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*** TRANSFERASE 05-DEC-14 4RWQ ***elNémo ID: 2401161742511318419Job options:ID = 2401161742511318419 JOBID = TRANSFERASE 05-DEC-14 4RWQ USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER TRANSFERASE 05-DEC-14 4RWQ TITLE CRYSTAL STRUCTURE OF THE APO-STATE OF PORCINE OAS1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 2'-5'-OLIGOADENYLATE SYNTHASE 1; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: (2-5')OLIGO(A) SYNTHASE 1, 2-5A SYNTHASE 1, P42 OAS; COMPND 5 EC: 2.7.7.84; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 3 ORGANISM_COMMON: PIGS,SWINE,WILD BOAR; SOURCE 4 ORGANISM_TAXID: 9823; SOURCE 5 GENE: OAS1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET9D KEYWDS INTERFERON-INDUCED, DSRNA-ACTIVATED, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR J.LOHOEFENER,N.STEINKE,P.KAY-FEDOROV,P.BARUCH,A.NIKULIN,S.TISHCHENKO, AUTHOR 2 D.J.MANSTEIN,R.FEDOROV REVDAT 1 20-MAY-15 4RWQ 0 JRNL AUTH J.LOHOFENER,N.STEINKE,P.KAY-FEDOROV,P.BARUCH,A.NIKULIN, JRNL AUTH 2 S.TISHCHENKO,D.J.MANSTEIN,R.FEDOROV JRNL TITL THE ACTIVATION MECHANISM OF 2'-5'-OLIGOADENYLATE SYNTHETASE JRNL TITL 2 GIVES NEW INSIGHTS INTO OAS/CGAS TRIGGERS OF INNATE JRNL TITL 3 IMMUNITY. JRNL REF STRUCTURE V. 23 851 2015 JRNL REFN ISSN 0969-2126 JRNL PMID 25892109 JRNL DOI 10.1016/J.STR.2015.03.012 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 15906 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.212 REMARK 3 R VALUE (WORKING SET) : 0.210 REMARK 3 FREE R VALUE : 0.260 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 793 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 45.5033 - 5.6301 1.00 2561 120 0.1807 0.2077 REMARK 3 2 5.6301 - 4.4701 1.00 2524 136 0.1989 0.2490 REMARK 3 3 4.4701 - 3.9054 1.00 2546 124 0.2046 0.2532 REMARK 3 4 3.9054 - 3.5485 1.00 2474 135 0.2320 0.3154 REMARK 3 5 3.5485 - 3.2942 1.00 2507 139 0.2597 0.3274 REMARK 3 6 3.2942 - 3.1000 1.00 2501 139 0.2822 0.3420 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.000 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.30 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 5746 REMARK 3 ANGLE : 0.660 7764 REMARK 3 CHIRALITY : 0.040 838 REMARK 3 PLANARITY : 0.004 1006 REMARK 3 DIHEDRAL : 12.495 2190 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain 'A' and (resid 1 through 22 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.9680 21.0452 16.9723 REMARK 3 T TENSOR REMARK 3 T11: 1.0362 T22: 1.4018 REMARK 3 T33: 1.0913 T12: -0.5237 REMARK 3 T13: -0.2274 T23: 0.3117 REMARK 3 L TENSOR REMARK 3 L11: 2.1744 L22: 2.2258 REMARK 3 L33: 6.5789 L12: 2.1010 REMARK 3 L13: -3.5712 L23: -3.1906 REMARK 3 S TENSOR REMARK 3 S11: -0.4156 S12: -0.9233 S13: 0.8171 REMARK 3 S21: -0.0647 S22: -0.3577 S23: -0.5021 REMARK 3 S31: -1.3717 S32: 2.0315 S33: 0.0002 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain 'A' and (resid 23 through 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.1811 6.9510 38.4206 REMARK 3 T TENSOR REMARK 3 T11: 0.4740 T22: 0.5139 REMARK 3 T33: 0.5448 T12: 0.1327 REMARK 3 T13: 0.0189 T23: -0.0898 REMARK 3 L TENSOR REMARK 3 L11: 6.2121 L22: 3.0501 REMARK 3 L33: 4.2730 L12: 2.9117 REMARK 3 L13: 1.1811 L23: 1.7716 REMARK 3 S TENSOR REMARK 3 S11: -0.1306 S12: -0.8559 S13: 0.4348 REMARK 3 S21: -0.1326 S22: -0.1312 S23: 0.2735 REMARK 3 S31: -0.2387 S32: -0.4206 S33: 0.0729 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain 'A' and (resid 112 through 132 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.9902 17.7833 40.1201 REMARK 3 T TENSOR REMARK 3 T11: 0.7955 T22: 0.7142 REMARK 3 T33: 0.7975 T12: 0.0555 REMARK 3 T13: 0.0442 T23: -0.1143 REMARK 3 L TENSOR REMARK 3 L11: 2.4441 L22: 8.8749 REMARK 3 L33: 5.5946 L12: 0.7957 REMARK 3 L13: -3.6434 L23: -0.8307 REMARK 3 S TENSOR REMARK 3 S11: -0.2575 S12: 0.2385 S13: 0.4173 REMARK 3 S21: -0.2096 S22: 0.5820 S23: -0.3493 REMARK 3 S31: -0.0784 S32: 0.0074 S33: -0.2336 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain 'A' and (resid 133 through 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.8711 1.9298 26.8039 REMARK 3 T TENSOR REMARK 3 T11: 0.5115 T22: 0.3807 REMARK 3 T33: 0.4850 T12: -0.0019 REMARK 3 T13: 0.0544 T23: 0.0902 REMARK 3 L TENSOR REMARK 3 L11: 3.4259 L22: 4.0576 REMARK 3 L33: 4.5676 L12: 0.3831 REMARK 3 L13: 0.4039 L23: 1.2540 REMARK 3 S TENSOR REMARK 3 S11: 0.0203 S12: -0.2151 S13: 0.4605 REMARK 3 S21: 0.2382 S22: -0.1814 S23: -0.2362 REMARK 3 S31: -0.1993 S32: 0.1069 S33: 0.1881 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: chain 'A' and (resid 202 through 346 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.7183 9.6907 9.5795 REMARK 3 T TENSOR REMARK 3 T11: 0.9653 T22: 0.8989 REMARK 3 T33: 0.7051 T12: -0.3176 REMARK 3 T13: -0.1851 T23: 0.4054 REMARK 3 L TENSOR REMARK 3 L11: 3.1528 L22: 4.5072 REMARK 3 L33: 2.5830 L12: 1.0686 REMARK 3 L13: -0.1605 L23: 0.5247 REMARK 3 S TENSOR REMARK 3 S11: -0.3879 S12: 0.9517 S13: 0.5726 REMARK 3 S21: -0.5697 S22: 0.0112 S23: 0.0536 REMARK 3 S31: -0.8418 S32: 0.5553 S33: 0.2477 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: chain 'B' and (resid 1 through 43 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.6650 -34.6842 29.5217 REMARK 3 T TENSOR REMARK 3 T11: 0.8463 T22: 1.2532 REMARK 3 T33: 0.8872 T12: -0.1599 REMARK 3 T13: -0.1711 T23: 0.4650 REMARK 3 L TENSOR REMARK 3 L11: 5.4235 L22: 2.0376 REMARK 3 L33: 1.0091 L12: 1.1388 REMARK 3 L13: 0.5539 L23: 0.0376 REMARK 3 S TENSOR REMARK 3 S11: 0.3579 S12: -1.7260 S13: -0.6935 REMARK 3 S21: 0.1425 S22: 0.0795 S23: 0.2981 REMARK 3 S31: 0.2683 S32: -0.3465 S33: -0.1826 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: chain 'B' and (resid 44 through 93 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.6910 -27.2618 13.3395 REMARK 3 T TENSOR REMARK 3 T11: 0.4954 T22: 1.0665 REMARK 3 T33: 0.5392 T12: -0.0788 REMARK 3 T13: -0.0633 T23: 0.0141 REMARK 3 L TENSOR REMARK 3 L11: 3.4528 L22: 5.2977 REMARK 3 L33: 4.3790 L12: -1.0894 REMARK 3 L13: 1.3663 L23: -1.4374 REMARK 3 S TENSOR REMARK 3 S11: 0.0030 S12: -0.1609 S13: -0.5249 REMARK 3 S21: 0.3257 S22: 0.4241 S23: -0.3278 REMARK 3 S31: -0.0587 S32: -0.6038 S33: -0.0025 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: chain 'B' and (resid 94 through 185 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.1763 -29.0775 13.3992 REMARK 3 T TENSOR REMARK 3 T11: 0.5541 T22: 0.8249 REMARK 3 T33: 0.6746 T12: -0.0724 REMARK 3 T13: -0.0130 T23: 0.0485 REMARK 3 L TENSOR REMARK 3 L11: 2.9362 L22: 3.6116 REMARK 3 L33: 3.4538 L12: -2.0795 REMARK 3 L13: 0.5683 L23: -1.4584 REMARK 3 S TENSOR REMARK 3 S11: 0.0417 S12: 0.1826 S13: -0.1610 REMARK 3 S21: -0.1060 S22: -0.2220 S23: -0.5747 REMARK 3 S31: 0.1995 S32: 0.7777 S33: 0.0900 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: chain 'B' and (resid 186 through 346 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.9877 -29.6421 15.0201 REMARK 3 T TENSOR REMARK 3 T11: 0.5578 T22: 0.5298 REMARK 3 T33: 0.7725 T12: -0.0931 REMARK 3 T13: -0.0852 T23: 0.0899 REMARK 3 L TENSOR REMARK 3 L11: 5.3294 L22: 3.6457 REMARK 3 L33: 4.2636 L12: 1.8458 REMARK 3 L13: -1.0280 L23: -1.9625 REMARK 3 S TENSOR REMARK 3 S11: 0.2720 S12: 0.1375 S13: -1.2899 REMARK 3 S21: 0.0932 S22: 0.0705 S23: 0.0203 REMARK 3 S31: 0.3885 S32: -0.4720 S33: -0.3092 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4RWQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-14. REMARK 100 THE RCSB ID CODE IS RCSB087890. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-JUL-13 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.87260 REMARK 200 MONOCHROMATOR : SILICON 111 CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SADABS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15919 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 46.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.39 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M (NH4)2SO4, 0.1 M SODIUM ACETATE REMARK 280 PH 5.5, 10% PEG 2000 MME, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 39.92000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.54000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.92000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 72.54000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN A 347 REMARK 465 LYS A 348 REMARK 465 ILE A 349 REMARK 465 GLY A 350 REMARK 465 SER A 351 REMARK 465 HIS A 352 REMARK 465 HIS A 353 REMARK 465 HIS A 354 REMARK 465 HIS A 355 REMARK 465 HIS A 356 REMARK 465 HIS A 357 REMARK 465 GLN B 347 REMARK 465 LYS B 348 REMARK 465 ILE B 349 REMARK 465 GLY B 350 REMARK 465 SER B 351 REMARK 465 HIS B 352 REMARK 465 HIS B 353 REMARK 465 HIS B 354 REMARK 465 HIS B 355 REMARK 465 HIS B 356 REMARK 465 HIS B 357 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 NH1 ARG B 72 OE2 GLU B 143 1.71 REMARK 500 NH1 ARG B 72 CD GLU B 143 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD2 ASP B 50 NH1 ARG B 92 2555 1.51 REMARK 500 OD2 ASP B 50 CZ ARG B 92 2555 1.55 REMARK 500 OD2 ASP B 50 NH2 ARG B 92 2555 1.63 REMARK 500 CD1 LEU B 69 OE1 GLN B 139 2556 1.83 REMARK 500 CD1 LEU B 69 NE2 GLN B 139 2556 1.90 REMARK 500 CG ASP B 50 NH1 ARG B 92 2555 1.96 REMARK 500 CD1 LEU B 69 CD GLN B 139 2556 2.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 3 -11.00 90.88 REMARK 500 ASP A 10 -66.58 -103.27 REMARK 500 LEU A 11 -59.06 69.40 REMARK 500 ASP A 17 -71.53 -89.51 REMARK 500 PHE A 45 -131.41 55.87 REMARK 500 GLN A 46 147.32 86.78 REMARK 500 THR A 67 -68.21 -126.85 REMARK 500 THR A 68 -71.39 -89.32 REMARK 500 LEU A 69 -70.59 -127.16 REMARK 500 GLU A 126 9.84 80.68 REMARK 500 ARG A 129 -68.58 -142.25 REMARK 500 ALA A 130 154.28 68.17 REMARK 500 THR A 221 -64.87 -105.15 REMARK 500 SER A 244 -73.86 -102.04 REMARK 500 ASP A 277 -162.35 -164.82 REMARK 500 LEU B 3 -124.50 66.70 REMARK 500 HIS B 18 -68.94 -128.36 REMARK 500 THR B 68 -120.21 67.16 REMARK 500 ARG B 70 -176.50 82.84 REMARK 500 ASP B 74 70.18 50.75 REMARK 500 ARG B 129 -76.70 -123.22 REMARK 500 GLN B 141 -4.15 66.42 REMARK 500 ASN B 224 -1.82 83.20 REMARK 500 ASN B 334 -142.66 52.76 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4RWN RELATED DB: PDB REMARK 900 RELATED ID: 4RWO RELATED DB: PDB REMARK 900 RELATED ID: 4RWP RELATED DB: PDB DBREF 4RWQ A 1 349 UNP Q29599 OAS1_PIG 1 349 DBREF 4RWQ B 1 349 UNP Q29599 OAS1_PIG 1 349 SEQADV 4RWQ GLY A 350 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ SER A 351 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS A 352 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS A 353 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS A 354 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS A 355 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS A 356 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS A 357 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ GLY B 350 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ SER B 351 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS B 352 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS B 353 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS B 354 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS B 355 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS B 356 UNP Q29599 EXPRESSION TAG SEQADV 4RWQ HIS B 357 UNP Q29599 EXPRESSION TAG SEQRES 1 A 357 MET GLU LEU ARG HIS THR PRO ALA ARG ASP LEU ASP LYS SEQRES 2 A 357 PHE ILE GLU ASP HIS LEU LEU PRO ASN THR CYS PHE ARG SEQRES 3 A 357 THR GLN VAL LYS GLU ALA ILE ASP ILE VAL CYS ARG PHE SEQRES 4 A 357 LEU LYS GLU ARG CYS PHE GLN GLY THR ALA ASP PRO VAL SEQRES 5 A 357 ARG VAL SER LYS VAL VAL LYS GLY GLY SER SER GLY LYS SEQRES 6 A 357 GLY THR THR LEU ARG GLY ARG SER ASP ALA ASP LEU VAL SEQRES 7 A 357 VAL PHE LEU THR LYS LEU THR SER PHE GLU ASP GLN LEU SEQRES 8 A 357 ARG ARG ARG GLY GLU PHE ILE GLN GLU ILE ARG ARG GLN SEQRES 9 A 357 LEU GLU ALA CYS GLN ARG GLU GLN LYS PHE LYS VAL THR SEQRES 10 A 357 PHE GLU VAL GLN SER PRO ARG ARG GLU ASN PRO ARG ALA SEQRES 11 A 357 LEU SER PHE VAL LEU SER SER PRO GLN LEU GLN GLN GLU SEQRES 12 A 357 VAL GLU PHE ASP VAL LEU PRO ALA PHE ASP ALA LEU GLY SEQRES 13 A 357 GLN TRP THR PRO GLY TYR LYS PRO ASN PRO GLU ILE TYR SEQRES 14 A 357 VAL GLN LEU ILE LYS GLU CYS LYS SER ARG GLY LYS GLU SEQRES 15 A 357 GLY GLU PHE SER THR CYS PHE THR GLU LEU GLN ARG ASP SEQRES 16 A 357 PHE LEU ARG ASN ARG PRO THR LYS LEU LYS SER LEU ILE SEQRES 17 A 357 ARG LEU VAL LYS HIS TRP TYR GLN THR CYS LYS LYS THR SEQRES 18 A 357 HIS GLY ASN LYS LEU PRO PRO GLN TYR ALA LEU GLU LEU SEQRES 19 A 357 LEU THR VAL TYR ALA TRP GLU GLN GLY SER ARG LYS THR SEQRES 20 A 357 ASP PHE SER THR ALA GLN GLY PHE GLN THR VAL LEU GLU SEQRES 21 A 357 LEU VAL LEU LYS HIS GLN LYS LEU CYS ILE PHE TRP GLU SEQRES 22 A 357 ALA TYR TYR ASP PHE THR ASN PRO VAL VAL GLY ARG CYS SEQRES 23 A 357 MET LEU GLN GLN LEU LYS LYS PRO ARG PRO VAL ILE LEU SEQRES 24 A 357 ASP PRO ALA ASP PRO THR GLY ASN VAL GLY GLY GLY ASP SEQRES 25 A 357 THR HIS SER TRP GLN ARG LEU ALA GLN GLU ALA ARG VAL SEQRES 26 A 357 TRP LEU GLY TYR PRO CYS CYS LYS ASN LEU ASP GLY SER SEQRES 27 A 357 LEU VAL GLY ALA TRP THR MET LEU GLN LYS ILE GLY SER SEQRES 28 A 357 HIS HIS HIS HIS HIS HIS SEQRES 1 B 357 MET GLU LEU ARG HIS THR PRO ALA ARG ASP LEU ASP LYS SEQRES 2 B 357 PHE ILE GLU ASP HIS LEU LEU PRO ASN THR CYS PHE ARG SEQRES 3 B 357 THR GLN VAL LYS GLU ALA ILE ASP ILE VAL CYS ARG PHE SEQRES 4 B 357 LEU LYS GLU ARG CYS PHE GLN GLY THR ALA ASP PRO VAL SEQRES 5 B 357 ARG VAL SER LYS VAL VAL LYS GLY GLY SER SER GLY LYS SEQRES 6 B 357 GLY THR THR LEU ARG GLY ARG SER ASP ALA ASP LEU VAL SEQRES 7 B 357 VAL PHE LEU THR LYS LEU THR SER PHE GLU ASP GLN LEU SEQRES 8 B 357 ARG ARG ARG GLY GLU PHE ILE GLN GLU ILE ARG ARG GLN SEQRES 9 B 357 LEU GLU ALA CYS GLN ARG GLU GLN LYS PHE LYS VAL THR SEQRES 10 B 357 PHE GLU VAL GLN SER PRO ARG ARG GLU ASN PRO ARG ALA SEQRES 11 B 357 LEU SER PHE VAL LEU SER SER PRO GLN LEU GLN GLN GLU SEQRES 12 B 357 VAL GLU PHE ASP VAL LEU PRO ALA PHE ASP ALA LEU GLY SEQRES 13 B 357 GLN TRP THR PRO GLY TYR LYS PRO ASN PRO GLU ILE TYR SEQRES 14 B 357 VAL GLN LEU ILE LYS GLU CYS LYS SER ARG GLY LYS GLU SEQRES 15 B 357 GLY GLU PHE SER THR CYS PHE THR GLU LEU GLN ARG ASP SEQRES 16 B 357 PHE LEU ARG ASN ARG PRO THR LYS LEU LYS SER LEU ILE SEQRES 17 B 357 ARG LEU VAL LYS HIS TRP TYR GLN THR CYS LYS LYS THR SEQRES 18 B 357 HIS GLY ASN LYS LEU PRO PRO GLN TYR ALA LEU GLU LEU SEQRES 19 B 357 LEU THR VAL TYR ALA TRP GLU GLN GLY SER ARG LYS THR SEQRES 20 B 357 ASP PHE SER THR ALA GLN GLY PHE GLN THR VAL LEU GLU SEQRES 21 B 357 LEU VAL LEU LYS HIS GLN LYS LEU CYS ILE PHE TRP GLU SEQRES 22 B 357 ALA TYR TYR ASP PHE THR ASN PRO VAL VAL GLY ARG CYS SEQRES 23 B 357 MET LEU GLN GLN LEU LYS LYS PRO ARG PRO VAL ILE LEU SEQRES 24 B 357 ASP PRO ALA ASP PRO THR GLY ASN VAL GLY GLY GLY ASP SEQRES 25 B 357 THR HIS SER TRP GLN ARG LEU ALA GLN GLU ALA ARG VAL SEQRES 26 B 357 TRP LEU GLY TYR PRO CYS CYS LYS ASN LEU ASP GLY SER SEQRES 27 B 357 LEU VAL GLY ALA TRP THR MET LEU GLN LYS ILE GLY SER SEQRES 28 B 357 HIS HIS HIS HIS HIS HIS FORMUL 3 HOH *(H2 O) HELIX 1 1 LEU A 11 HIS A 18 1 8 HELIX 2 2 ASN A 22 CYS A 44 1 23 HELIX 3 3 GLU A 88 ARG A 93 1 6 HELIX 4 4 ARG A 93 GLN A 112 1 20 HELIX 5 5 ASN A 165 ARG A 179 1 15 HELIX 6 6 PHE A 185 CYS A 188 5 4 HELIX 7 7 PHE A 189 ASN A 199 1 11 HELIX 8 8 PRO A 201 GLY A 223 1 23 HELIX 9 9 ASN A 224 LEU A 226 5 3 HELIX 10 10 PRO A 228 GLN A 242 1 15 HELIX 11 11 SER A 250 LYS A 264 1 15 HELIX 12 12 HIS A 265 LYS A 267 5 3 HELIX 13 13 ASN A 280 LYS A 292 1 13 HELIX 14 14 ASP A 312 TRP A 326 1 15 HELIX 15 15 TYR A 329 LYS A 333 5 5 HELIX 16 16 GLU B 2 THR B 6 5 5 HELIX 17 17 ASP B 10 HIS B 18 1 9 HELIX 18 18 ASN B 22 CYS B 44 1 23 HELIX 19 19 GLU B 88 ARG B 93 1 6 HELIX 20 20 ARG B 93 GLN B 112 1 20 HELIX 21 21 ASN B 165 GLY B 180 1 16 HELIX 22 22 PHE B 185 CYS B 188 5 4 HELIX 23 23 PHE B 189 ARG B 198 1 10 HELIX 24 24 PRO B 201 GLY B 223 1 23 HELIX 25 25 PRO B 228 GLN B 242 1 15 HELIX 26 26 SER B 250 LYS B 264 1 15 HELIX 27 27 HIS B 265 LYS B 267 5 3 HELIX 28 28 ASN B 280 LYS B 292 1 13 HELIX 29 29 ASP B 312 LEU B 327 1 16 HELIX 30 30 TYR B 329 ASN B 334 1 6 SHEET 1 A 5 VAL A 54 LYS A 65 0 SHEET 2 A 5 ARG A 72 LEU A 81 -1 O ASP A 76 N GLY A 60 SHEET 3 A 5 GLN A 142 VAL A 148 1 O ASP A 147 N ALA A 75 SHEET 4 A 5 PHE A 133 SER A 137 -1 N LEU A 135 O VAL A 144 SHEET 5 A 5 THR A 117 VAL A 120 -1 N GLU A 119 O VAL A 134 SHEET 1 B 3 VAL A 54 LYS A 65 0 SHEET 2 B 3 ARG A 72 LEU A 81 -1 O ASP A 76 N GLY A 60 SHEET 3 B 3 ALA A 151 PHE A 152 1 O ALA A 151 N VAL A 79 SHEET 1 C 3 CYS A 269 ILE A 270 0 SHEET 2 C 3 VAL A 297 LEU A 299 1 O LEU A 299 N ILE A 270 SHEET 3 C 3 ASN A 307 VAL A 308 -1 O VAL A 308 N ILE A 298 SHEET 1 D 5 VAL B 54 LYS B 59 0 SHEET 2 D 5 ASP B 76 LEU B 81 -1 O VAL B 78 N VAL B 58 SHEET 3 D 5 GLU B 143 PHE B 152 1 O LEU B 149 N LEU B 77 SHEET 4 D 5 SER B 132 SER B 136 -1 N LEU B 135 O VAL B 144 SHEET 5 D 5 THR B 117 VAL B 120 -1 N GLU B 119 O VAL B 134 SHEET 1 E 3 CYS B 269 ILE B 270 0 SHEET 2 E 3 VAL B 297 ASP B 300 1 O VAL B 297 N ILE B 270 SHEET 3 E 3 ASP B 303 ASN B 307 -1 O GLY B 306 N ASP B 300 CISPEP 1 ARG A 295 PRO A 296 0 0.99 CISPEP 2 ASP B 50 PRO B 51 0 -27.23 CISPEP 3 ARG B 295 PRO B 296 0 2.10 CRYST1 79.840 145.080 80.140 90.00 106.40 90.00 C 1 2 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012525 0.000000 0.003686 0.00000 SCALE2 0.000000 0.006893 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013007 0.00000 ATOM 1 N MET A 1 -11.523 26.386 18.364 1.00127.09 N ANISOU 1 N MET A 1 16012 17207 15069 -7370 -3168 2076 N ATOM 2 CA MET A 1 -12.164 27.670 18.103 1.00140.74 C ANISOU 2 CA MET A 1 18411 18117 16945 -7589 -3210 1813 C ATOM 3 C MET A 1 -13.670 27.515 17.909 1.00154.04 C ANISOU 3 C MET A 1 20429 19171 18926 -6949 -3106 1702 C ATOM 4 O MET A 1 -14.287 26.615 18.477 1.00154.28 O ANISOU 4 O MET A 1 20267 19378 18975 -6454 -3047 1662 O ATOM 5 CB MET A 1 -11.536 28.352 16.883 1.00137.62 C ANISOU 5 CB MET A 1 18148 17527 16616 -7988 -3231 2009 C ATOM 6 CG MET A 1 -10.796 27.414 15.942 1.00130.19 C ANISOU 6 CG MET A 1 16693 17091 15683 -7859 -3157 2437 C ATOM 7 SD MET A 1 -9.635 28.295 14.884 1.00127.37 S ANISOU 7 SD MET A 1 16382 16744 15271 -8542 -3225 2645 S ATOM 8 CE MET A 1 -8.863 26.930 14.022 1.00111.01 C ANISOU 8 CE MET A 1 13662 15321 13197 -8241 -3051 3154 C ATOM 9 N GLU A 2 -14.256 28.398 17.105 1.00164.03 N ANISOU 9 N GLU A 2 22178 19732 20414 -6965 -3077 1687 N ATOM 10 CA GLU A 2 -15.689 28.370 16.833 1.00165.72 C ANISOU 10 CA GLU A 2 22684 19379 20904 -6392 -2985 1663 C ATOM 11 C GLU A 2 -16.066 27.070 16.138 1.00160.34 C ANISOU 11 C GLU A 2 21626 18985 20310 -5889 -2918 1943 C ATOM 12 O GLU A 2 -17.121 26.494 16.399 1.00163.25 O ANISOU 12 O GLU A 2 21997 19255 20777 -5375 -2856 1907 O ATOM 13 CB GLU A 2 -16.098 29.569 15.976 1.00172.92 C ANISOU 13 CB GLU A 2 24118 19560 22022 -6529 -2951 1702 C ATOM 14 CG GLU A 2 -15.167 30.765 16.096 1.00177.95 C ANISOU 14 CG GLU A 2 25064 20034 22514 -7242 -2993 1556 C ATOM 15 CD GLU A 2 -15.771 31.900 16.900 1.00183.70 C ANISOU 15 CD GLU A 2 26423 20109 23265 -7343 -2887 1224 C ATOM 16 OE1 GLU A 2 -16.581 31.624 17.809 1.00182.08 O ANISOU 16 OE1 GLU A 2 26281 19817 23086 -6960 -2820 1037 O ATOM 17 OE2 GLU A 2 -15.435 33.071 16.623 1.00190.42 O ANISOU 17 OE2 GLU A 2 27740 20509 24103 -7806 -2834 1150 O ATOM 18 N LEU A 3 -15.190 26.642 15.235 1.00154.37 N ANISOU 18 N LEU A 3 20586 18569 19500 -6074 -2903 2224 N ATOM 19 CA LEU A 3 -15.303 25.380 14.505 1.00144.43 C ANISOU 19 CA LEU A 3 19011 17608 18258 -5713 -2774 2501 C ATOM 20 C LEU A 3 -16.056 25.536 13.192 1.00139.26 C ANISOU 20 C LEU A 3 18608 16506 17798 -5578 -2736 2699 C ATOM 21 O LEU A 3 -16.050 24.636 12.356 1.00133.91 O ANISOU 21 O LEU A 3 17761 16016 17103 -5425 -2612 2943 O ATOM 22 CB LEU A 3 -15.945 24.289 15.372 1.00135.57 C ANISOU 22 CB LEU A 3 17676 16752 17081 -5214 -2688 2407 C ATOM 23 CG LEU A 3 -17.428 23.979 15.151 1.00125.94 C ANISOU 23 CG LEU A 3 16665 15161 16024 -4727 -2637 2389 C ATOM 24 CD1 LEU A 3 -17.586 22.632 14.463 1.00108.94 C ANISOU 24 CD1 LEU A 3 14283 13295 13814 -4435 -2454 2631 C ATOM 25 CD2 LEU A 3 -18.194 24.013 16.464 1.00133.99 C ANISOU 25 CD2 LEU A 3 17761 16105 17044 -4449 -2671 2090 C ATOM 26 N ARG A 4 -16.685 26.687 12.999 1.00139.92 N ANISOU 26 N ARG A 4 19114 16002 18049 -5654 -2815 2618 N ATOM 27 CA ARG A 4 -17.237 27.008 11.700 1.00141.85 C ANISOU 27 CA ARG A 4 19568 15870 18459 -5619 -2806 2866 C ATOM 28 C ARG A 4 -16.044 27.113 10.770 1.00154.47 C ANISOU 28 C ARG A 4 21058 17649 19986 -6062 -2807 3061 C ATOM 29 O ARG A 4 -16.072 26.645 9.632 1.00155.99 O ANISOU 29 O ARG A 4 21192 17880 20196 -6044 -2742 3330 O ATOM 30 CB ARG A 4 -17.995 28.334 11.749 1.00136.32 C ANISOU 30 CB ARG A 4 19334 14509 17951 -5617 -2849 2782 C ATOM 31 CG ARG A 4 -18.819 28.627 10.507 1.00131.05 C ANISOU 31 CG ARG A 4 18846 13483 17464 -5474 -2842 3094 C ATOM 32 CD ARG A 4 -18.855 30.118 10.211 1.00138.79 C ANISOU 32 CD ARG A 4 20267 13863 18602 -5699 -2847 3105 C ATOM 33 NE ARG A 4 -19.941 30.792 10.915 1.00140.37 N ANISOU 33 NE ARG A 4 20782 13591 18962 -5350 -2772 3000 N ATOM 34 CZ ARG A 4 -20.681 31.764 10.393 1.00143.08 C ANISOU 34 CZ ARG A 4 21470 13376 19517 -5213 -2702 3196 C ATOM 35 NH1 ARG A 4 -20.454 32.184 9.158 1.00142.03 N ANISOU 35 NH1 ARG A 4 21410 13102 19453 -5428 -2734 3490 N ATOM 36 NH2 ARG A 4 -21.648 32.319 11.108 1.00147.73 N ANISOU 36 NH2 ARG A 4 22332 13549 20251 -4841 -2573 3125 N ATOM 37 N HIS A 5 -14.992 27.742 11.285 1.00155.31 N ANISOU 37 N HIS A 5 21145 17883 19982 -6499 -2875 2923 N ATOM 38 CA HIS A 5 -13.758 27.962 10.540 1.00153.51 C ANISOU 38 CA HIS A 5 20793 17864 19669 -6970 -2888 3101 C ATOM 39 C HIS A 5 -12.714 26.873 10.770 1.00139.41 C ANISOU 39 C HIS A 5 18482 16807 17679 -6998 -2799 3237 C ATOM 40 O HIS A 5 -11.674 26.856 10.118 1.00137.77 O ANISOU 40 O HIS A 5 18091 16870 17385 -7258 -2752 3426 O ATOM 41 CB HIS A 5 -13.170 29.335 10.886 1.00165.03 C ANISOU 41 CB HIS A 5 22536 19090 21077 -7442 -2983 2894 C ATOM 42 CG HIS A 5 -14.199 30.351 11.275 1.00171.16 C ANISOU 42 CG HIS A 5 23841 19171 22020 -7384 -3008 2692 C ATOM 43 ND1 HIS A 5 -15.103 30.140 12.293 1.00168.08 N ANISOU 43 ND1 HIS A 5 23526 18673 21662 -7007 -2981 2481 N ATOM 44 CD2 HIS A 5 -14.474 31.579 10.776 1.00177.84 C ANISOU 44 CD2 HIS A 5 25132 19456 22983 -7433 -2955 2639 C ATOM 45 CE1 HIS A 5 -15.887 31.197 12.409 1.00170.67 C ANISOU 45 CE1 HIS A 5 24363 18334 22149 -6950 -2935 2362 C ATOM 46 NE2 HIS A 5 -15.527 32.084 11.500 1.00177.29 N ANISOU 46 NE2 HIS A 5 25464 18840 23058 -7279 -2932 2488 N ATOM 47 N THR A 6 -12.991 25.962 11.693 1.00134.04 N ANISOU 47 N THR A 6 17552 16462 16916 -6636 -2734 3147 N ATOM 48 CA THR A 6 -12.047 24.894 11.984 1.00131.42 C ANISOU 48 CA THR A 6 16708 16826 16398 -6581 -2598 3326 C ATOM 49 C THR A 6 -11.864 24.043 10.739 1.00122.47 C ANISOU 49 C THR A 6 15468 15776 15291 -6433 -2369 3660 C ATOM 50 O THR A 6 -12.819 23.451 10.246 1.00135.56 O ANISOU 50 O THR A 6 17283 17195 17029 -6082 -2253 3694 O ATOM 51 CB THR A 6 -12.530 24.018 13.150 1.00131.09 C ANISOU 51 CB THR A 6 16459 17070 16277 -6152 -2537 3182 C ATOM 52 OG1 THR A 6 -12.663 24.823 14.326 1.00137.20 O ANISOU 52 OG1 THR A 6 17366 17765 16997 -6338 -2729 2860 O ATOM 53 CG2 THR A 6 -11.535 22.904 13.419 1.00130.32 C ANISOU 53 CG2 THR A 6 15822 17697 15996 -6046 -2345 3437 C ATOM 54 N PRO A 7 -10.642 23.990 10.218 1.00112.35 N ANISOU 54 N PRO A 7 13933 14836 13917 -6733 -2288 3916 N ATOM 55 CA PRO A 7 -10.423 23.321 8.930 1.00117.77 C ANISOU 55 CA PRO A 7 14610 15517 14619 -6615 -2030 4203 C ATOM 56 C PRO A 7 -10.638 21.810 9.001 1.00116.34 C ANISOU 56 C PRO A 7 14228 15614 14363 -6165 -1690 4372 C ATOM 57 O PRO A 7 -10.884 21.270 10.080 1.00104.91 O ANISOU 57 O PRO A 7 12595 14418 12849 -5865 -1665 4249 O ATOM 58 CB PRO A 7 -8.955 23.642 8.610 1.00 99.29 C ANISOU 58 CB PRO A 7 12007 13558 12161 -6883 -1999 4358 C ATOM 59 CG PRO A 7 -8.595 24.792 9.505 1.00114.72 C ANISOU 59 CG PRO A 7 13972 15559 14058 -7326 -2314 4154 C ATOM 60 CD PRO A 7 -9.404 24.588 10.743 1.00118.75 C ANISOU 60 CD PRO A 7 14478 16063 14578 -7205 -2419 3950 C ATOM 61 N ALA A 8 -10.535 21.141 7.856 1.00127.27 N ANISOU 61 N ALA A 8 15700 16934 15722 -5946 -1393 4510 N ATOM 62 CA ALA A 8 -10.732 19.696 7.792 1.00126.67 C ANISOU 62 CA ALA A 8 15545 17033 15549 -5514 -986 4630 C ATOM 63 C ALA A 8 -9.423 18.923 7.909 1.00131.87 C ANISOU 63 C ALA A 8 15787 18228 16090 -5371 -645 4906 C ATOM 64 O ALA A 8 -9.433 17.700 8.048 1.00119.75 O ANISOU 64 O ALA A 8 14161 16868 14469 -4955 -248 5004 O ATOM 65 CB ALA A 8 -11.441 19.320 6.500 1.00120.15 C ANISOU 65 CB ALA A 8 15107 15809 14735 -5291 -800 4514 C ATOM 66 N ARG A 9 -8.307 19.639 7.838 1.00143.39 N ANISOU 66 N ARG A 9 17010 19933 17540 -5681 -779 5023 N ATOM 67 CA ARG A 9 -6.989 19.020 7.919 1.00141.95 C ANISOU 67 CA ARG A 9 16381 20302 17252 -5534 -483 5332 C ATOM 68 C ARG A 9 -6.730 18.350 9.264 1.00141.63 C ANISOU 68 C ARG A 9 15871 20846 17097 -5338 -393 5508 C ATOM 69 O ARG A 9 -6.147 17.270 9.321 1.00146.54 O ANISOU 69 O ARG A 9 16237 21792 17650 -4889 28 5732 O ATOM 70 CB ARG A 9 -5.891 20.041 7.609 1.00150.34 C ANISOU 70 CB ARG A 9 17277 21545 18300 -5961 -710 5419 C ATOM 71 CG ARG A 9 -5.372 19.980 6.180 1.00153.48 C ANISOU 71 CG ARG A 9 17861 21709 18748 -5887 -475 5472 C ATOM 72 CD ARG A 9 -3.955 19.432 6.121 1.00159.80 C ANISOU 72 CD ARG A 9 18207 23046 19464 -5735 -176 5824 C ATOM 73 NE ARG A 9 -2.956 20.475 6.328 1.00164.45 N ANISOU 73 NE ARG A 9 18510 23994 19980 -6208 -507 5938 N ATOM 74 CZ ARG A 9 -1.813 20.297 6.982 1.00167.09 C ANISOU 74 CZ ARG A 9 18284 25027 20175 -6218 -478 6255 C ATOM 75 NH1 ARG A 9 -1.518 19.112 7.497 1.00161.19 N ANISOU 75 NH1 ARG A 9 17192 24672 19382 -5716 -117 6504 N ATOM 76 NH2 ARG A 9 -0.964 21.306 7.121 1.00172.21 N ANISOU 76 NH2 ARG A 9 18734 25986 20713 -6708 -805 6318 N ATOM 77 N ASP A 10 -7.151 18.994 10.347 1.00133.94 N ANISOU 77 N ASP A 10 14800 19982 16107 -5646 -769 5378 N ATOM 78 CA ASP A 10 -6.945 18.415 11.666 1.00128.82 C ANISOU 78 CA ASP A 10 13727 19886 15333 -5369 -733 5415 C ATOM 79 C ASP A 10 -8.230 17.812 12.208 1.00134.50 C ANISOU 79 C ASP A 10 14711 20303 16091 -4931 -693 5107 C ATOM 80 O ASP A 10 -8.337 16.598 12.366 1.00136.59 O ANISOU 80 O ASP A 10 14864 20738 16297 -4448 -290 5268 O ATOM 81 CB ASP A 10 -6.437 19.484 12.630 1.00123.81 C ANISOU 81 CB ASP A 10 12852 19587 14602 -5839 -1190 5272 C ATOM 82 CG ASP A 10 -7.184 20.792 12.490 1.00116.06 C ANISOU 82 CG ASP A 10 12386 17975 13735 -6246 -1609 4832 C ATOM 83 OD1 ASP A 10 -8.398 20.815 12.774 1.00104.98 O ANISOU 83 OD1 ASP A 10 11348 16105 12433 -6014 -1701 4488 O ATOM 84 OD2 ASP A 10 -6.560 21.798 12.095 1.00115.76 O ANISOU 84 OD2 ASP A 10 12391 17908 13683 -6785 -1820 4854 O ATOM 85 N LEU A 11 -9.210 18.661 12.484 1.00136.62 N ANISOU 85 N LEU A 11 15346 20109 16455 -5090 -1076 4681 N ATOM 86 CA LEU A 11 -10.531 18.191 12.871 1.00128.17 C ANISOU 86 CA LEU A 11 14557 18704 15436 -4706 -1063 4395 C ATOM 87 C LEU A 11 -10.511 17.552 14.251 1.00120.03 C ANISOU 87 C LEU A 11 13185 18135 14288 -4385 -1024 4343 C ATOM 88 O LEU A 11 -11.210 17.987 15.162 1.00112.10 O ANISOU 88 O LEU A 11 12287 17007 13301 -4374 -1303 4003 O ATOM 89 CB LEU A 11 -11.071 17.198 11.841 1.00119.39 C ANISOU 89 CB LEU A 11 13713 17309 14339 -4409 -664 4531 C ATOM 90 CG LEU A 11 -12.571 17.276 11.554 1.00 96.92 C ANISOU 90 CG LEU A 11 11343 13899 11582 -4298 -783 4243 C ATOM 91 CD1 LEU A 11 -13.067 18.708 11.662 1.00 90.91 C ANISOU 91 CD1 LEU A 11 10807 12767 10968 -4622 -1262 3973 C ATOM 92 CD2 LEU A 11 -12.885 16.702 10.182 1.00 89.95 C ANISOU 92 CD2 LEU A 11 10782 12719 10676 -4302 -475 4414 C ATOM 93 N ASP A 12 -9.700 16.509 14.393 1.00120.20 N ANISOU 93 N ASP A 12 12800 18682 14187 -4104 -643 4710 N ATOM 94 CA ASP A 12 -9.643 15.752 15.634 1.00110.79 C ANISOU 94 CA ASP A 12 11252 17971 12874 -3742 -541 4739 C ATOM 95 C ASP A 12 -9.160 16.607 16.791 1.00109.85 C ANISOU 95 C ASP A 12 10820 18266 12651 -4092 -961 4616 C ATOM 96 O ASP A 12 -9.703 16.537 17.890 1.00119.28 O ANISOU 96 O ASP A 12 11985 19543 13794 -3947 -1113 4361 O ATOM 97 CB ASP A 12 -8.725 14.540 15.481 1.00110.47 C ANISOU 97 CB ASP A 12 10811 18436 12726 -3372 4 5255 C ATOM 98 CG ASP A 12 -9.047 13.718 14.253 1.00117.39 C ANISOU 98 CG ASP A 12 12059 18891 13653 -3124 491 5395 C ATOM 99 OD1 ASP A 12 -9.130 14.303 13.154 1.00112.67 O ANISOU 99 OD1 ASP A 12 11786 17878 13144 -3449 411 5355 O ATOM 100 OD2 ASP A 12 -9.214 12.488 14.384 1.00122.87 O ANISOU 100 OD2 ASP A 12 12749 19660 14275 -2631 975 5546 O ATOM 101 N LYS A 13 -8.146 17.426 16.543 1.00106.04 N ANISOU 101 N LYS A 13 10132 18047 12112 -4598 -1144 4787 N ATOM 102 CA LYS A 13 -7.604 18.259 17.607 1.00116.62 C ANISOU 102 CA LYS A 13 11202 19826 13284 -5054 -1529 4684 C ATOM 103 C LYS A 13 -8.691 19.113 18.249 1.00124.60 C ANISOU 103 C LYS A 13 12683 20308 14353 -5221 -1890 4109 C ATOM 104 O LYS A 13 -8.580 19.505 19.410 1.00138.97 O ANISOU 104 O LYS A 13 14363 22434 16007 -5450 -2133 3932 O ATOM 105 CB LYS A 13 -6.480 19.143 17.062 1.00118.79 C ANISOU 105 CB LYS A 13 11309 20343 13484 -5669 -1689 4904 C ATOM 106 CG LYS A 13 -5.415 18.368 16.297 1.00106.21 C ANISOU 106 CG LYS A 13 9277 19215 11861 -5491 -1295 5506 C ATOM 107 CD LYS A 13 -4.433 19.297 15.600 1.00110.09 C ANISOU 107 CD LYS A 13 9677 19844 12309 -6108 -1459 5695 C ATOM 108 CE LYS A 13 -3.482 18.517 14.703 1.00111.39 C ANISOU 108 CE LYS A 13 9554 20292 12479 -5773 -1032 6214 C ATOM 109 NZ LYS A 13 -2.590 19.414 13.916 1.00114.88 N ANISOU 109 NZ LYS A 13 10045 20721 12883 -6213 -1206 6279 N ATOM 110 N PHE A 14 -9.743 19.398 17.488 1.00118.50 N ANISOU 110 N PHE A 14 12469 18756 13800 -5110 -1900 3849 N ATOM 111 CA PHE A 14 -10.881 20.139 18.014 1.00121.49 C ANISOU 111 CA PHE A 14 13309 18580 14271 -5153 -2160 3365 C ATOM 112 C PHE A 14 -11.751 19.237 18.882 1.00124.00 C ANISOU 112 C PHE A 14 13595 18940 14581 -4610 -2049 3209 C ATOM 113 O PHE A 14 -12.234 19.653 19.936 1.00129.52 O ANISOU 113 O PHE A 14 14400 19580 15231 -4661 -2251 2885 O ATOM 114 CB PHE A 14 -11.714 20.740 16.879 1.00116.61 C ANISOU 114 CB PHE A 14 13235 17184 13888 -5189 -2197 3231 C ATOM 115 CG PHE A 14 -12.954 21.447 17.350 1.00111.61 C ANISOU 115 CG PHE A 14 13063 15964 13378 -5130 -2392 2814 C ATOM 116 CD1 PHE A 14 -12.888 22.749 17.816 1.00120.48 C ANISOU 116 CD1 PHE A 14 14450 16843 14483 -5593 -2650 2551 C ATOM 117 CD2 PHE A 14 -14.183 20.808 17.331 1.00101.93 C ANISOU 117 CD2 PHE A 14 12026 14431 12270 -4622 -2281 2704 C ATOM 118 CE1 PHE A 14 -14.026 23.402 18.253 1.00122.34 C ANISOU 118 CE1 PHE A 14 15136 16503 14846 -5487 -2754 2205 C ATOM 119 CE2 PHE A 14 -15.323 21.455 17.769 1.00 98.22 C ANISOU 119 CE2 PHE A 14 11941 13455 11924 -4525 -2431 2380 C ATOM 120 CZ PHE A 14 -15.244 22.753 18.230 1.00108.90 C ANISOU 120 CZ PHE A 14 13558 14532 13286 -4927 -2648 2140 C ATOM 121 N ILE A 15 -11.950 18.004 18.429 1.00122.62 N ANISOU 121 N ILE A 15 13312 18840 14436 -4113 -1698 3433 N ATOM 122 CA ILE A 15 -12.748 17.030 19.166 1.00119.19 C ANISOU 122 CA ILE A 15 12851 18456 13979 -3585 -1542 3316 C ATOM 123 C ILE A 15 -12.076 16.665 20.485 1.00120.68 C ANISOU 123 C ILE A 15 12550 19343 13961 -3540 -1566 3395 C ATOM 124 O ILE A 15 -12.730 16.578 21.525 1.00123.10 O ANISOU 124 O ILE A 15 12895 19648 14228 -3370 -1677 3118 O ATOM 125 CB ILE A 15 -12.980 15.747 18.342 1.00110.48 C ANISOU 125 CB ILE A 15 11781 17297 12901 -3129 -1090 3566 C ATOM 126 CG1 ILE A 15 -13.685 16.076 17.026 1.00110.31 C ANISOU 126 CG1 ILE A 15 12237 16641 13035 -3231 -1082 3508 C ATOM 127 CG2 ILE A 15 -13.793 14.734 19.137 1.00 98.94 C ANISOU 127 CG2 ILE A 15 10313 15891 11390 -2614 -914 3437 C ATOM 128 CD1 ILE A 15 -13.923 14.872 16.142 1.00102.51 C ANISOU 128 CD1 ILE A 15 11373 15561 12014 -2906 -623 3727 C ATOM 129 N GLU A 16 -10.764 16.463 20.434 1.00121.76 N ANISOU 129 N GLU A 16 12202 20105 13955 -3700 -1461 3805 N ATOM 130 CA GLU A 16 -9.995 16.066 21.608 1.00128.89 C ANISOU 130 CA GLU A 16 12540 21804 14628 -3675 -1469 4004 C ATOM 131 C GLU A 16 -9.980 17.161 22.674 1.00134.91 C ANISOU 131 C GLU A 16 13336 22677 15249 -4201 -1924 3664 C ATOM 132 O GLU A 16 -9.866 16.875 23.866 1.00147.75 O ANISOU 132 O GLU A 16 14660 24788 16688 -4148 -1997 3642 O ATOM 133 CB GLU A 16 -8.563 15.703 21.204 1.00139.27 C ANISOU 133 CB GLU A 16 13298 23797 15823 -3759 -1253 4599 C ATOM 134 CG GLU A 16 -7.726 15.105 22.324 1.00146.74 C ANISOU 134 CG GLU A 16 13560 25675 16521 -3645 -1191 4953 C ATOM 135 CD GLU A 16 -6.346 14.682 21.859 1.00155.16 C ANISOU 135 CD GLU A 16 14035 27431 17486 -3642 -915 5633 C ATOM 136 OE1 GLU A 16 -5.535 14.255 22.708 1.00159.30 O ANISOU 136 OE1 GLU A 16 13913 28821 17791 -3582 -868 6034 O ATOM 137 OE2 GLU A 16 -6.073 14.774 20.643 1.00156.56 O ANISOU 137 OE2 GLU A 16 14379 27308 17797 -3693 -735 5798 O ATOM 138 N ASP A 17 -10.105 18.413 22.243 1.00123.07 N ANISOU 138 N ASP A 17 12238 20703 13819 -4720 -2201 3399 N ATOM 139 CA ASP A 17 -10.065 19.541 23.168 1.00130.06 C ANISOU 139 CA ASP A 17 13275 21597 14543 -5298 -2570 3055 C ATOM 140 C ASP A 17 -11.444 19.909 23.716 1.00134.48 C ANISOU 140 C ASP A 17 14383 21480 15232 -5121 -2676 2524 C ATOM 141 O ASP A 17 -11.739 19.675 24.888 1.00131.81 O ANISOU 141 O ASP A 17 13957 21366 14758 -5020 -2739 2341 O ATOM 142 CB ASP A 17 -9.440 20.763 22.490 1.00130.65 C ANISOU 142 CB ASP A 17 13550 21493 14599 -5985 -2767 3044 C ATOM 143 CG ASP A 17 -7.958 20.588 22.218 1.00137.12 C ANISOU 143 CG ASP A 17 13767 23113 15218 -6299 -2731 3561 C ATOM 144 OD1 ASP A 17 -7.319 19.765 22.905 1.00144.34 O ANISOU 144 OD1 ASP A 17 14077 24831 15935 -6127 -2635 3896 O ATOM 145 OD2 ASP A 17 -7.432 21.278 21.320 1.00126.67 O ANISOU 145 OD2 ASP A 17 12558 21637 13935 -6706 -2789 3663 O ATOM 146 N HIS A 18 -12.283 20.486 22.861 1.00139.78 N ANISOU 146 N HIS A 18 15602 21347 16162 -5075 -2684 2314 N ATOM 147 CA HIS A 18 -13.568 21.033 23.293 1.00141.92 C ANISOU 147 CA HIS A 18 16409 20943 16572 -4943 -2775 1862 C ATOM 148 C HIS A 18 -14.656 19.974 23.473 1.00126.95 C ANISOU 148 C HIS A 18 14527 18902 14807 -4230 -2593 1805 C ATOM 149 O HIS A 18 -15.421 20.021 24.437 1.00124.29 O ANISOU 149 O HIS A 18 14350 18420 14456 -4065 -2652 1499 O ATOM 150 CB HIS A 18 -14.049 22.093 22.296 1.00151.80 C ANISOU 150 CB HIS A 18 18202 21428 18048 -5147 -2837 1736 C ATOM 151 CG HIS A 18 -13.152 23.290 22.204 1.00161.60 C ANISOU 151 CG HIS A 18 19569 22675 19158 -5886 -3014 1700 C ATOM 152 ND1 HIS A 18 -12.033 23.446 22.993 1.00169.04 N ANISOU 152 ND1 HIS A 18 20164 24291 19774 -6394 -3141 1762 N ATOM 153 CD2 HIS A 18 -13.213 24.390 21.416 1.00161.95 C ANISOU 153 CD2 HIS A 18 20053 22152 19330 -6231 -3076 1625 C ATOM 154 CE1 HIS A 18 -11.442 24.590 22.694 1.00174.88 C ANISOU 154 CE1 HIS A 18 21147 24872 20427 -7059 -3277 1701 C ATOM 155 NE2 HIS A 18 -12.138 25.181 21.740 1.00171.12 N ANISOU 155 NE2 HIS A 18 21164 23617 20235 -6952 -3227 1609 N ATOM 156 N LEU A 19 -14.725 19.023 22.547 1.00116.29 N ANISOU 156 N LEU A 19 13041 17583 13560 -3842 -2352 2093 N ATOM 157 CA LEU A 19 -15.825 18.062 22.520 1.00103.18 C ANISOU 157 CA LEU A 19 11481 15715 12006 -3239 -2160 2037 C ATOM 158 C LEU A 19 -15.689 16.946 23.553 1.00102.74 C ANISOU 158 C LEU A 19 11038 16214 11784 -2877 -2014 2095 C ATOM 159 O LEU A 19 -16.684 16.509 24.132 1.00 78.94 O ANISOU 159 O LEU A 19 8157 13032 8806 -2502 -1976 1878 O ATOM 160 CB LEU A 19 -15.953 17.450 21.124 1.00 87.20 C ANISOU 160 CB LEU A 19 9532 13502 10099 -3040 -1919 2309 C ATOM 161 CG LEU A 19 -16.296 18.432 20.004 1.00 97.73 C ANISOU 161 CG LEU A 19 11265 14255 11615 -3315 -2044 2279 C ATOM 162 CD1 LEU A 19 -16.520 17.698 18.693 1.00112.80 C ANISOU 162 CD1 LEU A 19 13259 16015 13586 -3128 -1791 2536 C ATOM 163 CD2 LEU A 19 -17.517 19.256 20.379 1.00 94.41 C ANISOU 163 CD2 LEU A 19 11260 13271 11340 -3263 -2236 1935 C ATOM 164 N LEU A 20 -14.463 16.482 23.774 1.00107.96 N ANISOU 164 N LEU A 20 11203 17555 12261 -2975 -1919 2423 N ATOM 165 CA LEU A 20 -14.218 15.379 24.698 1.00111.05 C ANISOU 165 CA LEU A 20 11172 18532 12487 -2603 -1737 2573 C ATOM 166 C LEU A 20 -14.650 15.722 26.120 1.00113.91 C ANISOU 166 C LEU A 20 11555 18989 12738 -2668 -1977 2221 C ATOM 167 O LEU A 20 -14.230 16.738 26.675 1.00112.51 O ANISOU 167 O LEU A 20 11398 18910 12441 -3200 -2267 2061 O ATOM 168 CB LEU A 20 -12.740 14.984 24.680 1.00111.88 C ANISOU 168 CB LEU A 20 10692 19406 12412 -2733 -1605 3068 C ATOM 169 CG LEU A 20 -12.426 13.605 24.096 1.00112.40 C ANISOU 169 CG LEU A 20 10512 19709 12486 -2202 -1107 3505 C ATOM 170 CD1 LEU A 20 -12.943 13.491 22.671 1.00114.56 C ANISOU 170 CD1 LEU A 20 11219 19353 12954 -2101 -905 3508 C ATOM 171 CD2 LEU A 20 -10.932 13.324 24.152 1.00123.78 C ANISOU 171 CD2 LEU A 20 11328 21950 13755 -2314 -968 4054 C ATOM 172 N PRO A 21 -15.495 14.866 26.714 1.00107.99 N ANISOU 172 N PRO A 21 10832 18198 12001 -2158 -1834 2090 N ATOM 173 CA PRO A 21 -16.013 15.076 28.069 1.00104.71 C ANISOU 173 CA PRO A 21 10461 17839 11486 -2155 -2020 1746 C ATOM 174 C PRO A 21 -14.920 14.964 29.124 1.00109.40 C ANISOU 174 C PRO A 21 10527 19260 11781 -2403 -2112 1931 C ATOM 175 O PRO A 21 -13.879 14.360 28.867 1.00110.87 O ANISOU 175 O PRO A 21 10229 20040 11856 -2364 -1943 2398 O ATOM 176 CB PRO A 21 -17.041 13.953 28.228 1.00 92.55 C ANISOU 176 CB PRO A 21 9003 16137 10024 -1502 -1772 1675 C ATOM 177 CG PRO A 21 -16.558 12.881 27.316 1.00 88.09 C ANISOU 177 CG PRO A 21 8222 15779 9468 -1194 -1396 2104 C ATOM 178 CD PRO A 21 -15.972 13.598 26.133 1.00100.68 C ANISOU 178 CD PRO A 21 9917 17184 11155 -1581 -1451 2269 C ATOM 179 N ASN A 22 -15.159 15.543 30.295 1.00121.22 N ANISOU 179 N ASN A 22 12116 20809 13134 -2665 -2358 1595 N ATOM 180 CA ASN A 22 -14.198 15.468 31.385 1.00 91.34 C ANISOU 180 CA ASN A 22 7835 17859 9012 -2972 -2484 1760 C ATOM 181 C ASN A 22 -14.140 14.052 31.944 1.00107.93 C ANISOU 181 C ASN A 22 9472 20507 11031 -2370 -2225 2046 C ATOM 182 O ASN A 22 -15.157 13.498 32.361 1.00 99.56 O ANISOU 182 O ASN A 22 8616 19148 10066 -1899 -2117 1801 O ATOM 183 CB ASN A 22 -14.561 16.467 32.486 1.00 93.98 C ANISOU 183 CB ASN A 22 8491 18033 9185 -3451 -2782 1280 C ATOM 184 CG ASN A 22 -13.406 16.748 33.429 1.00124.31 C ANISOU 184 CG ASN A 22 11882 22740 12610 -4060 -2992 1448 C ATOM 185 OD1 ASN A 22 -12.648 15.849 33.792 1.00131.26 O ANISOU 185 OD1 ASN A 22 12114 24451 13309 -3881 -2900 1893 O ATOM 186 ND2 ASN A 22 -13.264 18.007 33.826 1.00131.62 N ANISOU 186 ND2 ASN A 22 13160 23489 13360 -4806 -3252 1120 N ATOM 187 N THR A 23 -12.944 13.473 31.951 1.00 82.69 N ANISOU 187 N THR A 23 10231 10990 10198 -2146 1422 -2280 N ATOM 188 CA THR A 23 -12.754 12.098 32.399 1.00 84.14 C ANISOU 188 CA THR A 23 10040 11361 10570 -1752 1469 -2379 C ATOM 189 C THR A 23 -13.057 11.958 33.887 1.00 68.28 C ANISOU 189 C THR A 23 7899 9339 8704 -1343 1288 -2300 C ATOM 190 O THR A 23 -13.616 10.952 34.327 1.00 57.35 O ANISOU 190 O THR A 23 6403 7924 7463 -969 1219 -2197 O ATOM 191 CB THR A 23 -11.318 11.612 32.124 1.00101.79 C ANISOU 191 CB THR A 23 11869 13973 12831 -1904 1673 -2707 C ATOM 192 OG1 THR A 23 -10.987 11.844 30.749 1.00108.58 O ANISOU 192 OG1 THR A 23 12846 14918 13493 -2374 1871 -2818 O ATOM 193 CG2 THR A 23 -11.184 10.128 32.432 1.00106.92 C ANISOU 193 CG2 THR A 23 12153 14729 13744 -1478 1687 -2793 C ATOM 194 N CYS A 24 -12.689 12.977 34.654 1.00 71.24 N ANISOU 194 N CYS A 24 8295 9751 9021 -1456 1213 -2353 N ATOM 195 CA CYS A 24 -12.907 12.969 36.095 1.00 82.00 C ANISOU 195 CA CYS A 24 9527 11176 10454 -1149 1054 -2317 C ATOM 196 C CYS A 24 -14.385 13.122 36.435 1.00 85.69 C ANISOU 196 C CYS A 24 10264 11351 10942 -926 909 -2103 C ATOM 197 O CYS A 24 -14.885 12.492 37.366 1.00 77.87 O ANISOU 197 O CYS A 24 9146 10427 10013 -602 810 -2017 O ATOM 198 CB CYS A 24 -12.097 14.082 36.761 1.00 85.17 C ANISOU 198 CB CYS A 24 9876 11715 10771 -1384 1035 -2489 C ATOM 199 SG CYS A 24 -10.313 13.957 36.504 1.00124.63 S ANISOU 199 SG CYS A 24 14484 17130 15742 -1657 1202 -2786 S ATOM 200 N PHE A 25 -15.078 13.962 35.673 1.00 91.75 N ANISOU 200 N PHE A 25 11394 11810 11658 -1117 883 -2015 N ATOM 201 CA PHE A 25 -16.490 14.227 35.919 1.00 79.15 C ANISOU 201 CA PHE A 25 10031 9930 10114 -911 735 -1855 C ATOM 202 C PHE A 25 -17.358 13.017 35.588 1.00 64.51 C ANISOU 202 C PHE A 25 8155 8041 8317 -647 736 -1693 C ATOM 203 O PHE A 25 -18.341 12.748 36.276 1.00 65.42 O ANISOU 203 O PHE A 25 8268 8102 8485 -371 636 -1604 O ATOM 204 CB PHE A 25 -16.956 15.442 35.116 1.00 81.02 C ANISOU 204 CB PHE A 25 10650 9808 10325 -1176 658 -1783 C ATOM 205 CG PHE A 25 -18.383 15.827 35.377 1.00 81.38 C ANISOU 205 CG PHE A 25 10892 9549 10478 -943 482 -1667 C ATOM 206 CD1 PHE A 25 -18.742 16.439 36.567 1.00 77.63 C ANISOU 206 CD1 PHE A 25 10364 9046 10087 -775 385 -1796 C ATOM 207 CD2 PHE A 25 -19.367 15.580 34.433 1.00 84.53 C ANISOU 207 CD2 PHE A 25 11500 9724 10892 -904 416 -1465 C ATOM 208 CE1 PHE A 25 -20.054 16.795 36.813 1.00 73.97 C ANISOU 208 CE1 PHE A 25 10026 8330 9749 -551 238 -1756 C ATOM 209 CE2 PHE A 25 -20.681 15.934 34.673 1.00 80.59 C ANISOU 209 CE2 PHE A 25 11133 8967 10519 -673 243 -1388 C ATOM 210 CZ PHE A 25 -21.025 16.543 35.864 1.00 79.38 C ANISOU 210 CZ PHE A 25 10901 8783 10478 -487 160 -1549 C ATOM 211 N ARG A 26 -16.992 12.293 34.533 1.00 54.95 N ANISOU 211 N ARG A 26 6913 6879 7086 -761 865 -1686 N ATOM 212 CA ARG A 26 -17.721 11.088 34.150 1.00 58.18 C ANISOU 212 CA ARG A 26 7292 7251 7564 -546 885 -1569 C ATOM 213 C ARG A 26 -17.673 10.048 35.261 1.00 64.87 C ANISOU 213 C ARG A 26 7851 8267 8532 -204 847 -1553 C ATOM 214 O ARG A 26 -18.702 9.502 35.655 1.00 70.92 O ANISOU 214 O ARG A 26 8651 8951 9345 31 765 -1404 O ATOM 215 CB ARG A 26 -17.157 10.492 32.857 1.00 65.61 C ANISOU 215 CB ARG A 26 8201 8263 8466 -763 1060 -1651 C ATOM 216 CG ARG A 26 -17.400 11.334 31.616 1.00 91.26 C ANISOU 216 CG ARG A 26 11776 11359 11540 -1141 1077 -1589 C ATOM 217 CD ARG A 26 -17.140 10.541 30.339 1.00111.80 C ANISOU 217 CD ARG A 26 14343 14071 14064 -1342 1258 -1671 C ATOM 218 NE ARG A 26 -15.795 9.971 30.292 1.00118.49 N ANISOU 218 NE ARG A 26 14845 15217 14959 -1420 1457 -1957 N ATOM 219 CZ ARG A 26 -15.516 8.691 30.518 1.00118.42 C ANISOU 219 CZ ARG A 26 14522 15319 15151 -1144 1538 -2089 C ATOM 220 NH1 ARG A 26 -16.489 7.839 30.808 1.00116.94 N ANISOU 220 NH1 ARG A 26 14354 14974 15104 -814 1448 -1939 N ATOM 221 NH2 ARG A 26 -14.262 8.262 30.454 1.00120.86 N ANISOU 221 NH2 ARG A 26 14488 15888 15546 -1203 1697 -2380 N ATOM 222 N THR A 27 -16.469 9.788 35.762 1.00 71.81 N ANISOU 222 N THR A 27 8441 9391 9453 -200 891 -1692 N ATOM 223 CA THR A 27 -16.257 8.811 36.825 1.00 76.05 C ANISOU 223 CA