.868 1.00 67.71 N ANISOU 1966 N ALA A1043 8133 7799 9795 -1338 1469 434 N ATOM 1967 CA ALA A1043 17.012 3.792 278.790 1.00 58.41 C ANISOU 1967 CA ALA A1043 6795 6733 8663 -1207 1375 355 C ATOM 1968 C ALA A1043 16.142 4.990 279.153 1.00 54.40 C ANISOU 1968 C ALA A1043 6159 6388 8122 -1186 1377 260 C ATOM 1969 O ALA A1043 16.489 6.133 278.833 1.00 46.67 O ANISOU 1969 O ALA A1043 5129 5468 7137 -1049 1272 262 O ATOM 1970 CB ALA A1043 16.506 3.132 277.509 1.00 42.38 C ANISOU 1970 CB ALA A1043 4676 4713 6713 -1237 1382 248 C ATOM 1971 N GLY A1044 15.013 4.753 279.815 1.00 52.22 N ANISOU 1971 N GLY A1044 5833 6187 7820 -1324 1494 166 N ATOM 1972 CA GLY A1044 14.072 5.813 280.120 1.00 43.67 C ANISOU 1972 CA GLY A1044 4605 5275 6712 -1299 1498 38 C ATOM 1973 C GLY A1044 14.675 6.998 280.848 1.00 49.76 C ANISOU 1973 C GLY A1044 5417 6066 7423 -1179 1420 114 C ATOM 1974 O GLY A1044 15.106 6.880 281.998 1.00 75.48 O ANISOU 1974 O GLY A1044 8796 9269 10612 -1227 1467 217 O ATOM 1975 N GLY A1045 14.708 8.150 280.182 1.00 51.15 N ANISOU 1975 N GLY A1045 5504 6311 7617 -1024 1296 63 N ATOM 1976 CA GLY A1045 15.221 9.366 280.790 1.00 42.60 C ANISOU 1976 CA GLY A1045 4459 5247 6481 -910 1212 119 C ATOM 1977 C GLY A1045 16.696 9.320 281.116 1.00 58.32 C ANISOU 1977 C GLY A1045 6611 7106 8443 -865 1161 309 C ATOM 1978 O GLY A1045 17.163 10.094 281.959 1.00 61.18 O ANISOU 1978 O GLY A1045 7029 7469 8746 -813 1124 372 O ATOM 1979 N LEU A1046 17.452 8.444 280.449 1.00 57.38 N ANISOU 1979 N LEU A1046 6558 6880 8366 -875 1151 388 N ATOM 1980 CA LEU A1046 18.857 8.254 280.800 1.00 44.69 C ANISOU 1980 CA LEU A1046 5090 5157 6734 -833 1106 547 C ATOM 1981 C LEU A1046 19.658 9.538 280.625 1.00 38.09 C ANISOU 1981 C LEU A1046 4257 4344 5873 -702 982 592 C ATOM 1982 O LEU A1046 20.476 9.887 281.482 1.00 59.80 O ANISOU 1982 O LEU A1046 7094 7055 8570 -671 955 690 O ATOM 1983 CB LEU A1046 19.465 7.134 279.956 1.00 46.72 C ANISOU 1983 CB LEU A1046 5391 5314 7048 -847 1104 588 C ATOM 1984 CG LEU A1046 20.887 6.702 280.324 1.00 47.48 C ANISOU 1984 CG LEU A1046 5623 5293 7126 -802 1060 728 C ATOM 1985 CD1 LEU A1046 20.918 6.130 281.738 1.00 54.88 C ANISOU 1985 CD1 LEU A1046 6693 6159 8001 -878 1130 805 C ATOM 1986 CD2 LEU A1046 21.417 5.673 279.324 1.00 42.70 C ANISOU 1986 CD2 LEU A1046 5032 4606 6584 -794 1044 732 C ATOM 1987 N PHE A1047 19.446 10.252 279.523 1.00 46.07 N ANISOU 1987 N PHE A1047 5183 5410 6913 -631 902 522 N ATOM 1988 CA PHE A1047 20.269 11.415 279.211 1.00 53.11 C ANISOU 1988 CA PHE A1047 6102 6304 7774 -530 783 571 C ATOM 1989 C PHE A1047 19.852 12.671 279.964 1.00 55.92 C ANISOU 1989 C PHE A1047 6449 6720 8076 -479 739 538 C ATOM 1990 O PHE A1047 20.492 13.713 279.789 1.00 57.52 O ANISOU 1990 O PHE A1047 6693 6916 8246 -405 638 579 O ATOM 1991 CB PHE A1047 20.233 11.712 277.704 1.00 54.09 C ANISOU 1991 CB PHE A1047 6172 6450 7930 -481 705 517 C ATOM 1992 CG PHE A1047 20.714 10.574 276.831 1.00 61.84 C ANISOU 1992 CG PHE A1047 7154 7381 8963 -517 734 537 C ATOM 1993 CD1 PHE A1047 21.427 9.509 277.358 1.00 54.40 C ANISOU 1993 CD1 PHE A1047 6279 6358 8033 -562 794 618 C ATOM 1994 CD2 PHE A1047 20.452 10.584 275.469 1.00 62.77 C ANISOU 1994 CD2 PHE A1047 7212 7527 9110 -496 691 468 C ATOM 1995 CE1 PHE A1047 21.860 8.471 276.543 1.00 56.57 C ANISOU 1995 CE1 PHE A1047 6555 6582 8357 -580 810 620 C ATOM 1996 CE2 PHE A1047 20.887 9.549 274.650 1.00 50.96 C ANISOU 1996 CE2 PHE A1047 5712 5992 7660 -525 716 474 C ATOM 1997 CZ PHE A1047 21.590 8.494 275.190 1.00 52.90 C ANISOU 1997 CZ PHE A1047 6017 6157 7924 -564 776 546 C ATOM 1998 N GLU A1048 18.806 12.615 280.783 1.00 45.95 N ANISOU 1998 N GLU A1048 5138 5520 6801 -522 814 458 N ATOM 1999 CA GLU A1048 18.381 13.808 281.497 1.00 43.21 C ANISOU 1999 CA GLU A1048 4774 5239 6405 -461 768 407 C ATOM 2000 C GLU A1048 19.464 14.247 282.475 1.00 48.99 C ANISOU 2000 C GLU A1048 5621 5916 7077 -441 741 536 C ATOM 2001 O GLU A1048 20.191 13.429 283.045 1.00 60.99 O ANISOU 2001 O GLU A1048 7220 7370 8584 -498 798 641 O ATOM 2002 CB GLU A1048 17.071 13.555 282.238 1.00 59.39 C ANISOU 2002 CB GLU A1048 6733 7388 8447 -527 872 280 C ATOM 2003 CG GLU A1048 15.895 13.247 281.324 1.00 76.32 C ANISOU 2003 CG GLU A1048 8738 9613 10648 -540 891 120 C ATOM 2004 CD GLU A1048 14.648 12.868 282.099 1.00106.11 C ANISOU 2004 CD GLU A1048 12406 13500 14409 -636 1017 -17 C ATOM 2005 OE1 GLU A1048 13.532 13.161 281.618 1.00118.63 O ANISOU 2005 OE1 GLU A1048 13847 15202 16025 -604 1001 -196 O ATOM 2006 OE2 GLU A1048 14.786 12.282 283.195 1.00116.07 O ANISOU 2006 OE2 GLU A1048 13734 14744 15625 -746 1130 48 O ATOM 2007 N GLY A1049 19.578 15.563 282.653 1.00 54.20 N ANISOU 2007 N GLY A1049 6297 6598 7699 -353 641 521 N ATOM 2008 CA GLY A1049 20.569 16.135 283.537 1.00 45.86 C ANISOU 2008 CA GLY A1049 5341 5500 6585 -329 602 626 C ATOM 2009 C GLY A1049 21.945 16.297 282.932 1.00 62.40 C ANISOU 2009 C GLY A1049 7509 7520 8679 -306 524 739 C ATOM 2010 O GLY A1049 22.772 17.023 283.501 1.00 67.55 O ANISOU 2010 O GLY A1049 8232 8149 9283 -277 467 806 O ATOM 2011 N PHE A1050 22.226 15.648 281.809 1.00 58.15 N ANISOU 2011 N PHE A1050 6950 6955 8190 -325 525 751 N ATOM 2012 CA PHE A1050 23.499 15.786 281.123 1.00 52.71 C ANISOU 2012 CA PHE A1050 6310 6220 7496 -315 460 833 C ATOM 2013 C PHE A1050 23.306 16.624 279.869 1.00 51.12 C ANISOU 2013 C PHE A1050 6097 6032 7296 -277 367 783 C ATOM 2014 O PHE A1050 22.286 16.503 279.185 1.00 69.99 O ANISOU 2014 O PHE A1050 8423 8453 9718 -264 369 691 O ATOM 2015 CB PHE A1050 24.067 14.417 280.750 1.00 54.24 C ANISOU 2015 CB PHE A1050 6499 6376 7736 -361 523 878 C ATOM 2016 CG PHE A1050 24.258 13.509 281.920 1.00 51.41 C ANISOU 2016 CG PHE A1050 6186 5980 7368 -396 601 933 C ATOM 2017 CD1 PHE A1050 23.236 12.680 282.344 1.00 46.25 C ANISOU 2017 CD1 PHE A1050 5512 5328 6731 -453 698 889 C ATOM 2018 CD2 PHE A1050 25.460 13.490 282.600 1.00 61.98 C ANISOU 2018 CD2 PHE A1050 7595 7283 8672 -378 572 1025 C ATOM 2019 CE1 PHE A1050 23.410 11.843 283.428 1.00 61.21 C ANISOU 2019 CE1 PHE A1050 7482 7174 8599 -499 766 950 C ATOM 2020 CE2 PHE A1050 25.644 12.656 283.683 1.00 59.99 C ANISOU 2020 CE2 PHE A1050 7411 6985 8400 -401 627 1080 C ATOM 2021 CZ PHE A1050 24.617 11.830 284.099 1.00 66.04 C ANISOU 2021 CZ PHE A1050 8183 7737 9173 -465 724 1050 C ATOM 2022 N ASP A1051 24.279 17.478 279.569 1.00 47.22 N ANISOU 2022 N ASP A1051 5670 5515 6758 -265 283 841 N ATOM 2023 CA ASP A1051 24.266 18.235 278.325 1.00 72.95 C ANISOU 2023 CA ASP A1051 8954 8768 9995 -250 192 815 C ATOM 2024 C ASP A1051 25.376 17.795 277.382 1.00 55.17 C ANISOU 2024 C ASP A1051 6711 6508 7743 -303 196 870 C ATOM 2025 O ASP A1051 25.607 18.446 276.357 1.00 46.43 O ANISOU 2025 O ASP A1051 5649 5396 6597 -315 126 868 O ATOM 2026 CB ASP A1051 24.355 19.735 278.615 1.00 75.14 C ANISOU 2026 CB ASP A1051 9322 9022 10204 -210 84 821 C ATOM 2027 CG ASP A1051 25.635 20.124 279.312 1.00 80.51 C ANISOU 2027 CG ASP A1051 10069 9682 10841 -246 72 914 C ATOM 2028 OD1 ASP A1051 26.271 19.249 279.939 1.00 64.98 O ANISOU 2028 OD1 ASP A1051 8068 7725 8895 -276 149 964 O ATOM 2029 OD2 ASP A1051 25.995 21.317 279.236 1.00 97.28 O ANISOU 2029 OD2 ASP A1051 12285 11775 12903 -242 -21 933 O ATOM 2030 N LEU A1052 26.071 16.708 277.712 1.00 36.81 N ANISOU 2030 N LEU A1052 4351 4182 5452 -335 273 913 N ATOM 2031 CA LEU A1052 26.939 16.010 276.777 1.00 46.05 C ANISOU 2031 CA LEU A1052 5495 5363 6641 -373 292 930 C ATOM 2032 C LEU A1052 26.808 14.521 277.047 1.00 49.36 C ANISOU 2032 C LEU A1052 5860 5766 7129 -376 381 923 C ATOM 2033 O LEU A1052 26.920 14.086 278.196 1.00 54.41 O ANISOU 2033 O LEU A1052 6518 6380 7775 -368 420 959 O ATOM 2034 CB LEU A1052 28.401 16.450 276.917 1.00 48.44 C ANISOU 2034 CB LEU A1052 5834 5678 6894 -404 260 992 C ATOM 2035 CG LEU A1052 29.393 15.787 275.953 1.00 45.22 C ANISOU 2035 CG LEU A1052 5380 5306 6497 -443 280 988 C ATOM 2036 CD1 LEU A1052 29.024 16.065 274.502 1.00 46.46 C ANISOU 2036 CD1 LEU A1052 5537 5483 6633 -476 255 945 C ATOM 2037 CD2 LEU A1052 30.810 16.263 276.223 1.00 45.15 C ANISOU 2037 CD2 LEU A1052 5385 5333 6437 -479 254 1027 C ATOM 2038 N VAL A1053 26.563 13.745 275.996 1.00 46.68 N ANISOU 2038 N VAL A1053 5469 5433 6832 -391 409 877 N ATOM 2039 CA VAL A1053 26.372 12.304 276.111 1.00 44.29 C ANISOU 2039 CA VAL A1053 5131 5099 6597 -400 486 862 C ATOM 2040 C VAL A1053 27.223 11.634 275.048 1.00 44.85 C ANISOU 2040 C VAL A1053 5168 5182 6690 -409 486 849 C ATOM 2041 O VAL A1053 27.117 11.970 273.864 1.00 46.24 O ANISOU 2041 O VAL A1053 5318 5398 6854 -424 457 807 O ATOM 2042 CB VAL A1053 24.890 11.920 275.945 1.00 39.89 C ANISOU 2042 CB VAL A1053 4531 4543 6082 -412 531 786 C ATOM 2043 CG1 VAL A1053 24.706 10.408 275.845 1.00 34.80 C ANISOU 2043 CG1 VAL A1053 3863 3856 5503 -443 609 765 C ATOM 2044 CG2 VAL A1053 24.062 12.480 277.093 1.00 54.32 C ANISOU 2044 CG2 VAL A1053 6375 6378 7886 -405 544 779 C ATOM 2045 N LEU A1054 28.055 10.684 275.463 1.00 34.30 N ANISOU 2045 N LEU A1054 3837 3814 5382 -395 511 877 N ATOM 2046 CA LEU A1054 28.946 9.977 274.551 1.00 46.57 C ANISOU 2046 CA LEU A1054 5347 5388 6961 -389 509 847 C ATOM 2047 C LEU A1054 28.629 8.495 274.622 1.00 47.29 C ANISOU 2047 C LEU A1054 5438 5407 7124 -376 560 822 C ATOM 2048 O LEU A1054 28.848 7.855 275.657 1.00 52.87 O ANISOU 2048 O LEU A1054 6202 6044 7844 -351 573 865 O ATOM 2049 CB LEU A1054 30.409 10.232 274.897 1.00 54.76 C ANISOU 2049 CB LEU A1054 6384 6460 7961 -367 470 880 C ATOM 2050 CG LEU A1054 30.841 11.697 274.920 1.00 57.78 C ANISOU 2050 CG LEU A1054 6784 6905 8266 -400 421 909 C ATOM 2051 CD1 LEU A1054 32.324 11.800 275.295 1.00 61.60 C ANISOU 2051 CD1 LEU A1054 7248 7437 8721 -387 392 923 C ATOM 2052 CD2 LEU A1054 30.566 12.369 273.575 1.00 53.74 C ANISOU 2052 CD2 LEU A1054 6255 6447 7717 -453 404 870 C ATOM 2053 N LEU A1055 28.132 7.950 273.520 1.00 43.50 N ANISOU 2053 N LEU A1055 4909 4935 6684 -395 582 753 N ATOM 2054 CA LEU A1055 27.772 6.544 273.444 1.00 46.50 C ANISOU 2054 CA LEU A1055 5295 5239 7133 -395 629 719 C ATOM 2055 C LEU A1055 28.881 5.804 272.707 1.00 47.51 C ANISOU 2055 C LEU A1055 5388 5377 7287 -353 606 680 C ATOM 2056 O LEU A1055 29.288 6.215 271.614 1.00 42.48 O ANISOU 2056 O LEU A1055 4684 4829 6628 -361 586 633 O ATOM 2057 CB LEU A1055 26.421 6.384 272.751 1.00 43.18 C ANISOU 2057 CB LEU A1055 4835 4825 6745 -444 668 651 C ATOM 2058 CG LEU A1055 25.293 7.209 273.385 1.00 43.57 C ANISOU 2058 CG LEU A1055 4892 4894 6768 -474 682 658 C ATOM 2059 CD1 LEU A1055 23.985 6.887 272.699 1.00 53.13 C ANISOU 2059 CD1 LEU A1055 6044 6122 8019 -516 718 565 C ATOM 2060 CD2 LEU A1055 25.179 6.953 274.885 1.00 50.13 C ANISOU 2060 CD2 LEU A1055 5799 5659 7590 -486 719 722 C ATOM 2061 N GLY A1056 29.394 4.752 273.322 1.00 54.56 N ANISOU 2061 N GLY A1056 6333 6183 8216 -305 604 694 N ATOM 2062 CA GLY A1056 30.443 3.938 272.728 1.00 43.49 C ANISOU 2062 CA GLY A1056 4894 4784 6845 -241 573 638 C ATOM 2063 C GLY A1056 29.994 2.496 272.636 1.00 51.74 C ANISOU 2063 C GLY A1056 5991 5706 7961 -230 596 602 C ATOM 2064 O GLY A1056 29.378 1.971 273.564 1.00 40.19 O ANISOU 2064 O GLY A1056 4634 4128 6511 -252 622 654 O ATOM 2065 N CYS A1057 30.298 1.857 271.509 1.00 62.60 N ANISOU 2065 N CYS A1057 7301 7108 9376 -206 590 510 N ATOM 2066 CA CYS A1057 29.875 0.479 271.310 1.00 69.12 C ANISOU 2066 CA CYS A1057 8182 7810 10272 -198 607 465 C ATOM 2067 C CYS A1057 30.762 -0.180 270.264 1.00 63.42 C ANISOU 2067 C CYS A1057 7384 7129 9584 -124 569 358 C ATOM 2068 O CYS A1057 31.101 0.433 269.251 1.00 63.82 O ANISOU 2068 O CYS A1057 7318 7324 9607 -137 570 298 O ATOM 2069 CB CYS A1057 28.401 0.415 270.891 1.00 69.58 C ANISOU 2069 CB CYS A1057 8233 7850 10353 -302 676 443 C ATOM 2070 SG CYS A1057 27.698 -1.232 270.863 1.00 74.64 S ANISOU 2070 SG CYS A1057 8968 8320 11072 -333 711 400 S ATOM 2071 N SER A1058 31.138 -1.425 270.530 1.00 59.26 N ANISOU 2071 N SER A1058 6934 6472 9109 -48 533 330 N ATOM 2072 CA SER A1058 31.926 -2.224 269.607 1.00 51.97 C ANISOU 2072 CA SER A1058 5947 5571 8228 40 491 209 C ATOM 2073 C SER A1058 31.005 -3.016 268.684 1.00 50.44 C ANISOU 2073 C SER A1058 5752 5324 8091 -17 536 137 C ATOM 2074 O SER A1058 29.842 -3.275 269.000 1.00 51.79 O ANISOU 2074 O SER A1058 6004 5395 8281 -108 588 181 O ATOM 2075 CB SER A1058 32.846 -3.172 270.377 1.00 61.05 C ANISOU 2075 CB SER A1058 7193 6597 9405 177 405 204 C ATOM 2076 OG SER A1058 32.134 -3.866 271.387 1.00 46.39 O ANISOU 2076 OG SER A1058 5525 4537 7564 150 410 292 O ATOM 2077 N THR A1059 31.543 -3.405 267.532 1.00 55.71 N ANISOU 2077 N THR A1059 6317 6068 8781 33 518 13 N ATOM 2078 CA THR A1059 30.776 -4.100 266.505 1.00 65.36 C ANISOU 2078 CA THR A1059 7518 7265 10053 -14 554 -75 C ATOM 2079 C THR A1059 31.109 -5.589 266.516 1.00 65.35 C ANISOU 2079 C THR A1059 7602 7102 10125 80 502 -147 C ATOM 2080 O THR A1059 32.278 -5.973 266.617 1.00 66.86 O ANISOU 2080 O THR A1059 7781 7298 10325 214 426 -202 O ATOM 2081 CB THR A1059 31.062 -3.514 265.120 1.00 42.48 C ANISOU 2081 CB THR A1059 4459 4565 7118 -33 571 -172 C ATOM 2082 OG1 THR A1059 30.931 -2.088 265.158 1.00 47.75 O ANISOU 2082 OG1 THR A1059 5074 5364 7704 -107 597 -100 O ATOM 2083 CG2 THR A1059 30.086 -4.050 264.107 1.00 42.69 C ANISOU 2083 CG2 THR A1059 4463 4574 7183 -97 611 -251 C ATOM 2084 N TRP A1060 30.075 -6.421 266.390 1.00 70.54 N ANISOU 2084 N TRP A1060 8346 7621 10835 9 538 -159 N ATOM 2085 CA TRP A1060 30.215 -7.871 266.510 1.00 70.61 C ANISOU 2085 CA TRP A1060 8485 7433 10912 78 487 -211 C ATOM 2086 C TRP A1060 29.436 -8.571 265.403 1.00 84.23 C ANISOU 2086 C TRP A1060 10176 9136 12690 14 526 -320 C ATOM 2087 O TRP A1060 28.713 -9.541 265.634 1.00101.80 O ANISOU 2087 O TRP A1060 12539 11176 14964 -43 540 -318 O ATOM 2088 CB TRP A1060 29.766 -8.333 267.895 1.00 60.44 C ANISOU 2088 CB TRP A1060 7409 5932 9622 39 484 -86 C ATOM 2089 CG TRP A1060 30.660 -7.795 268.947 1.00 62.63 C ANISOU 2089 CG TRP A1060 7726 6221 9849 128 425 3 C ATOM 2090 CD1 TRP A1060 30.575 -6.575 269.548 1.00 66.40 C ANISOU 2090 CD1 TRP A1060 8156 6812 10261 75 462 101 C ATOM 2091 CD2 TRP A1060 31.809 -8.441 269.504 1.00 61.80 C ANISOU 2091 CD2 TRP A1060 7712 6016 9752 299 307 -12 C ATOM 2092 NE1 TRP A1060 31.598 -6.424 270.455 1.00 90.17 N ANISOU 2092 NE1 TRP A1060 11219 9803 13239 191 382 152 N ATOM 2093 CE2 TRP A1060 32.369 -7.558 270.448 1.00 76.10 C ANISOU 2093 CE2 TRP A1060 9520 7895 11501 335 282 82 C ATOM 2094 CE3 TRP A1060 32.415 -9.682 269.300 1.00 49.90 C ANISOU 2094 CE3 TRP A1060 6292 4366 8300 437 208 -105 C ATOM 2095 CZ2 TRP A1060 33.505 -7.879 271.189 1.00 78.59 C ANISOU 2095 CZ2 TRP A1060 9907 8147 11805 502 163 84 C ATOM 2096 CZ3 TRP A1060 33.539 -10.000 270.036 1.00 68.05 C ANISOU 2096 CZ3 TRP A1060 8670 6597 10589 614 82 -105 C ATOM 2097 CH2 TRP A1060 34.074 -9.103 270.968 1.00 84.46 C ANISOU 2097 CH2 TRP A1060 10734 8755 12603 645 60 -12 C ATOM 2098 N GLY A1061 29.597 -8.098 264.170 1.00 80.17 N ANISOU 2098 N GLY A1061 9488 8811 12161 15 545 -419 N ATOM 2099 CA GLY A1061 28.943 -8.737 263.047 1.00 98.51 C ANISOU 2099 CA GLY A1061 11767 11132 14529 -33 573 -535 C ATOM 2100 C GLY A1061 29.647 -10.011 262.623 1.00108.24 C ANISOU 2100 C GLY A1061 13039 12261 15825 92 502 -660 C ATOM 2101 O GLY A1061 30.590 -9.960 261.828 1.00117.75 O ANISOU 2101 O GLY A1061 14118 13603 17019 193 465 -772 O ATOM 2102 N ASP A1062 29.210 -11.157 263.154 1.00101.75 N ANISOU 2102 N ASP A1062 12397 11199 15065 82 480 -648 N ATOM 2103 CA ASP A1062 29.793 -12.439 262.767 1.00124.73 C ANISOU 2103 CA ASP A1062 15374 13977 18041 208 397 -772 C ATOM 2104 C ASP A1062 29.740 -12.628 261.255 1.00127.06 C ANISOU 2104 C ASP A1062 15511 14408 18357 212 416 -939 C ATOM 2105 O ASP A1062 30.771 -12.779 260.588 1.00142.68 O ANISOU 2105 O ASP A1062 17382 16492 20337 349 359 -1065 O ATOM 2106 CB ASP A1062 29.058 -13.576 263.478 1.00124.23 C ANISOU 2106 CB ASP A1062 15553 13621 18029 145 388 -723 C ATOM 2107 CG ASP A1062 29.642 -14.936 263.158 1.00126.78 C ANISOU 2107 CG ASP A1062 15982 13768 18419 283 283 -846 C ATOM 2108 OD1 ASP A1062 29.396 -15.447 262.045 1.00126.93 O ANISOU 2108 OD1 ASP A1062 15928 13818 18483 276 294 -986 O ATOM 2109 OD2 ASP A1062 30.350 -15.492 264.027 1.00124.77 O ANISOU 2109 OD2 ASP A1062 15894 13343 18170 409 181 -808 O ATOM 2110 N ASP A1063 28.533 -12.656 260.707 1.00107.95 N ANISOU 2110 N ASP A1063 13072 11992 15951 61 493 -953 N ATOM 2111 CA ASP A1063 28.305 -12.545 259.275 1.00121.30 C ANISOU 2111 CA ASP A1063 14602 13849 17639 36 525 -1089 C ATOM 2112 C ASP A1063 27.556 -11.274 258.916 1.00120.74 C ANISOU 2112 C ASP A1063 14407 13971 17499 -91 604 -1033 C ATOM 2113 O ASP A1063 27.702 -10.773 257.799 1.00124.80 O ANISOU 2113 O ASP A1063 14773 14677 17968 -90 618 -1119 O ATOM 2114 CB ASP A1063 27.511 -13.759 258.758 1.00139.40 C ANISOU 2114 CB ASP A1063 16974 15983 20010 -18 529 -1189 C ATOM 2115 CG ASP A1063 28.105 -14.357 257.487 1.00139.22 C ANISOU 2115 CG ASP A1063 16850 16037 20012 86 486 -1380 C ATOM 2116 OD1 ASP A1063 28.081 -13.672 256.440 1.00136.43 O ANISOU 2116 OD1 ASP A1063 16322 15910 19606 61 523 -1449 O ATOM 2117 OD2 ASP A1063 28.582 -15.513 257.531 1.00127.84 O ANISOU 2117 OD2 ASP A1063 15512 14426 18635 194 410 -1465 O ATOM 2118 N SER A1064 26.780 -10.731 259.853 1.00113.85 N ANISOU 2118 N SER A1064 13601 13049 16608 -196 650 -896 N ATOM 2119 CA SER A1064 25.978 -9.534 259.653 1.00102.76 C ANISOU 2119 CA SER A1064 12099 11802 15143 -303 710 -843 C ATOM 2120 C SER A1064 26.632 -8.330 260.319 1.00102.56 C ANISOU 2120 C SER A1064 12046 11882 15042 -268 701 -725 C ATOM 2121 O SER A1064 27.858 -8.186 260.293 1.00103.86 O ANISOU 2121 O SER A1064 12175 12107 15179 -159 655 -738 O ATOM 2122 CB SER A1064 24.580 -9.773 260.223 1.00109.27 C ANISOU 2122 CB SER A1064 13002 12514 16003 -447 770 -799 C ATOM 2123 OG SER A1064 24.676 -10.093 261.601 1.00101.60 O ANISOU 2123 OG SER A1064 12187 11372 15045 -457 769 -683 O ATOM 2124 N ILE A1065 25.818 -7.465 260.915 1.00101.95 N ANISOU 2124 N ILE A1065 11975 11832 14928 -361 744 -624 N ATOM 2125 CA ILE A1065 26.273 -6.301 261.660 1.00 70.31 C ANISOU 2125 CA ILE A1065 7959 7904 10851 -345 738 -505 C ATOM 2126 C ILE A1065 25.499 -6.283 262.969 1.00 66.51 C ANISOU 2126 C ILE A1065 7589 7297 10384 -420 774 -394 C ATOM 2127 O ILE A1065 24.264 -6.305 262.961 1.00 78.04 O ANISOU 2127 O ILE A1065 9047 8742 11862 -529 825 -407 O ATOM 2128 CB ILE A1065 26.042 -5.009 260.856 1.00 80.70 C ANISOU 2128 CB ILE A1065 9155 9421 12085 -382 747 -511 C ATOM 2129 CG1 ILE A1065 26.344 -3.772 261.696 1.00 73.54 C ANISOU 2129 CG1 ILE A1065 8259 8575 11108 -383 742 -384 C ATOM 2130 CG2 ILE A1065 24.607 -4.965 260.343 1.00106.73 C ANISOU 2130 CG2 ILE A1065 12420 12735 15398 -480 784 -559 C ATOM 2131 CD1 ILE A1065 26.493 -2.516 260.845 1.00 66.87 C ANISOU 2131 CD1 ILE A1065 7326 7916 10167 -400 729 -389 C ATOM 2132 N GLU A1066 26.216 -6.282 264.090 1.00 70.44 N ANISOU 2132 N GLU A1066 8180 7714 10870 -365 747 -297 N ATOM 2133 CA GLU A1066 25.568 -6.414 265.387 1.00 58.21 C ANISOU 2133 CA GLU A1066 6760 6033 9326 -439 783 -193 C ATOM 2134 C GLU A1066 26.292 -5.568 266.420 1.00 58.07 C ANISOU 2134 C GLU A1066 6773 6042 9248 -386 756 -74 C ATOM 2135 O GLU A1066 27.525 -5.534 266.453 1.00 63.13 O ANISOU 2135 O GLU A1066 7405 6708 9876 -268 692 -74 O ATOM 2136 CB GLU A1066 25.523 -7.875 265.854 1.00 60.46 C ANISOU 2136 CB GLU A1066 7209 6091 9672 -444 773 -203 C ATOM 2137 CG GLU A1066 24.391 -8.676 265.252 1.00 77.97 C ANISOU 2137 CG GLU A1066 9434 8247 11945 -561 827 -292 C ATOM 2138 CD GLU A1066 23.909 -9.760 266.183 1.00117.14 C ANISOU 2138 CD GLU A1066 14597 12976 16935 -647 853 -247 C ATOM 2139 OE1 GLU A1066 24.714 -10.658 266.516 1.00123.85 O ANISOU 2139 OE1 GLU A1066 15591 13660 17807 -556 784 -235 O ATOM 2140 OE2 GLU A1066 22.731 -9.699 266.597 1.00130.23 O ANISOU 2140 OE2 GLU A1066 16275 14620 18587 -808 939 -228 O ATOM 2141 N LEU A1067 25.512 -4.893 267.258 1.00 67.64 N ANISOU 2141 N LEU A1067 8013 7262 10426 -474 804 11 N ATOM 2142 CA LEU A1067 26.057 -4.133 268.368 1.00 63.51 C ANISOU 2142 CA LEU A1067 7536 6748 9845 -438 784 127 C ATOM 2143 C LEU A1067 26.490 -5.070 269.488 1.00 46.97 C ANISOU 2143 C LEU A1067 5622 4462 7763 -405 757 195 C ATOM 2144 O LEU A1067 25.959 -6.170 269.652 1.00 69.83 O ANISOU 2144 O LEU A1067 8632 7200 10699 -463 781 179 O ATOM 2145 CB LEU A1067 25.028 -3.145 268.921 1.00 63.57 C ANISOU 2145 CB LEU A1067 7518 6824 9810 -538 842 182 C ATOM 2146 CG LEU A1067 24.162 -2.357 267.940 1.00 62.14 C ANISOU 2146 CG LEU A1067 7197 6793 9620 -590 867 110 C ATOM 2147 CD1 LEU A1067 23.455 -1.223 268.672 1.00 50.63 C ANISOU 2147 CD1 LEU A1067 5721 5407 8111 -641 894 168 C ATOM 2148 CD2 LEU A1067 24.974 -1.815 266.776 1.00 54.99 C ANISOU 2148 CD2 LEU A1067 6187 6017 8690 -513 813 59 C ATOM 2149 N GLN A1068 27.465 -4.616 270.268 1.00 47.23 N ANISOU 2149 N GLN A1068 5690 4503 7753 -315 702 271 N ATOM 2150 CA GLN A1068 27.843 -5.326 271.479 1.00 47.58 C ANISOU 2150 CA GLN A1068 5922 4369 7787 -279 664 353 C ATOM 2151 C GLN A1068 26.604 -5.584 272.327 1.00 52.45 C ANISOU 2151 C GLN A1068 6663 4878 8387 -434 750 419 C ATOM 2152 O GLN A1068 25.751 -4.708 272.497 1.00 57.71 O ANISOU 2152 O GLN A1068 7256 5650 9022 -535 822 441 O ATOM 2153 CB GLN A1068 28.883 -4.511 272.253 1.00 59.73 C ANISOU 2153 CB GLN A1068 7455 5972 9269 -180 603 426 C ATOM 2154 CG GLN A1068 29.593 -5.262 273.361 1.00 59.20 C ANISOU 2154 CG GLN A1068 7574 5733 9186 -90 526 492 C ATOM 2155 CD GLN A1068 28.807 -5.266 274.648 1.00 64.78 C ANISOU 2155 CD GLN A1068 8446 6327 9841 -200 578 612 C ATOM 2156 OE1 GLN A1068 27.889 -4.468 274.830 1.00 52.88 O ANISOU 2156 OE1 GLN A1068 6881 4908 8304 -323 667 645 O ATOM 2157 NE2 GLN A1068 29.161 -6.166 275.551 1.00 55.33 N ANISOU 2157 NE2 GLN A1068 7462 4935 8626 -153 518 672 N ATOM 2158 N ASP A1069 26.507 -6.804 272.860 1.00 46.24 N ANISOU 2158 N ASP A1069 6073 3881 7617 -457 739 444 N ATOM 2159 CA ASP A1069 25.226 -7.289 273.363 1.00 47.05 C ANISOU 2159 CA ASP A1069 6286 3883 7710 -644 840 470 C ATOM 2160 C ASP A1069 24.695 -6.446 274.514 1.00 46.59 C ANISOU 2160 C ASP A1069 6255 3874 7573 -736 904 570 C ATOM 2161 O ASP A1069 23.476 -6.297 274.659 1.00 64.12 O ANISOU 2161 O ASP A1069 8447 6133 9782 -902 1012 553 O ATOM 2162 CB ASP A1069 25.353 -8.746 273.793 1.00 48.99 C ANISOU 2162 CB ASP A1069 6777 3869 7969 -655 804 492 C ATOM 2163 CG ASP A1069 24.012 -9.425 273.901 1.00 73.34 C ANISOU 