HEADER SIGNALING PROTEIN 08-JUN-17 5XRA TITLE CRYSTAL STRUCTURE OF THE HUMAN CB1 IN COMPLEX WITH AGONIST AM11542 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 3-148,UNP RESIDUES 332- COMPND 5 414; COMPND 6 SYNONYM: CB1,CANN6,CB1,CANN6; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, DESULFOVIBRIO VULGARIS (STRAIN SOURCE 3 HILDENBOROUGH / ATCC 29579 / DSM 644 / NCIMB 8303); SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606, 882; SOURCE 6 STRAIN: HILDENBOROUGH / ATCC 29579 / DSM 644 / NCIMB 8303; SOURCE 7 GENE: CNR1, CNR, DVU_2680; SOURCE 8 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS MEMBRANE PROTEIN, HUMAN G PROTEIN-COUPLED RECEPTOR, STABILIZING KEYWDS 2 AGONISTS, LIPIDIC CUBIC PHASE, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.HUA,K.VEMURI,P.S.NIKAS,R.B.LAPRAIRIE,Y.WU,L.QU,M.PU,A.KORDE,J.SHAN, AUTHOR 2 J.H.HO,G.W.HAN,K.DING,X.LI,H.LIU,M.A.HANSON,S.ZHAO,L.M.BOHN, AUTHOR 3 A.MAKRIYANNIS,R.C.STEVENS,Z.J.LIU REVDAT 5 18-OCT-17 5XRA 1 REMARK REVDAT 4 16-AUG-17 5XRA 1 REMARK REVDAT 3 09-AUG-17 5XRA 1 JRNL REVDAT 2 19-JUL-17 5XRA 1 JRNL REVDAT 1 12-JUL-17 5XRA 0 JRNL AUTH T.HUA,K.VEMURI,S.P.NIKAS,R.B.LAPRAIRIE,Y.WU,L.QU,M.PU, JRNL AUTH 2 A.KORDE,S.JIANG,J.H.HO,G.W.HAN,K.DING,X.LI,H.LIU,M.A.HANSON, JRNL AUTH 3 S.ZHAO,L.M.BOHN,A.MAKRIYANNIS,R.C.STEVENS,Z.J.LIU JRNL TITL CRYSTAL STRUCTURES OF AGONIST-BOUND HUMAN CANNABINOID JRNL TITL 2 RECEPTOR CB1 JRNL REF NATURE V. 547 468 2017 JRNL REFN ESSN 1476-4687 JRNL PMID 28678776 JRNL DOI 10.1038/NATURE23272 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.10.1_2155 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) : 37.91 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6 REMARK 3 NUMBER OF REFLECTIONS : 16669 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.235 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.830 REMARK 3 FREE R VALUE TEST SET COUNT : 805 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 37.9164 - 5.0847 0.96 2833 150 0.1973 0.1973 REMARK 3 2 5.0847 - 4.0373 0.95 2712 140 0.1998 0.2613 REMARK 3 3 4.0373 - 3.5274 0.95 2670 141 0.2483 0.2639 REMARK 3 4 3.5274 - 3.2051 0.94 2615 141 0.2834 0.2953 REMARK 3 5 3.2051 - 2.9754 0.91 2530 128 0.3411 0.3856 REMARK 3 6 2.9754 - 2.8001 0.90 2504 105 0.3920 0.4027 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) : 0.530 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.490 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 : 0.003 3539 REMARK 3 ANGLE : 0.732 4811 REMARK 3 CHIRALITY : 0.040 562 REMARK 3 PLANARITY : 0.004 580 REMARK 3 DIHEDRAL : 17.271 2033 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 104 THROUGH 306 ) REMARK 3 ORIGIN FOR THE GROUP (A): -45.7418-153.3025 304.1440 REMARK 3 T TENSOR REMARK 3 T11: 0.4955 T22: 0.3907 REMARK 3 T33: 0.4658 T12: 0.0257 REMARK 3 T13: -0.0231 T23: -0.0634 REMARK 3 L TENSOR REMARK 3 L11: 4.3323 L22: 1.3921 REMARK 3 L33: 2.6335 L12: 0.1288 REMARK 3 L13: -0.2432 L23: 0.4963 REMARK 3 S TENSOR REMARK 3 S11: 0.0429 S12: 0.3638 S13: -0.2032 REMARK 3 S21: -0.1574 S22: 0.0364 S23: -0.1851 REMARK 3 S31: -0.0318 S32: -0.1245 S33: -0.0875 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1148 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.2031-118.0939 257.7939 REMARK 3 T TENSOR REMARK 3 T11: 0.6676 T22: 0.5114 REMARK 3 T33: 0.8596 T12: -0.0197 REMARK 3 T13: 0.0125 T23: 0.0200 REMARK 3 L TENSOR REMARK 3 L11: 6.7869 L22: 5.0614 REMARK 3 L33: 6.1613 L12: -1.9751 REMARK 3 L13: 0.3850 L23: -1.6483 REMARK 3 S TENSOR REMARK 3 S11: -0.0179 S12: -0.2164 S13: 0.3033 REMARK 3 S21: 0.3632 S22: 0.0139 S23: -0.1697 REMARK 3 S31: -0.3488 S32: -0.0999 S33: 0.0210 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 337 THROUGH 414 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.6663-150.5189 299.6294 REMARK 3 T TENSOR REMARK 3 T11: 0.5129 T22: 0.6980 REMARK 3 T33: 0.7613 T12: 0.0487 REMARK 3 T13: 0.1202 T23: -0.0593 REMARK 3 L TENSOR REMARK 3 L11: 2.0424 L22: 7.0438 REMARK 3 L33: 2.1106 L12: 2.4253 REMARK 3 L13: 1.0435 L23: 1.1763 REMARK 3 S TENSOR REMARK 3 S11: -0.1483 S12: 0.0702 S13: 0.0338 REMARK 3 S21: 0.1335 S22: 0.1464 S23: 0.1466 REMARK 3 S31: -0.1037 S32: 0.2170 S33: 0.0220 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THERE ARE SOME UNKNOWN DENSITIES LOCATED REMARK 3 AT THE END OF THE SIDE CHAIN OF SER152, WHICH MIGHT BE REMARK 3 PHOSPHORYLATION REMARK 3 BUT NOT CHEMICALLY CONFIRMED YET. THEY HAVE NOT BEEN MODELLED. REMARK 4 REMARK 4 5XRA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JUN-17. REMARK 100 THE DEPOSITION ID IS D_1300004019. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-DEC-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA 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 : NULL 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 : 16685 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 37.910 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5 REMARK 200 DATA REDUNDANCY : 6.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.4100 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) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.80 REMARK 200 R MERGE FOR SHELL (I) : 0.56200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.070 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: 5TGZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE TRIHYDRATE PH REMARK 280 6.4, 300-350 MM C4H4KNAO6, 30% PEG400, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 293.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21 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,-Z+1/2 REMARK 290 4555 -X+1/2,-Y,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.02500 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.45000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.02500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.45000 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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 99 REMARK 465 GLU A 100 REMARK 465 ASN A 101 REMARK 465 PHE A 102 REMARK 465 MET A 103 REMARK 465 PRO A 332 REMARK 465 ASP A 333 REMARK 465 GLN A 334 REMARK 465 ALA A 335 REMARK 465 ARG A 336 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 LYS A 183 CG CD CE NZ REMARK 470 LYS A 232 NZ REMARK 470 LYS A1003 CG CD CE NZ REMARK 470 LYS A1087 CG CD CE NZ REMARK 470 ARG A1145 CZ NH1 NH2 REMARK 470 ILE A1148 CG1 CG2 CD1 REMARK 470 MET A 337 CG SD CE REMARK 470 ARG A 400 CG CD NE CZ NH1 NH2 REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 603 REMARK 610 OLA A 604 REMARK 610 OLC A 605 REMARK 610 OLC A 606 DBREF 5XRA A 99 306 UNP P21554 CNR1_HUMAN 99 306 DBREF 5XRA A 1003 1148 UNP P00323 FLAV_DESVH 3 148 DBREF 5XRA A 356 414 UNP P21554 CNR1_HUMAN 332 414 SEQADV 5XRA ALA A 210 UNP P21554 THR 210 ENGINEERED MUTATION SEQADV 5XRA LYS A 273 UNP P21554 GLU 273 ENGINEERED MUTATION SEQADV 5XRA VAL A 283 UNP P21554 THR 283 ENGINEERED MUTATION SEQADV 5XRA ALA A 1002 UNP P21554 LINKER SEQADV 5XRA TRP A 1098 UNP P00323 TYR 98 ENGINEERED MUTATION SEQADV 5XRA GLU A 340 UNP P21554 ARG 340 ENGINEERED MUTATION SEQRES 1 A 438 GLY GLU ASN PHE MET ASP ILE GLU CYS PHE MET VAL LEU SEQRES 2 A 438 ASN PRO SER GLN GLN LEU ALA ILE ALA VAL LEU SER LEU SEQRES 3 A 438 THR LEU GLY THR PHE THR VAL LEU GLU ASN LEU LEU VAL SEQRES 4 A 438 LEU CYS VAL ILE LEU HIS SER ARG SER LEU ARG CYS ARG SEQRES 5 A 438 PRO SER TYR HIS PHE ILE GLY SER LEU ALA VAL ALA ASP SEQRES 6 A 438 LEU LEU GLY SER VAL ILE PHE VAL TYR SER PHE ILE ASP SEQRES 7 A 438 PHE HIS VAL PHE HIS ARG LYS ASP SER ARG ASN VAL PHE SEQRES 8 A 438 LEU PHE LYS LEU GLY GLY VAL THR ALA SER PHE THR ALA SEQRES 9 A 438 SER VAL GLY SER LEU PHE LEU ALA ALA ILE ASP ARG TYR SEQRES 10 A 438 ILE SER ILE HIS ARG PRO LEU ALA TYR LYS ARG ILE VAL SEQRES 11 A 438 THR ARG PRO LYS ALA VAL VAL ALA PHE CYS LEU MET TRP SEQRES 12 A 438 THR ILE ALA ILE VAL ILE ALA VAL LEU PRO LEU LEU GLY SEQRES 13 A 438 TRP ASN CYS GLU LYS LEU GLN SER VAL CYS SER ASP ILE SEQRES 14 A 438 PHE PRO HIS ILE ASP LYS THR TYR LEU MET PHE TRP ILE SEQRES 15 A 438 GLY VAL VAL SER VAL LEU LEU LEU PHE ILE VAL TYR ALA SEQRES 16 A 438 TYR MET TYR ILE LEU TRP LYS ALA HIS SER HIS ALA VAL SEQRES 17 A 438 ALA LYS ALA LEU ILE VAL TYR GLY SER THR THR GLY ASN SEQRES 18 A 438 THR GLU TYR THR ALA GLU THR ILE ALA ARG GLU LEU ALA SEQRES 19 A 438 ASP ALA GLY TYR GLU VAL ASP SER ARG ASP ALA ALA SER SEQRES 20 A 438 VAL GLU ALA GLY GLY LEU PHE GLU GLY PHE ASP LEU VAL SEQRES 21 A 438 LEU LEU GLY CYS SER THR TRP GLY ASP ASP SER ILE GLU SEQRES 22 A 438 LEU GLN ASP ASP PHE ILE PRO LEU PHE ASP SER LEU GLU SEQRES 23 A 438 GLU THR GLY ALA GLN GLY ARG LYS VAL ALA CYS PHE GLY SEQRES 24 A 438 CYS GLY ASP SER SER TRP GLU TYR PHE CYS GLY ALA VAL SEQRES 25 A 438 ASP ALA ILE GLU GLU LYS LEU LYS ASN LEU GLY ALA GLU SEQRES 26 A 438 ILE VAL GLN ASP GLY LEU ARG ILE ASP GLY ASP PRO ARG SEQRES 27 A 438 ALA ALA ARG ASP ASP ILE VAL GLY TRP ALA HIS ASP VAL SEQRES 28 A 438 ARG GLY ALA ILE PRO ASP GLN ALA ARG MET ASP ILE GLU SEQRES 29 A 438 LEU ALA LYS THR LEU VAL LEU ILE LEU VAL VAL LEU ILE SEQRES 30 A 438 ILE CYS TRP GLY PRO LEU LEU ALA ILE MET VAL TYR ASP SEQRES 31 A 438 VAL PHE GLY LYS MET ASN LYS LEU ILE LYS THR VAL PHE SEQRES 32 A 438 ALA PHE CYS SER MET LEU CYS LEU LEU ASN SER THR VAL SEQRES 33 A 438 ASN PRO ILE ILE TYR ALA LEU ARG SER LYS ASP LEU ARG SEQRES 34 A 438 HIS ALA PHE ARG SER MET PHE PRO SER HET FMN A 601 31 HET 8D3 A 602 28 HET OLA A 603 13 HET OLA A 604 13 HET OLC A 605 17 HET OLC A 606 13 HET PEG A 607 7 HET CLR A 608 28 HETNAM FMN FLAVIN MONONUCLEOTIDE HETNAM 8D3 (6AR,10AR)-3-(8-BROMANYL-2-METHYL-OCTAN-2-YL)-6,6,9- HETNAM 2 8D3 TRIMETHYL-6A,7,10,10A-TETRAHYDROBENZO[C]CHROMEN-1-OL HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM CLR CHOLESTEROL HETSYN FMN RIBOFLAVIN MONOPHOSPHATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 FMN C17 H21 N4 O9 P FORMUL 3 8D3 C25 H37 BR O2 FORMUL 4 OLA 2(C18 H34 O2) FORMUL 6 OLC 2(C21 H40 O4) FORMUL 8 PEG C4 H10 O3 FORMUL 9 CLR C27 H46 O HELIX 1 AA1 ASP A 104 MET A 109 5 6 HELIX 2 AA2 ASN A 112 ARG A 148 1 37 HELIX 3 AA3 TYR A 153 VAL A 179 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 ASN A 256 GLN A 261 1 6 HELIX 8 AA8 ASP A 272 VAL A 306 1 35 HELIX 9 AA9 GLY A 1013 ALA A 1029 1 17 HELIX 10 AB1 ALA A 1039 VAL A 1041 5 3 HELIX 11 AB2 ASP A 1070 SER A 1077 1 8 HELIX 12 AB3 LEU A 1078 GLY A 1082 5 5 HELIX 13 AB4 CYS A 1102 GLY A 1116 1 15 HELIX 14 AB5 ASP A 1129 ALA A 1132 5 4 HELIX 15 AB6 ALA A 1133 ALA A 1147 1 15 HELIX 16 AB7 ASP A 338 GLY A 369 1 32 HELIX 17 AB8 ASN A 372 TYR A 397 1 26 HELIX 18 AB9 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 LEU A1124 N CYS A1090 SSBOND 1 CYS A 257 CYS A 264 1555 1555 2.04 CRYST1 66.050 75.870 138.900 90.00 90.00 90.00 P 21 2 21 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 0.015140 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013180 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007199 0.00000 ATOM 1 N ASP A 104 -43.566-180.918 309.935 1.00106.59 N ANISOU 1 N ASP A 104 14055 7097 19345 227 -537 -68 N ATOM 2 CA ASP A 104 -42.274-180.863 310.610 1.00109.43 C ANISOU 2 CA ASP A 104 14390 7459 19729 507 -618 173 C ATOM 3 C ASP A 104 -41.687-179.457 310.544 1.00106.87 C ANISOU 3 C ASP A 104 13992 7498 19116 623 -669 116 C ATOM 4 O ASP A 104 -41.277-178.999 309.477 1.00107.16 O ANISOU 4 O ASP A 104 13955 7680 19081 679 -629 -278 O ATOM 5 CB ASP A 104 -41.303-181.868 309.994 1.00115.47 C ANISOU 5 CB ASP A 104 15118 7981 20774 698 -592 -45 C ATOM 6 CG ASP A 104 -39.934-181.820 310.637 1.00118.61 C ANISOU 6 CG ASP A 104 15465 8400 21200 996 -679 178 C ATOM 7 OD1 ASP A 104 -39.684-182.619 311.562 1.00124.51 O ANISOU 7 OD1 ASP A 104 16264 8928 22117 1081 -727 537 O ATOM 8 OD2 ASP A 104 -39.107-180.980 310.226 1.00114.66 O ANISOU 8 OD2 ASP A 104 14867 8150 20548 1144 -699 -2 O ATOM 9 N ILE A 105 -41.630-178.785 311.697 1.00104.98 N ANISOU 9 N ILE A 105 13768 7416 18704 656 -756 516 N ATOM 10 CA ILE A 105 -41.214-177.386 311.726 1.00 99.80 C ANISOU 10 CA ILE A 105 13050 7098 17771 734 -811 483 C ATOM 11 C ILE A 105 -39.758-177.233 311.302 1.00 97.82 C ANISOU 11 C ILE A 105 12697 6915 17556 1002 -837 304 C ATOM 12 O ILE A 105 -39.388-176.229 310.679 1.00 93.85 O ANISOU 12 O ILE A 105 12125 6683 16849 1041 -823 53 O ATOM 13 CB ILE A 105 -41.459-176.790 313.126 1.00 97.57 C ANISOU 13 CB ILE A 105 12799 7042 17230 702 -895 952 C ATOM 14 CG1 ILE A 105 -42.910-177.016 313.558 1.00 99.06 C ANISOU 14 CG1 ILE A 105 13073 7199 17367 425 -850 1130 C ATOM 15 CG2 ILE A 105 -41.130-175.304 313.147 1.00 89.14 C ANISOU 15 CG2 ILE A 105 11672 6495 15704 735 -914 868 C ATOM 16 CD1 ILE A 105 -43.231-176.484 314.946 1.00 97.95 C ANISOU 16 CD1 ILE A 105 12955 7345 16916 375 -910 1574 C ATOM 17 N GLU A 106 -38.914-178.223 311.603 1.00 99.74 N ANISOU 17 N GLU A 106 12921 6950 18025 1182 -863 421 N ATOM 18 CA GLU A 106 -37.477-178.078 311.390 1.00 99.63 C ANISOU 18 CA GLU A 106 12788 7022 18045 1448 -900 310 C ATOM 19 C GLU A 106 -37.093-178.034 309.915 1.00 94.89 C ANISOU 19 C GLU A 106 12111 6460 17485 1476 -799 -214 C ATOM 20 O GLU A 106 -35.980-177.602 309.594 1.00 91.51 O ANISOU 20 O GLU A 106 11562 6190 17016 1661 -813 -362 O ATOM 21 CB GLU A 106 -36.732-179.217 312.087 1.00109.03 C ANISOU 21 CB GLU A 106 13977 7969 19479 1635 -955 574 C ATOM 22 CG GLU A 106 -35.653-178.754 313.052 1.00113.96 C ANISOU 22 CG GLU A 106 14514 8787 20000 1861 -1084 869 C ATOM 23 CD GLU A 106 -34.924-179.910 313.702 1.00124.52 C ANISOU 23 CD GLU A 106 15848 9891 21573 2058 -1142 1127 C ATOM 24 OE1 GLU A 106 -35.281-180.282 314.839 1.00128.31 O ANISOU 24 OE1 GLU A 106 16406 10312 22035 2032 -1209 1565 O ATOM 25 OE2 GLU A 106 -33.997-180.456 313.070 1.00128.32 O ANISOU 25 OE2 GLU A 106 16247 10258 22252 2241 -1116 894 O ATOM 26 N CYS A 107 -37.977-178.464 309.010 1.00 95.13 N ANISOU 26 N CYS A 107 12191 6379 17574 1291 -699 -500 N ATOM 27 CA CYS A 107 -37.657-178.424 307.586 1.00 94.30 C ANISOU 27 CA CYS A 107 12006 6362 17463 1305 -602 -996 C ATOM 28 C CYS A 107 -37.596-177.004 307.039 1.00 90.28 C ANISOU 28 C CYS A 107 11437 6225 16641 1274 -584 -1194 C ATOM 29 O CYS A 107 -37.066-176.800 305.941 1.00 89.52 O ANISOU 29 O CYS A 107 11250 6276 16489 1326 -510 -1566 O ATOM 30 CB CYS A 107 -38.680-179.235 306.787 1.00 96.43 C ANISOU 30 CB CYS A 107 12335 6455 17850 1104 -512 -1248 C ATOM 31 SG CYS A 107 -38.444-181.025 306.843 1.00104.07 S ANISOU 31 SG CYS A 107 13335 6967 19241 1176 -491 -1227 S ATOM 32 N PHE A 108 -38.119-176.025 307.774 1.00 86.58 N ANISOU 32 N PHE A 108 11016 5915 15965 1191 -646 -952 N ATOM 33 CA PHE A 108 -38.209-174.645 307.318 1.00 81.67 C ANISOU 33 CA PHE A 108 10362 5717 14953 1120 -616 -1093 C ATOM 34 C PHE A 108 -37.070-173.776 307.833 1.00 82.33 C ANISOU 34 C PHE A 108 10360 6078 14846 1283 -673 -952 C ATOM 35 O PHE A 108 -37.136-172.549 307.702 1.00 78.74 O ANISOU 35 O PHE A 108 9891 6001 14025 1208 -654 -978 O ATOM 36 CB PHE A 108 -39.546-174.033 307.750 1.00 77.52 C ANISOU 36 CB PHE A 108 9937 5374 14144 882 -620 -916 C ATOM 37 CG PHE A 108 -40.753-174.758 307.224 1.00 75.11 C ANISOU 37 CG PHE A 108 9696 4862 13982 687 -564 -1069 C ATOM 38 CD1 PHE A 108 -41.159-175.959 307.783 1.00 73.94 C ANISOU 38 CD1 PHE A 108 9609 4296 14188 649 -587 -897 C ATOM 39 CD2 PHE A 108 -41.497-174.225 306.186 1.00 73.55 C ANISOU 39 CD2 PHE A 108 9490 4896 13559 532 -491 -1371 C ATOM 40 CE1 PHE A 108 -42.270-176.622 307.305 1.00 75.08 C ANISOU 40 CE1 PHE A 108 9801 4278 14450 442 -528 -1049 C ATOM 41 CE2 PHE A 108 -42.615-174.882 305.707 1.00 72.95 C ANISOU 41 CE2 PHE A 108 9450 4663 13603 342 -448 -1530 C ATOM 42 CZ PHE A 108 -43.000-176.082 306.267 1.00 73.71 C ANISOU 42 CZ PHE A 108 9603 4336 14068 288 -465 -1386 C ATOM 43 N MET A 109 -36.031-174.373 308.407 1.00 86.85 N ANISOU 43 N MET A 109 10864 6469 15666 1504 -743 -807 N ATOM 44 CA MET A 109 -35.033-173.638 309.172 1.00 88.70 C ANISOU 44 CA MET A 109 11011 6961 15730 1644 -825 -605 C ATOM 45 C MET A 109 -33.671-173.685 308.494 1.00 97.39 C ANISOU 45 C MET A 109 11947 8103 16953 1853 -797 -866 C ATOM 46 O MET A 109 -33.192-174.762 308.122 1.00 98.17 O ANISOU 46 O MET A 109 11997 7890 17415 2006 -783 -1000 O ATOM 47 CB MET A 109 -34.921-174.199 310.590 1.00 87.12 C ANISOU 47 CB MET A 109 10842 6596 15662 1738 -956 -156 C ATOM 48 CG MET A 109 -36.183-174.074 311.419 1.00 81.52 C ANISOU 48 CG MET A 109 10273 5909 14792 1533 -982 142 C ATOM 49 SD MET A 109 -35.890-174.487 313.148 1.00 79.10 S ANISOU 49 SD MET A 109 9979 5548 14528 1650 -1138 701 S ATOM 50 CE MET A 109 -37.520-174.226 313.842 1.00 77.61 C ANISOU 50 CE MET A 109 9941 5447 14099 1360 -1119 949 C ATOM 51 N VAL A 110 -33.054-172.514 308.341 1.00103.79 N ANISOU 51 N VAL A 110 12669 9304 17463 1853 -781 -940 N ATOM 52 CA VAL A 110 -31.637-172.438 308.007 1.00107.45 C ANISOU 52 CA VAL A 110 12948 9871 18007 2055 -774 -1102 C ATOM 53 C VAL A 110 -30.846-172.895 309.224 1.00109.59 C ANISOU 53 C VAL A 110 13148 10047 18445 2262 -921 -776 C ATOM 54 O VAL A 110 -30.888-172.262 310.284 1.00109.74 O ANISOU 54 O VAL A 110 13185 10267 18245 2224 -1018 -474 O ATOM 55 CB VAL A 110 -31.241-171.015 307.594 1.00106.45 C ANISOU 55 CB VAL A 110 12748 10184 17512 1964 -715 -1231 C ATOM 56 CG1 VAL A 110 -29.822-170.990 307.053 1.00109.48 C ANISOU 56 CG1 VAL A 110 12924 10683 17989 2145 -676 -1454 C ATOM 57 CG2 VAL A 110 -32.219-170.465 306.577 1.00104.44 C ANISOU 57 CG2 VAL A 110 12592 10051 17040 1746 -593 -1452 C ATOM 58 N LEU A 111 -30.127-174.003 309.080 1.00106.89 N ANISOU 58 N LEU A 111 12716 9406 18490 2490 -942 -840 N ATOM 59 CA LEU A 111 -29.475-174.640 310.211 1.00104.15 C ANISOU 59 CA LEU A 111 12318 8939 18315 2694 -1085 -495 C ATOM 60 C LEU A 111 -27.957-174.611 310.121 1.00 96.87 C ANISOU 60 C LEU A 111 11169 8180 17457 2932 -1111 -601 C ATOM 61 O LEU A 111 -27.285-175.117 311.026 1.00 97.06 O ANISOU 61 O LEU A 111 11130 8170 17580 3114 -1230 -323 O ATOM 62 CB LEU A 111 -29.980-176.081 310.344 1.00111.25 C ANISOU 62 CB LEU A 111 13352 9456 19463 2690 -1068 -371 C ATOM 63 CG LEU A 111 -31.486-176.188 310.603 1.00113.30 C ANISOU 63 CG LEU A 111 13817 9560 19671 2448 -1053 -217 C ATOM 64 CD1 LEU A 111 -31.955-177.633 310.721 1.00117.35 C ANISOU 64 CD1 LEU A 111 14449 9690 20449 2432 -1028 -107 C ATOM 65 CD2 LEU A 111 -31.846-175.414 311.850 1.00113.18 C ANISOU 65 CD2 LEU A 111 13840 9712 19451 2402 -1183 179 C ATOM 66 N ASN A 112 -27.404-174.022 309.075 1.00 90.67 N ANISOU 66 N ASN A 112 10253 7597 16600 2931 -1002 -982 N ATOM 67 CA ASN A 112 -25.959-173.889 308.958 1.00 89.64 C ANISOU 67 CA ASN A 112 9882 7669 16509 3135 -1014 -1102 C ATOM 68 C ASN A 112 -25.467-172.831 309.939 1.00 84.84 C ANISOU 68 C ASN A 112 9173 7414 15648 3138 -1137 -867 C ATOM 69 O ASN A 112 -25.908-171.677 309.861 1.00 77.87 O ANISOU 69 O ASN A 112 8355 6828 14405 2901 -1086 -893 O ATOM 70 CB ASN A 112 -25.593-173.523 307.523 1.00 89.80 C ANISOU 70 CB ASN A 112 9799 7852 16470 3084 -837 -1571 C ATOM 71 CG ASN A 112 -24.097-173.480 307.286 1.00 94.04 C ANISOU 71 CG ASN A 112 10073 8600 17059 3280 -823 -1727 C ATOM 72 OD1 ASN A 112 -23.305-173.729 308.190 1.00 97.59 O ANISOU 72 OD1 ASN A 112 10409 9076 17596 3466 -954 -1495 O ATOM 73 ND2 ASN A 112 -23.703-173.173 306.055 1.00 94.68 N ANISOU 73 ND2 ASN A 112 10046 8858 17070 3235 -660 -2119 N ATOM 74 N PRO A 113 -24.580-173.176 310.880 1.00 84.95 N ANISOU 74 N PRO A 113 9043 7447 15788 3370 -1292 -628 N ATOM 75 CA PRO A 113 -24.138-172.174 311.868 1.00 80.17 C ANISOU 75 CA PRO A 113 8349 7244 14869 3326 -1408 -410 C ATOM 76 C PRO A 113 -23.499-170.946 311.245 1.00 78.51 C ANISOU 76 C PRO A 113 7994 7442 14395 3202 -1308 -694 C ATOM 77 O PRO A 113 -23.736-169.827 311.718 1.00 77.09 O ANISOU 77 O PRO A 113 7851 7561 13877 3006 -1328 -606 O ATOM 78 CB PRO A 113 -23.143-172.961 312.732 1.00 81.81 C ANISOU 78 CB PRO A 113 8380 7384 15318 3648 -1582 -174 C ATOM 79 CG PRO A 113 -23.576-174.383 312.598 1.00 83.82 C ANISOU 79 CG PRO A 113 8801 7208 15840 3721 -1541 -85 C ATOM 80 CD PRO A 113 -24.062-174.520 311.183 1.00 84.58 C ANISOU 80 CD PRO A 113 8980 7145 16012 3587 -1338 -490 C ATOM 81 N SER A 114 -22.691-171.120 310.198 1.00 77.79 N ANISOU 81 N SER A 114 7733 7369 14456 3306 -1194 -1038 N ATOM 82 CA SER A 114 -22.116-169.964 309.516 1.00 77.76 C ANISOU 82 CA SER A 114 7595 7744 14205 3162 -1074 -1301 C ATOM 83 C SER A 114 -23.204-169.114 308.874 1.00 79.61 C ANISOU 83 C SER A 114 8039 8048 14161 2849 -938 -1401 C ATOM 84 O SER A 114 -23.105-167.882 308.837 1.00 78.16 O ANISOU 84 O SER A 114 7833 8179 13684 2659 -891 -1437 O ATOM 85 CB SER A 114 -21.096-170.423 308.475 1.00 80.37 C ANISOU 85 CB SER A 114 7698 8081 14756 3337 -962 -1651 C ATOM 86 OG SER A 114 -20.017-171.117 309.082 1.00 85.08 O ANISOU 86 OG SER A 114 8071 8651 15607 3645 -1095 -1561 O ATOM 87 N GLN A 115 -24.259-169.756 308.371 1.00 81.42 N ANISOU 87 N GLN A 115 8467 7978 14489 2793 -875 -1446 N ATOM 88 CA GLN A 115 -25.347-169.006 307.750 1.00 78.07 C ANISOU 88 CA GLN A 115 8233 7626 13805 2516 -758 -1531 C ATOM 89 C GLN A 115 -26.216-168.320 308.795 1.00 72.15 C ANISOU 89 C GLN A 115 7650 6952 12812 2350 -855 -1219 C ATOM 90 O GLN A 115 -26.711-167.211 308.563 1.00 68.95 O ANISOU 90 O GLN A 115 7326 6754 12118 2132 -786 -1253 O ATOM 91 CB GLN A 115 -26.184-169.931 306.867 1.00 81.84 C ANISOU 91 CB GLN A 115 8842 7791 14461 2504 -667 -1708 C ATOM 92 CG GLN A 115 -25.455-170.424 305.632 1.00 87.10 C ANISOU 92 CG GLN A 115 9352 8443 15300 2621 -534 -2096 C ATOM 93 CD GLN A 115 -26.246-171.460 304.859 1.00 90.98 C ANISOU 93 CD GLN A 115 9959 8605 16004 2624 -462 -2292 C ATOM 94 OE1 GLN A 115 -27.257-171.972 305.340 1.00 92.32 O ANISOU 94 OE1 GLN A 115 10314 8507 16258 2565 -527 -2109 O ATOM 95 NE2 GLN A 115 -25.789-171.774 303.653 1.00 93.40 N ANISOU 95 NE2 GLN A 115 10146 8944 16396 2680 -321 -2680 N ATOM 96 N GLN A 116 -26.420-168.963 309.949 1.00 73.61 N ANISOU 96 N GLN A 116 7884 6973 13111 2454 -1010 -910 N ATOM 97 CA GLN A 116 -27.179-168.325 311.022 1.00 71.90 C ANISOU 97 CA GLN A 116 7800 6871 12647 2308 -1101 -620 C ATOM 98 C GLN A 116 -26.517-167.029 311.467 1.00 69.44 C ANISOU 98 C GLN A 116 7370 6950 12062 2227 -1129 -616 C ATOM 99 O GLN A 116 -27.201-166.039 311.753 1.00 68.98 O ANISOU 99 O GLN A 116 7423 7054 11731 2025 -1113 -559 O ATOM 100 CB GLN A 116 -27.318-169.269 312.217 1.00 74.35 C ANISOU 100 CB GLN A 116 8147 6987 13117 2453 -1264 -270 C ATOM 101 CG GLN A 116 -28.070-170.555 311.949 1.00 77.96 C ANISOU 101 CG GLN A 116 8741 7014 13868 2505 -1245 -225 C ATOM 102 CD GLN A 116 -28.263-171.373 313.212 1.00 82.31 C ANISOU 102 CD GLN A 116 9341 7388 14543 2619 -1402 183 C ATOM 103 OE1 GLN A 116 -28.060-170.876 314.323 1.00 85.65 O ANISOU 103 OE1 GLN A 116 9727 8057 14761 2622 -1524 442 O ATOM 104 NE2 GLN A 116 -28.653-172.634 313.051 1.00 83.82 N ANISOU 104 NE2 GLN A 116 9617 7159 15073 2709 -1398 244 N ATOM 105 N LEU A 117 -25.185-167.022 311.537 1.00 69.74 N ANISOU 105 N LEU A 117 7173 7140 12185 2382 -1170 -691 N ATOM 106 CA LEU A 117 -24.464-165.830 311.968 1.00 71.37 C ANISOU 106 CA LEU A 117 7241 7716 12162 2296 -1198 -711 C ATOM 107 C LEU A 117 -24.699-164.670 311.009 1.00 73.69 C ANISOU 107 C LEU A 117 7581 8166 12251 2062 -1027 -944 C ATOM 108 O LEU A 117 -25.054-163.564 311.431 1.00 71.14 O ANISOU 108 O LEU A 117 7323 8027 11680 1876 -1029 -890 O ATOM 109 CB LEU A 117 -22.973-166.138 312.082 1.00 66.01 C ANISOU 109 CB LEU A 117 6273 7168 11641 2511 -1263 -780 C ATOM 110 CG LEU A 117 -22.062-164.931 312.308 1.00 66.28 C ANISOU 110 CG LEU A 117 6117 7590 11476 2409 -1266 -877 C ATOM 111 CD1 LEU A 117 -22.289-164.338 313.688 1.00 65.03 C ANISOU 111 CD1 LEU A 117 5990 7622 11098 2333 -1423 -633 C ATOM 112 CD2 LEU A 117 -20.610-165.317 312.116 1.00 71.06 C ANISOU 112 CD2 LEU A 117 6413 8318 12267 2618 -1292 -1011 C ATOM 113 N ALA A 118 -24.499-164.907 309.709 1.00 74.96 N ANISOU 113 N ALA A 118 7706 8260 12516 2072 -875 -1204 N ATOM 114 CA ALA A 118 -24.738-163.862 308.719 1.00 70.24 C ANISOU 114 CA ALA A 118 7156 7811 11720 1858 -707 -1395 C ATOM 115 C ALA A 118 -26.174-163.360 308.784 1.00 68.47 C ANISOU 115 C ALA A 118 7192 7517 11308 1667 -684 -1285 C ATOM 116 O ALA A 118 -26.424-162.154 308.676 1.00 64.50 O ANISOU 116 O ALA A 118 6742 7184 10581 1478 -623 -1300 O ATOM 117 CB ALA A 118 -24.413-164.382 307.319 1.00 60.03 C ANISOU 117 CB ALA A 118 5791 6460 10556 1914 -552 -1678 C ATOM 118 N ILE A 119 -27.131-164.273 308.965 1.00 70.27 N ANISOU 118 N ILE A 119 7575 7487 11638 1713 -731 -1175 N ATOM 119 CA ILE A 119 -28.522-163.869 309.145 1.00 66.33 C ANISOU 119 CA ILE A 119 7299 6935 10968 1545 -724 -1058 C ATOM 120 C ILE A 119 -28.658-162.974 310.369 1.00 63.39 C ANISOU 120 C ILE A 119 6952 6734 10399 1460 -825 -856 C ATOM 121 O ILE A 119 -29.364-161.959 310.340 1.00 62.36 O ANISOU 121 O ILE A 119 6932 6705 10055 1286 -777 -848 O ATOM 122 CB ILE A 119 -29.429-165.110 309.242 1.00 67.60 C ANISOU 122 CB ILE A 119 7591 6789 11306 1609 -764 -966 C ATOM 123 CG1 ILE A 119 -29.506-165.817 307.889 1.00 67.95 C ANISOU 123 CG1 ILE A 119 7633 6681 11504 1642 -641 -1230 C ATOM 124 CG2 ILE A 119 -30.819-164.729 309.729 1.00 66.74 C ANISOU 124 CG2 ILE A 119 7681 6658 11020 1448 -785 -799 C ATOM 125 CD1 ILE A 119 -30.363-167.059 307.902 1.00 70.56 C ANISOU 125 CD1 ILE A 119 8082 6683 12046 1686 -669 -1181 C ATOM 126 N ALA A 120 -27.969-163.323 311.456 1.00 64.17 N ANISOU 126 N ALA A 120 6938 6880 10563 1591 -968 -698 N ATOM 127 CA ALA A 120 -28.035-162.504 312.661 1.00 65.50 C ANISOU 127 CA ALA A 120 7108 7251 10529 1514 -1070 -534 C ATOM 128 C ALA A 120 -27.385-161.145 312.445 1.00 69.40 C ANISOU 128 C ALA A 120 7503 8002 10862 1381 -1006 -693 C ATOM 129 O ALA A 120 -27.903-160.123 312.911 1.00 72.67 O ANISOU 129 O ALA A 120 7999 8539 11074 1226 -1006 -658 O ATOM 130 CB ALA A 120 -27.374-163.233 313.828 1.00 66.60 C ANISOU 130 CB ALA A 120 7126 7420 10758 1695 -1246 -329 C ATOM 131 N VAL A 121 -26.256-161.110 311.735 1.00 69.27 N ANISOU 131 N VAL A 121 7306 8065 10947 1436 -943 -876 N ATOM 132 CA VAL A 121 -25.525-159.858 311.563 1.00 65.76 C ANISOU 132 CA VAL A 121 6746 7860 10379 1298 -879 -1015 C ATOM 133 C VAL A 121 -26.335-158.872 310.730 1.00 60.47 C ANISOU 133 C VAL A 121 6239 7175 9562 1091 -727 -1102 C ATOM 134 O VAL A 121 -26.537-157.720 311.130 1.00 61.16 O ANISOU 134 O VAL A 121 6370 7378 9491 933 -719 -1090 O ATOM 135 CB VAL A 121 -24.142-160.121 310.942 1.00 69.61 C ANISOU 135 CB VAL A 121 6986 8447 11016 1401 -832 -1190 C ATOM 136 CG1 VAL A 121 -23.448-158.806 310.634 1.00 68.24 C ANISOU 136 CG1 VAL A 121 6699 8504 10725 1219 -737 -1337 C ATOM 137 CG2 VAL A 121 -23.292-160.957 311.884 1.00 73.80 C ANISOU 137 CG2 VAL A 121 7334 9025 11682 1619 -1005 -1084 C ATOM 138 N LEU A 122 -26.815-159.307 309.561 1.00 56.93 N ANISOU 138 N LEU A 122 5879 6586 9166 1094 -607 -1194 N ATOM 139 CA LEU A 122 -27.573-158.402 308.702 1.00 57.65 C ANISOU 139 CA LEU A 122 6114 6683 9108 918 -469 -1255 C ATOM 140 C LEU A 122 -28.860-157.943 309.374 1.00 62.16 C ANISOU 140 C LEU A 122 6885 7195 9539 826 -522 -1103 C ATOM 141 O LEU A 122 -29.221-156.762 309.298 1.00 66.89 O ANISOU 141 O LEU A 122 7558 7863 9993 674 -464 -1107 O ATOM 142 CB LEU A 122 -27.890-159.074 307.367 1.00 57.67 C ANISOU 142 CB LEU A 122 6160 6579 9171 952 -351 -1385 C ATOM 143 CG LEU A 122 -26.737-159.295 306.390 1.00 60.79 C ANISOU 143 CG LEU A 122 6367 7075 9657 1005 -242 -1587 C ATOM 144 CD1 LEU A 122 -27.291-159.522 304.994 1.00 59.39 C ANISOU 144 CD1 LEU A 122 6269 6861 9435 966 -98 -1726 C ATOM 145 CD2 LEU A 122 -25.774-158.118 306.408 1.00 62.88 C ANISOU 145 CD2 LEU A 122 6493 7560 9837 885 -183 -1633 C ATOM 146 N SER A 123 -29.563-158.862 310.038 1.00 62.78 N ANISOU 146 N SER A 123 7047 7138 9669 916 -626 -965 N ATOM 147 CA SER A 123 -30.853-158.524 310.631 1.00 64.27 C ANISOU 147 CA SER A 123 7412 7285 9722 832 -664 -829 C ATOM 148 C SER A 123 -30.698-157.502 311.751 1.00 66.37 C ANISOU 148 C SER A 123 7653 7716 9849 754 -734 -764 C ATOM 149 O SER A 123 -31.432-156.509 311.802 1.00 65.05 O ANISOU 149 O SER A 123 7594 7582 9540 628 -690 -764 O ATOM 150 CB SER A 123 -31.538-159.788 311.150 1.00 64.37 C ANISOU 150 CB SER A 123 7496 7129 9833 933 -754 -683 C ATOM 151 OG SER A 123 -31.671-160.744 310.117 1.00 64.52 O ANISOU 151 OG SER A 123 7532 6978 10005 996 -688 -782 O ATOM 152 N LEU A 124 -29.745-157.728 312.658 1.00 67.36 N ANISOU 152 N LEU A 124 7627 7952 10015 835 -846 -721 N ATOM 153 CA LEU A 124 -29.604-156.839 313.805 1.00 65.84 C ANISOU 153 CA LEU A 124 7396 7942 9677 762 -927 -682 C ATOM 154 C LEU A 124 -29.041-155.485 313.397 1.00 66.11 C ANISOU 154 C LEU A 124 7373 8091 9654 614 -833 -850 C ATOM 155 O LEU A 124 -29.492-154.446 313.894 1.00 66.46 O ANISOU 155 O LEU A 124 7483 8199 9569 490 -828 -866 O ATOM 156 CB LEU A 124 -28.730-157.497 314.872 1.00 68.59 C ANISOU 156 CB LEU A 124 7581 8413 10066 896 -1087 -583 C ATOM 157 CG LEU A 124 -29.508-158.536 315.678 1.00 71.05 C ANISOU 157 CG LEU A 124 7983 8637 10377 997 -1196 -351 C ATOM 158 CD1 LEU A 124 -28.673-159.130 316.793 1.00 74.24 C ANISOU 158 CD1 LEU A 124 8228 9186 10794 1137 -1365 -210 C ATOM 159 CD2 LEU A 124 -30.771-157.900 316.237 1.00 70.01 C ANISOU 159 CD2 LEU A 124 8015 8534 10052 870 -1187 -283 C ATOM 160 N THR A 125 -28.060-155.473 312.495 1.00 67.30 N ANISOU 160 N THR A 125 7398 8263 9910 619 -750 -980 N ATOM 161 CA THR A 125 -27.511-154.210 312.016 1.00 67.27 C ANISOU 161 CA THR A 125 7340 8349 9870 458 -640 -1121 C ATOM 162 C THR A 125 -28.588-153.375 311.332 1.00 67.84 C ANISOU 162 C THR A 125 7614 8308 9855 328 -519 -1119 C ATOM 163 O THR A 125 -28.848-152.229 311.720 1.00 65.82 O ANISOU 163 O THR A 125 7412 8080 9517 197 -500 -1141 O ATOM 164 CB THR A 125 -26.338-154.479 311.071 1.00 67.00 C ANISOU 164 CB THR A 125 7131 8367 9958 489 -554 -1248 C ATOM 165 OG1 THR A 125 -25.217-154.959 311.825 1.00 66.48 O ANISOU 165 OG1 THR A 125 6843 8449 9968 596 -674 -1264 O ATOM 166 CG2 THR A 125 -25.940-153.213 310.337 1.00 69.53 C ANISOU 166 CG2 THR A 125 7428 8745 10244 298 -403 -1363 C ATOM 167 N LEU A 126 -29.247-153.948 310.322 1.00 68.78 N ANISOU 167 N LEU A 126 7841 8299 9993 372 -441 -1100 N ATOM 168 CA LEU A 126 -30.253-153.196 309.578 1.00 67.15 C ANISOU 168 CA LEU A 126 7809 8011 9695 269 -333 -1087 C ATOM 169 C LEU A 126 -31.464-152.873 310.441 1.00 69.12 C ANISOU 169 C LEU A 126 8208 8212 9845 249 -404 -986 C ATOM 170 O LEU A 126 -31.978-151.748 310.399 1.00 69.67 O ANISOU 170 O LEU A 126 8369 8262 9839 143 -349 -989 O ATOM 171 CB LEU A 126 -30.673-153.975 308.334 1.00 61.30 C ANISOU 171 CB LEU A 126 7125 7189 8978 326 -251 -1107 C ATOM 172 CG LEU A 126 -29.579-154.060 307.273 1.00 59.99 C ANISOU 172 CG LEU A 126 6821 7100 8874 320 -138 -1233 C ATOM 173 CD1 LEU A 126 -30.057-154.836 306.061 1.00 59.58 C ANISOU 173 CD1 LEU A 126 6822 6995 8819 373 -59 -1284 C ATOM 174 CD2 LEU A 126 -29.129-152.660 306.881 1.00 59.47 C ANISOU 174 CD2 LEU A 126 6736 7112 8747 154 -25 -1263 C ATOM 175 N GLY A 127 -31.937-153.843 311.227 1.00 69.50 N ANISOU 175 N GLY A 127 8277 8234 9896 351 -520 -890 N ATOM 176 CA GLY A 127 -33.110-153.608 312.051 1.00 68.47 C ANISOU 176 CA GLY A 127 8270 8087 9657 330 -577 -796 C ATOM 177 C GLY A 127 -32.926-152.458 313.025 1.00 68.89 C ANISOU 177 C GLY A 127 8297 8252 9626 243 -611 -836 C ATOM 178 O GLY A 127 -33.814-151.620 313.183 1.00 68.19 O ANISOU 178 O GLY A 127 8318 8138 9452 176 -579 -836 O ATOM 179 N THR A 128 -31.765-152.396 313.677 1.00 70.19 N ANISOU 179 N THR A 128 8302 8548 9820 246 -678 -888 N ATOM 180 CA THR A 128 -31.538-151.335 314.653 1.00 73.01 C ANISOU 180 CA THR A 128 8613 9029 10098 152 -718 -964 C ATOM 181 C THR A 128 -31.427-149.976 313.974 1.00 74.77 C ANISOU 181 C THR A 128 8875 9188 10348 7 -588 -1085 C ATOM 182 O THR A 128 -32.012-148.993 314.444 1.00 77.14 O ANISOU 182 O THR A 128 9251 9474 10587 -73 -574 -1132 O ATOM 183 CB THR A 128 -30.284-151.627 315.470 1.00 74.25 C ANISOU 183 CB THR A 128 8566 9371 10273 187 -831 -1001 C ATOM 184 OG1 THR A 128 -30.349-152.961 315.986 1.00 76.54 O ANISOU 184 OG1 THR A 128 8826 9690 10565 341 -947 -848 O ATOM 185 CG2 THR A 128 -30.181-150.647 316.628 1.00 73.14 C ANISOU 185 CG2 THR A 128 8376 9393 10022 90 -894 -1096 C ATOM 186 N PHE A 129 -30.679-149.899 312.871 1.00 73.25 N ANISOU 186 N PHE A 129 8628 8953 10253 -27 -487 -1135 N ATOM 187 CA PHE A 129 -30.627-148.655 312.109 1.00 71.61 C ANISOU 187 CA PHE A 129 8473 8660 10077 -169 -348 -1201 C ATOM 188 C PHE A 129 -32.018-148.250 311.644 1.00 68.43 C ANISOU 188 C PHE A 129 8275 8111 9614 -169 -287 -1121 C ATOM 189 O PHE A 129 -32.374-147.067 311.679 1.00 69.84 O ANISOU 189 O PHE A 129 8531 8211 9795 -264 -228 -1154 O ATOM 190 CB PHE A 129 -29.681-148.801 310.916 1.00 75.62 C ANISOU 190 CB PHE A 129 8887 9174 10670 -198 -238 -1236 C ATOM 191 CG PHE A 129 -28.245-149.035 311.299 1.00 82.88 C ANISOU 191 CG PHE A 129 9577 10252 11662 -208 -283 -1335 C ATOM 192 CD1 PHE A 129 -27.788-148.716 312.566 1.00 84.75 C ANISOU 192 CD1 PHE A 129 9706 10614 11883 -241 -398 -1406 C ATOM 193 CD2 PHE A 129 -27.352-149.572 310.387 1.00 86.04 C ANISOU 193 CD2 PHE A 129 9851 10704 12136 -181 -212 -1372 C ATOM 194 CE1 PHE A 129 -26.468-148.931 312.919 1.00 87.00 C ANISOU 194 CE1 PHE A 129 9756 11073 12226 -244 -453 -1499 C ATOM 195 CE2 PHE A 129 -26.030-149.786 310.733 1.00 87.90 C ANISOU 195 CE2 PHE A 129 9851 11102 12444 -178 -255 -1469 C ATOM 196 CZ PHE A 129 -25.588-149.467 312.000 1.00 88.62 C ANISOU 196 CZ PHE A 129 9832 11319 12521 -208 -382 -1526 C ATOM 197 N THR A 130 -32.828-149.225 311.227 1.00 65.90 N ANISOU 197 N THR A 130 8037 7749 9255 -59 -303 -1022 N ATOM 198 CA THR A 130 -34.183-148.919 310.782 1.00 63.79 C ANISOU 198 CA THR A 130 7939 7376 8921 -49 -258 -948 C ATOM 199 C THR A 130 -35.052-148.443 311.937 1.00 63.18 C ANISOU 199 C THR A 130 7927 7308 8773 -48 -328 -944 C ATOM 200 O THR A 130 -35.828-147.492 311.786 1.00 63.50 O ANISOU 200 O THR A 130 8072 7265 8791 -84 -274 -942 O ATOM 201 CB THR A 130 -34.808-150.144 310.119 1.00 61.06 C ANISOU 201 CB THR A 130 7640 7004 8556 52 -267 -873 C ATOM 202 OG1 THR A 130 -33.877-150.712 309.190 1.00 62.84 O ANISOU 202 OG1 THR A 130 7776 7252 8849 66 -211 -915 O ATOM 203 CG2 THR A 130 -36.067-149.746 309.381 1.00 59.79 C ANISOU 203 CG2 THR A 130 7625 6767 8324 51 -205 -811 C ATOM 204 N VAL A 131 -34.941-149.092 313.098 1.00 62.46 N ANISOU 204 N VAL A 131 7767 7327 8639 0 -448 -937 N ATOM 205 CA VAL A 131 -35.726-148.676 314.257 1.00 63.55 C ANISOU 205 CA VAL A 131 7945 7522 8678 -3 -510 -948 C ATOM 206 C VAL A 131 -35.360-147.255 314.662 1.00 67.81 C ANISOU 206 C VAL A 131 8466 8058 9242 -110 -473 -1093 C ATOM 207 O VAL A 131 -36.235-146.414 314.897 1.00 70.00 O ANISOU 207 O VAL A 131 8834 8277 9487 -129 -441 -1130 O ATOM 208 CB VAL A 131 -35.532-149.664 315.421 1.00 65.19 C ANISOU 208 CB VAL A 131 8067 7886 8817 62 -644 -891 C ATOM 209 CG1 VAL A 131 -36.078-149.075 316.713 1.00 64.66 C ANISOU 209 CG1 VAL A 131 8003 7944 8621 35 -701 -941 C ATOM 210 CG2 VAL A 131 -36.221-150.975 315.107 1.00 66.16 C ANISOU 210 CG2 VAL A 131 8244 7959 8936 156 -669 -740 C ATOM 211 N LEU A 132 -34.059-146.959 314.727 1.00 68.17 N ANISOU 211 N LEU A 132 8384 8157 9360 -183 -473 -1191 N ATOM 212 CA LEU A 132 -33.627-145.634 315.161 1.00 65.87 C ANISOU 212 CA LEU A 132 8060 7852 9116 -310 -440 -1355 C ATOM 213 C LEU A 132 -33.948-144.563 314.126 1.00 65.92 C ANISOU 213 C LEU A 132 8183 7640 9224 -383 -296 -1356 C ATOM 214 O LEU A 132 -34.237-143.419 314.494 1.00 64.73 O ANISOU 214 O LEU A 132 8079 7399 9116 -454 -259 -1460 O ATOM 215 CB LEU A 132 -32.131-145.648 315.470 1.00 63.86 C ANISOU 215 CB LEU A 132 7615 7730 8917 -383 -479 -1463 C ATOM 216 CG LEU A 132 -31.702-146.554 316.627 1.00 61.21 C ANISOU 216 CG LEU A 132 7143 7636 8476 -307 -638 -1458 C ATOM 217 CD1 LEU A 132 -30.222-146.392 316.916 1.00 59.96 C ANISOU 217 CD1 LEU A 132 6777 7628 8377 -384 -679 -1587 C ATOM 218 CD2 LEU A 132 -32.526-146.268 317.875 1.00 60.49 C ANISOU 218 CD2 LEU A 132 7089 7653 8240 -296 -716 -1504 C ATOM 219 N GLU A 133 -33.903-144.908 312.837 1.00 69.38 N ANISOU 219 N GLU A 133 8665 7992 9703 -362 -213 -1241 N ATOM 220 CA GLU A 133 -34.249-143.947 311.794 1.00 71.97 C ANISOU 220 CA GLU A 133 9108 8134 10103 -418 -81 -1191 C ATOM 221 C GLU A 133 -35.707-143.518 311.904 1.00 73.33 C ANISOU 221 C GLU A 133 9432 8204 10226 -345 -79 -1137 C ATOM 222 O GLU A 133 -36.009-142.339 312.121 1.00 76.43 O ANISOU 222 O GLU A 133 9886 8463 10691 -396 -32 -1198 O ATOM 223 CB GLU A 133 -33.971-144.544 310.414 1.00 72.08 C ANISOU 223 CB GLU A 133 9126 8141 10118 -397 -2 -1075 C ATOM 224 CG GLU A 133 -32.541-144.397 309.936 1.00 77.71 C ANISOU 224 CG GLU A 133 9706 8899 10920 -508 67 -1131 C ATOM 225 CD GLU A 133 -32.325-145.042 308.585 1.00 82.94 C ANISOU 225 CD GLU A 133 10364 9594 11557 -477 150 -1038 C ATOM 226 OE1 GLU A 133 -32.572-146.260 308.464 1.00 85.33 O ANISOU 226 OE1 GLU A 133 10650 9977 11795 -356 89 -1010 O ATOM 227 OE2 GLU A 133 -31.928-144.330 307.641 1.00 85.33 O ANISOU 227 OE2 GLU A 133 10679 9840 11902 -578 281 -995 O ATOM 228 N ASN A 134 -36.629-144.472 311.747 1.00 70.78 N ANISOU 228 N ASN A 134 9162 7936 9797 -224 -126 -1032 N ATOM 229 CA ASN A 134 -38.049-144.139 311.756 1.00 67.83 C ANISOU 229 CA ASN A 134 8909 7494 9370 -147 -123 -977 C ATOM 230 C ASN A 134 -38.485-143.560 313.093 1.00 68.64 C ANISOU 230 C ASN A 134 9004 7625 9451 -147 -177 -1102 C ATOM 231 O ASN A 134 -39.381-142.710 313.135 1.00 67.97 O ANISOU 231 O ASN A 134 9003 7435 9387 -115 -141 -1117 O ATOM 232 CB ASN A 134 -38.880-145.373 311.413 1.00 63.01 C ANISOU 232 CB ASN A 134 8325 6962 8653 -42 -169 -864 C ATOM 233 CG ASN A 134 -38.720-145.790 309.967 1.00 63.41 C ANISOU 233 CG ASN A 134 8400 6984 8709 -33 -101 -768 C ATOM 234 OD1 ASN A 134 -39.335-145.208 309.073 1.00 64.82 O ANISOU 234 OD1 ASN A 134 8666 7084 8880 -16 -33 -690 O ATOM 235 ND2 ASN A 134 -37.884-146.796 309.727 1.00 64.39 N ANISOU 235 ND2 ASN A 134 8440 7185 8841 -35 -120 -775 N ATOM 236 N LEU A 135 -37.872-144.005 314.191 1.00 69.46 N ANISOU 236 N LEU A 135 8998 7888 9505 -172 -265 -1196 N ATOM 237 CA LEU A 135 -38.141-143.380 315.480 1.00 69.79 C ANISOU 237 CA LEU A 135 9012 7999 9505 -191 -311 -1350 C ATOM 238 C LEU A 135 -37.831-141.888 315.436 1.00 69.08 C ANISOU 238 C LEU A 135 8948 7737 9564 -287 -231 -1496 C ATOM 239 O LEU A 135 -38.629-141.067 315.902 1.00 73.39 O ANISOU 239 O LEU A 135 9550 8212 10124 -263 -210 -1591 O ATOM 240 CB LEU A 135 -37.330-144.073 316.573 1.00 73.37 C ANISOU 240 CB LEU A 135 9325 8683 9868 -214 -423 -1415 C ATOM 241 CG LEU A 135 -37.457-143.556 318.002 1.00 80.55 C ANISOU 241 CG LEU A 135 10173 9746 10687 -243 -485 -1593 C ATOM 242 CD1 LEU A 135 -38.880-143.733 318.503 1.00 80.52 C ANISOU 242 CD1 LEU A 135 10239 9803 10552 -150 -499 -1551 C ATOM 243 CD2 LEU A 135 -36.469-144.276 318.903 1.00 85.47 C ANISOU 243 CD2 LEU A 135 10642 10620 11214 -264 -602 -1622 C ATOM 244 N LEU A 136 -36.686-141.518 314.854 1.00 66.08 N ANISOU 244 N LEU A 136 8523 7276 9310 -397 -175 -1520 N ATOM 245 CA LEU A 136 -36.325-140.107 314.756 1.00 65.44 C ANISOU 245 CA LEU A 136 8467 6993 9404 -514 -86 -1645 C ATOM 246 C LEU A 136 -37.281-139.352 313.843 1.00 64.82 C ANISOU 246 C LEU A 136 8548 6665 9415 -458 13 -1525 C ATOM 247 O LEU A 136 -37.653-138.209 314.137 1.00 66.09 O ANISOU 247 O LEU A 136 8767 6648 9697 -480 60 -1633 O ATOM 248 CB LEU A 136 -34.888-139.960 314.257 1.00 63.84 C ANISOU 248 CB LEU A 136 8168 6775 9315 -661 -37 -1671 C ATOM 249 CG LEU A 136 -34.402-138.518 314.059 1.00 63.92 C ANISOU 249 CG LEU A 136 8200 6549 9539 -818 71 -1782 C ATOM 250 CD1 LEU A 136 -34.368-137.759 315.379 1.00 62.58 C ANISOU 250 CD1 LEU A 136 7974 6397 9407 -885 23 -2060 C ATOM 251 CD2 LEU A 136 -33.037-138.489 313.381 1.00 62.87 C ANISOU 251 CD2 LEU A 136 7963 6420 9504 -969 138 -1766 C ATOM 252 N VAL A 137 -37.681-139.969 312.727 1.00 63.00 N ANISOU 252 N VAL A 137 8384 6422 9130 -379 43 -1307 N ATOM 253 CA VAL A 137 -38.660-139.347 311.836 1.00 63.35 C ANISOU 253 CA VAL A 137 8568 6279 9223 -301 117 -1163 C ATOM 254 C VAL A 137 -39.915-138.984 312.615 1.00 65.68 C ANISOU 254 C VAL A 137 8915 6555 9487 -187 77 -1237 C ATOM 255 O VAL A 137 -40.390-137.845 312.566 1.00 70.79 O ANISOU 255 O VAL A 137 9640 6990 10269 -166 135 -1267 O ATOM 256 CB VAL A 137 -38.978-140.277 310.653 1.00 59.42 C ANISOU 256 CB VAL A 137 8105 5857 8614 -225 128 -949 C ATOM 257 CG1 VAL A 137 -40.046-139.660 309.768 1.00 56.29 C ANISOU 257 CG1 VAL A 137 7837 5315 8235 -129 184 -790 C ATOM 258 CG2 VAL A 137 -37.715-140.567 309.854 1.00 59.39 C ANISOU 258 CG2 VAL A 137 8038 5884 8642 -335 185 -900 C ATOM 259 N LEU A 138 -40.449-139.943 313.377 1.00 60.50 N ANISOU 259 N LEU A 138 8208 6118 8663 -111 -19 -1269 N ATOM 260 CA LEU A 138 -41.627-139.672 314.195 1.00 57.37 C ANISOU 260 CA LEU A 138 7832 5755 8210 -10 -51 -1355 C ATOM 261 C LEU A 138 -41.363-138.576 315.217 1.00 59.11 C ANISOU 261 C LEU A 138 8023 5900 8535 -73 -38 -1605 C ATOM 262 O LEU A 138 -42.274-137.810 315.551 1.00 63.42 O ANISOU 262 O LEU A 138 8614 6351 9130 8 -13 -1691 O ATOM 263 CB LEU A 138 -42.085-140.949 314.897 1.00 56.99 C ANISOU 263 CB LEU A 138 7718 5978 7957 46 -148 -1334 C ATOM 264 CG LEU A 138 -42.584-142.054 313.968 1.00 57.13 C ANISOU 264 CG LEU A 138 7766 6058 7884 115 -163 -1123 C ATOM 265 CD1 LEU A 138 -42.774-143.351 314.734 1.00 57.71 C ANISOU 265 CD1 LEU A 138 7767 6363 7797 133 -254 -1101 C ATOM 266 CD2 LEU A 138 -43.877-141.630 313.288 1.00 55.48 C ANISOU 266 CD2 LEU A 138 7642 5756 7681 229 -123 -1030 C ATOM 267 N CYS A 139 -40.131-138.483 315.722 1.00 59.72 N ANISOU 267 N CYS A 139 8012 6028 8653 -214 -55 -1744 N ATOM 268 CA CYS A 139 -39.814-137.425 316.673 1.00 67.28 C ANISOU 268 CA CYS A 139 8928 6920 9715 -297 -42 -2021 C ATOM 269 C CYS A 139 -39.868-136.055 316.011 1.00 68.90 C ANISOU 269 C CYS A 139 9235 6759 10183 -329 73 -2038 C ATOM 270 O CYS A 139 -40.390-135.099 316.595 1.00 68.72 O ANISOU 270 O CYS A 139 9240 6605 10267 -301 101 -2225 O ATOM 271 CB CYS A 139 -38.440-137.661 317.295 1.00 74.45 C ANISOU 271 CB CYS A 139 9697 7989 10602 -450 -95 -2165 C ATOM 272 SG CYS A 139 -37.937-136.371 318.450 1.00 87.06 S ANISOU 272 SG CYS A 139 11219 9533 12326 -586 -84 -2552 S ATOM 273 N VAL A 140 -39.344-135.938 314.791 1.00 67.67 N ANISOU 273 N VAL A 140 9137 6436 10139 -383 146 -1841 N ATOM 274 CA VAL A 140 -39.335-134.632 314.143 1.00 66.47 C ANISOU 274 CA VAL A 140 9088 5922 10247 -425 261 -1813 C ATOM 275 C VAL A 140 -40.706-134.298 313.558 1.00 64.80 C ANISOU 275 C VAL A 140 9004 5559 10057 -232 290 -1647 C ATOM 276 O VAL A 140 -41.052-133.118 313.420 1.00 65.86 O ANISOU 276 O VAL A 140 9224 5389 10412 -207 362 -1676 O ATOM 277 CB VAL A 140 -38.225-134.565 313.080 1.00 65.27 C ANISOU 277 CB VAL A 140 8937 5668 10193 -572 340 -1653 C ATOM 278 CG1 VAL A 140 -38.048-133.136 312.600 1.00 70.36 C ANISOU 278 CG1 VAL A 140 9676 5925 11132 -658 464 -1639 C ATOM 279 CG2 VAL A 140 -36.915-135.076 313.653 1.00 64.57 C ANISOU 279 CG2 VAL A 140 8690 5789 10055 -734 294 -1809 C ATOM 280 N ILE A 141 -41.512-135.309 313.216 1.00 62.12 N ANISOU 280 N ILE A 141 8673 5421 9508 -92 232 -1478 N ATOM 281 CA ILE A 141 -42.898-135.044 312.830 1.00 62.25 C ANISOU 281 CA ILE A 141 8775 5357 9519 102 239 -1358 C ATOM 282 C ILE A 141 -43.626-134.324 313.957 1.00 64.30 C ANISOU 282 C ILE A 141 9019 5565 9847 180 227 -1610 C ATOM 283 O ILE A 141 -44.249-133.275 313.753 1.00 65.25 O ANISOU 283 O ILE A 141 9218 5421 10154 276 284 -1612 O ATOM 284 CB ILE A 141 -43.628-136.346 312.452 1.00 59.76 C ANISOU 284 CB ILE A 141 8438 5311 8955 212 168 -1191 C ATOM 285 CG1 ILE A 141 -42.947-137.051 311.281 1.00 57.56 C ANISOU 285 CG1 ILE A 141 8170 5087 8612 146 187 -974 C ATOM 286 CG2 ILE A 141 -45.076-136.046 312.092 1.00 60.67 C ANISOU 286 CG2 ILE A 141 8614 5375 9061 409 168 -1087 C ATOM 287 CD1 ILE A 141 -42.808-136.208 310.049 1.00 60.45 C ANISOU 287 CD1 ILE A 141 8636 5214 9118 141 282 -774 C ATOM 288 N LEU A 142 -43.553-134.881 315.168 1.00 64.61 N ANISOU 288 N LEU A 142 8952 5864 9734 147 155 -1825 N ATOM 289 CA LEU A 142 -44.303-134.331 316.290 1.00 68.77 C ANISOU 289 CA LEU A 142 9442 6419 10270 226 145 -2085 C ATOM 290 C LEU A 142 -43.762-132.976 316.726 1.00 72.33 C ANISOU 290 C LEU A 142 9907 6586 10987 137 212 -2338 C ATOM 291 O LEU A 142 -44.524-132.145 317.231 1.00 73.51 O ANISOU 291 O LEU A 142 10071 6608 11250 240 242 -2520 O ATOM 292 CB LEU A 142 -44.295-135.315 317.460 1.00 70.02 C ANISOU 292 CB LEU A 142 9474 6966 10162 198 53 -2225 C ATOM 293 CG LEU A 142 -45.447-136.324 317.526 1.00 71.50 C ANISOU 293 CG LEU A 142 9639 7411 10119 336 0 -2088 C ATOM 294 CD1 LEU A 142 -45.664-137.045 316.200 1.00 69.60 C ANISOU 294 CD1 LEU A 142 9463 7138 9843 385 -1 -1763 C ATOM 295 CD2 LEU A 142 -45.201-137.328 318.640 1.00 72.28 C ANISOU 295 CD2 LEU A 142 9620 7876 9968 273 -84 -2177 C ATOM 296 N HIS A 143 -42.463-132.729 316.545 1.00 75.26 N ANISOU 296 N HIS A 143 10265 6853 11476 -57 240 -2372 N ATOM 297 CA HIS A 143 -41.941-131.401 316.846 1.00 79.83 C ANISOU 297 CA HIS A 143 10864 7118 12348 -167 316 -2606 C ATOM 298 C HIS A 143 -42.377-130.392 315.791 1.00 82.62 C ANISOU 298 C HIS A 143 11368 7040 12984 -87 418 -2415 C ATOM 299 O HIS A 143 -42.684-129.240 316.116 1.00 84.55 O ANISOU 299 O HIS A 143 11657 6985 13482 -55 477 -2600 O ATOM 300 CB HIS A 143 -40.418-131.433 316.956 1.00 79.84 C ANISOU 300 CB HIS A 143 10787 7151 12398 -415 319 -2699 C ATOM 301 CG HIS A 143 -39.820-130.122 317.359 1.00 82.68 C ANISOU 301 CG HIS A 143 11145 7207 13062 -566 393 -2980 C ATOM 302 ND1 HIS A 143 -39.822-129.672 318.663 1.00 85.18 N ANISOU 302 ND1 HIS A 143 11369 7610 13386 -608 362 -3389 N ATOM 303 CD2 HIS A 143 -39.214-129.156 316.630 1.00 83.77 C ANISOU 303 CD2 HIS A 143 11361 6955 13515 -695 503 -2918 C ATOM 304 CE1 HIS A 143 -39.237-128.490 318.719 1.00 86.02 C ANISOU 304 CE1 HIS A 143 11495 7376 13815 -759 446 -3592 C ATOM 305 NE2 HIS A 143 -38.858-128.153 317.499 1.00 85.04 N ANISOU 305 NE2 HIS A 143 11476 6943 13892 -819 535 -3299 N ATOM 306 N SER A 144 -42.418-130.810 314.523 1.00 82.10 N ANISOU 306 N SER A 144 11378 6940 12876 -47 438 -2044 N ATOM 307 CA SER A 144 -42.848-129.909 313.459 1.00 85.62 C ANISOU 307 CA SER A 144 11965 7013 13553 41 525 -1805 C ATOM 308 C SER A 144 -44.303-129.500 313.633 1.00 91.28 C ANISOU 308 C SER A 144 12727 7650 14307 299 512 -1819 C ATOM 309 O SER A 144 -44.662-128.340 313.402 1.00 94.31 O ANISOU 309 O SER A 144 13201 7654 14978 377 583 -1810 O ATOM 310 CB SER A 144 -42.649-130.565 312.096 1.00 81.88 C ANISOU 310 CB SER A 144 11542 6613 12956 39 538 -1414 C ATOM 311 OG SER A 144 -43.238-129.780 311.074 1.00 84.04 O ANISOU 311 OG SER A 144 11947 6590 13395 160 605 -1143 O ATOM 312 N ARG A 145 -45.160-130.443 314.027 1.00 96.54 N ANISOU 312 N ARG A 145 13324 8662 14696 436 425 -1834 N ATOM 313 CA ARG A 145 -46.550-130.098 314.290 1.00101.77 C ANISOU 313 CA ARG A 145 13993 9299 15377 677 412 -1882 C ATOM 314 C ARG A 145 -46.694-129.156 315.479 1.00 99.31 C ANISOU 314 C ARG A 145 13642 8843 15247 689 442 -2280 C ATOM 315 O ARG A 145 -47.714-128.469 315.584 1.00 99.10 O ANISOU 315 O ARG A 145 13639 8658 15356 892 465 -2340 O ATOM 316 CB ARG A 145 -47.382-131.362 314.513 1.00106.70 C ANISOU 316 CB ARG A 145 14531 10349 15660 783 320 -1827 C ATOM 317 CG ARG A 145 -48.056-131.880 313.250 1.00112.19 C ANISOU 317 CG ARG A 145 15278 11100 16249 914 299 -1458 C ATOM 318 CD ARG A 145 -49.210-132.819 313.574 1.00118.28 C ANISOU 318 CD ARG A 145 15960 12219 16762 1053 224 -1457 C ATOM 319 NE ARG A 145 -50.250-132.770 312.550 1.00125.95 N ANISOU 319 NE ARG A 145 16970 13164 17722 1248 212 -1196 N ATOM 320 CZ ARG A 145 -51.321-133.557 312.531 1.00127.60 C ANISOU 320 CZ ARG A 145 17102 13656 17724 1370 151 -1140 C ATOM 321 NH1 ARG A 145 -52.215-133.436 311.561 1.00128.81 N ANISOU 321 NH1 ARG A 145 17277 13792 17872 1544 135 -910 N ATOM 322 NH2 ARG A 145 -51.497-134.467 313.478 1.00126.13 N ANISOU 322 NH2 ARG A 145 16810 13782 17332 1312 107 -1302 N ATOM 323 N SER A 146 -45.694-129.101 316.364 1.00 95.79 N ANISOU 323 N SER A 146 13126 8460 14809 483 441 -2569 N ATOM 324 CA SER A 146 -45.743-128.160 317.478 1.00 98.03 C ANISOU 324 CA SER A 146 13365 8612 15269 470 474 -2989 C ATOM 325 C SER A 146 -45.672-126.716 317.004 1.00 99.23 C ANISOU 325 C SER A 146 13636 8209 15857 488 579 -3004 C ATOM 326 O SER A 146 -46.268-125.831 317.626 1.00101.14 O ANISOU 326 O SER A 146 13874 8326 16227 595 605 -3225 O ATOM 327 CB SER A 146 -44.598-128.430 318.456 1.00 99.17 C ANISOU 327 CB SER A 146 13396 8973 15311 227 440 -3285 C ATOM 328 OG SER A 146 -44.775-129.652 319.146 1.00100.51 O ANISOU 328 OG SER A 146 13448 9645 15096 236 342 -3315 O ATOM 329 N LEU A 147 -44.945-126.455 315.919 1.00 96.66 N ANISOU 329 N LEU A 147 13413 7618 15696 377 634 -2713 N ATOM 330 CA LEU A 147 -44.645-125.092 315.516 1.00 98.07 C ANISOU 330 CA LEU A 147 13701 7357 16205 330 719 -2652 C ATOM 331 C LEU A 147 -45.193-124.715 314.149 1.00101.52 C ANISOU 331 C LEU A 147 14285 7499 16789 490 764 -2212 C ATOM 332 O LEU A 147 -45.142-123.532 313.792 1.00108.60 O ANISOU 332 O LEU A 147 15283 8045 17934 494 820 -2114 O ATOM 333 CB LEU A 147 -43.124-124.859 315.527 1.00 97.60 C ANISOU 333 CB LEU A 147 13620 7235 16228 9 756 -2712 C ATOM 334 CG LEU A 147 -42.340-125.436 316.712 1.00 95.54 C ANISOU 334 CG LEU A 147 13195 7327 15781 -180 696 -3084 C ATOM 335 CD1 LEU A 147 -40.876-125.028 316.635 1.00 97.14 C ANISOU 335 CD1 LEU A 147 13366 7435 16108 -481 738 -3129 C ATOM 336 CD2 LEU A 147 -42.939-125.020 318.050 1.00 96.78 C ANISOU 336 CD2 LEU A 147 13269 7625 15879 -94 658 -3473 C ATOM 337 N ARG A 148 -45.711-125.667 313.376 1.00 98.17 N ANISOU 337 N ARG A 148 13869 7257 16176 618 727 -1920 N ATOM 338 CA ARG A 148 -46.188-125.397 312.024 1.00 99.70 C ANISOU 338 CA ARG A 148 14186 7251 16446 764 757 -1468 C ATOM 339 C ARG A 148 -47.493-126.146 311.801 1.00 98.93 C ANISOU 339 C ARG A 148 14048 7465 16077 1032 666 -1322 C ATOM 340 O ARG A 148 -47.534-127.374 311.915 1.00 94.22 O ANISOU 340 O ARG A 148 13363 7307 15132 1000 588 -1311 O ATOM 341 CB ARG A 148 -45.143-125.805 310.981 1.00 98.91 C ANISOU 341 CB ARG A 148 14131 7189 16263 560 792 -1150 C ATOM 342 CG ARG A 148 -43.819-125.055 311.095 1.00100.36 C ANISOU 342 CG ARG A 148 14341 7070 16723 272 893 -1265 C ATOM 343 CD ARG A 148 -43.754-123.915 310.104 1.00105.81 C ANISOU 343 CD ARG A 148 15175 7375 17653 281 971 -935 C ATOM 344 NE ARG A 148 -44.035-124.386 308.752 1.00109.42 N ANISOU 344 NE ARG A 148 15707 7859 18010 379 995 -465 N ATOM 345 CZ ARG A 148 -43.101-124.672 307.851 1.00114.66 C ANISOU 345 CZ ARG A 148 16391 8582 18594 185 1054 -201 C ATOM 346 NH1 ARG A 148 -41.819-124.520 308.151 1.00117.12 N ANISOU 346 NH1 ARG A 148 16658 8825 19018 -118 1124 -367 N ATOM 347 NH2 ARG A 148 -43.449-125.103 306.646 1.00115.61 N ANISOU 347 NH2 ARG A 148 16559 8859 18507 289 1043 214 N ATOM 348 N CYS A 149 -48.549-125.402 311.471 1.00104.01 N ANISOU 348 N CYS A 149 14750 7873 16898 1295 676 -1206 N ATOM 349 CA CYS A 149 -49.881-125.966 311.295 1.00103.81 C ANISOU 349 CA CYS A 149 14665 8126 16654 1564 592 -1095 C ATOM 350 C CYS A 149 -50.075-126.626 309.934 1.00 99.39 C ANISOU 350 C CYS A 149 14144 7743 15875 1616 551 -639 C ATOM 351 O CYS A 149 -50.903-127.536 309.814 1.00 92.90 O ANISOU 351 O CYS A 149 13239 7294 14764 1741 466 -574 O ATOM 352 CB CYS A 149 -50.921-124.854 311.501 1.00111.80 C ANISOU 352 CB CYS A 149 15702 8817 17961 1844 616 -1171 C ATOM 