HEADER MEMBRANE PROTEIN 01-MAY-19 6OS1 TITLE STRUCTURE OF SYNTHETIC NANOBODY-STABILIZED ANGIOTENSIN II TYPE 1 TITLE 2 RECEPTOR BOUND TO TRV023 COMPND MOL_ID: 1; COMPND 2 MOLECULE: TYPE-1 ANGIOTENSIN II RECEPTOR,SOLUBLE CYTOCHROME B562 BRIL COMPND 3 FUSION PROTEIN; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: AT1AR,AT1BR,ANGIOTENSIN II TYPE-1 RECEPTOR,AT1,CYTOCHROME B- COMPND 6 562; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: NANOBODY NB.AT110I1_LE; COMPND 10 CHAIN: D; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: TRV023 PEPTIDE; COMPND 14 CHAIN: B; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: AGTR1, AGTR1A, AGTR1B, AT2R1, AT2R1B, CYBC; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDNA-ZEO-TETO; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 14 ORGANISM_TAXID: 32630; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 18 MOL_ID: 3; SOURCE 19 SYNTHETIC: YES; SOURCE 20 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 21 ORGANISM_TAXID: 32630 KEYWDS GPCR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR L.M.WINGLER,D.P.STAUS,M.A.SKIBA,C.MCMAHON,A.L.W.KLEINHENZ, AUTHOR 2 R.J.LEFKOWITZ,A.C.KRUSE REVDAT 2 04-MAR-20 6OS1 1 JRNL REVDAT 1 19-FEB-20 6OS1 0 JRNL AUTH L.M.WINGLER,M.A.SKIBA,C.MCMAHON,D.P.STAUS,A.L.W.KLEINHENZ, JRNL AUTH 2 C.M.SUOMIVUORI,N.R.LATORRACA,R.O.DROR,R.J.LEFKOWITZ, JRNL AUTH 3 A.C.KRUSE JRNL TITL ANGIOTENSIN AND BIASED ANALOGS INDUCE STRUCTURALLY DISTINCT JRNL TITL 2 ACTIVE CONFORMATIONS WITHIN A GPCR. JRNL REF SCIENCE V. 367 888 2020 JRNL REFN ESSN 1095-9203 JRNL PMID 32079768 JRNL DOI 10.1126/SCIENCE.AAY9813 REMARK 2 REMARK 2 RESOLUTION. 2.79 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.14_3260) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.40 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 3 NUMBER OF REFLECTIONS : 17764 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.241 REMARK 3 R VALUE (WORKING SET) : 0.239 REMARK 3 FREE R VALUE : 0.282 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 888 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 47.4094 - 5.0745 0.98 2936 156 0.2143 0.2579 REMARK 3 2 5.0745 - 4.0285 1.00 2858 150 0.1972 0.2223 REMARK 3 3 4.0285 - 3.5195 1.00 2822 149 0.2655 0.3147 REMARK 3 4 3.5195 - 3.1977 1.00 2798 147 0.2984 0.3994 REMARK 3 5 3.1977 - 2.9686 1.00 2800 147 0.3249 0.3735 REMARK 3 6 2.9686 - 2.7936 0.95 2662 139 0.3539 0.4040 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) : 0.480 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.690 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 85.74 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.55 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 225 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.9126 -13.4647 -57.0137 REMARK 3 T TENSOR REMARK 3 T11: 0.4776 T22: 0.5117 REMARK 3 T33: 0.4377 T12: -0.0090 REMARK 3 T13: -0.0138 T23: -0.0220 REMARK 3 L TENSOR REMARK 3 L11: 1.5778 L22: 1.2809 REMARK 3 L33: 2.1088 L12: -0.1309 REMARK 3 L13: -0.4309 L23: -0.7555 REMARK 3 S TENSOR REMARK 3 S11: 0.0076 S12: 0.1737 S13: 0.1566 REMARK 3 S21: -0.0682 S22: -0.1514 S23: -0.1924 REMARK 3 S31: -0.1547 S32: 0.0806 S33: 0.1529 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 266 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.0178 -47.8622 -16.9204 REMARK 3 T TENSOR REMARK 3 T11: 1.0985 T22: 1.1405 REMARK 3 T33: 0.9498 T12: 0.0079 REMARK 3 T13: 0.1233 T23: 0.1346 REMARK 3 L TENSOR REMARK 3 L11: 4.3521 L22: 9.8076 REMARK 3 L33: 7.1062 L12: -0.9664 REMARK 3 L13: 1.2020 L23: -4.6234 REMARK 3 S TENSOR REMARK 3 S11: -0.5003 S12: -0.1448 S13: -0.7505 REMARK 3 S21: -0.9366 S22: 0.4577 S23: -0.2350 REMARK 3 S31: 1.2556 S32: -0.4712 S33: 0.0123 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 267 THROUGH 1318 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.6911 -29.6058 -43.3914 REMARK 3 T TENSOR REMARK 3 T11: 0.6222 T22: 0.5369 REMARK 3 T33: 0.5517 T12: -0.0060 REMARK 3 T13: -0.0053 T23: 0.0112 REMARK 3 L TENSOR REMARK 3 L11: 1.9525 L22: 1.2424 REMARK 3 L33: 3.7121 L12: -0.1873 REMARK 3 L13: -0.2761 L23: -0.5638 REMARK 3 S TENSOR REMARK 3 S11: -0.1617 S12: -0.3018 S13: -0.1782 REMARK 3 S21: 0.1320 S22: -0.0553 S23: -0.1347 REMARK 3 S31: 0.5260 S32: 0.1711 S33: 0.3064 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.1454 -14.5006 -10.3740 REMARK 3 T TENSOR REMARK 3 T11: 0.9423 T22: 1.1991 REMARK 3 T33: 0.6260 T12: 0.0096 REMARK 3 T13: 0.1558 T23: 0.0060 REMARK 3 L TENSOR REMARK 3 L11: 4.5313 L22: 6.7257 REMARK 3 L33: 8.1230 L12: 5.2363 REMARK 3 L13: 5.6903 L23: 5.7904 REMARK 3 S TENSOR REMARK 3 S11: 0.4726 S12: -0.8324 S13: 0.0148 REMARK 3 S21: 0.6658 S22: -0.6492 S23: 0.3675 REMARK 3 S31: 1.3302 S32: -0.0253 S33: 0.4216 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 33 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.5126 -16.0348 -17.9898 REMARK 3 T TENSOR REMARK 3 T11: 0.8868 T22: 0.7113 REMARK 3 T33: 0.6067 T12: 0.0456 REMARK 3 T13: -0.0853 T23: -0.0885 REMARK 3 L TENSOR REMARK 3 L11: 3.9509 L22: 5.8410 REMARK 3 L33: 7.2088 L12: -0.6490 REMARK 3 L13: -1.5876 L23: -5.3036 REMARK 3 S TENSOR REMARK 3 S11: 0.0176 S12: -0.0901 S13: -0.3875 REMARK 3 S21: -0.6406 S22: -0.1577 S23: 0.1390 REMARK 3 S31: -0.1298 S32: -0.2357 S33: 0.0138 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 60 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.7737 -16.3493 -11.3948 REMARK 3 T TENSOR REMARK 3 T11: 0.7446 T22: 0.9190 REMARK 3 T33: 0.4839 T12: -0.0136 REMARK 3 T13: -0.0220 T23: -0.0036 REMARK 3 L TENSOR REMARK 3 L11: 4.1029 L22: 7.8770 REMARK 3 L33: 6.0764 L12: 3.1687 REMARK 3 L13: 2.6628 L23: 0.8485 REMARK 3 S TENSOR REMARK 3 S11: 0.3710 S12: 0.1587 S13: -0.3672 REMARK 3 S21: 0.5379 S22: -0.1126 S23: -0.2323 REMARK 3 S31: -0.0154 S32: 0.1693 S33: -0.1614 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 99 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.2127 -19.6490 -29.3444 REMARK 3 T TENSOR REMARK 3 T11: 0.4002 T22: 0.9587 REMARK 3 T33: 0.5547 T12: 0.0425 REMARK 3 T13: -0.1136 T23: 0.0217 REMARK 3 L TENSOR REMARK 3 L11: 5.7003 L22: 6.1850 REMARK 3 L33: 6.9757 L12: -3.9507 REMARK 3 L13: 4.0737 L23: -4.2168 REMARK 3 S TENSOR REMARK 3 S11: 0.1095 S12: 1.4167 S13: 0.1435 REMARK 3 S21: 0.1042 S22: -0.4415 S23: 0.0668 REMARK 3 S31: -0.4567 S32: -0.9878 S33: 0.2336 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 114 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.7202 -7.3726 -12.4364 REMARK 3 T TENSOR REMARK 3 T11: 0.9456 T22: 0.6384 REMARK 3 T33: 0.6763 T12: -0.0573 REMARK 3 T13: -0.2052 T23: 0.0216 REMARK 3 L TENSOR REMARK 3 L11: 4.7014 L22: 7.0889 REMARK 3 L33: 3.4648 L12: 5.7552 REMARK 3 L13: 3.8717 L23: 4.8537 REMARK 3 S TENSOR REMARK 3 S11: -0.6325 S12: 0.0598 S13: 0.6214 REMARK 3 S21: -0.0276 S22: -0.1264 S23: 0.4778 REMARK 3 S31: -0.9627 S32: -0.0519 S33: 1.0703 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 8 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.8409 -16.7070 -72.5748 REMARK 3 T TENSOR REMARK 3 T11: 0.7828 T22: 0.8411 REMARK 3 T33: 0.3804 T12: 0.1457 REMARK 3 T13: -0.0472 T23: 0.1540 REMARK 3 L TENSOR REMARK 3 L11: 6.8309 L22: 7.6897 REMARK 3 L33: 1.9998 L12: 1.2839 REMARK 3 L13: 1.0868 L23: -6.0400 REMARK 3 S TENSOR REMARK 3 S11: -0.7180 S12: -1.4146 S13: -0.7297 REMARK 3 S21: 1.4270 S22: 1.1584 S23: 1.0731 REMARK 3 S31: -1.1315 S32: -0.9407 S33: -0.4899 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 6OS1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-19. REMARK 100 THE DEPOSITION ID IS D_1000241240. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-NOV-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17795 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.790 REMARK 200 RESOLUTION RANGE LOW (A) : 47.403 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : 10.54 REMARK 200 R MERGE (I) : 0.20600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5 REMARK 200 DATA REDUNDANCY IN SHELL : 8.61 REMARK 200 R MERGE FOR SHELL (I) : 1.88200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.850 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: 6OS2 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN COMPLEX WAS RECONSTITUTED WITH REMARK 280 A 10:1 (W/W) MIXTURE OF MONOOLEIN AND CHOLESTEROL. CRYSTALS WERE REMARK 280 GROWN IN 100 MM TRIS PH 8, 50-70 MM MGCL2, 30% PEG 300, 2-4% 1,3- REMARK 280 BUTANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.33500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.99500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 113.79500 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.33500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.99500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 113.79500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.33500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.99500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 113.79500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.33500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.99500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 113.79500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5000 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, 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 ASP A -6 REMARK 465 TYR A -5 REMARK 465 LYS A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 ASP A 0 REMARK 465 LYS A 1 REMARK 465 ILE A 2 REMARK 465 LEU A 3 REMARK 465 ASN A 4 REMARK 465 SER A 5 REMARK 465 SER A 6 REMARK 465 THR A 7 REMARK 465 GLU A 8 REMARK 465 ASP A 9 REMARK 465 GLY A 10 REMARK 465 THR A 269 REMARK 465 PRO A 270 REMARK 465 PRO A 271 REMARK 465 LYS A 272 REMARK 465 LEU A 273 REMARK 465 GLU A 274 REMARK 465 ASP A 275 REMARK 465 LYS A 276 REMARK 465 SER A 277 REMARK 465 PRO A 278 REMARK 465 ASP A 279 REMARK 465 SER A 280 REMARK 465 PRO A 281 REMARK 465 GLU A 282 REMARK 465 MET A 283 REMARK 465 LYS A 284 REMARK 465 ASP A 285 REMARK 465 PHE A 286 REMARK 465 THR A 1222 REMARK 465 THR A 1223 REMARK 465 ARG A 1224 REMARK 465 ASN A 1225 REMARK 465 ALA A 1226 REMARK 465 GLU A 1227 REMARK 465 ILE A 1228 REMARK 465 GLN A 1229 REMARK 465 TYR A 1319 REMARK 465 GLU D 128 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 12 CG CD CE NZ REMARK 470 ARG A 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 20 CG CD CE NZ REMARK 470 LYS A 58 CG CD CE NZ REMARK 470 ARG A 139 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 173 CG CD OE1 OE2 REMARK 470 ASN A 176 CG OD1 ND2 REMARK 470 GLU A 185 CG CD OE1 OE2 REMARK 470 LEU A 191 CG CD1 CD2 REMARK 470 ILE A 193 CG1 CG2 CD1 REMARK 470 ILE A 201 CD1 REMARK 470 LYS A 220 CG CD CE NZ REMARK 470 LYS A 224 CG CD CE NZ REMARK 470 GLU A 233 CG CD OE1 OE2 REMARK 470 LEU A 239 CG CD1 CD2 REMARK 470 LYS A 240 CG CD CE NZ REMARK 470 GLU A 243 CG CD OE1 OE2 REMARK 470 LYS A 252 CG CD CE NZ REMARK 470 ASP A 253 CG OD1 OD2 REMARK 470 LEU A 255 CG CD1 CD2 REMARK 470 ARG A 259 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 266 CG CD OE1 NE2 REMARK 470 LYS A 267 CG CD CE NZ REMARK 470 ARG A 287 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 291 CG OD1 OD2 REMARK 470 ILE A 292 CG1 CG2 CD1 REMARK 470 VAL A 294 CG1 CG2 REMARK 470 ASP A 298 CG OD1 OD2 REMARK 470 ASP A 299 CG OD1 OD2 REMARK 470 LYS A 302 CG CD CE NZ REMARK 470 LEU A 303 CG CD1 CD2 REMARK 470 ASN A 305 CG OD1 ND2 REMARK 470 GLU A 306 CG CD OE1 OE2 REMARK 470 LYS A 308 CG CD CE NZ REMARK 470 VAL A 309 CG1 CG2 REMARK 470 LYS A 310 CG CD CE NZ REMARK 470 GLU A 311 CG CD OE1 OE2 REMARK 470 GLN A 313 CG CD OE1 NE2 REMARK 470 GLU A 317 CG CD OE1 OE2 REMARK 470 GLN A 318 CG CD OE1 NE2 REMARK 470 LYS A 320 CG CD CE NZ REMARK 470 LYS A1230 CG CD CE NZ REMARK 470 LYS A1232 CG CD CE NZ REMARK 470 ARG A1272 CG CD NE CZ NH1 NH2 REMARK 470 ARG A1275 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1307 CG CD CE NZ REMARK 470 LYS A1308 CG CD CE NZ REMARK 470 ARG A1311 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1318 CG CD CE NZ REMARK 470 GLN D 5 CG CD OE1 NE2 REMARK 470 GLU D 44 CG CD OE1 OE2 REMARK 470 ASN D 58 CG OD1 ND2 REMARK 470 LYS D 64 CG CD CE NZ REMARK 470 LYS D 75 CG CD CE NZ REMARK 470 GLN D 118 CG CD OE1 NE2 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 59 87.73 55.95 REMARK 500 TYR A 92 70.32 57.19 REMARK 500 PHE A 204 -58.08 -151.27 REMARK 500 LYS A 267 58.21 -92.37 REMARK 500 LEU A 319 -71.59 -71.32 REMARK 500 PRO B 7 89.61 -68.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1401 REMARK 610 OLC A 1402 REMARK 610 OLC A 1403 REMARK 610 OLC A 1404 REMARK 610 OLC A 1405 REMARK 610 OLC A 1406 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1407 DBREF 6OS1 A 2 226 UNP P30556 AGTR1_HUMAN 2 226 DBREF 6OS1 A 227 1226 UNP P0ABE7 C562_ECOLX 24 122 DBREF 6OS1 A 1227 1319 UNP P30556 AGTR1_HUMAN 227 319 DBREF 6OS1 D 1 128 PDB 6OS1 6OS1 1 128 DBREF 6OS1 B 1 8 PDB 6OS1 6OS1 1 8 SEQADV 6OS1 ASP A -6 UNP P30556 EXPRESSION TAG SEQADV 6OS1 TYR A -5 UNP P30556 EXPRESSION TAG SEQADV 6OS1 LYS A -4 UNP P30556 EXPRESSION TAG SEQADV 6OS1 ASP A -3 UNP P30556 EXPRESSION TAG SEQADV 6OS1 ASP A -2 UNP P30556 EXPRESSION TAG SEQADV 6OS1 ASP A -1 UNP P30556 EXPRESSION TAG SEQADV 6OS1 ASP A 0 UNP P30556 EXPRESSION TAG SEQADV 6OS1 LYS A 1 UNP P30556 EXPRESSION TAG SEQADV 6OS1 TRP A 232 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQRES 1 A 425 ASP TYR LYS ASP ASP ASP ASP LYS ILE LEU ASN SER SER SEQRES 2 A 425 THR GLU ASP GLY ILE LYS ARG ILE GLN ASP ASP CYS PRO SEQRES 3 A 425 LYS ALA GLY ARG HIS ASN TYR ILE PHE VAL MET ILE PRO SEQRES 4 A 425 THR LEU TYR SER ILE ILE PHE VAL VAL GLY ILE PHE GLY SEQRES 5 A 425 ASN SER LEU VAL VAL ILE VAL ILE TYR PHE TYR MET LYS SEQRES 6 A 425 LEU LYS THR VAL ALA SER VAL PHE LEU LEU ASN LEU ALA SEQRES 7 A 425 LEU ALA ASP LEU CYS PHE LEU LEU THR LEU PRO LEU TRP SEQRES 8 A 425 ALA VAL TYR THR ALA MET GLU TYR ARG TRP PRO PHE GLY SEQRES 9 A 425 ASN TYR LEU CYS LYS ILE ALA SER ALA SER VAL SER PHE SEQRES 10 A 425 ASN LEU TYR ALA SER VAL PHE LEU LEU THR CYS LEU SER SEQRES 11 A 425 ILE ASP ARG TYR LEU ALA ILE VAL HIS PRO MET LYS SER SEQRES 12 A 425 ARG LEU ARG ARG THR MET LEU VAL ALA LYS VAL THR CYS SEQRES 13 A 425 ILE ILE ILE TRP LEU LEU ALA GLY LEU ALA SER LEU PRO SEQRES 14 A 425 ALA ILE ILE HIS ARG ASN VAL PHE PHE ILE GLU ASN THR SEQRES 15 A 425 ASN ILE THR VAL CYS ALA PHE HIS TYR GLU SER GLN ASN SEQRES 16 A 425 SER THR LEU PRO ILE GLY LEU GLY LEU THR LYS ASN ILE SEQRES 17 A 425 LEU GLY PHE LEU PHE PRO PHE LEU ILE ILE LEU THR SER SEQRES 18 A 425 TYR THR LEU ILE TRP LYS ALA LEU LYS LYS ALA TYR ASP SEQRES 19 A 425 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 20 A 425 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 21 A 425 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 22 A 425 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 23 A 425 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 24 A 425 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 25 A 425 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 26 A 425 LEU LYS THR THR ARG ASN ALA GLU ILE GLN LYS ASN LYS SEQRES 27 A 425 PRO ARG ASN ASP ASP ILE PHE LYS ILE ILE MET ALA ILE SEQRES 28 A 425 VAL LEU PHE PHE PHE PHE SER TRP ILE PRO HIS GLN ILE SEQRES 29 A 425 PHE THR PHE LEU ASP VAL LEU ILE GLN LEU GLY ILE ILE SEQRES 30 A 425 ARG ASP CYS ARG ILE ALA ASP ILE VAL ASP THR ALA MET SEQRES 31 A 425 PRO ILE THR ILE CYS ILE ALA TYR PHE ASN ASN CYS LEU SEQRES 32 A 425 ASN PRO LEU PHE TYR GLY PHE LEU GLY LYS LYS PHE LYS SEQRES 33 A 425 ARG TYR PHE LEU GLN LEU LEU LYS TYR SEQRES 1 D 128 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL ALA SEQRES 2 D 128 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 128 ASN ILE PHE ASP VAL ASP ILE MET GLY TRP TYR ARG GLN SEQRES 4 D 128 ALA PRO GLY LYS GLU ARG GLU LEU VAL ALA SER ILE THR SEQRES 5 D 128 ASP GLY GLY SER THR ASN TYR ALA ASP SER VAL LYS GLY SEQRES 6 D 128 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 D 128 TYR LEU ALA MET ALA SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 D 128 VAL TYR TYR CYS ALA ALA VAL ALA TYR PRO ASP ILE PRO SEQRES 9 D 128 THR TYR PHE ASP TYR ASP SER ASP ASN PHE TYR TRP GLY SEQRES 10 D 128 GLN GLY THR GLN VAL THR VAL SER SER LEU GLU SEQRES 1 B 8 SAR ARG VAL TYR LYS HIS PRO ALA HET SAR B 1 5 HET OLC A1401 10 HET OLC A1402 15 HET OLC A1403 10 HET OLC A1404 8 HET OLC A1405 13 HET OLC A1406 10 HET CLR A1407 28 HETNAM SAR SARCOSINE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM CLR CHOLESTEROL HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 3 SAR C3 H7 N O2 FORMUL 4 OLC 6(C21 H40 O4) FORMUL 10 CLR C27 H46 O FORMUL 11 HOH *17(H2 O) HELIX 1 AA1 HIS A 24 MET A 57 1 34 HELIX 2 AA2 THR A 61 THR A 80 1 20 HELIX 3 AA3 THR A 80 MET A 90 1 11 HELIX 4 AA4 PHE A 96 HIS A 132 1 37 HELIX 5 AA5 THR A 141 SER A 160 1 20 HELIX 6 AA6 LEU A 161 HIS A 166 1 6 HELIX 7 AA7 GLY A 194 LEU A 202 1 9 HELIX 8 AA8 PHE A 204 LYS A 244 1 41 HELIX 9 AA9 ASN A 247 LYS A 267 1 21 HELIX 10 AB1 GLY A 289 ASN A 305 1 17 HELIX 11 AB2 VAL A 309 LYS A 320 1 12 HELIX 12 AB3 ASP A 1237 LEU A 1268 1 32 HELIX 13 AB4 ASP A 1273 LEU A 1297 1 25 HELIX 14 AB5 LEU A 1297 GLY A 1306 1 10 HELIX 15 AB6 GLY A 1306 LYS A 1318 1 13 HELIX 16 AB7 LYS D 86 THR D 90 5 5 SHEET 1 AA1 4 LYS A 12 ILE A 14 0 SHEET 2 AA1 4 ASN A 168 ILE A 172 1 O PHE A 171 N LYS A 12 SHEET 3 AA1 4 ILE A 177 TYR A 184 -1 O VAL A 179 N PHE A 170 SHEET 4 AA1 4 ARG B 2 TYR B 4 -1 O TYR B 4 N PHE A 182 SHEET 1 AA2 4 GLN D 3 SER D 7 0 SHEET 2 AA2 4 SER D 17 SER D 25 -1 O SER D 21 N SER D 7 SHEET 3 AA2 4 THR D 77 ALA D 83 -1 O LEU D 80 N LEU D 20 SHEET 4 AA2 4 THR D 68 ASP D 72 -1 N THR D 68 O ALA D 81 SHEET 1 AA3 6 GLY D 10 ALA D 13 0 SHEET 2 AA3 6 THR D 120 SER D 125 1 O THR D 123 N VAL D 12 SHEET 3 AA3 6 ALA D 91 VAL D 98 -1 N TYR D 93 O THR D 120 SHEET 4 AA3 6 ILE D 33 GLN D 39 -1 N TYR D 37 O TYR D 94 SHEET 5 AA3 6 ARG D 45 THR D 52 -1 O ALA D 49 N TRP D 36 SHEET 6 AA3 6 THR D 57 TYR D 59 -1 O ASN D 58 N SER D 50 SHEET 1 AA4 4 GLY D 10 ALA D 13 0 SHEET 2 AA4 4 THR D 120 SER D 125 1 O THR D 123 N VAL D 12 SHEET 3 AA4 4 ALA D 91 VAL D 98 -1 N TYR D 93 O THR D 120 SHEET 4 AA4 4 PHE D 114 TRP D 116 -1 O TYR D 115 N ALA D 97 SSBOND 1 CYS A 18 CYS A 1274 1555 1555 2.03 SSBOND 2 CYS A 101 CYS A 180 1555 1555 2.03 SSBOND 3 CYS D 22 CYS D 95 1555 1555 2.03 LINK C SAR B 1 N ARG B 2 1555 1555 1.33 SITE 1 AC1 2 CYS A 121 OLC A1406 SITE 1 AC2 5 MET A1243 ALA A1244 LEU A1247 ASN A1294 SITE 2 AC2 5 OLC A1405 SITE 1 AC3 3 LEU A1268 PHE A1304 LYS A1310 SITE 1 AC4 1 TRP A 219 SITE 1 AC5 2 GLY A 194 OLC A1402 SITE 1 AC6 3 THR A 120 ILE A 151 OLC A1401 SITE 1 AC7 2 ILE A 51 LEU A1316 CRYST1 60.670 101.990 227.590 90.00 90.00 90.00 I 2 2 2 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 0.016483 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009805 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004394 0.00000 ATOM 1 N ILE A 11 -12.235 -0.342 -82.681 1.00115.12 N ANISOU 1 N ILE A 11 14749 16307 12684 1003 992 2634 N ATOM 2 CA ILE A 11 -11.735 -1.460 -81.892 1.00114.32 C ANISOU 2 CA ILE A 11 14616 16180 12642 921 979 2427 C ATOM 3 C ILE A 11 -10.982 -2.440 -82.784 1.00117.57 C ANISOU 3 C ILE A 11 15011 16777 12884 956 1081 2405 C ATOM 4 O ILE A 11 -10.666 -2.130 -83.933 1.00126.23 O ANISOU 4 O ILE A 11 16113 18003 13843 1026 1173 2568 O ATOM 5 CB ILE A 11 -12.880 -2.165 -81.143 1.00103.87 C ANISOU 5 CB ILE A 11 13316 14852 11297 921 843 2196 C ATOM 6 CG1 ILE A 11 -13.961 -2.621 -82.125 1.00107.87 C ANISOU 6 CG1 ILE A 11 13859 15578 11548 1026 792 2151 C ATOM 7 CG2 ILE A 11 -13.468 -1.246 -80.083 1.00 90.94 C ANISOU 7 CG2 ILE A 11 11693 13010 9851 885 762 2205 C ATOM 8 CD1 ILE A 11 -15.146 -3.287 -81.462 1.00107.07 C ANISOU 8 CD1 ILE A 11 13769 15490 11423 1019 657 1941 C ATOM 9 N LYS A 12 -10.696 -3.623 -82.250 1.00104.25 N ANISOU 9 N LYS A 12 13309 15098 11202 916 1072 2208 N ATOM 10 CA LYS A 12 -9.941 -4.643 -82.962 1.00 90.35 C ANISOU 10 CA LYS A 12 11543 13486 9298 956 1179 2163 C ATOM 11 C LYS A 12 -10.885 -5.640 -83.621 1.00 95.14 C ANISOU 11 C LYS A 12 12228 14267 9656 1029 1127 1991 C ATOM 12 O LYS A 12 -11.918 -6.006 -83.052 1.00 98.23 O ANISOU 12 O LYS A 12 12647 14630 10044 1008 998 1828 O ATOM 13 CB LYS A 12 -8.990 -5.376 -82.013 1.00 71.10 C ANISOU 13 CB LYS A 12 9047 10950 7017 878 1214 2062 C ATOM 14 N ARG A 13 -10.523 -6.074 -84.826 1.00 92.16 N ANISOU 14 N ARG A 13 11884 14071 9063 1110 1228 2028 N ATOM 15 CA ARG A 13 -11.282 -7.065 -85.579 1.00 88.14 C ANISOU 15 CA ARG A 13 11460 13738 8290 1169 1190 1861 C ATOM 16 C ARG A 13 -10.511 -8.378 -85.566 1.00 84.36 C ANISOU 16 C ARG A 13 11006 13282 7765 1173 1283 1704 C ATOM 17 O ARG A 13 -9.366 -8.433 -86.027 1.00 85.82 O ANISOU 17 O ARG A 13 11165 13504 7939 1213 1438 1811 O ATOM 18 CB ARG A 13 -11.528 -6.594 -87.012 1.00 95.72 C ANISOU 18 CB ARG A 13 12464 14900 9006 1268 1234 2009 C ATOM 19 N ILE A 14 -11.137 -9.431 -85.039 1.00 82.25 N ANISOU 19 N ILE A 14 10788 12989 7475 1136 1197 1461 N ATOM 20 CA ILE A 14 -10.490 -10.724 -84.868 1.00 83.21 C ANISOU 20 CA ILE A 14 10944 13094 7578 1140 1278 1297 C ATOM 21 C ILE A 14 -11.329 -11.798 -85.549 1.00 80.23 C ANISOU 21 C ILE A 14 10692 12846 6947 1166 1232 1086 C ATOM 22 O ILE A 14 -12.452 -11.560 -85.994 1.00 71.45 O ANISOU 22 O ILE A 14 9618 11835 5694 1162 1114 1058 O ATOM 23 CB ILE A 14 -10.271 -11.077 -83.382 1.00 84.43 C ANISOU 23 CB ILE A 14 11040 13052 7986 1053 1231 1198 C ATOM 24 CG1 ILE A 14 -11.615 -11.252 -82.672 1.00 91.05 C ANISOU 24 CG1 ILE A 14 11906 13838 8851 987 1053 1040 C ATOM 25 CG2 ILE A 14 -9.435 -10.008 -82.697 1.00 70.65 C ANISOU 25 CG2 ILE A 14 9177 11183 6484 1008 1264 1396 C ATOM 26 CD1 ILE A 14 -11.495 -11.778 -81.259 1.00 91.91 C ANISOU 26 CD1 ILE A 14 11977 13775 9171 909 1007 918 C ATOM 27 N GLN A 15 -10.758 -12.999 -85.619 1.00 89.33 N ANISOU 27 N GLN A 15 11906 13991 8042 1190 1326 938 N ATOM 28 CA GLN A 15 -11.412 -14.168 -86.190 1.00100.67 C ANISOU 28 CA GLN A 15 13482 15517 9252 1198 1297 710 C ATOM 29 C GLN A 15 -11.566 -15.227 -85.110 1.00 98.17 C ANISOU 29 C GLN A 15 13187 15043 9069 1128 1252 500 C ATOM 30 O GLN A 15 -10.619 -15.500 -84.364 1.00102.90 O ANISOU 30 O GLN A 15 13732 15514 9851 1133 1342 520 O ATOM 31 CB GLN A 15 -10.610 -14.727 -87.370 1.00107.26 C ANISOU 31 CB GLN A 15 14408 16478 9867 1307 1472 710 C ATOM 32 CG GLN A 15 -10.584 -13.831 -88.597 1.00113.23 C ANISOU 32 CG GLN A 15 15167 17422 10433 1382 1516 899 C ATOM 33 CD GLN A 15 -11.736 -14.105 -89.545 1.00123.01 C ANISOU 33 CD GLN A 15 16524 18839 11375 1381 1408 780 C ATOM 34 OE1 GLN A 15 -12.213 -15.235 -89.649 1.00135.76 O ANISOU 34 OE1 GLN A 15 18257 20464 12859 1350 1368 537 O ATOM 35 NE2 GLN A 15 -12.190 -13.070 -90.242 1.00116.12 N ANISOU 35 NE2 GLN A 15 15619 18107 10393 1412 1357 955 N ATOM 36 N ASP A 16 -12.754 -15.819 -85.025 1.00 84.55 N ANISOU 36 N ASP A 16 11535 13337 7252 1060 1113 310 N ATOM 37 CA ASP A 16 -13.029 -16.865 -84.050 1.00 87.21 C ANISOU 37 CA ASP A 16 11905 13530 7701 986 1066 108 C ATOM 38 C ASP A 16 -12.814 -18.229 -84.693 1.00 90.01 C ANISOU 38 C ASP A 16 12417 13909 7872 1019 1157 -88 C ATOM 39 O ASP A 16 -13.368 -18.512 -85.761 1.00 99.02 O ANISOU 39 O ASP A 16 13669 15200 8756 1028 1133 -172 O ATOM 40 CB ASP A 16 -14.458 -16.744 -83.517 1.00 94.11 C ANISOU 40 CB ASP A 16 12758 14400 8597 883 866 18 C ATOM 41 CG ASP A 16 -14.712 -17.632 -82.313 1.00105.79 C ANISOU 41 CG ASP A 16 14242 15715 10240 799 816 -148 C ATOM 42 OD1 ASP A 16 -13.760 -18.287 -81.837 1.00106.65 O ANISOU 42 OD1 ASP A 16 14364 15702 10456 826 932 -182 O ATOM 43 OD2 ASP A 16 -15.867 -17.672 -81.840 1.00108.68 O ANISOU 43 OD2 ASP A 16 14591 16077 10626 712 665 -233 O ATOM 44 N ASP A 17 -12.005 -19.069 -84.043 1.00 87.62 N ANISOU 44 N ASP A 17 12130 13460 7700 1038 1263 -158 N ATOM 45 CA ASP A 17 -11.723 -20.395 -84.583 1.00 82.97 C ANISOU 45 CA ASP A 17 11706 12859 6959 1083 1372 -344 C ATOM 46 C ASP A 17 -12.984 -21.251 -84.619 1.00 87.31 C ANISOU 46 C ASP A 17 12379 13405 7388 974 1234 -586 C ATOM 47 O ASP A 17 -13.339 -21.811 -85.663 1.00 96.77 O ANISOU 47 O ASP A 17 13728 14711 8330 982 1244 -718 O ATOM 48 CB ASP A 17 -10.631 -21.078 -83.758 1.00 89.42 C ANISOU 48 CB ASP A 17 12497 13509 7968 1135 1509 -348 C ATOM 49 CG ASP A 17 -9.311 -20.333 -83.808 1.00 98.00 C ANISOU 49 CG ASP A 17 13457 14619 9158 1236 1655 -110 C ATOM 50 OD1 ASP A 17 -9.084 -19.588 -84.784 1.00 98.39 O ANISOU 50 OD1 ASP A 17 13494 14819 9072 1296 1705 26 O ATOM 51 OD2 ASP A 17 -8.499 -20.497 -82.873 1.00 97.36 O ANISOU 51 OD2 ASP A 17 13284 14416 9293 1253 1718 -50 O ATOM 52 N CYS A 18 -13.674 -21.365 -83.484 1.00 84.47 N ANISOU 52 N CYS A 18 11959 12930 7208 865 1103 -648 N ATOM 53 CA CYS A 18 -14.926 -22.110 -83.383 1.00 90.14 C ANISOU 53 CA CYS A 18 12762 13641 7845 740 959 -858 C ATOM 54 C CYS A 18 -16.054 -21.117 -83.132 1.00 82.23 C ANISOU 54 C CYS A 18 11640 12731 6872 658 769 -778 C ATOM 55 O CYS A 18 -16.387 -20.828 -81.974 1.00 88.82 O ANISOU 55 O CYS A 18 12366 13462 7921 599 687 -745 O ATOM 56 CB CYS A 18 -14.858 -23.152 -82.263 1.00101.59 C ANISOU 56 CB CYS A 18 14243 14882 9474 685 973 -995 C ATOM 57 SG CYS A 18 -13.298 -24.068 -82.153 1.00110.76 S ANISOU 57 SG CYS A 18 15481 15898 10706 819 1217 -1008 S ATOM 58 N PRO A 19 -16.672 -20.563 -84.179 1.00 79.48 N ANISOU 58 N PRO A 19 11306 12582 6311 662 696 -739 N ATOM 59 CA PRO A 19 -17.696 -19.532 -83.950 1.00 85.95 C ANISOU 59 CA PRO A 19 11997 13493 7166 612 530 -631 C ATOM 60 C PRO A 19 -19.000 -20.082 -83.399 1.00 89.15 C ANISOU 60 C PRO A 19 12398 13888 7588 472 362 -790 C ATOM 61 O PRO A 19 -19.737 -19.340 -82.739 1.00 85.89 O ANISOU 61 O PRO A 19 11856 13482 7296 435 244 -703 O ATOM 62 CB PRO A 19 -17.887 -18.916 -85.342 1.00 65.40 C ANISOU 62 CB PRO A 19 9424 11120 4304 672 519 -541 C ATOM 63 CG PRO A 19 -17.533 -20.017 -86.281 1.00 77.26 C ANISOU 63 CG PRO A 19 11108 12669 5578 688 611 -713 C ATOM 64 CD PRO A 19 -16.431 -20.798 -85.613 1.00 85.13 C ANISOU 64 CD PRO A 19 12151 13456 6738 727 771 -774 C ATOM 65 N LYS A 20 -19.311 -21.351 -83.645 1.00 81.72 N ANISOU 65 N LYS A 20 11595 12926 6529 393 353 -1015 N ATOM 66 CA LYS A 20 -20.555 -21.948 -83.178 1.00 91.46 C ANISOU 66 CA LYS A 20 12824 14155 7771 242 195 -1168 C ATOM 67 C LYS A 20 -20.441 -22.555 -81.784 1.00100.70 C ANISOU 67 C LYS A 20 13967 15099 9196 186 213 -1236 C ATOM 68 O LYS A 20 -21.407 -23.161 -81.307 1.00108.50 O ANISOU 68 O LYS A 20 14954 16061 10209 55 100 -1365 O ATOM 69 CB LYS A 20 -21.028 -23.020 -84.166 1.00 89.61 C ANISOU 69 CB LYS A 20 12763 14010 7275 159 163 -1387 C ATOM 70 N ALA A 21 -19.298 -22.403 -81.121 1.00 81.77 N ANISOU 70 N ALA A 21 11539 12548 6983 277 348 -1143 N ATOM 71 CA ALA A 21 -19.088 -23.005 -79.810 1.00 79.96 C ANISOU 71 CA ALA A 21 11287 12111 6982 236 375 -1197 C ATOM 72 C ALA A 21 -19.801 -22.186 -78.741 1.00 84.12 C ANISOU 72 C ALA A 21 11650 12623 7689 189 253 -1097 C ATOM 73 O ALA A 21 -19.543 -20.986 -78.593 1.00 90.78 O ANISOU 73 O ALA A 21 12381 13503 8608 259 250 -913 O ATOM 74 CB ALA A 21 -17.595 -23.106 -79.505 1.00 82.33 C ANISOU 74 CB ALA A 21 11599 12280 7404 354 556 -1120 C ATOM 75 N GLY A 22 -20.698 -22.833 -77.999 1.00 80.13 N ANISOU 75 N GLY A 22 11137 12057 7252 70 159 -1216 N ATOM 76 CA GLY A 22 -21.377 -22.202 -76.888 1.00 70.65 C ANISOU 76 CA GLY A 22 9793 10829 6224 30 60 -1139 C ATOM 77 C GLY A 22 -22.554 -21.325 -77.250 1.00 72.98 C ANISOU 77 C GLY A 22 9989 11307 6435 1 -86 -1070 C ATOM 78 O GLY A 22 -23.142 -20.710 -76.351 1.00 81.82 O ANISOU 78 O GLY A 22 10987 12409 7693 -13 -159 -995 O ATOM 79 N ARG A 23 -22.924 -21.244 -78.526 1.00 83.07 N ANISOU 79 N ARG A 23 11313 12765 7484 1 -129 -1088 N ATOM 80 CA ARG A 23 -24.022 -20.386 -78.971 1.00 87.58 C ANISOU 80 CA ARG A 23 11782 13536 7959 -10 -267 -1001 C ATOM 81 C ARG A 23 -25.269 -21.253 -79.107 1.00 80.18 C ANISOU 81 C ARG A 23 10856 12689 6918 -164 -401 -1163 C ATOM 82 O ARG A 23 -25.582 -21.765 -80.183 1.00 82.52 O ANISOU 82 O ARG A 23 11241 13120 6991 -218 -444 -1266 O ATOM 83 CB ARG A 23 -23.669 -19.685 -80.276 1.00 97.32 C ANISOU 83 CB ARG A 23 13043 14932 9000 87 -240 -896 C ATOM 84 CG ARG A 23 -22.266 -19.104 -80.298 1.00110.26 C ANISOU 84 CG ARG A 23 14700 16474 10721 217 -83 -763 C ATOM 85 CD ARG A 23 -22.154 -17.938 -81.264 1.00112.95 C ANISOU 85 CD ARG A 23 15002 16975 10940 321 -80 -579 C ATOM 86 NE ARG A 23 -22.655 -16.696 -80.683 1.00115.32 N ANISOU 86 NE ARG A 23 15160 17283 11374 362 -148 -406 N ATOM 87 CZ ARG A 23 -23.878 -16.215 -80.879 1.00119.16 C ANISOU 87 CZ ARG A 23 15564 17923 11789 343 -285 -361 C ATOM 88 NH1 ARG A 23 -24.737 -16.869 -81.649 1.00118.74 N ANISOU 88 NH1 ARG A 23 15544 18043 11527 267 -386 -478 N ATOM 89 NH2 ARG A 23 -24.241 -15.076 -80.308 1.00121.67 N ANISOU 89 NH2 ARG A 23 15766 18220 12242 401 -322 -200 N ATOM 90 N HIS A 24 -25.988 -21.415 -77.999 1.00 78.04 N ANISOU 90 N HIS A 24 10496 12349 6808 -241 -469 -1186 N ATOM 91 CA HIS A 24 -27.195 -22.226 -77.953 1.00 72.82 C ANISOU 91 CA HIS A 24 9820 11762 6086 -403 -596 -1325 C ATOM 92 C HIS A 24 -28.345 -21.393 -77.409 1.00 77.76 C ANISOU 92 C HIS A 24 10256 12504 6784 -411 -720 -1206 C ATOM 93 O HIS A 24 -28.159 -20.587 -76.493 1.00 75.07 O ANISOU 93 O HIS A 24 9823 12076 6624 -322 -685 -1076 O ATOM 94 CB HIS A 24 -26.989 -23.473 -77.088 1.00 62.09 C ANISOU 94 CB HIS A 24 8544 10194 4855 -503 -542 -1483 C ATOM 95 CG HIS A 24 -25.925 -24.394 -77.599 1.00 82.11 C ANISOU 95 CG HIS A 24 11271 12605 7322 -489 -412 -1607 C ATOM 96 ND1 HIS A 24 -26.198 -25.661 -78.067 1.00 92.24 N ANISOU 96 ND1 HIS A 24 12699 13862 8487 -621 -426 -1812 N ATOM 97 CD2 HIS A 24 -24.587 -24.228 -77.722 1.00 87.50 C ANISOU 97 CD2 HIS A 24 12026 13183 8038 -354 -260 -1551 C ATOM 98 CE1 HIS A 24 -25.074 -26.238 -78.452 1.00 91.01 C ANISOU 98 CE1 HIS A 24 12706 13582 8294 -552 -279 -1881 C ATOM 99 NE2 HIS A 24 -24.081 -25.389 -78.253 1.00 89.62 N ANISOU 99 NE2 HIS A 24 12478 13367 8208 -388 -176 -1719 N ATOM 100 N ASN A 25 -29.536 -21.599 -77.976 1.00 90.63 N ANISOU 100 N ASN A 25 11831 14337 8268 -517 -865 -1253 N ATOM 101 CA ASN A 25 -30.686 -20.789 -77.590 1.00 97.96 C ANISOU 101 CA ASN A 25 12566 15411 9243 -508 -982 -1125 C ATOM 102 C ASN A 25 -31.134 -21.073 -76.162 1.00 95.92 C ANISOU 102 C ASN A 25 12223 15018 9203 -566 -985 -1144 C ATOM 103 O ASN A 25 -31.597 -20.158 -75.471 1.00106.06 O ANISOU 103 O ASN A 25 13365 16326 10606 -486 -1006 -1001 O ATOM 104 CB ASN A 25 -31.840 -21.017 -78.567 1.00 95.06 C ANISOU 104 CB ASN A 25 12146 15315 8658 -618 -1144 -1168 C ATOM 105 CG ASN A 25 -31.570 -20.421 -79.933 1.00 90.74 C ANISOU 105 CG ASN A 25 11641 14948 7886 -529 -1157 -1095 C ATOM 106 OD1 ASN A 25 -31.631 -21.113 -80.950 1.00110.90 O ANISOU 106 OD1 ASN A 25 14301 17612 10224 -621 -1203 -1223 O ATOM 107 ND2 ASN A 25 -31.267 -19.128 -79.964 1.00 78.72 N ANISOU 107 ND2 ASN A 25 10046 13453 6410 -351 -1114 -888 N ATOM 108 N TYR A 26 -31.010 -22.320 -75.699 1.00 94.80 N ANISOU 108 N TYR A 26 12173 14732 9116 -698 -956 -1313 N ATOM 109 CA TYR A 26 -31.393 -22.621 -74.324 1.00105.60 C ANISOU 109 CA TYR A 26 13465 15971 10687 -750 -948 -1322 C ATOM 110 C TYR A 26 -30.451 -21.979 -73.316 1.00100.15 C ANISOU 110 C TYR A 26 12774 15089 10191 -607 -826 -1219 C ATOM 111 O TYR A 26 -30.838 -21.787 -72.158 1.00104.03 O ANISOU 111 O TYR A 26 13169 15514 10842 -603 -826 -1171 O ATOM 112 CB TYR A 26 -31.463 -24.137 -74.102 1.00118.33 C ANISOU 112 CB TYR A 26 15188 17463 12310 -927 -940 -1520 C ATOM 113 CG TYR A 26 -30.146 -24.874 -74.237 1.00131.47 C ANISOU 113 CG TYR A 26 17051 18920 13982 -900 -800 -1623 C ATOM 114 CD1 TYR A 26 -29.775 -25.458 -75.441 1.00136.44 C ANISOU 114 CD1 TYR A 26 17835 19587 14420 -939 -789 -1743 C ATOM 115 CD2 TYR A 26 -29.285 -25.005 -73.153 1.00131.15 C ANISOU 115 CD2 TYR A 26 17041 18654 14134 -832 -679 -1599 C ATOM 116 CE1 TYR A 26 -28.579 -26.141 -75.565 1.00137.32 C ANISOU 116 CE1 TYR A 26 18126 19511 14540 -895 -647 -1830 C ATOM 117 CE2 TYR A 26 -28.087 -25.682 -73.269 1.00127.19 C ANISOU 117 CE2 TYR A 26 16705 17976 13644 -793 -547 -1677 C ATOM 118 CZ TYR A 26 -27.738 -26.247 -74.476 1.00132.09 C ANISOU 118 CZ TYR A 26 17475 18632 14081 -819 -526 -1790 C ATOM 119 OH TYR A 26 -26.546 -26.924 -74.596 1.00129.71 O ANISOU 119 OH TYR A 26 17336 18157 13792 -762 -381 -1860 O ATOM 120 N ILE A 27 -29.228 -21.642 -73.728 1.00 85.79 N ANISOU 120 N ILE A 27 11054 13188 8356 -495 -722 -1183 N ATOM 121 CA ILE A 27 -28.324 -20.904 -72.853 1.00 79.61 C ANISOU 121 CA ILE A 27 10257 12247 7745 -368 -621 -1072 C ATOM 122 C ILE A 27 -28.711 -19.433 -72.800 1.00 81.35 C ANISOU 122 C ILE A 27 10352 12566 7991 -250 -660 -890 C ATOM 123 O ILE A 27 -28.739 -18.825 -71.725 1.00 83.33 O ANISOU 123 O ILE A 27 10533 12726 8403 -194 -639 -810 O ATOM 124 CB ILE A 27 -26.866 -21.094 -73.314 1.00 70.02 C ANISOU 124 CB ILE A 27 9177 10917 6509 -299 -494 -1088 C ATOM 125 CG1 ILE A 27 -26.334 -22.453 -72.856 1.00 84.36 C ANISOU 125 CG1 ILE A 27 11108 12561 8383 -378 -421 -1239 C ATOM 126 CG2 ILE A 27 -25.981 -19.961 -72.804 1.00 56.66 C ANISOU 126 CG2 ILE A 27 7446 9136 4945 -161 -418 -931 C ATOM 127 CD1 ILE A 27 -24.863 -22.650 -73.130 1.00 89.05 C ANISOU 127 CD1 ILE A 27 11815 13033 8985 -292 -281 -1238 C ATOM 128 N PHE A 28 -29.033 -18.844 -73.953 1.00 90.01 N ANISOU 128 N PHE A 28 11427 13847 8925 -207 -715 -822 N ATOM 129 CA PHE A 28 -29.397 -17.434 -74.017 1.00 89.11 C ANISOU 129 CA PHE A 28 11206 13824 8827 -81 -744 -637 C ATOM 130 C PHE A 28 -30.719 -17.128 -73.328 1.00 82.18 C ANISOU 130 C PHE A 28 10179 13035 8013 -97 -837 -591 C ATOM 131 O PHE A 28 -31.036 -15.950 -73.133 1.00 94.52 O ANISOU 131 O PHE A 28 11654 14632 9625 23 -843 -436 O ATOM 132 CB PHE A 28 -29.458 -16.981 -75.477 1.00 96.19 C ANISOU 132 CB PHE A 28 12118 14913 9517 -31 -782 -571 C ATOM 133 CG PHE A 28 -28.171 -17.179 -76.225 1.00 92.93 C ANISOU 133 CG PHE A 28 11844 14435 9029 4 -680 -595 C ATOM 134 CD1 PHE A 28 -26.955 -16.940 -75.609 1.00 86.30 C ANISOU 134 CD1 PHE A 28 11060 13391 8340 69 -554 -559 C ATOM 135 CD2 PHE A 28 -28.177 -17.614 -77.540 1.00 98.61 C ANISOU 135 CD2 PHE A 28 12637 15308 9522 -28 -708 -654 C ATOM 136 CE1 PHE A 28 -25.769 -17.123 -76.292 1.00 89.91 C ANISOU 136 CE1 PHE A 28 11628 13803 8733 108 -451 -567 C ATOM 137 CE2 PHE A 28 -26.992 -17.800 -78.229 1.00 91.51 C ANISOU 137 CE2 PHE A 28 11865 14355 8548 18 -598 -671 C ATOM 138 CZ PHE A 28 -25.787 -17.554 -77.604 1.00 88.83 C ANISOU 138 CZ PHE A 28 11565 13815 8370 90 -466 -622 C ATOM 139 N VAL A 29 -31.492 -18.146 -72.958 1.00 67.29 N ANISOU 139 N VAL A 29 8260 11179 6128 -238 -899 -714 N ATOM 140 CA VAL A 29 -32.769 -17.961 -72.288 1.00 63.67 C ANISOU 140 CA VAL A 29 7645 10818 5729 -261 -980 -669 C ATOM 141 C VAL A 29 -32.688 -18.325 -70.810 1.00 80.44 C ANISOU 141 C VAL A 29 9759 12756 8047 -290 -922 -713 C ATOM 142 O VAL A 29 -33.253 -17.626 -69.965 1.00 83.40 O ANISOU 142 O VAL A 29 10028 13131 8528 -218 -923 -617 O ATOM 143 CB VAL A 29 -33.878 -18.770 -72.997 1.00 67.98 C ANISOU 143 CB VAL A 29 8130 11578 6123 -413 -1112 -754 C ATOM 144 CG1 VAL A 29 -35.190 -18.674 -72.233 1.00 70.52 C ANISOU 144 CG1 VAL A 29 8270 12004 6519 -447 -1187 -703 C ATOM 145 CG2 VAL A 29 -34.056 -18.278 -74.425 1.00 66.96 C ANISOU 145 CG2 VAL A 29 7991 11663 5786 -370 -1182 -690 C ATOM 146 N MET A 30 -31.977 -19.403 -70.476 1.00 86.91 N ANISOU 146 N MET A 30 10696 13416 8911 -384 -863 -850 N ATOM 147 CA MET A 30 -31.941 -19.869 -69.093 1.00 83.62 C ANISOU 147 CA MET A 30 10270 12838 8662 -422 -813 -891 C ATOM 148 C MET A 30 -30.898 -19.126 -68.266 1.00 76.79 C ANISOU 148 C MET A 30 9451 11791 7937 -295 -709 -816 C ATOM 149 O MET A 30 -31.164 -18.764 -67.113 1.00 75.56 O ANISOU 149 O MET A 30 9233 11568 7908 -257 -689 -770 O ATOM 150 CB MET A 30 -31.676 -21.374 -69.053 1.00 86.61 C ANISOU 150 CB MET A 30 10754 13119 9034 -575 -793 -1060 C ATOM 151 CG MET A 30 -31.589 -21.950 -67.648 1.00 88.49 C ANISOU 151 CG MET A 30 10993 13190 9439 -616 -736 -1096 C ATOM 152 SD MET A 30 -31.429 -23.745 -67.634 1.00 94.16 S ANISOU 152 SD MET A 30 11834 13790 10152 -797 -713 -1282 S ATOM 153 CE MET A 30 -29.891 -23.960 -68.524 1.00104.34 C ANISOU 153 CE MET A 30 13307 14966 11370 -731 -618 -1335 C ATOM 154 N ILE A 31 -29.709 -18.894 -68.831 1.00 69.46 N ANISOU 154 N ILE A 31 8627 10787 6979 -233 -642 -804 N ATOM 155 CA ILE A 31 -28.634 -18.260 -68.062 1.00 72.54 C ANISOU 155 CA ILE A 31 9057 11004 7500 -138 -550 -739 C ATOM 156 C ILE A 31 -29.006 -16.855 -67.596 1.00 80.85 C ANISOU 156 C ILE A 31 10027 12073 8619 -21 -561 -597 C ATOM 157 O ILE A 31 -28.740 -16.530 -66.425 1.00 89.35 O ANISOU 157 O ILE A 31 11099 13020 9831 13 -518 -574 O ATOM 158 CB ILE A 31 -27.319 -18.293 -68.864 1.00 67.63 C ANISOU 158 CB ILE A 31 8546 10324 6828 -100 -476 -740 C ATOM 159 CG1 ILE A 31 -26.913 -19.736 -69.160 1.00 63.29 C ANISOU 159 CG1 ILE A 31 8095 9722 6229 -201 -444 -888 C ATOM 160 CG2 ILE A 31 -26.210 -17.577 -68.106 1.00 52.87 C ANISOU 160 CG2 ILE A 31 6700 8295 5092 -17 -394 -660 C ATOM 161 CD1 ILE A 31 -26.660 -20.564 -67.919 1.00 69.21 C ANISOU 161 CD1 ILE A 31 8867 10312 7117 -255 -399 -958 C ATOM 162 N PRO A 32 -29.594 -15.983 -68.423 1.00 85.65 N ANISOU 162 N PRO A 32 10576 12829 9137 50 -611 -498 N ATOM 163 CA PRO A 32 -30.035 -14.682 -67.889 1.00 78.70 C ANISOU 163 CA PRO A 32 9625 11944 8332 170 -611 -366 C ATOM 164 C PRO A 32 -31.067 -14.803 -66.782 1.00 83.05 C ANISOU 164 C PRO A 32 10083 12507 8965 155 -638 -380 C ATOM 165 O PRO A 32 -31.086 -13.966 -65.871 1.00 85.67 O ANISOU 165 O PRO A 32 10401 12745 9404 243 -600 -314 O ATOM 166 CB PRO A 32 -30.611 -13.974 -69.123 1.00 67.74 C ANISOU 166 CB PRO A 32 8185 10742 6810 239 -668 -262 C ATOM 167 CG PRO A 32 -29.918 -14.605 -70.268 1.00 76.04 C ANISOU 167 CG PRO A 32 9321 11838 7732 182 -664 -322 C ATOM 168 CD PRO A 32 -29.755 -16.041 -69.888 1.00 79.16 C ANISOU 168 CD PRO A 32 9765 12172 8140 41 -659 -490 C ATOM 169 N THR A 33 -31.931 -15.819 -66.835 1.00 78.80 N ANISOU 169 N THR A 33 9484 12079 8376 41 -701 -464 N ATOM 170 CA THR A 33 -32.891 -16.030 -65.756 1.00 79.49 C ANISOU 170 CA THR A 33 9475 12183 8544 17 -717 -472 C ATOM 171 C THR A 33 -32.185 -16.404 -64.459 1.00 79.19 C ANISOU 171 C THR A 33 9506 11942 8641 -4 -639 -532 C ATOM 172 O THR A 33 -32.566 -15.935 -63.380 1.00 81.17 O ANISOU 172 O THR A 33 9712 12146 8984 55 -612 -491 O ATOM 173 CB THR A 33 -33.898 -17.111 -66.154 1.00 70.62 C ANISOU 173 CB THR A 33 8273 11220 7339 -127 -802 -550 C ATOM 174 OG1 THR A 33 -34.669 -16.659 -67.275 1.00 71.53 O ANISOU 174 OG1 THR A 33 8301 11554 7323 -100 -888 -477 O ATOM 175 CG2 THR A 33 -34.835 -17.429 -64.997 1.00 58.50 C ANISOU 175 CG2 THR A 33 6632 9699 5894 -164 -807 -554 C ATOM 176 N LEU A 34 -31.147 -17.238 -64.546 1.00 71.18 N ANISOU 176 N LEU A 34 8602 10810 7632 -79 -599 -624 N ATOM 177 CA LEU A 34 -30.402 -17.622 -63.352 1.00 69.16 C ANISOU 177 CA LEU A 34 8408 10374 7497 -95 -529 -669 C ATOM 178 C LEU A 34 -29.666 -16.431 -62.750 1.00 81.74 C ANISOU 178 C LEU A 34 10037 11850 9172 24 -476 -585 C ATOM 179 O LEU A 34 -29.609 -16.286 -61.524 1.00 87.91 O ANISOU 179 O LEU A 34 10818 12534 10048 44 -443 -585 O ATOM 180 CB LEU A 34 -29.425 -18.748 -63.683 1.00 61.57 C ANISOU 180 CB LEU A 34 7553 9322 6518 -182 -492 -770 C ATOM 181 CG LEU A 34 -30.068 -20.099 -63.997 1.00 68.72 C ANISOU 181 CG LEU A 34 8455 10286 7369 -324 -531 -880 C ATOM 182 CD1 LEU A 34 -29.015 -21.126 -64.379 1.00 76.72 C ANISOU 182 CD1 LEU A 34 9597 11188 8366 -382 -475 -974 C ATOM 183 CD2 LEU A 34 -30.877 -20.577 -62.805 1.00 71.18 C ANISOU 183 CD2 LEU A 34 8697 10582 7766 -381 -536 -897 C ATOM 184 N TYR A 35 -29.097 -15.567 -63.596 1.00 79.55 N ANISOU 184 N TYR A 35 9794 11577 8853 98 -468 -515 N ATOM 185 CA TYR A 35 -28.442 -14.366 -63.089 1.00 77.62 C ANISOU 185 CA TYR A 35 9588 11215 8688 197 -423 -432 C ATOM 186 C TYR A 35 -29.429 -13.451 -62.376 1.00 64.90 C ANISOU 186 C TYR A 35 7912 9625 7120 284 -434 -367 C ATOM 187 O TYR A 35 -29.041 -12.707 -61.469 1.00 64.00 O ANISOU 187 O TYR A 35 7840 9384 7094 341 -393 -339 O ATOM 188 CB TYR A 35 -27.753 -13.615 -64.231 1.00 87.94 C ANISOU 188 CB TYR A 35 10938 12535 9941 253 -411 -354 C ATOM 189 CG TYR A 35 -26.526 -14.309 -64.782 1.00 84.96 C ANISOU 189 CG TYR A 35 10636 12105 9538 196 -371 -402 C ATOM 190 CD1 TYR A 35 -25.895 -15.321 -64.069 1.00 80.22 C ANISOU 190 CD1 TYR A 35 10075 11408 8996 122 -337 -492 C ATOM 191 CD2 TYR A 35 -25.996 -13.948 -66.014 1.00 81.33 C ANISOU 191 CD2 TYR A 35 10208 11697 8997 229 -359 -345 C ATOM 192 CE1 TYR A 35 -24.772 -15.955 -64.570 1.00 75.11 C ANISOU 192 CE1 TYR A 35 9494 10715 8330 90 -289 -526 C ATOM 193 CE2 TYR A 35 -24.874 -14.576 -66.522 1.00 76.34 C ANISOU 193 CE2 TYR A 35 9642 11024 8339 192 -308 -382 C ATOM 194 CZ TYR A 35 -24.267 -15.578 -65.796 1.00 73.08 C ANISOU 194 CZ TYR A 35 9264 10513 7990 127 -271 -473 C ATOM 195 OH TYR A 35 -23.150 -16.206 -66.299 1.00 78.03 O ANISOU 195 OH TYR A 35 9952 11100 8594 109 -209 -500 O ATOM 196 N SER A 36 -30.704 -13.492 -62.768 1.00 72.26 N ANISOU 196 N SER A 36 8743 10722 7989 298 -487 -341 N ATOM 197 CA SER A 36 -31.716 -12.705 -62.071 1.00 72.16 C ANISOU 197 CA SER A 36 8657 10744 8017 395 -486 -273 C ATOM 198 C SER A 36 -32.024 -13.296 -60.702 1.00 75.20 C ANISOU 198 C SER A 36 9024 11071 8477 352 -461 -340 C ATOM 199 O SER A 36 -32.230 -12.557 -59.732 1.00 76.28 O ANISOU 199 O SER A 36 9168 11135 8680 439 -420 -307 O ATOM 200 CB SER A 36 -32.986 -12.616 -62.917 1.00 69.68 C ANISOU 200 CB SER A 36 8216 10648 7611 424 -553 -211 C ATOM 201 OG SER A 36 -32.718 -12.033 -64.180 1.00 74.92 O ANISOU 201 OG SER A 36 8897 11376 8193 474 -575 -137 O ATOM 202 N ILE A 37 -32.061 -14.626 -60.604 1.00 73.47 N ANISOU 202 N ILE A 37 8791 10878 8245 219 -480 -435 N ATOM 203 CA ILE A 37 -32.307 -15.271 -59.318 1.00 77.01 C ANISOU 203 CA ILE A 37 9225 11272 8762 172 -450 -489 C ATOM 204 C ILE A 37 -31.147 -15.017 -58.364 1.00 78.42 C ANISOU 204 C ILE A 37 9515 11260 9020 194 -390 -512 C ATOM 205 O ILE A 37 -31.351 -14.754 -57.173 1.00 80.37 O ANISOU 205 O ILE A 37 9765 11450 9324 234 -354 -510 O ATOM 206 CB ILE A 37 -32.560 -16.777 -59.518 1.00 68.22 C ANISOU 206 CB ILE A 37 8085 10214 7620 17 -481 -579 C ATOM 207 CG1 ILE A 37 -33.733 -16.996 -60.476 1.00 65.74 C ANISOU 207 CG1 ILE A 37 7654 10104 7218 -24 -557 -559 C ATOM 208 CG2 ILE A 37 -32.824 -17.458 -58.184 1.00 56.59 C ANISOU 208 CG2 ILE A 37 6596 8685 6220 -31 -444 -618 C ATOM 209 CD1 ILE A 37 -34.011 -18.452 -60.780 1.00 57.36 C ANISOU 209 CD1 ILE A 37 6580 9090 6122 -196 -595 -657 C ATOM 210 N ILE A 38 -29.913 -15.089 -58.869 1.00 73.33 N ANISOU 210 N ILE A 38 8961 10526 8375 166 -378 -531 N ATOM 211 CA ILE A 38 -28.748 -14.797 -58.038 1.00 58.05 C ANISOU 211 CA ILE A 38 7117 8428 6512 179 -332 -541 C ATOM 212 C ILE A 38 -28.759 -13.337 -57.603 1.00 71.49 C ANISOU 212 C ILE A 38 8847 10067 8250 292 -313 -473 C ATOM 213 O ILE A 38 -28.353 -13.002 -56.483 1.00 82.62 O ANISOU 213 O ILE A 38 10309 11366 9717 308 -284 -487 O ATOM 214 CB ILE A 38 -27.453 -15.154 -58.793 1.00 53.81 C ANISOU 214 CB ILE A 38 6649 7833 5964 132 -320 -558 C ATOM 215 CG1 ILE A 38 -27.445 -16.636 -59.173 1.00 56.06 C ANISOU 215 CG1 ILE A 38 6930 8157 6214 29 -325 -637 C ATOM 216 CG2 ILE A 38 -26.228 -14.811 -57.957 1.00 42.14 C ANISOU 216 CG2 ILE A 38 5243 6207 4560 137 -283 -554 C ATOM 217 CD1 ILE A 38 -26.247 -17.045 -60.004 1.00 45.01 C ANISOU 217 CD1 ILE A 38 5597 6713 4792 0 -300 -653 C ATOM 218 N PHE A 39 -29.235 -12.447 -58.476 1.00 71.52 N ANISOU 218 N PHE A 39 8824 10135 8214 371 -329 -397 N ATOM 219 CA PHE A 39 -29.227 -11.021 -58.166 1.00 71.46 C ANISOU 219 CA PHE A 39 8861 10045 8245 485 -302 -328 C ATOM 220 C PHE A 39 -30.195 -10.695 -57.035 1.00 71.75 C ANISOU 220 C PHE A 39 8868 10082 8309 556 -278 -330 C ATOM 221 O PHE A 39 -29.823 -10.035 -56.058 1.00 70.55 O ANISOU 221 O PHE A 39 8797 9798 8210 595 -241 -342 O ATOM 222 CB PHE A 39 -29.565 -10.213 -59.419 1.00 66.10 C ANISOU 222 CB PHE A 39 8157 9444 7515 564 -319 -230 C ATOM 223 CG PHE A 39 -29.513 -8.726 -59.214 1.00 69.05 C ANISOU 223 CG PHE A 39 8592 9709 7933 685 -283 -150 C ATOM 224 CD1 PHE A 39 -28.300 -8.056 -59.217 1.00 67.83 C ANISOU 224 CD1 PHE A 39 8546 9399 7829 672 -257 -133 C ATOM 225 CD2 PHE A 39 -30.675 -7.996 -59.026 1.00 54.95 C ANISOU 225 CD2 PHE A 39 6759 7976 6144 812 -270 -86 C ATOM 226 CE1 PHE A 39 -28.248 -6.688 -59.031 1.00 57.97 C ANISOU 226 CE1 PHE A 39 7371 8029 6627 769 -221 -64 C ATOM 227 CE2 PHE A 39 -30.629 -6.627 -58.839 1.00 58.91 C ANISOU 227 CE2 PHE A 39 7338 8356 6691 931 -224 -15 C ATOM 228 CZ PHE A 39 -29.413 -5.973 -58.842 1.00 60.33 C ANISOU 228 CZ PHE A 39 7640 8362 6921 903 -201 -8 C ATOM 229 N VAL A 40 -31.443 -11.153 -57.147 1.00 74.13 N ANISOU 229 N VAL A 40 9055 10539 8572 569 -298 -318 N ATOM 230 CA VAL A 40 -32.449 -10.827 -56.140 1.00 75.13 C ANISOU 230 CA VAL A 40 9137 10690 8720 652 -264 -304 C ATOM 231 C VAL A 40 -32.101 -11.477 -54.805 1.00 84.81 C ANISOU 231 C VAL A 40 10406 11832 9986 588 -234 -387 C ATOM 232 O VAL A 40 -32.165 -10.836 -53.750 1.00 84.28 O ANISOU 232 O VAL A 40 10395 11678 9949 662 -185 -393 O ATOM 233 CB VAL A 40 -33.849 -11.247 -56.623 1.00 64.19 C ANISOU 233 CB VAL A 40 7591 9513 7284 665 -297 -260 C ATOM 234 CG1 VAL A 40 -34.893 -10.932 -55.565 1.00 52.17 C ANISOU 234 CG1 VAL A 40 6008 8028 5785 762 -248 -233 C ATOM 235 CG2 VAL A 40 -34.187 -10.553 -57.934 1.00 80.27 C ANISOU 235 CG2 VAL A 40 9582 11649 9269 739 -333 -165 C ATOM 236 N VAL A 41 -31.725 -12.756 -54.832 1.00 75.65 N ANISOU 236 N VAL A 41 9231 10693 8821 455 -257 -451 N ATOM 237 CA VAL A 41 -31.384 -13.455 -53.596 1.00 54.26 C ANISOU 237 CA VAL A 41 6557 7914 6146 395 -229 -515 C ATOM 238 C VAL A 41 -30.082 -12.916 -53.017 1.00 68.90 C ANISOU 238 C VAL A 41 8541 9599 8037 398 -210 -540 C ATOM 239 O VAL A 41 -29.938 -12.782 -51.795 1.00 81.73 O ANISOU 239 O VAL A 41 10216 11155 9682 414 -179 -569 O ATOM 240 CB VAL A 41 -31.314 -14.972 -53.846 1.00 49.40 C ANISOU 240 CB VAL A 41 5898 7350 5520 257 -253 -567 C ATOM 241 CG1 VAL A 41 -30.855 -15.702 -52.594 1.00 49.36 C ANISOU 241 CG1 VAL A 41 5937 7266 5552 203 -219 -616 C ATOM 242 CG2 VAL A 41 -32.668 -15.495 -54.301 1.00 58.39 C ANISOU 242 CG2 VAL A 41 6903 8658 6624 232 -279 -547 C ATOM 243 N GLY A 42 -29.117 -12.589 -53.879 1.00 73.79 N ANISOU 243 N GLY A 42 9213 10162 8660 377 -231 -526 N ATOM 244 CA GLY A 42 -27.845 -12.082 -53.390 1.00 58.23 C ANISOU 244 CA GLY A 42 7349 8045 6729 361 -222 -540 C ATOM 245 C GLY A 42 -27.959 -10.704 -52.767 1.00 61.14 C ANISOU 245 C GLY A 42 7792 8321 7118 457 -197 -520 C ATOM 246 O GLY A 42 -27.379 -10.443 -51.709 1.00 70.24 O ANISOU 246 O GLY A 42 9023 9372 8292 442 -186 -559 O ATOM 247 N ILE A 43 -28.695 -9.800 -53.416 1.00 61.73 N ANISOU 247 N ILE A 43 7849 8426 7180 558 -188 -457 N ATOM 248 CA ILE A 43 -28.882 -8.463 -52.860 1.00 59.06 C ANISOU 248 CA ILE A 43 7596 7981 6863 664 -151 -438 C ATOM 249 C ILE A 43 -29.696 -8.531 -51.573 1.00 70.78 C ANISOU 249 C ILE A 43 9080 9477 8337 719 -111 -479 C ATOM 250 O ILE A 43 -29.438 -7.789 -50.620 1.00 77.13 O ANISOU 250 O ILE A 43 9994 10158 9154 757 -80 -515 O ATOM 251 CB ILE A 43 -29.536 -7.537 -53.903 1.00 56.03 C ANISOU 251 CB ILE A 43 7187 7634 6469 777 -141 -343 C ATOM 252 CG1 ILE A 43 -28.581 -7.289 -55.073 1.00 67.55 C ANISOU 252 CG1 ILE A 43 8672 9057 7935 728 -169 -296 C ATOM 253 CG2 ILE A 43 -29.946 -6.214 -53.275 1.00 52.18 C ANISOU 253 CG2 ILE A 43 6789 7032 6004 910 -86 -322 C ATOM 254 CD1 ILE A 43 -27.322 -6.542 -54.688 1.00 65.77 C ANISOU 254 CD1 ILE A 43 8578 8646 7764 683 -161 -312 C ATOM 255 N PHE A 44 -30.678 -9.433 -51.517 1.00 82.03 N ANISOU 255 N PHE A 44 10384 11051 9732 717 -109 -477 N ATOM 256 CA PHE A 44 -31.495 -9.566 -50.316 1.00 87.22 C ANISOU 256 CA PHE A 44 11024 11739 10375 772 -61 -503 C ATOM 257 C PHE A 44 -30.684 -10.125 -49.152 1.00 90.24 C ANISOU 257 C PHE A 44 11481 12044 10761 685 -60 -581 C ATOM 258 O PHE A 44 -30.680 -9.555 -48.055 1.00103.41 O ANISOU 258 O PHE A 44 13239 13634 12418 740 -20 -618 O ATOM 259 CB PHE A 44 -32.706 -10.455 -50.604 1.00 89.34 C ANISOU 259 CB PHE A 44 11130 12196 10619 768 -64 -469 C ATOM 260 CG PHE A 44 -33.374 -10.994 -49.370 1.00105.67 C ANISOU 260 CG PHE A 44 13162 14314 12675 778 -17 -495 C ATOM 261 CD1 PHE A 44 -33.124 -12.288 -48.939 1.00111.18 C ANISOU 261 CD1 PHE A 44 13826 15044 13373 651 -32 -539 C ATOM 262 CD2 PHE A 44 -34.252 -10.209 -48.641 1.00115.19 C ANISOU 262 CD2 PHE A 44 14371 15531 13867 924 53 -470 C ATOM 263 CE1 PHE A 44 -33.735 -12.788 -47.805 1.00112.06 C ANISOU 263 CE1 PHE A 44 13903 15204 13471 660 17 -550 C ATOM 264 CE2 PHE A 44 -34.867 -10.704 -47.506 1.00120.91 C ANISOU 264 CE2 PHE A 44 15058 16310 14571 939 106 -486 C ATOM 265 CZ PHE A 44 -34.608 -11.994 -47.087 1.00116.43 C ANISOU 265 CZ PHE A 44 14453 15781 14003 802 86 -523 C ATOM 266 N GLY A 45 -29.989 -11.241 -49.375 1.00 81.69 N ANISOU 266 N GLY A 45 10368 10984 9686 556 -100 -607 N ATOM 267 CA GLY A 45 -29.301 -11.901 -48.277 1.00 84.78 C ANISOU 267 CA GLY A 45 10808 11328 10077 481 -99 -662 C ATOM 268 C GLY A 45 -28.099 -11.121 -47.778 1.00 83.43 C ANISOU 268 C GLY A 45 10770 11012 9919 462 -116 -695 C ATOM 269 O GLY A 45 -27.933 -10.918 -46.572 1.00 96.79 O ANISOU 269 O GLY A 45 12534 12653 11588 471 -99 -739 O ATOM 270 N ASN A 46 -27.244 -10.673 -48.699 1.00 69.79 N ANISOU 270 N ASN A 46 9073 9223 8222 428 -150 -673 N ATOM 271 CA ASN A 46 -26.011 -10.001 -48.303 1.00 67.35 C ANISOU 271 CA ASN A 46 8873 8784 7933 380 -175 -697 C ATOM 272 C ASN A 46 -26.257 -8.617 -47.715 1.00 71.66 C ANISOU 272 C ASN A 46 9535 9221 8473 462 -149 -718 C ATOM 273 O ASN A 46 -25.409 -8.120 -46.968 1.00 83.40 O ANISOU 273 O ASN A 46 11124 10603 9961 413 -170 -762 O ATOM 274 CB ASN A 46 -25.060 -9.903 -49.496 1.00 74.49 C ANISOU 274 CB ASN A 46 9767 9660 8876 321 -209 -654 C ATOM 275 CG ASN A 46 -24.534 -11.257 -49.931 1.00 88.43 C ANISOU 275 CG ASN A 46 11452 11500 10646 235 -228 -649 C ATOM 276 OD1 ASN A 46 -24.211 -12.106 -49.100 1.00 99.36 O ANISOU 276 OD1 ASN A 46 12828 12900 12024 184 -232 -681 O ATOM 277 ND2 ASN A 46 -24.453 -11.468 -51.239 1.00 94.58 N ANISOU 277 ND2 ASN A 46 12181 12325 11430 227 -233 -608 N ATOM 278 N SER A 47 -27.389 -7.983 -48.031 1.00 67.44 N ANISOU 278 N SER A 47 8986 8708 7929 586 -104 -686 N ATOM 279 CA SER A 47 -27.687 -6.686 -47.431 1.00 68.29 C ANISOU 279 CA SER A 47 9220 8698 8031 683 -61 -709 C ATOM 280 C SER A 47 -28.068 -6.836 -45.964 1.00 73.22 C ANISOU 280 C SER A 47 9897 9323 8602 713 -27 -780 C ATOM 281 O SER A 47 -27.630 -6.046 -45.120 1.00 84.47 O ANISOU 281 O SER A 47 11465 10620 10009 714 -20 -843 O ATOM 282 CB SER A 47 -28.803 -5.984 -48.202 1.00 69.28 C ANISOU 282 CB SER A 47 9307 8854 8163 829 -13 -637 C ATOM 283 OG SER A 47 -28.439 -5.783 -49.557 1.00 87.00 O ANISOU 283 OG SER A 47 11513 11101 10442 807 -44 -565 O ATOM 284 N LEU A 48 -28.883 -7.844 -45.642 1.00 69.04 N ANISOU 284 N LEU A 48 9254 8936 8040 731 -3 -772 N ATOM 285 CA LEU A 48 -29.267 -8.070 -44.254 1.00 67.60 C ANISOU 285 CA LEU A 48 9112 8774 7799 762 38 -827 C ATOM 286 C LEU A 48 -28.070 -8.454 -43.394 1.00 68.71 C ANISOU 286 C LEU A 48 9328 8861 7918 638 -14 -890 C ATOM 287 O LEU A 48 -28.032 -8.118 -42.205 1.00 77.95 O ANISOU 287 O LEU A 48 10603 9987 9028 660 7 -953 O ATOM 288 CB LEU A 48 -30.346 -9.150 -44.176 1.00 58.41 C ANISOU 288 CB LEU A 48 7796 7781 6617 787 74 -787 C ATOM 289 CG LEU A 48 -31.670 -8.829 -44.871 1.00 71.82 C ANISOU 289 CG LEU A 48 9393 9570 8325 913 123 -716 C ATOM 290 CD1 LEU A 48 -32.629 -10.003 -44.768 1.00 79.28 C ANISOU 290 CD1 LEU A 48 10176 10690 9257 898 144 -677 C ATOM 291 CD2 LEU A 48 -32.292 -7.572 -44.283 1.00 78.99 C ANISOU 291 CD2 LEU A 48 10402 10404 9206 1077 203 -727 C ATOM 292 N VAL A 49 -27.089 -9.151 -43.972 1.00 64.47 N ANISOU 292 N VAL A 49 8740 8336 7420 514 -81 -870 N ATOM 293 CA VAL A 49 -25.888 -9.506 -43.222 1.00 66.88 C ANISOU 293 CA VAL A 49 9098 8605 7710 400 -136 -910 C ATOM 294 C VAL A 49 -25.132 -8.251 -42.803 1.00 71.88 C ANISOU 294 C VAL A 49 9886 9091 8334 379 -165 -965 C ATOM 295 O VAL A 49 -24.624 -8.160 -41.678 1.00 84.92 O ANISOU 295 O VAL A 49 11623 10712 9930 333 -190 -1026 O ATOM 296 CB VAL A 49 -25.001 -10.454 -44.052 1.00 60.97 C ANISOU 296 CB VAL A 49 8256 7898 7013 293 -188 -864 C ATOM 297 CG1 VAL A 49 -23.690 -10.730 -43.334 1.00 69.68 C ANISOU 297 CG1 VAL A 49 9399 8970 8105 185 -248 -886 C ATOM 298 CG2 VAL A 49 -25.738 -11.754 -44.336 1.00 54.48 C ANISOU 298 CG2 VAL A 49 7306 7202 6193 297 -160 -828 C ATOM 299 N VAL A 50 -25.057 -7.260 -43.693 1.00 61.44 N ANISOU 299 N VAL A 50 8606 7675 7063 405 -164 -942 N ATOM 300 CA VAL A 50 -24.375 -6.014 -43.359 1.00 62.64 C ANISOU 300 CA VAL A 50 8916 7665 7219 373 -187 -994 C ATOM 301 C VAL A 50 -25.179 -5.222 -42.334 1.00 69.90 C ANISOU 301 C VAL A 50 9970 8519 8072 482 -125 -1068 C ATOM 302 O VAL A 50 -24.613 -4.592 -41.433 1.00 73.15 O ANISOU 302 O VAL A 50 10527 8827 8441 431 -151 -1151 O ATOM 303 CB VAL A 50 -24.115 -5.193 -44.636 1.00 55.98 C ANISOU 303 CB VAL A 50 8082 6734 6455 377 -191 -934 C ATOM 304 CG1 VAL A 50 -23.402 -3.891 -44.300 1.00 59.30 C ANISOU 304 CG1 VAL A 50 8674 6967 6891 327 -213 -984 C ATOM 305 CG2 VAL A 50 -23.304 -6.006 -45.632 1.00 56.35 C ANISOU 305 CG2 VAL A 50 8002 6855 6553 278 -241 -863 C ATOM 306 N ILE A 51 -26.509 -5.248 -42.448 1.00 67.49 N ANISOU 306 N ILE A 51 9616 8278 7751 632 -41 -1040 N ATOM 307 CA ILE A 51 -27.352 -4.479 -41.538 1.00 78.52 C ANISOU 307 CA ILE A 51 11134 9616 9083 765 40 -1100 C ATOM 308 C ILE A 51 -27.271 -5.040 -40.123 1.00 78.03 C ANISOU 308 C ILE A 51 11114 9611 8923 733 38 -1175 C ATOM 309 O ILE A 51 -27.251 -4.286 -39.142 1.00 91.70 O ANISOU 309 O ILE A 51 13014 11245 10583 766 63 -1267 O ATOM 310 CB ILE A 51 -28.801 -4.448 -42.059 1.00 76.29 C ANISOU 310 CB ILE A 51 10754 9420 8812 938 132 -1028 C ATOM 311 CG1 ILE A 51 -28.871 -3.689 -43.385 1.00 67.62 C ANISOU 311 CG1 ILE A 51 9642 8253 7795 985 135 -952 C ATOM 312 CG2 ILE A 51 -29.733 -3.818 -41.035 1.00 66.08 C ANISOU 312 CG2 ILE A 51 9567 8094 7446 1094 234 -1081 C ATOM 313 CD1 ILE A 51 -30.241 -3.690 -44.015 1.00 49.05 C ANISOU 313 CD1 ILE A 51 7169 6012 5455 1148 208 -862 C ATOM 314 N VAL A 52 -27.212 -6.365 -39.991 1.00 67.96 N ANISOU 314 N VAL A 52 9699 8487 7636 670 11 -1138 N ATOM 315 CA VAL A 52 -27.180 -6.975 -38.665 1.00 65.47 C ANISOU 315 CA VAL A 52 9410 8241 7222 649 15 -1188 C ATOM 316 C VAL A 52 -25.803 -6.826 -38.027 1.00 81.49 C ANISOU 316 C VAL A 52 11544 10202 9217 503 -82 -1254 C ATOM 317 O VAL A 52 -25.689 -6.540 -36.831 1.00 89.12 O ANISOU 317 O VAL A 52 12635 11147 10080 503 -81 -1337 O ATOM 318 CB VAL A 52 -27.609 -8.450 -38.753 1.00 59.69 C ANISOU 318 CB VAL A 52 8497 7683 6499 631 26 -1114 C ATOM 319 CG1 VAL A 52 -27.428 -9.138 -37.410 1.00 69.05 C ANISOU 319 CG1 VAL A 52 9709 8941 7587 598 25 -1148 C ATOM 320 CG2 VAL A 52 -29.055 -8.553 -39.212 1.00 58.23 C ANISOU 320 CG2 VAL A 52 8208 7583 6333 767 118 -1055 C ATOM 321 N ILE A 53 -24.739 -7.005 -38.807 1.00 83.98 N ANISOU 321 N ILE A 53 11807 10493 9609 377 -168 -1216 N ATOM 322 CA ILE A 53 -23.391 -7.007 -38.244 1.00 83.05 C ANISOU 322 CA ILE A 53 11745 10344 9465 227 -269 -1256 C ATOM 323 C ILE A 53 -22.928 -5.589 -37.932 1.00 85.72 C ANISOU 323 C ILE A 53 12274 10512 9784 192 -298 -1346 C ATOM 324 O ILE A 53 -22.549 -5.276 -36.797 1.00 90.87 O ANISOU 324 O ILE A 53 13052 11137 10339 143 -334 -1435 O ATOM 325 CB ILE A 53 -22.412 -7.719 -39.195 1.00 77.97 C ANISOU 325 CB ILE A 53 10967 9745 8914 114 -339 -1172 C ATOM 326 CG1 ILE A 53 -22.724 -9.214 -39.261 1.00 81.75 C ANISOU 326 CG1 ILE A 53 11290 10377 9397 128 -317 -1102 C ATOM 327 CG2 ILE A 53 -20.977 -7.493 -38.751 1.00 76.31 C ANISOU 327 CG2 ILE A 53 10806 9497 8691 -39 -446 -1198 C ATOM 328 CD1 ILE A 53 -21.801 -9.984 -40.171 1.00 97.93 C ANISOU 328 CD1 ILE A 53 13217 12464 11528 37 -368 -1024 C ATOM 329 N TYR A 54 -22.948 -4.710 -38.935 1.00 87.07 N ANISOU 329 N TYR A 54 12477 10562 10043 212 -282 -1324 N ATOM 330 CA TYR A 54 -22.357 -3.387 -38.784 1.00 91.05 C ANISOU 330 CA TYR A 54 13162 10880 10554 150 -316 -1399 C ATOM 331 C TYR A 54 -23.214 -2.434 -37.961 1.00110.61 C ANISOU 331 C TYR A 54 15830 13247 12949 272 -235 -1502 C ATOM 332 O TYR A 54 -22.673 -1.489 -37.376 1.00122.96 O ANISOU 332 O TYR A 54 17579 14663 14476 200 -271 -1602 O ATOM 333 CB TYR A 54 -22.086 -2.774 -40.161 1.00 77.53 C ANISOU 333 CB TYR A 54 11421 9069 8966 134 -317 -1325 C ATOM 334 CG TYR A 54 -21.320 -1.470 -40.115 1.00 75.75 C ANISOU 334 CG TYR A 54 11371 8642 8770 37 -359 -1384 C ATOM 335 CD1 TYR A 54 -19.944 -1.457 -39.929 1.00 69.48 C ANISOU 335 CD1 TYR A 54 10579 7831 7991 -164 -475 -1396 C ATOM 336 CD2 TYR A 54 -21.972 -0.252 -40.264 1.00 75.26 C ANISOU 336 CD2 TYR A 54 11468 8403 8726 143 -281 -1420 C ATOM 337 CE1 TYR A 54 -19.239 -0.268 -39.886 1.00 70.61 C ANISOU 337 CE1 TYR A 54 10877 7785 8165 -276 -519 -1450 C ATOM 338 CE2 TYR A 54 -21.275 0.942 -40.224 1.00 87.63 C ANISOU 338 CE2 TYR A 54 13208 9761 10326 43 -316 -1476 C ATOM 339 CZ TYR A 54 -19.909 0.927 -40.035 1.00 85.50 C ANISOU 339 CZ TYR A 54 12937 9478 10071 -177 -439 -1494 C ATOM 340 OH TYR A 54 -19.211 2.113 -39.994 1.00 92.87 O ANISOU 340 OH TYR A 54 14041 10202 11044 -299 -478 -1549 O ATOM 341 N PHE A 55 -24.527 -2.656 -37.891 1.00109.75 N ANISOU 341 N PHE A 55 15684 13206 12812 453 -124 -1481 N ATOM 342 CA PHE A 55 -25.421 -1.730 -37.206 1.00100.53 C ANISOU 342 CA PHE A 55 14689 11934 11572 602 -23 -1565 C ATOM 343 C PHE A 55 -26.007 -2.272 -35.912 1.00 90.11 C ANISOU 343 C PHE A 55 13395 10729 10114 671 25 -1624 C ATOM 344 O PHE A 55 -26.352 -1.481 -35.032 1.00 86.39 O ANISOU 344 O PHE A 55 13115 10160 9550 747 83 -1731 O ATOM 345 CB PHE A 55 -26.569 -1.314 -38.136 1.00 87.44 C ANISOU 345 CB PHE A 55 12981 10255 9988 788 88 -1484 C ATOM 346 CG PHE A 55 -26.116 -0.567 -39.360 1.00 85.72 C ANISOU 346 CG PHE A 55 12773 9904 9891 751 61 -1426 C ATOM 347 CD1 PHE A 55 -25.965 0.811 -39.330 1.00 80.25 C ANISOU 347 CD1 PHE A 55 12291 8982 9219 774 90 -1487 C ATOM 348 CD2 PHE A 55 -25.840 -1.241 -40.538 1.00 81.48 C ANISOU 348 CD2 PHE A 55 12047 9467 9446 693 14 -1309 C ATOM 349 CE1 PHE A 55 -25.548 1.502 -40.454 1.00 81.84 C ANISOU 349 CE1 PHE A 55 12503 9059 9535 739 72 -1418 C ATOM 350 CE2 PHE A 55 -25.422 -0.555 -41.665 1.00 72.81 C ANISOU 350 CE2 PHE A 55 10958 8257 8449 663 -4 -1245 C ATOM 351 CZ PHE A 55 -25.276 0.817 -41.623 1.00 68.67 C ANISOU 351 CZ PHE A 55 10634 7508 7949 686 26 -1293 C ATOM 352 N TYR A 56 -26.133 -3.593 -35.768 1.00 85.41 N ANISOU 352 N TYR A 56 12622 10331 9500 650 10 -1557 N ATOM 353 CA TYR A 56 -26.686 -4.182 -34.557 1.00 83.31 C ANISOU 353 CA TYR A 56 12364 10185 9103 713 60 -1593 C ATOM 354 C TYR A 56 -25.651 -4.889 -33.691 1.00 91.08 C ANISOU 354 C TYR A 56 13351 11250 10006 555 -47 -1626 C ATOM 355 O TYR A 56 -25.973 -5.264 -32.559 1.00106.35 O ANISOU 355 O TYR A 56 15325 13273 11810 596 -13 -1665 O ATOM 356 CB TYR A 56 -27.813 -5.167 -34.908 1.00 83.90 C ANISOU 356 CB TYR A 56 12240 10431 9208 827 145 -1481 C ATOM 357 CG TYR A 56 -29.126 -4.503 -35.270 1.00 88.62 C ANISOU 357 CG TYR A 56 12843 11000 9828 1027 277 -1456 C ATOM 358 CD1 TYR A 56 -29.348 -3.161 -34.991 1.00102.22 C ANISOU 358 CD1 TYR A 56 14769 12552 11517 1127 338 -1542 C ATOM 359 CD2 TYR A 56 -30.147 -5.221 -35.881 1.00 92.10 C ANISOU 359 CD2 TYR A 56 13086 11586 10323 1117 340 -1342 C ATOM 360 CE1 TYR A 56 -30.546 -2.550 -35.315 1.00112.45 C ANISOU 360 CE1 TYR A 56 16063 13825 12836 1331 466 -1504 C ATOM 361 CE2 TYR A 56 -31.349 -4.619 -36.209 1.00 98.10 C ANISOU 361 CE2 TYR A 56 13829 12343 11103 1305 456 -1303 C ATOM 362 CZ TYR A 56 -31.543 -3.283 -35.924 1.00111.41 C ANISOU 362 CZ TYR A 56 15711 13861 12757 1421 523 -1378 C ATOM 363 OH TYR A 56 -32.737 -2.678 -36.247 1.00117.68 O ANISOU 363 OH TYR A 