HEADER MEMBRANE PROTEIN 01-MAY-19 6OS2 TITLE STRUCTURE OF SYNTHETIC NANOBODY-STABILIZED ANGIOTENSIN II TYPE 1 TITLE 2 RECEPTOR BOUND TO TRV026 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: TRV026 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 3 29-JUL-20 6OS2 1 COMPND REMARK HETNAM LINK REVDAT 3 2 1 SITE REVDAT 2 04-MAR-20 6OS2 1 JRNL REVDAT 1 19-FEB-20 6OS2 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. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.17 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.91 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 19379 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.238 REMARK 3 R VALUE (WORKING SET) : 0.233 REMARK 3 FREE R VALUE : 0.285 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.320 REMARK 3 FREE R VALUE TEST SET COUNT : 1811 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 46.9100 - 6.3400 1.00 1464 150 0.1988 0.2428 REMARK 3 2 6.3300 - 5.0300 1.00 1388 144 0.2349 0.2700 REMARK 3 3 5.0300 - 4.3900 1.00 1367 140 0.1868 0.2506 REMARK 3 4 4.3900 - 3.9900 1.00 1360 140 0.1987 0.2565 REMARK 3 5 3.9900 - 3.7100 1.00 1358 140 0.2300 0.2849 REMARK 3 6 3.7100 - 3.4900 1.00 1345 138 0.2392 0.3292 REMARK 3 7 3.4900 - 3.3100 1.00 1354 139 0.2639 0.3101 REMARK 3 8 3.3100 - 3.1700 1.00 1325 136 0.2881 0.3494 REMARK 3 9 3.1700 - 3.0500 1.00 1354 139 0.3083 0.3952 REMARK 3 10 3.0500 - 2.9400 1.00 1328 136 0.3215 0.3635 REMARK 3 11 2.9400 - 2.8500 1.00 1342 138 0.3188 0.3613 REMARK 3 12 2.8500 - 2.7700 1.00 1333 137 0.3211 0.3265 REMARK 3 13 2.7700 - 2.7000 0.98 1303 134 0.3594 0.3980 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.720 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 70.55 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 83.80 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 : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.7611 -11.4328 -57.6442 REMARK 3 T TENSOR REMARK 3 T11: 0.4559 T22: 0.6655 REMARK 3 T33: 0.4304 T12: 0.0409 REMARK 3 T13: 0.0307 T23: 0.0064 REMARK 3 L TENSOR REMARK 3 L11: 1.5758 L22: 1.5702 REMARK 3 L33: 3.0859 L12: -0.0940 REMARK 3 L13: 0.0052 L23: 0.0434 REMARK 3 S TENSOR REMARK 3 S11: 0.0521 S12: 0.2649 S13: 0.2287 REMARK 3 S21: -0.0502 S22: -0.0935 S23: -0.0830 REMARK 3 S31: -0.2475 S32: 0.0544 S33: 0.1066 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 132 THROUGH 165 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.8640 -9.9476 -43.0290 REMARK 3 T TENSOR REMARK 3 T11: 0.5902 T22: 0.7841 REMARK 3 T33: 0.4602 T12: -0.1296 REMARK 3 T13: -0.1090 T23: -0.0107 REMARK 3 L TENSOR REMARK 3 L11: 1.8112 L22: 2.2510 REMARK 3 L33: 3.9127 L12: 0.2144 REMARK 3 L13: -0.7527 L23: -1.3705 REMARK 3 S TENSOR REMARK 3 S11: 0.0268 S12: -0.1145 S13: -0.2150 REMARK 3 S21: 0.6101 S22: -0.2586 S23: -0.4933 REMARK 3 S31: -0.5402 S32: 0.9018 S33: 0.2587 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 166 THROUGH 266 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.9900 -30.0708 -44.5482 REMARK 3 T TENSOR REMARK 3 T11: 0.5112 T22: 0.7283 REMARK 3 T33: 0.4414 T12: -0.0664 REMARK 3 T13: -0.0073 T23: -0.0892 REMARK 3 L TENSOR REMARK 3 L11: 1.1763 L22: 2.4638 REMARK 3 L33: 4.0576 L12: -0.0740 REMARK 3 L13: -0.3149 L23: -1.8908 REMARK 3 S TENSOR REMARK 3 S11: -0.1884 S12: 0.0190 S13: -0.1216 REMARK 3 S21: -0.2735 S22: -0.0382 S23: -0.1672 REMARK 3 S31: 0.7554 S32: -0.4679 S33: 0.2165 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 267 THROUGH 305 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.4322 -50.6531 -12.5445 REMARK 3 T TENSOR REMARK 3 T11: 1.5661 T22: 1.5825 REMARK 3 T33: 1.0058 T12: 0.2702 REMARK 3 T13: -0.2083 T23: 0.1714 REMARK 3 L TENSOR REMARK 3 L11: 5.7983 L22: 1.2122 REMARK 3 L33: 8.9172 L12: -1.9511 REMARK 3 L13: 0.7047 L23: 1.3544 REMARK 3 S TENSOR REMARK 3 S11: 0.0875 S12: 0.2957 S13: 0.2829 REMARK 3 S21: 1.0428 S22: -0.9346 S23: -0.3878 REMARK 3 S31: 2.7766 S32: 2.3233 S33: 0.7677 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 306 THROUGH 1237 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.7114 -44.1604 -13.5037 REMARK 3 T TENSOR REMARK 3 T11: 1.7378 T22: 1.2428 REMARK 3 T33: 0.8648 T12: -0.2721 REMARK 3 T13: -0.1098 T23: 0.1819 REMARK 3 L TENSOR REMARK 3 L11: 4.5622 L22: 4.4203 REMARK 3 L33: 4.0568 L12: 0.4381 REMARK 3 L13: -0.6864 L23: -3.5341 REMARK 3 S TENSOR REMARK 3 S11: -0.1195 S12: -0.7452 S13: -0.8358 REMARK 3 S21: 1.0091 S22: 0.4183 S23: -0.6946 REMARK 3 S31: 1.6123 S32: -1.2896 S33: 0.2588 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1238 THROUGH 1318 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.3037 -22.3053 -54.8352 REMARK 3 T TENSOR REMARK 3 T11: 0.4308 T22: 0.7367 REMARK 3 T33: 0.3965 T12: -0.0401 REMARK 3 T13: -0.0184 T23: -0.0092 REMARK 3 L TENSOR REMARK 3 L11: 2.2305 L22: 2.0257 REMARK 3 L33: 3.2457 L12: -0.8106 REMARK 3 L13: -0.8675 L23: -0.4575 REMARK 3 S TENSOR REMARK 3 S11: -0.1861 S12: -0.2151 S13: 0.0601 REMARK 3 S21: 0.1292 S22: 0.1410 S23: 0.0700 REMARK 3 S31: 0.4233 S32: 0.1559 S33: 0.0574 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.2071 -13.0808 -12.8766 REMARK 3 T TENSOR REMARK 3 T11: 0.8588 T22: 1.0084 REMARK 3 T33: 0.5046 T12: 0.0183 REMARK 3 T13: 0.0191 T23: -0.0606 REMARK 3 L TENSOR REMARK 3 L11: 4.6546 L22: 6.5391 REMARK 3 L33: 8.1270 L12: 3.4397 REMARK 3 L13: 5.7850 L23: 4.9055 REMARK 3 S TENSOR REMARK 3 S11: 0.2666 S12: -1.3821 S13: 0.4751 REMARK 3 S21: 0.5063 S22: -0.4883 S23: 0.3504 REMARK 3 S31: 0.2770 S32: -0.6989 S33: 0.1899 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 45 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.0410 -17.6485 -13.0713 REMARK 3 T TENSOR REMARK 3 T11: 0.6667 T22: 0.8821 REMARK 3 T33: 0.4557 T12: 0.0261 REMARK 3 T13: 0.0358 T23: -0.0091 REMARK 3 L TENSOR REMARK 3 L11: 5.7740 L22: 5.2018 REMARK 3 L33: 6.9266 L12: 1.4757 REMARK 3 L13: 5.4781 L23: 2.1264 REMARK 3 S TENSOR REMARK 3 S11: 0.1809 S12: -0.0872 S13: -0.3911 REMARK 3 S21: -0.1861 S22: -0.0861 S23: -0.2094 REMARK 3 S31: 0.0694 S32: 0.2141 S33: -0.1953 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 99 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.4662 -14.4527 -22.2471 REMARK 3 T TENSOR REMARK 3 T11: 0.7724 T22: 0.9240 REMARK 3 T33: 0.4655 T12: 0.0485 REMARK 3 T13: -0.0917 T23: -0.0235 REMARK 3 L TENSOR REMARK 3 L11: 4.3845 L22: 5.5996 REMARK 3 L33: 6.6490 L12: 4.2932 REMARK 3 L13: 5.5791 L23: 5.5759 REMARK 3 S TENSOR REMARK 3 S11: -0.3284 S12: -0.1535 S13: 0.5150 REMARK 3 S21: 0.6040 S22: -0.2488 S23: 0.4823 REMARK 3 S31: -0.8038 S32: -0.7783 S33: 1.0248 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.5863 -16.6015 -72.7843 REMARK 3 T TENSOR REMARK 3 T11: 0.5214 T22: 0.8774 REMARK 3 T33: 0.3927 T12: 0.0907 REMARK 3 T13: -0.0891 T23: -0.0895 REMARK 3 L TENSOR REMARK 3 L11: 3.4397 L22: 4.7366 REMARK 3 L33: 5.0049 L12: 3.8387 REMARK 3 L13: -3.6136 L23: -4.7724 REMARK 3 S TENSOR REMARK 3 S11: -0.7054 S12: 0.5359 S13: -0.8766 REMARK 3 S21: -0.3945 S22: 1.1443 S23: 0.1150 REMARK 3 S31: 1.7115 S32: 0.8365 S33: -0.4254 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 6OS2 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_1000241241. 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 : 19466 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 46.910 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 7.433 REMARK 200 R MERGE (I) : 0.20200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.8700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7 REMARK 200 DATA REDUNDANCY IN SHELL : 6.91 REMARK 200 R MERGE FOR SHELL (I) : 2.05300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.660 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 6DO1 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 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, 65 MM MGCL2, 26-28% PEG 300, 4.5% 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 29.98000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.67500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 112.95000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.98000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.67500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 112.95000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.98000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.67500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 112.95000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.98000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.67500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 112.95000 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: 5270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23950 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 ARG A 287 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 LEU D 127 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 LYS A 20 CG CD CE NZ REMARK 470 ASN A 188 CG OD1 ND2 REMARK 470 ILE A 193 CG1 CG2 CD1 REMARK 470 ILE A 201 CD1 REMARK 470 GLU A 229 CG CD OE1 OE2 REMARK 470 GLU A 233 CG CD OE1 OE2 REMARK 470 LYS A 240 CG CD CE NZ REMARK 470 GLU A 243 CG CD OE1 OE2 REMARK 470 LYS A 244 CG CD CE NZ REMARK 470 VAL A 251 CG1 CG2 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 LYS A 267 CG CD CE NZ 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 GLN A 296 CG CD OE1 NE2 REMARK 470 ASP A 298 CG OD1 OD2 REMARK 470 LYS A 302 CG CD CE NZ 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 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 A1308 CG CD CE NZ REMARK 470 LYS A1318 CG CD CE NZ REMARK 470 SER D 21 OG REMARK 470 SER D 25 OG 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 82.94 56.02 REMARK 500 PHE A 204 -58.85 -144.58 REMARK 500 ASN A1231 47.29 -153.22 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 1402 REMARK 610 OLC A 1403 REMARK 610 OLC A 1404 REMARK 610 OLC A 1405 REMARK 610 OLC A 1406 REMARK 610 OLC A 1407 DBREF 6OS2 A 2 226 UNP P30556 AGTR1_HUMAN 2 226 DBREF 6OS2 A 227 1226 UNP P0ABE7 C562_ECOLX 24 122 DBREF 6OS2 A 1227 1319 UNP P30556 AGTR1_HUMAN 227 319 DBREF 6OS2 D 1 128 PDB 6OS2 6OS2 1 128 DBREF 6OS2 B 1 8 PDB 6OS2 6OS2 1 8 SEQADV 6OS2 ASP A -6 UNP P30556 EXPRESSION TAG SEQADV 6OS2 TYR A -5 UNP P30556 EXPRESSION TAG SEQADV 6OS2 LYS A -4 UNP P30556 EXPRESSION TAG SEQADV 6OS2 ASP A -3 UNP P30556 EXPRESSION TAG SEQADV 6OS2 ASP A -2 UNP P30556 EXPRESSION TAG SEQADV 6OS2 ASP A -1 UNP P30556 EXPRESSION TAG SEQADV 6OS2 ASP A 0 UNP P30556 EXPRESSION TAG SEQADV 6OS2 LYS A 1 UNP P30556 EXPRESSION TAG SEQADV 6OS2 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 TYR HIS PRO NH2 HET SAR B 1 5 HET NH2 B 8 1 HET NAG A1401 14 HET OLC A1402 10 HET OLC A1403 16 HET OLC A1404 10 HET OLC A1405 8 HET OLC A1406 13 HET OLC A1407 10 HET CLR A1408 28 HETNAM SAR SARCOSINE HETNAM NH2 AMINO GROUP HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 3 NH2 H2 N FORMUL 4 NAG C8 H15 N O6 FORMUL 5 OLC 6(C21 H40 O4) FORMUL 11 CLR C27 H46 O FORMUL 12 HOH *21(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 GLU A 306 1 18 HELIX 11 AB2 LYS A 308 LYS A 320 1 13 HELIX 12 AB3 ASP A 1237 LEU A 1268 1 32 HELIX 13 AB4 ASP A 1273 CYS A 1296 1 24 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 ARG B 2 N TYR A 184 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 MET D 82 N LEU D 18 SHEET 4 AA2 4 THR D 68 ASP D 72 -1 N SER D 70 O TYR D 79 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 2.02 SSBOND 3 CYS D 22 CYS D 95 1555 1555 2.03 LINK ND2 ASN A 176 C1 NAG A1401 1555 1555 1.44 LINK C SAR B 1 N ARG B 2 1555 1555 1.33 LINK C PRO B 7 N NH2 B 8 1555 1555 1.33 CRYST1 59.960 101.350 225.900 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 0.016678 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009867 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004427 0.00000 ATOM 1 N ILE A 11 -11.841 -0.200 -81.722 1.00 92.16 N ANISOU 1 N ILE A 11 12061 14490 8466 -127 1745 3077 N ATOM 2 CA ILE A 11 -11.448 -1.405 -81.002 1.00 90.25 C ANISOU 2 CA ILE A 11 11580 14375 8334 -108 1742 2828 C ATOM 3 C ILE A 11 -10.710 -2.357 -81.936 1.00104.29 C ANISOU 3 C ILE A 11 13222 16481 9923 -86 1879 2778 C ATOM 4 O ILE A 11 -10.516 -2.058 -83.114 1.00114.22 O ANISOU 4 O ILE A 11 14568 17871 10961 -96 1979 2935 O ATOM 5 CB ILE A 11 -12.667 -2.091 -80.364 1.00 89.18 C ANISOU 5 CB ILE A 11 11435 14172 8278 92 1554 2629 C ATOM 6 CG1 ILE A 11 -13.720 -2.403 -81.429 1.00107.15 C ANISOU 6 CG1 ILE A 11 13818 16565 10330 294 1476 2641 C ATOM 7 CG2 ILE A 11 -13.254 -1.216 -79.266 1.00 83.39 C ANISOU 7 CG2 ILE A 11 10801 13129 7754 67 1439 2648 C ATOM 8 CD1 ILE A 11 -14.992 -3.007 -80.877 1.00105.21 C ANISOU 8 CD1 ILE A 11 13559 16266 10151 473 1291 2462 C ATOM 9 N LYS A 12 -10.301 -3.504 -81.404 1.00 91.86 N ANISOU 9 N LYS A 12 11444 15032 8426 -47 1886 2559 N ATOM 10 CA LYS A 12 -9.533 -4.477 -82.166 1.00 86.02 C ANISOU 10 CA LYS A 12 10564 14593 7527 -8 2021 2483 C ATOM 11 C LYS A 12 -10.454 -5.469 -82.865 1.00 79.72 C ANISOU 11 C LYS A 12 9817 13923 6550 219 1937 2344 C ATOM 12 O LYS A 12 -11.530 -5.811 -82.366 1.00 77.13 O ANISOU 12 O LYS A 12 9537 13476 6295 339 1766 2221 O ATOM 13 CB LYS A 12 -8.558 -5.227 -81.256 1.00 81.70 C ANISOU 13 CB LYS A 12 9777 14116 7149 -65 2074 2320 C ATOM 14 N ARG A 13 -10.017 -5.929 -84.035 1.00 83.40 N ANISOU 14 N ARG A 13 10271 14643 6775 266 2063 2360 N ATOM 15 CA ARG A 13 -10.730 -6.935 -84.812 1.00 94.95 C ANISOU 15 CA ARG A 13 11780 16259 8038 462 2001 2215 C ATOM 16 C ARG A 13 -9.971 -8.251 -84.719 1.00 98.32 C ANISOU 16 C ARG A 13 12027 16867 8461 525 2087 1999 C ATOM 17 O ARG A 13 -8.777 -8.306 -85.035 1.00 97.45 O ANISOU 17 O ARG A 13 11798 16927 8301 452 2273 2042 O ATOM 18 CB ARG A 13 -10.882 -6.501 -86.270 1.00107.03 C ANISOU 18 CB ARG A 13 13461 17942 9263 493 2070 2384 C ATOM 19 CG ARG A 13 -11.731 -5.257 -86.467 1.00109.98 C ANISOU 19 CG ARG A 13 14040 18137 9612 475 1970 2602 C ATOM 20 CD ARG A 13 -11.910 -4.950 -87.944 1.00106.88 C ANISOU 20 CD ARG A 13 13804 17915 8890 528 2026 2761 C ATOM 21 NE ARG A 13 -12.711 -3.750 -88.163 1.00110.82 N ANISOU 21 NE ARG A 13 14512 18239 9356 533 1927 2984 N ATOM 22 CZ ARG A 13 -13.021 -3.269 -89.363 1.00127.27 C ANISOU 22 CZ ARG A 13 16771 20423 11164 585 1943 3165 C ATOM 23 NH1 ARG A 13 -13.755 -2.170 -89.470 1.00130.00 N ANISOU 23 NH1 ARG A 13 17311 20584 11498 608 1842 3370 N ATOM 24 NH2 ARG A 13 -12.596 -3.887 -90.456 1.00139.61 N ANISOU 24 NH2 ARG A 13 18324 22271 12451 627 2060 3141 N ATOM 25 N ILE A 14 -10.661 -9.307 -84.288 1.00 94.27 N ANISOU 25 N ILE A 14 11498 16320 8001 662 1954 1770 N ATOM 26 CA ILE A 14 -10.052 -10.611 -84.074 1.00 85.29 C ANISOU 26 CA ILE A 14 10220 15304 6883 744 2011 1551 C ATOM 27 C ILE A 14 -10.823 -11.659 -84.867 1.00 85.68 C ANISOU 27 C ILE A 14 10363 15461 6729 916 1940 1380 C ATOM 28 O ILE A 14 -11.925 -11.417 -85.360 1.00 84.95 O ANISOU 28 O ILE A 14 10418 15335 6523 965 1816 1411 O ATOM 29 CB ILE A 14 -10.001 -10.996 -82.581 1.00 81.61 C ANISOU 29 CB ILE A 14 9640 14661 6708 723 1922 1418 C ATOM 30 CG1 ILE A 14 -11.416 -11.186 -82.031 1.00 83.70 C ANISOU 30 CG1 ILE A 14 10009 14739 7054 790 1709 1323 C ATOM 31 CG2 ILE A 14 -9.259 -9.937 -81.783 1.00 81.38 C ANISOU 31 CG2 ILE A 14 9526 14525 6871 540 1976 1575 C ATOM 32 CD1 ILE A 14 -11.450 -11.669 -80.599 1.00 64.31 C ANISOU 32 CD1 ILE A 14 7461 12120 4855 780 1622 1184 C ATOM 33 N GLN A 15 -10.219 -12.841 -84.979 1.00 93.17 N ANISOU 33 N GLN A 15 11226 16542 7633 1011 2018 1192 N ATOM 34 CA GLN A 15 -10.796 -13.976 -85.694 1.00100.88 C ANISOU 34 CA GLN A 15 12293 17616 8420 1166 1966 995 C ATOM 35 C GLN A 15 -10.997 -15.110 -84.697 1.00 95.42 C ANISOU 35 C GLN A 15 11548 16797 7910 1236 1869 759 C ATOM 36 O GLN A 15 -10.023 -15.710 -84.229 1.00 93.94 O ANISOU 36 O GLN A 15 11232 16644 7816 1266 1969 671 O ATOM 37 CB GLN A 15 -9.891 -14.410 -86.847 1.00107.21 C ANISOU 37 CB GLN A 15 13079 18687 8970 1237 2160 976 C ATOM 38 CG GLN A 15 -10.439 -15.555 -87.686 1.00110.75 C ANISOU 38 CG GLN A 15 13646 19241 9193 1394 2114 765 C ATOM 39 CD GLN A 15 -11.427 -15.091 -88.739 1.00110.76 C ANISOU 39 CD GLN A 15 13826 19308 8950 1405 2026 850 C ATOM 40 OE1 GLN A 15 -11.671 -13.895 -88.894 1.00110.06 O ANISOU 40 OE1 GLN A 15 13780 19187 8851 1312 2010 1082 O ATOM 41 NE2 GLN A 15 -11.997 -16.040 -89.473 1.00109.22 N ANISOU 41 NE2 GLN A 15 13746 19164 8589 1511 1948 657 N ATOM 42 N ASP A 16 -12.254 -15.403 -84.373 1.00 68.40 N ANISOU 42 N ASP A 16 8222 13235 4533 1262 1677 664 N ATOM 43 CA ASP A 16 -12.564 -16.446 -83.405 1.00 70.14 C ANISOU 43 CA ASP A 16 8415 13313 4921 1307 1578 455 C ATOM 44 C ASP A 16 -12.365 -17.820 -84.034 1.00 79.26 C ANISOU 44 C ASP A 16 9620 14579 5918 1441 1620 235 C ATOM 45 O ASP A 16 -12.879 -18.095 -85.123 1.00 78.76 O ANISOU 45 O ASP A 16 9677 14634 5616 1499 1598 183 O ATOM 46 CB ASP A 16 -13.999 -16.294 -82.900 1.00 71.38 C ANISOU 46 CB ASP A 16 8650 13306 5167 1277 1370 430 C ATOM 47 CG ASP A 16 -14.289 -17.161 -81.686 1.00 99.26 C ANISOU 47 CG ASP A 16 12143 16662 8908 1283 1277 259 C ATOM 48 OD1 ASP A 16 -13.368 -17.860 -81.211 1.00106.80 O ANISOU 48 OD1 ASP A 16 13021 17610 9946 1321 1363 168 O ATOM 49 OD2 ASP A 16 -15.440 -17.139 -81.202 1.00106.58 O ANISOU 49 OD2 ASP A 16 13113 17467 9914 1255 1119 223 O ATOM 50 N ASP A 17 -11.616 -18.682 -83.343 1.00 78.39 N ANISOU 50 N ASP A 17 9425 14424 5935 1499 1676 102 N ATOM 51 CA ASP A 17 -11.374 -20.029 -83.852 1.00 78.34 C ANISOU 51 CA ASP A 17 9482 14489 5796 1644 1719 -119 C ATOM 52 C ASP A 17 -12.657 -20.851 -83.858 1.00 83.24 C ANISOU 52 C ASP A 17 10256 14988 6382 1663 1540 -298 C ATOM 53 O ASP A 17 -12.979 -21.512 -84.852 1.00 84.42 O ANISOU 53 O ASP A 17 10532 15235 6308 1738 1534 -427 O ATOM 54 CB ASP A 17 -10.295 -20.720 -83.018 1.00 77.82 C ANISOU 54 CB ASP A 17 9293 14384 5892 1716 1808 -206 C ATOM 55 CG ASP A 17 -8.969 -19.987 -83.057 1.00 83.21 C ANISOU 55 CG ASP A 17 9795 15223 6599 1690 1989 -45 C ATOM 56 OD1 ASP A 17 -8.670 -19.352 -84.090 1.00 85.19 O ANISOU 56 OD1 ASP A 17 10046 15662 6661 1668 2102 75 O ATOM 57 OD2 ASP A 17 -8.226 -20.047 -82.055 1.00 86.56 O ANISOU 57 OD2 ASP A 17 10074 15590 7225 1684 2017 -37 O ATOM 58 N CYS A 18 -13.403 -20.823 -82.751 1.00 73.42 N ANISOU 58 N CYS A 18 9002 13540 5353 1586 1395 -311 N ATOM 59 CA CYS A 18 -14.668 -21.541 -82.613 1.00 76.64 C ANISOU 59 CA CYS A 18 9529 13831 5759 1569 1221 -467 C ATOM 60 C CYS A 18 -15.763 -20.510 -82.361 1.00 63.42 C ANISOU 60 C CYS A 18 7846 12103 4146 1457 1085 -327 C ATOM 61 O CYS A 18 -16.123 -20.241 -81.206 1.00 76.30 O ANISOU 61 O CYS A 18 9418 13572 6001 1387 1008 -291 O ATOM 62 CB CYS A 18 -14.605 -22.572 -81.487 1.00 81.78 C ANISOU 62 CB CYS A 18 10180 14290 6604 1589 1178 -622 C ATOM 63 SG CYS A 18 -13.042 -23.487 -81.370 1.00 79.43 S ANISOU 63 SG CYS A 18 9834 14025 6321 1742 1354 -723 S ATOM 64 N PRO A 19 -16.316 -19.911 -83.421 1.00 81.36 N ANISOU 64 N PRO A 19 10180 14514 6218 1452 1051 -244 N ATOM 65 CA PRO A 19 -17.317 -18.849 -83.229 1.00 70.69 C ANISOU 65 CA PRO A 19 8818 13121 4919 1377 926 -94 C ATOM 66 C PRO A 19 -18.671 -19.349 -82.750 1.00 74.87 C ANISOU 66 C PRO A 19 9380 13548 5519 1336 737 -221 C ATOM 67 O PRO A 19 -19.524 -18.521 -82.406 1.00 75.13 O ANISOU 67 O PRO A 19 9382 13535 5628 1289 631 -111 O ATOM 68 CB PRO A 19 -17.424 -18.216 -84.622 1.00 69.64 C ANISOU 68 CB PRO A 19 8758 13188 4515 1410 951 21 C ATOM 69 CG PRO A 19 -17.059 -19.320 -85.555 1.00 67.88 C ANISOU 69 CG PRO A 19 8620 13098 4074 1494 1013 -160 C ATOM 70 CD PRO A 19 -16.013 -20.139 -84.844 1.00 81.40 C ANISOU 70 CD PRO A 19 10271 14727 5929 1530 1131 -275 C ATOM 71 N LYS A 20 -18.899 -20.660 -82.717 1.00 75.17 N ANISOU 71 N LYS A 20 9481 13548 5533 1352 695 -446 N ATOM 72 CA LYS A 20 -20.159 -21.220 -82.252 1.00 78.99 C ANISOU 72 CA LYS A 20 9989 13941 6084 1287 524 -575 C ATOM 73 C LYS A 20 -20.049 -21.873 -80.882 1.00 74.21 C ANISOU 73 C LYS A 20 9345 13128 5725 1242 518 -665 C ATOM 74 O LYS A 20 -21.056 -22.366 -80.362 1.00 75.33 O ANISOU 74 O LYS A 20 9499 13182 5943 1169 392 -766 O ATOM 75 CB LYS A 20 -20.693 -22.239 -83.266 1.00 64.19 C ANISOU 75 CB LYS A 20 8239 12165 3985 1304 455 -771 C ATOM 76 N ALA A 21 -18.860 -21.890 -80.285 1.00 65.19 N ANISOU 76 N ALA A 21 8152 11917 4701 1281 649 -626 N ATOM 77 CA ALA A 21 -18.672 -22.521 -78.985 1.00 65.90 C ANISOU 77 CA ALA A 21 8215 11815 5008 1254 644 -701 C ATOM 78 C ALA A 21 -19.356 -21.699 -77.900 1.00 72.10 C ANISOU 78 C ALA A 21 8913 12494 5988 1163 562 -589 C ATOM 79 O ALA A 21 -19.038 -20.521 -77.708 1.00 81.68 O ANISOU 79 O ALA A 21 10046 13728 7261 1152 601 -410 O ATOM 80 CB ALA A 21 -17.183 -22.675 -78.684 1.00 62.94 C ANISOU 80 CB ALA A 21 7791 11430 4695 1335 798 -677 C ATOM 81 N GLY A 22 -20.296 -22.321 -77.189 1.00 66.80 N ANISOU 81 N GLY A 22 8264 11705 5411 1092 452 -697 N ATOM 82 CA GLY A 22 -21.009 -21.675 -76.113 1.00 62.73 C ANISOU 82 CA GLY A 22 7669 11093 5072 1013 379 -617 C ATOM 83 C GLY A 22 -22.267 -20.940 -76.523 1.00 71.78 C ANISOU 83 C GLY A 22 8785 12330 6159 975 264 -557 C ATOM 84 O GLY A 22 -23.085 -20.614 -75.656 1.00 72.13 O ANISOU 84 O GLY A 22 8768 12302 6336 914 190 -532 O ATOM 85 N ARG A 23 -22.447 -20.667 -77.814 1.00 77.69 N ANISOU 85 N ARG A 23 9570 13245 6704 1019 247 -531 N ATOM 86 CA ARG A 23 -23.635 -19.970 -78.305 1.00 67.09 C ANISOU 86 CA ARG A 23 8197 12012 5284 1007 126 -468 C ATOM 87 C ARG A 23 -24.773 -20.975 -78.425 1.00 71.92 C ANISOU 87 C ARG A 23 8832 12650 5845 935 -4 -650 C ATOM 88 O ARG A 23 -24.933 -21.653 -79.442 1.00 87.50 O ANISOU 88 O ARG A 23 10885 14732 7629 941 -40 -765 O ATOM 89 CB ARG A 23 -23.353 -19.284 -79.637 1.00 68.85 C ANISOU 89 CB ARG A 23 8460 12407 5293 1084 154 -359 C ATOM 90 CG ARG A 23 -22.688 -17.920 -79.514 1.00 65.77 C ANISOU 90 CG ARG A 23 8031 11999 4959 1122 240 -132 C ATOM 91 CD ARG A 23 -21.193 -18.034 -79.270 1.00 70.80 C ANISOU 91 CD ARG A 23 8668 12582 5651 1135 406 -106 C ATOM 92 NE ARG A 23 -20.599 -16.742 -78.941 1.00 75.35 N ANISOU 92 NE ARG A 23 9199 13112 6318 1129 480 101 N ATOM 93 CZ ARG A 23 -19.296 -16.540 -78.775 1.00 77.87 C ANISOU 93 CZ ARG A 23 9490 13412 6684 1125 622 167 C ATOM 94 NH1 ARG A 23 -18.843 -15.330 -78.474 1.00 72.57 N ANISOU 94 NH1 ARG A 23 8785 12691 6096 1093 676 352 N ATOM 95 NH2 ARG A 23 -18.445 -17.547 -78.914 1.00 81.98 N ANISOU 95 NH2 ARG A 23 10015 13966 7168 1154 710 45 N ATOM 96 N HIS A 24 -25.573 -21.073 -77.366 1.00 64.79 N ANISOU 96 N HIS A 24 7858 11651 5108 856 -74 -680 N ATOM 97 CA HIS A 24 -26.732 -21.953 -77.328 1.00 56.74 C ANISOU 97 CA HIS A 24 6834 10655 4068 753 -197 -839 C ATOM 98 C HIS A 24 -27.939 -21.174 -76.830 1.00 63.32 C ANISOU 98 C HIS A 24 7533 11540 4986 723 -301 -763 C ATOM 99 O HIS A 24 -27.814 -20.307 -75.960 1.00 61.55 O ANISOU 99 O HIS A 24 7239 11234 4915 753 -259 -635 O ATOM 100 CB HIS A 24 -26.478 -23.171 -76.435 1.00 65.79 C ANISOU 100 CB HIS A 24 8041 11621 5336 668 -161 -987 C ATOM 101 CG HIS A 24 -25.454 -24.116 -76.982 1.00 76.83 C ANISOU 101 CG HIS A 24 9581 12973 6637 714 -77 -1097 C ATOM 102 ND1 HIS A 24 -25.761 -25.401 -77.375 1.00 86.32 N ANISOU 102 ND1 HIS A 24 10900 14147 7750 646 -124 -1296 N ATOM 103 CD2 HIS A 24 -24.130 -23.958 -77.214 1.00 81.78 C ANISOU 103 CD2 HIS A 24 10248 13583 7240 825 54 -1040 C ATOM 104 CE1 HIS A 24 -24.668 -25.997 -77.817 1.00 87.49 C ANISOU 104 CE1 HIS A 24 11166 14253 7822 735 -23 -1361 C ATOM 105 NE2 HIS A 24 -23.664 -25.143 -77.730 1.00 85.13 N ANISOU 105 NE2 HIS A 24 10810 13974 7561 846 88 -1206 N ATOM 106 N ASN A 25 -29.111 -21.492 -77.387 1.00 76.34 N ANISOU 106 N ASN A 25 9142 13333 6531 665 -437 -849 N ATOM 107 CA ASN A 25 -30.312 -20.726 -77.070 1.00 80.72 C ANISOU 107 CA ASN A 25 9547 13983 7141 663 -543 -777 C ATOM 108 C ASN A 25 -30.773 -20.968 -75.637 1.00 70.97 C ANISOU 108 C ASN A 25 8228 12617 6120 567 -532 -813 C ATOM 109 O ASN A 25 -31.268 -20.047 -74.977 1.00 80.84 O ANISOU 109 O ASN A 25 9365 13871 7481 612 -544 -703 O ATOM 110 CB ASN A 25 -31.427 -21.062 -78.059 1.00 80.58 C ANISOU 110 CB ASN A 25 9487 14182 6947 621 -700 -869 C ATOM 111 CG ASN A 25 -31.143 -20.545 -79.457 1.00 92.11 C ANISOU 111 CG ASN A 25 11014 15805 8180 739 -727 -795 C ATOM 112 OD1 ASN A 25 -31.190 -21.296 -80.430 1.00105.57 O ANISOU 112 OD1 ASN A 25 12801 17613 9698 702 -779 -921 O ATOM 113 ND2 ASN A 25 -30.844 -19.255 -79.562 1.00 86.19 N ANISOU 113 ND2 ASN A 25 10242 15071 7436 877 -688 -591 N ATOM 114 N TYR A 26 -30.623 -22.197 -75.133 1.00 63.62 N ANISOU 114 N TYR A 26 7365 11564 5245 442 -505 -963 N ATOM 115 CA TYR A 26 -31.007 -22.467 -73.752 1.00 77.04 C ANISOU 115 CA TYR A 26 9003 13135 7134 344 -482 -988 C ATOM 116 C TYR A 26 -30.085 -21.776 -72.755 1.00 79.76 C ANISOU 116 C TYR A 26 9355 13317 7632 422 -363 -861 C ATOM 117 O TYR A 26 -30.471 -21.594 -71.596 1.00 78.94 O ANISOU 117 O TYR A 26 9178 13137 7677 378 -347 -838 O ATOM 118 CB TYR A 26 -31.043 -23.975 -73.489 1.00 82.87 C ANISOU 118 CB TYR A 26 9842 13763 7882 187 -482 -1169 C ATOM 119 CG TYR A 26 -29.730 -24.694 -73.707 1.00 93.10 C ANISOU 119 CG TYR A 26 11318 14910 9144 230 -385 -1222 C ATOM 120 CD1 TYR A 26 -29.413 -25.242 -74.943 1.00 99.98 C ANISOU 120 CD1 TYR A 26 12303 15851 9832 255 -406 -1316 C ATOM 121 CD2 TYR A 26 -28.815 -24.841 -72.672 1.00 88.45 C ANISOU 121 CD2 TYR A 26 10784 14125 8698 254 -276 -1184 C ATOM 122 CE1 TYR A 26 -28.218 -25.907 -75.145 1.00101.05 C ANISOU 122 CE1 TYR A 26 12596 15863 9935 317 -309 -1372 C ATOM 123 CE2 TYR A 26 -27.617 -25.503 -72.864 1.00 81.84 C ANISOU 123 CE2 TYR A 26 10092 13171 7832 315 -190 -1233 C ATOM 124 CZ TYR A 26 -27.323 -26.034 -74.102 1.00 91.69 C ANISOU 124 CZ TYR A 26 11445 14490 8902 353 -202 -1327 C ATOM 125 OH TYR A 26 -26.132 -26.694 -74.298 1.00 93.93 O ANISOU 125 OH TYR A 26 11867 14669 9154 436 -108 -1381 O ATOM 126 N ILE A 27 -28.883 -21.386 -73.181 1.00 77.63 N ANISOU 126 N ILE A 27 9169 13006 7323 529 -279 -783 N ATOM 127 CA ILE A 27 -28.000 -20.605 -72.322 1.00 71.21 C ANISOU 127 CA ILE A 27 8349 12063 6644 595 -179 -657 C ATOM 128 C ILE A 27 -28.436 -19.146 -72.289 1.00 66.10 C ANISOU 128 C ILE A 27 7609 11481 6025 680 -204 -500 C ATOM 129 O ILE A 27 -28.439 -18.510 -71.230 1.00 68.64 O ANISOU 129 O ILE A 27 7883 11705 6492 689 -170 -429 O ATOM 130 CB ILE A 27 -26.542 -20.753 -72.792 1.00 66.34 C ANISOU 130 CB ILE A 27 7834 11395 5975 663 -76 -634 C ATOM 131 CG1 ILE A 27 -26.010 -22.144 -72.451 1.00 68.85 C ANISOU 131 CG1 ILE A 27 8250 11593 6315 605 -35 -779 C ATOM 132 CG2 ILE A 27 -25.659 -19.670 -72.184 1.00 49.85 C ANISOU 132 CG2 ILE A 27 5720 9226 3996 729 11 -479 C ATOM 133 CD1 ILE A 27 -24.601 -22.375 -72.920 1.00 77.27 C ANISOU 133 CD1 ILE A 27 9399 12633 7327 692 68 -772 C ATOM 134 N PHE A 28 -28.824 -18.597 -73.442 1.00 77.29 N ANISOU 134 N PHE A 28 9013 13059 7296 752 -267 -444 N ATOM 135 CA PHE A 28 -29.238 -17.203 -73.529 1.00 80.17 C ANISOU 135 CA PHE A 28 9315 13475 7670 857 -297 -286 C ATOM 136 C PHE A 28 -30.526 -16.915 -72.768 1.00 70.19 C ANISOU 136 C PHE A 28 7921 12246 6503 844 -374 -298 C ATOM 137 O PHE A 28 -30.847 -15.741 -72.552 1.00 67.70 O ANISOU 137 O PHE A 28 7559 11930 6234 945 -386 -172 O ATOM 138 CB PHE A 28 -29.403 -16.803 -74.996 1.00 81.32 C ANISOU 138 CB PHE A 28 9491 13795 7614 941 -357 -225 C ATOM 139 CG PHE A 28 -28.146 -16.947 -75.804 1.00 84.81 C ANISOU 139 CG PHE A 28 10052 14228 7944 967 -266 -196 C ATOM 140 CD1 PHE A 28 -26.913 -16.667 -75.241 1.00 73.91 C ANISOU 140 CD1 PHE A 28 8718 12698 6665 970 -135 -128 C ATOM 141 CD2 PHE A 28 -28.196 -17.372 -77.121 1.00 86.81 C ANISOU 141 CD2 PHE A 28 10362 14639 7983 986 -309 -243 C ATOM 142 CE1 PHE A 28 -25.754 -16.801 -75.978 1.00 76.47 C ANISOU 142 CE1 PHE A 28 9127 13041 6888 995 -41 -102 C ATOM 143 CE2 PHE A 28 -27.040 -17.508 -77.863 1.00 79.65 C ANISOU 143 CE2 PHE A 28 9558 13741 6964 1018 -210 -219 C ATOM 144 CZ PHE A 28 -25.817 -17.222 -77.290 1.00 76.26 C ANISOU 144 CZ PHE A 28 9157 13173 6645 1023 -70 -146 C ATOM 145 N VAL A 29 -31.264 -17.944 -72.358 1.00 67.45 N ANISOU 145 N VAL A 29 7516 11927 6183 724 -421 -445 N ATOM 146 CA VAL A 29 -32.496 -17.774 -71.604 1.00 70.12 C ANISOU 146 CA VAL A 29 7709 12324 6610 696 -480 -468 C ATOM 147 C VAL A 29 -32.312 -18.135 -70.135 1.00 70.09 C ANISOU 147 C VAL A 29 7701 12152 6778 608 -399 -509 C ATOM 148 O VAL A 29 -32.770 -17.407 -69.251 1.00 77.82 O ANISOU 148 O VAL A 29 8599 13105 7866 652 -383 -452 O ATOM 149 CB VAL A 29 -33.640 -18.599 -72.233 1.00 70.57 C ANISOU 149 CB VAL A 29 7677 12574 6563 602 -603 -595 C ATOM 150 CG1 VAL A 29 -34.903 -18.483 -71.396 1.00 64.48 C ANISOU 150 CG1 VAL A 29 6727 11885 5889 559 -651 -623 C ATOM 151 CG2 VAL A 29 -33.900 -18.146 -73.660 1.00 78.64 C ANISOU 151 CG2 VAL A 29 8696 13785 7400 703 -700 -546 C ATOM 152 N MET A 30 -31.637 -19.250 -69.853 1.00 68.91 N ANISOU 152 N MET A 30 7650 11885 6647 497 -345 -607 N ATOM 153 CA MET A 30 -31.527 -19.730 -68.479 1.00 71.30 C ANISOU 153 CA MET A 30 7961 12038 7093 406 -279 -649 C ATOM 154 C MET A 30 -30.469 -18.966 -67.691 1.00 73.56 C ANISOU 154 C MET A 30 8305 12163 7483 485 -182 -543 C ATOM 155 O MET A 30 -30.692 -18.623 -66.524 1.00 78.17 O ANISOU 155 O MET A 30 8846 12673 8184 473 -147 -520 O ATOM 156 CB MET A 30 -31.220 -21.228 -68.473 1.00 71.98 C ANISOU 156 CB MET A 30 8150 12045 7156 269 -266 -787 C ATOM 157 CG MET A 30 -31.210 -21.864 -67.093 1.00 84.71 C ANISOU 157 CG MET A 30 9785 13506 8895 162 -208 -830 C ATOM 158 SD MET A 30 -31.237 -23.666 -67.165 1.00 95.27 S ANISOU 158 SD MET A 30 11248 14756 10193 -15 -219 -997 S ATOM 159 CE MET A 30 -29.738 -23.996 -68.088 1.00 86.09 C ANISOU 159 CE MET A 30 10254 13513 8944 94 -175 -1006 C ATOM 160 N ILE A 31 -29.315 -18.692 -68.305 1.00 62.13 N ANISOU 160 N ILE A 31 6949 10671 5988 557 -137 -483 N ATOM 161 CA ILE A 31 -28.228 -18.030 -67.580 1.00 65.34 C ANISOU 161 CA ILE A 31 7402 10932 6491 605 -51 -391 C ATOM 162 C ILE A 31 -28.603 -16.619 -67.132 1.00 76.16 C ANISOU 162 C ILE A 31 8714 12295 7929 688 -53 -275 C ATOM 163 O ILE A 31 -28.340 -16.276 -65.969 1.00 84.72 O ANISOU 163 O ILE A 31 9801 13257 9131 677 -5 -253 O ATOM 164 CB ILE A 31 -26.935 -18.066 -68.414 1.00 64.76 C ANISOU 164 CB ILE A 31 7417 10845 6344 653 3 -353 C ATOM 165 CG1 ILE A 31 -26.481 -19.511 -68.624 1.00 65.82 C ANISOU 165 CG1 ILE A 31 7627 10950 6431 591 19 -481 C ATOM 166 CG2 ILE A 31 -25.836 -17.266 -67.735 1.00 51.15 C ANISOU 166 CG2 ILE A 31 5718 9000 4717 689 83 -250 C ATOM 167 CD1 ILE A 31 -26.113 -20.221 -67.342 1.00 60.52 C ANISOU 167 CD1 ILE A 31 6989 10125 5879 525 62 -536 C ATOM 168 N PRO A 32 -29.195 -15.760 -67.977 1.00 71.75 N ANISOU 168 N PRO A 32 8115 11850 7298 781 -109 -199 N ATOM 169 CA PRO A 32 -29.617 -14.443 -67.464 1.00 64.68 C ANISOU 169 CA PRO A 32 7181 10919 6474 875 -111 -97 C ATOM 170 C PRO A 32 -30.653 -14.534 -66.357 1.00 70.42 C ANISOU 170 C PRO A 32 7811 11651 7295 848 -126 -160 C ATOM 171 O PRO A 32 -30.640 -13.711 -65.433 1.00 63.62 O ANISOU 171 O PRO A 32 6952 10688 6531 895 -87 -111 O ATOM 172 CB PRO A 32 -30.176 -13.745 -68.712 1.00 53.02 C ANISOU 172 CB PRO A 32 5684 9585 4877 987 -184 -16 C ATOM 173 CG PRO A 32 -29.499 -14.412 -69.848 1.00 67.37 C ANISOU 173 CG PRO A 32 7568 11467 6563 954 -183 -36 C ATOM 174 CD PRO A 32 -29.369 -15.845 -69.438 1.00 73.08 C ANISOU 174 CD PRO A 32 8292 12168 7306 823 -167 -189 C ATOM 175 N THR A 33 -31.558 -15.514 -66.427 1.00 78.33 N ANISOU 175 N THR A 33 8730 12771 8263 764 -177 -271 N ATOM 176 CA THR A 33 -32.530 -15.701 -65.355 1.00 73.04 C ANISOU 176 CA THR A 33 7954 12122 7674 715 -175 -333 C ATOM 177 C THR A 33 -31.842 -16.105 -64.056 1.00 74.13 C ANISOU 177 C THR A 33 8162 12085 7917 630 -87 -365 C ATOM 178 O THR A 33 -32.230 -15.651 -62.972 1.00 72.61 O ANISOU 178 O THR A 33 7929 11850 7809 646 -51 -358 O ATOM 179 CB THR A 33 -33.570 -16.746 -65.764 1.00 67.07 C ANISOU 179 CB THR A 33 7096 11533 6854 607 -246 -446 C ATOM 180 OG1 THR A 33 -34.300 -16.275 -66.904 1.00 73.97 O ANISOU 180 OG1 THR A 33 7887 12594 7625 700 -344 -413 O ATOM 181 CG2 THR A 33 -34.543 -17.018 -64.625 1.00 61.84 C ANISOU 181 CG2 THR A 33 6317 10906 6274 530 -227 -508 C ATOM 182 N LEU A 34 -30.810 -16.947 -64.146 1.00 69.14 N ANISOU 182 N LEU A 34 7639 11358 7273 553 -53 -399 N ATOM 183 CA LEU A 34 -30.077 -17.349 -62.950 1.00 64.62 C ANISOU 183 CA LEU A 34 7139 10626 6788 488 19 -420 C ATOM 184 C LEU A 34 -29.314 -16.177 -62.346 1.00 67.94 C ANISOU 184 C LEU A 34 7604 10931 7280 573 66 -324 C ATOM 185 O LEU A 34 -29.287 -16.014 -61.120 1.00 65.39 O ANISOU 185 O LEU A 34 7289 10519 7036 550 107 -331 O ATOM 186 CB LEU A 34 -29.125 -18.497 -63.281 1.00 58.73 C ANISOU 186 CB LEU A 34 6497 9812 6005 419 37 -475 C ATOM 187 CG LEU A 34 -29.788 -19.840 -63.588 1.00 62.07 C ANISOU 187 CG LEU A 34 6920 10289 6373 300 0 -592 C ATOM 188 CD1 LEU A 34 -28.752 -20.875 -63.998 1.00 66.06 C ANISOU 188 CD1 LEU A 34 7555 10708 6838 271 21 -644 C ATOM 189 CD2 LEU A 34 -30.575 -20.315 -62.381 1.00 58.60 C ANISOU 189 CD2 LEU A 34 6441 9821 6003 192 18 -643 C ATOM 190 N TYR A 35 -28.687 -15.350 -63.189 1.00 71.20 N ANISOU 190 N TYR A 35 8053 11342 7657 660 63 -234 N ATOM 191 CA TYR A 35 -27.997 -14.165 -62.688 1.00 67.85 C ANISOU 191 CA TYR A 35 7679 10802 7299 720 103 -142 C ATOM 192 C TYR A 35 -28.952 -13.230 -61.959 1.00 72.06 C ANISOU 192 C TYR A 35 8163 11327 7889 788 95 -123 C ATOM 193 O TYR A 35 -28.556 -12.566 -60.994 1.00 63.80 O ANISOU 193 O TYR A 35 7165 10157 6920 798 135 -98 O ATOM 194 CB TYR A 35 -27.311 -13.424 -63.837 1.00 65.09 C ANISOU 194 CB TYR A 35 7376 10465 6890 788 101 -39 C ATOM 195 CG TYR A 35 -26.101 -14.130 -64.410 1.00 67.93 C ANISOU 195 CG TYR A 35 7788 10817 7203 739 136 -45 C ATOM 196 CD1 TYR A 35 -25.488 -15.172 -63.727 1.00 62.07 C ANISOU 196 CD1 TYR A 35 7068 10016 6499 661 167 -124 C ATOM 197 CD2 TYR A 35 -25.565 -13.745 -65.633 1.00 61.22 C ANISOU 197 CD2 TYR A 35 6970 10025 6266 783 142 33 C ATOM 198 CE1 TYR A 35 -24.380 -15.814 -64.249 1.00 55.52 C ANISOU 198 CE1 TYR A 35 6279 9187 5627 645 202 -134 C ATOM 199 CE2 TYR A 35 -24.458 -14.381 -66.162 1.00 59.04 C ANISOU 199 CE2 TYR A 35 6730 9762 5942 753 186 22 C ATOM 200 CZ TYR A 35 -23.870 -15.415 -65.466 1.00 58.46 C ANISOU 200 CZ TYR A 35 6667 9632 5914 692 216 -65 C ATOM 201 OH TYR A 35 -22.767 -16.052 -65.989 1.00 72.18 O ANISOU 201 OH TYR A 35 8432 11390 7604 688 263 -81 O ATOM 202 N SER A 36 -30.210 -13.166 -62.401 1.00 76.52 N ANISOU 202 N SER A 36 8630 12032 8412 841 43 -140 N ATOM 203 CA SER A 36 -31.191 -12.332 -61.715 1.00 75.16 C ANISOU 203 CA SER A 36 8393 11874 8290 929 41 -132 C ATOM 204 C SER A 36 -31.561 -12.918 -60.359 1.00 69.19 C ANISOU 204 C SER A 36 7600 11091 7597 844 88 -221 C ATOM 205 O SER A 36 -31.796 -12.174 -59.400 1.00 71.22 O ANISOU 205 O SER A 36 7863 11282 7914 901 125 -215 O ATOM 206 CB SER A 36 -32.434 -12.161 -62.587 1.00 80.25 C ANISOU 206 CB SER A 36 8916 12708 8866 1018 -34 -127 C ATOM 207 OG SER A 36 -32.112 -11.529 -63.814 1.00 87.25 O ANISOU 207 OG SER A 36 9853 13617 9681 1110 -77 -30 O ATOM 208 N ILE A 37 -31.620 -14.248 -60.258 1.00 60.15 N ANISOU 208 N ILE A 37 6433 9991 6431 707 89 -303 N ATOM 209 CA ILE A 37 -31.894 -14.881 -58.973 1.00 61.96 C ANISOU 209 CA ILE A 37 6650 10185 6708 609 140 -373 C ATOM 210 C ILE A 37 -30.737 -14.652 -58.009 1.00 64.50 C ANISOU 210 C ILE A 37 7097 10325 7087 592 195 -351 C ATOM 211 O ILE A 37 -30.945 -14.333 -56.832 1.00 68.82 O ANISOU 211 O ILE A 37 7650 10819 7679 593 240 -368 O ATOM 212 CB ILE A 37 -32.182 -16.381 -59.167 1.00 59.60 C ANISOU 212 CB ILE A 37 6327 9950 6369 457 126 -457 C ATOM 213 CG1 ILE A 37 -33.418 -16.576 -60.047 1.00 50.35 C ANISOU 213 CG1 ILE A 37 5013 8980 5140 455 60 -492 C ATOM 214 CG2 ILE A 37 -32.365 -17.070 -57.822 1.00 53.31 C ANISOU 214 CG2 ILE A 37 5545 9096 5613 344 186 -512 C ATOM 215 CD1 ILE A 37 -33.746 -18.027 -60.332 1.00 52.58 C ANISOU 215 CD1 ILE A 37 5284 9318 5378 285 37 -583 C ATOM 216 N ILE A 38 -29.501 -14.805 -58.491 1.00 68.76 N ANISOU 216 N ILE A 38 7729 10779 7616 576 191 -315 N ATOM 217 CA ILE A 38 -28.333 -14.544 -57.654 1.00 50.02 C ANISOU 217 CA ILE A 38 5455 8257 5294 559 229 -291 C ATOM 218 C ILE A 38 -28.305 -13.085 -57.219 1.00 58.31 C ANISOU 218 C ILE A 38 6530 9234 6389 650 242 -235 C ATOM 219 O ILE A 38 -27.898 -12.763 -56.096 1.00 74.89 O ANISOU 219 O ILE A 38 8687 11233 8535 631 273 -246 O ATOM 220 CB ILE A 38 -27.045 -14.938 -58.401 1.00 47.74 C ANISOU 220 CB ILE A 38 5229 7929 4982 537 223 -260 C ATOM 221 CG1 ILE A 38 -27.089 -16.415 -58.802 1.00 58.60 C ANISOU 221 CG1 ILE A 38 6605 9351 6309 461 212 -329 C ATOM 222 CG2 ILE A 38 -25.815 -14.659 -57.547 1.00 48.21 C ANISOU 222 CG2 ILE A 38 5362 7861 5093 515 251 -234 C ATOM 223 CD1 ILE A 38 -25.915 -16.849 -59.652 1.00 40.93 C ANISOU 223 CD1 ILE A 38 4419 7098 4035 467 213 -311 C ATOM 224 N PHE A 39 -28.750 -12.181 -58.094 1.00 57.66 N ANISOU 224 N PHE A 39 6421 9198 6289 753 214 -178 N ATOM 225 CA PHE A 39 -28.749 -10.760 -57.765 1.00 54.05 C ANISOU 225 CA PHE A 39 6015 8646 5874 851 225 -122 C ATOM 226 C PHE A 39 -29.743 -10.450 -56.652 1.00 54.68 C ANISOU 226 C PHE A 39 6058 8732 5986 897 252 -180 C ATOM 227 O PHE A 39 -29.398 -9.787 -55.667 1.00 61.95 O ANISOU 227 O PHE A 39 7058 9529 6952 907 285 -188 O ATOM 228 CB PHE A 39 -29.059 -9.936 -59.015 1.00 62.54 C ANISOU 228 CB PHE A 39 7084 9767 6911 964 186 -36 C ATOM 229 CG PHE A 39 -29.055 -8.453 -58.781 1.00 70.87 C ANISOU 229 CG PHE A 39 8223 10697 8008 1073 194 30 C ATOM 230 CD1 PHE A 39 -27.862 -7.755 -58.708 1.00 68.41 C ANISOU 230 CD1 PHE A 39 8035 10227 7730 1033 214 93 C ATOM 231 CD2 PHE A 39 -30.244 -7.757 -58.637 1.00 71.27 C ANISOU 231 CD2 PHE A 39 8228 10786 8063 1216 182 26 C ATOM 232 CE1 PHE A 39 -27.853 -6.390 -58.492 1.00 69.21 C ANISOU 232 CE1 PHE A 39 8240 10185 7871 1117 220 150 C ATOM 233 CE2 PHE A 39 -30.242 -6.391 -58.421 1.00 72.94 C ANISOU 233 CE2 PHE A 39 8545 10856 8314 1332 190 83 C ATOM 234 CZ PHE A 39 -29.044 -5.707 -58.349 1.00 72.05 C ANISOU 234 CZ PHE A 39 8581 10559 8235 1274 209 144 C ATOM 235 N VAL A 40 -30.983 -10.923 -56.789 1.00 63.06 N ANISOU 235 N VAL A 40 6993 9949 7019 920 242 -227 N ATOM 236 CA VAL A 40 -32.005 -10.635 -55.786 1.00 65.47 C ANISOU 236 CA VAL A 40 7235 10294 7345 973 281 -282 C ATOM 237 C VAL A 40 -31.654 -11.301 -54.460 1.00 67.22 C ANISOU 237 C VAL A 40 7502 10453 7585 853 337 -347 C ATOM 238 O VAL A 40 -31.745 -10.682 -53.393 1.00 63.91 O ANISOU 238 O VAL A 40 7130 9962 7191 895 383 -373 O ATOM 239 CB VAL A 40 -33.391 -11.075 -56.289 1.00 59.68 C ANISOU 239 CB VAL A 40 6326 9776 6574 1004 256 -316 C ATOM 240 CG1 VAL A 40 -34.440 -10.863 -55.207 1.00 46.73 C ANISOU 240 CG1 VAL A 40 4597 8206 4952 1052 313 -377 C ATOM 241 CG2 VAL A 40 -33.765 -10.314 -57.552 1.00 47.21 C ANISOU 241 CG2 VAL A 40 4708 8265 4964 1148 189 -244 C ATOM 242 N VAL A 41 -31.246 -12.570 -54.506 1.00 68.53 N ANISOU 242 N VAL A 41 7671 10639 7729 712 333 -374 N ATOM 243 CA VAL A 41 -30.906 -13.285 -53.280 1.00 61.33 C ANISOU 243 CA VAL A 41 6814 9666 6822 602 380 -421 C ATOM 244 C VAL A 41 -29.633 -12.717 -52.662 1.00 68.30 C ANISOU 244 C VAL A 41 7835 10381 7735 603 384 -394 C ATOM 245 O VAL A 41 -29.511 -12.621 -51.435 1.00 74.54 O ANISOU 245 O VAL A 41 8682 11110 8529 578 422 -428 O ATOM 246 CB VAL A 41 -30.780 -14.794 -53.563 1.00 53.41 C ANISOU 246 CB VAL A 41 5802 8706 5788 464 368 -450 C ATOM 247 CG1 VAL A 41 -30.293 -15.534 -52.330 1.00 65.25 C ANISOU 247 CG1 VAL A 41 7387 10120 7284 362 409 -479 C ATOM 248 CG2 VAL A 41 -32.115 -15.357 -54.025 1.00 56.02 C ANISOU 248 CG2 VAL A 41 5990 9206 6087 430 363 -491 C ATOM 249 N GLY A 42 -28.672 -12.318 -53.497 1.00 66.05 N ANISOU 249 N GLY A 42 7601 10032 7464 623 346 -334 N ATOM 250 CA GLY A 42 -27.420 -11.799 -52.971 1.00 52.45 C ANISOU 250 CA GLY A 42 5988 8170 5772 600 343 -309 C ATOM 251 C GLY A 42 -27.568 -10.433 -52.329 1.00 58.49 C ANISOU 251 C GLY A 42 6814 8843 6568 678 359 -307 C ATOM 252 O GLY A 42 -27.019 -10.182 -51.252 1.00 63.35 O ANISOU 252 O GLY A 42 7510 9365 7194 639 371 -336 O ATOM 253 N ILE A 43 -28.299 -9.526 -52.983 1.00 65.48 N ANISOU 253 N ILE A 43 7673 9747 7460 796 354 -276 N ATOM 254 CA ILE A 43 -28.515 -8.202 -52.409 1.00 62.10 C ANISOU 254 CA ILE A 43 7324 9210 7061 892 371 -280 C ATOM 255 C ILE A 43 -29.366 -8.297 -51.149 1.00 67.56 C ANISOU 255 C ILE A 43 7997 9935 7739 917 423 -369 C ATOM 256 O ILE A 43 -29.184 -7.516 -50.208 1.00 73.57 O ANISOU 256 O ILE A 43 8859 10581 8512 944 445 -406 O ATOM 257 CB ILE A 43 -29.145 -7.263 -53.457 1.00 56.42 C ANISOU 257 CB ILE A 43 6589 8502 6347 1036 349 -216 C ATOM 258 CG1 ILE A 43 -28.203 -7.081 -54.649 1.00 62.15 C ANISOU 258 CG1 ILE A 43 7355 9186 7072 1001 310 -118 C ATOM 259 CG2 ILE A 43 -29.472 -5.907 -52.849 1.00 47.73 C ANISOU 259 CG2 ILE A 43 5588 7271 5276 1160 370 -228 C ATOM 260 CD1 ILE A 43 -26.890 -6.417 -54.298 1.00 65.59 C ANISOU 260 CD1 ILE A 43 7925 9448 7547 921 309 -86 C ATOM 261 N PHE A 44 -30.290 -9.257 -51.095 1.00 76.47 N ANISOU 261 N PHE A 44 9000 11220 8834 896 446 -408 N ATOM 262 CA PHE A 44 -31.129 -9.414 -49.911 1.00 77.97 C ANISOU 262 CA PHE A 44 9157 11467 8999 906 512 -486 C ATOM 263 C PHE A 44 -30.328 -9.953 -48.732 1.00 79.63 C ANISOU 263 C PHE A 44 9466 11602 9190 783 532 -523 C ATOM 264 O PHE A 44 -30.392 -9.409 -47.624 1.00 92.52 O ANISOU 264 O PHE A 44 11173 13175 10807 812 573 -575 O ATOM 265 CB PHE A 44 -32.310 -10.334 -50.226 1.00 86.03 C ANISOU 265 CB PHE A 44 10007 12688 9990 886 532 -510 C ATOM 266 CG PHE A 44 -33.020 -10.853 -49.006 1.00107.23 C ANISOU 266 CG PHE A 44 12652 15453 12639 835 612 -581 C ATOM 267 CD1 PHE A 44 -32.778 -12.136 -48.541 1.00111.50 C ANISOU 267 CD1 PHE A 44 13199 16018 13147 669 629 -596 C ATOM 268 CD2 PHE A 44 -33.929 -10.060 -48.326 1.00112.96 C ANISOU 268 CD2 PHE A 44 13339 16226 13356 962 675 -628 C ATOM 269 CE1 PHE A 44 -33.428 -12.618 -47.420 1.00110.26 C ANISOU 269 CE1 PHE A 44 13015 15933 12944 610 710 -647 C ATOM 270 CE2 PHE A 44 -34.583 -10.537 -47.204 1.00111.65 C ANISOU 270 CE2 PHE A 44 13129 16150 13142 911 763 -690 C ATOM 271 CZ PHE A 44 -34.332 -11.817 -46.752 1.00110.83 C ANISOU 271 CZ PHE A 44 13036 16072 13002 726 782 -694 C ATOM 272 N GLY A 45 -29.563 -11.024 -48.953 1.00 69.57 N ANISOU 272 N GLY A 45 8200 10329 7906 656 502 -500 N ATOM 273 CA GLY A 45 -28.888 -11.677 -47.842 1.00 62.74 C ANISOU 273 CA GLY A 45 7416 9411 7009 551 513 -527 C ATOM 274 C GLY A 45 -27.700 -10.889 -47.325 1.00 63.78 C ANISOU 274 C GLY A 45 7678 9397 7159 545 478 -521 C ATOM 275 O GLY A 45 -27.560 -10.676 -46.117 1.00 71.42 O ANISOU 275 O GLY A 45 8725 10317 8093 528 499 -569 O ATOM 276 N ASN A 46 -26.825 -10.447 -48.230 1.00 54.09 N ANISOU 276 N ASN A 46 6469 8106 5977 548 425 -465 N ATOM 277 CA ASN A 46 -25.602 -9.773 -47.812 1.00 52.20 C ANISOU 277 CA ASN A 46 6334 7741 5758 507 385 -456 C ATOM 278 C ASN A 46 -25.861 -8.383 -47.246 1.00 58.40 C ANISOU 278 C ASN A 46 7211 8422 6557 577 400 -493 C ATOM 279 O ASN A 46 -25.011 -7.860 -46.518 1.00 69.69 O ANISOU 279 O ASN A 46 8743 9750 7988 524 372 -517 O ATOM 280 CB ASN A 46 -24.623 -9.693 -48.983 1.00 59.61 C ANISOU 280 CB ASN A 46 7254 8658 6738 478 338 -379 C ATOM 281 CG ASN A 46 -24.098 -11.055 -49.394 1.00 75.54 C ANISOU 281 CG ASN A 46 9212 10753 8737 413 320 -357 C ATOM 282 OD1 ASN A 46 -23.729 -11.872 -48.550 1.00 75.80 O ANISOU 282 OD1 ASN A 46 9268 10792 8739 356 313 -385 O ATOM 283 ND2 ASN A 46 -24.073 -11.311 -50.696 1.00 88.63 N ANISOU 283 ND2 ASN A 46 10806 12465 10405 432 311 -307 N ATOM 284 N SER A 47 -27.005 -7.771 -47.560 1.00 54.73 N ANISOU 284 N SER A 47 6714 7980 6099 700 439 -503 N ATOM 285 CA SER A 47 -27.331 -6.487 -46.948 1.00 44.81 C ANISOU 285 CA SER A 47 5562 6612 4850 792 462 -551 C ATOM 286 C SER A 47 -27.761 -6.666 -45.499 1.00 63.73 C ANISOU 286 C SER A 47 8001 9031 7185 790 512 -648 C ATOM 287 O SER A 47 -27.441 -5.832 -44.644 1.00 68.26 O ANISOU 287 O SER A 47 8708 9484 7745 798 512 -706 O ATOM 288 CB SER A 47 -28.423 -5.779 -47.747 1.00 45.72 C ANISOU 288 CB SER A 47 5629 6753 4989 956 485 -528 C ATOM 289 OG SER A 47 -27.981 -5.476 -49.059 1.00 72.89 O ANISOU 289 OG SER A 47 9062 10162 8473 962 437 -432 O ATOM 290 N LEU A 48 -28.485 -7.748 -45.203 1.00 64.69 N ANISOU 290 N LEU A 48 8018 9303 7259 768 559 -667 N ATOM 291 CA LEU A 48 -28.885 -8.013 -43.826 1.00 58.95 C ANISOU 291 CA LEU A 48 7330 8613 6456 752 618 -746 C ATOM 292 C LEU A 48 -27.689 -8.371 -42.954 1.00 69.11 C ANISOU 292 C LEU A 48 8728 9829 7703 624 571 -759 C ATOM 293 O LEU A 48 -27.666 -8.026 -41.768 1.00 89.21 O ANISOU 293 O LEU A 48 11375 12336 10185 624 595 -831 O ATOM 294 CB LEU A 48 -29.929 -9.129 -43.792 1.00 45.88 C ANISOU 294 CB LEU A 48 5535 7138 4760 731 683 -749 C ATOM 295 CG LEU A 48 -31.262 -8.798 -44.466 1.00 56.82 C ANISOU 295 CG LEU A 48 6782 8638 6169 861 731 -752 C ATOM 296 CD1 LEU A 48 -32.115 -10.045 -44.607 1.00 65.69 C ANISOU 296 CD1 LEU A 48 7752 9945 7261 787 775 -744 C ATOM 297 CD2 LEU A 48 -32.005 -7.726 -43.684 1.00 58.88 C ANISOU 297 CD2 LEU A 48 7084 8883 6404 1009 801 -830 C ATOM 298 N VAL A 49 -26.690 -9.054 -43.519 1.00 62.97 N ANISOU 298 N VAL A 49 7930 9043 6955 527 502 -693 N ATOM 299 CA VAL A 49 -25.485 -9.376 -42.759 1.00 60.37 C ANISOU 299 CA VAL A 49 7685 8661 6590 422 442 -697 C ATOM 300 C VAL A 49 -24.761 -8.100 -42.347 1.00 70.19 C ANISOU 300 C VAL A 49 9051 9767 7850 419 396 -737 C ATOM 301 O VAL A 49 -24.259 -7.989 -41.221 1.00 81.71 O ANISOU 301 O VAL A 49 10608 11190 9246 367 371 -791 O ATOM 302 CB VAL A 49 -24.572 -10.310 -43.576 1.00 56.16 C ANISOU 302 CB VAL A 49 7088 8156 6092 348 381 -618 C ATOM 303 CG1 VAL A 49 -23.261 -10.556 -42.843 1.00 64.89 C ANISOU 303 CG1 VAL A 49 8263 9223 7169 261 307 -618 C ATOM 304 CG2 VAL A 49 -25.281 -11.626 -43.860 1.00 50.43 C ANISOU 304 CG2 VAL A 49 6277 7542 5341 333 423 -595 C ATOM 305 N VAL A 50 -24.704 -7.115 -43.245 1.00 62.36 N ANISOU 305 N VAL A 50 8066 8692 6935 467 383 -709 N ATOM 306 CA VAL A 50 -24.057 -5.848 -42.918 1.00 60.91 C ANISOU 306 CA VAL A 50 8016 8352 6774 448 342 -746 C ATOM 307 C VAL A 50 -24.879 -5.075 -41.894 1.00 64.89 C ANISOU 307 C VAL A 50 8632 8800 7223 537 398 -853 C ATOM 308 O VAL A 50 -24.328 -4.456 -40.976 1.00 72.64 O ANISOU 308 O VAL A 50 9749 9682 8168 487 364 -926 O ATOM 309 CB VAL A 50 -23.822 -5.025 -44.199 1.00 53.34 C ANISOU 309 CB VAL A 50 7054 7307 5908 473 321 -673 C ATOM 310 CG1 VAL A 50 -23.214 -3.671 -43.862 1.00 48.78 C ANISOU 310 CG1 VAL A 50 6636 6541 5356 436 284 -710 C ATOM 311 CG2 VAL A 50 -22.928 -5.788 -45.163 1.00 52.88 C ANISOU 311 CG2 VAL A 50 6888 7317 5887 384 275 -576 C ATOM 312 N ILE A 51 -26.207 -5.102 -42.029 1.00 67.12 N ANISOU 312 N ILE A 51 8852 9155 7493 672 483 -870 N ATOM 313 CA ILE A 51 -27.065 -4.372 -41.101 1.00 74.67 C ANISOU 313 CA ILE A 51 9899 10078 8394 786 553 -976 C ATOM 314 C ILE A 51 -26.960 -4.955 -39.696 1.00 80.24 C ANISOU 314 C ILE A 51 10658 10845 8985 718 574 -1051 C ATOM 315 O ILE A 51 -26.911 -4.216 -38.705 1.00100.16 O ANISOU 315 O ILE A 51 13328 13282 11446 740 584 -1151 O ATOM 316 CB ILE A 51 -28.519 -4.370 -41.610 1.00 63.29 C ANISOU 316 CB ILE A 51 8337 8745 6965 951 641 -970 C ATOM 317 CG1 ILE A 51 -28.645 -3.502 -42.864 1.00 66.30 C ANISOU 317 CG1 ILE A 51 8713 9036 7442 1051 614 -905 C ATOM 318 CG2 ILE A 51 -29.472 -3.886 -40.527 1.00 67.70 C ANISOU 318 CG2 ILE A 51 8952 9324 7446 1075 735 -1085 C ATOM 319 CD1 ILE A 51 -30.028 -3.508 -43.477 1.00 59.78 C ANISOU 319 CD1 ILE A 51 7747 8339 6629 1222 678 -889 C ATOM 320 N VAL A 52 -26.911 -6.283 -39.586 1.00 65.97 N ANISOU 320 N VAL A 52 8751 9177 7137 634 578 -1004 N ATOM 321 CA VAL A 52 -26.877 -6.914 -38.270 1.00 64.43 C ANISOU 321 CA VAL A 52 8613 9049 6819 574 602 -1056 C ATOM 322 C VAL A 52 -25.508 -6.742 -37.621 1.00 71.12 C ANISOU 322 C VAL A 52 9585 9804 7632 458 495 -1076 C ATOM 323 O VAL A 52 -25.406 -6.472 -36.419 1.00 79.66 O ANISOU 323 O VAL A 52 10791 10867 8608 445 498 -1162 O ATOM 324 CB VAL A 52 -27.271 -8.398 -38.383 1.00 59.08 C ANISOU 324 CB VAL A 52 7810 8527 6110 517 640 -988 C ATOM 325 CG1 VAL A 52 -27.064 -9.105 -37.055 1.00 61.27 C ANISOU 325 CG1 VAL A 52 8169 8857 6253 441 652 -1016 C ATOM 326 CG2 VAL A 52 -28.717 -8.530 -38.833 1.00 47.71 C ANISOU 326 CG2 VAL A 52 6238 7203 4686 615 748 -988 C ATOM 327 N ILE A 53 -24.437 -6.886 -38.400 1.00 72.99 N ANISOU 327 N ILE A 53 9784 9998 7949 374 398 -1001 N ATOM 328 CA ILE A 53 -23.094 -6.870 -37.826 1.00 67.37 C ANISOU 328 CA ILE A 53 9148 9242 7208 254 287 -1011 C ATOM 329 C ILE A 53 -22.640 -5.445 -37.535 1.00 70.95 C ANISOU 329 C ILE A 53 9742 9539 7679 238 241 -1092 C ATOM 330 O ILE A 53 -22.198 -5.136 -36.423 1.00 84.59 O ANISOU 330 O ILE A 53 11592 11234 9315 184 196 -1177 O ATOM 331 CB ILE A 53 -22.107 -7.596 -38.758 1.00 69.60 C ANISOU 331 CB ILE A 53 9317 9561 7566 176 210 -904 C ATOM 332 CG1 ILE A 53 -22.345 -9.105 -38.714 1.00 72.58 C ANISOU 332 CG1 ILE A 53 9611 10068 7898 171 235 -843 C ATOM 333 CG2 ILE A 53 -20.673 -7.267 -38.380 1.00 72.61 C ANISOU 333 CG2 ILE A 53 9748 9895 7944 60 88 -914 C ATOM 334 CD1 ILE A 53 -21.371 -9.891 -39.553 1.00 84.74 C ANISOU 334 CD1 ILE A 53 11053 11644 9499 118 164 -751 C ATOM 335 N TYR A 54 -22.737 -4.557 -38.525 1.00 64.91 N ANISOU 335 N TYR A 54 8974 8668 7022 278 248 -1068 N ATOM 336 CA TYR A 54 -22.170 -3.222 -38.378 1.00 73.01 C ANISOU 336 CA TYR A 54 10147 9514 8079 234 195 -1129 C ATOM 337 C TYR A 54 -23.016 -2.320 -37.487 1.00 92.24 C ANISOU 337 C TYR A 54 12745 11857 10446 340 259 -1261 C ATOM 338 O TYR A 54 -22.471 -1.429 -36.826 1.00103.55 O ANISOU 338 O TYR A 54 14342 13154 11849 277 205 -1353 O ATOM 339 CB TYR A 54 -21.988 -2.575 -39.753 1.00 61.49 C ANISOU 339 CB TYR A 54 8654 7958 6752 241 186 -1043 C ATOM 340 CG TYR A 54 -21.259 -1.251 -39.720 1.00 59.11 C ANISOU 340 CG TYR A 54 8510 7455 6495 156 126 -1085 C ATOM 341 CD1 TYR A 54 -19.871 -1.203 -39.684 1.00 65.17 C ANISOU 341 CD1 TYR A 54 9272 8206 7285 -34 20 -1064 C ATOM 342 CD2 TYR A 54 -21.956 -0.049 -39.729 1.00 58.71 C ANISOU 342 CD2 TYR A 54 8614 7229 6465 265 174 -1145 C ATOM 343 CE1 TYR A 54 -19.198 0.004 -39.655 1.00 72.89 C ANISOU 343 CE1 TYR A 54 10394 8996 8305 -144 -36 -1102 C ATOM 344 CE2 TYR A 54 -21.291 1.163 -39.700 1.00 72.59 C ANISOU 344 CE2 TYR A 54 10543 8773 8265 173 119 -1184 C ATOM 345 CZ TYR A 54 -19.913 1.183 -39.664 1.00 79.45 C ANISOU 345 CZ TYR A 54 11403 9627 9156 -47 14 -1162 C ATOM 346 OH TYR A 54 -19.247 2.387 -39.635 1.00 87.90 O ANISOU 346 OH TYR A 54 12645 10484 10270 -171 -41 -1201 O ATOM 347 N PHE A 55 -24.332 -2.527 -37.450 1.00 92.85 N ANISOU 347 N PHE A 55 12776 12010 10492 499 374 -1278 N ATOM 348 CA PHE A 55 -25.230 -1.628 -36.736 1.00 80.66 C ANISOU 348 CA PHE A 55 11368 10388 8890 638 454 -1402 C ATOM 349 C PHE A 55 -25.812 -2.213 -35.459 1.00 63.32 C ANISOU 349 C PHE A 55 9192 8325 6542 670 525 -1487 C ATOM 350 O PHE A 55 -26.072 -1.460 -34.519 1.00 64.59 O ANISOU 350 O PHE A 55 9515 8410 6616 729 558 -1618 O ATOM 351 CB PHE A 55 -26.379 -1.190 -37.653 1.00 71.74 C ANISOU 351 CB PHE A 55 10171 9248 7838 827 542 -1368 C ATOM 352 CG PHE A 55 -25.924 -0.460 -38.885 1.00 72.85 C ANISOU 352 CG PHE A 55 10328 9242 8111 819 485 -1283 C ATOM 353 CD1 PHE A 55 -25.788 0.918 -38.879 1.00 70.56 C ANISOU 353 CD1 PHE A 55 10234 8719 7858 865 468 -1342 C ATOM 354 CD2 PHE A 55 -25.627 -1.153 -40.047 1.00 64.07 C ANISOU 354 CD2 PHE A 55 9051 8215 7078 762 452 -1145 C ATOM 355 CE1 PHE A 55 -25.366 1.593 -40.010 1.00 70.33 C ANISOU 355 CE1 PHE A 55 10235 8546 7942 845 421 -1249 C ATOM 356 CE2 PHE A 55 -25.204 -0.485 -41.181 1.00 58.73 C ANISOU 356 CE2 PHE A 55 8394 7413 6505 751 408 -1059 C ATOM 357 CZ PHE A 55 -25.074 0.890 -41.163 1.00 65.06 C ANISOU 357 CZ PHE A 55 9391 7985 7343 788 394 -1104 C ATOM 358 N TYR A 56 -26.024 -3.527 -35.395 1.00 58.58 N ANISOU 358 N TYR A 56 8446 7913 5898 631 553 -1416 N ATOM 359 CA TYR A 56 -26.568 -4.157 -34.200 1.00 70.55 C ANISOU 359 CA TYR A 56 9984 9562 7261 643 628 -1476 C ATOM 360 C TYR A 56 -25.514 -4.860 -33.354 1.00 73.31 C ANISOU 360 C TYR A 56 10392 9952 7511 486 534 -1468 C ATOM 361 O TYR A 56 -25.805 -5.220 -32.209 1.00 95.06 O ANISOU 361 O TYR A 56 13215 12790 10112 485 582 -1526 O ATOM 362 CB TYR A 56 -27.668 -5.159 -34.577 1.00 79.06 C ANISOU 362 CB TYR A 56 10878 10823 8339 702 739 -1404 C ATOM 363 CG TYR A 56 -28.974 -4.516 -34.991 1.00 91.25 C ANISOU 363 CG TYR A 56 12359 12389 9924 887 855 -1442 C ATOM 364 CD1 TYR A 56 -29.254 -3.194 -34.669 1.00 98.80 C ANISOU 364 CD1 TYR A 56 13455 13211 10872 1018 884 -1555 C ATOM 365 CD2 TYR A 56 -29.930 -5.235 -35.697 1.00 88.54 C ANISOU 365 CD2 TYR A 56 11817 12201 9625 935 931 -1368 C ATOM 366 CE1 TYR A 56 -30.448 -2.605 -35.043 1.00 94.79 C ANISOU 366 CE1 TYR A 56 12884 12730 10401 1217 987 -1587 C ATOM 367 CE2 TYR A 56 -31.126 -4.654 -36.075 1.00 90.82 C ANISOU 367 CE2 TYR A 56 12023 12537 9948 1115 1027 -1401 C ATOM 368 CZ TYR A 56 -31.380 -3.340 -35.746 1.00 93.32 C ANISOU 368 CZ TYR A 56 12475 12725 10257 1268 1056 -1506 C ATOM 369 OH TYR A 56 -32.570 -2.759 -36.121 1.00 91.17 O ANISOU 369 OH TYR A 56 12116 12507 10019 1477 1148 -1536 O ATOM 370 N MET A 57 -24.304 -5.062 -33.882 1.00 74.27 N ANISOU 370 N MET A 57 10484 10027 7706 363 403 -1396 N ATOM 371 CA MET A 57 -23.234 -5.712 -33.138 1.00 85.00 C ANISOU 371 CA MET A 57 11882 11436 8978 232 296 -1382 C ATOM 372 C MET A 57 -21.973 -4.874 -32.995 1.00 97.56 C ANISOU 372 C MET A 57 13570 12906 10593 122 155 -1430 C ATOM 373 O MET A 57 -21.141 -5.195 -32.140 1.00112.46 O ANISOU 373 O MET A 57 15513 14838 12379 26 58 -1452 O ATOM 374 CB MET A 57 -22.861 -7.052 -33.791 1.00 84.82 C ANISOU 374 CB MET A 57 11703 11522 9003 178 264 -1240 C ATOM 375 CG MET A 57 -23.924 -8.116 -33.630 1.00 74.44 C ANISOU 375 CG MET A 57 10316 10340 7626 230 382 -1195 C ATOM 376 SD MET A 57 -23.305 -9.772 -33.957 1.00 80.82 S ANISOU 376 SD MET A 57 11023 11247 8440 150 325 -1055 S ATOM 377 CE MET A 57 -24.671 -10.741 -33.338 1.00 77.99 C ANISOU 377 CE MET A 57 10653 11014 7967 183 479 -1040 C ATOM 378 N LYS A 58 -21.799 -3.833 -33.810 1.00 87.58 N ANISOU 378 N LYS A 58 12326 11495 9456 124 136 -1440 N ATOM 379 CA LYS A 58 -20.725 -2.851 -33.665 1.00 84.07 C ANISOU 379 CA LYS A 58 11993 10912 9038 3 17 -1500 C ATOM 380 C LYS A 58 -19.333 -3.452 -33.853 1.00 85.63 C ANISOU 380 C LYS A 58 12090 11183 9264 -155 -123 -1421 C ATOM 381 O LYS A 58 -18.340 -2.832 -33.458 1.00102.09 O ANISOU 381 O LYS A 58 14250 13204 11336 -288 -238 -1479 O ATOM 382 CB LYS A 58 -20.805 -2.141 -32.307 1.00 87.44 C ANISOU 382 CB LYS A 58 12629 11275 9321 -3 5 -1665 C ATOM 383 CG LYS A 58 -22.168 -1.550 -31.981 1.00 93.79 C ANISOU 383 CG LYS A 58 13535 12024 10077 175 151 -1761 C ATOM 384 CD LYS A 58 -22.510 -0.390 -32.899 1.00106.50 C ANISOU 384 CD LYS A 58 15198 13442 11826 250 186 -1771 C ATOM 385 CE LYS A 58 -23.820 0.264 -32.489 1.00112.43 C ANISOU 385 CE LYS A 58 16057 14140 12521 453 325 -1881 C ATOM 386 NZ LYS A 58 -24.149 1.440 -33.341 1.00113.11 N ANISOU 386 NZ LYS A 58 16222 14020 12736 550 351 -1889 N ATOM 387 N LEU A 59 -19.240 -4.645 -34.448 1.00 81.43 N ANISOU 387 N LEU A 59 11386 10786 8767 -142 -115 -1295 N ATOM 388 CA LEU A 59 -17.959 -5.296 -34.716 1.00 79.76 C ANISOU 388 CA LEU A 59 11057 10660 8587 -255 -235 -1213 C ATOM 389 C LEU A 59 -17.126 -5.465 -33.451 1.00 81.57 C ANISOU 389 C LEU A 59 11359 10952 8682 -346 -354 -1276 C ATOM 390 O LEU A 59 -16.237 -4.652 -33.177 1.00 88.67 O ANISOU 390 O LEU A 59 12314 11792 9587 -469 -461 -1339 O ATOM 391 CB LEU A 59 -17.159 -4.506 -35.757 1.00 79.02 C ANISOU 391 CB LEU A 59 10910 10475 8639 -348 -289 -1173 C ATOM 392 CG LEU A 59 -17.626 -4.525 -37.211 1.00 69.25 C ANISOU 392 CG LEU A 59 9565 9210 7535 -279 -205 -1072 C ATOM 393 CD1 LEU A 59 -16.920 -3.433 -37.995 1.00 60.72 C ANISOU 393 CD1 LEU A 59 8498 8004 6569 -382 -248 -1055 C ATOM 394 CD2 LEU A 59 -17.358 -5.883 -37.833 1.00 61.78 C ANISOU 394 CD2 LEU A 59 8443 8418 6613 -256 -207 -956 C ATOM 395 N LYS A 60 -17.391 -6.519 -32.679 1.00 79.38 N ANISOU 395 N LYS A 60 11086 10798 8278 -296 -342 -1256 N ATOM 396 CA LYS A 60 -16.685 -6.750 -31.427 1.00 71.67 C ANISOU 396 CA LYS A 60 10188 9896 7148 -361 -457 -1307 C ATOM 397 C LYS A 60 -15.698 -7.907 -31.481 1.00 68.18 C ANISOU 397 C LYS A 60 9616 9594 6694 -388 -563 -1197 C ATOM 398 O LYS A 60 -14.887 -8.046 -30.559 1.00 77.38 O ANISOU 398 O LYS A 60 10822 10835 7746 -448 -692 -1227 O ATOM 399 CB LYS A 60 -17.687 -6.996 -30.290 1.00 63.32 C ANISOU 399 CB LYS A 60 9271 8871 5915 -281 -368 -1373 C ATOM 400 CG LYS A 60 -18.552 -5.793 -29.955 1.00 55.92 C ANISOU 400 CG LYS A 60 8486 7810 4953 -238 -277 -1511 C ATOM 401 CD LYS A 60 -19.531 -6.109 -28.838 1.00 69.95 C ANISOU 401 CD LYS A 60 10382 9651 6545 -154 -174 -1572 C ATOM 402 CE LYS A 60 -20.323 -4.875 -28.439 1.00 90.02 C ANISOU 402 CE LYS A 60 13080 12074 9050 -91 -86 -1726 C ATOM 403 NZ LYS A 60 -19.439 -3.795 -27.921 1.00102.71 N ANISOU 403 NZ LYS A 60 14830 13571 10623 -198 -218 -1854 N ATOM 404 N THR A 61 -15.736 -8.733 -32.521 1.00 68.71 N ANISOU 404 N THR A 61 9537 9701 6870 -336 -518 -1076 N ATOM 405 CA THR A 61 -14.859 -9.888 -32.641 1.00 63.07 C ANISOU 405 CA THR A 61 8707 9108 6150 -328 -606 -971 C ATOM 406 C THR A 61 -14.089 -9.827 -33.954 1.00 75.86 C ANISOU 406 C THR A 61 10152 10734 7938 -360 -636 -899 C ATOM 407 O THR A 61 -14.394 -9.034 -34.848 1.00 97.29 O ANISOU 407 O THR A 61 12839 13357 10771 -380 -571 -910 O ATOM 408 CB THR A 61 -15.653 -11.198 -32.557 1.00 62.08 C ANISOU 408 CB THR A 61 8591 9031 5965 -223 -515 -890 C ATOM 409 OG1 THR A 61 -16.671 -11.209 -33.566 1.00 55.25 O ANISOU 409 OG1 THR A 61 7678 8106 5207 -169 -372 -863 O ATOM 410 CG2 THR A 61 -16.299 -11.347 -31.187 1.00 66.87 C ANISOU 410 CG2 THR A 61 9366 9659 6384 -204 -485 -945 C ATOM 411 N VAL A 62 -13.072 -10.685 -34.056 1.00 67.21 N ANISOU 411 N VAL A 62 8939 9753 6843 -353 -734 -821 N ATOM 412 CA VAL A 62 -12.303 -10.786 -35.292 1.00 64.66 C ANISOU 412 CA VAL A 62 8436 9468 6665 -367 -751 -747 C ATOM 413 C VAL A 62 -13.150 -11.399 -36.399 1.00 73.09 C ANISOU 413 C VAL A 62 9457 10497 7816 -271 -615 -676 C ATOM 414 O VAL A 62 -13.127 -10.937 -37.546 1.00 80.22 O ANISOU 414 O VAL A 62 10275 11363 8842 -290 -565 -651 O ATOM 415 CB VAL A 62 -11.013 -11.593 -35.052 1.00 51.05 C ANISOU 415 CB VAL A 62 6592 7895 4910 -356 -889 -689 C ATOM 416 CG1 VAL A 62 -10.311 -11.888 -36.370 1.00 56.66 C ANISOU 416 CG1 VAL A 62 7107 8663 5757 -339 -879 -607 C ATOM 417 CG2 VAL A 62 -10.088 -10.844 -34.108 1.00 60.83 C ANISOU 417 CG2 VAL A 62 7843 9189 6079 -477 -1041 -765 C ATOM 418 N ALA A 63 -13.919 -12.442 -36.072 1.00 63.98 N ANISOU 418 N ALA A 63 8367 9353 6589 -177 -554 -643 N ATOM 419 CA ALA A 63 -14.749 -13.096 -37.077 1.00 62.10 C ANISOU 419 CA ALA A 63 8089 9087 6421 -102 -435 -585 C ATOM 420 C ALA A 63 -15.840 -12.171 -37.597 1.00 67.19 C ANISOU 420 C ALA A 63 8767 9638 7124 -110 -323 -632 C ATOM 421 O ALA A 63 -16.323 -12.352 -38.721 1.00 69.56 O ANISOU 421 O ALA A 63 8996 9921 7512 -71 -246 -590 O ATOM 422 CB ALA A 63 -15.362 -14.372 -36.500 1.00 55.24 C ANISOU 422 CB ALA A 63 7299 8236 5452 -29 -395 -543 C ATOM 423 N SER A 64 -16.246 -11.180 -36.799 1.00 61.60 N ANISOU 423 N SER A 64 8171 8871 6363 -149 -316 -722 N ATOM 424 CA SER A 64 -17.231 -10.215 -37.273 1.00 60.63 C ANISOU 424 CA SER A 64 8085 8654 6299 -132 -217 -768 C ATOM 425 C SER A 64 -16.646 -9.299 -38.340 1.00 62.13 C ANISOU 425 C SER A 64 8201 8788 6618 -183 -240 -751 C ATOM 426 O SER A 64 -17.361 -8.886 -39.261 1.00 62.61 O ANISOU 426 O SER A 64 8239 8792 6756 -140 -157 -734 O ATOM 427 CB SER A 64 -17.771 -9.392 -36.103 1.00 62.44 C ANISOU 427 CB SER A 64 8468 8827 6429 -143 -201 -878 C ATOM 428 OG SER A 64 -16.749 -8.606 -35.516 1.00 76.76 O ANISOU 428 OG SER A 64 10332 10615 8219 -240 -318 -938 O ATOM 429 N VAL A 65 -15.356 -8.971 -38.235 1.00 62.01 N ANISOU 429 N VAL A 65 8143 8796 6621 -280 -352 -750 N ATOM 430 CA VAL A 65 -14.714 -8.147 -39.254 1.00 61.11 C ANISOU 430 CA VAL A 65 7954 8640 6626 -353 -368 -719 C ATOM 431 C VAL A 65 -14.610 -8.912 -40.567 1.00 67.31 C ANISOU 431 C VAL A 65 8593 9491 7491 -298 -322 -615 C ATOM 432 O VAL A 65 -14.863 -8.360 -41.645 1.00 72.03 O ANISOU 432 O VAL A 65 9159 10035 8174 -295 -263 -579 O ATOM 433 CB VAL A 65 -13.334 -7.672 -38.765 1.00 57.55 C ANISOU 433 CB VAL A 65 7471 8225 6169 -492 -501 -745 C ATOM 434 CG1 VAL A 65 -12.714 -6.713 -39.769 1.00 54.28 C ANISOU 434 CG1 VAL A 65 6994 7757 5874 -598 -504 -713 C ATOM 435 CG2 VAL A 65 -13.455 -7.020 -37.402 1.00 64.98 C ANISOU 435 CG2 VAL A 65 8575 9109 7008 -546 -556 -862 C ATOM 436 N PHE A 66 -14.233 -10.191 -40.499 1.00 69.49 N ANISOU 436 N PHE A 66 8791 9880 7731 -245 -349 -566 N ATOM 437 CA PHE A 66 -14.182 -11.011 -41.705 1.00 64.06 C ANISOU 437 CA PHE A 66 7986 9250 7104 -178 -301 -483 C ATOM 438 C PHE A 66 -15.567 -11.182 -42.312 1.00 62.33 C ANISOU 438 C PHE A 66 7806 8977 6900 -98 -187 -477 C ATOM 439 O PHE A 66 -15.738 -11.062 -43.531 1.00 78.43 O ANISOU 439 O PHE A 66 9777 11013 9009 -76 -135 -431 O ATOM 440 CB PHE A 66 -13.568 -12.375 -41.389 1.00 60.03 C ANISOU 440 CB PHE A 66 7420 8845 6543 -119 -354 -443 C ATOM 441 CG PHE A 66 -12.118 -12.316 -41.003 1.00 66.07 C ANISOU 441 CG PHE A 66 8097 9705 7304 -176 -474 -435 C ATOM 442 CD1 PHE A 66 -11.306 -11.291 -41.461 1.00 69.81 C ANISOU 442 CD1 PHE A 66 8487 10190 7849 -287 -508 -436 C ATOM 443 CD2 PHE A 66 -11.566 -13.286 -40.183 1.00 71.65 C ANISOU 443 CD2 PHE A 66 8801 10494 7930 -123 -555 -421 C ATOM 444 CE1 PHE A 66 -9.970 -11.235 -41.108 1.00 75.82 C ANISOU 444 CE1 PHE A 66 9138 11064 8607 -354 -622 -431 C ATOM 445 CE2 PHE A 66 -10.232 -13.236 -39.826 1.00 84.77 C ANISOU 445 CE2 PHE A 66 10357 12268 9584 -164 -677 -413 C ATOM 446 CZ PHE A 66 -9.433 -12.209 -40.289 1.00 86.61 C ANISOU 446 CZ PHE A 66 10482 12533 9894 -286 -710 -423 C ATOM 447 N LEU A 67 -16.572 -11.455 -41.476 1.00 49.59 N ANISOU 447 N LEU A 67 6293 7337 5211 -57 -146 -522 N ATOM 448 CA LEU A 67 -17.921 -11.668 -41.988 1.00 59.89 C ANISOU 448 CA LEU A 67 7610 8620 6526 12 -41 -520 C ATOM 449 C LEU A 67 -18.510 -10.391 -42.575 1.00 64.04 C ANISOU 449 C LEU A 67 8154 9065 7113 18 7 -541 C ATOM 450 O LEU A 67 -19.307 -10.457 -43.518 1.00 73.22 O ANISOU 450 O LEU A 67 9271 10232 8316 75 73 -512 O ATOM 451 CB LEU A 67 -18.825 -12.214 -40.883 1.00 59.44 C ANISOU 451 CB LEU A 67 7644 8572 6369 39 -1 -561 C ATOM 452 CG LEU A 67 -20.111 -12.889 -41.360 1.00 62.79 C ANISOU 452 CG LEU A 67 8046 9019 6792 94 99 -546 C ATOM 453 CD1 LEU A 67 -19.779 -14.026 -42.311 1.00 63.13 C ANISOU 453 CD1 LEU A 67 8008 9108 6872 111 92 -477 C ATOM 454 CD2 LEU A 67 -20.933 -13.398 -40.187 1.00 63.11 C ANISOU 454 CD2 LEU A 67 8173 9080 6726 97 148 -581 C ATOM 455 N LEU A 68 -18.137 -9.227 -42.037 1.00 51.99 N ANISOU 455 N LEU A 68 6703 7461 5590 -39 -32 -592 N ATOM 456 CA LEU A 68 -18.607 -7.969 -42.610 1.00 52.50 C ANISOU 456 CA LEU A 68 6811 7419 5716 -25 8 -604 C ATOM 457 C LEU A 68 -18.005 -7.741 -43.990 1.00 61.43 C ANISOU 457 C LEU A 68 7850 8553 6938 -52 3 -518 C ATOM 458 O LEU A 68 -18.725 -7.455 -44.953 1.00 67.98 O ANISOU 458 O LEU A 68 8661 9358 7809 14 62 -480 O ATOM 459 CB LEU A 68 -18.273 -6.803 -41.679 1.00 45.70 C ANISOU 459 CB LEU A 68 6081 6450 4834 -92 -37 -686 C ATOM 460 CG LEU A 68 -18.608 -5.419 -42.241 1.00 64.49 C ANISOU 460 CG LEU A 68 8539 8683 7281 -83 -6 -695 C ATOM 461 CD1 LEU A 68 -20.104 -5.283 -42.482 1.00 65.42 C ANISOU 461 CD1 LEU A 68 8683 8778 7394 67 93 -711 C ATOM 462 CD2 LEU A 68 -18.106 -4.313 -41.326 1.00 58.94 C ANISOU 462 CD2 LEU A 68 7982 7854 6557 -174 -63 -785 C ATOM 463 N ASN A 69 -16.681 -7.865 -44.105 1.00 71.10 N ANISOU 463 N ASN A 69 9007 9822 8184 -146 -68 -484 N ATOM 464 CA ASN A 69 -16.024 -7.688 -45.393 1.00 74.58 C ANISOU 464 CA ASN A 69 9351 10288 8698 -181 -61 -399 C ATOM 465 C ASN A 69 -16.351 -8.810 -46.370 1.00 83.21 C ANISOU 465 C ASN A 69 10341 11482 9793 -92 -13 -339 C ATOM 466 O ASN A 69 -16.254 -8.605 -47.585 1.00 89.10 O ANISOU 466 O ASN A 69 11028 12241 10584 -84 21 -272 O ATOM 467 CB ASN A 69 -14.512 -7.582 -45.197 1.00 69.39 C ANISOU 467 CB ASN A 69 8622 9684 8058 -307 -144 -383 C ATOM 468 CG ASN A 69 -14.105 -6.302 -44.494 1.00 83.10 C ANISOU 468 CG ASN A 69 10462 11307 9806 -430 -196 -440 C ATOM 469 OD1 ASN A 69 -13.259 -6.311 -43.602 1.00 92.36 O ANISOU 469 OD1 ASN A 69 11625 12519 10947 -521 -283 -483 O ATOM 470 ND2 ASN A 69 -14.713 -5.190 -44.892 1.00 87.36 N ANISOU 470 ND2 ASN A 69 11109 11700 10386 -432 -149 -441 N ATOM 471 N LEU A 70 -16.731 -9.989 -45.870 1.00 80.69 N ANISOU 471 N LEU A 70 10011 11229 9419 -31 -10 -361 N ATOM 472 CA LEU A 70 -17.173 -11.055 -46.762 1.00 64.59 C ANISOU 472 CA LEU A 70 7902 9262 7376 46 37 -321 C ATOM 473 C LEU A 70 -18.495 -10.704 -47.428 1.00 58.85 C ANISOU 473 C LEU A 70 7197 8501 6661 111 107 -320 C ATOM 474 O LEU A 70 -18.741 -11.110 -48.569 1.00 79.15 O ANISOU 474 O LEU A 70 9705 11122 9247 153 140 -276 O ATOM 475 CB LEU A 70 -17.296 -12.369 -45.991 1.00 64.05 C ANISOU 475 CB LEU A 70 7847 9244 7245 80 23 -343 C ATOM 476 CG LEU A 70 -17.448 -13.656 -46.804 1.00 66.37 C ANISOU 476 CG LEU A 70 8084 9601 7532 140 52 -309 C ATOM 477 CD1 LEU A 70 -16.219 -13.892 -47.667 1.00 60.45 C ANISOU 477 CD1 LEU A 70 7234 8917 6817 141 25 -259 C ATOM 478 CD2 LEU A 70 -17.695 -14.842 -45.884 1.00 82.18 C ANISOU 478 CD2 LEU A 70 10144 11613 9468 162 42 -330 C ATOM 479 N ALA A 71 -19.353 -9.952 -46.736 1.00 68.93 N ANISOU 479 N ALA A 71 8561 9706 7925 130 129 -372 N ATOM 480 CA ALA A 71 -20.611 -9.514 -47.327 1.00 73.73 C ANISOU 480 CA ALA A 71 9175 10295 8545 210 189 -372 C ATOM 481 C ALA A 71 -20.437 -8.258 -48.170 1.00 73.03 C ANISOU 481 C ALA A 71 9109 10126 8513 213 191 -326 C ATOM 482 O ALA A 71 -21.170 -8.068 -49.147 1.00 76.73 O ANISOU 482 O ALA A 71 9548 10610 8995 286 226 -287 O ATOM 483 CB ALA A 71 -21.651 -9.275 -46.231 1.00 41.81 C ANISOU 483 CB ALA A 71 5206 6223 4459 253 224 -449 C ATOM 484 N LEU A 72 -19.483 -7.395 -47.811 1.00 70.19 N ANISOU 484 N LEU A 72 8808 9682 8180 127 150 -327 N ATOM 485 CA LEU A 72 -19.227 -6.203 -48.614 1.00 64.60 C ANISOU 485 CA LEU A 72 8141 8877 7525 105 154 -270 C ATOM 486 C LEU A 72 -18.640 -6.568 -49.971 1.00 74.10 C ANISOU 486 C LEU A 72 9241 10162 8749 87 163 -173 C ATOM 487 O LEU A 72 -19.051 -6.017 -50.999 1.00 67.86 O ANISOU 487 O LEU A 72 8462 9344 7976 136 194 -108 O ATOM 488 CB LEU A 72 -18.292 -5.252 -47.867 1.00 56.42 C ANISOU 488 CB LEU A 72 7195 7730 6512 -17 104 -300 C ATOM 489 CG LEU A 72 -18.855 -4.553 -46.630 1.00 50.59 C ANISOU 489 CG LEU A 72 6599 6876 5748 3 99 -403 C ATOM 490 CD1 LEU A 72 -17.842 -3.566 -46.071 1.00 46.96 C ANISOU 490 CD1 LEU A 72 6235 6298 5311 -142 39 -433 C ATOM 491 CD2 LEU A 72 -20.164 -3.854 -46.960 1.00 49.59 C ANISOU 491 CD2 LEU A 72 6548 6665 5629 145 159 -409 C ATOM 492 N ALA A 73 -17.678 -7.494 -49.995 1.00 76.19 N ANISOU 492 N ALA A 73 9409 10534 9005 30 138 -160 N ATOM 493 CA ALA A 73 -17.082 -7.907 -51.261 1.00 74.63 C ANISOU 493 CA ALA A 73 9110 10430 8815 23 157 -79 C ATOM 494 C ALA A 73 -18.098 -8.599 -52.159 1.00 73.32 C ANISOU 494 C ALA A 73 8908 10334 8617 137 200 -62 C ATOM 495 O ALA A 73 -17.991 -8.524 -53.389 1.00 81.66 O ANISOU 495 O ALA A 73 9923 11435 9670 155 227 8 O ATOM 496 CB ALA A 73 -15.886 -8.825 -51.006 1.00 81.13 C ANISOU 496 CB ALA A 73 9834 11362 9630 -30 123 -82 C ATOM 497 N ASP A 74 -19.087 -9.273 -51.569 1.00 60.99 N ANISOU 497 N ASP A 74 7360 8790 7025 203 205 -127 N ATOM 498 CA ASP A 74 -20.118 -9.916 -52.376 1.00 64.45 C ANISOU 498 CA ASP A 74 7756 9301 7432 289 237 -122 C ATOM 499 C ASP A 74 -21.062 -8.887 -52.987 1.00 65.25 C ANISOU 499 C ASP A 74 7894 9355 7542 360 258 -90 C ATOM 500 O ASP A 74 -21.502 -9.045 -54.132 1.00 73.30 O ANISOU 500 O ASP A 74 8870 10440 8539 414 271 -46 O ATOM 501 CB ASP A 74 -20.893 -10.928 -51.533 1.00 59.11 C ANISOU 501 CB ASP A 74 7077 8661 6720 313 241 -196 C ATOM 502 CG ASP A 74 -20.062 -12.145 -51.172 1.00 60.82 C ANISOU 502 CG ASP A 74 7265 8927 6916 274 220 -212 C ATOM 503 OD1 ASP A 74 -18.854 -12.160 -51.490 1.00 66.60 O ANISOU 503 OD1 ASP A 74 7963 9679 7665 238 199 -174 O ATOM 504 OD2 ASP A 74 -20.618 -13.090 -50.572 1.00 69.56 O ANISOU 504 OD2 ASP A 74 8385 10056 7989 282 226 -257 O ATOM 505 N LEU A 75 -21.382 -7.825 -52.243 1.00 56.12 N ANISOU 505 N LEU A 75 6828 8084 6411 370 256 -114 N ATOM 506 CA LEU A 75 -22.241 -6.776 -52.785 1.00 66.36 C ANISOU 506 CA LEU A 75 8175 9318 7719 463 273 -79 C ATOM 507 C LEU A 75 -21.579 -6.060 -53.955 1.00 78.02 C ANISOU 507 C LEU A 75 9674 10759 9213 438 272 28 C ATOM 508 O LEU A 75 -22.267 -5.641 -54.894 1.00 84.68 O ANISOU 508 O LEU A 75 10522 11612 10040 530 282 87 O ATOM 509 CB LEU A 75 -22.608 -5.774 -51.690 1.00 62.67 C ANISOU 509 CB LEU A 75 7823 8714 7274 487 275 -137 C ATOM 510 CG LEU A 75 -23.521 -6.277 -50.571 1.00 54.54 C ANISOU 510 CG LEU A 75 6784 7726 6214 537 295 -238 C ATOM 511 CD1 LEU A 75 -23.686 -5.211 -49.500 1.00 56.11 C ANISOU 511 CD1 LEU A 75 7114 7783 6424 558 301 -302 C ATOM 512 CD2 LEU A 75 -24.874 -6.691 -51.128 1.00 46.04 C ANISOU 512 CD2 LEU A 75 5619 6764 5112 656 323 -240 C ATOM 513 N CYS A 76 -20.253 -5.908 -53.918 1.00 76.52 N ANISOU 513 N CYS A 76 9488 10539 9046 313 261 61 N ATOM 514 CA CYS A 76 -19.552 -5.269 -55.027 1.00 84.10 C ANISOU 514 CA CYS A 76 10460 11479 10014 265 275 172 C ATOM 515 C CYS A 76 -19.577 -6.135 -56.280 1.00 73.69 C ANISOU 515 C CYS A 76 9040 10317 8643 308 295 224 C ATOM 516 O CYS A 76 -19.630 -5.606 -57.396 1.00 73.17 O ANISOU 516 O CYS A 76 8995 10252 8554 335 314 320 O ATOM 517 CB CYS A 76 -18.110 -4.955 -54.627 1.00 92.48 C ANISOU 517 CB CYS A 76 11523 12500 11114 103 261 186 C ATOM 518 SG CYS A 76 -17.951 -3.787 -53.256 1.00 92.40 S ANISOU 518 SG CYS A 76 11661 12291 11156 24 227 121 S ATOM 519 N PHE A 77 -19.538 -7.460 -56.119 1.00 69.65 N ANISOU 519 N PHE A 77 8432 9928 8103 316 290 163 N ATOM 520 CA PHE A 77 -19.644 -8.348 -57.272 1.00 65.76 C ANISOU 520 CA PHE A 77 7860 9574 7551 362 307 189 C ATOM 521 C PHE A 77 -21.041 -8.301 -57.877 1.00 66.28 C ANISOU 521 C PHE A 77 7933 9674 7576 478 303 191 C ATOM 522 O PHE A 77 -21.194 -8.316 -59.104 1.00 72.59 O ANISOU 522 O PHE A 77 8713 10548 8321 521 312 253 O ATOM 523 CB PHE A 77 -19.280 -9.777 -56.867 1.00 63.14 C ANISOU 523 CB PHE A 77 7454 9334 7202 346 301 114 C ATOM 524 CG PHE A 77 -19.779 -10.827 -57.822 1.00 60.86 C ANISOU 524 CG PHE A 77 7112 9164 6847 409 310 99 C ATOM 525 CD1 PHE A 77 -19.117 -11.071 -59.014 1.00 78.08 C ANISOU 525 CD1 PHE A 77 9252 11434 8981 411 337 153 C ATOM 526 CD2 PHE A 77 -20.906 -11.576 -57.522 1.00 65.97 C ANISOU 526 CD2 PHE A 77 7752 9841 7473 455 295 25 C ATOM 527 CE1 PHE A 77 -19.574 -12.037 -59.891 1.00 90.77 C ANISOU 527 CE1 PHE A 77 10828 13145 10517 466 341 124 C ATOM 528 CE2 PHE A 77 -21.367 -12.543 -58.395 1.00 76.56 C ANISOU 528 CE2 PHE A 77 9054 11284 8751 492 296 0 C ATOM 529 CZ PHE A 77 -20.700 -12.773 -59.581 1.00 90.67 C ANISOU 529 CZ PHE A 77 10816 13147 10488 501 315 44 C ATOM 530 N LEU A 78 -22.071 -8.238 -57.031 1.00 66.55 N ANISOU 530 N LEU A 78 7987 9671 7627 532 289 123 N ATOM 531 CA LEU A 78 -23.445 -8.216 -57.516 1.00 61.38 C ANISOU 531 CA LEU A 78 7308 9076 6938 646 279 117 C ATOM 532 C LEU A 78 -23.789 -6.919 -58.237 1.00 73.87 C ANISOU 532 C LEU A 78 8958 10592 8517 727 275 211 C ATOM 533 O LEU A 78 -24.773 -6.885 -58.982 1.00 78.04 O ANISOU 533 O LEU A 78 9452 11199 9000 832 257 233 O ATOM 534 CB LEU A 78 -24.410 -8.437 -56.352 1.00 48.71 C ANISOU 534 CB LEU A 78 5692 7464 5352 679 278 22 C ATOM 535 CG LEU A 78 -24.226 -9.751 -55.592 1.00 61.91 C ANISOU 535 CG LEU A 78 7317 9190 7016 605 283 -62 C ATOM 536 CD1 LEU A 78 -24.802 -9.638 -54.194 1.00 71.85 C ANISOU 536 CD1 LEU A 78 8603 10400 8296 608 296 -138 C ATOM 537 CD2 LEU A 78 -24.862 -10.908 -56.345 1.00 51.32 C ANISOU 537 CD2 LEU A 78 5891 7989 5621 616 275 -89 C ATOM 538 N LEU A 79 -23.009 -5.855 -58.029 1.00 70.18 N ANISOU 538 N LEU A 79 8591 9978 8094 677 286 269 N ATOM 539 CA LEU A 79 -23.260 -4.608 -58.743 1.00 71.39 C ANISOU 539 CA LEU A 79 8841 10038 8244 749 285 374 C ATOM 540 C LEU A 79 -23.011 -4.755 -60.237 1.00 83.96 C ANISOU 540 C LEU A 79 10405 11732 9763 759 289 479 C ATOM 541 O LEU A 79 -23.709 -4.133 -61.046 1.00 95.89 O ANISOU 541 O LEU A 79 11959 13242 11233 872 273 557 O ATOM 542 CB LEU A 79 -22.393 -3.487 -58.169 1.00 69.10 C ANISOU 542 CB LEU A 79 8683 9552 8019 658 297 409 C ATOM 543 CG LEU A 79 -22.785 -2.963 -56.787 1.00 72.55 C ANISOU 543 CG LEU A 79 9198 9854 8512 678 290 314 C ATOM 544 CD1 LEU A 79 -21.849 -1.848 -56.344 1.00 83.37 C ANISOU 544 CD1 LEU A 79 10714 11025 9940 564 293 346 C ATOM 545 CD2 LEU A 79 -24.228 -2.485 -56.791 1.00 61.77 C ANISOU 545 CD2 LEU A 79 7861 8472 7136 871 282 300 C ATOM 546 N THR A 80 -22.029 -5.566 -60.623 1.00 93.02 N ANISOU 546 N THR A 80 11484 12973 10884 655 311 482 N ATOM 547 CA THR A 80 -21.726 -5.814 -62.025 1.00 88.68 C ANISOU 547 CA THR A 80 10905 12539 10248 662 327 567 C ATOM 548 C THR A 80 -22.465 -7.022 -62.584 1.00 80.20 C ANISOU 548 C THR A 80 9730 11643 9097 730 303 501 C ATOM 549 O THR A 80 -22.334 -7.312 -63.777 1.00 91.72 O ANISOU 549 O THR A 80 11169 13215 10465 749 311 554 O ATOM 550 CB THR A 80 -20.217 -6.008 -62.213 1.00 93.14 C ANISOU 550 CB THR A 80 11445 13125 10819 523 375 605 C ATOM 551 OG1 THR A 80 -19.780 -7.141 -61.450 1.00 87.09 O ANISOU 551 OG1 THR A 80 10589 12421 10079 471 374 492 O ATOM 552 CG2 THR A 80 -19.459 -4.773 -61.751 1.00 97.03 C ANISOU 552 CG2 THR A 80 12037 13447 11384 423 395 675 C ATOM 553 N LEU A 81 -23.236 -7.725 -61.757 1.00 73.73 N ANISOU 553 N LEU A 81 8856 10853 8305 756 277 385 N ATOM 554 CA LEU A 81 -23.948 -8.928 -62.172 1.00 67.07 C ANISOU 554 CA LEU A 81 7923 10164 7398 788 251 308 C ATOM 555 C LEU A 81 -25.045 -8.631 -63.195 1.00 62.24 C ANISOU 555 C LEU A 81 7294 9647 6707 904 208 353 C ATOM 556 O LEU A 81 -25.206 -9.408 -64.146 1.00 66.60 O ANISOU 556 O LEU A 81 7798 10338 7169 911 190 338 O ATOM 557 CB LEU A 81 -24.530 -9.648 -60.952 1.00 66.97 C ANISOU 557 CB LEU A 81 7864 10144 7436 767 241 187 C ATOM 558 CG LEU A 81 -25.091 -11.049 -61.202 1.00 59.01 C ANISOU 558 CG LEU A 81 6777 9270 6376 752 222 96 C ATOM 559 CD1 LEU A 81 -24.037 -11.940 -61.839 1.00 51.04 C ANISOU 559 CD1 LEU A 81 5766 8308 5320 692 243 90 C ATOM 560 CD2 LEU A 81 -25.598 -11.662 -59.907 1.00 62.13 C ANISOU 560 CD2 LEU A 81 7145 9638 6822 712 225 -4 C ATOM 561 N PRO A 82 -25.831 -7.553 -63.051 1.00 59.94 N ANISOU 561 N PRO A 82 7042 9291 6439 1006 185 402 N ATOM 562 CA PRO A 82 -26.774 -7.216 -64.131 1.00 61.79 C ANISOU 562 CA PRO A 82 7260 9631 6588 1133 133 464 C ATOM 563 C PRO A 82 -26.095 -6.932 -65.458 1.00 73.37 C ANISOU 563 C PRO A 82 8785 11134 7961 1130 142 584 C ATOM 564 O PRO A 82 -26.700 -7.161 -66.513 1.00 73.05 O ANISOU 564 O PRO A 82 8707 11237 7810 1202 95 610 O ATOM 565 CB PRO A 82 -27.498 -5.975 -63.590 1.00 54.70 C ANISOU 565 CB PRO A 82 6420 8616 5748 1255 118 506 C ATOM 566 CG PRO A 82 -27.413 -6.109 -62.124 1.00 50.85 C ANISOU 566 CG PRO A 82 5928 8031 5362 1196 152 405 C ATOM 567 CD PRO A 82 -26.067 -6.713 -61.861 1.00 59.95 C ANISOU 567 CD PRO A 82 7100 9142 6537 1032 196 384 C ATOM 568 N LEU A 83 -24.854 -6.437 -65.438 1.00 69.79 N ANISOU 568 N LEU A 83 8415 10565 7537 1041 202 658 N ATOM 569 CA LEU A 83 -24.131 -6.210 -66.685 1.00 62.16 C ANISOU 569 CA LEU A 83 7497 9647 6472 1021 230 776 C ATOM 570 C LEU A 83 -23.876 -7.521 -67.417 1.00 67.04 C ANISOU 570 C LEU A 83 8030 10448 6993 981 236 708 C ATOM 571 O LEU A 83 -23.962 -7.580 -68.649 1.00 72.62 O ANISOU 571 O LEU A 83 8750 11273 7571 1026 225 770 O ATOM 572 CB LEU A 83 -22.815 -5.482 -66.410 1.00 50.61 C ANISOU 572 CB LEU A 83 6118 8039 5071 903 302 858 C ATOM 573 CG LEU A 83 -22.808 -3.956 -66.540 1.00 56.35 C ANISOU 573 CG LEU A 83 6993 8596 5823 935 308 1003 C ATOM 574 CD1 LEU A 83 -23.898 -3.322 -65.689 1.00 59.43 C ANISOU 574 CD1 LEU A 83 7424 8868 6288 1053 256 964 C ATOM 575 CD2 LEU A 83 -21.443 -3.395 -66.168 1.00 66.71 C ANISOU 575 CD2 LEU A 83 8366 9776 7203 771 379 1060 C ATOM 576 N TRP A 84 -23.562 -8.585 -66.676 1.00 59.21 N ANISOU 576 N TRP A 84 6968 9476 6055 905 251 578 N ATOM 577 CA TRP A 84 -23.378 -9.896 -67.286 1.00 58.29 C ANISOU 577 CA TRP A 84 6791 9505 5852 879 254 494 C ATOM 578 C TRP A 84 -24.698 -10.580 -67.608 1.00 60.20 C ANISOU 578 C TRP A 84 6975 9870 6030 942 176 408 C ATOM 579 O TRP A 84 -24.730 -11.457 -68.478 1.00 47.22 O ANISOU 579 O TRP A 84 5308 8356 4276 939 162 358 O ATOM 580 CB TRP A 84 -22.547 -10.799 -66.371 1.00 57.15 C ANISOU 580 CB TRP A 84 6609 9319 5785 787 295 394 C ATOM 581 CG TRP A 84 -21.205 -10.237 -66.014 1.00 58.92 C ANISOU 581 CG TRP A 84 6860 9456 6073 711 362 464 C ATOM 582 CD1 TRP A 84 -20.808 -9.778 -64.793 1.00 49.22 C ANISOU 582 CD1 TRP A 84 5643 8093 4965 652 371 456 C ATOM 583 CD2 TRP A 84 -20.082 -10.073 -66.889 1.00 60.81 C ANISOU 583 CD2 TRP A 84 7104 9751 6249 674 430 548 C ATOM 584 NE1 TRP A 84 -19.507 -9.340 -64.851 1.00 52.65 N ANISOU 584 NE1 TRP A 84 6083 8499 5423 571 430 527 N ATOM 585 CE2 TRP A 84 -19.039 -9.510 -66.127 1.00 57.81 C ANISOU 585 CE2 TRP A 84 6726 9272 5968 582 473 588 C ATOM 586 CE3 TRP A 84 -19.856 -10.347 -68.241 1.00 67.15 C ANISOU 586 CE3 TRP A 84 7909 10691 6913 705 460 590 C ATOM 587 CZ2 TRP A 84 -17.790 -9.218 -66.672 1.00 61.70 C ANISOU 587 CZ2 TRP A 84 7202 9807 6435 512 550 674 C ATOM 588 CZ3 TRP A 84 -18.616 -10.056 -68.780 1.00 68.57 C ANISOU 588 CZ3 TRP A 84 8085 10911 7060 648 546 676 C ATOM 589 CH2 TRP A 84 -17.599 -9.497 -67.997 1.00 61.81 C ANISOU 589 CH2 TRP A 84 7210 9961 6313 549 592 719 C ATOM 590 N ALA A 85 -25.783 -10.204 -66.928 1.00 70.51 N ANISOU 590 N ALA A 85 8250 11144 7397 995 125 383 N ATOM 591 CA ALA A 85 -27.082 -10.808 -67.208 1.00 73.79 C ANISOU 591 CA ALA A 85 8582 11699 7755 1041 48 304 C ATOM 592 C ALA A 85 -27.584 -10.408 -68.590 1.00 73.63 C ANISOU 592 C ALA A 85 8569 11810 7596 1136 -9 385 C ATOM 593 O ALA A 85 -27.987 -11.263 -69.387 1.00 73.49 O ANISOU 593 O ALA A 85 8507 11946 7469 1127 -57 320 O ATOM 594 CB ALA A 85 -28.090 -10.411 -66.129 1.00 74.41 C ANISOU 594 CB ALA A 85 8609 11732 7932 1085 22 266 C ATOM 595 N VAL A 86 -27.569 -9.107 -68.892 1.00 76.20 N ANISOU 595 N VAL A 86 8966 12070 7917 1228 -10 529 N ATOM 596 CA VAL A 86 -27.973 -8.650 -70.215 1.00 79.09 C ANISOU 596 CA VAL A 86 9361 12553 8138 1330 -65 630 C ATOM 597 C VAL A 86 -26.909 -8.960 -71.259 1.00 77.13 C ANISOU 597 C VAL A 86 9177 12357 7770 1272 -12 680 C ATOM 598 O VAL A 86 -27.222 -9.047 -72.452 1.00 76.35 O ANISOU 598 O VAL A 86 9088 12407 7514 1329 -61 720 O ATOM 599 CB VAL A 86 -28.291 -7.144 -70.192 1.00 77.50 C ANISOU 599 CB VAL A 86 9241 12240 7966 1458 -80 780 C ATOM 600 CG1 VAL A 86 -29.423 -6.857 -69.217 1.00 71.65 C ANISOU 600 CG1 VAL A 86 8424 11474 7327 1545 -128 719 C ATOM 601 CG2 VAL A 86 -27.056 -6.350 -69.820 1.00 86.49 C ANISOU 601 CG2 VAL A 86 10505 13176 9181 1387 16 877 C ATOM 602 N TYR A 87 -25.652 -9.124 -70.838 1.00 78.74 N ANISOU 602 N TYR A 87 9418 12460 8039 1165 85 678 N ATOM 603 CA TYR A 87 -24.603 -9.543 -71.762 1.00 67.70 C ANISOU 603 CA TYR A 87 8056 11135 6530 1111 152 706 C ATOM 604 C TYR A 87 -24.909 -10.920 -72.336 1.00 69.96 C ANISOU 604 C TYR A 87 8286 11587 6710 1097 115 564 C ATOM 605 O TYR A 87 -24.855 -11.125 -73.554 1.00 69.99 O ANISOU 605 O TYR A 87 8320 11728 6547 1128 106 590 O ATOM 606 CB TYR A 87 -23.252 -9.536 -71.043 1.00 74.15 C ANISOU 606 CB TYR A 87 8886 11831 7455 1002 256 711 C ATOM 607 CG TYR A 87 -22.083 -10.049 -71.856 1.00 75.11 C ANISOU 607 CG TYR A 87 9017 12043 7480 950 342 725 C ATOM 608 CD1 TYR A 87 -21.668 -9.393 -73.007 1.00 83.15 C ANISOU 608 CD1 TYR A 87 10101 13125 8367 970 384 868 C ATOM 609 CD2 TYR A 87 -21.376 -11.175 -71.453 1.00 61.39 C ANISOU 609 CD2 TYR A 87 7223 10326 5776 889 387 599 C ATOM 610 CE1 TYR A 87 -20.593 -9.854 -73.745 1.00 74.05 C ANISOU 610 CE1 TYR A 87 8944 12075 7117 927 478 878 C ATOM 611 CE2 TYR A 87 -20.299 -11.643 -72.184 1.00 60.59 C ANISOU 611 CE2 TYR A 87 7118 10318 5585 865 474 605 C ATOM 612 CZ TYR A 87 -19.913 -10.978 -73.328 1.00 67.82 C ANISOU 612 CZ TYR A 87 8085 11314 6368 881 524 741 C ATOM 613 OH TYR A 87 -18.843 -11.438 -74.060 1.00 67.95 O ANISOU 613 OH TYR A 87 8088 11444 6286 862 624 744 O ATOM 614 N THR A 88 -25.251 -11.875 -71.469 1.00 73.94 N ANISOU 614 N THR A 88 8722 12071 7300 1044 93 411 N ATOM 615 CA THR A 88 -25.623 -13.205 -71.937 1.00 68.55 C ANISOU 615 CA THR A 88 8005 11514 6526 1015 52 265 C ATOM 616 C THR A 88 -26.987 -13.197 -72.614 1.00 70.65 C ANISOU 616 C THR A 88 8226 11928 6689 1078 -67 245 C ATOM 617 O THR A 88 -27.253 -14.035 -73.484 1.00 76.99 O ANISOU 617 O THR A 88 9029 12870 7356 1065 -112 161 O ATOM 618 CB THR A 88 -25.612 -14.192 -70.769 1.00 60.66 C ANISOU 618 CB THR A 88 6965 10432 5652 930 64 122 C ATOM 619 OG1 THR A 88 -24.399 -14.034 -70.022 1.00 63.01 O ANISOU 619 OG1 THR A 88 7290 10598 6055 887 158 155 O ATOM 620 CG2 THR A 88 -25.702 -15.626 -71.272 1.00 64.76 C ANISOU 620 CG2 THR A 88 7489 11037 6079 883 43 -28 C ATOM 621 N ALA A 89 -27.859 -12.258 -72.240 1.00 61.94 N ANISOU 621 N ALA A 89 7085 10805 5644 1152 -122 318 N ATOM 622 CA ALA A 89 -29.185 -12.200 -72.846 1.00 56.42 C ANISOU 622 CA ALA A 89 6316 10270 4850 1227 -245 305 C ATOM 623 C ALA A 89 -29.112 -11.786 -74.310 1.00 72.48 C ANISOU 623 C ALA A 89 8414 12433 6690 1309 -281 408 C ATOM 624 O ALA A 89 -29.871 -12.297 -75.142 1.00 86.18 O ANISOU 624 O ALA A 89 10105 14352 8286 1328 -380 348 O ATOM 625 CB ALA A 89 -30.081 -11.240 -72.065 1.00 58.68 C ANISOU 625 CB ALA A 89 6543 10506 5248 1317 -286 362 C ATOM 626 N MET A 90 -28.211 -10.864 -74.646 1.00 74.22 N ANISOU 626 N MET A 90 8741 12567 6891 1348 -205 566 N ATOM 627 CA MET A 90 -28.105 -10.375 -76.015 1.00 66.16 C ANISOU 627 CA MET A 90 7800 11662 5677 1426 -227 690 C ATOM 628 C MET A 90 -27.147 -11.236 -76.829 1.00 74.51 C ANISOU 628 C MET A 90 8909 12799 6601 1352 -157 635 C ATOM 629 O MET A 90 -26.510 -10.746 -77.767 1.00 58.04 O ANISOU 629 O MET A 90 6916 10755 4381 1383 -106 761 O ATOM 630 CB MET A 90 -27.653 -8.916 -76.040 1.00 60.04 C ANISOU 630 CB MET A 90 7129 10750 4933 1496 -175 901 C ATOM 631 CG MET A 90 -28.557 -7.962 -75.279 1.00 68.29 C ANISOU 631 CG MET A 90 8149 11697 6100 1600 -237 960 C ATOM 632 SD MET A 90 -28.211 -6.239 -75.684 1.00 88.23 S ANISOU 632 SD MET A 90 10844 14076 8604 1708 -205 1221 S ATOM 633 CE MET A 90 -26.431 -6.195 -75.499 1.00 79.27 C ANISOU 633 CE MET A 90 9802 12793 7523 1535 -31 1270 C ATOM 634 N GLU A 91 -27.041 -12.516 -76.468 1.00 64.38 N ANISOU 634 N GLU A 91 7577 11533 5352 1258 -147 450 N ATOM 635 CA GLU A 91 -26.196 -13.477 -77.173 1.00 62.89 C ANISOU 635 CA GLU A 91 7439 11415 5041 1206 -82 365 C ATOM 636 C GLU A 91 -24.734 -13.027 -77.176 1.00 55.79 C ANISOU 636 C GLU A 91 6604 10427 4168 1184 70 472 C ATOM 637 O GLU A 91 -24.062 -13.016 -78.209 1.00 95.30 O ANISOU 637 O GLU A 91 11673 15528 9010 1202 132 526 O ATOM 638 CB GLU A 91 -26.713 -13.721 -78.592 1.00 75.85 C ANISOU 638 CB GLU A 91 9116 13267 6437 1260 -164 353 C ATOM 639 CG GLU A 91 -28.203 -14.036 -78.647 1.00 81.40 C ANISOU 639 CG GLU A 91 9731 14088 7107 1276 -329 261 C ATOM 640 CD GLU A 91 -28.625 -14.688 -79.948 1.00 93.07 C ANISOU 640 CD GLU A 91 11240 15780 8342 1288 -417 180 C ATOM 641 OE1 GLU A 91 -27.750 -14.928 -80.807 1.00100.82 O ANISOU 641 OE1 GLU A 91 12322 16814 9173 1293 -339 189 O ATOM 642 OE2 GLU A 91 -29.832 -14.967 -80.111 1.00 96.46 O ANISOU 642 OE2 GLU A 91 11587 16339 8724 1290 -563 101 O ATOM 643 N TYR A 92 -24.251 -12.643 -75.993 1.00 61.28 N ANISOU 643 N TYR A 92 7274 10948 5063 1137 131 502 N ATOM 644 CA TYR A 92 -22.858 -12.256 -75.768 1.00 55.46 C ANISOU 644 CA TYR A 92 6565 10123 4385 1089 268 587 C ATOM 645 C TYR A 92 -22.473 -11.036 -76.609 1.00 65.70 C ANISOU 645 C TYR A 92 7939 11440 5582 1124 314 796 C ATOM 646 O TYR A 92 -21.552 -11.069 -77.427 1.00 68.74 O ANISOU 646 O TYR A 92 8363 11908 5847 1109 411 852 O ATOM 647 CB TYR A 92 -21.912 -13.434 -76.024 1.00 64.85 C ANISOU 647 CB TYR A 92 7748 11373 5521 1050 351 466 C ATOM 648 CG TYR A 92 -22.098 -14.579 -75.053 1.00 75.64 C ANISOU 648 CG TYR A 92 9064 12668 7006 1006 323 283 C ATOM 649 CD1 TYR A 92 -21.905 -14.395 -73.689 1.00 72.30 C ANISOU 649 CD1 TYR A 92 8598 12088 6785 957 337 278 C ATOM 650 CD2 TYR A 92 -22.461 -15.843 -75.498 1.00 77.33 C ANISOU 650 CD2 TYR A 92 9293 12967 7124 1008 281 116 C ATOM 651 CE1 TYR A 92 -22.074 -15.437 -72.796 1.00 72.53 C ANISOU 651 CE1 TYR A 92 8597 12049 6911 916 314 127 C ATOM 652 CE2 TYR A 92 -22.631 -16.891 -74.611 1.00 63.14 C ANISOU 652 CE2 TYR A 92 7474 11083 5432 959 259 -38 C ATOM 653 CZ TYR A 92 -22.437 -16.683 -73.263 1.00 66.21 C ANISOU 653 CZ TYR A 92 7819 11320 6017 916 277 -25 C ATOM 654 OH TYR A 92 -22.604 -17.723 -72.378 1.00 66.20 O ANISOU 654 OH TYR A 92 7811 11231 6110 867 258 -163 O ATOM 655 N ARG A 93 -23.204 -9.947 -76.384 1.00 61.60 N ANISOU 655 N ARG A 93 7450 10843 5113 1177 249 913 N ATOM 656 CA ARG A 93 -22.888 -8.640 -76.943 1.00 57.33 C ANISOU 656 CA ARG A 93 7008 10258 4516 1204 289 1130 C ATOM 657 C ARG A 93 -22.649 -7.671 -75.794 1.00 69.17 C ANISOU 657 C ARG A 93 8527 11534 6220 1162 318 1206 C ATOM 658 O ARG A 93 -23.474 -7.576 -74.880 1.00 73.81 O ANISOU 658 O ARG A 93 9074 12033 6935 1198 242 1142 O ATOM 659 CB ARG A 93 -24.013 -8.124 -77.843 1.00 58.99 C ANISOU 659 CB ARG A 93 7271 10568 4576 1334 174 1217 C ATOM 660 CG ARG A 93 -24.182 -8.886 -79.145 1.00 60.27 C ANISOU 660 CG ARG A 93 7443 10959 4498 1372 143 1169 C ATOM 661 CD ARG A 93 -25.303 -8.288 -79.978 1.00 82.67 C ANISOU 661 CD ARG A 93 10326 13900 7185 1508 13 1268 C ATOM 662 NE ARG A 93 -25.481 -8.989 -81.246 1.00 82.89 N ANISOU 662 NE ARG A 93 10372 14159 6963 1541 -28 1218 N ATOM 663 CZ ARG A 93 -26.217 -10.085 -81.395 1.00 87.81 C ANISOU 663 CZ ARG A 93 10914 14922 7526 1542 -129 1026 C ATOM 664 NH1 ARG A 93 -26.845 -10.611 -80.351 1.00 89.92 N ANISOU 664 NH1 ARG A 93 11070 15126 7969 1508 -190 878 N ATOM 665 NH2 ARG A 93 -26.325 -10.657 -82.586 1.00 87.12 N ANISOU 665 NH2 ARG A 93 10866 15039 7198 1566 -167 981 N ATOM 666 N TRP A 94 -21.524 -6.958 -75.840 1.00 68.56 N ANISOU 666 N TRP A 94 8509 11372 6168 1077 432 1337 N ATOM 667 CA TRP A 94 -21.144 -6.053 -74.760 1.00 75.14 C ANISOU 667 CA TRP A 94 9374 11987 7190 1008 464 1398 C ATOM 668 C TRP A 94 -21.364 -4.606 -75.181 1.00 74.86 C ANISOU 668 C TRP A 94 9487 11836 7122 1052 457 1608 C ATOM 669 O TRP A 94 -20.574 -4.061 -75.967 1.00 73.79 O ANISOU 669 O TRP A 94 9431 11713 6891 992 544 1761 O ATOM 670 CB TRP A 94 -19.683 -6.278 -74.359 1.00 73.97 C ANISOU 670 CB TRP A 94 9176 11813 7115 856 590 1385 C ATOM 671 CG TRP A 94 -19.293 -5.513 -73.137 1.00 55.42 C ANISOU 671 CG TRP A 94 6844 9251 4961 767 607 1409 C ATOM 672 CD1 TRP A 94 -18.563 -4.361 -73.087 1.00 61.00 C ANISOU 672 CD1 TRP A 94 7640 9824 5714 667 674 1565 C ATOM 673 CD2 TRP A 94 -19.627 -5.836 -71.783 1.00 53.67 C ANISOU 673 CD2 TRP A 94 6562 8925 4906 758 554 1271 C ATOM 674 NE1 TRP A 94 -18.417 -3.951 -71.784 1.00 77.76 N ANISOU 674 NE1 TRP A 94 9762 11763 8021 598 659 1519 N ATOM 675 CE2 TRP A 94 -19.061 -4.839 -70.964 1.00 87.14 C ANISOU 675 CE2 TRP A 94 10858 12972 9280 660 588 1341 C ATOM 676 CE3 TRP A 94 -20.348 -6.872 -71.182 1.00 57.97 C ANISOU 676 CE3 TRP A 94 7018 9518 5490 813 485 1095 C ATOM 677 CZ2 TRP A 94 -19.194 -4.849 -69.577 1.00 75.43 C ANISOU 677 CZ2 TRP A 94 9346 11356 7958 629 551 1237 C ATOM 678 CZ3 TRP A 94 -20.478 -6.881 -69.806 1.00 64.63 C ANISOU 678 CZ3 TRP A 94 7831 10229 6495 779 458 1006 C ATOM 679 CH2 TRP A 94 -19.903 -5.877 -69.019 1.00 73.63 C ANISOU 679 CH2 TRP A 94 9029 11190 7756 695 490 1074 C ATOM 680 N PRO A 95 -22.411 -3.941 -74.692 1.00 72.50 N ANISOU 680 N PRO A 95 9234 11418 6895 1160 361 1627 N ATOM 681 CA PRO A 95 -22.670 -2.541 -75.070 1.00 75.87 C ANISOU 681 CA PRO A 95 9829 11706 7294 1228 347 1830 C ATOM 682 C PRO A 95 -22.206 -1.502 -74.054 1.00 75.39 C ANISOU 682 C PRO A 95 9861 11372 7412 1146 392 1890 C ATOM 683 O PRO A 95 -22.524 -0.322 -74.236 1.00 75.42 O ANISOU 683 O PRO A 95 10026 11218 7412 1215 371 2045 O ATOM 684 CB PRO A 95 -24.197 -2.528 -75.170 1.00 75.08 C ANISOU 684 CB PRO A 95 9708 11665 7155 1429 205 1794 C ATOM 685 CG PRO A 95 -24.614 -3.441 -74.045 1.00 63.81 C ANISOU 685 CG PRO A 95 8125 10256 5865 1410 167 1576 C ATOM 686 CD PRO A 95 -23.534 -4.509 -73.926 1.00 62.84 C ANISOU 686 CD PRO A 95 7911 10213 5751 1248 257 1466 C ATOM 687 N PHE A 96 -21.484 -1.899 -73.008 1.00 75.55 N ANISOU 687 N PHE A 96 9798 11327 7580 1007 444 1772 N ATOM 688 CA PHE A 96 -21.131 -1.000 -71.918 1.00 70.63 C ANISOU 688 CA PHE A 96 9256 10452 7129 925 466 1793 C ATOM 689 C PHE A 96 -19.749 -0.380 -72.081 1.00 74.06 C ANISOU 689 C PHE A 96 9762 10798 7581 727 581 1917 C ATOM 690 O PHE A 96 -19.260 0.267 -71.150 1.00 77.31 O ANISOU 690 O PHE A 96 10229 11012 8135 613 605 1916 O ATOM 691 CB PHE A 96 -21.222 -1.738 -70.583 1.00 71.35 C ANISOU 691 CB PHE A 96 9219 10525 7367 891 442 1590 C ATOM 692 CG PHE A 96 -22.551 -2.392 -70.350 1.00 70.29 C ANISOU 692 CG PHE A 96 8998 10487 7224 1053 342 1463 C ATOM 693 CD1 PHE A 96 -23.676 -1.626 -70.095 1.00 68.92 C ANISOU 693 CD1 PHE A 96 8896 10212 7080 1211 266 1492 C ATOM 694 CD2 PHE A 96 -22.676 -3.770 -70.392 1.00 66.13 C ANISOU 694 CD2 PHE A 96 8316 10153 6657 1046 326 1315 C ATOM 695 CE1 PHE A 96 -24.902 -2.222 -69.885 1.00 55.70 C ANISOU 695 CE1 PHE A 96 7113 8655 5397 1349 180 1376 C ATOM 696 CE2 PHE A 96 -23.899 -4.372 -70.180 1.00 62.18 C ANISOU 696 CE2 PHE A 96 7730 9747 6150 1165 238 1201 C ATOM 697 CZ PHE A 96 -25.014 -3.596 -69.926 1.00 57.84 C ANISOU 697 CZ PHE A 96 7226 9122 5631 1311 166 1232 C ATOM 698 N GLY A 97 -19.113 -0.557 -73.234 1.00 78.31 N ANISOU 698 N GLY A 97 10297 11486 7971 673 654 2021 N ATOM 699 CA GLY A 97 -17.823 0.050 -73.480 1.00 75.67 C ANISOU 699 CA GLY A 97 10015 11096 7640 475 774 2154 C ATOM 700 C GLY A 97 -16.674 -0.760 -72.913 1.00 79.78 C ANISOU 700 C GLY A 97 10358 11716 8237 311 850 2034 C ATOM 701 O GLY A 97 -16.841 -1.823 -72.311 1.00 86.68 O ANISOU 701 O GLY A 97 11086 12686 9161 354 810 1851 O ATOM 702 N ASN A 98 -15.468 -0.225 -73.113 1.00 80.57 N ANISOU 702 N ASN A 98 10473 11794 8345 115 961 2150 N ATOM 703 CA ASN A 98 -14.257 -0.923 -72.698 1.00 68.02 C ANISOU 703 CA ASN A 98 8700 10331 6815 -38 1040 2060 C ATOM 704 C ASN A 98 -13.949 -0.708 -71.220 1.00 79.62 C ANISOU 704 C ASN A 98 10133 11634 8486 -145 1000 1956 C ATOM 705 O ASN A 98 -13.431 -1.617 -70.561 1.00 77.05 O ANISOU 705 O ASN A 98 9636 11415 8225 -178 1002 1810 O ATOM 706 CB ASN A 98 -13.079 -0.468 -73.562 1.00 66.87 C ANISOU 706 CB ASN A 98 8552 10271 6584 -212 1183 2227 C ATOM 707 CG ASN A 98 -11.936 -1.459 -73.559 1.00 82.12 C ANISOU 707 CG ASN A 98 10255 12437 8509 -299 1274 2135 C ATOM 708 OD1 ASN A 98 -12.069 -2.577 -74.058 1.00103.42 O ANISOU 708 OD1 ASN A 98 12848 15344 11104 -172 1282 2037 O ATOM 709 ND2 ASN A 98 -10.798 -1.051 -73.012 1.00 83.71 N ANISOU 709 ND2 ASN A 98 10381 12610 8817 -514 1342 2164 N ATOM 710 N TYR A 99 -14.266 0.473 -70.685 1.00 84.13 N ANISOU 710 N TYR A 99 10876 11941 9149 -188 960 2027 N ATOM 711 CA TYR A 99 -13.990 0.754 -69.279 1.00 76.66 C ANISOU 711 CA TYR A 99 9920 10828 8379 -294 917 1924 C ATOM 712 C TYR A 99 -14.843 -0.113 -68.362 1.00 83.59 C ANISOU 712 C TYR A 99 10717 11726 9319 -138 818 1726 C ATOM 713 O TYR A 99 -14.334 -0.714 -67.409 1.00 89.37 O ANISOU 713 O TYR A 99 11319 12496 10142 -207 805 1591 O ATOM 714 CB TYR A 99 -14.229 2.236 -68.986 1.00 97.20 C ANISOU 714 CB TYR A 99 12759 13124 11050 -356 897 2038 C ATOM 715 CG TYR A 99 -13.010 3.112 -69.170 1.00121.67 C ANISOU 715 CG TYR A 99 15911 16143 14176 -625 990 2178 C ATOM 716 CD1 TYR A 99 -12.487 3.836 -68.106 1.00126.68 C ANISOU 716 CD1 TYR A 99 16605 16571 14955 -810 971 2142 C ATOM 717 CD2 TYR A 99 -12.381 3.211 -70.403 1.00133.66 C ANISOU 717 CD2 TYR A 99 17420 17799 15566 -709 1098 2342 C ATOM 718 CE1 TYR A 99 -11.374 4.639 -68.267 1.00131.51 C ANISOU 718 CE1 TYR A 99 17259 17114 15595 -1085 1053 2266 C ATOM 719 CE2 TYR A 99 -11.267 4.010 -70.574 1.00136.23 C ANISOU 719 CE2 TYR A 99 17782 18064 15916 -979 1193 2476 C ATOM 720 CZ TYR A 99 -10.768 4.722 -69.502 1.00136.77 C ANISOU 720 CZ TYR A 99 17902 17924 16140 -1174 1168 2437 C ATOM 721 OH TYR A 99 -9.659 5.519 -69.665 1.00142.67 O ANISOU 721 OH TYR A 99 18679 18614 16914 -1470 1258 2567 O ATOM 722 N LEU A 100 -16.148 -0.190 -68.635 1.00 82.85 N ANISOU 722 N LEU A 100 10694 