THR A 27 8696 10094 10105 95 807 -1636 C ATOM 224 C THR A 27 -17.090 9.144 38.060 1.00 77.91 C ANISOU 224 C THR A 27 8988 10348 10266 251 652 -1507 C ATOM 225 O THR A 27 -17.663 8.256 38.691 1.00 82.04 O ANISOU 225 O THR A 27 9437 10898 10836 479 567 -1342 O ATOM 226 CB THR A 27 -14.769 8.730 37.221 1.00 80.55 C ANISOU 226 CB THR A 27 8935 10945 10727 53 832 -1817 C ATOM 227 OG1 THR A 27 -13.974 8.480 36.055 1.00 81.52 O ANISOU 227 OG1 THR A 27 8967 11099 10909 -125 1009 -2009 O ATOM 228 CG2 THR A 27 -14.542 7.618 38.233 1.00 83.40 C ANISOU 228 CG2 THR A 27 9010 11445 11232 367 691 -1701 C ATOM 229 N GLN A 28 -17.162 10.429 38.392 1.00 72.06 N ANISOU 229 N GLN A 28 8377 9594 9409 100 623 -1600 N ATOM 230 CA GLN A 28 -17.947 10.882 39.533 1.00 77.61 C ANISOU 230 CA GLN A 28 9112 10343 10034 211 508 -1571 C ATOM 231 C GLN A 28 -19.439 10.660 39.307 1.00 81.40 C ANISOU 231 C GLN A 28 9782 10612 10536 349 472 -1430 C ATOM 232 O GLN A 28 -20.164 10.273 40.223 1.00 84.44 O ANISOU 232 O GLN A 28 10097 11111 10876 510 402 -1351 O ATOM 233 CB GLN A 28 -17.676 12.360 39.817 1.00 78.86 C ANISOU 233 CB GLN A 28 9368 10475 10119 8 497 -1767 C ATOM 234 CG GLN A 28 -16.276 12.652 40.326 1.00 80.39 C ANISOU 234 CG GLN A 28 9338 10948 10258 -138 517 -1932 C ATOM 235 CD GLN A 28 -16.052 14.126 40.597 1.00 88.36 C ANISOU 235 CD GLN A 28 10466 11895 11210 -368 510 -2142 C ATOM 236 OE1 GLN A 28 -15.257 14.497 41.460 1.00 88.43 O ANISOU 236 OE1 GLN A 28 10288 12172 11139 -456 490 -2300 O ATOM 237 NE2 GLN A 28 -16.752 14.977 39.856 1.00 98.24 N ANISOU 237 NE2 GLN A 28 12031 12778 12518 -473 504 -2142 N ATOM 238 N VAL A 29 -19.891 10.906 38.081 1.00 79.80 N ANISOU 238 N VAL A 29 9807 10137 10377 254 515 -1399 N ATOM 239 CA VAL A 29 -21.297 10.737 37.733 1.00 66.29 C ANISOU 239 CA VAL A 29 8261 8230 8695 372 466 -1277 C ATOM 240 C VAL A 29 -21.694 9.264 37.739 1.00 57.64 C ANISOU 240 C VAL A 29 7055 7202 7644 545 489 -1118 C ATOM 241 O VAL A 29 -22.724 8.897 38.306 1.00 53.29 O ANISOU 241 O VAL A 29 6493 6675 7079 694 432 -1030 O ATOM 242 CB VAL A 29 -21.614 11.352 36.355 1.00 62.40 C ANISOU 242 CB VAL A 29 8041 7449 8218 196 469 -1248 C ATOM 243 CG1 VAL A 29 -22.981 10.898 35.862 1.00 74.92 C ANISOU 243 CG1 VAL A 29 9746 8879 9840 326 415 -1106 C ATOM 244 CG2 VAL A 29 -21.548 12.870 36.426 1.00 44.56 C ANISOU 244 CG2 VAL A 29 5946 5023 5960 48 388 -1356 C ATOM 245 N LYS A 30 -20.870 8.425 37.114 1.00 48.13 N ANISOU 245 N LYS A 30 5755 6025 6507 509 576 -1109 N ATOM 246 CA LYS A 30 -21.124 6.987 37.059 1.00 47.25 C ANISOU 246 CA LYS A 30 5540 5914 6499 667 591 -979 C ATOM 247 C LYS A 30 -21.261 6.388 38.456 1.00 59.46 C ANISOU 247 C LYS A 30 6916 7642 8035 844 484 -853 C ATOM 248 O LYS A 30 -22.072 5.489 38.677 1.00 71.32 O ANISOU 248 O LYS A 30 8421 9108 9569 960 446 -689 O ATOM 249 CB LYS A 30 -20.010 6.269 36.293 1.00 54.63 C ANISOU 249 CB LYS A 30 6336 6862 7559 615 701 -1076 C ATOM 250 CG LYS A 30 -19.864 6.701 34.842 1.00 80.02 C ANISOU 250 CG LYS A 30 9711 9964 10729 372 831 -1197 C ATOM 251 CD LYS A 30 -21.144 6.477 34.055 1.00 94.48 C ANISOU 251 CD LYS A 30 11763 11606 12527 361 828 -1085 C ATOM 252 CE LYS A 30 -20.985 6.931 32.612 1.00 96.08 C ANISOU 252 CE LYS A 30 12138 11742 12626 67 930 -1172 C ATOM 253 NZ LYS A 30 -22.218 6.700 31.811 1.00 99.32 N ANISOU 253 NZ LYS A 30 12749 12001 12986 42 901 -1054 N ATOM 254 N GLU A 31 -20.465 6.892 39.395 1.00 71.07 N ANISOU 254 N GLU A 31 8241 9329 9433 825 428 -921 N ATOM 255 CA GLU A 31 -20.541 6.443 40.780 1.00 67.85 C ANISOU 255 CA GLU A 31 7677 9158 8946 931 304 -786 C ATOM 256 C GLU A 31 -21.820 6.942 41.441 1.00 62.34 C ANISOU 256 C GLU A 31 7083 8518 8087 933 272 -771 C ATOM 257 O GLU A 31 -22.471 6.208 42.183 1.00 63.09 O ANISOU 257 O GLU A 31 7128 8734 8111 1000 207 -597 O ATOM 258 CB GLU A 31 -19.321 6.917 41.571 1.00 70.83 C ANISOU 258 CB GLU A 31 7858 9798 9258 876 247 -889 C ATOM 259 CG GLU A 31 -18.016 6.260 41.156 1.00 86.23 C ANISOU 259 CG GLU A 31 9608 11764 11391 913 251 -916 C ATOM 260 CD GLU A 31 -16.823 6.805 41.916 1.00 95.61 C ANISOU 260 CD GLU A 31 10578 13244 12506 843 186 -1038 C ATOM 261 OE1 GLU A 31 -17.016 7.699 42.766 1.00105.28 O ANISOU 261 OE1 GLU A 31 11827 14651 13521 746 146 -1106 O ATOM 262 OE2 GLU A 31 -15.692 6.339 41.662 1.00 95.31 O ANISOU 262 OE2 GLU A 31 10319 13266 12630 882 177 -1101 O ATOM 263 N ALA A 32 -22.174 8.193 41.162 1.00 59.03 N ANISOU 263 N ALA A 32 6799 8006 7623 847 312 -965 N ATOM 264 CA ALA A 32 -23.378 8.796 41.723 1.00 55.20 C ANISOU 264 CA ALA A 32 6371 7559 7042 870 288 -1040 C ATOM 265 C ALA A 32 -24.631 8.062 41.253 1.00 65.15 C ANISOU 265 C ALA A 32 7718 8688 8347 958 299 -897 C ATOM 266 O ALA A 32 -25.585 7.899 42.012 1.00 61.22 O ANISOU 266 O ALA A 32 7164 8350 7746 996 279 -882 O ATOM 267 CB ALA A 32 -23.455 10.268 41.353 1.00 43.29 C ANISOU 267 CB ALA A 32 4999 5875 5574 789 297 -1278 C ATOM 268 N ILE A 33 -24.621 7.623 39.999 1.00 68.64 N ANISOU 268 N ILE A 33 8282 8877 8922 957 342 -819 N ATOM 269 CA ILE A 33 -25.728 6.848 39.452 1.00 68.78 C ANISOU 269 CA ILE A 33 8375 8774 8985 1016 354 -690 C ATOM 270 C ILE A 33 -25.832 5.501 40.160 1.00 73.93 C ANISOU 270 C ILE A 33 8902 9574 9614 1073 334 -484 C ATOM 271 O ILE A 33 -26.928 5.042 40.483 1.00 89.14 O ANISOU 271 O ILE A 33 10827 11560 11481 1093 324 -398 O ATOM 272 CB ILE A 33 -25.572 6.626 37.933 1.00 69.58 C ANISOU 272 CB ILE A 33 8622 8614 9201 957 412 -672 C ATOM 273 CG1 ILE A 33 -25.602 7.964 37.194 1.00 57.39 C ANISOU 273 CG1 ILE A 33 7248 6901 7657 856 390 -803 C ATOM 274 CG2 ILE A 33 -26.672 5.717 37.404 1.00 69.89 C ANISOU 274 CG2 ILE A 33 8718 8559 9278 998 425 -550 C ATOM 275 CD1 ILE A 33 -26.889 8.735 37.380 1.00 56.01 C ANISOU 275 CD1 ILE A 33 7142 6659 7480 928 299 -858 C ATOM 276 N ASP A 34 -24.682 4.879 40.410 1.00 62.68 N ANISOU 276 N ASP A 34 7365 8205 8248 1087 312 -400 N ATOM 277 CA ASP A 34 -24.637 3.595 41.102 1.00 67.78 C ANISOU 277 CA ASP A 34 7905 8935 8913 1142 237 -155 C ATOM 278 C ASP A 34 -25.187 3.704 42.520 1.00 68.08 C ANISOU 278 C ASP A 34 7862 9294 8711 1096 159 -70 C ATOM 279 O ASP A 34 -25.805 2.770 43.026 1.00 82.74 O ANISOU 279 O ASP A 34 9707 11218 10513 1077 108 154 O ATOM 280 CB ASP A 34 -23.207 3.051 41.135 1.00 84.17 C ANISOU 280 CB ASP A 34 9838 11000 11142 1198 183 -108 C ATOM 281 CG ASP A 34 -22.723 2.601 39.771 1.00106.87 C ANISOU 281 CG ASP A 34 12747 13598 14261 1225 284 -204 C ATOM 282 OD1 ASP A 34 -23.568 2.202 38.941 1.00103.47 O ANISOU 282 OD1 ASP A 34 12450 12975 13888 1211 358 -193 O ATOM 283 OD2 ASP A 34 -21.499 2.643 39.530 1.00120.26 O ANISOU 283 OD2 ASP A 34 14313 15303 16076 1241 296 -318 O ATOM 284 N ILE A 35 -24.957 4.848 43.157 1.00 56.89 N ANISOU 284 N ILE A 35 6390 8088 7137 1041 158 -263 N ATOM 285 CA ILE A 35 -25.504 5.100 44.485 1.00 59.90 C ANISOU 285 CA ILE A 35 6674 8836 7249 955 119 -271 C ATOM 286 C ILE A 35 -27.020 5.240 44.410 1.00 66.66 C ANISOU 286 C ILE A 35 7588 9700 8039 938 192 -352 C ATOM 287 O ILE A 35 -27.747 4.655 45.212 1.00 75.03 O ANISOU 287 O ILE A 35 8585 11006 8917 853 176 -223 O ATOM 288 CB ILE A 35 -24.904 6.370 45.120 1.00 67.45 C ANISOU 288 CB ILE A 35 7547 10003 8078 891 121 -542 C ATOM 289 CG1 ILE A 35 -23.384 6.245 45.242 1.00 70.81 C ANISOU 289 CG1 ILE A 35 7873 10477 8554 891 43 -482 C ATOM 290 CG2 ILE A 35 -25.523 6.629 46.485 1.00 74.73 C ANISOU 290 CG2 ILE A 35 8347 11354 8693 769 109 -614 C ATOM 291 CD1 ILE A 35 -22.933 5.096 46.115 1.00 79.07 C ANISOU 291 CD1 ILE A 35 8789 11741 9514 884 -112 -153 C ATOM 292 N VAL A 36 -27.488 6.013 43.434 1.00 64.72 N ANISOU 292 N VAL A 36 7453 9199 7938 1002 257 -557 N ATOM 293 CA VAL A 36 -28.916 6.237 43.236 1.00 60.09 C ANISOU 293 CA VAL A 36 6891 8596 7345 1022 301 -669 C ATOM 294 C VAL A 36 -29.630 4.957 42.812 1.00 57.47 C ANISOU 294 C VAL A 36 6605 8182 7048 1014 314 -423 C ATOM 295 O VAL A 36 -30.680 4.614 43.358 1.00 67.24 O ANISOU 295 O VAL A 36 7769 9627 8151 951 339 -407 O ATOM 296 CB VAL A 36 -29.170 7.334 42.181 1.00 61.25 C ANISOU 296 CB VAL A 36 7163 8433 7677 1102 306 -886 C ATOM 297 CG1 VAL A 36 -30.648 7.413 41.833 1.00 60.70 C ANISOU 297 CG1 VAL A 36 7095 8316 7652 1159 312 -968 C ATOM 298 CG2 VAL A 36 -28.664 8.678 42.682 1.00 66.91 C ANISOU 298 CG2 VAL A 36 7843 9201 8381 1092 289 -1162 C ATOM 299 N CYS A 37 -29.054 4.256 41.839 1.00 54.83 N ANISOU 299 N CYS A 37 6377 7562 6893 1053 310 -265 N ATOM 300 CA CYS A 37 -29.618 3.000 41.349 1.00 63.87 C ANISOU 300 CA CYS A 37 7577 8575 8115 1036 325 -57 C ATOM 301 C CYS A 37 -29.781 1.985 42.473 1.00 67.71 C ANISOU 301 C CYS A 37 7980 9289 8459 941 274 194 C ATOM 302 O CYS A 37 -30.801 1.304 42.566 1.00 66.63 O ANISOU 302 O CYS A 37 7852 9201 8263 859 296 300 O ATOM 303 CB CYS A 37 -28.737 2.412 40.244 1.00 67.62 C ANISOU 303 CB CYS A 37 8140 8736 8816 1083 340 11 C ATOM 304 SG CYS A 37 -29.212 0.748 39.716 1.00 76.47 S ANISOU 304 SG CYS A 37 9317 9653 10086 1057 355 236 S ATOM 305 N ARG A 38 -28.769 1.896 43.329 1.00 76.10 N ANISOU 305 N ARG A 38 8962 10503 9450 926 188 305 N ATOM 306 CA ARG A 38 -28.794 0.970 44.453 1.00 81.81 C ANISOU 306 CA ARG A 38 9623 11450 10011 805 87 606 C ATOM 307 C ARG A 38 -29.745 1.474 45.536 1.00 80.31 C ANISOU 307 C ARG A 38 9337 11701 9475 637 128 508 C ATOM 308 O ARG A 38 -30.267 0.694 46.332 1.00 88.80 O ANISOU 308 O ARG A 38 10388 12999 10352 456 86 745 O ATOM 309 CB ARG A 38 -27.382 0.779 45.013 1.00 79.99 C ANISOU 309 CB ARG A 38 9314 11267 9812 846 -57 757 C ATOM 310 CG ARG A 38 -27.213 -0.446 45.894 1.00 91.48 C ANISOU 310 CG ARG A 38 10748 12806 11203 751 -236 1178 C ATOM 311 CD ARG A 38 -25.760 -0.908 45.940 1.00110.51 C ANISOU 311 CD ARG A 38 13086 15069 13835 888 -411 1342 C ATOM 312 NE ARG A 38 -24.852 0.131 46.422 1.00120.61 N ANISOU 312 NE ARG A 38 14234 16610 14983 904 -434 1150 N ATOM 313 CZ ARG A 38 -23.980 0.780 45.657 1.00119.27 C ANISOU 313 CZ ARG A 38 14023 16285 15009 1041 -365 886 C ATOM 314 NH1 ARG A 38 -23.886 0.500 44.365 1.00116.46 N ANISOU 314 NH1 ARG A 38 13741 15541 14966 1167 -264 778 N ATOM 315 NH2 ARG A 38 -23.195 1.709 46.187 1.00118.12 N ANISOU 315 NH2 ARG A 38 13757 16400 14722 1012 -390 718 N ATOM 316 N PHE A 39 -29.966 2.785 45.552 1.00 67.60 N ANISOU 316 N PHE A 39 7668 10214 7804 678 212 142 N ATOM 317 CA PHE A 39 -30.868 3.408 46.513 1.00 65.04 C ANISOU 317 CA PHE A 39 7205 10313 7195 541 283 -77 C ATOM 318 C PHE A 39 -32.328 3.204 46.120 1.00 68.03 C ANISOU 318 C PHE A 39 7575 10690 7582 512 380 -166 C ATOM 319 O PHE A 39 -33.159 2.847 46.954 1.00 77.91 O ANISOU 319 O PHE A 39 8720 12310 8573 312 426 -143 O ATOM 320 CB PHE A 39 -30.563 4.903 46.636 1.00 72.91 C ANISOU 320 CB PHE A 39 8129 11373 8201 623 325 -483 C ATOM 321 CG PHE A 39 -31.252 5.577 47.789 1.00 77.05 C ANISOU 321 CG PHE A 39 8463 12375 8438 479 400 -777 C ATOM 322 CD1 PHE A 39 -30.650 5.628 49.036 1.00 73.52 C ANISOU 322 CD1 PHE A 39 7899 12356 7681 295 364 -750 C ATOM 323 CD2 PHE A 39 -32.492 6.170 47.625 1.00 74.26 C ANISOU 323 CD2 PHE A 39 8020 12068 8128 522 503 -1110 C ATOM 324 CE1 PHE A 39 -31.276 6.250 50.099 1.00 72.58 C ANISOU 324 CE1 PHE A 39 7582 12728 7267 124 461 -1077 C ATOM 325 CE2 PHE A 39 -33.123 6.793 48.685 1.00 78.90 C ANISOU 325 CE2 PHE A 39 8387 13118 8475 391 598 -1460 C ATOM 326 CZ PHE A 39 -32.514 6.835 49.923 1.00 79.59 C ANISOU 326 CZ PHE A 39 8364 13655 8223 175 593 -1460 C ATOM 327 N LEU A 40 -32.631 3.430 44.845 1.00 71.56 N ANISOU 327 N LEU A 40 8125 10758 8306 681 405 -269 N ATOM 328 CA LEU A 40 -34.004 3.356 44.356 1.00 61.24 C ANISOU 328 CA LEU A 40 6788 9442 7038 680 474 -389 C ATOM 329 C LEU A 40 -34.568 1.940 44.420 1.00 59.06 C ANISOU 329 C LEU A 40 6549 9207 6685 509 485 -77 C ATOM 330 O LEU A 40 -35.754 1.752 44.688 1.00 71.81 O ANISOU 330 O LEU A 40 8056 11059 8169 385 557 -160 O ATOM 331 CB LEU A 40 -34.091 3.880 42.920 1.00 57.91 C ANISOU 331 CB LEU A 40 6490 8604 6910 874 454 -510 C ATOM 332 CG LEU A 40 -33.795 5.365 42.696 1.00 51.52 C ANISOU 332 CG LEU A 40 5674 7684 6218 1024 423 -819 C ATOM 333 CD1 LEU A 40 -33.955 5.725 41.228 1.00 42.12 C ANISOU 333 CD1 LEU A 40 4638 6090 5274 1152 369 -843 C ATOM 334 CD2 LEU A 40 -34.687 6.238 43.566 1.00 45.80 C ANISOU 334 CD2 LEU A 40 4735 7274 5394 1028 464 -1170 C ATOM 335 N LYS A 41 -33.721 0.947 44.171 1.00 57.75 N ANISOU 335 N LYS A 41 6521 8797 6624 499 410 260 N ATOM 336 CA LYS A 41 -34.162 -0.444 44.194 1.00 61.24 C ANISOU 336 CA LYS A 41 7031 9183 7053 336 394 578 C ATOM 337 C LYS A 41 -34.618 -0.858 45.589 1.00 79.40 C ANISOU 337 C LYS A 41 9231 11940 8997 53 387 737 C ATOM 338 O LYS A 41 -35.628 -1.546 45.742 1.00 99.93 O ANISOU 338 O LYS A 41 11818 14672 11479 -154 440 833 O ATOM 339 CB LYS A 41 -33.045 -1.370 43.707 1.00 47.79 C ANISOU 339 CB LYS A 41 5471 7087 5599 418 291 866 C ATOM 340 CG LYS A 41 -32.742 -1.237 42.224 1.00 48.75 C ANISOU 340 CG LYS A 41 5695 6795 6034 608 333 720 C ATOM 341 CD LYS A 41 -31.747 -2.286 41.755 1.00 50.90 C ANISOU 341 CD LYS A 41 6058 6703 6578 674 260 938 C ATOM 342 CE LYS A 41 -30.380 -2.080 42.382 1.00 75.63 C ANISOU 342 CE LYS A 41 9131 9874 9733 765 149 1020 C ATOM 343 NZ LYS A 41 -29.392 -3.072 41.875 1.00 89.28 N ANISOU 343 NZ LYS A 41 10897 11233 11794 875 70 1171 N ATOM 344 N GLU A 42 -33.868 -0.437 46.601 1.00 77.53 N ANISOU 344 N GLU A 42 8920 11976 8561 4 324 764 N ATOM 345 CA GLU A 42 -34.189 -0.764 47.985 1.00 80.17 C ANISOU 345 CA GLU A 42 9160 12814 8487 -318 306 924 C ATOM 346 C GLU A 42 -35.307 0.101 48.567 1.00 78.53 C ANISOU 346 C GLU A 42 8737 13102 7998 -455 479 513 C ATOM 347 O GLU A 42 -36.247 -0.411 49.176 1.00 86.19 O ANISOU 347 O GLU A 42 9631 14427 8690 -757 550 577 O ATOM 348 CB GLU A 42 -32.938 -0.630 48.856 1.00 92.52 C ANISOU 348 CB GLU A 42 10707 14530 9916 -340 155 1098 C ATOM 349 CG GLU A 42 -33.194 -0.799 50.344 1.00112.55 C ANISOU 349 CG GLU A 42 13138 17670 11954 -715 125 1243 C ATOM 350 CD GLU A 42 -31.991 -0.426 51.187 1.00120.57 C ANISOU 350 CD GLU A 42 14100 18903 12806 -730 -24 1332 C ATOM 351 OE1 GLU A 42 -30.968 -0.003 50.609 1.00123.41 O ANISOU 351 OE1 GLU A 42 14488 18940 13460 -439 -89 1251 O ATOM 352 OE2 GLU A 42 -32.069 -0.552 52.427 1.00119.66 O ANISOU 352 OE2 GLU A 42 13904 19319 12243 -1065 -75 1475 O ATOM 353 N ARG A 43 -35.125 1.404 48.479 1.00 64.63 N ANISOU 353 N ARG A 43 6865 11387 6304 -259 538 88 N ATOM 354 CA ARG A 43 -36.070 2.330 49.052 1.00 72.70 C ANISOU 354 CA ARG A 43 7645 12846 7133 -336 690 -380 C ATOM 355 C ARG A 43 -37.451 2.354 48.414 1.00 82.23 C ANISOU 355 C ARG A 43 8756 14031 8457 -298 806 -618 C ATOM 356 O ARG A 43 -38.450 2.428 49.115 1.00 76.78 O ANISOU 356 O ARG A 43 7846 13817 7509 -515 936 -845 O ATOM 357 CB ARG A 43 -35.463 3.723 49.079 1.00 60.62 C ANISOU 357 CB ARG A 43 6038 11279 5717 -117 696 -777 C ATOM 358 CG ARG A 43 -34.242 3.803 49.974 1.00 89.43 C ANISOU 358 CG ARG A 43 9699 15125 9154 -224 604 -626 C ATOM 359 CD ARG A 43 -34.643 3.721 51.435 1.00102.79 C ANISOU 359 CD ARG A 43 11199 17513 10342 -598 674 -688 C ATOM 360 NE ARG A 43 -35.367 4.917 51.840 1.00102.89 N ANISOU 360 NE ARG A 43 10958 17849 10287 -587 845 -1317 N ATOM 361 CZ ARG A 43 -34.819 5.926 52.502 1.00 94.76 C ANISOU 361 CZ ARG A 43 9803 17050 9153 -591 872 -1664 C ATOM 362 NH1 ARG A 43 -33.541 5.877 52.843 1.00 78.98 N ANISOU 362 NH1 ARG A 43 7905 15036 7069 -622 735 -1418 N ATOM 363 NH2 ARG A 43 -35.549 6.980 52.827 1.00103.20 N ANISOU 363 NH2 ARG A 43 10624 18362 10226 -561 1030 -2282 N ATOM 364 N CYS A 44 -37.516 2.295 47.092 1.00 78.72 N ANISOU 364 N CYS A 44 8451 13078 8381 -47 761 -586 N ATOM 365 CA CYS A 44 -38.769 2.572 46.415 1.00 75.63 C ANISOU 365 CA CYS A 44 7939 12660 8135 44 834 -869 C ATOM 366 C CYS A 44 -39.804 1.556 46.818 1.00 86.09 C ANISOU 366 C CYS A 44 9176 14310 9223 -274 925 -738 C ATOM 367 O CYS A 44 -39.518 0.370 46.849 1.00 97.39 O ANISOU 367 O CYS A 44 10785 15640 10580 -464 878 -297 O ATOM 368 CB CYS A 44 -38.576 2.535 44.906 1.00 65.68 C ANISOU 368 CB CYS A 44 6878 10826 7253 303 745 -777 C ATOM 369 SG CYS A 44 -38.079 4.109 44.186 1.00 82.95 S ANISOU 369 SG CYS A 44 9088 12683 9747 661 663 -1110 S ATOM 370 N PHE A 45 -40.986 2.043 47.166 1.00 84.00 N ANISOU 370 N PHE A 45 8623 14438 8855 -339 1051 -1141 N ATOM 371 CA PHE A 45 -42.033 1.177 47.653 1.00 83.99 C ANISOU 371 CA PHE A 45 8490 14844 8577 -700 1169 -1078 C ATOM 372 C PHE A 45 -41.455 0.426 48.845 1.00 90.22 C ANISOU 372 C PHE A 45 9361 15961 8956 -1086 1169 -713 C ATOM 373 O PHE A 45 -40.887 1.042 49.743 1.00108.75 O ANISOU 373 O PHE A 45 11625 18597 11100 -1132 1179 -842 O ATOM 374 CB PHE A 45 -42.509 0.241 46.543 1.00 88.18 C ANISOU 374 CB PHE A 45 9178 15012 9315 -693 1128 -825 C ATOM 375 CG PHE A 45 -42.993 0.961 45.321 1.00 84.20 C ANISOU 375 CG PHE A 45 8619 14186 9186 -333 1079 -1118 C ATOM 376 CD1 PHE A 45 -44.152 1.712 45.359 1.00 86.45 C ANISOU 376 CD1 PHE A 45 8569 14768 9510 -254 1152 -1600 C ATOM 377 CD2 PHE A 45 -42.284 0.895 44.138 1.00 81.82 C ANISOU 377 CD2 PHE A 45 8587 13304 9196 -84 945 -916 C ATOM 378 CE1 PHE A 45 -44.599 2.379 44.239 1.00 84.20 C ANISOU 378 CE1 PHE A 45 8239 14172 9583 82 1048 -1820 C ATOM 379 CE2 PHE A 45 -42.724 1.561 43.013 1.00 80.59 C ANISOU 379 CE2 PHE A 45 8403 12879 9339 199 869 -1135 C ATOM 380 CZ PHE A 45 -43.884 2.304 43.063 1.00 81.70 C ANISOU 380 CZ PHE A 45 8229 13284 9529 291 897 -1559 C ATOM 381 N GLN A 46 -41.627 -0.885 48.865 1.00 79.24 N ANISOU 381 N GLN A 46 8132 14530 7443 -1380 1142 -261 N ATOM 382 CA GLN A 46 -41.027 -1.704 49.896 1.00 85.74 C ANISOU 382 CA GLN A 46 9088 15569 7919 -1745 1070 197 C ATOM 383 C GLN A 46 -42.028 -1.680 51.022 1.00102.30 C ANISOU 383 C GLN A 46 10914 18431 9524 -2196 1251 -11 C ATOM 384 O GLN A 46 -42.714 -0.679 51.211 1.00100.59 O ANISOU 384 O GLN A 46 10379 18578 9263 -2118 1415 -594 O ATOM 385 CB GLN A 46 -39.705 -1.089 50.338 1.00 81.62 C ANISOU 385 CB GLN A 46 8632 14987 7392 -1572 950 244 C ATOM 386 CG GLN A 46 -39.140 -1.658 51.625 1.00 86.17 C ANISOU 386 CG GLN A 46 9266 15945 7531 -1964 858 637 C ATOM 387 CD GLN A 46 -37.929 -0.888 52.104 1.00 86.49 C ANISOU 387 CD GLN A 46 9301 16022 7538 -1800 755 582 C ATOM 388 OE1 GLN A 46 -37.871 0.332 51.980 1.00 91.17 O ANISOU 388 OE1 GLN A 46 9730 16670 8239 -1548 847 78 O ATOM 389 NE2 GLN A 46 -36.953 -1.597 52.651 1.00 78.33 N ANISOU 389 NE2 GLN A 46 8442 14941 6376 -1942 542 1105 N ATOM 390 N GLY A 47 -42.132 -2.764 51.780 1.00130.32 N ANISOU 390 N GLY A 47 14572 22234 12708 -2685 1221 445 N ATOM 391 CA GLY A 47 -43.084 -2.812 52.876 1.00134.71 C ANISOU 391 CA GLY A 47 14873 23587 12725 -3207 1412 267 C ATOM 392 C GLY A 47 -44.447 -2.477 52.302 1.00125.51 C ANISOU 392 C GLY A 47 13418 22583 11687 -3148 1625 -255 C ATOM 393 O GLY A 47 -45.284 -1.852 52.949 1.00128.07 O ANISOU 393 O GLY A 47 13376 23538 11747 -3327 1832 -771 O ATOM 394 N THR A 48 -44.651 -2.898 51.061 1.00117.13 N ANISOU 394 N THR A 48 12508 20937 11059 -2883 1557 -143 N ATOM 395 CA THR A 48 -45.805 -2.478 50.291 1.00 99.19 C ANISOU 395 CA THR A 48 9972 18703 9012 -2706 1693 -628 C ATOM 396 C THR A 48 -46.510 -3.667 49.688 1.00 87.83 C ANISOU 396 C THR A 48 8661 17085 7626 -2950 1699 -330 C ATOM 397 O THR A 48 -45.886 -4.657 49.315 1.00 78.29 O ANISOU 397 O THR A 48 7817 15386 6543 -3003 1545 218 O ATOM 398 CB THR A 48 -45.405 -1.534 49.148 1.00 78.94 C ANISOU 398 CB THR A 48 7432 15582 6981 -2067 1589 -897 C ATOM 399 OG1 THR A 48 -44.156 -0.911 49.460 1.00116.74 O ANISOU 399 OG1 THR A 48 12349 20196 11811 -1844 1478 -835 O ATOM 400 CG2 THR A 48 -46.459 -0.469 48.952 1.00 72.71 C ANISOU 400 CG2 THR A 48 6225 15079 6320 -1856 1718 -1585 C ATOM 401 N ALA A 49 -47.822 -3.552 49.583 1.00 90.97 N ANISOU 401 N ALA A 49 8732 17877 7955 -3090 1877 -733 N ATOM 402 CA ALA A 49 -48.628 -4.614 49.028 1.00 90.97 C ANISOU 402 CA ALA A 49 8800 17782 7982 -3362 1909 -529 C ATOM 403 C ALA A 49 -48.230 -4.857 47.588 1.00 86.11 C ANISOU 403 C ALA A 49 8453 16383 7883 -2945 1740 -356 C ATOM 404 O ALA A 49 -48.241 -5.994 47.124 1.00 75.42 O ANISOU 404 O ALA A 49 7360 14691 6604 -3145 1683 45 O ATOM 405 CB ALA A 49 -50.102 -4.263 49.120 1.00 82.92 C ANISOU 405 CB ALA A 49 7306 17364 6833 -3524 2129 -1093 C ATOM 406 N ASP A 50 -47.913 -3.789 46.861 1.00 93.37 N ANISOU 406 N ASP A 50 9303 17019 9153 -2393 1663 -676 N ATOM 407 CA ASP A 50 -47.808 -3.933 45.412 1.00 96.54 C ANISOU 407 CA ASP A 50 9883 16811 9988 -2057 1537 -611 C ATOM 408 C ASP A 50 -46.426 -4.458 45.022 1.00112.13 C ANISOU 408 C ASP A 50 12289 18160 12156 -1913 1371 -133 C ATOM 409 O ASP A 50 -45.410 -3.845 45.353 1.00125.94 O ANISOU 409 O ASP A 50 14119 19798 13936 -1692 1294 -100 O ATOM 410 CB ASP A 50 -48.087 -2.595 44.723 1.00 98.20 C ANISOU 410 CB ASP A 50 9857 16962 10492 -1565 1491 -1109 C ATOM 411 CG ASP A 50 -48.456 -2.751 43.256 1.00106.82 C ANISOU 411 CG ASP A 50 11024 17638 11923 -1342 1388 -1121 C ATOM 412 OD1 ASP A 50 -47.890 -3.632 42.578 1.00114.44 O ANISOU 412 OD1 ASP A 50 12328 18145 13010 -1387 1314 -738 O ATOM 413 OD2 ASP A 50 -49.316 -1.983 42.778 1.00104.16 O ANISOU 413 OD2 ASP A 50 10394 17442 11741 -1123 1369 -1530 O ATOM 414 N PRO A 51 -46.388 -5.600 44.316 1.00101.20 N ANISOU 414 N PRO A 51 11158 16372 10920 -2044 1320 201 N ATOM 415 CA PRO A 51 -45.153 -6.266 43.881 1.00 84.37 C ANISOU 415 CA PRO A 51 9402 13629 9026 -1922 1172 616 C ATOM 416 C PRO A 51 -44.263 -5.415 42.973 1.00 75.29 C ANISOU 416 C PRO A 51 8333 12068 8203 -1418 1070 470 C ATOM 417 O PRO A 51 -43.096 -5.759 42.786 1.00 79.13 O ANISOU 417 O PRO A 51 9067 12136 8864 -1289 961 741 O ATOM 418 CB PRO A 51 -45.671 -7.491 43.120 1.00 89.45 C ANISOU 418 CB PRO A 51 10198 13981 9808 -2146 1181 805 C ATOM 419 CG PRO A 51 -47.004 -7.761 43.711 1.00 99.91 C ANISOU 419 CG PRO A 51 11287 15860 10816 -2569 1332 681 C ATOM 420 CD PRO A 51 -47.580 -6.412 44.013 1.00102.79 C ANISOU 420 CD PRO A 51 11273 16728 11053 -2378 1418 180 C ATOM 421 N VAL A 52 -44.807 -4.339 42.410 1.00 72.83 N ANISOU 421 N VAL A 52 7814 11872 7987 -1153 1090 56 N ATOM 422 CA VAL A 52 -44.038 -3.462 41.530 1.00 69.70 C ANISOU 422 CA VAL A 52 7506 11110 7868 -731 984 -69 C ATOM 423 C VAL A 52 -42.825 -2.875 42.249 1.00 77.45 C ANISOU 423 C VAL A 52 8559 12056 8812 -584 929 7 C ATOM 424 O VAL A 52 -42.954 -2.265 43.311 1.00 91.50 O ANISOU 424 O VAL A 52 10153 14244 10368 -643 980 -146 O ATOM 425 CB VAL A 52 -44.908 -2.314 40.980 1.00 63.41 C ANISOU 425 CB VAL A 52 6456 10469 7168 -492 970 -502 C ATOM 426 CG1 VAL A 52 -44.052 -1.310 40.224 1.00 60.65 C ANISOU 426 CG1 VAL A 52 6223 9760 7062 -108 840 -586 C ATOM 427 CG2 VAL A 52 -46.006 -2.863 40.085 1.00 64.70 C ANISOU 427 CG2 VAL A 52 6549 10635 7398 -601 985 -572 C ATOM 428 N ARG A 53 -41.650 -3.061 41.657 1.00 74.03 N ANISOU 428 N ARG A 53 8372 11164 8593 -410 836 206 N ATOM 429 CA ARG A 53 -40.399 -2.611 42.257 1.00 75.53 C ANISOU 429 CA ARG A 53 8633 11296 8769 -281 771 301 C ATOM 430 C ARG A 53 -39.433 -2.134 41.179 1.00 68.42 C ANISOU 430 C ARG A 53 7885 9956 8156 22 694 258 C ATOM 431 O ARG A 53 -39.607 -2.447 40.002 1.00 61.70 O ANISOU 431 O ARG A 53 7132 8815 7495 77 688 243 O ATOM 432 CB ARG A 53 -39.760 -3.737 43.073 1.00 69.94 C ANISOU 432 CB ARG A 53 8064 10555 7956 -513 725 720 C ATOM 433 CG ARG A 53 -39.273 -3.318 44.448 1.00 72.23 C ANISOU 433 CG ARG A 53 8265 11215 7965 -607 701 777 C ATOM 434 CD ARG A 53 -40.440 -3.067 45.386 1.00 75.97 C ANISOU 434 CD ARG A 53 8499 12286 8081 -881 826 589 C ATOM 435 NE ARG A 53 -41.242 -4.269 45.600 1.00 76.22 N ANISOU 435 NE ARG A 53 8570 12420 7969 -1255 868 840 N ATOM 436 CZ ARG A 53 -42.375 -4.298 46.295 1.00 84.44 C ANISOU 436 CZ ARG A 53 9402 13991 8691 -1575 1002 696 C ATOM 437 NH1 ARG A 53 -42.849 -3.188 46.844 1.00 78.88 N ANISOU 437 NH1 ARG A 53 8408 13758 7804 -1532 1110 262 N ATOM 438 NH2 ARG A 53 -43.038 -5.437 46.439 1.00 99.84 N ANISOU 438 NH2 ARG A 53 11420 15999 10515 -1953 1034 958 N ATOM 439 N VAL A 54 -38.415 -1.379 41.580 1.00 70.96 N ANISOU 439 N VAL A 54 8219 10262 8481 177 644 226 N ATOM 440 CA VAL A 54 -37.401 -0.930 40.634 1.00 66.73 C ANISOU 440 CA VAL A 54 7823 9351 8180 407 585 193 C ATOM 441 C VAL A 54 -36.379 -2.035 40.395 1.00 64.79 C ANISOU 441 C VAL A 54 7747 8788 8084 380 547 486 C ATOM 442 O VAL A 54 -35.681 -2.454 41.317 1.00 50.97 O ANISOU 442 O VAL A 54 6002 7100 6264 319 493 700 O ATOM 443 CB VAL A 54 -36.679 0.335 41.132 1.00 44.10 C ANISOU 443 CB VAL A 54 4895 6585 5275 564 549 18 C ATOM 444 CG1 VAL A 54 -35.559 0.716 40.178 1.00 42.09 C ANISOU 444 CG1 VAL A 54 4793 5967 5234 735 500 12 C ATOM 445 CG2 VAL A 54 -37.664 1.481 41.293 1.00 55.82 C ANISOU 445 CG2 VAL A 54 6199 8306 6703 639 569 -326 C ATOM 446 N SER A 55 -36.298 -2.507 39.155 1.00 71.03 N ANISOU 446 N SER A 55 8656 9243 9087 422 562 479 N ATOM 447 CA SER A 55 -35.358 -3.567 38.808 1.00 72.58 C ANISOU 447 CA SER A 55 8979 9099 9498 424 538 673 C ATOM 448 C SER A 55 -33.951 -3.038 38.546 1.00 61.78 C ANISOU 448 C SER A 55 7640 7569 8265 610 502 616 C ATOM 449 O SER A 55 -32.968 -3.599 39.028 1.00 64.91 O ANISOU 449 O SER A 55 8043 7852 8766 646 435 789 O ATOM 450 CB SER A 55 -35.858 -4.337 37.584 1.00 71.48 C ANISOU 450 CB SER A 55 8930 8703 9524 357 598 623 C ATOM 451 OG SER A 55 -36.103 -3.464 36.495 1.00 72.12 O ANISOU 451 OG SER A 55 9022 8768 9613 441 627 378 O ATOM 452 N LYS A 56 -33.864 -1.954 37.781 1.00 59.32 N ANISOU 452 N LYS A 56 7338 7247 7953 713 528 382 N ATOM 453 CA LYS A 56 -32.574 -1.407 37.377 1.00 58.72 C ANISOU 453 CA LYS A 56 7293 7033 7985 834 518 298 C ATOM 454 C LYS A 56 -32.678 0.055 36.950 1.00 53.16 C ANISOU 454 C LYS A 56 6599 6401 7198 899 509 86 C ATOM 455 O LYS A 56 -33.766 0.552 36.659 1.00 75.70 O ANISOU 455 O LYS A 56 9448 9337 9979 884 498 -10 O ATOM 456 CB LYS A 56 -31.978 -2.244 36.244 1.00 56.49 C ANISOU 456 CB LYS A 56 7090 6440 7933 828 574 272 C ATOM 457 CG LYS A 56 -32.903 -2.417 35.051 1.00 47.95 C ANISOU 457 CG LYS A 56 6086 5276 6856 732 639 157 C ATOM 458 CD LYS A 56 -32.404 -3.509 34.119 1.00 52.50 C ANISOU 458 CD LYS A 56 6715 5576 7657 684 717 110 C ATOM 459 CE LYS A 56 -33.373 -3.740 32.971 1.00 54.44 C ANISOU 459 CE LYS A 56 7030 5788 7864 544 780 -8 C ATOM 460 NZ LYS A 56 -32.985 -4.917 32.146 1.00 64.01 N ANISOU 460 NZ LYS A 56 8275 6744 9300 470 877 -101 N ATOM 461 N VAL A 57 -31.538 0.737 36.919 1.00 48.34 N ANISOU 461 N VAL A 57 5998 5748 6622 967 496 17 N ATOM 462 CA VAL A 57 -31.475 2.123 36.468 1.00 55.39 C ANISOU 462 CA VAL A 57 6938 6637 7471 1002 467 -155 C ATOM 463 C VAL A 57 -30.378 2.291 35.419 1.00 70.24 C ANISOU 463 C VAL A 57 8913 8331 9443 966 509 -221 C ATOM 464 O VAL A 57 -29.211 1.996 35.677 1.00100.28 O ANISOU 464 O VAL A 57 12664 12119 13319 986 539 -209 O ATOM 465 CB VAL A 57 -31.219 3.090 37.641 1.00 59.64 C ANISOU 465 CB VAL A 57 7382 7374 7906 1062 418 -225 C ATOM 466 CG1 VAL A 57 -30.961 4.494 37.126 1.00 49.88 C ANISOU 466 CG1 VAL A 57 6223 6044 6686 1090 373 -393 C ATOM 467 CG2 VAL A 57 -32.393 3.078 38.612 1.00 52.10 C ANISOU 467 CG2 VAL A 57 6308 6669 6821 1057 404 -236 C ATOM 468 N VAL A 58 -30.760 2.763 34.236 1.00 52.34 N ANISOU 468 N VAL A 58 6769 5956 7163 894 503 -293 N ATOM 469 CA VAL A 58 -29.831 2.887 33.116 1.00 45.84 C ANISOU 469 CA VAL A 58 6041 5010 6367 782 566 -368 C ATOM 470 C VAL A 58 -29.769 4.320 32.587 1.00 52.66 C ANISOU 470 C VAL A 58 7032 5831 7145 716 481 -425 C ATOM 471 O VAL A 58 -30.791 4.998 32.495 1.00 52.00 O ANISOU 471 O VAL A 58 7004 5731 7025 751 358 -407 O ATOM 472 CB VAL A 58 -30.225 1.939 31.957 1.00 42.15 C ANISOU 472 CB VAL A 58 5634 4453 5929 661 643 -383 C ATOM 473 CG1 VAL A 58 -29.211 2.014 30.824 1.00 40.48 C ANISOU 473 CG1 VAL A 58 5487 4183 5708 497 743 -509 C ATOM 474 CG2 VAL A 58 -30.356 0.509 32.458 1.00 41.42 C ANISOU 474 CG2 VAL A 58 5441 4329 5968 716 705 -318 C ATOM 475 N LYS A 59 -28.567 4.778 32.250 1.00 61.38 N ANISOU 475 N LYS A 59 8174 6910 8239 617 531 -495 N ATOM 476 CA LYS A 59 -28.398 6.078 31.609 1.00 61.95 C ANISOU 476 CA LYS A 59 8409 6901 8227 486 446 -514 C ATOM 477 C LYS A 59 -28.744 5.986 30.126 1.00 71.86 C ANISOU 477 C LYS A 59 9826 8092 9385 274 443 -481 C ATOM 478 O LYS A 59 -28.322 5.055 29.440 1.00 72.66 O ANISOU 478 O LYS A 59 9898 8236 9473 151 593 -545 O ATOM 479 CB LYS A 59 -26.966 6.589 31.786 1.00 59.39 C ANISOU 479 CB LYS A 59 8060 6611 7895 394 516 -606 C ATOM 480 CG LYS A 59 -26.674 7.886 31.045 1.00 51.71 C ANISOU 480 CG LYS A 59 7289 5533 6827 186 435 -602 C ATOM 481 CD LYS A 59 -25.194 8.228 31.088 1.00 58.09 C ANISOU 481 CD LYS A 59 8052 6416 7605 31 545 -718 C ATOM 482 CE LYS A 59 -24.889 9.470 30.266 1.00 71.34 C ANISOU 482 CE LYS A 59 9963 7980 9164 -252 468 -683 C ATOM 483 NZ LYS A 59 -23.438 9.806 30.281 1.00 65.76 N ANISOU 483 NZ LYS A 59 9196 7384 8407 -453 596 -818 N ATOM 484 N GLY A 60 -29.513 6.953 29.637 1.00 79.73 N ANISOU 484 N GLY A 60 10983 8987 10323 228 259 -392 N ATOM 485 CA GLY A 60 -29.918 6.973 28.243 1.00 81.92 C ANISOU 485 CA GLY A 60 11430 9234 10464 -3 202 -315 C ATOM 486 C GLY A 60 -29.063 7.895 27.395 1.00 77.70 C ANISOU 486 C GLY A 60 11090 8649 9785 -299 171 -279 C ATOM 487 O GLY A 60 -27.875 8.078 27.661 1.00 79.42 O ANISOU 487 O GLY A 60 11269 8910 9998 -381 301 -379 O ATOM 488 N GLY A 61 -29.672 8.473 26.364 1.00 72.25 N ANISOU 488 N GLY A 61 10607 7885 8962 -486 -15 -121 N ATOM 489 CA GLY A 61 -28.972 9.378 25.472 1.00 74.93 C ANISOU 489 CA GLY A 61 11176 8178 9118 -839 -80 -25 C ATOM 490 C GLY A 61 -28.577 10.675 26.150 1.00 82.68 C ANISOU 490 C GLY A 61 12243 8956 10214 -774 -226 22 C ATOM 491 O GLY A 61 -29.224 11.113 27.101 1.00 82.35 O ANISOU 491 O GLY A 61 12129 8772 10390 -450 -369 15 O ATOM 492 N SER A 62 -27.509 11.291 25.655 1.00 87.52 N ANISOU 492 N SER A 62 13002 9574 10678 -1112 -175 37 N ATOM 493 CA SER A 62 -27.014 12.540 26.221 1.00 86.52 C ANISOU 493 CA SER A 62 12979 9240 10653 -1119 -299 66 C ATOM 494 C SER A 62 -26.545 13.494 25.127 1.00 95.82 C ANISOU 494 C SER A 62 14476 10318 11615 -1588 -430 268 C ATOM 495 O SER A 62 -25.952 13.071 24.134 1.00 99.61 O ANISOU 495 O SER A 62 15012 11026 11809 -1980 -268 264 O ATOM 496 CB SER A 62 -25.874 12.265 27.203 1.00 94.76 C ANISOU 496 CB SER A 62 13799 10435 11770 -1036 -44 -183 C ATOM 497 OG SER A 62 -24.812 11.573 26.570 1.00104.15 O ANISOU 497 OG SER A 62 14913 11888 12772 -1328 226 -313 O ATOM 498 N SER A 63 -26.817 14.782 25.314 1.00107.05 N ANISOU 498 N SER A 63 16103 11395 13176 -1568 -725 433 N ATOM 499 CA SER A 63 -26.420 15.798 24.347 1.00119.64 C ANISOU 499 CA SER A 63 18046 12827 14586 -2033 -910 690 C ATOM 500 C SER A 63 -25.816 17.017 25.036 1.00126.01 C ANISOU 500 C SER A 63 18960 13343 15575 -2055 -1010 670 C ATOM 501 O SER A 63 -26.451 17.635 25.891 1.00125.04 O ANISOU 501 O SER A 63 18807 12914 15789 -1681 -1214 636 O ATOM 502 CB SER A 63 -27.616 16.223 23.495 1.00125.14 C ANISOU 502 CB SER A 63 18982 13294 15272 -2059 -1304 1036 C ATOM 503 OG SER A 63 -28.645 16.771 24.300 1.00121.21 O ANISOU 503 OG SER A 63 18430 12456 15169 -1578 -1586 1047 O ATOM 504 N GLY A 64 -24.587 17.356 24.661 1.00131.45 N ANISOU 504 N GLY A 64 19755 14148 16042 -2514 -852 651 N ATOM 505 CA GLY A 64 -23.926 18.528 25.202 1.00135.67 C ANISOU 505 CA GLY A 64 20418 14417 16715 -2626 -937 632 C ATOM 506 C GLY A 64 -24.597 19.808 24.746 1.00144.64 C ANISOU 506 C GLY A 64 21938 15031 17987 -2729 -1394 989 C ATOM 507 O GLY A 64 -24.752 20.042 23.547 1.00147.42 O ANISOU 507 O GLY A 64 22583 15340 18090 -3130 -1574 1327 O ATOM 508 N LYS A 65 -24.993 20.642 25.702 1.00147.95 N ANISOU 508 N LYS A 65 22353 15052 18810 -2379 -1597 908 N ATOM 509 CA LYS A 65 -25.662 21.899 25.390 1.00157.92 C ANISOU 509 CA LYS A 65 23952 15727 20322 -2393 -2072 1210 C ATOM 510 C LYS A 65 -24.652 23.041 25.352 1.00159.55 C ANISOU 510 C LYS A 65 24432 15667 20524 -2827 -2128 1280 C ATOM 511 O LYS A 65 -23.942 23.289 26.327 1.00152.45 O ANISOU 511 O LYS A 65 23374 14793 19755 -2753 -1930 958 O ATOM 512 CB LYS A 65 -26.767 22.188 26.412 1.00162.86 C ANISOU 512 CB LYS A 65 24394 16040 21445 -1750 -2277 1029 C ATOM 513 CG LYS A 65 -27.963 22.962 25.862 1.00167.20 C ANISOU 513 CG LYS A 65 25178 16074 22278 -1595 -2806 1352 C ATOM 514 CD LYS A 65 -27.647 24.435 25.645 1.00172.83 C ANISOU 514 CD LYS A 65 26188 16303 23178 -1814 -3103 1544 C ATOM 515 CE LYS A 65 -28.841 25.179 25.070 1.00173.18 C ANISOU 515 CE LYS A 65 26280 16050 23471 -1576 -3563 1814 C ATOM 516 NZ LYS A 65 -28.543 26.621 24.852 1.00177.16 N ANISOU 516 NZ LYS A 65 26995 16171 24147 -1749 -3812 1976 N ATOM 517 N GLY A 66 -24.593 23.731 24.217 1.00165.43 N ANISOU 517 N GLY A 66 25591 16172 21093 -3313 -2409 1715 N ATOM 518 CA GLY A 66 -23.669 24.836 24.044 1.00167.18 C ANISOU 518 CA GLY A 66 25986 16281 21253 -3702 -2432 1790 C ATOM 519 C GLY A 66 -23.983 26.030 24.924 1.00176.15 C ANISOU 519 C GLY A 66 27125 16889 22915 -3345 -2676 1681 C ATOM 520 O GLY A 66 -25.092 26.565 24.894 1.00175.52 O ANISOU 520 O GLY A 66 27066 16452 23174 -2963 -3039 1817 O ATOM 521 N THR A 67 -22.997 26.447 25.710 1.00186.74 N ANISOU 521 N THR A 67 28414 18213 24327 -3478 -2462 1397 N ATOM 522 CA THR A 67 -23.108 27.650 26.527 1.00201.42 C ANISOU 522 CA THR A 67 30278 19600 26652 -3235 -2640 1245 C ATOM 523 C THR A 67 -21.917 28.553 26.231 1.00220.28 C ANISOU 523 C THR A 67 32861 21963 28871 -3785 -2571 1326 C ATOM 524 O THR A 67 -22.067 29.628 25.651 1.00229.46 O ANISOU 524 O THR A 67 34270 22784 30131 -3930 -2869 1623 O ATOM 525 CB THR A 67 -23.162 27.325 28.031 1.00192.49 C ANISOU 525 CB THR A 67 28842 18462 25832 -2796 -2453 720 C ATOM 526 OG1 THR A 67 -24.266 26.449 28.294 1.00188.43 O ANISOU 526 OG1 THR A 67 28133 18014 25446 -2299 -2505 639 O ATOM 527 CG2 THR A 67 -23.329 28.598 28.844 1.00190.76 C ANISOU 527 CG2 THR A 67 28605 17781 26092 -2559 -2616 515 C ATOM 528 N THR A 68 -20.733 28.104 26.635 1.00228.44 N ANISOU 528 N THR A 68 33769 23377 29653 -4093 -2184 1050 N ATOM 529 CA THR A 68 -19.488 28.718 26.193 1.00234.31 C ANISOU 529 CA THR A 68 34650 24266 30110 -4695 -2049 1121 C ATOM 530 C THR A 68 -19.064 28.015 24.910 1.00230.68 C ANISOU 530 C THR A 68 34273 24306 29068 -5174 -1908 1382 C ATOM 531 O THR A 68 -19.135 28.580 23.819 1.00238.63 O ANISOU 531 O THR A 68 35555 25249 29866 -5497 -2128 1775 O ATOM 532 CB THR A 68 -18.381 28.608 27.256 1.00238.03 C ANISOU 532 CB THR A 68 34885 24973 30584 -4802 -1696 650 C ATOM 533 OG1 THR A 68 -18.082 27.227 27.494 1.00232.14 O ANISOU 533 OG1 THR A 68 33868 24752 29584 -4772 -1359 404 O ATOM 534 CG2 THR A 68 -18.830 29.254 28.557 1.00240.19 C ANISOU 534 CG2 THR A 68 35053 24811 31399 -4337 -1818 327 C ATOM 535 N LEU A 69 -18.625 26.770 25.061 1.00208.71 N ANISOU 535 N LEU A 69 31234 22039 26026 -5221 -1537 1128 N ATOM 536 CA LEU A 69 -18.505 25.845 23.943 1.00186.77 C ANISOU 536 CA LEU A 69 28450 19750 22763 -5534 -1379 1281 C ATOM 537 C LEU A 69 -19.260 24.579 24.334 1.00181.74 C ANISOU 537 C LEU A 69 27595 19234 22223 -5112 -1275 1119 C ATOM 538 O LEU A 69 -20.325 24.288 23.788 1.00182.07 O ANISOU 538 O LEU A 69 27738 19155 22283 -4910 -1506 1375 O ATOM 539 CB LEU A 69 -17.039 25.553 23.611 1.00175.82 C ANISOU 539 CB LEU A 69 26919 18948 20936 -6084 -966 1075 C ATOM 540 CG LEU A 69 -16.176 24.881 24.684 1.00161.53 C ANISOU 540 CG LEU A 69 24718 17463 19193 -5997 -566 562 C ATOM 541 CD1 LEU A 69 -16.426 23.381 24.722 1.00147.26 C ANISOU 541 CD1 LEU A 69 22619 16034 17298 -5789 -313 355 C ATOM 542 CD2 LEU A 69 -14.704 25.177 24.446 1.00163.69 C ANISOU 542 CD2 LEU A 69 24886 18163 19147 -6522 -277 389 C ATOM 543 N ARG A 70 -18.705 23.831 25.284 1.00177.12 N ANISOU 543 N ARG A 70 26638 18966 21693 -4903 -929 679 N ATOM 544 CA ARG A 70 -19.480 22.848 26.029 1.00170.13 C ANISOU 544 CA ARG A 70 25397 18225 21018 -4213 -854 463 C ATOM 545 C ARG A 70 -19.391 23.183 27.518 1.00172.38 C ANISOU 545 C ARG A 70 25450 18377 21668 -3783 -825 121 C ATOM 546 O ARG A 70 -18.342 23.012 28.146 1.00168.53 O ANISOU 546 O ARG A 70 24709 18215 21109 -3872 -542 -190 O ATOM 547 CB ARG A 70 -18.972 21.432 25.736 1.00161.37 C ANISOU 547 CB ARG A 70 23944 17764 19607 -4238 -459 254 C ATOM 548 CG ARG A 70 -19.723 20.314 26.442 1.00151.69 C ANISOU 548 CG ARG A 70 22370 16697 18567 -3591 -374 67 C ATOM 549 CD ARG A 70 -19.142 18.960 26.052 1.00146.13 C ANISOU 549 CD ARG A 70 21359 16558 17606 -3663 -9 -131 C ATOM 550 NE ARG A 70 -19.842 17.861 26.715 1.00140.64 N ANISOU 550 NE ARG A 70 20361 15984 17092 -3085 58 -275 N ATOM 551 CZ ARG A 70 -19.548 17.404 27.929 1.00141.59 C ANISOU 551 CZ ARG A 70 20145 16251 17401 -2705 197 -551 C ATOM 552 NH1 ARG A 70 -18.562 17.952 28.627 1.00146.91 N ANISOU 552 NH1 ARG A 70 20717 16990 18113 -2816 287 -743 N ATOM 553 NH2 ARG A 70 -20.242 16.401 28.447 1.00133.16 N ANISOU 553 NH2 ARG A 70 18848 15280 16465 -2245 234 -621 N ATOM 554 N GLY A 71 -20.483 23.704 28.069 1.00183.83 N ANISOU 554 N GLY A 71 26975 19366 23506 -3340 -1127 162 N ATOM 555 CA GLY A 71 -20.562 23.968 29.494 1.00186.46 C ANISOU 555 CA GLY A 71 27065 19615 24167 -2916 -1096 -199 C ATOM 556 C GLY A 71 -21.464 23.021 30.257 1.00184.89 C ANISOU 556 C GLY A 71 26525 19618 24108 -2306 -1032 -382 C ATOM 557 O GLY A 71 -21.396 22.935 31.483 1.00183.90 O ANISOU 557 O GLY A 71 26117 19621 24136 -1996 -917 -717 O ATOM 558 N ARG A 72 -22.309 22.300 29.526 1.00174.04 N ANISOU 558 N ARG A 72 25177 18302 22650 -2175 -1106 -159 N ATOM 559 CA ARG A 72 -23.364 21.510 30.147 1.00145.71 C ANISOU 559 CA ARG A 72 21318 14828 19216 -1628 -1102 -282 C ATOM 560 C ARG A 72 -23.870 20.415 29.213 1.00139.20 C ANISOU 560 C ARG A 72 20476 14249 18165 -1631 -1054 -74 C ATOM 561 O ARG A 72 -23.635 20.459 28.005 1.00146.48 O ANISOU 561 O ARG A 72 21645 15166 18846 -2035 -1104 199 O ATOM 562 CB ARG A 72 -24.520 22.421 30.572 1.00138.46 C ANISOU 562 CB ARG A 72 20489 13401 18717 -1277 -1448 -291 C ATOM 563 CG ARG A 72 -25.321 21.911 31.757 1.00128.53 C ANISOU 563 CG ARG A 72 18870 12308 17659 -740 -1374 -603 C ATOM 564 CD ARG A 72 -26.385 22.910 32.176 1.00122.97 C ANISOU 564 CD ARG A 72 18212 11109 17403 -412 -1698 -699 C ATOM 565 NE ARG A 72 -27.477 22.981 31.211 1.00122.07 N ANISOU 565 NE ARG A 72 18273 10706 17403 -311 -2018 -383 N ATOM 566 CZ ARG A 72 -28.584 22.251 31.286 1.00114.09 C ANISOU 566 CZ ARG A 72 17051 9852 16445 43 -2047 -408 C ATOM 567 NH1 ARG A 72 -28.747 21.394 32.284 1.00102.83 N ANISOU 567 NH1 ARG A 72 15258 8854 14960 307 -1770 -712 N ATOM 568 NH2 ARG A 72 -29.529 22.377 30.364 1.00114.31 N ANISOU 568 NH2 ARG A 72 17236 9625 16572 107 -2367 -111 N ATOM 569 N SER A 73 -24.565 19.434 29.778 1.00128.22 N ANISOU 569 N SER A 73 18796 13090 16832 -1218 -953 -210 N ATOM 570 CA SER A 73 -25.152 18.358 28.989 1.00120.26 C ANISOU 570 CA SER A 73 17749 12294 15651 -1187 -909 -56 C ATOM 571 C SER A 73 -26.483 17.905 29.581 1.00109.10 C ANISOU 571 C SER A 73 16145 10858 14451 -695 -1008 -123 C ATOM 572 O SER A 73 -26.685 17.963 30.793 1.00 94.11 O ANISOU 572 O SER A 73 14023 8991 12743 -377 -960 -374 O ATOM 573 CB SER A 73 -24.187 17.174 28.896 1.00123.04 C ANISOU 573 CB SER A 73 17886 13127 15738 -1337 -538 -190 C ATOM 574 OG SER A 73 -22.977 17.550 28.261 1.00132.46 O ANISOU 574 OG SER A 73 19215 14404 16711 -1824 -423 -164 O ATOM 575 N ASP A 74 -27.390 17.460 28.717 1.00116.76 N ANISOU 575 N ASP A 74 17191 11812 15359 -670 -1141 88 N ATOM 576 CA ASP A 74 -28.675 16.929 29.159 1.00116.42 C ANISOU 576 CA ASP A 74 16946 11805 15484 -253 -1216 23 C ATOM 577 C ASP A 74 -28.772 15.439 28.852 1.00111.08 C ANISOU 577 C ASP A 74 16101 11518 14586 -256 -975 16 C ATOM 578 O ASP A 74 -28.595 15.020 27.708 1.00119.86 O ANISOU 578 O ASP A 74 17354 12726 15460 -551 -947 192 O ATOM 579 CB ASP A 74 -29.832 17.681 28.496 1.00128.53 C ANISOU 579 CB ASP A 74 18669 12968 17200 -163 -1625 249 C ATOM 580 CG ASP A 74 -29.912 19.131 28.931 1.00135.61 C ANISOU 580 CG ASP A 74 19697 13398 18431 -66 -1901 212 C ATOM 581 OD1 ASP A 74 -30.553 19.409 29.966 1.00134.10 O ANISOU 581 OD1 ASP A 74 19286 13120 18545 324 -1947 -56 O ATOM 582 OD2 ASP A 74 -29.337 19.995 28.235 1.00141.50 O ANISOU 582 OD2 ASP A 74 20765 13862 19136 -403 -2069 436 O ATOM 583 N ALA A 75 -29.051 14.641 29.877 1.00 86.94 N ANISOU 583 N ALA A 75 12746 8686 11602 45 -802 -192 N ATOM 584 CA ALA A 75 -29.136 13.196 29.708 1.00 75.85 C ANISOU 584 CA ALA A 75 11179 7595 10045 60 -582 -208 C ATOM 585 C ALA A 75 -30.458 12.644 30.229 1.00 70.97 C ANISOU 585 C ALA A 75 10371 7044 9551 387 -638 -258 C ATOM 586 O ALA A 75 -31.143 13.289 31.021 1.00 78.64 O ANISOU 586 O ALA A 75 11251 7903 10727 640 -776 -367 O ATOM 587 CB ALA A 75 -27.969 12.515 30.405 1.00 72.86 C ANISOU 587 CB ALA A 75 10618 7471 9593 28 -289 -376 C ATOM 588 N ASP A 76 -30.810 11.448 29.771 1.00 61.48 N ANISOU 588 N ASP A 76 9095 6035 8229 359 -519 -211 N ATOM 589 CA ASP A 76 -32.031 10.784 30.211 1.00 72.54 C ANISOU 589 CA ASP A 76 10307 7544 9709 606 -539 -256 C ATOM 590 C ASP A 76 -31.706 9.583 31.091 1.00 66.96 C ANISOU 590 C ASP A 76 9380 7096 8967 689 -276 -371 C ATOM 591 O ASP A 76 -30.886 8.741 30.728 1.00 72.65 O ANISOU 591 O ASP A 76 10104 7919 9580 534 -91 -357 O ATOM 592 CB ASP A 76 -32.869 10.340 29.008 1.00 94.57 C ANISOU 592 CB ASP A 76 13189 10336 12405 497 -647 -99 C ATOM 593 CG ASP A 76 -33.362 11.507 28.176 1.00109.52 C ANISOU 593 CG ASP A 76 15297 11968 14348 436 -984 74 C ATOM 594 OD1 ASP A 76 -33.621 12.584 28.753 1.00119.70 O ANISOU 594 OD1 ASP A 76 16585 13039 15856 623 -1175 25 O ATOM 595 OD2 ASP A 76 -33.494 11.346 26.944 1.00107.02 O ANISOU 595 OD2 ASP A 76 15149 11657 13858 191 -1071 256 O ATOM 596 N LEU A 77 -32.347 9.510 32.252 1.00 58.55 N ANISOU 596 N LEU A 77 8113 6137 7997 923 -271 -489 N ATOM 597 CA LEU A 77 -32.161 8.377 33.149 1.00 53.80 C ANISOU 597 CA LEU A 77 7320 5774 7348 980 -73 -536 C ATOM 598 C LEU A 77 -33.451 7.574 33.264 1.00 60.74 C ANISOU 598 C LEU A 77 8070 6781 8229 1069 -75 -523 C ATOM 599 O LEU A 77 -34.421 8.032 33.864 1.00 76.81 O ANISOU 599 O LEU A 77 9976 8872 10335 1224 -167 -628 O ATOM 600 CB LEU A 77 -31.707 8.851 34.529 1.00 53.49 C ANISOU 600 CB LEU A 77 7142 5844 7337 1090 -33 -678 C ATOM 601 CG LEU A 77 -31.197 7.749 35.458 1.00 60.05 C ANISOU 601 CG LEU A 77 7812 6915 8090 1096 134 -661 C ATOM 602 CD1 LEU A 77 -29.894 7.176 34.923 1.00 80.04 C ANISOU 602 CD1 LEU A 77 10410 9409 10593 960 243 -586 C ATOM 603 CD2 LEU A 77 -31.022 8.266 36.876 1.00 48.20 C ANISOU 603 CD2 LEU A 77 6156 5592 6565 1183 142 -804 C ATOM 604 N VAL A 78 -33.457 6.372 32.697 1.00 60.55 N ANISOU 604 N VAL A 78 8059 6808 8138 959 37 -431 N ATOM 605 CA VAL A 78 -34.662 5.550 32.689 1.00 64.93 C ANISOU 605 CA VAL A 78 8508 7478 8684 988 42 -413 C ATOM 606 C VAL A 78 -34.702 4.588 33.876 1.00 67.92 C ANISOU 606 C VAL A 78 8717 8050 9040 1028 182 -415 C ATOM 607 O VAL A 78 -33.801 3.770 34.067 1.00 56.53 O ANISOU 607 O VAL A 78 7284 6604 7592 967 303 -348 O