56 16484 14657 13574 1629 646 -1324 O ATOM 364 N MET A 57 -24.424 -5.078 -34.184 1.00 88.79 N ANISOU 364 N MET A 57 13012 10941 9784 385 -170 -1600 N ATOM 365 CA MET A 57 -23.356 -5.679 -33.398 1.00 84.91 C ANISOU 365 CA MET A 57 12513 10529 9219 236 -281 -1618 C ATOM 366 C MET A 57 -22.097 -4.830 -33.317 1.00 95.75 C ANISOU 366 C MET A 57 14008 11779 10595 71 -401 -1691 C ATOM 367 O MET A 57 -21.303 -5.032 -32.392 1.00117.01 O ANISOU 367 O MET A 57 16744 14528 13188 -41 -493 -1737 O ATOM 368 CB MET A 57 -22.985 -7.062 -33.956 1.00 88.85 C ANISOU 368 CB MET A 57 12789 11176 9794 177 -320 -1489 C ATOM 369 CG MET A 57 -24.058 -8.115 -33.749 1.00 95.28 C ANISOU 369 CG MET A 57 13484 12133 10584 293 -224 -1421 C ATOM 370 SD MET A 57 -23.492 -9.776 -34.158 1.00 98.25 S ANISOU 370 SD MET A 57 13644 12657 11028 208 -273 -1291 S ATOM 371 CE MET A 57 -24.893 -10.745 -33.613 1.00 89.42 C ANISOU 371 CE MET A 57 12442 11675 9857 339 -149 -1239 C ATOM 372 N LYS A 58 -21.880 -3.912 -34.260 1.00 83.10 N ANISOU 372 N LYS A 58 12452 10020 9101 47 -407 -1694 N ATOM 373 CA LYS A 58 -20.816 -2.911 -34.172 1.00 84.21 C ANISOU 373 CA LYS A 58 12734 10014 9250 -110 -506 -1771 C ATOM 374 C LYS A 58 -19.424 -3.536 -34.213 1.00 96.32 C ANISOU 374 C LYS A 58 14147 11641 10808 -305 -650 -1716 C ATOM 375 O LYS A 58 -18.456 -2.933 -33.743 1.00108.74 O ANISOU 375 O LYS A 58 15822 13151 12345 -464 -756 -1786 O ATOM 376 CB LYS A 58 -20.974 -2.043 -32.919 1.00 64.79 C ANISOU 376 CB LYS A 58 10519 7458 6639 -104 -500 -1933 C ATOM 377 N LEU A 59 -19.320 -4.746 -34.769 1.00 86.50 N ANISOU 377 N LEU A 59 12689 10550 9628 -295 -651 -1589 N ATOM 378 CA LEU A 59 -18.041 -5.416 -34.990 1.00 84.81 C ANISOU 378 CA LEU A 59 12334 10430 9459 -448 -765 -1508 C ATOM 379 C LEU A 59 -17.231 -5.556 -33.705 1.00 86.36 C ANISOU 379 C LEU A 59 12583 10707 9525 -568 -874 -1565 C ATOM 380 O LEU A 59 -16.400 -4.697 -33.395 1.00 86.89 O ANISOU 380 O LEU A 59 12756 10691 9569 -713 -972 -1635 O ATOM 381 CB LEU A 59 -17.217 -4.662 -36.039 1.00 78.81 C ANISOU 381 CB LEU A 59 11564 9550 8828 -558 -815 -1474 C ATOM 382 CG LEU A 59 -17.718 -4.688 -37.483 1.00 70.11 C ANISOU 382 CG LEU A 59 10370 8406 7862 -468 -732 -1384 C ATOM 383 CD1 LEU A 59 -16.882 -3.761 -38.347 1.00 72.22 C ANISOU 383 CD1 LEU A 59 10663 8541 8236 -582 -780 -1359 C ATOM 384 CD2 LEU A 59 -17.677 -6.103 -38.025 1.00 68.19 C ANISOU 384 CD2 LEU A 59 9917 8329 7665 -433 -716 -1265 C ATOM 385 N LYS A 60 -17.453 -6.637 -32.958 1.00 90.95 N ANISOU 385 N LYS A 60 13087 11451 10017 -517 -864 -1529 N ATOM 386 CA LYS A 60 -16.757 -6.850 -31.698 1.00 90.14 C ANISOU 386 CA LYS A 60 13026 11452 9771 -613 -966 -1569 C ATOM 387 C LYS A 60 -15.772 -8.010 -31.729 1.00 98.42 C ANISOU 387 C LYS A 60 13878 12669 10848 -690 -1047 -1436 C ATOM 388 O LYS A 60 -15.020 -8.183 -30.763 1.00105.39 O ANISOU 388 O LYS A 60 14770 13654 11619 -786 -1152 -1447 O ATOM 389 CB LYS A 60 -17.769 -7.079 -30.565 1.00 72.53 C ANISOU 389 CB LYS A 60 10894 9283 7382 -488 -889 -1635 C ATOM 390 CG LYS A 60 -18.719 -5.915 -30.335 1.00 60.97 C ANISOU 390 CG LYS A 60 9641 7661 5864 -395 -801 -1773 C ATOM 391 CD LYS A 60 -19.726 -6.236 -29.244 1.00 73.72 C ANISOU 391 CD LYS A 60 11332 9360 7320 -256 -709 -1820 C ATOM 392 CE LYS A 60 -20.687 -5.080 -29.019 1.00 93.28 C ANISOU 392 CE LYS A 60 14019 11680 9744 -141 -605 -1952 C ATOM 393 NZ LYS A 60 -19.978 -3.844 -28.585 1.00101.63 N ANISOU 393 NZ LYS A 60 15292 12588 10735 -269 -695 -2100 N ATOM 394 N THR A 61 -15.750 -8.803 -32.797 1.00 91.81 N ANISOU 394 N THR A 61 12869 11865 10149 -647 -1000 -1311 N ATOM 395 CA THR A 61 -14.878 -9.964 -32.892 1.00 85.82 C ANISOU 395 CA THR A 61 11927 11252 9428 -690 -1052 -1178 C ATOM 396 C THR A 61 -14.146 -9.954 -34.228 1.00 80.62 C ANISOU 396 C THR A 61 11146 10551 8934 -747 -1067 -1090 C ATOM 397 O THR A 61 -14.437 -9.153 -35.121 1.00 91.29 O ANISOU 397 O THR A 61 12545 11769 10370 -740 -1028 -1123 O ATOM 398 CB THR A 61 -15.665 -11.274 -32.732 1.00 88.90 C ANISOU 398 CB THR A 61 12226 11747 9804 -556 -954 -1101 C ATOM 399 OG1 THR A 61 -16.772 -11.283 -33.642 1.00 86.91 O ANISOU 399 OG1 THR A 61 11969 11415 9639 -441 -832 -1103 O ATOM 400 CG2 THR A 61 -16.180 -11.419 -31.308 1.00101.34 C ANISOU 400 CG2 THR A 61 13899 13400 11205 -511 -947 -1158 C ATOM 401 N VAL A 62 -13.180 -10.866 -34.354 1.00 75.48 N ANISOU 401 N VAL A 62 10334 10021 8323 -793 -1118 -969 N ATOM 402 CA VAL A 62 -12.417 -10.980 -35.593 1.00 71.07 C ANISOU 402 CA VAL A 62 9647 9445 7911 -836 -1122 -873 C ATOM 403 C VAL A 62 -13.273 -11.597 -36.693 1.00 80.48 C ANISOU 403 C VAL A 62 10781 10599 9198 -705 -992 -828 C ATOM 404 O VAL A 62 -13.210 -11.179 -37.856 1.00 94.98 O ANISOU 404 O VAL A 62 12594 12355 11139 -710 -962 -809 O ATOM 405 CB VAL A 62 -11.130 -11.790 -35.351 1.00 61.19 C ANISOU 405 CB VAL A 62 8238 8343 6668 -906 -1205 -749 C ATOM 406 CG1 VAL A 62 -10.398 -12.043 -36.660 1.00 69.60 C ANISOU 406 CG1 VAL A 62 9161 9403 7882 -921 -1183 -638 C ATOM 407 CG2 VAL A 62 -10.227 -11.065 -34.366 1.00 73.13 C ANISOU 407 CG2 VAL A 62 9797 9903 8087 -1061 -1353 -793 C ATOM 408 N ALA A 63 -14.091 -12.593 -36.344 1.00 78.97 N ANISOU 408 N ALA A 63 10567 10470 8968 -594 -917 -809 N ATOM 409 CA ALA A 63 -14.931 -13.247 -37.343 1.00 87.13 C ANISOU 409 CA ALA A 63 11545 11478 10083 -488 -804 -772 C ATOM 410 C ALA A 63 -15.978 -12.298 -37.912 1.00 82.06 C ANISOU 410 C ALA A 63 11001 10717 9460 -436 -744 -856 C ATOM 411 O ALA A 63 -16.415 -12.476 -39.055 1.00 83.88 O ANISOU 411 O ALA A 63 11182 10913 9776 -384 -679 -826 O ATOM 412 CB ALA A 63 -15.605 -14.479 -36.738 1.00 98.47 C ANISOU 412 CB ALA A 63 12944 12999 11472 -400 -740 -736 C ATOM 413 N SER A 64 -16.392 -11.292 -37.139 1.00 72.70 N ANISOU 413 N SER A 64 9958 9472 8192 -442 -763 -960 N ATOM 414 CA SER A 64 -17.367 -10.331 -37.644 1.00 76.54 C ANISOU 414 CA SER A 64 10542 9842 8699 -376 -700 -1030 C ATOM 415 C SER A 64 -16.765 -9.433 -38.716 1.00 72.19 C ANISOU 415 C SER A 64 9996 9185 8246 -441 -729 -1017 C ATOM 416 O SER A 64 -17.474 -9.007 -39.635 1.00 66.90 O ANISOU 416 O SER A 64 9341 8443 7635 -371 -663 -1016 O ATOM 417 CB SER A 64 -17.922 -9.491 -36.495 1.00 77.63 C ANISOU 417 CB SER A 64 10846 9931 8718 -354 -700 -1146 C ATOM 418 OG SER A 64 -16.895 -8.743 -35.866 1.00 92.08 O ANISOU 418 OG SER A 64 12759 11727 10500 -485 -809 -1199 O ATOM 419 N VAL A 65 -15.468 -9.134 -38.619 1.00 69.06 N ANISOU 419 N VAL A 65 9582 8790 7868 -576 -827 -995 N ATOM 420 CA VAL A 65 -14.816 -8.318 -39.639 1.00 71.54 C ANISOU 420 CA VAL A 65 9889 9010 8281 -651 -851 -965 C ATOM 421 C VAL A 65 -14.728 -9.081 -40.954 1.00 86.55 C ANISOU 421 C VAL A 65 11645 10957 10283 -603 -795 -857 C ATOM 422 O VAL A 65 -14.957 -8.518 -42.031 1.00 95.07 O ANISOU 422 O VAL A 65 12733 11956 11434 -578 -753 -837 O ATOM 423 CB VAL A 65 -13.427 -7.866 -39.152 1.00 78.20 C ANISOU 423 CB VAL A 65 10730 9863 9119 -822 -974 -959 C ATOM 424 CG1 VAL A 65 -12.776 -6.949 -40.177 1.00 69.64 C ANISOU 424 CG1 VAL A 65 9643 8675 8142 -909 -993 -922 C ATOM 425 CG2 VAL A 65 -13.537 -7.177 -37.804 1.00 83.07 C ANISOU 425 CG2 VAL A 65 11505 10443 9614 -876 -1035 -1082 C ATOM 426 N PHE A 66 -14.397 -10.373 -40.889 1.00 90.44 N ANISOU 426 N PHE A 66 12013 11575 10777 -585 -790 -785 N ATOM 427 CA PHE A 66 -14.337 -11.183 -42.101 1.00 82.76 C ANISOU 427 CA PHE A 66 10920 10641 9886 -535 -729 -697 C ATOM 428 C PHE A 66 -15.722 -11.373 -42.706 1.00 74.50 C ANISOU 428 C PHE A 66 9896 9567 8842 -414 -635 -725 C ATOM 429 O PHE A 66 -15.887 -11.294 -43.929 1.00 83.37 O ANISOU 429 O PHE A 66 10984 10664 10027 -383 -591 -689 O ATOM 430 CB PHE A 66 -13.697 -12.537 -41.797 1.00 77.69 C ANISOU 430 CB PHE A 66 10159 10120 9241 -533 -735 -619 C ATOM 431 CG PHE A 66 -12.266 -12.446 -41.354 1.00 79.86 C ANISOU 431 CG PHE A 66 10372 10451 9521 -646 -829 -561 C ATOM 432 CD1 PHE A 66 -11.447 -11.426 -41.811 1.00 83.58 C ANISOU 432 CD1 PHE A 66 10845 10868 10043 -749 -884 -547 C ATOM 433 CD2 PHE A 66 -11.738 -13.382 -40.479 1.00 78.57 C ANISOU 433 CD2 PHE A 66 10140 10400 9314 -650 -863 -511 C ATOM 434 CE1 PHE A 66 -10.129 -11.342 -41.404 1.00 89.36 C ANISOU 434 CE1 PHE A 66 11501 11669 10783 -865 -977 -486 C ATOM 435 CE2 PHE A 66 -10.421 -13.303 -40.069 1.00 82.41 C ANISOU 435 CE2 PHE A 66 10549 10960 9802 -752 -957 -445 C ATOM 436 CZ PHE A 66 -9.615 -12.281 -40.532 1.00 87.75 C ANISOU 436 CZ PHE A 66 11217 11593 10530 -865 -1017 -434 C ATOM 437 N LEU A 67 -16.730 -11.620 -41.866 1.00 69.42 N ANISOU 437 N LEU A 67 9305 8944 8127 -347 -603 -783 N ATOM 438 CA LEU A 67 -18.079 -11.833 -42.377 1.00 72.71 C ANISOU 438 CA LEU A 67 9723 9357 8546 -239 -519 -800 C ATOM 439 C LEU A 67 -18.670 -10.553 -42.954 1.00 67.72 C ANISOU 439 C LEU A 67 9174 8622 7932 -202 -498 -838 C ATOM 440 O LEU A 67 -19.507 -10.614 -43.862 1.00 82.64 O ANISOU 440 O LEU A 67 11033 10515 9851 -128 -440 -820 O ATOM 441 CB LEU A 67 -18.978 -12.388 -41.272 1.00 68.76 C ANISOU 441 CB LEU A 67 9248 8913 7965 -180 -486 -839 C ATOM 442 CG LEU A 67 -20.294 -13.021 -41.730 1.00 60.70 C ANISOU 442 CG LEU A 67 8180 7932 6952 -86 -402 -832 C ATOM 443 CD1 LEU A 67 -20.024 -14.143 -42.719 1.00 65.05 C ANISOU 443 CD1 LEU A 67 8619 8529 7568 -98 -381 -763 C ATOM 444 CD2 LEU A 67 -21.089 -13.535 -40.541 1.00 51.41 C ANISOU 444 CD2 LEU A 67 7022 6815 5696 -38 -366 -857 C ATOM 445 N LEU A 68 -18.253 -9.392 -42.445 1.00 55.41 N ANISOU 445 N LEU A 68 7725 6971 6356 -255 -544 -889 N ATOM 446 CA LEU A 68 -18.709 -8.129 -43.018 1.00 58.56 C ANISOU 446 CA LEU A 68 8216 7250 6784 -218 -518 -914 C ATOM 447 C LEU A 68 -18.124 -7.919 -44.408 1.00 76.68 C ANISOU 447 C LEU A 68 10447 9518 9170 -251 -520 -835 C ATOM 448 O LEU A 68 -18.854 -7.631 -45.364 1.00 77.27 O ANISOU 448 O LEU A 68 10513 9570 9275 -170 -465 -807 O ATOM 449 CB LEU A 68 -18.336 -6.966 -42.099 1.00 52.98 C ANISOU 449 CB LEU A 68 7662 6431 6038 -280 -567 -996 C ATOM 450 CG LEU A 68 -18.625 -5.572 -42.663 1.00 57.97 C ANISOU 450 CG LEU A 68 8409 6904 6712 -254 -540 -1017 C ATOM 451 CD1 LEU A 68 -20.122 -5.356 -42.829 1.00 65.49 C ANISOU 451 CD1 LEU A 68 9398 7842 7643 -86 -443 -1036 C ATOM 452 CD2 LEU A 68 -18.015 -4.490 -41.785 1.00 57.78 C ANISOU 452 CD2 LEU A 68 8544 6753 6656 -354 -600 -1103 C ATOM 453 N ASN A 69 -16.803 -8.059 -44.539 1.00 73.75 N ANISOU 453 N ASN A 69 10022 9162 8838 -367 -581 -788 N ATOM 454 CA ASN A 69 -16.161 -7.906 -45.837 1.00 71.64 C ANISOU 454 CA ASN A 69 9687 8883 8651 -399 -574 -702 C ATOM 455 C ASN A 69 -16.534 -9.021 -46.804 1.00 82.93 C ANISOU 455 C ASN A 69 11001 10413 10096 -325 -516 -644 C ATOM 456 O ASN A 69 -16.422 -8.831 -48.020 1.00104.98 O ANISOU 456 O ASN A 69 13757 13196 12935 -310 -487 -584 O ATOM 457 CB ASN A 69 -14.643 -7.845 -45.667 1.00 69.13 C ANISOU 457 CB ASN A 69 9321 8577 8369 -540 -648 -655 C ATOM 458 CG ASN A 69 -14.180 -6.547 -45.033 1.00 80.58 C ANISOU 458 CG ASN A 69 10892 9906 9819 -643 -712 -707 C ATOM 459 OD1 ASN A 69 -13.462 -6.552 -44.034 1.00 85.83 O ANISOU 459 OD1 ASN A 69 11569 10594 10449 -744 -790 -738 O ATOM 460 ND2 ASN A 69 -14.594 -5.426 -45.612 1.00 86.00 N ANISOU 460 ND2 ASN A 69 11674 10461 10542 -621 -680 -717 N ATOM 461 N LEU A 70 -16.971 -10.176 -46.296 1.00 67.45 N ANISOU 461 N LEU A 70 8992 8544 8095 -284 -498 -661 N ATOM 462 CA LEU A 70 -17.433 -11.238 -47.182 1.00 60.36 C ANISOU 462 CA LEU A 70 8004 7723 7206 -223 -443 -624 C ATOM 463 C LEU A 70 -18.745 -10.864 -47.858 1.00 58.18 C ANISOU 463 C LEU A 70 7753 7434 6918 -130 -393 -642 C ATOM 464 O LEU A 70 -18.980 -11.249 -49.009 1.00 79.92 O ANISOU 464 O LEU A 70 10450 10227 9687 -98 -360 -604 O ATOM 465 CB LEU A 70 -17.587 -12.544 -46.401 1.00 70.59 C ANISOU 465 CB LEU A 70 9253 9101 8468 -212 -434 -636 C ATOM 466 CG LEU A 70 -17.729 -13.821 -47.230 1.00 78.02 C ANISOU 466 CG LEU A 70 10108 10109 9426 -180 -384 -599 C ATOM 467 CD1 LEU A 70 -16.459 -14.086 -48.023 1.00 83.10 C ANISOU 467 CD1 LEU A 70 10690 10764 10120 -223 -388 -528 C ATOM 468 CD2 LEU A 70 -18.067 -15.005 -46.339 1.00 87.33 C ANISOU 468 CD2 LEU A 70 11263 11344 10575 -166 -367 -612 C ATOM 469 N ALA A 71 -19.604 -10.115 -47.165 1.00 69.53 N ANISOU 469 N ALA A 71 9274 8823 8321 -81 -386 -698 N ATOM 470 CA ALA A 71 -20.853 -9.662 -47.764 1.00 80.63 C ANISOU 470 CA ALA A 71 10693 10226 9718 20 -338 -700 C ATOM 471 C ALA A 71 -20.656 -8.420 -48.623 1.00 81.18 C ANISOU 471 C ALA A 71 10814 10202 9827 31 -336 -663 C ATOM 472 O ALA A 71 -21.351 -8.256 -49.632 1.00 82.59 O ANISOU 472 O ALA A 71 10961 10407 10010 102 -303 -622 O ATOM 473 CB ALA A 71 -21.891 -9.386 -46.674 1.00 76.62 C ANISOU 473 CB ALA A 71 10247 9709 9157 91 -313 -763 C ATOM 474 N LEU A 72 -19.726 -7.540 -48.243 1.00 74.33 N ANISOU 474 N LEU A 72 10025 9231 8987 -44 -375 -670 N ATOM 475 CA LEU A 72 -19.450 -6.360 -49.056 1.00 67.24 C ANISOU 475 CA LEU A 72 9182 8228 8137 -47 -369 -624 C ATOM 476 C LEU A 72 -18.832 -6.744 -50.394 1.00 81.24 C ANISOU 476 C LEU A 72 10860 10059 9950 -74 -363 -533 C ATOM 477 O LEU A 72 -19.141 -6.134 -51.425 1.00 88.95 O ANISOU 477 O LEU A 72 11842 11010 10944 -21 -332 -474 O ATOM 478 CB LEU A 72 -18.532 -5.400 -48.301 1.00 68.60 C ANISOU 478 CB LEU A 72 9460 8272 8334 -149 -418 -657 C ATOM 479 CG LEU A 72 -19.103 -4.716 -47.058 1.00 70.34 C ANISOU 479 CG LEU A 72 9818 8402 8508 -119 -417 -756 C ATOM 480 CD1 LEU A 72 -18.075 -3.777 -46.447 1.00 47.61 C ANISOU 480 CD1 LEU A 72 7048 5391 5650 -250 -477 -793 C ATOM 481 CD2 LEU A 72 -20.382 -3.967 -47.398 1.00 80.64 C ANISOU 481 CD2 LEU A 72 11189 9647 9806 29 -345 -758 C ATOM 482 N ALA A 73 -17.955 -7.750 -50.398 1.00 79.32 N ANISOU 482 N ALA A 73 10530 9896 9713 -146 -386 -514 N ATOM 483 CA ALA A 73 -17.345 -8.192 -51.647 1.00 84.50 C ANISOU 483 CA ALA A 73 11101 10612 10395 -160 -366 -433 C ATOM 484 C ALA A 73 -18.378 -8.824 -52.572 1.00 79.60 C ANISOU 484 C ALA A 73 10430 10081 9734 -65 -321 -424 C ATOM 485 O ALA A 73 -18.296 -8.674 -53.797 1.00 83.14 O ANISOU 485 O ALA A 73 10850 10554 10186 -42 -296 -359 O ATOM 486 CB ALA A 73 -16.208 -9.172 -51.360 1.00 85.22 C ANISOU 486 CB ALA A 73 11112 10767 10499 -238 -389 -414 C ATOM 487 N ASP A 74 -19.356 -9.535 -52.005 1.00 68.63 N ANISOU 487 N ASP A 74 9028 8748 8302 -16 -313 -484 N ATOM 488 CA ASP A 74 -20.396 -10.141 -52.829 1.00 63.63 C ANISOU 488 CA ASP A 74 8340 8207 7627 54 -282 -481 C ATOM 489 C ASP A 74 -21.321 -9.092 -53.429 1.00 69.36 C ANISOU 489 C ASP A 74 9100 8912 8343 140 -265 -451 C ATOM 490 O ASP A 74 -21.821 -9.276 -54.544 1.00 90.20 O ANISOU 490 O ASP A 74 11692 11628 10953 183 -250 -412 O ATOM 491 CB ASP A 74 -21.199 -11.150 -52.008 1.00 57.12 C ANISOU 491 CB ASP A 74 7487 7447 6769 69 -277 -544 C ATOM 492 CG ASP A 74 -20.380 -12.363 -51.611 1.00 76.81 C ANISOU 492 CG ASP A 74 9939 9973 9271 3 -282 -556 C ATOM 493 OD1 ASP A 74 -19.174 -12.401 -51.933 1.00 85.73 O ANISOU 493 OD1 ASP A 74 11057 11085 10433 -48 -290 -516 O ATOM 494 OD2 ASP A 74 -20.944 -13.279 -50.978 1.00 81.23 O ANISOU 494 OD2 ASP A 74 10476 10580 9809 7 -272 -596 O ATOM 495 N LEU A 75 -21.558 -7.989 -52.714 1.00 65.04 N ANISOU 495 N LEU A 75 8638 8262 7812 169 -266 -466 N ATOM 496 CA LEU A 75 -22.429 -6.943 -53.240 1.00 70.77 C ANISOU 496 CA LEU A 75 9400 8953 8534 270 -239 -425 C ATOM 497 C LEU A 75 -21.791 -6.238 -54.432 1.00 79.29 C ANISOU 497 C LEU A 75 10490 9993 9643 261 -233 -334 C ATOM 498 O LEU A 75 -22.491 -5.843 -55.371 1.00 87.69 O ANISOU 498 O LEU A 75 11535 11098 10686 347 -211 -272 O ATOM 499 CB LEU A 75 -22.771 -5.939 -52.140 1.00 70.30 C ANISOU 499 CB LEU A 75 9453 8772 8487 311 -229 -471 C ATOM 500 CG LEU A 75 -23.708 -6.439 -51.039 1.00 70.03 C ANISOU 500 CG LEU A 75 9412 8787 8409 360 -215 -545 C ATOM 501 CD1 LEU A 75 -23.912 -5.368 -49.978 1.00 67.13 C ANISOU 501 CD1 LEU A 75 9178 8285 8043 403 -195 -597 C ATOM 502 CD2 LEU A 75 -25.041 -6.872 -51.628 1.00 70.48 C ANISOU 502 CD2 LEU A 75 9375 8975 8428 461 -186 -514 C ATOM 503 N CYS A 76 -20.466 -6.070 -54.412 1.00 77.40 N ANISOU 503 N CYS A 76 10271 9687 9450 159 -252 -315 N ATOM 504 CA CYS A 76 -19.788 -5.439 -55.541 1.00 82.81 C ANISOU 504 CA CYS A 76 10957 10341 10165 141 -238 -216 C ATOM 505 C CYS A 76 -19.881 -6.303 -56.792 1.00 80.76 C ANISOU 505 C CYS A 76 10601 10226 9856 167 -222 -169 C ATOM 506 O CYS A 76 -20.011 -5.781 -57.906 1.00 90.53 O ANISOU 506 O CYS A 76 11835 11482 11080 215 -198 -83 O ATOM 507 CB CYS A 76 -18.327 -5.159 -55.187 1.00 91.60 C ANISOU 507 CB CYS A 76 12093 11370 11342 13 -263 -200 C ATOM 508 SG CYS A 76 -18.095 -4.009 -53.813 1.00 97.64 S ANISOU 508 SG CYS A 76 12994 11951 12155 -44 -294 -263 S ATOM 509 N PHE A 77 -19.814 -7.626 -56.629 1.00 67.17 N ANISOU 509 N PHE A 77 8813 8606 8102 135 -231 -223 N ATOM 510 CA PHE A 77 -19.968 -8.521 -57.771 1.00 78.83 C ANISOU 510 CA PHE A 77 10219 10213 9520 155 -214 -202 C ATOM 511 C PHE A 77 -21.394 -8.496 -58.304 1.00 76.63 C ANISOU 511 C PHE A 77 9918 10020 9178 248 -213 -202 C ATOM 512 O PHE A 77 -21.611 -8.572 -59.520 1.00 75.22 O ANISOU 512 O PHE A 77 9707 9928 8944 282 -203 -150 O ATOM 513 CB PHE A 77 -19.562 -9.942 -57.376 1.00 85.72 C ANISOU 513 CB PHE A 77 11043 11146 10382 99 -217 -266 C ATOM 514 CG PHE A 77 -20.253 -11.016 -58.169 1.00 88.44 C ANISOU 514 CG PHE A 77 11337 11613 10652 126 -206 -296 C ATOM 515 CD1 PHE A 77 -19.829 -11.336 -59.447 1.00 88.29 C ANISOU 515 CD1 PHE A 77 11297 11660 10590 129 -180 -253 C ATOM 516 CD2 PHE A 77 -21.324 -11.711 -57.629 1.00 90.94 C ANISOU 516 CD2 PHE A 77 11633 11981 10939 141 -220 -367 C ATOM 517 CE1 PHE A 77 -20.464 -12.324 -60.176 1.00 91.20 C ANISOU 517 CE1 PHE A 77 11636 12137 10880 141 -175 -296 C ATOM 518 CE2 PHE A 77 -21.963 -12.700 -58.353 1.00 87.08 C ANISOU 518 CE2 PHE A 77 11103 11600 10385 142 -218 -401 C ATOM 519 CZ PHE A 77 -21.532 -13.007 -59.628 1.00 86.72 C ANISOU 519 CZ PHE A 77 11048 11611 10289 139 -199 -372 C ATOM 520 N LEU A 78 -22.381 -8.389 -57.412 1.00 77.43 N ANISOU 520 N LEU A 78 10030 10111 9277 291 -224 -253 N ATOM 521 CA LEU A 78 -23.776 -8.374 -57.835 1.00 81.74 C ANISOU 521 CA LEU A 78 10533 10757 9768 380 -225 -243 C ATOM 522 C LEU A 78 -24.142 -7.105 -58.593 1.00 90.88 C ANISOU 522 C LEU A 78 11718 11888 10922 472 -210 -144 C ATOM 523 O LEU A 78 -25.124 -7.111 -59.343 1.00 98.85 O ANISOU 523 O LEU A 78 12672 13014 11872 545 -217 -103 O ATOM 524 CB LEU A 78 -24.691 -8.539 -56.621 1.00 71.74 C ANISOU 524 CB LEU A 78 9264 9488 8506 410 -227 -310 C ATOM 525 CG LEU A 78 -24.617 -9.895 -55.916 1.00 71.37 C ANISOU 525 CG LEU A 78 9177 9490 8451 334 -238 -394 C ATOM 526 CD1 LEU A 78 -25.178 -9.793 -54.511 1.00 75.30 C ANISOU 526 CD1 LEU A 78 9699 9947 8965 358 -230 -448 C ATOM 527 CD2 LEU A 78 -25.353 -10.959 -56.714 1.00 69.83 C ANISOU 527 CD2 LEU A 78 8895 9444 8194 323 -251 -407 C ATOM 528 N LEU A 79 -23.382 -6.021 -58.417 1.00 83.82 N ANISOU 528 N LEU A 79 10909 10847 10093 465 -193 -99 N ATOM 529 CA LEU A 79 -23.667 -4.796 -59.157 1.00 88.74 C ANISOU 529 CA LEU A 79 11570 11424 10722 555 -169 8 C ATOM 530 C LEU A 79 -23.377 -4.959 -60.643 1.00 93.25 C ANISOU 530 C LEU A 79 12092 12099 11240 557 -166 96 C ATOM 531 O LEU A 79 -24.080 -4.379 -61.478 1.00 99.64 O ANISOU 531 O LEU A 79 12886 12964 12008 656 -156 186 O ATOM 532 CB LEU A 79 -22.860 -3.632 -58.584 1.00 89.52 C ANISOU 532 CB LEU A 79 11785 11320 10910 525 -149 29 C ATOM 533 CG LEU A 79 -23.187 -3.222 -57.147 1.00 91.21 C ANISOU 533 CG LEU A 79 12079 11414 11163 537 -146 -57 C ATOM 534 CD1 LEU A 79 -22.339 -2.035 -56.720 1.00 95.33 C ANISOU 534 CD1 LEU A 79 12728 11726 11765 488 -134 -41 C ATOM 535 CD2 LEU A 79 -24.669 -2.909 -57.000 1.00 84.18 C ANISOU 535 CD2 LEU A 79 11177 10568 10239 686 -122 -49 C ATOM 536 N THR A 80 -22.355 -5.739 -60.990 1.00 95.25 N ANISOU 536 N THR A 80 12320 12386 11484 461 -169 78 N ATOM 537 CA THR A 80 -22.041 -6.034 -62.380 1.00 95.42 C ANISOU 537 CA THR A 80 12300 12518 11437 463 -158 147 C ATOM 538 C THR A 80 -22.858 -7.190 -62.939 1.00 79.93 C ANISOU 538 C THR A 80 10263 10739 9370 476 -185 93 C ATOM 539 O THR A 80 -22.774 -7.464 -64.142 1.00 84.77 O ANISOU 539 O THR A 80 10848 11462 9899 486 -180 139 O ATOM 540 CB THR A 80 -20.549 -6.353 -62.530 1.00103.94 C ANISOU 540 CB THR A 80 13385 13555 12552 365 -136 158 C ATOM 541 OG1 THR A 80 -20.231 -7.539 -61.789 1.00101.52 O ANISOU 541 OG1 THR A 80 13050 13270 12253 293 -151 48 O ATOM 542 CG2 THR A 80 -19.706 -5.199 -62.008 1.00105.27 C ANISOU 542 CG2 THR A 80 13622 13550 12827 326 -120 214 C ATOM 543 N LEU A 81 -23.644 -7.866 -62.100 1.00 75.38 N ANISOU 543 N LEU A 81 9656 10196 8791 468 -212 -2 N ATOM 544 CA LEU A 81 -24.414 -9.015 -62.566 1.00 79.12 C ANISOU 544 CA LEU A 81 10059 10830 9173 453 -243 -62 C ATOM 545 C LEU A 81 -25.483 -8.658 -63.597 1.00 83.78 C ANISOU 545 C LEU A 81 10599 11562 9671 536 -268 9 C ATOM 546 O LEU A 81 -25.640 -9.425 -64.564 1.00 85.22 O ANISOU 546 O LEU A 81 10744 11882 9754 507 -291 -8 O ATOM 547 CB LEU A 81 -25.029 -9.738 -61.360 1.00 80.41 C ANISOU 547 CB LEU A 81 10198 10988 9366 421 -261 -164 C ATOM 548 CG LEU A 81 -25.542 -11.160 -61.595 1.00 70.09 C ANISOU 548 CG LEU A 81 8833 9806 7992 359 -288 -249 C ATOM 549 CD1 LEU A 81 -24.425 -12.049 -62.118 1.00 68.66 C ANISOU 549 CD1 LEU A 81 8680 9617 7792 283 -266 -286 C ATOM 550 CD2 LEU A 81 -26.119 -11.721 -60.310 1.00 61.31 C ANISOU 550 CD2 LEU A 81 7699 8673 6924 332 -295 -327 C ATOM 551 N PRO A 82 -26.241 -7.559 -63.472 1.00 78.02 N ANISOU 551 N PRO A 82 9868 10815 8962 640 -267 89 N ATOM 552 CA PRO A 82 -27.196 -7.229 -64.545 1.00 82.31 C ANISOU 552 CA PRO A 82 10350 11516 9410 727 -294 179 C ATOM 553 C PRO A 82 -26.537 -6.981 -65.890 1.00 91.40 C ANISOU 553 C PRO A 82 11521 12716 10490 733 -283 266 C ATOM 554 O PRO A 82 -27.186 -7.160 -66.928 1.00 94.59 O ANISOU 554 O PRO A 82 11868 13296 10778 766 -320 310 O ATOM 555 CB PRO A 82 -27.895 -5.967 -64.019 1.00 65.88 C ANISOU 555 CB PRO A 82 8283 9358 7389 854 -271 262 C ATOM 556 CG PRO A 82 -27.774 -6.057 -62.550 1.00 60.77 C ANISOU 556 CG PRO A 82 7679 8575 6838 821 -251 168 C ATOM 557 CD PRO A 82 -26.429 -6.680 -62.303 1.00 66.83 C ANISOU 557 CD PRO A 82 8500 9252 7642 693 -242 93 C ATOM 558 N LEU A 83 -25.269 -6.566 -65.904 1.00 85.26 N ANISOU 558 N LEU A 83 10818 11801 9774 698 -234 297 N ATOM 559 CA LEU A 83 -24.568 -6.378 -67.171 1.00 68.06 C ANISOU 559 CA LEU A 83 8657 9676 7528 702 -211 386 C ATOM 560 C LEU A 83 -24.361 -7.706 -67.889 1.00 75.09 C ANISOU 560 C LEU A 83 9518 10708 8307 628 -229 302 C ATOM 561 O LEU A 83 -24.565 -7.799 -69.105 1.00 75.65 O ANISOU 561 O LEU A 83 9569 10924 8250 658 -241 354 O ATOM 562 CB LEU A 83 -23.229 -5.680 -66.933 1.00 60.30 C ANISOU 562 CB LEU A 83 7746 8514 6649 667 -151 441 C ATOM 563 CG LEU A 83 -23.204 -4.153 -67.042 1.00 62.27 C ANISOU 563 CG LEU A 83 8049 8647 6964 749 -117 584 C ATOM 564 CD1 LEU A 83 -24.164 -3.506 -66.055 1.00 51.69 C ANISOU 564 CD1 LEU A 83 6726 7223 5692 821 -129 570 C ATOM 565 CD2 LEU A 83 -21.789 -3.629 -66.839 1.00 67.68 C ANISOU 565 CD2 LEU A 83 8798 9168 7751 674 -66 627 C ATOM 566 N TRP A 84 -23.959 -8.746 -67.155 1.00 79.78 N ANISOU 566 N TRP A 84 10116 11258 8939 536 -228 172 N ATOM 567 CA TRP A 84 -23.771 -10.056 -67.766 1.00 76.36 C ANISOU 567 CA TRP A 84 9675 10931 8408 469 -235 79 C ATOM 568 C TRP A 84 -25.093 -10.728 -68.113 1.00 71.83 C ANISOU 568 C TRP A 84 9042 10523 7726 462 -306 18 C ATOM 569 O TRP A 84 -25.123 -11.587 -69.001 1.00 59.18 O ANISOU 569 O TRP A 84 7443 9038 6003 420 -321 -37 O ATOM 570 CB TRP A 84 -22.959 -10.962 -66.838 1.00 80.06 C ANISOU 570 CB TRP A 84 10168 11293 8959 383 -207 -28 C ATOM 571 CG TRP A 84 -21.622 -10.401 -66.468 1.00 74.29 C ANISOU 571 CG TRP A 84 9475 10419 8331 370 -149 30 C ATOM 572 CD1 TRP A 84 -21.258 -9.883 -65.260 1.00 60.72 C ANISOU 572 CD1 TRP A 84 7772 8556 6742 351 -145 30 C ATOM 573 CD2 TRP A 84 -20.472 -10.292 -67.314 1.00 76.54 C ANISOU 573 CD2 TRP A 84 9782 10705 8593 368 -90 100 C ATOM 574 NE1 TRP A 84 -19.951 -9.463 -65.299 1.00 66.15 N ANISOU 574 NE1 TRP A 84 8484 9156 7493 324 -97 96 N ATOM 575 CE2 TRP A 84 -19.445 -9.702 -66.550 1.00 72.27 C ANISOU 575 CE2 TRP A 84 9257 10020 8183 338 -57 146 C ATOM 576 CE3 TRP A 84 -20.209 -10.638 -68.643 1.00 79.25 C ANISOU 576 CE3 TRP A 84 10134 11166 8812 388 -60 128 C ATOM 577 CZ2 TRP A 84 -18.177 -9.451 -67.070 1.00 77.46 C ANISOU 577 CZ2 TRP A 84 9920 10651 8860 323 5 231 C ATOM 578 CZ3 TRP A 84 -18.950 -10.387 -69.158 1.00 87.84 C ANISOU 578 CZ3 TRP A 84 11237 12224 9915 388 14 211 C ATOM 579 CH2 TRP A 84 -17.950 -9.800 -68.373 1.00 88.38 C ANISOU 579 CH2 TRP A 84 11303 12151 10125 354 46 267 C ATOM 580 N ALA A 85 -26.181 -10.360 -67.433 1.00 77.58 N ANISOU 580 N ALA A 85 9717 11266 8492 500 -348 25 N ATOM 581 CA ALA A 85 -27.477 -10.965 -67.720 1.00 70.81 C ANISOU 581 CA ALA A 85 8781 10581 7541 484 -421 -20 C ATOM 582 C ALA A 85 -27.977 -10.565 -69.102 1.00 76.24 C ANISOU 582 C ALA A 85 9435 11447 8086 542 -460 73 C ATOM 583 O ALA A 85 -28.300 -11.424 -69.930 1.00 67.38 O ANISOU 583 O ALA A 85 8295 10476 6832 480 -508 11 O ATOM 584 CB ALA A 85 -28.488 -10.573 -66.643 1.00 74.29 C ANISOU 584 CB ALA A 85 9161 11004 8063 528 -442 -11 C ATOM 585 N VAL A 86 -28.050 -9.258 -69.370 1.00 90.55 N ANISOU 585 N VAL A 86 11245 13242 9916 659 -441 223 N ATOM 586 CA VAL A 86 -28.474 -8.793 -70.685 1.00 91.34 C ANISOU 586 CA VAL A 86 11313 13514 9877 729 -475 336 C ATOM 587 C VAL A 86 -27.428 -9.094 -71.748 1.00 77.80 C ANISOU 587 C VAL A 86 9669 11825 8068 694 -439 339 C ATOM 588 O VAL A 86 -27.761 -9.178 -72.936 1.00 83.89 O ANISOU 588 O VAL A 86 10420 12777 8677 712 -478 382 O ATOM 589 CB VAL A 86 -28.795 -7.287 -70.648 1.00 95.80 C ANISOU 589 CB VAL A 86 11868 14032 10500 876 -449 510 C ATOM 590 CG1 VAL A 86 -29.945 -7.014 -69.691 1.00 98.59 C ANISOU 590 CG1 VAL A 86 12146 14388 10925 933 -477 512 C ATOM 591 CG2 VAL A 86 -27.564 -6.492 -70.246 1.00 86.97 C ANISOU 591 CG2 VAL A 86 10851 12685 9508 893 -359 562 C ATOM 592 N TYR A 87 -26.164 -9.257 -71.352 1.00 73.99 N ANISOU 592 N TYR A 87 9264 11175 7673 647 -363 299 N ATOM 593 CA TYR A 87 -25.129 -9.640 -72.306 1.00 57.81 C ANISOU 593 CA TYR A 87 7276 9153 5538 618 -314 298 C ATOM 594 C TYR A 87 -25.368 -11.049 -72.832 1.00 70.77 C ANISOU 594 C TYR A 87 8923 10922 7043 529 -353 149 C ATOM 595 O TYR A 87 -25.316 -11.289 -74.044 1.00 75.38 O ANISOU 595 O TYR A 87 9530 11650 7463 535 -360 161 O ATOM 596 CB TYR A 87 -23.752 -9.528 -71.650 1.00 71.25 C ANISOU 596 CB TYR A 87 9036 10656 7379 586 -226 295 C ATOM 597 CG TYR A 87 -22.645 -10.199 -72.425 1.00 73.32 C ANISOU 597 CG TYR A 87 9351 10940 7568 549 -163 267 C ATOM 598 CD1 TYR A 87 -22.305 -9.765 -73.696 1.00 82.95 C ANISOU 598 CD1 TYR A 87 10590 12260 8667 604 -129 376 C ATOM 599 CD2 TYR A 87 -21.932 -11.259 -71.880 1.00 77.56 C ANISOU 599 CD2 TYR A 87 9917 11399 8155 472 -126 141 C ATOM 600 CE1 TYR A 87 -21.295 -10.371 -74.408 1.00 80.89 C ANISOU 600 CE1 TYR A 87 10377 12025 8331 584 -57 354 C ATOM 601 CE2 TYR A 87 -20.915 -11.871 -72.585 1.00 77.71 C ANISOU 601 CE2 TYR A 87 9983 11436 8107 457 -54 122 C ATOM 602 CZ TYR A 87 -20.602 -11.422 -73.850 1.00 79.92 C ANISOU 602 CZ TYR A 87 10283 11820 8264 515 -16 226 C ATOM 603 OH TYR A 87 -19.592 -12.023 -74.564 1.00 81.38 O ANISOU 603 OH TYR A 87 10515 12031 8376 514 70 210 O ATOM 604 N THR A 88 -25.634 -11.997 -71.931 1.00 81.56 N ANISOU 604 N THR A 88 10280 12236 8472 443 -376 6 N ATOM 605 CA THR A 88 -25.955 -13.355 -72.357 1.00 71.75 C ANISOU 605 CA THR A 88 9055 11093 7112 346 -414 -144 C ATOM 606 C THR A 88 -27.326 -13.421 -73.020 1.00 74.37 C ANISOU 606 C THR A 88 9315 11639 7305 338 -523 -141 C ATOM 607 O THR A 88 -27.562 -14.286 -73.871 1.00 75.39 O ANISOU 607 O THR A 88 9470 11896 7278 269 -563 -233 O ATOM 608 CB THR A 88 -25.891 -14.306 -71.160 1.00 67.03 C ANISOU 608 CB THR A 88 8467 10369 6634 258 -404 -279 C ATOM 609 OG1 THR A 88 -24.667 -14.094 -70.445 1.00 68.62 O ANISOU 609 OG1 THR A 88 8714 10386 6972 275 -316 -257 O ATOM 610 CG2 THR A 88 -25.951 -15.757 -71.618 1.00 66.94 C ANISOU 610 CG2 THR A 88 8506 10409 6517 153 -418 -437 C ATOM 611 N ALA A 89 -28.233 -12.511 -72.656 1.00 72.47 N ANISOU 611 N ALA A 89 8982 11444 7111 410 -570 -36 N ATOM 612 CA ALA A 89 -29.571 -12.523 -73.239 1.00 70.08 C ANISOU 612 CA ALA A 89 8581 11364 6681 409 -679 -12 C ATOM 613 C ALA A 89 -29.540 -12.138 -74.712 1.00 90.63 C ANISOU 613 C ALA A 89 11198 14141 9098 462 -703 78 C ATOM 614 O ALA A 89 -30.303 -12.684 -75.518 1.00101.53 O ANISOU 614 O ALA A 89 12539 15727 10310 405 -795 33 O ATOM 615 CB ALA A 89 -30.493 -11.587 -72.459 1.00 76.91 C ANISOU 615 CB ALA A 89 9342 12230 7651 500 -705 97 C ATOM 616 N MET A 90 -28.666 -11.201 -75.086 1.00 89.62 N ANISOU 616 N MET A 90 11123 13939 8990 563 -623 207 N ATOM 617 CA MET A 90 -28.534 -10.767 -76.471 1.00 82.22 C ANISOU 617 CA MET A 90 10205 13158 7876 626 -630 313 C ATOM 618 C MET A 90 -27.564 -11.630 -77.268 1.00 82.27 C ANISOU 618 C MET A 90 10322 13175 7763 560 -579 212 C ATOM 619 O MET A 90 -26.938 -11.136 -78.216 1.00 89.03 O ANISOU 619 O MET A 90 11225 14080 8521 627 -528 315 O ATOM 620 CB MET A 90 -28.108 -9.299 -76.526 1.00 74.45 C ANISOU 620 CB MET A 90 9224 12089 6973 768 -561 520 C ATOM 621 CG MET A 90 -29.118 -8.340 -75.919 1.00 82.22 C ANISOU 621 CG MET A 90 10114 13076 8052 865 -601 639 C ATOM 622 SD MET A 90 -28.717 -6.613 -76.247 1.00 93.58 S ANISOU 622 SD MET A 90 11577 14428 9552 1037 -523 892 S ATOM 623 CE MET A 90 -27.057 -6.520 -75.583 1.00 90.52 C ANISOU 623 CE MET A 90 11309 13752 9335 985 -395 852 C ATOM 624 N GLU A 91 -27.424 -12.907 -76.904 1.00 76.78 N ANISOU 624 N GLU A 91 9672 12429 7071 436 -582 19 N ATOM 625 CA GLU A 91 -26.569 -13.855 -77.620 1.00 70.98 C ANISOU 625 CA GLU A 91 9054 11696 6220 379 -526 -97 C ATOM 626 C GLU A 91 -25.118 -13.372 -77.655 1.00 72.07 C ANISOU 626 C GLU A 91 9261 11686 6437 451 -387 -13 C ATOM 627 O GLU A 91 -24.480 -13.318 -78.708 1.00 81.85 O ANISOU 627 O GLU A 91 10563 12999 7539 492 -332 29 O ATOM 628 CB GLU A 91 -27.103 -14.115 -79.031 1.00 69.02 C ANISOU 628 CB GLU A 91 8822 11695 5707 365 -599 -110 C ATOM 629 CG GLU A 91 -28.571 -14.508 -79.065 1.00 85.26 C ANISOU 629 CG GLU A 91 10788 13929 7680 284 -751 -173 C ATOM 630 CD GLU A 91 -29.053 -14.860 -80.457 1.00105.18 C ANISOU 630 CD GLU A 91 13334 16704 9924 249 -835 -205 C ATOM 631 OE1 GLU A 91 -28.240 -14.797 -81.403 1.00117.56 O ANISOU 631 OE1 GLU A 91 15001 18308 11359 298 -765 -181 O ATOM 632 OE2 GLU A 91 -30.245 -15.200 -80.604 1.00114.07 O ANISOU 632 OE2 GLU A 91 14378 18005 10960 168 -972 -253 O ATOM 633 N TYR A 92 -24.602 -13.019 -76.475 1.00 63.36 N ANISOU 633 N TYR A 92 8141 10381 5552 462 -332 14 N ATOM 634 CA TYR A 92 -23.229 -12.546 -76.290 1.00 67.46 C ANISOU 634 CA TYR A 92 8703 10748 6181 508 -211 96 C ATOM 635 C TYR A 92 -22.949 -11.315 -77.159 1.00 66.60 C ANISOU 635 C TYR A 92 8587 10704 6016 613 -177 296 C ATOM 636 O TYR A 92 -22.196 -11.356 -78.131 1.00 77.49 O ANISOU 636 O TYR A 92 10019 12143 7281 644 -107 341 O ATOM 637 CB TYR A 92 -22.215 -13.661 -76.578 1.00 71.89 C ANISOU 637 CB TYR A 92 9354 11266 6696 462 -125 -22 C ATOM 638 CG TYR A 92 -22.280 -14.833 -75.623 1.00 83.94 C ANISOU 638 CG TYR A 92 10899 12684 8309 369 -134 -198 C ATOM 639 CD1 TYR A 92 -22.125 -14.650 -74.255 1.00 81.99 C ANISOU 639 CD1 TYR A 92 10610 12273 8268 351 -128 -196 C ATOM 640 CD2 TYR A 92 -22.476 -16.125 -76.093 1.00 91.35 C ANISOU 640 CD2 TYR A 92 11909 13680 9120 298 -144 -365 C ATOM 641 CE1 TYR A 92 -22.179 -15.720 -73.380 1.00 74.96 C ANISOU 641 CE1 TYR A 92 9738 11290 7455 272 -131 -340 C ATOM 642 CE2 TYR A 92 -22.529 -17.200 -75.226 1.00 90.76 C ANISOU 642 CE2 TYR A 92 11860 13493 9132 215 -143 -514 C ATOM 643 CZ TYR A 92 -22.381 -16.992 -73.871 1.00 83.79 C ANISOU 643 CZ TYR A 92 10923 12458 8455 205 -136 -493 C ATOM 644 OH TYR A 92 -22.434 -18.061 -73.006 1.00 90.49 O ANISOU 644 OH TYR A 92 11797 13200 9387 128 -131 -626 O ATOM 645 N ARG A 93 -23.577 -10.207 -76.769 1.00 60.39 N ANISOU 645 N ARG A 93 7735 9896 5312 674 -218 423 N ATOM 646 CA ARG A 93 -23.361 -8.913 -77.406 1.00 63.24 C ANISOU 646 CA ARG A 93 8090 10279 5659 778 -181 632 C ATOM 647 C ARG A 93 -23.146 -7.863 -76.327 1.00 73.34 C ANISOU 647 C ARG A 93 9351 11355 7162 811 -150 726 C ATOM 648 O ARG A 93 -23.965 -7.733 -75.413 1.00 71.78 O ANISOU 648 O ARG A 93 9109 11107 7057 808 -209 687 O ATOM 649 CB ARG A 93 -24.540 -8.524 -78.305 1.00 65.95 C ANISOU 649 CB ARG A 93 8384 10842 5834 844 -271 715 C ATOM 650 CG ARG A 93 -24.650 -9.350 -79.576 1.00 62.00 C ANISOU 650 CG ARG A 93 7917 10558 5081 818 -300 649 C ATOM 651 CD ARG A 93 -25.776 -8.851 -80.466 1.00 83.04 C ANISOU 651 CD ARG A 93 10521 13457 7575 886 -397 757 C ATOM 652 NE ARG A 93 -25.876 -9.619 -81.704 1.00101.09 N ANISOU 652 NE ARG A 93 12850 15960 9599 853 -432 687 N ATOM 653 CZ ARG A 93 -26.642 -10.693 -81.858 1.00106.92 C ANISOU 653 CZ ARG A 93 13581 16832 10211 752 -534 512 C ATOM 654 NH1 ARG A 93 -27.382 -11.132 -80.848 1.00106.85 N ANISOU 654 NH1 ARG A 93 13511 16766 10322 678 -605 404 N ATOM 655 NH2 ARG A 93 -26.670 -11.330 -83.020 1.00105.56 N ANISOU 655 NH2 ARG A 93 13468 16849 9789 719 -562 445 N ATOM 656 N TRP A 94 -22.050 -7.114 -76.439 1.00 81.43 N ANISOU 656 N TRP A 94 10410 12264 8266 837 -56 850 N ATOM 657 CA TRP A 94 -21.647 -6.174 -75.399 1.00 86.95 C ANISOU 657 CA TRP A 94 11113 12746 9179 841 -21 920 C ATOM 658 C TRP A 94 -21.860 -4.740 -75.862 1.00 95.04 C ANISOU 658 C TRP A 94 12140 13751 10219 943 -1 1130 C ATOM 659 O TRP A 94 -21.099 -4.251 -76.713 1.00100.83 O ANISOU 659 O TRP A 94 12899 14501 10909 973 71 1265 O ATOM 660 CB TRP A 94 -20.183 -6.399 -75.020 1.00 83.30 C ANISOU 660 CB TRP A 94 10683 12143 8824 770 68 901 C ATOM 661 CG TRP A 94 -19.759 -5.647 -73.801 1.00 84.82 C ANISOU 661 CG TRP A 94 10884 12115 9231 738 85 928 C ATOM 662 CD1 TRP A 94 -18.984 -4.525 -73.755 1.00 76.37 C ANISOU 662 CD1 TRP A 94 9835 10910 8271 744 146 1077 C ATOM 663 CD2 TRP A 94 -20.093 -5.960 -72.444 1.00 90.09 C ANISOU 663 CD2 TRP A 94 11542 12669 10019 685 38 800 C ATOM 664 NE1 TRP A 94 -18.812 -4.122 -72.453 1.00 99.67 N ANISOU 664 NE1 TRP A 94 12800 13670 11400 692 133 1036 N ATOM 665 CE2 TRP A 94 -19.484 -4.987 -71.628 1.00102.12 C ANISOU 665 CE2 TRP A 94 13092 13996 11714 663 69 869 C ATOM 666 CE3 TRP A 94 -20.848 -6.970 -71.840 1.00 75.85 C ANISOU 666 CE3 TRP A 94 9715 10912 8192 650 -26 635 C ATOM 667 CZ2 TRP A 94 -19.606 -4.993 -70.241 1.00100.80 C ANISOU 667 CZ2 TRP A 94 12932 13688 11679 614 37 773 C ATOM 668 CZ3 TRP A 94 -20.968 -6.975 -70.463 1.00 92.33 C ANISOU 668 CZ3 TRP A 94 11801 12861 10419 607 -50 555 C ATOM 669 CH2 TRP A 94 -20.350 -5.993 -69.678 1.00106.38 C ANISOU 669 CH2 TRP A 94 13612 14456 12353 594 -19 621 C ATOM 670 N PRO A 95 -22.864 -4.030 -75.346 1.00 85.94 N ANISOU 670 N PRO A 95 10964 12563 9128 1008 -51 1174 N ATOM 671 CA PRO A 95 -23.086 -2.627 -75.736 1.00 75.91 C ANISOU 671 CA PRO A 95 9707 11249 7886 1121 -22 1383 C ATOM 672 C PRO A 95 -22.601 -1.589 -74.728 1.00 79.80 C ANISOU 672 C PRO A 95 10252 11471 8596 1116 31 1440 C ATOM 673 O PRO A 95 -22.863 -0.400 -74.941 1.00 81.10 O ANISOU 673 O PRO A 95 10443 11568 8804 1213 59 1607 O ATOM 674 CB PRO A 95 -24.613 -2.577 -75.845 1.00 72.45 C ANISOU 674 CB PRO A 95 9203 10963 7362 1210 -112 1393 C ATOM 675 CG PRO A 95 -25.063 -3.482 -74.729 1.00 69.27 C ANISOU 675 CG PRO A 95 8769 10529 7022 1130 -168 1192 C ATOM 676 CD PRO A 95 -24.009 -4.569 -74.590 1.00 79.01 C ANISOU 676 CD PRO A 95 10035 11728 8256 999 -139 1046 C ATOM 677 N PHE A 96 -21.915 -1.993 -73.661 1.00 86.29 N ANISOU 677 N PHE A 96 11097 12140 9551 1009 44 1311 N ATOM 678 CA PHE A 96 -21.586 -1.089 -72.566 1.00 86.40 C ANISOU 678 CA PHE A 96 11166 11903 9759 988 74 1331 C ATOM 679 C PHE A 96 -20.210 -0.447 -72.698 1.00 91.87 C ANISOU 679 C PHE A 96 11909 12448 10550 923 155 1433 C ATOM 680 O PHE A 96 -19.790 0.269 -71.783 1.00 92.94 O ANISOU 680 O PHE A 96 12100 12367 10847 876 175 1437 O ATOM 681 CB PHE A 96 -21.681 -1.833 -71.231 1.00 87.21 C ANISOU 681 CB PHE A 96 11261 11929 9946 906 32 1138 C ATOM 682 CG PHE A 96 -23.015 -2.478 -70.994 1.00 87.07 C ANISOU 682 CG PHE A 96 11185 12047 9850 953 -43 1039 C ATOM 683 CD1 PHE A 96 -24.120 -1.711 -70.661 1.00 90.00 C ANISOU 683 CD1 PHE A 96 11551 12395 10249 1063 -64 1093 C ATOM 684 CD2 PHE A 96 -23.165 -3.850 -71.103 1.00 83.22 C ANISOU 684 CD2 PHE A 96 10647 11707 9266 888 -87 897 C ATOM 685 CE1 PHE A 96 -25.350 -2.301 -70.443 1.00 80.44 C ANISOU 685 CE1 PHE A 96 10266 11326 8971 1102 -132 1016 C ATOM 686 CE2 PHE A 96 -24.393 -4.446 -70.886 1.00 81.04 C ANISOU 686 CE2 PHE A 96 10310 11558 8925 912 -159 812 C ATOM 687 CZ PHE A 96 -25.486 -3.670 -70.556 1.00 76.01 C ANISOU 687 CZ PHE A 96 9649 10916 8317 1017 -183 876 C ATOM 688 N GLY A 97 -19.502 -0.677 -73.799 1.00 94.25 N ANISOU 688 N GLY A 97 12194 12863 10755 914 202 1516 N ATOM 689 CA GLY A 97 -18.222 -0.044 -74.028 1.00 96.02 C ANISOU 689 CA GLY A 97 12447 12970 11066 854 285 1640 C ATOM 690 C GLY A 97 -17.057 -0.817 -73.436 1.00 98.29 C ANISOU 690 C GLY A 97 12712 13208 11427 719 305 1532 C ATOM 691 O GLY A 97 -17.213 -1.791 -72.696 1.00 97.88 O ANISOU 691 O GLY A 97 12635 13177 11377 671 257 1357 O ATOM 692 N ASN A 98 -15.852 -0.352 -73.775 1.00100.06 N ANISOU 692 N ASN A 98 12936 13368 11714 660 382 1655 N ATOM 693 CA ASN A 98 -14.630 -1.021 -73.348 1.00 92.73 C ANISOU 693 CA ASN A 98 11967 12416 10853 542 413 1592 C ATOM 694 C ASN A 98 -14.252 -0.703 -71.907 1.00 93.24 C ANISOU 694 C ASN A 98 12050 12275 11103 432 376 1515 C ATOM 695 O ASN A 98 -13.508 -1.474 -71.292 1.00 78.14 O ANISOU 695 O ASN A 98 10092 10360 9236 344 370 1419 O ATOM 696 CB ASN A 98 -13.477 -0.643 -74.281 1.00 89.07 C ANISOU 696 CB ASN A 98 11476 11982 10383 518 513 1769 C ATOM 697 CG ASN A 98 -12.273 -1.549 -74.119 1.00 93.66 C ANISOU 697 CG ASN A 98 11990 12609 10988 432 556 1717 C ATOM 698 OD1 ASN A 98 -12.182 -2.600 -74.754 1.00 92.57 O ANISOU 698 OD1 ASN A 98 11821 12639 10711 475 585 1659 O ATOM 699 ND2 ASN A 98 -11.339 -1.144 -73.267 1.00104.72 N ANISOU 699 ND2 ASN A 98 13369 13858 12561 310 562 1739 N ATOM 700 N TYR A 99 -14.740 0.410 -71.357 1.00 98.39 N ANISOU 700 N TYR A 99 12771 12755 11855 442 352 1556 N ATOM 701 CA TYR A 99 -14.436 0.741 -69.969 1.00 95.96 C ANISOU 701 CA TYR A 99 12501 12253 11707 336 312 1468 C ATOM 702 C TYR A 99 -15.272 -0.085 -68.998 1.00 89.15 C ANISOU 702 C TYR A 99 11636 11416 10820 353 236 1270 C ATOM 703 O TYR A 99 -14.771 -0.509 -67.951 1.00 87.24 O ANISOU 703 O TYR A 99 11382 11108 10656 253 202 1158 O ATOM 704 CB TYR A 99 -14.656 2.234 -69.721 1.00115.95 C ANISOU 704 CB TYR A 99 15132 14574 14351 343 325 1571 C ATOM 705 CG TYR A 99 -13.408 3.074 -69.874 1.00139.87 C ANISOU 705 CG TYR A 99 18173 17472 17500 224 381 1713 C ATOM 706 CD1 TYR A 99 -12.665 3.456 -68.764 1.00144.88 C ANISOU 706 CD1 TYR A 99 18838 17925 18284 70 352 1658 C ATOM 707 CD2 TYR A 99 -12.972 3.486 -71.127 1.00150.29 C ANISOU 707 CD2 TYR A 99 19470 18857 18776 256 460 1906 C ATOM 708 CE1 TYR A 99 -11.524 4.224 -68.897 1.00147.12 C ANISOU 708 CE1 TYR A 99 19122 18094 18682 -61 395 1790 C ATOM 709 CE2 TYR A 99 -11.831 4.254 -71.270 1.00152.12 C ANISOU 709 CE2 TYR A 99 19701 18972 19124 136 515 2047 C ATOM 710 CZ TYR A 99 -11.112 4.620 -70.151 1.00149.93 C ANISOU 710 CZ TYR A 99 19448 18514 19006 -28 480 1988 C ATOM 711 OH TYR A 99 -9.976 5.385 -70.287 1.00152.26 O ANISOU 711 OH TYR A 99 19733 18697 19420 -168 526 2131 O ATOM 712 N LEU A 100 -16.541 -0.327 -69.328 1.00 94.00 N ANISOU 712 N LEU A 100 12253 12135 11327 475 206 1234 N ATOM 713 CA LEU A 100 -17.418 -1.068 -68.430 1.00 84.33 C ANISOU 713 CA LEU A 100 11020 10939 10083 492 139 1063 C ATOM 714 C LEU A 100 -17.138 -2.565 -68.424 1.00 87.58 C ANISOU 714 C LEU A 100 11361 11496 10420 446 122 938 C ATOM 715 O LEU A 100 -17.578 -3.256 -67.499 1.00100.04 O ANISOU 715 O LEU A 100 12929 13071 12009 424 73 794 O ATOM 716 CB LEU A 100 -18.884 -0.818 -68.794 1.00 85.32 C ANISOU 716 CB LEU A 100 11153 11141 10122 632 112 1080 C ATOM 717 CG LEU A 100 -19.484 0.469 -68.225 1.00 88.59 C ANISOU 717 CG LEU A 100 11650 11377 10631 695 117 1135 C ATOM 718 CD1 LEU A 100 -20.933 0.630 -68.654 1.00 82.98 C ANISOU 718 CD1 LEU A 100 10921 10778 9828 851 94 1171 C ATOM 719 CD2 LEU A 100 -19.369 0.480 -66.707 1.00 90.79 C ANISOU 719 CD2 LEU A 100 11977 11495 11025 618 87 998 C ATOM 720 N ACYS A 101 -16.432 -3.084 -69.429 0.54 86.55 N ANISOU 720 N ACYS A 101 11187 11486 10210 438 170 994 N ATOM 721 N BCYS A 101 -16.413 -3.079 -69.420 0.46 86.48 N ANISOU 721 N BCYS A 101 11178 11476 10204 437 170 994 N ATOM 722 CA ACYS A 101 -16.091 -4.501 -69.416 0.54 84.70 C ANISOU 722 CA ACYS A 101 10903 11365 9914 402 169 875 C ATOM 723 CA BCYS A 101 -16.087 -4.501 -69.434 0.46 84.64 C ANISOU 723 CA BCYS A 101 10895 11359 9905 402 170 877 C ATOM 724 C ACYS A 101 -14.877 -4.773 -68.539 0.54 84.30 C ANISOU 724 C ACYS A 101 10827 11219 9983 290 183 841 C ATOM 725 C BCYS A 101 -14.854 -4.800 -68.589 0.46 84.32 C ANISOU 725 C BCYS A 101 10828 11228 9981 291 186 844 C ATOM 726 O ACYS A 101 -14.832 -5.790 -67.836 0.54 86.43 O ANISOU 726 O ACYS A 101 11073 11508 10257 254 157 711 O ATOM 727 O BCYS A 101 -14.774 -5.859 -67.957 0.46 86.07 O ANISOU 727 O BCYS A 101 11024 11477 10201 257 163 716 O ATOM 728 CB ACYS A 101 -15.834 -5.008 -70.834 0.54 84.66 C ANISOU 728 CB ACYS A 101 10873 11531 9763 450 223 935 C ATOM 729 CB BCYS A 101 -15.878 -4.984 -70.870 0.46 84.58 C ANISOU 729 CB BCYS A 101 10865 11524 9748 454 222 938 C ATOM 730 SG ACYS A 101 -15.329 -6.742 -70.867 0.54 84.12 S ANISOU 730 SG ACYS A 101 10769 11573 9621 415 243 790 S ATOM 731 SG BCYS A 101 -14.290 -4.523 -71.599 0.46 81.45 S ANISOU 731 SG BCYS A 101 10443 11113 9390 413 327 1106 S ATOM 732 N LYS A 102 -13.884 -3.881 -68.570 1.00 83.36 N ANISOU 732 N LYS A 102 10709 11003 9962 231 223 966 N ATOM 733 CA LYS A 102 -12.702 -4.068 -67.735 1.00 82.46 C ANISOU 733 CA LYS A 102 10555 10815 9963 115 226 949 C ATOM 734 C LYS A 102 -13.053 -4.015 -66.255 1.00 86.23 C ANISOU 734 C LYS A 102 11064 11170 10528 59 149 826 C ATOM 735 O LYS A 102 -12.427 -4.706 -65.445 1.00 99.95 O ANISOU 735 O LYS A 102 12759 12904 12312 -13 129 753 O ATOM 736 CB LYS A 102 -11.646 -3.013 -68.066 1.00 74.23 C ANISOU 736 CB LYS A 102 9501 9691 9012 46 276 1116 C ATOM 737 CG LYS A 102 -11.051 -3.140 -69.458 1.00 70.62 C ANISOU 737 CG LYS A 102 8997 9364 8472 91 368 1251 C ATOM 738 CD LYS A 102 -9.956 -2.109 -69.684 1.00 71.11 C ANISOU 738 CD LYS A 102 9035 9341 8643 4 419 1425 C ATOM 739 CE LYS A 102 -9.256 -2.323 -71.017 1.00 55.31 C ANISOU 739 CE LYS A 102 6975 7485 6557 50 524 1564 C ATOM 740 NZ LYS A 102 -8.604 -3.659 -71.098 1.00 64.50 N ANISOU 740 NZ LYS A 102 8058 8785 7664 60 563 1497 N ATOM 741 N ILE A 103 -14.048 -3.208 -65.887 1.00 70.52 N ANISOU 741 N ILE A 103 9150 9087 8556 100 111 808 N ATOM 742 CA ILE A 103 -14.505 -3.173 -64.502 1.00 69.52 C ANISOU 742 CA ILE A 103 9066 8857 8491 66 46 684 C ATOM 743 C ILE A 103 -15.332 -4.410 -64.178 1.00 72.80 C ANISOU 743 C ILE A 103 9453 9384 8824 116 13 545 C ATOM 744 O ILE A 103 -15.176 -5.012 -63.110 1.00 79.68 O ANISOU 744 O ILE A 103 10313 10231 9732 61 -24 439 O ATOM 745 CB ILE A 103 -15.293 -1.877 -64.237 1.00 64.99 C ANISOU 745 CB ILE A 103 8591 8139 7963 111 34 716 C ATOM 746 CG1 ILE A 103 -14.407 -0.653 -64.476 1.00 67.42 C ANISOU 746 CG1 ILE A 103 8941 8306 8369 38 68 851 C ATOM 747 CG2 ILE A 103 -15.848 -1.868 -62.820 1.00 67.81 C ANISOU 747 CG2 ILE A 103 9001 8400 8364 92 -22 580 C ATOM 748 CD1 ILE A 103 -13.212 -0.573 -63.553 1.00 80.90 C ANISOU 748 CD1 ILE A 103 10636 9918 10185 -123 40 825 C ATOM 749 N ALA A 104 -16.213 -4.814 -65.095 1.00 58.04 N ANISOU 749 N ALA A 104 7570 7643 6840 214 24 546 N ATOM 750 CA ALA A 104 -17.080 -5.961 -64.840 1.00 62.26 C ANISOU 750 CA ALA A 104 8079 8280 7298 247 -10 417 C ATOM 751 C ALA A 104 -16.278 -7.255 -64.764 1.00 68.75 C ANISOU 751 C ALA A 104 8849 9169 8103 192 7 352 C ATOM 752 O ALA A 104 -16.485 -8.072 -63.860 1.00 78.95 O ANISOU 752 O ALA A 104 10131 10458 9409 164 -24 239 O ATOM 753 CB ALA A 104 -18.158 -6.056 -65.919 1.00 64.72 C ANISOU 753 CB ALA A 104 8382 8726 7485 347 -12 442 C ATOM 754 N SER A 105 -15.357 -7.461 -65.709 1.00 75.83 N ANISOU 754 N SER A 105 9716 10129 8969 186 66 430 N ATOM 755 CA SER A 105 -14.549 -8.675 -65.690 1.00 85.93 C ANISOU 755 CA SER A 105 10950 11466 10234 154 99 380 C ATOM 756 C SER A 105 -13.601 -8.702 -64.499 1.00 85.59 C ANISOU 756 C SER A 105 10879 11329 10313 67 84 367 C ATOM 757 O SER A 105 -13.301 -9.780 -63.972 1.00 89.23 O ANISOU 757 O SER A 105 11310 11815 10778 49 86 291 O ATOM 758 CB SER A 105 -13.766 -8.810 -66.995 1.00 78.39 C ANISOU 758 CB SER A 105 9969 10602 9212 184 180 477 C ATOM 759 OG SER A 105 -14.643 -8.958 -68.098 1.00 91.68 O ANISOU 759 OG SER A 105 11681 12397 10757 261 186 473 O ATOM 760 N ALA A 106 -13.120 -7.537 -64.061 1.00 78.30 N ANISOU 760 N ALA A 106 9967 10297 9487 9 67 444 N ATOM 761 CA ALA A 106 -12.281 -7.494 -62.870 1.00 78.01 C ANISOU 761 CA ALA A 106 9905 10180 9556 -88 33 426 C ATOM 762 C ALA A 106 -13.102 -7.736 -61.611 1.00 77.94 C ANISOU 762 C ALA A 106 9936 10117 9560 -96 -36 296 C ATOM 763 O ALA A 106 -12.628 -8.381 -60.670 1.00 65.59 O ANISOU 763 O ALA A 106 8341 8549 8032 -147 -61 241 O ATOM 764 CB ALA A 106 -11.552 -6.154 -62.782 1.00 69.62 C ANISOU 764 CB ALA A 106 8854 9010 8589 -168 28 536 C ATOM 765 N SER A 107 -14.338 -7.230 -61.579 1.00 78.95 N ANISOU 765 N SER A 107 10129 10213 9655 -38 -61 257 N ATOM 766 CA SER A 107 -15.184 -7.408 -60.404 1.00 67.05 C ANISOU 766 CA SER A 107 8659 8662 8154 -34 -114 143 C ATOM 767 C SER A 107 -15.495 -8.878 -60.152 1.00 74.03 C ANISOU 767 C SER A 107 9502 9642 8985 -16 -116 47 C ATOM 768 O SER A 107 -15.645 -9.290 -58.996 1.00 84.83 O ANISOU 768 O SER A 107 10875 10980 10376 -45 -151 -33 O ATOM 769 CB SER A 107 -16.478 -6.610 -60.564 1.00 77.62 C ANISOU 769 CB SER A 107 10060 9969 9463 48 -126 138 C ATOM 770 OG SER A 107 -17.300 -6.732 -59.416 1.00 97.23 O ANISOU 770 OG SER A 107 12576 12415 11952 60 -165 36 O ATOM 771 N VAL A 108 -15.593 -9.680 -61.212 1.00 69.41 N ANISOU 771 N VAL A 108 8884 9164 8323 30 -75 54 N ATOM 772 CA VAL A 108 -15.850 -11.106 -61.037 1.00 77.91 C ANISOU 772 CA VAL A 108 9938 10311 9354 39 -68 -38 C ATOM 773 C VAL A 108 -14.589 -11.827 -60.577 1.00 82.09 C ANISOU 773 C VAL A 108 10422 10834 9935 -11 -44 -28 C ATOM 774 O VAL A 108 -14.640 -12.685 -59.689 1.00 76.14 O ANISOU 774 O VAL A 108 9659 10074 9196 -28 -59 -99 O ATOM 775 CB VAL A 108 -16.408 -11.709 -62.339 1.00 73.06 C ANISOU 775 CB VAL A 108 9322 9806 8630 96 -36 -48 C ATOM 776 CG1 VAL A 108 -16.783 -13.166 -62.131 1.00 56.97 C ANISOU 776 CG1 VAL A 108 7279 7818 6551 93 -30 -155 C ATOM 777 CG2 VAL A 108 -17.610 -10.912 -62.820 1.00 69.37 C ANISOU 777 CG2 VAL A 108 8880 9366 8112 149 -66 -32 C ATOM 778 N SER A 109 -13.439 -11.491 -61.168 1.00 77.90 N ANISOU 778 N SER A 109 9856 10311 9433 -29 -2 72 N ATOM 779 CA SER A 109 -12.185 -12.104 -60.740 1.00 79.39 C ANISOU 779 CA SER A 109 9981 10508 9675 -67 23 104 C ATOM 780 C SER A 109 -11.793 -11.639 -59.344 1.00 79.08 C ANISOU 780 C SER A 109 9931 10393 9722 -147 -44 98 C ATOM 781 O SER A 109 -11.260 -12.422 -58.549 1.00 62.05 O ANISOU 781 O SER A 109 7732 8250 7594 -169 -52 77 O ATOM 782 CB SER A 109 -11.076 -11.788 -61.743 1.00 75.26 C ANISOU 782 CB SER A 109 9408 10026 9162 -66 90 228 C ATOM 783 OG SER A 109 -11.376 -12.321 -63.021 1.00100.32 O ANISOU 783 OG SER A 109 12600 13280 12236 12 157 226 O ATOM 784 N PHE A 110 -12.050 -10.367 -59.027 1.00 81.22 N ANISOU 784 N PHE A 110 10247 10583 10030 -189 -92 116 N ATOM 785 CA PHE A 110 -11.740 -9.852 -57.697 1.00 69.88 C ANISOU 785 CA PHE A 110 8822 9069 8659 -272 -163 92 C ATOM 786 C PHE A 110 -12.546 -10.582 -56.630 1.00 72.80 C ANISOU 786 C PHE A 110 9221 9439 9000 -252 -200 -23 C ATOM 787 O PHE A 110 -12.005 -10.985 -55.594 1.00 60.44 O ANISOU 787 O PHE A 110 7627 7875 7463 -302 -236 -43 O ATOM 788 CB PHE A 110 -12.012 -8.348 -57.645 1.00 64.15 C ANISOU 788 CB PHE A 110 8170 8236 7969 -309 -195 118 C ATOM 789 CG PHE A 110 -11.627 -7.702 -56.346 1.00 87.13 C ANISOU 789 CG PHE A 110 11113 11055 10938 -409 -268 86 C ATOM 790 CD1 PHE A 110 -10.342 -7.227 -56.149 1.00 96.43 C ANISOU 790 CD1 PHE A 110 12240 12211 12186 -524 -293 164 C ATOM 791 CD2 PHE A 110 -12.555 -7.555 -55.327 1.00 91.29 C ANISOU 791 CD2 PHE A 110 11720 11524 11442 -394 -312 -21 C ATOM 792 CE1 PHE A 110 -9.985 -6.627 -54.958 1.00 98.70 C ANISOU 792 CE1 PHE A 110 12565 12421 12515 -632 -372 125 C ATOM 793 CE2 PHE A 110 -12.203 -6.957 -54.133 1.00 86.42 C ANISOU 793 CE2 PHE A 110 11150 10826 10861 -487 -380 -61 C ATOM 794 CZ PHE A 110 -10.916 -6.491 -53.950 1.00 90.87 C ANISOU 794 CZ PHE A 110 11671 11368 11489 -612 -415 6 C ATOM 795 N ASN A 111 -13.846 -10.768 -56.872 1.00 80.28 N ANISOU 795 N ASN A 111 10217 10396 9888 -180 -192 -90 N ATOM 796 CA ASN A 111 -14.696 -11.434 -55.892 1.00 76.20 C ANISOU 796 CA ASN A 111 9724 9885 9346 -161 -218 -190 C ATOM 797 C ASN A 111 -14.311 -12.896 -55.707 1.00 80.85 C ANISOU 797 C ASN A 111 10259 10538 9922 -154 -192 -211 C ATOM 798 O ASN A 111 -14.478 -13.443 -54.612 1.00 91.51 O ANISOU 798 O ASN A 111 11611 11883 11276 -169 -218 -263 O ATOM 799 CB ASN A 111 -16.163 -11.321 -56.306 1.00 78.61 C ANISOU 799 CB ASN A 111 10070 10206 9593 -88 -212 -239 C ATOM 800 CG ASN A 111 -17.097 -12.012 -55.333 1.00 81.41 C ANISOU 800 CG ASN A 111 10437 10575 9922 -71 -231 -330 C ATOM 801 OD1 ASN A 111 -17.420 -13.189 -55.494 1.00 82.05 O ANISOU 801 OD1 ASN A 111 10488 10717 9969 -54 -209 -368 O ATOM 802 ND2 ASN A 111 -17.533 -11.283 -54.313 1.00 83.41 N ANISOU 802 ND2 ASN A 111 10739 10764 10189 -76 -267 -365 N ATOM 803 N LEU A 112 -13.799 -13.542 -56.757 1.00 86.66 N ANISOU 803 N LEU A 112 10955 11331 10641 -126 -132 -169 N ATOM 804 CA LEU A 112 -13.388 -14.937 -56.636 1.00 84.00 C ANISOU 804 CA LEU A 112 10581 11036 10298 -107 -91 -186 C ATOM 805 C LEU A 112 -12.231 -15.078 -55.653 1.00 91.62 C ANISOU 805 C LEU A 112 11491 11995 11327 -154 -113 -137 C ATOM 806 O LEU A 112 -12.292 -15.879 -54.715 1.00 94.22 O ANISOU 806 O LEU A 112 11812 12325 11660 -154 -125 -173 O ATOM 807 CB LEU A 112 -13.009 -15.494 -58.011 1.00 85.20 C ANISOU 807 CB LEU A 112 10718 11242 10412 -58 -12 -152 C ATOM 808 CG LEU A 112 -12.872 -17.013 -58.178 1.00 84.49 C ANISOU 808 CG LEU A 112 10625 11179 10298 -15 51 -191 C ATOM 809 CD1 LEU A 112 -13.153 -17.409 -59.618 1.00 98.53 C ANISOU 809 CD1 LEU A 112 12436 13002 11998 35 115 -209 C ATOM 810 CD2 LEU A 112 -11.494 -17.513 -57.760 1.00 62.88 C ANISOU 810 CD2 LEU A 112 7819 8452 7621 -13 87 -115 C ATOM 811 N TYR A 113 -11.166 -14.299 -55.853 1.00 94.23 N ANISOU 811 N TYR A 113 11774 12325 11704 -199 -121 -45 N ATOM 812 CA TYR A 113 -10.019 -14.382 -54.956 1.00 94.74 C ANISOU 812 CA TYR A 113 11767 12406 11825 -256 -154 14 C ATOM 813 C TYR A 113 -10.354 -13.842 -53.571 1.00 93.94 C ANISOU 813 C TYR A 113 11704 12257 11731 -322 -247 -41 C ATOM 814 O TYR A 113 -9.918 -14.403 -52.560 1.00 98.63 O ANISOU 814 O TYR A 113 12261 12879 12336 -342 -279 -38 O ATOM 815 CB TYR A 113 -8.830 -13.629 -55.552 1.00 99.30 C ANISOU 815 CB TYR A 113 12272 13003 12453 -305 -143 132 C ATOM 816 CG TYR A 113 -8.219 -14.297 -56.763 1.00106.95 C ANISOU 816 CG TYR A 113 13186 14039 13411 -233 -39 203 C ATOM 817 CD1 TYR A 113 -7.217 -15.248 -56.623 1.00114.99 C ANISOU 817 CD1 TYR A 113 14113 15123 14456 -201 8 268 C ATOM 818 CD2 TYR A 113 -8.638 -13.972 -58.046 1.00102.11 C ANISOU 818 CD2 TYR A 113 12614 13429 12755 -188 17 211 C ATOM 819 CE1 TYR A 113 -6.653 -15.860 -57.726 1.00115.56 C ANISOU 819 CE1 TYR A 113 14144 15251 14512 -121 117 329 C ATOM 820 CE2 TYR A 113 -8.081 -14.579 -59.156 1.00101.59 C ANISOU 820 CE2 TYR A 113 12509 13428 12662 -118 117 268 C ATOM 821 CZ TYR A 113 -7.088 -15.522 -58.989 1.00110.21 C ANISOU 821 CZ TYR A 113 13519 14574 13782 -82 172 323 C ATOM 822 OH TYR A 113 -6.528 -16.128 -60.089 1.00124.51 O ANISOU 822 OH TYR A 113 15302 16445 15562 3 287 377 O ATOM 823 N ALA A 114 -11.131 -12.758 -53.503 1.00 90.13 N ANISOU 823 N ALA A 114 11301 11705 11238 -345 -286 -88 N ATOM 824 CA ALA A 114 -11.419 -12.133 -52.216 1.00 75.60 C ANISOU 824 CA ALA A 114 9518 9811 9398 -403 -365 -146 C ATOM 825 C ALA A 114 -12.281 -13.035 -51.340 1.00 79.84 C ANISOU 825 C ALA A 114 10083 10366 9887 -356 -369 -230 C ATOM 826 O ALA A 114 -11.969 -13.252 -50.163 1.00 79.10 O ANISOU 826 O ALA A 114 9982 10285 9788 -396 -418 -245 O ATOM 827 CB ALA A 114 -12.099 -10.780 -52.427 1.00 71.38 C ANISOU 827 CB ALA A 114 9076 9183 8863 -417 -385 -175 C ATOM 828 N SER A 115 -13.371 -13.569 -51.896 1.00 72.67 N ANISOU 828 N SER A 115 9205 9468 8940 -278 -319 -279 N ATOM 829 CA SER A 115 -14.270 -14.402 -51.101 1.00 82.16 C ANISOU 829 CA SER A 115 10430 10686 10103 -241 -316 -350 C ATOM 830 C SER A 115 -13.578 -15.675 -50.632 1.00 81.82 C ANISOU 830 C SER A 115 10326 10692 10069 -237 -298 -320 C ATOM 831 O SER A 115 -13.837 -16.159 -49.524 1.00 92.39 O ANISOU 831 O SER A 115 11675 12041 11389 -240 -319 -351 O ATOM 832 CB SER A 115 -15.524 -14.741 -51.905 1.00 82.21 C ANISOU 832 CB SER A 115 10462 10704 10070 -176 -271 -398 C ATOM 833 OG SER A 115 -16.240 -13.570 -52.256 1.00 95.64 O ANISOU 833 OG SER A 115 12214 12365 11760 -161 -286 -413 O ATOM 834 N VAL A 116 -12.691 -16.228 -51.457 1.00 69.48 N ANISOU 834 N VAL A 116 8701 9163 8534 -221 -250 -253 N ATOM 835 CA VAL A 116 -12.002 -17.459 -51.086 1.00 56.10 C ANISOU 835 CA VAL A 116 6951 7509 6855 -196 -217 -212 C ATOM 836 C VAL A 116 -10.894 -17.179 -50.075 1.00 69.44 C ANISOU 836 C VAL A 116 8581 9230 8573 -254 -281 -146 C ATOM 837 O VAL A 116 -10.650 -17.981 -49.167 1.00 79.97 O ANISOU 837 O VAL A 116 9887 10595 9903 -241 -288 -128 O ATOM 838 CB VAL A 116 -11.473 -18.163 -52.349 1.00 60.76 C ANISOU 838 CB VAL A 116 7506 8122 7459 -141 -129 -166 C ATOM 839 CG1 VAL A 116 -10.606 -19.344 -51.981 1.00 70.02 C ANISOU 839 CG1 VAL A 116 8620 9327 8659 -101 -85 -105 C ATOM 840 CG2 VAL A 116 -12.635 -18.624 -53.215 1.00 57.35 C ANISOU 840 CG2 VAL A 116 7139 7671 6981 -97 -79 -245 C ATOM 841 N PHE A 117 -10.216 -16.034 -50.202 1.00 65.99 N ANISOU 841 N PHE A 117 8121 8788 8163 -324 -331 -104 N ATOM 842 CA PHE A 117 -9.188 -15.679 -49.226 1.00 70.33 C ANISOU 842 CA PHE A 117 8612 9377 8733 -403 -410 -48 C ATOM 843 C PHE A 117 -9.799 -15.378 -47.863 1.00 71.97 C ANISOU 843 C PHE A 117 8890 9564 8893 -443 -487 -126 C ATOM 844 O PHE A 117 -9.209 -15.708 -46.827 1.00 79.60 O ANISOU 844 O PHE A 117 9812 10588 9846 -475 -540 -94 O ATOM 845 CB PHE A 117 -8.377 -14.480 -49.719 1.00 67.27 C ANISOU 845 CB PHE A 117 8192 8978 8390 -490 -447 10 C ATOM 846 CG PHE A 117 -7.466 -14.792 -50.873 1.00 78.97 C ANISOU 846 CG PHE A 117 9577 10510 9919 -458 -374 117 C ATOM 847 CD1 PHE A 117 -7.151 -16.102 -51.194 1.00 81.64 C ANISOU 847 CD1 PHE A 117 9855 10905 10260 -362 -292 162 C ATOM 848 CD2 PHE A 117 -6.921 -13.771 -51.634 1.00 80.48 C ANISOU 848 CD2 PHE A 117 9743 10684 10150 -520 -377 176 C ATOM 849 CE1 PHE A 117 -6.312 -16.388 -52.256 1.00 76.36 C ANISOU 849 CE1 PHE A 117 9105 10283 9625 -318 -211 258 C ATOM 850 CE2 PHE A 117 -6.082 -14.050 -52.696 1.00 76.26 C ANISOU 850 CE2 PHE A 117 9117 10207 9652 -483 -299 282 C ATOM 851 CZ PHE A 117 -5.776 -15.359 -53.007 1.00 75.66 C ANISOU 851 CZ PHE A 117 8983 10194 9570 -377 -214 320 C ATOM 852 N LEU A 118 -10.976 -14.748 -47.842 1.00 73.89 N ANISOU 852 N LEU A 118 9239 9736 9101 -434 -491 -222 N ATOM 853 CA LEU A 118 -11.628 -14.442 -46.572 1.00 62.04 C ANISOU 853 CA LEU A 118 7814 8214 7543 -456 -547 -301 C ATOM 854 C LEU A 118 -12.045 -15.714 -45.844 1.00 62.25 C ANISOU 854 C LEU A 118 7827 8292 7533 -395 -519 -311 C ATOM 855 O LEU A 118 -11.907 -15.807 -44.619 1.00 70.39 O ANISOU 855 O LEU A 118 8869 9357 8520 -423 -573 -320 O ATOM 856 CB LEU A 118 -12.835 -13.533 -46.804 1.00 54.78 C ANISOU 856 CB LEU A 118 7003 7211 6600 -433 -536 -389 C ATOM 857 CG LEU A 118 -12.526 -12.087 -47.197 1.00 63.23 C ANISOU 857 CG LEU A 118 8121 8204 7700 -500 -573 -389 C ATOM 858 CD1 LEU A 118 -13.801 -11.341 -47.548 1.00 78.52 C ANISOU 858 CD1 LEU A 118 10156 10060 9616 -442 -541 -458 C ATOM 859 CD2 LEU A 118 -11.782 -11.376 -46.079 1.00 50.95 C ANISOU 859 CD2 LEU A 118 6593 6634 6131 -610 -669 -404 C ATOM 860 N LEU A 119 -12.559 -16.704 -46.579 1.00 60.46 N ANISOU 860 N LEU A 119 7584 8069 7319 -317 -434 -307 N ATOM 861 CA LEU A 119 -12.895 -17.981 -45.959 1.00 60.43 C ANISOU 861 CA LEU A 119 7569 8097 7294 -266 -397 -303 C ATOM 862 C LEU A 119 -11.653 -18.695 -45.444 1.00 62.93 C ANISOU 862 C LEU A 119 7799 8479 7631 -269 -411 -204 C ATOM 863 O LEU A 119 -11.726 -19.424 -44.448 1.00 66.09 O ANISOU 863 O LEU A 119 8195 8914 8001 -249 -416 -188 O ATOM 864 CB LEU A 119 -13.639 -18.871 -46.953 1.00 61.06 C ANISOU 864 CB LEU A 119 7658 8154 7389 -200 -306 -324 C ATOM 865 CG LEU A 119 -14.980 -18.355 -47.473 1.00 62.78 C ANISOU 865 CG LEU A 119 7939 8332 7580 -187 -291 -409 C ATOM 866 CD1 LEU A 119 -15.559 -19.330 -48.481 1.00 60.00 C ANISOU 866 CD1 LEU A 119 7586 7974 7238 -143 -214 -426 C ATOM 867 CD2 LEU A 119 -15.950 -18.123 -46.326 1.00 76.82 C ANISOU 867 CD2 LEU A 119 9770 10110 9309 -187 -318 -467 C ATOM 868 N THR A 120 -10.512 -18.500 -46.107 1.00 78.15 N ANISOU 868 N THR A 120 9651 10434 9609 -289 -413 -126 N ATOM 869 CA THR A 120 -9.268 -19.103 -45.642 1.00 75.88 C ANISOU 869 CA THR A 120 9260 10227 9345 -286 -428 -13 C ATOM 870 C THR A 120 -8.848 -18.519 -44.299 1.00 66.33 C ANISOU 870 C THR A 120 8040 9073 8090 -367 -543 -5 C ATOM 871 O THR A 120 -8.527 -19.259 -43.361 1.00 50.81 O ANISOU 871 O THR A 120 6035 7173 6098 -344 -562 48 O ATOM 872 CB THR A 120 -8.168 -18.902 -46.685 1.00 76.50 C ANISOU 872 CB THR A 120 9248 10332 9487 -290 -401 75 C ATOM 873 OG1 THR A 120 -8.601 -19.426 -47.946 1.00 75.90 O ANISOU 873 OG1 THR A 120 9200 10207 9432 -214 -294 55 O ATOM 874 CG2 THR A 120 -6.893 -19.610 -46.258 1.00 78.32 C ANISOU 874 CG2 THR A 120 9351 10659 9746 -267 -404 209 C ATOM 875 N CYS A 121 -8.848 -17.189 -44.188 1.00 61.24 N ANISOU 875 N CYS A 121 7438 8398 7430 -462 -622 -58 N ATOM 876 CA CYS A 121 -8.486 -16.551 -42.928 1.00 56.27 C ANISOU 876 CA CYS A 121 6823 7814 6745 -555 -738 -74 C ATOM 877 C CYS A 121 -9.543 -16.783 -41.857 1.00 64.12 C ANISOU 877 C CYS A 121 7915 8795 7651 -523 -746 -159 C ATOM 878 O CYS A 121 -9.207 -16.912 -40.674 1.00 64.22 O ANISOU 878 O CYS A 121 7919 8883 7600 -556 -817 -143 O ATOM 879 CB CYS A 121 -8.265 -15.055 -43.143 1.00 61.46 C ANISOU 879 CB CYS A 121 7525 8413 7412 -670 -810 -120 C ATOM 880 SG CYS A 121 -6.965 -14.666 -44.334 1.00 80.60 S ANISOU 880 SG CYS A 121 9824 10863 9939 -725 -804 -3 S ATOM 881 N LEU A 122 -10.819 -16.840 -42.247 1.00 70.61 N ANISOU 881 N LEU A 122 8825 9539 8464 -460 -674 -243 N ATOM 882 CA LEU A 122 -11.874 -17.127 -41.282 1.00 66.46 C ANISOU 882 CA LEU A 122 8380 9012 7862 -421 -663 -311 C ATOM 883 C LEU A 122 -11.756 -18.543 -40.734 1.00 74.58 C ANISOU 883 C LEU A 122 9351 10109 8879 -356 -623 -236 C ATOM 884 O LEU A 122 -12.105 -18.788 -39.573 1.00 75.63 O ANISOU 884 O LEU A 122 9519 10283 8933 -348 -646 -249 O ATOM 885 CB LEU A 122 -13.245 -16.908 -41.927 1.00 72.13 C ANISOU 885 CB LEU A 122 9176 9646 8583 -367 -591 -397 C ATOM 886 CG LEU A 122 -14.499 -16.995 -41.053 1.00 87.40 C ANISOU 886 CG LEU A 122 11191 11575 10442 -324 -568 -472 C ATOM 887 CD1 LEU A 122 -15.529 -15.975 -41.512 1.00 91.52 C ANISOU 887 CD1 LEU A 122 11797 12018 10958 -309 -548 -562 C ATOM 888 CD2 LEU A 122 -15.096 -18.395 -41.089 1.00 87.46 C ANISOU 888 CD2 LEU A 122 11163 11606 10461 -252 -485 -437 C ATOM 889 N SER A 123 -11.269 -19.483 -41.547 1.00 73.20 N ANISOU 889 N SER A 123 9096 9940 8776 -303 -555 -153 N ATOM 890 CA SER A 123 -11.074 -20.846 -41.065 1.00 76.10 C ANISOU 890 CA SER A 123 9416 10353 9145 -235 -507 -70 C ATOM 891 C SER A 123 -9.865 -20.935 -40.141 