2163 CG ASP A1069 9950 6859 11059 -872 918 476 C ATOM 2164 OD1 ASP A1069 23.403 -9.677 272.840 1.00 83.65 O ANISOU 2164 OD1 ASP A1069 11138 8218 12427 -931 960 363 O ATOM 2165 OD2 ASP A1069 23.562 -9.698 275.034 1.00 80.26 O ANISOU 2165 OD2 ASP A1069 11010 7616 11869 -994 968 570 O ATOM 2166 N ASP A1070 25.573 -5.894 275.349 1.00 48.16 N ANISOU 2166 N ASP A1070 6499 4082 7716 -634 840 659 N ATOM 2167 CA ASP A1070 25.086 -5.103 276.471 1.00 52.45 C ANISOU 2167 CA ASP A1070 7075 4673 8181 -718 899 748 C ATOM 2168 C ASP A1070 24.472 -3.789 276.022 1.00 47.75 C ANISOU 2168 C ASP A1070 6263 4298 7582 -757 954 703 C ATOM 2169 O ASP A1070 23.725 -3.174 276.790 1.00 53.52 O ANISOU 2169 O ASP A1070 6992 5084 8259 -854 1024 740 O ATOM 2170 CB ASP A1070 26.215 -4.832 277.463 1.00 63.74 C ANISOU 2170 CB ASP A1070 8608 6060 9551 -591 807 848 C ATOM 2171 CG ASP A1070 26.725 -6.101 278.121 1.00 72.06 C ANISOU 2171 CG ASP A1070 9917 6874 10588 -549 739 904 C ATOM 2172 OD1 ASP A1070 25.890 -6.975 278.439 1.00 61.24 O ANISOU 2172 OD1 ASP A1070 8706 5357 9206 -695 806 923 O ATOM 2173 OD2 ASP A1070 27.952 -6.227 278.318 1.00 71.97 O ANISOU 2173 OD2 ASP A1070 9952 6821 10572 -375 614 923 O ATOM 2174 N PHE A1071 24.755 -3.353 274.797 1.00 59.43 N ANISOU 2174 N PHE A1071 7570 5902 9110 -683 919 619 N ATOM 2175 CA PHE A1071 24.239 -2.086 274.297 1.00 59.02 C ANISOU 2175 CA PHE A1071 7338 6042 9046 -702 946 578 C ATOM 2176 C PHE A1071 22.879 -2.215 273.625 1.00 62.46 C ANISOU 2176 C PHE A1071 7683 6530 9517 -825 1028 481 C ATOM 2177 O PHE A1071 22.151 -1.219 273.534 1.00 44.54 O ANISOU 2177 O PHE A1071 5299 4396 7226 -861 1057 450 O ATOM 2178 CB PHE A1071 25.219 -1.474 273.291 1.00 47.01 C ANISOU 2178 CB PHE A1071 5691 4635 7538 -576 866 539 C ATOM 2179 CG PHE A1071 25.252 0.026 273.314 1.00 50.72 C ANISOU 2179 CG PHE A1071 6056 5260 7956 -556 852 560 C ATOM 2180 CD1 PHE A1071 24.351 0.768 272.575 1.00 47.20 C ANISOU 2180 CD1 PHE A1071 5490 4933 7511 -605 880 495 C ATOM 2181 CD2 PHE A1071 26.190 0.694 274.077 1.00 40.12 C ANISOU 2181 CD2 PHE A1071 4746 3937 6561 -484 800 641 C ATOM 2182 CE1 PHE A1071 24.388 2.159 272.599 1.00 53.38 C ANISOU 2182 CE1 PHE A1071 6206 5837 8241 -580 851 516 C ATOM 2183 CE2 PHE A1071 26.233 2.076 274.107 1.00 49.24 C ANISOU 2183 CE2 PHE A1071 5823 5219 7666 -473 782 661 C ATOM 2184 CZ PHE A1071 25.330 2.809 273.369 1.00 48.17 C ANISOU 2184 CZ PHE A1071 5588 5185 7530 -521 805 602 C ATOM 2185 N ILE A1072 22.527 -3.410 273.145 1.00 48.26 N ANISOU 2185 N ILE A1072 5935 4628 7774 -883 1056 422 N ATOM 2186 CA ILE A1072 21.304 -3.551 272.354 1.00 51.60 C ANISOU 2186 CA ILE A1072 6249 5118 8239 -991 1124 307 C ATOM 2187 C ILE A1072 20.082 -3.061 273.118 1.00 62.41 C ANISOU 2187 C ILE A1072 7589 6555 9570 -1126 1217 299 C ATOM 2188 O ILE A1072 19.306 -2.270 272.541 1.00 68.19 O ANISOU 2188 O ILE A1072 8158 7442 10308 -1140 1231 212 O ATOM 2189 CB ILE A1072 21.164 -5.014 271.873 1.00 56.21 C ANISOU 2189 CB ILE A1072 6919 5554 8884 -1046 1140 250 C ATOM 2190 CG1 ILE A1072 22.338 -5.358 270.948 1.00 61.23 C ANISOU 2190 CG1 ILE A1072 7538 6166 9559 -892 1042 223 C ATOM 2191 CG2 ILE A1072 19.838 -5.215 271.158 1.00 45.34 C ANISOU 2191 CG2 ILE A1072 5431 4247 7548 -1176 1217 124 C ATOM 2192 CD1 ILE A1072 22.323 -6.778 270.400 1.00 49.52 C ANISOU 2192 CD1 ILE A1072 6141 4533 8141 -916 1037 156 C ATOM 2193 N PRO A1073 19.841 -3.447 274.371 1.00 54.63 N ANISOU 2193 N PRO A1073 6748 5472 8538 -1224 1277 374 N ATOM 2194 CA PRO A1073 18.643 -2.950 275.071 1.00 56.16 C ANISOU 2194 CA PRO A1073 6889 5761 8690 -1361 1377 342 C ATOM 2195 C PRO A1073 18.534 -1.438 275.056 1.00 53.96 C ANISOU 2195 C PRO A1073 6458 5665 8381 -1276 1343 327 C ATOM 2196 O PRO A1073 17.432 -0.897 274.898 1.00 62.81 O ANISOU 2196 O PRO A1073 7440 6921 9503 -1340 1392 224 O ATOM 2197 CB PRO A1073 18.816 -3.503 276.490 1.00 46.17 C ANISOU 2197 CB PRO A1073 5836 4351 7354 -1446 1424 458 C ATOM 2198 CG PRO A1073 19.664 -4.719 276.309 1.00 47.46 C ANISOU 2198 CG PRO A1073 6174 4311 7547 -1406 1368 510 C ATOM 2199 CD PRO A1073 20.625 -4.364 275.217 1.00 51.18 C ANISOU 2199 CD PRO A1073 6536 4835 8074 -1216 1254 483 C ATOM 2200 N LEU A1074 19.659 -0.737 275.204 1.00 49.34 N ANISOU 2200 N LEU A1074 5894 5085 7767 -1131 1251 416 N ATOM 2201 CA LEU A1074 19.638 0.721 275.128 1.00 49.33 C ANISOU 2201 CA LEU A1074 5772 5237 7734 -1049 1204 407 C ATOM 2202 C LEU A1074 19.355 1.179 273.709 1.00 53.68 C ANISOU 2202 C LEU A1074 6169 5897 8329 -993 1156 300 C ATOM 2203 O LEU A1074 18.606 2.141 273.493 1.00 67.41 O ANISOU 2203 O LEU A1074 7791 7767 10054 -984 1147 231 O ATOM 2204 CB LEU A1074 20.971 1.294 275.609 1.00 53.09 C ANISOU 2204 CB LEU A1074 6319 5685 8167 -925 1120 525 C ATOM 2205 CG LEU A1074 21.154 2.808 275.500 1.00 63.40 C ANISOU 2205 CG LEU A1074 7531 7124 9435 -839 1057 529 C ATOM 2206 CD1 LEU A1074 20.210 3.534 276.466 1.00 39.64 C ANISOU 2206 CD1 LEU A1074 4498 4186 6377 -898 1110 516 C ATOM 2207 CD2 LEU A1074 22.616 3.172 275.756 1.00 38.75 C ANISOU 2207 CD2 LEU A1074 4471 3970 6282 -729 973 630 C ATOM 2208 N PHE A1075 19.953 0.507 272.726 1.00 55.13 N ANISOU 2208 N PHE A1075 6357 6031 8561 -949 1116 281 N ATOM 2209 CA PHE A1075 19.758 0.909 271.340 1.00 60.45 C ANISOU 2209 CA PHE A1075 6900 6806 9261 -898 1067 185 C ATOM 2210 C PHE A1075 18.306 0.727 270.920 1.00 63.04 C ANISOU 2210 C PHE A1075 7125 7204 9623 -992 1125 51 C ATOM 2211 O PHE A1075 17.755 1.552 270.181 1.00 53.79 O ANISOU 2211 O PHE A1075 5835 6157 8446 -951 1081 -31 O ATOM 2212 CB PHE A1075 20.686 0.110 270.426 1.00 53.55 C ANISOU 2212 CB PHE A1075 6052 5868 8428 -842 1025 179 C ATOM 2213 CG PHE A1075 20.505 0.419 268.972 1.00 51.97 C ANISOU 2213 CG PHE A1075 5734 5768 8243 -803 980 82 C ATOM 2214 CD1 PHE A1075 21.059 1.562 268.416 1.00 56.58 C ANISOU 2214 CD1 PHE A1075 6269 6453 8777 -717 904 100 C ATOM 2215 CD2 PHE A1075 19.775 -0.427 268.160 1.00 67.51 C ANISOU 2215 CD2 PHE A1075 7653 7728 10269 -861 1012 -29 C ATOM 2216 CE1 PHE A1075 20.891 1.852 267.074 1.00 46.54 C ANISOU 2216 CE1 PHE A1075 4914 5269 7501 -689 860 17 C ATOM 2217 CE2 PHE A1075 19.606 -0.144 266.817 1.00 64.89 C ANISOU 2217 CE2 PHE A1075 7222 7492 9942 -822 965 -121 C ATOM 2218 CZ PHE A1075 20.166 0.997 266.274 1.00 53.98 C ANISOU 2218 CZ PHE A1075 5804 6207 8500 -735 888 -94 C ATOM 2219 N ASP A1076 17.663 -0.340 271.397 1.00 58.42 N ANISOU 2219 N ASP A1076 6589 6540 9067 -1123 1218 22 N ATOM 2220 CA ASP A1076 16.286 -0.606 271.007 1.00 57.62 C ANISOU 2220 CA ASP A1076 6376 6516 9001 -1231 1283 -124 C ATOM 2221 C ASP A1076 15.304 0.370 271.634 1.00 49.69 C ANISOU 2221 C ASP A1076 5274 5649 7958 -1260 1313 -181 C ATOM 2222 O ASP A1076 14.209 0.552 271.094 1.00 75.32 O ANISOU 2222 O ASP A1076 8377 9014 11229 -1295 1327 -329 O ATOM 2223 CB ASP A1076 15.904 -2.037 271.378 1.00 51.56 C ANISOU 2223 CB ASP A1076 5704 5619 8266 -1388 1382 -139 C ATOM 2224 CG ASP A1076 16.556 -3.063 270.471 1.00 61.77 C ANISOU 2224 CG ASP A1076 7056 6797 9615 -1357 1345 -146 C ATOM 2225 OD1 ASP A1076 17.139 -2.663 269.438 1.00 70.26 O ANISOU 2225 OD1 ASP A1076 8063 7927 10706 -1229 1257 -165 O ATOM 2226 OD2 ASP A1076 16.476 -4.269 270.784 1.00 78.34 O ANISOU 2226 OD2 ASP A1076 9278 8751 11738 -1466 1404 -136 O ATOM 2227 N SER A1077 15.665 1.006 272.746 1.00 44.56 N ANISOU 2227 N SER A1077 4690 4992 7248 -1238 1315 -80 N ATOM 2228 CA SER A1077 14.790 1.970 273.401 1.00 42.96 C ANISOU 2228 CA SER A1077 4396 4923 7006 -1252 1338 -141 C ATOM 2229 C SER A1077 15.426 3.353 273.438 1.00 53.41 C ANISOU 2229 C SER A1077 5710 6300 8282 -1094 1227 -77 C ATOM 2230 O SER A1077 15.170 4.141 274.351 1.00 56.50 O ANISOU 2230 O SER A1077 6094 6750 8624 -1085 1236 -65 O ATOM 2231 CB SER A1077 14.434 1.504 274.810 1.00 53.25 C ANISOU 2231 CB SER A1077 5783 6183 8266 -1396 1458 -100 C ATOM 2232 OG SER A1077 13.595 0.360 274.762 1.00 76.89 O ANISOU 2232 OG SER A1077 8772 9151 11293 -1572 1569 -188 O ATOM 2233 N LEU A1078 16.239 3.669 272.427 1.00 46.89 N ANISOU 2233 N LEU A1078 4888 5462 7466 -979 1125 -43 N ATOM 2234 CA LEU A1078 17.008 4.905 272.461 1.00 52.98 C ANISOU 2234 CA LEU A1078 5685 6261 8185 -854 1024 35 C ATOM 2235 C LEU A1078 16.112 6.136 272.451 1.00 39.63 C ANISOU 2235 C LEU A1078 3894 4698 6464 -797 971 -57 C ATOM 2236 O LEU A1078 16.495 7.181 272.987 1.00 60.39 O ANISOU 2236 O LEU A1078 6561 7345 9041 -726 914 5 O ATOM 2237 CB LEU A1078 17.974 4.951 271.275 1.00 50.19 C ANISOU 2237 CB LEU A1078 5349 5885 7838 -771 938 69 C ATOM 2238 CG LEU A1078 19.118 5.963 271.350 1.00 40.80 C ANISOU 2238 CG LEU A1078 4221 4692 6589 -676 851 178 C ATOM 2239 CD1 LEU A1078 19.920 5.819 272.647 1.00 37.67 C ANISOU 2239 CD1 LEU A1078 3928 4218 6166 -687 885 301 C ATOM 2240 CD2 LEU A1078 20.033 5.774 270.149 1.00 62.68 C ANISOU 2240 CD2 LEU A1078 7000 7452 9363 -631 796 191 C ATOM 2241 N GLU A1079 14.928 6.043 271.842 1.00 63.88 N ANISOU 2241 N GLU A1079 6840 7862 9570 -820 980 -216 N ATOM 2242 CA GLU A1079 14.027 7.189 271.785 1.00 61.17 C ANISOU 2242 CA GLU A1079 6396 7643 9202 -742 910 -329 C ATOM 2243 C GLU A1079 13.480 7.585 273.154 1.00 57.55 C ANISOU 2243 C GLU A1079 5917 7235 8713 -781 972 -349 C ATOM 2244 O GLU A1079 12.848 8.642 273.268 1.00 69.46 O ANISOU 2244 O GLU A1079 7354 8842 10195 -695 903 -438 O ATOM 2245 CB GLU A1079 12.872 6.904 270.818 1.00 41.58 C ANISOU 2245 CB GLU A1079 3771 5258 6768 -752 899 -515 C ATOM 2246 CG GLU A1079 11.803 5.937 271.322 1.00 58.54 C ANISOU 2246 CG GLU A1079 5823 7458 8961 -905 1039 -636 C ATOM 2247 CD GLU A1079 12.196 4.474 271.191 1.00 62.16 C ANISOU 2247 CD GLU A1079 6351 7803 9465 -1037 1141 -581 C ATOM 2248 OE1 GLU A1079 13.315 4.177 270.709 1.00 64.43 O ANISOU 2248 OE1 GLU A1079 6746 7980 9755 -994 1100 -458 O ATOM 2249 OE2 GLU A1079 11.368 3.613 271.566 1.00 76.71 O ANISOU 2249 OE2 GLU A1079 8140 9670 11337 -1187 1261 -672 O ATOM 2250 N GLU A1080 13.702 6.780 274.189 1.00 46.52 N ANISOU 2250 N GLU A1080 4592 5773 7311 -902 1094 -273 N ATOM 2251 CA GLU A1080 13.247 7.111 275.532 1.00 62.53 C ANISOU 2251 CA GLU A1080 6614 7851 9293 -954 1165 -284 C ATOM 2252 C GLU A1080 14.292 7.866 276.336 1.00 41.13 C ANISOU 2252 C GLU A1080 4028 5077 6522 -879 1114 -128 C ATOM 2253 O GLU A1080 13.988 8.334 277.436 1.00 59.21 O ANISOU 2253 O GLU A1080 6318 7414 8764 -898 1153 -135 O ATOM 2254 CB GLU A1080 12.857 5.835 276.280 1.00 60.75 C ANISOU 2254 CB GLU A1080 6421 7587 9075 -1147 1329 -285 C ATOM 2255 CG GLU A1080 11.729 5.060 275.631 1.00 53.20 C ANISOU 2255 CG GLU A1080 5335 6705 8175 -1254 1400 -456 C ATOM 2256 CD GLU A1080 11.525 3.722 276.288 1.00 64.88 C ANISOU 2256 CD GLU A1080 6892 8107 9653 -1463 1557 -430 C ATOM 2257 OE1 GLU A1080 11.382 2.715 275.559 1.00 57.04 O ANISOU 2257 OE1 GLU A1080 5900 7059 8715 -1543 1592 -467 O ATOM 2258 OE2 GLU A1080 11.527 3.679 277.539 1.00 82.27 O ANISOU 2258 OE2 GLU A1080 9172 10295 11792 -1552 1642 -371 O ATOM 2259 N THR A1081 15.504 8.014 275.806 1.00 45.69 N ANISOU 2259 N THR A1081 4701 5561 7096 -799 1030 -1 N ATOM 2260 CA THR A1081 16.616 8.559 276.573 1.00 39.68 C ANISOU 2260 CA THR A1081 4061 4734 6282 -747 991 149 C ATOM 2261 C THR A1081 16.556 10.069 276.744 1.00 40.39 C ANISOU 2261 C THR A1081 4132 4890 6324 -633 887 130 C ATOM 2262 O THR A1081 17.172 10.591 277.679 1.00 47.99 O ANISOU 2262 O THR A1081 5174 5824 7236 -611 875 223 O ATOM 2263 CB THR A1081 17.942 8.199 275.903 1.00 40.75 C ANISOU 2263 CB THR A1081 4284 4769 6430 -707 938 266 C ATOM 2264 OG1 THR A1081 17.933 8.641 274.538 1.00 47.53 O ANISOU 2264 OG1 THR A1081 5086 5666 7307 -635 847 210 O ATOM 2265 CG2 THR A1081 18.170 6.701 275.955 1.00 40.34 C ANISOU 2265 CG2 THR A1081 4287 4624 6418 -803 1027 300 C ATOM 2266 N GLY A1082 15.855 10.778 275.868 1.00 49.96 N ANISOU 2266 N GLY A1082 5254 6181 7548 -555 802 12 N ATOM 2267 CA GLY A1082 15.881 12.224 275.854 1.00 38.60 C ANISOU 2267 CA GLY A1082 3829 4776 6062 -432 676 -1 C ATOM 2268 C GLY A1082 16.913 12.816 274.921 1.00 65.80 C ANISOU 2268 C GLY A1082 7364 8156 9481 -358 557 92 C ATOM 2269 O GLY A1082 17.444 13.894 275.216 1.00 49.26 O ANISOU 2269 O GLY A1082 5346 6040 7331 -291 472 153 O ATOM 2270 N ALA A1083 17.208 12.151 273.798 1.00 64.75 N ANISOU 2270 N ALA A1083 7226 7997 9381 -379 554 98 N ATOM 2271 CA ALA A1083 18.293 12.568 272.917 1.00 57.22 C ANISOU 2271 CA ALA A1083 6358 6992 8392 -340 467 189 C ATOM 2272 C ALA A1083 17.955 13.797 272.082 1.00 60.98 C ANISOU 2272 C ALA A1083 6855 7495 8818 -243 322 135 C ATOM 2273 O ALA A1083 18.872 14.514 271.666 1.00 49.01 O ANISOU 2273 O ALA A1083 5443 5937 7244 -220 242 224 O ATOM 2274 CB ALA A1083 18.680 11.418 271.983 1.00 55.62 C ANISOU 2274 CB ALA A1083 6137 6763 8234 -395 515 196 C ATOM 2275 N GLN A1084 16.678 14.057 271.817 1.00 39.81 N ANISOU 2275 N GLN A1084 4087 4885 6156 -189 280 -12 N ATOM 2276 CA GLN A1084 16.322 15.163 270.936 1.00 50.93 C ANISOU 2276 CA GLN A1084 5536 6304 7513 -80 119 -69 C ATOM 2277 C GLN A1084 16.799 16.489 271.514 1.00 55.87 C ANISOU 2277 C GLN A1084 6281 6883 8064 -16 22 2 C ATOM 2278 O GLN A1084 16.506 16.828 272.666 1.00 46.82 O ANISOU 2278 O GLN A1084 5113 5756 6920 2 47 -16 O ATOM 2279 CB GLN A1084 14.816 15.202 270.711 1.00 41.62 C ANISOU 2279 CB GLN A1084 4225 5220 6370 -14 83 -264 C ATOM 2280 CG GLN A1084 14.373 16.318 269.786 1.00 44.95 C ANISOU 2280 CG GLN A1084 4701 5644 6735 121 -106 -335 C ATOM 2281 CD GLN A1084 12.875 16.469 269.751 1.00 50.50 C ANISOU 2281 CD GLN A1084 5259 6456 7474 213 -158 -549 C ATOM 2282 OE1 GLN A1084 12.140 15.516 270.004 1.00 65.65 O ANISOU 2282 OE1 GLN A1084 7018 8461 9465 147 -40 -657 O ATOM 2283 NE2 GLN A1084 12.410 17.672 269.444 1.00 64.36 N ANISOU 2283 NE2 GLN A1084 7073 8207 9175 365 -340 -622 N ATOM 2284 N GLY A1085 17.534 17.245 270.700 1.00 53.77 N ANISOU 2284 N GLY A1085 6149 6556 7726 9 -88 79 N ATOM 2285 CA GLY A1085 18.056 18.524 271.111 1.00 52.72 C ANISOU 2285 CA GLY A1085 6155 6362 7515 54 -189 152 C ATOM 2286 C GLY A1085 19.321 18.452 271.928 1.00 56.28 C ANISOU 2286 C GLY A1085 6667 6768 7948 -30 -112 298 C ATOM 2287 O GLY A1085 19.961 19.491 272.142 1.00 59.36 O ANISOU 2287 O GLY A1085 7186 7102 8267 -18 -193 372 O ATOM 2288 N ARG A1086 19.715 17.270 272.382 1.00 39.85 N ANISOU 2288 N ARG A1086 4508 4705 5927 -113 31 337 N ATOM 2289 CA ARG A1086 20.876 17.138 273.241 1.00 49.83 C ANISOU 2289 CA ARG A1086 5821 5934 7179 -175 95 460 C ATOM 2290 C ARG A1086 22.135 16.942 272.401 1.00 58.59 C ANISOU 2290 C ARG A1086 6989 7017 8256 -239 95 550 C ATOM 2291 O ARG A1086 22.078 16.509 271.245 1.00 38.24 O ANISOU 2291 O ARG A1086 4391 4454 5683 -256 90 519 O ATOM 2292 CB ARG A1086 20.687 15.972 274.217 1.00 45.66 C ANISOU 2292 CB ARG A1086 5202 5425 6719 -223 235 456 C ATOM 2293 CG ARG A1086 21.567 16.049 275.464 1.00 49.86 C ANISOU 2293 CG ARG A1086 5788 5927 7230 -251 277 558 C ATOM 2294 CD ARG A1086 21.193 14.984 276.472 1.00 35.26 C ANISOU 2294 CD ARG A1086 3880 4088 5429 -296 401 549 C ATOM 2295 NE ARG A1086 19.755 14.949 276.737 1.00 52.24 N ANISOU 2295 NE ARG A1086 5943 6299 7606 -281 429 424 N ATOM 2296 CZ ARG A1086 19.136 15.674 277.663 1.00 37.30 C ANISOU 2296 CZ ARG A1086 4041 4445 5687 -242 416 374 C ATOM 2297 NH1 ARG A1086 19.819 16.511 278.433 1.00 66.18 N ANISOU 2297 NH1 ARG A1086 7783 8073 9291 -214 370 450 N ATOM 2298 NH2 ARG A1086 17.825 15.563 277.820 1.00 37.72 N ANISOU 2298 NH2 ARG A1086 3989 4576 5766 -234 449 235 N ATOM 2299 N LYS A1087 23.276 17.289 272.993 1.00 50.85 N ANISOU 2299 N LYS A1087 6076 6009 7237 -277 102 650 N ATOM 2300 CA LYS A1087 24.573 17.160 272.341 1.00 48.50 C ANISOU 2300 CA LYS A1087 5817 5710 6902 -348 110 722 C ATOM 2301 C LYS A1087 25.136 15.767 272.603 1.00 59.99 C ANISOU 2301 C LYS A1087 7188 7180 8426 -385 223 739 C ATOM 2302 O LYS A1087 25.296 15.363 273.761 1.00 55.77 O ANISOU 2302 O LYS A1087 6635 6630 7923 -379 277 771 O ATOM 2303 CB LYS A1087 25.519 18.243 272.848 1.00 46.52 C ANISOU 2303 CB LYS A1087 5670 5433 6574 -374 56 801 C ATOM 2304 CG LYS A1087 25.088 19.635 272.429 1.00 53.10 C ANISOU 2304 CG LYS A1087 6624 6227 7326 -343 -72 791 C ATOM 2305 CD LYS A1087 25.860 20.716 273.162 1.00 64.81 C ANISOU 2305 CD LYS A1087 8213 7671 8740 -369 -123 861 C ATOM 2306 CE LYS A1087 25.572 22.086 272.577 1.00 62.41 C ANISOU 2306 CE LYS A1087 8067 7304 8343 -353 -263 859 C ATOM 2307 NZ LYS A1087 26.008 22.163 271.154 1.00 84.83 N ANISOU 2307 NZ LYS A1087 10975 10143 11112 -431 -291 877 N ATOM 2308 N VAL A1088 25.434 15.035 271.527 1.00 55.99 N ANISOU 2308 N VAL A1088 6641 6696 7935 -418 249 716 N ATOM 2309 CA VAL A1088 25.887 13.653 271.617 1.00 34.96 C ANISOU 2309 CA VAL A1088 3906 4036 5342 -437 339 714 C ATOM 2310 C VAL A1088 27.024 13.427 270.628 1.00 47.28 C ANISOU 2310 C VAL A1088 5459 5635 6872 -483 341 722 C ATOM 2311 O VAL A1088 27.237 14.202 269.695 1.00 48.43 O ANISOU 2311 O VAL A1088 5649 5809 6943 -516 287 720 O ATOM 2312 CB VAL A1088 24.748 12.649 271.340 1.00 39.90 C ANISOU 2312 CB VAL A1088 4458 4656 6045 -424 390 634 C ATOM 2313 CG1 VAL A1088 23.640 12.806 272.353 1.00 38.69 C ANISOU 2313 CG1 VAL A1088 4293 4489 5917 -397 407 607 C ATOM 2314 CG2 VAL A1088 24.196 12.839 269.935 1.00 63.48 C ANISOU 2314 CG2 VAL A1088 7431 7677 9014 -422 343 564 C ATOM 2315 N ALA A1089 27.738 12.325 270.833 1.00 36.79 N ANISOU 2315 N ALA A1089 4077 4307 5596 -484 401 724 N ATOM 2316 CA ALA A1089 28.785 11.899 269.917 1.00 50.10 C ANISOU 2316 CA ALA A1089 5724 6047 7267 -517 414 702 C ATOM 2317 C ALA A1089 29.118 10.451 270.232 1.00 48.25 C ANISOU 2317 C ALA A1089 5430 5784 7118 -482 472 678 C ATOM 2318 O ALA A1089 29.002 10.013 271.377 1.00 57.93 O ANISOU 2318 O ALA A1089 6674 6949 8386 -447 492 713 O ATOM 2319 CB ALA A1089 30.037 12.774 270.022 1.00 45.74 C ANISOU 2319 CB ALA A1089 5202 5545 6633 -563 385 747 C ATOM 2320 N CYS A1090 29.538 9.717 269.207 1.00 50.20 N ANISOU 2320 N CYS A1090 5620 6071 7382 -492 491 616 N ATOM 2321 CA CYS A1090 29.691 8.276 269.306 1.00 52.92 C ANISOU 2321 CA CYS A1090 5922 6372 7813 -449 532 575 C ATOM 2322 C CYS A1090 31.140 7.873 269.090 1.00 54.23 C ANISOU 2322 C CYS A1090 6037 6598 7971 -430 528 546 C ATOM 2323 O CYS A1090 31.897 8.549 268.388 1.00 65.63 O ANISOU 2323 O CYS A1090 7450 8143 9344 -478 514 526 O ATOM 2324 CB CYS A1090 28.809 7.557 268.282 1.00 58.12 C ANISOU 2324 CB CYS A1090 6545 7023 8516 -459 556 498 C ATOM 2325 SG CYS A1090 27.076 8.011 268.367 1.00 70.49 S ANISOU 2325 SG CYS A1090 8136 8553 10092 -475 555 492 S ATOM 2326 N PHE A1091 31.511 6.756 269.707 1.00 55.72 N ANISOU 2326 N PHE A1091 6220 6722 8228 -363 537 535 N ATOM 2327 CA PHE A1091 32.813 6.143 269.516 1.00 57.08 C ANISOU 2327 CA PHE A1091 6329 6946 8412 -313 523 477 C ATOM 2328 C PHE A1091 32.615 4.635 269.529 1.00 54.58 C ANISOU 2328 C PHE A1091 6020 6530 8187 -243 532 428 C ATOM 2329 O PHE A1091 31.543 4.134 269.871 1.00 72.35 O ANISOU 2329 O PHE A1091 8335 8671 10485 -250 557 455 O ATOM 2330 CB PHE A1091 33.819 6.596 270.591 1.00 56.13 C ANISOU 2330 CB PHE A1091 6220 6847 8261 -279 486 524 C ATOM 2331 CG PHE A1091 33.365 6.342 272.009 1.00 52.82 C ANISOU 2331 CG PHE A1091 5897 6300 7872 -231 475 608 C ATOM 2332 CD1 PHE A1091 32.367 7.116 272.586 1.00 49.57 C ANISOU 2332 CD1 PHE A1091 5553 5845 7434 -280 490 685 C ATOM 2333 CD2 PHE A1091 33.956 5.347 272.772 1.00 51.95 C ANISOU 2333 CD2 PHE A1091 5815 6116 7806 -135 444 604 C ATOM 2334 CE1 PHE A1091 31.952 6.890 273.895 1.00 52.61 C ANISOU 2334 CE1 PHE A1091 6026 6130 7834 -251 491 756 C ATOM 2335 CE2 PHE A1091 33.551 5.119 274.081 1.00 43.54 C ANISOU 2335 CE2 PHE A1091 4861 4933 6750 -105 436 688 C ATOM 2336 CZ PHE A1091 32.547 5.893 274.642 1.00 45.04 C ANISOU 2336 CZ PHE A1091 5110 5095 6908 -172 468 764 C ATOM 2337 N GLY A1092 33.648 3.906 269.128 1.00 60.09 N ANISOU 2337 N GLY A1092 6651 7271 8908 -179 511 343 N ATOM 2338 CA GLY A1092 33.547 2.462 269.105 1.00 61.45 C ANISOU 2338 CA GLY A1092 6847 7334 9165 -101 504 288 C ATOM 2339 C GLY A1092 34.798 1.791 268.585 1.00 66.18 C ANISOU 2339 C GLY A1092 7356 8007 9784 -14 467 170 C ATOM 2340 O GLY A1092 35.546 2.374 267.793 1.00 75.20 O ANISOU 2340 O GLY A1092 8387 9315 10871 -48 475 102 O ATOM 2341 N CYS A1093 35.041 0.565 269.029 1.00 64.09 N ANISOU 2341 N CYS A1093 7143 7621 9589 97 424 137 N ATOM 2342 CA CYS A1093 36.199 -0.203 268.603 1.00 63.11 C ANISOU 2342 CA CYS A1093 6934 7552 9493 213 371 4 C ATOM 2343 C CYS A1093 35.767 -1.258 267.596 1.00 56.74 C ANISOU 2343 C CYS A1093 6114 6697 8748 230 387 -95 C ATOM 2344 O CYS A1093 34.739 -1.918 267.773 1.00 71.86 O ANISOU 2344 O CYS A1093 8141 8450 10713 209 405 -50 O ATOM 2345 CB CYS A1093 36.886 -0.867 269.801 1.00 73.14 C ANISOU 2345 CB CYS A1093 8286 8710 10795 355 282 21 C ATOM 2346 SG CYS A1093 37.682 0.280 270.969 1.00 72.96 S ANISOU 2346 SG CYS A1093 8252 8768 10699 362 245 103 S ATOM 2347 N GLY A1094 36.553 -1.404 266.534 1.00 53.98 N ANISOU 2347 N GLY A1094 5623 6497 8390 258 385 -239 N ATOM 2348 CA GLY A1094 36.255 -2.371 265.499 1.00 59.27 C ANISOU 2348 CA GLY A1094 6265 7142 9113 280 397 -353 C ATOM 2349 C GLY A1094 37.518 -2.918 264.876 1.00 68.90 C ANISOU 2349 C GLY A1094 7348 8487 10343 393 352 -532 C ATOM 2350 O GLY A1094 38.590 -2.875 265.489 1.00 65.17 O ANISOU 2350 O GLY A1094 6830 8067 9863 493 290 -570 O ATOM 2351 N ASP A1095 37.405 -3.433 263.655 1.00 61.84 N ANISOU 2351 N ASP A1095 6379 7654 9465 384 380 -657 N ATOM 2352 CA ASP A1095 38.568 -3.936 262.938 1.00 79.99 C ANISOU 2352 CA ASP A1095 8525 10099 11768 484 348 -854 C ATOM 2353 C ASP A1095 38.242 -3.910 261.454 1.00 79.67 C ANISOU 2353 C ASP A1095 8391 10187 11694 390 420 -952 C ATOM 2354 O ASP A1095 37.174 -4.374 261.044 1.00 59.57 O ANISOU 2354 O ASP A1095 5925 7522 9188 349 445 -925 O ATOM 2355 CB ASP A1095 38.929 -5.346 263.404 1.00 91.79 C ANISOU 2355 CB ASP A1095 10086 11426 13364 682 243 -938 C ATOM 2356 CG ASP A1095 40.390 -5.671 263.202 1.00 90.47 C ANISOU 2356 CG ASP A1095 9760 11416 13198 832 175 -1131 C ATOM 2357 OD1 ASP A1095 40.760 -6.028 262.065 1.00 92.31 O ANISOU 2357 OD1 ASP A1095 9856 11788 13429 847 197 -1306 O ATOM 2358 OD2 ASP A1095 41.167 -5.576 264.179 1.00 93.18 O ANISOU 2358 OD2 ASP A1095 10108 11753 13542 937 98 -1121 O ATOM 2359 N SER A1096 39.156 -3.353 260.659 1.00 71.12 N ANISOU 2359 N SER A1096 7139 9354 10530 346 457 -1070 N ATOM 2360 CA SER A1096 38.863 -3.049 259.264 1.00 62.48 C ANISOU 2360 CA SER A1096 5968 8407 9365 220 536 -1139 C ATOM 2361 C SER A1096 38.775 -4.284 258.377 1.00 71.45 C ANISOU 2361 C SER