353 SG CYS A 149 -52.616-125.184 310.947 1.00113.39 S ANISOU 353 SG CYS A 149 15841 9250 17993 2218 527 -940 S ATOM 354 N ARG A 150 -49.307-126.222 308.925 1.00105.34 N ANISOU 354 N ARG A 150 15013 8265 16746 1503 615 -336 N ATOM 355 CA ARG A 150 -49.642-126.482 307.527 1.00112.62 C ANISOU 355 CA ARG A 150 15990 9279 17521 1605 591 119 C ATOM 356 C ARG A 150 -49.201-127.843 306.981 1.00114.26 C ANISOU 356 C ARG A 150 16140 9928 17345 1461 542 243 C ATOM 357 O ARG A 150 -49.998-128.499 306.297 1.00116.89 O ANISOU 357 O ARG A 150 16437 10543 17434 1609 467 446 O ATOM 358 CB ARG A 150 -49.071-125.355 306.660 1.00120.01 C ANISOU 358 CB ARG A 150 17078 9763 18758 1559 693 418 C ATOM 359 CG ARG A 150 -49.724-124.003 306.915 1.00128.26 C ANISOU 359 CG ARG A 150 18195 10333 20203 1769 733 392 C ATOM 360 CD ARG A 150 -50.980-123.826 306.079 1.00133.33 C ANISOU 360 CD ARG A 150 18854 11008 20797 2104 667 728 C ATOM 361 NE ARG A 150 -50.657-123.646 304.667 1.00138.00 N ANISOU 361 NE ARG A 150 19549 11555 21330 2075 690 1227 N ATOM 362 CZ ARG A 150 -51.560-123.525 303.699 1.00142.19 C ANISOU 362 CZ ARG A 150 20096 12172 21756 2325 621 1596 C ATOM 363 NH1 ARG A 150 -52.854-123.568 303.984 1.00142.78 N ANISOU 363 NH1 ARG A 150 20085 12368 21796 2629 527 1522 N ATOM 364 NH2 ARG A 150 -51.167-123.363 302.444 1.00144.77 N ANISOU 364 NH2 ARG A 150 20510 12498 21996 2266 645 2037 N ATOM 365 N PRO A 151 -47.969-128.310 307.216 1.00114.90 N ANISOU 365 N PRO A 151 16202 10087 17368 1184 579 124 N ATOM 366 CA PRO A 151 -47.549-129.585 306.611 1.00110.51 C ANISOU 366 CA PRO A 151 15592 9920 16477 1071 539 249 C ATOM 367 C PRO A 151 -48.142-130.777 307.355 1.00102.55 C ANISOU 367 C PRO A 151 14456 9307 15200 1121 435 32 C ATOM 368 O PRO A 151 -47.995-130.903 308.572 1.00 99.54 O ANISOU 368 O PRO A 151 14008 8967 14846 1060 418 -293 O ATOM 369 CB PRO A 151 -46.018-129.556 306.729 1.00111.95 C ANISOU 369 CB PRO A 151 15780 10015 16740 775 619 165 C ATOM 370 CG PRO A 151 -45.671-128.140 307.109 1.00115.49 C ANISOU 370 CG PRO A 151 16311 9992 17580 727 712 81 C ATOM 371 CD PRO A 151 -46.837-127.660 307.900 1.00116.88 C ANISOU 371 CD PRO A 151 16474 10065 17870 958 664 -104 C ATOM 372 N SER A 152 -48.790-131.671 306.602 1.00101.31 N ANISOU 372 N SER A 152 14263 9455 14777 1217 367 218 N ATOM 373 CA SER A 152 -49.602-132.726 307.203 1.00 98.79 C ANISOU 373 CA SER A 152 13828 9478 14228 1291 271 60 C ATOM 374 C SER A 152 -48.779-133.951 307.593 1.00 90.69 C ANISOU 374 C SER A 152 12730 8713 13013 1092 246 -77 C ATOM 375 O SER A 152 -48.971-134.501 308.684 1.00 85.85 O ANISOU 375 O SER A 152 12034 8259 12327 1072 200 -317 O ATOM 376 CB SER A 152 -50.720-133.129 306.242 1.00102.41 C ANISOU 376 CB SER A 152 14263 10142 14504 1477 205 296 C ATOM 377 OG SER A 152 -51.624-132.056 306.040 1.00104.35 O ANISOU 377 OG SER A 152 14536 10526 14586 1387 213 531 O ATOM 378 N TYR A 153 -47.881-134.400 306.708 1.00 86.90 N ANISOU 378 N TYR A 153 12276 8294 12449 954 276 81 N ATOM 379 CA TYR A 153 -47.028-135.572 306.929 1.00 84.18 C ANISOU 379 CA TYR A 153 11861 8176 11947 784 255 -22 C ATOM 380 C TYR A 153 -47.822-136.873 306.985 1.00 83.82 C ANISOU 380 C TYR A 153 11731 8460 11656 850 162 -48 C ATOM 381 O TYR A 153 -47.426-137.814 307.676 1.00 82.73 O ANISOU 381 O TYR A 153 11522 8487 11426 754 124 -201 O ATOM 382 CB TYR A 153 -46.186-135.431 308.200 1.00 82.10 C ANISOU 382 CB TYR A 153 11556 7840 11796 644 267 -299 C ATOM 383 CG TYR A 153 -45.266-134.241 308.203 1.00 85.32 C ANISOU 383 CG TYR A 153 12030 7928 12460 530 362 -317 C ATOM 384 CD1 TYR A 153 -44.536-133.901 307.074 1.00 85.89 C ANISOU 384 CD1 TYR A 153 12165 7884 12586 441 443 -91 C ATOM 385 CD2 TYR A 153 -45.132-133.452 309.335 1.00 87.74 C ANISOU 385 CD2 TYR A 153 12327 8057 12954 500 379 -570 C ATOM 386 CE1 TYR A 153 -43.693-132.812 307.074 1.00 88.02 C ANISOU 386 CE1 TYR A 153 12490 7847 13108 312 540 -98 C ATOM 387 CE2 TYR A 153 -44.295-132.364 309.345 1.00 88.58 C ANISOU 387 CE2 TYR A 153 12487 7851 13319 375 469 -609 C ATOM 388 CZ TYR A 153 -43.578-132.047 308.214 1.00 88.48 C ANISOU 388 CZ TYR A 153 12540 7705 13375 276 551 -363 C ATOM 389 OH TYR A 153 -42.744-130.958 308.239 1.00 90.39 O ANISOU 389 OH TYR A 153 12830 7621 13894 128 650 -397 O ATOM 390 N HIS A 154 -48.936-136.952 306.254 1.00 84.50 N ANISOU 390 N HIS A 154 11818 8647 11642 1009 123 109 N ATOM 391 CA HIS A 154 -49.754-138.161 306.292 1.00 81.57 C ANISOU 391 CA HIS A 154 11357 8578 11058 1054 39 73 C ATOM 392 C HIS A 154 -49.013-139.350 305.693 1.00 74.52 C ANISOU 392 C HIS A 154 10435 7867 10011 918 32 103 C ATOM 393 O HIS A 154 -48.964-140.430 306.293 1.00 71.31 O ANISOU 393 O HIS A 154 9959 7622 9513 852 -14 -28 O ATOM 394 CB HIS A 154 -51.074-137.925 305.561 1.00 86.84 C ANISOU 394 CB HIS A 154 12013 9328 11654 1249 -4 227 C ATOM 395 CG HIS A 154 -51.998-136.998 306.283 1.00 91.33 C ANISOU 395 CG HIS A 154 12572 9769 12359 1414 -11 154 C ATOM 396 ND1 HIS A 154 -52.387-137.209 307.589 1.00 92.88 N ANISOU 396 ND1 HIS A 154 12696 10027 12567 1417 -33 -84 N ATOM 397 CD2 HIS A 154 -52.607-135.856 305.888 1.00 96.19 C ANISOU 397 CD2 HIS A 154 13235 10204 13107 1591 3 285 C ATOM 398 CE1 HIS A 154 -53.196-136.236 307.966 1.00 96.84 C ANISOU 398 CE1 HIS A 154 13193 10400 13202 1588 -26 -126 C ATOM 399 NE2 HIS A 154 -53.346-135.402 306.953 1.00 98.92 N ANISOU 399 NE2 HIS A 154 13532 10497 13558 1704 -7 97 N ATOM 400 N PHE A 155 -48.434-139.170 304.506 1.00 71.76 N ANISOU 400 N PHE A 155 10136 7493 9634 878 81 280 N ATOM 401 CA PHE A 155 -47.685-140.253 303.879 1.00 68.49 C ANISOU 401 CA PHE A 155 9686 7252 9084 758 87 283 C ATOM 402 C PHE A 155 -46.404-140.553 304.647 1.00 68.44 C ANISOU 402 C PHE A 155 9657 7181 9166 599 118 127 C ATOM 403 O PHE A 155 -46.125-141.711 304.978 1.00 69.01 O ANISOU 403 O PHE A 155 9661 7399 9160 538 76 14 O ATOM 404 CB PHE A 155 -47.380-139.899 302.424 1.00 70.98 C ANISOU 404 CB PHE A 155 10050 7590 9329 755 144 506 C ATOM 405 CG PHE A 155 -46.183-140.611 301.865 1.00 75.34 C ANISOU 405 CG PHE A 155 10575 8239 9812 604 196 486 C ATOM 406 CD1 PHE A 155 -46.202-141.982 301.669 1.00 76.20 C ANISOU 406 CD1 PHE A 155 10606 8576 9772 570 149 380 C ATOM 407 CD2 PHE A 155 -45.040-139.906 301.528 1.00 78.09 C ANISOU 407 CD2 PHE A 155 10966 8445 10260 492 299 563 C ATOM 408 CE1 PHE A 155 -45.101-142.636 301.150 1.00 75.65 C ANISOU 408 CE1 PHE A 155 10498 8592 9654 451 201 339 C ATOM 409 CE2 PHE A 155 -43.938-140.555 301.011 1.00 77.83 C ANISOU 409 CE2 PHE A 155 10886 8525 10162 360 355 531 C ATOM 410 CZ PHE A 155 -43.968-141.922 300.822 1.00 76.07 C ANISOU 410 CZ PHE A 155 10582 8532 9790 351 304 412 C ATOM 411 N ILE A 156 -45.615-139.517 304.945 1.00 69.12 N ANISOU 411 N ILE A 156 9792 7043 9429 533 188 120 N ATOM 412 CA ILE A 156 -44.333-139.715 305.619 1.00 65.98 C ANISOU 412 CA ILE A 156 9352 6604 9113 377 214 -29 C ATOM 413 C ILE A 156 -44.535-140.352 306.989 1.00 62.78 C ANISOU 413 C ILE A 156 8877 6284 8691 378 134 -234 C ATOM 414 O ILE A 156 -43.778-141.244 307.393 1.00 61.09 O ANISOU 414 O ILE A 156 8595 6180 8437 291 107 -331 O ATOM 415 CB ILE A 156 -43.575-138.377 305.715 1.00 68.88 C ANISOU 415 CB ILE A 156 9778 6705 9690 295 305 -14 C ATOM 416 CG1 ILE A 156 -43.202-137.877 304.316 1.00 73.70 C ANISOU 416 CG1 ILE A 156 10449 7259 10295 262 397 226 C ATOM 417 CG2 ILE A 156 -42.333-138.522 306.582 1.00 66.27 C ANISOU 417 CG2 ILE A 156 9378 6357 9446 136 316 -205 C ATOM 418 CD1 ILE A 156 -42.498-136.536 304.308 1.00 76.66 C ANISOU 418 CD1 ILE A 156 10889 7340 10899 166 500 278 C ATOM 419 N GLY A 157 -45.562-139.917 307.720 1.00 62.28 N ANISOU 419 N GLY A 157 8824 6185 8653 484 96 -295 N ATOM 420 CA GLY A 157 -45.804-140.479 309.040 1.00 61.64 C ANISOU 420 CA GLY A 157 8673 6218 8529 480 29 -473 C ATOM 421 C GLY A 157 -46.240-141.932 308.986 1.00 58.73 C ANISOU 421 C GLY A 157 8245 6081 7990 493 -40 -454 C ATOM 422 O GLY A 157 -45.720-142.776 309.720 1.00 52.57 O ANISOU 422 O GLY A 157 7403 5403 7168 422 -81 -543 O ATOM 423 N SER A 158 -47.203-142.240 308.112 1.00 59.98 N ANISOU 423 N SER A 158 8415 6322 8054 583 -56 -334 N ATOM 424 CA SER A 158 -47.704-143.608 307.992 1.00 60.08 C ANISOU 424 CA SER A 158 8368 6532 7928 582 -115 -330 C ATOM 425 C SER A 158 -46.582-144.579 307.648 1.00 63.29 C ANISOU 425 C SER A 158 8748 6981 8316 474 -112 -339 C ATOM 426 O SER A 158 -46.469-145.656 308.246 1.00 62.09 O ANISOU 426 O SER A 158 8542 6921 8128 433 -161 -400 O ATOM 427 CB SER A 158 -48.807-143.664 306.933 1.00 58.84 C ANISOU 427 CB SER A 158 8217 6463 7677 681 -129 -212 C ATOM 428 OG SER A 158 -49.072-144.998 306.534 1.00 54.57 O ANISOU 428 OG SER A 158 7622 6090 7021 646 -172 -216 O ATOM 429 N LEU A 159 -45.736-144.206 306.685 1.00 66.86 N ANISOU 429 N LEU A 159 9235 7367 8802 432 -49 -272 N ATOM 430 CA LEU A 159 -44.639-145.076 306.273 1.00 66.84 C ANISOU 430 CA LEU A 159 9191 7414 8789 343 -34 -298 C ATOM 431 C LEU A 159 -43.687-145.354 307.429 1.00 65.61 C ANISOU 431 C LEU A 159 8984 7234 8713 270 -58 -415 C ATOM 432 O LEU A 159 -43.166-146.467 307.561 1.00 60.00 O ANISOU 432 O LEU A 159 8213 6598 7986 237 -92 -459 O ATOM 433 CB LEU A 159 -43.888-144.443 305.102 1.00 68.66 C ANISOU 433 CB LEU A 159 9457 7595 9035 302 56 -204 C ATOM 434 CG LEU A 159 -42.827-145.311 304.428 1.00 70.27 C ANISOU 434 CG LEU A 159 9604 7885 9209 227 90 -235 C ATOM 435 CD1 LEU A 159 -43.482-146.507 303.760 1.00 70.69 C ANISOU 435 CD1 LEU A 159 9626 8095 9136 270 48 -247 C ATOM 436 CD2 LEU A 159 -42.021-144.500 303.426 1.00 70.52 C ANISOU 436 CD2 LEU A 159 9662 7878 9256 166 198 -139 C ATOM 437 N ALA A 160 -43.451-144.352 308.280 1.00 69.86 N ANISOU 437 N ALA A 160 9535 7669 9339 250 -46 -474 N ATOM 438 CA ALA A 160 -42.537-144.535 309.403 1.00 68.34 C ANISOU 438 CA ALA A 160 9277 7491 9198 179 -80 -594 C ATOM 439 C ALA A 160 -43.101-145.514 310.425 1.00 64.35 C ANISOU 439 C ALA A 160 8723 7116 8610 213 -171 -635 C ATOM 440 O ALA A 160 -42.368-146.363 310.946 1.00 61.91 O ANISOU 440 O ALA A 160 8345 6880 8296 175 -218 -669 O ATOM 441 CB ALA A 160 -42.234-143.189 310.058 1.00 70.57 C ANISOU 441 CB ALA A 160 9580 7644 9591 139 -45 -679 C ATOM 442 N VAL A 161 -44.397-145.412 310.729 1.00 60.58 N ANISOU 442 N VAL A 161 8272 6677 8070 286 -194 -620 N ATOM 443 CA VAL A 161 -45.008-146.345 311.671 1.00 58.35 C ANISOU 443 CA VAL A 161 7940 6531 7700 302 -265 -634 C ATOM 444 C VAL A 161 -44.951-147.765 311.123 1.00 53.17 C ANISOU 444 C VAL A 161 7259 5933 7011 290 -296 -563 C ATOM 445 O VAL A 161 -44.603-148.710 311.841 1.00 49.50 O ANISOU 445 O VAL A 161 6744 5533 6532 263 -351 -562 O ATOM 446 CB VAL A 161 -46.453-145.920 311.991 1.00 59.55 C ANISOU 446 CB VAL A 161 8108 6728 7792 379 -268 -637 C ATOM 447 CG1 VAL A 161 -47.093-146.898 312.967 1.00 57.77 C ANISOU 447 CG1 VAL A 161 7822 6662 7465 372 -327 -634 C ATOM 448 CG2 VAL A 161 -46.477-144.508 312.550 1.00 62.35 C ANISOU 448 CG2 VAL A 161 8483 6995 8210 403 -233 -737 C ATOM 449 N ALA A 162 -45.278-147.935 309.839 1.00 52.37 N ANISOU 449 N ALA A 162 7191 5810 6899 313 -262 -506 N ATOM 450 CA ALA A 162 -45.279-149.267 309.242 1.00 51.84 C ANISOU 450 CA ALA A 162 7096 5786 6814 299 -284 -479 C ATOM 451 C ALA A 162 -43.894-149.900 309.291 1.00 56.26 C ANISOU 451 C ALA A 162 7613 6315 7449 255 -290 -510 C ATOM 452 O ALA A 162 -43.756-151.086 309.615 1.00 56.86 O ANISOU 452 O ALA A 162 7649 6409 7547 248 -337 -505 O ATOM 453 CB ALA A 162 -45.784-149.194 307.800 1.00 53.25 C ANISOU 453 CB ALA A 162 7306 5981 6946 327 -244 -441 C ATOM 454 N ASP A 163 -42.854-149.125 308.977 1.00 61.16 N ANISOU 454 N ASP A 163 8232 6882 8122 226 -239 -539 N ATOM 455 CA ASP A 163 -41.507-149.685 308.948 1.00 64.48 C ANISOU 455 CA ASP A 163 8586 7296 8616 192 -240 -580 C ATOM 456 C ASP A 163 -40.981-149.943 310.354 1.00 60.14 C ANISOU 456 C ASP A 163 7976 6780 8093 182 -314 -607 C ATOM 457 O ASP A 163 -40.294-150.944 310.589 1.00 59.23 O ANISOU 457 O ASP A 163 7796 6684 8026 193 -359 -607 O ATOM 458 CB ASP A 163 -40.567-148.756 308.180 1.00 71.58 C ANISOU 458 CB ASP A 163 9486 8153 9560 145 -153 -599 C ATOM 459 CG ASP A 163 -40.856-148.738 306.691 1.00 78.73 C ANISOU 459 CG ASP A 163 10430 9072 10413 155 -81 -554 C ATOM 460 OD1 ASP A 163 -41.631-149.598 306.225 1.00 81.00 O ANISOU 460 OD1 ASP A 163 10727 9410 10641 196 -107 -544 O ATOM 461 OD2 ASP A 163 -40.300-147.873 305.983 1.00 82.06 O ANISOU 461 OD2 ASP A 163 10866 9465 10847 112 3 -529 O ATOM 462 N LEU A 164 -41.292-149.058 311.303 1.00 56.39 N ANISOU 462 N LEU A 164 7516 6324 7588 170 -331 -633 N ATOM 463 CA LEU A 164 -40.828-149.251 312.674 1.00 55.23 C ANISOU 463 CA LEU A 164 7300 6259 7424 157 -407 -665 C ATOM 464 C LEU A 164 -41.431-150.511 313.283 1.00 57.78 C ANISOU 464 C LEU A 164 7607 6652 7694 195 -482 -578 C ATOM 465 O LEU A 164 -40.721-151.330 313.880 1.00 58.02 O ANISOU 465 O LEU A 164 7570 6731 7745 204 -548 -545 O ATOM 466 CB LEU A 164 -41.166-148.024 313.519 1.00 56.02 C ANISOU 466 CB LEU A 164 7416 6380 7488 135 -401 -745 C ATOM 467 CG LEU A 164 -40.777-148.088 314.997 1.00 58.07 C ANISOU 467 CG LEU A 164 7598 6780 7687 116 -481 -801 C ATOM 468 CD1 LEU A 164 -39.315-148.462 315.148 1.00 58.46 C ANISOU 468 CD1 LEU A 164 7549 6869 7794 84 -522 -827 C ATOM 469 CD2 LEU A 164 -41.069-146.761 315.677 1.00 59.53 C ANISOU 469 CD2 LEU A 164 7795 6972 7851 88 -457 -935 C ATOM 470 N LEU A 165 -42.746-150.684 313.137 1.00 58.86 N ANISOU 470 N LEU A 165 7799 6796 7770 216 -472 -529 N ATOM 471 CA LEU A 165 -43.400-151.880 313.660 1.00 57.57 C ANISOU 471 CA LEU A 165 7621 6683 7570 225 -527 -435 C ATOM 472 C LEU A 165 -42.917-153.131 312.940 1.00 60.09 C ANISOU 472 C LEU A 165 7926 6917 7990 237 -538 -391 C ATOM 473 O LEU A 165 -42.563-154.130 313.577 1.00 57.99 O ANISOU 473 O LEU A 165 7618 6655 7760 248 -600 -315 O ATOM 474 CB LEU A 165 -44.917-151.747 313.533 1.00 51.59 C ANISOU 474 CB LEU A 165 6907 5961 6736 231 -502 -411 C ATOM 475 CG LEU A 165 -45.606-150.778 314.488 1.00 50.66 C ANISOU 475 CG LEU A 165 6785 5947 6516 237 -499 -454 C ATOM 476 CD1 LEU A 165 -47.111-150.877 314.317 1.00 49.47 C ANISOU 476 CD1 LEU A 165 6648 5849 6299 252 -478 -423 C ATOM 477 CD2 LEU A 165 -45.209-151.082 315.923 1.00 52.73 C ANISOU 477 CD2 LEU A 165 6988 6338 6707 215 -561 -430 C ATOM 478 N GLY A 166 -42.895-153.092 311.606 1.00 59.96 N ANISOU 478 N GLY A 166 7937 6825 8019 241 -478 -439 N ATOM 479 CA GLY A 166 -42.554-154.283 310.845 1.00 62.24 C ANISOU 479 CA GLY A 166 8207 7036 8404 255 -478 -441 C ATOM 480 C GLY A 166 -41.155-154.786 311.135 1.00 66.32 C ANISOU 480 C GLY A 166 8652 7522 9024 283 -512 -451 C ATOM 481 O GLY A 166 -40.942-155.983 311.333 1.00 71.96 O ANISOU 481 O GLY A 166 9336 8174 9831 313 -557 -404 O ATOM 482 N SER A 167 -40.182-153.874 311.168 1.00 63.06 N ANISOU 482 N SER A 167 8203 7147 8611 274 -490 -510 N ATOM 483 CA SER A 167 -38.803-154.281 311.417 1.00 60.71 C ANISOU 483 CA SER A 167 7808 6851 8408 304 -523 -533 C ATOM 484 C SER A 167 -38.653-154.914 312.795 1.00 59.34 C ANISOU 484 C SER A 167 7587 6727 8231 338 -631 -433 C ATOM 485 O SER A 167 -37.948-155.918 312.948 1.00 63.17 O ANISOU 485 O SER A 167 8006 7173 8821 401 -683 -392 O ATOM 486 CB SER A 167 -37.870-153.081 311.274 1.00 63.73 C ANISOU 486 CB SER A 167 8148 7282 8784 260 -476 -620 C ATOM 487 OG SER A 167 -38.201-152.075 312.214 1.00 66.78 O ANISOU 487 OG SER A 167 8556 7733 9084 217 -498 -622 O ATOM 488 N VAL A 168 -39.308-154.346 313.808 1.00 57.93 N ANISOU 488 N VAL A 168 7435 6644 7930 306 -666 -388 N ATOM 489 CA VAL A 168 -39.192-154.889 315.157 1.00 59.69 C ANISOU 489 CA VAL A 168 7609 6965 8106 331 -768 -275 C ATOM 490 C VAL A 168 -39.784-156.291 315.223 1.00 61.13 C ANISOU 490 C VAL A 168 7819 7057 8350 365 -803 -129 C ATOM 491 O VAL A 168 -39.147-157.226 315.722 1.00 63.80 O ANISOU 491 O VAL A 168 8100 7377 8766 426 -877 -23 O ATOM 492 CB VAL A 168 -39.854-153.949 316.181 1.00 59.15 C ANISOU 492 CB VAL A 168 7558 7048 7869 283 -781 -287 C ATOM 493 CG1 VAL A 168 -40.085-154.680 317.495 1.00 57.51 C ANISOU 493 CG1 VAL A 168 7314 6968 7569 301 -875 -133 C ATOM 494 CG2 VAL A 168 -38.986-152.732 316.412 1.00 58.77 C ANISOU 494 CG2 VAL A 168 7454 7078 7796 248 -773 -431 C ATOM 495 N ILE A 169 -41.009-156.461 314.720 1.00 62.87 N ANISOU 495 N ILE A 169 8121 7215 8552 326 -751 -118 N ATOM 496 CA ILE A 169 -41.643-157.776 314.747 1.00 65.84 C ANISOU 496 CA ILE A 169 8522 7484 9008 329 -773 6 C ATOM 497 C ILE A 169 -40.851-158.765 313.899 1.00 66.35 C ANISOU 497 C ILE A 169 8562 7373 9276 388 -770 -29 C ATOM 498 O ILE A 169 -40.587-159.898 314.320 1.00 71.33 O ANISOU 498 O ILE A 169 9170 7905 10029 434 -827 95 O ATOM 499 CB ILE A 169 -43.109-157.684 314.284 1.00 65.47 C ANISOU 499 CB ILE A 169 8546 7429 8902 261 -714 -11 C ATOM 500 CG1 ILE A 169 -43.884-156.696 315.154 1.00 65.65 C ANISOU 500 CG1 ILE A 169 8577 7631 8735 222 -711 4 C ATOM 501 CG2 ILE A 169 -43.770-159.047 314.350 1.00 65.77 C ANISOU 501 CG2 ILE A 169 8601 7348 9040 233 -731 107 C ATOM 502 CD1 ILE A 169 -45.374-156.688 314.878 1.00 65.30 C ANISOU 502 CD1 ILE A 169 8573 7610 8629 167 -665 6 C ATOM 503 N PHE A 170 -40.448-158.346 312.697 1.00 61.19 N ANISOU 503 N PHE A 170 7905 6680 8664 394 -700 -194 N ATOM 504 CA PHE A 170 -39.704-159.241 311.815 1.00 58.16 C ANISOU 504 CA PHE A 170 7483 6154 8463 454 -683 -271 C ATOM 505 C PHE A 170 -38.405-159.693 312.467 1.00 56.41 C ANISOU 505 C PHE A 170 7165 5924 8345 549 -756 -214 C ATOM 506 O PHE A 170 -38.211-160.884 312.730 1.00 60.69 O ANISOU 506 O PHE A 170 7687 6330 9043 616 -807 -123 O ATOM 507 CB PHE A 170 -39.420-158.563 310.473 1.00 57.71 C ANISOU 507 CB PHE A 170 7424 6120 8382 436 -587 -453 C ATOM 508 CG PHE A 170 -38.597-159.402 309.532 1.00 60.89 C ANISOU 508 CG PHE A 170 7768 6418 8950 499 -554 -571 C ATOM 509 CD1 PHE A 170 -39.207-160.289 308.662 1.00 62.78 C ANISOU 509 CD1 PHE A 170 8039 6542 9273 490 -517 -653 C ATOM 510 CD2 PHE A 170 -37.213-159.303 309.516 1.00 60.42 C ANISOU 510 CD2 PHE A 170 7606 6390 8962 565 -556 -626 C ATOM 511 CE1 PHE A 170 -38.455-161.063 307.799 1.00 63.29 C ANISOU 511 CE1 PHE A 170 8041 6515 9490 553 -480 -798 C ATOM 512 CE2 PHE A 170 -36.457-160.076 308.657 1.00 60.70 C ANISOU 512 CE2 PHE A 170 7570 6345 9150 636 -518 -756 C ATOM 513 CZ PHE A 170 -37.079-160.955 307.797 1.00 63.46 C ANISOU 513 CZ PHE A 170 7958 6570 9581 633 -477 -849 C ATOM 514 N VAL A 171 -37.503-158.744 312.741 1.00 52.54 N ANISOU 514 N VAL A 171 6607 5575 7782 555 -764 -266 N ATOM 515 CA VAL A 171 -36.169-159.086 313.233 1.00 53.68 C ANISOU 515 CA VAL A 171 6628 5750 8019 650 -834 -243 C ATOM 516 C VAL A 171 -36.254-159.986 314.458 1.00 56.38 C ANISOU 516 C VAL A 171 6954 6078 8388 713 -951 -26 C ATOM 517 O VAL A 171 -35.503-160.961 314.578 1.00 56.55 O ANISOU 517 O VAL A 171 6904 6007 8576 829 -1010 38 O ATOM 518 CB VAL A 171 -35.358-157.808 313.520 1.00 50.44 C ANISOU 518 CB VAL A 171 6143 5524 7499 610 -830 -331 C ATOM 519 CG1 VAL A 171 -34.054-158.150 314.232 1.00 48.25 C ANISOU 519 CG1 VAL A 171 5714 5330 7289 704 -927 -294 C ATOM 520 CG2 VAL A 171 -35.072-157.066 312.225 1.00 48.65 C ANISOU 520 CG2 VAL A 171 5918 5286 7282 556 -708 -510 C ATOM 521 N TYR A 172 -37.184-159.698 315.373 1.00 56.73 N ANISOU 521 N TYR A 172 7063 6219 8274 646 -984 100 N ATOM 522 CA TYR A 172 -37.308-160.541 316.558 1.00 61.89 C ANISOU 522 CA TYR A 172 7703 6889 8922 693 -1088 340 C ATOM 523 C TYR A 172 -37.741-161.953 316.179 1.00 63.89 C ANISOU 523 C TYR A 172 8009 6881 9384 732 -1084 448 C ATOM 524 O TYR A 172 -37.073-162.935 316.524 1.00 65.56 O ANISOU 524 O TYR A 172 8168 6988 9755 846 -1158 582 O ATOM 525 CB TYR A 172 -38.287-159.935 317.568 1.00 63.26 C ANISOU 525 CB TYR A 172 7927 7248 8862 599 -1103 437 C ATOM 526 CG TYR A 172 -38.207-160.631 318.914 1.00 69.72 C ANISOU 526 CG TYR A 172 8707 8165 9619 645 -1216 699 C ATOM 527 CD1 TYR A 172 -38.756-161.895 319.101 1.00 74.11 C ANISOU 527 CD1 TYR A 172 9314 8549 10293 661 -1236 917 C ATOM 528 CD2 TYR A 172 -37.561-160.037 319.989 1.00 72.43 C ANISOU 528 CD2 TYR A 172 8957 8778 9786 666 -1304 733 C ATOM 529 CE1 TYR A 172 -38.667-162.543 320.315 1.00 77.74 C ANISOU 529 CE1 TYR A 172 9742 9101 10694 704 -1336 1199 C ATOM 530 CE2 TYR A 172 -37.471-160.680 321.213 1.00 77.15 C ANISOU 530 CE2 TYR A 172 9511 9506 10295 713 -1413 994 C ATOM 531 CZ TYR A 172 -38.028-161.932 321.368 1.00 79.71 C ANISOU 531 CZ TYR A 172 9897 9653 10735 736 -1427 1245 C ATOM 532 OH TYR A 172 -37.945-162.580 322.579 1.00 83.03 O ANISOU 532 OH TYR A 172 10280 10205 11062 782 -1533 1548 O ATOM 533 N SER A 173 -38.874-162.074 315.483 1.00 60.24 N ANISOU 533 N SER A 173 7646 6307 8934 639 -1000 388 N ATOM 534 CA SER A 173 -39.374-163.395 315.113 1.00 60.45 C ANISOU 534 CA SER A 173 7723 6074 9172 646 -988 460 C ATOM 535 C SER A 173 -38.390-164.121 314.204 1.00 61.00 C ANISOU 535 C SER A 173 7737 5947 9494 760 -975 329 C ATOM 536 O SER A 173 -38.213-165.340 314.312 1.00 61.68 O ANISOU 536 O SER A 173 7820 5808 9808 835 -1012 436 O ATOM 537 CB SER A 173 -40.738-163.264 314.435 1.00 58.05 C ANISOU 537 CB SER A 173 7508 5732 8817 513 -900 369 C ATOM 538 OG SER A 173 -41.670-162.634 315.296 1.00 57.72 O ANISOU 538 OG SER A 173 7500 5876 8553 421 -905 480 O ATOM 539 N PHE A 174 -37.728-163.379 313.315 1.00 58.69 N ANISOU 539 N PHE A 174 7395 5733 9171 777 -918 100 N ATOM 540 CA PHE A 174 -36.801-163.980 312.362 1.00 56.55 C ANISOU 540 CA PHE A 174 7054 5320 9114 881 -885 -65 C ATOM 541 C PHE A 174 -35.577-164.556 313.067 1.00 61.61 C ANISOU 541 C PHE A 174 7581 5931 9896 1044 -984 51 C ATOM 542 O PHE A 174 -35.179-165.698 312.809 1.00 62.31 O ANISOU 542 O PHE A 174 7639 5791 10245 1158 -1000 54 O ATOM 543 CB PHE A 174 -36.390-162.929 311.333 1.00 52.02 C ANISOU 543 CB PHE A 174 6445 4891 8429 842 -792 -306 C ATOM 544 CG PHE A 174 -35.898-163.496 310.042 1.00 53.22 C ANISOU 544 CG PHE A 174 6551 4923 8748 898 -714 -528 C ATOM 545 CD1 PHE A 174 -36.784-164.032 309.123 1.00 55.10 C ANISOU 545 CD1 PHE A 174 6861 5032 9041 837 -645 -648 C ATOM 546 CD2 PHE A 174 -34.549-163.472 309.734 1.00 56.32 C ANISOU 546 CD2 PHE A 174 6810 5362 9228 1005 -705 -639 C ATOM 547 CE1 PHE A 174 -36.334-164.544 307.927 1.00 59.27 C ANISOU 547 CE1 PHE A 174 7338 5482 9701 884 -569 -885 C ATOM 548 CE2 PHE A 174 -34.091-163.982 308.540 1.00 59.57 C ANISOU 548 CE2 PHE A 174 7164 5693 9777 1058 -621 -866 C ATOM 549 CZ PHE A 174 -34.985-164.519 307.634 1.00 61.47 C ANISOU 549 CZ PHE A 174 7485 5808 10061 998 -552 -995 C ATOM 550 N ILE A 175 -34.955-163.767 313.947 1.00 63.10 N ANISOU 550 N ILE A 175 7697 6353 9925 1062 -1053 134 N ATOM 551 CA ILE A 175 -33.821-164.258 314.726 1.00 64.63 C ANISOU 551 CA ILE A 175 7765 6574 10218 1221 -1169 266 C ATOM 552 C ILE A 175 -34.245-165.437 315.591 1.00 65.71 C ANISOU 552 C ILE A 175 7950 6541 10477 1286 -1259 557 C ATOM 553 O ILE A 175 -33.529-166.440 315.702 1.00 65.42 O ANISOU 553 O ILE A 175 7844 6337 10674 1451 -1323 647 O ATOM 554 CB ILE A 175 -33.228-163.120 315.580 1.00 62.36 C ANISOU 554 CB ILE A 175 7388 6608 9698 1195 -1232 287 C ATOM 555 CG1 ILE A 175 -32.581-162.051 314.697 1.00 60.96 C ANISOU 555 CG1 ILE A 175 7142 6558 9462 1140 -1140 15 C ATOM 556 CG2 ILE A 175 -32.217-163.664 316.577 1.00 63.32 C ANISOU 556 CG2 ILE A 175 7373 6807 9879 1356 -1379 469 C ATOM 557 CD1 ILE A 175 -31.315-162.505 314.027 1.00 62.70 C ANISOU 557 CD1 ILE A 175 7212 6729 9881 1275 -1129 -120 C ATOM 558 N ASP A 176 -35.425-165.337 316.208 1.00 67.33 N ANISOU 558 N ASP A 176 8270 6780 10532 1159 -1260 717 N ATOM 559 CA ASP A 176 -35.897-166.377 317.114 1.00 70.43 C ANISOU 559 CA ASP A 176 8713 7038 11008 1189 -1335 1033 C ATOM 560 C ASP A 176 -36.115-167.695 316.381 1.00 72.46 C ANISOU 560 C ASP A 176 9023 6900 11607 1238 -1294 1024 C ATOM 561 O ASP A 176 -35.806-168.769 316.908 1.00 74.24 O ANISOU 561 O ASP A 176 9236 6931 12040 1358 -1371 1255 O ATOM 562 CB ASP A 176 -37.189-165.914 317.787 1.00 72.00 C ANISOU 562 CB ASP A 176 9013 7382 10961 1016 -1314 1161 C ATOM 563 CG ASP A 176 -37.373-166.495 319.168 1.00 77.88 C ANISOU 563 CG ASP A 176 9761 8188 11640 1041 -1418 1532 C ATOM 564 OD1 ASP A 176 -36.402-167.058 319.715 1.00 80.66 O ANISOU 564 OD1 ASP A 176 10028 8526 12092 1202 -1526 1702 O ATOM 565 OD2 ASP A 176 -38.491-166.382 319.715 1.00 79.78 O ANISOU 565 OD2 ASP A 176 10080 8513 11718 902 -1390 1663 O ATOM 566 N PHE A 177 -36.637-167.632 315.157 1.00 71.29 N ANISOU 566 N PHE A 177 8931 6629 11527 1150 -1175 755 N ATOM 567 CA PHE A 177 -36.967-168.852 314.431 1.00 70.94 C ANISOU 567 CA PHE A 177 8938 6216 11800 1167 -1127 697 C ATOM 568 C PHE A 177 -35.733-169.499 313.807 1.00 72.34 C ANISOU 568 C PHE A 177 9010 6216 12259 1364 -1137 550 C ATOM 569 O PHE A 177 -35.562-170.719 313.897 1.00 77.16 O ANISOU 569 O PHE A 177 9625 6509 13182 1472 -1170 655 O ATOM 570 CB PHE A 177 -38.011-168.552 313.356 1.00 68.41 C ANISOU 570 CB PHE A 177 8697 5873 11421 996 -1005 446 C ATOM 571 CG PHE A 177 -38.405-169.749 312.545 1.00 70.61 C ANISOU 571 CG PHE A 177 9020 5798 12013 985 -950 326 C ATOM 572 CD1 PHE A 177 -39.343-170.647 313.025 1.00 70.67 C ANISOU 572 CD1 PHE A 177 9113 5580 12157 894 -959 525 C ATOM 573 CD2 PHE A 177 -37.841-169.977 311.301 1.00 71.82 C ANISOU 573 CD2 PHE A 177 9118 5848 12321 1053 -881 1 C ATOM 574 CE1 PHE A 177 -39.709-171.752 312.282 1.00 72.23 C ANISOU 574 CE1 PHE A 177 9347 5429 12668 866 -906 389 C ATOM 575 CE2 PHE A 177 -38.203-171.080 310.553 1.00 73.49 C ANISOU 575 CE2 PHE A 177 9362 5738 12825 1038 -829 -153 C ATOM 576 CZ PHE A 177 -39.139-171.968 311.043 1.00 73.56 C ANISOU 576 CZ PHE A 177 9461 5496 12994 941 -843 34 C ATOM 577 N HIS A 178 -34.868-168.708 313.173 1.00 69.08 N ANISOU 577 N HIS A 178 8496 5995 11755 1415 -1102 307 N ATOM 578 CA HIS A 178 -33.746-169.271 312.435 1.00 69.55 C ANISOU 578 CA HIS A 178 8438 5920 12069 1592 -1085 114 C ATOM 579 C HIS A 178 -32.516-169.525 313.293 1.00 70.27 C ANISOU 579 C HIS A 178 8390 6061 12249 1802 -1211 293 C ATOM 580 O HIS A 178 -31.789-170.492 313.047 1.00 76.24 O ANISOU 580 O HIS A 178 9068 6585 13315 1990 -1233 259 O ATOM 581 CB HIS A 178 -33.369-168.361 311.263 1.00 69.01 C ANISOU 581 CB HIS A 178 8309 6046 11867 1540 -972 -232 C ATOM 582 CG HIS A 178 -34.278-168.488 310.080 1.00 70.09 C ANISOU 582 CG HIS A 178 8536 6079 12016 1409 -849 -473 C ATOM 583 ND1 HIS A 178 -34.552-169.699 309.478 1.00 70.81 N ANISOU 583 ND1 HIS A 178 8656 5847 12401 1448 -812 -588 N ATOM 584 CD2 HIS A 178 -34.970-167.558 309.382 1.00 69.80 C ANISOU 584 CD2 HIS A 178 8558 6227 11736 1243 -759 -626 C ATOM 585 CE1 HIS A 178 -35.376-169.508 308.466 1.00 70.88 C ANISOU 585 CE1 HIS A 178 8729 5877 12324 1302 -709 -816 C ATOM 586 NE2 HIS A 178 -35.646-168.217 308.385 1.00 70.51 N ANISOU 586 NE2 HIS A 178 8702 6142 11947 1184 -679 -826 N ATOM 587 N VAL A 179 -32.256-168.683 314.295 1.00 65.68 N ANISOU 587 N VAL A 179 7764 5784 11407 1782 -1297 469 N ATOM 588 CA VAL A 179 -31.067-168.833 315.124 1.00 67.56 C ANISOU 588 CA VAL A 179 7845 6137 11687 1976 -1431 629 C ATOM 589 C VAL A 179 -31.375-169.610 316.399 1.00 68.83 C ANISOU 589 C VAL A 179 8056 6206 11892 2044 -1563 1042 C ATOM 590 O VAL A 179 -30.542-170.383 316.876 1.00 67.23 O ANISOU 590 O VAL A 179 7751 5909 11885 2260 -1672 1214 O ATOM 591 CB VAL A 179 -30.456-167.453 315.445 1.00 68.59 C ANISOU 591 CB VAL A 179 7867 6682 11511 1916 -1453 544 C ATOM 592 CG1 VAL A 179 -29.272-167.587 316.394 1.00 70.12 C ANISOU 592 CG1 VAL A 179 7879 7045 11717 2104 -1608 713 C ATOM 593 CG2 VAL A 179 -30.023-166.756 314.163 1.00 69.00 C ANISOU 593 CG2 VAL A 179 7859 6811 11548 1861 -1317 173 C ATOM 594 N PHE A 180 -32.577-169.435 316.959 1.00 68.11 N ANISOU 594 N PHE A 180 8112 6146 11620 1866 -1553 1219 N ATOM 595 CA PHE A 180 -32.941-170.105 318.201 1.00 70.73 C ANISOU 595 CA PHE A 180 8494 6435 11947 1900 -1664 1638 C ATOM 596 C PHE A 180 -33.815-171.332 317.987 1.00 73.23 C ANISOU 596 C PHE A 180 8949 6325 12548 1868 -1618 1773 C ATOM 597 O PHE A 180 -33.957-172.135 318.913 1.00 73.92 O ANISOU 597 O PHE A 180 9069 6294 12722 1929 -1707 2149 O ATOM 598 CB PHE A 180 -33.651-169.127 319.142 1.00 68.77 C ANISOU 598 CB PHE A 180 8293 6544 11293 1725 -1687 1772 C ATOM 599 CG PHE A 180 -32.762-168.035 319.655 1.00 69.22 C ANISOU 599 CG PHE A 180 8206 7012 11084 1760 -1762 1700 C ATOM 600 CD1 PHE A 180 -32.402-166.976 318.841 1.00 67.26 C ANISOU 600 CD1 PHE A 180 7903 6914 10738 1693 -1679 1344 C ATOM 601 CD2 PHE A 180 -32.274-168.076 320.950 1.00 69.84 C ANISOU 601 CD2 PHE A 180 8194 7332 11008 1853 -1916 1990 C ATOM 602 CE1 PHE A 180 -31.574-165.974 319.308 1.00 66.22 C ANISOU 602 CE1 PHE A 180 7633 7137 10391 1703 -1742 1262 C ATOM 603 CE2 PHE A 180 -31.449-167.077 321.424 1.00 70.16 C ANISOU 603 CE2 PHE A 180 8087 7763 10809 1870 -1989 1890 C ATOM 604 CZ PHE A 180 -31.097-166.025 320.603 1.00 68.20 C ANISOU 604 CZ PHE A 180 7787 7630 10495 1788 -1898 1517 C ATOM 605 N HIS A 181 -34.395-171.492 316.796 1.00 76.32 N ANISOU 605 N HIS A 181 9417 6495 13085 1765 -1483 1481 N ATOM 606 CA HIS A 181 -35.188-172.672 316.447 1.00 83.19 C ANISOU 606 CA HIS A 181 10404 6938 14265 1717 -1428 1538 C ATOM 607 C HIS A 181 -36.395-172.822 317.367 1.00 86.76 C ANISOU 607 C HIS A 181 10981 7404 14579 1539 -1438 1864 C ATOM 608 O HIS A 181 -36.700-173.917 317.843 1.00 90.18 O ANISOU 608 O HIS A 181 11477 7535 15250 1561 -1469 2150 O ATOM 609 CB HIS A 181 -34.330-173.938 316.465 1.00 90.22 C ANISOU 609 CB HIS A 181 11239 7465 15577 1962 -1493 1649 C ATOM 610 CG HIS A 181 -33.050-173.800 315.703 1.00 94.29 C ANISOU 610 CG HIS A 181 11598 8013 16215 2160 -1491 1351 C ATOM 611 ND1 HIS A 181 -31.834-174.204 316.209 1.00 98.50 N ANISOU 611 ND1 HIS A 181 11990 8538 16898 2427 -1612 1502 N ATOM 612 CD2 HIS A 181 -32.797-173.290 314.474 1.00 92.13 C ANISOU 612 CD2 HIS A 181 11273 7810 15924 2128 -1380 917 C ATOM 613 CE1 HIS A 181 -30.886-173.954 315.322 1.00 97.72 C ANISOU 613 CE1 HIS A 181 11752 8499 16878 2547 -1568 1156 C ATOM 614 NE2 HIS A 181 -31.444-173.397 314.263 1.00 93.78 N ANISOU 614 NE2 HIS A 181 11309 8051 16273 2363 -1423 803 N ATOM 615 N ARG A 182 -37.086-171.714 317.623 1.00 88.68 N ANISOU 615 N ARG A 182 11255 7996 14444 1361 -1404 1825 N ATOM 616 CA ARG A 182 -38.331-171.777 318.376 1.00 92.07 C ANISOU 616 CA ARG A 182 11787 8475 14719 1171 -1387 2077 C ATOM 617 C ARG A 182 -39.329-172.663 317.648 1.00 92.52 C ANISOU 617 C ARG A 182 11949 8159 15044 1034 -1285 1999 C ATOM 618 O ARG A 182 -39.661-172.419 316.484 1.00 88.98 O ANISOU 618 O ARG A 182 11516 7654 14638 955 -1187 1639 O ATOM 619 CB ARG A 182 -38.910-170.376 318.576 1.00 90.35 C ANISOU 619 CB ARG A 182 11572 8679 14079 1017 -1350 1961 C ATOM 620 CG ARG A 182 -38.282-169.585 319.711 1.00 94.61 C ANISOU 620 CG ARG A 182 12026 9609 14311 1087 -1456 2129 C ATOM 621 CD ARG A 182 -38.814-170.004 321.076 1.00101.45 C ANISOU 621 CD ARG A 182 12926 10576 15043 1039 -1521 2557 C ATOM 622 NE ARG A 182 -40.252-169.780 321.209 1.00104.14 N ANISOU 622 NE ARG A 182 13359 10986 15224 810 -1427 2582 N ATOM 623 CZ ARG A 182 -40.806-168.900 322.038 1.00104.77 C ANISOU 623 CZ ARG A 182 13428 11448 14933 702 -1427 2648 C ATOM 624 NH1 ARG A 182 -40.048-168.152 322.830 1.00104.29 N ANISOU 624 NH1 ARG A 182 13275 11735 14615 789 -1520 2687 N ATOM 625 NH2 ARG A 182 -42.125-168.774 322.082 1.00104.47 N ANISOU 625 NH2 ARG A 182 13457 11455 14782 507 -1333 2656 N ATOM 626 N LYS A 183 -39.774-173.713 318.327 1.00 96.83 N ANISOU 626 N LYS A 183 12561 8454 15776 1005 -1310 2342 N ATOM 627 CA LYS A 183 -40.887-174.539 317.856 1.00 96.86 C ANISOU 627 CA LYS A 183 12664 8126 16012 822 -1213 2315 C ATOM 628 C LYS A 183 -42.142-173.981 318.504 1.00 96.09 C ANISOU 628 C LYS A 183 12615 8305 15589 586 -1169 2463 C ATOM 629 O LYS A 183 -42.388-174.181 319.696 1.00 98.88 O ANISOU 629 O LYS A 183 12987 8760 15825 553 -1219 2864 O ATOM 630 CB LYS A 183 -40.665-176.004 318.203 1.00 99.75 C ANISOU 630 CB LYS A 183 13072 8026 16801 911 -1251 2606 C ATOM 631 N ASP A 184 -42.934-173.256 317.720 1.00 92.14 N ANISOU 631 N ASP A 184 12125 7956 14928 428 -1077 2143 N ATOM 632 CA ASP A 184 -44.123-172.601 318.233 1.00 90.25 C ANISOU 632 CA ASP A 184 11908 8012 14371 221 -1029 2223 C ATOM 633 C ASP A 184 -45.370-173.393 317.879 1.00 89.23 C ANISOU 633 C ASP A 184 11840 7635 14430 1 -936 2218 C ATOM 634 O ASP A 184 -45.431-174.080 316.851 1.00 89.24 O ANISOU 634 O ASP A 184 11860 7305 14741 -21 -887 1981 O ATOM 635 CB ASP A 184 -44.253-171.180 317.687 1.00 90.09 C ANISOU 635 CB ASP A 184 11847 8352 14031 196 -994 1900 C ATOM 636 CG ASP A 184 -43.408-170.181 318.447 1.00 91.44 C ANISOU 636 CG ASP A 184 11957 8875 13912 326 -1075 1974 C ATOM 637 OD1 ASP A 184 -43.296-170.322 319.681 1.00 95.84 O ANISOU 637 OD1 ASP A 184 12504 9563 14348 348 -1143 2313 O ATOM 638 OD2 ASP A 184 -42.869-169.248 317.818 1.00 86.42 O ANISOU 638 OD2 ASP A 184 11278 8398 13161 394 -1068 1694 O ATOM 639 N SER A 185 -46.360-173.306 318.771 1.00 89.55 N ANISOU 639 N SER A 185 11896 7855 14274 -171 -909 2474 N ATOM 640 CA SER A 185 -47.702-173.744 318.431 1.00 90.40 C ANISOU 640 CA SER A 185 12031 7849 14467 -420 -809 2421 C ATOM 641 C SER A 185 -48.106-173.091 317.124 1.00 82.83 C ANISOU 641 C SER A 185 11045 6975 13453 -472 -748 1952 C ATOM 642 O SER A 185 -47.644-171.992 316.803 1.00 81.05 O ANISOU 642 O SER A 185 10782 7024 12990 -362 -770 1747 O ATOM 643 CB SER A 185 -48.689-173.363 319.531 1.00 95.00 C ANISOU 643 CB SER A 185 12600 8756 14739 -587 -779 2696 C ATOM 644 OG SER A 185 -48.774-171.959 319.643 1.00 99.64 O ANISOU 644 OG SER A 185 13173 9570 15115 -458 -864 3015 O ATOM 645 N ARG A 186 -48.963-173.769 316.356 1.00 80.30 N ANISOU 645 N ARG A 186 10737 6421 13353 -646 -673 1782 N ATOM 646 CA ARG A 186 -49.283-173.245 315.036 1.00 79.54 C ANISOU 646 CA ARG A 186 10606 6407 13210 -680 -627 1337 C ATOM 647 C ARG A 186 -49.867-171.835 315.109 1.00 74.76 C ANISOU 647 C ARG A 186 9952 6276 12176 -714 -613 1243 C ATOM 648 O ARG A 186 -49.501-170.955 314.315 1.00 70.58 O ANISOU 648 O ARG A 186 9398 5917 11503 -615 -617 965 O ATOM 649 CB ARG A 186 -50.269-174.151 314.330 1.00 84.93 C ANISOU 649 CB ARG A 186 11289 6832 14149 -893 -553 1178 C ATOM 650 CG ARG A 186 -50.747-173.553 313.041 1.00 86.29 C ANISOU 650 CG ARG A 186 11409 7172 14206 -943 -514 743 C ATOM 651 CD ARG A 186 -51.844-174.302 312.506 1.00 91.09 C ANISOU 651 CD ARG A 186 11993 7621 14995 -1178 -450 598 C ATOM 652 NE ARG A 186 -52.920-174.112 313.455 1.00 94.52 N ANISOU 652 NE ARG A 186 12404 8259 15250 -1356 -420 861 N ATOM 653 CZ ARG A 186 -54.096-174.715 313.397 1.00100.27 C ANISOU 653 CZ ARG A 186 13095 8916 16088 -1611 -357 849 C ATOM 654 NH1 ARG A 186 -55.006-174.454 314.320 1.00102.47 N ANISOU 654 NH1 ARG A 186 13336 9429 16169 -1759 -323 1099 N ATOM 655 NH2 ARG A 186 -54.366-175.574 312.424 1.00104.23 N ANISOU 655 NH2 ARG A 186 13582 9128 16892 -1728 -323 570 N ATOM 656 N ASN A 187 -50.820-171.617 316.022 1.00 73.42 N ANISOU 656 N ASN A 187 9766 6320 11812 -858 -586 1466 N ATOM 657 CA ASN A 187 -51.520-170.340 316.032 1.00 69.99 C ANISOU 657 CA ASN A 187 9277 6303 11011 -894 -562 1345 C ATOM 658 C ASN A 187 -50.600-169.205 316.471 1.00 65.75 C ANISOU 658 C ASN A 187 8737 6029 10218 -700 -622 1362 C ATOM 659 O ASN A 187 -50.714-168.083 315.962 1.00 60.40 O ANISOU 659 O ASN A 187 8029 5592 9330 -654 -612 1137 O ATOM 660 CB ASN A 187 -52.740-170.418 316.938 1.00 72.16 C ANISOU 660 CB ASN A 187 9516 6755 11147 -1089 -511 1566 C ATOM 661 CG ASN A 187 -53.947-170.995 316.241 1.00 71.93 C ANISOU 661 CG ASN A 187 9446 6626 11258 -1309 -437 1413 C ATOM 662 OD1 ASN A 187 -53.925-171.214 315.029 1.00 68.49 O ANISOU 662 OD1 ASN A 187 9006 6032 10984 -1312 -430 1108 O ATOM 663 ND2 ASN A 187 -55.024-171.208 316.992 1.00 74.45 N ANISOU 663 ND2 ASN A 187 9720 7074 11496 -1503 -380 1607 N ATOM 664 N VAL A 188 -49.685-169.469 317.414 1.00 66.16 N ANISOU 664 N VAL A 188 8812 6038 10288 -588 -686 1629 N ATOM 665 CA VAL A 188 -48.768-168.419 317.856 1.00 63.39 C ANISOU 665 CA VAL A 188 8441 5941 9703 -420 -747 1624 C ATOM 666 C VAL A 188 -47.847-167.997 316.715 1.00 62.41 C ANISOU 666 C VAL A 188 8315 5737 9661 -278 -763 1318 C ATOM 667 O VAL A 188 -47.555-166.807 316.541 1.00 59.97 O ANISOU 667 O VAL A 188 7981 5669 9136 -207 -768 1162 O ATOM 668 CB VAL A 188 -47.970-168.889 319.080 1.00 65.17 C ANISOU 668 CB VAL A 188 8674 6156 9933 -330 -826 1976 C ATOM 669 CG1 VAL A 188 -46.921-167.855 319.465 1.00 64.51 C ANISOU 669 CG1 VAL A 188 8551 6326 9632 -162 -898 1929 C ATOM 670 CG2 VAL A 188 -48.906-169.159 320.250 1.00 66.52 C ANISOU 670 CG2 VAL A 188 8839 6483 9954 -481 -799 2292 C ATOM 671 N PHE A 189 -47.376-168.960 315.919 1.00 63.87 N ANISOU 671 N PHE A 189 8521 5581 10164 -240 -762 1224 N ATOM 672 CA PHE A 189 -46.527-168.621 314.782 1.00 61.83 C ANISOU 672 CA PHE A 189 8248 5269 9976 -117 -760 923 C ATOM 673 C PHE A 189 -47.283-167.782 313.760 1.00 64.12 C ANISOU 673 C PHE A 189 8524 5733 10107 -195 -696 630 C ATOM 674 O PHE A 189 -46.739-166.813 313.217 1.00 62.63 O ANISOU 674 O PHE A 189 8314 5703 9778 -105 -695 452 O ATOM 675 CB PHE A 189 -45.983-169.892 314.132 1.00 60.26 C ANISOU 675 CB PHE A 189 8065 4674 10159 -66 -760 854 C ATOM 676 CG PHE A 189 -45.277-169.647 312.831 1.00 58.37 C ANISOU 676 CG PHE A 189 7796 4394 9986 32 -735 507 C ATOM 677 CD1 PHE A 189 -43.941-169.289 312.812 1.00 56.89 C ANISOU 677 CD1 PHE A 189 7569 4249 9797 217 -778 473 C ATOM 678 CD2 PHE A 189 -45.952-169.766 311.627 1.00 58.95 C ANISOU 678 CD2 PHE A 189 7866 4424 10107 -69 -666 212 C ATOM 679 CE1 PHE A 189 -43.291-169.055 311.619 1.00 57.66 C ANISOU 679 CE1 PHE A 189 7628 4340 9939 295 -740 161 C ATOM 680 CE2 PHE A 189 -45.308-169.531 310.431 1.00 57.38 C ANISOU 680 CE2 PHE A 189 7634 4233 9934 15 -636 -98 C ATOM 681 CZ PHE A 189 -43.975-169.176 310.427 1.00 57.97 C ANISOU 681 CZ PHE A 189 7674 4345 10008 195 -667 -119 C ATOM 682 N LEU A 190 -48.533-168.154 313.469 1.00 67.15 N ANISOU 682 N LEU A 190 8909 6090 10516 -364 -644 584 N ATOM 683 CA LEU A 190 -49.350-167.354 312.561 1.00 66.95 C ANISOU 683 CA LEU A 190 8855 6266 10318 -431 -597 336 C ATOM 684 C LEU A 190 -49.552-165.947 313.102 1.00 68.73 C ANISOU 684 C LEU A 190 9063 6835 10217 -393 -604 381 C ATOM 685 O LEU A 190 -49.593-164.977 312.336 1.00 65.54 O ANISOU 685 O LEU A 190 8643 6593 9664 -349 -586 186 O ATOM 686 CB LEU A 190 -50.698-168.036 312.332 1.00 65.43 C ANISOU 686 CB LEU A 190 8642 6015 10204 -629 -551 305 C ATOM 687 CG LEU A 190 -50.661-169.327 311.519 1.00 64.97 C ANISOU 687 CG LEU A 190 8592 5615 10478 -693 -530 159 C ATOM 688 CD1 LEU A 190 -52.014-170.017 311.564 1.00 65.06 C ANISOU 688 CD1 LEU A 190 8574 5574 10572 -921 -486 175 C ATOM 689 CD2 LEU A 190 -50.263-169.025 310.086 1.00 62.31 C ANISOU 689 CD2 LEU A 190 8233 5303 10138 -622 -515 -192 C ATOM 690 N PHE A 191 -49.686-165.821 314.424 1.00 73.86 N ANISOU 690 N PHE A 191 9712 7599 10752 -408 -627 637 N ATOM 691 CA PHE A 191 -49.798-164.507 315.049 1.00 73.24 C ANISOU 691 CA PHE A 191 9613 7835 10382 -364 -633 659 C ATOM 692 C PHE A 191 -48.583-163.648 314.727 1.00 66.46 C ANISOU 692 C PHE A 191 8761 7022 9469 -208 -664 540 C ATOM 693 O PHE A 191 -48.716-162.522 314.230 1.00 65.92 O ANISOU 693 O PHE A 191 8683 7115 9248 -175 -641 380 O ATOM 694 CB PHE A 191 -49.961-164.676 316.561 1.00 81.09 C ANISOU 694 CB PHE A 191 10596 8945 11268 -401 -656 950 C ATOM 695 CG PHE A 191 -50.553-163.482 317.250 1.00 85.95 C ANISOU 695 CG PHE A 191 11173 9900 11584 -409 -639 946 C ATOM 696 CD1 PHE A 191 -51.906-163.217 317.156 1.00 88.55 C ANISOU 696 CD1 PHE A 191 11461 10377 11807 -522 -578 890 C ATOM 697 CD2 PHE A 191 -49.763-162.640 318.013 1.00 86.71 C ANISOU 697 CD2 PHE A 191 11261 10171 11515 -305 -682 981 C ATOM 698 CE1 PHE A 191 -52.462-162.128 317.792 1.00 89.00 C ANISOU 698 CE1 PHE A 191 11472 10737 11608 -511 -556 866 C ATOM 699 CE2 PHE A 191 -50.314-161.547 318.656 1.00 86.66 C ANISOU 699 CE2 PHE A 191 11215 10460 11252 -310 -660 942 C ATOM 700 CZ PHE A 191 -51.666-161.292 318.545 1.00 87.93 C ANISOU 700 CZ PHE A 191 11339 10752 11320 -405 -595 885 C ATOM 701 N LYS A 192 -47.383-164.171 314.995 1.00 59.31 N ANISOU 701 N LYS A 192 7864 5972 8701 -111 -715 626 N ATOM 702 CA LYS A 192 -46.162-163.431 314.693 1.00 55.27 C ANISOU 702 CA LYS A 192 7338 5506 8157 22 -741 510 C ATOM 703 C LYS A 192 -46.047-163.143 313.202 1.00 54.60 C ANISOU 703 C LYS A 192 7257 5364 8126 40 -690 241 C ATOM 704 O LYS A 192 -45.679-162.032 312.804 1.00 56.39 O ANISOU 704 O LYS A 192 7474 5729 8221 89 -672 115 O ATOM 705 CB LYS A 192 -44.943-164.209 315.186 1.00 55.86 C ANISOU 705 CB LYS A 192 7396 5431 8396 128 -809 647 C ATOM 706 CG LYS A 192 -44.932-164.445 316.686 1.00 56.34 C ANISOU 706 CG LYS A 192 7446 5594 8367 126 -872 940 C ATOM 707 CD LYS A 192 -43.796-165.368 317.098 1.00 54.57 C ANISOU 707 CD LYS A 192 7201 5200 8335 246 -950 1103 C ATOM 708 CE LYS A 192 -43.758-165.550 318.608 1.00 54.45 C ANISOU 708 CE LYS A 192 7167 5335 8186 251 -1023 1422 C ATOM 709 NZ LYS A 192 -42.588-166.358 319.047 1.00 56.26 N ANISOU 709 NZ LYS A 192 7361 5430 8584 397 -1117 1603 N ATOM 710 N LEU A 193 -46.359-164.132 312.362 1.00 54.48 N ANISOU 710 N LEU A 193 7251 5149 8302 -6 -662 149 N ATOM 711 CA LEU A 193 -46.388-163.882 310.927 1.00 54.41 C ANISOU 711 CA LEU A 193 7235 5139 8300 -3 -611 -113 C ATOM 712 C LEU A 193 -47.415-162.816 310.575 1.00 56.33 C ANISOU 712 C LEU A 193 7477 5611 8313 -63 -576 -189 C ATOM 713 O LEU A 193 -47.193-162.019 309.657 1.00 55.64 O ANISOU 713 O LEU A 193 7386 5623 8130 -21 -545 -345 O ATOM 714 CB LEU A 193 -46.685-165.176 310.170 1.00 52.20 C ANISOU 714 CB LEU A 193 6955 4622 8256 -62 -588 -223 C ATOM 715 CG LEU A 193 -46.429-165.129 308.664 1.00 52.67 C ANISOU 715 CG LEU A 193 6992 4678 8340 -40 -541 -514 C ATOM 716 CD1 LEU A 193 -44.947-164.927 308.387 1.00 52.91 C ANISOU 716 CD1 LEU A 193 7000 4680 8425 104 -542 -580 C ATOM 717 CD2 LEU A 193 -46.940-166.389 307.988 1.00 56.19 C ANISOU 717 CD2 LEU A 193 7431 4914 9006 -126 -518 -657 C ATOM 718 N GLY A 194 -48.531-162.775 311.306 1.00 59.77 N ANISOU 718 N GLY A 194 7911 6141 8658 -154 -577 -69 N ATOM 719 CA GLY A 194 -49.567-161.800 311.008 1.00 60.99 C ANISOU 719 CA GLY A 194 8049 6512 8613 -190 -549 -140 C ATOM 720 C GLY A 194 -49.099-160.371 311.195 1.00 63.60 C ANISOU 720 C GLY A 194 8390 7007 8769 -95 -549 -152 C ATOM 721 O GLY A 194 -49.389-159.499 310.371 1.00 65.98 O ANISOU 721 O GLY A 194 8689 7416 8963 -67 -521 -270 O ATOM 722 N GLY A 195 -48.373-160.108 312.284 1.00 61.23 N ANISOU 722 N GLY A 195 8095 6729 8440 -47 -582 -26 N ATOM 723 CA GLY A 195 -47.845-158.771 312.497 1.00 57.42 C ANISOU 723 CA GLY A 195 7618 6377 7823 28 -580 -62 C ATOM 724 C GLY A 195 -46.929-158.329 311.375 1.00 56.10 C ANISOU 724 C GLY A 195 7462 6155 7698 92 -555 -203 C ATOM 725 O GLY A 195 -47.048-157.215 310.858 1.00 53.15 O ANISOU 725 O GLY A 195 7101 5872 7221 119 -522 -281 O ATOM 726 N VAL A 196 -46.004-159.204 310.970 1.00 58.40 N ANISOU 726 N VAL A 196 7745 6296 8150 119 -565 -232 N ATOM 727 CA VAL A 196 -45.081-158.874 309.889 1.00 56.90 C ANISOU 727 CA VAL A 196 7548 6078 7994 172 -529 -372 C ATOM 728 C VAL A 196 -45.844-158.613 308.597 1.00 59.05 C ANISOU 728 C VAL A 196 7832 6406 8198 142 -477 -500 C ATOM 729 O VAL A 196 -45.559-157.652 307.872 1.00 61.13 O ANISOU 729 O VAL A 196 8104 6753 8371 171 -436 -567 O ATOM 730 CB VAL A 196 -44.041-159.995 309.712 1.00 52.70 C ANISOU 730 CB VAL A 196 6984 5378 7660 217 -546 -397 C ATOM 731 CG1 VAL A 196 -43.072-159.649 308.596 1.00 51.42 C ANISOU 731 CG1 VAL A 196 6795 5224 7517 266 -495 -554 C ATOM 732 CG2 VAL A 196 -43.301-160.234 311.012 1.00 48.59 C ANISOU 732 CG2 VAL A 196 6440 4834 7189 263 -614 -242 C ATOM 733 N THR A 197 -46.832-159.456 308.296 1.00 59.88 N ANISOU 733 N THR A 197 7932 6477 8343 76 -480 -527 N ATOM 734 CA THR A 197 -47.583-159.294 307.057 1.00 61.41 C ANISOU 734 CA THR A 197 8117 6760 8455 47 -445 -659 C ATOM 735 C THR A 197 -48.378-157.995 307.061 1.00 60.21 C ANISOU 735 C THR A 197 7978 6789 8112 62 -436 -618 C ATOM 736 O THR A 197 -48.389-157.269 306.063 1.00 58.71 O ANISOU 736 O THR A 197 7791 6697 7818 95 -405 -685 O ATOM 737 CB THR A 197 -48.504-160.493 306.840 1.00 62.93 C ANISOU 737 CB THR A 197 8285 6885 8742 -46 -456 -713 C ATOM 738 OG1 THR A 197 -47.768-161.702 307.060 1.00 65.25 O ANISOU 738 OG1 THR A 197 8577 6960 9257 -48 -467 -721 O ATOM 739 CG2 THR A 197 -49.038-160.495 305.421 1.00 62.54 C ANISOU 739 CG2 THR A 197 8205 6941 8615 -73 -428 -894 C ATOM 740 N ALA A 198 -49.027-157.672 308.183 1.00 61.48 N ANISOU 740 N ALA A 198 8139 6998 8221 47 -460 -502 N ATOM 741 CA ALA A 198 -49.819-156.447 308.246 1.00 61.19 C ANISOU 741 CA ALA A 198 8105 7115 8029 81 -451 -477 C ATOM 742 C ALA A 198 -48.942-155.209 308.107 1.00 62.82 C ANISOU 742 C ALA A 198 8351 7330 8188 160 -425 -476 C ATOM 743 O ALA A 198 -49.294-154.269 307.384 1.00 64.38 O ANISOU 743 O ALA A 198 8561 7606 8293 205 -401 -494 O ATOM 744 CB ALA A 198 -50.610-156.400 309.553 1.00 55.92 C ANISOU 744 CB ALA A 198 7416 6510 7319 51 -471 -377 C ATOM 745 N SER A 199 -47.791-155.194 308.782 1.00 60.24 N ANISOU 745 N SER A 199 8035 6920 7931 174 -433 -446 N ATOM 746 CA SER A 199 -46.937-154.011 308.768 1.00 58.78 C ANISOU 746 CA SER A 199 7877 6737 7722 222 -405 -453 C ATOM 747 C SER A 199 -46.326-153.783 307.392 1.00 60.28 C ANISOU 747 C SER A 199 8077 6914 7912 238 -355 -519 C ATOM 748 O SER A 199 -46.334-152.659 306.876 1.00 61.59 O ANISOU 748 O SER A 199 8272 7116 8012 267 -315 -509 O ATOM 749 CB SER A 199 -45.838-154.148 309.818 1.00 60.23 C ANISOU 749 CB SER A 199 8043 6868 7974 222 -434 -422 C ATOM 750 OG SER A 199 -46.322-154.766 310.995 1.00 64.57 O ANISOU 750 OG SER A 199 8574 7443 8518 197 -484 -343 O ATOM 751 N PHE A 200 -45.777-154.837 306.785 1.00 61.18 N ANISOU 751 N PHE A 200 8165 6976 8106 220 -350 -584 N ATOM 752 CA PHE A 200 -45.142-154.674 305.483 1.00 60.94 C ANISOU 752 CA PHE A 200 8128 6973 8054 231 -292 -661 C ATOM 753 C PHE A 200 -46.168-154.469 304.379 1.00 58.51 C ANISOU 753 C PHE A 200 7829 6786 7619 230 -274 -689 C ATOM 754 O PHE A 200 -45.893-153.753 303.410 1.00 58.34 O ANISOU 754 O PHE A 200 7819 6840 7508 248 -222 -690 O ATOM 755 CB PHE A 200 -44.242-155.871 305.183 1.00 65.49 C ANISOU 755 CB PHE A 200 8657 7467 8758 226 -287 -756 C ATOM 756 CG PHE A 200 -42.914-155.804 305.876 1.00 70.79 C ANISOU 756 CG PHE A 200 9300 8067 9532 251 -292 -737 C ATOM 757 CD1 PHE A 200 -41.917-154.968 305.402 1.00 74.36 C ANISOU 757 CD1 PHE A 200 9735 8559 9959 257 -231 -761 C ATOM 758 CD2 PHE A 200 -42.664-156.561 307.008 1.00 73.82 C ANISOU 758 CD2 PHE A 200 9662 8359 10028 263 -357 -682 C ATOM 759 CE1 PHE A 200 -40.693-154.895 306.037 1.00 76.18 C ANISOU 759 CE1 PHE A 200 9915 8750 10281 272 -240 -759 C ATOM 760 CE2 PHE A 200 -41.441-156.493 307.648 1.00 76.61 C ANISOU 760 CE2 PHE A 200 9968 8681 10458 296 -376 -664 C ATOM 761 CZ PHE A 200 -40.454-155.659 307.162 1.00 77.00 C ANISOU 761 CZ PHE A 200 9987 8781 10487 299 -319 -717 C ATOM 762 N THR A 201 -47.352-155.074 304.503 1.00 58.02 N ANISOU 762 N THR A 201 7750 6760 7536 204 -316 -699 N ATOM 763 CA THR A 201 -48.428-154.749 303.572 1.00 59.65 C ANISOU 763 CA THR A 201 7944 7119 7600 211 -316 -716 C ATOM 764 C THR A 201 -48.872-153.302 303.744 1.00 57.03 C ANISOU 764 C THR A 201 7650 6849 7169 277 -310 -600 C ATOM 765 O THR A 201 -49.195-152.625 302.762 1.00 53.05 O ANISOU 765 O THR A 201 7153 6460 6544 318 -291 -573 O ATOM 766 CB THR A 201 -49.610-155.701 303.765 1.00 62.47 C ANISOU 766 CB THR A 201 8255 7510 7972 154 -364 -763 C ATOM 767 OG1 THR A 201 -49.176-157.049 303.545 1.00 63.64 O ANISOU 767 OG1 THR A 201 8376 7557 8249 93 -364 -880 O ATOM 768 CG2 THR A 201 -50.734-155.376 302.796 1.00 65.87 C ANISOU 768 CG2 THR A 201 8647 8137 8244 165 -378 -793 C ATOM 769 N ALA A 202 -48.883-152.807 304.983 1.00 60.19 N ANISOU 769 N ALA A 202 8072 7176 7620 292 -325 -530 N ATOM 770 CA ALA A 202 -49.174-151.396 305.207 1.00 63.28 C ANISOU 770 CA ALA A 202 8502 7582 7960 361 -310 -447 C ATOM 771 C ALA A 202 -48.106-150.504 304.592 1.00 65.84 C ANISOU 771 C ALA A 202 8874 7851 8291 381 -250 -414 C ATOM 772 O ALA A 202 -48.414-149.408 304.110 1.00 69.11 O ANISOU 772 O ALA A 202 9324 8287 8649 440 -226 -336 O ATOM 773 CB ALA A 202 -49.304-151.114 306.704 1.00 62.27 C ANISOU 773 CB ALA A 202 8377 7400 7884 363 -333 -424 C ATOM 774 N SER A 203 -46.850-150.961 304.590 1.00 62.25 N ANISOU 774 N SER A 203 8412 7325 7914 333 -224 -461 N ATOM 775 CA SER A 203 -45.763-150.148 304.054 1.00 58.97 C ANISOU 775 CA SER A 203 8024 6868 7512 326 -155 -433 C ATOM 776 C SER A 203 -45.926-149.916 302.556 1.00 58.77 C ANISOU 776 C SER A 203 8006 6958 7365 342 -109 -400 C ATOM 777 O SER A 203 -45.739-148.795 302.070 1.00 60.29 O ANISOU 777 O SER A 203 8244 7143 7522 362 -57 -298 O ATOM 778 CB SER A 203 -44.418-150.811 304.353 1.00 61.51 C ANISOU 778 CB SER A 203 8307 7125 7940 277 -140 -507 C ATOM 779 OG SER A 203 -43.346-150.065 303.802 1.00 64.85 O ANISOU 779 OG SER A 203 8734 7530 8376 252 -63 -490 O ATOM 780 N VAL A 204 -46.272-150.965 301.806 1.00 60.92 N ANISOU 780 N VAL A 204 8233 7343 7572 327 -126 -485 N ATOM 781 CA VAL A 204 -46.451-150.800 300.367 1.00 64.07 C ANISOU 781 CA VAL A 204 8623 7907 7814 339 -89 -469 C ATOM 782 C VAL A 204 -47.752-150.062 300.071 1.00 64.14 C ANISOU 782 C VAL A 204 8652 8018 7701 411 -128 -356 C ATOM 783 O VAL A 204 -47.846-149.326 299.081 1.00 65.33 O ANISOU 783 O VAL A 204 8822 8279 7722 449 -95 -249 O ATOM 784 CB VAL A 204 -46.378-152.169 299.660 1.00 66.06 C ANISOU 784 CB VAL A 204 8806 8258 8036 296 -94 -640 C ATOM 785 CG1 VAL A 204 -47.203-153.203 300.400 1.00 68.48 C ANISOU 785 CG1 VAL A 204 9081 8515 8424 276 -172 -727 C ATOM 786 CG2 VAL A 204 -46.836-152.063 298.213 1.00 66.46 C ANISOU 786 CG2 VAL A 204 8831 8544 7878 309 -75 -645 C ATOM 787 N GLY A 205 -48.764-150.223 300.926 1.00 63.85 N ANISOU 787 N GLY A 205 8602 7957 7701 437 -197 -364 N ATOM 788 CA GLY A 205 -49.984-149.448 300.763 1.00 65.27 C ANISOU 788 CA GLY A 205 8782 8229 7787 526 -236 -261 C ATOM 789 C GLY A 205 -49.752-147.959 300.937 1.00 66.54 C ANISOU 789 C GLY A 205 9020 8277 7986 599 -196 -105 C ATOM 790 O GLY A 205 -50.356-147.141 300.239 1.00 70.77 O ANISOU 790 O GLY A 205 9571 8893 8427 688 -201 25 O ATOM 791 N SER A 206 -48.870-147.588 301.869 1.00 61.89 N ANISOU 791 N SER A 206 8474 7497 7544 563 -160 -116 N ATOM 792 CA SER A 206 -48.511-146.182 302.028 1.00 58.52 C ANISOU 792 CA SER A 206 8121 6925 7190 606 -110 3 C ATOM 793 C SER A 206 -47.819-145.654 300.778 1.00 61.43 C ANISOU 793 C SER A 206 8526 7326 7490 591 -37 122 C ATOM 794 O SER A 206 -48.157-144.576 300.274 1.00 64.36 O ANISOU 794 O SER A 206 8948 7669 7836 667 -15 287 O ATOM 795 CB SER A 206 -47.623-146.002 303.260 1.00 55.50 C ANISOU 795 CB SER A 206 7755 6363 6968 544 -90 -73 C ATOM 796 OG SER A 206 -48.315-146.364 304.441 1.00 53.90 O ANISOU 796 OG SER A 206 7520 6158 6801 562 -151 -156 O ATOM 797 N LEU A 207 -46.841-146.405 300.262 1.00 61.55 N ANISOU 797 N LEU A 207 8510 7401 7475 498 6 47 N ATOM 798 CA LEU A 207 -46.240-146.049 298.981 1.00 64.16 C ANISOU 798 CA LEU A 207 8854 7829 7696 473 84 151 C ATOM 799 C LEU A 207 -47.282-146.028 297.873 1.00 66.95 C ANISOU 799 C LEU A 207 9192 8405 7842 554 48 247 C ATOM 800 O LEU A 207 -47.192-145.212 296.948 1.00 69.36 O ANISOU 800 O LEU A 207 9535 8773 8046 582 98 431 O ATOM 801 CB LEU A 207 -45.119-147.028 298.633 1.00 64.22 C ANISOU 801 CB LEU A 207 8801 7904 7696 373 134 8 C ATOM 802 CG LEU A 207 -43.957-147.132 299.622 1.00 64.48 C ANISOU 