11615 9171 71 747 1711 N ATOM 723 CA LEU A 100 -17.051 -0.920 -67.753 1.00 78.47 C ANISOU 723 CA LEU A 100 10070 11071 8673 205 660 1535 C ATOM 724 C LEU A 100 -16.792 -2.421 -67.755 1.00 72.14 C ANISOU 724 C LEU A 100 9072 10502 7838 225 668 1399 C ATOM 725 O LEU A 100 -17.212 -3.105 -66.816 1.00 93.22 O ANISOU 725 O LEU A 100 11670 13173 10575 273 613 1248 O ATOM 726 CB LEU A 100 -18.505 -0.644 -68.137 1.00 82.28 C ANISOU 726 CB LEU A 100 10648 11515 9098 420 585 1558 C ATOM 727 CG LEU A 100 -19.034 0.741 -67.757 1.00 85.33 C ANISOU 727 CG LEU A 100 11238 11635 9550 462 552 1641 C ATOM 728 CD1 LEU A 100 -20.499 0.884 -68.135 1.00 81.22 C ANISOU 728 CD1 LEU A 100 10771 11121 8969 707 472 1653 C ATOM 729 CD2 LEU A 100 -18.834 0.996 -66.271 1.00 83.61 C ANISOU 729 CD2 LEU A 100 11033 11248 9487 381 531 1522 C ATOM 730 N CYS A 101 -16.118 -2.954 -68.775 1.00 79.01 N ANISOU 730 N CYS A 101 9865 11559 8598 192 740 1449 N ATOM 731 CA CYS A 101 -15.799 -4.377 -68.747 1.00 89.19 C ANISOU 731 CA CYS A 101 10988 13043 9858 219 751 1313 C ATOM 732 C CYS A 101 -14.522 -4.649 -67.964 1.00 89.35 C ANISOU 732 C CYS A 101 10891 13084 9975 69 797 1261 C ATOM 733 O CYS A 101 -14.419 -5.674 -67.281 1.00 82.88 O ANISOU 733 O CYS A 101 9963 12329 9198 98 769 1118 O ATOM 734 CB CYS A 101 -15.671 -4.938 -70.161 1.00 97.60 C ANISOU 734 CB CYS A 101 12020 14313 10751 276 807 1363 C ATOM 735 SG CYS A 101 -15.429 -6.726 -70.145 1.00103.78 S ANISOU 735 SG CYS A 101 12636 15301 11493 340 813 1178 S ATOM 736 N LYS A 102 -13.535 -3.753 -68.056 1.00 78.89 N ANISOU 736 N LYS A 102 9585 11708 8679 -96 865 1379 N ATOM 737 CA LYS A 102 -12.345 -3.892 -67.224 1.00 73.63 C ANISOU 737 CA LYS A 102 8796 11066 8114 -249 891 1330 C ATOM 738 C LYS A 102 -12.697 -3.823 -65.745 1.00 77.51 C ANISOU 738 C LYS A 102 9310 11401 8740 -257 798 1212 C ATOM 739 O LYS A 102 -11.992 -4.400 -64.911 1.00 93.68 O ANISOU 739 O LYS A 102 11233 13505 10856 -315 784 1116 O ATOM 740 CB LYS A 102 -11.318 -2.816 -67.577 1.00 70.34 C ANISOU 740 CB LYS A 102 8404 10614 7709 -453 975 1484 C ATOM 741 CG LYS A 102 -10.680 -2.979 -68.947 1.00 58.12 C ANISOU 741 CG LYS A 102 6796 9264 6023 -476 1093 1598 C ATOM 742 CD LYS A 102 -9.636 -1.900 -69.191 1.00 79.13 C ANISOU 742 CD LYS A 102 9473 11888 8706 -712 1183 1754 C ATOM 743 CE LYS A 102 -8.957 -2.068 -70.540 1.00 62.11 C ANISOU 743 CE LYS A 102 7246 9952 6402 -742 1319 1872 C ATOM 744 NZ LYS A 102 -8.254 -3.374 -70.659 1.00 61.46 N ANISOU 744 NZ LYS A 102 6932 10140 6279 -678 1369 1757 N ATOM 745 N ILE A 103 -13.782 -3.126 -65.403 1.00 61.88 N ANISOU 745 N ILE A 103 7487 9233 6792 -188 733 1217 N ATOM 746 CA ILE A 103 -14.243 -3.089 -64.020 1.00 63.37 C ANISOU 746 CA ILE A 103 7706 9283 7087 -173 652 1096 C ATOM 747 C ILE A 103 -15.087 -4.316 -63.702 1.00 73.44 C ANISOU 747 C ILE A 103 8911 10653 8341 -13 600 957 C ATOM 748 O ILE A 103 -14.942 -4.923 -62.635 1.00 91.03 O ANISOU 748 O ILE A 103 11072 12884 10633 -25 561 838 O ATOM 749 CB ILE A 103 -15.015 -1.784 -63.755 1.00 60.26 C ANISOU 749 CB ILE A 103 7513 8645 6736 -157 615 1155 C ATOM 750 CG1 ILE A 103 -14.105 -0.572 -63.969 1.00 67.11 C ANISOU 750 CG1 ILE A 103 8475 9389 7637 -349 665 1288 C ATOM 751 CG2 ILE A 103 -15.596 -1.779 -62.350 1.00 51.91 C ANISOU 751 CG2 ILE A 103 6492 7461 5771 -118 540 1018 C ATOM 752 CD1 ILE A 103 -12.892 -0.551 -63.064 1.00 79.04 C ANISOU 752 CD1 ILE A 103 9893 10901 9238 -553 669 1234 C ATOM 753 N ALA A 104 -15.975 -4.706 -64.621 1.00 61.35 N ANISOU 753 N ALA A 104 7395 9203 6713 129 596 974 N ATOM 754 CA ALA A 104 -16.854 -5.843 -64.368 1.00 60.40 C ANISOU 754 CA ALA A 104 7215 9164 6569 258 546 844 C ATOM 755 C ALA A 104 -16.076 -7.152 -64.334 1.00 60.70 C ANISOU 755 C ALA A 104 7114 9360 6588 240 572 758 C ATOM 756 O ALA A 104 -16.332 -8.010 -63.481 1.00 62.65 O ANISOU 756 O ALA A 104 7315 9613 6875 273 530 636 O ATOM 757 CB ALA A 104 -17.957 -5.900 -65.423 1.00 55.69 C ANISOU 757 CB ALA A 104 6663 8631 5867 397 526 883 C ATOM 758 N SER A 105 -15.124 -7.329 -65.254 1.00 70.51 N ANISOU 758 N SER A 105 8295 10732 7765 196 645 824 N ATOM 759 CA SER A 105 -14.317 -8.544 -65.248 1.00 74.07 C ANISOU 759 CA SER A 105 8616 11331 8196 203 676 743 C ATOM 760 C SER A 105 -13.369 -8.580 -64.057 1.00 64.96 C ANISOU 760 C SER A 105 7387 10142 7152 104 664 697 C ATOM 761 O SER A 105 -13.041 -9.664 -63.561 1.00 63.58 O ANISOU 761 O SER A 105 7129 10036 6991 145 649 596 O ATOM 762 CB SER A 105 -13.534 -8.666 -66.554 1.00 70.30 C ANISOU 762 CB SER A 105 8085 11016 7609 193 770 823 C ATOM 763 OG SER A 105 -14.408 -8.718 -67.668 1.00 68.77 O ANISOU 763 OG SER A 105 7963 10873 7293 292 770 858 O ATOM 764 N ALA A 106 -12.917 -7.415 -63.587 1.00 58.25 N ANISOU 764 N ALA A 106 6574 9182 6377 -28 665 768 N ATOM 765 CA ALA A 106 -12.084 -7.384 -62.391 1.00 65.37 C ANISOU 765 CA ALA A 106 7409 10053 7378 -131 634 717 C ATOM 766 C ALA A 106 -12.907 -7.664 -61.142 1.00 67.64 C ANISOU 766 C ALA A 106 7754 10222 7723 -76 546 603 C ATOM 767 O ALA A 106 -12.447 -8.364 -60.234 1.00 70.73 O ANISOU 767 O ALA A 106 8072 10649 8154 -82 510 518 O ATOM 768 CB ALA A 106 -11.376 -6.036 -62.272 1.00 49.94 C ANISOU 768 CB ALA A 106 5490 8007 5480 -311 656 818 C ATOM 769 N SER A 107 -14.130 -7.128 -61.080 1.00 68.52 N ANISOU 769 N SER A 107 7995 10204 7834 -15 514 605 N ATOM 770 CA SER A 107 -14.988 -7.369 -59.925 1.00 58.74 C ANISOU 770 CA SER A 107 6807 8870 6640 40 446 500 C ATOM 771 C SER A 107 -15.309 -8.849 -59.766 1.00 56.30 C ANISOU 771 C SER A 107 6428 8666 6295 138 429 399 C ATOM 772 O SER A 107 -15.492 -9.326 -58.640 1.00 68.80 O ANISOU 772 O SER A 107 8014 10212 7917 145 384 310 O ATOM 773 CB SER A 107 -16.276 -6.554 -60.048 1.00 65.32 C ANISOU 773 CB SER A 107 7770 9578 7469 114 426 525 C ATOM 774 OG SER A 107 -17.087 -6.703 -58.895 1.00 81.97 O ANISOU 774 OG SER A 107 9920 11607 9619 162 376 424 O ATOM 775 N VAL A 108 -15.380 -9.589 -60.874 1.00 69.93 N ANISOU 775 N VAL A 108 8109 10518 7942 210 466 411 N ATOM 776 CA VAL A 108 -15.582 -11.032 -60.791 1.00 78.24 C ANISOU 776 CA VAL A 108 9115 11654 8959 290 453 314 C ATOM 777 C VAL A 108 -14.322 -11.716 -60.276 1.00 80.85 C ANISOU 777 C VAL A 108 9353 12051 9318 258 460 280 C ATOM 778 O VAL A 108 -14.390 -12.621 -59.434 1.00 67.77 O ANISOU 778 O VAL A 108 7689 10382 7679 294 422 195 O ATOM 779 CB VAL A 108 -16.011 -11.589 -62.161 1.00 57.70 C ANISOU 779 CB VAL A 108 6510 9161 6254 373 485 325 C ATOM 780 CG1 VAL A 108 -16.060 -13.110 -62.127 1.00 42.98 C ANISOU 780 CG1 VAL A 108 4614 7365 4353 441 477 219 C ATOM 781 CG2 VAL A 108 -17.360 -11.016 -62.567 1.00 43.59 C ANISOU 781 CG2 VAL A 108 4800 7326 4436 423 457 349 C ATOM 782 N SER A 109 -13.154 -11.296 -60.767 1.00 78.65 N ANISOU 782 N SER A 109 8995 11849 9038 193 509 352 N ATOM 783 CA SER A 109 -11.903 -11.892 -60.309 1.00 73.71 C ANISOU 783 CA SER A 109 8252 11315 8439 175 512 326 C ATOM 784 C SER A 109 -11.543 -11.416 -58.907 1.00 75.50 C ANISOU 784 C SER A 109 8476 11456 8752 84 447 303 C ATOM 785 O SER A 109 -11.026 -12.193 -58.096 1.00 66.79 O ANISOU 785 O SER A 109 7317 10390 7669 113 406 242 O ATOM 786 CB SER A 109 -10.777 -11.569 -61.290 1.00 73.24 C ANISOU 786 CB SER A 109 8084 11395 8347 126 594 411 C ATOM 787 OG SER A 109 -11.097 -12.010 -62.598 1.00 94.20 O ANISOU 787 OG SER A 109 10752 14138 10903 215 657 427 O ATOM 788 N PHE A 110 -11.805 -10.141 -58.604 1.00 75.43 N ANISOU 788 N PHE A 110 8543 11329 8789 -20 431 349 N ATOM 789 CA PHE A 110 -11.514 -9.621 -57.271 1.00 67.43 C ANISOU 789 CA PHE A 110 7549 10225 7846 -114 364 314 C ATOM 790 C PHE A 110 -12.355 -10.321 -56.212 1.00 75.18 C ANISOU 790 C PHE A 110 8599 11136 8828 -33 303 215 C ATOM 791 O PHE A 110 -11.860 -10.638 -55.124 1.00 66.08 O ANISOU 791 O PHE A 110 7419 9988 7701 -58 246 162 O ATOM 792 CB PHE A 110 -11.752 -8.110 -57.234 1.00 63.65 C ANISOU 792 CB PHE A 110 7173 9603 7406 -228 364 374 C ATOM 793 CG PHE A 110 -11.386 -7.465 -55.927 1.00 71.19 C ANISOU 793 CG PHE A 110 8164 10459 8425 -343 296 330 C ATOM 794 CD1 PHE A 110 -10.092 -7.032 -55.694 1.00 78.45 C ANISOU 794 CD1 PHE A 110 8986 11438 9383 -496 284 359 C ATOM 795 CD2 PHE A 110 -12.339 -7.279 -54.938 1.00 65.48 C ANISOU 795 CD2 PHE A 110 7566 9598 7715 -305 245 256 C ATOM 796 CE1 PHE A 110 -9.751 -6.435 -54.497 1.00 76.01 C ANISOU 796 CE1 PHE A 110 8715 11043 9122 -614 209 308 C ATOM 797 CE2 PHE A 110 -12.003 -6.683 -53.738 1.00 63.48 C ANISOU 797 CE2 PHE A 110 7359 9257 7503 -408 181 205 C ATOM 798 CZ PHE A 110 -10.707 -6.259 -53.519 1.00 74.90 C ANISOU 798 CZ PHE A 110 8719 10754 8984 -566 157 228 C ATOM 799 N ASN A 111 -13.630 -10.577 -56.515 1.00 69.86 N ANISOU 799 N ASN A 111 8011 10411 8121 60 313 191 N ATOM 800 CA ASN A 111 -14.508 -11.217 -55.541 1.00 56.66 C ANISOU 800 CA ASN A 111 6402 8680 6446 119 270 105 C ATOM 801 C ASN A 111 -14.115 -12.666 -55.290 1.00 63.25 C ANISOU 801 C ASN A 111 7182 9599 7253 186 256 52 C ATOM 802 O ASN A 111 -14.306 -13.171 -54.178 1.00 78.36 O ANISOU 802 O ASN A 111 9133 11471 9171 197 211 -7 O ATOM 803 CB ASN A 111 -15.961 -11.138 -56.010 1.00 61.71 C ANISOU 803 CB ASN A 111 7118 9273 7056 192 287 96 C ATOM 804 CG ASN A 111 -16.920 -11.819 -55.053 1.00 73.77 C ANISOU 804 CG ASN A 111 8695 10758 8575 237 258 11 C ATOM 805 OD1 ASN A 111 -17.217 -13.005 -55.194 1.00 71.74 O ANISOU 805 OD1 ASN A 111 8423 10555 8282 292 261 -31 O ATOM 806 ND2 ASN A 111 -17.408 -11.070 -54.072 1.00 75.10 N ANISOU 806 ND2 ASN A 111 8935 10827 8774 210 236 -16 N ATOM 807 N LEU A 112 -13.571 -13.350 -56.299 1.00 72.69 N ANISOU 807 N LEU A 112 8302 10904 8412 239 297 72 N ATOM 808 CA LEU A 112 -13.164 -14.740 -56.118 1.00 78.46 C ANISOU 808 CA LEU A 112 8999 11696 9116 324 286 21 C ATOM 809 C LEU A 112 -12.035 -14.845 -55.100 1.00 82.85 C ANISOU 809 C LEU A 112 9489 12284 9708 295 236 14 C ATOM 810 O LEU A 112 -12.146 -15.563 -54.100 1.00 74.06 O ANISOU 810 O LEU A 112 8418 11130 8590 332 185 -35 O ATOM 811 CB LEU A 112 -12.750 -15.345 -57.463 1.00 74.12 C ANISOU 811 CB LEU A 112 8389 11260 8514 397 348 37 C ATOM 812 CG LEU A 112 -12.574 -16.867 -57.555 1.00 70.73 C ANISOU 812 CG LEU A 112 7964 10866 8043 515 349 -27 C ATOM 813 CD1 LEU A 112 -12.856 -17.345 -58.970 1.00 77.18 C ANISOU 813 CD1 LEU A 112 8790 11748 8787 584 411 -36 C ATOM 814 CD2 LEU A 112 -11.179 -17.308 -57.127 1.00 64.49 C ANISOU 814 CD2 LEU A 112 7068 10162 7271 556 336 -24 C ATOM 815 N TYR A 113 -10.936 -14.127 -55.338 1.00 94.97 N ANISOU 815 N TYR A 113 10914 13898 11271 223 247 68 N ATOM 816 CA TYR A 113 -9.795 -14.205 -54.432 1.00 85.46 C ANISOU 816 CA TYR A 113 9616 12758 10096 190 188 62 C ATOM 817 C TYR A 113 -10.137 -13.650 -53.055 1.00 75.83 C ANISOU 817 C TYR A 113 8481 11428 8905 110 109 28 C ATOM 818 O TYR A 113 -9.755 -14.232 -52.033 1.00 83.52 O ANISOU 818 O TYR A 113 9447 12416 9870 140 40 -8 O ATOM 819 CB TYR A 113 -8.599 -13.461 -55.028 1.00 83.12 C ANISOU 819 CB TYR A 113 9169 12586 9826 98 221 129 C ATOM 820 CG TYR A 113 -8.004 -14.129 -56.246 1.00 90.44 C ANISOU 820 CG TYR A 113 9987 13663 10713 192 302 155 C ATOM 821 CD1 TYR A 113 -7.012 -15.092 -56.119 1.00 95.82 C ANISOU 821 CD1 TYR A 113 10543 14482 11384 296 292 133 C ATOM 822 CD2 TYR A 113 -8.432 -13.795 -57.524 1.00 88.41 C ANISOU 822 CD2 TYR A 113 9757 13416 10420 191 390 200 C ATOM 823 CE1 TYR A 113 -6.464 -15.705 -57.229 1.00 96.13 C ANISOU 823 CE1 TYR A 113 10486 14661 11378 400 375 145 C ATOM 824 CE2 TYR A 113 -7.891 -14.402 -58.641 1.00 78.00 C ANISOU 824 CE2 TYR A 113 8348 12243 9048 280 470 216 C ATOM 825 CZ TYR A 113 -6.907 -15.356 -58.487 1.00 90.68 C ANISOU 825 CZ TYR A 113 9829 13980 10645 385 468 183 C ATOM 826 OH TYR A 113 -6.364 -15.962 -59.595 1.00106.72 O ANISOU 826 OH TYR A 113 11774 16159 12615 491 558 188 O ATOM 827 N ALA A 114 -10.865 -12.532 -53.005 1.00 59.17 N ANISOU 827 N ALA A 114 6462 9203 6816 21 118 39 N ATOM 828 CA ALA A 114 -11.168 -11.900 -51.724 1.00 57.08 C ANISOU 828 CA ALA A 114 6287 8832 6569 -54 52 -3 C ATOM 829 C ALA A 114 -12.060 -12.788 -50.864 1.00 62.48 C ANISOU 829 C ALA A 114 7070 9458 7213 35 25 -67 C ATOM 830 O ALA A 114 -11.805 -12.964 -49.667 1.00 66.41 O ANISOU 830 O ALA A 114 7594 9943 7696 18 -44 -106 O ATOM 831 CB ALA A 114 -11.821 -10.537 -51.952 1.00 52.22 C ANISOU 831 CB ALA A 114 5766 8093 5983 -139 79 19 C ATOM 832 N SER A 115 -13.114 -13.355 -51.456 1.00 57.47 N ANISOU 832 N SER A 115 6493 8793 6552 119 77 -76 N ATOM 833 CA SER A 115 -14.012 -14.214 -50.690 1.00 63.88 C ANISOU 833 CA SER A 115 7396 9552 7324 180 63 -130 C ATOM 834 C SER A 115 -13.300 -15.473 -50.212 1.00 70.16 C ANISOU 834 C SER A 115 8164 10404 8090 247 23 -143 C ATOM 835 O SER A 115 -13.534 -15.939 -49.091 1.00 73.80 O ANISOU 835 O SER A 115 8698 10823 8519 257 -19 -175 O ATOM 836 CB SER A 115 -15.235 -14.581 -51.528 1.00 53.55 C ANISOU 836 CB SER A 115 6131 8220 5995 236 123 -138 C ATOM 837 OG SER A 115 -15.920 -13.424 -51.973 1.00 74.56 O ANISOU 837 OG SER A 115 8819 10832 8678 202 152 -118 O ATOM 838 N VAL A 116 -12.427 -16.034 -51.047 1.00 67.28 N ANISOU 838 N VAL A 116 7700 10135 7727 304 39 -115 N ATOM 839 CA VAL A 116 -11.732 -17.260 -50.676 1.00 56.36 C ANISOU 839 CA VAL A 116 6297 8801 6316 401 2 -125 C ATOM 840 C VAL A 116 -10.613 -16.977 -49.674 1.00 67.86 C ANISOU 840 C VAL A 116 7683 10318 7783 368 -82 -116 C ATOM 841 O VAL A 116 -10.339 -17.804 -48.796 1.00 71.94 O ANISOU 841 O VAL A 116 8236 10834 8265 435 -142 -128 O ATOM 842 CB VAL A 116 -11.218 -17.965 -51.944 1.00 48.40 C ANISOU 842 CB VAL A 116 5210 7879 5301 497 56 -110 C ATOM 843 CG1 VAL A 116 -10.376 -19.159 -51.590 1.00 61.58 C ANISOU 843 CG1 VAL A 116 6856 9596 6947 622 18 -119 C ATOM 844 CG2 VAL A 116 -12.390 -18.405 -52.806 1.00 49.73 C ANISOU 844 CG2 VAL A 116 5467 7986 5442 528 119 -134 C ATOM 845 N PHE A 117 -9.964 -15.812 -49.767 1.00 65.88 N ANISOU 845 N PHE A 117 7339 10119 7574 258 -95 -92 N ATOM 846 CA PHE A 117 -8.966 -15.449 -48.765 1.00 64.34 C ANISOU 846 CA PHE A 117 7074 9988 7385 198 -189 -95 C ATOM 847 C PHE A 117 -9.615 -15.185 -47.411 1.00 68.24 C ANISOU 847 C PHE A 117 7707 10376 7844 147 -251 -139 C ATOM 848 O PHE A 117 -9.073 -15.574 -46.370 1.00 68.22 O ANISOU 848 O PHE A 117 7704 10413 7805 168 -340 -152 O ATOM 849 CB PHE A 117 -8.173 -14.222 -49.217 1.00 63.96 C ANISOU 849 CB PHE A 117 6902 10008 7390 58 -184 -62 C ATOM 850 CG PHE A 117 -7.278 -14.472 -50.398 1.00 69.55 C ANISOU 850 CG PHE A 117 7442 10864 8120 98 -126 -14 C ATOM 851 CD1 PHE A 117 -6.927 -15.761 -50.763 1.00 75.41 C ANISOU 851 CD1 PHE A 117 8130 11690 8831 268 -110 -14 C ATOM 852 CD2 PHE A 117 -6.786 -13.412 -51.143 1.00 56.36 C ANISOU 852 CD2 PHE A 117 5678 9244 6493 -33 -81 33 C ATOM 853 CE1 PHE A 117 -6.103 -15.988 -51.851 1.00 71.67 C ANISOU 853 CE1 PHE A 117 7502 11365 8367 320 -46 22 C ATOM 854 CE2 PHE A 117 -5.963 -13.632 -52.230 1.00 58.62 C ANISOU 854 CE2 PHE A 117 5804 9684 6785 0 -13 81 C ATOM 855 CZ PHE A 117 -5.621 -14.922 -52.584 1.00 62.14 C ANISOU 855 CZ PHE A 117 6185 10229 7195 183 7 70 C ATOM 856 N LEU A 118 -10.774 -14.520 -47.407 1.00 64.04 N ANISOU 856 N LEU A 118 7296 9721 7317 93 -204 -162 N ATOM 857 CA LEU A 118 -11.459 -14.229 -46.151 1.00 56.09 C ANISOU 857 CA LEU A 118 6423 8621 6268 53 -243 -211 C ATOM 858 C LEU A 118 -11.899 -15.509 -45.452 1.00 56.29 C ANISOU 858 C LEU A 118 6535 8629 6225 154 -257 -224 C ATOM 859 O LEU A 118 -11.793 -15.623 -44.226 1.00 65.01 O ANISOU 859 O LEU A 118 7705 9724 7271 142 -326 -248 O ATOM 860 CB LEU A 118 -12.657 -13.314 -46.406 1.00 43.12 C ANISOU 860 CB LEU A 118 4877 6863 4645 7 -175 -233 C ATOM 861 CG LEU A 118 -12.335 -11.848 -46.705 1.00 56.52 C ANISOU 861 CG LEU A 118 6556 8523 6398 -112 -175 -226 C ATOM 862 CD1 LEU A 118 -13.557 -11.126 -47.249 1.00 59.63 C ANISOU 862 CD1 LEU A 118 7039 8808 6812 -104 -98 -230 C ATOM 863 CD2 LEU A 118 -11.815 -11.151 -45.459 1.00 58.90 C ANISOU 863 CD2 LEU A 118 6900 8801 6680 -212 -263 -275 C ATOM 864 N LEU A 119 -12.396 -16.485 -46.216 1.00 49.96 N ANISOU 864 N LEU A 119 5748 7817 5420 246 -195 -207 N ATOM 865 CA LEU A 119 -12.752 -17.772 -45.627 1.00 52.21 C ANISOU 865 CA LEU A 119 6128 8067 5642 330 -206 -210 C ATOM 866 C LEU A 119 -11.525 -18.503 -45.101 1.00 54.27 C ANISOU 866 C LEU A 119 6340 8406 5874 406 -293 -184 C ATOM 867 O LEU A 119 -11.631 -19.284 -44.148 1.00 70.69 O ANISOU 867 O LEU A 119 8521 10451 7886 455 -336 -179 O ATOM 868 CB LEU A 119 -13.479 -18.641 -46.651 1.00 52.17 C ANISOU 868 CB LEU A 119 6152 8027 5644 395 -126 -206 C ATOM 869 CG LEU A 119 -14.846 -18.152 -47.125 1.00 59.82 C ANISOU 869 CG LEU A 119 7169 8934 6626 341 -47 -230 C ATOM 870 CD1 LEU A 119 -15.416 -19.116 -48.148 1.00 50.68 C ANISOU 870 CD1 LEU A 119 6029 7762 5465 397 11 -233 C ATOM 871 CD2 LEU A 119 -15.791 -17.990 -45.948 1.00 69.57 C ANISOU 871 CD2 LEU A 119 8517 10102 7813 291 -45 -260 C ATOM 872 N THR A 120 -10.361 -18.268 -45.708 1.00 52.78 N ANISOU 872 N THR A 120 5992 8331 5731 423 -319 -161 N ATOM 873 CA THR A 120 -9.135 -18.903 -45.238 1.00 60.63 C ANISOU 873 CA THR A 120 6906 9429 6702 512 -409 -136 C ATOM 874 C THR A 120 -8.714 -18.342 -43.886 1.00 55.76 C ANISOU 874 C THR A 120 6301 8844 6042 438 -519 -149 C ATOM 875 O THR A 120 -8.411 -19.097 -42.955 1.00 50.01 O ANISOU 875 O THR A 120 5629 8129 5245 518 -599 -135 O ATOM 876 CB THR A 120 -8.022 -18.716 -46.268 1.00 59.82 C ANISOU 876 CB THR A 120 6602 9469 6659 539 -396 -111 C ATOM 877 OG1 THR A 120 -8.454 -19.226 -47.536 1.00 54.84 O ANISOU 877 OG1 THR A 120 5977 8811 6049 609 -292 -107 O ATOM 878 CG2 THR A 120 -6.768 -19.453 -45.832 1.00 64.13 C ANISOU 878 CG2 THR A 120 7041 10145 7181 662 -487 -86 C ATOM 879 N CYS A 121 -8.688 -17.013 -43.759 1.00 58.42 N ANISOU 879 N CYS A 121 6601 9186 6412 286 -530 -177 N ATOM 880 CA CYS A 121 -8.332 -16.401 -42.484 1.00 63.84 C ANISOU 880 CA CYS A 121 7314 9894 7047 199 -637 -208 C ATOM 881 C CYS A 121 -9.405 -16.642 -41.430 1.00 65.62 C ANISOU 881 C CYS A 121 7745 10002 7185 202 -634 -238 C ATOM 882 O CYS A 121 -9.084 -16.794 -40.245 1.00 66.32 O ANISOU 882 O CYS A 121 7887 10120 7189 205 -732 -249 O ATOM 883 CB CYS A 121 -8.092 -14.904 -42.671 1.00 55.52 C ANISOU 883 CB CYS A 121 6198 8844 6053 25 -641 -239 C ATOM 884 SG CYS A 121 -6.779 -14.506 -43.848 1.00 66.66 S ANISOU 884 SG CYS A 121 7357 10412 7558 -21 -635 -194 S ATOM 885 N LEU A 122 -10.676 -16.679 -41.836 1.00 64.32 N ANISOU 885 N LEU A 122 7689 9720 7031 202 -522 -251 N ATOM 886 CA LEU A 122 -11.742 -17.000 -40.894 1.00 63.38 C ANISOU 886 CA LEU A 122 7746 9508 6826 206 -498 -273 C ATOM 887 C LEU A 122 -11.625 -18.433 -40.393 1.00 67.58 C ANISOU 887 C LEU A 122 8351 10043 7282 323 -530 -227 C ATOM 888 O LEU A 122 -11.959 -18.714 -39.236 1.00 65.57 O ANISOU 888 O LEU A 122 8227 9759 6926 321 -562 -231 O ATOM 889 CB LEU A 122 -13.107 -16.765 -41.544 1.00 54.39 C ANISOU 889 CB LEU A 122 6671 8273 5723 184 -371 -294 C ATOM 890 CG LEU A 122 -14.360 -16.873 -40.671 1.00 60.64 C ANISOU 890 CG LEU A 122 7617 8987 6436 165 -319 -325 C ATOM 891 CD1 LEU A 122 -15.352 -15.782 -41.039 1.00 64.43 C ANISOU 891 CD1 LEU A 122 8111 9410 6960 106 -236 -373 C ATOM 892 CD2 LEU A 122 -15.004 -18.242 -40.815 1.00 60.58 C ANISOU 892 CD2 LEU A 122 7681 8943 6395 235 -263 -287 C ATOM 893 N SER A 123 -11.153 -19.348 -41.244 1.00 69.01 N ANISOU 893 N SER A 123 8465 10252 7505 430 -518 -182 N ATOM 894 CA SER A 123 -10.921 -20.719 -40.801 1.00 68.25 C ANISOU 894 CA SER A 123 8452 10138 7341 558 -557 -133 C ATOM 895 C SER A 123 -9.723 -20.796 -39.864 1.00 74.93 C ANISOU 895 C SER A 123 9250 11091 8127 608 -700 -109 C ATOM 896 O SER A 123 -9.749 -21.538 -38.875 1.00 80.64 O ANISOU 896 O SER A 123 10104 11787 8750 669 -756 -75 O ATOM 897 CB SER A 123 -10.715 -21.634 -42.008 1.00 56.57 C ANISOU 897 CB SER A 123 6924 8649 5920 672 -504 -106 C ATOM 898 OG SER A 123 -9.530 -21.298 -42.708 1.00 65.33 O ANISOU 898 OG SER A 123 7838 9889 7095 712 -542 -100 O ATOM 899 N ILE A 124 -8.662 -20.044 -40.163 1.00 71.74 N ANISOU 899 N ILE A 124 8659 10819 7780 576 -764 -122 N ATOM 900 CA ILE A 124 -7.504 -20.001 -39.275 1.00 56.88 C ANISOU 900 CA ILE A 124 6699 9069 5842 605 -915 -108 C ATOM 901 C ILE A 124 -7.887 -19.393 -37.933 1.00 63.39 C ANISOU 901 C ILE A 124 7650 9869 6565 499 -978 -146 C ATOM 902 O ILE A 124 -7.451 -19.862 -36.874 1.00 61.53 O ANISOU 902 O ILE A 124 7473 9684 6223 559 -1090 -120 O ATOM 903 CB ILE A 124 -6.349 -19.229 -39.941 1.00 60.70 C ANISOU 903 CB ILE A 124 6935 9712 6415 556 -958 -119 C ATOM 904 CG1 ILE A 124 -5.836 -19.990 -41.165 1.00 63.12 C ANISOU 904 CG1 ILE A 124 7115 10074 6795 696 -900 -78 C ATOM 905 CG2 ILE A 124 -5.221 -18.978 -38.949 1.00 55.41 C ANISOU 905 CG2 ILE A 124 6167 9201 5687 543 -1126 -119 C ATOM 906 CD1 ILE A 124 -4.703 -19.296 -41.885 1.00 61.59 C ANISOU 906 CD1 ILE A 124 6662 10056 6683 646 -921 -79 C ATOM 907 N ASP A 125 -8.714 -18.345 -37.955 1.00 66.05 N ANISOU 907 N ASP A 125 8041 10130 6926 353 -907 -208 N ATOM 908 CA ASP A 125 -9.161 -17.730 -36.709 1.00 57.20 C ANISOU 908 CA ASP A 125 7056 8976 5701 259 -949 -260 C ATOM 909 C ASP A 125 -9.990 -18.704 -35.883 1.00 63.02 C ANISOU 909 C ASP A 125 7995 9633 6318 332 -918 -226 C ATOM 910 O ASP A 125 -9.925 -18.694 -34.649 1.00 65.30 O ANISOU 910 O ASP A 125 8389 9946 6475 319 -998 -235 O ATOM 911 CB ASP A 125 -9.961 -16.462 -37.010 1.00 59.95 C ANISOU 911 CB ASP A 125 7432 9240 6106 119 -860 -335 C ATOM 912 CG ASP A 125 -10.378 -15.723 -35.754 1.00 74.20 C ANISOU 912 CG ASP A 125 9378 11013 7803 30 -897 -408 C ATOM 913 OD1 ASP A 125 -9.533 -15.014 -35.171 1.00 86.92 O ANISOU 913 OD1 ASP A 125 10942 12699 9383 -52 -1017 -452 O ATOM 914 OD2 ASP A 125 -11.552 -15.855 -35.347 1.00 81.97 O ANISOU 914 OD2 ASP A 125 10515 11904 8725 36 -805 -426 O ATOM 915 N ARG A 126 -10.773 -19.558 -36.549 1.00 68.52 N ANISOU 915 N ARG A 126 8752 10234 7047 398 -804 -186 N ATOM 916 CA ARG A 126 -11.569 -20.543 -35.826 1.00 61.33 C ANISOU 916 CA ARG A 126 8036 9239 6027 446 -764 -143 C ATOM 917 C ARG A 126 -10.699 -21.634 -35.219 1.00 58.24 C ANISOU 917 C ARG A 126 7688 8891 5550 581 -878 -62 C ATOM 918 O ARG A 126 -11.028 -22.162 -34.151 1.00 66.94 O ANISOU 918 O ARG A 126 8961 9959 6516 599 -901 -25 O ATOM 919 CB ARG A 126 -12.626 -21.149 -36.751 1.00 53.47 C ANISOU 919 CB ARG A 126 7088 8132 5097 455 -617 -127 C ATOM 920 CG ARG A 126 -13.858 -20.272 -36.960 1.00 67.97 C ANISOU 920 CG ARG A 126 8946 9915 6965 339 -498 -194 C ATOM 921 CD ARG A 126 -14.527 -19.920 -35.634 1.00 68.66 C ANISOU 921 CD ARG A 126 9176 9990 6922 273 -487 -225 C ATOM 922 NE ARG A 126 -13.999 -18.684 -35.061 1.00 61.71 N ANISOU 922 NE ARG A 126 8255 9173 6020 209 -566 -293 N ATOM 923 CZ ARG A 126 -14.095 -18.349 -33.779 1.00 54.86 C ANISOU 923 CZ ARG A 126 7501 8327 5017 170 -608 -326 C ATOM 924 NH1 ARG A 126 -14.698 -19.162 -32.921 1.00 65.78 N ANISOU 924 NH1 ARG A 126 9042 9684 6269 192 -572 -284 N ATOM 925 NH2 ARG A 126 -13.581 -17.204 -33.352 1.00 55.75 N ANISOU 925 NH2 ARG A 126 7580 8485 5117 101 -685 -403 N ATOM 926 N TYR A 127 -9.591 -21.986 -35.874 1.00 62.36 N ANISOU 926 N TYR A 127 8059 9493 6142 687 -949 -30 N ATOM 927 CA TYR A 127 -8.676 -22.960 -35.288 1.00 62.42 C ANISOU 927 CA TYR A 127 8092 9556 6069 844 -1072 47 C ATOM 928 C TYR A 127 -8.000 -22.401 -34.043 1.00 58.42 C ANISOU 928 C TYR A 127 7575 9174 5448 810 -1225 34 C ATOM 929 O TYR A 127 -7.896 -23.092 -33.023 1.00 58.78 O ANISOU 929 O TYR A 127 7764 9217 5354 890 -1303 95 O ATOM 930 CB TYR A 127 -7.631 -23.392 -36.315 1.00 53.22 C ANISOU 930 CB TYR A 127 6740 8471 5008 981 -1104 74 C ATOM 931 CG TYR A 127 -6.437 -24.081 -35.697 1.00 56.58 C ANISOU 931 CG TYR A 127 7125 9012 5363 1152 -1262 139 C ATOM 932 CD1 TYR A 127 -6.566 -25.324 -35.092 1.00 58.07 C ANISOU 932 CD1 TYR A 127 7510 9105 5448 1301 -1291 225 C ATOM 933 CD2 TYR A 127 -5.181 -23.489 -35.715 1.00 68.82 C ANISOU 933 CD2 TYR A 127 8437 10767 6945 1165 -1385 121 C ATOM 934 CE1 TYR A 127 -5.479 -25.957 -34.520 1.00 63.67 C ANISOU 934 CE1 TYR A 127 8187 9919 6086 1484 -1445 293 C ATOM 935 CE2 TYR A 127 -4.087 -24.116 -35.149 1.00 63.58 C ANISOU 935 CE2 TYR A 127 7712 10234 6213 1336 -1539 181 C ATOM 936 CZ TYR A 127 -4.242 -25.350 -34.554 1.00 64.23 C ANISOU 936 CZ TYR A 127 7998 10216 6191 1509 -1572 269 C ATOM 937 OH TYR A 127 -3.157 -25.979 -33.987 1.00 80.15 O ANISOU 937 OH TYR A 127 9958 12361 8133 1706 -1733 337 O ATOM 938 N LEU A 128 -7.538 -21.150 -34.104 1.00 54.69 N ANISOU 938 N LEU A 128 6947 8807 5024 685 -1273 -43 N ATOM 939 CA LEU A 128 -6.847 -20.563 -32.961 1.00 55.99 C ANISOU 939 CA LEU A 128 7095 9099 5079 632 -1432 -73 C ATOM 940 C LEU A 128 -7.804 -20.310 -31.802 1.00 56.09 C ANISOU 940 C LEU A 128 7335 9032 4943 546 -1407 -104 C ATOM 941 O LEU A 128 -7.438 -20.503 -30.638 1.00 64.90 O ANISOU 941 O LEU A 128 8539 10219 5904 576 -1531 -85 O ATOM 942 CB LEU A 128 -6.152 -19.266 -33.373 1.00 69.66 C ANISOU 942 CB LEU A 128 8617 10942 6908 490 -1481 -155 C ATOM 943 CG LEU A 128 -5.078 -19.379 -34.457 1.00 56.40 C ANISOU 943 CG LEU A 128 6680 9386 5362 554 -1508 -127 C ATOM 944 CD1 LEU A 128 -4.444 -18.023 -34.729 1.00 56.81 C ANISOU 944 CD1 LEU A 128 6548 9541 5494 371 -1553 -203 C ATOM 945 CD2 LEU A 128 -4.024 -20.401 -34.062 1.00 58.26 C ANISOU 945 CD2 LEU A 128 6843 9759 5534 747 -1648 -48 C ATOM 946 N ALA A 129 -9.032 -19.882 -32.097 1.00 73.83 N ANISOU 946 N ALA A 129 9677 11148 7228 448 -1248 -153 N ATOM 947 CA ALA A 129 -9.972 -19.560 -31.028 1.00 54.74 C ANISOU 947 CA ALA A 129 7457 8672 4669 369 -1204 -194 C ATOM 948 C ALA A 129 -10.442 -20.811 -30.298 1.00 73.96 C ANISOU 948 C ALA A 129 10091 11050 6962 466 -1184 -97 C ATOM 949 O ALA A 129 -10.655 -20.782 -29.080 1.00 75.45 O ANISOU 949 O ALA A 129 10433 11260 6976 443 -1225 -99 O ATOM 950 CB ALA A 129 -11.167 -18.794 -31.594 1.00 53.08 C ANISOU 950 CB ALA A 129 7273 8353 4542 261 -1034 -268 C ATOM 951 N ILE A 130 -10.611 -21.917 -31.019 1.00 60.30 N ANISOU 951 N ILE A 130 8375 9239 5296 569 -1118 -11 N ATOM 952 CA ILE A 130 -11.166 -23.117 -30.404 1.00 59.03 C ANISOU 952 CA ILE A 130 8429 8987 5011 639 -1079 88 C ATOM 953 C ILE A 130 -10.079 -23.939 -29.726 1.00 59.97 C ANISOU 953 C ILE A 130 8587 9177 5023 792 -1248 183 C ATOM 954 O ILE A 130 -10.278 -24.457 -28.623 1.00 63.38 O ANISOU 954 O ILE A 130 9212 9594 5276 818 -1282 248 O ATOM 955 CB ILE A 130 -11.928 -23.941 -31.457 1.00 55.78 C ANISOU 955 CB ILE A 130 8048 8435 4712 663 -930 129 C ATOM 956 CG1 ILE A 130 -13.128 -23.153 -31.983 1.00 63.15 C ANISOU 956 CG1 ILE A 130 8955 9314 5723 519 -769 42 C ATOM 957 CG2 ILE A 130 -12.379 -25.270 -30.871 1.00 57.22 C ANISOU 957 CG2 ILE A 130 8460 8505 4774 727 -898 242 C ATOM 958 CD1 ILE A 130 -13.798 -23.798 -33.172 1.00 69.30 C ANISOU 958 CD1 ILE A 130 9719 9984 6626 526 -642 61 C ATOM 959 N VAL A 131 -8.917 -24.064 -30.359 1.00 68.36 N ANISOU 959 N VAL A 131 9463 10329 6181 902 -1354 198 N ATOM 960 CA VAL A 131 -7.873 -24.951 -29.857 1.00 73.59 C ANISOU 960 CA VAL A 131 10142 11062 6758 1087 -1514 297 C ATOM 961 C VAL A 131 -6.932 -24.230 -28.898 1.00 79.41 C ANISOU 961 C VAL A 131 10792 11995 7386 1069 -1704 263 C ATOM 962 O VAL A 131 -6.520 -24.797 -27.884 1.00 67.24 O ANISOU 962 O VAL A 131 9366 10503 5678 1171 -1831 340 O ATOM 963 CB VAL A 131 -7.108 -25.574 -31.041 1.00 59.82 C ANISOU 963 CB VAL A 131 8236 9326 5165 1244 -1524 331 C ATOM 964 CG1 VAL A 131 -6.039 -26.529 -30.539 1.00 62.14 C ANISOU 964 CG1 VAL A 131 8545 9694 5372 1471 -1687 436 C ATOM 965 CG2 VAL A 131 -8.072 -26.292 -31.972 1.00 58.34 C ANISOU 965 CG2 VAL A 131 8154 8941 5070 1248 -1343 352 C ATOM 966 N HIS A 132 -6.570 -22.980 -29.189 1.00 86.14 N ANISOU 966 N HIS A 132 11201 12166 9364 352 -1440 1582 N ATOM 967 CA HIS A 132 -5.663 -22.200 -28.350 1.00 64.65 C ANISOU 967 CA HIS A 132 8483 9694 6388 171 -1721 1705 C ATOM 968 C HIS A 132 -6.341 -20.894 -27.947 1.00 70.72 C ANISOU 968 C HIS A 132 9558 10417 6895 -82 -1752 1532 C ATOM 969 O HIS A 132 -5.948 -19.811 -28.403 1.00 63.21 O ANISOU 969 O HIS A 132 8579 9574 5864 -278 -1854 1425 O ATOM 970 CB HIS A 132 -4.345 -21.923 -29.072 1.00 65.63 C ANISOU 970 CB HIS A 132 8266 10077 6593 135 -1875 1773 C ATOM 971 CG HIS A 132 -3.667 -23.154 -29.588 1.00 93.16 C ANISOU 971 CG HIS A 132 11450 13600 10345 418 -1806 1934 C ATOM 972 ND1 HIS A 132 -2.937 -23.165 -30.757 1.00 94.70 N ANISOU 972 ND1 HIS A 132 11343 13910 10730 482 -1776 1911 N ATOM 973 CD2 HIS A 132 -3.604 -24.414 -29.094 1.00 91.39 C ANISOU 973 CD2 HIS A 132 11199 13300 10223 667 -1745 2127 C ATOM 974 CE1 HIS A 132 -2.457 -24.379 -30.963 1.00 96.21 C ANISOU 974 CE1 HIS A 132 11339 14088 11127 772 -1689 2074 C ATOM 975 NE2 HIS A 132 -2.847 -25.155 -29.968 1.00 96.15 N ANISOU 975 NE2 HIS A 132 11499 13958 11076 889 -1670 2210 N ATOM 976 N PRO A 133 -7.362 -20.958 -27.085 1.00 68.90 N ANISOU 976 N PRO A 133 9635 10018 6524 -76 -1652 1507 N ATOM 977 CA PRO A 133 -8.085 -19.722 -26.741 1.00 66.40 C ANISOU 977 CA PRO A 133 9636 9629 5965 -275 -1634 1335 C ATOM 978 C PRO A 133 -7.245 -18.741 -25.946 1.00 70.63 C ANISOU 978 C PRO A 133 10292 10355 6189 -525 -1909 1385 C ATOM 979 O PRO A 133 -7.359 -17.526 -26.151 1.00 64.21 O ANISOU 979 O PRO A 133 9638 9528 5231 -725 -1939 1222 O ATOM 980 CB PRO A 133 -9.288 -20.230 -25.928 1.00 65.91 C ANISOU 980 CB PRO A 133 9838 9367 5837 -170 -1448 1347 C ATOM 981 CG PRO A 133 -9.338 -21.716 -26.162 1.00 70.62 C ANISOU 981 CG PRO A 133 10241 9888 6702 70 -1333 1477 C ATOM 982 CD PRO A 133 -7.924 -22.130 -26.397 1.00 64.38 C ANISOU 982 CD PRO A 133 9150 9306 6005 115 -1529 1639 C ATOM 983 N MET A 134 -6.396 -19.235 -25.045 1.00 67.50 N ANISOU 983 N MET A 134 9832 10136 5679 -527 -2116 1613 N ATOM 984 CA MET A 134 -5.624 -18.367 -24.165 1.00 73.42 C ANISOU 984 CA MET A 134 10717 11082 6096 -796 -2403 1673 C ATOM 985 C MET A 134 -4.317 -17.898 -24.793 1.00 77.59 C ANISOU 985 C MET A 134 10935 11875 6672 -955 -2633 1725 C ATOM 986 O MET A 134 -3.895 -16.760 -24.560 1.00 81.57 O ANISOU 986 O MET A 134 11578 12479 6938 -1256 -2816 1655 O ATOM 987 CB MET A 134 -5.334 -19.087 -22.844 1.00 89.25 C ANISOU 987 CB MET A 134 12800 13188 7921 -743 -2540 1915 C ATOM 988 CG MET A 134 -6.559 -19.295 -21.971 1.00 89.31 C ANISOU 988 CG MET A 134 13183 12969 7781 -663 -2350 1874 C ATOM 989 SD MET A 134 -7.236 -17.741 -21.359 1.00 94.89 S ANISOU 989 SD MET A 134 14393 13564 8096 -942 -2343 1640 S ATOM 990 CE MET A 134 -8.646 -18.330 -20.428 1.00 91.50 C ANISOU 990 CE MET A 134 14300 12898 7569 -755 -2069 1653 C ATOM 991 N LYS A 135 -3.663 -18.749 -25.585 1.00 81.42 N ANISOU 991 N LYS A 135 11012 12470 7454 -763 -2617 1848 N ATOM 992 CA LYS A 135 -2.365 -18.399 -26.148 1.00 80.68 C ANISOU 992 CA LYS A 135 10576 12665 7414 -890 -2825 1939 C ATOM 993 C LYS A 135 -2.467 -17.543 -27.404 1.00 70.06 C ANISOU 993 C LYS A 135 9169 11263 6188 -1000 -2727 1718 C ATOM 994 O LYS A 135 -1.497 -16.860 -27.748 1.00 99.36 O ANISOU 994 O LYS A 135 12694 15201 9859 -1210 -2915 1753 O ATOM 995 CB LYS A 135 -1.565 -19.667 -26.458 1.00 77.10 C ANISOU 995 CB LYS A 135 9709 12365 7221 -606 -2830 2185 C ATOM 996 CG LYS A 135 -1.201 -20.490 -25.233 1.00 89.82 C ANISOU 996 CG LYS A 135 11322 14095 8711 -500 -2973 2463 C ATOM 997 CD LYS A 135 -0.317 -21.670 -25.603 1.00103.75 C ANISOU 997 CD LYS A 135 12665 16016 10738 -200 -2972 2723 C ATOM 998 CE LYS A 135 -1.022 -22.607 -26.569 1.00104.64 C ANISOU 998 CE LYS A 135 12727 15841 11189 119 -2629 2618 C ATOM 999 NZ LYS A 135 -2.270 -23.168 -25.982 1.00 99.00 N ANISOU 999 NZ LYS A 135 12355 14813 10449 234 -2436 2550 N ATOM 1000 N SER A 136 -3.607 -17.561 -28.093 1.00 74.81 N ANISOU 1000 N SER A 136 9910 11586 6930 -875 -2445 1508 N ATOM 1001 CA SER A 136 -3.782 -16.807 -29.328 1.00 69.17 C ANISOU 1001 CA SER A 136 9139 10811 6332 -951 -2336 1310 C ATOM 1002 C SER A 136 -4.720 -15.619 -29.165 1.00 68.86 C ANISOU 1002 C SER A 136 9501 10574 6090 -1136 -2262 1088 C ATOM 1003 O SER A 136 -5.063 -14.972 -30.160 1.00 84.90 O ANISOU 1003 O SER A 136 11533 12517 8207 -1177 -2142 920 O ATOM 1004 CB SER A 136 -4.294 -17.726 -30.440 1.00 72.92 C ANISOU 1004 CB SER A 136 9422 11148 7138 -663 -2073 1246 C ATOM 1005 OG SER A 136 -5.581 -18.231 -30.131 1.00 61.03 O ANISOU 1005 OG SER A 136 8154 9381 5655 -512 -1862 1164 O ATOM 1006 N ARG A 137 -5.144 -15.313 -27.937 1.00 69.13 N ANISOU 1006 N ARG A 137 9884 10534 5847 -1234 -2320 1093 N ATOM 1007 CA ARG A 137 -6.079 -14.212 -27.733 1.00 63.90 C ANISOU 1007 CA ARG A 137 9632 9661 4985 -1367 -2214 889 C ATOM 1008 C ARG A 137 -5.412 -12.863 -27.973 1.00 64.92 C ANISOU 1008 C ARG A 137 9848 9869 4949 -1690 -2381 805 C ATOM 1009 O ARG A 137 -5.996 -11.982 -28.616 1.00 63.39 O ANISOU 1009 O ARG A 137 9817 9514 4755 -1745 -2242 623 O ATOM 1010 CB ARG A 137 -6.670 -14.286 -26.323 1.00 65.29 C ANISOU 1010 CB ARG A 137 10175 9741 4893 -1371 -2214 923 C ATOM 1011 CG ARG A 137 -7.511 -13.082 -25.907 1.00 79.46 C ANISOU 1011 CG ARG A 137 12439 11330 6422 -1512 -2118 734 C ATOM 1012 CD ARG A 137 -8.593 -12.754 -26.927 1.00 97.05 C ANISOU 1012 CD ARG A 137 14699 13345 8829 -1373 -1828 553 C ATOM 1013 NE ARG A 137 -9.382 -13.923 -27.302 1.00103.03 N ANISOU 1013 NE ARG A 137 15269 14026 9853 -1076 -1611 589 N ATOM 1014 CZ ARG A 137 -10.292 -13.925 -28.270 1.00 85.59 C ANISOU 1014 CZ ARG A 137 12995 11680 7844 -932 -1375 470 C ATOM 1015 NH1 ARG A 137 -10.964 -15.034 -28.547 1.00 90.08 N ANISOU 1015 NH1 ARG A 137 13403 12187 8637 -705 -1203 508 N ATOM 1016 NH2 ARG A 137 -10.528 -12.820 -28.963 1.00 71.29 N ANISOU 1016 NH2 ARG A 137 11286 9797 6004 -1027 -1315 319 N ATOM 1017 N LEU A 138 -4.189 -12.682 -27.474 1.00 85.37 N ANISOU 1017 N LEU A 138 12328 12713 7397 -1913 -2680 948 N ATOM 1018 CA LEU A 138 -3.525 -11.390 -27.597 1.00 97.94 C ANISOU 1018 CA LEU A 138 14028 14378 8806 -2273 -2860 878 C ATOM 1019 C LEU A 138 -3.020 -11.127 -29.009 1.00100.58 C ANISOU 1019 C LEU A 138 14030 14799 9386 -2294 -2825 844 C ATOM 1020 O LEU A 138 -2.804 -9.964 -29.369 1.00104.77 O ANISOU 1020 O LEU A 138 14701 15298 9809 -2558 -2878 735 O ATOM 1021 CB LEU A 138 -2.375 -11.303 -26.596 1.00 90.74 C ANISOU 1021 CB LEU A 138 13082 13742 7652 -2539 -3212 1057 C ATOM 1022 CG LEU A 138 -2.826 -11.487 -25.147 1.00 87.32 C ANISOU 1022 CG LEU A 138 13014 13238 6926 -2548 -3264 1091 C ATOM 1023 CD1 LEU A 138 -1.643 -11.417 -24.205 1.00 83.73 C ANISOU 1023 CD1 LEU A 138 12469 13054 6292 -2783 -3582 1263 C ATOM 1024 CD2 LEU A 138 -3.876 -10.449 -24.780 1.00 74.12 C ANISOU 1024 CD2 LEU A 138 11904 11247 5012 -2650 -3105 850 C ATOM 1025 N ARG A 139 -2.831 -12.173 -29.813 1.00 89.80 N ANISOU 1025 N ARG A 139 12255 13528 8337 -2024 -2726 935 N ATOM 1026 CA ARG A 139 -2.440 -12.012 -31.206 1.00 85.70 C ANISOU 1026 CA ARG A 139 11429 13080 8052 -2003 -2653 897 C ATOM 1027 C ARG A 139 -3.625 -11.755 -32.127 1.00 90.63 C ANISOU 1027 C ARG A 139 12196 13433 8805 -1852 -2359 684 C ATOM 1028 O ARG A 139 -3.438 -11.199 -33.215 1.00 94.14 O ANISOU 1028 O ARG A 139 12520 13895 9354 -1914 -2304 608 O ATOM 1029 CB ARG A 139 -1.686 -13.256 -31.686 1.00 91.08 C ANISOU 1029 CB ARG A 139 11627 13978 9001 -1765 -2660 1084 C ATOM 1030 CG ARG A 139 -0.462 -13.597 -30.851 1.00108.85 C ANISOU 1030 CG ARG A 139 13660 16544 11153 -1872 -2951 1340 C ATOM 1031 CD ARG A 139 0.185 -14.889 -31.319 1.00123.28 C ANISOU 1031 CD ARG A 139 15031 18550 13258 -1568 -2909 1535 C ATOM 1032 NE ARG A 139 1.388 -15.207 -30.554 1.00130.90 N ANISOU 1032 NE ARG A 139 15745 19852 14138 -1648 -3189 1815 N ATOM 1033 CZ ARG A 139 2.149 -16.275 -30.772 1.00130.78 C ANISOU 1033 CZ ARG A 139 15323 20041 14328 -1392 -3193 2041 C ATOM 1034 NH1 ARG A 139 1.831 -17.131 -31.733 1.00136.93 N ANISOU 1034 NH1 ARG A 139 15936 20693 15399 -1055 -2925 1997 N ATOM 1035 NH2 ARG A 139 3.227 -16.488 -30.029 1.00117.47 N ANISOU 1035 NH2 ARG A 139 13402 18687 12545 -1471 -3463 2317 N ATOM 1036 N ARG A 140 -4.831 -12.141 -31.719 1.00 80.95 N ANISOU 1036 N ARG A 140 11211 11977 7568 -1660 -2171 603 N ATOM 1037 CA ARG A 140 -6.038 -11.961 -32.525 1.00 57.74 C ANISOU 1037 CA ARG A 140 8388 8807 4745 -1506 -1898 427 C ATOM 1038 C ARG A 140 -6.800 -10.760 -31.975 1.00 65.14 C ANISOU 1038 C ARG A 140 9787 9538 5424 -1656 -1850 288 C ATOM 1039 O ARG A 140 -7.663 -10.891 -31.106 1.00 69.56 O ANISOU 1039 O ARG A 140 10626 9946 5858 -1570 -1757 262 O ATOM 1040 CB ARG A 140 -6.890 -13.225 -32.509 1.00 56.24 C ANISOU 1040 CB ARG A 140 8124 8512 4734 -1196 -1708 445 C ATOM 1041 CG ARG A 140 -6.244 -14.424 -33.185 1.00 69.71 C ANISOU 1041 CG ARG A 140 9417 10361 6709 -1013 -1702 556 C ATOM 1042 CD ARG A 140 -6.881 -15.737 -32.740 1.00 71.45 C ANISOU 1042 CD ARG A 140 9627 10477 7043 -761 -1576 620 C ATOM 1043 NE ARG A 140 -8.340 -15.695 -32.767 1.00 80.69 N ANISOU 1043 NE ARG A 140 11030 11412 8215 -666 -1352 482 N ATOM 1044 CZ ARG A 140 -9.105 -15.582 -31.685 1.00 95.48 C ANISOU 1044 CZ ARG A 140 13204 13163 9912 -670 -1313 484 C ATOM 1045 NH1 ARG A 140 -8.548 -15.499 -30.484 1.00 97.68 N ANISOU 1045 NH1 ARG A 140 13615 13521 9980 -774 -1492 603 N ATOM 1046 NH2 ARG A 140 -10.425 -15.550 -31.804 1.00103.85 N ANISOU 1046 NH2 ARG A 140 14426 14039 10996 -572 -1095 377 N ATOM 1047 N THR A 141 -6.480 -9.580 -32.493 1.00 66.53 N ANISOU 1047 N THR A 141 10057 9702 5518 -1872 -1897 204 N ATOM 1048 CA THR A 141 -7.106 -8.333 -32.078 1.00 65.23 C ANISOU 1048 CA THR A 141 10355 9321 5110 -2017 -1840 70 C ATOM 1049 C THR A 141 -7.900 -7.741 -33.238 1.00 68.52 C ANISOU 1049 C THR A 141 10803 9582 5651 -1914 -1615 -63 C ATOM 1050 O THR A 141 -7.979 -8.310 -34.330 1.00 74.23 O ANISOU 1050 O THR A 141 11198 10374 6630 -1752 -1517 -59 O ATOM 1051 CB THR A 141 -6.055 -7.339 -31.577 1.00 79.96 C ANISOU 1051 CB THR A 141 12381 11271 6730 -2398 -2097 89 C ATOM 1052 OG1 THR A 141 -5.168 -6.997 -32.649 1.00 83.74 O ANISOU 1052 OG1 THR A 141 12565 11906 7347 -2538 -2182 116 O ATOM 1053 CG2 THR A 141 -5.253 -7.942 -30.437 1.00 90.21 C ANISOU 1053 CG2 THR A 141 13620 12763 7892 -2505 -2344 242 C ATOM 1054 N MET A 142 -8.496 -6.574 -32.986 1.00 66.32 N ANISOU 1054 N MET A 142 10942 9086 5171 -2006 -1529 -178 N ATOM 1055 CA MET A 142 -9.229 -5.875 -34.035 1.00 62.55 C ANISOU 1055 CA MET A 142 10522 8462 4782 -1915 -1325 -282 C ATOM 1056 C MET A 142 -8.285 -5.238 -35.046 1.00 73.91 C ANISOU 1056 C MET A 142 11785 10010 6288 -2118 -1433 -279 C ATOM 1057 O MET A 142 -8.613 -5.160 -36.235 1.00 76.83 O ANISOU 1057 O MET A 142 11982 10376 6834 -1999 -1297 -313 O ATOM 1058 CB MET A 142 -10.144 -4.818 -33.417 1.00 67.84 C ANISOU 1058 CB MET A 142 11710 8852 5214 -1919 -1179 -388 C ATOM 1059 CG MET A 142 -11.179 -5.385 -32.462 1.00 76.28 C ANISOU 1059 CG MET A 142 12957 9814 6213 -1699 -1032 -386 C ATOM 1060 SD MET A 142 -12.402 -6.403 -33.306 1.00 70.29 S ANISOU 1060 SD MET A 142 11882 9066 5758 -1321 -774 -373 S ATOM 1061 CE MET A 142 -13.194 -5.172 -34.337 1.00 74.51 C ANISOU 1061 CE MET A 142 12574 9430 6305 -1251 -567 -470 C ATOM 1062 N LEU A 143 -7.116 -4.779 -34.594 1.00 77.90 N ANISOU 1062 N LEU A 143 12324 10627 6645 -2437 -1679 -227 N ATOM 1063 CA LEU A 143 -6.144 -4.196 -35.513 1.00 75.17 C ANISOU 1063 CA LEU A 143 11786 10412 6363 -2657 -1788 -200 C ATOM 1064 C LEU A 143 -5.591 -5.245 -36.469 1.00 80.04 C ANISOU 1064 C LEU A 143 11854 11288 7269 -2510 -1799 -104 C ATOM 1065 O LEU A 143 -5.397 -4.967 -37.658 1.00 89.97 O ANISOU 1065 O LEU A 143 12923 12597 8665 -2510 -1733 -116 O ATOM 1066 CB LEU A 143 -5.013 -3.535 -34.725 1.00 62.22 C ANISOU 1066 CB LEU A 143 10287 8863 4492 -3061 -2068 -150 C ATOM 1067 CG LEU A 143 -3.867 -2.932 -35.538 1.00 76.51 C ANISOU 1067 CG LEU A 143 11879 10844 6349 -3348 -2213 -91 C ATOM 1068 CD1 LEU A 143 -4.378 -1.831 -36.454 1.00 74.37 C ANISOU 1068 CD1 LEU A 143 11829 10350 6080 -3376 -2036 -202 C ATOM 1069 CD2 LEU A 143 -2.778 -2.408 -34.617 1.00 67.10 C ANISOU 1069 CD2 LEU A 143 10804 9769 4923 -3764 -2511 -24 C ATOM 1070 N VAL A 144 -5.332 -6.455 -35.969 1.00 79.08 N ANISOU 1070 N VAL A 144 11492 11321 7233 -2374 -1869 -3 N ATOM 1071 CA VAL A 144 -4.847 -7.526 -36.833 1.00 64.62 C ANISOU 1071 CA VAL A 144 9178 9703 5673 -2197 -1849 84 C ATOM 1072 C VAL A 144 -5.917 -7.924 -37.844 1.00 70.41 C ANISOU 1072 C VAL A 144 9843 10313 6598 -1907 -1585 -16 C ATOM 1073 O VAL A 144 -5.615 -8.201 -39.011 1.00 75.06 O ANISOU 1073 O VAL A 144 10133 11015 7371 -1830 -1522 -9 O ATOM 1074 CB VAL A 144 -4.392 -8.729 -35.986 1.00 68.43 C ANISOU 1074 CB VAL A 144 9469 10340 6192 -2094 -1967 223 C ATOM 1075 CG1 VAL A 144 -3.907 -9.862 -36.878 1.00 56.49 C ANISOU 1075 CG1 VAL A 144 7492 9013 4959 -1879 -1914 310 C ATOM 1076 CG2 VAL A 144 -3.303 -8.308 -35.010 1.00 69.12 C ANISOU 1076 CG2 VAL A 144 9599 10592 6072 -2403 -2256 339 C ATOM 1077 N ALA A 145 -7.182 -7.944 -37.417 1.00 64.88 N ANISOU 1077 N ALA A 145 9415 9393 5844 -1751 -1426 -103 N ATOM 1078 CA ALA A 145 -8.261 -8.354 -38.311 1.00 55.24 C ANISOU 1078 CA ALA A 145 8117 8079 4792 -1495 -1194 -184 C ATOM 1079 C ALA A 145 -8.450 -7.361 -39.451 1.00 61.58 C ANISOU 1079 C ALA A 145 8953 8835 5611 -1549 -1103 -260 C ATOM 1080 O ALA A 145 -8.762 -7.756 -40.581 1.00 62.29 O ANISOU 1080 O ALA A 145 8822 8970 5873 -1401 -981 -292 O ATOM 1081 CB ALA A 145 -9.560 -8.517 -37.524 1.00 50.02 C ANISOU 1081 CB ALA A 145 7729 7221 4057 -1337 -1050 -233 C ATOM 1082 N LYS A 146 -8.267 -6.068 -39.178 1.00 51.08 N ANISOU 1082 N LYS A 146 7916 7403 4088 -1766 -1158 -289 N ATOM 1083 CA LYS A 146 -8.441 -5.062 -40.220 1.00 67.74 C ANISOU 1083 CA LYS A 146 10090 9447 6201 -1818 -1067 -344 C ATOM 1084 C LYS A 146 -7.235 -5.002 -41.150 1.00 71.04 C ANISOU 1084 C LYS A 146 10194 10081 6717 -1971 -1175 -283 C ATOM 1085 O LYS A 146 -7.393 -4.815 -42.361 1.00 65.98 O ANISOU 1085 O LYS A 146 9416 9470 6183 -1903 -1066 -308 O ATOM 1086 CB LYS A 146 -8.710 -3.695 -39.590 1.00 71.56 C ANISOU 1086 CB LYS A 146 11044 9704 6441 -1987 -1062 -397 C ATOM 1087 CG LYS A 146 -10.019 -3.630 -38.817 1.00 67.49 C ANISOU 1087 CG LYS A 146 10851 8966 5826 -1795 -898 -457 C ATOM 1088 CD LYS A 146 -10.254 -2.252 -38.224 1.00 75.22 C ANISOU 1088 CD LYS A 146 12332 9694 6554 -1942 -866 -517 C ATOM 1089 CE LYS A 146 -11.559 -2.210 -37.445 1.00 82.19 C ANISOU 1089 CE LYS A 146 13523 10369 7336 -1716 -674 -563 C ATOM 1090 NZ LYS A 146 -11.809 -0.873 -36.842 1.00 95.37 N ANISOU 1090 NZ LYS A 146 15727 11764 8747 -1829 -612 -628 N ATOM 1091 N VAL A 147 -6.025 -5.159 -40.606 1.00 76.12 N ANISOU 1091 N VAL A 147 10708 10895 7319 -2175 -1387 -188 N ATOM 1092 CA VAL A 147 -4.837 -5.209 -41.453 1.00 74.70 C ANISOU 1092 CA VAL A 147 10176 10959 7246 -2300 -1480 -102 C ATOM 1093 C VAL A 147 -4.860 -6.456 -42.328 1.00 67.24 C ANISOU 1093 C VAL A 147 8840 10164 6543 -2026 -1372 -82 C ATOM 1094 O VAL A 147 -4.416 -6.423 -43.483 1.00 75.55 O ANISOU 1094 O VAL A 147 9652 11347 7708 -2019 -1321 -66 O ATOM 1095 CB VAL A 147 -3.562 -5.137 -40.592 1.00 76.27 C ANISOU 1095 CB VAL A 147 10298 11340 7342 -2578 -1741 21 C ATOM 1096 CG1 VAL A 147 -2.323 -5.387 -41.438 1.00 72.01 C ANISOU 1096 CG1 VAL A 147 9318 11100 6940 -2661 -1821 143 C ATOM 1097 CG2 VAL A 147 -3.466 -3.782 -39.907 1.00 82.26 C ANISOU 1097 CG2 VAL A 147 11472 11940 7844 -2906 -1848 -19 C ATOM 1098 N THR A 148 -5.383 -7.569 -41.809 1.00 62.31 N ANISOU 1098 N THR A 148 8170 9512 5995 -1800 -1326 -85 N ATOM 1099 CA THR A 148 -5.530 -8.766 -42.631 1.00 65.16 C ANISOU 1099 CA THR A 148 8225 9959 6573 -1540 -1202 -90 C ATOM 1100 C THR A 148 -6.463 -8.511 -43.808 1.00 72.29 C ANISOU 1100 C THR A 148 9161 10765 7540 -1416 -1006 -207 C ATOM 1101 O THR A 148 -6.227 -9.003 -44.917 1.00 80.51 O ANISOU 1101 O THR A 148 9945 11923 8722 -1313 -925 -217 O ATOM 1102 CB THR A 148 -6.042 -9.929 -41.779 1.00 59.98 C ANISOU 1102 CB THR A 148 7581 9241 5968 -1344 -1178 -76 C ATOM 1103 OG1 THR A 148 -5.096 -10.218 -40.742 1.00 63.00 O ANISOU 1103 OG1 THR A 148 7899 9748 6289 -1447 -1371 57 O ATOM 1104 CG2 THR A 148 -6.246 -11.174 -42.630 1.00 56.96 C ANISOU 1104 CG2 THR A 148 6936 8904 5802 -1091 -1038 -99 C ATOM 1105 N CYS A 149 -7.519 -7.723 -43.592 1.00 69.96 N ANISOU 1105 N CYS A 149 9183 10267 7131 -1419 -926 -287 N ATOM 1106 CA CYS A 149 -8.487 -7.482 -44.657 1.00 68.10 C ANISOU 1106 CA CYS A 149 8969 9958 6946 -1289 -750 -374 C ATOM 1107 C CYS A 149 -7.930 -6.543 -45.721 1.00 68.49 C ANISOU 1107 C CYS A 149 8965 10082 6976 -1426 -748 -365 C ATOM 1108 O CYS A 149 -8.183 -6.737 -46.916 1.00 76.92 O ANISOU 1108 O CYS A 149 9874 11216 8137 -1319 -639 -402 O ATOM 1109 CB CYS A 149 -9.786 -6.928 -44.073 1.00 69.09 C ANISOU 1109 CB CYS A 149 9428 9862 6960 -1219 -651 -431 C ATOM 1110 SG CYS A 149 -10.761 -8.149 -43.161 1.00 66.94 S ANISOU 1110 SG CYS A 149 9177 9511 6745 -1008 -582 -445 S ATOM 1111 N ILE A 150 -7.172 -5.519 -45.316 1.00 70.68 N ANISOU 1111 N ILE A 150 9385 10351 7121 -1679 -870 -315 N ATOM 1112 CA ILE A 150 -6.604 -4.612 -46.309 1.00 75.22 C ANISOU 1112 CA ILE A 150 9913 10990 7676 -1833 -866 -291 C ATOM 1113 C ILE A 150 -5.539 -5.322 -47.134 1.00 79.84 C ANISOU 1113 C ILE A 150 10088 11844 8404 -1830 -897 -225 C ATOM 1114 O ILE A 150 -5.325 -4.983 -48.305 1.00 98.30 O ANISOU 1114 O ILE A 150 12304 14267 10780 -1843 -823 -221 O ATOM 1115 CB ILE A 150 -6.049 -3.334 -45.646 1.00 79.98 C ANISOU 1115 CB ILE A 150 10795 11499 8097 -2141 -991 -255 C ATOM 1116 CG1 ILE A 150 -4.798 -3.637 -44.819 1.00111.87 C ANISOU 1116 CG1 ILE A 150 14691 15705 12108 -2349 -1206 -159 C ATOM 1117 CG2 ILE A 150 -7.115 -2.669 -44.788 1.00 71.40 C ANISOU 1117 CG2 ILE A 150 10148 10125 6857 -2109 -930 -326 C ATOM 1118 CD1 ILE A 150 -4.142 -2.407 -44.228 1.00135.00 C ANISOU 1118 CD1 ILE A 150 17879 18568 14848 -2712 -1356 -125 C ATOM 1119 N ILE A 151 -4.861 -6.315 -46.555 1.00 64.45 N ANISOU 1119 N ILE A 151 7924 10033 6530 -1794 -993 -162 N ATOM 1120 CA ILE A 151 -3.931 -7.124 -47.336 1.00 70.69 C ANISOU 1120 CA ILE A 151 8321 11070 7469 -1723 -982 -95 C ATOM 1121 C ILE A 151 -4.697 -8.045 -48.277 1.00 65.55 C ANISOU 1121 C ILE A 151 7554 10402 6949 -1440 -796 -191 C ATOM 1122 O ILE A 151 -4.283 -8.272 -49.420 1.00 72.68 O ANISOU 1122 O ILE A 151 8235 11446 7932 -1382 -711 -189 O ATOM 1123 CB ILE A 151 -2.990 -7.913 -46.405 1.00 69.24 C ANISOU 1123 CB ILE A 151 7946 11037 7325 -1740 -1131 24 C ATOM 1124 CG1 ILE A 151 -2.114 -6.957 -45.594 1.00 53.27 C ANISOU 1124 CG1 ILE A 151 6008 9079 5155 -2073 -1341 127 C ATOM 