1.00 77.23 C ANISOU 891 C SER A 123 9476 10607 9261 -263 -588 32 C ATOM 892 O SER A 123 -9.885 -21.678 -39.154 1.00 81.44 O ANISOU 892 O SER A 123 10000 11197 9746 -227 -590 83 O ATOM 893 CB SER A 123 -10.919 -21.804 -42.246 1.00 58.95 C ANISOU 893 CB SER A 123 7204 8138 7058 -163 -401 -22 C ATOM 894 OG SER A 123 -9.752 -21.510 -42.992 1.00 72.84 O ANISOU 894 OG SER A 123 8878 9924 8872 -178 -413 48 O ATOM 895 N ILE A 124 -8.801 -20.190 -40.450 1.00 61.15 N ANISOU 895 N ILE A 124 7370 8612 7253 -333 -658 73 N ATOM 896 CA ILE A 124 -7.635 -20.158 -39.570 1.00 58.17 C ANISOU 896 CA ILE A 124 6898 8361 6844 -380 -755 171 C ATOM 897 C ILE A 124 -8.002 -19.533 -38.230 1.00 79.68 C ANISOU 897 C ILE A 124 9700 11126 9450 -451 -858 100 C ATOM 898 O ILE A 124 -7.524 -19.963 -37.173 1.00 74.95 O ANISOU 898 O ILE A 124 9055 10638 8784 -451 -916 171 O ATOM 899 CB ILE A 124 -6.472 -19.411 -40.251 1.00 56.15 C ANISOU 899 CB ILE A 124 6544 8141 6650 -459 -809 229 C ATOM 900 CG1 ILE A 124 -6.012 -20.162 -41.502 1.00 68.06 C ANISOU 900 CG1 ILE A 124 7969 9630 8261 -368 -694 316 C ATOM 901 CG2 ILE A 124 -5.309 -19.222 -39.287 1.00 47.55 C ANISOU 901 CG2 ILE A 124 5349 7198 5518 -537 -934 323 C ATOM 902 CD1 ILE A 124 -4.842 -19.510 -42.208 1.00 60.01 C ANISOU 902 CD1 ILE A 124 6836 8660 7307 -434 -729 395 C ATOM 903 N ASP A 125 -8.865 -18.513 -38.253 1.00 78.67 N ANISOU 903 N ASP A 125 9695 10911 9285 -502 -877 -40 N ATOM 904 CA ASP A 125 -9.325 -17.903 -37.011 1.00 66.99 C ANISOU 904 CA ASP A 125 8316 9455 7683 -555 -955 -127 C ATOM 905 C ASP A 125 -10.107 -18.892 -36.156 1.00 67.12 C ANISOU 905 C ASP A 125 8368 9506 7630 -462 -899 -116 C ATOM 906 O ASP A 125 -10.025 -18.847 -34.924 1.00 78.97 O ANISOU 906 O ASP A 125 9897 11092 9017 -487 -968 -117 O ATOM 907 CB ASP A 125 -10.181 -16.674 -37.317 1.00 63.86 C ANISOU 907 CB ASP A 125 8052 8938 7273 -598 -956 -274 C ATOM 908 CG ASP A 125 -10.684 -15.989 -36.063 1.00 92.48 C ANISOU 908 CG ASP A 125 11801 12572 10765 -640 -1022 -377 C ATOM 909 OD1 ASP A 125 -9.880 -15.306 -35.395 1.00100.51 O ANISOU 909 OD1 ASP A 125 12825 13643 11723 -751 -1143 -389 O ATOM 910 OD2 ASP A 125 -11.883 -16.134 -35.741 1.00103.03 O ANISOU 910 OD2 ASP A 125 13228 13868 12051 -565 -953 -447 O ATOM 911 N ARG A 126 -10.860 -19.795 -36.787 1.00 61.33 N ANISOU 911 N ARG A 126 7636 8710 6958 -363 -775 -102 N ATOM 912 CA ARG A 126 -11.623 -20.777 -36.023 1.00 56.22 C ANISOU 912 CA ARG A 126 7018 8086 6259 -285 -712 -79 C ATOM 913 C ARG A 126 -10.713 -21.831 -35.406 1.00 63.66 C ANISOU 913 C ARG A 126 7863 9134 7192 -244 -724 71 C ATOM 914 O ARG A 126 -10.980 -22.317 -34.301 1.00 79.69 O ANISOU 914 O ARG A 126 9915 11230 9133 -213 -728 105 O ATOM 915 CB ARG A 126 -12.679 -21.436 -36.909 1.00 60.46 C ANISOU 915 CB ARG A 126 7582 8521 6869 -213 -583 -109 C ATOM 916 CG ARG A 126 -13.934 -20.601 -37.113 1.00 72.49 C ANISOU 916 CG ARG A 126 9207 9970 8367 -223 -561 -244 C ATOM 917 CD ARG A 126 -14.591 -20.247 -35.785 1.00 92.86 C ANISOU 917 CD ARG A 126 11868 12596 10820 -225 -589 -297 C ATOM 918 NE ARG A 126 -14.138 -18.957 -35.271 1.00 99.21 N ANISOU 918 NE ARG A 126 12727 13417 11549 -302 -697 -367 N ATOM 919 CZ ARG A 126 -14.411 -18.500 -34.053 1.00 91.77 C ANISOU 919 CZ ARG A 126 11866 12525 10477 -317 -743 -420 C ATOM 920 NH1 ARG A 126 -15.135 -19.229 -33.216 1.00 89.07 N ANISOU 920 NH1 ARG A 126 11547 12233 10065 -253 -686 -397 N ATOM 921 NH2 ARG A 126 -13.957 -17.314 -33.672 1.00 93.09 N ANISOU 921 NH2 ARG A 126 12099 12690 10581 -401 -842 -496 N ATOM 922 N TYR A 127 -9.638 -22.203 -36.105 1.00 62.16 N ANISOU 922 N TYR A 127 7560 8965 7091 -232 -720 174 N ATOM 923 CA TYR A 127 -8.694 -23.159 -35.538 1.00 62.01 C ANISOU 923 CA TYR A 127 7436 9055 7069 -179 -730 335 C ATOM 924 C TYR A 127 -8.013 -22.591 -34.300 1.00 76.04 C ANISOU 924 C TYR A 127 9186 10980 8727 -256 -876 364 C ATOM 925 O TYR A 127 -7.733 -23.323 -33.343 1.00 82.81 O ANISOU 925 O TYR A 127 10003 11940 9519 -208 -892 469 O ATOM 926 CB TYR A 127 -7.654 -23.560 -36.584 1.00 52.01 C ANISOU 926 CB TYR A 127 6050 7788 5921 -143 -691 439 C ATOM 927 CG TYR A 127 -6.429 -24.218 -35.993 1.00 57.42 C ANISOU 927 CG TYR A 127 6600 8614 6602 -102 -731 617 C ATOM 928 CD1 TYR A 127 -6.501 -25.487 -35.434 1.00 46.20 C ANISOU 928 CD1 TYR A 127 5165 7215 5175 12 -659 729 C ATOM 929 CD2 TYR A 127 -5.201 -23.570 -35.993 1.00 66.38 C ANISOU 929 CD2 TYR A 127 7616 9865 7741 -177 -840 685 C ATOM 930 CE1 TYR A 127 -5.384 -26.091 -34.889 1.00 60.82 C ANISOU 930 CE1 TYR A 127 6885 9202 7021 67 -692 909 C ATOM 931 CE2 TYR A 127 -4.077 -24.167 -35.452 1.00 68.25 C ANISOU 931 CE2 TYR A 127 7709 10252 7972 -134 -880 863 C ATOM 932 CZ TYR A 127 -4.175 -25.428 -34.902 1.00 73.05 C ANISOU 932 CZ TYR A 127 8303 10882 8570 -3 -805 977 C ATOM 933 OH TYR A 127 -3.060 -26.028 -34.362 1.00 81.01 O ANISOU 933 OH TYR A 127 9162 12048 9572 56 -843 1170 O ATOM 934 N LEU A 128 -7.743 -21.285 -34.296 1.00 71.56 N ANISOU 934 N LEU A 128 8644 10421 8123 -379 -984 272 N ATOM 935 CA LEU A 128 -7.084 -20.670 -33.150 1.00 71.94 C ANISOU 935 CA LEU A 128 8678 10607 8048 -476 -1137 280 C ATOM 936 C LEU A 128 -8.067 -20.384 -32.020 1.00 74.00 C ANISOU 936 C LEU A 128 9083 10873 8160 -483 -1158 173 C ATOM 937 O LEU A 128 -7.712 -20.503 -30.844 1.00 63.78 O ANISOU 937 O LEU A 128 7780 9716 6740 -504 -1243 218 O ATOM 938 CB LEU A 128 -6.379 -19.384 -33.582 1.00 68.54 C ANISOU 938 CB LEU A 128 8231 10171 7642 -621 -1245 220 C ATOM 939 CG LEU A 128 -5.300 -19.529 -34.657 1.00 61.73 C ANISOU 939 CG LEU A 128 7213 9325 6916 -627 -1232 335 C ATOM 940 CD1 LEU A 128 -4.745 -18.168 -35.049 1.00 50.34 C ANISOU 940 CD1 LEU A 128 5769 7861 5495 -786 -1333 269 C ATOM 941 CD2 LEU A 128 -4.187 -20.451 -34.180 1.00 54.70 C ANISOU 941 CD2 LEU A 128 6153 8606 6023 -579 -1266 529 C ATOM 942 N ALA A 129 -9.305 -20.013 -32.354 1.00 75.40 N ANISOU 942 N ALA A 129 9389 10916 8344 -461 -1078 38 N ATOM 943 CA ALA A 129 -10.275 -19.655 -31.326 1.00 67.63 C ANISOU 943 CA ALA A 129 8542 9935 7218 -458 -1083 -67 C ATOM 944 C ALA A 129 -10.816 -20.868 -30.580 1.00 73.26 C ANISOU 944 C ALA A 129 9251 10706 7878 -348 -1003 20 C ATOM 945 O ALA A 129 -11.261 -20.727 -29.436 1.00 84.09 O ANISOU 945 O ALA A 129 10704 12145 9102 -346 -1030 -18 O ATOM 946 CB ALA A 129 -11.433 -18.871 -31.946 1.00 72.87 C ANISOU 946 CB ALA A 129 9328 10447 7913 -454 -1014 -221 C ATOM 947 N ILE A 130 -10.785 -22.047 -31.192 1.00 71.59 N ANISOU 947 N ILE A 130 8957 10465 7781 -257 -901 135 N ATOM 948 CA ILE A 130 -11.354 -23.247 -30.596 1.00 68.46 C ANISOU 948 CA ILE A 130 8563 10093 7358 -156 -808 224 C ATOM 949 C ILE A 130 -10.286 -24.106 -29.929 1.00 75.29 C ANISOU 949 C ILE A 130 9319 11095 8193 -117 -851 405 C ATOM 950 O ILE A 130 -10.520 -24.671 -28.860 1.00 69.05 O ANISOU 950 O ILE A 130 8547 10390 7298 -69 -843 473 O ATOM 951 CB ILE A 130 -12.129 -24.050 -31.664 1.00 67.55 C ANISOU 951 CB ILE A 130 8447 9835 7384 -83 -657 228 C ATOM 952 CG1 ILE A 130 -13.260 -23.202 -32.247 1.00 75.61 C ANISOU 952 CG1 ILE A 130 9563 10744 8419 -114 -620 63 C ATOM 953 CG2 ILE A 130 -12.678 -25.343 -31.077 1.00 54.88 C ANISOU 953 CG2 ILE A 130 6844 8238 5768 8 -556 330 C ATOM 954 CD1 ILE A 130 -13.990 -23.861 -33.397 1.00 68.96 C ANISOU 954 CD1 ILE A 130 8716 9777 7709 -67 -496 53 C ATOM 955 N VAL A 131 -9.107 -24.205 -30.537 1.00 81.87 N ANISOU 955 N VAL A 131 10031 11962 9114 -130 -894 495 N ATOM 956 CA VAL A 131 -8.071 -25.102 -30.031 1.00 78.48 C ANISOU 956 CA VAL A 131 9477 11664 8676 -70 -920 690 C ATOM 957 C VAL A 131 -7.099 -24.376 -29.107 1.00 75.08 C ANISOU 957 C VAL A 131 8993 11420 8116 -165 -1099 718 C ATOM 958 O VAL A 131 -6.666 -24.934 -28.096 1.00 77.83 O ANISOU 958 O VAL A 131 9290 11917 8366 -125 -1146 846 O ATOM 959 CB VAL A 131 -7.341 -25.770 -31.212 1.00 67.06 C ANISOU 959 CB VAL A 131 7919 10159 7403 -5 -844 794 C ATOM 960 CG1 VAL A 131 -6.355 -26.813 -30.707 1.00 76.00 C ANISOU 960 CG1 VAL A 131 8923 11416 8539 90 -843 1013 C ATOM 961 CG2 VAL A 131 -8.347 -26.398 -32.164 1.00 53.86 C ANISOU 961 CG2 VAL A 131 6321 8298 5846 64 -680 737 C ATOM 962 N HIS A 132 -6.748 -23.128 -29.422 1.00 71.46 N ANISOU 962 N HIS A 132 8546 10958 7649 -297 -1206 602 N ATOM 963 CA HIS A 132 -5.798 -22.341 -28.636 1.00 59.66 C ANISOU 963 CA HIS A 132 7003 9628 6035 -421 -1390 610 C ATOM 964 C HIS A 132 -6.465 -21.045 -28.182 1.00 70.23 C ANISOU 964 C HIS A 132 8509 10921 7255 -541 -1465 399 C ATOM 965 O HIS A 132 -6.108 -19.955 -28.650 1.00 71.07 O ANISOU 965 O HIS A 132 8630 10983 7390 -668 -1545 300 O ATOM 966 CB HIS A 132 -4.535 -22.040 -29.441 1.00 75.94 C ANISOU 966 CB HIS A 132 8908 11735 8209 -487 -1457 688 C ATOM 967 CG HIS A 132 -3.860 -23.259 -29.990 1.00 98.02 C ANISOU 967 CG HIS A 132 11547 14564 11131 -353 -1365 890 C ATOM 968 ND1 HIS A 132 -3.922 -24.489 -29.371 1.00101.96 N ANISOU 968 ND1 HIS A 132 12012 15126 11601 -214 -1298 1037 N ATOM 969 CD2 HIS A 132 -3.109 -23.435 -31.103 1.00100.00 C ANISOU 969 CD2 HIS A 132 11673 14786 11535 -328 -1319 972 C ATOM 970 CE1 HIS A 132 -3.237 -25.370 -30.078 1.00104.53 C ANISOU 970 CE1 HIS A 132 12206 15449 12061 -105 -1213 1196 C ATOM 971 NE2 HIS A 132 -2.734 -24.756 -31.134 1.00100.31 N ANISOU 971 NE2 HIS A 132 11613 14865 11635 -168 -1223 1158 N ATOM 972 N PRO A 133 -7.431 -21.126 -27.261 1.00 85.61 N ANISOU 972 N PRO A 133 10588 12874 9068 -501 -1434 331 N ATOM 973 CA PRO A 133 -8.163 -19.904 -26.886 1.00 92.34 C ANISOU 973 CA PRO A 133 11616 13658 9810 -589 -1477 122 C ATOM 974 C PRO A 133 -7.314 -18.905 -26.123 1.00 90.31 C ANISOU 974 C PRO A 133 11378 13522 9415 -748 -1670 63 C ATOM 975 O PRO A 133 -7.431 -17.695 -26.358 1.00 84.57 O ANISOU 975 O PRO A 133 10754 12699 8679 -862 -1724 -98 O ATOM 976 CB PRO A 133 -9.322 -20.437 -26.027 1.00103.14 C ANISOU 976 CB PRO A 133 13094 15033 11063 -483 -1382 102 C ATOM 977 CG PRO A 133 -9.352 -21.925 -26.263 1.00106.48 C ANISOU 977 CG PRO A 133 13406 15468 11582 -346 -1264 285 C ATOM 978 CD PRO A 133 -7.937 -22.306 -26.544 1.00 99.94 C ANISOU 978 CD PRO A 133 12404 14744 10825 -368 -1345 441 C ATOM 979 N MET A 134 -6.459 -19.373 -25.215 1.00 84.26 N ANISOU 979 N MET A 134 10516 12962 8539 -764 -1778 193 N ATOM 980 CA MET A 134 -5.687 -18.479 -24.360 1.00 74.35 C ANISOU 980 CA MET A 134 9281 11844 7124 -930 -1976 134 C ATOM 981 C MET A 134 -4.386 -18.017 -25.008 1.00 79.20 C ANISOU 981 C MET A 134 9743 12507 7843 -1065 -2098 193 C ATOM 982 O MET A 134 -3.976 -16.867 -24.814 1.00 80.09 O ANISOU 982 O MET A 134 9916 12623 7892 -1244 -2237 70 O ATOM 983 CB MET A 134 -5.383 -19.164 -23.025 1.00 76.47 C ANISOU 983 CB MET A 134 9514 12340 7203 -891 -2049 251 C ATOM 984 CG MET A 134 -6.613 -19.446 -22.178 1.00 86.56 C ANISOU 984 CG MET A 134 10955 13598 8334 -784 -1950 184 C ATOM 985 SD MET A 134 -7.436 -17.941 -21.623 1.00 89.20 S ANISOU 985 SD MET A 134 11558 13834 8501 -896 -1997 -109 S ATOM 986 CE MET A 134 -8.835 -18.625 -20.739 1.00 87.57 C ANISOU 986 CE MET A 134 11484 13634 8156 -722 -1839 -117 C ATOM 987 N LYS A 135 -3.728 -18.886 -25.776 1.00 76.40 N ANISOU 987 N LYS A 135 9193 12185 7649 -985 -2042 380 N ATOM 988 CA LYS A 135 -2.427 -18.548 -26.340 1.00 74.18 C ANISOU 988 CA LYS A 135 8737 11983 7466 -1100 -2150 469 C ATOM 989 C LYS A 135 -2.521 -17.676 -27.586 1.00 74.99 C ANISOU 989 C LYS A 135 8876 11892 7727 -1177 -2108 358 C ATOM 990 O LYS A 135 -1.558 -16.970 -27.901 1.00 77.09 O ANISOU 990 O LYS A 135 9048 12205 8037 -1330 -2225 373 O ATOM 991 CB LYS A 135 -1.647 -19.824 -26.666 1.00 71.04 C ANISOU 991 CB LYS A 135 8115 11704 7174 -964 -2094 724 C ATOM 992 CG LYS A 135 -1.286 -20.659 -25.447 1.00 80.03 C ANISOU 992 CG LYS A 135 9180 13066 8162 -896 -2159 877 C ATOM 993 CD LYS A 135 -0.420 -21.849 -25.827 1.00 90.48 C ANISOU 993 CD LYS A 135 10276 14496 9605 -756 -2100 1139 C ATOM 994 CE LYS A 135 -1.158 -22.798 -26.757 1.00 98.10 C ANISOU 994 CE LYS A 135 11273 15266 10734 -566 -1869 1174 C ATOM 995 NZ LYS A 135 -2.375 -23.366 -26.114 1.00 94.73 N ANISOU 995 NZ LYS A 135 11009 14767 10219 -457 -1766 1122 N ATOM 996 N SER A 136 -3.649 -17.704 -28.296 1.00 74.64 N ANISOU 996 N SER A 136 8956 11640 7764 -1079 -1947 258 N ATOM 997 CA SER A 136 -3.802 -16.963 -29.541 1.00 73.54 C ANISOU 997 CA SER A 136 8848 11319 7775 -1128 -1892 171 C ATOM 998 C SER A 136 -4.758 -15.783 -29.416 1.00 82.39 C ANISOU 998 C SER A 136 10196 12278 8831 -1203 -1895 -58 C ATOM 999 O SER A 136 -5.175 -15.227 -30.436 1.00103.04 O ANISOU 999 O SER A 136 12866 14720 11563 -1207 -1820 -136 O ATOM 1000 CB SER A 136 -4.274 -17.899 -30.656 1.00 69.61 C ANISOU 1000 CB SER A 136 8299 10711 7438 -957 -1704 245 C ATOM 1001 OG SER A 136 -5.551 -18.437 -30.361 1.00 59.63 O ANISOU 1001 OG SER A 136 7163 9366 6127 -829 -1584 183 O ATOM 1002 N ARG A 137 -5.113 -15.384 -28.194 1.00 84.17 N ANISOU 1002 N ARG A 137 10557 12556 8868 -1252 -1975 -162 N ATOM 1003 CA ARG A 137 -6.043 -14.273 -28.021 1.00 82.32 C ANISOU 1003 CA ARG A 137 10551 12162 8566 -1301 -1963 -379 C ATOM 1004 C ARG A 137 -5.357 -12.927 -28.229 1.00 87.05 C ANISOU 1004 C ARG A 137 11195 12701 9179 -1509 -2094 -479 C ATOM 1005 O ARG A 137 -5.930 -12.025 -28.850 1.00 79.44 O ANISOU 1005 O ARG A 137 10363 11541 8279 -1536 -2041 -610 O ATOM 1006 CB ARG A 137 -6.689 -14.346 -26.635 1.00 69.31 C ANISOU 1006 CB ARG A 137 9045 10589 6700 -1267 -1985 -459 C ATOM 1007 CG ARG A 137 -7.564 -13.152 -26.264 1.00 82.32 C ANISOU 1007 CG ARG A 137 10941 12090 8247 -1315 -1981 -688 C ATOM 1008 CD ARG A 137 -8.596 -12.831 -27.339 1.00 95.18 C ANISOU 1008 CD ARG A 137 12650 13497 10017 -1223 -1822 -765 C ATOM 1009 NE ARG A 137 -9.406 -13.987 -27.708 1.00102.55 N ANISOU 1009 NE ARG A 137 13518 14426 11021 -1034 -1660 -670 N ATOM 1010 CZ ARG A 137 -10.292 -13.987 -28.699 1.00102.74 C ANISOU 1010 CZ ARG A 137 13567 14295 11173 -939 -1520 -700 C ATOM 1011 NH1 ARG A 137 -10.988 -15.082 -28.972 1.00108.18 N ANISOU 1011 NH1 ARG A 137 14196 14992 11918 -790 -1387 -616 N ATOM 1012 NH2 ARG A 137 -10.479 -12.890 -29.422 1.00 86.98 N ANISOU 1012 NH2 ARG A 137 11660 12139 9251 -998 -1514 -811 N ATOM 1013 N LEU A 138 -4.130 -12.774 -27.729 1.00101.97 N ANISOU 1013 N LEU A 138 12972 14756 11015 -1662 -2266 -409 N ATOM 1014 CA LEU A 138 -3.438 -11.496 -27.849 1.00113.65 C ANISOU 1014 CA LEU A 138 14495 16183 12505 -1887 -2403 -502 C ATOM 1015 C LEU A 138 -2.941 -11.232 -29.264 1.00114.64 C ANISOU 1015 C LEU A 138 14501 16208 12851 -1924 -2356 -430 C ATOM 1016 O LEU A 138 -2.592 -10.090 -29.581 1.00122.97 O ANISOU 1016 O LEU A 138 15619 17158 13948 -2097 -2429 -518 O ATOM 1017 CB LEU A 138 -2.273 -11.440 -26.862 1.00113.06 C ANISOU 1017 CB LEU A 138 14321 16339 12298 -2055 -2613 -443 C ATOM 1018 CG LEU A 138 -2.678 -11.616 -25.397 1.00105.77 C ANISOU 1018 CG LEU A 138 13524 15535 11128 -2036 -2678 -518 C ATOM 1019 CD1 LEU A 138 -1.458 -11.585 -24.496 1.00116.31 C ANISOU 1019 CD1 LEU A 138 14738 17122 12331 -2209 -2899 -444 C ATOM 1020 CD2 LEU A 138 -3.683 -10.551 -24.985 1.00 79.30 C ANISOU 1020 CD2 LEU A 138 10473 11991 7665 -2073 -2653 -773 C ATOM 1021 N ARG A 139 -2.898 -12.255 -30.118 1.00100.71 N ANISOU 1021 N ARG A 139 12574 14468 11223 -1768 -2232 -272 N ATOM 1022 CA ARG A 139 -2.501 -12.088 -31.508 1.00 92.37 C ANISOU 1022 CA ARG A 139 11410 13321 10364 -1776 -2165 -199 C ATOM 1023 C ARG A 139 -3.686 -11.917 -32.449 1.00 92.32 C ANISOU 1023 C ARG A 139 11536 13093 10449 -1651 -1994 -292 C ATOM 1024 O ARG A 139 -3.484 -11.570 -33.618 1.00113.47 O ANISOU 1024 O ARG A 139 14166 15674 13274 -1668 -1938 -261 O ATOM 1025 CB ARG A 139 -1.655 -13.283 -31.965 1.00 86.76 C ANISOU 1025 CB ARG A 139 10443 12771 9749 -1680 -2128 31 C ATOM 1026 N ARG A 140 -4.905 -12.150 -31.973 1.00 64.73 N ANISOU 1026 N ARG A 140 8196 9531 6866 -1527 -1909 -394 N ATOM 1027 CA ARG A 140 -6.123 -12.024 -32.772 1.00 59.06 C ANISOU 1027 CA ARG A 140 7595 8626 6219 -1403 -1753 -478 C ATOM 1028 C ARG A 140 -6.913 -10.832 -32.236 1.00 72.61 C ANISOU 1028 C ARG A 140 9549 10202 7838 -1462 -1776 -678 C ATOM 1029 O ARG A 140 -7.773 -10.978 -31.366 1.00 89.11 O ANISOU 1029 O ARG A 140 11764 12296 9799 -1385 -1746 -763 O ATOM 1030 CB ARG A 140 -6.942 -13.311 -32.720 1.00 61.73 C ANISOU 1030 CB ARG A 140 7906 9001 6549 -1204 -1622 -419 C ATOM 1031 CG ARG A 140 -6.330 -14.473 -33.488 1.00 81.18 C ANISOU 1031 CG ARG A 140 10167 11544 9132 -1117 -1559 -237 C ATOM 1032 CD ARG A 140 -6.965 -15.804 -33.104 1.00 87.54 C ANISOU 1032 CD ARG A 140 10952 12406 9904 -951 -1459 -172 C ATOM 1033 NE ARG A 140 -8.423 -15.740 -33.054 1.00 99.74 N ANISOU 1033 NE ARG A 140 12653 13832 11413 -860 -1355 -293 N ATOM 1034 CZ ARG A 140 -9.133 -15.740 -31.929 1.00 98.68 C ANISOU 1034 CZ ARG A 140 12632 13728 11136 -833 -1363 -366 C ATOM 1035 NH1 ARG A 140 -8.518 -15.805 -30.756 1.00 81.67 N ANISOU 1035 NH1 ARG A 140 10463 11718 8848 -892 -1477 -337 N ATOM 1036 NH2 ARG A 140 -10.456 -15.675 -31.976 1.00102.86 N ANISOU 1036 NH2 ARG A 140 13280 14155 11646 -744 -1257 -462 N ATOM 1037 N THR A 141 -6.617 -9.651 -32.764 1.00 79.05 N ANISOU 1037 N THR A 141 10430 10888 8718 -1593 -1819 -748 N ATOM 1038 CA THR A 141 -7.261 -8.411 -32.354 1.00 76.68 C ANISOU 1038 CA THR A 141 10366 10425 8343 -1655 -1836 -937 C ATOM 1039 C THR A 141 -8.011 -7.802 -33.535 1.00 71.73 C ANISOU 1039 C THR A 141 9817 9593 7846 -1585 -1712 -980 C ATOM 1040 O THR A 141 -7.972 -8.310 -34.658 1.00 77.80 O ANISOU 1040 O THR A 141 10454 10356 8750 -1508 -1627 -869 O ATOM 1041 CB THR A 141 -6.236 -7.420 -31.793 1.00 82.89 C ANISOU 1041 CB THR A 141 11196 11222 9077 -1895 -2012 -995 C ATOM 1042 OG1 THR A 141 -5.312 -7.050 -32.824 1.00 81.51 O ANISOU 1042 OG1 THR A 141 10891 11017 9061 -2010 -2044 -899 O ATOM 1043 CG2 THR A 141 -5.471 -8.043 -30.635 1.00106.03 C ANISOU 1043 CG2 THR A 141 14034 14385 11868 -1965 -2148 -939 C ATOM 1044 N MET A 142 -8.702 -6.691 -33.265 1.00 71.89 N ANISOU 1044 N MET A 142 10058 9443 7815 -1607 -1698 -1142 N ATOM 1045 CA MET A 142 -9.450 -6.007 -34.314 1.00 65.54 C ANISOU 1045 CA MET A 142 9339 8442 7121 -1535 -1584 -1181 C ATOM 1046 C MET A 142 -8.524 -5.356 -35.333 1.00 69.74 C ANISOU 1046 C MET A 142 9797 8901 7800 -1672 -1626 -1112 C ATOM 1047 O MET A 142 -8.865 -5.283 -36.520 1.00 69.01 O ANISOU 1047 O MET A 142 9668 8721 7832 -1592 -1525 -1057 O ATOM 1048 CB MET A 142 -10.379 -4.962 -33.698 1.00 71.26 C ANISOU 1048 CB MET A 142 10325 9000 7751 -1513 -1554 -1364 C ATOM 1049 CG MET A 142 -11.433 -5.541 -32.769 1.00 78.30 C ANISOU 1049 CG MET A 142 11295 9956 8502 -1356 -1486 -1428 C ATOM 1050 SD MET A 142 -12.659 -6.528 -33.646 1.00 90.30 S ANISOU 1050 SD MET A 142 12713 11491 10104 -1113 -1303 -1341 S ATOM 1051 CE MET A 142 -13.405 -5.278 -34.690 1.00 93.26 C ANISOU 1051 CE MET A 142 13224 11625 10587 -1063 -1209 -1407 C ATOM 1052 N LEU A 143 -7.359 -4.875 -34.894 1.00 69.54 N ANISOU 1052 N LEU A 143 9745 8920 7757 -1884 -1775 -1109 N ATOM 1053 CA LEU A 143 -6.415 -4.261 -35.823 1.00 66.88 C ANISOU 1053 CA LEU A 143 9323 8526 7562 -2030 -1816 -1028 C ATOM 1054 C LEU A 143 -5.835 -5.293 -36.783 1.00 78.98 C ANISOU 1054 C LEU A 143 10598 10199 9210 -1964 -1769 -833 C ATOM 1055 O LEU A 143 -5.599 -4.990 -37.959 1.00 84.45 O ANISOU 1055 O LEU A 143 11229 10819 10040 -1971 -1712 -755 O ATOM 1056 CB LEU A 143 -5.300 -3.559 -35.048 1.00 64.68 C ANISOU 1056 CB LEU A 143 9061 8281 7231 -2288 -1997 -1067 C ATOM 1057 CG LEU A 143 -4.185 -2.913 -35.874 1.00 73.19 C ANISOU 1057 CG LEU A 143 10033 9324 8453 -2478 -2059 -972 C ATOM 1058 CD1 LEU A 143 -4.749 -1.853 -36.807 1.00 75.53 C ANISOU 1058 CD1 LEU A 143 10479 9361 8857 -2464 -1961 -1023 C ATOM 1059 CD2 LEU A 143 -3.117 -2.322 -34.966 1.00 65.20 C ANISOU 1059 CD2 LEU A 143 9027 8374 7372 -2748 -2255 -1014 C ATOM 1060 N VAL A 144 -5.603 -6.516 -36.304 1.00 79.48 N ANISOU 1060 N VAL A 144 10519 10462 9218 -1890 -1783 -750 N ATOM 1061 CA VAL A 144 -5.047 -7.559 -37.161 1.00 78.21 C ANISOU 1061 CA VAL A 144 10128 10429 9161 -1811 -1726 -570 C ATOM 1062 C VAL A 144 -6.057 -7.973 -38.225 1.00 78.06 C ANISOU 1062 C VAL A 144 10125 10318 9216 -1617 -1556 -556 C ATOM 1063 O VAL A 144 -5.694 -8.225 -39.381 1.00 85.82 O ANISOU 1063 O VAL A 144 10986 11306 10316 -1583 -1491 -445 O ATOM 1064 CB VAL A 144 -4.591 -8.759 -36.311 1.00 77.61 C ANISOU 1064 CB VAL A 144 9915 10572 9003 -1769 -1777 -484 C ATOM 1065 CG1 VAL A 144 -4.048 -9.869 -37.199 1.00 72.67 C ANISOU 1065 CG1 VAL A 144 9069 10059 8484 -1666 -1700 -301 C ATOM 1066 CG2 VAL A 144 -3.545 -8.322 -35.297 1.00 73.72 C ANISOU 1066 CG2 VAL A 144 9390 10194 8428 -1973 -1961 -487 C ATOM 1067 N ALA A 145 -7.339 -8.046 -37.858 1.00 71.44 N ANISOU 1067 N ALA A 145 9435 9406 8304 -1489 -1483 -668 N ATOM 1068 CA ALA A 145 -8.360 -8.457 -38.816 1.00 74.20 C ANISOU 1068 CA ALA A 145 9794 9686 8713 -1314 -1334 -658 C ATOM 1069 C ALA A 145 -8.529 -7.427 -39.925 1.00 81.15 C ANISOU 1069 C ALA A 145 10736 10404 9692 -1338 -1287 -671 C ATOM 1070 O ALA A 145 -8.773 -7.788 -41.082 1.00101.33 O ANISOU 1070 O ALA A 145 13221 12947 12334 -1244 -1190 -600 O ATOM 1071 CB ALA A 145 -9.687 -8.697 -38.099 1.00 82.07 C ANISOU 1071 CB ALA A 145 10922 10653 9606 -1186 -1273 -766 C ATOM 1072 N LYS A 146 -8.403 -6.140 -39.595 1.00 76.63 N ANISOU 1072 N LYS A 146 10304 9704 9107 -1465 -1352 -762 N ATOM 1073 CA LYS A 146 -8.560 -5.103 -40.609 1.00 84.45 C ANISOU 1073 CA LYS A 146 11366 10526 10195 -1487 -1303 -765 C ATOM 1074 C LYS A 146 -7.358 -5.055 -41.545 1.00 76.41 C ANISOU 1074 C LYS A 146 10186 9552 9294 -1593 -1328 -623 C ATOM 1075 O LYS A 146 -7.514 -4.846 -42.753 1.00 71.72 O ANISOU 1075 O LYS A 146 9565 8893 8793 -1539 -1243 -558 O ATOM 1076 CB LYS A 146 -8.783 -3.745 -39.943 1.00 94.47 C ANISOU 1076 CB LYS A 146 12853 11622 11419 -1590 -1357 -907 C ATOM 1077 CG LYS A 146 -10.072 -3.658 -39.142 1.00 89.65 C ANISOU 1077 CG LYS A 146 12417 10948 10696 -1461 -1304 -1047 C ATOM 1078 CD LYS A 146 -10.269 -2.271 -38.552 1.00 85.55 C ANISOU 1078 CD LYS A 146 12134 10237 10136 -1551 -1341 -1192 C ATOM 1079 CE LYS A 146 -11.570 -2.187 -37.769 1.00 94.53 C ANISOU 1079 CE LYS A 146 13441 11318 11156 -1400 -1270 -1324 C ATOM 1080 NZ LYS A 146 -11.783 -0.833 -37.187 1.00101.09 N ANISOU 1080 NZ LYS A 146 14524 11944 11940 -1470 -1290 -1476 N ATOM 1081 N VAL A 147 -6.151 -5.246 -41.006 1.00 69.20 N ANISOU 1081 N VAL A 147 9155 8763 8373 -1742 -1443 -563 N ATOM 1082 CA VAL A 147 -4.964 -5.285 -41.855 1.00 72.05 C ANISOU 1082 CA VAL A 147 9335 9195 8846 -1835 -1460 -409 C ATOM 1083 C VAL A 147 -4.958 -6.547 -42.709 1.00 72.80 C ANISOU 1083 C VAL A 147 9261 9414 8986 -1671 -1355 -283 C ATOM 1084 O VAL A 147 -4.470 -6.534 -43.846 1.00 74.02 O ANISOU 1084 O VAL A 147 9310 9575 9239 -1666 -1297 -169 O ATOM 1085 CB VAL A 147 -3.691 -5.168 -40.996 1.00 75.22 C ANISOU 1085 CB VAL A 147 9640 9718 9223 -2037 -1617 -371 C ATOM 1086 CG1 VAL A 147 -2.443 -5.304 -41.855 1.00 79.05 C ANISOU 1086 CG1 VAL A 147 9906 10305 9825 -2121 -1626 -190 C ATOM 1087 CG2 VAL A 147 -3.677 -3.840 -40.255 1.00 75.98 C ANISOU 1087 CG2 VAL A 147 9925 9667 9277 -2221 -1722 -509 C ATOM 1088 N THR A 148 -5.503 -7.649 -42.190 1.00 72.72 N ANISOU 1088 N THR A 148 9232 9497 8902 -1535 -1322 -302 N ATOM 1089 CA THR A 148 -5.623 -8.859 -42.996 1.00 85.41 C ANISOU 1089 CA THR A 148 10713 11191 10547 -1375 -1212 -205 C ATOM 1090 C THR A 148 -6.534 -8.629 -44.196 1.00 78.56 C ANISOU 1090 C THR A 148 9915 10205 9729 -1263 -1090 -225 C ATOM 1091 O THR A 148 -6.245 -9.096 -45.304 1.00 83.19 O ANISOU 1091 O THR A 148 10396 10829 10383 -1199 -1010 -124 O ATOM 1092 CB THR A 148 -6.145 -10.013 -42.138 1.00 93.03 C ANISOU 1092 CB THR A 148 11673 12249 11424 -1261 -1198 -232 C ATOM 1093 OG1 THR A 148 -5.180 -10.334 -41.127 1.00 94.83 O ANISOU 1093 OG1 THR A 148 11807 12618 11606 -1353 -1310 -181 O ATOM 1094 CG2 THR A 148 -6.405 -11.248 -42.991 1.00 95.93 C ANISOU 1094 CG2 THR A 148 11946 12671 11832 -1097 -1075 -153 C ATOM 1095 N CYS A 149 -7.628 -7.889 -43.999 1.00 77.59 N ANISOU 1095 N CYS A 149 9969 9944 9567 -1232 -1072 -349 N ATOM 1096 CA CYS A 149 -8.581 -7.676 -45.083 1.00 79.81 C ANISOU 1096 CA CYS A 149 10311 10130 9884 -1116 -963 -362 C ATOM 1097 C CYS A 149 -8.006 -6.771 -46.167 1.00 75.72 C ANISOU 1097 C CYS A 149 9774 9536 9459 -1189 -948 -288 C ATOM 1098 O CYS A 149 -8.194 -7.033 -47.361 1.00 91.10 O ANISOU 1098 O CYS A 149 11671 11491 11451 -1100 -858 -220 O ATOM 1099 CB CYS A 149 -9.883 -7.097 -44.531 1.00 86.52 C ANISOU 1099 CB CYS A 149 11343 10864 10668 -1054 -945 -500 C ATOM 1100 SG CYS A 149 -10.826 -8.247 -43.504 1.00 91.25 S ANISOU 1100 SG CYS A 149 11958 11553 11160 -932 -924 -571 S ATOM 1101 N ILE A 150 -7.304 -5.703 -45.777 1.00 69.45 N ANISOU 1101 N ILE A 150 9026 8670 8692 -1356 -1034 -297 N ATOM 1102 CA ILE A 150 -6.760 -4.791 -46.780 1.00 85.44 C ANISOU 1102 CA ILE A 150 11038 10612 10812 -1437 -1015 -217 C ATOM 1103 C ILE A 150 -5.659 -5.468 -47.587 1.00 95.05 C ANISOU 1103 C ILE A 150 12048 11972 12096 -1453 -991 -56 C ATOM 1104 O ILE A 150 -5.445 -5.133 -48.758 1.00111.21 O ANISOU 1104 O ILE A 150 14055 13988 14211 -1441 -923 36 O ATOM 1105 CB ILE A 150 -6.265 -3.486 -46.125 1.00 83.46 C ANISOU 1105 CB ILE A 150 10896 10236 10580 -1632 -1116 -271 C ATOM 1106 CG1 ILE A 150 -5.101 -3.758 -45.173 1.00101.78 C ANISOU 1106 CG1 ILE A 150 13109 12682 12880 -1794 -1244 -246 C ATOM 1107 CG2 ILE A 150 -7.406 -2.790 -45.397 1.00 74.25 C ANISOU 1107 CG2 ILE A 150 9954 8912 9344 -1589 -1117 -434 C ATOM 1108 CD1 ILE A 150 -4.546 -2.513 -44.515 1.00118.44 C ANISOU 1108 CD1 ILE A 150 15323 14676 15002 -2015 -1358 -307 C ATOM 1109 N ILE A 151 -4.947 -6.426 -46.989 1.00 84.05 N ANISOU 1109 N ILE A 151 10518 10738 10678 -1469 -1037 -10 N ATOM 1110 CA ILE A 151 -4.006 -7.229 -47.762 1.00 82.92 C ANISOU 1110 CA ILE A 151 10177 10739 10591 -1439 -989 145 C ATOM 1111 C ILE A 151 -4.759 -8.148 -48.715 1.00 84.06 C ANISOU 1111 C ILE A 151 10311 10906 10722 -1240 -855 158 C ATOM 1112 O ILE A 151 -4.349 -8.347 -49.865 1.00 86.94 O ANISOU 1112 O ILE A 151 10585 11309 11138 -1194 -773 264 O ATOM 1113 CB ILE A 151 -3.076 -8.019 -46.822 1.00 73.68 C ANISOU 1113 CB ILE A 151 8864 9734 9396 -1491 -1071 199 C ATOM 1114 CG1 ILE A 151 -2.146 -7.068 -46.067 1.00 79.48 C ANISOU 1114 CG1 ILE A 151 9581 10469 10149 -1718 -1213 208 C ATOM 1115 CG2 ILE A 151 -2.267 -9.046 -47.600 1.00 69.96 C ANISOU 1115 CG2 ILE A 151 8197 9412 8974 -1406 -992 355 C ATOM 1116 CD1 ILE A 151 -1.159 -7.772 -45.161 1.00 84.65 C ANISOU 1116 CD1 ILE A 151 10076 11311 10775 -1780 -1308 280 C ATOM 1117 N ILE A 152 -5.880 -8.711 -48.257 1.00 82.65 N ANISOU 1117 N ILE A 152 10226 10706 10470 -1125 -832 50 N ATOM 1118 CA ILE A 152 -6.696 -9.562 -49.118 1.00 79.50 C ANISOU 1118 CA ILE A 152 9831 10323 10054 -956 -717 45 C ATOM 1119 C ILE A 152 -7.253 -8.759 -50.287 1.00 72.73 C ANISOU 1119 C ILE A 152 9045 9365 9223 -923 -652 48 C ATOM 1120 O ILE A 152 -7.342 -9.260 -51.415 1.00 71.26 O ANISOU 1120 O ILE A 152 8811 9218 9046 -829 -560 104 O ATOM 1121 CB ILE A 152 -7.812 -10.235 -48.296 1.00 71.35 C ANISOU 1121 CB ILE A 152 8882 9286 8942 -865 -714 -69 C ATOM 1122 CG1 ILE A 152 -7.216 -11.297 -47.369 1.00 71.49 C ANISOU 1122 CG1 ILE A 152 8806 9425 8933 -864 -752 -37 C ATOM 1123 CG2 ILE A 152 -8.867 -10.848 -49.204 1.00 72.44 C ANISOU 1123 CG2 ILE A 152 9053 9411 9060 -719 -610 -96 C ATOM 1124 CD1 ILE A 152 -8.233 -11.990 -46.495 1.00 66.21 C ANISOU 1124 CD1 ILE A 152 8211 8759 8187 -784 -747 -132 C ATOM 1125 N TRP A 153 -7.624 -7.498 -50.044 1.00 75.87 N ANISOU 1125 N TRP A 153 9566 9631 9629 -995 -695 -9 N ATOM 1126 CA TRP A 153 -8.077 -6.648 -51.141 1.00 81.34 C ANISOU 1126 CA TRP A 153 10324 10227 10353 -963 -634 16 C ATOM 1127 C TRP A 153 -6.963 -6.419 -52.155 1.00 80.77 C ANISOU 1127 C TRP A 153 10138 10196 10354 -1022 -602 162 C ATOM 1128 O TRP A 153 -7.213 -6.378 -53.365 1.00 79.35 O ANISOU 1128 O TRP A 153 9951 10016 10183 -942 -517 221 O ATOM 1129 CB TRP A 153 -8.589 -5.306 -50.611 1.00 81.15 C ANISOU 1129 CB TRP A 153 10463 10037 10335 -1030 -682 -65 C ATOM 1130 CG TRP A 153 -9.724 -5.381 -49.622 1.00 88.91 C ANISOU 1130 CG TRP A 153 11566 10973 11241 -963 -701 -205 C ATOM 1131 CD1 TRP A 153 -9.812 -4.713 -48.435 1.00109.81 C ANISOU 1131 CD1 TRP A 153 14327 13534 13861 -1045 -776 -303 C ATOM 1132 CD2 TRP A 153 -10.931 -6.149 -49.738 1.00 88.04 C ANISOU 1132 CD2 TRP A 153 11477 10904 11070 -804 -640 -261 C ATOM 1133 NE1 TRP A 153 -10.991 -5.020 -47.803 1.00115.96 N ANISOU 1133 NE1 TRP A 153 15192 14303 14563 -934 -756 -410 N ATOM 1134 CE2 TRP A 153 -11.696 -5.899 -48.581 1.00102.65 C ANISOU 1134 CE2 TRP A 153 13443 12696 12862 -791 -675 -381 C ATOM 1135 CE3 TRP A 153 -11.438 -7.026 -50.703 1.00 98.30 C ANISOU 1135 CE3 TRP A 153 12710 12286 12354 -681 -560 -224 C ATOM 1136 CZ2 TRP A 153 -12.937 -6.492 -48.365 1.00106.28 C ANISOU 1136 CZ2 TRP A 153 13937 13186 13259 -658 -629 -449 C ATOM 1137 CZ3 TRP A 153 -12.670 -7.613 -50.485 1.00105.92 C ANISOU 1137 CZ3 TRP A 153 13713 13274 13256 -565 -527 -301 C ATOM 1138 CH2 TRP A 153 -13.406 -7.344 -49.326 1.00102.31 C ANISOU 1138 CH2 TRP A 153 13354 12765 12752 -554 -559 -405 C ATOM 1139 N LEU A 154 -5.725 -6.267 -51.679 1.00 76.43 N ANISOU 1139 N LEU A 154 9493 9695 9853 -1164 -669 229 N ATOM 1140 CA LEU A 154 -4.610 -6.032 -52.592 1.00 71.61 C ANISOU 1140 CA LEU A 154 8756 9136 9317 -1227 -635 383 C ATOM 1141 C LEU A 154 -4.225 -7.304 -53.337 1.00 79.65 C ANISOU 1141 C LEU A 154 9634 10308 10323 -1105 -544 469 C ATOM 1142 O LEU A 154 -3.955 -7.263 -54.543 1.00 91.38 O ANISOU 1142 O LEU A 154 11067 11821 11833 -1058 -455 568 O ATOM 1143 CB LEU A 154 -3.411 -5.473 -51.826 1.00 67.14 C ANISOU 1143 CB LEU A 154 8116 8587 8808 -1428 -742 434 C ATOM 1144 CG LEU A 154 -3.579 -4.069 -51.242 1.00 80.20 C ANISOU 1144 CG LEU A 154 9917 10067 10486 -1580 -826 360 C ATOM 1145 CD1 LEU A 154 -2.285 -3.598 -50.594 1.00 86.08 C ANISOU 1145 CD1 LEU A 154 10567 10852 11287 -1801 -938 421 C ATOM 1146 CD2 LEU A 154 -4.035 -3.090 -52.313 1.00 77.85 C ANISOU 1146 CD2 LEU A 154 9717 9629 10234 -1557 -750 396 C ATOM 1147 N LEU A 155 -4.191 -8.442 -52.640 1.00 81.34 N ANISOU 1147 N LEU A 155 9793 10619 10496 -1046 -559 435 N ATOM 1148 CA LEU A 155 -3.852 -9.697 -53.302 1.00 79.70 C ANISOU 1148 CA LEU A 155 9472 10535 10276 -919 -463 506 C ATOM 1149 C LEU A 155 -4.925 -10.113 -54.301 1.00 79.76 C ANISOU 1149 C LEU A 155 9564 10510 10230 -768 -361 453 C ATOM 1150 O LEU A 155 -4.607 -10.716 -55.332 1.00 89.67 O ANISOU 1150 O LEU A 155 10755 11835 11482 -680 -261 526 O ATOM 1151 CB LEU A 155 -3.632 -10.800 -52.267 1.00 80.67 C ANISOU 1151 CB LEU A 155 9533 10748 10369 -887 -500 483 C ATOM 1152 CG LEU A 155 -2.449 -10.608 -51.315 1.00 78.43 C ANISOU 1152 CG LEU A 155 9131 10544 10126 -1025 -603 557 C ATOM 1153 CD1 LEU A 155 -2.271 -11.827 -50.423 1.00 74.85 C ANISOU 1153 CD1 LEU A 155 8611 10194 9635 -958 -621 556 C ATOM 1154 CD2 LEU A 155 -1.173 -10.313 -52.090 1.00 70.16 C ANISOU 1154 CD2 LEU A 155 7924 9577 9155 -1086 -571 725 C ATOM 1155 N ALA A 156 -6.192 -9.805 -54.017 1.00 77.38 N ANISOU 1155 N ALA A 156 9406 10113 9881 -736 -384 328 N ATOM 1156 CA ALA A 156 -7.252 -10.102 -54.974 1.00 85.00 C ANISOU 1156 CA ALA A 156 10444 11061 10793 -609 -303 283 C ATOM 1157 C ALA A 156 -7.202 -9.148 -56.161 1.00 86.31 C ANISOU 1157 C ALA A 156 10629 11185 10979 -616 -256 357 C ATOM 1158 O ALA A 156 -7.391 -9.566 -57.309 1.00 92.07 O ANISOU 1158 O ALA A 156 11346 11964 11672 -521 -169 392 O ATOM 1159 CB ALA A 156 -8.616 -10.039 -54.289 1.00 89.52 C ANISOU 1159 CB ALA A 156 11140 11561 11312 -571 -341 145 C ATOM 1160 N GLY A 157 -6.950 -7.863 -55.903 1.00 77.44 N ANISOU 1160 N GLY A 157 9546 9969 9910 -729 -312 383 N ATOM 1161 CA GLY A 157 -6.796 -6.918 -56.997 1.00 74.28 C ANISOU 1161 CA GLY A 157 9160 9523 9541 -743 -264 477 C ATOM 1162 C GLY A 157 -5.568 -7.206 -57.839 1.00 84.33 C ANISOU 1162 C GLY A 157 10291 10901 10849 -758 -199 626 C ATOM 1163 O GLY A 157 -5.585 -7.028 -59.060 1.00 97.98 O ANISOU 1163 O GLY A 157 12014 12652 12561 -698 -115 704 O ATOM 1164 N LEU A 158 -4.484 -7.652 -57.199 1.00 74.06 N ANISOU 1164 N LEU A 158 8869 9678 9593 -831 -233 675 N ATOM 1165 CA LEU A 158 -3.301 -8.066 -57.945 1.00 75.00 C ANISOU 1165 CA LEU A 158 8833 9918 9744 -824 -158 824 C ATOM 1166 C LEU A 158 -3.579 -9.309 -58.781 1.00 77.74 C ANISOU 1166 C LEU A 158 9162 10360 10017 -651 -47 815 C ATOM 1167 O LEU A 158 -3.016 -9.461 -59.872 1.00 88.74 O ANISOU 1167 O LEU A 158 10486 11828 11405 -597 53 924 O ATOM 1168 CB LEU A 158 -2.138 -8.319 -56.986 1.00 73.18 C ANISOU 1168 CB LEU A 158 8465 9765 9574 -931 -227 882 C ATOM 1169 CG LEU A 158 -0.800 -8.741 -57.597 1.00 86.87 C ANISOU 1169 CG LEU A 158 10011 11642 11354 -926 -153 1053 C ATOM 1170 CD1 LEU A 158 -0.222 -7.623 -58.451 1.00 99.76 C ANISOU 1170 CD1 LEU A 158 11606 13250 13049 -1019 -120 1186 C ATOM 1171 CD2 LEU A 158 0.180 -9.156 -56.511 1.00 84.65 C ANISOU 1171 CD2 LEU A 158 9589 11458 11118 -1010 -233 1100 C ATOM 1172 N ALA A 159 -4.444 -10.200 -58.293 1.00 63.96 N ANISOU 1172 N ALA A 159 7483 8611 8209 -565 -58 686 N ATOM 1173 CA ALA A 159 -4.791 -11.395 -59.053 1.00 65.97 C ANISOU 1173 CA ALA A 159 7744 8932 8390 -415 42 656 C ATOM 1174 C ALA A 159 -5.736 -11.072 -60.204 1.00 80.98 C ANISOU 1174 C ALA A 159 9745 10804 10220 -342 96 626 C ATOM 1175 O ALA A 159 -5.637 -11.672 -61.279 1.00 76.36 O ANISOU 1175 O ALA A 159 9147 10289 9578 -245 197 657 O ATOM 1176 CB ALA A 159 -5.411 -12.442 -58.128 1.00 51.90 C ANISOU 1176 CB ALA A 159 6001 7147 6573 -366 9 535 C ATOM 1177 N SER A 160 -6.657 -10.132 -59.997 1.00 89.93 N ANISOU 1177 N SER A 160 10982 11840 11349 -380 33 566 N ATOM 1178 CA SER A 160 -7.559 -9.683 -61.050 1.00 98.46 C ANISOU 1178 CA SER A 160 12146 12901 12364 -313 72 557 C ATOM 1179 C SER A 160 -6.934 -8.621 -61.945 1.00 98.89 C ANISOU 1179 C SER A 160 12174 12946 12453 -353 113 699 C ATOM 1180 O SER A 160 -7.638 -8.039 -62.776 1.00 86.32 O ANISOU 1180 O SER A 160 10653 11332 10813 -305 137 714 O ATOM 1181 CB SER A 160 -8.857 -9.147 -60.440 1.00104.58 C ANISOU 1181 CB SER A 160 13036 13580 13120 -315 -2 446 C ATOM 1182 OG SER A 160 -8.617 -7.976 -59.678 1.00115.73 O ANISOU 1182 OG SER A 160 14474 14885 14611 -424 -72 466 O ATOM 1183 N LEU A 161 -5.637 -8.359 -61.787 1.00102.72 N ANISOU 1183 N LEU A 161 12552 13456 13020 -441 119 813 N ATOM 1184 CA LEU A 161 -4.978 -7.356 -62.618 1.00101.53 C ANISOU 1184 CA LEU A 161 12366 13297 12913 -493 164 964 C ATOM 1185 C LEU A 161 -4.967 -7.708 -64.103 1.00102.45 C ANISOU 1185 C LEU A 161 12471 13512 12944 -374 285 1037 C ATOM 1186 O LEU A 161 -5.206 -6.800 -64.920 1.00117.58 O ANISOU 1186 O LEU A 161 14433 15396 14848 -371 315 1114 O ATOM 1187 CB LEU A 161 -3.553 -7.118 -62.100 1.00 96.40 C ANISOU 1187 CB LEU A 161 11580 12676 12370 -622 143 1077 C ATOM 1188 CG LEU A 161 -2.852 -5.846 -62.580 1.00 91.02 C ANISOU 1188 CG LEU A 161 10865 11948 11770 -736 155 1229 C ATOM 1189 CD1 LEU A 161 -3.616 -4.614 -62.122 1.00 75.33 C ANISOU 1189 CD1 LEU A 161 9019 9784 9820 -817 74 1172 C ATOM 1190 CD2 LEU A 161 -1.416 -5.807 -62.082 1.00 95.60 C ANISOU 1190 CD2 LEU A 161 11283 12592 12451 -866 133 1343 C ATOM 1191 N PRO A 162 -4.699 -8.950 -64.529 1.00 92.70 N ANISOU 1191 N PRO A 162 11186 12392 11643 -273 363 1021 N ATOM 1192 CA PRO A 162 -4.797 -9.255 -65.966 1.00 84.85 C ANISOU 1192 CA PRO A 162 10208 11488 10543 -157 477 1070 C ATOM 1193 C PRO A 162 -6.200 -9.106 -66.525 1.00 81.74 C ANISOU 1193 C PRO A 162 9947 11069 10043 -85 459 978 C ATOM 1194 O PRO A 162 -6.346 -8.884 -67.733 1.00 92.61 O ANISOU 1194 O PRO A 162 11349 12504 11334 -18 531 1043 O ATOM 1195 CB PRO A 162 -4.310 -10.709 -66.054 1.00 87.59 C ANISOU 1195 CB PRO A 162 10501 11934 10845 -66 553 1035 C ATOM 1196 CG PRO A 162 -4.491 -11.254 -64.680 1.00 83.14 C ANISOU 1196 CG PRO A 162 9935 11319 10337 -108 463 926 C ATOM 1197 CD PRO A 162 -4.192 -10.109 -63.772 1.00 82.16 C ANISOU 1197 CD PRO A 162 9780 11112 10327 -255 361 974 C ATOM 1198 N ALA A 163 -7.237 -9.222 -65.692 1.00 89.27 N ANISOU 1198 N ALA A 163 10977 11950 10992 -93 368 837 N ATOM 1199 CA ALA A 163 -8.604 -8.995 -66.146 1.00102.60 C ANISOU 1199 CA ALA A 163 12771 13624 12589 -31 340 764 C ATOM 1200 C ALA A 163 -8.892 -7.521 -66.400 1.00108.56 C ANISOU 1200 C ALA A 163 13569 14298 13380 -67 315 854 C ATOM 1201 O ALA A 163 -9.948 -7.193 -66.948 1.00117.26 O ANISOU 1201 O ALA A 163 14744 15404 14405 -2 303 832 O ATOM 1202 CB ALA A 163 -9.594 -9.556 -65.123 1.00105.50 C ANISOU 1202 CB ALA A 163 13191 13945 12950 -30 258 601 C ATOM 1203 N ILE A 164 -7.980 -6.629 -66.015 1.00107.43 N ANISOU 1203 N ILE A 164 13382 14081 13355 -171 305 959 N ATOM 1204 CA ILE A 164 -8.103 -5.212 -66.317 1.00 98.93 C ANISOU 1204 CA ILE A 164 12354 12909 12327 -211 298 1062 C ATOM 1205 C ILE A 164 -7.248 -4.807 -67.514 1.00 99.59 C ANISOU 1205 C ILE A 164 12381 13059 12401 -205 396 1241 C ATOM 1206 O ILE A 164 -7.596 -3.849 -68.216 1.00101.12 O ANISOU 1206 O ILE A 164 12627 13212 12581 -184 419 1336 O ATOM 1207 CB ILE A 164 -7.749 -4.356 -65.080 1.00 90.60 C ANISOU 1207 CB ILE A 164 11312 11701 11410 -351 215 1054 C ATOM 1208 CG1 ILE A 164 -8.317 -5.008 -63.816 1.00107.74 C ANISOU 1208 CG1 ILE A 164 13512 13841 13582 -359 132 883 C ATOM 1209 CG2 ILE A 164 -8.278 -2.940 -65.235 1.00 81.86 C ANISOU 1209 CG2 ILE A 164 10304 10454 10345 -371 199 1113 C ATOM 1210 CD1 ILE A 164 -7.923 -4.313 -62.537 1.00121.09 C ANISOU 1210 CD1 ILE A 164 15221 15402 15385 -497 47 855 C ATOM 1211 N ILE A 165 -6.160 -5.522 -67.780 1.00 96.03 N ANISOU 1211 N ILE A 165 11822 12714 11953 -210 464 1299 N ATOM 1212 CA ILE A 165 -5.215 -5.137 -68.822 1.00 93.32 C ANISOU 1212 CA ILE A 165 11406 12442 11610 -212 568 1483 C ATOM 1213 C ILE A 165 -5.579 -5.761 -70.161 1.00 99.85 C ANISOU 1213 C ILE A 165 12259 13410 12272 -63 663 1495 C ATOM 1214 O ILE A 165 -5.587 -5.081 -71.190 1.00 99.92 O ANISOU 1214 O ILE A 165 12286 13447 12232 -28 726 1623 O ATOM 1215 CB ILE A 165 -3.779 -5.520 -68.396 1.00 89.78 C ANISOU 1215 CB ILE A 165 10811 12047 11256 -292 598 1560 C ATOM 1216 CG1 ILE A 165 -3.410 -4.845 -67.076 1.00 94.02 C ANISOU 1216 CG1 ILE A 165 11325 12454 11943 -459 488 1546 C ATOM 1217 CG2 ILE A 165 -2.761 -5.173 -69.492 1.00 92.47 C ANISOU 1217 CG2 ILE A 165 11058 12479 11598 -289 720 1763 C ATOM 1218 CD1 ILE A 165 -3.388 -3.334 -67.146 1.00104.32 C ANISOU 1218 CD1 ILE A 165 12679 13623 13336 -568 462 1650 C ATOM 1219 N HIS A 166 -5.891 -7.059 -70.164 1.00 97.44 N ANISOU 1219 N HIS A 166 11963 13188 11871 23 676 1362 N ATOM 1220 CA HIS A 166 -6.086 -7.809 -71.397 1.00 90.88 C ANISOU 1220 CA HIS A 166 11160 12497 10874 152 771 1354 C ATOM 1221 C HIS A 166 -7.549 -7.965 -71.795 1.00 86.82 C ANISOU 1221 C HIS A 166 10763 11999 10227 228 719 1236 C ATOM 1222 O HIS A 166 -7.824 -8.469 -72.890 1.00 89.10 O ANISOU 1222 O HIS A 166 11090 12405 10357 325 783 1226 O ATOM 1223 CB HIS A 166 -5.436 -9.192 -71.272 1.00 89.10 C ANISOU 1223 CB HIS A 166 10881 12352 10621 202 835 1287 C ATOM 1224 CG HIS A 166 -3.966 -9.144 -70.995 1.00 96.35 C ANISOU 1224 CG HIS A 166 11660 13293 11656 147 896 1422 C ATOM 1225 ND1 HIS A 166 -3.446 -8.782 -69.770 1.00102.27 N ANISOU 1225 ND1 HIS A 166 12335 13957 12565 24 816 1439 N ATOM 1226 CD2 HIS A 166 -2.902 -9.405 -71.791 1.00104.60 C ANISOU 1226 CD2 HIS A 166 12618 14450 12675 200 1031 1552 C ATOM 1227 CE1 HIS A 166 -2.127 -8.827 -69.823 1.00105.07 C ANISOU 1227 CE1 HIS A 166 12551 14377 12992 -5 889 1578 C ATOM 1228 NE2 HIS A 166 -1.772 -9.202 -71.038 1.00105.01 N ANISOU 1228 NE2 HIS A 166 12530 14489 12879 106 1026 1654 N ATOM 1229 N ARG A 167 -8.488 -7.560 -70.944 1.00 78.80 N ANISOU 1229 N ARG A 167 9801 10877 9262 188 607 1147 N ATOM 1230 CA ARG A 167 -9.910 -7.635 -71.275 1.00 74.54 C ANISOU 1230 CA ARG A 167 9351 10364 8607 256 551 1051 C ATOM 1231 C ARG A 167 -10.270 -6.445 -72.155 1.00 84.97 C ANISOU 1231 C ARG A 167 10706 11690 9888 290 566 1191 C ATOM 1232 O ARG A 167 -10.432 -5.324 -71.670 1.00 86.55 O ANISOU 1232 O ARG A 167 10925 11766 10194 240 521 1256 O ATOM 1233 CB ARG A 167 -10.759 -7.658 -70.010 1.00 89.62 C ANISOU 1233 CB ARG A 167 11294 12169 10588 213 440 917 C ATOM 1234 CG ARG A 167 -11.218 -9.041 -69.587 1.00 89.60 C ANISOU 1234 CG ARG A 167 11303 12211 10529 235 415 744 C ATOM 1235 CD ARG A 167 -12.410 -9.512 -70.405 1.00 64.22 C ANISOU 1235 CD ARG A 167 8149 9098 7153 313 397 664 C ATOM 1236 NE ARG A 167 -12.917 -10.797 -69.929 1.00 74.02 N ANISOU 1236 NE ARG A 167 9410 10360 8355 314 368 495 N ATOM 1237 CZ ARG A 167 -14.091 -11.313 -70.276 1.00 77.20 C ANISOU 1237 CZ ARG A 167 9859 10831 8642 347 322 391 C ATOM 1238 NH1 ARG A 167 -14.892 -10.652 -71.100 1.00 74.54 N ANISOU 1238 NH1 ARG A 167 9546 10565 8210 392 296 442 N ATOM 1239 NH2 ARG A 167 -14.468 -12.488 -69.793 1.00 81.48 N ANISOU 1239 NH2 ARG A 167 10418 11375 9165 331 301 244 N ATOM 1240 N ASN A 168 -10.401 -6.686 -73.455 1.00 92.81 N ANISOU 1240 N ASN A 168 11718 12824 10723 377 631 1239 N ATOM 1241 CA ASN A 168 -10.765 -5.652 -74.410 1.00 85.25 C ANISOU 1241 CA ASN A 168 10792 11897 9701 428 651 1385 C ATOM 1242 C ASN A 168 -12.002 -6.077 -75.189 1.00 76.41 C ANISOU 1242 C ASN A 168 9733 10908 8393 524 614 1308 C ATOM 1243 O ASN A 168 -12.401 -7.245 -75.187 1.00 66.12 O ANISOU 1243 O ASN A 168 8446 9682 6993 544 593 1150 O ATOM 1244 CB ASN A 168 -9.607 -5.349 -75.371 1.00 90.62 C ANISOU 1244 CB ASN A 168 11426 12646 10359 440 776 1564 C ATOM 1245 CG ASN A 168 -8.476 -4.595 -74.700 1.00105.90 C ANISOU 1245 CG ASN A 168 13293 14454 12492 328 801 1683 C ATOM 1246 OD1 ASN A 168 -8.489 -3.366 -74.633 1.00109.28 O ANISOU 1246 OD1 ASN A 168 13736 14774 13011 285 788 1809 O ATOM 1247 ND2 ASN A 168 -7.489 -5.330 -74.201 1.00112.75 N ANISOU 1247 ND2 ASN A 168 14083 15331 13425 279 836 1649 N ATOM 1248 N VAL A 169 -12.610 -5.104 -75.859 1.00 81.88 N ANISOU 1248 N VAL A 169 10457 11623 9031 578 603 1428 N ATOM 1249 CA VAL A 169 -13.786 -5.340 -76.687 1.00 85.55 C ANISOU 1249 CA VAL A 169 10963 12233 9308 668 559 1390 C ATOM 1250 C VAL A 169 -13.321 -5.629 -78.108 1.00 93.97 C ANISOU 1250 C VAL A 169 12038 13474 10194 734 652 1473 C ATOM 1251 O VAL A 169 -12.602 -4.825 -78.712 1.00 91.80 O ANISOU 1251 O VAL A 169 11748 13198 9935 749 735 1661 O ATOM 1252 CB VAL A 169 -14.742 -4.139 -76.649 1.00 78.93 C ANISOU 1252 CB VAL A 169 10150 11339 8500 711 499 1487 C ATOM 1253 CG1 VAL A 169 -15.795 -4.267 -77.732 1.00 87.63 C ANISOU 1253 CG1 VAL A 169 11274 12631 9390 811 463 1500 C ATOM 1254 CG2 VAL A 169 -15.398 -4.034 -75.282 1.00 71.15 C ANISOU 1254 CG2 VAL A 169 9171 10210 7654 666 407 1371 C ATOM 1255 N PHE A 170 -13.726 -6.779 -78.640 1.00 93.73 N ANISOU 1255 N PHE A 170 12037 13589 9987 768 642 1333 N ATOM 1256 CA PHE A 170 -13.323 -7.215 -79.967 1.00 78.44 C ANISOU 1256 CA PHE A 170 10126 11826 7850 835 731 1375 C ATOM 1257 C PHE A 170 -14.530 -7.280 -80.893 1.00 80.86 C ANISOU 1257 C PHE A 170 10481 12304 7938 902 661 1350 C ATOM 1258 O PHE A 170 -15.661 -7.513 -80.456 1.00 74.85 O ANISOU 1258 O PHE A 170 9727 11550 7162 888 543 1233 O ATOM 1259 CB PHE A 170 -12.637 -8.586 -79.918 1.00 60.19 C ANISOU 1259 CB PHE A 170 7827 9544 5497 820 796 1226 C ATOM 1260 CG PHE A 170 -11.374 -8.603 -79.106 1.00 74.81 C ANISOU 1260 CG PHE A 170 9614 11265 7544 764 870 1267 C ATOM 1261 CD1 PHE A 170 -10.166 -8.229 -79.671 1.00 72.05 C ANISOU 1261 CD1 PHE A 170 9221 10944 7211 785 1001 1435 C ATOM 1262 CD2 PHE A 170 -11.393 -8.996 -77.778 1.00 71.75 C ANISOU 1262 CD2 PHE A 170 9201 10741 7320 689 808 1147 C ATOM 1263 CE1 PHE A 170 -9.001 -8.245 -78.927 1.00 68.90 C ANISOU 1263 CE1 PHE A 170 8742 10445 6991 727 1060 1483 C ATOM 1264 CE2 PHE A 170 -10.231 -9.015 -77.029 1.00 71.19 C ANISOU 1264 CE2 PHE A 170 9060 10569 7418 635 864 1191 C ATOM 1265 CZ PHE A 170 -9.034 -8.639 -77.605 1.00 72.00 C ANISOU 1265 CZ PHE A 170 9109 10709 7540 651 986 1360 C ATOM 1266 N PHE A 171 -14.274 -7.069 -82.181 1.00 88.67 N ANISOU 1266 N PHE A 171 11494 13445 8750 976 734 1470 N ATOM 1267 CA PHE A 171 -15.290 -7.150 -83.225 1.00 84.84 C ANISOU 1267 CA PHE A 171 11052 13160 8023 1042 673 1463 C ATOM 1268 C PHE A 171 -15.052 -8.434 -84.011 1.00 80.76 C ANISOU 1268 C PHE A 171 10601 12792 7293 1057 722 1315 C ATOM 1269 O PHE A 171 -14.122 -8.510 -84.821 1.00 90.86 O ANISOU 1269 O PHE A 171 11902 14143 8479 1105 852 1398 O ATOM 1270 CB PHE A 171 -15.237 -5.923 -84.133 1.00 84.40 C ANISOU 1270 CB PHE A 171 10988 13176 7904 1122 717 1716 C ATOM 1271 CG PHE A 171 -16.265 -5.931 -85.229 1.00 93.24 C ANISOU 1271 CG PHE A 171 12141 14522 8763 1198 648 1734 C ATOM 1272 CD1 PHE A 171 -17.552 -5.478 -84.992 1.00 97.21 C ANISOU 1272 CD1 PHE A 171 12621 15052 9264 1216 514 1739 C ATOM 1273 CD2 PHE A 171 -15.942 -6.381 -86.500 1.00 96.80 C ANISOU 1273 CD2 PHE A 171 12644 15171 8964 1254 719 1751 C ATOM 1274 CE1 PHE A 171 -18.500 -5.482 -85.997 1.00101.07 C ANISOU 1274 CE1 PHE A 171 13123 15770 9510 1282 439 1767 C ATOM 1275 CE2 PHE A 171 -16.886 -6.387 -87.510 1.00101.08 C ANISOU 1275 CE2 PHE A 171 13216 15938 9250 1315 644 1767 C ATOM 1276 CZ PHE A 171 -18.166 -5.936 -87.257 1.00104.12 C ANISOU 1276 CZ PHE A 171 13563 16357 9639 1326 498 1778 C ATOM 1277 N ILE A 172 -15.884 -9.440 -83.765 1.00 76.43 N ANISOU 1277 N ILE A 172 10089 12283 6667 1014 625 1097 N ATOM 1278 CA ILE A 172 -15.745 -10.733 -84.427 1.00 80.60 C ANISOU 1278 CA ILE A 172 10703 12923 6998 1015 664 924 C ATOM 1279 C ILE A 172 -16.203 -10.601 -85.874 1.00 82.52 C ANISOU 1279 C ILE A 172 11000 13402 6950 1084 655 980 C ATOM 1280 O ILE A 172 -17.371 -10.304 -86.142 1.00 85.09 O ANISOU 1280 O ILE A 172 11315 13843 7174 1084 524 983 O ATOM 1281 CB ILE A 172 -16.542 -11.820 -83.691 1.00 80.50 C ANISOU 1281 CB ILE A 172 10718 12866 7004 930 557 678 C ATOM 1282 CG1 ILE A 172 -16.043 -11.963 -82.251 1.00 76.59 C ANISOU 1282 CG1 ILE A 172 10170 12146 6784 869 571 633 C ATOM 1283 CG2 ILE A 172 -16.445 -13.146 -84.432 1.00 80.55 C ANISOU 1283 CG2 ILE A 172 10837 12972 6797 925 598 491 C ATOM 1284 CD1 ILE A 172 -16.789 -13.010 -81.450 1.00 83.28 C ANISOU 1284 CD1 ILE A 172 11040 12936 7667 785 478 409 C ATOM 1285 N GLU A 173 -15.281 -10.827 -86.812 1.00 88.29 N ANISOU 1285 N GLU A 173 11786 14221 7540 1148 796 1030 N ATOM 1286 CA GLU A 173 -15.600 -10.723 -88.230 1.00 80.75 C ANISOU 1286 CA GLU A 173 10892 13502 6285 1220 802 1087 C ATOM 1287 C GLU A 173 -16.417 -11.902 -88.742 1.00 78.72 C ANISOU 1287 C GLU A 173 10739 13384 5787 1181 715 844 C ATOM 1288 O GLU A 173 -17.101 -11.765 -89.761 1.00 80.14 O ANISOU 1288 O GLU A 173 10957 13777 5715 1213 650 868 O ATOM 1289 CB GLU A 173 -14.314 -10.600 -89.051 1.00 72.27 C ANISOU 1289 CB GLU A 173 9846 12479 5134 1305 996 1220 C ATOM 1290 N ASN A 174 -16.363 -13.050 -88.062 1.00 96.50 N ANISOU 1290 N ASN A 174 13038 15521 8107 1106 709 616 N ATOM 1291 CA ASN A 174 -17.110 -14.217 -88.523 1.00103.32 C ANISOU 1291 CA ASN A 174 14014 16492 8752 1049 630 372 C ATOM 1292 C ASN A 174 -18.613 -14.006 -88.391 1.00111.36 C ANISOU 1292 C ASN A 174 14983 17607 9722 978 421 331 C ATOM 1293 O ASN A 174 -19.381 -14.419 -89.267 1.00127.03 O ANISOU 1293 O ASN A 174 17034 19788 11445 954 332 237 O ATOM 1294 CB ASN A 174 -16.677 -15.461 -87.746 1.00108.61 C ANISOU 1294 CB ASN A 174 14745 16985 9535 987 682 154 C ATOM 1295 CG ASN A 174 -15.398 -16.071 -88.286 1.00111.87 C ANISOU 1295 CG ASN A 174 15252 17379 9874 1067 883 131 C ATOM 1296 OD1 ASN A 174 -14.370 -16.088 -87.609 1.00106.50 O ANISOU 1296 OD1 ASN A 174 14525 16541 9399 1096 1004 188 O ATOM 1297 ND2 ASN A 174 -15.459 -16.585 -89.509 1.00127.14 N ANISOU 1297 ND2 ASN A 174 17319 19484 11507 1106 920 49 N ATOM 1298 N THR A 175 -19.052 -13.367 -87.307 1.00111.15 N ANISOU 1298 N THR A 175 14838 17456 9939 945 341 401 N ATOM 1299 CA THR A 175 -20.472 -13.197 -87.036 1.00104.88 C ANISOU 1299 CA THR A 175 13978 16742 9130 885 153 367 C ATOM 1300 C THR A 175 -20.901 -11.743 -86.900 1.00107.34 C ANISOU 1300 C THR A 175 14171 17076 9537 955 104 612 C ATOM 1301 O THR A 175 -22.084 -11.490 -86.642 1.00114.73 O ANISOU 1301 O THR A 175 15033 18083 10475 927 -43 613 O ATOM 1302 CB THR A 175 -20.865 -13.960 -85.763 1.00100.19 C ANISOU 1302 CB THR A 175 13362 15978 8728 774 89 185 C ATOM 1303 OG1 THR A 175 -20.052 -13.518 -84.669 1.00105.36 O ANISOU 1303 OG1 THR A 175 13959 16404 9669 791 175 266 O ATOM 1304 CG2 THR A 175 -20.677 -15.457 -85.957 1.00107.21 C ANISOU 1304 CG2 THR A 175 14381 16852 9503 697 118 -69 C ATOM 1305 N ASN A 176 -19.985 -10.787 -87.070 1.00104.27 N ANISOU 1305 N ASN A 176 13761 16628 9230 1046 226 824 N ATOM 1306 CA ASN A 176 -20.293 -9.361 -86.933 1.00 98.49 C ANISOU 1306 CA ASN A 176 12936 15880 8605 1117 199 1066 C ATOM 1307 C ASN A 176 -20.908 -9.063 -85.568 1.00 97.14 C ANISOU 1307 C ASN A 176 12682 15540 8688 1068 114 1038 C ATOM 1308 O ASN A 176 -21.856 -8.284 -85.443 1.00 91.76 O ANISOU 1308 O ASN A 176 11928 14905 8029 1106 18 1143 O ATOM 1309 CB ASN A 176 -21.208 -8.883 -88.063 1.00 88.02 C ANISOU 1309 CB ASN A 176 11597 14817 7030 1184 109 1178 C ATOM 1310 N ILE A 177 -20.360 -9.694 -84.534 1.00101.75 N ANISOU 1310 N ILE A 177 13275 15928 9456 993 154 900 N ATOM 1311 CA ILE A 177 -20.869 -9.583 -83.172 1.00 94.56 C ANISOU 1311 CA ILE A 177 12301 14854 8774 938 83 843 C ATOM 1312 C ILE A 177 -19.786 -8.951 -82.309 1.00 90.44 C ANISOU 1312 C ILE A 177 11759 14100 8504 943 188 940 C ATOM 1313 O ILE A 177 -18.665 -9.471 -82.229 1.00 89.83 O ANISOU 1313 O ILE A 177 11719 13942 8470 919 296 895 O ATOM 1314 CB ILE A 177 -21.295 -10.947 -82.611 1.00 93.19 C ANISOU 1314 CB ILE A 177 12154 14661 8594 830 20 586 C ATOM 1315 CG1 ILE A 177 -22.449 -11.526 -83.432 1.00102.35 C ANISOU 1315 CG1 ILE A 177 13326 16053 9509 801 -104 489 C ATOM 1316 CG2 ILE A 177 -21.704 -10.815 -81.163 1.00 89.85 C ANISOU 1316 CG2 ILE A 177 11665 14064 8409 781 -34 542 C ATOM 1317 CD1 ILE A 177 -22.964 -12.852 -82.915 1.00103.89 C ANISOU 1317 CD1 ILE A 177 13549 16226 9697 678 -174 240 C ATOM 1318 N THR A 178 -20.122 -7.837 -81.663 1.00 95.56 N ANISOU 1318 N THR A 178 12349 14644 9316 973 158 1072 N ATOM 1319 CA THR A 178 -19.188 -7.105 -80.814 1.00 88.69 C ANISOU 1319 CA THR A 178 11463 13550 8685 962 239 1168 C ATOM 1320 C THR A 178 -19.230 -7.697 -79.409 1.00 93.54 C ANISOU 1320 C THR A 178 12061 14002 9479 874 201 1002 C ATOM 1321 O THR A 178 -20.254 -7.614 -78.724 1.00 89.97 O ANISOU 1321 O THR A 178 11575 13528 9080 863 104 946 O ATOM 1322 CB THR A 178 -19.536 -5.618 -80.796 1.00 76.76 C ANISOU 1322 CB THR A 178 9922 11985 7258 1035 229 1379 C ATOM 1323 OG1 THR A 178 -19.390 -5.075 -82.114 1.00 95.33 O ANISOU 1323 OG1 THR A 178 12291 14488 9444 1120 277 1552 O ATOM 1324 CG2 THR A 178 -18.626 -4.869 -79.842 1.00 66.96 C ANISOU 1324 CG2 THR A 178 8676 10500 6268 998 298 1456 C ATOM 1325 N VAL A 179 -18.118 -8.296 -78.981 1.00 95.39 N ANISOU 1325 N VAL A 179 12312 14131 9801 819 283 935 N ATOM 1326 CA VAL A 179 -18.020 -8.948 -77.683 1.00 80.12 C ANISOU 1326 CA VAL A 179 10366 12052 8025 739 258 785 C ATOM 1327 C VAL A 179 -16.782 -8.434 -76.959 1.00 86.69 C ANISOU 1327 C VAL A 179 11176 12707 9055 708 340 869 C ATOM 1328 O VAL A 179 -15.914 -7.781 -77.540 1.00 91.96 O ANISOU 1328 O VAL A 179 11840 13372 9728 737 426 1024 O ATOM 1329 CB VAL A 179 -17.959 -10.487 -77.798 1.00 65.33 C ANISOU 1329 CB VAL A 179 8534 10238 6051 693 263 587 C ATOM 1330 CG1 VAL A 179 -19.079 -11.010 -78.675 1.00 68.60 C ANISOU 1330 CG1 VAL A 179 8975 10843 6246 704 182 504 C ATOM 1331 CG2 VAL A 179 -16.603 -10.925 -78.334 1.00 52.87 C ANISOU 1331 CG2 VAL A 179 6987 8660 4441 709 397 610 C ATOM 1332 N ACYS A 180 -16.710 -8.752 -75.669 0.37 81.22 N ANISOU 1332 N ACYS A 180 10465 11873 8520 641 308 768 N ATOM 1333 N BCYS A 180 -16.719 -8.731 -75.663 0.63 80.82 N ANISOU 1333 N BCYS A 180 10414 11821 8471 642 307 770 N ATOM 1334 CA ACYS A 180 -15.550 -8.462 -74.838 0.37 78.11 C ANISOU 1334 CA ACYS A 180 10044 11323 8310 590 366 815 C ATOM 1335 CA BCYS A 180 -15.548 -8.463 -74.839 0.63 79.41 C ANISOU 1335 CA BCYS A 180 10209 11487 8475 590 366 815 C ATOM 1336 C ACYS A 180 -15.060 -9.766 -74.226 0.37 66.77 C ANISOU 1336 C ACYS A 180 8607 9857 6905 539 385 660 C ATOM 1337 C BCYS A 180 -15.065 -9.781 -74.254 0.63 66.68 C ANISOU 1337 C BCYS A 180 8596 9849 6889 540 386 660 C ATOM 1338 O ACYS A 180 -15.841 -10.493 -73.603 0.37 59.17 O ANISOU 1338 O ACYS A 180 7656 8886 5941 510 315 512 O ATOM 1339 O BCYS A 180 -15.859 -10.539 -73.687 0.63 57.33 O ANISOU 1339 O BCYS A 180 7425 8663 5694 514 317 509 O ATOM 1340 CB ACYS A 180 -15.893 -7.454 -73.740 0.37 82.05 C ANISOU 1340 CB ACYS A 180 10528 11666 8980 560 307 855 C ATOM 1341 CB BCYS A 180 -15.859 -7.456 -73.725 0.63 83.98 C ANISOU 1341 CB BCYS A 180 10773 11908 9229 558 308 856 C ATOM 1342 SG ACYS A 180 -14.497 -7.004 -72.697 0.37 79.86 S ANISOU 1342 SG ACYS A 180 10218 11204 8919 472 355 912 S ATOM 1343 SG BCYS A 180 -17.093 -7.991 -72.510 0.63 68.26 S ANISOU 1343 SG BCYS A 180 8782 9871 7285 528 195 678 S ATOM 1344 N ALA A 181 -13.774 -10.056 -74.401 1.00 57.88 N ANISOU 1344 N ALA A 181 7462 8719 5810 533 486 708 N ATOM 1345 CA ALA A 181 -13.216 -11.336 -73.983 1.00 65.63 C ANISOU 1345 CA ALA A 181 8446 9685 6807 511 526 583 C ATOM 1346 C ALA A 181 -11.697 -11.237 -73.952 1.00 76.37 C ANISOU 1346 C ALA A 181 9751 11010 8258 505 634 693 C ATOM 1347 O ALA A 181 -11.112 -10.194 -74.258 1.00 75.74 O ANISOU 1347 O ALA A 181 9632 10919 8228 504 673 860 O ATOM 1348 CB ALA A 181 -13.662 -12.454 -74.926 1.00 68.54 C ANISOU 1348 CB ALA A 181 8883 10182 6978 554 548 462 C ATOM 1349 N PHE A 182 -11.066 -12.342 -73.565 1.00 78.55 N ANISOU 1349 N PHE A 182 10018 11269 8559 502 685 607 N ATOM 1350 CA PHE A 182 -9.644 -12.546 -73.785 1.00 87.50 C ANISOU 1350 CA PHE A 182 11094 12418 9734 525 807 704 C ATOM 1351 C PHE A 182 -9.451 -13.203 -75.145 1.00 86.64 C ANISOU 1351 C PHE A 182 11043 12442 9436 618 915 694 C ATOM 1352 O PHE A 182 -10.212 -14.096 -75.528 1.00 91.62 O ANISOU 1352 O PHE A 182 11762 13119 9929 647 897 542 O ATOM 1353 CB PHE A 182 -9.035 -13.427 -72.692 1.00 89.00 C ANISOU 1353 CB PHE A 182 11242 12529 10043 495 817 631 C ATOM 1354 CG PHE A 182 -9.145 -12.852 -71.307 1.00 91.91 C ANISOU 1354 CG PHE A 182 11561 12778 10584 402 714 633 C ATOM 1355 CD1 PHE A 182 -8.186 -11.973 -70.830 1.00 98.79 C ANISOU 1355 CD1 PHE A 182 12341 13599 11596 344 722 776 C ATOM 1356 CD2 PHE A 182 -10.196 -13.204 -70.477 1.00 81.79 C ANISOU 1356 CD2 PHE A 182 10324 11435 9317 368 611 490 C ATOM 1357 CE1 PHE A 182 -8.279 -11.449 -69.554 1.00 92.98 C ANISOU 1357 CE1 PHE A 182 11574 12752 11002 252 624 764 C ATOM 1358 CE2 PHE A 182 -10.295 -12.683 -69.199 1.00 69.14 C ANISOU 1358 CE2 PHE A 182 8687 9727 7857 291 524 487 C ATOM 1359 CZ PHE A 182 -9.334 -11.806 -68.737 1.00 75.56 C ANISOU 1359 CZ PHE A 182 9423 10488 8798 233 528 617 C ATOM 1360 N HIS A 183 -8.436 -12.754 -75.876 1.00 68.50 N ANISOU 1360 N HIS A 183 8697 10205 7124 660 1028 854 N ATOM 1361 CA HIS A 183 -8.147 -13.274 -77.211 1.00 56.18 C ANISOU 1361 CA HIS A 183 7194 8780 5374 759 1148 863 C ATOM 1362 C HIS A 183 -6.945 -14.206 -77.112 1.00 61.03 C ANISOU 1362 C HIS A 183 7770 9396 6024 811 1283 863 C ATOM 1363 O HIS A 183 -5.801 -13.755 -77.018 1.00 70.14 O ANISOU 1363 O HIS A 183 8813 10553 7283 812 1365 1026 O ATOM 1364 CB HIS A 183 -7.894 -12.138 -78.196 1.00 73.57 C ANISOU 1364 CB HIS A 183 9371 11068 7515 788 1198 1056 C ATOM 1365 CG HIS A 183 -7.760 -12.593 -79.616 1.00 81.62 C ANISOU 1365 CG HIS A 183 10462 12242 8307 893 1311 1061 C ATOM 1366 ND1 HIS A 183 -7.106 -11.852 -80.577 1.00 78.74 N ANISOU 1366 ND1 HIS A 183 10064 11974 7881 944 1416 1254 N ATOM 1367 CD2 HIS A 183 -8.199 -13.713 -80.238 1.00 78.98 C ANISOU 1367 CD2 HIS A 183 10243 11982 7784 954 1338 893 C ATOM 1368 CE1 HIS A 183 -7.146 -12.498 -81.729 1.00 82.68 C ANISOU 1368 CE1 HIS A 183 10653 12610 8153 1041 1504 1205 C ATOM 1369 NE2 HIS A 183 -7.804 -13.629 -81.551 1.00 82.76 N ANISOU 1369 NE2 HIS A 183 10759 12604 8081 1045 1457 980 N ATOM 1370 N TYR A 184 -7.209 -15.514 -77.137 1.00 64.37 N ANISOU 1370 N TYR A 184 8281 9814 6361 855 1309 685 N ATOM 1371 CA TYR A 184 -6.152 -16.524 -77.071 1.00 83.49 C ANISOU 1371 CA TYR A 184 10685 12230 8806 930 1448 673 C ATOM 1372 C TYR A 184 -5.532 -16.663 -78.458 1.00 73.37 C ANISOU 1372 C TYR A 184 9443 11082 7354 1046 1610 745 C ATOM 1373 O TYR A 184 -5.798 -17.607 -79.207 1.00 89.51 O ANISOU 1373 O TYR A 184 11617 13170 9221 1122 1677 610 O ATOM 1374 CB TYR A 184 -6.701 -17.854 -76.569 1.00 94.84 C ANISOU 1374 CB TYR A 184 12222 13590 10222 934 1422 458 C ATOM 1375 CG TYR A 184 -7.206 -17.834 -75.142 1.00 89.57 C ANISOU 1375 CG TYR A 184 11512 12798 9723 831 1283 396 C ATOM 1376 CD1 TYR A 184 -6.903 -16.781 -74.288 1.00 79.11 C ANISOU 1376 CD1 TYR A 184 10061 11427 8569 753 1209 526 C ATOM 1377 CD2 TYR A 184 -7.981 -18.875 -74.648 1.00 97.09 C ANISOU 1377 CD2 TYR A 184 12557 13676 10657 809 1229 205 C ATOM 1378 CE1 TYR A 184 -7.363 -16.764 -72.984 1.00 83.13 C ANISOU 1378 CE1 TYR A 184 10542 11829 9214 666 1088 464 C ATOM 1379 CE2 TYR A 184 -8.444 -18.867 -73.346 1.00 92.84 C ANISOU 1379 CE2 TYR A 184 11979 13034 10263 723 1112 156 C ATOM 1380 CZ TYR A 184 -8.133 -17.810 -72.519 1.00 95.88 C ANISOU 1380 CZ TYR A 184 12243 13385 10804 657 1043 284 C ATOM 1381 OH TYR A 184 -8.593 -17.799 -71.222 1.00104.39 O ANISOU 1381 OH TYR A 184 13290 14365 12007 577 931 230 O ATOM 1382 N GLU A 185 -4.683 -15.696 -78.801 1.00 65.49 N ANISOU 1382 N GLU A 185 8333 10145 6406 1055 1678 961 N ATOM 1383 CA GLU A 185 -4.061 -15.678 -80.118 1.00 78.53 C ANISOU 1383 CA GLU A 185 10006 11936 7898 1166 1840 1060 C ATOM 1384 C GLU A 185 -3.163 -16.895 -80.307 1.00 92.33 C ANISOU 1384 C GLU A 185 11772 13702 9607 1288 2010 1013 C ATOM 1385 O GLU A 185 -2.493 -17.347 -79.374 1.00 96.79 O ANISOU 1385 O GLU A 185 12248 14189 10337 1284 2033 1025 O ATOM 1386 CB GLU A 185 -3.254 -14.393 -80.306 1.00 73.61 C ANISOU 1386 CB GLU A 185 9238 11361 7371 1137 1882 1320 C ATOM 1387 N SER A 186 -3.156 -17.428 -81.531 1.00102.37 N ANISOU 1387 N SER A 186 13165 15080 10653 1404 2134 962 N ATOM 1388 CA SER A 186 -2.362 -18.618 -81.818 1.00111.72 C ANISOU 1388 CA SER A 186 14397 16274 11777 1541 2315 905 C ATOM 1389 C SER A 186 -0.869 -18.331 -81.710 1.00104.01 C ANISOU 1389 C SER A 186 13237 15348 10933 1607 2468 1135 C ATOM 1390 O SER A 186 -0.110 -19.156 -81.189 1.00102.28 O ANISOU 1390 O SER A 186 12971 15081 10808 1679 2564 1127 O ATOM 1391 CB SER A 186 -2.711 -19.157 -83.205 1.00122.21 C ANISOU 1391 CB SER A 186 15911 17711 12814 1647 2412 796 C ATOM 1392 OG SER A 186 -2.639 -18.134 -84.183 1.00129.13 O ANISOU 1392 OG SER A 186 16757 18732 13575 1662 2443 958 O ATOM 1393 N GLN A 187 -0.429 -17.172 -82.196 1.00 91.89 N ANISOU 1393 N GLN A 187 11591 13912 9411 1585 2496 1352 N ATOM 1394 CA GLN A 187 0.964 -16.767 -82.091 1.00 75.35 C ANISOU 1394 CA GLN A 187 9297 11878 7454 1619 2627 1593 C ATOM 1395 C GLN A 187 1.040 -15.274 -81.809 1.00 90.21 C ANISOU 1395 C GLN A 187 11037 13763 9477 1475 2524 1790 C ATOM 1396 O GLN A 187 0.138 -14.512 -82.169 1.00 99.37 O ANISOU 1396 O GLN A 187 12270 14923 10561 1407 2416 1777 O ATOM 1397 CB GLN A 187 1.758 -17.097 -83.362 1.00 72.91 C ANISOU 1397 CB GLN A 187 9011 11722 6967 1793 2864 1683 C ATOM 1398 CG GLN A 187 2.071 -18.572 -83.532 1.00 78.83 C ANISOU 1398 CG GLN A 187 9871 12457 7624 1956 3014 1531 C ATOM 1399 CD GLN A 187 3.358 -18.807 -84.294 1.00 79.70 C ANISOU 1399 CD GLN A 187 9900 12703 7679 2128 3272 1699 C ATOM 1400 OE1 GLN A 187 3.512 -18.364 -85.432 1.00 93.48 O ANISOU 1400 OE1 GLN A 187 11676 14588 9256 2194 3379 1796 O ATOM 1401 NE2 GLN A 187 4.297 -19.500 -83.663 1.00 87.13 N ANISOU 1401 NE2 GLN A 187 10731 13614 8760 2211 3377 1747 N ATOM 1402 N ASN A 188 2.134 -14.869 -81.160 1.00 98.20 N ANISOU 1402 N ASN A 188 11844 14774 10694 1429 2560 1976 N ATOM 1403 CA ASN A 188 2.391 -13.472 -80.812 1.00110.66 C ANISOU 1403 CA ASN A 188 13278 16336 12432 