802 CG LEU A 207 8822 7760 7916 298 164 -87 C ATOM 803 CD1 LEU A 207 -43.039-148.284 299.245 1.00 65.67 C ANISOU 803 CD1 LEU A 207 8890 8000 8061 236 194 -246 C ATOM 804 CD2 LEU A 207 -43.184-145.825 299.689 1.00 64.14 C ANISOU 804 CD2 LEU A 207 8834 7577 7961 256 248 42 C ATOM 805 N PHE A 208 -48.282-146.908 297.960 1.00 65.33 N ANISOU 805 N PHE A 208 8924 8331 7568 585 -41 134 N ATOM 806 CA PHE A 208 -49.338-146.949 296.955 1.00 66.35 C ANISOU 806 CA PHE A 208 9010 8709 7489 659 -95 197 C ATOM 807 C PHE A 208 -50.184-145.681 296.982 1.00 68.22 C ANISOU 807 C PHE A 208 9296 8906 7721 795 -124 414 C ATOM 808 O PHE A 208 -50.502-145.118 295.928 1.00 69.91 O ANISOU 808 O PHE A 208 9514 9279 7770 866 -124 588 O ATOM 809 CB PHE A 208 -50.206-148.189 297.174 1.00 62.61 C ANISOU 809 CB PHE A 208 8446 8361 6982 638 -181 3 C ATOM 810 CG PHE A 208 -51.439-148.230 296.324 1.00 62.13 C ANISOU 810 CG PHE A 208 8316 8571 6719 712 -256 39 C ATOM 811 CD1 PHE A 208 -51.359-148.543 294.978 1.00 62.72 C ANISOU 811 CD1 PHE A 208 8343 8915 6572 694 -247 24 C ATOM 812 CD2 PHE A 208 -52.683-147.973 296.874 1.00 59.69 C ANISOU 812 CD2 PHE A 208 7971 8279 6427 801 -338 72 C ATOM 813 CE1 PHE A 208 -52.497-148.587 294.194 1.00 62.64 C ANISOU 813 CE1 PHE A 208 8252 9194 6356 761 -330 49 C ATOM 814 CE2 PHE A 208 -53.824-148.017 296.096 1.00 58.38 C ANISOU 814 CE2 PHE A 208 7717 8390 6074 873 -417 99 C ATOM 815 CZ PHE A 208 -53.731-148.324 294.753 1.00 60.23 C ANISOU 815 CZ PHE A 208 7905 8898 6082 853 -419 90 C ATOM 816 N LEU A 209 -50.551-145.211 298.178 1.00 67.66 N ANISOU 816 N LEU A 209 9254 8631 7825 844 -149 407 N ATOM 817 CA LEU A 209 -51.389-144.020 298.276 1.00 68.53 C ANISOU 817 CA LEU A 209 9399 8674 7964 994 -176 584 C ATOM 818 C LEU A 209 -50.629-142.768 297.856 1.00 69.36 C ANISOU 818 C LEU A 209 9609 8611 8135 1013 -90 799 C ATOM 819 O LEU A 209 -51.189-141.895 297.182 1.00 69.70 O ANISOU 819 O LEU A 209 9680 8688 8115 1139 -102 1017 O ATOM 820 CB LEU A 209 -51.932-143.871 299.698 1.00 63.91 C ANISOU 820 CB LEU A 209 8807 7928 7549 1035 -212 482 C ATOM 821 CG LEU A 209 -53.096-144.790 300.073 1.00 57.39 C ANISOU 821 CG LEU A 209 7870 7281 6654 1054 -302 344 C ATOM 822 CD1 LEU A 209 -53.618-144.476 301.470 1.00 54.94 C ANISOU 822 CD1 LEU A 209 7549 6835 6491 1100 -319 268 C ATOM 823 CD2 LEU A 209 -54.208-144.679 299.042 1.00 56.13 C ANISOU 823 CD2 LEU A 209 7641 7376 6312 1171 -371 447 C ATOM 824 N ALA A 210 -49.356-142.659 298.246 1.00 66.69 N ANISOU 824 N ALA A 210 9322 8088 7929 889 -2 751 N ATOM 825 CA ALA A 210 -48.543-141.534 297.795 1.00 64.84 C ANISOU 825 CA ALA A 210 9179 7693 7765 866 96 950 C ATOM 826 C ALA A 210 -48.448-141.505 296.276 1.00 68.58 C ANISOU 826 C ALA A 210 9648 8401 8009 870 128 1136 C ATOM 827 O ALA A 210 -48.536-140.436 295.661 1.00 73.77 O ANISOU 827 O ALA A 210 10373 9000 8657 938 165 1403 O ATOM 828 CB ALA A 210 -47.150-141.603 298.415 1.00 62.07 C ANISOU 828 CB ALA A 210 8847 7164 7571 707 181 831 C ATOM 829 N ALA A 211 -48.272-142.674 295.655 1.00 67.89 N ANISOU 829 N ALA A 211 9478 8584 7733 798 117 1000 N ATOM 830 CA ALA A 211 -48.229-142.737 294.199 1.00 69.88 C ANISOU 830 CA ALA A 211 9705 9124 7722 799 144 1141 C ATOM 831 C ALA A 211 -49.524-142.217 293.587 1.00 70.09 C ANISOU 831 C ALA A 211 9724 9311 7596 970 55 1341 C ATOM 832 O ALA A 211 -49.497-141.498 292.581 1.00 69.67 O ANISOU 832 O ALA A 211 9706 9368 7398 1017 90 1611 O ATOM 833 CB ALA A 211 -47.953-144.170 293.744 1.00 69.15 C ANISOU 833 CB ALA A 211 9510 9292 7471 704 135 891 C ATOM 834 N ILE A 212 -50.667-142.562 294.187 1.00 69.95 N ANISOU 834 N ILE A 212 9651 9322 7605 1068 -60 1227 N ATOM 835 CA ILE A 212 -51.949-142.059 293.697 1.00 74.13 C ANISOU 835 CA ILE A 212 10147 10011 8007 1250 -157 1404 C ATOM 836 C ILE A 212 -51.991-140.541 293.782 1.00 76.96 C ANISOU 836 C ILE A 212 10617 10110 8515 1374 -122 1705 C ATOM 837 O ILE A 212 -52.432-139.861 292.846 1.00 79.42 O ANISOU 837 O ILE A 212 10940 10554 8682 1497 -146 1986 O ATOM 838 CB ILE A 212 -53.113-142.694 294.481 1.00 74.53 C ANISOU 838 CB ILE A 212 10103 10119 8096 1314 -272 1202 C ATOM 839 CG1 ILE A 212 -53.184-144.198 294.225 1.00 75.15 C ANISOU 839 CG1 ILE A 212 10070 10456 8026 1191 -311 930 C ATOM 840 CG2 ILE A 212 -54.431-142.028 294.112 1.00 76.26 C ANISOU 840 CG2 ILE A 212 10274 10476 8225 1523 -373 1387 C ATOM 841 CD1 ILE A 212 -54.444-144.841 294.745 1.00 74.80 C ANISOU 841 CD1 ILE A 212 9912 10531 7976 1238 -423 767 C ATOM 842 N ASP A 213 -51.538-139.988 294.909 1.00 75.45 N ANISOU 842 N ASP A 213 10504 9545 8620 1347 -69 1651 N ATOM 843 CA ASP A 213 -51.514-138.541 295.088 1.00 77.14 C ANISOU 843 CA ASP A 213 10829 9448 9034 1449 -24 1896 C ATOM 844 C ASP A 213 -50.731-137.862 293.970 1.00 77.74 C ANISOU 844 C ASP A 213 10984 9529 9025 1402 73 2199 C ATOM 845 O ASP A 213 -51.217-136.915 293.342 1.00 77.20 O ANISOU 845 O ASP A 213 10965 9435 8933 1550 60 2514 O ATOM 846 CB ASP A 213 -50.921-138.210 296.460 1.00 76.53 C ANISOU 846 CB ASP A 213 10810 8998 9271 1372 33 1720 C ATOM 847 CG ASP A 213 -50.858-136.720 296.734 1.00 80.03 C ANISOU 847 CG ASP A 213 11367 9072 9968 1461 88 1919 C ATOM 848 OD1 ASP A 213 -51.510-135.947 296.009 1.00 84.18 O ANISOU 848 OD1 ASP A 213 11924 9606 10454 1628 61 2201 O ATOM 849 OD2 ASP A 213 -50.160-136.319 297.689 1.00 79.15 O ANISOU 849 OD2 ASP A 213 11310 8658 10105 1368 155 1789 O ATOM 850 N ARG A 214 -49.519-138.348 293.694 1.00 78.66 N ANISOU 850 N ARG A 214 11105 9693 9089 1200 173 2119 N ATOM 851 CA ARG A 214 -48.700-137.733 292.654 1.00 81.76 C ANISOU 851 CA ARG A 214 11561 10114 9390 1126 286 2402 C ATOM 852 C ARG A 214 -49.293-137.953 291.268 1.00 81.23 C ANISOU 852 C ARG A 214 11438 10468 8959 1213 235 2603 C ATOM 853 O ARG A 214 -49.291-137.037 290.438 1.00 84.48 O ANISOU 853 O ARG A 214 11914 10886 9297 1274 276 2969 O ATOM 854 CB ARG A 214 -47.274-138.273 292.715 1.00 85.72 C ANISOU 854 CB ARG A 214 12048 10607 9915 892 407 2233 C ATOM 855 CG ARG A 214 -46.385-137.525 293.684 1.00 91.59 C ANISOU 855 CG ARG A 214 12872 10928 10999 786 501 2197 C ATOM 856 CD ARG A 214 -44.924-137.698 293.323 1.00 96.74 C ANISOU 856 CD ARG A 214 13510 11610 11636 567 645 2171 C ATOM 857 NE ARG A 214 -44.085-136.706 293.987 1.00100.05 N ANISOU 857 NE ARG A 214 14009 11639 12368 458 747 2219 N ATOM 858 CZ ARG A 214 -43.840-135.493 293.502 1.00102.20 C ANISOU 858 CZ ARG A 214 14381 11715 12737 439 842 2543 C ATOM 859 NH1 ARG A 214 -44.369-135.119 292.345 1.00104.14 N ANISOU 859 NH1 ARG A 214 14660 12138 12772 537 843 2878 N ATOM 860 NH2 ARG A 214 -43.065-134.653 294.174 1.00102.53 N ANISOU 860 NH2 ARG A 214 14483 11386 13088 317 936 2538 N ATOM 861 N TYR A 215 -49.793-139.161 290.993 1.00 79.10 N ANISOU 861 N TYR A 215 11044 10556 8456 1212 147 2372 N ATOM 862 CA TYR A 215 -50.384-139.435 289.686 1.00 79.92 C ANISOU 862 CA TYR A 215 11071 11108 8186 1285 86 2515 C ATOM 863 C TYR A 215 -51.544-138.494 289.399 1.00 83.73 C ANISOU 863 C TYR A 215 11574 11601 8639 1523 -14 2828 C ATOM 864 O TYR A 215 -51.657-137.953 288.293 1.00 87.75 O ANISOU 864 O TYR A 215 12096 12321 8924 1593 -10 3160 O ATOM 865 CB TYR A 215 -50.845-140.892 289.608 1.00 76.95 C ANISOU 865 CB TYR A 215 10551 11065 7623 1242 -4 2159 C ATOM 866 CG TYR A 215 -51.639-141.229 288.360 1.00 76.58 C ANISOU 866 CG TYR A 215 10397 11512 7186 1325 -95 2243 C ATOM 867 CD1 TYR A 215 -50.998-141.518 287.160 1.00 76.26 C ANISOU 867 CD1 TYR A 215 10322 11813 6841 1228 -23 2298 C ATOM 868 CD2 TYR A 215 -53.029-141.266 288.384 1.00 75.46 C ANISOU 868 CD2 TYR A 215 10174 11530 6969 1497 -252 2252 C ATOM 869 CE1 TYR A 215 -51.719-141.829 286.020 1.00 78.30 C ANISOU 869 CE1 TYR A 215 10471 12566 6715 1299 -112 2356 C ATOM 870 CE2 TYR A 215 -53.757-141.575 287.248 1.00 76.75 C ANISOU 870 CE2 TYR A 215 10220 12178 6762 1569 -348 2314 C ATOM 871 CZ TYR A 215 -53.098-141.856 286.070 1.00 78.78 C ANISOU 871 CZ TYR A 215 10449 12777 6707 1469 -280 2363 C ATOM 872 OH TYR A 215 -53.820-142.165 284.940 1.00 80.90 O ANISOU 872 OH TYR A 215 10590 13568 6580 1536 -381 2407 O ATOM 873 N ILE A 216 -52.412-138.277 290.389 1.00 84.83 N ANISOU 873 N ILE A 216 11708 11525 8999 1658 -104 2737 N ATOM 874 CA ILE A 216 -53.554-137.388 290.200 1.00 89.24 C ANISOU 874 CA ILE A 216 12267 12077 9565 1912 -205 3011 C ATOM 875 C ILE A 216 -53.085-135.957 289.972 1.00 93.62 C ANISOU 875 C ILE A 216 12976 12304 10293 1973 -112 3411 C ATOM 876 O ILE A 216 -53.671-135.217 289.171 1.00 97.40 O ANISOU 876 O ILE A 216 13467 12887 10653 2153 -164 3775 O ATOM 877 CB ILE A 216 -54.513-137.495 291.399 1.00 87.21 C ANISOU 877 CB ILE A 216 11955 11656 9525 2030 -301 2784 C ATOM 878 CG1 ILE A 216 -55.163-138.880 291.430 1.00 84.82 C ANISOU 878 CG1 ILE A 216 11489 11720 9020 1980 -403 2454 C ATOM 879 CG2 ILE A 216 -55.573-136.406 291.348 1.00 88.99 C ANISOU 879 CG2 ILE A 216 12188 11787 9836 2312 -385 3063 C ATOM 880 CD1 ILE A 216 -56.236-139.028 292.484 1.00 82.74 C ANISOU 880 CD1 ILE A 216 11143 11378 8915 2095 -498 2260 C ATOM 881 N SER A 217 -52.012-135.548 290.657 1.00 92.51 N ANISOU 881 N SER A 217 12948 11764 10437 1820 24 3358 N ATOM 882 CA SER A 217 -51.487-134.198 290.473 1.00 94.83 C ANISOU 882 CA SER A 217 13391 11704 10937 1839 129 3719 C ATOM 883 C SER A 217 -51.097-133.949 289.021 1.00 98.96 C ANISOU 883 C SER A 217 13936 12504 11161 1805 186 4094 C ATOM 884 O SER A 217 -51.388-132.883 288.466 1.00103.58 O ANISOU 884 O SER A 217 14601 12978 11776 1949 189 4517 O ATOM 885 CB SER A 217 -50.288-133.970 291.394 1.00 93.64 C ANISOU 885 CB SER A 217 13328 11146 11106 1628 270 3543 C ATOM 886 OG SER A 217 -49.170-134.732 290.974 1.00 94.78 O ANISOU 886 OG SER A 217 13439 11491 11082 1386 368 3422 O ATOM 887 N ILE A 218 -50.446-134.923 288.387 1.00100.21 N ANISOU 887 N ILE A 218 14018 13032 11025 1623 232 3951 N ATOM 888 CA ILE A 218 -50.044-134.766 286.994 1.00106.81 C ANISOU 888 CA ILE A 218 14855 14199 11528 1574 297 4277 C ATOM 889 C ILE A 218 -51.229-134.972 286.059 1.00109.62 C ANISOU 889 C ILE A 218 15111 15022 11518 1780 139 4442 C ATOM 890 O ILE A 218 -51.402-134.230 285.085 1.00112.59 O ANISOU 890 O ILE A 218 15526 15538 11714 1880 142 4886 O ATOM 891 CB ILE A 218 -48.893-135.734 286.662 1.00107.33 C ANISOU 891 CB ILE A 218 14859 14506 11414 1311 413 4026 C ATOM 892 CG1 ILE A 218 -47.731-135.548 287.640 1.00107.26 C ANISOU 892 CG1 ILE A 218 14924 14060 11770 1116 552 3848 C ATOM 893 CG2 ILE A 218 -48.428-135.542 285.225 1.00109.26 C ANISOU 893 CG2 ILE A 218 15096 15123 11295 1247 499 4356 C ATOM 894 CD1 ILE A 218 -47.052-134.203 287.540 1.00110.76 C ANISOU 894 CD1 ILE A 218 15511 14134 12437 1059 692 4226 C ATOM 895 N HIS A 219 -52.064-135.975 286.342 1.00108.81 N ANISOU 895 N HIS A 219 14872 15174 11299 1842 -2 4098 N ATOM 896 CA HIS A 219 -53.109-136.365 285.400 1.00113.54 C ANISOU 896 CA HIS A 219 15336 16297 11506 1994 -153 4180 C ATOM 897 C HIS A 219 -54.198-135.304 285.298 1.00116.60 C ANISOU 897 C HIS A 219 15749 16594 11961 2290 -270 4555 C ATOM 898 O HIS A 219 -54.676-135.003 284.197 1.00119.84 O ANISOU 898 O HIS A 219 16114 17367 12051 2422 -340 4888 O ATOM 899 CB HIS A 219 -53.704-137.712 285.813 1.00111.98 C ANISOU 899 CB HIS A 219 14981 16348 11218 1957 -264 3692 C ATOM 900 CG HIS A 219 -54.366-138.453 284.693 1.00114.15 C ANISOU 900 CG HIS A 219 15093 17248 11031 1996 -378 3653 C ATOM 901 ND1 HIS A 219 -53.662-138.986 283.634 1.00115.49 N ANISOU 901 ND1 HIS A 219 15218 17813 10851 1843 -304 3635 N ATOM 902 CD2 HIS A 219 -55.666-138.757 284.470 1.00115.61 C ANISOU 902 CD2 HIS A 219 15132 17755 11038 2164 -560 3603 C ATOM 903 CE1 HIS A 219 -54.501-139.583 282.807 1.00117.62 C ANISOU 903 CE1 HIS A 219 15327 18619 10743 1913 -439 3567 C ATOM 904 NE2 HIS A 219 -55.724-139.458 283.291 1.00117.66 N ANISOU 904 NE2 HIS A 219 15266 18593 10848 2103 -599 3550 N ATOM 905 N ARG A 220 -54.613-134.735 286.427 1.00116.24 N ANISOU 905 N ARG A 220 15763 16086 12317 2409 -296 4502 N ATOM 906 CA ARG A 220 -55.642-133.694 286.454 1.00119.93 C ANISOU 906 CA ARG A 220 16249 16404 12914 2714 -401 4826 C ATOM 907 C ARG A 220 -55.196-132.600 287.412 1.00116.01 C ANISOU 907 C ARG A 220 15925 15237 12915 2734 -294 4921 C ATOM 908 O ARG A 220 -55.695-132.491 288.538 1.00112.93 O ANISOU 908 O ARG A 220 15525 14553 12829 2824 -335 4686 O ATOM 909 CB ARG A 220 -57.004-134.271 286.850 1.00123.48 C ANISOU 909 CB ARG A 220 16526 17086 13306 2893 -587 4575 C ATOM 910 CG ARG A 220 -57.461-135.429 285.967 1.00127.77 C ANISOU 910 CG ARG A 220 16881 18286 13378 2844 -695 4412 C ATOM 911 CD ARG A 220 -58.972-135.571 285.951 1.00132.89 C ANISOU 911 CD ARG A 220 17352 19221 13920 3091 -898 4375 C ATOM 912 NE ARG A 220 -59.421-136.820 286.557 1.00133.57 N ANISOU 912 NE ARG A 220 17287 19490 13976 2977 -961 3869 N ATOM 913 CZ ARG A 220 -60.698-137.137 286.744 1.00136.35 C ANISOU 913 CZ ARG A 220 17459 20080 14269 3134 -1121 3732 C ATOM 914 NH1 ARG A 220 -61.653-136.295 286.374 1.00140.24 N ANISOU 914 NH1 ARG A 220 17892 20670 14724 3433 -1244 4054 N ATOM 915 NH2 ARG A 220 -61.021-138.293 287.305 1.00134.07 N ANISOU 915 NH2 ARG A 220 17042 19927 13970 2992 -1157 3284 N ATOM 916 N PRO A 221 -54.253-131.753 286.985 1.00116.31 N ANISOU 916 N PRO A 221 16118 15028 13047 2642 -149 5261 N ATOM 917 CA PRO A 221 -53.682-130.760 287.912 1.00115.45 C ANISOU 917 CA PRO A 221 16171 14261 13433 2608 -28 5299 C ATOM 918 C PRO A 221 -54.690-129.755 288.433 1.00115.72 C ANISOU 918 C PRO A 221 16241 13948 13780 2916 -116 5457 C ATOM 919 O PRO A 221 -54.576-129.315 289.585 1.00113.51 O ANISOU 919 O PRO A 221 16027 13190 13912 2914 -68 5249 O ATOM 920 CB PRO A 221 -52.597-130.080 287.064 1.00118.05 C ANISOU 920 CB PRO A 221 16633 14494 13728 2452 134 5700 C ATOM 921 CG PRO A 221 -53.027-130.298 285.650 1.00120.74 C ANISOU 921 CG PRO A 221 16890 15395 13591 2531 54 5995 C ATOM 922 CD PRO A 221 -53.680-131.647 285.633 1.00117.90 C ANISOU 922 CD PRO A 221 16343 15552 12903 2556 -82 5625 C ATOM 923 N LEU A 222 -55.676-129.375 287.623 1.00119.12 N ANISOU 923 N LEU A 222 16604 14618 14039 3137 -254 5717 N ATOM 924 CA LEU A 222 -56.664-128.406 288.075 1.00119.28 C ANISOU 924 CA LEU A 222 16626 14321 14374 3388 -351 5762 C ATOM 925 C LEU A 222 -57.662-129.033 289.043 1.00118.71 C ANISOU 925 C LEU A 222 16411 14336 14356 3566 -468 5411 C ATOM 926 O LEU A 222 -57.975-128.441 290.082 1.00118.46 O ANISOU 926 O LEU A 222 16416 13877 14718 3681 -460 5265 O ATOM 927 CB LEU A 222 -57.380-127.797 286.871 1.00122.57 C ANISOU 927 CB LEU A 222 17001 14975 14594 3536 -466 6109 C ATOM 928 CG LEU A 222 -56.413-127.211 285.840 1.00124.65 C ANISOU 928 CG LEU A 222 17397 15204 14760 3357 -348 6472 C ATOM 929 CD1 LEU A 222 -57.155-126.524 284.708 1.00129.38 C ANISOU 929 CD1 LEU A 222 17967 16001 15189 3526 -464 6832 C ATOM 930 CD2 LEU A 222 -55.433-126.254 286.511 1.00123.83 C ANISOU 930 CD2 LEU A 222 17494 14440 15117 3218 -178 6525 C ATOM 931 N ALA A 223 -58.157-130.230 288.731 1.00117.58 N ANISOU 931 N ALA A 223 16100 14750 13823 3576 -573 5247 N ATOM 932 CA ALA A 223 -59.086-130.937 289.603 1.00113.80 C ANISOU 932 CA ALA A 223 15463 14408 13367 3679 -682 4860 C ATOM 933 C ALA A 223 -58.403-131.592 290.797 1.00111.24 C ANISOU 933 C ALA A 223 15165 13863 13238 3420 -581 4379 C ATOM 934 O ALA A 223 -59.097-132.147 291.656 1.00109.85 O ANISOU 934 O ALA A 223 14868 13751 13120 3458 -650 4027 O ATOM 935 CB ALA A 223 -59.848-131.998 288.804 1.00112.37 C ANISOU 935 CB ALA A 223 15075 14904 12718 3703 -832 4779 C ATOM 936 N TYR A 224 -57.070-131.539 290.865 1.00109.33 N ANISOU 936 N TYR A 224 15066 13384 13089 3158 -422 4367 N ATOM 937 CA TYR A 224 -56.342-132.170 291.962 1.00103.06 C ANISOU 937 CA TYR A 224 14290 12407 12461 2914 -334 3934 C ATOM 938 C TYR A 224 -56.758-131.611 293.316 1.00104.48 C ANISOU 938 C TYR A 224 14488 12174 13034 3027 -332 3722 C ATOM 939 O TYR A 224 -56.789-132.348 294.308 1.00101.67 O ANISOU 939 O TYR A 224 14064 11834 12732 2921 -336 3320 O ATOM 940 CB TYR A 224 -54.838-131.989 291.749 1.00 99.95 C ANISOU 940 CB TYR A 224 14040 11808 12128 2646 -164 4012 C ATOM 941 CG TYR A 224 -53.983-132.385 292.929 1.00 95.68 C ANISOU 941 CG TYR A 224 13533 11008 11815 2417 -70 3620 C ATOM 942 CD1 TYR A 224 -53.672-133.714 293.167 1.00 90.60 C ANISOU 942 CD1 TYR A 224 12793 10647 10986 2229 -81 3272 C ATOM 943 CD2 TYR A 224 -53.475-131.427 293.798 1.00 95.27 C ANISOU 943 CD2 TYR A 224 13602 10427 12167 2391 28 3597 C ATOM 944 CE1 TYR A 224 -52.888-134.079 294.238 1.00 85.52 C ANISOU 944 CE1 TYR A 224 12171 9787 10536 2037 -6 2945 C ATOM 945 CE2 TYR A 224 -52.689-131.784 294.876 1.00 91.01 C ANISOU 945 CE2 TYR A 224 13078 9695 11808 2184 102 3239 C ATOM 946 CZ TYR A 224 -52.397-133.113 295.091 1.00 85.35 C ANISOU 946 CZ TYR A 224 12261 9286 10882 2015 81 2929 C ATOM 947 OH TYR A 224 -51.614-133.477 296.164 1.00 81.26 O ANISOU 947 OH TYR A 224 11749 8596 10530 1826 143 2601 O ATOM 948 N LYS A 225 -57.085-130.318 293.378 1.00109.58 N ANISOU 948 N LYS A 225 15222 12453 13959 3246 -322 3985 N ATOM 949 CA LYS A 225 -57.435-129.697 294.649 1.00109.02 C ANISOU 949 CA LYS A 225 15170 11973 14279 3358 -305 3763 C ATOM 950 C LYS A 225 -58.783-130.170 295.184 1.00108.48 C ANISOU 950 C LYS A 225 14914 12159 14144 3561 -443 3528 C ATOM 951 O LYS A 225 -59.066-129.973 296.370 1.00105.28 O ANISOU 951 O LYS A 225 14485 11522 13994 3608 -426 3237 O ATOM 952 CB LYS A 225 -57.429-128.173 294.504 1.00115.50 C ANISOU 952 CB LYS A 225 16135 12307 15442 3548 -254 4108 C ATOM 953 CG LYS A 225 -56.081-127.596 294.080 1.00116.22 C ANISOU 953 CG LYS A 225 16413 12090 15656 3326 -97 4340 C ATOM 954 CD LYS A 225 -56.091-127.147 292.625 1.00119.84 C ANISOU 954 CD LYS A 225 16922 12700 15912 3405 -115 4871 C ATOM 955 CE LYS A 225 -54.742-126.583 292.207 1.00120.49 C ANISOU 955 CE LYS A 225 17170 12505 16105 3136 49 5073 C ATOM 956 NZ LYS A 225 -53.679-127.624 292.184 1.00114.77 N ANISOU 956 NZ LYS A 225 16431 12014 15161 2823 142 4878 N ATOM 957 N ARG A 226 -59.613-130.792 294.344 1.00112.56 N ANISOU 957 N ARG A 226 15284 13168 14314 3670 -575 3633 N ATOM 958 CA ARG A 226 -60.896-131.329 294.785 1.00117.55 C ANISOU 958 CA ARG A 226 15712 14095 14859 3833 -704 3404 C ATOM 959 C ARG A 226 -60.811-132.804 295.160 1.00116.32 C ANISOU 959 C ARG A 226 15439 14283 14473 3584 -720 3022 C ATOM 960 O ARG A 226 -61.392-133.220 296.168 1.00116.02 O ANISOU 960 O ARG A 226 15291 14275 14515 3593 -744 2700 O ATOM 961 CB ARG A 226 -61.957-131.139 293.695 1.00124.96 C ANISOU 961 CB ARG A 226 16526 15387 15564 4108 -855 3722 C ATOM 962 CG ARG A 226 -63.292-131.816 293.998 1.00128.80 C ANISOU 962 CG ARG A 226 16764 16266 15908 4248 -996 3485 C ATOM 963 CD ARG A 226 -64.333-131.555 292.914 1.00136.57 C ANISOU 963 CD ARG A 226 17608 17615 16666 4536 -1157 3806 C ATOM 964 NE ARG A 226 -64.059-132.282 291.676 1.00142.39 N ANISOU 964 NE ARG A 226 18311 18809 16980 4397 -1209 3955 N ATOM 965 CZ ARG A 226 -64.647-133.424 291.331 1.00145.25 C ANISOU 965 CZ ARG A 226 18473 19705 17008 4314 -1315 3750 C ATOM 966 NH1 ARG A 226 -65.547-133.980 292.131 1.00145.96 N ANISOU 966 NH1 ARG A 226 18380 19938 17139 4345 -1377 3414 N ATOM 967 NH2 ARG A 226 -64.337-134.011 290.184 1.00146.07 N ANISOU 967 NH2 ARG A 226 18553 20209 16737 4188 -1353 3870 N ATOM 968 N ILE A 227 -60.093-133.606 294.371 1.00111.59 N ANISOU 968 N ILE A 227 14859 13942 13597 3360 -700 3053 N ATOM 969 CA ILE A 227 -60.093-135.051 294.587 1.00104.26 C ANISOU 969 CA ILE A 227 13812 13347 12453 3146 -727 2714 C ATOM 970 C ILE A 227 -59.213-135.444 295.771 1.00 94.71 C ANISOU 970 C ILE A 227 12678 11861 11445 2913 -614 2397 C ATOM 971 O ILE A 227 -59.523-136.405 296.485 1.00 90.62 O ANISOU 971 O ILE A 227 12054 11493 10885 2810 -641 2080 O ATOM 972 CB ILE A 227 -59.662-135.779 293.302 1.00105.49 C ANISOU 972 CB ILE A 227 13949 13885 12248 3007 -745 2829 C ATOM 973 CG1 ILE A 227 -60.510-135.311 292.118 1.00110.35 C ANISOU 973 CG1 ILE A 227 14486 14804 12639 3247 -865 3172 C ATOM 974 CG2 ILE A 227 -59.788-137.288 293.472 1.00103.32 C ANISOU 974 CG2 ILE A 227 13538 13943 11774 2808 -784 2471 C ATOM 975 CD1 ILE A 227 -60.186-136.014 290.818 1.00111.91 C ANISOU 975 CD1 ILE A 227 14640 15444 12437 3123 -891 3268 C ATOM 976 N VAL A 228 -58.114-134.733 296.002 1.00 93.20 N ANISOU 976 N VAL A 228 12662 11280 11470 2820 -490 2480 N ATOM 977 CA VAL A 228 -57.219-135.009 297.120 1.00 87.70 C ANISOU 977 CA VAL A 228 12030 10329 10962 2608 -391 2194 C ATOM 978 C VAL A 228 -57.419-133.911 298.154 1.00 89.79 C ANISOU 978 C VAL A 228 12354 10181 11581 2744 -351 2143 C ATOM 979 O VAL A 228 -57.022-132.759 297.937 1.00 89.91 O ANISOU 979 O VAL A 228 12499 9859 11803 2817 -287 2368 O ATOM 980 CB VAL A 228 -55.751-135.093 296.680 1.00 82.75 C ANISOU 980 CB VAL A 228 11529 9594 10317 2371 -277 2266 C ATOM 981 CG1 VAL A 228 -54.851-135.301 297.890 1.00 77.56 C ANISOU 981 CG1 VAL A 228 10922 8681 9867 2175 -189 1975 C ATOM 982 CG2 VAL A 228 -55.562-136.215 295.674 1.00 82.76 C ANISOU 982 CG2 VAL A 228 11458 10017 9969 2243 -310 2270 C ATOM 983 N THR A 229 -58.036-134.262 299.278 1.00 86.45 N ANISOU 983 N THR A 229 11832 9783 11231 2772 -381 1842 N ATOM 984 CA THR A 229 -58.249-133.334 300.375 1.00 86.49 C ANISOU 984 CA THR A 229 11869 9440 11553 2890 -339 1713 C ATOM 985 C THR A 229 -57.693-133.936 301.656 1.00 88.15 C ANISOU 985 C THR A 229 12069 9595 11830 2682 -283 1352 C ATOM 986 O THR A 229 -57.528-135.152 301.776 1.00 90.11 O ANISOU 986 O THR A 229 12247 10113 11877 2507 -306 1199 O ATOM 987 CB THR A 229 -59.737-132.999 300.566 1.00 64.61 C ANISOU 987 CB THR A 229 8958 6784 8807 3184 -432 1704 C ATOM 988 OG1 THR A 229 -60.417-134.131 301.119 1.00 73.77 O ANISOU 988 OG1 THR A 229 9949 8295 9786 3122 -492 1438 O ATOM 989 CG2 THR A 229 -60.381-132.630 299.238 1.00 67.46 C ANISOU 989 CG2 THR A 229 9291 7310 9031 3395 -519 2067 C ATOM 990 N ARG A 230 -57.403-133.061 302.616 1.00 88.65 N ANISOU 990 N ARG A 230 12199 9301 12182 2706 -211 1217 N ATOM 991 CA ARG A 230 -56.954-133.531 303.922 1.00 84.52 C ANISOU 991 CA ARG A 230 11652 8751 11712 2534 -168 873 C ATOM 992 C ARG A 230 -57.976-134.437 304.603 1.00 80.73 C ANISOU 992 C ARG A 230 10999 8605 11071 2571 -238 655 C ATOM 993 O ARG A 230 -57.560-135.455 305.184 1.00 75.07 O ANISOU 993 O ARG A 230 10243 8048 10233 2368 -232 470 O ATOM 994 CB ARG A 230 -56.591-132.325 304.799 1.00 92.55 C ANISOU 994 CB ARG A 230 12753 9346 13065 2577 -85 747 C ATOM 995 CG ARG A 230 -55.549-132.602 305.870 1.00 96.10 C ANISOU 995 CG ARG A 230 13234 9701 13580 2335 -18 466 C ATOM 996 CD ARG A 230 -56.195-133.000 307.184 1.00 98.47 C ANISOU 996 CD ARG A 230 13407 10162 13846 2358 -40 139 C ATOM 997 NE ARG A 230 -57.292-132.105 307.538 1.00104.23 N ANISOU 997 NE ARG A 230 14081 10783 14737 2625 -49 80 N ATOM 998 CZ ARG A 230 -57.961-132.161 308.684 1.00107.23 C ANISOU 998 CZ ARG A 230 14346 11272 15126 2688 -49 -207 C ATOM 999 NH1 ARG A 230 -57.643-133.067 309.597 1.00106.25 N ANISOU 999 NH1 ARG A 230 14158 11365 14847 2497 -45 -433 N ATOM 1000 NH2 ARG A 230 -58.948-131.310 308.920 1.00109.44 N ANISOU 1000 NH2 ARG A 230 14566 11452 15565 2951 -51 -261 N ATOM 1001 N PRO A 231 -59.288-134.155 304.579 1.00 79.57 N ANISOU 1001 N PRO A 231 10734 8580 10918 2813 -301 673 N ATOM 1002 CA PRO A 231 -60.239-135.140 305.123 1.00 79.01 C ANISOU 1002 CA PRO A 231 10482 8873 10666 2808 -360 484 C ATOM 1003 C PRO A 231 -60.248-136.459 304.368 1.00 76.29 C ANISOU 1003 C PRO A 231 10076 8875 10036 2656 -422 548 C ATOM 1004 O PRO A 231 -60.336-137.523 304.994 1.00 76.50 O ANISOU 1004 O PRO A 231 10018 9108 9940 2498 -429 359 O ATOM 1005 CB PRO A 231 -61.588-134.416 305.016 1.00 79.86 C ANISOU 1005 CB PRO A 231 10472 9029 10841 3122 -415 535 C ATOM 1006 CG PRO A 231 -61.242-132.977 305.033 1.00 81.18 C ANISOU 1006 CG PRO A 231 10772 8763 11310 3276 -357 627 C ATOM 1007 CD PRO A 231 -59.960-132.878 304.271 1.00 80.89 C ANISOU 1007 CD PRO A 231 10918 8532 11285 3104 -311 829 C ATOM 1008 N LYS A 232 -60.167-136.422 303.035 1.00 73.38 N ANISOU 1008 N LYS A 232 9746 8579 9557 2696 -464 809 N ATOM 1009 CA LYS A 232 -60.165-137.660 302.260 1.00 71.40 C ANISOU 1009 CA LYS A 232 9432 8662 9037 2551 -520 836 C ATOM 1010 C LYS A 232 -58.926-138.497 302.554 1.00 72.11 C ANISOU 1010 C LYS A 232 9604 8698 9096 2268 -457 717 C ATOM 1011 O LYS A 232 -59.007-139.728 302.647 1.00 72.24 O ANISOU 1011 O LYS A 232 9540 8947 8959 2116 -486 586 O ATOM 1012 CB LYS A 232 -60.253-137.353 300.765 1.00 72.69 C ANISOU 1012 CB LYS A 232 9619 8929 9070 2654 -571 1135 C ATOM 1013 CG LYS A 232 -61.655-137.061 300.246 1.00 75.61 C ANISOU 1013 CG LYS A 232 9840 9536 9353 2911 -679 1249 C ATOM 1014 CD LYS A 232 -61.622-136.802 298.747 1.00 76.52 C ANISOU 1014 CD LYS A 232 9984 9790 9302 2996 -734 1565 C ATOM 1015 CE LYS A 232 -63.017-136.689 298.152 1.00 77.32 C ANISOU 1015 CE LYS A 232 9904 10208 9264 3239 -865 1673 C ATOM 1016 N ALA A 233 -57.768-137.848 302.699 1.00 72.21 N ANISOU 1016 N ALA A 233 9770 8398 9267 2194 -372 759 N ATOM 1017 CA ALA A 233 -56.529-138.587 302.921 1.00 66.76 C ANISOU 1017 CA ALA A 233 9145 7666 8555 1944 -317 659 C ATOM 1018 C ALA A 233 -56.536-139.293 304.271 1.00 63.77 C ANISOU 1018 C ALA A 233 8704 7324 8200 1831 -310 390 C ATOM 1019 O ALA A 233 -56.056-140.427 304.385 1.00 61.68 O ANISOU 1019 O ALA A 233 8417 7187 7833 1653 -314 296 O ATOM 1020 CB ALA A 233 -55.329-137.646 302.812 1.00 66.02 C ANISOU 1020 CB ALA A 233 9207 7241 8638 1890 -225 759 C ATOM 1021 N VAL A 234 -57.074-138.642 305.305 1.00 63.77 N ANISOU 1021 N VAL A 234 8673 7221 8337 1937 -297 266 N ATOM 1022 CA VAL A 234 -57.152-139.272 306.621 1.00 62.10 C ANISOU 1022 CA VAL A 234 8391 7088 8117 1836 -288 27 C ATOM 1023 C VAL A 234 -57.994-140.540 306.552 1.00 61.61 C ANISOU 1023 C VAL A 234 8191 7360 7858 1784 -352 -19 C ATOM 1024 O VAL A 234 -57.611-141.593 307.076 1.00 59.05 O ANISOU 1024 O VAL A 234 7844 7130 7463 1607 -350 -124 O ATOM 1025 CB VAL A 234 -57.706-138.280 307.659 1.00 63.56 C ANISOU 1025 CB VAL A 234 8546 7144 8459 1980 -259 -111 C ATOM 1026 CG1 VAL A 234 -58.008-138.993 308.958 1.00 61.86 C ANISOU 1026 CG1 VAL A 234 8229 7101 8175 1889 -255 -337 C ATOM 1027 CG2 VAL A 234 -56.716-137.149 307.892 1.00 65.58 C ANISOU 1027 CG2 VAL A 234 8940 7041 8938 1974 -186 -120 C ATOM 1028 N VAL A 235 -59.150-140.458 305.889 1.00 63.81 N ANISOU 1028 N VAL A 235 8371 7817 8056 1937 -412 65 N ATOM 1029 CA VAL A 235 -60.022-141.623 305.761 1.00 62.69 C ANISOU 1029 CA VAL A 235 8083 7997 7741 1876 -472 10 C ATOM 1030 C VAL A 235 -59.324-142.734 304.988 1.00 60.79 C ANISOU 1030 C VAL A 235 7877 7841 7378 1688 -488 46 C ATOM 1031 O VAL A 235 -59.369-143.906 305.382 1.00 57.40 O ANISOU 1031 O VAL A 235 7387 7543 6879 1528 -497 -64 O ATOM 1032 CB VAL A 235 -61.355-141.217 305.103 1.00 61.46 C ANISOU 1032 CB VAL A 235 7799 8031 7523 2087 -542 95 C ATOM 1033 CG1 VAL A 235 -62.081-142.437 304.561 1.00 60.94 C ANISOU 1033 CG1 VAL A 235 7590 8302 7264 1994 -612 66 C ATOM 1034 CG2 VAL A 235 -62.228-140.477 306.102 1.00 59.96 C ANISOU 1034 CG2 VAL A 235 7517 7825 7439 2252 -525 -16 C ATOM 1035 N ALA A 236 -58.650-142.383 303.889 1.00 61.97 N ANISOU 1035 N ALA A 236 8125 7912 7509 1704 -485 201 N ATOM 1036 CA ALA A 236 -58.002-143.393 303.057 1.00 61.81 C ANISOU 1036 CA ALA A 236 8125 7994 7366 1544 -493 214 C ATOM 1037 C ALA A 236 -56.923-144.144 303.829 1.00 64.17 C ANISOU 1037 C ALA A 236 8483 8169 7730 1347 -442 88 C ATOM 1038 O ALA A 236 -56.895-145.380 303.833 1.00 70.06 O ANISOU 1038 O ALA A 236 9176 9040 8405 1207 -461 -6 O ATOM 1039 CB ALA A 236 -57.417-142.745 301.802 1.00 61.58 C ANISOU 1039 CB ALA A 236 8188 7913 7295 1600 -481 411 C ATOM 1040 N PHE A 237 -56.019-143.410 304.487 1.00 61.36 N ANISOU 1040 N PHE A 237 8231 7564 7521 1336 -379 83 N ATOM 1041 CA PHE A 237 -54.950-144.061 305.243 1.00 61.36 C ANISOU 1041 CA PHE A 237 8273 7465 7577 1167 -341 -26 C ATOM 1042 C PHE A 237 -55.512-144.936 306.354 1.00 63.33 C ANISOU 1042 C PHE A 237 8431 7828 7804 1098 -366 -164 C ATOM 1043 O PHE A 237 -55.017-146.044 306.591 1.00 62.00 O ANISOU 1043 O PHE A 237 8252 7691 7613 954 -370 -223 O ATOM 1044 CB PHE A 237 -53.998-143.018 305.826 1.00 62.83 C ANISOU 1044 CB PHE A 237 8560 7391 7921 1171 -277 -29 C ATOM 1045 CG PHE A 237 -52.957-142.537 304.859 1.00 64.42 C ANISOU 1045 CG PHE A 237 8860 7463 8155 1139 -230 96 C ATOM 1046 CD1 PHE A 237 -51.716-143.152 304.791 1.00 64.25 C ANISOU 1046 CD1 PHE A 237 8870 7400 8140 986 -196 57 C ATOM 1047 CD2 PHE A 237 -53.215-141.467 304.022 1.00 65.35 C ANISOU 1047 CD2 PHE A 237 9029 7504 8298 1268 -215 264 C ATOM 1048 CE1 PHE A 237 -50.755-142.706 303.903 1.00 65.10 C ANISOU 1048 CE1 PHE A 237 9051 7417 8269 945 -138 167 C ATOM 1049 CE2 PHE A 237 -52.259-141.016 303.132 1.00 66.40 C ANISOU 1049 CE2 PHE A 237 9248 7531 8448 1222 -158 403 C ATOM 1050 CZ PHE A 237 -51.027-141.636 303.073 1.00 66.29 C ANISOU 1050 CZ PHE A 237 9256 7499 8430 1053 -114 346 C ATOM 1051 N CYS A 238 -56.542-144.452 307.052 1.00 67.56 N ANISOU 1051 N CYS A 238 8895 8423 8350 1203 -376 -209 N ATOM 1052 CA CYS A 238 -57.168-145.259 308.093 1.00 68.63 C ANISOU 1052 CA CYS A 238 8930 8703 8442 1130 -388 -319 C ATOM 1053 C CYS A 238 -57.712-146.561 307.519 1.00 67.60 C ANISOU 1053 C CYS A 238 8716 8766 8204 1031 -434 -318 C ATOM 1054 O CYS A 238 -57.475-147.642 308.070 1.00 69.29 O ANISOU 1054 O CYS A 238 8909 9010 8409 881 -432 -369 O ATOM 1055 CB CYS A 238 -58.277-144.462 308.781 1.00 71.30 C ANISOU 1055 CB CYS A 238 9183 9112 8796 1276 -384 -375 C ATOM 1056 SG CYS A 238 -57.709-143.179 309.923 1.00 73.46 S ANISOU 1056 SG CYS A 238 9528 9172 9212 1348 -322 -471 S ATOM 1057 N LEU A 239 -58.427-146.481 306.393 1.00 65.60 N ANISOU 1057 N LEU A 239 8409 8642 7872 1111 -476 -258 N ATOM 1058 CA LEU A 239 -58.971-147.694 305.789 1.00 65.56 C ANISOU 1058 CA LEU A 239 8311 8829 7768 1005 -521 -292 C ATOM 1059 C LEU A 239 -57.867-148.588 305.238 1.00 70.55 C ANISOU 1059 C LEU A 239 9021 9377 8407 860 -511 -304 C ATOM 1060 O LEU A 239 -57.930-149.815 305.383 1.00 73.87 O ANISOU 1060 O LEU A 239 9395 9848 8825 713 -521 -379 O ATOM 1061 CB LEU A 239 -59.978-147.342 304.693 1.00 63.94 C ANISOU 1061 CB LEU A 239 8015 8822 7457 1131 -581 -239 C ATOM 1062 CG LEU A 239 -61.379-146.974 305.190 1.00 64.09 C ANISOU 1062 CG LEU A 239 7884 9016 7452 1244 -608 -270 C ATOM 1063 CD1 LEU A 239 -62.415-147.159 304.090 1.00 62.64 C ANISOU 1063 CD1 LEU A 239 7563 9104 7135 1306 -688 -249 C ATOM 1064 CD2 LEU A 239 -61.747-147.791 306.425 1.00 63.62 C ANISOU 1064 CD2 LEU A 239 7746 9010 7417 1104 -578 -382 C ATOM 1065 N MET A 240 -56.849-147.997 304.604 1.00 69.29 N ANISOU 1065 N MET A 240 8974 9083 8271 897 -484 -234 N ATOM 1066 CA MET A 240 -55.738-148.792 304.090 1.00 64.97 C ANISOU 1066 CA MET A 240 8487 8466 7734 773 -464 -262 C ATOM 1067 C MET A 240 -55.090-149.612 305.199 1.00 60.41 C ANISOU 1067 C MET A 240 7928 7769 7257 646 -442 -336 C ATOM 1068 O MET A 240 -54.792-150.798 305.012 1.00 56.98 O ANISOU 1068 O MET A 240 7475 7338 6836 529 -450 -400 O ATOM 1069 CB MET A 240 -54.706-147.885 303.415 1.00 66.24 C ANISOU 1069 CB MET A 240 8755 8501 7911 827 -419 -166 C ATOM 1070 CG MET A 240 -53.547-148.624 302.749 1.00 67.00 C ANISOU 1070 CG MET A 240 8894 8561 8004 717 -389 -204 C ATOM 1071 SD MET A 240 -52.188-149.047 303.864 1.00 68.67 S ANISOU 1071 SD MET A 240 9163 8557 8373 609 -345 -270 S ATOM 1072 CE MET A 240 -51.561-147.419 304.270 1.00 71.12 C ANISOU 1072 CE MET A 240 9565 8691 8767 690 -293 -175 C ATOM 1073 N TRP A 241 -54.865-148.997 306.361 1.00 62.90 N ANISOU 1073 N TRP A 241 8275 7978 7645 674 -418 -329 N ATOM 1074 CA TRP A 241 -54.315-149.736 307.493 1.00 65.65 C ANISOU 1074 CA TRP A 241 8629 8255 8059 567 -409 -373 C ATOM 1075 C TRP A 241 -55.256-150.846 307.938 1.00 64.95 C ANISOU 1075 C TRP A 241 8446 8292 7941 479 -437 -408 C ATOM 1076 O TRP A 241 -54.811-151.951 308.271 1.00 65.59 O ANISOU 1076 O TRP A 241 8527 8321 8072 363 -441 -422 O ATOM 1077 CB TRP A 241 -54.030-148.784 308.653 1.00 67.02 C ANISOU 1077 CB TRP A 241 8835 8348 8281 617 -383 -380 C ATOM 1078 CG TRP A 241 -52.673-148.173 308.602 1.00 67.30 C ANISOU 1078 CG TRP A 241 8962 8213 8394 616 -351 -371 C ATOM 1079 CD1 TRP A 241 -52.303-147.053 307.918 1.00 67.82 C ANISOU 1079 CD1 TRP A 241 9093 8183 8494 693 -319 -327 C ATOM 1080 CD2 TRP A 241 -51.496-148.648 309.264 1.00 66.59 C ANISOU 1080 CD2 TRP A 241 8899 8036 8364 527 -346 -397 C ATOM 1081 NE1 TRP A 241 -50.967-146.801 308.113 1.00 66.84 N ANISOU 1081 NE1 TRP A 241 9028 7917 8450 639 -286 -340 N ATOM 1082 CE2 TRP A 241 -50.449-147.766 308.937 1.00 65.80 C ANISOU 1082 CE2 TRP A 241 8867 7802 8331 544 -308 -391 C ATOM 1083 CE3 TRP A 241 -51.227-149.734 310.105 1.00 66.54 C ANISOU 1083 CE3 TRP A 241 8861 8056 8367 436 -372 -410 C ATOM 1084 CZ2 TRP A 241 -49.153-147.936 309.418 1.00 66.49 C ANISOU 1084 CZ2 TRP A 241 8973 7804 8485 474 -300 -422 C ATOM 1085 CZ3 TRP A 241 -49.942-149.901 310.581 1.00 66.45 C ANISOU 1085 CZ3 TRP A 241 8875 7954 8417 388 -372 -421 C ATOM 1086 CH2 TRP A 241 -48.920-149.008 310.237 1.00 66.44 C ANISOU 1086 CH2 TRP A 241 8925 7845 8476 407 -339 -439 C ATOM 1087 N THR A 242 -56.561-150.571 307.945 1.00 61.36 N ANISOU 1087 N THR A 242 7900 7997 7416 534 -454 -416 N ATOM 1088 CA THR A 242 -57.521-151.559 308.424 1.00 59.98 C ANISOU 1088 CA THR A 242 7618 7955 7217 431 -468 -447 C ATOM 1089 C THR A 242 -57.564-152.773 307.507 1.00 56.96 C ANISOU 1089 C THR A 242 7207 7591 6843 315 -494 -488 C ATOM 1090 O THR A 242 -57.533-153.917 307.976 1.00 56.97 O ANISOU 1090 O THR A 242 7187 7553 6906 174 -490 -501 O ATOM 1091 CB THR A 242 -58.906-150.932 308.540 1.00 65.10 C ANISOU 1091 CB THR A 242 8151 8796 7788 524 -478 -461 C ATOM 1092 OG1 THR A 242 -58.840-149.776 309.384 1.00 66.71 O ANISOU 1092 OG1 THR A 242 8381 8963 8004 643 -448 -456 O ATOM 1093 CG2 THR A 242 -59.862-151.929 309.140 1.00 68.33 C ANISOU 1093 CG2 THR A 242 8436 9351 8174 394 -478 -490 C ATOM 1094 N ILE A 243 -57.642-152.542 306.195 1.00 53.48 N ANISOU 1094 N ILE A 243 6762 7213 6344 370 -518 -510 N ATOM 1095 CA ILE A 243 -57.630-153.646 305.239 1.00 51.13 C ANISOU 1095 CA ILE A 243 6432 6949 6046 262 -539 -594 C ATOM 1096 C ILE A 243 -56.393-154.510 305.438 1.00 57.09 C ANISOU 1096 C ILE A 243 7273 7496 6924 165 -513 -616 C ATOM 1097 O ILE A 243 -56.468-155.744 305.411 1.00 65.22 O ANISOU 1097 O ILE A 243 8268 8482 8029 33 -519 -686 O ATOM 1098 CB ILE A 243 -57.713-153.105 303.800 1.00 47.80 C ANISOU 1098 CB ILE A 243 6003 6654 5506 353 -566 -604 C ATOM 1099 CG1 ILE A 243 -59.052-152.402 303.568 1.00 46.08 C ANISOU 1099 CG1 ILE A 243 5673 6662 5172 459 -610 -578 C ATOM 1100 CG2 ILE A 243 -57.494-154.228 302.793 1.00 47.45 C ANISOU 1100 CG2 ILE A 243 5930 6645 5452 239 -580 -731 C ATOM 1101 CD1 ILE A 243 -59.121-151.664 302.249 1.00 47.61 C ANISOU 1101 CD1 ILE A 243 5866 6993 5231 584 -643 -531 C ATOM 1102 N ALA A 244 -55.237-153.877 305.658 1.00 55.92 N ANISOU 1102 N ALA A 244 7226 7206 6813 230 -484 -560 N ATOM 1103 CA ALA A 244 -53.998-154.632 305.804 1.00 55.91 C ANISOU 1103 CA ALA A 244 7288 7025 6929 164 -465 -581 C ATOM 1104 C ALA A 244 -54.049-155.554 307.016 1.00 53.84 C ANISOU 1104 C ALA A 244 7012 6675 6770 66 -470 -550 C ATOM 1105 O ALA A 244 -53.576-156.695 306.957 1.00 55.49 O ANISOU 1105 O ALA A 244 7227 6764 7093 -19 -472 -587 O ATOM 1106 CB ALA A 244 -52.810-153.676 305.902 1.00 55.96 C ANISOU 1106 CB ALA A 244 7384 6928 6952 245 -434 -527 C ATOM 1107 N ILE A 245 -54.628-155.082 308.121 1.00 52.33 N ANISOU 1107 N ILE A 245 6798 6545 6541 82 -469 -478 N ATOM 1108 CA ILE A 245 -54.732-155.916 309.315 1.00 55.75 C ANISOU 1108 CA ILE A 245 7211 6934 7037 -15 -469 -415 C ATOM 1109 C ILE A 245 -55.657-157.102 309.060 1.00 61.60 C ANISOU 1109 C ILE A 245 7875 7707 7822 -148 -477 -450 C ATOM 1110 O ILE A 245 -55.360-158.236 309.457 1.00 64.74 O ANISOU 1110 O ILE A 245 8284 7971 8344 -253 -477 -414 O ATOM 1111 CB ILE A 245 -55.200-155.069 310.513 1.00 54.00 C ANISOU 1111 CB ILE A 245 6966 6822 6728 31 -456 -352 C ATOM 1112 CG1 ILE A 245 -54.127-154.041 310.882 1.00 58.27 C ANISOU 1112 CG1 ILE A 245 7585 7292 7265 130 -448 -340 C ATOM 1113 CG2 ILE A 245 -55.535-155.953 311.705 1.00 50.82 C ANISOU 1113 CG2 ILE A 245 6523 6441 6346 -83 -451 -265 C ATOM 1114 CD1 ILE A 245 -54.490-153.157 312.055 1.00 60.97 C ANISOU 1114 CD1 ILE A 245 7901 7738 7525 180 -432 -325 C ATOM 1115 N VAL A 246 -56.779-156.864 308.377 1.00 62.10 N ANISOU 1115 N VAL A 246 7855 7943 7799 -146 -486 -520 N ATOM 1116 CA VAL A 246 -57.728-157.936 308.087 1.00 60.57 C ANISOU 1116 CA VAL A 246 7566 7801 7646 -291 -494 -582 C ATOM 1117 C VAL A 246 -57.115-158.977 307.156 1.00 64.10 C ANISOU 1117 C VAL A 246 8044 8095 8217 -367 -502 -689 C ATOM 1118 O VAL A 246 -57.419-160.172 307.262 1.00 68.34 O ANISOU 1118 O VAL A 246 8546 8541 8882 -518 -497 -721 O ATOM 1119 CB VAL A 246 -59.022-157.338 307.506 1.00 58.57 C ANISOU 1119 CB VAL A 246 7194 7804 7255 -253 -514 -648 C ATOM 1120 CG1 VAL A 246 -59.948-158.430 306.982 1.00 58.73 C ANISOU 1120 CG1 VAL A 246 7100 7898 7317 -417 -528 -755 C ATOM 1121 CG2 VAL A 246 -59.727-156.506 308.561 1.00 58.10 C ANISOU 1121 CG2 VAL A 246 7082 7886 7108 -190 -495 -565 C ATOM 1122 N ILE A 247 -56.242-158.560 306.239 1.00 63.35 N ANISOU 1122 N ILE A 247 8011 7963 8096 -271 -507 -753 N ATOM 1123 CA ILE A 247 -55.640-159.528 305.332 1.00 65.73 C ANISOU 1123 CA ILE A 247 8328 8142 8506 -332 -506 -888 C ATOM 1124 C ILE A 247 -54.674-160.445 306.078 1.00 66.91 C ANISOU 1124 C ILE A 247 8544 8021 8856 -380 -490 -831 C ATOM 1125 O ILE A 247 -54.503-161.613 305.707 1.00 67.59 O ANISOU 1125 O ILE A 247 8621 7958 9101 -473 -486 -934 O ATOM 1126 CB ILE A 247 -54.966-158.792 304.159 1.00 65.79 C ANISOU 1126 CB ILE A 247 8370 8223 8404 -218 -503 -961 C ATOM 1127 CG1 ILE A 247 -56.031-158.084 303.318 1.00 66.58 C ANISOU 1127 CG1 ILE A 247 8389 8597 8311 -174 -533 -1005 C ATOM 1128 CG2 ILE A 247 -54.159-159.750 303.302 1.00 67.34 C ANISOU 1128 CG2 ILE A 247 8580 8298 8708 -264 -488 -1120 C ATOM 1129 CD1 ILE A 247 -55.553-157.626 301.964 1.00 68.00 C ANISOU 1129 CD1 ILE A 247 8581 8890 8365 -97 -532 -1081 C ATOM 1130 N ALA A 248 -54.062-159.959 307.155 1.00 67.86 N ANISOU 1130 N ALA A 248 8724 8078 8980 -316 -485 -673 N ATOM 1131 CA ALA A 248 -53.098-160.745 307.914 1.00 66.87 C ANISOU 1131 CA ALA A 248 8654 7728 9027 -334 -484 -588 C ATOM 1132 C ALA A 248 -53.729-161.561 309.038 1.00 64.94 C ANISOU 1132 C ALA A 248 8386 7423 8866 -451 -485 -451 C ATOM 1133 O ALA A 248 -53.011-162.297 309.722 1.00 67.46 O ANISOU 1133 O ALA A 248 8746 7554 9331 -465 -492 -343 O ATOM 1134 CB ALA A 248 -52.014-159.831 308.497 1.00 67.25 C ANISOU 1134 CB ALA A 248 8763 7764 9024 -211 -486 -493 C ATOM 1135 N VAL A 249 -55.044-161.460 309.245 1.00 60.86 N ANISOU 1135 N VAL A 249 7793 7070 8260 -534 -477 -440 N ATOM 1136 CA VAL A 249 -55.697-162.154 310.353 1.00 61.75 C ANISOU 1136 CA VAL A 249 7873 7163 8427 -662 -463 -289 C ATOM 1137 C VAL A 249 -56.405-163.433 309.913 1.00 60.89 C ANISOU 1137 C VAL A 249 7711 6943 8483 -840 -450 -362 C ATOM 1138 O VAL A 249 -56.740-164.268 310.768 1.00 60.78 O ANISOU 1138 O VAL A 249 7685 6831 8576 -969 -430 -216 O ATOM 1139 CB VAL A 249 -56.680-161.208 311.082 1.00 64.61 C ANISOU 1139 CB VAL A 249 8168 7795 8586 -649 -448 -220 C ATOM 1140 CG1 VAL A 249 -57.848-160.856 310.192 1.00 65.73 C ANISOU 1140 CG1 VAL A 249 8209 8134 8632 -672 -448 -370 C ATOM 1141 CG2 VAL A 249 -57.162-161.803 312.400 1.00 70.76 C ANISOU 1141 CG2 VAL A 249 8916 8589 9381 -770 -421 -31 C ATOM 1142 N LEU A 250 -56.608-163.631 308.611 1.00 60.55 N ANISOU 1142 N LEU A 250 7632 6908 8466 -860 -458 -584 N ATOM 1143 CA LEU A 250 -57.327-164.813 308.138 1.00 64.58 C ANISOU 1143 CA LEU A 250 8077 7322 9138 -1045 -447 -703 C ATOM 1144 C LEU A 250 -56.643-166.127 308.497 1.00 68.16 C ANISOU 1144 C LEU A 250 8597 7416 9883 -1126 -433 -639 C ATOM 1145 O LEU A 250 -57.341-167.050 308.955 1.00 68.70 O ANISOU 1145 O LEU A 250 8628 7378 10098 -1306 -407 -573 O ATOM 1146 CB LEU A 250 -57.550-164.692 306.628 1.00 64.24 C ANISOU 1146 CB LEU A 250 7979 7396 9035 -1033 -467 -980 C ATOM 1147 CG LEU A 250 -58.066-163.315 306.213 1.00 61.87 C ANISOU 1147 CG LEU A 250 7626 7428 8452 -909 -490 -1005 C ATOM 1148 CD1 LEU A 250 -57.411-162.870 304.918 1.00 61.31 C ANISOU 1148 CD1 LEU A 250 7582 7419 8296 -791 -509 -1173 C ATOM 1149 CD2 LEU A 250 -59.580-163.328 306.074 1.00 62.00 C ANISOU 1149 CD2 LEU A 250 7494 7685 8379 -1027 -498 -1070 C ATOM 1150 N PRO A 251 -55.323-166.302 308.313 1.00 69.20 N ANISOU 1150 N PRO A 251 8820 7347 10128 -1003 -445 -650 N ATOM 1151 CA PRO A 251 -54.706-167.573 308.736 1.00 70.61 C ANISOU 1151 CA PRO A 251 9056 7166 10609 -1057 -438 -564 C ATOM 1152 C PRO A 251 -54.943-167.886 310.200 1.00 72.93 C ANISOU 1152 C PRO A 251 9370 7400 10939 -1125 -429 -243 C ATOM 1153 O PRO A 251 -55.169-169.048 310.562 1.00 76.13 O ANISOU 1153 O PRO A 251 9784 7556 11584 -1264 -409 -151 O ATOM 1154 CB PRO A 251 -53.216-167.355 308.436 1.00 68.76 C ANISOU 1154 CB PRO A 251 8893 6816 10416 -866 -458 -602 C ATOM 1155 CG PRO A 251 -53.198-166.337 307.369 1.00 65.67 C ANISOU 1155 CG PRO A 251 8472 6674 9807 -778 -461 -808 C ATOM 1156 CD PRO A 251 -54.336-165.413 307.675 1.00 65.97 C ANISOU 1156 CD PRO A 251 8455 7014 9598 -817 -462 -741 C ATOM 1157 N LEU A 252 -54.907-166.863 311.054 1.00 72.43 N ANISOU 1157 N LEU A 252 9313 7566 10640 -1037 -440 -73 N ATOM 1158 CA LEU A 252 -55.215-167.059 312.464 1.00 74.20 C ANISOU 1158 CA LEU A 252 9540 7816 10834 -1106 -428 226 C ATOM 1159 C LEU A 252 -56.665-167.488 312.655 1.00 73.53 C ANISOU 1159 C LEU A 252 9366 7826 10747 -1323 -379 249 C ATOM 1160 O LEU A 252 -56.965-168.325 313.513 1.00 73.36 O ANISOU 1160 O LEU A 252 9347 7684 10843 -1460 -350 472 O ATOM 1161 CB LEU A 252 -54.918-165.773 313.231 1.00 77.46 C ANISOU 1161 CB LEU A 252 9962 8498 10973 -966 -446 332 C ATOM 1162 CG LEU A 252 -55.091-165.761 314.746 1.00 83.30 C ANISOU 1162 CG LEU A 252 10697 9346 11606 -1005 -437 625 C ATOM 1163 CD1 LEU A 252 -54.540-167.031 315.371 1.00 87.19 C ANISOU 1163 CD1 LEU A 252 11246 9550 12331 -1059 -448 859 C ATOM 1164 CD2 LEU A 252 -54.402-164.538 315.305 1.00 82.98 C ANISOU 1164 CD2 LEU A 252 10678 9509 11343 -835 -469 654 C ATOM 1165 N LEU A 253 -57.578-166.933 311.854 1.00 76.29 N ANISOU 1165 N LEU A 253 9625 8400 10963 -1360 -369 32 N ATOM 1166 CA LEU A 253 -58.984-167.311 311.931 1.00 80.96 C ANISOU 1166 CA LEU A 253 10099 9114 11549 -1570 -326 16 C ATOM 1167 C LEU A 253 -59.264-168.677 311.322 1.00 88.09 C ANISOU 1167 C LEU A 253 10985 9733 12752 -1763 -305 -95 C ATOM 1168 O LEU A 253 -60.363-169.208 311.516 1.00 91.04 O ANISOU 1168 O LEU A 253 11261 10152 13177 -1979 -261 -78 O ATOM 1169 CB LEU A 253 -59.853-166.262 311.236 1.00 80.99 C ANISOU 1169 CB LEU A 253 9993 9466 11315 -1524 -336 -184 C ATOM 1170 CG LEU A 253 -59.882-164.859 311.845 1.00 77.07 C ANISOU 1170 CG LEU A 253 9486 9260 10536 -1357 -343 -101 C ATOM 1171 CD1 LEU A 253 -60.670-163.910 310.955 1.00 75.13 C ANISOU 1171 CD1 LEU A 253 9138 9298 10108 -1287 -363 -305 C ATOM 1172 CD2 LEU A 253 -60.466-164.892 313.249 1.00 74.91 C ANISOU 1172 CD2 LEU A 253 9167 9118 10179 -1450 -293 136 C ATOM 1173 N GLY A 254 -58.312-169.250 310.595 1.00 92.12 N ANISOU 1173 N GLY A 254 11576 9956 13471 -1698 -331 -226 N ATOM 1174 CA GLY A 254 -58.529-170.541 309.979 1.00 93.94 C ANISOU 1174 CA GLY A 254 11791 9888 14012 -1873 -309 -376 C ATOM 1175 C GLY A 254 -58.484-170.500 308.467 1.00 92.64 C ANISOU 1175 C GLY A 254 11584 9760 13854 -1844 -334 -764 C ATOM 1176 O GLY A 254 -59.387-171.012 307.800 1.00 96.19 O ANISOU 1176 O GLY A 254 11933 10239 14377 -2028 -319 -979 O ATOM 1177 N TRP A 255 -57.453-169.863 307.916 1.00 88.00 N ANISOU 1177 N TRP A 255 11060 9207 13171 -1624 -369 -860 N ATOM 1178 CA TRP A 255 -57.134-170.010 306.503 1.00 86.46 C ANISOU 1178 CA TRP A 255 10842 8997 13011 -1586 -384 -1209 C ATOM 1179 C TRP A 255 -55.706-170.527 306.412 1.00 90.00 C ANISOU 1179 C TRP A 255 11398 9122 13675 -1449 -386 -1217 C ATOM 1180 O TRP A 255 -54.830-169.907 305.801 1.00 91.26 O ANISOU 1180 O TRP A 255 11587 9369 13719 -1269 -404 -1326 O ATOM 1181 CB TRP A 255 -57.311-168.694 305.744 1.00 80.63 C ANISOU 1181 CB TRP A 255 10052 8657 11926 -1454 -416 -1338 C ATOM 1182 CG TRP A 255 -57.235-168.858 304.250 1.00 77.38 C ANISOU 1182 CG TRP A 255 9587 8316 11496 -1452 -429 -1697 C ATOM 1183 CD1 TRP A 255 -56.853-169.976 303.560 1.00 78.04 C ANISOU 1183 CD1 TRP A 255 9674 8138 11838 -1527 -411 -1939 C ATOM 1184 CD2 TRP A 255 -57.550-167.870 303.265 1.00 76.36 C ANISOU 1184 CD2 TRP A 255 9390 8558 11066 -1367 -460 -1855 C ATOM 1185 NE1 TRP A 255 -56.906-169.740 302.209 1.00 78.61 N ANISOU 1185 NE1 TRP A 255 9677 8430 11763 -1501 -428 -2257 N ATOM 1186 CE2 TRP A 255 -57.331-168.454 302.001 1.00 77.82 C ANISOU 1186 CE2 TRP A 255 9533 8724 11311 -1403 -461 -2190 C ATOM 1187 CE3 TRP A 255 -57.993-166.546 303.328 1.00 74.18 C ANISOU 1187 CE3 TRP A 255 9081 8622 10480 -1257 -487 -1743 C ATOM 1188 CZ2 TRP A 255 -57.542-167.762 300.812 1.00 77.87 C ANISOU 1188 CZ2 TRP A 255 9466 9075 11046 -1337 -492 -2389 C ATOM 1189 CZ3 TRP A 255 -58.202-165.860 302.145 1.00 73.32 C ANISOU 1189 CZ3 TRP A 255 8908 8814 10136 -1182 -520 -1923 C ATOM 1190 CH2 TRP A 255 -57.976-166.469 300.905 1.00 75.81 C ANISOU 1190 CH2 TRP A 255 9182 9137 10486 -1226 -523 -2231 C ATOM 1191 N ASN A 256 -55.483-171.667 307.048 1.00 91.13 N ANISOU 1191 N ASN A 256 11593 8891 14142 -1533 -366 -1084 N ATOM 1192 CA ASN A 256 -54.203-172.340 307.138 1.00 89.38 C ANISOU 1192 CA ASN A 256 11461 8314 14186 -1405 -370 -1051 C ATOM 1193 C ASN A 256 -54.336-173.706 306.480 1.00 92.83 C ANISOU 1193 C ASN A 256 11882 8394 14994 -1545 -339 -1294 C ATOM 1194 O ASN A 256 -55.443-174.164 306.181 1.00 96.01 O ANISOU 1194 O ASN A 256 12211 8813 15456 -1769 -314 -1430 O ATOM 1195 CB ASN A 256 -53.786-172.474 308.604 1.00 87.60 C ANISOU 1195 CB ASN A 256 11314 7944 14026 -1356 -382 -629 C ATOM 1196 CG ASN A 256 -54.954-172.839 309.489 1.00 87.72 C ANISOU 1196 CG ASN A 256 11299 7970 14059 -1575 -352 -402 C ATOM 1197 OD1 ASN A 256 -55.701-173.761 309.183 1.00 91.11 O ANISOU 1197 OD1 ASN A 256 11690 8218 14711 -1782 -314 -514 O ATOM 1198 ND2 ASN A 256 -55.145-172.091 310.569 1.00 85.73 N ANISOU 1198 ND2 ASN A 256 11054 7954 13566 -1542 -361 -105 N ATOM 1199 N CYS A 257 -53.203-174.375 306.258 1.00 91.82 N ANISOU 1199 N CYS A 257 11814 7938 15136 -1416 -339 -1366 N ATOM 1200 CA CYS A 257 -53.279-175.651 305.559 1.00 93.64 C ANISOU 1200 CA CYS A 257 12027 7808 15742 -1533 -304 -1648 C ATOM 1201 C CYS A 257 -53.783-176.763 306.476 1.00 95.48 C ANISOU 1201 C CYS A 257 12302 7655 16323 -1714 -278 -1402 C ATOM 1202 O CYS A 257 -54.456-177.690 306.005 1.00 97.54 O ANISOU 1202 O CYS A 257 12521 7696 16844 -1924 -239 -1621 O ATOM 1203 CB CYS A 257 -51.918-176.022 304.970 1.00 94.46 C ANISOU 1203 CB CYS A 257 12165 7686 16040 -1323 -304 -1839 C ATOM 1204 SG CYS A 257 -50.601-176.409 306.139 1.00 94.97 S ANISOU 1204 SG CYS A 257 12335 7400 16347 -1103 -334 -1447 S ATOM 1205 N GLU A 258 -53.498-176.682 307.784 1.00 94.15 N ANISOU 1205 N GLU A 258 12208 7412 16155 -1652 -296 -947 N ATOM 1206 CA GLU A 258 -53.880-177.761 308.690 1.00 96.82 C ANISOU 1206 CA GLU A 258 12594 7371 16823 -1813 -267 -657 C ATOM 1207 C GLU A 258 -55.399-177.851 308.834 1.00 94.47 C ANISOU 1207 C GLU A 258 12219 7221 16455 -2122 -221 -647 C ATOM 1208 O GLU A 258 -55.975-178.942 308.751 1.00 97.94 O ANISOU 1208 O GLU A 258 12647 7327 17237 -2346 -172 -705 O ATOM 1209 CB GLU A 258 -53.211-177.550 310.045 1.00 99.54 C ANISOU 1209 CB GLU A 258 13022 7688 17112 -1663 -305 -161 C ATOM 1210 CG GLU A 258 -51.883-176.824 309.944 1.00101.00 C ANISOU 1210 CG GLU A 258 13235 7998 17144 -1351 -364 -176 C ATOM 1211 CD GLU A 258 -50.799-177.426 310.819 1.00105.82 C ANISOU 1211 CD GLU A 258 13926 8284 17996 -1175 -406 155 C ATOM 1212 OE1 GLU A 258 -51.061-177.691 312.009 1.00108.54 O ANISOU 1212 OE1 GLU A 258 14313 8568 18359 -1239 -413 579 O ATOM 1213 OE2 GLU A 258 -49.680-177.640 310.304 1.00106.49 O ANISOU 1213 OE2 GLU A 258 14021 8194 18245 -967 -431 -7 O ATOM 1214 N LYS A 259 -56.073-176.711 309.056 1.00 88.82 N ANISOU 1214 N LYS A 259 11437 6998 15311 -2141 -232 -581 N ATOM 1215 CA LYS A 259 -57.523-176.760 309.214 1.00 89.83 C ANISOU 1215 CA LYS A 259 11465 7306 15359 -2422 -188 -574 C ATOM 1216 C LYS A 259 -58.223-176.980 307.875 1.00 88.06 C ANISOU 1216 C LYS A 259 11128 7158 15175 -2574 -176 -1060 C ATOM 1217 O LYS A 259 -59.248-177.665 307.814 1.00 91.48 O ANISOU 1217 O LYS A 259 11482 7506 15771 -2855 -129 -1137 O ATOM 1218 CB LYS A 259 -58.035-175.478 309.856 1.00 88.34 C ANISOU 1218 CB LYS A 259 11227 7621 14718 -2375 -203 -378 C ATOM 1219 CG LYS A 259 -57.971-175.487 311.373 1.00 90.82 C ANISOU 1219 CG LYS A 259 11601 7914 14992 -2377 -188 115 C ATOM 1220 CD LYS A 259 -59.334-175.190 311.974 1.00 94.74 C ANISOU 1220 CD LYS A 259 11988 8721 15288 -2597 -136 248 C ATOM 1221 CE LYS A 259 -59.355-175.475 313.465 1.00 98.79 C ANISOU 1221 CE LYS A 259 12552 9179 15806 -2654 -102 737 C ATOM 1222 NZ LYS A 259 -60.680-175.167 314.072 1.00101.11 N ANISOU 1222 NZ LYS A 259 12720 9811 15886 -2869 -38 858 N ATOM 1223 N LEU A 260 -57.687-176.407 306.787 1.00 83.76 N ANISOU 1223 N LEU A 260 10562 6793 14470 -2401 -216 -1393 N ATOM 1224 CA LEU A 260 -58.285-176.584 305.469 1.00 85.96 C ANISOU 1224 CA LEU A 260 10724 7196 14741 -2527 -215 -1866 C ATOM 1225 C LEU A 260 -57.961-177.935 304.848 1.00 91.55 C ANISOU 1225 C LEU A 260 11452 7428 15906 -2626 -182 -2150 C ATOM 1226 O LEU A 260 -58.566-178.282 303.830 1.00 92.11 O ANISOU 1226 O LEU A 260 11413 7567 16017 -2784 -174 -2560 O ATOM 1227 CB LEU A 260 -57.825-175.465 304.540 1.00 82.87 C ANISOU 1227 CB LEU A 260 10303 7197 13988 -2307 -264 -2089 C ATOM 1228 CG LEU A 260 -58.950-174.654 303.893 1.00 82.12 C ANISOU 1228 CG LEU A 260 10059 7605 13539 -2395 -290 -2274 C ATOM 1229 CD1 LEU A 260 -59.851-174.053 304.958 1.00 80.95 C ANISOU 1229 CD1 LEU A 260 9872 7689 13198 -2470 -285 -1937 C ATOM 1230 CD2 LEU A 260 -58.381-173.572 302.993 1.00 78.34 C ANISOU 1230 CD2 LEU A 260 9571 7470 12724 -2163 -335 -2440 C ATOM 1231 N GLN A 261 -57.028-178.692 305.431 1.00 95.06 N ANISOU 1231 N GLN A 261 12023 7400 16694 -2531 -166 -1952 N ATOM 1232 CA GLN A 261 -56.631-180.007 304.921 1.00 98.23 C ANISOU 1232 CA GLN A 261 12477 7424 17421 -2531 -132 -2139 C ATOM 1233 C GLN A 261 -56.168-179.917 303.467 1.00 95.92 C ANISOU 1233 C GLN A 261 12129 7305 17010 -2404 -145 -2627 C ATOM 1234 O GLN A 261 -56.582-180.699 302.607 1.00 98.79 O ANISOU 1234 O GLN A 261 12440 7640 17457 -2516 -120 -2948 O ATOM 1235 CB GLN A 261 -57.767-181.025 305.074 1.00104.08 C ANISOU 1235 CB GLN A 261 13185 8012 18348 -2835 -82 -2134 C ATOM 1236 CG GLN A 261 -58.226-181.254 306.508 1.00107.41 C ANISOU 1236 CG GLN A 261 13661 8262 18887 -2980 -51 -1631 C ATOM 1237 CD GLN A 261 -57.281-182.138 307.306 1.00111.18 C ANISOU 1237 CD GLN A 261 14304 8296 19645 -2832 -37 -1293 C ATOM 1238 OE1 GLN A 261 -56.101-182.271 306.980 1.00111.76 O ANISOU 1238 OE1 GLN A 261 14447 8227 19790 -2565 -64 -1373 O ATOM 1239 NE2 GLN A 261 -57.805-182.754 308.359 1.00112.89 N ANISOU 1239 NE2 GLN A 261 14571 8314 20007 -3005 7 -908 N ATOM 1240 N SER A 262 -55.294-178.952 303.195 1.00 91.40 N ANISOU 1240 N SER A 262 11566 6928 16235 -2171 -181 -2674 N ATOM 1241 CA SER A 262 -54.804-178.690 301.849 1.00 96.19 C ANISOU 1241 CA SER A 262 12112 7770 16665 -2041 -187 -3095 C ATOM 1242 C SER A 262 -53.279-178.706 301.851 