A1096 7064 9517 10568 309 521 -1303 C ATOM 2362 O SER A1096 38.310 -4.167 257.238 1.00 74.62 O ANISOU 2362 O SER A1096 7430 10003 10919 210 581 -1350 O ATOM 2363 CB SER A1096 39.923 -2.100 258.708 1.00 61.12 C ANISOU 2363 CB SER A1096 5640 8515 9069 124 588 -1220 C ATOM 2364 OG SER A1096 41.224 -2.538 259.055 1.00 85.45 O ANISOU 2364 OG SER A1096 8592 11696 12177 258 537 -1368 O ATOM 2365 N SER A1097 39.205 -5.451 258.846 1.00 76.42 N ANISOU 2365 N SER A1097 7708 10027 11302 495 434 -1395 N ATOM 2366 CA SER A1097 39.104 -6.657 258.034 1.00 79.33 C ANISOU 2366 CA SER A1097 8054 10350 11739 587 409 -1555 C ATOM 2367 C SER A1097 37.693 -7.222 257.990 1.00 79.10 C ANISOU 2367 C SER A1097 8187 10092 11776 545 417 -1461 C ATOM 2368 O SER A1097 37.470 -8.236 257.321 1.00 97.22 O ANISOU 2368 O SER A1097 10483 12323 14131 607 396 -1584 O ATOM 2369 CB SER A1097 40.075 -7.718 258.549 1.00 94.88 C ANISOU 2369 CB SER A1097 9999 12257 13795 816 293 -1697 C ATOM 2370 OG SER A1097 41.415 -7.307 258.334 1.00102.55 O ANISOU 2370 OG SER A1097 10772 13488 14706 857 292 -1847 O ATOM 2371 N TRP A1098 36.745 -6.599 258.679 1.00 92.41 N ANISOU 2371 N TRP A1098 9999 11661 13452 439 446 -1261 N ATOM 2372 CA TRP A1098 35.336 -6.927 258.545 1.00 96.10 C ANISOU 2372 CA TRP A1098 10589 11963 13963 360 474 -1182 C ATOM 2373 C TRP A1098 34.690 -5.984 257.541 1.00 95.68 C ANISOU 2373 C TRP A1098 10475 12062 13817 197 557 -1159 C ATOM 2374 O TRP A1098 35.181 -4.882 257.284 1.00 88.29 O ANISOU 2374 O TRP A1098 9460 11313 12775 119 594 -1136 O ATOM 2375 CB TRP A1098 34.621 -6.839 259.892 1.00 84.68 C ANISOU 2375 CB TRP A1098 9309 10309 12556 340 458 -997 C ATOM 2376 CG TRP A1098 34.670 -8.108 260.669 1.00 77.96 C ANISOU 2376 CG TRP A1098 8592 9223 11807 469 379 -1010 C ATOM 2377 CD1 TRP A1098 33.806 -9.156 260.575 1.00 81.95 C ANISOU 2377 CD1 TRP A1098 9215 9530 12391 465 371 -1026 C ATOM 2378 CD2 TRP A1098 35.633 -8.468 261.662 1.00 76.42 C ANISOU 2378 CD2 TRP A1098 8444 8953 11638 619 288 -1009 C ATOM 2379 NE1 TRP A1098 34.169 -10.149 261.451 1.00 78.49 N ANISOU 2379 NE1 TRP A1098 8917 8885 12020 595 280 -1025 N ATOM 2380 CE2 TRP A1098 35.290 -9.750 262.129 1.00 79.12 C ANISOU 2380 CE2 TRP A1098 8957 9036 12068 703 221 -1015 C ATOM 2381 CE3 TRP A1098 36.750 -7.832 262.200 1.00 60.25 C ANISOU 2381 CE3 TRP A1098 6318 7033 9543 688 251 -1009 C ATOM 2382 CZ2 TRP A1098 36.025 -10.406 263.110 1.00 72.58 C ANISOU 2382 CZ2 TRP A1098 8238 8062 11278 866 107 -1015 C ATOM 2383 CZ3 TRP A1098 37.479 -8.484 263.172 1.00 75.80 C ANISOU 2383 CZ3 TRP A1098 8369 8874 11556 856 141 -1020 C ATOM 2384 CH2 TRP A1098 37.115 -9.757 263.618 1.00 75.87 C ANISOU 2384 CH2 TRP A1098 8564 8616 11649 950 64 -1020 C ATOM 2385 N GLU A1099 33.573 -6.433 256.969 1.00 90.96 N ANISOU 2385 N GLU A1099 9928 11379 13256 142 580 -1168 N ATOM 2386 CA GLU A1099 32.978 -5.685 255.870 1.00 97.66 C ANISOU 2386 CA GLU A1099 10722 12370 14014 13 638 -1176 C ATOM 2387 C GLU A1099 32.526 -4.301 256.319 1.00 96.80 C ANISOU 2387 C GLU A1099 10656 12303 13822 -99 666 -1010 C ATOM 2388 O GLU A1099 32.690 -3.317 255.586 1.00 98.95 O ANISOU 2388 O GLU A1099 10874 12746 13976 -189 697 -1007 O ATOM 2389 CB GLU A1099 31.809 -6.463 255.266 1.00 97.49 C ANISOU 2389 CB GLU A1099 10746 12240 14056 -16 646 -1224 C ATOM 2390 CG GLU A1099 31.305 -5.900 253.943 1.00111.14 C ANISOU 2390 CG GLU A1099 12412 14125 15692 -118 686 -1274 C ATOM 2391 CD GLU A1099 30.965 -6.991 252.953 1.00138.91 C ANISOU 2391 CD GLU A1099 15898 17619 19262 -89 682 -1432 C ATOM 2392 OE1 GLU A1099 29.784 -7.093 252.554 1.00148.74 O ANISOU 2392 OE1 GLU A1099 17180 18810 20525 -156 693 -1426 O ATOM 2393 OE2 GLU A1099 31.882 -7.756 252.584 1.00145.81 O ANISOU 2393 OE2 GLU A1099 16705 18535 20162 6 663 -1575 O ATOM 2394 N TYR A1100 31.954 -4.205 257.511 1.00 82.18 N ANISOU 2394 N TYR A1100 8910 10294 12022 -99 652 -875 N ATOM 2395 CA TYR A1100 31.403 -2.954 258.018 1.00 76.79 C ANISOU 2395 CA TYR A1100 8275 9629 11273 -190 669 -726 C ATOM 2396 C TYR A1100 32.233 -2.525 259.225 1.00 66.40 C ANISOU 2396 C TYR A1100 6984 8296 9950 -146 647 -637 C ATOM 2397 O TYR A1100 31.908 -2.842 260.369 1.00 62.09 O ANISOU 2397 O TYR A1100 6531 7592 9469 -110 628 -551 O ATOM 2398 CB TYR A1100 29.932 -3.132 258.358 1.00 70.42 C ANISOU 2398 CB TYR A1100 7555 8678 10523 -240 680 -661 C ATOM 2399 CG TYR A1100 29.141 -3.693 257.197 1.00 80.33 C ANISOU 2399 CG TYR A1100 8778 9947 11798 -272 694 -768 C ATOM 2400 CD1 TYR A1100 28.886 -2.922 256.070 1.00 89.55 C ANISOU 2400 CD1 TYR A1100 9894 11265 12867 -340 705 -801 C ATOM 2401 CD2 TYR A1100 28.666 -4.998 257.219 1.00 83.02 C ANISOU 2401 CD2 TYR A1100 9154 10143 12247 -239 691 -839 C ATOM 2402 CE1 TYR A1100 28.169 -3.430 255.000 1.00102.92 C ANISOU 2402 CE1 TYR A1100 11558 12976 14572 -365 710 -906 C ATOM 2403 CE2 TYR A1100 27.948 -5.517 256.155 1.00 99.38 C ANISOU 2403 CE2 TYR A1100 11192 12231 14338 -272 703 -947 C ATOM 2404 CZ TYR A1100 27.702 -4.730 255.047 1.00107.31 C ANISOU 2404 CZ TYR A1100 12130 13397 15245 -330 711 -983 C ATOM 2405 OH TYR A1100 26.988 -5.246 253.987 1.00110.27 O ANISOU 2405 OH TYR A1100 12470 13793 15633 -357 714 -1095 O ATOM 2406 N PHE A1101 33.313 -1.799 258.954 1.00 45.98 N ANISOU 2406 N PHE A1101 4315 5880 7276 -159 651 -663 N ATOM 2407 CA PHE A1101 34.195 -1.331 260.014 1.00 64.69 C ANISOU 2407 CA PHE A1101 6687 8261 9629 -120 627 -597 C ATOM 2408 C PHE A1101 33.440 -0.402 260.955 1.00 62.31 C ANISOU 2408 C PHE A1101 6488 7882 9307 -184 630 -427 C ATOM 2409 O PHE A1101 32.920 0.636 260.537 1.00 52.87 O ANISOU 2409 O PHE A1101 5306 6754 8028 -287 653 -369 O ATOM 2410 CB PHE A1101 35.406 -0.628 259.401 1.00 53.39 C ANISOU 2410 CB PHE A1101 5136 7055 8093 -159 645 -671 C ATOM 2411 CG PHE A1101 36.258 0.104 260.394 1.00 57.92 C ANISOU 2411 CG PHE A1101 5702 7673 8631 -152 627 -604 C ATOM 2412 CD1 PHE A1101 36.841 -0.565 261.456 1.00 64.20 C ANISOU 2412 CD1 PHE A1101 6509 8376 9507 -18 570 -610 C ATOM 2413 CD2 PHE A1101 36.495 1.459 260.252 1.00 55.56 C ANISOU 2413 CD2 PHE A1101 5397 7502 8213 -279 657 -538 C ATOM 2414 CE1 PHE A1101 37.631 0.108 262.364 1.00 61.44 C ANISOU 2414 CE1 PHE A1101 6147 8076 9123 -7 547 -557 C ATOM 2415 CE2 PHE A1101 37.283 2.134 261.154 1.00 68.74 C ANISOU 2415 CE2 PHE A1101 7055 9214 9849 -281 640 -485 C ATOM 2416 CZ PHE A1101 37.853 1.461 262.212 1.00 62.83 C ANISOU 2416 CZ PHE A1101 6300 8388 9185 -143 586 -498 C ATOM 2417 N CYS A1102 33.377 -0.786 262.229 1.00 66.79 N ANISOU 2417 N CYS A1102 7136 8300 9940 -116 599 -351 N ATOM 2418 CA CYS A1102 32.640 -0.034 263.243 1.00 65.32 C ANISOU 2418 CA CYS A1102 7045 8031 9741 -166 604 -201 C ATOM 2419 C CYS A1102 31.223 0.292 262.774 1.00 62.52 C ANISOU 2419 C CYS A1102 6728 7647 9380 -255 637 -169 C ATOM 2420 O CYS A1102 30.737 1.413 262.920 1.00 45.03 O ANISOU 2420 O CYS A1102 4539 5471 7102 -324 643 -88 O ATOM 2421 CB CYS A1102 33.389 1.242 263.632 1.00 54.50 C ANISOU 2421 CB CYS A1102 5651 6777 8279 -204 597 -136 C ATOM 2422 SG CYS A1102 34.788 0.974 264.737 1.00 63.27 S ANISOU 2422 SG CYS A1102 6743 7886 9409 -92 545 -140 S ATOM 2423 N GLY A1103 30.548 -0.705 262.204 1.00 60.36 N ANISOU 2423 N GLY A1103 6456 7305 9174 -248 650 -244 N ATOM 2424 CA GLY A1103 29.155 -0.534 261.831 1.00 59.58 C ANISOU 2424 CA GLY A1103 6381 7176 9081 -322 675 -234 C ATOM 2425 C GLY A1103 28.251 -0.189 262.995 1.00 69.25 C ANISOU 2425 C GLY A1103 7687 8299 10326 -355 686 -125 C ATOM 2426 O GLY A1103 27.133 0.290 262.780 1.00 58.56 O ANISOU 2426 O GLY A1103 6334 6956 8958 -415 700 -116 O ATOM 2427 N ALA A1104 28.708 -0.421 264.227 1.00 65.15 N ANISOU 2427 N ALA A1104 7234 7688 9833 -312 676 -52 N ATOM 2428 CA ALA A1104 27.883 -0.118 265.392 1.00 63.00 C ANISOU 2428 CA ALA A1104 7042 7328 9569 -350 695 47 C ATOM 2429 C ALA A1104 27.749 1.386 265.600 1.00 62.29 C ANISOU 2429 C ALA A1104 6938 7334 9396 -387 685 119 C ATOM 2430 O ALA A1104 26.663 1.878 265.928 1.00 61.68 O ANISOU 2430 O ALA A1104 6881 7243 9312 -438 703 150 O ATOM 2431 CB ALA A1104 28.473 -0.778 266.637 1.00 46.99 C ANISOU 2431 CB ALA A1104 5107 5173 7576 -293 679 107 C ATOM 2432 N VAL A1105 28.841 2.136 265.423 1.00 61.10 N ANISOU 2432 N VAL A1105 6754 7284 9177 -365 655 136 N ATOM 2433 CA VAL A1105 28.765 3.582 265.603 1.00 64.12 C ANISOU 2433 CA VAL A1105 7146 7741 9475 -406 637 206 C ATOM 2434 C VAL A1105 27.975 4.215 264.466 1.00 54.02 C ANISOU 2434 C VAL A1105 5841 6538 8148 -459 631 164 C ATOM 2435 O VAL A1105 27.308 5.240 264.660 1.00 59.39 O ANISOU 2435 O VAL A1105 6553 7232 8779 -488 610 211 O ATOM 2436 CB VAL A1105 30.176 4.195 265.730 1.00 61.49 C ANISOU 2436 CB VAL A1105 6791 7496 9078 -390 611 230 C ATOM 2437 CG1 VAL A1105 30.969 3.494 266.831 1.00 74.30 C ANISOU 2437 CG1 VAL A1105 8437 9044 10749 -315 599 256 C ATOM 2438 CG2 VAL A1105 30.932 4.119 264.416 1.00 69.28 C ANISOU 2438 CG2 VAL A1105 7697 8605 10023 -406 613 137 C ATOM 2439 N ASP A1106 28.033 3.629 263.269 1.00 51.42 N ANISOU 2439 N ASP A1106 5456 6254 7825 -464 638 69 N ATOM 2440 CA ASP A1106 27.165 4.072 262.181 1.00 55.84 C ANISOU 2440 CA ASP A1106 6003 6872 8343 -505 624 20 C ATOM 2441 C ASP A1106 25.698 3.933 262.560 1.00 50.77 C ANISOU 2441 C ASP A1106 5375 6159 7757 -513 630 14 C ATOM 2442 O ASP A1106 24.904 4.861 262.371 1.00 54.30 O ANISOU 2442 O ASP A1106 5838 6638 8154 -529 594 23 O ATOM 2443 CB ASP A1106 27.457 3.265 260.917 1.00 53.71 C ANISOU 2443 CB ASP A1106 5671 6657 8081 -505 636 -91 C ATOM 2444 CG ASP A1106 28.845 3.500 260.393 1.00 79.71 C ANISOU 2444 CG ASP A1106 8928 10059 11301 -513 637 -112 C ATOM 2445 OD1 ASP A1106 29.376 4.606 260.624 1.00 92.54 O ANISOU 2445 OD1 ASP A1106 10584 11741 12837 -549 619 -41 O ATOM 2446 OD2 ASP A1106 29.409 2.587 259.756 1.00 90.35 O ANISOU 2446 OD2 ASP A1106 10213 11439 12678 -487 655 -208 O ATOM 2447 N ALA A1107 25.320 2.768 263.086 1.00 40.12 N ANISOU 2447 N ALA A1107 4024 4713 6508 -504 673 -13 N ATOM 2448 CA ALA A1107 23.924 2.524 263.428 1.00 39.90 C ANISOU 2448 CA ALA A1107 3993 4633 6532 -536 697 -41 C ATOM 2449 C ALA A1107 23.465 3.433 264.558 1.00 50.67 C ANISOU 2449 C ALA A1107 5398 5984 7872 -543 692 41 C ATOM 2450 O ALA A1107 22.322 3.907 264.555 1.00 51.14 O ANISOU 2450 O ALA A1107 5433 6070 7927 -561 683 6 O ATOM 2451 CB ALA A1107 23.732 1.059 263.811 1.00 38.77 C ANISOU 2451 CB ALA A1107 3865 4376 6489 -549 750 -78 C ATOM 2452 N ILE A1108 24.338 3.686 265.536 1.00 47.71 N ANISOU 2452 N ILE A1108 5074 5575 7477 -521 692 136 N ATOM 2453 CA ILE A1108 23.965 4.543 266.656 1.00 49.06 C ANISOU 2453 CA ILE A1108 5286 5735 7620 -526 687 211 C ATOM 2454 C ILE A1108 23.819 5.986 266.190 1.00 36.39 C ANISOU 2454 C ILE A1108 3680 4217 5929 -515 621 223 C ATOM 2455 O ILE A1108 22.848 6.669 266.535 1.00 52.49 O ANISOU 2455 O ILE A1108 5719 6270 7955 -515 603 214 O ATOM 2456 CB ILE A1108 24.991 4.402 267.798 1.00 41.64 C ANISOU 2456 CB ILE A1108 4408 4736 6678 -500 695 304 C ATOM 2457 CG1 ILE A1108 24.884 3.001 268.418 1.00 46.99 C ANISOU 2457 CG1 ILE A1108 5126 5296 7433 -511 748 299 C ATOM 2458 CG2 ILE A1108 24.782 5.486 268.870 1.00 39.18 C ANISOU 2458 CG2 ILE A1108 4138 4432 6318 -500 680 383 C ATOM 2459 CD1 ILE A1108 25.857 2.728 269.569 1.00 60.63 C ANISOU 2459 CD1 ILE A1108 6932 6949 9156 -471 741 386 C ATOM 2460 N GLU A1109 24.764 6.467 265.381 1.00 41.69 N ANISOU 2460 N GLU A1109 4356 4949 6534 -509 582 235 N ATOM 2461 CA GLU A1109 24.694 7.841 264.894 1.00 36.02 C ANISOU 2461 CA GLU A1109 3675 4293 5718 -512 511 256 C ATOM 2462 C GLU A1109 23.468 8.076 264.019 1.00 55.59 C ANISOU 2462 C GLU A1109 6133 6803 8188 -506 471 174 C ATOM 2463 O GLU A1109 22.839 9.139 264.097 1.00 50.49 O ANISOU 2463 O GLU A1109 5525 6169 7490 -484 405 183 O ATOM 2464 CB GLU A1109 25.958 8.184 264.116 1.00 51.49 C ANISOU 2464 CB GLU A1109 5649 6318 7598 -538 493 275 C ATOM 2465 CG GLU A1109 27.037 8.801 264.970 1.00 71.79 C ANISOU 2465 CG GLU A1109 8261 8891 10126 -545 488 363 C ATOM 2466 CD GLU A1109 28.293 9.108 264.176 1.00 91.61 C ANISOU 2466 CD GLU A1109 10767 11488 12554 -593 484 361 C ATOM 2467 OE1 GLU A1109 28.349 8.712 262.990 1.00 77.41 O ANISOU 2467 OE1 GLU A1109 8932 9744 10735 -616 492 290 O ATOM 2468 OE2 GLU A1109 29.216 9.748 264.733 1.00103.85 O ANISOU 2468 OE2 GLU A1109 12344 13061 14054 -615 475 420 O ATOM 2469 N GLU A1110 23.134 7.118 263.147 1.00 36.78 N ANISOU 2469 N GLU A1110 3690 4433 5852 -515 497 85 N ATOM 2470 CA GLU A1110 21.958 7.278 262.299 1.00 52.42 C ANISOU 2470 CA GLU A1110 5640 6451 7826 -502 451 -8 C ATOM 2471 C GLU A1110 20.687 7.362 263.131 1.00 56.67 C ANISOU 2471 C GLU A1110 6143 6968 8420 -485 457 -46 C ATOM 2472 O GLU A1110 19.786 8.150 262.824 1.00 73.10 O ANISOU 2472 O GLU A1110 8221 9089 10465 -447 382 -97 O ATOM 2473 CB GLU A1110 21.859 6.126 261.301 1.00 51.95 C ANISOU 2473 CB GLU A1110 5516 6407 7815 -520 486 -104 C ATOM 2474 CG GLU A1110 20.798 6.342 260.222 1.00 86.09 C ANISOU 2474 CG GLU A1110 9809 10787 12114 -503 425 -208 C ATOM 2475 CD GLU A1110 21.065 7.577 259.368 1.00121.35 C ANISOU 2475 CD GLU A1110 14357 15307 16444 -487 325 -177 C ATOM 2476 OE1 GLU A1110 22.249 7.863 259.079 1.00131.81 O ANISOU 2476 OE1 GLU A1110 15737 16652 17695 -520 330 -110 O ATOM 2477 OE2 GLU A1110 20.091 8.268 258.992 1.00130.74 O ANISOU 2477 OE2 GLU A1110 15561 16520 17593 -443 238 -227 O ATOM 2478 N LYS A1111 20.586 6.551 264.185 1.00 38.11 N ANISOU 2478 N LYS A1111 3769 4560 6151 -513 541 -31 N ATOM 2479 CA LYS A1111 19.409 6.633 265.043 1.00 51.92 C ANISOU 2479 CA LYS A1111 5478 6307 7941 -519 564 -75 C ATOM 2480 C LYS A1111 19.408 7.938 265.824 1.00 62.97 C ANISOU 2480 C LYS A1111 6928 7718 9278 -477 509 -10 C ATOM 2481 O LYS A1111 18.357 8.566 265.994 1.00 57.45 O ANISOU 2481 O LYS A1111 6193 7062 8573 -444 468 -78 O ATOM 2482 CB LYS A1111 19.348 5.429 265.985 1.00 60.19 C ANISOU 2482 CB LYS A1111 6517 7280 9071 -583 674 -64 C ATOM 2483 CG LYS A1111 17.967 5.182 266.590 1.00 38.56 C ANISOU 2483 CG LYS A1111 3710 4560 6379 -629 726 -153 C ATOM 2484 CD LYS A1111 17.854 3.779 267.162 1.00 43.73 C ANISOU 2484 CD LYS A1111 4376 5133 7108 -722 836 -159 C ATOM 2485 CE LYS A1111 16.425 3.444 267.542 1.00 40.10 C ANISOU 2485 CE LYS A1111 3833 4713 6689 -801 901 -274 C ATOM 2486 NZ LYS A1111 16.282 2.007 267.918 1.00 56.54 N ANISOU 2486 NZ LYS A1111 5948 6702 8834 -916 1008 -286 N ATOM 2487 N LEU A1112 20.582 8.380 266.282 1.00 36.62 N ANISOU 2487 N LEU A1112 3670 4349 5894 -472 500 108 N ATOM 2488 CA LEU A1112 20.661 9.654 266.986 1.00 60.59 C ANISOU 2488 CA LEU A1112 6766 7388 8866 -435 442 171 C ATOM 2489 C LEU A1112 20.290 10.819 266.078 1.00 45.15 C ANISOU 2489 C LEU A1112 4848 5476 6831 -383 322 137 C ATOM 2490 O LEU A1112 19.679 11.789 266.538 1.00 47.47 O ANISOU 2490 O LEU A1112 5166 5778 7094 -332 257 124 O ATOM 2491 CB LEU A1112 22.062 9.848 267.571 1.00 38.80 C ANISOU 2491 CB LEU A1112 4078 4592 6071 -449 455 293 C ATOM 2492 CG LEU A1112 22.405 8.981 268.788 1.00 53.80 C ANISOU 2492 CG LEU A1112 5978 6435 8030 -474 543 343 C ATOM 2493 CD1 LEU A1112 23.854 9.192 269.187 1.00 44.59 C ANISOU 2493 CD1 LEU A1112 4869 5249 6825 -472 535 443 C ATOM 2494 CD2 LEU A1112 21.476 9.280 269.964 1.00 38.61 C ANISOU 2494 CD2 LEU A1112 4049 4503 6120 -472 566 335 C ATOM 2495 N LYS A1113 20.638 10.745 264.792 1.00 51.48 N ANISOU 2495 N LYS A1113 5666 6302 7592 -392 285 118 N ATOM 2496 CA LYS A1113 20.164 11.753 263.849 1.00 45.65 C ANISOU 2496 CA LYS A1113 4984 5593 6769 -344 162 80 C ATOM 2497 C LYS A1113 18.651 11.693 263.714 1.00 44.19 C ANISOU 2497 C LYS A1113 4717 5444 6630 -285 122 -54 C ATOM 2498 O LYS A1113 17.967 12.720 263.791 1.00 54.13 O ANISOU 2498 O LYS A1113 6012 6710 7844 -208 16 -89 O ATOM 2499 CB LYS A1113 20.831 11.566 262.487 1.00 43.68 C ANISOU 2499 CB LYS A1113 4770 5370 6457 -382 143 81 C ATOM 2500 CG LYS A1113 21.999 12.507 262.259 1.00 73.24 C ANISOU 2500 CG LYS A1113 8641 9105 10083 -422 100 188 C ATOM 2501 CD LYS A1113 22.531 12.475 260.829 1.00 96.82 C ANISOU 2501 CD LYS A1113 11672 12135 12979 -471 77 176 C ATOM 2502 CE LYS A1113 24.056 12.627 260.807 1.00102.09 C ANISOU 2502 CE LYS A1113 12387 12822 13580 -560 126 264 C ATOM 2503 NZ LYS A1113 24.580 13.143 259.507 1.00107.29 N ANISOU 2503 NZ LYS A1113 13141 13526 14098 -628 81 272 N ATOM 2504 N ASN A1114 18.109 10.491 263.525 1.00 38.02 N ANISOU 2504 N ASN A1114 3821 4686 5939 -317 203 -143 N ATOM 2505 CA ASN A1114 16.668 10.336 263.388 1.00 40.90 C ANISOU 2505 CA ASN A1114 4081 5106 6354 -276 178 -292 C ATOM 2506 C ASN A1114 15.902 10.799 264.620 1.00 52.58 C ANISOU 2506 C ASN A1114 5517 6599 7862 -245 186 -326 C ATOM 2507 O ASN A1114 14.702 11.080 264.520 1.00 39.81 O ANISOU 2507 O ASN A1114 3818 5047 6261 -185 130 -462 O ATOM 2508 CB ASN A1114 16.339 8.880 263.099 1.00 48.06 C ANISOU 2508 CB ASN A1114 4880 6026 7355 -346 283 -373 C ATOM 2509 CG ASN A1114 16.813 8.449 261.734 1.00 52.98 C ANISOU 2509 CG ASN A1114 5522 6659 7951 -359 260 -387 C ATOM 2510 OD1 ASN A1114 16.927 9.267 260.821 1.00 62.47 O ANISOU 2510 OD1 ASN A1114 6793 7883 9059 -308 148 -384 O ATOM 2511 ND2 ASN A1114 17.107 7.166 261.586 1.00 57.41 N ANISOU 2511 ND2 ASN A1114 6035 7197 8583 -428 360 -404 N ATOM 2512 N LEU A1115 16.552 10.859 265.778 1.00 38.38 N ANISOU 2512 N LEU A1115 3761 4752 6068 -281 253 -218 N ATOM 2513 CA LEU A1115 15.906 11.302 267.003 1.00 38.58 C ANISOU 2513 CA LEU A1115 3752 4797 6111 -260 270 -246 C ATOM 2514 C LEU A1115 16.069 12.794 267.249 1.00 61.47 C ANISOU 2514 C LEU A1115 6748 7682 8926 -168 145 -200 C ATOM 2515 O LEU A1115 15.559 13.301 268.254 1.00 53.13 O ANISOU 2515 O LEU A1115 5667 6646 7874 -135 144 -230 O ATOM 2516 CB LEU A1115 16.453 10.504 268.194 1.00 60.47 C ANISOU 2516 CB LEU A1115 6528 7520 8927 -351 409 -158 C ATOM 2517 CG LEU A1115 16.178 8.993 268.144 1.00 38.52 C ANISOU 2517 CG LEU A1115 3674 4732 6231 -450 534 -207 C ATOM 2518 CD1 LEU A1115 16.770 8.295 269.372 1.00 38.27 C ANISOU 2518 CD1 LEU A1115 3689 4628 6223 -529 648 -105 C ATOM 2519 CD2 LEU A1115 14.687 8.695 268.016 1.00 39.59 C ANISOU 2519 CD2 LEU A1115 3672 4955 6416 -464 555 -384 C ATOM 2520 N GLY A1116 16.737 13.515 266.352 1.00 40.48 N ANISOU 2520 N GLY A1116 4207 4989 6184 -133 39 -136 N ATOM 2521 CA GLY A1116 16.898 14.940 266.531 1.00 41.47 C ANISOU 2521 CA GLY A1116 4453 5080 6222 -57 -89 -90 C ATOM 2522 C GLY A1116 17.974 15.331 267.515 1.00 59.81 C ANISOU 2522 C GLY A1116 6864 7346 8515 -100 -48 53 C ATOM 2523 O GLY A1116 17.984 16.474 267.985 1.00 52.59 O ANISOU 2523 O GLY A1116 6037 6401 7544 -41 -139 80 O ATOM 2524 N ALA A1117 18.876 14.419 267.858 1.00 36.88 N ANISOU 2524 N ALA A1117 3941 4424 5649 -193 75 137 N ATOM 2525 CA ALA A1117 20.010 14.789 268.686 1.00 51.04 C ANISOU 2525 CA ALA A1117 5816 6170 7407 -230 101 267 C ATOM 2526 C ALA A1117 20.930 15.738 267.926 1.00 46.87 C ANISOU 2526 C ALA A1117 5425 5610 6773 -240 8 347 C ATOM 2527 O ALA A1117 20.991 15.728 266.694 1.00 59.59 O ANISOU 2527 O ALA A1117 7065 7233 8342 -251 -38 326 O ATOM 2528 CB ALA A1117 20.784 13.544 269.124 1.00 37.40 C ANISOU 2528 CB ALA A1117 4041 4430 5741 -309 235 323 C ATOM 2529 N GLU A1118 21.635 16.583 268.674 1.00 35.88 N ANISOU 2529 N GLU A1118 4123 4180 5329 -248 -20 436 N ATOM 2530 CA GLU A1118 22.631 17.484 268.093 1.00 58.34 C ANISOU 2530 CA GLU A1118 7108 6993 8065 -293 -90 520 C ATOM 2531 C GLU A1118 23.988 16.791 268.146 1.00 42.13 C ANISOU 2531 C GLU A1118 5029 4959 6018 -390 10 596 C ATOM 2532 O GLU A1118 24.697 16.859 269.152 1.00 38.66 O ANISOU 2532 O GLU A1118 4593 4508 5588 -412 52 660 O ATOM 2533 CB GLU A1118 22.655 18.821 268.830 1.00 54.12 C ANISOU 2533 CB GLU A1118 6691 6406 7468 -255 -183 562 C ATOM 2534 CG GLU A1118 23.601 19.848 268.214 1.00 64.01 C ANISOU 2534 CG GLU A1118 8113 7614 8594 -321 -262 646 C ATOM 2535 CD GLU A1118 23.727 21.117 269.053 1.00 80.93 C ANISOU 2535 CD GLU A1118 10380 9691 10680 -295 -348 692 C ATOM 2536 OE1 GLU A1118 22.862 21.351 269.930 1.00 80.19 O ANISOU 2536 OE1 GLU A1118 10247 9587 10635 -195 -376 638 O ATOM 2537 OE2 GLU A1118 24.697 21.880 268.836 1.00 70.23 O ANISOU 2537 OE2 GLU A1118 9159 8298 9228 -381 -384 774 O ATOM 2538 N ILE A1119 24.355 16.123 267.056 1.00 40.75 N ANISOU 2538 N ILE A1119 4824 4822 5838 -439 43 576 N ATOM 2539 CA ILE A1119 25.637 15.429 266.990 1.00 55.43 C ANISOU 2539 CA ILE A1119 6642 6715 7704 -516 129 619 C ATOM 2540 C ILE A1119 26.738 16.473 266.851 1.00 45.90 C ANISOU 2540 C ILE A1119 5546 5511 6382 -592 88 695 C ATOM 2541 O ILE A1119 26.764 17.244 265.886 1.00 52.74 O ANISOU 2541 O ILE A1119 6519 6376 7145 -634 17 702 O ATOM 2542 CB ILE A1119 25.665 14.417 265.835 1.00 35.45 C ANISOU 2542 CB ILE A1119 4040 4233 5198 -541 174 557 C ATOM 2543 CG1 ILE A1119 24.528 13.404 266.010 1.00 41.61 C ANISOU 2543 CG1 ILE A1119 4716 5003 6091 -481 216 477 C ATOM 2544 CG2 ILE A1119 27.009 13.709 265.798 1.00 53.67 C ANISOU 2544 CG2 ILE A1119 6293 6584 7515 -602 254 579 C ATOM 2545 CD1 ILE A1119 24.478 12.332 264.954 1.00 48.10 C ANISOU 2545 CD1 ILE A1119 5463 5862 6949 -500 260 406 C ATOM 2546 N VAL A1120 27.646 16.503 267.826 1.00 45.23 N ANISOU 2546 N VAL A1120 5447 5429 6308 -618 130 751 N ATOM 2547 CA VAL A1120 28.641 17.568 267.882 1.00 58.02 C ANISOU 2547 CA VAL A1120 7168 7053 7823 -700 93 816 C ATOM 2548 C VAL A1120 29.748 17.350 266.859 1.00 48.12 C ANISOU 2548 C VAL A1120 5900 5881 6503 -812 135 809 C ATOM 2549 O VAL A1120 30.295 18.318 266.322 1.00 69.36 O ANISOU 2549 O VAL A1120 8703 8579 9071 -912 94 843 O ATOM 2550 CB VAL A1120 29.213 17.704 269.306 1.00 51.79 C ANISOU 2550 CB VAL A1120 6361 6250 7067 -687 117 865 C ATOM 2551 CG1 VAL A1120 28.150 18.247 270.254 1.00 55.20 C ANISOU 2551 CG1 VAL A1120 6836 6611 7528 -596 64 870 C ATOM 2552 CG2 VAL A1120 29.761 16.375 269.811 1.00 47.72 C ANISOU 2552 CG2 VAL A1120 5711 5774 6647 -664 211 847 C ATOM 2553 N GLN A1121 30.099 16.104 266.563 1.00 47.31 N ANISOU 2553 N GLN A1121 5666 5839 6471 -805 216 757 N ATOM 2554 CA GLN A1121 31.126 15.840 265.564 1.00 70.91 C ANISOU 2554 CA GLN A1121 8619 8926 9398 -905 261 725 C ATOM 2555 C GLN A1121 31.067 14.372 265.176 1.00 70.18 C ANISOU 2555 C GLN A1121 8387 8873 9404 -852 329 647 C ATOM 2556 O GLN A1121 30.326 13.582 265.765 1.00 68.97 O ANISOU 2556 O GLN A1121 8180 8664 9363 -755 344 630 O ATOM 2557 CB GLN A1121 32.513 16.213 266.083 1.00 64.79 C ANISOU 2557 CB GLN A1121 7826 8214 8577 -986 291 752 C ATOM 2558 CG GLN A1121 32.995 15.329 267.202 1.00 71.54 C ANISOU 2558 CG GLN A1121 8562 9077 9543 -906 337 741 C ATOM 2559 