1277 2475 2174 C ATOM 1404 C ASN A 188 1.246 -12.896 -79.976 1.00111.33 C ANISOU 1404 C ASN A 188 13428 16277 12596 1125 2244 2056 C ATOM 1405 O ASN A 188 0.597 -11.914 -80.343 1.00116.31 O ANISOU 1405 O ASN A 188 14105 16897 13190 1060 2168 2104 O ATOM 1406 CB ASN A 188 2.641 -12.632 -82.069 1.00115.45 C ANISOU 1406 CB ASN A 188 13875 17072 12918 1316 2585 2360 C ATOM 1407 CG ASN A 188 3.871 -13.080 -82.833 1.00124.94 C ANISOU 1407 CG ASN A 188 14985 18426 14060 1463 2824 2508 C ATOM 1408 OD1 ASN A 188 4.863 -13.502 -82.240 1.00132.22 O ANISOU 1408 OD1 ASN A 188 15756 19358 15122 1482 2894 2582 O ATOM 1409 ND2 ASN A 188 3.810 -12.994 -84.157 1.00128.38 N ANISOU 1409 ND2 ASN A 188 15508 18991 14279 1575 2954 2559 N ATOM 1410 N SER A 189 1.007 -13.533 -78.834 1.00104.29 N ANISOU 1410 N SER A 189 12539 15275 11813 1081 2144 1910 N ATOM 1411 CA SER A 189 -0.043 -13.134 -77.908 1.00106.98 C ANISOU 1411 CA SER A 189 12936 15478 12233 950 1937 1786 C ATOM 1412 C SER A 189 0.583 -12.476 -76.686 1.00122.05 C ANISOU 1412 C SER A 189 14683 17306 14384 807 1847 1893 C ATOM 1413 O SER A 189 1.532 -13.013 -76.105 1.00121.88 O ANISOU 1413 O SER A 189 14539 17302 14468 821 1900 1942 O ATOM 1414 CB SER A 189 -0.890 -14.337 -77.487 1.00116.38 C ANISOU 1414 CB SER A 189 14262 16600 13355 995 1880 1533 C ATOM 1415 OG SER A 189 -0.091 -15.330 -76.868 1.00133.37 O ANISOU 1415 OG SER A 189 16347 18739 15590 1051 1952 1510 O ATOM 1416 N THR A 190 0.051 -11.317 -76.303 1.00135.32 N ANISOU 1416 N THR A 190 16368 18902 16146 672 1712 1930 N ATOM 1417 CA THR A 190 0.539 -10.594 -75.135 1.00144.76 C ANISOU 1417 CA THR A 190 17438 20008 17558 514 1609 2011 C ATOM 1418 C THR A 190 -0.082 -11.083 -73.833 1.00134.78 C ANISOU 1418 C THR A 190 16214 18625 16370 455 1463 1828 C ATOM 1419 O THR A 190 0.295 -10.589 -72.764 1.00132.34 O ANISOU 1419 O THR A 190 15813 18243 16226 325 1367 1869 O ATOM 1420 CB THR A 190 0.278 -9.094 -75.296 1.00154.31 C ANISOU 1420 CB THR A 190 18650 21156 18824 397 1541 2133 C ATOM 1421 OG1 THR A 190 -1.125 -8.868 -75.483 1.00156.48 O ANISOU 1421 OG1 THR A 190 19090 21367 18997 412 1447 1998 O ATOM 1422 CG2 THR A 190 1.039 -8.546 -76.494 1.00155.78 C ANISOU 1422 CG2 THR A 190 18771 21460 18959 439 1691 2350 C ATOM 1423 N LEU A 191 -1.015 -12.030 -73.892 1.00123.35 N ANISOU 1423 N LEU A 191 14904 17161 14803 540 1442 1629 N ATOM 1424 CA LEU A 191 -1.632 -12.553 -72.687 1.00107.90 C ANISOU 1424 CA LEU A 191 12987 15099 12911 492 1316 1461 C ATOM 1425 C LEU A 191 -0.768 -13.657 -72.080 1.00108.98 C ANISOU 1425 C LEU A 191 13038 15260 13109 544 1378 1449 C ATOM 1426 O LEU A 191 -0.094 -14.395 -72.804 1.00116.03 O ANISOU 1426 O LEU A 191 13908 16246 13931 669 1531 1493 O ATOM 1427 CB LEU A 191 -3.024 -13.097 -72.992 1.00 95.76 C ANISOU 1427 CB LEU A 191 11623 13533 11227 546 1265 1264 C ATOM 1428 N PRO A 192 -0.760 -13.778 -70.752 1.00100.78 N ANISOU 1428 N PRO A 192 11953 14141 12198 459 1267 1398 N ATOM 1429 CA PRO A 192 0.010 -14.853 -70.117 1.00100.04 C ANISOU 1429 CA PRO A 192 11777 14071 12162 518 1319 1395 C ATOM 1430 C PRO A 192 -0.481 -16.226 -70.554 1.00103.98 C ANISOU 1430 C PRO A 192 12405 14569 12532 665 1404 1239 C ATOM 1431 O PRO A 192 -1.644 -16.408 -70.922 1.00 98.67 O ANISOU 1431 O PRO A 192 11890 13853 11747 678 1362 1087 O ATOM 1432 CB PRO A 192 -0.228 -14.624 -68.620 1.00104.50 C ANISOU 1432 CB PRO A 192 12308 14541 12856 390 1155 1340 C ATOM 1433 CG PRO A 192 -0.580 -13.174 -68.514 1.00 98.94 C ANISOU 1433 CG PRO A 192 11608 13781 12202 248 1047 1390 C ATOM 1434 CD PRO A 192 -1.348 -12.859 -69.764 1.00 97.28 C ANISOU 1434 CD PRO A 192 11520 13588 11854 309 1097 1364 C ATOM 1435 N ILE A 193 0.429 -17.199 -70.505 1.00109.95 N ANISOU 1435 N ILE A 193 13093 15376 13308 774 1525 1283 N ATOM 1436 CA ILE A 193 0.121 -18.539 -70.999 1.00114.20 C ANISOU 1436 CA ILE A 193 13763 15901 13727 923 1633 1146 C ATOM 1437 C ILE A 193 -0.903 -19.220 -70.099 1.00118.48 C ANISOU 1437 C ILE A 193 14418 16321 14277 885 1520 953 C ATOM 1438 O ILE A 193 -1.979 -19.629 -70.550 1.00126.70 O ANISOU 1438 O ILE A 193 15626 17315 15198 902 1501 787 O ATOM 1439 CB ILE A 193 1.406 -19.377 -71.121 1.00107.45 C ANISOU 1439 CB ILE A 193 12802 15119 12904 1064 1804 1257 C ATOM 1440 N GLY A 194 -0.584 -19.353 -68.814 1.00115.80 N ANISOU 1440 N GLY A 194 13984 15939 14076 829 1441 979 N ATOM 1441 CA GLY A 194 -1.468 -20.037 -67.892 1.00119.37 C ANISOU 1441 CA GLY A 194 14529 16281 14543 799 1346 817 C ATOM 1442 C GLY A 194 -2.192 -19.110 -66.940 1.00125.47 C ANISOU 1442 C GLY A 194 15291 16995 15386 639 1159 783 C ATOM 1443 O GLY A 194 -1.932 -19.123 -65.733 1.00131.48 O ANISOU 1443 O GLY A 194 15973 17727 16257 579 1077 807 O ATOM 1444 N LEU A 195 -3.109 -18.298 -67.471 1.00127.31 N ANISOU 1444 N LEU A 195 15607 17213 15550 578 1092 729 N ATOM 1445 CA LEU A 195 -3.865 -17.391 -66.614 1.00124.52 C ANISOU 1445 CA LEU A 195 15261 16795 15256 444 928 691 C ATOM 1446 C LEU A 195 -4.902 -18.147 -65.794 1.00115.53 C ANISOU 1446 C LEU A 195 14218 15569 14107 430 851 523 C ATOM 1447 O LEU A 195 -5.127 -17.829 -64.620 1.00122.90 O ANISOU 1447 O LEU A 195 15122 16450 15126 344 739 506 O ATOM 1448 CB LEU A 195 -4.532 -16.303 -67.456 1.00136.65 C ANISOU 1448 CB LEU A 195 16854 18343 16723 403 894 701 C ATOM 1449 CG LEU A 195 -4.833 -15.001 -66.714 1.00136.62 C ANISOU 1449 CG LEU A 195 16819 18281 16809 271 759 739 C ATOM 1450 CD1 LEU A 195 -3.538 -14.380 -66.213 1.00136.72 C ANISOU 1450 CD1 LEU A 195 16680 18318 16951 202 759 902 C ATOM 1451 CD2 LEU A 195 -5.591 -14.030 -67.605 1.00132.78 C ANISOU 1451 CD2 LEU A 195 16404 17799 16248 258 738 750 C ATOM 1452 N GLY A 196 -5.544 -19.151 -66.394 1.00104.73 N ANISOU 1452 N GLY A 196 12972 14188 12633 507 911 397 N ATOM 1453 CA GLY A 196 -6.489 -19.973 -65.661 1.00 89.74 C ANISOU 1453 CA GLY A 196 11160 12208 10730 490 851 247 C ATOM 1454 C GLY A 196 -5.847 -20.866 -64.621 1.00 75.92 C ANISOU 1454 C GLY A 196 9355 10419 9073 520 875 264 C ATOM 1455 O GLY A 196 -6.539 -21.336 -63.711 1.00 70.27 O ANISOU 1455 O GLY A 196 8682 9633 8384 482 805 172 O ATOM 1456 N LEU A 197 -4.540 -21.115 -64.737 1.00 71.94 N ANISOU 1456 N LEU A 197 8751 9968 8616 593 976 393 N ATOM 1457 CA LEU A 197 -3.844 -21.889 -63.715 1.00 75.15 C ANISOU 1457 CA LEU A 197 9083 10354 9115 629 994 440 C ATOM 1458 C LEU A 197 -3.782 -21.137 -62.393 1.00 89.44 C ANISOU 1458 C LEU A 197 10796 12159 11028 511 849 490 C ATOM 1459 O LEU A 197 -3.821 -21.761 -61.327 1.00 91.02 O ANISOU 1459 O LEU A 197 10984 12319 11280 509 811 468 O ATOM 1460 CB LEU A 197 -2.434 -22.246 -64.187 1.00 66.41 C ANISOU 1460 CB LEU A 197 7870 9327 8037 744 1138 588 C ATOM 1461 CG LEU A 197 -2.323 -23.251 -65.334 1.00 66.20 C ANISOU 1461 CG LEU A 197 7949 9294 7911 892 1310 536 C ATOM 1462 CD1 LEU A 197 -0.864 -23.530 -65.660 1.00 56.42 C ANISOU 1462 CD1 LEU A 197 6580 8143 6713 1016 1457 705 C ATOM 1463 CD2 LEU A 197 -3.055 -24.540 -64.990 1.00 69.86 C ANISOU 1463 CD2 LEU A 197 8556 9640 8346 938 1332 382 C ATOM 1464 N THR A 198 -3.688 -19.806 -62.440 1.00 89.00 N ANISOU 1464 N THR A 198 10679 12138 10997 411 770 556 N ATOM 1465 CA THR A 198 -3.671 -19.022 -61.209 1.00 93.79 C ANISOU 1465 CA THR A 198 11219 12729 11689 288 628 585 C ATOM 1466 C THR A 198 -4.989 -19.155 -60.456 1.00 76.96 C ANISOU 1466 C THR A 198 9199 10509 9531 238 529 433 C ATOM 1467 O THR A 198 -5.000 -19.277 -59.226 1.00 68.96 O ANISOU 1467 O THR A 198 8156 9473 8571 192 450 423 O ATOM 1468 CB THR A 198 -3.373 -17.555 -61.523 1.00109.32 C ANISOU 1468 CB THR A 198 13128 14725 13684 188 575 674 C ATOM 1469 OG1 THR A 198 -2.124 -17.458 -62.219 1.00115.38 O ANISOU 1469 OG1 THR A 198 13775 15585 14478 230 674 830 O ATOM 1470 CG2 THR A 198 -3.293 -16.739 -60.241 1.00112.14 C ANISOU 1470 CG2 THR A 198 13431 15055 14123 53 431 692 C ATOM 1471 N LYS A 199 -6.112 -19.144 -61.179 1.00 68.08 N ANISOU 1471 N LYS A 199 8198 9348 8321 249 533 320 N ATOM 1472 CA LYS A 199 -7.404 -19.366 -60.540 1.00 72.30 C ANISOU 1472 CA LYS A 199 8828 9813 8829 212 453 183 C ATOM 1473 C LYS A 199 -7.541 -20.781 -59.995 1.00 82.72 C ANISOU 1473 C LYS A 199 10184 11093 10152 269 496 119 C ATOM 1474 O LYS A 199 -8.407 -21.024 -59.148 1.00 93.00 O ANISOU 1474 O LYS A 199 11535 12343 11458 229 427 34 O ATOM 1475 CB LYS A 199 -8.543 -19.078 -61.521 1.00 72.03 C ANISOU 1475 CB LYS A 199 8898 9772 8699 213 449 91 C ATOM 1476 CG LYS A 199 -8.672 -17.617 -61.921 1.00 87.72 C ANISOU 1476 CG LYS A 199 10869 11777 10684 156 394 147 C ATOM 1477 CD LYS A 199 -9.982 -17.355 -62.649 1.00102.95 C ANISOU 1477 CD LYS A 199 12894 13705 12519 159 367 57 C ATOM 1478 CE LYS A 199 -10.086 -18.181 -63.920 1.00125.41 C ANISOU 1478 CE LYS A 199 15798 16596 15256 237 463 14 C ATOM 1479 NZ LYS A 199 -11.383 -17.966 -64.619 1.00136.74 N ANISOU 1479 NZ LYS A 199 17315 18052 16589 231 421 -71 N ATOM 1480 N ASN A 200 -6.709 -21.716 -60.457 1.00 81.35 N ANISOU 1480 N ASN A 200 9993 10938 9979 368 616 165 N ATOM 1481 CA ASN A 200 -6.778 -23.090 -59.972 1.00 81.17 C ANISOU 1481 CA ASN A 200 10015 10857 9966 433 672 116 C ATOM 1482 C ASN A 200 -6.032 -23.251 -58.652 1.00 78.99 C ANISOU 1482 C ASN A 200 9634 10595 9784 426 632 210 C ATOM 1483 O ASN A 200 -6.616 -23.659 -57.642 1.00 85.49 O ANISOU 1483 O ASN A 200 10488 11368 10626 394 574 156 O ATOM 1484 CB ASN A 200 -6.218 -24.050 -61.027 1.00 82.28 C ANISOU 1484 CB ASN A 200 10201 10999 10065 558 830 121 C ATOM 1485 CG ASN A 200 -7.103 -24.151 -62.253 1.00 84.05 C ANISOU 1485 CG ASN A 200 10557 11206 10173 563 865 -2 C ATOM 1486 OD1 ASN A 200 -8.323 -24.013 -62.165 1.00 90.92 O ANISOU 1486 OD1 ASN A 200 11505 12040 10999 488 781 -116 O ATOM 1487 ND2 ASN A 200 -6.491 -24.397 -63.405 1.00 83.67 N ANISOU 1487 ND2 ASN A 200 10530 11196 10066 654 988 27 N ATOM 1488 N ILE A 201 -4.737 -22.933 -58.640 1.00 74.28 N ANISOU 1488 N ILE A 201 8903 10078 9243 452 661 359 N ATOM 1489 CA ILE A 201 -3.933 -23.161 -57.444 1.00 80.60 C ANISOU 1489 CA ILE A 201 9587 10915 10122 452 623 462 C ATOM 1490 C ILE A 201 -4.134 -22.041 -56.429 1.00 87.37 C ANISOU 1490 C ILE A 201 10393 11793 11009 310 462 469 C ATOM 1491 O ILE A 201 -4.422 -22.295 -55.254 1.00 90.80 O ANISOU 1491 O ILE A 201 10831 12208 11461 277 388 447 O ATOM 1492 CB ILE A 201 -2.447 -23.339 -57.818 1.00 85.20 C ANISOU 1492 CB ILE A 201 10029 11593 10752 539 720 630 C ATOM 1493 CG1 ILE A 201 -1.575 -23.349 -56.561 1.00 97.40 C ANISOU 1493 CG1 ILE A 201 11423 13208 12375 516 651 756 C ATOM 1494 CG2 ILE A 201 -1.987 -22.266 -58.797 1.00 87.34 C ANISOU 1494 CG2 ILE A 201 10240 11932 11012 499 733 695 C ATOM 1495 N LEU A 202 -3.993 -20.785 -56.862 1.00 85.44 N ANISOU 1495 N LEU A 202 10113 11582 10766 226 410 500 N ATOM 1496 CA LEU A 202 -4.139 -19.669 -55.933 1.00 80.29 C ANISOU 1496 CA LEU A 202 9432 10932 10141 89 263 500 C ATOM 1497 C LEU A 202 -5.599 -19.420 -55.576 1.00 66.83 C ANISOU 1497 C LEU A 202 7864 9141 8388 40 192 348 C ATOM 1498 O LEU A 202 -5.897 -18.985 -54.457 1.00 81.72 O ANISOU 1498 O LEU A 202 9755 11011 10286 -38 85 318 O ATOM 1499 CB LEU A 202 -3.511 -18.406 -56.525 1.00 88.89 C ANISOU 1499 CB LEU A 202 10450 12065 11258 11 240 587 C ATOM 1500 CG LEU A 202 -3.632 -17.116 -55.710 1.00 89.65 C ANISOU 1500 CG LEU A 202 10539 12140 11384 -141 97 578 C ATOM 1501 CD1 LEU A 202 -2.963 -17.272 -54.353 1.00 93.59 C ANISOU 1501 CD1 LEU A 202 10945 12690 11925 -197 10 632 C ATOM 1502 CD2 LEU A 202 -3.046 -15.937 -56.472 1.00 79.06 C ANISOU 1502 CD2 LEU A 202 9144 10821 10074 -215 95 668 C ATOM 1503 N GLY A 203 -6.516 -19.697 -56.498 1.00 69.87 N ANISOU 1503 N GLY A 203 8355 9480 8712 88 249 254 N ATOM 1504 CA GLY A 203 -7.925 -19.452 -56.295 1.00 67.93 C ANISOU 1504 CA GLY A 203 8219 9170 8419 49 189 125 C ATOM 1505 C GLY A 203 -8.732 -20.613 -55.764 1.00 63.43 C ANISOU 1505 C GLY A 203 7719 8554 7826 88 206 33 C ATOM 1506 O GLY A 203 -9.916 -20.434 -55.466 1.00 65.02 O ANISOU 1506 O GLY A 203 7994 8715 7994 52 154 -64 O ATOM 1507 N PHE A 204 -8.138 -21.799 -55.632 1.00 59.43 N ANISOU 1507 N PHE A 204 7191 8050 7342 163 284 70 N ATOM 1508 CA PHE A 204 -8.885 -22.949 -55.138 1.00 66.62 C ANISOU 1508 CA PHE A 204 8175 8899 8238 195 309 -9 C ATOM 1509 C PHE A 204 -7.993 -23.948 -54.412 1.00 66.94 C ANISOU 1509 C PHE A 204 8159 8945 8329 262 359 77 C ATOM 1510 O PHE A 204 -8.230 -24.251 -53.240 1.00 71.09 O ANISOU 1510 O PHE A 204 8680 9458 8872 241 308 77 O ATOM 1511 CB PHE A 204 -9.617 -23.646 -56.288 1.00 65.82 C ANISOU 1511 CB PHE A 204 8180 8752 8078 238 391 -107 C ATOM 1512 CG PHE A 204 -10.369 -24.876 -55.868 1.00 75.48 C ANISOU 1512 CG PHE A 204 9486 9899 9295 255 425 -187 C ATOM 1513 CD1 PHE A 204 -11.608 -24.771 -55.257 1.00 75.99 C ANISOU 1513 CD1 PHE A 204 9598 9936 9340 186 351 -273 C ATOM 1514 CD2 PHE A 204 -9.839 -26.138 -56.083 1.00 76.81 C ANISOU 1514 CD2 PHE A 204 9685 10020 9481 344 538 -170 C ATOM 1515 CE1 PHE A 204 -12.303 -25.900 -54.867 1.00 76.44 C ANISOU 1515 CE1 PHE A 204 9724 9923 9398 188 384 -337 C ATOM 1516 CE2 PHE A 204 -10.529 -27.271 -55.695 1.00 77.70 C ANISOU 1516 CE2 PHE A 204 9883 10043 9595 350 573 -240 C ATOM 1517 CZ PHE A 204 -11.763 -27.152 -55.087 1.00 73.62 C ANISOU 1517 CZ PHE A 204 9405 9503 9062 264 493 -322 C ATOM 1518 N LEU A 205 -6.970 -24.463 -55.099 1.00 59.45 N ANISOU 1518 N LEU A 205 7166 8022 7402 353 463 158 N ATOM 1519 CA LEU A 205 -6.167 -25.554 -54.551 1.00 80.86 C ANISOU 1519 CA LEU A 205 9831 10732 10161 447 534 246 C ATOM 1520 C LEU A 205 -5.528 -25.165 -53.222 1.00 86.36 C ANISOU 1520 C LEU A 205 10408 11502 10904 404 436 351 C ATOM 1521 O LEU A 205 -5.756 -25.814 -52.195 1.00 85.61 O ANISOU 1521 O LEU A 205 10325 11382 10821 416 415 355 O ATOM 1522 CB LEU A 205 -5.099 -25.976 -55.561 1.00 98.82 C ANISOU 1522 CB LEU A 205 12062 13037 12448 562 668 331 C ATOM 1523 CG LEU A 205 -4.103 -27.038 -55.088 1.00111.35 C ANISOU 1523 CG LEU A 205 13582 14634 14092 687 758 451 C ATOM 1524 CD1 LEU A 205 -4.820 -28.335 -54.744 1.00112.80 C ANISOU 1524 CD1 LEU A 205 13894 14692 14272 742 820 371 C ATOM 1525 CD2 LEU A 205 -3.028 -27.274 -56.137 1.00112.58 C ANISOU 1525 CD2 LEU A 205 13682 14837 14257 806 895 544 C ATOM 1526 N PHE A 206 -4.721 -24.104 -53.222 1.00 84.48 N ANISOU 1526 N PHE A 206 10054 11356 10688 346 373 439 N ATOM 1527 CA PHE A 206 -4.053 -23.687 -51.990 1.00 75.18 C ANISOU 1527 CA PHE A 206 8760 10262 9544 287 266 534 C ATOM 1528 C PHE A 206 -5.027 -23.272 -50.893 1.00 87.14 C ANISOU 1528 C PHE A 206 10341 11743 11024 189 145 441 C ATOM 1529 O PHE A 206 -4.852 -23.719 -49.746 1.00113.62 O ANISOU 1529 O PHE A 206 13661 15128 14383 195 102 486 O ATOM 1530 CB PHE A 206 -3.047 -22.571 -52.294 1.00 62.94 C ANISOU 1530 CB PHE A 206 7080 8809 8024 218 218 636 C ATOM 1531 CG PHE A 206 -1.740 -23.064 -52.846 1.00 77.51 C ANISOU 1531 CG PHE A 206 8795 10738 9917 320 321 789 C ATOM 1532 CD1 PHE A 206 -1.486 -24.421 -52.961 1.00 86.15 C ANISOU 1532 CD1 PHE A 206 9900 11810 11024 474 448 828 C ATOM 1533 CD2 PHE A 206 -0.758 -22.169 -53.237 1.00 79.84 C ANISOU 1533 CD2 PHE A 206 8956 11131 10248 263 299 901 C ATOM 1534 CE1 PHE A 206 -0.281 -24.876 -53.465 1.00 87.35 C ANISOU 1534 CE1 PHE A 206 9930 12041 11219 589 557 976 C ATOM 1535 CE2 PHE A 206 0.449 -22.617 -53.741 1.00 83.53 C ANISOU 1535 CE2 PHE A 206 9287 11691 10760 365 402 1056 C ATOM 1536 CZ PHE A 206 0.688 -23.972 -53.855 1.00 85.55 C ANISOU 1536 CZ PHE A 206 9553 11929 11024 537 535 1094 C ATOM 1537 N PRO A 207 -6.047 -22.441 -51.145 1.00 72.73 N ANISOU 1537 N PRO A 207 8609 9866 9160 109 91 322 N ATOM 1538 CA PRO A 207 -6.945 -22.073 -50.036 1.00 70.43 C ANISOU 1538 CA PRO A 207 8378 9549 8834 34 -10 241 C ATOM 1539 C PRO A 207 -7.773 -23.234 -49.515 1.00 71.17 C ANISOU 1539 C PRO A 207 8549 9585 8908 91 34 186 C ATOM 1540 O PRO A 207 -8.014 -23.314 -48.304 1.00 87.12 O ANISOU 1540 O PRO A 207 10571 11621 10909 62 -30 186 O ATOM 1541 CB PRO A 207 -7.826 -20.975 -50.647 1.00 63.20 C ANISOU 1541 CB PRO A 207 7540 8586 7887 -35 -49 140 C ATOM 1542 CG PRO A 207 -7.055 -20.462 -51.808 1.00 52.16 C ANISOU 1542 CG PRO A 207 6087 7216 6514 -30 -7 203 C ATOM 1543 CD PRO A 207 -6.348 -21.656 -52.356 1.00 68.05 C ANISOU 1543 CD PRO A 207 8056 9249 8550 83 112 274 C ATOM 1544 N PHE A 208 -8.224 -24.136 -50.392 1.00 73.57 N ANISOU 1544 N PHE A 208 8922 9820 9210 163 143 139 N ATOM 1545 CA PHE A 208 -9.031 -25.264 -49.935 1.00 66.36 C ANISOU 1545 CA PHE A 208 8088 8837 8287 201 189 87 C ATOM 1546 C PHE A 208 -8.232 -26.176 -49.014 1.00 65.83 C ANISOU 1546 C PHE A 208 7961 8797 8256 269 215 202 C ATOM 1547 O PHE A 208 -8.775 -26.721 -48.046 1.00 84.90 O ANISOU 1547 O PHE A 208 10411 11187 10660 267 200 192 O ATOM 1548 CB PHE A 208 -9.570 -26.050 -51.131 1.00 57.84 C ANISOU 1548 CB PHE A 208 7101 7676 7200 251 297 10 C ATOM 1549 CG PHE A 208 -10.217 -27.354 -50.760 1.00 60.44 C ANISOU 1549 CG PHE A 208 7511 7918 7536 287 362 -28 C ATOM 1550 CD1 PHE A 208 -11.493 -27.382 -50.221 1.00 57.40 C ANISOU 1550 CD1 PHE A 208 7190 7497 7122 220 317 -117 C ATOM 1551 CD2 PHE A 208 -9.553 -28.554 -50.958 1.00 66.09 C ANISOU 1551 CD2 PHE A 208 8239 8583 8291 390 476 31 C ATOM 1552 CE1 PHE A 208 -12.091 -28.581 -49.880 1.00 63.73 C ANISOU 1552 CE1 PHE A 208 8063 8215 7938 239 378 -144 C ATOM 1553 CE2 PHE A 208 -10.145 -29.756 -50.619 1.00 69.29 C ANISOU 1553 CE2 PHE A 208 8731 8887 8710 415 542 -1 C ATOM 1554 CZ PHE A 208 -11.416 -29.769 -50.079 1.00 64.93 C ANISOU 1554 CZ PHE A 208 8238 8300 8133 331 490 -87 C ATOM 1555 N LEU A 209 -6.940 -26.354 -49.296 1.00 56.18 N ANISOU 1555 N LEU A 209 6640 7631 7074 335 259 324 N ATOM 1556 CA LEU A 209 -6.109 -27.185 -48.434 1.00 73.00 C ANISOU 1556 CA LEU A 209 8695 9804 9239 414 283 456 C ATOM 1557 C LEU A 209 -5.897 -26.541 -47.070 1.00 80.80 C ANISOU 1557 C LEU A 209 9608 10889 10202 336 145 507 C ATOM 1558 O LEU A 209 -5.666 -27.248 -46.083 1.00 88.61 O ANISOU 1558 O LEU A 209 10568 11906 11193 383 142 587 O ATOM 1559 CB LEU A 209 -4.769 -27.467 -49.111 1.00 77.10 C ANISOU 1559 CB LEU A 209 9110 10379 9807 513 366 585 C ATOM 1560 CG LEU A 209 -4.862 -28.304 -50.388 1.00 90.72 C ANISOU 1560 CG LEU A 209 10921 12004 11545 616 524 541 C ATOM 1561 CD1 LEU A 209 -3.514 -28.387 -51.079 1.00102.20 C ANISOU 1561 CD1 LEU A 209 12261 13531 13040 715 609 673 C ATOM 1562 CD2 LEU A 209 -5.400 -29.695 -50.082 1.00 90.84 C ANISOU 1562 CD2 LEU A 209 11044 11897 11572 697 617 514 C ATOM 1563 N ILE A 210 -5.970 -25.212 -46.993 1.00 70.75 N ANISOU 1563 N ILE A 210 8314 9667 8902 220 32 462 N ATOM 1564 CA ILE A 210 -5.915 -24.544 -45.697 1.00 65.11 C ANISOU 1564 CA ILE A 210 7563 9030 8145 131 -104 477 C ATOM 1565 C ILE A 210 -7.269 -24.614 -45.004 1.00 61.00 C ANISOU 1565 C ILE A 210 7165 8445 7570 97 -130 361 C ATOM 1566 O ILE A 210 -7.348 -24.832 -43.790 1.00 63.82 O ANISOU 1566 O ILE A 210 7516 8846 7887 89 -184 391 O ATOM 1567 CB ILE A 210 -5.438 -23.091 -45.864 1.00 69.00 C ANISOU 1567 CB ILE A 210 8001 9583 8634 14 -208 471 C ATOM 1568 CG1 ILE A 210 -4.088 -23.050 -46.582 1.00 68.42 C ANISOU 1568 CG1 ILE A 210 7790 9586 8621 45 -172 603 C ATOM 1569 CG2 ILE A 210 -5.338 -22.406 -44.511 1.00 79.53 C ANISOU 1569 CG2 ILE A 210 9313 10991 9913 -85 -351 473 C ATOM 1570 CD1 ILE A 210 -3.553 -21.650 -46.789 1.00 72.73 C ANISOU 1570 CD1 ILE A 210 8275 10184 9175 -83 -269 612 C ATOM 1571 N ILE A 211 -8.354 -24.433 -45.761 1.00 67.25 N ANISOU 1571 N ILE A 211 8059 9142 8350 80 -92 235 N ATOM 1572 CA ILE A 211 -9.692 -24.548 -45.189 1.00 64.88 C ANISOU 1572 CA ILE A 211 7860 8788 8004 55 -103 134 C ATOM 1573 C ILE A 211 -9.943 -25.972 -44.707 1.00 68.93 C ANISOU 1573 C ILE A 211 8400 9262 8530 132 -23 174 C ATOM 1574 O ILE A 211 -10.508 -26.188 -43.628 1.00 73.49 O ANISOU 1574 O ILE A 211 9006 9850 9067 119 -53 168 O ATOM 1575 CB ILE A 211 -10.751 -24.099 -46.214 1.00 60.72 C ANISOU 1575 CB ILE A 211 7415 8186 7468 26 -77 9 C ATOM 1576 CG1 ILE A 211 -10.597 -22.608 -46.524 1.00 61.92 C ANISOU 1576 CG1 ILE A 211 7554 8366 7607 -49 -159 -24 C ATOM 1577 CG2 ILE A 211 -12.154 -24.397 -45.707 1.00 64.31 C ANISOU 1577 CG2 ILE A 211 7955 8594 7885 11 -71 -80 C ATOM 1578 CD1 ILE A 211 -11.592 -22.088 -47.537 1.00 59.01 C ANISOU 1578 CD1 ILE A 211 7256 7939 7225 -66 -138 -126 C ATOM 1579 N LEU A 212 -9.517 -26.964 -45.492 1.00 74.19 N ANISOU 1579 N LEU A 212 9063 9876 9250 217 87 219 N ATOM 1580 CA LEU A 212 -9.697 -28.355 -45.087 1.00 73.23 C ANISOU 1580 CA LEU A 212 8980 9692 9153 294 176 264 C ATOM 1581 C LEU A 212 -8.846 -28.691 -43.868 1.00 76.70 C ANISOU 1581 C LEU A 212 9336 10219 9589 338 141 408 C ATOM 1582 O LEU A 212 -9.293 -29.422 -42.976 1.00 64.65 O ANISOU 1582 O LEU A 212 7845 8672 8049 361 160 437 O ATOM 1583 CB LEU A 212 -9.360 -29.289 -46.250 1.00 60.82 C ANISOU 1583 CB LEU A 212 7441 8031 7637 381 309 273 C ATOM 1584 CG LEU A 212 -9.462 -30.792 -45.978 1.00 65.23 C ANISOU 1584 CG LEU A 212 8058 8491 8235 469 422 321 C ATOM 1585 CD1 LEU A 212 -10.895 -31.187 -45.657 1.00 69.56 C ANISOU 1585 CD1 LEU A 212 8713 8954 8763 404 429 219 C ATOM 1586 CD2 LEU A 212 -8.932 -31.591 -47.158 1.00 54.43 C ANISOU 1586 CD2 LEU A 212 6727 7036 6917 565 556 329 C ATOM 1587 N THR A 213 -7.621 -28.165 -43.809 1.00 73.38 N ANISOU 1587 N THR A 213 8796 9907 9177 346 87 507 N ATOM 1588 CA THR A 213 -6.739 -28.468 -42.685 1.00 68.28 C ANISOU 1588 CA THR A 213 8052 9370 8520 386 42 656 C ATOM 1589 C THR A 213 -7.230 -27.809 -41.401 1.00 64.97 C ANISOU 1589 C THR A 213 7646 9026 8015 295 -84 623 C ATOM 1590 O THR A 213 -7.136 -28.401 -40.319 1.00 75.40 O ANISOU 1590 O THR A 213 8949 10396 9302 333 -97 710 O ATOM 1591 CB THR A 213 -5.310 -28.023 -43.002 1.00 67.86 C ANISOU 1591 CB THR A 213 7852 9433 8500 402 9 773 C ATOM 1592 OG1 THR A 213 -4.867 -28.660 -44.207 1.00 72.68 O ANISOU 1592 OG1 THR A 213 8457 9976 9181 503 143 803 O ATOM 1593 CG2 THR A 213 -4.366 -28.392 -41.866 1.00 75.11 C ANISOU 1593 CG2 THR A 213 8649 10486 9402 448 -44 942 C ATOM 1594 N SER A 214 -7.759 -26.587 -41.500 1.00 54.00 N ANISOU 1594 N SER A 214 6294 7642 6580 183 -171 502 N ATOM 1595 CA SER A 214 -8.212 -25.876 -40.309 1.00 54.80 C ANISOU 1595 CA SER A 214 6424 7807 6589 101 -284 457 C ATOM 1596 C SER A 214 -9.373 -26.601 -39.640 1.00 77.52 C ANISOU 1596 C SER A 214 9396 10627 9429 130 -233 417 C ATOM 1597 O SER A 214 -9.358 -26.834 -38.426 1.00 93.36 O ANISOU 1597 O SER A 214 11395 12706 11370 136 -276 474 O ATOM 1598 CB SER A 214 -8.606 -24.443 -40.671 1.00 50.22 C ANISOU 1598 CB SER A 214 5886 7214 5981 -9 -363 329 C ATOM 1599 OG SER A 214 -7.477 -23.693 -41.084 1.00 57.10 O ANISOU 1599 OG SER A 214 6663 8152 6881 -57 -426 380 O ATOM 1600 N TYR A 215 -10.390 -26.974 -40.419 1.00 70.08 N ANISOU 1600 N TYR A 215 8540 9563 8524 142 -143 325 N ATOM 1601 CA TYR A 215 -11.554 -27.645 -39.854 1.00 69.76 C ANISOU 1601 CA TYR A 215 8581 9468 8458 154 -91 289 C ATOM 1602 C TYR A 215 -11.287 -29.103 -39.505 1.00 63.43 C ANISOU 1602 C TYR A 215 7772 8632 7698 247 3 409 C ATOM 1603 O TYR A 215 -12.005 -29.666 -38.673 1.00 69.19 O ANISOU 1603 O TYR A 215 8546 9348 8394 255 30 425 O ATOM 1604 CB TYR A 215 -12.739 -27.544 -40.817 1.00 62.89 C ANISOU 1604 CB TYR A 215 7791 8492 7613 120 -37 155 C ATOM 1605 CG TYR A 215 -13.299 -26.144 -40.934 1.00 61.39 C ANISOU 1605 CG TYR A 215 7625 8328 7372 42 -119 42 C ATOM 1606 CD1 TYR A 215 -14.059 -25.593 -39.910 1.00 55.33 C ANISOU 1606 CD1 TYR A 215 6896 7603 6524 6 -171 -5 C ATOM 1607 CD2 TYR A 215 -13.067 -25.373 -42.064 1.00 69.14 C ANISOU 1607 CD2 TYR A 215 8598 9288 8384 14 -134 -13 C ATOM 1608 CE1 TYR A 215 -14.571 -24.313 -40.008 1.00 52.36 C ANISOU 1608 CE1 TYR A 215 6555 7235 6104 -50 -233 -107 C ATOM 1609 CE2 TYR A 215 -13.576 -24.092 -42.172 1.00 71.45 C ANISOU 1609 CE2 TYR A 215 8921 9590 8638 -47 -201 -106 C ATOM 1610 CZ TYR A 215 -14.326 -23.567 -41.141 1.00 69.05 C ANISOU 1610 CZ TYR A 215 8661 9316 8259 -76 -248 -154 C ATOM 1611 OH TYR A 215 -14.835 -22.293 -41.244 1.00 81.79 O ANISOU 1611 OH TYR A 215 10316 10923 9836 -121 -302 -245 O ATOM 1612 N THR A 216 -10.278 -29.728 -40.118 1.00 66.47 N ANISOU 1612 N THR A 216 8104 8998 8154 324 62 502 N ATOM 1613 CA THR A 216 -9.903 -31.079 -39.713 1.00 63.74 C ANISOU 1613 CA THR A 216 7752 8617 7850 430 154 635 C ATOM 1614 C THR A 216 -9.283 -31.077 -38.321 1.00 64.97 C ANISOU 1614 C THR A 216 7833 8913 7940 454 77 768 C ATOM 1615 O THR A 216 -9.546 -31.977 -37.515 1.00 59.46 O ANISOU 1615 O THR A 216 7162 8199 7232 508 126 852 O ATOM 1616 CB THR A 216 -8.938 -31.690 -40.732 1.00 63.38 C ANISOU 1616 CB THR A 216 7669 8519 7893 525 246 703 C ATOM 1617 OG1 THR A 216 -9.571 -31.752 -42.016 1.00 62.03 O ANISOU 1617 OG1 THR A 216 7583 8220 7765 500 318 571 O ATOM 1618 CG2 THR A 216 -8.526 -33.094 -40.311 1.00 53.27 C ANISOU 1618 CG2 THR A 216 6392 7185 6663 652 353 849 C ATOM 1619 N LEU A 217 -8.463 -30.067 -38.021 1.00 72.76 N ANISOU 1619 N LEU A 217 8726 10041 8876 407 -48 793 N ATOM 1620 CA LEU A 217 -7.899 -29.945 -36.682 1.00 80.09 C ANISOU 1620 CA LEU A 217 9585 11126 9720 408 -145 904 C ATOM 1621 C LEU A 217 -8.971 -29.608 -35.653 1.00 80.77 C ANISOU 1621 C LEU A 217 9756 11234 9700 344 -195 827 C ATOM 1622 O LEU A 217 -8.886 -30.055 -34.504 1.00 86.98 O ANISOU 1622 O LEU A 217 10528 12104 10417 379 -216 928 O ATOM 1623 CB LEU A 217 -6.793 -28.891 -36.677 1.00 72.98 C ANISOU 1623 CB LEU A 217 8569 10368 8791 346 -276 933 C ATOM 1624 CG LEU A 217 -5.541 -29.286 -37.463 1.00 66.37 C ANISOU 1624 CG LEU A 217 7612 9557 8049 427 -228 1059 C ATOM 1625 CD1 LEU A 217 -4.615 -28.097 -37.661 1.00 63.24 C ANISOU 1625 CD1 LEU A 217 7105 9284 7638 332 -354 1061 C ATOM 1626 CD2 LEU A 217 -4.818 -30.418 -36.752 1.00 62.42 C ANISOU 1626 CD2 LEU A 217 7034 9125 7559 558 -185 1261 C ATOM 1627 N ILE A 218 -9.978 -28.824 -36.043 1.00 72.15 N ANISOU 1627 N ILE A 218 8748 10077 8589 259 -209 658 N ATOM 1628 CA ILE A 218 -11.124 -28.602 -35.167 1.00 65.73 C ANISOU 1628 CA ILE A 218 8019 9270 7684 218 -224 584 C ATOM 1629 C ILE A 218 -11.897 -29.900 -34.975 1.00 74.53 C ANISOU 1629 C ILE A 218 9189 10294 8837 284 -97 635 C ATOM 1630 O ILE A 218 -12.392 -30.191 -33.879 1.00 87.44 O ANISOU 1630 O ILE A 218 10852 11977 10393 294 -96 677 O ATOM 1631 CB ILE A 218 -12.020 -27.485 -35.734 1.00 50.84 C ANISOU 1631 CB ILE A 218 6201 7332 5782 131 -254 404 C ATOM 1632 CG1 ILE A 218 -11.220 -26.192 -35.898 1.00 53.45 C ANISOU 1632 CG1 ILE A 218 6489 7735 6083 57 -376 361 C ATOM 1633 CG2 ILE A 218 -13.226 -27.255 -34.836 1.00 47.44 C ANISOU 1633 CG2 ILE A 218 5852 6915 5258 105 -255 335 C ATOM 1634 CD1 ILE A 218 -11.984 -25.088 -36.598 1.00 47.41 C ANISOU 1634 CD1 ILE A 218 5790 6903 5320 -13 -395 201 C ATOM 1635 N TRP A 219 -12.007 -30.702 -36.037 1.00 62.50 N ANISOU 1635 N TRP A 219 7685 8633 7428 324 14 632 N ATOM 1636 CA TRP A 219 -12.652 -32.007 -35.933 1.00 63.55 C ANISOU 1636 CA TRP A 219 7876 8655 7613 376 140 684 C ATOM 1637 C TRP A 219 -11.907 -32.908 -34.955 1.00 67.92 C ANISOU 1637 C TRP A 219 8386 9267 8154 471 163 875 C ATOM 1638 O TRP A 219 -12.516 -33.542 -34.086 1.00 51.67 O ANISOU 1638 O TRP A 219 6368 7202 6062 489 208 935 O ATOM 1639 CB TRP A 219 -12.725 -32.654 -37.319 1.00 54.98 C ANISOU 1639 CB TRP A 219 6830 7412 6650 396 246 638 C ATOM 1640 CG TRP A 219 -13.498 -33.942 -37.386 1.00 57.17 C ANISOU 1640 CG TRP A 219 7188 7542 6991 419 376 659 C ATOM 1641 CD1 TRP A 219 -13.179 -35.126 -36.785 1.00 67.29 C ANISOU 1641 CD1 TRP A 219 8481 8779 8308 506 459 808 C ATOM 1642 CD2 TRP A 219 -14.702 -34.181 -38.125 1.00 67.40 C ANISOU 1642 CD2 TRP A 219 8567 8714 8329 347 437 531 C ATOM 1643 NE1 TRP A 219 -14.118 -36.081 -37.089 1.00 73.91 N ANISOU 1643 NE1 TRP A 219 9414 9457 9213 483 571 775 N ATOM 1644 CE2 TRP A 219 -15.063 -35.526 -37.912 1.00 72.64 C ANISOU 1644 CE2 TRP A 219 9293 9252 9055 379 554 603 C ATOM 1645 CE3 TRP A 219 -15.513 -33.386 -38.940 1.00 71.73 C ANISOU 1645 CE3 TRP A 219 9138 9249 8867 257 401 371 C ATOM 1646 CZ2 TRP A 219 -16.200 -36.093 -38.484 1.00 78.16 C ANISOU 1646 CZ2 TRP A 219 10075 9818 9807 305 628 511 C ATOM 1647 CZ3 TRP A 219 -16.640 -33.951 -39.507 1.00 80.56 C ANISOU 1647 CZ3 TRP A 219 10327 10252 10030 195 472 287 C ATOM 1648 CH2 TRP A 219 -16.974 -35.291 -39.276 1.00 84.30 C ANISOU 1648 CH2 TRP A 219 10859 10604 10565 210 580 353 C ATOM 1649 N LYS A 220 -10.579 -32.972 -35.081 1.00 71.57 N ANISOU 1649 N LYS A 220 8757 9796 8641 537 135 985 N ATOM 1650 CA LYS A 220 -9.794 -33.862 -34.233 1.00 72.21 C ANISOU 1650 CA LYS A 220 8782 9939 8715 647 160 1187 C ATOM 1651 C LYS A 220 -9.760 -33.388 -32.786 1.00 75.87 C ANISOU 1651 C LYS A 220 9212 10582 9033 620 47 1245 C ATOM 1652 O LYS A 220 -9.714 -34.214 -31.867 1.00 77.15 O ANISOU 1652 O LYS A 220 9372 10778 9164 694 85 1391 O ATOM 1653 CB LYS A 220 -8.373 -33.990 -34.783 1.00 57.59 C ANISOU 1653 CB LYS A 220 6821 8132 6927 730 158 1297 C ATOM 1654 N ALA A 221 -9.782 -32.073 -32.561 1.00 68.75 N ANISOU 1654 N ALA A 221 8294 9792 8036 516 -89 1135 N ATOM 1655 CA ALA A 221 -9.740 -31.557 -31.196 1.00 55.69 C ANISOU 1655 CA ALA A 221 6624 8309 6225 482 -203 1168 C ATOM 1656 C ALA A 221 -11.059 -31.803 -30.475 1.00 66.71 C ANISOU 1656 C ALA A 221 8126 9668 7554 467 -148 1122 C ATOM 1657 O ALA A 221 -11.075 -32.257 -29.324 1.00 77.71 O ANISOU 1657 O ALA A 221 9518 11155 8855 511 -152 1238 O ATOM 1658 CB ALA A 221 -9.398 -30.067 -31.207 1.00 48.30 C ANISOU 1658 CB ALA A 221 5663 7477 5210 368 -356 1048 C ATOM 1659 N LEU A 222 -12.181 -31.507 -31.137 1.00 65.34 N ANISOU 1659 N LEU A 222 8035 9370 7423 407 -94 964 N ATOM 1660 CA LEU A 222 -13.483 -31.744 -30.524 1.00 60.10 C ANISOU 1660 CA LEU A 222 7454 8676 6707 391 -31 926 C ATOM 1661 C LEU A 222 -13.750 -33.230 -30.325 1.00 67.65 C ANISOU 1661 C LEU A 222 8430 9540 7735 470 105 1067 C ATOM 1662 O LEU A 222 -14.503 -33.606 -29.420 1.00 74.58 O ANISOU 1662 O LEU A 222 9349 10444 8546 478 149 1114 O ATOM 1663 CB LEU A 222 -14.588 -31.115 -31.374 1.00 59.81 C ANISOU 1663 CB LEU A 222 7480 8537 6711 313 -5 740 C ATOM 1664 CG LEU A 222 -14.582 -29.588 -31.480 1.00 65.25 C ANISOU 1664 CG LEU A 222 8175 9293 7322 236 -123 593 C ATOM 1665 CD1 LEU A 222 -15.666 -29.111 -32.433 1.00 62.84 C ANISOU 1665 CD1 LEU A 222 7922 8880 7075 182 -80 437 C ATOM 1666 CD2 LEU A 222 -14.756 -28.957 -30.107 1.00 59.56 C ANISOU 1666 CD2 LEU A 222 7484 8717 6429 220 -200 588 C ATOM 1667 N LYS A 223 -13.149 -34.085 -31.155 1.00 75.06 N ANISOU 1667 N LYS A 223 9346 10365 8808 531 182 1138 N ATOM 1668 CA LYS A 223 -13.316 -35.524 -30.983 1.00 78.00 C ANISOU 1668 CA LYS A 223 9752 10625 9259 610 319 1277 C ATOM 1669 C LYS A 223 -12.609 -36.011 -29.725 1.00 80.73 C ANISOU 1669 C LYS A 223 10047 11104 9521 702 296 1482 C ATOM 1670 O LYS A 223 -13.175 -36.782 -28.941 1.00 89.94 O ANISOU 1670 O LYS A 223 11257 12252 10665 735 373 1582 O ATOM 1671 CB LYS A 223 -12.798 -36.266 -32.214 1.00 84.59 C ANISOU 1671 CB LYS A 223 10592 11295 10251 663 411 1290 C ATOM 1672 CG LYS A 223 -13.892 -36.787 -33.129 1.00 83.36 C ANISOU 1672 CG LYS A 223 10534 10939 10200 604 523 1174 C ATOM 1673 CD LYS A 223 -14.766 -37.803 -32.412 1.00 85.31 C ANISOU 1673 CD LYS A 223 10847 11107 10461 609 627 1258 C ATOM 1674 CE LYS A 223 -15.861 -38.331 -33.322 1.00 93.90 C ANISOU 1674 CE LYS A 223 12024 12002 11652 526 727 1141 C ATOM 1675 NZ LYS A 223 -16.707 -39.350 -32.641 1.00 98.12 N ANISOU 1675 NZ LYS A 223 12618 12451 12213 514 833 1233 N ATOM 1676 N LYS A 224 -11.365 -35.570 -29.514 1.00 77.27 N ANISOU 1676 N LYS A 224 9512 10813 9034 742 191 1555 N ATOM 1677 CA LYS A 224 -10.635 -35.968 -28.316 1.00 76.15 C ANISOU 1677 CA LYS A 224 9306 10829 8797 828 150 1757 C ATOM 1678 C LYS A 224 -11.295 -35.429 -27.054 1.00 81.94 C ANISOU 1678 C LYS A 224 10074 11709 9350 774 77 1735 C ATOM 1679 O LYS A 224 -11.204 -36.054 -25.991 1.00 94.90 O ANISOU 1679 O LYS A 224 11708 13438 10913 845 95 1902 O ATOM 1680 CB LYS A 224 -9.184 -35.493 -28.403 1.00 70.06 C ANISOU 1680 CB LYS A 224 8405 10208 8006 860 33 1830 C ATOM 1681 N ALA A 225 -11.964 -34.279 -27.150 1.00 69.37 N ANISOU 1681 N ALA A 225 8525 10144 7686 659 4 1538 N ATOM 1682 CA ALA A 225 -12.658 -33.725 -25.993 1.00 64.85 C ANISOU 1682 CA ALA A 225 8003 9700 6937 616 -49 1498 C ATOM 1683 C ALA A 225 -13.988 -34.428 -25.749 1.00 60.45 C ANISOU 1683 C ALA A 225 7529 9035 6402 622 92 1503 C ATOM 1684 O ALA A 225 -14.363 -34.668 -24.596 1.00 86.58 O ANISOU 1684 O ALA A 225 10864 12446 9587 650 106 1592 O ATOM 1685 CB ALA A 225 -12.873 -32.223 -26.178 1.00 60.59 C ANISOU 1685 CB ALA A 225 7488 9217 6316 504 -167 1288 C ATOM 1686 N TYR A 226 -14.714 -34.766 -26.818 1.00 86.32 N ANISOU 1686 N TYR A 226 11470 12136 9193 -437 1060 1606 N ATOM 1687 CA TYR A 226 -15.996 -35.443 -26.649 1.00 85.53 C ANISOU 1687 CA TYR A 226 11558 12141 8798 -513 811 1421 C ATOM 1688 C TYR A 226 -15.805 -36.906 -26.268 1.00 84.85 C ANISOU 1688 C TYR A 226 11563 11985 8690 -449 1079 1261 C ATOM 1689 O TYR A 226 -16.563 -37.441 -25.450 1.00 83.02 O ANISOU 1689 O TYR A 226 11227 11836 8480 -436 855 1161 O ATOM 1690 CB TYR A 226 -16.832 -35.324 -27.924 1.00 88.75 C ANISOU 1690 CB TYR A 226 12418 12581 8720 -756 702 1444 C ATOM 1691 CG TYR A 226 -17.465 -33.963 -28.130 1.00 91.38 C ANISOU 1691 CG TYR A 226 12649 13009 9061 -810 295 1603 C ATOM 1692 CD1 TYR A 226 -17.253 -32.929 -27.227 1.00 85.28 C ANISOU 1692 CD1 TYR A 226 11475 12237 8690 -635 78 1677 C ATOM 1693 CD2 TYR A 226 -18.287 -33.718 -29.223 1.00 97.60 C ANISOU 1693 CD2 TYR A 226 13795 13848 9439 -1029 88 1681 C ATOM 1694 CE1 TYR A 226 -17.833 -31.686 -27.412 1.00 90.32 C ANISOU 1694 CE1 TYR A 226 12077 12898 9342 -639 -281 1817 C ATOM 1695 CE2 TYR A 226 -18.873 -32.480 -29.415 1.00100.70 C ANISOU 1695 CE2 TYR A 226 14088 14309 9867 -1042 -286 1862 C ATOM 1696 CZ TYR A 226 -18.643 -31.468 -28.507 1.00 94.52 C ANISOU 1696 CZ TYR A 226 12907 13498 9507 -827 -444 1925 C ATOM 1697 OH TYR A 226 -19.224 -30.235 -28.695 1.00 88.76 O ANISOU 1697 OH TYR A 226 12131 12774 8819 -796 -802 2098 O ATOM 1698 N ASP A 227 -14.803 -37.571 -26.850 1.00 87.36 N ANISOU 1698 N ASP A 227 12081 12139 8973 -381 1592 1268 N ATOM 1699 CA ASP A 227 -14.529 -38.955 -26.477 1.00 87.98 C ANISOU 1699 CA ASP A 227 12274 12087 9069 -267 1870 1129 C ATOM 1700 C ASP A 227 -14.050 -39.063 -25.036 1.00 93.49 C ANISOU 1700 C ASP A 227 12445 12823 10252 -54 1778 1165 C ATOM 1701 O ASP A 227 -14.312 -40.072 -24.371 1.00 96.21 O ANISOU 1701 O ASP A 227 12814 13124 10616 1 1774 1055 O ATOM 1702 CB ASP A 227 -13.496 -39.568 -27.423 1.00 99.27 C ANISOU 1702 CB ASP A 227 14042 13311 10367 -141 2513 1153 C ATOM 1703 CG ASP A 227 -14.067 -39.872 -28.795 1.00 99.32 C ANISOU 1703 CG ASP A 227 14793 13211 9733 -338 2612 1034 C ATOM 1704 OD1 ASP A 227 -15.276 -39.637 -29.004 1.00 94.39 O ANISOU 1704 OD1 ASP A 227 14358 12685 8822 -619 2115 961 O ATOM 1705 OD2 ASP A 227 -13.307 -40.349 -29.663 1.00 99.56 O ANISOU 1705 OD2 ASP A 227 15235 13059 9536 -194 3184 1034 O ATOM 1706 N LEU A 228 -13.348 -38.041 -24.538 1.00 95.56 N ANISOU 1706 N LEU A 228 12273 13141 10895 42 1663 1334 N ATOM 1707 CA LEU A 228 -12.922 -38.049 -23.143 1.00 82.88 C ANISOU 1707 CA LEU A 228 10240 11560 9692 217 1462 1366 C ATOM 1708 C LEU A 228 -14.118 -37.962 -22.203 1.00 84.28 C ANISOU 1708 C LEU A 228 10394 11886 9744 210 1017 1231 C ATOM 1709 O LEU A 228 -14.161 -38.654 -21.179 1.00 92.04 O ANISOU 1709 O LEU A 228 11261 12885 10826 342 962 1184 O ATOM 1710 CB LEU A 228 -11.953 -36.897 -22.883 1.00 87.79 C ANISOU 1710 CB LEU A 228 10472 12158 10727 248 1327 1584 C ATOM 1711 CG LEU A 228 -11.515 -36.704 -21.430 1.00 87.26 C ANISOU 1711 CG LEU A 228 10035 12088 11030 386 971 1617 C ATOM 1712 CD1 LEU A 228 -10.714 -37.903 -20.946 1.00 84.11 C ANISOU 1712 CD1 LEU A 228 9474 11621 10861 566 1258 1674 C ATOM 1713 CD2 LEU A 228 -10.720 -35.418 -21.270 1.00 95.71 C ANISOU 1713 CD2 LEU A 228 10807 13082 12476 313 687 1827 C ATOM 1714 N GLU A 229 -15.097 -37.118 -22.535 1.00 84.33 N ANISOU 1714 N GLU A 229 10498 12008 9537 88 726 1211 N ATOM 1715 CA GLU A 229 -16.285 -36.996 -21.697 1.00 77.45 C ANISOU 1715 CA GLU A 229 9560 11307 8559 140 386 1144 C ATOM 1716 C GLU A 229 -17.093 -38.288 -21.693 1.00 80.43 C ANISOU 1716 C GLU A 229 10097 11735 8729 42 479 1076 C ATOM 1717 O GLU A 229 -17.629 -38.688 -20.653 1.00 78.74 O ANISOU 1717 O GLU A 229 9739 11632 8548 154 367 1071 O ATOM 1718 CB GLU A 229 -17.145 -35.826 -22.173 1.00 86.48 C ANISOU 1718 CB GLU A 229 10746 12551 9561 69 96 1192 C ATOM 1719 CG GLU A 229 -18.335 -35.523 -21.277 1.00104.20 C ANISOU 1719 CG GLU A 229 12858 14988 11745 220 -194 1183 C ATOM 1720 CD GLU A 229 -19.170 -34.367 -21.790 1.00115.48 C ANISOU 1720 CD GLU A 229 14307 16496 13076 209 -456 1267 C ATOM 1721 OE1 GLU A 229 -20.381 -34.562 -22.028 1.00116.75 O ANISOU 1721 OE1 GLU A 229 14447 16840 13073 140 -569 1341 O ATOM 1722 OE2 GLU A 229 -18.613 -33.263 -21.963 1.00117.67 O ANISOU 1722 OE2 GLU A 229 14599 16636 13474 258 -571 1300 O ATOM 1723 N ASP A 230 -17.189 -38.955 -22.846 1.00 96.99 N ANISOU 1723 N ASP A 230 12538 13725 10588 -178 676 1036 N ATOM 1724 CA ASP A 230 -17.909 -40.222 -22.905 1.00114.13 C ANISOU 1724 CA ASP A 230 14931 15857 12576 -340 701 973 C ATOM 1725 C ASP A 230 -17.197 -41.311 -22.115 1.00104.31 C ANISOU 1725 C ASP A 230 13643 14466 11524 -172 955 934 C ATOM 1726 O ASP A 230 -17.847 -42.234 -21.612 1.00101.84 O ANISOU 1726 O ASP A 230 13365 14151 11177 -246 893 934 O ATOM 1727 CB ASP A 230 -18.098 -40.656 -24.359 1.00131.44 C ANISOU 1727 CB ASP A 230 17644 17890 14407 -618 801 903 C ATOM 1728 CG ASP A 230 -19.052 -39.754 -25.115 1.00139.30 C ANISOU 1728 CG ASP A 230 18702 19046 15177 -834 452 983 C ATOM 1729 OD1 ASP A 230 -19.555 -38.785 -24.510 1.00137.75 O ANISOU 1729 OD1 ASP A 230 18121 19073 15143 -725 182 1095 O ATOM 1730 OD2 ASP A 230 -19.301 -40.015 -26.310 1.00144.57 O ANISOU 1730 OD2 ASP A 230 19848 19599 15484 -1088 439 939 O ATOM 1731 N ASN A 231 -15.870 -41.226 -21.996 1.00 97.32 N ANISOU 1731 N ASN A 231 12646 13453 10877 45 1227 954 N ATOM 1732 CA ASN A 231 -15.144 -42.190 -21.177 1.00 94.95 C ANISOU 1732 CA ASN A 231 12244 13022 10813 248 1430 969 C ATOM 1733 C ASN A 231 -15.436 -41.983 -19.696 1.00100.79 C ANISOU 1733 C ASN A 231 12636 13941 11718 400 1134 1034 C ATOM 1734 O ASN A 231 -15.618 -42.955 -18.953 1.00108.99 O ANISOU 1734 O ASN A 231 13682 14942 12789 458 1165 1053 O ATOM 1735 CB ASN A 231 -13.643 -42.093 -21.450 1.00 89.81 C ANISOU 1735 CB ASN A 231 11467 12220 10438 453 1779 1057 C ATOM 1736 CG ASN A 231 -13.264 -42.638 -22.813 1.00 92.48 C ANISOU 1736 CG ASN A 231 12241 12338 10560 412 2235 998 C ATOM 1737 OD1 ASN A 231 -13.942 -43.511 -23.356 1.00 88.13 O ANISOU 1737 OD1 ASN A 231 12171 11641 9675 259 2298 846 O ATOM 1738 ND2 ASN A 231 -12.173 -42.128 -23.372 1.00104.02 N ANISOU 1738 ND2 ASN A 231 13566 13757 12200 546 2553 1138 N ATOM 1739 N TRP A 232 -15.487 -40.726 -19.248 1.00 97.99 N ANISOU 1739 N TRP A 232 12043 13753 11437 479 851 1072 N ATOM 1740 CA TRP A 232 -15.849 -40.457 -17.860 1.00 98.79 C ANISOU 1740 CA TRP A 232 11946 14011 11580 665 579 1102 C ATOM 1741 C TRP A 232 -17.313 -40.787 -17.601 1.00 96.67 C ANISOU 1741 C TRP A 232 11728 13935 11069 584 481 1118 C ATOM 1742 O TRP A 232 -17.660 -41.290 -16.526 1.00109.16 O ANISOU 1742 O TRP A 232 13229 15611 12637 721 450 1182 O ATOM 1743 CB TRP A 232 -15.560 -38.997 -17.508 1.00100.45 C ANISOU 1743 CB TRP A 232 12012 14272 11883 779 283 1105 C ATOM 1744 CG TRP A 232 -14.101 -38.674 -17.421 1.00 98.82 C ANISOU 1744 CG TRP A 232 11638 13896 12012 842 280 1179 C ATOM 1745 CD1 TRP A 232 -13.392 -37.854 -18.248 1.00105.28 C ANISOU 1745 CD1 TRP A 232 12386 14615 13002 735 300 1250 C ATOM 1746 CD2 TRP A 232 -13.169 -39.169 -16.451 1.00103.19 C ANISOU 1746 CD2 TRP A 232 12022 14370 12814 1006 233 1262 C ATOM 1747 NE1 TRP A 232 -12.077 -37.804 -17.852 1.00110.51 N ANISOU 1747 NE1 TRP A 232 12788 15151 14052 805 271 1396 N ATOM 1748 CE2 TRP A 232 -11.914 -38.604 -16.752 1.00106.20 C ANISOU 1748 CE2 TRP A 232 12177 14614 13560 975 202 1400 C ATOM 1749 CE3 TRP A 232 -13.275 -40.035 -15.358 1.00108.70 C ANISOU 1749 CE3 TRP A 232 12722 15104 13474 1168 199 1278 C ATOM 1750 CZ2 TRP A 232 -10.773 -38.876 -16.000 1.00112.06 C ANISOU 1750 CZ2 TRP A 232 12654 15261 14662 1090 92 1563 C ATOM 1751 CZ3 TRP A 232 -12.141 -40.304 -14.612 1.00112.56 C ANISOU 1751 CZ3 TRP A 232 13018 15487 14264 1302 92 1410 C ATOM 1752 CH2 TRP A 232 -10.907 -39.726 -14.937 1.00114.24 C ANISOU 1752 CH2 TRP A 232 12966 15569 14869 1258 18 1554 C ATOM 1753 N GLU A 233 -18.186 -40.511 -18.573 1.00 95.96 N ANISOU 1753 N GLU A 233 11745 13916 10800 357 424 1112 N ATOM 1754 CA GLU A 233 -19.594 -40.862 -18.421 1.00 93.94 C ANISOU 1754 CA GLU A 233 11441 13856 10395 232 310 1214 C ATOM 1755 C GLU A 233 -19.793 -42.372 -18.398 1.00 87.67 C ANISOU 1755 C GLU A 233 10787 12936 9586 46 456 1251 C ATOM 1756 O GLU A 233 -20.753 -42.860 -17.790 1.00 89.54 O ANISOU 1756 O GLU A 233 10886 13332 9805 -5 391 1410 O ATOM 1757 CB GLU A 233 -20.418 -40.234 -19.544 1.00105.52 C ANISOU 1757 CB GLU A 233 12973 15409 11711 -3 142 1245 C ATOM 1758 N THR A 234 -18.903 -43.124 -19.049 1.00 87.89 N ANISOU 1758 N THR A 234 11097 12662 9636 -40 677 1136 N ATOM 1759 CA THR A 234 -18.995 -44.579 -19.010 1.00 89.50 C ANISOU 1759 CA THR A 234 11523 12647 9834 -186 813 1147 C ATOM 1760 C THR A 234 -18.584 -45.117 -17.644 1.00 88.78 C ANISOU 1760 C THR A 234 11236 12568 9928 82 898 1247 C ATOM 1761 O THR A 234 -19.167 -46.090 -17.151 1.00 87.66 O ANISOU 1761 O THR A 234 11124 12392 9791 -26 898 1370 O ATOM 1762 CB THR A 234 -18.130 -45.189 -20.114 1.00 93.72 C ANISOU 1762 CB THR A 234 12495 12813 10300 -259 1085 980 C ATOM 1763 OG1 THR A 234 -18.513 -44.639 -21.381 1.00113.53 O ANISOU 1763 OG1 THR A 234 15254 15323 12558 -501 991 898 O ATOM 1764 CG2 THR A 234 -18.296 -46.701 -20.159 1.00 85.23 C ANISOU 1764 CG2 THR A 234 11772 11421 9189 -416 1194 960 C ATOM 1765 N LEU A 235 -17.587 -44.490 -17.014 1.00 90.55 N ANISOU 1765 N LEU A 235 11269 12827 10308 403 928 1230 N ATOM 1766 CA LEU A 235 -17.145 -44.937 -15.696 1.00 91.72 C ANISOU 1766 CA LEU A 235 11270 12989 10591 663 939 1339 C ATOM 1767 C LEU A 235 -18.206 -44.669 -14.635 1.00 97.81 C ANISOU 1767 C LEU A 235 11867 14071 11225 744 769 1481 C ATOM 1768 O LEU A 235 -18.456 -45.519 -13.772 1.00102.75 O ANISOU 1768 O LEU A 235 12481 14711 11850 800 825 1636 O ATOM 1769 CB LEU A 235 -15.832 -44.250 -15.321 1.00 92.10 C ANISOU 1769 CB LEU A 235 11154 12992 10847 931 902 1316 C ATOM 1770 CG LEU A 235 -14.629 -44.488 -16.235 1.00 95.94 C ANISOU 1770 CG LEU A 235 11699 13211 11544 944 1161 1271 C ATOM 1771 CD1 LEU A 235 -13.430 -43.681 -15.762 1.00 94.97 C ANISOU 1771 CD1 LEU A 235 11282 13097 11706 1154 1033 1347 C ATOM 1772 CD2 LEU A 235 -14.288 -45.965 -16.299 1.00100.77 C ANISOU 1772 CD2 LEU A 235 12504 13543 12242 976 1452 1309 C ATOM 1773 N ASN A 236 -18.838 -43.495 -14.682 1.00103.03 N ANISOU 1773 N ASN A 236 12404 14975 11766 787 600 1461 N ATOM 1774 CA ASN A 236 -19.831 -43.149 -13.668 1.00110.27 C ANISOU 1774 CA ASN A 236 13162 16199 12534 969 527 1614 C ATOM 1775 C ASN A 236 -21.109 -43.960 -13.842 1.00109.84 C ANISOU 1775 C ASN A 236 13021 16273 12440 705 595 1834 C ATOM 1776 O ASN A 236 -21.726 -44.374 -12.853 1.00117.00 O ANISOU 1776 O ASN A 236 13800 17364 13292 827 676 2062 O ATOM 1777 CB ASN A 236 -20.133 -41.652 -13.718 1.00122.46 C ANISOU 1777 CB ASN A 236 14634 17913 13981 1145 356 1533 C ATOM 1778 CG ASN A 236 -18.927 -40.803 -13.366 1.00130.27 C ANISOU 1778 CG ASN A 236 15705 18756 15034 1368 201 1364 C ATOM 1779 OD1 ASN A 236 -17.788 -41.263 -13.433 1.00129.06 O ANISOU 1779 OD1 ASN A 236 15591 18384 15060 1331 230 1319 O ATOM 1780 ND2 ASN A 236 -19.174 -39.554 -12.986 1.00134.81 N ANISOU 1780 ND2 ASN A 236 16302 19429 15492 1604 18 1299 N ATOM 1781 N ASP A 237 -21.526 -44.194 -15.088 1.00104.17 N ANISOU 1781 N ASP A 237 12382 15455 11742 322 542 1804 N ATOM 1782 CA ASP A 237 -22.741 -44.969 -15.322 1.00109.90 C ANISOU 1782 CA ASP A 237 13012 16265 12480 -24 495 2050 C ATOM 1783 C ASP A 237 -22.546 -46.433 -14.948 1.00111.52 C ANISOU 1783 C ASP A 237 13372 16228 12771 -178 619 2151 C ATOM 1784 O ASP A 237 -23.466 -47.073 -14.428 1.00112.71 O ANISOU 1784 O ASP A 237 13339 16512 12975 -323 624 2464 O ATOM 1785 CB ASP A 237 -23.180 -44.839 -16.780 1.00128.24 C ANISOU 1785 CB ASP A 237 15474 18493 14757 -430 304 1977 C ATOM 1786 CG ASP A 237 -23.698 -43.453 -17.111 1.00141.40 C ANISOU 1786 CG ASP A 237 16927 20434 16365 -311 147 1992 C ATOM 1787 OD1 ASP A 237 -23.713 -42.591 -16.208 1.00146.67 O ANISOU 1787 OD1 ASP A 237 17376 21329 17023 106 205 2028 O ATOM 1788 OD2 ASP A 237 -24.090 -43.227 -18.275 1.00144.46 O ANISOU 1788 OD2 ASP A 237 17421 20779 16688 -621 -52 1967 O ATOM 1789 N ASN A 238 -21.356 -46.982 -15.205 1.00111.46 N ANISOU 1789 N ASN A 238 13680 15857 12813 -135 739 1934 N ATOM 1790 CA ASN A 238 -21.097 -48.373 -14.844 1.00117.86 C ANISOU 1790 CA ASN A 238 14684 16375 13724 -226 864 2026 C ATOM 1791 C ASN A 238 -20.896 -48.538 -13.343 1.00124.78 C ANISOU 1791 C ASN A 238 15365 17413 14633 123 966 2227 C ATOM 1792 O ASN A 238 -21.210 -49.600 -12.792 1.00133.17 O ANISOU 1792 O ASN A 238 16463 18375 15762 16 1033 2460 O ATOM 1793 CB ASN A 238 -19.882 -48.900 -15.607 1.00112.87 C ANISOU 1793 CB ASN A 238 14446 15293 13145 -202 1019 1761 C ATOM 1794 CG ASN A 238 -20.201 -49.230 -17.051 1.00123.17 C ANISOU 1794 CG ASN A 238 16141 16327 14330 -601 954 1597 C ATOM 1795 OD1 ASN A 238 -20.445 -50.386 -17.396 1.00119.78 O ANISOU 1795 OD1 ASN A 238 16067 15545 13899 -884 948 1610 O ATOM 1796 ND2 ASN A 238 -20.211 -48.211 -17.902 1.00131.54 N ANISOU 1796 ND2 ASN A 238 17201 17519 15260 -637 872 1445 N ATOM 1797 N LEU A 239 -20.372 -47.512 -12.667 1.00114.42 N ANISOU 1797 N LEU A 239 13904 16319 13253 521 947 2150 N ATOM 1798 CA LEU A 239 -20.250 -47.576 -11.215 1.00 94.80 C ANISOU 1798 CA LEU A 239 11324 14002 10695 863 992 2332 C ATOM 1799 C LEU A 239 -21.616 -47.625 -10.545 1.00 94.42 C ANISOU 1799 C LEU A 239 11052 14303 10520 843 1054 2663 C ATOM 1800 O LEU A 239 -21.777 -48.284 -9.511 1.00107.61 O ANISOU 1800 O LEU A 239 12708 16040 12138 968 1173 2928 O ATOM 1801 CB LEU A 239 -19.443 -46.383 -10.701 1.00 86.98 C ANISOU 1801 CB LEU A 239 10311 13121 9616 1246 865 2152 C ATOM 1802 N LYS A 240 -22.610 -46.941 -11.118 1.00 91.30 N ANISOU 1802 N LYS A 240 10453 14145 10090 704 994 2705 N ATOM 1803 CA LYS A 240 -23.967 -47.033 -10.593 1.00 99.55 C ANISOU 1803 CA LYS A 240 11181 15545 11099 676 1099 3107 C ATOM 1804 C LYS A 240 -24.593 -48.387 -10.901 1.00109.38 C ANISOU 1804 C LYS A 240 12382 16632 12547 179 1104 3404 C ATOM 1805 O LYS A 240 -25.480 -48.838 -10.169 1.00107.38 O ANISOU 1805 O LYS A 240 11863 16613 12321 154 1248 3843 O ATOM 1806 CB LYS A 240 -24.829 -45.906 -11.162 1.00 96.16 C ANISOU 1806 CB LYS A 240 10492 15404 10641 690 1011 3115 C ATOM 1807 N VAL A 241 -24.151 -49.043 -11.976 1.00120.41 N ANISOU 1807 N VAL A 241 14067 17609 14074 -214 956 3191 N ATOM 1808 CA VAL A 241 -24.649 -50.378 -12.289 1.00129.74 C ANISOU 1808 CA VAL A 241 15347 18515 15432 -715 892 3422 C ATOM 1809 C VAL A 241 -24.124 -51.392 -11.279 1.00131.53 C ANISOU 1809 C VAL A 241 15722 18551 15703 -567 1077 3586 C ATOM 1810 O VAL A 241 -24.846 -52.306 -10.863 1.00139.88 O ANISOU 1810 O VAL A 241 16672 19586 16889 -835 1105 3993 O ATOM 1811 CB VAL A 241 -24.275 -50.762 -13.733 1.00129.03 C ANISOU 1811 CB VAL A 241 15683 17967 15376 -1113 691 3090 C ATOM 1812 CG1 VAL A 241 -24.592 -52.226 -14.000 1.00133.14 C ANISOU 1812 CG1 VAL A 241 16483 18055 16047 -1604 590 3254 C ATOM 1813 CG2 VAL A 241 -25.007 -49.873 -14.723 1.00132.16 C ANISOU 1813 CG2 VAL A 241 15927 18571 15718 -1340 450 3034 C ATOM 1814 N ILE A 242 -22.864 -51.242 -10.862 1.00121.45 N ANISOU 1814 N ILE A 242 14666 17132 14349 -156 1178 3325 N ATOM 1815 CA ILE A 242 -22.289 -52.160 -9.882 1.00121.11 C ANISOU 1815 CA ILE A 242 14767 16906 14343 28 1315 3500 C ATOM 1816 C ILE A 242 -23.002 -52.025 -8.543 1.00130.13 C ANISOU 1816 C ILE A 242 15623 18485 15336 263 1464 3921 C ATOM 1817 O ILE A 242 -23.257 -53.022 -7.854 1.00141.63 O ANISOU 1817 O ILE A 242 17099 19859 16855 177 1573 4289 O ATOM 1818 CB ILE A 242 -20.774 -51.916 -9.745 1.00110.58 C ANISOU 1818 CB ILE A 242 13647 15369 13000 423 1332 3180 C ATOM 1819 CG1 ILE A 242 -20.077 -52.116 -11.092 1.00110.60 C ANISOU 1819 CG1 ILE A 242 13932 14949 13142 241 1303 2822 C ATOM 1820 CG2 ILE A 242 -20.173 -52.838 -8.695 1.00105.35 C ANISOU 1820 CG2 ILE A 242 13111 14532 12384 640 1424 3405 C ATOM 1821 CD1 ILE A 242 -18.584 -51.872 -11.051 1.00107.59 C ANISOU 1821 CD1 ILE A 242 13645 14389 12845 620 1358 2592 C ATOM 1822 N GLU A 243 -23.341 -50.793 -8.154 1.00121.88 N ANISOU 1822 N GLU A 243 14352 17887 14071 589 1500 3889 N ATOM 1823 CA GLU A 243 -24.052 -50.584 -6.897 1.00107.29 C ANISOU 1823 CA GLU A 243 12296 16469 12000 901 1723 4278 C ATOM 1824 C GLU A 243 -25.462 -51.159 -6.945 1.00111.14 C ANISOU 1824 C GLU A 243 12413 17158 12657 532 1850 4800 C ATOM 1825 O GLU A 243 -26.003 -51.556 -5.907 1.00108.19 O ANISOU 1825 O GLU A 243 11894 17025 12188 675 2108 5265 O ATOM 1826 CB GLU A 243 -24.097 -49.093 -6.562 1.00100.22 C ANISOU 1826 CB GLU A 243 11337 15932 10810 1372 1739 4077 C ATOM 1827 N LYS A 244 -26.068 -51.214 -8.129 1.00123.32 N ANISOU 1827 N LYS A 244 13794 18611 14451 42 1655 4777 N ATOM 1828 CA LYS A 244 -27.402 -51.772 -8.301 1.00144.89 C ANISOU 1828 CA LYS A 244 16116 21501 17436 -417 1659 5313 C ATOM 1829 C LYS A 244 -27.382 -53.212 -8.795 1.00168.14 C ANISOU 1829 C LYS A 244 19285 23931 20670 -1032 1467 5443 C ATOM 1830 O LYS A 244 -28.448 -53.774 -9.068 1.00167.96 O ANISOU 1830 O LYS A 244 18953 23943 20920 -1549 1354 5894 O ATOM 1831 CB LYS A 244 -28.215 -50.907 -9.271 1.00140.24 C ANISOU 1831 CB LYS A 244 15190 21146 16950 -613 1469 5280 C ATOM 1832 CG LYS A 244 -28.391 -49.464 -8.823 1.00133.93 C ANISOU 1832 CG LYS A 244 14173 20818 15897 -3 1662 5195 C ATOM 1833 CD LYS A 244 -29.151 -49.379 -7.510 1.00132.05 C ANISOU 1833 CD LYS A 244 13585 21054 15533 406 2097 5729 C ATOM 1834 CE LYS A 244 -29.355 -47.934 -7.084 1.00121.10 C ANISOU 1834 CE LYS A 244 12091 20069 13852 1068 2306 5609 C ATOM 1835 NZ LYS A 244 -30.134 -47.832 -5.820 1.00116.55 N ANISOU 1835 NZ LYS A 244 11239 19961 13085 1549 2817 6135 N ATOM 1836 N ALA A 245 -26.205 -53.821 -8.917 1.00182.89 N ANISOU 1836 N ALA A 245 21681 25298 22510 -986 1412 5086 N ATOM 1837 CA ALA A 245 -26.103 -55.188 -9.399 1.00187.85 C ANISOU 1837 CA ALA A 245 22652 25341 23383 -1498 1246 5149 C ATOM 1838 C ALA A 245 -26.487 -56.178 -8.303 1.00182.94 C ANISOU 1838 C ALA A 245 21922 24718 22869 -1560 1430 5732 C ATOM 1839 O ALA A 245 -26.468 -55.865 -7.109 1.00180.09 O ANISOU 1839 O ALA A 245 21365 24750 22312 -1091 1729 5984 O ATOM 1840 CB ALA A 245 -24.688 -55.479 -9.898 1.00190.73 C ANISOU 1840 CB ALA A 245 23603 25170 23697 -1326 1206 4602 C ATOM 1841 N ASP A 246 -26.836 -57.394 -8.728 1.00180.95 N ANISOU 1841 N ASP A 246 21867 23982 22904 -2158 1231 5950 N ATOM 1842 CA ASP A 246 -27.247 -58.442 -7.807 1.00178.36 C ANISOU 1842 CA ASP A 246 21457 23570 22742 -2327 1365 6559 C ATOM 1843 C ASP A 246 -26.484 -59.749 -7.983 1.00179.42 C ANISOU 1843 C ASP A 246 22228 22917 23027 -2526 1248 6440 C ATOM 1844 O ASP A 246 -26.698 -60.677 -7.197 1.00195.25 O ANISOU 1844 O ASP A 246 24240 24774 25174 -2648 1350 6942 O ATOM 1845 CB ASP A 246 -28.753 -58.717 -7.946 1.00181.43 C ANISOU 1845 CB ASP A 246 21311 24182 23442 -2951 1232 7199 C ATOM 1846 CG ASP A 246 -29.603 -57.532 -7.526 1.00181.43 C ANISOU 1846 CG ASP A 246 20599 25002 23334 -2649 1469 7485 C ATOM 1847 OD1 ASP A 246 -29.159 -56.761 -6.650 1.00178.79 O ANISOU 1847 OD1 ASP A 246 20211 25072 22649 -1936 1835 7383 O ATOM 1848 OD2 ASP A 246 -30.715 -57.373 -8.071 1.00185.72 O ANISOU 1848 OD2 ASP A 246 20658 25762 24145 -3115 1269 7825 O ATOM 1849 N ASN A 247 -25.609 -59.853 -8.981 1.00168.32 N ANISOU 1849 N ASN A 247 21371 20991 21592 -2528 1075 5824 N ATOM 1850 CA ASN A 247 -24.813 -61.056 -9.175 1.00161.35 C ANISOU 1850 CA ASN A 247 21145 19322 20839 -2597 1028 5675 C ATOM 1851 C ASN A 247 -23.449 -60.664 -9.727 1.00152.03 C ANISOU 1851 C ASN A 247 20370 17898 19495 -2101 1123 5012 C ATOM 1852 O ASN A 247 -23.197 -59.502 -10.056 1.00147.85 O ANISOU 1852 O ASN A 247 19633 17770 18775 -1824 1160 4677 O ATOM 1853 CB ASN A 247 -25.522 -62.060 -10.095 1.00163.15 C ANISOU 1853 CB ASN A 247 21738 18932 21320 -3395 649 5761 C ATOM 1854 CG ASN A 247 -25.970 -61.444 -11.410 1.00162.46 C ANISOU 1854 CG ASN A 247 21709 18864 21155 -3764 327 5394 C ATOM 1855 OD1 ASN A 247 -25.286 -60.595 -11.981 1.00159.61 O ANISOU 1855 OD1 ASN A 247 21463 18625 20555 -3391 410 4864 O ATOM 1856 ND2 ASN A 247 -27.128 -61.873 -11.897 1.00165.39 N ANISOU 1856 ND2 ASN A 247 21990 19109 21740 -4532 -76 5722 N ATOM 1857 N ALA A 248 -22.564 -61.658 -9.826 1.00146.35 N ANISOU 1857 N ALA A 248 20218 16501 18888 -1979 1178 4867 N ATOM 1858 CA ALA A 248 -21.208 -61.406 -10.298 1.00135.95 C ANISOU 1858 CA ALA A 248 19227 14936 17490 -1463 1339 4340 C ATOM 1859 C ALA A 248 -21.146 -61.168 -11.801 1.00139.24 C ANISOU 1859 C ALA A 248 20040 15054 17811 -1692 1217 3820 C ATOM 1860 O ALA A 248 -20.164 -60.592 -12.283 1.00132.63 O ANISOU 1860 O ALA A 248 19303 14218 16871 -1267 1391 3408 O ATOM 1861 CB ALA A 248 -20.293 -62.572 -9.919 1.00129.00 C ANISOU 1861 CB ALA A 248 18799 13420 16793 -1192 1483 4408 C ATOM 1862 N ALA A 249 -22.163 -61.597 -12.551 1.00147.98 N ANISOU 1862 N ALA A 249 21378 15904 18944 -2369 903 3865 N ATOM 1863 CA ALA A 249 -22.150 -61.393 -13.996 1.00156.47 C ANISOU 1863 CA ALA A 249 22935 16675 19842 -2610 740 3376 C ATOM 1864 C ALA A 249 -22.340 -59.924 -14.350 1.00154.60 C ANISOU 1864 C ALA A 249 22212 17127 19404 -2496 721 3199 C ATOM 1865 O ALA A 249 -21.660 -59.401 -15.241 1.00145.09 O ANISOU 1865 O ALA A 249 21288 15833 18005 -2273 823 2737 O ATOM 1866 CB ALA A 249 -23.229 -62.250 -14.658 1.00163.04 C ANISOU 1866 CB ALA A 249 24176 17027 20745 -3429 286 3507 C ATOM 1867 N GLN A 250 -23.261 -59.242 -13.664 1.00157.88 N ANISOU 1867 N GLN A 250 21908 18217 19862 -2617 626 3587 N ATOM 1868 CA GLN A 250 -23.475 -57.822 -13.919 1.00155.14 C ANISOU 1868 CA GLN A 250 21104 18499 19344 -2463 611 3449 C ATOM 1869 C GLN A 250 -22.276 -56.987 -13.490 1.00154.58 C ANISOU 1869 C GLN A 250 20886 18685 19164 -1746 938 3190 C ATOM 1870 O GLN A 250 -21.975 -55.966 -14.120 1.00160.40 O ANISOU 1870 O GLN A 250 21559 19642 19744 -1584 945 2876 O ATOM 1871 CB GLN A 250 -24.739 -57.348 -13.203 1.00152.76 C ANISOU 1871 CB GLN A 250 20079 18827 19134 -2669 504 3971 C ATOM 1872 CG GLN A 250 -26.013 -58.011 -13.699 1.00156.34 C ANISOU 1872 CG GLN A 250 20518 19112 19773 -3452 102 4311 C ATOM 1873 CD GLN A 250 -27.108 -58.027 -12.651 1.00156.25 C ANISOU 1873 CD GLN A 250 19782 19609 19976 -3594 143 5013 C ATOM 1874 OE1 GLN A 250 -26.873 -57.705 -11.486 1.00155.85 O ANISOU 1874 OE1 GLN A 250 19379 19961 19874 -3080 509 5223 O ATOM 1875 NE2 GLN A 250 -28.313 -58.406 -13.059 1.00155.94 N ANISOU 1875 NE2 GLN A 250 19525 19553 20171 -4294 -237 5411 N ATOM 1876 N VAL A 251 -21.581 -57.401 -12.429 1.00147.67 N ANISOU 1876 N VAL A 251 19955 17770 18382 -1343 1163 3352 N ATOM 1877 CA VAL A 251 -20.388 -56.681 -11.998 1.00133.63 C ANISOU 1877 CA VAL A 251 18039 16185 16549 -718 1377 3151 C ATOM 1878 C VAL A 251 -19.238 -56.929 -12.966 1.00140.91 C ANISOU 1878 C VAL A 251 19431 16608 17500 -529 1524 2733 C ATOM 1879 O VAL A 251 -18.429 -56.032 -13.234 1.00138.01 O ANISOU 1879 O VAL A 251 18932 16422 17083 -188 1631 2484 O ATOM 1880 CB VAL A 251 -20.016 -57.080 -10.558 1.00121.93 C ANISOU 1880 CB VAL A 251 16379 14808 15140 -368 1501 3496 C ATOM 1881 CG1 VAL A 251 -18.828 -56.264 -10.066 1.00118.01 C ANISOU 1881 CG1 VAL A 251 15706 14532 14598 215 1597 3329 C ATOM 1882 CG2 VAL A 251 -21.210 -56.901 -9.634 1.00115.74 C ANISOU 1882 CG2 VAL A 251 15184 14512 14281 -527 1452 3951 C ATOM 1883 N LYS A 252 -19.147 -58.146 -13.509 1.00146.56 N ANISOU 1883 N LYS A 252 20719 16666 18301 -735 1551 2672 N ATOM 1884 CA LYS A 252 -18.091 -58.453 -14.468 1.00148.28 C ANISOU 1884 CA LYS A 252 21455 16375 18511 -490 1784 2288 C ATOM 1885 C LYS A 252 -18.275 -57.687 -15.771 1.00142.63 C ANISOU 1885 C LYS A 252 20924 15724 17545 -681 1728 1924 C ATOM 1886 O LYS A 252 -17.287 -57.306 -16.410 1.00148.48 O ANISOU 1886 O LYS A 252 21807 16371 18237 -325 2000 1644 O ATOM 1887 CB LYS A 252 -18.047 -59.957 -14.739 1.00154.54 C ANISOU 1887 CB LYS A 252 22936 16381 19403 -646 1824 2291 C ATOM 1888 N ASP A 253 -19.523 -57.449 -16.179 1.00133.77 N ANISOU 1888 N ASP A 253 19771 14776 16278 -1236 1380 1977 N ATOM 1889 CA ASP A 253 -19.765 -56.700 -17.408 1.00124.20 C ANISOU 1889 CA ASP A 253 18749 13642 14799 -1442 1264 1672 C ATOM 1890 C ASP A 253 -19.424 -55.226 -17.233 1.00126.93 C ANISOU 1890 C ASP A 253 18509 14614 15104 -1108 1350 1627 C ATOM 1891 O ASP A 253 -18.850 -54.605 -18.134 1.00133.34 O ANISOU 1891 O ASP A 253 19498 15410 15754 -962 1486 1337 O ATOM 1892 CB ASP A 253 -21.219 -56.867 -17.847 1.00118.66 C ANISOU 1892 CB ASP A 253 18115 12960 14009 -2150 785 1815 C ATOM 1893 N ALA A 254 -19.764 -54.650 -16.078 1.00121.85 N ANISOU 1893 N ALA A 254 17218 14497 14581 -976 1282 1921 N ATOM 1894 CA ALA A 254 -19.496 -53.233 -15.854 1.00125.63 C ANISOU 1894 CA ALA A 254 17219 15507 15009 -676 1303 1869 C ATOM 1895 C ALA A 254 -18.018 -52.983 -15.585 1.00132.02 C ANISOU 1895 C ALA A 254 17973 16249 15939 -138 1588 1741 C ATOM 1896 O ALA A 254 -17.465 -51.969 -16.028 1.00130.03 O ANISOU 1896 O ALA A 254 17584 16178 15644 43 1643 1570 O ATOM 1897 CB ALA A 254 -20.350 -52.713 -14.699 1.00125.92 C ANISOU 1897 CB ALA A 254 16694 16078 15074 -656 1162 2205 C ATOM 1898 N LEU A 255 -17.360 -53.892 -14.860 1.00137.92 N ANISOU 1898 N LEU A 255 18793 16731 16877 106 1747 1873 N ATOM 1899 CA LEU A 255 -15.944 -53.708 -14.559 1.00141.60 C ANISOU 1899 CA LEU A 255 19121 17143 17538 607 1969 1838 C ATOM 1900 C LEU A 255 -15.079 -53.847 -15.805 1.00142.49 C ANISOU 1900 C LEU A 255 19594 16883 17662 731 2273 1567 C ATOM 1901 O LEU A 255 -14.045 -53.178 -15.916 1.00133.51 O ANISOU 1901 O LEU A 255 18206 15856 16666 1065 2436 1528 O ATOM 1902 CB LEU A 255 -15.499 -54.705 -13.489 1.00139.88 C ANISOU 1902 CB LEU A 255 18894 16722 17533 842 2035 2098 C ATOM 1903 N THR A 256 -15.479 -54.704 -16.747 1.00146.64 N ANISOU 1903 N THR A 256 20729 16954 18031 467 2353 1400 N ATOM 1904 CA THR A 256 -14.735 -54.824 -17.996 1.00142.89 C ANISOU 1904 CA THR A 256 20717 16119 17455 622 2702 1123 C ATOM 1905 C THR A 256 -14.895 -53.574 -18.852 1.00132.43 C ANISOU 1905 C THR A 256 19282 15132 15903 493 2644 955 C ATOM 1906 O THR A 256 -13.940 -53.129 -19.500 1.00137.47 O ANISOU 1906 O THR A 256 19930 15740 16561 791 2980 852 O ATOM 1907 CB THR A 256 -15.192 -56.066 -18.764 1.00142.31 C ANISOU 1907 CB THR A 256 21477 15412 17182 356 2739 950 C ATOM 1908 OG1 THR A 256 -15.039 -57.225 -17.936 1.00143.30 O ANISOU 1908 OG1 THR A 256 21711 15186 17552 477 2783 1140 O ATOM 1909 CG2 THR A 256 -14.368 -56.248 -20.032 1.00141.38 C ANISOU 1909 CG2 THR A 256 21958 14882 16878 616 3188 649 C ATOM 1910 N LYS A 257 -16.095 -52.987 -18.860 1.00116.43 N ANISOU 1910 N LYS A 257 17114 13436 13687 68 2238 978 N ATOM 1911 CA LYS A 257 -16.313 -51.759 -19.617 1.00105.28 C ANISOU 1911 CA LYS A 257 15582 12347 12073 -50 2136 859 C ATOM 1912 C LYS A 257 -15.594 -50.574 -18.986 1.00113.00 C ANISOU 1912 C LYS A 257 15919 13748 13267 288 2170 968 C ATOM 1913 O LYS A 257 -15.238 -49.622 -19.690 1.00119.32 O ANISOU 1913 O LYS A 257 16654 14692 13989 336 2241 876 O ATOM 1914 CB LYS A 257 -17.810 -51.474 -19.736 1.00 95.53 C ANISOU 1914 CB LYS A 257 14305 11350 10642 -558 1676 919 C ATOM 1915 CG LYS A 257 -18.578 -52.525 -20.520 1.00102.18 C ANISOU 1915 CG LYS A 257 15811 11753 11261 -1014 1505 819 C ATOM 1916 CD