1.00103.50 C ANISOU 1242 C SER A 262 13121 8532 17673 -1744 -186 -3045 C ATOM 1243 O SER A 262 -52.636-178.920 302.883 1.00104.25 O ANISOU 1243 O SER A 262 13315 8344 17952 -1634 -194 -2690 O ATOM 1244 CB SER A 262 -55.335-177.352 301.318 1.00 95.14 C ANISOU 1244 CB SER A 262 11875 8141 16131 -2066 -228 -3252 C ATOM 1245 OG SER A 262 -54.892-176.272 302.122 1.00 92.33 O ANISOU 1245 OG SER A 262 11586 7980 15513 -1883 -260 -2868 O ATOM 1246 N VAL A 263 -52.701-178.475 300.670 1.00110.37 N ANISOU 1246 N VAL A 263 13934 9617 18384 -1614 -177 -3399 N ATOM 1247 CA VAL A 263 -51.251-178.454 300.529 1.00114.72 C ANISOU 1247 CA VAL A 263 14529 10073 18987 -1340 -167 -3402 C ATOM 1248 C VAL A 263 -50.675-177.280 301.310 1.00115.89 C ANISOU 1248 C VAL A 263 14726 10328 18979 -1191 -212 -3108 C ATOM 1249 O VAL A 263 -51.214-176.164 301.287 1.00110.18 O ANISOU 1249 O VAL A 263 13970 9961 17933 -1238 -242 -3071 O ATOM 1250 CB VAL A 263 -50.855-178.391 299.043 1.00115.60 C ANISOU 1250 CB VAL A 263 14546 10456 18922 -1263 -135 -3850 C ATOM 1251 CG1 VAL A 263 -51.284-179.662 298.330 1.00118.54 C ANISOU 1251 CG1 VAL A 263 14869 10674 19496 -1389 -92 -4142 C ATOM 1252 CG2 VAL A 263 -51.470-177.172 298.368 1.00113.26 C ANISOU 1252 CG2 VAL A 263 14168 10663 18204 -1326 -163 -4012 C ATOM 1253 N CYS A 264 -49.579-177.531 302.019 1.00123.70 N ANISOU 1253 N CYS A 264 15788 11058 20152 -995 -219 -2864 N ATOM 1254 CA CYS A 264 -48.919-176.513 302.819 1.00126.29 C ANISOU 1254 CA CYS A 264 16160 11478 20346 -837 -267 -2565 C ATOM 1255 C CYS A 264 -47.770-175.887 302.038 1.00121.03 C ANISOU 1255 C CYS A 264 15453 11027 19507 -618 -254 -2769 C ATOM 1256 O CYS A 264 -47.150-176.526 301.184 1.00124.13 O ANISOU 1256 O CYS A 264 15801 11360 20002 -536 -208 -3052 O ATOM 1257 CB CYS A 264 -48.389-177.097 304.134 1.00133.01 C ANISOU 1257 CB CYS A 264 17099 11959 21480 -749 -296 -2147 C ATOM 1258 SG CYS A 264 -49.614-177.914 305.189 1.00138.85 S ANISOU 1258 SG CYS A 264 17895 12437 22425 -1003 -295 -1824 S ATOM 1259 N SER A 265 -47.506-174.616 302.332 1.00109.02 N ANISOU 1259 N SER A 265 13940 9868 17615 -521 -281 -2557 N ATOM 1260 CA SER A 265 -46.350-173.938 301.766 1.00100.43 C ANISOU 1260 CA SER A 265 12815 8983 16360 -322 -264 -2674 C ATOM 1261 C SER A 265 -45.064-174.616 302.223 1.00 97.66 C ANISOU 1261 C SER A 265 12477 8290 16339 -126 -269 -2601 C ATOM 1262 O SER A 265 -44.964-175.098 303.354 1.00100.59 O ANISOU 1262 O SER A 265 12910 8378 16931 -98 -314 -2278 O ATOM 1263 CB SER A 265 -46.349-172.466 302.186 1.00 94.01 C ANISOU 1263 CB SER A 265 12021 8560 15138 -275 -295 -2412 C ATOM 1264 OG SER A 265 -45.081-171.866 301.981 1.00 92.23 O ANISOU 1264 OG SER A 265 11771 8457 14816 -83 -281 -2425 O ATOM 1265 N ASP A 266 -44.082-174.670 301.326 1.00 93.67 N ANISOU 1265 N ASP A 266 11902 7828 15860 16 -223 -2899 N ATOM 1266 CA ASP A 266 -42.756-175.151 301.686 1.00 95.88 C ANISOU 1266 CA ASP A 266 12164 7888 16378 237 -227 -2823 C ATOM 1267 C ASP A 266 -41.865-174.045 302.229 1.00 93.34 C ANISOU 1267 C ASP A 266 11832 7794 15839 390 -262 -2588 C ATOM 1268 O ASP A 266 -40.878-174.337 302.913 1.00 97.11 O ANISOU 1268 O ASP A 266 12298 8085 16514 566 -298 -2416 O ATOM 1269 CB ASP A 266 -42.080-175.804 300.476 1.00101.66 C ANISOU 1269 CB ASP A 266 12802 8664 17161 314 -148 -3202 C ATOM 1270 CG ASP A 266 -42.767-177.086 300.044 1.00107.82 C ANISOU 1270 CG ASP A 266 13587 9228 18153 186 -116 -3377 C ATOM 1271 OD1 ASP A 266 -42.899-178.004 300.880 1.00111.47 O ANISOU 1271 OD1 ASP A 266 14114 9330 18910 179 -147 -3152 O ATOM 1272 OD2 ASP A 266 -43.185-177.171 298.871 1.00109.29 O ANISOU 1272 OD2 ASP A 266 13708 9614 18203 88 -60 -3735 O ATOM 1273 N ILE A 267 -42.194-172.791 301.942 1.00 85.81 N ANISOU 1273 N ILE A 267 10874 7263 14465 325 -252 -2559 N ATOM 1274 CA ILE A 267 -41.443-171.651 302.455 1.00 80.45 C ANISOU 1274 CA ILE A 267 10188 6835 13545 434 -277 -2328 C ATOM 1275 C ILE A 267 -41.936-171.241 303.836 1.00 77.16 C ANISOU 1275 C ILE A 267 9853 6412 13052 388 -358 -1906 C ATOM 1276 O ILE A 267 -41.142-171.047 304.760 1.00 79.10 O ANISOU 1276 O ILE A 267 10097 6621 13335 512 -410 -1658 O ATOM 1277 CB ILE A 267 -41.537-170.477 301.461 1.00 76.53 C ANISOU 1277 CB ILE A 267 9653 6769 12655 389 -221 -2491 C ATOM 1278 CG1 ILE A 267 -40.766-170.789 300.179 1.00 80.04 C ANISOU 1278 CG1 ILE A 267 9997 7280 13136 464 -134 -2882 C ATOM 1279 CG2 ILE A 267 -41.027-169.204 302.103 1.00 72.98 C ANISOU 1279 CG2 ILE A 267 9215 6557 11956 449 -248 -2222 C ATOM 1280 CD1 ILE A 267 -40.907-169.716 299.128 1.00 79.21 C ANISOU 1280 CD1 ILE A 267 9854 7604 12637 408 -72 -3025 C ATOM 1281 N PHE A 268 -43.249-171.105 303.987 1.00 75.07 N ANISOU 1281 N PHE A 268 9643 6212 12668 210 -367 -1835 N ATOM 1282 CA PHE A 268 -43.855-170.646 305.220 1.00 72.20 C ANISOU 1282 CA PHE A 268 9344 5902 12186 147 -427 -1470 C ATOM 1283 C PHE A 268 -44.542-171.793 305.929 1.00 71.05 C ANISOU 1283 C PHE A 268 9248 5425 12322 51 -453 -1319 C ATOM 1284 O PHE A 268 -45.387-172.477 305.331 1.00 72.18 O ANISOU 1284 O PHE A 268 9389 5449 12586 -92 -418 -1512 O ATOM 1285 CB PHE A 268 -44.867-169.537 304.956 1.00 71.08 C ANISOU 1285 CB PHE A 268 9213 6108 11684 23 -415 -1471 C ATOM 1286 CG PHE A 268 -44.259-168.292 304.404 1.00 70.15 C ANISOU 1286 CG PHE A 268 9065 6305 11284 104 -389 -1542 C ATOM 1287 CD1 PHE A 268 -43.700-167.350 305.246 1.00 69.47 C ANISOU 1287 CD1 PHE A 268 8993 6351 11050 184 -424 -1309 C ATOM 1288 CD2 PHE A 268 -44.246-168.061 303.040 1.00 70.94 C ANISOU 1288 CD2 PHE A 268 9115 6575 11263 91 -328 -1844 C ATOM 1289 CE1 PHE A 268 -43.135-166.202 304.740 1.00 68.27 C ANISOU 1289 CE1 PHE A 268 8815 6456 10668 239 -392 -1368 C ATOM 1290 CE2 PHE A 268 -43.683-166.915 302.527 1.00 70.49 C ANISOU 1290 CE2 PHE A 268 9034 6797 10952 154 -296 -1875 C ATOM 1291 CZ PHE A 268 -43.126-165.983 303.378 1.00 69.12 C ANISOU 1291 CZ PHE A 268 8883 6714 10666 223 -324 -1634 C ATOM 1292 N PRO A 269 -44.220-172.030 307.191 1.00 65.12 N ANISOU 1292 N PRO A 269 8535 4532 11674 112 -513 -974 N ATOM 1293 CA PRO A 269 -44.931-173.051 307.954 1.00 64.80 C ANISOU 1293 CA PRO A 269 8548 4194 11877 2 -532 -765 C ATOM 1294 C PRO A 269 -46.411-172.703 308.101 1.00 62.30 C ANISOU 1294 C PRO A 269 8254 4054 11363 -223 -512 -711 C ATOM 1295 O PRO A 269 -46.780-171.546 308.323 1.00 59.06 O ANISOU 1295 O PRO A 269 7838 3995 10607 -247 -521 -635 O ATOM 1296 CB PRO A 269 -44.204-173.043 309.302 1.00 62.55 C ANISOU 1296 CB PRO A 269 8287 3855 11622 134 -608 -371 C ATOM 1297 CG PRO A 269 -42.853-172.534 308.999 1.00 62.14 C ANISOU 1297 CG PRO A 269 8175 3915 11520 344 -626 -476 C ATOM 1298 CD PRO A 269 -43.036-171.525 307.910 1.00 63.34 C ANISOU 1298 CD PRO A 269 8290 4386 11390 298 -566 -778 C ATOM 1299 N HIS A 270 -47.255-173.734 307.968 1.00 67.66 N ANISOU 1299 N HIS A 270 8948 4474 12287 -388 -483 -763 N ATOM 1300 CA HIS A 270 -48.686-173.702 308.301 1.00 66.05 C ANISOU 1300 CA HIS A 270 8750 4368 11977 -619 -464 -666 C ATOM 1301 C HIS A 270 -49.511-172.856 307.338 1.00 64.68 C ANISOU 1301 C HIS A 270 8518 4553 11505 -718 -434 -943 C ATOM 1302 O HIS A 270 -50.639-172.464 307.673 1.00 63.79 O ANISOU 1302 O HIS A 270 8388 4640 11211 -870 -428 -847 O ATOM 1303 CB HIS A 270 -48.944-173.205 309.728 1.00 64.29 C ANISOU 1303 CB HIS A 270 8562 4293 11572 -632 -503 -239 C ATOM 1304 CG HIS A 270 -48.005-173.768 310.751 1.00 68.52 C ANISOU 1304 CG HIS A 270 9145 4588 12302 -494 -553 83 C ATOM 1305 ND1 HIS A 270 -48.424-174.593 311.770 1.00 73.63 N ANISOU 1305 ND1 HIS A 270 9837 5014 13125 -591 -561 420 N ATOM 1306 CD2 HIS A 270 -46.670-173.628 310.936 1.00 71.00 C ANISOU 1306 CD2 HIS A 270 9457 4865 12654 -264 -603 139 C ATOM 1307 CE1 HIS A 270 -47.411-174.901 312.554 1.00 76.39 C ANISOU 1307 CE1 HIS A 270 10216 5218 13592 -416 -622 687 C ATOM 1308 NE2 HIS A 270 -46.322-174.348 312.050 1.00 75.56 N ANISOU 1308 NE2 HIS A 270 10075 5216 13417 -212 -651 506 N ATOM 1309 N ILE A 271 -49.021-172.569 306.134 1.00 65.77 N ANISOU 1309 N ILE A 271 8614 4798 11579 -636 -414 -1281 N ATOM 1310 CA ILE A 271 -49.659-171.597 305.251 1.00 68.09 C ANISOU 1310 CA ILE A 271 8852 5480 11538 -687 -399 -1488 C ATOM 1311 C ILE A 271 -50.244-172.332 304.050 1.00 71.18 C ANISOU 1311 C ILE A 271 9184 5813 12049 -820 -362 -1873 C ATOM 1312 O ILE A 271 -49.509-172.897 303.225 1.00 68.87 O ANISOU 1312 O ILE A 271 8870 5370 11925 -748 -335 -2148 O ATOM 1313 CB ILE A 271 -48.675-170.503 304.820 1.00 65.54 C ANISOU 1313 CB ILE A 271 8523 5407 10974 -501 -402 -1541 C ATOM 1314 CG1 ILE A 271 -48.353-169.613 306.009 1.00 63.82 C ANISOU 1314 CG1 ILE A 271 8348 5313 10587 -413 -441 -1193 C ATOM 1315 CG2 ILE A 271 -49.268-169.657 303.707 1.00 62.93 C ANISOU 1315 CG2 ILE A 271 8136 5435 10341 -544 -382 -1772 C ATOM 1316 CD1 ILE A 271 -49.538-168.828 306.525 1.00 61.75 C ANISOU 1316 CD1 ILE A 271 8083 5309 10071 -523 -453 -1040 C ATOM 1317 N ASP A 272 -51.577-172.305 303.947 1.00 75.65 N ANISOU 1317 N ASP A 272 9704 6524 12514 -1014 -359 -1913 N ATOM 1318 CA ASP A 272 -52.240-172.763 302.737 1.00 80.03 C ANISOU 1318 CA ASP A 272 10175 7142 13090 -1150 -336 -2304 C ATOM 1319 C ASP A 272 -51.727-171.978 301.536 1.00 81.71 C ANISOU 1319 C ASP A 272 10342 7671 13034 -1025 -330 -2565 C ATOM 1320 O ASP A 272 -51.515-170.765 301.611 1.00 85.77 O ANISOU 1320 O ASP A 272 10869 8483 13239 -910 -347 -2419 O ATOM 1321 CB ASP A 272 -53.752-172.602 302.873 1.00 84.02 C ANISOU 1321 CB ASP A 272 10615 7852 13459 -1360 -346 -2274 C ATOM 1322 CG ASP A 272 -54.507-173.132 301.667 1.00 96.63 C ANISOU 1322 CG ASP A 272 12104 9533 15077 -1523 -334 -2689 C ATOM 1323 OD1 ASP A 272 -53.923-173.920 300.896 1.00104.97 O ANISOU 1323 OD1 ASP A 272 13151 10385 16347 -1509 -308 -2993 O ATOM 1324 OD2 ASP A 272 -55.690-172.768 301.499 1.00100.10 O ANISOU 1324 OD2 ASP A 272 12455 10258 15320 -1662 -353 -2725 O ATOM 1325 N LYS A 273 -51.518-172.681 300.423 1.00 81.98 N ANISOU 1325 N LYS A 273 10321 7637 13192 -1052 -299 -2957 N ATOM 1326 CA LYS A 273 -50.936-172.033 299.253 1.00 81.96 C ANISOU 1326 CA LYS A 273 10270 7939 12933 -935 -281 -3204 C ATOM 1327 C LYS A 273 -51.889-171.020 298.631 1.00 80.59 C ANISOU 1327 C LYS A 273 10028 8244 12349 -995 -309 -3244 C ATOM 1328 O LYS A 273 -51.438-170.025 298.054 1.00 83.13 O ANISOU 1328 O LYS A 273 10341 8873 12373 -870 -304 -3247 O ATOM 1329 CB LYS A 273 -50.519-173.082 298.223 1.00 88.33 C ANISOU 1329 CB LYS A 273 11019 8580 13963 -956 -235 -3643 C ATOM 1330 CG LYS A 273 -49.376-173.974 298.685 1.00 92.90 C ANISOU 1330 CG LYS A 273 11654 8703 14941 -834 -206 -3624 C ATOM 1331 CD LYS A 273 -48.698-174.666 297.514 1.00 96.51 C ANISOU 1331 CD LYS A 273 12042 9116 15511 -778 -147 -4062 C ATOM 1332 CE LYS A 273 -47.541-175.536 297.982 1.00 98.09 C ANISOU 1332 CE LYS A 273 12286 8933 16050 -613 -120 -3958 C ATOM 1333 NZ LYS A 273 -46.831-176.182 296.843 1.00101.45 N ANISOU 1333 NZ LYS A 273 12629 9412 16503 -527 -53 -4300 N ATOM 1334 N THR A 274 -53.201-171.244 298.744 1.00 78.65 N ANISOU 1334 N THR A 274 9726 8069 12087 -1181 -337 -3260 N ATOM 1335 CA THR A 274 -54.156-170.324 298.134 1.00 77.26 C ANISOU 1335 CA THR A 274 9465 8356 11533 -1222 -375 -3302 C ATOM 1336 C THR A 274 -54.138-168.967 298.826 1.00 77.29 C ANISOU 1336 C THR A 274 9525 8568 11275 -1091 -401 -2934 C ATOM 1337 O THR A 274 -54.245-167.926 298.166 1.00 76.36 O ANISOU 1337 O THR A 274 9374 8813 10826 -1006 -419 -2938 O ATOM 1338 CB THR A 274 -55.560-170.927 298.160 1.00 75.87 C ANISOU 1338 CB THR A 274 9194 8207 11426 -1456 -400 -3410 C ATOM 1339 OG1 THR A 274 -55.552-172.178 297.465 1.00 77.45 O ANISOU 1339 OG1 THR A 274 9339 8200 11887 -1589 -373 -3792 O ATOM 1340 CG2 THR A 274 -56.555-169.993 297.488 1.00 76.79 C ANISOU 1340 CG2 THR A 274 9199 8828 11150 -1477 -452 -3460 C ATOM 1341 N TYR A 275 -54.003-168.954 300.155 1.00 77.34 N ANISOU 1341 N TYR A 275 9614 8349 11424 -1073 -402 -2613 N ATOM 1342 CA TYR A 275 -53.845-167.684 300.856 1.00 75.39 C ANISOU 1342 CA TYR A 275 9422 8270 10954 -941 -420 -2300 C ATOM 1343 C TYR A 275 -52.583-166.964 300.403 1.00 76.09 C ANISOU 1343 C TYR A 275 9560 8427 10922 -752 -399 -2301 C ATOM 1344 O TYR A 275 -52.594-165.744 300.201 1.00 78.59 O ANISOU 1344 O TYR A 275 9882 9017 10961 -656 -410 -2197 O ATOM 1345 CB TYR A 275 -53.819-167.906 302.367 1.00 75.93 C ANISOU 1345 CB TYR A 275 9561 8095 11195 -959 -422 -1984 C ATOM 1346 CG TYR A 275 -53.384-166.679 303.136 1.00 74.75 C ANISOU 1346 CG TYR A 275 9474 8074 10855 -809 -435 -1704 C ATOM 1347 CD1 TYR A 275 -54.242-165.601 303.306 1.00 73.96 C ANISOU 1347 CD1 TYR A 275 9339 8272 10491 -798 -457 -1593 C ATOM 1348 CD2 TYR A 275 -52.112-166.597 303.687 1.00 75.39 C ANISOU 1348 CD2 TYR A 275 9636 7978 11030 -676 -427 -1569 C ATOM 1349 CE1 TYR A 275 -53.845-164.475 304.006 1.00 72.25 C ANISOU 1349 CE1 TYR A 275 9179 8149 10124 -666 -463 -1371 C ATOM 1350 CE2 TYR A 275 -51.705-165.475 304.386 1.00 74.33 C ANISOU 1350 CE2 TYR A 275 9548 7964 10729 -557 -439 -1348 C ATOM 1351 CZ TYR A 275 -52.576-164.418 304.544 1.00 72.37 C ANISOU 1351 CZ TYR A 275 9276 7988 10235 -557 -453 -1257 C ATOM 1352 OH TYR A 275 -52.173-163.303 305.242 1.00 69.14 O ANISOU 1352 OH TYR A 275 8912 7673 9684 -445 -460 -1069 O ATOM 1353 N LEU A 276 -51.481-167.703 300.239 1.00 74.57 N ANISOU 1353 N LEU A 276 9399 7983 10950 -697 -365 -2416 N ATOM 1354 CA LEU A 276 -50.250-167.085 299.760 1.00 72.44 C ANISOU 1354 CA LEU A 276 9153 7794 10576 -533 -333 -2440 C ATOM 1355 C LEU A 276 -50.441-166.484 298.375 1.00 75.74 C ANISOU 1355 C LEU A 276 9504 8574 10700 -522 -318 -2653 C ATOM 1356 O LEU A 276 -50.013-165.353 298.118 1.00 75.94 O ANISOU 1356 O LEU A 276 9549 8819 10487 -416 -307 -2541 O ATOM 1357 CB LEU A 276 -49.113-168.108 299.744 1.00 71.53 C ANISOU 1357 CB LEU A 276 9053 7358 10769 -475 -297 -2570 C ATOM 1358 CG LEU A 276 -47.776-167.596 299.203 1.00 70.55 C ANISOU 1358 CG LEU A 276 8925 7322 10559 -317 -252 -2632 C ATOM 1359 CD1 LEU A 276 -47.298-166.395 300.004 1.00 67.32 C ANISOU 1359 CD1 LEU A 276 8575 7009 9996 -215 -268 -2313 C ATOM 1360 CD2 LEU A 276 -46.727-168.698 299.203 1.00 71.52 C ANISOU 1360 CD2 LEU A 276 9038 7123 11014 -247 -220 -2782 C ATOM 1361 N MET A 277 -51.093-167.222 297.473 1.00 79.65 N ANISOU 1361 N MET A 277 9915 9143 11205 -638 -319 -2957 N ATOM 1362 CA MET A 277 -51.352-166.698 296.137 1.00 83.10 C ANISOU 1362 CA MET A 277 10273 9973 11327 -633 -315 -3157 C ATOM 1363 C MET A 277 -52.243-165.465 296.193 1.00 78.38 C ANISOU 1363 C MET A 277 9666 9697 10417 -615 -365 -2936 C ATOM 1364 O MET A 277 -52.054-164.515 295.423 1.00 78.50 O ANISOU 1364 O MET A 277 9668 10017 10141 -529 -357 -2910 O ATOM 1365 CB MET A 277 -51.986-167.778 295.261 1.00 92.41 C ANISOU 1365 CB MET A 277 11348 11182 12580 -780 -318 -3543 C ATOM 1366 CG MET A 277 -52.171-167.341 293.823 1.00102.51 C ANISOU 1366 CG MET A 277 12531 12903 13513 -774 -316 -3777 C ATOM 1367 SD MET A 277 -50.647-166.643 293.159 1.00109.58 S ANISOU 1367 SD MET A 277 13460 13934 14239 -593 -236 -3770 S ATOM 1368 CE MET A 277 -51.245-165.866 291.662 1.00113.31 C ANISOU 1368 CE MET A 277 13826 15004 14222 -599 -256 -3903 C ATOM 1369 N PHE A 278 -53.222-165.460 297.100 1.00 73.71 N ANISOU 1369 N PHE A 278 9078 9042 9887 -691 -412 -2767 N ATOM 1370 CA PHE A 278 -54.067-164.283 297.268 1.00 71.62 C ANISOU 1370 CA PHE A 278 8798 9054 9359 -649 -458 -2554 C ATOM 1371 C PHE A 278 -53.246-163.083 297.722 1.00 71.65 C ANISOU 1371 C PHE A 278 8900 9065 9258 -485 -437 -2281 C ATOM 1372 O PHE A 278 -53.390-161.979 297.185 1.00 69.78 O ANISOU 1372 O PHE A 278 8657 9099 8757 -397 -448 -2191 O ATOM 1373 CB PHE A 278 -55.186-164.580 298.265 1.00 70.72 C ANISOU 1373 CB PHE A 278 8657 8856 9358 -762 -496 -2435 C ATOM 1374 CG PHE A 278 -55.904-163.355 298.746 1.00 67.75 C ANISOU 1374 CG PHE A 278 8276 8695 8771 -687 -533 -2185 C ATOM 1375 CD1 PHE A 278 -56.690-162.615 297.879 1.00 66.07 C ANISOU 1375 CD1 PHE A 278 7975 8853 8277 -650 -578 -2226 C ATOM 1376 CD2 PHE A 278 -55.795-162.943 300.064 1.00 65.76 C ANISOU 1376 CD2 PHE A 278 8100 8284 8601 -643 -525 -1916 C ATOM 1377 CE1 PHE A 278 -57.352-161.485 298.317 1.00 63.95 C ANISOU 1377 CE1 PHE A 278 7697 8757 7844 -558 -612 -2003 C ATOM 1378 CE2 PHE A 278 -56.455-161.815 300.509 1.00 64.65 C ANISOU 1378 CE2 PHE A 278 7948 8331 8284 -565 -552 -1721 C ATOM 1379 CZ PHE A 278 -57.235-161.085 299.634 1.00 63.66 C ANISOU 1379 CZ PHE A 278 7737 8539 7911 -516 -594 -1765 C ATOM 1380 N TRP A 279 -52.368-163.286 298.706 1.00 73.67 N ANISOU 1380 N TRP A 279 9244 9022 9727 -445 -409 -2145 N ATOM 1381 CA TRP A 279 -51.581-162.176 299.231 1.00 72.46 C ANISOU 1381 CA TRP A 279 9173 8864 9496 -312 -390 -1908 C ATOM 1382 C TRP A 279 -50.627-161.620 298.182 1.00 72.57 C ANISOU 1382 C TRP A 279 9190 9025 9358 -223 -342 -1984 C ATOM 1383 O TRP A 279 -50.376-160.409 298.145 1.00 71.89 O ANISOU 1383 O TRP A 279 9144 9068 9103 -133 -331 -1813 O ATOM 1384 CB TRP A 279 -50.808-162.616 300.471 1.00 70.39 C ANISOU 1384 CB TRP A 279 8980 8282 9484 -294 -381 -1772 C ATOM 1385 CG TRP A 279 -49.989-161.517 301.052 1.00 67.46 C ANISOU 1385 CG TRP A 279 8677 7913 9043 -177 -367 -1563 C ATOM 1386 CD1 TRP A 279 -50.391-160.600 301.977 1.00 67.31 C ANISOU 1386 CD1 TRP A 279 8694 7937 8944 -144 -391 -1343 C ATOM 1387 CD2 TRP A 279 -48.629-161.201 300.737 1.00 66.99 C ANISOU 1387 CD2 TRP A 279 8642 7819 8991 -87 -320 -1579 C ATOM 1388 NE1 TRP A 279 -49.363-159.736 302.264 1.00 67.06 N ANISOU 1388 NE1 TRP A 279 8715 7883 8881 -48 -366 -1230 N ATOM 1389 CE2 TRP A 279 -48.268-160.085 301.516 1.00 68.02 C ANISOU 1389 CE2 TRP A 279 8827 7961 9054 -17 -322 -1362 C ATOM 1390 CE3 TRP A 279 -47.677-161.757 299.875 1.00 67.37 C ANISOU 1390 CE3 TRP A 279 8659 7838 9100 -64 -270 -1774 C ATOM 1391 CZ2 TRP A 279 -46.999-159.514 301.461 1.00 68.24 C ANISOU 1391 CZ2 TRP A 279 8877 7969 9080 59 -279 -1325 C ATOM 1392 CZ3 TRP A 279 -46.418-161.188 299.820 1.00 68.06 C ANISOU 1392 CZ3 TRP A 279 8762 7923 9173 23 -224 -1728 C ATOM 1393 CH2 TRP A 279 -46.091-160.078 300.608 1.00 67.98 C ANISOU 1393 CH2 TRP A 279 8805 7921 9102 76 -230 -1501 C ATOM 1394 N ILE A 280 -50.078-162.486 297.328 1.00 72.29 N ANISOU 1394 N ILE A 280 9110 8968 9389 -250 -304 -2244 N ATOM 1395 CA ILE A 280 -49.198-162.014 296.261 1.00 72.59 C ANISOU 1395 CA ILE A 280 9132 9191 9257 -180 -245 -2333 C ATOM 1396 C ILE A 280 -49.959-161.088 295.321 1.00 70.84 C ANISOU 1396 C ILE A 280 8872 9346 8697 -167 -265 -2300 C ATOM 1397 O ILE A 280 -49.477-160.009 294.958 1.00 71.68 O ANISOU 1397 O ILE A 280 9011 9606 8618 -85 -231 -2150 O ATOM 1398 CB ILE A 280 -48.582-163.203 295.503 1.00 75.16 C ANISOU 1398 CB ILE A 280 9396 9447 9714 -214 -197 -2665 C ATOM 1399 CG1 ILE A 280 -47.638-163.989 296.412 1.00 76.61 C ANISOU 1399 CG1 ILE A 280 9620 9250 10238 -181 -176 -2654 C ATOM 1400 CG2 ILE A 280 -47.846-162.722 294.262 1.00 74.43 C ANISOU 1400 CG2 ILE A 280 9262 9632 9388 -160 -127 -2782 C ATOM 1401 CD1 ILE A 280 -47.099-165.248 295.778 1.00 80.53 C ANISOU 1401 CD1 ILE A 280 10054 9617 10928 -200 -132 -2991 C ATOM 1402 N GLY A 281 -51.169-161.492 294.928 1.00 67.95 N ANISOU 1402 N GLY A 281 8431 9135 8253 -251 -323 -2425 N ATOM 1403 CA GLY A 281 -51.929-160.704 293.972 1.00 67.64 C ANISOU 1403 CA GLY A 281 8333 9484 7882 -227 -358 -2401 C ATOM 1404 C GLY A 281 -52.270-159.319 294.483 1.00 68.23 C ANISOU 1404 C GLY A 281 8469 9625 7830 -126 -386 -2063 C ATOM 1405 O GLY A 281 -52.288-158.351 293.717 1.00 72.96 O ANISOU 1405 O GLY A 281 9066 10484 8173 -48 -382 -1950 O ATOM 1406 N VAL A 282 -52.543-159.201 295.783 1.00 64.62 N ANISOU 1406 N VAL A 282 8067 8934 7551 -124 -409 -1896 N ATOM 1407 CA VAL A 282 -52.845-157.896 296.362 1.00 62.32 C ANISOU 1407 CA VAL A 282 7832 8673 7174 -23 -429 -1609 C ATOM 1408 C VAL A 282 -51.622-156.990 296.296 1.00 62.73 C ANISOU 1408 C VAL A 282 7975 8665 7195 69 -360 -1460 C ATOM 1409 O VAL A 282 -51.701-155.841 295.847 1.00 64.71 O ANISOU 1409 O VAL A 282 8250 9074 7264 155 -355 -1293 O ATOM 1410 CB VAL A 282 -53.353-158.055 297.806 1.00 58.50 C ANISOU 1410 CB VAL A 282 7374 7972 6881 -52 -459 -1500 C ATOM 1411 CG1 VAL A 282 -53.600-156.693 298.434 1.00 55.59 C ANISOU 1411 CG1 VAL A 282 7059 7622 6439 60 -469 -1244 C ATOM 1412 CG2 VAL A 282 -54.622-158.894 297.830 1.00 59.50 C ANISOU 1412 CG2 VAL A 282 7396 8179 7031 -164 -516 -1634 C ATOM 1413 N VAL A 283 -50.469-157.500 296.732 1.00 60.12 N ANISOU 1413 N VAL A 283 7687 8102 7053 50 -305 -1514 N ATOM 1414 CA VAL A 283 -49.250-156.700 296.739 1.00 59.45 C ANISOU 1414 CA VAL A 283 7669 7957 6963 114 -235 -1391 C ATOM 1415 C VAL A 283 -48.757-156.439 295.320 1.00 61.26 C ANISOU 1415 C VAL A 283 7864 8432 6979 129 -177 -1461 C ATOM 1416 O VAL A 283 -48.193-155.374 295.038 1.00 59.71 O ANISOU 1416 O VAL A 283 7713 8298 6676 182 -125 -1292 O ATOM 1417 CB VAL A 283 -48.182-157.397 297.602 1.00 61.31 C ANISOU 1417 CB VAL A 283 7931 7908 7456 96 -204 -1441 C ATOM 1418 CG1 VAL A 283 -46.871-156.637 297.558 1.00 61.77 C ANISOU 1418 CG1 VAL A 283 8029 7929 7513 146 -130 -1348 C ATOM 1419 CG2 VAL A 283 -48.673-157.526 299.036 1.00 61.42 C ANISOU 1419 CG2 VAL A 283 7981 7723 7634 84 -260 -1325 C ATOM 1420 N SER A 284 -48.966-157.385 294.402 1.00 64.88 N ANISOU 1420 N SER A 284 8238 9044 7369 72 -178 -1712 N ATOM 1421 CA SER A 284 -48.509-157.193 293.028 1.00 67.25 C ANISOU 1421 CA SER A 284 8490 9630 7431 80 -117 -1798 C ATOM 1422 C SER A 284 -49.293-156.086 292.336 1.00 69.22 C ANISOU 1422 C SER A 284 8739 10177 7385 135 -151 -1602 C ATOM 1423 O SER A 284 -48.741-155.344 291.514 1.00 69.53 O ANISOU 1423 O SER A 284 8788 10405 7227 170 -88 -1495 O ATOM 1424 CB SER A 284 -48.626-158.503 292.252 1.00 67.82 C ANISOU 1424 CB SER A 284 8461 9808 7501 4 -116 -2154 C ATOM 1425 OG SER A 284 -47.922-159.543 292.906 1.00 68.23 O ANISOU 1425 OG SER A 284 8517 9548 7860 -27 -88 -2318 O ATOM 1426 N VAL A 285 -50.583-155.963 292.652 1.00 69.78 N ANISOU 1426 N VAL A 285 8790 10299 7425 145 -249 -1540 N ATOM 1427 CA VAL A 285 -51.397-154.916 292.045 1.00 73.42 C ANISOU 1427 CA VAL A 285 9239 11033 7623 225 -297 -1337 C ATOM 1428 C VAL A 285 -50.961-153.547 292.551 1.00 74.07 C ANISOU 1428 C VAL A 285 9434 10971 7736 320 -259 -1011 C ATOM 1429 O VAL A 285 -50.803-152.600 291.770 1.00 77.29 O ANISOU 1429 O VAL A 285 9865 11560 7941 384 -230 -823 O ATOM 1430 CB VAL A 285 -52.890-155.178 292.312 1.00 73.90 C ANISOU 1430 CB VAL A 285 9224 11188 7666 218 -413 -1375 C ATOM 1431 CG1 VAL A 285 -53.681-153.876 292.288 1.00 75.95 C ANISOU 1431 CG1 VAL A 285 9501 11581 7776 348 -468 -1082 C ATOM 1432 CG2 VAL A 285 -53.441-156.152 291.283 1.00 73.50 C ANISOU 1432 CG2 VAL A 285 9038 11432 7455 134 -455 -1666 C ATOM 1433 N LEU A 286 -50.756-153.423 293.865 1.00 69.66 N ANISOU 1433 N LEU A 286 8947 10087 7433 324 -257 -940 N ATOM 1434 CA LEU A 286 -50.244-152.175 294.423 1.00 67.05 C ANISOU 1434 CA LEU A 286 8721 9587 7168 395 -214 -682 C ATOM 1435 C LEU A 286 -48.905-151.811 293.797 1.00 68.38 C ANISOU 1435 C LEU A 286 8926 9767 7290 375 -103 -638 C ATOM 1436 O LEU A 286 -48.695-150.671 293.367 1.00 70.91 O ANISOU 1436 O LEU A 286 9298 10142 7502 429 -61 -410 O ATOM 1437 CB LEU A 286 -50.106-152.294 295.943 1.00 63.45 C ANISOU 1437 CB LEU A 286 8315 8812 6981 382 -226 -675 C ATOM 1438 CG LEU A 286 -51.329-152.708 296.765 1.00 61.97 C ANISOU 1438 CG LEU A 286 8087 8591 6867 380 -315 -716 C ATOM 1439 CD1 LEU A 286 -51.005-152.673 298.253 1.00 59.08 C ANISOU 1439 CD1 LEU A 286 7778 7941 6729 369 -310 -675 C ATOM 1440 CD2 LEU A 286 -52.527-151.825 296.447 1.00 61.58 C ANISOU 1440 CD2 LEU A 286 8013 8724 6662 480 -377 -568 C ATOM 1441 N LEU A 287 -47.990-152.780 293.723 1.00 67.62 N ANISOU 1441 N LEU A 287 8793 9618 7282 299 -48 -851 N ATOM 1442 CA LEU A 287 -46.643-152.497 293.238 1.00 68.30 C ANISOU 1442 CA LEU A 287 8891 9714 7347 272 68 -833 C ATOM 1443 C LEU A 287 -46.640-152.150 291.756 1.00 71.79 C ANISOU 1443 C LEU A 287 9292 10507 7479 276 115 -790 C ATOM 1444 O LEU A 287 -45.881-151.276 291.322 1.00 73.14 O ANISOU 1444 O LEU A 287 9499 10722 7568 276 207 -614 O ATOM 1445 CB LEU A 287 -45.730-153.689 293.511 1.00 65.09 C ANISOU 1445 CB LEU A 287 8433 9179 7118 213 106 -1090 C ATOM 1446 CG LEU A 287 -45.368-153.899 294.979 1.00 63.25 C ANISOU 1446 CG LEU A 287 8244 8609 7179 212 79 -1078 C ATOM 1447 CD1 LEU A 287 -44.631-155.210 295.151 1.00 66.85 C ANISOU 1447 CD1 LEU A 287 8638 8954 7810 177 97 -1327 C ATOM 1448 CD2 LEU A 287 -44.529-152.737 295.484 1.00 60.47 C ANISOU 1448 CD2 LEU A 287 7958 8126 6891 225 138 -872 C ATOM 1449 N LEU A 288 -47.473-152.823 290.959 1.00 71.52 N ANISOU 1449 N LEU A 288 9174 10740 7259 270 57 -948 N ATOM 1450 CA LEU A 288 -47.492-152.531 289.530 1.00 73.58 C ANISOU 1450 CA LEU A 288 9382 11391 7182 274 95 -913 C ATOM 1451 C LEU A 288 -48.049-151.139 289.257 1.00 74.60 C ANISOU 1451 C LEU A 288 9576 11621 7148 362 70 -544 C ATOM 1452 O LEU A 288 -47.547-150.431 288.377 1.00 77.24 O ANISOU 1452 O LEU A 288 9922 12149 7275 368 150 -367 O ATOM 1453 CB LEU A 288 -48.289-153.596 288.775 1.00 74.14 C ANISOU 1453 CB LEU A 288 9334 11746 7091 239 26 -1201 C ATOM 1454 CG LEU A 288 -47.583-154.944 288.595 1.00 72.71 C ANISOU 1454 CG LEU A 288 9075 11536 7017 154 81 -1586 C ATOM 1455 CD1 LEU A 288 -48.252-155.772 287.509 1.00 74.58 C ANISOU 1455 CD1 LEU A 288 9184 12137 7017 110 37 -1870 C ATOM 1456 CD2 LEU A 288 -46.102-154.751 288.293 1.00 71.50 C ANISOU 1456 CD2 LEU A 288 8929 11367 6871 134 227 -1583 C ATOM 1457 N PHE A 289 -49.075-150.722 290.004 1.00 73.22 N ANISOU 1457 N PHE A 289 9439 11312 7068 436 -33 -415 N ATOM 1458 CA PHE A 289 -49.601-149.372 289.826 1.00 74.35 C ANISOU 1458 CA PHE A 289 9646 11497 7106 546 -59 -61 C ATOM 1459 C PHE A 289 -48.545-148.327 290.158 1.00 72.81 C ANISOU 1459 C PHE A 289 9565 11056 7043 542 53 174 C ATOM 1460 O PHE A 289 -48.359-147.357 289.414 1.00 74.37 O ANISOU 1460 O PHE A 289 9804 11372 7080 580 104 446 O ATOM 1461 CB PHE A 289 -50.845-149.154 290.687 1.00 74.13 C ANISOU 1461 CB PHE A 289 9623 11347 7196 635 -181 -5 C ATOM 1462 CG PHE A 289 -51.333-147.732 290.672 1.00 78.16 C ANISOU 1462 CG PHE A 289 10205 11821 7670 772 -204 350 C ATOM 1463 CD1 PHE A 289 -52.097-147.261 289.619 1.00 81.03 C ANISOU 1463 CD1 PHE A 289 10519 12520 7748 870 -265 524 C ATOM 1464 CD2 PHE A 289 -51.003-146.858 291.695 1.00 78.65 C ANISOU 1464 CD2 PHE A 289 10378 11516 7988 810 -166 507 C ATOM 1465 CE1 PHE A 289 -52.536-145.950 289.592 1.00 82.06 C ANISOU 1465 CE1 PHE A 289 10718 12588 7872 1017 -288 872 C ATOM 1466 CE2 PHE A 289 -51.437-145.548 291.673 1.00 80.11 C ANISOU 1466 CE2 PHE A 289 10632 11628 8177 943 -181 819 C ATOM 1467 CZ PHE A 289 -52.207-145.093 290.622 1.00 81.98 C ANISOU 1467 CZ PHE A 289 10827 12169 8152 1055 -241 1013 C ATOM 1468 N ILE A 290 -47.855-148.502 291.290 1.00 68.94 N ANISOU 1468 N ILE A 290 9122 10224 6847 491 91 83 N ATOM 1469 CA ILE A 290 -46.749-147.615 291.644 1.00 68.68 C ANISOU 1469 CA ILE A 290 9175 9961 6958 457 200 250 C ATOM 1470 C ILE A 290 -45.740-147.552 290.506 1.00 72.62 C ANISOU 1470 C ILE A 290 9644 10678 7271 382 326 282 C ATOM 1471 O ILE A 290 -45.227-146.479 290.165 1.00 73.49 O ANISOU 1471 O ILE A 290 9817 10758 7347 373 413 546 O ATOM 1472 CB ILE A 290 -46.089-148.082 292.956 1.00 64.16 C ANISOU 1472 CB ILE A 290 8618 9067 6691 400 210 81 C ATOM 1473 CG1 ILE A 290 -47.095-148.040 294.106 1.00 63.67 C ANISOU 1473 CG1 ILE A 290 8586 8818 6788 467 99 76 C ATOM 1474 CG2 ILE A 290 -44.870-147.231 293.280 1.00 62.50 C ANISOU 1474 CG2 ILE A 290 8470 8653 6624 342 323 210 C ATOM 1475 CD1 ILE A 290 -46.567-148.648 295.388 1.00 61.79 C ANISOU 1475 CD1 ILE A 290 8349 8322 6805 414 92 -90 C ATOM 1476 N VAL A 291 -45.446-148.701 289.897 1.00 74.72 N ANISOU 1476 N VAL A 291 9807 11166 7418 323 345 9 N ATOM 1477 CA VAL A 291 -44.561-148.719 288.738 1.00 78.24 C ANISOU 1477 CA VAL A 291 10198 11886 7644 256 470 5 C ATOM 1478 C VAL A 291 -45.198-147.970 287.573 1.00 80.77 C ANISOU 1478 C VAL A 291 10523 12539 7627 309 462 266 C ATOM 1479 O VAL A 291 -44.561-147.119 286.943 1.00 81.13 O ANISOU 1479 O VAL A 291 10602 12676 7550 278 573 513 O ATOM 1480 CB VAL A 291 -44.206-150.167 288.355 1.00 77.94 C ANISOU 1480 CB VAL A 291 10037 12013 7565 198 486 -389 C ATOM 1481 CG1 VAL A 291 -43.490-150.199 287.015 1.00 79.16 C ANISOU 1481 CG1 VAL A 291 10113 12540 7426 141 611 -417 C ATOM 1482 CG2 VAL A 291 -43.346-150.795 289.437 1.00 75.59 C ANISOU 1482 CG2 VAL A 291 9734 11383 7602 156 512 -585 C ATOM 1483 N TYR A 292 -46.467-148.266 287.280 1.00 80.92 N ANISOU 1483 N TYR A 292 10502 12754 7491 389 329 230 N ATOM 1484 CA TYR A 292 -47.149-147.595 286.176 1.00 83.94 C ANISOU 1484 CA TYR A 292 10871 13489 7532 461 297 486 C ATOM 1485 C TYR A 292 -47.195-146.089 286.392 1.00 84.81 C ANISOU 1485 C TYR A 292 11111 13398 7716 536 319 928 C ATOM 1486 O TYR A 292 -46.891-145.310 285.481 1.00 86.71 O ANISOU 1486 O TYR A 292 11375 13832 7738 538 395 1216 O ATOM 1487 CB TYR A 292 -48.565-148.148 286.007 1.00 82.69 C ANISOU 1487 CB TYR A 292 10633 13547 7238 540 131 359 C ATOM 1488 CG TYR A 292 -49.438-147.290 285.115 1.00 85.39 C ANISOU 1488 CG TYR A 292 10967 14205 7273 657 60 681 C ATOM 1489 CD1 TYR A 292 -49.379-147.408 283.733 1.00 87.87 C ANISOU 1489 CD1 TYR A 292 11194 15014 7178 638 85 702 C ATOM 1490 CD2 TYR A 292 -50.318-146.357 285.655 1.00 85.16 C ANISOU 1490 CD2 TYR A 292 11008 13994 7355 798 -33 963 C ATOM 1491 CE1 TYR A 292 -50.171-146.623 282.912 1.00 90.04 C ANISOU 1491 CE1 TYR A 292 11455 15603 7153 758 9 1027 C ATOM 1492 CE2 TYR A 292 -51.112-145.566 284.842 1.00 86.47 C ANISOU 1492 CE2 TYR A 292 11160 14441 7253 931 -107 1279 C ATOM 1493 CZ TYR A 292 -51.035-145.706 283.472 1.00 88.83 C ANISOU 1493 CZ TYR A 292 11375 15239 7138 912 -90 1325 C ATOM 1494 OH TYR A 292 -51.824-144.925 282.658 1.00 90.71 O ANISOU 1494 OH TYR A 292 11592 15781 7092 1056 -175 1667 O ATOM 1495 N ALA A 293 -47.577-145.661 287.598 1.00 82.17 N ANISOU 1495 N ALA A 293 10858 12671 7691 597 260 987 N ATOM 1496 CA ALA A 293 -47.729-144.236 287.872 1.00 81.64 C ANISOU 1496 CA ALA A 293 10914 12370 7737 682 272 1371 C ATOM 1497 C ALA A 293 -46.429-143.484 287.618 1.00 83.11 C ANISOU 1497 C ALA A 293 11170 12437 7972 577 443 1567 C ATOM 1498 O ALA A 293 -46.409-142.484 286.891 1.00 87.64 O ANISOU 1498 O ALA A 293 11801 13088 8412 612 492 1927 O ATOM 1499 CB ALA A 293 -48.202-144.029 289.311 1.00 77.68 C ANISOU 1499 CB ALA A 293 10472 11464 7579 743 199 1316 C ATOM 1500 N TYR A 294 -45.326-143.964 288.194 1.00 79.79 N ANISOU 1500 N TYR A 294 10737 11836 7744 445 535 1345 N ATOM 1501 CA TYR A 294 -44.065-143.240 288.075 1.00 81.62 C ANISOU 1501 CA TYR A 294 11016 11936 8058 327 700 1507 C ATOM 1502 C TYR A 294 -43.487-143.351 286.669 1.00 84.93 C ANISOU 1502 C TYR A 294 11368 12768 8135 250 814 1588 C ATOM 1503 O TYR A 294 -42.901-142.388 286.161 1.00 85.90 O ANISOU 1503 O TYR A 294 11544 12884 8208 191 935 1899 O ATOM 1504 CB TYR A 294 -43.075-143.741 289.125 1.00 80.67 C ANISOU 1504 CB TYR A 294 10877 11540 8235 220 751 1236 C ATOM 1505 CG TYR A 294 -43.483-143.383 290.539 1.00 82.28 C ANISOU 1505 CG TYR A 294 11159 11339 8766 277 666 1212 C ATOM 1506 CD1 TYR A 294 -44.388-142.354 290.780 1.00 84.12 C ANISOU 1506 CD1 TYR A 294 11490 11408 9064 394 602 1470 C ATOM 1507 CD2 TYR A 294 -42.970-144.072 291.631 1.00 82.01 C ANISOU 1507 CD2 TYR A 294 11090 11101 8968 223 650 932 C ATOM 1508 CE1 TYR A 294 -44.768-142.019 292.067 1.00 83.11 C ANISOU 1508 CE1 TYR A 294 11419 10937 9220 448 534 1418 C ATOM 1509 CE2 TYR A 294 -43.345-143.744 292.924 1.00 81.43 C ANISOU 1509 CE2 TYR A 294 11079 10706 9157 270 575 905 C ATOM 1510 CZ TYR A 294 -44.244-142.718 293.135 1.00 82.00 C ANISOU 1510 CZ TYR A 294 11242 10633 9279 378 523 1133 C ATOM 1511 OH TYR A 294 -44.618-142.389 294.418 1.00 81.30 O ANISOU 1511 OH TYR A 294 11202 10250 9438 426 458 1077 O ATOM 1512 N MET A 295 -43.643-144.508 286.020 1.00 86.19 N ANISOU 1512 N MET A 295 11403 13291 8053 241 784 1307 N ATOM 1513 CA MET A 295 -43.249-144.612 284.617 1.00 89.42 C ANISOU 1513 CA MET A 295 11733 14161 8081 183 882 1370 C ATOM 1514 C MET A 295 -44.080-143.675 283.750 1.00 89.68 C ANISOU 1514 C MET A 295 11817 14420 7838 283 838 1782 C ATOM 1515 O MET A 295 -43.564-143.072 282.800 1.00 89.40 O ANISOU 1515 O MET A 295 11784 14615 7568 225 959 2054 O ATOM 1516 CB MET A 295 -43.384-146.056 284.132 1.00 92.18 C ANISOU 1516 CB MET A 295 11935 14848 8241 166 843 943 C ATOM 1517 CG MET A 295 -42.366-147.009 284.739 1.00 94.17 C ANISOU 1517 CG MET A 295 12120 14933 8729 70 914 562 C ATOM 1518 SD MET A 295 -40.722-146.856 284.015 1.00 99.95 S ANISOU 1518 SD MET A 295 12777 15845 9355 -83 1152 571 S ATOM 1519 CE MET A 295 -40.839-148.027 282.666 1.00103.61 C ANISOU 1519 CE MET A 295 13068 16899 9401 -95 1172 239 C ATOM 1520 N TYR A 296 -45.371-143.541 284.064 1.00 91.06 N ANISOU 1520 N TYR A 296 12023 14542 8034 436 667 1847 N ATOM 1521 CA TYR A 296 -46.211-142.570 283.371 1.00 95.03 C ANISOU 1521 CA TYR A 296 12575 15208 8323 567 605 2269 C ATOM 1522 C TYR A 296 -45.701-141.152 283.587 1.00 92.08 C ANISOU 1522 C TYR A 296 12350 14491 8146 558 709 2703 C ATOM 1523 O TYR A 296 -45.664-140.347 282.649 1.00 94.09 O ANISOU 1523 O TYR A 296 12639 14940 8169 577 765 3098 O ATOM 1524 CB TYR A 296 -47.658-142.702 283.851 1.00 97.66 C ANISOU 1524 CB TYR A 296 12897 15501 8708 741 401 2222 C ATOM 1525 CG TYR A 296 -48.585-141.612 283.359 1.00103.37 C ANISOU 1525 CG TYR A 296 13675 16309 9294 917 317 2671 C ATOM 1526 CD1 TYR A 296 -48.763-140.440 284.087 1.00105.20 C ANISOU 1526 CD1 TYR A 296 14045 16090 9835 1013 314 2976 C ATOM 1527 CD2 TYR A 296 -49.294-141.759 282.176 1.00108.74 C ANISOU 1527 CD2 TYR A 296 14257 17522 9538 998 233 2780 C ATOM 1528 CE1 TYR A 296 -49.608-139.443 283.642 1.00109.38 C ANISOU 1528 CE1 TYR A 296 14622 16668 10270 1198 234 3395 C ATOM 1529 CE2 TYR A 296 -50.145-140.768 281.724 1.00112.90 C ANISOU 1529 CE2 TYR A 296 14823 18136 9938 1182 144 3215 C ATOM 1530 CZ TYR A 296 -50.298-139.612 282.462 1.00113.52 C ANISOU 1530 CZ TYR A 296 15047 17730 10357 1289 145 3529 C ATOM 1531 OH TYR A 296 -51.143-138.623 282.017 1.00117.41 O ANISOU 1531 OH TYR A 296 15577 18281 10753 1496 54 3970 O ATOM 1532 N ILE A 297 -45.303-140.829 284.820 1.00 87.47 N ANISOU 1532 N ILE A 297 11852 13395 7987 523 736 2637 N ATOM 1533 CA ILE A 297 -44.844-139.479 285.133 1.00 87.16 C ANISOU 1533 CA ILE A 297 11954 12974 8191 501 832 3002 C ATOM 1534 C ILE A 297 -43.551-139.163 284.389 1.00 93.45 C ANISOU 1534 C ILE A 297 12745 13889 8875 314 1038 3158 C ATOM 1535 O ILE A 297 -43.372-138.053 283.873 1.00 98.16 O ANISOU 1535 O ILE A 297 13430 14424 9442 303 1123 3593 O ATOM 1536 CB ILE A 297 -44.683-139.318 286.656 1.00 82.68 C ANISOU 1536 CB ILE A 297 11454 11877 8085 489 811 2820 C ATOM 1537 CG1 ILE A 297 -46.049-139.371 287.345 1.00 81.08 C ANISOU 1537 CG1 ILE A 297 11265 11558 7986 685 624 2754 C ATOM 1538 CG2 ILE A 297 -43.964-138.020 286.989 1.00 83.90 C ANISOU 1538 CG2 ILE A 297 11735 11627 8517 413 938 3115 C ATOM 1539 CD1 ILE A 297 -45.973-139.463 288.854 1.00 76.47 C ANISOU 1539 CD1 ILE A 297 10716 10550 7791 672 591 2503 C ATOM 1540 N LEU A 298 -42.633-140.129 284.320 1.00 95.65 N ANISOU 1540 N LEU A 298 12911 14335 9096 166 1125 2813 N ATOM 1541 CA LEU A 298 -41.387-139.919 283.590 1.00 98.48 C ANISOU 1541 CA LEU A 298 13231 14861 9326 -18 1330 2922 C ATOM 1542 C LEU A 298 -41.654-139.693 282.107 1.00101.64 C ANISOU 1542 C LEU A 298 13598 15766 9257 4 1369 3222 C ATOM 1543 O LEU A 298 -41.140-138.740 281.510 1.00104.72 O ANISOU 1543 O LEU A 298 14044 16172 9572 -78 1508 3622 O ATOM 1544 CB LEU A 298 -40.453-141.111 283.796 1.00 97.68 C ANISOU 1544 CB LEU A 298 12991 14875 9249 -143 1398 2453 C ATOM 1545 CG LEU A 298 -40.035-141.365 285.245 1.00 96.49 C ANISOU 1545 CG LEU A 298 12858 14266 9537 -176 1368 2174 C ATOM 1546 CD1 LEU A 298 -39.247-142.659 285.370 1.00 94.89 C ANISOU 1546 CD1 LEU A 298 12506 14212 9336 -256 1408 1719 C ATOM 1547 CD2 LEU A 298 -39.236-140.187 285.778 1.00 98.06 C ANISOU 1547 CD2 LEU A 298 13152 14074 10034 -292 1489 2420 C ATOM 1548 N TRP A 299 -42.454-140.571 281.495 1.00104.50 N ANISOU 1548 N TRP A 299 13859 16558 9290 105 1248 3033 N ATOM 1549 CA TRP A 299 -42.873-140.378 280.110 1.00112.36 C ANISOU 1549 CA TRP A 299 14810 18084 9799 151 1250 3309 C ATOM 1550 C TRP A 299 -43.485-138.997 279.913 1.00115.16 C ANISOU 1550 C TRP A 299 15309 18278 10170 268 1215 3891 C ATOM 1551 O TRP A 299 -43.110-138.261 278.994 1.00121.68 O ANISOU 1551 O TRP A 299 16162 19309 10762 212 1334 4302 O ATOM 1552 CB TRP A 299 -43.871-141.473 279.715 1.00115.49 C ANISOU 1552 CB TRP A 299 15082 18890 9910 265 1079 2987 C ATOM 1553 CG TRP A 299 -44.418-141.379 278.307 1.00124.67 C ANISOU 1553 CG TRP A 299 16172 20666 10530 326 1048 3218 C ATOM 1554 CD1 TRP A 299 -45.131-140.346 277.765 1.00129.69 C ANISOU 1554 CD1 TRP A 299 16885 21399 10994 457 985 3738 C ATOM 1555 CD2 TRP A 299 -44.328-142.379 277.284 1.00129.21 C ANISOU 1555 CD2 TRP A 299 16574 21856 10663 270 1066 2921 C ATOM 1556 NE1 TRP A 299 -45.468-140.632 276.466 1.00134.06 N ANISOU 1556 NE1 TRP A 299 17321 22613 11005 482 959 3803 N ATOM 1557 CE2 TRP A 299 -44.991-141.874 276.147 1.00134.07 C ANISOU 1557 CE2 TRP A 299 17166 22954 10821 362 1011 3290 C ATOM 1558 CE3 TRP A 299 -43.746-143.648 277.216 1.00129.06 C ANISOU 1558 CE3 TRP A 299 16414 22026 10597 158 1124 2373 C ATOM 1559 CZ2 TRP A 299 -45.085-142.594 274.958 1.00137.87 C ANISOU 1559 CZ2 TRP A 299 17482 23959 10942 322 987 3031 C ATOM 1560 CZ3 TRP A 299 -43.841-144.360 276.034 1.00132.85 C ANISOU 1560 CZ3 TRP A 299 16734 23155 10586 132 1133 2177 C ATOM 1561 CH2 TRP A 299 -44.505-143.831 274.922 1.00136.98 C ANISOU 1561 CH2 TRP A 299 17233 24049 10763 206 1057 2485 C ATOM 1562 N LYS A 300 -44.438-138.633 280.776 1.00113.75 N ANISOU 1562 N LYS A 300 15218 17731 10272 435 1056 3937 N ATOM 1563 CA LYS A 300 -45.139-137.363 280.624 1.00116.00 C ANISOU 1563 CA LYS A 300 15632 17841 10603 589 1001 4466 C ATOM 1564 C LYS A 300 -44.179-136.184 280.721 1.00117.55 C ANISOU 1564 C LYS A 300 15962 17660 11042 459 1189 4844 C ATOM 1565 O LYS A 300 -44.261-135.242 279.926 1.00120.98 O ANISOU 1565 O LYS A 300 16468 18179 11321 494 1240 5359 O ATOM 1566 CB LYS A 300 -46.238-137.247 281.681 1.00114.93 C ANISOU 1566 CB LYS A 300 15549 17342 10779 784 814 4368 C ATOM 1567 CG LYS A 300 -47.261-136.151 281.419 1.00118.82 C ANISOU 1567 CG LYS A 300 16130 17752 11264 1011 706 4853 C ATOM 1568 CD LYS A 300 -48.369-136.631 280.492 1.00122.36 C ANISOU 1568 CD LYS A 300 16456 18777 11259 1179 538 4889 C ATOM 1569 CE LYS A 300 -49.468-135.586 280.359 1.00126.33 C ANISOU 1569 CE LYS A 300 17029 19178 11793 1443 404 5346 C ATOM 1570 NZ LYS A 300 -50.698-136.141 279.727 1.00128.36 N ANISOU 1570 NZ LYS A 300 17136 19938 11697 1616 198 5262 N ATOM 1571 N ALA A 301 -43.257-136.222 281.685 1.00115.74 N ANISOU 1571 N ALA A 301 15763 17020 11195 301 1294 4603 N ATOM 1572 CA ALA A 301 -42.314-135.120 281.845 1.00120.22 C ANISOU 1572 CA ALA A 301 16443 17207 12027 148 1476 4917 C ATOM 1573 C ALA A 301 -41.350-135.036 280.668 1.00122.42 C ANISOU 1573 C ALA A 301 16663 17878 11973 -42 1675 5134 C ATOM 1574 O ALA A 301 -40.966-133.937 280.250 1.00128.50 O ANISOU 1574 O ALA A 301 17533 18504 12788 -117 1805 5610 O ATOM 1575 CB ALA A 301 -41.546-135.272 283.158 1.00120.53 C ANISOU 1575 CB ALA A 301 16494 16779 12521 17 1527 4558 C ATOM 1576 N HIS A 302 -40.950-136.187 280.120 1.00119.51 N ANISOU 1576 N HIS A 302 16129 18003 11275 -124 1710 4790 N ATOM 1577 CA HIS A 302 -39.981-136.193 279.028 1.00124.87 C ANISOU 1577 CA HIS A 302 16724 19100 11620 -313 1914 4936 C ATOM 1578 C HIS A 302 -40.525-135.485 277.794 1.00132.59 C ANISOU 1578 C HIS A 302 17745 20438 12196 -233 1918 5489 C ATOM 1579 O HIS A 302 -39.793-134.752 277.119 1.00137.54 O ANISOU 1579 O HIS A 302 18404 21093 12762 -386 2086 5811 O ATOM 1580 CB HIS A 302 -39.585-137.629 278.686 1.00123.21 C ANISOU 1580 CB HIS A 302 16317 19361 11135 -378 1931 4409 C ATOM 1581 CG HIS A 302 -38.790-137.749 277.425 1.00127.60 C ANISOU 1581 CG HIS A 302 16758 20470 11254 -534 2122 4524 C ATOM 1582 ND1 HIS A 302 -37.478-137.332 277.327 1.00130.73 N ANISOU 1582 ND1 HIS A 302 17130 20798 11744 -770 2363 4626 N ATOM 1583 CD2 HIS A 302 -39.121-138.232 276.204 1.00132.04 C ANISOU 1583 CD2 HIS A 302 17208 21693 11267 -495 2113 4542 C ATOM 1584 CE1 HIS A 302 -37.037-137.557 276.104 1.00134.77 C ANISOU 1584 CE1 HIS A 302 17520 21904 11781 -867 2502 4710 C ATOM 1585 NE2 HIS A 302 -38.015-138.103 275.401 1.00135.85 N ANISOU 1585 NE2 HIS A 302 17612 22423 11580 -695 2328 4596 N ATOM 1586 N SER A 303 -41.806-135.694 277.480 1.00133.89 N ANISOU 1586 N SER A 303 17903 20833 12138 2 1707 5531 N ATOM 1587 CA SER A 303 -42.383-135.067 276.295 1.00141.85 C ANISOU 1587 CA SER A 303 18936 22068 12893 91 1630 5852 C ATOM 1588 C SER A 303 -42.383-133.548 276.414 1.00147.09 C ANISOU 1588 C SER A 303 19792 22214 13881 105 1667 6363 C ATOM 1589 O SER A 303 -42.031-132.843 275.460 1.00153.05 O ANISOU 1589 O SER A 303 20583 23071 14498 24 1754 6680 O ATOM 1590 CB SER A 303 -43.802-135.586 276.059 1.00144.28 C ANISOU 1590 CB SER A 303 19177 22656 12986 339 1371 5718 C ATOM 1591 OG SER A 303 -43.782-136.895 275.515 1.00144.97 O ANISOU 1591 OG SER A 303 19077 23305 12701 298 1345 5274 O ATOM 1592 N HIS A 304 -42.764-133.025 277.579 1.00145.71 N ANISOU 1592 N HIS A 304 19741 21472 14149 206 1604 6432 N ATOM 1593 CA HIS A 304 -42.844-131.584 277.775 1.00149.90 C ANISOU 1593 CA HIS A 304 20457 21455 15044 236 1622 6856 C ATOM 1594 C HIS A 304 -41.488-130.936 278.024 1.00151.58 C ANISOU 1594 C HIS A 304 20743 21316 15533 -44 1870 6982 C ATOM 1595 O HIS A 304 -41.414-129.704 278.074 1.00155.65 O ANISOU 1595 O HIS A 304 21412 21382 16344 -64 1909 7324 O ATOM 1596 CB HIS A 304 -43.782-131.266 278.943 1.00148.36 C ANISOU 1596 CB HIS A 304 20354 20772 15242 456 1461 6827 C ATOM 1597 CG HIS A 304 -45.166-131.811 278.772 1.00149.34 C ANISOU 1597 CG HIS A 304 20400 21204 15139 730 1214 6711 C ATOM 1598 ND1 HIS A 304 -46.023-131.371 277.787 1.00154.53 N ANISOU 1598 ND1 HIS A 304 21049 22105 15561 890 1081 6966 N ATOM 1599 CD2 HIS A 304 -45.845-132.754 279.467 1.00145.80 C ANISOU 1599 CD2 HIS A 304 19867 20861 14668 864 1077 6362 C ATOM 1600 CE1 HIS A 304 -47.168-132.024 277.878 1.00153.45 C ANISOU 1600 CE1 HIS A 304 20812 22218 15272 1103 873 6764 C ATOM 1601 NE2 HIS A 304 -47.086-132.869 278.889 1.00147.85 N ANISOU 1601 NE2 HIS A 304 20060 21428 14688 1088 866 6395 N ATOM 1602 N ALA A 305 -40.423-131.725 278.178 1.00145.38 N ANISOU 1602 N ALA A 305 19841 20726 14672 -264 2036 6698 N ATOM 1603 CA ALA A 305 -39.114-131.154 278.487 1.00140.78 C ANISOU 1603 CA ALA A 305 19296 19818 14374 -545 2273 6777 C ATOM 1604 C ALA A 305 -38.606-130.287 277.343 1.00143.19 C ANISOU 1604 C ALA A 305 19655 20223 14529 -684 2399 7148 C ATOM 1605 O ALA A 305 -38.245-129.120 277.543 1.00146.63 O ANISOU 1605 O ALA A 305 20236 20172 15307 -786 2484 7439 O ATOM 1606 CB ALA A 305 -38.118-132.270 278.805 1.00137.11 C ANISOU 1606 CB ALA A 305 18654 19624 13818 -735 2417 6372 C ATOM 1607 N VAL A 306 -38.570-130.838 276.134 1.00140.25 N ANISOU 1607 N VAL A 306 19165 20475 13649 -694 2413 7129 N ATOM 1608 CA VAL A 306 -38.056-130.138 274.963 1.00143.37 C ANISOU 1608 CA VAL A 306 19591 21048 13836 -828 2544 7470 C ATOM 1609 C VAL A 306 -39.226-129.545 274.192 1.00147.38 C ANISOU 1609 C VAL A 306 20186 21645 14165 -590 2359 7815 C ATOM 1610 O VAL A 306 -40.223-130.231 273.934 1.00147.47 O ANISOU 1610 O VAL A 306 20117 22007 13909 -370 2163 7664 O ATOM 1611 CB VAL A 306 -37.229-131.078 274.071 1.00142.34 C ANISOU 1611 CB VAL A 306 19261 21561 13261 -990 2689 7225 C ATOM 1612 CG1 VAL A 306 -36.829-130.370 272.787 1.00148.80 C ANISOU 1612 CG1 VAL A 306 20107 22610 13820 -1099 2810 7597 C ATOM 1613 CG2 VAL A 306 -36.001-131.566 274.822 1.00139.61 C ANISOU 1613 CG2 VAL A 306 18814 21111 13120 -1231 2884 6906 C ATOM 1614 N ALA A1002 -39.107-128.273 273.827 1.00151.56 N ANISOU 1614 N ALA A1002 20872 21860 14852 -637 2420 8269 N ATOM 1615 CA ALA A1002 -40.134-127.616 273.035 1.00134.40 C ANISOU 1615 CA ALA A1002 18779 19771 12518 -419 2261 8642 C ATOM 1616 C ALA A1002 -40.040-128.048 271.576 1.00174.72 C ANISOU 1616 C ALA A1002 23757 25586 17042 -448 2293 8712 C ATOM 1617 O ALA A1002 -38.958-128.343 271.060 1.00181.02 O ANISOU 1617 O ALA A1002 24468 26665 17644 -688 2499 8638 O ATOM 1618 CB ALA A1002 -40.009-126.097 273.147 1.00138.65 C ANISOU 1618 CB ALA A1002 19533 19710 13438 -462 2319 9102 C ATOM 1619 N LYS A1003 -41.192-128.086 270.912 1.00105.37 N ANISOU 1619 N LYS A1003 13852 13124 13060 706 13 2427 N ATOM 1620 CA LYS A1003 -41.295-128.537 269.531 1.00103.80 C ANISOU 1620 CA LYS A1003 13544 12508 13386 517 61 2364 C ATOM 1621 C LYS A1003 -41.655-127.364 268.630 1.00100.57 C ANISOU 1621 C LYS A1003 13074 12050 13086 381 58 1945 C ATOM 1622 O LYS A1003 -42.620-126.641 268.901 1.00101.99 O ANISOU 1622 O LYS A1003 13274 12384 13092 372 202 1853 O ATOM 1623 CB LYS A1003 -42.339-129.648 269.395 1.00104.69 C ANISOU 1623 CB LYS A1003 13640 12398 13741 403 316 2724 C ATOM 1624 N ALA A1004 -40.887-127.187 267.558 1.00 96.46 N ANISOU 1624 N ALA A1004 12475 11327 12848 309 -82 1724 N ATOM 1625 CA ALA A1004 -41.092-126.111 266.601 1.00 92.53 C ANISOU 1625 CA ALA A1004 11921 10760 12478 192 -91 1383 C ATOM 1626 C ALA A1004 -41.511-126.678 265.250 1.00 89.38 C ANISOU 1626 C ALA A1004 11445 10063 12452 61 7 1371 C ATOM 1627 O ALA A1004 -41.080-127.764 264.851 1.00 90.96 O ANISOU 1627 O ALA A1004 11639 10059 12862 74 -9 1507 O ATOM 1628 CB ALA A1004 -39.824-125.266 266.442 1.00 91.73 C ANISOU 1628 CB ALA A1004 11772 10718 12362 206 -334 1143 C ATOM 1629 N LEU A1005 -42.349-125.922 264.543 1.00 85.71 N ANISOU 1629 N LEU A1005 10939 9574 12054 -39 92 1190 N ATOM 1630 CA LEU A1005 -42.943-126.357 263.281 1.00 83.35 C ANISOU 1630 CA LEU A1005 10572 9056 12040 -165 159 1148 C ATOM 1631 C LEU A1005 -42.839-125.212 262.282 1.00 82.45 C ANISOU 1631 C LEU A1005 10410 8946 11973 -194 117 879 C ATOM 1632 O LEU A1005 -43.459-124.161 262.474 1.00 83.90 O ANISOU 1632 O LEU A1005 10592 9251 12037 -186 164 778 O ATOM 1633 CB LEU A1005 -44.398-126.784 263.491 1.00 82.74 C ANISOU 1633 CB LEU A1005 10449 8987 12002 -267 327 1313 C ATOM 1634 CG LEU A1005 -45.220-127.422 262.369 1.00 80.55 C ANISOU 1634 CG LEU A1005 10088 8501 12018 -442 356 1294 C ATOM 1635 CD1 LEU A1005 -45.986-126.366 261.596 1.00 78.90 C ANISOU 1635 CD1 LEU A1005 9777 8401 11801 -479 377 1096 C ATOM 1636 CD2 LEU A1005 -44.344-128.240 261.437 1.00 79.08 C ANISOU 1636 CD2 LEU A1005 9968 8037 12042 -444 236 1202 C ATOM 1637 N ILE A1006 -42.063-125.414 261.220 1.00 80.82 N ANISOU 1637 N ILE A1006 10169 8606 11932 -197 49 785 N ATOM 1638 CA ILE A1006 -41.819-124.389 260.210 1.00 78.99 C ANISOU 1638 CA ILE A1006 9884 8384 11743 -213 27 601 C ATOM 1639 C ILE A1006 -42.417-124.882 258.899 1.00 77.54 C ANISOU 1639 C ILE A1006 9677 8084 11701 -263 73 543 C ATOM 1640 O ILE A1006 -41.825-125.725 258.215 1.00 77.12 O ANISOU 1640 O ILE A1006 9639 7911 11752 -220 49 524 O ATOM 1641 CB ILE A1006 -40.328-124.075 260.045 1.00 79.19 C ANISOU 1641 CB ILE A1006 9854 8434 11800 -159 -75 563 C ATOM 1642 CG1 ILE A1006 -39.695-123.712 261.390 1.00 81.10 C ANISOU 1642 CG1 ILE A1006 10114 8809 11892 -128 -193 596 C ATOM 1643 CG2 ILE A1006 -40.133-122.945 259.042 1.00 77.51 C ANISOU 1643 CG2 ILE A1006 9577 8229 11645 -199 -63 444 C ATOM 1644 CD1 ILE A1006 -38.196-123.497 261.312 1.00 80.36 C ANISOU 1644 CD1 ILE A1006 9894 8771 11867 -105 -332 590 C ATOM 1645 N VAL A1007 -43.584-124.363 258.537 1.00 77.05 N ANISOU 1645 N VAL A1007 9579 8071 11627 -324 126 500 N ATOM 1646 CA VAL A1007 -44.121-124.545 257.193 1.00 74.85 C ANISOU 1646 CA VAL A1007 9264 7746 11428 -364 115 405 C ATOM 1647 C VAL A1007 -43.647-123.369 256.353 1.00 70.86 C ANISOU 1647 C VAL A1007 8734 7318 10871 -296 116 319 C ATOM 1648 O VAL A1007 -43.951-122.212 256.663 1.00 69.84 O ANISOU 1648 O VAL A1007 8589 7262 10685 -278 145 322 O ATOM 1649 CB VAL A1007 -45.653-124.639 257.201 1.00 76.13 C ANISOU 1649 CB VAL A1007 9344 7962 11621 -467 146 443 C ATOM 1650 CG1 VAL A1007 -46.171-124.859 255.786 1.00 78.20 C ANISOU 1650 CG1 VAL A1007 9565 8210 11937 -512 71 318 C ATOM 1651 CG2 VAL A1007 -46.106-125.763 258.107 1.00 77.13 C ANISOU 1651 CG2 VAL A1007 9469 8006 11832 -568 177 602 C ATOM 1652 N TYR A1008 -42.887-123.657 255.301 1.00 68.83 N ANISOU 1652 N TYR A1008 8486 7034 10633 -236 101 258 N ATOM 1653 CA TYR A1008 -42.320-122.619 254.456 1.00 67.33 C ANISOU 1653 CA TYR A1008 8254 6927 10401 -174 136 251 C ATOM 1654 C TYR A1008 -42.754-122.821 253.012 1.00 68.51 C ANISOU 1654 C TYR A1008 8412 7137 10481 -119 138 175 C ATOM 1655 O TYR A1008 -42.824-123.954 252.525 1.00 69.62 O ANISOU 1655 O TYR A1008 8613 7220 10620 -96 95 71 O ATOM 1656 CB TYR A1008 -40.786-122.595 254.553 1.00 68.43 C ANISOU 1656 CB TYR A1008 8347 7071 10582 -117 149 299 C ATOM 1657 CG TYR A1008 -40.091-123.767 253.897 1.00 72.44 C ANISOU 1657 CG TYR A1008 8870 7554 11101 3 170 259 C ATOM 1658 CD1 TYR A1008 -39.717-123.718 252.560 1.00 74.22 C ANISOU 1658 CD1 TYR A1008 9077 7872 11251 123 246 223 C ATOM 1659 CD2 TYR A1008 -39.795-124.919 254.615 1.00 73.62 C ANISOU 1659 CD2 TYR A1008 9070 7587 11317 36 128 268 C ATOM 1660 CE1 TYR A1008 -39.087-124.781 251.954 1.00 76.38 C ANISOU 1660 CE1 TYR A1008 9394 8124 11503 292 284 145 C ATOM 1661 CE2 TYR A1008 -39.156-125.989 254.015 1.00 74.92 C ANISOU 1661 CE2 TYR A1008 9277 7678 11509 195 154 211 C ATOM 1662 CZ TYR A1008 -38.803-125.912 252.684 1.00 76.02 C ANISOU 1662 CZ TYR A1008 9411 7914 11561 333 235 124 C ATOM 1663 OH TYR A1008 -38.167-126.969 252.071 1.00 76.33 O ANISOU 1663 OH TYR A1008 9522 7886 11596 550 280 28 O ATOM 1664 N GLY A1009 -43.048-121.715 252.336 1.00 71.60 N ANISOU 1664 N GLY A1009 8766 7634 10806 -83 172 221 N ATOM 1665 CA GLY A1009 -43.352-121.746 250.920 1.00 75.09 C ANISOU 1665 CA GLY A1009 9218 8201 11110 9 167 178 C ATOM 1666 C GLY A1009 -42.408-120.871 250.124 1.00 79.83 C ANISOU 1666 C GLY A1009 9784 8902 11645 115 280 306 C ATOM 1667 O GLY A1009 -42.470-119.642 250.216 1.00 81.35 O ANISOU 1667 O GLY A1009 9938 9089 11883 98 327 451 O ATOM 1668 N SER A1010 -41.522-121.486 249.345 1.00 84.77 N ANISOU 1668 N SER A1010 10424 9607 12177 236 343 273 N ATOM 1669 CA SER A1010 -40.560-120.756 248.534 1.00 88.10 C ANISOU 1669 CA SER A1010 10770 10173 12530 344 498 451 C ATOM 1670 C SER A1010 -40.533-121.328 247.125 1.00 93.12 C ANISOU 1670 C SER A1010 11477 11019 12884 555 547 366 C ATOM 1671 O SER A1010 -40.843-122.502 246.905 1.00 95.13 O ANISOU 1671 O SER A1010 11852 11243 13050 616 452 117 O ATOM 1672 CB SER A1010 -39.151-120.806 249.138 1.00 87.80 C ANISOU 1672 CB SER A1010 10611 10092 12656 322 581 549 C ATOM 1673 OG SER A1010 -38.615-122.115 249.095 1.00 91.62 O ANISOU 1673 OG SER A1010 11131 10576 13106 448 586 405 O ATOM 1674 N THR A1011 -40.149-120.481 246.172 1.00 92.20 N ANISOU 1674 N THR A1011 11305 11105 12623 671 695 578 N ATOM 1675 CA THR A1011 -40.098-120.840 244.760 1.00 92.72 C ANISOU 1675 CA THR A1011 11449 11449 12331 921 768 530 C ATOM 1676 C THR A1011 -38.677-121.011 244.246 1.00 96.97 C ANISOU 1676 C THR A1011 11894 12159 12792 1108 1015 659 C ATOM 1677 O THR A1011 -38.365-122.026 243.613 1.00103.17 O ANISOU 1677 O THR A1011 12783 13065 13351 1338 1053 446 O ATOM 1678 CB THR A1011 -40.834-119.781 243.925 1.00 89.25 C ANISOU 1678 CB THR A1011 11015 11192 11704 977 775 731 C ATOM 1679 OG1 THR A1011 -42.248-119.918 244.114 