ATOM 608 CB VAL A 78 -34.793 4.752 31.367 1.00 44.85 C ANISOU 608 CB VAL A 78 6080 4876 6083 812 76 -329 C ATOM 609 CG1 VAL A 78 -33.455 4.159 30.951 1.00 57.32 C ANISOU 609 CG1 VAL A 78 7744 6398 7639 670 237 -317 C ATOM 610 CG2 VAL A 78 -35.859 3.672 31.493 1.00 45.65 C ANISOU 610 CG2 VAL A 78 6061 5109 6175 804 129 -320 C ATOM 611 N VAL A 79 -35.754 4.706 34.679 1.00 65.86 N ANISOU 611 N VAL A 79 8289 7964 8770 1120 149 -494 N ATOM 612 CA VAL A 79 -35.953 3.828 35.825 1.00 58.93 C ANISOU 612 CA VAL A 79 7259 7316 7816 1094 262 -466 C ATOM 613 C VAL A 79 -36.896 2.688 35.460 1.00 53.38 C ANISOU 613 C VAL A 79 6522 6675 7085 988 311 -388 C ATOM 614 O VAL A 79 -38.058 2.915 35.127 1.00 51.51 O ANISOU 614 O VAL A 79 6205 6512 6854 1009 244 -474 O ATOM 615 CB VAL A 79 -36.518 4.594 37.035 1.00 67.48 C ANISOU 615 CB VAL A 79 8147 8636 8855 1192 239 -644 C ATOM 616 CG1 VAL A 79 -36.804 3.639 38.183 1.00 81.11 C ANISOU 616 CG1 VAL A 79 9729 10658 10431 1086 352 -580 C ATOM 617 CG2 VAL A 79 -35.553 5.686 37.468 1.00 61.62 C ANISOU 617 CG2 VAL A 79 7437 7830 8145 1272 201 -746 C ATOM 618 N PHE A 80 -36.390 1.461 35.521 1.00 49.24 N ANISOU 618 N PHE A 80 6047 6105 6557 876 414 -236 N ATOM 619 CA PHE A 80 -37.173 0.295 35.133 1.00 54.13 C ANISOU 619 CA PHE A 80 6662 6730 7175 740 470 -163 C ATOM 620 C PHE A 80 -37.968 -0.279 36.299 1.00 65.15 C ANISOU 620 C PHE A 80 7905 8388 8461 656 516 -115 C ATOM 621 O PHE A 80 -37.427 -0.512 37.379 1.00 77.99 O ANISOU 621 O PHE A 80 9494 10114 10023 636 543 -14 O ATOM 622 CB PHE A 80 -36.263 -0.783 34.543 1.00 55.24 C ANISOU 622 CB PHE A 80 6934 6633 7423 655 548 -53 C ATOM 623 CG PHE A 80 -35.659 -0.406 33.223 1.00 56.29 C ANISOU 623 CG PHE A 80 7200 6577 7613 647 542 -134 C ATOM 624 CD1 PHE A 80 -34.461 0.286 33.166 1.00 71.80 C ANISOU 624 CD1 PHE A 80 9219 8457 9605 715 535 -166 C ATOM 625 CD2 PHE A 80 -36.290 -0.741 32.038 1.00 54.88 C ANISOU 625 CD2 PHE A 80 7084 6344 7425 528 547 -185 C ATOM 626 CE1 PHE A 80 -33.903 0.636 31.952 1.00 72.20 C ANISOU 626 CE1 PHE A 80 9391 8382 9660 641 545 -240 C ATOM 627 CE2 PHE A 80 -35.738 -0.395 30.822 1.00 56.42 C ANISOU 627 CE2 PHE A 80 7403 6424 7609 457 546 -254 C ATOM 628 CZ PHE A 80 -34.543 0.294 30.778 1.00 64.14 C ANISOU 628 CZ PHE A 80 8442 7328 8601 503 551 -279 C ATOM 629 N LEU A 81 -39.257 -0.507 36.066 1.00 60.71 N ANISOU 629 N LEU A 81 7246 7967 7853 577 519 -183 N ATOM 630 CA LEU A 81 -40.130 -1.097 37.073 1.00 55.76 C ANISOU 630 CA LEU A 81 6464 7636 7088 427 585 -154 C ATOM 631 C LEU A 81 -40.638 -2.456 36.607 1.00 54.47 C ANISOU 631 C LEU A 81 6363 7390 6945 210 649 -23 C ATOM 632 O LEU A 81 -40.715 -2.720 35.407 1.00 68.71 O ANISOU 632 O LEU A 81 8265 8988 8853 198 636 -53 O ATOM 633 CB LEU A 81 -41.308 -0.170 37.386 1.00 53.03 C ANISOU 633 CB LEU A 81 5878 7598 6672 497 551 -410 C ATOM 634 CG LEU A 81 -40.982 1.196 37.996 1.00 53.29 C ANISOU 634 CG LEU A 81 5814 7723 6713 701 492 -602 C ATOM 635 CD1 LEU A 81 -40.774 2.250 36.916 1.00 67.67 C ANISOU 635 CD1 LEU A 81 7728 9272 8713 912 345 -703 C ATOM 636 CD2 LEU A 81 -42.069 1.624 38.965 1.00 51.45 C ANISOU 636 CD2 LEU A 81 5276 7908 6364 681 536 -852 C ATOM 637 N THR A 82 -40.979 -3.316 37.560 1.00 46.09 N ANISOU 637 N THR A 82 5251 6496 5767 5 715 121 N ATOM 638 CA THR A 82 -41.438 -4.664 37.242 1.00 58.26 C ANISOU 638 CA THR A 82 6868 7922 7344 -237 772 265 C ATOM 639 C THR A 82 -42.890 -4.889 37.643 1.00 69.03 C ANISOU 639 C THR A 82 8041 9656 8531 -457 832 180 C ATOM 640 O THR A 82 -43.548 -3.990 38.169 1.00 70.42 O ANISOU 640 O THR A 82 7996 10192 8570 -398 834 -23 O ATOM 641 CB THR A 82 -40.568 -5.729 37.932 1.00 49.58 C ANISOU 641 CB THR A 82 5915 6624 6298 -355 771 577 C ATOM 642 OG1 THR A 82 -40.484 -5.445 39.334 1.00 54.43 O ANISOU 642 OG1 THR A 82 6434 7551 6698 -417 758 682 O ATOM 643 CG2 THR A 82 -39.171 -5.738 37.339 1.00 50.90 C ANISOU 643 CG2 THR A 82 6239 6403 6700 -153 725 619 C ATOM 644 N LYS A 83 -43.375 -6.101 37.381 1.00 67.86 N ANISOU 644 N LYS A 83 7964 9412 8406 -719 887 304 N ATOM 645 CA LYS A 83 -44.728 -6.522 37.737 1.00 70.00 C ANISOU 645 CA LYS A 83 8062 10033 8502 -1004 963 244 C ATOM 646 C LYS A 83 -45.812 -5.638 37.122 1.00 72.70 C ANISOU 646 C LYS A 83 8161 10650 8813 -893 945 -95 C ATOM 647 O LYS A 83 -46.883 -5.461 37.703 1.00 90.13 O ANISOU 647 O LYS A 83 10108 13288 10849 -1030 1002 -252 O ATOM 648 CB LYS A 83 -44.887 -6.561 39.259 1.00 74.15 C ANISOU 648 CB LYS A 83 8477 10927 8769 -1197 1013 359 C ATOM 649 CG LYS A 83 -43.986 -7.575 39.942 1.00 68.22 C ANISOU 649 CG LYS A 83 7960 9929 8032 -1365 982 763 C ATOM 650 CD LYS A 83 -44.266 -8.983 39.442 1.00 62.15 C ANISOU 650 CD LYS A 83 7363 8850 7399 -1638 1001 959 C ATOM 651 CE LYS A 83 -43.401 -10.004 40.161 1.00 66.76 C ANISOU 651 CE LYS A 83 8178 9134 8054 -1788 917 1390 C ATOM 652 NZ LYS A 83 -43.635 -9.990 41.632 1.00 82.71 N ANISOU 652 NZ LYS A 83 10121 11585 9721 -2059 915 1595 N ATOM 653 N LEU A 84 -45.530 -5.088 35.946 1.00 63.40 N ANISOU 653 N LEU A 84 7054 9236 7799 -658 852 -208 N ATOM 654 CA LEU A 84 -46.536 -4.349 35.193 1.00 64.80 C ANISOU 654 CA LEU A 84 7030 9603 7987 -551 770 -470 C ATOM 655 C LEU A 84 -47.129 -5.247 34.115 1.00 61.20 C ANISOU 655 C LEU A 84 6631 9051 7570 -759 784 -473 C ATOM 656 O LEU A 84 -46.425 -6.064 33.522 1.00 61.75 O ANISOU 656 O LEU A 84 6949 8774 7740 -852 822 -332 O ATOM 657 CB LEU A 84 -45.943 -3.085 34.570 1.00 60.51 C ANISOU 657 CB LEU A 84 6534 8891 7565 -204 617 -565 C ATOM 658 CG LEU A 84 -45.401 -2.022 35.528 1.00 56.19 C ANISOU 658 CG LEU A 84 5915 8428 7007 20 588 -628 C ATOM 659 CD1 LEU A 84 -44.937 -0.798 34.756 1.00 48.85 C ANISOU 659 CD1 LEU A 84 5053 7289 6220 317 415 -712 C ATOM 660 CD2 LEU A 84 -46.448 -1.642 36.563 1.00 55.66 C ANISOU 660 CD2 LEU A 84 5508 8822 6817 -15 638 -848 C ATOM 661 N THR A 85 -48.426 -5.097 33.871 1.00 72.74 N ANISOU 661 N THR A 85 7836 10837 8966 -834 755 -670 N ATOM 662 CA THR A 85 -49.130 -5.958 32.927 1.00 79.47 C ANISOU 662 CA THR A 85 8700 11678 9819 -1078 773 -703 C ATOM 663 C THR A 85 -48.779 -5.640 31.477 1.00 89.67 C ANISOU 663 C THR A 85 10140 12724 11209 -947 637 -736 C ATOM 664 O THR A 85 -48.513 -6.543 30.682 1.00 88.30 O ANISOU 664 O THR A 85 10155 12322 11073 -1140 696 -683 O ATOM 665 CB THR A 85 -50.653 -5.845 33.103 1.00 74.39 C ANISOU 665 CB THR A 85 7687 11512 9065 -1202 768 -929 C ATOM 666 OG1 THR A 85 -50.996 -6.084 34.474 1.00 67.55 O ANISOU 666 OG1 THR A 85 6663 10951 8053 -1377 915 -927 O ATOM 667 CG2 THR A 85 -51.366 -6.857 32.219 1.00 89.57 C ANISOU 667 CG2 THR A 85 9622 13445 10965 -1517 805 -959 C ATOM 668 N SER A 86 -48.774 -4.356 31.136 1.00 90.35 N ANISOU 668 N SER A 86 10142 12855 11334 -643 451 -828 N ATOM 669 CA SER A 86 -48.553 -3.942 29.755 1.00 74.09 C ANISOU 669 CA SER A 86 8212 10629 9309 -565 287 -832 C ATOM 670 C SER A 86 -47.643 -2.724 29.641 1.00 65.28 C ANISOU 670 C SER A 86 7218 9319 8268 -257 142 -778 C ATOM 671 O SER A 86 -47.361 -2.048 30.631 1.00 67.58 O ANISOU 671 O SER A 86 7434 9639 8604 -60 145 -793 O ATOM 672 CB SER A 86 -49.890 -3.648 29.075 1.00 77.48 C ANISOU 672 CB SER A 86 8388 11355 9697 -589 114 -988 C ATOM 673 OG SER A 86 -50.579 -2.604 29.739 1.00 81.18 O ANISOU 673 OG SER A 86 8554 12069 10224 -332 -20 -1131 O ATOM 674 N PHE A 87 -47.189 -2.456 28.421 1.00 55.47 N ANISOU 674 N PHE A 87 6163 7898 7016 -260 23 -725 N ATOM 675 CA PHE A 87 -46.347 -1.299 28.136 1.00 51.67 C ANISOU 675 CA PHE A 87 5825 7224 6583 -35 -132 -653 C ATOM 676 C PHE A 87 -47.078 0.011 28.415 1.00 63.42 C ANISOU 676 C PHE A 87 7097 8839 8159 249 -385 -732 C ATOM 677 O PHE A 87 -46.460 1.010 28.780 1.00 63.02 O ANISOU 677 O PHE A 87 7105 8639 8201 474 -474 -706 O ATOM 678 CB PHE A 87 -45.877 -1.327 26.679 1.00 50.73 C ANISOU 678 CB PHE A 87 5934 6966 6375 -184 -213 -584 C ATOM 679 CG PHE A 87 -44.923 -2.446 26.367 1.00 59.14 C ANISOU 679 CG PHE A 87 7207 7849 7414 -410 37 -571 C ATOM 680 CD1 PHE A 87 -45.393 -3.712 26.059 1.00 56.27 C ANISOU 680 CD1 PHE A 87 6820 7542 7018 -677 187 -649 C ATOM 681 CD2 PHE A 87 -43.555 -2.227 26.369 1.00 50.38 C ANISOU 681 CD2 PHE A 87 6295 6504 6344 -355 118 -511 C ATOM 682 CE1 PHE A 87 -44.517 -4.740 25.768 1.00 54.15 C ANISOU 682 CE1 PHE A 87 6722 7056 6795 -854 404 -681 C ATOM 683 CE2 PHE A 87 -42.674 -3.251 26.077 1.00 50.97 C ANISOU 683 CE2 PHE A 87 6511 6405 6451 -527 338 -551 C ATOM 684 CZ PHE A 87 -43.156 -4.509 25.777 1.00 51.22 C ANISOU 684 CZ PHE A 87 6517 6452 6490 -762 476 -642 C ATOM 685 N GLU A 88 -48.396 -0.004 28.241 1.00 77.64 N ANISOU 685 N GLU A 88 8632 10907 9960 239 -506 -853 N ATOM 686 CA GLU A 88 -49.219 1.189 28.413 1.00 79.62 C ANISOU 686 CA GLU A 88 8621 11270 10359 535 -781 -974 C ATOM 687 C GLU A 88 -49.235 1.664 29.865 1.00 72.63 C ANISOU 687 C GLU A 88 7531 10481 9585 739 -672 -1142 C ATOM 688 O GLU A 88 -49.501 2.835 30.142 1.00 66.15 O ANISOU 688 O GLU A 88 6551 9635 8949 1042 -876 -1265 O ATOM 689 CB GLU A 88 -50.647 0.916 27.931 1.00 95.82 C ANISOU 689 CB GLU A 88 10380 13635 12393 461 -917 -1101 C ATOM 690 CG GLU A 88 -51.523 2.152 27.808 1.00109.11 C ANISOU 690 CG GLU A 88 11783 15391 14284 792 -1282 -1220 C ATOM 691 CD GLU A 88 -52.927 1.824 27.336 1.00111.15 C ANISOU 691 CD GLU A 88 11709 15996 14529 718 -1425 -1360 C ATOM 692 OE1 GLU A 88 -53.248 0.624 27.209 1.00110.44 O ANISOU 692 OE1 GLU A 88 11603 16109 14250 382 -1204 -1384 O ATOM 693 OE2 GLU A 88 -53.707 2.768 27.090 1.00115.60 O ANISOU 693 OE2 GLU A 88 12017 16612 15293 997 -1775 -1451 O ATOM 694 N ASP A 89 -48.942 0.750 30.786 1.00 67.89 N ANISOU 694 N ASP A 89 6938 9983 8874 558 -364 -1148 N ATOM 695 CA ASP A 89 -48.956 1.062 32.211 1.00 71.96 C ANISOU 695 CA ASP A 89 7259 10671 9412 663 -229 -1304 C ATOM 696 C ASP A 89 -47.934 2.132 32.581 1.00 75.38 C ANISOU 696 C ASP A 89 7832 10850 9958 916 -300 -1281 C ATOM 697 O ASP A 89 -48.173 2.938 33.478 1.00 93.34 O ANISOU 697 O ASP A 89 9883 13255 12327 1113 -317 -1500 O ATOM 698 CB ASP A 89 -48.702 -0.202 33.036 1.00 76.45 C ANISOU 698 CB ASP A 89 7883 11363 9803 359 77 -1216 C ATOM 699 CG ASP A 89 -49.876 -1.158 33.011 1.00 77.18 C ANISOU 699 CG ASP A 89 7765 11772 9786 86 173 -1301 C ATOM 700 OD1 ASP A 89 -51.013 -0.694 32.791 1.00 76.85 O ANISOU 700 OD1 ASP A 89 7408 11987 9803 178 40 -1523 O ATOM 701 OD2 ASP A 89 -49.662 -2.372 33.215 1.00 83.77 O ANISOU 701 OD2 ASP A 89 8742 12587 10500 -221 369 -1150 O ATOM 702 N GLN A 90 -46.800 2.144 31.887 1.00 60.03 N ANISOU 702 N GLN A 90 6240 8566 8002 890 -329 -1054 N ATOM 703 CA GLN A 90 -45.752 3.116 32.179 1.00 62.15 C ANISOU 703 CA GLN A 90 6662 8590 8362 1081 -386 -1020 C ATOM 704 C GLN A 90 -46.194 4.522 31.783 1.00 63.01 C ANISOU 704 C GLN A 90 6680 8580 8683 1367 -701 -1127 C ATOM 705 O GLN A 90 -45.678 5.512 32.300 1.00 57.58 O ANISOU 705 O GLN A 90 6008 7746 8125 1565 -764 -1203 O ATOM 706 CB GLN A 90 -44.449 2.745 31.465 1.00 67.14 C ANISOU 706 CB GLN A 90 7661 8927 8923 946 -327 -780 C ATOM 707 CG GLN A 90 -44.393 3.137 29.997 1.00 65.22 C ANISOU 707 CG GLN A 90 7603 8492 8686 917 -545 -657 C ATOM 708 CD GLN A 90 -43.094 2.723 29.333 1.00 59.22 C ANISOU 708 CD GLN A 90 7160 7512 7830 741 -434 -490 C ATOM 709 OE1 GLN A 90 -42.432 3.530 28.680 1.00 65.54 O ANISOU 709 OE1 GLN A 90 8150 8114 8639 765 -573 -397 O ATOM 710 NE2 GLN A 90 -42.726 1.457 29.492 1.00 49.76 N ANISOU 710 NE2 GLN A 90 6008 6344 6555 551 -188 -463 N ATOM 711 N LEU A 91 -47.145 4.600 30.857 1.00 68.07 N ANISOU 711 N LEU A 91 7225 9267 9373 1384 -920 -1126 N ATOM 712 CA LEU A 91 -47.705 5.878 30.434 1.00 70.53 C ANISOU 712 CA LEU A 91 7427 9441 9931 1671 -1285 -1198 C ATOM 713 C LEU A 91 -48.777 6.377 31.401 1.00 71.53 C ANISOU 713 C LEU A 91 7102 9819 10257 1915 -1317 -1568 C ATOM 714 O LEU A 91 -48.825 7.562 31.732 1.00 80.23 O ANISOU 714 O LEU A 91 8098 10757 11630 2216 -1507 -1729 O ATOM 715 CB LEU A 91 -48.285 5.763 29.023 1.00 72.25 C ANISOU 715 CB LEU A 91 7713 9627 10110 1582 -1552 -1024 C ATOM 716 CG LEU A 91 -47.299 5.371 27.921 1.00 75.02 C ANISOU 716 CG LEU A 91 8483 9773 10249 1314 -1537 -711 C ATOM 717 CD1 LEU A 91 -48.012 5.238 26.586 1.00 73.59 C ANISOU 717 CD1 LEU A 91 8326 9656 9980 1184 -1802 -572 C ATOM 718 CD2 LEU A 91 -46.167 6.384 27.829 1.00 76.05 C ANISOU 718 CD2 LEU A 91 8895 9544 10457 1409 -1646 -570 C ATOM 719 N ARG A 92 -49.635 5.465 31.850 1.00 69.03 N ANISOU 719 N ARG A 92 6509 9904 9815 1764 -1121 -1728 N ATOM 720 CA ARG A 92 -50.757 5.822 32.713 1.00 75.90 C ANISOU 720 CA ARG A 92 6892 11111 10835 1936 -1115 -2131 C ATOM 721 C ARG A 92 -50.333 6.015 34.165 1.00 79.72 C ANISOU 721 C ARG A 92 7260 11747 11283 1959 -849 -2362 C ATOM 722 O ARG A 92 -50.787 6.940 34.838 1.00 92.10 O ANISOU 722 O ARG A 92 8514 13401 13080 2223 -917 -2724 O ATOM 723 CB ARG A 92 -51.848 4.753 32.636 1.00 82.17 C ANISOU 723 CB ARG A 92 7425 12329 11467 1697 -990 -2221 C ATOM 724 CG ARG A 92 -52.283 4.402 31.224 1.00 93.16 C ANISOU 724 CG ARG A 92 8921 13646 12829 1604 -1221 -2007 C ATOM 725 CD ARG A 92 -53.370 3.344 31.246 1.00103.00 C ANISOU 725 CD ARG A 92 9885 15334 13917 1341 -1073 -2138 C ATOM 726 NE ARG A 92 -53.051 2.277 32.190 1.00113.86 N ANISOU 726 NE ARG A 92 11311 16912 15037 1017 -662 -2134 N ATOM 727 CZ ARG A 92 -53.833 1.230 32.431 1.00127.88 C ANISOU 727 CZ ARG A 92 12896 19059 16634 703 -461 -2221 C ATOM 728 NH1 ARG A 92 -54.989 1.099 31.794 1.00130.34 N ANISOU 728 NH1 ARG A 92 12923 19617 16985 674 -611 -2357 N ATOM 729 NH2 ARG A 92 -53.457 0.314 33.311 1.00135.99 N ANISOU 729 NH2 ARG A 92 14019 20209 17442 400 -129 -2154 N ATOM 730 N ARG A 93 -49.461 5.133 34.641 1.00 74.20 N ANISOU 730 N ARG A 93 6802 11084 10306 1678 -558 -2165 N ATOM 731 CA ARG A 93 -49.018 5.157 36.031 1.00 71.51 C ANISOU 731 CA ARG A 93 6374 10946 9850 1623 -305 -2325 C ATOM 732 C ARG A 93 -47.780 6.032 36.195 1.00 78.58 C ANISOU 732 C ARG A 93 7529 11481 10846 1790 -368 -2248 C ATOM 733 O ARG A 93 -47.183 6.081 37.271 1.00 91.18 O ANISOU 733 O ARG A 93 9116 13206 12325 1730 -179 -2331 O ATOM 734 CB ARG A 93 -48.738 3.737 36.527 1.00 57.07 C ANISOU 734 CB ARG A 93 4662 9338 7684 1227 -5 -2119 C ATOM 735 CG ARG A 93 -49.893 2.775 36.298 1.00 58.71 C ANISOU 735 CG ARG A 93 4664 9870 7774 993 70 -2159 C ATOM 736 CD ARG A 93 -49.591 1.386 36.834 1.00 57.68 C ANISOU 736 CD ARG A 93 4681 9890 7345 586 340 -1926 C ATOM 737 NE ARG A 93 -49.482 1.370 38.289 1.00 63.37 N ANISOU 737 NE ARG A 93 5249 10949 7881 457 547 -2056 N ATOM 738 CZ ARG A 93 -49.369 0.264 39.017 1.00 63.21 C ANISOU 738 CZ ARG A 93 5297 11135 7584 80 760 -1870 C ATOM 739 NH1 ARG A 93 -49.275 0.344 40.338 1.00 60.72 N ANISOU 739 NH1 ARG A 93 4840 11171 7060 -62 921 -1980 N ATOM 740 NH2 ARG A 93 -49.354 -0.923 38.426 1.00 58.30 N ANISOU 740 NH2 ARG A 93 4892 10366 6894 -175 799 -1575 N ATOM 741 N ARG A 94 -47.396 6.704 35.113 1.00 74.85 N ANISOU 741 N ARG A 94 7293 10583 10564 1959 -639 -2075 N ATOM 742 CA ARG A 94 -46.229 7.583 35.093 1.00 71.77 C ANISOU 742 CA ARG A 94 7172 9818 10279 2085 -726 -1982 C ATOM 743 C ARG A 94 -46.220 8.582 36.247 1.00 70.11 C ANISOU 743 C ARG A 94 6730 9681 10226 2291 -695 -2356 C ATOM 744 O ARG A 94 -45.194 8.779 36.898 1.00 92.79 O ANISOU 744 O ARG A 94 9748 12493 13013 2242 -565 -2336 O ATOM 745 CB ARG A 94 -46.165 8.335 33.762 1.00 77.62 C ANISOU 745 CB ARG A 94 8125 10143 11224 2230 -1078 -1791 C ATOM 746 CG ARG A 94 -44.909 9.166 33.571 1.00 78.00 C ANISOU 746 CG ARG A 94 8502 9788 11346 2280 -1167 -1639 C ATOM 747 CD ARG A 94 -44.962 9.935 32.263 1.00 87.31 C ANISOU 747 CD ARG A 94 9891 10585 12699 2370 -1544 -1422 C ATOM 748 NE ARG A 94 -43.693 10.587 31.957 1.00 95.96 N ANISOU 748 NE ARG A 94 11343 11317 13799 2318 -1602 -1226 N ATOM 749 CZ ARG A 94 -42.728 10.035 31.228 1.00 99.80 C ANISOU 749 CZ ARG A 94 12159 11718 14043 2046 -1508 -923 C ATOM 750 NH1 ARG A 94 -42.887 8.817 30.727 1.00103.71 N ANISOU 750 NH1 ARG A 94 12682 12423 14300 1824 -1357 -792 N ATOM 751 NH2 ARG A 94 -41.606 10.701 30.999 1.00 97.36 N ANISOU 751 NH2 ARG A 94 12133 11117 13740 1983 -1554 -786 N ATOM 752 N GLY A 95 -47.365 9.207 36.498 1.00 70.21 N ANISOU 752 N GLY A 95 6356 9841 10479 2517 -815 -2731 N ATOM 753 CA GLY A 95 -47.490 10.167 37.580 1.00 71.75 C ANISOU 753 CA GLY A 95 6270 10133 10860 2719 -775 -3187 C ATOM 754 C GLY A 95 -47.365 9.516 38.944 1.00 63.13 C ANISOU 754 C GLY A 95 5004 9548 9435 2470 -397 -3371 C ATOM 755 O GLY A 95 -46.892 10.135 39.897 1.00 64.01 O ANISOU 755 O GLY A 95 5039 9726 9555 2513 -292 -3630 O ATOM 756 N GLU A 96 -47.796 8.263 39.034 1.00 62.27 N ANISOU 756 N GLU A 96 4839 9801 9018 2177 -205 -3228 N ATOM 757 CA GLU A 96 -47.687 7.494 40.268 1.00 69.70 C ANISOU 757 CA GLU A 96 5663 11231 9589 1863 128 -3297 C ATOM 758 C GLU A 96 -46.230 7.159 40.564 1.00 75.43 C ANISOU 758 C GLU A 96 6773 11787 10100 1698 228 -2948 C ATOM 759 O GLU A 96 -45.790 7.198 41.713 1.00 74.67 O ANISOU 759 O GLU A 96 6604 11965 9801 1566 407 -3073 O ATOM 760 CB GLU A 96 -48.518 6.213 40.174 1.00 72.59 C ANISOU 760 CB GLU A 96 5919 11954 9709 1564 269 -3174 C ATOM 761 CG GLU A 96 -48.333 5.253 41.336 1.00 76.54 C ANISOU 761 CG GLU A 96 6389 12907 9785 1163 576 -3103 C ATOM 762 CD GLU A 96 -48.938 3.890 41.062 1.00 84.35 C ANISOU 762 CD GLU A 96 7397 14102 10551 827 684 -2859 C ATOM 763 OE1 GLU A 96 -49.451 3.682 39.943 1.00 87.67 O ANISOU 763 OE1 GLU A 96 7853 14324 11134 909 535 -2763 O ATOM 764 OE2 GLU A 96 -48.898 3.026 41.962 1.00 97.05 O ANISOU 764 OE2 GLU A 96 8993 16066 11813 457 904 -2750 O ATOM 765 N PHE A 97 -45.486 6.831 39.513 1.00 77.19 N ANISOU 765 N PHE A 97 7381 11589 10361 1694 109 -2530 N ATOM 766 CA PHE A 97 -44.079 6.478 39.648 1.00 53.09 C ANISOU 766 CA PHE A 97 4667 8350 7152 1562 183 -2208 C ATOM 767 C PHE A 97 -43.215 7.721 39.826 1.00 66.01 C ANISOU 767 C PHE A 97 6397 9720 8964 1768 82 -2338 C ATOM 768 O PHE A 97 -42.181 7.676 40.492 1.00 51.93 O ANISOU 768 O PHE A 97 4735 7966 7029 1667 187 -2254 O ATOM 769 CB PHE A 97 -43.609 5.677 38.431 1.00 50.37 C ANISOU 769 CB PHE A 97 4655 7684 6798 1469 118 -1792 C ATOM 770 CG PHE A 97 -44.310 4.357 38.265 1.00 59.79 C ANISOU 770 CG PHE A 97 5803 9092 7823 1226 231 -1646 C ATOM 771 CD1 PHE A 97 -44.948 3.753 39.336 1.00 52.59 C ANISOU 771 CD1 PHE A 97 4650 8635 6696 1021 417 -1762 C ATOM 772 CD2 PHE A 97 -44.326 3.718 37.036 1.00 69.43 C ANISOU 772 CD2 PHE A 97 7225 10074 9082 1160 158 -1403 C ATOM 773 CE1 PHE A 97 -45.592 2.540 39.184 1.00 54.38 C ANISOU 773 CE1 PHE A 97 4854 9033 6774 759 516 -1615 C ATOM 774 CE2 PHE A 97 -44.967 2.504 36.878 1.00 68.78 C ANISOU 774 CE2 PHE A 97 7106 10161 8866 919 264 -1294 C ATOM 775 CZ PHE A 97 -45.600 1.914 37.954 1.00 64.12 C ANISOU 775 CZ PHE A 97 6293 9983 8088 720 438 -1387 C ATOM 776 N ILE A 98 -43.646 8.828 39.228 1.00 68.49 N ANISOU 776 N ILE A 98 6653 9762 9609 2049 -144 -2533 N ATOM 777 CA ILE A 98 -42.923 10.090 39.328 1.00 67.85 C ANISOU 777 CA ILE A 98 6669 9365 9746 2239 -270 -2671 C ATOM 778 C ILE A 98 -42.842 10.551 40.782 1.00 76.23 C ANISOU 778 C ILE A 98 7473 10759 10730 2228 -95 -3068 C ATOM 779 O ILE A 98 -41.837 11.121 41.205 1.00 83.22 O ANISOU 779 O ILE A 98 8491 11517 11611 2225 -75 -3097 O ATOM 780 CB ILE A 98 -43.583 11.192 38.448 1.00 94.99 C ANISOU 780 CB ILE A 98 10068 12423 13601 2548 -594 -2803 C ATOM 781 CG1 ILE A 98 -42.678 11.551 37.269 1.00 82.34 C ANISOU 781 CG1 ILE A 98 8890 10305 12090 2549 -803 -2424 C ATOM 782 CG2 ILE A 98 -43.900 12.449 39.251 1.00110.35 C ANISOU 782 CG2 ILE A 98 11743 14347 15840 2798 -654 -3309 C ATOM 783 CD1 ILE A 98 -42.444 10.415 36.310 1.00 66.83 C ANISOU 783 CD1 ILE A 98 7166 8332 9894 2326 -765 -2000 C ATOM 784 N GLN A 99 -43.891 10.272 41.551 1.00 87.88 N ANISOU 784 N GLN A 99 8571 12708 12112 2181 47 -3389 N ATOM 785 CA GLN A 99 -43.962 10.718 42.937 1.00 93.21 C ANISOU 785 CA GLN A 99 8950 13788 12679 2132 232 -3837 C ATOM 786 C GLN A 99 -43.114 9.841 43.853 1.00 93.99 C ANISOU 786 C GLN A 99 9161 14237 12314 1779 464 -3606 C ATOM 787 O GLN A 99 -42.448 10.341 44.758 1.00106.65 O ANISOU 787 O GLN A 99 10730 15982 13811 1723 553 -3793 O ATOM 788 CB GLN A 99 -45.414 10.732 43.421 1.00101.78 C ANISOU 788 CB GLN A 99 9595 15289 13788 2132 302 -4255 C ATOM 789 CG GLN A 99 -45.620 11.449 44.747 1.00108.95 C ANISOU 789 CG GLN A 99 10278 16503 14614 2010 410 -4686 C ATOM 790 CD GLN A 99 -47.071 11.457 45.184 1.00123.65 C ANISOU 790 CD GLN A 99 11766 18735 16479 1938 448 -5050 C ATOM 791 OE1 GLN A 99 -47.798 10.485 44.981 1.00125.46 O ANISOU 791 OE1 GLN A 99 11875 19260 16533 1798 539 -4947 O ATOM 792 NE2 GLN A 99 -47.502 12.562 45.782 1.00133.41 N ANISOU 792 NE2 GLN A 99 12803 19961 17927 2022 380 -5499 N ATOM 793 N GLU A 100 -43.144 8.534 43.614 1.00 82.24 N ANISOU 793 N GLU A 100 7804 12876 10567 1540 541 -3196 N ATOM 794 CA GLU A 100 -42.395 7.589 44.435 1.00 85.53 C ANISOU 794 CA GLU A 100 8337 13582 10578 1210 706 -2907 C ATOM 795 C GLU A 100 -40.893 7.742 44.222 1.00 86.01 C ANISOU 795 C GLU A 100 8734 13286 10658 1241 628 -2611 C ATOM 796 O GLU A 100 -40.113 7.670 45.171 1.00 95.16 O ANISOU 796 O GLU A 100 9906 14675 11576 1079 715 -2577 O ATOM 797 CB GLU A 100 -42.830 6.152 44.136 1.00 85.89 C ANISOU 797 CB GLU A 100 8459 13752 10425 965 770 -2536 C ATOM 798 CG GLU A 100 -42.096 5.088 44.944 1.00 80.44 C ANISOU 798 CG GLU A 100 7909 13296 9361 627 884 -2171 C ATOM 799 CD GLU A 100 -42.447 5.116 46.422 1.00 80.50 C ANISOU 799 CD GLU A 100 7636 13942 9009 361 1059 -2421 C ATOM 800 OE1 GLU A 100 -43.462 5.745 46.788 1.00 91.68 O ANISOU 800 OE1 GLU A 100 8703 15678 10452 402 1143 -2912 O ATOM 801 OE2 GLU A 100 -41.706 4.504 47.220 1.00 60.06 O ANISOU 801 OE2 GLU A 100 5159 11552 6108 99 1104 -2136 O ATOM 802 N ILE A 101 -40.492 7.952 42.972 1.00 75.24 N ANISOU 802 N ILE A 101 7626 11400 9560 1423 461 -2404 N ATOM 803 CA ILE A 101 -39.087 8.166 42.647 1.00 68.00 C ANISOU 803 CA ILE A 101 7002 10149 8684 1446 395 -2169 C ATOM 804 C ILE A 101 -38.591 9.483 43.239 1.00 76.36 C ANISOU 804 C ILE A 101 7994 11169 9851 1565 366 -2509 C ATOM 805 O ILE A 101 -37.532 9.531 43.865 1.00 94.18 O ANISOU 805 O ILE A 101 10324 13506 11953 1457 418 -2446 O ATOM 806 CB ILE A 101 -38.851 8.162 41.123 1.00 65.91 C ANISOU 806 CB ILE A 101 7008 9385 8648 1563 237 -1916 C ATOM 807 CG1 ILE A 101 -39.127 6.773 40.544 1.00 70.18 C ANISOU 807 CG1 ILE A 101 7642 9948 9074 1410 287 -1587 C ATOM 808 CG2 ILE A 101 -37.428 8.584 40.797 1.00 53.00 C ANISOU 808 CG2 ILE A 101 5629 7443 7066 1573 183 -1763 C ATOM 809 CD1 ILE A 101 -38.923 6.683 39.048 1.00 54.58 C ANISOU 809 CD1 ILE A 101 5912 7561 7264 1468 160 -1371 C ATOM 810 N ARG A 102 -39.370 10.544 43.047 1.00 68.34 N ANISOU 810 N ARG A 102 6822 10021 9123 1789 267 -2882 N ATOM 811 CA ARG A 102 -39.017 11.870 43.550 1.00 66.24 C ANISOU 811 CA ARG A 102 6484 9647 9038 1922 224 -3263 C ATOM 812 C ARG A 102 -38.908 11.881 45.071 1.00 82.49 C ANISOU 812 C ARG A 102 8292 12249 10803 1744 429 -3567 C ATOM 813 O ARG A 102 -38.068 12.580 45.637 1.00 95.38 O ANISOU 813 O ARG A 102 9952 13869 12420 1719 447 -3731 O ATOM 814 CB ARG A 102 -40.049 12.904 43.096 1.00 63.46 C ANISOU 814 CB ARG A 102 5968 9040 9105 2221 54 -3626 C ATOM 815 CG ARG A 102 -39.658 14.344 43.373 1.00 72.57 C ANISOU 815 CG ARG A 102 7107 9908 10559 2392 -46 -3995 C ATOM 816 CD ARG A 102 -40.811 15.289 43.082 1.00 79.21 C ANISOU 816 CD ARG A 102 7793 10515 11788 2590 -250 -4240 C ATOM 817 NE ARG A 102 -40.386 16.685 43.092 1.00 99.36 N ANISOU 817 NE ARG A 102 10452 12646 14655 2683 -416 -4398 N ATOM 818 CZ ARG A 102 -40.065 17.373 42.002 1.00110.44 C ANISOU 818 CZ ARG A 102 12145 13451 16366 2818 -685 -4164 C ATOM 819 NH1 ARG A 102 -40.125 16.796 40.810 1.00100.52 N ANISOU 819 NH1 ARG A 102 11096 11968 15130 2874 -823 -3776 N ATOM 820 NH2 ARG A 102 -39.687 18.639 42.102 1.00127.12 N ANISOU 820 NH2 ARG A 102 14343 15203 18753 2868 -822 -4314 N ATOM 821 N ARG A 103 -39.750 11.104 45.722 1.00 77.83 N ANISOU 821 N ARG A 103 7458 12160 9952 1581 584 -3639 N ATOM 822 CA ARG A 103 -39.747 11.026 47.159 1.00 71.89 C ANISOU 822 CA ARG A 103 6461 12009 8846 1341 784 -3906 C ATOM 823 C ARG A 103 -38.458 10.449 47.702 1.00 85.76 C ANISOU 823 C ARG A 103 8420 13903 10263 1094 825 -3537 C ATOM 824 O ARG A 103 -37.903 10.992 48.620 1.00 99.80 O ANISOU 824 O ARG A 103 10108 15923 11890 994 891 -3776 O ATOM 825 CB ARG A 103 -40.928 10.181 47.620 1.00 72.04 C ANISOU 825 CB ARG A 103 6211 12545 8615 1149 936 -3978 C ATOM 826 CG ARG A 103 -41.336 10.336 49.077 1.00 91.14 C ANISOU 826 CG ARG A 103 8281 15650 10696 892 1147 -4410 C ATOM 827 CD ARG A 103 -41.424 11.794 49.517 1.00113.51 C ANISOU 827 CD ARG A 103 10993 18316 13818 1020 1054 -4894 C ATOM 828 NE ARG A 103 -41.274 11.963 50.967 1.00117.21 N ANISOU 828 NE ARG A 103 11274 19333 13927 686 1189 -5143 N ATOM 829 CZ ARG A 103 -40.274 12.612 51.559 1.00104.77 C ANISOU 829 CZ ARG A 103 9757 17761 12291 630 1186 -5253 C ATOM 830 NH1 ARG A 103 -39.310 13.167 50.846 1.00 87.54 N ANISOU 830 NH1 ARG A 103 7823 15054 10382 878 1066 -5144 N ATOM 831 NH2 ARG A 103 -40.241 12.703 52.876 1.00115.31 N ANISOU 831 NH2 ARG A 103 10892 19643 13276 294 1299 -5477 N ATOM 832 N GLN A 104 -37.962 9.374 47.111 1.00 80.49 N ANISOU 832 N GLN A 104 8012 13064 9505 1009 772 -2979 N ATOM 833 CA GLN A 104 -36.730 8.728 47.544 1.00 77.95 C ANISOU 833 CA GLN A 104 7867 12827 8922 816 768 -2595 C ATOM 834 C GLN A 104 -35.493 9.459 47.029 1.00 87.43 C ANISOU 834 C GLN A 104 9280 13602 10339 967 654 -2546 C ATOM 835 O GLN A 104 -34.437 9.418 47.660 1.00 89.74 O ANISOU 835 O GLN A 104 9614 14040 10443 838 654 -2440 O ATOM 836 CB GLN A 104 -36.707 7.270 47.082 1.00 70.97 C ANISOU 836 CB GLN A 104 7155 11878 7933 692 745 -2060 C ATOM 837 CG GLN A 104 -37.985 6.506 47.387 1.00 69.80 C ANISOU 837 CG GLN A 104 6833 12084 7604 518 849 -2072 C ATOM 838 CD GLN A 104 -38.329 6.487 48.862 1.00 90.68 C ANISOU 838 CD GLN A 104 9219 15399 9836 221 992 -2284 C ATOM 839 OE1 GLN A 104 -37.848 5.639 49.612 1.00110.11 O ANISOU 839 OE1 GLN A 104 11740 18144 11954 -66 999 -1944 O ATOM 840 NE2 GLN A 104 -39.164 7.428 49.288 1.00101.25 N ANISOU 840 NE2 GLN A 104 10258 17002 11210 278 1095 -2857 N ATOM 841 N LEU A 105 -35.622 10.116 45.880 1.00 91.28 N ANISOU 841 N LEU A 105 9897 13582 11201 1211 544 -2605 N ATOM 842 CA LEU A 105 -34.519 10.897 45.326 1.00 86.11 C ANISOU 842 CA LEU A 105 9449 12521 10747 1310 441 -2576 C ATOM 843 C LEU A 105 -34.161 12.051 46.254 1.00 87.44 C ANISOU 843 C LEU A 105 9478 12835 10909 1299 474 -3007 C ATOM 844 O LEU A 105 -32.986 12.362 46.449 1.00 91.74 O ANISOU 844 O LEU A 105 10127 13327 11404 1226 455 -2955 O ATOM 845 CB LEU A 105 -34.866 11.432 43.935 1.00 82.11 C ANISOU 845 CB LEU A 105 9113 11474 10610 1523 295 -2547 C ATOM 846 CG LEU A 105 -34.675 10.493 42.742 1.00 71.83 C ANISOU 846 CG LEU A 105 8043 9910 9339 1508 242 -2105 C ATOM 847 CD1 LEU A 105 -34.949 11.234 41.444 1.00 75.31 C ANISOU 847 CD1 LEU A 105 8653 9865 10094 1669 75 -2100 C ATOM 848 CD2 LEU A 105 -33.278 9.893 42.734 1.00 63.48 C ANISOU 848 CD2 LEU A 105 7142 8837 8140 1372 274 -1803 C ATOM 849 N GLU A 106 -35.183 12.684 46.819 1.00 87.10 N ANISOU 849 N GLU A 106 9176 12987 10930 1366 530 -3472 N ATOM 850 CA GLU A 106 -34.977 13.745 47.795 1.00 83.43 C ANISOU 850 CA GLU A 106 8530 12710 10458 1338 592 -3973 C ATOM 851 C GLU A 106 -34.393 13.169 49.079 1.00 95.91 C ANISOU 851 C GLU A 106 9989 14902 11548 1027 730 -3929 C ATOM 852 O GLU A 106 -33.531 13.780 49.710 1.00111.25 O ANISOU 852 O GLU A 106 11917 16952 13401 929 747 -4110 O ATOM 853 CB GLU A 106 -36.290 14.476 48.082 1.00 80.31 C ANISOU 853 CB GLU A 106 7834 12400 10280 1496 631 -4537 C ATOM 854 CG GLU A 106 -36.831 15.261 46.897 1.00 83.70 C ANISOU 854 CG GLU A 106 8366 12193 11244 1828 429 -4614 C ATOM 855 CD GLU A 106 -38.230 15.796 47.139 1.00 90.70 C ANISOU 855 CD GLU A 106 8985 13129 12349 1908 382 -4936 C ATOM 856 OE1 GLU A 106 -38.864 15.378 48.131 1.00 90.87 O ANISOU 856 OE1 GLU A 106 8722 13716 12087 1719 547 -5138 O ATOM 857 OE2 GLU A 106 -38.695 16.634 46.338 1.00 81.83 O ANISOU 857 OE2 GLU A 106 7930 11493 11668 2139 166 -4979 O ATOM 858 N ALA A 107 -34.863 11.983 49.455 1.00 87.63 N ANISOU 858 N ALA A 107 8865 14255 10176 847 808 -3666 N ATOM 859 CA ALA A 107 -34.361 11.297 50.639 1.00 79.93 C ANISOU 859 CA ALA A 107 7803 13864 8703 517 890 -3514 C ATOM 860 C ALA A 107 -32.922 10.841 50.429 1.00 82.62 C ANISOU 860 C ALA A 107 8386 14028 8978 466 771 -3045 C ATOM 861 O ALA A 107 -32.127 10.805 51.368 1.00 99.27 O ANISOU 861 O ALA A 107 10436 16504 10779 256 775 -3018 O ATOM 862 CB ALA A 107 -35.250 10.113 50.986 1.00 75.60 C ANISOU 862 CB ALA A 107 7156 13715 7855 316 970 -3286 C ATOM 863 N CYS A 108 -32.593 10.493 49.188 1.00 81.92 N ANISOU 863 N CYS A 108 8545 13406 9174 648 662 -2699 N ATOM 864 CA CYS A 108 -31.241 10.072 48.843 1.00 83.15 C ANISOU 864 CA CYS A 108 8896 13362 9335 632 559 -2311 C ATOM 865 C CYS A 108 -30.267 11.239 48.948 1.00 83.07 C ANISOU 865 C CYS A 108 8907 13224 9432 661 530 -2580 C ATOM 866 O CYS A 108 -29.108 11.063 49.320 1.00 91.67 O ANISOU 866 O CYS A 108 10019 14436 10377 551 481 -2413 O ATOM 867 CB CYS A 108 -31.204 9.482 47.432 1.00 79.89 C ANISOU 867 CB CYS A 108 8711 12439 9203 796 485 -1970 C ATOM 868 SG CYS A 108 -29.577 8.894 46.910 1.00 97.30 S ANISOU 868 SG CYS A 108 11100 14408 11463 791 386 -1564 S ATOM 869 N GLN A 109 -30.750 12.432 48.616 1.00 78.26 N ANISOU 869 N GLN A 109 8282 12354 9100 808 544 -2998 N ATOM 870 CA GLN A 109 -29.934 13.637 48.682 1.00 79.51 C ANISOU 870 CA GLN A 109 8477 12330 9402 818 515 -3291 C ATOM 871 C GLN A 109 -29.538 13.945 50.122 1.00 93.77 C ANISOU 871 C GLN A 109 10064 14691 10873 596 596 -3578 C ATOM 872 O GLN A 109 -28.425 14.397 50.389 1.00103.86 O ANISOU 872 O GLN A 109 11372 15991 12100 496 566 -3624 O ATOM 873 CB GLN A 109 -30.685 14.822 48.070 1.00 84.06 C ANISOU 873 CB GLN A 109 9082 12468 10388 1029 477 -3671 C ATOM 874 CG GLN A 109 -29.857 16.088 47.935 1.00 99.35 C ANISOU 874 CG GLN A 109 11123 14080 12547 1034 419 -3927 C ATOM 875 CD GLN A 109 -30.631 17.222 47.290 1.00103.56 C ANISOU 875 CD GLN A 109 11711 14099 13539 1257 324 -4243 C ATOM 876 OE1 GLN A 109 -31.854 17.162 47.164 1.00 96.15 O ANISOU 876 OE1 GLN A 109 10652 13142 12739 1422 317 -4380 O ATOM 877 NE2 GLN A 109 -29.920 18.263 46.874 1.00112.35 N ANISOU 877 NE2 GLN A 109 13002 14781 14906 1256 230 -4352 N ATOM 878 N ARG A 110 -30.460 13.695 51.047 1.00 94.27 N ANISOU 878 N ARG A 110 9893 15245 10681 485 706 -3787 N ATOM 879 CA ARG A 110 -30.214 13.935 52.464 1.00 93.57 C ANISOU 879 CA ARG A 110 9573 15780 10199 216 799 -4082 C ATOM 880 C ARG A 110 -29.356 12.845 53.102 1.00 97.65 C ANISOU 880 C ARG A 110 10102 16719 10281 -31 736 -3594 C ATOM 881 O ARG A 110 -28.396 13.137 53.815 1.00102.52 O ANISOU 881 O ARG A 110 10660 17614 10680 -206 707 -3657 O ATOM 882 CB ARG A 110 -31.542 14.051 53.217 1.00 87.32 C ANISOU 882 CB ARG A 110 8500 15421 9256 140 959 -4512 C ATOM 883 CG ARG A 110 -32.327 15.316 52.911 1.00 85.35 C ANISOU 883 CG ARG A 110 8143 14841 9445 378 1007 -5135 C ATOM 884 CD ARG A 110 -33.790 15.003 52.642 1.00 91.93 C ANISOU 884 CD ARG A 110 8850 15654 10425 486 1036 -5177 C ATOM 885 NE ARG A 110 -34.378 14.165 53.683 1.00101.41 N ANISOU 885 NE ARG A 110 9831 17555 11144 166 1159 -5126 N ATOM 886 CZ ARG A 110 -35.603 13.653 53.623 1.00103.37 C ANISOU 886 CZ ARG A 110 9945 17943 11387 158 1210 -5125 C ATOM 887 NH1 ARG A 110 -36.372 13.892 52.570 1.00 99.11 N ANISOU 887 NH1 ARG A 110 9452 16906 11299 479 1138 -5174 N ATOM 888 NH2 ARG A 110 -36.059 12.900 54.615 1.00109.10 N ANISOU 888 NH2 ARG A 110 10492 19315 11645 -199 1314 -5057 N ATOM 889 N GLU A 111 -29.707 11.589 52.844 1.00 98.84 N ANISOU 889 N GLU A 111 10327 16901 10326 -47 692 -3105 N ATOM 890 CA GLU A 111 -29.061 10.461 53.509 1.00 97.60 C ANISOU 890 CA GLU A 111 10174 17124 9785 -276 592 -2610 C ATOM 891 C GLU A 111 -27.710 10.082 52.904 1.00 95.89 C ANISOU 891 C GLU A 111 10131 16569 9733 -170 421 -2201 C ATOM 892 O GLU A 111 -26.755 9.810 53.632 1.00100.51 O ANISOU 892 O GLU A 111 10657 17472 10059 -337 312 -2012 O ATOM 893 CB GLU A 111 -29.989 9.244 53.490 1.00 88.39 C ANISOU 893 CB GLU A 111 9026 16084 8475 -355 601 -2250 C ATOM 894 CG GLU A 111 -31.303 9.458 54.224 1.00 87.65 C ANISOU 894 CG GLU A 111 8707 16459 8136 -532 783 -2639 C ATOM 895 CD GLU A 111 -32.168 8.215 54.246 1.00 92.05 C ANISOU 895 CD GLU A 111 9287 17176 8512 -676 794 -2258 C ATOM 896 OE1 GLU A 111 -31.728 7.173 53.716 1.00 94.13 O ANISOU 896 OE1 GLU A 111 9755 17151 8861 -628 645 -1686 O ATOM 897 OE2 GLU A 111 -33.290 8.279 54.791 1.00 99.10 O ANISOU 897 OE2 GLU A 111 9979 18484 9192 -850 957 -2560 O ATOM 898 N GLN A 112 -27.629 10.064 51.578 1.00106.05 N ANISOU 898 N GLN A 112 14482 12949 12861 3473 -1513 -1823 N ATOM 899 CA GLN A 112 -26.414 9.618 50.902 1.00 93.76 C ANISOU 899 CA GLN A 112 12400 11545 11681 3585 -1559 -1781 C ATOM 900 C GLN A 112 -25.451 10.767 50.618 1.00 97.90 C ANISOU 900 C GLN A 112 12372 12274 12553 3330 -1872 -1935 C ATOM 901 O GLN A 112 -25.865 11.861 50.233 1.00 90.34 O ANISOU 901 O GLN A 112 11379 11297 11648 2962 -1802 -2065 O ATOM 902 CB GLN A 112 -26.763 8.899 49.596 1.00 79.72 C ANISOU 902 CB GLN A 112 10566 9651 10073 3494 -992 -1709 C ATOM 903 CG GLN A 112 -27.540 7.606 49.785 1.00 85.86 C ANISOU 903 CG GLN A 112 11838 10218 10568 3722 -638 -1574 C ATOM 904 CD GLN A 112 -26.710 6.510 50.425 1.00 96.49 C ANISOU 904 CD GLN A 112 13229 11549 11884 4221 -743 -1423 C ATOM 905 OE1 GLN A 112 -25.480 6.540 50.382 1.00102.61 O ANISOU 905 OE1 GLN A 112 13537 12489 12960 4392 -999 -1389 O ATOM 906 NE2 GLN A 112 -27.382 5.533 51.024 1.00101.29 N ANISOU 906 NE2 GLN A 112 14385 11947 12153 4470 -525 -1314 N ATOM 907 N LYS A 113 -24.163 10.505 50.813 1.00106.32 N ANISOU 907 N LYS A 113 12991 13523 13881 3536 -2196 -1907 N ATOM 908 CA LYS A 113 -23.123 11.486 50.532 1.00106.98 C ANISOU 908 CA LYS A 113 12468 13806 14374 3285 -2473 -2062 C ATOM 909 C LYS A 113 -22.573 11.293 49.124 1.00105.35 C ANISOU 909 C LYS A 113 11782 13578 14667 3181 -2031 -2039 C ATOM 910 O LYS A 113 -22.294 10.169 48.706 1.00100.59 O ANISOU 910 O LYS A 113 11113 12911 14197 3473 -1747 -1871 O ATOM 911 CB LYS A 113 -21.994 11.383 51.559 1.00115.65 C ANISOU 911 CB LYS A 113 13265 15150 15529 3532 -3130 -2046 C ATOM 912 CG LYS A 113 -22.442 11.578 52.998 1.00116.88 C ANISOU 912 CG LYS A 113 13980 15309 15119 3622 -3599 -2078 C ATOM 913 CD LYS A 113 -21.276 11.437 53.961 1.00125.69 C ANISOU 913 CD LYS A 113 14789 16708 16260 3858 -4330 -2042 C ATOM 914 CE LYS A 113 -21.723 11.617 55.402 1.00129.81 C ANISOU 914 CE LYS A 113 15990 17203 16127 3929 -4796 -2077 C ATOM 915 NZ LYS A 113 -20.589 11.476 56.356 1.00134.54 N ANISOU 915 NZ LYS A 113 16318 18115 16688 4146 -5606 -2026 N ATOM 916 N PHE A 114 -22.415 12.393 48.395 1.00105.21 N ANISOU 916 N PHE A 114 11492 13571 14911 2766 -1919 -2206 N ATOM 917 CA PHE A 114 -21.940 12.330 47.018 1.00 99.71 C ANISOU 917 CA PHE A 114 10435 12804 14646 2620 -1443 -2200 C ATOM 918 C PHE A 114 -20.692 13.177 46.802 1.00106.01 C ANISOU 918 C PHE A 114 10562 13748 15970 2411 -1619 -2353 C ATOM 919 O PHE A 114 -20.453 14.148 47.521 1.00105.49 O ANISOU 919 O PHE A 114 10383 13814 15886 2210 -2059 -2522 O ATOM 920 CB PHE A 114 -23.041 12.774 46.054 1.00 91.31 C ANISOU 920 CB PHE A 114 9740 11551 13401 2296 -989 -2225 C ATOM 921 CG PHE A 114 -24.221 11.848 46.016 1.00 86.90 C ANISOU 921 CG PHE A 114 9734 10850 12434 2440 -734 -2080 C ATOM 922 CD1 PHE A 114 -24.257 10.791 45.123 1.00 82.85 C ANISOU 922 CD1 PHE A 114 9304 10205 11971 2528 -275 -1965 C ATOM 923 CD2 PHE A 114 -25.293 12.033 46.873 1.00 83.94 C ANISOU 923 CD2 PHE A 114 9811 10442 11638 2457 -907 -2072 C ATOM 924 CE1 PHE A 114 -25.340 9.936 45.084 1.00 79.76 C ANISOU 924 CE1 PHE A 114 9412 9679 11213 2595 -36 -1863 C ATOM 925 CE2 PHE A 114 -26.378 11.181 46.840 1.00 83.96 C ANISOU 925 CE2 PHE A 114 10269 10308 11323 2554 -646 -1953 C ATOM 926 CZ PHE A 114 -26.401 10.131 45.944 1.00 82.08 C ANISOU 926 CZ PHE A 114 10085 9967 11135 2605 -231 -1857 C ATOM 927 N LYS A 115 -19.901 12.801 45.803 1.00116.16 N ANISOU 927 N LYS A 115 11428 14978 17731 2431 -1227 -2307 N ATOM 928 CA LYS A 115 -18.702 13.548 45.448 1.00 97.74 C ANISOU 928 CA LYS A 115 8408 12740 15988 2211 -1267 -2450 C ATOM 929 C LYS A 115 -19.082 14.826 44.710 1.00 95.01 C ANISOU 929 C LYS A 115 8188 12262 15649 1705 -1001 -2640 C ATOM 930 O LYS A 115 -18.542 15.898 44.983 1.00 97.62 O ANISOU 930 O LYS A 115 8201 12688 16203 1409 -1251 -2842 O ATOM 931 CB LYS A 115 -17.769 12.689 44.593 1.00111.37 C ANISOU 931 CB LYS A 115 9686 14384 18247 2424 -816 -2319 C ATOM 932 CG LYS A 115 -16.386 13.284 44.386 1.00118.83 C ANISOU 932 CG LYS A 115 9791 15448 19910 2274 -878 -2438 C ATOM 933 CD LYS A 115 -15.396 12.248 43.864 1.00111.21 C ANISOU 933 CD LYS A 115 8326 14420 19509 2630 -502 -2248 C ATOM 934 CE LYS A 115 -14.940 11.286 44.959 1.00131.41 C ANISOU 934 CE LYS A 115 10632 17208 22091 3180 -1019 -2030 C ATOM 935 NZ LYS A 115 -15.923 10.206 45.261 1.00111.70 N ANISOU 935 NZ LYS A 115 8868 14582 18989 3537 -921 -1831 N ATOM 936 N VAL A 116 -20.018 14.703 43.775 1.00108.71 N ANISOU 936 N VAL A 116 10408 13772 17125 1600 -499 -2569 N ATOM 937 CA VAL A 116 -20.564 15.863 43.082 1.00108.47 C ANISOU 937 CA VAL A 116 10607 13600 17007 1188 -253 -2682 C ATOM 938 C VAL A 116 -21.686 16.480 43.907 1.00 84.44 C ANISOU 938 C VAL A 116 8034 10580 13468 1119 -566 -2709 C ATOM 939 O VAL A 116 -22.014 15.991 44.988 1.00 84.39 O ANISOU 939 O VAL A 116 8201 10682 13179 1365 -945 -2659 O ATOM 940 CB VAL A 116 -21.102 15.496 41.686 1.00 84.60 C ANISOU 940 CB VAL A 116 7915 10342 13885 1096 370 -2568 C ATOM 941 CG1 VAL A 116 -19.972 15.026 40.788 1.00 99.31 C ANISOU 941 CG1 VAL A 116 9379 12098 16254 1119 806 -2561 C ATOM 942 CG2 VAL A 116 -22.183 14.431 41.797 1.00 81.11 C ANISOU 942 CG2 VAL A 116 7980 9869 12970 1324 409 -2391 C ATOM 943 N THR A 117 -22.278 17.552 43.393 1.00 84.28 N ANISOU 943 N THR A 117 8252 10424 13347 806 -362 -2768 N ATOM 944 CA THR A 117 -23.386 18.198 44.082 1.00 93.61 C ANISOU 944 CA THR A 117 9879 11572 14115 752 -548 -2766 C ATOM 945 C THR A 117 -24.714 17.646 43.582 1.00 95.01 C ANISOU 945 C THR A 117 10525 11651 13923 852 -297 -2555 C ATOM 946 O THR A 117 -25.094 17.865 42.432 1.00 73.58 O ANISOU 946 O THR A 117 7934 8818 11207 693 70 -2475 O ATOM 947 CB THR A 117 -23.363 19.726 43.889 1.00106.11 C ANISOU 947 CB THR A 117 11481 13038 15797 391 -452 -2919 C ATOM 948 OG1 THR A 117 -23.449 20.035 42.492 1.00125.91 O ANISOU 948 OG1 THR A 117 14027 15380 18433 215 43 -2851 O ATOM 949 CG2 THR A 117 -22.082 20.317 44.457 1.00 98.51 C ANISOU 949 CG2 THR A 117 10048 12182 15198 212 -732 -3170 C ATOM 950 N PHE A 118 -25.415 16.927 44.453 1.00 95.08 N ANISOU 950 N PHE A 118 10804 11709 13612 1101 -505 -2465 N ATOM 951 CA PHE A 118 -26.701 16.343 44.096 1.00 98.15 C ANISOU 951 CA PHE A 118 11586 12023 13683 1171 -298 -2282 C ATOM 952 C PHE A 118 -27.792 17.401 44.185 1.00105.78 C ANISOU 952 C PHE A 118 12828 12896 14465 1020 -261 -2239 C ATOM 953 O PHE A 118 -28.011 17.996 45.240 1.00115.31 O ANISOU 953 O PHE A 118 14168 14082 15562 1048 -477 -2310 O ATOM 954 CB PHE A 118 -27.029 15.156 45.002 1.00100.49 C ANISOU 954 CB PHE A 118 12075 12363 13743 1489 -459 -2206 C ATOM 955 CG PHE A 118 -28.078 14.239 44.442 1.00101.20 C ANISOU 955 CG PHE A 118 12467 12382 13602 1529 -182 -2044 C ATOM 956 CD1 PHE A 118 -27.727 13.197 43.599 1.00103.29 C ANISOU 956 CD1 PHE A 118 12689 12620 13936 1567 84 -1988 C ATOM 957 CD2 PHE A 118 -29.415 14.416 44.757 1.00101.40 C ANISOU 957 CD2 PHE A 118 12815 12351 13362 1506 -159 -1953 C ATOM 958 CE1 PHE A 118 -28.688 12.351 43.081 1.00100.85 C ANISOU 958 CE1 PHE A 118 12688 12242 13389 1532 329 -1875 C ATOM 959 CE2 PHE A 118 -30.380 13.572 44.242 1.00 98.03 C ANISOU 959 CE2 PHE A 118 12608 11883 12755 1488 65 -1823 C ATOM 960 CZ PHE A 118 -30.016 12.539 43.403 1.00 97.72 C ANISOU 960 CZ PHE A 118 12557 11831 12741 1476 290 -1798 C ATOM 961 N GLU A 119 -28.477 17.630 43.070 1.00106.38 N ANISOU 961 N GLU A 119 13018 12904 14500 869 24 -2107 N ATOM 962 CA GLU A 119 -29.464 18.696 42.992 1.00105.19 C ANISOU 962 CA GLU A 119 13065 12659 14244 760 97 -2012 C ATOM 963 C GLU A 119 -30.811 18.178 42.515 1.00100.35 C ANISOU 963 C GLU A 119 12671 12052 13406 797 212 -1781 C ATOM 964 O GLU A 119 -30.947 17.763 41.368 1.00100.28 O ANISOU 964 O GLU A 119 12673 12067 13361 684 374 -1682 O ATOM 965 CB GLU A 119 -28.968 19.800 42.054 1.00118.58 C ANISOU 965 CB GLU A 119 14654 14263 16139 518 298 -2048 C ATOM 966 CG GLU A 119 -29.928 20.960 41.869 1.00129.18 C ANISOU 966 CG GLU A 119 16206 15477 17400 445 422 -1906 C ATOM 967 CD GLU A 119 -29.761 22.026 42.930 1.00144.09 C ANISOU 967 CD GLU A 119 18151 17252 19344 416 337 -2054 C ATOM 968 OE1 GLU A 119 -29.422 21.675 44.079 1.00149.96 O ANISOU 968 OE1 GLU A 119 18885 18051 20042 510 85 -2207 O ATOM 969 OE2 GLU A 119 -29.957 23.216 42.613 1.00148.21 O ANISOU 969 OE2 GLU A 119 18778 17609 19928 294 534 -2015 O ATOM 970 N VAL A 120 -31.807 18.214 43.394 1.00 99.97 N ANISOU 970 N VAL A 120 12805 11972 13207 929 137 -1700 N ATOM 971 CA VAL A 120 -33.159 17.818 43.022 1.00 88.12 C ANISOU 971 CA VAL A 120 11432 10491 11560 941 231 -1478 C ATOM 972 C VAL A 120 -33.970 19.049 42.642 1.00 85.90 C ANISOU 972 C VAL A 120 11175 10135 11328 871 328 -1301 C ATOM 973 O VAL A 120 -34.237 19.912 43.478 1.00 92.61 O ANISOU 973 O VAL A 120 12113 10856 12220 952 345 -1309 O ATOM 974 CB VAL A 120 -33.870 17.063 44.157 1.00 77.96 C ANISOU 974 CB VAL A 120 10314 9178 10129 1139 178 -1462 C ATOM 975 CG1 VAL A 120 -35.310 16.766 43.772 1.00 62.40 C ANISOU 975 CG1 VAL A 120 8392 7229 8086 1108 289 -1237 C ATOM 976 CG2 VAL A 120 -33.128 15.778 44.483 1.00 79.71 C ANISOU 976 CG2 VAL A 120 10554 9453 10280 1256 110 -1585 C ATOM 977 N GLN A 121 -34.356 19.124 41.373 1.00 85.79 N ANISOU 977 N GLN A 121 11125 10183 11287 729 406 -1128 N ATOM 978 CA GLN A 121 -35.048 20.295 40.853 1.00 93.13 C ANISOU 978 CA GLN A 121 12067 11050 12267 699 490 -907 C ATOM 979 C GLN A 121 -36.437 20.465 41.458 1.00112.03 C ANISOU 979 C GLN A 121 14475 13422 14669 857 496 -688 C ATOM 980 O GLN A 121 -37.087 19.492 41.840 1.00112.29 O ANISOU 980 O GLN A 121 14499 13536 14631 911 441 -659 O ATOM 981 CB GLN A 121 -35.154 20.211 39.329 1.00 77.10 C ANISOU 981 CB GLN A 121 10045 9111 10138 518 519 -749 C ATOM 982 CG GLN A 121 -33.813 20.173 38.613 1.00 69.54 C ANISOU 982 CG GLN A 121 9100 8109 9215 357 629 -940 C ATOM 983 CD GLN A 121 -33.031 21.463 38.765 1.00 81.11 C ANISOU 983 CD GLN A 121 10548 9395 10874 333 767 -1046 C ATOM 984 OE1 GLN A 121 -32.297 21.647 39.736 1.00 87.79 O ANISOU 984 OE1 GLN A 121 11307 10181 11868 377 736 -1278 O ATOM 985 NE2 GLN A 121 -33.185 22.364 