1125 CG2 ILE A 151 -2.120 -8.873 -47.206 1.00 71.78 C ANISOU 1125 CG2 ILE A 151 7862 11595 7814 -1594 -1078 99 C ATOM 1126 CD1 ILE A 151 -1.217 -7.651 -44.588 1.00 73.74 C ANISOU 1126 CD1 ILE A 151 8417 11843 7757 -2108 -1518 267 C ATOM 1127 N ILE A 152 -5.830 -8.581 -47.816 1.00 53.64 N ANISOU 1127 N ILE A 152 6203 8724 5453 -1276 -730 -276 N ATOM 1128 CA ILE A 152 -6.659 -9.423 -48.674 1.00 64.86 C ANISOU 1128 CA ILE A 152 7545 10119 6981 -1050 -569 -375 C ATOM 1129 C ILE A 152 -7.187 -8.620 -49.856 1.00 64.40 C ANISOU 1129 C ILE A 152 7542 10050 6877 -1067 -466 -436 C ATOM 1130 O ILE A 152 -7.252 -9.122 -50.985 1.00 73.32 O ANISOU 1130 O ILE A 152 8510 11268 8078 -957 -361 -487 O ATOM 1131 CB ILE A 152 -7.797 -10.063 -47.856 1.00 70.77 C ANISOU 1131 CB ILE A 152 8455 10693 7741 -913 -529 -434 C ATOM 1132 CG1 ILE A 152 -7.247 -11.182 -46.969 1.00 68.68 C ANISOU 1132 CG1 ILE A 152 8076 10462 7556 -839 -597 -368 C ATOM 1133 CG2 ILE A 152 -8.891 -10.599 -48.769 1.00 66.22 C ANISOU 1133 CG2 ILE A 152 7859 10069 7232 -748 -374 -544 C ATOM 1134 CD1 ILE A 152 -8.292 -11.853 -46.107 1.00 60.78 C ANISOU 1134 CD1 ILE A 152 7231 9297 6568 -720 -557 -406 C ATOM 1135 N TRP A 153 -7.556 -7.356 -49.624 1.00 65.11 N ANISOU 1135 N TRP A 153 7879 10027 6835 -1199 -489 -428 N ATOM 1136 CA TRP A 153 -7.976 -6.506 -50.734 1.00 67.15 C ANISOU 1136 CA TRP A 153 8194 10280 7042 -1214 -396 -454 C ATOM 1137 C TRP A 153 -6.838 -6.295 -51.725 1.00 76.12 C ANISOU 1137 C TRP A 153 9108 11611 8201 -1315 -402 -397 C ATOM 1138 O TRP A 153 -7.045 -6.358 -52.943 1.00 81.09 O ANISOU 1138 O TRP A 153 9635 12323 8852 -1237 -296 -433 O ATOM 1139 CB TRP A 153 -8.483 -5.154 -50.225 1.00 63.58 C ANISOU 1139 CB TRP A 153 8074 9643 6441 -1329 -410 -437 C ATOM 1140 CG TRP A 153 -9.638 -5.200 -49.256 1.00 80.01 C ANISOU 1140 CG TRP A 153 10394 11531 8477 -1219 -376 -480 C ATOM 1141 CD1 TRP A 153 -9.762 -4.473 -48.107 1.00 96.93 C ANISOU 1141 CD1 TRP A 153 12832 13502 10494 -1318 -430 -462 C ATOM 1142 CD2 TRP A 153 -10.831 -5.996 -49.355 1.00 81.66 C ANISOU 1142 CD2 TRP A 153 10572 11704 8751 -1001 -272 -542 C ATOM 1143 NE1 TRP A 153 -10.949 -4.768 -47.484 1.00103.56 N ANISOU 1143 NE1 TRP A 153 13818 14209 11322 -1151 -349 -503 N ATOM 1144 CE2 TRP A 153 -11.623 -5.700 -48.228 1.00 91.73 C ANISOU 1144 CE2 TRP A 153 12108 12799 9947 -963 -258 -544 C ATOM 1145 CE3 TRP A 153 -11.304 -6.931 -50.282 1.00 93.83 C ANISOU 1145 CE3 TRP A 153 11900 13350 10400 -850 -190 -598 C ATOM 1146 CZ2 TRP A 153 -12.858 -6.303 -48.004 1.00 93.49 C ANISOU 1146 CZ2 TRP A 153 12349 12963 10209 -778 -161 -580 C ATOM 1147 CZ3 TRP A 153 -12.530 -7.528 -50.057 1.00 96.10 C ANISOU 1147 CZ3 TRP A 153 12220 13571 10722 -695 -113 -643 C ATOM 1148 CH2 TRP A 153 -13.293 -7.212 -48.928 1.00 90.99 C ANISOU 1148 CH2 TRP A 153 11801 12763 10009 -659 -98 -625 C ATOM 1149 N LEU A 154 -5.627 -6.041 -51.222 1.00 65.53 N ANISOU 1149 N LEU A 154 7684 10366 6848 -1498 -526 -299 N ATOM 1150 CA LEU A 154 -4.494 -5.813 -52.113 1.00 55.03 C ANISOU 1150 CA LEU A 154 6119 9246 5543 -1607 -526 -220 C ATOM 1151 C LEU A 154 -4.111 -7.083 -52.863 1.00 63.42 C ANISOU 1151 C LEU A 154 6868 10485 6743 -1409 -435 -238 C ATOM 1152 O LEU A 154 -3.852 -7.041 -54.071 1.00 81.51 O ANISOU 1152 O LEU A 154 9018 12903 9048 -1376 -331 -242 O ATOM 1153 CB LEU A 154 -3.300 -5.276 -51.324 1.00 58.56 C ANISOU 1153 CB LEU A 154 6527 9780 5945 -1870 -696 -93 C ATOM 1154 CG LEU A 154 -3.463 -3.888 -50.704 1.00 69.74 C ANISOU 1154 CG LEU A 154 8281 11017 7201 -2122 -782 -76 C ATOM 1155 CD1 LEU A 154 -2.145 -3.398 -50.122 1.00 73.29 C ANISOU 1155 CD1 LEU A 154 8645 11601 7601 -2431 -963 55 C ATOM 1156 CD2 LEU A 154 -4.007 -2.900 -51.724 1.00 66.42 C ANISOU 1156 CD2 LEU A 154 8019 10503 6714 -2144 -661 -104 C ATOM 1157 N LEU A 155 -4.069 -8.221 -52.165 1.00 66.14 N ANISOU 1157 N LEU A 155 7121 10828 7179 -1269 -461 -248 N ATOM 1158 CA LEU A 155 -3.725 -9.476 -52.826 1.00 75.10 C ANISOU 1158 CA LEU A 155 8003 12088 8443 -1060 -354 -273 C ATOM 1159 C LEU A 155 -4.785 -9.870 -53.847 1.00 83.79 C ANISOU 1159 C LEU A 155 9169 13115 9551 -898 -197 -421 C ATOM 1160 O LEU A 155 -4.464 -10.433 -54.900 1.00 93.70 O ANISOU 1160 O LEU A 155 10257 14490 10853 -788 -79 -456 O ATOM 1161 CB LEU A 155 -3.533 -10.582 -51.789 1.00 73.57 C ANISOU 1161 CB LEU A 155 7743 11868 8341 -939 -411 -242 C ATOM 1162 CG LEU A 155 -2.314 -10.434 -50.877 1.00 74.22 C ANISOU 1162 CG LEU A 155 7681 12093 8425 -1075 -574 -71 C ATOM 1163 CD1 LEU A 155 -2.162 -11.645 -49.969 1.00 79.69 C ANISOU 1163 CD1 LEU A 155 8296 12770 9214 -908 -609 -27 C ATOM 1164 CD2 LEU A 155 -1.054 -10.214 -51.700 1.00 67.68 C ANISOU 1164 CD2 LEU A 155 6560 11527 7630 -1141 -553 44 C ATOM 1165 N ALA A 156 -6.056 -9.584 -53.554 1.00 83.88 N ANISOU 1165 N ALA A 156 9421 12943 9505 -882 -192 -503 N ATOM 1166 CA ALA A 156 -7.111 -9.849 -54.527 1.00 81.79 C ANISOU 1166 CA ALA A 156 9207 12641 9228 -763 -70 -625 C ATOM 1167 C ALA A 156 -7.027 -8.885 -55.703 1.00 77.71 C ANISOU 1167 C ALA A 156 8687 12220 8620 -843 -15 -611 C ATOM 1168 O ALA A 156 -7.211 -9.288 -56.857 1.00 85.91 O ANISOU 1168 O ALA A 156 9641 13346 9656 -755 91 -683 O ATOM 1169 CB ALA A 156 -8.482 -9.762 -53.857 1.00 84.57 C ANISOU 1169 CB ALA A 156 9780 12805 9547 -723 -79 -682 C ATOM 1170 N GLY A 157 -6.753 -7.607 -55.431 1.00 75.89 N ANISOU 1170 N GLY A 157 8569 11964 8301 -1018 -85 -520 N ATOM 1171 CA GLY A 157 -6.577 -6.654 -56.513 1.00 73.50 C ANISOU 1171 CA GLY A 157 8271 11745 7912 -1104 -31 -482 C ATOM 1172 C GLY A 157 -5.340 -6.942 -57.342 1.00 80.77 C ANISOU 1172 C GLY A 157 8929 12888 8871 -1128 16 -430 C ATOM 1173 O GLY A 157 -5.341 -6.753 -58.562 1.00 91.39 O ANISOU 1173 O GLY A 157 10216 14341 10166 -1104 117 -444 O ATOM 1174 N LEU A 158 -4.267 -7.399 -56.691 1.00 78.96 N ANISOU 1174 N LEU A 158 8530 12748 8724 -1167 -50 -355 N ATOM 1175 CA LEU A 158 -3.080 -7.818 -57.427 1.00 81.34 C ANISOU 1175 CA LEU A 158 8544 13282 9079 -1145 17 -290 C ATOM 1176 C LEU A 158 -3.357 -9.056 -58.270 1.00 79.71 C ANISOU 1176 C LEU A 158 8232 13122 8930 -901 169 -411 C ATOM 1177 O LEU A 158 -2.766 -9.221 -59.343 1.00 91.87 O ANISOU 1177 O LEU A 158 9613 14831 10462 -852 289 -402 O ATOM 1178 CB LEU A 158 -1.926 -8.077 -56.457 1.00 80.53 C ANISOU 1178 CB LEU A 158 8263 13281 9055 -1220 -97 -160 C ATOM 1179 CG LEU A 158 -0.575 -8.462 -57.063 1.00 92.52 C ANISOU 1179 CG LEU A 158 9441 15070 10640 -1194 -31 -46 C ATOM 1180 CD1 LEU A 158 0.001 -7.308 -57.870 1.00 99.26 C ANISOU 1180 CD1 LEU A 158 10246 16061 11409 -1400 -9 52 C ATOM 1181 CD2 LEU A 158 0.397 -8.905 -55.981 1.00 98.41 C ANISOU 1181 CD2 LEU A 158 9997 15921 11474 -1223 -157 92 C ATOM 1182 N ALA A 159 -4.252 -9.931 -57.806 1.00 78.87 N ANISOU 1182 N ALA A 159 8231 12863 8874 -757 173 -528 N ATOM 1183 CA ALA A 159 -4.619 -11.111 -58.580 1.00 68.15 C ANISOU 1183 CA ALA A 159 6829 11508 7556 -557 311 -664 C ATOM 1184 C ALA A 159 -5.573 -10.773 -59.719 1.00 64.74 C ANISOU 1184 C ALA A 159 6516 11072 7009 -552 390 -771 C ATOM 1185 O ALA A 159 -5.496 -11.388 -60.788 1.00 64.94 O ANISOU 1185 O ALA A 159 6476 11185 7013 -450 520 -857 O ATOM 1186 CB ALA A 159 -5.242 -12.166 -57.667 1.00 56.64 C ANISOU 1186 CB ALA A 159 5448 9880 6190 -436 284 -740 C ATOM 1187 N SER A 160 -6.467 -9.808 -59.516 1.00 61.65 N ANISOU 1187 N SER A 160 6305 10585 6533 -652 319 -760 N ATOM 1188 CA SER A 160 -7.388 -9.359 -60.552 1.00 78.56 C ANISOU 1188 CA SER A 160 8547 12747 8556 -650 374 -821 C ATOM 1189 C SER A 160 -6.789 -8.275 -61.438 1.00 83.80 C ANISOU 1189 C SER A 160 9174 13550 9118 -758 409 -723 C ATOM 1190 O SER A 160 -7.523 -7.639 -62.201 1.00 76.10 O ANISOU 1190 O SER A 160 8299 12590 8027 -773 436 -730 O ATOM 1191 CB SER A 160 -8.688 -8.851 -59.923 1.00 78.03 C ANISOU 1191 CB SER A 160 8680 12518 8451 -667 302 -831 C ATOM 1192 OG SER A 160 -8.462 -7.680 -59.158 1.00 86.11 O ANISOU 1192 OG SER A 160 9811 13463 9443 -795 219 -710 O ATOM 1193 N LEU A 161 -5.479 -8.050 -61.351 1.00 91.53 N ANISOU 1193 N LEU A 161 10002 14641 10135 -837 409 -614 N ATOM 1194 CA LEU A 161 -4.785 -7.050 -62.153 1.00 84.05 C ANISOU 1194 CA LEU A 161 9001 13834 9101 -964 449 -501 C ATOM 1195 C LEU A 161 -4.792 -7.397 -63.642 1.00 82.93 C ANISOU 1195 C LEU A 161 8785 13851 8875 -869 600 -566 C ATOM 1196 O LEU A 161 -4.997 -6.498 -64.468 1.00 94.70 O ANISOU 1196 O LEU A 161 10344 15399 10241 -941 634 -515 O ATOM 1197 CB LEU A 161 -3.351 -6.869 -61.647 1.00 89.56 C ANISOU 1197 CB LEU A 161 9512 14644 9872 -1082 408 -358 C ATOM 1198 CG LEU A 161 -2.605 -5.630 -62.144 1.00 87.25 C ANISOU 1198 CG LEU A 161 9188 14464 9500 -1288 411 -205 C ATOM 1199 CD1 LEU A 161 -3.404 -4.372 -61.840 1.00 79.30 C ANISOU 1199 CD1 LEU A 161 8463 13271 8397 -1429 331 -172 C ATOM 1200 CD2 LEU A 161 -1.224 -5.552 -61.515 1.00 84.67 C ANISOU 1200 CD2 LEU A 161 8647 14269 9256 -1426 344 -56 C ATOM 1201 N PRO A 162 -4.567 -8.656 -64.044 1.00 81.54 N ANISOU 1201 N PRO A 162 8492 13741 8747 -707 701 -676 N ATOM 1202 CA PRO A 162 -4.697 -8.983 -65.475 1.00 84.32 C ANISOU 1202 CA PRO A 162 8828 14226 8982 -623 847 -764 C ATOM 1203 C PRO A 162 -6.101 -8.785 -66.015 1.00 90.91 C ANISOU 1203 C PRO A 162 9851 14998 9691 -615 822 -862 C ATOM 1204 O PRO A 162 -6.259 -8.573 -67.224 1.00 83.02 O ANISOU 1204 O PRO A 162 8870 14128 8545 -609 905 -885 O ATOM 1205 CB PRO A 162 -4.272 -10.457 -65.544 1.00 82.58 C ANISOU 1205 CB PRO A 162 8503 14023 8852 -442 954 -880 C ATOM 1206 CG PRO A 162 -4.437 -10.970 -64.160 1.00 81.27 C ANISOU 1206 CG PRO A 162 8355 13687 8837 -415 843 -885 C ATOM 1207 CD PRO A 162 -4.070 -9.818 -63.284 1.00 81.64 C ANISOU 1207 CD PRO A 162 8392 13719 8910 -589 705 -713 C ATOM 1208 N ALA A 163 -7.126 -8.845 -65.163 1.00 99.94 N ANISOU 1208 N ALA A 163 11125 15969 10880 -612 712 -905 N ATOM 1209 CA ALA A 163 -8.486 -8.559 -65.601 1.00 95.72 C ANISOU 1209 CA ALA A 163 10736 15402 10233 -607 676 -958 C ATOM 1210 C ALA A 163 -8.709 -7.081 -65.891 1.00 96.60 C ANISOU 1210 C ALA A 163 10934 15536 10234 -705 643 -810 C ATOM 1211 O ALA A 163 -9.747 -6.729 -66.462 1.00106.02 O ANISOU 1211 O ALA A 163 12220 16751 11311 -686 628 -816 O ATOM 1212 CB ALA A 163 -9.490 -9.038 -64.551 1.00 92.56 C ANISOU 1212 CB ALA A 163 10426 14823 9921 -569 584 -1022 C ATOM 1213 N ILE A 164 -7.773 -6.216 -65.512 1.00 91.08 N ANISOU 1213 N ILE A 164 10210 14832 9565 -815 628 -667 N ATOM 1214 CA ILE A 164 -7.867 -4.795 -65.812 1.00 84.86 C ANISOU 1214 CA ILE A 164 9533 14037 8673 -920 615 -519 C ATOM 1215 C ILE A 164 -6.918 -4.374 -66.928 1.00 85.77 C ANISOU 1215 C ILE A 164 9547 14344 8698 -986 716 -436 C ATOM 1216 O ILE A 164 -7.177 -3.354 -67.588 1.00 86.53 O ANISOU 1216 O ILE A 164 9742 14467 8668 -1040 737 -332 O ATOM 1217 CB ILE A 164 -7.614 -3.944 -64.550 1.00 75.85 C ANISOU 1217 CB ILE A 164 8499 12717 7605 -1042 518 -410 C ATOM 1218 CG1 ILE A 164 -8.214 -4.628 -63.321 1.00 81.71 C ANISOU 1218 CG1 ILE A 164 9292 13296 8457 -972 436 -498 C ATOM 1219 CG2 ILE A 164 -8.199 -2.549 -64.714 1.00 69.23 C ANISOU 1219 CG2 ILE A 164 7866 11781 6656 -1105 506 -288 C ATOM 1220 CD1 ILE A 164 -7.980 -3.878 -62.026 1.00101.96 C ANISOU 1220 CD1 ILE A 164 11989 15682 11070 -1091 341 -412 C ATOM 1221 N ILE A 165 -5.844 -5.120 -67.170 1.00 83.05 N ANISOU 1221 N ILE A 165 9011 14135 8410 -967 794 -466 N ATOM 1222 CA ILE A 165 -4.853 -4.743 -68.173 1.00 82.40 C ANISOU 1222 CA ILE A 165 8808 14252 8249 -1027 910 -371 C ATOM 1223 C ILE A 165 -5.170 -5.360 -69.529 1.00 89.86 C ANISOU 1223 C ILE A 165 9734 15356 9052 -904 1035 -481 C ATOM 1224 O ILE A 165 -5.117 -4.683 -70.559 1.00104.40 O ANISOU 1224 O ILE A 165 11602 17324 10741 -947 1106 -402 O ATOM 1225 CB ILE A 165 -3.441 -5.141 -67.692 1.00 74.84 C ANISOU 1225 CB ILE A 165 7627 13384 7425 -1067 940 -309 C ATOM 1226 CG1 ILE A 165 -3.129 -4.486 -66.344 1.00 87.59 C ANISOU 1226 CG1 ILE A 165 9276 14855 9148 -1227 791 -200 C ATOM 1227 CG2 ILE A 165 -2.394 -4.763 -68.730 1.00 70.87 C ANISOU 1227 CG2 ILE A 165 6970 13112 6844 -1127 1079 -193 C ATOM 1228 CD1 ILE A 165 -3.145 -2.974 -66.380 1.00103.54 C ANISOU 1228 CD1 ILE A 165 11446 16812 11084 -1430 743 -46 C ATOM 1229 N HIS A 166 -5.508 -6.650 -69.554 1.00 78.90 N ANISOU 1229 N HIS A 166 9031 11820 9129 1207 270 1186 N ATOM 1230 CA HIS A 166 -5.670 -7.371 -70.810 1.00 79.50 C ANISOU 1230 CA HIS A 166 9242 12002 8961 1244 399 1184 C ATOM 1231 C HIS A 166 -7.120 -7.536 -71.245 1.00 81.82 C ANISOU 1231 C HIS A 166 9622 12470 8997 1248 272 1058 C ATOM 1232 O HIS A 166 -7.366 -7.766 -72.434 1.00 85.55 O ANISOU 1232 O HIS A 166 10229 13032 9243 1276 337 1086 O ATOM 1233 CB HIS A 166 -5.014 -8.752 -70.712 1.00 80.56 C ANISOU 1233 CB HIS A 166 9416 12119 9075 1213 554 1123 C ATOM 1234 CG HIS A 166 -3.532 -8.700 -70.506 1.00 84.81 C ANISOU 1234 CG HIS A 166 9850 12535 9839 1230 710 1295 C ATOM 1235 ND1 HIS A 166 -2.958 -8.512 -69.268 1.00 87.69 N ANISOU 1235 ND1 HIS A 166 10048 12810 10460 1167 638 1315 N ATOM 1236 CD2 HIS A 166 -2.507 -8.803 -71.384 1.00 87.39 C ANISOU 1236 CD2 HIS A 166 10203 12832 10167 1302 933 1474 C ATOM 1237 CE1 HIS A 166 -1.643 -8.506 -69.391 1.00 89.75 C ANISOU 1237 CE1 HIS A 166 10213 13007 10880 1185 794 1511 C ATOM 1238 NE2 HIS A 166 -1.343 -8.680 -70.665 1.00 90.36 N ANISOU 1238 NE2 HIS A 166 10397 13122 10813 1278 988 1616 N ATOM 1239 N ARG A 167 -8.077 -7.438 -70.325 1.00 79.59 N ANISOU 1239 N ARG A 167 9261 12250 8730 1220 96 933 N ATOM 1240 CA ARG A 167 -9.484 -7.485 -70.703 1.00 74.17 C ANISOU 1240 CA ARG A 167 8601 11763 7815 1224 -38 857 C ATOM 1241 C ARG A 167 -9.826 -6.295 -71.586 1.00 81.40 C ANISOU 1241 C ARG A 167 9541 12722 8664 1336 -73 1007 C ATOM 1242 O ARG A 167 -9.682 -5.142 -71.170 1.00 83.51 O ANISOU 1242 O ARG A 167 9750 12884 9098 1417 -116 1100 O ATOM 1243 CB ARG A 167 -10.367 -7.491 -69.458 1.00 63.31 C ANISOU 1243 CB ARG A 167 7103 10449 6501 1200 -196 734 C ATOM 1244 CG ARG A 167 -10.790 -8.870 -68.992 1.00 65.89 C ANISOU 1244 CG ARG A 167 7439 10865 6730 1071 -217 562 C ATOM 1245 CD ARG A 167 -11.961 -9.398 -69.804 1.00 62.69 C ANISOU 1245 CD ARG A 167 7091 10694 6034 1007 -302 512 C ATOM 1246 NE ARG A 167 -12.437 -10.678 -69.288 1.00 60.39 N ANISOU 1246 NE ARG A 167 6816 10478 5651 854 -341 353 N ATOM 1247 CZ ARG A 167 -13.622 -11.205 -69.572 1.00 65.19 C ANISOU 1247 CZ ARG A 167 7424 11308 6036 745 -469 291 C ATOM 1248 NH1 ARG A 167 -14.467 -10.561 -70.366 1.00 61.33 N ANISOU 1248 NH1 ARG A 167 6900 11009 5393 788 -574 382 N ATOM 1249 NH2 ARG A 167 -13.966 -12.375 -69.054 1.00 73.77 N ANISOU 1249 NH2 ARG A 167 8540 12433 7055 583 -498 154 N ATOM 1250 N ASN A 168 -10.277 -6.572 -72.805 1.00 86.47 N ANISOU 1250 N ASN A 168 10296 13509 9049 1338 -58 1034 N ATOM 1251 CA ASN A 168 -10.611 -5.520 -73.751 1.00 78.95 C ANISOU 1251 CA ASN A 168 9379 12615 8003 1450 -86 1190 C ATOM 1252 C ASN A 168 -11.873 -5.894 -74.510 1.00 69.86 C ANISOU 1252 C ASN A 168 8270 11728 6545 1423 -210 1151 C ATOM 1253 O ASN A 168 -12.329 -7.041 -74.489 1.00 61.38 O ANISOU 1253 O ASN A 168 7238 10770 5315 1288 -251 1010 O ATOM 1254 CB ASN A 168 -9.460 -5.254 -74.730 1.00 82.22 C ANISOU 1254 CB ASN A 168 9908 12904 8429 1492 102 1344 C ATOM 1255 CG ASN A 168 -8.692 -3.991 -74.396 1.00 90.01 C ANISOU 1255 CG ASN A 168 10828 13698 9675 1569 137 1505 C ATOM 1256 OD1 ASN A 168 -9.163 -2.882 -74.649 1.00 91.62 O ANISOU 1256 OD1 ASN A 168 11030 13908 9873 1669 60 1614 O ATOM 1257 ND2 ASN A 168 -7.501 -4.152 -73.831 1.00 92.37 N ANISOU 1257 ND2 ASN A 168 11079 13823 10196 1517 250 1534 N ATOM 1258 N VAL A 169 -12.438 -4.898 -75.181 1.00 70.73 N ANISOU 1258 N VAL A 169 8373 11933 6569 1541 -280 1293 N ATOM 1259 CA VAL A 169 -13.578 -5.093 -76.066 1.00 72.78 C ANISOU 1259 CA VAL A 169 8662 12467 6526 1521 -410 1311 C ATOM 1260 C VAL A 169 -13.043 -5.435 -77.451 1.00 82.93 C ANISOU 1260 C VAL A 169 10163 13750 7595 1489 -293 1371 C ATOM 1261 O VAL A 169 -12.293 -4.654 -78.046 1.00 98.04 O ANISOU 1261 O VAL A 169 12146 15536 9569 1600 -171 1524 O ATOM 1262 CB VAL A 169 -14.468 -3.842 -76.106 1.00 65.75 C ANISOU 1262 CB VAL A 169 7651 11691 5638 1695 -536 1457 C ATOM 1263 CG1 VAL A 169 -15.362 -3.867 -77.323 1.00 86.42 C ANISOU 1263 CG1 VAL A 169 10315 14581 7939 1693 -644 1546 C ATOM 1264 CG2 VAL A 169 -15.301 -3.748 -74.838 1.00 82.49 C ANISOU 1264 CG2 VAL A 169 9576 13888 7877 1726 -660 1380 C ATOM 1265 N PHE A 170 -13.417 -6.606 -77.959 1.00 72.00 N ANISOU 1265 N PHE A 170 8909 12497 5951 1331 -326 1253 N ATOM 1266 CA PHE A 170 -12.932 -7.094 -79.241 1.00 70.83 C ANISOU 1266 CA PHE A 170 9023 12335 5554 1294 -205 1279 C ATOM 1267 C PHE A 170 -14.083 -7.204 -80.230 1.00 72.70 C ANISOU 1267 C PHE A 170 9338 12850 5436 1223 -387 1308 C ATOM 1268 O PHE A 170 -15.170 -7.679 -79.886 1.00 76.66 O ANISOU 1268 O PHE A 170 9742 13558 5825 1092 -589 1222 O ATOM 1269 CB PHE A 170 -12.244 -8.456 -79.093 1.00 73.43 C ANISOU 1269 CB PHE A 170 9526 12533 5840 1164 -61 1114 C ATOM 1270 CG PHE A 170 -10.978 -8.412 -78.286 1.00 74.72 C ANISOU 1270 CG PHE A 170 9621 12443 6328 1237 136 1121 C ATOM 1271 CD1 PHE A 170 -9.788 -7.999 -78.861 1.00 77.62 C ANISOU 1271 CD1 PHE A 170 10067 12650 6775 1355 360 1267 C ATOM 1272 CD2 PHE A 170 -10.976 -8.790 -76.954 1.00 64.18 C ANISOU 1272 CD2 PHE A 170 8129 11045 5210 1179 92 1001 C ATOM 1273 CE1 PHE A 170 -8.621 -7.959 -78.124 1.00 73.65 C ANISOU 1273 CE1 PHE A 170 9466 11946 6571 1403 522 1304 C ATOM 1274 CE2 PHE A 170 -9.811 -8.752 -76.211 1.00 64.61 C ANISOU 1274 CE2 PHE A 170 8111 10887 5553 1231 249 1024 C ATOM 1275 CZ PHE A 170 -8.632 -8.337 -76.796 1.00 64.21 C ANISOU 1275 CZ PHE A 170 8117 10694 5586 1336 457 1182 C ATOM 1276 N PHE A 171 -13.834 -6.760 -81.459 1.00 74.33 N ANISOU 1276 N PHE A 171 9709 13073 5460 1301 -320 1445 N ATOM 1277 CA PHE A 171 -14.793 -6.885 -82.547 1.00 77.81 C ANISOU 1277 CA PHE A 171 10264 13773 5527 1224 -488 1489 C ATOM 1278 C PHE A 171 -14.507 -8.180 -83.299 1.00 77.94 C ANISOU 1278 C PHE A 171 10620 13756 5237 1047 -412 1349 C ATOM 1279 O PHE A 171 -13.416 -8.353 -83.852 1.00 81.65 O ANISOU 1279 O PHE A 171 11312 14028 5684 1118 -165 1367 O ATOM 1280 CB PHE A 171 -14.706 -5.679 -83.482 1.00 77.05 C ANISOU 1280 CB PHE A 171 10188 13710 5378 1411 -461 1722 C ATOM 1281 CG PHE A 171 -15.773 -5.647 -84.541 1.00 79.95 C ANISOU 1281 CG PHE A 171 10627 14376 5372 1351 -667 1802 C ATOM 1282 CD1 PHE A 171 -16.990 -5.031 -84.297 1.00 83.31 C ANISOU 1282 CD1 PHE A 171 10798 15066 5789 1393 -910 1902 C ATOM 1283 CD2 PHE A 171 -15.554 -6.221 -85.782 1.00 82.07 C ANISOU 1283 CD2 PHE A 171 11222 14670 5289 1263 -614 1793 C ATOM 1284 CE1 PHE A 171 -17.971 -4.996 -85.270 1.00 86.43 C ANISOU 1284 CE1 PHE A 171 11230 15769 5842 1332 -1117 2004 C ATOM 1285 CE2 PHE A 171 -16.532 -6.189 -86.758 1.00 84.88 C ANISOU 1285 CE2 PHE A 171 11654 15312 5285 1186 -828 1873 C ATOM 1286 CZ PHE A 171 -17.742 -5.576 -86.502 1.00 88.23 C ANISOU 1286 CZ PHE A 171 11788 16021 5715 1212 -1090 1987 C ATOM 1287 N ILE A 172 -15.477 -9.088 -83.311 1.00 77.61 N ANISOU 1287 N ILE A 172 10629 13903 4956 818 -616 1218 N ATOM 1288 CA ILE A 172 -15.307 -10.399 -83.927 1.00 79.05 C ANISOU 1288 CA ILE A 172 11182 14029 4825 620 -566 1057 C ATOM 1289 C ILE A 172 -15.687 -10.288 -85.399 1.00106.82 C ANISOU 1289 C ILE A 172 14952 17700 7934 579 -645 1146 C ATOM 1290 O ILE A 172 -16.850 -10.052 -85.734 1.00108.26 O ANISOU 1290 O ILE A 172 15027 18179 7926 473 -925 1214 O ATOM 1291 CB ILE A 172 -16.143 -11.467 -83.213 1.00 93.34 C ANISOU 1291 CB ILE A 172 12958 15944 6565 351 -757 872 C ATOM 1292 CG1 ILE A 172 -15.673 -11.626 -81.765 1.00 75.60 C ANISOU 1292 CG1 ILE A 172 10494 13525 4707 402 -655 781 C ATOM 1293 CG2 ILE A 172 -16.060 -12.793 -83.955 1.00 80.83 C ANISOU 1293 CG2 ILE A 172 11819 14286 4606 126 -728 707 C ATOM 1294 CD1 ILE A 172 -16.431 -12.679 -80.990 1.00 75.24 C ANISOU 1294 CD1 ILE A 172 10410 13563 4614 145 -818 609 C ATOM 1295 N GLU A 173 -14.700 -10.460 -86.282 1.00113.64 N ANISOU 1295 N GLU A 173 16146 18375 8656 669 -394 1162 N ATOM 1296 CA GLU A 173 -14.960 -10.410 -87.716 1.00 86.73 C ANISOU 1296 CA GLU A 173 13036 15087 4831 636 -443 1239 C ATOM 1297 C GLU A 173 -15.825 -11.570 -88.190 1.00 89.12 C ANISOU 1297 C GLU A 173 13624 15526 4710 314 -660 1074 C ATOM 1298 O GLU A 173 -16.492 -11.445 -89.223 1.00 98.09 O ANISOU 1298 O GLU A 173 14915 16870 5486 218 -840 1147 O ATOM 1299 CB GLU A 173 -13.642 -10.404 -88.493 1.00 92.39 C ANISOU 1299 CB GLU A 173 14057 15554 5492 820 -86 1292 C ATOM 1300 CG GLU A 173 -12.772 -9.182 -88.251 1.00103.42 C ANISOU 1300 CG GLU A 173 15203 16833 7258 1104 114 1496 C ATOM 1301 CD GLU A 173 -11.458 -9.247 -89.007 1.00114.79 C ANISOU 1301 CD GLU A 173 16917 18054 8645 1274 480 1572 C ATOM 1302 OE1 GLU A 173 -11.155 -10.313 -89.583 1.00120.02 O ANISOU 1302 OE1 GLU A 173 17971 18622 9009 1202 612 1442 O ATOM 1303 OE2 GLU A 173 -10.730 -8.233 -89.026 1.00118.93 O ANISOU 1303 OE2 GLU A 173 17275 18495 9416 1480 642 1771 O ATOM 1304 N ASN A 174 -15.828 -12.691 -87.463 1.00 88.16 N ANISOU 1304 N ASN A 174 13590 15292 4615 131 -657 862 N ATOM 1305 CA ASN A 174 -16.608 -13.849 -87.887 1.00102.40 C ANISOU 1305 CA ASN A 174 15708 17188 6011 -213 -863 697 C ATOM 1306 C ASN A 174 -18.102 -13.555 -87.866 1.00107.72 C ANISOU 1306 C ASN A 174 16103 18260 6567 -425 -1280 777 C ATOM 1307 O ASN A 174 -18.831 -13.945 -88.785 1.00122.87 O ANISOU 1307 O ASN A 174 18263 20361 8060 -663 -1502 770 O ATOM 1308 CB ASN A 174 -16.292 -15.052 -86.995 1.00106.77 C ANISOU 1308 CB ASN A 174 16387 17519 6660 -353 -766 470 C ATOM 1309 CG ASN A 174 -15.180 -15.918 -87.554 1.00111.27 C ANISOU 1309 CG ASN A 174 17478 17753 7048 -288 -436 347 C ATOM 1310 OD1 ASN A 174 -14.108 -16.031 -86.961 1.00 88.28 O ANISOU 1310 OD1 ASN A 174 14536 14583 4421 -82 -133 324 O ATOM 1311 ND2 ASN A 174 -15.436 -16.543 -88.698 1.00115.60 N ANISOU 1311 ND2 ASN A 174 18513 18304 7106 -459 -492 276 N ATOM 1312 N THR A 175 -18.579 -12.867 -86.826 1.00105.77 N ANISOU 1312 N THR A 175 15350 18160 6679 -339 -1390 865 N ATOM 1313 CA THR A 175 -20.009 -12.661 -86.634 1.00106.36 C ANISOU 1313 CA THR A 175 15105 18627 6679 -519 -1762 956 C ATOM 1314 C THR A 175 -20.393 -11.195 -86.470 1.00102.79 C ANISOU 1314 C THR A 175 14217 18381 6460 -243 -1828 1207 C ATOM 1315 O THR A 175 -21.565 -10.906 -86.199 1.00103.67 O ANISOU 1315 O THR A 175 13998 18785 6605 -321 -2094 1309 O ATOM 1316 CB THR A 175 -20.505 -13.456 -85.419 1.00 90.81 C ANISOU 1316 CB THR A 175 12949 16684 4871 -729 -1869 810 C ATOM 1317 OG1 THR A 175 -19.782 -13.046 -84.251 1.00100.03 O ANISOU 1317 OG1 THR A 175 13868 17639 6499 -480 -1647 791 O ATOM 1318 CG2 THR A 175 -20.304 -14.948 -85.636 1.00 93.64 C ANISOU 1318 CG2 THR A 175 13767 16831 4979 -1031 -1840 567 C ATOM 1319 N ASN A 176 -19.446 -10.265 -86.624 1.00 99.55 N ANISOU 1319 N ASN A 176 13801 17771 6253 84 -1576 1313 N ATOM 1320 CA ASN A 176 -19.700 -8.833 -86.448 1.00 96.62 C ANISOU 1320 CA ASN A 176 13072 17526 6111 368 -1605 1548 C ATOM 1321 C ASN A 176 -20.283 -8.528 -85.071 1.00 95.30 C ANISOU 1321 C ASN A 176 12473 17454 6284 420 -1698 1556 C ATOM 1322 O ASN A 176 -21.038 -7.568 -84.901 1.00 92.85 O ANISOU 1322 O ASN A 176 11845 17371 6063 575 -1835 1746 O ATOM 1323 CB ASN A 176 -20.617 -8.289 -87.549 1.00112.27 C ANISOU 1323 CB ASN A 176 15038 19846 7772 351 -1843 1750 C ATOM 1324 CG ASN A 176 -20.029 -8.463 -88.935 1.00139.28 C ANISOU 1324 CG ASN A 176 18901 23173 10848 333 -1740 1761 C ATOM 1325 OD1 ASN A 176 -18.824 -8.314 -89.134 1.00134.92 O ANISOU 1325 OD1 ASN A 176 18556 22308 10400 504 -1432 1737 O ATOM 1326 ND2 ASN A 176 -20.880 -8.782 -89.903 1.00167.67 N ANISOU 1326 ND2 ASN A 176 22645 26932 14131 121 -1974 1778 N ATOM 1327 N ILE A 177 -19.934 -9.343 -84.078 1.00 92.79 N ANISOU 1327 N ILE A 177 12154 16958 6144 310 -1612 1357 N ATOM 1328 CA ILE A 177 -20.456 -9.223 -82.723 1.00 88.56 C ANISOU 1328 CA ILE A 177 11251 16497 5902 333 -1686 1337 C ATOM 1329 C ILE A 177 -19.365 -8.643 -81.836 1.00 88.67 C ANISOU 1329 C ILE A 177 11190 16180 6319 585 -1422 1313 C ATOM 1330 O ILE A 177 -18.237 -9.151 -81.812 1.00 77.44 O ANISOU 1330 O ILE A 177 10004 14455 4964 579 -1198 1189 O ATOM 1331 CB ILE A 177 -20.943 -10.580 -82.185 1.00 93.67 C ANISOU 1331 CB ILE A 177 11940 17206 6446 -1 -1808 1142 C ATOM 1332 CG1 ILE A 177 -22.145 -11.073 -82.995 1.00 96.35 C ANISOU 1332 CG1 ILE A 177 12308 17911 6390 -290 -2120 1194 C ATOM 1333 CG2 ILE A 177 -21.302 -10.476 -80.713 1.00 79.56 C ANISOU 1333 CG2 ILE A 177 9796 15448 4983 51 -1830 1113 C ATOM 1334 CD1 ILE A 177 -22.675 -12.416 -82.545 1.00102.96 C ANISOU 1334 CD1 ILE A 177 13216 18749 7154 -656 -2244 1006 C ATOM 1335 N THR A 178 -19.702 -7.580 -81.112 1.00 93.19 N ANISOU 1335 N THR A 178 11446 16812 7151 807 -1450 1442 N ATOM 1336 CA THR A 178 -18.766 -6.908 -80.218 1.00 75.06 C ANISOU 1336 CA THR A 178 9072 14217 5232 1026 -1243 1436 C ATOM 1337 C THR A 178 -18.847 -7.563 -78.843 1.00 72.86 C ANISOU 1337 C THR A 178 8648 13877 5157 929 -1246 1270 C ATOM 1338 O THR A 178 -19.865 -7.451 -78.151 1.00 83.18 O ANISOU 1338 O THR A 178 9692 15406 6507 925 -1405 1298 O ATOM 1339 CB THR A 178 -19.080 -5.417 -80.140 1.00 78.41 C ANISOU 1339 CB THR A 178 9294 14694 5803 1316 -1265 1651 C ATOM 1340 OG1 THR A 178 -18.753 -4.793 -81.389 1.00 95.97 O ANISOU 1340 OG1 THR A 178 11688 16906 7870 1420 -1214 1805 O ATOM 1341 CG2 THR A 178 -18.289 -4.760 -79.030 1.00 72.96 C ANISOU 1341 CG2 THR A 178 8518 13708 5494 1493 -1102 1629 C ATOM 1342 N VAL A 179 -17.779 -8.255 -78.451 1.00 73.27 N ANISOU 1342 N VAL A 179 8866 13643 5331 865 -1063 1113 N ATOM 1343 CA VAL A 179 -17.719 -8.939 -77.169 1.00 72.68 C ANISOU 1343 CA VAL A 179 8689 13482 5445 772 -1047 954 C ATOM 1344 C VAL A 179 -16.550 -8.381 -76.369 1.00 80.45 C ANISOU 1344 C VAL A 179 9643 14151 6774 949 -846 949 C ATOM 1345 O VAL A 179 -15.668 -7.699 -76.895 1.00 98.33 O ANISOU 1345 O VAL A 179 12006 16245 9110 1092 -701 1049 O ATOM 1346 CB VAL A 179 -17.580 -10.468 -77.322 1.00 69.23 C ANISOU 1346 CB VAL A 179 8484 13001 4819 498 -1034 765 C ATOM 1347 CG1 VAL A 179 -18.518 -10.987 -78.397 1.00 93.07 C ANISOU 1347 CG1 VAL A 179 11628 16287 7449 291 -1225 781 C ATOM 1348 CG2 VAL A 179 -16.139 -10.847 -77.633 1.00 68.45 C ANISOU 1348 CG2 VAL A 179 8658 12578 4774 544 -771 702 C ATOM 1349 N CYS A 180 -16.558 -8.682 -75.074 1.00 87.13 N ANISOU 1349 N CYS A 180 10348 14931 7826 921 -847 842 N ATOM 1350 CA CYS A 180 -15.441 -8.394 -74.187 1.00 95.87 C ANISOU 1350 CA CYS A 180 11437 15746 9244 1024 -684 811 C ATOM 1351 C CYS A 180 -14.891 -9.714 -73.669 1.00 77.35 C ANISOU 1351 C CYS A 180 9199 13272 6919 856 -599 634 C ATOM 1352 O CYS A 180 -15.657 -10.572 -73.218 1.00 66.72 O ANISOU 1352 O CYS A 180 7811 12060 5479 693 -710 520 O ATOM 1353 CB CYS A 180 -15.865 -7.503 -73.022 1.00106.90 C ANISOU 1353 CB CYS A 180 12599 17149 10870 1166 -753 847 C ATOM 1354 SG CYS A 180 -14.510 -7.134 -71.899 1.00 89.31 S ANISOU 1354 SG CYS A 180 10366 14568 9001 1248 -595 811 S ATOM 1355 N ALA A 181 -13.572 -9.873 -73.728 1.00 76.20 N ANISOU 1355 N ALA A 181 9183 12873 6898 898 -398 629 N ATOM 1356 CA ALA A 181 -12.979 -11.180 -73.481 1.00 75.82 C ANISOU 1356 CA ALA A 181 9284 12697 6826 769 -286 486 C ATOM 1357 C ALA A 181 -11.473 -11.039 -73.316 1.00 74.89 C ANISOU 1357 C ALA A 181 9208 12317 6928 880 -62 542 C ATOM 1358 O ALA A 181 -10.899 -9.966 -73.514 1.00 71.91 O ANISOU 1358 O ALA A 181 8765 11862 6696 1021 -2 690 O ATOM 1359 CB ALA A 181 -13.292 -12.144 -74.626 1.00 75.12 C ANISOU 1359 CB ALA A 181 9464 12690 6388 624 -286 424 C ATOM 1360 N PHE A 182 -10.846 -12.149 -72.932 1.00 78.63 N ANISOU 1360 N PHE A 182 9789 12661 7426 809 60 436 N ATOM 1361 CA PHE A 182 -9.419 -12.351 -73.131 1.00 73.29 C ANISOU 1361 CA PHE A 182 9204 11778 6865 903 305 505 C ATOM 1362 C PHE A 182 -9.223 -13.000 -74.495 1.00 73.25 C ANISOU 1362 C PHE A 182 9502 11768 6563 896 441 506 C ATOM 1363 O PHE A 182 -9.916 -13.965 -74.831 1.00 81.26 O ANISOU 1363 O PHE A 182 10712 12849 7314 754 381 369 O ATOM 1364 CB PHE A 182 -8.821 -13.245 -72.044 1.00 75.38 C ANISOU 1364 CB PHE A 182 9439 11909 7294 864 385 411 C ATOM 1365 CG PHE A 182 -8.849 -12.648 -70.665 1.00 75.71 C ANISOU 1365 CG PHE A 182 9217 11928 7620 874 271 410 C ATOM 1366 CD1 PHE A 182 -7.899 -11.718 -70.276 1.00 76.37 C ANISOU 1366 CD1 PHE A 182 9151 11893 7971 980 331 552 C ATOM 1367 CD2 PHE A 182 -9.808 -13.043 -69.746 1.00 79.09 C ANISOU 1367 CD2 PHE A 182 9563 12451 8039 766 107 272 C ATOM 1368 CE1 PHE A 182 -7.917 -11.178 -69.003 1.00 77.77 C ANISOU 1368 CE1 PHE A 182 9137 12031 8382 975 217 540 C ATOM 1369 CE2 PHE A 182 -9.830 -12.508 -68.472 1.00 81.68 C ANISOU 1369 CE2 PHE A 182 9683 12749 8603 788 16 266 C ATOM 1370 CZ PHE A 182 -8.883 -11.576 -68.099 1.00 68.82 C ANISOU 1370 CZ PHE A 182 7943 10984 7221 892 67 391 C ATOM 1371 N HIS A 183 -8.289 -12.471 -75.279 1.00 61.67 N ANISOU 1371 N HIS A 183 8091 10217 5125 1037 623 665 N ATOM 1372 CA HIS A 183 -7.997 -13.003 -76.605 1.00 64.38 C ANISOU 1372 CA HIS A 183 8744 10539 5179 1067 788 685 C ATOM 1373 C HIS A 183 -6.783 -13.919 -76.503 1.00 64.15 C ANISOU 1373 C HIS A 183 8846 10319 5209 1148 1069 687 C ATOM 1374 O HIS A 183 -5.657 -13.449 -76.313 1.00 87.27 O ANISOU 1374 O HIS A 183 11631 13149 8381 1287 1240 849 O ATOM 1375 CB HIS A 183 -7.756 -11.880 -77.610 1.00 73.08 C ANISOU 1375 CB HIS A 183 9840 11683 6246 1190 836 878 C ATOM 1376 CG HIS A 183 -7.646 -12.355 -79.026 1.00 70.70 C ANISOU 1376 CG HIS A 183 9877 11388 5597 1217 977 893 C ATOM 1377 ND1 HIS A 183 -6.832 -11.745 -79.956 1.00 79.00 N ANISOU 1377 ND1 HIS A 183 10993 12394 6631 1373 1174 1085 N ATOM 1378 CD2 HIS A 183 -8.249 -13.382 -79.670 1.00 73.53 C ANISOU 1378 CD2 HIS A 183 10553 11787 5596 1097 947 742 C ATOM 1379 CE1 HIS A 183 -6.936 -12.378 -81.111 1.00 71.46 C ANISOU 1379 CE1 HIS A 183 10388 11451 5312 1369 1271 1045 C ATOM 1380 NE2 HIS A 183 -7.791 -13.374 -80.965 1.00 71.61 N ANISOU 1380 NE2 HIS A 183 10580 11515 5113 1195 1129 832 N ATOM 1381 N TYR A 184 -7.014 -15.227 -76.631 1.00 64.95 N ANISOU 1381 N TYR A 184 9223 10371 5083 1058 1117 521 N ATOM 1382 CA TYR A 184 -5.941 -16.219 -76.558 1.00 65.56 C ANISOU 1382 CA TYR A 184 9469 10260 5179 1161 1401 517 C ATOM 1383 C TYR A 184 -5.277 -16.308 -77.929 1.00 69.35 C ANISOU 1383 C TYR A 184 10235 10682 5434 1310 1659 623 C ATOM 1384 O TYR A 184 -5.470 -17.254 -78.696 1.00 70.14 O ANISOU 1384 O TYR A 184 10733 10721 5196 1279 1752 510 O ATOM 1385 CB TYR A 184 -6.477 -17.572 -76.105 1.00 65.58 C ANISOU 1385 CB TYR A 184 9690 10202 5024 1009 1353 296 C ATOM 1386 CG TYR A 184 -6.996 -17.606 -74.683 1.00 80.42 C ANISOU 1386 CG TYR A 184 11296 12126 7133 885 1146 204 C ATOM 1387 CD1 TYR A 184 -6.846 -16.515 -73.836 1.00 61.18 C ANISOU 1387 CD1 TYR A 184 8469 9749 5027 933 1040 311 C ATOM 1388 CD2 TYR A 184 -7.629 -18.737 -74.184 1.00 63.11 C ANISOU 1388 CD2 TYR A 184 9263 9902 4813 713 1063 13 C ATOM 1389 CE1 TYR A 184 -7.319 -16.547 -72.537 1.00 59.19 C ANISOU 1389 CE1 TYR A 184 7998 9532 4960 834 865 226 C ATOM 1390 CE2 TYR A 184 -8.102 -18.779 -72.887 1.00 73.87 C ANISOU 1390 CE2 TYR A 184 10380 11313 6375 608 890 -60 C ATOM 1391 CZ TYR A 184 -7.945 -17.682 -72.068 1.00 71.38 C ANISOU 1391 CZ TYR A 184 9682 11063 6376 679 797 45 C ATOM 1392 OH TYR A 184 -8.416 -17.720 -70.776 1.00 68.51 O ANISOU 1392 OH TYR A 184 9101 10742 6187 588 637 -29 O ATOM 1393 N GLU A 185 -4.475 -15.290 -78.234 1.00 73.80 N ANISOU 1393 N GLU A 185 10608 11254 6178 1469 1780 849 N ATOM 1394 CA GLU A 185 -3.813 -15.216 -79.529 1.00 79.81 C ANISOU 1394 CA GLU A 185 11598 11980 6746 1630 2038 988 C ATOM 1395 C GLU A 185 -2.827 -16.367 -79.690 1.00 76.10 C ANISOU 1395 C GLU A 185 11371 11340 6202 1785 2379 993 C ATOM 1396 O GLU A 185 -2.176 -16.789 -78.730 1.00 71.25 O ANISOU 1396 O GLU A 185 10593 10641 5837 1838 2469 1012 O ATOM 1397 CB GLU A 185 -3.100 -13.870 -79.670 1.00 81.92 C ANISOU 1397 CB GLU A 185 11566 12288 7270 1752 2097 1254 C ATOM 1398 CG GLU A 185 -2.663 -13.520 -81.080 1.00102.38 C ANISOU 1398 CG GLU A 185 14359 14892 9647 1895 2306 1415 C ATOM 1399 CD GLU A 185 -2.189 -12.084 -81.191 1.00119.72 C ANISOU 1399 CD GLU A 185 16258 17142 12089 1961 2300 1670 C ATOM 1400 OE1 GLU A 185 -2.513 -11.281 -80.290 1.00124.76 O ANISOU 1400 OE1 GLU A 185 16591 17816 12996 1865 2068 1679 O ATOM 1401 OE2 GLU A 185 -1.492 -11.757 -82.174 1.00124.88 O ANISOU 1401 OE2 GLU A 185 17002 17789 12659 2108 2534 1864 O ATOM 1402 N SER A 186 -2.725 -16.879 -80.919 1.00 93.66 N ANISOU 1402 N SER A 186 14007 13515 8067 1870 2575 981 N ATOM 1403 CA SER A 186 -1.917 -18.070 -81.168 1.00101.56 C ANISOU 1403 CA SER A 186 15327 14334 8927 2038 2916 963 C ATOM 1404 C SER A 186 -0.441 -17.808 -80.891 1.00105.16 C ANISOU 1404 C SER A 186 15514 14742 9700 2299 3229 1235 C ATOM 1405 O SER A 186 0.229 -18.609 -80.229 1.00119.60 O ANISOU 1405 O SER A 186 17327 16458 11658 2407 3405 1243 O ATOM 1406 CB SER A 186 -2.120 -18.550 -82.605 1.00115.81 C ANISOU 1406 CB SER A 186 17660 16090 10252 2085 3064 903 C ATOM 1407 OG SER A 186 -1.337 -19.700 -82.874 1.00121.51 O ANISOU 1407 OG SER A 186 18743 16612 10815 2281 3423 886 O ATOM 1408 N GLN A 187 0.085 -16.692 -81.390 1.00 82.89 N ANISOU 1408 N GLN A 187 12471 12016 7007 2399 3300 1480 N ATOM 1409 CA GLN A 187 1.484 -16.346 -81.190 1.00 85.84 C ANISOU 1409 CA GLN A 187 12550 12380 7686 2615 3579 1780 C ATOM 1410 C GLN A 187 1.611 -14.859 -80.900 1.00101.62 C ANISOU 1410 C GLN A 187 14107 14504 10001 2537 3401 1976 C ATOM 1411 O GLN A 187 0.762 -14.057 -81.300 1.00100.07 O ANISOU 1411 O GLN A 187 13922 14392 9707 2406 3168 1926 O ATOM 1412 CB GLN A 187 2.344 -16.715 -82.407 1.00 83.72 C ANISOU 1412 CB GLN A 187 12571 12057 7181 2891 4004 1946 C ATOM 1413 CG GLN A 187 2.552 -18.207 -82.593 1.00 93.31 C ANISOU 1413 CG GLN A 187 14221 13102 8131 3038 4267 1807 C ATOM 1414 CD GLN A 187 3.578 -18.523 -83.662 1.00 93.20 C ANISOU 1414 CD GLN A 187 14450 13031 7932 3369 4739 2015 C ATOM 1415 OE1 GLN A 187 3.946 -17.661 -84.460 1.00104.34 O ANISOU 1415 OE1 GLN A 187 15770 14539 9336 3455 4844 2229 O ATOM 1416 NE2 GLN A 187 4.050 -19.762 -83.679 1.00102.42 N ANISOU 1416 NE2 GLN A 187 15886 13999 9032 3518 4942 1934 N ATOM 1417 N ASN A 188 2.689 -14.504 -80.196 1.00104.54 N ANISOU 1417 N ASN A 188 14097 14881 10744 2616 3509 2210 N ATOM 1418 CA ASN A 188 3.007 -13.114 -79.865 1.00100.46 C ANISOU 1418 CA ASN A 188 13175 14447 10549 2535 3366 2425 C ATOM 1419 C ASN A 188 1.874 -12.452 -79.083 1.00 92.54 C ANISOU 1419 C ASN A 188 12042 13479 9641 2288 2942 2235 C ATOM 1420 O ASN A 188 1.495 -11.310 -79.348 1.00 94.74 O ANISOU 1420 O ASN A 188 12221 13814 9960 2209 2777 2305 O ATOM 1421 CB ASN A 188 3.343 -12.308 -81.122 1.00 98.35 C ANISOU 1421 CB ASN A 188 12967 14237 10165 2637 3529 2647 C ATOM 1422 N SER A 189 1.329 -13.176 -78.109 1.00 99.45 N ANISOU 1422 N SER A 189 12926 14317 10545 2183 2779 2006 N ATOM 1423 CA SER A 189 0.260 -12.658 -77.268 1.00107.54 C ANISOU 1423 CA SER A 189 13823 15381 11658 1975 2404 1829 C ATOM 1424 C SER A 189 0.850 -12.055 -76.000 1.00115.19 C ANISOU 1424 C SER A 189 14402 16332 13033 1909 2290 1943 C ATOM 1425 O SER A 189 1.668 -12.689 -75.325 1.00121.16 O ANISOU 1425 O SER A 189 15040 17042 13955 1962 2416 2002 O ATOM 1426 CB SER A 189 -0.737 -13.763 -76.915 1.00111.68 C ANISOU 1426 CB SER A 189 14577 15886 11971 1875 2278 1522 C ATOM 1427 OG SER A 189 -0.123 -14.777 -76.141 1.00119.16 O ANISOU 1427 OG SER A 189 15504 16745 13027 1926 2409 1490 O ATOM 1428 N THR A 190 0.434 -10.829 -75.681 1.00110.20 N ANISOU 1428 N THR A 190 13592 15731 12547 1795 2051 1979 N ATOM 1429 CA THR A 190 0.902 -10.153 -74.478 1.00105.25 C ANISOU 1429 CA THR A 190 12646 15069 12275 1700 1905 2069 C ATOM 1430 C THR A 190 0.226 -10.661 -73.212 1.00103.78 C ANISOU 1430 C THR A 190 12415 14866 12151 1585 1690 1833 C ATOM 1431 O THR A 190 0.621 -10.254 -72.113 1.00 96.42 O ANISOU 1431 O THR A 190 11250 13896 11491 1503 1567 1884 O ATOM 1432 CB THR A 190 0.683 -8.643 -74.603 1.00 96.51 C ANISOU 1432 CB THR A 190 11428 13965 11278 1627 1737 2185 C ATOM 1433 OG1 THR A 190 -0.702 -8.379 -74.860 1.00 99.08 O ANISOU 1433 OG1 THR A 190 11912 14340 11394 1583 1536 1991 O ATOM 1434 CG2 THR A 190 1.522 -8.075 -75.738 1.00 81.65 C ANISOU 1434 CG2 THR A 190 9545 12094 9384 1727 1959 2463 C ATOM 1435 N LEU A 191 -0.771 -11.530 -73.337 1.00 98.20 N ANISOU 1435 N LEU A 191 11931 14187 11192 1562 1635 1588 N ATOM 1436 CA LEU A 191 -1.464 -12.095 -72.188 1.00 94.01 C ANISOU 1436 CA LEU A 191 11371 13653 10697 1453 1450 1370 C ATOM 1437 C LEU A 191 -0.623 -13.208 -71.564 1.00 90.67 C ANISOU 1437 C LEU A 191 10921 13161 10369 1504 1612 1378 C ATOM 1438 O LEU A 191 -0.025 -14.011 -72.285 1.00 92.96 O ANISOU 1438 O LEU A 191 11371 13418 10532 1635 1876 1437 O ATOM 1439 CB LEU A 191 -2.826 -12.645 -72.610 1.00 96.74 C ANISOU 1439 CB LEU A 191 11957 14070 10731 1385 1333 1135 C ATOM 1440 CG LEU A 191 -3.726 -13.301 -71.561 1.00101.55 C ANISOU 1440 CG LEU A 191 12560 14700 11325 1258 1144 906 C ATOM 1441 CD1 LEU A 191 -4.313 -12.270 -70.613 1.00 98.19 C ANISOU 1441 CD1 LEU A 191 11912 14315 11080 1180 888 885 C ATOM 1442 CD2 LEU A 191 -4.830 -14.085 -72.243 1.00106.67 C ANISOU 1442 CD2 LEU A 191 13478 15422 11628 1184 1093 721 C ATOM 1443 N PRO A 192 -0.547 -13.270 -70.233 1.00 84.84 N ANISOU 1443 N PRO A 192 9997 12397 9843 1422 1472 1330 N ATOM 1444 CA PRO A 192 0.175 -14.374 -69.591 1.00 79.69 C ANISOU 1444 CA PRO A 192 9321 11688 9271 1478 1613 1337 C ATOM 1445 C PRO A 192 -0.442 -15.720 -69.943 1.00 81.58 C ANISOU 1445 C PRO A 192 9874 11896 9227 1500 1706 1132 C ATOM 1446 O PRO A 192 -1.651 -15.841 -70.155 1.00 88.93 O ANISOU 1446 O PRO A 192 10973 12869 9949 1393 1553 930 O ATOM 1447 CB PRO A 192 0.043 -14.067 -68.093 1.00 83.66 C ANISOU 1447 CB PRO A 192 9601 12183 10004 1350 1377 1281 C ATOM 1448 CG PRO A 192 -1.089 -13.089 -67.989 1.00 79.19 C ANISOU 1448 CG PRO A 192 9031 11662 9394 1235 1119 1162 C ATOM 1449 CD PRO A 192 -1.040 -12.291 -69.252 1.00 76.98 C ANISOU 1449 CD PRO A 192 8813 11412 9022 1294 1194 1288 C ATOM 1450 N ILE A 193 0.415 -16.740 -70.002 1.00 86.68 N ANISOU 1450 N ILE A 193 10602 12469 9863 1639 1960 1200 N ATOM 1451 CA ILE A 193 -0.016 -18.058 -70.461 1.00 98.73 C ANISOU 1451 CA ILE A 193 12494 13921 11100 1675 2093 1025 C ATOM 1452 C ILE A 193 -0.963 -18.694 -69.450 1.00 91.89 C ANISOU 1452 C ILE A 193 11674 13040 10202 1508 1882 784 C ATOM 1453 O ILE A 193 -2.084 -19.091 -69.786 1.00 97.61 O ANISOU 1453 O ILE A 193 12635 13779 10674 1382 1769 577 O ATOM 1454 CB ILE A 193 1.202 -18.958 -70.733 1.00109.04 C ANISOU 1454 CB ILE A 193 13886 15132 12412 1907 2448 1181 C ATOM 1455 N GLY A 194 -0.524 -18.805 -68.200 1.00 92.26 N ANISOU 1455 N GLY A 194 11489 13069 10497 1495 1822 823 N ATOM 1456 CA GLY A 194 -1.308 -19.491 -67.193 1.00101.12 C ANISOU 1456 CA GLY A 194 12655 14171 11596 1356 1657 618 C ATOM 1457 C GLY A 194 -2.082 -18.578 -66.266 1.00107.57 C ANISOU 1457 C GLY A 194 13236 15084 12550 1189 1343 542 C ATOM 1458 O GLY A 194 -1.965 -18.689 -65.042 1.00115.80 O ANISOU 1458 O GLY A 194 14115 16116 13767 1141 1241 526 O ATOM 1459 N LEU A 195 -2.880 -17.668 -66.832 1.00109.81 N ANISOU 1459 N LEU A 195 13515 15461 12746 1115 1196 503 N ATOM 1460 CA LEU A 195 -3.720 -16.821 -65.992 1.00112.06 C ANISOU 1460 CA LEU A 195 13617 15832 13130 989 920 426 C ATOM 1461 C LEU A 195 -4.831 -17.626 -65.330 1.00120.48 C ANISOU 1461 C LEU A 195 14776 16933 14069 852 784 209 C ATOM 1462 O LEU A 195 -5.305 -17.254 -64.251 1.00133.57 O ANISOU 1462 O LEU A 195 16271 18635 15845 777 602 151 O ATOM 1463 CB LEU A 195 -4.310 -15.666 -66.806 1.00113.94 C ANISOU 1463 CB LEU A 195 13836 16161 13295 978 817 459 C ATOM 1464 CG LEU A 195 -5.564 -15.915 -67.648 1.00112.59 C ANISOU 1464 CG LEU A 195 13866 16091 12824 898 738 317 C ATOM 1465 CD1 LEU A 195 -6.197 -14.596 -68.059 1.00108.73 C ANISOU 1465 CD1 LEU A 195 13276 15710 12328 897 586 370 C ATOM 1466 CD2 LEU A 195 -5.245 -16.752 -68.874 1.00110.92 C ANISOU 1466 CD2 LEU A 195 13941 15828 12377 954 951 322 C ATOM 1467 N GLY A 196 -5.256 -18.727 -65.956 1.00102.11 N ANISOU 1467 N GLY A 196 12726 14580 11490 811 872 93 N ATOM 1468 CA GLY A 196 -6.223 -19.609 -65.331 1.00 87.88 C ANISOU 1468 CA GLY A 196 11021 12802 9569 656 757 -92 C ATOM 1469 C GLY A 196 -5.640 -20.520 -64.275 1.00 73.70 C ANISOU 1469 C GLY A 196 9215 10890 7897 676 835 -108 C ATOM 1470 O GLY A 196 -6.375 -20.980 -63.395 1.00 71.32 O ANISOU 1470 O GLY A 196 8897 10620 7582 547 705 -232 O ATOM 1471 N LEU A 197 -4.335 -20.793 -64.343 1.00 71.92 N ANISOU 1471 N LEU A 197 8989 10546 7792 843 1050 34 N ATOM 1472 CA LEU A 197 -3.693 -21.582 -63.299 1.00 70.34 C ANISOU 1472 CA LEU A 197 8745 10250 7730 889 1122 56 C ATOM 1473 C LEU A 197 -3.629 -20.819 -61.983 1.00 79.87 C ANISOU 1473 C LEU A 197 9634 11523 9191 843 932 94 C ATOM 1474 O LEU A 197 -3.648 -21.435 -60.912 1.00 77.31 O ANISOU 1474 O LEU A 197 9277 11163 8933 803 890 44 O ATOM 1475 CB LEU A 197 -2.289 -22.000 -63.735 1.00 62.80 C ANISOU 1475 CB LEU A 197 7833 9184 6846 1107 1409 240 C ATOM 1476 CG LEU A 197 -2.193 -23.045 -64.847 1.00 62.07 C ANISOU 1476 CG LEU A 197 8127 8969 6486 1193 1654 196 C ATOM 1477 CD1 LEU A 197 -0.739 -23.392 -65.123 1.00 56.88 C ANISOU 1477 CD1 LEU A 197 7460 8220 5931 1457 1959 415 C ATOM 1478 CD2 LEU A 197 -2.984 -24.292 -64.481 1.00 55.35 C ANISOU 1478 CD2 LEU A 197 7559 8026 5446 1063 1625 -9 C ATOM 1479 N THR A 198 -3.555 -19.486 -62.041 1.00 81.30 N ANISOU 1479 N THR A 198 9608 11783 9501 847 816 183 N ATOM 1480 CA THR A 198 -3.531 -18.694 -60.816 1.00 73.07 C ANISOU 1480 CA THR A 198 8319 10778 8669 794 626 206 C ATOM 1481 C THR A 198 -4.832 -18.847 -60.037 1.00 63.59 C ANISOU 1481 C THR A 198 7136 9647 7377 656 437 13 C ATOM 1482 O THR A 198 -4.817 -18.963 -58.807 1.00 62.15 O ANISOU 1482 O THR A 198 6852 9456 7306 617 343 -16 O ATOM 1483 CB THR A 198 -3.269 -17.223 -61.143 1.00 77.49 C ANISOU 1483 CB THR A 198 8717 11376 9348 815 544 329 C ATOM 1484 OG1 THR A 198 -2.050 -17.108 -61.887 1.00 87.68 O ANISOU 1484 OG1 THR A 198 9971 12620 10724 934 732 532 O ATOM 1485 CG2 THR A 198 -3.151 -16.404 -59.866 1.00 76.76 C ANISOU 1485 CG2 THR A 198 8426 11285 9457 756 353 352 C ATOM 1486 N LYS A 199 -5.969 -18.854 -60.738 1.00 69.60 N ANISOU 1486 N LYS A 199 8018 10495 7931 581 379 -103 N ATOM 1487 CA LYS A 199 -7.240 -19.122 -60.077 1.00 60.80 C ANISOU 1487 CA LYS A 199 6907 9478 6715 449 221 -260 C ATOM 1488 C LYS A 199 -7.325 -20.548 -59.551 1.00 71.89 C ANISOU 1488 C LYS A 199 8453 10817 8046 377 286 -353 C ATOM 1489 O LYS A 199 -8.097 -20.807 -58.622 1.00 82.83 O ANISOU 1489 O LYS A 199 9791 12265 9418 276 168 -448 O ATOM 1490 CB LYS A 199 -8.408 -18.852 -61.029 1.00 56.03 C ANISOU 1490 CB LYS A 199 6378 9013 5899 374 140 -328 C ATOM 1491 CG LYS A 199 -8.656 -17.378 -61.317 1.00 60.53 C ANISOU 1491 CG LYS A 199 6797 9669 6531 439 34 -253 C ATOM 1492 CD LYS A 199 -9.997 -17.153 -62.002 1.00 75.25 C ANISOU 1492 CD LYS A 199 8690 11714 8188 363 -81 -314 C ATOM 1493 CE LYS A 199 -10.043 -17.801 -63.375 1.00110.38 C ANISOU 1493 CE LYS A 199 13361 16164 12413 318 14 -326 C ATOM 1494 NZ LYS A 199 -11.365 -17.606 -64.036 1.00127.57 N ANISOU 1494 NZ LYS A 199 15550 18545 14377 218 -127 -367 N ATOM 1495 N ASN A 200 -6.548 -21.475 -60.115 1.00 69.69 N ANISOU 1495 N ASN A 200 8360 10407 7713 440 486 -318 N ATOM 1496 CA ASN A 200 -6.605 -22.864 -59.672 1.00 64.48 C ANISOU 1496 CA ASN A 200 7883 9650 6968 383 565 -401 C ATOM 1497 C ASN A 200 -5.910 -23.044 -58.327 1.00 58.17 C ANISOU 1497 C ASN A 200 6930 8793 6379 440 562 -342 C ATOM 1498 O ASN A 200 -6.508 -23.544 -57.368 1.00 69.95 O ANISOU 1498 O ASN A 200 8417 10304 7857 335 471 -435 O ATOM 1499 CB ASN A 200 -5.981 -23.779 -60.728 1.00 61.77 C ANISOU 1499 CB ASN A 200 7831 9160 6480 467 803 -378 C ATOM 1500 CG ASN A 200 -6.848 -23.921 -61.963 1.00 62.49 C ANISOU 1500 CG ASN A 200 8155 9293 6294 355 785 -478 C ATOM 1501 OD1 ASN A 200 -8.072 -23.823 -61.891 1.00 65.75 O ANISOU 1501 OD1 ASN A 200 8555 9839 6587 168 598 -590 O ATOM 1502 ND2 ASN A 200 -6.214 -24.156 -63.106 1.00 76.36 N ANISOU 1502 ND2 ASN A 200 10123 10950 7938 472 982 -422 N ATOM 1503 N ILE A 201 -4.647 -22.639 -58.235 1.00 61.03 N ANISOU 1503 N ILE A 201 7155 9099 6934 596 654 -173 N ATOM 1504 CA ILE A 201 -3.861 -22.880 -57.028 1.00 62.32 C ANISOU 1504 CA ILE A 201 7177 9214 7287 650 653 -88 C ATOM 1505 C ILE A 201 -4.048 -21.765 -56.006 1.00 72.07 C ANISOU 1505 C ILE A 201 8162 10542 8680 590 429 -79 C ATOM 1506 O ILE A 201 -4.344 -22.025 -54.837 1.00 90.07 O ANISOU 1506 O ILE A 201 10393 12833 10997 527 326 -138 O ATOM 1507 CB ILE A 201 -2.373 -23.081 -57.392 1.00 70.24 C ANISOU 1507 CB ILE A 201 8140 10133 8416 842 861 121 C ATOM 1508 CG1 ILE A 201 -1.515 -23.120 -56.127 1.00 84.53 C ANISOU 1508 CG1 ILE A 201 9741 11934 10440 887 817 247 C ATOM 1509 CG2 ILE A 201 -1.887 -22.003 -58.354 1.00 68.83 C ANISOU 1509 CG2 ILE A 201 7854 10001 8296 910 893 249 C ATOM 1510 N LEU A 202 -3.886 -20.506 -56.419 1.00 65.78 N ANISOU 1510 N LEU A 202 7231 9798 7964 611 356 -5 N ATOM 1511 CA LEU A 202 -4.019 -19.404 -55.473 1.00 69.47 C ANISOU 1511 CA LEU A 202 7517 10315 8564 561 153 2 C ATOM 1512 C LEU A 202 -5.475 -19.143 -55.114 1.00 68.81 C ANISOU 1512 C LEU A 202 7467 10326 8353 462 2 -173 C ATOM 1513 O LEU A 202 -5.765 -18.673 -54.008 1.00 82.26 O ANISOU 1513 O LEU A 202 9082 12053 10119 425 -143 -212 O ATOM 1514 CB LEU A 202 -3.375 -18.139 -56.046 1.00 78.25 C ANISOU 1514 CB LEU A 202 8508 11427 9797 606 128 145 C ATOM 1515 CG LEU A 202 -3.448 -16.870 -55.193 1.00 79.68 C ANISOU 1515 CG LEU A 202 8558 11617 10100 551 -79 157 C ATOM 1516 CD1 LEU A 202 -2.780 -17.087 -53.843 1.00 82.94 C ANISOU 1516 CD1 LEU A 202 8873 11990 10651 517 -160 205 C ATOM 1517 CD2 LEU A 202 -2.824 -15.690 -55.922 1.00 77.95 C ANISOU 1517 CD2 LEU A 202 8261 11376 9982 578 -87 305 C ATOM 1518 N GLY A 203 -6.400 -19.453 -56.017 1.00 63.67 N ANISOU 1518 N GLY A 203 6942 9738 7512 421 34 -268 N ATOM 1519 CA GLY A 203 -7.801 -19.167 -55.785 1.00 46.52 C ANISOU 1519 CA GLY A 203 4759 7697 5218 336 -103 -394 C ATOM 1520 C GLY A 203 -8.605 -20.338 -55.260 1.00 47.64 C ANISOU 1520 C GLY A 203 4992 7877 5231 224 -107 -514 C ATOM 1521 O GLY A 203 -9.760 -20.166 -54.861 1.00 50.13 O ANISOU 1521 O