CD GLN A1121 34.132 15.948 267.986 1.00102.96 C ANISOU 2559 CD GLN A1121 12543 13100 13479 -963 337 773 C ATOM 2560 OE1 GLN A1121 34.171 17.173 268.179 1.00 97.19 O ANISOU 2560 OE1 GLN A1121 11928 12339 12662 -1032 288 830 O ATOM 2561 NE2 GLN A1121 35.056 15.122 268.430 1.00118.80 N ANISOU 2561 NE2 GLN A1121 14424 15171 15542 -930 381 729 N ATOM 2562 N ASP A1122 31.867 14.017 264.173 1.00 58.84 N ANISOU 2562 N ASP A1122 6900 7537 7918 -927 371 594 N ATOM 2563 CA ASP A1122 31.830 12.675 263.615 1.00 40.66 C ANISOU 2563 CA ASP A1122 4478 5273 5697 -880 425 506 C ATOM 2564 C ASP A1122 32.381 11.656 264.601 1.00 52.95 C ANISOU 2564 C ASP A1122 5928 6822 7370 -800 469 486 C ATOM 2565 O ASP A1122 33.209 11.967 265.460 1.00 63.64 O ANISOU 2565 O ASP A1122 7271 8192 8716 -807 470 520 O ATOM 2566 CB ASP A1122 32.621 12.621 262.314 1.00 60.97 C ANISOU 2566 CB ASP A1122 7022 7970 8175 -983 460 443 C ATOM 2567 CG ASP A1122 32.006 13.476 261.241 1.00 82.19 C ANISOU 2567 CG ASP A1122 9838 10651 10740 -1057 410 462 C ATOM 2568 OD1 ASP A1122 30.826 13.849 261.403 1.00 87.35 O ANISOU 2568 OD1 ASP A1122 10573 11204 11411 -993 343 498 O ATOM 2569 OD2 ASP A1122 32.696 13.780 260.248 1.00 89.71 O ANISOU 2569 OD2 ASP A1122 10811 11703 11571 -1178 434 435 O ATOM 2570 N GLY A1123 31.921 10.419 264.452 1.00 69.75 N ANISOU 2570 N GLY A1123 7984 8918 9600 -724 497 426 N ATOM 2571 CA GLY A1123 32.221 9.404 265.438 1.00 77.86 C ANISOU 2571 CA GLY A1123 8950 9896 10736 -635 521 417 C ATOM 2572 C GLY A1123 33.673 8.969 265.406 1.00 62.99 C ANISOU 2572 C GLY A1123 6975 8109 8847 -633 543 359 C ATOM 2573 O GLY A1123 34.352 9.026 264.379 1.00 71.35 O ANISOU 2573 O GLY A1123 7979 9287 9843 -698 565 288 O ATOM 2574 N LEU A1124 34.148 8.520 266.564 1.00 57.13 N ANISOU 2574 N LEU A1124 6217 7322 8169 -556 534 379 N ATOM 2575 CA LEU A1124 35.487 7.964 266.703 1.00 57.37 C ANISOU 2575 CA LEU A1124 6149 7435 8214 -515 537 306 C ATOM 2576 C LEU A1124 35.441 6.470 266.403 1.00 71.17 C ANISOU 2576 C LEU A1124 7840 9141 10060 -417 546 218 C ATOM 2577 O LEU A1124 34.747 5.710 267.090 1.00 53.95 O ANISOU 2577 O LEU A1124 5715 6820 7964 -339 536 252 O ATOM 2578 CB LEU A1124 36.031 8.217 268.107 1.00 53.78 C ANISOU 2578 CB LEU A1124 5717 6945 7773 -464 504 367 C ATOM 2579 CG LEU A1124 37.391 7.607 268.449 1.00 64.58 C ANISOU 2579 CG LEU A1124 6982 8391 9166 -390 485 283 C ATOM 2580 CD1 LEU A1124 38.469 8.088 267.484 1.00 75.42 C ANISOU 2580 CD1 LEU A1124 8243 9959 10454 -485 512 185 C ATOM 2581 CD2 LEU A1124 37.749 7.957 269.886 1.00 70.68 C ANISOU 2581 CD2 LEU A1124 7799 9113 9942 -340 441 357 C ATOM 2582 N ARG A1125 36.185 6.054 265.380 1.00 76.27 N ANISOU 2582 N ARG A1125 8382 9909 10688 -428 567 98 N ATOM 2583 CA ARG A1125 36.241 4.663 264.943 1.00 61.72 C ANISOU 2583 CA ARG A1125 6481 8038 8931 -333 569 -8 C ATOM 2584 C ARG A1125 37.671 4.176 265.120 1.00 74.71 C ANISOU 2584 C ARG A1125 8012 9784 10589 -255 546 -116 C ATOM 2585 O ARG A1125 38.578 4.632 264.414 1.00 81.11 O ANISOU 2585 O ARG A1125 8717 10777 11322 -325 571 -202 O ATOM 2586 CB ARG A1125 35.787 4.532 263.491 1.00 50.97 C ANISOU 2586 CB ARG A1125 5086 6741 7537 -400 607 -80 C ATOM 2587 CG ARG A1125 34.360 4.993 263.269 1.00 49.86 C ANISOU 2587 CG ARG A1125 5047 6511 7386 -459 614 5 C ATOM 2588 CD ARG A1125 34.209 5.753 261.966 1.00 56.16 C ANISOU 2588 CD ARG A1125 5841 7424 8073 -576 636 -21 C ATOM 2589 NE ARG A1125 32.946 6.483 261.935 1.00 71.37 N ANISOU 2589 NE ARG A1125 7873 9273 9973 -620 617 67 N ATOM 2590 CZ ARG A1125 31.782 5.941 261.596 1.00 78.94 C ANISOU 2590 CZ ARG A1125 8854 10150 10989 -591 615 50 C ATOM 2591 NH1 ARG A1125 31.725 4.662 261.249 1.00 94.03 N ANISOU 2591 NH1 ARG A1125 10705 12036 12987 -531 634 -42 N ATOM 2592 NH2 ARG A1125 30.675 6.675 261.604 1.00 70.08 N ANISOU 2592 NH2 ARG A1125 7813 8976 9839 -620 587 112 N ATOM 2593 N ILE A1126 37.868 3.255 266.058 1.00 73.12 N ANISOU 2593 N ILE A1126 7835 9469 10478 -114 494 -120 N ATOM 2594 CA ILE A1126 39.194 2.779 266.433 1.00 71.85 C ANISOU 2594 CA ILE A1126 7577 9386 10338 -4 445 -225 C ATOM 2595 C ILE A1126 39.422 1.429 265.772 1.00 83.22 C ANISOU 2595 C ILE A1126 8956 10812 11853 110 424 -370 C ATOM 2596 O ILE A1126 38.639 0.491 265.966 1.00 75.44 O ANISOU 2596 O ILE A1126 8070 9645 10948 181 404 -342 O ATOM 2597 CB ILE A1126 39.346 2.688 267.958 1.00 61.27 C ANISOU 2597 CB ILE A1126 6324 7922 9034 95 378 -135 C ATOM 2598 CG1 ILE A1126 39.388 4.099 268.548 1.00 59.92 C ANISOU 2598 CG1 ILE A1126 6182 7805 8780 -15 394 -25 C ATOM 2599 CG2 ILE A1126 40.620 1.918 268.343 1.00 58.93 C ANISOU 2599 CG2 ILE A1126 5939 7674 8777 255 299 -263 C ATOM 2600 CD1 ILE A1126 38.894 4.188 269.963 1.00 60.57 C ANISOU 2600 CD1 ILE A1126 6401 7726 8886 34 355 112 C ATOM 2601 N ASP A1127 40.496 1.336 264.994 1.00 90.21 N ANISOU 2601 N ASP A1127 9678 11891 12707 120 432 -534 N ATOM 2602 CA ASP A1127 40.873 0.108 264.311 1.00 89.67 C ANISOU 2602 CA ASP A1127 9529 11840 12703 240 406 -703 C ATOM 2603 C ASP A1127 41.918 -0.629 265.137 1.00 76.09 C ANISOU 2603 C ASP A1127 7762 10105 11043 433 304 -798 C ATOM 2604 O ASP A1127 42.919 -0.037 265.555 1.00 96.11 O ANISOU 2604 O ASP A1127 10199 12787 13533 438 285 -841 O ATOM 2605 CB ASP A1127 41.425 0.413 262.919 1.00 90.79 C ANISOU 2605 CB ASP A1127 9508 12221 12767 138 477 -850 C ATOM 2606 CG ASP A1127 41.568 -0.824 262.072 1.00 98.60 C ANISOU 2606 CG ASP A1127 10424 13219 13819 247 461 -1022 C ATOM 2607 OD1 ASP A1127 41.468 -1.935 262.630 1.00106.50 O ANISOU 2607 OD1 ASP A1127 11491 14047 14928 419 380 -1044 O ATOM 2608 OD2 ASP A1127 41.783 -0.686 260.850 1.00103.08 O ANISOU 2608 OD2 ASP A1127 10880 13961 14323 157 527 -1136 O ATOM 2609 N GLY A1128 41.684 -1.918 265.372 1.00 63.28 N ANISOU 2609 N GLY A1128 6219 8303 9519 594 232 -835 N ATOM 2610 CA GLY A1128 42.654 -2.699 266.111 1.00 81.89 C ANISOU 2610 CA GLY A1128 8555 10627 11932 804 111 -934 C ATOM 2611 C GLY A1128 42.716 -2.275 267.570 1.00 79.60 C ANISOU 2611 C GLY A1128 8380 10231 11633 840 52 -788 C ATOM 2612 O GLY A1128 41.716 -1.878 268.177 1.00 69.78 O ANISOU 2612 O GLY A1128 7296 8838 10380 749 86 -598 O ATOM 2613 N ASP A1129 43.917 -2.346 268.136 1.00 77.64 N ANISOU 2613 N ASP A1129 8040 10075 11385 978 -40 -892 N ATOM 2614 CA ASP A1129 44.082 -2.081 269.560 1.00 88.92 C ANISOU 2614 CA ASP A1129 9581 11399 12805 1043 -117 -774 C ATOM 2615 C ASP A1129 43.921 -0.590 269.833 1.00 81.61 C ANISOU 2615 C ASP A1129 8632 10584 11790 850 -30 -646 C ATOM 2616 O ASP A1129 44.570 0.229 269.174 1.00 81.36 O ANISOU 2616 O ASP A1129 8423 10795 11695 741 33 -736 O ATOM 2617 CB ASP A1129 45.447 -2.560 270.043 1.00 90.12 C ANISOU 2617 CB ASP A1129 9627 11635 12979 1257 -254 -941 C ATOM 2618 CG ASP A1129 45.458 -2.888 271.527 1.00100.73 C ANISOU 2618 CG ASP A1129 11160 12774 14340 1399 -379 -828 C ATOM 2619 OD1 ASP A1129 44.998 -3.994 271.886 1.00109.78 O ANISOU 2619 OD1 ASP A1129 12494 13673 15545 1526 -460 -790 O ATOM 2620 OD2 ASP A1129 45.921 -2.053 272.332 1.00 92.64 O ANISOU 2620 OD2 ASP A1129 10107 11828 13262 1376 -397 -776 O ATOM 2621 N PRO A1130 43.078 -0.195 270.791 1.00 78.82 N ANISOU 2621 N PRO A1130 8460 10063 11425 795 -23 -445 N ATOM 2622 CA PRO A1130 42.931 1.240 271.070 1.00 82.17 C ANISOU 2622 CA PRO A1130 8871 10584 11766 625 48 -333 C ATOM 2623 C PRO A1130 44.140 1.839 271.757 1.00 90.56 C ANISOU 2623 C PRO A1130 9829 11794 12786 669 -11 -391 C ATOM 2624 O PRO A1130 44.376 3.047 271.631 1.00 98.78 O ANISOU 2624 O PRO A1130 10795 12986 13751 516 51 -367 O ATOM 2625 CB PRO A1130 41.688 1.293 271.967 1.00 78.22 C ANISOU 2625 CB PRO A1130 8592 9853 11275 587 59 -129 C ATOM 2626 CG PRO A1130 41.668 -0.029 272.643 1.00 68.20 C ANISOU 2626 CG PRO A1130 7452 8385 10076 768 -41 -133 C ATOM 2627 CD PRO A1130 42.211 -1.014 271.655 1.00 80.56 C ANISOU 2627 CD PRO A1130 8910 10002 11696 873 -73 -316 C ATOM 2628 N ARG A1131 44.911 1.034 272.486 1.00 94.76 N ANISOU 2628 N ARG A1131 10362 12281 13361 875 -138 -470 N ATOM 2629 CA ARG A1131 46.102 1.554 273.146 1.00 93.98 C ANISOU 2629 CA ARG A1131 10146 12337 13225 933 -207 -548 C ATOM 2630 C ARG A1131 47.145 2.014 272.134 1.00 78.60 C ANISOU 2630 C ARG A1131 7933 10693 11238 861 -156 -749 C ATOM 2631 O ARG A1131 47.926 2.927 272.424 1.00 64.40 O ANISOU 2631 O ARG A1131 6017 9072 9379 790 -149 -790 O ATOM 2632 CB ARG A1131 46.679 0.489 274.078 1.00 98.28 C ANISOU 2632 CB ARG A1131 10757 12759 13824 1194 -374 -606 C ATOM 2633 CG ARG A1131 45.709 0.059 275.185 1.00109.05 C ANISOU 2633 CG ARG A1131 12404 13825 15203 1244 -421 -402 C ATOM 2634 CD ARG A1131 45.923 -1.390 275.629 1.00120.86 C ANISOU 2634 CD ARG A1131 14027 15130 16763 1489 -571 -457 C ATOM 2635 NE ARG A1131 44.922 -1.828 276.608 1.00127.29 N ANISOU 2635 NE ARG A1131 15132 15656 17576 1498 -596 -256 N ATOM 2636 CZ ARG A1131 43.739 -2.363 276.301 1.00116.49 C ANISOU 2636 CZ ARG A1131 13920 14105 16238 1417 -526 -155 C ATOM 2637 NH1 ARG A1131 43.385 -2.538 275.032 1.00107.33 N ANISOU 2637 NH1 ARG A1131 12657 13008 15116 1337 -436 -230 N ATOM 2638 NH2 ARG A1131 42.902 -2.726 277.267 1.00 99.47 N ANISOU 2638 NH2 ARG A1131 12020 11707 14067 1408 -542 16 N ATOM 2639 N ALA A1132 47.163 1.409 270.946 1.00 72.11 N ANISOU 2639 N ALA A1132 7014 9940 10444 863 -114 -880 N ATOM 2640 CA ALA A1132 48.074 1.802 269.878 1.00 67.77 C ANISOU 2640 CA ALA A1132 6216 9690 9845 769 -46 -1077 C ATOM 2641 C ALA A1132 47.567 2.995 269.076 1.00 85.48 C ANISOU 2641 C ALA A1132 8452 12035 11993 485 107 -987 C ATOM 2642 O ALA A1132 48.255 3.433 268.148 1.00102.82 O ANISOU 2642 O ALA A1132 10464 14479 14123 360 184 -1131 O ATOM 2643 CB ALA A1132 48.316 0.623 268.930 1.00 74.37 C ANISOU 2643 CB ALA A1132 6954 10561 10743 898 -69 -1267 C ATOM 2644 N ALA A1133 46.383 3.521 269.403 1.00 80.26 N ANISOU 2644 N ALA A1133 7988 11189 11316 379 150 -762 N ATOM 2645 CA ALA A1133 45.800 4.664 268.709 1.00 78.45 C ANISOU 2645 CA ALA A1133 7791 11019 10996 132 269 -663 C ATOM 2646 C ALA A1133 45.362 5.735 269.703 1.00 81.66 C ANISOU 2646 C ALA A1133 8334 11335 11358 44 267 -475 C ATOM 2647 O ALA A1133 44.371 6.436 269.478 1.00 88.64 O ANISOU 2647 O ALA A1133 9342 12135 12201 -95 328 -330 O ATOM 2648 CB ALA A1133 44.620 4.226 267.838 1.00 65.03 C ANISOU 2648 CB ALA A1133 6191 9196 9322 90 325 -602 C ATOM 2649 N ARG A1134 46.105 5.882 270.804 1.00 79.17 N ANISOU 2649 N ARG A1134 7992 11041 11048 132 190 -487 N ATOM 2650 CA ARG A1134 45.684 6.766 271.888 1.00 70.56 C ANISOU 2650 CA ARG A1134 7039 9845 9925 80 173 -315 C ATOM 2651 C ARG A1134 45.663 8.231 271.462 1.00 84.24 C ANISOU 2651 C ARG A1134 8766 11692 11548 -162 260 -260 C ATOM 2652 O ARG A1134 44.822 8.998 271.942 1.00 75.79 O ANISOU 2652 O ARG A1134 7850 10497 10449 -240 273 -93 O ATOM 2653 CB ARG A1134 46.607 6.579 273.093 1.00 73.05 C ANISOU 2653 CB ARG A1134 7313 10182 10262 232 64 -364 C ATOM 2654 CG ARG A1134 46.184 7.362 274.332 1.00 80.05 C ANISOU 2654 CG ARG A1134 8348 10949 11119 205 36 -192 C ATOM 2655 CD ARG A1134 47.154 7.155 275.486 1.00 69.80 C ANISOU 2655 CD ARG A1134 7005 9683 9834 361 -81 -253 C ATOM 2656 NE ARG A1134 46.911 8.084 276.589 1.00 87.86 N ANISOU 2656 NE ARG A1134 9405 11905 12074 307 -99 -111 N ATOM 2657 CZ ARG A1134 47.374 9.333 276.635 1.00102.97 C ANISOU 2657 CZ ARG A1134 11255 13959 13910 146 -60 -115 C ATOM 2658 NH1 ARG A1134 48.101 9.818 275.635 1.00 93.65 N ANISOU 2658 NH1 ARG A1134 9904 12996 12682 5 7 -246 N ATOM 2659 NH2 ARG A1134 47.109 10.108 277.680 1.00111.88 N ANISOU 2659 NH2 ARG A1134 12497 15011 15002 115 -85 11 N ATOM 2660 N ASP A1135 46.575 8.642 270.576 1.00104.03 N ANISOU 2660 N ASP A1135 11106 14434 13986 -287 317 -403 N ATOM 2661 CA ASP A1135 46.604 10.038 270.149 1.00 98.79 C ANISOU 2661 CA ASP A1135 10465 13866 13203 -536 395 -350 C ATOM 2662 C ASP A1135 45.287 10.456 269.506 1.00 81.80 C ANISOU 2662 C ASP A1135 8486 11575 11020 -646 451 -201 C ATOM 2663 O ASP A1135 44.853 11.603 269.667 1.00 78.64 O ANISOU 2663 O ASP A1135 8208 11127 10546 -788 470 -76 O ATOM 2664 CB ASP A1135 47.763 10.275 269.177 1.00 89.91 C ANISOU 2664 CB ASP A1135 9139 13024 12000 -672 463 -541 C ATOM 2665 CG ASP A1135 49.099 10.405 269.881 1.00 95.99 C ANISOU 2665 CG ASP A1135 9738 13970 12764 -634 418 -681 C ATOM 2666 OD1 ASP A1135 49.107 10.705 271.093 1.00 96.36 O ANISOU 2666 OD1 ASP A1135 9855 13924 12834 -561 344 -595 O ATOM 2667 OD2 ASP A1135 50.142 10.222 269.219 1.00 94.10 O ANISOU 2667 OD2 ASP A1135 9287 13976 12491 -679 456 -887 O ATOM 2668 N ASP A1136 44.636 9.545 268.782 1.00 66.93 N ANISOU 2668 N ASP A1136 6616 9623 9192 -576 467 -220 N ATOM 2669 CA ASP A1136 43.355 9.877 268.170 1.00 68.35 C ANISOU 2669 CA ASP A1136 6946 9675 9347 -662 507 -95 C ATOM 2670 C ASP A1136 42.257 9.978 269.221 1.00 59.07 C ANISOU 2670 C ASP A1136 5943 8275 8227 -583 459 74 C ATOM 2671 O ASP A1136 41.453 10.917 269.197 1.00 74.36 O ANISOU 2671 O ASP A1136 8010 10136 10109 -687 473 195 O ATOM 2672 CB ASP A1136 42.993 8.833 267.114 1.00 78.94 C ANISOU 2672 CB ASP A1136 8241 11017 10735 -609 536 -179 C ATOM 2673 CG ASP A1136 44.118 8.593 266.125 1.00 95.77 C ANISOU 2673 CG ASP A1136 10183 13386 12817 -667 584 -372 C ATOM 2674 OD1 ASP A1136 45.290 8.819 266.499 1.00108.43 O ANISOU 2674 OD1 ASP A1136 11657 15147 14396 -676 574 -472 O ATOM 2675 OD2 ASP A1136 43.832 8.174 264.980 1.00 79.35 O ANISOU 2675 OD2 ASP A1136 8076 11349 10724 -703 632 -435 O ATOM 2676 N ILE A1137 42.214 9.028 270.156 1.00 57.96 N ANISOU 2676 N ILE A1137 5811 8026 8186 -400 398 78 N ATOM 2677 CA ILE A1137 41.191 9.055 271.199 1.00 72.33 C ANISOU 2677 CA ILE A1137 7790 9646 10048 -336 364 228 C ATOM 2678 C ILE A1137 41.254 10.372 271.958 1.00 85.18 C ANISOU 2678 C ILE A1137 9484 11277 11603 -428 352 323 C ATOM 2679 O ILE A1137 40.231 11.030 272.185 1.00 96.54 O ANISOU 2679 O ILE A1137 11052 12607 13021 -481 361 442 O ATOM 2680 CB ILE A1137 41.353 7.854 272.148 1.00 72.14 C ANISOU 2680 CB ILE A1137 7777 9515 10118 -140 296 212 C ATOM 2681 CG1 ILE A1137 41.302 6.543 271.356 1.00 75.82 C ANISOU 2681 CG1 ILE A1137 8190 9963 10656 -48 298 109 C ATOM 2682 CG2 ILE A1137 40.260 7.883 273.222 1.00 78.71 C ANISOU 2682 CG2 ILE A1137 8779 10151 10977 -102 277 365 C ATOM 2683 CD1 ILE A1137 41.515 5.293 272.191 1.00 60.18 C ANISOU 2683 CD1 ILE A1137 6245 7860 8760 148 217 85 C ATOM 2684 N VAL A1138 42.458 10.776 272.362 1.00 86.03 N ANISOU 2684 N VAL A1138 9497 11517 11672 -444 328 257 N ATOM 2685 CA VAL A1138 42.618 12.028 273.091 1.00 76.57 C ANISOU 2685 CA VAL A1138 8360 10329 10405 -536 313 335 C ATOM 2686 C VAL A1138 42.310 13.211 272.182 1.00 76.40 C ANISOU 2686 C VAL A1138 8394 10352 10283 -739 368 374 C ATOM 2687 O VAL A1138 41.697 14.197 272.609 1.00 68.12 O ANISOU 2687 O VAL A1138 7478 9216 9190 -805 355 487 O ATOM 2688 CB VAL A1138 44.036 12.115 273.684 1.00 77.63 C ANISOU 2688 CB VAL A1138 8362 10610 10523 -509 273 233 C ATOM 2689 CG1 VAL A1138 44.184 13.357 274.533 1.00 89.45 C ANISOU 2689 CG1 VAL A1138 9929 12103 11954 -598 252 312 C ATOM 2690 CG2 VAL A1138 44.348 10.878 274.516 1.00 68.90 C ANISOU 2690 CG2 VAL A1138 7222 9447 9511 -287 197 188 C ATOM 2691 N GLY A1139 42.719 13.130 270.914 1.00 73.00 N ANISOU 2691 N GLY A1139 7877 10053 9807 -839 424 279 N ATOM 2692 CA GLY A1139 42.401 14.195 269.977 1.00 63.21 C ANISOU 2692 CA GLY A1139 6721 8841 8456 -1035 470 321 C ATOM 2693 C GLY A1139 40.908 14.338 269.758 1.00 55.10 C ANISOU 2693 C GLY A1139 5855 7638 7444 -1016 460 440 C ATOM 2694 O GLY A1139 40.382 15.454 269.707 1.00 51.71 O ANISOU 2694 O GLY A1139 5564 7146 6938 -1119 447 531 O ATOM 2695 N TRP A1140 40.205 13.211 269.632 1.00 75.65 N ANISOU 2695 N TRP A1140 8443 10158 10143 -881 459 429 N ATOM 2696 CA TRP A1140 38.755 13.246 269.472 1.00 48.37 C ANISOU 2696 CA TRP A1140 5114 6550 6712 -853 451 519 C ATOM 2697 C TRP A1140 38.086 13.821 270.714 1.00 59.60 C ANISOU 2697 C TRP A1140 6651 7841 8153 -804 404 632 C ATOM 2698 O TRP A1140 37.184 14.661 270.610 1.00 53.76 O ANISOU 2698 O TRP A1140 6032 7023 7370 -853 385 707 O ATOM 2699 CB TRP A1140 38.231 11.839 269.173 1.00 50.77 C ANISOU 2699 CB TRP A1140 5368 6800 7121 -729 464 471 C ATOM 2700 CG TRP A1140 36.767 11.775 268.837 1.00 44.86 C ANISOU 2700 CG TRP A1140 4718 5928 6399 -713 465 530 C ATOM 2701 CD1 TRP A1140 36.197 12.004 267.619 1.00 49.12 C ANISOU 2701 CD1 TRP A1140 5287 6486 6889 -789 484 515 C ATOM 2702 CD2 TRP A1140 35.691 11.445 269.726 1.00 47.86 C ANISOU 2702 CD2 TRP A1140 5172 6159 6854 -619 445 601 C ATOM 2703 NE1 TRP A1140 34.834 11.843 267.695 1.00 51.03 N ANISOU 2703 NE1 TRP A1140 5605 6605 7180 -736 469 562 N ATOM 2704 CE2 TRP A1140 34.498 11.498 268.977 1.00 58.31 C ANISOU 2704 CE2 TRP A1140 6548 7428 8178 -640 453 612 C ATOM 2705 CE3 TRP A1140 35.621 11.110 271.081 1.00 49.46 C ANISOU 2705 CE3 TRP A1140 5402 6277 7115 -527 423 650 C ATOM 2706 CZ2 TRP A1140 33.247 11.231 269.539 1.00 56.13 C ANISOU 2706 CZ2 TRP A1140 6331 7032 7964 -578 447 656 C ATOM 2707 CZ3 TRP A1140 34.375 10.845 271.639 1.00 51.97 C ANISOU 2707 CZ3 TRP A1140 5794 6468 7484 -477 424 707 C ATOM 2708 CH2 TRP A1140 33.208 10.908 270.868 1.00 48.96 C ANISOU 2708 CH2 TRP A1140 5444 6050 7108 -506 440 703 C ATOM 2709 N ALA A1141 38.523 13.389 271.901 1.00 52.59 N ANISOU 2709 N ALA A1141 5729 6930 7322 -702 377 638 N ATOM 2710 CA ALA A1141 37.942 13.916 273.131 1.00 59.63 C ANISOU 2710 CA ALA A1141 6724 7710 8222 -659 338 737 C ATOM 2711 C ALA A1141 38.167 15.412 273.248 1.00 62.50 C ANISOU 2711 C ALA A1141 7161 8100 8485 -781 316 784 C ATOM 2712 O ALA A1141 37.344 16.119 273.843 1.00 68.86 O ANISOU 2712 O ALA A1141 8080 8806 9277 -774 285 865 O ATOM 2713 CB ALA A1141 38.533 13.205 274.346 1.00 40.55 C ANISOU 2713 CB ALA A1141 4267 5276 5863 -536 307 730 C ATOM 2714 N HIS A1142 39.272 15.911 272.689 1.00 68.44 N ANISOU 2714 N HIS A1142 7852 8988 9163 -900 331 726 N ATOM 2715 CA HIS A1142 39.537 17.344 272.719 1.00 61.98 C ANISOU 2715 CA HIS A1142 7124 8188 8240 -1043 312 768 C ATOM 2716 C HIS A1142 38.546 18.091 271.838 1.00 59.41 C ANISOU 2716 C HIS A1142 6938 7784 7849 -1124 304 824 C ATOM 2717 O HIS A1142 38.090 19.184 272.194 1.00 58.27 O ANISOU 2717 O HIS A1142 6933 7557 7651 -1166 257 897 O ATOM 2718 CB HIS A1142 40.979 17.616 272.282 1.00 68.07 C ANISOU 2718 CB HIS A1142 7787 9136 8940 -1174 344 678 C ATOM 2719 CG HIS A1142 42.006 17.154 273.270 1.00 78.92 C ANISOU 2719 CG HIS A1142 9033 10591 10361 -1092 326 616 C ATOM 2720 ND1 HIS A1142 41.691 16.852 274.577 1.00 86.37 N ANISOU 2720 ND1 HIS A1142 10007 11435 11376 -942 274 670 N ATOM 2721 CD2 HIS A1142 43.339 16.939 273.146 1.00 82.70 C ANISOU 2721 CD2 HIS A1142 9352 11248 10822 -1135 346 494 C ATOM 2722 CE1 HIS A1142 42.783 16.474 275.216 1.00 82.77 C ANISOU 2722 CE1 HIS A1142 9430 11078 10941 -887 253 593 C ATOM 2723 NE2 HIS A1142 43.798 16.522 274.372 1.00 72.54 N ANISOU 2723 NE2 HIS A1142 8006 9957 9597 -996 293 478 N ATOM 2724 N ASP A1143 38.178 17.506 270.699 1.00 57.05 N ANISOU 2724 N ASP A1143 6613 7506 7556 -1133 339 785 N ATOM 2725 CA ASP A1143 37.234 18.173 269.810 1.00 66.62 C ANISOU 2725 CA ASP A1143 7963 8647 8702 -1196 317 830 C ATOM 2726 C ASP A1143 35.819 18.114 270.374 1.00 66.61 C ANISOU 2726 C ASP A1143 8041 8497 8771 -1064 271 889 C ATOM 2727 O ASP A1143 35.058 19.082 270.257 1.00 69.99 O ANISOU 2727 O ASP A1143 8611 8839 9141 -1088 214 942 O ATOM 2728 CB ASP A1143 37.297 17.545 268.419 1.00 66.32 C ANISOU 2728 CB ASP A1143 7867 8689 8643 -1245 367 761 C ATOM 2729 CG ASP A1143 38.695 17.544 267.848 1.00 88.00 C ANISOU 2729 CG ASP A1143 10511 11609 11317 -1380 425 679 C ATOM 2730 OD1 ASP A1143 39.513 18.397 268.259 1.00100.70 O ANISOU 2730 OD1 ASP A1143 12141 13268 12852 -1490 420 690 O ATOM 2731 OD2 ASP A1143 38.974 16.679 266.992 1.00 95.24 O ANISOU 2731 OD2 ASP A1143 11317 12619 12249 -1380 477 592 O ATOM 2732 N VAL A1144 35.451 16.989 270.992 1.00 67.41 N ANISOU 2732 N VAL A1144 8055 8567 8989 -927 293 872 N ATOM 2733 CA VAL A1144 34.148 16.885 271.642 1.00 57.28 C ANISOU 2733 CA VAL A1144 6828 7165 7769 -820 266 914 C ATOM 2734 C VAL A1144 34.060 17.848 272.815 1.00 65.67 C ANISOU 2734 C VAL A1144 7975 8170 8806 -808 216 976 C ATOM 2735 O VAL A1144 32.978 18.354 273.136 1.00 57.81 O ANISOU 2735 O VAL A1144 7062 7089 7813 -761 175 1006 O ATOM 2736 CB VAL A1144 33.895 15.426 272.080 1.00 66.58 C ANISOU 2736 CB VAL A1144 7911 8323 9065 -706 309 883 C ATOM 2737 CG1 VAL A1144 33.294 15.350 273.484 1.00 73.60 C ANISOU 2737 CG1 VAL A1144 8835 9126 10004 -618 296 933 C ATOM 2738 CG2 VAL A1144 32.979 14.729 271.091 1.00 58.85 C ANISOU 2738 CG2 VAL A1144 6912 7323 8125 -684 333 841 C ATOM 2739 N ARG A1145 35.192 18.116 273.471 1.00 65.80 N ANISOU 2739 N ARG A1145 7962 8241 8796 -844 215 982 N ATOM 2740 CA ARG A1145 35.206 18.968 274.657 1.00 71.93 C ANISOU 2740 CA ARG A1145 8810 8969 9550 -830 169 1034 C ATOM 2741 C ARG A1145 34.491 20.291 274.417 1.00 70.07 C ANISOU 2741 C ARG A1145 8725 8658 9239 -878 105 1074 C ATOM 2742 O ARG A1145 33.818 20.813 275.313 1.00 52.86 O ANISOU 2742 O ARG A1145 6615 6403 7068 -814 61 1107 O ATOM 2743 CB ARG A1145 36.656 19.207 275.081 1.00 68.46 C ANISOU 2743 CB ARG A1145 8316 8624 9074 -894 172 1017 C ATOM 2744 CG ARG A1145 36.894 20.341 276.064 1.00 61.99 C ANISOU 2744 CG ARG A1145 7580 7771 8201 -925 119 1062 C ATOM 2745 CD ARG A1145 38.380 20.645 276.138 1.00 78.65 C ANISOU 2745 CD ARG A1145 9623 9999 10259 -1027 128 1022 C ATOM 2746 NE ARG A1145 38.909 21.065 274.839 1.00 86.07 N ANISOU 2746 NE ARG A1145 10569 11017 11117 -1188 155 988 N ATOM 2747 CZ ARG A1145 40.200 21.085 274.513 1.00 83.65 C ANISOU 2747 CZ ARG A1145 10165 10854 10765 -1301 190 920 C ATOM 2748 NH1 ARG A1145 41.123 20.702 275.387 1.00 89.76 N ANISOU 2748 NH1 ARG A1145 10819 11711 11576 -1252 189 872 N ATOM 2749 NH2 ARG A1145 40.571 21.486 273.303 1.00 71.27 N ANISOU 2749 NH2 ARG A1145 8618 9356 9107 -1465 225 890 N ATOM 2750 N GLY A1146 34.624 20.847 273.215 1.00 71.06 N ANISOU 2750 N GLY A1146 8914 8802 9283 -987 92 1067 N ATOM 2751 CA GLY A1146 34.089 22.163 272.926 1.00 58.41 C ANISOU 2751 CA GLY A1146 7487 7115 7592 -1037 10 1106 C ATOM 2752 C GLY A1146 32.586 22.211 272.731 1.00 73.65 C ANISOU 2752 C GLY A1146 9479 8950 9554 -927 -41 1103 C ATOM 2753 O GLY A1146 32.046 23.255 272.354 1.00 70.81 O ANISOU 2753 O GLY A1146 9273 8511 9120 -945 -128 1123 O ATOM 2754 N ALA A1147 31.895 21.095 272.985 1.00 75.00 N ANISOU 2754 N ALA A1147 9536 9128 9831 -815 7 1071 N ATOM 2755 CA ALA A1147 30.440 21.084 272.863 1.00 50.60 C ANISOU 2755 