1.00 85.66 O ANISOU 1679 OG1 THR A1011 10632 10678 11236 891 533 557 O ATOM 1680 CG2 THR A1011 -40.505-119.934 242.449 1.00 92.88 C ANISOU 1680 CG2 THR A1011 11538 12016 11737 1272 905 773 C ATOM 1681 N THR A1012 -37.799-120.042 244.500 1.00 95.71 N ANISOU 1681 N THR A1012 11527 12009 12830 1018 1184 999 N ATOM 1682 CA THR A1012 -36.402-120.132 244.102 1.00 96.61 C ANISOU 1682 CA THR A1012 11456 12320 12931 1166 1440 1189 C ATOM 1683 C THR A1012 -35.494-120.551 245.251 1.00 91.58 C ANISOU 1683 C THR A1012 10656 11514 12627 1045 1411 1164 C ATOM 1684 O THR A1012 -34.269-120.553 245.092 1.00 93.22 O ANISOU 1684 O THR A1012 10627 11889 12903 1135 1609 1362 O ATOM 1685 CB THR A1012 -35.927-118.797 243.525 1.00100.20 C ANISOU 1685 CB THR A1012 11729 12927 13416 1123 1655 1646 C ATOM 1686 OG1 THR A1012 -36.114-117.761 244.496 1.00100.05 O ANISOU 1686 OG1 THR A1012 11635 12603 13778 791 1537 1793 O ATOM 1687 CG2 THR A1012 -36.709-118.455 242.266 1.00103.20 C ANISOU 1687 CG2 THR A1012 12265 13553 13393 1323 1707 1724 C ATOM 1688 N GLY A1013 -36.062-120.901 246.403 1.00 83.52 N ANISOU 1688 N GLY A1013 9729 10204 11800 859 1174 957 N ATOM 1689 CA GLY A1013 -35.287-121.372 247.529 1.00 80.54 C ANISOU 1689 CA GLY A1013 9226 9694 11680 775 1108 931 C ATOM 1690 C GLY A1013 -34.865-120.310 248.520 1.00 81.18 C ANISOU 1690 C GLY A1013 9120 9651 12072 482 1035 1128 C ATOM 1691 O GLY A1013 -34.135-120.630 249.468 1.00 81.58 O ANISOU 1691 O GLY A1013 9038 9647 12314 413 952 1124 O ATOM 1692 N ASN A1014 -35.299-119.060 248.341 1.00 78.98 N ANISOU 1692 N ASN A1014 8844 9316 11850 319 1042 1289 N ATOM 1693 CA ASN A1014 -34.904-118.001 249.265 1.00 75.93 C ANISOU 1693 CA ASN A1014 8326 8749 11776 30 944 1423 C ATOM 1694 C ASN A1014 -35.555-118.185 250.631 1.00 71.65 C ANISOU 1694 C ASN A1014 7936 7975 11315 -106 697 1178 C ATOM 1695 O ASN A1014 -34.871-118.171 251.662 1.00 70.35 O ANISOU 1695 O ASN A1014 7658 7744 11329 -244 567 1158 O ATOM 1696 CB ASN A1014 -35.254-116.633 248.680 1.00 77.47 C ANISOU 1696 CB ASN A1014 8535 8871 12030 -76 1022 1656 C ATOM 1697 CG ASN A1014 -34.330-116.231 247.547 1.00 81.78 C ANISOU 1697 CG ASN A1014 8856 9652 12563 -6 1289 2013 C ATOM 1698 OD1 ASN A1014 -33.216-115.762 247.776 1.00 86.24 O ANISOU 1698 OD1 ASN A1014 9140 10226 13401 -178 1340 2238 O ATOM 1699 ND2 ASN A1014 -34.791-116.411 246.315 1.00 83.09 N ANISOU 1699 ND2 ASN A1014 9127 10042 12403 246 1456 2082 N ATOM 1700 N THR A1015 -36.879-118.352 250.662 1.00 68.56 N ANISOU 1700 N THR A1015 7778 7496 10775 -61 629 1008 N ATOM 1701 CA THR A1015 -37.558-118.545 251.939 1.00 70.80 C ANISOU 1701 CA THR A1015 8190 7611 11100 -158 449 818 C ATOM 1702 C THR A1015 -37.208-119.891 252.558 1.00 74.43 C ANISOU 1702 C THR A1015 8649 8102 11530 -87 385 697 C ATOM 1703 O THR A1015 -37.188-120.020 253.788 1.00 73.38 O ANISOU 1703 O THR A1015 8542 7882 11458 -175 249 628 O ATOM 1704 CB THR A1015 -39.071-118.415 251.763 1.00 67.48 C ANISOU 1704 CB THR A1015 7949 7140 10551 -116 422 718 C ATOM 1705 OG1 THR A1015 -39.360-117.256 250.971 1.00 67.38 O ANISOU 1705 OG1 THR A1015 7938 7117 10545 -110 502 877 O ATOM 1706 CG2 THR A1015 -39.759-118.279 253.114 1.00 66.13 C ANISOU 1706 CG2 THR A1015 7877 6823 10427 -210 293 587 C ATOM 1707 N GLU A1016 -36.929-120.902 251.730 1.00 78.70 N ANISOU 1707 N GLU A1016 9183 8757 11961 101 481 670 N ATOM 1708 CA GLU A1016 -36.405-122.158 252.255 1.00 80.63 C ANISOU 1708 CA GLU A1016 9425 8985 12227 206 438 596 C ATOM 1709 C GLU A1016 -35.083-121.932 252.972 1.00 80.18 C ANISOU 1709 C GLU A1016 9136 8994 12335 158 399 734 C ATOM 1710 O GLU A1016 -34.863-122.446 254.075 1.00 79.62 O ANISOU 1710 O GLU A1016 9067 8867 12318 138 264 705 O ATOM 1711 CB GLU A1016 -36.233-123.174 251.128 1.00 85.16 C ANISOU 1711 CB GLU A1016 10055 9640 12661 458 560 514 C ATOM 1712 CG GLU A1016 -35.537-124.452 251.567 1.00 88.25 C ANISOU 1712 CG GLU A1016 10446 9972 13112 625 543 463 C ATOM 1713 CD GLU A1016 -35.680-125.569 250.557 1.00 92.32 C ANISOU 1713 CD GLU A1016 11131 10461 13485 882 622 280 C ATOM 1714 OE1 GLU A1016 -35.958-126.714 250.969 1.00 93.93 O ANISOU 1714 OE1 GLU A1016 11501 10446 13743 943 536 146 O ATOM 1715 OE2 GLU A1016 -35.527-125.299 249.348 1.00 94.29 O ANISOU 1715 OE2 GLU A1016 11369 10897 13560 1027 767 269 O ATOM 1716 N TYR A1017 -34.186-121.157 252.355 1.00 79.62 N ANISOU 1716 N TYR A1017 8839 9067 12347 133 510 914 N ATOM 1717 CA TYR A1017 -32.916-120.847 252.998 1.00 79.76 C ANISOU 1717 CA TYR A1017 8566 9174 12566 35 440 1062 C ATOM 1718 C TYR A1017 -33.122-120.102 254.309 1.00 81.13 C ANISOU 1718 C TYR A1017 8781 9198 12846 -227 193 996 C ATOM 1719 O TYR A1017 -32.353-120.294 255.257 1.00 81.72 O ANISOU 1719 O TYR A1017 8710 9329 13012 -278 26 1012 O ATOM 1720 CB TYR A1017 -32.028-120.030 252.061 1.00 81.63 C ANISOU 1720 CB TYR A1017 8520 9583 12914 -4 619 1315 C ATOM 1721 CG TYR A1017 -30.772-119.525 252.731 1.00 84.84 C ANISOU 1721 CG TYR A1017 8566 10076 13592 -194 506 1484 C ATOM 1722 CD1 TYR A1017 -29.650-120.336 252.844 1.00 86.99 C ANISOU 1722 CD1 TYR A1017 8553 10573 13927 -21 535 1584 C ATOM 1723 CD2 TYR A1017 -30.711-118.241 253.261 1.00 85.39 C ANISOU 1723 CD2 TYR A1017 8577 9992 13875 -542 346 1532 C ATOM 1724 CE1 TYR A1017 -28.502-119.882 253.461 1.00 90.07 C ANISOU 1724 CE1 TYR A1017 8555 11087 14579 -212 392 1749 C ATOM 1725 CE2 TYR A1017 -29.570-117.781 253.883 1.00 88.62 C ANISOU 1725 CE2 TYR A1017 8644 10472 14556 -765 183 1656 C ATOM 1726 CZ TYR A1017 -28.468-118.604 253.978 1.00 91.28 C ANISOU 1726 CZ TYR A1017 8648 11089 14947 -611 199 1775 C ATOM 1727 OH TYR A1017 -27.325-118.149 254.593 1.00 97.51 O ANISOU 1727 OH TYR A1017 9035 11993 16020 -849 0 1911 O ATOM 1728 N THR A1018 -34.140-119.243 254.380 1.00 82.50 N ANISOU 1728 N THR A1018 9155 9203 12988 -362 160 914 N ATOM 1729 CA THR A1018 -34.445-118.578 255.641 1.00 82.74 C ANISOU 1729 CA THR A1018 9290 9085 13060 -547 -59 789 C ATOM 1730 C THR A1018 -34.951-119.581 256.669 1.00 80.12 C ANISOU 1730 C THR A1018 9119 8756 12565 -445 -167 650 C ATOM 1731 O THR A1018 -34.513-119.575 257.825 1.00 80.52 O ANISOU 1731 O THR A1018 9145 8834 12614 -512 -363 603 O ATOM 1732 CB THR A1018 -35.468-117.463 255.422 1.00 81.23 C ANISOU 1732 CB THR A1018 9289 8705 12868 -637 -30 736 C ATOM 1733 OG1 THR A1018 -34.978-116.551 254.432 1.00 82.96 O ANISOU 1733 OG1 THR A1018 9366 8902 13253 -727 88 934 O ATOM 1734 CG2 THR A1018 -35.711-116.707 256.720 1.00 81.02 C ANISOU 1734 CG2 THR A1018 9399 8518 12868 -784 -245 565 C ATOM 1735 N ALA A1019 -35.863-120.467 256.259 1.00 78.20 N ANISOU 1735 N ALA A1019 9037 8494 12183 -292 -53 601 N ATOM 1736 CA ALA A1019 -36.380-121.476 257.177 1.00 78.14 C ANISOU 1736 CA ALA A1019 9168 8461 12059 -216 -121 537 C ATOM 1737 C ALA A1019 -35.275-122.415 257.646 1.00 79.87 C ANISOU 1737 C ALA A1019 9254 8775 12317 -106 -192 626 C ATOM 1738 O ALA A1019 -35.211-122.767 258.830 1.00 80.30 O ANISOU 1738 O ALA A1019 9355 8854 12301 -99 -331 635 O ATOM 1739 CB ALA A1019 -37.510-122.261 256.510 1.00 77.65 C ANISOU 1739 CB ALA A1019 9260 8327 11915 -125 -3 484 C ATOM 1740 N GLU A1020 -34.391-122.825 256.733 1.00 81.80 N ANISOU 1740 N GLU A1020 9327 9103 12650 20 -87 713 N ATOM 1741 CA GLU A1020 -33.283-123.696 257.116 1.00 82.96 C ANISOU 1741 CA GLU A1020 9309 9356 12855 182 -139 821 C ATOM 1742 C GLU A1020 -32.294-122.970 258.020 1.00 84.63 C ANISOU 1742 C GLU A1020 9286 9719 13152 40 -347 896 C ATOM 1743 O GLU A1020 -31.742-123.567 258.951 1.00 84.17 O ANISOU 1743 O GLU A1020 9161 9749 13072 128 -501 963 O ATOM 1744 CB GLU A1020 -32.582-124.231 255.868 1.00 85.04 C ANISOU 1744 CB GLU A1020 9432 9704 13174 401 60 884 C ATOM 1745 CG GLU A1020 -33.439-125.171 255.037 1.00 88.49 C ANISOU 1745 CG GLU A1020 10128 9984 13509 571 201 752 C ATOM 1746 CD GLU A1020 -32.766-125.589 253.748 1.00 93.86 C ANISOU 1746 CD GLU A1020 10714 10778 14173 829 408 761 C ATOM 1747 OE1 GLU A1020 -31.973-124.793 253.204 1.00 94.74 O ANISOU 1747 OE1 GLU A1020 10562 11107 14327 811 510 896 O ATOM 1748 OE2 GLU A1020 -33.026-126.717 253.280 1.00 96.79 O ANISOU 1748 OE2 GLU A1020 11277 11013 14487 1054 474 636 O ATOM 1749 N THR A1021 -32.051-121.682 257.758 1.00 86.82 N ANISOU 1749 N THR A1021 9436 10015 13537 -185 -376 895 N ATOM 1750 CA THR A1021 -31.224-120.889 258.660 1.00 90.21 C ANISOU 1750 CA THR A1021 9669 10535 14070 -392 -636 908 C ATOM 1751 C THR A1021 -31.914-120.682 260.005 1.00 88.78 C ANISOU 1751 C THR A1021 9746 10283 13704 -471 -858 735 C ATOM 1752 O THR A1021 -31.246-120.636 261.045 1.00 88.84 O ANISOU 1752 O THR A1021 9652 10425 13680 -522 -1124 722 O ATOM 1753 CB THR A1021 -30.881-119.544 258.010 1.00 94.40 C ANISOU 1753 CB THR A1021 10036 11017 14814 -649 -609 954 C ATOM 1754 OG1 THR A1021 -30.139-119.769 256.804 1.00 97.42 O ANISOU 1754 OG1 THR A1021 10141 11547 15329 -544 -371 1168 O ATOM 1755 CG2 THR A1021 -30.051-118.675 258.947 1.00 98.32 C ANISOU 1755 CG2 THR A1021 10342 11551 15466 -927 -932 920 C ATOM 1756 N ILE A1022 -33.246-120.575 260.007 1.00 89.73 N ANISOU 1756 N ILE A1022 10183 10237 13675 -458 -752 609 N ATOM 1757 CA ILE A1022 -33.982-120.435 261.260 1.00 90.38 C ANISOU 1757 CA ILE A1022 10510 10297 13533 -472 -895 466 C ATOM 1758 C ILE A1022 -33.962-121.740 262.044 1.00 95.12 C ANISOU 1758 C ILE A1022 11163 11016 13963 -274 -931 570 C ATOM 1759 O ILE A1022 -33.740-121.746 263.261 1.00 99.75 O ANISOU 1759 O ILE A1022 11795 11734 14371 -261 -1142 543 O ATOM 1760 CB ILE A1022 -35.424-119.970 260.985 1.00 85.15 C ANISOU 1760 CB ILE A1022 10108 9464 12781 -482 -733 350 C ATOM 1761 CG1 ILE A1022 -35.450-118.504 260.555 1.00 84.66 C ANISOU 1761 CG1 ILE A1022 10048 9250 12867 -664 -754 249 C ATOM 1762 CG2 ILE A1022 -36.298-120.176 262.214 1.00 82.59 C ANISOU 1762 CG2 ILE A1022 10018 9179 12182 -406 -784 262 C ATOM 1763 CD1 ILE A1022 -36.807-118.041 260.071 1.00 83.25 C ANISOU 1763 CD1 ILE A1022 10072 8923 12635 -621 -575 182 C ATOM 1764 N ALA A1023 -34.202-122.865 261.364 1.00 97.81 N ANISOU 1764 N ALA A1023 11519 11297 14346 -107 -737 691 N ATOM 1765 CA ALA A1023 -34.253-124.152 262.049 1.00105.84 C ANISOU 1765 CA ALA A1023 12617 12341 15256 81 -748 830 C ATOM 1766 C ALA A1023 -32.926-124.493 262.713 1.00111.71 C ANISOU 1766 C ALA A1023 13145 13289 16010 182 -956 963 C ATOM 1767 O ALA A1023 -32.908-125.123 263.776 1.00116.74 O ANISOU 1767 O ALA A1023 13862 14018 16474 302 -1069 1077 O ATOM 1768 CB ALA A1023 -34.651-125.254 261.067 1.00109.99 C ANISOU 1768 CB ALA A1023 13209 12689 15893 222 -530 894 C ATOM 1769 N ARG A1024 -31.809-124.081 262.109 1.00111.17 N ANISOU 1769 N ARG A1024 12774 13328 16139 144 -1004 988 N ATOM 1770 CA ARG A1024 -30.504-124.402 262.672 1.00117.40 C ANISOU 1770 CA ARG A1024 13276 14358 16971 247 -1215 1137 C ATOM 1771 C ARG A1024 -30.251-123.651 263.976 1.00120.90 C ANISOU 1771 C ARG A1024 13712 14985 17239 91 -1560 1047 C ATOM 1772 O ARG A1024 -29.611-124.196 264.882 1.00123.71 O ANISOU 1772 O ARG A1024 13971 15556 17476 233 -1776 1177 O ATOM 1773 CB ARG A1024 -29.409-124.098 261.650 1.00121.15 C ANISOU 1773 CB ARG A1024 13369 14939 17722 230 -1148 1215 C ATOM 1774 CG ARG A1024 -28.035-124.635 262.013 1.00128.99 C ANISOU 1774 CG ARG A1024 13987 16212 18813 405 -1309 1422 C ATOM 1775 CD ARG A1024 -27.245-125.005 260.765 1.00132.93 C ANISOU 1775 CD ARG A1024 14184 16779 19543 588 -1058 1564 C ATOM 1776 NE ARG A1024 -27.740-126.235 260.153 1.00135.11 N ANISOU 1776 NE ARG A1024 14705 16854 19777 923 -786 1586 N ATOM 1777 CZ ARG A1024 -27.256-126.763 259.033 1.00138.85 C ANISOU 1777 CZ ARG A1024 15040 17346 20370 1180 -524 1652 C ATOM 1778 NH1 ARG A1024 -26.261-126.167 258.391 1.00141.27 N ANISOU 1778 NH1 ARG A1024 14921 17910 20844 1147 -452 1763 N ATOM 1779 NH2 ARG A1024 -27.768-127.888 258.552 1.00139.36 N ANISOU 1779 NH2 ARG A1024 15393 17167 20390 1470 -328 1605 N ATOM 1780 N GLU A1025 -30.747-122.416 264.094 1.00116.91 N ANISOU 1780 N GLU A1025 13328 14394 16698 -172 -1632 815 N ATOM 1781 CA GLU A1025 -30.620-121.683 265.351 1.00113.80 C ANISOU 1781 CA GLU A1025 13011 14139 16090 -302 -1974 644 C ATOM 1782 C GLU A1025 -31.464-122.327 266.443 1.00108.22 C ANISOU 1782 C GLU A1025 12627 13501 14989 -107 -1976 661 C ATOM 1783 O GLU A1025 -31.053-122.373 267.608 1.00111.92 O ANISOU 1783 O GLU A1025 13111 14218 15197 -49 -2266 652 O ATOM 1784 CB GLU A1025 -31.022-120.221 265.148 1.00113.30 C ANISOU 1784 CB GLU A1025 13057 13883 16108 -591 -2019 369 C ATOM 1785 CG GLU A1025 -30.383-119.235 266.127 1.00120.01 C ANISOU 1785 CG GLU A1025 13866 14839 16893 -806 -2448 142 C ATOM 1786 CD GLU A1025 -31.021-119.243 267.508 1.00123.63 C ANISOU 1786 CD GLU A1025 14673 15419 16881 -681 -2619 -44 C ATOM 1787 OE1 GLU A1025 -32.180-119.690 267.636 1.00122.42 O ANISOU 1787 OE1 GLU A1025 14815 15204 16497 -491 -2352 -18 O ATOM 1788 OE2 GLU A1025 -30.360-118.794 268.469 1.00127.14 O ANISOU 1788 OE2 GLU A1025 15083 16050 17176 -775 -3027 -214 O ATOM 1789 N LEU A1026 -32.649-122.828 266.086 1.00101.57 N ANISOU 1789 N LEU A1026 12029 12471 14092 -10 -1660 707 N ATOM 1790 CA LEU A1026 -33.495-123.496 267.068 1.00101.37 C ANISOU 1790 CA LEU A1026 12270 12516 13730 160 -1602 802 C ATOM 1791 C LEU A1026 -32.945-124.867 267.440 1.00107.11 C ANISOU 1791 C LEU A1026 12917 13354 14425 404 -1623 1130 C ATOM 1792 O LEU A1026 -33.210-125.360 268.542 1.00110.16 O ANISOU 1792 O LEU A1026 13458 13904 14493 555 -1682 1273 O ATOM 1793 CB LEU A1026 -34.922-123.615 266.535 1.00 95.18 C ANISOU 1793 CB LEU A1026 11700 11504 12962 149 -1270 784 C ATOM 1794 CG LEU A1026 -35.802-122.387 266.771 1.00 91.79 C ANISOU 1794 CG LEU A1026 11390 10971 12514 -16 -1232 494 C ATOM 1795 CD1 LEU A1026 -35.294-121.195 265.985 1.00 89.09 C ANISOU 1795 CD1 LEU A1026 11175 10447 12229 -8 -916 522 C ATOM 1796 CD2 LEU A1026 -37.234-122.693 266.390 1.00 93.23 C ANISOU 1796 CD2 LEU A1026 11759 11339 12327 7 -1424 310 C ATOM 1797 N ALA A1027 -32.185-125.495 266.541 1.00108.51 N ANISOU 1797 N ALA A1027 12866 13449 14913 483 -1555 1270 N ATOM 1798 CA ALA A1027 -31.538-126.758 266.879 1.00110.26 C ANISOU 1798 CA ALA A1027 13004 13745 15145 761 -1591 1581 C ATOM 1799 C ALA A1027 -30.477-126.561 267.953 1.00116.59 C ANISOU 1799 C ALA A1027 13622 14923 15752 830 -1969 1647 C ATOM 1800 O ALA A1027 -30.294-127.423 268.821 1.00119.29 O ANISOU 1800 O ALA A1027 14018 15409 15898 1072 -2057 1912 O ATOM 1801 CB ALA A1027 -30.926-127.388 265.627 1.00107.89 C ANISOU 1801 CB ALA A1027 12504 13280 15207 880 -1423 1664 C ATOM 1802 N ASP A1028 -29.769-125.429 267.913 1.00119.91 N ANISOU 1802 N ASP A1028 13820 15505 16235 609 -2216 1425 N ATOM 1803 CA ASP A1028 -28.753-125.153 268.923 1.00126.69 C ANISOU 1803 CA ASP A1028 14475 16744 16919 622 -2647 1438 C ATOM 1804 C ASP A1028 -29.378-124.968 270.300 1.00128.86 C ANISOU 1804 C ASP A1028 15074 17206 16682 667 -2822 1359 C ATOM 1805 O ASP A1028 -28.821-125.422 271.307 1.00134.13 O ANISOU 1805 O ASP A1028 15692 18200 17070 860 -3093 1529 O ATOM 1806 CB ASP A1028 -27.945-123.915 268.533 1.00130.17 C ANISOU 1806 CB ASP A1028 14607 17254 17597 297 -2882 1196 C ATOM 1807 CG ASP A1028 -27.322-124.035 267.156 1.00131.51 C ANISOU 1807 CG ASP A1028 14434 17303 18230 271 -2662 1312 C ATOM 1808 OD1 ASP A1028 -27.169-125.174 266.668 1.00131.87 O ANISOU 1808 OD1 ASP A1028 14418 17300 18386 569 -2432 1570 O ATOM 1809 OD2 ASP A1028 -26.981-122.989 266.564 1.00132.00 O ANISOU 1809 OD2 ASP A1028 14301 17311 18541 -33 -2709 1152 O ATOM 1810 N ALA A1029 -30.534-124.310 270.365 1.00126.51 N ANISOU 1810 N ALA A1029 15103 16740 16227 531 -2662 1118 N ATOM 1811 CA ALA A1029 -31.207-124.056 271.631 1.00128.90 C ANISOU 1811 CA ALA A1029 15729 17245 16003 610 -2768 1017 C ATOM 1812 C ALA A1029 -31.918-125.281 272.188 1.00128.87 C ANISOU 1812 C ALA A1029 15935 17284 15744 903 -2525 1396 C ATOM 1813 O ALA A1029 -32.461-125.210 273.296 1.00131.91 O ANISOU 1813 O ALA A1029 16576 17906 15639 1026 -2567 1398 O ATOM 1814 CB ALA A1029 -32.212-122.915 271.473 1.00125.89 C ANISOU 1814 CB ALA A1029 15602 16666 15563 414 -2641 642 C ATOM 1815 N GLY A1030 -31.932-126.391 271.458 1.00126.22 N ANISOU 1815 N GLY A1030 15513 16718 15725 1020 -2266 1716 N ATOM 1816 CA GLY A1030 -32.590-127.587 271.937 1.00126.60 C ANISOU 1816 CA GLY A1030 15755 16724 15623 1253 -2037 2112 C ATOM 1817 C GLY A1030 -34.077-127.598 271.655 1.00124.78 C ANISOU 1817 C GLY A1030 15772 16241 15399 1153 -1656 2088 C ATOM 1818 O GLY A1030 -34.885-127.850 272.553 1.00128.29 O ANISOU 1818 O GLY A1030 16432 16826 15488 1257 -1533 2263 O ATOM 1819 N TYR A1031 -34.451-127.302 270.416 1.00118.94 N ANISOU 1819 N TYR A1031 14974 15173 15043 960 -1467 1893 N ATOM 1820 CA TYR A1031 -35.818-127.462 269.947 1.00115.20 C ANISOU 1820 CA TYR A1031 14660 14443 14668 861 -1122 1904 C ATOM 1821 C TYR A1031 -35.933-128.737 269.121 1.00115.87 C ANISOU 1821 C TYR A1031 14717 14175 15134 907 -919 2161 C ATOM 1822 O TYR A1031 -34.943-129.267 268.610 1.00116.34 O ANISOU 1822 O TYR A1031 14629 14141 15434 1011 -1010 2230 O ATOM 1823 CB TYR A1031 -36.262-126.259 269.108 1.00109.09 C ANISOU 1823 CB TYR A1031 13867 13546 14036 632 -1068 1510 C ATOM 1824 CG TYR A1031 -36.740-125.065 269.906 1.00108.11 C ANISOU 1824 CG TYR A1031 13890 13638 13549 592 -1146 1243 C ATOM 1825 CD1 TYR A1031 -35.852-124.086 270.329 1.00110.11 C ANISOU 1825 CD1 TYR A1031 14100 14072 13665 542 -1479 968 C ATOM 1826 CD2 TYR A1031 -38.084-124.910 270.224 1.00105.59 C ANISOU 1826 CD2 TYR A1031 13745 13331 13043 607 -892 1250 C ATOM 1827 CE1 TYR A1031 -36.287-122.992 271.054 1.00111.61 C ANISOU 1827 CE1 TYR A1031 14480 14402 13524 527 -1569 663 C ATOM 1828 CE2 TYR A1031 -38.528-123.817 270.947 1.00106.92 C ANISOU 1828 CE2 TYR A1031 14075 13689 12862 638 -938 977 C ATOM 1829 CZ TYR A1031 -37.624-122.862 271.359 1.00110.54 C ANISOU 1829 CZ TYR A1031 14551 14276 13173 606 -1283 659 C ATOM 1830 OH TYR A1031 -38.060-121.774 272.080 1.00113.46 O ANISOU 1830 OH TYR A1031 15135 14780 13194 658 -1348 329 O ATOM 1831 N GLU A1032 -37.161-129.232 269.001 1.00116.30 N ANISOU 1831 N GLU A1032 14909 14030 15250 836 -648 2294 N ATOM 1832 CA GLU A1032 -37.464-130.369 268.135 1.00118.64 C ANISOU 1832 CA GLU A1032 15224 13914 15941 816 -473 2456 C ATOM 1833 C GLU A1032 -38.159-129.800 266.902 1.00115.78 C ANISOU 1833 C GLU A1032 14827 13352 15812 594 -351 2138 C ATOM 1834 O GLU A1032 -39.383-129.670 266.857 1.00117.12 O ANISOU 1834 O GLU A1032 15057 13470 15974 446 -179 2133 O ATOM 1835 CB GLU A1032 -38.318-131.403 268.859 1.00125.26 C ANISOU 1835 CB GLU A1032 16207 14647 16740 848 -290 2871 C ATOM 1836 CG GLU A1032 -38.460-132.715 268.106 1.00129.86 C ANISOU 1836 CG GLU A1032 16842 14734 17763 836 -175 3053 C ATOM 1837 CD GLU A1032 -39.309-133.729 268.847 1.00136.64 C ANISOU 1837 CD GLU A1032 17829 15441 18646 814 6 3517 C ATOM 1838 OE1 GLU A1032 -38.955-134.086 269.990 1.00140.84 O ANISOU 1838 OE1 GLU A1032 18416 16186 18909 1015 -29 3883 O ATOM 1839 OE2 GLU A1032 -40.335-134.164 268.285 1.00137.88 O ANISOU 1839 OE2 GLU A1032 18016 15281 19092 585 173 3538 O ATOM 1840 N VAL A1033 -37.363-129.455 265.896 1.00113.29 N ANISOU 1840 N VAL A1033 14387 12965 15693 589 -436 1902 N ATOM 1841 CA VAL A1033 -37.839-128.712 264.735 1.00111.24 C ANISOU 1841 CA VAL A1033 14084 12601 15581 415 -357 1602 C ATOM 1842 C VAL A1033 -38.240-129.679 263.630 1.00110.95 C ANISOU 1842 C VAL A1033 14097 12206 15853 391 -227 1600 C ATOM 1843 O VAL A1033 -37.527-130.646 263.335 1.00113.36 O ANISOU 1843 O VAL A1033 14412 12330 16330 552 -244 1698 O ATOM 1844 CB VAL A1033 -36.763-127.726 264.243 1.00110.76 C ANISOU 1844 CB VAL A1033 13852 12690 15542 412 -501 1381 C ATOM 1845 CG1 VAL A1033 -37.290-126.891 263.086 1.00108.44 C ANISOU 1845 CG1 VAL A1033 13530 12306 15365 252 -405 1131 C ATOM 1846 CG2 VAL A1033 -36.298-126.835 265.384 1.00112.66 C ANISOU 1846 CG2 VAL A1033 14063 13241 15501 411 -699 1341 C ATOM 1847 N ASP A1034 -39.390-129.412 263.016 1.00108.32 N ANISOU 1847 N ASP A1034 13798 11772 15584 207 -113 1469 N ATOM 1848 CA ASP A1034 -39.858-130.138 261.836 1.00105.68 C ANISOU 1848 CA ASP A1034 13515 11126 15513 141 -44 1369 C ATOM 1849 C ASP A1034 -40.211-129.086 260.789 1.00 98.64 C ANISOU 1849 C ASP A1034 12549 10324 14606 34 -28 1085 C ATOM 1850 O ASP A1034 -41.284-128.481 260.848 1.00 96.29 O ANISOU 1850 O ASP A1034 12233 10110 14242 -114 27 1043 O ATOM 1851 CB ASP A1034 -41.053-131.029 262.164 1.00109.63 C ANISOU 1851 CB ASP A1034 14107 11414 16135 -6 47 1556 C ATOM 1852 CG ASP A1034 -41.458-131.917 261.001 1.00112.96 C ANISOU 1852 CG ASP A1034 14607 11460 16852 -92 50 1419 C ATOM 1853 OD1 ASP A1034 -40.561-132.480 260.337 1.00116.22 O ANISOU 1853 OD1 ASP A1034 15088 11688 17384 81 2 1311 O ATOM 1854 OD2 ASP A1034 -42.674-132.053 260.750 1.00112.73 O ANISOU 1854 OD2 ASP A1034 14565 11336 16930 -321 90 1406 O ATOM 1855 N SER A1035 -39.304-128.852 259.846 1.00 96.60 N ANISOU 1855 N SER A1035 12230 10075 14399 136 -57 926 N ATOM 1856 CA SER A1035 -39.520-127.864 258.797 1.00 95.17 C ANISOU 1856 CA SER A1035 11982 9988 14190 65 -30 716 C ATOM 1857 C SER A1035 -40.114-128.557 257.577 1.00 93.34 C ANISOU 1857 C SER A1035 11836 9554 14076 44 6 568 C ATOM 1858 O SER A1035 -39.514-129.490 257.032 1.00 97.90 O ANISOU 1858 O SER A1035 12484 9960 14756 193 7 521 O ATOM 1859 CB SER A1035 -38.216-127.153 258.438 1.00 97.24 C ANISOU 1859 CB SER A1035 12103 10416 14429 173 -59 673 C ATOM 1860 OG SER A1035 -37.273-128.054 257.887 1.00100.37 O ANISOU 1860 OG SER A1035 12481 10726 14929 374 -38 684 O ATOM 1861 N ARG A1036 -41.290-128.104 257.153 1.00 87.71 N ANISOU 1861 N ARG A1036 11118 8869 13338 -116 20 479 N ATOM 1862 CA ARG A1036 -42.024-128.731 256.064 1.00 84.89 C ANISOU 1862 CA ARG A1036 10834 8352 13067 -178 -7 315 C ATOM 1863 C ARG A1036 -42.236-127.739 254.933 1.00 79.32 C ANISOU 1863 C ARG A1036 10067 7836 12236 -169 0 154 C ATOM 1864 O ARG A1036 -42.689-126.613 255.163 1.00 78.32 O ANISOU 1864 O ARG A1036 9843 7892 12021 -234 26 201 O ATOM 1865 CB ARG A1036 -43.374-129.271 256.545 1.00 89.70 C ANISOU 1865 CB ARG A1036 11449 8841 13792 -399 -28 401 C ATOM 1866 CG ARG A1036 -43.286-130.602 257.271 1.00 95.27 C ANISOU 1866 CG ARG A1036 12262 9252 14683 -423 -35 566 C ATOM 1867 CD ARG A1036 -44.593-131.371 257.153 1.00101.06 C ANISOU 1867 CD ARG A1036 12998 9776 15624 -686 -81 588 C ATOM 1868 NE ARG A1036 -44.369-132.810 257.061 1.00108.19 N ANISOU 1868 NE ARG A1036 14082 10243 16784 -697 -141 595 N ATOM 1869 CZ ARG A1036 -45.291-133.686 256.679 1.00112.69 C ANISOU 1869 CZ ARG A1036 14697 10508 17611 -943 -239 538 C ATOM 1870 NH1 ARG A1036 -44.998-134.976 256.621 1.00115.74 N ANISOU 1870 NH1 ARG A1036 15293 10423 18261 -936 -300 532 N ATOM 1871 NH2 ARG A1036 -46.507-133.274 256.347 1.00112.57 N ANISOU 1871 NH2 ARG A1036 14509 10644 17617 -1195 -292 486 N ATOM 1872 N ASP A1037 -41.902-128.162 253.718 1.00 78.07 N ANISOU 1872 N ASP A1037 9983 7627 12051 -54 -16 -30 N ATOM 1873 CA ASP A1037 -42.339-127.447 252.531 1.00 74.93 C ANISOU 1873 CA ASP A1037 9558 7408 11505 -43 -26 -166 C ATOM 1874 C ASP A1037 -43.860-127.389 252.513 1.00 73.13 C ANISOU 1874 C ASP A1037 9291 7186 11311 -255 -122 -195 C ATOM 1875 O ASP A1037 -44.539-128.373 252.817 1.00 73.19 O ANISOU 1875 O ASP A1037 9344 6986 11478 -404 -207 -219 O ATOM 1876 CB ASP A1037 -41.809-128.149 251.276 1.00 78.25 C ANISOU 1876 CB ASP A1037 10110 7782 11840 148 -34 -385 C ATOM 1877 CG ASP A1037 -42.107-127.388 249.992 1.00 79.22 C ANISOU 1877 CG ASP A1037 10213 8157 11729 216 -32 -492 C ATOM 1878 OD1 ASP A1037 -43.192-126.782 249.866 1.00 80.72 O ANISOU 1878 OD1 ASP A1037 10333 8457 11880 68 -109 -476 O ATOM 1879 OD2 ASP A1037 -41.245-127.407 249.089 1.00 79.87 O ANISOU 1879 OD2 ASP A1037 10340 8357 11650 452 59 -566 O ATOM 1880 N ALA A1038 -44.399-126.221 252.159 1.00 72.48 N ANISOU 1880 N ALA A1038 9098 7334 11106 -269 -107 -161 N ATOM 1881 CA ALA A1038 -45.846-126.055 252.116 1.00 73.59 C ANISOU 1881 CA ALA A1038 9136 7548 11277 -430 -192 -159 C ATOM 1882 C ALA A1038 -46.498-126.903 251.032 1.00 78.52 C ANISOU 1882 C ALA A1038 9814 8122 11897 -499 -371 -381 C ATOM 1883 O ALA A1038 -47.694-127.196 251.129 1.00 79.82 O ANISOU 1883 O ALA A1038 9866 8287 12176 -698 -487 -381 O ATOM 1884 CB ALA A1038 -46.203-124.583 251.906 1.00 71.25 C ANISOU 1884 CB ALA A1038 8725 7495 10852 -361 -135 -66 C ATOM 1885 N ALA A1039 -45.738-127.320 250.017 1.00 83.29 N ANISOU 1885 N ALA A1039 10578 8700 12370 -336 -401 -578 N ATOM 1886 CA ALA A1039 -46.313-128.073 248.911 1.00 89.38 C ANISOU 1886 CA ALA A1039 11448 9436 13074 -373 -608 -861 C ATOM 1887 C ALA A1039 -46.854-129.431 249.336 1.00 95.56 C ANISOU 1887 C ALA A1039 12304 9861 14143 -608 -761 -970 C ATOM 1888 O ALA A1039 -47.662-130.015 248.606 1.00 98.92 O ANISOU 1888 O ALA A1039 12763 10233 14589 -751 -999 -1204 O ATOM 1889 CB ALA A1039 -45.272-128.261 247.809 1.00 89.70 C ANISOU 1889 CB ALA A1039 11680 9536 12865 -83 -565 -1061 C ATOM 1890 N SER A1040 -46.446-129.942 250.512 1.00 93.35 N ANISOU 1890 N SER A1040 12044 9330 14092 -666 -649 -789 N ATOM 1891 CA SER A1040 -46.750-131.308 250.930 1.00 95.24 C ANISOU 1891 CA SER A1040 12395 9155 14638 -861 -757 -835 C ATOM 1892 C SER A1040 -47.125-131.344 252.414 1.00 96.29 C ANISOU 1892 C SER A1040 12375 9219 14991 -1042 -637 -471 C ATOM 1893 O SER A1040 -46.377-131.842 253.253 1.00 94.30 O ANISOU 1893 O SER A1040 12221 8766 14844 -963 -525 -311 O ATOM 1894 CB SER A1040 -45.560-132.232 250.670 1.00 94.92 C ANISOU 1894 CB SER A1040 12636 8811 14618 -626 -727 -1001 C ATOM 1895 OG SER A1040 -44.457-131.876 251.488 1.00 91.72 O ANISOU 1895 OG SER A1040 12204 8469 14177 -419 -510 -760 O ATOM 1896 N VAL A1041 -48.299-130.820 252.764 1.00 95.99 N ANISOU 1896 N VAL A1041 12086 9386 15000 -1255 -650 -316 N ATOM 1897 CA VAL A1041 -48.739-130.833 254.154 1.00105.06 C ANISOU 1897 CA VAL A1041 13082 10536 16299 -1393 -501 40 C ATOM 1898 C VAL A1041 -50.219-131.176 254.240 1.00120.64 C ANISOU 1898 C VAL A1041 14812 12522 18503 -1735 -601 138 C ATOM 1899 O VAL A1041 -50.995-130.934 253.311 1.00128.68 O ANISOU 1899 O VAL A1041 15701 13694 19498 -1836 -780 -42 O ATOM 1900 CB VAL A1041 -48.476-129.490 254.877 1.00101.86 C ANISOU 1900 CB VAL A1041 12563 10481 15656 -1206 -302 224 C ATOM 1901 CG1 VAL A1041 -46.994-129.141 254.872 1.00101.41 C ANISOU 1901 CG1 VAL A1041 12683 10422 15427 -927 -224 166 C ATOM 1902 CG2 VAL A1041 -49.307-128.374 254.265 1.00102.75 C ANISOU 1902 CG2 VAL A1041 12482 10931 15626 -1192 -333 167 C ATOM 1903 N GLU A1042 -50.604-131.740 255.380 1.00129.39 N ANISOU 1903 N GLU A1042 15830 13502 19829 -1909 -481 461 N ATOM 1904 CA GLU A1042 -51.998-131.996 255.710 1.00136.31 C ANISOU 1904 CA GLU A1042 16393 14450 20951 -2242 -500 673 C ATOM 1905 C GLU A1042 -52.513-130.828 256.542 1.00133.70 C ANISOU 1905 C GLU A1042 15801 14581 20418 -2114 -260 938 C ATOM 1906 O GLU A1042 -51.958-130.525 257.603 1.00133.13 O ANISOU 1906 O GLU A1042 15808 14584 20192 -1930 -34 1148 O ATOM 1907 CB GLU A1042 -52.147-133.318 256.463 1.00142.64 C ANISOU 1907 CB GLU A1042 17237 14838 22121 -2506 -471 932 C ATOM 1908 CG GLU A1042 -51.765-134.538 255.633 1.00151.15 C ANISOU 1908 CG GLU A1042 18598 15373 23458 -2640 -728 638 C ATOM 1909 CD GLU A1042 -51.813-135.832 256.421 1.00160.59 C ANISOU 1909 CD GLU A1042 19885 16076 25057 -2875 -685 934 C ATOM 1910 OE1 GLU A1042 -51.926-135.775 257.663 1.00162.98 O ANISOU 1910 OE1 GLU A1042 20062 16498 25365 -2872 -423 1398 O ATOM 1911 OE2 GLU A1042 -51.735-136.909 255.796 1.00166.16 O ANISOU 1911 OE2 GLU A1042 20807 16261 26064 -3047 -913 705 O ATOM 1912 N ALA A1043 -53.563-130.169 256.050 1.00129.69 N ANISOU 1912 N ALA A1043 14993 14391 19892 -2182 -325 908 N ATOM 1913 CA ALA A1043 -54.070-128.974 256.718 1.00126.77 C ANISOU 1913 CA ALA A1043 14399 14451 19318 -1988 -96 1106 C ATOM 1914 C ALA A1043 -54.638-129.304 258.092 1.00128.86 C ANISOU 1914 C ALA A1043 14475 14799 19689 -2086 166 1524 C ATOM 1915 O ALA A1043 -54.330-128.626 259.079 1.00127.81 O ANISOU 1915 O ALA A1043 14398 14859 19304 -1830 416 1674 O ATOM 1916 CB ALA A1043 -55.123-128.298 255.844 1.00128.80 C ANISOU 1916 CB ALA A1043 14349 15023 19567 -2013 -233 1014 C ATOM 1917 N GLY A1044 -55.464-130.343 258.178 1.00134.40 N ANISOU 1917 N GLY A1044 14956 15357 20752 -2461 109 1720 N ATOM 1918 CA GLY A1044 -56.097-130.703 259.431 1.00139.19 C ANISOU 1918 CA GLY A1044 15334 16079 21471 -2576 389 2191 C ATOM 1919 C GLY A1044 -55.122-131.049 260.538 1.00140.68 C ANISOU 1919 C GLY A1044 15830 16110 21512 -2412 595 2391 C ATOM 1920 O GLY A1044 -54.245-131.898 260.356 1.00141.19 O ANISOU 1920 O GLY A1044 16205 15745 21697 -2472 462 2297 O ATOM 1921 N GLY A1045 -55.266-130.390 261.687 1.00138.57 N ANISOU 1921 N GLY A1045 15487 16206 20958 -2168 911 2656 N ATOM 1922 CA GLY A1045 -54.384-130.639 262.814 1.00139.36 C ANISOU 1922 CA GLY A1045 15862 16248 20841 -1980 1089 2859 C ATOM 1923 C GLY A1045 -52.919-130.439 262.504 1.00134.32 C ANISOU 1923 C GLY A1045 15635 15392 20010 -1751 923 2526 C ATOM 1924 O GLY A1045 -52.068-131.097 263.111 1.00136.16 O ANISOU 1924 O GLY A1045 16105 15418 20212 -1692 945 2668 O ATOM 1925 N LEU A1046 -52.601-129.539 261.569 1.00125.13 N ANISOU 1925 N LEU A1046 14534 14290 18720 -1609 766 2125 N ATOM 1926 CA LEU A1046 -51.214-129.366 261.151 1.00117.51 C ANISOU 1926 CA LEU A1046 13895 13134 17619 -1423 616 1834 C ATOM 1927 C LEU A1046 -50.342-128.880 262.301 1.00115.82 C ANISOU 1927 C LEU A1046 13862 13074 17069 -1144 751 1926 C ATOM 1928 O LEU A1046 -49.175-129.273 262.416 1.00116.13 O ANISOU 1928 O LEU A1046 14132 12921 17070 -1049 664 1880 O ATOM 1929 CB LEU A1046 -51.137-128.391 259.976 1.00114.60 C ANISOU 1929 CB LEU A1046 13520 12858 17165 -1325 470 1468 C ATOM 1930 CG LEU A1046 -49.718-128.088 259.495 1.00112.10 C ANISOU 1930 CG LEU A1046 13478 12406 16710 -1134 355 1206 C ATOM 1931 CD1 LEU A1046 -49.038-129.362 259.018 1.00112.20 C ANISOU 1931 CD1 LEU A1046 13663 12032 16935 -1237 216 1147 C ATOM 1932 CD2 LEU A1046 -49.719-127.033 258.404 1.00110.47 C ANISOU 1932 CD2 LEU A1046 13244 12329 16399 -1030 262 935 C ATOM 1933 N PHE A1047 -50.889-128.035 263.166 1.00115.06 N ANISOU 1933 N PHE A1047 13662 13341 16714 -988 950 2043 N ATOM 1934 CA PHE A1047 -50.121-127.468 264.262 1.00113.27 C ANISOU 1934 CA PHE A1047 13626 13297 16115 -715 1034 2063 C ATOM 1935 C PHE A1047 -50.259-128.259 265.555 1.00116.87 C ANISOU 1935 C PHE A1047 14093 13848 16463 -703 1219 2480 C ATOM 1936 O PHE A1047 -49.654-127.873 266.560 1.00117.28 O ANISOU 1936 O PHE A1047 14310 14098 16151 -464 1271 2512 O ATOM 1937 CB PHE A1047 -50.540-126.015 264.498 1.00110.71 C ANISOU 1937 CB PHE A1047 13261 13292 15511 -487 1134 1889 C ATOM 1938 CG PHE A1047 -50.516-125.168 263.259 1.00108.13 C ANISOU 1938 CG PHE A1047 12910 12887 15287 -480 984 1560 C ATOM 1939 CD1 PHE A1047 -49.562-125.376 262.276 1.00106.19 C ANISOU 1939 CD1 PHE A1047 12793 12373 15183 -555 764 1352 C ATOM 1940 CD2 PHE A1047 -51.454-124.167 263.074 1.00109.05 C ANISOU 1940 CD2 PHE A1047 12870 13220 15343 -363 1085 1490 C ATOM 1941 CE1 PHE A1047 -49.544-124.601 261.134 1.00105.24 C ANISOU 1941 CE1 PHE A1047 12651 12217 15119 -532 653 1107 C ATOM 1942 CE2 PHE A1047 -51.437-123.385 261.936 1.00108.14 C ANISOU 1942 CE2 PHE A1047 12742 13036 15312 -334 951 1245 C ATOM 1943 CZ PHE A1047 -50.482-123.605 260.964 1.00106.39 C ANISOU 1943 CZ PHE A1047 12655 12562 15208 -429 738 1066 C ATOM 1944 N GLU A1048 -51.022-129.352 265.546 1.00120.89 N ANISOU 1944 N GLU A1048 14433 14220 17279 -963 1303 2808 N ATOM 1945 CA GLU A1048 -51.275-130.139 266.748 1.00124.10 C ANISOU 1945 CA GLU A1048 14819 14719 17615 -972 1522 3301 C ATOM 1946 C GLU A1048 -49.978-130.541 267.437 1.00120.51 C ANISOU 1946 C GLU A1048 14670 14166 16953 -784 1441 3375 C ATOM 1947 O GLU A1048 -49.105-131.165 266.828 1.00115.50 O ANISOU 1947 O GLU A1048 14191 13150 16543 -843 1226 3253 O ATOM 1948 CB GLU A1048 -52.083-131.388 266.389 1.00130.30 C ANISOU 1948 CB GLU A1048 15403 15206 18900 -1362 1548 3618 C ATOM 1949 CG GLU A1048 -52.117-132.434 267.494 1.00138.73 C ANISOU 1949 CG GLU A1048 16499 16223 19991 -1412 1745 4189 C ATOM 1950 CD GLU A1048 -52.344-133.837 266.967 1.00144.99 C ANISOU 1950 CD GLU A1048 17257 16466 21368 -1807 1641 4403 C ATOM 1951 OE1 GLU A1048 -53.071-134.612 267.622 1.00150.45 O ANISOU 1951 OE1 GLU A1048 17776 17137 22252 -2011 1856 4940 O ATOM 1952 OE2 GLU A1048 -51.794-134.167 265.896 1.00143.96 O ANISOU 1952 OE2 GLU A1048 17280 15911 21507 -1909 1351 4037 O ATOM 1953 N GLY A1049 -49.858-130.173 268.710 1.00122.56 N ANISOU 1953 N GLY A1049 15008 14803 16757 -523 1608 3570 N ATOM 1954 CA GLY A1049 -48.743-130.603 269.529 1.00122.33 C ANISOU 1954 CA GLY A1049 15226 14768 16486 -330 1531 3722 C ATOM 1955 C GLY A1049 -47.487-129.770 269.432 1.00122.01 C ANISOU 1955 C GLY A1049 15390 14781 16188 -108 1272 3293 C ATOM 1956 O GLY A1049 -46.421-130.242 269.843 1.00123.37 O ANISOU 1956 O GLY A1049 15725 14885 16263 17 1128 3384 O ATOM 1957 N PHE A1050 -47.569-128.547 268.917 1.00119.28 N ANISOU 1957 N PHE A1050 15020 14551 15749 -56 1203 2859 N ATOM 1958 CA PHE A1050 -46.398-127.700 268.727 1.00114.69 C ANISOU 1958 CA PHE A1050 14594 13976 15005 86 949 2458 C ATOM 1959 C PHE A1050 -46.476-126.494 269.652 1.00115.22 C ANISOU 1959 C PHE A1050 14761 14435 14580 330 990 2274 C ATOM 1960 O PHE A1050 -47.454-125.740 269.616 1.00114.78 O ANISOU 1960 O PHE A1050 14624 14537 14449 371 1161 2170 O ATOM 1961 CB PHE A1050 -46.277-127.249 267.273 1.00108.74 C ANISOU 1961 CB PHE A1050 13772 12962 14584 -60 806 2099 C ATOM 1962 CG PHE A1050 -45.782-128.321 266.357 1.00108.61 C ANISOU 1962 CG PHE A1050 13748 12560 14961 -216 686 2145 C ATOM 1963 CD1 PHE A1050 -44.441-128.665 266.339 1.00108.55 C ANISOU 1963 CD1 PHE A1050 13853 12430 14960 -117 501 2103 C ATOM 1964 CD2 PHE A1050 -46.655-128.993 265.520 1.00109.08 C ANISOU 1964 CD2 PHE A1050 13681 12386 15379 -446 746 2214 C ATOM 1965 CE1 PHE A1050 -43.978-129.655 265.498 1.00109.28 C ANISOU 1965 CE1 PHE A1050 13963 12163 15395 -194 416 2121 C ATOM 1966 CE2 PHE A1050 -46.199-129.985 264.678 1.00109.86 C ANISOU 1966 CE2 PHE A1050 13828 12099 15815 -560 622 2193 C ATOM 1967 CZ PHE A1050 -44.859-130.317 264.665 1.00109.96 C ANISOU 1967 CZ PHE A1050 13984 11981 15815 -408 477 2143 C ATOM 1968 N ASP A1051 -45.439-126.316 270.475 1.00120.76 N ANISOU 1968 N ASP A1051 15642 15293 14948 509 815 2216 N ATOM 1969 CA ASP A1051 -45.345-125.112 271.291 1.00124.10 C ANISOU 1969 CA ASP A1051 16220 16033 14901 734 770 1927 C ATOM 1970 C ASP A1051 -45.246-123.864 270.426 1.00120.41 C ANISOU 1970 C ASP A1051 15757 15406 14588 680 641 1450 C ATOM 1971 O ASP A1051 -45.775-122.809 270.794 1.00121.98 O ANISOU 1971 O ASP A1051 16042 15766 14537 835 718 1210 O ATOM 1972 CB ASP A1051 -44.137-125.201 272.226 1.00128.99 C ANISOU 1972 CB ASP A1051 17011 16832 15168 892 516 1920 C ATOM 1973 CG ASP A1051 -44.245-126.349 273.210 1.00134.25 C ANISOU 1973 CG ASP A1051 17705 17700 15604 1008 656 2441 C ATOM 1974 OD1 ASP A1051 -45.378-126.788 273.493 1.00137.36 O ANISOU 1974 OD1 ASP A1051 18018 18201 15972 1011 995 2774 O ATOM 1975 OD2 ASP A1051 -43.195-126.807 273.708 1.00135.57 O ANISOU 1975 OD2 ASP A1051 17952 17933 15625 1101 430 2553 O ATOM 1976 N LEU A1052 -44.591-123.968 269.272 1.00110.40 N ANISOU 1976 N LEU A1052 14408 13816 13724 489 465 1326 N ATOM 1977 CA LEU A1052 -44.361-122.829 268.398 1.00102.50 C ANISOU 1977 CA LEU A1052 13408 12647 12890 426 340 945 C ATOM 1978 C LEU A1052 -44.479-123.264 266.945 1.00100.59 C ANISOU 1978 C LEU A1052 13000 12114 13106 225 355 977 C ATOM 1979 O LEU A1052 -43.996-124.334 266.566 1.00102.84 O ANISOU 1979 O LEU A1052 13227 12253 13594 132 305 1155 O ATOM 1980 CB LEU A1052 -42.981-122.212 268.650 1.00 96.83 C ANISOU 1980 CB LEU A1052 12798 11918 12074 440 22 690 C ATOM 1981 CG LEU A1052 -42.563-121.056 267.744 1.00 91.22 C ANISOU 1981 CG LEU A1052 12079 10989 11592 332 -120 355 C ATOM 1982 CD1 LEU A1052 -43.492-119.868 267.933 1.00 91.16 C ANISOU 1982 CD1 LEU A1052 12189 11003 11444 449 -3 121 C ATOM 1983 CD2 LEU A1052 -41.122-120.667 268.024 1.00 89.83 C ANISOU 1983 CD2 LEU A1052 11935 10810 11388 281 -451 184 C ATOM 1984 N VAL A1053 -45.127-122.426 266.140 1.00 97.86 N ANISOU 1984 N VAL A1053 12598 11686 12897 192 418 798 N ATOM 1985 CA VAL A1053 -45.274-122.642 264.706 1.00 95.86 C ANISOU 1985 CA VAL A1053 12209 11211 13000 34 407 778 C ATOM 1986 C VAL A1053 -44.731-121.416 263.986 1.00 92.70 C ANISOU 1986 C VAL A1053 11849 10694 12680 31 282 500 C ATOM 1987 O VAL A1053 -44.987-120.281 264.399 1.00 97.61 O ANISOU 1987 O VAL A1053 12566 11366 13155 142 294 326 O ATOM 1988 CB VAL A1053 -46.744-122.901 264.315 1.00 96.49 C ANISOU 1988 CB VAL A1053 12132 11338 13193 -13 607 912 C ATOM 1989 CG1 VAL A1053 -46.882-123.030 262.806 1.00 93.28 C ANISOU 1989 CG1 VAL A1053 11610 10741 13090 -157 542 839 C ATOM 1990 CG2 VAL A1053 -47.270-124.147 265.012 1.00 99.55 C ANISOU 1990 CG2 VAL A1053 12452 11802 13569 -67 741 1245 C ATOM 1991 N LEU A1054 -43.973-121.645 262.917 1.00 86.65 N ANISOU 1991 N LEU A1054 11020 9758 12145 -78 178 470 N ATOM 1992 CA LEU A1054 -43.401-120.567 262.123 1.00 81.74 C ANISOU 1992 CA LEU A1054 10402 9019 11637 -109 87 292 C ATOM 1993 C LEU A1054 -43.885-120.691 260.688 1.00 78.82 C ANISOU 1993 C LEU A1054 9924 8559 11466 -166 151 318 C ATOM 1994 O LEU A1054 -43.727-121.744 260.061 1.00 76.08 O ANISOU 1994 O LEU A1054 9513 8165 11229 -225 148 401 O ATOM 1995 CB LEU A1054 -41.873-120.590 262.180 1.00 80.51 C ANISOU 1995 CB LEU A1054 10237 8821 11532 -161 -94 256 C ATOM 1996 CG LEU A1054 -41.302-120.362 263.581 1.00 82.00 C ANISOU 1996 CG LEU A1054 10529 9133 11493 -108 -233 194 C ATOM 1997 CD1 LEU A1054 -39.788-120.229 263.545 1.00 81.11 C ANISOU 1997 CD1 LEU A1054 10336 9004 11477 -187 -451 156 C ATOM 1998 CD2 LEU A1054 -41.938-119.136 264.218 1.00 83.16 C ANISOU 1998 CD2 LEU A1054 10831 9297 11470 -32 -221 -7 C ATOM 1999 N LEU A1055 -44.478-119.619 260.176 1.00 79.97 N ANISOU 1999 N LEU A1055 10070 8676 11639 -124 197 238 N ATOM 2000 CA LEU A1055 -45.015-119.585 258.823 1.00 77.22 C ANISOU 2000 CA LEU A1055 9624 8299 11417 -144 237 268 C ATOM 2001 C LEU A1055 -44.135-118.675 257.979 1.00 78.94 C ANISOU 2001 C LEU A1055 9860 8403 11732 -159 181 222 C ATOM 2002 O LEU A1055 -44.143-117.452 258.155 1.00 78.29 O ANISOU 2002 O LEU A1055 9851 8233 11662 -112 178 159 O ATOM 2003 CB LEU A1055 -46.467-119.115 258.823 1.00 75.49 C ANISOU 2003 CB LEU A1055 9347 8175 11161 -51 346 289 C ATOM 2004 CG LEU A1055 -47.420-120.105 259.492 1.00 72.46 C ANISOU 2004 CG LEU A1055 8868 7934 10728 -76 433 406 C ATOM 2005 CD1 LEU A1055 -48.867-119.729 259.224 1.00 73.13 C ANISOU 2005 CD1 LEU A1055 8795 8161 10828 4 537 465 C ATOM 2006 CD2 LEU A1055 -47.133-121.519 259.011 1.00 70.34 C ANISOU 2006 CD2 LEU A1055 8546 7606 10575 -235 369 480 C ATOM 2007 N GLY A1056 -43.371-119.276 257.076 1.00 81.97 N ANISOU 2007 N GLY A1056 10182 8774 12191 -212 152 265 N ATOM 2008 CA GLY A1056 -42.544-118.517 256.165 1.00 82.63 C ANISOU 2008 CA GLY A1056 10235 8799 12363 -226 147 295 C ATOM 2009 C GLY A1056 -43.054-118.602 254.746 1.00 82.30 C ANISOU 2009 C GLY A1056 10142 8823 12307 -170 206 351 C ATOM 2010 O GLY A1056 -42.963-119.653 254.108 1.00 82.76 O ANISOU 2010 O GLY A1056 10169 8948 12329 -159 203 340 O ATOM 2011 N CYS A1057 -43.603-117.506 254.242 1.00 77.01 N ANISOU 2011 N CYS A1057 9485 8127 11649 -111 245 402 N ATOM 2012 CA CYS A1057 -44.135-117.472 252.893 1.00 72.66 C ANISOU 2012 CA CYS A1057 8888 7689 11032 -28 277 477 C ATOM 2013 C CYS A1057 -43.471-116.354 252.104 1.00 72.73 C ANISOU 2013 C CYS A1057 8899 7636 11099 2 339 631 C ATOM 2014 O CYS A1057 -42.981-115.370 252.664 1.00 73.92 O ANISOU 2014 O CYS A1057 9095 7599 11392 -55 343 665 O ATOM 2015 CB CYS A1057 -45.654-117.281 252.895 1.00 69.08 C ANISOU 2015 CB CYS A1057 8403 7317 10526 56 271 471 C ATOM 2016 SG CYS A1057 -46.406-117.316 251.251 1.00 65.72 S ANISOU 2016 SG CYS A1057 7902 7100 9970 168 238 550 S ATOM 2017 N SER A1058 -43.460-116.522 250.790 1.00 73.81 N ANISOU 2017 N SER A1058 8996 7929 11119 88 381 728 N ATOM 2018 CA SER A1058 -42.903-115.540 249.878 1.00 73.81 C ANISOU 2018 CA SER A1058 8982 7921 11143 136 478 956 C ATOM 2019 C SER A1058 -44.016-114.662 249.319 1.00 75.27 C ANISOU 2019 C SER A1058 9199 8126 11274 281 484 1080 C ATOM 2020 O SER A1058 -45.179-115.069 249.256 1.00 77.48 O ANISOU 2020 O SER A1058 9460 8540 11438 364 406 986 O ATOM 2021 CB SER A1058 -42.151-116.232 248.743 1.00 74.16 C ANISOU 2021 CB SER A1058 8969 8185 11023 205 554 1020 C ATOM 2022 OG SER A1058 -41.288-115.331 248.077 1.00 77.72 O ANISOU 2022 OG SER A1058 9364 8631 11534 211 694 1298 O ATOM 2023 N THR A1059 -43.649-113.446 248.924 1.00 78.12 N ANISOU 2023 N THR A1059 9587 8345 11751 306 571 1322 N ATOM 2024 CA THR A1059 -44.596-112.481 248.386 1.00 78.19 C ANISOU 2024 CA THR A1059 9638 8332 11740 485 589 1502 C ATOM 2025 C THR A1059 -44.414-112.423 246.874 1.00 80.86 C ANISOU 2025 C THR A1059 9935 8926 11863 622 669 1766 C ATOM 2026 O THR A1059 -43.317-112.132 246.382 1.00 65.38 O ANISOU 2026 O THR A1059 7947 6945 9948 560 799 1977 O ATOM 2027 CB THR A1059 -44.402-111.104 249.013 1.00 81.55 C ANISOU 2027 CB THR A1059 10169 8354 12462 445 626 1606 C ATOM 2028 OG1 THR A1059 -44.280-111.252 250.431 1.00 81.97 O ANISOU 2028 OG1 THR A1059 10280 8215 12650 312 548 1324 O ATOM 2029 CG2 THR A1059 -45.608-110.219 248.714 1.00 65.55 C ANISOU 2029 CG2 THR A1059 8201 6273 10431 694 632 1741 C ATOM 2030 N TRP A1060 -45.502-112.689 246.137 1.00 83.26 N ANISOU 2030 N TRP A1060 10214 9506 11915 815 590 1770 N ATOM 2031 CA TRP A1060 -45.377-112.945 244.711 1.00 87.47 C ANISOU 2031 CA TRP A1060 10727 10385 12122 971 623 1934 C ATOM 2032 C TRP A1060 -46.400-112.201 243.858 1.00 92.78 C ANISOU 2032 C TRP A1060 11398 11224 12629 1225 579 2180 C ATOM 2033 O TRP A1060 -46.714-112.670 242.753 1.00 95.10 O ANISOU 2033 O TRP A1060 11673 11907 12555 1385 510 2206 O ATOM 2034 CB TRP A1060 -45.489-114.436 244.439 1.00 82.97 C ANISOU 2034 CB TRP A1060 10133 10093 11299 951 501 1615 C ATOM 2035 CG TRP A1060 -44.157-115.038 244.489 1.00 81.34 C ANISOU 2035 CG TRP A1060 9933 9864 11110 849 621 1556 C ATOM 2036 CD1 TRP A1060 -43.499-115.489 245.595 1.00 81.20 C ANISOU 2036 CD1 TRP A1060 9897 9620 11334 653 627 1383 C ATOM 2037 CD2 TRP A1060 -43.257-115.185 243.393 1.00 82.58 C ANISOU 2037 CD2 TRP A1060 10090 10263 11024 975 775 1714 C ATOM 2038 NE1 TRP A1060 -42.252-115.944 245.246 1.00 82.28 N ANISOU 2038 NE1 TRP A1060 9999 9841 11423 650 759 1418 N ATOM 2039 CE2 TRP A1060 -42.079-115.768 243.897 1.00 83.44 C ANISOU 2039 CE2 TRP A1060 10152 10278 11272 851 873 1617 C ATOM 2040 CE3 TRP A1060 -43.340-114.899 242.026 1.00 84.72 C ANISOU 2040 CE3 TRP A1060 10388 10866 10936 1214 849 1942 C ATOM 2041 CZ2 TRP A1060 -40.991-116.070 243.087 1.00 86.48 C ANISOU 2041 CZ2 TRP A1060 10492 10887 11477 968 1066 1739 C ATOM 2042 CZ3 TRP A1060 -42.265-115.202 241.223 1.00 88.95 C ANISOU 2042 CZ3 TRP A1060 10912 11634 11252 1327 1050 2058 C ATOM 2043 CH2 TRP A1060 -41.102-115.779 241.755 1.00 89.67 C ANISOU 2043 CH2 TRP A1060 10932 11623 11516 1209 1171 1956 C ATOM 2044 N GLY A1061 -46.902-111.064 244.308 1.00 98.02 N ANISOU 2044 N GLY A1061 12094 11616 13533 1296 606 2353 N ATOM 2045 CA GLY A1061 -47.896-110.353 243.533 1.00104.45 C ANISOU 2045 CA GLY A1061 12891 12589 14207 1584 560 2618 C ATOM 2046 C GLY A1061 -47.340-109.571 242.364 1.00112.64 C ANISOU 2046 C GLY A1061 13987 13702 15110 1737 711 3082 C ATOM 2047 O GLY A1061 -46.533-108.651 242.545 1.00115.91 O ANISOU 2047 O GLY A1061 14480 13749 15810 1651 889 3347 O ATOM 2048 N ASP A1062 -47.764-109.946 241.156 1.00115.61 N ANISOU 2048 N ASP A1062 14322 14562 15045 1953 630 3188 N ATOM 2049 CA ASP A1062 -47.364-109.233 239.950 1.00123.48 C ANISOU 2049 CA ASP A1062 15371 15728 15817 2161 783 3683 C ATOM 2050 C ASP A1062 -48.123-107.918 239.813 1.00127.04 C ANISOU 2050 C ASP A1062 15857 15989 16425 2406 798 4090 C ATOM 2051 O ASP A1062 -47.516-106.855 239.642 1.00131.92 O ANISOU 2051 O ASP A1062 16566 16291 17266 2420 1009 4527 O ATOM 2052 CB ASP A1062 -47.599-110.123 238.725 1.00128.18 C ANISOU 2052 CB ASP A1062 15942 16951 15810 2350 662 3610 C ATOM 2053 CG ASP A1062 -47.247-109.437 237.414 1.00135.47 C ANISOU 2053 CG ASP A1062 16924 18155 16392 2622 831 4151 C ATOM 2054 OD1 ASP A1062 -46.445-108.481 237.423 1.00138.98 O ANISOU 2054 OD1 ASP A1062 17412 18291 17102 2575 1105 4588 O ATOM 2055 OD2 ASP A1062 -47.768-109.870 236.366 1.00137.60 O ANISOU 2055 OD2 ASP A1062 17196 18964 16120 2875 679 4147 O ATOM 2056 N ASP A1063 -49.454-107.973 239.875 1.00123.16 N ANISOU 2056 N ASP A1063 15277 15675 15844 2605 575 3975 N ATOM 2057 CA ASP A1063 -50.309-106.795 239.872 1.00122.29 C ANISOU 2057 CA ASP A1063 15178 15380 15907 2895 572 4314 C ATOM 2058 C ASP A1063 -50.663-106.352 241.286 1.00117.24 C ANISOU 2058 C ASP A1063 14563 14223 15759 2808 588 4087 C ATOM 2059 O ASP A1063 -50.564-105.166 241.620 1.00117.12 O ANISOU 2059 O ASP A1063 14691 13715 16095 2904 726 4348 O ATOM 2060 CB ASP A1063 -51.582-107.097 239.069 1.00125.63 C ANISOU 2060 CB ASP A1063 15434 16375 15923 3210 310 4348 C ATOM 2061 CG ASP A1063 -52.291-105.848 238.596 1.00131.60 C ANISOU 2061 CG ASP A1063 16204 17076 16724 3618 331 4864 C ATOM 2062 OD1 ASP A1063 -51.987-105.367 237.484 1.00135.25 O ANISOU 2062 OD1 ASP A1063 16747 17735 16908 3828 411 5336 O ATOM 2063 OD2 ASP A1063 -53.172-105.359 239.327 1.00132.56 O ANISOU 2063 OD2 ASP A1063 16252 16976 17137 3764 279 4818 O ATOM 2064 N SER A1064 -51.054-107.305 242.131 1.00113.93 N ANISOU 2064 N SER A1064 14027 13897 15363 2632 455 3599 N ATOM 2065 CA SER A1064 -51.423-107.076 243.520 1.00111.32 C ANISOU 2065 CA SER A1064 13710 13188 15398 2568 477 3332 C ATOM 2066 C SER A1064 -50.851-108.214 244.349 1.00107.05 C ANISOU 2066 C SER A1064 13145 12643 14885 2200 449 2885 C ATOM 2067 O SER A1064 -50.446-109.239 243.809 1.00105.36 O ANISOU 2067 O SER A1064 12873 12748 14410 2047 378 2757 O ATOM 2068 CB SER A1064 -52.941-107.011 243.682 1.00112.49 C ANISOU 2068 CB SER A1064 13656 13576 15509 2861 338 3301 C ATOM 2069 OG SER A1064 -53.536-108.209 243.210 1.00110.61 O ANISOU 2069 OG SER A1064 13178 13901 14949 2794 117 3107 O ATOM 2070 N ILE A1065 -50.864-108.043 245.675 1.00106.76 N ANISOU 2070 N ILE A1065 13169 12254 15141 2097 501 2639 N ATOM 2071 CA ILE A1065 -50.265-109.022 246.581 1.00105.51 C ANISOU 2071 CA ILE A1065 13009 12051 15027 1771 487 2265 C ATOM 2072 C ILE A1065 -50.810-110.415 246.299 1.00104.54 C ANISOU 2072 C ILE A1065 12684 12396 14640 1685 326 2052 C ATOM 2073 O ILE A1065 -52.022-110.607 246.154 1.00104.59 O ANISOU 2073 O ILE A1065 12501 12685 14553 1842 208 2046 O ATOM 2074 CB ILE A1065 -50.525-108.621 248.044 1.00105.21 C ANISOU 2074 CB ILE A1065 13052 11673 15249 1767 540 2039 C ATOM 2075 CG1 ILE A1065 -50.009-107.210 248.324 1.00107.98 C ANISOU 2075 CG1 ILE A1065 13649 11485 15894 1840 655 2191 C ATOM 2076 CG2 ILE A1065 -49.884-109.623 248.992 1.00102.51 C ANISOU 2076 CG2 ILE A1065 12716 11315 14920 1454 519 1703 C ATOM 2077 CD1 ILE A1065 -50.327-106.721 249.720 1.00108.66 C ANISOU 2077 CD1 ILE A1065 13869 11238 16180 1906 693 1922 C ATOM 2078 N GLU A1066 -49.907-111.395 246.226 1.00104.12 N ANISOU 2078 N GLU A1066 12659 12408 14495 1431 311 1879 N ATOM 2079 CA GLU A1066 -50.267-112.797 246.058 1.00104.23 C ANISOU 2079 CA GLU A1066 12539 12743 14318 1302 151 1627 C ATOM 2080 C GLU A1066 -49.318-113.668 246.869 1.00100.81 C ANISOU 2080 C GLU A1066 12178 12140 13985 1026 193 1376 C ATOM 2081 O GLU A1066 -48.127-113.365 246.978 1.00101.10 O ANISOU 2081 O GLU A1066 12339 11965 14109 939 317 1434 O ATOM 2082 CB GLU A1066 -50.228-113.222 244.583 1.00108.63 C ANISOU 2082 CB GLU A1066 13077 13669 14528 1393 44 1707 C ATOM 2083 CG GLU A1066 -51.372-112.682 243.741 1.00114.89 C ANISOU 2083 CG GLU A1066 13743 14762 15147 1669 -86 1919 C ATOM 2084 CD GLU A1066 -51.467-113.357 242.388 1.00120.99 C ANISOU 2084 CD GLU A1066 14494 15975 15501 1741 -266 1891 C ATOM 2085 OE1 GLU A1066 -51.510-112.644 241.364 1.00126.43 O ANISOU 2085 OE1 GLU A1066 15220 16861 15957 1996 -255 2202 O ATOM 2086 OE2 GLU A1066 -51.494-114.605 242.348 1.00120.84 O ANISOU 2086 OE2 GLU A1066 14445 16094 15374 1555 -424 1555 O ATOM 2087 N LEU A1067 -49.851-114.752 247.430 1.00 96.70 N ANISOU 2087 N LEU A1067 11554 11718 13468 885 85 1131 N ATOM 2088 CA LEU A1067 -49.041-115.695 248.187 1.00 91.04 C ANISOU 2088 CA LEU A1067 10901 10859 12832 656 108 922 C ATOM 2089 C LEU A1067 -48.298-116.644 247.249 1.00 89.90 C ANISOU 2089 C LEU A1067 10811 10850 12498 600 53 827 C ATOM 2090 O LEU A1067 -48.649-116.807 246.077 1.00 92.22 O ANISOU 2090 O LEU A1067 11082 11402 12555 711 -47 850 O ATOM 2091 CB LEU A1067 -49.902-116.514 249.153 1.00 89.41 C ANISOU 2091 CB LEU A1067 10570 10681 12719 532 40 756 C ATOM 2092 CG LEU A1067 -50.603-115.855 250.347 1.00 90.04 C ANISOU 2092 CG LEU A1067 10595 10663 12952 599 134 791 C ATOM 2093 CD1 LEU A1067 -49.707-114.828 251.012 1.00 90.28 C ANISOU 2093 CD1 LEU A1067 10821 10389 13094 646 273 827 C ATOM 2094 CD2 LEU A1067 -51.936-115.240 249.949 1.00 93.07 C ANISOU 2094 CD2 LEU A1067 10793 11256 13313 809 94 927 C ATOM 2095 N GLN A1068 -47.259-117.276 247.790 1.00 86.51 N ANISOU 2095 N GLN A1068 10459 10260 12149 460 115 709 N ATOM 2096 CA GLN A1068 -46.558-118.325 247.062 1.00 85.56 C ANISOU 2096 CA GLN A1068 10401 10239 11869 444 83 572 C ATOM 2097 C GLN A1068 -47.507-119.487 246.791 1.00 87.31 C ANISOU 2097 C GLN A1068 10582 10586 12006 376 -126 341 C ATOM 2098 O GLN A1068 -48.304-119.869 247.652 1.00 86.89 O ANISOU 2098 O GLN A1068 10438 10457 12119 237 -199 271 O ATOM 2099 CB GLN A1068 -45.344-118.794 247.866 1.00 83.10 C ANISOU 2099 CB GLN A1068 10143 9725 11707 332 180 509 C ATOM 2100 CG GLN A1068 -44.189-119.315 247.030 1.00 82.66 C ANISOU 2100 CG GLN A1068 10144 9758 11504 419 261 488 C ATOM 2101 CD GLN A1068 -44.379-120.756 246.607 1.00 80.09 C ANISOU 2101 CD GLN A1068 9893 9490 11048 429 135 210 C ATOM 2102 OE1 GLN A1068 -45.133-121.504 247.228 1.00 77.52 O ANISOU 2102 OE1 GLN A1068 9562 9052 10838 290 -4 50 O ATOM 2103 NE2 GLN A1068 -43.692-121.155 245.543 1.00 81.15 N ANISOU 2103 NE2 GLN A1068 10103 9785 10945 600 194 157 N ATOM 2104 N ASP A1069 -47.415-120.053 245.582 1.00 90.26 N ANISOU 2104 N ASP A1069 11024 11156 12115 470 -221 222 N ATOM 2105 CA ASP A1069 -48.416-121.015 245.124 1.00 96.06 C ANISOU 2105 CA ASP A1069 11724 12015 12759 391 -485 -18 C ATOM 2106 C ASP A1069 -48.527-122.212 246.064 1.00 92.61 C ANISOU 2106 C ASP A1069 11291 11322 12575 150 -558 -221 C ATOM 2107 O ASP A1069 -49.628-122.623 246.426 1.00 91.64 O ANISOU 2107 O ASP A1069 11024 11200 12593 -23 -719 -279 O ATOM 2108 CB ASP A1069 -48.092-121.487 243.705 1.00105.23 C ANISOU 2108 CB ASP A1069 13029 13406 13549 556 -581 -181 C ATOM 2109 CG ASP A1069 -48.463-120.467 242.648 1.00113.99 C ANISOU 2109 CG ASP A1069 14099 14857 14355 786 -597 32 C ATOM 2110 OD1 ASP A1069 -49.179-119.498 242.977 1.00117.13 O ANISOU 2110 OD1 ASP A1069 14343 15290 14872 803 -587 274 O ATOM 2111 OD2 ASP A1069 -48.049-120.641 241.484 1.00118.03 O ANISOU 2111 OD2 ASP A1069 14744 15611 14490 984 -613 -34 O ATOM 2112 N ASP A1070 -47.405-122.801 246.460 1.00 91.02 N ANISOU 2112 N ASP A1070 11227 10908 12447 139 -435 -293 N ATOM 2113 CA ASP A1070 -47.497-123.976 247.324 1.00 89.09 C ANISOU 2113 CA ASP A1070 11009 10398 12442 -64 -501 -438 C ATOM 2114 C ASP A1070 -48.129-123.633 248.667 1.00 86.97 C ANISOU 2114 C ASP A1070 10582 10037 12424 -222 -441 -261 C ATOM 2115 O ASP A1070 -48.789-124.480 249.278 1.00 88.64 O ANISOU 