GLY A 203 5258 8325 5462 150 -221 -596 O ATOM 1522 N PHE A 204 -8.017 -21.535 -55.253 1.00 43.42 N ANISOU 1522 N PHE A 204 4591 7229 4679 215 25 -512 N ATOM 1523 CA PHE A 204 -8.746 -22.707 -54.785 1.00 56.40 C ANISOU 1523 CA PHE A 204 6355 8882 6194 88 28 -620 C ATOM 1524 C PHE A 204 -7.854 -23.697 -54.046 1.00 55.86 C ANISOU 1524 C PHE A 204 6355 8665 6206 131 135 -582 C ATOM 1525 O PHE A 204 -8.110 -24.010 -52.880 1.00 60.99 O ANISOU 1525 O PHE A 204 6954 9329 6890 83 70 -617 O ATOM 1526 CB PHE A 204 -9.436 -23.412 -55.954 1.00 44.80 C ANISOU 1526 CB PHE A 204 5095 7433 4496 -23 80 -694 C ATOM 1527 CG PHE A 204 -10.195 -24.643 -55.549 1.00 63.77 C ANISOU 1527 CG PHE A 204 7647 9830 6754 -195 74 -797 C ATOM 1528 CD1 PHE A 204 -11.449 -24.539 -54.971 1.00 63.11 C ANISOU 1528 CD1 PHE A 204 7455 9923 6601 -339 -76 -863 C ATOM 1529 CD2 PHE A 204 -9.653 -25.904 -55.740 1.00 58.20 C ANISOU 1529 CD2 PHE A 204 7196 8938 5978 -206 231 -813 C ATOM 1530 CE1 PHE A 204 -12.150 -25.667 -54.594 1.00 65.77 C ANISOU 1530 CE1 PHE A 204 7918 10262 6808 -524 -86 -939 C ATOM 1531 CE2 PHE A 204 -10.349 -27.036 -55.364 1.00 63.77 C ANISOU 1531 CE2 PHE A 204 8068 9615 6546 -385 222 -903 C ATOM 1532 CZ PHE A 204 -11.600 -26.917 -54.790 1.00 63.83 C ANISOU 1532 CZ PHE A 204 7950 9811 6494 -561 56 -965 C ATOM 1533 N LEU A 205 -6.813 -24.200 -54.715 1.00 55.60 N ANISOU 1533 N LEU A 205 6437 8494 6194 239 312 -498 N ATOM 1534 CA LEU A 205 -6.017 -25.292 -54.159 1.00 60.63 C ANISOU 1534 CA LEU A 205 7170 8988 6877 304 445 -448 C ATOM 1535 C LEU A 205 -5.402 -24.909 -52.817 1.00 62.67 C ANISOU 1535 C LEU A 205 7213 9261 7338 359 357 -363 C ATOM 1536 O LEU A 205 -5.682 -25.537 -51.790 1.00 68.46 O ANISOU 1536 O LEU A 205 7966 9982 8064 301 316 -409 O ATOM 1537 CB LEU A 205 -4.930 -25.707 -55.152 1.00 70.43 C ANISOU 1537 CB LEU A 205 8542 10098 8120 465 670 -336 C ATOM 1538 CG LEU A 205 -3.901 -26.720 -54.644 1.00 93.65 C ANISOU 1538 CG LEU A 205 11554 12894 11135 602 840 -231 C ATOM 1539 CD1 LEU A 205 -4.563 -28.051 -54.318 1.00 97.62 C ANISOU 1539 CD1 LEU A 205 12326 13294 11472 497 887 -359 C ATOM 1540 CD2 LEU A 205 -2.779 -26.903 -55.656 1.00102.22 C ANISOU 1540 CD2 LEU A 205 12718 13883 12239 808 1079 -82 C ATOM 1541 N PHE A 206 -4.553 -23.881 -52.809 1.00 60.30 N ANISOU 1541 N PHE A 206 6717 8985 7210 454 319 -232 N ATOM 1542 CA PHE A 206 -3.902 -23.472 -51.565 1.00 65.62 C ANISOU 1542 CA PHE A 206 7201 9670 8062 480 210 -141 C ATOM 1543 C PHE A 206 -4.891 -23.070 -50.477 1.00 77.65 C ANISOU 1543 C PHE A 206 8671 11279 9555 364 18 -266 C ATOM 1544 O PHE A 206 -4.743 -23.549 -49.339 1.00 94.27 O ANISOU 1544 O PHE A 206 10756 13364 11696 349 -24 -260 O ATOM 1545 CB PHE A 206 -2.901 -22.346 -51.848 1.00 62.21 C ANISOU 1545 CB PHE A 206 6581 9253 7803 554 178 24 C ATOM 1546 CG PHE A 206 -1.597 -22.821 -52.423 1.00 73.01 C ANISOU 1546 CG PHE A 206 7925 10554 9261 700 371 218 C ATOM 1547 CD1 PHE A 206 -1.323 -24.175 -52.533 1.00 70.31 C ANISOU 1547 CD1 PHE A 206 7742 10122 8850 787 563 234 C ATOM 1548 CD2 PHE A 206 -0.640 -21.912 -52.841 1.00 80.88 C ANISOU 1548 CD2 PHE A 206 8745 11576 10411 759 372 401 C ATOM 1549 CE1 PHE A 206 -0.122 -24.612 -53.059 1.00 73.11 C ANISOU 1549 CE1 PHE A 206 8075 10422 9282 965 770 432 C ATOM 1550 CE2 PHE A 206 0.564 -22.343 -53.366 1.00 77.78 C ANISOU 1550 CE2 PHE A 206 8298 11151 10104 912 568 611 C ATOM 1551 CZ PHE A 206 0.823 -23.695 -53.475 1.00 78.77 C ANISOU 1551 CZ PHE A 206 8578 11196 10156 1033 777 629 C ATOM 1552 N PRO A 207 -5.896 -22.222 -50.727 1.00 69.74 N ANISOU 1552 N PRO A 207 7643 10374 8479 299 -93 -365 N ATOM 1553 CA PRO A 207 -6.786 -21.843 -49.617 1.00 66.97 C ANISOU 1553 CA PRO A 207 7240 10107 8098 229 -247 -461 C ATOM 1554 C PRO A 207 -7.636 -22.991 -49.102 1.00 71.43 C ANISOU 1554 C PRO A 207 7910 10700 8530 137 -219 -564 C ATOM 1555 O PRO A 207 -7.856 -23.088 -47.888 1.00 82.83 O ANISOU 1555 O PRO A 207 9318 12166 9986 111 -295 -591 O ATOM 1556 CB PRO A 207 -7.645 -20.724 -50.221 1.00 64.54 C ANISOU 1556 CB PRO A 207 6888 9901 7732 221 -330 -515 C ATOM 1557 CG PRO A 207 -6.893 -20.251 -51.416 1.00 74.19 C ANISOU 1557 CG PRO A 207 8102 11074 9012 288 -259 -418 C ATOM 1558 CD PRO A 207 -6.217 -21.465 -51.950 1.00 77.33 C ANISOU 1558 CD PRO A 207 8609 11382 9390 311 -85 -371 C ATOM 1559 N PHE A 208 -8.129 -23.863 -49.987 1.00 61.34 N ANISOU 1559 N PHE A 208 6779 9414 7112 73 -116 -620 N ATOM 1560 CA PHE A 208 -8.933 -24.995 -49.535 1.00 62.59 C ANISOU 1560 CA PHE A 208 7056 9586 7140 -52 -94 -707 C ATOM 1561 C PHE A 208 -8.128 -25.913 -48.626 1.00 72.50 C ANISOU 1561 C PHE A 208 8368 10714 8464 -10 -25 -651 C ATOM 1562 O PHE A 208 -8.653 -26.431 -47.633 1.00 78.34 O ANISOU 1562 O PHE A 208 9123 11482 9162 -86 -65 -696 O ATOM 1563 CB PHE A 208 -9.478 -25.772 -50.734 1.00 54.34 C ANISOU 1563 CB PHE A 208 6202 8523 5920 -154 -6 -768 C ATOM 1564 CG PHE A 208 -10.117 -27.084 -50.372 1.00 53.59 C ANISOU 1564 CG PHE A 208 6279 8394 5691 -308 32 -839 C ATOM 1565 CD1 PHE A 208 -11.396 -27.126 -49.843 1.00 47.89 C ANISOU 1565 CD1 PHE A 208 5492 7833 4871 -467 -78 -910 C ATOM 1566 CD2 PHE A 208 -9.440 -28.278 -50.570 1.00 50.89 C ANISOU 1566 CD2 PHE A 208 6167 7853 5315 -289 189 -821 C ATOM 1567 CE1 PHE A 208 -11.986 -28.332 -49.512 1.00 46.52 C ANISOU 1567 CE1 PHE A 208 5474 7628 4575 -638 -49 -960 C ATOM 1568 CE2 PHE A 208 -10.024 -29.486 -50.240 1.00 50.36 C ANISOU 1568 CE2 PHE A 208 6293 7725 5117 -446 223 -884 C ATOM 1569 CZ PHE A 208 -11.299 -29.513 -49.710 1.00 49.14 C ANISOU 1569 CZ PHE A 208 6064 7735 4871 -638 96 -954 C ATOM 1570 N LEU A 209 -6.850 -26.125 -48.948 1.00 60.09 N ANISOU 1570 N LEU A 209 6819 9015 6999 121 87 -535 N ATOM 1571 CA LEU A 209 -6.001 -26.953 -48.099 1.00 60.52 C ANISOU 1571 CA LEU A 209 6903 8963 7130 192 154 -447 C ATOM 1572 C LEU A 209 -5.759 -26.304 -46.743 1.00 70.95 C ANISOU 1572 C LEU A 209 8042 10348 8568 205 -1 -404 C ATOM 1573 O LEU A 209 -5.514 -27.009 -45.758 1.00 83.88 O ANISOU 1573 O LEU A 209 9706 11943 10221 212 4 -371 O ATOM 1574 CB LEU A 209 -4.674 -27.234 -48.802 1.00 66.57 C ANISOU 1574 CB LEU A 209 7695 9612 7989 359 319 -296 C ATOM 1575 CG LEU A 209 -4.765 -28.117 -50.046 1.00 75.11 C ANISOU 1575 CG LEU A 209 9033 10578 8926 375 514 -334 C ATOM 1576 CD1 LEU A 209 -3.430 -28.166 -50.765 1.00 82.15 C ANISOU 1576 CD1 LEU A 209 9916 11382 9917 582 691 -161 C ATOM 1577 CD2 LEU A 209 -5.229 -29.517 -49.674 1.00 77.11 C ANISOU 1577 CD2 LEU A 209 9537 10719 9044 300 599 -409 C ATOM 1578 N ILE A 210 -5.818 -24.974 -46.670 1.00 67.04 N ANISOU 1578 N ILE A 210 7391 9941 8141 208 -141 -404 N ATOM 1579 CA ILE A 210 -5.711 -24.302 -45.380 1.00 61.90 C ANISOU 1579 CA ILE A 210 6625 9336 7560 200 -303 -390 C ATOM 1580 C ILE A 210 -7.043 -24.351 -44.642 1.00 59.45 C ANISOU 1580 C ILE A 210 6353 9120 7116 106 -377 -531 C ATOM 1581 O ILE A 210 -7.082 -24.535 -43.420 1.00 65.43 O ANISOU 1581 O ILE A 210 7105 9887 7868 91 -443 -534 O ATOM 1582 CB ILE A 210 -5.217 -22.856 -45.569 1.00 56.34 C ANISOU 1582 CB ILE A 210 5786 8654 6968 234 -421 -331 C ATOM 1583 CG1 ILE A 210 -3.898 -22.838 -46.343 1.00 48.99 C ANISOU 1583 CG1 ILE A 210 4786 7655 6173 320 -333 -161 C ATOM 1584 CG2 ILE A 210 -5.041 -22.174 -44.222 1.00 70.82 C ANISOU 1584 CG2 ILE A 210 7555 10503 8850 211 -597 -322 C ATOM 1585 CD1 ILE A 210 -3.358 -21.446 -46.601 1.00 64.35 C ANISOU 1585 CD1 ILE A 210 6604 9612 8234 324 -446 -83 C ATOM 1586 N ILE A 211 -8.152 -24.191 -45.368 1.00 64.32 N ANISOU 1586 N ILE A 211 6999 9823 7616 44 -364 -631 N ATOM 1587 CA ILE A 211 -9.470 -24.305 -44.750 1.00 61.89 C ANISOU 1587 CA ILE A 211 6697 9639 7178 -42 -412 -734 C ATOM 1588 C ILE A 211 -9.719 -25.734 -44.284 1.00 60.04 C ANISOU 1588 C ILE A 211 6581 9368 6865 -130 -330 -751 C ATOM 1589 O ILE A 211 -10.222 -25.961 -43.177 1.00 68.74 O ANISOU 1589 O ILE A 211 7675 10525 7920 -168 -371 -777 O ATOM 1590 CB ILE A 211 -10.560 -23.828 -45.728 1.00 58.51 C ANISOU 1590 CB ILE A 211 6243 9341 6648 -90 -422 -800 C ATOM 1591 CG1 ILE A 211 -10.380 -22.343 -46.050 1.00 56.28 C ANISOU 1591 CG1 ILE A 211 5859 9086 6439 11 -506 -779 C ATOM 1592 CG2 ILE A 211 -11.947 -24.086 -45.156 1.00 63.23 C ANISOU 1592 CG2 ILE A 211 6814 10100 7110 -185 -453 -870 C ATOM 1593 CD1 ILE A 211 -11.398 -21.801 -47.031 1.00 55.16 C ANISOU 1593 CD1 ILE A 211 5677 9080 6201 -7 -518 -819 C ATOM 1594 N LEU A 212 -9.366 -26.718 -45.115 1.00 56.75 N ANISOU 1594 N LEU A 212 6301 8841 6420 -158 -202 -733 N ATOM 1595 CA LEU A 212 -9.555 -28.114 -44.732 1.00 55.62 C ANISOU 1595 CA LEU A 212 6318 8620 6194 -244 -113 -746 C ATOM 1596 C LEU A 212 -8.685 -28.483 -43.537 1.00 63.24 C ANISOU 1596 C LEU A 212 7274 9502 7253 -158 -113 -661 C ATOM 1597 O LEU A 212 -9.127 -29.208 -42.639 1.00 62.84 O ANISOU 1597 O LEU A 212 7284 9454 7136 -229 -109 -679 O ATOM 1598 CB LEU A 212 -9.253 -29.030 -45.918 1.00 45.97 C ANISOU 1598 CB LEU A 212 5300 7258 4911 -266 35 -745 C ATOM 1599 CG LEU A 212 -9.276 -30.536 -45.648 1.00 55.49 C ANISOU 1599 CG LEU A 212 6737 8317 6028 -341 152 -749 C ATOM 1600 CD1 LEU A 212 -10.643 -30.975 -45.151 1.00 65.38 C ANISOU 1600 CD1 LEU A 212 8019 9682 7139 -557 88 -836 C ATOM 1601 CD2 LEU A 212 -8.881 -31.309 -46.896 1.00 53.71 C ANISOU 1601 CD2 LEU A 212 6760 7920 5728 -329 311 -752 C ATOM 1602 N THR A 213 -7.444 -27.991 -43.506 1.00 61.82 N ANISOU 1602 N THR A 213 7008 9259 7223 -14 -123 -552 N ATOM 1603 CA THR A 213 -6.561 -28.285 -42.381 1.00 67.01 C ANISOU 1603 CA THR A 213 7630 9862 7968 64 -148 -445 C ATOM 1604 C THR A 213 -7.066 -27.638 -41.097 1.00 58.63 C ANISOU 1604 C THR A 213 6480 8911 6886 23 -308 -489 C ATOM 1605 O THR A 213 -7.026 -28.258 -40.028 1.00 63.61 O ANISOU 1605 O THR A 213 7153 9526 7490 13 -318 -462 O ATOM 1606 CB THR A 213 -5.137 -27.818 -42.690 1.00 74.57 C ANISOU 1606 CB THR A 213 8475 10766 9093 204 -144 -291 C ATOM 1607 OG1 THR A 213 -4.636 -28.525 -43.831 1.00 78.61 O ANISOU 1607 OG1 THR A 213 9092 11168 9607 278 42 -236 O ATOM 1608 CG2 THR A 213 -4.219 -28.069 -41.502 1.00 67.15 C ANISOU 1608 CG2 THR A 213 7467 9804 8242 271 -201 -156 C ATOM 1609 N SER A 214 -7.553 -26.398 -41.184 1.00 55.80 N ANISOU 1609 N SER A 214 6021 8654 6525 12 -421 -553 N ATOM 1610 CA SER A 214 -8.009 -25.692 -39.990 1.00 52.81 C ANISOU 1610 CA SER A 214 5597 8360 6108 3 -556 -598 C ATOM 1611 C SER A 214 -9.182 -26.412 -39.337 1.00 60.77 C ANISOU 1611 C SER A 214 6674 9448 6969 -82 -517 -676 C ATOM 1612 O SER A 214 -9.210 -26.594 -38.114 1.00 64.00 O ANISOU 1612 O SER A 214 7105 9871 7341 -80 -563 -664 O ATOM 1613 CB SER A 214 -8.387 -24.253 -40.342 1.00 40.89 C ANISOU 1613 CB SER A 214 4010 6920 4606 30 -653 -653 C ATOM 1614 OG SER A 214 -7.234 -23.472 -40.600 1.00 61.28 O ANISOU 1614 OG SER A 214 6528 9429 7329 88 -725 -564 O ATOM 1615 N TYR A 215 -10.163 -26.833 -40.136 1.00 46.98 N ANISOU 1615 N TYR A 215 4958 7763 5130 -172 -437 -743 N ATOM 1616 CA TYR A 215 -11.329 -27.507 -39.581 1.00 56.30 C ANISOU 1616 CA TYR A 215 6176 9044 6173 -284 -403 -793 C ATOM 1617 C TYR A 215 -11.065 -28.971 -39.256 1.00 57.06 C ANISOU 1617 C TYR A 215 6416 9025 6240 -354 -306 -751 C ATOM 1618 O TYR A 215 -11.778 -29.542 -38.423 1.00 69.50 O ANISOU 1618 O TYR A 215 8026 10661 7721 -436 -291 -762 O ATOM 1619 CB TYR A 215 -12.515 -27.383 -40.540 1.00 51.95 C ANISOU 1619 CB TYR A 215 5584 8628 5526 -386 -381 -857 C ATOM 1620 CG TYR A 215 -13.103 -25.991 -40.570 1.00 47.32 C ANISOU 1620 CG TYR A 215 4857 8192 4932 -304 -466 -891 C ATOM 1621 CD1 TYR A 215 -13.881 -25.525 -39.520 1.00 57.98 C ANISOU 1621 CD1 TYR A 215 6144 9677 6210 -266 -504 -909 C ATOM 1622 CD2 TYR A 215 -12.872 -25.139 -41.642 1.00 56.20 C ANISOU 1622 CD2 TYR A 215 5931 9311 6112 -245 -493 -897 C ATOM 1623 CE1 TYR A 215 -14.417 -24.252 -39.537 1.00 59.88 C ANISOU 1623 CE1 TYR A 215 6288 10032 6430 -155 -558 -933 C ATOM 1624 CE2 TYR A 215 -13.405 -23.865 -41.668 1.00 55.02 C ANISOU 1624 CE2 TYR A 215 5678 9275 5950 -152 -560 -919 C ATOM 1625 CZ TYR A 215 -14.176 -23.426 -40.613 1.00 63.59 C ANISOU 1625 CZ TYR A 215 6718 10483 6962 -99 -589 -938 C ATOM 1626 OH TYR A 215 -14.709 -22.158 -40.635 1.00 78.13 O ANISOU 1626 OH TYR A 215 8488 12418 8780 27 -633 -954 O ATOM 1627 N THR A 216 -10.064 -29.591 -39.885 1.00 54.10 N ANISOU 1627 N THR A 216 6136 8483 5939 -309 -225 -692 N ATOM 1628 CA THR A 216 -9.672 -30.938 -39.481 1.00 58.42 C ANISOU 1628 CA THR A 216 6844 8888 6464 -329 -122 -634 C ATOM 1629 C THR A 216 -9.032 -30.924 -38.098 1.00 69.46 C ANISOU 1629 C THR A 216 8203 10275 7914 -239 -185 -553 C ATOM 1630 O THR A 216 -9.255 -31.836 -37.293 1.00 64.86 O ANISOU 1630 O THR A 216 7721 9658 7264 -288 -142 -528 O ATOM 1631 CB THR A 216 -8.718 -31.546 -40.511 1.00 53.60 C ANISOU 1631 CB THR A 216 6355 8098 5913 -255 4 -575 C ATOM 1632 OG1 THR A 216 -9.363 -31.599 -41.789 1.00 61.93 O ANISOU 1632 OG1 THR A 216 7485 9159 6887 -357 54 -660 O ATOM 1633 CG2 THR A 216 -8.309 -32.954 -40.102 1.00 55.14 C ANISOU 1633 CG2 THR A 216 6751 8122 6078 -244 131 -507 C ATOM 1634 N LEU A 217 -8.240 -29.890 -37.802 1.00 72.65 N ANISOU 1634 N LEU A 217 8471 10706 8426 -123 -298 -505 N ATOM 1635 CA LEU A 217 -7.657 -29.761 -36.471 1.00 69.38 C ANISOU 1635 CA LEU A 217 8022 10299 8039 -62 -395 -429 C ATOM 1636 C LEU A 217 -8.730 -29.492 -35.423 1.00 73.80 C ANISOU 1636 C LEU A 217 8586 10985 8469 -129 -461 -512 C ATOM 1637 O LEU A 217 -8.634 -29.976 -34.289 1.00 83.20 O ANISOU 1637 O LEU A 217 9830 12170 9611 -125 -480 -466 O ATOM 1638 CB LEU A 217 -6.605 -28.653 -36.468 1.00 63.14 C ANISOU 1638 CB LEU A 217 7099 9511 7381 32 -526 -358 C ATOM 1639 CG LEU A 217 -5.352 -28.942 -37.295 1.00 64.65 C ANISOU 1639 CG LEU A 217 7250 9600 7715 127 -455 -221 C ATOM 1640 CD1 LEU A 217 -4.475 -27.706 -37.413 1.00 66.96 C ANISOU 1640 CD1 LEU A 217 7384 9924 8136 173 -597 -150 C ATOM 1641 CD2 LEU A 217 -4.577 -30.093 -36.678 1.00 66.52 C ANISOU 1641 CD2 LEU A 217 7547 9751 7978 198 -384 -78 C ATOM 1642 N ILE A 218 -9.757 -28.719 -35.783 1.00 71.09 N ANISOU 1642 N ILE A 218 8184 10764 8061 -174 -485 -619 N ATOM 1643 CA ILE A 218 -10.886 -28.518 -34.880 1.00 62.32 C ANISOU 1643 CA ILE A 218 7069 9794 6816 -214 -506 -681 C ATOM 1644 C ILE A 218 -11.658 -29.819 -34.704 1.00 65.61 C ANISOU 1644 C ILE A 218 7571 10227 7132 -342 -388 -676 C ATOM 1645 O ILE A 218 -12.104 -30.150 -33.598 1.00 75.17 O ANISOU 1645 O ILE A 218 8817 11496 8250 -364 -383 -662 O ATOM 1646 CB ILE A 218 -11.789 -27.387 -35.403 1.00 53.69 C ANISOU 1646 CB ILE A 218 5877 8840 5684 -201 -540 -768 C ATOM 1647 CG1 ILE A 218 -11.004 -26.078 -35.506 1.00 54.33 C ANISOU 1647 CG1 ILE A 218 5912 8874 5857 -87 -661 -771 C ATOM 1648 CG2 ILE A 218 -13.004 -27.210 -34.506 1.00 43.67 C ANISOU 1648 CG2 ILE A 218 4588 7737 4269 -211 -527 -808 C ATOM 1649 CD1 ILE A 218 -11.771 -24.960 -36.175 1.00 56.85 C ANISOU 1649 CD1 ILE A 218 6155 9295 6152 -48 -682 -842 C ATOM 1650 N TRP A 219 -11.825 -30.577 -35.791 1.00 54.86 N ANISOU 1650 N TRP A 219 6266 8805 5775 -440 -293 -684 N ATOM 1651 CA TRP A 219 -12.485 -31.877 -35.715 1.00 56.57 C ANISOU 1651 CA TRP A 219 6604 8997 5893 -598 -189 -675 C ATOM 1652 C TRP A 219 -11.757 -32.804 -34.749 1.00 62.48 C ANISOU 1652 C TRP A 219 7482 9609 6650 -558 -150 -586 C ATOM 1653 O TRP A 219 -12.381 -33.454 -33.903 1.00 49.90 O ANISOU 1653 O TRP A 219 5945 8057 4958 -645 -114 -566 O ATOM 1654 CB TRP A 219 -12.558 -32.496 -37.113 1.00 55.22 C ANISOU 1654 CB TRP A 219 6531 8731 5718 -705 -108 -702 C ATOM 1655 CG TRP A 219 -13.327 -33.788 -37.207 1.00 50.92 C ANISOU 1655 CG TRP A 219 6147 8144 5054 -918 -17 -705 C ATOM 1656 CD1 TRP A 219 -13.024 -34.974 -36.601 1.00 56.24 C ANISOU 1656 CD1 TRP A 219 7008 8663 5698 -956 65 -645 C ATOM 1657 CD2 TRP A 219 -14.508 -34.028 -37.984 1.00 56.20 C ANISOU 1657 CD2 TRP A 219 6817 8923 5614 -1141 -11 -758 C ATOM 1658 NE1 TRP A 219 -13.951 -35.930 -36.937 1.00 54.10 N ANISOU 1658 NE1 TRP A 219 6874 8378 5303 -1202 125 -666 N ATOM 1659 CE2 TRP A 219 -14.872 -35.375 -37.787 1.00 53.10 C ANISOU 1659 CE2 TRP A 219 6627 8423 5125 -1332 70 -733 C ATOM 1660 CE3 TRP A 219 -15.296 -33.232 -38.821 1.00 66.65 C ANISOU 1660 CE3 TRP A 219 7988 10429 6906 -1203 -73 -812 C ATOM 1661 CZ2 TRP A 219 -15.990 -35.943 -38.395 1.00 57.65 C ANISOU 1661 CZ2 TRP A 219 7258 9073 5575 -1615 73 -761 C ATOM 1662 CZ3 TRP A 219 -16.405 -33.798 -39.424 1.00 66.10 C ANISOU 1662 CZ3 TRP A 219 7947 10455 6711 -1465 -71 -830 C ATOM 1663 CH2 TRP A 219 -16.741 -35.140 -39.208 1.00 67.28 C ANISOU 1663 CH2 TRP A 219 8299 10497 6765 -1684 -6 -805 C ATOM 1664 N LYS A 220 -10.428 -32.876 -34.863 1.00 61.78 N ANISOU 1664 N LYS A 220 7425 9369 6679 -419 -153 -511 N ATOM 1665 CA LYS A 220 -9.660 -33.757 -33.990 1.00 62.96 C ANISOU 1665 CA LYS A 220 7682 9397 6842 -354 -116 -399 C ATOM 1666 C LYS A 220 -9.646 -33.245 -32.555 1.00 63.49 C ANISOU 1666 C LYS A 220 7681 9570 6871 -301 -231 -371 C ATOM 1667 O LYS A 220 -9.668 -34.040 -31.608 1.00 65.74 O ANISOU 1667 O LYS A 220 8063 9823 7091 -315 -198 -306 O ATOM 1668 CB LYS A 220 -8.234 -33.910 -34.520 1.00 66.57 C ANISOU 1668 CB LYS A 220 8152 9702 7440 -199 -85 -294 C ATOM 1669 CG LYS A 220 -8.135 -34.685 -35.824 1.00 72.86 C ANISOU 1669 CG LYS A 220 9095 10345 8243 -222 70 -305 C ATOM 1670 CD LYS A 220 -6.685 -34.938 -36.209 1.00 77.98 C ANISOU 1670 CD LYS A 220 9755 10852 9023 -25 138 -164 C ATOM 1671 CE LYS A 220 -6.588 -35.787 -37.466 1.00 91.72 C ANISOU 1671 CE LYS A 220 11701 12412 10738 -22 323 -177 C ATOM 1672 NZ LYS A 220 -5.174 -36.072 -37.838 1.00100.81 N ANISOU 1672 NZ LYS A 220 12858 13434 12011 211 427 -14 N ATOM 1673 N ALA A 221 -9.614 -31.923 -32.372 1.00 59.30 N ANISOU 1673 N ALA A 221 7014 9152 6365 -240 -364 -419 N ATOM 1674 CA ALA A 221 -9.578 -31.362 -31.024 1.00 54.89 C ANISOU 1674 CA ALA A 221 6439 8675 5743 -189 -480 -406 C ATOM 1675 C ALA A 221 -10.884 -31.623 -30.284 1.00 60.92 C ANISOU 1675 C ALA A 221 7242 9563 6342 -274 -425 -459 C ATOM 1676 O ALA A 221 -10.878 -32.049 -29.123 1.00 72.75 O ANISOU 1676 O ALA A 221 8814 11071 7756 -264 -432 -405 O ATOM 1677 CB ALA A 221 -9.283 -29.863 -31.086 1.00 45.65 C ANISOU 1677 CB ALA A 221 5165 7562 4619 -116 -629 -457 C ATOM 1678 N LEU A 222 -12.019 -31.367 -30.940 1.00 67.62 N ANISOU 1678 N LEU A 222 8028 10527 7139 -357 -369 -546 N ATOM 1679 CA LEU A 222 -13.308 -31.616 -30.305 1.00 62.43 C ANISOU 1679 CA LEU A 222 7365 10023 6332 -441 -303 -565 C ATOM 1680 C LEU A 222 -13.541 -33.103 -30.070 1.00 67.22 C ANISOU 1680 C LEU A 222 8093 10561 6888 -576 -190 -495 C ATOM 1681 O LEU A 222 -14.213 -33.478 -29.103 1.00 62.17 O ANISOU 1681 O LEU A 222 7482 10012 6129 -622 -146 -461 O ATOM 1682 CB LEU A 222 -14.434 -31.027 -31.156 1.00 60.93 C ANISOU 1682 CB LEU A 222 7045 9997 6111 -501 -275 -639 C ATOM 1683 CG LEU A 222 -14.380 -29.514 -31.377 1.00 54.76 C ANISOU 1683 CG LEU A 222 6163 9284 5360 -359 -369 -706 C ATOM 1684 CD1 LEU A 222 -15.500 -29.062 -32.300 1.00 47.15 C ANISOU 1684 CD1 LEU A 222 5062 8487 4366 -410 -330 -751 C ATOM 1685 CD2 LEU A 222 -14.444 -28.774 -30.051 1.00 52.98 C ANISOU 1685 CD2 LEU A 222 5973 9119 5038 -228 -424 -715 C ATOM 1686 N LYS A 223 -12.993 -33.960 -30.935 1.00 73.96 N ANISOU 1686 N LYS A 223 9041 11242 7819 -634 -130 -468 N ATOM 1687 CA LYS A 223 -13.131 -35.400 -30.737 1.00 68.02 C ANISOU 1687 CA LYS A 223 8458 10372 7013 -759 -17 -400 C ATOM 1688 C LYS A 223 -12.367 -35.863 -29.503 1.00 74.07 C ANISOU 1688 C LYS A 223 9321 11055 7768 -652 -29 -297 C ATOM 1689 O LYS A 223 -12.874 -36.679 -28.726 1.00 74.63 O ANISOU 1689 O LYS A 223 9487 11131 7736 -741 39 -242 O ATOM 1690 CB LYS A 223 -12.652 -36.151 -31.979 1.00 58.47 C ANISOU 1690 CB LYS A 223 7379 8965 5872 -812 61 -402 C ATOM 1691 CG LYS A 223 -13.774 -36.738 -32.819 1.00 60.49 C ANISOU 1691 CG LYS A 223 7692 9250 6042 -1057 131 -456 C ATOM 1692 CD LYS A 223 -14.562 -37.775 -32.032 1.00 64.41 C ANISOU 1692 CD LYS A 223 8302 9756 6417 -1236 203 -399 C ATOM 1693 CE LYS A 223 -15.719 -38.334 -32.846 1.00 74.68 C ANISOU 1693 CE LYS A 223 9645 11108 7624 -1530 243 -437 C ATOM 1694 NZ LYS A 223 -16.478 -39.376 -32.097 1.00 87.28 N ANISOU 1694 NZ LYS A 223 11353 12708 9104 -1738 312 -362 N ATOM 1695 N LYS A 224 -11.147 -35.356 -29.308 1.00 72.24 N ANISOU 1695 N LYS A 224 9056 10755 7636 -474 -120 -253 N ATOM 1696 CA LYS A 224 -10.378 -35.714 -28.120 1.00 78.61 C ANISOU 1696 CA LYS A 224 9932 11510 8426 -372 -162 -138 C ATOM 1697 C LYS A 224 -11.086 -35.261 -26.850 1.00 72.76 C ANISOU 1697 C LYS A 224 9169 10934 7540 -380 -217 -157 C ATOM 1698 O LYS A 224 -11.049 -35.954 -25.827 1.00 86.39 O ANISOU 1698 O LYS A 224 11000 12641 9181 -378 -191 -70 O ATOM 1699 CB LYS A 224 -8.977 -35.108 -28.194 1.00 87.74 C ANISOU 1699 CB LYS A 224 11011 12609 9716 -207 -281 -71 C ATOM 1700 CG LYS A 224 -8.129 -35.620 -29.345 1.00 94.09 C ANISOU 1700 CG LYS A 224 11840 13250 10660 -150 -199 -14 C ATOM 1701 CD LYS A 224 -6.841 -34.821 -29.470 1.00101.90 C ANISOU 1701 CD LYS A 224 12690 14239 11790 -3 -327 66 C ATOM 1702 CE LYS A 224 -6.061 -35.216 -30.714 1.00107.65 C ANISOU 1702 CE LYS A 224 13421 14830 12653 76 -220 127 C ATOM 1703 NZ LYS A 224 -4.837 -34.383 -30.883 1.00108.59 N ANISOU 1703 NZ LYS A 224 13363 14980 12918 202 -343 228 N ATOM 1704 N ALA A 225 -11.740 -34.098 -26.898 1.00 67.34 N ANISOU 1704 N ALA A 225 8365 10408 6814 -372 -280 -264 N ATOM 1705 CA ALA A 225 -12.463 -33.598 -25.735 1.00 68.83 C ANISOU 1705 CA ALA A 225 8555 10753 6846 -347 -305 -287 C ATOM 1706 C ALA A 225 -13.770 -34.351 -25.519 1.00 73.04 C ANISOU 1706 C ALA A 225 9102 11392 7257 -489 -157 -274 C ATOM 1707 O ALA A 225 -14.118 -34.680 -24.379 1.00 81.63 O ANISOU 1707 O ALA A 225 10260 12541 8213 -486 -122 -218 O ATOM 1708 CB ALA A 225 -12.730 -32.101 -25.886 1.00 50.22 C ANISOU 1708 CB ALA A 225 6094 8509 4477 -263 -398 -396 C ATOM 1709 N TYR A 226 -14.507 -34.635 -26.596 1.00 67.09 N ANISOU 1709 N TYR A 226 8283 10671 6537 -629 -75 -313 N ATOM 1710 CA TYR A 226 -15.786 -35.324 -26.447 1.00 58.92 C ANISOU 1710 CA TYR A 226 7233 9763 5391 -805 47 -281 C ATOM 1711 C TYR A 226 -15.589 -36.785 -26.064 1.00 60.91 C ANISOU 1711 C TYR A 226 7666 9862 5615 -922 134 -177 C ATOM 1712 O TYR A 226 -16.338 -37.320 -25.238 1.00 61.71 O ANISOU 1712 O TYR A 226 7797 10056 5594 -1011 212 -108 O ATOM 1713 CB TYR A 226 -16.603 -35.210 -27.735 1.00 62.33 C ANISOU 1713 CB TYR A 226 7544 10282 5857 -951 79 -338 C ATOM 1714 CG TYR A 226 -17.205 -33.841 -27.962 1.00 64.14 C ANISOU 1714 CG TYR A 226 7581 10719 6071 -848 31 -412 C ATOM 1715 CD1 TYR A 226 -17.119 -32.852 -26.991 1.00 69.33 C ANISOU 1715 CD1 TYR A 226 8216 11462 6664 -649 -17 -433 C ATOM 1716 CD2 TYR A 226 -17.870 -33.541 -29.144 1.00 70.10 C ANISOU 1716 CD2 TYR A 226 8200 11575 6860 -945 34 -457 C ATOM 1717 CE1 TYR A 226 -17.669 -31.601 -27.193 1.00 70.09 C ANISOU 1717 CE1 TYR A 226 8176 11718 6736 -529 -42 -496 C ATOM 1718 CE2 TYR A 226 -18.424 -32.292 -29.355 1.00 75.27 C ANISOU 1718 CE2 TYR A 226 8683 12416 7499 -825 1 -507 C ATOM 1719 CZ TYR A 226 -18.321 -31.326 -28.376 1.00 68.98 C ANISOU 1719 CZ TYR A 226 7883 11682 6643 -608 -27 -527 C ATOM 1720 OH TYR A 226 -18.871 -30.081 -28.579 1.00 63.44 O ANISOU 1720 OH TYR A 226 7050 11137 5916 -464 -42 -573 O ATOM 1721 N ASP A 227 -14.590 -37.449 -26.652 1.00 62.72 N ANISOU 1721 N ASP A 227 8026 9853 5951 -911 136 -153 N ATOM 1722 CA ASP A 227 -14.319 -38.835 -26.286 1.00 69.73 C ANISOU 1722 CA ASP A 227 9125 10560 6812 -987 229 -46 C ATOM 1723 C ASP A 227 -13.827 -38.949 -24.849 1.00 71.65 C ANISOU 1723 C ASP A 227 9432 10804 6987 -853 200 50 C ATOM 1724 O ASP A 227 -14.076 -39.965 -24.190 1.00 71.19 O ANISOU 1724 O ASP A 227 9518 10687 6845 -937 289 147 O ATOM 1725 CB ASP A 227 -13.301 -39.451 -27.245 1.00 73.97 C ANISOU 1725 CB ASP A 227 9800 10835 7471 -948 259 -32 C ATOM 1726 CG ASP A 227 -13.864 -39.661 -28.637 1.00 84.07 C ANISOU 1726 CG ASP A 227 11097 12073 8771 -1124 311 -116 C ATOM 1727 OD1 ASP A 227 -15.044 -39.317 -28.860 1.00 83.24 O ANISOU 1727 OD1 ASP A 227 10866 12164 8598 -1289 305 -174 O ATOM 1728 OD2 ASP A 227 -13.128 -40.172 -29.507 1.00 89.34 O ANISOU 1728 OD2 ASP A 227 11907 12522 9516 -1092 360 -114 O ATOM 1729 N LEU A 228 -13.130 -37.926 -24.349 1.00 69.74 N ANISOU 1729 N LEU A 228 9106 10623 6769 -660 68 31 N ATOM 1730 CA LEU A 228 -12.706 -37.941 -22.953 1.00 61.02 C ANISOU 1730 CA LEU A 228 8071 9543 5572 -548 14 117 C ATOM 1731 C LEU A 228 -13.901 -37.819 -22.017 1.00 69.82 C ANISOU 1731 C LEU A 228 9170 10853 6506 -611 74 114 C ATOM 1732 O LEU A 228 -13.982 -38.528 -21.007 1.00 80.70 O ANISOU 1732 O LEU A 228 10668 12221 7774 -623 126 218 O ATOM 1733 CB LEU A 228 -11.701 -36.819 -22.694 1.00 61.35 C ANISOU 1733 CB LEU A 228 8040 9602 5667 -368 -167 92 C ATOM 1734 CG LEU A 228 -11.137 -36.741 -21.274 1.00 70.45 C ANISOU 1734 CG LEU A 228 9277 10779 6711 -259 -267 181 C ATOM 1735 CD1 LEU A 228 -10.439 -38.041 -20.904 1.00 66.01 C ANISOU 1735 CD1 LEU A 228 8852 10062 6168 -242 -212 348 C ATOM 1736 CD2 LEU A 228 -10.189 -35.559 -21.133 1.00 76.27 C ANISOU 1736 CD2 LEU A 228 9946 11535 7496 -135 -474 149 C ATOM 1737 N GLU A 229 -14.841 -36.925 -22.338 1.00 65.85 N ANISOU 1737 N GLU A 229 8517 10537 5965 -637 81 13 N ATOM 1738 CA GLU A 229 -16.051 -36.801 -21.532 1.00 70.66 C ANISOU 1738 CA GLU A 229 9084 11360 6405 -677 171 31 C ATOM 1739 C GLU A 229 -16.886 -38.073 -21.581 1.00 59.11 C ANISOU 1739 C GLU A 229 7663 9902 4895 -902 324 127 C ATOM 1740 O GLU A 229 -17.547 -38.419 -20.595 1.00 88.77 O ANISOU 1740 O GLU A 229 11450 13774 8506 -936 411 212 O ATOM 1741 CB GLU A 229 -16.876 -35.604 -22.005 1.00 57.05 C ANISOU 1741 CB GLU A 229 7175 9837 4665 -635 165 -74 C ATOM 1742 N ASP A 230 -16.868 -38.781 -22.713 1.00 96.40 N ANISOU 1742 N ASP A 230 12408 14492 9727 -1068 358 119 N ATOM 1743 CA ASP A 230 -17.589 -40.045 -22.807 1.00100.28 C ANISOU 1743 CA ASP A 230 12988 14944 10170 -1322 484 209 C ATOM 1744 C ASP A 230 -16.932 -41.129 -21.963 1.00 94.50 C ANISOU 1744 C ASP A 230 12492 14014 9399 -1305 530 331 C ATOM 1745 O ASP A 230 -17.616 -42.047 -21.495 1.00 99.39 O ANISOU 1745 O ASP A 230 13197 14643 9923 -1481 638 434 O ATOM 1746 CB ASP A 230 -17.681 -40.492 -24.266 1.00112.10 C ANISOU 1746 CB ASP A 230 14505 16318 11769 -1507 495 154 C ATOM 1747 CG ASP A 230 -18.578 -39.595 -25.093 1.00125.21 C ANISOU 1747 CG ASP A 230 15924 18207 13443 -1575 464 67 C ATOM 1748 OD1 ASP A 230 -19.250 -38.723 -24.504 1.00130.36 O ANISOU 1748 OD1 ASP A 230 16393 19118 14019 -1484 464 67 O ATOM 1749 OD2 ASP A 230 -18.611 -39.761 -26.331 1.00133.60 O ANISOU 1749 OD2 ASP A 230 16993 19190 14580 -1705 447 7 O ATOM 1750 N ASN A 231 -15.616 -41.044 -21.757 1.00 80.75 N ANISOU 1750 N ASN A 231 10849 12103 7730 -1100 447 340 N ATOM 1751 CA ASN A 231 -14.937 -42.033 -20.926 1.00 76.38 C ANISOU 1751 CA ASN A 231 10507 11376 7138 -1048 484 478 C ATOM 1752 C ASN A 231 -15.267 -41.834 -19.451 1.00 81.45 C ANISOU 1752 C ASN A 231 11153 12182 7614 -977 485 551 C ATOM 1753 O ASN A 231 -15.437 -42.810 -18.712 1.00 81.83 O ANISOU 1753 O ASN A 231 11354 12168 7569 -1045 577 681 O ATOM 1754 CB ASN A 231 -13.428 -41.969 -21.156 1.00 72.01 C ANISOU 1754 CB ASN A 231 10015 10633 6714 -840 390 499 C ATOM 1755 CG ASN A 231 -13.026 -42.470 -22.531 1.00 70.81 C ANISOU 1755 CG ASN A 231 9931 10271 6702 -892 439 463 C ATOM 1756 OD1 ASN A 231 -13.711 -43.304 -23.124 1.00 61.77 O ANISOU 1756 OD1 ASN A 231 8900 9033 5535 -1104 556 459 O ATOM 1757 ND2 ASN A 231 -11.910 -41.964 -23.043 1.00 80.11 N ANISOU 1757 ND2 ASN A 231 11052 11373 8014 -710 351 446 N ATOM 1758 N TRP A 232 -15.362 -40.579 -19.004 1.00 75.79 N ANISOU 1758 N TRP A 232 10295 11660 6841 -835 391 472 N ATOM 1759 CA TRP A 232 -15.754 -40.322 -17.622 1.00 83.28 C ANISOU 1759 CA TRP A 232 11276 12769 7600 -757 406 528 C ATOM 1760 C TRP A 232 -17.209 -40.704 -17.383 1.00 89.61 C ANISOU 1760 C TRP A 232 12016 13750 8281 -934 573 579 C ATOM 1761 O TRP A 232 -17.551 -41.236 -16.321 1.00 99.08 O ANISOU 1761 O TRP A 232 13313 15002 9331 -951 658 696 O ATOM 1762 CB TRP A 232 -15.521 -38.854 -17.266 1.00 90.25 C ANISOU 1762 CB TRP A 232 12073 13786 8435 -563 271 417 C ATOM 1763 CG TRP A 232 -14.083 -38.439 -17.314 1.00 96.00 C ANISOU 1763 CG TRP A 232 12847 14369 9260 -412 84 399 C ATOM 1764 CD1 TRP A 232 -13.520 -37.528 -18.160 1.00105.17 C ANISOU 1764 CD1 TRP A 232 13901 15501 10559 -346 -41 289 C ATOM 1765 CD2 TRP A 232 -13.021 -38.924 -16.483 1.00 97.91 C ANISOU 1765 CD2 TRP A 232 13235 14495 9472 -318 -4 521 C ATOM 1766 NE1 TRP A 232 -12.175 -37.413 -17.905 1.00107.02 N ANISOU 1766 NE1 TRP A 232 14191 15618 10855 -231 -202 342 N ATOM 1767 CE2 TRP A 232 -11.844 -38.260 -16.881 1.00103.06 C ANISOU 1767 CE2 TRP A 232 13836 15069 10252 -207 -188 487 C ATOM 1768 CE3 TRP A 232 -12.952 -39.854 -15.441 1.00103.78 C ANISOU 1768 CE3 TRP A 232 14138 15205 10091 -318 52 672 C ATOM 1769 CZ2 TRP A 232 -10.612 -38.497 -16.273 1.00108.72 C ANISOU 1769 CZ2 TRP A 232 14632 15698 10979 -102 -326 611 C ATOM 1770 CZ3 TRP A 232 -11.728 -40.088 -14.840 1.00106.46 C ANISOU 1770 CZ3 TRP A 232 14574 15443 10434 -197 -82 785 C ATOM 1771 CH2 TRP A 232 -10.575 -39.412 -15.257 1.00108.03 C ANISOU 1771 CH2 TRP A 232 14695 15587 10765 -92 -273 759 C ATOM 1772 N GLU A 233 -18.079 -40.441 -18.361 1.00 87.70 N ANISOU 1772 N GLU A 233 11601 13621 8098 -1074 621 510 N ATOM 1773 CA GLU A 233 -19.480 -40.824 -18.227 1.00 91.07 C ANISOU 1773 CA GLU A 233 11925 14252 8427 -1272 771 589 C ATOM 1774 C GLU A 233 -19.646 -42.337 -18.195 1.00 92.98 C ANISOU 1774 C GLU A 233 12330 14336 8660 -1516 872 724 C ATOM 1775 O GLU A 233 -20.557 -42.845 -17.532 1.00 98.87 O ANISOU 1775 O GLU A 233 13062 15223 9282 -1653 996 850 O ATOM 1776 CB GLU A 233 -20.302 -40.223 -19.367 1.00 90.66 C ANISOU 1776 CB GLU A 233 11636 14361 8448 -1378 772 505 C ATOM 1777 N THR A 234 -18.780 -43.071 -18.898 1.00 91.26 N ANISOU 1777 N THR A 234 12283 13822 8567 -1568 832 710 N ATOM 1778 CA THR A 234 -18.847 -44.528 -18.862 1.00 92.61 C ANISOU 1778 CA THR A 234 12677 13788 8722 -1781 933 834 C ATOM 1779 C THR A 234 -18.417 -45.064 -17.502 1.00 94.53 C ANISOU 1779 C THR A 234 13098 13969 8851 -1663 974 973 C ATOM 1780 O THR A 234 -18.985 -46.044 -17.005 1.00108.19 O ANISOU 1780 O THR A 234 14948 15671 10490 -1847 1093 1111 O ATOM 1781 CB THR A 234 -17.981 -45.121 -19.975 1.00 94.18 C ANISOU 1781 CB THR A 234 13048 13667 9067 -1815 900 781 C ATOM 1782 OG1 THR A 234 -18.404 -44.598 -21.241 1.00108.06 O ANISOU 1782 OG1 THR A 234 14652 15494 10912 -1929 857 653 O ATOM 1783 CG2 THR A 234 -18.099 -46.638 -20.000 1.00 85.94 C ANISOU 1783 CG2 THR A 234 12289 12373 7992 -2040 1017 901 C ATOM 1784 N LEU A 235 -17.420 -44.429 -16.881 1.00 87.29 N ANISOU 1784 N LEU A 235 12202 13034 7930 -1372 866 949 N ATOM 1785 CA LEU A 235 -16.971 -44.860 -15.561 1.00 77.18 C ANISOU 1785 CA LEU A 235 11085 11715 6523 -1247 881 1085 C ATOM 1786 C LEU A 235 -18.057 -44.647 -14.513 1.00 81.89 C ANISOU 1786 C LEU A 235 11609 12580 6923 -1287 978 1154 C ATOM 1787 O LEU A 235 -18.371 -45.556 -13.736 1.00 95.92 O ANISOU 1787 O LEU A 235 13527 14330 8589 -1379 1089 1309 O ATOM 1788 CB LEU A 235 -15.695 -44.113 -15.169 1.00 73.51 C ANISOU 1788 CB LEU A 235 10634 11208 6088 -955 710 1046 C ATOM 1789 CG LEU A 235 -14.434 -44.390 -15.989 1.00 89.56 C ANISOU 1789 CG LEU A 235 12737 12986 8305 -862 625 1036 C ATOM 1790 CD1 LEU A 235 -13.292 -43.497 -15.530 1.00 94.72 C ANISOU 1790 CD1 LEU A 235 13343 13671 8976 -607 434 1017 C ATOM 1791 CD2 LEU A 235 -14.042 -45.853 -15.889 1.00 95.83 C ANISOU 1791 CD2 LEU A 235 13779 13520 9111 -915 732 1196 C ATOM 1792 N ASN A 236 -18.645 -43.448 -14.479 1.00 88.02 N ANISOU 1792 N ASN A 236 12176 13618 7650 -1204 952 1050 N ATOM 1793 CA ASN A 236 -19.633 -43.137 -13.451 1.00100.86 C ANISOU 1793 CA ASN A 236 13733 15514 9075 -1181 1065 1122 C ATOM 1794 C ASN A 236 -20.908 -43.952 -13.634 1.00100.93 C ANISOU 1794 C ASN A 236 13658 15640 9052 -1478 1242 1245 C ATOM 1795 O ASN A 236 -21.513 -44.395 -12.651 1.00107.44 O ANISOU 1795 O ASN A 236 14524 16583 9715 -1522 1373 1394 O ATOM 1796 CB ASN A 236 -19.946 -41.641 -13.459 1.00105.44 C ANISOU 1796 CB ASN A 236 14132 16320 9609 -993 1014 983 C ATOM 1797 CG ASN A 236 -18.739 -40.792 -13.114 1.00106.39 C ANISOU 1797 CG ASN A 236 14357 16339 9726 -732 826 876 C ATOM 1798 OD1 ASN A 236 -17.597 -41.222 -13.274 1.00107.00 O ANISOU 1798 OD1 ASN A 236 14564 16186 9907 -702 708 886 O ATOM 1799 ND2 ASN A 236 -18.986 -39.579 -12.633 1.00105.62 N ANISOU 1799 ND2 ASN A 236 14213 16415 9504 -542 798 786 N ATOM 1800 N ASP A 237 -21.335 -44.159 -14.882 1.00101.38 N ANISOU 1800 N ASP A 237 13597 15673 9251 -1700 1243 1196 N ATOM 1801 CA ASP A 237 -22.527 -44.966 -15.123 1.00110.42 C ANISOU 1801 CA ASP A 237 14660 16927 10368 -2037 1379 1325 C ATOM 1802 C ASP A 237 -22.298 -46.418 -14.724 1.00115.94 C ANISOU 1802 C ASP A 237 15636 17379 11036 -2220 1452 1477 C ATOM 1803 O ASP A 237 -23.186 -47.055 -14.146 1.00121.22 O ANISOU 1803 O ASP A 237 16294 18171 11593 -2416 1588 1646 O ATOM 1804 CB ASP A 237 -22.946 -44.871 -16.590 1.00109.18 C ANISOU 1804 CB ASP A 237 14348 16779 10357 -2251 1329 1234 C ATOM 1805 CG ASP A 237 -23.461 -43.495 -16.961 1.00111.75 C ANISOU 1805 CG ASP A 237 14368 17397 10694 -2103 1291 1127 C ATOM 1806 OD1 ASP A 237 -23.362 -42.575 -16.121 1.00113.46 O ANISOU 1806 OD1 ASP A 237 14535 17763 10813 -1812 1298 1099 O ATOM 1807 OD2 ASP A 237 -23.968 -43.334 -18.091 1.00113.19 O ANISOU 1807 OD2 ASP A 237 14384 17653 10972 -2277 1255 1075 O ATOM 1808 N ASN A 238 -21.113 -46.958 -15.018 1.00123.41 N ANISOU 1808 N ASN A 238 16834 17978 12078 -2149 1374 1436 N ATOM 1809 CA ASN A 238 -20.813 -48.330 -14.624 1.00124.16 C ANISOU 1809 CA ASN A 238 17231 17804 12140 -2279 1452 1586 C ATOM 1810 C ASN A 238 -20.621 -48.454 -13.118 1.00129.46 C ANISOU 1810 C ASN A 238 18007 18538 12645 -2101 1506 1724 C ATOM 1811 O ASN A 238 -20.970 -49.487 -12.537 1.00139.25 O ANISOU 1811 O ASN A 238 19412 19701 13794 -2267 1626 1897 O ATOM 1812 CB ASN A 238 -19.575 -48.833 -15.366 1.00120.11 C ANISOU 1812 CB ASN A 238 16954 16912 11770 -2198 1375 1521 C ATOM 1813 CG ASN A 238 -19.861 -49.163 -16.818 1.00126.87 C ANISOU 1813 CG ASN A 238 17822 17633 12749 -2453 1367 1428 C ATOM 1814 OD1 ASN A 238 -19.976 -50.330 -17.190 1.00124.91 O ANISOU 1814 OD1 ASN A 238 17823 17132 12505 -2695 1442 1500 O ATOM 1815 ND2 ASN A 238 -19.984 -48.132 -17.646 1.00133.97 N ANISOU 1815 ND2 ASN A 238 18479 18688 13734 -2404 1274 1269 N ATOM 1816 N LEU A 239 -20.071 -47.421 -12.472 1.00121.57 N ANISOU 1816 N LEU A 239 16935 17666 11589 -1780 1414 1652 N ATOM 1817 CA LEU A 239 -19.979 -47.431 -11.015 1.00104.15 C ANISOU 1817 CA LEU A 239 14830 15553 9189 -1615 1457 1774 C ATOM 1818 C LEU A 239 -21.363 -47.482 -10.381 1.00107.50 C ANISOU 1818 C LEU A 239 15123 16269 9452 -1765 1632 1895 C ATOM 1819 O LEU A 239 -21.557 -48.128 -9.345 1.00110.96 O ANISOU 1819 O LEU A 239 15703 16720 9737 -1784 1740 2068 O ATOM 1820 CB LEU A 239 -19.206 -46.206 -10.527 1.00 96.27 C ANISOU 1820 CB LEU A 239 13789 14646 8143 -1279 1304 1654 C ATOM 1821 CG LEU A 239 -17.685 -46.263 -10.673 1.00 96.53 C ANISOU 1821 CG LEU A 239 13972 14422 8283 -1093 1132 1617 C ATOM 1822 CD1 LEU A 239 -17.069 -44.903 -10.394 1.00 93.57 C ANISOU 1822 CD1 LEU A 239 13513 14164 7875 -833 956 1480 C ATOM 1823 CD2 LEU A 239 -17.104 -47.316 -9.746 1.00 95.47 C ANISOU 1823 CD2 LEU A 239 14098 14119 8058 -1051 1165 1810 C ATOM 1824 N LYS A 240 -22.339 -46.806 -10.992 1.00102.36 N ANISOU 1824 N LYS A 240 14191 15870 8832 -1863 1670 1828 N ATOM 1825 CA LYS A 240 -23.716 -46.920 -10.526 1.00104.34 C ANISOU 1825 CA LYS A 240 14269 16424 8952 -2028 1853 1979 C ATOM 1826 C LYS A 240 -24.294 -48.295 -10.835 1.00112.49 C ANISOU 1826 C LYS A 240 15380 17340 10019 -2427 1955 2146 C ATOM 1827 O LYS A 240 -25.135 -48.796 -10.080 1.00121.42 O ANISOU 1827 O LYS A 240 16483 18634 11015 -2569 2115 2344 O ATOM 1828 CB LYS A 240 -24.578 -45.826 -11.155 1.00 97.92 C ANISOU 1828 CB LYS A 240 13112 15922 8173 -2009 1862 1885 C ATOM 1829 N VAL A 241 -23.858 -48.916 -11.933 1.00113.62 N ANISOU 1829 N VAL A 241 15642 17197 10333 -2618 1870 2076 N ATOM 1830 CA VAL A 241 -24.297 -50.273 -12.245 1.00115.68 C ANISOU 1830 CA VAL A 241 16063 17277 10613 -3012 1951 2220 C ATOM 1831 C VAL A 241 -23.717 -51.263 -11.241 1.00114.46 C ANISOU 1831 C VAL A 241 16246 16883 10362 -2963 2020 2374 C ATOM 1832 O VAL A 241 -24.384 -52.224 -10.839 1.00122.67 O ANISOU 1832 O VAL A 241 17381 17908 11321 -3238 2150 2569 O ATOM 1833 CB VAL A 241 -23.917 -50.635 -13.694 1.00113.43 C ANISOU 1833 CB VAL A 241 15876 16714 10508 -3196 1845 2084 C ATOM 1834 CG1 VAL A 241 -24.137 -52.117 -13.957 1.00119.53 C ANISOU 1834 CG1 VAL A 241 16937 17199 11281 -3576 1916 2216 C ATOM 1835 CG2 VAL A 241 -24.724 -49.800 -14.676 1.00103.66 C ANISOU 1835 CG2 VAL A 241 14293 15749 9345 -3319 1791 1979 C ATOM 1836 N ILE A 242 -22.472 -51.040 -10.812 1.00112.32 N ANISOU 1836 N ILE A 242 16151 16432 10094 -2619 1931 2307 N ATOM 1837 CA ILE A 242 -21.857 -51.920 -9.822 1.00116.06 C ANISOU 1837 CA ILE A 242 16933 16696 10468 -2530 1984 2467 C ATOM 1838 C ILE A 242 -22.587 -51.819 -8.488 1.00130.33 C ANISOU 1838 C ILE A 242 18674 18788 12059 -2494 2115 2633 C ATOM 1839 O ILE A 242 -22.815 -52.829 -7.812 1.00145.62 O ANISOU 1839 O ILE A 242 20806 20630 13895 -2635 2238 2836 O ATOM 1840 CB ILE A 242 -20.359 -51.594 -9.676 1.00112.24 C ANISOU 1840 CB ILE A 242 16596 16013 10037 -2162 1836 2376 C ATOM 1841 CG1 ILE A 242 -19.619 -51.887 -10.982 1.00111.72 C ANISOU 1841 CG1 ILE A 242 16631 15640 10179 -2197 1749 2253 C ATOM 1842 CG2 ILE A 242 -19.745 -52.387 -8.531 1.00116.92 C ANISOU 1842 CG2 ILE A 242 17471 16448 10504 -2032 1881 2563 C ATOM 1843 CD1 ILE A 242 -18.159 -51.496 -10.962 1.00109.71 C ANISOU 1843 CD1 ILE A 242 16453 15231 10001 -1842 1601 2182 C ATOM 1844 N GLU A 243 -22.969 -50.602 -8.091 1.00121.11 N ANISOU 1844 N GLU A 243 17251 17962 10804 -2296 2105 2557 N ATOM 1845 CA GLU A 243 -23.680 -50.425 -6.829 1.00109.41 C ANISOU 1845 CA GLU A 243 15713 16764 9093 -2223 2252 2710 C ATOM 1846 C GLU A 243 -25.056 -51.077 -6.860 1.00106.97 C ANISOU 1846 C GLU A 243 15263 16638 8744 -2591 2442 2902 C ATOM 1847 O GLU A 243 -25.536 -51.555 -5.825 1.00115.05 O ANISOU 1847 O GLU A 243 16351 17770 9593 -2629 2598 3110 O ATOM 1848 CB GLU A 243 -23.806 -48.937 -6.503 1.00 96.99 C ANISOU 1848 CB GLU A 243 13930 15493 7430 -1917 2213 2570 C ATOM 1849 N LYS A 244 -25.701 -51.109 -8.024 1.00101.76 N ANISOU 1849 N LYS A 244 14404 16024 8234 -2876 2426 2852 N ATOM 1850 CA LYS A 244 -27.004 -51.739 -8.184 1.00108.90 C ANISOU 1850 CA LYS A 244 15146 17113 9119 -3282 2571 3047 C ATOM 1851 C LYS A 244 -26.904 -53.162 -8.718 1.00137.32 C ANISOU 1851 C LYS A 244 19020 20351 12804 -3672 2567 3139 C ATOM 1852 O LYS A 244 -27.930 -53.756 -9.066 1.00144.73 O ANISOU 1852 O LYS A 244 19846 21393 13751 -4088 2644 3286 O ATOM 1853 CB LYS A 244 -27.887 -50.895 -9.106 1.00102.95 C ANISOU 1853 CB LYS A 244 13990 16673 8454 -3387 2547 2966 C ATOM 1854 N ALA A 245 -25.699 -53.719 -8.791 1.00147.69 N ANISOU 1854 N ALA A 245 20698 21245 14174 -3550 2481 3067 N ATOM 1855 CA ALA A 245 -25.528 -55.074 -9.293 1.00152.23 C ANISOU 1855 CA ALA A 245 21602 21426 14815 -3876 2494 3145 C ATOM 1856 C ALA A 245 -25.987 -56.095 -8.259 1.00156.40 C ANISOU 1856 C ALA A 245 22312 21922 15190 -4057 2662 3423 C ATOM 1857 O ALA A 245 -25.999 -55.833 -7.053 1.00153.48 O ANISOU 1857 O ALA A 245 21913 21738 14663 -3824 2748 3535 O ATOM 1858 CB ALA A 245 -24.067 -55.326 -9.667 1.00150.42 C ANISOU 1858 CB ALA A 245 21698 20768 14688 -3629 2377 3005 C ATOM 1859 N ASP A 246 -26.368 -57.277 -8.747 1.00162.40 N ANISOU 1859 N ASP A 246 23290 22429 15984 -4490 2707 3535 N ATOM 1860 CA ASP A 246 -26.850 -58.346 -7.884 1.00161.72 C ANISOU 1860 CA ASP A 246 23404 22276 15766 -4729 2866 3812 C ATOM 1861 C ASP A 246 -26.135 -59.675 -8.078 1.00149.34 C ANISOU 1861 C ASP A 246 22365 20152 14226 -4860 2876 3866 C ATOM 1862 O ASP A 246 -26.271 -60.552 -7.218 1.00138.25 O ANISOU 1862 O ASP A 246 21193 18632 12703 -4962 3006 4094 O ATOM 1863 CB ASP A 246 -28.358 -58.561 -8.086 1.00173.35 C ANISOU 1863 CB ASP A 246 24599 24057 17209 -5223 2952 3984 C ATOM 1864 CG ASP A 246 -29.181 -57.368 -7.640 1.00181.58 C ANISOU 1864 CG ASP A 246 25130 25679 18185 -5064 3008 4012 C ATOM 1865 OD1 ASP A 246 -28.763 -56.678 -6.686 1.00183.57 O ANISOU 1865 OD1 ASP A 246 25334 26084 18330 -4625 3051 3993 O ATOM 1866 OD2 ASP A 246 -30.247 -57.120 -8.242 1.00186.60 O ANISOU 1866 OD2 ASP A 246 25421 26615 18862 -5375 3009 4060 O ATOM 1867 N ASN A 247 -25.388 -59.859 -9.164 1.00147.24 N ANISOU 1867 N ASN A 247 22310 19532 14102 -4845 2761 3676 N ATOM 1868 CA ASN A 247 -24.629 -61.079 -9.394 1.00145.82 C ANISOU 1868 CA ASN A 247 22665 18796 13945 -4902 2790 3718 C ATOM 1869 C ASN A 247 -23.229 -60.721 -9.875 1.00135.32 C ANISOU 1869 C ASN A 247 21476 17211 12729 -4463 2680 3516 C ATOM 1870 O ASN A 247 -22.909 -59.556 -10.123 1.00120.25 O ANISOU 1870 O ASN A 247 19255 15545 10891 -4183 2567 3336 O ATOM 1871 CB ASN A 247 -25.336 -62.002 -10.400 1.00149.80 C ANISOU 1871 CB ASN A 247 23378 19055 14486 -5470 2796 3737 C ATOM 1872 CG ASN A 247 -25.705 -61.296 -11.694 1.00149.71 C ANISOU 1872 CG ASN A 247 23100 19190 14593 -5632 2657 3518 C ATOM 1873 OD1 ASN A 247 -24.926 -60.514 -12.238 1.00150.96 O ANISOU 1873 OD1 ASN A 247 23164 19339 14855 -5290 2551 3300 O ATOM 1874 ND2 ASN A 247 -26.904 -61.574 -12.193 1.00150.28 N ANISOU 1874 ND2 ASN A 247 23042 19409 14648 -6169 2650 3593 N ATOM 1875 N ALA A 248 -22.386 -61.749 -10.005 1.00140.45 N ANISOU 1875 N ALA A 248 22608 17363 13395 -4400 2725 3564 N ATOM 1876 CA ALA A 248 -21.005 -61.533 -10.420 1.00141.40 C ANISOU 1876 CA ALA A 248 22871 17231 13622 -3969 2647 3424 C ATOM 1877 C ALA A 248 -20.891 -61.141 -11.887 1.00142.66 C ANISOU 1877 C ALA A 248 22973 17302 13929 -4049 2544 3180 C ATOM 1878 O ALA A 248 -19.878 -60.552 -12.278 1.00144.71 O ANISOU 1878 O ALA A 248 23178 17511 14293 -3675 2455 3037 O ATOM 1879 CB ALA A 248 -20.173 -62.787 -10.150 1.00144.29 C ANISOU 1879 CB ALA A 248 23774 17092 13956 -3854 2754 3576 C ATOM 1880 N ALA A 249 -21.899 -61.452 -12.704 1.00148.97 N ANISOU 1880 N ALA A 249 23777 18092 14733 -4537 2545 3141 N ATOM 1881 CA ALA A 249 -21.832 -61.107 -14.120 1.00144.56 C ANISOU 1881 CA ALA A 249 23186 17449 14293 -4634 2443 2912 C ATOM 1882 C ALA A 249 -22.033 -59.612 -14.337 1.00139.44 C ANISOU 1882 C ALA A 249 21989 17275 13716 -4466 2313 2750 C ATOM 1883 O ALA A 249 -21.364 -59.006 -15.182 1.00126.82 O ANISOU 1883 O ALA A 249 20328 15625 12234 -4251 2217 2555 O ATOM 1884 CB ALA A 249 -22.867 -61.909 -14.907 1.00143.97 C ANISOU 1884 CB ALA A 249 23299 17226 14177 -5241 2459 2932 C ATOM 1885 N GLN A 250 -22.953 -59.001 -13.585 1.00146.14 N ANISOU 1885 N GLN A 250 22451 18584 14491 -4550 2322 2837 N ATOM 1886 CA GLN A 250 -23.184 -57.567 -13.721 1.00143.45 C ANISOU 1886 CA GLN A 250 21618 18686 14202 -4367 2218 2695 C ATOM 1887 C GLN A 250 -21.983 -56.756 -13.252 1.00143.23 C ANISOU 1887 C GLN A 250 21524 18683 14216 -3813 2152 2604 C ATOM 1888 O GLN A 250 -21.691 -55.699 -13.823 1.00148.82 O ANISOU 1888 O GLN A 250 21979 19548 15018 -3618 2036 2419 O ATOM 1889 CB GLN A 250 -24.438 -57.162 -12.944 1.00147.20 C ANISOU 1889 CB GLN A 250 21729 19632 14568 -4545 2280 2839 C ATOM 1890 CG GLN A 250 -25.730 -57.704 -13.533 1.00155.05 C ANISOU 1890 CG GLN A 250 22654 20717 15541 -5119 2305 2930 C ATOM 1891 CD GLN A 250 -26.914 -57.537 -12.601 1.00161.04 C ANISOU 1891 CD GLN A 250 23092 21916 16179 -5286 2411 3147 C ATOM 1892 OE1 GLN A 250 -26.749 -57.269 -11.411 1.00163.54 O ANISOU 1892 OE1 GLN A 250 23349 22390 16400 -4995 2497 3248 O ATOM 1893 NE2 GLN A 250 -28.118 -57.695 -13.138 1.00162.41 N ANISOU 1893 NE2 GLN A 250 23055 22304 16349 -5757 2405 3232 N ATOM 1894 N VAL A 251 -21.278 -57.230 -12.225 1.00138.24 N ANISOU 1894 N VAL A 251 21115 17901 13510 -3570 2214 2743 N ATOM 1895 CA VAL A 251 -20.084 -56.529 -11.767 1.00124.40 C ANISOU 1895 CA VAL A 251 19312 16166 11788 -3077 2126 2682 C ATOM 1896 C VAL A 251 -18.915 -56.768 -12.714 1.00129.04 C ANISOU 1896 C VAL A 251 20120 16387 12522 -2894 2066 2569 C ATOM 1897 O VAL A 251 -18.076 -55.879 -12.905 1.00129.13 O ANISOU 1897 O VAL A 251 19967 16475 12621 -2568 1946 2445 O ATOM 1898 CB VAL A 251 -19.733 -56.949 -10.330 1.00108.61 C ANISOU 1898 CB VAL A 251 17463 14158 9644 -2883 2196 2888 C ATOM 1899 N LYS A 252 -18.834 -57.956 -13.318 1.00136.91 N ANISOU 1899 N LYS A 252 21502 16978 13542 -3097 2156 2617 N ATOM 1900 CA LYS A 252 -17.746 -58.236 -14.249 1.00133.89 C ANISOU 1900 CA LYS A 252 21357 16233 13284 -2902 2137 2524 C ATOM 1901 C LYS A 252 -17.906 -57.447 -15.541 1.00132.67 C ANISOU 1901 C LYS A 252 20988 16172 13248 -2981 2034 2290 C ATOM 1902 O LYS A 252 -16.921 -56.942 -16.092 1.00134.51 O ANISOU 1902 O LYS A 252 21176 16335 13598 -2676 1963 2179 O ATOM 1903 CB LYS A 252 -17.677 -59.735 -14.542 1.00135.30 C ANISOU 1903 CB LYS A 252 22060 15923 13424 -3095 2283 2636 C ATOM 1904 N ASP A 253 -19.139 -57.330 -16.040 1.00121.97 N ANISOU 1904 N ASP A 253 19487 14992 11865 -3392 2024 2230 N ATOM 1905 CA ASP A 253 -19.368 -56.575 -17.268 1.00110.03 C ANISOU 1905 CA ASP A 253 17764 13590 10451 -3482 1920 2020 C ATOM 1906 C ASP A 253 -19.107 -55.089 -17.058 1.00104.73 C ANISOU 1906 C ASP A 253 16649 13302 9843 -3169 1796 1909 C ATOM 1907 O ASP A 253 -18.566 -54.417 -17.945 1.00105.80 O ANISOU 1907 O ASP A 253 16679 13427 10095 -3012 1706 1744 O ATOM 1908 CB ASP A 253 -20.793 -56.806 -17.769 1.00 99.54 C ANISOU 1908 CB ASP A 253 16356 12401 9066 -4009 1923 2020 C ATOM 1909 N ALA A 254 -19.475 -54.559 -15.890 1.00 98.85 N ANISOU 1909 N ALA A 254 15667 12882 9011 -3071 1795 1999 N ATOM 1910 CA ALA A 254 -19.264 -53.142 -15.616 1.00102.51 C ANISOU 1910 CA ALA A 254 15760 13684 9504 -2782 1681 1893 C ATOM 1911 C ALA A 254 -17.798 -52.834 -15.336 1.00111.94 C ANISOU 1911 C ALA A 254 17027 14741 10764 -2350 1605 1873 C ATOM 1912 O ALA A 254 -17.289 -51.793 -15.765 1.00110.90 O ANISOU 1912 O ALA A 254 16685 14727 10726 -2140 1483 1728 O ATOM 1913 CB ALA A 254 -20.137 -52.699 -14.443 1.00100.57 C ANISOU 1913 CB ALA A 254 15287 13810 9113 -2805 1723 1997 C ATOM 1914 N LEU A 255 -17.104 -53.722 -14.619 1.00123.41 N ANISOU 1914 