37.802 1.00 84.82 N ANISOU 985 NE2 GLN A 121 11128 9776 11325 245 915 -875 N ATOM 986 N SER A 122 -36.878 21.716 41.541 1.00120.87 N ANISOU 986 N SER A 122 15621 14398 15907 935 621 -530 N ATOM 987 CA SER A 122 -38.237 22.040 41.952 1.00117.99 C ANISOU 987 CA SER A 122 15219 13981 15630 1109 701 -258 C ATOM 988 C SER A 122 -39.203 21.548 40.877 1.00113.22 C ANISOU 988 C SER A 122 14433 13604 14981 1044 570 39 C ATOM 989 O SER A 122 -38.764 21.200 39.779 1.00107.68 O ANISOU 989 O SER A 122 13732 13046 14135 852 452 31 O ATOM 990 CB SER A 122 -38.381 23.549 42.176 1.00118.66 C ANISOU 990 CB SER A 122 15401 13817 15869 1221 929 -138 C ATOM 991 OG SER A 122 -37.487 24.003 43.177 1.00119.73 O ANISOU 991 OG SER A 122 15738 13747 16006 1207 1020 -448 O ATOM 992 N PRO A 123 -40.513 21.488 41.188 1.00118.78 N ANISOU 992 N PRO A 123 14985 14337 15810 1179 593 295 N ATOM 993 CA PRO A 123 -41.461 21.080 40.146 1.00124.94 C ANISOU 993 CA PRO A 123 15537 15375 16561 1076 394 588 C ATOM 994 C PRO A 123 -41.309 21.919 38.880 1.00139.99 C ANISOU 994 C PRO A 123 17454 17340 18395 1014 307 809 C ATOM 995 O PRO A 123 -41.331 23.149 38.934 1.00141.42 O ANISOU 995 O PRO A 123 17678 17337 18716 1191 477 970 O ATOM 996 CB PRO A 123 -42.821 21.315 40.805 1.00116.98 C ANISOU 996 CB PRO A 123 14301 14322 15826 1290 505 862 C ATOM 997 CG PRO A 123 -42.559 21.091 42.253 1.00112.43 C ANISOU 997 CG PRO A 123 13916 13503 15297 1420 742 599 C ATOM 998 CD PRO A 123 -41.165 21.608 42.506 1.00116.24 C ANISOU 998 CD PRO A 123 14694 13824 15650 1394 796 303 C ATOM 999 N ARG A 124 -41.161 21.238 37.749 1.00146.34 N ANISOU 999 N ARG A 124 18285 18365 18951 758 80 816 N ATOM 1000 CA ARG A 124 -40.768 21.881 36.502 1.00150.45 C ANISOU 1000 CA ARG A 124 18953 18907 19303 656 20 958 C ATOM 1001 C ARG A 124 -41.940 22.552 35.804 1.00148.44 C ANISOU 1001 C ARG A 124 18519 18789 19093 768 -159 1445 C ATOM 1002 O ARG A 124 -43.037 21.997 35.747 1.00149.75 O ANISOU 1002 O ARG A 124 18407 19188 19305 740 -394 1646 O ATOM 1003 CB ARG A 124 -40.124 20.854 35.566 1.00156.98 C ANISOU 1003 CB ARG A 124 19972 19870 19802 323 -106 763 C ATOM 1004 CG ARG A 124 -39.662 21.416 34.234 1.00156.59 C ANISOU 1004 CG ARG A 124 20176 19803 19518 185 -120 885 C ATOM 1005 CD ARG A 124 -38.564 22.446 34.423 1.00156.48 C ANISOU 1005 CD ARG A 124 20324 19493 19638 290 203 740 C ATOM 1006 NE ARG A 124 -37.432 21.895 35.162 1.00153.99 N ANISOU 1006 NE ARG A 124 20030 19060 19419 235 379 314 N ATOM 1007 CZ ARG A 124 -36.443 21.204 34.606 1.00155.35 C ANISOU 1007 CZ ARG A 124 20365 19211 19451 21 468 71 C ATOM 1008 NH1 ARG A 124 -36.444 20.974 33.300 1.00151.77 N ANISOU 1008 NH1 ARG A 124 20150 18811 18704 -195 433 180 N ATOM 1009 NH2 ARG A 124 -35.453 20.740 35.356 1.00159.48 N ANISOU 1009 NH2 ARG A 124 20827 19647 20122 31 599 -266 N ATOM 1010 N ARG A 125 -41.687 23.733 35.248 1.00150.59 N ANISOU 1010 N ARG A 125 18942 18916 19359 888 -48 1642 N ATOM 1011 CA ARG A 125 -42.721 24.543 34.614 1.00154.50 C ANISOU 1011 CA ARG A 125 19286 19503 19915 1083 -196 2163 C ATOM 1012 C ARG A 125 -42.521 24.602 33.104 1.00167.74 C ANISOU 1012 C ARG A 125 21214 21317 21201 886 -433 2333 C ATOM 1013 O ARG A 125 -41.409 24.411 32.611 1.00164.33 O ANISOU 1013 O ARG A 125 21141 20776 20522 660 -309 2044 O ATOM 1014 CB ARG A 125 -42.727 25.957 35.199 1.00146.02 C ANISOU 1014 CB ARG A 125 18256 18092 19135 1439 180 2328 C ATOM 1015 CG ARG A 125 -43.465 26.078 36.522 1.00141.05 C ANISOU 1015 CG ARG A 125 17359 17342 18890 1700 380 2368 C ATOM 1016 CD ARG A 125 -43.485 27.516 37.014 1.00140.81 C ANISOU 1016 CD ARG A 125 17460 16928 19114 2030 812 2541 C ATOM 1017 NE ARG A 125 -42.283 28.245 36.620 1.00140.43 N ANISOU 1017 NE ARG A 125 17824 16635 18898 1924 1035 2340 N ATOM 1018 CZ ARG A 125 -42.218 29.567 36.499 1.00140.50 C ANISOU 1018 CZ ARG A 125 18041 16328 19015 2140 1377 2551 C ATOM 1019 NH1 ARG A 125 -43.288 30.311 36.742 1.00141.63 N ANISOU 1019 NH1 ARG A 125 18017 16357 19439 2519 1539 2999 N ATOM 1020 NH2 ARG A 125 -41.082 30.146 36.135 1.00140.45 N ANISOU 1020 NH2 ARG A 125 18404 16092 18868 1983 1605 2320 N ATOM 1021 N GLU A 126 -43.612 24.846 32.380 1.00189.60 N ANISOU 1021 N GLU A 126 23794 24325 23920 975 -776 2813 N ATOM 1022 CA GLU A 126 -43.614 24.827 30.919 1.00209.63 C ANISOU 1022 CA GLU A 126 26606 27036 26008 775 -1096 3027 C ATOM 1023 C GLU A 126 -43.709 23.390 30.422 1.00227.20 C ANISOU 1023 C GLU A 126 28862 29567 27898 325 -1450 2812 C ATOM 1024 O GLU A 126 -43.540 23.113 29.234 1.00232.94 O ANISOU 1024 O GLU A 126 29937 30414 28156 45 -1688 2863 O ATOM 1025 CB GLU A 126 -42.375 25.521 30.345 1.00208.58 C ANISOU 1025 CB GLU A 126 27018 26578 25655 733 -749 2878 C ATOM 1026 CG GLU A 126 -42.283 25.473 28.829 1.00207.19 C ANISOU 1026 CG GLU A 126 27261 26515 24946 508 -1007 3067 C ATOM 1027 CD GLU A 126 -43.348 26.314 28.153 1.00207.53 C ANISOU 1027 CD GLU A 126 27213 26713 24927 781 -1336 3704 C ATOM 1028 OE1 GLU A 126 -43.829 27.282 28.779 1.00207.49 O ANISOU 1028 OE1 GLU A 126 26939 26570 25326 1210 -1155 3990 O ATOM 1029 OE2 GLU A 126 -43.706 26.006 26.997 1.00208.20 O ANISOU 1029 OE2 GLU A 126 27516 27045 24545 573 -1773 3931 O ATOM 1030 N ASN A 127 -43.975 22.488 31.365 1.00234.53 N ANISOU 1030 N ASN A 127 29486 30576 29051 253 -1433 2563 N ATOM 1031 CA ASN A 127 -44.183 21.068 31.097 1.00243.22 C ANISOU 1031 CA ASN A 127 30582 31928 29904 -163 -1696 2342 C ATOM 1032 C ASN A 127 -45.383 20.557 31.894 1.00260.16 C ANISOU 1032 C ASN A 127 32167 34283 32398 -108 -1864 2451 C ATOM 1033 O ASN A 127 -45.727 21.139 32.930 1.00262.10 O ANISOU 1033 O ASN A 127 32107 34383 33098 258 -1625 2547 O ATOM 1034 CB ASN A 127 -42.931 20.264 31.446 1.00229.19 C ANISOU 1034 CB ASN A 127 29137 29935 28010 -359 -1352 1803 C ATOM 1035 CG ASN A 127 -41.721 20.689 30.636 1.00221.04 C ANISOU 1035 CG ASN A 127 28615 28678 26693 -448 -1127 1676 C ATOM 1036 OD1 ASN A 127 -41.703 21.769 30.046 1.00226.63 O ANISOU 1036 OD1 ASN A 127 29463 29305 27341 -294 -1123 1956 O ATOM 1037 ND2 ASN A 127 -40.702 19.838 30.605 1.00209.17 N ANISOU 1037 ND2 ASN A 127 27394 27043 25038 -679 -892 1265 N ATOM 1038 N PRO A 128 -46.008 19.472 31.445 1.00272.51 N ANISOU 1038 N PRO A 128 33628 36152 33763 -492 -2220 2413 N ATOM 1039 CA PRO A 128 -47.231 18.974 32.094 1.00274.61 C ANISOU 1039 CA PRO A 128 33320 36630 34388 -492 -2380 2534 C ATOM 1040 C PRO A 128 -47.028 18.547 33.551 1.00264.42 C ANISOU 1040 C PRO A 128 31922 35089 33458 -326 -1921 2216 C ATOM 1041 O PRO A 128 -47.865 18.846 34.402 1.00270.71 O ANISOU 1041 O PRO A 128 32272 35865 34719 -56 -1814 2401 O ATOM 1042 CB PRO A 128 -47.605 17.761 31.239 1.00279.45 C ANISOU 1042 CB PRO A 128 34019 37558 34603 -1065 -2784 2415 C ATOM 1043 CG PRO A 128 -47.038 18.065 29.895 1.00282.53 C ANISOU 1043 CG PRO A 128 34916 37993 34438 -1262 -3012 2494 C ATOM 1044 CD PRO A 128 -45.763 18.818 30.148 1.00277.25 C ANISOU 1044 CD PRO A 128 34641 36924 33778 -963 -2525 2337 C ATOM 1045 N ARG A 129 -45.923 17.862 33.826 1.00235.64 N ANISOU 1045 N ARG A 129 28698 31236 29597 -469 -1639 1763 N ATOM 1046 CA ARG A 129 -45.549 17.468 35.182 1.00201.15 C ANISOU 1046 CA ARG A 129 24339 26611 25477 -293 -1231 1457 C ATOM 1047 C ARG A 129 -44.041 17.580 35.363 1.00185.36 C ANISOU 1047 C ARG A 129 22784 24333 23310 -226 -933 1127 C ATOM 1048 O ARG A 129 -43.551 18.444 36.090 1.00184.82 O ANISOU 1048 O ARG A 129 22743 24029 23452 95 -682 1106 O ATOM 1049 CB ARG A 129 -46.011 16.040 35.475 1.00190.11 C ANISOU 1049 CB ARG A 129 22879 25316 24038 -600 -1244 1233 C ATOM 1050 CG ARG A 129 -45.789 15.068 34.327 1.00186.38 C ANISOU 1050 CG ARG A 129 22704 25020 23090 -1104 -1477 1078 C ATOM 1051 CD ARG A 129 -45.304 13.719 34.833 1.00180.07 C ANISOU 1051 CD ARG A 129 22179 24073 22166 -1301 -1195 662 C ATOM 1052 NE ARG A 129 -45.711 12.628 33.952 1.00183.56 N ANISOU 1052 NE ARG A 129 22764 24711 22269 -1840 -1406 562 N ATOM 1053 CZ ARG A 129 -46.904 12.044 33.989 1.00185.16 C ANISOU 1053 CZ ARG A 129 22634 25130 22590 -2104 -1601 637 C ATOM 1054 NH1 ARG A 129 -47.815 12.446 34.865 1.00184.45 N ANISOU 1054 NH1 ARG A 129 22022 25074 22987 -1839 -1572 837 N ATOM 1055 NH2 ARG A 129 -47.188 11.057 33.150 1.00186.91 N ANISOU 1055 NH2 ARG A 129 23054 25512 22453 -2661 -1790 502 N ATOM 1056 N ALA A 130 -43.313 16.705 34.679 1.00165.41 N ANISOU 1056 N ALA A 130 20603 21828 20420 -550 -950 871 N ATOM 1057 CA ALA A 130 -41.861 16.808 34.580 1.00142.82 C ANISOU 1057 CA ALA A 130 18109 18737 17419 -523 -694 602 C ATOM 1058 C ALA A 130 -41.146 16.549 35.900 1.00121.50 C ANISOU 1058 C ALA A 130 15423 15809 14934 -292 -386 311 C ATOM 1059 O ALA A 130 -41.704 16.752 36.978 1.00114.70 O ANISOU 1059 O ALA A 130 14342 14893 14346 -55 -316 360 O ATOM 1060 CB ALA A 130 -41.453 18.160 34.009 1.00145.37 C ANISOU 1060 CB ALA A 130 18517 18975 17744 -371 -684 799 C ATOM 1061 N LEU A 131 -39.899 16.108 35.794 1.00112.73 N ANISOU 1061 N LEU A 131 14583 14556 13694 -355 -197 24 N ATOM 1062 CA LEU A 131 -39.015 15.964 36.939 1.00101.38 C ANISOU 1062 CA LEU A 131 13167 12924 12430 -125 26 -234 C ATOM 1063 C LEU A 131 -37.580 15.954 36.435 1.00 96.61 C ANISOU 1063 C LEU A 131 12770 12191 11749 -187 193 -441 C ATOM 1064 O LEU A 131 -37.337 15.674 35.262 1.00114.01 O ANISOU 1064 O LEU A 131 15177 14424 13719 -441 208 -434 O ATOM 1065 CB LEU A 131 -39.320 14.673 37.698 1.00 93.68 C ANISOU 1065 CB LEU A 131 12212 11947 11434 -136 93 -390 C ATOM 1066 CG LEU A 131 -38.415 14.357 38.890 1.00 96.00 C ANISOU 1066 CG LEU A 131 12576 12061 11841 117 270 -633 C ATOM 1067 CD1 LEU A 131 -38.738 12.985 39.461 1.00 89.40 C ANISOU 1067 CD1 LEU A 131 11848 11197 10923 97 373 -755 C ATOM 1068 CD2 LEU A 131 -36.950 14.444 38.490 1.00105.01 C ANISOU 1068 CD2 LEU A 131 13832 13106 12959 113 376 -811 C ATOM 1069 N SER A 132 -36.625 16.239 37.313 1.00 88.93 N ANISOU 1069 N SER A 132 11751 11068 10972 26 325 -628 N ATOM 1070 CA SER A 132 -35.224 16.058 36.948 1.00 77.03 C ANISOU 1070 CA SER A 132 10344 9445 9480 -22 505 -839 C ATOM 1071 C SER A 132 -34.301 16.276 38.142 1.00 74.42 C ANISOU 1071 C SER A 132 9876 9008 9392 219 548 -1038 C ATOM 1072 O SER A 132 -34.692 16.889 39.135 1.00 60.73 O ANISOU 1072 O SER A 132 8047 7253 7775 397 457 -1008 O ATOM 1073 CB SER A 132 -34.836 17.003 35.809 1.00 71.54 C ANISOU 1073 CB SER A 132 9744 8695 8743 -167 579 -749 C ATOM 1074 OG SER A 132 -35.057 18.354 36.173 1.00 98.80 O ANISOU 1074 OG SER A 132 13076 12098 12365 -23 536 -626 O ATOM 1075 N PHE A 133 -33.078 15.767 38.043 1.00 81.28 N ANISOU 1075 N PHE A 133 11959 7895 11030 -775 -414 -2075 N ATOM 1076 CA PHE A 133 -32.062 16.052 39.048 1.00 72.76 C ANISOU 1076 CA PHE A 133 10936 6864 9846 -1009 -603 -2264 C ATOM 1077 C PHE A 133 -30.737 16.401 38.378 1.00 79.10 C ANISOU 1077 C PHE A 133 11643 7507 10905 -1248 -756 -2071 C ATOM 1078 O PHE A 133 -30.366 15.806 37.366 1.00 92.86 O ANISOU 1078 O PHE A 133 13227 9306 12748 -1256 -716 -1731 O ATOM 1079 CB PHE A 133 -31.893 14.875 40.018 1.00 68.87 C ANISOU 1079 CB PHE A 133 10415 6803 8949 -1044 -633 -2266 C ATOM 1080 CG PHE A 133 -31.249 13.659 39.410 1.00 68.57 C ANISOU 1080 CG PHE A 133 10195 6992 8868 -1078 -660 -1887 C ATOM 1081 CD1 PHE A 133 -32.014 12.704 38.763 1.00 75.86 C ANISOU 1081 CD1 PHE A 133 11045 8048 9731 -907 -481 -1660 C ATOM 1082 CD2 PHE A 133 -29.880 13.456 39.512 1.00 74.78 C ANISOU 1082 CD2 PHE A 133 10870 7864 9680 -1274 -873 -1787 C ATOM 1083 CE1 PHE A 133 -31.427 11.579 38.214 1.00 82.91 C ANISOU 1083 CE1 PHE A 133 11793 9123 10588 -923 -506 -1341 C ATOM 1084 CE2 PHE A 133 -29.287 12.334 38.963 1.00 75.82 C ANISOU 1084 CE2 PHE A 133 10825 8197 9787 -1268 -896 -1468 C ATOM 1085 CZ PHE A 133 -30.061 11.395 38.314 1.00 76.06 C ANISOU 1085 CZ PHE A 133 10819 8327 9753 -1088 -709 -1247 C ATOM 1086 N VAL A 134 -30.033 17.374 38.948 1.00 86.15 N ANISOU 1086 N VAL A 134 12625 8208 11899 -1456 -920 -2310 N ATOM 1087 CA VAL A 134 -28.812 17.897 38.344 1.00 91.73 C ANISOU 1087 CA VAL A 134 13236 8729 12887 -1728 -1046 -2175 C ATOM 1088 C VAL A 134 -27.562 17.465 39.106 1.00 89.19 C ANISOU 1088 C VAL A 134 12768 8690 12431 -1970 -1266 -2228 C ATOM 1089 O VAL A 134 -27.508 17.550 40.332 1.00 91.29 O ANISOU 1089 O VAL A 134 13133 9086 12465 -2015 -1400 -2528 O ATOM 1090 CB VAL A 134 -28.847 19.439 38.271 1.00 91.28 C ANISOU 1090 CB VAL A 134 13382 8176 13124 -1834 -1086 -2393 C ATOM 1091 CG1 VAL A 134 -27.603 19.971 37.578 1.00 84.09 C ANISOU 1091 CG1 VAL A 134 12371 7069 12512 -2164 -1180 -2227 C ATOM 1092 CG2 VAL A 134 -30.101 19.907 37.550 1.00 92.29 C ANISOU 1092 CG2 VAL A 134 13660 8011 13394 -1549 -911 -2351 C ATOM 1093 N LEU A 135 -26.562 16.993 38.369 1.00 92.51 N ANISOU 1093 N LEU A 135 12944 9220 12986 -2112 -1307 -1944 N ATOM 1094 CA LEU A 135 -25.267 16.661 38.950 1.00 83.47 C ANISOU 1094 CA LEU A 135 11600 8327 11786 -2337 -1542 -1985 C ATOM 1095 C LEU A 135 -24.209 17.639 38.453 1.00 78.73 C ANISOU 1095 C LEU A 135 10889 7480 11547 -2673 -1625 -1994 C ATOM 1096 O LEU A 135 -23.864 17.643 37.272 1.00 77.65 O ANISOU 1096 O LEU A 135 10611 7245 11648 -2742 -1495 -1714 O ATOM 1097 CB LEU A 135 -24.869 15.225 38.605 1.00 72.76 C ANISOU 1097 CB LEU A 135 10003 7348 10296 -2224 -1533 -1683 C ATOM 1098 CG LEU A 135 -25.793 14.123 39.125 1.00 70.19 C ANISOU 1098 CG LEU A 135 9784 7281 9604 -1943 -1461 -1643 C ATOM 1099 CD1 LEU A 135 -25.284 12.752 38.708 1.00 67.75 C ANISOU 1099 CD1 LEU A 135 9254 7274 9214 -1848 -1472 -1340 C ATOM 1100 CD2 LEU A 135 -25.932 14.211 40.636 1.00 72.73 C ANISOU 1100 CD2 LEU A 135 10285 7745 9604 -1962 -1630 -1961 C ATOM 1101 N SER A 136 -23.696 18.469 39.354 1.00 91.96 N ANISOU 1101 N SER A 136 12635 9058 13248 -2905 -1832 -2325 N ATOM 1102 CA SER A 136 -22.725 19.488 38.971 1.00 99.27 C ANISOU 1102 CA SER A 136 13475 9716 14528 -3277 -1911 -2374 C ATOM 1103 C SER A 136 -21.496 19.492 39.875 1.00107.83 C ANISOU 1103 C SER A 136 14351 11044 15576 -3560 -2221 -2592 C ATOM 1104 O SER A 136 -21.590 19.243 41.077 1.00106.22 O ANISOU 1104 O SER A 136 14234 11057 15069 -3494 -2415 -2850 O ATOM 1105 CB SER A 136 -23.378 20.872 38.978 1.00 96.82 C ANISOU 1105 CB SER A 136 13507 8877 14402 -3332 -1851 -2594 C ATOM 1106 OG SER A 136 -23.866 21.199 40.268 1.00 98.88 O ANISOU 1106 OG SER A 136 13997 9142 14432 -3260 -1983 -3001 O ATOM 1107 N SER A 137 -20.342 19.774 39.279 1.00111.23 N ANISOU 1107 N SER A 137 14499 11456 16308 -3883 -2267 -2490 N ATOM 1108 CA SER A 137 -19.090 19.894 40.016 1.00 99.19 C ANISOU 1108 CA SER A 137 12715 10149 14823 -4193 -2576 -2707 C ATOM 1109 C SER A 137 -18.442 21.242 39.717 1.00100.42 C ANISOU 1109 C SER A 137 12877 9914 15366 -4643 -2596 -2851 C ATOM 1110 O SER A 137 -17.696 21.372 38.746 1.00101.12 O ANISOU 1110 O SER A 137 12708 9960 15754 -4883 -2479 -2631 O ATOM 1111 CB SER A 137 -18.138 18.750 39.661 1.00 94.64 C ANISOU 1111 CB SER A 137 11681 10031 14245 -4168 -2638 -2463 C ATOM 1112 OG SER A 137 -16.951 18.817 40.432 1.00100.75 O ANISOU 1112 OG SER A 137 12170 11058 15050 -4430 -2977 -2690 O ATOM 1113 N PRO A 138 -18.734 22.251 40.554 1.00112.61 N ANISOU 1113 N PRO A 138 14729 11162 16898 -4770 -2731 -3231 N ATOM 1114 CA PRO A 138 -18.300 23.642 40.360 1.00126.55 C ANISOU 1114 CA PRO A 138 16607 12450 19024 -5192 -2749 -3407 C ATOM 1115 C PRO A 138 -16.788 23.802 40.194 1.00133.80 C ANISOU 1115 C PRO A 138 17095 13529 20213 -5666 -2902 -3418 C ATOM 1116 O PRO A 138 -16.346 24.792 39.611 1.00135.60 O ANISOU 1116 O PRO A 138 17349 13371 20802 -6054 -2819 -3412 O ATOM 1117 CB PRO A 138 -18.780 24.341 41.640 1.00126.82 C ANISOU 1117 CB PRO A 138 16992 12315 18880 -5182 -2951 -3892 C ATOM 1118 CG PRO A 138 -18.988 23.244 42.631 1.00121.38 C ANISOU 1118 CG PRO A 138 16238 12152 17727 -4882 -3116 -3982 C ATOM 1119 CD PRO A 138 -19.455 22.077 41.825 1.00111.26 C ANISOU 1119 CD PRO A 138 14820 11117 16335 -4530 -2883 -3542 C ATOM 1120 N GLN A 139 -16.014 22.847 40.700 1.00132.24 N ANISOU 1120 N GLN A 139 16508 13887 19850 -5636 -3124 -3435 N ATOM 1121 CA GLN A 139 -14.564 22.876 40.541 1.00138.81 C ANISOU 1121 CA GLN A 139 16844 14954 20943 -6044 -3277 -3454 C ATOM 1122 C GLN A 139 -14.184 22.765 39.068 1.00130.78 C ANISOU 1122 C GLN A 139 15578 13878 20233 -6170 -2945 -3050 C ATOM 1123 O GLN A 139 -13.356 23.527 38.569 1.00135.43 O ANISOU 1123 O GLN A 139 15993 14307 21155 -6628 -2877 -3052 O ATOM 1124 CB GLN A 139 -13.904 21.749 41.341 1.00147.22 C ANISOU 1124 CB GLN A 139 17541 16645 21749 -5884 -3595 -3521 C ATOM 1125 CG GLN A 139 -14.089 21.844 42.850 1.00149.91 C ANISOU 1125 CG GLN A 139 18103 17110 21748 -5819 -3963 -3927 C ATOM 1126 CD GLN A 139 -15.436 21.322 43.316 1.00146.28 C ANISOU 1126 CD GLN A 139 18076 16643 20862 -5338 -3865 -3896 C ATOM 1127 OE1 GLN A 139 -16.283 20.945 42.506 1.00136.93 O ANISOU 1127 OE1 GLN A 139 17032 15331 19665 -5057 -3534 -3586 O ATOM 1128 NE2 GLN A 139 -15.637 21.294 44.628 1.00148.62 N ANISOU 1128 NE2 GLN A 139 18580 17096 20794 -5259 -4151 -4226 N ATOM 1129 N LEU A 140 -14.798 21.808 38.380 1.00126.62 N ANISOU 1129 N LEU A 140 15055 13503 19552 -5765 -2713 -2701 N ATOM 1130 CA LEU A 140 -14.552 21.600 36.958 1.00125.26 C ANISOU 1130 CA LEU A 140 14688 13305 19598 -5828 -2377 -2311 C ATOM 1131 C LEU A 140 -15.556 22.371 36.107 1.00130.84 C ANISOU 1131 C LEU A 140 15858 13457 20396 -5790 -2071 -2125 C ATOM 1132 O LEU A 140 -15.472 22.366 34.877 1.00129.44 O ANISOU 1132 O LEU A 140 15623 13183 20376 -5861 -1776 -1793 O ATOM 1133 CB LEU A 140 -14.615 20.109 36.621 1.00108.18 C ANISOU 1133 CB LEU A 140 12269 11610 17223 -5415 -2305 -2046 C ATOM 1134 CG LEU A 140 -13.585 19.218 37.316 1.00112.26 C ANISOU 1134 CG LEU A 140 12303 12683 17665 -5387 -2609 -2167 C ATOM 1135 CD1 LEU A 140 -13.905 17.749 37.092 1.00102.06 C ANISOU 1135 CD1 LEU A 140 10901 11753 16125 -4904 -2549 -1918 C ATOM 1136 CD2 LEU A 140 -12.183 19.545 36.824 1.00117.83 C ANISOU 1136 CD2 LEU A 140 12493 13536 18741 -5840 -2606 -2183 C ATOM 1137 N GLN A 141 -16.502 23.025 36.778 1.00134.32 N ANISOU 1137 N GLN A 141 16760 13548 20726 -5661 -2151 -2348 N ATOM 1138 CA GLN A 141 -17.575 23.775 36.124 1.00137.61 C ANISOU 1138 CA GLN A 141 17647 13422 21217 -5545 -1921 -2217 C ATOM 1139 C GLN A 141 -18.367 22.906 35.150 1.00129.20 C ANISOU 1139 C GLN A 141 16616 12468 20007 -5140 -1654 -1823 C ATOM 1140 O GLN A 141 -18.897 23.398 34.154 1.00129.60 O ANISOU 1140 O GLN A 141 16911 12147 20184 -5120 -1424 -1579 O ATOM 1141 CB GLN A 141 -17.015 25.001 35.397 1.00141.69 C ANISOU 1141 CB GLN A 141 18252 13462 22122 -6038 -1806 -2154 C ATOM 1142 CG GLN A 141 -16.372 26.028 36.316 1.00145.41 C ANISOU 1142 CG GLN A 141 18779 13803 22668 -6395 -1981 -2556 C ATOM 1143 CD GLN A 141 -15.947 27.282 35.579 1.00152.40 C ANISOU 1143 CD GLN A 141 19829 14281 23794 -6765 -1717 -2475 C ATOM 1144 OE1 GLN A 141 -16.144 27.404 34.370 1.00161.57 O ANISOU 1144 OE1 GLN A 141 21072 15238 25078 -6747 -1416 -2114 O ATOM 1145 NE2 GLN A 141 -15.360 28.225 36.307 1.00154.10 N ANISOU 1145 NE2 GLN A 141 20095 14382 24074 -7075 -1829 -2807 N ATOM 1146 N GLN A 142 -18.442 21.612 35.446 1.00119.53 N ANISOU 1146 N GLN A 142 15163 11742 18509 -4821 -1703 -1764 N ATOM 1147 CA GLN A 142 -19.205 20.681 34.626 1.00110.30 C ANISOU 1147 CA GLN A 142 14017 10710 17180 -4433 -1477 -1434 C ATOM 1148 C GLN A 142 -20.582 20.453 35.236 1.00109.34 C ANISOU 1148 C GLN A 142 14234 10529 16782 -4011 -1496 -1547 C ATOM 1149 O GLN A 142 -20.722 20.359 36.455 1.00110.33 O ANISOU 1149 O GLN A 142 14418 10788 16713 -3936 -1706 -1850 O ATOM 1150 CB GLN A 142 -18.460 19.353 34.479 1.00102.41 C ANISOU 1150 CB GLN A 142 12572 10263 16075 -4338 -1495 -1282 C ATOM 1151 CG GLN A 142 -17.076 19.483 33.864 1.00108.86 C ANISOU 1151 CG GLN A 142 12978 11216 17169 -4733 -1450 -1190 C ATOM 1152 CD GLN A 142 -17.113 20.063 32.465 1.00113.72 C ANISOU 1152 CD GLN A 142 13690 11521 17996 -4916 -1128 -891 C ATOM 1153 OE1 GLN A 142 -16.723 21.210 32.246 1.00121.84 O ANISOU 1153 OE1 GLN A 142 14817 12198 19277 -5315 -1092 -937 O ATOM 1154 NE2 GLN A 142 -17.579 19.270 31.507 1.00104.04 N ANISOU 1154 NE2 GLN A 142 12460 10417 16654 -4638 -896 -581 N ATOM 1155 N GLU A 143 -21.598 20.366 34.385 1.00103.17 N ANISOU 1155 N GLU A 143 13664 9565 15971 -3744 -1272 -1313 N ATOM 1156 CA GLU A 143 -22.967 20.212 34.856 1.00105.14 C ANISOU 1156 CA GLU A 143 14201 9751 15998 -3355 -1253 -1422 C ATOM 1157 C GLU A 143 -23.776 19.305 33.934 1.00 96.25 C ANISOU 1157 C GLU A 143 13067 8758 14744 -3017 -1043 -1102 C ATOM 1158 O GLU A 143 -23.649 19.377 32.712 1.00104.91 O ANISOU 1158 O GLU A 143 14136 9738 15986 -3072 -872 -802 O ATOM 1159 CB GLU A 143 -23.637 21.583 34.978 1.00118.26 C ANISOU 1159 CB GLU A 143 16247 10864 17822 -3388 -1254 -1612 C ATOM 1160 CG GLU A 143 -25.046 21.551 35.539 1.00128.13 C ANISOU 1160 CG GLU A 143 17762 12048 18873 -2992 -1230 -1792 C ATOM 1161 CD GLU A 143 -25.609 22.939 35.773 1.00144.25 C ANISOU 1161 CD GLU A 143 20165 13543 21101 -3008 -1261 -2041 C ATOM 1162 OE1 GLU A 143 -26.807 23.048 36.111 1.00151.59 O ANISOU 1162 OE1 GLU A 143 21302 14376 21920 -2670 -1214 -2198 O ATOM 1163 OE2 GLU A 143 -24.853 23.921 35.622 1.00147.15 O ANISOU 1163 OE2 GLU A 143 20604 13570 21736 -3361 -1329 -2091 O ATOM 1164 N VAL A 144 -24.597 18.443 34.526 1.00 82.57 N ANISOU 1164 N VAL A 144 11367 7280 12726 -2691 -1052 -1171 N ATOM 1165 CA VAL A 144 -25.468 17.564 33.756 1.00 82.23 C ANISOU 1165 CA VAL A 144 11328 7365 12552 -2375 -870 -915 C ATOM 1166 C VAL A 144 -26.816 17.386 34.458 1.00 82.61 C ANISOU 1166 C VAL A 144 11581 7426 12380 -2056 -851 -1099 C ATOM 1167 O VAL A 144 -26.876 17.183 35.671 1.00 87.26 O ANISOU 1167 O VAL A 144 12196 8190 12770 -2032 -974 -1360 O ATOM 1168 CB VAL A 144 -24.807 16.183 33.515 1.00 68.83 C ANISOU 1168 CB VAL A 144 9317 6112 10722 -2336 -856 -713 C ATOM 1169 CG1 VAL A 144 -24.351 15.560 34.827 1.00 73.28 C ANISOU 1169 CG1 VAL A 144 9767 7001 11074 -2341 -1067 -924 C ATOM 1170 CG2 VAL A 144 -25.750 15.252 32.766 1.00 64.85 C ANISOU 1170 CG2 VAL A 144 8839 5727 10076 -2024 -677 -483 C ATOM 1171 N GLU A 145 -27.896 17.477 33.689 1.00 73.20 N ANISOU 1171 N GLU A 145 10529 6066 11218 -1818 -696 -969 N ATOM 1172 CA GLU A 145 -29.238 17.323 34.238 1.00 77.09 C ANISOU 1172 CA GLU A 145 11167 6587 11536 -1513 -644 -1144 C ATOM 1173 C GLU A 145 -29.909 16.064 33.700 1.00 79.82 C ANISOU 1173 C GLU A 145 11399 7225 11702 -1273 -508 -922 C ATOM 1174 O GLU A 145 -30.114 15.925 32.494 1.00 91.46 O ANISOU 1174 O GLU A 145 12849 8626 13276 -1200 -402 -651 O ATOM 1175 CB GLU A 145 -30.092 18.553 33.923 1.00 79.05 C ANISOU 1175 CB GLU A 145 11668 6382 11986 -1396 -609 -1249 C ATOM 1176 CG GLU A 145 -31.512 18.476 34.457 1.00 85.31 C ANISOU 1176 CG GLU A 145 12565 7211 12637 -1065 -539 -1467 C ATOM 1177 CD GLU A 145 -32.288 19.758 34.233 1.00 94.20 C ANISOU 1177 CD GLU A 145 13930 7870 13993 -917 -540 -1613 C ATOM 1178 OE1 GLU A 145 -31.689 20.741 33.749 1.00102.15 O ANISOU 1178 OE1 GLU A 145 15068 8488 15256 -1099 -608 -1545 O ATOM 1179 OE2 GLU A 145 -33.498 19.783 34.541 1.00 92.17 O ANISOU 1179 OE2 GLU A 145 13724 7626 13668 -619 -470 -1798 O ATOM 1180 N PHE A 146 -30.246 15.148 34.601 1.00 65.36 N ANISOU 1180 N PHE A 146 9522 5720 9592 -1169 -514 -1038 N ATOM 1181 CA PHE A 146 -30.861 13.884 34.213 1.00 63.43 C ANISOU 1181 CA PHE A 146 9182 5749 9168 -978 -391 -851 C ATOM 1182 C PHE A 146 -32.382 13.937 34.312 1.00 66.50 C ANISOU 1182 C PHE A 146 9678 6107 9483 -720 -264 -977 C ATOM 1183 O PHE A 146 -32.936 14.250 35.366 1.00 59.51 O ANISOU 1183 O PHE A 146 8896 5242 8475 -668 -269 -1273 O ATOM 1184 CB PHE A 146 -30.329 12.739 35.078 1.00 71.56 C ANISOU 1184 CB PHE A 146 10111 7145 9932 -1025 -465 -857 C ATOM 1185 CG PHE A 146 -28.889 12.397 34.818 1.00 74.32 C ANISOU 1185 CG PHE A 146 10276 7601 10361 -1214 -582 -696 C ATOM 1186 CD1 PHE A 146 -27.873 13.058 35.487 1.00 76.85 C ANISOU 1186 CD1 PHE A 146 10566 7881 10753 -1439 -765 -858 C ATOM 1187 CD2 PHE A 146 -28.553 11.407 33.908 1.00 64.67 C ANISOU 1187 CD2 PHE A 146 8891 6533 9148 -1163 -509 -411 C ATOM 1188 CE1 PHE A 146 -26.548 12.742 35.251 1.00 78.46 C ANISOU 1188 CE1 PHE A 146 10542 8215 11052 -1609 -873 -733 C ATOM 1189 CE2 PHE A 146 -27.231 11.086 33.668 1.00 59.63 C ANISOU 1189 CE2 PHE A 146 8043 6015 8599 -1311 -601 -293 C ATOM 1190 CZ PHE A 146 -26.227 11.755 34.340 1.00 77.26 C ANISOU 1190 CZ PHE A 146 10210 8227 10919 -1533 -783 -452 C ATOM 1191 N ASP A 147 -33.050 13.627 33.206 1.00 69.77 N ANISOU 1191 N ASP A 147 10051 6494 9963 -560 -150 -768 N ATOM 1192 CA ASP A 147 -34.504 13.539 33.187 1.00 62.29 C ANISOU 1192 CA ASP A 147 9135 5572 8961 -307 -35 -873 C ATOM 1193 C ASP A 147 -34.925 12.101 33.459 1.00 55.52 C ANISOU 1193 C ASP A 147 8169 5086 7841 -252 61 -809 C ATOM 1194 O ASP A 147 -34.626 11.199 32.676 1.00 50.66 O ANISOU 1194 O ASP A 147 7453 4598 7198 -265 92 -547 O ATOM 1195 CB ASP A 147 -35.062 14.020 31.844 1.00 69.20 C ANISOU 1195 CB ASP A 147 10031 6215 10046 -157 -1 -694 C ATOM 1196 CG ASP A 147 -36.548 14.342 31.903 1.00 93.95 C ANISOU 1196 CG ASP A 147 13190 9301 13205 121 66 -878 C ATOM 1197 OD1 ASP A 147 -37.263 13.750 32.739 1.00 99.59 O ANISOU 1197 OD1 ASP A 147 13840 10270 13731 196 156 -1070 O ATOM 1198 OD2 ASP A 147 -37.002 15.191 31.108 1.00107.53 O ANISOU 1198 OD2 ASP A 147 14991 10732 15133 266 29 -828 O ATOM 1199 N VAL A 148 -35.620 11.889 34.571 1.00 58.34 N ANISOU 1199 N VAL A 148 8564 5607 7996 -202 122 -1057 N ATOM 1200 CA VAL A 148 -36.037 10.547 34.958 1.00 58.14 C ANISOU 1200 CA VAL A 148 8479 5910 7702 -190 224 -1001 C ATOM 1201 C VAL A 148 -37.257 10.101 34.158 1.00 59.08 C ANISOU 1201 C VAL A 148 8502 6087 7857 -12 371 -932 C ATOM 1202 O VAL A 148 -38.300 10.756 34.172 1.00 55.46 O ANISOU 1202 O VAL A 148 8035 5550 7486 147 442 -1126 O ATOM 1203 CB VAL A 148 -36.349 10.467 36.464 1.00 58.98 C ANISOU 1203 CB VAL A 148 8683 6191 7537 -236 261 -1281 C ATOM 1204 CG1 VAL A 148 -36.908 9.099 36.821 1.00 73.70 C ANISOU 1204 CG1 VAL A 148 10520 8363 9120 -241 395 -1200 C ATOM 1205 CG2 VAL A 148 -35.099 10.765 37.277 1.00 55.55 C ANISOU 1205 CG2 VAL A 148 8335 5745 7027 -422 76 -1344 C ATOM 1206 N LEU A 149 -37.114 8.980 33.458 1.00 54.91 N ANISOU 1206 N LEU A 149 7892 5700 7271 -30 404 -674 N ATOM 1207 CA LEU A 149 -38.176 8.459 32.607 1.00 51.41 C ANISOU 1207 CA LEU A 149 7346 5327 6859 108 517 -596 C ATOM 1208 C LEU A 149 -38.540 7.032 32.998 1.00 64.64 C ANISOU 1208 C LEU A 149 8988 7281 8290 46 629 -542 C ATOM 1209 O LEU A 149 -37.936 6.080 32.504 1.00 72.89 O ANISOU 1209 O LEU A 149 10019 8390 9286 -18 605 -312 O ATOM 1210 CB LEU A 149 -37.756 8.506 31.135 1.00 50.63 C ANISOU 1210 CB LEU A 149 7205 5091 6941 146 456 -331 C ATOM 1211 CG LEU A 149 -37.268 9.848 30.586 1.00 62.91 C ANISOU 1211 CG LEU A 149 8832 6337 8734 164 349 -307 C ATOM 1212 CD1 LEU A 149 -36.896 9.720 29.117 1.00 64.15 C ANISOU 1212 CD1 LEU A 149 8965 6411 8997 177 326 -17 C ATOM 1213 CD2 LEU A 149 -38.315 10.933 30.784 1.00 58.00 C ANISOU 1213 CD2 LEU A 149 8248 5549 8240 343 352 -540 C ATOM 1214 N PRO A 150 -39.523 6.882 33.899 1.00 66.49 N ANISOU 1214 N PRO A 150 9219 7672 8371 57 765 -762 N ATOM 1215 CA PRO A 150 -40.004 5.568 34.340 1.00 59.44 C ANISOU 1215 CA PRO A 150 8323 7026 7236 -37 901 -718 C ATOM 1216 C PRO A 150 -40.492 4.710 33.177 1.00 50.20 C ANISOU 1216 C PRO A 150 7036 5899 6140 5 951 -534 C ATOM 1217 O PRO A 150 -41.202 5.204 32.303 1.00 51.18 O ANISOU 1217 O PRO A 150 7034 5958 6453 149 956 -570 O ATOM 1218 CB PRO A 150 -41.161 5.916 35.281 1.00 56.31 C ANISOU 1218 CB PRO A 150 7899 6764 6731 -12 1073 -1028 C ATOM 1219 CG PRO A 150 -40.845 7.281 35.768 1.00 62.49 C ANISOU 1219 CG PRO A 150 8749 7380 7613 54 984 -1241 C ATOM 1220 CD PRO A 150 -40.205 7.979 34.605 1.00 60.50 C ANISOU 1220 CD PRO A 150 8473 6859 7655 146 812 -1081 C ATOM 1221 N ALA A 151 -40.107 3.439 33.172 1.00 43.23 N ANISOU 1221 N ALA A 151 6208 5114 5104 -110 967 -346 N ATOM 1222 CA ALA A 151 -40.499 2.531 32.104 1.00 51.99 C ANISOU 1222 CA ALA A 151 7233 6256 6264 -93 1009 -189 C ATOM 1223 C ALA A 151 -40.620 1.099 32.609 1.00 57.42 C ANISOU 1223 C ALA A 151 8010 7080 6725 -246 1105 -99 C ATOM 1224 O ALA A 151 -39.888 0.683 33.505 1.00 62.17 O ANISOU 1224 O ALA A 151 8773 7704 7147 -343 1064 -38 O ATOM 1225 CB ALA A 151 -39.502 2.605 30.958 1.00 46.79 C ANISOU 1225 CB ALA A 151 6568 5450 5762 -35 868 24 C ATOM 1226 N PHE A 152 -41.555 0.354 32.030 1.00 63.72 N ANISOU 1226 N PHE A 152 8717 7960 7533 -270 1217 -89 N ATOM 1227 CA PHE A 152 -41.704 -1.064 32.329 1.00 64.38 C ANISOU 1227 CA PHE A 152 8908 8122 7433 -432 1310 19 C ATOM 1228 C PHE A 152 -40.466 -1.813 31.855 1.00 57.13 C ANISOU 1228 C PHE A 152 8114 7078 6515 -421 1169 265 C ATOM 1229 O PHE A 152 -39.853 -1.432 30.859 1.00 45.25 O ANISOU 1229 O PHE A 152 6537 5472 5184 -299 1055 347 O ATOM 1230 CB PHE A 152 -42.971 -1.616 31.665 1.00 58.67 C ANISOU 1230 CB PHE A 152 8028 7497 6766 -474 1444 -47 C ATOM 1231 CG PHE A 152 -43.008 -3.117 31.564 1.00 51.89 C ANISOU 1231 CG PHE A 152 7288 6639 5786 -638 1506 101 C ATOM 1232 CD1 PHE A 152 -43.159 -3.901 32.696 1.00 59.55 C ANISOU 1232 CD1 PHE A 152 8438 7674 6515 -840 1632 124 C ATOM 1233 CD2 PHE A 152 -42.910 -3.742 30.332 1.00 40.18 C ANISOU 1233 CD2 PHE A 152 5768 5079 4418 -597 1441 214 C ATOM 1234 CE1 PHE A 152 -43.200 -5.281 32.602 1.00 54.11 C ANISOU 1234 CE1 PHE A 152 7899 6934 5728 -997 1683 273 C ATOM 1235 CE2 PHE A 152 -42.950 -5.121 30.231 1.00 40.42 C ANISOU 1235 CE2 PHE A 152 5930 5071 4356 -745 1493 329 C ATOM 1236 CZ PHE A 152 -43.096 -5.891 31.367 1.00 42.10 C ANISOU 1236 CZ PHE A 152 6331 5310 4354 -945 1611 365 C ATOM 1237 N ASP A 153 -40.090 -2.873 32.565 1.00 57.47 N ANISOU 1237 N ASP A 153 8349 7126 6360 -541 1179 384 N ATOM 1238 CA ASP A 153 -38.927 -3.645 32.158 1.00 58.74 C ANISOU 1238 CA ASP A 153 8613 7168 6537 -493 1040 596 C ATOM 1239 C ASP A 153 -39.377 -4.792 31.264 1.00 60.85 C ANISOU 1239 C ASP A 153 8888 7392 6841 -528 1109 681 C ATOM 1240 O ASP A 153 -39.951 -5.774 31.732 1.00 72.48 O ANISOU 1240 O ASP A 153 10493 8880 8166 -678 1215 710 O ATOM 1241 CB ASP A 153 -38.181 -4.179 33.384 1.00 62.12 C ANISOU 1241 CB ASP A 153 9270 7592 6742 -561 960 693 C ATOM 1242 CG ASP A 153 -36.817 -4.752 33.041 1.00 78.74 C ANISOU 1242 CG ASP A 153 11432 9580 8903 -452 772 880 C ATOM 1243 OD1 ASP A 153 -36.466 -4.806 31.843 1.00 91.60 O ANISOU 1243 OD1 ASP A 153 12931 11141 10730 -345 743 930 O ATOM 1244 OD2 ASP A 153 -36.096 -5.157 33.976 1.00 79.51 O ANISOU 1244 OD2 ASP A 153 11703 9670 8838 -464 651 971 O ATOM 1245 N ALA A 154 -39.094 -4.658 29.973 1.00 47.21 N ANISOU 1245 N ALA A 154 7036 5604 5299 -405 1051 720 N ATOM 1246 CA ALA A 154 -39.463 -5.667 28.989 1.00 45.81 C ANISOU 1246 CA ALA A 154 6861 5382 5162 -423 1096 770 C ATOM 1247 C ALA A 154 -38.438 -6.792 28.925 1.00 69.73 C ANISOU 1247 C ALA A 154 10063 8280 8153 -391 1018 938 C ATOM 1248 O ALA A 154 -38.790 -7.970 28.853 1.00 75.79 O ANISOU 1248 O ALA A 154 10963 8978 8857 -481 1074 983 O ATOM 1249 CB ALA A 154 -39.632 -5.026 27.622 1.00 43.87 C ANISOU 1249 CB ALA A 154 6434 5144 5089 -301 1066 730 C ATOM 1250 N LEU A 155 -37.165 -6.412 28.957 1.00 71.85 N ANISOU 1250 N LEU A 155 10318 8504 8475 -261 883 1017 N ATOM 1251 CA LEU A 155 -36.071 -7.354 28.768 1.00 67.06 C ANISOU 1251 CA LEU A 155 9812 7784 7882 -166 787 1154 C ATOM 1252 C LEU A 155 -35.816 -8.192 30.014 1.00 81.71 C ANISOU 1252 C LEU A 155 11906 9579 9560 -225 730 1250 C ATOM 1253 O LEU A 155 -35.268 -9.291 29.928 1.00 94.01 O ANISOU 1253 O LEU A 155 13609 11004 11107 -160 667 1362 O ATOM 1254 CB LEU A 155 -34.796 -6.608 28.372 1.00 56.97 C ANISOU 1254 CB LEU A 155 8385 6518 6741 -17 670 1186 C ATOM 1255 CG LEU A 155 -34.903 -5.696 27.148 1.00 60.80 C ANISOU 1255 CG LEU A 155 8679 7046 7376 33 720 1132 C ATOM 1256 CD1 LEU A 155 -33.596 -4.959 26.914 1.00 73.48 C ANISOU 1256 CD1 LEU A 155 10149 8665 9104 122 631 1174 C ATOM 1257 CD2 LEU A 155 -35.301 -6.492 25.914 1.00 58.48 C ANISOU 1257 CD2 LEU A 155 8390 6716 7112 65 799 1135 C ATOM 1258 N GLY A 156 -36.219 -7.673 31.170 1.00 85.55 N ANISOU 1258 N GLY A 156 12454 10154 9896 -338 748 1204 N ATOM 1259 CA GLY A 156 -35.958 -8.348 32.427 1.00 90.25 C ANISOU 1259 CA GLY A 156 13310 10711 10272 -403 681 1311 C ATOM 1260 C GLY A 156 -34.466 -8.399 32.683 1.00 82.32 C ANISOU 1260 C GLY A 156 12318 9658 9302 -226 445 1418 C ATOM 1261 O GLY A 156 -33.798 -7.366 32.719 1.00 73.89 O ANISOU 1261 O GLY A 156 11073 8677 8324 -153 347 1354 O ATOM 1262 N GLN A 157 -33.940 -9.606 32.858 1.00 81.52 N ANISOU 1262 N GLN A 157 12421 9410 9144 -155 344 1574 N ATOM 1263 CA GLN A 157 -32.504 -9.787 33.007 1.00 77.63 C ANISOU 1263 CA GLN A 157 11902 8876 8718 55 100 1667 C ATOM 1264 C GLN A 157 -31.887 -10.050 31.639 1.00 74.89 C ANISOU 1264 C GLN A 157 11356 8464 8634 234 103 1654 C ATOM 1265 O GLN A 157 -32.115 -11.099 31.037 1.00 76.20 O ANISOU 1265 O GLN A 157 11639 8476 8837 272 164 1701 O ATOM 1266 CB GLN A 157 -32.197 -10.941 33.963 1.00 87.85 C ANISOU 1266 CB GLN A 157 13536 10031 9812 84 -46 1849 C ATOM 1267 CG GLN A 157 -32.937 -10.864 35.289 1.00100.17 C ANISOU 1267 CG GLN A 157 15359 11654 11049 -132 -2 1881 C ATOM 1268 CD GLN A 157 -32.710 -12.088 36.154 1.00104.05 C ANISOU 1268 CD GLN A 157 16248 11972 11313 -122 -136 2102 C ATOM 1269 OE1 GLN A 157 -31.784 -12.865 35.920 1.00107.64 O ANISOU 1269 OE1 GLN A 157 16762 12266 11869 103 -335 2225 O ATOM 1270 NE2 GLN A 157 -33.561 -12.269 37.158 1.00 99.30 N ANISOU 1270 NE2 GLN A 157 15931 11398 10398 -361 -23 2154 N ATOM 1271 N TRP A 158 -31.102 -9.093 31.154 1.00 73.66 N ANISOU 1271 N TRP A 158 10913 8424 8652 327 50 1580 N ATOM 1272 CA TRP A 158 -30.524 -9.189 29.820 1.00 67.22 C ANISOU 1272 CA TRP A 158 9888 7592 8061 471 96 1551 C ATOM 1273 C TRP A 158 -29.048 -8.815 29.813 1.00 72.68 C ANISOU 1273 C TRP A 158 10351 8363 8902 634 -74 1554 C ATOM 1274 O TRP A 158 -28.644 -7.817 30.409 1.00 82.51 O ANISOU 1274 O TRP A 158 11474 9728 10149 577 -168 1513 O ATOM 1275 CB TRP A 158 -31.289 -8.296 28.839 1.00 72.91 C ANISOU 1275 CB TRP A 158 10448 8389 8865 368 285 1442 C ATOM 1276 CG TRP A 158 -30.719 -8.312 27.452 1.00 78.11 C ANISOU 1276 CG TRP A 158 10918 9058 9703 488 353 1417 C ATOM 1277 CD1 TRP A 158 -31.025 -9.187 26.450 1.00 73.64 C ANISOU 1277 CD1 TRP A 158 10407 8407 9165 543 458 1406 C ATOM 1278 CD2 TRP A 158 -29.740 -7.413 26.914 1.00 76.33 C ANISOU 1278 CD2 TRP A 158 10429 8939 9633 546 336 1390 C ATOM 1279 NE1 TRP A 158 -30.299 -8.889 25.322 1.00 69.83 N ANISOU 1279 NE1 TRP A 158 9720 7990 8822 646 515 1371 N ATOM 1280 CE2 TRP A 158 -29.502 -7.804 25.581 1.00 64.51 C ANISOU 1280 CE2 TRP A 158 8844 7435 8232 638 453 1372 C ATOM 1281 CE3 TRP A 158 -29.042 -6.316 27.429 1.00 73.15 C ANISOU 1281 CE3 TRP A 158 9864 8635 9294 504 241 1370 C ATOM 1282 CZ2 TRP A 158 -28.595 -7.139 24.758 1.00 61.22 C ANISOU 1282 CZ2 TRP A 158 8183 7122 7956 682 503 1351 C ATOM 1283 CZ3 TRP A 158 -28.144 -5.655 26.610 1.00 60.52 C ANISOU 1283 CZ3 TRP A 158 8013 7118 7863 532 279 1350 C ATOM 1284 CH2 TRP A 158 -27.929 -6.068 25.289 1.00 60.27 C ANISOU 1284 CH2 TRP A 158 7899 7093 7910 616 421 1349 C ATOM 1285 N THR A 159 -28.250 -9.627 29.128 1.00 71.40 N ANISOU 1285 N THR A 159 10118 8138 8875 834 -107 1580 N ATOM 1286 CA THR A 159 -26.823 -9.370 28.985 1.00 73.81 C ANISOU 1286 CA THR A 159 10143 8546 9356 1001 -241 1560 C ATOM 1287 C THR A 159 -26.448 -9.316 27.507 1.00 79.00 C ANISOU 1287 C THR A 159 10568 9247 10201 1079 -65 1487 C ATOM 1288 O THR A 159 -27.050 -10.014 26.690 1.00 77.66 O ANISOU 1288 O THR A 159 10519 8973 10017 1103 83 1475 O ATOM 1289 CB THR A 159 -25.979 -10.448 29.695 1.00 71.63 C ANISOU 1289 CB THR A 159 9966 8180 9071 1229 -484 1648 C ATOM 1290 OG1 THR A 159 -26.282 -11.735 29.143 1.00 74.94 O ANISOU 1290 OG1 THR A 159 10582 8394 9495 1355 -415 1688 O ATOM 1291 CG2 THR A 159 -26.273 -10.459 31.188 1.00 82.89 C ANISOU 1291 CG2 THR A 159 11647 9583 10262 1142 -672 1739 C ATOM 1292 N PRO A 160 -25.461 -8.474 27.158 1.00 80.59 N ANISOU 1292 N PRO A 160 10443 9612 10566 1095 -73 1431 N ATOM 1293 CA PRO A 160 -24.975 -8.362 25.778 1.00 78.07 C ANISOU 1293 CA PRO A 160 9893 9369 10399 1151 115 1367 C ATOM 1294 C PRO A 160 -24.545 -9.708 25.199 1.00 78.65 C ANISOU 1294 C PRO A 160 9993 9355 10537 1404 134 1348 C ATOM 1295 O PRO A 160 -23.974 -10.531 25.913 1.00 92.59 O ANISOU 1295 O PRO A 160 11805 11048 12328 1596 -65 1381 O ATOM 1296 CB PRO A 160 -23.780 -7.415 25.906 1.00 78.09 C ANISOU 1296 CB PRO A 160 9547 9560 10566 1123 45 1325 C ATOM 1297 CG PRO A 160 -24.097 -6.582 27.098 1.00 71.54 C ANISOU 1297 CG PRO A 160 8799 8740 9642 955 -111 1345 C ATOM 1298 CD PRO A 160 -24.806 -7.501 28.052 1.00 73.83 C ANISOU 1298 CD PRO A 160 9425 8886 9740 1015 -242 1415 C ATOM 1299 N GLY A 161 -24.823 -9.923 23.918 1.00 73.68 N ANISOU 1299 N GLY A 161 9351 8722 9923 1414 358 1288 N ATOM 1300 CA GLY A 161 -24.521 -11.189 23.276 1.00 84.87 C ANISOU 1300 CA GLY A 161 10820 10035 11392 1648 405 1231 C ATOM 1301 C GLY A 161 -25.752 -12.067 23.183 1.00 99.86 C ANISOU 1301 C GLY A 161 13089 11713 13142 1604 447 1249 C ATOM 1302 O GLY A 161 -25.749 -13.096 22.508 1.00 93.93 O ANISOU 1302 O GLY A 161 12441 10836 12413 1753 515 1181 O ATOM 1303 N TYR A 162 -26.811 -11.653 23.870 1.00105.48 N ANISOU 1303 N TYR A 162 13989 12379 13708 1387 415 1322 N ATOM 1304 CA TYR A 162 -28.073 -12.381 23.860 1.00 96.61 C ANISOU 1304 CA TYR A 162 13183 11076 12447 1281 467 1333 C ATOM 1305 C TYR A 162 -29.160 -11.588 23.148 1.00 77.65 C ANISOU 1305 C TYR A 162 10770 8768 9965 1064 634 1286 C ATOM 1306 O TYR A 162 -29.513 -10.487 23.569 1.00 73.83 O ANISOU 1306 O TYR A 162 10212 8397 9445 912 626 1314 O ATOM 1307 CB TYR A 162 -28.518 -12.707 25.287 1.00104.30 C ANISOU 1307 CB TYR A 162 14401 11926 13302 1205 307 1447 C ATOM 1308 CG TYR A 162 -27.743 -13.831 25.934 1.00111.93 C ANISOU 1308 CG TYR A 162 15508 12715 14305 1432 120 1519 C ATOM 1309 CD1 TYR A 162 -26.447 -13.636 26.392 1.00116.09 C ANISOU 1309 CD1 TYR A 162 15828 13336 14946 1632 -59 1541 C ATOM 1310 CD2 TYR A 162 -28.313 -15.087 26.096 1.00119.33 C ANISOU 1310 CD2 TYR A 162 16789 13380 15171 1446 105 1566 C ATOM 1311 CE1 TYR A 162 -25.738 -14.662 26.987 1.00126.63 C ANISOU 1311 CE1 TYR A 162 17291 14502 16320 1881 -270 1612 C ATOM 1312 CE2 TYR A 162 -27.613 -16.117 26.691 1.00127.51 C ANISOU 1312 CE2 TYR A 162 17997 14209 16242 1676 -89 1653 C ATOM 1313 CZ TYR A 162 -26.326 -15.900 27.134 1.00129.68 C ANISOU 1313 CZ TYR A 162 18058 14587 16627 1914 -288 1678 C ATOM 1314 OH TYR A 162 -25.625 -16.925 27.727 1.00131.13 O ANISOU 1314 OH TYR A 162 18411 14561 16853 2184 -519 1769 O ATOM 1315 N LYS A 163 -29.687 -12.151 22.066 1.00 67.86 N ANISOU 1315 N LYS A 163 9610 7476 8697 1065 765 1203 N ATOM 1316 CA LYS A 163 -30.776 -11.517 21.334 1.00 61.25 C ANISOU 1316 CA LYS A 163 8774 6725 7772 887 885 1157 C ATOM 1317 C LYS A 163 -32.074 -11.637 22.125 1.00 52.87 C ANISOU 1317 C LYS A 163 7897 5586 6604 696 854 1181 C ATOM 1318 O LYS A 163 -32.469 -12.740 22.506 1.00 60.56 O ANISOU 1318 O LYS A 163 9090 6384 7538 677 828 1185 O ATOM 1319 CB LYS A 163 -30.933 -12.143 19.948 1.00 69.51 C ANISOU 1319 CB LYS A 163 9860 7756 8794 945 1010 1043 C ATOM 1320 CG LYS A 163 -31.985 -11.473 19.079 1.00 87.13 C ANISOU 1320 CG LYS A 163 12081 10100 10923 792 1097 997 C ATOM 1321 CD LYS A 163 -32.115 -12.172 17.737 1.00 89.73 C ANISOU 1321 CD LYS A 163 12478 10424 11191 848 1198 870 C ATOM 1322 CE LYS A 163 -30.823 -12.092 16.939 1.00 72.70 C ANISOU 1322 CE LYS A 163 10170 8368 9083 1021 1297 837 C ATOM 1323 NZ LYS A 163 -30.484 -10.693 16.561 1.00 55.32 N ANISOU 1323 NZ LYS A 163 7778 6371 6872 959 1356 916 N ATOM 1324 N PRO A 164 -32.736 -10.497 22.380 1.00 37.96 N ANISOU 1324 N PRO A 164 5924 3822 4677 551 867 1191 N ATOM 1325 CA PRO A 164 -33.969 -10.437 23.175 1.00 44.34 C ANISOU 1325 CA PRO A 164 6845 4612 5391 368 866 1186 C ATOM 1326 C PRO A 164 -35.055 -11.376 22.662 1.00 52.84 C ANISOU 1326 C PRO A 164 8065 5604 6407 264 937 1109 C ATOM 1327 O PRO A 164 -35.129 -11.638 21.461 1.00 58.15 O ANISOU 1327 O PRO A 164 8713 6288 7092 310 990 1032 O ATOM 1328 CB PRO A 164 -34.406 -8.976 23.032 1.00 40.09 C ANISOU 1328 CB PRO A 164 6138 4230 4863 297 889 1162 C ATOM 1329 CG PRO A 164 -33.146 -8.235 22.762 1.00 42.07 C ANISOU 1329 CG PRO A 164 6229 4547 5210 411 859 1209 C ATOM 1330 CD PRO A 164 -32.312 -9.161 21.925 1.00 40.09 C ANISOU 1330 CD PRO A 164 5981 4251 5001 556 893 1200 C ATOM 1331 N ASN A 165 -35.878 -11.879 23.577 1.00 53.21 N ANISOU 1331 N ASN A 165 8265 5576 6377 104 943 1122 N ATOM 1332 CA ASN A 165 -36.976 -12.772 23.231 1.00 57.38 C ANISOU 1332 CA ASN A 165 8919 6023 6859 -54 1014 1040 C ATOM 1333 C ASN A 165 -37.935 -12.112 22.246 1.00 61.17 C ANISOU 1333 C ASN A 165 9228 6672 7344 -124 1067 914 C ATOM 1334 O ASN A 165 -38.497 -11.057 22.539 1.00 66.53 O ANISOU 1334 O ASN A 165 9757 7505 8017 -179 1074 894 O ATOM 1335 CB ASN A 165 -37.726 -13.201 24.496 1.00 65.82 C ANISOU 1335 CB ASN A 165 10150 7026 7832 -262 1043 1087 C ATOM 1336 CG ASN A 165 -38.614 -14.415 24.276 1.00 76.00 C ANISOU 1336 CG ASN A 165 11621 8164 9090 -449 1115 1028 C ATOM 1337 OD1 ASN A 165 -39.091 -14.664 23.170 1.00 80.15 O ANISOU 1337 OD1 ASN A 165 12089 8706 9657 -473 1147 901 O ATOM 1338 ND2 ASN A 165 -38.841 -15.177 25.340 1.00 82.27 N ANISOU 1338 ND2 ASN A 165 12656 8806 9797 -602 1135 1123 N ATOM 1339 N PRO A 166 -38.115 -12.729 21.067 1.00 61.36 N ANISOU 1339 N PRO A 166 9281 6661 7373 -103 1088 819 N ATOM 1340 CA PRO A 166 -39.040 -12.231 20.041 1.00 51.66 C ANISOU 1340 CA PRO A 166 7914 5592 6122 -157 1098 698 C ATOM 1341 C PRO A 166 -40.463 -12.053 20.567 1.00 48.06 C ANISOU 1341 C PRO A 166 7384 5228 5647 -372 1124 620 C ATOM 1342 O PRO A 166 -41.199 -11.211 20.056 1.00 42.94 O ANISOU 1342 O PRO A 166 6556 4756 5002 -376 1098 546 O ATOM 1343 CB PRO A 166 -38.989 -13.321 18.967 1.00 39.38 C ANISOU 1343 CB PRO A 166 6484 3934 4545 -138 1110 595 C ATOM 1344 CG PRO A 166 -37.643 -13.934 19.128 1.00 53.10 C ANISOU 1344 CG PRO A 166 8346 5504 6324 38 1110 672 C ATOM 1345 CD PRO A 166 -37.363 -13.908 20.603 1.00 60.52 C ANISOU 1345 CD PRO A 166 9345 6361 7288 6 1084 809 C ATOM 1346 N GLU A 167 -40.834 -12.836 21.578 1.00 53.24 N ANISOU 1346 N GLU A 167 8179 5769 6281 -545 1177 639 N ATOM 1347 CA GLU A 167 -42.147 -12.724 22.209 1.00 63.62 C ANISOU 1347 CA GLU A 167 9406 7191 7575 -779 1245 557 C ATOM 1348 C GLU A 167 -42.363 -11.336 22.806 1.00 62.86 C ANISOU 1348 C GLU A 167 9109 7285 7490 -726 1244 564 C ATOM 1349 O GLU A 167 -43.485 -10.832 22.838 1.00 65.39 O ANISOU 1349 O GLU A 167 9239 7775 7829 -824 1277 440 O ATOM 1350 CB GLU A 167 -42.312 -13.788 23.299 1.00 84.45 C ANISOU 1350 CB GLU A 167 12277 9654 10155 -988 1327 620 C ATOM 1351 