2115 O ASP A1070 10732 10122 12826 -424 -532 -310 O ATOM 2116 CB ASP A1070 -46.115-124.597 247.513 1.00 88.50 C ANISOU 2116 CB ASP A1070 11099 10136 12392 19 -369 -503 C ATOM 2117 CG ASP A1070 -45.491-125.007 246.202 1.00 93.56 C ANISOU 2117 CG ASP A1070 11902 10896 12752 230 -387 -693 C ATOM 2118 OD1 ASP A1070 -46.204-125.610 245.371 1.00 96.75 O ANISOU 2118 OD1 ASP A1070 12378 11367 13016 213 -604 -936 O ATOM 2119 OD2 ASP A1070 -44.297-124.711 245.994 1.00 94.34 O ANISOU 2119 OD2 ASP A1070 12042 11046 12757 417 -187 -601 O ATOM 2120 N PHE A1071 -47.971-122.390 249.124 1.00 84.57 N ANISOU 2120 N PHE A1071 10218 9793 12122 -126 -285 -51 N ATOM 2121 CA PHE A1071 -48.546-121.965 250.389 1.00 82.19 C ANISOU 2121 CA PHE A1071 9802 9438 11990 -204 -206 84 C ATOM 2122 C PHE A1071 -50.046-121.691 250.287 1.00 85.88 C ANISOU 2122 C PHE A1071 10055 10094 12481 -234 -298 142 C ATOM 2123 O PHE A1071 -50.719-121.626 251.332 1.00 85.90 O ANISOU 2123 O PHE A1071 9928 10091 12619 -301 -228 239 O ATOM 2124 CB PHE A1071 -47.821-120.713 250.892 1.00 77.94 C ANISOU 2124 CB PHE A1071 9314 8851 11449 -79 -37 228 C ATOM 2125 CG PHE A1071 -47.785-120.576 252.394 1.00 75.95 C ANISOU 2125 CG PHE A1071 9061 8476 11322 -138 59 280 C ATOM 2126 CD1 PHE A1071 -46.652-120.931 253.113 1.00 75.68 C ANISOU 2126 CD1 PHE A1071 9132 8291 11331 -180 106 260 C ATOM 2127 CD2 PHE A1071 -48.876-120.076 253.086 1.00 74.86 C ANISOU 2127 CD2 PHE A1071 8806 8415 11222 -113 103 355 C ATOM 2128 CE1 PHE A1071 -46.616-120.797 254.496 1.00 74.33 C ANISOU 2128 CE1 PHE A1071 8979 8056 11205 -208 167 300 C ATOM 2129 CE2 PHE A1071 -48.847-119.944 254.465 1.00 74.53 C ANISOU 2129 CE2 PHE A1071 8791 8307 11219 -120 205 388 C ATOM 2130 CZ PHE A1071 -47.717-120.304 255.170 1.00 73.73 C ANISOU 2130 CZ PHE A1071 8825 8064 11124 -174 224 353 C ATOM 2131 N ILE A1072 -50.597-121.559 249.080 1.00 90.40 N ANISOU 2131 N ILE A1072 10565 10874 12907 -168 -452 98 N ATOM 2132 CA ILE A1072 -51.974-121.102 248.941 1.00 95.39 C ANISOU 2132 CA ILE A1072 10942 11742 13558 -147 -546 197 C ATOM 2133 C ILE A1072 -52.970-122.125 249.488 1.00 94.95 C ANISOU 2133 C ILE A1072 10675 11691 13710 -411 -663 154 C ATOM 2134 O ILE A1072 -53.885-121.703 250.209 1.00 94.91 O ANISOU 2134 O ILE A1072 10433 11805 13825 -404 -582 321 O ATOM 2135 CB ILE A1072 -52.322-120.658 247.495 1.00100.05 C ANISOU 2135 CB ILE A1072 11503 12608 13905 15 -714 192 C ATOM 2136 CG1 ILE A1072 -52.374-121.819 246.485 1.00106.40 C ANISOU 2136 CG1 ILE A1072 12367 13482 14577 -109 -985 -77 C ATOM 2137 CG2 ILE A1072 -51.375-119.559 247.032 1.00 96.58 C ANISOU 2137 CG2 ILE A1072 11243 12153 13301 264 -546 333 C ATOM 2138 CD1 ILE A1072 -52.593-121.495 245.064 1.00110.89 C ANISOU 2138 CD1 ILE A1072 12955 14360 14819 71 -1167 -116 C ATOM 2139 N PRO A1073 -52.884-123.444 249.213 1.00 96.93 N ANISOU 2139 N PRO A1073 10988 11807 14034 -641 -837 -44 N ATOM 2140 CA PRO A1073 -53.900-124.329 249.788 1.00100.58 C ANISOU 2140 CA PRO A1073 11210 12243 14762 -937 -937 -17 C ATOM 2141 C PRO A1073 -53.861-124.352 251.303 1.00 98.49 C ANISOU 2141 C PRO A1073 10896 11848 14678 -991 -675 191 C ATOM 2142 O PRO A1073 -54.914-124.408 251.953 1.00102.04 O ANISOU 2142 O PRO A1073 11044 12432 15295 -1109 -630 369 O ATOM 2143 CB PRO A1073 -53.554-125.702 249.183 1.00103.34 C ANISOU 2143 CB PRO A1073 11740 12354 15169 -1150 -1166 -299 C ATOM 2144 CG PRO A1073 -52.693-125.390 248.003 1.00102.96 C ANISOU 2144 CG PRO A1073 11952 12371 14795 -906 -1228 -492 C ATOM 2145 CD PRO A1073 -51.891-124.255 248.481 1.00 97.80 C ANISOU 2145 CD PRO A1073 11383 11744 14034 -649 -931 -291 C ATOM 2146 N LEU A1074 -52.663-124.280 251.886 1.00 92.72 N ANISOU 2146 N LEU A1074 10433 10903 13892 -888 -497 189 N ATOM 2147 CA LEU A1074 -52.550-124.211 253.338 1.00 89.53 C ANISOU 2147 CA LEU A1074 10018 10426 13574 -890 -264 375 C ATOM 2148 C LEU A1074 -53.185-122.934 253.875 1.00 92.46 C ANISOU 2148 C LEU A1074 10230 11034 13867 -684 -95 537 C ATOM 2149 O LEU A1074 -53.831-122.951 254.930 1.00 94.16 O ANISOU 2149 O LEU A1074 10283 11338 14155 -707 62 710 O ATOM 2150 CB LEU A1074 -51.080-124.311 253.751 1.00 85.90 C ANISOU 2150 CB LEU A1074 9861 9736 13042 -799 -165 320 C ATOM 2151 CG LEU A1074 -50.733-124.467 255.236 1.00 86.05 C ANISOU 2151 CG LEU A1074 9932 9667 13097 -803 19 477 C ATOM 2152 CD1 LEU A1074 -50.501-123.117 255.910 1.00 85.23 C ANISOU 2152 CD1 LEU A1074 9866 9683 12833 -575 180 534 C ATOM 2153 CD2 LEU A1074 -51.792-125.278 255.974 1.00 88.55 C ANISOU 2153 CD2 LEU A1074 10041 10011 13593 -1011 61 661 C ATOM 2154 N PHE A1075 -53.022-121.816 253.160 1.00 93.36 N ANISOU 2154 N PHE A1075 10396 11249 13829 -455 -106 500 N ATOM 2155 CA PHE A1075 -53.603-120.559 253.619 1.00 93.11 C ANISOU 2155 CA PHE A1075 10258 11375 13746 -212 50 631 C ATOM 2156 C PHE A1075 -55.124-120.640 253.668 1.00 99.04 C ANISOU 2156 C PHE A1075 10622 12410 14600 -240 31 771 C ATOM 2157 O PHE A1075 -55.748-120.158 254.622 1.00 99.11 O ANISOU 2157 O PHE A1075 10488 12544 14625 -104 234 913 O ATOM 2158 CB PHE A1075 -53.173-119.404 252.716 1.00 90.88 C ANISOU 2158 CB PHE A1075 10106 11094 13329 23 24 608 C ATOM 2159 CG PHE A1075 -53.803-118.090 253.083 1.00 87.97 C ANISOU 2159 CG PHE A1075 9663 10819 12942 306 167 732 C ATOM 2160 CD1 PHE A1075 -53.255-117.305 254.084 1.00 84.95 C ANISOU 2160 CD1 PHE A1075 9478 10259 12541 449 351 718 C ATOM 2161 CD2 PHE A1075 -54.950-117.649 252.442 1.00 89.06 C ANISOU 2161 CD2 PHE A1075 9539 11218 13081 448 98 845 C ATOM 2162 CE1 PHE A1075 -53.835-116.100 254.433 1.00 85.77 C ANISOU 2162 CE1 PHE A1075 9563 10390 12636 745 482 787 C ATOM 2163 CE2 PHE A1075 -55.535-116.446 252.788 1.00 89.79 C ANISOU 2163 CE2 PHE A1075 9574 11370 13174 767 246 963 C ATOM 2164 CZ PHE A1075 -54.976-115.670 253.785 1.00 87.98 C ANISOU 2164 CZ PHE A1075 9587 10907 12934 924 448 921 C ATOM 2165 N ASP A1076 -55.740-121.243 252.645 1.00105.92 N ANISOU 2165 N ASP A1076 11303 13413 15528 -404 -218 725 N ATOM 2166 CA ASP A1076 -57.196-121.327 252.609 1.00113.86 C ANISOU 2166 CA ASP A1076 11865 14731 16665 -462 -281 874 C ATOM 2167 C ASP A1076 -57.741-122.178 253.749 1.00115.68 C ANISOU 2167 C ASP A1076 11882 14966 17105 -697 -142 1029 C ATOM 2168 O ASP A1076 -58.875-121.962 254.194 1.00118.53 O ANISOU 2168 O ASP A1076 11852 15616 17567 -657 -35 1241 O ATOM 2169 CB ASP A1076 -57.655-121.896 251.266 1.00119.83 C ANISOU 2169 CB ASP A1076 12479 15619 17433 -639 -647 747 C ATOM 2170 CG ASP A1076 -57.509-120.906 250.133 1.00122.93 C ANISOU 2170 CG ASP A1076 12962 16161 17584 -344 -761 707 C ATOM 2171 OD1 ASP A1076 -56.854-119.860 250.337 1.00121.90 O ANISOU 2171 OD1 ASP A1076 13060 15931 17325 -52 -555 764 O ATOM 2172 OD2 ASP A1076 -58.041-121.173 249.036 1.00126.89 O ANISOU 2172 OD2 ASP A1076 13315 16875 18024 -413 -1069 625 O ATOM 2173 N SER A1077 -56.955-123.141 254.240 1.00112.92 N ANISOU 2173 N SER A1077 11762 14319 16823 -919 -118 969 N ATOM 2174 CA SER A1077 -57.420-124.099 255.234 1.00112.48 C ANISOU 2174 CA SER A1077 11525 14232 16980 -1178 1 1165 C ATOM 2175 C SER A1077 -56.904-123.786 256.633 1.00111.16 C ANISOU 2175 C SER A1077 11532 14018 16685 -996 335 1302 C ATOM 2176 O SER A1077 -56.770-124.702 257.453 1.00112.32 O ANISOU 2176 O SER A1077 11701 14036 16941 -1190 434 1446 O ATOM 2177 CB SER A1077 -57.016-125.516 254.829 1.00112.24 C ANISOU 2177 CB SER A1077 11625 13876 17145 -1553 -226 1038 C ATOM 2178 OG SER A1077 -57.741-125.949 253.693 1.00113.98 O ANISOU 2178 OG SER A1077 11630 14175 17502 -1775 -560 910 O ATOM 2179 N LEU A1078 -56.625-122.511 256.930 1.00108.49 N ANISOU 2179 N LEU A1078 11333 13774 16116 -623 496 1261 N ATOM 2180 CA LEU A1078 -56.047-122.165 258.227 1.00106.80 C ANISOU 2180 CA LEU A1078 11338 13514 15726 -438 756 1313 C ATOM 2181 C LEU A1078 -56.962-122.569 259.379 1.00114.11 C ANISOU 2181 C LEU A1078 11986 14680 16692 -468 1014 1610 C ATOM 2182 O LEU A1078 -56.489-123.048 260.419 1.00116.27 O ANISOU 2182 O LEU A1078 12414 14884 16878 -494 1165 1713 O ATOM 2183 CB LEU A1078 -55.744-120.671 258.284 1.00100.87 C ANISOU 2183 CB LEU A1078 10771 12790 14763 -51 848 1184 C ATOM 2184 CG LEU A1078 -54.357-120.297 257.758 1.00 95.54 C ANISOU 2184 CG LEU A1078 10480 11819 14001 -20 706 954 C ATOM 2185 CD1 LEU A1078 -54.132-118.807 257.888 1.00 93.78 C ANISOU 2185 CD1 LEU A1078 10430 11566 13639 315 794 857 C ATOM 2186 CD2 LEU A1078 -53.285-121.076 258.504 1.00 92.34 C ANISOU 2186 CD2 LEU A1078 10316 11213 13555 -159 716 925 C ATOM 2187 N GLU A1079 -58.277-122.375 259.219 1.00119.50 N ANISOU 2187 N GLU A1079 12231 15685 17490 -444 1077 1784 N ATOM 2188 CA GLU A1079 -59.212-122.765 260.271 1.00128.92 C ANISOU 2188 CA GLU A1079 13086 17165 18732 -471 1364 2125 C ATOM 2189 C GLU A1079 -59.054-124.237 260.632 1.00130.96 C ANISOU 2189 C GLU A1079 13316 17239 19203 -897 1335 2316 C ATOM 2190 O GLU A1079 -59.196-124.616 261.800 1.00131.92 O ANISOU 2190 O GLU A1079 13393 17476 19256 -885 1617 2594 O ATOM 2191 CB GLU A1079 -60.645-122.464 259.838 1.00134.13 C ANISOU 2191 CB GLU A1079 13193 18212 19559 -437 1385 2303 C ATOM 2192 CG GLU A1079 -61.000-122.922 258.428 1.00136.91 C ANISOU 2192 CG GLU A1079 13331 18511 20179 -751 987 2202 C ATOM 2193 CD GLU A1079 -60.661-121.880 257.383 1.00137.02 C ANISOU 2193 CD GLU A1079 13538 18485 20039 -476 790 1928 C ATOM 2194 OE1 GLU A1079 -60.839-122.159 256.179 1.00138.00 O ANISOU 2194 OE1 GLU A1079 13556 18594 20284 -668 449 1808 O ATOM 2195 OE2 GLU A1079 -60.216-120.779 257.770 1.00135.97 O ANISOU 2195 OE2 GLU A1079 13675 18330 19659 -67 970 1835 O ATOM 2196 N GLU A1080 -58.751-125.080 259.643 1.00131.47 N ANISOU 2196 N GLU A1080 13435 17006 19514 -1251 1001 2174 N ATOM 2197 CA GLU A1080 -58.623-126.511 259.888 1.00134.89 C ANISOU 2197 CA GLU A1080 13868 17169 20215 -1661 942 2339 C ATOM 2198 C GLU A1080 -57.344-126.867 260.637 1.00131.18 C ANISOU 2198 C GLU A1080 13861 16409 19571 -1580 1028 2312 C ATOM 2199 O GLU A1080 -57.280-127.936 261.254 1.00133.18 O ANISOU 2199 O GLU A1080 14122 16491 19990 -1816 1099 2567 O ATOM 2200 CB GLU A1080 -58.672-127.273 258.563 1.00138.81 C ANISOU 2200 CB GLU A1080 14334 17401 21006 -2021 532 2118 C ATOM 2201 CG GLU A1080 -59.783-126.821 257.629 1.00144.61 C ANISOU 2201 CG GLU A1080 14648 18443 21855 -2068 348 2071 C ATOM 2202 CD GLU A1080 -59.740-127.523 256.287 1.00148.68 C ANISOU 2202 CD GLU A1080 15203 18717 22569 -2384 -103 1777 C ATOM 2203 OE1 GLU A1080 -59.288-128.685 256.236 1.00150.46 O ANISOU 2203 OE1 GLU A1080 15627 18533 23009 -2700 -241 1717 O ATOM 2204 OE2 GLU A1080 -60.155-126.910 255.282 1.00150.11 O ANISOU 2204 OE2 GLU A1080 15243 19119 22675 -2287 -323 1600 O ATOM 2205 N THR A1081 -56.331-126.004 260.597 1.00124.22 N ANISOU 2205 N THR A1081 13344 15469 18384 -1263 1011 2040 N ATOM 2206 CA THR A1081 -55.047-126.285 261.226 1.00121.36 C ANISOU 2206 CA THR A1081 13384 14869 17857 -1178 1036 1992 C ATOM 2207 C THR A1081 -55.080-126.158 262.743 1.00120.98 C ANISOU 2207 C THR A1081 13367 15040 17558 -989 1351 2263 C ATOM 2208 O THR A1081 -54.072-126.461 263.392 1.00120.44 O ANISOU 2208 O THR A1081 13599 14828 17334 -918 1362 2273 O ATOM 2209 CB THR A1081 -53.972-125.349 260.669 1.00117.97 C ANISOU 2209 CB THR A1081 13272 14335 17216 -937 899 1632 C ATOM 2210 OG1 THR A1081 -54.339-123.990 260.934 1.00118.42 O ANISOU 2210 OG1 THR A1081 13286 14664 17044 -623 1041 1569 O ATOM 2211 CG2 THR A1081 -53.813-125.538 259.170 1.00117.85 C ANISOU 2211 CG2 THR A1081 13271 14134 17372 -1083 611 1384 C ATOM 2212 N GLY A1082 -56.195-125.722 263.320 1.00122.39 N ANISOU 2212 N GLY A1082 13236 15600 17665 -873 1609 2485 N ATOM 2213 CA GLY A1082 -56.247-125.509 264.757 1.00124.52 C ANISOU 2213 CA GLY A1082 13560 16146 17606 -622 1935 2716 C ATOM 2214 C GLY A1082 -55.283-124.444 265.236 1.00118.67 C ANISOU 2214 C GLY A1082 13216 15424 16448 -241 1933 2408 C ATOM 2215 O GLY A1082 -54.621-124.625 266.264 1.00119.16 O ANISOU 2215 O GLY A1082 13521 15523 16232 -116 2022 2486 O ATOM 2216 N ALA A1083 -55.188-123.334 264.502 1.00115.03 N ANISOU 2216 N ALA A1083 12825 14933 15950 -67 1810 2069 N ATOM 2217 CA ALA A1083 -54.253-122.275 264.860 1.00111.44 C ANISOU 2217 CA ALA A1083 12745 14420 15179 233 1761 1751 C ATOM 2218 C ALA A1083 -54.640-121.563 266.148 1.00113.31 C ANISOU 2218 C ALA A1083 13047 14988 15017 606 2050 1786 C ATOM 2219 O ALA A1083 -53.785-120.916 266.761 1.00112.45 O ANISOU 2219 O ALA A1083 13289 14831 14605 818 1997 1542 O ATOM 2220 CB ALA A1083 -54.151-121.258 263.721 1.00110.38 C ANISOU 2220 CB ALA A1083 12650 14137 15151 312 1583 1445 C ATOM 2221 N GLN A1084 -55.896-121.677 266.575 1.00116.65 N ANISOU 2221 N GLN A1084 13132 15763 15426 695 2348 2076 N ATOM 2222 CA GLN A1084 -56.387-120.888 267.697 1.00116.90 C ANISOU 2222 CA GLN A1084 13213 16158 15045 1134 2664 2078 C ATOM 2223 C GLN A1084 -55.623-121.210 268.977 1.00117.07 C ANISOU 2223 C GLN A1084 13552 16275 14653 1250 2739 2123 C ATOM 2224 O GLN A1084 -55.464-122.377 269.346 1.00117.23 O ANISOU 2224 O GLN A1084 13506 16308 14727 1010 2773 2463 O ATOM 2225 CB GLN A1084 -57.881-121.138 267.901 1.00119.24 C ANISOU 2225 CB GLN A1084 13005 16870 15433 1185 3005 2468 C ATOM 2226 CG GLN A1084 -58.552-120.101 268.783 1.00122.87 C ANISOU 2226 CG GLN A1084 13472 17723 15491 1733 3354 2411 C ATOM 2227 CD GLN A1084 -59.548-120.709 269.745 1.00129.13 C ANISOU 2227 CD GLN A1084 13902 19023 16138 1820 3794 2908 C ATOM 2228 OE1 GLN A1084 -60.080-121.793 269.507 1.00130.70 O ANISOU 2228 OE1 GLN A1084 13697 19282 16680 1427 3841 3338 O ATOM 2229 NE2 GLN A1084 -59.800-120.015 270.848 1.00133.59 N ANISOU 2229 NE2 GLN A1084 14615 19952 16190 2338 4125 2853 N ATOM 2230 N GLY A1085 -55.151-120.163 269.652 1.00117.02 N ANISOU 2230 N GLY A1085 13907 16322 14234 1625 2742 1777 N ATOM 2231 CA GLY A1085 -54.467-120.306 270.920 1.00118.52 C ANISOU 2231 CA GLY A1085 14417 16677 13941 1800 2782 1765 C ATOM 2232 C GLY A1085 -53.021-120.733 270.836 1.00113.68 C ANISOU 2232 C GLY A1085 14094 15745 13355 1567 2414 1623 C ATOM 2233 O GLY A1085 -52.449-121.126 271.860 1.00115.17 O ANISOU 2233 O GLY A1085 14486 16099 13174 1658 2416 1712 O ATOM 2234 N ARG A1086 -52.404-120.660 269.661 1.00109.23 N ANISOU 2234 N ARG A1086 13541 14771 13189 1301 2107 1424 N ATOM 2235 CA ARG A1086 -51.044-121.134 269.459 1.00106.24 C ANISOU 2235 CA ARG A1086 13360 14110 12895 1081 1781 1331 C ATOM 2236 C ARG A1086 -50.097-119.966 269.232 1.00105.32 C ANISOU 2236 C ARG A1086 13533 13767 12717 1170 1506 848 C ATOM 2237 O ARG A1086 -50.447-118.987 268.566 1.00104.23 O ANISOU 2237 O ARG A1086 13387 13493 12722 1246 1496 616 O ATOM 2238 CB ARG A1086 -50.976-122.095 268.273 1.00103.89 C ANISOU 2238 CB ARG A1086 12844 13525 13103 702 1656 1507 C ATOM 2239 CG ARG A1086 -51.901-123.277 268.418 1.00107.10 C ANISOU 2239 CG ARG A1086 12959 14064 13672 534 1880 1975 C ATOM 2240 CD ARG A1086 -51.649-124.299 267.341 1.00104.89 C ANISOU 2240 CD ARG A1086 12559 13436 13860 162 1693 2073 C ATOM 2241 NE ARG A1086 -51.960-125.640 267.818 1.00107.82 N ANISOU 2241 NE ARG A1086 12802 13814 14349 -23 1822 2524 N ATOM 2242 CZ ARG A1086 -51.127-126.373 268.547 1.00110.93 C ANISOU 2242 CZ ARG A1086 13389 14153 14607 -11 1780 2703 C ATOM 2243 NH1 ARG A1086 -49.933-125.895 268.871 1.00109.22 N ANISOU 2243 NH1 ARG A1086 13462 13912 14125 164 1588 2444 N ATOM 2244 NH2 ARG A1086 -51.480-127.586 268.945 1.00115.53 N ANISOU 2244 NH2 ARG A1086 13858 14696 15344 -184 1915 3162 N ATOM 2245 N LYS A1087 -48.896-120.077 269.791 1.00106.41 N ANISOU 2245 N LYS A1087 13908 13860 12664 1151 1273 729 N ATOM 2246 CA LYS A1087 -47.864-119.072 269.579 1.00106.42 C ANISOU 2246 CA LYS A1087 14142 13621 12673 1148 967 304 C ATOM 2247 C LYS A1087 -47.304-119.202 268.167 1.00103.57 C ANISOU 2247 C LYS A1087 13647 12904 12800 853 783 283 C ATOM 2248 O LYS A1087 -46.812-120.269 267.785 1.00101.32 O ANISOU 2248 O LYS A1087 13246 12545 12704 649 708 500 O ATOM 2249 CB LYS A1087 -46.759-119.236 270.618 1.00109.96 C ANISOU 2249 CB LYS A1087 14815 14189 12774 1196 744 216 C ATOM 2250 N VAL A1088 -47.395-118.127 267.384 1.00102.72 N ANISOU 2250 N VAL A1088 13569 12576 12884 863 728 38 N ATOM 2251 CA VAL A1088 -46.940-118.132 265.999 1.00 99.99 C ANISOU 2251 CA VAL A1088 13102 11945 12943 632 593 35 C ATOM 2252 C VAL A1088 -46.113-116.884 265.728 1.00100.14 C ANISOU 2252 C VAL A1088 13300 11705 13046 617 384 -282 C ATOM 2253 O VAL A1088 -46.287-115.842 266.371 1.00102.82 O ANISOU 2253 O VAL A1088 13846 12015 13205 806 378 -534 O ATOM 2254 CB VAL A1088 -48.118-118.214 264.995 1.00 99.35 C ANISOU 2254 CB VAL A1088 12791 11862 13097 618 772 185 C ATOM 2255 CG1 VAL A1088 -47.624-118.652 263.622 1.00 96.62 C ANISOU 2255 CG1 VAL A1088 12316 11310 13085 378 639 244 C ATOM 2256 CG2 VAL A1088 -49.195-119.158 265.490 1.00102.19 C ANISOU 2256 CG2 VAL A1088 12962 12498 13369 651 1008 478 C ATOM 2257 N ALA A1089 -45.196-117.003 264.771 1.00 97.28 N ANISOU 2257 N ALA A1089 12857 11138 12968 395 219 -263 N ATOM 2258 CA ALA A1089 -44.507-115.871 264.175 1.00 97.94 C ANISOU 2258 CA ALA A1089 13023 10938 13252 314 62 -458 C ATOM 2259 C ALA A1089 -44.391-116.124 262.680 1.00 96.13 C ANISOU 2259 C ALA A1089 12602 10587 13337 165 87 -291 C ATOM 2260 O ALA A1089 -44.409-117.273 262.230 1.00 95.21 O ANISOU 2260 O ALA A1089 12328 10574 13273 84 132 -101 O ATOM 2261 CB ALA A1089 -43.120-115.647 264.791 1.00 98.64 C ANISOU 2261 CB ALA A1089 13214 10964 13300 187 -217 -620 C ATOM 2262 N CYS A1090 -44.283-115.046 261.911 1.00 95.93 N ANISOU 2262 N CYS A1090 12614 10328 13509 146 59 -362 N ATOM 2263 CA CYS A1090 -44.214-115.140 260.462 1.00 91.98 C ANISOU 2263 CA CYS A1090 11957 9753 13239 53 98 -196 C ATOM 2264 C CYS A1090 -42.904-114.557 259.956 1.00 88.71 C ANISOU 2264 C CYS A1090 11537 9136 13034 -128 -47 -209 C ATOM 2265 O CYS A1090 -42.339-113.638 260.555 1.00 92.66 O ANISOU 2265 O CYS A1090 12175 9451 13580 -181 -182 -376 O ATOM 2266 CB CYS A1090 -45.389-114.417 259.798 1.00 93.61 C ANISOU 2266 CB CYS A1090 12156 9912 13500 217 238 -153 C ATOM 2267 SG CYS A1090 -46.991-115.177 260.125 1.00 97.68 S ANISOU 2267 SG CYS A1090 12541 10726 13847 390 426 -55 S ATOM 2268 N PHE A1091 -42.422-115.110 258.847 1.00 81.76 N ANISOU 2268 N PHE A1091 10488 8298 12279 -224 -21 -34 N ATOM 2269 CA PHE A1091 -41.264-114.574 258.151 1.00 77.66 C ANISOU 2269 CA PHE A1091 9893 7640 11976 -381 -89 41 C ATOM 2270 C PHE A1091 -41.498-114.716 256.655 1.00 74.08 C ANISOU 2270 C PHE A1091 9322 7238 11589 -343 49 242 C ATOM 2271 O PHE A1091 -42.444-115.373 256.214 1.00 73.02 O ANISOU 2271 O PHE A1091 9160 7251 11334 -227 139 281 O ATOM 2272 CB PHE A1091 -39.961-115.260 258.594 1.00 77.06 C ANISOU 2272 CB PHE A1091 9699 7659 11920 -519 -224 46 C ATOM 2273 CG PHE A1091 -39.892-116.735 258.286 1.00 74.75 C ANISOU 2273 CG PHE A1091 9287 7580 11535 -462 -158 154 C ATOM 2274 CD1 PHE A1091 -40.480-117.667 259.127 1.00 73.94 C ANISOU 2274 CD1 PHE A1091 9247 7600 11248 -377 -154 114 C ATOM 2275 CD2 PHE A1091 -39.194-117.191 257.178 1.00 73.40 C ANISOU 2275 CD2 PHE A1091 8951 7470 11465 -483 -92 303 C ATOM 2276 CE1 PHE A1091 -40.398-119.025 258.853 1.00 71.86 C ANISOU 2276 CE1 PHE A1091 8905 7444 10956 -338 -108 213 C ATOM 2277 CE2 PHE A1091 -39.106-118.546 256.899 1.00 71.72 C ANISOU 2277 CE2 PHE A1091 8677 7392 11181 -401 -43 353 C ATOM 2278 CZ PHE A1091 -39.708-119.464 257.738 1.00 71.50 C ANISOU 2278 CZ PHE A1091 8733 7412 11022 -343 -65 304 C ATOM 2279 N GLY A1092 -40.646-114.073 255.869 1.00 73.03 N ANISOU 2279 N GLY A1092 9111 6997 11639 -448 57 380 N ATOM 2280 CA GLY A1092 -40.795-114.147 254.430 1.00 73.36 C ANISOU 2280 CA GLY A1092 9060 7133 11679 -379 196 588 C ATOM 2281 C GLY A1092 -39.781-113.278 253.719 1.00 79.25 C ANISOU 2281 C GLY A1092 9714 7756 12641 -506 234 796 C ATOM 2282 O GLY A1092 -39.259-112.306 254.273 1.00 81.63 O ANISOU 2282 O GLY A1092 10058 7799 13158 -664 140 771 O ATOM 2283 N CYS A1093 -39.521-113.651 252.471 1.00 82.28 N ANISOU 2283 N CYS A1093 9973 8330 12960 -439 372 1002 N ATOM 2284 CA CYS A1093 -38.615-112.927 251.595 1.00 85.08 C ANISOU 2284 CA CYS A1093 10197 8648 13483 -529 479 1292 C ATOM 2285 C CYS A1093 -39.396-112.021 250.649 1.00 88.22 C ANISOU 2285 C CYS A1093 10688 8967 13864 -404 593 1503 C ATOM 2286 O CYS A1093 -40.600-112.188 250.438 1.00 84.85 O ANISOU 2286 O CYS A1093 10375 8618 13246 -211 594 1427 O ATOM 2287 CB CYS A1093 -37.746-113.900 250.791 1.00 84.10 C ANISOU 2287 CB CYS A1093 9871 8838 13243 -472 601 1416 C ATOM 2288 SG CYS A1093 -36.626-114.904 251.788 1.00 84.23 S ANISOU 2288 SG CYS A1093 9728 8951 13323 -576 481 1262 S ATOM 2289 N GLY A1094 -38.686-111.056 250.080 1.00 97.69 N ANISOU 2289 N GLY A1094 11810 10022 15284 -520 687 1806 N ATOM 2290 CA GLY A1094 -39.307-110.102 249.183 1.00105.01 C ANISOU 2290 CA GLY A1094 12830 10846 16224 -393 803 2084 C ATOM 2291 C GLY A1094 -38.270-109.152 248.629 1.00115.65 C ANISOU 2291 C GLY A1094 14050 12023 17868 -584 925 2479 C ATOM 2292 O GLY A1094 -37.065-109.371 248.767 1.00117.44 O ANISOU 2292 O GLY A1094 14059 12311 18253 -798 940 2551 O ATOM 2293 N ASP A1095 -38.755-108.084 247.998 1.00121.79 N ANISOU 2293 N ASP A1095 14942 12589 18745 -502 1016 2774 N ATOM 2294 CA ASP A1095 -37.888-107.075 247.405 1.00128.61 C ANISOU 2294 CA ASP A1095 15697 13238 19931 -693 1158 3234 C ATOM 2295 C ASP A1095 -38.479-105.694 247.641 1.00128.97 C ANISOU 2295 C ASP A1095 15987 12722 20294 -711 1102 3333 C ATOM 2296 O ASP A1095 -39.691-105.496 247.513 1.00127.46 O ANISOU 2296 O ASP A1095 16000 12502 19928 -414 1087 3271 O ATOM 2297 CB ASP A1095 -37.690-107.322 245.900 1.00134.95 C ANISOU 2297 CB ASP A1095 16354 14473 20447 -496 1434 3679 C ATOM 2298 CG ASP A1095 -36.714-106.342 245.264 1.00143.26 C ANISOU 2298 CG ASP A1095 17241 15356 21835 -708 1635 4242 C ATOM 2299 OD1 ASP A1095 -36.109-105.526 245.990 1.00148.52 O ANISOU 2299 OD1 ASP A1095 17880 15543 23008 -1064 1528 4266 O ATOM 2300 OD2 ASP A1095 -36.542-106.398 244.028 1.00146.01 O ANISOU 2300 OD2 ASP A1095 17481 16061 21933 -526 1897 4670 O ATOM 2301 N SER A1096 -37.606-104.739 247.975 1.00128.20 N ANISOU 2301 N SER A1096 15853 12166 20690 -1060 1062 3492 N ATOM 2302 CA SER A1096 -38.038-103.375 248.253 1.00128.17 C ANISOU 2302 CA SER A1096 16119 11512 21067 -1104 993 3563 C ATOM 2303 C SER A1096 -38.548-102.658 247.009 1.00125.61 C ANISOU 2303 C SER A1096 15865 11148 20714 -863 1226 4117 C ATOM 2304 O SER A1096 -39.303-101.688 247.138 1.00126.41 O ANISOU 2304 O SER A1096 16244 10778 21008 -722 1186 4153 O ATOM 2305 CB SER A1096 -36.886-102.578 248.869 1.00135.40 C ANISOU 2305 CB SER A1096 16964 11922 22560 -1600 858 3593 C ATOM 2306 OG SER A1096 -36.236-103.323 249.884 1.00135.65 O ANISOU 2306 OG SER A1096 16859 12108 22572 -1823 641 3160 O ATOM 2307 N SER A1097 -38.149-103.107 245.815 1.00123.41 N ANISOU 2307 N SER A1097 15351 11365 20175 -775 1472 4552 N ATOM 2308 CA SER A1097 -38.590-102.457 244.584 1.00122.23 C ANISOU 2308 CA SER A1097 15261 11255 19927 -519 1698 5130 C ATOM 2309 C SER A1097 -40.100-102.508 244.426 1.00118.36 C ANISOU 2309 C SER A1097 15007 10874 19088 -57 1630 4976 C ATOM 2310 O SER A1097 -40.700-101.582 243.869 1.00124.12 O ANISOU 2310 O SER A1097 15897 11361 19901 157 1709 5352 O ATOM 2311 CB SER A1097 -37.921-103.103 243.371 1.00121.93 C ANISOU 2311 CB SER A1097 14938 11854 19537 -443 1975 5550 C ATOM 2312 OG SER A1097 -36.531-102.847 243.352 1.00125.94 O ANISOU 2312 OG SER A1097 15167 12262 20421 -847 2099 5852 O ATOM 2313 N TRP A1098 -40.726-103.582 244.888 1.00111.13 N ANISOU 2313 N TRP A1098 14090 10329 17804 102 1487 4468 N ATOM 2314 CA TRP A1098 -42.170-103.699 244.809 1.00107.57 C ANISOU 2314 CA TRP A1098 13789 10029 17055 502 1403 4310 C ATOM 2315 C TRP A1098 -42.814-102.844 245.891 1.00109.22 C ANISOU 2315 C TRP A1098 14247 9641 17612 531 1256 4042 C ATOM 2316 O TRP A1098 -42.282-102.710 246.996 1.00107.63 O ANISOU 2316 O TRP A1098 14109 9073 17714 246 1132 3704 O ATOM 2317 CB TRP A1098 -42.583-105.165 244.936 1.00 99.13 C ANISOU 2317 CB TRP A1098 12605 9532 15528 608 1304 3887 C ATOM 2318 CG TRP A1098 -41.984-106.007 243.847 1.00 97.23 C ANISOU 2318 CG TRP A1098 12175 9854 14915 643 1446 4092 C ATOM 2319 CD1 TRP A1098 -40.719-106.515 243.806 1.00 96.92 C ANISOU 2319 CD1 TRP A1098 11956 9950 14920 398 1546 4121 C ATOM 2320 CD2 TRP A1098 -42.619-106.415 242.628 1.00 96.49 C ANISOU 2320 CD2 TRP A1098 12054 10281 14326 979 1501 4286 C ATOM 2321 NE1 TRP A1098 -40.528-107.220 242.642 1.00 96.27 N ANISOU 2321 NE1 TRP A1098 11761 10430 14389 591 1694 4307 N ATOM 2322 CE2 TRP A1098 -41.681-107.174 241.902 1.00 96.06 C ANISOU 2322 CE2 TRP A1098 11844 10646 14008 938 1651 4390 C ATOM 2323 CE3 TRP A1098 -43.890-106.216 242.083 1.00 96.69 C ANISOU 2323 CE3 TRP A1098 12160 10488 14089 1330 1421 4370 C ATOM 2324 CZ2 TRP A1098 -41.974-107.735 240.660 1.00 96.02 C ANISOU 2324 CZ2 TRP A1098 11815 11216 13453 1238 1718 4532 C ATOM 2325 CZ3 TRP A1098 -44.180-106.774 240.849 1.00 96.63 C ANISOU 2325 CZ3 TRP A1098 12096 11067 13551 1592 1450 4529 C ATOM 2326 CH2 TRP A1098 -43.226-107.523 240.152 1.00 96.62 C ANISOU 2326 CH2 TRP A1098 11991 11457 13263 1547 1595 4587 C ATOM 2327 N GLU A1099 -43.957-102.244 245.552 1.00113.64 N ANISOU 2327 N GLU A1099 14950 10121 18107 909 1266 4196 N ATOM 2328 CA GLU A1099 -44.594-101.293 246.458 1.00115.89 C ANISOU 2328 CA GLU A1099 15499 9810 18725 1027 1174 3993 C ATOM 2329 C GLU A1099 -44.958-101.944 247.785 1.00113.60 C ANISOU 2329 C GLU A1099 15245 9561 18355 992 1009 3341 C ATOM 2330 O GLU A1099 -44.758-101.351 248.852 1.00118.46 O ANISOU 2330 O GLU A1099 16067 9653 19291 864 913 3037 O ATOM 2331 CB GLU A1099 -45.836-100.694 245.799 1.00117.09 C ANISOU 2331 CB GLU A1099 15739 9991 18758 1522 1225 4288 C ATOM 2332 CG GLU A1099 -46.621 -99.757 246.702 1.00119.79 C ANISOU 2332 CG GLU A1099 16356 9757 19401 1757 1160 4063 C ATOM 2333 CD GLU A1099 -45.869 -98.478 247.004 1.00125.37 C ANISOU 2333 CD GLU A1099 17332 9609 20695 1537 1180 4212 C ATOM 2334 OE1 GLU A1099 -45.106 -98.020 246.130 1.00128.36 O ANISOU 2334 OE1 GLU A1099 17670 9847 21255 1353 1300 4743 O ATOM 2335 OE2 GLU A1099 -46.040 -97.930 248.113 1.00127.17 O ANISOU 2335 OE2 GLU A1099 17816 9302 21201 1544 1076 3799 O ATOM 2336 N TYR A1100 -45.490-103.163 247.742 1.00106.38 N ANISOU 2336 N TYR A1100 14147 9260 17013 1104 969 3123 N ATOM 2337 CA TYR A1100 -45.910-103.873 248.949 1.00103.16 C ANISOU 2337 CA TYR A1100 13746 8959 16493 1092 848 2584 C ATOM 2338 C TYR A1100 -44.764-104.772 249.388 1.00100.97 C ANISOU 2338 C TYR A1100 13347 8828 16190 702 790 2369 C ATOM 2339 O TYR A1100 -44.637-105.915 248.949 1.00100.89 O ANISOU 2339 O TYR A1100 13138 9314 15881 662 798 2351 O ATOM 2340 CB TYR A1100 -47.180-104.669 248.688 1.00101.42 C ANISOU 2340 CB TYR A1100 13371 9272 15891 1404 830 2508 C ATOM 2341 CG TYR A1100 -48.165-103.946 247.804 1.00105.63 C ANISOU 2341 CG TYR A1100 13912 9845 16377 1799 885 2868 C ATOM 2342 CD1 TYR A1100 -48.990-102.956 248.316 1.00109.45 C ANISOU 2342 CD1 TYR A1100 14567 9961 17060 2107 904 2842 C ATOM 2343 CD2 TYR A1100 -48.264-104.249 246.452 1.00107.16 C ANISOU 2343 CD2 TYR A1100 13953 10463 16301 1906 916 3234 C ATOM 2344 CE1 TYR A1100 -49.889-102.290 247.510 1.00114.05 C ANISOU 2344 CE1 TYR A1100 15136 10588 17608 2512 949 3206 C ATOM 2345 CE2 TYR A1100 -49.160-103.588 245.638 1.00111.93 C ANISOU 2345 CE2 TYR A1100 14552 11148 16830 2292 939 3593 C ATOM 2346 CZ TYR A1100 -49.971-102.611 246.172 1.00115.59 C ANISOU 2346 CZ TYR A1100 15156 11232 17529 2594 954 3596 C ATOM 2347 OH TYR A1100 -50.867-101.950 245.364 1.00120.94 O ANISOU 2347 OH TYR A1100 15810 12000 18141 3020 972 3987 O ATOM 2348 N PHE A1101 -43.914-104.247 250.268 1.00100.23 N ANISOU 2348 N PHE A1101 13379 8284 16419 422 709 2190 N ATOM 2349 CA PHE A1101 -42.771-105.010 250.754 1.00 95.98 C ANISOU 2349 CA PHE A1101 12702 7876 15891 65 628 2008 C ATOM 2350 C PHE A1101 -43.257-106.132 251.662 1.00 90.99 C ANISOU 2350 C PHE A1101 12033 7579 14960 131 536 1587 C ATOM 2351 O PHE A1101 -43.761-105.877 252.761 1.00 93.72 O ANISOU 2351 O PHE A1101 12557 7732 15322 216 449 1254 O ATOM 2352 CB PHE A1101 -41.792-104.099 251.487 1.00 98.04 C ANISOU 2352 CB PHE A1101 13090 7575 16585 -264 508 1914 C ATOM 2353 CG PHE A1101 -40.606-104.825 252.054 1.00 95.69 C ANISOU 2353 CG PHE A1101 12611 7432 16313 -619 388 1737 C ATOM 2354 CD1 PHE A1101 -39.842-105.655 251.251 1.00 94.32 C ANISOU 2354 CD1 PHE A1101 12138 7681 16018 -733 496 1992 C ATOM 2355 CD2 PHE A1101 -40.253-104.677 253.385 1.00 97.61 C ANISOU 2355 CD2 PHE A1101 12987 7425 16675 -797 164 1313 C ATOM 2356 CE1 PHE A1101 -38.753-106.327 251.764 1.00 94.30 C ANISOU 2356 CE1 PHE A1101 11940 7838 16052 -1009 392 1856 C ATOM 2357 CE2 PHE A1101 -39.161-105.346 253.904 1.00 97.56 C ANISOU 2357 CE2 PHE A1101 12786 7601 16682 -1098 27 1180 C ATOM 2358 CZ PHE A1101 -38.410-106.172 253.092 1.00 95.60 C ANISOU 2358 CZ PHE A1101 12208 7763 16353 -1199 146 1467 C ATOM 2359 N CYS A1102 -43.105-107.373 251.198 1.00 82.61 N ANISOU 2359 N CYS A1102 10758 7008 13621 109 569 1611 N ATOM 2360 CA CYS A1102 -43.471-108.567 251.960 1.00 77.38 C ANISOU 2360 CA CYS A1102 10039 6656 12708 133 495 1286 C ATOM 2361 C CYS A1102 -44.924-108.506 252.428 1.00 76.32 C ANISOU 2361 C CYS A1102 9992 6574 12434 421 499 1129 C ATOM 2362 O CYS A1102 -45.238-108.706 253.603 1.00 78.56 O ANISOU 2362 O CYS A1102 10356 6827 12664 442 440 831 O ATOM 2363 CB CYS A1102 -42.522-108.776 253.141 1.00 79.55 C ANISOU 2363 CB CYS A1102 10339 6793 13092 -126 360 1018 C ATOM 2364 SG CYS A1102 -40.828-109.212 252.676 1.00 82.40 S ANISOU 2364 SG CYS A1102 10471 7254 13583 -446 355 1197 S ATOM 2365 N GLY A1103 -45.824-108.223 251.483 1.00 75.62 N ANISOU 2365 N GLY A1103 9862 6608 12261 669 576 1358 N ATOM 2366 CA GLY A1103 -47.242-108.217 251.793 1.00 76.38 C ANISOU 2366 CA GLY A1103 9951 6837 12233 962 590 1266 C ATOM 2367 C GLY A1103 -47.791-109.574 252.180 1.00 77.08 C ANISOU 2367 C GLY A1103 9870 7336 12082 937 552 1077 C ATOM 2368 O GLY A1103 -48.836-109.643 252.835 1.00 81.03 O ANISOU 2368 O GLY A1103 10338 7936 12513 1118 574 955 O ATOM 2369 N ALA A1104 -47.109-110.654 251.788 1.00 74.85 N ANISOU 2369 N ALA A1104 9472 7278 11688 729 510 1069 N ATOM 2370 CA ALA A1104 -47.556-111.993 252.158 1.00 72.22 C ANISOU 2370 CA ALA A1104 9005 7252 11184 669 463 903 C ATOM 2371 C ALA A1104 -47.514-112.189 253.667 1.00 71.96 C ANISOU 2371 C ALA A1104 9051 7118 11174 608 457 663 C ATOM 2372 O ALA A1104 -48.402-112.825 254.245 1.00 68.97 O ANISOU 2372 O ALA A1104 8580 6936 10692 667 473 577 O ATOM 2373 CB ALA A1104 -46.696-113.045 251.460 1.00 70.76 C ANISOU 2373 CB ALA A1104 8741 7240 10904 492 425 919 C ATOM 2374 N VAL A1105 -46.482-111.651 254.322 1.00 74.66 N ANISOU 2374 N VAL A1105 9548 7177 11641 481 428 569 N ATOM 2375 CA VAL A1105 -46.393-111.734 255.773 1.00 75.02 C ANISOU 2375 CA VAL A1105 9706 7151 11648 455 395 327 C ATOM 2376 C VAL A1105 -47.497-110.921 256.438 1.00 78.27 C ANISOU 2376 C VAL A1105 10225 7483 12030 730 473 231 C ATOM 2377 O VAL A1105 -47.893-111.221 257.571 1.00 79.29 O ANISOU 2377 O VAL A1105 10398 7713 12016 805 502 58 O ATOM 2378 CB VAL A1105 -44.988-111.289 256.227 1.00 74.89 C ANISOU 2378 CB VAL A1105 9811 6867 11777 238 286 234 C ATOM 2379 CG1 VAL A1105 -44.837-111.391 257.738 1.00 74.36 C ANISOU 2379 CG1 VAL A1105 9880 6771 11602 224 208 -40 C ATOM 2380 CG2 VAL A1105 -43.927-112.129 255.536 1.00 75.33 C ANISOU 2380 CG2 VAL A1105 9707 7059 11856 26 251 362 C ATOM 2381 N ASP A1106 -48.029-109.910 255.747 1.00 81.64 N ANISOU 2381 N ASP A1106 10693 7754 12571 925 529 365 N ATOM 2382 CA ASP A1106 -49.148-109.149 256.294 1.00 87.23 C ANISOU 2382 CA ASP A1106 11484 8404 13257 1263 629 291 C ATOM 2383 C ASP A1106 -50.444-109.945 256.235 1.00 88.49 C ANISOU 2383 C ASP A1106 11373 9002 13247 1428 720 376 C ATOM 2384 O ASP A1106 -51.221-109.945 257.197 1.00 91.26 O ANISOU 2384 O ASP A1106 11718 9473 13484 1629 826 256 O ATOM 2385 CB ASP A1106 -49.307-107.831 255.542 1.00 94.03 C ANISOU 2385 CB ASP A1106 12469 8934 14325 1451 658 451 C ATOM 2386 CG ASP A1106 -48.186-106.869 255.828 1.00100.44 C ANISOU 2386 CG ASP A1106 13564 9229 15371 1289 571 345 C ATOM 2387 OD1 ASP A1106 -47.461-107.090 256.819 1.00102.21 O ANISOU 2387 OD1 ASP A1106 13904 9371 15560 1100 476 76 O ATOM 2388 OD2 ASP A1106 -48.025-105.892 255.069 1.00103.40 O ANISOU 2388 OD2 ASP A1106 14034 9278 15974 1338 583 548 O ATOM 2389 N ALA A1107 -50.698-110.622 255.113 1.00 89.22 N ANISOU 2389 N ALA A1107 11230 9355 13316 1345 678 582 N ATOM 2390 CA ALA A1107 -51.949-111.358 254.962 1.00 92.15 C ANISOU 2390 CA ALA A1107 11302 10129 13581 1444 713 671 C ATOM 2391 C ALA A1107 -52.038-112.508 255.956 1.00 93.35 C ANISOU 2391 C ALA A1107 11362 10483 13623 1281 741 550 C ATOM 2392 O ALA A1107 -53.109-112.779 256.512 1.00 95.50 O ANISOU 2392 O ALA A1107 11446 11006 13833 1418 847 580 O ATOM 2393 CB ALA A1107 -52.085-111.873 253.529 1.00 91.32 C ANISOU 2393 CB ALA A1107 11005 10241 13452 1354 598 858 C ATOM 2394 N ILE A1108 -50.920-113.193 256.197 1.00 92.94 N ANISOU 2394 N ILE A1108 11419 10340 13554 1003 662 455 N ATOM 2395 CA ILE A1108 -50.927-114.333 257.109 1.00 94.65 C ANISOU 2395 CA ILE A1108 11568 10722 13673 854 684 395 C ATOM 2396 C ILE A1108 -51.185-113.871 258.537 1.00101.14 C ANISOU 2396 C ILE A1108 12521 11531 14378 1036 814 266 C ATOM 2397 O ILE A1108 -52.086-114.378 259.216 1.00104.71 O ANISOU 2397 O ILE A1108 12813 12244 14729 1118 944 324 O ATOM 2398 CB ILE A1108 -49.608-115.116 257.001 1.00 91.33 C ANISOU 2398 CB ILE A1108 11239 10196 13267 574 565 342 C ATOM 2399 CG1 ILE A1108 -49.379-115.579 255.563 1.00 88.12 C ANISOU 2399 CG1 ILE A1108 10728 9836 12918 456 465 440 C ATOM 2400 CG2 ILE A1108 -49.619-116.308 257.946 1.00 90.74 C ANISOU 2400 CG2 ILE A1108 11112 10261 13104 446 588 329 C ATOM 2401 CD1 ILE A1108 -48.019-116.190 255.338 1.00 85.19 C ANISOU 2401 CD1 ILE A1108 10442 9360 12566 259 383 398 C ATOM 2402 N GLU A1109 -50.396-112.903 259.016 1.00101.87 N ANISOU 2402 N GLU A1109 12904 11327 14473 1099 778 90 N ATOM 2403 CA GLU A1109 -50.568-112.414 260.380 1.00105.82 C ANISOU 2403 CA GLU A1109 13594 11809 14803 1303 871 -104 C ATOM 2404 C GLU A1109 -51.959-111.834 260.601 1.00113.33 C ANISOU 2404 C GLU A1109 14451 12913 15696 1681 1076 -65 C ATOM 2405 O GLU A1109 -52.478-111.882 261.721 1.00115.73 O ANISOU 2405 O GLU A1109 14787 13402 15785 1883 1232 -147 O ATOM 2406 CB GLU A1109 -49.503-111.366 260.708 1.00106.23 C ANISOU 2406 CB GLU A1109 13985 11460 14916 1282 737 -343 C ATOM 2407 CG GLU A1109 -48.090-111.920 260.808 1.00102.82 C ANISOU 2407 CG GLU A1109 13613 10942 14514 942 544 -396 C ATOM 2408 CD GLU A1109 -47.073-110.866 261.198 1.00101.40 C ANISOU 2408 CD GLU A1109 13718 10381 14430 873 376 -633 C ATOM 2409 OE1 GLU A1109 -46.037-111.229 261.794 1.00100.73 O ANISOU 2409 OE1 GLU A1109 13694 10290 14287 668 212 -748 O ATOM 2410 OE2 GLU A1109 -47.310-109.674 260.913 1.00101.72 O ANISOU 2410 OE2 GLU A1109 13913 10112 14626 1020 391 -698 O ATOM 2411 N GLU A1110 -52.579-111.289 259.552 1.00118.64 N ANISOU 2411 N GLU A1110 14992 13553 16534 1815 1090 85 N ATOM 2412 CA GLU A1110 -53.921-110.740 259.708 1.00127.12 C ANISOU 2412 CA GLU A1110 15920 14805 17574 2215 1284 156 C ATOM 2413 C GLU A1110 -54.958-111.839 259.890 1.00130.56 C ANISOU 2413 C GLU A1110 15947 15733 17926 2185 1409 358 C ATOM 2414 O GLU A1110 -55.958-111.635 260.587 1.00131.47 O ANISOU 2414 O GLU A1110 15928 16094 17930 2501 1632 392 O ATOM 2415 CB GLU A1110 -54.278-109.862 258.509 1.00130.45 C ANISOU 2415 CB GLU A1110 16297 15074 18196 2385 1239 305 C ATOM 2416 CG GLU A1110 -55.462-108.943 258.760 1.00137.40 C ANISOU 2416 CG GLU A1110 17121 16015 19071 2895 1433 336 C ATOM 2417 CD GLU A1110 -55.217-107.982 259.909 1.00143.32 C ANISOU 2417 CD GLU A1110 18276 16451 19730 3182 1539 20 C ATOM 2418 OE1 GLU A1110 -54.053-107.576 260.112 1.00143.76 O ANISOU 2418 OE1 GLU A1110 18696 16088 19837 2989 1388 -197 O ATOM 2419 OE2 GLU A1110 -56.186-107.636 260.614 1.00147.93 O ANISOU 2419 OE2 GLU A1110 18804 17218 20185 3606 1765 -24 O ATOM 2420 N LYS A1111 -54.742-113.004 259.278 1.00133.37 N ANISOU 2420 N LYS A1111 16096 16228 18349 1813 1276 496 N ATOM 2421 CA LYS A1111 -55.646-114.128 259.487 1.00137.32 C ANISOU 2421 CA LYS A1111 16217 17126 18834 1696 1362 690 C ATOM 2422 C LYS A1111 -55.314-114.894 260.759 1.00138.85 C ANISOU 2422 C LYS A1111 16495 17408 18854 1584 1472 654 C ATOM 2423 O LYS A1111 -56.221-115.416 261.416 1.00142.12 O ANISOU 2423 O LYS A1111 16646 18154 19200 1644 1668 823 O ATOM 2424 CB LYS A1111 -55.612-115.064 258.278 1.00137.29 C ANISOU 2424 CB LYS A1111 15991 17185 18987 1353 1148 816 C ATOM 2425 CG LYS A1111 -56.100-114.408 257.000 1.00140.54 C ANISOU 2425 CG LYS A1111 16270 17624 19506 1489 1035 904 C ATOM 2426 CD LYS A1111 -57.474-113.793 257.207 1.00147.40 C ANISOU 2426 CD LYS A1111 16847 18771 20385 1853 1203 1046 C ATOM 2427 CE LYS A1111 -57.726-112.645 256.243 1.00151.15 C ANISOU 2427 CE LYS A1111 17350 19155 20923 2150 1137 1107 C ATOM 2428 NZ LYS A1111 -57.687-113.077 254.821 1.00151.41 N ANISOU 2428 NZ LYS A1111 17234 19278 21015 1939 873 1210 N ATOM 2429 N LEU A1112 -54.032-114.969 261.122 1.00134.11 N ANISOU 2429 N LEU A1112 16229 16548 18180 1430 1353 476 N ATOM 2430 CA LEU A1112 -53.654-115.641 262.361 1.00132.96 C ANISOU 2430 CA LEU A1112 16189 16504 17825 1367 1433 458 C ATOM 2431 C LEU A1112 -54.117-114.848 263.576 1.00135.38 C ANISOU 2431 C LEU A1112 16641 16940 17856 1761 1659 338 C ATOM 2432 O LEU A1112 -54.692-115.411 264.514 1.00139.12 O ANISOU 2432 O LEU A1112 16990 17736 18135 1846 1872 481 O ATOM 2433 CB LEU A1112 -52.142-115.862 262.402 1.00131.17 C ANISOU 2433 CB LEU A1112 16249 16001 17590 1133 1214 300 C ATOM 2434 CG LEU A1112 -51.594-116.495 263.680 1.00128.84 C ANISOU 2434 CG LEU A1112 15840 15604 17508 788 1028 401 C ATOM 2435 CD1 LEU A1112 -52.154-117.894 263.866 1.00127.00 C ANISOU 2435 CD1 LEU A1112 15842 15169 17245 619 860 279 C ATOM 2436 CD2 LEU A1112 -50.073-116.518 263.661 1.00129.56 C ANISOU 2436 CD2 LEU A1112 15633 15923 17669 612 1096 645 C ATOM 2437 N LYS A1113 -53.875-113.534 263.578 1.00133.07 N ANISOU 2437 N LYS A1113 16629 16390 17540 2020 1626 81 N ATOM 2438 CA LYS A1113 -54.352-112.704 264.680 1.00133.49 C ANISOU 2438 CA LYS A1113 16871 16532 17316 2456 1835 -100 C ATOM 2439 C LYS A1113 -55.872-112.664 264.725 1.00132.01 C ANISOU 2439 C LYS A1113 16322 16724 17111 2773 2140 126 C ATOM 2440 O LYS A1113 -56.457-112.455 265.794 1.00135.74 O ANISOU 2440 O LYS A1113 16826 17461 17287 3126 2408 86 O ATOM 2441 CB LYS A1113 -53.778-111.292 264.561 1.00134.89 C ANISOU 2441 CB LYS A1113 17446 16254 17552 2642 1702 -441 C ATOM 2442 CG LYS A1113 -53.469-110.628 265.895 1.00137.42 C ANISOU 2442 CG LYS A1113 18175 16510 17530 2925 1745 -804 C ATOM 2443 CD LYS A1113 -52.372-109.584 265.742 1.00135.98 C ANISOU 2443 CD LYS A1113 18411 15767 17487 2843 1462 -1155 C ATOM 2444 CE LYS A1113 -51.945-109.019 267.086 1.00138.21 C ANISOU 2444 CE LYS A1113 19129 15976 17411 3060 1416 -1583 C ATOM 2445 NZ LYS A1113 -50.756-108.131 266.958 1.00137.54 N ANISOU 2445 NZ LYS A1113 19415 15327 17518 2860 1074 -1921 N ATOM 2446 N ASN A1114 -56.526-112.864 263.580 1.00127.50 N ANISOU 2446 N ASN A1114 15387 16226 16831 2669 2103 367 N ATOM 2447 CA ASN A1114 -57.977-112.976 263.560 1.00129.11 C ANISOU 2447 CA ASN A1114 15136 16854 17065 2905 2356 637 C ATOM 2448 C ASN A1114 -58.450-114.344 264.034 1.00127.61 C ANISOU 2448 C ASN A1114 14583 17067 16836 2644 2489 943 C ATOM 2449 O ASN A1114 -59.503-114.436 264.676 1.00131.93 O ANISOU 2449 O ASN A1114 14826 18029 17272 2894 2802 1145 O ATOM 2450 CB ASN A1114 -58.508-112.702 262.154 1.00129.37 C ANISOU 2450 CB ASN A1114 14890 16853 17410 2879 2213 787 C ATOM 2451 CG ASN A1114 -60.019-112.768 262.078 1.00135.24 C ANISOU 2451 CG ASN A1114 15100 18067 18220 3123 2434 1078 C ATOM 2452 OD1 ASN A1114 -60.599-113.845 261.947 1.00135.60 O ANISOU 2452 OD1 ASN A1114 14707 18444 18370 2834 2446 1353 O ATOM 2453 ND2 ASN A1114 -60.666-111.611 262.143 1.00139.98 N ANISOU 2453 ND2 ASN A1114 15715 18678 18791 3656 2599 1028 N ATOM 2454 N LEU A1115 -57.697-115.404 263.742 1.00121.75 N ANISOU 2454 N LEU A1115 13858 16203 16200 2162 2278 1006 N ATOM 2455 CA LEU A1115 -58.071-116.745 264.173 1.00121.53 C ANISOU 2455 CA LEU A1115 13527 16456 16193 1875 2383 1316 C ATOM 2456 C LEU A1115 -57.728-117.025 265.630 1.00122.57 C ANISOU 2456 C LEU A1115 13877 16732 15963 1992 2591 1323 C ATOM 2457 O LEU A1115 -58.121-118.076 266.147 1.00123.62 O ANISOU 2457 O LEU A1115 13760 17121 16088 1809 2745 1647 O ATOM 2458 CB LEU A1115 -57.408-117.795 263.278 1.00116.21 C ANISOU 2458 CB LEU A1115 12824 15548 15782 1357 2074 1366 C ATOM 2459 CG LEU A1115 -58.118-118.074 261.951 1.00113.80 C ANISOU 2459 CG LEU A1115 12140 15292 15808 1156 1904 1493 C ATOM 2460 CD1 LEU A1115 -57.539-119.308 261.273 1.00110.09 C ANISOU 2460 CD1 LEU A1115 11661 14621 15547 666 1641 1526 C ATOM 2461 CD2 LEU A1115 -59.615-118.233 262.174 1.00117.74 C ANISOU 2461 CD2 LEU A1115 12107 16239 16392 1257 2137 1802 C ATOM 2462 N GLY A1116 -57.008-116.128 266.302 1.00122.84 N ANISOU 2462 N GLY A1116 14371 16606 15698 2279 2583 985 N ATOM 2463 CA GLY A1116 -56.768-116.258 267.724 1.00124.76 C ANISOU 2463 CA GLY A1116 14838 17057 15507 2475 2772 957 C ATOM 2464 C GLY A1116 -55.394-116.748 268.122 1.00123.56 C ANISOU 2464 C GLY A1116 15043 16683 15222 2224 2525 821 C ATOM 2465 O GLY A1116 -55.114-116.836 269.324 1.00128.16 O ANISOU 2465 O GLY A1116 15843 17460 15391 2402 2637 784 O ATOM 2466 N ALA A1117 -54.534-117.082 267.166 1.00115.03 N ANISOU 2466 N ALA A1117 14011 15246 14450 1851 2198 759 N ATOM 2467 CA ALA A1117 -53.165-117.448 267.498 1.00112.66 C ANISOU 2467 CA ALA A1117 14018 14740 14046 1655 1951 622 C ATOM 2468 C ALA A1117 -52.416-116.234 268.033 1.00113.89 C ANISOU 2468 C ALA A1117 14603 14719 13951 1902 1821 184 C ATOM 2469 O ALA A1117 -52.522-115.132 267.489 1.00115.09 O ANISOU 2469 O ALA A1117 14854 14642 14232 2047 1766 -55 O ATOM 2470 CB ALA A1117 -52.455-118.012 266.269 1.00107.45 C ANISOU 2470 CB ALA A1117 13286 13762 13778 1256 1669 651 C ATOM 2471 N GLU A1118 -51.664-116.433 269.113 1.00115.25 N ANISOU 2471 N GLU A1118 15035 14986 13767 1948 1751 83 N ATOM 2472 CA GLU A1118 -50.915-115.340 269.727 1.00117.32 C ANISOU 2472 CA GLU A1118 15717 15084 13774 2143 1569 -374 C ATOM 2473 C GLU A1118 -49.648-115.089 268.921 1.00113.85 C ANISOU 2473 C GLU A1118 15393 14212 13652 1817 1184 -565 C ATOM 2474 O GLU A1118 -48.755-115.942 268.874 1.00112.11 O ANISOU 2474 O GLU A1118 15131 13974 13492 1540 1000 -440 O ATOM 2475 CB GLU A1118 -50.570-115.655 271.179 1.00119.44 C ANISOU 2475 CB GLU A1118 16209 15673 13499 2317 1593 -418 C ATOM 2476 CG GLU A1118 -49.732-114.564 271.838 1.00122.19 C ANISOU 2476 CG GLU A1118 17010 15846 13572 2478 1326 -951 C ATOM 2477 CD GLU A1118 -49.125-114.993 273.158 1.00125.68 C ANISOU 2477 CD GLU A1118 17676 16608 13468 2581 1231 -1003 C ATOM 2478 OE1 GLU A1118 -48.069-114.441 273.532 1.00126.24 O ANISOU 2478 OE1 GLU A1118 18052 16505 13410 2526 862 -1392 O ATOM 2479 OE2 GLU A1118 -49.700-115.881 273.820 1.00127.56 O ANISOU 2479 OE2 GLU A1118 17773 17284 13412 2706 1512 -632 O ATOM 2480 N ILE A1119 -49.557-113.918 268.293 1.00113.76 N ANISOU 2480 N ILE A1119 15514 13852 13857 1869 1078 -836 N ATOM 2481 CA ILE A1119 -48.336-113.568 267.579 1.00113.76 C ANISOU 2481 CA ILE A1119 15609 13459 14157 1565 744 -988 C ATOM 2482 C ILE A1119 -47.256-113.235 268.602 1.00120.26 C ANISOU 2482 C ILE A1119 16747 14234 14712 1548 474 -1311 C ATOM 2483 O ILE A1119 -47.395-112.306 269.407 1.00126.66 O ANISOU 2483 O ILE A1119 17866 14999 15262 1814 453 -1663 O ATOM 2484 CB ILE A1119 -48.577-112.421 266.585 1.00111.21 C ANISOU 2484 CB ILE A1119 15324 12762 14168 1611 727 -1108 C ATOM 2485 CG1 ILE A1119 -49.062-111.145 267.278 1.00119.83 C ANISOU 2485 CG1 ILE A1119 16732 13721 15075 1995 797 -1458 C ATOM 2486 CG2 ILE A1119 -49.586-112.846 265.528 1.00108.23 C ANISOU 2486 CG2 ILE A1119 14600 12495 14026 1610 933 -773 C ATOM 2487 CD1 ILE A1119 -48.056-110.007 267.230 1.00122.56 C ANISOU 2487 CD1 ILE A1119 17407 13569 15591 1884 490 -1826 C ATOM 2488 N VAL A1120 -46.188-114.030 268.605 1.00121.24 N ANISOU 2488 N VAL A1120 16794 14392 14881 1260 253 -1204 N ATOM 2489 CA VAL A1120 -45.107-113.820 269.561 1.00127.05 C ANISOU 2489 CA VAL A1120 17763 15144 15364 1216 -57 -1477 C ATOM 2490 C VAL A1120 -44.339-112.553 269.219 1.00129.09 C ANISOU 2490 C VAL A1120 18210 14956 15881 1075 -348 -1843 C ATOM 2491 O VAL A1120 -43.950-111.783 270.105 1.00133.70 O ANISOU 2491 O VAL A1120 19103 15468 16228 1165 -565 -2242 O ATOM 2492 CB VAL A1120 -44.189-115.053 269.587 1.00126.95 C ANISOU 2492 CB VAL A1120 17562 15302 15372 975 -206 -1207 C ATOM 2493 CG1 VAL A1120 -43.096-114.881 270.610 1.00131.22 C ANISOU 2493 CG1 VAL A1120 18296 15935 15625 947 -556 -1459 C ATOM 2494 CG2 VAL A1120 -44.996-116.299 269.875 1.00128.39 C ANISOU 2494 CG2 VAL A1120 17572 15835 15375 1083 90 -810 C ATOM 2495 N GLN A1121 -44.122-112.313 267.930 1.00123.85 N ANISOU 2495 N GLN A1121 17374 13982 15703 849 -361 -1711 N ATOM 2496 CA GLN A1121 -43.363-111.163 267.475 1.00127.01 C ANISOU 2496 CA GLN A1121 17900 13924 16433 658 -609 -1953 C ATOM 2497 C GLN A1121 -43.848-110.779 266.088 1.00127.52 C ANISOU 2497 C GLN A1121 17815 13727 16911 616 -429 -1740 C ATOM 2498 O GLN A1121 -44.469-111.578 265.383 1.00124.58 O ANISOU 2498 O GLN A1121 17191 13552 16592 643 -202 -1412 O ATOM 2499 CB GLN A1121 -41.863-111.461 267.451 1.00125.76 C ANISOU 2499 CB GLN A1121 17621 13734 16428 295 -952 -1947 C ATOM 2500 CG GLN A1121 -41.035-110.526 268.295 1.00130.79 C ANISOU 2500 CG GLN A1121 18525 14169 17002 196 -1331 -2382 C ATOM 2501 CD GLN A1121 -39.609-110.996 268.419 1.00128.30 C ANISOU 2501 CD GLN A1121 18008 13955 16786 -136 -1674 -2331 C ATOM 2502 OE1 GLN A1121 -39.233-111.609 269.415 1.00129.07 O ANISOU 2502 OE1 GLN A1121 18134 14399 16507 -75 -1839 -2393 O ATOM 2503 NE2 GLN A1121 -38.804-110.719 267.400 1.00126.50 N ANISOU 2503 NE2 GLN A1121 17549 13460 17053 -466 -1771 -2178 N ATOM 2504 N ASP A1122 -43.556-109.541 265.706 1.00133.80 N ANISOU 2504 N ASP A1122 18776 14065 17997 544 -554 -1926 N ATOM 2505 CA ASP A1122 -43.900-109.090 264.370 1.00134.25 C ANISOU 2505 CA ASP A1122 18708 13867 18435 509 -409 -1688 C ATOM 2506 C ASP A1122 -43.062-109.830 263.332 1.00127.46 C ANISOU 2506 C ASP A1122 17521 13082 17828 182 -453 -1355 C ATOM 2507 O ASP A1122 -42.008-110.399 263.632 1.00126.02 O ANISOU 2507 O ASP A1122 17233 13020 17631 -53 -646 -1354 O ATOM 2508 CB ASP A1122 -43.711-107.579 264.248 1.00140.33 C ANISOU 2508 CB ASP A1122 19757 14076 19488 500 -535 -1926 C ATOM 2509 CG ASP A1122 -44.795-106.802 264.967 1.00147.16 C ANISOU 2509 CG ASP A1122 20944 14832 20139 936 -400 -2218 C ATOM 2510 OD1 ASP A1122 -45.945-107.285 265.006 1.00145.83 O ANISOU 2510 OD1 ASP A1122 20669 15002 19738 1258 -108 -2075 O ATOM 2511 OD2 ASP A1122 -44.502-105.711 265.496 1.00152.43 O ANISOU 2511 OD2 ASP A1122 21962 15073 20884 962 -587 -2595 O ATOM 2512 N GLY A1123 -43.553-109.818 262.096 1.00117.80 N ANISOU 2512 N GLY A1123 16134 11815 16811 207 -269 -1069 N ATOM 2513 CA GLY A1123 -42.959-110.634 261.057 1.00107.74 C ANISOU 2513 CA GLY A1123 14565 10685 15688 -9 -249 -760 C ATOM 2514 C GLY A1123 -41.512-110.276 260.780 1.00102.60 C ANISOU 2514 C GLY A1123 13845 9826 15310 -339 -457 -739 C ATOM 2515 O GLY A1123 -41.038-109.175 261.064 1.00106.61 O ANISOU 2515 O GLY A1123 14522 9972 16012 -455 -618 -913 O ATOM 2516 N LEU A1124 -40.798-111.252 260.229 1.00 93.59 N ANISOU 2516 N LEU A1124 12440 8916 14203 -494 -454 -523 N ATOM 2517 CA LEU A1124 -39.445-111.058 259.728 1.00 90.19 C ANISOU 2517 CA LEU A1124 11832 8384 14053 -787 -582 -398 C ATOM 2518 C LEU A1124 -39.528-110.827 258.227 1.00 89.02 C ANISOU 2518 C LEU A1124 11543 8174 14107 -796 -388 -79 C ATOM 2519 O LEU A1124 -40.084-111.655 257.498 1.00 87.58 O ANISOU 2519 O LEU A1124 11253 8239 13782 -650 -212 84 O ATOM 2520 CB LEU A1124 -38.560-112.263 260.039 1.00 84.45 C ANISOU 2520 CB LEU A1124 10889 7977 13221 -880 -673 -340 C ATOM 2521 CG LEU A1124 -37.159-112.216 259.425 1.00 82.51 C ANISOU 2521 CG LEU A1124 10364 7723 13262 -1143 -757 -151 C ATOM 2522 CD1 LEU A1124 -36.229-111.335 260.246 1.00 84.67 C ANISOU 2522 CD1 LEU A1124 10662 7788 13722 -1405 -1069 -343 C ATOM 2523 CD2 LEU A1124 -36.589-113.616 259.259 1.00 79.92 C ANISOU 2523 CD2 LEU A1124 9796 7750 12821 -1097 -716 2 C ATOM 2524 N ARG A1125 -38.984-109.706 257.768 1.00 90.89 N ANISOU 2524 N ARG A1125 11790 8076 14667 -972 -431 13 N ATOM 2525 CA ARG A1125 -39.114-109.286 256.380 1.00 89.95 C ANISOU 2525 CA ARG A1125 11580 7881 14714 -950 -234 354 C ATOM 2526 C ARG A1125 -37.726-109.092 255.792 1.00 89.31 C ANISOU 2526 C ARG A1125 11242 7765 14926 -1252 -262 603 C ATOM 2527 O ARG A1125 -36.920-108.327 256.332 1.00 93.63 O ANISOU 2527 O ARG A1125 11794 8025 15756 -1527 -460 518 O ATOM 2528 CB ARG A1125 -39.938-108.003 256.286 1.00 94.25 C ANISOU 2528 CB ARG A1125 12385 8023 15402 -826 -193 330 C ATOM 2529 CG ARG A1125 -41.232-108.081 257.069 1.00 96.60 C ANISOU 2529 CG ARG A1125 12908 8365 15430 -515 -168 58 C ATOM 2530 CD ARG A1125 -41.791-106.707 257.353 1.00104.31 C ANISOU 2530 CD ARG A1125 14185 8866 16583 -390 -188 -73 C ATOM 2531 NE ARG A1125 -43.010-106.456 256.597 1.00106.11 N ANISOU 2531 NE ARG A1125 14445 9127 16746 -61 21 116 N ATOM 2532 CZ ARG A1125 -44.232-106.714 257.050 1.00105.52 C ANISOU 2532 CZ ARG A1125 14441 9242 16412 269 115 -27 C ATOM 2533 NH1 ARG A1125 -44.404-107.229 258.259 1.00103.08 N ANISOU 2533 NH1 ARG A1125 14206 9102 15859 323 51 -342 N ATOM 2534 NH2 ARG A1125 -45.282-106.452 256.292 1.00106.42 N ANISOU 2534 NH2 ARG A1125 14524 9411 16501 556 277 180 N ATOM 2535 N ILE A1126 -37.452-109.783 254.691 1.00 84.54 N ANISOU 2535 N ILE A1126 10404 7464 14254 -1199 -70 903 N ATOM 2536 CA ILE A1126 -36.152-109.752 254.039 1.00 87.01 C ANISOU 2536 CA ILE A1126 10409 7855 14794 -1425 -23 1197 C ATOM 2537 C ILE A1126 -36.320-109.175 252.641 1.00 88.52 C ANISOU 2537 C ILE A1126 10555 8011 15067 -1358 229 1597 C ATOM 2538 O ILE A1126 -37.297-109.476 251.946 1.00 86.87 O ANISOU 2538 O ILE A1126 10450 7960 14596 -1074 384 1658 O ATOM 2539 CB ILE A1126 -35.517-111.157 253.988 1.00 84.43 C ANISOU 2539 CB ILE A1126 9837 7973 14271 -1363 10 1207 C ATOM 2540 CG1 ILE A1126 -35.245-111.657 255.405 1.00 86.24 C ANISOU 2540 CG1 ILE A1126 10100 8238 14430 -1432 -253 880 C ATOM 2541 CG2 ILE A1126 -34.235-111.151 253.171 1.00 86.79 C ANISOU 2541 CG2 ILE A1126 9774 8427 14775 -1517 130 1557 C ATOM 2542 CD1 ILE A1126 -34.782-113.083 255.462 1.00 88.78 C ANISOU 2542 CD1 ILE A1126 10237 8942 14554 -1310 -227 885 C ATOM 2543 N ASP A1127 -35.371-108.333 252.244 1.00 93.69 N ANISOU 2543 N ASP A1127 11039 8470 16088 -1629 256 1891 N ATOM 2544 CA ASP A1127 -35.319-107.760 250.908 1.00 98.62 C ANISOU 2544 CA ASP A1127 11579 9090 16801 -1590 521 2366 C ATOM 2545 C ASP A1127 -34.060-108.257 250.216 1.00 96.35 C ANISOU 2545 C ASP A1127 10883 9158 16568 -1706 684 2697 C ATOM 2546 O ASP A1127 -32.975-108.244 250.807 1.00 91.66 O ANISOU 2546 O ASP A1127 10042 8540 16246 -2006 542 2676 O ATOM 2547 CB ASP A1127 -35.337-106.232 250.965 1.00107.90 C ANISOU 2547 CB ASP A1127 12907 9681 18410 -1803 465 2518 C ATOM 2548 CG ASP A1127 -34.371-105.684 251.988 1.00114.72 C ANISOU 2548 CG ASP A1127 13692 10202 19693 -2232 183 2342 C ATOM 2549 OD1 ASP A1127 -33.964-106.449 252.886 1.00115.37 O ANISOU 2549 OD1 ASP A1127 13682 10495 19658 -2297 -16 2013 O ATOM 2550 OD2 ASP A1127 -34.019-104.492 