LYS A 257 -20.077 -52.289 -20.446 1.00108.29 C ANISOU 1916 CD LYS A 257 16358 12814 11974 -1531 998 1010 C ATOM 1917 CE LYS A 257 -20.843 -53.390 -21.162 1.00118.60 C ANISOU 1917 CE LYS A 257 18314 13639 13110 -2072 710 959 C ATOM 1918 NZ LYS A 257 -22.316 -53.198 -21.065 1.00119.97 N ANISOU 1918 NZ LYS A 257 18146 14115 13322 -2610 182 1248 N ATOM 1919 N MET A 258 -15.373 -50.609 -17.670 1.00108.96 N ANISOU 1919 N MET A 258 14980 13413 13008 502 2085 1176 N ATOM 1920 CA MET A 258 -14.635 -49.533 -17.017 1.00103.33 C ANISOU 1920 CA MET A 258 13746 13025 12490 795 2028 1270 C ATOM 1921 C MET A 258 -13.141 -49.628 -17.303 1.00105.65 C ANISOU 1921 C MET A 258 13972 13111 13058 1154 2377 1288 C ATOM 1922 O MET A 258 -12.471 -48.601 -17.456 1.00107.69 O ANISOU 1922 O MET A 258 13914 13556 13448 1277 2375 1315 O ATOM 1923 CB MET A 258 -14.891 -49.552 -15.510 1.00102.76 C ANISOU 1923 CB MET A 258 13340 13189 12517 911 1786 1484 C ATOM 1924 CG MET A 258 -16.286 -49.102 -15.113 1.00108.19 C ANISOU 1924 CG MET A 258 13919 14211 12976 663 1498 1544 C ATOM 1925 SD MET A 258 -16.496 -48.977 -13.327 1.00113.23 S ANISOU 1925 SD MET A 258 14237 15156 13629 905 1308 1798 S ATOM 1926 CE MET A 258 -15.262 -47.741 -12.928 1.00109.25 C ANISOU 1926 CE MET A 258 13458 14790 13263 1247 1174 1736 C ATOM 1927 N ARG A 259 -12.604 -50.848 -17.374 1.00105.61 N ANISOU 1927 N ARG A 259 14239 12707 13182 1334 2684 1313 N ATOM 1928 CA ARG A 259 -11.195 -51.011 -17.715 1.00106.39 C ANISOU 1928 CA ARG A 259 14234 12604 13584 1735 3101 1387 C ATOM 1929 C ARG A 259 -10.924 -50.579 -19.150 1.00115.67 C ANISOU 1929 C ARG A 259 15680 13693 14576 1714 3441 1213 C ATOM 1930 O ARG A 259 -9.882 -49.977 -19.437 1.00116.97 O ANISOU 1930 O ARG A 259 15508 13944 14992 1966 3689 1340 O ATOM 1931 CB ARG A 259 -10.766 -52.462 -17.499 1.00106.23 C ANISOU 1931 CB ARG A 259 14506 12129 13726 1985 3388 1457 C ATOM 1932 N ALA A 260 -11.851 -50.874 -20.064 1.00121.39 N ANISOU 1932 N ALA A 260 17013 14250 14862 1396 3436 963 N ATOM 1933 CA ALA A 260 -11.689 -50.437 -21.446 1.00125.23 C ANISOU 1933 CA ALA A 260 17857 14664 15060 1357 3724 794 C ATOM 1934 C ALA A 260 -11.840 -48.926 -21.567 1.00121.01 C ANISOU 1934 C ALA A 260 16887 14584 14507 1197 3466 849 C ATOM 1935 O ALA A 260 -11.146 -48.289 -22.368 1.00120.89 O ANISOU 1935 O ALA A 260 16830 14610 14490 1326 3773 879 O ATOM 1936 CB ALA A 260 -12.697 -51.153 -22.345 1.00124.78 C ANISOU 1936 CB ALA A 260 18631 14284 14497 1005 3654 516 C ATOM 1937 N ALA A 261 -12.740 -48.334 -20.779 1.00115.11 N ANISOU 1937 N ALA A 261 15826 14163 13746 943 2936 889 N ATOM 1938 CA ALA A 261 -12.909 -46.886 -20.811 1.00102.50 C ANISOU 1938 CA ALA A 261 13858 12942 12146 831 2667 937 C ATOM 1939 C ALA A 261 -11.730 -46.168 -20.169 1.00108.22 C ANISOU 1939 C ALA A 261 13989 13815 13314 1121 2700 1151 C ATOM 1940 O ALA A 261 -11.403 -45.043 -20.562 1.00114.29 O ANISOU 1940 O ALA A 261 14535 14749 14141 1089 2655 1210 O ATOM 1941 CB ALA A 261 -14.213 -46.490 -20.118 1.00 91.00 C ANISOU 1941 CB ALA A 261 12262 11765 10549 564 2153 934 C ATOM 1942 N ALA A 262 -11.082 -46.797 -19.185 1.00118.62 N ANISOU 1942 N ALA A 262 15050 15056 14965 1376 2727 1303 N ATOM 1943 CA ALA A 262 -9.925 -46.176 -18.550 1.00120.90 C ANISOU 1943 CA ALA A 262 14762 15461 15714 1607 2663 1552 C ATOM 1944 C ALA A 262 -8.728 -46.125 -19.490 1.00125.73 C ANISOU 1944 C ALA A 262 15259 15936 16576 1818 3181 1697 C ATOM 1945 O ALA A 262 -7.925 -45.188 -19.417 1.00126.91 O ANISOU 1945 O ALA A 262 14924 16232 17063 1858 3099 1917 O ATOM 1946 CB ALA A 262 -9.563 -46.924 -17.267 1.00122.20 C ANISOU 1946 CB ALA A 262 14709 15575 16147 1820 2515 1713 C ATOM 1947 N LEU A 263 -8.591 -47.117 -20.373 1.00134.12 N ANISOU 1947 N LEU A 263 16782 16699 17479 1961 3724 1599 N ATOM 1948 CA LEU A 263 -7.485 -47.105 -21.325 1.00137.27 C ANISOU 1948 CA LEU A 263 17120 16977 18061 2239 4346 1760 C ATOM 1949 C LEU A 263 -7.724 -46.087 -22.434 1.00135.99 C ANISOU 1949 C LEU A 263 17118 16953 17599 2017 4430 1689 C ATOM 1950 O LEU A 263 -6.783 -45.428 -22.893 1.00137.22 O ANISOU 1950 O LEU A 263 16902 17198 18039 2148 4725 1956 O ATOM 1951 CB LEU A 263 -7.279 -48.502 -21.909 1.00141.74 C ANISOU 1951 CB LEU A 263 18257 17123 18474 2534 4940 1645 C ATOM 1952 CG LEU A 263 -6.984 -49.614 -20.899 1.00138.51 C ANISOU 1952 CG LEU A 263 17741 16508 18377 2797 4918 1751 C ATOM 1953 CD1 LEU A 263 -6.711 -50.931 -21.610 1.00144.24 C ANISOU 1953 CD1 LEU A 263 19112 16739 18952 3136 5561 1629 C ATOM 1954 CD2 LEU A 263 -5.819 -49.232 -19.998 1.00136.16 C ANISOU 1954 CD2 LEU A 263 16569 16400 18764 3059 4821 2183 C ATOM 1955 N ASP A 264 -8.975 -45.947 -22.880 1.00131.54 N ANISOU 1955 N ASP A 264 17074 16412 16492 1669 4161 1387 N ATOM 1956 CA ASP A 264 -9.293 -44.926 -23.873 1.00130.73 C ANISOU 1956 CA ASP A 264 17130 16455 16086 1438 4147 1344 C ATOM 1957 C ASP A 264 -9.128 -43.527 -23.295 1.00120.46 C ANISOU 1957 C ASP A 264 15193 15467 15110 1300 3700 1545 C ATOM 1958 O ASP A 264 -8.668 -42.612 -23.988 1.00116.38 O ANISOU 1958 O ASP A 264 14530 15040 14647 1258 3846 1708 O ATOM 1959 CB ASP A 264 -10.715 -45.126 -24.400 1.00139.97 C ANISOU 1959 CB ASP A 264 18948 17583 16651 1081 3858 1025 C ATOM 1960 CG ASP A 264 -10.816 -46.271 -25.387 1.00158.92 C ANISOU 1960 CG ASP A 264 22164 19604 18614 1145 4298 806 C ATOM 1961 OD1 ASP A 264 -10.571 -47.429 -24.987 1.00166.20 O ANISOU 1961 OD1 ASP A 264 23255 20248 19646 1353 4499 755 O ATOM 1962 OD2 ASP A 264 -11.143 -46.014 -26.564 1.00164.56 O ANISOU 1962 OD2 ASP A 264 23415 20265 18846 993 4419 682 O ATOM 1963 N ALA A 265 -9.499 -43.341 -22.026 1.00116.89 N ANISOU 1963 N ALA A 265 14414 15152 14849 1235 3157 1543 N ATOM 1964 CA ALA A 265 -9.299 -42.047 -21.384 1.00113.37 C ANISOU 1964 CA ALA A 265 13470 14919 14686 1136 2692 1698 C ATOM 1965 C ALA A 265 -7.824 -41.773 -21.122 1.00119.35 C ANISOU 1965 C ALA A 265 13645 15659 16046 1329 2840 2060 C ATOM 1966 O ALA A 265 -7.415 -40.609 -21.050 1.00121.75 O ANISOU 1966 O ALA A 265 13591 16062 16606 1201 2570 2245 O ATOM 1967 CB ALA A 265 -10.091 -41.977 -20.078 1.00104.55 C ANISOU 1967 CB ALA A 265 12272 13927 13527 1076 2120 1586 C ATOM 1968 N GLN A 266 -7.014 -42.824 -20.975 1.00120.39 N ANISOU 1968 N GLN A 266 13654 15642 16447 1629 3240 2201 N ATOM 1969 CA GLN A 266 -5.585 -42.625 -20.758 1.00117.87 C ANISOU 1969 CA GLN A 266 12680 15325 16779 1825 3394 2633 C ATOM 1970 C GLN A 266 -4.875 -42.230 -22.046 1.00126.37 C ANISOU 1970 C GLN A 266 13678 16392 17944 1884 3998 2865 C ATOM 1971 O GLN A 266 -3.877 -41.502 -22.004 1.00128.12 O ANISOU 1971 O GLN A 266 13274 16697 18709 1874 3979 3281 O ATOM 1972 CB GLN A 266 -4.960 -43.890 -20.169 1.00113.55 C ANISOU 1972 CB GLN A 266 11991 14626 16528 2183 3642 2762 C ATOM 1973 N LYS A 267 -5.370 -42.695 -23.192 1.00119.94 N ANISOU 1973 N LYS A 267 16239 16905 12430 3689 -316 3843 N ATOM 1974 CA LYS A 267 -4.778 -42.361 -24.488 1.00130.59 C ANISOU 1974 CA LYS A 267 17445 18199 13975 3707 -318 3706 C ATOM 1975 C LYS A 267 -5.460 -41.126 -25.082 1.00137.75 C ANISOU 1975 C LYS A 267 18232 19097 15010 3324 -377 3372 C ATOM 1976 O LYS A 267 -6.017 -41.145 -26.179 1.00141.44 O ANISOU 1976 O LYS A 267 18813 19256 15673 3190 -267 3225 O ATOM 1977 CB LYS A 267 -4.866 -43.555 -25.430 1.00128.87 C ANISOU 1977 CB LYS A 267 17516 17538 13909 3890 -106 3807 C ATOM 1978 N ALA A 268 -5.404 -40.037 -24.323 1.00133.58 N ANISOU 1978 N ALA A 268 17480 18917 14358 3155 -556 3256 N ATOM 1979 CA ALA A 268 -6.010 -38.778 -24.741 1.00126.91 C ANISOU 1979 CA ALA A 268 16524 18088 13610 2812 -626 2949 C ATOM 1980 C ALA A 268 -4.945 -37.776 -25.172 1.00125.82 C ANISOU 1980 C ALA A 268 16052 18243 13509 2786 -794 2835 C ATOM 1981 O ALA A 268 -3.767 -37.930 -24.849 1.00124.01 O ANISOU 1981 O ALA A 268 15636 18303 13180 3004 -891 2991 O ATOM 1982 CB ALA A 268 -6.859 -38.201 -23.618 1.00116.62 C ANISOU 1982 CB ALA A 268 15249 16918 12145 2609 -691 2864 C ATOM 1983 N ARG A 287 1.599 -39.815 -17.076 1.00146.34 N ANISOU 1983 N ARG A 287 17555 23771 14277 4426 -1755 4441 N ATOM 1984 CA ARG A 287 2.266 -38.866 -16.192 1.00144.75 C ANISOU 1984 CA ARG A 287 17050 24055 13892 4244 -2002 4315 C ATOM 1985 C ARG A 287 1.607 -38.837 -14.819 1.00162.98 C ANISOU 1985 C ARG A 287 19509 26465 15952 4155 -2048 4320 C ATOM 1986 O ARG A 287 2.119 -38.212 -13.889 1.00171.03 O ANISOU 1986 O ARG A 287 20330 27869 16785 4032 -2237 4238 O ATOM 1987 CB ARG A 287 2.262 -37.465 -16.807 1.00136.63 C ANISOU 1987 CB ARG A 287 15813 23168 12933 3909 -2164 4023 C ATOM 1988 N HIS A 288 0.471 -39.512 -14.692 1.00175.92 N ANISOU 1988 N HIS A 288 21502 27758 17583 4205 -1868 4415 N ATOM 1989 CA HIS A 288 -0.252 -39.564 -13.427 1.00189.72 C ANISOU 1989 CA HIS A 288 23414 29576 19095 4128 -1876 4436 C ATOM 1990 C HIS A 288 -0.734 -40.997 -13.216 1.00198.93 C ANISOU 1990 C HIS A 288 24904 30400 20279 4381 -1642 4720 C ATOM 1991 O HIS A 288 -0.278 -41.935 -13.879 1.00207.61 O ANISOU 1991 O HIS A 288 26068 31272 21544 4636 -1506 4896 O ATOM 1992 CB HIS A 288 -1.389 -38.532 -13.411 1.00186.38 C ANISOU 1992 CB HIS A 288 23081 29122 18614 3799 -1920 4176 C ATOM 1993 CG HIS A 288 -1.581 -37.872 -12.081 1.00188.03 C ANISOU 1993 CG HIS A 288 23247 29650 18546 3627 -2066 4055 C ATOM 1994 ND1 HIS A 288 -0.718 -36.912 -11.598 1.00189.71 N ANISOU 1994 ND1 HIS A 288 23168 30267 18646 3479 -2307 3881 N ATOM 1995 CD2 HIS A 288 -2.528 -38.040 -11.128 1.00188.94 C ANISOU 1995 CD2 HIS A 288 23580 29736 18472 3574 -1998 4079 C ATOM 1996 CE1 HIS A 288 -1.129 -36.512 -10.407 1.00190.85 C ANISOU 1996 CE1 HIS A 288 23369 30604 18542 3351 -2384 3791 C ATOM 1997 NE2 HIS A 288 -2.225 -37.182 -10.099 1.00190.11 N ANISOU 1997 NE2 HIS A 288 23574 30265 18394 3414 -2197 3911 N ATOM 1998 N GLY A 289 -1.671 -41.174 -12.287 1.00195.26 N ANISOU 1998 N GLY A 289 24658 29888 19643 4301 -1585 4759 N ATOM 1999 CA GLY A 289 -2.088 -42.499 -11.877 1.00188.40 C ANISOU 1999 CA GLY A 289 24088 28735 18758 4504 -1382 5033 C ATOM 2000 C GLY A 289 -3.267 -43.077 -12.633 1.00178.30 C ANISOU 2000 C GLY A 289 23156 26948 17643 4460 -1145 5079 C ATOM 2001 O GLY A 289 -4.236 -43.533 -12.020 1.00174.65 O ANISOU 2001 O GLY A 289 22951 26323 17085 4398 -1018 5170 O ATOM 2002 N PHE A 290 -3.202 -43.064 -13.967 1.00171.13 N ANISOU 2002 N PHE A 290 22257 25787 16978 4478 -1078 5016 N ATOM 2003 CA PHE A 290 -4.202 -43.789 -14.744 1.00165.13 C ANISOU 2003 CA PHE A 290 21841 24491 16411 4444 -832 5061 C ATOM 2004 C PHE A 290 -3.965 -45.291 -14.679 1.00174.62 C ANISOU 2004 C PHE A 290 23289 25390 17667 4737 -653 5360 C ATOM 2005 O PHE A 290 -4.918 -46.073 -14.768 1.00172.46 O ANISOU 2005 O PHE A 290 23361 24713 17454 4694 -450 5463 O ATOM 2006 CB PHE A 290 -4.204 -43.306 -16.194 1.00160.31 C ANISOU 2006 CB PHE A 290 21156 23636 16121 4287 -797 4796 C ATOM 2007 CG PHE A 290 -5.381 -42.439 -16.540 1.00157.14 C ANISOU 2007 CG PHE A 290 20798 23065 15842 3872 -764 4463 C ATOM 2008 CD1 PHE A 290 -5.326 -41.068 -16.360 1.00156.53 C ANISOU 2008 CD1 PHE A 290 20463 23296 15714 3626 -950 4179 C ATOM 2009 CD2 PHE A 290 -6.545 -42.998 -17.042 1.00151.66 C ANISOU 2009 CD2 PHE A 290 20407 21907 15309 3729 -546 4437 C ATOM 2010 CE1 PHE A 290 -6.409 -40.268 -16.676 1.00152.68 C ANISOU 2010 CE1 PHE A 290 20023 22652 15336 3280 -912 3883 C ATOM 2011 CE2 PHE A 290 -7.632 -42.205 -17.360 1.00146.76 C ANISOU 2011 CE2 PHE A 290 19805 21164 14794 3369 -516 4146 C ATOM 2012 CZ PHE A 290 -7.563 -40.838 -17.177 1.00146.28 C ANISOU 2012 CZ PHE A 290 19488 21409 14681 3162 -695 3873 C ATOM 2013 N ASP A 291 -2.707 -45.711 -14.524 1.00185.69 N ANISOU 2013 N ASP A 291 24519 26970 19065 5009 -717 5477 N ATOM 2014 CA ASP A 291 -2.417 -47.115 -14.270 1.00194.73 C ANISOU 2014 CA ASP A 291 25885 27867 20237 5289 -561 5742 C ATOM 2015 C ASP A 291 -2.814 -47.531 -12.861 1.00195.40 C ANISOU 2015 C ASP A 291 26092 28059 20094 5280 -554 5901 C ATOM 2016 O ASP A 291 -3.023 -48.723 -12.615 1.00211.13 O ANISOU 2016 O ASP A 291 28368 29743 22107 5430 -387 6119 O ATOM 2017 CB ASP A 291 -0.931 -47.398 -14.500 1.00199.15 C ANISOU 2017 CB ASP A 291 26199 28630 20839 5596 -628 5819 C ATOM 2018 N ILE A 292 -2.918 -46.576 -11.934 1.00181.27 N ANISOU 2018 N ILE A 292 24102 26690 18081 5103 -732 5791 N ATOM 2019 CA ILE A 292 -3.400 -46.892 -10.594 1.00170.53 C ANISOU 2019 CA ILE A 292 22863 25441 16489 5070 -720 5924 C ATOM 2020 C ILE A 292 -4.885 -47.226 -10.630 1.00169.83 C ANISOU 2020 C ILE A 292 23122 24976 16430 4863 -527 5945 C ATOM 2021 O ILE A 292 -5.338 -48.175 -9.980 1.00160.09 O ANISOU 2021 O ILE A 292 22141 23553 15131 4916 -390 6157 O ATOM 2022 CB ILE A 292 -3.103 -45.730 -9.630 1.00160.57 C ANISOU 2022 CB ILE A 292 21300 24732 14978 4926 -962 5766 C ATOM 2023 N LEU A 293 -5.666 -46.454 -11.389 1.00173.80 N ANISOU 2023 N LEU A 293 23638 25372 17028 4613 -510 5731 N ATOM 2024 CA LEU A 293 -7.081 -46.768 -11.551 1.00178.10 C ANISOU 2024 CA LEU A 293 24494 25556 17619 4401 -311 5745 C ATOM 2025 C LEU A 293 -7.271 -48.055 -12.343 1.00187.89 C ANISOU 2025 C LEU A 293 26056 26243 19091 4517 -85 5916 C ATOM 2026 O LEU A 293 -8.119 -48.885 -11.996 1.00197.51 O ANISOU 2026 O LEU A 293 27574 27170 20301 4440 91 6067 O ATOM 2027 CB LEU A 293 -7.803 -45.605 -12.233 1.00167.43 C ANISOU 2027 CB LEU A 293 23059 24244 16314 4127 -349 5471 C ATOM 2028 CG LEU A 293 -9.248 -45.851 -12.674 1.00161.00 C ANISOU 2028 CG LEU A 293 22508 23010 15655 3834 -135 5383 C ATOM 2029 CD1 LEU A 293 -10.132 -46.200 -11.486 1.00162.14 C ANISOU 2029 CD1 LEU A 293 22825 23227 15555 3753 -44 5553 C ATOM 2030 CD2 LEU A 293 -9.797 -44.642 -13.417 1.00157.03 C ANISOU 2030 CD2 LEU A 293 21832 22504 15328 3498 -190 4965 C ATOM 2031 N VAL A 294 -6.486 -48.242 -13.407 1.00170.85 N ANISOU 2031 N VAL A 294 23844 23933 17139 4690 -84 5884 N ATOM 2032 CA VAL A 294 -6.601 -49.454 -14.212 1.00155.56 C ANISOU 2032 CA VAL A 294 22222 21458 15424 4807 127 6011 C ATOM 2033 C VAL A 294 -6.157 -50.672 -13.412 1.00168.31 C ANISOU 2033 C VAL A 294 23995 22986 16968 5051 198 6284 C ATOM 2034 O VAL A 294 -6.740 -51.756 -13.531 1.00168.57 O ANISOU 2034 O VAL A 294 24382 22571 17096 5041 394 6424 O ATOM 2035 CB VAL A 294 -5.795 -49.307 -15.515 1.00137.77 C ANISOU 2035 CB VAL A 294 19851 19107 13387 4954 106 5895 C ATOM 2036 N GLY A 295 -5.121 -50.518 -12.586 1.00171.78 N ANISOU 2036 N GLY A 295 24178 23851 17241 5262 38 6361 N ATOM 2037 CA GLY A 295 -4.671 -51.631 -11.767 1.00176.39 C ANISOU 2037 CA GLY A 295 24894 24390 17735 5511 97 6630 C ATOM 2038 C GLY A 295 -5.661 -51.990 -10.676 1.00181.50 C ANISOU 2038 C GLY A 295 25757 24992 18214 5344 172 6767 C ATOM 2039 O GLY A 295 -5.834 -53.166 -10.345 1.00189.68 O ANISOU 2039 O GLY A 295 27078 25730 19261 5450 318 6992 O ATOM 2040 N GLN A 296 -6.326 -50.984 -10.102 1.00175.61 N ANISOU 2040 N GLN A 296 24878 24544 17303 5079 76 6631 N ATOM 2041 CA GLN A 296 -7.329 -51.254 -9.079 1.00174.86 C ANISOU 2041 CA GLN A 296 24968 24434 17035 4901 158 6747 C ATOM 2042 C GLN A 296 -8.605 -51.826 -9.683 1.00165.44 C ANISOU 2042 C GLN A 296 24128 22728 16005 4663 387 6765 C ATOM 2043 O GLN A 296 -9.324 -52.576 -9.011 1.00180.02 O ANISOU 2043 O GLN A 296 26219 24403 17777 4575 518 6946 O ATOM 2044 CB GLN A 296 -7.626 -49.980 -8.288 1.00173.73 C ANISOU 2044 CB GLN A 296 24571 24783 16655 4703 -7 6573 C ATOM 2045 CG GLN A 296 -6.507 -49.580 -7.337 1.00175.55 C ANISOU 2045 CG GLN A 296 24504 25529 16668 4895 -224 6596 C ATOM 2046 CD GLN A 296 -6.707 -48.201 -6.741 1.00173.12 C ANISOU 2046 CD GLN A 296 23938 25689 16152 4686 -406 6358 C ATOM 2047 OE1 GLN A 296 -6.847 -47.215 -7.464 1.00167.99 O ANISOU 2047 OE1 GLN A 296 23141 25105 15581 4525 -481 6104 O ATOM 2048 NE2 GLN A 296 -6.725 -48.126 -5.416 1.00176.32 N ANISOU 2048 NE2 GLN A 296 24297 26412 16284 4686 -477 6432 N ATOM 2049 N ILE A 297 -8.906 -51.487 -10.938 1.00144.59 N ANISOU 2049 N ILE A 297 21513 19845 13581 4541 437 6583 N ATOM 2050 CA ILE A 297 -10.007 -52.145 -11.634 1.00136.14 C ANISOU 2050 CA ILE A 297 20785 18251 12693 4323 659 6600 C ATOM 2051 C ILE A 297 -9.640 -53.591 -11.947 1.00144.70 C ANISOU 2051 C ILE A 297 22164 18884 13931 4526 803 6801 C ATOM 2052 O ILE A 297 -10.478 -54.495 -11.849 1.00133.51 O ANISOU 2052 O ILE A 297 21073 17090 12565 4377 980 6933 O ATOM 2053 CB ILE A 297 -10.384 -51.360 -12.905 1.00124.59 C ANISOU 2053 CB ILE A 297 19261 16667 11411 4145 666 6342 C ATOM 2054 CG1 ILE A 297 -11.026 -50.022 -12.534 1.00122.39 C ANISOU 2054 CG1 ILE A 297 18757 16777 10969 3899 563 6152 C ATOM 2055 CG2 ILE A 297 -11.325 -52.170 -13.786 1.00118.21 C ANISOU 2055 CG2 ILE A 297 18812 15279 10825 3951 892 6354 C ATOM 2056 CD1 ILE A 297 -11.418 -49.180 -13.730 1.00115.33 C ANISOU 2056 CD1 ILE A 297 17781 15790 10248 3711 560 5882 C ATOM 2057 N ASP A 298 -8.379 -53.833 -12.316 1.00165.18 N ANISOU 2057 N ASP A 298 24646 21520 16596 4865 731 6826 N ATOM 2058 CA ASP A 298 -7.921 -55.200 -12.538 1.00168.30 C ANISOU 2058 CA ASP A 298 25310 21525 17111 5107 863 7015 C ATOM 2059 C ASP A 298 -7.937 -56.012 -11.249 1.00163.65 C ANISOU 2059 C ASP A 298 24855 20985 16338 5203 895 7291 C ATOM 2060 O ASP A 298 -8.132 -57.232 -11.290 1.00169.68 O ANISOU 2060 O ASP A 298 25957 21326 17189 5260 1055 7465 O ATOM 2061 CB ASP A 298 -6.518 -55.193 -13.145 1.00170.93 C ANISOU 2061 CB ASP A 298 25445 21972 17529 5468 777 6978 C ATOM 2062 N ASP A 299 -7.734 -55.359 -10.103 1.00151.42 N ANISOU 2062 N ASP A 299 23056 19943 14532 5217 744 7330 N ATOM 2063 CA ASP A 299 -7.837 -56.060 -8.828 1.00142.56 C ANISOU 2063 CA ASP A 299 22059 18893 13215 5283 773 7591 C ATOM 2064 C ASP A 299 -9.284 -56.422 -8.519 1.00142.04 C ANISOU 2064 C ASP A 299 22281 18554 13132 4931 933 7656 C ATOM 2065 O ASP A 299 -9.555 -57.477 -7.933 1.00141.25 O ANISOU 2065 O ASP A 299 22451 18225 12993 4957 1050 7898 O ATOM 2066 CB ASP A 299 -7.245 -55.205 -7.708 1.00138.05 C ANISOU 2066 CB ASP A 299 21136 18952 12363 5373 562 7586 C ATOM 2067 N ALA A 300 -10.228 -55.559 -8.904 1.00146.95 N ANISOU 2067 N ALA A 300 22844 19208 13781 4595 943 7448 N ATOM 2068 CA ALA A 300 -11.638 -55.877 -8.716 1.00161.62 C ANISOU 2068 CA ALA A 300 24952 20819 15638 4235 1108 7497 C ATOM 2069 C ALA A 300 -12.100 -56.960 -9.682 1.00166.42 C ANISOU 2069 C ALA A 300 25925 20793 16513 4140 1304 7546 C ATOM 2070 O ALA A 300 -13.035 -57.707 -9.372 1.00171.16 O ANISOU 2070 O ALA A 300 26798 21118 17116 3913 1456 7688 O ATOM 2071 CB ALA A 300 -12.489 -54.618 -8.881 1.00163.55 C ANISOU 2071 CB ALA A 300 25008 21304 15829 3921 1068 7253 C ATOM 2072 N LEU A 301 -11.464 -57.059 -10.852 1.00164.29 N ANISOU 2072 N LEU A 301 25666 20292 16464 4297 1303 7422 N ATOM 2073 CA LEU A 301 -11.803 -58.123 -11.791 1.00158.75 C ANISOU 2073 CA LEU A 301 25324 18981 16012 4230 1482 7445 C ATOM 2074 C LEU A 301 -11.376 -59.489 -11.271 1.00166.32 C ANISOU 2074 C LEU A 301 26551 19684 16959 4458 1566 7723 C ATOM 2075 O LEU A 301 -11.970 -60.506 -11.646 1.00168.30 O ANISOU 2075 O LEU A 301 27158 19433 17354 4314 1732 7799 O ATOM 2076 CB LEU A 301 -11.162 -57.849 -13.152 1.00147.19 C ANISOU 2076 CB LEU A 301 23792 17370 14765 4368 1456 7230 C ATOM 2077 CG LEU A 301 -11.871 -56.836 -14.052 1.00148.34 C ANISOU 2077 CG LEU A 301 23824 17524 15013 4068 1448 6954 C ATOM 2078 CD1 LEU A 301 -11.031 -56.529 -15.281 1.00155.22 C ANISOU 2078 CD1 LEU A 301 24587 18323 16065 4265 1398 6766 C ATOM 2079 CD2 LEU A 301 -13.238 -57.363 -14.457 1.00147.62 C ANISOU 2079 CD2 LEU A 301 24045 16998 15046 3662 1631 6934 C ATOM 2080 N LYS A 302 -10.355 -59.533 -10.411 1.00167.83 N ANISOU 2080 N LYS A 302 26578 20214 16978 4806 1452 7875 N ATOM 2081 CA LYS A 302 -9.922 -60.797 -9.830 1.00163.54 C ANISOU 2081 CA LYS A 302 26278 19463 16399 5049 1528 8158 C ATOM 2082 C LYS A 302 -10.908 -61.332 -8.800 1.00168.29 C ANISOU 2082 C LYS A 302 27089 19993 16860 4802 1619 8373 C ATOM 2083 O LYS A 302 -10.947 -62.545 -8.571 1.00167.00 O ANISOU 2083 O LYS A 302 27244 19475 16733 4875 1739 8595 O ATOM 2084 CB LYS A 302 -8.540 -60.634 -9.194 1.00161.07 C ANISOU 2084 CB LYS A 302 25696 19577 15928 5487 1374 8258 C ATOM 2085 N LEU A 303 -11.705 -60.460 -8.183 1.00174.07 N ANISOU 2085 N LEU A 303 27653 21055 17429 4513 1570 8312 N ATOM 2086 CA LEU A 303 -12.702 -60.883 -7.207 1.00182.60 C ANISOU 2086 CA LEU A 303 28903 22113 18363 4252 1662 8505 C ATOM 2087 C LEU A 303 -14.017 -61.285 -7.861 1.00192.25 C ANISOU 2087 C LEU A 303 30395 22890 19760 3818 1839 8455 C ATOM 2088 O LEU A 303 -14.623 -62.286 -7.464 1.00193.02 O ANISOU 2088 O LEU A 303 30788 22691 19859 3669 1972 8669 O ATOM 2089 CB LEU A 303 -12.955 -59.767 -6.191 1.00177.71 C ANISOU 2089 CB LEU A 303 27973 22084 17465 4151 1537 8457 C ATOM 2090 N ALA A 304 -14.469 -60.526 -8.862 1.00200.71 N ANISOU 2090 N ALA A 304 31365 23917 20978 3601 1840 8179 N ATOM 2091 CA ALA A 304 -15.739 -60.839 -9.509 1.00203.67 C ANISOU 2091 CA ALA A 304 31961 23909 21515 3164 1999 8112 C ATOM 2092 C ALA A 304 -15.666 -62.138 -10.301 1.00206.99 C ANISOU 2092 C ALA A 304 32757 23711 22179 3189 2132 8180 C ATOM 2093 O ALA A 304 -16.687 -62.815 -10.472 1.00212.34 O ANISOU 2093 O ALA A 304 33693 24036 22952 2840 2276 8236 O ATOM 2094 CB ALA A 304 -16.166 -59.685 -10.416 1.00197.70 C ANISOU 2094 CB ALA A 304 30994 23271 20852 2957 1962 7796 C ATOM 2095 N ASN A 305 -14.478 -62.502 -10.788 1.00202.01 N ANISOU 2095 N ASN A 305 32156 22955 21645 3592 2086 8170 N ATOM 2096 CA ASN A 305 -14.309 -63.751 -11.519 1.00191.16 C ANISOU 2096 CA ASN A 305 31148 21001 20482 3667 2213 8222 C ATOM 2097 C ASN A 305 -14.345 -64.975 -10.613 1.00176.03 C ANISOU 2097 C ASN A 305 29519 18880 18486 3736 2300 8551 C ATOM 2098 O ASN A 305 -14.674 -66.068 -11.086 1.00182.49 O ANISOU 2098 O ASN A 305 30698 19172 19466 3635 2437 8611 O ATOM 2099 CB ASN A 305 -12.991 -63.730 -12.295 1.00193.11 C ANISOU 2099 CB ASN A 305 31317 21220 20836 4105 2147 8109 C ATOM 2100 N GLU A 306 -14.024 -64.819 -9.328 1.00170.65 N ANISOU 2100 N GLU A 306 28692 18598 17551 3899 2221 8760 N ATOM 2101 CA GLU A 306 -14.013 -65.929 -8.381 1.00174.19 C ANISOU 2101 CA GLU A 306 29396 18893 17896 3987 2294 9093 C ATOM 2102 C GLU A 306 -15.322 -66.062 -7.615 1.00184.21 C ANISOU 2102 C GLU A 306 30762 20176 19054 3541 2377 9235 C ATOM 2103 O GLU A 306 -15.329 -66.591 -6.495 1.00174.21 O ANISOU 2103 O GLU A 306 29584 19002 17605 3603 2393 9518 O ATOM 2104 CB GLU A 306 -12.841 -65.779 -7.410 1.00166.13 C ANISOU 2104 CB GLU A 306 28172 18297 16654 4445 2163 9257 C ATOM 2105 N GLY A 307 -16.432 -65.600 -8.187 1.00203.08 N ANISOU 2105 N GLY A 307 33128 22491 21542 3093 2434 9051 N ATOM 2106 CA GLY A 307 -17.724 -65.708 -7.547 1.00213.13 C ANISOU 2106 CA GLY A 307 34467 23795 22719 2645 2526 9173 C ATOM 2107 C GLY A 307 -18.001 -64.692 -6.461 1.00216.96 C ANISOU 2107 C GLY A 307 34635 24888 22913 2581 2439 9196 C ATOM 2108 O GLY A 307 -19.115 -64.679 -5.923 1.00215.34 O ANISOU 2108 O GLY A 307 34448 24765 22608 2201 2520 9282 O ATOM 2109 N LYS A 308 -17.034 -63.845 -6.118 1.00214.37 N ANISOU 2109 N LYS A 308 34013 25001 22439 2932 2278 9117 N ATOM 2110 CA LYS A 308 -17.238 -62.827 -5.095 1.00210.61 C ANISOU 2110 CA LYS A 308 33232 25115 21674 2890 2184 9104 C ATOM 2111 C LYS A 308 -17.967 -61.635 -5.704 1.00201.24 C ANISOU 2111 C LYS A 308 31810 24126 20527 2597 2168 8799 C ATOM 2112 O LYS A 308 -17.461 -61.000 -6.635 1.00210.11 O ANISOU 2112 O LYS A 308 32787 25257 21790 2717 2090 8555 O ATOM 2113 CB LYS A 308 -15.901 -62.396 -4.495 1.00211.00 C ANISOU 2113 CB LYS A 308 33051 25565 21554 3364 2007 9128 C ATOM 2114 N VAL A 309 -19.153 -61.334 -5.180 1.00182.41 N ANISOU 2114 N VAL A 309 29384 21911 18013 2219 2247 8818 N ATOM 2115 CA VAL A 309 -19.986 -60.258 -5.693 1.00168.72 C ANISOU 2115 CA VAL A 309 27438 20366 16302 1919 2257 8549 C ATOM 2116 C VAL A 309 -19.976 -59.046 -4.769 1.00170.65 C ANISOU 2116 C VAL A 309 27349 21239 16252 1979 2146 8456 C ATOM 2117 O VAL A 309 -19.908 -57.908 -5.238 1.00161.04 O ANISOU 2117 O VAL A 309 25876 20270 15042 1986 2060 8186 O ATOM 2118 CB VAL A 309 -21.429 -60.753 -5.935 1.00160.34 C ANISOU 2118 CB VAL A 309 26548 19039 15333 1415 2442 8599 C ATOM 2119 N LYS A 310 -20.041 -59.268 -3.455 1.00176.75 N ANISOU 2119 N LYS A 310 28126 22272 16758 2024 2145 8670 N ATOM 2120 CA LYS A 310 -20.067 -58.157 -2.510 1.00184.94 C ANISOU 2120 CA LYS A 310 28864 23905 17500 2074 2044 8569 C ATOM 2121 C LYS A 310 -18.700 -57.507 -2.343 1.00191.63 C ANISOU 2121 C LYS A 310 29484 25063 18264 2498 1828 8466 C ATOM 2122 O LYS A 310 -18.621 -56.308 -2.053 1.00199.59 O ANISOU 2122 O LYS A 310 30198 26523 19114 2529 1711 8255 O ATOM 2123 CB LYS A 310 -20.586 -58.634 -1.153 1.00186.05 C ANISOU 2123 CB LYS A 310 29093 24222 17374 1981 2119 8827 C ATOM 2124 N GLU A 311 -17.619 -58.271 -2.521 1.00192.47 N ANISOU 2124 N GLU A 311 29713 24946 18471 2820 1773 8605 N ATOM 2125 CA GLU A 311 -16.285 -57.708 -2.343 1.00189.73 C ANISOU 2125 CA GLU A 311 29128 24918 18041 3214 1566 8525 C ATOM 2126 C GLU A 311 -15.911 -56.789 -3.500 1.00185.92 C ANISOU 2126 C GLU A 311 28444 24460 17737 3249 1471 8213 C ATOM 2127 O GLU A 311 -15.221 -55.782 -3.301 1.00191.54 O ANISOU 2127 O GLU A 311 28855 25592 18328 3418 1291 8043 O ATOM 2128 CB GLU A 311 -15.257 -58.830 -2.196 1.00188.47 C ANISOU 2128 CB GLU A 311 29147 24528 17934 3560 1551 8775 C ATOM 2129 N ALA A 312 -16.356 -57.118 -4.715 1.00177.46 N ANISOU 2129 N ALA A 312 27536 22942 16949 3079 1587 8129 N ATOM 2130 CA ALA A 312 -16.026 -56.291 -5.870 1.00152.90 C ANISOU 2130 CA ALA A 312 24254 19825 14015 3107 1508 7843 C ATOM 2131 C ALA A 312 -16.734 -54.943 -5.821 1.00149.53 C ANISOU 2131 C ALA A 312 23568 19774 13473 2876 1463 7593 C ATOM 2132 O ALA A 312 -16.196 -53.944 -6.313 1.00155.67 O ANISOU 2132 O ALA A 312 24100 20775 14274 2979 1322 7360 O ATOM 2133 CB ALA A 312 -16.376 -57.028 -7.162 1.00147.57 C ANISOU 2133 CB ALA A 312 23841 18566 13662 2970 1652 7815 C ATOM 2134 N GLN A 313 -17.933 -54.892 -5.236 1.00149.58 N ANISOU 2134 N GLN A 313 23620 19861 13351 2566 1583 7636 N ATOM 2135 CA GLN A 313 -18.657 -53.629 -5.147 1.00147.49 C ANISOU 2135 CA GLN A 313 23111 19964 12965 2361 1557 7395 C ATOM 2136 C GLN A 313 -17.999 -52.670 -4.163 1.00166.32 C ANISOU 2136 C GLN A 313 25210 22916 15070 2566 1362 7304 C ATOM 2137 O GLN A 313 -18.117 -51.449 -4.317 1.00165.24 O ANISOU 2137 O GLN A 313 24825 23091 14867 2512 1268 7038 O ATOM 2138 CB GLN A 313 -20.111 -53.883 -4.749 1.00131.98 C ANISOU 2138 CB GLN A 313 21258 17958 10931 1985 1750 7474 C ATOM 2139 N ALA A 314 -17.307 -53.198 -3.151 1.00177.69 N ANISOU 2139 N ALA A 314 26683 24492 16338 2795 1296 7512 N ATOM 2140 CA ALA A 314 -16.643 -52.334 -2.181 1.00189.51 C ANISOU 2140 CA ALA A 314 27915 26528 17562 2977 1101 7422 C ATOM 2141 C ALA A 314 -15.420 -51.658 -2.788 1.00192.19 C ANISOU 2141 C ALA A 314 28033 27007 17985 3223 893 7238 C ATOM 2142 O ALA A 314 -15.147 -50.485 -2.504 1.00196.99 O ANISOU 2142 O ALA A 314 28369 28035 18443 3243 728 7009 O ATOM 2143 CB ALA A 314 -16.254 -53.137 -0.941 1.00192.91 C ANISOU 2143 CB ALA A 314 28447 27063 17786 3147 1094 7711 C ATOM 2144 N ALA A 315 -14.672 -52.380 -3.625 1.00186.45 N ANISOU 2144 N ALA A 315 27417 25932 17493 3406 897 7327 N ATOM 2145 CA ALA A 315 -13.500 -51.789 -4.262 1.00180.86 C ANISOU 2145 CA ALA A 315 26490 25354 16876 3635 712 7164 C ATOM 2146 C ALA A 315 -13.889 -50.784 -5.339 1.00175.20 C ANISOU 2146 C ALA A 315 25641 24622 16305 3455 691 6863 C ATOM 2147 O ALA A 315 -13.165 -49.808 -5.565 1.00177.43 O ANISOU 2147 O ALA A 315 25655 25198 16561 3552 504 6655 O ATOM 2148 CB ALA A 315 -12.612 -52.884 -4.851 1.00176.68 C ANISOU 2148 CB ALA A 315 26118 24459 16551 3898 743 7345 C ATOM 2149 N ALA A 316 -15.023 -51.001 -6.010 1.00164.20 N ANISOU 2149 N ALA A 316 24427 22899 15063 3182 879 6836 N ATOM 2150 CA ALA A 316 -15.469 -50.059 -7.031 1.00156.84 C ANISOU 2150 CA ALA A 316 23378 21953 14262 3006 874 6560 C ATOM 2151 C ALA A 316 -15.963 -48.755 -6.419 1.00158.05 C ANISOU 2151 C ALA A 316 23285 22580 14185 2862 783 6339 C ATOM 2152 O ALA A 316 -15.770 -47.685 -7.006 1.00154.29 O ANISOU 2152 O ALA A 316 22604 22275 13742 2841 665 6079 O ATOM 2153 CB ALA A 316 -16.564 -50.693 -7.888 1.00154.81 C ANISOU 2153 CB ALA A 316 23378 21220 14224 2741 1104 6598 C ATOM 2154 N GLU A 317 -16.593 -48.821 -5.245 1.00160.53 N ANISOU 2154 N GLU A 317 23624 23110 14262 2764 836 6429 N ATOM 2155 CA GLU A 317 -17.087 -47.619 -4.586 1.00156.17 C ANISOU 2155 CA GLU A 317 22857 23005 13476 2641 761 6207 C ATOM 2156 C GLU A 317 -15.981 -46.824 -3.907 1.00164.14 C ANISOU 2156 C GLU A 317 23622 24452 14291 2851 504 6081 C ATOM 2157 O GLU A 317 -16.180 -45.641 -3.612 1.00168.81 O ANISOU 2157 O GLU A 317 24017 25394 14730 2766 398 5820 O ATOM 2158 CB GLU A 317 -18.159 -47.984 -3.556 1.00147.37 C ANISOU 2158 CB GLU A 317 21852 21973 12170 2466 920 6344 C ATOM 2159 N GLN A 318 -14.825 -47.441 -3.655 1.00165.63 N ANISOU 2159 N GLN A 318 23817 24631 14483 3115 400 6252 N ATOM 2160 CA GLN A 318 -13.736 -46.740 -2.985 1.00162.24 C ANISOU 2160 CA GLN A 318 23143 24631 13869 3296 152 6145 C ATOM 2161 C GLN A 318 -12.963 -45.833 -3.935 1.00161.63 C ANISOU 2161 C GLN A 318 22848 24636 13929 3345 -24 5892 C ATOM 2162 O GLN A 318 -12.409 -44.818 -3.499 1.00166.92 O ANISOU 2162 O GLN A 318 23281 25702 14440 3363 -232 5684 O ATOM 2163 CB GLN A 318 -12.785 -47.745 -2.334 1.00162.60 C ANISOU 2163 CB GLN A 318 23253 24671 13858 3566 112 6433 C ATOM 2164 N LEU A 319 -12.913 -46.175 -5.222 1.00157.07 N ANISOU 2164 N LEU A 319 22352 23687 13640 3352 53 5901 N ATOM 2165 CA LEU A 319 -12.183 -45.373 -6.196 1.00152.70 C ANISOU 2165 CA LEU A 319 21598 23191 13230 3397 -102 5680 C ATOM 2166 C LEU A 319 -12.896 -44.056 -6.471 1.00160.09 C ANISOU 2166 C LEU A 319 22399 24312 14116 3160 -149 5357 C ATOM 2167 O LEU A 319 -12.428 -42.991 -6.056 1.00155.35 O ANISOU 2167 O LEU A 319 21568 24094 13362 3148 -353 5135 O ATOM 2168 CB LEU A 319 -11.992 -46.153 -7.498 1.00143.39 C ANISOU 2168 CB LEU A 319 20569 21545 12370 3476 14 5780 C ATOM 2169 CG LEU A 319 -10.572 -46.651 -7.771 1.00132.36 C ANISOU 2169 CG LEU A 319 19091 20127 11074 3779 -96 5893 C ATOM 2170 CD1 LEU A 319 -9.615 -45.476 -7.899 1.00118.76 C ANISOU 2170 CD1 LEU A 319 17024 18799 9299 3827 -352 5656 C ATOM 2171 CD2 LEU A 319 -10.120 -47.598 -6.672 1.00131.69 C ANISOU 2171 CD2 LEU A 319 19091 20105 10842 3973 -84 6168 C ATOM 2172 N LYS A 320 -14.024 -44.118 -7.171 1.00164.73 N ANISOU 2172 N LYS A 320 23122 24607 14860 2947 36 5296 N ATOM 2173 CA LYS A 320 -14.783 -42.919 -7.503 1.00169.12 C ANISOU 2173 CA LYS A 320 23532 25229 15498 2666 10 4898 C ATOM 2174 C LYS A 320 -16.186 -42.978 -6.908 1.00171.18 C ANISOU 2174 C LYS A 320 23906 25501 15633 2458 195 4914 C ATOM 2175 O LYS A 320 -16.353 -42.997 -5.688 1.00171.57 O ANISOU 2175 O LYS A 320 23974 25864 15349 2515 194 5046 O ATOM 2176 CB LYS A 320 -14.861 -42.737 -9.021 1.00166.38 C ANISOU 2176 CB LYS A 320 23157 24509 15550 2537 40 4682 C ATOM 2177 N LYS A1230 -19.392 -31.862 -15.343 1.00 97.88 N ANISOU 2177 N LYS A1230 13402 15510 8279 913 -309 1428 N ATOM 2178 CA LYS A1230 -20.703 -32.427 -15.047 1.00109.80 C ANISOU 2178 CA LYS A1230 14990 17000 9730 851 -102 1532 C ATOM 2179 C LYS A1230 -21.790 -31.745 -15.869 1.00125.15 C ANISOU 2179 C LYS A1230 16887 18817 11846 715 -14 1323 C ATOM 2180 O LYS A1230 -22.803 -32.359 -16.207 1.00134.86 O ANISOU 2180 O LYS A1230 18153 19932 13155 622 159 1418 O ATOM 2181 CB LYS A1230 -21.016 -32.306 -13.554 1.00109.40 C ANISOU 2181 CB LYS A1230 14971 17270 9327 914 -87 1572 C ATOM 2182 N ASN A1231 -21.575 -30.469 -16.190 1.00126.94 N ANISOU 2182 N ASN A1231 17035 19069 12126 700 -137 1043 N ATOM 2183 CA ASN A1231 -22.524 -29.685 -16.970 1.00122.57 C ANISOU 2183 CA ASN A1231 16433 18409 11727 605 -73 834 C ATOM 2184 C ASN A1231 -21.760 -28.862 -18.009 1.00106.32 C ANISOU 2184 C ASN A1231 14313 16194 9891 579 -219 647 C ATOM 2185 O ASN A1231 -21.748 -27.634 -17.997 1.00116.86 O ANISOU 2185 O ASN A1231 15615 17579 11208 574 -308 402 O ATOM 2186 CB ASN A1231 -23.374 -28.799 -16.061 1.00121.11 C ANISOU 2186 CB ASN A1231 16242 18454 11320 628 -34 667 C ATOM 2187 CG ASN A1231 -24.583 -28.226 -16.772 1.00118.32 C ANISOU 2187 CG ASN A1231 15838 18018 11101 557 81 516 C ATOM 2188 OD1 ASN A1231 -25.014 -28.746 -17.801 1.00108.07 O ANISOU 2188 OD1 ASN A1231 14514 16522 10027 466 166 589 O ATOM 2189 ND2 ASN A1231 -25.139 -27.151 -16.225 1.00120.22 N ANISOU 2189 ND2 ASN A1231 16068 18417 11194 607 82 304 N ATOM 2190 N LYS A1232 -21.100 -29.558 -18.933 1.00 75.60 N ANISOU 2190 N LYS A1232 10417 12100 6206 566 -237 769 N ATOM 2191 CA LYS A1232 -20.325 -28.897 -19.972 1.00 71.32 C ANISOU 2191 CA LYS A1232 9808 11414 5875 538 -362 628 C ATOM 2192 C LYS A1232 -21.109 -28.844 -21.276 1.00 80.03 C ANISOU 2192 C LYS A1232 10893 12285 7230 439 -263 563 C ATOM 2193 O LYS A1232 -21.783 -29.817 -21.636 1.00 90.61 O ANISOU 2193 O LYS A1232 12278 13510 8641 392 -118 712 O ATOM 2194 CB LYS A1232 -19.001 -29.625 -20.208 1.00 67.61 C ANISOU 2194 CB LYS A1232 9327 10898 5463 610 -451 795 C ATOM 2195 N PRO A1233 -21.044 -27.722 -21.992 1.00 80.70 N ANISOU 2195 N PRO A1233 10920 12299 7445 396 -341 345 N ATOM 2196 CA PRO A1233 -21.743 -27.630 -23.280 1.00 80.10 C ANISOU 2196 CA PRO A1233 10817 12019 7599 311 -260 287 C ATOM 2197 C PRO A1233 -21.190 -28.638 -24.276 1.00 73.28 C ANISOU 2197 C PRO A1233 9964 10955 6923 291 -236 442 C ATOM 2198 O PRO A1233 -19.986 -28.900 -24.323 1.00 68.75 O ANISOU 2198 O PRO A1233 9381 10372 6369 352 -334 515 O ATOM 2199 CB PRO A1233 -21.476 -26.189 -23.728 1.00 85.17 C ANISOU 2199 CB PRO A1233 11409 12633 8318 294 -378 43 C ATOM 2200 CG PRO A1233 -21.130 -25.454 -22.471 1.00 87.42 C ANISOU 2200 CG PRO A1233 11717 13127 8372 351 -478 -62 C ATOM 2201 CD PRO A1233 -20.411 -26.448 -21.613 1.00 83.43 C ANISOU 2201 CD PRO A1233 11234 12750 7715 412 -503 139 C ATOM 2202 N ARG A1234 -22.088 -29.206 -25.078 1.00 76.19 N ANISOU 2202 N ARG A1234 10351 11176 7420 208 -105 489 N ATOM 2203 CA ARG A1234 -21.707 -30.216 -26.053 1.00 82.07 C ANISOU 2203 CA ARG A1234 11139 11710 8333 184 -62 621 C ATOM 2204 C ARG A1234 -22.709 -30.212 -27.196 1.00 83.35 C ANISOU 2204 C ARG A1234 11284 11725 8661 62 31 555 C ATOM 2205 O ARG A1234 -23.919 -30.127 -26.970 1.00 94.50 O ANISOU 2205 O ARG A1234 12678 13207 10019 -11 126 528 O ATOM 2206 CB ARG A1234 -21.633 -31.606 -25.411 1.00 74.49 C ANISOU 2206 CB ARG A1234 10291 10735 7276 219 26 864 C ATOM 2207 CG ARG A1234 -21.296 -32.723 -26.382 1.00 63.19 C ANISOU 2207 CG ARG A1234 8947 9056 6007 206 88 998 C ATOM 2208 CD ARG A1234 -21.058 -34.030 -25.650 1.00 72.34 C ANISOU 2208 CD ARG A1234 10242 10185 7058 273 162 1245 C ATOM 2209 NE ARG A1234 -20.833 -35.139 -26.570 1.00 79.34 N ANISOU 2209 NE ARG A1234 11251 10800 8094 263 239 1364 N ATOM 2210 CZ ARG A1234 -20.478 -36.361 -26.190 1.00 95.95 C ANISOU 2210 CZ ARG A1234 13510 12800 10147 342 308 1587 C ATOM 2211 NH1 ARG A1234 -20.302 -36.630 -24.903 1.00105.55 N ANISOU 2211 NH1 ARG A1234 14760 14181 11163 433 304 1730 N ATOM 2212 NH2 ARG A1234 -20.295 -37.314 -27.094 1.00 97.70 N ANISOU 2212 NH2 ARG A1234 13866 12748 10509 337 382 1668 N ATOM 2213 N ASN A1235 -22.196 -30.302 -28.421 1.00 78.29 N ANISOU 2213 N ASN A1235 10635 10903 8209 43 2 533 N ATOM 2214 CA ASN A1235 -23.019 -30.326 -29.629 1.00 89.85 C ANISOU 2214 CA ASN A1235 12080 12228 9830 -73 71 472 C ATOM 2215 C ASN A1235 -22.514 -31.460 -30.515 1.00 97.42 C ANISOU 2215 C ASN A1235 13130 12972 10914 -88 115 591 C ATOM 2216 O ASN A1235 -21.511 -31.306 -31.218 1.00106.59 O ANISOU 2216 O ASN A1235 14273 14047 12179 -25 41 568 O ATOM 2217 CB ASN A1235 -22.970 -28.984 -30.353 1.00 86.29 C ANISOU 2217 CB ASN A1235 11527 11781 9478 -75 -17 276 C ATOM 2218 CG ASN A1235 -23.915 -28.923 -31.538 1.00 66.68 C ANISOU 2218 CG ASN A1235 9010 9198 7129 -183 49 213 C ATOM 2219 OD1 ASN A1235 -24.754 -29.804 -31.727 1.00 58.72 O ANISOU 2219 OD1 ASN A1235 8040 8148 6125 -280 160 295 O ATOM 2220 ND2 ASN A1235 -23.788 -27.872 -32.341 1.00 52.27 N ANISOU 2220 ND2 ASN A1235 7113 7341 5407 -177 -22 72 N ATOM 2221 N ASP A1236 -23.209 -32.599 -30.480 1.00 87.49 N ANISOU 2221 N ASP A1236 11975 11625 9641 -174 240 718 N ATOM 2222 CA ASP A1236 -22.818 -33.745 -31.292 1.00 95.15 C ANISOU 2222 CA ASP A1236 13074 12360 10718 -190 296 824 C ATOM 2223 C ASP A1236 -23.091 -33.541 -32.776 1.00100.30 C ANISOU 2223 C ASP A1236 13697 12873 11540 -283 300 707 C ATOM 2224 O ASP A1236 -22.652 -34.365 -33.586 1.00 95.36 O ANISOU 2224 O ASP A1236 13179 12046 11007 -280 335 760 O ATOM 2225 CB ASP A1236 -23.535 -35.003 -30.800 1.00 94.16 C ANISOU 2225 CB ASP A1236 13095 12158 10523 -284 430 989 C ATOM 2226 CG ASP A1236 -23.046 -35.458 -29.439 1.00101.27 C ANISOU 2226 CG ASP A1236 14063 13156 11258 -164 434 1151 C ATOM 2227 OD1 ASP A1236 -21.834 -35.326 -29.169 1.00103.16 O ANISOU 2227 OD1 ASP A1236 14294 13428 11475 12 343 1186 O ATOM 2228 OD2 ASP A1236 -23.873 -35.945 -28.640 1.00107.95 O ANISOU 2228 OD2 ASP A1236 14961 14066 11988 -248 527 1252 O ATOM 2229 N ASP A1237 -23.799 -32.479 -33.150 1.00 96.25 N ANISOU 2229 N ASP A1237 13049 12463 11058 -351 268 552 N ATOM 2230 CA ASP A1237 -24.040 -32.155 -34.548 1.00 91.73 C ANISOU 2230 CA ASP A1237 12433 11791 10631 -425 257 442 C ATOM 2231 C ASP A1237 -22.997 -31.205 -35.122 1.00 86.64 C ANISOU 2231 C ASP A1237 11707 11143 10067 -316 142 347 C ATOM 2232 O ASP A1237 -23.129 -30.792 -36.279 1.00 89.12 O ANISOU 2232 O ASP A1237 11976 11394 10493 -362 125 255 O ATOM 2233 CB ASP A1237 -25.437 -31.551 -34.720 1.00 92.75 C ANISOU 2233 CB ASP A1237 12455 12039 10747 -550 292 345 C ATOM 2234 CG ASP A1237 -26.543 -32.556 -34.462 1.00113.84 C ANISOU 2234 CG ASP A1237 15184 14707 13362 -710 413 439 C ATOM 2235 OD1 ASP A1237 -26.227 -33.739 -34.216 1.00123.31 O ANISOU 2235 OD1 ASP A1237 16538 15772 14544 -734 474 576 O ATOM 2236 OD2 ASP A1237 -27.728 -32.163 -34.506 1.00120.15 O ANISOU 2236 OD2 ASP A1237 15875 15644 14133 -813 451 384 O ATOM 2237 N ILE A1238 -21.970 -30.847 -34.346 1.00 82.37 N ANISOU 2237 N ILE A1238 11145 10685 9468 -185 61 372 N ATOM 2238 CA ILE A1238 -20.923 -29.972 -34.857 1.00 72.88 C ANISOU 2238 CA ILE A1238 9860 9491 8341 -109 -50 295 C ATOM 2239 C ILE A1238 -20.110 -30.660 -35.945 1.00 78.86 C ANISOU 2239 C ILE A1238 10666 10086 9213 -72 -33 349 C ATOM 2240 O ILE A1238 -19.525 -29.985 -36.800 1.00 80.86 O ANISOU 2240 O ILE A1238 10843 10320 9559 -55 -94 277 O ATOM 2241 CB ILE A1238 -20.012 -29.490 -33.710 1.00 65.97 C ANISOU 2241 CB ILE A1238 8942 8767 7358 -2 -149 313 C ATOM 2242 CG1 ILE A1238 -19.153 -28.307 -34.161 1.00 53.42 C ANISOU 2242 CG1 ILE A1238 7244 7215 5836 22 -273 203 C ATOM 2243 CG2 ILE A1238 -19.125 -30.621 -33.207 1.00 51.97 C ANISOU 2243 CG2 ILE A1238 7246 6972 5529 105 -132 487 C ATOM 2244 CD1 ILE A1238 -19.953 -27.090 -34.569 1.00 60.18 C ANISOU 2244 CD1 ILE A1238 8042 8084 6738 -54 -296 40 C ATOM 2245 N PHE A1239 -20.069 -31.995 -35.947 1.00 76.26 N ANISOU 2245 N PHE A1239 10473 9631 8872 -56 57 478 N ATOM 2246 CA PHE A1239 -19.341 -32.708 -36.989 1.00 74.35 C ANISOU 2246 CA PHE A1239 10301 9221 8725 1 91 521 C ATOM 2247 C PHE A1239 -20.085 -32.667 -38.316 1.00 82.95 C ANISOU 2247 C PHE A1239 11405 10196 9918 -128 136 421 C ATOM 2248 O PHE A1239 -19.454 -32.652 -39.379 1.00 71.28 O ANISOU 2248 O PHE A1239 9920 8636 8528 -85 127 391 O ATOM 2249 CB PHE A1239 -19.086 -34.150 -36.553 1.00 61.71 C ANISOU 2249 CB PHE A1239 8878 7493 7075 72 179 686 C ATOM 2250 CG PHE A1239 -18.326 -34.262 -35.262 1.00 79.64 C ANISOU 2250 CG PHE A1239 11135 9895 9229 217 133 807 C ATOM 2251 CD1 PHE A1239 -16.944 -34.178 -35.248 1.00 81.95 C ANISOU 2251 CD1 PHE A1239 11363 10249 9526 394 63 864 C ATOM 2252 CD2 PHE A1239 -18.994 -34.442 -34.062 1.00 88.55 C ANISOU 2252 CD2 PHE A1239 12301 11113 10232 176 158 868 C ATOM 2253 CE1 PHE A1239 -16.241 -34.276 -34.063 1.00 77.72 C ANISOU 2253 CE1 PHE A1239 10797 9864 8868 526 7 978 C ATOM 2254 CE2 PHE A1239 -18.296 -34.541 -32.873 1.00 85.97 C ANISOU 2254 CE2 PHE A1239 11961 10925 9778 311 109 981 C ATOM 2255 CZ PHE A1239 -16.918 -34.458 -32.873 1.00 86.48 C ANISOU 2255 CZ PHE A1239 11959 11054 9846 486 28 1035 C ATOM 2256 N LYS A1240 -21.419 -32.645 -38.279 1.00 84.72 N ANISOU 2256 N LYS A1240 11634 10434 10120 -284 183 372 N ATOM 2257 CA LYS A1240 -22.184 -32.444 -39.504 1.00 72.66 C ANISOU 2257 CA LYS A1240 10085 8851 8674 -412 204 269 C ATOM 2258 C LYS A1240 -22.021 -31.025 -40.031 1.00 70.28 C ANISOU 2258 C LYS A1240 9622 8655 8428 -387 111 150 C ATOM 2259 O LYS A1240 -22.070 -30.806 -41.247 1.00 79.89 O ANISOU 2259 O LYS A1240 10817 9813 9724 -425 106 83 O ATOM 2260 CB LYS A1240 -23.661 -32.754 -39.261 1.00 71.94 C ANISOU 2260 CB LYS A1240 10007 8795 8533 -587 273 260 C ATOM 2261 CG LYS A1240 -23.929 -34.165 -38.764 1.00 77.42 C ANISOU 2261 CG LYS A1240 10878 9366 9174 -652 374 385 C ATOM 2262 CD LYS A1240 -25.409 -34.381 -38.497 1.00 72.79 C ANISOU 2262 CD LYS A1240 10270 8854 8532 -853 438 381 C ATOM 2263 CE LYS A1240 -25.677 -35.783 -37.976 1.00 78.39 C ANISOU 2263 CE LYS A1240 11172 9425 9190 -947 543 518 C ATOM 2264 NZ LYS A1240 -27.120 -35.998 -37.680 1.00 97.15 N ANISOU 2264 NZ LYS A1240 13504 11902 11505 -1168 609 528 N ATOM 2265 N ILE A1241 -21.825 -30.054 -39.137 1.00 57.77 N ANISOU 2265 N ILE A1241 7940 7217 6794 -326 37 121 N ATOM 2266 CA ILE A1241 -21.613 -28.675 -39.566 1.00 61.89 C ANISOU 2266 CA ILE A1241 8340 7809 7369 -304 -52 13 C ATOM 2267 C ILE A1241 -20.249 -28.529 -40.228 1.00 76.25 C ANISOU 2267 C ILE A1241 10136 9573 9262 -220 -105 30 C ATOM 2268 O ILE A1241 -20.121 -27.922 -41.298 1.00 82.74 O ANISOU 2268 O ILE A1241 10905 10364 10168 -240 -130 -31 O ATOM 2269 CB ILE A1241 -21.768 -27.715 -38.373 1.00 66.83 C ANISOU 2269 CB ILE A1241 8901 8584 7910 -269 -113 -35 C ATOM 2270 CG1 ILE A1241 -23.170 -27.836 -37.771 1.00 78.89 C ANISOU 2270 CG1 ILE A1241 10428 10192 9354 -339 -45 -48 C ATOM 2271 CG2 ILE A1241 -21.485 -26.282 -38.799 1.00 63.40 C ANISOU 2271 CG2 ILE A1241 8376 8181 7534 -250 -205 -146 C ATOM 2272 CD1 ILE A1241 -23.391 -26.961 -36.556 1.00 90.19 C ANISOU 2272 CD1 ILE A1241 11815 11774 10678 -286 -88 -102 C ATOM 2273 N ILE A1242 -19.208 -29.082 -39.599 1.00 80.51 N ANISOU 2273 N ILE A1242 10705 10120 9763 -119 -119 127 N ATOM 2274 CA ILE A1242 -17.876 -29.061 -40.198 1.00 82.33 C ANISOU 2274 CA ILE A1242 10895 10333 10055 -27 -158 164 C ATOM 2275 C ILE A1242 -17.882 -29.805 -41.527 1.00 77.29 C ANISOU 2275 C ILE A1242 10328 9546 9492 -34 -77 174 C ATOM 2276 O ILE A1242 -17.201 -29.411 -42.482 1.00 69.88 O ANISOU 2276 O ILE A1242 9328 8598 8625 -5 -100 153 O ATOM 2277 CB ILE A1242 -16.843 -29.649 -39.218 1.00 85.03 C ANISOU 2277 CB ILE A1242 11248 10738 10323 101 -181 285 C ATOM 2278 CG1 ILE A1242 -16.758 -28.794 -37.952 1.00 71.33 C ANISOU 2278 CG1 ILE A1242 9435 9169 8496 98 -278 255 C ATOM 2279 CG2 ILE A1242 -15.475 -29.764 -39.874 1.00 78.81 C ANISOU 2279 CG2 ILE A1242 10398 9954 9590 212 -204 343 C ATOM 2280 CD1 ILE A1242 -15.784 -29.323 -36.922 1.00 57.85 C ANISOU 2280 CD1 ILE A1242 7723 7564 6693 222 -316 377 C ATOM 2281 N MET A1243 -18.661 -30.886 -41.612 1.00 85.14 N ANISOU 2281 N MET A1243 11460 10423 10464 -85 20 204 N ATOM 2282 CA MET A1243 -18.772 -31.626 -42.865 1.00 81.54 C ANISOU 2282 CA MET A1243 11102 9815 10065 -112 96 191 C ATOM 2283 C MET A1243 -19.432 -30.784 -43.949 1.00 75.75 C ANISOU 2283 C MET A1243 10290 9103 9389 -220 72 73 C ATOM 2284 O MET A1243 -18.999 -30.801 -45.107 1.00 70.61 O ANISOU 2284 O MET A1243 9641 8396 8792 -198 86 48 O ATOM 2285 CB MET A1243 -19.558 -32.918 -42.638 1.00 89.10 C ANISOU 2285 CB MET A1243 12240 10635 10979 -183 197 238 C ATOM 2286 CG MET A1243 -19.711 -33.786 -43.876 1.00102.85 C ANISOU 2286 CG MET A1243 14122 12196 12761 -228 277 209 C ATOM 2287 SD MET A1243 -18.157 -34.543 -44.385 1.00121.90 S ANISOU 2287 SD MET A1243 16625 14492 15198 -4 320 288 S ATOM 2288 CE MET A1243 -17.777 -35.531 -42.941 1.00124.90 C ANISOU 2288 CE MET A1243 17130 14823 15502 114 361 450 C ATOM 2289 N ALA A1244 -20.478 -30.034 -43.592 1.00 69.57 N ANISOU 2289 N ALA A1244 9435 8411 8586 -321 41 8 N ATOM 2290 CA ALA A1244 -21.195 -29.243 -44.585 1.00 62.06 C ANISOU 2290 CA ALA A1244 8410 7492 7680 -406 19 -88 C ATOM 2291 C ALA A1244 -20.391 -28.029 -45.032 1.00 63.51 C ANISOU 2291 C ALA A1244 8478 7732 7921 -341 -62 -121 C ATOM 2292 O ALA A1244 -20.486 -27.623 -46.195 1.00 67.43 O ANISOU 2292 O ALA A1244 8941 8213 8467 -369 -67 -165 O ATOM 2293 CB ALA A1244 -22.551 -28.806 -44.032 1.00 59.03 C ANISOU 2293 CB ALA A1244 7973 7207 7248 -502 17 -136 C ATOM 2294 N ILE A1245 -19.601 -27.440 -44.133 1.00 68.58 N ANISOU 2294 N ILE A1245 9062 8446 8552 -268 -128 -97 N ATOM 2295 CA ILE A1245 -18.837 -26.246 -44.482 1.00 66.53 C ANISOU 2295 CA ILE A1245 8698 8234 8346 -241 -209 -126 C ATOM 2296 C ILE A1245 -17.779 -26.568 -45.531 1.00 70.90 C ANISOU 2296 C ILE A1245 9241 8742 8955 -188 -190 -80 C ATOM 2297 O ILE A1245 -17.583 -25.809 -46.488 1.00 71.22 O ANISOU 2297 O ILE A1245 9222 8787 9053 -210 -214 -109 O ATOM 2298 CB ILE A1245 -18.214 -25.626 -43.217 1.00 64.59 C ANISOU 2298 CB ILE A1245 8402 8080 8059 -200 -291 -119 C ATOM 2299 CG1 ILE A1245 -19.299 -24.989 -42.345 1.00 65.90 C ANISOU 2299 CG1 ILE A1245 8569 8301 8168 -243 -311 -192 C ATOM 2300 CG2 ILE A1245 -17.147 -24.606 -43.583 1.00 58.11 C ANISOU 2300 CG2 ILE A1245 7486 7296 7296 -193 -374 -127 C ATOM 2301 CD1 ILE A1245 -18.770 -24.363 -41.074 1.00 65.57 C ANISOU 2301 CD1 ILE A1245 8500 8350 8063 -211 -393 -207 C ATOM 2302 N VAL A1246 -17.089 -27.699 -45.377 1.00 67.30 N ANISOU 2302 N VAL A1246 8848 8246 8476 -104 -138 2 N ATOM 2303 CA VAL A1246 -16.020 -28.050 -46.307 1.00 68.05 C ANISOU 2303 CA VAL A1246 8928 8318 8609 -19 -107 52 C ATOM 2304 C VAL A1246 -16.596 -28.449 -47.661 1.00 73.55 C ANISOU 2304 C VAL A1246 9699 8918 9330 -65 -34 4 C ATOM 2305 O VAL A1246 -16.122 -28.001 -48.712 1.00 80.00 O ANISOU 2305 O VAL A1246 10457 9752 10187 -53 -35 -5 O ATOM 2306 CB VAL A1246 -15.141 -29.166 -45.716 1.00 66.50 C ANISOU 2306 CB VAL A1246 8788 8107 8372 119 -64 158 C ATOM 2307 CG1 VAL A1246 -14.052 -29.560 -46.702 1.00 66.50 C ANISOU 2307 CG1 VAL A1246 8767 8097 8401 237 -16 210 C ATOM 2308 CG2 VAL A1246 -14.536 -28.720 -44.394 1.00 66.93 C ANISOU 2308 CG2 VAL A1246 8752 8294 8385 160 -152 206 C ATOM 2309 N LEU A1247 -17.627 -29.297 -47.657 1.00 72.98 N ANISOU 2309 N LEU A1247 9755 8752 9223 -131 28 -26 N ATOM 2310 CA LEU A1247 -18.199 -29.766 -48.915 1.00 69.61 C ANISOU 2310 CA LEU A1247 9410 8240 8799 -193 88 -82 C ATOM 2311 C LEU A1247 -18.933 -28.654 -49.654 1.00 80.81 C ANISOU 2311 C LEU A1247 10730 9732 10243 -291 37 -157 C ATOM 2312 O LEU A1247 -19.048 -28.703 -50.884 1.00 83.79 O ANISOU 2312 O LEU A1247 11125 10087 10624 -316 63 -194 O ATOM 2313 CB LEU A1247 -19.136 -30.946 -48.662 1.00 55.95 C ANISOU 2313 CB LEU A1247 7842 6397 7021 -276 159 -94 C ATOM 2314 CG LEU A1247 -18.490 -32.206 -48.083 1.00 48.37 C ANISOU 2314 CG LEU A1247 7031 5317 6032 -170 229 -10 C ATOM 2315 CD1 LEU A1247 -19.507 -33.333 -47.977 1.00 46.61 C ANISOU 2315 CD1 LEU A1247 6990 4954 5766 -294 302 -27 C ATOM 2316 CD2 LEU A1247 -17.295 -32.634 -48.922 1.00 46.24 C ANISOU 2316 CD2 LEU A1247 6800 4990 5778 -15 277 22 C ATOM 2317 N PHE A1248 -19.437 -27.650 -48.932 1.00 75.62 N ANISOU 2317 N PHE A1248 9977 9162 9591 -333 -33 -179 N ATOM 2318 CA PHE A1248 -20.096 -26.531 -49.597 1.00 69.69 C ANISOU 2318 CA PHE A1248 9141 8474 8865 -392 -80 -236 C ATOM 2319 C PHE A1248 -19.089 -25.678 -50.357 1.00 76.28 C ANISOU 2319 C PHE A1248 9897 9332 9753 -339 -115 -213 C ATOM 2320 O PHE A1248 -19.394 -25.162 -51.438 1.00 91.23 O ANISOU 2320 O PHE A1248 11762 11241 11661 -369 -120 -237 O ATOM 2321 CB PHE A1248 -20.857 -25.684 -48.578 1.00 67.74 C ANISOU 2321 CB PHE A1248 8834 8300 8605 -419 -133 -267 C ATOM 2322 CG PHE A1248 -21.829 -24.720 -49.193 1.00 76.24 C ANISOU 2322 CG PHE A1248 9845 9433 9691 -463 -164 -321 C ATOM 2323 CD1 PHE A1248 -23.092 -25.140 -49.576 1.00 72.61 C ANISOU 2323 CD1 PHE A1248 9393 9009 9187 -544 -130 -356 C ATOM 2324 CD2 PHE A1248 -21.485 -23.391 -49.381 1.00 86.40 C ANISOU 2324 CD2 PHE A1248 11064 10741 11024 -426 -227 -329 C ATOM 2325 CE1 PHE A1248 -23.991 -24.256 -50.140 1.00 73.57 C ANISOU 2325 CE1 PHE A1248 9438 9210 9307 -559 -161 -392 C ATOM 2326 CE2 PHE A1248 -22.381 -22.502 -49.944 1.00 75.11 C ANISOU 2326 CE2 PHE A1248 9587 9352 9598 -437 -250 -363 C ATOM 2327 CZ PHE A1248 -23.636 -22.935 -50.323 1.00 72.25 C ANISOU 2327 CZ PHE A1248 9215 9050 9187 -490 -218 -392 C ATOM 2328 N PHE A1249 -17.883 -25.517 -49.808 1.00 75.35 N ANISOU 2328 N PHE A1249 9737 9235 9659 -267 -142 -156 N ATOM 2329 CA PHE A1249 -16.840 -24.787 -50.518 1.00 70.42 C ANISOU 2329 CA PHE A1249 9025 8649 9082 -236 -168 -117 C ATOM 2330 C PHE A1249 -16.281 -25.599 -51.677 1.00 73.53 C ANISOU 2330 C PHE A1249 9455 9015 9467 -181 -88 -87 C ATOM 2331 O PHE A1249 -15.883 -25.028 -52.699 1.00 83.14 O ANISOU 2331 O PHE A1249 10616 10265 10709 -183 -87 -71 O ATOM 2332 CB PHE A1249 -15.719 -24.401 -49.550 1.00 57.69 C ANISOU 2332 CB PHE A1249 7334 7099 7485 -195 -228 -64 C ATOM 2333 CG PHE A1249 -14.578 -23.667 -50.198 1.00 58.71 C ANISOU 2333 CG PHE A1249 7355 7289 7664 -190 -256 -11 C ATOM 2334 CD1 PHE A1249 -14.610 -22.288 -50.330 1.00 58.55 C ANISOU 2334 CD1 PHE A1249 7274 7282 7690 -273 -328 -31 C ATOM 2335 CD2 PHE A1249 -13.467 -24.353 -50.665 1.00 67.35 C ANISOU 2335 CD2 PHE A1249 8411 8427 8753 -100 -203 67 C ATOM 2336 CE1 PHE A1249 -13.561 -21.610 -50.922 1.00 68.86 C ANISOU 2336 CE1 PHE A1249 8480 8643 9039 -296 -350 31 C ATOM 2337 CE2 PHE A1249 -12.416 -23.680 -51.259 1.00 60.26 C ANISOU 2337 CE2 PHE A1249 7389 7615 7893 -106 -221 129 C ATOM 2338 CZ PHE A1249 -12.463 -22.307 -51.387 1.00 63.58 C ANISOU 2338 CZ PHE A1249 7748 8048 8363 -221 -297 113 C ATOM 2339 N PHE A1250 -16.246 -26.925 -51.541 1.00 68.66 N ANISOU 2339 N PHE A1250 8948 8332 8810 -126 -15 -77 N ATOM 2340 CA PHE A1250 -15.637 -27.770 -52.563 1.00 78.43 C ANISOU 2340 CA PHE A1250 10246 9527 10026 -45 72 -57 C ATOM 2341 C PHE A1250 -16.576 -27.977 -53.748 1.00 83.46 C ANISOU 2341 C PHE A1250 10963 10116 10630 -124 110 -135 C ATOM 2342 O PHE A1250 -16.220 -27.682 -54.893 1.00 83.87 O ANISOU 2342 O PHE A1250 10983 10206 10678 -105 132 -134 O ATOM 2343 CB PHE A1250 -15.230 -29.114 -51.951 1.00 82.03 C ANISOU 2343 CB PHE A1250 10821 9901 10446 60 140 -16 C ATOM 2344 CG PHE A1250 -14.492 -30.014 -52.900 1.00 81.10 C ANISOU 2344 CG PHE A1250 10785 9730 10300 185 240 3 C ATOM 2345 CD1 PHE A1250 -13.139 -29.833 -53.137 1.00 84.72 C ANISOU 2345 CD1 PHE A1250 11130 10287 10771 324 255 86 C ATOM 2346 CD2 PHE A1250 -15.148 -31.046 -53.549 1.00 78.00 C ANISOU 2346 CD2 PHE A1250 10583 9195 9860 160 320 -65 C ATOM 2347 CE1 PHE A1250 -12.456 -30.662 -54.007 1.00 86.89 C ANISOU 2347 CE1 PHE A1250 11480 10526 11009 468 360 103 C ATOM 2348 CE2 PHE A1250 -14.471 -31.878 -54.421 1.00 78.53 C ANISOU 2348 CE2 PHE A1250 10752 9197 9888 291 420 -63 C ATOM 2349 CZ PHE A1250 -13.123 -31.685 -54.650 1.00 80.86 C ANISOU 2349 CZ PHE A1250 10932 9597 10194 461 446 23 C ATOM 2350 N PHE A1251 -17.784 -28.482 -53.488 1.00 77.19 N ANISOU 2350 N PHE A1251 10264 9261 9804 -222 117 -198 N ATOM 2351 CA PHE A1251 -18.716 -28.796 -54.566 1.00 50.70 C ANISOU 2351 CA PHE A1251 6982 5879 6401 -317 144 -277 C ATOM 2352 C PHE A1251 -19.269 -27.561 -55.263 1.00 70.93 C ANISOU 2352 C PHE A1251 9424 8550 8974 -381 80 -299 C ATOM 2353 O PHE A1251 -19.862 -27.696 -56.339 1.00 88.16 O ANISOU 2353 O PHE A1251 11641 10748 11107 -442 93 -352 O ATOM 2354 CB PHE A1251 -19.872 -29.644 -54.033 1.00 46.99 C ANISOU 2354 CB PHE A1251 6624 5340 5891 -433 162 -328 C ATOM 2355 CG PHE A1251 -19.515 -31.086 -53.820 1.00 60.74 C ANISOU 2355 CG PHE A1251 8550 6926 7600 -391 249 -320 C ATOM 2356 CD1 PHE A1251 -19.420 -31.953 -54.896 1.00 56.05 C ANISOU 2356 CD1 PHE A1251 8104 6234 6957 -389 320 -374 C ATOM 2357 CD2 PHE A1251 -19.277 -31.577 -52.547 1.00 80.99 C ANISOU 2357 CD2 PHE A1251 11160 9436 10176 -344 262 -258 C ATOM 2358 CE1 PHE A1251 -19.093 -33.282 -54.708 1.00 59.07 C ANISOU 2358 CE1 PHE A1251 8692 6440 7311 -336 408 -370 C ATOM 2359 CE2 PHE A1251 -18.950 -32.906 -52.352 1.00 88.99 C ANISOU 2359 CE2 PHE A1251 12365 10286 11160 -289 348 -235 C ATOM 2360 CZ PHE A1251 -18.857 -33.759 -53.434 1.00 80.18 C ANISOU 2360 CZ PHE A1251 11413 9047 10005 -282 423 -293 C ATOM 2361 N SER A1252 -19.098 -26.370 -54.688 1.00 73.09 N ANISOU 2361 N SER A1252 9573 8893 9304 -368 9 -261 N ATOM 2362 CA SER A1252 -19.571 -25.164 -55.360 1.00 82.25 C ANISOU 2362 CA SER A1252 10642 10130 10478 -405 -45 -267 C ATOM 2363 C SER A1252 -18.562 -24.663 -56.384 1.00 78.15 C ANISOU 2363 C SER A1252 10073 9643 9975 -349 -32 -213 C ATOM 2364 O SER A1252 -18.949 -24.156 -57.443 1.00 91.62 O ANISOU 2364 O SER A1252 11756 11398 11656 -375 -40 -218 O ATOM 2365 CB SER A1252 -19.875 -24.071 -54.335 1.00 94.15 C ANISOU 2365 CB SER A1252 12070 11669 12034 -414 -120 -258 C ATOM 2366 OG SER A1252 -18.734 -23.774 -53.549 1.00109.37 O ANISOU 2366 OG SER A1252 13960 13586 14011 -359 -143 -207 O ATOM 2367 N TRP A1253 -17.267 -24.801 -56.093 1.00 62.49 N ANISOU 2367 N TRP A1253 8062 7655 8025 -271 -10 -151 N ATOM 2368 CA TRP A1253 -16.223 -24.292 -56.972 1.00 63.40 C ANISOU 2368 CA TRP A1253 8104 7828 8155 -224 8 -82 C ATOM 2369 C TRP A1253 -15.632 -25.345 -57.898 1.00 72.99 C ANISOU 2369 C TRP A1253 9386 9039 9309 -143 108 -81 C ATOM 2370 O TRP A1253 -15.061 -24.980 -58.932 1.00 86.52 O ANISOU 2370 O TRP A1253 11050 10819 11005 -114 139 -37 O ATOM 2371 CB TRP A1253 -15.090 -23.668 -56.147 1.00 70.43 C ANISOU 2371 CB TRP A1253 8888 8759 9113 -197 -33 -6 C ATOM 2372 CG TRP A1253 -15.472 -22.394 -55.462 1.00 77.84 C ANISOU 2372 CG TRP A1253 9771 9696 10108 -274 -129 -9 C ATOM 2373 CD1 TRP A1253 -15.767 -22.229 -54.140 1.00 76.24 C ANISOU 2373 CD1 TRP A1253 9575 9468 9925 -296 -187 -41 C ATOM 2374 CD2 TRP A1253 -15.603 -21.102 -56.067 1.00 87.02 C ANISOU 2374 CD2 TRP A1253 10886 10872 11307 -331 -173 18 C ATOM 2375 NE1 TRP A1253 -16.072 -20.914 -53.884 1.00 81.52 N ANISOU 2375 NE1 TRP A1253 10210 10126 10638 -356 -262 -50 N ATOM 2376 CE2 TRP A1253 -15.979 -20.202 -55.051 1.00 85.54 C ANISOU 2376 CE2 TRP A1253 10691 10646 11163 -378 -255 -9 C ATOM 2377 CE3 TRP A1253 -15.439 -20.620 -57.369 1.00 91.76 C ANISOU 2377 CE3 TRP A1253 11459 11508 11897 -339 -146 68 C ATOM 2378 CZ2 TRP A1253 -16.193 -18.847 -55.296 1.00 92.28 C ANISOU 2378 CZ2 TRP A1253 11530 11470 12061 -428 -308 9 C ATOM 2379 CZ3 TRP A1253 -15.652 -19.276 -57.610 1.00 95.30 C ANISOU 2379 CZ3 TRP A1253 11881 11938 12389 -395 -201 102 C ATOM 2380 CH2 TRP A1253 -16.025 -18.404 -56.579 1.00 95.80 C ANISOU 2380 CH2 TRP A1253 11956 11937 12506 -436 -281 71 C ATOM 2381 N ILE A1254 -15.754 -26.627 -57.568 1.00 70.34 N ANISOU 2381 N ILE A1254 9173 8619 8932 -102 165 -125 N ATOM 2382 CA ILE A1254 -15.109 -27.682 -58.350 1.00 62.44 C ANISOU 2382 CA ILE A1254 8267 7587 7870 4 270 -131 C ATOM 2383 C ILE A1254 -15.726 -27.853 -59.740 1.00 74.06 C ANISOU 2383 C ILE A1254 9816 9065 9259 -43 305 -203 C ATOM 2384 O ILE A1254 -15.035 -28.366 -60.631 1.00 75.78 O ANISOU 2384 O ILE A1254 10081 9294 9417 56 391 -200 O ATOM 2385 CB ILE A1254 -15.093 -29.015 -57.577 1.00 53.77 C ANISOU 2385 CB ILE A1254 7317 6361 6753 65 324 -155 C ATOM 2386 CG1 ILE A1254 -13.930 -29.888 -58.052 1.00 56.37 C ANISOU 2386 CG1 ILE A1254 7704 6672 7042 247 432 -118 C ATOM 2387 CG2 ILE A1254 -16.397 -29.780 -57.732 1.00 56.29 C ANISOU 2387 CG2 ILE A1254 7802 6568 7017 -53 335 -264 C ATOM 2388 CD1 ILE A1254 -12.579 -29.218 -57.939 1.00 66.40 C ANISOU 2388 CD1 ILE A1254 8784 8091 8356 358 427 2 C ATOM 2389 N PRO A1255 -16.981 -27.458 -60.011 1.00 68.84 N ANISOU 2389 N PRO A1255 9163 8416 8575 -177 246 -265 N ATOM 2390 CA PRO A1255 -17.404 -27.457 -61.422 1.00 71.67 C ANISOU 2390 CA PRO A1255 9562 8828 8842 -213 267 -315 C ATOM 2391 C PRO A1255 -16.755 -26.350 -62.231 1.00 75.94 C ANISOU 2391 C PRO A1255 9970 9493 9390 -171 259 -227 C ATOM 2392 O PRO A1255 -16.367 -26.577 -63.384 1.00 84.17 O ANISOU 2392 O PRO A1255 11045 10587 10350 -121 322 -231 O ATOM 2393 CB PRO A1255 -18.929 -27.285 -61.338 1.00 70.68 C ANISOU 2393 CB PRO A1255 9447 8717 8691 -363 194 -387 C ATOM 2394 CG PRO A1255 -19.287 -27.707 -59.967 1.00 69.86 C ANISOU 2394 CG PRO A1255 9374 8527 8644 -399 174 -400 C ATOM 2395 CD PRO A1255 -18.146 -27.243 -59.129 1.00 74.12 C ANISOU 2395 CD PRO A1255 9826 9062 9272 -292 172 -305 C ATOM 2396 N HIS A1256 -16.616 -25.153 -61.655 1.00 66.02 N ANISOU 2396 N HIS A1256 8578 8281 8227 -195 187 -146 N ATOM 2397 CA HIS A1256 -16.043 -24.036 -62.398 1.00 63.62 C ANISOU 2397 CA HIS A1256 8160 8074 7936 -183 177 -49 C ATOM 2398 C HIS A1256 -14.535 -24.174 -62.560 1.00 68.13 C ANISOU 2398 C HIS A1256 8669 8696 8522 -81 250 36 C ATOM 2399 O HIS A1256 -13.983 -23.742 -63.578 1.00 75.14 O ANISOU 2399 O HIS A1256 9501 9678 9369 -55 291 104 O ATOM 2400 CB HIS A1256 -16.385 -22.717 -61.703 1.00 68.61 C ANISOU 2400 CB HIS A1256 8700 8706 8664 -249 79 1 C ATOM 2401 CG HIS A1256 -15.756 -21.517 -62.339 1.00 74.00 C ANISOU 2401 CG HIS A1256 9286 9455 9377 -256 68 115 C ATOM 2402 ND1 HIS A1256 -14.526 -21.028 -61.952 1.00 82.22 N ANISOU 2402 ND1 HIS A1256 10231 10517 10490 -246 72 208 N ATOM 2403 CD2 HIS A1256 -16.186 -20.706 -63.334 1.00 79.64 C ANISOU 2403 CD2 HIS A1256 9984 10222 10053 -282 52 160 C ATOM 2404 CE1 HIS A1256 -14.226 -19.969 -62.682 1.00 85.61 C ANISOU 2404 CE1 HIS A1256 10600 10996 10933 -282 64 306 C ATOM 2405 NE2 HIS A1256 -15.216 -19.752 -63.529 1.00 84.02 N ANISOU 2405 NE2 HIS A1256 10451 10808 10664 -293 54 283 N ATOM 2406 N GLN A1257 -13.854 -24.768 -61.579 1.00 69.68 N ANISOU 2406 N GLN A1257 8861 8850 8765 -17 269 47 N ATOM 2407 CA GLN A1257 -12.402 -24.877 -61.635 1.00 72.80 C ANISOU 2407 CA GLN A1257 9161 9329 9172 91 332 142 C ATOM 2408 C GLN A1257 -11.924 -25.959 -62.594 1.00 81.22 C ANISOU 2408 C GLN A1257 10314 10415 10132 226 459 116 C ATOM 2409 O GLN A1257 -10.775 -25.900 -63.046 1.00 81.74 O ANISOU 2409 O GLN A1257 10279 10598 10180 324 529 206 O ATOM 2410 CB GLN A1257 -11.837 -25.141 -60.238 1.00 75.70 C ANISOU 2410 CB GLN A1257 9483 9669 9609 130 301 172 C ATOM 2411 CG GLN A1257 -12.052 -24.001 -59.252 1.00 82.99 C ANISOU 2411 CG GLN A1257 10314 10590 10627 10 181 200 C ATOM 2412 CD GLN A1257 -11.317 -22.734 -59.648 1.00 87.23 C ANISOU 2412 CD GLN A1257 10700 11232 11212 -55 149 304 C ATOM 2413 OE1 GLN A1257 -10.326 -22.777 -60.378 1.00 81.81 O ANISOU 2413 OE1 GLN A1257 9926 10658 10499 5 218 386 O ATOM 2414 NE2 GLN A1257 -11.801 -21.595 -59.166 1.00 89.31 N ANISOU 2414 NE2 GLN A1257 10937 11454 11542 -177 50 304 N ATOM 2415 N ILE A1258 -12.767 -26.940 -62.915 1.00 87.01 N ANISOU 2415 N ILE A1258 11232 11041 10787 228 494 -6 N ATOM 2416 CA ILE A1258 -12.370 -27.979 -63.859 1.00 87.56 C ANISOU 2416 CA ILE A1258 11424 11102 10742 356 617 -56 C ATOM 2417 C ILE A1258 -12.450 -27.463 -65.290 1.00 78.38 C ANISOU 2417 C ILE A1258 10237 10057 9487 334 646 -50 C ATOM 2418 O ILE A1258 -11.511 -27.624 -66.078 1.00 74.71 O ANISOU 2418 O ILE A1258 9738 9693 8954 461 746 -1 O ATOM 2419 CB ILE A1258 -13.228 -29.242 -63.661 1.00 81.44 C ANISOU 2419 CB ILE A1258 10883 10148 9913 340 641 -197 C ATOM 2420 CG1 ILE A1258 -12.846 -29.941 -62.355 1.00 76.34 C ANISOU 2420 CG1 ILE A1258 10276 9393 9336 419 651 -173 C ATOM 2421 CG2 ILE A1258 -13.070 -30.188 -64.843 1.00 66.35 C ANISOU 2421 CG2 ILE A1258 9140 8209 7863 436 757 -283 C ATOM 2422 CD1 ILE A1258 -13.639 -31.199 -62.080 1.00 70.66 C ANISOU 2422 CD1 ILE A1258 9801 8473 8573 390 682 -293 C ATOM 2423 N PHE A1259 -13.571 -26.833 -65.650 1.00 66.38 N ANISOU 2423 N PHE A1259 8727 8544 7952 185 562 -91 N ATOM 2424 CA PHE A1259 -13.692 -26.244 -66.978 1.00 68.96 C ANISOU 2424 CA PHE A1259 9021 8997 8182 163 576 -67 C ATOM 2425 C PHE A1259 -12.772 -25.045 -67.160 