N LEU A 255 18767 15953 12168 -2218 1671 2034 N ATOM 1915 CA LEU A 255 -15.690 -53.493 -14.340 1.00134.56 C ANISOU 1915 CA LEU A 255 20228 17257 13644 -1816 1591 2057 C ATOM 1916 C LEU A 255 -14.837 -53.660 -15.591 1.00135.84 C ANISOU 1916 C LEU A 255 20505 17138 13969 -1718 1575 1961 C ATOM 1917 O LEU A 255 -13.787 -53.019 -15.713 1.00135.27 O ANISOU 1917 O LEU A 255 20317 17086 13993 -1408 1468 1923 O ATOM 1918 CB LEU A 255 -15.209 -54.436 -13.237 1.00137.22 C ANISOU 1918 CB LEU A 255 20833 17427 13878 -1694 1671 2284 C ATOM 1919 N THR A 256 -15.265 -54.514 -16.525 1.00133.53 N ANISOU 1919 N THR A 256 20452 16585 13700 -1984 1679 1931 N ATOM 1920 CA THR A 256 -14.547 -54.641 -17.788 1.00127.62 C ANISOU 1920 CA THR A 256 19833 15574 13083 -1897 1683 1825 C ATOM 1921 C THR A 256 -14.703 -53.384 -18.634 1.00128.42 C ANISOU 1921 C THR A 256 19589 15922 13281 -1892 1551 1618 C ATOM 1922 O THR A 256 -13.743 -52.932 -19.270 1.00134.13 O ANISOU 1922 O THR A 256 20258 16577 14128 -1641 1495 1548 O ATOM 1923 CB THR A 256 -15.040 -55.869 -18.555 1.00117.43 C ANISOU 1923 CB THR A 256 18938 13925 11753 -2212 1823 1832 C ATOM 1924 OG1 THR A 256 -14.891 -57.037 -17.738 1.00114.96 O ANISOU 1924 OG1 THR A 256 18970 13362 11346 -2209 1953 2035 O ATOM 1925 CG2 THR A 256 -14.245 -56.053 -19.840 1.00108.80 C ANISOU 1925 CG2 THR A 256 18036 12533 10770 -2085 1854 1728 C ATOM 1926 N LYS A 257 -15.904 -52.801 -18.648 1.00120.72 N ANISOU 1926 N LYS A 257 18368 15246 12253 -2157 1508 1537 N ATOM 1927 CA LYS A 257 -16.113 -51.556 -19.377 1.00109.63 C ANISOU 1927 CA LYS A 257 16629 14095 10931 -2138 1385 1355 C ATOM 1928 C LYS A 257 -15.369 -50.395 -18.732 1.00102.79 C ANISOU 1928 C LYS A 257 15498 13454 10104 -1785 1258 1332 C ATOM 1929 O LYS A 257 -15.026 -49.424 -19.416 1.00100.39 O ANISOU 1929 O LYS A 257 14990 13251 9903 -1664 1154 1194 O ATOM 1930 CB LYS A 257 -17.607 -51.242 -19.468 1.00103.95 C ANISOU 1930 CB LYS A 257 15699 13662 10136 -2483 1383 1313 C ATOM 1931 CG LYS A 257 -18.407 -52.255 -20.270 1.00103.56 C ANISOU 1931 CG LYS A 257 15876 13423 10048 -2898 1462 1319 C ATOM 1932 CD LYS A 257 -19.895 -51.947 -20.222 1.00105.34 C ANISOU 1932 CD LYS A 257 15838 13991 10197 -3241 1451 1331 C ATOM 1933 CE LYS A 257 -20.699 -52.991 -20.979 1.00110.30 C ANISOU 1933 CE LYS A 257 16698 14437 10774 -3708 1500 1357 C ATOM 1934 NZ LYS A 257 -22.162 -52.718 -20.920 1.00106.47 N ANISOU 1934 NZ LYS A 257 15911 14324 10218 -4059 1482 1411 N ATOM 1935 N MET A 258 -15.110 -50.472 -17.425 1.00101.92 N ANISOU 1935 N MET A 258 15404 13418 9902 -1633 1257 1469 N ATOM 1936 CA MET A 258 -14.371 -49.409 -16.754 1.00 88.20 C ANISOU 1936 CA MET A 258 13461 11874 8174 -1327 1115 1453 C ATOM 1937 C MET A 258 -12.877 -49.499 -17.038 1.00 86.82 C ANISOU 1937 C MET A 258 13369 11493 8125 -1036 1056 1495 C ATOM 1938 O MET A 258 -12.211 -48.469 -17.192 1.00 75.47 O ANISOU 1938 O MET A 258 11726 10181 6769 -843 911 1419 O ATOM 1939 CB MET A 258 -14.631 -49.451 -15.249 1.00 80.17 C ANISOU 1939 CB MET A 258 12454 11019 6989 -1276 1124 1587 C ATOM 1940 CG MET A 258 -16.010 -48.961 -14.847 1.00 83.66 C ANISOU 1940 CG MET A 258 12716 11766 7306 -1472 1164 1548 C ATOM 1941 SD MET A 258 -16.203 -48.828 -13.060 1.00 91.49 S ANISOU 1941 SD MET A 258 13721 12963 8076 -1348 1177 1692 S ATOM 1942 CE MET A 258 -14.873 -47.694 -12.666 1.00 76.36 C ANISOU 1942 CE MET A 258 11711 11112 6192 -978 957 1626 C ATOM 1943 N ARG A 259 -12.332 -50.716 -17.104 1.00 96.36 N ANISOU 1943 N ARG A 259 14877 12387 9349 -996 1172 1633 N ATOM 1944 CA ARG A 259 -10.923 -50.870 -17.452 1.00101.60 C ANISOU 1944 CA ARG A 259 15605 12860 10138 -698 1147 1704 C ATOM 1945 C ARG A 259 -10.661 -50.432 -18.887 1.00104.12 C ANISOU 1945 C ARG A 259 15845 13109 10608 -691 1132 1547 C ATOM 1946 O ARG A 259 -9.645 -49.785 -19.169 1.00104.27 O ANISOU 1946 O ARG A 259 15706 13166 10745 -446 1032 1545 O ATOM 1947 CB ARG A 259 -10.482 -52.319 -17.244 1.00114.81 C ANISOU 1947 CB ARG A 259 17647 14195 11782 -638 1310 1896 C ATOM 1948 CG ARG A 259 -9.086 -52.618 -17.767 1.00123.57 C ANISOU 1948 CG ARG A 259 18841 15085 13026 -318 1335 1993 C ATOM 1949 CD ARG A 259 -8.731 -54.086 -17.612 1.00132.75 C ANISOU 1949 CD ARG A 259 20408 15885 14147 -244 1527 2185 C ATOM 1950 NE ARG A 259 -7.547 -54.443 -18.388 1.00136.95 N ANISOU 1950 NE ARG A 259 21048 16177 14809 52 1606 2264 N ATOM 1951 CZ ARG A 259 -6.305 -54.412 -17.916 1.00140.50 C ANISOU 1951 CZ ARG A 259 21409 16652 15324 416 1560 2463 C ATOM 1952 NH1 ARG A 259 -6.078 -54.041 -16.664 1.00143.05 N ANISOU 1952 NH1 ARG A 259 21556 17216 15582 507 1413 2589 N ATOM 1953 NH2 ARG A 259 -5.289 -54.754 -18.698 1.00141.00 N ANISOU 1953 NH2 ARG A 259 21557 16508 15507 690 1661 2549 N ATOM 1954 N ALA A 260 -11.567 -50.771 -19.807 1.00114.70 N ANISOU 1954 N ALA A 260 17287 14354 11938 -973 1223 1426 N ATOM 1955 CA ALA A 260 -11.404 -50.348 -21.193 1.00117.12 C ANISOU 1955 CA ALA A 260 17535 14603 12364 -985 1209 1271 C ATOM 1956 C ALA A 260 -11.564 -48.839 -21.333 1.00107.16 C ANISOU 1956 C ALA A 260 15886 13674 11157 -951 1037 1126 C ATOM 1957 O ALA A 260 -10.860 -48.206 -22.128 1.00114.14 O ANISOU 1957 O ALA A 260 16646 14554 12167 -798 975 1054 O ATOM 1958 CB ALA A 260 -12.405 -51.081 -22.087 1.00125.34 C ANISOU 1958 CB ALA A 260 18796 15477 13351 -1333 1323 1182 C ATOM 1959 N ALA A 261 -12.482 -48.245 -20.566 1.00 81.54 N ANISOU 1959 N ALA A 261 12458 10711 7811 -1080 972 1091 N ATOM 1960 CA ALA A 261 -12.667 -46.800 -20.625 1.00 83.39 C ANISOU 1960 CA ALA A 261 12365 11242 8077 -1026 823 959 C ATOM 1961 C ALA A 261 -11.517 -46.059 -19.956 1.00 97.53 C ANISOU 1961 C ALA A 261 14028 13114 9913 -723 680 1014 C ATOM 1962 O ALA A 261 -11.172 -44.948 -20.373 1.00105.87 O ANISOU 1962 O ALA A 261 14874 14298 11054 -624 553 909 O ATOM 1963 CB ALA A 261 -13.996 -46.410 -19.979 1.00 79.27 C ANISOU 1963 CB ALA A 261 11707 10993 7418 -1219 826 924 C ATOM 1964 N ALA A 262 -10.916 -46.652 -18.921 1.00104.80 N ANISOU 1964 N ALA A 262 15078 13967 10774 -588 687 1187 N ATOM 1965 CA ALA A 262 -9.790 -46.008 -18.253 1.00 99.79 C ANISOU 1965 CA ALA A 262 14326 13419 10170 -328 525 1265 C ATOM 1966 C ALA A 262 -8.577 -45.930 -19.171 1.00 99.83 C ANISOU 1966 C ALA A 262 14286 13285 10360 -143 492 1293 C ATOM 1967 O ALA A 262 -7.881 -44.908 -19.201 1.00 98.05 O ANISOU 1967 O ALA A 262 13852 13192 10209 -10 324 1267 O ATOM 1968 CB ALA A 262 -9.443 -46.754 -16.966 1.00 97.03 C ANISOU 1968 CB ALA A 262 14133 13032 9704 -234 540 1467 C ATOM 1969 N LEU A 263 -8.305 -46.998 -19.924 1.00 99.87 N ANISOU 1969 N LEU A 263 14499 13016 10431 -130 658 1356 N ATOM 1970 CA LEU A 263 -7.196 -46.963 -20.870 1.00 98.81 C ANISOU 1970 CA LEU A 263 14328 12750 10465 66 667 1394 C ATOM 1971 C LEU A 263 -7.491 -46.036 -22.042 1.00102.60 C ANISOU 1971 C LEU A 263 14636 13309 11037 -21 621 1191 C ATOM 1972 O LEU A 263 -6.568 -45.423 -22.592 1.00105.14 O ANISOU 1972 O LEU A 263 14797 13657 11495 148 545 1204 O ATOM 1973 CB LEU A 263 -6.880 -48.374 -21.368 1.00 97.11 C ANISOU 1973 CB LEU A 263 14435 12195 10267 124 887 1509 C ATOM 1974 CG LEU A 263 -6.514 -49.400 -20.294 1.00100.76 C ANISOU 1974 CG LEU A 263 15101 12537 10645 241 958 1736 C ATOM 1975 CD1 LEU A 263 -5.975 -50.674 -20.928 1.00 98.13 C ANISOU 1975 CD1 LEU A 263 15094 11840 10353 372 1182 1858 C ATOM 1976 CD2 LEU A 263 -5.513 -48.822 -19.303 1.00104.99 C ANISOU 1976 CD2 LEU A 263 15418 13270 11203 477 774 1899 C ATOM 1977 N ASP A 264 -8.761 -45.924 -22.441 1.00 98.45 N ANISOU 1977 N ASP A 264 14129 12837 10442 -286 664 1023 N ATOM 1978 CA ASP A 264 -9.130 -44.934 -23.447 1.00 96.79 C ANISOU 1978 CA ASP A 264 13731 12744 10301 -369 599 837 C ATOM 1979 C ASP A 264 -8.895 -43.521 -22.933 1.00 90.11 C ANISOU 1979 C ASP A 264 12598 12165 9476 -275 395 787 C ATOM 1980 O ASP A 264 -8.396 -42.658 -23.665 1.00 96.42 O ANISOU 1980 O ASP A 264 13230 13014 10392 -194 309 718 O ATOM 1981 CB ASP A 264 -10.591 -45.113 -23.858 1.00107.01 C ANISOU 1981 CB ASP A 264 15078 14082 11500 -677 671 702 C ATOM 1982 CG ASP A 264 -10.741 -45.753 -25.223 1.00118.30 C ANISOU 1982 CG ASP A 264 16688 15289 12971 -796 795 632 C ATOM 1983 OD1 ASP A 264 -10.958 -46.981 -25.287 1.00124.96 O ANISOU 1983 OD1 ASP A 264 17831 15900 13749 -907 938 694 O ATOM 1984 OD2 ASP A 264 -10.636 -45.027 -26.234 1.00121.84 O ANISOU 1984 OD2 ASP A 264 17005 15784 13505 -781 747 516 O ATOM 1985 N ALA A 265 -9.248 -43.266 -21.671 1.00 88.97 N ANISOU 1985 N ALA A 265 12417 12180 9205 -287 319 822 N ATOM 1986 CA ALA A 265 -9.046 -41.941 -21.099 1.00 90.55 C ANISOU 1986 CA ALA A 265 12411 12603 9389 -205 124 768 C ATOM 1987 C ALA A 265 -7.570 -41.646 -20.867 1.00107.81 C ANISOU 1987 C ALA A 265 14520 14766 11676 13 -15 897 C ATOM 1988 O ALA A 265 -7.167 -40.477 -20.864 1.00115.94 O ANISOU 1988 O ALA A 265 15376 15927 12749 68 -189 839 O ATOM 1989 CB ALA A 265 -9.829 -41.809 -19.793 1.00 79.61 C ANISOU 1989 CB ALA A 265 11056 11380 7813 -267 100 775 C ATOM 1990 N GLN A 266 -6.750 -42.682 -20.674 1.00119.17 N ANISOU 1990 N GLN A 266 16085 16043 13153 136 56 1087 N ATOM 1991 CA GLN A 266 -5.321 -42.460 -20.480 1.00117.56 C ANISOU 1991 CA GLN A 266 15769 15846 13054 348 -74 1254 C ATOM 1992 C GLN A 266 -4.650 -42.022 -21.775 1.00111.82 C ANISOU 1992 C GLN A 266 14901 15068 12516 424 -72 1223 C ATOM 1993 O GLN A 266 -3.788 -41.136 -21.766 1.00127.12 O ANISOU 1993 O GLN A 266 16637 17120 14543 515 -250 1270 O ATOM 1994 CB GLN A 266 -4.658 -43.725 -19.933 1.00129.03 C ANISOU 1994 CB GLN A 266 17386 17148 14491 489 24 1493 C ATOM 1995 CG GLN A 266 -3.176 -43.561 -19.633 1.00138.66 C ANISOU 1995 CG GLN A 266 18457 18414 15812 716 -115 1716 C ATOM 1996 CD GLN A 266 -2.543 -44.827 -19.090 1.00141.69 C ANISOU 1996 CD GLN A 266 19000 18658 16178 888 -4 1976 C ATOM 1997 OE1 GLN A 266 -3.191 -45.870 -19.001 1.00145.96 O ANISOU 1997 OE1 GLN A 266 19797 19027 16634 833 190 1980 O ATOM 1998 NE2 GLN A 266 -1.269 -44.742 -18.723 1.00141.74 N ANISOU 1998 NE2 GLN A 266 18854 18740 16263 1091 -132 2211 N ATOM 1999 N LYS A 267 -5.034 -42.628 -22.900 1.00142.64 N ANISOU 1999 N LYS A 267 11991 25058 17148 2101 -2124 4697 N ATOM 2000 CA LYS A 267 -4.478 -42.274 -24.205 1.00139.30 C ANISOU 2000 CA LYS A 267 11258 25019 16650 2216 -1856 4972 C ATOM 2001 C LYS A 267 -5.177 -41.032 -24.764 1.00133.89 C ANISOU 2001 C LYS A 267 10341 24069 16461 1665 -1802 5108 C ATOM 2002 O LYS A 267 -5.774 -41.038 -25.840 1.00137.14 O ANISOU 2002 O LYS A 267 10771 24523 16812 1830 -1590 5072 O ATOM 2003 CB LYS A 267 -4.591 -43.454 -25.162 1.00136.29 C ANISOU 2003 CB LYS A 267 11138 24901 15745 2948 -1617 4785 C ATOM 2004 N ALA A 268 -5.090 -39.949 -23.999 1.00130.96 N ANISOU 2004 N ALA A 268 9782 23408 16569 1027 -2012 5247 N ATOM 2005 CA ALA A 268 -5.706 -38.685 -24.382 1.00128.14 C ANISOU 2005 CA ALA A 268 9273 22707 16705 508 -2008 5384 C ATOM 2006 C ALA A 268 -4.647 -37.669 -24.792 1.00136.60 C ANISOU 2006 C ALA A 268 9945 24050 17905 219 -1986 5930 C ATOM 2007 O ALA A 268 -3.506 -37.728 -24.332 1.00139.66 O ANISOU 2007 O ALA A 268 10134 24772 18157 200 -2070 6120 O ATOM 2008 CB ALA A 268 -6.553 -38.140 -23.241 1.00120.80 C ANISOU 2008 CB ALA A 268 8494 21146 16258 -31 -2274 5082 C ATOM 2009 N HIS A 288 -1.046 -38.276 -14.604 1.00153.87 N ANISOU 2009 N HIS A 288 12277 26069 20116 -1003 -4124 4555 N ATOM 2010 CA HIS A 288 -1.042 -39.580 -15.255 1.00148.51 C ANISOU 2010 CA HIS A 288 11821 25751 18855 -220 -3920 4673 C ATOM 2011 C HIS A 288 -1.128 -40.708 -14.231 1.00154.33 C ANISOU 2011 C HIS A 288 12998 26569 19070 247 -4101 4451 C ATOM 2012 O HIS A 288 -0.347 -41.659 -14.270 1.00154.44 O ANISOU 2012 O HIS A 288 13126 27055 18498 951 -4027 4540 O ATOM 2013 CB HIS A 288 0.209 -39.744 -16.122 1.00142.43 C ANISOU 2013 CB HIS A 288 10681 25660 17774 174 -3707 5027 C ATOM 2014 CG HIS A 288 1.485 -39.405 -15.415 1.00140.59 C ANISOU 2014 CG HIS A 288 10069 25890 17458 69 -3882 5090 C ATOM 2015 ND1 HIS A 288 1.892 -38.107 -15.195 1.00140.50 N ANISOU 2015 ND1 HIS A 288 9647 25799 17938 -638 -4010 5171 N ATOM 2016 CD2 HIS A 288 2.447 -40.196 -14.884 1.00142.07 C ANISOU 2016 CD2 HIS A 288 10245 26625 17110 603 -3950 5064 C ATOM 2017 CE1 HIS A 288 3.048 -38.112 -14.556 1.00144.97 C ANISOU 2017 CE1 HIS A 288 9907 26890 18284 -571 -4158 5182 C ATOM 2018 NE2 HIS A 288 3.407 -39.367 -14.356 1.00144.67 N ANISOU 2018 NE2 HIS A 288 10090 27260 17617 188 -4122 5120 N ATOM 2019 N GLY A 289 -2.085 -40.593 -13.313 1.00148.20 N ANISOU 2019 N GLY A 289 12616 25216 18478 -140 -4273 4092 N ATOM 2020 CA GLY A 289 -2.323 -41.632 -12.331 1.00139.62 C ANISOU 2020 CA GLY A 289 12352 23812 16884 239 -4224 3708 C ATOM 2021 C GLY A 289 -3.378 -42.615 -12.792 1.00136.55 C ANISOU 2021 C GLY A 289 12802 22840 16240 558 -3859 3445 C ATOM 2022 O GLY A 289 -4.018 -43.287 -11.978 1.00135.41 O ANISOU 2022 O GLY A 289 13463 22143 15842 604 -3764 3048 O ATOM 2023 N PHE A 290 -3.566 -42.701 -14.111 1.00138.29 N ANISOU 2023 N PHE A 290 12823 23206 16514 758 -3648 3664 N ATOM 2024 CA PHE A 290 -4.576 -43.597 -14.664 1.00132.97 C ANISOU 2024 CA PHE A 290 12878 22021 15625 1025 -3308 3380 C ATOM 2025 C PHE A 290 -4.164 -45.056 -14.525 1.00132.71 C ANISOU 2025 C PHE A 290 13480 22074 14871 1845 -3188 3346 C ATOM 2026 O PHE A 290 -5.025 -45.933 -14.395 1.00126.07 O ANISOU 2026 O PHE A 290 13500 20602 13798 1959 -2955 2978 O ATOM 2027 CB PHE A 290 -4.838 -43.250 -16.132 1.00127.99 C ANISOU 2027 CB PHE A 290 11798 21611 15223 1057 -3140 3617 C ATOM 2028 CG PHE A 290 -5.651 -41.996 -16.331 1.00115.58 C ANISOU 2028 CG PHE A 290 9905 19682 14327 298 -3176 3541 C ATOM 2029 CD1 PHE A 290 -5.350 -40.832 -15.641 1.00120.37 C ANISOU 2029 CD1 PHE A 290 10053 20279 15404 -310 -3473 3622 C ATOM 2030 CD2 PHE A 290 -6.707 -41.978 -17.227 1.00103.11 C ANISOU 2030 CD2 PHE A 290 8488 17792 12898 229 -2930 3367 C ATOM 2031 CE1 PHE A 290 -6.093 -39.683 -15.827 1.00118.27 C ANISOU 2031 CE1 PHE A 290 9559 19627 15749 -942 -3527 3545 C ATOM 2032 CE2 PHE A 290 -7.451 -40.830 -17.420 1.00105.39 C ANISOU 2032 CE2 PHE A 290 8508 17770 13766 -377 -2976 3301 C ATOM 2033 CZ PHE A 290 -7.144 -39.682 -16.720 1.00110.98 C ANISOU 2033 CZ PHE A 290 8819 18403 14944 -948 -3276 3398 C ATOM 2034 N ASP A 291 -2.857 -45.334 -14.549 1.00145.25 N ANISOU 2034 N ASP A 291 14665 24438 16086 2422 -3349 3719 N ATOM 2035 CA ASP A 291 -2.388 -46.695 -14.315 1.00147.95 C ANISOU 2035 CA ASP A 291 15647 24855 15712 3282 -3283 3689 C ATOM 2036 C ASP A 291 -2.669 -47.143 -12.887 1.00144.75 C ANISOU 2036 C ASP A 291 16020 23889 15091 3185 -3337 3366 C ATOM 2037 O ASP A 291 -2.811 -48.344 -12.633 1.00149.36 O ANISOU 2037 O ASP A 291 17483 24108 15157 3729 -3189 3215 O ATOM 2038 CB ASP A 291 -0.893 -46.796 -14.620 1.00159.62 C ANISOU 2038 CB ASP A 291 16424 27409 16816 3944 -3475 4149 C ATOM 2039 N ILE A 292 -2.751 -46.199 -11.947 1.00141.74 N ANISOU 2039 N ILE A 292 15351 23420 15082 2511 -3549 3261 N ATOM 2040 CA ILE A 292 -3.123 -46.546 -10.580 1.00134.36 C ANISOU 2040 CA ILE A 292 15125 21976 13948 2369 -3587 2937 C ATOM 2041 C ILE A 292 -4.597 -46.925 -10.512 1.00132.45 C ANISOU 2041 C ILE A 292 15722 20785 13816 1979 -3284 2509 C ATOM 2042 O ILE A 292 -4.990 -47.814 -9.747 1.00133.49 O ANISOU 2042 O ILE A 292 16746 20423 13552 2139 -3155 2291 O ATOM 2043 CB ILE A 292 -2.791 -45.386 -9.624 1.00120.71 C ANISOU 2043 CB ILE A 292 12796 20483 12585 1770 -3924 2896 C ATOM 2044 N LEU A 293 -5.435 -46.258 -11.309 1.00138.78 N ANISOU 2044 N LEU A 293 16246 21351 15133 1459 -3160 2392 N ATOM 2045 CA LEU A 293 -6.852 -46.606 -11.358 1.00139.70 C ANISOU 2045 CA LEU A 293 17061 20684 15335 1088 -2862 1959 C ATOM 2046 C LEU A 293 -7.070 -47.924 -12.091 1.00144.78 C ANISOU 2046 C LEU A 293 18387 21091 15533 1668 -2562 1924 C ATOM 2047 O LEU A 293 -7.855 -48.768 -11.641 1.00149.06 O ANISOU 2047 O LEU A 293 19827 20988 15820 1600 -2337 1605 O ATOM 2048 CB LEU A 293 -7.642 -45.476 -12.021 1.00134.29 C ANISOU 2048 CB LEU A 293 15832 19898 15293 444 -2845 1840 C ATOM 2049 CG LEU A 293 -8.998 -45.775 -12.671 1.00121.93 C ANISOU 2049 CG LEU A 293 14702 17797 13830 195 -2516 1468 C ATOM 2050 CD1 LEU A 293 -10.023 -46.269 -11.663 1.00106.86 C ANISOU 2050 CD1 LEU A 293 13615 15227 11759 -177 -2355 984 C ATOM 2051 CD2 LEU A 293 -9.516 -44.538 -13.388 1.00123.06 C ANISOU 2051 CD2 LEU A 293 14161 18018 14578 -291 -2566 1458 C ATOM 2052 N VAL A 294 -6.381 -48.122 -13.218 1.00144.17 N ANISOU 2052 N VAL A 294 17899 21533 15345 2229 -2555 2240 N ATOM 2053 CA VAL A 294 -6.533 -49.362 -13.973 1.00138.87 C ANISOU 2053 CA VAL A 294 17854 20661 14250 2840 -2305 2170 C ATOM 2054 C VAL A 294 -6.010 -50.545 -13.169 1.00149.96 C ANISOU 2054 C VAL A 294 20087 21863 15026 3453 -2310 2191 C ATOM 2055 O VAL A 294 -6.556 -51.653 -13.242 1.00150.05 O ANISOU 2055 O VAL A 294 21027 21267 14716 3682 -2071 1955 O ATOM 2056 CB VAL A 294 -5.828 -49.246 -15.337 1.00128.88 C ANISOU 2056 CB VAL A 294 15878 20122 12968 3365 -2328 2513 C ATOM 2057 N GLY A 295 -4.947 -50.333 -12.391 1.00160.33 N ANISOU 2057 N GLY A 295 21096 23677 16147 3730 -2587 2469 N ATOM 2058 CA GLY A 295 -4.439 -51.396 -11.542 1.00167.50 C ANISOU 2058 CA GLY A 295 22794 24420 16430 4352 -2615 2510 C ATOM 2059 C GLY A 295 -5.407 -51.796 -10.448 1.00163.97 C ANISOU 2059 C GLY A 295 23285 23103 15912 3874 -2456 2176 C ATOM 2060 O GLY A 295 -5.466 -52.968 -10.065 1.00175.17 O ANISOU 2060 O GLY A 295 25699 24031 16826 4319 -2316 2130 O ATOM 2061 N GLN A 296 -6.176 -50.837 -9.929 1.00147.29 N ANISOU 2061 N GLN A 296 20890 20791 14282 2978 -2475 1948 N ATOM 2062 CA GLN A 296 -7.186 -51.155 -8.926 1.00131.77 C ANISOU 2062 CA GLN A 296 19738 18082 12248 2460 -2300 1612 C ATOM 2063 C GLN A 296 -8.420 -51.796 -9.548 1.00128.36 C ANISOU 2063 C GLN A 296 19973 16929 11868 2155 -1922 1276 C ATOM 2064 O GLN A 296 -9.076 -52.620 -8.901 1.00139.57 O ANISOU 2064 O GLN A 296 22345 17687 12997 2004 -1700 1079 O ATOM 2065 CB GLN A 296 -7.577 -49.896 -8.153 1.00116.04 C ANISOU 2065 CB GLN A 296 17181 16192 10717 1663 -2474 1436 C ATOM 2066 N ILE A 297 -8.755 -51.430 -10.787 1.00122.17 N ANISOU 2066 N ILE A 297 18697 16287 11436 2040 -1839 1209 N ATOM 2067 CA ILE A 297 -9.827 -52.121 -11.495 1.00123.64 C ANISOU 2067 CA ILE A 297 19471 15889 11619 1847 -1496 867 C ATOM 2068 C ILE A 297 -9.426 -53.563 -11.778 1.00141.32 C ANISOU 2068 C ILE A 297 22577 17819 13300 2614 -1362 950 C ATOM 2069 O ILE A 297 -10.249 -54.482 -11.685 1.00140.29 O ANISOU 2069 O ILE A 297 23375 16953 12978 2431 -1080 661 O ATOM 2070 CB ILE A 297 -10.192 -51.367 -12.787 1.00112.53 C ANISOU 2070 CB ILE A 297 17273 14812 10670 1647 -1466 796 C ATOM 2071 CG1 ILE A 297 -10.718 -49.968 -12.463 1.00100.51 C ANISOU 2071 CG1 ILE A 297 15039 13446 9703 877 -1591 674 C ATOM 2072 CG2 ILE A 297 -11.225 -52.145 -13.592 1.00111.47 C ANISOU 2072 CG2 ILE A 297 17700 14173 10480 1528 -1130 411 C ATOM 2073 CD1 ILE A 297 -11.154 -49.182 -13.682 1.00 97.19 C ANISOU 2073 CD1 ILE A 297 13899 13304 9724 675 -1557 624 C ATOM 2074 N ASP A 298 -8.153 -53.785 -12.116 1.00160.95 N ANISOU 2074 N ASP A 298 24783 20867 15506 3482 -1569 1335 N ATOM 2075 CA ASP A 298 -7.664 -55.146 -12.310 1.00166.44 C ANISOU 2075 CA ASP A 298 26330 21286 15624 4339 -1494 1419 C ATOM 2076 C ASP A 298 -7.711 -55.944 -11.014 1.00169.58 C ANISOU 2076 C ASP A 298 27768 21071 15596 4394 -1439 1427 C ATOM 2077 O ASP A 298 -7.856 -57.171 -11.046 1.00175.35 O ANISOU 2077 O ASP A 298 29548 21154 15922 4787 -1263 1353 O ATOM 2078 CB ASP A 298 -6.241 -55.119 -12.868 1.00170.04 C ANISOU 2078 CB ASP A 298 26158 22622 15828 5294 -1758 1829 C ATOM 2079 N ASP A 299 -7.589 -55.270 -9.867 1.00166.55 N ANISOU 2079 N ASP A 299 27134 20866 15283 4015 -1592 1517 N ATOM 2080 CA ASP A 299 -7.733 -55.960 -8.590 1.00159.88 C ANISOU 2080 CA ASP A 299 27253 19469 14023 4002 -1518 1532 C ATOM 2081 C ASP A 299 -9.192 -56.297 -8.311 1.00149.96 C ANISOU 2081 C ASP A 299 26744 17336 12898 3137 -1159 1141 C ATOM 2082 O ASP A 299 -9.496 -57.367 -7.770 1.00160.95 O ANISOU 2082 O ASP A 299 29267 18007 13880 3222 -954 1127 O ATOM 2083 CB ASP A 299 -7.152 -55.108 -7.462 1.00158.52 C ANISOU 2083 CB ASP A 299 26520 19849 13862 3882 -1806 1708 C ATOM 2084 CG ASP A 299 -5.665 -54.862 -7.624 1.00160.16 C ANISOU 2084 CG ASP A 299 26019 20970 13863 4725 -2158 2088 C ATOM 2085 OD1 ASP A 299 -4.986 -55.708 -8.242 1.00165.20 O ANISOU 2085 OD1 ASP A 299 26960 21701 14108 5613 -2165 2271 O ATOM 2086 OD2 ASP A 299 -5.176 -53.824 -7.131 1.00156.80 O ANISOU 2086 OD2 ASP A 299 24724 21195 13658 4497 -2434 2179 O ATOM 2087 N ALA A 300 -10.109 -55.395 -8.671 1.00135.18 N ANISOU 2087 N ALA A 300 24257 15530 11574 2299 -1078 829 N ATOM 2088 CA ALA A 300 -11.530 -55.680 -8.503 1.00129.58 C ANISOU 2088 CA ALA A 300 24137 14118 10978 1459 -732 413 C ATOM 2089 C ALA A 300 -11.998 -56.769 -9.459 1.00135.52 C ANISOU 2089 C ALA A 300 25608 14287 11595 1618 -451 217 C ATOM 2090 O ALA A 300 -12.948 -57.497 -9.149 1.00134.11 O ANISOU 2090 O ALA A 300 26298 13372 11285 1114 -139 -45 O ATOM 2091 CB ALA A 300 -12.350 -54.406 -8.703 1.00120.77 C ANISOU 2091 CB ALA A 300 22125 13310 10452 633 -749 108 C ATOM 2092 N LEU A 301 -11.350 -56.895 -10.620 1.00140.15 N ANISOU 2092 N LEU A 301 25835 15217 12200 2292 -557 325 N ATOM 2093 CA LEU A 301 -11.693 -57.967 -11.547 1.00149.38 C ANISOU 2093 CA LEU A 301 27694 15858 13205 2551 -333 108 C ATOM 2094 C LEU A 301 -11.292 -59.331 -11.002 1.00169.21 C ANISOU 2094 C LEU A 301 31473 17682 15137 3126 -257 272 C ATOM 2095 O LEU A 301 -11.952 -60.333 -11.299 1.00173.56 O ANISOU 2095 O LEU A 301 32954 17444 15548 2987 10 3 O ATOM 2096 CB LEU A 301 -11.032 -57.723 -12.903 1.00136.53 C ANISOU 2096 CB LEU A 301 25307 14877 11692 3209 -489 196 C ATOM 2097 CG LEU A 301 -11.697 -56.689 -13.811 1.00123.35 C ANISOU 2097 CG LEU A 301 22645 13658 10564 2658 -459 -48 C ATOM 2098 CD1 LEU A 301 -10.832 -56.410 -15.029 1.00132.05 C ANISOU 2098 CD1 LEU A 301 22951 15521 11700 3403 -640 174 C ATOM 2099 CD2 LEU A 301 -13.074 -57.175 -14.233 1.00117.64 C ANISOU 2099 CD2 LEU A 301 22442 12298 9957 1994 -118 -597 C ATOM 2100 N LYS A 302 -10.219 -59.391 -10.209 1.00181.36 N ANISOU 2100 N LYS A 302 33083 19499 16325 3778 -494 700 N ATOM 2101 CA LYS A 302 -9.804 -60.662 -9.626 1.00187.01 C ANISOU 2101 CA LYS A 302 35045 19560 16448 4405 -440 900 C ATOM 2102 C LYS A 302 -10.805 -61.158 -8.591 1.00174.72 C ANISOU 2102 C LYS A 302 34482 17126 14779 3609 -139 770 C ATOM 2103 O LYS A 302 -10.896 -62.367 -8.349 1.00179.50 O ANISOU 2103 O LYS A 302 36338 16880 14981 3862 34 817 O ATOM 2104 CB LYS A 302 -8.416 -60.524 -9.000 1.00194.52 C ANISOU 2104 CB LYS A 302 35731 21155 17021 5317 -784 1379 C ATOM 2105 N LEU A 303 -11.561 -60.248 -7.975 1.00169.08 N ANISOU 2105 N LEU A 303 33248 16601 14396 2653 -73 610 N ATOM 2106 CA LEU A 303 -12.560 -60.652 -6.993 1.00169.44 C ANISOU 2106 CA LEU A 303 34126 15940 14315 1835 232 480 C ATOM 2107 C LEU A 303 -13.849 -61.112 -7.663 1.00168.17 C ANISOU 2107 C LEU A 303 34394 15128 14376 1042 602 0 C ATOM 2108 O LEU A 303 -14.440 -62.117 -7.252 1.00181.32 O ANISOU 2108 O LEU A 303 37207 15917 15769 712 901 -56 O ATOM 2109 CB LEU A 303 -12.845 -59.498 -6.030 1.00137.73 C ANISOU 2109 CB LEU A 303 29362 12459 10511 1186 136 462 C ATOM 2110 CG LEU A 303 -11.635 -58.891 -5.317 1.00137.80 C ANISOU 2110 CG LEU A 303 28804 13203 10351 1833 -252 858 C ATOM 2111 CD1 LEU A 303 -12.064 -57.744 -4.413 1.00133.73 C ANISOU 2111 CD1 LEU A 303 27580 13141 10089 1104 -341 730 C ATOM 2112 CD2 LEU A 303 -10.887 -59.952 -4.525 1.00145.26 C ANISOU 2112 CD2 LEU A 303 30794 13774 10625 2603 -272 1265 C ATOM 2113 N ALA A 304 -14.296 -60.394 -8.696 1.00153.01 N ANISOU 2113 N ALA A 304 31566 13637 12933 721 589 -345 N ATOM 2114 CA ALA A 304 -15.544 -60.752 -9.363 1.00161.28 C ANISOU 2114 CA ALA A 304 32888 14203 14189 -42 922 -862 C ATOM 2115 C ALA A 304 -15.422 -62.061 -10.131 1.00181.56 C ANISOU 2115 C ALA A 304 36420 16055 16508 446 1051 -946 C ATOM 2116 O ALA A 304 -16.422 -62.764 -10.315 1.00188.52 O ANISOU 2116 O ALA A 304 38001 16237 17393 -210 1376 -1321 O ATOM 2117 CB ALA A 304 -15.980 -59.626 -10.300 1.00152.28 C ANISOU 2117 CB ALA A 304 30506 13776 13578 -378 844 -1185 C ATOM 2118 N ASN A 305 -14.215 -62.405 -10.587 1.00193.53 N ANISOU 2118 N ASN A 305 37980 17756 17797 1584 795 -632 N ATOM 2119 CA ASN A 305 -14.037 -63.647 -11.330 1.00200.09 C ANISOU 2119 CA ASN A 305 39744 17913 18369 2164 874 -740 C ATOM 2120 C ASN A 305 -14.117 -64.866 -10.420 1.00200.78 C ANISOU 2120 C ASN A 305 41354 16930 18003 2170 1064 -566 C ATOM 2121 O ASN A 305 -14.511 -65.948 -10.870 1.00209.26 O ANISOU 2121 O ASN A 305 43428 17129 18950 2147 1260 -811 O ATOM 2122 CB ASN A 305 -12.702 -63.627 -12.075 1.00204.55 C ANISOU 2122 CB ASN A 305 39853 19093 18774 3446 530 -463 C ATOM 2123 N GLU A 306 -13.753 -64.715 -9.149 1.00208.04 N ANISOU 2123 N GLU A 306 37414 15719 25915 -4282 -1538 6170 N ATOM 2124 CA GLU A 306 -13.773 -65.812 -8.192 1.00203.28 C ANISOU 2124 CA GLU A 306 36887 14868 25483 -4313 -1587 6721 C ATOM 2125 C GLU A 306 -15.110 -65.949 -7.474 1.00198.96 C ANISOU 2125 C GLU A 306 36351 14889 24355 -4915 -1698 7036 C ATOM 2126 O GLU A 306 -15.199 -66.696 -6.494 1.00192.62 O ANISOU 2126 O GLU A 306 35555 14039 23592 -4937 -1785 7567 O ATOM 2127 CB GLU A 306 -12.650 -65.636 -7.166 1.00194.48 C ANISOU 2127 CB GLU A 306 35536 13765 24594 -3692 -1844 7190 C ATOM 2128 N GLY A 307 -16.144 -65.250 -7.933 1.00191.77 N ANISOU 2128 N GLY A 307 35396 14542 22925 -5384 -1677 6755 N ATOM 2129 CA GLY A 307 -17.452 -65.333 -7.319 1.00196.60 C ANISOU 2129 CA GLY A 307 35928 15767 23003 -5935 -1738 7055 C ATOM 2130 C GLY A 307 -17.687 -64.394 -6.159 1.00197.24 C ANISOU 2130 C GLY A 307 35717 16705 22519 -5804 -1993 7428 C ATOM 2131 O GLY A 307 -18.738 -64.489 -5.512 1.00198.12 O ANISOU 2131 O GLY A 307 35705 17378 22195 -6177 -2010 7736 O ATOM 2132 N LYS A 308 -16.750 -63.494 -5.870 1.00199.20 N ANISOU 2132 N LYS A 308 35824 17100 22762 -5266 -2182 7394 N ATOM 2133 CA LYS A 308 -16.898 -62.535 -4.777 1.00203.40 C ANISOU 2133 CA LYS A 308 36013 18521 22749 -5052 -2413 7610 C ATOM 2134 C LYS A 308 -17.628 -61.310 -5.314 1.00201.04 C ANISOU 2134 C LYS A 308 35374 19000 22013 -5169 -2310 7124 C ATOM 2135 O LYS A 308 -17.030 -60.452 -5.968 1.00207.13 O ANISOU 2135 O LYS A 308 35930 19836 22936 -4824 -2302 6638 O ATOM 2136 CB LYS A 308 -15.539 -62.167 -4.193 1.00201.49 C ANISOU 2136 CB LYS A 308 35643 18161 22752 -4384 -2677 7720 C ATOM 2137 N VAL A 309 -18.927 -61.230 -5.040 1.00208.09 N ANISOU 2137 N VAL A 309 36192 20486 22388 -5648 -2219 7299 N ATOM 2138 CA VAL A 309 -19.736 -60.110 -5.511 1.00165.34 C ANISOU 2138 CA VAL A 309 30429 15835 16559 -5782 -2089 6926 C ATOM 2139 C VAL A 309 -19.709 -58.949 -4.525 1.00162.74 C ANISOU 2139 C VAL A 309 29793 16307 15735 -5403 -2232 6990 C ATOM 2140 O VAL A 309 -19.677 -57.785 -4.931 1.00157.95 O ANISOU 2140 O VAL A 309 28882 16138 14995 -5182 -2191 6557 O ATOM 2141 CB VAL A 309 -21.177 -60.583 -5.786 1.00167.59 C ANISOU 2141 CB VAL A 309 30745 16369 16564 -6497 -1898 7106 C ATOM 2142 N LYS A 310 -19.720 -59.241 -3.223 1.00173.16 N ANISOU 2142 N LYS A 310 31209 17821 16764 -5327 -2394 7527 N ATOM 2143 CA LYS A 310 -19.676 -58.176 -2.226 1.00175.48 C ANISOU 2143 CA LYS A 310 31296 18849 16531 -4978 -2533 7572 C ATOM 2144 C LYS A 310 -18.299 -57.526 -2.158 1.00173.29 C ANISOU 2144 C LYS A 310 30946 18377 16521 -4385 -2797 7288 C ATOM 2145 O LYS A 310 -18.197 -56.316 -1.926 1.00171.45 O ANISOU 2145 O LYS A 310 30483 18683 15978 -4097 -2864 7004 O ATOM 2146 CB LYS A 310 -20.075 -58.721 -0.856 1.00181.41 C ANISOU 2146 CB LYS A 310 32174 19883 16871 -5066 -2622 8217 C ATOM 2147 N GLU A 311 -17.234 -58.306 -2.358 1.00173.50 N ANISOU 2147 N GLU A 311 31157 17625 17140 -4198 -2941 7380 N ATOM 2148 CA GLU A 311 -15.889 -57.743 -2.304 1.00174.72 C ANISOU 2148 CA GLU A 311 31198 17582 17606 -3649 -3208 7188 C ATOM 2149 C GLU A 311 -15.586 -56.889 -3.528 1.00173.99 C ANISOU 2149 C GLU A 311 30859 17445 17804 -3481 -3078 6533 C ATOM 2150 O GLU A 311 -14.792 -55.945 -3.442 1.00176.63 O ANISOU 2150 O GLU A 311 30977 17939 18193 -3067 -3278 6292 O ATOM 2151 CB GLU A 311 -14.855 -58.860 -2.169 1.00180.27 C ANISOU 2151 CB GLU A 311 32129 17465 18900 -3473 -3360 7554 C ATOM 2152 N ALA A 312 -16.202 -57.200 -4.670 1.00176.46 N ANISOU 2152 N ALA A 312 31200 17551 18296 -3818 -2763 6256 N ATOM 2153 CA ALA A 312 -15.960 -56.423 -5.880 1.00149.83 C ANISOU 2153 CA ALA A 312 27592 14161 15175 -3682 -2620 5661 C ATOM 2154 C ALA A 312 -16.674 -55.077 -5.837 1.00145.34 C ANISOU 2154 C ALA A 312 26685 14439 14099 -3682 -2561 5378 C ATOM 2155 O ALA A 312 -16.149 -54.077 -6.339 1.00140.95 O ANISOU 2155 O ALA A 312 25859 14009 13686 -3363 -2591 4969 O ATOM 2156 CB ALA A 312 -16.394 -57.218 -7.112 1.00157.89 C ANISOU 2156 CB ALA A 312 28794 14699 16498 -4073 -2318 5461 C ATOM 2157 N GLN A 313 -17.870 -55.034 -5.244 1.00146.70 N ANISOU 2157 N GLN A 313 26853 15184 13702 -4021 -2455 5617 N ATOM 2158 CA GLN A 313 -18.612 -53.780 -5.162 1.00153.39 C ANISOU 2158 CA GLN A 313 27385 16825 14070 -3997 -2342 5393 C ATOM 2159 C GLN A 313 -17.898 -52.769 -4.274 1.00158.36 C ANISOU 2159 C GLN A 313 27907 17767 14495 -3505 -2606 5320 C ATOM 2160 O GLN A 313 -17.919 -51.565 -4.553 1.00158.75 O ANISOU 2160 O GLN A 313 27678 18201 14438 -3297 -2560 4938 O ATOM 2161 CB GLN A 313 -20.026 -54.038 -4.644 1.00145.76 C ANISOU 2161 CB GLN A 313 26436 16388 12556 -4440 -2145 5753 C ATOM 2162 CG GLN A 313 -20.908 -54.839 -5.588 1.00159.16 C ANISOU 2162 CG GLN A 313 28180 17905 14389 -5009 -1898 5792 C ATOM 2163 CD GLN A 313 -22.267 -55.147 -4.990 1.00163.10 C ANISOU 2163 CD GLN A 313 28661 18927 14382 -5453 -1733 6249 C ATOM 2164 OE1 GLN A 313 -22.450 -55.090 -3.773 1.00169.92 O ANISOU 2164 OE1 GLN A 313 29583 20143 14835 -5337 -1803 6623 O ATOM 2165 NE2 GLN A 313 -23.231 -55.473 -5.844 1.00158.49 N ANISOU 2165 NE2 GLN A 313 27989 18418 13811 -5976 -1517 6245 N ATOM 2166 N ALA A 314 -17.260 -53.239 -3.200 1.00167.09 N ANISOU 2166 N ALA A 314 29237 18704 15544 -3333 -2899 5692 N ATOM 2167 CA ALA A 314 -16.604 -52.325 -2.271 1.00173.13 C ANISOU 2167 CA ALA A 314 29952 19783 16048 -2930 -3203 5646 C ATOM 2168 C ALA A 314 -15.358 -51.700 -2.889 1.00169.05 C ANISOU 2168 C ALA A 314 29247 18923 16060 -2532 -3406 5262 C ATOM 2169 O ALA A 314 -15.051 -50.531 -2.628 1.00170.12 O ANISOU 2169 O ALA A 314 29215 19403 16019 -2257 -3553 4985 O ATOM 2170 CB ALA A 314 -16.253 -53.055 -0.976 1.00176.66 C ANISOU 2170 CB ALA A 314 30685 20162 16276 -2893 -3491 6196 C ATOM 2171 N ALA A 315 -14.628 -52.462 -3.708 1.00165.91 N ANISOU 2171 N ALA A 315 28882 17834 16322 -2491 -3402 5251 N ATOM 2172 CA ALA A 315 -13.413 -51.934 -4.321 1.00159.58 C ANISOU 2172 CA ALA A 315 27872 16693 16068 -2096 -3568 4952 C ATOM 2173 C ALA A 315 -13.727 -50.797 -5.286 1.00158.25 C ANISOU 2173 C ALA A 315 27378 16829 15919 -2049 -3356 4407 C ATOM 2174 O ALA A 315 -13.045 -49.766 -5.282 1.00158.45 O ANISOU 2174 O ALA A 315 27172 16984 16049 -1719 -3549 4153 O ATOM 2175 CB ALA A 315 -12.656 -53.054 -5.034 1.00155.94 C ANISOU 2175 CB ALA A 315 27536 15417 16295 -2049 -3515 5076 C ATOM 2176 N ALA A 316 -14.757 -50.965 -6.119 1.00160.65 N ANISOU 2176 N ALA A 316 27648 17257 16133 -2396 -2976 4248 N ATOM 2177 CA ALA A 316 -15.136 -49.903 -7.046 1.00152.58 C ANISOU 2177 CA ALA A 316 26292 16569 15113 -2374 -2761 3788 C ATOM 2178 C ALA A 316 -15.732 -48.707 -6.316 1.00160.37 C ANISOU 2178 C ALA A 316 27117 18274 15542 -2295 -2779 3693 C ATOM 2179 O ALA A 316 -15.578 -47.567 -6.768 1.00150.38 O ANISOU 2179 O ALA A 316 25553 17235 14349 -2082 -2748 3328 O ATOM 2180 CB ALA A 316 -16.124 -50.437 -8.082 1.00139.16 C ANISOU 2180 CB ALA A 316 24602 14855 13420 -2815 -2384 3700 C ATOM 2181 N GLU A 317 -16.412 -48.945 -5.194 1.00184.84 N ANISOU 2181 N GLU A 317 30420 21725 18086 -2450 -2804 4024 N ATOM 2182 CA GLU A 317 -16.985 -47.857 -4.414 1.00191.69 C ANISOU 2182 CA GLU A 317 31204 23252 18378 -2344 -2778 3943 C ATOM 2183 C GLU A 317 -15.918 -47.031 -3.706 1.00194.29 C ANISOU 2183 C GLU A 317 31540 23570 18711 -1926 -3170 3800 C ATOM 2184 O GLU A 317 -16.161 -45.862 -3.392 1.00195.23 O ANISOU 2184 O GLU A 317 31546 24126 18509 -1762 -3143 3549 O ATOM 2185 CB GLU A 317 -17.979 -48.422 -3.394 1.00198.61 C ANISOU 2185 CB GLU A 317 32320 24496 18647 -2613 -2671 4377 C ATOM 2186 CG GLU A 317 -18.731 -47.383 -2.570 1.00199.64 C ANISOU 2186 CG GLU A 317 32410 25329 18116 -2510 -2544 4325 C ATOM 2187 CD GLU A 317 -19.702 -46.558 -3.394 1.00197.89 C ANISOU 2187 CD GLU A 317 31842 25523 17823 -2598 -2135 4059 C ATOM 2188 OE1 GLU A 317 -20.095 -47.009 -4.492 1.00197.08 O ANISOU 2188 OE1 GLU A 317 31569 25267 18044 -2875 -1928 4030 O ATOM 2189 OE2 GLU A 317 -20.073 -45.455 -2.941 1.00198.68 O ANISOU 2189 OE2 GLU A 317 31853 26099 17537 -2391 -2019 3886 O ATOM 2190 N GLN A 318 -14.738 -47.603 -3.463 1.00194.03 N ANISOU 2190 N GLN A 318 31634 23036 19052 -1758 -3534 3966 N ATOM 2191 CA GLN A 318 -13.733 -46.909 -2.667 1.00196.85 C ANISOU 2191 CA GLN A 318 32014 23409 19372 -1428 -3977 3916 C ATOM 2192 C GLN A 318 -12.873 -45.972 -3.504 1.00192.69 C ANISOU 2192 C GLN A 318 31155 22694 19364 -1140 -4085 3501 C ATOM 2193 O GLN A 318 -12.314 -45.009 -2.966 1.00200.70 O ANISOU 2193 O GLN A 318 32124 23865 20268 -911 -4388 3332 O ATOM 2194 CB GLN A 318 -12.848 -47.926 -1.941 1.00201.47 C ANISOU 2194 CB GLN A 318 32839 23593 20118 -1378 -4354 4374 C ATOM 2195 N LEU A 319 -12.753 -46.224 -4.807 1.00182.36 N ANISOU 2195 N LEU A 319 29627 21054 18605 -1162 -3847 3337 N ATOM 2196 CA LEU A 319 -11.848 -45.433 -5.630 1.00168.55 C ANISOU 2196 CA LEU A 319 27544 19094 17402 -873 -3945 3011 C ATOM 2197 C LEU A 319 -12.524 -44.209 -6.238 1.00157.49 C ANISOU 2197 C LEU A 319 25855 18115 15867 -859 -3673 2589 C ATOM 2198 O LEU A 319 -11.932 -43.124 -6.259 1.00151.02 O ANISOU 2198 O LEU A 319 24823 17358 15200 -601 -3863 2334 O ATOM 2199 CB LEU A 319 -11.247 -46.308 -6.732 1.00163.51 C ANISOU 2199 CB LEU A 319 26829 17862 17437 -845 -3818 3055 C ATOM 2200 CG LEU A 319 -10.106 -45.699 -7.549 1.00161.35 C ANISOU 2200 CG LEU A 319 26211 17286 17809 -503 -3938 2832 C ATOM 2201 CD1 LEU A 319 -9.170 -44.893 -6.664 1.00162.26 C ANISOU 2201 CD1 LEU A 319 26241 17473 17940 -227 -4439 2869 C ATOM 2202 CD2 LEU A 319 -9.342 -46.803 -8.245 1.00164.41 C ANISOU 2202 CD2 LEU A 319 26644 17021 18804 -418 -3869 3013 C ATOM 2203 N LYS A 320 -13.748 -44.354 -6.732 1.00154.14 N ANISOU 2203 N LYS A 320 25403 17979 15184 -1141 -3243 2541 N ATOM 2204 CA LYS A 320 -14.472 -43.224 -7.303 1.00150.85 C ANISOU 2204 CA LYS A 320 24682 17993 14640 -1131 -2954 2211 C ATOM 2205 C LYS A 320 -15.961 -43.306 -6.984 1.00148.04 C ANISOU 2205 C LYS A 320 24408 18158 13685 -1433 -2604 2338 C ATOM 2206 O LYS A 320 -16.361 -43.242 -5.822 1.00153.50 O ANISOU 2206 O LYS A 320 25336 19144 13843 -1446 -2670 2507 O ATOM 2207 CB LYS A 320 -14.259 -43.159 -8.817 1.00152.12 C ANISOU 2207 CB LYS A 320 24520 17926 15351 -1122 -2740 1982 C ATOM 2208 N LYS A1230 -18.939 -31.576 -15.119 1.00 85.53 N ANISOU 2208 N LYS A1230 11927 12794 7776 -34 -138 265 N ATOM 2209 CA LYS A1230 -20.177 -32.168 -14.625 1.00101.90 C ANISOU 2209 CA LYS A1230 14160 15268 9290 -314 121 528 C ATOM 2210 C LYS A1230 -21.368 -31.744 -15.478 1.00104.91 C ANISOU 2210 C LYS A1230 14043 16192 9626 -462 572 742 C ATOM 2211 O LYS A1230 -22.402 -32.412 -15.496 1.00113.83 O ANISOU 2211 O LYS A1230 15173 17679 10397 -802 787 1035 O ATOM 2212 CB LYS A1230 -20.411 -31.779 -13.164 1.00105.05 C ANISOU 2212 CB LYS A1230 14928 15728 9261 -123 108 487 C ATOM 2213 N ASN A1231 -21.215 -30.630 -16.186 1.00 97.74 N ANISOU 2213 N ASN A1231 12684 15351 9101 -219 700 633 N ATOM 2214 CA ASN A1231 -22.277 -30.105 -17.036 1.00 99.23 C ANISOU 2214 CA ASN A1231 12333 16067 9303 -322 1115 871 C ATOM 2215 C ASN A1231 -21.655 -29.290 -18.168 1.00 90.72 C ANISOU 2215 C ASN A1231 10785 14893 8790 -131 1108 740 C ATOM 2216 O ASN A1231 -22.075 -28.171 -18.467 1.00 83.76 O ANISOU 2216 O ASN A1231 9477 14267 8080 83 1380 796 O ATOM 2217 CB ASN A1231 -23.266 -29.276 -16.216 1.00104.46 C ANISOU 2217 CB ASN A1231 12931 17100 9658 -128 1472 1000 C ATOM 2218 CG ASN A1231 -24.519 -28.922 -16.990 1.00109.08 C ANISOU 2218 CG ASN A1231 12951 18294 10200 -282 1919 1369 C ATOM 2219 OD1 ASN A1231 -24.848 -29.558 -17.992 1.00118.62 O ANISOU 2219 OD1 ASN A1231 13909 19718 11444 -661 1936 1574 O ATOM 2220 ND2 ASN A1231 -25.229 -27.900 -16.527 1.00102.82 N ANISOU 2220 ND2 ASN A1231 11964 17780 9324 9 2288 1468 N ATOM 2221 N LYS A1232 -20.636 -29.854 -18.811 1.00 90.75 N ANISOU 2221 N LYS A1232 10857 14520 9102 -189 818 592 N ATOM 2222 CA LYS A1232 -19.901 -29.121 -19.831 1.00 88.36 C ANISOU 2222 CA LYS A1232 10136 14089 9348 21 786 474 C ATOM 2223 C LYS A1232 -20.752 -28.959 -21.088 1.00 81.79 C ANISOU 2223 C LYS A1232 8772 13762 8542 -205 1112 724 C ATOM 2224 O LYS A1232 -21.505 -29.868 -21.453 1.00 71.06 O ANISOU 2224 O LYS A1232 7463 12685 6852 -629 1211 926 O ATOM 2225 CB LYS A1232 -18.598 -29.842 -20.173 1.00 70.13 C ANISOU 2225 CB LYS A1232 8047 11257 7343 36 433 293 C ATOM 2226 N PRO A1233 -20.666 -27.813 -21.763 1.00 84.84 N ANISOU 2226 N PRO A1233 8641 14280 9314 46 1264 739 N ATOM 2227 CA PRO A1233 -21.386 -27.650 -23.031 1.00 78.53 C ANISOU 2227 CA PRO A1233 7304 13980 8555 -173 1537 1006 C ATOM 2228 C PRO A1233 -20.827 -28.576 -24.099 1.00 73.73 C ANISOU 2228 C PRO A1233 6745 13246 8025 -441 1387 953 C ATOM 2229 O PRO A1233 -19.614 -28.773 -24.204 1.00 65.38 O ANISOU 2229 O PRO A1233 5871 11692 7279 -257 1135 709 O ATOM 2230 CB PRO A1233 -21.153 -26.177 -23.389 1.00 77.15 C ANISOU 2230 CB PRO A1233 6614 13843 8856 236 1680 1003 C ATOM 2231 CG PRO A1233 -20.742 -25.522 -22.104 1.00 78.84 C ANISOU 2231 CG PRO A1233 7130 13690 9136 611 1570 769 C ATOM 2232 CD PRO A1233 -19.995 -26.572 -21.344 1.00 86.96 C ANISOU 2232 CD PRO A1233 8789 14273 9977 518 1199 543 C ATOM 2233 N ARG A1234 -21.726 -29.144 -24.897 1.00 73.14 N ANISOU 2233 N ARG A1234 6509 13626 7657 -885 1552 1198 N ATOM 2234 CA ARG A1234 -21.340 -30.127 -25.898 1.00 78.22 C ANISOU 2234 CA ARG A1234 7292 14164 8266 -1202 1445 1127 C ATOM 2235 C ARG A1234 -22.362 -30.129 -27.024 1.00 81.31 C ANISOU 2235 C ARG A1234 7255 15192 8448 -1605 1669 1432 C ATOM 2236 O ARG A1234 -23.566 -30.022 -26.779 1.00 91.75 O ANISOU 2236 O ARG A1234 8446 16915 9499 -1804 1802 1711 O ATOM 2237 CB ARG A1234 -21.219 -31.524 -25.277 1.00 78.13 C ANISOU 2237 CB ARG A1234 7945 13811 7931 -1488 1245 1013 C ATOM 2238 CG ARG A1234 -20.927 -32.634 -26.269 1.00 77.65 C ANISOU 2238 CG ARG A1234 8117 13602 7783 -1847 1176 924 C ATOM 2239 CD ARG A1234 -20.584 -33.926 -25.551 1.00 71.12 C ANISOU 2239 CD ARG A1234 7968 12292 6762 -2017 970 787 C ATOM 2240 NE ARG A1234 -20.507 -35.056 -26.469 1.00 75.03 N ANISOU 2240 NE ARG A1234 8748 12651 7110 -2420 953 709 N ATOM 2241 CZ ARG A1234 -20.105 -36.273 -26.119 1.00 84.45 C ANISOU 2241 CZ ARG A1234 10535 13354 8200 -2580 803 578 C ATOM 2242 NH1 ARG A1234 -19.738 -36.515 -24.869 1.00 91.08 N ANISOU 2242 NH1 ARG A1234 11708 13836 9062 -2375 634 546 N ATOM 2243 NH2 ARG A1234 -20.067 -37.246 -27.019 1.00 89.68 N ANISOU 2243 NH2 ARG A1234 11476 13872 8728 -2945 825 481 N ATOM 2244 N ASN A1235 -21.869 -30.248 -28.257 1.00 72.03 N ANISOU 2244 N ASN A1235 5919 14019 7429 -1683 1659 1367 N ATOM 2245 CA ASN A1235 -22.718 -30.278 -29.448 1.00 73.25 C ANISOU 2245 CA ASN A1235 5939 14421 7473 -1949 1657 1527 C ATOM 2246 C ASN A1235 -22.206 -31.392 -30.356 1.00 72.82 C ANISOU 2246 C ASN A1235 6089 14373 7209 -2360 1640 1392 C ATOM 2247 O ASN A1235 -21.221 -31.209 -31.078 1.00 67.20 O ANISOU 2247 O ASN A1235 5239 13528 6768 -2165 1677 1240 O ATOM 2248 CB ASN A1235 -22.716 -28.931 -30.160 1.00 76.23 C ANISOU 2248 CB ASN A1235 6029 14639 8295 -1504 1639 1553 C ATOM 2249 CG ASN A1235 -23.568 -28.930 -31.415 1.00 69.43 C ANISOU 2249 CG ASN A1235 5147 13917 7317 -1705 1555 1682 C ATOM 2250 OD1 ASN A1235 -24.456 -29.766 -31.578 1.00 69.91 O ANISOU 2250 OD1 ASN A1235 5339 14235 6990 -2131 1481 1795 O ATOM 2251 ND2 ASN A1235 -23.300 -27.987 -32.311 1.00 66.24 N ANISOU 2251 ND2 ASN A1235 4589 13342 7238 -1419 1546 1670 N ATOM 2252 N ASP A1236 -22.879 -32.543 -30.321 1.00 76.30 N ANISOU 2252 N ASP A1236 6891 14924 7177 -2926 1590 1442 N ATOM 2253 CA ASP A1236 -22.483 -33.673 -31.152 1.00 83.79 C ANISOU 2253 CA ASP A1236 8225 15715 7897 -3335 1547 1250 C ATOM 2254 C ASP A1236 -22.775 -33.453 -32.630 1.00 92.42 C ANISOU 2254 C ASP A1236 9080 17059 8977 -3445 1534 1287 C ATOM 2255 O ASP A1236 -22.393 -34.296 -33.449 1.00 99.69 O ANISOU 2255 O ASP A1236 10273 17948 9658 -3818 1582 1120 O ATOM 2256 CB ASP A1236 -23.177 -34.947 -30.668 1.00 94.42 C ANISOU 2256 CB ASP A1236 10107 16983 8785 -3894 1435 1277 C ATOM 2257 CG ASP A1236 -22.600 -35.463 -29.364 1.00106.58 C ANISOU 2257 CG ASP A1236 12163 17907 10427 -3640 1290 1094 C ATOM 2258 OD1 ASP A1236 -21.368 -35.365 -29.178 1.00104.54 O ANISOU 2258 OD1 ASP A1236 12078 17097 10545 -3159 1214 818 O ATOM 2259 OD2 ASP A1236 -23.376 -35.966 -28.524 1.00112.91 O ANISOU 2259 OD2 ASP A1236 13172 18797 10934 -3925 1245 1264 O ATOM 2260 N ASP A1237 -23.437 -32.355 -32.991 1.00 93.31 N ANISOU 2260 N ASP A1237 8820 17304 9329 -3096 1450 1467 N ATOM 2261 CA ASP A1237 -23.692 -32.015 -34.383 1.00 91.02 C ANISOU 2261 CA ASP A1237 8369 17165 9051 -3097 1381 1510 C ATOM 2262 C ASP A1237 -22.672 -31.031 -34.940 1.00 87.25 C ANISOU 2262 C ASP A1237 7643 16475 9032 -2567 1475 1428 C ATOM 2263 O ASP A1237 -22.838 -30.555 -36.068 1.00 91.32 O ANISOU 2263 O ASP A1237 8022 17081 9594 -2494 1431 1494 O ATOM 2264 CB ASP A1237 -25.105 -31.448 -34.540 1.00 88.27 C ANISOU 2264 CB ASP A1237 7837 17060 8641 -3093 1231 1788 C ATOM 2265 CG ASP A1237 -26.181 -32.490 -34.309 1.00 99.90 C ANISOU 2265 CG ASP A1237 9505 18787 9666 -3665 1089 1894 C ATOM 2266 OD1 ASP A1237 -25.833 -33.671 -34.095 1.00105.21 O ANISOU 2266 OD1 ASP A1237 10535 19387 10054 -4111 1100 1732 O ATOM 2267 OD2 ASP A1237 -27.376 -32.130 -34.343 1.00100.86 O ANISOU 2267 OD2 ASP A1237 9450 19143 9729 -3682 970 2145 O ATOM 2268 N ILE A1238 -21.622 -30.712 -34.178 1.00 66.52 N ANISOU 2268 N ILE A1238 9329 11491 4455 2222 1344 1300 N ATOM 2269 CA ILE A1238 -20.600 -29.803 -34.685 1.00 76.35 C ANISOU 2269 CA ILE A1238 10404 12886 5719 2199 1063 1067 C ATOM 2270 C ILE A1238 -19.794 -30.470 -35.792 1.00 78.97 C ANISOU 2270 C ILE A1238 10737 13088 6181 2151 1002 1092 C ATOM 2271 O ILE A1238 -19.271 -29.792 -36.684 1.00 73.51 O ANISOU 2271 O ILE A1238 9884 12416 5630 2015 820 921 O ATOM 2272 CB ILE A1238 -19.694 -29.312 -33.539 1.00 66.67 C ANISOU 2272 CB ILE A1238 9172 11984 4176 2475 914 982 C ATOM 2273 CG1 ILE A1238 -18.835 -28.135 -34.004 1.00 65.25 C ANISOU 2273 CG1 ILE A1238 8784 11959 4050 2387 629 709 C ATOM 2274 CG2 ILE A1238 -18.814 -30.441 -33.017 1.00 68.77 C ANISOU 2274 CG2 ILE A1238 9591 12325 4214 2770 953 1167 C ATOM 2275 CD1 ILE A1238 -19.640 -26.938 -34.458 1.00 63.48 C ANISOU 2275 CD1 ILE A1238 8423 11665 4030 2132 590 528 C ATOM 2276 N PHE A1239 -19.689 -31.801 -35.766 1.00 65.32 N ANISOU 2276 N PHE A1239 9202 11211 4407 2268 1167 1310 N ATOM 2277 CA PHE A1239 -18.977 -32.504 -36.827 1.00 66.70 C ANISOU 2277 CA PHE A1239 9408 11236 4698 2239 1137 1339 C ATOM 2278 C PHE A1239 -19.743 -32.442 -38.141 1.00 65.35 C ANISOU 2278 C PHE A1239 9178 10809 4841 1896 1168 1277 C ATOM 2279 O PHE A1239 -19.131 -32.359 -39.212 1.00 64.72 O ANISOU 2279 O PHE A1239 9024 10680 4886 1808 1050 1184 O ATOM 2280 CB PHE A1239 -18.720 -33.952 -36.414 1.00 66.96 C ANISOU 2280 CB PHE A1239 9696 11148 4597 2467 1329 1592 C ATOM 2281 CG PHE A1239 -17.978 -34.086 -35.114 1.00 83.23 C ANISOU 2281 CG PHE A1239 11822 13478 6323 2835 1304 1679 C ATOM 2282 CD1 PHE A1239 -16.597 -33.985 -35.076 1.00 84.96 C ANISOU 2282 CD1 PHE A1239 11961 13927 6392 3056 1112 1624 C ATOM 2283 CD2 PHE A1239 -18.663 -34.311 -33.931 1.00 90.35 C ANISOU 2283 CD2 PHE A1239 12855 14424 7050 2965 1470 1822 C ATOM 2284 CE1 PHE A1239 -15.913 -34.107 -33.881 1.00 72.23 C ANISOU 2284 CE1 PHE A1239 10393 12597 4454 3400 1068 1701 C ATOM 2285 CE2 PHE A1239 -17.984 -34.433 -32.734 1.00 73.73 C ANISOU 2285 CE2 PHE A1239 10818 12588 4610 3320 1439 1903 C ATOM 2286 CZ PHE A1239 -16.608 -34.331 -32.710 1.00 74.20 C ANISOU 2286 CZ PHE A1239 10791 12888 4514 3537 1227 1839 C ATOM 2287 N LYS A1240 -21.077 -32.477 -38.082 1.00 69.38 N ANISOU 2287 N LYS A1240 9712 11176 5473 1707 1324 1332 N ATOM 2288 CA LYS A1240 -21.870 -32.263 -39.287 1.00 62.47 C ANISOU 2288 CA LYS A1240 8742 10113 4881 1376 1321 1254 C ATOM 2289 C LYS A1240 -21.718 -30.839 -39.804 1.00 65.69 C ANISOU 2289 C LYS A1240 8908 10670 5382 1254 1103 1026 C ATOM 2290 O LYS A1240 -21.753 -30.615 -41.020 1.00 82.48 O ANISOU 2290 O LYS A1240 10943 12693 7702 1053 1022 934 O ATOM 2291 CB LYS A1240 -23.342 -32.570 -39.011 1.00 61.59 C ANISOU 2291 CB LYS A1240 8672 9860 4870 1210 1531 1369 C ATOM 2292 CG LYS A1240 -23.599 -33.970 -38.479 1.00 65.37 C ANISOU 2292 CG LYS A1240 9401 10158 5279 1299 1778 1609 C ATOM 2293 CD LYS A1240 -25.060 -34.151 -38.098 1.00 78.61 C ANISOU 2293 CD LYS A1240 11078 11734 7054 1127 1988 1724 C ATOM 2294 CE LYS A1240 -25.311 -35.528 -37.506 1.00 90.53 C ANISOU 2294 CE LYS A1240 12847 13050 8499 1210 2256 1977 C ATOM 2295 NZ LYS A1240 -26.721 -35.682 -37.052 1.00 92.96 N ANISOU 2295 NZ LYS A1240 13134 13285 8902 1042 2476 2104 N ATOM 2296 N ILE A1241 -21.551 -29.870 -38.902 1.00 58.78 N ANISOU 2296 N ILE A1241 7940 10027 4365 1375 1013 932 N ATOM 2297 CA ILE A1241 -21.344 -28.488 -39.322 1.00 64.32 C ANISOU 2297 CA ILE A1241 8436 10850 5153 1269 817 714 C ATOM 2298 C ILE A1241 -19.969 -28.325 -39.959 1.00 71.12 C ANISOU 2298 C ILE A1241 9226 11787 6008 1320 628 612 C ATOM 2299 O ILE A1241 -19.827 -27.677 -41.003 1.00 67.15 O ANISOU 2299 O ILE A1241 8588 11245 5681 1147 514 489 O ATOM 2300 CB ILE A1241 -21.533 -27.535 -38.127 1.00 57.94 C ANISOU 2300 CB ILE A1241 7583 10249 4184 1387 783 628 C ATOM 2301 CG1 ILE A1241 -22.958 -27.644 -37.581 1.00 66.50 C ANISOU 2301 CG1 ILE A1241 8713 11261 5291 1332 990 737 C ATOM 2302 CG2 ILE A1241 -21.215 -26.103 -38.529 1.00 56.50 C ANISOU 2302 CG2 ILE A1241 7215 10165 4089 1283 585 395 C ATOM 2303 CD1 ILE A1241 -23.204 -26.815 -36.339 1.00 73.32 C ANISOU 2303 CD1 ILE A1241 9571 12320 5968 1481 992 668 C ATOM 2304 N ILE A1242 -18.938 -28.909 -39.343 1.00 74.70 N ANISOU 2304 N ILE A1242 9763 12365 6256 1569 600 675 N ATOM 2305 CA ILE A1242 -17.598 -28.869 -39.924 1.00 69.96 C ANISOU 2305 CA ILE A1242 9079 11857 5645 1637 439 605 C ATOM 2306 C ILE A1242 -17.586 -29.569 -41.276 1.00 69.16 C ANISOU 2306 C ILE A1242 9019 11525 5731 1502 493 658 C ATOM 2307 O ILE A1242 -16.965 -29.093 -42.235 1.00 75.25 O ANISOU 2307 O ILE A1242 9660 12313 6618 1409 365 549 O ATOM 2308 CB ILE A1242 -16.578 -29.492 -38.952 1.00 72.43 C ANISOU 2308 CB ILE A1242 9472 12361 5685 1960 417 696 C ATOM 2309 CG1 ILE A1242 -16.458 -28.645 -37.684 1.00 60.72 C ANISOU 2309 CG1 ILE A1242 7927 11146 3997 2084 316 596 C ATOM 2310 CG2 ILE A1242 -15.222 -29.650 -39.623 1.00 69.15 C ANISOU 2310 CG2 ILE A1242 8968 12035 5272 2045 284 664 C ATOM 2311 CD1 ILE A1242 -15.588 -29.270 -36.616 1.00 63.26 C ANISOU 2311 CD1 ILE A1242 8333 11687 4015 2419 296 699 C ATOM 2312 N MET A1243 -18.277 -30.707 -41.377 1.00 71.48 N ANISOU 2312 N MET A1243 9506 11597 6057 1483 689 823 N ATOM 2313 CA MET A1243 -18.358 -31.416 -42.650 1.00 66.10 C ANISOU 2313 CA MET A1243 8896 10677 5543 1341 746 856 C ATOM 2314 C MET A1243 -19.074 -30.579 -43.702 1.00 62.24 C ANISOU 2314 C MET A1243 8256 10111 5281 1041 676 723 C ATOM 2315 O MET A1243 -18.682 -30.574 -44.875 1.00 52.94 O ANISOU 2315 O MET A1243 7037 8859 4218 943 611 662 O ATOM 2316 CB MET A1243 -19.070 -32.756 -42.456 1.00 76.32 C ANISOU 2316 CB MET A1243 10437 11729 6833 1347 977 1045 C ATOM 2317 CG MET A1243 -19.189 -33.590 -43.721 1.00 78.36 C ANISOU 2317 CG MET A1243 10811 11716 7247 1196 1045 1066 C ATOM 2318 SD MET A1243 -17.591 -34.166 -44.323 1.00 98.77 S ANISOU 2318 SD MET A1243 13458 14323 9746 1426 981 1075 S ATOM 2319 CE MET A1243 -17.045 -35.156 -42.934 1.00106.46 C ANISOU 2319 CE MET A1243 14636 15351 10463 1798 1118 1284 C ATOM 2320 N ALA A1244 -20.123 -29.858 -43.300 1.00 59.14 N ANISOU 2320 N ALA A1244 7782 9745 4945 913 696 684 N ATOM 2321 CA ALA A1244 -20.877 -29.056 -44.257 1.00 51.95 C ANISOU 2321 CA ALA A1244 6725 8773 4240 653 638 578 C ATOM 2322 C ALA A1244 -20.084 -27.835 -44.705 1.00 51.01 C ANISOU 2322 C ALA A1244 6419 8805 4159 639 443 412 C ATOM 2323 O ALA A1244 -20.177 -27.423 -45.866 1.00 67.09 O ANISOU 2323 O ALA A1244 8365 10775 6353 472 377 341 O ATOM 2324 CB ALA A1244 -22.216 -28.636 -43.652 1.00 62.04 C ANISOU 2324 CB ALA A1244 7960 10051 5561 553 730 602 C ATOM 2325 N ILE A1245 -19.300 -27.244 -43.801 1.00 55.09 N ANISOU 2325 N ILE A1245 6878 9526 4530 808 349 348 N ATOM 2326 CA ILE A1245 -18.515 -26.065 -44.155 1.00 56.39 C ANISOU 2326 CA ILE A1245 6864 9824 4739 774 169 185 C ATOM 2327 C ILE A1245 -17.454 -26.417 -45.191 1.00 58.12 C ANISOU 2327 C ILE A1245 7054 10025 5005 782 101 180 C ATOM 2328 O ILE A1245 -17.245 -25.678 -46.161 1.00 60.75 O ANISOU 2328 O ILE A1245 7258 10343 5479 644 14 88 O ATOM 2329 CB ILE A1245 -17.891 -25.444 -42.892 1.00 61.22 C ANISOU 2329 CB ILE A1245 7428 10664 5167 942 78 104 C ATOM 2330 CG1 ILE A1245 -18.969 -24.772 -42.039 1.00 61.87 C ANISOU 2330 CG1 ILE A1245 7516 10766 5227 911 133 67 C ATOM 2331 CG2 ILE A1245 -16.799 -24.452 -43.261 1.00 50.93 C ANISOU 2331 CG2 ILE A1245 5950 9498 3902 912 -110 -55 C ATOM 2332 CD1 ILE A1245 -18.445 -24.181 -40.751 1.00 56.96 C ANISOU 2332 CD1 ILE A1245 6879 10364 4399 1076 47 -29 C ATOM 2333 N VAL A1246 -16.775 -27.550 -45.009 1.00 63.80 N ANISOU 2333 N VAL A1246 7897 10740 5602 960 156 292 N ATOM 2334 CA VAL A1246 -15.705 -27.932 -45.926 1.00 63.38 C ANISOU 2334 CA VAL A1246 7822 10687 5572 1010 109 298 C ATOM 2335 C VAL A1246 -16.274 -28.306 -47.289 1.00 71.45 C ANISOU 2335 C VAL A1246 8902 11483 6763 825 174 315 C ATOM 2336 O VAL A1246 -15.793 -27.844 -48.330 1.00 82.99 O ANISOU 2336 O VAL A1246 10257 12950 8325 740 96 246 O ATOM 2337 CB VAL A1246 -14.872 -29.079 -45.328 1.00 66.18 C ANISOU 2337 CB VAL A1246 8311 11094 5741 1284 168 429 C ATOM 2338 CG1 VAL A1246 -13.841 -29.564 -46.333 1.00 57.53 C ANISOU 2338 CG1 VAL A1246 7206 9981 4673 1354 150 451 C ATOM 2339 CG2 VAL A1246 -14.200 -28.630 -44.039 1.00 53.77 C ANISOU 2339 CG2 VAL A1246 6653 9796 3981 1474 68 396 C ATOM 2340 N LEU A1247 -17.312 -29.146 -47.304 1.00 76.15 N ANISOU 2340 N LEU A1247 9666 11883 7386 752 317 407 N ATOM 2341 CA LEU A1247 -17.856 -29.622 -48.572 1.00 68.73 C ANISOU 2341 CA LEU A1247 8798 10734 6584 572 369 413 C ATOM 2342 C LEU A1247 -18.587 -28.520 -49.330 1.00 69.65 C ANISOU 2342 C LEU A1247 8749 10852 6862 339 287 307 C ATOM 2343 O LEU A1247 -18.619 -28.541 -50.565 1.00 82.32 O ANISOU 2343 O LEU A1247 10344 12369 8563 216 261 271 O ATOM 2344 CB LEU A1247 -18.785 -30.812 -48.331 1.00 60.33 C ANISOU 2344 CB LEU A1247 7949 9460 5515 529 540 530 C ATOM 2345 CG LEU A1247 -18.109 -32.082 -47.809 1.00 58.70 C ANISOU 2345 CG LEU A1247 7958 9184 5162 761 656 660 C ATOM 2346 CD1 LEU A1247 -19.114 -33.213 -47.669 1.00 53.48 C ANISOU 2346 CD1 LEU A1247 7518 8272 4530 670 842 772 C ATOM 2347 CD2 LEU A1247 -16.962 -32.491 -48.721 1.00 52.17 C ANISOU 2347 CD2 LEU A1247 7171 8337 4315 870 622 645 C ATOM 2348 N PHE A1248 -19.177 -27.556 -48.618 1.00 63.66 N ANISOU 2348 N PHE A1248 7870 10194 6122 293 251 259 N ATOM 2349 CA PHE A1248 -19.843 -26.450 -49.300 1.00 59.60 C ANISOU 2349 CA PHE A1248 7202 9685 5758 106 181 172 C ATOM 2350 C PHE A1248 -18.843 -25.565 -50.032 1.00 68.12 C ANISOU 2350 C PHE A1248 8142 10856 6884 106 51 77 C ATOM 2351 O PHE A1248 -19.161 -25.021 -51.094 1.00 83.29 O ANISOU 2351 O PHE A1248 9986 12731 8930 -39 10 37 O ATOM 2352 CB PHE A1248 -20.652 -25.622 -48.302 1.00 53.50 C ANISOU 2352 CB PHE A1248 6352 8993 4984 93 191 146 C ATOM 2353 CG PHE A1248 -21.621 -24.674 -48.943 1.00 65.90 C ANISOU 2353 CG PHE A1248 7793 10539 6709 -84 162 95 C ATOM 2354 CD1 PHE A1248 -22.850 -25.123 -49.396 1.00 72.96 C ANISOU 2354 CD1 PHE A1248 8706 11324 7692 -235 240 159 C ATOM 2355 CD2 PHE A1248 -21.309 -23.332 -49.085 1.00 75.21 C ANISOU 2355 CD2 PHE A1248 8828 11804 7945 -100 59 -12 C ATOM 2356 CE1 PHE A1248 -23.747 -24.254 -49.984 1.00 70.37 C ANISOU 2356 CE1 PHE A1248 8242 11002 7495 -372 209 127 C ATOM 2357 CE2 PHE A1248 -22.204 -22.458 -49.672 1.00 67.30 C ANISOU 2357 CE2 PHE A1248 7718 10774 7079 -232 45 -39 C ATOM 2358 CZ PHE A1248 -23.425 -22.920 -50.121 1.00 63.87 C ANISOU 2358 CZ PHE A1248 7290 10258 6718 -355 116 35 C ATOM 2359 N PHE A1249 -17.637 -25.409 -49.482 1.00 66.46 N ANISOU 2359 N PHE A1249 7891 10787 6574 265 -12 49 N ATOM 2360 CA PHE A1249 -16.601 -24.650 -50.172 1.00 57.93 C ANISOU 2360 CA PHE A1249 6668 9796 5547 256 -121 -28 C ATOM 2361 C PHE A1249 -16.030 -25.428 -51.350 1.00 59.20 C ANISOU 2361 C PHE A1249 6890 9879 5725 268 -92 22 C ATOM 2362 O PHE A1249 -15.685 -24.833 -52.377 1.00 65.24 O ANISOU 2362 O PHE A1249 7557 10647 6584 184 -143 -21 O ATOM 2363 CB PHE A1249 -15.488 -24.276 -49.191 1.00 50.04 C ANISOU 2363 CB PHE A1249 5582 8997 4434 409 -206 -79 C ATOM 2364 CG PHE A1249 -14.359 -23.502 -49.814 1.00 50.55 C ANISOU 2364 CG PHE A1249 5475 9169 4562 385 -312 -153 C ATOM 2365 CD1 PHE A1249 -14.405 -22.120 -49.881 1.00 46.08 C ANISOU 2365 CD1 PHE A1249 4761 8641 4105 254 -394 -268 C ATOM 2366 CD2 PHE A1249 -13.247 -24.155 -50.324 1.00 50.94 C ANISOU 2366 CD2 PHE A1249 5514 9274 4566 499 -314 -101 C ATOM 2367 CE1 PHE A1249 -13.369 -21.404 -50.450 1.00 68.39 C ANISOU 2367 CE1 PHE A1249 7427 11552 7005 211 -476 -327 C ATOM 2368 CE2 PHE A1249 -12.210 -23.445 -50.896 1.00 51.80 C ANISOU 2368 CE2 PHE A1249 5445 9494 4742 470 -396 -156 C ATOM 2369 CZ PHE A1249 -12.271 -22.068 -50.958 1.00 54.68 C ANISOU 2369 CZ PHE A1249 5658 9890 5226 313 -477 -268 C ATOM 2370 N PHE A1250 -15.924 -26.751 -51.220 1.00 58.34 N ANISOU 2370 N PHE A1250 6959 9689 5520 382 1 115 N ATOM 2371 CA PHE A1250 -15.305 -27.566 -52.259 1.00 55.13 C ANISOU 2371 CA PHE A1250 6642 9199 5104 430 42 156 C ATOM 2372 C PHE A1250 -16.235 -27.744 -53.455 1.00 69.78 C ANISOU 2372 C PHE A1250 8569 10878 7065 236 77 144 C ATOM 2373 O PHE A1250 -15.872 -27.423 -54.591 1.00 73.64 O ANISOU 2373 O PHE A1250 9004 11366 7611 181 40 109 O ATOM 2374 CB PHE A1250 -14.901 -28.925 -51.680 1.00 57.74 C ANISOU 2374 CB PHE A1250 7167 9478 5294 633 145 261 C ATOM 2375 CG PHE A1250 -14.156 -29.803 -52.646 1.00 69.51 C ANISOU 2375 CG PHE A1250 8772 10883 6755 729 203 303 C ATOM 2376 CD1 PHE A1250 -12.793 -29.644 -52.837 1.00 81.29 C ANISOU 2376 CD1 PHE A1250 10151 12539 8196 896 155 306 C ATOM 2377 CD2 PHE A1250 -14.816 -30.794 -53.354 1.00 74.33 C ANISOU 2377 CD2 PHE A1250 9602 11253 7385 652 309 334 C ATOM 2378 CE1 PHE A1250 -12.104 -30.453 -53.722 1.00 82.26 C ANISOU 2378 CE1 PHE A1250 10384 12589 8283 1012 226 351 C ATOM 2379 CE2 PHE A1250 -14.132 -31.606 -54.240 1.00 73.21 C ANISOU 2379 CE2 PHE A1250 9594 11020 7202 754 372 359 C ATOM 2380 CZ PHE A1250 -12.774 -31.435 -54.424 1.00 74.06 C ANISOU 2380 CZ PHE A1250 9593 11293 7253 949 338 373 C ATOM 2381 N PHE A1251 -17.447 -28.252 -53.214 1.00 69.11 N ANISOU 2381 N PHE A1251 8598 10658 7002 127 148 175 N ATOM 2382 CA PHE A1251 -18.355 -28.558 -54.313 1.00 60.63 C ANISOU 2382 CA PHE A1251 7593 9430 6012 -64 170 159 C ATOM 2383 C PHE A1251 -18.906 -27.310 -54.989 1.00 63.49 C ANISOU 2383 C PHE A1251 7771 9859 6493 -227 75 91 C ATOM 2384 O PHE A1251 -19.459 -27.413 -56.089 1.00 66.84 O ANISOU 2384 O PHE A1251 8220 10205 6972 -367 61 69 O ATOM 2385 CB PHE A1251 -19.508 -29.431 -53.819 1.00 60.34 C ANISOU 2385 CB PHE A1251 7702 9246 5980 -157 272 214 C ATOM 2386 CG PHE A1251 -19.132 -30.868 -53.610 1.00 60.87 C ANISOU 2386 CG PHE A1251 8014 9160 5953 -40 393 288 C ATOM 2387 CD1 PHE A1251 -18.975 -31.718 -54.692 1.00 48.22 C ANISOU 2387 CD1 PHE A1251 6577 7397 4347 -79 432 272 C ATOM 2388 CD2 PHE A1251 -18.938 -31.371 -52.336 1.00 66.42 C ANISOU 2388 CD2 PHE A1251 8800 9875 6561 122 476 377 C ATOM 2389 CE1 PHE A1251 -18.629 -33.042 -54.507 1.00 60.23 C ANISOU 2389 CE1 PHE A1251 8352 8747 5786 40 560 339 C ATOM 2390 CE2 PHE A1251 -18.592 -32.695 -52.143 1.00 66.70 C ANISOU 2390 CE2 PHE A1251 9079 9753 6511 250 605 463 C ATOM 2391 CZ PHE A1251 -18.438 -33.532 -53.231 1.00 68.69 C ANISOU 2391 CZ PHE A1251 9504 9820 6775 208 652 444 C ATOM 2392 N SER A1252 -18.778 -26.139 -54.364 1.00 64.29 N ANISOU 2392 N SER A1252 7701 10100 6627 -207 9 55 N ATOM 2393 CA SER A1252 -19.238 -24.916 -55.010 1.00 63.54 C ANISOU 2393 CA SER A1252 7447 10050 6646 -335 -65 4 C ATOM 2394 C SER A1252 -18.205 -24.363 -55.981 1.00 46.36 C ANISOU 2394 C SER A1252 5191 7929 4495 -309 -123 -26 C ATOM 2395 O SER A1252 -18.575 -23.762 -56.995 1.00 60.85 O ANISOU 2395 O SER A1252 6963 9752 6408 -415 -159 -41 O ATOM 2396 CB SER A1252 -19.589 -23.860 -53.961 1.00 79.42 C ANISOU 2396 CB SER A1252 9333 12153 8690 -329 -93 -29 C ATOM 2397 OG SER A1252 -18.468 -23.542 -53.156 1.00103.23 O ANISOU 2397 OG SER A1252 12302 15281 11638 -189 -130 -63 O ATOM 2398 N TRP A1253 -16.916 -24.561 -55.701 1.00 46.31 N ANISOU 2398 N TRP A1253 5179 7999 4419 -160 -128 -24 N ATOM 2399 CA TRP A1253 -15.858 -24.027 -56.547 1.00 55.62 C ANISOU 2399 CA TRP A1253 6258 9250 5627 -131 -168 -40 C ATOM 2400 C TRP A1253 -15.232 -25.061 -57.473 1.00 57.16 C ANISOU 2400 C TRP A1253 6578 9389 5750 -52 -113 1 C ATOM 2401 O TRP A1253 -14.636 -24.675 -58.484 1.00 68.88 O ANISOU 2401 O TRP A1253 7999 10907 7263 -57 -124 0 O ATOM 2402 CB TRP A1253 -14.753 -23.399 -55.688 1.00 62.25 C ANISOU 2402 CB TRP A1253 6957 10247 6450 -30 -221 -73 C ATOM 2403 CG TRP A1253 -15.162 -22.132 -54.999 1.00 70.06 C ANISOU 2403 CG TRP A1253 7816 11287 7517 -115 -283 -142 C ATOM 2404 CD1 TRP A1253 -15.413 -21.966 -53.668 1.00 74.60 C ANISOU 2404 CD1 TRP A1253 8387 11915 8044 -74 -301 -178 C ATOM 2405 CD2 TRP A1253 -15.368 -20.852 -55.609 1.00 75.10 C ANISOU 2405 CD2 TRP A1253 8331 11916 8289 -242 -321 -183 C ATOM 2406 NE1 TRP A1253 -15.761 -20.662 -53.411 1.00 75.01 N ANISOU 2406 NE1 TRP A1253 8327 11984 8190 -169 -350 -254 N ATOM 2407 CE2 TRP A1253 -15.741 -19.957 -54.586 1.00 71.48 C ANISOU 2407 CE2 TRP A1253 7807 11488 7862 -273 -360 -253 C ATOM 2408 CE3 TRP A1253 -15.272 -20.376 -56.920 1.00 76.83 C ANISOU 2408 CE3 TRP A1253 8503 12097 8592 -319 -317 -160 C ATOM 2409 CZ2 TRP A1253 -16.019 -18.615 -54.833 1.00 66.67 C ANISOU 2409 CZ2 TRP A1253 7098 10853 7382 -379 -388 -303 C ATOM 2410 CZ3 TRP A1253 -15.549 -19.043 -57.163 1.00 78.22 C ANISOU 2410 CZ3 TRP A1253 8569 12258 8893 -421 -345 -192 C ATOM 2411 CH2 TRP A1253 -15.918 -18.178 -56.126 1.00 76.64 C ANISOU 2411 CH2 TRP A1253 8316 12068 8736 -451 -377 -264 C ATOM 2412 N ILE A1254 -15.356 -26.351 -57.171 1.00 58.33 N ANISOU 2412 N ILE A1254 6915 9442 5805 26 -39 41 N ATOM 2413 CA ILE A1254 -14.701 -27.385 -57.972 1.00 57.07 C ANISOU 2413 CA ILE A1254 6907 9211 5566 131 30 73 C ATOM 2414 C ILE A1254 -15.295 -27.507 -59.377 1.00 66.94 C ANISOU 2414 C ILE A1254 8238 10353 6844 -3 35 46 C ATOM 2415 O ILE A1254 -14.578 -27.962 -60.280 1.00 83.28 O ANISOU 2415 O ILE A1254 10384 12403 8855 83 76 54 O ATOM 2416 CB ILE A1254 -14.704 -28.743 -57.243 1.00 57.16 C ANISOU 2416 CB ILE A1254 7129 9116 5473 258 124 128 C ATOM 2417 CG1 ILE A1254 -13.563 -29.625 -57.756 1.00 59.44 C ANISOU 2417 CG1 ILE A1254 7533 9388 5664 459 197 170 C ATOM 2418 CG2 ILE A1254 -16.019 -29.484 -57.414 1.00 50.24 C ANISOU 2418 CG2 ILE A1254 6434 8039 4614 102 176 122 C ATOM 2419 CD1 ILE A1254 -12.196 -28.991 -57.639 1.00 58.61 C ANISOU 2419 CD1 ILE A1254 7223 9502 5543 613 153 187 C ATOM 2420 N PRO A1255 -16.555 -27.128 -59.650 1.00 64.83 N ANISOU 2420 N PRO A1255 7954 10031 6649 -197 -6 14 N ATOM 2421 CA PRO A1255 -16.962 -27.093 -61.066 1.00 66.87 C ANISOU 2421 CA PRO A1255 8255 10239 6913 -306 -27 -16 C ATOM 2422 C PRO A1255 -16.318 -25.953 -61.831 1.00 64.21 C ANISOU 2422 C PRO A1255 7749 10028 6620 -291 -73 -12 C ATOM 2423 O PRO A1255 -15.894 -26.143 -62.978 1.00 61.96 O ANISOU 2423 O PRO A1255 7524 9734 6283 -261 -54 -13 O ATOM 2424 CB PRO A1255 -18.490 -26.944 -60.996 1.00 63.57 C ANISOU 2424 CB PRO A1255 7824 9769 6562 -504 -68 -38 C ATOM 2425 CG PRO A1255 -18.859 -27.371 -59.628 1.00 55.85 C ANISOU 2425 CG PRO A1255 6879 8754 5588 -487 -24 -13 C ATOM 2426 CD PRO A1255 -17.726 -26.914 -58.778 1.00 64.23 C ANISOU 2426 CD PRO A1255 7844 9930 6630 -314 -22 10 C ATOM 2427 N HIS A1256 -16.225 -24.769 -61.222 1.00 69.14 N ANISOU 2427 N HIS A1256 8175 10758 7336 -310 -123 -9 N ATOM 2428 CA HIS A1256 -15.649 -23.621 -61.914 1.00 70.63 C ANISOU 2428 CA HIS A1256 8206 11041 7590 -317 -152 2 C ATOM 2429 C HIS A1256 -14.149 -23.791 -62.121 1.00 68.76 C ANISOU 2429 C HIS A1256 7936 10883 7307 -166 -108 30 C ATOM 2430 O HIS A1256 -13.613 -23.392 -63.161 1.00 63.04 O ANISOU 2430 O HIS A1256 7165 10200 6588 -152 -88 58 O ATOM 2431 CB HIS A1256 -15.943 -22.340 -61.134 1.00 68.23 C ANISOU 2431 CB HIS A1256 7725 10797 7402 -384 -205 -14 C ATOM 2432 CG HIS A1256 -15.441 -21.097 -61.801 1.00 56.84 C ANISOU 2432 CG HIS A1256 6132 9416 6048 -413 -221 3 C ATOM 2433 ND1 HIS A1256 -16.035 -20.563 -62.923 1.00 62.37 N ANISOU 2433 ND1 HIS A1256 6825 10093 6781 -490 -229 33 N ATOM 2434 CD2 HIS A1256 -14.401 -20.283 -61.503 1.00 62.36 C ANISOU 2434 CD2 HIS A1256 6684 10198 6811 -382 -225 0 C ATOM 2435 CE1 HIS A1256 -15.383 -19.473 -63.288 1.00 68.28 C ANISOU 2435 CE1 HIS A1256 7442 10889 7614 -495 -220 61 C ATOM 2436 NE2 HIS A1256 -14.387 -19.281 -62.442 1.00 61.12 N ANISOU 2436 NE2 HIS A1256 6444 10041 6736 -446 -219 35 N ATOM 2437 N GLN A1257 -13.456 -24.383 -61.145 1.00 68.15 N ANISOU 2437 N GLN A1257 7873 10843 7177 -38 -85 36 N ATOM 2438 CA GLN A1257 -12.005 -24.505 -61.243 1.00 61.56 C ANISOU 2438 CA GLN A1257 6965 10122 6303 120 -49 72 C ATOM 2439 C GLN A1257 -11.589 -25.583 -62.235 1.00 60.33 C ANISOU 2439 C GLN A1257 6984 9903 6037 236 40 105 C ATOM 2440 O GLN A1257 -10.514 -25.483 -62.838 1.00 65.42 O ANISOU 2440 O GLN A1257 7553 10643 6662 343 85 146 O ATOM 2441 CB GLN A1257 -11.407 -24.793 -59.866 1.00 60.41 C ANISOU 2441 CB GLN A1257 6769 10066 6118 242 -65 74 C ATOM 2442 CG GLN A1257 -11.643 -23.694 -58.841 1.00 70.41 C ANISOU 2442 CG GLN A1257 7868 11412 7473 147 -154 22 C ATOM 2443 CD GLN A1257 -10.953 -22.393 -59.201 1.00 83.65 C ANISOU 2443 CD GLN A1257 9321 13198 9264 73 -197 4 C ATOM 2444 OE1 GLN A1257 -9.983 -22.380 -59.959 1.00 89.94 O ANISOU 2444 OE1 GLN A1257 10044 14067 10061 134 -159 47 O ATOM 2445 NE2 GLN A1257 -11.452 -21.289 -58.657 1.00 97.75 N ANISOU 2445 NE2 GLN A1257 11004 14986 11150 -58 -262 -56 N ATOM 2446 N ILE A1258 -12.413 -26.616 -62.417 1.00 63.08 N ANISOU 2446 N ILE A1258 7565 10090 6312 214 74 86 N ATOM 2447 CA ILE A1258 -12.082 -27.666 -63.377 1.00 66.32 C ANISOU 2447 CA ILE A1258 8182 10410 6608 318 163 94 C ATOM 2448 C ILE A1258 -12.166 -27.130 -64.801 1.00 64.93 C ANISOU 2448 C ILE A1258 7989 10250 6433 246 158 85 C ATOM 2449 O ILE A1258 -11.244 -27.311 -65.604 1.00 69.95 O ANISOU 2449 O ILE A1258 8641 10934 7001 379 230 119 O ATOM 2450 CB ILE A1258 -12.994 -28.889 -63.175 1.00 60.72 C ANISOU 2450 CB ILE A1258 7740 9497 5833 278 199 59 C ATOM 2451 CG1 ILE A1258 -12.541 -29.694 -61.955 1.00 52.86 C ANISOU 2451 CG1 ILE A1258 6815 8480 4789 440 256 104 C ATOM 2452 CG2 ILE A1258 -13.008 -29.762 -64.422 1.00 51.58 C ANISOU 2452 CG2 ILE A1258 6818 8211 4570 306 266 26 C ATOM 2453 CD1 ILE A1258 -13.434 -30.873 -61.634 1.00 56.39 C ANISOU 2453 CD1 ILE A1258 7527 8706 5191 390 313 86 C ATOM 2454 N PHE A1259 -13.272 -26.460 -65.135 1.00 61.74 N ANISOU 2454 N PHE A1259 7546 9818 6093 53 80 51 N ATOM 2455 CA PHE A1259 -13.407 -25.901 -66.476 1.00 60.73 C ANISOU 2455 CA PHE A1259 7402 9723 5951 -3 70 56 C ATOM 2456 C PHE A1259 -12.481 -24.709 -66.681 1.00 59.54 C ANISOU 2456 C PHE A1259 7018 9722 5881 38 81 123 C ATOM 2457 O PHE A1259 -12.114 -24.404 -67.821 1.00 61.16 O ANISOU 2457 O PHE A1259 7219 9973 6046 69 122 160 O ATOM 2458 CB PHE A1259 -14.862 -25.513 -66.742 1.00 64.04 C ANISOU 2458 CB PHE A1259 7828 10093 6410 -202 -21 15 C ATOM 2459 CG PHE A1259 -15.768 -26.690 -66.975 1.00 68.44 C ANISOU 2459 CG PHE A1259 8618 10507 6879 -277 -29 -57 C ATOM 2460 CD1 PHE A1259 -15.871 -27.262 -68.231 1.00 68.09 C ANISOU 2460 CD1 PHE A1259 8746 10416 6708 -278 -16 -99 C ATOM 2461 CD2 PHE A1259 -16.509 -27.227 -65.937 1.00 63.04 C ANISOU 2461 CD2 PHE A1259 7984 9734 6236 -356 -44 -85 C ATOM 2462 CE1 PHE A1259 -16.700 -28.346 -68.450 1.00 65.53 C ANISOU 2462 CE1 PHE A1259 8642 9947 6308 -377 -31 -186 C ATOM 2463 CE2 PHE A1259 -17.341 -28.312 -66.148 1.00 65.91 C ANISOU 2463 CE2 PHE A1259 8556 9949 6537 -455 -43 -151 C ATOM 2464 CZ PHE A1259 -17.436 -28.872 -67.407 1.00 70.64 C ANISOU 2464 CZ PHE A1259 9327 10493 7020 -476 -42 -211 C ATOM 2465 N THR A1260 -12.097 -24.027 -65.601 1.00 61.60 N ANISOU 2465 N THR A1260 7092 10061 6251 31 50 136 N ATOM 2466 CA THR A1260 -11.051 -23.016 -65.709 1.00 62.45 C ANISOU 2466 CA THR A1260 6980 10304 6445 62 70 190 C ATOM 2467 C THR A1260 -9.716 -23.659 -66.061 1.00 56.96 C ANISOU 2467 C THR A1260 6287 9689 5665 252 167 241 C ATOM 2468 O THR A1260 -8.958 -23.127 -66.880 1.00 59.63 O ANISOU 2468 O THR A1260 6519 10114 6022 288 227 304 O ATOM 2469 CB THR A1260 -10.943 -22.226 -64.404 1.00 68.65 C ANISOU 2469 CB THR A1260 7583 11149 7353 1 2 164 C ATOM 2470 OG1 THR A1260 -12.162 -21.507 -64.178 1.00 77.12 O ANISOU 2470 OG1 THR A1260 8645 12151 8507 -157 -67 128 O ATOM 2471 CG2 THR A1260 -9.784 -21.243 -64.464 1.00 58.03 C ANISOU 2471 CG2 THR A1260 6006 9938 6106 7 21 205 C ATOM 2472 N PHE A1261 -9.419 -24.814 -65.459 1.00 46.68 N ANISOU 2472 N PHE A1261 5107 8360 4269 390 198 228 N ATOM 2473 CA PHE A1261 -8.210 -25.547 -65.816 1.00 51.65 C ANISOU 2473 CA PHE A1261 5762 9062 4802 609 304 285 C ATOM 2474 C PHE A1261 -8.294 -26.085 -67.239 1.00 60.92 C ANISOU 2474 C PHE A1261 7130 10158 5858 665 392 293 C ATOM 2475 O PHE A1261 -7.285 -26.133 -67.951 1.00 63.31 O ANISOU 2475 O PHE A1261 7385 10557 6112 809 491 359 O ATOM 2476 CB PHE A1261 -7.976 -26.681 -64.819 1.00 53.58 C ANISOU 2476 CB PHE A1261 6121 9272 4964 763 325 280 C ATOM 2477 CG PHE A1261 -6.777 -27.527 -65.133 1.00 62.96 C ANISOU 2477 CG PHE A1261 7351 10528 6042 1025 445 347 C ATOM 2478 CD1 PHE A1261 -5.501 -27.079 -64.838 1.00 64.04 C ANISOU 2478 CD1 PHE A1261 7224 10887 6219 1142 462 417 C ATOM 2479 CD2 PHE A1261 -6.927 -28.775 -65.716 1.00 50.81 C ANISOU 2479 CD2 PHE A1261 6114 8831 4361 1154 545 337 C ATOM 2480 CE1 PHE A1261 -4.396 -27.856 -65.124 1.00 65.78 C ANISOU 2480 CE1 PHE A1261 7463 11194 6338 1406 581 494 C ATOM 2481 CE2 PHE A1261 -5.826 -29.556 -66.004 1.00 62.31 C ANISOU 2481 CE2 PHE A1261 7622 10341 5710 1424 673 405 C ATOM 2482 CZ PHE A1261 -4.558 -29.096 -65.708 1.00 63.70 C ANISOU 2482 CZ PHE A1261 7515 10761 5926 1562 693 492 C ATOM 2483 N LEU A1262 -9.490 -26.497 -67.670 1.00 69.77 N ANISOU 2483 N LEU A1262 8465 11120 6924 552 355 224 N ATOM 2484 CA LEU A1262 -9.669 -26.916 -69.056 1.00 72.58 C ANISOU 2484 CA LEU A1262 9011 11413 7153 580 413 208 C ATOM 2485 C LEU A1262 -9.462 -25.754 -70.017 1.00 74.55 C ANISOU 2485 C LEU A1262 9101 11779 7446 528 419 270 C ATOM 2486 O LEU A1262 -9.003 -25.956 -71.147 1.00 82.64 O ANISOU 2486 O LEU A1262 10211 12832 8356 634 509 301 O ATOM 2487 CB LEU A1262 -11.059 -27.528 -69.247 1.00 65.80 C ANISOU 2487 CB LEU A1262 8383 10381 6238 432 344 108 C ATOM 2488 CG LEU A1262 -11.176 -29.053 -69.156 1.00 68.70 C ANISOU 2488 CG LEU A1262 9052 10573 6479 521 407 43 C ATOM 2489 CD1 LEU A1262 -10.513 -29.587 -67.897 1.00 82.36 C ANISOU 2489 CD1 LEU A1262 10755 12300 8237 663 455 85 C ATOM 2490 CD2 LEU A1262 -12.636 -29.478 -69.212 1.00 74.83 C ANISOU 2490 CD2 LEU A1262 9996 11193 7245 310 319 -59 C ATOM 2491 N ASP A1263 -9.791 -24.533 -69.587 1.00 64.54 N ANISOU 2491 N ASP A1263 7617 10570 6335 376 339 292 N ATOM 2492 CA ASP A1263 -9.511 -23.360 -70.405 1.00 70.14 C ANISOU 2492 CA ASP A1263 8169 11375 7107 332 365 373 C ATOM 2493 C ASP A1263 -8.014 -23.144 -70.580 1.00 77.99 C ANISOU 2493 C ASP A1263 9001 12510 8122 475 483 467 C ATOM 2494 O ASP A1263 -7.579 -22.639 -71.622 1.00 93.78 O ANISOU 2494 O ASP A1263 10954 14577 10100 510 567 550 O ATOM 2495 CB ASP A1263 -10.157 -22.121 -69.784 1.00 70.07 C ANISOU 2495 CB ASP A1263 7981 11368 7273 149 268 373 C ATOM 2496 CG ASP A1263 -9.789 -20.844 -70.512 1.00 78.06 C ANISOU 2496 CG ASP A1263 8829 12455 8376 105 315 472 C ATOM 2497 OD1 ASP A1263 -10.361 -20.587 -71.591 1.00 85.07 O ANISOU 2497 OD1 ASP A1263 9803 13325 9195 82 323 506 O ATOM 2498 OD2 ASP A1263 -8.923 -20.100 -70.007 1.00 90.17 O ANISOU 2498 OD2 ASP A1263 10150 14067 10046 89 343 516 O ATOM 2499 N VAL A1264 -7.214 -23.521 -69.581 1.00 57.90 N ANISOU 2499 N VAL A1264 6359 10028 5614 566 493 467 N ATOM 2500 CA VAL A1264 -5.767 -23.365 -69.688 1.00 61.65 C ANISOU 2500 CA VAL A1264 6643 10669 6112 705 597 560 C ATOM 2501 C VAL A1264 -5.198 -24.345 -70.706 1.00 69.28 C ANISOU 2501 C VAL A1264 7784 11643 6896 923 739 601 C ATOM 2502 O VAL A1264 -4.281 -24.009 -71.465 1.00 73.40 O ANISOU 2502 O VAL A1264 8188 12290 7412 1015 858 702 O ATOM 2503 CB VAL A1264 -5.108 -23.538 -68.307 1.00 60.01 C ANISOU 2503 CB VAL A1264 6276 10555 5972 756 549 544 C ATOM 2504 CG1 VAL A1264 -3.613 -23.269 -68.392 1.00 64.55 C ANISOU 2504 CG1 VAL A1264 6597 11340 6591 875 640 643 C ATOM 2505 CG2 VAL A1264 -5.762 -22.620 -67.290 1.00 57.14 C ANISOU 2505 CG2 VAL A1264 5783 10166 5761 547 409 480 C ATOM 2506 N LEU A1265 -5.729 -25.571 -70.740 1.00 69.68 N ANISOU 2506 N LEU A1265 8126 11553 6797 1009 742 524 N ATOM 2507 CA LEU A1265 -5.247 -26.558 -71.702 1.00 78.85 C ANISOU 2507 CA LEU A1265 9501 12690 7770 1224 882 541 C ATOM 2508 C LEU A1265 -5.526 -26.115 -73.133 1.00 78.03 C ANISOU 2508 C LEU A1265 9475 12587 7584 1189 931 564 C ATOM 2509 O LEU A1265 -4.700 -26.326 -74.028 1.00 79.51 O ANISOU 2509 O LEU A1265 9689 12855 7664 1368 1078 636 O ATOM 2510 CB LEU A1265 -5.887 -27.918 -71.424 1.00 68.22 C ANISOU 2510 CB LEU A1265 8480 11146 6294 1284 869 435 C ATOM 2511 CG LEU A1265 -5.573 -28.558 -70.070 1.00 69.39 C ANISOU 2511 CG LEU A1265 8604 11281 6479 1375 851 432 C ATOM 2512 CD1 LEU A1265 -6.263 -29.907 -69.936 1.00 54.27 C ANISOU 2512 CD1 LEU A1265 7049 9133 4439 1421 867 339 C ATOM 2513 CD2 LEU A1265 -4.071 -28.699 -69.880 1.00 55.32 C ANISOU 2513 CD2 LEU A1265 6643 9687 4687 1626 967 544 C ATOM 2514 N ILE A1266 -6.688 -25.500 -73.368 1.00 75.28 N ANISOU 2514 N ILE A1266 9162 12166 7274 976 814 514 N ATOM 2515 CA ILE A1266 -6.988 -24.972 -74.694 1.00 71.61 C ANISOU 2515 CA ILE A1266 8753 11728 6726 947 847 552 C ATOM 2516 C ILE A1266 -6.067 -23.805 -75.024 1.00 72.19 C ANISOU 2516 C ILE A1266 8547 11967 6915 960 939 705 C ATOM 2517 O ILE A1266 -5.669 -23.624 -76.181 1.00 82.06 O ANISOU 2517 O ILE A1266 9832 13287 8059 1058 1057 787 O ATOM 2518 CB ILE A1266 -8.471 -24.564 -74.781 1.00 71.56 C ANISOU 2518 CB ILE A1266 8822 11629 6740 728 689 476 C ATOM 2519 CG1 ILE A1266 -9.373 -25.734 -74.383 1.00 69.05 C ANISOU 2519 CG1 ILE A1266 8756 11147 6333 683 603 327 C ATOM 2520 CG2 ILE A1266 -8.815 -24.087 -76.182 1.00 53.09 C ANISOU 2520 CG2 ILE A1266 6558 9335 4280 725 713 520 C ATOM 2521 CD1 ILE A1266 -10.849 -25.402 -74.402 1.00 53.36 C ANISOU 2521 CD1 ILE A1266 6811 9093 4372 465 445 253 C ATOM 2522 N GLN A1267 -5.703 -23.006 -74.019 1.00 70.30 N ANISOU 2522 N GLN A1267 8032 11790 6889 859 895 744 N ATOM 2523 CA GLN A1267 -4.837 -21.857 -74.259 1.00 63.27 C ANISOU 2523 CA GLN A1267 6865 11037 6139 829 982 880 C ATOM 2524 C GLN A1267 -3.398 -22.289 -74.517 1.00 62.26 C ANISOU 2524 C GLN A1267 6633 11059 5965 1041 1149 975 C ATOM 2525 O GLN A1267 -2.724 -21.730 -75.389 1.00 73.75 O ANISOU 2525 O GLN A1267 7979 12619 7423 1090 1288 1104 O ATOM 2526 CB GLN A1267 -4.908 -20.898 -73.072 1.00 66.79 C ANISOU 2526 CB GLN A1267 7066 11490 6823 638 873 863 C ATOM 2527 CG GLN A1267 -4.063 -19.649 -73.227 1.00 83.28 C ANISOU 2527 CG GLN A1267 8866 13688 9089 557 953 987 C ATOM 2528 CD GLN A1267 -4.132 -18.755 -72.009 1.00 87.73 C ANISOU 2528 CD GLN A1267 9218 14240 9875 363 838 937 C ATOM 2529 OE1 GLN A1267 -4.767 -19.097 -71.012 1.00 95.68 O ANISOU 2529 OE1 GLN A1267 10286 15178 10891 312 703 818 O ATOM 2530 NE2 GLN A1267 -3.477 -17.602 -72.080 1.00 92.44 N ANISOU 2530 NE2 GLN A1267 9573 14898 10651 249 898 1025 N ATOM 2531 N LEU A1268 -2.910 -23.280 -73.768 1.00 62.01 N ANISOU 2531 N LEU A1268 6628 11047 5887 1183 1149 927 N ATOM 2532 CA LEU A1268 -1.544 -23.758 -73.943 1.00 69.20 C ANISOU 2532 CA LEU A1268 7427 12119 6749 1416 1308 1023 C ATOM 2533 C LEU A1268 -1.349 -24.542 -75.233 1.00 78.07 C ANISOU 2533 C LEU A1268 8797 13225 7639 1636 1469 1055 C ATOM 2534 O LEU A1268 -0.201 -24.769 -75.629 1.00 76.58 O ANISOU 2534 O LEU A1268 8503 13189 7405 1841 1637 1165 O ATOM 2535 CB LEU A1268 -1.134 -24.629 -72.753 1.00 62.73 C ANISOU 2535 CB LEU A1268 6583 11324 5927 1535 1261 972 C ATOM 2536 CG LEU A1268 -0.988 -23.928 -71.402 1.00 65.44 C ANISOU 2536 CG LEU A1268 6644 11746 6473 1374 1121 949 C ATOM 2537 CD1 LEU A1268 -0.635 -24.927 -70.311 1.00 76.52 C ANISOU 2537 CD1 LEU A1268 8071 13181 7824 1537 1081 909 C ATOM 2538 CD2 LEU A1268 0.059 -22.828 -71.486 1.00 58.36 C ANISOU 2538 CD2 LEU A1268 5372 11057 5746 1304 1180 1064 C ATOM 2539 N GLY A1269 -2.426 -24.953 -75.893 1.00 68.57 N ANISOU 2539 N GLY A1269 7913 11857 6284 1600 1422 960 N ATOM 2540 CA GLY A1269 -2.321 -25.777 -77.077 1.00 69.18 C ANISOU 2540 CA GLY A1269 8270 11902 6113 1805 1556 953 C ATOM 2541 C GLY A1269 -2.380 -27.265 -76.825 1.00 79.97 C ANISOU 2541 C GLY A1269 9930 13137 7318 1983 1575 840 C ATOM 2542 O GLY A1269 -2.191 -28.042 -77.768 1.00 82.36 O ANISOU 2542 O GLY A1269 10489 13401 7403 2179 1702 820 O ATOM 2543 N ILE A1270 -2.627 -27.688 -75.582 1.00 60.27 N ANISOU 2543 N ILE A1270 7421 10562 4914 1930 1465 769 N ATOM 2544 CA ILE A1270 -2.750 -29.112 -75.289 1.00 78.22 C ANISOU 2544 CA ILE A1270 9999 12674 7047 2090 1493 671 C ATOM 2545 C ILE A1270 -3.962 -29.699 -75.998 1.00 82.34 C ANISOU 2545 C ILE A1270 10898 12979 7410 1992 1430 517 C ATOM 2546 O ILE A1270 -3.949 -30.866 -76.409 1.00 96.55 O ANISOU 2546 O ILE A1270 13023 14637 9025 2157 1517 438 O ATOM 2547 CB ILE A1270 -2.818 -29.337 -73.765 1.00 74.86 C ANISOU 2547 CB ILE A1270 9467 12218 6758 2042 1386 646 C ATOM 2548 CG1 ILE A1270 -1.704 -28.561 -73.059 1.00 83.16 C ANISOU 2548 CG1 ILE A1270 10103 13519 7976 2083 1404 779 C ATOM 2549 CG2 ILE A1270 -2.715 -30.820 -73.436 1.00 78.05 C ANISOU 2549 CG2 ILE A1270 10169 12462 7023 2256 1460 588 C ATOM 2550 CD1 ILE A1270 -0.309 -29.002 -73.445 1.00 93.29 C ANISOU 2550 CD1 ILE A1270 11300 14969 9177 2398 1600 902 C ATOM 2551 N ILE A1271 -5.020 -28.907 -76.158 1.00 77.99 N ANISOU 2551 N ILE A1271 10309 12398 6925 1724 1278 469 N ATOM 2552 CA ILE A1271 -6.214 -29.310 -76.893 1.00 79.02 C ANISOU 2552 CA ILE A1271 10742 12372 6912 1599 1192 327 C ATOM 2553 C ILE A1271 -6.663 -28.136 -77.752 1.00 75.42 C ANISOU 2553 C ILE A1271 10163 12028 6464 1459 1137 380 C ATOM 2554 O ILE A1271 -6.754 -27.003 -77.268 1.00 70.61 O ANISOU 2554 O ILE A1271 9267 11513 6050 1313 1066 464 O ATOM 2555 CB ILE A1271 -7.348 -29.766 -75.952 1.00 81.20 C ANISOU 2555 CB ILE A1271 11124 12466 7262 1398 1030 197 C ATOM 2556 CG1 ILE A1271 -7.468 -28.821 -74.754 1.00 93.55 C ANISOU 2556 CG1 ILE A1271 12363 14111 9072 1241 923 263 C ATOM 2557 CG2 ILE A1271 -7.116 -31.195 -75.488 1.00 91.99 C ANISOU 2557 CG2 ILE A1271 12756 13657 8540 1552 1108 122 C ATOM 2558 CD1 ILE A1271 -8.448 -29.291 -73.698 1.00100.85 C ANISOU 2558 CD1 ILE A1271 13370 14877 10073 1080 796 161 C ATOM 2559 N ARG A1272 -6.932 -28.404 -79.031 1.00 78.34 N ANISOU 2559 N ARG A1272 10765 12388 6615 1516 1174 333 N ATOM 2560 CA ARG A1272 -7.354 -27.375 -79.975 1.00 76.99 C ANISOU 2560 CA ARG A1272 10516 12331 6407 1426 1136 397 C ATOM 2561 C ARG A1272 -8.678 -27.712 -80.649 1.00 86.76 C ANISOU 2561 C ARG A1272 12009 13477 7480 1284 985 242 C ATOM 2562 O ARG A1272 -9.074 -27.020 -81.595 1.00111.50 O ANISOU 2562 O ARG A1272 15132 16712 10519 1248 952 286 O ATOM 2563 CB ARG A1272 -6.271 -27.148 -81.034 1.00 85.82 C ANISOU 2563 CB ARG A1272 11615 13599 7393 1657 1341 531 C ATOM 2564 N ASP A1273 -9.370 -28.751 -80.190 1.00 83.54 N ANISOU 2564 N ASP A1273 11822 12888 7034 1200 892 68 N ATOM 2565 CA ASP A1273 -10.636 -29.143 -80.793 1.00 83.07 C ANISOU 2565 CA ASP A1273 11989 12748 6825 1038 736 -97 C ATOM 2566 C ASP A1273 -11.730 -28.150 -80.418 1.00 76.91 C ANISOU 2566 C ASP A1273 10991 12028 6204 786 547 -72 C ATOM 2567 O ASP A1273 -11.885 -27.793 -79.247 1.00 86.87 O ANISOU 2567 O ASP A1273 12051 13259 7697 675 495 -33 O ATOM 2568 CB ASP A1273 -11.017 -30.552 -80.337 1.00 91.82 C ANISOU 2568 CB ASP A1273 13387 13623 7877 1000 710 -284 C ATOM 2569 CG ASP A1273 -12.252 -31.083 -81.039 1.00113.56 C ANISOU 2569 CG ASP A1273 16393 16293 10463 820 553 -480 C ATOM 2570 OD1 ASP A1273 -12.691 -30.471 -82.035 1.00127.13 O ANISOU 2570 OD1 ASP A1273 18095 18156 12052 781 477 -472 O ATOM 2571 OD2 ASP A1273 -12.785 -32.120 -80.590 1.00119.23 O ANISOU 2571 OD2 ASP A1273 17322 16803 11176 714 506 -637 O ATOM 2572 N CYS A1274 -12.490 -27.702 -81.420 1.00 68.60 N ANISOU 2572 N CYS A1274 9980 11070 5013 713 447 -90 N ATOM 2573 CA CYS A1274 -13.629 -26.830 -81.160 1.00 68.92 C ANISOU 2573 CA CYS A1274 9836 11173 5179 497 267 -69 C ATOM 2574 C CYS A1274 -14.810 -27.571 -80.548 1.00 66.83 C ANISOU 2574 C CYS A1274 9669 10773 4952 276 98 -244 C ATOM 2575 O CYS A1274 -15.724 -26.920 -80.031 1.00 65.14 O ANISOU 2575 O CYS A1274 9268 10596 4886 100 -37 -220 O ATOM 2576 CB CYS A1274 -14.076 -26.134 -82.448 1.00 79.99 C ANISOU 2576 CB CYS A1274 11248 12741 6402 515 212 -17 C ATOM 2577 SG CYS A1274 -13.041 -24.743 -82.968 1.00 92.31 S ANISOU 2577 SG CYS A1274 12580 14477 8015 692 385 254 S ATOM 2578 N ARG A1275 -14.818 -28.905 -80.595 1.00 70.86 N ANISOU 2578 N ARG A1275 10467 11120 5337 282 116 -413 N ATOM 2579 CA ARG A1275 -15.904 -29.657 -79.973 1.00 76.41 C ANISOU 2579 CA ARG A1275 11263 11674 6096 53 -22 -572 C ATOM 2580 C ARG A1275 -15.816 -29.595 -78.454 1.00 81.62 C ANISOU 2580 C ARG A1275 11750 12241 7020 -5 2 -511 C ATOM 2581 O ARG A1275 -16.831 -29.401 -77.775 1.00 88.20 O ANISOU 2581 O ARG A1275 12463 13058 7991 -213 -128 -538 O ATOM 2582 CB ARG A1275 -15.886 -31.108 -80.453 1.00 88.77 C ANISOU 2582 CB ARG A1275 13212 13055 7461 72 11 -770 C ATOM 2583 N ILE A1276 -14.612 -29.758 -77.901 1.00 85.35 N ANISOU 2583 N ILE A1276 12202 12673 7556 187 168 -427 N ATOM 2584 CA ILE A1276 -14.441 -29.633 -76.459 1.00 81.89 C ANISOU 2584 CA ILE A1276 11590 12179 7344 158 187 -361 C ATOM 2585 C ILE A1276 -14.430 -28.176 -76.017 1.00 76.30 C ANISOU 2585 C ILE A1276 10533 11637 6819 115 145 -212 C ATOM 2586 O ILE A1276 -14.656 -27.894 -74.834 1.00 80.13 O ANISOU 2586 O ILE A1276 10859 12097 7490 31 109 -181 O ATOM 2587 CB ILE A1276 -13.162 -30.351 -75.995 1.00 75.89 C ANISOU 2587 CB ILE A1276 10920 11341 6575 389 365 -324 C ATOM 2588 CG1 ILE A1276 -11.945 -29.872 -76.790 1.00 89.14 C ANISOU 2588 CG1 ILE A1276 12532 13168 8168 622 503 -208 C ATOM 2589 CG2 ILE A1276 -13.324 -31.856 -76.131 1.00 84.20 C ANISOU 2589 CG2 ILE A1276 12338 12167 7489 409 411 -477 C ATOM 2590 CD1 ILE A1276 -11.149 -28.772 -76.114 1.00 97.69 C ANISOU 2590 CD1 ILE A1276 13271 14406 9440 680 548 -37 C ATOM 2591 N ALA A1277 -14.164 -27.241 -76.930 1.00 63.68 N ANISOU 2591 N ALA A1277 8829 10196 5170 178 161 -118 N ATOM 2592 CA ALA A1277 -14.289 -25.830 -76.586 1.00 68.15 C ANISOU 2592 CA ALA A1277 9095 10885 5912 116 121 15 C ATOM 2593 C ALA A1277 -15.749 -25.430 -76.436 1.00 75.95 C ANISOU 2593 C ALA A1277 10016 11884 6958 -96 -53 -30 C ATOM 2594 O ALA A1277 -16.059 -24.479 -75.709 1.00 69.22 O ANISOU 2594 O ALA A1277 8938 11071 6291 -174 -96 46 O ATOM 2595 CB ALA A1277 -13.600 -24.964 -77.642 1.00 57.73 C ANISOU 2595 CB ALA A1277 7700 9712 4523 246 209 146 C ATOM 2596 N ASP A1278 -16.655 -26.144 -77.108 1.00 77.96 N ANISOU 2596 N ASP A1278 10457 12108 7054 -191 -155 -157 N ATOM 2597 CA ASP A1278 -18.078 -25.859 -76.972 1.00 78.97 C ANISOU 2597 CA ASP A1278 10502 12272 7233 -395 -326 -201 C ATOM 2598 C ASP A1278 -18.589 -26.276 -75.599 1.00 87.35 C ANISOU 2598 C ASP A1278 11512 13210 8468 -530 -360 -253 C ATOM 2599 O ASP A1278 -19.255 -25.493 -74.911 1.00 89.94 O ANISOU 2599 O ASP A1278 11631 13587 8956 -628 -426 -195 O ATOM 2600 CB ASP A1278 -18.859 -26.565 -78.080 1.00 75.96 C ANISOU 2600 CB ASP A1278 10325 11911 6626 -474 -436 -338 C ATOM 2601 CG ASP A1278 -20.352 -26.337 -77.974 1.00 84.73 C ANISOU 2601 CG ASP A1278 11323 13088 7782 -690 -623 -384 C ATOM 2602 OD1 ASP A1278 -20.789 -25.176 -78.122 1.00 87.26 O ANISOU 2602 OD1 ASP A1278 11429 13560 8165 -690 -682 -263 O ATOM 2603 OD2 ASP A1278 -21.090 -27.318 -77.745 1.00 92.31 O ANISOU 2603 OD2 ASP A1278 12405 13947 8721 -858 -703 -534 O ATOM 2604 N ILE A1279 -18.283 -27.506 -75.179 1.00 87.98 N ANISOU 2604 N ILE A1279 11792 13125 8512 -522 -300 -353 N ATOM 2605 CA ILE A1279 -18.738 -27.982 -73.878 1.00 94.60 C ANISOU 2605 CA ILE A1279 12607 13840 9499 -636 -311 -388 C ATOM 2606 C ILE A1279 -18.085 -27.206 -72.739 1.00 86.74 C ANISOU 2606 C ILE A1279 11395 12876 8685 -551 -243 -265 C ATOM 2607 O ILE A1279 -18.658 -27.116 -71.646 1.00 99.98 O ANISOU 2607 O ILE A1279 12969 14517 10503 -652 -277 -260 O ATOM 2608 CB ILE A1279 -18.483 -29.498 -73.748 1.00 92.37 C ANISOU 2608 CB ILE A1279 12620 13351 9125 -621 -238 -507 C ATOM 2609 CG1 ILE A1279 -19.147 -30.057 -72.487 1.00106.79 C ANISOU 2609 CG1 ILE A1279 14444 15041 11089 -763 -250 -538 C ATOM 2610 CG2 ILE A1279 -16.994 -29.802 -73.750 1.00 75.43 C ANISOU 2610 CG2 ILE A1279 10566 11170 6925 -366 -72 -453 C ATOM 2611 CD1 ILE A1279 -20.646 -29.860 -72.446 1.00112.20 C ANISOU 2611 CD1 ILE A1279 15026 15768 11835 -1019 -402 -588 C ATOM 2612 N VAL A1280 -16.907 -26.626 -72.968 1.00 73.22 N ANISOU 2612 N VAL A1280 9605 11242 6972 -374 -147 -169 N ATOM 2613 CA VAL A1280 -16.283 -25.786 -71.950 1.00 62.20 C ANISOU 2613 CA VAL A1280 7987 9897 5749 -319 -102 -69 C ATOM 2614 C VAL A1280 -16.937 -24.410 -71.911 1.00 69.64 C ANISOU 2614 C VAL A1280 8701 10946 6813 -413 -182 3 C ATOM 2615 O VAL A1280 -17.199 -23.866 -70.832 1.00 70.97 O ANISOU 2615 O VAL A1280 8717 11113 7136 -471 -207 27 O ATOM 2616 CB VAL A1280 -14.765 -25.692 -72.197 1.00 56.77 C ANISOU 2616 CB VAL A1280 7279 9261 5028 -114 31 6 C ATOM 2617 CG1 VAL A1280 -14.166 -24.528 -71.423 1.00 55.21 C ANISOU 2617 CG1 VAL A1280 6814 9157 5009 -94 51 106 C ATOM 2618 CG2 VAL A1280 -14.085 -26.993 -71.800 1.00 59.00 C ANISOU 2618 CG2 VAL A1280 7750 9434 5235 9 123 -45 C ATOM 2619 N ASP A1281 -17.223 -23.831 -73.079 1.00 68.86 N ANISOU 2619 N ASP A1281 8591 10940 6635 -415 -216 41 N ATOM 2620 CA ASP A1281 -17.850 -22.517 -73.132 1.00 63.85 C ANISOU 2620 CA ASP A1281 7759 10395 6105 -476 -276 126 C ATOM 2621 C ASP A1281 -19.329 -22.550 -72.769 1.00 67.40 C ANISOU 2621 C ASP A1281 8169 10843 6597 -638 -406 75 C ATOM 2622 O ASP A1281 -19.903 -21.496 -72.477 1.00 62.34 O ANISOU 2622 O ASP A1281 7354 10258 6075 -678 -446 145 O ATOM 2623 CB ASP A1281 -17.674 -21.904 -74.522 1.00 66.06 C ANISOU 2623 CB ASP A1281 8047 10783 6269 -399 -260 207 C ATOM 2624 CG ASP A1281 -16.279 -21.353 -74.741 1.00 67.29 C ANISOU 2624 CG ASP A1281 8140 10971 6457 -256 -117 313 C ATOM 2625 OD1 ASP A1281 -15.663 -20.890 -73.758 1.00 77.72 O ANISOU 2625 OD1 ASP A1281 9319 12263 7946 -251 -65 349 O ATOM 2626 OD2 ASP A1281 -15.798 -21.379 -75.894 1.00 76.06 O ANISOU 2626 OD2 ASP A1281 9335 12145 7420 -152 -56 359 O ATOM 2627 N THR A1282 -19.959 -23.724 -72.783 1.00 77.75 N ANISOU 2627 N THR A1282 9634 12086 7820 -733 -462 -44 N ATOM 2628 CA THR A1282 -21.339 -23.839 -72.327 1.00 76.87 C ANISOU 2628 CA THR A1282 9460 11980 7768 -904 -574 -90 C ATOM 2629 C THR A1282 -21.428 -24.051 -70.823 1.00 66.87 C ANISOU 2629 C THR A1282 8136 10618 6654 -950 -536 -100 C ATOM 2630 O THR A1282 -22.296 -23.469 -70.164 1.00 78.26 O ANISOU 2630 O THR A1282 9421 12100 8215 -1031 -585 -69 O ATOM 2631 CB THR A1282 -22.052 -24.991 -73.043 1.00 88.27 C ANISOU 2631 CB THR A1282 11087 13392 9058 -1024 -657 -219 C ATOM 2632 OG1 THR A1282 -21.286 -26.194 -72.904 1.00 97.17 O ANISOU 2632 OG1 THR A1282 12443 14364 10112 -979 -568 -304 O ATOM 2633 CG2 THR A1282 -22.240 -24.674 -74.514 1.00 93.59 C ANISOU 2633 CG2 THR A1282 11795 14201 9562 -993 -729 -214 C ATOM 2634 N ALA A1283 -20.543 -24.879 -70.267 1.00 55.55 N ANISOU 2634 N ALA A1283 6832 9069 5206 -879 -444 -136 N ATOM 2635 CA ALA A1283 -20.569 -25.165 -68.841 1.00 55.11 C ANISOU 2635 CA ALA A1283 6745 8932 5263 -898 -403 -140 C ATOM 2636 C ALA A1283 -20.010 -24.027 -67.999 1.00 49.54 C ANISOU 2636 C ALA A1283 5845 8286 4690 -815 -366 -57 C ATOM 2637 O ALA A1283 -20.318 -23.954 -66.805 1.00 67.47 O ANISOU 2637 O ALA A1283 8047 10531 7058 -846 -359 -55 O ATOM 2638 CB ALA A1283 -19.791 -26.448 -68.548 1.00 57.83 C ANISOU 2638 CB ALA A1283 7303 9139 5531 -822 -312 -192 C ATOM 2639 N MET A1284 -19.201 -23.144 -68.587 1.00 58.24 N ANISOU 2639 N MET A1284 6866 9466 5798 -717 -338 7 N ATOM 2640 CA MET A1284 -18.602 -22.063 -67.806 1.00 62.54 C ANISOU 2640 CA MET A1284 7237 10051 6477 -662 -304 67 C ATOM 2641 C MET A1284 -19.643 -21.131 -67.198 1.00 74.79 C ANISOU 2641 C MET A1284 8638 11628 8152 -750 -360 89 C ATOM 2642 O MET A1284 -19.513 -20.796 -66.007 1.00 80.27 O ANISOU 2642 O MET A1284 9252 12303 8942 -743 -343 82 O ATOM 2643 CB MET A1284 -17.591 -21.298 -68.667 1.00 63.57 C ANISOU 2643 CB MET A1284 7308 10246 6599 -567 -251 139 C ATOM 2644 CG MET A1284 -16.800 -20.252 -67.899 1.00 67.84 C ANISOU 2644 CG MET A1284 7679 10814 7283 -531 -211 184 C ATOM 2645 SD MET A1284 -15.771 -20.965 -66.600 1.00 75.37 S ANISOU 2645 SD MET A1284 8637 11750 8249 -454 -168 136 S ATOM 2646 CE MET A1284 -14.606 -21.916 -67.573 1.00 70.02 C ANISOU 2646 CE MET A1284 8087 11092 7427 -313 -82 156 C ATOM 2647 N PRO A1285 -20.676 -20.674 -67.918 1.00 71.40 N ANISOU 2647 N PRO A1285 8163 11250 7715 -818 -426 116 N ATOM 2648 CA PRO A1285 -21.741 -19.921 -67.233 1.00 68.43 C ANISOU 2648 CA PRO A1285 7650 10898 7453 -881 -467 139 C ATOM 2649 C PRO A1285 -22.486 -20.749 -66.202 1.00 64.93 C ANISOU 2649 C PRO A1285 7236 10408 7028 -963 -480 80 C ATOM 2650 O PRO A1285 -22.952 -20.199 -65.196 1.00 65.60 O ANISOU 2650 O PRO A1285 7217 10493 7215 -974 -470 92 O ATOM 2651 CB PRO A1285 -22.661 -19.486 -68.382 1.00 64.83 C ANISOU 2651 CB PRO A1285 7151 10532 6949 -915 -539 188 C ATOM 2652 CG PRO A1285 -21.798 -19.507 -69.588 1.00 65.80 C ANISOU 2652 CG PRO A1285 7356 10680 6964 -840 -515 216 C ATOM 2653 CD PRO A1285 -20.865 -20.658 -69.380 1.00 69.77 C ANISOU 2653 CD PRO A1285 8009 11106 7393 -812 -463 142 C ATOM 2654 N ILE A1286 -22.616 -22.059 -66.425 1.00 52.69 N ANISOU 2654 N ILE A1286 5834 8805 5379 -1021 -489 18 N ATOM 2655 CA ILE A1286 -23.247 -22.926 -65.434 1.00 56.36 C ANISOU 2655 CA ILE A1286 6344 9202 5867 -1103 -476 -24 C ATOM 2656 C ILE A1286 -22.404 -22.987 -64.167 1.00 61.45 C ANISOU 2656 C ILE A1286 7002 9792 6554 -1008 -396 -24 C ATOM 2657 O ILE A1286 -22.928 -22.897 -63.050 1.00 56.57 O ANISOU 2657 O ILE A1286 6325 9166 6002 -1031 -376 -17 O ATOM 2658 CB ILE A1286 -23.482 -24.328 -66.024 1.00 51.48 C ANISOU 2658 CB ILE A1286 5915 8507 5139 -1193 -490 -96 C ATOM 2659 CG1 ILE A1286 -24.427 -24.253 -67.225 1.00 54.42 C ANISOU 2659 CG1 ILE A1286 6258 8965 5455 -1306 -596 -114 C ATOM 2660 CG2 ILE A1286 -24.036 -25.271 -64.965 1.00 46.02 C ANISOU 2660 CG2 ILE A1286 5288 7716 4480 -1280 -447 -124 C ATOM 2661 CD1 ILE A1286 -25.830 -23.821 -66.870 1.00 64.30 C ANISOU 2661 CD1 ILE A1286 7331 10304 6795 -1427 -660 -84 C ATOM 2662 N THR A1287 -21.086 -23.137 -64.318 1.00 62.22 N ANISOU 2662 N THR A1287 7168 9871 6604 -889 -350 -26 N ATOM 2663 CA THR A1287 -20.210 -23.209 -63.153 1.00 59.35 C ANISOU 2663 CA THR A1287 6800 9489 6261 -786 -293 -27 C ATOM 2664 C THR A1287 -20.134 -21.877 -62.419 1.00 56.85 C ANISOU 2664 C THR A1287 6307 9240 6055 -762 -305 -6 C ATOM 2665 O THR A1287 -19.954 -21.855 -61.196 1.00 71.43 O ANISOU 2665 O THR A1287 8129 11086 7924 -720 -282 -21 O ATOM 2666 CB THR A1287 -18.813 -23.663 -63.572 1.00 55.39 C ANISOU 2666 CB THR A1287 6383 8982 5682 -657 -244 -26 C ATOM 2667 OG1 THR A1287 -18.282 -22.753 -64.544 1.00 62.20 O ANISOU 2667 OG1 THR A1287 7156 9916 6560 -628 -256 7 O ATOM 2668 CG2 THR A1287 -18.862 -25.063 -64.165 1.00 49.32 C ANISOU 2668 CG2 THR A1287 5831 8114 4795 -662 -213 -59 C ATOM 2669 N ILE A1288 -20.264 -20.761 -63.141 1.00 58.09 N ANISOU 2669 N ILE A1288 6354 9446 6271 -781 -335 26 N ATOM 2670 CA ILE A1288 -20.299 -19.458 -62.486 1.00 53.89 C ANISOU 2670 CA ILE A1288 5679 8943 5853 -770 -337 36 C ATOM 2671 C ILE A1288 -21.590 -19.297 -61.693 1.00 55.01 C ANISOU 2671 C ILE A1288 5777 9082 6044 -827 -350 32 C ATOM 2672 O ILE A1288 -21.593 -18.739 -60.589 1.00 56.05 O ANISOU 2672 O ILE A1288 5852 9214 6232 -798 -332 8 O ATOM 2673 CB ILE A1288 -20.118 -18.334 -63.523 1.00 54.21 C ANISOU 2673 CB ILE A1288 5639 9012 5948 -766 -344 90 C ATOM 2674 CG1 ILE A1288 -18.699 -18.359 -64.094 1.00 61.24 C ANISOU 2674 CG1 ILE A1288 6543 9916 6808 -700 -307 103 C ATOM 2675 CG2 ILE A1288 -20.423 -16.974 -62.910 1.00 43.42 C ANISOU 2675 CG2 ILE A1288 4153 7637 4709 -769 -338 99 C ATOM 2676 CD1 ILE A1288 -18.442 -17.299 -65.143 1.00 75.52 C ANISOU 2676 CD1 ILE A1288 8284 11744 8667 -694 -289 176 C ATOM 2677 N CYS A1289 -22.706 -19.796 -62.235 1.00 58.21 N ANISOU 2677 N CYS A1289 6201 9495 6422 -910 -380 51 N ATOM 2678 CA CYS A1289 -23.971 -19.736 -61.511 1.00 59.12 C ANISOU 2678 CA CYS A1289 6252 9627 6585 -967 -380 61 C ATOM 2679 C CYS A1289 -23.942 -20.586 -60.248 1.00 60.80 C ANISOU 2679 C CYS A1289 6537 9796 6771 -959 -328 30 C ATOM 2680 O CYS A1289 -24.672 -20.299 -59.295 1.00 73.84 O ANISOU 2680 O CYS A1289 8124 11463 8467 -961 -298 39 O ATOM 2681 CB CYS A1289 -25.121 -20.180 -62.415 1.00 50.20 C ANISOU 2681 CB CYS A1289 5105 8538 5429 -1076 -434 85 C ATOM 2682 SG CYS A1289 -25.596 -18.981 -63.677 1.00 65.59 S ANISOU 2682 SG CYS A1289 6932 10582 7409 -1061 -496 154 S ATOM 2683 N ILE A1290 -23.116 -21.628 -60.219 1.00 59.04 N ANISOU 2683 N ILE A1290 6451 9517 6465 -931 -304 4 N ATOM 2684 CA ILE A1290 -23.018 -22.484 -59.041 1.00 66.79 C ANISOU 2684 CA ILE A1290 7520 10452 7405 -898 -243 -5 C ATOM 2685 C ILE A1290 -22.025 -21.924 -58.030 1.00 69.80 C ANISOU 2685 C ILE A1290 7870 10869 7783 -769 -226 -28 C ATOM 2686 O ILE A1290 -22.278 -21.952 -56.823 1.00 69.64 O ANISOU 2686 O ILE A1290 7847 10859 7753 -730 -188 -29 O ATOM 2687 CB ILE A1290 -22.645 -23.919 -59.465 1.00 60.16 C ANISOU 2687 CB ILE A1290 6863 9522 6472 -910 -214 -15 C ATOM 2688 CG1 ILE A1290 -23.758 -24.527 -60.321 1.00 58.06 C ANISOU 2688 CG1 ILE A1290 6633 9218 6208 -1073 -242 -18 C ATOM 2689 CG2 ILE A1290 -22.370 -24.791 -58.248 1.00 50.83 C ANISOU 2689 CG2 ILE A1290 5791 8284 5239 -839 -136 -2 C ATOM 2690 CD1 ILE A1290 -23.461 -25.930 -60.803 1.00 59.38 C ANISOU 2690 CD1 ILE A1290 7010 9263 6287 -1103 -209 -48 C ATOM 2691 N ALA A1291 -20.896 -21.396 -58.504 1.00 76.16 N ANISOU 2691 N ALA A1291 8642 11704 8589 -705 -253 -46 N ATOM 2692 CA ALA A1291 -19.858 -20.922 -57.594 1.00 59.65 C ANISOU 2692 CA ALA A1291 6507 9665 6491 -603 -255 -81 C ATOM 2693 C ALA A1291 -20.279 -19.639 -56.889 1.00 60.08 C ANISOU 2693 C ALA A1291 6446 9752 6630 -615 -271 -114 C ATOM 2694 O ALA A1291 -20.173 -19.531 -55.662 1.00 83.55 O ANISOU 2694 O ALA A1291 9417 12756 9572 -558 -261 -152 O ATOM 2695 CB ALA A1291 -18.550 -20.712 -58.358 1.00 58.18 C ANISOU 2695 CB ALA A1291 6292 9512 6300 -553 -273 -85 C ATOM 2696 N TYR A1292 -20.763 -18.656 -57.646 1.00 62.22 N ANISOU 2696 N TYR A1292 6633 10012 6994 -675 -290 -99 N ATOM 2697 CA TYR A1292 -21.039 -17.338 -57.091 1.00 63.35 C ANISOU 2697 CA TYR A1292 6687 10159 7226 -672 -292 -132 C ATOM 2698 C TYR A1292 -22.409 -17.228 -56.437 1.00 65.48 C ANISOU 2698 C TYR A1292 6942 10426 7513 -684 -259 -116 C ATOM 2699 O TYR A1292 -22.646 -16.270 -55.693 1.00 74.18 O ANISOU 2699 O TYR A1292 7999 11523 8662 -651 -243 -157 O ATOM 2700 CB TYR A1292 -20.891 -16.272 -58.180 1.00 53.58 C ANISOU 2700 CB TYR A1292 5376 8896 6084 -705 -306 -104 C ATOM 2701 CG TYR A1292 -19.458 -16.090 -58.625 1.00 62.50 C ANISOU 2701 CG TYR A1292 6488 10039 7221 -692 -319 -122 C ATOM 2702 CD1 TYR A1292 -18.900 -16.915 -59.593 1.00 58.18 C ANISOU 2702 