251.903 1.00119.76 O ANISOU 2550 OD2 ASP A1127 14365 10353 20786 -2510 138 2534 O ATOM 2551 N GLY A1128 -34.208-108.699 248.971 1.00100.19 N ANISOU 2551 N GLY A1128 11286 10008 16773 -1447 975 2993 N ATOM 2552 CA GLY A1128 -33.071-109.254 248.274 1.00104.42 C ANISOU 2552 CA GLY A1128 11443 10947 17287 -1463 1183 3293 C ATOM 2553 C GLY A1128 -32.687-110.622 248.820 1.00105.90 C ANISOU 2553 C GLY A1128 11506 11473 17257 -1352 1094 2976 C ATOM 2554 O GLY A1128 -33.475-111.321 249.463 1.00103.59 O ANISOU 2554 O GLY A1128 11447 11184 16728 -1196 934 2575 O ATOM 2555 N ASP A1129 -31.442-110.992 248.551 1.00110.24 N ANISOU 2555 N ASP A1129 11662 12311 17914 -1425 1219 3204 N ATOM 2556 CA ASP A1129 -30.930-112.286 248.980 1.00112.22 C ANISOU 2556 CA ASP A1129 11760 12885 17994 -1279 1164 2975 C ATOM 2557 C ASP A1129 -30.910-112.360 250.505 1.00110.71 C ANISOU 2557 C ASP A1129 11643 12456 17966 -1488 780 2592 C ATOM 2558 O ASP A1129 -30.390-111.447 251.160 1.00115.11 O ANISOU 2558 O ASP A1129 12090 12737 18910 -1857 580 2625 O ATOM 2559 CB ASP A1129 -29.525-112.497 248.412 1.00119.68 C ANISOU 2559 CB ASP A1129 12210 14185 19077 -1309 1388 3348 C ATOM 2560 CG ASP A1129 -29.042-113.929 248.548 1.00122.88 C ANISOU 2560 CG ASP A1129 12476 14968 19245 -1018 1419 3168 C ATOM 2561 OD1 ASP A1129 -29.274-114.546 249.604 1.00121.36 O ANISOU 2561 OD1 ASP A1129 12420 14677 19015 -1014 1142 2795 O ATOM 2562 OD2 ASP A1129 -28.420-114.440 247.594 1.00126.15 O ANISOU 2562 OD2 ASP A1129 12653 15779 19500 -764 1738 3415 O ATOM 2563 N PRO A1130 -31.466-113.418 251.108 1.00104.65 N ANISOU 2563 N PRO A1130 11071 11781 16911 -1271 658 2231 N ATOM 2564 CA PRO A1130 -31.399-113.537 252.573 1.00101.53 C ANISOU 2564 CA PRO A1130 10741 11232 16604 -1429 313 1909 C ATOM 2565 C PRO A1130 -30.002-113.822 253.090 1.00101.75 C ANISOU 2565 C PRO A1130 10359 11450 16851 -1590 185 1995 C ATOM 2566 O PRO A1130 -29.676-113.396 254.206 1.00104.29 O ANISOU 2566 O PRO A1130 10659 11607 17359 -1850 -139 1823 O ATOM 2567 CB PRO A1130 -32.351-114.702 252.883 1.00 96.32 C ANISOU 2567 CB PRO A1130 10360 10671 15568 -1123 293 1612 C ATOM 2568 CG PRO A1130 -33.133-114.929 251.634 1.00 95.60 C ANISOU 2568 CG PRO A1130 10409 10682 15234 -870 559 1712 C ATOM 2569 CD PRO A1130 -32.266-114.493 250.504 1.00100.32 C ANISOU 2569 CD PRO A1130 10724 11447 15946 -890 808 2100 C ATOM 2570 N ARG A1131 -29.172-114.536 252.317 1.00100.82 N ANISOU 2570 N ARG A1131 9913 11700 16696 -1413 421 2243 N ATOM 2571 CA ARG A1131 -27.803-114.827 252.737 1.00104.38 C ANISOU 2571 CA ARG A1131 9896 12392 17372 -1524 321 2377 C ATOM 2572 C ARG A1131 -27.077-113.559 253.174 1.00109.74 C ANISOU 2572 C ARG A1131 10315 12867 18514 -2020 106 2518 C ATOM 2573 O ARG A1131 -26.196-113.612 254.040 1.00111.66 O ANISOU 2573 O ARG A1131 10264 13200 18964 -2220 -180 2474 O ATOM 2574 CB ARG A1131 -27.047-115.523 251.596 1.00107.93 C ANISOU 2574 CB ARG A1131 10010 13260 17737 -1235 698 2694 C ATOM 2575 CG ARG A1131 -27.715-116.816 251.105 1.00108.47 C ANISOU 2575 CG ARG A1131 10364 13485 17366 -747 884 2507 C ATOM 2576 CD ARG A1131 -27.374-117.149 249.650 1.00113.74 C ANISOU 2576 CD ARG A1131 10880 14482 17855 -433 1317 2778 C ATOM 2577 NE ARG A1131 -28.430-117.937 249.011 1.00114.40 N ANISOU 2577 NE ARG A1131 11389 14563 17513 -72 1445 2541 N ATOM 2578 CZ ARG A1131 -28.368-119.247 248.782 1.00117.05 C ANISOU 2578 CZ ARG A1131 11805 15069 17598 323 1539 2369 C ATOM 2579 NH1 ARG A1131 -29.386-119.867 248.200 1.00115.50 N ANISOU 2579 NH1 ARG A1131 12008 14820 17056 577 1601 2126 N ATOM 2580 NH2 ARG A1131 -27.289-119.937 249.126 1.00119.99 N ANISOU 2580 NH2 ARG A1131 11854 15653 18084 468 1554 2437 N ATOM 2581 N ALA A1132 -27.452-112.409 252.605 1.00113.05 N ANISOU 2581 N ALA A1132 10849 12990 19115 -2229 209 2685 N ATOM 2582 CA ALA A1132 -26.859-111.139 253.010 1.00121.93 C ANISOU 2582 CA ALA A1132 11791 13802 20736 -2740 -17 2795 C ATOM 2583 C ALA A1132 -27.266-110.757 254.430 1.00124.27 C ANISOU 2583 C ALA A1132 12398 13749 21071 -2944 -489 2319 C ATOM 2584 O ALA A1132 -26.471-110.166 255.172 1.00128.56 O ANISOU 2584 O ALA A1132 12716 14162 21969 -3344 -827 2265 O ATOM 2585 CB ALA A1132 -27.266-110.041 252.024 1.00125.24 C ANISOU 2585 CB ALA A1132 12325 13930 21330 -2860 232 3113 C ATOM 2586 N ALA A1133 -28.504-111.070 254.819 1.00120.97 N ANISOU 2586 N ALA A1133 12485 13195 20283 -2676 -522 1968 N ATOM 2587 CA ALA A1133 -29.059-110.652 256.102 1.00122.39 C ANISOU 2587 CA ALA A1133 13024 13062 20417 -2791 -899 1516 C ATOM 2588 C ALA A1133 -28.962-111.752 257.152 1.00119.83 C ANISOU 2588 C ALA A1133 12715 13032 19784 -2608 -1118 1233 C ATOM 2589 O ALA A1133 -29.705-111.719 258.134 1.00118.53 O ANISOU 2589 O ALA A1133 12922 12720 19395 -2540 -1328 861 O ATOM 2590 CB ALA A1133 -30.515-110.213 255.932 1.00120.67 C ANISOU 2590 CB ALA A1133 13320 12528 20000 -2597 -776 1350 C ATOM 2591 N ARG A1134 -28.060-112.723 256.958 1.00116.33 N ANISOU 2591 N ARG A1134 11873 13012 19315 -2494 -1051 1431 N ATOM 2592 CA ARG A1134 -27.990-113.870 257.861 1.00110.98 C ANISOU 2592 CA ARG A1134 11218 12611 18337 -2260 -1219 1236 C ATOM 2593 C ARG A1134 -27.994-113.452 259.328 1.00110.43 C ANISOU 2593 C ARG A1134 11324 12410 18226 -2453 -1684 874 C ATOM 2594 O ARG A1134 -28.612-114.113 260.171 1.00108.82 O ANISOU 2594 O ARG A1134 11408 12282 17657 -2222 -1787 631 O ATOM 2595 CB ARG A1134 -26.743-114.690 257.542 1.00112.52 C ANISOU 2595 CB ARG A1134 10884 13232 18638 -2173 -1150 1525 C ATOM 2596 CG ARG A1134 -26.646-115.981 258.310 1.00112.53 C ANISOU 2596 CG ARG A1134 10901 13509 18344 -1862 -1267 1408 C ATOM 2597 CD ARG A1134 -25.250-116.575 258.218 1.00117.40 C ANISOU 2597 CD ARG A1134 10941 14528 19139 -1809 -1292 1680 C ATOM 2598 NE ARG A1134 -25.065-117.639 259.199 1.00118.89 N ANISOU 2598 NE ARG A1134 11145 14939 19090 -1556 -1506 1572 N ATOM 2599 CZ ARG A1134 -25.355-118.916 258.976 1.00118.35 C ANISOU 2599 CZ ARG A1134 11205 14993 18770 -1115 -1285 1613 C ATOM 2600 NH1 ARG A1134 -25.158-119.818 259.928 1.00119.89 N ANISOU 2600 NH1 ARG A1134 11418 15353 18783 -900 -1495 1564 N ATOM 2601 NH2 ARG A1134 -25.842-119.292 257.802 1.00115.67 N ANISOU 2601 NH2 ARG A1134 10992 14599 18358 -885 -870 1703 N ATOM 2602 N ASP A1135 -27.314-112.346 259.647 1.00112.41 N ANISOU 2602 N ASP A1135 11411 12460 18841 -2883 -1974 835 N ATOM 2603 CA ASP A1135 -27.352-111.820 261.011 1.00113.08 C ANISOU 2603 CA ASP A1135 11721 12387 18856 -3071 -2452 419 C ATOM 2604 C ASP A1135 -28.768-111.437 261.420 1.00108.44 C ANISOU 2604 C ASP A1135 11755 11476 17973 -2899 -2410 77 C ATOM 2605 O ASP A1135 -29.193-111.716 262.548 1.00105.38 O ANISOU 2605 O ASP A1135 11654 11161 17226 -2752 -2634 -254 O ATOM 2606 CB ASP A1135 -26.421-110.616 261.132 1.00121.89 C ANISOU 2606 CB ASP A1135 12573 13257 20482 -3610 -2776 420 C ATOM 2607 CG ASP A1135 -25.028-111.000 261.576 1.00127.61 C ANISOU 2607 CG ASP A1135 12728 14374 21383 -3806 -3094 542 C ATOM 2608 OD1 ASP A1135 -24.597-112.131 261.276 1.00124.82 O ANISOU 2608 OD1 ASP A1135 12059 14476 20890 -3517 -2903 807 O ATOM 2609 OD2 ASP A1135 -24.365-110.170 262.234 1.00134.01 O ANISOU 2609 OD2 ASP A1135 13405 15030 22482 -4243 -3555 359 O ATOM 2610 N ASP A1136 -29.512-110.788 260.522 1.00108.03 N ANISOU 2610 N ASP A1136 11900 11098 18050 -2885 -2112 178 N ATOM 2611 CA ASP A1136 -30.882-110.400 260.843 1.00106.54 C ANISOU 2611 CA ASP A1136 12249 10627 17605 -2680 -2041 -111 C ATOM 2612 C ASP A1136 -31.773-111.621 261.026 1.00100.51 C ANISOU 2612 C ASP A1136 11660 10170 16358 -2249 -1836 -147 C ATOM 2613 O ASP A1136 -32.675-111.617 261.872 1.00 97.06 O ANISOU 2613 O ASP A1136 11593 9681 15605 -2067 -1900 -447 O ATOM 2614 CB ASP A1136 -31.441-109.487 259.752 1.00106.83 C ANISOU 2614 CB ASP A1136 12405 10287 17900 -2725 -1763 77 C ATOM 2615 CG ASP A1136 -30.659-108.198 259.617 1.00112.79 C ANISOU 2615 CG ASP A1136 13035 10635 19184 -3182 -1961 133 C ATOM 2616 OD1 ASP A1136 -30.115-107.725 260.637 1.00118.05 O ANISOU 2616 OD1 ASP A1136 13732 11161 19960 -3448 -2387 -179 O ATOM 2617 OD2 ASP A1136 -30.586-107.657 258.493 1.00112.94 O ANISOU 2617 OD2 ASP A1136 12930 10473 19509 -3284 -1704 497 O ATOM 2618 N ILE A1137 -31.537-112.675 260.244 1.00100.55 N ANISOU 2618 N ILE A1137 11406 10486 16310 -2078 -1580 156 N ATOM 2619 CA ILE A1137 -32.314-113.903 260.390 1.00101.03 C ANISOU 2619 CA ILE A1137 11616 10787 15983 -1718 -1409 139 C ATOM 2620 C ILE A1137 -32.021-114.556 261.736 1.00106.02 C ANISOU 2620 C ILE A1137 12281 11646 16356 -1648 -1691 -41 C ATOM 2621 O ILE A1137 -32.930-114.817 262.532 1.00106.94 O ANISOU 2621 O ILE A1137 12714 11779 16140 -1462 -1705 -237 O ATOM 2622 CB ILE A1137 -32.025-114.870 259.230 1.00 98.32 C ANISOU 2622 CB ILE A1137 11016 10674 15667 -1552 -1107 460 C ATOM 2623 CG1 ILE A1137 -32.235-114.179 257.883 1.00 97.14 C ANISOU 2623 CG1 ILE A1137 10826 10364 15719 -1606 -838 670 C ATOM 2624 CG2 ILE A1137 -32.912-116.100 259.337 1.00 95.24 C ANISOU 2624 CG2 ILE A1137 10817 10432 14940 -1227 -952 422 C ATOM 2625 CD1 ILE A1137 -31.932-115.071 256.695 1.00 95.78 C ANISOU 2625 CD1 ILE A1137 10432 10447 15512 -1411 -539 945 C ATOM 2626 N VAL A1138 -30.742-114.831 262.004 1.00106.85 N ANISOU 2626 N VAL A1138 12032 11969 16598 -1779 -1910 60 N ATOM 2627 CA VAL A1138 -30.360-115.477 263.255 1.00107.48 C ANISOU 2627 CA VAL A1138 12108 12316 16413 -1690 -2205 -60 C ATOM 2628 C VAL A1138 -30.684-114.584 264.443 1.00109.39 C ANISOU 2628 C VAL A1138 12668 12414 16483 -1810 -2538 -451 C ATOM 2629 O VAL A1138 -31.051-115.074 265.519 1.00109.85 O ANISOU 2629 O VAL A1138 12945 12655 16139 -1615 -2668 -607 O ATOM 2630 CB VAL A1138 -28.868-115.864 263.215 1.00112.18 C ANISOU 2630 CB VAL A1138 12196 13198 17230 -1800 -2390 156 C ATOM 2631 CG1 VAL A1138 -28.436-116.483 264.534 1.00116.99 C ANISOU 2631 CG1 VAL A1138 12789 14111 17549 -1691 -2739 56 C ATOM 2632 CG2 VAL A1138 -28.609-116.824 262.065 1.00110.22 C ANISOU 2632 CG2 VAL A1138 11688 13106 17086 -1584 -2020 505 C ATOM 2633 N GLY A1139 -30.568-113.265 264.273 1.00112.41 N ANISOU 2633 N GLY A1139 13104 12454 17153 -2113 -2670 -613 N ATOM 2634 CA GLY A1139 -31.009-112.358 265.319 1.00115.52 C ANISOU 2634 CA GLY A1139 13885 12636 17373 -2180 -2957 -1052 C ATOM 2635 C GLY A1139 -32.498-112.462 265.585 1.00111.40 C ANISOU 2635 C GLY A1139 13819 12037 16472 -1841 -2696 -1206 C ATOM 2636 O GLY A1139 -32.941-112.381 266.733 1.00113.25 O ANISOU 2636 O GLY A1139 14366 12348 16316 -1693 -2866 -1517 O ATOM 2637 N TRP A1140 -33.291-112.653 264.526 1.00105.28 N ANISOU 2637 N TRP A1140 13065 11151 15785 -1700 -2278 -981 N ATOM 2638 CA TRP A1140 -34.734-112.796 264.695 1.00104.64 C ANISOU 2638 CA TRP A1140 13329 11038 15390 -1388 -2016 -1075 C ATOM 2639 C TRP A1140 -35.069-114.045 265.494 1.00105.86 C ANISOU 2639 C TRP A1140 13530 11582 15112 -1118 -1972 -1025 C ATOM 2640 O TRP A1140 -35.851-113.991 266.451 1.00107.94 O ANISOU 2640 O TRP A1140 14093 11917 15002 -918 -1979 -1236 O ATOM 2641 CB TRP A1140 -35.428-112.847 263.336 1.00101.74 C ANISOU 2641 CB TRP A1140 12907 10537 15212 -1311 -1628 -814 C ATOM 2642 CG TRP A1140 -36.921-112.746 263.434 1.00101.24 C ANISOU 2642 CG TRP A1140 13146 10410 14912 -1037 -1391 -911 C ATOM 2643 CD1 TRP A1140 -37.637-111.651 263.815 1.00103.94 C ANISOU 2643 CD1 TRP A1140 13798 10473 15222 -968 -1410 -1178 C ATOM 2644 CD2 TRP A1140 -37.882-113.772 263.140 1.00 98.35 C ANISOU 2644 CD2 TRP A1140 12773 10257 14338 -791 -1102 -735 C ATOM 2645 NE1 TRP A1140 -38.981-111.928 263.783 1.00101.93 N ANISOU 2645 NE1 TRP A1140 13690 10301 14739 -670 -1131 -1153 N ATOM 2646 CE2 TRP A1140 -39.159-113.221 263.367 1.00 98.27 C ANISOU 2646 CE2 TRP A1140 13022 10138 14180 -591 -953 -878 C ATOM 2647 CE3 TRP A1140 -37.788-115.099 262.707 1.00 95.67 C ANISOU 2647 CE3 TRP A1140 12234 10165 13949 -723 -966 -481 C ATOM 2648 CZ2 TRP A1140 -40.332-113.951 263.180 1.00 94.32 C ANISOU 2648 CZ2 TRP A1140 12528 9809 13501 -370 -685 -746 C ATOM 2649 CZ3 TRP A1140 -38.955-115.822 262.522 1.00 91.85 C ANISOU 2649 CZ3 TRP A1140 11811 9786 13299 -525 -722 -384 C ATOM 2650 CH2 TRP A1140 -40.209-115.246 262.759 1.00 90.95 C ANISOU 2650 CH2 TRP A1140 11899 9600 13056 -372 -589 -502 C ATOM 2651 N ALA A1141 -34.498-115.186 265.096 1.00104.74 N ANISOU 2651 N ALA A1141 13097 11684 15014 -1084 -1899 -723 N ATOM 2652 CA ALA A1141 -34.710-116.429 265.828 1.00101.78 C ANISOU 2652 CA ALA A1141 12755 11628 14291 -844 -1864 -611 C ATOM 2653 C ALA A1141 -34.507-116.219 267.320 1.00105.72 C ANISOU 2653 C ALA A1141 13435 12310 14424 -796 -2186 -859 C ATOM 2654 O ALA A1141 -35.347-116.614 268.131 1.00105.76 O ANISOU 2654 O ALA A1141 13683 12472 14029 -557 -2090 -898 O ATOM 2655 CB ALA A1141 -33.773-117.517 265.301 1.00 99.84 C ANISOU 2655 CB ALA A1141 12163 11567 14206 -833 -1843 -298 C ATOM 2656 N HIS A1142 -33.417-115.543 267.692 1.00110.82 N ANISOU 2656 N HIS A1142 13963 12951 15192 -1029 -2577 -1032 N ATOM 2657 CA HIS A1142 -33.126-115.306 269.103 1.00118.62 C ANISOU 2657 CA HIS A1142 15129 14144 15798 -992 -2956 -1316 C ATOM 2658 C HIS A1142 -34.243-114.516 269.776 1.00123.78 C ANISOU 2658 C HIS A1142 16245 14659 16124 -840 -2901 -1677 C ATOM 2659 O HIS A1142 -34.721-114.892 270.853 1.00126.55 O ANISOU 2659 O HIS A1142 16834 15291 15956 -576 -2920 -1765 O ATOM 2660 CB HIS A1142 -31.790-114.578 269.243 1.00123.25 C ANISOU 2660 CB HIS A1142 15478 14694 16656 -1340 -3424 -1476 C ATOM 2661 CG HIS A1142 -31.185-114.688 270.606 1.00128.55 C ANISOU 2661 CG HIS A1142 16204 15708 16931 -1301 -3885 -1683 C ATOM 2662 ND1 HIS A1142 -31.657-113.980 271.691 1.00132.09 N ANISOU 2662 ND1 HIS A1142 17078 16148 16962 -1219 -4110 -2133 N ATOM 2663 CD2 HIS A1142 -30.145-115.425 271.063 1.00131.20 C ANISOU 2663 CD2 HIS A1142 16228 16435 17189 -1295 -4174 -1503 C ATOM 2664 CE1 HIS A1142 -30.934-114.276 272.755 1.00136.65 C ANISOU 2664 CE1 HIS A1142 17614 17115 17190 -1181 -4537 -2232 C ATOM 2665 NE2 HIS A1142 -30.010-115.151 272.402 1.00136.16 N ANISOU 2665 NE2 HIS A1142 17092 17304 17340 -1230 -4591 -1836 N ATOM 2666 N ASP A1143 -34.672-113.413 269.156 1.00125.27 N ANISOU 2666 N ASP A1143 16569 14429 16600 -969 -2811 -1864 N ATOM 2667 CA ASP A1143 -35.748-112.608 269.728 1.00129.08 C ANISOU 2667 CA ASP A1143 17490 14749 16805 -769 -2728 -2214 C ATOM 2668 C ASP A1143 -37.023-113.430 269.880 1.00127.24 C ANISOU 2668 C ASP A1143 17379 14748 16218 -396 -2304 -2016 C ATOM 2669 O ASP A1143 -37.580-113.542 270.978 1.00128.91 O ANISOU 2669 O ASP A1143 17854 15208 15916 -123 -2296 -2177 O ATOM 2670 CB ASP A1143 -36.009-111.376 268.860 1.00129.87 C ANISOU 2670 CB ASP A1143 17681 14317 17349 -939 -2655 -2351 C ATOM 2671 CG ASP A1143 -34.878-110.372 268.908 1.00136.21 C ANISOU 2671 CG ASP A1143 18431 14820 18502 -1335 -3097 -2602 C ATOM 2672 OD1 ASP A1143 -34.026-110.474 269.814 1.00140.93 O ANISOU 2672 OD1 ASP A1143 18993 15639 18915 -1446 -3513 -2792 O ATOM 2673 OD2 ASP A1143 -34.850-109.471 268.044 1.00136.87 O ANISOU 2673 OD2 ASP A1143 18501 14449 19056 -1544 -3042 -2590 O ATOM 2674 N VAL A1144 -37.505-114.003 268.775 1.00124.31 N ANISOU 2674 N VAL A1144 16807 14316 16110 -385 -1949 -1660 N ATOM 2675 CA VAL A1144 -38.717-114.819 268.820 1.00122.25 C ANISOU 2675 CA VAL A1144 16596 14250 15602 -102 -1565 -1441 C ATOM 2676 C VAL A1144 -38.539-115.989 269.778 1.00123.55 C ANISOU 2676 C VAL A1144 16735 14834 15373 51 -1602 -1259 C ATOM 2677 O VAL A1144 -39.459-116.344 270.527 1.00124.40 O ANISOU 2677 O VAL A1144 17008 15172 15086 316 -1402 -1216 O ATOM 2678 CB VAL A1144 -39.092-115.291 267.404 1.00116.94 C ANISOU 2678 CB VAL A1144 15687 13439 15307 -172 -1269 -1118 C ATOM 2679 CG1 VAL A1144 -40.231-116.299 267.459 1.00113.27 C ANISOU 2679 CG1 VAL A1144 15209 13184 14644 45 -934 -865 C ATOM 2680 CG2 VAL A1144 -39.480-114.104 266.555 1.00118.17 C ANISOU 2680 CG2 VAL A1144 15912 13222 15767 -245 -1192 -1253 C ATOM 2681 N ARG A1145 -37.354-116.602 269.778 1.00122.90 N ANISOU 2681 N ARG A1145 16427 14876 15394 -91 -1841 -1110 N ATOM 2682 CA ARG A1145 -37.063-117.639 270.762 1.00126.57 C ANISOU 2682 CA ARG A1145 16884 15728 15479 76 -1927 -923 C ATOM 2683 C ARG A1145 -37.150-117.083 272.176 1.00139.57 C ANISOU 2683 C ARG A1145 18838 17610 16583 242 -2150 -1243 C ATOM 2684 O ARG A1145 -37.638-117.760 273.088 1.00145.33 O ANISOU 2684 O ARG A1145 19698 18675 16846 506 -2035 -1092 O ATOM 2685 CB ARG A1145 -35.678-118.231 270.507 1.00122.27 C ANISOU 2685 CB ARG A1145 16023 15268 15165 -78 -2188 -737 C ATOM 2686 CG ARG A1145 -35.448-119.614 271.057 1.00117.42 C ANISOU 2686 CG ARG A1145 15323 14966 14325 118 -2162 -372 C ATOM 2687 CD ARG A1145 -34.213-120.233 270.421 1.00109.77 C ANISOU 2687 CD ARG A1145 13991 14003 13714 7 -2307 -145 C ATOM 2688 NE ARG A1145 -33.029-119.390 270.556 1.00106.83 N ANISOU 2688 NE ARG A1145 13452 13667 13473 -212 -2731 -379 N ATOM 2689 N GLY A1146 -36.700-115.842 272.370 1.00146.07 N ANISOU 2689 N GLY A1146 19798 18251 17452 93 -2466 -1687 N ATOM 2690 CA GLY A1146 -36.674-115.270 273.708 1.00152.00 C ANISOU 2690 CA GLY A1146 20878 19215 17661 252 -2745 -2079 C ATOM 2691 C GLY A1146 -38.056-115.136 274.319 1.00153.49 C ANISOU 2691 C GLY A1146 21399 19528 17390 620 -2394 -2167 C ATOM 2692 O GLY A1146 -38.282-115.529 275.465 1.00158.71 O ANISOU 2692 O GLY A1146 22248 20609 17446 905 -2405 -2165 O ATOM 2693 N ALA A1147 -38.997-114.580 273.562 1.00148.02 N ANISOU 2693 N ALA A1147 20764 18514 16962 646 -2067 -2213 N ATOM 2694 CA ALA A1147 -40.349-114.412 274.074 1.00148.72 C ANISOU 2694 CA ALA A1147 21104 18740 16660 1018 -1698 -2271 C ATOM 2695 C ALA A1147 -41.014-115.771 274.255 1.00142.74 C ANISOU 2695 C ALA A1147 20182 18361 15691 1201 -1328 -1740 C ATOM 2696 O ALA A1147 -41.007-116.606 273.344 1.00139.57 O ANISOU 2696 O ALA A1147 19476 17866 15689 1031 -1165 -1339 O ATOM 2697 CB ALA A1147 -41.168-113.530 273.136 1.00150.29 C ANISOU 2697 CB ALA A1147 21342 18514 17249 1011 -1450 -2392 C ATOM 2698 N ILE A1148 -41.576-115.990 275.441 1.00142.05 N ANISOU 2698 N ILE A1148 20309 18692 14970 1548 -1197 -1739 N ATOM 2699 CA ILE A1148 -42.209-117.254 275.804 1.00137.70 C ANISOU 2699 CA ILE A1148 19623 18517 14179 1721 -847 -1201 C ATOM 2700 C ILE A1148 -42.915-117.098 277.147 1.00140.65 C ANISOU 2700 C ILE A1148 20291 19351 13797 2153 -675 -1294 C ATOM 2701 O ILE A1148 -43.222-118.084 277.818 1.00141.04 O ANISOU 2701 O ILE A1148 20291 19808 13487 2330 -462 -862 O ATOM 2702 CB ILE A1148 -41.189-118.407 275.855 1.00135.72 C ANISOU 2702 CB ILE A1148 19163 18403 14000 1561 -1060 -830 C ATOM 2703 N MET A 337 -38.055-129.441 283.165 1.00164.30 N ANISOU 2703 N MET A 337 24998 17545 19885 -3968 -4311 2026 N ATOM 2704 CA MET A 337 -37.487-130.780 283.051 1.00161.57 C ANISOU 2704 CA MET A 337 24503 17636 19251 -4016 -3727 1850 C ATOM 2705 C MET A 337 -37.613-131.555 284.363 1.00159.30 C ANISOU 2705 C MET A 337 23486 17640 19401 -3474 -3320 1602 C ATOM 2706 O MET A 337 -37.943-132.741 284.357 1.00158.62 O ANISOU 2706 O MET A 337 23178 17730 19360 -3319 -3135 1503 O ATOM 2707 CB MET A 337 -36.020-130.703 282.622 1.00162.38 C ANISOU 2707 CB MET A 337 24901 18019 18778 -4480 -3224 1789 C ATOM 2708 N ASP A 338 -37.351-130.870 285.478 1.00157.24 N ANISOU 2708 N ASP A 338 22899 17408 19437 -3215 -3197 1506 N ATOM 2709 CA ASP A 338 -37.405-131.462 286.817 1.00153.82 C ANISOU 2709 CA ASP A 338 21849 17223 19375 -2745 -2820 1277 C ATOM 2710 C ASP A 338 -36.523-132.706 286.909 1.00149.78 C ANISOU 2710 C ASP A 338 21157 17161 18593 -2783 -2228 1101 C ATOM 2711 O ASP A 338 -36.965-133.786 287.307 1.00146.65 O ANISOU 2711 O ASP A 338 20429 16914 18377 -2507 -2055 986 O ATOM 2712 CB ASP A 338 -38.845-131.784 287.223 1.00156.43 C ANISOU 2712 CB ASP A 338 21858 17339 20238 -2338 -3115 1264 C ATOM 2713 CG ASP A 338 -39.667-130.541 287.494 1.00161.84 C ANISOU 2713 CG ASP A 338 22545 17587 21359 -2182 -3618 1354 C ATOM 2714 OD1 ASP A 338 -39.070-129.461 287.691 1.00163.48 O ANISOU 2714 OD1 ASP A 338 22919 17705 21489 -2305 -3664 1391 O ATOM 2715 OD2 ASP A 338 -40.910-130.645 287.520 1.00162.96 O ANISOU 2715 OD2 ASP A 338 22498 17460 21959 -1933 -3969 1374 O ATOM 2716 N ILE A 339 -35.250-132.538 286.544 1.00146.78 N ANISOU 2716 N ILE A 339 20985 16980 17807 -3136 -1914 1070 N ATOM 2717 CA ILE A 339 -34.332-133.674 286.491 1.00142.27 C ANISOU 2717 CA ILE A 339 20254 16796 17008 -3210 -1368 888 C ATOM 2718 C ILE A 339 -34.143-134.281 287.874 1.00138.82 C ANISOU 2718 C ILE A 339 19248 16599 16898 -2775 -1048 688 C ATOM 2719 O ILE A 339 -34.150-135.509 288.035 1.00140.27 O ANISOU 2719 O ILE A 339 19187 16992 17116 -2617 -788 561 O ATOM 2720 CB ILE A 339 -32.988-133.246 285.876 1.00142.84 C ANISOU 2720 CB ILE A 339 20613 17001 16657 -3683 -1079 865 C ATOM 2721 CG1 ILE A 339 -33.194-132.760 284.443 1.00146.88 C ANISOU 2721 CG1 ILE A 339 21779 17268 16760 -4176 -1376 1068 C ATOM 2722 CG2 ILE A 339 -31.991-134.395 285.918 1.00142.64 C ANISOU 2722 CG2 ILE A 339 20334 17358 16507 -3719 -495 631 C ATOM 2723 CD1 ILE A 339 -31.911-132.556 283.689 1.00149.45 C ANISOU 2723 CD1 ILE A 339 22421 17745 16618 -4707 -996 1014 C ATOM 2724 N GLU A 340 -33.964-133.435 288.893 1.00135.63 N ANISOU 2724 N GLU A 340 18664 16149 16720 -2596 -1078 659 N ATOM 2725 CA GLU A 340 -33.791-133.935 290.254 1.00130.95 C ANISOU 2725 CA GLU A 340 17610 15748 16395 -2222 -813 484 C ATOM 2726 C GLU A 340 -34.959-134.817 290.670 1.00124.41 C ANISOU 2726 C GLU A 340 16536 14884 15852 -1867 -877 447 C ATOM 2727 O GLU A 340 -34.769-135.842 291.335 1.00119.62 O ANISOU 2727 O GLU A 340 15630 14501 15318 -1661 -586 305 O ATOM 2728 CB GLU A 340 -33.629-132.765 291.223 1.00132.00 C ANISOU 2728 CB GLU A 340 17677 15761 16714 -2107 -913 476 C ATOM 2729 CG GLU A 340 -32.393-131.928 290.962 1.00135.48 C ANISOU 2729 CG GLU A 340 18310 16259 16906 -2451 -817 495 C ATOM 2730 CD GLU A 340 -31.118-132.737 291.068 1.00136.22 C ANISOU 2730 CD GLU A 340 18207 16703 16846 -2557 -370 336 C ATOM 2731 OE1 GLU A 340 -31.035-133.603 291.964 1.00134.65 O ANISOU 2731 OE1 GLU A 340 17658 16682 16822 -2263 -169 195 O ATOM 2732 OE2 GLU A 340 -30.199-132.513 290.253 1.00138.48 O ANISOU 2732 OE2 GLU A 340 18691 17068 16856 -2946 -220 343 O ATOM 2733 N LEU A 341 -36.177-134.436 290.281 1.00122.39 N ANISOU 2733 N LEU A 341 16397 14326 15781 -1802 -1277 573 N ATOM 2734 CA LEU A 341 -37.327-135.304 290.493 1.00117.08 C ANISOU 2734 CA LEU A 341 15494 13601 15389 -1520 -1344 540 C ATOM 2735 C LEU A 341 -37.182-136.611 289.724 1.00113.94 C ANISOU 2735 C LEU A 341 15141 13397 14753 -1638 -1172 520 C ATOM 2736 O LEU A 341 -37.451-137.689 290.267 1.00114.14 O ANISOU 2736 O LEU A 341 14879 13575 14913 -1405 -960 407 O ATOM 2737 CB LEU A 341 -38.607-134.582 290.074 1.00118.61 C ANISOU 2737 CB LEU A 341 15799 13396 15873 -1466 -1856 681 C ATOM 2738 CG LEU A 341 -39.813-135.468 289.757 1.00117.95 C ANISOU 2738 CG LEU A 341 15579 13209 16026 -1310 -2026 697 C ATOM 2739 CD1 LEU A 341 -40.365-136.112 291.020 1.00114.50 C ANISOU 2739 CD1 LEU A 341 14676 12871 15958 -920 -1760 517 C ATOM 2740 CD2 LEU A 341 -40.888-134.671 289.035 1.00122.42 C ANISOU 2740 CD2 LEU A 341 16330 13342 16844 -1354 -2624 869 C ATOM 2741 N ALA A 342 -36.755-136.534 288.460 1.00113.21 N ANISOU 2741 N ALA A 342 15438 13287 14288 -2022 -1250 622 N ATOM 2742 CA ALA A 342 -36.657-137.728 287.626 1.00112.70 C ANISOU 2742 CA ALA A 342 15474 13370 13978 -2168 -1092 589 C ATOM 2743 C ALA A 342 -35.722-138.762 288.239 1.00108.45 C ANISOU 2743 C ALA A 342 14629 13185 13392 -2055 -578 381 C ATOM 2744 O ALA A 342 -36.028-139.960 288.244 1.00109.58 O ANISOU 2744 O ALA A 342 14615 13438 13583 -1919 -443 302 O ATOM 2745 CB ALA A 342 -36.190-137.350 286.221 1.00118.34 C ANISOU 2745 CB ALA A 342 16721 14007 14237 -2663 -1194 706 C ATOM 2746 N LYS A 343 -34.577-138.316 288.764 1.00103.72 N ANISOU 2746 N LYS A 343 13938 12745 12727 -2111 -319 291 N ATOM 2747 CA LYS A 343 -33.648-139.237 289.413 1.00 99.89 C ANISOU 2747 CA LYS A 343 13135 12553 12266 -1987 102 95 C ATOM 2748 C LYS A 343 -34.315-139.973 290.569 1.00 97.94 C ANISOU 2748 C LYS A 343 12530 12342 12341 -1567 125 27 C ATOM 2749 O LYS A 343 -34.140-141.187 290.725 1.00 97.73 O ANISOU 2749 O LYS A 343 12320 12478 12336 -1452 347 -86 O ATOM 2750 CB LYS A 343 -32.419-138.480 289.914 1.00100.88 C ANISOU 2750 CB LYS A 343 13189 12787 12353 -2091 283 26 C ATOM 2751 CG LYS A 343 -31.521-137.907 288.832 1.00104.10 C ANISOU 2751 CG LYS A 343 13913 13213 12428 -2549 388 44 C ATOM 2752 CD LYS A 343 -30.457-137.026 289.466 1.00106.28 C ANISOU 2752 CD LYS A 343 14080 13557 12743 -2623 506 -9 C ATOM 2753 CE LYS A 343 -29.181-136.992 288.645 1.00111.33 C ANISOU 2753 CE LYS A 343 14830 14343 13128 -3035 839 -112 C ATOM 2754 NZ LYS A 343 -28.060-136.388 289.418 1.00113.02 N ANISOU 2754 NZ LYS A 343 14814 14660 13468 -3055 990 -206 N ATOM 2755 N THR A 344 -35.085-139.252 291.388 1.00 95.89 N ANISOU 2755 N THR A 344 12183 11915 12337 -1350 -87 83 N ATOM 2756 CA THR A 344 -35.697-139.865 292.563 1.00 92.34 C ANISOU 2756 CA THR A 344 11429 11490 12166 -997 -14 2 C ATOM 2757 C THR A 344 -36.693-140.950 292.172 1.00 88.60 C ANISOU 2757 C THR A 344 10899 10984 11779 -894 -62 14 C ATOM 2758 O THR A 344 -36.713-142.029 292.775 1.00 87.18 O ANISOU 2758 O THR A 344 10510 10940 11675 -715 138 -84 O ATOM 2759 CB THR A 344 -36.382-138.798 293.418 1.00 93.51 C ANISOU 2759 CB THR A 344 11524 11433 12572 -826 -196 31 C ATOM 2760 OG1 THR A 344 -37.393-138.138 292.646 1.00 97.92 O ANISOU 2760 OG1 THR A 344 12249 11716 13240 -887 -551 164 O ATOM 2761 CG2 THR A 344 -35.369-137.771 293.902 1.00 93.65 C ANISOU 2761 CG2 THR A 344 11597 11483 12502 -921 -146 11 C ATOM 2762 N LEU A 345 -37.527-140.682 291.165 1.00 88.30 N ANISOU 2762 N LEU A 345 11066 10746 11736 -1019 -362 142 N ATOM 2763 CA LEU A 345 -38.533-141.658 290.758 1.00 88.44 C ANISOU 2763 CA LEU A 345 11035 10705 11863 -937 -459 162 C ATOM 2764 C LEU A 345 -37.891-142.940 290.249 1.00 87.11 C ANISOU 2764 C LEU A 345 10890 10758 11449 -1036 -196 79 C ATOM 2765 O LEU A 345 -38.324-144.043 290.605 1.00 85.67 O ANISOU 2765 O LEU A 345 10517 10643 11391 -857 -85 12 O ATOM 2766 CB LEU A 345 -39.444-141.060 289.687 1.00 91.70 C ANISOU 2766 CB LEU A 345 11706 10830 12305 -1093 -902 330 C ATOM 2767 CG LEU A 345 -40.428-140.003 290.180 1.00 93.42 C ANISOU 2767 CG LEU A 345 11820 10759 12918 -923 -1218 391 C ATOM 2768 CD1 LEU A 345 -41.189-139.397 289.013 1.00 96.82 C ANISOU 2768 CD1 LEU A 345 12543 10872 13374 -1111 -1732 576 C ATOM 2769 CD2 LEU A 345 -41.384-140.613 291.190 1.00 92.00 C ANISOU 2769 CD2 LEU A 345 11249 10559 13147 -586 -1115 284 C ATOM 2770 N VAL A 346 -36.860-142.815 289.410 1.00 86.43 N ANISOU 2770 N VAL A 346 11039 10774 11027 -1332 -75 67 N ATOM 2771 CA VAL A 346 -36.158-143.991 288.907 1.00 83.68 C ANISOU 2771 CA VAL A 346 10697 10622 10475 -1434 221 -57 C ATOM 2772 C VAL A 346 -35.583-144.802 290.060 1.00 80.59 C ANISOU 2772 C VAL A 346 9944 10427 10249 -1169 519 -214 C ATOM 2773 O VAL A 346 -35.679-146.036 290.079 1.00 81.85 O ANISOU 2773 O VAL A 346 9986 10669 10443 -1064 655 -299 O ATOM 2774 CB VAL A 346 -35.063-143.569 287.909 1.00 82.95 C ANISOU 2774 CB VAL A 346 10895 10598 10023 -1821 371 -85 C ATOM 2775 CG1 VAL A 346 -34.250-144.774 287.473 1.00 83.38 C ANISOU 2775 CG1 VAL A 346 10900 10851 9929 -1908 743 -271 C ATOM 2776 CG2 VAL A 346 -35.683-142.874 286.708 1.00 83.43 C ANISOU 2776 CG2 VAL A 346 11405 10432 9862 -2126 32 94 C ATOM 2777 N LEU A 347 -34.996-144.121 291.048 1.00 76.67 N ANISOU 2777 N LEU A 347 9293 9980 9856 -1066 586 -246 N ATOM 2778 CA LEU A 347 -34.409-144.821 292.185 1.00 74.97 C ANISOU 2778 CA LEU A 347 8787 9915 9784 -840 800 -373 C ATOM 2779 C LEU A 347 -35.449-145.648 292.931 1.00 75.48 C ANISOU 2779 C LEU A 347 8696 9930 10054 -567 754 -368 C ATOM 2780 O LEU A 347 -35.185-146.797 293.304 1.00 79.88 O ANISOU 2780 O LEU A 347 9106 10591 10654 -446 911 -460 O ATOM 2781 CB LEU A 347 -33.748-143.824 293.134 1.00 73.41 C ANISOU 2781 CB LEU A 347 8509 9733 9651 -797 805 -384 C ATOM 2782 CG LEU A 347 -32.964-144.461 294.280 1.00 70.18 C ANISOU 2782 CG LEU A 347 7852 9454 9357 -614 969 -503 C ATOM 2783 CD1 LEU A 347 -31.689-145.099 293.752 1.00 70.00 C ANISOU 2783 CD1 LEU A 347 7739 9591 9268 -746 1189 -638 C ATOM 2784 CD2 LEU A 347 -32.658-143.438 295.360 1.00 70.18 C ANISOU 2784 CD2 LEU A 347 7819 9416 9432 -548 900 -487 C ATOM 2785 N ILE A 348 -36.636-145.080 293.161 1.00 71.16 N ANISOU 2785 N ILE A 348 8168 9206 9662 -475 544 -271 N ATOM 2786 CA ILE A 348 -37.691-145.821 293.850 1.00 69.58 C ANISOU 2786 CA ILE A 348 7810 8949 9680 -251 540 -281 C ATOM 2787 C ILE A 348 -38.018-147.097 293.090 1.00 69.91 C ANISOU 2787 C ILE A 348 7868 9026 9670 -280 568 -295 C ATOM 2788 O ILE A 348 -38.076-148.189 293.667 1.00 67.17 O ANISOU 2788 O ILE A 348 7382 8750 9388 -138 709 -362 O ATOM 2789 CB ILE A 348 -38.942-144.944 294.031 1.00 69.08 C ANISOU 2789 CB ILE A 348 7734 8660 9855 -174 317 -204 C ATOM 2790 CG1 ILE A 348 -38.601-143.675 294.810 1.00 66.27 C ANISOU 2790 CG1 ILE A 348 7377 8250 9550 -143 304 -213 C ATOM 2791 CG2 ILE A 348 -40.040-145.727 294.737 1.00 69.34 C ANISOU 2791 CG2 ILE A 348 7574 8632 10139 27 372 -244 C ATOM 2792 CD1 ILE A 348 -39.799-142.800 295.091 1.00 65.76 C ANISOU 2792 CD1 ILE A 348 7258 7940 9788 -39 117 -181 C ATOM 2793 N LEU A 349 -38.227-146.976 291.776 1.00 71.72 N ANISOU 2793 N LEU A 349 8306 9187 9758 -487 416 -226 N ATOM 2794 CA LEU A 349 -38.533-148.147 290.965 1.00 69.12 C ANISOU 2794 CA LEU A 349 8041 8873 9348 -548 429 -245 C ATOM 2795 C LEU A 349 -37.388-149.150 290.991 1.00 69.27 C ANISOU 2795 C LEU A 349 8000 9091 9230 -556 731 -392 C ATOM 2796 O LEU A 349 -37.618-150.361 291.094 1.00 68.93 O ANISOU 2796 O LEU A 349 7867 9081 9243 -453 817 -452 O ATOM 2797 CB LEU A 349 -38.853-147.721 289.533 1.00 68.57 C ANISOU 2797 CB LEU A 349 8288 8675 9089 -823 192 -141 C ATOM 2798 CG LEU A 349 -40.107-146.852 289.406 1.00 69.72 C ANISOU 2798 CG LEU A 349 8476 8566 9450 -799 -195 10 C ATOM 2799 CD1 LEU A 349 -40.450-146.587 287.948 1.00 71.61 C ANISOU 2799 CD1 LEU A 349 9086 8643 9479 -1094 -502 134 C ATOM 2800 CD2 LEU A 349 -41.279-147.499 290.133 1.00 68.44 C ANISOU 2800 CD2 LEU A 349 8036 8324 9645 -543 -243 -2 C ATOM 2801 N VAL A 350 -36.146-148.669 290.909 1.00 69.72 N ANISOU 2801 N VAL A 350 8084 9262 9147 -677 889 -463 N ATOM 2802 CA VAL A 350 -35.006-149.573 291.024 1.00 72.05 C ANISOU 2802 CA VAL A 350 8246 9716 9412 -656 1168 -632 C ATOM 2803 C VAL A 350 -34.983-150.219 292.402 1.00 71.59 C ANISOU 2803 C VAL A 350 7931 9696 9576 -366 1217 -674 C ATOM 2804 O VAL A 350 -34.756-151.426 292.534 1.00 71.88 O ANISOU 2804 O VAL A 350 7862 9778 9671 -267 1329 -769 O ATOM 2805 CB VAL A 350 -33.691-148.832 290.721 1.00 73.59 C ANISOU 2805 CB VAL A 350 8470 10009 9481 -850 1327 -712 C ATOM 2806 CG1 VAL A 350 -32.502-149.741 290.980 1.00 74.17 C ANISOU 2806 CG1 VAL A 350 8317 10219 9643 -787 1596 -913 C ATOM 2807 CG2 VAL A 350 -33.679-148.348 289.281 1.00 74.82 C ANISOU 2807 CG2 VAL A 350 8955 10121 9352 -1197 1317 -680 C ATOM 2808 N VAL A 351 -35.238-149.430 293.448 1.00 70.52 N ANISOU 2808 N VAL A 351 7726 9516 9551 -243 1124 -604 N ATOM 2809 CA VAL A 351 -35.294-149.982 294.800 1.00 70.34 C ANISOU 2809 CA VAL A 351 7543 9501 9680 -16 1157 -629 C ATOM 2810 C VAL A 351 -36.427-150.996 294.914 1.00 74.58 C ANISOU 2810 C VAL A 351 8062 9967 10307 98 1128 -600 C ATOM 2811 O VAL A 351 -36.233-152.116 295.402 1.00 73.08 O ANISOU 2811 O VAL A 351 7792 9807 10169 209 1204 -657 O ATOM 2812 CB VAL A 351 -35.437-148.853 295.836 1.00 67.53 C ANISOU 2812 CB VAL A 351 7181 9092 9386 50 1085 -575 C ATOM 2813 CG1 VAL A 351 -35.927-149.407 297.160 1.00 68.22 C ANISOU 2813 CG1 VAL A 351 7200 9137 9583 239 1110 -579 C ATOM 2814 CG2 VAL A 351 -34.108-148.140 296.021 1.00 66.41 C ANISOU 2814 CG2 VAL A 351 7013 9033 9186 -31 1126 -626 C ATOM 2815 N LEU A 352 -37.623-150.621 294.453 1.00 78.24 N ANISOU 2815 N LEU A 352 8595 10315 10819 63 993 -509 N ATOM 2816 CA LEU A 352 -38.774-151.517 294.549 1.00 79.66 C ANISOU 2816 CA LEU A 352 8728 10414 11128 152 960 -483 C ATOM 2817 C LEU A 352 -38.525-152.822 293.804 1.00 80.32 C ANISOU 2817 C LEU A 352 8842 10549 11128 111 1022 -542 C ATOM 2818 O LEU A 352 -38.747-153.911 294.347 1.00 80.62 O ANISOU 2818 O LEU A 352 8806 10585 11241 226 1090 -574 O ATOM 2819 CB LEU A 352 -40.029-150.830 294.009 1.00 80.85 C ANISOU 2819 CB LEU A 352 8913 10404 11401 104 756 -387 C ATOM 2820 CG LEU A 352 -40.889-150.045 294.999 1.00 80.82 C ANISOU 2820 CG LEU A 352 8793 10283 11634 225 726 -365 C ATOM 2821 CD1 LEU A 352 -42.268-149.783 294.412 1.00 82.43 C ANISOU 2821 CD1 LEU A 352 8954 10295 12073 210 508 -297 C ATOM 2822 CD2 LEU A 352 -40.999-150.786 296.320 1.00 80.23 C ANISOU 2822 CD2 LEU A 352 8608 10245 11632 371 928 -430 C ATOM 2823 N ILE A 353 -38.065-152.732 292.555 1.00 82.00 N ANISOU 2823 N ILE A 353 9195 10792 11169 -72 1011 -564 N ATOM 2824 CA ILE A 353 -37.851-153.932 291.750 1.00 82.63 C ANISOU 2824 CA ILE A 353 9335 10902 11160 -133 1094 -649 C ATOM 2825 C ILE A 353 -36.786-154.819 292.383 1.00 82.30 C ANISOU 2825 C ILE A 353 9147 10959 11165 -10 1287 -785 C ATOM 2826 O ILE A 353 -36.896-156.051 292.374 1.00 85.02 O ANISOU 2826 O ILE A 353 9457 11285 11560 64 1335 -845 O ATOM 2827 CB ILE A 353 -37.491-153.542 290.304 1.00 84.54 C ANISOU 2827 CB ILE A 353 9814 11149 11161 -405 1085 -667 C ATOM 2828 CG1 ILE A 353 -38.707-152.921 289.610 1.00 85.77 C ANISOU 2828 CG1 ILE A 353 10147 11146 11296 -524 795 -510 C ATOM 2829 CG2 ILE A 353 -36.985-154.749 289.525 1.00 84.42 C ANISOU 2829 CG2 ILE A 353 9864 11178 11033 -482 1257 -815 C ATOM 2830 CD1 ILE A 353 -38.364-152.123 288.374 1.00 87.60 C ANISOU 2830 CD1 ILE A 353 10686 11346 11253 -828 721 -476 C ATOM 2831 N ILE A 354 -35.753-154.210 292.966 1.00 81.17 N ANISOU 2831 N ILE A 354 8910 10894 11037 17 1364 -833 N ATOM 2832 CA ILE A 354 -34.680-154.994 293.567 1.00 81.22 C ANISOU 2832 CA ILE A 354 8755 10957 11147 137 1481 -962 C ATOM 2833 C ILE A 354 -35.164-155.693 294.834 1.00 80.41 C ANISOU 2833 C ILE A 354 8581 10790 11180 342 1405 -906 C ATOM 2834 O ILE A 354 -34.785-156.837 295.109 1.00 80.78 O ANISOU 2834 O ILE A 354 8557 10814 11320 445 1432 -982 O ATOM 2835 CB ILE A 354 -33.453-154.099 293.832 1.00 79.41 C ANISOU 2835 CB ILE A 354 8434 10809 10928 91 1544 -1024 C ATOM 2836 CG1 ILE A 354 -32.742-153.774 292.516 1.00 82.21 C ANISOU 2836 CG1 ILE A 354 8856 11232 11148 -145 1705 -1135 C ATOM 2837 CG2 ILE A 354 -32.486-154.764 294.796 1.00 78.03 C ANISOU 2837 CG2 ILE A 354 8063 10644 10941 258 1557 -1117 C ATOM 2838 CD1 ILE A 354 -31.502-152.920 292.682 1.00 84.21 C ANISOU 2838 CD1 ILE A 354 8995 11565 11436 -225 1797 -1215 C ATOM 2839 N CYS A 355 -36.031-155.040 295.608 1.00 81.27 N ANISOU 2839 N CYS A 355 8727 10847 11307 387 1317 -783 N ATOM 2840 CA CYS A 355 -36.413-155.571 296.915 1.00 82.99 C ANISOU 2840 CA CYS A 355 8928 11001 11604 529 1290 -740 C ATOM 2841 C CYS A 355 -37.584-156.551 296.835 1.00 84.71 C ANISOU 2841 C CYS A 355 9180 11136 11871 558 1284 -698 C ATOM 2842 O CYS A 355 -37.472-157.695 297.288 1.00 87.52 O ANISOU 2842 O CYS A 355 9537 11451 12267 635 1290 -721 O ATOM 2843 CB CYS A 355 -36.733-154.418 297.872 1.00 83.18 C ANISOU 2843 CB CYS A 355 8982 10998 11623 543 1262 -669 C ATOM 2844 SG CYS A 355 -35.280-153.437 298.317 1.00 84.63 S ANISOU 2844 SG CYS A 355 9131 11257 11767 524 1239 -713 S ATOM 2845 N TRP A 356 -38.712-156.121 296.266 1.00 84.39 N ANISOU 2845 N TRP A 356 9165 11047 11854 490 1244 -635 N ATOM 2846 CA TRP A 356 -39.895-156.976 296.256 1.00 83.88 C ANISOU 2846 CA TRP A 356 9098 10891 11881 507 1230 -597 C ATOM 2847 C TRP A 356 -39.860-158.018 295.146 1.00 82.35 C ANISOU 2847 C TRP A 356 8946 10693 11649 454 1207 -641 C ATOM 2848 O TRP A 356 -40.454-159.091 295.298 1.00 82.96 O ANISOU 2848 O TRP A 356 9025 10703 11791 487 1209 -635 O ATOM 2849 CB TRP A 356 -41.162-156.132 296.121 1.00 83.58 C ANISOU 2849 CB TRP A 356 9021 10766 11968 466 1162 -526 C ATOM 2850 CG TRP A 356 -41.499-155.361 297.352 1.00 85.59 C ANISOU 2850 CG TRP A 356 9232 10984 12306 526 1238 -513 C ATOM 2851 CD1 TRP A 356 -41.416-154.011 297.520 1.00 88.18 C ANISOU 2851 CD1 TRP A 356 9548 11304 12653 517 1211 -503 C ATOM 2852 CD2 TRP A 356 -41.967-155.893 298.596 1.00 87.45 C ANISOU 2852 CD2 TRP A 356 9465 11167 12593 580 1374 -523 C ATOM 2853 NE1 TRP A 356 -41.808-153.666 298.791 1.00 89.09 N ANISOU 2853 NE1 TRP A 356 9644 11367 12838 571 1337 -525 N ATOM 2854 CE2 TRP A 356 -42.150-154.804 299.472 1.00 89.23 C ANISOU 2854 CE2 TRP A 356 9683 11360 12859 594 1451 -537 C ATOM 2855 CE3 TRP A 356 -42.249-157.184 299.054 1.00 87.13 C ANISOU 2855 CE3 TRP A 356 9463 11091 12553 593 1444 -524 C ATOM 2856 CZ2 TRP A 356 -42.604-154.966 300.779 1.00 90.44 C ANISOU 2856 CZ2 TRP A 356 9886 11453 13026 602 1627 -565 C ATOM 2857 CZ3 TRP A 356 -42.699-157.343 300.351 1.00 87.57 C ANISOU 2857 CZ3 TRP A 356 9574 11083 12617 592 1597 -530 C ATOM 2858 CH2 TRP A 356 -42.874-156.240 301.198 1.00 89.53 C ANISOU 2858 CH2 TRP A 356 9832 11306 12879 587 1703 -557 C ATOM 2859 N GLY A 357 -39.186-157.724 294.036 1.00 80.35 N ANISOU 2859 N GLY A 357 8753 10501 11277 349 1202 -696 N ATOM 2860 CA GLY A 357 -39.182-158.590 292.880 1.00 80.94 C ANISOU 2860 CA GLY A 357 8916 10559 11276 258 1204 -760 C ATOM 2861 C GLY A 357 -38.749-160.012 293.177 1.00 83.67 C ANISOU 2861 C GLY A 357 9225 10889 11676 361 1283 -853 C ATOM 2862 O GLY A 357 -39.543-160.955 293.095 1.00 86.90 O ANISOU 2862 O GLY A 357 9666 11213 12141 374 1238 -829 O ATOM 2863 N PRO A 358 -37.469-160.193 293.520 1.00 81.74 N ANISOU 2863 N PRO A 358 8903 10704 11452 433 1380 -964 N ATOM 2864 CA PRO A 358 -36.976-161.551 293.813 1.00 79.07 C ANISOU 2864 CA PRO A 358 8517 10309 11218 550 1411 -1061 C ATOM 2865 C PRO A 358 -37.757-162.256 294.906 1.00 79.61 C ANISOU 2865 C PRO A 358 8600 10276 11373 656 1322 -952 C ATOM 2866 O PRO A 358 -37.980-163.471 294.821 1.00 79.87 O ANISOU 2866 O PRO A 358 8669 10218 11462 694 1302 -983 O ATOM 2867 CB PRO A 358 -35.518-161.305 294.226 1.00 77.42 C ANISOU 2867 CB PRO A 358 8170 10156 11089 624 1470 -1174 C ATOM 2868 CG PRO A 358 -35.148-160.029 293.550 1.00 77.91 C ANISOU 2868 CG PRO A 358 8243 10329 11031 477 1547 -1194 C ATOM 2869 CD PRO A 358 -36.391-159.191 293.556 1.00 80.57 C ANISOU 2869 CD PRO A 358 8693 10654 11265 402 1445 -1018 C ATOM 2870 N LEU A 359 -38.182-161.519 295.933 1.00 76.17 N ANISOU 2870 N LEU A 359 8160 9842 10939 682 1287 -834 N ATOM 2871 CA LEU A 359 -38.932-162.124 297.028 1.00 72.19 C ANISOU 2871 CA LEU A 359 7710 9238 10480 732 1256 -741 C ATOM 2872 C LEU A 359 -40.234-162.737 296.531 1.00 69.11 C ANISOU 2872 C LEU A 359 7355 8776 10129 664 1251 -695 C ATOM 2873 O LEU A 359 -40.524-163.910 296.796 1.00 70.66 O ANISOU 2873 O LEU A 359 7607 8875 10366 687 1232 -687 O ATOM 2874 CB LEU A 359 -39.211-161.073 298.100 1.00 70.48 C ANISOU 2874 CB LEU A 359 7507 9037 10235 729 1277 -658 C ATOM 2875 CG LEU A 359 -39.809-161.590 299.403 1.00 71.40 C ANISOU 2875 CG LEU A 359 7731 9049 10347 738 1298 -583 C ATOM 2876 CD1 LEU A 359 -38.706-162.061 300.339 1.00 72.14 C ANISOU 2876 CD1 LEU A 359 7917 9094 10399 811 1202 -587 C ATOM 2877 CD2 LEU A 359 -40.661-160.510 300.045 1.00 70.99 C ANISOU 2877 CD2 LEU A 359 7681 9001 10293 682 1399 -534 C ATOM 2878 N LEU A 360 -41.033-161.953 295.803 1.00 66.43 N ANISOU 2878 N LEU A 360 6986 8459 9795 572 1234 -659 N ATOM 2879 CA LEU A 360 -42.319-162.445 295.319 1.00 64.77 C ANISOU 2879 CA LEU A 360 6777 8160 9673 499 1183 -611 C ATOM 2880 C LEU A 360 -42.143-163.620 294.367 1.00 67.25 C ANISOU 2880 C LEU A 360 7171 8434 9948 468 1141 -680 C ATOM 2881 O LEU A 360 -42.925-164.576 294.402 1.00 68.98 O ANISOU 2881 O LEU A 360 7412 8553 10243 447 1111 -652 O ATOM 2882 CB LEU A 360 -43.088-161.316 294.636 1.00 61.29 C ANISOU 2882 CB LEU A 360 6287 7716 9284 412 1095 -560 C ATOM 2883 CG LEU A 360 -43.575-160.188 295.545 1.00 61.48 C ANISOU 2883 CG LEU A 360 6210 7733 9417 442 1141 -509 C ATOM 2884 CD1 LEU A 360 -44.308-159.132 294.740 1.00 65.00 C ANISOU 2884 CD1 LEU A 360 6600 8130 9968 368 990 -463 C ATOM 2885 CD2 LEU A 360 -44.466-160.745 296.646 1.00 60.04 C ANISOU 2885 CD2 LEU A 360 5970 7467 9375 464 1255 -486 C ATOM 2886 N ALA A 361 -41.118-163.566 293.512 1.00 66.67 N ANISOU 2886 N ALA A 361 7143 8427 9760 448 1164 -786 N ATOM 2887 CA ALA A 361 -40.913-164.624 292.528 1.00 67.63 C ANISOU 2887 CA ALA A 361 7360 8500 9834 402 1165 -891 C ATOM 2888 C ALA A 361 -40.727-165.979 293.199 1.00 69.31 C ANISOU 2888 C ALA A 361 7572 8619 10143 516 1177 -927 C ATOM 2889 O ALA A 361 -41.313-166.979 292.767 1.00 71.02 O ANISOU 2889 O ALA A 361 7865 8734 10385 475 1130 -938 O ATOM 2890 CB ALA A 361 -39.710-164.293 291.646 1.00 68.45 C ANISOU 2890 CB ALA A 361 7503 8692 9812 349 1268 -1042 C ATOM 2891 N ILE A 362 -39.919-166.031 294.261 1.00 68.38 N ANISOU 2891 N ILE A 362 7392 8508 10082 647 1204 -936 N ATOM 2892 CA ILE A 362 -39.712-167.286 294.978 1.00 68.84 C ANISOU 2892 CA ILE A 362 7487 8436 10234 748 1156 -945 C ATOM 2893 C ILE A 362 -41.025-167.786 295.564 1.00 68.94 C ANISOU 2893 C ILE A 362 7571 8350 10272 691 1113 -805 C ATOM 2894 O ILE A 362 -41.303-168.992 295.570 1.00 69.84 O ANISOU 2894 O ILE A 362 7766 8335 10437 695 1063 -811 O ATOM 2895 CB ILE A 362 -38.637-167.111 296.066 1.00 68.64 C ANISOU 2895 CB ILE A 362 7411 8408 10262 877 1120 -951 C ATOM 2896 CG1 ILE A 362 -37.300-166.706 295.441 1.00 68.97 C ANISOU 2896 CG1 ILE A 362 7326 8533 10345 925 1182 -1121 C ATOM 2897 CG2 ILE A 362 -38.475-168.390 296.865 1.00 68.77 C ANISOU 2897 CG2 ILE A 362 7513 8245 10372 965 1001 -929 C ATOM 2898 CD1 ILE A 362 -36.194-166.492 296.455 1.00 68.53 C ANISOU 2898 CD1 ILE A 362 7186 8457 10394 1050 1098 -1133 C ATOM 2899 N MET A 363 -41.854-166.871 296.069 1.00 69.25 N ANISOU 2899 N MET A 363 7573 8438 10302 629 1149 -694 N ATOM 2900 CA MET A 363 -43.162-167.268 296.577 1.00 71.81 C ANISOU 2900 CA MET A 363 7921 8669 10695 547 1165 -593 C ATOM 2901 C MET A 363 -44.038-167.820 295.461 1.00 71.50 C ANISOU 2901 C MET A 363 7876 8573 10717 452 1100 -605 C ATOM 2902 O MET A 363 -44.725-168.830 295.647 1.00 70.24 O ANISOU 2902 O MET A 363 7769 8295 10624 402 1081 -571 O ATOM 2903 CB MET A 363 -43.841-166.083 297.258 1.00 76.45 C ANISOU 2903 CB MET A 363 8424 9309 11315 503 1255 -522 C ATOM 2904 CG MET A 363 -43.134-165.596 298.509 1.00 81.47 C ANISOU 2904 CG MET A 363 9122 9972 11861 561 1316 -499 C ATOM 2905 SD MET A 363 -43.734-163.970 299.004 1.00 85.98 S ANISOU 2905 SD MET A 363 9584 10615 12469 521 1437 -472 S ATOM 2906 CE MET A 363 -42.937-163.769 300.594 1.00 87.12 C ANISOU 2906 CE MET A 363 9902 10746 12454 549 1496 -445 C ATOM 2907 N VAL A 364 -44.023-167.168 294.294 1.00 74.33 N ANISOU 2907 N VAL A 364 8204 8999 11040 401 1046 -647 N ATOM 2908 CA VAL A 364 -44.751-167.678 293.133 1.00 78.04 C ANISOU 2908 CA VAL A 364 8725 9396 11529 288 932 -660 C ATOM 2909 C VAL A 364 -44.341-169.115 292.842 1.00 81.91 C ANISOU 2909 C VAL A 364 9341 9794 11988 311 922 -745 C ATOM 2910 O VAL A 364 -45.186-169.979 292.575 1.00 82.51 O ANISOU 2910 O VAL A 364 9464 9752 12134 234 846 -718 O ATOM 2911 CB VAL A 364 -44.517-166.765 291.915 1.00 76.34 C ANISOU 2911 CB VAL A 364 8553 9252 11200 203 858 -696 C ATOM 2912 CG1 VAL A 364 -45.157-167.357 290.672 1.00 77.48 C ANISOU 2912 CG1 VAL A 364 8828 9299 11311 58 706 -713 C ATOM 2913 CG2 VAL A 364 -45.057-165.369 292.185 1.00 74.17 C ANISOU 2913 CG2 VAL A 364 8154 9022 11004 183 819 -602 C ATOM 2914 N TYR A 365 -43.034-169.388 292.894 1.00 84.64 N ANISOU 2914 N TYR A 365 9722 10171 12265 420 991 -861 N ATOM 2915 CA TYR A 365 -42.523-170.751 292.782 1.00 89.31 C ANISOU 2915 CA TYR A 365 10404 10643 12888 483 981 -964 C ATOM 2916 C TYR A 365 -43.220-171.685 293.762 1.00 86.83 C ANISOU 2916 C TYR A 365 10132 10188 12672 492 925 -854 C ATOM 2917 O TYR A 365 -43.778-172.717 293.373 1.00 87.25 O ANISOU 2917 O TYR A 365 10277 10111 12764 431 861 -863 O ATOM 2918 CB TYR A 365 -41.018-170.760 293.047 1.00 97.61 C ANISOU 2918 CB TYR A 365 11404 11727 13957 633 1049 -1097 C ATOM 2919 CG TYR A 365 -40.136-170.515 291.852 1.00106.58 C ANISOU 2919 CG TYR A 365 12541 12935 15021 605 1156 -1295 C ATOM 2920 CD1 TYR A 365 -40.395-169.480 290.965 1.00109.20 C ANISOU 2920 CD1 TYR A 365 12909 13387 15197 456 1196 -1288 C ATOM 2921 CD2 TYR A 365 -39.018-171.305 291.631 1.00113.05 C ANISOU 2921 CD2 TYR A 365 13331 13681 15942 714 1224 -1501 C ATOM 2922 CE1 TYR A 365 -39.572-169.256 289.875 1.00113.19 C ANISOU 2922 CE1 TYR A 365 13469 13950 15587 377 1333 -1476 C ATOM 2923 CE2 TYR A 365 -38.193-171.089 290.552 1.00117.22 C ANISOU 2923 CE2 TYR A 365 13856 14271 16412 659 1395 -1721 C ATOM 2924 CZ TYR A 365 -38.472-170.065 289.677 1.00117.95 C ANISOU 2924 CZ TYR A 365 14032 14497 16287 472 1466 -1705 C ATOM 2925 OH TYR A 365 -37.645-169.851 288.599 1.00121.88 O ANISOU 2925 OH TYR A 365 14579 15049 16680 365 1673 -1930 O ATOM 2926 N ASP A 366 -43.181-171.331 295.050 1.00 85.89 N ANISOU 2926 N ASP A 366 9982 10081 12572 541 956 -750 N ATOM 2927 CA ASP A 366 -43.738-172.194 296.087 1.00 87.15 C ANISOU 2927 CA ASP A 366 10242 10096 12775 509 931 -644 C ATOM 2928 C ASP A 366 -45.202-172.512 295.818 1.00 89.38 C ANISOU 2928 C ASP A 366 10515 10318 13129 347 937 -570 C ATOM 2929 O ASP A 366 -45.663-173.626 296.092 1.00 93.13 O ANISOU 2929 O ASP A 366 11101 10639 13646 288 896 -531 O ATOM 2930 CB ASP A 366 -43.574-171.530 297.453 1.00 85.80 C ANISOU 2930 CB ASP A 366 10088 9960 12554 527 991 -546 C ATOM 2931 CG ASP A 366 -44.090-172.391 298.583 1.00 89.33 C ANISOU 2931 CG ASP A 366 10712 10244 12984 444 986 -434 C ATOM 2932 OD1 ASP A 366 -43.959-173.630 298.494 1.00 93.53 O ANISOU 2932 OD1 ASP A 366 11374 10614 13549 456 872 -442 O ATOM 2933 OD2 ASP A 366 -44.627-171.827 299.559 1.00 89.51 O ANISOU 2933 OD2 ASP A 366 10768 10289 12954 351 1108 -346 O ATOM 2934 N VAL A 367 -45.946-171.547 295.273 1.00 88.59 N ANISOU 2934 N VAL A 367 10274 10315 13072 268 962 -550 N ATOM 2935 CA VAL A 367 -47.356-171.775 294.970 1.00 91.75 C ANISOU 2935 CA VAL A 367 10605 10640 13617 118 931 -492 C ATOM 2936 C VAL A 367 -47.507-172.881 293.933 1.00 93.72 C ANISOU 2936 C VAL A 367 10965 10776 13868 65 791 -547 C ATOM 2937 O VAL A 367 -48.362-173.765 294.066 1.00 93.80 O ANISOU 2937 O VAL A 367 11004 10653 13982 -39 758 -500 O ATOM 2938 CB VAL A 367 -48.021-170.466 294.503 1.00 91.32 C ANISOU 2938 CB VAL A 367 10363 10674 13660 68 912 -469 C ATOM 2939 CG1 VAL A 367 -49.513-170.670 294.297 1.00 92.51 C ANISOU 2939 CG1 VAL A 367 10378 10717 14052 -79 855 -415 C ATOM 2940 CG2 VAL A 367 -47.775-169.353 295.502 1.00 90.56 C ANISOU 2940 CG2 VAL A 367 10175 10679 13554 129 1062 -441 C ATOM 2941 N PHE A 368 -46.669-172.862 292.897 1.00 97.23 N ANISOU 2941 N PHE A 368 11489 11263 14191 116 729 -661 N ATOM 2942 CA PHE A 368 -46.826-173.750 291.750 1.00101.29 C ANISOU 2942 CA PHE A 368 12140 11674 14673 38 612 -742 C ATOM 2943 C PHE A 368 -45.932-174.982 291.835 1.00104.89 C ANISOU 2943 C PHE A 368 12743 12018 15093 139 629 -853 C ATOM 2944 O PHE A 368 -46.417-176.112 291.722 1.00104.81 O ANISOU 2944 O PHE A 368 12837 11847 15139 79 551 -851 O ATOM 2945 CB PHE A 368 -46.528-173.003 290.437 1.00102.29 C ANISOU 2945 CB PHE A 368 12320 11884 14660 -24 556 -825 C ATOM 2946 CG PHE A 368 -47.511-171.901 290.098 1.00103.91 C ANISOU 2946 CG PHE A 368 12414 12132 14933 -141 437 -714 C ATOM 2947 CD1 PHE A 368 -47.707-171.526 288.779 1.00106.22 C ANISOU 2947 CD1 PHE A 368 12838 12410 15110 -283 275 -740 C ATOM 2948 CD2 PHE A 368 -48.210-171.223 291.082 1.00104.97 C ANISOU 2948 CD2 PHE A 368 12334 12297 15252 -120 480 -595 C ATOM 2949 CE1 PHE A 368 -48.593-170.514 288.452 1.00107.64 C ANISOU 2949 CE1 PHE A 368 12922 12583 15392 -383 93 -628 C ATOM 2950 CE2 PHE A 368 -49.093-170.210 290.764 1.00106.04 C ANISOU 2950 CE2 PHE A 368 12330 12436 15526 -203 352 -516 C ATOM 2951 CZ PHE A 368 -49.285-169.856 289.447 1.00107.72 C ANISOU 2951 CZ PHE A 368 12660 12614 15657 -324 126 -522 C ATOM 2952 N GLY A 369 -44.632-174.787 292.033 1.00108.91 N ANISOU 2952 N GLY A 369 13243 12589 15548 293 714 -957 N ATOM 2953 CA GLY A 369 -43.656-175.847 291.925 1.00112.58 C ANISOU 2953 CA GLY A 369 13802 12930 16045 413 714 -1110 C ATOM 2954 C GLY A 369 -43.226-176.414 293.263 1.00117.52 C ANISOU 2954 C GLY A 369 14436 13445 16771 541 670 -1039 C ATOM 2955 O GLY A 369 -43.879-176.229 294.294 1.00117.70 O ANISOU 2955 O GLY A 369 14458 13463 16799 488 659 -861 O ATOM 2956 N LYS A 370 -42.101-177.126 293.234 1.00120.56 N ANISOU 2956 N LYS A 370 14844 13716 17246 698 642 -1192 N ATOM 2957 CA LYS A 370 -41.538-177.786 294.402 1.00125.12 C ANISOU 2957 CA LYS A 370 15472 14128 17942 827 516 -1135 C ATOM 2958 C LYS A 370 -40.321-177.011 294.887 1.00123.89 C ANISOU 2958 C LYS A 370 15171 14063 17838 985 533 -1191 C ATOM 2959 O LYS A 370 -39.568-176.453 294.081 1.00124.40 O ANISOU 2959 O LYS A 370 15096 14251 17921 1040 657 -1372 O ATOM 2960 CB LYS A 370 -41.142-179.229 294.074 1.00128.19 C ANISOU 2960 CB LYS A 370 15968 14259 18482 911 403 -1271 C ATOM 2961 CG LYS A 370 -41.825-179.790 292.832 1.00129.98 C ANISOU 2961 CG LYS A 370 16281 14447 18657 785 452 -1375 C ATOM 2962 CD LYS A 370 -41.137-181.056 292.338 1.00131.30 C ANISOU 2962 CD LYS A 370 16523 14371 18994 903 391 -1593 C ATOM 2963 CE LYS A 370 -41.570-181.406 290.920 1.00132.70 C ANISOU 2963 CE LYS A 370 16801 14541 19077 772 485 -1759 C ATOM 2964 NZ LYS A 370 -40.739-182.494 290.329 1.00135.11 N ANISOU 2964 NZ LYS A 370 17156 14624 19557 898 499 -2043 N ATOM 2965 N MET A 371 -40.129-176.979 296.202 1.00119.40 N ANISOU 2965 N MET A 371 14660 13422 17283 1030 407 -1038 N ATOM 2966 CA MET A 371 -39.049-176.225 296.824 1.00114.36 C ANISOU 2966 CA MET A 371 13905 12848 16697 1161 369 -1056 C ATOM 2967 C MET A 371 -37.988-177.179 297.354 1.00110.59 C ANISOU 2967 C MET A 371 13454 12111 16456 1342 125 -1122 C ATOM 2968 O MET A 371 -38.299-178.097 298.119 1.00111.55 O ANISOU 2968 O MET A 371 13794 12003 16589 1318 -76 -988 O ATOM 2969 CB MET A 371 -39.578-175.350 297.963 1.00115.67 C ANISOU 2969 CB MET A 371 14149 13111 16689 1058 380 -836 C ATOM 2970 CG MET A 371 -40.449-174.181 297.528 1.00117.55 C ANISOU 2970 CG MET A 371 14293 13594 16776 922 595 -792 C ATOM 2971 SD MET A 371 -39.499-172.744 296.998 1.00119.10 S ANISOU 2971 SD MET A 371 14259 14029 16963 1001 712 -915 S ATOM 2972 CE MET A 371 -39.419-173.016 295.232 1.00119.88 C ANISOU 2972 CE MET A 371 14277 14180 17093 979 828 -1129 C ATOM 2973 N ASN A 372 -36.741-176.957 296.949 1.00107.67 N ANISOU 2973 N ASN A 372 12858 11755 16296 1512 133 -1332 N ATOM 2974 CA ASN A 372 -35.609-177.691 297.488 1.00108.73 C ANISOU 2974 CA ASN A 372 12938 11628 16745 1714 -136 -1414 C ATOM 2975 C ASN A 372 -34.929-176.851 298.567 1.00107.20 C ANISOU 2975 C ASN A 372 12701 11469 16561 1766 -296 -1297 C ATOM 2976 O ASN A 372 -35.305-175.706 298.831 1.00105.20 O ANISOU 2976 O ASN A 372 12454 11452 16066 1651 -157 -1180 O ATOM 2977 CB ASN A 372 -34.636-178.081 296.371 1.00110.62 C ANISOU 2977 CB ASN A 372 12917 11818 17295 1870 -15 -1763 C ATOM 2978 CG ASN A 372 -33.928-176.886 295.762 1.00109.45 C ANISOU 2978 CG ASN A 372 12496 11933 17157 1877 243 -1931 C ATOM 2979 OD1 ASN A 372 -34.344-175.743 295.942 1.00106.25 O ANISOU 2979 OD1 ASN A 372 12111 11772 16488 1752 354 -1786 O ATOM 2980 ND2 ASN A 372 -32.854-177.148 295.027 1.00111.78 N ANISOU 2980 ND2 ASN A 372 12531 12164 17774 2013 358 -2255 N ATOM 2981 N LYS A 373 -33.908-177.434 299.201 1.00107.39 N ANISOU 2981 N LYS A 373 12684 11228 16892 1943 -625 -1333 N ATOM 2982 CA LYS A 373 -33.232-176.752 300.300 1.00103.28 C ANISOU 2982 CA LYS A 373 12167 10685 16391 1981 -862 -1207 C ATOM 2983 C LYS A 373 -32.528-175.483 299.838 1.00 98.15 C ANISOU 2983 C LYS A 373 11193 10307 15792 2019 -642 -1355 C ATOM 2984 O LYS A 373 -32.480-174.499 300.587 1.00 97.86 O ANISOU 2984 O LYS A 373 11211 10391 15578 1949 -685 -1207 O ATOM 2985 CB LYS A 373 -32.236-177.700 300.970 1.00107.89 C ANISOU 2985 CB LYS A 373 12753 10879 17359 2171 -1330 -1228 C ATOM 2986 CG LYS A 373 -31.148-177.011 301.788 1.00110.04 C ANISOU 2986 CG LYS A 373 12901 11103 17807 2268 -1609 -1199 C ATOM 2987 CD LYS A 373 -30.363-178.016 302.614 1.00114.65 C ANISOU 2987 CD LYS A 373 13576 11239 18747 2423 -2181 -1150 C ATOM 2988 CE LYS A 373 -29.044-177.446 303.110 1.00117.52 C ANISOU 2988 CE LYS A 373 13674 11517 19461 2575 -2482 -1217 C ATOM 2989 NZ LYS A 373 -28.002-177.457 302.047 1.00118.60 N ANISOU 2989 NZ LYS A 373 13240 11680 20143 2800 -2305 -1606 N ATOM 2990 N LEU A 374 -31.990-175.475 298.616 1.00 95.03 N ANISOU 2990 N LEU A 374 10490 10003 15615 2101 -387 -1652 N ATOM 2991 CA LEU A 374 -31.268-174.302 298.134 1.00 91.95 C ANISOU 2991 CA LEU A 374 9806 9856 15276 2106 -160 -1805 C ATOM 2992 C LEU A 374 -32.176-173.080 298.071 1.00 88.18 C ANISOU 2992 C LEU A 374 9455 9691 14357 1900 79 -1638 C ATOM 2993 O LEU A 374 -31.805-171.992 298.524 1.00 86.55 O ANISOU 2993 O LEU A 374 9175 9624 14084 1874 75 -1576 O ATOM 2994 CB LEU A 374 -30.662-174.580 296.759 1.00 91.91 C ANISOU 2994 CB LEU A 374 9515 9885 15520 2168 142 -2167 C ATOM 2995 CG LEU A 374 -29.842-173.402 296.231 1.00 90.81 C ANISOU 2995 CG LEU A 374 9081 9981 15440 2138 405 -2343 C ATOM 2996 CD1 LEU A 374 -28.447-173.411 296.839 1.00 94.54 C ANISOU 2996 CD1 LEU A 374 9235 10286 16400 2335 164 -2471 C ATOM 2997 CD2 LEU A 374 -29.784-173.390 294.711 1.00 88.98 C ANISOU 2997 CD2 LEU A 374 8741 9885 15181 2045 847 -2637 C ATOM 2998 N ILE A 375 -33.377-173.245 297.513 1.00 86.44 N ANISOU 2998 N ILE A 375 9417 9560 13864 1755 263 -1569 N ATOM 2999 CA ILE A 375 -34.260-172.101 297.314 1.00 80.30 C ANISOU 2999 CA ILE A 375 8715 9049 12748 1575 475 -1442 C ATOM 3000 C ILE A 375 -34.791-171.590 298.648 1.00 77.70 C ANISOU 3000 C ILE A 375 8580 8719 12223 1507 326 -1173 C ATOM 3001 O ILE A 375 -34.854-170.375 298.877 1.00 75.07 O ANISOU 3001 O ILE A 375 8214 8569 11741 1437 419 -1106 O ATOM 3002 CB ILE A 375 -35.399-172.465 296.346 1.00 79.68 C ANISOU 3002 CB ILE A 375 8756 9024 12495 1440 655 -1447 C ATOM 3003 CG1 ILE A 375 -34.827-172.843 294.979 1.00 82.84 C ANISOU 3003 CG1 ILE A 375 9017 9434 13025 1463 845 -1737 C ATOM 3004 CG2 ILE A 375 -36.349-171.297 296.191 1.00 76.32 C ANISOU 3004 CG2 ILE A 375 8386 8822 11790 1269 807 -1309 C ATOM 3005 CD1 ILE A 375 -35.878-173.231 293.963 1.00 83.40 C ANISOU 3005 CD1 ILE A 375 9245 9530 12912 1312 977 -1750 C ATOM 3006 N LYS A 376 -35.194-172.501 299.541 1.00 78.12 N ANISOU 3006 N LYS A 376 8869 8556 12257 1502 108 -1022 N ATOM 3007 CA LYS A 376 -35.540-172.109 300.905 1.00 78.73 C ANISOU 3007 CA LYS A 376 9185 8593 12137 1412 -28 -793 C ATOM 3008 C LYS A 376 -34.453-171.228 301.503 1.00 78.74 C ANISOU 3008 C LYS A 376 9079 8631 12208 1488 -161 -804 C ATOM 3009 O LYS A 376 -34.733-170.183 302.100 1.00 76.88 O ANISOU 3009 O LYS A 376 8925 8526 11758 1386 -90 -694 O ATOM 3010 CB LYS A 376 -35.738-173.344 301.784 1.00 82.79 C ANISOU 3010 CB LYS A 376 9993 8808 12658 1398 -304 -658 C ATOM 3011 CG LYS A 376 -36.917-174.233 301.451 1.00 86.00 C ANISOU 3011 CG LYS A 376 10560 9149 12968 1282 -199 -604 C ATOM 3012 CD LYS A 376 -36.994-175.345 302.488 1.00 90.77 C ANISOU 3012 CD LYS A 376 11504 9437 13548 1238 -500 -445 C ATOM 3013 CE LYS A 376 -38.232-176.207 302.335 1.00 93.18 C ANISOU 3013 CE LYS A 376 12003 9664 13735 1079 -394 -364 C ATOM 3014 NZ LYS A 376 -38.368-177.147 303.485 1.00 97.01 N ANISOU 3014 NZ LYS A 376 12892 9844 14125 974 -670 -175 N ATOM 3015 N THR A 377 -33.196-171.647 301.340 1.00 81.90 N ANISOU 3015 N THR A 377 9275 8898 12945 1668 -357 -957 N ATOM 3016 CA THR A 377 -32.068-170.891 301.872 1.00 81.94 C ANISOU 3016 CA THR A 377 9134 8909 13092 1747 -527 -985 C ATOM 3017 C THR A 377 -31.986-169.507 301.240 1.00 77.24 C ANISOU 3017 C THR A 377 8329 8623 12396 1686 -220 -1068 C ATOM 3018 O THR A 377 -31.802-168.503 301.939 1.00 74.74 O ANISOU 3018 O THR A 377 8060 8389 11948 1630 -270 -971 O ATOM 3019 CB THR A 377 -30.773-171.670 301.637 1.00 86.29 C ANISOU 3019 CB THR A 377 9416 9243 14125 1963 -765 -1181 C ATOM 3020 OG1 THR A 377 -30.843-172.930 302.316 1.00 88.90 O ANISOU 3020 OG1 THR A 377 9981 9241 14554 2019 -1122 -1076 O ATOM 3021 CG2 THR A 377 -29.575-170.886 302.143 1.00 88.34 C ANISOU 3021 CG2 THR A 377 9470 9497 14596 2042 -961 -1225 C ATOM 3022 N VAL A 378 -32.115-169.438 299.913 1.00 75.08 N ANISOU 3022 N VAL A 378 7860 8505 12163 1676 86 -1246 N ATOM 3023 CA VAL A 378 -32.109-168.148 299.228 1.00 72.36 C ANISOU 3023 CA VAL A 378 7373 8432 11689 1583 364 -1308 C ATOM 3024 C VAL A 378 -33.201-167.248 299.784 1.00 71.14 C ANISOU 3024 C VAL A 378 7441 8405 11186 1432 436 -1093 C ATOM 3025 O VAL A 378 -32.986-166.050 300.010 1.00 72.16 O ANISOU 3025 O VAL A 378 7524 8672 11222 1381 488 -1061 O ATOM 3026 CB VAL A 378 -32.267-168.346 297.709 1.00 72.15 C ANISOU 3026 CB VAL A 378 7222 8512 11680 1539 661 -1505 C ATOM 3027 CG1 VAL A 378 -32.411-167.001 297.010 1.00 70.92 C ANISOU 3027 CG1 VAL A 378 7008 8610 11329 1397 912 -1525 C ATOM 3028 CG2 VAL A 378 -31.086-169.114 297.149 1.00 77.04 C ANISOU 3028 CG2 VAL A 378 7583 9008 12679 1681 663 -1777 C ATOM 3029 N PHE A 379 -34.385-167.812 300.026 1.00 69.70 N ANISOU 3029 N PHE A 379 7486 8161 10837 1355 451 -959 N ATOM 3030 CA PHE A 379 -35.499-167.001 300.498 1.00 68.57 C ANISOU 3030 CA PHE A 379 7504 8121 10429 1211 570 -799 C ATOM 3031 C PHE A 379 -35.185-166.345 301.834 1.00 69.83 C ANISOU 3031 C PHE A 379 7804 8243 10484 1188 431 -678 C ATOM 3032 O PHE A 379 -35.502-165.168 302.043 1.00 69.08 O ANISOU 3032 O PHE A 379 7717 8284 10245 1109 556 -634 O ATOM 3033 CB PHE A 379 -36.762-167.847 300.612 1.00 65.44 C ANISOU 3033 CB PHE A 379 7298 7633 9935 1123 612 -698 C ATOM 3034 CG PHE A 379 -37.972-167.047 300.960 1.00 60.30 C ANISOU 3034 CG PHE A 379 6739 7076 9097 977 784 -584 C ATOM 3035 CD1 PHE A 379 -38.671-166.378 299.973 1.00 57.35 C ANISOU 3035 CD1 PHE A 379 6229 6851 8710 916 963 -623 C ATOM 3036 CD2 PHE A 379 -38.391-166.931 302.274 1.00 59.37 C ANISOU 3036 CD2 PHE A 379 6851 6876 8829 888 763 -450 C ATOM 3037 CE1 PHE A 379 -39.778-165.624 300.285 1.00 68.39 C ANISOU 3037 CE1 PHE A 379 7656 8303 10024 805 1101 -542 C ATOM 3038 CE2 PHE A 379 -39.498-166.177 302.592 1.00 58.60 C ANISOU 3038 CE2 PHE A 379 6797 6852 8616 756 972 -392 C ATOM 3039 CZ PHE A 379 -40.191-165.525 301.597 1.00 69.59 C ANISOU 3039 CZ PHE A 379 7988 8381 10071 733 1133 -443 C ATOM 3040 N ALA A 380 -34.575-167.094 302.756 1.00 72.12 N ANISOU 3040 N ALA A 380 8237 8324 10841 1247 148 -622 N ATOM 3041 CA ALA A 380 -34.197-166.515 304.042 1.00 73.01 C ANISOU 3041 CA ALA A 380 8545 8371 10826 1200 -33 -505 C ATOM 3042 C ALA A 380 -33.297-165.302 303.853 1.00 73.43 C ANISOU 3042 C ALA A 380 8373 8573 10954 1244 -20 -589 C ATOM 3043 O ALA A 380 -33.474-164.276 304.521 1.00 74.04 O ANISOU 3043 O ALA A 380 8575 8721 10837 1149 23 -513 O ATOM 3044 CB ALA A 380 -33.509-167.565 304.911 1.00 73.40 C ANISOU 3044 CB ALA A 380 8780 8132 10978 1260 -428 -436 C ATOM 3045 N PHE A 381 -32.333-165.395 302.935 1.00 72.76 N ANISOU 3045 N PHE A 381 7960 8531 11154 1371 -29 -764 N ATOM 3046 CA PHE A 381 -31.482-164.246 302.651 1.00 72.86 C ANISOU 3046 CA PHE A 381 7741 8692 11250 1383 22 -858 C ATOM 3047 C PHE A 381 -32.236-163.181 301.866 1.00 72.04 C ANISOU 3047 C PHE A 381 7588 8828 10957 1270 356 -872 C ATOM 3048 O PHE A 381 -32.011-161.982 302.065 1.00 75.12 O ANISOU 3048 O PHE A 381 7950 9328 11262 1213 398 -855 O ATOM 3049 CB PHE A 381 -30.229-164.695 301.903 1.00 75.28 C ANISOU 3049 CB PHE A 381 7698 8960 11947 1523 -36 -1072 C ATOM 3050 CG PHE A 381 -29.209-165.354 302.784 1.00 79.51 C ANISOU 3050 CG PHE A 381 8208 9243 12759 1649 -448 -1067 C ATOM 3051 CD1 PHE A 381 -29.266-166.715 303.038 1.00 82.30 C ANISOU 3051 CD1 PHE A 381 8665 9353 13254 1741 -670 -1045 C ATOM 3052 CD2 PHE A 381 -28.199-164.610 303.370 1.00 81.35 C ANISOU 3052 CD2 PHE A 381 8326 9455 13129 1669 -657 -1075 C ATOM 3053 CE1 PHE A 381 -28.330-167.321 303.854 1.00 85.97 C ANISOU 3053 CE1 PHE A 381 9122 9540 14004 1859 -1122 -1026 C ATOM 3054 CE2 PHE A 381 -27.260-165.209 304.186 1.00 85.20 C ANISOU 3054 CE2 PHE A 381 8790 9674 13909 1783 -1110 -1060 C ATOM 3055 CZ PHE A 381 -27.326-166.567 304.429 1.00 87.01 C ANISOU 3055 CZ PHE A 381 9128 9644 14290 1882 -1358 -1032 C ATOM 3056 N CYS A 382 -33.140-163.593 300.974 1.00 71.39 N ANISOU 3056 N CYS A 382 7508 8801 10816 1232 557 -896 N ATOM 3057 CA CYS A 382 -33.943-162.611 300.252 1.00 70.90 C ANISOU 3057 CA CYS A 382 7428 8916 10593 1119 797 -885 C ATOM 3058 C CYS A 382 -34.958-161.936 301.165 1.00 71.36 C ANISOU 3058 C CYS A 382 7691 8978 10443 1029 831 -729 C ATOM 3059 O CYS A 382 -35.312-160.775 300.937 1.00 73.54 O ANISOU 3059 O CYS A 382 7937 9372 10632 958 952 -714 O ATOM 3060 CB CYS A 382 -34.646-163.264 299.063 1.00 72.38 C ANISOU 3060 CB CYS A 382 7587 9128 10784 1086 944 -946 C ATOM 3061 SG CYS A 382 -33.592-163.463 297.607 1.00 75.96 S ANISOU 3061 SG CYS A 382 7808 9653 11401 1104 1070 -1186 S ATOM 3062 N SER A 383 -35.440-162.638 302.195 1.00 70.69 N ANISOU 3062 N SER A 383 7827 8750 10283 1015 740 -623 N ATOM 3063 CA SER A 383 -36.308-161.994 303.175 1.00 72.94 C ANISOU 3063 CA SER A 383 8317 9022 10373 906 825 -514 C ATOM 3064 C SER A 383 -35.627-160.790 303.807 1.00 76.68 C ANISOU 3064 C SER A 383 8813 9546 10778 891 771 -508 C ATOM 3065 O SER A 383 -36.295-159.812 304.164 1.00 74.28 O ANISOU 3065 O SER A 383 8578 9291 10352 808 919 -479 O ATOM 3066 CB SER A 383 -36.726-162.995 304.253 1.00 75.32 C ANISOU 3066 CB SER A 383 8909 9141 10570 851 737 -412 C ATOM 3067 OG SER A 383 -37.598-163.976 303.725 1.00 76.20 O ANISOU 3067 OG SER A 383 9017 9208 10728 831 826 -407 O ATOM 3068 N MET A 384 -34.300-160.840 303.943 1.00 80.80 N ANISOU 3068 N MET A 384 9254 10036 11409 971 554 -550 N ATOM 3069 CA MET A 384 -33.545-159.705 304.457 1.00 78.35 C ANISOU 3069 CA MET A 384 8940 9768 11061 952 472 -551 C ATOM 3070 C MET A 384 -33.654-158.482 303.558 1.00 74.38 C ANISOU 3070 C MET A 384 8244 9449 10567 919 669 -616 C ATOM 3071 O MET A 384 -33.462-157.358 304.036 1.00 68.04 O ANISOU 3071 O MET A 384 7492 8684 9676 867 667 -598 O ATOM 3072 CB MET A 384 -32.075-160.085 304.616 1.00 79.89 C ANISOU 3072 CB MET A 384 9008 9880 11466 1052 182 -604 C ATOM 3073 CG MET A 384 -31.448-159.585 305.896 1.00 84.41 C ANISOU 3073 CG MET A 384 9781 10344 11945 1009 -73 -525 C ATOM 3074 SD MET A 384 -31.670-160.778 307.225 1.00 89.41 S ANISOU 3074 SD MET A 384 10836 10702 12436 967 -359 -376 S ATOM 3075 CE MET A 384 -30.569-162.078 306.671 1.00 91.59 C ANISOU 3075 CE MET A 384 10837 10836 13128 1158 -656 -463 C ATOM 3076 N LEU A 385 -33.946-158.675 302.268 1.00 77.27 N ANISOU 3076 N LEU A 385 8430 9909 11021 931 816 -687 N ATOM 3077 CA LEU A 385 -34.042-157.546 301.347 1.00 82.05 C ANISOU 3077 CA LEU A 385 8908 10657 11610 868 960 -730 C ATOM 3078 C LEU A 385 -35.125-156.562 301.766 1.00 88.91 C ANISOU 3078 C LEU A 385 9901 11534 12346 795 1064 -652 C ATOM 3079 O LEU A 385 -35.039-155.373 301.440 1.00 92.57 O ANISOU 3079 O LEU A 385 10315 12070 12786 744 1107 -662 O ATOM 3080 CB LEU A 385 -34.311-158.043 299.925 1.00 81.57 C ANISOU 3080 CB LEU A 385 8726 10657 11611 853 1077 -803 C ATOM 3081 CG LEU A 385 -33.118-158.238 298.986 1.00 83.63 C ANISOU 3081 CG LEU A 385 8793 10980 12003 863 1104 -953 C ATOM 3082 CD1 LEU A 385 -32.530-156.892 298.595 1.00 83.45 C ANISOU 3082 CD1 LEU A 385 8694 11070 11943 767 1163 -987 C ATOM 3083 CD2 LEU A 385 -32.059-159.132 299.611 1.00 87.08 C ANISOU 3083 CD2 LEU A 385 9141 11316 12629 984 945 -1018 C ATOM 3084 N CYS A 386 -36.150-157.032 302.481 1.00 93.14 N ANISOU 3084 N CYS A 386 10593 11979 12816 779 1118 -588 N ATOM 3085 CA CYS A 386 -37.231-156.140 302.887 1.00 96.26 C ANISOU 3085 CA CYS A 386 11061 12359 13155 714 1261 -557 C ATOM 3086 C CYS A 386 -36.761-155.130 303.926 1.00 92.54 C ANISOU 3086 C CYS A 386 10719 11868 12573 681 1232 -550 C ATOM 3087 O CYS A 386 -37.136-153.954 303.864 1.00 93.58 O ANISOU 3087 O CYS A 386 10824 12024 12709 647 1315 -568 O ATOM 3088 CB CYS A 386 -38.412-156.949 303.417 1.00106.28 C ANISOU 3088 CB CYS A 386 12444 13530 14408 678 1379 -522 C ATOM 3089 SG CYS A 386 -39.361-157.772 302.123 1.00112.79 S ANISOU 3089 SG CYS A 386 13106 14365 15382 686 1432 -529 S ATOM 3090 N LEU A 387 -35.949-155.570 304.893 1.00 87.19 N ANISOU 3090 N LEU A 387 10204 11121 11804 684 1081 -524 N ATOM 3091 CA LEU A 387 -35.379-154.645 305.869 1.00 82.33 C ANISOU 3091 CA LEU A 387 9745 10472 11064 634 1004 -516 C ATOM 3092 C LEU A 387 -34.670-153.490 305.177 1.00 80.08 C ANISOU 3092 C LEU A 387 9270 10297 10860 647 967 -561 C ATOM 3093 O LEU A 387 -34.831-152.325 305.555 1.00 82.21 O ANISOU 3093 O LEU A 387 9611 10565 11060 594 1024 -572 O ATOM 3094 CB LEU A 387 -34.405-155.380 306.790 1.00 80.79 C ANISOU 3094 CB LEU A 387 9729 10166 10801 638 741 -469 C ATOM 3095 CG LEU A 387 -34.980-156.281 307.878 1.00 80.95 C ANISOU 3095 CG LEU A 387 10088 10029 10640 557 735 -397 C ATOM 3096 CD1 LEU A 387 -33.860-156.766 308.784 1.00 81.85 C ANISOU 3096 CD1 LEU A 387 10410 9999 10689 547 375 -332 C ATOM 3097 CD2 LEU A 387 -36.037-155.537 308.673 1.00 83.23 C ANISOU 3097 CD2 LEU A 387 10610 10281 10733 423 1002 -410 C ATOM 3098 N LEU A 388 -33.875-153.809 304.154 1.00 76.64 N ANISOU 3098 N LEU A 388 8604 9945 10570 699 891 -601 N ATOM 3099 CA LEU A 388 -33.162-152.790 303.392 1.00 73.50 C ANISOU 3099 CA LEU A 388 8037 9653 10237 670 885 -650 C ATOM 3100 C LEU A 388 -34.117-151.722 302.874 1.00 72.42 C ANISOU 3100 C LEU A 388 7901 9550 10064 612 1035 -638 C ATOM 3101 O LEU A 388 -33.857-150.521 303.003 1.00 72.02 O ANISOU 3101 O LEU A 388 7872 9513 9980 560 1020 -642 O ATOM 3102 CB LEU A 388 -32.418-153.453 302.234 1.00 71.79 C ANISOU 3102 CB LEU A 388 7588 9514 10175 701 881 -726 C ATOM 3103 CG LEU A 388 -31.289-152.667 301.577 1.00 71.28 C ANISOU 3103 CG LEU A 388 7344 9544 10194 642 871 -803 C ATOM 3104 CD1 LEU A 388 -30.106-152.565 302.525 1.00 72.35 C ANISOU 3104 CD1 LEU A 388 7451 9626 10413 668 664 -820 C ATOM 3105 CD2 LEU A 388 -30.887-153.332 300.273 1.00 72.60 C ANISOU 3105 CD2 LEU A 388 7319 9785 10480 631 981 -909 C ATOM 3106 N ASN A 389 -35.234-152.153 302.282 1.00 72.10 N ANISOU 3106 N ASN A 389 7836 9500 10059 622 1149 -624 N ATOM 3107 CA ASN A 389 -36.257-151.216 301.831 1.00 72.12 C ANISOU 3107 CA ASN A 389 7824 9482 10095 584 1234 -610 C ATOM 3108 C ASN A 389 -36.719-150.318 302.973 1.00 71.37 C ANISOU 3108 C ASN A 389 7863 9300 9955 571 1292 -614 C ATOM 3109 O ASN A 389 -36.884-149.106 302.793 1.00 71.57 O ANISOU 3109 O ASN A 389 7876 9306 10012 540 1292 -623 O ATOM 3110 CB ASN A 389 -37.434-151.991 301.233 1.00 74.59 C ANISOU 3110 CB ASN A 389 8086 9760 10494 601 1306 -594 C ATOM 3111 CG ASN A 389 -38.373-151.112 300.432 1.00 76.86 C ANISOU 3111 CG ASN A 389 8309 10007 10888 564 1306 -576 C ATOM 3112 OD1 ASN A 389 -38.001-150.572 299.390 1.00 78.23 O ANISOU 3112 OD1 ASN A 389 8449 10226 11050 501 1222 -562 O ATOM 3113 ND2 ASN A 389 -39.609-150.984 300.902 1.00 77.36 N ANISOU 3113 ND2 ASN A 389 8358 9962 11072 587 1396 -582 N ATOM 3114 N SER A 390 -36.908-150.894 304.163 1.00 71.53 N ANISOU 3114 N SER A 390 8044 9249 9885 577 1344 -615 N ATOM 3115 CA SER A 390 -37.297-150.096 305.321 1.00 72.92 C ANISOU 3115 CA SER A 390 8399 9331 9975 532 1445 -649 C ATOM 3116 C SER A 390 -36.201-149.119 305.732 1.00 72.09 C ANISOU 3116 C SER A 390 8375 9241 9774 497 1309 -654 C ATOM 3117 O SER A 390 -36.501-148.073 306.317 1.00 74.38 O ANISOU 3117 O SER A 390 8771 9462 10027 458 1385 -699 O ATOM 3118 CB SER A 390 -37.649-151.005 306.498 1.00 75.11 C ANISOU 3118 CB SER A 390 8908 9519 10112 490 1535 -645 C ATOM 3119 OG SER A 390 -38.824-151.751 306.245 1.00 76.35 O ANISOU 3119 OG SER A 390 8994 9642 10374 495 1705 -655 O ATOM 3120 N THR A 391 -34.938-149.441 305.448 1.00 69.07 N ANISOU 3120 N THR A 391 7928 8935 9382 508 1116 -627 N ATOM 3121 CA THR A 391 -33.844-148.558 305.838 1.00 68.15 C ANISOU 3121 CA THR A 391 7858 8826 9210 462 965 -634 C ATOM 3122 C THR A 391 -33.702-147.379 304.881 1.00 69.86 C ANISOU 3122 C THR A 391 7926 9106 9513 429 975 -649 C ATOM 3123 O THR A 391 -33.413-146.258 305.313 1.00 74.73 O ANISOU 3123 O THR A 391 8631 9685 10079 374 934 -664 O ATOM 3124 CB THR A 391 -32.532-149.342 305.914 1.00 67.15 C ANISOU 3124 CB THR A 391 7667 8729 9119 484 746 -619 C ATOM 3125 OG1 THR A 391 -32.686-150.448 306.813 1.00 71.02 O ANISOU 3125 OG1 THR A 391 8343 9120 9520 503 683 -582 O ATOM 3126 CG2 THR A 391 -31.402-148.451 306.415 1.00 64.69 C ANISOU 3126 CG2 THR A 391 7390 8405 8784 425 562 -628 C ATOM 3127 N VAL A 392 -33.905-147.606 303.582 1.00 67.76 N ANISOU 3127 N VAL A 392 7475 8918 9353 439 1015 -643 N ATOM 3128 CA VAL A 392 -33.720-146.527 302.618 1.00 70.52 C ANISOU 3128 CA VAL A 392 7743 9307 9743 364 996 -638 C ATOM 3129 C VAL A 392 -34.954-145.644 302.491 1.00 72.42 C ANISOU 3129 C VAL A 392 8034 9445 10038 366 1060 -627 C ATOM 3130 O VAL A 392 -34.832-144.491 302.058 1.00 72.68 O ANISOU 3130 O VAL A 392 8077 9451 10087 298 1000 -614 O ATOM 3131 CB VAL A 392 -33.324-147.084 301.240 1.00 68.46 C ANISOU 3131 CB VAL A 392 7327 9154 9533 323 1004 -642 C ATOM 3132 CG1 VAL A 392 -32.183-148.079 301.385 1.00 66.08 C ANISOU 3132 CG1 VAL A 392 6919 8921 9266 352 962 -692 C ATOM 3133 CG2 VAL A 392 -34.518-147.730 300.552 1.00 69.70 C ANISOU 3133 CG2 VAL A 392 7464 9283 9736 360 1076 -617 C ATOM 3134 N ASN A 393 -36.135-146.145 302.858 1.00 73.58 N ANISOU 3134 N ASN A 393 8199 9513 10244 437 1173 -640 N ATOM 3135 CA ASN A 393 -37.342-145.324 302.772 1.00 74.60 C ANISOU 3135 CA ASN A 393 8313 9511 10520 458 1230 -661 C ATOM 3136 C ASN A 393 -37.252-144.022 303.562 1.00 77.07 C ANISOU 3136 C ASN A 393 8740 9725 10819 437 1236 -711 C ATOM 3137 O ASN A 393 -37.678-142.983 303.022 1.00 79.59 O ANISOU 3137 O ASN A 393 9019 9950 11272 427 1170 -707 O ATOM 3138 CB ASN A 393 -38.560-146.146 303.213 1.00 74.15 C ANISOU 3138 CB ASN A 393 8226 9380 10566 524 1394 -699 C ATOM 3139 CG ASN A 393 -39.110-147.009 302.099 1.00 74.36 C ANISOU 3139 CG ASN A 393 8110 9440 10703 541 1354 -650 C ATOM 3140 OD1 ASN A 393 -38.553-147.054 301.003 1.00 74.22 O ANISOU 3140 OD1 ASN A 393 8050 9503 10647 494 1220 -593 O ATOM 3141 ND2 ASN A 393 -40.207-147.702 302.373 1.00 74.58 N ANISOU 3141 ND2 ASN A 393 8080 9398 10858 584 1486 -682 N ATOM 3142 N PRO A 394 -36.744-143.983 304.802 1.00 76.41 N ANISOU 3142 N PRO A 394 8824 9628 10579 419 1286 -756 N ATOM 3143 CA PRO A 394 -36.549-142.675 305.449 1.00 78.48 C ANISOU 3143 CA PRO A 394 9219 9792 10809 379 1273 -810 C ATOM 3144 C PRO A 394 -35.650-141.761 304.642 1.00 77.41 C ANISOU 3144 C PRO A 394 9036 9704 10671 310 1080 -751 C ATOM 3145 O PRO A 394 -35.868-140.544 304.598 1.00 80.20 O ANISOU 3145 O PRO A 394 9429 9945 11099 288 1042 -776 O ATOM 3146 CB PRO A 394 -35.921-143.040 306.802 1.00 79.01 C ANISOU 3146 CB PRO A 394 9518 9856 10647 333 1296 -841 C ATOM 3147 CG PRO A 394 -36.309-144.447 307.039 1.00 79.43 C ANISOU 3147 CG PRO A 394 9578 9943 10659 365 1390 -825 C ATOM 3148 CD PRO A 394 -36.350-145.089 305.693 1.00 76.57 C ANISOU 3148 CD PRO A 394 8967 9689 10438 416 1322 -755 C ATOM 3149 N ILE A 395 -34.645-142.334 303.979 1.00 75.98 N ANISOU 3149 N ILE A 395 8769 9674 10426 263 972 -688 N ATOM 3150 CA ILE A 395 -33.716-141.541 303.185 1.00 75.05 C ANISOU 3150 CA ILE A 395 8609 9613 10294 152 838 -646 C ATOM 3151 C ILE A 395 -34.387-141.040 301.911 1.00 73.13 C ANISOU 3151 C ILE A 395 8307 9324 10154 114 799 -593 C ATOM 3152 O ILE A 395 -34.157-139.904 301.478 1.00 73.17 O ANISOU 3152 O ILE A 395 8367 9268 10164 17 695 -562 O ATOM 3153 CB ILE A 395 -32.456-142.372 302.884 1.00 74.57 C ANISOU 3153 CB ILE A 395 8440 9712 10181 104 787 -636 C ATOM 3154 CG1 ILE A 395 -31.738-142.728 304.189 1.00 76.05 C ANISOU 3154 CG1 ILE A 395 8712 9891 10291 130 725 -668 C ATOM 3155 CG2 ILE A 395 -31.535-141.632 301.931 1.00 74.76 C ANISOU 3155 CG2 ILE A 395 8398 9804 10203 -49 718 -616 C ATOM 3156 CD1 ILE A 395 -30.490-143.555 303.996 1.00 78.31 C ANISOU 3156 CD1 ILE A 395 8844 10290 10621 112 633 -679 C ATOM 3157 N ILE A 396 -35.238-141.866 301.300 1.00 71.48 N ANISOU 3157 N ILE A 396 8015 9120 10026 174 847 -573 N ATOM 3158 CA ILE A 396 -35.836-141.507 300.016 1.00 70.60 C ANISOU 3158 CA ILE A 396 7883 8946 9996 114 744 -503 C ATOM 3159 C ILE A 396 -36.830-140.365 300.183 1.00 69.21 C ANISOU 3159 C ILE A 396 7745 8550 10002 160 664 -508 C ATOM 3160 O ILE A 396 -36.814-139.391 299.422 1.00 70.85 O ANISOU 3160 O ILE A 396 8023 8661 10234 61 491 -442 O ATOM 3161 CB ILE A 396 -36.505-142.734 299.371 1.00 72.90 C ANISOU 3161 CB ILE A 396 8084 9279 10336 161 785 -484 C ATOM 3162 CG1 ILE A 396 -35.469-143.802 299.029 1.00 74.76 C ANISOU 3162 CG1 ILE A 396 8274 9704 10427 110 854 -497 C ATOM 3163 CG2 ILE A 396 -37.265-142.328 298.117 1.00 74.61 C ANISOU 3163 CG2 ILE A 396 8326 9384 10640 88 621 -401 C ATOM 3164 CD1 ILE A 396 -36.085-145.090 298.538 1.00 74.91 C ANISOU 3164 CD1 ILE A 396 8224 9756 10484 165 906 -493 C ATOM 3165 N TYR A 397 -37.716-140.469 301.173 1.00 66.61 N ANISOU 3165 N TYR A 397 7376 8116 9815 298 793 -598 N ATOM 3166 CA TYR A 397 -38.844-139.555 301.303 1.00 66.19 C ANISOU 3166 CA TYR A 397 7286 7826 10038 375 754 -647 C ATOM 3167 C TYR A 397 -38.652-138.542 302.423 1.00 64.87 C ANISOU 3167 C TYR A 397 7225 7553 9868 395 831 -751 C ATOM 3168 O TYR A 397 -38.678-137.333 302.171 1.00 69.73 O ANISOU 3168 O TYR A 397 7893 8016 10584 366 678 -740 O ATOM 3169 CB TYR A 397 -40.133-140.354 301.528 1.00 68.70 C ANISOU 3169 CB TYR A 397 7445 8069 10589 500 894 -716 C ATOM 3170 CG TYR A 397 -40.389-141.403 300.476 1.00 69.77 C ANISOU 3170 CG TYR A 397 7492 8290 10727 479 810 -621 C ATOM 3171 CD1 TYR A 397 -41.051-141.085 299.299 1.00 71.15 C ANISOU 3171 CD1 TYR A 397 7613 8332 11088 452 563 -535 C ATOM 3172 CD2 TYR A 397 -39.969-142.714 300.659 1.00 71.86 C ANISOU 3172 CD2 TYR A 397 7754 8741 10807 475 947 -616 C ATOM 3173 CE1 TYR A 397 -41.293-142.043 298.335 1.00 72.60 C ANISOU 3173 CE1 TYR A 397 7761 8580 11245 409 476 -453 C ATOM 3174 CE2 TYR A 397 -40.203-143.680 299.701 1.00 72.05 C ANISOU 3174 CE2 TYR A 397 7715 8831 10830 452 881 -547 C ATOM 3175 CZ TYR A 397 -40.866-143.339 298.540 1.00 73.17 C ANISOU 3175 CZ TYR A 397 7822 8851 11128 412 656 -469 C ATOM 3176 OH TYR A 397 -41.101-144.298 297.582 1.00 74.64 O ANISOU 3176 OH TYR A 397 7988 9088 11283 365 579 -404 O ATOM 3177 N ALA A 398 -38.475-139.009 303.660 1.00 61.45 N ANISOU 3177 N ALA A 398 6864 7176 9307 426 1049 -850 N ATOM 3178 CA ALA A 398 -38.394-138.096 304.796 1.00 63.74 C ANISOU 3178 CA ALA A 398 7304 7344 9570 426 1147 -972 C ATOM 3179 C ALA A 398 -37.255-137.101 304.619 1.00 68.65 C ANISOU 3179 C ALA A 398 8056 7986 10043 315 949 -907 C ATOM 3180 O ALA A 398 -37.449-135.889 304.755 1.00 70.52 O ANISOU 3180 O ALA A 398 8356 8044 10396 314 886 -959 O ATOM 3181 CB ALA A 398 -38.232-138.889 306.093 1.00 60.84 C ANISOU 3181 CB ALA A 398 7078 7043 8994 418 1376 -1058 C ATOM 3182 N LEU A 399 -36.063-137.596 304.281 1.00 69.04 N ANISOU 3182 N LEU A 399 8125 8235 9871 217 849 -807 N ATOM 3183 CA LEU A 399 -34.926-136.703 304.087 1.00 70.04 C ANISOU 3183 CA LEU A 399 8343 8391 9879 84 681 -754 C ATOM 3184 C LEU A 399 -35.181-135.702 302.966 1.00 71.57 C ANISOU 3184 C LEU A 399 8521 8467 10205 22 504 -677 C ATOM 3185 O LEU A 399 -34.686-134.570 303.020 1.00 74.34 O ANISOU 3185 O LEU A 399 8987 8729 10529 -70 385 -668 O ATOM 3186 CB LEU A 399 -33.670-137.522 303.797 1.00 68.79 C ANISOU 3186 CB LEU A 399 8131 8458 9549 -7 633 -687 C ATOM 3187 CG LEU A 399 -32.331-136.816 304.003 1.00 67.62 C ANISOU 3187 CG LEU A 399 8053 8357 9283 -150 506 -671 C ATOM 3188 CD1 LEU A 399 -32.243-136.263 305.414 1.00 60.54 C ANISOU 3188 CD1 LEU A 399 7348 7345 8308 -134 513 -757 C ATOM 3189 CD2 LEU A 399 -31.193-137.785 303.740 1.00 58.86 C ANISOU 3189 CD2 LEU A 399 6811 7449 8105 -209 484 -644 C ATOM 3190 N ARG A 400 -35.958-136.089 301.954 1.00 70.54 N ANISOU 3190 N ARG A 400 8281 8310 10210 54 454 -613 N ATOM 3191 CA ARG A 400 -36.231-135.211 300.824 1.00 72.36 C ANISOU 3191 CA ARG A 400 8553 8398 10543 -33 224 -512 C ATOM 3192 C ARG A 400 -37.260-134.130 301.135 1.00 73.81 C ANISOU 3192 C ARG A 400 8749 8278 11018 75 137 -578 C ATOM 3193 O ARG A 400 -37.460-133.238 300.303 1.00 73.62 O ANISOU 3193 O ARG A 400 8797 8079 11097 1 -116 -487 O ATOM 3194 CB ARG A 400 -36.700-136.035 299.622 1.00 71.71 C ANISOU 3194 CB ARG A 400 8391 8366 10487 -59 153 -415 C ATOM 3195 N SER A 401 -37.908-134.176 302.297 1.00 76.00 N ANISOU 3195 N SER A 401 8974 8467 11436 232 342 -742 N ATOM 3196 CA SER A 401 -38.939-133.200 302.635 1.00 81.31 C ANISOU 3196 CA SER A 401 9609 8831 12456 354 314 -859 C ATOM 3197 C SER A 401 -38.293-131.931 303.179 1.00 82.69 C ANISOU 3197 C SER A 401 9974 8889 12557 285 248 -903 C ATOM 3198 O SER A 401 -37.555-131.977 304.169 1.00 80.70 O ANISOU 3198 O SER A 401 9849 8748 12065 241 409 -978 O ATOM 3199 CB SER A 401 -39.916-133.785 303.653 1.00 82.50 C ANISOU 3199 CB SER A 401 9628 8928 12791 516 635 -1056 C ATOM 3200 OG SER A 401 -40.950-132.863 303.956 1.00 83.84 O ANISOU 3200 OG SER A 401 9706 8779 13370 643 650 -1212 O ATOM 3201 N LYS A 402 -38.579-130.798 302.531 1.00 86.38 N ANISOU 3201 N LYS A 402 10481 9107 13231 266 -26 -850 N ATOM 3202 CA LYS A 402 -38.017-129.520 302.961 1.00 90.23 C ANISOU 3202 CA LYS A 402 11159 9448 13675 194 -122 -886 C ATOM 3203 C LYS A 402 -38.459-129.168 304.374 1.00 92.30 C ANISOU 3203 C LYS A 402 11441 9572 14058 326 150 -1140 C ATOM 3204 O LYS A 402 -37.649-128.734 305.202 1.00 92.00 O ANISOU 3204 O LYS A 402 11598 9576 13784 241 225 -1201 O ATOM 3205 CB LYS A 402 -38.432-128.415 301.991 1.00 94.66 C ANISOU 3205 CB LYS A 402 11767 9710 14489 164 -494 -782 C ATOM 3206 CG LYS A 402 -37.333-127.922 301.075 1.00 95.94 C ANISOU 3206 CG LYS A 402 12143 9951 14358 -101 -753 -567 C ATOM 3207 CD LYS A 402 -37.813-126.720 300.281 1.00 99.55 C ANISOU 3207 CD LYS A 402 12715 10047 15062 -141 -1146 -469 C ATOM 3208 CE LYS A 402 -36.721-126.166 299.384 1.00101.62 C ANISOU 3208 CE LYS A 402 13242 10368 14999 -458 -1376 -258 C ATOM 3209 NZ LYS A 402 -37.205-125.000 298.595 1.00105.92 N ANISOU 3209 NZ LYS A 402 13960 10526 15759 -524 -1807 -137 N ATOM 3210 N ASP A 403 -39.751-129.339 304.663 1.00 95.25 N ANISOU 3210 N ASP A 403 11619 9765 14807 516 308 -1305 N ATOM 3211 CA ASP A 403 -40.282-128.955 305.966 1.00 99.80 C ANISOU 3211 CA ASP A 403 12221 10175 15523 619 626 -1589 C ATOM 3212 C ASP A 403 -39.616-129.740 307.089 1.00 97.92 C ANISOU 3212 C ASP A 403 12159 10187 14860 534 942 -1661 C ATOM 3213 O ASP A 403 -39.321-129.186 308.155 1.00 97.43 O ANISOU 3213 O ASP A 403 12317 10047 14657 490 1102 -1819 O ATOM 3214 CB ASP A 403 -41.795-129.167 305.988 1.00103.91 C ANISOU 3214 CB ASP A 403 12439 10479 16562 818 786 -1767 C ATOM 3215 CG ASP A 403 -42.505-128.430 304.874 1.00107.29 C ANISOU 3215 CG ASP A 403 12688 10612 17464 910 393 -1685 C ATOM 3216 OD1 ASP A 403 -42.351-127.194 304.783 1.00111.06 O ANISOU 3216 OD1 ASP A 403 13279 10842 18077 905 167 -1695 O ATOM 3217 OD2 ASP A 403 -43.216-129.089 304.086 1.00105.12 O ANISOU 3217 OD2 ASP A 403 12181 10333 17427 978 276 -1601 O ATOM 3218 N LEU A 404 -39.367-131.033 306.862 1.00 95.80 N ANISOU 3218 N LEU A 404 11826 10196 14379 500 1004 -1543 N ATOM 3219 CA LEU A 404 -38.748-131.870 307.885 1.00 92.94 C ANISOU 3219 CA LEU A 404 11643 10041 13630 417 1234 -1584 C ATOM 3220 C LEU A 404 -37.358-131.367 308.252 1.00 86.90 C ANISOU 3220 C LEU A 404 11141 9367 12510 257 1071 -1507 C ATOM 3221 O LEU A 404 -37.004-131.309 309.436 1.00 86.30 O ANISOU 3221 O LEU A 404 11313 9280 12198 188 1224 -1624 O ATOM 3222 CB LEU A 404 -38.680-133.318 307.398 1.00 95.80 C ANISOU 3222 CB LEU A 404 11869 10654 13875 417 1255 -1448 C ATOM 3223 CG LEU A 404 -38.033-134.319 308.356 1.00100.12 C ANISOU 3223 CG LEU A 404 12601 11395 14045 333 1419 -1456 C ATOM 3224 CD1 LEU A 404 -38.879-134.437 309.577 1.00102.05 C ANISOU 3224 CD1 LEU A 404 12963 11505 14306 357 1791 -1687 C ATOM 3225 CD2 LEU A 404 -37.867-135.681 307.724 1.00101.18 C ANISOU 3225 CD2 LEU A 404 12589 11754 14099 341 1380 -1309 C ATOM 3226 N ARG A 405 -36.554-131.006 307.250 1.00 83.57 N ANISOU 3226 N ARG A 405 10686 9025 12042 170 760 -1313 N ATOM 3227 CA ARG A 405 -35.208-130.515 307.525 1.00 85.14 C ANISOU 3227 CA ARG A 405 11081 9307 11961 4 598 -1243 C ATOM 3228 C ARG A 405 -35.246-129.214 308.318 1.00 89.53 C ANISOU 3228 C ARG A 405 11853 9616 12549 -18 601 -1390 C ATOM 3229 O ARG A 405 -34.437-129.012 309.231 1.00 91.33 O ANISOU 3229 O ARG A 405 12314 9870 12516 -130 600 -1434 O ATOM 3230 CB ARG A 405 -34.435-130.337 306.218 1.00 86.31 C ANISOU 3230 CB ARG A 405 11137 9570 12086 -114 323 -1034 C ATOM 3231 CG ARG A 405 -34.041-131.657 305.573 1.00 86.63 C ANISOU 3231 CG ARG A 405 11016 9883 12017 -136 338 -912 C ATOM 3232 CD ARG A 405 -33.072-131.465 304.419 1.00 88.47 C ANISOU 3232 CD ARG A 405 11204 10241 12168 -311 137 -747 C ATOM 3233 NE ARG A 405 -33.739-131.014 303.202 1.00 91.78 N ANISOU 3233 NE ARG A 405 11578 10538 12757 -323 -1 -654 N ATOM 3234 CZ ARG A 405 -33.138-130.904 302.022 1.00 95.83 C ANISOU 3234 CZ ARG A 405 12093 11133 13185 -505 -143 -509 C ATOM 3235 NH1 ARG A 405 -33.819-130.487 300.963 1.00 99.10 N ANISOU 3235 NH1 ARG A 405 12535 11394 13724 -536 -311 -413 N ATOM 3236 NH2 ARG A 405 -31.854-131.213 301.899 1.00 96.32 N ANISOU 3236 NH2 ARG A 405 12137 11411 13048 -672 -121 -470 N ATOM 3237 N HIS A 406 -36.183-128.321 307.988 1.00 91.64 N ANISOU 3237 N HIS A 406 12052 9614 13155 87 579 -1473 N ATOM 3238 CA HIS A 406 -36.352-127.110 308.784 1.00 94.84 C ANISOU 3238 CA HIS A 406 12651 9745 13638 91 621 -1657 C ATOM 3239 C HIS A 406 -36.786-127.449 310.204 1.00 91.72 C ANISOU 3239 C HIS A 406 12416 9302 13131 122 998 -1905 C ATOM 3240 O HIS A 406 -36.366-126.793 311.165 1.00 93.09 O ANISOU 3240 O HIS A 406 12881 9369 13120 30 1052 -2032 O ATOM 3241 CB HIS A 406 -37.368-126.182 308.118 1.00102.91 C ANISOU 3241 CB HIS A 406 13522 10451 15128 227 508 -1712 C ATOM 3242 CG HIS A 406 -36.991-125.772 306.729 1.00107.11 C ANISOU 3242 CG HIS A 406 13988 10983 15726 150 114 -1459 C ATOM 3243 ND1 HIS A 406 -35.682-125.681 306.308 1.00107.64 N ANISOU 3243 ND1 HIS A 406 14186 11245 15466 -64 -90 -1262 N ATOM 3244 CD2 HIS A 406 -37.753-125.433 305.662 1.00110.21 C ANISOU 3244 CD2 HIS A 406 14220 11185 16468 231 -116 -1374 C ATOM 3245 CE1 HIS A 406 -35.653-125.301 305.043 1.00108.78 C ANISOU 3245 CE1 HIS A 406 14286 11331 15713 -135 -383 -1072 C ATOM 3246 NE2 HIS A 406 -36.897-125.144 304.627 1.00110.40 N ANISOU 3246 NE2 HIS A 406 14341 11296 16312 39 -436 -1122 N ATOM 3247 N ALA A 407 -37.621-128.480 310.355 1.00 89.11 N ANISOU 3247 N ALA A 407 11933 9041 12885 221 1268 -1978 N ATOM 3248 CA ALA A 407 -38.086-128.876 311.680 1.00 90.15 C ANISOU 3248 CA ALA A 407 12254 9125 12875 205 1671 -2216 C ATOM 3249 C ALA A 407 -36.971-129.525 312.490 1.00 88.33 C ANISOU 3249 C ALA A 407 12341 9101 12120 22 1643 -2133 C ATOM 3250 O ALA A 407 -36.905-129.352 313.713 1.00 91.42 O ANISOU 3250 O ALA A 407 13076 9397 12263 -83 1845 -2306 O ATOM 3251 CB ALA A 407 -39.274-129.826 311.552 1.00 89.35 C ANISOU 3251 CB ALA A 407 11891 9038 13021 333 1961 -2304 C ATOM 3252 N PHE A 408 -36.095-130.286 311.832 1.00 83.33 N ANISOU 3252 N PHE A 408 11608 8728 11326 -27 1385 -1880 N ATOM 3253 CA PHE A 408 -34.958-130.869 312.535 1.00 81.89 C ANISOU 3253 CA PHE A 408 11681 8708 10727 -186 1271 -1790 C ATOM 3254 C PHE A 408 -34.001-129.783 313.009 1.00 82.92 C ANISOU 3254 C PHE A 408 12075 8742 10688 -327 1054 -1797 C ATOM 3255 O PHE A 408 -33.536-129.805 314.155 1.00 84.71 O ANISOU 3255 O PHE A 408 12664 8926 10598 -463 1073 -1868 O ATOM 3256 CB PHE A 408 -34.239-131.874 311.635 1.00 80.29 C ANISOU 3256 CB PHE A 408 11244 8776 10487 -186 1049 -1551 C ATOM 3257 CG PHE A 408 -33.068-132.543 312.295 1.00 81.38 C ANISOU 3257 CG PHE A 408 11576 9052 10292 -321 880 -1458 C ATOM 3258 CD1 PHE A 408 -33.252-133.338 313.413 1.00 82.87 C ANISOU 3258 CD1 PHE A 408 12036 9224 10227 -376 1036 -1530 C ATOM 3259 CD2 PHE A 408 -31.786-132.379 311.798 1.00 81.07 C ANISOU 3259 CD2 PHE A 408 11452 9136 10216 -411 552 -1304 C ATOM 3260 CE1 PHE A 408 -32.180-133.955 314.027 1.00 83.26 C ANISOU 3260 CE1 PHE A 408 12281 9355 9999 -501 802 -1430 C ATOM 3261 CE2 PHE A 408 -30.709-132.995 312.406 1.00 82.54 C ANISOU 3261 CE2 PHE A 408 11767 9414 10181 -520 349 -1229 C ATOM 3262 CZ PHE A 408 -30.906-133.785 313.523 1.00 83.41 C ANISOU 3262 CZ PHE A 408 12161 9484 10049 -557 440 -1282 C ATOM 3263 N ARG A 409 -33.703-128.814 312.138 1.00 82.04 N ANISOU 3263 N ARG A 409 11823 8577 10772 -319 827 -1717 N ATOM 3264 CA ARG A 409 -32.874-127.682 312.536 1.00 82.80 C ANISOU 3264 CA ARG A 409 12158 8555 10749 -458 625 -1733 C ATOM 3265 C ARG A 409 -33.535-126.868 313.639 1.00 86.23 C ANISOU 3265 C ARG A 409 12900 8708 11157 -461 861 -2001 C ATOM 3266 O ARG A 409 -32.844-126.245 314.454 1.00 83.98 O ANISOU 3266 O ARG A 409 12945 8329 10634 -612 758 -2056 O ATOM 3267 CB ARG A 409 -32.587-126.803 311.319 1.00 84.70 C ANISOU 3267 CB ARG A 409 12201 8764 11219 -463 368 -1598 C ATOM 3268 CG ARG A 409 -31.587-125.693 311.565 1.00 91.03 C ANISOU 3268 CG ARG A 409 13212 9471 11904 -635 119 -1574 C ATOM 3269 CD ARG A 409 -31.105-125.104 310.255 1.00 92.50 C ANISOU 3269 CD ARG A 409 13208 9690 12246 -702 -142 -1389 C ATOM 3270 NE ARG A 409 -29.778-124.514 310.390 1.00 94.69 N ANISOU 3270 NE ARG A 409 13613 10006 12361 -921 -396 -1305 N ATOM 3271 CZ ARG A 409 -28.951-124.300 309.373 1.00 95.84 C ANISOU 3271 CZ ARG A 409 13606 10269 12541 -1065 -602 -1127 C ATOM 3272 NH1 ARG A 409 -27.759-123.761 309.587 1.00 97.87 N ANISOU 3272 NH1 ARG A 409 13956 10547 12682 -1276 -809 -1077 N ATOM 3273 NH2 ARG A 409 -29.313-124.634 308.141 1.00 95.30 N ANISOU 3273 NH2 ARG A 409 13305 10287 12618 -1023 -593 -1008 N ATOM 3274 N SER A 410 -34.870-126.873 313.687 1.00 90.95 N ANISOU 3274 N SER A 410 13387 9155 12015 -304 1189 -2189 N ATOM 3275 CA SER A 410 -35.595-126.124 314.709 1.00 95.81 C ANISOU 3275 CA SER A 410 14257 9485 12661 -301 1496 -2500 C ATOM 3276 C SER A 410 -35.298-126.633 316.114 1.00 96.78 C ANISOU 3276 C SER A 410 14826 9626 12320 -480 1694 -2617 C ATOM 3277 O SER A 410 -35.397-125.871 317.082 1.00101.41 O ANISOU 3277 O SER A 410 15771 9991 12769 -577 1856 -2844 O ATOM 3278 CB SER A 410 -37.096-126.193 314.430 1.00100.37 C ANISOU 3278 CB SER A 410 14544 9909 13683 -95 1831 -2692 C ATOM 3279 OG SER A 410 -37.845-125.864 315.587 1.00108.21 O ANISOU 3279 OG SER A 410 15777 10672 14665 -116 2265 -3039 O ATOM 3280 N MET A 411 -34.936-127.910 316.250 1.00 93.07 N ANISOU 3280 N MET A 411 14377 9393 11593 -541 1669 -2469 N ATOM 3281 CA MET A 411 -34.702-128.491 317.567 1.00 94.62 C ANISOU 3281 CA MET A 411 15045 9582 11326 -733 1813 -2552 C ATOM 3282 C MET A 411 -33.394-128.033 318.199 1.00 97.05 C ANISOU 3282 C MET A 411 15735 9871 11270 -944 1449 -2462 C ATOM 3283 O MET A 411 -33.115-128.415 319.341 1.00 98.57 O ANISOU 3283 O MET A 411 16398 10014 11038 -1140 1489 -2517 O ATOM 3284 CB MET A 411 -34.734-130.017 317.471 1.00 93.91 C ANISOU 3284 CB MET A 411 14856 9716 11109 -727 1844 -2404 C ATOM 3285 CG MET A 411 -36.036-130.558 316.896 1.00 95.28 C ANISOU 3285 CG MET A 411 14660 9908 11633 -541 2197 -2491 C ATOM 3286 SD MET A 411 -36.066-132.349 316.693 1.00 93.12 S ANISOU 3286 SD MET A 411 14262 9888 11230 -533 2208 -2305 S ATOM 3287 CE MET A 411 -35.861-132.892 318.386 1.00 96.05 C ANISOU 3287 CE MET A 411 15311 10171 11011 -816 2383 -2410 C ATOM 3288 N PHE A 412 -32.596-127.226 317.502 1.00 98.20 N ANISOU 3288 N PHE A 412 15716 10034 11563 -935 1084 -2326 N ATOM 3289 CA PHE A 412 -31.328-126.731 318.007 1.00101.35 C ANISOU 3289 CA PHE A 412 16412 10408 11690 -1136 705 -2237 C ATOM 3290 C PHE A 412 -31.447-125.266 318.413 1.00107.27 C ANISOU 3290 C PHE A 412 17408 10881 12468 -1193 745 -2431 C ATOM 3291 O PHE A 412 -32.252-124.521 317.846 1.00108.56 O ANISOU 3291 O PHE A 412 17354 10910 12985 -1036 920 -2550 O ATOM 3292 CB PHE A 412 -30.234-126.886 316.946 1.00 97.35 C ANISOU 3292 CB PHE A 412 15536 10119 11333 -1127 278 -1955 C ATOM 3293 CG PHE A 412 -30.077-128.294 316.447 1.00 95.82 C ANISOU 3293 CG PHE A 412 15064 10183 11161 -1055 234 -1782 C ATOM 3294 CD1 PHE A 412 -29.344-129.221 317.169 1.00 97.16 C ANISOU 3294 CD1 PHE A 412 15442 10432 11044 -1178 43 -1691 C ATOM 3295 CD2 PHE A 412 -30.673-128.694 315.262 1.00 92.82 C ANISOU 3295 CD2 PHE A 412 14237 9935 11094 -870 355 -1712 C ATOM 3296 CE1 PHE A 412 -29.202-130.519 316.716 1.00 94.75 C ANISOU 3296 CE1 PHE A 412 14879 10333 10788 -1100 -8 -1545 C ATOM 3297 CE2 PHE A 412 -30.533-129.991 314.803 1.00 90.47 C ANISOU 3297 CE2 PHE A 412 13701 9860 10815 -808 325 -1570 C ATOM 3298 CZ PHE A 412 -29.797-130.904 315.531 1.00 91.71 C ANISOU 3298 CZ PHE A 412 14044 10093 10709 -914 155 -1493 C ATOM 3299 N PRO A 413 -30.668-124.826 319.401 1.00112.27 N ANISOU 3299 N PRO A 413 18510 11397 12750 -1417 556 -2469 N ATOM 3300 CA PRO A 413 -30.753-123.426 319.832 1.00116.33 C ANISOU 3300 CA PRO A 413 19298 11630 13274 -1484 592 -2668 C ATOM 3301 C PRO A 413 -30.247-122.484 318.751 1.00114.96 C ANISOU 3301 C PRO A 413 18792 11457 13431 -1422 280 -2528 C ATOM 3302 O PRO A 413 -29.217-122.731 318.118 1.00112.26 O ANISOU 3302 O PRO A 413 18228 11313 13111 -1479 -99 -2269 O ATOM 3303 CB PRO A 413 -29.861-123.383 321.077 1.00118.77 C ANISOU 3303 CB PRO A 413 20194 11851 13082 -1774 370 -2680 C ATOM 3304 CG PRO A 413 -28.888-124.494 320.870 1.00115.73 C ANISOU 3304 CG PRO A 413 19667 11727 12576 -1832 -7 -2387 C ATOM 3305 CD PRO A 413 -29.659-125.577 320.168 1.00112.32 C ANISOU 3305 CD PRO A 413 18829 11494 12352 -1624 255 -2329 C ATOM 3306 N SER A 414 -30.988-121.400 318.541 1.00115.38 N ANISOU 3306 N SER A 414 18813 11266 13761 -1316 452 -2713 N ATOM 3307 CA SER A 414 -30.647-120.408 317.525 1.00114.58 C ANISOU 3307 CA SER A 414 18460 11106 13969 -1274 167 -2591 C ATOM 3308 C SER A 414 -31.490-119.149 317.696 1.00116.94 C ANISOU 3308 C SER A 414 18876 11038 14518 -1184 355 -2860 C ATOM 3309 O SER A 414 -31.117-118.230 318.425 1.00119.67 O ANISOU 3309 O SER A 414 19601 11166 14704 -1329 281 -2994 O ATOM 3310 CB SER A 414 -30.844-120.982 316.118 1.00111.31 C ANISOU 3310 CB SER A 414 17512 10909 13872 -1111 95 -2370 C ATOM 3311 OG SER A 414 -29.931-122.035 315.855 1.00107.71 O ANISOU 3311 OG SER A 414 16914 10772 13237 -1197 -109 -2130 O TER 3312 SER A 414 HETATM 3313 N1 FMN A 601 -41.702-109.014 246.665 1.00 68.82 N HETATM 3314 C2 FMN A 601 -42.450-108.310 247.556 1.00 68.82 C HETATM 3315 O2 FMN A 601 -41.990-108.013 248.608 1.00 66.78 O HETATM 3316 N3 FMN A 601 -43.727-107.943 247.242 1.00 69.31 N HETATM 3317 C4 FMN A 601 -44.243-108.276 246.065 1.00 68.57 C HETATM 3318 O4 FMN A 601 -45.351-107.964 245.782 1.00 67.82 O HETATM 3319 C4A FMN A 601 -43.489-108.989 245.165 1.00 69.11 C HETATM 3320 N5 FMN A 601 -44.028-109.321 243.971 1.00 70.56 N HETATM 3321 C5A FMN A 601 -43.306-110.014 243.081 1.00 72.25 C HETATM 3322 C6 FMN A 601 -43.879-110.355 241.839 1.00 72.22 C HETATM 3323 C7 FMN A 601 -43.142-111.071 240.908 1.00 73.35 C HETATM 3324 C7M FMN A 601 -43.882-111.372 239.608 1.00 74.07 C HETATM 3325 C8 FMN A 601 -41.840-111.452 241.204 1.00 75.00 C HETATM 3326 C8M FMN A 601 -41.006-112.239 240.196 1.00 76.68 C HETATM 3327 C9 FMN A 601 -41.278-111.115 242.427 1.00 75.05 C HETATM 3328 C9A FMN A 601 -42.022-110.386 243.380 1.00 73.90 C HETATM 3329 N10 FMN A 601 -41.480-110.061 244.571 1.00 72.88 N HETATM 3330 C10 FMN A 601 -42.218-109.354 245.471 1.00 69.40 C HETATM 3331 C1' FMN A 601 -40.130-110.393 245.028 1.00 76.10 C HETATM 3332 C2' FMN A 601 -40.057-111.859 245.496 1.00 77.96 C HETATM 3333 O2' FMN A 601 -40.794-112.037 246.674 1.00 78.43 O HETATM 3334 C3' FMN A 601 -38.606-112.296 245.732 1.00 79.68 C HETATM 3335 O3' FMN A 601 -38.060-112.817 244.552 1.00 80.26 O HETATM 3336 C4' FMN A 601 -38.529-113.354 246.839 1.00 79.04 C HETATM 3337 O4' FMN A 601 -37.269-113.297 247.448 1.00 77.87 O HETATM 3338 C5' FMN A 601 -38.740-114.767 246.284 1.00 77.40 C HETATM 3339 O5' FMN A 601 -38.155-115.676 247.178 1.00 74.61 O HETATM 3340 P FMN A 601 -38.608-117.264 247.216 1.00 66.83 P HETATM 3341 O1P FMN A 601 -40.038-117.429 246.759 1.00 64.36 O HETATM 3342 O2P FMN A 601 -37.707-118.076 246.319 1.00 67.99 O HETATM 3343 O3P FMN A 601 -38.472-117.756 248.636 1.00 64.97 O HETATM 3344 C1 8D3 A 602 -39.903-164.552 306.043 1.00 58.33 C HETATM 3345 O1 8D3 A 602 -39.004-165.489 305.620 1.00 60.51 O HETATM 3346 O2 8D3 A 602 -41.883-163.801 308.965 1.00 52.80 O HETATM 3347 C2 8D3 A 602 -40.234-163.510 305.189 1.00 59.63 C HETATM 3348 C3 8D3 A 602 -41.142-162.550 305.603 1.00 60.34 C HETATM 3349 C5 8D3 A 602 -40.472-164.644 307.330 1.00 56.27 C HETATM 3350 C6 8D3 A 602 -41.403-164.717 310.006 1.00 57.55 C HETATM 3351 C4 8D3 A 602 -41.720-162.689 306.855 1.00 57.65 C HETATM 3352 C10 8D3 A 602 -40.264-168.129 309.641 1.00 57.61 C HETATM 3353 C11 8D3 A 602 -40.254-168.156 308.247 1.00 58.04 C HETATM 3354 C12 8D3 A 602 -40.459-166.976 307.509 1.00 58.27 C HETATM 3355 C13 8D3 A 602 -40.191-165.652 308.265 1.00 57.91 C HETATM 3356 C14 8D3 A 602 -42.477-164.847 311.087 1.00 56.69 C HETATM 3357 C15 8D3 A 602 -40.107-164.179 310.625 1.00 59.27 C HETATM 3358 C16 8D3 A 602 -40.038-169.359 307.582 1.00 55.97 C HETATM 3359 C17 8D3 A 602 -41.492-161.475 304.778 1.00 60.52 C HETATM 3360 C18 8D3 A 602 -43.005-161.239 304.730 1.00 61.69 C HETATM 3361 C19 8D3 A 602 -41.009-161.751 303.355 1.00 59.05 C HETATM 3362 C20 8D3 A 602 -40.799-160.215 305.291 1.00 60.32 C HETATM 3363 C21 8D3 A 602 -43.733-162.448 304.138 1.00 65.48 C HETATM 3364 C22 8D3 A 602 -45.235-162.158 304.090 1.00 70.24 C HETATM 3365 C23 8D3 A 602 -45.965-163.352 303.464 1.00 75.68 C HETATM 3366 C24 8D3 A 602 -47.465-163.057 303.404 1.00 80.55 C HETATM 3367 C25 8D3 A 602 -48.229-164.218 302.754 1.00 84.59 C HETATM 3368 C7 8D3 A 602 -41.230-163.558 307.805 1.00 54.46 C HETATM 3369 C8 8D3 A 602 -41.238-165.971 309.314 1.00 59.80 C HETATM 3370 C9 8D3 A 602 -40.483-166.894 310.237 1.00 59.27 C HETATM 3371 BR1 8D3 A 602 -48.015-165.878 303.742 1.00 87.54 BR HETATM 3372 C1 OLA A 603 -17.579-168.576 307.726 1.00 86.25 C HETATM 3373 O1 OLA A 603 -17.009-169.426 306.995 1.00 84.87 O HETATM 3374 O2 OLA A 603 -17.460-168.641 308.975 1.00 89.12 O HETATM 3375 C2 OLA A 603 -18.411-167.462 307.098 1.00 83.49 C HETATM 3376 C3 OLA A 603 -17.714-166.121 307.318 1.00 83.14 C HETATM 3377 C4 OLA A 603 -18.414-165.355 308.438 1.00 83.00 C HETATM 3378 C5 OLA A 603 -19.358-164.318 307.834 1.00 81.81 C HETATM 3379 C6 OLA A 603 -19.054-162.950 308.440 1.00 81.24 C HETATM 3380 C7 OLA A 603 -20.355-162.172 308.632 1.00 81.59 C HETATM 3381 C8 OLA A 603 -20.346-160.920 307.756 1.00 80.37 C HETATM 3382 C9 OLA A 603 -21.431-161.040 306.687 1.00 80.26 C HETATM 3383 C10 OLA A 603 -21.791-159.990 305.976 1.00 81.36 C HETATM 3384 C11 OLA A 603 -21.131-158.632 306.207 1.00 82.47 C HETATM 3385 C1 OLA A 604 -49.600-137.350 311.101 1.00 94.75 C HETATM 3386 O1 OLA A 604 -50.309-137.513 310.075 1.00 96.18 O HETATM 3387 O2 OLA A 604 -49.835-136.386 311.875 1.00 96.19 O HETATM 3388 C2 OLA A 604 -48.460-138.323 311.403 1.00 90.61 C HETATM 3389 C3 OLA A 604 -48.489-138.747 312.872 1.00 88.65 C HETATM 3390 C4 OLA A 604 -47.882-140.142 313.028 1.00 86.53 C HETATM 3391 C5 OLA A 604 -47.441-140.364 314.476 1.00 84.96 C HETATM 3392 C6 OLA A 604 -48.497-141.173 315.230 1.00 84.28 C HETATM 3393 C7 OLA A 604 -47.809-142.171 316.161 1.00 84.02 C HETATM 3394 C8 OLA A 604 -48.809-143.226 316.635 1.00 82.99 C HETATM 3395 C9 OLA A 604 -48.490-144.569 315.977 1.00 82.39 C HETATM 3396 C10 OLA A 604 -48.396-145.669 316.699 1.00 82.12 C HETATM 3397 C11 OLA A 604 -48.599-145.630 318.212 1.00 81.77 C HETATM 3398 C10 OLC A 605 -34.083-153.302 317.637 1.00 85.36 C HETATM 3399 C9 OLC A 605 -33.954-154.574 317.325 1.00 88.36 C HETATM 3400 C8 OLC A 605 -35.173-155.495 317.303 1.00 91.52 C HETATM 3401 C24 OLC A 605 -36.112-166.087 323.455 1.00107.11 C HETATM 3402 C7 OLC A 605 -35.416-156.078 318.695 1.00 93.31 C HETATM 3403 C6 OLC A 605 -34.244-156.972 319.098 1.00 95.37 C HETATM 3404 C5 OLC A 605 -34.640-158.442 318.969 1.00 96.76 C HETATM 3405 C4 OLC A 605 -33.665-159.316 319.758 1.00 97.76 C HETATM 3406 C3 OLC A 605 -33.956-160.790 319.479 1.00100.25 C HETATM 3407 C2 OLC A 605 -33.683-161.617 320.736 1.00103.02 C HETATM 3408 C21 OLC A 605 -34.504-164.971 321.895 1.00105.90 C HETATM 3409 C1 OLC A 605 -34.280-163.016 320.584 1.00105.19 C HETATM 3410 C22 OLC A 605 -34.773-165.361 323.350 1.00105.90 C HETATM 3411 O19 OLC A 605 -34.225-163.567 319.537 1.00105.79 O HETATM 3412 O25 OLC A 605 -36.082-167.245 322.665 1.00108.58 O HETATM 3413 O23 OLC A 605 -33.750-166.200 323.811 1.00104.25 O HETATM 3414 O20 OLC A 605 -34.890-163.641 321.681 1.00105.95 O HETATM 3415 C24 OLC A 606 -51.592-137.141 301.766 1.00105.58 C HETATM 3416 C6 OLC A 606 -59.424-140.554 296.605 1.00 86.73 C HETATM 3417 C5 OLC A 606 -58.413-139.655 297.315 1.00 88.58 C HETATM 3418 C4 OLC A 606 -57.106-140.417 297.522 1.00 91.15 C HETATM 3419 C3 OLC A 606 -56.311-139.789 298.667 1.00 94.47 C HETATM 3420 C2 OLC A 606 -55.115-139.025 298.102 1.00 99.20 C HETATM 3421 C21 OLC A 606 -51.881-138.904 300.005 1.00103.24 C HETATM 3422 C1 OLC A 606 -53.827-139.464 298.798 1.00102.60 C HETATM 3423 C22 OLC A 606 -51.163-137.607 300.376 1.00104.26 C HETATM 3424 O19 OLC A 606 -53.326-140.498 298.510 1.00103.76 O HETATM 3425 O25 OLC A 606 -50.725-136.134 302.214 1.00106.38 O HETATM 3426 O23 OLC A 606 -49.777-137.815 300.353 1.00104.45 O HETATM 3427 O20 OLC A 606 -53.235-138.641 299.764 1.00103.27 O HETATM 3428 C1 PEG A 607 -58.469-146.065 299.588 1.00106.17 C HETATM 3429 O1 PEG A 607 -58.247-147.429 299.823 1.00106.33 O HETATM 3430 C2 PEG A 607 -59.965-145.816 299.411 1.00106.44 C HETATM 3431 O2 PEG A 607 -60.240-144.464 299.645 1.00106.96 O HETATM 3432 C3 PEG A 607 -61.604-144.163 299.724 1.00106.07 C HETATM 3433 C4 PEG A 607 -61.816-142.695 299.358 1.00105.12 C HETATM 3434 O4 PEG A 607 -62.377-142.013 300.447 1.00104.37 O HETATM 3435 C1 CLR A 608 -50.574-143.627 310.905 1.00 63.31 C HETATM 3436 C2 CLR A 608 -50.565-142.216 310.320 1.00 62.00 C HETATM 3437 C3 CLR A 608 -51.568-142.177 309.173 1.00 60.29 C HETATM 3438 C4 CLR A 608 -52.975-142.305 309.763 1.00 60.10 C HETATM 3439 C5 CLR A 608 -53.051-143.618 310.530 1.00 61.86 C HETATM 3440 C6 CLR A 608 -54.169-144.284 310.514 1.00 62.78 C HETATM 3441 C7 CLR A 608 -54.332-145.663 311.099 1.00 64.11 C HETATM 3442 C8 CLR A 608 -53.366-145.908 312.270 1.00 64.48 C HETATM 3443 C9 CLR A 608 -51.964-145.402 311.910 1.00 65.26 C HETATM 3444 C10 CLR A 608 -51.953-143.944 311.492 1.00 63.65 C HETATM 3445 C11 CLR A 608 -50.991-145.618 313.063 1.00 64.08 C HETATM 3446 C12 CLR A 608 -50.888-147.111 313.382 1.00 63.61 C HETATM 3447 C13 CLR A 608 -52.271-147.680 313.717 1.00 61.71 C HETATM 3448 C14 CLR A 608 -53.214-147.408 312.504 1.00 62.69 C HETATM 3449 C15 CLR A 608 -54.478-148.174 312.916 1.00 61.27 C HETATM 3450 C16 CLR A 608 -53.906-149.467 313.564 1.00 59.53 C HETATM 3451 C17 CLR A 608 -52.404-149.201 313.849 1.00 61.32 C HETATM 3452 C18 CLR A 608 -52.866-146.976 314.943 1.00 58.77 C HETATM 3453 C19 CLR A 608 -52.152-143.087 312.745 1.00 63.46 C HETATM 3454 C20 CLR A 608 -52.038-149.795 315.223 1.00 62.46 C HETATM 3455 C21 CLR A 608 -50.560-149.618 315.593 1.00 59.32 C HETATM 3456 C22 CLR A 608 -52.301-151.302 315.170 1.00 68.59 C HETATM 3457 C23 CLR A 608 -51.281-151.952 314.230 1.00 71.64 C HETATM 3458 C24 CLR A 608 -51.518-153.461 314.141 1.00 72.54 C HETATM 3459 C25 CLR A 608 -50.343-154.121 313.416 1.00 72.94 C HETATM 3460 C26 CLR A 608 -50.699-155.570 313.081 1.00 73.28 C HETATM 3461 C27 CLR A 608 -49.110-154.108 314.323 1.00 71.62 C HETATM 3462 O1 CLR A 608 -51.423-140.941 308.467 1.00 60.43 O CONECT 1204 1258 CONECT 1258 1204 CONECT 3313 3314 3330 CONECT 3314 3313 3315 3316 CONECT 3315 3314 CONECT 3316 3314 3317 CONECT 3317 3316 3318 3319 CONECT 3318 3317 CONECT 3319 3317 3320 3330 CONECT 3320 3319 3321 CONECT 3321 3320 3322 3328 CONECT 3322 3321 3323 CONECT 3323 3322 3324 3325 CONECT 3324 3323 CONECT 3325 3323 3326 3327 CONECT 3326 3325 CONECT 3327 3325 3328 CONECT 3328 3321 3327 3329 CONECT 3329 3328 3330 3331 CONECT 3330 3313 3319 3329 CONECT 3331 3329 3332 CONECT 3332 3331 3333 3334 CONECT 3333 3332 CONECT 3334 3332 3335 3336 CONECT 3335 3334 CONECT 3336 3334 3337 3338 CONECT 3337 3336 CONECT 3338 3336 3339 CONECT 3339 3338 3340 CONECT 3340 3339 3341 3342 3343 CONECT 3341 3340 CONECT 3342 3340 CONECT 3343 3340 CONECT 3344 3345 3347 3349 CONECT 3345 3344 CONECT 3346 3350 3368 CONECT 3347 3344 3348 CONECT 3348 3347 3351 3359 CONECT 3349 3344 3355 3368 CONECT 3350 3346 3356 3357 3369 CONECT 3351 3348 3368 CONECT 3352 3353 3370 CONECT 3353 3352 3354 3358 CONECT 3354 3353 3355 CONECT 3355 3349 3354 3369 CONECT 3356 3350 CONECT 3357 3350 CONECT 3358 3353 CONECT 3359 3348 3360 3361 3362 CONECT 3360 3359 3363 CONECT 3361 3359 CONECT 3362 3359 CONECT 3363 3360 3364 CONECT 3364 3363 3365 CONECT 3365 3364 3366 CONECT 3366 3365 3367 CONECT 3367 3366 3371 CONECT 3368 3346 3349 3351 CONECT 3369 3350 3355 3370 CONECT 3370 3352 3369 CONECT 3371 3367 CONECT 3372 3373 3374 3375 CONECT 3373 3372 CONECT 3374 3372 CONECT 3375 3372 3376 CONECT 3376 3375 3377 CONECT 3377 3376 3378 CONECT 3378 3377 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3383 CONECT 3385 3386 3387 3388 CONECT 3386 3385 CONECT 3387 3385 CONECT 3388 3385 3389 CONECT 3389 3388 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 CONECT 3398 3399 CONECT 3399 3398 3400 CONECT 3400 3399 3402 CONECT 3401 3410 3412 CONECT 3402 3400 3403 CONECT 3403 3402 3404 CONECT 3404 3403 3405 CONECT 3405 3404 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3409 CONECT 3408 3410 3414 CONECT 3409 3407 3411 3414 CONECT 3410 3401 3408 3413 CONECT 3411 3409 CONECT 3412 3401 CONECT 3413 3410 CONECT 3414 3408 3409 CONECT 3415 3423 3425 CONECT 3416 3417 CONECT 3417 3416 3418 CONECT 3418 3417 3419 CONECT 3419 3418 3420 CONECT 3420 3419 3422 CONECT 3421 3423 3427 CONECT 3422 3420 3424 3427 CONECT 3423 3415 3421 3426 CONECT 3424 3422 CONECT 3425 3415 CONECT 3426 3423 CONECT 3427 3421 3422 CONECT 3428 3429 3430 CONECT 3429 3428 CONECT 3430 3428 3431 CONECT 3431 3430 3432 CONECT 3432 3431 3433 CONECT 3433 3432 3434 CONECT 3434 3433 CONECT 3435 3436 3444 CONECT 3436 3435 3437 CONECT 3437 3436 3438 3462 CONECT 3438 3437 3439 CONECT 3439 3438 3440 3444 CONECT 3440 3439 3441 CONECT 3441 3440 3442 CONECT 3442 3441 3443 3448 CONECT 3443 3442 3444 3445 CONECT 3444 3435 3439 3443 3453 CONECT 3445 3443 3446 CONECT 3446 3445 3447 CONECT 3447 3446 3448 3451 3452 CONECT 3448 3442 3447 3449 CONECT 3449 3448 3450 CONECT 3450 3449 3451 CONECT 3451 3447 3450 3454 CONECT 3452 3447 CONECT 3453 3444 CONECT 3454 3451 3455 3456 CONECT 3455 3454 CONECT 3456 3454 3457 CONECT 3457 3456 3458 CONECT 3458 3457 3459 CONECT 3459 3458 3460 3461 CONECT 3460 3459 CONECT 3461 3459 CONECT 3462 3437 MASTER 288 0 8 18 10 0 0 6 3461 1 152 34 END