1.00 78.27 C ANISOU 2425 C PHE A1259 10005 10311 9421 175 575 101 C ATOM 2426 O PHE A1259 -12.430 -24.710 -68.299 1.00 98.24 O ANISOU 2426 O PHE A1259 12499 12965 11861 204 629 156 O ATOM 2427 CB PHE A1259 -15.144 -25.849 -67.250 1.00 69.26 C ANISOU 2427 CB PHE A1259 9102 9028 8186 15 478 -136 C ATOM 2428 CG PHE A1259 -16.061 -27.024 -67.442 1.00 80.27 C ANISOU 2428 CG PHE A1259 10685 10332 9483 -32 487 -302 C ATOM 2429 CD1 PHE A1259 -16.135 -27.666 -68.667 1.00 86.31 C ANISOU 2429 CD1 PHE A1259 11572 11139 10084 -5 552 -386 C ATOM 2430 CD2 PHE A1259 -16.843 -27.489 -66.398 1.00 75.19 C ANISOU 2430 CD2 PHE A1259 10104 9564 8902 -116 431 -374 C ATOM 2431 CE1 PHE A1259 -16.974 -28.750 -68.849 1.00 84.92 C ANISOU 2431 CE1 PHE A1259 11585 10867 9813 -80 554 -550 C ATOM 2432 CE2 PHE A1259 -17.684 -28.572 -66.573 1.00 65.70 C ANISOU 2432 CE2 PHE A1259 9078 8274 7611 -194 439 -520 C ATOM 2433 CZ PHE A1259 -17.749 -29.203 -67.800 1.00 82.37 C ANISOU 2433 CZ PHE A1259 11319 10413 9564 -185 496 -613 C ATOM 2434 N THR A1260 -12.368 -24.391 -66.068 1.00 72.08 N ANISOU 2434 N THR A1260 9101 9508 8778 138 513 183 N ATOM 2435 CA THR A1260 -11.310 -23.392 -66.160 1.00 68.97 C ANISOU 2435 CA THR A1260 8528 9234 8443 133 520 341 C ATOM 2436 C THR A1260 -9.991 -24.039 -66.561 1.00 61.69 C ANISOU 2436 C THR A1260 7547 8427 7467 287 648 399 C ATOM 2437 O THR A1260 -9.255 -23.506 -67.399 1.00 51.09 O ANISOU 2437 O THR A1260 6094 7236 6084 304 707 511 O ATOM 2438 CB THR A1260 -11.166 -22.653 -64.828 1.00 63.69 C ANISOU 2438 CB THR A1260 7764 8512 7924 48 419 391 C ATOM 2439 OG1 THR A1260 -12.356 -21.898 -64.566 1.00 76.98 O ANISOU 2439 OG1 THR A1260 9492 10108 9649 -72 313 351 O ATOM 2440 CG2 THR A1260 -9.968 -21.714 -64.858 1.00 51.55 C ANISOU 2440 CG2 THR A1260 6042 7097 6448 15 424 549 C ATOM 2441 N PHE A1261 -9.682 -25.199 -65.975 1.00 54.96 N ANISOU 2441 N PHE A1261 6767 7509 6605 410 700 334 N ATOM 2442 CA PHE A1261 -8.485 -25.936 -66.363 1.00 64.75 C ANISOU 2442 CA PHE A1261 7966 8857 7778 602 834 381 C ATOM 2443 C PHE A1261 -8.595 -26.471 -67.785 1.00 75.40 C ANISOU 2443 C PHE A1261 9432 10254 8964 691 947 320 C ATOM 2444 O PHE A1261 -7.584 -26.565 -68.490 1.00 68.74 O ANISOU 2444 O PHE A1261 8500 9570 8047 823 1062 400 O ATOM 2445 CB PHE A1261 -8.236 -27.077 -65.376 1.00 70.15 C ANISOU 2445 CB PHE A1261 8734 9433 8487 733 862 327 C ATOM 2446 CG PHE A1261 -7.008 -27.888 -65.678 1.00 70.08 C ANISOU 2446 CG PHE A1261 8687 9529 8409 972 1005 381 C ATOM 2447 CD1 PHE A1261 -5.750 -27.414 -65.344 1.00 69.27 C ANISOU 2447 CD1 PHE A1261 8337 9624 8357 1033 1022 540 C ATOM 2448 CD2 PHE A1261 -7.113 -29.128 -66.286 1.00 64.38 C ANISOU 2448 CD2 PHE A1261 8179 8716 7567 1139 1125 269 C ATOM 2449 CE1 PHE A1261 -4.619 -28.160 -65.617 1.00 69.89 C ANISOU 2449 CE1 PHE A1261 8357 9832 8365 1278 1160 601 C ATOM 2450 CE2 PHE A1261 -5.986 -29.878 -66.562 1.00 66.53 C ANISOU 2450 CE2 PHE A1261 8427 9082 7769 1395 1269 318 C ATOM 2451 CZ PHE A1261 -4.737 -29.393 -66.227 1.00 68.81 C ANISOU 2451 CZ PHE A1261 8443 9594 8107 1477 1289 490 C ATOM 2452 N LEU A1262 -9.806 -26.827 -68.221 1.00 79.88 N ANISOU 2452 N LEU A1262 10188 10702 9459 618 915 179 N ATOM 2453 CA LEU A1262 -9.999 -27.249 -69.604 1.00 71.37 C ANISOU 2453 CA LEU A1262 9229 9680 8207 674 1002 107 C ATOM 2454 C LEU A1262 -9.821 -26.086 -70.571 1.00 72.54 C ANISOU 2454 C LEU A1262 9235 10015 8313 609 999 230 C ATOM 2455 O LEU A1262 -9.411 -26.293 -71.719 1.00 85.06 O ANISOU 2455 O LEU A1262 10841 11727 9751 704 1107 237 O ATOM 2456 CB LEU A1262 -11.381 -27.880 -69.775 1.00 70.88 C ANISOU 2456 CB LEU A1262 9390 9466 8077 576 948 -74 C ATOM 2457 CG LEU A1262 -11.484 -29.404 -69.653 1.00 76.63 C ANISOU 2457 CG LEU A1262 10357 10026 8734 680 1026 -230 C ATOM 2458 CD1 LEU A1262 -10.788 -29.914 -68.399 1.00 69.54 C ANISOU 2458 CD1 LEU A1262 9437 9031 7956 789 1049 -185 C ATOM 2459 CD2 LEU A1262 -12.941 -29.838 -69.669 1.00 86.24 C ANISOU 2459 CD2 LEU A1262 11756 11104 9908 511 942 -392 C ATOM 2460 N ASP A1263 -10.124 -24.863 -70.129 1.00 65.22 N ANISOU 2460 N ASP A1263 8179 9099 7505 453 883 328 N ATOM 2461 CA ASP A1263 -9.868 -23.691 -70.957 1.00 70.70 C ANISOU 2461 CA ASP A1263 8742 9946 8174 387 883 474 C ATOM 2462 C ASP A1263 -8.374 -23.457 -71.148 1.00 82.26 C ANISOU 2462 C ASP A1263 10025 11584 9645 475 988 631 C ATOM 2463 O ASP A1263 -7.955 -22.950 -72.195 1.00 97.77 O ANISOU 2463 O ASP A1263 11917 13713 11520 483 1057 737 O ATOM 2464 CB ASP A1263 -10.527 -22.459 -70.336 1.00 77.37 C ANISOU 2464 CB ASP A1263 9521 10721 9155 212 739 539 C ATOM 2465 CG ASP A1263 -10.141 -21.172 -71.038 1.00 95.73 C ANISOU 2465 CG ASP A1263 11720 13171 11483 138 739 717 C ATOM 2466 OD1 ASP A1263 -10.581 -20.965 -72.187 1.00102.87 O ANISOU 2466 OD1 ASP A1263 12673 14156 12257 139 763 731 O ATOM 2467 OD2 ASP A1263 -9.396 -20.368 -70.440 1.00103.54 O ANISOU 2467 OD2 ASP A1263 12565 14177 12598 70 713 847 O ATOM 2468 N VAL A1264 -7.560 -23.822 -70.155 1.00 68.62 N ANISOU 2468 N VAL A1264 8211 9847 8016 542 1003 659 N ATOM 2469 CA VAL A1264 -6.117 -23.640 -70.272 1.00 73.53 C ANISOU 2469 CA VAL A1264 8627 10671 8641 626 1099 815 C ATOM 2470 C VAL A1264 -5.533 -24.629 -71.273 1.00 83.05 C ANISOU 2470 C VAL A1264 9884 11998 9671 848 1273 783 C ATOM 2471 O VAL A1264 -4.608 -24.298 -72.025 1.00 86.68 O ANISOU 2471 O VAL A1264 10192 12681 10062 904 1377 917 O ATOM 2472 CB VAL A1264 -5.451 -23.770 -68.890 1.00 81.09 C ANISOU 2472 CB VAL A1264 9467 11607 9738 640 1051 854 C ATOM 2473 CG1 VAL A1264 -3.955 -23.509 -68.991 1.00 75.51 C ANISOU 2473 CG1 VAL A1264 8507 11152 9034 705 1137 1030 C ATOM 2474 CG2 VAL A1264 -6.097 -22.816 -67.900 1.00 83.68 C ANISOU 2474 CG2 VAL A1264 9775 11801 10219 427 881 860 C ATOM 2475 N LEU A1265 -6.060 -25.856 -71.302 1.00 81.29 N ANISOU 2475 N LEU A1265 9886 11631 9368 974 1313 603 N ATOM 2476 CA LEU A1265 -5.560 -26.854 -72.243 1.00 83.48 C ANISOU 2476 CA LEU A1265 10261 11991 9468 1201 1483 543 C ATOM 2477 C LEU A1265 -5.813 -26.429 -73.684 1.00 86.44 C ANISOU 2477 C LEU A1265 10664 12500 9680 1169 1536 556 C ATOM 2478 O LEU A1265 -4.989 -26.690 -74.569 1.00 96.77 O ANISOU 2478 O LEU A1265 11925 13995 10849 1332 1689 605 O ATOM 2479 CB LEU A1265 -6.202 -28.212 -71.960 1.00 69.45 C ANISOU 2479 CB LEU A1265 8764 9981 7641 1304 1501 334 C ATOM 2480 CG LEU A1265 -5.779 -28.899 -70.660 1.00 65.46 C ANISOU 2480 CG LEU A1265 8259 9359 7253 1409 1494 330 C ATOM 2481 CD1 LEU A1265 -6.507 -30.222 -70.487 1.00 60.35 C ANISOU 2481 CD1 LEU A1265 7926 8454 6549 1485 1517 128 C ATOM 2482 CD2 LEU A1265 -4.272 -29.105 -70.634 1.00 64.41 C ANISOU 2482 CD2 LEU A1265 7936 9433 7105 1638 1626 470 C ATOM 2483 N ILE A1266 -6.947 -25.774 -73.940 1.00 78.45 N ANISOU 2483 N ILE A1266 9722 11412 8671 973 1415 518 N ATOM 2484 CA ILE A1266 -7.206 -25.250 -75.276 1.00 73.41 C ANISOU 2484 CA ILE A1266 9095 10921 7878 935 1449 557 C ATOM 2485 C ILE A1266 -6.293 -24.068 -75.572 1.00 74.14 C ANISOU 2485 C ILE A1266 8932 11227 8011 880 1482 801 C ATOM 2486 O ILE A1266 -5.877 -23.865 -76.719 1.00 74.56 O ANISOU 2486 O ILE A1266 8943 11478 7910 938 1590 880 O ATOM 2487 CB ILE A1266 -8.690 -24.865 -75.421 1.00 72.30 C ANISOU 2487 CB ILE A1266 9085 10659 7729 755 1303 465 C ATOM 2488 CG1 ILE A1266 -9.590 -26.015 -74.966 1.00 70.38 C ANISOU 2488 CG1 ILE A1266 9071 10202 7467 764 1259 235 C ATOM 2489 CG2 ILE A1266 -9.005 -24.488 -76.860 1.00 60.99 C ANISOU 2489 CG2 ILE A1266 7687 9388 6099 743 1339 491 C ATOM 2490 CD1 ILE A1266 -11.067 -25.680 -74.990 1.00 57.80 C ANISOU 2490 CD1 ILE A1266 7572 8518 5872 583 1109 148 C ATOM 2491 N GLN A1267 -5.958 -23.278 -74.549 1.00 77.33 N ANISOU 2491 N GLN A1267 9169 11599 8615 757 1393 923 N ATOM 2492 CA GLN A1267 -5.107 -22.111 -74.758 1.00 75.65 C ANISOU 2492 CA GLN A1267 8722 11565 8455 659 1413 1156 C ATOM 2493 C GLN A1267 -3.668 -22.517 -75.054 1.00 80.47 C ANISOU 2493 C GLN A1267 9159 12416 8998 827 1580 1263 C ATOM 2494 O GLN A1267 -3.015 -21.922 -75.919 1.00 82.02 O ANISOU 2494 O GLN A1267 9215 12834 9114 812 1671 1427 O ATOM 2495 CB GLN A1267 -5.169 -21.199 -73.532 1.00 74.15 C ANISOU 2495 CB GLN A1267 8428 11255 8489 468 1263 1230 C ATOM 2496 CG GLN A1267 -4.302 -19.957 -73.629 1.00 85.73 C ANISOU 2496 CG GLN A1267 9672 12871 10030 321 1267 1465 C ATOM 2497 CD GLN A1267 -4.385 -19.094 -72.385 1.00 99.71 C ANISOU 2497 CD GLN A1267 11376 14498 12012 126 1114 1509 C ATOM 2498 OE1 GLN A1267 -5.136 -19.393 -71.457 1.00106.13 O ANISOU 2498 OE1 GLN A1267 12304 15112 12910 112 1007 1367 O ATOM 2499 NE2 GLN A1267 -3.609 -18.016 -72.360 1.00104.31 N ANISOU 2499 NE2 GLN A1267 11778 15183 12672 -35 1106 1703 N ATOM 2500 N LEU A1268 -3.157 -23.529 -74.349 1.00 91.23 N ANISOU 2500 N LEU A1268 10523 13752 10388 997 1628 1184 N ATOM 2501 CA LEU A1268 -1.782 -23.967 -74.560 1.00 92.16 C ANISOU 2501 CA LEU A1268 10459 14118 10441 1192 1790 1289 C ATOM 2502 C LEU A1268 -1.601 -24.705 -75.879 1.00 94.70 C ANISOU 2502 C LEU A1268 10885 14574 10522 1409 1970 1232 C ATOM 2503 O LEU A1268 -0.485 -24.737 -76.408 1.00104.53 O ANISOU 2503 O LEU A1268 11946 16092 11678 1546 2123 1365 O ATOM 2504 CB LEU A1268 -1.330 -24.862 -73.406 1.00 81.11 C ANISOU 2504 CB LEU A1268 9045 12646 9130 1342 1788 1228 C ATOM 2505 CG LEU A1268 -1.276 -24.225 -72.017 1.00 84.52 C ANISOU 2505 CG LEU A1268 9344 12993 9777 1160 1625 1291 C ATOM 2506 CD1 LEU A1268 -0.843 -25.248 -70.978 1.00100.84 C ANISOU 2506 CD1 LEU A1268 11415 15006 11892 1347 1637 1231 C ATOM 2507 CD2 LEU A1268 -0.342 -23.026 -72.014 1.00 74.95 C ANISOU 2507 CD2 LEU A1268 7824 12017 8637 992 1613 1524 C ATOM 2508 N GLY A1269 -2.663 -25.295 -76.418 1.00 71.94 N ANISOU 2508 N GLY A1269 8286 11523 7524 1439 1957 1036 N ATOM 2509 CA GLY A1269 -2.569 -26.089 -77.622 1.00 79.81 C ANISOU 2509 CA GLY A1269 9428 12619 8278 1645 2118 940 C ATOM 2510 C GLY A1269 -2.611 -27.585 -77.410 1.00 85.39 C ANISOU 2510 C GLY A1269 10364 13169 8912 1887 2198 731 C ATOM 2511 O GLY A1269 -2.372 -28.332 -78.366 1.00 91.56 O ANISOU 2511 O GLY A1269 11276 14032 9483 2093 2353 643 O ATOM 2512 N ILE A1270 -2.898 -28.046 -76.191 1.00 79.68 N ANISOU 2512 N ILE A1270 9709 12216 8347 1871 2102 651 N ATOM 2513 CA ILE A1270 -2.995 -29.480 -75.943 1.00 84.30 C ANISOU 2513 CA ILE A1270 10548 12610 8873 2089 2175 458 C ATOM 2514 C ILE A1270 -4.202 -30.065 -76.663 1.00 89.44 C ANISOU 2514 C ILE A1270 11532 13071 9378 2033 2150 226 C ATOM 2515 O ILE A1270 -4.168 -31.216 -77.115 1.00 97.68 O ANISOU 2515 O ILE A1270 12818 14024 10271 2236 2270 61 O ATOM 2516 CB ILE A1270 -3.049 -29.755 -74.428 1.00 84.43 C ANISOU 2516 CB ILE A1270 10551 12433 9094 2063 2071 452 C ATOM 2517 CG1 ILE A1270 -1.932 -28.998 -73.707 1.00 87.70 C ANISOU 2517 CG1 ILE A1270 10608 13063 9650 2058 2059 687 C ATOM 2518 CG2 ILE A1270 -2.941 -31.246 -74.149 1.00 69.34 C ANISOU 2518 CG2 ILE A1270 8889 10333 7125 2322 2171 296 C ATOM 2519 CD1 ILE A1270 -0.539 -29.410 -74.132 1.00105.35 C ANISOU 2519 CD1 ILE A1270 12678 15568 11782 2349 2255 800 C ATOM 2520 N ILE A1271 -5.279 -29.292 -76.788 1.00 92.43 N ANISOU 2520 N ILE A1271 11934 13393 9792 1763 1994 207 N ATOM 2521 CA ILE A1271 -6.483 -29.716 -77.493 1.00100.21 C ANISOU 2521 CA ILE A1271 13193 14249 10634 1669 1945 3 C ATOM 2522 C ILE A1271 -6.967 -28.557 -78.354 1.00112.02 C ANISOU 2522 C ILE A1271 14582 15917 12062 1489 1874 99 C ATOM 2523 O ILE A1271 -7.072 -27.423 -77.876 1.00106.56 O ANISOU 2523 O ILE A1271 13693 15267 11528 1318 1762 260 O ATOM 2524 CB ILE A1271 -7.589 -30.176 -76.522 1.00 90.35 C ANISOU 2524 CB ILE A1271 12122 12701 9509 1519 1797 -149 C ATOM 2525 CG1 ILE A1271 -7.703 -29.208 -75.342 1.00 98.65 C ANISOU 2525 CG1 ILE A1271 12957 13722 10805 1348 1650 -2 C ATOM 2526 CG2 ILE A1271 -7.320 -31.593 -76.037 1.00 84.49 C ANISOU 2526 CG2 ILE A1271 11600 11751 8752 1713 1890 -296 C ATOM 2527 CD1 ILE A1271 -8.689 -29.650 -74.282 1.00105.51 C ANISOU 2527 CD1 ILE A1271 13969 14323 11796 1219 1521 -128 C ATOM 2528 N ARG A1272 -7.252 -28.841 -79.625 1.00126.79 N ANISOU 2528 N ARG A1272 16598 17886 13692 1534 1942 2 N ATOM 2529 CA ARG A1272 -7.706 -27.827 -80.569 1.00122.11 C ANISOU 2529 CA ARG A1272 15925 17476 12996 1394 1889 98 C ATOM 2530 C ARG A1272 -9.023 -28.199 -81.238 1.00127.88 C ANISOU 2530 C ARG A1272 16895 18131 13562 1278 1797 -104 C ATOM 2531 O ARG A1272 -9.418 -27.547 -82.211 1.00146.02 O ANISOU 2531 O ARG A1272 19165 20603 15715 1203 1769 -49 O ATOM 2532 CB ARG A1272 -6.634 -27.574 -81.633 1.00112.06 C ANISOU 2532 CB ARG A1272 14529 16498 11552 1556 2067 236 C ATOM 2533 N ASP A1273 -9.709 -29.226 -80.743 1.00111.97 N ANISOU 2533 N ASP A1273 15109 15873 11560 1253 1748 -329 N ATOM 2534 CA ASP A1273 -10.970 -29.646 -81.338 1.00101.16 C ANISOU 2534 CA ASP A1273 13960 14444 10032 1115 1652 -532 C ATOM 2535 C ASP A1273 -12.068 -28.640 -81.013 1.00 88.97 C ANISOU 2535 C ASP A1273 12299 12907 8599 869 1451 -455 C ATOM 2536 O ASP A1273 -12.215 -28.214 -79.864 1.00 99.70 O ANISOU 2536 O ASP A1273 13542 14143 10197 782 1360 -374 O ATOM 2537 CB ASP A1273 -11.351 -31.036 -80.827 1.00108.06 C ANISOU 2537 CB ASP A1273 15115 15039 10904 1134 1661 -782 C ATOM 2538 CG ASP A1273 -12.601 -31.585 -81.490 1.00129.13 C ANISOU 2538 CG ASP A1273 18023 17656 13387 970 1568 -1011 C ATOM 2539 OD1 ASP A1273 -13.039 -31.018 -82.514 1.00143.88 O ANISOU 2539 OD1 ASP A1273 19852 19736 15079 896 1524 -991 O ATOM 2540 OD2 ASP A1273 -13.147 -32.587 -80.983 1.00131.49 O ANISOU 2540 OD2 ASP A1273 18546 17706 13708 907 1537 -1206 O ATOM 2541 N CYS A1274 -12.838 -28.256 -82.033 1.00 81.36 N ANISOU 2541 N CYS A1274 11366 12099 7449 771 1385 -478 N ATOM 2542 CA CYS A1274 -13.973 -27.367 -81.828 1.00 81.10 C ANISOU 2542 CA CYS A1274 11236 12089 7489 567 1197 -414 C ATOM 2543 C CYS A1274 -15.172 -28.070 -81.207 1.00 75.48 C ANISOU 2543 C CYS A1274 10673 11189 6819 408 1066 -618 C ATOM 2544 O CYS A1274 -16.142 -27.397 -80.842 1.00 80.88 O ANISOU 2544 O CYS A1274 11262 11880 7587 251 911 -569 O ATOM 2545 CB CYS A1274 -14.395 -26.720 -83.151 1.00115.65 C ANISOU 2545 CB CYS A1274 15583 16722 11635 534 1167 -352 C ATOM 2546 SG CYS A1274 -13.333 -25.367 -83.715 1.00132.63 S ANISOU 2546 SG CYS A1274 17492 19108 13795 629 1261 -24 S ATOM 2547 N ARG A1275 -15.134 -29.398 -81.083 1.00 73.89 N ANISOU 2547 N ARG A1275 10702 10817 6555 445 1129 -837 N ATOM 2548 CA ARG A1275 -16.218 -30.114 -80.421 1.00 81.63 C ANISOU 2548 CA ARG A1275 11826 11604 7587 271 1015 -1019 C ATOM 2549 C ARG A1275 -16.086 -30.032 -78.905 1.00 84.84 C ANISOU 2549 C ARG A1275 12143 11810 8282 253 982 -946 C ATOM 2550 O ARG A1275 -17.069 -29.774 -78.202 1.00 82.54 O ANISOU 2550 O ARG A1275 11800 11459 8104 80 841 -954 O ATOM 2551 CB ARG A1275 -16.244 -31.573 -80.881 1.00 79.58 C ANISOU 2551 CB ARG A1275 11883 11208 7147 300 1097 -1283 C ATOM 2552 N ILE A1276 -14.875 -30.249 -78.384 1.00 89.51 N ANISOU 2552 N ILE A1276 12706 12320 8983 437 1111 -871 N ATOM 2553 CA ILE A1276 -14.652 -30.114 -76.950 1.00 97.88 C ANISOU 2553 CA ILE A1276 13667 13221 10302 432 1079 -786 C ATOM 2554 C ILE A1276 -14.656 -28.653 -76.522 1.00 96.95 C ANISOU 2554 C ILE A1276 13274 13221 10342 368 988 -566 C ATOM 2555 O ILE A1276 -14.920 -28.354 -75.353 1.00104.24 O ANISOU 2555 O ILE A1276 14115 14030 11461 293 906 -517 O ATOM 2556 CB ILE A1276 -13.340 -30.809 -76.536 1.00106.57 C ANISOU 2556 CB ILE A1276 14811 14227 11456 660 1239 -767 C ATOM 2557 CG1 ILE A1276 -12.165 -30.313 -77.382 1.00111.51 C ANISOU 2557 CG1 ILE A1276 15302 15076 11992 843 1370 -625 C ATOM 2558 CG2 ILE A1276 -13.481 -32.320 -76.649 1.00112.70 C ANISOU 2558 CG2 ILE A1276 15904 14798 12119 715 1316 -996 C ATOM 2559 CD1 ILE A1276 -11.366 -29.191 -76.747 1.00112.10 C ANISOU 2559 CD1 ILE A1276 15082 15256 12253 868 1360 -377 C ATOM 2560 N ALA A1277 -14.361 -27.730 -77.440 1.00 90.08 N ANISOU 2560 N ALA A1277 12274 12568 9385 396 1005 -429 N ATOM 2561 CA ALA A1277 -14.488 -26.313 -77.126 1.00 80.82 C ANISOU 2561 CA ALA A1277 10881 11479 8349 318 912 -227 C ATOM 2562 C ALA A1277 -15.944 -25.889 -76.998 1.00 83.75 C ANISOU 2562 C ALA A1277 11250 11843 8727 142 745 -270 C ATOM 2563 O ALA A1277 -16.231 -24.892 -76.326 1.00 86.79 O ANISOU 2563 O ALA A1277 11492 12211 9271 76 654 -142 O ATOM 2564 CB ALA A1277 -13.789 -25.469 -78.192 1.00 70.06 C ANISOU 2564 CB ALA A1277 9399 10340 6879 391 985 -56 C ATOM 2565 N ASP A1278 -16.865 -26.625 -77.623 1.00 84.18 N ANISOU 2565 N ASP A1278 11459 11919 8606 66 705 -448 N ATOM 2566 CA ASP A1278 -18.282 -26.305 -77.499 1.00 86.30 C ANISOU 2566 CA ASP A1278 11703 12217 8868 -101 545 -490 C ATOM 2567 C ASP A1278 -18.816 -26.710 -76.131 1.00 94.50 C ANISOU 2567 C ASP A1278 12761 13058 10089 -193 479 -564 C ATOM 2568 O ASP A1278 -19.522 -25.935 -75.475 1.00 88.59 O ANISOU 2568 O ASP A1278 11886 12312 9461 -272 369 -488 O ATOM 2569 CB ASP A1278 -19.071 -26.990 -78.616 1.00 82.42 C ANISOU 2569 CB ASP A1278 11358 11842 8117 -176 515 -660 C ATOM 2570 CG ASP A1278 -20.564 -26.756 -78.503 1.00 87.50 C ANISOU 2570 CG ASP A1278 11955 12555 8736 -354 347 -708 C ATOM 2571 OD1 ASP A1278 -20.997 -25.592 -78.638 1.00 89.38 O ANISOU 2571 OD1 ASP A1278 12026 12934 9002 -360 263 -548 O ATOM 2572 OD2 ASP A1278 -21.306 -27.736 -78.281 1.00 92.11 O ANISOU 2572 OD2 ASP A1278 12671 13055 9271 -487 302 -899 O ATOM 2573 N ILE A1279 -18.485 -27.923 -75.679 1.00105.17 N ANISOU 2573 N ILE A1279 14275 14230 11453 -171 552 -708 N ATOM 2574 CA ILE A1279 -18.946 -28.377 -74.373 1.00110.94 C ANISOU 2574 CA ILE A1279 15036 14771 12344 -257 502 -767 C ATOM 2575 C ILE A1279 -18.308 -27.571 -73.247 1.00 98.46 C ANISOU 2575 C ILE A1279 13290 13129 10992 -190 500 -600 C ATOM 2576 O ILE A1279 -18.875 -27.484 -72.152 1.00104.07 O ANISOU 2576 O ILE A1279 13960 13743 11840 -273 425 -602 O ATOM 2577 CB ILE A1279 -18.683 -29.887 -74.204 1.00114.73 C ANISOU 2577 CB ILE A1279 15760 15056 12776 -236 592 -946 C ATOM 2578 CG1 ILE A1279 -19.422 -30.434 -72.980 1.00123.04 C ANISOU 2578 CG1 ILE A1279 16867 15927 13956 -369 528 -1018 C ATOM 2579 CG2 ILE A1279 -17.194 -30.172 -74.097 1.00109.38 C ANISOU 2579 CG2 ILE A1279 15106 14312 12142 -15 744 -883 C ATOM 2580 CD1 ILE A1279 -20.921 -30.235 -73.032 1.00126.32 C ANISOU 2580 CD1 ILE A1279 17240 16432 14323 -590 384 -1079 C ATOM 2581 N VAL A1280 -17.146 -26.963 -73.491 1.00 84.96 N ANISOU 2581 N VAL A1280 11477 11487 9316 -52 579 -455 N ATOM 2582 CA VAL A1280 -16.553 -26.072 -72.500 1.00 73.10 C ANISOU 2582 CA VAL A1280 9808 9951 8017 -20 560 -296 C ATOM 2583 C VAL A1280 -17.244 -24.714 -72.516 1.00 85.58 C ANISOU 2583 C VAL A1280 11244 11623 9650 -105 445 -177 C ATOM 2584 O VAL A1280 -17.537 -24.142 -71.460 1.00 87.01 O ANISOU 2584 O VAL A1280 11344 11726 9990 -154 370 -127 O ATOM 2585 CB VAL A1280 -15.037 -25.945 -72.739 1.00 61.24 C ANISOU 2585 CB VAL A1280 8236 8504 6529 135 685 -180 C ATOM 2586 CG1 VAL A1280 -14.461 -24.797 -71.924 1.00 63.84 C ANISOU 2586 CG1 VAL A1280 8374 8840 7044 125 646 -1 C ATOM 2587 CG2 VAL A1280 -14.336 -27.248 -72.388 1.00 71.61 C ANISOU 2587 CG2 VAL A1280 9681 9697 7832 254 794 -280 C ATOM 2588 N ASP A1281 -17.525 -24.182 -73.708 1.00 83.15 N ANISOU 2588 N ASP A1281 10912 11480 9201 -109 434 -128 N ATOM 2589 CA ASP A1281 -18.197 -22.892 -73.810 1.00 78.94 C ANISOU 2589 CA ASP A1281 10260 11029 8704 -160 332 -2 C ATOM 2590 C ASP A1281 -19.659 -22.959 -73.386 1.00 76.62 C ANISOU 2590 C ASP A1281 9977 10724 8412 -269 208 -95 C ATOM 2591 O ASP A1281 -20.235 -21.923 -73.038 1.00 66.45 O ANISOU 2591 O ASP A1281 8588 9453 7205 -289 123 4 O ATOM 2592 CB ASP A1281 -18.090 -22.354 -75.238 1.00 75.08 C ANISOU 2592 CB ASP A1281 9750 10732 8045 -121 359 90 C ATOM 2593 CG ASP A1281 -16.749 -21.701 -75.517 1.00 90.93 C ANISOU 2593 CG ASP A1281 11673 12780 10096 -36 458 264 C ATOM 2594 OD1 ASP A1281 -16.266 -20.941 -74.652 1.00101.02 O ANISOU 2594 OD1 ASP A1281 12854 13968 11561 -46 442 381 O ATOM 2595 OD2 ASP A1281 -16.176 -21.949 -76.598 1.00101.82 O ANISOU 2595 OD2 ASP A1281 13080 14292 11314 32 552 283 O ATOM 2596 N THR A1282 -20.271 -24.142 -73.408 1.00 81.81 N ANISOU 2596 N THR A1282 10755 11352 8978 -339 201 -277 N ATOM 2597 CA THR A1282 -21.647 -24.284 -72.946 1.00 89.75 C ANISOU 2597 CA THR A1282 11749 12369 9985 -463 89 -362 C ATOM 2598 C THR A1282 -21.730 -24.501 -71.441 1.00 79.02 C ANISOU 2598 C THR A1282 10379 10834 8810 -496 73 -389 C ATOM 2599 O THR A1282 -22.665 -24.014 -70.796 1.00 70.35 O ANISOU 2599 O THR A1282 9196 9755 7778 -555 -18 -372 O ATOM 2600 CB THR A1282 -22.341 -25.445 -73.665 1.00 95.05 C ANISOU 2600 CB THR A1282 12556 13095 10464 -568 78 -547 C ATOM 2601 OG1 THR A1282 -21.541 -26.628 -73.558 1.00106.95 O ANISOU 2601 OG1 THR A1282 14232 14447 11958 -538 187 -663 O ATOM 2602 CG2 THR A1282 -22.564 -25.113 -75.128 1.00 99.84 C ANISOU 2602 CG2 THR A1282 13152 13921 10861 -554 59 -524 C ATOM 2603 N ALA A1283 -20.769 -25.226 -70.868 1.00 72.04 N ANISOU 2603 N ALA A1283 9577 9795 8000 -445 163 -424 N ATOM 2604 CA ALA A1283 -20.784 -25.516 -69.441 1.00 68.00 C ANISOU 2604 CA ALA A1283 9067 9125 7645 -468 152 -446 C ATOM 2605 C ALA A1283 -20.240 -24.375 -68.592 1.00 56.33 C ANISOU 2605 C ALA A1283 7453 7614 6337 -405 131 -299 C ATOM 2606 O ALA A1283 -20.447 -24.381 -67.374 1.00 70.83 O ANISOU 2606 O ALA A1283 9268 9352 8293 -432 98 -307 O ATOM 2607 CB ALA A1283 -19.987 -26.790 -69.155 1.00 65.45 C ANISOU 2607 CB ALA A1283 8897 8651 7321 -422 255 -534 C ATOM 2608 N MET A1284 -19.555 -23.399 -69.198 1.00 59.73 N ANISOU 2608 N MET A1284 7800 8121 6774 -333 148 -165 N ATOM 2609 CA MET A1284 -19.011 -22.296 -68.407 1.00 75.44 C ANISOU 2609 CA MET A1284 9680 10061 8923 -301 124 -34 C ATOM 2610 C MET A1284 -20.107 -21.427 -67.802 1.00 76.61 C ANISOU 2610 C MET A1284 9766 10207 9137 -349 17 -12 C ATOM 2611 O MET A1284 -20.007 -21.091 -66.608 1.00 69.88 O ANISOU 2611 O MET A1284 8880 9252 8418 -354 -12 2 O ATOM 2612 CB MET A1284 -18.031 -21.478 -69.253 1.00 92.78 C ANISOU 2612 CB MET A1284 11812 12336 11104 -240 173 111 C ATOM 2613 CG MET A1284 -17.106 -20.588 -68.437 1.00100.42 C ANISOU 2613 CG MET A1284 12688 13233 12233 -227 170 234 C ATOM 2614 SD MET A1284 -15.968 -21.536 -67.407 1.00 91.43 S ANISOU 2614 SD MET A1284 11555 12005 11179 -183 237 192 S ATOM 2615 CE MET A1284 -15.043 -22.425 -68.657 1.00 87.90 C ANISOU 2615 CE MET A1284 11149 11663 10584 -84 373 187 C ATOM 2616 N PRO A1285 -21.156 -21.022 -68.531 1.00 74.23 N ANISOU 2616 N PRO A1285 9441 10024 8740 -373 -43 -7 N ATOM 2617 CA PRO A1285 -22.244 -20.288 -67.863 1.00 83.06 C ANISOU 2617 CA PRO A1285 10494 11148 9916 -389 -134 8 C ATOM 2618 C PRO A1285 -22.976 -21.115 -66.821 1.00 80.18 C ANISOU 2618 C PRO A1285 10151 10732 9582 -459 -159 -117 C ATOM 2619 O PRO A1285 -23.532 -20.549 -65.873 1.00 77.30 O ANISOU 2619 O PRO A1285 9733 10333 9305 -452 -209 -103 O ATOM 2620 CB PRO A1285 -23.170 -19.895 -69.024 1.00 85.12 C ANISOU 2620 CB PRO A1285 10719 11588 10033 -384 -185 40 C ATOM 2621 CG PRO A1285 -22.302 -19.921 -70.226 1.00 80.96 C ANISOU 2621 CG PRO A1285 10226 11124 9412 -349 -120 97 C ATOM 2622 CD PRO A1285 -21.349 -21.049 -69.992 1.00 73.16 C ANISOU 2622 CD PRO A1285 9320 10043 8435 -363 -32 8 C ATOM 2623 N ILE A1286 -22.993 -22.441 -66.969 1.00 83.83 N ANISOU 2623 N ILE A1286 10702 11180 9968 -524 -118 -237 N ATOM 2624 CA ILE A1286 -23.654 -23.291 -65.983 1.00 83.56 C ANISOU 2624 CA ILE A1286 10702 11085 9961 -610 -132 -342 C ATOM 2625 C ILE A1286 -22.868 -23.309 -64.679 1.00 82.56 C ANISOU 2625 C ILE A1286 10587 10800 9982 -568 -100 -320 C ATOM 2626 O ILE A1286 -23.443 -23.199 -63.589 1.00 81.35 O ANISOU 2626 O ILE A1286 10399 10614 9896 -596 -137 -336 O ATOM 2627 CB ILE A1286 -23.848 -24.710 -66.548 1.00 83.47 C ANISOU 2627 CB ILE A1286 10818 11071 9826 -704 -93 -475 C ATOM 2628 CG1 ILE A1286 -24.781 -24.682 -67.760 1.00 83.64 C ANISOU 2628 CG1 ILE A1286 10815 11280 9683 -773 -147 -511 C ATOM 2629 CG2 ILE A1286 -24.387 -25.645 -65.476 1.00 84.28 C ANISOU 2629 CG2 ILE A1286 10978 11077 9967 -805 -92 -566 C ATOM 2630 CD1 ILE A1286 -26.187 -24.229 -67.436 1.00 89.48 C ANISOU 2630 CD1 ILE A1286 11430 12159 10409 -843 -244 -508 C ATOM 2631 N THR A1287 -21.542 -23.443 -64.766 1.00 80.90 N ANISOU 2631 N THR A1287 10414 10513 9811 -496 -32 -278 N ATOM 2632 CA THR A1287 -20.724 -23.521 -63.560 1.00 75.29 C ANISOU 2632 CA THR A1287 9703 9681 9222 -456 -9 -253 C ATOM 2633 C THR A1287 -20.682 -22.193 -62.815 1.00 71.57 C ANISOU 2633 C THR A1287 9132 9198 8862 -429 -71 -167 C ATOM 2634 O THR A1287 -20.575 -22.181 -61.583 1.00 86.59 O ANISOU 2634 O THR A1287 11027 11025 10849 -430 -88 -176 O ATOM 2635 CB THR A1287 -19.307 -23.971 -63.915 1.00 71.84 C ANISOU 2635 CB THR A1287 9303 9207 8785 -374 77 -219 C ATOM 2636 OG1 THR A1287 -18.733 -23.056 -64.857 1.00 77.69 O ANISOU 2636 OG1 THR A1287 9974 10034 9511 -330 86 -119 O ATOM 2637 CG2 THR A1287 -19.326 -25.368 -64.517 1.00 66.27 C ANISOU 2637 CG2 THR A1287 8739 8473 7970 -380 149 -323 C ATOM 2638 N ILE A1288 -20.758 -21.072 -63.535 1.00 66.42 N ANISOU 2638 N ILE A1288 8419 8611 8205 -405 -102 -84 N ATOM 2639 CA ILE A1288 -20.770 -19.770 -62.876 1.00 66.56 C ANISOU 2639 CA ILE A1288 8379 8587 8326 -381 -158 -11 C ATOM 2640 C ILE A1288 -22.056 -19.589 -62.078 1.00 68.61 C ANISOU 2640 C ILE A1288 8620 8854 8593 -396 -217 -68 C ATOM 2641 O ILE A1288 -22.048 -19.019 -60.980 1.00 72.15 O ANISOU 2641 O ILE A1288 9056 9229 9129 -380 -249 -64 O ATOM 2642 CB ILE A1288 -20.573 -18.647 -63.912 1.00 69.16 C ANISOU 2642 CB ILE A1288 8673 8963 8640 -348 -169 104 C ATOM 2643 CG1 ILE A1288 -19.186 -18.752 -64.549 1.00 75.56 C ANISOU 2643 CG1 ILE A1288 9480 9780 9451 -337 -100 177 C ATOM 2644 CG2 ILE A1288 -20.761 -17.279 -63.273 1.00 57.89 C ANISOU 2644 CG2 ILE A1288 7224 7460 7311 -324 -228 169 C ATOM 2645 CD1 ILE A1288 -18.923 -17.712 -65.615 1.00 84.19 C ANISOU 2645 CD1 ILE A1288 10545 10924 10519 -318 -97 307 C ATOM 2646 N CYS A1289 -23.177 -20.084 -62.606 1.00 71.91 N ANISOU 2646 N CYS A1289 9031 9380 8910 -431 -233 -124 N ATOM 2647 CA CYS A1289 -24.445 -20.018 -61.889 1.00 78.86 C ANISOU 2647 CA CYS A1289 9869 10312 9783 -448 -279 -173 C ATOM 2648 C CYS A1289 -24.472 -20.905 -60.652 1.00 83.08 C ANISOU 2648 C CYS A1289 10438 10775 10355 -500 -258 -250 C ATOM 2649 O CYS A1289 -25.403 -20.786 -59.849 1.00 97.85 O ANISOU 2649 O CYS A1289 12263 12685 12229 -509 -286 -281 O ATOM 2650 CB CYS A1289 -25.598 -20.402 -62.819 1.00 81.01 C ANISOU 2650 CB CYS A1289 10103 10754 9924 -497 -305 -208 C ATOM 2651 SG CYS A1289 -25.893 -19.235 -64.165 1.00 91.78 S ANISOU 2651 SG CYS A1289 11408 12243 11222 -412 -346 -99 S ATOM 2652 N ILE A1290 -23.491 -21.784 -60.483 1.00 77.51 N ANISOU 2652 N ILE A1290 9807 9977 9668 -522 -204 -273 N ATOM 2653 CA ILE A1290 -23.400 -22.648 -59.311 1.00 68.97 C ANISOU 2653 CA ILE A1290 8773 8816 8618 -557 -179 -324 C ATOM 2654 C ILE A1290 -22.414 -22.098 -58.291 1.00 76.59 C ANISOU 2654 C ILE A1290 9729 9687 9686 -494 -184 -278 C ATOM 2655 O ILE A1290 -22.712 -22.035 -57.098 1.00 99.46 O ANISOU 2655 O ILE A1290 12617 12557 12617 -495 -203 -298 O ATOM 2656 CB ILE A1290 -23.023 -24.085 -59.737 1.00 62.41 C ANISOU 2656 CB ILE A1290 8050 7935 7728 -606 -113 -380 C ATOM 2657 CG1 ILE A1290 -24.193 -24.750 -60.465 1.00 54.72 C ANISOU 2657 CG1 ILE A1290 7098 7050 6643 -717 -121 -455 C ATOM 2658 CG2 ILE A1290 -22.590 -24.908 -58.532 1.00 58.02 C ANISOU 2658 CG2 ILE A1290 7561 7267 7217 -608 -76 -398 C ATOM 2659 CD1 ILE A1290 -23.912 -26.170 -60.902 1.00 55.74 C ANISOU 2659 CD1 ILE A1290 7374 7100 6706 -779 -56 -529 C ATOM 2660 N ALA A1291 -21.230 -21.685 -58.748 1.00 75.11 N ANISOU 2660 N ALA A1291 9535 9466 9537 -446 -169 -213 N ATOM 2661 CA ALA A1291 -20.210 -21.189 -57.830 1.00 71.67 C ANISOU 2661 CA ALA A1291 9078 8964 9190 -412 -184 -169 C ATOM 2662 C ALA A1291 -20.617 -19.854 -57.219 1.00 69.07 C ANISOU 2662 C ALA A1291 8708 8618 8917 -401 -252 -153 C ATOM 2663 O ALA A1291 -20.542 -19.670 -55.999 1.00 89.16 O ANISOU 2663 O ALA A1291 11255 11119 11501 -398 -280 -176 O ATOM 2664 CB ALA A1291 -18.870 -21.064 -58.555 1.00 64.74 C ANISOU 2664 CB ALA A1291 8178 8087 8331 -382 -149 -94 C ATOM 2665 N TYR A1292 -21.057 -18.911 -58.052 1.00 64.65 N ANISOU 2665 N TYR A1292 8125 8087 8350 -384 -277 -113 N ATOM 2666 CA TYR A1292 -21.372 -17.571 -57.577 1.00 58.64 C ANISOU 2666 CA TYR A1292 7358 7279 7644 -351 -332 -92 C ATOM 2667 C TYR A1292 -22.747 -17.469 -56.932 1.00 67.87 C ANISOU 2667 C TYR A1292 8518 8489 8781 -319 -356 -155 C ATOM 2668 O TYR A1292 -23.020 -16.471 -56.257 1.00 71.97 O ANISOU 2668 O TYR A1292 9052 8954 9341 -270 -393 -159 O ATOM 2669 CB TYR A1292 -21.253 -16.570 -58.729 1.00 63.92 C ANISOU 2669 CB TYR A1292 8020 7948 8318 -328 -342 -2 C ATOM 2670 CG TYR A1292 -19.822 -16.337 -59.160 1.00 71.21 C ANISOU 2670 CG TYR A1292 8937 8832 9289 -365 -321 78 C ATOM 2671 CD1 TYR A1292 -19.194 -17.202 -60.047 1.00 63.64 C ANISOU 2671 CD1 TYR A1292 7959 7944 8279 -378 -262 103 C ATOM 2672 CD2 TYR A1292 -19.094 -15.262 -58.667 1.00 74.25 C ANISOU 2672 CD2 TYR A1292 9335 9115 9760 -393 -358 126 C ATOM 2673 CE1 TYR A1292 -17.885 -16.997 -60.438 1.00 66.67 C ANISOU 2673 CE1 TYR A1292 8310 8326 8697 -402 -233 187 C ATOM 2674 CE2 TYR A1292 -17.784 -15.049 -59.053 1.00 74.50 C ANISOU 2674 CE2 TYR A1292 9335 9141 9832 -450 -340 210 C ATOM 2675 CZ TYR A1292 -17.185 -15.920 -59.938 1.00 73.72 C ANISOU 2675 CZ TYR A1292 9190 9141 9680 -447 -274 247 C ATOM 2676 OH TYR A1292 -15.881 -15.713 -60.325 1.00 80.67 O ANISOU 2676 OH TYR A1292 10013 10047 10590 -493 -245 341 O ATOM 2677 N PHE A1293 -23.617 -18.464 -57.118 1.00 64.69 N ANISOU 2677 N PHE A1293 8095 8183 8301 -349 -333 -204 N ATOM 2678 CA PHE A1293 -24.861 -18.490 -56.357 1.00 74.91 C ANISOU 2678 CA PHE A1293 9355 9546 9561 -332 -346 -258 C ATOM 2679 C PHE A1293 -24.626 -19.000 -54.941 1.00 83.06 C ANISOU 2679 C PHE A1293 10415 10527 10615 -355 -335 -308 C ATOM 2680 O PHE A1293 -25.191 -18.463 -53.982 1.00 96.90 O ANISOU 2680 O PHE A1293 12157 12288 12374 -306 -353 -337 O ATOM 2681 CB PHE A1293 -25.904 -19.352 -57.069 1.00 72.04 C ANISOU 2681 CB PHE A1293 8947 9325 9100 -390 -332 -287 C ATOM 2682 CG PHE A1293 -27.180 -19.523 -56.294 1.00 77.02 C ANISOU 2682 CG PHE A1293 9514 10063 9686 -396 -336 -332 C ATOM 2683 CD1 PHE A1293 -28.091 -18.484 -56.195 1.00 85.06 C ANISOU 2683 CD1 PHE A1293 10462 11163 10692 -292 -367 -312 C ATOM 2684 CD2 PHE A1293 -27.472 -20.725 -55.669 1.00 74.09 C ANISOU 2684 CD2 PHE A1293 9156 9715 9280 -497 -302 -385 C ATOM 2685 CE1 PHE A1293 -29.267 -18.638 -55.483 1.00 84.82 C ANISOU 2685 CE1 PHE A1293 10351 11266 10611 -284 -362 -346 C ATOM 2686 CE2 PHE A1293 -28.646 -20.885 -54.956 1.00 79.09 C ANISOU 2686 CE2 PHE A1293 9715 10470 9865 -517 -299 -413 C ATOM 2687 CZ PHE A1293 -29.544 -19.840 -54.864 1.00 81.21 C ANISOU 2687 CZ PHE A1293 9889 10850 10117 -408 -327 -395 C ATOM 2688 N ASN A1294 -23.793 -20.033 -54.794 1.00 68.14 N ANISOU 2688 N ASN A1294 8569 8591 8731 -411 -300 -314 N ATOM 2689 CA ASN A1294 -23.451 -20.523 -53.464 1.00 66.77 C ANISOU 2689 CA ASN A1294 8426 8373 8571 -420 -292 -341 C ATOM 2690 C ASN A1294 -22.538 -19.552 -52.729 1.00 78.57 C ANISOU 2690 C ASN A1294 9931 9790 10133 -377 -335 -324 C ATOM 2691 O ASN A1294 -22.582 -19.475 -51.496 1.00 83.67 O ANISOU 2691 O ASN A1294 10590 10425 10776 -363 -351 -357 O ATOM 2692 CB ASN A1294 -22.792 -21.898 -53.565 1.00 61.18 C ANISOU 2692 CB ASN A1294 7772 7629 7844 -467 -240 -338 C ATOM 2693 CG ASN A1294 -23.732 -22.957 -54.104 1.00 71.45 C ANISOU 2693 CG ASN A1294 9095 8982 9073 -544 -199 -375 C ATOM 2694 OD1 ASN A1294 -24.949 -22.858 -53.952 1.00 77.60 O ANISOU 2694 OD1 ASN A1294 9827 9849 9809 -578 -210 -405 O ATOM 2695 ND2 ASN A1294 -23.171 -23.980 -54.737 1.00 86.21 N ANISOU 2695 ND2 ASN A1294 11036 10800 10920 -573 -151 -376 N ATOM 2696 N ASN A1295 -21.708 -18.806 -53.462 1.00 67.27 N ANISOU 2696 N ASN A1295 8495 8312 8752 -368 -356 -273 N ATOM 2697 CA ASN A1295 -20.819 -17.845 -52.819 1.00 61.40 C ANISOU 2697 CA ASN A1295 7763 7494 8072 -364 -405 -259 C ATOM 2698 C ASN A1295 -21.585 -16.643 -52.284 1.00 60.69 C ANISOU 2698 C ASN A1295 7702 7366 7993 -316 -448 -298 C ATOM 2699 O ASN A1295 -21.225 -16.100 -51.233 1.00 79.57 O ANISOU 2699 O ASN A1295 10127 9700 10404 -317 -489 -335 O ATOM 2700 CB ASN A1295 -19.734 -17.396 -53.797 1.00 63.77 C ANISOU 2700 CB ASN A1295 8045 7763 8421 -391 -408 -180 C ATOM 2701 CG ASN A1295 -18.681 -16.527 -53.140 1.00 88.27 C ANISOU 2701 CG ASN A1295 11152 10800 11588 -431 -463 -162 C ATOM 2702 OD1 ASN A1295 -17.747 -17.030 -52.516 1.00 94.02 O ANISOU 2702 OD1 ASN A1295 11851 11550 12321 -459 -470 -154 O ATOM 2703 ND2 ASN A1295 -18.826 -15.214 -53.278 1.00107.49 N ANISOU 2703 ND2 ASN A1295 13625 13152 14064 -437 -505 -151 N ATOM 2704 N CYS A1296 -22.638 -16.215 -52.983 1.00 71.70 N ANISOU 2704 N CYS A1296 9084 8794 9363 -264 -440 -292 N ATOM 2705 CA CYS A1296 -23.460 -15.111 -52.502 1.00 88.13 C ANISOU 2705 CA CYS A1296 11198 10844 11445 -178 -467 -326 C ATOM 2706 C CYS A1296 -24.320 -15.496 -51.306 1.00 81.64 C ANISOU 2706 C CYS A1296 10365 10091 10565 -140 -453 -404 C ATOM 2707 O CYS A1296 -24.851 -14.604 -50.636 1.00 87.74 O ANISOU 2707 O CYS A1296 11176 10830 11330 -53 -470 -448 O ATOM 2708 CB CYS A1296 -24.348 -14.583 -53.631 1.00 98.13 C ANISOU 2708 CB CYS A1296 12438 12157 12691 -107 -460 -278 C ATOM 2709 SG CYS A1296 -23.460 -13.644 -54.895 1.00107.54 S ANISOU 2709 SG CYS A1296 13669 13244 13946 -123 -478 -172 S ATOM 2710 N LEU A1297 -24.474 -16.788 -51.028 1.00 70.53 N ANISOU 2710 N LEU A1297 8917 8771 9111 -197 -417 -418 N ATOM 2711 CA LEU A1297 -25.169 -17.258 -49.839 1.00 66.48 C ANISOU 2711 CA LEU A1297 8392 8330 8537 -183 -395 -474 C ATOM 2712 C LEU A1297 -24.216 -17.609 -48.705 1.00 66.08 C ANISOU 2712 C LEU A1297 8389 8226 8491 -221 -410 -497 C ATOM 2713 O LEU A1297 -24.672 -18.023 -47.634 1.00 68.82 O ANISOU 2713 O LEU A1297 8736 8633 8779 -210 -390 -534 O ATOM 2714 CB LEU A1297 -26.038 -18.474 -50.179 1.00 58.87 C ANISOU 2714 CB LEU A1297 7364 7495 7509 -241 -344 -467 C ATOM 2715 CG LEU A1297 -27.212 -18.220 -51.126 1.00 71.89 C ANISOU 2715 CG LEU A1297 8934 9259 9121 -210 -337 -452 C ATOM 2716 CD1 LEU A1297 -27.943 -19.517 -51.440 1.00 63.97 C ANISOU 2716 CD1 LEU A1297 7875 8380 8052 -319 -297 -453 C ATOM 2717 CD2 LEU A1297 -28.163 -17.196 -50.527 1.00 70.18 C ANISOU 2717 CD2 LEU A1297 8686 9102 8877 -80 -343 -479 C ATOM 2718 N ASN A1298 -22.903 -17.454 -48.915 1.00 61.22 N ANISOU 2718 N ASN A1298 7801 7523 7935 -263 -444 -465 N ATOM 2719 CA ASN A1298 -21.947 -17.783 -47.858 1.00 67.43 C ANISOU 2719 CA ASN A1298 8612 8292 8716 -294 -469 -475 C ATOM 2720 C ASN A1298 -22.018 -16.815 -46.683 1.00 80.11 C ANISOU 2720 C ASN A1298 10271 9866 10301 -257 -518 -548 C ATOM 2721 O ASN A1298 -22.028 -17.283 -45.531 1.00 73.13 O ANISOU 2721 O ASN A1298 9399 9034 9354 -253 -518 -581 O ATOM 2722 CB ASN A1298 -20.534 -17.868 -48.443 1.00 57.52 C ANISOU 2722 CB ASN A1298 7341 6991 7522 -348 -492 -412 C ATOM 2723 CG ASN A1298 -20.052 -19.295 -48.596 1.00 69.88 C ANISOU 2723 CG ASN A1298 8885 8600 9066 -366 -442 -363 C ATOM 2724 OD1 ASN A1298 -20.803 -20.243 -48.367 1.00 75.39 O ANISOU 2724 OD1 ASN A1298 9596 9339 9711 -361 -391 -374 O ATOM 2725 ND2 ASN A1298 -18.795 -19.456 -48.986 1.00 85.88 N ANISOU 2725 ND2 ASN A1298 10882 10617 11131 -387 -452 -303 N ATOM 2726 N PRO A1299 -22.054 -15.489 -46.874 1.00 80.43 N ANISOU 2726 N PRO A1299 10361 9815 10382 -228 -560 -579 N ATOM 2727 CA PRO A1299 -22.192 -14.606 -45.703 1.00 75.94 C ANISOU 2727 CA PRO A1299 9874 9203 9778 -186 -601 -672 C ATOM 2728 C PRO A1299 -23.479 -14.828 -44.930 1.00 78.91 C ANISOU 2728 C PRO A1299 10245 9676 10061 -89 -550 -729 C ATOM 2729 O PRO A1299 -23.530 -14.533 -43.729 1.00 83.27 O ANISOU 2729 O PRO A1299 10853 10237 10547 -56 -569 -808 O ATOM 2730 CB PRO A1299 -22.137 -13.199 -46.316 1.00 80.51 C ANISOU 2730 CB PRO A1299 10530 9635 10424 -165 -636 -681 C ATOM 2731 CG PRO A1299 -21.413 -13.373 -47.598 1.00 78.92 C ANISOU 2731 CG PRO A1299 10277 9409 10300 -241 -636 -579 C ATOM 2732 CD PRO A1299 -21.844 -14.711 -48.109 1.00 82.60 C ANISOU 2732 CD PRO A1299 10644 10007 10732 -236 -572 -528 C ATOM 2733 N LEU A1300 -24.522 -15.343 -45.582 1.00 74.62 N ANISOU 2733 N LEU A1300 9628 9226 9498 -49 -487 -692 N ATOM 2734 CA LEU A1300 -25.779 -15.601 -44.889 1.00 70.54 C ANISOU 2734 CA LEU A1300 9074 8840 8889 31 -431 -731 C ATOM 2735 C LEU A1300 -25.729 -16.907 -44.105 1.00 76.92 C ANISOU 2735 C LEU A1300 9846 9751 9630 -38 -396 -713 C ATOM 2736 O LEU A1300 -26.259 -16.985 -42.991 1.00 81.18 O ANISOU 2736 O LEU A1300 10391 10374 10080 9 -369 -758 O ATOM 2737 CB LEU A1300 -26.933 -15.622 -45.892 1.00 72.14 C ANISOU 2737 CB LEU A1300 9190 9132 9088 82 -386 -691 C ATOM 2738 CG LEU A1300 -28.341 -15.760 -45.312 1.00 77.20 C ANISOU 2738 CG LEU A1300 9756 9944 9631 170 -325 -718 C ATOM 2739 CD1 LEU A1300 -28.648 -14.598 -44.381 1.00 83.75 C ANISOU 2739 CD1 LEU A1300 10665 10737 10419 322 -330 -803 C ATOM 2740 CD2 LEU A1300 -29.374 -15.848 -46.425 1.00 82.62 C ANISOU 2740 CD2 LEU A1300 10329 10751 10312 197 -297 -664 C ATOM 2741 N PHE A1301 -25.095 -17.939 -44.667 1.00 83.72 N ANISOU 2741 N PHE A1301 10681 10603 10527 -138 -388 -644 N ATOM 2742 CA PHE A1301 -25.023 -19.225 -43.979 1.00 86.33 C ANISOU 2742 CA PHE A1301 11003 11001 10799 -195 -348 -611 C ATOM 2743 C PHE A1301 -24.093 -19.158 -42.773 1.00 84.34 C ANISOU 2743 C PHE A1301 10807 10728 10511 -190 -392 -633 C ATOM 2744 O PHE A1301 -24.417 -19.688 -41.704 1.00 82.96 O ANISOU 2744 O PHE A1301 10640 10636 10245 -181 -362 -637 O ATOM 2745 CB PHE A1301 -24.567 -20.316 -44.948 1.00 92.41 C ANISOU 2745 CB PHE A1301 11758 11740 11614 -280 -322 -537 C ATOM 2746 CG PHE A1301 -25.559 -20.618 -46.035 1.00 94.16 C ANISOU 2746 CG PHE A1301 11925 12014 11839 -312 -279 -522 C ATOM 2747 CD1 PHE A1301 -25.158 -21.252 -47.200 1.00 98.12 C ANISOU 2747 CD1 PHE A1301 12430 12469 12384 -374 -267 -480 C ATOM 2748 CD2 PHE A1301 -26.894 -20.273 -45.893 1.00 93.65 C ANISOU 2748 CD2 PHE A1301 11797 12065 11720 -275 -252 -551 C ATOM 2749 CE1 PHE A1301 -26.067 -21.534 -48.202 1.00 93.97 C ANISOU 2749 CE1 PHE A1301 11854 12006 11842 -418 -240 -475 C ATOM 2750 CE2 PHE A1301 -27.808 -20.552 -46.893 1.00 89.82 C ANISOU 2750 CE2 PHE A1301 11239 11662 11225 -315 -225 -533 C ATOM 2751 CZ PHE A1301 -27.393 -21.184 -48.048 1.00 87.79 C ANISOU 2751 CZ PHE A1301 10996 11354 11008 -397 -225 -499 C ATOM 2752 N TYR A1302 -22.932 -18.515 -42.927 1.00 83.30 N ANISOU 2752 N TYR A1302 10707 10503 10441 -206 -466 -640 N ATOM 2753 CA TYR A1302 -22.015 -18.369 -41.801 1.00 73.09 C ANISOU 2753 CA TYR A1302 9453 9216 9104 -215 -528 -665 C ATOM 2754 C TYR A1302 -22.623 -17.530 -40.686 1.00 81.74 C ANISOU 2754 C TYR A1302 10605 10342 10112 -150 -544 -769 C ATOM 2755 O TYR A1302 -22.280 -17.714 -39.513 1.00 78.20 O ANISOU 2755 O TYR A1302 10185 9955 9574 -147 -571 -794 O ATOM 2756 CB TYR A1302 -20.698 -17.748 -42.268 1.00 63.94 C ANISOU 2756 CB TYR A1302 8297 7971 8027 -271 -609 -652 C ATOM 2757 CG TYR A1302 -19.697 -18.743 -42.810 1.00 81.04 C ANISOU 2757 CG TYR A1302 10406 10151 10234 -314 -601 -549 C ATOM 2758 CD1 TYR A1302 -18.774 -19.354 -41.971 1.00 79.58 C ANISOU 2758 CD1 TYR A1302 10205 10031 9999 -322 -634 -509 C ATOM 2759 CD2 TYR A1302 -19.669 -19.066 -44.160 1.00 92.75 C ANISOU 2759 CD2 TYR A1302 11854 11593 11793 -330 -558 -489 C ATOM 2760 CE1 TYR A1302 -17.855 -20.262 -42.460 1.00 74.51 C ANISOU 2760 CE1 TYR A1302 9514 9406 9390 -326 -617 -409 C ATOM 2761 CE2 TYR A1302 -18.753 -19.973 -44.659 1.00 83.44 C ANISOU 2761 CE2 TYR A1302 10637 10425 10641 -344 -538 -403 C ATOM 2762 CZ TYR A1302 -17.848 -20.568 -43.804 1.00 70.53 C ANISOU 2762 CZ TYR A1302 8987 8849 8964 -333 -564 -361 C ATOM 2763 OH TYR A1302 -16.934 -21.471 -44.295 1.00 55.46 O ANISOU 2763 OH TYR A1302 7040 6956 7077 -312 -535 -268 O ATOM 2764 N GLY A1303 -23.523 -16.606 -41.028 1.00 82.50 N ANISOU 2764 N GLY A1303 10721 10404 10221 -81 -526 -829 N ATOM 2765 CA GLY A1303 -24.157 -15.796 -40.003 1.00 74.48 C ANISOU 2765 CA GLY A1303 9772 9413 9114 12 -526 -936 C ATOM 2766 C GLY A1303 -25.114 -16.592 -39.137 1.00 68.19 C ANISOU 2766 C GLY A1303 8933 8782 8195 60 -446 -929 C ATOM 2767 O GLY A1303 -25.179 -16.389 -37.922 1.00 77.45 O ANISOU 2767 O GLY A1303 10158 10015 9255 105 -452 -997 O ATOM 2768 N PHE A1304 -25.864 -17.513 -39.745 1.00 68.22 N ANISOU 2768 N PHE A1304 8844 8868 8209 36 -369 -847 N ATOM 2769 CA PHE A1304 -26.829 -18.313 -39.001 1.00 75.64 C ANISOU 2769 CA PHE A1304 9731 9972 9036 51 -284 -822 C ATOM 2770 C PHE A1304 -26.175 -19.278 -38.021 1.00 71.39 C ANISOU 2770 C PHE A1304 9221 9479 8424 -8 -285 -774 C ATOM 2771 O PHE A1304 -26.880 -19.851 -37.183 1.00 78.79 O ANISOU 2771 O PHE A1304 10135 10550 9250 3 -216 -752 O ATOM 2772 CB PHE A1304 -27.729 -19.085 -39.968 1.00 81.44 C ANISOU 2772 CB PHE A1304 10362 10776 9804 -2 -213 -745 C ATOM 2773 CG PHE A1304 -28.720 -18.220 -40.694 1.00 95.91 C ANISOU 2773 CG PHE A1304 12136 12645 11660 87 -195 -779 C ATOM 2774 CD1 PHE A1304 -29.089 -16.987 -40.182 1.00 93.98 C ANISOU 2774 CD1 PHE A1304 11935 12399 11375 238 -203 -870 C ATOM 2775 CD2 PHE A1304 -29.284 -18.640 -41.888 1.00101.84 C ANISOU 2775 CD2 PHE A1304 12797 13433 12463 31 -170 -720 C ATOM 2776 CE1 PHE A1304 -30.000 -16.188 -40.846 1.00 90.31 C ANISOU 2776 CE1 PHE A1304 11420 11968 10926 353 -182 -886 C ATOM 2777 CE2 PHE A1304 -30.197 -17.845 -42.557 1.00100.20 C ANISOU 2777 CE2 PHE A1304 12522 13286 12265 130 -159 -736 C ATOM 2778 CZ PHE A1304 -30.555 -16.618 -42.034 1.00 95.18 C ANISOU 2778 CZ PHE A1304 11925 12646 11593 302 -162 -811 C ATOM 2779 N LEU A1305 -24.857 -19.478 -38.105 1.00 65.77 N ANISOU 2779 N LEU A1305 8549 8674 7765 -65 -358 -745 N ATOM 2780 CA LEU A1305 -24.175 -20.296 -37.108 1.00 65.52 C ANISOU 2780 CA LEU A1305 8545 8697 7651 -90 -369 -692 C ATOM 2781 C LEU A1305 -24.124 -19.600 -35.755 1.00 71.07 C ANISOU 2781 C LEU A1305 9305 9474 8224 -26 -408 -784 C ATOM 2782 O LEU A1305 -24.198 -20.263 -34.714 1.00 79.54 O ANISOU 2782 O LEU A1305 10390 10659 9173 -16 -379 -745 O ATOM 2783 CB LEU A1305 -22.763 -20.639 -37.584 1.00 52.47 C ANISOU 2783 CB LEU A1305 6897 6957 6082 -145 -438 -631 C ATOM 2784 CG LEU A1305 -22.669 -21.568 -38.796 1.00 50.34 C ANISOU 2784 CG LEU A1305 6594 6621 5914 -199 -389 -535 C ATOM 2785 CD1 LEU A1305 -21.221 -21.746 -39.226 1.00 48.01 C ANISOU 2785 CD1 LEU A1305 6292 6261 5689 -220 -452 -481 C ATOM 2786 CD2 LEU A1305 -23.309 -22.914 -38.486 1.00 45.04 C ANISOU 2786 CD2 LEU A1305 5929 6004 5180 -226 -293 -448 C ATOM 2787 N GLY A1306 -24.002 -18.273 -35.747 1.00 52.29 N ANISOU 2787 N GLY A1306 6978 7028 5862 17 -472 -906 N ATOM 2788 CA GLY A1306 -24.000 -17.530 -34.498 1.00 68.32 C ANISOU 2788 CA GLY A1306 9088 9112 7757 78 -510 -1021 C ATOM 2789 C GLY A1306 -25.408 -17.397 -33.949 1.00 77.41 C ANISOU 2789 C GLY A1306 10233 10382 8797 187 -407 -1066 C ATOM 2790 O GLY A1306 -26.335 -17.011 -34.669 1.00 66.99 O ANISOU 2790 O GLY A1306 8874 9046 7533 244 -348 -1081 O ATOM 2791 N LYS A1307 -25.572 -17.722 -32.664 1.00 83.91 N ANISOU 2791 N LYS A1307 11081 11349 9451 224 -382 -1079 N ATOM 2792 CA LYS A1307 -26.892 -17.652 -32.047 1.00 82.12 C ANISOU 2792 CA LYS A1307 10830 11273 9097 332 -271 -1111 C ATOM 2793 C LYS A1307 -27.383 -16.216 -31.923 1.00 79.65 C ANISOU 2793 C LYS A1307 10598 10909 8755 468 -277 -1276 C ATOM 2794 O LYS A1307 -28.588 -15.963 -32.034 1.00 70.60 O ANISOU 2794 O LYS A1307 9399 9850 7577 580 -179 -1293 O ATOM 2795 CB LYS A1307 -26.868 -18.325 -30.675 1.00 72.63 C ANISOU 2795 CB LYS A1307 9646 10244 7707 340 -241 -1077 C ATOM 2796 N LYS A1308 -26.473 -15.266 -31.694 1.00 82.61 N ANISOU 2796 N LYS A1308 11103 11145 9139 461 -391 -1397 N ATOM 2797 CA LYS A1308 -26.881 -13.870 -31.581 1.00 87.42 C ANISOU 2797 CA LYS A1308 11834 11657 9724 591 -397 -1563 C ATOM 2798 C LYS A1308 -27.253 -13.292 -32.941 1.00 87.93 C ANISOU 2798 C LYS A1308 11876 11573 9962 624 -384 -1545 C ATOM 2799 O LYS A1308 -28.190 -12.492 -33.045 1.00100.20 O ANISOU 2799 O LYS A1308 13463 13114 11494 788 -320 -1617 O ATOM 2800 CB LYS A1308 -25.768 -13.049 -30.930 1.00 93.09 C ANISOU 2800 CB LYS A1308 12717 12256 10396 536 -531 -1701 C ATOM 2801 N PHE A1309 -26.530 -13.683 -33.994 1.00 87.88 N ANISOU 2801 N PHE A1309 11810 11463 10117 486 -439 -1444 N ATOM 2802 CA PHE A1309 -26.872 -13.223 -35.337 1.00 73.64 C ANISOU 2802 CA PHE A1309 9974 9539 8465 512 -425 -1408 C ATOM 2803 C PHE A1309 -28.240 -13.740 -35.760 1.00 68.30 C ANISOU 2803 C PHE A1309 9155 9024 7773 602 -303 -1330 C ATOM 2804 O PHE A1309 -29.022 -13.014 -36.384 1.00 63.83 O ANISOU 2804 O PHE A1309 8582 8426 7246 727 -265 -1350 O ATOM 2805 CB PHE A1309 -25.796 -13.665 -36.332 1.00 75.33 C ANISOU 2805 CB PHE A1309 10144 9646 8831 344 -498 -1308 C ATOM 2806 CG PHE A1309 -25.984 -13.115 -37.721 1.00101.29 C ANISOU 2806 CG PHE A1309 13416 12803 12265 359 -497 -1270 C ATOM 2807 CD1 PHE A1309 -26.791 -13.767 -38.641 1.00103.71 C ANISOU 2807 CD1 PHE A1309 13587 13198 12619 374 -422 -1166 C ATOM 2808 CD2 PHE A1309 -25.343 -11.951 -38.110 1.00114.24 C ANISOU 2808 CD2 PHE A1309 15183 14237 13989 343 -574 -1334 C ATOM 2809 CE1 PHE A1309 -26.961 -13.265 -39.917 1.00105.89 C ANISOU 2809 CE1 PHE A1309 13847 13376 13011 393 -427 -1125 C ATOM 2810 CE2 PHE A1309 -25.509 -11.444 -39.386 1.00115.74 C ANISOU 2810 CE2 PHE A1309 15364 14309 14302 362 -569 -1282 C ATOM 2811 CZ PHE A1309 -26.319 -12.102 -40.290 1.00108.78 C ANISOU 2811 CZ PHE A1309 14340 13536 13456 397 -497 -1176 C ATOM 2812 N LYS A1310 -28.545 -14.997 -35.428 1.00 64.69 N ANISOU 2812 N LYS A1310 8580 8744 7253 535 -243 -1232 N ATOM 2813 CA LYS A1310 -29.859 -15.550 -35.737 1.00 58.23 C ANISOU 2813 CA LYS A1310 7612 8108 6404 582 -130 -1157 C ATOM 2814 C LYS A1310 -30.964 -14.806 -35.000 1.00 78.55 C ANISOU 2814 C LYS A1310 10189 10811 8845 784 -50 -1244 C ATOM 2815 O LYS A1310 -32.102 -14.748 -35.480 1.00 79.13 O ANISOU 2815 O LYS A1310 10139 11014 8914 874 29 -1207 O ATOM 2816 CB LYS A1310 -29.892 -17.038 -35.386 1.00 65.24 C ANISOU 2816 CB LYS A1310 8410 9136 7242 447 -82 -1039 C ATOM 2817 CG LYS A1310 -31.129 -17.773 -35.874 1.00 81.43 C ANISOU 2817 CG LYS A1310 10295 11363 9281 422 21 -943 C ATOM 2818 CD LYS A1310 -31.317 -19.089 -35.135 1.00 84.29 C ANISOU 2818 CD LYS A1310 10608 11870 9549 308 87 -845 C ATOM 2819 CE LYS A1310 -30.084 -19.970 -35.238 1.00 81.68 C ANISOU 2819 CE LYS A1310 10351 11401 9283 162 25 -776 C ATOM 2820 NZ LYS A1310 -30.259 -21.247 -34.494 1.00 87.15 N ANISOU 2820 NZ LYS A1310 11025 12207 9882 65 95 -667 N ATOM 2821 N ARG A1311 -30.650 -14.225 -33.840 1.00 89.94 N ANISOU 2821 N ARG A1311 11766 12238 10169 864 -69 -1364 N ATOM 2822 CA ARG A1311 -31.659 -13.506 -33.070 1.00 90.73 C ANISOU 2822 CA ARG A1311 11889 12461 10124 1081 17 -1460 C ATOM 2823 C ARG A1311 -32.029 -12.188 -33.742 1.00 83.14 C ANISOU 2823 C ARG A1311 11006 11352 9234 1256 11 -1544 C ATOM 2824 O ARG A1311 -33.214 -11.863 -33.881 1.00 90.74 O ANISOU 2824 O ARG A1311 11878 12452 10147 1440 109 -1538 O ATOM 2825 CB ARG A1311 -31.159 -13.265 -31.646 1.00 91.62 C ANISOU 2825 CB ARG A1311 12147 12590 10074 1112 -7 -1578 C ATOM 2826 N TYR A1312 -31.027 -11.414 -34.166 1.00 78.05 N ANISOU 2826 N TYR A1312 10525 10431 8700 1206 -100 -1611 N ATOM 2827 CA TYR A1312 -31.309 -10.141 -34.821 1.00 87.76 C ANISOU 2827 CA TYR A1312 11863 11480 10003 1367 -107 -1678 C ATOM 2828 C TYR A1312 -31.897 -10.338 -36.212 1.00 87.91 C ANISOU 2828 C TYR A1312 11722 11532 10148 1378 -78 -1542 C ATOM 2829 O TYR A1312 -32.697 -9.511 -36.667 1.00 82.69 O ANISOU 2829 O TYR A1312 11069 10852 9496 1583 -31 -1556 O ATOM 2830 CB TYR A1312 -30.040 -9.292 -34.907 1.00 84.68 C ANISOU 2830 CB TYR A1312 11694 10782 9698 1270 -234 -1773 C ATOM 2831 CG TYR A1312 -29.527 -8.794 -33.575 1.00 89.77 C ANISOU 2831 CG TYR A1312 12532 11372 10206 1283 -276 -1942 C ATOM 2832 CD1 TYR A1312 -30.166 -7.757 -32.907 1.00 83.44 C ANISOU 2832 CD1 TYR A1312 11894 10522 9288 1514 -222 -2097 C ATOM 2833 CD2 TYR A1312 -28.394 -9.348 -32.995 1.00 95.27 C ANISOU 2833 CD2 TYR A1312 13250 12072 10876 1073 -371 -1950 C ATOM 2834 CE1 TYR A1312 -29.697 -7.295 -31.692 1.00 87.73 C ANISOU 2834 CE1 TYR A1312 12630 11014 9687 1518 -265 -2269 C ATOM 2835 CE2 TYR A1312 -27.918 -8.892 -31.780 1.00 98.48 C ANISOU 2835 CE2 TYR A1312 13828 12452 11139 1072 -422 -2109 C ATOM 2836 CZ TYR A1312 -28.573 -7.866 -31.134 1.00 93.49 C ANISOU 2836 CZ TYR A1312 13369 11764 10387 1286 -371 -2275 C ATOM 2837 OH TYR A1312 -28.101 -7.409 -29.925 1.00 89.53 O ANISOU 2837 OH TYR A1312 13055 11237 9726 1278 -426 -2450 O ATOM 2838 N PHE A1313 -31.514 -11.415 -36.902 1.00 78.77 N ANISOU 2838 N PHE A1313 10426 10425 9077 1171 -107 -1412 N ATOM 2839 CA PHE A1313 -32.016 -11.645 -38.253 1.00 66.61 C ANISOU 2839 CA PHE A1313 8742 8924 7644 1158 -92 -1293 C ATOM 2840 C PHE A1313 -33.515 -11.918 -38.246 1.00 78.22 C ANISOU 2840 C PHE A1313 10022 10678 9021 1298 22 -1241 C ATOM 2841 O PHE A1313 -34.246 -11.421 -39.111 1.00100.70 O ANISOU 2841 O PHE A1313 12796 13559 11907 1428 45 -1198 O ATOM 2842 CB PHE A1313 -31.260 -12.804 -38.902 1.00 74.82 C ANISOU 2842 CB PHE A1313 9697 9956 8775 907 -140 -1184 C ATOM 2843 CG PHE A1313 -31.507 -12.941 -40.379 1.00 83.30 C ANISOU 2843 CG PHE A1313 10667 11022 9961 868 -149 -1082 C ATOM 2844 CD1 PHE A1313 -32.533 -13.742 -40.855 1.00 90.78 C ANISOU 2844 CD1 PHE A1313 11417 12198 10876 848 -83 -991 C ATOM 2845 CD2 PHE A1313 -30.709 -12.272 -41.292 1.00 82.53 C ANISOU 2845 CD2 PHE A1313 10667 10700 9989 837 -225 -1074 C ATOM 2846 CE1 PHE A1313 -32.760 -13.869 -42.213 1.00 93.06 C ANISOU 2846 CE1 PHE A1313 11613 12496 11248 806 -101 -907 C ATOM 2847 CE2 PHE A1313 -30.931 -12.395 -42.650 1.00 88.28 C ANISOU 2847 CE2 PHE A1313 11303 11437 10801 808 -232 -978 C ATOM 2848 CZ PHE A1313 -31.957 -13.195 -43.111 1.00 90.57 C ANISOU 2848 CZ PHE A1313 11402 11961 11049 796 -174 -900 C ATOM 2849 N LEU A1314 -33.993 -12.702 -37.277 1.00 73.43 N ANISOU 2849 N LEU A1314 9323 10294 8285 1274 94 -1232 N ATOM 2850 CA LEU A1314 -35.416 -13.003 -37.200 1.00 84.42 C ANISOU 2850 CA LEU A1314 10507 11991 9576 1384 207 -1174 C ATOM 2851 C LEU A1314 -36.231 -11.828 -36.676 1.00 91.22 C ANISOU 2851 C LEU A1314 11415 12908 10337 1698 276 -1268 C ATOM 2852 O LEU A1314 -37.447 -11.791 -36.891 1.00 98.53 O ANISOU 2852 O LEU A1314 12155 14081 11201 1843 363 -1212 O ATOM 2853 CB LEU A1314 -35.648 -14.234 -36.323 1.00 87.63 C ANISOU 2853 CB LEU A1314 10805 12617 9873 1240 270 -1119 C ATOM 2854 CG LEU A1314 -35.009 -15.535 -36.815 1.00 91.08 C ANISOU 2854 CG LEU A1314 11194 13017 10394 950 225 -1013 C ATOM 2855 CD1 LEU A1314 -35.348 -16.687 -35.882 1.00104.09 C ANISOU 2855 CD1 LEU A1314 12757 14870 11923 831 302 -948 C ATOM 2856 CD2 LEU A1314 -35.444 -15.846 -38.239 1.00 91.50 C ANISOU 2856 CD2 LEU A1314 11105 13106 10553 870 210 -919 C ATOM 2857 N GLN A1315 -35.596 -10.872 -35.994 1.00 87.30 N ANISOU 2857 N GLN A1315 11161 12193 9814 1810 241 -1411 N ATOM 2858 CA GLN A1315 -36.321 -9.688 -35.545 1.00 95.04 C ANISOU 2858 CA GLN A1315 12233 13178 10702 2132 311 -1516 C ATOM 2859 C GLN A1315 -36.624 -8.753 -36.709 1.00 99.14 C ANISOU 2859 C GLN A1315 12777 13559 11332 2294 291 -1487 C ATOM 2860 O GLN A1315 -37.683 -8.115 -36.739 1.00 97.80 O ANISOU 2860 O GLN A1315 12548 13518 11093 2579 379 -1490 O ATOM 2861 CB GLN A1315 -35.526 -8.957 -34.462 1.00105.49 C ANISOU 2861 CB GLN A1315 13839 14288 11953 2180 272 -1695 C ATOM 2862 CG GLN A1315 -35.489 -9.673 -33.122 1.00113.43 C ANISOU 2862 CG GLN A1315 14825 15484 12791 2115 317 -1735 C ATOM 2863 CD GLN A1315 -34.843 -8.837 -32.034 1.00126.81 C ANISOU 2863 CD GLN A1315 16800 16999 14383 2194 280 -1931 C ATOM 2864 OE1 GLN A1315 -34.433 -7.701 -32.269 1.00129.07 O ANISOU 2864 OE1 GLN A1315 17311 17000 14730 2288 223 -2044 O ATOM 2865 NE2 GLN A1315 -34.751 -9.397 -30.833 1.00130.71 N ANISOU 2865 NE2 GLN A1315 17294 17659 14712 2147 311 -1970 N ATOM 2866 N LEU A1316 -35.706 -8.655 -37.674 1.00103.61 N ANISOU 2866 N LEU A1316 13426 13875 12064 2130 182 -1449 N ATOM 2867 CA LEU A1316 -35.950 -7.821 -38.846 1.00 96.93 C ANISOU 2867 CA LEU A1316 12606 12900 11323 2267 161 -1396 C ATOM 2868 C LEU A1316 -37.086 -8.367 -39.700 1.00 98.53 C ANISOU 2868 C LEU A1316 12510 13410 11516 2317 217 -1246 C ATOM 2869 O LEU A1316 -37.843 -7.589 -40.292 1.00113.77 O ANISOU 2869 O LEU A1316 14409 15370 13448 2563 251 -1209 O ATOM 2870 CB LEU A1316 -34.676 -7.697 -39.682 1.00 87.14 C ANISOU 2870 CB LEU A1316 11503 11357 10251 2051 38 -1373 C ATOM 2871 CG LEU A1316 -33.722 -6.555 -39.329 1.00 85.02 C ANISOU 2871 CG LEU A1316 11556 10720 10027 2077 -28 -1505 C ATOM 2872 CD1 LEU A1316 -32.447 -6.652 -40.148 1.00 84.51 C ANISOU 2872 CD1 LEU A1316 11563 10426 10119 1816 -143 -1454 C ATOM 2873 CD2 LEU A1316 -34.402 -5.212 -39.552 1.00 82.21 C ANISOU 2873 CD2 LEU A1316 11344 10230 9662 2398 19 -1546 C ATOM 2874 N LEU A1317 -37.225 -9.691 -39.775 1.00 94.79 N ANISOU 2874 N LEU A1317 11823 13166 11028 2087 224 -1158 N ATOM 2875 CA LEU A1317 -38.279 -10.282 -40.589 1.00 98.46 C ANISOU 2875 CA LEU A1317 12000 13936 11476 2082 263 -1024 C ATOM 2876 C LEU A1317 -39.621 -10.301 -39.868 1.00112.51 C ANISOU 2876 C LEU A1317 13590 16067 13093 2286 388 -1016 C ATOM 2877 O LEU A1317 -40.669 -10.234 -40.520 1.00117.76 O ANISOU 2877 O LEU A1317 14036 16980 13727 2410 427 -923 O ATOM 2878 CB LEU A1317 -37.887 -11.701 -41.005 1.00 85.18 C ANISOU 2878 CB LEU A1317 10190 12331 9843 1735 222 -939 C ATOM 2879 CG LEU A1317 -36.586 -11.828 -41.801 1.00 76.54 C ANISOU 2879 CG LEU A1317 9242 10940 8901 1532 110 -928 C ATOM 2880 CD1 LEU A1317 -36.339 -13.273 -42.205 1.00 76.68 C ANISOU 2880 CD1 LEU A1317 9134 11052 8948 1229 90 -847 C ATOM 2881 CD2 LEU A1317 -36.610 -10.921 -43.022 1.00 77.05 C ANISOU 2881 CD2 LEU A1317 9343 10877 9056 1656 63 -885 C ATOM 2882 N LYS A1318 -39.613 -10.389 -38.542 1.00117.16 N ANISOU 2882 N LYS A1318 14243 16707 13567 2325 451 -1105 N ATOM 2883 CA LYS A1318 -40.851 -10.413 -37.769 1.00108.66 C ANISOU 2883 CA LYS A1318 12984 15983 12319 2523 585 -1097 C ATOM 2884 C LYS A1318 -41.499 -9.033 -37.724 1.00104.31 C ANISOU 2884 C LYS A1318 12507 15411 11715 2936 644 -1158 C ATOM 2885 O LYS A1318 -40.829 -8.029 -37.485 1.00 99.78 O ANISOU 2885 O LYS A1318 12231 14504 11176 3074 609 -1281 O ATOM 2886 CB LYS A1318 -40.587 -10.917 -36.348 1.00 90.08 C ANISOU 2886 CB LYS A1318 10696 13687 9843 2444 638 -1172 C TER 2887 LYS A1318 ATOM 2888 N GLN D 1 -24.882 -12.311 -20.106 1.00129.76 N ANISOU 2888 N GLN D 1 14555 16225 18524 44 -1049 -3636 N ATOM 2889 CA GLN D 1 -23.451 -12.045 -20.008 1.00130.17 C ANISOU 2889 CA GLN D 1 15033 16322 18105 84 -947 -3023 C ATOM 2890 C GLN D 1 -22.799 -12.883 -18.915 1.00126.46 C ANISOU 2890 C GLN D 1 14601 16396 17051 -111 -189 -2776 C ATOM 2891 O GLN D 1 -23.446 -13.265 -17.940 1.00136.37 O ANISOU 2891 O GLN D 1 15473 18050 18291 -331 216 -3191 O ATOM 2892 CB GLN D 1 -23.200 -10.558 -19.748 1.00134.64 C ANISOU 2892 CB GLN D 1 15388 16749 19019 277 -1451 -3300 C ATOM 2893 CG GLN D 1 -23.336 -9.685 -20.983 1.00138.43 C ANISOU 2893 CG GLN D 1 16186 16545 19868 417 -2359 -3239 C ATOM 2894 CD GLN D 1 -22.265 -9.976 -22.016 1.00143.18 C ANISOU 2894 CD GLN D 1 17547 16937 19919 267 -2397 -2430 C ATOM 2895 OE1 GLN D 1 -22.547 -10.071 -23.211 1.00154.23 O ANISOU 2895 OE1 GLN D 1 19344 17872 21384 199 -2848 -2242 O ATOM 2896 NE2 GLN D 1 -21.025 -10.117 -21.560 1.00134.11 N ANISOU 2896 NE2 GLN D 1 16578 16160 18218 187 -1928 -2004 N ATOM 2897 N VAL D 2 -21.512 -13.164 -19.088 1.00112.69 N ANISOU 2897 N VAL D 2 13334 14671 14810 -76 -39 -2140 N ATOM 2898 CA VAL D 2 -20.728 -13.936 -18.132 1.00102.40 C ANISOU 2898 CA VAL D 2 12172 13766 12969 -198 509 -1850 C ATOM 2899 C VAL D 2 -19.708 -12.980 -17.526 1.00 99.96 C ANISOU 2899 C VAL D 2 11789 13631 12561 -87 475 -1768 C ATOM 2900 O VAL D 2 -18.704 -12.637 -18.161 1.00 95.21 O ANISOU 2900 O VAL D 2 11480 12897 11799 42 287 -1392 O ATOM 2901 CB VAL D 2 -20.050 -15.144 -18.787 1.00 92.85 C ANISOU 2901 CB VAL D 2 11513 12443 11323 -183 666 -1287 C ATOM 2902 CG1 VAL D 2 -19.302 -15.962 -17.745 1.00 89.26 C ANISOU 2902 CG1 VAL D 2 11240 12298 10377 -275 1071 -1041 C ATOM 2903 CG2 VAL D 2 -21.080 -16.002 -19.508 1.00 94.26 C ANISOU 2903 CG2 VAL D 2 11799 12392 11624 -290 633 -1354 C ATOM 2904 N GLN D 3 -19.961 -12.546 -16.296 1.00 98.22 N ANISOU 2904 N GLN D 3 11167 13751 12401 -195 679 -2156 N ATOM 2905 CA GLN D 3 -19.093 -11.599 -15.616 1.00 98.42 C ANISOU 2905 CA GLN D 3 11084 13954 12358 -107 647 -2132 C ATOM 2906 C GLN D 3 -18.017 -12.329 -14.816 1.00 82.39 C ANISOU 2906 C GLN D 3 9330 12229 9747 -194 1060 -1706 C ATOM 2907 O GLN D 3 -18.167 -13.495 -14.442 1.00 76.97 O ANISOU 2907 O GLN D 3 8846 11656 8742 -390 1373 -1567 O ATOM 2908 CB GLN D 3 -19.908 -10.692 -14.694 1.00114.59 C ANISOU 2908 CB GLN D 3 12528 16213 14797 -165 618 -2847 C ATOM 2909 CG GLN D 3 -21.021 -9.935 -15.401 1.00126.91 C ANISOU 2909 CG GLN D 3 13748 17428 17044 -2 79 -3407 C ATOM 2910 CD GLN D 3 -21.864 -9.111 -14.447 1.00138.08 C ANISOU 2910 CD GLN D 3 14452 19105 18906 -17 54 -4285 C ATOM 2911 OE1 GLN D 3 -21.573 -9.031 -13.254 1.00138.26 O ANISOU 2911 OE1 GLN D 3 14266 19596 18672 -201 477 -4440 O ATOM 2912 NE2 GLN D 3 -22.917 -8.494 -14.970 1.00143.75 N ANISOU 2912 NE2 GLN D 3 14784 19522 20312 178 -480 -4923 N ATOM 2913 N LEU D 4 -16.920 -11.620 -14.558 1.00 72.56 N ANISOU 2913 N LEU D 4 8125 11077 8366 -63 985 -1504 N ATOM 2914 CA LEU D 4 -15.787 -12.160 -13.816 1.00 71.34 C ANISOU 2914 CA LEU D 4 8199 11174 7731 -75 1255 -1142 C ATOM 2915 C LEU D 4 -15.381 -11.160 -12.744 1.00 92.62 C ANISOU 2915 C LEU D 4 10622 14143 10424 -108 1296 -1322 C ATOM 2916 O LEU D 4 -14.962 -10.042 -13.063 1.00 90.20 O ANISOU 2916 O LEU D 4 10206 13762 10303 35 1013 -1353 O ATOM 2917 CB LEU D 4 -14.606 -12.457 -14.745 1.00 69.22 C ANISOU 2917 CB LEU D 4 8269 10787 7243 140 1136 -693 C ATOM 2918 CG LEU D 4 -14.839 -13.477 -15.862 1.00 71.54 C ANISOU 2918 CG LEU D 4 8859 10825 7499 191 1098 -512 C ATOM 2919 CD1 LEU D 4 -13.585 -13.641 -16.706 1.00 67.64 C ANISOU 2919 CD1 LEU D 4 8584 10338 6777 364 1027 -220 C ATOM 2920 CD2 LEU D 4 -15.279 -14.813 -15.287 1.00 70.06 C ANISOU 2920 CD2 LEU D 4 8870 10652 7099 65 1337 -454 C ATOM 2921 N GLN D 5 -15.504 -11.560 -11.482 1.00114.18 N ANISOU 2921 N GLN D 5 13305 17177 12902 -360 1619 -1428 N ATOM 2922 CA GLN D 5 -15.117 -10.729 -10.351 1.00113.66 C ANISOU 2922 CA GLN D 5 13009 17408 12769 -444 1709 -1601 C ATOM 2923 C GLN D 5 -13.746 -11.165 -9.850 1.00108.89 C ANISOU 2923 C GLN D 5 12747 16916 11711 -379 1776 -1116 C ATOM 2924 O GLN D 5 -13.512 -12.357 -9.627 1.00117.71 O ANISOU 2924 O GLN D 5 14238 18004 12482 -477 1884 -831 O ATOM 2925 CB GLN D 5 -16.147 -10.823 -9.224 1.00110.50 C ANISOU 2925 CB GLN D 5 12321 17331 12333 -868 2029 -2108 C ATOM 2926 N GLU D 6 -12.848 -10.201 -9.676 1.00 99.48 N ANISOU 2926 N GLU D 6 11440 15818 10539 -213 1646 -1050 N ATOM 2927 CA GLU D 6 -11.482 -10.465 -9.253 1.00100.01 C ANISOU 2927 CA GLU D 6 11737 16010 10253 -99 1651 -672 C ATOM 2928 C GLU D 6 -11.240 -9.904 -7.857 1.00 99.71 C ANISOU 2928 C GLU D 6 11567 16267 10050 -292 1783 -799 C ATOM 2929 O GLU D 6 -11.907 -8.966 -7.414 1.00100.87 O ANISOU 2929 O GLU D 6 11367 16538 10422 -427 1825 -1207 O ATOM 2930 CB GLU D 6 -10.478 -9.861 -10.240 1.00 98.56 C ANISOU 2930 CB GLU D 6 11544 15764 10139 181 1418 -479 C ATOM 2931 CG GLU D 6 -10.765 -10.189 -11.695 1.00108.96 C ANISOU 2931 CG GLU D 6 12977 16814 11607 286 1278 -411 C ATOM 2932 CD GLU D 6 -9.714 -9.630 -12.632 1.00107.79 C ANISOU 2932 CD GLU D 6 12861 16700 11394 390 1101 -250 C ATOM 2933 OE1 GLU D 6 -8.579 -9.386 -12.173 1.00110.60 O ANISOU 2933 OE1 GLU D 6 13171 17316 11537 449 1135 -143 O ATOM 2934 OE2 GLU D 6 -10.024 -9.431 -13.825 1.00102.49 O ANISOU 2934 OE2 GLU D 6 12274 15817 10851 352 923 -250 O ATOM 2935 N SER D 7 -10.265 -10.494 -7.170 1.00 90.47 N ANISOU 2935 N SER D 7 10676 15191 