CG GLU A 167 -42.278 -15.225 22.798 1.00101.79 C ANISOU 1351 CG GLU A 167 14707 11611 12358 -1077 1333 596 C ATOM 1352 CD GLU A 167 -43.591 -15.667 22.180 1.00115.38 C ANISOU 1352 CD GLU A 167 16337 13404 14099 -1322 1383 407 C ATOM 1353 OE1 GLU A 167 -43.657 -16.810 21.682 1.00121.28 O ANISOU 1353 OE1 GLU A 167 17271 13949 14860 -1421 1383 349 O ATOM 1354 OE2 GLU A 167 -44.558 -14.876 22.196 1.00117.97 O ANISOU 1354 OE2 GLU A 167 16398 13986 14441 -1411 1412 299 O ATOM 1355 N ILE A 168 -41.280 -10.728 23.282 1.00 54.44 N ANISOU 1355 N ILE A 168 8073 6185 6426 -566 1199 689 N ATOM 1356 CA ILE A 168 -41.338 -9.394 23.869 1.00 57.79 C ANISOU 1356 CA ILE A 168 8345 6745 6869 -506 1187 687 C ATOM 1357 C ILE A 168 -41.718 -8.354 22.821 1.00 51.41 C ANISOU 1357 C ILE A 168 7331 6069 6135 -385 1127 613 C ATOM 1358 O ILE A 168 -42.535 -7.468 23.074 1.00 53.06 O ANISOU 1358 O ILE A 168 7377 6407 6378 -393 1133 523 O ATOM 1359 CB ILE A 168 -39.992 -9.001 24.507 1.00 62.37 C ANISOU 1359 CB ILE A 168 9002 7251 7445 -373 1126 825 C ATOM 1360 CG1 ILE A 168 -39.558 -10.055 25.527 1.00 69.70 C ANISOU 1360 CG1 ILE A 168 10165 8036 8282 -456 1139 924 C ATOM 1361 CG2 ILE A 168 -40.087 -7.632 25.154 1.00 53.18 C ANISOU 1361 CG2 ILE A 168 7705 6199 6301 -337 1112 795 C ATOM 1362 CD1 ILE A 168 -38.209 -9.778 26.153 1.00 75.59 C ANISOU 1362 CD1 ILE A 168 10970 8725 9024 -313 1038 1049 C ATOM 1363 N TYR A 169 -41.118 -8.472 21.641 1.00 49.75 N ANISOU 1363 N TYR A 169 7142 5821 5938 -262 1069 650 N ATOM 1364 CA TYR A 169 -41.413 -7.569 20.536 1.00 52.81 C ANISOU 1364 CA TYR A 169 7395 6316 6355 -147 997 617 C ATOM 1365 C TYR A 169 -42.816 -7.808 19.992 1.00 56.58 C ANISOU 1365 C TYR A 169 7761 6913 6826 -238 976 461 C ATOM 1366 O TYR A 169 -43.466 -6.884 19.505 1.00 59.73 O ANISOU 1366 O TYR A 169 8007 7429 7257 -156 897 409 O ATOM 1367 CB TYR A 169 -40.375 -7.733 19.425 1.00 50.18 C ANISOU 1367 CB TYR A 169 7140 5932 5994 -19 971 697 C ATOM 1368 CG TYR A 169 -39.044 -7.100 19.751 1.00 56.21 C ANISOU 1368 CG TYR A 169 7917 6640 6799 88 973 832 C ATOM 1369 CD1 TYR A 169 -38.979 -5.859 20.370 1.00 56.66 C ANISOU 1369 CD1 TYR A 169 7888 6724 6916 116 943 871 C ATOM 1370 CD2 TYR A 169 -37.852 -7.745 19.452 1.00 66.01 C ANISOU 1370 CD2 TYR A 169 9242 7803 8034 160 1004 897 C ATOM 1371 CE1 TYR A 169 -37.767 -5.274 20.673 1.00 56.01 C ANISOU 1371 CE1 TYR A 169 7802 6595 6883 178 936 976 C ATOM 1372 CE2 TYR A 169 -36.632 -7.169 19.754 1.00 68.01 C ANISOU 1372 CE2 TYR A 169 9458 8038 8346 241 1002 1001 C ATOM 1373 CZ TYR A 169 -36.597 -5.932 20.364 1.00 60.68 C ANISOU 1373 CZ TYR A 169 8443 7140 7473 232 964 1042 C ATOM 1374 OH TYR A 169 -35.388 -5.351 20.667 1.00 58.30 O ANISOU 1374 OH TYR A 169 8090 6822 7240 279 953 1128 O ATOM 1375 N VAL A 170 -43.276 -9.052 20.079 1.00 55.43 N ANISOU 1375 N VAL A 170 7690 6724 6645 -407 1033 385 N ATOM 1376 CA VAL A 170 -44.625 -9.402 19.656 1.00 47.79 C ANISOU 1376 CA VAL A 170 6590 5881 5685 -543 1016 212 C ATOM 1377 C VAL A 170 -45.658 -8.637 20.479 1.00 51.11 C ANISOU 1377 C VAL A 170 6791 6459 6170 -601 1049 115 C ATOM 1378 O VAL A 170 -46.590 -8.049 19.930 1.00 67.70 O ANISOU 1378 O VAL A 170 8676 8726 8321 -551 963 -6 O ATOM 1379 CB VAL A 170 -44.881 -10.919 19.781 1.00 40.80 C ANISOU 1379 CB VAL A 170 5854 4880 4767 -768 1094 151 C ATOM 1380 CG1 VAL A 170 -46.365 -11.225 19.673 1.00 58.08 C ANISOU 1380 CG1 VAL A 170 7859 7221 6989 -978 1104 -46 C ATOM 1381 CG2 VAL A 170 -44.095 -11.678 18.723 1.00 40.82 C ANISOU 1381 CG2 VAL A 170 6040 4751 4719 -686 1047 172 C ATOM 1382 N GLN A 171 -45.476 -8.639 21.796 1.00 52.11 N ANISOU 1382 N GLN A 171 6972 6539 6287 -690 1167 160 N ATOM 1383 CA GLN A 171 -46.369 -7.917 22.696 1.00 62.05 C ANISOU 1383 CA GLN A 171 8034 7952 7589 -742 1238 48 C ATOM 1384 C GLN A 171 -46.316 -6.416 22.432 1.00 64.72 C ANISOU 1384 C GLN A 171 8224 8361 8007 -491 1128 42 C ATOM 1385 O GLN A 171 -47.330 -5.724 22.523 1.00 67.53 O ANISOU 1385 O GLN A 171 8340 8876 8442 -451 1116 -110 O ATOM 1386 CB GLN A 171 -46.010 -8.203 24.156 1.00 65.27 C ANISOU 1386 CB GLN A 171 8592 8291 7918 -878 1384 116 C ATOM 1387 CG GLN A 171 -46.081 -9.671 24.540 1.00 85.17 C ANISOU 1387 CG GLN A 171 11311 10698 10351 -1137 1495 153 C ATOM 1388 CD GLN A 171 -45.690 -9.914 25.986 1.00102.72 C ANISOU 1388 CD GLN A 171 13727 12849 12453 -1257 1614 255 C ATOM 1389 OE1 GLN A 171 -45.510 -8.974 26.761 1.00 98.69 O ANISOU 1389 OE1 GLN A 171 13165 12415 11918 -1172 1631 254 O ATOM 1390 NE2 GLN A 171 -45.555 -11.182 26.357 1.00104.61 N ANISOU 1390 NE2 GLN A 171 14217 12927 12604 -1456 1686 344 N ATOM 1391 N LEU A 172 -45.127 -5.922 22.104 1.00 67.22 N ANISOU 1391 N LEU A 172 8678 8548 8314 -323 1050 204 N ATOM 1392 CA LEU A 172 -44.930 -4.506 21.821 1.00 58.81 C ANISOU 1392 CA LEU A 172 7534 7488 7324 -108 945 234 C ATOM 1393 C LEU A 172 -45.693 -4.075 20.576 1.00 54.75 C ANISOU 1393 C LEU A 172 6880 7072 6853 18 800 171 C ATOM 1394 O LEU A 172 -46.410 -3.075 20.591 1.00 52.10 O ANISOU 1394 O LEU A 172 6377 6810 6609 147 727 83 O ATOM 1395 CB LEU A 172 -43.442 -4.196 21.650 1.00 45.04 C ANISOU 1395 CB LEU A 172 5966 5590 5559 -9 910 425 C ATOM 1396 CG LEU A 172 -43.101 -2.772 21.207 1.00 36.21 C ANISOU 1396 CG LEU A 172 4816 4427 4515 177 805 491 C ATOM 1397 CD1 LEU A 172 -43.438 -1.767 22.298 1.00 36.70 C ANISOU 1397 CD1 LEU A 172 4797 4491 4658 211 823 402 C ATOM 1398 CD2 LEU A 172 -41.639 -2.669 20.807 1.00 44.67 C ANISOU 1398 CD2 LEU A 172 6033 5376 5562 221 794 673 C ATOM 1399 N ILE A 173 -45.530 -4.839 19.501 1.00 59.11 N ANISOU 1399 N ILE A 173 7511 7617 7330 -4 747 208 N ATOM 1400 CA ILE A 173 -46.154 -4.525 18.220 1.00 47.39 C ANISOU 1400 CA ILE A 173 5939 6233 5834 113 580 167 C ATOM 1401 C ILE A 173 -47.676 -4.620 18.288 1.00 57.78 C ANISOU 1401 C ILE A 173 6989 7742 7221 59 535 -54 C ATOM 1402 O ILE A 173 -48.380 -3.719 17.832 1.00 63.31 O ANISOU 1402 O ILE A 173 7527 8540 7989 233 380 -112 O ATOM 1403 CB ILE A 173 -45.634 -5.455 17.109 1.00 43.72 C ANISOU 1403 CB ILE A 173 5638 5735 5239 75 553 220 C ATOM 1404 CG1 ILE A 173 -44.132 -5.244 16.907 1.00 56.14 C ANISOU 1404 CG1 ILE A 173 7417 7158 6757 157 601 420 C ATOM 1405 CG2 ILE A 173 -46.384 -5.210 15.809 1.00 41.72 C ANISOU 1405 CG2 ILE A 173 5307 5616 4929 175 363 159 C ATOM 1406 CD1 ILE A 173 -43.480 -6.279 16.022 1.00 69.03 C ANISOU 1406 CD1 ILE A 173 9213 8749 8266 120 631 445 C ATOM 1407 N LYS A 174 -48.176 -5.710 18.864 1.00 60.49 N ANISOU 1407 N LYS A 174 7286 8137 7560 -185 666 -175 N ATOM 1408 CA LYS A 174 -49.615 -5.920 18.998 1.00 46.23 C ANISOU 1408 CA LYS A 174 5189 6543 5835 -296 662 -407 C ATOM 1409 C LYS A 174 -50.280 -4.809 19.805 1.00 56.24 C ANISOU 1409 C LYS A 174 6217 7920 7233 -175 682 -513 C ATOM 1410 O LYS A 174 -51.398 -4.393 19.500 1.00 82.55 O ANISOU 1410 O LYS A 174 9255 11444 10668 -92 575 -690 O ATOM 1411 CB LYS A 174 -49.903 -7.275 19.648 1.00 47.50 C ANISOU 1411 CB LYS A 174 5386 6698 5963 -631 850 -489 C ATOM 1412 CG LYS A 174 -49.628 -8.473 18.752 1.00 58.62 C ANISOU 1412 CG LYS A 174 6975 8020 7280 -762 809 -474 C ATOM 1413 CD LYS A 174 -49.959 -9.778 19.462 1.00 63.65 C ANISOU 1413 CD LYS A 174 7679 8601 7903 -1109 995 -546 C ATOM 1414 CE LYS A 174 -49.813 -10.972 18.532 1.00 64.62 C ANISOU 1414 CE LYS A 174 7976 8616 7959 -1239 940 -579 C ATOM 1415 NZ LYS A 174 -50.089 -12.259 19.230 1.00 56.38 N ANISOU 1415 NZ LYS A 174 7054 7456 6913 -1590 1118 -625 N ATOM 1416 N GLU A 175 -49.589 -4.330 20.834 1.00 64.71 N ANISOU 1416 N GLU A 175 7407 8874 8304 -151 809 -425 N ATOM 1417 CA GLU A 175 -50.122 -3.272 21.684 1.00 71.68 C ANISOU 1417 CA GLU A 175 8100 9835 9299 -32 851 -548 C ATOM 1418 C GLU A 175 -49.978 -1.903 21.023 1.00 77.06 C ANISOU 1418 C GLU A 175 8763 10448 10069 302 639 -489 C ATOM 1419 O GLU A 175 -50.834 -1.034 21.187 1.00 74.41 O ANISOU 1419 O GLU A 175 8190 10214 9869 473 577 -649 O ATOM 1420 CB GLU A 175 -49.428 -3.282 23.047 1.00 63.13 C ANISOU 1420 CB GLU A 175 7180 8653 8152 -145 1051 -491 C ATOM 1421 CG GLU A 175 -50.055 -2.351 24.071 1.00 72.98 C ANISOU 1421 CG GLU A 175 8240 10004 9486 -69 1144 -670 C ATOM 1422 CD GLU A 175 -49.547 -2.604 25.476 1.00 78.53 C ANISOU 1422 CD GLU A 175 9106 10664 10069 -246 1358 -647 C ATOM 1423 OE1 GLU A 175 -48.814 -3.595 25.675 1.00 89.12 O ANISOU 1423 OE1 GLU A 175 10687 11901 11273 -434 1424 -489 O ATOM 1424 OE2 GLU A 175 -49.882 -1.812 26.382 1.00 76.16 O ANISOU 1424 OE2 GLU A 175 8704 10430 9803 -183 1449 -794 O ATOM 1425 N CYS A 176 -48.894 -1.713 20.277 1.00 88.71 N ANISOU 1425 N CYS A 176 10492 11744 11470 394 536 -263 N ATOM 1426 CA CYS A 176 -48.674 -0.460 19.561 1.00 92.36 C ANISOU 1426 CA CYS A 176 11001 12102 11989 673 340 -160 C ATOM 1427 C CYS A 176 -49.595 -0.341 18.352 1.00 83.57 C ANISOU 1427 C CYS A 176 9739 11121 10892 819 112 -219 C ATOM 1428 O CYS A 176 -49.889 0.761 17.893 1.00 87.07 O ANISOU 1428 O CYS A 176 10146 11520 11416 1079 -76 -194 O ATOM 1429 CB CYS A 176 -47.215 -0.338 19.113 1.00 90.94 C ANISOU 1429 CB CYS A 176 11128 11715 11710 682 333 103 C ATOM 1430 SG CYS A 176 -46.171 0.638 20.216 1.00111.42 S ANISOU 1430 SG CYS A 176 13863 14103 14369 714 426 193 S ATOM 1431 N LYS A 177 -50.041 -1.481 17.836 1.00 64.94 N ANISOU 1431 N LYS A 177 7313 8910 8452 654 110 -296 N ATOM 1432 CA LYS A 177 -50.923 -1.498 16.676 1.00 78.21 C ANISOU 1432 CA LYS A 177 8847 10748 10120 764 -130 -374 C ATOM 1433 C LYS A 177 -52.362 -1.175 17.067 1.00 89.58 C ANISOU 1433 C LYS A 177 9885 12410 11740 841 -192 -644 C ATOM 1434 O LYS A 177 -53.039 -0.402 16.390 1.00 97.71 O ANISOU 1434 O LYS A 177 10769 13514 12840 1102 -447 -688 O ATOM 1435 CB LYS A 177 -50.854 -2.859 15.979 1.00 81.13 C ANISOU 1435 CB LYS A 177 9298 11189 10339 540 -115 -391 C ATOM 1436 CG LYS A 177 -51.731 -2.983 14.746 1.00 89.07 C ANISOU 1436 CG LYS A 177 10169 12379 11295 624 -383 -489 C ATOM 1437 CD LYS A 177 -51.462 -4.291 14.018 1.00 93.88 C ANISOU 1437 CD LYS A 177 10930 13008 11732 403 -361 -503 C ATOM 1438 CE LYS A 177 -51.642 -5.485 14.942 1.00 97.43 C ANISOU 1438 CE LYS A 177 11317 13469 12234 71 -113 -644 C ATOM 1439 NZ LYS A 177 -51.318 -6.769 14.261 1.00105.78 N ANISOU 1439 NZ LYS A 177 12563 14485 13143 -133 -91 -665 N ATOM 1440 N SER A 178 -52.821 -1.766 18.166 1.00 94.61 N ANISOU 1440 N SER A 178 10343 13158 12446 617 44 -825 N ATOM 1441 CA SER A 178 -54.187 -1.560 18.634 1.00 98.08 C ANISOU 1441 CA SER A 178 10353 13850 13061 646 49 -1117 C ATOM 1442 C SER A 178 -54.381 -0.178 19.252 1.00100.41 C ANISOU 1442 C SER A 178 10539 14095 13518 943 24 -1176 C ATOM 1443 O SER A 178 -55.314 0.544 18.901 1.00118.66 O ANISOU 1443 O SER A 178 12567 16536 15983 1206 -175 -1328 O ATOM 1444 CB SER A 178 -54.570 -2.641 19.648 1.00102.47 C ANISOU 1444 CB SER A 178 10785 14538 13610 268 355 -1277 C ATOM 1445 OG SER A 178 -53.735 -2.586 20.792 1.00 96.15 O ANISOU 1445 OG SER A 178 10208 13572 12751 168 602 -1173 O ATOM 1446 N ARG A 179 -53.492 0.184 20.172 1.00 88.15 N ANISOU 1446 N ARG A 179 9213 12346 11935 913 208 -1069 N ATOM 1447 CA ARG A 179 -53.609 1.442 20.901 1.00 87.97 C ANISOU 1447 CA ARG A 179 9122 12244 12059 1159 220 -1155 C ATOM 1448 C ARG A 179 -53.048 2.617 20.106 1.00 84.94 C ANISOU 1448 C ARG A 179 8953 11609 11711 1487 -43 -954 C ATOM 1449 O ARG A 179 -53.243 3.775 20.475 1.00 79.70 O ANISOU 1449 O ARG A 179 8242 10840 11200 1748 -105 -1029 O ATOM 1450 CB ARG A 179 -52.892 1.341 22.250 1.00 94.24 C ANISOU 1450 CB ARG A 179 10083 12940 12783 968 512 -1141 C ATOM 1451 CG ARG A 179 -53.259 0.110 23.071 1.00101.83 C ANISOU 1451 CG ARG A 179 10941 14098 13654 599 793 -1267 C ATOM 1452 CD ARG A 179 -54.364 0.392 24.082 1.00107.14 C ANISOU 1452 CD ARG A 179 11260 15007 14441 590 979 -1590 C ATOM 1453 NE ARG A 179 -55.632 0.751 23.451 1.00118.31 N ANISOU 1453 NE ARG A 179 12258 16646 16050 792 815 -1818 N ATOM 1454 CZ ARG A 179 -56.103 1.991 23.372 1.00119.81 C ANISOU 1454 CZ ARG A 179 12271 16822 16429 1171 660 -1951 C ATOM 1455 NH1 ARG A 179 -55.413 2.999 23.886 1.00110.99 N ANISOU 1455 NH1 ARG A 179 11377 15461 15333 1360 664 -1886 N ATOM 1456 NH2 ARG A 179 -57.266 2.222 22.779 1.00124.03 N ANISOU 1456 NH2 ARG A 179 12404 17578 17143 1366 484 -2160 N ATOM 1457 N GLY A 180 -52.354 2.314 19.014 1.00 93.68 N ANISOU 1457 N GLY A 180 10313 12609 12672 1466 -186 -705 N ATOM 1458 CA GLY A 180 -51.692 3.339 18.229 1.00105.84 C ANISOU 1458 CA GLY A 180 12118 13897 14201 1709 -397 -466 C ATOM 1459 C GLY A 180 -50.420 3.797 18.916 1.00120.54 C ANISOU 1459 C GLY A 180 14275 15492 16035 1638 -241 -301 C ATOM 1460 O GLY A 180 -49.857 3.064 19.731 1.00124.13 O ANISOU 1460 O GLY A 180 14788 15963 16413 1381 -5 -310 O ATOM 1461 N LYS A 181 -49.969 5.004 18.582 1.00132.12 N ANISOU 1461 N LYS A 181 15934 16703 17562 1858 -389 -147 N ATOM 1462 CA LYS A 181 -48.806 5.619 19.223 1.00134.73 C ANISOU 1462 CA LYS A 181 16519 16770 17904 1797 -272 -15 C ATOM 1463 C LYS A 181 -47.551 4.755 19.112 1.00126.45 C ANISOU 1463 C LYS A 181 15688 15689 16670 1519 -123 184 C ATOM 1464 O LYS A 181 -47.074 4.206 20.105 1.00130.90 O ANISOU 1464 O LYS A 181 16254 16282 17201 1319 81 126 O ATOM 1465 CB LYS A 181 -49.106 5.909 20.695 1.00141.65 C ANISOU 1465 CB LYS A 181 17247 17666 18905 1778 -98 -265 C ATOM 1466 CG LYS A 181 -50.352 6.746 20.923 1.00147.17 C ANISOU 1466 CG LYS A 181 17691 18415 19813 2071 -209 -517 C ATOM 1467 CD LYS A 181 -50.661 6.870 22.406 1.00145.02 C ANISOU 1467 CD LYS A 181 17263 18218 19618 2015 17 -799 C ATOM 1468 CE LYS A 181 -50.859 5.503 23.040 1.00138.19 C ANISOU 1468 CE LYS A 181 16252 17643 18612 1694 264 -907 C ATOM 1469 NZ LYS A 181 -51.145 5.602 24.497 1.00137.74 N ANISOU 1469 NZ LYS A 181 16079 17681 18576 1613 506 -1165 N ATOM 1470 N GLU A 182 -47.020 4.640 17.899 1.00110.71 N ANISOU 1470 N GLU A 182 13878 13641 14546 1523 -229 415 N ATOM 1471 CA GLU A 182 -45.845 3.813 17.652 1.00 94.00 C ANISOU 1471 CA GLU A 182 11940 11511 12266 1298 -92 584 C ATOM 1472 C GLU A 182 -44.557 4.471 18.141 1.00 85.71 C ANISOU 1472 C GLU A 182 11087 10232 11249 1227 2 733 C ATOM 1473 O GLU A 182 -44.279 5.627 17.823 1.00 90.46 O ANISOU 1473 O GLU A 182 11827 10624 11918 1348 -102 858 O ATOM 1474 CB GLU A 182 -45.724 3.498 16.160 1.00 99.47 C ANISOU 1474 CB GLU A 182 12757 12249 12787 1327 -216 752 C ATOM 1475 CG GLU A 182 -46.907 2.744 15.578 1.00111.91 C ANISOU 1475 CG GLU A 182 14145 14067 14308 1363 -332 599 C ATOM 1476 CD GLU A 182 -46.786 2.547 14.080 1.00127.27 C ANISOU 1476 CD GLU A 182 16248 16057 16050 1407 -481 757 C ATOM 1477 OE1 GLU A 182 -45.914 3.194 13.463 1.00136.57 O ANISOU 1477 OE1 GLU A 182 17680 17071 17140 1444 -502 998 O ATOM 1478 OE2 GLU A 182 -47.562 1.745 13.519 1.00126.87 O ANISOU 1478 OE2 GLU A 182 16074 16215 15916 1385 -570 633 O ATOM 1479 N GLY A 183 -43.777 3.726 18.919 1.00 77.70 N ANISOU 1479 N GLY A 183 10085 9247 10189 1026 183 719 N ATOM 1480 CA GLY A 183 -42.444 4.156 19.305 1.00 71.80 C ANISOU 1480 CA GLY A 183 9492 8329 9459 927 262 854 C ATOM 1481 C GLY A 183 -42.335 4.940 20.600 1.00 76.84 C ANISOU 1481 C GLY A 183 10110 8852 10233 925 299 733 C ATOM 1482 O GLY A 183 -41.298 5.544 20.873 1.00 95.03 O ANISOU 1482 O GLY A 183 12534 10991 12580 855 321 831 O ATOM 1483 N GLU A 184 -43.396 4.937 21.399 1.00 69.89 N ANISOU 1483 N GLU A 184 9070 8070 9415 988 313 503 N ATOM 1484 CA GLU A 184 -43.377 5.634 22.682 1.00 73.60 C ANISOU 1484 CA GLU A 184 9525 8459 9982 989 365 343 C ATOM 1485 C GLU A 184 -42.701 4.796 23.765 1.00 70.71 C ANISOU 1485 C GLU A 184 9174 8182 9509 775 518 305 C ATOM 1486 O GLU A 184 -42.279 5.318 24.796 1.00 75.14 O ANISOU 1486 O GLU A 184 9785 8666 10101 729 554 220 O ATOM 1487 CB GLU A 184 -44.797 5.998 23.117 1.00 88.72 C ANISOU 1487 CB GLU A 184 11246 10468 11997 1153 345 86 C ATOM 1488 CG GLU A 184 -45.466 7.046 22.245 1.00 97.81 C ANISOU 1488 CG GLU A 184 12389 11487 13287 1424 149 102 C ATOM 1489 CD GLU A 184 -46.846 7.423 22.747 1.00110.57 C ANISOU 1489 CD GLU A 184 13763 13213 15035 1619 130 -190 C ATOM 1490 OE1 GLU A 184 -47.377 8.465 22.308 1.00120.56 O ANISOU 1490 OE1 GLU A 184 15025 14326 16454 1888 -44 -217 O ATOM 1491 OE2 GLU A 184 -47.402 6.674 23.577 1.00116.70 O ANISOU 1491 OE2 GLU A 184 14353 14226 15762 1506 293 -393 O ATOM 1492 N PHE A 185 -42.605 3.494 23.519 1.00 59.28 N ANISOU 1492 N PHE A 185 7706 6886 7930 652 588 365 N ATOM 1493 CA PHE A 185 -42.090 2.550 24.507 1.00 48.01 C ANISOU 1493 CA PHE A 185 6313 5540 6387 472 710 345 C ATOM 1494 C PHE A 185 -40.598 2.266 24.338 1.00 48.52 C ANISOU 1494 C PHE A 185 6509 5516 6408 383 702 538 C ATOM 1495 O PHE A 185 -40.052 1.379 24.995 1.00 66.18 O ANISOU 1495 O PHE A 185 8791 7806 8547 263 765 560 O ATOM 1496 CB PHE A 185 -42.891 1.252 24.449 1.00 46.44 C ANISOU 1496 CB PHE A 185 6030 5527 6089 382 795 283 C ATOM 1497 CG PHE A 185 -44.371 1.460 24.577 1.00 63.18 C ANISOU 1497 CG PHE A 185 7957 7780 8266 450 815 73 C ATOM 1498 CD1 PHE A 185 -44.914 1.955 25.751 1.00 62.93 C ANISOU 1498 CD1 PHE A 185 7850 7803 8258 449 901 -126 C ATOM 1499 CD2 PHE A 185 -45.219 1.175 23.521 1.00 66.12 C ANISOU 1499 CD2 PHE A 185 8209 8247 8668 519 744 53 C ATOM 1500 CE1 PHE A 185 -46.276 2.157 25.870 1.00 67.17 C ANISOU 1500 CE1 PHE A 185 8162 8492 8869 524 939 -348 C ATOM 1501 CE2 PHE A 185 -46.583 1.373 23.635 1.00 46.85 C ANISOU 1501 CE2 PHE A 185 5536 5958 6305 591 748 -162 C ATOM 1502 CZ PHE A 185 -47.111 1.864 24.811 1.00 53.15 C ANISOU 1502 CZ PHE A 185 6229 6815 7149 598 856 -365 C ATOM 1503 N SER A 186 -39.952 3.009 23.443 1.00 48.20 N ANISOU 1503 N SER A 186 6529 5345 6441 443 626 681 N ATOM 1504 CA SER A 186 -38.523 2.852 23.170 1.00 53.11 C ANISOU 1504 CA SER A 186 7225 5905 7049 359 634 849 C ATOM 1505 C SER A 186 -37.649 2.961 24.422 1.00 66.56 C ANISOU 1505 C SER A 186 8950 7581 8759 256 644 806 C ATOM 1506 O SER A 186 -36.540 2.427 24.457 1.00 65.03 O ANISOU 1506 O SER A 186 8767 7404 8536 182 656 904 O ATOM 1507 CB SER A 186 -38.068 3.894 22.146 1.00 63.30 C ANISOU 1507 CB SER A 186 8580 7048 8421 408 574 993 C ATOM 1508 OG SER A 186 -38.811 3.794 20.944 1.00 79.34 O ANISOU 1508 OG SER A 186 10621 9116 10409 510 535 1051 O ATOM 1509 N THR A 187 -38.150 3.654 25.441 1.00 62.01 N ANISOU 1509 N THR A 187 8372 6973 8217 266 629 644 N ATOM 1510 CA THR A 187 -37.407 3.857 26.682 1.00 52.80 C ANISOU 1510 CA THR A 187 7243 5790 7028 169 613 575 C ATOM 1511 C THR A 187 -37.091 2.545 27.399 1.00 47.34 C ANISOU 1511 C THR A 187 6570 5240 6176 81 654 591 C ATOM 1512 O THR A 187 -36.093 2.444 28.112 1.00 62.23 O ANISOU 1512 O THR A 187 8490 7127 8027 7 602 614 O ATOM 1513 CB THR A 187 -38.179 4.773 27.650 1.00 70.29 C ANISOU 1513 CB THR A 187 9467 7965 9275 207 610 355 C ATOM 1514 OG1 THR A 187 -39.447 4.183 27.961 1.00 85.85 O ANISOU 1514 OG1 THR A 187 11374 10087 11158 244 701 223 O ATOM 1515 CG2 THR A 187 -38.401 6.141 27.026 1.00 80.99 C ANISOU 1515 CG2 THR A 187 10842 9119 10812 315 539 343 C ATOM 1516 N CYS A 188 -37.946 1.545 27.210 1.00 48.88 N ANISOU 1516 N CYS A 188 6749 5544 6277 88 732 579 N ATOM 1517 CA CYS A 188 -37.762 0.243 27.843 1.00 58.60 C ANISOU 1517 CA CYS A 188 8045 6867 7354 1 774 613 C ATOM 1518 C CYS A 188 -36.569 -0.496 27.246 1.00 61.37 C ANISOU 1518 C CYS A 188 8416 7186 7714 8 729 787 C ATOM 1519 O CYS A 188 -35.949 -1.337 27.896 1.00 72.66 O ANISOU 1519 O CYS A 188 9917 8638 9051 -33 702 840 O ATOM 1520 CB CYS A 188 -39.027 -0.605 27.694 1.00 58.55 C ANISOU 1520 CB CYS A 188 8017 6958 7270 -26 880 551 C ATOM 1521 SG CYS A 188 -40.559 0.255 28.123 1.00 88.02 S ANISOU 1521 SG CYS A 188 11637 10771 11037 5 955 315 S ATOM 1522 N PHE A 189 -36.268 -0.180 25.994 1.00 63.71 N ANISOU 1522 N PHE A 189 8655 7436 8116 71 721 872 N ATOM 1523 CA PHE A 189 -35.211 -0.849 25.246 1.00 58.76 C ANISOU 1523 CA PHE A 189 8016 6805 7507 93 716 1007 C ATOM 1524 C PHE A 189 -33.887 -0.087 25.288 1.00 54.37 C ANISOU 1524 C PHE A 189 7398 6204 7054 74 655 1067 C ATOM 1525 O PHE A 189 -32.946 -0.430 24.571 1.00 57.68 O ANISOU 1525 O PHE A 189 7759 6638 7516 95 672 1162 O ATOM 1526 CB PHE A 189 -35.666 -1.073 23.807 1.00 47.48 C ANISOU 1526 CB PHE A 189 6569 5385 6085 152 770 1055 C ATOM 1527 CG PHE A 189 -36.956 -1.833 23.705 1.00 43.36 C ANISOU 1527 CG PHE A 189 6074 4920 5481 146 815 976 C ATOM 1528 CD1 PHE A 189 -36.976 -3.209 23.858 1.00 50.57 C ANISOU 1528 CD1 PHE A 189 7054 5854 6308 110 854 982 C ATOM 1529 CD2 PHE A 189 -38.151 -1.171 23.479 1.00 54.61 C ANISOU 1529 CD2 PHE A 189 7450 6368 6930 175 810 886 C ATOM 1530 CE1 PHE A 189 -38.163 -3.912 23.777 1.00 59.60 C ANISOU 1530 CE1 PHE A 189 8215 7045 7387 58 905 900 C ATOM 1531 CE2 PHE A 189 -39.340 -1.868 23.396 1.00 57.47 C ANISOU 1531 CE2 PHE A 189 7788 6813 7235 147 852 790 C ATOM 1532 CZ PHE A 189 -39.347 -3.241 23.544 1.00 51.21 C ANISOU 1532 CZ PHE A 189 7061 6044 6353 66 908 796 C ATOM 1533 N THR A 190 -33.835 0.955 26.116 1.00 55.16 N ANISOU 1533 N THR A 190 7500 6258 7202 23 595 989 N ATOM 1534 CA THR A 190 -32.666 1.828 26.243 1.00 59.07 C ANISOU 1534 CA THR A 190 7929 6699 7816 -40 528 1016 C ATOM 1535 C THR A 190 -31.348 1.067 26.419 1.00 57.21 C ANISOU 1535 C THR A 190 7609 6541 7587 -50 480 1085 C ATOM 1536 O THR A 190 -30.302 1.510 25.941 1.00 43.44 O ANISOU 1536 O THR A 190 5748 4793 5965 -96 474 1143 O ATOM 1537 CB THR A 190 -32.832 2.797 27.437 1.00 58.62 C ANISOU 1537 CB THR A 190 7915 6587 7771 -103 449 873 C ATOM 1538 OG1 THR A 190 -34.073 3.503 27.317 1.00 60.57 O ANISOU 1538 OG1 THR A 190 8219 6762 8034 -54 491 781 O ATOM 1539 CG2 THR A 190 -31.689 3.802 27.487 1.00 57.07 C ANISOU 1539 CG2 THR A 190 7651 6312 7721 -204 374 883 C ATOM 1540 N GLU A 191 -31.403 -0.074 27.100 1.00 58.20 N ANISOU 1540 N GLU A 191 7790 6734 7589 -7 445 1079 N ATOM 1541 CA GLU A 191 -30.224 -0.918 27.278 1.00 60.93 C ANISOU 1541 CA GLU A 191 8063 7142 7947 40 370 1142 C ATOM 1542 C GLU A 191 -29.611 -1.328 25.942 1.00 54.93 C ANISOU 1542 C GLU A 191 7187 6405 7280 106 465 1229 C ATOM 1543 O GLU A 191 -28.390 -1.384 25.800 1.00 67.27 O ANISOU 1543 O GLU A 191 8589 8026 8946 123 428 1257 O ATOM 1544 CB GLU A 191 -30.573 -2.167 28.087 1.00 79.94 C ANISOU 1544 CB GLU A 191 10615 9569 10189 94 324 1152 C ATOM 1545 CG GLU A 191 -30.749 -1.925 29.573 1.00 89.27 C ANISOU 1545 CG GLU A 191 11908 10773 11239 26 211 1081 C ATOM 1546 CD GLU A 191 -31.006 -3.207 30.337 1.00 93.32 C ANISOU 1546 CD GLU A 191 12604 11291 11564 60 171 1134 C ATOM 1547 OE1 GLU A 191 -31.715 -4.086 29.804 1.00 97.14 O ANISOU 1547 OE1 GLU A 191 13175 11732 12003 86 284 1178 O ATOM 1548 OE2 GLU A 191 -30.492 -3.340 31.468 1.00 91.46 O ANISOU 1548 OE2 GLU A 191 12442 11093 11216 50 15 1137 O ATOM 1549 N LEU A 192 -30.468 -1.615 24.968 1.00 50.94 N ANISOU 1549 N LEU A 192 6750 5875 6731 142 589 1252 N ATOM 1550 CA LEU A 192 -30.014 -2.029 23.646 1.00 48.73 C ANISOU 1550 CA LEU A 192 6397 5629 6489 202 699 1315 C ATOM 1551 C LEU A 192 -29.487 -0.837 22.851 1.00 48.36 C ANISOU 1551 C LEU A 192 6245 5582 6547 118 764 1363 C ATOM 1552 O LEU A 192 -28.591 -0.981 22.020 1.00 50.81 O ANISOU 1552 O LEU A 192 6434 5959 6912 128 853 1412 O ATOM 1553 CB LEU A 192 -31.149 -2.711 22.879 1.00 50.87 C ANISOU 1553 CB LEU A 192 6795 5882 6653 251 785 1308 C ATOM 1554 CG LEU A 192 -31.997 -3.731 23.641 1.00 49.52 C ANISOU 1554 CG LEU A 192 6764 5680 6370 269 750 1261 C ATOM 1555 CD1 LEU A 192 -33.101 -4.275 22.752 1.00 62.05 C ANISOU 1555 CD1 LEU A 192 8436 7262 7879 279 834 1233 C ATOM 1556 CD2 LEU A 192 -31.136 -4.859 24.170 1.00 63.74 C ANISOU 1556 CD2 LEU A 192 8580 7472 8167 350 688 1286 C ATOM 1557 N GLN A 193 -30.052 0.338 23.109 1.00 48.04 N ANISOU 1557 N GLN A 193 6261 5457 6535 30 732 1346 N ATOM 1558 CA GLN A 193 -29.627 1.561 22.437 1.00 41.99 C ANISOU 1558 CA GLN A 193 5453 4634 5870 -75 782 1412 C ATOM 1559 C GLN A 193 -28.213 1.949 22.850 1.00 44.89 C ANISOU 1559 C GLN A 193 5639 5043 6373 -182 748 1410 C ATOM 1560 O GLN A 193 -27.397 2.336 22.014 1.00 62.10 O ANISOU 1560 O GLN A 193 7712 7255 8630 -267 853 1486 O ATOM 1561 CB GLN A 193 -30.597 2.705 22.739 1.00 46.36 C ANISOU 1561 CB GLN A 193 6132 5043 6442 -113 726 1375 C ATOM 1562 CG GLN A 193 -31.993 2.502 22.172 1.00 53.03 C ANISOU 1562 CG GLN A 193 7101 5865 7182 -8 751 1371 C ATOM 1563 CD GLN A 193 -32.959 3.591 22.595 1.00 61.86 C ANISOU 1563 CD GLN A 193 8310 6849 8346 2 681 1300 C ATOM 1564 OE1 GLN A 193 -32.667 4.383 23.491 1.00 58.84 O ANISOU 1564 OE1 GLN A 193 7924 6381 8050 -69 614 1227 O ATOM 1565 NE2 GLN A 193 -34.119 3.636 21.950 1.00 70.89 N ANISOU 1565 NE2 GLN A 193 9524 7976 9435 102 683 1301 N ATOM 1566 N ARG A 194 -27.930 1.842 24.144 1.00 56.32 N ANISOU 1566 N ARG A 194 7050 6510 7840 -191 603 1318 N ATOM 1567 CA ARG A 194 -26.603 2.145 24.665 1.00 55.46 C ANISOU 1567 CA ARG A 194 6741 6467 7863 -287 522 1287 C ATOM 1568 C ARG A 194 -25.586 1.111 24.198 1.00 48.26 C ANISOU 1568 C ARG A 194 5634 5715 6989 -193 570 1320 C ATOM 1569 O ARG A 194 -24.493 1.462 23.757 1.00 44.49 O ANISOU 1569 O ARG A 194 4937 5320 6649 -286 629 1336 O ATOM 1570 CB ARG A 194 -26.623 2.209 26.192 1.00 54.51 C ANISOU 1570 CB ARG A 194 6658 6345 7706 -300 324 1173 C ATOM 1571 CG ARG A 194 -27.297 3.448 26.752 1.00 74.37 C ANISOU 1571 CG ARG A 194 9312 8713 10234 -414 275 1090 C ATOM 1572 CD ARG A 194 -26.612 4.714 26.261 1.00 92.76 C ANISOU 1572 CD ARG A 194 11551 10947 12746 -602 311 1110 C ATOM 1573 NE ARG A 194 -25.170 4.679 26.486 1.00108.64 N ANISOU 1573 NE ARG A 194 13309 13085 14884 -706 243 1091 N ATOM 1574 CZ ARG A 194 -24.576 5.080 27.605 1.00115.06 C ANISOU 1574 CZ ARG A 194 14048 13925 15746 -805 58 964 C ATOM 1575 NH1 ARG A 194 -25.300 5.551 28.611 1.00118.17 N ANISOU 1575 NH1 ARG A 194 14629 14220 16051 -816 -57 841 N ATOM 1576 NH2 ARG A 194 -23.257 5.012 27.719 1.00115.78 N ANISOU 1576 NH2 ARG A 194 13861 14159 15971 -893 -14 939 N ATOM 1577 N ASP A 195 -25.960 -0.161 24.292 1.00 48.17 N ANISOU 1577 N ASP A 195 5699 5739 6864 -13 553 1318 N ATOM 1578 CA ASP A 195 -25.092 -1.260 23.880 1.00 42.50 C ANISOU 1578 CA ASP A 195 4826 5139 6185 132 587 1326 C ATOM 1579 C ASP A 195 -24.749 -1.174 22.396 1.00 48.58 C ANISOU 1579 C ASP A 195 5496 5969 6992 112 816 1376 C ATOM 1580 O ASP A 195 -23.701 -1.649 21.962 1.00 69.06 O ANISOU 1580 O ASP A 195 7867 8695 9678 177 883 1356 O ATOM 1581 CB ASP A 195 -25.754 -2.605 24.190 1.00 41.37 C ANISOU 1581 CB ASP A 195 4862 4953 5905 313 536 1323 C ATOM 1582 CG ASP A 195 -24.908 -3.786 23.757 1.00 57.78 C ANISOU 1582 CG ASP A 195 6812 7106 8035 503 560 1314 C ATOM 1583 OD1 ASP A 195 -24.066 -4.243 24.558 1.00 76.06 O ANISOU 1583 OD1 ASP A 195 9009 9473 10417 604 391 1289 O ATOM 1584 OD2 ASP A 195 -25.085 -4.258 22.614 1.00 58.70 O ANISOU 1584 OD2 ASP A 195 6950 7230 8122 566 734 1321 O ATOM 1585 N PHE A 196 -25.640 -0.560 21.625 1.00 42.23 N ANISOU 1585 N PHE A 196 4859 5081 6107 31 933 1436 N ATOM 1586 CA PHE A 196 -25.432 -0.395 20.194 1.00 44.67 C ANISOU 1586 CA PHE A 196 5138 5446 6391 -8 1149 1504 C ATOM 1587 C PHE A 196 -24.304 0.598 19.918 1.00 61.13 C ANISOU 1587 C PHE A 196 7008 7595 8622 -202 1237 1540 C ATOM 1588 O PHE A 196 -23.467 0.370 19.045 1.00 74.32 O ANISOU 1588 O PHE A 196 8510 9408 10321 -216 1417 1553 O ATOM 1589 CB PHE A 196 -26.730 0.065 19.519 1.00 41.41 C ANISOU 1589 CB PHE A 196 4980 4917 5836 -34 1197 1571 C ATOM 1590 CG PHE A 196 -26.686 0.024 18.015 1.00 48.47 C ANISOU 1590 CG PHE A 196 5912 5878 6627 -44 1398 1647 C ATOM 1591 CD1 PHE A 196 -26.855 -1.172 17.335 1.00 54.71 C ANISOU 1591 CD1 PHE A 196 6739 6751 7299 109 1480 1600 C ATOM 1592 CD2 PHE A 196 -26.493 1.183 17.282 1.00 45.24 C ANISOU 1592 CD2 PHE A 196 5535 5433 6220 -215 1503 1766 C ATOM 1593 CE1 PHE A 196 -26.820 -1.212 15.953 1.00 46.05 C ANISOU 1593 CE1 PHE A 196 5696 5734 6066 97 1664 1652 C ATOM 1594 CE2 PHE A 196 -26.458 1.150 15.900 1.00 48.73 C ANISOU 1594 CE2 PHE A 196 6049 5951 6517 -235 1691 1851 C ATOM 1595 CZ PHE A 196 -26.622 -0.049 15.235 1.00 44.60 C ANISOU 1595 CZ PHE A 196 5549 5543 5853 -75 1772 1785 C ATOM 1596 N LEU A 197 -24.287 1.699 20.664 1.00 56.42 N ANISOU 1596 N LEU A 197 6421 6896 8121 -368 1125 1540 N ATOM 1597 CA LEU A 197 -23.299 2.753 20.446 1.00 58.05 C ANISOU 1597 CA LEU A 197 6451 7125 8481 -609 1204 1574 C ATOM 1598 C LEU A 197 -22.081 2.670 21.370 1.00 70.88 C ANISOU 1598 C LEU A 197 7761 8882 10288 -657 1080 1463 C ATOM 1599 O LEU A 197 -21.132 3.439 21.217 1.00 52.60 O ANISOU 1599 O LEU A 197 5237 6621 8128 -879 1148 1465 O ATOM 1600 CB LEU A 197 -23.963 4.122 20.609 1.00 48.05 C ANISOU 1600 CB LEU A 197 5397 5629 7232 -784 1154 1632 C ATOM 1601 CG LEU A 197 -25.227 4.355 19.779 1.00 52.66 C ANISOU 1601 CG LEU A 197 6285 6070 7652 -719 1218 1740 C ATOM 1602 CD1 LEU A 197 -25.860 5.691 20.129 1.00 57.22 C ANISOU 1602 CD1 LEU A 197 7060 6394 8285 -839 1123 1768 C ATOM 1603 CD2 LEU A 197 -24.913 4.280 18.294 1.00 62.56 C ANISOU 1603 CD2 LEU A 197 7544 7411 8816 -768 1457 1873 C ATOM 1604 N ARG A 198 -22.104 1.745 22.325 1.00 64.08 N ANISOU 1604 N ARG A 198 6870 8073 9405 -460 888 1371 N ATOM 1605 CA ARG A 198 -21.002 1.620 23.278 1.00 69.01 C ANISOU 1605 CA ARG A 198 7209 8830 10181 -467 709 1265 C ATOM 1606 C ARG A 198 -19.833 0.813 22.717 1.00 75.94 C ANISOU 1606 C ARG A 198 7743 9938 11171 -357 810 1225 C ATOM 1607 O ARG A 198 -18.670 1.132 22.969 1.00 91.82 O ANISOU 1607 O ARG A 198 9412 12103 13371 -465 767 1152 O ATOM 1608 CB ARG A 198 -21.490 0.989 24.585 1.00 82.16 C ANISOU 1608 CB ARG A 198 9019 10451 11748 -300 441 1202 C ATOM 1609 CG ARG A 198 -20.398 0.811 25.631 1.00 96.22 C ANISOU 1609 CG ARG A 198 10538 12375 13648 -276 198 1100 C ATOM 1610 CD ARG A 198 -20.967 0.617 27.029 1.00 96.57 C ANISOU 1610 CD ARG A 198 10798 12345 13548 -204 -72 1054 C ATOM 1611 NE ARG A 198 -21.927 -0.481 27.098 1.00 93.27 N ANISOU 1611 NE ARG A 198 10655 11848 12935 14 -67 1114 N ATOM 1612 CZ ARG A 198 -23.234 -0.319 27.277 1.00 92.31 C ANISOU 1612 CZ ARG A 198 10852 11577 12646 -13 -23 1140 C ATOM 1613 NH1 ARG A 198 -23.740 0.900 27.411 1.00 89.08 N ANISOU 1613 NH1 ARG A 198 10537 11067 12243 -206 5 1107 N ATOM 1614 NH2 ARG A 198 -24.035 -1.375 27.326 1.00 90.75 N ANISOU 1614 NH2 ARG A 198 10870 11323 12289 152 -8 1187 N ATOM 1615 N ASN A 199 -20.146 -0.224 21.948 1.00 73.34 N ANISOU 1615 N ASN A 199 7491 9639 10735 -143 944 1251 N ATOM 1616 CA ASN A 199 -19.129 -1.156 21.473 1.00 92.86 C ANISOU 1616 CA ASN A 199 9661 12316 13307 34 1032 1178 C ATOM 1617 C ASN A 199 -18.387 -0.650 20.241 1.00109.36 C ANISOU 1617 C ASN A 199 11520 14561 15473 -140 1349 1192 C ATOM 1618 O ASN A 199 -17.478 -1.312 19.737 1.00116.99 O ANISOU 1618 O ASN A 199 12187 15730 16533 -13 1476 1106 O ATOM 1619 CB ASN A 199 -19.764 -2.513 21.169 1.00 99.77 C ANISOU 1619 CB ASN A 199 10739 13132 14037 334 1047 1174 C ATOM 1620 CG ASN A 199 -20.761 -2.446 20.028 1.00110.57 C ANISOU 1620 CG ASN A 199 12386 14408 15218 287 1276 1255 C ATOM 1621 OD1 ASN A 199 -20.405 -2.640 18.866 1.00110.71 O ANISOU 1621 OD1 ASN A 199 12313 14541 15213 297 1527 1245 O ATOM 1622 ND2 ASN A 199 -22.017 -2.171 20.356 1.00115.78 N ANISOU 1622 ND2 ASN A 199 13378 14881 15733 241 1187 1321 N ATOM 1623 N ARG A 200 -18.778 0.524 19.759 1.00100.19 N ANISOU 1623 N ARG A 200 10506 13299 14264 -426 1484 1300 N ATOM 1624 CA ARG A 200 -18.157 1.118 18.582 1.00 82.57 C ANISOU 1624 CA ARG A 200 8124 11190 12060 -647 1805 1354 C ATOM 1625 C ARG A 200 -16.721 1.556 18.869 1.00 91.22 C ANISOU 1625 C ARG A 200 8747 12496 13417 -829 1828 1258 C ATOM 1626 O ARG A 200 -16.386 1.884 20.008 1.00 96.12 O ANISOU 1626 O ARG A 200 9237 13099 14187 -883 1565 1185 O ATOM 1627 CB ARG A 200 -18.987 2.307 18.093 1.00 74.12 C ANISOU 1627 CB ARG A 200 7387 9907 10870 -903 1895 1522 C ATOM 1628 CG ARG A 200 -20.423 1.952 17.748 1.00 69.32 C ANISOU 1628 CG ARG A 200 7199 9121 10017 -733 1864 1603 C ATOM 1629 CD ARG A 200 -20.481 0.826 16.727 1.00 69.36 C ANISOU 1629 CD ARG A 200 7218 9267 9871 -524 2053 1578 C ATOM 1630 NE ARG A 200 -21.853 0.444 16.407 1.00 65.99 N ANISOU 1630 NE ARG A 200 7164 8688 9220 -379 2001 1632 N ATOM 1631 CZ ARG A 200 -22.179 -0.525 15.557 1.00 65.23 C ANISOU 1631 CZ ARG A 200 7164 8663 8958 -200 2123 1598 C ATOM 1632 NH1 ARG A 200 -21.230 -1.213 14.938 1.00 75.51 N ANISOU 1632 NH1 ARG A 200 8229 10176 10285 -120 2319 1506 N ATOM 1633 NH2 ARG A 200 -23.453 -0.805 15.326 1.00 57.11 N ANISOU 1633 NH2 ARG A 200 6453 7503 7745 -101 2048 1634 N ATOM 1634 N PRO A 201 -15.864 1.549 17.832 1.00 94.32 N ANISOU 1634 N PRO A 201 8871 13112 13857 -933 2149 1243 N ATOM 1635 CA PRO A 201 -14.471 1.999 17.946 1.00 83.55 C ANISOU 1635 CA PRO A 201 7002 11988 12754 -1150 2230 1141 C ATOM 1636 C PRO A 201 -14.353 3.437 18.448 1.00 91.50 C ANISOU 1636 C PRO A 201 8032 12854 13882 -1561 2151 1206 C ATOM 1637 O PRO A 201 -15.283 4.226 18.282 1.00 90.98 O ANISOU 1637 O PRO A 201 8383 12512 13674 -1716 2158 1364 O ATOM 1638 CB PRO A 201 -13.949 1.882 16.512 1.00 73.33 C ANISOU 1638 CB PRO A 201 5561 10909 11393 -1241 2673 1161 C ATOM 1639 CG PRO A 201 -14.780 0.813 15.904 1.00 76.57 C ANISOU 1639 CG PRO A 201 6269 11269 11557 -900 2731 1173 C ATOM 1640 CD PRO A 201 -16.147 0.980 16.502 1.00 94.92 C ANISOU 1640 CD PRO A 201 9079 13259 13728 -830 2458 1290 C ATOM 1641 N THR A 202 -13.215 3.758 19.057 1.00101.80 N ANISOU 1641 N THR A 202 11142 14731 12807 -3440 -1719 3740 N ATOM 1642 CA THR A 202 -12.986 5.075 19.642 1.00 95.87 C ANISOU 1642 CA THR A 202 10541 13866 12020 -3727 -1961 3836 C ATOM 1643 C THR A 202 -13.115 6.197 18.614 1.00101.60 C ANISOU 1643 C THR A 202 11344 14606 12654 -3992 -1838 3919 C ATOM 1644 O THR A 202 -13.712 7.238 18.892 1.00104.25 O ANISOU 1644 O THR A 202 12002 14724 12884 -4140 -1961 3956 O ATOM 1645 CB THR A 202 -11.593 5.155 20.297 1.00 89.30 C ANISOU 1645 CB THR A 202 9379 13167 11382 -3857 -2180 3908 C ATOM 1646 OG1 THR A 202 -11.437 4.076 21.227 1.00 94.20 O ANISOU 1646 OG1 THR A 202 9931 13774 12086 -3600 -2321 3862 O ATOM 1647 CG2 THR A 202 -11.419 6.479 21.027 1.00 86.05 C ANISOU 1647 CG2 THR A 202 9163 12609 10924 -4161 -2455 3977 C ATOM 1648 N LYS A 203 -12.558 5.979 17.427 1.00104.81 N ANISOU 1648 N LYS A 203 11467 15255 13099 -4050 -1587 3947 N ATOM 1649 CA LYS A 203 -12.599 6.980 16.367 1.00108.42 C ANISOU 1649 CA LYS A 203 11999 15749 13445 -4316 -1453 4055 C ATOM 1650 C LYS A 203 -14.022 7.247 15.885 1.00104.59 C ANISOU 1650 C LYS A 203 11913 15081 12747 -4233 -1391 4037 C ATOM 1651 O LYS A 203 -14.361 8.375 15.525 1.00114.40 O ANISOU 1651 O LYS A 203 13380 16196 13891 -4443 -1435 4150 O ATOM 1652 CB LYS A 203 -11.721 6.550 15.190 1.00114.57 C ANISOU 1652 CB LYS A 203 12401 16850 14281 -4386 -1154 4069 C ATOM 1653 CG LYS A 203 -10.280 7.020 15.295 1.00121.66 C ANISOU 1653 CG LYS A 203 12928 17917 15381 -4654 -1197 4159 C ATOM 1654 CD LYS A 203 -10.201 8.539 15.266 1.00124.42 C ANISOU 1654 CD LYS A 203 13474 18133 15666 -5026 -1323 4318 C ATOM 1655 CE LYS A 203 -8.775 9.027 15.462 1.00126.89 C ANISOU 1655 CE LYS A 203 13408 18600 16206 -5319 -1387 4397 C ATOM 1656 NZ LYS A 203 -8.236 8.640 16.795 1.00114.15 N ANISOU 1656 NZ LYS A 203 11620 16955 14795 -5214 -1693 4335 N ATOM 1657 N LEU A 204 -14.853 6.210 15.882 1.00 92.86 N ANISOU 1657 N LEU A 204 10504 13568 11211 -3926 -1299 3898 N ATOM 1658 CA LEU A 204 -16.240 6.356 15.458 1.00 83.25 C ANISOU 1658 CA LEU A 204 9620 12186 9826 -3824 -1256 3861 C ATOM 1659 C LEU A 204 -17.059 7.093 16.513 1.00 87.75 C ANISOU 1659 C LEU A 204 10530 12428 10386 -3819 -1494 3855 C ATOM 1660 O LEU A 204 -17.863 7.965 16.187 1.00100.22 O ANISOU 1660 O LEU A 204 12372 13832 11876 -3895 -1536 3910 O ATOM 1661 CB LEU A 204 -16.864 4.991 15.163 1.00 80.21 C ANISOU 1661 CB LEU A 204 9192 11869 9416 -3517 -1081 3694 C ATOM 1662 CG LEU A 204 -18.326 5.015 14.707 1.00 79.18 C ANISOU 1662 CG LEU A 204 9359 11590 9138 -3397 -1044 3631 C ATOM 1663 CD1 LEU A 204 -18.503 5.954 13.524 1.00 68.73 C ANISOU 1663 CD1 LEU A 204 8141 10318 7656 -3607 -995 3768 C ATOM 1664 CD2 LEU A 204 -18.810 3.615 14.357 1.00 71.97 C ANISOU 1664 CD2 LEU A 204 8364 10763 8216 -3129 -857 3452 C ATOM 1665 N LYS A 205 -16.848 6.740 17.778 1.00 77.68 N ANISOU 1665 N LYS A 205 9252 11063 9201 -3728 -1649 3787 N ATOM 1666 CA LYS A 205 -17.567 7.376 18.877 1.00 68.54 C ANISOU 1666 CA LYS A 205 8422 9601 8018 -3731 -1847 3749 C ATOM 1667 C LYS A 205 -17.193 8.850 18.997 1.00 74.76 C ANISOU 1667 C LYS A 205 9325 10264 8816 -4042 -2005 3870 C ATOM 1668 O LYS A 205 -18.001 9.672 19.430 1.00 69.88 O ANISOU 1668 O LYS A 205 9021 9368 8163 -4077 -2105 3849 O ATOM 1669 CB LYS A 205 -17.290 6.652 20.196 1.00 68.27 C ANISOU 1669 CB LYS A 205 8372 9529 8037 -3599 -1981 3665 C ATOM 1670 CG LYS A 205 -17.761 5.208 20.217 1.00 66.46 C ANISOU 1670 CG LYS A 205 8084 9355 7814 -3288 -1834 3548 C ATOM 1671 CD LYS A 205 -17.708 4.623 21.620 1.00 66.29 C ANISOU 1671 CD LYS A 205 8157 9228 7804 -3167 -1989 3490 C ATOM 1672 CE LYS A 205 -16.297 4.642 22.184 1.00 76.41 C ANISOU 1672 CE LYS A 205 9194 10654 9186 -3289 -2187 3584 C ATOM 1673 NZ LYS A 205 -16.248 4.082 23.564 1.00 87.46 N ANISOU 1673 NZ LYS A 205 10722 11952 10558 -3179 -2377 3553 N ATOM 1674 N SER A 206 -15.964 9.177 18.610 1.00 91.88 N ANISOU 1674 N SER A 206 11230 12628 11054 -4270 -2011 3988 N ATOM 1675 CA SER A 206 -15.514 10.563 18.590 1.00103.78 C ANISOU 1675 CA SER A 206 12820 14027 12587 -4602 -2137 4116 C ATOM 1676 C SER A 206 -16.167 11.304 17.431 1.00 97.42 C ANISOU 1676 C SER A 206 12185 13143 11686 -4691 -2017 4225 C ATOM 1677 O SER A 206 -16.469 12.494 17.530 1.00 97.64 O ANISOU 1677 O SER A 206 12460 12925 11715 -4866 -2133 4300 O ATOM 1678 CB SER A 206 -13.990 10.637 18.481 1.00111.59 C ANISOU 1678 CB SER A 206 13435 15262 13702 -4834 -2158 4207 C ATOM 1679 OG SER A 206 -13.538 10.055 17.272 1.00120.25 O ANISOU 1679 OG SER A 206 14244 16648 14796 -4819 -1898 4254 O ATOM 1680 N LEU A 207 -16.379 10.590 16.330 1.00 94.08 N ANISOU 1680 N LEU A 207 11642 12923 11180 -4568 -1795 4232 N ATOM 1681 CA LEU A 207 -17.057 11.150 15.168 1.00 92.52 C ANISOU 1681 CA LEU A 207 11619 12681 10853 -4623 -1699 4340 C ATOM 1682 C LEU A 207 -18.519 11.439 15.489 1.00 81.37 C ANISOU 1682 C LEU A 207 10548 10958 9410 -4414 -1798 4243 C ATOM 1683 O LEU A 207 -19.063 12.462 15.076 1.00 76.64 O ANISOU 1683 O LEU A 207 10157 10169 8792 -4432 -1861 4263 O ATOM 1684 CB LEU A 207 -16.955 10.198 13.974 1.00 95.46 C ANISOU 1684 CB LEU A 207 11793 13363 11113 -4532 -1441 4330 C ATOM 1685 CG LEU A 207 -17.735 10.590 12.717 1.00 94.87 C ANISOU 1685 CG LEU A 207 11908 13275 10862 -4505 -1357 4374 C ATOM 1686 CD1 LEU A 207 -17.266 11.937 12.187 1.00107.87 C ANISOU 1686 CD1 LEU A 207 13645 14850 12490 -4726 -1406 4485 C ATOM 1687 CD2 LEU A 207 -17.610 9.515 11.648 1.00 81.84 C ANISOU 1687 CD2 LEU A 207 10075 11950 9071 -4452 -1095 4357 C ATOM 1688 N ILE A 208 -19.146 10.530 16.229 1.00 70.27 N ANISOU 1688 N ILE A 208 9172 9500 8027 -4166 -1801 4087 N ATOM 1689 CA ILE A 208 -20.536 10.696 16.636 1.00 68.36 C ANISOU 1689 CA ILE A 208 9214 8970 7789 -3979 -1866 3985 C ATOM 1690 C ILE A 208 -20.705 11.942 17.500 1.00 87.01 C ANISOU 1690 C ILE A 208 11818 11006 10235 -4104 -2054 3987 C ATOM 1691 O ILE A 208 -21.640 12.719 17.306 1.00 88.35 O ANISOU 1691 O ILE A 208 12198 10937 10432 -4031 -2100 3950 O ATOM 1692 CB ILE A 208 -21.051 9.462 17.405 1.00 65.92 C ANISOU 1692 CB ILE A 208 8876 8670 7502 -3691 -1809 3776 C ATOM 1693 CG1 ILE A 208 -21.057 8.233 16.495 1.00 65.06 C ANISOU 1693 CG1 ILE A 208 8555 8836 7328 -3532 -1609 3726 C ATOM 1694 CG2 ILE A 208 -22.448 9.712 17.950 1.00 64.37 C ANISOU 1694 CG2 ILE A 208 8956 8164 7338 -3528 -1857 3655 C ATOM 1695 CD1 ILE A 208 -21.562 6.975 17.166 1.00 62.93 C ANISOU 1695 CD1 ILE A 208 8260 8558 7093 -3260 -1537 3535 C ATOM 1696 N ARG A 209 -19.787 12.135 18.444 1.00 95.93 N ANISOU 1696 N ARG A 209 12897 12132 11419 -4267 -2167 3991 N ATOM 1697 CA ARG A 209 -19.818 13.306 19.315 1.00 94.58 C ANISOU 1697 CA ARG A 209 12953 11667 11317 -4404 -2341 3951 C ATOM 1698 C ARG A 209 -19.645 14.597 18.519 1.00 90.16 C ANISOU 1698 C ARG A 209 12449 11020 10786 -4550 -2368 4036 C ATOM 1699 O ARG A 209 -20.143 15.651 18.916 1.00 97.81 O ANISOU 1699 O ARG A 209 13660 11683 11822 -4573 -2468 3982 O ATOM 1700 CB ARG A 209 -18.739 13.204 20.396 1.00 88.20 C ANISOU 1700 CB ARG A 209 12049 10922 10539 -4575 -2479 3936 C ATOM 1701 CG ARG A 209 -19.285 12.906 21.785 1.00 93.35 C ANISOU 1701 CG ARG A 209 12906 11394 11170 -4429 -2565 3737 C ATOM 1702 CD ARG A 209 -18.186 12.939 22.837 1.00 94.19 C ANISOU 1702 CD ARG A 209 12940 11569 11280 -4603 -2753 3714 C ATOM 1703 NE ARG A 209 -17.282 11.799 22.726 1.00 95.41 N ANISOU 1703 NE ARG A 209 12747 12065 11442 -4528 -2728 3752 N ATOM 1704 CZ ARG A 209 -17.406 10.678 23.430 1.00 95.18 C ANISOU 1704 CZ ARG A 209 12691 12109 11363 -4305 -2728 3650 C ATOM 1705 NH1 ARG A 209 -18.398 10.546 24.300 1.00 82.07 N ANISOU 1705 NH1 ARG A 209 11340 10226 9618 -4158 -2730 3502 N ATOM 1706 NH2 ARG A 209 -16.538 9.689 23.266 1.00105.17 N ANISOU 1706 NH2 ARG A 209 13622 13660 12677 -4230 -2712 3698 N ATOM 1707 N LEU A 210 -18.938 14.510 17.397 1.00 75.34 N ANISOU 1707 N LEU A 210 10363 9404 8859 -4650 -2264 4171 N ATOM 1708 CA LEU A 210 -18.787 15.651 16.503 1.00110.42 C ANISOU 1708 CA LEU A 210 14874 13780 13299 -4784 -2265 4278 C ATOM 1709 C LEU A 210 -20.115 15.964 15.823 1.00105.73 C ANISOU 1709 C LEU A 210 14489 13006 12679 -4585 -2248 4268 C ATOM 1710 O LEU A 210 -20.486 17.127 15.662 1.00102.22 O ANISOU 1710 O LEU A 210 14238 12306 12294 -4628 -2333 4307 O ATOM 1711 CB LEU A 210 -17.704 15.383 15.457 1.00101.56 C ANISOU 1711 CB LEU A 210 13482 12999 12105 -4947 -2121 4415 C ATOM 1712 CG LEU A 210 -17.528 16.457 14.381 1.00 82.49 C ANISOU 1712 CG LEU A 210 11151 10546 9647 -5093 -2086 4549 C ATOM 1713 CD1 LEU A 210 -17.159 17.793 15.008 1.00 84.91 C ANISOU 1713 CD1 LEU A 210 11603 10583 10073 -5289 -2244 4569 C ATOM 1714 CD2 LEU A 210 -16.484 16.032 13.362 1.00 84.34 C ANISOU 1714 CD2 LEU A 210 11117 11139 9789 -5247 -1891 4657 C ATOM 1715 N VAL A 211 -20.825 14.913 15.426 1.00 96.46 N ANISOU 1715 N VAL A 211 13263 11958 11431 -4371 -2146 4222 N ATOM 1716 CA VAL A 211 -22.136 15.056 14.806 1.00 93.49 C ANISOU 1716 CA VAL A 211 13048 11432 11041 -4175 -2153 4212 C ATOM 1717 C VAL A 211 -23.163 15.507 15.843 1.00 93.46 C ANISOU 1717 C VAL A 211 13267 11059 11185 -4037 -2265 4080 C ATOM 1718 O VAL A 211 -24.099 16.244 15.526 1.00 83.17 O ANISOU 1718 O VAL A 211 12133 9512 9955 -3946 -2336 4100 O ATOM 1719 CB VAL A 211 -22.595 13.735 14.150 1.00 82.64 C ANISOU 1719 CB VAL A 211 11549 10303 9546 -4003 -2016 4182 C ATOM 1720 CG1 VAL A 211 -23.944 13.909 13.469 1.00 87.02 C ANISOU 1720 CG1 VAL A 211 12257 10715 10093 -3827 -2063 4189 C ATOM 1721 CG2 VAL A 211 -21.556 13.254 13.149 1.00 73.56 C ANISOU 1721 CG2 VAL A 211 10182 9521 8248 -4147 -1867 4288 C ATOM 