CA ALA A1147 6475 5972 6779 -713 -33 1045 C ATOM 2756 C ALA A1147 29.804 22.161 273.732 1.00 47.98 C ANISOU 2756 C ALA A1147 6247 5560 6423 -654 -117 1062 C ATOM 2757 O ALA A1147 28.862 22.838 273.303 1.00 64.37 O ANISOU 2757 O ALA A1147 8416 7575 8468 -607 -203 1040 O ATOM 2758 CB ALA A1147 29.891 19.710 273.238 1.00 61.05 C ANISOU 2758 CB ALA A1147 7660 7318 8219 -625 44 1008 C ATOM 2759 N ILE A1148 30.294 22.326 274.950 1.00 73.97 N ANISOU 2759 N ILE A1148 9524 8854 9727 -643 -104 1091 N ATOM 2760 CA ILE A1148 29.831 23.368 275.866 1.00 80.03 C ANISOU 2760 CA ILE A1148 10386 9554 10467 -591 -181 1101 C ATOM 2761 C ILE A1148 30.927 24.420 275.970 1.00 67.86 C ANISOU 2761 C ILE A1148 8952 7997 8833 -699 -228 1149 C ATOM 2762 O ILE A1148 32.088 24.064 276.203 1.00 74.67 O ANISOU 2762 O ILE A1148 9749 8929 9694 -776 -169 1170 O ATOM 2763 CB ILE A1148 29.481 22.799 277.255 1.00 75.56 C ANISOU 2763 CB ILE A1148 9732 9002 9975 -502 -130 1092 C ATOM 2764 CG1 ILE A1148 28.160 22.031 277.182 1.00 67.34 C ANISOU 2764 CG1 ILE A1148 8614 7963 9007 -411 -97 1032 C ATOM 2765 CG2 ILE A1148 29.368 23.913 278.316 1.00 69.69 C ANISOU 2765 CG2 ILE A1148 9078 8209 9191 -468 -201 1103 C ATOM 2766 CD1 ILE A1148 28.303 20.606 276.719 1.00 70.88 C ANISOU 2766 CD1 ILE A1148 8946 8462 9524 -427 0 1021 C ATOM 2767 N PRO A 332 30.613 25.709 275.814 1.00 59.80 N ANISOU 2767 N PRO A 332 8098 6887 7734 -710 -337 1160 N ATOM 2768 CA PRO A 332 31.674 26.726 275.757 1.00 64.65 C ANISOU 2768 CA PRO A 332 8837 7479 8248 -847 -379 1206 C ATOM 2769 C PRO A 332 32.518 26.762 277.025 1.00 66.29 C ANISOU 2769 C PRO A 332 8986 7728 8473 -864 -344 1223 C ATOM 2770 O PRO A 332 32.033 26.502 278.127 1.00 67.98 O ANISOU 2770 O PRO A 332 9139 7939 8750 -750 -335 1209 O ATOM 2771 CB PRO A 332 30.899 28.037 275.568 1.00 63.28 C ANISOU 2771 CB PRO A 332 8870 7172 8002 -811 -522 1207 C ATOM 2772 CG PRO A 332 29.570 27.624 275.024 1.00 53.44 C ANISOU 2772 CG PRO A 332 7597 5904 6805 -678 -552 1154 C ATOM 2773 CD PRO A 332 29.276 26.307 275.654 1.00 54.65 C ANISOU 2773 CD PRO A 332 7536 6150 7078 -597 -438 1120 C ATOM 2774 N ASP A 333 33.798 27.111 276.851 1.00 65.03 N ANISOU 2774 N ASP A 333 8846 7614 8247 -1018 -324 1247 N ATOM 2775 CA ASP A 333 34.727 27.162 277.977 1.00 79.31 C ANISOU 2775 CA ASP A 333 10592 9477 10065 -1043 -299 1253 C ATOM 2776 C ASP A 333 34.189 28.023 279.113 1.00 80.26 C ANISOU 2776 C ASP A 333 10806 9508 10180 -959 -378 1261 C ATOM 2777 O ASP A 333 34.303 27.657 280.290 1.00 63.59 O ANISOU 2777 O ASP A 333 8609 7432 8120 -882 -352 1255 O ATOM 2778 CB ASP A 333 36.086 27.694 277.514 1.00 66.79 C ANISOU 2778 CB ASP A 333 9038 7951 8390 -1241 -284 1261 C ATOM 2779 CG ASP A 333 36.820 26.721 276.616 1.00 91.06 C ANISOU 2779 CG ASP A 333 11971 11152 11474 -1318 -189 1230 C ATOM 2780 OD1 ASP A 333 36.643 25.498 276.792 1.00 97.02 O ANISOU 2780 OD1 ASP A 333 12571 11967 12326 -1207 -128 1204 O ATOM 2781 OD2 ASP A 333 37.576 27.178 275.733 1.00 90.31 O ANISOU 2781 OD2 ASP A 333 11926 11100 11286 -1496 -174 1226 O ATOM 2782 N GLN A 334 33.596 29.173 278.780 1.00 68.25 N ANISOU 2782 N GLN A 334 9472 7868 8593 -965 -484 1269 N ATOM 2783 CA GLN A 334 33.179 30.117 279.810 1.00 52.28 C ANISOU 2783 CA GLN A 334 7550 5758 6555 -892 -572 1263 C ATOM 2784 C GLN A 334 32.084 29.531 280.689 1.00 61.94 C ANISOU 2784 C GLN A 334 8674 6991 7869 -704 -556 1223 C ATOM 2785 O GLN A 334 32.024 29.813 281.891 1.00 70.00 O ANISOU 2785 O GLN A 334 9688 8007 8901 -641 -572 1211 O ATOM 2786 CB GLN A 334 32.699 31.417 279.167 1.00 71.39 C ANISOU 2786 CB GLN A 334 10207 8032 8885 -918 -706 1271 C ATOM 2787 CG GLN A 334 32.393 32.526 280.172 1.00 67.13 C ANISOU 2787 CG GLN A 334 9795 7393 8320 -852 -813 1256 C ATOM 2788 CD GLN A 334 33.602 32.909 281.012 1.00 98.13 C ANISOU 2788 CD GLN A 334 13716 11357 12213 -967 -789 1279 C ATOM 2789 OE1 GLN A 334 33.468 33.262 282.185 1.00113.06 O ANISOU 2789 OE1 GLN A 334 15604 13232 14123 -887 -821 1256 O ATOM 2790 NE2 GLN A 334 34.791 32.838 280.418 1.00 95.84 N ANISOU 2790 NE2 GLN A 334 13414 11129 11870 -1159 -731 1311 N ATOM 2791 N ALA A 335 31.196 28.726 280.105 1.00 64.04 N ANISOU 2791 N ALA A 335 8865 7276 8192 -624 -521 1195 N ATOM 2792 CA ALA A 335 30.148 28.087 280.894 1.00 60.07 C ANISOU 2792 CA ALA A 335 8257 6799 7769 -475 -486 1147 C ATOM 2793 C ALA A 335 30.736 27.055 281.844 1.00 61.93 C ANISOU 2793 C ALA A 335 8346 7126 8057 -473 -377 1166 C ATOM 2794 O ALA A 335 30.381 27.011 283.027 1.00 69.93 O ANISOU 2794 O ALA A 335 9330 8151 9091 -397 -366 1149 O ATOM 2795 CB ALA A 335 29.115 27.439 279.974 1.00 64.42 C ANISOU 2795 CB ALA A 335 8755 7357 8366 -411 -471 1105 C ATOM 2796 N ARG A 336 31.638 26.210 281.344 1.00 51.83 N ANISOU 2796 N ARG A 336 6983 5914 6794 -553 -303 1196 N ATOM 2797 CA ARG A 336 32.256 25.210 282.207 1.00 62.85 C ANISOU 2797 CA ARG A 336 8260 7384 8235 -537 -221 1211 C ATOM 2798 C ARG A 336 33.134 25.869 283.261 1.00 67.92 C ANISOU 2798 C ARG A 336 8938 8036 8833 -565 -254 1231 C ATOM 2799 O ARG A 336 33.149 25.439 284.420 1.00 75.22 O ANISOU 2799 O ARG A 336 9816 8985 9779 -501 -226 1235 O ATOM 2800 CB ARG A 336 33.072 24.220 281.375 1.00 68.14 C ANISOU 2800 CB ARG A 336 8834 8125 8932 -600 -153 1219 C ATOM 2801 CG ARG A 336 32.373 23.721 280.120 1.00 63.46 C ANISOU 2801 CG ARG A 336 8221 7523 8367 -598 -130 1197 C ATOM 2802 CD ARG A 336 33.074 22.499 279.536 1.00 59.37 C ANISOU 2802 CD ARG A 336 7585 7081 7892 -629 -52 1190 C ATOM 2803 NE ARG A 336 34.500 22.720 279.309 1.00 62.68 N ANISOU 2803 NE ARG A 336 7982 7568 8266 -734 -50 1195 N ATOM 2804 CZ ARG A 336 35.019 23.238 278.199 1.00 65.57 C ANISOU 2804 CZ ARG A 336 8386 7959 8570 -854 -61 1188 C ATOM 2805 NH1 ARG A 336 34.237 23.605 277.193 1.00 61.69 N ANISOU 2805 NH1 ARG A 336 7974 7414 8050 -874 -89 1187 N ATOM 2806 NH2 ARG A 336 36.332 23.394 278.093 1.00 64.75 N ANISOU 2806 NH2 ARG A 336 8240 7941 8423 -961 -46 1175 N ATOM 2807 N MET A 337 33.864 26.920 282.882 1.00 60.80 N ANISOU 2807 N MET A 337 8129 7113 7861 -671 -315 1242 N ATOM 2808 CA MET A 337 34.733 27.593 283.840 1.00 63.38 C ANISOU 2808 CA MET A 337 8486 7452 8143 -712 -350 1252 C ATOM 2809 C MET A 337 33.922 28.286 284.924 1.00 67.91 C ANISOU 2809 C MET A 337 9135 7960 8707 -614 -408 1238 C ATOM 2810 O MET A 337 34.310 28.278 286.096 1.00 65.79 O ANISOU 2810 O MET A 337 8840 7722 8434 -583 -405 1239 O ATOM 2811 CB MET A 337 35.627 28.597 283.120 1.00 71.72 C ANISOU 2811 CB MET A 337 9637 8494 9119 -873 -397 1261 C ATOM 2812 CG MET A 337 36.740 29.173 283.992 1.00105.26 C ANISOU 2812 CG MET A 337 13890 12781 13323 -946 -421 1258 C ATOM 2813 SD MET A 337 37.168 30.875 283.549 1.00122.91 S ANISOU 2813 SD MET A 337 16330 14924 15446 -1113 -516 1267 S ATOM 2814 CE MET A 337 35.672 31.745 284.026 1.00120.32 C ANISOU 2814 CE MET A 337 16162 14438 15115 -967 -620 1263 C ATOM 2815 N ASP A 338 32.795 28.896 284.556 1.00 49.91 N ANISOU 2815 N ASP A 338 6947 5596 6420 -557 -466 1213 N ATOM 2816 CA ASP A 338 31.945 29.525 285.558 1.00 51.97 C ANISOU 2816 CA ASP A 338 7261 5810 6675 -449 -521 1175 C ATOM 2817 C ASP A 338 31.351 28.503 286.515 1.00 74.98 C ANISOU 2817 C ASP A 338 10054 8790 9644 -347 -437 1157 C ATOM 2818 O ASP A 338 31.055 28.839 287.667 1.00 71.64 O ANISOU 2818 O ASP A 338 9646 8370 9206 -283 -453 1132 O ATOM 2819 CB ASP A 338 30.833 30.316 284.880 1.00 59.99 C ANISOU 2819 CB ASP A 338 8387 6731 7676 -389 -612 1131 C ATOM 2820 CG ASP A 338 31.212 31.755 284.637 1.00 87.85 C ANISOU 2820 CG ASP A 338 12103 10152 11123 -454 -736 1139 C ATOM 2821 OD1 ASP A 338 32.424 32.050 284.587 1.00 84.67 O ANISOU 2821 OD1 ASP A 338 11737 9760 10675 -591 -732 1185 O ATOM 2822 OD2 ASP A 338 30.297 32.592 284.501 1.00 88.37 O ANISOU 2822 OD2 ASP A 338 12284 10123 11169 -368 -842 1091 O ATOM 2823 N ILE A 339 31.167 27.262 286.063 1.00 58.16 N ANISOU 2823 N ILE A 339 7816 6711 7571 -339 -347 1168 N ATOM 2824 CA ILE A 339 30.583 26.231 286.915 1.00 56.35 C ANISOU 2824 CA ILE A 339 7496 6531 7384 -266 -261 1157 C ATOM 2825 C ILE A 339 31.612 25.687 287.892 1.00 62.14 C ANISOU 2825 C ILE A 339 8192 7314 8105 -284 -223 1203 C ATOM 2826 O ILE A 339 31.307 25.464 289.069 1.00 47.54 O ANISOU 2826 O ILE A 339 6337 5484 6242 -231 -196 1199 O ATOM 2827 CB ILE A 339 29.984 25.108 286.049 1.00 64.46 C ANISOU 2827 CB ILE A 339 8440 7579 8474 -258 -186 1148 C ATOM 2828 CG1 ILE A 339 28.728 25.606 285.330 1.00 65.77 C ANISOU 2828 CG1 ILE A 339 8631 7708 8651 -208 -230 1081 C ATOM 2829 CG2 ILE A 339 29.654 23.860 286.899 1.00 47.78 C ANISOU 2829 CG2 ILE A 339 6249 5511 6395 -222 -85 1156 C ATOM 2830 CD1 ILE A 339 28.289 24.713 284.205 1.00 65.63 C ANISOU 2830 CD1 ILE A 339 8546 7705 8687 -218 -179 1069 C ATOM 2831 N GLU A 340 32.837 25.435 287.429 1.00 60.24 N ANISOU 2831 N GLU A 340 7925 7102 7863 -358 -222 1239 N ATOM 2832 CA GLU A 340 33.857 24.941 288.346 1.00 72.78 C ANISOU 2832 CA GLU A 340 9474 8742 9438 -356 -207 1267 C ATOM 2833 C GLU A 340 34.289 26.023 289.327 1.00 69.73 C ANISOU 2833 C GLU A 340 9155 8349 8989 -362 -276 1261 C ATOM 2834 O GLU A 340 34.607 25.717 290.481 1.00 74.42 O ANISOU 2834 O GLU A 340 9740 8973 9563 -318 -270 1273 O ATOM 2835 CB GLU A 340 35.057 24.401 287.571 1.00 68.73 C ANISOU 2835 CB GLU A 340 8891 8282 8941 -422 -193 1278 C ATOM 2836 CG GLU A 340 35.896 25.445 286.859 1.00103.03 C ANISOU 2836 CG GLU A 340 13270 12636 13242 -536 -247 1265 C ATOM 2837 CD GLU A 340 37.254 24.912 286.460 1.00126.30 C ANISOU 2837 CD GLU A 340 16121 15674 16194 -600 -229 1253 C ATOM 2838 OE1 GLU A 340 37.604 23.791 286.890 1.00122.31 O ANISOU 2838 OE1 GLU A 340 15532 15214 15726 -531 -196 1254 O ATOM 2839 OE2 GLU A 340 37.972 25.615 285.718 1.00136.39 O ANISOU 2839 OE2 GLU A 340 17411 16980 17432 -722 -251 1236 O ATOM 2840 N LEU A 341 34.304 27.286 288.898 1.00 62.53 N ANISOU 2840 N LEU A 341 8327 7390 8040 -416 -348 1242 N ATOM 2841 CA LEU A 341 34.538 28.372 289.843 1.00 54.92 C ANISOU 2841 CA LEU A 341 7444 6405 7020 -415 -420 1227 C ATOM 2842 C LEU A 341 33.439 28.421 290.894 1.00 62.63 C ANISOU 2842 C LEU A 341 8440 7365 7990 -305 -413 1199 C ATOM 2843 O LEU A 341 33.718 28.581 292.087 1.00 79.21 O ANISOU 2843 O LEU A 341 10552 9491 10054 -274 -426 1197 O ATOM 2844 CB LEU A 341 34.631 29.709 289.107 1.00 69.71 C ANISOU 2844 CB LEU A 341 9432 8203 8850 -496 -506 1213 C ATOM 2845 CG LEU A 341 35.936 30.062 288.388 1.00 74.49 C ANISOU 2845 CG LEU A 341 10046 8834 9423 -647 -523 1229 C ATOM 2846 CD1 LEU A 341 35.837 31.466 287.812 1.00 68.07 C ANISOU 2846 CD1 LEU A 341 9397 7917 8550 -730 -615 1221 C ATOM 2847 CD2 LEU A 341 37.125 29.960 289.321 1.00 63.25 C ANISOU 2847 CD2 LEU A 341 8561 7491 7978 -678 -522 1226 C ATOM 2848 N ALA A 342 32.183 28.282 290.474 1.00 53.33 N ANISOU 2848 N ALA A 342 7260 6159 6844 -247 -391 1167 N ATOM 2849 CA ALA A 342 31.092 28.261 291.440 1.00 49.24 C ANISOU 2849 CA ALA A 342 6738 5653 6319 -153 -368 1120 C ATOM 2850 C ALA A 342 31.166 27.022 292.324 1.00 64.65 C ANISOU 2850 C ALA A 342 8621 7670 8274 -132 -272 1154 C ATOM 2851 O ALA A 342 30.965 27.111 293.541 1.00 76.95 O ANISOU 2851 O ALA A 342 10196 9255 9787 -91 -261 1139 O ATOM 2852 CB ALA A 342 29.751 28.329 290.714 1.00 52.78 C ANISOU 2852 CB ALA A 342 7176 6076 6802 -100 -366 1058 C ATOM 2853 N LYS A 343 31.459 25.859 291.735 1.00 72.49 N ANISOU 2853 N LYS A 343 9549 8682 9312 -160 -205 1198 N ATOM 2854 CA LYS A 343 31.589 24.640 292.529 1.00 70.03 C ANISOU 2854 CA LYS A 343 9205 8408 8997 -141 -129 1239 C ATOM 2855 C LYS A 343 32.739 24.751 293.523 1.00 58.10 C ANISOU 2855 C LYS A 343 7721 6920 7432 -139 -171 1274 C ATOM 2856 O LYS A 343 32.603 24.360 294.689 1.00 60.24 O ANISOU 2856 O LYS A 343 8019 7211 7657 -103 -143 1289 O ATOM 2857 CB LYS A 343 31.786 23.431 291.611 1.00 63.66 C ANISOU 2857 CB LYS A 343 8337 7600 8252 -165 -71 1272 C ATOM 2858 CG LYS A 343 30.495 22.901 291.002 1.00 67.92 C ANISOU 2858 CG LYS A 343 8839 8129 8838 -157 -1 1238 C ATOM 2859 CD LYS A 343 30.748 21.718 290.071 1.00 72.41 C ANISOU 2859 CD LYS A 343 9353 8692 9467 -182 49 1267 C ATOM 2860 CE LYS A 343 29.441 21.118 289.552 1.00 93.96 C ANISOU 2860 CE LYS A 343 12042 11417 12242 -181 123 1226 C ATOM 2861 NZ LYS A 343 28.637 20.480 290.637 1.00109.70 N ANISOU 2861 NZ LYS A 343 14048 13424 14207 -173 204 1220 N ATOM 2862 N THR A 344 33.877 25.292 293.084 1.00 58.95 N ANISOU 2862 N THR A 344 7826 7033 7538 -186 -238 1282 N ATOM 2863 CA THR A 344 35.032 25.403 293.968 1.00 62.79 C ANISOU 2863 CA THR A 344 8321 7558 7978 -184 -286 1299 C ATOM 2864 C THR A 344 34.730 26.301 295.161 1.00 73.91 C ANISOU 2864 C THR A 344 9799 8963 9319 -152 -326 1273 C ATOM 2865 O THR A 344 35.112 25.989 296.294 1.00 62.14 O ANISOU 2865 O THR A 344 8327 7504 7780 -113 -332 1291 O ATOM 2866 CB THR A 344 36.239 25.937 293.195 1.00 61.37 C ANISOU 2866 CB THR A 344 8111 7401 7806 -263 -343 1288 C ATOM 2867 OG1 THR A 344 36.506 25.090 292.071 1.00 66.04 O ANISOU 2867 OG1 THR A 344 8629 8008 8455 -291 -301 1299 O ATOM 2868 CG2 THR A 344 37.476 25.989 294.080 1.00 44.57 C ANISOU 2868 CG2 THR A 344 5967 5332 5636 -259 -395 1286 C ATOM 2869 N LEU A 345 34.042 27.422 294.931 1.00 69.70 N ANISOU 2869 N LEU A 345 9314 8390 8779 -159 -363 1227 N ATOM 2870 CA LEU A 345 33.784 28.353 296.024 1.00 62.75 C ANISOU 2870 CA LEU A 345 8500 7507 7837 -123 -411 1187 C ATOM 2871 C LEU A 345 32.895 27.726 297.090 1.00 69.71 C ANISOU 2871 C LEU A 345 9381 8422 8683 -56 -340 1180 C ATOM 2872 O LEU A 345 33.141 27.891 298.291 1.00 59.07 O ANISOU 2872 O LEU A 345 8070 7106 7269 -29 -357 1177 O ATOM 2873 CB LEU A 345 33.153 29.637 295.486 1.00 47.37 C ANISOU 2873 CB LEU A 345 6614 5494 5891 -128 -478 1128 C ATOM 2874 CG LEU A 345 34.067 30.566 294.684 1.00 54.23 C ANISOU 2874 CG LEU A 345 7532 6316 6757 -218 -562 1132 C ATOM 2875 CD1 LEU A 345 33.292 31.791 294.200 1.00 55.52 C ANISOU 2875 CD1 LEU A 345 7794 6387 6912 -205 -642 1077 C ATOM 2876 CD2 LEU A 345 35.294 31.008 295.496 1.00 64.50 C ANISOU 2876 CD2 LEU A 345 8850 7650 8007 -261 -615 1138 C ATOM 2877 N VAL A 346 31.860 26.992 296.678 1.00 54.54 N ANISOU 2877 N VAL A 346 7421 6501 6799 -41 -257 1172 N ATOM 2878 CA VAL A 346 30.954 26.410 297.660 1.00 66.00 C ANISOU 2878 CA VAL A 346 8876 7994 8208 -7 -174 1157 C ATOM 2879 C VAL A 346 31.679 25.368 298.499 1.00 72.49 C ANISOU 2879 C VAL A 346 9721 8839 8983 -11 -140 1234 C ATOM 2880 O VAL A 346 31.349 25.163 299.674 1.00 69.09 O ANISOU 2880 O VAL A 346 9335 8443 8475 6 -102 1234 O ATOM 2881 CB VAL A 346 29.722 25.815 296.958 1.00 59.17 C ANISOU 2881 CB VAL A 346 7954 7132 7394 -10 -88 1122 C ATOM 2882 CG1 VAL A 346 28.746 25.217 297.976 1.00 64.99 C ANISOU 2882 CG1 VAL A 346 8691 7927 8076 -5 14 1094 C ATOM 2883 CG2 VAL A 346 29.036 26.882 296.129 1.00 53.59 C ANISOU 2883 CG2 VAL A 346 7237 6398 6728 16 -148 1038 C ATOM 2884 N LEU A 347 32.679 24.702 297.925 1.00 53.29 N ANISOU 2884 N LEU A 347 7267 6391 6591 -29 -158 1296 N ATOM 2885 CA LEU A 347 33.445 23.732 298.696 1.00 71.24 C ANISOU 2885 CA LEU A 347 9575 8674 8820 -9 -155 1361 C ATOM 2886 C LEU A 347 34.315 24.432 299.734 1.00 71.46 C ANISOU 2886 C LEU A 347 9646 8732 8773 17 -241 1356 C ATOM 2887 O LEU A 347 34.352 24.023 300.900 1.00 72.35 O ANISOU 2887 O LEU A 347 9826 8862 8803 48 -232 1384 O ATOM 2888 CB LEU A 347 34.291 22.880 297.752 1.00 75.20 C ANISOU 2888 CB LEU A 347 10025 9158 9390 -16 -167 1402 C ATOM 2889 CG LEU A 347 34.636 21.459 298.193 1.00 79.52 C ANISOU 2889 CG LEU A 347 10612 9685 9916 18 -142 1466 C ATOM 2890 CD1 LEU A 347 35.060 20.651 296.974 1.00 95.10 C ANISOU 2890 CD1 LEU A 347 12517 11636 11979 11 -134 1479 C ATOM 2891 CD2 LEU A 347 35.734 21.460 299.245 1.00 71.98 C ANISOU 2891 CD2 LEU A 347 9705 8754 8889 70 -227 1488 C ATOM 2892 N ILE A 348 35.011 25.498 299.330 1.00 69.46 N ANISOU 2892 N ILE A 348 9367 8485 8541 -4 -324 1320 N ATOM 2893 CA ILE A 348 35.766 26.305 300.285 1.00 77.35 C ANISOU 2893 CA ILE A 348 10403 9514 9471 10 -408 1298 C ATOM 2894 C ILE A 348 34.862 26.748 301.425 1.00 69.67 C ANISOU 2894 C ILE A 348 9498 8555 8419 43 -385 1267 C ATOM 2895 O ILE A 348 35.235 26.677 302.602 1.00 70.72 O ANISOU 2895 O ILE A 348 9682 8720 8467 76 -411 1279 O ATOM 2896 CB ILE A 348 36.399 27.522 299.584 1.00 77.08 C ANISOU 2896 CB ILE A 348 10346 9472 9469 -47 -488 1252 C ATOM 2897 CG1 ILE A 348 37.250 27.094 298.379 1.00 78.69 C ANISOU 2897 CG1 ILE A 348 10473 9684 9744 -99 -494 1270 C ATOM 2898 CG2 ILE A 348 37.224 28.341 300.578 1.00 65.38 C ANISOU 2898 CG2 ILE A 348 8899 8024 7919 -43 -575 1222 C ATOM 2899 CD1 ILE A 348 38.546 26.371 298.728 1.00 83.50 C ANISOU 2899 CD1 ILE A 348 11034 10352 10340 -76 -534 1286 C ATOM 2900 N LEU A 349 33.661 27.220 301.089 1.00 60.54 N ANISOU 2900 N LEU A 349 8337 7381 7285 38 -340 1216 N ATOM 2901 CA LEU A 349 32.740 27.722 302.102 1.00 65.71 C ANISOU 2901 CA LEU A 349 9034 8066 7867 71 -316 1158 C ATOM 2902 C LEU A 349 32.312 26.618 303.062 1.00 73.37 C ANISOU 2902 C LEU A 349 10040 9075 8761 78 -223 1200 C ATOM 2903 O LEU A 349 32.368 26.792 304.285 1.00 73.81 O ANISOU 2903 O LEU A 349 10157 9172 8717 99 -231 1191 O ATOM 2904 CB LEU A 349 31.521 28.344 301.424 1.00 53.15 C ANISOU 2904 CB LEU A 349 7412 6458 6324 79 -293 1076 C ATOM 2905 CG LEU A 349 30.411 28.838 302.351 1.00 51.67 C ANISOU 2905 CG LEU A 349 7240 6322 6072 120 -258 983 C ATOM 2906 CD1 LEU A 349 30.940 29.871 303.330 1.00 56.71 C ANISOU 2906 CD1 LEU A 349 7939 6972 6638 150 -348 943 C ATOM 2907 CD2 LEU A 349 29.272 29.413 301.529 1.00 55.18 C ANISOU 2907 CD2 LEU A 349 7638 6750 6577 148 -257 886 C ATOM 2908 N VAL A 350 31.869 25.476 302.529 1.00 61.00 N ANISOU 2908 N VAL A 350 8452 7493 7233 52 -134 1245 N ATOM 2909 CA VAL A 350 31.370 24.405 303.389 1.00 64.84 C ANISOU 2909 CA VAL A 350 8999 8000 7637 35 -38 1289 C ATOM 2910 C VAL A 350 32.471 23.919 304.319 1.00 67.90 C ANISOU 2910 C VAL A 350 9474 8382 7942 62 -96 1366 C ATOM 2911 O VAL A 350 32.231 23.649 305.503 1.00 53.15 O ANISOU 2911 O VAL A 350 7695 6543 5955 60 -62 1383 O ATOM 2912 CB VAL A 350 30.790 23.257 302.541 1.00 61.67 C ANISOU 2912 CB VAL A 350 8567 7567 7300 -9 57 1325 C ATOM 2913 CG1 VAL A 350 30.469 22.040 303.414 1.00 56.89 C ANISOU 2913 CG1 VAL A 350 8058 6959 6600 -47 148 1390 C ATOM 2914 CG2 VAL A 350 29.534 23.727 301.824 1.00 69.61 C ANISOU 2914 CG2 VAL A 350 9487 8597 8367 -27 117 1230 C ATOM 2915 N VAL A 351 33.698 23.806 303.804 1.00 66.44 N ANISOU 2915 N VAL A 351 9265 8168 7811 89 -188 1405 N ATOM 2916 CA VAL A 351 34.813 23.389 304.650 1.00 67.82 C ANISOU 2916 CA VAL A 351 9510 8346 7912 136 -267 1458 C ATOM 2917 C VAL A 351 35.051 24.421 305.742 1.00 70.73 C ANISOU 2917 C VAL A 351 9918 8766 8191 160 -330 1412 C ATOM 2918 O VAL A 351 35.341 24.074 306.893 1.00 82.87 O ANISOU 2918 O VAL A 351 11552 10319 9614 192 -353 1447 O ATOM 2919 CB VAL A 351 36.077 23.152 303.799 1.00 70.47 C ANISOU 2919 CB VAL A 351 9776 8666 8333 163 -355 1475 C ATOM 2920 CG1 VAL A 351 37.312 22.958 304.692 1.00 43.21 C ANISOU 2920 CG1 VAL A 351 6373 5238 4809 231 -466 1496 C ATOM 2921 CG2 VAL A 351 35.877 21.938 302.891 1.00 72.23 C ANISOU 2921 CG2 VAL A 351 9981 8836 8628 153 -295 1524 C ATOM 2922 N LEU A 352 34.906 25.705 305.406 1.00 66.81 N ANISOU 2922 N LEU A 352 9362 8288 7736 147 -364 1333 N ATOM 2923 CA LEU A 352 35.140 26.753 306.392 1.00 67.47 C ANISOU 2923 CA LEU A 352 9482 8412 7740 169 -431 1277 C ATOM 2924 C LEU A 352 34.074 26.734 307.479 1.00 60.66 C ANISOU 2924 C LEU A 352 8690 7591 6768 171 -351 1253 C ATOM 2925 O LEU A 352 34.370 26.998 308.649 1.00 69.07 O ANISOU 2925 O LEU A 352 9824 8696 7723 198 -390 1244 O ATOM 2926 CB LEU A 352 35.187 28.117 305.705 1.00 72.47 C ANISOU 2926 CB LEU A 352 10059 9033 8445 149 -492 1197 C ATOM 2927 CG LEU A 352 35.419 29.291 306.653 1.00 71.05 C ANISOU 2927 CG LEU A 352 9921 8883 8192 169 -570 1129 C ATOM 2928 CD1 LEU A 352 36.486 30.215 306.094 1.00 71.93 C ANISOU 2928 CD1 LEU A 352 9999 8974 8357 137 -681 1098 C ATOM 2929 CD2 LEU A 352 34.117 30.040 306.879 1.00 65.86 C ANISOU 2929 CD2 LEU A 352 9276 8232 7515 181 -524 1043 C ATOM 2930 N ILE A 353 32.830 26.413 307.116 1.00 65.61 N ANISOU 2930 N ILE A 353 9292 8219 7416 136 -236 1232 N ATOM 2931 CA ILE A 353 31.766 26.332 308.111 1.00 61.25 C ANISOU 2931 CA ILE A 353 8790 7729 6755 118 -139 1192 C ATOM 2932 C ILE A 353 31.952 25.103 308.987 1.00 81.08 C ANISOU 2932 C ILE A 353 11417 10240 9150 96 -90 1290 C ATOM 2933 O ILE A 353 31.635 25.130 310.182 1.00105.64 O ANISOU 2933 O ILE A 353 14610 13406 12122 86 -55 1277 O ATOM 2934 CB ILE A 353 30.387 26.324 307.426 1.00 62.16 C ANISOU 2934 CB ILE A 353 8825 7862 6929 82 -30 1120 C ATOM 2935 CG1 ILE A 353 30.198 27.594 306.594 1.00 64.54 C ANISOU 2935 CG1 ILE A 353 9043 8147 7332 120 -104 1022 C ATOM 2936 CG2 ILE A 353 29.279 26.207 308.462 1.00 57.56 C ANISOU 2936 CG2 ILE A 353 8273 7370 6226 47 84 1059 C ATOM 2937 CD1 ILE A 353 28.945 27.593 305.740 1.00 64.38 C ANISOU 2937 CD1 ILE A 353 8936 8140 7387 107 -26 945 C ATOM 2938 N ILE A 354 32.465 24.010 308.420 1.00 79.91 N ANISOU 2938 N ILE A 354 11290 10025 9048 90 -91 1388 N ATOM 2939 CA ILE A 354 32.599 22.777 309.188 1.00 70.20 C ANISOU 2939 CA ILE A 354 10202 8766 7705 73 -56 1488 C ATOM 2940 C ILE A 354 33.683 22.927 310.243 1.00 68.65 C ANISOU 2940 C ILE A 354 10103 8580 7403 140 -176 1522 C ATOM 2941 O ILE A 354 33.537 22.452 311.375 1.00 90.15 O ANISOU 2941 O ILE A 354 12968 11314 9971 125 -149 1566 O ATOM 2942 CB ILE A 354 32.875 21.590 308.242 1.00 69.09 C ANISOU 2942 CB ILE A 354 10062 8538 7650 65 -44 1570 C ATOM 2943 CG1 ILE A 354 31.573 21.159 307.556 1.00 66.15 C ANISOU 2943 CG1 ILE A 354 9640 8165 7331 -23 104 1545 C ATOM 2944 CG2 ILE A 354 33.506 20.407 308.989 1.00 64.93 C ANISOU 2944 CG2 ILE A 354 9706 7948 7015 89 -81 1682 C ATOM 2945 CD1 ILE A 354 31.742 20.084 306.491 1.00 67.19 C ANISOU 2945 CD1 ILE A 354 9756 8210 7562 -34 120 1609 C ATOM 2946 N CYS A 355 34.774 23.608 309.905 1.00 63.79 N ANISOU 2946 N CYS A 355 9414 7966 6859 206 -308 1495 N ATOM 2947 CA CYS A 355 35.921 23.685 310.799 1.00 89.28 C ANISOU 2947 CA CYS A 355 12713 11208 10000 278 -437 1517 C ATOM 2948 C CYS A 355 35.804 24.827 311.800 1.00104.57 C ANISOU 2948 C CYS A 355 14667 13220 11844 286 -466 1441 C ATOM 2949 O CYS A 355 35.984 24.626 313.006 1.00104.05 O ANISOU 2949 O CYS A 355 14726 13181 11629 310 -493 1467 O ATOM 2950 CB CYS A 355 37.199 23.853 309.982 1.00 82.24 C ANISOU 2950 CB CYS A 355 11720 10304 9225 332 -562 