8507 -288 1799 -488 N ATOM 2936 CA SER D 7 -9.904 -10.082 -5.820 1.00 90.77 C ANISOU 2936 CA SER D 7 10688 15491 8310 -506 1898 -534 C ATOM 2937 C SER D 7 -8.558 -10.696 -5.468 1.00 91.98 C ANISOU 2937 C SER D 7 11169 15631 8150 -327 1729 -135 C ATOM 2938 O SER D 7 -8.109 -11.655 -6.103 1.00 90.38 O ANISOU 2938 O SER D 7 11225 15220 7896 -88 1567 100 O ATOM 2939 CB SER D 7 -10.968 -10.499 -4.798 1.00 93.10 C ANISOU 2939 CB SER D 7 11042 15939 8392 -1046 2173 -791 C ATOM 2940 OG SER D 7 -11.190 -11.898 -4.837 1.00 96.40 O ANISOU 2940 OG SER D 7 11933 16176 8521 -1228 2168 -544 O ATOM 2941 N GLY D 8 -7.919 -10.128 -4.446 1.00 91.11 N ANISOU 2941 N GLY D 8 11018 15733 7865 -419 1728 -117 N ATOM 2942 CA GLY D 8 -6.656 -10.627 -3.939 1.00 92.43 C ANISOU 2942 CA GLY D 8 11460 15890 7770 -254 1502 190 C ATOM 2943 C GLY D 8 -5.472 -9.712 -4.164 1.00 92.09 C ANISOU 2943 C GLY D 8 11125 16025 7840 68 1379 221 C ATOM 2944 O GLY D 8 -4.378 -10.017 -3.672 1.00110.65 O ANISOU 2944 O GLY D 8 13612 18414 10018 228 1170 394 O ATOM 2945 N GLY D 9 -5.647 -8.607 -4.885 1.00 77.31 N ANISOU 2945 N GLY D 9 8889 14245 6241 134 1443 46 N ATOM 2946 CA GLY D 9 -4.536 -7.719 -5.148 1.00 82.31 C ANISOU 2946 CA GLY D 9 9295 15070 6907 316 1327 82 C ATOM 2947 C GLY D 9 -4.103 -6.944 -3.918 1.00 91.68 C ANISOU 2947 C GLY D 9 10407 16477 7949 166 1340 60 C ATOM 2948 O GLY D 9 -4.815 -6.844 -2.918 1.00 92.22 O ANISOU 2948 O GLY D 9 10533 16580 7928 -124 1479 -61 O ATOM 2949 N GLY D 10 -2.903 -6.383 -4.002 1.00 88.66 N ANISOU 2949 N GLY D 10 9877 16294 7517 318 1215 138 N ATOM 2950 CA GLY D 10 -2.364 -5.606 -2.904 1.00 79.96 C ANISOU 2950 CA GLY D 10 8701 15403 6275 197 1199 137 C ATOM 2951 C GLY D 10 -0.895 -5.325 -3.113 1.00 88.62 C ANISOU 2951 C GLY D 10 9645 16739 7289 394 1044 230 C ATOM 2952 O GLY D 10 -0.243 -5.889 -3.998 1.00 89.44 O ANISOU 2952 O GLY D 10 9683 16885 7416 623 967 246 O ATOM 2953 N LEU D 11 -0.379 -4.432 -2.273 1.00100.98 N ANISOU 2953 N LEU D 11 11111 18504 8751 277 1016 228 N ATOM 2954 CA LEU D 11 1.021 -4.028 -2.307 1.00 97.03 C ANISOU 2954 CA LEU D 11 10417 18301 8151 392 886 269 C ATOM 2955 C LEU D 11 1.790 -4.802 -1.243 1.00 92.97 C ANISOU 2955 C LEU D 11 10043 17816 7465 538 717 377 C ATOM 2956 O LEU D 11 1.467 -4.718 -0.053 1.00 93.63 O ANISOU 2956 O LEU D 11 10334 17838 7403 341 721 446 O ATOM 2957 CB LEU D 11 1.156 -2.521 -2.088 1.00 97.84 C ANISOU 2957 CB LEU D 11 10362 18568 8244 159 886 212 C ATOM 2958 CG LEU D 11 2.552 -1.945 -1.829 1.00104.30 C ANISOU 2958 CG LEU D 11 10988 19742 8899 162 778 246 C ATOM 2959 CD1 LEU D 11 3.546 -2.383 -2.892 1.00102.01 C ANISOU 2959 CD1 LEU D 11 10483 19702 8573 308 746 179 C ATOM 2960 CD2 LEU D 11 2.486 -0.428 -1.761 1.00111.52 C ANISOU 2960 CD2 LEU D 11 11838 20727 9809 -122 732 205 C ATOM 2961 N VAL D 12 2.807 -5.549 -1.674 1.00 84.93 N ANISOU 2961 N VAL D 12 8915 16889 6467 865 527 341 N ATOM 2962 CA VAL D 12 3.622 -6.365 -0.787 1.00 81.60 C ANISOU 2962 CA VAL D 12 8643 16402 5957 1094 193 400 C ATOM 2963 C VAL D 12 5.088 -6.145 -1.140 1.00 91.08 C ANISOU 2963 C VAL D 12 9400 17989 7215 1359 38 191 C ATOM 2964 O VAL D 12 5.431 -5.747 -2.256 1.00 91.79 O ANISOU 2964 O VAL D 12 9121 18383 7374 1357 213 -9 O ATOM 2965 CB VAL D 12 3.252 -7.866 -0.878 1.00 83.63 C ANISOU 2965 CB VAL D 12 9263 16257 6255 1310 -37 457 C ATOM 2966 CG1 VAL D 12 3.743 -8.462 -2.189 1.00 84.31 C ANISOU 2966 CG1 VAL D 12 9053 16422 6558 1690 -89 218 C ATOM 2967 CG2 VAL D 12 3.794 -8.641 0.318 1.00 97.46 C ANISOU 2967 CG2 VAL D 12 11404 17763 7863 1411 -514 598 C ATOM 2968 N ALA D 13 5.956 -6.395 -0.162 1.00112.37 N ANISOU 2968 N ALA D 13 12143 20697 9854 1524 -307 208 N ATOM 2969 CA ALA D 13 7.387 -6.247 -0.368 1.00109.64 C ANISOU 2969 CA ALA D 13 11309 20756 9593 1796 -492 -82 C ATOM 2970 C ALA D 13 7.906 -7.322 -1.322 1.00 96.22 C ANISOU 2970 C ALA D 13 9348 19079 8131 2256 -682 -438 C ATOM 2971 O ALA D 13 7.197 -8.260 -1.700 1.00101.63 O ANISOU 2971 O ALA D 13 10324 19384 8906 2396 -747 -385 O ATOM 2972 CB ALA D 13 8.129 -6.313 0.966 1.00118.42 C ANISOU 2972 CB ALA D 13 12568 21799 10626 1895 -907 7 C ATOM 2973 N ALA D 14 9.170 -7.174 -1.712 1.00 99.02 N ANISOU 2973 N ALA D 14 9110 19925 8590 2473 -766 -868 N ATOM 2974 CA ALA D 14 9.784 -8.117 -2.637 1.00 99.32 C ANISOU 2974 CA ALA D 14 8750 20105 8883 2920 -927 -1380 C ATOM 2975 C ALA D 14 9.989 -9.470 -1.968 1.00106.45 C ANISOU 2975 C ALA D 14 9964 20456 10025 3488 -1627 -1432 C ATOM 2976 O ALA D 14 10.452 -9.555 -0.827 1.00129.67 O ANISOU 2976 O ALA D 14 13115 23188 12965 3621 -2095 -1309 O ATOM 2977 CB ALA D 14 11.118 -7.574 -3.145 1.00102.69 C ANISOU 2977 CB ALA D 14 8378 21301 9338 2937 -818 -1950 C ATOM 2978 N GLY D 15 9.642 -10.533 -2.688 1.00105.38 N ANISOU 2978 N GLY D 15 9920 20038 10082 3798 -1764 -1605 N ATOM 2979 CA GLY D 15 9.766 -11.880 -2.175 1.00109.99 C ANISOU 2979 CA GLY D 15 10901 19992 10897 4325 -2533 -1653 C ATOM 2980 C GLY D 15 8.595 -12.370 -1.355 1.00108.18 C ANISOU 2980 C GLY D 15 11631 19030 10444 4058 -2725 -997 C ATOM 2981 O GLY D 15 8.683 -13.457 -0.772 1.00112.83 O ANISOU 2981 O GLY D 15 12733 19006 11132 4373 -3471 -936 O ATOM 2982 N GLY D 16 7.503 -11.612 -1.293 1.00102.39 N ANISOU 2982 N GLY D 16 11163 18337 9405 3453 -2122 -556 N ATOM 2983 CA GLY D 16 6.352 -11.996 -0.500 1.00111.13 C ANISOU 2983 CA GLY D 16 13089 18890 10243 3072 -2193 -33 C ATOM 2984 C GLY D 16 5.479 -13.045 -1.157 1.00112.88 C ANISOU 2984 C GLY D 16 13677 18689 10523 3139 -2243 24 C ATOM 2985 O GLY D 16 5.981 -13.938 -1.847 1.00104.65 O ANISOU 2985 O GLY D 16 12472 17516 9773 3666 -2607 -319 O ATOM 2986 N SER D 17 4.168 -12.948 -0.949 1.00115.67 N ANISOU 2986 N SER D 17 14486 18849 10613 2607 -1883 393 N ATOM 2987 CA SER D 17 3.237 -13.923 -1.498 1.00119.61 C ANISOU 2987 CA SER D 17 15382 18945 11118 2578 -1907 487 C ATOM 2988 C SER D 17 1.841 -13.320 -1.537 1.00111.90 C ANISOU 2988 C SER D 17 14535 18056 9926 1966 -1262 715 C ATOM 2989 O SER D 17 1.478 -12.503 -0.687 1.00125.38 O ANISOU 2989 O SER D 17 16317 19924 11398 1510 -1005 874 O ATOM 2990 CB SER D 17 3.234 -15.218 -0.678 1.00135.96 C ANISOU 2990 CB SER D 17 18267 20334 13058 2627 -2686 706 C ATOM 2991 OG SER D 17 2.255 -16.124 -1.155 1.00147.71 O ANISOU 2991 OG SER D 17 20201 21432 14490 2497 -2690 836 O ATOM 2992 N LEU D 18 1.066 -13.737 -2.536 1.00100.69 N ANISOU 2992 N LEU D 18 13107 16534 8617 1981 -1030 665 N ATOM 2993 CA LEU D 18 -0.319 -13.312 -2.679 1.00 87.99 C ANISOU 2993 CA LEU D 18 11585 14960 6888 1473 -503 786 C ATOM 2994 C LEU D 18 -1.124 -14.461 -3.270 1.00 88.90 C ANISOU 2994 C LEU D 18 12080 14680 7020 1478 -596 848 C ATOM 2995 O LEU D 18 -0.571 -15.457 -3.744 1.00 91.71 O ANISOU 2995 O LEU D 18 12555 14767 7525 1924 -1026 764 O ATOM 2996 CB LEU D 18 -0.441 -12.060 -3.555 1.00 83.45 C ANISOU 2996 CB LEU D 18 10388 14824 6496 1445 5 597 C ATOM 2997 CG LEU D 18 -0.036 -10.715 -2.950 1.00 81.92 C ANISOU 2997 CG LEU D 18 9883 15005 6240 1261 191 572 C ATOM 2998 CD1 LEU D 18 -0.124 -9.613 -3.994 1.00 85.15 C ANISOU 2998 CD1 LEU D 18 9809 15724 6819 1226 532 405 C ATOM 2999 CD2 LEU D 18 -0.909 -10.389 -1.752 1.00 82.06 C ANISOU 2999 CD2 LEU D 18 10209 14964 6006 747 341 716 C ATOM 3000 N ARG D 19 -2.446 -14.310 -3.238 1.00 86.97 N ANISOU 3000 N ARG D 19 11989 14410 6643 984 -207 933 N ATOM 3001 CA ARG D 19 -3.359 -15.304 -3.798 1.00 87.58 C ANISOU 3001 CA ARG D 19 12413 14154 6708 889 -221 994 C ATOM 3002 C ARG D 19 -4.506 -14.566 -4.474 1.00 91.11 C ANISOU 3002 C ARG D 19 12512 14819 7285 622 345 857 C ATOM 3003 O ARG D 19 -5.381 -14.020 -3.795 1.00 90.56 O ANISOU 3003 O ARG D 19 12452 14898 7061 113 653 827 O ATOM 3004 CB ARG D 19 -3.881 -16.254 -2.719 1.00 91.99 C ANISOU 3004 CB ARG D 19 13767 14337 6849 405 -517 1263 C ATOM 3005 CG ARG D 19 -4.764 -17.373 -3.250 1.00 93.37 C ANISOU 3005 CG ARG D 19 14379 14136 6960 261 -599 1350 C ATOM 3006 CD ARG D 19 -5.248 -18.275 -2.125 1.00112.42 C ANISOU 3006 CD ARG D 19 17679 16190 8845 -383 -926 1644 C ATOM 3007 NE ARG D 19 -6.045 -19.394 -2.621 1.00123.34 N ANISOU 3007 NE ARG D 19 19547 17188 10128 -561 -1060 1749 N ATOM 3008 CZ ARG D 19 -5.549 -20.588 -2.928 1.00134.78 C ANISOU 3008 CZ ARG D 19 21507 18075 11626 -182 -1749 1879 C ATOM 3009 NH1 ARG D 19 -4.252 -20.825 -2.789 1.00143.87 N ANISOU 3009 NH1 ARG D 19 22693 19001 12970 435 -2382 1855 N ATOM 3010 NH2 ARG D 19 -6.349 -21.547 -3.373 1.00134.47 N ANISOU 3010 NH2 ARG D 19 21925 17694 11473 -401 -1846 1982 N ATOM 3011 N LEU D 20 -4.500 -14.550 -5.804 1.00 90.47 N ANISOU 3011 N LEU D 20 12117 14761 7496 950 445 716 N ATOM 3012 CA LEU D 20 -5.546 -13.896 -6.576 1.00 77.95 C ANISOU 3012 CA LEU D 20 10249 13282 6084 756 837 583 C ATOM 3013 C LEU D 20 -6.691 -14.865 -6.832 1.00 78.87 C ANISOU 3013 C LEU D 20 10722 13097 6147 531 874 637 C ATOM 3014 O LEU D 20 -6.470 -16.028 -7.182 1.00 80.83 O ANISOU 3014 O LEU D 20 11312 13041 6360 743 591 744 O ATOM 3015 CB LEU D 20 -4.992 -13.379 -7.904 1.00 75.62 C ANISOU 3015 CB LEU D 20 9535 13148 6050 1094 892 434 C ATOM 3016 CG LEU D 20 -3.790 -12.436 -7.827 1.00 82.82 C ANISOU 3016 CG LEU D 20 10077 14412 6978 1256 868 349 C ATOM 3017 CD1 LEU D 20 -3.331 -12.038 -9.221 1.00 77.63 C ANISOU 3017 CD1 LEU D 20 9093 13941 6460 1406 946 187 C ATOM 3018 CD2 LEU D 20 -4.123 -11.206 -7.000 1.00 95.18 C ANISOU 3018 CD2 LEU D 20 11491 16169 8503 937 1041 341 C ATOM 3019 N SER D 21 -7.917 -14.379 -6.657 1.00 87.74 N ANISOU 3019 N SER D 21 11737 14313 7286 108 1196 506 N ATOM 3020 CA SER D 21 -9.115 -15.178 -6.863 1.00100.84 C ANISOU 3020 CA SER D 21 13657 15773 8886 -201 1296 492 C ATOM 3021 C SER D 21 -9.950 -14.583 -7.988 1.00 93.72 C ANISOU 3021 C SER D 21 12354 14903 8353 -135 1505 260 C ATOM 3022 O SER D 21 -9.907 -13.376 -8.245 1.00 96.07 O ANISOU 3022 O SER D 21 12218 15390 8894 -47 1596 76 O ATOM 3023 CB SER D 21 -9.956 -15.263 -5.582 1.00111.72 C ANISOU 3023 CB SER D 21 15254 17276 9919 -876 1487 431 C ATOM 3024 OG SER D 21 -9.221 -15.857 -4.527 1.00138.64 O ANISOU 3024 OG SER D 21 19172 20580 12925 -1028 1204 698 O ATOM 3025 N CYS D 22 -10.711 -15.446 -8.660 1.00 88.42 N ANISOU 3025 N CYS D 22 11888 13992 7717 -195 1505 280 N ATOM 3026 CA CYS D 22 -11.591 -15.005 -9.740 1.00 87.10 C ANISOU 3026 CA CYS D 22 11414 13782 7898 -156 1625 68 C ATOM 3027 C CYS D 22 -12.687 -16.047 -9.913 1.00 81.28 C ANISOU 3027 C CYS D 22 10959 12846 7077 -446 1691 59 C ATOM 3028 O CYS D 22 -12.414 -17.157 -10.381 1.00 78.36 O ANISOU 3028 O CYS D 22 10987 12197 6590 -292 1505 293 O ATOM 3029 CB CYS D 22 -10.813 -14.809 -11.035 1.00 96.45 C ANISOU 3029 CB CYS D 22 12482 14877 9288 296 1466 145 C ATOM 3030 SG CYS D 22 -11.861 -14.433 -12.459 1.00116.15 S ANISOU 3030 SG CYS D 22 14786 17197 12149 294 1477 -31 S ATOM 3031 N ALA D 23 -13.913 -15.690 -9.544 1.00 84.33 N ANISOU 3031 N ALA D 23 11111 13393 7539 -865 1936 -269 N ATOM 3032 CA ALA D 23 -15.067 -16.567 -9.678 1.00 87.47 C ANISOU 3032 CA ALA D 23 11693 13691 7850 -1241 2054 -361 C ATOM 3033 C ALA D 23 -15.967 -16.068 -10.799 1.00 95.92 C ANISOU 3033 C ALA D 23 12358 14682 9405 -1089 2070 -662 C ATOM 3034 O ALA D 23 -16.199 -14.862 -10.933 1.00 98.49 O ANISOU 3034 O ALA D 23 12188 15136 10098 -966 2066 -991 O ATOM 3035 CB ALA D 23 -15.856 -16.645 -8.369 1.00 93.84 C ANISOU 3035 CB ALA D 23 12508 14822 8324 -1955 2347 -620 C ATOM 3036 N ALA D 24 -16.471 -17.000 -11.603 1.00 96.44 N ANISOU 3036 N ALA D 24 12682 14483 9479 -1096 2010 -548 N ATOM 3037 CA ALA D 24 -17.336 -16.669 -12.725 1.00 95.92 C ANISOU 3037 CA ALA D 24 12322 14270 9853 -966 1953 -792 C ATOM 3038 C ALA D 24 -18.792 -16.633 -12.281 1.00 95.42 C ANISOU 3038 C ALA D 24 11939 14420 9895 -1449 2189 -1299 C ATOM 3039 O ALA D 24 -19.253 -17.512 -11.546 1.00 87.12 O ANISOU 3039 O ALA D 24 11147 13508 8448 -1967 2405 -1301 O ATOM 3040 CB ALA D 24 -17.161 -17.679 -13.859 1.00100.89 C ANISOU 3040 CB ALA D 24 13358 14528 10447 -737 1779 -461 C ATOM 3041 N SER D 25 -19.512 -15.610 -12.734 1.00100.72 N ANISOU 3041 N SER D 25 12056 15117 11097 -1314 2101 -1773 N ATOM 3042 CA SER D 25 -20.917 -15.433 -12.404 1.00 98.53 C ANISOU 3042 CA SER D 25 11293 15088 11056 -1688 2285 -2444 C ATOM 3043 C SER D 25 -21.705 -15.116 -13.667 1.00 90.77 C ANISOU 3043 C SER D 25 10058 13784 10648 -1399 1970 -2691 C ATOM 3044 O SER D 25 -21.172 -14.549 -14.626 1.00 80.31 O ANISOU 3044 O SER D 25 8821 12103 9590 -945 1587 -2455 O ATOM 3045 CB SER D 25 -21.116 -14.316 -11.370 1.00 94.98 C ANISOU 3045 CB SER D 25 10267 15051 10769 -1821 2423 -3025 C ATOM 3046 OG SER D 25 -22.488 -14.143 -11.062 1.00108.13 O ANISOU 3046 OG SER D 25 11343 17034 12707 -2175 2613 -3836 O ATOM 3047 N GLY D 26 -22.982 -15.488 -13.657 1.00 89.38 N ANISOU 3047 N GLY D 26 9588 13748 10623 -1733 2117 -3187 N ATOM 3048 CA GLY D 26 -23.856 -15.229 -14.783 1.00 94.14 C ANISOU 3048 CA GLY D 26 9929 14039 11802 -1490 1772 -3494 C ATOM 3049 C GLY D 26 -23.825 -16.266 -15.880 1.00108.54 C ANISOU 3049 C GLY D 26 12299 15460 13481 -1415 1653 -2965 C ATOM 3050 O GLY D 26 -24.244 -15.967 -17.004 1.00109.60 O ANISOU 3050 O GLY D 26 12368 15215 14059 -1130 1257 -3040 O ATOM 3051 N ASN D 27 -23.346 -17.473 -15.597 1.00113.77 N ANISOU 3051 N ASN D 27 13536 16149 13541 -1667 1916 -2448 N ATOM 3052 CA ASN D 27 -23.268 -18.542 -16.581 1.00115.39 C ANISOU 3052 CA ASN D 27 14284 15972 13586 -1586 1800 -1973 C ATOM 3053 C ASN D 27 -24.195 -19.683 -16.183 1.00120.08 C ANISOU 3053 C ASN D 27 15031 16726 13866 -2172 2088 -2090 C ATOM 3054 O ASN D 27 -24.276 -20.051 -15.007 1.00120.29 O ANISOU 3054 O ASN D 27 15126 17122 13456 -2697 2415 -2177 O ATOM 3055 CB ASN D 27 -21.833 -19.059 -16.719 1.00113.29 C ANISOU 3055 CB ASN D 27 14621 15509 12917 -1313 1729 -1289 C ATOM 3056 CG ASN D 27 -21.272 -19.578 -15.410 1.00115.50 C ANISOU 3056 CG ASN D 27 15177 16047 12660 -1626 1973 -1106 C ATOM 3057 OD1 ASN D 27 -21.578 -19.054 -14.339 1.00116.56 O ANISOU 3057 OD1 ASN D 27 14978 16571 12739 -1954 2200 -1457 O ATOM 3058 ND2 ASN D 27 -20.448 -20.616 -15.490 1.00113.56 N ANISOU 3058 ND2 ASN D 27 15559 15566 12022 -1533 1874 -592 N ATOM 3059 N ILE D 28 -24.896 -20.238 -17.172 1.00115.70 N ANISOU 3059 N ILE D 28 14576 15896 13489 -2155 1951 -2085 N ATOM 3060 CA ILE D 28 -25.783 -21.364 -16.904 1.00113.26 C ANISOU 3060 CA ILE D 28 14466 15714 12852 -2758 2198 -2167 C ATOM 3061 C ILE D 28 -25.004 -22.675 -16.884 1.00117.40 C ANISOU 3061 C ILE D 28 15879 15960 12768 -2848 2169 -1452 C ATOM 3062 O ILE D 28 -25.355 -23.600 -16.142 1.00129.78 O ANISOU 3062 O ILE D 28 17813 17681 13817 -3489 2373 -1389 O ATOM 3063 CB ILE D 28 -26.923 -21.400 -17.936 1.00109.96 C ANISOU 3063 CB ILE D 28 13754 15120 12907 -2714 2033 -2513 C ATOM 3064 CG1 ILE D 28 -27.627 -20.044 -17.999 1.00112.19 C ANISOU 3064 CG1 ILE D 28 13164 15566 13898 -2501 1876 -3277 C ATOM 3065 CG2 ILE D 28 -27.924 -22.495 -17.598 1.00110.62 C ANISOU 3065 CG2 ILE D 28 13968 15423 12640 -3433 2328 -2682 C ATOM 3066 CD1 ILE D 28 -28.771 -19.994 -18.988 1.00112.39 C ANISOU 3066 CD1 ILE D 28 12856 15377 14470 -2415 1599 -3692 C ATOM 3067 N PHE D 29 -23.941 -22.776 -17.675 1.00107.42 N ANISOU 3067 N PHE D 29 14984 14291 11540 -2257 1880 -959 N ATOM 3068 CA PHE D 29 -23.139 -23.985 -17.778 1.00 99.68 C ANISOU 3068 CA PHE D 29 14779 12984 10111 -2186 1735 -390 C ATOM 3069 C PHE D 29 -21.725 -23.714 -17.277 1.00 94.07 C ANISOU 3069 C PHE D 29 14235 12279 9230 -1831 1635 -106 C ATOM 3070 O PHE D 29 -21.342 -22.574 -17.004 1.00 90.27 O ANISOU 3070 O PHE D 29 13297 12031 8971 -1627 1692 -287 O ATOM 3071 CB PHE D 29 -23.113 -24.503 -19.222 1.00 99.57 C ANISOU 3071 CB PHE D 29 15017 12528 10288 -1803 1484 -173 C ATOM 3072 CG PHE D 29 -24.468 -24.876 -19.754 1.00 98.29 C ANISOU 3072 CG PHE D 29 14750 12313 10284 -2139 1533 -413 C ATOM 3073 CD1 PHE D 29 -25.309 -23.911 -20.285 1.00 91.20 C ANISOU 3073 CD1 PHE D 29 13220 11506 9925 -2066 1510 -865 C ATOM 3074 CD2 PHE D 29 -24.902 -26.190 -19.719 1.00 99.88 C ANISOU 3074 CD2 PHE D 29 15505 12338 10107 -2531 1530 -208 C ATOM 3075 CE1 PHE D 29 -26.556 -24.250 -20.770 1.00 86.90 C ANISOU 3075 CE1 PHE D 29 12525 10921 9571 -2349 1515 -1146 C ATOM 3076 CE2 PHE D 29 -26.149 -26.536 -20.204 1.00 96.97 C ANISOU 3076 CE2 PHE D 29 15016 11956 9871 -2873 1589 -449 C ATOM 3077 CZ PHE D 29 -26.977 -25.565 -20.730 1.00 89.30 C ANISOU 3077 CZ PHE D 29 13338 11120 9470 -2768 1598 -938 C ATOM 3078 N ASP D 30 -20.948 -24.788 -17.158 1.00104.89 N ANISOU 3078 N ASP D 30 16269 13360 10223 -1744 1426 310 N ATOM 3079 CA ASP D 30 -19.599 -24.682 -16.622 1.00109.78 C ANISOU 3079 CA ASP D 30 17061 13967 10682 -1406 1268 533 C ATOM 3080 C ASP D 30 -18.686 -23.932 -17.585 1.00 91.42 C ANISOU 3080 C ASP D 30 14406 11614 8715 -736 1168 521 C ATOM 3081 O ASP D 30 -18.770 -24.097 -18.805 1.00100.18 O ANISOU 3081 O ASP D 30 15516 12515 10032 -474 1075 529 O ATOM 3082 CB ASP D 30 -19.027 -26.071 -16.338 1.00123.35 C ANISOU 3082 CB ASP D 30 19584 15293 11990 -1416 919 903 C ATOM 3083 CG ASP D 30 -19.711 -26.756 -15.172 1.00128.13 C ANISOU 3083 CG ASP D 30 20668 15936 12078 -2228 957 988 C ATOM 3084 OD1 ASP D 30 -20.153 -26.050 -14.242 1.00131.72 O ANISOU 3084 OD1 ASP D 30 20797 16831 12419 -2713 1282 761 O ATOM 3085 OD2 ASP D 30 -19.802 -28.002 -15.183 1.00129.12 O ANISOU 3085 OD2 ASP D 30 21524 15656 11879 -2433 643 1258 O ATOM 3086 N VAL D 31 -17.809 -23.100 -17.022 1.00 90.80 N ANISOU 3086 N VAL D 31 14072 11773 8655 -538 1195 494 N ATOM 3087 CA VAL D 31 -16.826 -22.386 -17.826 1.00 79.16 C ANISOU 3087 CA VAL D 31 12326 10343 7408 -28 1115 478 C ATOM 3088 C VAL D 31 -15.780 -23.369 -18.336 1.00 79.07 C ANISOU 3088 C VAL D 31 12688 10089 7267 386 860 649 C ATOM 3089 O VAL D 31 -15.328 -24.262 -17.606 1.00 93.83 O ANISOU 3089 O VAL D 31 14976 11795 8880 410 651 801 O ATOM 3090 CB VAL D 31 -16.184 -21.257 -17.002 1.00 76.09 C ANISOU 3090 CB VAL D 31 11576 10292 7042 16 1209 390 C ATOM 3091 CG1 VAL D 31 -15.173 -20.494 -17.837 1.00 84.82 C ANISOU 3091 CG1 VAL D 31 12428 11490 8308 415 1139 364 C ATOM 3092 CG2 VAL D 31 -17.254 -20.317 -16.472 1.00 75.23 C ANISOU 3092 CG2 VAL D 31 11054 10418 7112 -355 1419 103 C ATOM 3093 N ASP D 32 -15.392 -23.212 -19.601 1.00 81.88 N ANISOU 3093 N ASP D 32 12908 10408 7795 689 826 576 N ATOM 3094 CA ASP D 32 -14.482 -24.154 -20.241 1.00 85.26 C ANISOU 3094 CA ASP D 32 13582 10660 8154 1092 612 580 C ATOM 3095 C ASP D 32 -13.057 -23.994 -19.722 1.00 87.54 C ANISOU 3095 C ASP D 32 13732 11151 8379 1451 498 498 C ATOM 3096 O ASP D 32 -12.538 -24.884 -19.039 1.00 98.41 O ANISOU 3096 O ASP D 32 15439 12327 9627 1640 202 557 O ATOM 3097 CB ASP D 32 -14.520 -23.977 -21.761 1.00 76.58 C ANISOU 3097 CB ASP D 32 12349 9551 7196 1189 672 457 C ATOM 3098 CG ASP D 32 -13.955 -25.172 -22.502 1.00 98.55 C ANISOU 3098 CG ASP D 32 15406 12116 9923 1527 477 375 C ATOM 3099 OD1 ASP D 32 -14.624 -26.226 -22.528 1.00108.21 O ANISOU 3099 OD1 ASP D 32 17051 12969 11096 1466 320 495 O ATOM 3100 OD2 ASP D 32 -12.844 -25.058 -23.061 1.00110.63 O ANISOU 3100 OD2 ASP D 32 16712 13869 11453 1829 476 137 O ATOM 3101 N ILE D 33 -12.415 -22.872 -20.042 1.00 85.98 N ANISOU 3101 N ILE D 33 11166 10859 10642 -1413 -3121 -383 N ATOM 3102 CA ILE D 33 -11.027 -22.618 -19.673 1.00 87.44 C ANISOU 3102 CA ILE D 33 11635 10854 10733 -1081 -2678 -600 C ATOM 3103 C ILE D 33 -10.926 -21.221 -19.078 1.00 93.50 C ANISOU 3103 C ILE D 33 12169 11927 11431 -665 -2458 -468 C ATOM 3104 O ILE D 33 -11.565 -20.282 -19.565 1.00109.97 O ANISOU 3104 O ILE D 33 14156 14248 13380 -568 -2613 -366 O ATOM 3105 CB ILE D 33 -10.081 -22.763 -20.886 1.00106.12 C ANISOU 3105 CB ILE D 33 14654 12886 12780 -1111 -2658 -967 C ATOM 3106 CG1 ILE D 33 -10.185 -24.165 -21.487 1.00127.43 C ANISOU 3106 CG1 ILE D 33 17732 15196 15491 -1515 -2844 -1139 C ATOM 3107 CG2 ILE D 33 -8.640 -22.468 -20.492 1.00 73.22 C ANISOU 3107 CG2 ILE D 33 10676 8586 8556 -772 -2203 -1080 C ATOM 3108 CD1 ILE D 33 -9.367 -24.352 -22.746 1.00139.94 C ANISOU 3108 CD1 ILE D 33 20039 16431 16703 -1511 -2802 -1490 C ATOM 3109 N MET D 34 -10.125 -21.086 -18.021 1.00 85.06 N ANISOU 3109 N MET D 34 11040 10842 10438 -428 -2100 -456 N ATOM 3110 CA MET D 34 -9.882 -19.802 -17.381 1.00 84.16 C ANISOU 3110 CA MET D 34 10838 10925 10214 -76 -1877 -388 C ATOM 3111 C MET D 34 -8.384 -19.603 -17.191 1.00 79.13 C ANISOU 3111 C MET D 34 10498 10112 9456 48 -1602 -581 C ATOM 3112 O MET D 34 -7.629 -20.566 -17.027 1.00 75.84 O ANISOU 3112 O MET D 34 10176 9505 9135 -51 -1484 -642 O ATOM 3113 CB MET D 34 -10.600 -19.701 -16.029 1.00 87.91 C ANISOU 3113 CB MET D 34 10875 11650 10879 76 -1749 -84 C ATOM 3114 CG MET D 34 -12.076 -20.066 -16.078 1.00 99.81 C ANISOU 3114 CG MET D 34 11965 13370 12586 -59 -1994 231 C ATOM 3115 SD MET D 34 -12.927 -19.870 -14.500 1.00 98.50 S ANISOU 3115 SD MET D 34 11285 13521 12620 226 -1752 662 S ATOM 3116 CE MET D 34 -12.779 -18.103 -14.252 1.00 91.68 C ANISOU 3116 CE MET D 34 10618 12774 11443 708 -1490 636 C ATOM 3117 N GLY D 35 -7.962 -18.344 -17.214 1.00 70.03 N ANISOU 3117 N GLY D 35 9479 9023 8105 262 -1493 -631 N ATOM 3118 CA GLY D 35 -6.560 -18.025 -17.074 1.00 63.16 C ANISOU 3118 CA GLY D 35 8839 8032 7127 331 -1282 -747 C ATOM 3119 C GLY D 35 -6.358 -16.630 -16.523 1.00 64.86 C ANISOU 3119 C GLY D 35 9108 8349 7188 523 -1168 -727 C ATOM 3120 O GLY D 35 -7.310 -15.950 -16.135 1.00 72.18 O ANISOU 3120 O GLY D 35 9916 9419 8089 670 -1182 -621 O ATOM 3121 N TRP D 36 -5.094 -16.210 -16.498 1.00 60.67 N ANISOU 3121 N TRP D 36 8774 7724 6553 519 -1040 -799 N ATOM 3122 CA TRP D 36 -4.704 -14.913 -15.959 1.00 65.96 C ANISOU 3122 CA TRP D 36 9587 8417 7060 612 -952 -808 C ATOM 3123 C TRP D 36 -3.791 -14.197 -16.942 1.00 65.33 C ANISOU 3123 C TRP D 36 9780 8194 6848 594 -936 -892 C ATOM 3124 O TRP D 36 -2.852 -14.797 -17.475 1.00 64.27 O ANISOU 3124 O TRP D 36 9686 7979 6753 508 -889 -891 O ATOM 3125 CB TRP D 36 -3.997 -15.062 -14.606 1.00 68.94 C ANISOU 3125 CB TRP D 36 9878 8871 7444 545 -847 -736 C ATOM 3126 CG TRP D 36 -4.908 -15.440 -13.478 1.00 72.15 C ANISOU 3126 CG TRP D 36 10059 9435 7920 630 -813 -625 C ATOM 3127 CD1 TRP D 36 -5.191 -16.701 -13.041 1.00 65.55 C ANISOU 3127 CD1 TRP D 36 8935 8678 7292 577 -803 -506 C ATOM 3128 CD2 TRP D 36 -5.651 -14.548 -12.638 1.00 68.64 C ANISOU 3128 CD2 TRP D 36 9683 9067 7331 816 -737 -591 C ATOM 3129 NE1 TRP D 36 -6.065 -16.649 -11.982 1.00 63.66 N ANISOU 3129 NE1 TRP D 36 8528 8600 7061 713 -738 -374 N ATOM 3130 CE2 TRP D 36 -6.363 -15.339 -11.716 1.00 60.43 C ANISOU 3130 CE2 TRP D 36 8348 8193 6419 886 -679 -424 C ATOM 3131 CE3 TRP D 36 -5.783 -13.157 -12.578 1.00 67.34 C ANISOU 3131 CE3 TRP D 36 9839 8813 6934 958 -673 -669 C ATOM 3132 CZ2 TRP D 36 -7.196 -14.786 -10.745 1.00 62.08 C ANISOU 3132 CZ2 TRP D 36 8564 8511 6511 1128 -540 -317 C ATOM 3133 CZ3 TRP D 36 -6.611 -12.610 -11.613 1.00 69.34 C ANISOU 3133 CZ3 TRP D 36 10157 9129 7060 1200 -525 -593 C ATOM 3134 CH2 TRP D 36 -7.307 -13.423 -10.710 1.00 68.59 C ANISOU 3134 CH2 TRP D 36 9755 9231 7077 1301 -450 -411 C ATOM 3135 N TYR D 37 -4.068 -12.915 -17.172 1.00 66.35 N ANISOU 3135 N TYR D 37 10100 8281 6827 710 -931 -925 N ATOM 3136 CA TYR D 37 -3.235 -12.050 -17.994 1.00 58.78 C ANISOU 3136 CA TYR D 37 9397 7184 5752 699 -896 -963 C ATOM 3137 C TYR D 37 -2.790 -10.851 -17.170 1.00 77.09 C ANISOU 3137 C TYR D 37 11914 9424 7954 666 -826 -968 C ATOM 3138 O TYR D 37 -3.524 -10.372 -16.301 1.00 84.64 O ANISOU 3138 O TYR D 37 12919 10398 8841 773 -787 -980 O ATOM 3139 CB TYR D 37 -3.986 -11.558 -19.239 1.00 61.70 C ANISOU 3139 CB TYR D 37 9884 7525 6033 857 -962 -986 C ATOM 3140 CG TYR D 37 -4.368 -12.640 -20.224 1.00 77.71 C ANISOU 3140 CG TYR D 37 11840 9593 8095 824 -1089 -1017 C ATOM 3141 CD1 TYR D 37 -5.457 -13.468 -19.988 1.00 70.24 C ANISOU 3141 CD1 TYR D 37 10666 8773 7251 793 -1226 -987 C ATOM 3142 CD2 TYR D 37 -3.652 -12.818 -21.401 1.00 76.89 C ANISOU 3142 CD2 TYR D 37 11934 9383 7898 812 -1070 -1063 C ATOM 3143 CE1 TYR D 37 -5.813 -14.453 -20.889 1.00 75.23 C ANISOU 3143 CE1 TYR D 37 11310 9392 7882 683 -1391 -1040 C ATOM 3144 CE2 TYR D 37 -4.001 -13.798 -22.308 1.00 62.77 C ANISOU 3144 CE2 TYR D 37 10206 7577 6065 766 -1189 -1134 C ATOM 3145 CZ TYR D 37 -5.082 -14.612 -22.047 1.00 70.85 C ANISOU 3145 CZ TYR D 37 11044 8694 7180 669 -1374 -1142 C ATOM 3146 OH TYR D 37 -5.435 -15.591 -22.946 1.00 78.90 O ANISOU 3146 OH TYR D 37 12197 9651 8129 546 -1541 -1237 O ATOM 3147 N ARG D 38 -1.583 -10.362 -17.447 1.00 78.21 N ANISOU 3147 N ARG D 38 12195 9461 8059 513 -802 -939 N ATOM 3148 CA ARG D 38 -1.074 -9.162 -16.801 1.00 80.30 C ANISOU 3148 CA ARG D 38 12722 9593 8194 388 -788 -954 C ATOM 3149 C ARG D 38 -0.501 -8.219 -17.849 1.00 70.78 C ANISOU 3149 C ARG D 38 11735 8211 6949 372 -758 -918 C ATOM 3150 O ARG D 38 -0.061 -8.646 -18.920 1.00 67.18 O ANISOU 3150 O ARG D 38 11181 7780 6562 407 -734 -840 O ATOM 3151 CB ARG D 38 -0.004 -9.483 -15.743 1.00 75.26 C ANISOU 3151 CB ARG D 38 11984 9045 7567 86 -845 -872 C ATOM 3152 CG ARG D 38 1.373 -9.815 -16.297 1.00 75.34 C ANISOU 3152 CG ARG D 38 11835 9099 7691 -110 -852 -679 C ATOM 3153 CD ARG D 38 2.437 -9.637 -15.224 1.00 87.22 C ANISOU 3153 CD ARG D 38 13288 10697 9157 -465 -962 -539 C ATOM 3154 NE ARG D 38 3.766 -10.037 -15.679 1.00 88.49 N ANISOU 3154 NE ARG D 38 13187 10970 9465 -628 -943 -238 N ATOM 3155 CZ ARG D 38 4.351 -11.185 -15.355 1.00 94.65 C ANISOU 3155 CZ ARG D 38 13604 11976 10384 -652 -896 -16 C ATOM 3156 NH1 ARG D 38 3.726 -12.050 -14.568 1.00103.90 N ANISOU 3156 NH1 ARG D 38 14640 13269 11567 -560 -889 -90 N ATOM 3157 NH2 ARG D 38 5.563 -11.467 -15.813 1.00 97.78 N ANISOU 3157 NH2 ARG D 38 13755 12479 10918 -739 -822 331 N ATOM 3158 N GLN D 39 -0.516 -6.927 -17.528 1.00 67.37 N ANISOU 3158 N GLN D 39 11644 7568 6385 337 -731 -969 N ATOM 3159 CA GLN D 39 -0.018 -5.885 -18.421 1.00 82.41 C ANISOU 3159 CA GLN D 39 13787 9262 8263 313 -685 -911 C ATOM 3160 C GLN D 39 0.874 -4.947 -17.622 1.00 94.79 C ANISOU 3160 C GLN D 39 15638 10628 9752 -40 -745 -907 C ATOM 3161 O GLN D 39 0.381 -4.152 -16.814 1.00 82.74 O ANISOU 3161 O GLN D 39 14476 8902 8060 -32 -716 -1048 O ATOM 3162 CB GLN D 39 -1.170 -5.120 -19.075 1.00 96.15 C ANISOU 3162 CB GLN D 39 15731 10879 9921 669 -574 -957 C ATOM 3163 CG GLN D 39 -0.719 -4.021 -20.023 1.00106.15 C ANISOU 3163 CG GLN D 39 17251 11916 11165 684 -496 -869 C ATOM 3164 CD GLN D 39 -1.869 -3.414 -20.802 1.00114.19 C ANISOU 3164 CD GLN D 39 18388 12886 12113 1085 -378 -842 C ATOM 3165 OE1 GLN D 39 -3.001 -3.895 -20.738 1.00121.17 O ANISOU 3165 OE1 GLN D 39 19104 13954 12982 1335 -383 -856 O ATOM 3166 NE2 GLN D 39 -1.584 -2.352 -21.546 1.00111.48 N ANISOU 3166 NE2 GLN D 39 18299 12315 11742 1141 -273 -748 N ATOM 3167 N ALA D 40 2.182 -5.041 -17.845 1.00116.73 N ANISOU 3167 N ALA D 40 18269 13451 12633 -355 -824 -718 N ATOM 3168 CA ALA D 40 3.120 -4.155 -17.178 1.00120.03 C ANISOU 3168 CA ALA D 40 18920 13697 12987 -797 -956 -661 C ATOM 3169 C ALA D 40 2.999 -2.738 -17.743 1.00125.14 C ANISOU 3169 C ALA D 40 20016 13959 13571 -777 -875 -697 C ATOM 3170 O ALA D 40 2.561 -2.552 -18.883 1.00125.87 O ANISOU 3170 O ALA D 40 20101 14004 13719 -446 -717 -655 O ATOM 3171 CB ALA D 40 4.548 -4.667 -17.346 1.00121.21 C ANISOU 3171 CB ALA D 40 18684 14059 13310 -1127 -1058 -333 C ATOM 3172 N PRO D 41 3.368 -1.722 -16.964 1.00127.19 N ANISOU 3172 N PRO D 41 20712 13924 13692 -1135 -982 -772 N ATOM 3173 CA PRO D 41 3.291 -0.345 -17.472 1.00132.31 C ANISOU 3173 CA PRO D 41 21845 14133 14295 -1133 -877 -795 C ATOM 3174 C PRO D 41 4.250 -0.127 -18.633 1.00136.71 C ANISOU 3174 C PRO D 41 22167 14704 15073 -1265 -869 -477 C ATOM 3175 O PRO D 41 5.438 -0.449 -18.551 1.00143.12 O ANISOU 3175 O PRO D 41 22664 15697 16018 -1672 -1041 -219 O ATOM 3176 CB PRO D 41 3.670 0.504 -16.253 1.00133.23 C ANISOU 3176 CB PRO D 41 22504 13925 14193 -1609 -1050 -950 C ATOM 3177 CG PRO D 41 4.443 -0.419 -15.369 1.00125.43 C ANISOU 3177 CG PRO D 41 21150 13305 13203 -2003 -1326 -864 C ATOM 3178 CD PRO D 41 3.814 -1.765 -15.560 1.00123.18 C ANISOU 3178 CD PRO D 41 20341 13440 13023 -1562 -1208 -854 C ATOM 3179 N GLY D 42 3.721 0.425 -19.722 1.00133.60 N ANISOU 3179 N GLY D 42 21900 14148 14714 -890 -649 -441 N ATOM 3180 CA GLY D 42 4.504 0.685 -20.910 1.00130.22 C ANISOU 3180 CA GLY D 42 21288 13726 14466 -918 -579 -125 C ATOM 3181 C GLY D 42 4.808 -0.528 -21.762 1.00116.67 C ANISOU 3181 C GLY D 42 19021 12436 12874 -692 -522 71 C ATOM 3182 O GLY D 42 5.547 -0.400 -22.746 1.00116.37 O ANISOU 3182 O GLY D 42 18815 12436 12965 -682 -426 377 O ATOM 3183 N LYS D 43 4.266 -1.695 -21.422 1.00108.48 N ANISOU 3183 N LYS D 43 17737 11690 11792 -500 -550 -80 N ATOM 3184 CA LYS D 43 4.512 -2.922 -22.162 1.00 99.16 C ANISOU 3184 CA LYS D 43 16142 10842 10693 -286 -476 60 C ATOM 3185 C LYS D 43 3.182 -3.545 -22.566 1.00 89.23 C ANISOU 3185 C LYS D 43 14890 9694 9319 158 -412 -176 C ATOM 3186 O LYS D 43 2.118 -3.188 -22.054 1.00 79.67 O ANISOU 3186 O LYS D 43 13883 8385 8001 286 -433 -397 O ATOM 3187 CB LYS D 43 5.341 -3.917 -21.338 1.00 97.40 C ANISOU 3187 CB LYS D 43 15560 10877 10569 -568 -594 182 C ATOM 3188 CG LYS D 43 6.705 -3.390 -20.925 1.00 97.08 C ANISOU 3188 CG LYS D 43 15412 10820 10656 -1069 -719 506 C ATOM 3189 CD LYS D 43 7.469 -4.415 -20.102 1.00103.59 C ANISOU 3189 CD LYS D 43 15823 11967 11572 -1307 -834 694 C ATOM 3190 CE LYS D 43 8.828 -3.881 -19.680 1.00116.58 C ANISOU 3190 CE LYS D 43 17289 13661 13346 -1862 -1017 1095 C ATOM 3191 NZ LYS D 43 9.586 -4.869 -18.865 1.00118.35 N ANISOU 3191 NZ LYS D 43 17053 14259 13657 -2079 -1132 1359 N ATOM 3192 N GLU D 44 3.255 -4.490 -23.498 1.00 92.58 N ANISOU 3192 N GLU D 44 15103 10322 9753 387 -329 -96 N ATOM 3193 CA GLU D 44 2.063 -5.163 -23.987 1.00100.97 C ANISOU 3193 CA GLU D 44 16161 11506 10697 720 -334 -287 C ATOM 3194 C GLU D 44 1.609 -6.238 -23.004 1.00 93.46 C ANISOU 3194 C GLU D 44 15020 10711 9778 653 -447 -453 C ATOM 3195 O GLU D 44 2.386 -6.747 -22.191 1.00 96.53 O ANISOU 3195 O GLU D 44 15231 11173 10273 412 -480 -383 O ATOM 3196 CB GLU D 44 2.320 -5.783 -25.361 1.00100.03 C ANISOU 3196 CB GLU D 44 16003 11494 10511 954 -220 -176 C ATOM 3197 N ARG D 45 0.326 -6.579 -23.087 1.00 82.76 N ANISOU 3197 N ARG D 45 13669 9433 8341 865 -510 -622 N ATOM 3198 CA ARG D 45 -0.235 -7.612 -22.231 1.00 71.99 C ANISOU 3198 CA ARG D 45 12109 8216 7027 824 -606 -746 C ATOM 3199 C ARG D 45 0.328 -8.978 -22.610 1.00 71.65 C ANISOU 3199 C ARG D 45 11889 8289 7045 795 -583 -709 C ATOM 3200 O ARG D 45 0.662 -9.239 -23.769 1.00 89.09 O ANISOU 3200 O ARG D 45 14178 10486 9185 919 -505 -651 O ATOM 3201 CB ARG D 45 -1.762 -7.616 -22.337 1.00 68.67 C ANISOU 3201 CB ARG D 45 11683 7875 6532 1046 -683 -847 C ATOM 3202 CG ARG D 45 -2.465 -8.481 -21.302 1.00 77.53 C ANISOU 3202 CG ARG D 45 12591 9136 7732 1004 -767 -926 C ATOM 3203 CD ARG D 45 -3.978 -8.346 -21.395 1.00 74.06 C ANISOU 3203 CD ARG D 45 12082 8807 7249 1226 -833 -918 C ATOM 3204 NE ARG D 45 -4.422 -6.973 -21.165 1.00 80.23 N ANISOU 3204 NE ARG D 45 13073 9462 7951 1410 -712 -865 N ATOM 3205 CZ ARG D 45 -5.696 -6.606 -21.071 1.00 82.97 C ANISOU 3205 CZ ARG D 45 13356 9899 8268 1670 -687 -768 C ATOM 3206 NH1 ARG D 45 -6.659 -7.510 -21.184 1.00 87.28 N ANISOU 3206 NH1 ARG D 45 13585 10701 8875 1712 -836 -700 N ATOM 3207 NH2 ARG D 45 -6.008 -5.334 -20.862 1.00 82.02 N ANISOU 3207 NH2 ARG D 45 13493 9604 8066 1887 -502 -701 N ATOM 3208 N GLU D 46 0.443 -9.853 -21.612 1.00 78.19 N ANISOU 3208 N GLU D 46 12516 9210 7984 660 -618 -730 N ATOM 3209 CA GLU D 46 0.978 -11.190 -21.818 1.00 81.18 C ANISOU 3209 CA GLU D 46 12752 9651 8440 656 -544 -674 C ATOM 3210 C GLU D 46 0.203 -12.185 -20.967 1.00 76.72 C ANISOU 3210 C GLU D 46 12014 9179 7959 618 -635 -783 C ATOM 3211 O GLU D 46 -0.438 -11.824 -19.977 1.00 81.72 O ANISOU 3211 O GLU D 46 12577 9866 8606 566 -725 -842 O ATOM 3212 CB GLU D 46 2.474 -11.260 -21.482 1.00 96.29 C ANISOU 3212 CB GLU D 46 14522 11596 10469 509 -414 -416 C ATOM 3213 CG GLU D 46 2.810 -10.860 -20.054 1.00101.75 C ANISOU 3213 CG GLU D 46 15068 12362 11229 244 -518 -355 C ATOM 3214 CD GLU D 46 4.270 -11.083 -19.716 1.00108.47 C ANISOU 3214 CD GLU D 46 15684 13324 12205 57 -441 -20 C ATOM 3215 OE1 GLU D 46 4.955 -11.799 -20.476 1.00112.22 O ANISOU 3215 OE1 GLU D 46 16064 13824 12750 205 -242 179 O ATOM 3216 OE2 GLU D 46 4.735 -10.541 -18.691 1.00111.97 O ANISOU 3216 OE2 GLU D 46 16050 13834 12657 -234 -576 70 O ATOM 3217 N LEU D 47 0.271 -13.452 -21.369 1.00 67.88 N ANISOU 3217 N LEU D 47 10862 8048 6883 661 -578 -796 N ATOM 3218 CA LEU D 47 -0.382 -14.524 -20.633 1.00 69.53 C ANISOU 3218 CA LEU D 47 10900 8311 7208 604 -644 -860 C ATOM 3219 C LEU D 47 0.520 -15.003 -19.503 1.00 70.14 C ANISOU 3219 C LEU D 47 10738 8472 7441 493 -533 -685 C ATOM 3220 O LEU D 47 1.714 -15.242 -19.708 1.00 67.25 O ANISOU 3220 O LEU D 47 10337 8095 7120 501 -358 -491 O ATOM 3221 CB LEU D 47 -0.722 -15.685 -21.568 1.00 61.60 C ANISOU 3221 CB LEU D 47 10048 7189 6168 660 -640 -963 C ATOM 3222 CG LEU D 47 -1.337 -16.929 -20.921 1.00 60.96 C ANISOU 3222 CG LEU D 47 9817 7104 6240 565 -697 -1006 C ATOM 3223 CD1 LEU D 47 -2.702 -16.614 -20.327 1.00 63.89 C ANISOU 3223 CD1 LEU D 47 10005 7618 6652 502 -929 -1061 C ATOM 3224 CD2 LEU D 47 -1.433 -18.067 -21.926 1.00 66.34 C ANISOU 3224 CD2 LEU D 47 10782 7573 6853 577 -669 -1122 C ATOM 3225 N VAL D 48 -0.053 -15.142 -18.308 1.00 78.65 N ANISOU 3225 N VAL D 48 11628 9665 8591 412 -622 -701 N ATOM 3226 CA VAL D 48 0.701 -15.586 -17.141 1.00 79.61 C ANISOU 3226 CA VAL D 48 11508 9918 8823 299 -554 -518 C ATOM 3227 C VAL D 48 0.504 -17.084 -16.950 1.00 77.43 C ANISOU 3227 C VAL D 48 11082 9627 8712 339 -465 -472 C ATOM 3228 O VAL D 48 1.472 -17.852 -16.941 1.00 67.15 O ANISOU 3228 O VAL D 48 9681 8320 7513 361 -281 -272 O ATOM 3229 CB VAL D 48 0.283 -14.812 -15.878 1.00 73.77 C ANISOU 3229 CB VAL D 48 10718 9303 8008 204 -674 -549 C ATOM 3230 CG1 VAL D 48 1.040 -15.331 -14.667 1.00 79.12 C ANISOU 3230 CG1 VAL D 48 11151 10161 8751 67 -643 -347 C ATOM 3231 CG2 VAL D 48 0.523 -13.325 -16.067 1.00 66.89 C ANISOU 3231 CG2 VAL D 48 10088 8359 6970 147 -737 -605 C ATOM 3232 N ALA D 49 -0.748 -17.506 -16.796 1.00 80.02 N ANISOU 3232 N ALA D 49 11380 9941 9081 353 -577 -610 N ATOM 3233 CA ALA D 49 -1.056 -18.912 -16.586 1.00 77.89 C ANISOU 3233 CA ALA D 49 10993 9610 8990 344 -515 -570 C ATOM 3234 C ALA D 49 -2.489 -19.175 -17.022 1.00 68.96 C ANISOU 3234 C ALA D 49 9909 8418 7875 314 -705 -732 C ATOM 3235 O ALA D 49 -3.315 -18.261 -17.094 1.00 68.94 O ANISOU 3235 O ALA D 49 9912 8510 7772 339 -862 -804 O ATOM 3236 CB ALA D 49 -0.854 -19.321 -15.123 1.00 89.59 C ANISOU 3236 CB ALA D 49 12164 11279 10596 300 -454 -379 C ATOM 3237 N SER D 50 -2.770 -20.444 -17.311 1.00 64.25 N ANISOU 3237 N SER D 50 9348 7655 7410 253 -687 -751 N ATOM 3238 CA SER D 50 -4.105 -20.872 -17.701 1.00 71.85 C ANISOU 3238 CA SER D 50 10316 8567 8418 129 -921 -851 C ATOM 3239 C SER D 50 -4.294 -22.319 -17.274 1.00 69.94 C ANISOU 3239 C SER D 50 9985 8177 8411 13 -859 -777 C ATOM 3240 O SER D 50 -3.362 -23.124 -17.358 1.00 67.21 O ANISOU 3240 O SER D 50 9784 7631 8122 63 -617 -738 O ATOM 3241 CB SER D 50 -4.326 -20.730 -19.211 1.00 82.76 C ANISOU 3241 CB SER D 50 12070 9781 9593 94 -1067 -1050 C ATOM 3242 OG SER D 50 -3.442 -21.566 -19.938 1.00 85.24 O ANISOU 3242 OG SER D 50 12731 9801 9855 122 -875 -1122 O ATOM 3243 N ILE D 51 -5.500 -22.642 -16.814 1.00 64.43 N ANISOU 3243 N ILE D 51 9038 7574 7868 -121 -1047 -708 N ATOM 3244 CA ILE D 51 -5.829 -23.989 -16.363 1.00 66.28 C ANISOU 3244 CA ILE D 51 9162 7658 8365 -270 -1013 -606 C ATOM 3245 C ILE D 51 -7.197 -24.364 -16.917 1.00 69.18 C ANISOU 3245 C ILE D 51 9505 7979 8800 -544 -1361 -642 C ATOM 3246 O ILE D 51 -8.133 -23.558 -16.894 1.00 81.03 O ANISOU 3246 O ILE D 51 10774 9752 10262 -547 -1578 -568 O ATOM 3247 CB ILE D 51 -5.793 -24.098 -14.822 1.00 76.79 C ANISOU 3247 CB ILE D 51 10064 9228 9885 -168 -848 -341 C ATOM 3248 CG1 ILE D 51 -6.176 -25.509 -14.368 1.00 73.46 C ANISOU 3248 CG1 ILE D 51 9509 8637 9767 -318 -795 -194 C ATOM 3249 CG2 ILE D 51 -6.692 -23.049 -14.176 1.00 70.18 C ANISOU 3249 CG2 ILE D 51 8930 8739 8995 -83 -977 -240 C ATOM 3250 CD1 ILE D 51 -6.029 -25.730 -12.880 1.00 75.01 C ANISOU 3250 CD1 ILE D 51 9306 9068 10128 -187 -594 97 C ATOM 3251 N THR D 52 -7.306 -25.586 -17.431 1.00 74.80 N ANISOU 3251 N THR D 52 10476 8337 9609 -781 -1412 -727 N ATOM 3252 CA THR D 52 -8.542 -26.064 -18.024 1.00 82.34 C ANISOU 3252 CA THR D 52 11448 9216 10620 -1152 -1809 -753 C ATOM 3253 C THR D 52 -9.366 -26.823 -16.985 1.00 85.43 C ANISOU 3253 C THR D 52 11380 9688 11390 -1322 -1852 -458 C ATOM 3254 O THR D 52 -8.939 -27.043 -15.849 1.00 93.50 O ANISOU 3254 O THR D 52 12130 10796 12599 -1125 -1550 -265 O ATOM 3255 CB THR D 52 -8.247 -26.945 -19.237 1.00 92.09 C ANISOU 3255 CB THR D 52 13339 9961 11692 -1377 -1881 -1045 C ATOM 3256 OG1 THR D 52 -7.597 -28.149 -18.809 1.00 80.53 O ANISOU 3256 OG1 THR D 52 12057 8121 10422 -1369 -1562 -1022 O ATOM 3257 CG2 THR D 52 -7.343 -26.213 -20.217 1.00 86.30 C ANISOU 3257 CG2 THR D 52 13047 9163 10581 -1139 -1759 -1282 C ATOM 3258 N ASP D 53 -10.572 -27.234 -17.384 1.00 81.43 N ANISOU 3258 N ASP D 53 10766 9179 10995 -1711 -2252 -383 N ATOM 3259 CA ASP D 53 -11.444 -27.983 -16.487 1.00 87.86 C ANISOU 3259 CA ASP D 53 11111 10071 12202 -1914 -2319 -44 C ATOM 3260 C ASP D 53 -10.889 -29.361 -16.152 1.00 99.30 C ANISOU 3260 C ASP D 53 12793 11064 13874 -2036 -2083 -68 C ATOM 3261 O ASP D 53 -11.331 -29.972 -15.173 1.00111.31 O ANISOU 3261 O ASP D 53 13901 12647 15744 -2096 -2000 250 O ATOM 3262 CB ASP D 53 -12.838 -28.117 -17.101 1.00109.26 C ANISOU 3262 CB ASP D 53 13633 12892 14988 -2372 -2853 95 C ATOM 3263 CG ASP D 53 -12.799 -28.619 -18.532 1.00133.58 C ANISOU 3263 CG ASP D 53 17368 15570 17815 -2777 -3185 -268 C ATOM 3264 OD1 ASP D 53 -11.856 -28.254 -19.265 1.00136.22 O ANISOU 3264 OD1 ASP D 53 18237 15720 17801 -2568 -3033 -618 O ATOM 3265 OD2 ASP D 53 -13.710 -29.378 -18.923 1.00146.31 O ANISOU 3265 OD2 ASP D 53 18980 17051 19560 -3319 -3606 -188 O ATOM 3266 N GLY D 54 -9.937 -29.862 -16.936 1.00 96.53 N ANISOU 3266 N GLY D 54 13098 10250 13330 -2032 -1928 -397 N ATOM 3267 CA GLY D 54 -9.339 -31.154 -16.669 1.00 91.44 C ANISOU 3267 CA GLY D 54 12741 9121 12880 -2073 -1623 -401 C ATOM 3268 C GLY D 54 -8.192 -31.085 -15.683 1.00 84.04 C ANISOU 3268 C GLY D 54 11616 8298 12016 -1592 -1094 -236 C ATOM 3269 O GLY D 54 -7.899 -32.065 -14.991 1.00 85.29 O ANISOU 3269 O GLY D 54 11720 8239 12447 -1558 -810 -49 O ATOM 3270 N GLY D 55 -7.534 -29.932 -15.610 1.00 79.84 N ANISOU 3270 N GLY D 55 10983 8111 11243 -1243 -975 -275 N ATOM 3271 CA GLY D 55 -6.428 -29.725 -14.690 1.00 80.51 C ANISOU 3271 CA GLY D 55 10859 8382 11350 -848 -559 -92 C ATOM 3272 C GLY D 55 -5.094 -29.428 -15.344 1.00 93.52 C ANISOU 3272 C GLY D 55 12906 9891 12737 -581 -291 -249 C ATOM 3273 O GLY D 55 -4.116 -29.185 -14.623 1.00 98.64 O ANISOU 3273 O GLY D 55 13343 10747 13390 -291 10 -51 O ATOM 3274 N SER D 56 -4.993 -29.436 -16.671 1.00102.96 N ANISOU 3274 N SER D 56 14657 10771 13691 -668 -388 -556 N ATOM 3275 CA SER D 56 -3.726 -29.143 -17.328 1.00 95.78 C ANISOU 3275 CA SER D 56 14108 9746 12538 -370 -87 -644 C ATOM 3276 C SER D 56 -3.420 -27.653 -17.239 1.00 91.03 C ANISOU 3276 C SER D 56 13242 9606 11740 -202 -176 -630 C ATOM 3277 O SER D 56 -4.267 -26.813 -17.557 1.00 91.74 O ANISOU 3277 O SER D 56 13252 9900 11704 -341 -529 -762 O ATOM 3278 CB SER D 56 -3.768 -29.593 -18.787 1.00 97.99 C ANISOU 3278 CB SER D 56 15125 9540 12566 -490 -148 -980 C ATOM 3279 OG SER D 56 -3.950 -30.995 -18.883 1.00106.38 O ANISOU 3279 OG SER D 56 16558 10078 13783 -656 -30 -1019 O ATOM 3280 N THR D 57 -2.204 -27.328 -16.808 1.00 87.28 N ANISOU 3280 N THR D 57 12628 9289 11244 86 145 -433 N ATOM 3281 CA THR D 57 -1.782 -25.951 -16.606 1.00 83.96 C ANISOU 3281 CA THR D 57 11980 9262 10659 202 76 -391 C ATOM 3282 C THR D 57 -0.665 -25.592 -17.576 1.00 81.57 C ANISOU 3282 C THR D 57 12007 8842 10144 403 289 -424 C ATOM 3283 O THR D 57 0.135 -26.444 -17.974 1.00 91.04 O ANISOU 3283 O THR D 57 13469 9753 11370 572 635 -334 O ATOM 3284 CB THR D 57 -1.309 -25.720 -15.164 1.00 78.35 C ANISOU 3284 CB THR D 57 10770 8919 10083 293 193 -77 C ATOM 3285 OG1 THR D 57 -0.276 -26.659 -14.841 1.00 70.47 O ANISOU 3285 OG1 THR D 57 9737 7806 9231 461 571 196 O ATOM 3286 CG2 THR D 57 -2.465 -25.892 -14.191 1.00 76.72 C ANISOU 3286 CG2 THR D 57 10229 8881 10042 150 3 -18 C ATOM 3287 N ASN D 58 -0.620 -24.315 -17.953 1.00 72.71 N ANISOU 3287 N ASN D 58 10876 7933 8818 415 120 -517 N ATOM 3288 CA ASN D 58 0.403 -23.796 -18.857 1.00 72.87 C ANISOU 3288 CA ASN D 58 11146 7899 8644 604 306 -499 C ATOM 3289 C ASN D 58 0.873 -22.455 -18.311 1.00 73.44 C ANISOU 3289 C ASN D 58 10899 8343 8662 610 221 -362 C ATOM 3290 O ASN D 58 0.098 -21.495 -18.269 1.00 76.25 O ANISOU 3290 O ASN D 58 11203 8848 8918 498 -67 -520 O ATOM 3291 CB ASN D 58 -0.133 -23.650 -20.281 1.00 67.52 C ANISOU 3291 CB ASN D 58 10966 6980 7709 571 156 -817 C ATOM 3292 N TYR D 59 2.134 -22.389 -17.896 1.00 79.39 N ANISOU 3292 N TYR D 59 11450 9236 9479 730 470 -39 N ATOM 3293 CA TYR D 59 2.713 -21.184 -17.322 1.00 84.24 C ANISOU 3293 CA TYR D 59 11794 10173 10039 657 365 118 C ATOM 3294 C TYR D 59 3.652 -20.516 -18.318 1.00 80.73 C ANISOU 3294 C TYR D 59 11512 9695 9466 774 500 217 C ATOM 3295 O TYR D 59 4.124 -21.133 -19.277 1.00 84.70 O ANISOU 3295 O TYR D 59 12276 9970 9937 987 778 266 O ATOM 3296 CB TYR D 59 3.477 -21.499 -16.031 1.00 75.36 C ANISOU 3296 CB TYR D 59 10247 9316 9071 624 466 488 C ATOM 3297 CG TYR D 59 2.636 -22.124 -14.942 1.00 73.89 C ANISOU 3297 CG TYR D 59 9863 9204 9008 538 370 457 C ATOM 3298 CD1 TYR D 59 2.596 -23.502 -14.774 1.00 79.92 C ANISOU 3298 CD1 TYR D 59 10596 9803 9967 643 597 578 C ATOM 3299 CD2 TYR D 59 1.888 -21.337 -14.078 1.00 72.44 C ANISOU 3299 CD2 TYR D 59 9552 9229 8741 383 95 333 C ATOM 3300 CE1 TYR D 59 1.831 -24.078 -13.778 1.00 84.85 C ANISOU 3300 CE1 TYR D 59 11011 10500 10728 568 525 597 C ATOM 3301 CE2 TYR D 59 1.119 -21.904 -13.079 1.00 74.05 C ANISOU 3301 CE2 TYR D 59 9560 9523 9052 349 48 356 C ATOM 3302 CZ TYR D 59 1.094 -23.274 -12.934 1.00 84.44 C ANISOU 3302 CZ TYR D 59 10790 10703 10589 428 251 499 C ATOM 3303 OH TYR D 59 0.331 -23.844 -11.941 1.00 88.85 O ANISOU 3303 OH TYR D 59 11127 11355 11277 395 219 567 O ATOM 3304 N ALA D 60 3.918 -19.237 -18.074 1.00 86.14 N ANISOU 3304 N ALA D 60 9598 13967 9166 430 188 -1513 N ATOM 3305 CA ALA D 60 4.905 -18.510 -18.852 1.00 82.90 C ANISOU 3305 CA ALA D 60 8950 13905 8644 272 494 -1658 C ATOM 3306 C ALA D 60 6.307 -18.791 -18.320 1.00 97.01 C ANISOU 3306 C ALA D 60 10291 15752 10815 394 441 -1833 C ATOM 3307 O ALA D 60 6.491 -19.269 -17.198 1.00113.38 O ANISOU 3307 O ALA D 60 12319 17563 13196 553 102 -1745 O ATOM 3308 CB ALA D 60 4.618 -17.008 -18.824 1.00 70.26 C ANISOU 3308 CB ALA D 60 7567 12408 6722 -44 581 -1352 C ATOM 3309 N ASP D 61 7.307 -18.485 -19.149 1.00100.29 N ANISOU 3309 N ASP D 61 10370 16526 11209 288 770 -2079 N ATOM 3310 CA ASP D 61 8.689 -18.771 -18.780 1.00106.23 C ANISOU 3310 CA ASP D 61 10580 17388 12396 419 745 -2300 C ATOM 3311 C ASP D 61 9.203 -17.856 -17.676 1.00109.77 C ANISOU 3311 C ASP D 61 10971 17801 12934 233 524 -1988 C ATOM 3312 O ASP D 61 10.162 -18.219 -16.987 1.00107.01 O ANISOU 3312 O ASP D 61 10233 17402 13026 383 298 -2073 O ATOM 3313 CB ASP D 61 9.593 -18.659 -20.008 1.00113.94 C ANISOU 3313 CB ASP D 61 11166 18820 13305 307 1239 -2681 C ATOM 3314 CG ASP D 61 9.166 -19.584 -21.131 1.00128.91 C ANISOU 3314 CG ASP D 61 13153 20751 15074 472 1476 -3045 C ATOM 3315 OD1 ASP D 61 8.539 -20.624 -20.840 1.00133.42 O ANISOU 3315 OD1 ASP D 61 13897 20964 15832 791 1190 -3099 O ATOM 3316 OD2 ASP D 61 9.459 -19.271 -22.304 1.00137.82 O ANISOU 3316 OD2 ASP D 61 14222 22260 15884 242 1941 -3275 O ATOM 3317 N SER D 62 8.591 -16.688 -17.490 1.00113.43 N ANISOU 3317 N SER D 62 11825 18260 13013 -79 543 -1641 N ATOM 3318 CA SER D 62 9.048 -15.732 -16.491 1.00111.96 C ANISOU 3318 CA SER D 62 11665 18025 12850 -295 346 -1362 C ATOM 3319 C SER D 62 8.446 -15.968 -15.111 1.00117.61 C ANISOU 3319 C SER D 62 12699 18329 13659 -176 -80 -1110 C ATOM 3320 O SER D 62 8.922 -15.373 -14.138 1.00135.60 O ANISOU 3320 O SER D 62 15006 20520 15995 -325 -308 -917 O ATOM 3321 CB SER D 62 8.730 -14.303 -16.945 1.00104.68 C ANISOU 3321 CB SER D 62 11050 17251 11474 -694 555 -1133 C ATOM 3322 OG SER D 62 7.336 -14.125 -17.131 1.00109.52 O ANISOU 3322 OG SER D 62 12157 17670 11784 -673 545 -968 O ATOM 3323 N VAL D 63 7.420 -16.810 -15.000 1.00 96.44 N ANISOU 3323 N VAL D 63 10279 15403 10962 38 -189 -1107 N ATOM 3324 CA VAL D 63 6.774 -17.067 -13.717 1.00 81.49 C ANISOU 3324 CA VAL D 63 8722 13151 9088 82 -534 -873 C ATOM 3325 C VAL D 63 6.756 -18.564 -13.440 1.00 82.53 C ANISOU 3325 C VAL D 63 8772 13043 9541 380 -807 -1011 C ATOM 3326 O VAL D 63 6.107 -19.023 -12.493 1.00 71.80 O ANISOU 3326 O VAL D 63 7732 11382 8168 395 -1085 -832 O ATOM 3327 CB VAL D 63 5.349 -16.486 -13.682 1.00 72.78 C ANISOU 3327 CB VAL D 63 8085 11951 7616 -30 -419 -667 C ATOM 3328 CG1 VAL D 63 5.376 -14.986 -13.937 1.00 83.07 C ANISOU 3328 CG1 VAL D 63 9516 13408 8639 -299 -225 -528 C ATOM 3329 CG2 VAL D 63 4.463 -17.192 -14.696 1.00 75.80 C ANISOU 3329 CG2 VAL D 63 8512 12362 7927 112 -262 -806 C ATOM 3330 N LYS D 64 7.466 -19.334 -14.261 1.00 92.21 N ANISOU 3330 N LYS D 64 9595 14393 11049 602 -724 -1344 N ATOM 3331 CA LYS D 64 7.518 -20.778 -14.076 1.00 85.68 C ANISOU 3331 CA LYS D 64 8696 13283 10575 921 -1023 -1512 C ATOM 3332 C LYS D 64 8.269 -21.118 -12.795 1.00 97.03 C ANISOU 3332 C LYS D 64 10058 14447 12361 982 -1536 -1381 C ATOM 3333 O LYS D 64 9.333 -20.557 -12.517 1.00101.89 O ANISOU 3333 O LYS D 64 10344 15208 13161 913 -1599 -1384 O ATOM 3334 CB LYS D 64 8.188 -21.442 -15.278 1.00 84.71 C ANISOU 3334 CB LYS D 64 8138 13355 10693 1170 -779 -1967 C ATOM 3335 N GLY D 65 7.710 -22.041 -12.011 1.00107.03 N ANISOU 3335 N GLY D 65 11651 15310 13704 1068 -1938 -1244 N ATOM 3336 CA GLY D 65 8.288 -22.432 -10.745 1.00114.96 C ANISOU 3336 CA GLY D 65 12716 15988 14974 1076 -2512 -1064 C ATOM 3337 C GLY D 65 7.936 -21.544 -9.572 1.00106.62 C ANISOU 3337 C GLY D 65 12086 14860 13564 708 -2641 -673 C ATOM 3338 O GLY D 65 8.144 -21.951 -8.423 1.00111.34 O ANISOU 3338 O GLY D 65 12919 15131 14253 636 -3152 -465 O ATOM 3339 N ARG D 66 7.409 -20.347 -9.820 1.00 91.25 N ANISOU 3339 N ARG D 66 10286 13180 11206 467 -2217 -576 N ATOM 3340 CA ARG D 66 7.025 -19.413 -8.770 1.00 78.37 C ANISOU 3340 CA ARG D 66 9078 11485 9216 136 -2266 -271 C ATOM 3341 C ARG D 66 5.519 -19.333 -8.578 1.00 86.11 C ANISOU 3341 C ARG D 66 10532 12390 9796 6 -2049 -134 C ATOM 3342 O ARG D 66 5.032 -19.435 -7.447 1.00 85.74 O ANISOU 3342 O ARG D 66 10911 12117 9550 -187 -2251 81 O ATOM 3343 CB ARG D 66 7.579 -18.017 -9.087 1.00 71.76 C ANISOU 3343 CB ARG D 66 8069 10950 8246 -45 -1992 -268 C ATOM 3344 CG ARG D 66 9.092 -17.955 -9.194 1.00 83.80 C ANISOU 3344 CG ARG D 66 9069 12605 10165 6 -2179 -387 C ATOM 3345 CD ARG D 66 9.519 -16.758 -10.023 1.00 86.51 C ANISOU 3345 CD ARG D 66 9167 13329 10374 -167 -1771 -456 C ATOM 3346 NE ARG D 66 8.883 -15.527 -9.565 1.00 85.24 N ANISOU 3346 NE ARG D 66 9478 13146 9762 -475 -1640 -219 N ATOM 3347 CZ ARG D 66 8.875 -14.391 -10.254 1.00 92.91 C ANISOU 3347 CZ ARG D 66 10444 14357 10501 -668 -1298 -213 C ATOM 3348 NH1 ARG D 66 9.465 -14.329 -11.440 1.00 97.06 N ANISOU 3348 NH1 ARG D 66 10530 15208 11141 -644 -1014 -414 N ATOM 3349 NH2 ARG D 66 8.271 -13.319 -9.760 1.00 95.19 N ANISOU 3349 NH2 ARG D 66 11193 14543 10430 -897 -1238 -20 N ATOM 3350 N PHE D 67 4.765 -19.151 -9.658 1.00 86.37 N ANISOU 3350 N PHE D 67 10495 12620 9702 83 -1642 -257 N ATOM 3351 CA PHE D 67 3.316 -19.061 -9.579 1.00 79.52 C ANISOU 3351 CA PHE D 67 9966 11714 8533 -15 -1433 -152 C ATOM 3352 C PHE D 67 2.694 -20.448 -9.683 1.00 74.52 C ANISOU 3352 C PHE D 67 9410 10888 8017 102 -1593 -192 C ATOM 3353 O PHE D 67 3.237 -21.348 -10.329 1.00 76.40 O ANISOU 3353 O PHE D 67 9399 11082 8547 332 -1729 -383 O ATOM 3354 CB PHE D 67 2.757 -18.160 -10.684 1.00 76.90 C ANISOU 3354 CB PHE D 67 9544 11648 8026 -10 -1010 -228 C ATOM 3355 CG PHE D 67 3.102 -16.701 -10.526 1.00 77.34 C ANISOU 3355 CG PHE D 67 9649 11831 7906 -179 -861 -144 C ATOM 3356 CD1 PHE D 67 3.843 -16.254 -9.443 1.00 88.21 C ANISOU 3356 CD1 PHE D 67 11141 13105 9267 -335 -1076 -24 C ATOM 3357 CD2 PHE D 67 2.670 -15.774 -11.460 1.00 84.99 C ANISOU 3357 CD2 PHE D 67 10599 12982 8711 -208 -561 -169 C ATOM 3358 CE1 PHE D 67 4.157 -14.914 -9.304 1.00 89.47 C ANISOU 3358 CE1 PHE D 67 11391 13346 9259 -514 -967 48 C ATOM 3359 CE2 PHE D 67 2.978 -14.433 -11.325 1.00 86.28 C ANISOU 3359 CE2 PHE D 67 10862 13205 8717 -378 -471 -82 C ATOM 3360 CZ PHE D 67 3.722 -14.003 -10.245 1.00 87.86 C ANISOU 3360 CZ PHE D 67 11173 13303 8908 -530 -661 17 C ATOM 3361 N THR D 68 1.542 -20.610 -9.036 1.00 72.52 N ANISOU 3361 N THR D 68 9503 10518 7534 -71 -1563 -29 N ATOM 3362 CA THR D 68 0.809 -21.874 -9.050 1.00 75.50 C ANISOU 3362 CA THR D 68 10016 10702 7969 -56 -1719 -17 C ATOM 3363 C THR D 68 -0.671 -21.558 -9.212 1.00 81.55 C ANISOU 3363 C THR D 68 10913 11587 8486 -195 -1386 48 C ATOM 3364 O THR D 68 -1.294 -21.011 -8.296 1.00 91.04 O ANISOU 3364 O THR D 68 12356 12793 9443 -425 -1260 198 O ATOM 3365 CB THR D 68 1.058 -22.678 -7.774 1.00 76.41 C ANISOU 3365 CB THR D 68 10447 10484 8100 -216 -2166 169 C ATOM 3366 OG1 THR D 68 2.451 -23.002 -7.676 1.00 98.79 O ANISOU 3366 OG1 THR D 68 13090 13184 11261 -38 -2545 98 O ATOM 3367 CG2 THR D 68 0.244 -23.963 -7.789 1.00 71.25 C ANISOU 3367 CG2 THR D 68 9988 9608 7477 -266 -2341 212 C ATOM 3368 N ILE D 69 -1.229 -21.900 -10.368 1.00 73.16 N ANISOU 3368 N ILE D 69 9682 10623 7494 -59 -1248 -86 N ATOM 3369 CA ILE D 69 -2.631 -21.643 -10.667 1.00 68.52 C ANISOU 3369 CA ILE D 69 9130 10154 6753 -161 -988 -37 C ATOM 3370 C ILE D 69 -3.437 -22.899 -10.366 1.00 67.57 C ANISOU 3370 C ILE D 69 9176 9845 6654 -296 -1168 40 C ATOM 3371 O ILE D 69 -2.963 -24.029 -10.532 1.00 67.87 O ANISOU 3371 O ILE D 69 9254 9668 6866 -211 -1481 -19 O ATOM 3372 CB ILE D 69 -2.817 -21.182 -12.130 1.00 77.19 C ANISOU 3372 CB ILE D 69 9990 11465 7876 4 -783 -189 C ATOM 3373 CG1 ILE D 69 -4.244 -20.682 -12.366 1.00 82.76 C ANISOU 3373 CG1 ILE D 69 10690 12286 8471 -86 -566 -113 C ATOM 3374 CG2 ILE D 69 -2.469 -22.300 -13.104 1.00 66.51 C ANISOU 3374 CG2 ILE D 69 8537 10041 6691 167 -945 -376 C ATOM 3375 CD1 ILE D 69 -4.473 -20.130 -13.756 1.00 57.53 C ANISOU 3375 CD1 ILE D 69 7334 9262 5262 29 -442 -209 C ATOM 3376 N SER D 70 -4.665 -22.697 -9.894 1.00 61.85 N ANISOU 3376 N SER D 70 8542 9189 5769 -517 -973 163 N ATOM 3377 CA SER D 70 -5.567 -23.795 -9.581 1.00 69.20 C ANISOU 3377 CA SER D 70 9624 9987 6682 -741 -1097 265 C ATOM 3378 C SER D 70 -6.995 -23.322 -9.805 1.00 77.55 C ANISOU 3378 C SER D 70 10528 11267 7672 -860 -768 289 C ATOM 3379 O SER D 70 -7.246 -22.143 -10.068 1.00 77.16 O ANISOU 3379 O SER D 70 10301 11421 7598 -747 -486 234 O ATOM 3380 CB SER D 70 -5.372 -24.290 -8.144 1.00 85.21 C ANISOU 3380 CB SER D 70 12014 11805 8559 -1036 -1292 452 C ATOM 3381 OG SER D 70 -5.637 -23.259 -7.210 1.00 90.44 O ANISOU 3381 OG SER D 70 12773 12612 8977 -1214 -995 523 O ATOM 3382 N ARG D 71 -7.937 -24.255 -9.698 1.00 86.13 N ANISOU 3382 N ARG D 71 11671 12294 8759 -1095 -838 375 N ATOM 3383 CA ARG D 71 -9.338 -23.916 -9.898 1.00 82.73 C ANISOU 3383 CA ARG D 71 11014 12086 8335 -1221 -555 392 C ATOM 3384 C ARG D 71 -10.217 -24.929 -9.181 1.00 85.45 C ANISOU 3384 C ARG D 71 11505 12364 8598 -1637 -604 544 C ATOM 3385 O ARG D 71 -9.813 -26.067 -8.929 1.00 80.48 O ANISOU 3385 O ARG D 71 11167 11465 7948 -1786 -952 633 O ATOM 3386 CB ARG D 71 -9.698 -23.857 -11.387 1.00 66.86 C ANISOU 3386 CB ARG D 71 8733 10167 6504 -995 -603 279 C ATOM 3387 CG ARG D 71 -9.584 -25.183 -12.117 1.00 65.65 C ANISOU 3387 CG ARG D 71 8687 9812 6445 -1009 -956 249 C ATOM 3388 CD ARG D 71 -10.019 -25.045 -13.567 1.00 82.38 C ANISOU 3388 CD ARG D 71 10595 12039 8667 -847 -988 137 C ATOM 3389 NE ARG D 71 -11.452 -24.791 -13.693 1.00 85.29 N ANISOU 3389 NE ARG D 71 10718 12588 9101 -1015 -858 222 N ATOM 3390 CZ ARG D 71 -12.068 -24.538 -14.844 1.00 83.48 C ANISOU 3390 CZ ARG D 71 10291 12463 8964 -929 -918 178 C ATOM 3391 NH1 ARG D 71 -11.375 -24.501 -15.974 1.00 74.01 N ANISOU 3391 NH1 ARG D 71 9172 11221 7727 -717 -1059 44 N ATOM 3392 NH2 ARG D 71 -13.376 -24.320 -14.865 1.00 77.62 N ANISOU 3392 NH2 ARG D 71 9265 11877 8350 -1076 -841 261 N ATOM 3393 N ASP D 72 -11.430 -24.488 -8.855 1.00 83.74 N ANISOU 3393 N ASP D 72 11074 12390 8355 -1832 -255 565 N ATOM 3394 CA ASP D 72 -12.461 -25.329 -8.256 1.00 93.16 C ANISOU 3394 CA ASP D 72 12312 13616 9470 -2294 -203 700 C ATOM 3395 C ASP D 72 -13.641 -25.361 -9.219 1.00 94.65 C ANISOU 3395 C ASP D 72 12066 13994 9903 -2272 -136 655 C ATOM 3396 O ASP D 72 -14.380 -24.377 -9.334 1.00 91.49 O ANISOU 3396 O ASP D 72 11282 13858 9623 -2154 201 561 O ATOM 3397 CB ASP D 72 -12.877 -24.798 -6.884 1.00105.16 C ANISOU 3397 CB ASP D 72 13924 15303 10731 -2608 209 737 C ATOM 3398 CG ASP D 72 -13.832 -25.728 -6.159 1.00118.29 C ANISOU 3398 CG ASP D 72 15689 17016 12240 -3188 290 893 C ATOM 3399 OD1 ASP D 72 -14.038 -26.866 -6.632 1.00123.23 O ANISOU 3399 OD1 ASP D 72 16393 17475 12953 -3358 -62 1010 O ATOM 3400 OD2 ASP D 72 -14.380 -25.320 -5.113 1.00122.47 O ANISOU 3400 OD2 ASP D 72 16242 17753 12539 -3503 719 886 O ATOM 3401 N ASN D 73 -13.814 -26.490 -9.911 1.00102.93 N ANISOU 3401 N ASN D 73 13184 14877 11050 -2378 -498 716 N ATOM 3402 CA ASN D 73 -14.863 -26.598 -10.920 1.00101.92 C ANISOU 3402 CA ASN D 73 12681 14891 11152 -2379 -539 690 C ATOM 3403 C ASN D 73 -16.261 -26.511 -10.324 1.00107.14 C ANISOU 3403 C ASN D 73 13002 15840 11867 -2752 -209 758 C ATOM 3404 O ASN D 73 -17.218 -26.248 -11.061 1.00101.90 O ANISOU 3404 O ASN D 73 11894 15364 11458 -2701 -178 719 O ATOM 3405 CB ASN D 73 -14.713 -27.907 -11.696 1.00 97.04 C ANISOU 3405 CB ASN D 73 12296 13991 10584 -2465 -1019 728 C ATOM 3406 CG ASN D 73 -13.408 -27.983 -12.464 1.00 96.74 C ANISOU 3406 CG ASN D 73 12489 13717 10551 -2054 -1288 582 C ATOM 3407 OD1 ASN D 73 -12.873 -26.965 -12.903 1.00101.08 O ANISOU 3407 OD1 ASN D 73 12895 14387 11122 -1695 -1139 455 O ATOM 3408 ND2 ASN D 73 -12.888 -29.193 -12.630 1.00108.40 N ANISOU 3408 ND2 ASN D 73 14318 14849 12019 -2115 -1682 585 N ATOM 3409 N ALA D 74 -16.404 -26.724 -9.015 1.00114.56 N ANISOU 3409 N ALA D 74 14129 16828 12571 -3146 34 852 N ATOM 3410 CA ALA D 74 -17.721 -26.643 -8.392 1.00118.98 C ANISOU 3410 CA ALA D 74 14330 17717 13162 -3542 441 875 C ATOM 3411 C ALA D 74 -18.216 -25.202 -8.341 1.00116.26 C ANISOU 3411 C ALA D 74 13488 17687 13000 -3221 912 668 C ATOM 3412 O ALA D 74 -19.372 -24.920 -8.680 1.00121.98 O ANISOU 3412 O ALA D 74 13644 18677 14026 -3240 1097 601 O ATOM 3413 CB ALA D 74 -17.677 -27.250 -6.990 1.00127.22 C ANISOU 3413 CB ALA D 74 15791 18730 13818 -4109 599 1026 C ATOM 3414 N LYS D 75 -17.355 -24.277 -7.924 1.00111.56 N ANISOU 3414 N LYS D 75 13089 17039 12259 -2918 1073 560 N ATOM 3415 CA LYS D 75 -17.717 -22.872 -7.798 1.00109.36 C ANISOU 3415 CA LYS D 75 12437 16977 12138 -2592 1488 346 C ATOM 3416 C LYS D 75 -17.286 -22.034 -8.994 1.00113.18 C ANISOU 3416 C LYS D 75 12764 17362 12877 -2024 1243 260 C ATOM 3417 O LYS D 75 -17.539 -20.824 -9.004 1.00115.51 O ANISOU 3417 O LYS D 75 12787 17762 13340 -1708 1493 94 O ATOM 3418 CB LYS D 75 -17.114 -22.286 -6.516 1.00102.60 C ANISOU 3418 CB LYS D 75 11941 16119 10924 -2675 1836 273 C ATOM 3419 N ASN D 76 -16.652 -22.644 -9.996 1.00113.88 N ANISOU 3419 N ASN D 76 13046 17238 12984 -1906 764 355 N ATOM 3420 CA ASN D 76 -16.160 -21.937 -11.180 1.00110.51 C ANISOU 3420 CA ASN D 76 12557 16725 12709 -1457 525 292 C ATOM 3421 C ASN D 76 -15.248 -20.777 -10.788 1.00103.80 C ANISOU 3421 C ASN D 76 11887 15824 11730 -1171 700 193 C ATOM 3422 O ASN D 76 -15.390 -19.647 -11.260 1.00110.50 O ANISOU 3422 O ASN D 76 12529 16711 12747 -853 759 101 O ATOM 3423 CB ASN D 76 -17.319 -21.458 -12.057 1.00106.10 C ANISOU 3423 CB ASN D 76 11470 16319 12525 -1308 485 252 C ATOM 3424 CG ASN D 76 -18.001 -22.595 -12.792 1.00105.96 C ANISOU 3424 CG ASN D 76 11332 16297 12632 -1555 160 366 C ATOM 3425 OD1 ASN D 76 -19.205 -22.809 -12.650 1.00107.59 O ANISOU 3425 OD1 ASN D 76 11119 16693 13067 -1770 264 386 O ATOM 3426 ND2 ASN D 76 -17.232 -23.332 -13.585 1.00100.62 N ANISOU 3426 ND2 ASN D 76 11011 15406 11815 -1536 -228 417 N ATOM 3427 N THR D 77 -14.298 -21.072 -9.905 1.00 85.31 N ANISOU 3427 N THR D 77 9963 13362 9090 -1310 729 230 N ATOM 3428 CA THR D 77 -13.337 -20.097 -9.416 1.00 80.16 C ANISOU 3428 CA THR D 77 9538 12641 8278 -1120 850 159 C ATOM 3429 C THR D 77 -11.930 -20.554 -9.774 1.00 71.65 C ANISOU 3429 C THR D 77 8798 11354 7072 -1035 502 216 C ATOM 3430 O THR D 77 -11.663 -21.754 -9.886 1.00 69.33 O ANISOU 3430 O THR D 77 8668 10933 6741 -1193 234 302 O ATOM 3431 CB THR D 77 -13.462 -19.911 -7.894 1.00 80.62 C ANISOU 3431 CB THR D 77 9784 12758 8088 -1390 1211 133 C ATOM 3432 OG1 THR D 77 -14.846 -19.818 -7.536 1.00 82.51 O ANISOU 3432 OG1 THR D 77 9661 13231 8460 -1546 1571 55 O ATOM 3433 CG2 THR D 77 -12.751 -18.643 -7.441 1.00 70.69 C ANISOU 3433 CG2 THR D 77 8695 11452 6714 -1175 1375 21 C ATOM 3434 N VAL D 78 -11.032 -19.590 -9.966 1.00 64.39 N ANISOU 3434 N VAL D 78 7964 10390 6113 -783 501 154 N ATOM 3435 CA VAL D 78 -9.635 -19.860 -10.284 1.00 65.47 C ANISOU 3435 CA VAL D 78 8328 10379 6170 -682 231 167 C ATOM 3436 C VAL D 78 -8.759 -19.075 -9.319 1.00 75.09 C ANISOU 3436 C VAL D 78 9780 11544 7208 -689 335 159 C ATOM 3437 O VAL D 78 -8.970 -17.874 -9.118 1.00 70.21 O ANISOU 3437 O VAL D 78 9113 10991 6574 -587 565 92 O ATOM 3438 CB VAL D 78 -9.298 -19.501 -11.743 1.00 78.30 C ANISOU 3438 CB VAL D 78 9803 12030 7917 -418 83 104 C ATOM 3439 CG1 VAL D 78 -7.794 -19.483 -11.957 1.00 80.37 C ANISOU 3439 CG1 VAL D 78 10227 12208 8104 -309 -71 65 C ATOM 3440 CG2 VAL D 78 -9.944 -20.496 -12.679 1.00 83.11 C ANISOU 3440 CG2 VAL D 78 10290 12641 8648 -456 -108 112 C ATOM 3441 N TYR D 79 -7.781 -19.753 -8.726 1.00 84.52 N ANISOU 3441 N TYR D 79 11242 12585 8285 -807 118 225 N ATOM 3442 CA TYR D 79 -6.882 -19.160 -7.746 1.00 82.96 C ANISOU 3442 CA TYR D 79 11306 12310 7905 -873 125 248 C ATOM 3443 C TYR D 79 -5.469 -19.127 -8.310 1.00 83.24 C ANISOU 3443 C TYR D 79 11333 12265 8029 -685 -148 224 C ATOM 3444 O TYR D 79 -4.981 -20.134 -8.833 1.00 95.20 O ANISOU 3444 O TYR D 79 12803 13688 9680 -620 -419 219 O ATOM 3445 CB TYR D 79 -6.913 -19.946 -6.434 1.00 77.86 C ANISOU 3445 CB TYR D 79 11000 11542 7043 -1225 49 372 C ATOM 3446 CG TYR D 79 -8.309 -20.221 -5.922 1.00 76.45 C ANISOU 3446 CG TYR D 79 10796 11483 6767 -1488 344 389 C ATOM 3447 CD1 TYR D 79 -8.968 -19.304 -5.114 1.00 89.41 C ANISOU 3447 CD1 TYR D 79 12473 13261 8236 -1601 766 302 C ATOM 3448 CD2 TYR D 79 -8.969 -21.399 -6.249 1.00 77.02 C ANISOU 3448 CD2 TYR D 79 10795 11538 6931 -1636 217 466 C ATOM 3449 CE1 TYR D 79 -10.245 -19.552 -4.646 1.00 99.06 C ANISOU 3449 CE1 TYR D 79 13596 14646 9395 -1853 1100 276 C ATOM 3450 CE2 TYR D 79 -10.246 -21.656 -5.786 1.00 95.47 C ANISOU 3450 CE2 TYR D 79 13055 14026 9193 -1930 506 485 C ATOM 3451 CZ TYR D 79 -10.879 -20.729 -4.985 1.00100.47 C ANISOU 3451 CZ TYR D 79 13661 14841 9671 -2036 971 382 C ATOM 3452 OH TYR D 79 -12.150 -20.980 -4.521 1.00 96.69 O ANISOU 3452 OH TYR D 79 13034 14563 9142 -2339 1322 361 O ATOM 3453 N LEU D 80 -4.818 -17.971 -8.206 1.00 77.77 N ANISOU 3453 N LEU D 80 10670 11605 7275 -606 -67 188 N ATOM 3454 CA LEU D 80 -3.441 -17.788 -8.656 1.00 75.70 C ANISOU 3454 CA LEU D 80 10350 11319 7095 -481 -271 160 C ATOM 3455 C LEU D 80 -2.577 -17.526 -7.427 1.00 91.84 C ANISOU 3455 C LEU D 80 12665 13236 8993 -649 -412 240 C ATOM 3456 O LEU D 80 -2.565 -16.414 -6.891 1.00 96.23 O ANISOU 3456 O LEU D 80 13370 