1722 N LYS A 212 -22.974 15.067 17.084 1.00 95.02 N ANISOU 1722 N LYS A 212 13467 11209 11427 -4028 -2279 3953 N ATOM 1723 CA LYS A 212 -23.855 15.455 18.182 1.00 96.18 C ANISOU 1723 CA LYS A 212 13839 11011 11695 -3926 -2349 3803 C ATOM 1724 C LYS A 212 -23.845 16.965 18.403 1.00 99.11 C ANISOU 1724 C LYS A 212 14400 11076 12182 -4052 -2469 3821 C ATOM 1725 O LYS A 212 -24.896 17.578 18.594 1.00 90.10 O ANISOU 1725 O LYS A 212 13447 9617 11168 -3927 -2506 3755 O ATOM 1726 CB LYS A 212 -23.453 14.741 19.476 1.00 95.32 C ANISOU 1726 CB LYS A 212 13723 10932 11562 -3948 -2350 3681 C ATOM 1727 CG LYS A 212 -23.862 13.278 19.551 1.00 89.96 C ANISOU 1727 CG LYS A 212 12941 10426 10815 -3759 -2229 3621 C ATOM 1728 CD LYS A 212 -23.458 12.669 20.887 1.00104.25 C ANISOU 1728 CD LYS A 212 14770 12249 12592 -3759 -2246 3489 C ATOM 1729 CE LYS A 212 -23.894 11.216 20.997 1.00109.24 C ANISOU 1729 CE LYS A 212 15285 13049 13172 -3499 -2100 3359 C ATOM 1730 NZ LYS A 212 -23.470 10.607 22.289 1.00105.76 N ANISOU 1730 NZ LYS A 212 14875 12630 12679 -3480 -2129 3240 N ATOM 1731 N HIS A 213 -22.656 17.559 18.375 1.00105.58 N ANISOU 1731 N HIS A 213 15159 11978 12979 -4301 -2524 3911 N ATOM 1732 CA HIS A 213 -22.516 18.993 18.605 1.00112.39 C ANISOU 1732 CA HIS A 213 16199 12552 13952 -4449 -2631 3930 C ATOM 1733 C HIS A 213 -23.035 19.794 17.417 1.00109.34 C ANISOU 1733 C HIS A 213 15882 12056 13606 -4405 -2640 4076 C ATOM 1734 O HIS A 213 -23.578 20.885 17.587 1.00113.96 O ANISOU 1734 O HIS A 213 16670 12296 14334 -4391 -2717 4064 O ATOM 1735 CB HIS A 213 -21.057 19.357 18.884 1.00121.70 C ANISOU 1735 CB HIS A 213 17274 13864 15101 -4750 -2690 3992 C ATOM 1736 CG HIS A 213 -20.864 20.779 19.314 1.00131.07 C ANISOU 1736 CG HIS A 213 18657 14738 16405 -4919 -2800 3978 C ATOM 1737 ND1 HIS A 213 -19.685 21.465 19.113 1.00140.51 N ANISOU 1737 ND1 HIS A 213 19776 16006 17606 -5202 -2847 4088 N ATOM 1738 CD2 HIS A 213 -21.699 21.642 19.938 1.00132.06 C ANISOU 1738 CD2 HIS A 213 19049 14466 16663 -4848 -2855 3858 C ATOM 1739 CE1 HIS A 213 -19.804 22.690 19.592 1.00143.17 C ANISOU 1739 CE1 HIS A 213 20335 16000 18065 -5299 -2935 4037 C ATOM 1740 NE2 HIS A 213 -21.016 22.824 20.099 1.00137.72 N ANISOU 1740 NE2 HIS A 213 19855 15017 17455 -5084 -2939 3895 N ATOM 1741 N TRP A 214 -22.860 19.248 16.217 1.00105.55 N ANISOU 1741 N TRP A 214 15243 11863 12996 -4388 -2562 4214 N ATOM 1742 CA TRP A 214 -23.358 19.882 15.001 1.00 94.26 C ANISOU 1742 CA TRP A 214 13890 10369 11557 -4352 -2584 4374 C ATOM 1743 C TRP A 214 -24.871 20.048 15.069 1.00 81.32 C ANISOU 1743 C TRP A 214 12410 8439 10048 -4093 -2650 4314 C ATOM 1744 O TRP A 214 -25.420 21.058 14.629 1.00 83.30 O ANISOU 1744 O TRP A 214 12815 8432 10404 -4065 -2745 4410 O ATOM 1745 CB TRP A 214 -22.973 19.060 13.768 1.00 96.82 C ANISOU 1745 CB TRP A 214 14031 11079 11677 -4373 -2471 4495 C ATOM 1746 CG TRP A 214 -23.301 19.730 12.466 1.00106.20 C ANISOU 1746 CG TRP A 214 15315 12236 12800 -4391 -2503 4684 C ATOM 1747 CD1 TRP A 214 -22.465 20.495 11.707 1.00119.10 C ANISOU 1747 CD1 TRP A 214 16965 13928 14361 -4619 -2485 4858 C ATOM 1748 CD2 TRP A 214 -24.554 19.694 11.769 1.00103.70 C ANISOU 1748 CD2 TRP A 214 15101 11821 12481 -4184 -2573 4730 C ATOM 1749 NE1 TRP A 214 -23.117 20.937 10.583 1.00121.60 N ANISOU 1749 NE1 TRP A 214 17410 14186 14607 -4567 -2538 5015 N ATOM 1750 CE2 TRP A 214 -24.401 20.460 10.597 1.00109.39 C ANISOU 1750 CE2 TRP A 214 15911 12547 13106 -4299 -2609 4943 C ATOM 1751 CE3 TRP A 214 -25.789 19.088 12.023 1.00101.02 C ANISOU 1751 CE3 TRP A 214 14784 11386 12215 -3923 -2615 4620 C ATOM 1752 CZ2 TRP A 214 -25.436 20.638 9.680 1.00105.97 C ANISOU 1752 CZ2 TRP A 214 15592 12034 12638 -4157 -2715 5055 C ATOM 1753 CZ3 TRP A 214 -26.815 19.267 11.112 1.00104.57 C ANISOU 1753 CZ3 TRP A 214 15320 11756 12654 -3783 -2719 4727 C ATOM 1754 CH2 TRP A 214 -26.632 20.035 9.955 1.00103.95 C ANISOU 1754 CH2 TRP A 214 15333 11692 12470 -3898 -2782 4944 C ATOM 1755 N TYR A 215 -25.534 19.042 15.629 1.00 85.32 N ANISOU 1755 N TYR A 215 12872 8980 10565 -3906 -2599 4161 N ATOM 1756 CA TYR A 215 -26.983 19.047 15.775 1.00 95.48 C ANISOU 1756 CA TYR A 215 14272 10003 12001 -3659 -2644 4086 C ATOM 1757 C TYR A 215 -27.448 20.109 16.766 1.00102.64 C ANISOU 1757 C TYR A 215 15387 10470 13140 -3640 -2715 3974 C ATOM 1758 O TYR A 215 -28.467 20.766 16.555 1.00 97.28 O ANISOU 1758 O TYR A 215 14827 9491 12645 -3493 -2794 3995 O ATOM 1759 CB TYR A 215 -27.468 17.665 16.216 1.00 87.90 C ANISOU 1759 CB TYR A 215 13211 9191 10997 -3497 -2543 3941 C ATOM 1760 CG TYR A 215 -28.931 17.611 16.583 1.00 73.22 C ANISOU 1760 CG TYR A 215 11454 7037 9330 -3260 -2570 3832 C ATOM 1761 CD1 TYR A 215 -29.909 17.566 15.602 1.00 82.29 C ANISOU 1761 CD1 TYR A 215 12586 8155 10525 -3103 -2647 3934 C ATOM 1762 CD2 TYR A 215 -29.334 17.593 17.913 1.00 77.71 C ANISOU 1762 CD2 TYR A 215 12136 7355 10035 -3204 -2522 3624 C ATOM 1763 CE1 TYR A 215 -31.245 17.514 15.932 1.00 93.32 C ANISOU 1763 CE1 TYR A 215 14042 9268 12147 -2887 -2686 3839 C ATOM 1764 CE2 TYR A 215 -30.671 17.540 18.253 1.00 80.42 C ANISOU 1764 CE2 TYR A 215 12558 7410 10590 -2995 -2519 3508 C ATOM 1765 CZ TYR A 215 -31.623 17.499 17.259 1.00 88.91 C ANISOU 1765 CZ TYR A 215 13578 8447 11755 -2832 -2606 3619 C ATOM 1766 OH TYR A 215 -32.957 17.445 17.594 1.00 91.28 O ANISOU 1766 OH TYR A 215 13884 8492 12308 -2587 -2588 3450 O ATOM 1767 N GLN A 216 -26.693 20.271 17.848 1.00103.03 N ANISOU 1767 N GLN A 216 15480 10479 13188 -3790 -2692 3853 N ATOM 1768 CA GLN A 216 -27.042 21.227 18.892 1.00 96.45 C ANISOU 1768 CA GLN A 216 14861 9238 12546 -3799 -2732 3705 C ATOM 1769 C GLN A 216 -26.845 22.668 18.428 1.00 96.19 C ANISOU 1769 C GLN A 216 14950 8966 12631 -3910 -2831 3836 C ATOM 1770 O GLN A 216 -27.565 23.570 18.858 1.00 92.37 O ANISOU 1770 O GLN A 216 14646 8080 12370 -3829 -2868 3754 O ATOM 1771 CB GLN A 216 -26.216 20.963 20.152 1.00 96.00 C ANISOU 1771 CB GLN A 216 14833 9234 12408 -3962 -2704 3543 C ATOM 1772 CG GLN A 216 -26.484 19.613 20.802 1.00 91.72 C ANISOU 1772 CG GLN A 216 14225 8857 11767 -3848 -2608 3402 C ATOM 1773 CD GLN A 216 -27.852 19.535 21.455 1.00 82.33 C ANISOU 1773 CD GLN A 216 13190 7353 10738 -3630 -2541 3210 C ATOM 1774 OE1 GLN A 216 -28.863 19.321 20.786 1.00 85.98 O ANISOU 1774 OE1 GLN A 216 13610 7754 11306 -3425 -2520 3249 O ATOM 1775 NE2 GLN A 216 -27.888 19.709 22.771 1.00 76.65 N ANISOU 1775 NE2 GLN A 216 12655 6429 10039 -3686 -2508 2993 N ATOM 1776 N THR A 217 -25.868 22.878 17.551 1.00 95.62 N ANISOU 1776 N THR A 217 14781 9129 12422 -4097 -2855 4036 N ATOM 1777 CA THR A 217 -25.606 24.205 17.005 1.00105.47 C ANISOU 1777 CA THR A 217 16146 10168 13758 -4226 -2936 4192 C ATOM 1778 C THR A 217 -26.751 24.655 16.105 1.00112.89 C ANISOU 1778 C THR A 217 17168 10906 14821 -4020 -3010 4321 C ATOM 1779 O THR A 217 -27.075 25.840 16.042 1.00116.95 O ANISOU 1779 O THR A 217 17848 11067 15521 -4018 -3090 4379 O ATOM 1780 CB THR A 217 -24.289 24.244 16.205 1.00109.52 C ANISOU 1780 CB THR A 217 16528 10998 14085 -4486 -2915 4382 C ATOM 1781 OG1 THR A 217 -24.297 23.210 15.213 1.00112.79 O ANISOU 1781 OG1 THR A 217 16764 11783 14309 -4416 -2849 4485 O ATOM 1782 CG2 THR A 217 -23.095 24.047 17.128 1.00108.20 C ANISOU 1782 CG2 THR A 217 16281 10975 13857 -4715 -2891 4276 C ATOM 1783 N CYS A 218 -27.355 23.702 15.403 1.00116.20 N ANISOU 1783 N CYS A 218 17466 11545 15141 -3850 -2995 4370 N ATOM 1784 CA CYS A 218 -28.484 23.995 14.530 1.00118.43 C ANISOU 1784 CA CYS A 218 17802 11668 15527 -3648 -3103 4498 C ATOM 1785 C CYS A 218 -29.805 23.981 15.295 1.00127.23 C ANISOU 1785 C CYS A 218 18984 12444 16914 -3382 -3130 4318 C ATOM 1786 O CYS A 218 -30.821 24.469 14.801 1.00137.38 O ANISOU 1786 O CYS A 218 20328 13485 18384 -3198 -3251 4400 O ATOM 1787 CB CYS A 218 -28.538 22.994 13.375 1.00115.08 C ANISOU 1787 CB CYS A 218 17224 11636 14863 -3606 -3089 4628 C ATOM 1788 SG CYS A 218 -27.063 22.974 12.332 1.00102.53 S ANISOU 1788 SG CYS A 218 15549 10444 12965 -3907 -3016 4830 S ATOM 1789 N LYS A 219 -29.785 23.420 16.500 1.00126.11 N ANISOU 1789 N LYS A 219 18832 12281 16803 -3364 -3017 4072 N ATOM 1790 CA LYS A 219 -30.998 23.292 17.301 1.00126.51 C ANISOU 1790 CA LYS A 219 18940 12022 17107 -3128 -2990 3864 C ATOM 1791 C LYS A 219 -31.358 24.609 17.980 1.00129.87 C ANISOU 1791 C LYS A 219 19563 11957 17826 -3105 -3018 3762 C ATOM 1792 O LYS A 219 -32.514 24.841 18.333 1.00138.67 O ANISOU 1792 O LYS A 219 20726 12733 19228 -2879 -3020 3633 O ATOM 1793 CB LYS A 219 -30.837 22.187 18.347 1.00122.41 C ANISOU 1793 CB LYS A 219 18369 11658 16484 -3136 -2837 3634 C ATOM 1794 CG LYS A 219 -32.153 21.694 18.929 1.00117.67 C ANISOU 1794 CG LYS A 219 17780 10830 16099 -2885 -2774 3436 C ATOM 1795 CD LYS A 219 -31.938 20.565 19.921 1.00116.56 C ANISOU 1795 CD LYS A 219 17614 10858 15817 -2917 -2612 3230 C ATOM 1796 CE LYS A 219 -33.263 19.963 20.362 1.00115.88 C ANISOU 1796 CE LYS A 219 17520 10569 15939 -2680 -2525 3042 C ATOM 1797 NZ LYS A 219 -34.171 20.986 20.948 1.00114.87 N ANISOU 1797 NZ LYS A 219 17539 9943 16165 -2550 -2515 2870 N ATOM 1798 N LYS A 220 -30.362 25.470 18.159 1.00126.29 N ANISOU 1798 N LYS A 220 19209 11455 17321 -3340 -3031 3808 N ATOM 1799 CA LYS A 220 -30.585 26.782 18.752 1.00132.95 C ANISOU 1799 CA LYS A 220 20250 11833 18433 -3348 -3049 3716 C ATOM 1800 C LYS A 220 -30.996 27.784 17.678 1.00138.97 C ANISOU 1800 C LYS A 220 21067 12384 19353 -3274 -3197 3964 C ATOM 1801 O LYS A 220 -31.217 28.961 17.961 1.00142.60 O ANISOU 1801 O LYS A 220 21687 12434 20061 -3264 -3226 3934 O ATOM 1802 CB LYS A 220 -29.331 27.263 19.486 1.00139.70 C ANISOU 1802 CB LYS A 220 21195 12712 19173 -3651 -3009 3642 C ATOM 1803 CG LYS A 220 -28.121 27.454 18.589 1.00138.11 C ANISOU 1803 CG LYS A 220 20919 12804 18753 -3902 -3073 3902 C ATOM 1804 CD LYS A 220 -26.833 27.509 19.395 1.00123.03 C ANISOU 1804 CD LYS A 220 19020 11027 16701 -4198 -3037 3804 C ATOM 1805 CE LYS A 220 -26.863 28.628 20.422 1.00113.19 C ANISOU 1805 CE LYS A 220 17995 9347 15664 -4277 -3033 3613 C ATOM 1806 NZ LYS A 220 -25.605 28.677 21.217 1.00112.54 N ANISOU 1806 NZ LYS A 220 17923 9403 15435 -4581 -3036 3517 N ATOM 1807 N THR A 221 -31.096 27.302 16.442 1.00145.58 N ANISOU 1807 N THR A 221 21780 13499 20035 -3227 -3291 4207 N ATOM 1808 CA THR A 221 -31.505 28.132 15.315 1.00152.19 C ANISOU 1808 CA THR A 221 22675 14183 20967 -3158 -3457 4474 C ATOM 1809 C THR A 221 -32.941 27.825 14.895 1.00156.33 C ANISOU 1809 C THR A 221 23128 14577 21692 -2828 -3570 4488 C ATOM 1810 O THR A 221 -33.824 28.676 15.001 1.00159.12 O ANISOU 1810 O THR A 221 23565 14507 22386 -2639 -3657 4472 O ATOM 1811 CB THR A 221 -30.573 27.937 14.104 1.00144.29 C ANISOU 1811 CB THR A 221 21614 13580 19629 -3367 -3498 4753 C ATOM 1812 OG1 THR A 221 -29.225 28.241 14.482 1.00148.33 O ANISOU 1812 OG1 THR A 221 22158 14205 19998 -3673 -3401 4739 O ATOM 1813 CG2 THR A 221 -30.992 28.843 12.957 1.00135.95 C ANISOU 1813 CG2 THR A 221 20659 12352 18646 -3314 -3676 5038 C ATOM 1814 N HIS A 222 -33.165 26.606 14.414 1.00161.87 N ANISOU 1814 N HIS A 222 23663 15639 22202 -2758 -3571 4513 N ATOM 1815 CA HIS A 222 -34.482 26.197 13.932 1.00172.00 C ANISOU 1815 CA HIS A 222 24845 16851 23657 -2465 -3702 4537 C ATOM 1816 C HIS A 222 -35.409 25.745 15.057 1.00173.40 C ANISOU 1816 C HIS A 222 24967 16795 24124 -2247 -3597 4227 C ATOM 1817 O HIS A 222 -36.614 25.601 14.853 1.00171.47 O ANISOU 1817 O HIS A 222 24628 16380 24141 -1975 -3704 4201 O ATOM 1818 CB HIS A 222 -34.343 25.075 12.900 1.00177.87 C ANISOU 1818 CB HIS A 222 25440 18074 24067 -2496 -3745 4685 C ATOM 1819 CG HIS A 222 -34.366 25.552 11.481 1.00186.40 C ANISOU 1819 CG HIS A 222 26562 19246 25015 -2526 -3942 4998 C ATOM 1820 ND1 HIS A 222 -33.766 24.856 10.453 1.00188.10 N ANISOU 1820 ND1 HIS A 222 26714 19913 24840 -2675 -3935 5154 N ATOM 1821 CD2 HIS A 222 -34.924 26.649 10.918 1.00191.14 C ANISOU 1821 CD2 HIS A 222 27272 19539 25814 -2428 -4143 5177 C ATOM 1822 CE1 HIS A 222 -33.949 25.508 9.318 1.00191.37 C ANISOU 1822 CE1 HIS A 222 27216 20300 25194 -2683 -4120 5416 C ATOM 1823 NE2 HIS A 222 -34.649 26.598 9.572 1.00193.21 N ANISOU 1823 NE2 HIS A 222 27554 20077 25781 -2532 -4263 5448 N ATOM 1824 N GLY A 223 -34.850 25.523 16.242 1.00174.75 N ANISOU 1824 N GLY A 223 25189 16955 24253 -2369 -3390 3984 N ATOM 1825 CA GLY A 223 -35.640 25.064 17.370 1.00171.71 C ANISOU 1825 CA GLY A 223 24781 16360 24100 -2202 -3244 3663 C ATOM 1826 C GLY A 223 -35.859 23.563 17.353 1.00169.62 C ANISOU 1826 C GLY A 223 24350 16425 23673 -2148 -3171 3597 C ATOM 1827 O GLY A 223 -34.973 22.805 16.964 1.00173.68 O ANISOU 1827 O GLY A 223 24802 17363 23825 -2324 -3142 3708 O ATOM 1828 N ASN A 224 -37.043 23.134 17.778 1.00163.81 N ANISOU 1828 N ASN A 224 23529 15481 23232 -1901 -3127 3403 N ATOM 1829 CA ASN A 224 -37.373 21.713 17.846 1.00153.88 C ANISOU 1829 CA ASN A 224 22108 14492 21868 -1832 -3033 3303 C ATOM 1830 C ASN A 224 -37.842 21.145 16.509 1.00154.89 C ANISOU 1830 C ASN A 224 22043 14888 21918 -1711 -3221 3521 C ATOM 1831 O ASN A 224 -38.174 19.963 16.413 1.00150.93 O ANISOU 1831 O ASN A 224 21340 14711 21294 -1615 -3108 3382 O ATOM 1832 CB ASN A 224 -38.445 21.467 18.910 1.00152.14 C ANISOU 1832 CB ASN A 224 21799 14059 21946 -1595 -2804 2890 C ATOM 1833 CG ASN A 224 -37.927 21.677 20.320 1.00147.11 C ANISOU 1833 CG ASN A 224 21357 13277 21261 -1741 -2566 2621 C ATOM 1834 OD1 ASN A 224 -36.884 22.297 20.525 1.00149.65 O ANISOU 1834 OD1 ASN A 224 21889 13544 21429 -1998 -2622 2740 O ATOM 1835 ND2 ASN A 224 -38.656 21.157 21.301 1.00138.27 N ANISOU 1835 ND2 ASN A 224 20174 12102 20262 -1595 -2297 2252 N ATOM 1836 N LYS A 225 -37.877 21.994 15.486 1.00163.66 N ANISOU 1836 N LYS A 225 23204 15914 23063 -1708 -3477 3815 N ATOM 1837 CA LYS A 225 -38.349 21.596 14.163 1.00165.12 C ANISOU 1837 CA LYS A 225 23259 16318 23162 -1612 -3708 4050 C ATOM 1838 C LYS A 225 -37.537 20.445 13.571 1.00162.04 C ANISOU 1838 C LYS A 225 22805 16457 22305 -1796 -3647 4155 C ATOM 1839 O LYS A 225 -38.095 19.541 12.952 1.00172.33 O ANISOU 1839 O LYS A 225 23929 18019 23530 -1676 -3693 4136 O ATOM 1840 CB LYS A 225 -38.320 22.793 13.209 1.00171.22 C ANISOU 1840 CB LYS A 225 24122 16982 23952 -1619 -3940 4314 C ATOM 1841 CG LYS A 225 -39.158 23.973 13.672 1.00173.58 C ANISOU 1841 CG LYS A 225 24470 16751 24733 -1412 -4016 4230 C ATOM 1842 CD LYS A 225 -40.602 23.567 13.909 1.00174.07 C ANISOU 1842 CD LYS A 225 24327 16587 25223 -1078 -4078 4055 C ATOM 1843 CE LYS A 225 -41.417 24.729 14.452 1.00181.28 C ANISOU 1843 CE LYS A 225 25258 16971 26650 -856 -4100 3919 C ATOM 1844 NZ LYS A 225 -42.831 24.343 14.706 1.00183.13 N ANISOU 1844 NZ LYS A 225 25236 16990 27356 -517 -4129 3707 N ATOM 1845 N LEU A 226 -36.233 20.447 13.794 1.00144.86 N ANISOU 1845 N LEU A 226 20714 14506 19818 -2058 -3490 4169 N ATOM 1846 CA LEU A 226 -35.400 19.406 13.219 1.00124.81 C ANISOU 1846 CA LEU A 226 18092 12465 16866 -2222 -3405 4246 C ATOM 1847 C LEU A 226 -35.657 18.049 13.852 1.00106.65 C ANISOU 1847 C LEU A 226 15635 10358 14529 -2131 -3206 3988 C ATOM 1848 O LEU A 226 -36.238 17.959 14.924 1.00 98.57 O ANISOU 1848 O LEU A 226 14577 9132 13744 -1987 -3062 3696 O ATOM 1849 CB LEU A 226 -33.925 19.773 13.314 1.00124.92 C ANISOU 1849 CB LEU A 226 18179 12668 16616 -2500 -3281 4294 C ATOM 1850 CG LEU A 226 -33.518 20.999 14.116 1.00120.47 C ANISOU 1850 CG LEU A 226 17773 11776 16223 -2587 -3258 4238 C ATOM 1851 CD1 LEU A 226 -34.165 21.001 15.485 1.00125.45 C ANISOU 1851 CD1 LEU A 226 18452 12068 17147 -2457 -3158 3966 C ATOM 1852 CD2 LEU A 226 -32.014 20.998 14.258 1.00107.81 C ANISOU 1852 CD2 LEU A 226 16178 10439 14347 -2868 -3131 4261 C ATOM 1853 N PRO A 227 -35.232 16.997 13.167 1.00 75.74 N ANISOU 1853 N PRO A 227 11599 6882 10298 -2196 -3146 4027 N ATOM 1854 CA PRO A 227 -35.439 15.624 13.648 1.00 72.61 C ANISOU 1854 CA PRO A 227 11014 6738 9837 -2089 -2919 3734 C ATOM 1855 C PRO A 227 -34.683 15.323 14.943 1.00105.22 C ANISOU 1855 C PRO A 227 15182 10871 13926 -2185 -2681 3539 C ATOM 1856 O PRO A 227 -33.752 16.051 15.273 1.00111.87 O ANISOU 1856 O PRO A 227 16171 11626 14708 -2386 -2698 3658 O ATOM 1857 CB PRO A 227 -34.896 14.767 12.497 1.00 71.91 C ANISOU 1857 CB PRO A 227 10836 7095 9392 -2192 -2925 3873 C ATOM 1858 CG PRO A 227 -34.996 15.635 11.301 1.00 92.57 C ANISOU 1858 CG PRO A 227 13565 9661 11946 -2257 -3198 4203 C ATOM 1859 CD PRO A 227 -34.701 17.014 11.792 1.00 77.06 C ANISOU 1859 CD PRO A 227 11801 7316 10163 -2352 -3292 4344 C ATOM 1860 N PRO A 228 -35.090 14.269 15.672 1.00 80.18 N ANISOU 1860 N PRO A 228 11887 7791 10786 -2053 -2474 3251 N ATOM 1861 CA PRO A 228 -34.408 13.862 16.908 1.00 72.95 C ANISOU 1861 CA PRO A 228 11021 6900 9797 -2136 -2268 3077 C ATOM 1862 C PRO A 228 -32.916 13.597 16.705 1.00 76.14 C ANISOU 1862 C PRO A 228 11432 7599 9900 -2373 -2248 3238 C ATOM 1863 O PRO A 228 -32.501 13.220 15.609 1.00 81.07 O ANISOU 1863 O PRO A 228 11964 8504 10334 -2438 -2297 3406 O ATOM 1864 CB PRO A 228 -35.138 12.576 17.300 1.00 76.79 C ANISOU 1864 CB PRO A 228 11352 7509 10316 -1956 -2073 2811 C ATOM 1865 CG PRO A 228 -36.497 12.730 16.718 1.00 80.20 C ANISOU 1865 CG PRO A 228 11680 7800 10994 -1750 -2170 2763 C ATOM 1866 CD PRO A 228 -36.295 13.458 15.420 1.00 83.08 C ANISOU 1866 CD PRO A 228 12072 8208 11286 -1822 -2437 3073 C ATOM 1867 N GLN A 229 -32.128 13.792 17.758 1.00 71.41 N ANISOU 1867 N GLN A 229 10935 6937 9260 -2506 -2177 3175 N ATOM 1868 CA GLN A 229 -30.679 13.626 17.682 1.00 69.19 C ANISOU 1868 CA GLN A 229 10630 6910 8749 -2734 -2173 3317 C ATOM 1869 C GLN A 229 -30.290 12.171 17.441 1.00 68.70 C ANISOU 1869 C GLN A 229 10372 7224 8506 -2684 -2030 3256 C ATOM 1870 O GLN A 229 -29.248 11.888 16.850 1.00 75.67 O ANISOU 1870 O GLN A 229 11157 8384 9212 -2829 -2027 3403 O ATOM 1871 CB GLN A 229 -30.017 14.138 18.963 1.00 76.15 C ANISOU 1871 CB GLN A 229 11659 7627 9647 -2877 -2160 3234 C ATOM 1872 CG GLN A 229 -28.500 14.212 18.896 1.00 82.23 C ANISOU 1872 CG GLN A 229 12388 8615 10239 -3137 -2203 3397 C ATOM 1873 CD GLN A 229 -27.870 14.453 20.252 1.00 89.69 C ANISOU 1873 CD GLN A 229 13454 9451 11173 -3264 -2204 3276 C ATOM 1874 OE1 GLN A 229 -28.414 14.053 21.281 1.00 91.97 O ANISOU 1874 OE1 GLN A 229 13823 9626 11495 -3141 -2110 3049 O ATOM 1875 NE2 GLN A 229 -26.716 15.112 20.261 1.00 88.41 N ANISOU 1875 NE2 GLN A 229 13288 9351 10953 -3497 -2297 3388 N ATOM 1876 N TYR A 230 -31.137 11.256 17.904 1.00 61.38 N ANISOU 1876 N TYR A 230 9386 6290 7647 -2481 -1896 3030 N ATOM 1877 CA TYR A 230 -30.898 9.823 17.759 1.00 59.51 C ANISOU 1877 CA TYR A 230 8980 6352 7279 -2409 -1748 2945 C ATOM 1878 C TYR A 230 -30.757 9.426 16.289 1.00 80.26 C ANISOU 1878 C TYR A 230 11464 9254 9776 -2421 -1780 3081 C ATOM 1879 O TYR A 230 -30.036 8.485 15.956 1.00 74.74 O ANISOU 1879 O TYR A 230 10628 8843 8927 -2449 -1678 3085 O ATOM 1880 CB TYR A 230 -32.034 9.031 18.413 1.00 58.20 C ANISOU 1880 CB TYR A 230 8796 6076 7242 -2197 -1600 2687 C ATOM 1881 CG TYR A 230 -31.749 7.557 18.605 1.00 56.43 C ANISOU 1881 CG TYR A 230 8447 6084 6911 -2130 -1430 2577 C ATOM 1882 CD1 TYR A 230 -30.446 7.078 18.645 1.00 56.09 C ANISOU 1882 CD1 TYR A 230 8340 6272 6701 -2242 -1412 2672 C ATOM 1883 CD2 TYR A 230 -32.786 6.644 18.741 1.00 55.55 C ANISOU 1883 CD2 TYR A 230 8268 5943 6896 -1953 -1287 2378 C ATOM 1884 CE1 TYR A 230 -30.185 5.732 18.819 1.00 54.82 C ANISOU 1884 CE1 TYR A 230 8065 6286 6477 -2160 -1265 2578 C ATOM 1885 CE2 TYR A 230 -32.535 5.298 18.915 1.00 60.95 C ANISOU 1885 CE2 TYR A 230 8856 6800 7500 -1894 -1129 2284 C ATOM 1886 CZ TYR A 230 -31.234 4.847 18.954 1.00 58.61 C ANISOU 1886 CZ TYR A 230 8513 6713 7044 -1988 -1123 2389 C ATOM 1887 OH TYR A 230 -30.982 3.505 19.127 1.00 57.93 O ANISOU 1887 OH TYR A 230 8332 6767 6912 -1909 -974 2303 O ATOM 1888 N ALA A 231 -31.449 10.151 15.416 1.00 74.05 N ANISOU 1888 N ALA A 231 10717 8371 9046 -2400 -1924 3191 N ATOM 1889 CA ALA A 231 -31.407 9.878 13.985 1.00 74.47 C ANISOU 1889 CA ALA A 231 10684 8676 8937 -2430 -1977 3327 C ATOM 1890 C ALA A 231 -30.020 10.143 13.408 1.00 84.03 C ANISOU 1890 C ALA A 231 11887 10109 9931 -2670 -1979 3547 C ATOM 1891 O ALA A 231 -29.529 9.380 12.577 1.00 89.97 O ANISOU 1891 O ALA A 231 12519 11175 10492 -2713 -1889 3573 O ATOM 1892 CB ALA A 231 -32.450 10.710 13.259 1.00 75.28 C ANISOU 1892 CB ALA A 231 10859 8595 9149 -2359 -2179 3428 C ATOM 1893 N LEU A 232 -29.395 11.228 13.853 1.00 86.32 N ANISOU 1893 N LEU A 232 12300 10232 10265 -2835 -2066 3686 N ATOM 1894 CA LEU A 232 -28.072 11.605 13.366 1.00 78.84 C ANISOU 1894 CA LEU A 232 11335 9470 9152 -3093 -2064 3897 C ATOM 1895 C LEU A 232 -27.000 10.647 13.877 1.00 76.20 C ANISOU 1895 C LEU A 232 10826 9384 8740 -3138 -1895 3799 C ATOM 1896 O LEU A 232 -26.011 10.388 13.190 1.00 73.76 O ANISOU 1896 O LEU A 232 10395 9355 8276 -3286 -1815 3909 O ATOM 1897 CB LEU A 232 -27.733 13.042 13.776 1.00 70.58 C ANISOU 1897 CB LEU A 232 10431 8164 8223 -3221 -2186 3976 C ATOM 1898 CG LEU A 232 -28.445 14.188 13.047 1.00 73.47 C ANISOU 1898 CG LEU A 232 10939 8314 8661 -3201 -2354 4102 C ATOM 1899 CD1 LEU A 232 -28.436 13.962 11.541 1.00 74.38 C ANISOU 1899 CD1 LEU A 232 11004 8692 8566 -3236 -2364 4247 C ATOM 1900 CD2 LEU A 232 -29.866 14.402 13.559 1.00 81.59 C ANISOU 1900 CD2 LEU A 232 12084 8995 9921 -2999 -2460 4028 C ATOM 1901 N GLU A 233 -27.201 10.126 15.083 1.00 75.47 N ANISOU 1901 N GLU A 233 10727 9187 8763 -3008 -1837 3595 N ATOM 1902 CA GLU A 233 -26.265 9.176 15.674 1.00 61.58 C ANISOU 1902 CA GLU A 233 8812 7628 6958 -3015 -1714 3508 C ATOM 1903 C GLU A 233 -26.267 7.858 14.907 1.00 78.57 C ANISOU 1903 C GLU A 233 10775 10070 9009 -2895 -1553 3427 C ATOM 1904 O GLU A 233 -25.211 7.320 14.576 1.00 61.09 O ANISOU 1904 O GLU A 233 8387 8116 6710 -2975 -1456 3468 O ATOM 1905 CB GLU A 233 -26.607 8.929 17.145 1.00 60.26 C ANISOU 1905 CB GLU A 233 8733 7258 6906 -2902 -1703 3323 C ATOM 1906 CG GLU A 233 -26.612 10.186 18.001 1.00 67.37 C ANISOU 1906 CG GLU A 233 9840 7859 7899 -3022 -1842 3353 C ATOM 1907 CD GLU A 233 -26.977 9.906 19.446 1.00 85.13 C ANISOU 1907 CD GLU A 233 12209 9926 10212 -2926 -1807 3154 C ATOM 1908 OE1 GLU A 233 -27.138 10.875 20.218 1.00 97.30 O ANISOU 1908 OE1 GLU A 233 13945 11198 11826 -3005 -1894 3123 O ATOM 1909 OE2 GLU A 233 -27.102 8.718 19.810 1.00 87.19 O ANISOU 1909 OE2 GLU A 233 12387 10301 10441 -2781 -1684 3025 O ATOM 1910 N LEU A 234 -27.462 7.346 14.625 1.00 73.92 N ANISOU 1910 N LEU A 234 10208 9425 8452 -2705 -1520 3295 N ATOM 1911 CA LEU A 234 -27.608 6.101 13.879 1.00 62.42 C ANISOU 1911 CA LEU A 234 8598 8210 6909 -2594 -1372 3185 C ATOM 1912 C LEU A 234 -27.150 6.266 12.433 1.00 60.62 C ANISOU 1912 C LEU A 234 8314 8233 6486 -2733 -1362 3336 C ATOM 1913 O LEU A 234 -26.668 5.318 11.814 1.00 60.71 O ANISOU 1913 O LEU A 234 8174 8509 6386 -2723 -1204 3273 O ATOM 1914 CB LEU A 234 -29.060 5.621 13.920 1.00 60.36 C ANISOU 1914 CB LEU A 234 8375 7812 6747 -2387 -1362 3004 C ATOM 1915 CG LEU A 234 -29.616 5.242 15.294 1.00 62.35 C ANISOU 1915 CG LEU A 234 8681 7841 7169 -2246 -1303 2822 C ATOM 1916 CD1 LEU A 234 -31.084 4.863 15.193 1.00 55.50 C ANISOU 1916 CD1 LEU A 234 7821 6845 6423 -2070 -1281 2649 C ATOM 1917 CD2 LEU A 234 -28.810 4.106 15.900 1.00 62.76 C ANISOU 1917 CD2 LEU A 234 8625 8027 7195 -2206 -1151 2737 C ATOM 1918 N LEU A 235 -27.303 7.474 11.901 1.00 62.31 N ANISOU 1918 N LEU A 235 8669 8352 6656 -2867 -1521 3533 N ATOM 1919 CA LEU A 235 -26.893 7.764 10.533 1.00 71.34 C ANISOU 1919 CA LEU A 235 9814 9717 7576 -3032 -1521 3711 C ATOM 1920 C LEU A 235 -25.372 7.755 10.411 1.00 78.48 C ANISOU 1920 C LEU A 235 10588 10844 8387 -3238 -1389 3814 C ATOM 1921 O LEU A 235 -24.824 7.348 9.386 1.00 87.52 O ANISOU 1921 O LEU A 235 11641 12276 9337 -3336 -1252 3853 O ATOM 1922 CB LEU A 235 -27.455 9.112 10.077 1.00 77.29 C ANISOU 1922 CB LEU A 235 10778 10265 8323 -3123 -1746 3928 C ATOM 1923 CG LEU A 235 -27.286 9.462 8.598 1.00 79.64 C ANISOU 1923 CG LEU A 235 11145 10760 8353 -3289 -1780 4138 C ATOM 1924 CD1 LEU A 235 -27.973 8.426 7.722 1.00 68.72 C ANISOU 1924 CD1 LEU A 235 9703 9591 6817 -3160 -1723 3992 C ATOM 1925 CD2 LEU A 235 -27.828 10.854 8.311 1.00 83.38 C ANISOU 1925 CD2 LEU A 235 11815 10968 8897 -3320 -2015 4302 C ATOM 1926 N THR A 236 -24.699 8.206 11.465 1.00 74.49 N ANISOU 1926 N THR A 236 10067 10210 8024 -3310 -1429 3845 N ATOM 1927 CA THR A 236 -23.241 8.207 11.508 1.00 71.46 C ANISOU 1927 CA THR A 236 9515 10022 7614 -3500 -1327 3927 C ATOM 1928 C THR A 236 -22.709 6.778 11.550 1.00 65.77 C ANISOU 1928 C THR A 236 8543 9549 6896 -3372 -1119 3747 C ATOM 1929 O THR A 236 -21.701 6.458 10.918 1.00 67.36 O ANISOU 1929 O THR A 236 8557 10020 7017 -3491 -960 3786 O ATOM 1930 CB THR A 236 -22.713 8.990 12.725 1.00 66.79 C ANISOU 1930 CB THR A 236 8968 9221 7189 -3603 -1459 3977 C ATOM 1931 OG1 THR A 236 -23.211 10.333 12.685 1.00 67.93 O ANISOU 1931 OG1 THR A 236 9338 9099 7372 -3684 -1635 4084 O ATOM 1932 CG2 THR A 236 -21.193 9.019 12.729 1.00 68.55 C ANISOU 1932 CG2 THR A 236 8976 9658 7412 -3814 -1379 4065 C ATOM 1933 N VAL A 237 -23.399 5.922 12.299 1.00 68.68 N ANISOU 1933 N VAL A 237 8909 9810 7374 -3128 -1107 3547 N ATOM 1934 CA VAL A 237 -23.051 4.509 12.373 1.00 62.66 C ANISOU 1934 CA VAL A 237 7939 9224 6643 -2972 -921 3370 C ATOM 1935 C VAL A 237 -23.207 3.857 11.004 1.00 74.92 C ANISOU 1935 C VAL A 237 9423 11021 8024 -2959 -752 3311 C ATOM 1936 O VAL A 237 -22.356 3.076 10.576 1.00 64.49 O ANISOU 1936 O VAL A 237 7890 9938 6675 -2966 -556 3250 O ATOM 1937 CB VAL A 237 -23.925 3.764 13.400 1.00 60.27 C ANISOU 1937 CB VAL A 237 7701 8722 6477 -2729 -939 3182 C ATOM 1938 CG1 VAL A 237 -23.566 2.285 13.436 1.00 59.74 C ANISOU 1938 CG1 VAL A 237 7437 8807 6457 -2567 -749 3017 C ATOM 1939 CG2 VAL A 237 -23.770 4.387 14.777 1.00 59.77 C ANISOU 1939 CG2 VAL A 237 7741 8429 6538 -2757 -1093 3222 C ATOM 1940 N TYR A 238 -24.296 4.195 10.321 1.00 77.42 N ANISOU 1940 N TYR A 238 9915 11272 8228 -2942 -834 3323 N ATOM 1941 CA TYR A 238 -24.574 3.664 8.992 1.00 64.60 C ANISOU 1941 CA TYR A 238 8278 9873 6396 -2952 -716 3266 C ATOM 1942 C TYR A 238 -23.499 4.078 7.993 1.00 67.42 C ANISOU 1942 C TYR A 238 8573 10491 6552 -3199 -599 3425 C ATOM 1943 O TYR A 238 -23.112 3.296 7.126 1.00 94.50 O ANISOU 1943 O TYR A 238 11888 14182 9835 -3218 -384 3324 O ATOM 1944 CB TYR A 238 -25.951 4.131 8.511 1.00 64.49 C ANISOU 1944 CB TYR A 238 8471 9720 6311 -2904 -899 3287 C ATOM 1945 CG TYR A 238 -26.293 3.709 7.099 1.00 74.85 C ANISOU 1945 CG TYR A 238 9812 11266 7362 -2944 -834 3246 C ATOM 1946 CD1 TYR A 238 -26.743 2.424 6.826 1.00 75.66 C ANISOU 1946 CD1 TYR A 238 9824 11474 7451 -2790 -694 2985 C ATOM 1947 CD2 TYR A 238 -26.174 4.600 6.039 1.00 74.53 C ANISOU 1947 CD2 TYR A 238 9914 11333 7072 -3153 -918 3470 C ATOM 1948 CE1 TYR A 238 -27.059 2.036 5.538 1.00 88.68 C ANISOU 1948 CE1 TYR A 238 11518 13342 8835 -2845 -644 2924 C ATOM 1949 CE2 TYR A 238 -26.487 4.221 4.748 1.00 75.88 C ANISOU 1949 CE2 TYR A 238 10146 11731 6955 -3209 -873 3435 C ATOM 1950 CZ TYR A 238 -26.929 2.938 4.503 1.00 87.92 C ANISOU 1950 CZ TYR A 238 11574 13370 8461 -3056 -739 3149 C ATOM 1951 OH TYR A 238 -27.243 2.557 3.218 1.00108.09 O ANISOU 1951 OH TYR A 238 14207 16157 10705 -3130 -703 3091 O ATOM 1952 N ALA A 239 -23.018 5.311 8.123 1.00 68.68 N ANISOU 1952 N ALA A 239 8815 10571 6709 -3403 -722 3663 N ATOM 1953 CA ALA A 239 -21.980 5.827 7.238 1.00 71.68 C ANISOU 1953 CA ALA A 239 9147 11177 6911 -3677 -601 3840 C ATOM 1954 C ALA A 239 -20.673 5.058 7.410 1.00 93.25 C ANISOU 1954 C ALA A 239 11563 14135 9733 -3701 -352 3741 C ATOM 1955 O ALA A 239 -19.935 4.847 6.448 1.00100.89 O ANISOU 1955 O ALA A 239 12419 15380 10536 -3850 -125 3755 O ATOM 1956 CB ALA A 239 -21.759 7.310 7.490 1.00 72.91 C ANISOU 1956 CB ALA A 239 9457 11147 7098 -3891 -793 4109 C ATOM 1957 N TRP A 240 -20.393 4.642 8.641 1.00 81.34 N ANISOU 1957 N TRP A 240 9914 12505 8488 -3554 -395 3641 N ATOM 1958 CA TRP A 240 -19.181 3.888 8.938 1.00 84.12 C ANISOU 1958 CA TRP A 240 9940 13035 8985 -3535 -209 3553 C ATOM 1959 C TRP A 240 -19.320 2.420 8.545 1.00 89.45 C ANISOU 1959 C TRP A 240 10471 13859 9656 -3318 16 3302 C ATOM 1960 O TRP A 240 -18.378 1.813 8.037 1.00 93.70 O ANISOU 1960 O TRP A 240 10758 14638 10206 -3350 264 3228 O ATOM 1961 CB TRP A 240 -18.833 4.000 10.424 1.00 94.95 C ANISOU 1961 CB TRP A 240 11241 14214 10620 -3461 -384 3560 C ATOM 1962 CG TRP A 240 -17.615 3.219 10.813 1.00 82.75 C ANISOU 1962 CG TRP A 240 9346 12831 9262 -3414 -253 3486 C ATOM 1963 CD1 TRP A 240 -16.318 3.641 10.757 1.00 73.80 C ANISOU 1963 CD1 TRP A 240 7971 11856 8214 -3620 -199 3597 C ATOM 1964 CD2 TRP A 240 -17.580 1.879 11.317 1.00 84.63 C ANISOU 1964 CD2 TRP A 240 9421 13076 9657 -3139 -167 3292 C ATOM 1965 NE1 TRP A 240 -15.478 2.645 11.194 1.00 82.69 N ANISOU 1965 NE1 TRP A 240 8770 13094 9555 -3472 -101 3479 N ATOM 1966 CE2 TRP A 240 -16.227 1.553 11.544 1.00 81.14 C ANISOU 1966 CE2 TRP A 240 8631 12797 9403 -3172 -83 3301 C ATOM 1967 CE3 TRP A 240 -18.560 0.922 11.598 1.00 67.75 C ANISOU 1967 CE3 TRP A 240 7392 10810 7540 -2874 -154 3115 C ATOM 1968 CZ2 TRP A 240 -15.831 0.312 12.039 1.00 86.92 C ANISOU 1968 CZ2 TRP A 240 9133 13551 10342 -2927 -6 3154 C ATOM 1969 CZ3 TRP A 240 -18.164 -0.310 12.090 1.00 67.61 C ANISOU 1969 CZ3 TRP A 240 7169 10809 7709 -2654 -58 2971 C ATOM 1970 CH2 TRP A 240 -16.812 -0.603 12.305 1.00 83.09 C ANISOU 1970 CH2 TRP A 240 8796 12918 9856 -2671 5 2998 C ATOM 1971 N GLU A 241 -20.500 1.854 8.781 1.00 93.24 N ANISOU 1971 N GLU A 241 11101 14184 10144 -3102 -56 3158 N ATOM 1972 CA GLU A 241 -20.740 0.444 8.497 1.00 90.74 C ANISOU 1972 CA GLU A 241 10674 13954 9848 -2894 141 2904 C ATOM 1973 C GLU A 241 -20.747 0.151 7.000 1.00 86.67 C ANISOU 1973 C GLU A 241 10166 13701 9063 -2995 356 2832 C ATOM 1974 O GLU A 241 -20.504 -0.981 6.582 1.00 84.17 O ANISOU 1974 O GLU A 241 9697 13525 8760 -2884 596 2618 O ATOM 1975 CB GLU A 241 -22.063 -0.011 9.118 1.00 85.73 C ANISOU 1975 CB GLU A 241 10208 13074 9291 -2674 10 2774 C ATOM 1976 CG GLU A 241 -22.026 -0.138 10.632 1.00 92.66 C ANISOU 1976 CG GLU A 241 11068 13718 10422 -2535 -122 2774 C ATOM 1977 CD GLU A 241 -23.323 -0.674 11.202 1.00 97.31 C ANISOU 1977 CD GLU A 241 11813 14079 11084 -2335 -189 2627 C ATOM 1978 OE1 GLU A 241 -24.301 -0.810 10.436 1.00 98.49 O ANISOU 1978 OE1 GLU A 241 12073 14238 11111 -2312 -175 2537 O ATOM 1979 OE2 GLU A 241 -23.366 -0.962 12.417 1.00 94.08 O ANISOU 1979 OE2 GLU A 241 11414 13484 10848 -2212 -257 2601 O ATOM 1980 N GLN A 242 -21.026 1.170 6.195 1.00 86.14 N ANISOU 1980 N GLN A 242 10297 13689 8745 -3208 269 3009 N ATOM 1981 CA GLN A 242 -21.099 0.985 4.752 1.00 95.27 C ANISOU 1981 CA GLN A 242 11522 15098 9577 -3335 444 2963 C ATOM 1982 C GLN A 242 -19.863 1.525 4.037 1.00117.75 C ANISOU 1982 C GLN A 242 14262 18196 12282 -3612 643 3109 C ATOM 1983 O GLN A 242 -19.656 2.736 3.960 1.00116.61 O ANISOU 1983 O GLN A 242 14239 18012 12055 -3831 509 3375 O ATOM 1984 CB GLN A 242 -22.357 1.654 4.193 1.00 89.58 C ANISOU 1984 CB GLN A 242 11122 14285 8631 -3383 204 3065 C ATOM 1985 CG GLN A 242 -23.662 1.112 4.763 1.00 87.52 C ANISOU 1985 CG GLN A 242 10946 13799 8510 -3129 35 2899 C ATOM 1986 CD GLN A 242 -23.931 -0.327 4.360 1.00 97.32 C ANISOU 1986 CD GLN A 242 12089 15157 9731 -2973 243 2582 C ATOM 1987 OE1 GLN A 242 -23.407 -0.812 3.357 1.00111.56 O ANISOU 1987 OE1 GLN A 242 13838 17227 11324 -3070 483 2484 O ATOM 1988 NE2 GLN A 242 -24.752 -1.017 5.144 1.00 68.37 N ANISOU 1988 NE2 GLN A 242 8409 11283 6284 -2741 172 2410 N ATOM 1989 N GLY A 243 -19.048 0.614 3.515 1.00142.16 N ANISOU 1989 N GLY A 243 17121 21530 15363 -3604 981 2924 N ATOM 1990 CA GLY A 243 -17.938 0.982 2.655 1.00152.52 C ANISOU 1990 CA GLY A 243 18320 23119 16511 -3875 1246 3012 C ATOM 1991 C GLY A 243 -16.600 1.239 3.324 1.00155.89 C ANISOU 1991 C GLY A 243 18422 23581 17227 -3951 1335 3099 C ATOM 1992 O GLY A 243 -15.561 1.182 2.666 1.00161.51 O ANISOU 1992 O GLY A 243 18931 24548 17887 -4124 1644 3083 O ATOM 1993 N SER A 244 -16.611 1.524 4.622 1.00146.88 N ANISOU 1993 N SER A 244 17225 22195 16389 -3836 1072 3180 N ATOM 1994 CA SER A 244 -15.368 1.818 5.328 1.00141.35 C ANISOU 1994 CA SER A 244 16216 21519 15971 -3918 1092 3270 C ATOM 1995 C SER A 244 -14.894 0.621 6.147 1.00137.20 C ANISOU 1995 C SER A 244 15368 20968 15792 -3629 1162 3060 C ATOM 1996 O SER A 244 -13.934 -0.052 5.768 1.00140.11 O ANISOU 1996 O SER A 244 15412 21546 16277 -3615 1458 2930 O ATOM 1997 CB SER A 244 -15.539 3.040 6.233 1.00134.77 C ANISOU 1997 CB SER A 244 15539 20441 15228 -4029 740 3517 C ATOM 1998 OG SER A 244 -16.484 2.793 7.257 1.00132.87 O ANISOU 1998 OG SER A 244 15447 19919 15119 -3777 474 3454 O ATOM 1999 N ARG A 245 -15.576 0.364 7.261 1.00127.23 N ANISOU 1999 N ARG A 245 14205 19439 14699 -3400 897 3031 N ATOM 2000 CA ARG A 245 -15.258 -0.758 8.145 1.00116.76 C ANISOU 2000 CA ARG A 245 12638 18035 13688 -3112 908 2870 C ATOM 2001 C ARG A 245 -13.799 -0.749 8.598 1.00110.63 C ANISOU 2001 C ARG A 245 11460 17375 13198 -3164 959 2924 C ATOM 2002 O ARG A 245 -13.183 -1.803 8.754 1.00110.03 O ANISOU 2002 O ARG A 245 11081 17361 13362 -2967 1113 2768 O ATOM 2003 CB ARG A 245 -15.578 -2.088 7.455 1.00117.28 C ANISOU 2003 CB ARG A 245 12651 18189 13720 -2909 1183 2594 C ATOM 2004 CG ARG A 245 -17.051 -2.294 7.143 1.00109.43 C ANISOU 2004 CG ARG A 245 12007 17066 12504 -2821 1104 2503 C ATOM 2005 CD ARG A 245 -17.862 -2.503 8.410 1.00 95.89 C ANISOU 2005 CD ARG A 245 10433 15041 10961 -2608 830 2503 C ATOM 2006 NE ARG A 245 -19.266 -2.780 8.119 1.00 96.42 N ANISOU 2006 NE ARG A 245 10779 14988 10867 -2517 776 2390 N ATOM 2007 CZ ARG A 245 -20.168 -3.111 9.037 1.00103.72 C ANISOU 2007 CZ ARG A 245 11844 15654 11911 -2333 607 2339 C ATOM 2008 NH1 ARG A 245 -19.816 -3.210 10.311 1.00100.50 N ANISOU 2008 NH1 ARG A 245 11363 15079 11744 -2222 471 2401 N ATOM 2009 NH2 ARG A 245 -21.424 -3.345 8.680 1.00109.28 N ANISOU 2009 NH2 ARG A 245 12762 16272 12488 -2272 573 2226 N ATOM 2010 N LYS A 246 -13.253 0.444 8.809 1.00112.11 N ANISOU 2010 N LYS A 246 11635 17578 13385 -3430 818 3144 N ATOM 2011 CA LYS A 246 -11.860 0.583 9.217 1.00110.74 C ANISOU 2011 CA LYS A 246 11060 17525 13491 -3523 837 3207 C ATOM 2012 C LYS A 246 -11.743 1.081 10.653 1.00111.23 C ANISOU 2012 C LYS A 246 11144 17370 13749 -3504 447 3339 C ATOM 2013 O LYS A 246 -12.527 1.921 11.095 1.00 94.19 O ANISOU 2013 O LYS A 246 9331 15008 11449 -3586 197 3458 O ATOM 2014 CB LYS A 246 -11.119 1.534 8.274 1.00 96.04 C ANISOU 2014 CB LYS A 246 9111 15885 11496 -3895 1024 3341 C ATOM 2015 CG LYS A 246 -11.080 1.070 6.829 1.00 97.29 C ANISOU 2015 CG LYS A 246 9242 16297 11428 -3957 1440 3209 C ATOM 2016 CD LYS A 246 -10.370 2.081 5.943 1.00109.23 C ANISOU 2016 CD LYS A 246 10711 18015 12776 -4359 1629 3372 C ATOM 2017 CE LYS A 246 -10.341 1.619 4.496 1.00120.86 C ANISOU 2017 CE LYS A 246 12199 19754 13968 -4443 2060 3234 C ATOM 2018 NZ LYS A 246 -9.633 2.588 3.615 1.00122.82 N ANISOU 2018 NZ LYS A 246 12433 20200 14032 -4848 2273 3399 N ATOM 2019 N THR A 247 -10.758 0.556 11.376 1.00118.99 N ANISOU 2019 N THR A 247 11757 18396 15060 -3392 392 3312 N ATOM 2020 CA THR A 247 -10.505 0.972 12.750 1.00117.40 C ANISOU 2020 CA THR A 247 11554 18022 15031 -3390 11 3430 C ATOM 2021 C THR A 247 -9.979 2.403 12.789 1.00118.88 C ANISOU 2021 C THR A 247 11752 18236 15180 -3766 -123 3624 C ATOM 2022 O THR A 247 -10.414 3.214 13.608 1.00 83.82 O ANISOU 2022 O THR A 247 7585 13585 10677 -3857 -429 3733 O ATOM 2023 CB THR A 247 -9.496 0.041 13.446 1.00118.21 C ANISOU 2023 CB THR A 247 11229 18184 15502 -3183 -40 3370 C ATOM 2024 OG1 THR A 247 -8.253 0.063 12.733 1.00125.16 O ANISOU 2024 OG1 THR A 247 11649 19341 16565 -3328 203 3358 O ATOM 2025 CG2 THR A 247 -10.027 -1.383 13.486 1.00119.65 C ANISOU 2025 CG2 THR A 247 11426 18288 15748 -2806 79 3188 C ATOM 2026 N ASP A 248 -9.040 2.704 11.898 1.00120.83 N ANISOU 2026 N ASP A 248 11705 18735 15470 -3995 128 3656 N ATOM 2027 CA ASP A 248 -8.493 4.050 11.783 1.00117.90 C ANISOU 2027 CA ASP A 248 11331 18397 15068 -4389 54 3843 C ATOM 2028 C ASP A 248 -8.911 4.691 10.465 1.00119.18 C ANISOU 2028 C ASP A 248 11728 18646 14908 -4627 313 3912 C ATOM 2029 O ASP A 248 -8.687 4.131 9.392 1.00124.23 O ANISOU 2029 O ASP A 248 12222 19512 15468 -4620 680 3814 O ATOM 2030 CB ASP A 248 -6.968 4.025 11.895 1.00132.17 C ANISOU 2030 CB ASP A 248 12589 20421 17209 -4523 115 3857 C ATOM 2031 CG ASP A 248 -6.352 5.404 11.757 1.00144.61 C ANISOU 2031 CG ASP A 248 14140 22030 18775 -4964 59 4043 C ATOM 2032 OD1 ASP A 248 -6.990 6.389 12.187 1.00142.58 O ANISOU 2032 OD1 ASP A 248 14275 21544 18357 -5113 -199 4172 O ATOM 2033 OD2 ASP A 248 -5.231 5.504 11.217 1.00152.49 O ANISOU 2033 OD2 ASP A 248 14721 23271 19945 -5166 289 4053 O ATOM 2034 N PHE A 249 -9.521 5.868 10.555 1.00117.63 N ANISOU 2034 N PHE A 249 11912 18260 14523 -4837 117 4080 N ATOM 2035 CA PHE A 249 -9.981 6.584 9.372 1.00108.86 C ANISOU 2035 CA PHE A 249 11078 17190 13092 -5068 294 4196 C ATOM 2036 C PHE A 249 -9.869 8.091 9.564 1.00 92.51 C ANISOU 2036 C PHE A 249 9239 14926 10983 -5348 83 4376 C ATOM 2037 O PHE A 249 -9.410 8.562 10.606 1.00 92.75 O ANISOU 2037 O PHE A 249 9177 14833 11229 -5428 -174 4428 O ATOM 2038 CB PHE A 249 -11.426 6.199 9.040 1.00101.00 C ANISOU 2038 CB PHE A 249 10480 16061 11833 -4837 271 4124 C ATOM 2039 CG PHE A 249 -12.377 6.340 10.197 1.00 84.31 C ANISOU 2039 CG PHE A 249 8646 13622 9768 -4643 -86 4114 C ATOM 2040 CD1 PHE A 249 -13.000 7.550 10.459 1.00 83.55 C ANISOU 2040 CD1 PHE A 249 8901 13274 9571 -4803 -326 4279 C ATOM 2041 CD2 PHE A 249 -12.652 5.259 11.020 1.00 81.98 C ANISOU 2041 CD2 PHE A 249 8267 13258 9623 -4303 -164 3937 C ATOM 2042 CE1 PHE A 249 -13.875 7.681 11.521 1.00 80.56 C ANISOU 2042 CE1 PHE A 249 8772 12597 9241 -4628 -613 4241 C ATOM 2043 CE2 PHE A 249 -13.526 5.385 12.084 1.00 78.98 C ANISOU 2043 CE2 PHE A 249 8156 12587 9266 -4147 -454 3921 C ATOM 2044 CZ PHE A 249 -14.138 6.597 12.334 1.00 78.29 C ANISOU 2044 CZ PHE A 249 8403 12266 9076 -4310 -666 4060 C ATOM 2045 N SER A 250 -10.289 8.843 8.553 1.00 93.55 N ANISOU 2045 N SER A 250 9696 15006 10843 -5456 174 4437 N ATOM 2046 CA SER A 250 -10.260 10.298 8.620 1.00110.65 C ANISOU 2046 CA SER A 250 12125 16943 12973 -5664 -14 4576 C ATOM 2047 C SER A 250 -11.614 10.849 9.047 1.00104.72 C ANISOU 2047 C SER A 250 11826 15861 12102 -5543 -310 4628 C ATOM 2048 O SER A 250 -12.653 10.440 8.528 1.00103.61 O ANISOU 2048 O SER A 250 11909 15699 11761 -5375 -276 4594 O ATOM 2049 CB SER A 250 -9.850 10.890 7.271 1.00 98.73 C ANISOU 2049 CB SER A 250 10695 15550 11269 -5865 248 4634 C ATOM 2050 OG SER A 250 -9.892 12.306 7.301 1.00100.26 O ANISOU 2050 OG SER A 250 11161 15500 11434 -6056 67 4780 O ATOM 2051 N THR A 251 -11.595 11.779 9.996 1.00118.51 N ANISOU 2051 N THR A 251 13695 17347 13985 -5629 -596 4690 N ATOM 2052 CA THR A 251 -12.819 12.383 10.507 1.00120.46 C ANISOU 2052 CA THR A 251 14344 17251 14173 -5509 -867 4709 C ATOM 2053 C THR A 251 -13.468 13.273 9.449 1.00124.27 C ANISOU 2053 C THR A 251 15162 17611 14444 -5555 -846 4798 C ATOM 2054 O THR A 251 -14.693 13.385 9.384 1.00126.29 O ANISOU 2054 O THR A 251 15709 17675 14602 -5379 -971 4785 O ATOM 2055 CB THR A 251 -12.548 13.211 11.779 1.00122.09 C ANISOU 2055 CB THR A 251 14602 17211 14577 -5614 -1154 4727 C ATOM 2056 OG1 THR A 251 -11.757 12.441 12.694 1.00119.32 O ANISOU 2056 OG1 THR A 251 13905 17004 14426 -5617 -1195 4670 O ATOM 2057 CG2 THR A 251 -13.853 13.606 12.452 1.00124.73 C ANISOU 2057 CG2 THR A 251 15310 17198 14885 -5441 -1395 4690 C ATOM 2058 N ALA A 252 -12.638 13.898 8.619 1.00122.27 N ANISOU 2058 N ALA A 252 14854 17468 14137 -5792 -688 4891 N ATOM 2059 CA ALA A 252 -13.127 14.767 7.554 1.00118.91 C ANISOU 2059 CA ALA A 252 14736 16937 13505 -5868 -666 5009 C ATOM 2060 C ALA A 252 -13.891 13.969 6.502 1.00113.89 C ANISOU 2060 C ALA A 252 14199 16465 12609 -5712 -514 4973 C ATOM 2061 O ALA A 252 -14.867 14.453 5.929 1.00106.57 O ANISOU 2061 O ALA A 252 13586 15381 11523 -5644 -623 5041 O ATOM 2062 CB ALA A 252 -11.972 15.521 6.913 1.00123.50 C ANISOU 2062 CB ALA A 252 15223 17618 14085 -6177 -494 5118 C ATOM 2063 N GLN A 253 -13.438 12.744 6.253 1.00113.23 N ANISOU 2063 N GLN A 253 13833 16694 12494 -5657 -269 4861 N ATOM 2064 CA GLN A 253 -14.103 11.853 5.310 1.00102.46 C ANISOU 2064 CA GLN A 253 12541 15511 10880 -5517 -106 4790 C ATOM 2065 C GLN A 253 -15.479 11.444 5.827 1.00103.04 C ANISOU 2065 C GLN A 253 12805 15399 10947 -5242 -330 4724 C ATOM 2066 O GLN A 253 -16.463 11.459 5.086 1.00 89.57 O ANISOU 2066 O GLN A 253 11349 13651 9031 -5151 -377 4740 O ATOM 2067 CB GLN A 253 -13.249 10.610 5.053 1.00 97.02 C ANISOU 2067 CB GLN A 253 11473 15180 10208 -5510 226 4651 C ATOM 2068 CG GLN A 253 -11.926 10.880 4.354 1.00101.66 C ANISOU 2068 CG GLN A 253 11847 15985 10795 -5767 518 4682 C ATOM 2069 CD GLN A 253 -12.047 10.880 2.843 1.00102.09 C ANISOU 2069 CD GLN A 253 12079 16207 10504 -5860 766 4700 C ATOM 2070 OE1 GLN A 253 -13.148 10.838 2.296 1.00137.99 O ANISOU 2070 OE1 GLN A 253 16937 20688 14805 -5750 664 4718 O ATOM 2071 NE2 GLN A 253 -10.909 10.918 2.159 1.00106.25 N ANISOU 2071 NE2 GLN A 253 12403 16952 11014 -6067 1092 4690 N ATOM 2072 N GLY A 254 -15.537 11.079 7.104 1.00102.53 N ANISOU 2072 N GLY A 254 12619 15224 11115 -5118 -470 4651 N ATOM 2073 CA GLY A 254 -16.773 10.639 7.724 1.00 91.58 C ANISOU 2073 CA GLY A 254 11387 13653 9755 -4862 -650 4572 C ATOM 2074 C GLY A 254 -17.791 11.752 7.884 1.00 94.63 C ANISOU 2074 C GLY A 254 12119 13687 10150 -4811 -925 4642 C ATOM 2075 O GLY A 254 -18.981 11.552 7.645 1.00 88.65 O ANISOU 2075 O GLY A 254 11548 12826 9307 -4630 -1015 4605 O ATOM 2076 N PHE A 255 -17.322 12.928 8.289 1.00107.56 N ANISOU 2076 N PHE A 255 13823 15136 11911 -4972 -1055 4736 N ATOM 2077 CA PHE A 255 -18.200 14.076 8.483 1.00100.76 C ANISOU 2077 CA PHE A 255 13267 13918 11100 -4932 -1298 4797 C ATOM 2078 C PHE A 255 -18.806 14.525 7.158 1.00114.38 C ANISOU 2078 C PHE A 255 15205 15644 12610 -4947 -1289 4908 C ATOM 2079 O PHE A 255 -19.937 15.010 7.113 1.00124.98 O ANISOU 2079 O PHE A 255 16780 16741 13967 -4809 -1475 4931 O ATOM 2080 CB PHE A 255 -17.438 15.229 9.139 1.00 90.58 C ANISOU 2080 CB PHE A 255 11992 12444 9978 -5134 -1408 4870 C ATOM 2081 CG PHE A 255 -18.306 16.399 9.508 1.00 86.80 C ANISOU 2081 CG PHE A 255 11811 11572 9598 -5083 -1645 4908 C ATOM 2082 CD1 PHE A 255 -19.202 16.308 10.560 1.00 83.97 C ANISOU 2082 CD1 PHE A 255 11554 10968 9383 -4881 -1809 4785 C ATOM 2083 CD2 PHE A 255 -18.218 17.592 8.810 1.00 90.12 C ANISOU 2083 CD2 PHE A 255 12409 11857 9978 -5240 -1686 5066 C ATOM 2084 CE1 PHE A 255 -20.001 17.382 10.905 1.00 84.46 C ANISOU 2084 CE1 PHE A 255 11870 10660 9560 -4827 -1997 4803 C ATOM 2085 CE2 PHE A 255 -19.013 18.671 9.151 1.00 93.94 C ANISOU 2085 CE2 PHE A 255 13150 11962 10581 -5182 -1894 5103 C ATOM 2086 CZ PHE A 255 -19.906 18.566 10.200 1.00 87.78 C ANISOU 2086 CZ PHE A 255 12451 10943 9959 -4972 -2045 4963 C ATOM 2087 N GLN A 256 -18.047 14.358 6.080 1.00115.89 N ANISOU 2087 N GLN A 256 15313 16114 12608 -5118 -1069 4978 N ATOM 2088 CA GLN A 256 -18.533 14.670 4.742 1.00118.94 C ANISOU 2088 CA GLN A 256 15909 16548 12737 -5156 -1044 5090 C ATOM 2089 C GLN A 256 -19.581 13.653 4.305 1.00111.33 C ANISOU 2089 C GLN A 256 14992 15691 11617 -4938 -1045 4989 C ATOM 2090 O GLN A 256 -20.584 14.004 3.683 1.00106.89 O ANISOU 2090 O GLN A 256 14663 15011 10939 -4857 -1198 5059 O ATOM 2091 CB GLN A 256 -17.375 14.700 3.742 1.00129.54 C ANISOU 2091 CB GLN A 256 17151 18173 13896 -5414 -768 5169 C ATOM 2092 CG GLN A 256 -17.793 14.949 2.299 1.00133.15 C ANISOU 2092 CG GLN A 256 17842 18713 14035 -5480 -721 5287 C ATOM 2093 CD GLN A 256 -18.226 16.381 2.049 1.00136.56 C ANISOU 2093 CD GLN A 256 18570 18834 14483 -5554 -945 5490 C ATOM 2094 OE1 GLN A 256 -17.947 17.275 2.847 1.00143.63 O ANISOU 2094 OE1 GLN A 256 19478 19481 15614 -5617 -1071 5543 O ATOM 2095 NE2 GLN A 256 -18.911 16.604 0.934 1.00137.47 N ANISOU 2095 NE2 GLN A 256 18929 18959 14343 -5549 -1002 5604 N ATOM 2096 N THR A 257 -19.340 12.390 4.644 1.00108.46 N ANISOU 2096 N THR A 257 14398 15547 11264 -4846 -883 4830 N ATOM 2097 CA THR A 257 -20.242 11.303 4.280 1.00 89.68 C ANISOU 2097 CA THR A 257 12039 13293 8742 -4656 -852 4713 C ATOM 2098 C THR A 257 -21.595 11.453 4.970 1.00 86.75 C ANISOU 2098 C THR A 257 11826 12617 8517 -4424 -1131 4677 C ATOM 2099 O THR A 257 -22.636 11.164 4.383 1.00107.94 O ANISOU 2099 O THR A 257 14647 15301 11065 -4303 -1218 4662 O ATOM 2100 CB THR A 257 -19.639 9.930 4.640 1.00 91.95 C ANISOU 2100 CB THR A 257 12029 13849 9058 -4604 -607 4548 C ATOM 2101 OG1 THR A 257 -18.325 9.820 4.078 1.00109.45 O ANISOU 2101 OG1 THR A 257 14051 16337 11196 -4814 -327 4564 O ATOM 2102 CG2 THR A 257 -20.509 8.802 4.106 1.00 92.32 C ANISOU 2102 CG2 THR A 257 12107 14051 8918 -4444 -540 4422 C ATOM 2103 N VAL A 258 -21.573 11.912 6.216 1.00 86.88 N ANISOU 2103 N VAL A 258 11821 12378 8810 -4372 -1267 4655 N ATOM 2104 CA VAL A 258 -22.798 12.086 6.988 1.00 89.19 C ANISOU 2104 CA VAL A 258 12251 12363 9275 -4157 -1493 4598 C ATOM 2105 C VAL A 258 -23.643 13.236 6.442 1.00 99.57 C ANISOU 2105 C VAL A 258 13820 13431 10581 -4146 -1710 4733 C ATOM 2106 O VAL A 258 -24.862 13.114 6.311 1.00102.00 O ANISOU 2106 O VAL A 258 14241 13616 10900 -3969 -1856 4710 O ATOM 2107 CB VAL A 258 -22.491 12.337 8.479 1.00 76.73 C ANISOU 2107 CB VAL A 258 10611 10573 7970 -4130 -1565 4528 C ATOM 2108 CG1 VAL A 258 -23.757 12.711 9.235 1.00 74.97 C ANISOU 2108 CG1 VAL A 258 10559 10002 7925 -3932 -1774 4468 C ATOM 2109 CG2 VAL A 258 -21.840 11.110 9.098 1.00 74.77 C ANISOU 2109 CG2 VAL A 258 10118 10540 7753 -4098 -1396 4408 C ATOM 2110 N LEU A 259 -22.988 14.346 6.112 1.00 96.88 N ANISOU 2110 N LEU A 259 13560 13018 10233 -4340 -1733 4882 N ATOM 2111 CA LEU A 259 -23.690 15.532 5.630 1.00 98.98 C ANISOU 2111 CA LEU A 259 14070 13023 10515 -4341 -1941 5037 C ATOM 2112 C LEU A 259 -24.354 15.313 4.272 1.00104.83 C ANISOU 2112 C LEU A 259 14933 13906 10990 -4316 -1975 5127 C ATOM 2113 O LEU A 259 -25.407 15.886 3.995 1.00112.50 O ANISOU 2113 O LEU A 259 16081 14660 12005 -4201 -2200 5211 O ATOM 2114 CB LEU A 259 -22.733 16.723 5.549 1.00 88.96 C ANISOU 2114 CB LEU A 259 12861 11657 9282 -4580 -1930 5186 C ATOM 2115 CG LEU A 259 -22.324 17.360 6.878 1.00 88.08 C ANISOU 2115 CG LEU A 259 12718 11297 9452 -4613 -1998 5130 C ATOM 2116 CD1 LEU A 259 -21.536 18.634 6.633 1.00 91.82 C ANISOU 2116 CD1 LEU A 259 13290 11649 9949 -4857 -2014 5298 C ATOM 2117 CD2 LEU A 259 -23.546 17.640 7.739 1.00 86.08 C ANISOU 2117 CD2 LEU A 259 12585 10698 9424 -4380 -2205 5046 C ATOM 2118 N GLU A 260 -23.741 14.489 3.428 1.00106.15 N ANISOU 2118 N GLU A 260 15008 14440 10886 -4424 -1756 5106 N ATOM 2119 CA GLU A 260 -24.297 14.227 2.105 1.00116.23 C ANISOU 2119 CA GLU A 260 16418 15885 11859 -4428 -1778 5175 C ATOM 2120 C GLU A 260 -25.503 13.297 2.200 1.00123.01 C ANISOU 2120 C GLU A 260 17263 16760 12714 -4190 -1889 5041 C ATOM 2121 O GLU A 260 -26.329 13.243 1.289 1.00131.57 O ANISOU 2121 O GLU A 260 18489 17887 13613 -4143 -2025 5100 O ATOM 2122 CB GLU A 260 -23.238 13.628 1.173 1.00119.40 C ANISOU 2122 CB GLU A 260 16736 16675 11954 -4633 -1475 5167 C ATOM 2123 CG GLU A 260 -22.988 12.143 1.374 1.00118.13 C ANISOU 2123 CG GLU A 260 16350 16805 11728 -4563 -1248 4952 C ATOM 2124 CD GLU A 260 -22.099 11.551 0.299 1.00118.57 C ANISOU 2124 CD GLU A 260 16346 17242 11464 -4750 -937 4927 C ATOM 2125 OE1 GLU A 260 -21.983 10.308 0.240 1.00117.01 O ANISOU 2125 OE1 GLU A 260 15989 17299 11169 -4693 -737 4745 O ATOM 2126 OE2 GLU A 260 -21.516 12.327 -0.488 1.00115.18 O ANISOU 2126 OE2 GLU A 260 16032 16851 10882 -4956 -874 5081 O ATOM 2127 N LEU A 261 -25.601 12.567 3.308 1.00112.98 N ANISOU 2127 N LEU A 261 15827 15454 11645 -4050 -1840 4868 N ATOM 2128 CA LEU A 261 -26.730 11.674 3.538 1.00107.20 C ANISOU 2128 CA LEU A 261 15070 14716 10944 -3831 -1933 4737 C ATOM 2129 C LEU A 261 -27.964 12.456 3.973 1.00104.18 C ANISOU 2129 C LEU A 261 14822 13959 10801 -3657 -2242 4792 C ATOM 2130 O LEU A 261 -29.094 12.032 3.734 1.00104.60 O ANISOU 2130 O LEU A 261 14911 13990 10841 -3500 -2398 4756 O ATOM 2131 CB LEU A 261 -26.379 10.617 4.588 1.00 94.88 C ANISOU 2131 CB LEU A 261 13300 13236 9515 -3749 -1757 4548 C ATOM 2132 CG LEU A 261 -25.399 9.524 4.156 1.00 87.34 C ANISOU 2132 CG LEU A 261 12172 12669 8345 -3859 -1447 4455 C ATOM 2133 CD1 LEU A 261 -25.090 8.591 5.316 1.00 77.80 C ANISOU 2133 CD1 LEU A 261 10762 11480 7319 -3760 -1310 4300 C ATOM 2134 CD2 LEU A 261 -25.950 8.746 2.970 1.00 89.22 C ANISOU 2134 CD2 LEU A 261 12470 13167 8261 -3852 -1410 4411 C ATOM 2135 N VAL A 262 -27.739 13.601 4.611 1.00101.47 N ANISOU 2135 N VAL A 262 14543 13323 10687 -3690 -2330 4874 N ATOM 2136 CA VAL A 262 -28.831 14.461 5.052 1.00102.84 C ANISOU 2136 CA VAL A 262 14841 13112 11120 -3531 -2598 4927 C ATOM 2137 C VAL A 262 -29.608 14.988 3.849 1.00107.60 C ANISOU 2137 C VAL A 262 15610 13687 11587 -3513 -2817 5099 C ATOM 2138 O VAL A 262 -30.828 15.145 3.900 1.00113.77 O ANISOU 2138 O VAL A 262 16442 14266 12521 -3323 -3054 5112 O ATOM 2139 CB VAL A 262 -28.312 15.644 5.894 1.00116.14 C ANISOU 2139 CB VAL A 262 16582 14500 13045 -3605 -2626 4976 C ATOM 2140 CG1 VAL A 262 -29.473 16.451 6.458 1.00117.75 C ANISOU 2140 CG1 VAL A 262 16901 14288 13550 -3419 -2872 4996 C ATOM 2141 CG2 VAL A 262 -27.417 15.142 7.017 1.00116.23 C ANISOU 2141 CG2 VAL A 262 16437 14574 13153 -3653 -2431 4819 C ATOM 2142 N LEU A 263 -28.888 15.249 2.762 1.00101.42 N ANISOU 2142 N LEU A 263 14908 13110 10518 -3714 -2738 5236 N ATOM 2143 CA LEU A 263 -29.499 15.721 1.526 1.00 98.79 C ANISOU 2143 CA LEU A 263 14756 12786 9995 -3728 -2935 5416 C ATOM 2144 C LEU A 263 -30.156 14.570 0.769 1.00109.12 C ANISOU 2144 C LEU A 263 16031 14374 11053 -3652 -2962 5327 C ATOM 2145 O LEU A 263 -31.054 14.779 -0.048 1.00129.52 O ANISOU 2145 O LEU A 263 18740 16931 13540 -3583 -3206 5430 O ATOM 2146 CB LEU A 263 -28.452 16.404 0.645 1.00103.25 C ANISOU 2146 CB LEU A 263 15443 13469 10318 -3993 -2817 5596 C ATOM 2147 CG LEU A 263 -27.559 17.434 1.341 1.00 96.71 C ANISOU 2147 CG LEU A 263 14626 12428 9692 -4124 -2745 5668 C ATOM 2148 CD1 LEU A 263 -26.545 18.014 0.366 1.00111.33 C ANISOU 2148 CD1 LEU A 263 16593 14425 11281 -4401 -2614 5853 C ATOM 2149 CD2 LEU A 263 -28.393 18.538 1.972 1.00 97.30 C ANISOU 2149 CD2 LEU A 263 14811 12054 10105 -3977 -3015 5749 C ATOM 2150 N LYS A 264 -29.699 13.355 1.053 1.00 97.84 N ANISOU 2150 N LYS A 264 14435 13214 9526 -3665 -2720 5132 N ATOM 2151 CA LYS A 264 -30.210 12.151 0.405 1.00 88.65 C ANISOU 2151 CA LYS A 264 13230 12341 8111 -3615 -2704 5008 C ATOM 2152 C LYS A 264 -31.376 11.539 1.177 1.00 85.66 C ANISOU 2152 C LYS A 264 12751 11827 7969 -3367 -2868 4867 C ATOM 2153 O LYS A 264 -31.819 10.436 0.859 1.00102.25 O ANISOU 2153 O LYS A 264 14788 14156 9905 -3315 -2852 4727 O ATOM 2154 CB LYS A 264 -29.098 11.112 0.242 1.00 87.62 C ANISOU 2154 CB LYS A 264 12970 12578 7742 -3762 -2338 4867 C ATOM 2155 CG LYS A 264 -28.056 11.464 -0.809 1.00 91.24 C ANISOU 2155 CG LYS A 264 13524 13253 7890 -4015 -2157 4983 C ATOM 2156 CD LYS A 264 -27.038 10.344 -0.963 1.00 90.42 C ANISOU 2156 CD LYS A 264 13259 13514 7583 -4134 -1781 4814 C ATOM 2157 CE LYS A 264 -25.999 10.675 -2.022 1.00102.54 C ANISOU 2157 CE LYS A 264 14878 15267 8814 -4392 -1570 4916 C ATOM 2158 NZ LYS A 264 -25.011 9.573 -2.188 1.00108.69 N ANISOU 2158 NZ LYS A 264 15475 16399 9425 -4496 -1179 4733 N ATOM 2159 N HIS A 265 -31.845 12.252 2.199 1.00 84.40 N ANISOU 2159 N HIS A 265 12579 11295 8192 -3228 -3012 4892 N ATOM 2160 CA HIS A 265 -32.859 11.750 3.129 1.00 86.16 C ANISOU 2160 CA HIS A 265 12696 11344 8696 -3001 -3130 4758 C ATOM 2161 C HIS A 265 -34.063 11.096 2.448 1.00105.08 C ANISOU 2161 C HIS A 265 15078 13850 10999 -2870 -3364 4713 C ATOM 2162 O HIS A 265 -34.567 10.078 2.918 1.00117.54 O ANISOU 2162 O HIS A 265 16482 15486 12692 -2721 -3285 4447 O ATOM 2163 CB HIS A 265 -33.343 12.887 4.034 1.00 81.63 C ANISOU 2163 CB HIS A 265 12168 10318 8528 -2878 -3300 4828 C ATOM 2164 CG HIS A 265 -33.991 14.017 3.296 1.00 90.36 C ANISOU 2164 CG HIS A 265 13423 11224 9687 -2841 -3595 5026 C ATOM 2165 ND1 HIS A 265 -33.272 14.947 2.577 1.00 99.29 N ANISOU 2165 ND1 HIS A 265 14704 12365 10657 -3021 -3582 5212 N ATOM 2166 CD2 HIS A 265 -35.293 14.368 3.168 1.00 92.05 C ANISOU 2166 CD2 HIS A 265 13649 11213 10114 -2640 -3918 5076 C ATOM 2167 CE1 HIS A 265 -34.102 15.821 2.036 1.00104.20 C ANISOU 2167 CE1 HIS A 265 15445 12774 11372 -2932 -3882 5377 C ATOM 2168 NE2 HIS A 265 -35.334 15.492 2.380 1.00100.93 N ANISOU 2168 NE2 HIS A 265 14938 12216 11197 -2694 -4095 5294 N ATOM 2169 N GLN A 266 -34.516 11.672 1.339 1.00114.95 N ANISOU 2169 N GLN A 266 16460 15114 12102 -2892 -3594 4861 N ATOM 2170 CA GLN A 266 -35.648 11.117 0.604 1.00 91.74 C ANISOU 2170 CA GLN A 266 13502 12292 9064 -2782 -3858 4814 C ATOM 2171 C GLN A 266 -35.322 9.747 0.010 1.00 92.62 C ANISOU 2171 C GLN A 266 13561 12839 8790 -2889 -3671 4636 C ATOM 2172 O GLN A 266 -36.220 8.963 -0.294 1.00112.65 O ANISOU 2172 O GLN A 266 16005 15491 11305 -2780 -3811 4463 O ATOM 2173 CB GLN A 266 -36.085 12.073 -0.506 1.00 92.20 C ANISOU 2173 CB GLN A 266 13735 12283 9016 -2803 -4139 5029 C ATOM 2174 CG GLN A 266 -34.999 12.381 -1.522 1.00105.92 C ANISOU 2174 CG GLN A 266 15651 14247 10347 -3063 -3958 5162 C ATOM 2175 CD GLN A 266 -35.554 12.973 -2.801 1.00128.22 C ANISOU 2175 CD GLN A 266 18662 17093 12961 -3090 -4247 5351 C ATOM 2176 OE1 GLN A 266 -36.757 12.913 -3.053 1.00133.58 O ANISOU 2176 OE1 GLN A 266 19308 17697 13748 -2917 -4581 5344 O ATOM 2177 NE2 GLN A 266 -34.679 13.548 -3.618 1.00131.15 N ANISOU 2177 NE2 GLN A 266 19223 17569 13039 -3308 -4127 5522 N ATOM 2178 N LYS A 267 -34.034 9.472 -0.164 1.00 89.69 N ANISOU 2178 N LYS A 267 13215 12696 8168 -3090 -3321 4617 N ATOM 2179 CA LYS A 267 -33.585 8.205 -0.732 1.00 88.25 C ANISOU 2179 CA LYS A 267 12988 12924 7619 -3205 -3088 4437 C ATOM 2180 C LYS A 267 -33.192 7.202 0.357 1.00 81.67 C ANISOU 2180 C LYS A 267 11898 12094 7038 -3088 -2743 4103 C ATOM 2181 O LYS A 267 -32.862 6.053 0.064 1.00 85.31 O ANISOU 2181 O LYS A 267 12257 12823 7333 -3111 -2489 3848 O ATOM 2182 CB LYS A 267 -32.406 8.453 -1.679 1.00 88.96 C ANISOU 2182 CB LYS A 267 13201 13242 7356 -3452 -2845 4525 C ATOM 2183 CG LYS A 267 -32.103 7.320 -2.647 1.00101.25 C ANISOU 2183 CG LYS A 267 14774 15225 8473 -3585 -2649 4353 C ATOM 2184 CD LYS A 267 -30.904 7.660 -3.517 1.00119.02 C ANISOU 2184 CD LYS A 267 17139 17669 10416 -3829 -2387 4447 C ATOM 2185 CE LYS A 267 -30.586 6.541 -4.491 1.00132.15 C ANISOU 2185 CE LYS A 267 18826 19745 11638 -3964 -2155 4247 C ATOM 2186 NZ LYS A 267 -29.410 6.875 -5.341 1.00134.05 N ANISOU 2186 NZ LYS A 267 19172 20171 11592 -4205 -1875 4331 N ATOM 2187 N LEU A 268 -33.249 7.633 1.613 1.00 80.65 N ANISOU 2187 N LEU A 268 11675 11647 7321 -2953 -2732 4087 N ATOM 2188 CA LEU A 268 -32.706 6.839 2.714 1.00 80.32 C ANISOU 2188 CA LEU A 268 11429 11585 7502 -2865 -2411 3825 C ATOM 2189 C LEU A 268 -33.705 5.890 3.368 1.00 74.31 C ANISOU 2189 C LEU A 268 10481 10723 7029 -2618 -2388 3488 C ATOM 2190 O LEU A 268 -34.707 6.317 3.941 1.00 72.69 O ANISOU 2190 O LEU A 268 10248 10235 7134 -2450 -2584 3467 O ATOM 2191 CB LEU A 268 -32.124 7.760 3.788 1.00 76.70 C ANISOU 2191 CB LEU A 268 10991 10858 7295 -2886 -2384 3972 C ATOM 2192 CG LEU A 268 -30.838 8.506 3.433 1.00 86.85 C ANISOU 2192 CG LEU A 268 12395 12246 8358 -3156 -2294 4248 C ATOM 2193 CD1 LEU A 268 -30.292 9.209 4.662 1.00 74.55 C ANISOU 2193 CD1 LEU A 268 10815 10420 7088 -3163 -2253 4309 C ATOM 2194 CD2 LEU A 268 -29.806 7.554 2.850 1.00 93.35 C ANISOU 2194 CD2 LEU A 268 13126 13454 8890 -3298 -1973 4137 C ATOM 2195 N CYS A 269 -33.409 4.597 3.284 1.00 75.12 N ANISOU 2195 N CYS A 269 10452 11046 7043 -2600 -2125 3217 N ATOM 2196 CA CYS A 269 -34.145 3.580 4.021 1.00 69.58 C ANISOU 2196 CA CYS A 269 9572 10246 6620 -2396 -2026 2890 C ATOM 2197 C CYS A 269 -33.148 2.718 4.793 1.00 70.55 C ANISOU 2197 C CYS A 269 9569 10427 6808 -2383 -1669 2726 C ATOM 2198 O CYS A 269 -32.367 1.978 4.196 1.00 67.83 O ANISOU 2198 O CYS A 269 9190 10349 6231 -2477 -1457 2645 O ATOM 2199 CB CYS A 269 -34.988 2.727 3.071 1.00 71.03 C ANISOU 2199 CB CYS A 269 9719 10611 6657 -2369 -2103 2694 C ATOM 2200 SG CYS A 269 -36.040 1.503 3.880 1.00 71.33 S ANISOU 2200 SG CYS A 269 9539 10507 7056 -2146 -1997 2295 S ATOM 2201 N ILE A 270 -33.179 2.815 6.121 1.00 71.83 N ANISOU 2201 N ILE A 270 9669 10336 7287 -2264 -1608 2676 N ATOM 2202 CA ILE A 270 -32.171 2.170 6.963 1.00 67.46 C ANISOU 2202 CA ILE A 270 9017 9806 6807 -2252 -1330 2583 C ATOM 2203 C ILE A 270 -32.789 1.399 8.129 1.00 60.49 C ANISOU 2203 C ILE A 270 8036 8717 6229 -2060 -1223 2345 C ATOM 2204 O ILE A 270 -33.651 1.917 8.839 1.00 60.59 O ANISOU 2204 O ILE A 270 8079 8470 6471 -1963 -1349 2339 O ATOM 2205 CB ILE A 270 -31.173 3.203 7.537 1.00 62.92 C ANISOU 2205 CB ILE A 270 8508 9148 6251 -2367 -1345 2826 C ATOM 2206 CG1 ILE A 270 -30.568 4.057 6.420 1.00 65.54 C ANISOU 2206 CG1 ILE A 270 8955 9655 6290 -2585 -1437 3090 C ATOM 2207 CG2 ILE A 270 -30.073 2.509 8.325 1.00 70.36 C ANISOU 2207 CG2 ILE A 270 9328 10148 7259 -2359 -1098 2742 C ATOM 2208 CD1 ILE A 270 -29.638 5.140 6.917 1.00 65.90 C ANISOU 2208 CD1 ILE A 270 9066 9603 6370 -2728 -1466 3332 C ATOM 2209 N PHE A 271 -32.337 0.164 8.327 1.00 59.51 N ANISOU 2209 N PHE A 271 7800 8698 6112 -2009 -977 2151 N ATOM 2210 CA PHE A 271 -32.802 -0.651 9.444 1.00 58.46 C ANISOU 2210 CA PHE A 271 7599 8374 6240 -1850 -846 1947 C ATOM 2211 C PHE A 271 -31.706 -1.600 9.921 1.00 76.01 C ANISOU 2211 C PHE A 271 9734 10677 8469 -1827 -597 1875 C ATOM 2212 O PHE A 271 -30.815 -1.968 9.154 1.00 84.46 O ANISOU 2212 O PHE A 271 10746 11987 9359 -1906 -485 1886 O ATOM 2213 CB PHE A 271 -34.055 -1.441 9.051 1.00 60.57 C ANISOU 2213 CB PHE A 271 7808 8619 6588 -1757 -854 1709 C ATOM 2214 CG PHE A 271 -33.794 -2.566 8.087 1.00 62.35 C ANISOU 2214 CG PHE A 271 7963 9088 6641 -1787 -706 1538 C ATOM 2215 CD1 PHE A 271 -33.628 -2.315 6.734 1.00 73.79 C ANISOU 2215 CD1 PHE A 271 9456 10787 7794 -1917 -799 1603 C ATOM 2216 CD2 PHE A 271 -33.731 -3.877 8.531 1.00 57.77 C ANISOU 2216 CD2 PHE A 271 7293 8473 6185 -1693 -468 1308 C ATOM 2217 CE1 PHE A 271 -33.393 -3.350 5.845 1.00 62.24 C ANISOU 2217 CE1 PHE A 271 7947 9547 6154 -1956 -641 1413 C ATOM 2218 CE2 PHE A 271 -33.497 -4.915 7.647 1.00 58.96 C ANISOU 2218 CE2 PHE A 271 7385 8820 6198 -1718 -317 1123 C ATOM 2219 CZ PHE A 271 -33.328 -4.650 6.303 1.00 61.16 C ANISOU 2219 CZ PHE A 271 7706 9359 6173 -1852 -396 1161 C ATOM 2220 N TRP A 272 -31.776 -1.993 11.190 1.00 66.43 N ANISOU 2220 N TRP A 272 8514 9260 7466 -1718 -510 1803 N ATOM 2221 CA TRP A 272 -30.792 -2.907 11.761 1.00 60.73 C ANISOU 2221 CA TRP A 272 7713 8576 6787 -1669 -313 1755 C ATOM 2222 C TRP A 272 -31.435 -4.178 12.306 1.00 56.34 C ANISOU 2222 C TRP A 272 7123 7884 6401 -1523 -152 1524 C ATOM 2223 O TRP A 272 -32.439 -4.130 13.016 1.00 71.70 O ANISOU 2223 O TRP A 272 9132 9611 8499 -1458 -178 1450 O ATOM 2224 CB TRP A 272 -29.994 -2.215 12.867 1.00 63.53 C ANISOU 2224 CB TRP A 272 8118 8821 7199 -1700 -370 1933 C ATOM 2225 CG TRP A 272 -28.926 -1.303 12.352 1.00 57.66 C ANISOU 2225 CG TRP A 272 7357 8247 6303 -1860 -451 2147 C ATOM 2226 CD1 TRP A 272 -27.669 -1.656 11.958 1.00 56.08 C ANISOU 2226 CD1 TRP A 272 7023 8263 6023 -1919 -337 2195 C ATOM 2227 CD2 TRP A 272 -29.018 0.115 12.177 1.00 57.31 C ANISOU 2227 CD2 TRP A 272 7424 8157 6193 -1989 -648 2340 C ATOM 2228 NE1 TRP A 272 -26.972 -0.546 11.547 1.00 57.31 N ANISOU 2228 NE1 TRP A 272 7196 8523 6055 -2097 -439 2406 N ATOM 2229 CE2 TRP A 272 -27.779 0.554 11.672 1.00 72.31 C ANISOU 2229 CE2 TRP A 272 9262 10256 7956 -2145 -637 2506 C ATOM 2230 CE3 TRP A 272 -30.029 1.056 12.398 1.00 56.65 C ANISOU 2230 CE3 TRP A 272 7480 7867 6179 -1985 -824 2385 C ATOM 2231 CZ2 TRP A 272 -27.523 1.893 11.384 1.00 75.74 C ANISOU 2231 CZ2 TRP A 272 9792 10680 8305 -2315 -798 2728 C ATOM 2232 CZ3 TRP A 272 -29.773 2.383 12.112 1.00 57.67 C ANISOU 2232 CZ3 TRP A 272 7703 7973 6236 -2128 -995 2603 C ATOM 2233 CH2 TRP A 272 -28.531 2.790 11.610 1.00 70.54 C ANISOU 2233 CH2 TRP A 272 9293 9796 7713 -2300 -983 2778 C ATOM 2234 N GLU A 273 -30.840 -5.315 11.961 1.00 54.09 N ANISOU 2234 N GLU A 273 6734 7716 6102 -1479 34 1405 N ATOM 2235 CA GLU A 273 -31.321 -6.620 12.397 1.00 53.64 C ANISOU 2235 CA GLU A 273 6649 7523 6209 -1352 207 1192 C ATOM 2236 C GLU A 273 -30.613 -7.093 13.664 1.00 67.87 C ANISOU 2236 C GLU A 273 8465 9177 8147 -1262 293 1256 C ATOM 2237 O GLU A 273 -30.728 -8.256 14.048 1.00 71.09 O ANISOU 2237 O GLU A 273 8854 9470 8686 -1156 454 1120 O ATOM 2238 CB GLU A 273 -31.156 -7.655 11.285 1.00 58.57 C ANISOU 2238 CB GLU A 273 7169 8321 6763 -1345 364 1000 C ATOM 2239 CG GLU A 273 -31.944 -7.334 10.025 1.00 57.41 C ANISOU 2239 CG GLU A 273 7034 8327 6453 -1440 262 915 C ATOM 2240 CD GLU A 273 -32.566 -8.565 9.398 1.00 63.59 C ANISOU 2240 CD GLU A 273 7766 9124 7269 -1404 404 621 C ATOM 2241 OE1 GLU A 273 -32.525 -8.689 8.155 1.00 83.75 O ANISOU 2241 OE1 GLU A 273 10301 11902 9617 -1491 408 528 O ATOM 2242 OE2 GLU A 273 -33.103 -9.407 10.147 1.00 56.66 O ANISOU 2242 OE2 GLU A 273 6884 8031 6613 -1304 516 479 O ATOM 2243 N ALA A 274 -29.832 -6.202 14.267 1.00 64.41 N ANISOU 2243 N ALA A 274 8063 8743 7668 -1314 174 1471 N ATOM 2244 CA ALA A 274 -29.087 -6.507 15.486 1.00 57.96 C ANISOU 2244 CA ALA A 274 7272 7807 6945 -1248 193 1565 C ATOM 2245 C ALA A 274 -29.928 -7.199 16.564 1.00 74.41 C ANISOU 2245 C ALA A 274 9481 9621 9170 -1147 275 1466 C ATOM 2246 O ALA A 274 -29.678 -8.357 16.898 1.00 83.02 O ANISOU 2246 O ALA A 274 10545 10639 10362 -1040 413 1398 O ATOM 2247 CB ALA A 274 -28.473 -5.233 16.047 1.00 52.29 C ANISOU 2247 CB ALA A 274 6617 7095 6156 -1354 5 1785 C ATOM 2248 N TYR A 275 -30.918 -6.494 17.105 1.00 75.52 N ANISOU 2248 N TYR A 275 9762 9603 9329 -1184 206 1459 N ATOM 2249 CA TYR A 275 -31.677 -7.010 18.244 1.00 52.50 C ANISOU 2249 CA TYR A 275 6988 6431 6528 -1121 307 1382 C ATOM 2250 C TYR A 275 -32.996 -7.699 17.875 1.00 66.90 C ANISOU 2250 C TYR A 275 8789 8157 8474 -1083 448 1153 C ATOM 2251 O TYR A 275 -33.682 -8.234 18.747 1.00 50.13 O ANISOU 2251 O TYR A 275 6770 5821 6458 -1046 577 1071 O ATOM 2252 CB TYR A 275 -31.944 -5.876 19.236 1.00 50.70 C ANISOU 2252 CB TYR A 275 6931 6063 6269 -1187 191 1484 C ATOM 2253 CG TYR A 275 -30.676 -5.207 19.721 1.00 64.86 C ANISOU 2253 CG TYR A 275 8758 7932 7952 -1247 37 1695 C ATOM 2254 CD1 TYR A 275 -29.903 -5.782 20.723 1.00 65.06 C ANISOU 2254 CD1 TYR A 275 8855 7894 7969 -1204 45 1783 C ATOM 2255 CD2 TYR A 275 -30.246 -4.007 19.169 1.00 56.88 C ANISOU 2255 CD2 TYR A 275 7708 7051 6853 -1355 -133 1815 C ATOM 2256 CE1 TYR A 275 -28.741 -5.178 21.164 1.00 51.26 C ANISOU 2256 CE1 TYR A 275 7113 6227 6137 -1269 -126 1968 C ATOM 2257 CE2 TYR A 275 -29.086 -3.396 19.604 1.00 50.89 C ANISOU 2257 CE2 TYR A 275 6961 6360 6015 -1434 -274 1995 C ATOM 2258 CZ TYR A 275 -28.338 -3.985 20.602 1.00 54.05 C ANISOU 2258 CZ TYR A 275 7406 6712 6417 -1391 -277 2062 C ATOM 2259 OH TYR A 275 -27.182 -3.380 21.038 1.00 57.12 O ANISOU 2259 OH TYR A 275 7782 7178 6742 -1479 -446 2233 O ATOM 2260 N TYR A 276 -33.347 -7.694 16.592 1.00 66.93 N ANISOU 2260 N TYR A 276 8660 8318 8450 -1109 424 1050 N ATOM 2261 CA TYR A 276 -34.506 -8.453 16.118 1.00 62.62 C ANISOU 2261 CA TYR A 276 8058 7711 8024 -1086 537 815 C ATOM 2262 C TYR A 276 -34.340 -8.844 14.653 1.00 59.73 C ANISOU 2262 C TYR A 276 7550 7575 7569 -1111 530 710 C ATOM 2263 O TYR A 276 -33.373 -8.452 14.012 1.00 68.65 O ANISOU 2263 O TYR A 276 8633 8912 8540 -1150 456 826 O ATOM 2264 CB TYR A 276 -35.801 -7.656 16.312 1.00 50.72 C ANISOU 2264 CB TYR A 276 6580 6081 6610 -1119 461 756 C ATOM 2265 CG TYR A 276 -35.752 -6.230 15.808 1.00 50.75 C ANISOU 2265 CG TYR A 276 6580 6194 6507 -1183 225 898 C ATOM 2266 CD1 TYR A 276 -35.796 -5.947 14.449 1.00 51.56 C ANISOU 2266 CD1 TYR A 276 6583 6508 6499 -1231 92 892 C ATOM 2267 CD2 TYR A 276 -35.683 -5.164 16.695 1.00 50.28 C ANISOU 2267 CD2 TYR A 276 6642 6011 6451 -1205 137 1039 C ATOM 2268 CE1 TYR A 276 -35.757 -4.645 13.989 1.00 51.91 C ANISOU 2268 CE1 TYR A 276 6650 6626 6447 -1294 -131 1051 C ATOM 2269 CE2 TYR A 276 -35.647 -3.861 16.242 1.00 50.57 C ANISOU 2269 CE2 TYR A 276 6689 6108 6418 -1264 -76 1174 C ATOM 2270 CZ TYR A 276 -35.683 -3.607 14.890 1.00 51.39 C ANISOU 2270 CZ TYR A 276 6694 6409 6422 -1305 -212 1194 C ATOM 2271 OH TYR A 276 -35.646 -2.309 14.440 1.00 64.69 O ANISOU 2271 OH TYR A 276 8412 8129 8036 -1368 -431 1357 O ATOM 2272 N ASP A 277 -35.281 -9.590 14.095 1.00 58.85 N ANISOU 2272 N ASP A 277 7375 7438 7548 -1108 612 480 N ATOM 2273 CA ASP A 277 -35.202 -9.958 12.683 1.00 69.70 C ANISOU 2273 CA ASP A 277 8646 9036 8802 -1152 600 351 C ATOM 2274 C ASP A 277 -36.486 -10.490 12.095 1.00 69.36 C ANISOU 2274 C ASP A 277 8538 8959 8858 -1180 613 98 C ATOM 2275 O ASP A 277 -37.534 -10.287 12.647 1.00 64.86 O ANISOU 2275 O ASP A 277 7971 8219 8454 -1176 590 44 O ATOM 2276 CB ASP A 277 -34.107 -10.967 12.438 1.00 79.18 C ANISOU 2276 CB ASP A 277 9802 10312 9971 -1102 775 307 C ATOM 2277 CG ASP A 277 -33.922 -11.893 13.582 1.00 87.77 C ANISOU 2277 CG ASP A 277 10942 11155 11250 -997 951 295 C ATOM 2278 OD1 ASP A 277 -33.232 -11.488 14.521 1.00 93.31 O ANISOU 2278 OD1 ASP A 277 11711 11790 11951 -960 912 501 O ATOM 2279 OD2 ASP A 277 -34.471 -13.006 13.558 1.00 94.74 O ANISOU 2279 OD2 ASP A 277 11813 11904 12278 -963 1115 88 O ATOM 2280 N PHE A 278 -36.381 -11.164 10.954 1.00 71.19 N ANISOU 2280 N PHE A 278 8702 9360 8987 -1219 655 -72 N ATOM 2281 CA PHE A 278 -37.543 -11.636 10.210 1.00 71.02 C ANISOU 2281 CA PHE A 278 8609 9353 9023 -1275 622 -326 C ATOM 2282 C PHE A 278 -37.903 -13.078 10.560 1.00 75.29 C ANISOU 2282 C PHE A 278 9127 9700 9780 -1238 872 -573 C ATOM 2283 O PHE A 278 -38.818 -13.652 9.970 1.00 95.95 O ANISOU 2283 O PHE A 278 11673 12313 12470 -1297 874 -821 O ATOM 2284 CB PHE A 278 -37.295 -11.521 8.703 1.00 73.32 C ANISOU 2284 CB PHE A 278 8874 9949 9037 -1371 509 -390 C ATOM 2285 CG PHE A 278 -37.164 -10.107 8.213 1.00 74.37 C ANISOU 2285 CG PHE A 278 9043 10257 8956 -1435 240 -152 C ATOM 2286 CD1 PHE A 278 -38.277 -9.400 7.788 1.00 69.69 C ANISOU 2286 CD1 PHE A 278 8423 9685 8373 -1482 -18 -155 C ATOM 2287 CD2 PHE A 278 -35.926 -9.486 8.169 1.00 83.13 C ANISOU 2287 CD2 PHE A 278 10207 11501 9878 -1450 239 79 C ATOM 2288 CE1 PHE A 278 -38.160 -8.100 7.334 1.00 69.23 C ANISOU 2288 CE1 PHE A 278 8418 9754 8132 -1534 -277 85 C ATOM 2289 CE2 PHE A 278 -35.803 -8.185 7.715 1.00 78.33 C ANISOU 2289 CE2 PHE A 278 9652 11029 9080 -1526 2 309 C ATOM 2290 CZ PHE A 278 -36.921 -7.492 7.297 1.00 67.49 C ANISOU 2290 CZ PHE A 278 8280 9653 7711 -1564 -258 320 C ATOM 2291 N THR A 279 -37.175 -13.660 11.509 1.00 69.52 N ANISOU 2291 N THR A 279 8459 8802 9154 -1146 1066 -498 N ATOM 2292 CA THR A 279 -37.433 -15.031 11.941 1.00 66.02 C ANISOU 2292 CA THR A 279 8025 8129 8928 -1104 1311 -690 C ATOM 2293 C THR A 279 -38.843 -15.159 12.512 1.00 68.22 C ANISOU 2293 C THR A 279 8290 8195 9435 -1149 1341 -816 C ATOM 2294 O THR A 279 -39.516 -16.172 12.313 1.00 71.34 O ANISOU 2294 O THR A 279 8642 8470 9992 -1188 1480 -1065 O ATOM 2295 CB THR A 279 -36.406 -15.494 12.993 1.00 60.81 C ANISOU 2295 CB THR A 279 7458 7306 8342 -986 1465 -523 C ATOM 2296 OG1 THR A 279 -35.080 -15.282 12.494 1.00 57.95 O ANISOU 2296 OG1 THR A 279 7062 7151 7805 -944 1433 -402 O ATOM 2297 CG2 THR A 279 -36.591 -16.970 13.318 1.00 61.45 C ANISOU 2297 CG2 THR A 279 7568 7137 8645 -939 1716 -706 C ATOM 2298 N ASN A 280 -39.288 -14.121 13.212 1.00 70.03 N ANISOU 2298 N ASN A 280 8546 8371 9691 -1151 1223 -657 N ATOM 2299 CA ASN A 280 -40.648 -14.076 13.736 1.00 76.50 C ANISOU 2299 CA ASN A 280 9317 9008 10740 -1195 1257 -778 C ATOM 2300 C ASN A 280 -41.590 -13.390 12.750 1.00 84.74 C ANISOU 2300 C ASN A 280 10206 10216 11774 -1267 1017 -886 C ATOM 2301 O ASN A 280 -41.320 -12.274 12.305 1.00 73.67 O ANISOU 2301 O ASN A 280 8801 8992 10199 -1264 780 -722 O ATOM 2302 CB ASN A 280 -40.680 -13.360 15.087 1.00 74.47 C ANISOU 2302 CB ASN A 280 9177 8579 10541 -1156 1292 -580 C ATOM 2303 CG ASN A 280 -42.049 -13.406 15.738 1.00 77.34 C ANISOU 2303 CG ASN A 280 9488 8732 11164 -1202 1402 -723 C ATOM 2304 OD1 ASN A 280 -42.852 -12.485 15.590 1.00 83.51 O ANISOU 2304 OD1 ASN A 280 10164 9550 12016 -1223 1251 -742 O ATOM 2305 ND2 ASN A 280 -42.323 -14.484 16.464 1.00 73.88 N ANISOU 2305 ND2 ASN A 280 9118 8062 10892 -1219 1676 -824 N ATOM 2306 N PRO A 281 -42.699 -14.065 12.404 1.00 86.43 N ANISOU 2306 N PRO A 281 10292 10364 12185 -1337 1063 -1156 N ATOM 2307 CA PRO A 281 -43.677 -13.579 11.422 1.00 70.87 C ANISOU 2307 CA PRO A 281 8147 8545 10233 -1407 807 -1286 C ATOM 2308 C PRO A 281 -44.284 -12.228 11.793 1.00 69.98 C ANISOU 2308 C PRO A 281 7976 8414 10200 -1372 608 -1134 C ATOM 2309 O PRO A 281 -44.405 -11.355 10.934 1.00 76.22 O ANISOU 2309 O PRO A 281 8707 9397 10854 -1382 306 -1058 O ATOM 2310 CB PRO A 281 -44.751 -14.672 11.430 1.00 71.43 C ANISOU 2310 CB PRO A 281 8092 8462 10587 -1488 963 -1600 C ATOM 2311 CG PRO A 281 -44.049 -15.891 11.917 1.00 72.09 C ANISOU 2311 CG PRO A 281 8311 8385 10695 -1471 1278 -1651 C ATOM 2312 CD PRO A 281 -43.055 -15.397 12.921 1.00 79.27 C ANISOU 2312 CD PRO A 281 9397 9221 11500 -1363 1356 -1351 C ATOM 2313 N VAL A 282 -44.657 -12.065 13.058 1.00 63.75 N ANISOU 2313 N VAL A 282 7217 7383 9622 -1333 783 -1092 N ATOM 2314 CA VAL A 282 -45.268 -10.826 13.527 1.00 61.68 C ANISOU 2314 CA VAL A 282 6899 7055 9481 -1289 647 -984 C ATOM 2315 C VAL A 282 -44.287 -9.659 13.441 1.00 62.38 C ANISOU 2315 C VAL A 282 7124 7270 9307 -1234 450 -689 C ATOM 2316 O VAL A 282 -44.637 -8.574 12.975 1.00 66.50 O ANISOU 2316 O VAL A 282 7574 7870 9821 -1214 180 -598 O ATOM 2317 CB VAL A 282 -45.773 -10.961 14.977 1.00 60.04 C ANISOU 2317 CB VAL A 282 6736 6558 9518 -1276 940 -1017 C ATOM 2318 CG1 VAL A 282 -46.431 -9.668 15.436 1.00 59.36 C ANISOU 2318 CG1 VAL A 282 6582 6393 9581 -1224 824 -945 C ATOM 2319 CG2 VAL A 282 -46.740 -12.128 15.095 1.00 60.75 C ANISOU 2319 CG2 VAL A 282 6693 6506 9884 -1356 1165 -1302 C ATOM 2320 N VAL A 283 -43.057 -9.893 13.888 1.00 68.57 N ANISOU 2320 N VAL A 283 8096 8062 9895 -1213 578 -536 N ATOM 2321 CA VAL A 283 -42.016 -8.872 13.859 1.00 66.32 C ANISOU 2321 CA VAL A 283 7937 7893 9369 -1185 418 -262 C ATOM 2322 C VAL A 283 -41.636 -8.520 12.424 1.00 63.81 C ANISOU 2322 C VAL A 283 7571 7858 8815 -1227 164 -208 C ATOM 2323 O VAL A 283 -41.398 -7.356 12.100 1.00 60.97 O ANISOU 2323 O VAL A 283 7244 7590 8333 -1228 -65 -15 O ATOM 2324 CB VAL A 283 -40.756 -9.330 14.623 1.00 70.43 C ANISOU 2324 CB VAL A 283 8632 8372 9756 -1158 602 -127 C ATOM 2325 CG1 VAL A 283 -39.692 -8.242 14.606 1.00 61.39 C ANISOU 2325 CG1 VAL A 283 7588 7348 8389 -1153 432 145 C ATOM 2326 CG2 VAL A 283 -41.112 -9.707 16.052 1.00 81.92 C ANISOU 2326 CG2 VAL A 283 10183 9551 11390 -1135 847 -159 C ATOM 2327 N GLY A 284 -41.591 -9.537 11.568 1.00 74.21 N ANISOU 2327 N GLY A 284 8832 9303 10063 -1273 215 -384 N ATOM 2328 CA GLY A 284 -41.223 -9.359 10.175 1.00 58.55 C ANISOU 2328 CA GLY A 284 6833 7604 7811 -1337 16 -366 C ATOM 2329 C GLY A 284 -42.137 -8.413 9.419 1.00 75.04 C ANISOU 2329 C GLY A 284 8830 9780 9900 -1366 -315 -337 C ATOM 2330 O GLY A 284 -41.665 -7.513 8.724 1.00 69.45 O ANISOU 2330 O GLY A 284 8188 9248 8954 -1398 -538 -138 O ATOM 2331 N ARG A 285 -43.445 -8.617 9.553 1.00 69.11 N ANISOU 2331 N ARG A 285 7922 8903 9434 -1358 -352 -527 N ATOM 2332 CA ARG A 285 -44.425 -7.781 8.867 1.00 65.63 C ANISOU 2332 CA ARG A 285 7354 8524 9060 -1363 -695 -512 C ATOM 2333 C ARG A 285 -44.350 -6.331 9.331 1.00 63.96 C ANISOU 2333 C ARG A 285 7196 8223 8883 -1289 -862 -240 C ATOM 2334 O ARG A 285 -44.318 -5.414 8.510 1.00 73.34 O ANISOU 2334 O ARG A 285 8410 9546 9909 -1304 -1175 -67 O ATOM 2335 CB ARG A 285 -45.840 -8.324 9.077 1.00 77.75 C ANISOU 2335 CB ARG A 285 8663 9914 10966 -1362 -669 -786 C ATOM 2336 CG ARG A 285 -46.127 -9.618 8.336 1.00 81.75 C ANISOU 2336 CG ARG A 285 9092 10525 11443 -1464 -602 -1075 C ATOM 2337 CD ARG A 285 -47.604 -9.971 8.401 1.00 79.35 C ANISOU 2337 CD ARG A 285 8526 10103 11520 -1486 -648 -1332 C ATOM 2338 NE ARG A 285 -48.057 -10.184 9.772 1.00 87.54 N ANISOU 2338 NE ARG A 285 9505 10844 12911 -1433 -339 -1399 N ATOM 2339 CZ ARG A 285 -48.107 -11.372 10.365 1.00 89.86 C ANISOU 2339 CZ ARG A 285 9810 10988 13346 -1483 9 -1591 C ATOM 2340 NH1 ARG A 285 -47.734 -12.461 9.706 1.00 94.10 N ANISOU 2340 NH1 ARG A 285 10397 11625 13733 -1571 90 -1753 N ATOM 2341 NH2 ARG A 285 -48.532 -11.473 11.617 1.00 83.43 N ANISOU 2341 NH2 ARG A 285 8973 9910 12818 -1451 287 -1624 N ATOM 2342 N CYS A 286 -44.323 -6.131 10.645 1.00 60.77 N ANISOU 2342 N CYS A 286 6831 7579 8679 -1220 -651 -204 N ATOM 2343 CA CYS A 286 -44.219 -4.794 11.222 1.00 67.87 C ANISOU 2343 CA CYS A 286 7802 8354 9630 -1155 -764 20 C ATOM 2344 C CYS A 286 -42.950 -4.091 10.758 1.00 71.30 C ANISOU 2344 C CYS A 286 8423 8955 9714 -1197 -894 300 C ATOM 2345 O CYS A 286 -42.935 -2.875 10.563 1.00 81.08 O ANISOU 2345 O CYS A 286 9708 10177 10923 -1180 -1130 504 O ATOM 2346 CB CYS A 286 -44.248 -4.863 12.750 1.00 75.84 C ANISOU 2346 CB CYS A 286 8871 9099 10844 -1103 -466 -16 C ATOM 2347 SG CYS A 286 -43.817 -3.312 13.577 1.00 62.85 S ANISOU 2347 SG CYS A 286 7382 7298 9202 -1049 -548 241 S ATOM 2348 N MET A 287 -41.888 -4.868 10.582 1.00 71.16 N ANISOU 2348 N MET A 287 8501 9082 9454 -1255 -727 304 N ATOM 2349 CA MET A 287 -40.613 -4.337 10.123 1.00 58.16 C ANISOU 2349 CA MET A 287 7000 7613 7484 -1316 -800 543 C ATOM 2350 C MET A 287 -40.711 -3.889 8.667 1.00 60.29 C ANISOU 2350 C MET A 287 7267 8121 7520 -1393 -1090 624 C ATOM 2351 O MET A 287 -40.100 -2.896 8.273 1.00 78.98 O ANISOU 2351 O MET A 287 9744 10574 9692 -1442 -1257 878 O ATOM 2352 CB MET A 287 -39.512 -5.386 10.299 1.00 60.39 C ANISOU 2352 CB MET A 287 7339 7983 7622 -1341 -529 493 C ATOM 2353 CG MET A 287 -38.117 -4.915 9.937 1.00 60.52 C ANISOU 2353 CG MET A 287 7464 8180 7349 -1407 -552 720 C ATOM 2354 SD MET A 287 -36.844 -5.768 10.890 1.00 71.99 S ANISOU 2354 SD MET A 287 8965 9591 8799 -1371 -243 727 S ATOM 2355 CE MET A 287 -37.438 -7.457 10.837 1.00 55.38 C ANISOU 2355 CE MET A 287 6768 7433 6842 -1324 -10 395 C ATOM 2356 N LEU A 288 -41.494 -4.617 7.876 1.00 71.17 N ANISOU 2356 N LEU A 288 8532 9600 8910 -1419 -1155 412 N ATOM 2357 CA LEU A 288 -41.717 -4.261 6.478 1.00 80.03 C ANISOU 2357 CA LEU A 288 9667 10954 9785 -1503 -1458 471 C ATOM 2358 C LEU A 288 -42.646 -3.057 6.349 1.00 79.44 C ANISOU 2358 C LEU A 288 9543 10772 9867 -1447 -1809 620 C ATOM 2359 O LEU A 288 -42.570 -2.307 5.376 1.00 76.37 O ANISOU 2359 O LEU A 288 9239 10535 9244 -1509 -2104 813 O ATOM 2360 CB LEU A 288 -42.293 -5.451 5.707 1.00 66.05 C ANISOU 2360 CB LEU A 288 7796 9321 7979 -1561 -1435 169 C ATOM 2361 CG LEU A 288 -41.352 -6.639 5.499 1.00 65.44 C ANISOU 2361 CG LEU A 288 7780 9378 7706 -1624 -1127 15 C ATOM 2362 CD1 LEU A 288 -42.083 -7.796 4.838 1.00 67.25 C ANISOU 2362 CD1 LEU A 288 7907 9686 7959 -1682 -1105 -320 C ATOM 2363 CD2 LEU A 288 -40.148 -6.221 4.672 1.00 66.09 C ANISOU 2363 CD2 LEU A 288 8026 9716 7369 -1725 -1153 214 C ATOM 2364 N GLN A 289 -43.522 -2.880 7.334 1.00 80.47 N ANISOU 2364 N GLN A 289 9541 10633 10401 -1329 -1767 531 N ATOM 2365 CA GLN A 289 -44.437 -1.744 7.359 1.00 79.02 C ANISOU 2365 CA GLN A 289 9276 10295 10454 -1240 -2066 647 C ATOM 2366 C GLN A 289 -43.673 -0.429 7.468 1.00 80.05 C ANISOU 2366 C GLN A 289 9594 10372 10450 -1240 -2192 985 C ATOM 2367 O GLN A 289 -44.060 0.578 6.875 1.00 84.90 O ANISOU 2367 O GLN A 289 10223 10970 11066 -1217 -2533 1176 O ATOM 2368 CB GLN A 289 -45.424 -1.872 8.523 1.00 83.50 C ANISOU 2368 CB GLN A 289 9661 10571 11495 -1118 -1903 452 C ATOM 2369 CG GLN A 289 -46.402 -3.030 8.400 1.00 92.58 C ANISOU 2369 CG GLN A 289 10589 11735 12853 -1127 -1817 121 C ATOM 2370 CD GLN A 289 -47.496 -2.769 7.385 1.00105.65 C ANISOU 2370 CD GLN A 289 12053 13476 14613 -1114 -2213 75 C ATOM 2371 OE1 GLN A 289 -48.070 -1.681 7.340 1.00120.13 O ANISOU 2371 OE1 GLN A 289 13815 15193 16635 -1017 -2488 220 O ATOM 2372 NE2 GLN A 289 -47.785 -3.766 6.557 1.00101.31 N ANISOU 2372 NE2 GLN A 289 11423 13122 13950 -1212 -2259 -128 N ATOM 2373 N GLN A 290 -42.583 -0.451 8.228 1.00 78.58 N ANISOU 2373 N GLN A 290 9549 10149 10159 -1270 -1928 1063 N ATOM 2374 CA GLN A 290 -41.779 0.742 8.458 1.00 77.26 C ANISOU 2374 CA GLN A 290 9556 9914 9885 -1295 -2009 1360 C ATOM 2375 C GLN A 290 -40.894 1.070 7.259 1.00 82.12 C ANISOU 2375 C GLN A 290 10323 10801 10080 -1439 -2169 1588 C ATOM 2376 O GLN A 290 -40.605 2.236 6.994 1.00 83.93 O ANISOU 2376 O GLN A 290 10678 10987 10225 -1474 -2376 1863 O ATOM 2377 CB GLN A 290 -40.917 0.565 9.710 1.00 67.06 C ANISOU 2377 CB GLN A 290 8350 8502 8627 -1293 -1692 1352 C ATOM 2378 CG GLN A 290 -41.712 0.285 10.975 1.00 63.63 C ANISOU 2378 CG GLN A 290 7820 7797 8559 -1178 -1495 1145 C ATOM 2379 CD GLN A 290 -42.543 1.473 11.418 1.00 67.30 C ANISOU 2379 CD GLN A 290 8256 7997 9317 -1079 -1659 1205 C ATOM 2380 OE1 GLN A 290 -42.124 2.622 11.285 1.00 73.48 O ANISOU 2380 OE1 GLN A 290 9165 8723 10031 -1100 -1839 1445 O ATOM 2381 NE2 GLN A 290 -43.730 1.200 11.946 1.00 78.43 N ANISOU 2381 NE2 GLN A 290 9492 9229 11078 -975 -1581 979 N ATOM 2382 N LEU A 291 -40.467 0.039 6.538 1.00 77.83 N ANISOU 2382 N LEU A 291 9776 10522 9275 -1530 -2054 1466 N ATOM 2383 CA LEU A 291 -39.585 0.223 5.390 1.00 78.78 C ANISOU 2383 CA LEU A 291 10043 10925 8963 -1688 -2137 1644 C ATOM 2384 C LEU A 291 -40.319 0.856 4.212 1.00 83.37 C ANISOU 2384 C LEU A 291 10665 11604 9409 -1727 -2533 1776 C ATOM 2385 O LEU A 291 -39.706 1.492 3.355 1.00 97.65 O ANISOU 2385 O LEU A 291 12645 13575 10882 -1859 -2676 2025 O ATOM 2386 CB LEU A 291 -38.970 -1.113 4.966 1.00 78.75 C ANISOU 2386 CB LEU A 291 10017 11162 8741 -1764 -1871 1431 C ATOM 2387 CG LEU A 291 -38.081 -1.813 5.997 1.00 67.77 C ANISOU 2387 CG LEU A 291 8600 9705 7445 -1729 -1500 1335 C ATOM 2388 CD1 LEU A 291 -37.510 -3.104 5.430 1.00 63.83 C ANISOU 2388 CD1 LEU A 291 8073 9429 6750 -1789 -1261 1127 C ATOM 2389 CD2 LEU A 291 -36.967 -0.891 6.474 1.00 66.52 C ANISOU 2389 CD2 LEU A 291 8557 9509 7210 -1780 -1464 1610 C ATOM 2390 N LYS A 292 -41.635 0.678 4.175 1.00 79.72 N ANISOU 2390 N LYS A 292 10040 11041 9209 -1620 -2717 1616 N ATOM 2391 CA LYS A 292 -42.448 1.217 3.093 1.00 80.97 C ANISOU 2391 CA LYS A 292 10208 11281 9277 -1636 -3144 1731 C ATOM 2392 C LYS A 292 -43.047 2.572 3.464 1.00 82.92 C ANISOU 2392 C LYS A 292 10446 11245 9814 -1512 -3429 1963 C ATOM 2393 O LYS A 292 -43.784 3.171 2.682 1.00 96.66 O ANISOU 2393 O LYS A 292 12183 12993 11550 -1488 -3830 2101 O ATOM 2394 CB LYS A 292 -43.552 0.228 2.718 1.00 78.26 C ANISOU 2394 CB LYS A 292 9661 11011 9064 -1601 -3224 1414 C ATOM 2395 CG LYS A 292 -43.019 -1.125 2.271 1.00 83.51 C ANISOU 2395 CG LYS A 292 10346 11932 9453 -1725 -2954 1162 C ATOM 2396 CD LYS A 292 -44.141 -2.093 1.939 1.00 94.89 C ANISOU 2396 CD LYS A 292 11586 13419 11050 -1710 -3036 831 C ATOM 2397 CE LYS A 292 -43.586 -3.445 1.519 1.00103.06 C ANISOU 2397 CE LYS A 292 12656 14671 11829 -1832 -2745 561 C ATOM 2398 NZ LYS A 292 -44.667 -4.415 1.194 1.00113.80 N ANISOU 2398 NZ LYS A 292 13828 16063 13347 -1844 -2819 219 N ATOM 2399 N LYS A 293 -42.724 3.047 4.664 1.00 73.46 N ANISOU 2399 N LYS A 293 9253 9789 8871 -1431 -3228 2003 N ATOM 2400 CA LYS A 293 -43.134 4.376 5.107 1.00 77.58 C ANISOU 2400 CA LYS A 293 9796 10010 9673 -1319 -3441 2211 C ATOM 2401 C LYS A 293 -42.423 5.456 4.295 1.00 92.67 C ANISOU 2401 C LYS A 293 11960 11988 11264 -1441 -3683 2603 C ATOM 2402 O LYS A 293 -41.373 5.196 3.706 1.00 90.57 O ANISOU 2402 O LYS A 293 11858 11980 10573 -1623 -3571 2703 O ATOM 2403 CB LYS A 293 -42.841 4.556 6.599 1.00 82.51 C ANISOU 2403 CB LYS A 293 10404 10363 10582 -1240 -3129 2131 C ATOM 2404 CG LYS A 293 -43.888 3.960 7.522 1.00 81.36 C ANISOU 2404 CG LYS A 293 10016 10028 10870 -1084 -2968 1808 C ATOM 2405 CD LYS A 293 -43.595 4.318 8.969 1.00 83.44 C ANISOU 2405 CD LYS A 293 10323 10016 11363 -1024 -2690 1766 C ATOM 2406 CE LYS A 293 -43.474 5.824 9.150 1.00 90.03 C ANISOU 2406 CE LYS A 293 11291 10613 12303 -986 -2889 2029 C ATOM 2407 NZ LYS A 293 -43.090 6.194 10.541 1.00 76.72 N ANISOU 2407 NZ LYS A 293 9688 8677 10786 -960 -2620 1977 N ATOM 2408 N PRO A 294 -42.996 6.673 4.253 1.00118.99 N ANISOU 2408 N PRO A 294 15323 15074 14814 -1343 -4004 2826 N ATOM 2409 CA PRO A 294 -42.345 7.783 3.549 1.00127.53 C ANISOU 2409 CA PRO A 294 16670 16163 15622 -1465 -4235 3228 C ATOM 2410 C PRO A 294 -40.956 8.095 4.102 1.00136.76 C ANISOU 2410 C PRO A 294 18021 17325 16617 -1610 -3938 3354 C ATOM 2411 O PRO A 294 -40.779 8.214 5.314 1.00128.00 O ANISOU 2411 O PRO A 294 16860 15992 15784 -1536 -3705 3241 O ATOM 2412 CB PRO A 294 -43.303 8.961 3.778 1.00126.37 C ANISOU 2412 CB PRO A 294 16474 15648 15893 -1276 -4567 3379 C ATOM 2413 CG PRO A 294 -44.164 8.551 4.932 1.00127.39 C ANISOU 2413 CG PRO A 294 16325 15548 16528 -1071 -4379 3037 C ATOM 2414 CD PRO A 294 -44.304 7.071 4.801 1.00126.00 C ANISOU 2414 CD PRO A 294 15992 15654 16229 -1114 -4170 2716 C ATOM 2415 N ARG A 295 -39.985 8.222 3.204 1.00142.57 N ANISOU 2415 N ARG A 295 18967 18313 16890 -1829 -3948 3580 N ATOM 2416 CA ARG A 295 -38.596 8.466 3.579 1.00 78.29 C ANISOU 2416 CA ARG A 295 10969 10214 8562 -1999 -3676 3703 C ATOM 2417 C ARG A 295 -38.392 9.918 4.015 1.00 79.36 C ANISOU 2417 C ARG A 295 11256 10020 8877 -2004 -3818 3992 C ATOM 2418 O ARG A 295 -39.134 10.801 3.588 1.00100.93 O ANISOU 2418 O ARG A 295 14055 12564 11731 -1928 -4171 4194 O ATOM 2419 CB ARG A 295 -37.663 8.118 2.413 1.00 79.72 C ANISOU 2419 CB ARG A 295 11304 10783 8203 -2244 -3613 3833 C ATOM 2420 CG ARG A 295 -37.451 6.623 2.195 1.00 78.12 C ANISOU 2420 CG ARG A 295 10970 10895 7817 -2272 -3339 3512 C ATOM 2421 CD ARG A 295 -38.627 5.976 1.480 1.00 79.79 C ANISOU 2421 CD ARG A 295 11085 11218 8016 -2183 -3560 3339 C ATOM 2422 NE ARG A 295 -38.567 4.519 1.531 1.00 80.40 N ANISOU 2422 NE ARG A 295 11010 11503 8038 -2175 -3276 2976 N ATOM 2423 CZ ARG A 295 -37.957 3.764 0.623 1.00 99.57 C ANISOU 2423 CZ ARG A 295 13509 14273 10049 -2339 -3134 2903 C ATOM 2424 NH1 ARG A 295 -37.351 4.329 -0.412 1.00 81.82 N ANISOU 2424 NH1 ARG A 295 11490 12224 7374 -2541 -3237 3173 N ATOM 2425 NH2 ARG A 295 -37.953 2.444 0.750 1.00101.18 N ANISOU 2425 NH2 ARG A 295 13569 14610 10265 -2309 -2873 2556 N ATOM 2426 N PRO A 296 -37.383 10.175 4.868 1.00109.41 N ANISOU 2426 N PRO A 296 15115 13742 12713 -2093 -3561 4012 N ATOM 2427 CA PRO A 296 -36.418 9.221 5.432 1.00 94.07 C ANISOU 2427 CA PRO A 296 13091 11996 10655 -2173 -3175 3811 C ATOM 2428 C PRO A 296 -36.998 8.337 6.529 1.00 91.39 C ANISOU 2428 C PRO A 296 12544 11552 10626 -1980 -2976 3451 C ATOM 2429 O PRO A 296 -37.834 8.780 7.317 1.00 97.99 O ANISOU 2429 O PRO A 296 13325 12076 11831 -1813 -3049 3370 O ATOM 2430 CB PRO A 296 -35.328 10.130 6.002 1.00 90.30 C ANISOU 2430 CB PRO A 296 12751 11383 10176 -2321 -3084 4012 C ATOM 2431 CG PRO A 296 -36.047 11.367 6.366 1.00 96.99 C ANISOU 2431 CG PRO A 296 13685 11833 11332 -2217 -3339 4157 C ATOM 2432 CD PRO A 296 -37.113 11.550 5.321 1.00110.71 C ANISOU 2432 CD PRO A 296 15437 13580 13047 -2126 -3674 4263 C ATOM 2433 N VAL A 297 -36.546 7.090 6.568 1.00 69.29 N ANISOU 2433 N VAL A 297 9640 9004 7682 -2008 -2710 3236 N ATOM 2434 CA VAL A 297 -36.958 6.159 7.605 1.00 72.78 C ANISOU 2434 CA VAL A 297 9916 9360 8377 -1858 -2487 2915 C ATOM 2435 C VAL A 297 -35.734 5.513 8.249 1.00 81.77 C ANISOU 2435 C VAL A 297 11043 10619 9407 -1941 -2169 2844 C ATOM 2436 O VAL A 297 -34.988 4.777 7.600 1.00 82.08 O ANISOU 2436 O VAL A 297 11061 10950 9176 -2045 -2034 2824 O ATOM 2437 CB VAL A 297 -37.909 5.072 7.044 1.00 66.91 C ANISOU 2437 CB VAL A 297 9018 8760 7643 -1764 -2503 2673 C ATOM 2438 CG1 VAL A 297 -37.455 4.613 5.663 1.00 70.47 C ANISOU 2438 CG1 VAL A 297 9525 9569 7682 -1914 -2546 2738 C ATOM 2439 CG2 VAL A 297 -38.021 3.899 8.008 1.00 72.04 C ANISOU 2439 CG2 VAL A 297 9523 9380 8469 -1667 -2198 2358 C ATOM 2440 N ILE A 298 -35.518 5.816 9.524 1.00 83.38 N ANISOU 2440 N ILE A 298 11262 10594 9825 -1896 -2060 2806 N ATOM 2441 CA ILE A 298 -34.450 5.186 10.289 1.00 70.57 C ANISOU 2441 CA ILE A 298 9614 9054 8145 -1947 -1799 2733 C ATOM 2442 C ILE A 298 -35.062 4.338 11.393 1.00 71.08 C ANISOU 2442 C ILE A 298 9589 8973 8446 -1789 -1622 2460 C ATOM 2443 O ILE A 298 -35.609 4.865 12.362 1.00 87.09 O ANISOU 2443 O ILE A 298 11659 10722 10710 -1709 -1636 2411 O ATOM 2444 CB ILE A 298 -33.484 6.219 10.909 1.00 71.90 C ANISOU 2444 CB ILE A 298 9906 9104 8311 -2073 -1821 2933 C ATOM 2445 CG1 ILE A 298 -32.817 7.066 9.822 1.00 67.01 C ANISOU 2445 CG1 ILE A 298 9386 8620 7454 -2263 -1966 3223 C ATOM 2446 CG2 ILE A 298 -32.431 5.520 11.756 1.00 81.82 C ANISOU 2446 CG2 ILE A 298 11109 10446 9534 -2110 -1592 2852 C ATOM 2447 CD1 ILE A 298 -33.543 8.360 9.509 1.00 68.65 C ANISOU 2447 CD1 ILE A 298 9728 8589 7766 -2257 -2245 3411 C ATOM 2448 N LEU A 299 -34.964 3.022 11.248 1.00 62.16 N ANISOU 2448 N LEU A 299 8348 8021 7250 -1752 -1437 