1506 C ATOM 2951 SG CYS A 355 37.495 22.512 308.807 1.00 88.11 S ANISOU 2951 SG CYS A 355 12434 10968 10078 343 -547 1578 S ATOM 2952 N TRP A 356 35.525 26.030 311.310 1.00 95.49 N ANISOU 2952 N TRP A 356 13407 12099 10776 270 -472 1344 N ATOM 2953 CA TRP A 356 35.465 27.203 312.164 1.00 79.14 C ANISOU 2953 CA TRP A 356 11347 10089 8633 286 -515 1257 C ATOM 2954 C TRP A 356 34.089 27.431 312.768 1.00 74.70 C ANISOU 2954 C TRP A 356 10815 9580 7989 247 -393 1199 C ATOM 2955 O TRP A 356 33.977 28.160 313.760 1.00 76.53 O ANISOU 2955 O TRP A 356 11085 9872 8119 265 -416 1133 O ATOM 2956 CB TRP A 356 35.882 28.439 311.372 1.00 59.46 C ANISOU 2956 CB TRP A 356 8746 7586 6261 287 -597 1175 C ATOM 2957 CG TRP A 356 37.352 28.648 311.347 1.00 62.77 C ANISOU 2957 CG TRP A 356 9143 8006 6702 318 -735 1183 C ATOM 2958 CD1 TRP A 356 38.236 28.151 310.439 1.00 70.66 C ANISOU 2958 CD1 TRP A 356 10075 8976 7796 318 -781 1224 C ATOM 2959 CD2 TRP A 356 38.117 29.417 312.277 1.00 71.28 C ANISOU 2959 CD2 TRP A 356 10249 9131 7703 351 -843 1132 C ATOM 2960 NE1 TRP A 356 39.510 28.564 310.744 1.00 63.93 N ANISOU 2960 NE1 TRP A 356 9198 8161 6933 345 -909 1193 N ATOM 2961 CE2 TRP A 356 39.464 29.344 311.869 1.00 79.58 C ANISOU 2961 CE2 TRP A 356 11241 10186 8811 364 -951 1139 C ATOM 2962 CE3 TRP A 356 37.795 30.161 313.415 1.00 65.71 C ANISOU 2962 CE3 TRP A 356 9607 8473 6885 369 -859 1069 C ATOM 2963 CZ2 TRP A 356 40.487 29.986 312.560 1.00 80.32 C ANISOU 2963 CZ2 TRP A 356 11333 10330 8855 390 -1075 1085 C ATOM 2964 CZ3 TRP A 356 38.811 30.798 314.098 1.00 76.78 C ANISOU 2964 CZ3 TRP A 356 11020 9915 8237 399 -984 1024 C ATOM 2965 CH2 TRP A 356 40.141 30.706 313.669 1.00 90.70 C ANISOU 2965 CH2 TRP A 356 12720 11681 10061 407 -1091 1033 C ATOM 2966 N GLY A 357 33.048 26.833 312.198 1.00 68.22 N ANISOU 2966 N GLY A 357 9965 8748 7206 192 -264 1208 N ATOM 2967 CA GLY A 357 31.712 26.962 312.722 1.00 71.02 C ANISOU 2967 CA GLY A 357 10325 9176 7484 146 -136 1135 C ATOM 2968 C GLY A 357 31.618 26.612 314.193 1.00 74.45 C ANISOU 2968 C GLY A 357 10894 9673 7721 126 -99 1157 C ATOM 2969 O GLY A 357 31.229 27.442 315.020 1.00 87.38 O ANISOU 2969 O GLY A 357 12536 11393 9273 137 -93 1059 O ATOM 2970 N PRO A 358 31.964 25.370 314.551 1.00 77.23 N ANISOU 2970 N PRO A 358 11374 9982 7989 98 -76 1285 N ATOM 2971 CA PRO A 358 31.851 24.963 315.964 1.00 77.69 C ANISOU 2971 CA PRO A 358 11596 10089 7835 66 -39 1321 C ATOM 2972 C PRO A 358 32.507 25.933 316.933 1.00 91.35 C ANISOU 2972 C PRO A 358 13355 11875 9478 138 -154 1264 C ATOM 2973 O PRO A 358 31.907 26.273 317.962 1.00 79.88 O ANISOU 2973 O PRO A 358 11956 10515 7879 105 -91 1202 O ATOM 2974 CB PRO A 358 32.533 23.587 315.986 1.00 67.02 C ANISOU 2974 CB PRO A 358 10390 8636 6439 65 -70 1479 C ATOM 2975 CG PRO A 358 33.302 23.500 314.701 1.00 77.96 C ANISOU 2975 CG PRO A 358 11665 9939 8017 127 -162 1506 C ATOM 2976 CD PRO A 358 32.514 24.286 313.722 1.00 74.56 C ANISOU 2976 CD PRO A 358 11057 9541 7733 99 -97 1401 C ATOM 2977 N LEU A 359 33.724 26.393 316.633 1.00 90.06 N ANISOU 2977 N LEU A 359 13152 11669 9398 227 -316 1274 N ATOM 2978 CA LEU A 359 34.376 27.362 317.507 1.00 78.40 C ANISOU 2978 CA LEU A 359 11693 10245 7849 289 -431 1209 C ATOM 2979 C LEU A 359 33.536 28.626 317.642 1.00 78.47 C ANISOU 2979 C LEU A 359 11613 10331 7873 280 -390 1056 C ATOM 2980 O LEU A 359 33.393 29.172 318.742 1.00 86.92 O ANISOU 2980 O LEU A 359 12739 11480 8808 291 -398 991 O ATOM 2981 CB LEU A 359 35.770 27.696 316.977 1.00 79.75 C ANISOU 2981 CB LEU A 359 11803 10368 8130 364 -600 1221 C ATOM 2982 CG LEU A 359 36.570 28.660 317.862 1.00 92.85 C ANISOU 2982 CG LEU A 359 13480 12081 9719 423 -732 1152 C ATOM 2983 CD1 LEU A 359 37.674 27.922 318.615 1.00 94.13 C ANISOU 2983 CD1 LEU A 359 13756 12236 9772 487 -846 1235 C ATOM 2984 CD2 LEU A 359 37.132 29.797 317.027 1.00 93.92 C ANISOU 2984 CD2 LEU A 359 13475 12199 10011 437 -825 1067 C ATOM 2985 N LEU A 360 32.970 29.105 316.533 1.00 74.24 N ANISOU 2985 N LEU A 360 10944 9770 7493 268 -355 992 N ATOM 2986 CA LEU A 360 32.099 30.273 316.595 1.00 71.63 C ANISOU 2986 CA LEU A 360 10534 9499 7182 279 -329 836 C ATOM 2987 C LEU A 360 30.903 30.019 317.504 1.00 82.10 C ANISOU 2987 C LEU A 360 11898 10937 8360 227 -181 775 C ATOM 2988 O LEU A 360 30.509 30.893 318.284 1.00 84.30 O ANISOU 2988 O LEU A 360 12171 11300 8560 253 -185 650 O ATOM 2989 CB LEU A 360 31.632 30.657 315.190 1.00 66.97 C ANISOU 2989 CB LEU A 360 9817 8852 6777 279 -320 789 C ATOM 2990 CG LEU A 360 32.715 31.193 314.253 1.00 77.16 C ANISOU 2990 CG LEU A 360 11062 10048 8208 312 -460 815 C ATOM 2991 CD1 LEU A 360 32.160 31.404 312.851 1.00 87.16 C ANISOU 2991 CD1 LEU A 360 12229 11254 9634 300 -437 785 C ATOM 2992 CD2 LEU A 360 33.309 32.492 314.787 1.00 91.47 C ANISOU 2992 CD2 LEU A 360 12888 11867 9998 359 -590 725 C ATOM 2993 N ALA A 361 30.309 28.827 317.417 1.00 73.11 N ANISOU 2993 N ALA A 361 10798 9803 7177 144 -45 853 N ATOM 2994 CA ALA A 361 29.207 28.496 318.311 1.00 72.02 C ANISOU 2994 CA ALA A 361 10702 9784 6878 62 113 797 C ATOM 2995 C ALA A 361 29.646 28.531 319.768 1.00 81.79 C ANISOU 2995 C ALA A 361 12085 11082 7909 63 84 816 C ATOM 2996 O ALA A 361 28.866 28.926 320.642 1.00 89.39 O ANISOU 2996 O ALA A 361 13050 12172 8741 30 169 703 O ATOM 2997 CB ALA A 361 28.640 27.121 317.963 1.00 59.52 C ANISOU 2997 CB ALA A 361 9162 8177 5274 -51 257 897 C ATOM 2998 N ILE A 362 30.883 28.121 320.050 1.00 77.12 N ANISOU 2998 N ILE A 362 11611 10411 7280 106 -39 946 N ATOM 2999 CA ILE A 362 31.393 28.205 321.414 1.00 91.01 C ANISOU 2999 CA ILE A 362 13514 12223 8844 125 -94 962 C ATOM 3000 C ILE A 362 31.481 29.659 321.851 1.00 89.10 C ANISOU 3000 C ILE A 362 13194 12052 8608 200 -178 806 C ATOM 3001 O ILE A 362 31.117 30.006 322.981 1.00 75.50 O ANISOU 3001 O ILE A 362 11532 10438 6717 185 -140 731 O ATOM 3002 CB ILE A 362 32.755 27.491 321.520 1.00 87.00 C ANISOU 3002 CB ILE A 362 13131 11612 8314 181 -235 1117 C ATOM 3003 CG1 ILE A 362 32.572 25.985 321.297 1.00 86.31 C ANISOU 3003 CG1 ILE A 362 13164 11448 8181 106 -150 1268 C ATOM 3004 CG2 ILE A 362 33.414 27.762 322.880 1.00 59.94 C ANISOU 3004 CG2 ILE A 362 9839 8238 4698 228 -331 1117 C ATOM 3005 CD1 ILE A 362 33.871 25.214 321.177 1.00 89.32 C ANISOU 3005 CD1 ILE A 362 13648 11714 8574 185 -302 1406 C ATOM 3006 N AMET A 363 31.963 30.536 320.967 0.50 79.63 N ANISOU 3006 N AMET A 363 11871 10791 7594 274 -293 752 N ATOM 3007 N BMET A 363 31.954 30.534 320.962 0.50 79.60 N ANISOU 3007 N BMET A 363 11866 10787 7591 274 -292 751 N ATOM 3008 CA AMET A 363 32.059 31.949 321.315 0.50 81.35 C ANISOU 3008 CA AMET A 363 12031 11051 7826 343 -385 602 C ATOM 3009 CA BMET A 363 32.066 31.946 321.305 0.50 81.28 C ANISOU 3009 CA BMET A 363 12022 11042 7819 343 -385 603 C ATOM 3010 C AMET A 363 30.682 32.571 321.489 0.50 86.00 C ANISOU 3010 C AMET A 363 12540 11744 8393 327 -270 434 C ATOM 3011 C BMET A 363 30.695 32.591 321.458 0.50 86.05 C ANISOU 3011 C BMET A 363 12543 11748 8405 328 -273 434 C ATOM 3012 O AMET A 363 30.527 33.524 322.260 0.50 85.23 O ANISOU 3012 O AMET A 363 12440 11722 8224 371 -308 301 O ATOM 3013 O BMET A 363 30.556 33.581 322.185 0.50 85.71 O ANISOU 3013 O BMET A 363 12493 11774 8298 376 -316 298 O ATOM 3014 CB AMET A 363 32.852 32.703 320.246 0.50 81.56 C ANISOU 3014 CB AMET A 363 11965 10974 8052 400 -527 590 C ATOM 3015 CB BMET A 363 32.890 32.675 320.244 0.50 81.56 C ANISOU 3015 CB BMET A 363 11967 10971 8051 400 -529 595 C ATOM 3016 CG AMET A 363 34.258 32.169 320.039 0.50 83.33 C ANISOU 3016 CG AMET A 363 12234 11121 8306 420 -645 722 C ATOM 3017 CG BMET A 363 34.317 32.151 320.113 0.50 83.24 C ANISOU 3017 CG BMET A 363 12230 11111 8285 422 -651 725 C ATOM 3018 SD AMET A 363 35.198 32.047 321.573 0.50 85.65 S ANISOU 3018 SD AMET A 363 12672 11474 8396 461 -743 754 S ATOM 3019 SD BMET A 363 35.276 32.950 318.807 0.50 78.24 S ANISOU 3019 SD BMET A 363 11483 10374 7871 449 -792 709 S ATOM 3020 CE AMET A 363 36.039 30.495 321.291 0.50 86.65 C ANISOU 3020 CE AMET A 363 12881 11527 8515 461 -769 944 C ATOM 3021 CE BMET A 363 35.138 34.674 319.263 0.50 65.53 C ANISOU 3021 CE BMET A 363 9849 8791 6258 488 -879 530 C ATOM 3022 N VAL A 364 29.676 32.049 320.787 1.00 96.41 N ANISOU 3022 N VAL A 364 13783 13075 9773 269 -134 424 N ATOM 3023 CA VAL A 364 28.315 32.539 320.974 1.00 97.23 C ANISOU 3023 CA VAL A 364 13793 13302 9849 257 -18 244 C ATOM 3024 C VAL A 364 27.794 32.116 322.342 1.00 94.25 C ANISOU 3024 C VAL A 364 13504 13072 9233 180 108 215 C ATOM 3025 O VAL A 364 27.085 32.873 323.014 1.00 98.49 O ANISOU 3025 O VAL A 364 13992 13738 9692 202 147 38 O ATOM 3026 CB VAL A 364 27.406 32.032 319.838 1.00 89.93 C ANISOU 3026 CB VAL A 364 12756 12362 9053 211 92 235 C ATOM 3027 CG1 VAL A 364 25.939 32.354 320.119 1.00 97.34 C ANISOU 3027 CG1 VAL A 364 13585 13459 9941 189 229 36 C ATOM 3028 CG2 VAL A 364 27.826 32.650 318.516 1.00 62.76 C ANISOU 3028 CG2 VAL A 364 9229 8786 5830 290 -37 235 C ATOM 3029 N TYR A 365 28.140 30.901 322.776 1.00 92.71 N ANISOU 3029 N TYR A 365 13454 12859 8913 90 169 385 N ATOM 3030 CA TYR A 365 27.772 30.465 324.118 1.00 92.33 C ANISOU 3030 CA TYR A 365 13532 12936 8612 2 278 381 C ATOM 3031 C TYR A 365 28.436 31.323 325.185 1.00 96.35 C ANISOU 3031 C TYR A 365 14111 13491 9008 83 157 323 C ATOM 3032 O TYR A 365 27.911 31.449 326.297 1.00107.40 O ANISOU 3032 O TYR A 365 15562 15033 10211 34 243 237 O ATOM 3033 CB TYR A 365 28.156 28.998 324.318 1.00 89.88 C ANISOU 3033 CB TYR A 365 13404 12554 8190 -99 331 595 C ATOM 3034 CG TYR A 365 27.063 28.013 323.966 1.00101.35 C ANISOU 3034 CG TYR A 365 14846 14047 9618 -250 536 615 C ATOM 3035 CD1 TYR A 365 25.932 27.888 324.764 1.00108.38 C ANISOU 3035 CD1 TYR A 365 15740 15109 10330 -378 724 506 C ATOM 3036 CD2 TYR A 365 27.170 27.196 322.848 1.00101.34 C ANISOU 3036 CD2 TYR A 365 14824 13917 9762 -275 546 733 C ATOM 3037 CE1 TYR A 365 24.930 26.984 324.452 1.00119.48 C ANISOU 3037 CE1 TYR A 365 17129 16561 11707 -539 920 513 C ATOM 3038 CE2 TYR A 365 26.174 26.288 322.526 1.00106.47 C ANISOU 3038 CE2 TYR A 365 15464 14600 10388 -423 732 745 C ATOM 3039 CZ TYR A 365 25.055 26.184 323.332 1.00117.10 C ANISOU 3039 CZ TYR A 365 16815 16120 11559 -561 920 635 C ATOM 3040 OH TYR A 365 24.062 25.281 323.015 1.00112.34 O ANISOU 3040 OH TYR A 365 16195 15560 10928 -729 1114 637 O ATOM 3041 N ASP A 366 29.587 31.916 324.870 1.00 96.02 N ANISOU 3041 N ASP A 366 14066 13339 9080 195 -38 360 N ATOM 3042 CA ASP A 366 30.341 32.678 325.856 1.00 93.98 C ANISOU 3042 CA ASP A 366 13877 13112 8718 268 -167 313 C ATOM 3043 C ASP A 366 29.739 34.059 326.082 1.00 95.55 C ANISOU 3043 C ASP A 366 13960 13400 8945 335 -187 86 C ATOM 3044 O ASP A 366 29.643 34.519 327.226 1.00115.18 O ANISOU 3044 O ASP A 366 16500 15997 11266 346 -186 -8 O ATOM 3045 CB ASP A 366 31.792 32.804 325.396 1.00 90.58 C ANISOU 3045 CB ASP A 366 13470 12543 8402 350 -364 419 C ATOM 3046 CG ASP A 366 32.640 33.616 326.347 1.00117.43 C ANISOU 3046 CG ASP A 366 16930 15975 11712 425 -511 363 C ATOM 3047 OD1 ASP A 366 32.283 33.712 327.542 1.00133.90 O ANISOU 3047 OD1 ASP A 366 19100 18180 13598 405 -461 303 O ATOM 3048 OD2 ASP A 366 33.671 34.157 325.896 1.00119.59 O ANISOU 3048 OD2 ASP A 366 17165 16162 12110 493 -674 373 O ATOM 3049 N VAL A 367 29.325 34.727 325.006 1.00 88.38 N ANISOU 3049 N VAL A 367 12902 12439 8239 385 -211 -9 N ATOM 3050 CA VAL A 367 28.893 36.118 325.107 1.00 88.60 C ANISOU 3050 CA VAL A 367 12836 12510 8317 477 -275 -224 C ATOM 3051 C VAL A 367 27.520 36.213 325.762 1.00 94.27 C ANISOU 3051 C VAL A 367 13492 13414 8911 444 -113 -400 C ATOM 3052 O VAL A 367 27.342 36.911 326.767 1.00 98.84 O ANISOU 3052 O VAL A 367 14087 14103 9365 482 -126 -542 O ATOM 3053 CB VAL A 367 28.905 36.799 323.723 1.00 82.43 C ANISOU 3053 CB VAL A 367 11944 11595 7780 545 -370 -263 C ATOM 3054 CG1 VAL A 367 30.321 37.188 323.342 1.00 69.85 C ANISOU 3054 CG1 VAL A 367 10403 9854 6283 586 -556 -163 C ATOM 3055 CG2 VAL A 367 28.275 35.918 322.634 1.00 80.46 C ANISOU 3055 CG2 VAL A 367 11621 11312 7639 485 -255 -190 C ATOM 3056 N PHE A 368 26.527 35.520 325.204 1.00103.85 N ANISOU 3056 N PHE A 368 14624 14677 10157 370 46 -409 N ATOM 3057 CA PHE A 368 25.158 35.671 325.687 1.00110.77 C ANISOU 3057 CA PHE A 368 15400 15749 10938 337 204 -612 C ATOM 3058 C PHE A 368 25.020 35.153 327.112 1.00105.86 C ANISOU 3058 C PHE A 368 14895 15285 10043 232 325 -604 C ATOM 3059 O PHE A 368 24.705 35.911 328.037 1.00108.77 O ANISOU 3059 O PHE A 368 15247 15787 10293 273 326 -778 O ATOM 3060 CB PHE A 368 24.191 34.945 324.750 1.00115.23 C ANISOU 3060 CB PHE A 368 15851 16337 11596 263 349 -615 C ATOM 3061 CG PHE A 368 24.072 35.579 323.396 1.00118.92 C ANISOU 3061 CG PHE A 368 16192 16681 12312 374 241 -672 C ATOM 3062 CD1 PHE A 368 23.518 36.839 323.259 1.00122.18 C ANISOU 3062 CD1 PHE A 368 16491 17128 12804 511 156 -904 C ATOM 3063 CD2 PHE A 368 24.508 34.916 322.261 1.00124.21 C ANISOU 3063 CD2 PHE A 368 16870 17197 13128 346 216 -496 C ATOM 3064 CE1 PHE A 368 23.405 37.433 322.017 1.00129.32 C ANISOU 3064 CE1 PHE A 368 17309 17904 13921 614 44 -950 C ATOM 3065 CE2 PHE A 368 24.396 35.505 321.011 1.00126.32 C ANISOU 3065 CE2 PHE A 368 17037 17352 13608 439 116 -545 C ATOM 3066 CZ PHE A 368 23.844 36.764 320.890 1.00129.35 C ANISOU 3066 CZ PHE A 368 17326 17760 14061 571 27 -766 C ATOM 3067 N GLY A 369 25.245 33.858 327.305 1.00105.33 N ANISOU 3067 N GLY A 369 14958 15199 9865 94 426 -404 N ATOM 3068 CA GLY A 369 25.173 33.262 328.622 1.00116.08 C ANISOU 3068 CA GLY A 369 16472 16686 10949 -23 536 -365 C ATOM 3069 C GLY A 369 26.528 32.775 329.085 1.00125.19 C ANISOU 3069 C GLY A 369 17838 17711 12018 -13 408 -144 C ATOM 3070 O GLY A 369 27.553 33.118 328.491 1.00127.44 O ANISOU 3070 O GLY A 369 18122 17838 12460 99 223 -63 O ATOM 3071 N LYS A 370 26.548 31.980 330.150 1.00134.44 N ANISOU 3071 N LYS A 370 19193 18954 12932 -132 500 -52 N ATOM 3072 CA LYS A 370 27.794 31.425 330.647 1.00139.49 C ANISOU 3072 CA LYS A 370 20051 19478 13472 -113 370 153 C ATOM 3073 C LYS A 370 28.194 30.202 329.823 1.00128.65 C ANISOU 3073 C LYS A 370 18762 17940 12180 -166 372 376 C ATOM 3074 O LYS A 370 27.485 29.764 328.911 1.00 74.97 O ANISOU 3074 O LYS A 370 11860 11122 5503 -232 485 377 O ATOM 3075 CB LYS A 370 27.665 31.072 332.128 1.00135.63 C ANISOU 3075 CB LYS A 370 19755 19118 12660 -212 451 165 C ATOM 3076 N MET A 371 29.362 29.657 330.147 1.00149.18 N ANISOU 3076 N MET A 371 21547 20421 14712 -124 233 556 N ATOM 3077 CA MET A 371 29.859 28.430 329.553 1.00144.62 C ANISOU 3077 CA MET A 371 21089 19685 14177 -158 212 770 C ATOM 3078 C MET A 371 29.290 27.219 330.291 1.00139.27 C ANISOU 3078 C MET A 371 20633 19041 13244 -337 376 881 C ATOM 3079 O MET A 371 28.532 27.340 331.257 1.00143.76 O ANISOU 3079 O MET A 371 21256 19767 13599 -445 513 793 O ATOM 3080 CB MET A 371 31.384 28.421 329.602 1.00148.63 C ANISOU 3080 CB MET A 371 21688 20062 14721 -16 -27 886 C ATOM 3081 CG MET A 371 32.036 29.429 328.678 1.00146.33 C ANISOU 3081 CG MET A 371 21194 19710 14695 125 -182 807 C ATOM 3082 SD MET A 371 31.835 28.978 326.953 1.00152.72 S ANISOU 3082 SD MET A 371 21850 20393 15782 114 -144 865 S ATOM 3083 CE MET A 371 32.643 27.381 326.925 1.00158.09 C ANISOU 3083 CE MET A 371 22748 20929 16389 96 -195 1109 C ATOM 3084 N ASN A 372 29.662 26.032 329.823 1.00130.96 N ANISOU 3084 N ASN A 372 19718 17834 12207 -375 362 1074 N ATOM 3085 CA ASN A 372 29.418 24.794 330.541 1.00124.52 C ANISOU 3085 CA ASN A 372 19181 16991 11138 -532 465 1224 C ATOM 3086 C ASN A 372 30.741 24.058 330.668 1.00125.86 C ANISOU 3086 C ASN A 372 19571 16978 11271 -425 259 1422 C ATOM 3087 O ASN A 372 31.662 24.263 329.873 1.00116.98 O ANISOU 3087 O ASN A 372 18342 15744 10361 -266 85 1450 O ATOM 3088 CB ASN A 372 28.389 23.907 329.824 1.00127.96 C ANISOU 3088 CB ASN A 372 19594 17411 11615 -707 671 1258 C ATOM 3089 CG ASN A 372 27.945 22.727 330.664 1.00152.12 C ANISOU 3089 CG ASN A 372 22952 20464 14383 -914 812 1388 C ATOM 3090 OD1 ASN A 372 27.913 22.793 331.894 1.00161.29 O ANISOU 3090 OD1 ASN A 372 24288 21716 15280 -975 838 1384 O ATOM 3091 ND2 ASN A 372 27.613 21.628 329.996 1.00155.86 N ANISOU 3091 ND2 ASN A 372 23503 20822 14896 -1031 902 1506 N ATOM 3092 N LYS A 373 30.839 23.202 331.686 1.00133.43 N ANISOU 3092 N LYS A 373 20841 17908 11947 -513 275 1552 N ATOM 3093 CA LYS A 373 32.020 22.355 331.799 1.00131.75 C ANISOU 3093 CA LYS A 373 20863 17510 11686 -406 74 1742 C ATOM 3094 C LYS A 373 32.241 21.556 330.522 1.00127.55 C ANISOU 3094 C LYS A 373 20285 16807 11372 -378 44 1846 C ATOM 3095 O LYS A 373 33.389 21.297 330.141 1.00125.41 O ANISOU 3095 O LYS A 373 20043 16400 11206 -210 -167 1928 O ATOM 3096 CB LYS A 373 31.887 21.407 332.990 1.00138.32 C ANISOU 3096 CB LYS A 373 22074 18315 12168 -535 119 1879 C ATOM 3097 CG LYS A 373 33.129 20.546 333.223 1.00127.91 C ANISOU 3097 CG LYS A 373 21027 16800 10775 -397 -119 2065 C ATOM 3098 CD LYS A 373 32.793 19.156 333.741 1.00112.54 C ANISOU 3098 CD LYS A 373 19464 14729 8568 -561 -43 2253 C ATOM 3099 CE LYS A 373 32.572 19.149 335.243 1.00111.17 C ANISOU 3099 CE LYS A 373 19564 14646 8028 -667 0 2274 C ATOM 3100 NZ LYS A 373 32.379 17.766 335.761 1.00104.95 N ANISOU 3100 NZ LYS A 373 19020 13719 7136 -793 44 2421 N ATOM 3101 N LEU A 374 31.159 21.165 329.847 1.00124.91 N ANISOU 3101 N LEU A 374 19867 16487 11107 -540 253 1828 N ATOM 3102 CA LEU A 374 31.288 20.354 328.643 1.00118.24 C ANISOU 3102 CA LEU A 374 18988 15483 10457 -528 239 1924 C ATOM 3103 C LEU A 374 31.776 21.183 327.461 1.00125.68 C ANISOU 3103 C LEU A 374 19613 16417 11724 -364 131 1828 C ATOM 3104 O LEU A 374 32.577 20.705 326.650 1.00123.07 O ANISOU 3104 O LEU A 374 19272 15941 11549 -254 -3 1913 O ATOM 3105 CB LEU A 374 29.950 19.693 328.312 1.00106.30 C ANISOU 3105 CB LEU A 374 17480 14000 8909 -764 499 1923 C ATOM 3106 CG LEU A 374 29.964 18.705 327.142 1.00120.51 C ANISOU 3106 CG LEU A 374 19282 15629 10877 -783 507 2030 C ATOM 3107 CD1 LEU A 374 30.968 17.582 327.379 1.00135.64 C ANISOU 3107 CD1 LEU A 374 21512 17331 12694 -709 334 2234 C ATOM 3108 CD2 LEU A 374 28.574 18.134 326.920 1.00126.25 C ANISOU 3108 CD2 LEU A 374 20005 16412 11552 -1036 776 2005 C ATOM 3109 N ILE A 375 31.305 22.427 327.343 1.00119.58 N ANISOU 3109 N ILE A 375 18589 15797 11049 -348 185 1645 N ATOM 3110 CA ILE A 375 31.692 23.246 326.198 1.00101.62 C ANISOU 3110 CA ILE A 375 16037 13506 9068 -216 91 1556 C ATOM 3111 C ILE A 375 33.160 23.642 326.300 1.00 92.62 C ANISOU 3111 C ILE A 375 14904 12303 7983 -25 -160 1583 C ATOM 3112 O ILE A 375 33.837 23.809 325.278 1.00100.57 O ANISOU 3112 O ILE A 375 15766 13234 9213 79 -271 1584 O ATOM 3113 CB ILE A 375 30.784 24.483 326.071 1.00 90.54 C ANISOU 3113 CB ILE A 375 14392 12265 7743 -240 198 1349 C ATOM 3114 CG1 ILE A 375 29.309 24.094 326.220 1.00 99.03 C ANISOU 3114 CG1 ILE A 375 15463 13445 8717 -437 451 1294 C ATOM 3115 CG2 ILE A 375 31.002 25.141 324.718 1.00 76.33 C ANISOU 3115 CG2 ILE A 375 12341 10420 6243 -141 128 1280 C ATOM 3116 CD1 ILE A 375 28.348 25.271 326.242 1.00 96.37 C ANISOU 3116 CD1 ILE A 375 14900 13287 8428 -449 552 1067 C ATOM 3117 N LYS A 376 33.677 23.801 327.522 1.00 89.22 N ANISOU 3117 N LYS A 376 14637 11914 7349 18 -252 1597 N ATOM 3118 CA LYS A 376 35.096 24.088 327.704 1.00100.05 C ANISOU 3118 CA LYS A 376 16024 13237 8753 196 -496 1617 C ATOM 3119 C LYS A 376 35.973 22.908 327.307 1.00109.89 C ANISOU 3119 C LYS A 376 17410 14318 10026 271 -624 1776 C ATOM 3120 O LYS A 376 37.165 23.100 327.039 1.00107.33 O ANISOU 3120 O LYS A 376 17023 13951 9807 427 -824 1772 O ATOM 3121 CB LYS A 376 35.380 24.473 329.160 1.00104.00 C ANISOU 3121 CB LYS A 376 16681 13825 9008 222 -562 1591 C ATOM 3122 CG LYS A 376 34.861 25.850 329.576 1.00113.00 C ANISOU 3122 CG LYS A 376 17659 15129 10147 208 -504 1404 C ATOM 3123 CD LYS A 376 36.000 26.777 329.995 1.00118.17 C ANISOU 3123 CD LYS A 376 18259 15815 10825 362 -717 1330 C ATOM 3124 CE LYS A 376 35.490 28.047 330.656 1.00111.28 C ANISOU 3124 CE LYS A 376 17290 15097 9897 347 -670 1152 C ATOM 3125 NZ LYS A 376 34.863 27.797 331.977 1.00104.83 N ANISOU 3125 NZ LYS A 376 16671 14380 8779 254 -566 1156 N ATOM 3126 N THR A 377 35.413 21.697 327.261 1.00118.49 N ANISOU 3126 N THR A 377 18684 15316 11021 162 -517 1904 N ATOM 3127 CA THR A 377 36.171 20.499 326.913 1.00121.12 C ANISOU 3127 CA THR A 377 19178 15476 11367 238 -641 2053 C ATOM 3128 C THR A 377 36.184 20.256 325.406 1.00111.63 C ANISOU 3128 C THR A 377 17779 14197 10440 256 -621 2051 C ATOM 3129 O THR A 377 37.241 19.981 324.830 1.00128.57 O ANISOU 3129 O THR A 377 19881 16257 12713 403 -795 2080 O ATOM 3130 CB THR A 377 35.595 19.277 327.639 1.00122.32 C ANISOU 3130 CB THR A 377 19668 15543 11265 103 -547 2200 C ATOM 3131 OG1 THR A 377 34.195 19.159 327.354 1.00141.06 O ANISOU 3131 OG1 THR A 377 21992 17972 13634 -109 -284 2173 O ATOM 3132 CG2 THR A 377 35.799 19.397 329.146 1.00112.34 C ANISOU 3132 CG2 THR A 377 18641 14334 9708 106 -606 2222 C ATOM 3133 N VAL A 378 35.024 20.352 324.752 1.00 92.14 N ANISOU 3133 N VAL A 378 15180 11768 8060 111 -413 2006 N ATOM 3134 CA VAL A 378 34.988 20.206 323.302 1.00105.29 C ANISOU 3134 CA VAL A 378 16650 13373 9984 126 -391 1994 C ATOM 3135 C VAL A 378 35.747 21.335 322.621 1.00105.05 C ANISOU 3135 C VAL A 378 16353 13395 10167 257 -515 1878 C ATOM 3136 O VAL A 378 36.174 21.189 321.470 1.00 99.36 O ANISOU 3136 O VAL A 378 15492 12610 9649 314 -566 1880 O ATOM 3137 CB VAL A 378 33.535 20.150 322.791 1.00 92.63 C ANISOU 3137 CB VAL A 378 14955 11819 8423 -55 -147 1949 C ATOM 3138 CG1 VAL A 378 32.788 18.988 323.435 1.00 94.72 C ANISOU 3138 CG1 VAL A 378 15490 12030 8470 -218 -10 2063 C ATOM 3139 CG2 VAL A 378 32.819 21.464 323.065 1.00 86.20 C ANISOU 3139 CG2 VAL A 378 13957 11177 7616 -95 -53 1783 C ATOM 3140 N PHE A 379 35.926 22.464 323.310 1.00114.20 N ANISOU 3140 N PHE A 379 17446 14670 11276 297 -563 1773 N ATOM 3141 CA PHE A 379 36.650 23.588 322.730 1.00111.53 C ANISOU 3141 CA PHE A 379 16879 14377 11122 399 -680 1661 C ATOM 3142 C PHE A 379 38.083 23.209 322.382 1.00102.91 C ANISOU 3142 C PHE A 379 15782 13208 10109 544 -887 1708 C ATOM 3143 O PHE A 379 38.639 23.718 321.402 1.00 98.60 O ANISOU 3143 O PHE A 379 15037 12662 9766 595 -952 1647 O ATOM 3144 CB PHE A 379 36.630 24.771 323.699 1.00108.09 C ANISOU 3144 CB PHE A 379 16418 14066 10586 414 -708 1546 C ATOM 3145 CG PHE A 379 37.576 25.875 323.329 1.00 95.08 C ANISOU 3145 CG PHE A 379 14591 12451 9086 517 -860 1443 C ATOM 3146 CD1 PHE A 379 37.216 26.831 322.393 1.00 98.03 C ANISOU 3146 CD1 PHE A 379 14750 12848 9648 492 -814 1337 C ATOM 3147 CD2 PHE A 379 38.825 25.961 323.920 1.00 69.82 C ANISOU 3147 CD2 PHE A 379 11444 9255 5828 633 -1052 1447 C ATOM 3148 CE1 PHE A 379 38.087 27.847 322.052 1.00 85.33 C ANISOU 3148 CE1 PHE A 379 13000 11258 8163 560 -949 1247 C ATOM 3149 CE2 PHE A 379 39.698 26.975 323.582 1.00 78.40 C ANISOU 3149 CE2 PHE A 379 12363 10380 7046 702 -1182 1344 C ATOM 3150 CZ PHE A 379 39.330 27.919 322.650 1.00 84.06 C ANISOU 3150 CZ PHE A 379 12884 11112 7945 655 -1126 1248 C ATOM 3151 N ALA A 380 38.698 22.322 323.169 1.00 99.05 N ANISOU 3151 N ALA A 380 15516 12659 9459 611 -995 1808 N ATOM 3152 CA ALA A 380 40.057 21.887 322.868 1.00106.83 C ANISOU 3152 CA ALA A 380 16493 13583 10514 767 -1203 1834 C ATOM 3153 C ALA A 380 40.124 21.162 321.531 1.00107.62 C ANISOU 3153 C ALA A 380 16499 13586 10803 772 -1181 1877 C ATOM 3154 O ALA A 380 41.144 21.236 320.836 1.00103.72 O ANISOU 3154 O ALA A 380 15863 13088 10458 879 -1315 1834 O ATOM 3155 CB ALA A 380 40.583 20.993 323.991 1.00106.89 C ANISOU 3155 CB ALA A 380 16788 13530 10296 848 -1330 1935 C ATOM 3156 N PHE A 381 39.050 20.473 321.146 1.00100.78 N ANISOU 3156 N PHE A 381 15702 12656 9933 649 -1008 1948 N ATOM 3157 CA PHE A 381 39.021 19.759 319.877 1.00 94.08 C ANISOU 3157 CA PHE A 381 14772 11715 9258 644 -976 1986 C ATOM 3158 C PHE A 381 38.420 20.593 318.757 1.00 93.49 C ANISOU 3158 C PHE A 381 14436 11700 9386 565 -853 1893 C ATOM 3159 O PHE A 381 38.795 20.416 317.591 1.00 86.15 O ANISOU 3159 O PHE A 381 13363 10731 8639 599 -880 1880 O ATOM 3160 CB PHE A 381 38.235 18.454 320.031 1.00 95.73 C ANISOU 3160 CB PHE A 381 15215 11806 9352 551 -867 2118 C ATOM 3161 CG PHE A 381 38.615 17.660 321.255 1.00111.86 C ANISOU 3161 CG PHE A 381 17572 13776 11154 601 -970 2222 C ATOM 3162 CD1 PHE A 381 39.834 17.003 321.322 1.00118.58 C ANISOU 3162 CD1 PHE A 381 18518 14539 11999 780 -1190 2265 C ATOM 3163 CD2 PHE A 381 37.753 17.569 322.337 1.00111.99 C ANISOU 3163 CD2 PHE A 381 17792 13817 10942 472 -850 2269 C ATOM 3164 CE1 PHE A 381 40.188 16.273 322.443 1.00120.38 C ANISOU 3164 CE1 PHE A 381 19057 14686 11996 841 -1306 2362 C ATOM 3165 CE2 PHE A 381 38.100 16.840 323.463 1.00120.40 C ANISOU 3165 CE2 PHE A 381 19174 14806 11768 509 -949 2374 C ATOM 3166 CZ PHE A 381 39.319 16.191 323.515 1.00122.36 C ANISOU 3166 CZ PHE A 381 19533 14948 12011 700 -1185 2425 C ATOM 3167 N CYS A 382 37.499 21.503 319.082 1.00101.84 N ANISOU 3167 N CYS A 382 15433 12853 10409 467 -727 1819 N ATOM 3168 CA CYS A 382 36.959 22.395 318.064 1.00 95.54 C ANISOU 3168 CA CYS A 382 14402 12106 9794 414 -640 1720 C ATOM 3169 C CYS A 382 38.008 23.391 317.589 1.00101.12 C ANISOU 3169 C CYS A 382 14930 12854 10637 504 -784 1630 C ATOM 3170 O CYS A 382 38.000 23.784 316.417 1.00105.54 O ANISOU 3170 O CYS A 382 15315 13406 11379 488 -765 1582 O ATOM 3171 CB CYS A 382 35.733 23.133 318.601 1.00 87.19 C ANISOU 3171 CB CYS A 382 13329 11143 8657 309 -490 1644 C ATOM 3172 SG CYS A 382 34.287 22.089 318.846 1.00107.20 S ANISOU 3172 SG CYS A 382 16005 13659 11068 150 -271 1712 S ATOM 3173 N SER A 383 38.914 23.811 318.473 1.00 92.30 N ANISOU 3173 N SER A 383 13858 11783 9430 589 -926 1602 N ATOM 3174 CA SER A 383 39.986 24.701 318.045 1.00 88.23 C ANISOU 3174 CA SER A 383 13176 11312 9036 656 -1063 1511 C ATOM 3175 C SER A 383 40.959 23.986 317.118 1.00 87.64 C ANISOU 3175 C SER A 383 13029 11182 9087 727 -1159 1542 C ATOM 3176 O SER A 383 41.567 24.624 316.251 1.00 94.15 O ANISOU 3176 O SER A 383 13673 12037 10063 731 -1209 1467 O ATOM 3177 CB SER A 383 40.722 25.263 319.260 1.00 82.13 C ANISOU 3177 CB SER A 383 12469 10610 8128 727 -1195 1465 C ATOM 3178 OG SER A 383 41.460 24.252 319.921 1.00 85.59 O ANISOU 3178 OG SER A 383 13063 11010 8446 825 -1312 1545 O ATOM 3179 N MET A 384 41.118 22.669 317.276 1.00 79.68 N ANISOU 3179 N MET A 384 12167 10093 8013 779 -1186 1646 N ATOM 3180 CA MET A 384 41.953 21.914 316.348 1.00 78.82 C ANISOU 3180 CA MET A 384 11986 9932 8028 855 -1271 1663 C ATOM 3181 C MET A 384 41.286 21.766 314.989 1.00 80.89 C ANISOU 3181 C MET A 384 12125 10153 8457 768 -1138 1669 C ATOM 3182 O MET A 384 41.979 21.647 313.973 1.00 80.52 O ANISOU 3182 O MET A 384 11935 10104 8555 804 -1192 1634 O ATOM 3183 CB MET A 384 42.280 20.538 316.928 1.00 82.37 C ANISOU 3183 CB MET A 384 12654 10288 8355 949 -1354 1769 C ATOM 3184 CG MET A 384 43.365 20.566 317.984 1.00 98.49 C ANISOU 3184 CG MET A 384 14781 12369 10272 1088 -1550 1746 C ATOM 3185 SD MET A 384 44.969 21.088 317.329 1.00 98.79 S ANISOU 3185 SD MET A 384 14564 12503 10467 1208 -1737 1606 S ATOM 3186 CE MET A 384 45.487 19.629 316.424 1.00 92.46 C ANISOU 3186 CE MET A 384 13775 11597 9758 1316 -1806 1655 C ATOM 3187 N LEU A 385 39.952 21.758 314.947 1.00 81.54 N ANISOU 3187 N LEU A 385 12255 10211 8514 652 -966 1702 N ATOM 3188 CA LEU A 385 39.262 21.847 313.663 1.00 86.90 C ANISOU 3188 CA LEU A 385 12796 10870 9353 569 -845 1684 C ATOM 3189 C LEU A 385 39.673 23.108 312.915 1.00 82.10 C ANISOU 3189 C LEU A 385 11981 10331 8884 556 -881 1575 C ATOM 3190 O LEU A 385 39.856 23.083 311.693 1.00 77.41 O ANISOU 3190 O LEU A 385 11254 9719 8441 539 -869 1556 O ATOM 3191 CB LEU A 385 37.743 21.825 313.865 1.00 89.99 C ANISOU 3191 CB LEU A 385 13249 11257 9686 450 -662 1704 C ATOM 3192 CG LEU A 385 37.064 20.488 314.170 1.00 89.33 C ANISOU 3192 CG LEU A 385 13351 11089 9501 401 -571 1814 C ATOM 3193 CD1 LEU A 385 35.567 20.667 314.327 1.00 84.25 C ANISOU 3193 CD1 LEU A 385 12719 10482 8809 265 -380 1793 C ATOM 3194 CD2 LEU A 385 37.342 19.479 313.090 1.00 72.27 C ANISOU 3194 CD2 LEU A 385 11166 8833 7461 424 -582 1868 C ATOM 3195 N CYS A 386 39.829 24.221 313.635 1.00 78.39 N ANISOU 3195 N CYS A 386 11493 9934 8356 557 -926 1503 N ATOM 3196 CA CYS A 386 40.215 25.468 312.988 1.00 83.73 C ANISOU 3196 CA CYS A 386 12006 10660 9148 529 -966 1401 C ATOM 3197 C CYS A 386 41.542 25.331 312.253 1.00 92.74 C ANISOU 3197 C CYS A 386 13031 11815 10393 576 -1083 1374 C ATOM 3198 O CYS A 386 41.745 25.979 311.219 1.00110.23 O ANISOU 3198 O CYS A 386 15106 14042 12736 520 -1077 1318 O ATOM 3199 CB CYS A 386 40.294 26.592 314.020 1.00 85.78 C ANISOU 3199 CB CYS A 386 12291 10987 9313 533 -1017 1327 C ATOM 3200 SG CYS A 386 38.755 26.879 314.915 1.00 91.45 S ANISOU 3200 SG CYS A 386 13119 11722 9905 478 -878 1322 S ATOM 3201 N LEU A 387 42.453 24.497 312.759 1.00 89.59 N ANISOU 3201 N LEU A 387 12689 11419 9933 678 -1194 1405 N ATOM 3202 CA LEU A 387 43.752 24.348 312.109 1.00 84.28 C ANISOU 3202 CA LEU A 387 11883 10786 9354 733 -1310 1352 C ATOM 3203 C LEU A 387 43.632 23.558 310.813 1.00 86.85 C ANISOU 3203 C LEU A 387 12134 11057 9807 715 -1249 1385 C ATOM 3204 O LEU A 387 44.178 23.959 309.778 1.00101.97 O ANISOU 3204 O LEU A 387 13886 13014 11846 673 -1260 1318 O ATOM 3205 CB LEU A 387 44.754 23.673 313.050 1.00 78.37 C ANISOU 3205 CB LEU A 387 11214 10060 8502 873 -1466 1357 C ATOM 3206 CG LEU A 387 46.177 23.545 312.483 1.00 88.75 C ANISOU 3206 CG LEU A 387 12367 11448 9906 946 -1602 1267 C ATOM 3207 CD1 LEU A 387 46.801 24.919 312.261 1.00 88.74 C ANISOU 3207 CD1 LEU A 387 12199 11555 9962 867 -1637 1142 C ATOM 3208 CD2 LEU A 387 47.064 22.704 313.386 1.00 93.41 C ANISOU 3208 CD2 LEU A 387 13052 12048 10393 1115 -1768 1271 C ATOM 3209 N LEU A 388 42.923 22.428 310.845 1.00 71.30 N ANISOU 3209 N LEU A 388 10291 8996 7803 734 -1181 1484 N ATOM 3210 CA LEU A 388 42.863 21.582 309.660 1.00 81.13 C ANISOU 3210 CA LEU A 388 11475 10186 9164 730 -1135 1512 C ATOM 3211 C LEU A 388 42.039 22.200 308.538 1.00 94.79 C ANISOU 3211 C LEU A 388 13094 11911 11011 604 -1002 1492 C ATOM 3212 O LEU A 388 42.022 21.650 307.432 1.00103.61 O ANISOU 3212 O LEU A 388 14136 12996 12235 589 -963 1500 O ATOM 3213 CB LEU A 388 42.326 20.196 310.019 1.00 80.22 C ANISOU 3213 CB LEU A 388 11545 9961 8975 775 -1102 1624 C ATOM 3214 CG LEU A 388 40.878 20.044 310.468 1.00 97.99 C ANISOU 3214 CG LEU A 388 13937 12153 11143 679 -950 1700 C ATOM 3215 CD1 LEU A 388 40.018 19.510 309.343 1.00 95.04 C ANISOU 3215 CD1 LEU A 388 13520 11715 10875 600 -818 1732 C ATOM 3216 CD2 LEU A 388 40.824 19.118 311.657 1.00112.77 C ANISOU 3216 CD2 LEU A 388 16046 13957 12844 737 -992 1791 C ATOM 3217 N ASN A 389 41.362 23.322 308.785 1.00 81.78 N ANISOU 3217 N ASN A 389 11439 10291 9344 525 -943 1459 N ATOM 3218 CA ASN A 389 40.819 24.097 307.676 1.00 79.12 C ANISOU 3218 CA ASN A 389 10989 9954 9120 426 -863 1417 C ATOM 3219 C ASN A 389 41.943 24.702 306.849 1.00 71.61 C ANISOU 3219 C ASN A 389 9885 9060 8263 405 -942 1339 C ATOM 3220 O ASN A 389 41.863 24.753 305.617 1.00 71.79 O ANISOU 3220 O ASN A 389 9812 9070 8394 344 -895 1325 O ATOM 3221 CB ASN A 389 39.893 25.193 308.196 1.00 77.79 C ANISOU 3221 CB ASN A 389 10857 9797 8902 368 -807 1383 C ATOM 3222 CG ASN A 389 39.354 26.069 307.088 1.00 85.09 C ANISOU 3222 CG ASN A 389 11688 10708 9934 284 -752 1334 C ATOM 3223 OD1 ASN A 389 38.381 25.719 306.418 1.00 84.13 O ANISOU 3223 OD1 ASN A 389 11560 10542 9862 248 -651 1359 O ATOM 3224 ND2 ASN A 389 39.985 27.218 306.887 1.00 78.89 N ANISOU 3224 ND2 ASN A 389 10839 9956 9179 248 -825 1261 N ATOM 3225 N SER A 390 43.001 25.162 307.514 1.00 74.08 N ANISOU 3225 N SER A 390 10173 9446 8530 444 -1060 1282 N ATOM 3226 CA SER A 390 44.160 25.704 306.822 1.00 81.23 C ANISOU 3226 CA SER A 390 10926 10427 9509 407 -1133 1193 C ATOM 3227 C SER A 390 45.011 24.624 306.169 1.00 84.03 C ANISOU 3227 C SER A 390 11194 10808 9926 472 -1176 1185 C ATOM 3228 O SER A 390 45.900 24.956 305.377 1.00 92.83 O ANISOU 3228 O SER A 390 12160 11998 11113 423 -1211 1103 O ATOM 3229 CB SER A 390 45.012 26.515 307.804 1.00 93.85 C ANISOU 3229 CB SER A 390 12518 12106 11034 426 -1247 1120 C ATOM 3230 OG SER A 390 44.261 27.568 308.390 1.00110.66 O ANISOU 3230 OG SER A 390 14724 14213 13109 372 -1215 1112 O ATOM 3231 N THR A 391 44.767 23.350 306.477 1.00 82.07 N ANISOU 3231 N THR A 391 11040 10499 9645 575 -1176 1260 N ATOM 3232 CA THR A 391 45.536 22.262 305.885 1.00 88.53 C ANISOU 3232 CA THR A 391 11789 11327 10521 659 -1230 1244 C ATOM 3233 C THR A 391 44.858 21.696 304.650 1.00 82.46 C ANISOU 3233 C THR A 391 10987 10493 9851 605 -1117 1285 C ATOM 3234 O THR A 391 45.540 21.324 303.689 1.00 97.16 O ANISOU 3234 O THR A 391 12717 12399 11800 613 -1137 1230 O ATOM 3235 CB THR A 391 45.755 21.137 306.904 1.00 94.94 C ANISOU 3235 CB THR A 391 12747 12090 11237 816 -1321 1299 C ATOM 3236 OG1 THR A 391 44.554 20.372 307.056 1.00110.70 O ANISOU 3236 OG1 THR A 391 14907 13958 13193 806 -1220 1419 O ATOM 3237 CG2 THR A 391 46.156 21.703 308.239 1.00 68.29 C ANISOU 3237 CG2 THR A 391 9442 8764 7741 865 -1418 1276 C ATOM 3238 N VAL A 392 43.525 21.628 304.650 1.00 64.68 N ANISOU 3238 N VAL A 392 8842 8149 7585 548 -998 1369 N ATOM 3239 CA VAL A 392 42.820 21.061 303.509 1.00 68.50 C ANISOU 3239 CA VAL A 392 9297 8572 8159 499 -893 1405 C ATOM 3240 C VAL A 392 42.593 22.084 302.406 1.00 75.63 C ANISOU 3240 C VAL A 392 10079 9509 9147 371 -828 1355 C ATOM 3241 O VAL A 392 42.355 21.695 301.256 1.00 68.06 O ANISOU 3241 O VAL A 392 9056 8528 8276 332 -767 1357 O ATOM 3242 CB VAL A 392 41.471 20.457 303.929 1.00 64.71 C ANISOU 3242 CB VAL A 392 8972 7988 7626 485 -790 1503 C ATOM 3243 CG1 VAL A 392 41.682 19.324 304.923 1.00 62.52 C ANISOU 3243 CG1 VAL A 392 8850 7652 7252 596 -852 1568 C ATOM 3244 CG2 VAL A 392 40.550 21.529 304.506 1.00 80.43 C ANISOU 3244 CG2 VAL A 392 11011 9987 9561 409 -726 1502 C ATOM 3245 N ASN A 393 42.657 23.378 302.713 1.00 67.73 N ANISOU 3245 N ASN A 393 9062 8553 8120 305 -847 1309 N ATOM 3246 CA ASN A 393 42.498 24.377 301.659 1.00 78.47 C ANISOU 3246 CA ASN A 393 10340 9927 9549 183 -803 1266 C ATOM 3247 C ASN A 393 43.594 24.261 300.611 1.00 84.35 C ANISOU 3247 C ASN A 393 10936 10745 10367 146 -836 1200 C ATOM 3248 O ASN A 393 43.271 24.234 299.411 1.00 70.78 O ANISOU 3248 O ASN A 393 9166 9007 8721 73 -768 1201 O ATOM 3249 CB ASN A 393 42.433 25.779 302.275 1.00 72.87 C ANISOU 3249 CB ASN A 393 9664 9235 8786 125 -836 1226 C ATOM 3250 CG ASN A 393 41.049 26.116 302.796 1.00 76.84 C ANISOU 3250 CG ASN A 393 10281 9668 9246 124 -768 1266 C ATOM 3251 OD1 ASN A 393 40.068 25.457 302.451 1.00 84.34 O ANISOU 3251 OD1 ASN A 393 11264 10562 10221 132 -680 1317 O ATOM 3252 ND2 ASN A 393 40.959 27.146 303.623 1.00 66.83 N ANISOU 3252 ND2 ASN A 393 9064 8413 7914 112 -807 1231 N ATOM 3253 N PRO A 394 44.877 24.174 300.967 1.00 84.34 N ANISOU 3253 N PRO A 394 10856 10840 10350 191 -934 1132 N ATOM 3254 CA PRO A 394 45.887 23.872 299.941 1.00 90.18 C ANISOU 3254 CA PRO A 394 11436 11670 11159 162 -952 1053 C ATOM 3255 C PRO A 394 45.638 22.553 299.231 1.00 98.43 C ANISOU 3255 C PRO A 394 12464 12671 12264 232 -911 1088 C ATOM 3256 O PRO A 394 46.040 22.398 298.071 1.00103.19 O ANISOU 3256 O PRO A 394 12946 13325 12936 175 -880 1036 O ATOM 3257 CB PRO A 394 47.198 23.860 300.737 1.00 76.52 C ANISOU 3257 CB PRO A 394 9633 10055 9387 237 -1078 964 C ATOM 3258 CG PRO A 394 46.923 24.746 301.895 1.00 84.54 C ANISOU 3258 CG PRO A 394 10753 11049 10318 229 -1113 983 C ATOM 3259 CD PRO A 394 45.498 24.495 302.262 1.00 79.10 C ANISOU 3259 CD PRO A 394 10227 10227 9601 256 -1035 1101 C ATOM 3260 N ILE A 395 44.981 21.596 299.888 1.00 95.42 N ANISOU 3260 N ILE A 395 12209 12195 11852 344 -905 1173 N ATOM 3261 CA ILE A 395 44.619 20.354 299.212 1.00 79.16 C ANISOU 3261 CA ILE A 395 10158 10070 9848 399 -861 1213 C ATOM 3262 C ILE A 395 43.477 20.600 298.234 1.00 84.63 C ANISOU 3262 C ILE A 395 10862 10697 10595 287 -733 1258 C ATOM 3263 O ILE A 395 43.429 20.001 297.153 1.00102.61 O ANISOU 3263 O ILE A 395 13073 12968 12947 272 -688 1247 O ATOM 3264 CB ILE A 395 44.258 19.265 300.240 1.00 76.51 C ANISOU 3264 CB ILE A 395 9983 9637 9449 532 -895 1294 C ATOM 3265 CG1 ILE A 395 45.434 19.026 301.199 1.00 82.36 C ANISOU 3265 CG1 ILE A 395 10722 10441 10130 663 -1046 1243 C ATOM 3266 CG2 ILE A 395 43.870 17.969 299.527 1.00 65.90 C ANISOU 3266 CG2 ILE A 395 8665 8210 8164 578 -852 1334 C ATOM 3267 CD1 ILE A 395 45.130 18.062 302.337 1.00 76.26 C ANISOU 3267 CD1 ILE A 395 10147 9563 9265 789 -1098 1330 C ATOM 3268 N ILE A 396 42.542 21.484 298.591 1.00 85.03 N ANISOU 3268 N ILE A 396 10993 10705 10609 215 -680 1298 N ATOM 3269 CA ILE A 396 41.429 21.786 297.694 1.00 87.55 C ANISOU 3269 CA ILE A 396 11322 10968 10976 125 -577 1326 C ATOM 3270 C ILE A 396 41.929 22.527 296.462 1.00 80.83 C ANISOU 3270 C ILE A 396 10355 10176 10181 16 -570 1263 C ATOM 3271 O ILE A 396 41.488 22.258 295.338 1.00 86.72 O ANISOU 3271 O ILE A 396 11064 10896 10988 -31 -505 1269 O ATOM 3272 CB ILE A 396 40.340 22.588 298.433 1.00 88.69 C ANISOU 3272 CB ILE A 396 11573 11063 11064 95 -539 1360 C ATOM 3273 CG1 ILE A 396 39.715 21.743 299.547 1.00 90.06 C ANISOU 3273 CG1 ILE A 396 11868 11181 11171 175 -518 1426 C ATOM 3274 CG2 ILE A 396 39.247 23.044 297.459 1.00 72.47 C ANISOU 3274 CG2 ILE A 396 9514 8962 9061 14 -455 1364 C ATOM 3275 CD1 ILE A 396 38.910 22.548 300.551 1.00101.45 C ANISOU 3275 CD1 ILE A 396 13401 12613 12534 159 -498 1435 C ATOM 3276 N TYR A 397 42.852 23.472 296.647 1.00 82.14 N ANISOU 3276 N TYR A 397 10469 10421 10319 -38 -634 1200 N ATOM 3277 CA TYR A 397 43.393 24.195 295.503 1.00 74.66 C ANISOU 3277 CA TYR A 397 9429 9533 9406 -170 -622 1140 C ATOM 3278 C TYR A 397 44.044 23.237 294.516 1.00 81.34 C ANISOU 3278 C TYR A 397 10151 10441 10314 -158 -606 1098 C ATOM 3279 O TYR A 397 43.917 23.405 293.298 1.00 95.15 O ANISOU 3279 O TYR A 397 11854 12197 12102 -257 -550 1084 O ATOM 3280 CB TYR A 397 44.408 25.241 295.961 1.00 62.39 C ANISOU 3280 CB TYR A 397 7835 8065 7804 -239 -695 1069 C ATOM 3281 CG TYR A 397 43.950 26.139 297.089 1.00 85.77 C ANISOU 3281 CG TYR A 397 10913 10977 10699 -230 -731 1093 C ATOM 3282 CD1 TYR A 397 42.612 26.477 297.253 1.00 85.33 C ANISOU 3282 CD1 TYR A 397 10977 10812 10633 -223 -684 1155 C ATOM 3283 CD2 TYR A 397 44.869 26.658 297.986 1.00 90.02 C ANISOU 3283 CD2 TYR A 397 11428 11590 11185 -227 -815 1036 C ATOM 3284 CE1 TYR A 397 42.207 27.305 298.288 1.00 83.59 C ANISOU 3284 CE1 TYR A 397 10852 10558 10350 -209 -718 1159 C ATOM 3285 CE2 TYR A 397 44.478 27.481 299.020 1.00 93.07 C ANISOU 3285 CE2 TYR A 397 11919 11936 11508 -217 -850 1049 C ATOM 3286 CZ TYR A 397 43.146 27.803 299.168 1.00 88.88 C ANISOU 3286 CZ TYR A 397 11508 11296 10966 -206 -801 1110 C ATOM 3287 OH TYR A 397 42.751 28.625 300.198 1.00 93.72 O ANISOU 3287 OH TYR A 397 12217 11878 11515 -190 -836 1107 O ATOM 3288 N ALA A 398 44.734 22.215 295.024 1.00 85.50 N ANISOU 3288 N ALA A 398 10631 11011 10845 -30 -661 1073 N ATOM 3289 CA ALA A 398 45.466 21.308 294.149 1.00 89.20 C ANISOU 3289 CA ALA A 398 10970 11551 11372 1 -662 1008 C ATOM 3290 C ALA A 398 44.524 20.440 293.326 1.00 92.74 C ANISOU 3290 C ALA A 398 11453 11906 11877 19 -581 1067 C ATOM 3291 O ALA A 398 44.827 20.112 292.175 1.00107.99 O ANISOU 3291 O ALA A 398 13281 13888 13860 -25 -545 1016 O ATOM 3292 CB ALA A 398 46.406 20.432 294.974 1.00 86.56 C ANISOU 3292 CB ALA A 398 10595 11271 11025 162 -766 958 C ATOM 3293 N LEU A 399 43.383 20.053 293.891 1.00 84.36 N ANISOU 3293 N LEU A 399 10531 10719 10803 75 -547 1165 N ATOM 3294 CA LEU A 399 42.504 19.115 293.204 1.00 94.94 C ANISOU 3294 CA LEU A 399 11904 11974 12197 96 -473 1213 C ATOM 3295 C LEU A 399 41.612 19.775 292.162 1.00 96.65 C ANISOU 3295 C LEU A 399 12120 12161 12443 -28 -386 1230 C ATOM 3296 O LEU A 399 41.146 19.088 291.245 1.00113.58 O ANISOU 3296 O LEU A 399 14242 14272 14642 -34 -329 1237 O ATOM 3297 CB LEU A 399 41.624 18.377 294.217 1.00 93.61 C ANISOU 3297 CB LEU A 399 11884 11690 11994 185 -462 1303 C ATOM 3298 CG LEU A 399 42.360 17.439 295.177 1.00 98.33 C ANISOU 3298 CG LEU A 399 12527 12278 12557 328 -555 1305 C ATOM 3299 CD1 LEU A 399 41.387 16.784 296.151 1.00103.83 C ANISOU 3299 CD1 LEU A 399 13403 12851 13198 377 -527 1405 C ATOM 3300 CD2 LEU A 399 43.150 16.372 294.428 1.00 87.57 C ANISOU 3300 CD2 LEU A 399 11073 10941 11257 407 -594 1244 C ATOM 3301 N ARG A 400 41.365 21.077 292.273 1.00 72.40 N ANISOU 3301 N ARG A 400 9081 9095 9334 -121 -385 1232 N ATOM 3302 CA ARG A 400 40.414 21.755 291.403 1.00 85.43 C ANISOU 3302 CA ARG A 400 10764 10697 11000 -216 -325 1250 C ATOM 3303 C ARG A 400 41.053 22.759 290.461 1.00 91.43 C ANISOU 3303 C ARG A 400 11468 11520 11751 -350 -335 1198 C ATOM 3304 O ARG A 400 40.545 22.956 289.357 1.00105.78 O ANISOU 3304 O ARG A 400 13289 13312 13592 -423 -291 1201 O ATOM 3305 CB ARG A 400 39.358 22.475 292.246 1.00 73.15 C ANISOU 3305 CB ARG A 400 9325 9067 9400 -208 -320 1294 C ATOM 3306 CG ARG A 400 38.702 21.576 293.289 1.00 62.79 C ANISOU 3306 CG ARG A 400 8084 7702 8073 -105 -298 1345 C ATOM 3307 CD ARG A 400 37.207 21.830 293.411 1.00 75.07 C ANISOU 3307 CD ARG A 400 9714 9187 9622 -114 -236 1373 C ATOM 3308 NE ARG A 400 36.548 21.794 292.105 1.00 79.71 N ANISOU 3308 NE ARG A 400 10266 9751 10270 -165 -185 1361 N ATOM 3309 CZ ARG A 400 36.209 20.681 291.459 1.00 97.41 C ANISOU 3309 CZ ARG A 400 12476 11970 12566 -148 -128 1373 C ATOM 3310 NH1 ARG A 400 36.461 19.492 291.995 1.00 98.55 N ANISOU 3310 NH1 ARG A 400 12635 12099 12712 -82 -119 1403 N ATOM 3311 NH2 ARG A 400 35.618 20.758 290.269 1.00109.18 N ANISOU 3311 NH2 ARG A 400 13935 13446 14104 -195 -90 1355 N ATOM 3312 N SER A 401 42.141 23.403 290.867 1.00 78.36 N ANISOU 3312 N SER A 401 9771 9947 10056 -395 -393 1148 N ATOM 3313 CA SER A 401 42.830 24.365 290.014 1.00 79.22 C ANISOU 3313 CA SER A 401 9837 10121 10141 -553 -396 1094 C ATOM 3314 C SER A 401 43.793 23.605 289.112 1.00 82.20 C ANISOU 3314 C SER A 401 10064 10615 10554 -579 -374 1022 C ATOM 3315 O SER A 401 44.921 23.297 289.504 1.00 82.00 O ANISOU 3315 O SER A 401 9930 10703 10525 -548 -417 948 O ATOM 3316 CB SER A 401 43.556 25.404 290.855 1.00 82.25 C ANISOU 3316 CB SER A 401 10238 10549 10464 -608 -462 1060 C ATOM 3317 OG SER A 401 44.320 26.258 290.030 1.00 85.18 O ANISOU 3317 OG SER A 401 10570 10990 10804 -785 -458 1003 O ATOM 3318 N LYS A 402 43.349 23.316 287.887 1.00104.49 N ANISOU 3318 N LYS A 402 12874 13419 13409 -631 -312 1029 N ATOM 3319 CA LYS A 402 44.180 22.567 286.952 1.00112.66 C ANISOU 3319 CA LYS A 402 13762 14568 14475 -654 -283 951 C ATOM 3320 C LYS A 402 45.406 23.372 286.539 1.00108.30 C ANISOU 3320 C LYS A 402 13118 14159 13872 -816 -290 857 C ATOM 3321 O LYS A 402 46.455 22.791 286.238 1.00113.17 O ANISOU 3321 O LYS A 402 13574 14920 14506 -812 -290 754 O ATOM 3322 CB LYS A 402 43.362 22.163 285.719 1.00119.98 C ANISOU 3322 CB LYS A 402 14707 15441 15437 -685 -213 980 C ATOM 3323 CG LYS A 402 41.900 21.771 286.001 1.00126.93 C ANISOU 3323 CG LYS A 402 15705 16172 16352 -584 -193 1073 C ATOM 3324 CD LYS A 402 41.776 20.592 286.967 1.00128.17 C ANISOU 3324 CD LYS A 402 15855 16294 16550 -413 -212 1093 C ATOM 3325 CE LYS A 402 40.326 20.371 287.392 1.00116.63 C ANISOU 3325 CE LYS A 402 14513 14699 15103 -349 -182 1177 C ATOM 3326 NZ LYS A 402 40.165 19.221 288.332 1.00 94.65 N ANISOU 3326 NZ LYS A 402 11755 11868 12340 -210 -192 1208 N ATOM 3327 N ASP A 403 45.302 24.704 286.537 1.00101.61 N ANISOU 3327 N ASP A 403 12371 13276 12960 -962 -298 882 N ATOM 3328 CA ASP A 403 46.439 25.536 286.159 1.00104.47 C ANISOU 3328 CA ASP A 403 12664 13767 13261 -1152 -296 795 C ATOM 3329 C ASP A 403 47.510 25.544 287.239 1.00116.37 C ANISOU 3329 C ASP A 403 14068 15389 14759 -1105 -360 714 C ATOM 3330 O ASP A 403 48.701 25.662 286.927 1.00116.58 O ANISOU 3330 O ASP A 403 13948 15587 14762 -1213 -352 595 O ATOM 3331 CB ASP A 403 45.970 26.961 285.869 1.00113.99 C ANISOU 3331 CB ASP A 403 14045 14873 14395 -1322 -300 852 C ATOM 3332 CG ASP A 403 45.035 27.033 284.681 1.00127.30 C ANISOU 3332 CG ASP A 403 15831 16460 16076 -1378 -251 915 C ATOM 3333 OD1 ASP A 403 43.825 26.779 284.861 1.00134.69 O ANISOU 3333 OD1 ASP A 403 16864 17261 17051 -1250 -260 995 O ATOM 3334 OD2 ASP A 403 45.511 27.342 283.567 1.00128.94 O ANISOU 3334 OD2 ASP A 403 16020 16735 16236 -1557 -204 877 O ATOM 3335 N LEU A 404 47.114 25.418 288.507 1.00129.31 N ANISOU 3335 N LEU A 404 15774 16950 16410 -950 -422 766 N ATOM 3336 CA LEU A 404 48.097 25.421 289.586 1.00126.37 C ANISOU 3336 CA LEU A 404 15314 16679 16020 -890 -496 690 C ATOM 3337 C