13807 9388 -720 -252 239 O ATOM 3457 CB LEU D 80 -3.338 -16.646 -9.663 1.00 71.82 C ANISOU 3457 CB LEU D 80 9683 10965 6639 -318 -115 85 C ATOM 3458 CG LEU D 80 -1.945 -16.404 -10.250 1.00 70.43 C ANISOU 3458 CG LEU D 80 9392 10836 6533 -244 -252 40 C ATOM 3459 CD1 LEU D 80 -1.524 -17.565 -11.141 1.00 57.24 C ANISOU 3459 CD1 LEU D 80 7517 9192 5041 -119 -404 -57 C ATOM 3460 CD2 LEU D 80 -1.894 -15.088 -11.011 1.00 77.32 C ANISOU 3460 CD2 LEU D 80 10211 11821 7347 -200 -93 19 C ATOM 3461 N ALA D 81 -1.858 -18.553 -6.983 1.00 96.05 N ANISOU 3461 N ALA D 81 13290 13610 9593 -714 -757 308 N ATOM 3462 CA ALA D 81 -0.981 -18.449 -5.822 1.00 76.78 C ANISOU 3462 CA ALA D 81 11126 11014 7033 -899 -1010 417 C ATOM 3463 C ALA D 81 0.378 -17.931 -6.280 1.00 81.31 C ANISOU 3463 C ALA D 81 11477 11631 7788 -753 -1174 361 C ATOM 3464 O ALA D 81 1.160 -18.670 -6.888 1.00 77.68 O ANISOU 3464 O ALA D 81 10754 11146 7614 -576 -1412 295 O ATOM 3465 CB ALA D 81 -0.850 -19.797 -5.120 1.00 81.40 C ANISOU 3465 CB ALA D 81 11932 11360 7636 -1048 -1392 546 C ATOM 3466 N MET D 82 0.656 -16.664 -5.992 1.00 81.15 N ANISOU 3466 N MET D 82 11548 11674 7613 -837 -1036 367 N ATOM 3467 CA MET D 82 1.915 -16.031 -6.360 1.00 79.68 C ANISOU 3467 CA MET D 82 11154 11556 7563 -786 -1163 336 C ATOM 3468 C MET D 82 2.881 -16.098 -5.185 1.00 81.93 C ANISOU 3468 C MET D 82 11658 11661 7809 -986 -1557 464 C ATOM 3469 O MET D 82 2.531 -15.712 -4.065 1.00 69.73 O ANISOU 3469 O MET D 82 10549 9992 5955 -1235 -1559 563 O ATOM 3470 CB MET D 82 1.689 -14.578 -6.783 1.00 83.05 C ANISOU 3470 CB MET D 82 11593 12114 7848 -798 -851 292 C ATOM 3471 CG MET D 82 0.772 -14.421 -7.987 1.00 94.66 C ANISOU 3471 CG MET D 82 12868 13734 9364 -614 -547 196 C ATOM 3472 SD MET D 82 0.639 -12.718 -8.568 1.00 98.23 S ANISOU 3472 SD MET D 82 13367 14262 9694 -627 -311 178 S ATOM 3473 CE MET D 82 -0.123 -11.929 -7.154 1.00 94.00 C ANISOU 3473 CE MET D 82 13283 13535 8897 -767 -188 202 C ATOM 3474 N ALA D 83 4.090 -16.594 -5.443 1.00 90.84 N ANISOU 3474 N ALA D 83 12479 12778 9258 -884 -1894 445 N ATOM 3475 CA ALA D 83 5.116 -16.716 -4.418 1.00 86.59 C ANISOU 3475 CA ALA D 83 12074 12055 8772 -1052 -2375 579 C ATOM 3476 C ALA D 83 6.444 -16.231 -4.978 1.00100.05 C ANISOU 3476 C ALA D 83 13321 13914 10778 -976 -2494 503 C ATOM 3477 O ALA D 83 6.675 -16.273 -6.190 1.00113.58 O ANISOU 3477 O ALA D 83 14578 15854 12722 -757 -2265 326 O ATOM 3478 CB ALA D 83 5.250 -18.161 -3.918 1.00 80.91 C ANISOU 3478 CB ALA D 83 11434 11073 8234 -1010 -2831 660 C ATOM 3479 N SER D 84 7.316 -15.774 -4.078 1.00100.25 N ANISOU 3479 N SER D 84 13481 13831 10778 -1202 -2851 637 N ATOM 3480 CA SER D 84 8.617 -15.215 -4.443 1.00 99.26 C ANISOU 3480 CA SER D 84 12916 13866 10933 -1218 -2989 592 C ATOM 3481 C SER D 84 8.455 -14.080 -5.452 1.00 92.04 C ANISOU 3481 C SER D 84 11835 13245 9892 -1236 -2482 484 C ATOM 3482 O SER D 84 9.044 -14.082 -6.535 1.00 94.21 O ANISOU 3482 O SER D 84 11585 13778 10434 -1099 -2317 330 O ATOM 3483 CB SER D 84 9.553 -16.300 -4.979 1.00104.96 C ANISOU 3483 CB SER D 84 13040 14617 12222 -926 -3277 460 C ATOM 3484 OG SER D 84 10.800 -15.752 -5.368 1.00116.72 O ANISOU 3484 OG SER D 84 14015 16324 14010 -961 -3346 386 O ATOM 3485 N LEU D 85 7.637 -13.098 -5.081 1.00 83.84 N ANISOU 3485 N LEU D 85 11274 12150 8432 -1421 -2236 556 N ATOM 3486 CA LEU D 85 7.311 -12.007 -5.988 1.00 80.54 C ANISOU 3486 CA LEU D 85 10810 11921 7871 -1440 -1818 488 C ATOM 3487 C LEU D 85 8.521 -11.115 -6.231 1.00 86.74 C ANISOU 3487 C LEU D 85 11355 12849 8753 -1652 -1918 517 C ATOM 3488 O LEU D 85 9.276 -10.793 -5.310 1.00 74.21 O ANISOU 3488 O LEU D 85 9903 11138 7154 -1889 -2272 636 O ATOM 3489 CB LEU D 85 6.151 -11.183 -5.430 1.00 79.02 C ANISOU 3489 CB LEU D 85 11183 11569 7271 -1542 -1586 529 C ATOM 3490 CG LEU D 85 4.780 -11.856 -5.501 1.00 86.98 C ANISOU 3490 CG LEU D 85 12327 12533 8190 -1349 -1339 470 C ATOM 3491 CD1 LEU D 85 3.716 -10.995 -4.843 1.00 83.17 C ANISOU 3491 CD1 LEU D 85 12331 11910 7360 -1443 -1094 462 C ATOM 3492 CD2 LEU D 85 4.414 -12.146 -6.948 1.00108.50 C ANISOU 3492 CD2 LEU D 85 14661 15472 11093 -1102 -1075 353 C ATOM 3493 N LYS D 86 8.698 -10.718 -7.485 1.00101.55 N ANISOU 3493 N LYS D 86 12894 14992 10700 -1615 -1617 420 N ATOM 3494 CA LYS D 86 9.777 -9.853 -7.927 1.00 95.10 C ANISOU 3494 CA LYS D 86 11810 14376 9949 -1870 -1623 442 C ATOM 3495 C LYS D 86 9.235 -8.486 -8.326 1.00 97.54 C ANISOU 3495 C LYS D 86 12487 14661 9911 -2067 -1369 512 C ATOM 3496 O LYS D 86 8.047 -8.345 -8.638 1.00 97.90 O ANISOU 3496 O LYS D 86 12818 14616 9765 -1911 -1128 487 O ATOM 3497 CB LYS D 86 10.514 -10.483 -9.118 1.00 80.31 C ANISOU 3497 CB LYS D 86 9256 12855 8405 -1738 -1457 258 C ATOM 3498 CG LYS D 86 11.142 -11.833 -8.818 1.00 92.41 C ANISOU 3498 CG LYS D 86 10364 14375 10373 -1485 -1741 144 C ATOM 3499 CD LYS D 86 11.826 -12.405 -10.049 1.00 99.15 C ANISOU 3499 CD LYS D 86 10539 15584 11549 -1322 -1493 -118 C ATOM 3500 CE LYS D 86 12.408 -13.781 -9.770 1.00116.13 C ANISOU 3500 CE LYS D 86 12265 17657 14202 -993 -1807 -275 C ATOM 3501 NZ LYS D 86 13.044 -14.369 -10.981 1.00128.78 N ANISOU 3501 NZ LYS D 86 13199 19602 16130 -791 -1505 -611 N ATOM 3502 N PRO D 87 10.077 -7.448 -8.322 1.00101.55 N ANISOU 3502 N PRO D 87 12999 15224 10360 -2418 -1459 609 N ATOM 3503 CA PRO D 87 9.605 -6.127 -8.769 1.00108.94 C ANISOU 3503 CA PRO D 87 14322 16083 10987 -2615 -1276 688 C ATOM 3504 C PRO D 87 9.186 -6.093 -10.228 1.00111.99 C ANISOU 3504 C PRO D 87 14526 16695 11329 -2531 -923 620 C ATOM 3505 O PRO D 87 8.492 -5.153 -10.635 1.00112.67 O ANISOU 3505 O PRO D 87 14997 16644 11171 -2602 -809 691 O ATOM 3506 CB PRO D 87 10.811 -5.213 -8.507 1.00103.70 C ANISOU 3506 CB PRO D 87 13619 15462 10319 -3062 -1500 814 C ATOM 3507 CG PRO D 87 11.986 -6.134 -8.449 1.00 97.41 C ANISOU 3507 CG PRO D 87 12170 14928 9912 -3060 -1674 752 C ATOM 3508 CD PRO D 87 11.469 -7.401 -7.842 1.00 96.82 C ANISOU 3508 CD PRO D 87 12083 14717 9989 -2671 -1789 668 C ATOM 3509 N GLU D 88 9.583 -7.083 -11.031 1.00113.06 N ANISOU 3509 N GLU D 88 14121 17145 11692 -2382 -774 474 N ATOM 3510 CA GLU D 88 9.139 -7.144 -12.417 1.00104.13 C ANISOU 3510 CA GLU D 88 12881 16226 10457 -2325 -442 393 C ATOM 3511 C GLU D 88 7.682 -7.571 -12.539 1.00 96.41 C ANISOU 3511 C GLU D 88 12187 15059 9387 -1983 -345 357 C ATOM 3512 O GLU D 88 7.056 -7.304 -13.570 1.00112.82 O ANISOU 3512 O GLU D 88 14368 17199 11301 -1976 -153 358 O ATOM 3513 CB GLU D 88 10.026 -8.101 -13.219 1.00105.44 C ANISOU 3513 CB GLU D 88 12395 16786 10882 -2268 -277 186 C ATOM 3514 CG GLU D 88 11.453 -7.614 -13.443 1.00123.50 C ANISOU 3514 CG GLU D 88 14275 19376 13275 -2651 -262 186 C ATOM 3515 CD GLU D 88 12.348 -7.815 -12.233 1.00129.14 C ANISOU 3515 CD GLU D 88 14772 19999 14295 -2681 -638 225 C ATOM 3516 OE1 GLU D 88 11.867 -8.349 -11.212 1.00130.80 O ANISOU 3516 OE1 GLU D 88 15210 19899 14587 -2426 -912 261 O ATOM 3517 OE2 GLU D 88 13.537 -7.440 -12.306 1.00134.09 O ANISOU 3517 OE2 GLU D 88 15003 20871 15072 -2998 -676 231 O ATOM 3518 N ASP D 89 7.131 -8.221 -11.515 1.00 83.92 N ANISOU 3518 N ASP D 89 10739 13252 7895 -1740 -491 340 N ATOM 3519 CA ASP D 89 5.750 -8.687 -11.545 1.00 79.93 C ANISOU 3519 CA ASP D 89 10439 12596 7334 -1449 -390 301 C ATOM 3520 C ASP D 89 4.739 -7.584 -11.264 1.00 70.04 C ANISOU 3520 C ASP D 89 9674 11079 5860 -1469 -359 397 C ATOM 3521 O ASP D 89 3.538 -7.870 -11.209 1.00 64.68 O ANISOU 3521 O ASP D 89 9128 10279 5168 -1235 -270 358 O ATOM 3522 CB ASP D 89 5.557 -9.824 -10.537 1.00 97.09 C ANISOU 3522 CB ASP D 89 12584 14643 9661 -1252 -545 254 C ATOM 3523 CG ASP D 89 6.325 -11.075 -10.915 1.00112.31 C ANISOU 3523 CG ASP D 89 14034 16758 11880 -1116 -604 118 C ATOM 3524 OD1 ASP D 89 6.958 -11.084 -11.991 1.00117.79 O ANISOU 3524 OD1 ASP D 89 14385 17724 12646 -1158 -448 15 O ATOM 3525 OD2 ASP D 89 6.294 -12.050 -10.135 1.00112.56 O ANISOU 3525 OD2 ASP D 89 14053 16652 12062 -978 -808 103 O ATOM 3526 N THR D 90 5.185 -6.342 -11.085 1.00 66.28 N ANISOU 3526 N THR D 90 9447 10496 5240 -1735 -440 506 N ATOM 3527 CA THR D 90 4.274 -5.231 -10.829 1.00 70.31 C ANISOU 3527 CA THR D 90 10431 10698 5586 -1716 -440 560 C ATOM 3528 C THR D 90 3.469 -4.937 -12.089 1.00 79.64 C ANISOU 3528 C THR D 90 11631 11904 6726 -1614 -321 581 C ATOM 3529 O THR D 90 3.993 -4.368 -13.052 1.00 85.01 O ANISOU 3529 O THR D 90 12297 12700 7303 -1857 -326 674 O ATOM 3530 CB THR D 90 5.053 -3.998 -10.381 1.00 68.75 C ANISOU 3530 CB THR D 90 10529 10343 5249 -2056 -610 672 C ATOM 3531 OG1 THR D 90 5.802 -4.306 -9.199 1.00 74.54 O ANISOU 3531 OG1 THR D 90 11263 11045 6015 -2175 -782 668 O ATOM 3532 CG2 THR D 90 4.102 -2.847 -10.084 1.00 70.03 C ANISOU 3532 CG2 THR D 90 11209 10120 5281 -1983 -629 681 C ATOM 3533 N ALA D 91 2.196 -5.324 -12.084 1.00 69.75 N ANISOU 3533 N ALA D 91 10416 10545 5541 -1298 -234 508 N ATOM 3534 CA ALA D 91 1.324 -5.119 -13.232 1.00 66.59 C ANISOU 3534 CA ALA D 91 10031 10135 5134 -1179 -198 539 C ATOM 3535 C ALA D 91 -0.121 -5.273 -12.780 1.00 69.69 C ANISOU 3535 C ALA D 91 10496 10331 5654 -838 -143 452 C ATOM 3536 O ALA D 91 -0.401 -5.627 -11.632 1.00 69.61 O ANISOU 3536 O ALA D 91 10517 10241 5691 -731 -72 355 O ATOM 3537 CB ALA D 91 1.650 -6.099 -14.364 1.00 71.41 C ANISOU 3537 CB ALA D 91 10292 11084 5756 -1205 -106 508 C ATOM 3538 N VAL D 92 -1.037 -4.998 -13.702 1.00 74.27 N ANISOU 3538 N VAL D 92 11097 10841 6282 -701 -184 490 N ATOM 3539 CA VAL D 92 -2.465 -5.188 -13.479 1.00 70.25 C ANISOU 3539 CA VAL D 92 10536 10195 5961 -372 -134 398 C ATOM 3540 C VAL D 92 -2.847 -6.550 -14.039 1.00 61.44 C ANISOU 3540 C VAL D 92 9081 9336 4927 -275 -60 357 C ATOM 3541 O VAL D 92 -2.690 -6.803 -15.239 1.00 81.10 O ANISOU 3541 O VAL D 92 11489 11975 7352 -360 -130 425 O ATOM 3542 CB VAL D 92 -3.293 -4.069 -14.129 1.00 72.24 C ANISOU 3542 CB VAL D 92 10990 10168 6291 -252 -313 471 C ATOM 3543 CG1 VAL D 92 -4.779 -4.350 -13.969 1.00 65.95 C ANISOU 3543 CG1 VAL D 92 10010 9279 5770 108 -260 353 C ATOM 3544 CG2 VAL D 92 -2.933 -2.728 -13.517 1.00 67.76 C ANISOU 3544 CG2 VAL D 92 10812 9280 5655 -336 -413 489 C ATOM 3545 N TYR D 93 -3.345 -7.427 -13.174 1.00 67.21 N ANISOU 3545 N TYR D 93 9663 10108 5765 -138 78 243 N ATOM 3546 CA TYR D 93 -3.663 -8.798 -13.544 1.00 71.22 C ANISOU 3546 CA TYR D 93 9893 10815 6352 -74 121 201 C ATOM 3547 C TYR D 93 -5.139 -8.911 -13.904 1.00 80.14 C ANISOU 3547 C TYR D 93 10893 11888 7667 138 119 178 C ATOM 3548 O TYR D 93 -6.008 -8.530 -13.114 1.00 67.42 O ANISOU 3548 O TYR D 93 9293 10142 6183 284 221 102 O ATOM 3549 CB TYR D 93 -3.309 -9.761 -12.410 1.00 63.45 C ANISOU 3549 CB TYR D 93 8854 9887 5366 -114 209 131 C ATOM 3550 CG TYR D 93 -1.820 -9.979 -12.259 1.00 61.80 C ANISOU 3550 CG TYR D 93 8646 9774 5063 -297 135 154 C ATOM 3551 CD1 TYR D 93 -1.009 -9.006 -11.688 1.00 60.39 C ANISOU 3551 CD1 TYR D 93 8674 9500 4773 -453 89 198 C ATOM 3552 CD2 TYR D 93 -1.224 -11.155 -12.694 1.00 67.21 C ANISOU 3552 CD2 TYR D 93 9101 10630 5805 -307 92 111 C ATOM 3553 CE1 TYR D 93 0.353 -9.199 -11.553 1.00 64.12 C ANISOU 3553 CE1 TYR D 93 9071 10078 5214 -631 -6 221 C ATOM 3554 CE2 TYR D 93 0.137 -11.358 -12.562 1.00 71.36 C ANISOU 3554 CE2 TYR D 93 9537 11248 6329 -433 16 99 C ATOM 3555 CZ TYR D 93 0.920 -10.377 -11.991 1.00 69.26 C ANISOU 3555 CZ TYR D 93 9424 10918 5973 -603 -36 164 C ATOM 3556 OH TYR D 93 2.275 -10.574 -11.858 1.00 74.82 O ANISOU 3556 OH TYR D 93 9968 11733 6728 -740 -138 154 O ATOM 3557 N TYR D 94 -5.411 -9.431 -15.097 1.00 87.27 N ANISOU 3557 N TYR D 94 11664 12907 8589 142 8 223 N ATOM 3558 CA TYR D 94 -6.762 -9.583 -15.611 1.00 75.39 C ANISOU 3558 CA TYR D 94 10003 11361 7280 310 -76 230 C ATOM 3559 C TYR D 94 -7.160 -11.053 -15.610 1.00 72.56 C ANISOU 3559 C TYR D 94 9413 11166 6991 312 -23 170 C ATOM 3560 O TYR D 94 -6.328 -11.940 -15.825 1.00 74.44 O ANISOU 3560 O TYR D 94 9641 11540 7105 196 -11 141 O ATOM 3561 CB TYR D 94 -6.881 -9.019 -17.030 1.00 61.89 C ANISOU 3561 CB TYR D 94 8397 9613 5506 263 -329 359 C ATOM 3562 CG TYR D 94 -6.504 -7.560 -17.152 1.00 63.56 C ANISOU 3562 CG TYR D 94 8898 9616 5634 213 -453 459 C ATOM 3563 CD1 TYR D 94 -7.467 -6.564 -17.059 1.00 66.01 C ANISOU 3563 CD1 TYR D 94 9263 9645 6173 424 -610 486 C ATOM 3564 CD2 TYR D 94 -5.185 -7.179 -17.363 1.00 63.27 C ANISOU 3564 CD2 TYR D 94 9068 9649 5322 -50 -430 519 C ATOM 3565 CE1 TYR D 94 -7.127 -5.229 -17.170 1.00 75.02 C ANISOU 3565 CE1 TYR D 94 10730 10527 7250 376 -780 583 C ATOM 3566 CE2 TYR D 94 -4.835 -5.847 -17.475 1.00 69.39 C ANISOU 3566 CE2 TYR D 94 10152 10212 6002 -156 -573 636 C ATOM 3567 CZ TYR D 94 -5.810 -4.876 -17.378 1.00 79.89 C ANISOU 3567 CZ TYR D 94 11604 11210 7542 58 -768 675 C ATOM 3568 OH TYR D 94 -5.467 -3.548 -17.490 1.00 86.93 O ANISOU 3568 OH TYR D 94 12859 11822 8349 -48 -965 796 O ATOM 3569 N CYS D 95 -8.442 -11.302 -15.369 1.00 79.60 N ANISOU 3569 N CYS D 95 10104 12030 8111 445 -1 138 N ATOM 3570 CA CYS D 95 -8.996 -12.649 -15.372 1.00 86.94 C ANISOU 3570 CA CYS D 95 10831 13083 9121 407 15 105 C ATOM 3571 C CYS D 95 -9.773 -12.873 -16.662 1.00 87.01 C ANISOU 3571 C CYS D 95 10718 13115 9227 435 -231 171 C ATOM 3572 O CYS D 95 -10.590 -12.034 -17.054 1.00102.10 O ANISOU 3572 O CYS D 95 12556 14922 11314 564 -371 223 O ATOM 3573 CB CYS D 95 -9.904 -12.869 -14.161 1.00 95.80 C ANISOU 3573 CB CYS D 95 11790 14204 10405 446 234 27 C ATOM 3574 SG CYS D 95 -10.605 -14.530 -14.051 1.00106.36 S ANISOU 3574 SG CYS D 95 12920 15674 11820 309 239 24 S ATOM 3575 N ALA D 96 -9.515 -14.002 -17.316 1.00 75.23 N ANISOU 3575 N ALA D 96 9225 11728 7632 319 -321 161 N ATOM 3576 CA ALA D 96 -10.163 -14.346 -18.572 1.00 67.11 C ANISOU 3576 CA ALA D 96 8152 10720 6625 286 -581 216 C ATOM 3577 C ALA D 96 -10.801 -15.722 -18.459 1.00 62.09 C ANISOU 3577 C ALA D 96 7350 10145 6097 218 -608 173 C ATOM 3578 O ALA D 96 -10.337 -16.579 -17.703 1.00 62.06 O ANISOU 3578 O ALA D 96 7363 10166 6051 157 -463 101 O ATOM 3579 CB ALA D 96 -9.171 -14.323 -19.740 1.00 65.42 C ANISOU 3579 CB ALA D 96 8191 10564 6101 156 -681 218 C ATOM 3580 N ALA D 97 -11.872 -15.927 -19.223 1.00 80.33 N ANISOU 3580 N ALA D 97 9521 12450 8550 204 -849 237 N ATOM 3581 CA ALA D 97 -12.609 -17.181 -19.180 1.00 84.97 C ANISOU 3581 CA ALA D 97 9950 13079 9256 94 -922 221 C ATOM 3582 C ALA D 97 -13.293 -17.417 -20.518 1.00 85.79 C ANISOU 3582 C ALA D 97 10059 13170 9367 16 -1291 293 C ATOM 3583 O ALA D 97 -13.670 -16.472 -21.216 1.00 84.34 O ANISOU 3583 O ALA D 97 9882 12933 9231 82 -1506 393 O ATOM 3584 CB ALA D 97 -13.642 -17.185 -18.048 1.00 79.37 C ANISOU 3584 CB ALA D 97 8906 12404 8849 121 -748 226 C ATOM 3585 N VAL D 98 -13.450 -18.692 -20.865 1.00 83.95 N ANISOU 3585 N VAL D 98 9868 12949 9079 -142 -1410 249 N ATOM 3586 CA VAL D 98 -14.116 -19.113 -22.093 1.00 87.29 C ANISOU 3586 CA VAL D 98 10345 13349 9473 -273 -1787 304 C ATOM 3587 C VAL D 98 -15.339 -19.931 -21.705 1.00 93.09 C ANISOU 3587 C VAL D 98 10761 14099 10510 -388 -1899 356 C ATOM 3588 O VAL D 98 -15.217 -20.940 -20.999 1.00 88.06 O ANISOU 3588 O VAL D 98 10122 13460 9876 -495 -1756 292 O ATOM 3589 CB VAL D 98 -13.181 -19.925 -23.003 1.00 76.85 C ANISOU 3589 CB VAL D 98 9411 12012 7776 -397 -1846 165 C ATOM 3590 CG1 VAL D 98 -13.937 -20.428 -24.224 1.00 72.70 C ANISOU 3590 CG1 VAL D 98 9002 11446 7176 -579 -2251 211 C ATOM 3591 CG2 VAL D 98 -11.983 -19.086 -23.419 1.00 71.21 C ANISOU 3591 CG2 VAL D 98 8954 11341 6761 -341 -1691 109 C ATOM 3592 N ALA D 99 -16.512 -19.502 -22.166 1.00 62.72 N ANISOU 3592 N ALA D 99 7791 7793 8246 -255 -1646 418 N ATOM 3593 CA ALA D 99 -17.761 -20.181 -21.850 1.00 65.47 C ANISOU 3593 CA ALA D 99 7982 8512 8380 -165 -1357 138 C ATOM 3594 C ALA D 99 -18.631 -20.245 -23.095 1.00 59.33 C ANISOU 3594 C ALA D 99 6720 8374 7449 -88 -1202 93 C ATOM 3595 O ALA D 99 -18.861 -19.222 -23.746 1.00 67.56 O ANISOU 3595 O ALA D 99 7731 9549 8390 150 -1293 263 O ATOM 3596 CB ALA D 99 -18.509 -19.469 -20.717 1.00 63.57 C ANISOU 3596 CB ALA D 99 8142 8076 7934 210 -1373 113 C ATOM 3597 N TYR D 100 -19.118 -21.458 -23.422 1.00 57.22 N ANISOU 3597 N TYR D 100 6098 8468 7176 -296 -1025 -132 N ATOM 3598 CA TYR D 100 -19.969 -21.681 -24.579 1.00 68.63 C ANISOU 3598 CA TYR D 100 7100 10494 8482 -255 -956 -223 C ATOM 3599 C TYR D 100 -21.426 -21.836 -24.156 1.00 74.41 C ANISOU 3599 C TYR D 100 7619 11554 9100 -147 -807 -293 C ATOM 3600 O TYR D 100 -21.714 -22.315 -23.055 1.00 83.49 O ANISOU 3600 O TYR D 100 8864 12556 10304 -216 -692 -319 O ATOM 3601 CB TYR D 100 -19.532 -22.936 -25.342 1.00 63.52 C ANISOU 3601 CB TYR D 100 6222 9998 7914 -539 -972 -430 C ATOM 3602 CG TYR D 100 -18.095 -22.910 -25.815 1.00 59.40 C ANISOU 3602 CG TYR D 100 5815 9277 7477 -588 -1052 -310 C ATOM 3603 CD1 TYR D 100 -17.738 -22.242 -26.979 1.00 76.79 C ANISOU 3603 CD1 TYR D 100 7875 11755 9546 -395 -1090 -114 C ATOM 3604 CD2 TYR D 100 -17.098 -23.565 -25.103 1.00 44.20 C ANISOU 3604 CD2 TYR D 100 4098 6934 5762 -807 -1074 -334 C ATOM 3605 CE1 TYR D 100 -16.426 -22.219 -27.417 1.00 73.33 C ANISOU 3605 CE1 TYR D 100 7452 11222 9187 -409 -1117 106 C ATOM 3606 CE2 TYR D 100 -15.784 -23.549 -25.534 1.00 57.60 C ANISOU 3606 CE2 TYR D 100 5820 8512 7553 -827 -1127 -152 C ATOM 3607 CZ TYR D 100 -15.454 -22.874 -26.691 1.00 68.69 C ANISOU 3607 CZ TYR D 100 7033 10238 8827 -623 -1133 93 C ATOM 3608 OH TYR D 100 -14.147 -22.855 -27.123 1.00 63.71 O ANISOU 3608 OH TYR D 100 6343 9572 8291 -614 -1142 380 O ATOM 3609 N PRO D 101 -22.371 -21.431 -25.009 1.00 80.89 N ANISOU 3609 N PRO D 101 8115 12860 9760 41 -796 -269 N ATOM 3610 CA PRO D 101 -23.791 -21.629 -24.685 1.00 76.75 C ANISOU 3610 CA PRO D 101 7265 12733 9165 131 -654 -259 C ATOM 3611 C PRO D 101 -24.218 -23.080 -24.840 1.00 78.52 C ANISOU 3611 C PRO D 101 7119 13146 9571 -289 -674 -423 C ATOM 3612 O PRO D 101 -23.395 -23.947 -25.153 1.00 72.09 O ANISOU 3612 O PRO D 101 6380 12112 8897 -597 -799 -607 O ATOM 3613 CB PRO D 101 -24.516 -20.723 -25.692 1.00 67.55 C ANISOU 3613 CB PRO D 101 5863 12004 7798 447 -704 -168 C ATOM 3614 CG PRO D 101 -23.451 -19.828 -26.271 1.00 77.36 C ANISOU 3614 CG PRO D 101 7417 12985 8993 579 -848 -70 C ATOM 3615 CD PRO D 101 -22.193 -20.628 -26.228 1.00 77.34 C ANISOU 3615 CD PRO D 101 7580 12629 9177 231 -909 -168 C ATOM 3616 N ASP D 102 -25.502 -23.357 -24.626 1.00 82.43 N ANISOU 3616 N ASP D 102 7203 14036 10081 -292 -583 -325 N ATOM 3617 CA ASP D 102 -26.013 -24.707 -24.816 1.00 86.00 C ANISOU 3617 CA ASP D 102 7265 14633 10776 -744 -705 -420 C ATOM 3618 C ASP D 102 -26.102 -25.031 -26.301 1.00 99.15 C ANISOU 3618 C ASP D 102 8710 16541 12420 -862 -1016 -646 C ATOM 3619 O ASP D 102 -26.452 -24.174 -27.118 1.00114.18 O ANISOU 3619 O ASP D 102 10505 18769 14108 -559 -1055 -607 O ATOM 3620 CB ASP D 102 -27.386 -24.858 -24.163 1.00 90.70 C ANISOU 3620 CB ASP D 102 7396 15626 11440 -728 -534 -128 C ATOM 3621 CG ASP D 102 -27.841 -26.303 -24.094 1.00102.67 C ANISOU 3621 CG ASP D 102 8530 17165 13314 -1285 -704 -123 C ATOM 3622 OD1 ASP D 102 -27.012 -27.203 -24.346 1.00104.04 O ANISOU 3622 OD1 ASP D 102 8924 16950 13656 -1639 -934 -398 O ATOM 3623 OD2 ASP D 102 -29.029 -26.540 -23.790 1.00113.79 O ANISOU 3623 OD2 ASP D 102 9406 18976 14852 -1360 -630 190 O ATOM 3624 N ILE D 103 -25.799 -26.282 -26.641 1.00 92.08 N ANISOU 3624 N ILE D 103 7788 15474 11722 -1262 -1267 -891 N ATOM 3625 CA ILE D 103 -25.684 -26.734 -28.027 1.00 81.60 C ANISOU 3625 CA ILE D 103 6493 14193 10320 -1284 -1586 -1162 C ATOM 3626 C ILE D 103 -24.756 -25.771 -28.759 1.00 74.18 C ANISOU 3626 C ILE D 103 5757 13373 9054 -922 -1538 -1220 C ATOM 3627 O ILE D 103 -25.204 -25.029 -29.646 1.00 77.27 O ANISOU 3627 O ILE D 103 6021 14121 9217 -640 -1580 -1164 O ATOM 3628 CB ILE D 103 -27.060 -26.831 -28.708 1.00 74.50 C ANISOU 3628 CB ILE D 103 5248 13594 9464 -1291 -1768 -1079 C ATOM 3629 CG1 ILE D 103 -28.061 -27.530 -27.788 1.00 73.75 C ANISOU 3629 CG1 ILE D 103 4833 13452 9736 -1612 -1750 -835 C ATOM 3630 CG2 ILE D 103 -26.958 -27.593 -30.022 1.00 70.18 C ANISOU 3630 CG2 ILE D 103 4849 12947 8871 -1345 -2168 -1385 C ATOM 3631 CD1 ILE D 103 -27.701 -28.966 -27.473 1.00 71.46 C ANISOU 3631 CD1 ILE D 103 4718 12640 9793 -2031 -1978 -965 C ATOM 3632 N PRO D 104 -23.466 -25.733 -28.417 1.00 64.60 N ANISOU 3632 N PRO D 104 4930 11771 7843 -896 -1418 -1234 N ATOM 3633 CA PRO D 104 -22.579 -24.696 -28.965 1.00 64.31 C ANISOU 3633 CA PRO D 104 5102 11754 7580 -558 -1322 -1095 C ATOM 3634 C PRO D 104 -22.204 -24.996 -30.410 1.00 72.60 C ANISOU 3634 C PRO D 104 6117 13082 8384 -405 -1504 -1288 C ATOM 3635 O PRO D 104 -21.660 -26.058 -30.718 1.00 78.76 O ANISOU 3635 O PRO D 104 7009 13737 9180 -524 -1649 -1563 O ATOM 3636 CB PRO D 104 -21.356 -24.756 -28.041 1.00 50.90 C ANISOU 3636 CB PRO D 104 3758 9538 6043 -657 -1192 -1010 C ATOM 3637 CG PRO D 104 -21.324 -26.170 -27.572 1.00 50.27 C ANISOU 3637 CG PRO D 104 3693 9223 6183 -1016 -1286 -1259 C ATOM 3638 CD PRO D 104 -22.759 -26.630 -27.485 1.00 53.26 C ANISOU 3638 CD PRO D 104 3724 9860 6653 -1191 -1384 -1313 C ATOM 3639 N THR D 105 -22.500 -24.050 -31.298 1.00 69.81 N ANISOU 3639 N THR D 105 5642 13116 7765 -83 -1503 -1142 N ATOM 3640 CA THR D 105 -22.028 -24.123 -32.674 1.00 71.62 C ANISOU 3640 CA THR D 105 5880 13667 7665 186 -1614 -1239 C ATOM 3641 C THR D 105 -20.592 -23.638 -32.821 1.00 71.29 C ANISOU 3641 C THR D 105 6041 13496 7550 370 -1423 -969 C ATOM 3642 O THR D 105 -20.078 -23.610 -33.945 1.00 83.17 O ANISOU 3642 O THR D 105 7534 15329 8736 674 -1434 -944 O ATOM 3643 CB THR D 105 -22.944 -23.310 -33.594 1.00 85.20 C ANISOU 3643 CB THR D 105 7372 15881 9120 468 -1690 -1138 C ATOM 3644 OG1 THR D 105 -22.953 -21.940 -33.176 1.00 95.13 O ANISOU 3644 OG1 THR D 105 8636 17105 10405 634 -1491 -728 O ATOM 3645 CG2 THR D 105 -24.364 -23.856 -33.549 1.00 86.72 C ANISOU 3645 CG2 THR D 105 7401 16093 9454 266 -1849 -1317 C ATOM 3646 N TYR D 106 -19.946 -23.256 -31.715 1.00 68.65 N ANISOU 3646 N TYR D 106 5874 12713 7495 212 -1268 -731 N ATOM 3647 CA TYR D 106 -18.553 -22.805 -31.706 1.00 58.26 C ANISOU 3647 CA TYR D 106 4699 11212 6227 297 -1143 -392 C ATOM 3648 C TYR D 106 -18.339 -21.623 -32.649 1.00 66.58 C ANISOU 3648 C TYR D 106 5633 12603 7059 623 -1095 25 C ATOM 3649 O TYR D 106 -17.304 -21.503 -33.307 1.00 73.02 O ANISOU 3649 O TYR D 106 6409 13571 7765 797 -1008 304 O ATOM 3650 CB TYR D 106 -17.600 -23.957 -32.031 1.00 65.51 C ANISOU 3650 CB TYR D 106 5690 12104 7096 292 -1140 -596 C ATOM 3651 CG TYR D 106 -17.656 -25.071 -31.010 1.00 80.49 C ANISOU 3651 CG TYR D 106 7740 13575 9269 -59 -1206 -930 C ATOM 3652 CD1 TYR D 106 -18.266 -26.283 -31.306 1.00 88.97 C ANISOU 3652 CD1 TYR D 106 8805 14717 10284 -154 -1401 -1403 C ATOM 3653 CD2 TYR D 106 -17.116 -24.903 -29.741 1.00 88.85 C ANISOU 3653 CD2 TYR D 106 8971 14130 10658 -301 -1128 -754 C ATOM 3654 CE1 TYR D 106 -18.324 -27.302 -30.371 1.00 93.29 C ANISOU 3654 CE1 TYR D 106 9476 14851 11121 -504 -1484 -1641 C ATOM 3655 CE2 TYR D 106 -17.170 -25.914 -28.800 1.00 89.80 C ANISOU 3655 CE2 TYR D 106 9227 13881 11011 -605 -1174 -1013 C ATOM 3656 CZ TYR D 106 -17.775 -27.111 -29.121 1.00 97.40 C ANISOU 3656 CZ TYR D 106 10142 14929 11937 -718 -1335 -1431 C ATOM 3657 OH TYR D 106 -17.831 -28.121 -28.187 1.00109.42 O ANISOU 3657 OH TYR D 106 11786 16062 13728 -1049 -1402 -1625 O ATOM 3658 N PHE D 107 -19.333 -20.740 -32.707 1.00 69.75 N ANISOU 3658 N PHE D 107 5954 13148 7400 730 -1140 120 N ATOM 3659 CA PHE D 107 -19.256 -19.498 -33.459 1.00 79.60 C ANISOU 3659 CA PHE D 107 7116 14639 8490 1014 -1128 559 C ATOM 3660 C PHE D 107 -19.917 -18.397 -32.647 1.00 98.03 C ANISOU 3660 C PHE D 107 9567 16686 10994 1019 -1184 739 C ATOM 3661 O PHE D 107 -20.973 -18.610 -32.046 1.00108.95 O ANISOU 3661 O PHE D 107 10937 18052 12407 968 -1202 461 O ATOM 3662 CB PHE D 107 -19.937 -19.617 -34.828 1.00 98.40 C ANISOU 3662 CB PHE D 107 9273 17668 10447 1315 -1176 422 C ATOM 3663 CG PHE D 107 -18.977 -19.679 -35.981 1.00107.56 C ANISOU 3663 CG PHE D 107 10354 19206 11308 1598 -1082 658 C ATOM 3664 CD1 PHE D 107 -18.811 -20.850 -36.701 1.00 99.20 C ANISOU 3664 CD1 PHE D 107 9293 18451 9948 1743 -1109 269 C ATOM 3665 CD2 PHE D 107 -18.237 -18.564 -36.343 1.00124.54 C ANISOU 3665 CD2 PHE D 107 12441 21411 13469 1755 -986 1302 C ATOM 3666 CE1 PHE D 107 -17.929 -20.908 -37.765 1.00101.73 C ANISOU 3666 CE1 PHE D 107 9553 19198 9903 2128 -975 504 C ATOM 3667 CE2 PHE D 107 -17.352 -18.616 -37.404 1.00126.98 C ANISOU 3667 CE2 PHE D 107 12615 22149 13480 2057 -833 1621 C ATOM 3668 CZ PHE D 107 -17.199 -19.789 -38.117 1.00115.31 C ANISOU 3668 CZ PHE D 107 11132 21061 11621 2294 -799 1217 C ATOM 3669 N ASP D 108 -19.293 -17.222 -32.631 1.00105.86 N ANISOU 3669 N ASP D 108 10671 17452 12097 1108 -1234 1237 N ATOM 3670 CA ASP D 108 -19.829 -16.095 -31.871 1.00102.86 C ANISOU 3670 CA ASP D 108 10513 16720 11849 1199 -1358 1398 C ATOM 3671 C ASP D 108 -19.285 -14.810 -32.472 1.00101.16 C ANISOU 3671 C ASP D 108 10324 16444 11670 1358 -1489 1982 C ATOM 3672 O ASP D 108 -18.071 -14.582 -32.448 1.00108.74 O ANISOU 3672 O ASP D 108 11333 17125 12857 1202 -1551 2384 O ATOM 3673 CB ASP D 108 -19.455 -16.206 -30.391 1.00 91.14 C ANISOU 3673 CB ASP D 108 9379 14580 10668 982 -1418 1309 C ATOM 3674 CG ASP D 108 -20.313 -15.323 -29.502 1.00 98.34 C ANISOU 3674 CG ASP D 108 10573 15205 11587 1195 -1523 1284 C ATOM 3675 OD1 ASP D 108 -20.936 -14.371 -30.018 1.00 96.51 O ANISOU 3675 OD1 ASP D 108 10307 15155 11209 1493 -1599 1457 O ATOM 3676 OD2 ASP D 108 -20.361 -15.580 -28.280 1.00102.82 O ANISOU 3676 OD2 ASP D 108 11417 15379 12271 1118 -1526 1096 O ATOM 3677 N TYR D 109 -20.175 -13.976 -33.006 1.00 85.73 N ANISOU 3677 N TYR D 109 8303 14748 9522 1653 -1549 2082 N ATOM 3678 CA TYR D 109 -19.803 -12.685 -33.564 1.00 93.10 C ANISOU 3678 CA TYR D 109 9283 15580 10509 1804 -1709 2660 C ATOM 3679 C TYR D 109 -20.015 -11.543 -32.578 1.00107.35 C ANISOU 3679 C TYR D 109 11512 16731 12544 1892 -2000 2812 C ATOM 3680 O TYR D 109 -19.867 -10.376 -32.953 1.00125.14 O ANISOU 3680 O TYR D 109 13932 18707 14909 1969 -2164 3173 O ATOM 3681 CB TYR D 109 -20.589 -12.418 -34.850 1.00 96.27 C ANISOU 3681 CB TYR D 109 9484 16510 10584 2044 -1564 2621 C ATOM 3682 CG TYR D 109 -20.467 -13.518 -35.880 1.00 95.64 C ANISOU 3682 CG TYR D 109 9110 17028 10199 2049 -1332 2403 C ATOM 3683 CD1 TYR D 109 -19.317 -13.653 -36.647 1.00 95.64 C ANISOU 3683 CD1 TYR D 109 8997 17179 10161 2017 -1194 2753 C ATOM 3684 CD2 TYR D 109 -21.502 -14.419 -36.088 1.00 90.93 C ANISOU 3684 CD2 TYR D 109 8370 16829 9352 2110 -1275 1859 C ATOM 3685 CE1 TYR D 109 -19.201 -14.657 -37.590 1.00 94.34 C ANISOU 3685 CE1 TYR D 109 8642 17572 9632 2148 -1008 2524 C ATOM 3686 CE2 TYR D 109 -21.396 -15.426 -37.029 1.00 88.46 C ANISOU 3686 CE2 TYR D 109 7895 16971 8744 2153 -1166 1609 C ATOM 3687 CZ TYR D 109 -20.243 -15.540 -37.777 1.00 92.97 C ANISOU 3687 CZ TYR D 109 8415 17712 9197 2224 -1034 1917 C ATOM 3688 OH TYR D 109 -20.132 -16.541 -38.715 1.00 97.52 O ANISOU 3688 OH TYR D 109 8891 18766 9397 2393 -952 1636 O ATOM 3689 N ASP D 110 -20.356 -11.854 -31.329 1.00102.48 N ANISOU 3689 N ASP D 110 11190 15729 12019 1847 -2018 2427 N ATOM 3690 CA ASP D 110 -20.595 -10.852 -30.297 1.00 99.13 C ANISOU 3690 CA ASP D 110 11279 14662 11725 2037 -2305 2466 C ATOM 3691 C ASP D 110 -19.494 -10.788 -29.253 1.00 98.36 C ANISOU 3691 C ASP D 110 11594 13789 11987 1760 -2559 2574 C ATOM 3692 O ASP D 110 -19.087 -9.692 -28.860 1.00101.68 O ANISOU 3692 O ASP D 110 12435 13569 12628 1822 -2980 2884 O ATOM 3693 CB ASP D 110 -21.934 -11.124 -29.600 1.00107.24 C ANISOU 3693 CB ASP D 110 12363 15881 12500 2336 -2134 1988 C ATOM 3694 CG ASP D 110 -22.222 -10.136 -28.487 1.00119.41 C ANISOU 3694 CG ASP D 110 14502 16803 14064 2681 -2402 1970 C ATOM 3695 OD1 ASP D 110 -22.451 -8.947 -28.791 1.00125.81 O ANISOU 3695 OD1 ASP D 110 15525 17432 14847 2997 -2666 2226 O ATOM 3696 OD2 ASP D 110 -22.220 -10.550 -27.308 1.00122.22 O ANISOU 3696 OD2 ASP D 110 15155 16845 14438 2678 -2368 1698 O ATOM 3697 N SER D 111 -18.998 -11.937 -28.791 1.00 95.86 N ANISOU 3697 N SER D 111 11193 13476 11753 1453 -2374 2327 N ATOM 3698 CA SER D 111 -17.940 -11.960 -27.792 1.00109.49 C ANISOU 3698 CA SER D 111 13288 14495 13819 1180 -2626 2420 C ATOM 3699 C SER D 111 -16.928 -13.077 -28.002 1.00109.11 C ANISOU 3699 C SER D 111 12932 14597 13928 783 -2438 2452 C ATOM 3700 O SER D 111 -15.995 -13.192 -27.200 1.00110.51 O ANISOU 3700 O SER D 111 13358 14225 14407 528 -2643 2547 O ATOM 3701 CB SER D 111 -18.539 -12.081 -26.380 1.00117.53 C ANISOU 3701 CB SER D 111 14778 15136 14743 1362 -2662 1984 C ATOM 3702 OG SER D 111 -19.385 -10.983 -26.088 1.00127.09 O ANISOU 3702 OG SER D 111 16354 16153 15782 1831 -2864 1965 O ATOM 3703 N ASP D 112 -17.079 -13.900 -29.043 1.00 99.57 N ANISOU 3703 N ASP D 112 11230 14096 12506 765 -2093 2362 N ATOM 3704 CA ASP D 112 -16.171 -15.013 -29.329 1.00 95.38 C ANISOU 3704 CA ASP D 112 10432 13762 12048 502 -1899 2349 C ATOM 3705 C ASP D 112 -16.081 -15.984 -28.153 1.00 92.59 C ANISOU 3705 C ASP D 112 10299 13083 11798 299 -1846 1923 C ATOM 3706 O ASP D 112 -15.048 -16.625 -27.940 1.00100.45 O ANISOU 3706 O ASP D 112 11256 13913 12996 51 -1833 2002 O ATOM 3707 CB ASP D 112 -14.777 -14.507 -29.719 1.00 93.67 C ANISOU 3707 CB ASP D 112 10098 13352 12141 324 -2064 3016 C ATOM 3708 CG ASP D 112 -13.966 -15.544 -30.475 1.00103.18 C ANISOU 3708 CG ASP D 112 10897 15037 13271 247 -1772 3089 C ATOM 3709 OD1 ASP D 112 -14.517 -16.621 -30.786 1.00105.98 O ANISOU 3709 OD1 ASP D 112 11119 15830 13317 341 -1502 2576 O ATOM 3710 OD2 ASP D 112 -12.778 -15.282 -30.755 1.00110.67 O ANISOU 3710 OD2 ASP D 112 11658 15917 14473 113 -1839 3682 O ATOM 3711 N ASN D 113 -17.164 -16.094 -27.380 1.00 76.34 N ANISOU 3711 N ASN D 113 8446 10965 9594 432 -1799 1519 N ATOM 3712 CA ASN D 113 -17.233 -16.938 -26.188 1.00 67.71 C ANISOU 3712 CA ASN D 113 7575 9588 8565 285 -1734 1163 C ATOM 3713 C ASN D 113 -16.126 -16.620 -25.187 1.00 76.27 C ANISOU 3713 C ASN D 113 9070 9945 9965 104 -2024 1359 C ATOM 3714 O ASN D 113 -15.775 -17.464 -24.356 1.00 72.36 O ANISOU 3714 O ASN D 113 8708 9217 9567 -88 -1975 1149 O ATOM 3715 CB ASN D 113 -17.199 -18.427 -26.555 1.00 50.79 C ANISOU 3715 CB ASN D 113 5105 7828 6365 77 -1471 859 C ATOM 3716 CG ASN D 113 -18.282 -18.809 -27.544 1.00 73.99 C ANISOU 3716 CG ASN D 113 7666 11429 9015 221 -1296 641 C ATOM 3717 OD1 ASN D 113 -19.434 -19.027 -27.167 1.00 79.04 O ANISOU 3717 OD1 ASN D 113 8258 12239 9535 302 -1208 392 O ATOM 3718 ND2 ASN D 113 -17.916 -18.896 -28.818 1.00 81.29 N ANISOU 3718 ND2 ASN D 113 8307 12760 9821 277 -1258 768 N ATOM 3719 N PHE D 114 -15.572 -15.412 -25.250 1.00 74.79 N ANISOU 3719 N PHE D 114 9935 8994 9489 -210 -2053 -75 N ATOM 3720 CA PHE D 114 -14.456 -15.000 -24.411 1.00 70.53 C ANISOU 3720 CA PHE D 114 9472 8521 8804 -296 -1901 -16 C ATOM 3721 C PHE D 114 -14.897 -13.833 -23.541 1.00 78.79 C ANISOU 3721 C PHE D 114 10573 9174 10188 23 -2311 -221 C ATOM 3722 O PHE D 114 -15.518 -12.886 -24.036 1.00 87.71 O ANISOU 3722 O PHE D 114 11908 9866 11552 67 -2969 -213 O ATOM 3723 CB PHE D 114 -13.250 -14.605 -25.269 1.00 68.48 C ANISOU 3723 CB PHE D 114 9571 8315 8135 -883 -2024 345 C ATOM 3724 CG PHE D 114 -11.936 -14.684 -24.547 1.00 58.28 C ANISOU 3724 CG PHE D 114 8228 7252 6664 -1018 -1665 371 C ATOM 3725 CD1 PHE D 114 -11.500 -13.636 -23.754 1.00 63.21 C ANISOU 3725 CD1 PHE D 114 9028 7642 7346 -944 -1913 385 C ATOM 3726 CD2 PHE D 114 -11.132 -15.805 -24.671 1.00 55.83 C ANISOU 3726 CD2 PHE D 114 7672 7359 6183 -1211 -1125 347 C ATOM 3727 CE1 PHE D 114 -10.289 -13.708 -23.093 1.00 59.94 C ANISOU 3727 CE1 PHE D 114 8568 7416 6791 -1067 -1620 404 C ATOM 3728 CE2 PHE D 114 -9.920 -15.882 -24.012 1.00 66.66 C ANISOU 3728 CE2 PHE D 114 8966 8883 7481 -1314 -878 326 C ATOM 3729 CZ PHE D 114 -9.498 -14.832 -23.223 1.00 61.06 C ANISOU 3729 CZ PHE D 114 8457 7946 6798 -1247 -1123 371 C ATOM 3730 N TYR D 115 -14.578 -13.901 -22.251 1.00 69.33 N ANISOU 3730 N TYR D 115 9200 8104 9036 220 -1970 -421 N ATOM 3731 CA TYR D 115 -14.998 -12.891 -21.291 1.00 67.52 C ANISOU 3731 CA TYR D 115 8946 7573 9137 511 -2244 -719 C ATOM 3732 C TYR D 115 -13.827 -12.512 -20.397 1.00 68.69 C ANISOU 3732 C TYR D 115 9222 7800 9075 388 -2081 -609 C ATOM 3733 O TYR D 115 -13.033 -13.370 -20.002 1.00 68.94 O ANISOU 3733 O TYR D 115 9180 8177 8838 253 -1596 -503 O ATOM 3734 CB TYR D 115 -16.175 -13.392 -20.444 1.00 67.66 C ANISOU 3734 CB TYR D 115 8552 7681 9474 885 -1946 -1253 C ATOM 3735 CG TYR D 115 -17.357 -13.849 -21.271 1.00 78.70 C ANISOU 3735 CG TYR D 115 9766 9020 11117 1035 -2070 -1415 C ATOM 3736 CD1 TYR D 115 -17.487 -15.177 -21.659 1.00 70.20 C ANISOU 3736 CD1 TYR D 115 8535 8312 9825 956 -1602 -1332 C ATOM 3737 CD2 TYR D 115 -18.337 -12.950 -21.672 1.00 74.26 C ANISOU 3737 CD2 TYR D 115 9175 7992 11049 1264 -2712 -1667 C ATOM 3738 CE1 TYR D 115 -18.562 -15.598 -22.419 1.00 73.33 C ANISOU 3738 CE1 TYR D 115 8765 8658 10438 1088 -1712 -1476 C ATOM 3739 CE2 TYR D 115 -19.417 -13.362 -22.432 1.00 72.70 C ANISOU 3739 CE2 TYR D 115 8802 7705 11116 1409 -2878 -1828 C ATOM 3740 CZ TYR D 115 -19.524 -14.687 -22.802 1.00 74.47 C ANISOU 3740 CZ TYR D 115 8887 8344 11064 1313 -2347 -1721 C ATOM 3741 OH TYR D 115 -20.596 -15.102 -23.558 1.00 78.76 O ANISOU 3741 OH TYR D 115 9257 8804 11864 1454 -2506 -1879 O ATOM 3742 N TRP D 116 -13.727 -11.224 -20.086 1.00 75.74 N ANISOU 3742 N TRP D 116 10304 8334 10139 444 -2545 -646 N ATOM 3743 CA TRP D 116 -12.658 -10.675 -19.266 1.00 80.75 C ANISOU 3743 CA TRP D 116 11091 8984 10607 335 -2478 -544 C ATOM 3744 C TRP D 116 -13.204 -10.249 -17.907 1.00 85.30 C ANISOU 3744 C TRP D 116 11461 9475 11476 651 -2395 -1010 C ATOM 3745 O TRP D 116 -14.395 -10.385 -17.612 1.00 94.40 O ANISOU 3745 O TRP D 116 12319 10582 12966 928 -2355 -1464 O ATOM 3746 CB TRP D 116 -11.988 -9.494 -19.972 1.00 88.33 C ANISOU 3746 CB TRP D 116 12477 9617 11468 60 -3065 -206 C ATOM 3747 CG TRP D 116 -11.197 -9.870 -21.185 1.00 89.81 C ANISOU 3747 CG TRP D 116 12905 9978 11242 -426 -3039 211 C ATOM 3748 CD1 TRP D 116 -11.646 -9.928 -22.472 1.00 71.76 C ANISOU 3748 CD1 TRP D 116 10795 7583 8886 -652 -3353 391 C ATOM 3749 CD2 TRP D 116 -9.812 -10.231 -21.227 1.00 87.79 C ANISOU 3749 CD2 TRP D 116 12720 10042 10595 -802 -2675 434 C ATOM 3750 NE1 TRP D 116 -10.628 -10.307 -23.313 1.00 66.22 N ANISOU 3750 NE1 TRP D 116 10276 7162 7721 -1200 -3145 692 N ATOM 3751 CE2 TRP D 116 -9.490 -10.499 -22.573 1.00 80.14 C ANISOU 3751 CE2 TRP D 116 11936 9192 9322 -1280 -2722 683 C ATOM 3752 CE3 TRP D 116 -8.812 -10.357 -20.257 1.00 82.36 C ANISOU 3752 CE3 TRP D 116 11943 9540 9809 -804 -2336 406 C ATOM 3753 CZ2 TRP D 116 -8.213 -10.885 -22.973 1.00 84.05 C ANISOU 3753 CZ2 TRP D 116 12458 10020 9458 -1757 -2385 816 C ATOM 3754 CZ3 TRP D 116 -7.545 -10.739 -20.656 1.00 85.96 C ANISOU 3754 CZ3 TRP D 116 12429 10271 9962 -1216 -2076 572 C ATOM 3755 CH2 TRP D 116 -7.256 -10.999 -22.002 1.00 89.29 C ANISOU 3755 CH2 TRP D 116 12965 10840 10121 -1687 -2074 732 C ATOM 3756 N GLY D 117 -12.307 -9.722 -17.073 1.00 71.29 N ANISOU 3756 N GLY D 117 9825 7698 9563 566 -2345 -942 N ATOM 3757 CA GLY D 117 -12.662 -9.176 -15.785 1.00 69.83 C ANISOU 3757 CA GLY D 117 9502 7436 9592 764 -2277 -1374 C ATOM 3758 C GLY D 117 -12.238 -7.721 -15.664 1.00 80.18 C ANISOU 3758 C GLY D 117 11049 8359 11059 776 -2809 -1325 C ATOM 3759 O GLY D 117 -11.674 -7.129 -16.588 1.00 84.54 O ANISOU 3759 O GLY D 117 11918 8689 11515 593 -3256 -925 O ATOM 3760 N GLN D 118 -12.527 -7.154 -14.491 1.00 86.51 N ANISOU 3760 N GLN D 118 11706 9091 12074 936 -2747 -1765 N ATOM 3761 CA GLN D 118 -12.182 -5.757 -14.244 1.00101.33 C ANISOU 3761 CA GLN D 118 13766 10583 14153 982 -3250 -1788 C ATOM 3762 C GLN D 118 -10.674 -5.579 -14.113 1.00 99.16 C ANISOU 3762 C GLN D 118 13843 10406 13424 683 -3188 -1272 C ATOM 3763 O GLN D 118 -10.074 -4.746 -14.802 1.00 91.39 O ANISOU 3763 O GLN D 118 13184 9146 12394 536 -3680 -923 O ATOM 3764 CB GLN D 118 -12.899 -5.254 -12.991 1.00115.79 C ANISOU 3764 CB GLN D 118 15288 12362 16344 1201 -3128 -2489 C ATOM 3765 N GLY D 119 -10.048 -6.349 -13.238 1.00 99.64 N ANISOU 3765 N GLY D 119 13865 10836 13155 551 -2630 -1231 N ATOM 3766 CA GLY D 119 -8.611 -6.267 -13.037 1.00 96.47 C ANISOU 3766 CA GLY D 119 13729 10529 12397 292 -2564 -819 C ATOM 3767 C GLY D 119 -8.280 -5.755 -11.647 1.00 96.73 C ANISOU 3767 C GLY D 119 13786 10555 12411 306 -2441 -1033 C ATOM 3768 O GLY D 119 -8.946 -4.857 -11.116 1.00 94.92 O ANISOU 3768 O GLY D 119 13468 10101 12495 490 -2640 -1436 O ATOM 3769 N THR D 120 -7.240 -6.332 -11.048 1.00 99.92 N ANISOU 3769 N THR D 120 14296 11187 12481 100 -2142 -800 N ATOM 3770 CA THR D 120 -6.775 -5.940 -9.726 1.00 99.23 C ANISOU 3770 CA THR D 120 14302 11108 12293 33 -2031 -925 C ATOM 3771 C THR D 120 -5.299 -5.579 -9.792 1.00 85.56 C ANISOU 3771 C THR D 120 12822 9327 10359 -156 -2181 -507 C ATOM 3772 O THR D 120 -4.519 -6.238 -10.488 1.00 71.37 O ANISOU 3772 O THR D 120 11050 7658 8408 -310 -2125 -186 O ATOM 3773 CB THR D 120 -6.991 -7.058 -8.696 1.00102.90 C ANISOU 3773 CB THR D 120 14690 11864 12542 -92 -1564 -1093 C ATOM 3774 OG1 THR D 120 -6.355 -8.260 -9.148 1.00107.83 O ANISOU 3774 OG1 THR D 120 15331 12673 12966 -225 -1414 -742 O ATOM 3775 CG2 THR D 120 -8.476 -7.318 -8.493 1.00 99.68 C ANISOU 3775 CG2 THR D 120 14016 11542 12316 30 -1355 -1615 C ATOM 3776 N GLN D 121 -4.921 -4.533 -9.063 1.00 94.63 N ANISOU 3776 N GLN D 121 14116 10301 11537 -158 -2356 -575 N ATOM 3777 CA GLN D 121 -3.543 -4.065 -9.062 1.00 99.26 C ANISOU 3777 CA GLN D 121 14933 10827 11954 -340 -2511 -231 C ATOM 3778 C GLN D 121 -2.687 -4.913 -8.129 1.00 94.28 C ANISOU 3778 C GLN D 121 14337 10393 11090 -505 -2230 -125 C ATOM 3779 O GLN D 121 -3.107 -5.264 -7.022 1.00 97.06 O ANISOU 3779 O GLN D 121 14679 10830 11369 -523 -2015 -350 O ATOM 3780 CB GLN D 121 -3.480 -2.597 -8.636 1.00107.84 C ANISOU 3780 CB GLN D 121 16173 11620 13180 -272 -2847 -340 C ATOM 3781 CG GLN D 121 -2.091 -1.984 -8.708 1.00112.52 C ANISOU 3781 CG GLN D 121 17017 12135 13600 -478 -3034 3 C ATOM 3782 CD GLN D 121 -1.641 -1.725 -10.132 1.00113.38 C ANISOU 3782 CD GLN D 121 17263 12173 13645 -660 -3299 319 C ATOM 3783 OE1 GLN D 121 -2.292 -0.992 -10.876 1.00116.71 O ANISOU 3783 OE1 GLN D 121 17781 12338 14225 -606 -3684 308 O ATOM 3784 NE2 GLN D 121 -0.523 -2.329 -10.519 1.00111.60 N ANISOU 3784 NE2 GLN D 121 17048 12156 13197 -925 -3126 563 N ATOM 3785 N VAL D 122 -1.482 -5.244 -8.587 1.00 80.67 N ANISOU 3785 N VAL D 122 12662 8728 9260 -676 -2263 182 N ATOM 3786 CA VAL D 122 -0.502 -5.985 -7.800 1.00 60.76 C ANISOU 3786 CA VAL D 122 10171 6295 6622 -819 -2153 294 C ATOM 3787 C VAL D 122 0.822 -5.243 -7.914 1.00 81.71 C ANISOU 3787 C VAL D 122 12946 8848 9253 -961 -2356 481 C ATOM 3788 O VAL D 122 1.428 -5.209 -8.993 1.00 93.14 O ANISOU 3788 O VAL D 122 14329 10345 10717 -1090 -2409 604 O ATOM 3789 CB VAL D 122 -0.355 -7.441 -8.265 1.00 60.87 C ANISOU 3789 CB VAL D 122 9989 6486 6652 -869 -1983 363 C ATOM 3790 CG1 VAL D 122 0.815 -8.107 -7.558 1.00 63.79 C ANISOU 3790 CG1 VAL D 122 10387 6836 7015 -1008 -2042 476 C ATOM 3791 CG2 VAL D 122 -1.640 -8.213 -8.008 1.00 73.02 C ANISOU 3791 CG2 VAL D 122 11442 8134 8169 -772 -1767 179 C ATOM 3792 N THR D 123 1.271 -4.649 -6.812 1.00 79.83 N ANISOU 3792 N THR D 123 12888 8493 8951 -992 -2445 470 N ATOM 3793 CA THR D 123 2.498 -3.868 -6.778 1.00 76.29 C ANISOU 3793 CA THR D 123 12563 7940 8483 -1123 -2636 618 C ATOM 3794 C THR D 123 3.505 -4.538 -5.854 1.00 73.12 C ANISOU 3794 C THR D 123 12182 7534 8065 -1232 -2649 684 C ATOM 3795 O THR D 123 3.144 -5.039 -4.785 1.00 66.24 O ANISOU 3795 O THR D 123 11411 6648 7109 -1238 -2596 628 O ATOM 3796 CB THR D 123 2.227 -2.432 -6.310 1.00 81.22 C ANISOU 3796 CB THR D 123 13398 8369 9094 -1059 -2822 551 C ATOM 3797 OG1 THR D 123 1.139 -1.881 -7.061 1.00 90.04 O ANISOU 3797 OG1 THR D 123 14489 9401 10320 -919 -2922 442 O ATOM 3798 CG2 THR D 123 3.460 -1.561 -6.508 1.00 79.12 C ANISOU 3798 CG2 THR D 123 13275 8001 8787 -1224 -3031 726 C ATOM 3799 N VAL D 124 4.768 -4.552 -6.276 1.00 81.28 N ANISOU 3799 N VAL D 124 13129 8568 9185 -1369 -2747 774 N ATOM 3800 CA VAL D 124 5.856 -5.155 -5.514 1.00 76.91 C ANISOU 3800 CA VAL D 124 12549 7939 8735 -1453 -2874 805 C ATOM 3801 C VAL D 124 7.004 -4.158 -5.457 1.00 91.14 C ANISOU 3801 C VAL D 124 14425 9649 10553 -1576 -3034 847 C ATOM 3802 O VAL D 124 7.580 -3.810 -6.495 1.00 98.69 O ANISOU 3802 O VAL D 124 15242 10701 11555 -1716 -3001 815 O ATOM 3803 CB VAL D 124 6.326 -6.484 -6.128 1.00 81.08 C ANISOU 3803 CB VAL D 124 12742 8558 9505 -1484 -2841 737 C ATOM 3804 CG1 VAL D 124 7.563 -6.993 -5.406 1.00 78.21 C ANISOU 3804 CG1 VAL D 124 12316 8025 9375 -1552 -3108 721 C ATOM 3805 CG2 VAL D 124 5.212 -7.520 -6.078 1.00 83.92 C ANISOU 3805 CG2 VAL D 124 13065 8990 9829 -1380 -2706 719 C ATOM 3806 N SER D 125 7.336 -3.701 -4.252 1.00107.44 N ANISOU 3806 N SER D 125 16731 11548 12545 -1585 -3194 902 N ATOM 3807 CA SER D 125 8.453 -2.790 -4.053 1.00115.28 C ANISOU 3807 CA SER D 125 17804 12438 13558 -1695 -3360 941 C ATOM 3808 C SER D 125 9.734 -3.581 -3.824 1.00122.99 C ANISOU 3808 C SER D 125 18578 13343 14811 -1779 -3535 889 C ATOM 3809 O SER D 125 9.731 -4.608 -3.139 1.00140.72 O ANISOU 3809 O SER D 125 20819 15480 17168 -1743 -3674 903 O ATOM 3810 CB SER D 125 8.190 -1.859 -2.868 1.00119.04 C ANISOU 3810 CB SER D 125 18627 12762 13842 -1670 -3459 995 C ATOM 3811 OG SER D 125 8.007 -2.593 -1.670 1.00124.07 O ANISOU 3811 OG SER D 125 19415 13315 14410 -1699 -3524 1014 O ATOM 3812 N SER D 126 10.833 -3.093 -4.404 1.00121.36 N ANISOU 3812 N SER D 126 18204 13172 14733 -1925 -3568 798 N ATOM 3813 CA SER D 126 12.098 -3.815 -4.319 1.00123.77 C ANISOU 3813 CA SER D 126 18195 13404 15428 -1992 -3747 618 C ATOM 3814 C SER D 126 12.667 -3.806 -2.905 1.00139.78 C ANISOU 3814 C SER D 126 20447 15134 17529 -1951 -4107 722 C ATOM 3815 O SER D 126 13.348 -4.758 -2.508 1.00141.44 O ANISOU 3815 O SER D 126 20473 15159 18110 -1928 -4402 622 O ATOM 3816 CB SER D 126 13.106 -3.223 -5.304 1.00113.82 C ANISOU 3816 CB SER D 126 16678 12308 14261 -2238 -3628 403 C ATOM 3817 OG SER D 126 13.201 -1.818 -5.154 1.00112.38 O ANISOU 3817 OG SER D 126 16826 12100 13774 -2345 -3638 555 O ATOM 3818 N LEU D 127 12.407 -2.753 -2.136 1.00144.95 N ANISOU 3818 N LEU D 127 21500 15706 17868 -1960 -4140 903 N ATOM 3819 CA LEU D 127 12.888 -2.680 -0.761 1.00143.77 C ANISOU 3819 CA LEU D 127 21633 15286 17707 -1989 -4472 1020 C ATOM 3820 C LEU D 127 11.781 -2.222 0.183 1.00140.26 C ANISOU 3820 C LEU D 127 21637 14818 16839 -1992 -4393 1184 C ATOM 3821 O LEU D 127 11.753 -2.605 1.353 1.00141.78 O ANISOU 3821 O LEU D 127 22121 14828 16920 -2094 -4618 1290 O ATOM 3822 CB LEU D 127 14.092 -1.738 -0.653 1.00147.41 C ANISOU 3822 CB LEU D 127 22072 15668 18268 -2081 -4611 970 C ATOM 3823 CG LEU D 127 15.365 -2.123 -1.412 1.00150.01 C ANISOU 3823 CG LEU D 127 21912 16025 19061 -2153 -4688 680 C ATOM 3824 CD1 LEU D 127 15.384 -1.508 -2.804 1.00148.06 C ANISOU 3824 CD1 LEU D 127 21448 16096 18713 -2301 -4314 527 C ATOM 3825 CD2 LEU D 127 16.606 -1.724 -0.628 1.00152.24 C ANISOU 3825 CD2 LEU D 127 22220 16070 19556 -2215 -5034 633 C TER 3826 LEU D 127 HETATM 3827 N SAR B 1 -7.486 -16.447 -82.735 1.00102.93 N HETATM 3828 CA SAR B 1 -7.637 -17.526 -81.773 1.00100.92 C HETATM 3829 C SAR B 1 -9.055 -17.749 -81.190 1.00 94.05 C HETATM 3830 O SAR B 1 -10.071 -17.355 -81.835 1.00 91.90 O HETATM 3831 CN SAR B 1 -7.061 -16.899 -84.037 1.00100.79 C ATOM 3832 N ARG B 2 -9.129 -18.355 -80.009 1.00118.47 N ANISOU 3832 N ARG B 2 15861 15234 13919 -1475 -1729 -395 N ATOM 3833 CA ARG B 2 -10.409 -18.599 -79.355 1.00105.65 C ANISOU 3833 CA ARG B 2 14194 13803 12146 -1483 -1857 -144 C ATOM 3834 C ARG B 2 -10.882 -17.338 -78.639 1.00 80.33 C ANISOU 3834 C ARG B 2 11210 10785 8528 -1087 -1938 -75 C ATOM 3835 O ARG B 2 -10.097 -16.419 -78.403 1.00 71.68 O ANISOU 3835 O ARG B 2 10233 9630 7373 -831 -1865 -243 O ATOM 3836 CB ARG B 2 -10.301 -19.769 -78.372 1.00113.18 C ANISOU 3836 CB ARG B 2 14912 14740 13353 -1345 -1629 151 C ATOM 3837 CG ARG B 2 -11.606 -20.524 -78.166 1.00114.27 C ANISOU 3837 CG ARG B 2 14690 14970 13757 -1284 -1454 504 C ATOM 3838 CD ARG B 2 -11.398 -21.810 -77.384 1.00112.62 C ANISOU 3838 CD ARG B 2 14163 14712 13914 -1234 -1262 811 C ATOM 3839 NE ARG B 2 -11.291 -21.579 -75.947 1.00101.47 N ANISOU 3839 NE ARG B 2 12807 13541 12207 -813 -1167 1108 N ATOM 3840 CZ ARG B 2 -12.321 -21.627 -75.108 1.00103.13 C ANISOU 3840 CZ ARG B 2 12845 14012 12327 -469 -989 1520 C ATOM 3841 NH1 ARG B 2 -13.536 -21.897 -75.564 1.00 94.73 N ANISOU 3841 NH1 ARG B 2 11481 12976 11537 -502 -918 1747 N ATOM 3842 NH2 ARG B 2 -12.137 -21.407 -73.814 1.00112.23 N ANISOU 3842 NH2 ARG B 2 14131 15401 13109 -102 -888 1746 N ATOM 3843 N VAL B 3 -12.167 -17.296 -78.298 1.00 76.14 N ANISOU 3843 N VAL B 3 10512 10407 8013 -868 -1782 206 N ATOM 3844 CA VAL B 3 -12.789 -16.134 -77.673 1.00 86.46 C ANISOU 3844 CA VAL B 3 12015 11852 8982 -450 -1755 277 C ATOM 3845 C VAL B 3 -13.435 -16.594 -76.373 1.00101.41 C ANISOU 3845 C VAL B 3 13808 13926 10798 -7 -1419 661 C ATOM 3846 O VAL B 3 -14.472 -17.270 -76.392 1.00125.09 O ANISOU 3846 O VAL B 3 16415 17007 14108 19 -1207 1041 O ATOM 3847 CB VAL B 3 -13.818 -15.470 -78.599 1.00 86.66 C ANISOU 3847 CB VAL B 3 11892 11894 9143 -576 -1828 336 C ATOM 3848 CG1 VAL B 3 -14.535 -14.341 -77.879 1.00 90.90 C ANISOU 3848 CG1 VAL B 3 12585 12521 9432 -78 -1699 454 C ATOM 3849 CG2 VAL B 3 -13.141 -14.955 -79.860 1.00 88.29 C ANISOU 3849 CG2 VAL B 3 12133 11951 9463 -939 -2034 -26 C ATOM 3850 N TYR B 4 -12.825 -16.231 -75.242 1.00 83.83 N ANISOU 3850 N TYR B 4 11937 11768 8147 324 -1394 603 N ATOM 3851 CA TYR B 4 -13.357 -16.575 -73.923 1.00 80.28 C ANISOU 3851 CA TYR B 4 11468 11546 7488 772 -1058 958 C ATOM 3852 C TYR B 4 -14.269 -15.441 -73.463 1.00 83.84 C ANISOU 3852 C TYR B 4 12164 12097 7593 1259 -853 984 C ATOM 3853 O TYR B 4 -13.903 -14.585 -72.656 1.00102.36 O ANISOU 3853 O TYR B 4 15035 14457 9398 1582 -874 770 O ATOM 3854 CB TYR B 4 -12.227 -16.832 -72.934 1.00 77.46 C ANISOU 3854 CB TYR B 4 11399 11220 6814 821 -1156 915 C ATOM 3855 CG TYR B 4 -12.699 -17.300 -71.574 1.00 84.66 C ANISOU 3855 CG TYR B 4 12282 12422 7462 1227 -820 1317 C ATOM 3856 CD1 TYR B 4 -13.016 -18.632 -71.350 1.00 98.21 C ANISOU 3856 CD1 TYR B 4 13455 14260 9599 1148 -613 1769 C ATOM 3857 CD2 TYR B 4 -12.824 -16.409 -70.514 1.00 78.06 C ANISOU 3857 CD2 TYR B 4 11962 11721 5975 1671 -705 1238 C ATOM 3858 CE1 TYR B 4 -13.449 -19.065 -70.111 1.00105.90 C ANISOU 3858 CE1 TYR B 4 14352 15551 10335 1515 -304 2206 C ATOM 3859 CE2 TYR B 4 -13.257 -16.833 -69.273 1.00 95.51 C ANISOU 3859 CE2 TYR B 4 14140 14201 7949 1999 -356 1582 C ATOM 3860 CZ TYR B 4 -13.567 -18.162 -69.077 1.00107.05 C ANISOU 3860 CZ TYR B 4 15048 15895 9733 1977 -161 2136 C ATOM 3861 OH TYR B 4 -13.997 -18.591 -67.842 1.00110.89 O ANISOU 3861 OH TYR B 4 15453 16675 10005 2289 179 2515 O ATOM 3862 N LYS B 5 -15.488 -15.443 -73.999 1.00 68.79 N ANISOU 3862 N LYS B 5 9874 10224 6039 1300 -657 1273 N ATOM 3863 CA LYS B 5 -16.456 -14.384 -73.754 1.00 78.15 C ANISOU 3863 CA LYS B 5 11176 11445 7073 1744 -407 1367 C ATOM 3864 C LYS B 5 -17.300 -14.624 -72.506 1.00 76.77 C ANISOU 3864 C LYS B 5 10949 11522 6698 2342 137 1811 C ATOM 3865 O LYS B 5 -18.407 -14.083 -72.405 1.00 89.18 O ANISOU 3865 O LYS B 5 12389 13129 8367 2717 486 2100 O ATOM 3866 CB LYS B 5 -17.352 -14.208 -74.982 1.00 88.03 C ANISOU 3866 CB LYS B 5 11994 12592 8860 1459 -489 1561 C ATOM 3867 CG LYS B 5 -17.624 -15.496 -75.739 1.00 84.90 C ANISOU 3867 CG LYS B 5 11063 12189 9006 976 -594 1860 C ATOM 3868 CD LYS B 5 -18.192 -15.212 -77.119 1.00 82.61 C ANISOU 3868 CD LYS B 5 10501 11763 9125 523 -859 1918 C ATOM 3869 CE LYS B 5 -18.286 -16.482 -77.949 1.00 88.20 C ANISOU 3869 CE LYS B 5 10832 12398 10281 -39 -1056 2074 C ATOM 3870 NZ LYS B 5 -18.774 -16.207 -79.328 1.00 88.61 N ANISOU 3870 NZ LYS B 5 10705 12333 10631 -562 -1381 2106 N ATOM 3871 N HIS B 6 -16.797 -15.415 -71.550 1.00 79.80 N ANISOU 3871 N HIS B 6 11406 12091 6824 2443 238 1924 N ATOM 3872 CA HIS B 6 -17.512 -15.649 -70.305 1.00 83.77 C ANISOU 3872 CA HIS B 6 11889 12896 7044 3018 767 2361 C ATOM 3873 C HIS B 6 -17.028 -14.688 -69.223 1.00 88.83 C ANISOU 3873 C HIS B 6 13326 13590 6834 3458 869 1982 C ATOM 3874 O HIS B 6 -15.873 -14.250 -69.244 1.00 96.51 O ANISOU 3874 O HIS B 6 14742 14349 7577 3163 423 1441 O ATOM 3875 CB HIS B 6 -17.307 -17.086 -69.834 1.00 89.21 C ANISOU 3875 CB HIS B 6 12162 13792 7942 2865 810 2781 C ATOM 3876 CG HIS B 6 -17.559 -18.112 -70.894 1.00 83.89 C ANISOU 3876 CG HIS B 6 10816 12981 8078 2355 609 3039 C ATOM 3877 ND1 HIS B 6 -18.810 -18.348 -71.421 1.00 83.19 N ANISOU 3877 ND1 HIS B 6 10184 12889 8534 2382 784 3532 N ATOM 3878 CD2 HIS B 6 -16.719 -18.969 -71.522 1.00 72.19 C ANISOU 3878 CD2 HIS B 6 9148 11324 6958 1799 245 2877 C ATOM 3879 CE1 HIS B 6 -18.730 -19.303 -72.330 1.00 75.39 C ANISOU 3879 CE1 HIS B 6 8762 11727 8155 1833 480 3618 C ATOM 3880 NE2 HIS B 6 -17.472 -19.698 -72.410 1.00 78.42 N ANISOU 3880 NE2 HIS B 6 9362 11998 8434 1498 193 3195 N ATOM 3881 N PRO B 7 -17.892 -14.338 -68.266 1.00 92.22 N ANISOU 3881 N PRO B 7 13894 14209 6935 4084 1433 2220 N ATOM 3882 CA PRO B 7 -17.447 -13.488 -67.153 1.00 86.21 C ANISOU 3882 CA PRO B 7 13811 13333 5610 4335 1469 1726 C ATOM 3883 C PRO B 7 -16.474 -14.210 -66.234 1.00 91.86 C ANISOU 3883 C PRO B 7 14628 14141 6136 4034 1235 1657 C ATOM 3884 O PRO B 7 -16.890 -14.850 -65.263 1.00114.94 O ANISOU 3884 O PRO B 7 17390 17358 8925 4289 1592 2037 O ATOM 3885 CB PRO B 7 -18.754 -13.140 -66.431 1.00 87.12 C ANISOU 3885 CB PRO B 7 13905 13618 5578 5066 2201 2087 C ATOM 3886 CG PRO B 7 -19.691 -14.243 -66.792 1.00 85.99 C ANISOU 3886 CG PRO B 7 12924 13766 5983 5108 2526 2903 C ATOM 3887 CD PRO B 7 -19.332 -14.639 -68.194 1.00 94.81 C ANISOU 3887 CD PRO B 7 13668 14733 7624 4491 2020 2915 C ATOM 3888 N ALA B 8 -15.182 -14.107 -66.546 1.00 95.95 N ANISOU 3888 N ALA B 8 15355 14412 6691 3477 642 1245 N ATOM 3889 CA ALA B 8 -14.094 -14.745 -65.795 1.00107.77 C ANISOU 3889 CA ALA B 8 16923 15958 8068 3094 353 1240 C ATOM 3890 C ALA B 8 -14.162 -16.272 -65.837 1.00108.61 C ANISOU 3890 C ALA B 8 16423 16341 8502 2938 439 1804 C ATOM 3891 O ALA B 8 -13.137 -16.933 -66.004 1.00106.82 O ANISOU 3891 O ALA B 8 16075 16041 8472 2464 64 1828 O ATOM 3892 CB ALA B 8 -14.081 -14.256 -64.346 1.00124.59 C ANISOU 3892 CB ALA B 8 19548 18179 9612 3363 526 1128 C ATOM 3893 OXT ALA B 8 -15.218 -16.893 -65.715 1.00113.67 O ANISOU 3893 OXT ALA B 8 16623 17262 9305 3272 880 2304 O TER 3894 ALA B 8 HETATM 3895 C24 OLC A1401 -5.406 -13.723 -38.031 1.00112.65 C HETATM 3896 C3 OLC A1401 -1.805 -16.888 -43.463 1.00 97.02 C HETATM 3897 C2 OLC A1401 -2.081 -16.855 -41.961 1.00 92.50 C HETATM 3898 C21 OLC A1401 -4.457 -14.538 -40.191 1.00108.78 C HETATM 3899 C1 OLC A1401 -2.998 -15.677 -41.638 1.00106.72 C HETATM 3900 C22 OLC A1401 -5.526 -14.779 -39.128 1.00111.08 C HETATM 3901 O19 OLC A1401 -2.960 -14.697 -42.302 1.00121.30 O HETATM 3902 O25 OLC A1401 -6.524 -13.795 -37.190 1.00108.86 O HETATM 3903 O23 OLC A1401 -6.795 -14.700 -39.715 1.00106.87 O HETATM 3904 O20 OLC A1401 -3.886 -15.761 -40.559 1.00108.41 O HETATM 3905 C8 OLC A1402 -23.933 -27.232 -54.505 1.00 96.99 C HETATM 3906 C24 OLC A1402 -25.421 -33.669 -43.875 1.00 98.76 C HETATM 3907 C7 OLC A1402 -23.078 -27.755 -53.354 1.00 92.35 C HETATM 3908 C6 OLC A1402 -23.970 -28.035 -52.146 1.00 97.80 C HETATM 3909 C5 OLC A1402 -23.178 -28.814 -51.099 1.00104.61 C HETATM 3910 C4 OLC A1402 -24.068 -29.096 -49.891 1.00106.88 C HETATM 3911 C3 OLC A1402 -23.311 -29.980 -48.902 1.00102.83 C HETATM 3912 C2 OLC A1402 -24.241 -30.400 -47.767 1.00102.01 C HETATM 3913 C21 OLC A1402 -23.369 -32.800 -44.995 1.00103.12 C HETATM 3914 C1 OLC A1402 -23.521 -31.414 -46.880 1.00116.38 C HETATM 3915 C22 OLC A1402 -24.024 -33.097 -43.648 1.00 99.05 C HETATM 3916 O19 OLC A1402 -22.522 -31.924 -47.261 1.00127.97 O HETATM 3917 O25 OLC A1402 -25.738 -34.551 -42.834 1.00 98.72 O HETATM 3918 O23 OLC A1402 -23.247 -34.028 -42.949 1.00102.34 O HETATM 3919 O20 OLC A1402 -24.038 -31.743 -45.622 1.00113.22 O HETATM 3920 C24 OLC A1403 -28.039 -24.793 -35.586 1.00130.13 C HETATM 3921 C3 OLC A1403 -26.344 -22.829 -42.376 1.00104.98 C HETATM 3922 C2 OLC A1403 -26.726 -23.932 -41.392 1.00106.67 C HETATM 3923 C21 OLC A1403 -27.292 -24.165 -37.884 1.00117.55 C HETATM 3924 C1 OLC A1403 -27.105 -23.304 -40.053 1.00115.95 C HETATM 3925 C22 OLC A1403 -28.328 -23.903 -36.793 1.00120.72 C HETATM 3926 O19 OLC A1403 -26.733 -22.211 -39.787 1.00127.74 O HETATM 3927 O25 OLC A1403 -28.333 -24.090 -34.410 1.00139.66 O HETATM 3928 O23 OLC A1403 -28.261 -22.559 -36.406 1.00109.39 O HETATM 3929 O20 OLC A1403 -27.891 -24.012 -39.138 1.00113.58 O HETATM 3930 C24 OLC A1404 -10.116 -38.091 -37.403 1.00124.28 C HETATM 3931 C21 OLC A1404 -11.247 -36.965 -39.320 1.00119.56 C HETATM 3932 C1 OLC A1404 -12.240 -35.783 -41.087 1.00116.19 C HETATM 3933 C22 OLC A1404 -9.907 -37.202 -38.628 1.00124.02 C HETATM 3934 O19 OLC A1404 -12.367 -34.688 -41.523 1.00109.08 O HETATM 3935 O25 OLC A1404 -8.878 -38.357 -36.803 1.00123.62 O HETATM 3936 O23 OLC A1404 -9.026 -37.832 -39.516 1.00127.84 O HETATM 3937 O20 OLC A1404 -11.055 -36.144 -40.437 1.00121.43 O HETATM 3938 C24 OLC A1405 -27.473 -35.087 -47.779 1.00111.67 C HETATM 3939 C6 OLC A1405 -28.895 -30.230 -54.760 1.00 91.07 C HETATM 3940 C5 OLC A1405 -29.046 -31.748 -54.682 1.00 90.78 C HETATM 3941 C4 OLC A1405 -28.187 -32.291 -53.542 1.00100.45 C HETATM 3942 C3 OLC A1405 -28.894 -32.062 -52.208 1.00108.92 C HETATM 3943 C2 OLC A1405 -28.043 -31.147 -51.330 1.00112.64 C HETATM 3944 C21 OLC A1405 -28.980 -33.217 -48.464 1.00110.36 C HETATM 3945 C1 OLC A1405 -28.308 -31.455 -49.858 1.00118.55 C HETATM 3946 C22 OLC A1405 -28.296 -33.901 -47.283 1.00110.43 C HETATM 3947 O19 OLC A1405 -28.761 -30.620 -49.151 1.00119.06 O HETATM 3948 O25 OLC A1405 -26.599 -35.502 -46.765 1.00113.08 O HETATM 3949 O23 OLC A1405 -27.451 -32.985 -46.644 1.00113.53 O HETATM 3950 O20 OLC A1405 -28.009 -32.720 -49.341 1.00112.77 O HETATM 3951 C10 OLC A1406 -4.485 -17.388 -48.856 1.00 97.77 C HETATM 3952 C9 OLC A1406 -5.138 -16.845 -47.850 1.00 95.66 C HETATM 3953 C11 OLC A1406 -4.570 -18.894 -49.097 1.00 91.94 C HETATM 3954 C8 OLC A1406 -5.052 -15.339 -47.608 1.00 88.36 C HETATM 3955 C12 OLC A1406 -3.626 -19.282 -50.232 1.00 86.70 C HETATM 3956 C7 OLC A1406 -3.591 -14.900 -47.663 1.00 80.68 C HETATM 3957 C6 OLC A1406 -3.485 -13.427 -47.278 1.00 79.55 C HETATM 3958 C5 OLC A1406 -3.229 -13.312 -45.777 1.00 81.68 C HETATM 3959 C4 OLC A1406 -3.171 -11.839 -45.381 1.00 84.41 C HETATM 3960 C3 OLC A1406 -2.729 -11.720 -43.924 1.00 91.93 C HETATM 3961 C1 CLR A1407 -36.468 -6.342 -45.616 1.00108.53 C HETATM 3962 C2 CLR A1407 -37.630 -6.502 -44.634 1.00109.74 C HETATM 3963 C3 CLR A1407 -37.263 -5.944 -43.275 1.00104.99 C HETATM 3964 C4 CLR A1407 -36.887 -4.479 -43.395 1.00 99.10 C HETATM 3965 C5 CLR A1407 -35.822 -4.246 -44.440 1.00103.66 C HETATM 3966 C6 CLR A1407 -34.743 -3.531 -44.153 1.00108.27 C HETATM 3967 C7 CLR A1407 -33.632 -3.231 -45.109 1.00116.15 C HETATM 3968 C8 CLR A1407 -34.052 -3.461 -46.553 1.00112.67 C HETATM 3969 C9 CLR A1407 -34.775 -4.809 -46.672 1.00101.64 C HETATM 3970 C10 CLR A1407 -36.070 -4.870 -45.810 1.00107.62 C HETATM 3971 C11 CLR A1407 -35.010 -5.218 -48.140 1.00 97.79 C HETATM 3972 C12 CLR A1407 -33.803 -5.029 -49.069 1.00102.55 C HETATM 3973 C13 CLR A1407 -33.223 -3.612 -48.971 1.00115.48 C HETATM 3974 C14 CLR A1407 -32.843 -3.476 -47.484 1.00117.11 C HETATM 3975 C15 CLR A1407 -31.815 -2.356 -47.466 1.00121.33 C HETATM 3976 C16 CLR A1407 -30.879 -2.912 -48.529 1.00124.04 C HETATM 3977 C17 CLR A1407 -31.828 -3.378 -49.659 1.00122.38 C HETATM 3978 C18 CLR A1407 -34.321 -2.593 -49.328 1.00115.04 C HETATM 3979 C19 CLR A1407 -37.234 -4.114 -46.480 1.00112.16 C HETATM 3980 C20 CLR A1407 -31.636 -2.540 -50.949 1.00116.40 C HETATM 3981 C21 CLR A1407 -32.129 -1.092 -50.884 1.00112.78 C HETATM 3982 C22 CLR A1407 -32.182 -3.263 -52.195 1.00117.36 C HETATM 3983 C23 CLR A1407 -32.320 -2.392 -53.443 1.00122.39 C HETATM 3984 C24 CLR A1407 -30.996 -1.937 -54.052 1.00121.31 C HETATM 3985 C25 CLR A1407 -30.352 -2.882 -55.049 1.00119.62 C HETATM 3986 C26 CLR A1407 -29.017 -2.340 -55.530 1.00118.16 C HETATM 3987 C27 CLR A1407 -31.278 -3.135 -56.227 1.00114.46 C HETATM 3988 O1 CLR A1407 -38.362 -6.084 -42.371 1.00103.42 O HETATM 3989 O HOH A1501 -13.957 -18.806 -79.530 1.00 61.66 O HETATM 3990 O HOH A1502 -18.618 -9.133 -74.290 1.00 79.20 O HETATM 3991 O HOH A1503 -22.214 -32.976 -22.091 1.00 68.87 O HETATM 3992 O HOH A1504 -4.963 -21.885 -25.051 1.00 40.58 O HETATM 3993 O HOH A1505 -23.472 -14.503 -32.990 1.00 57.24 O HETATM 3994 O HOH A1506 -6.809 -14.774 -63.217 1.00 74.23 O HETATM 3995 O HOH A1507 -16.270 -65.640 -14.189 1.00 67.42 O HETATM 3996 O HOH A1508 -17.538 -38.612 -36.098 1.00 65.18 O HETATM 3997 O HOH A1509 -16.411 3.638 -72.624 1.00 86.48 O HETATM 3998 O HOH A1510 -0.863 -22.811 -79.755 1.00 62.02 O HETATM 3999 O HOH A1511 -7.900 -8.852 -27.080 1.00 78.45 O HETATM 4000 O HOH A1512 -5.629 -37.134 -41.903 1.00 69.32 O HETATM 4001 O HOH A1513 0.163 -8.807 -67.112 1.00 76.80 O HETATM 4002 O HOH A1514 -0.832 -19.817 -31.364 1.00 57.38 O HETATM 4003 O HOH A1515 -26.881 -4.138 -79.312 1.00 67.73 O HETATM 4004 O HOH D 201 -1.484 -5.111 -24.599 1.00 70.69 O HETATM 4005 O HOH D 202 -24.268 -18.650 -21.861 1.00 64.14 O CONECT 57 2546 CONECT 730 1342 CONECT 1342 730 CONECT 2546 57 CONECT 3030 3574 CONECT 3574 3030 CONECT 3827 3828 3831 CONECT 3828 3827 3829 CONECT 3829 3828 3830 3832 CONECT 3830 3829 CONECT 3831 3827 CONECT 3832 3829 CONECT 3895 3900 3902 CONECT 3896 3897 CONECT 3897 3896 3899 CONECT 3898 3900 3904 CONECT 3899 3897 3901 3904 CONECT 3900 3895 3898 3903 CONECT 3901 3899 CONECT 3902 3895 CONECT 3903 3900 CONECT 3904 3898 3899 CONECT 3905 3907 CONECT 3906 3915 3917 CONECT 3907 3905 3908 CONECT 3908 3907 3909 CONECT 3909 3908 3910 CONECT 3910 3909 3911 CONECT 3911 3910 3912 CONECT 3912 3911 3914 CONECT 3913 3915 3919 CONECT 3914 3912 3916 3919 CONECT 3915 3906 3913 3918 CONECT 3916 3914 CONECT 3917 3906 CONECT 3918 3915 CONECT 3919 3913 3914 CONECT 3920 3925 3927 CONECT 3921 3922 CONECT 3922 3921 3924 CONECT 3923 3925 3929 CONECT 3924 3922 3926 3929 CONECT 3925 3920 3923 3928 CONECT 3926 3924 CONECT 3927 3920 CONECT 3928 3925 CONECT 3929 3923 3924 CONECT 3930 3933 3935 CONECT 3931 3933 3937 CONECT 3932 3934 3937 CONECT 3933 3930 3931 3936 CONECT 3934 3932 CONECT 3935 3930 CONECT 3936 3933 CONECT 3937 3931 3932 CONECT 3938 3946 3948 CONECT 3939 3940 CONECT 3940 3939 3941 CONECT 3941 3940 3942 CONECT 3942 3941 3943 CONECT 3943 3942 3945 CONECT 3944 3946 3950 CONECT 3945 3943 3947 3950 CONECT 3946 3938 3944 3949 CONECT 3947 3945 CONECT 3948 3938 CONECT 3949 3946 CONECT 3950 3944 3945 CONECT 3951 3952 3953 CONECT 3952 3951 3954 CONECT 3953 3951 3955 CONECT 3954 3952 3956 CONECT 3955 3953 CONECT 3956 3954 3957 CONECT 3957 3956 3958 CONECT 3958 3957 3959 CONECT 3959 3958 3960 CONECT 3960 3959 CONECT 3961 3962 3970 CONECT 3962 3961 3963 CONECT 3963 3962 3964 3988 CONECT 3964 3963 3965 CONECT 3965 3964 3966 3970 CONECT 3966 3965 3967 CONECT 3967 3966 3968 CONECT 3968 3967 3969 3974 CONECT 3969 3968 3970 3971 CONECT 3970 3961 3965 3969 3979 CONECT 3971 3969 3972 CONECT 3972 3971 3973 CONECT 3973 3972 3974 3977 3978 CONECT 3974 3968 3973 3975 CONECT 3975 3974 3976 CONECT 3976 3975 3977 CONECT 3977 3973 3976 3980 CONECT 3978 3973 CONECT 3979 3970 CONECT 3980 3977 3981 3982 CONECT 3981 3980 CONECT 3982 3980 3983 CONECT 3983 3982 3984 CONECT 3984 3983 3985 CONECT 3985 3984 3986 3987 CONECT 3986 3985 CONECT 3987 3985 CONECT 3988 3963 MASTER 527 0 8 16 18 0 8 6 3990 3 106 44 END