2277 N ATOM 2449 CA LEU A 299 -35.600 2.113 12.188 1.00 56.18 C ANISOU 2449 CA LEU A 299 7516 7128 6700 -1617 -1258 2026 C ATOM 2450 C LEU A 299 -34.733 1.908 13.424 1.00 76.49 C ANISOU 2450 C LEU A 299 10144 9622 9296 -1630 -1084 2024 C ATOM 2451 O LEU A 299 -33.579 1.491 13.323 1.00 76.60 O ANISOU 2451 O LEU A 299 10141 9815 9149 -1703 -994 2089 O ATOM 2452 CB LEU A 299 -35.897 0.772 11.517 1.00 56.10 C ANISOU 2452 CB LEU A 299 7379 7307 6629 -1578 -1139 1829 C ATOM 2453 CG LEU A 299 -36.912 -0.118 12.235 1.00 55.20 C ANISOU 2453 CG LEU A 299 7180 7033 6760 -1449 -990 1565 C ATOM 2454 CD1 LEU A 299 -38.234 0.614 12.393 1.00 76.88 C ANISOU 2454 CD1 LEU A 299 9896 9564 9753 -1367 -1143 1520 C ATOM 2455 CD2 LEU A 299 -37.105 -1.424 11.483 1.00 67.22 C ANISOU 2455 CD2 LEU A 299 8588 8738 8213 -1438 -880 1372 C ATOM 2456 N ASP A 300 -35.299 2.215 14.587 1.00 80.56 N ANISOU 2456 N ASP A 300 10723 9871 10015 -1559 -1043 1945 N ATOM 2457 CA ASP A 300 -34.611 2.047 15.861 1.00 74.43 C ANISOU 2457 CA ASP A 300 10035 8999 9246 -1574 -907 1936 C ATOM 2458 C ASP A 300 -34.207 0.589 16.055 1.00 70.24 C ANISOU 2458 C ASP A 300 9429 8595 8665 -1529 -701 1814 C ATOM 2459 O ASP A 300 -35.062 -0.296 16.070 1.00 77.64 O ANISOU 2459 O ASP A 300 10298 9491 9713 -1436 -579 1623 O ATOM 2460 CB ASP A 300 -35.508 2.513 17.013 1.00 81.83 C ANISOU 2460 CB ASP A 300 11068 9629 10395 -1504 -862 1822 C ATOM 2461 CG ASP A 300 -34.738 2.771 18.297 1.00 91.08 C ANISOU 2461 CG ASP A 300 12398 10689 11519 -1565 -799 1863 C ATOM 2462 OD1 ASP A 300 -33.698 2.119 18.526 1.00 96.30 O ANISOU 2462 OD1 ASP A 300 13056 11496 12037 -1610 -737 1918 O ATOM 2463 OD2 ASP A 300 -35.182 3.631 19.086 1.00 95.13 O ANISOU 2463 OD2 ASP A 300 13038 10963 12145 -1565 -819 1833 O ATOM 2464 N PRO A 301 -32.895 0.337 16.192 1.00 68.39 N ANISOU 2464 N PRO A 301 9193 8503 8289 -1596 -667 1925 N ATOM 2465 CA PRO A 301 -32.362 -1.015 16.393 1.00 65.05 C ANISOU 2465 CA PRO A 301 8695 8180 7842 -1539 -488 1837 C ATOM 2466 C PRO A 301 -32.963 -1.707 17.613 1.00 61.92 C ANISOU 2466 C PRO A 301 8379 7570 7579 -1444 -337 1692 C ATOM 2467 O PRO A 301 -33.079 -2.932 17.628 1.00 62.95 O ANISOU 2467 O PRO A 301 8449 7720 7751 -1367 -177 1567 O ATOM 2468 CB PRO A 301 -30.863 -0.774 16.592 1.00 55.59 C ANISOU 2468 CB PRO A 301 7487 7110 6524 -1630 -532 2016 C ATOM 2469 CG PRO A 301 -30.593 0.508 15.891 1.00 52.35 C ANISOU 2469 CG PRO A 301 7099 6768 6025 -1762 -709 2186 C ATOM 2470 CD PRO A 301 -31.821 1.342 16.094 1.00 62.84 C ANISOU 2470 CD PRO A 301 8538 7872 7465 -1734 -805 2146 C ATOM 2471 N ALA A 302 -33.319 -0.927 18.628 1.00 54.72 N ANISOU 2471 N ALA A 302 7618 6447 6726 -1462 -373 1707 N ATOM 2472 CA ALA A 302 -33.929 -1.473 19.834 1.00 58.29 C ANISOU 2472 CA ALA A 302 8185 6690 7273 -1401 -210 1575 C ATOM 2473 C ALA A 302 -35.458 -1.452 19.792 1.00 66.39 C ANISOU 2473 C ALA A 302 9184 7555 8486 -1336 -125 1387 C ATOM 2474 O ALA A 302 -36.114 -2.067 20.634 1.00 64.38 O ANISOU 2474 O ALA A 302 8995 7140 8325 -1292 63 1246 O ATOM 2475 CB ALA A 302 -33.434 -0.709 21.048 1.00 56.58 C ANISOU 2475 CB ALA A 302 8167 6340 6993 -1472 -265 1667 C ATOM 2476 N ASP A 303 -36.021 -0.747 18.815 1.00 72.60 N ANISOU 2476 N ASP A 303 9870 8382 9334 -1336 -267 1391 N ATOM 2477 CA ASP A 303 -37.470 -0.568 18.734 1.00 68.95 C ANISOU 2477 CA ASP A 303 9340 7766 9092 -1268 -235 1224 C ATOM 2478 C ASP A 303 -38.003 -0.787 17.320 1.00 60.55 C ANISOU 2478 C ASP A 303 8086 6859 8060 -1241 -348 1182 C ATOM 2479 O ASP A 303 -38.020 0.144 16.514 1.00 67.18 O ANISOU 2479 O ASP A 303 8899 7756 8869 -1266 -570 1304 O ATOM 2480 CB ASP A 303 -37.871 0.824 19.229 1.00 77.08 C ANISOU 2480 CB ASP A 303 10469 8594 10223 -1279 -338 1263 C ATOM 2481 CG ASP A 303 -39.337 0.903 19.622 1.00 68.32 C ANISOU 2481 CG ASP A 303 9298 7267 9393 -1193 -224 1052 C ATOM 2482 OD1 ASP A 303 -40.076 -0.072 19.371 1.00 56.85 O ANISOU 2482 OD1 ASP A 303 7705 5840 8054 -1140 -96 887 O ATOM 2483 OD2 ASP A 303 -39.754 1.940 20.178 1.00 53.85 O ANISOU 2483 OD2 ASP A 303 7545 5229 7686 -1182 -252 1036 O ATOM 2484 N PRO A 304 -38.431 -2.021 17.012 1.00 65.07 N ANISOU 2484 N PRO A 304 8545 7494 8683 -1201 -207 1015 N ATOM 2485 CA PRO A 304 -38.954 -2.367 15.684 1.00 67.66 C ANISOU 2485 CA PRO A 304 8705 7985 9017 -1192 -312 940 C ATOM 2486 C PRO A 304 -40.134 -1.491 15.265 1.00 73.85 C ANISOU 2486 C PRO A 304 9395 8675 9990 -1152 -495 903 C ATOM 2487 O PRO A 304 -40.317 -1.239 14.075 1.00 81.01 O ANISOU 2487 O PRO A 304 10217 9736 10828 -1168 -707 952 O ATOM 2488 CB PRO A 304 -39.392 -3.827 15.848 1.00 53.01 C ANISOU 2488 CB PRO A 304 6772 6111 7257 -1159 -79 718 C ATOM 2489 CG PRO A 304 -39.641 -3.984 17.310 1.00 53.79 C ANISOU 2489 CG PRO A 304 6984 5969 7484 -1134 134 658 C ATOM 2490 CD PRO A 304 -38.617 -3.116 17.978 1.00 65.01 C ANISOU 2490 CD PRO A 304 8581 7367 8752 -1170 63 869 C ATOM 2491 N THR A 305 -40.922 -1.039 16.236 1.00 72.68 N ANISOU 2491 N THR A 305 9264 8274 10076 -1097 -413 816 N ATOM 2492 CA THR A 305 -42.050 -0.155 15.959 1.00 68.45 C ANISOU 2492 CA THR A 305 8614 7609 9784 -1030 -579 775 C ATOM 2493 C THR A 305 -41.595 1.290 15.773 1.00 71.35 C ANISOU 2493 C THR A 305 9092 7932 10086 -1046 -820 1010 C ATOM 2494 O THR A 305 -42.083 1.998 14.892 1.00 92.89 O ANISOU 2494 O THR A 305 11737 10677 12882 -1013 -1083 1089 O ATOM 2495 CB THR A 305 -43.097 -0.203 17.088 1.00 61.06 C ANISOU 2495 CB THR A 305 7636 6404 9160 -964 -355 565 C ATOM 2496 OG1 THR A 305 -42.579 0.449 18.255 1.00 55.73 O ANISOU 2496 OG1 THR A 305 7174 5560 8441 -985 -244 634 O ATOM 2497 CG2 THR A 305 -43.454 -1.642 17.427 1.00 58.68 C ANISOU 2497 CG2 THR A 305 7266 6113 8916 -977 -76 353 C ATOM 2498 N GLY A 306 -40.661 1.719 16.615 1.00 74.28 N ANISOU 2498 N GLY A 306 9659 8236 10327 -1103 -745 1125 N ATOM 2499 CA GLY A 306 -40.198 3.094 16.613 1.00 88.38 C ANISOU 2499 CA GLY A 306 11572 9934 12073 -1140 -939 1330 C ATOM 2500 C GLY A 306 -39.407 3.486 15.381 1.00 77.97 C ANISOU 2500 C GLY A 306 10269 8841 10516 -1224 -1182 1569 C ATOM 2501 O GLY A 306 -38.440 2.822 15.010 1.00 61.42 O ANISOU 2501 O GLY A 306 8189 6976 8170 -1307 -1131 1636 O ATOM 2502 N ASN A 307 -39.824 4.576 14.746 1.00 86.86 N ANISOU 2502 N ASN A 307 11391 9886 11728 -1203 -1439 1702 N ATOM 2503 CA ASN A 307 -39.115 5.111 13.591 1.00 83.87 C ANISOU 2503 CA ASN A 307 11068 9693 11108 -1306 -1674 1960 C ATOM 2504 C ASN A 307 -38.513 6.476 13.901 1.00 90.85 C ANISOU 2504 C ASN A 307 12128 10409 11981 -1379 -1799 2178 C ATOM 2505 O ASN A 307 -39.233 7.462 14.059 1.00 92.53 O ANISOU 2505 O ASN A 307 12363 10363 12432 -1301 -1938 2205 O ATOM 2506 CB ASN A 307 -40.051 5.204 12.385 1.00 71.75 C ANISOU 2506 CB ASN A 307 9406 8227 9629 -1244 -1920 1980 C ATOM 2507 CG ASN A 307 -39.432 5.953 11.224 1.00 78.60 C ANISOU 2507 CG ASN A 307 10379 9243 10241 -1359 -2180 2277 C ATOM 2508 OD1 ASN A 307 -40.021 6.893 10.692 1.00114.43 O ANISOU 2508 OD1 ASN A 307 14933 13658 14886 -1315 -2454 2420 O ATOM 2509 ND2 ASN A 307 -38.231 5.548 10.833 1.00 76.20 N ANISOU 2509 ND2 ASN A 307 10149 9196 9608 -1509 -2090 2379 N ATOM 2510 N VAL A 308 -37.188 6.526 13.983 1.00 87.87 N ANISOU 2510 N VAL A 308 11863 10168 11355 -1530 -1749 2324 N ATOM 2511 CA VAL A 308 -36.487 7.745 14.367 1.00 80.37 C ANISOU 2511 CA VAL A 308 11084 9063 10388 -1637 -1843 2515 C ATOM 2512 C VAL A 308 -36.334 8.699 13.186 1.00 95.40 C ANISOU 2512 C VAL A 308 13048 11006 12194 -1720 -2113 2790 C ATOM 2513 O VAL A 308 -35.839 8.316 12.126 1.00 94.66 O ANISOU 2513 O VAL A 308 12925 11197 11847 -1813 -2160 2909 O ATOM 2514 CB VAL A 308 -35.094 7.430 14.946 1.00 65.82 C ANISOU 2514 CB VAL A 308 9311 7358 8341 -1782 -1699 2564 C ATOM 2515 CG1 VAL A 308 -34.493 8.671 15.581 1.00 59.48 C ANISOU 2515 CG1 VAL A 308 8682 6349 7569 -1898 -1783 2703 C ATOM 2516 CG2 VAL A 308 -35.189 6.305 15.965 1.00 56.68 C ANISOU 2516 CG2 VAL A 308 8107 6203 7226 -1703 -1452 2328 C ATOM 2517 N GLY A 309 -36.764 9.942 13.377 1.00113.03 N ANISOU 2517 N GLY A 309 15383 12939 14626 -1691 -2277 2889 N ATOM 2518 CA GLY A 309 -36.668 10.953 12.341 1.00119.67 C ANISOU 2518 CA GLY A 309 16318 13753 15397 -1768 -2550 3181 C ATOM 2519 C GLY A 309 -37.838 10.921 11.378 1.00125.48 C ANISOU 2519 C GLY A 309 16950 14493 16233 -1626 -2767 3195 C ATOM 2520 O GLY A 309 -37.800 11.549 10.320 1.00134.34 O ANISOU 2520 O GLY A 309 18152 15657 17233 -1690 -3016 3455 O ATOM 2521 N GLY A 310 -38.882 10.185 11.744 1.00116.16 N ANISOU 2521 N GLY A 310 15594 13271 15272 -1444 -2680 2922 N ATOM 2522 CA GLY A 310 -40.057 10.061 10.902 1.00116.73 C ANISOU 2522 CA GLY A 310 15521 13355 15477 -1303 -2897 2898 C ATOM 2523 C GLY A 310 -41.232 10.894 11.376 1.00116.86 C ANISOU 2523 C GLY A 310 15469 12988 15943 -1105 -3023 2829 C ATOM 2524 O GLY A 310 -41.203 11.470 12.464 1.00116.55 O ANISOU 2524 O GLY A 310 15500 12664 16118 -1069 -2888 2747 O ATOM 2525 N GLY A 311 -42.270 10.954 10.547 1.00114.25 N ANISOU 2525 N GLY A 311 14996 12651 15762 -975 -3289 2852 N ATOM 2526 CA GLY A 311 -43.481 11.682 10.875 1.00114.86 C ANISOU 2526 CA GLY A 311 14947 12375 16319 -755 -3431 2777 C ATOM 2527 C GLY A 311 -43.490 13.093 10.323 1.00119.89 C ANISOU 2527 C GLY A 311 15735 12776 17042 -737 -3777 3105 C ATOM 2528 O GLY A 311 -44.551 13.689 10.135 1.00132.91 O ANISOU 2528 O GLY A 311 17256 14180 19063 -539 -4017 3117 O ATOM 2529 N ASP A 312 -42.303 13.632 10.063 1.00113.56 N ANISOU 2529 N ASP A 312 15197 12033 15919 -942 -3804 3377 N ATOM 2530 CA ASP A 312 -42.181 14.955 9.463 1.00115.88 C ANISOU 2530 CA ASP A 312 15678 12107 16243 -968 -4126 3732 C ATOM 2531 C ASP A 312 -41.101 14.958 8.387 1.00113.21 C ANISOU 2531 C ASP A 312 15546 12080 15389 -1225 -4234 4055 C ATOM 2532 O ASP A 312 -39.934 14.684 8.667 1.00100.37 O ANISOU 2532 O ASP A 312 14034 10628 13474 -1432 -3994 4067 O ATOM 2533 CB ASP A 312 -41.870 16.002 10.535 1.00113.90 C ANISOU 2533 CB ASP A 312 15578 11453 16245 -967 -4009 3726 C ATOM 2534 CG ASP A 312 -42.157 17.422 10.073 1.00117.81 C ANISOU 2534 CG ASP A 312 16216 11590 16958 -905 -4353 4030 C ATOM 2535 OD1 ASP A 312 -42.135 17.676 8.851 1.00118.60 O ANISOU 2535 OD1 ASP A 312 16396 11811 16857 -959 -4673 4348 O ATOM 2536 OD2 ASP A 312 -42.403 18.288 10.939 1.00119.58 O ANISOU 2536 OD2 ASP A 312 16490 11398 17549 -808 -4299 3950 O ATOM 2537 N THR A 313 -41.494 15.267 7.156 1.00128.20 N ANISOU 2537 N THR A 313 17486 14050 17172 -1216 -4597 4317 N ATOM 2538 CA THR A 313 -40.543 15.336 6.055 1.00133.32 C ANISOU 2538 CA THR A 313 18354 14988 17312 -1473 -4698 4637 C ATOM 2539 C THR A 313 -39.956 16.736 5.920 1.00143.57 C ANISOU 2539 C THR A 313 19927 16014 18609 -1595 -4843 4991 C ATOM 2540 O THR A 313 -38.972 16.938 5.209 1.00147.39 O ANISOU 2540 O THR A 313 20560 16741 18699 -1833 -4742 5122 O ATOM 2541 CB THR A 313 -41.193 14.935 4.719 1.00133.16 C ANISOU 2541 CB THR A 313 18293 15222 17080 -1447 -5018 4754 C ATOM 2542 OG1 THR A 313 -40.218 15.004 3.671 1.00134.53 O ANISOU 2542 OG1 THR A 313 18700 15693 16723 -1720 -5040 5024 O ATOM 2543 CG2 THR A 313 -42.354 15.859 4.389 1.00134.64 C ANISOU 2543 CG2 THR A 313 18449 15075 17632 -1226 -5451 4921 C ATOM 2544 N HIS A 314 -40.563 17.698 6.606 1.00152.25 N ANISOU 2544 N HIS A 314 21022 16650 20174 -1417 -4943 4981 N ATOM 2545 CA HIS A 314 -40.085 19.075 6.576 1.00155.56 C ANISOU 2545 CA HIS A 314 21633 16823 20648 -1502 -4955 5134 C ATOM 2546 C HIS A 314 -39.061 19.316 7.677 1.00147.57 C ANISOU 2546 C HIS A 314 20719 15707 19645 -1658 -4633 5028 C ATOM 2547 O HIS A 314 -38.391 20.349 7.701 1.00151.58 O ANISOU 2547 O HIS A 314 21388 16075 20128 -1790 -4591 5135 O ATOM 2548 CB HIS A 314 -41.252 20.054 6.708 1.00167.19 C ANISOU 2548 CB HIS A 314 23055 17843 22625 -1228 -5226 5163 C ATOM 2549 CG HIS A 314 -42.202 20.017 5.552 1.00174.53 C ANISOU 2549 CG HIS A 314 23898 18869 23548 -1089 -5584 5292 C ATOM 2550 ND1 HIS A 314 -41.988 20.728 4.391 1.00178.15 N ANISOU 2550 ND1 HIS A 314 24528 19414 23749 -1200 -5769 5555 N ATOM 2551 CD2 HIS A 314 -43.367 19.350 5.375 1.00173.73 C ANISOU 2551 CD2 HIS A 314 23550 18794 23664 -857 -5798 5186 C ATOM 2552 CE1 HIS A 314 -42.981 20.503 3.550 1.00177.13 C ANISOU 2552 CE1 HIS A 314 24281 19364 23656 -1046 -6086 5609 C ATOM 2553 NE2 HIS A 314 -43.831 19.670 4.122 1.00174.96 N ANISOU 2553 NE2 HIS A 314 23736 19065 23676 -836 -6116 5378 N ATOM 2554 N SER A 315 -38.944 18.356 8.587 1.00129.52 N ANISOU 2554 N SER A 315 18334 13486 17393 -1648 -4415 4817 N ATOM 2555 CA SER A 315 -37.929 18.411 9.628 1.00103.19 C ANISOU 2555 CA SER A 315 15080 10116 14013 -1813 -4111 4695 C ATOM 2556 C SER A 315 -36.548 18.216 9.019 1.00101.10 C ANISOU 2556 C SER A 315 14887 10256 13271 -2107 -3954 4798 C ATOM 2557 O SER A 315 -35.601 18.927 9.354 1.00126.49 O ANISOU 2557 O SER A 315 18211 13416 16434 -2278 -3831 4821 O ATOM 2558 CB SER A 315 -38.192 17.351 10.698 1.00 87.07 C ANISOU 2558 CB SER A 315 12842 8160 12080 -1698 -3815 4290 C ATOM 2559 OG SER A 315 -39.326 17.686 11.477 1.00 89.46 O ANISOU 2559 OG SER A 315 13044 8097 12850 -1438 -3820 4065 O ATOM 2560 N TRP A 316 -36.447 17.249 8.114 1.00 89.89 N ANISOU 2560 N TRP A 316 13391 9238 11524 -2161 -3958 4840 N ATOM 2561 CA TRP A 316 -35.190 16.951 7.444 1.00 88.28 C ANISOU 2561 CA TRP A 316 13223 9427 10892 -2420 -3783 4909 C ATOM 2562 C TRP A 316 -34.880 17.984 6.368 1.00100.40 C ANISOU 2562 C TRP A 316 14905 10962 12279 -2540 -3918 5145 C ATOM 2563 O TRP A 316 -33.716 18.233 6.060 1.00 95.37 O ANISOU 2563 O TRP A 316 14331 10498 11406 -2771 -3759 5215 O ATOM 2564 CB TRP A 316 -35.228 15.548 6.839 1.00 82.07 C ANISOU 2564 CB TRP A 316 12317 9051 9813 -2432 -3718 4845 C ATOM 2565 CG TRP A 316 -35.328 14.468 7.869 1.00 82.96 C ANISOU 2565 CG TRP A 316 12275 9211 10033 -2339 -3513 4579 C ATOM 2566 CD1 TRP A 316 -36.467 13.998 8.456 1.00 81.75 C ANISOU 2566 CD1 TRP A 316 11954 8924 10184 -2076 -3508 4298 C ATOM 2567 CD2 TRP A 316 -34.245 13.725 8.441 1.00 97.12 C ANISOU 2567 CD2 TRP A 316 14000 11232 11668 -2470 -3200 4435 C ATOM 2568 NE1 TRP A 316 -36.160 13.005 9.355 1.00 84.70 N ANISOU 2568 NE1 TRP A 316 12191 9421 10569 -2049 -3203 4002 N ATOM 2569 CE2 TRP A 316 -34.802 12.819 9.364 1.00 98.21 C ANISOU 2569 CE2 TRP A 316 13961 11350 12003 -2277 -3029 4086 C ATOM 2570 CE3 TRP A 316 -32.859 13.738 8.260 1.00 97.67 C ANISOU 2570 CE3 TRP A 316 14110 11523 11475 -2720 -3033 4535 C ATOM 2571 CZ2 TRP A 316 -34.022 11.934 10.106 1.00100.17 C ANISOU 2571 CZ2 TRP A 316 14115 11772 12172 -2326 -2743 3893 C ATOM 2572 CZ3 TRP A 316 -32.086 12.859 8.996 1.00 93.42 C ANISOU 2572 CZ3 TRP A 316 13455 11158 10881 -2769 -2772 4362 C ATOM 2573 CH2 TRP A 316 -32.669 11.969 9.907 1.00 96.30 C ANISOU 2573 CH2 TRP A 316 13671 11487 11433 -2561 -2635 4038 C ATOM 2574 N GLN A 317 -35.923 18.580 5.799 1.00120.42 N ANISOU 2574 N GLN A 317 17488 13297 14971 -2382 -4214 5271 N ATOM 2575 CA GLN A 317 -35.748 19.645 4.818 1.00141.01 C ANISOU 2575 CA GLN A 317 20264 15846 17468 -2478 -4368 5518 C ATOM 2576 C GLN A 317 -35.099 20.863 5.464 1.00151.75 C ANISOU 2576 C GLN A 317 21750 16901 19008 -2575 -4295 5570 C ATOM 2577 O GLN A 317 -34.170 21.448 4.910 1.00153.45 O ANISOU 2577 O GLN A 317 22091 17205 19008 -2795 -4226 5723 O ATOM 2578 CB GLN A 317 -37.086 20.031 4.185 1.00149.36 C ANISOU 2578 CB GLN A 317 21326 16717 18707 -2254 -4729 5633 C ATOM 2579 CG GLN A 317 -37.586 19.046 3.144 1.00150.41 C ANISOU 2579 CG GLN A 317 21390 17202 18557 -2226 -4853 5644 C ATOM 2580 CD GLN A 317 -38.847 19.522 2.451 1.00149.99 C ANISOU 2580 CD GLN A 317 21336 16976 18678 -2020 -5245 5773 C ATOM 2581 OE1 GLN A 317 -39.623 20.296 3.011 1.00148.31 O ANISOU 2581 OE1 GLN A 317 21088 16355 18909 -1812 -5417 5780 O ATOM 2582 NE2 GLN A 317 -39.053 19.065 1.222 1.00153.92 N ANISOU 2582 NE2 GLN A 317 21870 17780 18832 -2074 -5386 5864 N ATOM 2583 N ARG A 318 -35.595 21.236 6.641 1.00152.25 N ANISOU 2583 N ARG A 318 21781 16597 19471 -2415 -4303 5432 N ATOM 2584 CA ARG A 318 -34.996 22.316 7.417 1.00151.27 C ANISOU 2584 CA ARG A 318 21774 16173 19528 -2507 -4216 5427 C ATOM 2585 C ARG A 318 -33.575 21.948 7.823 1.00145.46 C ANISOU 2585 C ARG A 318 21025 15699 18546 -2769 -3926 5345 C ATOM 2586 O ARG A 318 -32.705 22.811 7.940 1.00154.41 O ANISOU 2586 O ARG A 318 22268 16742 19658 -2952 -3860 5420 O ATOM 2587 CB ARG A 318 -35.836 22.621 8.658 1.00153.80 C ANISOU 2587 CB ARG A 318 22058 16067 20310 -2281 -4239 5239 C ATOM 2588 CG ARG A 318 -37.167 23.290 8.367 1.00168.62 C ANISOU 2588 CG ARG A 318 23936 17594 22537 -2010 -4528 5318 C ATOM 2589 CD ARG A 318 -37.999 23.414 9.632 1.00167.89 C ANISOU 2589 CD ARG A 318 23770 17101 22919 -1777 -4491 5075 C ATOM 2590 NE ARG A 318 -39.215 24.192 9.416 1.00171.88 N ANISOU 2590 NE ARG A 318 24248 17229 23829 -1504 -4752 5132 N ATOM 2591 CZ ARG A 318 -39.318 25.494 9.656 1.00174.32 C ANISOU 2591 CZ ARG A 318 24686 17137 24411 -1456 -4813 5184 C ATOM 2592 NH1 ARG A 318 -38.277 26.170 10.124 1.00170.70 N ANISOU 2592 NH1 ARG A 318 24402 16603 23854 -1679 -4640 5185 N ATOM 2593 NH2 ARG A 318 -40.464 26.122 9.431 1.00181.38 N ANISOU 2593 NH2 ARG A 318 25520 17703 25694 -1182 -5052 5227 N ATOM 2594 N LEU A 319 -33.352 20.655 8.037 1.00135.55 N ANISOU 2594 N LEU A 319 19621 14760 17123 -2780 -3764 5191 N ATOM 2595 CA LEU A 319 -32.038 20.152 8.411 1.00118.32 C ANISOU 2595 CA LEU A 319 17378 12852 14727 -2998 -3502 5102 C ATOM 2596 C LEU A 319 -31.110 20.106 7.201 1.00112.53 C ANISOU 2596 C LEU A 319 16667 12460 13629 -3223 -3438 5272 C ATOM 2597 O LEU A 319 -29.921 20.404 7.310 1.00120.45 O ANISOU 2597 O LEU A 319 17678 13561 14526 -3443 -3287 5296 O ATOM 2598 CB LEU A 319 -32.157 18.764 9.042 1.00107.48 C ANISOU 2598 CB LEU A 319 15840 11680 13318 -2916 -3352 4888 C ATOM 2599 CG LEU A 319 -30.890 18.184 9.671 1.00 93.14 C ANISOU 2599 CG LEU A 319 13933 10101 11355 -3093 -3097 4765 C ATOM 2600 CD1 LEU A 319 -30.409 19.069 10.809 1.00 84.40 C ANISOU 2600 CD1 LEU A 319 12907 8708 10453 -3166 -3061 4690 C ATOM 2601 CD2 LEU A 319 -31.134 16.765 10.158 1.00 94.16 C ANISOU 2601 CD2 LEU A 319 13913 10421 11442 -2989 -2970 4584 C ATOM 2602 N ALA A 320 -31.660 19.735 6.048 1.00103.73 N ANISOU 2602 N ALA A 320 15564 11524 12326 -3173 -3554 5386 N ATOM 2603 CA ALA A 320 -30.881 19.651 4.816 1.00 97.93 C ANISOU 2603 CA ALA A 320 14877 11111 11222 -3382 -3481 5540 C ATOM 2604 C ALA A 320 -30.477 21.036 4.323 1.00106.37 C ANISOU 2604 C ALA A 320 16137 11985 12296 -3528 -3568 5771 C ATOM 2605 O ALA A 320 -29.439 21.195 3.679 1.00 99.84 O ANISOU 2605 O ALA A 320 15353 11363 11218 -3767 -3428 5880 O ATOM 2606 CB ALA A 320 -31.664 18.915 3.740 1.00 93.98 C ANISOU 2606 CB ALA A 320 14369 10833 10506 -3291 -3602 5586 C ATOM 2607 N GLN A 321 -31.303 22.033 4.623 1.00113.17 N ANISOU 2607 N GLN A 321 17109 12437 13455 -3381 -3790 5846 N ATOM 2608 CA GLN A 321 -31.000 23.411 4.252 1.00128.42 C ANISOU 2608 CA GLN A 321 19236 14123 15437 -3499 -3884 6069 C ATOM 2609 C GLN A 321 -29.763 23.906 4.991 1.00137.55 C ANISOU 2609 C GLN A 321 20396 15230 16637 -3717 -3682 6021 C ATOM 2610 O GLN A 321 -28.888 24.537 4.398 1.00144.54 O ANISOU 2610 O GLN A 321 21386 16168 17363 -3950 -3619 6193 O ATOM 2611 CB GLN A 321 -32.190 24.328 4.541 1.00135.10 C ANISOU 2611 CB GLN A 321 20176 14508 16648 -3263 -4157 6131 C ATOM 2612 CG GLN A 321 -33.337 24.191 3.553 1.00141.79 C ANISOU 2612 CG GLN A 321 21054 15368 17451 -3083 -4427 6266 C ATOM 2613 CD GLN A 321 -34.499 25.110 3.876 1.00140.47 C ANISOU 2613 CD GLN A 321 20942 14728 17700 -2828 -4700 6321 C ATOM 2614 OE1 GLN A 321 -34.445 25.887 4.829 1.00138.84 O ANISOU 2614 OE1 GLN A 321 20774 14169 17811 -2791 -4667 6253 O ATOM 2615 NE2 GLN A 321 -35.560 25.024 3.081 1.00140.06 N ANISOU 2615 NE2 GLN A 321 20889 14665 17661 -2649 -4973 6434 N ATOM 2616 N GLU A 322 -29.695 23.615 6.286 1.00135.46 N ANISOU 2616 N GLU A 322 20020 14865 16585 -3650 -3586 5788 N ATOM 2617 CA GLU A 322 -28.550 24.016 7.093 1.00135.69 C ANISOU 2617 CA GLU A 322 20035 14855 16665 -3852 -3422 5715 C ATOM 2618 C GLU A 322 -27.363 23.087 6.855 1.00126.50 C ANISOU 2618 C GLU A 322 18714 14139 15210 -4055 -3186 5663 C ATOM 2619 O GLU A 322 -26.212 23.480 7.038 1.00132.00 O ANISOU 2619 O GLU A 322 19400 14889 15866 -4289 -3062 5689 O ATOM 2620 CB GLU A 322 -28.918 24.041 8.577 1.00139.73 C ANISOU 2620 CB GLU A 322 20508 15096 17486 -3714 -3413 5480 C ATOM 2621 CG GLU A 322 -30.054 24.996 8.912 1.00150.63 C ANISOU 2621 CG GLU A 322 22030 15998 19204 -3506 -3613 5503 C ATOM 2622 CD GLU A 322 -30.131 25.316 10.392 1.00155.17 C ANISOU 2622 CD GLU A 322 22623 16267 20070 -3450 -3557 5276 C ATOM 2623 OE1 GLU A 322 -29.090 25.220 11.076 1.00157.11 O ANISOU 2623 OE1 GLU A 322 22830 16619 20246 -3641 -3404 5168 O ATOM 2624 OE2 GLU A 322 -31.231 25.663 10.871 1.00154.68 O ANISOU 2624 OE2 GLU A 322 22609 15853 20307 -3217 -3667 5198 O ATOM 2625 N ALA A 323 -27.649 21.855 6.446 1.00112.38 N ANISOU 2625 N ALA A 323 16795 12663 13240 -3964 -3126 5585 N ATOM 2626 CA ALA A 323 -26.596 20.907 6.101 1.00 94.28 C ANISOU 2626 CA ALA A 323 14345 10797 10679 -4131 -2895 5537 C ATOM 2627 C ALA A 323 -25.891 21.350 4.825 1.00 98.17 C ANISOU 2627 C ALA A 323 14932 11462 10905 -4359 -2839 5760 C ATOM 2628 O ALA A 323 -24.705 21.086 4.635 1.00105.75 O ANISOU 2628 O ALA A 323 15793 12679 11709 -4575 -2632 5762 O ATOM 2629 CB ALA A 323 -27.164 19.507 5.938 1.00 91.19 C ANISOU 2629 CB ALA A 323 13815 10665 10166 -3969 -2845 5399 C ATOM 2630 N ARG A 324 -26.634 22.025 3.954 1.00106.78 N ANISOU 2630 N ARG A 324 16214 12404 11952 -4309 -3027 5954 N ATOM 2631 CA ARG A 324 -26.079 22.569 2.721 1.00112.74 C ANISOU 2631 CA ARG A 324 17114 13275 12447 -4524 -2994 6194 C ATOM 2632 C ARG A 324 -25.155 23.746 3.021 1.00119.15 C ANISOU 2632 C ARG A 324 18013 13885 13372 -4745 -2946 6309 C ATOM 2633 O ARG A 324 -24.122 23.920 2.373 1.00110.99 O ANISOU 2633 O ARG A 324 16998 13041 12134 -5003 -2779 6427 O ATOM 2634 CB ARG A 324 -27.201 23.006 1.775 1.00115.90 C ANISOU 2634 CB ARG A 324 17712 13541 12784 -4395 -3250 6383 C ATOM 2635 CG ARG A 324 -26.719 23.644 0.480 1.00120.22 C ANISOU 2635 CG ARG A 324 18458 14174 13045 -4614 -3238 6658 C ATOM 2636 CD ARG A 324 -26.149 22.608 -0.476 1.00120.26 C ANISOU 2636 CD ARG A 324 18401 14650 12644 -4754 -3026 6634 C ATOM 2637 NE ARG A 324 -27.181 21.701 -0.970 1.00128.16 N ANISOU 2637 NE ARG A 324 19382 15806 13509 -4557 -3152 6564 N ATOM 2638 CZ ARG A 324 -26.964 20.733 -1.854 1.00126.22 C ANISOU 2638 CZ ARG A 324 19107 15949 12903 -4634 -3009 6523 C ATOM 2639 NH1 ARG A 324 -25.747 20.541 -2.345 1.00127.71 N ANISOU 2639 NH1 ARG A 324 19273 16411 12840 -4894 -2719 6544 N ATOM 2640 NH2 ARG A 324 -27.964 19.955 -2.247 1.00118.57 N ANISOU 2640 NH2 ARG A 324 18127 15094 11830 -4455 -3152 6451 N ATOM 2641 N VAL A 325 -25.536 24.546 4.011 1.00119.24 N ANISOU 2641 N VAL A 325 18081 13509 13718 -4648 -3080 6266 N ATOM 2642 CA VAL A 325 -24.763 25.719 4.403 1.00118.16 C ANISOU 2642 CA VAL A 325 18042 13130 13725 -4847 -3058 6357 C ATOM 2643 C VAL A 325 -23.414 25.322 4.998 1.00126.48 C ANISOU 2643 C VAL A 325 18903 14407 14745 -5065 -2823 6227 C ATOM 2644 O VAL A 325 -22.385 25.919 4.680 1.00136.59 O ANISOU 2644 O VAL A 325 20217 15724 15955 -5336 -2713 6354 O ATOM 2645 CB VAL A 325 -25.532 26.584 5.423 1.00115.98 C ANISOU 2645 CB VAL A 325 17865 12376 13825 -4677 -3242 6295 C ATOM 2646 CG1 VAL A 325 -24.703 27.789 5.837 1.00117.87 C ANISOU 2646 CG1 VAL A 325 18215 12360 14211 -4899 -3212 6374 C ATOM 2647 CG2 VAL A 325 -26.865 27.028 4.843 1.00112.83 C ANISOU 2647 CG2 VAL A 325 17630 11733 13508 -4449 -3491 6437 C ATOM 2648 N TRP A 326 -23.426 24.305 5.855 1.00125.02 N ANISOU 2648 N TRP A 326 18514 14370 14618 -4949 -2753 5982 N ATOM 2649 CA TRP A 326 -22.207 23.841 6.511 1.00126.44 C ANISOU 2649 CA TRP A 326 18486 14762 14793 -5125 -2565 5851 C ATOM 2650 C TRP A 326 -21.247 23.163 5.536 1.00134.03 C ANISOU 2650 C TRP A 326 19316 16150 15460 -5317 -2342 5920 C ATOM 2651 O TRP A 326 -20.076 22.956 5.852 1.00136.31 O ANISOU 2651 O TRP A 326 19431 16620 15742 -5512 -2177 5870 O ATOM 2652 CB TRP A 326 -22.550 22.889 7.659 1.00115.94 C ANISOU 2652 CB TRP A 326 16993 13469 13591 -4932 -2562 5589 C ATOM 2653 CG TRP A 326 -22.971 23.595 8.914 1.00114.92 C ANISOU 2653 CG TRP A 326 16956 12950 13759 -4846 -2698 5476 C ATOM 2654 CD1 TRP A 326 -24.203 24.110 9.192 1.00114.01 C ANISOU 2654 CD1 TRP A 326 17004 12483 13831 -4626 -2871 5461 C ATOM 2655 CD2 TRP A 326 -22.157 23.861 10.064 1.00120.32 C ANISOU 2655 CD2 TRP A 326 17577 13552 14587 -4983 -2667 5353 C ATOM 2656 NE1 TRP A 326 -24.208 24.681 10.441 1.00119.08 N ANISOU 2656 NE1 TRP A 326 17703 12825 14719 -4619 -2921 5323 N ATOM 2657 CE2 TRP A 326 -22.964 24.540 10.998 1.00121.68 C ANISOU 2657 CE2 TRP A 326 17906 13318 15010 -4843 -2809 5254 C ATOM 2658 CE3 TRP A 326 -20.826 23.589 10.394 1.00120.07 C ANISOU 2658 CE3 TRP A 326 17366 13752 14503 -5216 -2540 5316 C ATOM 2659 CZ2 TRP A 326 -22.483 24.953 12.239 1.00123.90 C ANISOU 2659 CZ2 TRP A 326 18200 13422 15454 -4940 -2826 5110 C ATOM 2660 CZ3 TRP A 326 -20.350 24.000 11.626 1.00124.40 C ANISOU 2660 CZ3 TRP A 326 17910 14130 15227 -5310 -2589 5190 C ATOM 2661 CH2 TRP A 326 -21.177 24.674 12.533 1.00128.52 C ANISOU 2661 CH2 TRP A 326 18619 14251 15962 -5178 -2730 5084 C ATOM 2662 N LEU A 327 -21.746 22.817 4.353 1.00133.44 N ANISOU 2662 N LEU A 327 19321 16235 15144 -5265 -2337 6030 N ATOM 2663 CA LEU A 327 -20.896 22.264 3.305 1.00123.30 C ANISOU 2663 CA LEU A 327 17957 15336 13555 -5457 -2106 6101 C ATOM 2664 C LEU A 327 -20.008 23.353 2.712 1.00125.74 C ANISOU 2664 C LEU A 327 18391 15583 13803 -5754 -2029 6320 C ATOM 2665 O LEU A 327 -18.919 23.076 2.211 1.00121.35 O ANISOU 2665 O LEU A 327 17718 15309 13083 -5982 -1784 6351 O ATOM 2666 CB LEU A 327 -21.741 21.610 2.208 1.00117.31 C ANISOU 2666 CB LEU A 327 17286 14755 12533 -5326 -2136 6147 C ATOM 2667 CG LEU A 327 -22.392 20.270 2.555 1.00110.62 C ANISOU 2667 CG LEU A 327 16276 14082 11673 -5088 -2127 5926 C ATOM 2668 CD1 LEU A 327 -23.273 19.788 1.413 1.00103.94 C ANISOU 2668 CD1 LEU A 327 15551 13378 10564 -4984 -2196 5989 C ATOM 2669 CD2 LEU A 327 -21.333 19.233 2.892 1.00100.94 C ANISOU 2669 CD2 LEU A 327 14770 13189 10395 -5181 -1856 5762 C ATOM 2670 N GLY A 328 -20.482 24.594 2.777 1.00114.74 N ANISOU 2670 N GLY A 328 17232 13808 12556 -5751 -2226 6472 N ATOM 2671 CA GLY A 328 -19.726 25.730 2.283 1.00119.71 C ANISOU 2671 CA GLY A 328 18010 14316 13159 -6029 -2171 6694 C ATOM 2672 C GLY A 328 -18.720 26.224 3.305 1.00123.69 C ANISOU 2672 C GLY A 328 18387 14710 13899 -6213 -2099 6615 C ATOM 2673 O GLY A 328 -17.852 27.040 2.995 1.00123.81 O ANISOU 2673 O GLY A 328 18465 14672 13907 -6489 -2000 6768 O ATOM 2674 N TYR A 329 -18.843 25.725 4.530 1.00119.64 N ANISOU 2674 N TYR A 329 17705 14162 13592 -6069 -2154 6378 N ATOM 2675 CA TYR A 329 -17.927 26.084 5.606 1.00115.46 C ANISOU 2675 CA TYR A 329 17045 13546 13280 -6232 -2118 6275 C ATOM 2676 C TYR A 329 -16.612 25.321 5.461 1.00125.50 C ANISOU 2676 C TYR A 329 18028 15221 14436 -6446 -1859 6222 C ATOM 2677 O TYR A 329 -16.597 24.207 4.937 1.00113.81 O ANISOU 2677 O TYR A 329 16402 14079 12762 -6371 -1720 6164 O ATOM 2678 CB TYR A 329 -18.566 25.801 6.971 1.00111.30 C ANISOU 2678 CB TYR A 329 16464 12838 12986 -6002 -2274 6044 C ATOM 2679 CG TYR A 329 -19.732 26.706 7.310 1.00111.79 C ANISOU 2679 CG TYR A 329 16785 12452 13238 -5817 -2505 6072 C ATOM 2680 CD1 TYR A 329 -19.984 27.857 6.573 1.00116.12 C ANISOU 2680 CD1 TYR A 329 17585 12742 13792 -5892 -2584 6305 C ATOM 2681 CD2 TYR A 329 -20.575 26.414 8.374 1.00109.94 C ANISOU 2681 CD2 TYR A 329 16544 12041 13188 -5569 -2631 5868 C ATOM 2682 CE1 TYR A 329 -21.047 28.686 6.881 1.00116.93 C ANISOU 2682 CE1 TYR A 329 17906 12420 14103 -5708 -2792 6334 C ATOM 2683 CE2 TYR A 329 -21.640 27.237 8.690 1.00109.06 C ANISOU 2683 CE2 TYR A 329 16649 11510 13278 -5393 -2816 5880 C ATOM 2684 CZ TYR A 329 -21.871 28.371 7.941 1.00113.39 C ANISOU 2684 CZ TYR A 329 17426 11806 13853 -5457 -2901 6113 C ATOM 2685 OH TYR A 329 -22.929 29.194 8.252 1.00114.53 O ANISOU 2685 OH TYR A 329 17769 11517 14230 -5267 -3083 6129 O ATOM 2686 N PRO A 330 -15.502 25.919 5.928 1.00131.59 N ANISOU 2686 N PRO A 330 18705 15949 15344 -6714 -1789 6234 N ATOM 2687 CA PRO A 330 -14.167 25.309 5.842 1.00118.63 C ANISOU 2687 CA PRO A 330 16756 14666 13653 -6937 -1543 6188 C ATOM 2688 C PRO A 330 -14.052 23.972 6.575 1.00125.32 C ANISOU 2688 C PRO A 330 17308 15776 14532 -6778 -1508 5961 C ATOM 2689 O PRO A 330 -13.076 23.250 6.367 1.00114.60 O ANISOU 2689 O PRO A 330 15667 14755 13120 -6907 -1290 5918 O ATOM 2690 CB PRO A 330 -13.256 26.361 6.489 1.00121.71 C ANISOU 2690 CB PRO A 330 17128 14851 14264 -7213 -1566 6220 C ATOM 2691 CG PRO A 330 -14.164 27.228 7.291 1.00121.32 C ANISOU 2691 CG PRO A 330 17332 14357 14406 -7073 -1839 6192 C ATOM 2692 CD PRO A 330 -15.447 27.261 6.531 1.00120.35 C ANISOU 2692 CD PRO A 330 17461 14119 14149 -6831 -1935 6293 C ATOM 2693 N CYS A 331 -15.028 23.665 7.426 1.00128.74 N ANISOU 2693 N CYS A 331 17803 16046 15067 -6506 -1708 5820 N ATOM 2694 CA CYS A 331 -15.047 22.419 8.191 1.00115.25 C ANISOU 2694 CA CYS A 331 15855 14541 13394 -6337 -1697 5617 C ATOM 2695 C CYS A 331 -14.890 21.183 7.308 1.00121.71 C ANISOU 2695 C CYS A 331 16491 15762 13993 -6277 -1474 5598 C ATOM 2696 O CYS A 331 -14.215 20.225 7.685 1.00105.82 O ANISOU 2696 O CYS A 331 14183 14015 12010 -6284 -1354 5482 O ATOM 2697 CB CYS A 331 -16.348 22.315 8.988 1.00102.38 C ANISOU 2697 CB CYS A 331 14385 12651 11863 -6036 -1916 5493 C ATOM 2698 SG CYS A 331 -16.869 23.860 9.765 1.00165.49 S ANISOU 2698 SG CYS A 331 22675 20116 20086 -6057 -2156 5518 S ATOM 2699 N CYS A 332 -15.530 21.204 6.142 1.00142.80 N ANISOU 2699 N CYS A 332 19342 18469 16448 -6217 -1428 5710 N ATOM 2700 CA CYS A 332 -15.452 20.089 5.205 1.00147.59 C ANISOU 2700 CA CYS A 332 19823 19443 16813 -6171 -1209 5685 C ATOM 2701 C CYS A 332 -14.356 20.279 4.157 1.00154.51 C ANISOU 2701 C CYS A 332 20625 20555 17528 -6461 -934 5811 C ATOM 2702 O CYS A 332 -14.081 19.375 3.369 1.00156.91 O ANISOU 2702 O CYS A 332 20802 21185 17630 -6468 -698 5773 O ATOM 2703 CB CYS A 332 -16.800 19.897 4.503 1.00148.78 C ANISOU 2703 CB CYS A 332 20212 19529 16790 -5947 -1319 5718 C ATOM 2704 SG CYS A 332 -18.178 19.552 5.618 1.00180.84 S ANISOU 2704 SG CYS A 332 24339 23334 21039 -5593 -1589 5554 S ATOM 2705 N LYS A 333 -13.726 21.450 4.158 1.00154.17 N ANISOU 2705 N LYS A 333 20663 20338 17577 -6706 -945 5949 N ATOM 2706 CA LYS A 333 -12.758 21.791 3.119 1.00154.90 C ANISOU 2706 CA LYS A 333 20730 20606 17520 -6999 -676 6090 C ATOM 2707 C LYS A 333 -11.319 21.581 3.582 1.00156.48 C ANISOU 2707 C LYS A 333 20565 21001 17891 -7221 -472 6013 C ATOM 2708 O LYS A 333 -10.955 21.949 4.699 1.00152.99 O ANISOU 2708 O LYS A 333 20010 20403 17715 -7266 -618 5950 O ATOM 2709 CB LYS A 333 -12.952 23.242 2.670 1.00157.21 C ANISOU 2709 CB LYS A 333 21351 20584 17798 -7154 -787 6319 C ATOM 2710 CG LYS A 333 -14.406 23.692 2.629 1.00156.42 C ANISOU 2710 CG LYS A 333 21583 20179 17672 -6912 -1083 6386 C ATOM 2711 CD LYS A 333 -15.210 22.958 1.568 1.00155.44 C ANISOU 2711 CD LYS A 333 21575 20244 17241 -6752 -1045 6412 C ATOM 2712 CE LYS A 333 -14.899 23.483 0.178 1.00161.09 C ANISOU 2712 CE LYS A 333 22489 21041 17676 -6974 -886 6641 C ATOM 2713 NZ LYS A 333 -15.798 22.895 -0.851 1.00165.48 N ANISOU 2713 NZ LYS A 333 23213 21744 17918 -6822 -907 6678 N ATOM 2714 N ASN A 334 -10.502 20.994 2.710 1.00158.77 N ANISOU 2714 N ASN A 334 20664 21631 18029 -7364 -132 6010 N ATOM 2715 CA ASN A 334 -9.098 20.736 3.017 1.00155.96 C ANISOU 2715 CA ASN A 334 19912 21489 17857 -7574 100 5931 C ATOM 2716 C ASN A 334 -8.188 21.889 2.600 1.00157.67 C ANISOU 2716 C ASN A 334 20168 21614 18125 -7928 233 6096 C ATOM 2717 O ASN A 334 -8.662 22.975 2.265 1.00163.80 O ANISOU 2717 O ASN A 334 21296 22112 18829 -8005 100 6277 O ATOM 2718 CB ASN A 334 -8.637 19.436 2.352 1.00159.21 C ANISOU 2718 CB ASN A 334 20046 22315 18131 -7531 440 5805 C ATOM 2719 CG ASN A 334 -8.987 19.373 0.877 1.00168.81 C ANISOU 2719 CG ASN A 334 21507 23661 18973 -7570 649 5907 C ATOM 2720 OD1 ASN A 334 -9.294 20.389 0.253 1.00178.52 O ANISOU 2720 OD1 ASN A 334 23071 24700 20058 -7696 585 6107 O ATOM 2721 ND2 ASN A 334 -8.941 18.173 0.311 1.00166.66 N ANISOU 2721 ND2 ASN A 334 21077 23710 18537 -7464 898 5769 N ATOM 2722 N LEU A 335 -6.880 21.645 2.633 1.00156.68 N ANISOU 2722 N LEU A 335 19666 21715 18151 -8142 499 6031 N ATOM 2723 CA LEU A 335 -5.880 22.671 2.338 1.00152.88 C ANISOU 2723 CA LEU A 335 19154 21162 17773 -8503 656 6163 C ATOM 2724 C LEU A 335 -6.030 23.274 0.941 1.00167.40 C ANISOU 2724 C LEU A 335 21317 22985 19304 -8662 854 6376 C ATOM 2725 O LEU A 335 -5.707 24.443 0.727 1.00163.71 O ANISOU 2725 O LEU A 335 21021 22303 18880 -8913 856 6552 O ATOM 2726 CB LEU A 335 -4.464 22.101 2.500 1.00159.28 C ANISOU 2726 CB LEU A 335 19441 22270 18807 -8676 953 6027 C ATOM 2727 CG LEU A 335 -3.904 21.122 1.459 1.00142.71 C ANISOU 2727 CG LEU A 335 17109 20564 16552 -8700 1397 5953 C ATOM 2728 CD1 LEU A 335 -2.397 20.995 1.615 1.00146.67 C ANISOU 2728 CD1 LEU A 335 17106 21264 17359 -8942 1685 5858 C ATOM 2729 CD2 LEU A 335 -4.561 19.750 1.548 1.00137.90 C ANISOU 2729 CD2 LEU A 335 16406 20157 15831 -8359 1382 5779 C ATOM 2730 N ASP A 336 -6.519 22.479 -0.005 1.00169.54 N ANISOU 2730 N ASP A 336 21682 23477 19259 -8524 1014 6361 N ATOM 2731 CA ASP A 336 -6.703 22.950 -1.374 1.00171.16 C ANISOU 2731 CA ASP A 336 22214 23697 19123 -8666 1191 6563 C ATOM 2732 C ASP A 336 -7.857 23.940 -1.473 1.00170.36 C ANISOU 2732 C ASP A 336 22595 23225 18911 -8581 839 6765 C ATOM 2733 O ASP A 336 -7.892 24.780 -2.372 1.00177.58 O ANISOU 2733 O ASP A 336 23808 24030 19635 -8763 905 6995 O ATOM 2734 CB ASP A 336 -6.947 21.774 -2.321 1.00174.97 C ANISOU 2734 CB ASP A 336 22673 24525 19284 -8536 1439 6466 C ATOM 2735 CG ASP A 336 -5.705 20.935 -2.543 1.00179.87 C ANISOU 2735 CG ASP A 336 22844 25509 19989 -8666 1880 6297 C ATOM 2736 OD1 ASP A 336 -4.834 20.910 -1.649 1.00180.63 O ANISOU 2736 OD1 ASP A 336 22561 25619 20451 -8744 1906 6190 O ATOM 2737 OD2 ASP A 336 -5.599 20.300 -3.613 1.00184.63 O ANISOU 2737 OD2 ASP A 336 23467 26382 20302 -8689 2200 6264 O ATOM 2738 N GLY A 337 -8.799 23.837 -0.542 1.00165.61 N ANISOU 2738 N GLY A 337 22060 22423 18442 -8301 474 6679 N ATOM 2739 CA GLY A 337 -9.999 24.650 -0.585 1.00164.67 C ANISOU 2739 CA GLY A 337 22356 21953 18260 -8163 137 6833 C ATOM 2740 C GLY A 337 -11.131 23.877 -1.229 1.00161.24 C ANISOU 2740 C GLY A 337 22096 21633 17536 -7891 57 6808 C ATOM 2741 O GLY A 337 -12.244 24.381 -1.370 1.00158.75 O ANISOU 2741 O GLY A 337 22100 21064 17156 -7734 -223 6922 O ATOM 2742 N SER A 338 -10.836 22.643 -1.628 1.00157.56 N ANISOU 2742 N SER A 338 21406 21547 16912 -7838 309 6650 N ATOM 2743 CA SER A 338 -11.832 21.763 -2.224 1.00153.43 C ANISOU 2743 CA SER A 338 21010 21172 16114 -7595 260 6588 C ATOM 2744 C SER A 338 -12.436 20.848 -1.166 1.00146.38 C ANISOU 2744 C SER A 338 19927 20284 15406 -7285 75 6356 C ATOM 2745 O SER A 338 -12.140 20.981 0.021 1.00142.78 O ANISOU 2745 O SER A 338 19283 19697 15271 -7256 -43 6265 O ATOM 2746 CB SER A 338 -11.215 20.934 -3.352 1.00155.24 C ANISOU 2746 CB SER A 338 21142 21805 16037 -7720 665 6539 C ATOM 2747 OG SER A 338 -12.168 20.050 -3.916 1.00151.28 O ANISOU 2747 OG SER A 338 20764 21452 15263 -7498 614 6457 O ATOM 2748 N LEU A 339 -13.279 19.918 -1.600 1.00143.56 N ANISOU 2748 N LEU A 339 19630 20078 14837 -7065 50 6262 N ATOM 2749 CA LEU A 339 -13.928 18.991 -0.680 1.00127.77 C ANISOU 2749 CA LEU A 339 17473 18086 12989 -6769 -105 6052 C ATOM 2750 C LEU A 339 -13.036 17.788 -0.389 1.00121.36 C ANISOU 2750 C LEU A 339 16259 17610 12242 -6771 187 5837 C ATOM 2751 O LEU A 339 -12.351 17.283 -1.279 1.00126.92 O ANISOU 2751 O LEU A 339 16861 18615 12749 -6909 527 5806 O ATOM 2752 CB LEU A 339 -15.275 18.522 -1.241 1.00123.61 C ANISOU 2752 CB LEU A 339 17176 17555 12234 -6532 -273 6041 C ATOM 2753 CG LEU A 339 -16.371 19.569 -1.465 1.00125.53 C ANISOU 2753 CG LEU A 339 17788 17456 12454 -6456 -609 6234 C ATOM 2754 CD1 LEU A 339 -16.246 20.226 -2.834 1.00134.66 C ANISOU 2754 CD1 LEU A 339 19219 18656 13291 -6665 -519 6466 C ATOM 2755 CD2 LEU A 339 -17.751 18.952 -1.287 1.00120.12 C ANISOU 2755 CD2 LEU A 339 17182 16704 11753 -6138 -852 6133 C ATOM 2756 N VAL A 340 -13.047 17.338 0.862 1.00116.98 N ANISOU 2756 N VAL A 340 15478 16995 11972 -6616 61 5687 N ATOM 2757 CA VAL A 340 -12.290 16.156 1.263 1.00117.65 C ANISOU 2757 CA VAL A 340 15165 17370 12167 -6576 292 5487 C ATOM 2758 C VAL A 340 -12.836 14.919 0.560 1.00120.77 C ANISOU 2758 C VAL A 340 15554 18021 12311 -6404 446 5353 C ATOM 2759 O VAL A 340 -12.081 14.042 0.137 1.00125.64 O ANISOU 2759 O VAL A 340 15915 18952 12871 -6455 783 5227 O ATOM 2760 CB VAL A 340 -12.338 15.945 2.791 1.00112.19 C ANISOU 2760 CB VAL A 340 14283 16532 11811 -6427 70 5377 C ATOM 2761 CG1 VAL A 340 -11.611 14.666 3.182 1.00112.04 C ANISOU 2761 CG1 VAL A 340 13847 16810 11915 -6362 290 5187 C ATOM 2762 CG2 VAL A 340 -11.739 17.141 3.510 1.00116.68 C ANISOU 2762 CG2 VAL A 340 14853 16861 12620 -6618 -76 5482 C ATOM 2763 N GLY A 341 -14.156 14.863 0.428 1.00130.85 N ANISOU 2763 N GLY A 341 17105 19156 13456 -6202 204 5368 N ATOM 2764 CA GLY A 341 -14.810 13.743 -0.217 1.00136.51 C ANISOU 2764 CA GLY A 341 17851 20086 13929 -6041 304 5238 C ATOM 2765 C GLY A 341 -15.489 12.834 0.786 1.00140.28 C ANISOU 2765 C GLY A 341 18198 20518 14583 -5761 158 5068 C ATOM 2766 O GLY A 341 -15.134 12.819 1.964 1.00150.44 O ANISOU 2766 O GLY A 341 19285 21701 16174 -5713 73 5019 O ATOM 2767 N ALA A 342 -16.476 12.078 0.317 1.00140.86 N ANISOU 2767 N ALA A 342 18396 20668 14457 -5586 122 4982 N ATOM 2768 CA ALA A 342 -17.200 11.150 1.175 1.00130.57 C ANISOU 2768 CA ALA A 342 16990 19326 13295 -5323 9 4823 C ATOM 2769 C ALA A 342 -16.566 9.765 1.135 1.00134.37 C ANISOU 2769 C ALA A 342 17158 20134 13762 -5283 339 4617 C ATOM 2770 O ALA A 342 -15.499 9.576 0.550 1.00137.49 O ANISOU 2770 O ALA A 342 17381 20772 14087 -5453 656 4584 O ATOM 2771 CB ALA A 342 -18.660 11.078 0.764 1.00124.90 C ANISOU 2771 CB ALA A 342 16554 18493 12410 -5152 -222 4832 C ATOM 2772 N TRP A 343 -17.229 8.799 1.761 1.00135.86 N ANISOU 2772 N TRP A 343 17266 20319 14037 -5054 280 4471 N ATOM 2773 CA TRP A 343 -16.743 7.426 1.783 1.00138.52 C ANISOU 2773 CA TRP A 343 17304 20938 14391 -4981 583 4264 C ATOM 2774 C TRP A 343 -17.340 6.604 0.649 1.00149.18 C ANISOU 2774 C TRP A 343 18780 22506 15395 -4938 744 4134 C ATOM 2775 O TRP A 343 -18.545 6.657 0.400 1.00138.23 O ANISOU 2775 O TRP A 343 17660 21006 13854 -4834 519 4155 O ATOM 2776 CB TRP A 343 -17.062 6.766 3.127 1.00129.05 C ANISOU 2776 CB TRP A 343 15937 19615 13481 -4768 455 4177 C ATOM 2777 CG TRP A 343 -16.028 7.008 4.182 1.00109.26 C ANISOU 2777 CG TRP A 343 13151 17054 11307 -4827 446 4215 C ATOM 2778 CD1 TRP A 343 -14.704 7.274 3.988 1.00113.44 C ANISOU 2778 CD1 TRP A 343 13439 17740 11925 -5021 649 4241 C ATOM 2779 CD2 TRP A 343 -16.234 7.010 5.599 1.00 93.14 C ANISOU 2779 CD2 TRP A 343 11045 14790 9553 -4701 210 4227 C ATOM 2780 NE1 TRP A 343 -14.072 7.437 5.197 1.00117.97 N ANISOU 2780 NE1 TRP A 343 13784 18212 12829 -5026 526 4272 N ATOM 2781 CE2 TRP A 343 -14.990 7.281 6.202 1.00110.38 C ANISOU 2781 CE2 TRP A 343 12943 17018 11977 -4836 254 4267 C ATOM 2782 CE3 TRP A 343 -17.349 6.807 6.417 1.00 86.42 C ANISOU 2782 CE3 TRP A 343 10354 13706 8778 -4494 -29 4201 C ATOM 2783 CZ2 TRP A 343 -14.830 7.355 7.583 1.00106.22 C ANISOU 2783 CZ2 TRP A 343 12306 16317 11735 -4781 41 4289 C ATOM 2784 CZ3 TRP A 343 -17.188 6.881 7.789 1.00 93.20 C ANISOU 2784 CZ3 TRP A 343 11121 14358 9932 -4386 -214 4165 C ATOM 2785 CH2 TRP A 343 -15.939 7.153 8.358 1.00 96.44 C ANISOU 2785 CH2 TRP A 343 11269 14828 10543 -4540 -190 4222 C ATOM 2786 N THR A 344 -16.490 5.850 -0.042 1.00183.15 N ANISOU 2786 N THR A 344 22881 27119 19587 -5019 1135 3982 N ATOM 2787 CA THR A 344 -16.955 4.931 -1.071 1.00191.02 C ANISOU 2787 CA THR A 344 23975 28348 20258 -4982 1330 3800 C ATOM 2788 C THR A 344 -17.800 3.842 -0.423 1.00184.62 C ANISOU 2788 C THR A 344 23093 27516 19537 -4736 1264 3630 C ATOM 2789 O THR A 344 -17.374 3.211 0.542 1.00185.73 O ANISOU 2789 O THR A 344 22929 27650 19990 -4614 1345 3536 O ATOM 2790 CB THR A 344 -15.785 4.294 -1.844 1.00197.89 C ANISOU 2790 CB THR A 344 24606 29536 21046 -5100 1810 3623 C ATOM 2791 OG1 THR A 344 -14.951 3.562 -0.937 1.00197.75 O ANISOU 2791 OG1 THR A 344 24154 29581 21402 -4997 1996 3488 O ATOM 2792 CG2 THR A 344 -14.956 5.367 -2.535 1.00202.60 C ANISOU 2792 CG2 THR A 344 25286 30156 21537 -5363 1906 3796 C ATOM 2793 N MET A 345 -18.997 3.626 -0.957 1.00178.55 N ANISOU 2793 N MET A 345 22602 26732 18506 -4666 1106 3594 N ATOM 2794 CA MET A 345 -19.954 2.709 -0.349 1.00156.16 C ANISOU 2794 CA MET A 345 19740 23787 15808 -4383 981 3395 C ATOM 2795 C MET A 345 -19.779 1.282 -0.858 1.00147.40 C ANISOU 2795 C MET A 345 18468 22896 14641 -4259 1314 3026 C ATOM 2796 O MET A 345 -20.561 0.393 -0.521 1.00145.57 O ANISOU 2796 O MET A 345 18220 22554 14536 -4000 1241 2789 O ATOM 2797 CB MET A 345 -21.383 3.191 -0.607 1.00151.51 C ANISOU 2797 CB MET A 345 19496 23032 15040 -4336 607 3506 C ATOM 2798 CG MET A 345 -21.662 4.586 -0.069 1.00144.96 C ANISOU 2798 CG MET A 345 18831 21917 14330 -4402 263 3831 C ATOM 2799 SD MET A 345 -23.340 5.154 -0.401 1.00202.29 S ANISOU 2799 SD MET A 345 26443 28957 21460 -4300 -183 3940 S ATOM 2800 CE MET A 345 -23.292 6.791 0.325 1.00 94.52 C ANISOU 2800 CE MET A 345 12890 14917 8108 -4319 -486 4208 C ATOM 2801 N LEU A 346 -18.751 1.076 -1.677 1.00143.80 N ANISOU 2801 N LEU A 346 17895 22740 14003 -4456 1699 2969 N ATOM 2802 CA LEU A 346 -18.448 -0.240 -2.229 1.00127.33 C ANISOU 2802 CA LEU A 346 15647 20866 11868 -4360 2071 2601 C ATOM 2803 C LEU A 346 -18.175 -1.264 -1.131 1.00111.46 C ANISOU 2803 C LEU A 346 13295 18702 10354 -4034 2136 2359 C ATOM 2804 O LEU A 346 -17.655 -0.926 -0.068 1.00 92.85 O ANISOU 2804 O LEU A 346 10735 16186 8356 -3965 2026 2487 O ATOM 2805 CB LEU A 346 -17.247 -0.156 -3.173 1.00116.55 C ANISOU 2805 CB LEU A 346 14173 19833 10279 -4641 2509 2595 C ATOM 2806 CG LEU A 346 -17.335 0.874 -4.300 1.00111.24 C ANISOU 2806 CG LEU A 346 13854 19197 9215 -4881 2421 2786 C ATOM 2807 CD1 LEU A 346 -16.063 0.863 -5.134 1.00106.92 C ANISOU 2807 CD1 LEU A 346 13170 18862 8592 -5050 2852 2694 C ATOM 2808 CD2 LEU A 346 -18.555 0.619 -5.171 1.00102.54 C ANISOU 2808 CD2 LEU A 346 13119 18148 7695 -4880 2260 2709 C TER 2809 LEU A 346 MASTER 451 0 0 30 19 0 0 6 5617 2 0 56 END If you find results from this site helpful for your research, please cite one of our papers:
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