LEU A 404 48.939 24.154 289.559 1.00121.66 C ANISOU 3337 C LEU A 404 14537 16214 15475 -757 -518 593 C ATOM 3338 O LEU A 404 50.134 24.190 289.879 1.00103.45 O ANISOU 3338 O LEU A 404 12085 14067 13153 -767 -565 469 O ATOM 3339 CB LEU A 404 47.396 25.571 290.936 1.00113.48 C ANISOU 3339 CB LEU A 404 13816 14925 14376 -756 -555 775 C ATOM 3340 CG LEU A 404 48.251 26.087 292.097 1.00102.10 C ANISOU 3340 CG LEU A 404 12343 13562 12890 -742 -640 713 C ATOM 3341 CD1 LEU A 404 48.681 27.530 291.861 1.00110.07 C ANISOU 3341 CD1 LEU A 404 13383 14602 13838 -964 -637 674 C ATOM 3342 CD2 LEU A 404 47.495 25.969 293.410 1.00 90.85 C ANISOU 3342 CD2 LEU A 404 11048 12020 11450 -584 -690 799 C ATOM 3343 N ARG A 405 48.336 23.025 289.179 1.00118.54 N ANISOU 3343 N ARG A 405 14147 15755 15140 -628 -490 636 N ATOM 3344 CA ARG A 405 49.101 21.792 289.034 1.00109.00 C ANISOU 3344 CA ARG A 405 12781 14652 13981 -493 -520 538 C ATOM 3345 C ARG A 405 50.222 21.971 288.020 1.00121.80 C ANISOU 3345 C ARG A 405 14209 16475 15595 -637 -482 385 C ATOM 3346 O ARG A 405 51.370 21.589 288.270 1.00123.97 O ANISOU 3346 O ARG A 405 14311 16914 15876 -576 -539 242 O ATOM 3347 CB ARG A 405 48.177 20.646 288.618 1.00 87.82 C ANISOU 3347 CB ARG A 405 10158 11848 11360 -367 -484 614 C ATOM 3348 CG ARG A 405 47.311 20.109 289.745 1.00 81.38 C ANISOU 3348 CG ARG A 405 9497 10872 10551 -199 -527 729 C ATOM 3349 CD ARG A 405 45.861 19.905 289.320 1.00 94.53 C ANISOU 3349 CD ARG A 405 11300 12377 12242 -208 -450 852 C ATOM 3350 NE ARG A 405 45.684 18.858 288.319 1.00103.89 N ANISOU 3350 NE ARG A 405 12429 13555 13490 -169 -404 832 N ATOM 3351 CZ ARG A 405 44.527 18.246 288.077 1.00115.57 C ANISOU 3351 CZ ARG A 405 14008 14901 15005 -126 -354 919 C ATOM 3352 NH1 ARG A 405 43.438 18.567 288.765 1.00105.52 N ANISOU 3352 NH1 ARG A 405 12884 13501 13709 -118 -337 1026 N ATOM 3353 NH2 ARG A 405 44.455 17.302 287.151 1.00128.18 N ANISOU 3353 NH2 ARG A 405 15546 16498 16658 -93 -318 888 N ATOM 3354 N HIS A 406 49.906 22.568 286.869 1.00128.85 N ANISOU 3354 N HIS A 406 15128 17365 16464 -832 -389 405 N ATOM 3355 CA HIS A 406 50.910 22.742 285.826 1.00123.85 C ANISOU 3355 CA HIS A 406 14321 16929 15807 -1000 -333 262 C ATOM 3356 C HIS A 406 52.000 23.718 286.255 1.00125.47 C ANISOU 3356 C HIS A 406 14440 17286 15948 -1149 -360 155 C ATOM 3357 O HIS A 406 53.185 23.491 285.983 1.00134.70 O ANISOU 3357 O HIS A 406 15393 18673 17113 -1190 -359 -20 O ATOM 3358 CB HIS A 406 50.237 23.211 284.541 1.00113.77 C ANISOU 3358 CB HIS A 406 13135 15593 14501 -1184 -232 327 C ATOM 3359 CG HIS A 406 49.311 22.195 283.953 1.00122.25 C ANISOU 3359 CG HIS A 406 14252 16558 15639 -1056 -199 396 C ATOM 3360 ND1 HIS A 406 48.044 21.963 284.442 1.00127.47 N ANISOU 3360 ND1 HIS A 406 15083 17014 16335 -928 -217 542 N ATOM 3361 CD2 HIS A 406 49.481 21.333 282.927 1.00127.42 C ANISOU 3361 CD2 HIS A 406 14793 17290 16330 -1041 -148 326 C ATOM 3362 CE1 HIS A 406 47.469 21.009 283.731 1.00127.62 C ANISOU 3362 CE1 HIS A 406 15096 16985 16409 -848 -178 563 C ATOM 3363 NE2 HIS A 406 48.320 20.610 282.805 1.00124.95 N ANISOU 3363 NE2 HIS A 406 14591 16810 16074 -909 -138 436 N ATOM 3364 N ALA A 407 51.624 24.814 286.918 1.00115.50 N ANISOU 3364 N ALA A 407 13334 15918 14633 -1233 -384 243 N ATOM 3365 CA ALA A 407 52.630 25.727 287.450 1.00120.65 C ANISOU 3365 CA ALA A 407 13915 16701 15226 -1368 -418 143 C ATOM 3366 C ALA A 407 53.511 25.036 288.480 1.00137.44 C ANISOU 3366 C ALA A 407 15880 18954 17387 -1173 -519 26 C ATOM 3367 O ALA A 407 54.693 25.373 288.616 1.00140.41 O ANISOU 3367 O ALA A 407 16086 19530 17733 -1265 -539 -134 O ATOM 3368 CB ALA A 407 51.957 26.952 288.069 1.00122.91 C ANISOU 3368 CB ALA A 407 14421 16821 15457 -1458 -442 264 C ATOM 3369 N PHE A 408 52.951 24.076 289.220 1.00148.82 N ANISOU 3369 N PHE A 408 17380 20280 18884 -907 -587 100 N ATOM 3370 CA PHE A 408 53.745 23.288 290.157 1.00153.57 C ANISOU 3370 CA PHE A 408 17855 20980 19513 -692 -701 -4 C ATOM 3371 C PHE A 408 54.735 22.397 289.417 1.00153.89 C ANISOU 3371 C PHE A 408 17650 21224 19595 -644 -700 -187 C ATOM 3372 O PHE A 408 55.925 22.364 289.751 1.00159.10 O ANISOU 3372 O PHE A 408 18116 22086 20247 -620 -765 -367 O ATOM 3373 CB PHE A 408 52.814 22.460 291.046 1.00154.41 C ANISOU 3373 CB PHE A 408 18125 20890 19653 -443 -765 137 C ATOM 3374 CG PHE A 408 53.518 21.428 291.885 1.00149.31 C ANISOU 3374 CG PHE A 408 17388 20310 19033 -192 -893 49 C ATOM 3375 CD1 PHE A 408 54.687 21.737 292.567 1.00146.49 C ANISOU 3375 CD1 PHE A 408 16890 20125 18646 -172 -987 -100 C ATOM 3376 CD2 PHE A 408 52.993 20.150 292.010 1.00139.95 C ANISOU 3376 CD2 PHE A 408 16274 19004 17896 25 -929 113 C ATOM 3377 CE1 PHE A 408 55.328 20.784 293.344 1.00141.47 C ANISOU 3377 CE1 PHE A 408 16183 19541 18028 80 -1126 -187 C ATOM 3378 CE2 PHE A 408 53.625 19.195 292.784 1.00136.70 C ANISOU 3378 CE2 PHE A 408 15814 18628 17498 265 -1065 38 C ATOM 3379 CZ PHE A 408 54.795 19.512 293.454 1.00138.52 C ANISOU 3379 CZ PHE A 408 15903 19030 17698 303 -1170 -112 C ATOM 3380 N ARG A 409 54.264 21.672 288.399 1.00145.70 N ANISOU 3380 N ARG A 409 16609 20147 18603 -626 -629 -160 N ATOM 3381 CA ARG A 409 55.158 20.830 287.613 1.00139.21 C ANISOU 3381 CA ARG A 409 15553 19521 17821 -581 -622 -345 C ATOM 3382 C ARG A 409 56.158 21.651 286.808 1.00148.57 C ANISOU 3382 C ARG A 409 16550 20949 18951 -851 -542 -512 C ATOM 3383 O ARG A 409 57.187 21.109 286.389 1.00155.22 O ANISOU 3383 O ARG A 409 17145 22017 19813 -821 -552 -720 O ATOM 3384 CB ARG A 409 54.350 19.924 286.681 1.00128.70 C ANISOU 3384 CB ARG A 409 14276 18079 16543 -516 -558 -272 C ATOM 3385 CG ARG A 409 53.288 19.089 287.394 1.00126.06 C ANISOU 3385 CG ARG A 409 14139 17502 16257 -284 -618 -106 C ATOM 3386 CD ARG A 409 52.637 18.086 286.455 1.00130.24 C ANISOU 3386 CD ARG A 409 14690 17948 16846 -215 -563 -69 C ATOM 3387 NE ARG A 409 51.257 17.783 286.832 1.00133.20 N ANISOU 3387 NE ARG A 409 15302 18068 17241 -132 -553 134 N ATOM 3388 CZ ARG A 409 50.903 16.921 287.781 1.00132.80 C ANISOU 3388 CZ ARG A 409 15358 17882 17217 88 -642 202 C ATOM 3389 NH1 ARG A 409 51.825 16.265 288.474 1.00109.26 N ANISOU 3389 NH1 ARG A 409 12287 14980 14248 272 -766 90 N ATOM 3390 NH2 ARG A 409 49.619 16.717 288.044 1.00140.04 N ANISOU 3390 NH2 ARG A 409 16479 18588 18142 120 -610 375 N ATOM 3391 N SER A 410 55.884 22.940 286.584 1.00146.85 N ANISOU 3391 N SER A 410 16447 20690 18660 -1117 -464 -433 N ATOM 3392 CA SER A 410 56.860 23.800 285.920 1.00145.69 C ANISOU 3392 CA SER A 410 16148 20765 18441 -1408 -386 -586 C ATOM 3393 C SER A 410 58.159 23.861 286.711 1.00147.44 C ANISOU 3393 C SER A 410 16149 21214 18656 -1367 -473 -791 C ATOM 3394 O SER A 410 59.251 23.868 286.131 1.00149.77 O ANISOU 3394 O SER A 410 16197 21778 18929 -1494 -430 -1007 O ATOM 3395 CB SER A 410 56.285 25.203 285.731 1.00138.54 C ANISOU 3395 CB SER A 410 15458 19730 17452 -1680 -317 -446 C ATOM 3396 OG SER A 410 57.271 26.092 285.234 1.00137.79 O ANISOU 3396 OG SER A 410 15242 19840 17273 -1981 -248 -590 O ATOM 3397 N MET A 411 58.060 23.912 288.039 1.00148.51 N ANISOU 3397 N MET A 411 16365 21257 18804 -1194 -595 -736 N ATOM 3398 CA MET A 411 59.216 23.804 288.915 1.00156.30 C ANISOU 3398 CA MET A 411 17153 22441 19794 -1091 -709 -927 C ATOM 3399 C MET A 411 59.521 22.357 289.285 1.00153.74 C ANISOU 3399 C MET A 411 16709 22157 19549 -743 -830 -1017 C ATOM 3400 O MET A 411 60.117 22.105 290.339 1.00140.14 O ANISOU 3400 O MET A 411 14915 20497 17835 -556 -971 -1106 O ATOM 3401 CB MET A 411 58.995 24.637 290.178 1.00161.26 C ANISOU 3401 CB MET A 411 17938 22952 20381 -1085 -788 -830 C ATOM 3402 CG MET A 411 58.757 26.112 289.902 1.00164.66 C ANISOU 3402 CG MET A 411 18502 23331 20731 -1417 -693 -754 C ATOM 3403 SD MET A 411 58.550 27.100 291.397 1.00165.79 S ANISOU 3403 SD MET A 411 18817 23349 20828 -1403 -793 -665 S ATOM 3404 CE MET A 411 60.171 26.945 292.144 1.00168.55 C ANISOU 3404 CE MET A 411 18858 24008 21174 -1338 -905 -946 C ATOM 3405 N PHE A 412 59.113 21.409 288.445 1.00159.94 N ANISOU 3405 N PHE A 412 17487 22895 20388 -649 -786 -996 N ATOM 3406 CA PHE A 412 59.355 19.989 288.670 1.00152.08 C ANISOU 3406 CA PHE A 412 16403 21912 19468 -322 -903 -1079 C ATOM 3407 C PHE A 412 58.653 19.503 289.933 1.00138.22 C ANISOU 3407 C PHE A 412 14871 19915 17730 -58 -1034 -910 C ATOM 3408 O PHE A 412 57.848 18.571 289.884 1.00125.52 O ANISOU 3408 O PHE A 412 13405 18117 16169 117 -1052 -785 O ATOM 3409 CB PHE A 412 60.857 19.706 288.754 1.00154.28 C ANISOU 3409 CB PHE A 412 16357 22508 19756 -253 -986 -1386 C ATOM 3410 CG PHE A 412 61.629 20.181 287.554 1.00159.13 C ANISOU 3410 CG PHE A 412 16731 23394 20338 -533 -847 -1578 C ATOM 3411 CD1 PHE A 412 62.072 21.490 287.473 1.00158.30 C ANISOU 3411 CD1 PHE A 412 16577 23419 20151 -854 -760 -1625 C ATOM 3412 CD2 PHE A 412 61.911 19.318 286.507 1.00162.30 C ANISOU 3412 CD2 PHE A 412 16963 23921 20783 -484 -801 -1716 C ATOM 3413 CE1 PHE A 412 62.780 21.931 286.373 1.00160.90 C ANISOU 3413 CE1 PHE A 412 16701 24000 20434 -1140 -622 -1799 C ATOM 3414 CE2 PHE A 412 62.620 19.754 285.403 1.00160.74 C ANISOU 3414 CE2 PHE A 412 16545 23988 20541 -757 -663 -1898 C ATOM 3415 CZ PHE A 412 63.055 21.063 285.337 1.00161.29 C ANISOU 3415 CZ PHE A 412 16576 24187 20520 -1094 -569 -1937 C TER 3416 PHE A 412 HETATM 3417 CAE ZDG A2001 38.523 35.472 318.733 1.00113.89 C ANISOU 3417 CAE ZDG A2001 17511 13272 12489 -1030 -92 -908 C HETATM 3418 CAD ZDG A2001 38.396 34.520 317.542 1.00109.63 C ANISOU 3418 CAD ZDG A2001 16943 12734 11976 -1078 -81 -891 C HETATM 3419 CAA ZDG A2001 39.321 33.322 317.752 1.00109.73 C ANISOU 3419 CAA ZDG A2001 16962 12756 11973 -1054 -92 -914 C HETATM 3420 CAB ZDG A2001 39.986 32.350 317.916 1.00109.81 C ANISOU 3420 CAB ZDG A2001 16978 12772 11975 -1035 -101 -929 C HETATM 3421 CAC ZDG A2001 40.899 31.144 318.140 1.00116.18 C ANISOU 3421 CAC ZDG A2001 17788 13584 12772 -1010 -113 -951 C HETATM 3422 CAN ZDG A2001 40.495 29.873 317.767 1.00119.56 C ANISOU 3422 CAN ZDG A2001 18231 13991 13205 -1004 -131 -938 C HETATM 3423 CAM ZDG A2001 41.333 28.790 317.983 1.00120.70 C ANISOU 3423 CAM ZDG A2001 18382 14143 13336 -980 -140 -959 C HETATM 3424 CAJ ZDG A2001 42.136 31.331 318.729 1.00115.02 C ANISOU 3424 CAJ ZDG A2001 17616 13429 12655 -988 -147 -988 C HETATM 3425 CAK ZDG A2001 42.974 30.250 318.943 1.00110.43 C ANISOU 3425 CAK ZDG A2001 17031 12846 12080 -966 -164 -1006 C HETATM 3426 CAL ZDG A2001 42.574 28.980 318.571 1.00115.95 C ANISOU 3426 CAL ZDG A2001 17762 13560 12735 -962 -139 -989 C HETATM 3427 CAO ZDG A2001 43.502 27.787 318.810 1.00111.96 C ANISOU 3427 CAO ZDG A2001 17255 13054 12230 -936 -155 -1011 C HETATM 3428 CAS ZDG A2001 43.682 27.126 319.993 1.00110.58 C ANISOU 3428 CAS ZDG A2001 17113 12873 12031 -891 -189 -1025 C HETATM 3429 CBB ZDG A2001 42.989 27.464 321.309 1.00110.96 C ANISOU 3429 CBB ZDG A2001 17246 12905 12008 -806 -185 -1003 C HETATM 3430 NAP ZDG A2001 44.272 27.204 317.897 1.00118.27 N ANISOU 3430 NAP ZDG A2001 18048 13854 13036 -920 -123 -1009 N HETATM 3431 CAT ZDG A2001 44.405 27.578 316.503 1.00117.94 C ANISOU 3431 CAT ZDG A2001 18040 13806 12966 -879 -46 -974 C HETATM 3432 CAY ZDG A2001 45.468 28.377 316.108 1.00130.61 C ANISOU 3432 CAY ZDG A2001 19564 15386 14677 -852 63 -910 C HETATM 3433 CLA ZDG A2001 46.670 28.954 317.297 1.00137.28 CL ANISOU 3433 CLA ZDG A2001 20224 16161 15776 -904 -4 -914 CL HETATM 3434 CAX ZDG A2001 45.608 28.736 314.781 1.00135.28 C ANISOU 3434 CAX ZDG A2001 20225 15961 15214 -747 208 -831 C HETATM 3435 CAW ZDG A2001 44.691 28.301 313.841 1.00139.76 C ANISOU 3435 CAW ZDG A2001 20993 16534 15577 -657 167 -867 C HETATM 3436 CLB ZDG A2001 44.882 28.769 312.129 1.00153.02 CL ANISOU 3436 CLB ZDG A2001 22880 18173 17088 -414 350 -769 CL HETATM 3437 CAV ZDG A2001 43.629 27.502 314.232 1.00125.58 C ANISOU 3437 CAV ZDG A2001 19248 14733 13733 -714 -25 -964 C HETATM 3438 CAU ZDG A2001 43.483 27.137 315.563 1.00113.54 C ANISOU 3438 CAU ZDG A2001 17604 13229 12308 -831 -93 -991 C HETATM 3439 NAQ ZDG A2001 44.952 26.165 318.510 1.00117.87 N ANISOU 3439 NAQ ZDG A2001 17992 13800 12993 -900 -153 -1031 N HETATM 3440 CAR ZDG A2001 44.589 26.121 319.784 1.00119.91 C ANISOU 3440 CAR ZDG A2001 18277 14055 13230 -885 -201 -1044 C HETATM 3441 CBC ZDG A2001 45.110 25.114 320.806 1.00126.25 C ANISOU 3441 CBC ZDG A2001 19117 14846 14007 -829 -243 -1066 C HETATM 3442 OBE ZDG A2001 45.554 25.486 321.839 1.00132.79 O ANISOU 3442 OBE ZDG A2001 19996 15643 14816 -762 -321 -1108 O HETATM 3443 NBD ZDG A2001 45.051 23.694 320.486 1.00123.14 N ANISOU 3443 NBD ZDG A2001 18722 14458 13607 -832 -221 -1048 N HETATM 3444 NBF ZDG A2001 45.471 22.799 321.298 1.00116.89 N ANISOU 3444 NBF ZDG A2001 17961 13658 12795 -783 -242 -1055 N HETATM 3445 CBG ZDG A2001 44.504 21.906 321.461 1.00112.22 C ANISOU 3445 CBG ZDG A2001 17372 13043 12223 -769 -194 -984 C HETATM 3446 CBH ZDG A2001 44.877 20.729 322.363 1.00111.75 C ANISOU 3446 CBH ZDG A2001 17349 12967 12142 -696 -183 -962 C HETATM 3447 CBI ZDG A2001 46.239 20.104 322.079 1.00111.60 C ANISOU 3447 CBI ZDG A2001 17318 12967 12117 -715 -259 -1049 C HETATM 3448 CBJ ZDG A2001 47.221 21.152 321.575 1.00111.52 C ANISOU 3448 CBJ ZDG A2001 17267 12967 12138 -750 -307 -1115 C HETATM 3449 CBK ZDG A2001 46.563 22.265 320.772 1.00112.96 C ANISOU 3449 CBK ZDG A2001 17423 13162 12334 -799 -266 -1094 C HETATM 3450 N1 FMN A2002 34.586 -5.244 263.951 1.00 64.04 N HETATM 3451 C2 FMN A2002 33.945 -4.450 263.019 1.00 67.88 C HETATM 3452 O2 FMN A2002 34.348 -3.309 262.798 1.00 75.81 O HETATM 3453 N3 FMN A2002 32.850 -4.932 262.336 1.00 45.29 N HETATM 3454 C4 FMN A2002 32.394 -6.212 262.580 1.00 66.20 C HETATM 3455 O4 FMN A2002 31.415 -6.631 261.963 1.00 64.74 O HETATM 3456 C4A FMN A2002 33.038 -7.020 263.516 1.00 68.58 C HETATM 3457 N5 FMN A2002 32.585 -8.303 263.761 1.00 64.25 N HETATM 3458 C5A FMN A2002 33.227 -9.099 264.694 1.00 72.22 C HETATM 3459 C6 FMN A2002 32.764 -10.391 264.936 1.00 75.36 C HETATM 3460 C7 FMN A2002 33.399 -11.207 265.869 1.00 67.02 C HETATM 3461 C7M FMN A2002 32.846 -12.589 266.078 1.00 64.39 C HETATM 3462 C8 FMN A2002 34.509 -10.726 266.563 1.00 63.06 C HETATM 3463 C8M FMN A2002 35.226 -11.570 267.576 1.00 56.94 C HETATM 3464 C9 FMN A2002 34.966 -9.435 266.322 1.00 59.03 C HETATM 3465 C9A FMN A2002 34.334 -8.614 265.387 1.00 68.48 C HETATM 3466 N10 FMN A2002 34.788 -7.325 265.136 1.00 68.16 N HETATM 3467 C10 FMN A2002 34.142 -6.530 264.205 1.00 64.89 C HETATM 3468 C1' FMN A2002 35.978 -6.765 265.862 1.00 69.04 C HETATM 3469 C2' FMN A2002 35.543 -6.168 267.192 1.00 64.29 C HETATM 3470 O2' FMN A2002 34.635 -5.105 266.964 1.00 85.46 O HETATM 3471 C3' FMN A2002 36.827 -5.776 267.896 1.00 48.94 C HETATM 3472 O3' FMN A2002 37.382 -6.986 268.380 1.00 62.30 O HETATM 3473 C4' FMN A2002 36.652 -4.730 268.992 1.00 55.00 C HETATM 3474 O4' FMN A2002 37.920 -4.193 269.233 1.00 69.11 O HETATM 3475 C5' FMN A2002 36.140 -5.293 270.307 1.00 51.33 C HETATM 3476 O5' FMN A2002 35.448 -4.303 271.038 1.00 63.68 O HETATM 3477 P FMN A2002 35.301 -4.409 272.645 1.00 74.07 P HETATM 3478 O1P FMN A2002 35.260 -3.018 273.239 1.00 55.76 O HETATM 3479 O2P FMN A2002 34.047 -5.175 273.007 1.00 62.65 O HETATM 3480 O3P FMN A2002 36.495 -5.120 273.234 1.00 66.27 O HETATM 3481 C10 OLC A2003 29.462 47.035 298.300 1.00 95.71 C HETATM 3482 C9 OLC A2003 29.436 47.285 297.012 1.00 94.61 C HETATM 3483 C11 OLC A2003 30.674 46.870 299.147 1.00 91.67 C HETATM 3484 C8 OLC A2003 30.612 47.461 296.118 1.00 90.44 C HETATM 3485 C24 OLC A2003 31.543 50.052 284.601 1.00 93.72 C HETATM 3486 C12 OLC A2003 30.345 46.813 300.633 1.00 76.90 C HETATM 3487 C7 OLC A2003 30.478 46.680 294.816 1.00 88.38 C HETATM 3488 C6 OLC A2003 30.459 47.525 293.560 1.00 81.02 C HETATM 3489 C5 OLC A2003 31.735 47.457 292.757 1.00 83.84 C HETATM 3490 C4 OLC A2003 31.588 47.930 291.327 1.00 86.11 C HETATM 3491 C3 OLC A2003 30.249 47.619 290.695 1.00 80.03 C HETATM 3492 C2 OLC A2003 30.384 46.850 289.394 1.00 90.22 C HETATM 3493 C21 OLC A2003 30.801 49.506 286.927 1.00117.37 C HETATM 3494 C1 OLC A2003 30.029 47.657 288.184 1.00106.65 C HETATM 3495 C22 OLC A2003 31.964 49.606 285.981 1.00105.50 C HETATM 3496 O19 OLC A2003 28.945 47.691 287.678 1.00109.77 O HETATM 3497 O25 OLC A2003 32.666 50.469 283.847 1.00 91.67 O HETATM 3498 O23 OLC A2003 32.940 50.506 286.503 1.00 89.09 O HETATM 3499 O20 OLC A2003 31.077 48.337 287.728 1.00111.75 O HETATM 3500 C1 OLA A2004 39.735 29.525 291.534 1.00113.54 C HETATM 3501 O1 OLA A2004 40.738 29.993 290.950 1.00114.36 O HETATM 3502 O2 OLA A2004 39.440 28.326 291.340 1.00115.60 O HETATM 3503 C2 OLA A2004 38.889 30.398 292.456 1.00105.83 C HETATM 3504 C3 OLA A2004 38.804 31.812 291.884 1.00 97.68 C HETATM 3505 C4 OLA A2004 37.675 32.616 292.516 1.00 75.40 C HETATM 3506 C5 OLA A2004 37.526 33.913 291.739 1.00 75.08 C HETATM 3507 C6 OLA A2004 37.317 35.072 292.697 1.00 80.02 C HETATM 3508 C7 OLA A2004 38.218 36.232 292.309 1.00 74.33 C HETATM 3509 C8 OLA A2004 37.966 37.410 293.234 1.00 74.80 C HETATM 3510 C9 OLA A2004 38.983 38.491 292.920 1.00 84.02 C HETATM 3511 C10 OLA A2004 38.706 39.775 292.975 1.00 79.33 C HETATM 3512 C11 OLA A2004 37.345 40.315 293.359 1.00 66.83 C HETATM 3513 C12 OLA A2004 37.380 41.830 293.273 1.00 48.96 C HETATM 3514 C10 OLA A2005 26.344 43.870 293.390 1.00 85.49 C HETATM 3515 C11 OLA A2005 27.188 43.830 294.643 1.00 77.04 C HETATM 3516 C12 OLA A2005 26.284 43.742 295.869 1.00 75.79 C HETATM 3517 C13 OLA A2005 27.103 43.809 297.158 1.00 73.71 C HETATM 3518 C14 OLA A2005 26.261 43.449 298.383 1.00 72.52 C HETATM 3519 C15 OLA A2005 27.034 43.679 299.680 1.00 82.36 C HETATM 3520 C16 OLA A2005 26.280 43.120 300.886 1.00 94.76 C HETATM 3521 C17 OLA A2005 27.098 43.262 302.168 1.00 90.69 C HETATM 3522 C18 OLA A2005 26.438 42.552 303.346 1.00 72.18 C HETATM 3523 C6 OLA A2006 37.669 48.994 294.999 1.00 86.11 C HETATM 3524 C7 OLA A2006 36.427 48.251 295.474 1.00 95.31 C HETATM 3525 C8 OLA A2006 36.556 47.927 296.955 1.00104.59 C HETATM 3526 C9 OLA A2006 35.187 47.523 297.482 1.00110.13 C HETATM 3527 C10 OLA A2006 35.055 47.039 298.696 1.00109.22 C HETATM 3528 C11 OLA A2006 36.271 46.873 299.599 1.00104.31 C HETATM 3529 C12 OLA A2006 36.230 45.490 300.228 1.00 89.91 C HETATM 3530 C13 OLA A2006 35.506 45.571 301.559 1.00 82.19 C HETATM 3531 C14 OLA A2006 36.042 44.476 302.465 1.00 89.81 C HETATM 3532 C15 OLA A2006 35.184 44.407 303.715 1.00 93.53 C HETATM 3533 C16 OLA A2006 35.305 43.014 304.311 1.00 94.71 C HETATM 3534 C17 OLA A2006 35.392 43.137 305.823 1.00 86.37 C HETATM 3535 C18 OLA A2006 36.044 41.886 306.390 1.00 78.08 C HETATM 3536 C1 PEG A2007 20.777 20.775 279.667 1.00100.40 C HETATM 3537 O1 PEG A2007 20.641 19.916 280.806 1.00 86.30 O HETATM 3538 C2 PEG A2007 19.668 20.475 278.669 1.00 97.18 C HETATM 3539 O2 PEG A2007 20.160 20.625 277.336 1.00 95.61 O HETATM 3540 C3 PEG A2007 19.114 20.711 276.371 1.00 96.43 C HETATM 3541 C4 PEG A2007 18.756 19.307 275.909 1.00 91.48 C HETATM 3542 O4 PEG A2007 17.429 19.317 275.380 1.00 80.54 O HETATM 3543 O HOH A2101 32.051 -0.965 266.777 1.00 59.88 O HETATM 3544 O HOH A2102 35.261 -10.094 278.499 1.00 63.67 O HETATM 3545 O HOH A2103 34.502 34.467 284.184 1.00 53.81 O HETATM 3546 O HOH A2104 21.471 -1.670 278.122 1.00 55.72 O HETATM 3547 O HOH A2105 17.263 5.847 283.351 1.00 70.61 O HETATM 3548 O HOH A2106 24.324 23.139 277.910 1.00 54.78 O HETATM 3549 O HOH A2107 22.845 19.214 275.335 1.00 65.02 O HETATM 3550 O HOH A2108 28.664 32.074 281.974 1.00 72.18 O HETATM 3551 O HOH A2109 29.919 31.551 288.539 1.00 45.34 O CONECT 1258 1308 CONECT 1308 1258 CONECT 3417 3418 CONECT 3418 3417 3419 CONECT 3419 3418 3420 CONECT 3420 3419 3421 CONECT 3421 3420 3422 3424 CONECT 3422 3421 3423 CONECT 3423 3422 3426 CONECT 3424 3421 3425 CONECT 3425 3424 3426 CONECT 3426 3423 3425 3427 CONECT 3427 3426 3428 3430 CONECT 3428 3427 3429 3440 CONECT 3429 3428 CONECT 3430 3427 3431 3439 CONECT 3431 3430 3432 3438 CONECT 3432 3431 3433 3434 CONECT 3433 3432 CONECT 3434 3432 3435 CONECT 3435 3434 3436 3437 CONECT 3436 3435 CONECT 3437 3435 3438 CONECT 3438 3431 3437 CONECT 3439 3430 3440 CONECT 3440 3428 3439 3441 CONECT 3441 3440 3442 3443 CONECT 3442 3441 CONECT 3443 3441 3444 CONECT 3444 3443 3445 3449 CONECT 3445 3444 3446 CONECT 3446 3445 3447 CONECT 3447 3446 3448 CONECT 3448 3447 3449 CONECT 3449 3444 3448 CONECT 3450 3451 3467 CONECT 3451 3450 3452 3453 CONECT 3452 3451 CONECT 3453 3451 3454 CONECT 3454 3453 3455 3456 CONECT 3455 3454 CONECT 3456 3454 3457 3467 CONECT 3457 3456 3458 CONECT 3458 3457 3459 3465 CONECT 3459 3458 3460 CONECT 3460 3459 3461 3462 CONECT 3461 3460 CONECT 3462 3460 3463 3464 CONECT 3463 3462 CONECT 3464 3462 3465 CONECT 3465 3458 3464 3466 CONECT 3466 3465 3467 3468 CONECT 3467 3450 3456 3466 CONECT 3468 3466 3469 CONECT 3469 3468 3470 3471 CONECT 3470 3469 CONECT 3471 3469 3472 3473 CONECT 3472 3471 CONECT 3473 3471 3474 3475 CONECT 3474 3473 CONECT 3475 3473 3476 CONECT 3476 3475 3477 CONECT 3477 3476 3478 3479 3480 CONECT 3478 3477 CONECT 3479 3477 CONECT 3480 3477 CONECT 3481 3482 3483 CONECT 3482 3481 3484 CONECT 3483 3481 3486 CONECT 3484 3482 3487 CONECT 3485 3495 3497 CONECT 3486 3483 CONECT 3487 3484 3488 CONECT 3488 3487 3489 CONECT 3489 3488 3490 CONECT 3490 3489 3491 CONECT 3491 3490 3492 CONECT 3492 3491 3494 CONECT 3493 3495 3499 CONECT 3494 3492 3496 3499 CONECT 3495 3485 3493 3498 CONECT 3496 3494 CONECT 3497 3485 CONECT 3498 3495 CONECT 3499 3493 3494 CONECT 3500 3501 3502 3503 CONECT 3501 3500 CONECT 3502 3500 CONECT 3503 3500 3504 CONECT 3504 3503 3505 CONECT 3505 3504 3506 CONECT 3506 3505 3507 CONECT 3507 3506 3508 CONECT 3508 3507 3509 CONECT 3509 3508 3510 CONECT 3510 3509 3511 CONECT 3511 3510 3512 CONECT 3512 3511 3513 CONECT 3513 3512 CONECT 3514 3515 CONECT 3515 3514 3516 CONECT 3516 3515 3517 CONECT 3517 3516 3518 CONECT 3518 3517 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3521 CONECT 3521 3520 3522 CONECT 3522 3521 CONECT 3523 3524 CONECT 3524 3523 3525 CONECT 3525 3524 3526 CONECT 3526 3525 3527 CONECT 3527 3526 3528 CONECT 3528 3527 3529 CONECT 3529 3528 3530 CONECT 3530 3529 3531 CONECT 3531 3530 3532 CONECT 3532 3531 3533 CONECT 3533 3532 3534 CONECT 3534 3533 3535 CONECT 3535 3534 CONECT 3536 3537 3538 CONECT 3537 3536 CONECT 3538 3536 3539 CONECT 3539 3538 3540 CONECT 3540 3539 3541 CONECT 3541 3540 3542 CONECT 3542 3541 MASTER 315 0 7 17 10 0 13 6 3542 1 128 35 END