CD1 TYR A1292 5985 9509 6610 -685 -320 -78 C ATOM 2703 CD2 TYR A1292 -18.656 -15.106 -58.062 1.00 50.88 C ANISOU 2703 CD2 TYR A1292 4950 8564 5818 -690 -328 -188 C ATOM 2704 CE1 TYR A1292 -17.588 -16.758 -59.995 1.00 51.91 C ANISOU 2704 CE1 TYR A1292 5153 8745 5823 -660 -316 -80 C ATOM 2705 CE2 TYR A1292 -17.343 -14.940 -58.459 1.00 50.07 C ANISOU 2705 CE2 TYR A1292 4798 8490 5734 -694 -336 -197 C ATOM 2706 CZ TYR A1292 -16.815 -15.769 -59.425 1.00 50.22 C ANISOU 2706 CZ TYR A1292 4846 8544 5692 -671 -325 -133 C ATOM 2707 OH TYR A1292 -15.508 -15.608 -59.822 1.00 51.40 O ANISOU 2707 OH TYR A1292 4927 8741 5862 -663 -318 -128 O ATOM 2708 N PHE A1293 -23.316 -18.174 -56.690 1.00 55.18 N ANISOU 2708 N PHE A1293 5672 9121 6173 -734 -241 -61 N ATOM 2709 CA PHE A1293 -24.550 -18.211 -55.911 1.00 53.19 C ANISOU 2709 CA PHE A1293 5391 8887 5933 -743 -194 -36 C ATOM 2710 C PHE A1293 -24.295 -18.766 -54.517 1.00 66.29 C ANISOU 2710 C PHE A1293 7124 10555 7510 -674 -145 -67 C ATOM 2711 O PHE A1293 -24.811 -18.234 -53.527 1.00 86.38 O ANISOU 2711 O PHE A1293 9639 13124 10059 -622 -102 -83 O ATOM 2712 CB PHE A1293 -25.615 -19.039 -56.630 1.00 46.89 C ANISOU 2712 CB PHE A1293 4585 8096 5136 -847 -194 32 C ATOM 2713 CG PHE A1293 -26.847 -19.286 -55.805 1.00 60.36 C ANISOU 2713 CG PHE A1293 6247 9832 6854 -871 -129 72 C ATOM 2714 CD1 PHE A1293 -27.746 -18.262 -55.556 1.00 65.10 C ANISOU 2714 CD1 PHE A1293 6725 10484 7528 -838 -105 99 C ATOM 2715 CD2 PHE A1293 -27.107 -20.542 -55.281 1.00 58.34 C ANISOU 2715 CD2 PHE A1293 6076 9549 6540 -918 -77 95 C ATOM 2716 CE1 PHE A1293 -28.880 -18.485 -54.797 1.00 62.88 C ANISOU 2716 CE1 PHE A1293 6385 10248 7258 -849 -30 149 C ATOM 2717 CE2 PHE A1293 -28.240 -20.771 -54.522 1.00 59.50 C ANISOU 2717 CE2 PHE A1293 6171 9730 6707 -947 1 148 C ATOM 2718 CZ PHE A1293 -29.127 -19.741 -54.280 1.00 65.17 C ANISOU 2718 CZ PHE A1293 6745 10522 7495 -912 24 175 C ATOM 2719 N ASN A1294 -23.499 -19.834 -54.420 1.00 56.33 N ANISOU 2719 N ASN A1294 5967 9277 6159 -652 -145 -70 N ATOM 2720 CA ASN A1294 -23.124 -20.356 -53.112 1.00 47.57 C ANISOU 2720 CA ASN A1294 4934 8189 4950 -557 -102 -86 C ATOM 2721 C ASN A1294 -22.214 -19.390 -52.366 1.00 61.00 C ANISOU 2721 C ASN A1294 6597 9948 6632 -465 -145 -176 C ATOM 2722 O ASN A1294 -22.277 -19.309 -51.134 1.00 76.29 O ANISOU 2722 O ASN A1294 8561 11930 8497 -383 -116 -206 O ATOM 2723 CB ASN A1294 -22.440 -21.715 -53.258 1.00 41.65 C ANISOU 2723 CB ASN A1294 4313 7403 4108 -530 -86 -54 C ATOM 2724 CG ASN A1294 -23.374 -22.787 -53.783 1.00 62.73 C ANISOU 2724 CG ASN A1294 7053 9992 6787 -638 -34 15 C ATOM 2725 OD1 ASN A1294 -22.950 -23.707 -54.483 1.00 85.56 O ANISOU 2725 OD1 ASN A1294 10048 12819 9644 -660 -33 29 O ATOM 2726 ND2 ASN A1294 -24.654 -22.673 -53.450 1.00 60.42 N ANISOU 2726 ND2 ASN A1294 6706 9707 6545 -711 13 53 N ATOM 2727 N ASN A1295 -21.367 -18.652 -53.088 1.00 53.27 N ANISOU 2727 N ASN A1295 5556 8971 5713 -483 -211 -222 N ATOM 2728 CA ASN A1295 -20.457 -17.720 -52.430 1.00 57.04 C ANISOU 2728 CA ASN A1295 5988 9497 6189 -433 -261 -322 C ATOM 2729 C ASN A1295 -21.197 -16.518 -51.858 1.00 64.01 C ANISOU 2729 C ASN A1295 6827 10359 7134 -436 -242 -378 C ATOM 2730 O ASN A1295 -20.810 -16.001 -50.804 1.00 83.57 O ANISOU 2730 O ASN A1295 9312 12878 9561 -379 -262 -475 O ATOM 2731 CB ASN A1295 -19.374 -17.262 -53.406 1.00 51.76 C ANISOU 2731 CB ASN A1295 5253 8826 5586 -473 -318 -343 C ATOM 2732 CG ASN A1295 -18.354 -16.350 -52.755 1.00 66.30 C ANISOU 2732 CG ASN A1295 7030 10721 7438 -455 -377 -456 C ATOM 2733 OD1 ASN A1295 -17.505 -16.801 -51.986 1.00 74.00 O ANISOU 2733 OD1 ASN A1295 8015 11792 8310 -382 -416 -500 O ATOM 2734 ND2 ASN A1295 -18.429 -15.060 -53.062 1.00 64.51 N ANISOU 2734 ND2 ASN A1295 6740 10433 7337 -524 -386 -504 N ATOM 2735 N CYS A1296 -22.254 -16.060 -52.528 1.00 65.45 N ANISOU 2735 N CYS A1296 6967 10486 7416 -491 -206 -322 N ATOM 2736 CA CYS A1296 -23.045 -14.949 -52.014 1.00 67.74 C ANISOU 2736 CA CYS A1296 7226 10748 7765 -465 -166 -358 C ATOM 2737 C CYS A1296 -23.956 -15.354 -50.864 1.00 71.69 C ANISOU 2737 C CYS A1296 7767 11291 8182 -396 -92 -343 C ATOM 2738 O CYS A1296 -24.568 -14.479 -50.243 1.00 77.12 O ANISOU 2738 O CYS A1296 8445 11965 8892 -343 -45 -383 O ATOM 2739 CB CYS A1296 -23.874 -14.324 -53.138 1.00 69.21 C ANISOU 2739 CB CYS A1296 7341 10881 8076 -517 -148 -280 C ATOM 2740 SG CYS A1296 -22.902 -13.361 -54.323 1.00 80.23 S ANISOU 2740 SG CYS A1296 8692 12207 9583 -572 -201 -296 S ATOM 2741 N LEU A1297 -24.065 -16.648 -50.570 1.00 65.26 N ANISOU 2741 N LEU A1297 7007 10516 7272 -388 -65 -281 N ATOM 2742 CA LEU A1297 -24.781 -17.130 -49.398 1.00 63.72 C ANISOU 2742 CA LEU A1297 6863 10366 6983 -316 22 -253 C ATOM 2743 C LEU A1297 -23.849 -17.466 -48.243 1.00 56.26 C ANISOU 2743 C LEU A1297 6008 9485 5885 -210 3 -323 C ATOM 2744 O LEU A1297 -24.324 -17.860 -47.174 1.00 58.24 O ANISOU 2744 O LEU A1297 6317 9782 6029 -127 80 -298 O ATOM 2745 CB LEU A1297 -25.623 -18.358 -49.759 1.00 43.58 C ANISOU 2745 CB LEU A1297 4322 7805 4431 -384 86 -123 C ATOM 2746 CG LEU A1297 -26.769 -18.119 -50.743 1.00 64.45 C ANISOU 2746 CG LEU A1297 6857 10430 7202 -486 102 -48 C ATOM 2747 CD1 LEU A1297 -27.535 -19.407 -51.000 1.00 56.03 C ANISOU 2747 CD1 LEU A1297 5803 9356 6130 -583 155 57 C ATOM 2748 CD2 LEU A1297 -27.696 -17.034 -50.221 1.00 51.05 C ANISOU 2748 CD2 LEU A1297 5080 8762 5555 -422 163 -53 C ATOM 2749 N ASN A1298 -22.532 -17.320 -48.435 1.00 61.99 N ANISOU 2749 N ASN A1298 6734 10231 6589 -205 -97 -401 N ATOM 2750 CA ASN A1298 -21.594 -17.627 -47.356 1.00 67.97 C ANISOU 2750 CA ASN A1298 7553 11085 7187 -95 -137 -468 C ATOM 2751 C ASN A1298 -21.689 -16.640 -46.199 1.00 77.88 C ANISOU 2751 C ASN A1298 8823 12389 8378 -22 -143 -593 C ATOM 2752 O ASN A1298 -21.712 -17.088 -45.039 1.00 79.65 O ANISOU 2752 O ASN A1298 9126 12700 8436 97 -111 -598 O ATOM 2753 CB ASN A1298 -20.169 -17.717 -47.912 1.00 57.12 C ANISOU 2753 CB ASN A1298 6140 9747 5816 -113 -245 -512 C ATOM 2754 CG ASN A1298 -19.858 -19.080 -48.497 1.00 74.12 C ANISOU 2754 CG ASN A1298 8344 11890 7930 -101 -223 -395 C ATOM 2755 OD1 ASN A1298 -20.744 -19.918 -48.653 1.00 88.59 O ANISOU 2755 OD1 ASN A1298 10242 13660 9759 -118 -134 -289 O ATOM 2756 ND2 ASN A1298 -18.592 -19.307 -48.824 1.00 85.07 N ANISOU 2756 ND2 ASN A1298 9701 13333 9288 -73 -297 -417 N ATOM 2757 N PRO A1299 -21.733 -15.318 -46.413 1.00 73.61 N ANISOU 2757 N PRO A1299 8231 11790 7946 -74 -174 -698 N ATOM 2758 CA PRO A1299 -21.903 -14.411 -45.264 1.00 65.92 C ANISOU 2758 CA PRO A1299 7306 10842 6899 2 -166 -834 C ATOM 2759 C PRO A1299 -23.192 -14.640 -44.496 1.00 55.30 C ANISOU 2759 C PRO A1299 6019 9511 5482 98 -30 -763 C ATOM 2760 O PRO A1299 -23.261 -14.291 -43.311 1.00 59.96 O ANISOU 2760 O PRO A1299 6685 10162 5936 207 -10 -857 O ATOM 2761 CB PRO A1299 -21.873 -13.017 -45.906 1.00 63.53 C ANISOU 2761 CB PRO A1299 6950 10419 6768 -89 -193 -926 C ATOM 2762 CG PRO A1299 -21.106 -13.202 -47.159 1.00 66.26 C ANISOU 2762 CG PRO A1299 7214 10732 7230 -202 -262 -877 C ATOM 2763 CD PRO A1299 -21.490 -14.562 -47.656 1.00 67.56 C ANISOU 2763 CD PRO A1299 7381 10929 7362 -194 -218 -709 C ATOM 2764 N LEU A1300 -24.214 -15.218 -45.128 1.00 56.69 N ANISOU 2764 N LEU A1300 6156 9643 5740 58 65 -602 N ATOM 2765 CA LEU A1300 -25.462 -15.501 -44.429 1.00 48.11 C ANISOU 2765 CA LEU A1300 5095 8585 4600 136 209 -513 C ATOM 2766 C LEU A1300 -25.394 -16.826 -43.679 1.00 50.84 C ANISOU 2766 C LEU A1300 5522 9012 4783 207 263 -421 C ATOM 2767 O LEU A1300 -25.883 -16.926 -42.548 1.00 59.87 O ANISOU 2767 O LEU A1300 6733 10222 5792 328 359 -408 O ATOM 2768 CB LEU A1300 -26.626 -15.508 -45.421 1.00 55.09 C ANISOU 2768 CB LEU A1300 5874 9408 5650 48 281 -382 C ATOM 2769 CG LEU A1300 -28.027 -15.634 -44.821 1.00 60.61 C ANISOU 2769 CG LEU A1300 6549 10146 6333 112 439 -280 C ATOM 2770 CD1 LEU A1300 -28.324 -14.440 -43.933 1.00 69.67 C ANISOU 2770 CD1 LEU A1300 7735 11301 7436 246 493 -390 C ATOM 2771 CD2 LEU A1300 -29.072 -15.767 -45.918 1.00 61.85 C ANISOU 2771 CD2 LEU A1300 6569 10278 6654 3 477 -147 C ATOM 2772 N PHE A1301 -24.796 -17.851 -44.291 1.00 60.37 N ANISOU 2772 N PHE A1301 6739 10208 5993 147 217 -347 N ATOM 2773 CA PHE A1301 -24.694 -19.149 -43.631 1.00 66.39 C ANISOU 2773 CA PHE A1301 7601 11018 6608 223 283 -244 C ATOM 2774 C PHE A1301 -23.752 -19.090 -42.436 1.00 73.98 C ANISOU 2774 C PHE A1301 8649 12100 7358 383 227 -338 C ATOM 2775 O PHE A1301 -24.059 -19.638 -41.370 1.00 85.71 O ANISOU 2775 O PHE A1301 10229 13655 8681 511 323 -275 O ATOM 2776 CB PHE A1301 -24.230 -20.212 -44.628 1.00 70.18 C ANISOU 2776 CB PHE A1301 8090 11433 7144 133 251 -155 C ATOM 2777 CG PHE A1301 -25.232 -20.512 -45.705 1.00 77.03 C ANISOU 2777 CG PHE A1301 8889 12201 8177 -24 306 -56 C ATOM 2778 CD1 PHE A1301 -24.838 -21.114 -46.888 1.00 75.56 C ANISOU 2778 CD1 PHE A1301 8698 11940 8070 -132 251 -23 C ATOM 2779 CD2 PHE A1301 -26.570 -20.194 -45.534 1.00 80.49 C ANISOU 2779 CD2 PHE A1301 9263 12638 8682 -57 410 0 C ATOM 2780 CE1 PHE A1301 -25.758 -21.393 -47.881 1.00 64.18 C ANISOU 2780 CE1 PHE A1301 7197 10427 6762 -283 282 50 C ATOM 2781 CE2 PHE A1301 -27.494 -20.469 -46.523 1.00 70.05 C ANISOU 2781 CE2 PHE A1301 7853 11258 7506 -208 441 86 C ATOM 2782 CZ PHE A1301 -27.088 -21.069 -47.698 1.00 59.73 C ANISOU 2782 CZ PHE A1301 6549 9879 6266 -328 368 104 C ATOM 2783 N TYR A1302 -22.599 -18.433 -42.592 1.00 68.18 N ANISOU 2783 N TYR A1302 7880 11407 6620 376 73 -484 N ATOM 2784 CA TYR A1302 -21.687 -18.269 -41.466 1.00 63.92 C ANISOU 2784 CA TYR A1302 7399 11013 5876 514 -10 -599 C ATOM 2785 C TYR A1302 -22.309 -17.425 -40.363 1.00 62.16 C ANISOU 2785 C TYR A1302 7229 10838 5551 606 41 -698 C ATOM 2786 O TYR A1302 -21.978 -17.601 -39.185 1.00 60.41 O ANISOU 2786 O TYR A1302 7097 10753 5104 759 30 -742 O ATOM 2787 CB TYR A1302 -20.374 -17.641 -41.933 1.00 53.39 C ANISOU 2787 CB TYR A1302 5981 9717 4590 450 -189 -745 C ATOM 2788 CG TYR A1302 -19.388 -18.630 -42.507 1.00 56.96 C ANISOU 2788 CG TYR A1302 6410 10207 5026 456 -249 -662 C ATOM 2789 CD1 TYR A1302 -18.498 -19.308 -41.683 1.00 56.30 C ANISOU 2789 CD1 TYR A1302 6372 10284 4734 612 -304 -655 C ATOM 2790 CD2 TYR A1302 -19.342 -18.885 -43.870 1.00 65.18 C ANISOU 2790 CD2 TYR A1302 7388 11131 6245 328 -246 -588 C ATOM 2791 CE1 TYR A1302 -17.593 -20.214 -42.202 1.00 50.90 C ANISOU 2791 CE1 TYR A1302 5670 9636 4033 648 -344 -570 C ATOM 2792 CE2 TYR A1302 -18.440 -19.788 -44.398 1.00 56.30 C ANISOU 2792 CE2 TYR A1302 6257 10035 5098 355 -284 -516 C ATOM 2793 CZ TYR A1302 -17.568 -20.449 -43.560 1.00 49.33 C ANISOU 2793 CZ TYR A1302 5419 9305 4020 519 -328 -504 C ATOM 2794 OH TYR A1302 -16.668 -21.348 -44.082 1.00 64.86 O ANISOU 2794 OH TYR A1302 7382 11301 5962 575 -352 -422 O ATOM 2795 N GLY A1303 -23.207 -16.506 -40.721 1.00 53.08 N ANISOU 2795 N GLY A1303 6034 9584 4550 534 101 -732 N ATOM 2796 CA GLY A1303 -23.859 -15.695 -39.708 1.00 53.37 C ANISOU 2796 CA GLY A1303 6136 9651 4491 640 173 -823 C ATOM 2797 C GLY A1303 -24.800 -16.500 -38.832 1.00 54.39 C ANISOU 2797 C GLY A1303 6344 9843 4479 773 348 -674 C ATOM 2798 O GLY A1303 -24.826 -16.324 -37.611 1.00 59.82 O ANISOU 2798 O GLY A1303 7135 10637 4956 931 383 -740 O ATOM 2799 N PHE A1304 -25.579 -17.398 -39.439 1.00 53.52 N ANISOU 2799 N PHE A1304 6189 9671 4476 705 464 -471 N ATOM 2800 CA PHE A1304 -26.532 -18.205 -38.686 1.00 66.65 C ANISOU 2800 CA PHE A1304 7909 11377 6037 800 654 -305 C ATOM 2801 C PHE A1304 -25.863 -19.162 -37.708 1.00 73.21 C ANISOU 2801 C PHE A1304 8873 12320 6622 949 662 -254 C ATOM 2802 O PHE A1304 -26.551 -19.707 -36.838 1.00 77.43 O ANISOU 2802 O PHE A1304 9485 12908 7027 1064 828 -130 O ATOM 2803 CB PHE A1304 -27.430 -18.989 -39.644 1.00 58.84 C ANISOU 2803 CB PHE A1304 6831 10289 5238 650 755 -114 C ATOM 2804 CG PHE A1304 -28.430 -18.138 -40.372 1.00 70.14 C ANISOU 2804 CG PHE A1304 8125 11654 6870 554 795 -114 C ATOM 2805 CD1 PHE A1304 -28.821 -16.911 -39.860 1.00 70.97 C ANISOU 2805 CD1 PHE A1304 8226 11783 6958 650 825 -227 C ATOM 2806 CD2 PHE A1304 -28.982 -18.566 -41.567 1.00 83.63 C ANISOU 2806 CD2 PHE A1304 9718 13281 8776 380 803 -3 C ATOM 2807 CE1 PHE A1304 -29.741 -16.128 -40.528 1.00 71.41 C ANISOU 2807 CE1 PHE A1304 8157 11782 7193 594 871 -209 C ATOM 2808 CE2 PHE A1304 -29.903 -17.788 -42.240 1.00 82.33 C ANISOU 2808 CE2 PHE A1304 9414 13085 8781 312 831 10 C ATOM 2809 CZ PHE A1304 -30.283 -16.567 -41.720 1.00 79.26 C ANISOU 2809 CZ PHE A1304 9016 12722 8378 430 870 -83 C ATOM 2810 N LEU A1305 -24.552 -19.386 -37.829 1.00 55.48 N ANISOU 2810 N LEU A1305 6651 10124 4307 961 497 -330 N ATOM 2811 CA LEU A1305 -23.854 -20.196 -36.836 1.00 67.21 C ANISOU 2811 CA LEU A1305 8259 11746 5533 1141 490 -285 C ATOM 2812 C LEU A1305 -23.801 -19.495 -35.485 1.00 71.31 C ANISOU 2812 C LEU A1305 8865 12419 5810 1322 482 -418 C ATOM 2813 O LEU A1305 -23.864 -20.156 -34.441 1.00 60.71 O ANISOU 2813 O LEU A1305 7644 11190 4233 1505 573 -324 O ATOM 2814 CB LEU A1305 -22.443 -20.526 -37.322 1.00 56.27 C ANISOU 2814 CB LEU A1305 6845 10402 4134 1125 308 -337 C ATOM 2815 CG LEU A1305 -22.351 -21.431 -38.551 1.00 54.63 C ANISOU 2815 CG LEU A1305 6596 10055 4107 992 325 -199 C ATOM 2816 CD1 LEU A1305 -20.905 -21.597 -38.990 1.00 54.22 C ANISOU 2816 CD1 LEU A1305 6503 10067 4033 1002 149 -265 C ATOM 2817 CD2 LEU A1305 -22.985 -22.784 -38.268 1.00 55.34 C ANISOU 2817 CD2 LEU A1305 6800 10087 4139 1052 515 33 C ATOM 2818 N GLY A1306 -23.687 -18.170 -35.482 1.00 59.07 N ANISOU 2818 N GLY A1306 7273 10868 4304 1278 381 -637 N ATOM 2819 CA GLY A1306 -23.730 -17.410 -34.250 1.00 61.22 C ANISOU 2819 CA GLY A1306 7646 11263 4353 1435 377 -793 C ATOM 2820 C GLY A1306 -25.147 -17.218 -33.754 1.00 86.78 C ANISOU 2820 C GLY A1306 10929 14463 7580 1511 605 -705 C ATOM 2821 O GLY A1306 -25.985 -16.650 -34.461 1.00 80.02 O ANISOU 2821 O GLY A1306 9985 13471 6949 1398 680 -691 O ATOM 2822 N LYS A1307 -25.429 -17.691 -32.538 1.00 91.96 N ANISOU 2822 N LYS A1307 11717 15255 7968 1719 725 -632 N ATOM 2823 CA LYS A1307 -26.785 -17.609 -32.007 1.00 89.12 C ANISOU 2823 CA LYS A1307 11393 14882 7585 1810 971 -518 C ATOM 2824 C LYS A1307 -27.219 -16.167 -31.778 1.00 82.60 C ANISOU 2824 C LYS A1307 10578 14025 6780 1836 973 -727 C ATOM 2825 O LYS A1307 -28.413 -15.860 -31.867 1.00 75.54 O ANISOU 2825 O LYS A1307 9640 13064 5997 1845 1159 -641 O ATOM 2826 CB LYS A1307 -26.886 -18.413 -30.712 1.00 92.08 C ANISOU 2826 CB LYS A1307 11923 15421 7644 2045 1103 -393 C ATOM 2827 CG LYS A1307 -26.634 -19.895 -30.909 1.00 97.89 C ANISOU 2827 CG LYS A1307 12673 16150 8370 2038 1157 -148 C ATOM 2828 CD LYS A1307 -26.409 -20.609 -29.592 1.00 95.59 C ANISOU 2828 CD LYS A1307 12556 16037 7727 2298 1242 -47 C ATOM 2829 CE LYS A1307 -26.034 -22.060 -29.831 1.00 98.92 C ANISOU 2829 CE LYS A1307 13014 16424 8146 2301 1289 190 C ATOM 2830 NZ LYS A1307 -25.619 -22.741 -28.577 1.00104.50 N ANISOU 2830 NZ LYS A1307 13900 17316 8490 2579 1345 290 N ATOM 2831 N LYS A1308 -26.274 -15.272 -31.486 1.00 80.51 N ANISOU 2831 N LYS A1308 10372 13804 6416 1849 773 -1001 N ATOM 2832 CA LYS A1308 -26.619 -13.861 -31.361 1.00 67.65 C ANISOU 2832 CA LYS A1308 8776 12097 4831 1855 772 -1218 C ATOM 2833 C LYS A1308 -26.972 -13.263 -32.717 1.00 85.25 C ANISOU 2833 C LYS A1308 10853 14119 7418 1650 760 -1210 C ATOM 2834 O LYS A1308 -27.899 -12.451 -32.821 1.00 65.94 O ANISOU 2834 O LYS A1308 8400 11575 5079 1677 888 -1229 O ATOM 2835 CB LYS A1308 -25.467 -13.094 -30.713 1.00 70.82 C ANISOU 2835 CB LYS A1308 9284 12586 5040 1888 550 -1527 C ATOM 2836 N PHE A1309 -26.248 -13.656 -33.769 1.00 83.12 N ANISOU 2836 N PHE A1309 10466 13790 7326 1465 615 -1172 N ATOM 2837 CA PHE A1309 -26.572 -13.182 -35.111 1.00 69.59 C ANISOU 2837 CA PHE A1309 8610 11896 5934 1280 606 -1140 C ATOM 2838 C PHE A1309 -27.924 -13.712 -35.568 1.00 68.75 C ANISOU 2838 C PHE A1309 8409 11743 5970 1271 814 -888 C ATOM 2839 O PHE A1309 -28.720 -12.973 -36.159 1.00 77.24 O ANISOU 2839 O PHE A1309 9406 12710 7231 1230 888 -875 O ATOM 2840 CB PHE A1309 -25.473 -13.591 -36.092 1.00 73.34 C ANISOU 2840 CB PHE A1309 8990 12341 6535 1104 419 -1142 C ATOM 2841 CG PHE A1309 -25.644 -13.022 -37.476 1.00 73.77 C ANISOU 2841 CG PHE A1309 8914 12222 6891 922 388 -1128 C ATOM 2842 CD1 PHE A1309 -26.463 -13.646 -38.404 1.00 62.96 C ANISOU 2842 CD1 PHE A1309 7432 10789 5700 840 488 -911 C ATOM 2843 CD2 PHE A1309 -24.975 -11.869 -37.851 1.00 83.90 C ANISOU 2843 CD2 PHE A1309 10191 13411 8277 829 258 -1332 C ATOM 2844 CE1 PHE A1309 -26.620 -13.127 -39.673 1.00 63.69 C ANISOU 2844 CE1 PHE A1309 7409 10747 6042 692 453 -893 C ATOM 2845 CE2 PHE A1309 -25.128 -11.345 -39.122 1.00 85.07 C ANISOU 2845 CE2 PHE A1309 10231 13402 8691 680 243 -1299 C ATOM 2846 CZ PHE A1309 -25.951 -11.976 -40.034 1.00 75.39 C ANISOU 2846 CZ PHE A1309 8895 12135 7616 624 337 -1077 C ATOM 2847 N LYS A1310 -28.196 -14.994 -35.309 1.00 74.37 N ANISOU 2847 N LYS A1310 9120 12537 6599 1306 911 -682 N ATOM 2848 CA LYS A1310 -29.500 -15.560 -35.634 1.00 60.49 C ANISOU 2848 CA LYS A1310 7263 10752 4967 1279 1113 -446 C ATOM 2849 C LYS A1310 -30.617 -14.845 -34.886 1.00 62.38 C ANISOU 2849 C LYS A1310 7526 11026 5149 1437 1304 -444 C ATOM 2850 O LYS A1310 -31.752 -14.784 -35.372 1.00 89.34 O ANISOU 2850 O LYS A1310 10807 14404 8733 1397 1445 -303 O ATOM 2851 CB LYS A1310 -29.512 -17.055 -35.309 1.00 60.69 C ANISOU 2851 CB LYS A1310 7324 10845 4890 1294 1198 -241 C ATOM 2852 CG LYS A1310 -30.762 -17.794 -35.759 1.00 90.49 C ANISOU 2852 CG LYS A1310 10978 14581 8823 1205 1388 5 C ATOM 2853 CD LYS A1310 -30.863 -19.160 -35.094 1.00 87.99 C ANISOU 2853 CD LYS A1310 10747 14321 8364 1262 1523 200 C ATOM 2854 CE LYS A1310 -29.619 -19.998 -35.344 1.00 88.75 C ANISOU 2854 CE LYS A1310 10926 14397 8398 1221 1371 192 C ATOM 2855 NZ LYS A1310 -29.703 -21.325 -34.673 1.00 93.21 N ANISOU 2855 NZ LYS A1310 11602 14994 8820 1299 1519 395 N ATOM 2856 N ARG A1311 -30.314 -14.291 -33.710 1.00 88.78 N ANISOU 2856 N ARG A1311 11034 14452 8248 1624 1309 -604 N ATOM 2857 CA ARG A1311 -31.335 -13.610 -32.923 1.00 91.93 C ANISOU 2857 CA ARG A1311 11481 14886 8560 1808 1506 -612 C ATOM 2858 C ARG A1311 -31.679 -12.253 -33.526 1.00 87.59 C ANISOU 2858 C ARG A1311 10883 14201 8197 1780 1489 -748 C ATOM 2859 O ARG A1311 -32.856 -11.931 -33.722 1.00 91.64 O ANISOU 2859 O ARG A1311 11298 14692 8829 1831 1666 -630 O ATOM 2860 CB ARG A1311 -30.861 -13.461 -31.477 1.00 91.23 C ANISOU 2860 CB ARG A1311 11610 14932 8123 2026 1510 -756 C ATOM 2861 CG ARG A1311 -31.952 -13.067 -30.501 1.00101.41 C ANISOU 2861 CG ARG A1311 12973 16292 9266 2254 1759 -718 C ATOM 2862 CD ARG A1311 -31.423 -13.053 -29.078 1.00116.67 C ANISOU 2862 CD ARG A1311 15134 18379 10817 2474 1751 -854 C ATOM 2863 NE ARG A1311 -30.770 -14.311 -28.725 1.00125.30 N ANISOU 2863 NE ARG A1311 16266 19594 11747 2480 1700 -727 N ATOM 2864 CZ ARG A1311 -31.401 -15.366 -28.219 1.00127.32 C ANISOU 2864 CZ ARG A1311 16526 19946 11902 2575 1909 -463 C ATOM 2865 NH1 ARG A1311 -30.724 -16.469 -27.928 1.00117.24 N ANISOU 2865 NH1 ARG A1311 15308 18757 10481 2592 1858 -352 N ATOM 2866 NH2 ARG A1311 -32.708 -15.320 -28.005 1.00134.44 N ANISOU 2866 NH2 ARG A1311 17370 20857 12855 2659 2180 -299 N ATOM 2867 N TYR A1312 -30.661 -11.441 -33.831 1.00 81.48 N ANISOU 2867 N TYR A1312 10171 13334 7454 1702 1283 -986 N ATOM 2868 CA TYR A1312 -30.913 -10.146 -34.454 1.00 80.39 C ANISOU 2868 CA TYR A1312 10008 13032 7505 1670 1272 -1107 C ATOM 2869 C TYR A1312 -31.487 -10.295 -35.856 1.00 76.22 C ANISOU 2869 C TYR A1312 9266 12415 7281 1511 1287 -922 C ATOM 2870 O TYR A1312 -32.256 -9.436 -36.303 1.00 70.98 O ANISOU 2870 O TYR A1312 8543 11657 6768 1550 1378 -906 O ATOM 2871 CB TYR A1312 -29.628 -9.319 -34.507 1.00 70.11 C ANISOU 2871 CB TYR A1312 8814 11639 6186 1584 1049 -1392 C ATOM 2872 CG TYR A1312 -29.169 -8.779 -33.173 1.00 69.88 C ANISOU 2872 CG TYR A1312 9004 11675 5871 1740 1022 -1637 C ATOM 2873 CD1 TYR A1312 -29.788 -7.677 -32.597 1.00 70.66 C ANISOU 2873 CD1 TYR A1312 9236 11694 5916 1898 1149 -1775 C ATOM 2874 CD2 TYR A1312 -28.103 -9.358 -32.498 1.00 77.56 C ANISOU 2874 CD2 TYR A1312 10057 12794 6618 1740 866 -1736 C ATOM 2875 CE1 TYR A1312 -29.366 -7.176 -31.380 1.00 73.18 C ANISOU 2875 CE1 TYR A1312 9777 12072 5956 2037 1116 -2022 C ATOM 2876 CE2 TYR A1312 -27.675 -8.865 -31.281 1.00 84.13 C ANISOU 2876 CE2 TYR A1312 11087 13711 7167 1880 820 -1973 C ATOM 2877 CZ TYR A1312 -28.309 -7.774 -30.727 1.00 75.06 C ANISOU 2877 CZ TYR A1312 10082 12474 5963 2020 943 -2125 C ATOM 2878 OH TYR A1312 -27.884 -7.279 -29.516 1.00 82.22 O ANISOU 2878 OH TYR A1312 11207 13465 6570 2156 890 -2383 O ATOM 2879 N PHE A1313 -31.124 -11.367 -36.564 1.00 71.10 N ANISOU 2879 N PHE A1313 8508 11796 6712 1346 1200 -785 N ATOM 2880 CA PHE A1313 -31.610 -11.558 -37.926 1.00 59.90 C ANISOU 2880 CA PHE A1313 6895 10307 5557 1186 1192 -627 C ATOM 2881 C PHE A1313 -33.116 -11.787 -37.944 1.00 68.44 C ANISOU 2881 C PHE A1313 7842 11452 6711 1253 1405 -414 C ATOM 2882 O PHE A1313 -33.836 -11.193 -38.754 1.00 85.85 O ANISOU 2882 O PHE A1313 9913 13600 9105 1229 1444 -351 O ATOM 2883 CB PHE A1313 -30.878 -12.729 -38.583 1.00 66.77 C ANISOU 2883 CB PHE A1313 7709 11195 6464 1010 1063 -542 C ATOM 2884 CG PHE A1313 -31.155 -12.872 -40.053 1.00 72.56 C ANISOU 2884 CG PHE A1313 8272 11854 7446 831 1011 -427 C ATOM 2885 CD1 PHE A1313 -32.188 -13.677 -40.505 1.00 77.02 C ANISOU 2885 CD1 PHE A1313 8691 12466 8106 767 1119 -210 C ATOM 2886 CD2 PHE A1313 -30.379 -12.202 -40.983 1.00 72.87 C ANISOU 2886 CD2 PHE A1313 8292 11779 7615 720 854 -537 C ATOM 2887 CE1 PHE A1313 -32.442 -13.809 -41.858 1.00 78.71 C ANISOU 2887 CE1 PHE A1313 8752 12631 8523 603 1054 -120 C ATOM 2888 CE2 PHE A1313 -30.628 -12.329 -42.334 1.00 74.46 C ANISOU 2888 CE2 PHE A1313 8349 11927 8016 575 808 -429 C ATOM 2889 CZ PHE A1313 -31.661 -13.134 -42.773 1.00 75.65 C ANISOU 2889 CZ PHE A1313 8363 12140 8242 520 899 -227 C ATOM 2890 N LEU A1314 -33.611 -12.650 -37.055 1.00 66.57 N ANISOU 2890 N LEU A1314 7627 11344 6324 1341 1551 -289 N ATOM 2891 CA LEU A1314 -35.037 -12.947 -37.025 1.00 74.99 C ANISOU 2891 CA LEU A1314 8537 12491 7462 1387 1765 -73 C ATOM 2892 C LEU A1314 -35.855 -11.808 -36.430 1.00 82.18 C ANISOU 2892 C LEU A1314 9472 13415 8337 1609 1927 -122 C ATOM 2893 O LEU A1314 -37.051 -11.707 -36.720 1.00 78.36 O ANISOU 2893 O LEU A1314 8809 12986 7979 1644 2079 43 O ATOM 2894 CB LEU A1314 -35.286 -14.241 -36.250 1.00 71.66 C ANISOU 2894 CB LEU A1314 8140 12189 6900 1405 1893 90 C ATOM 2895 CG LEU A1314 -34.630 -15.484 -36.856 1.00 65.96 C ANISOU 2895 CG LEU A1314 7399 11437 6224 1199 1772 171 C ATOM 2896 CD1 LEU A1314 -35.038 -16.735 -36.097 1.00 71.10 C ANISOU 2896 CD1 LEU A1314 8079 12178 6757 1223 1941 361 C ATOM 2897 CD2 LEU A1314 -34.972 -15.609 -38.334 1.00 60.40 C ANISOU 2897 CD2 LEU A1314 6494 10664 5790 979 1688 253 C ATOM 2898 N GLN A1315 -35.243 -10.952 -35.607 1.00 90.36 N ANISOU 2898 N GLN A1315 10722 14408 9203 1762 1898 -347 N ATOM 2899 CA GLN A1315 -35.946 -9.763 -35.139 1.00 92.55 C ANISOU 2899 CA GLN A1315 11054 14655 9455 1978 2045 -422 C ATOM 2900 C GLN A1315 -36.146 -8.758 -36.266 1.00101.59 C ANISOU 2900 C GLN A1315 12101 15653 10845 1924 1988 -452 C ATOM 2901 O GLN A1315 -37.132 -8.012 -36.262 1.00115.68 O ANISOU 2901 O GLN A1315 13826 17432 12696 2084 2151 -395 O ATOM 2902 CB GLN A1315 -35.188 -9.116 -33.979 1.00 93.05 C ANISOU 2902 CB GLN A1315 11398 14696 9262 2137 2014 -686 C ATOM 2903 CG GLN A1315 -35.196 -9.929 -32.695 1.00106.95 C ANISOU 2903 CG GLN A1315 13275 16627 10735 2273 2119 -644 C ATOM 2904 CD GLN A1315 -34.530 -9.201 -31.542 1.00120.32 C ANISOU 2904 CD GLN A1315 15246 18318 12151 2447 2082 -921 C ATOM 2905 OE1 GLN A1315 -34.095 -8.058 -31.684 1.00124.98 O ANISOU 2905 OE1 GLN A1315 15946 18761 12779 2452 1987 -1156 O ATOM 2906 NE2 GLN A1315 -34.448 -9.862 -30.393 1.00118.38 N ANISOU 2906 NE2 GLN A1315 15124 18236 11620 2587 2159 -897 N ATOM 2907 N LEU A1316 -35.226 -8.724 -37.233 1.00 93.56 N ANISOU 2907 N LEU A1316 11067 14522 9959 1720 1770 -527 N ATOM 2908 CA LEU A1316 -35.398 -7.852 -38.390 1.00 85.21 C ANISOU 2908 CA LEU A1316 9914 13329 9134 1664 1719 -523 C ATOM 2909 C LEU A1316 -36.529 -8.340 -39.285 1.00 94.83 C ANISOU 2909 C LEU A1316 10856 14643 10532 1609 1798 -256 C ATOM 2910 O LEU A1316 -37.262 -7.532 -39.867 1.00 98.57 O ANISOU 2910 O LEU A1316 11229 15076 11149 1691 1867 -191 O ATOM 2911 CB LEU A1316 -34.092 -7.765 -39.180 1.00 71.91 C ANISOU 2911 CB LEU A1316 8277 11516 7530 1456 1479 -656 C ATOM 2912 CG LEU A1316 -33.324 -6.444 -39.131 1.00 80.66 C ANISOU 2912 CG LEU A1316 9566 12428 8654 1484 1403 -905 C ATOM 2913 CD1 LEU A1316 -32.062 -6.532 -39.974 1.00 77.57 C ANISOU 2913 CD1 LEU A1316 9171 11944 8356 1255 1178 -992 C ATOM 2914 CD2 LEU A1316 -34.204 -5.296 -39.599 1.00 83.73 C ANISOU 2914 CD2 LEU A1316 9922 12697 9195 1615 1531 -862 C ATOM 2915 N LEU A1317 -36.686 -9.659 -39.409 1.00 92.31 N ANISOU 2915 N LEU A1317 10414 14452 10206 1470 1788 -99 N ATOM 2916 CA LEU A1317 -37.728 -10.212 -40.266 1.00 92.97 C ANISOU 2916 CA LEU A1317 10226 14639 10458 1376 1840 137 C ATOM 2917 C LEU A1317 -39.084 -10.246 -39.573 1.00109.03 C ANISOU 2917 C LEU A1317 12138 16828 12462 1548 2087 297 C ATOM 2918 O LEU A1317 -40.119 -10.228 -40.249 1.00124.06 O ANISOU 2918 O LEU A1317 13796 18823 14519 1533 2151 471 O ATOM 2919 CB LEU A1317 -37.341 -11.620 -40.728 1.00 81.83 C ANISOU 2919 CB LEU A1317 8749 13276 9068 1134 1733 228 C ATOM 2920 CG LEU A1317 -36.487 -11.756 -41.994 1.00 76.54 C ANISOU 2920 CG LEU A1317 8057 12503 8523 924 1509 180 C ATOM 2921 CD1 LEU A1317 -35.132 -11.080 -41.843 1.00 80.60 C ANISOU 2921 CD1 LEU A1317 8785 12874 8967 940 1368 -49 C ATOM 2922 CD2 LEU A1317 -36.314 -13.223 -42.363 1.00 80.57 C ANISOU 2922 CD2 LEU A1317 8508 13063 9043 715 1448 287 C ATOM 2923 N LYS A1318 -39.102 -10.293 -38.245 1.00112.94 N ANISOU 2923 N LYS A1318 12788 17372 12752 1718 2228 246 N ATOM 2924 CA LYS A1318 -40.354 -10.323 -37.498 1.00104.97 C ANISOU 2924 CA LYS A1318 11671 16517 11694 1903 2489 402 C ATOM 2925 C LYS A1318 -41.051 -8.967 -37.546 1.00101.28 C ANISOU 2925 C LYS A1318 11179 16018 11287 2137 2605 377 C ATOM 2926 O LYS A1318 -40.425 -7.929 -37.335 1.00101.17 O ANISOU 2926 O LYS A1318 11381 15843 11214 2255 2555 166 O ATOM 2927 CB LYS A1318 -40.104 -10.733 -36.045 1.00 98.25 C ANISOU 2927 CB LYS A1318 11025 15728 10578 2041 2612 351 C TER 2928 LYS A1318 ATOM 2929 N GLN D 1 -24.587 -12.518 -20.047 1.00121.21 N ANISOU 2929 N GLN D 1 12117 17552 16384 1778 -1321 -5061 N ATOM 2930 CA GLN D 1 -23.159 -12.247 -19.930 1.00121.82 C ANISOU 2930 CA GLN D 1 12862 17270 16155 1751 -1274 -4447 C ATOM 2931 C GLN D 1 -22.511 -13.127 -18.867 1.00118.76 C ANISOU 2931 C GLN D 1 12505 17503 15115 1168 -606 -4023 C ATOM 2932 O GLN D 1 -23.179 -13.609 -17.952 1.00135.26 O ANISOU 2932 O GLN D 1 14046 20389 16957 781 -173 -4365 O ATOM 2933 CB GLN D 1 -22.918 -10.771 -19.606 1.00133.85 C ANISOU 2933 CB GLN D 1 14313 18577 17966 2212 -1639 -5003 C ATOM 2934 CG GLN D 1 -23.321 -9.818 -20.718 1.00150.11 C ANISOU 2934 CG GLN D 1 16602 19801 20632 2780 -2481 -5294 C ATOM 2935 CD GLN D 1 -22.503 -10.018 -21.979 1.00159.97 C ANISOU 2935 CD GLN D 1 18776 20206 21801 2734 -2782 -4429 C ATOM 2936 OE1 GLN D 1 -23.037 -10.374 -23.029 1.00168.46 O ANISOU 2936 OE1 GLN D 1 20048 20864 23095 2813 -3114 -4281 O ATOM 2937 NE2 GLN D 1 -21.199 -9.786 -21.881 1.00159.26 N ANISOU 2937 NE2 GLN D 1 19233 19900 21380 2579 -2658 -3894 N ATOM 2938 N VAL D 2 -21.205 -13.333 -18.997 1.00101.33 N ANISOU 2938 N VAL D 2 10954 14934 12614 1073 -558 -3304 N ATOM 2939 CA VAL D 2 -20.418 -14.100 -18.039 1.00 95.55 C ANISOU 2939 CA VAL D 2 10379 14626 11301 596 -87 -2869 C ATOM 2940 C VAL D 2 -19.450 -13.122 -17.385 1.00 95.33 C ANISOU 2940 C VAL D 2 10468 14558 11196 765 -92 -2968 C ATOM 2941 O VAL D 2 -18.391 -12.809 -17.940 1.00102.83 O ANISOU 2941 O VAL D 2 11936 14956 12178 937 -301 -2553 O ATOM 2942 CB VAL D 2 -19.680 -15.268 -18.702 1.00 88.63 C ANISOU 2942 CB VAL D 2 10111 13385 10178 376 -76 -2022 C ATOM 2943 CG1 VAL D 2 -18.931 -16.083 -17.658 1.00 83.30 C ANISOU 2943 CG1 VAL D 2 9618 13094 8939 -89 274 -1632 C ATOM 2944 CG2 VAL D 2 -20.658 -16.145 -19.470 1.00 91.26 C ANISOU 2944 CG2 VAL D 2 10372 13661 10641 259 -155 -1934 C ATOM 2945 N GLN D 3 -19.813 -12.634 -16.203 1.00 91.82 N ANISOU 2945 N GLN D 3 9522 14738 10629 678 151 -3555 N ATOM 2946 CA GLN D 3 -18.990 -11.670 -15.489 1.00102.27 C ANISOU 2946 CA GLN D 3 10910 16062 11887 839 133 -3724 C ATOM 2947 C GLN D 3 -17.899 -12.374 -14.691 1.00 90.14 C ANISOU 2947 C GLN D 3 9728 14739 9783 415 467 -3149 C ATOM 2948 O GLN D 3 -18.055 -13.519 -14.257 1.00 88.92 O ANISOU 2948 O GLN D 3 9606 14965 9217 -78 770 -2846 O ATOM 2949 CB GLN D 3 -19.854 -10.820 -14.557 1.00115.38 C ANISOU 2949 CB GLN D 3 11860 18316 13664 965 222 -4688 C ATOM 2950 CG GLN D 3 -20.889 -9.968 -15.275 1.00120.99 C ANISOU 2950 CG GLN D 3 12186 18758 15027 1506 -255 -5404 C ATOM 2951 CD GLN D 3 -21.899 -9.355 -14.325 1.00139.14 C ANISOU 2951 CD GLN D 3 13622 21802 17443 1609 -117 -6498 C ATOM 2952 OE1 GLN D 3 -22.488 -10.047 -13.495 1.00145.63 O ANISOU 2952 OE1 GLN D 3 13958 23495 17878 1112 434 -6748 O ATOM 2953 NE2 GLN D 3 -22.102 -8.047 -14.441 1.00146.83 N ANISOU 2953 NE2 GLN D 3 14413 22446 18929 2223 -644 -7191 N ATOM 2954 N LEU D 4 -16.784 -11.671 -14.500 1.00 76.78 N ANISOU 2954 N LEU D 4 8334 12762 8076 594 344 -3009 N ATOM 2955 CA LEU D 4 -15.642 -12.190 -13.757 1.00 78.20 C ANISOU 2955 CA LEU D 4 8849 13067 7798 288 550 -2532 C ATOM 2956 C LEU D 4 -15.246 -11.179 -12.693 1.00 92.80 C ANISOU 2956 C LEU D 4 10529 15176 9554 368 605 -2947 C ATOM 2957 O LEU D 4 -14.865 -10.050 -13.017 1.00 76.36 O ANISOU 2957 O LEU D 4 8510 12706 7799 755 308 -3153 O ATOM 2958 CB LEU D 4 -14.459 -12.480 -14.686 1.00 69.59 C ANISOU 2958 CB LEU D 4 8316 11352 6772 401 338 -1892 C ATOM 2959 CG LEU D 4 -14.658 -13.544 -15.766 1.00 72.01 C ANISOU 2959 CG LEU D 4 8861 11364 7135 336 264 -1447 C ATOM 2960 CD1 LEU D 4 -13.363 -13.777 -16.529 1.00 63.16 C ANISOU 2960 CD1 LEU D 4 8211 9764 6022 428 114 -947 C ATOM 2961 CD2 LEU D 4 -15.166 -14.842 -15.159 1.00 68.86 C ANISOU 2961 CD2 LEU D 4 8415 11394 6357 -117 507 -1253 C ATOM 2962 N GLN D 5 -15.337 -11.584 -11.430 1.00102.26 N ANISOU 2962 N GLN D 5 11570 17013 10273 -43 950 -3057 N ATOM 2963 CA GLN D 5 -14.937 -10.756 -10.299 1.00108.98 C ANISOU 2963 CA GLN D 5 12286 18178 10942 -34 1041 -3434 C ATOM 2964 C GLN D 5 -13.612 -11.273 -9.757 1.00100.76 C ANISOU 2964 C GLN D 5 11740 17033 9510 -281 1065 -2836 C ATOM 2965 O GLN D 5 -13.503 -12.451 -9.399 1.00103.32 O ANISOU 2965 O GLN D 5 12303 17545 9408 -735 1209 -2405 O ATOM 2966 CB GLN D 5 -16.006 -10.761 -9.206 1.00121.26 C ANISOU 2966 CB GLN D 5 13292 20597 12185 -365 1417 -4085 C ATOM 2967 CG GLN D 5 -17.159 -9.798 -9.453 1.00140.70 C ANISOU 2967 CG GLN D 5 15113 23224 15124 45 1316 -4987 C ATOM 2968 CD GLN D 5 -16.744 -8.344 -9.325 1.00152.44 C ANISOU 2968 CD GLN D 5 16539 24411 16971 593 980 -5459 C ATOM 2969 OE1 GLN D 5 -15.657 -8.035 -8.834 1.00154.53 O ANISOU 2969 OE1 GLN D 5 17156 24515 17044 575 939 -5178 O ATOM 2970 NE2 GLN D 5 -17.612 -7.441 -9.765 1.00158.38 N ANISOU 2970 NE2 GLN D 5 16859 25050 18267 1090 670 -6202 N ATOM 2971 N GLU D 6 -12.614 -10.398 -9.700 1.00 77.88 N ANISOU 2971 N GLU D 6 9014 13809 6766 7 860 -2829 N ATOM 2972 CA GLU D 6 -11.287 -10.753 -9.226 1.00 88.62 C ANISOU 2972 CA GLU D 6 10779 15042 7849 -143 815 -2358 C ATOM 2973 C GLU D 6 -10.977 -10.035 -7.919 1.00 97.23 C ANISOU 2973 C GLU D 6 11764 16501 8677 -220 905 -2716 C ATOM 2974 O GLU D 6 -11.438 -8.916 -7.678 1.00 96.24 O ANISOU 2974 O GLU D 6 11311 16501 8754 31 882 -3318 O ATOM 2975 CB GLU D 6 -10.224 -10.422 -10.277 1.00 81.41 C ANISOU 2975 CB GLU D 6 10160 13479 7294 173 521 -2021 C ATOM 2976 CG GLU D 6 -10.539 -9.193 -11.104 1.00 91.11 C ANISOU 2976 CG GLU D 6 11269 14347 9002 562 289 -2362 C ATOM 2977 CD GLU D 6 -9.874 -9.230 -12.463 1.00 90.95 C ANISOU 2977 CD GLU D 6 11569 13744 9246 693 67 -1960 C ATOM 2978 OE1 GLU D 6 -8.925 -10.022 -12.640 1.00 91.34 O ANISOU 2978 OE1 GLU D 6 11857 13706 9142 554 106 -1511 O ATOM 2979 OE2 GLU D 6 -10.307 -8.477 -13.356 1.00 92.22 O ANISOU 2979 OE2 GLU D 6 11749 13538 9753 920 -178 -2132 O ATOM 2980 N SER D 7 -10.192 -10.699 -7.075 1.00 94.37 N ANISOU 2980 N SER D 7 11710 16278 7871 -551 943 -2366 N ATOM 2981 CA SER D 7 -9.850 -10.173 -5.762 1.00 98.44 C ANISOU 2981 CA SER D 7 12204 17155 8043 -701 1023 -2641 C ATOM 2982 C SER D 7 -8.535 -10.793 -5.317 1.00 90.61 C ANISOU 2982 C SER D 7 11689 15947 6792 -862 827 -2111 C ATOM 2983 O SER D 7 -8.135 -11.857 -5.797 1.00 89.24 O ANISOU 2983 O SER D 7 11823 15501 6585 -964 683 -1595 O ATOM 2984 CB SER D 7 -10.957 -10.457 -4.741 1.00118.74 C ANISOU 2984 CB SER D 7 14517 20489 10111 -1175 1392 -3032 C ATOM 2985 OG SER D 7 -11.259 -11.841 -4.692 1.00124.21 O ANISOU 2985 OG SER D 7 15471 21326 10398 -1694 1491 -2573 O ATOM 2986 N GLY D 8 -7.868 -10.111 -4.391 1.00 90.98 N ANISOU 2986 N GLY D 8 11782 16100 6685 -848 769 -2295 N ATOM 2987 CA GLY D 8 -6.593 -10.565 -3.863 1.00 83.55 C ANISOU 2987 CA GLY D 8 11250 14958 5538 -954 516 -1897 C ATOM 2988 C GLY D 8 -5.421 -9.645 -4.138 1.00 79.35 C ANISOU 2988 C GLY D 8 10716 14037 5396 -559 271 -1932 C ATOM 2989 O GLY D 8 -4.319 -9.917 -3.640 1.00103.40 O ANISOU 2989 O GLY D 8 14024 16946 8316 -607 35 -1700 O ATOM 2990 N GLY D 9 -5.590 -8.571 -4.904 1.00 77.73 N ANISOU 2990 N GLY D 9 10256 13628 5651 -203 262 -2216 N ATOM 2991 CA GLY D 9 -4.486 -7.672 -5.162 1.00 76.11 C ANISOU 2991 CA GLY D 9 10091 13073 5756 49 27 -2232 C ATOM 2992 C GLY D 9 -4.079 -6.885 -3.931 1.00 83.46 C ANISOU 2992 C GLY D 9 11020 14211 6479 17 -27 -2534 C ATOM 2993 O GLY D 9 -4.816 -6.770 -2.951 1.00 82.57 O ANISOU 2993 O GLY D 9 10808 14541 6023 -146 152 -2861 O ATOM 2994 N GLY D 10 -2.870 -6.333 -3.989 1.00 77.93 N ANISOU 2994 N GLY D 10 10414 13224 5970 140 -265 -2454 N ATOM 2995 CA GLY D 10 -2.347 -5.560 -2.881 1.00 80.51 C ANISOU 2995 CA GLY D 10 10771 13680 6139 129 -374 -2712 C ATOM 2996 C GLY D 10 -0.869 -5.252 -3.000 1.00 82.88 C ANISOU 2996 C GLY D 10 11180 13675 6638 193 -647 -2533 C ATOM 2997 O GLY D 10 -0.145 -5.921 -3.743 1.00 79.26 O ANISOU 2997 O GLY D 10 10769 13004 6342 193 -729 -2201 O ATOM 2998 N LEU D 11 -0.411 -4.238 -2.269 1.00 88.33 N ANISOU 2998 N LEU D 11 11869 14373 7321 244 -792 -2809 N ATOM 2999 CA LEU D 11 0.990 -3.831 -2.283 1.00 80.97 C ANISOU 2999 CA LEU D 11 10991 13203 6570 261 -1052 -2709 C ATOM 3000 C LEU D 11 1.747 -4.655 -1.247 1.00 82.53 C ANISOU 3000 C LEU D 11 11351 13557 6448 123 -1188 -2548 C ATOM 3001 O LEU D 11 1.502 -4.533 -0.043 1.00117.78 O ANISOU 3001 O LEU D 11 15932 18277 10542 19 -1195 -2725 O ATOM 3002 CB LEU D 11 1.114 -2.334 -2.008 1.00 82.79 C ANISOU 3002 CB LEU D 11 11191 13309 6957 367 -1216 -3072 C ATOM 3003 CG LEU D 11 2.509 -1.743 -1.785 1.00 84.78 C ANISOU 3003 CG LEU D 11 11489 13382 7342 318 -1489 -3045 C ATOM 3004 CD1 LEU D 11 3.497 -2.225 -2.834 1.00 88.79 C ANISOU 3004 CD1 LEU D 11 11931 13703 8102 226 -1521 -2729 C ATOM 3005 CD2 LEU D 11 2.430 -0.226 -1.793 1.00 85.31 C ANISOU 3005 CD2 LEU D 11 11583 13224 7608 406 -1695 -3374 C ATOM 3006 N VAL D 12 2.668 -5.492 -1.719 1.00 81.19 N ANISOU 3006 N VAL D 12 11201 13231 6417 122 -1340 -2256 N ATOM 3007 CA VAL D 12 3.456 -6.371 -0.866 1.00 83.14 C ANISOU 3007 CA VAL D 12 11641 13509 6440 48 -1623 -2104 C ATOM 3008 C VAL D 12 4.932 -6.118 -1.143 1.00 95.14 C ANISOU 3008 C VAL D 12 12997 14840 8311 158 -1900 -2141 C ATOM 3009 O VAL D 12 5.315 -5.701 -2.241 1.00102.41 O ANISOU 3009 O VAL D 12 13671 15640 9600 212 -1807 -2172 O ATOM 3010 CB VAL D 12 3.093 -7.858 -1.093 1.00 87.09 C ANISOU 3010 CB VAL D 12 12317 13999 6773 -28 -1652 -1788 C ATOM 3011 CG1 VAL D 12 3.494 -8.300 -2.492 1.00 94.83 C ANISOU 3011 CG1 VAL D 12 13084 14768 8179 140 -1638 -1661 C ATOM 3012 CG2 VAL D 12 3.729 -8.748 -0.035 1.00 86.01 C ANISOU 3012 CG2 VAL D 12 12525 13831 6324 -140 -2073 -1637 C ATOM 3013 N ALA D 13 5.762 -6.357 -0.131 1.00111.68 N ANISOU 3013 N ALA D 13 15235 16935 10262 143 -2253 -2164 N ATOM 3014 CA ALA D 13 7.198 -6.190 -0.278 1.00118.33 C ANISOU 3014 CA ALA D 13 15857 17656 11447 248 -2553 -2277 C ATOM 3015 C ALA D 13 7.761 -7.226 -1.251 1.00 86.16 C ANISOU 3015 C ALA D 13 11583 13483 7669 381 -2655 -2186 C ATOM 3016 O ALA D 13 7.101 -8.202 -1.620 1.00 85.02 O ANISOU 3016 O ALA D 13 11577 13305 7423 401 -2596 -1978 O ATOM 3017 CB ALA D 13 7.892 -6.302 1.079 1.00 90.71 C ANISOU 3017 CB ALA D 13 12589 14149 7728 232 -2988 -2340 C ATOM 3018 N ALA D 14 9.004 -7.001 -1.667 1.00 90.54 N ANISOU 3018 N ALA D 14 11779 14025 8597 457 -2814 -2397 N ATOM 3019 CA ALA D 14 9.661 -7.914 -2.591 1.00 87.43 C ANISOU 3019 CA ALA D 14 11086 13614 8520 611 -2913 -2463 C ATOM 3020 C ALA D 14 9.910 -9.261 -1.926 1.00 89.99 C ANISOU 3020 C ALA D 14 11653 13781 8758 814 -3447 -2390 C ATOM 3021 O ALA D 14 10.320 -9.335 -0.765 1.00129.03 O ANISOU 3021 O ALA D 14 16841 18638 13545 838 -3881 -2416 O ATOM 3022 CB ALA D 14 10.979 -7.318 -3.084 1.00 89.29 C ANISOU 3022 CB ALA D 14 10807 13979 9141 584 -2945 -2814 C ATOM 3023 N GLY D 15 9.656 -10.333 -2.674 1.00 89.22 N ANISOU 3023 N GLY D 15 11548 13600 8751 949 -3478 -2292 N ATOM 3024 CA GLY D 15 9.812 -11.678 -2.166 1.00 92.08 C ANISOU 3024 CA GLY D 15 12230 13718 9040 1135 -4079 -2197 C ATOM 3025 C GLY D 15 8.616 -12.226 -1.419 1.00 91.93 C ANISOU 3025 C GLY D 15 12870 13582 8476 913 -4123 -1773 C ATOM 3026 O GLY D 15 8.646 -13.394 -1.010 1.00 94.78 O ANISOU 3026 O GLY D 15 13633 13677 8702 974 -4678 -1615 O ATOM 3027 N GLY D 16 7.569 -11.430 -1.231 1.00 89.44 N ANISOU 3027 N GLY D 16 12681 13463 7840 631 -3595 -1623 N ATOM 3028 CA GLY D 16 6.394 -11.878 -0.519 1.00 91.79 C ANISOU 3028 CA GLY D 16 13509 13788 7579 331 -3535 -1308 C ATOM 3029 C GLY D 16 5.560 -12.844 -1.345 1.00 88.30 C ANISOU 3029 C GLY D 16 13171 13271 7109 305 -3404 -1063 C ATOM 3030 O GLY D 16 5.972 -13.361 -2.384 1.00 87.08 O ANISOU 3030 O GLY D 16 12752 12982 7354 568 -3478 -1125 O ATOM 3031 N SER D 17 4.346 -13.084 -0.855 1.00 92.73 N ANISOU 3031 N SER D 17 14105 13966 7162 -53 -3190 -820 N ATOM 3032 CA SER D 17 3.421 -14.012 -1.485 1.00 87.58 C ANISOU 3032 CA SER D 17 13614 13262 6402 -168 -3074 -558 C ATOM 3033 C SER D 17 2.038 -13.384 -1.577 1.00 85.61 C ANISOU 3033 C SER D 17 13262 13365 5899 -439 -2416 -562 C ATOM 3034 O SER D 17 1.714 -12.432 -0.863 1.00 86.36 O ANISOU 3034 O SER D 17 13300 13742 5772 -594 -2150 -748 O ATOM 3035 CB SER D 17 3.343 -15.339 -0.718 1.00 92.02 C ANISOU 3035 CB SER D 17 14846 13582 6535 -424 -3669 -231 C ATOM 3036 OG SER D 17 4.613 -15.963 -0.648 1.00 94.62 O ANISOU 3036 OG SER D 17 15266 13520 7166 -90 -4407 -301 O ATOM 3037 N LEU D 18 1.219 -13.938 -2.469 1.00104.19 N ANISOU 3037 N LEU D 18 15570 15701 8318 -463 -2193 -410 N ATOM 3038 CA LEU D 18 -0.143 -13.462 -2.667 1.00 82.15 C ANISOU 3038 CA LEU D 18 12625 13229 5358 -673 -1630 -469 C ATOM 3039 C LEU D 18 -0.953 -14.557 -3.343 1.00 81.55 C ANISOU 3039 C LEU D 18 12700 13068 5217 -804 -1602 -192 C ATOM 3040 O LEU D 18 -0.401 -15.481 -3.947 1.00 81.12 O ANISOU 3040 O LEU D 18 12769 12670 5381 -616 -1966 -7 O ATOM 3041 CB LEU D 18 -0.176 -12.173 -3.496 1.00 78.63 C ANISOU 3041 CB LEU D 18 11676 12840 5358 -380 -1255 -774 C ATOM 3042 CG LEU D 18 -0.445 -10.881 -2.725 1.00 92.56 C ANISOU 3042 CG LEU D 18 13294 14884 6992 -442 -1023 -1107 C ATOM 3043 CD1 LEU D 18 -0.429 -9.675 -3.652 1.00 96.32 C ANISOU 3043 CD1 LEU D 18 13391 15272 7933 -162 -814 -1359 C ATOM 3044 CD2 LEU D 18 -1.773 -10.984 -2.004 1.00 82.37 C ANISOU 3044 CD2 LEU D 18 12089 13996 5211 -808 -727 -1187 C ATOM 3045 N ARG D 19 -2.275 -14.441 -3.232 1.00 82.03 N ANISOU 3045 N ARG D 19 12714 13464 4991 -1118 -1184 -225 N ATOM 3046 CA ARG D 19 -3.197 -15.414 -3.813 1.00 81.87 C ANISOU 3046 CA ARG D 19 12818 13420 4868 -1319 -1113 21 C ATOM 3047 C ARG D 19 -4.358 -14.659 -4.443 1.00 82.69 C ANISOU 3047 C ARG D 19 12472 13810 5136 -1279 -567 -247 C ATOM 3048 O ARG D 19 -5.220 -14.136 -3.730 1.00 97.74 O ANISOU 3048 O ARG D 19 14246 16170 6722 -1567 -234 -506 O ATOM 3049 CB ARG D 19 -3.697 -16.402 -2.759 1.00 86.97 C ANISOU 3049 CB ARG D 19 14014 14212 4819 -1949 -1294 302 C ATOM 3050 CG ARG D 19 -4.598 -17.495 -3.307 1.00108.42 C ANISOU 3050 CG ARG D 19 16925 16875 7393 -2235 -1289 598 C ATOM 3051 CD ARG D 19 -5.084 -18.413 -2.199 1.00110.61 C ANISOU 3051 CD ARG D 19 17760 17260 7007 -2950 -1458 883 C ATOM 3052 NE ARG D 19 -5.874 -19.527 -2.717 1.00117.18 N ANISOU 3052 NE ARG D 19 18746 17915 7860 -3193 -1496 1176 N ATOM 3053 CZ ARG D 19 -5.369 -20.712 -3.043 1.00121.00 C ANISOU 3053 CZ ARG D 19 19646 17811 8516 -3093 -2084 1532 C ATOM 3054 NH1 ARG D 19 -4.070 -20.942 -2.904 1.00125.96 N ANISOU 3054 NH1 ARG D 19 20531 17990 9337 -2724 -2690 1599 N ATOM 3055 NH2 ARG D 19 -6.161 -21.668 -3.509 1.00116.16 N ANISOU 3055 NH2 ARG D 19 19157 17056 7923 -3341 -2095 1763 N ATOM 3056 N LEU D 20 -4.381 -14.602 -5.771 1.00 77.12 N ANISOU 3056 N LEU D 20 11528 12850 4923 -923 -507 -237 N ATOM 3057 CA LEU D 20 -5.463 -13.958 -6.500 1.00 74.24 C ANISOU 3057 CA LEU D 20 10796 12638 4776 -835 -125 -476 C ATOM 3058 C LEU D 20 -6.589 -14.953 -6.744 1.00 75.35 C ANISOU 3058 C LEU D 20 11031 12897 4703 -1148 -17 -288 C ATOM 3059 O LEU D 20 -6.345 -16.136 -6.993 1.00 75.46 O ANISOU 3059 O LEU D 20 11381 12659 4632 -1249 -294 91 O ATOM 3060 CB LEU D 20 -4.962 -13.401 -7.834 1.00 70.18 C ANISOU 3060 CB LEU D 20 10067 11770 4829 -388 -150 -526 C ATOM 3061 CG LEU D 20 -3.717 -12.513 -7.789 1.00 84.54 C ANISOU 3061 CG LEU D 20 11803 13439 6877 -143 -283 -666 C ATOM 3062 CD1 LEU D 20 -3.325 -12.070 -9.190 1.00 66.19 C ANISOU 3062 CD1 LEU D 20 9326 10820 5002 127 -271 -684 C ATOM 3063 CD2 LEU D 20 -3.941 -11.312 -6.885 1.00 71.09 C ANISOU 3063 CD2 LEU D 20 9951 11993 5066 -178 -146 -1022 C ATOM 3064 N SER D 21 -7.824 -14.466 -6.669 1.00 81.70 N ANISOU 3064 N SER D 21 11521 14082 5440 -1292 347 -604 N ATOM 3065 CA SER D 21 -9.004 -15.284 -6.899 1.00 84.44 C ANISOU 3065 CA SER D 21 11857 14628 5597 -1633 507 -511 C ATOM 3066 C SER D 21 -9.855 -14.665 -7.998 1.00 79.32 C ANISOU 3066 C SER D 21 10777 13935 5427 -1303 696 -802 C ATOM 3067 O SER D 21 -9.805 -13.454 -8.237 1.00 79.10 O ANISOU 3067 O SER D 21 10449 13864 5741 -933 749 -1180 O ATOM 3068 CB SER D 21 -9.836 -15.439 -5.619 1.00 84.00 C ANISOU 3068 CB SER D 21 11797 15213 4905 -2265 776 -694 C ATOM 3069 N CYS D 22 -10.635 -15.510 -8.670 1.00 75.93 N ANISOU 3069 N CYS D 22 10370 13463 5017 -1449 724 -616 N ATOM 3070 CA CYS D 22 -11.521 -15.044 -9.735 1.00 74.37 C ANISOU 3070 CA CYS D 22 9809 13187 5262 -1159 832 -875 C ATOM 3071 C CYS D 22 -12.630 -16.071 -9.913 1.00 76.47 C ANISOU 3071 C CYS D 22 10062 13664 5330 -1557 948 -750 C ATOM 3072 O CYS D 22 -12.390 -17.148 -10.466 1.00 74.94 O ANISOU 3072 O CYS D 22 10225 13139 5109 -1638 737 -272 O ATOM 3073 CB CYS D 22 -10.754 -14.837 -11.035 1.00 82.29 C ANISOU 3073 CB CYS D 22 10933 13578 6755 -670 587 -672 C ATOM 3074 SG CYS D 22 -11.812 -14.446 -12.448 1.00 91.67 S ANISOU 3074 SG CYS D 22 11855 14542 8435 -371 590 -875 S ATOM 3075 N ALA D 23 -13.831 -15.735 -9.454 1.00 92.97 N ANISOU 3075 N ALA D 23 11711 16318 7294 -1803 1264 -1229 N ATOM 3076 CA ALA D 23 -14.994 -16.598 -9.594 1.00 86.83 C ANISOU 3076 CA ALA D 23 10817 15846 6329 -2247 1425 -1209 C ATOM 3077 C ALA D 23 -15.847 -16.131 -10.766 1.00 95.22 C ANISOU 3077 C ALA D 23 11464 16740 7977 -1814 1409 -1531 C ATOM 3078 O ALA D 23 -16.015 -14.928 -10.986 1.00 81.58 O ANISOU 3078 O ALA D 23 9361 14982 6655 -1346 1395 -2047 O ATOM 3079 CB ALA D 23 -15.828 -16.606 -8.312 1.00 90.19 C ANISOU 3079 CB ALA D 23 10959 17126 6184 -2904 1823 -1609 C ATOM 3080 N ALA D 24 -16.381 -17.090 -11.517 1.00100.36 N ANISOU 3080 N ALA D 24 12234 17227 8673 -1973 1336 -1225 N ATOM 3081 CA ALA D 24 -17.226 -16.795 -12.666 1.00 97.40 C ANISOU 3081 CA ALA D 24 11531 16649 8828 -1606 1259 -1479 C ATOM 3082 C ALA D 24 -18.688 -16.824 -12.237 1.00108.68 C ANISOU 3082 C ALA D 24 12363 18785 10145 -1983 1575 -2041 C ATOM 3083 O ALA D 24 -19.171 -17.842 -11.728 1.00118.52 O ANISOU 3083 O ALA D 24 13688 20438 10905 -2670 1767 -1842 O ATOM 3084 CB ALA D 24 -16.975 -17.794 -13.794 1.00 94.60 C ANISOU 3084 CB ALA D 24 11617 15711 8615 -1530 984 -877 C ATOM 3085 N SER D 25 -19.387 -15.712 -12.442 1.00108.64 N ANISOU 3085 N SER D 25 11766 18927 10586 -1558 1587 -2777 N ATOM 3086 CA SER D 25 -20.795 -15.592 -12.099 1.00105.18 C ANISOU 3086 CA SER D 25 10598 19210 10156 -1804 1867 -3510 C ATOM 3087 C SER D 25 -21.603 -15.260 -13.346 1.00105.41 C ANISOU 3087 C SER D 25 10321 18864 10867 -1282 1567 -3817 C ATOM 3088 O SER D 25 -21.124 -14.573 -14.253 1.00 89.36 O ANISOU 3088 O SER D 25 8520 16103 9330 -637 1153 -3729 O ATOM 3089 CB SER D 25 -21.019 -14.515 -11.030 1.00 98.92 C ANISOU 3089 CB SER D 25 9251 19046 9289 -1745 2107 -4340 C ATOM 3090 N GLY D 26 -22.835 -15.759 -13.383 1.00103.06 N ANISOU 3090 N GLY D 26 9525 19075 10560 -1622 1757 -4180 N ATOM 3091 CA GLY D 26 -23.724 -15.515 -14.499 1.00102.39 C ANISOU 3091 CA GLY D 26 9104 18684 11115 -1167 1444 -4531 C ATOM 3092 C GLY D 26 -23.650 -16.526 -15.620 1.00 99.29 C ANISOU 3092 C GLY D 26 9235 17684 10805 -1219 1202 -3778 C ATOM 3093 O GLY D 26 -24.161 -16.251 -16.712 1.00 99.44 O ANISOU 3093 O GLY D 26 9156 17241 11386 -747 829 -3944 O ATOM 3094 N ASN D 27 -23.036 -17.683 -15.391 1.00103.73 N ANISOU 3094 N ASN D 27 10381 18196 10834 -1758 1337 -2982 N ATOM 3095 CA ASN D 27 -22.912 -18.728 -16.399 1.00103.77 C ANISOU 3095 CA ASN D 27 10910 17633 10884 -1814 1086 -2281 C ATOM 3096 C ASN D 27 -23.830 -19.885 -16.027 1.00102.94 C ANISOU 3096 C ASN D 27 10651 18084 10378 -2609 1342 -2202 C ATOM 3097 O ASN D 27 -23.744 -20.418 -14.915 1.00114.23 O ANISOU 3097 O ASN D 27 12163 20068 11170 -3323 1662 -2071 O ATOM 3098 CB ASN D 27 -21.463 -19.203 -16.522 1.00 82.74 C ANISOU 3098 CB ASN D 27 9061 14395 7983 -1757 915 -1476 C ATOM 3099 CG ASN D 27 -20.879 -19.648 -15.195 1.00 84.69 C ANISOU 3099 CG ASN D 27 9533 15074 7573 -2334 1175 -1241 C ATOM 3100 OD1 ASN D 27 -21.158 -19.058 -14.151 1.00 88.74 O ANISOU 3100 OD1 ASN D 27 9629 16223 7864 -2557 1489 -1741 O ATOM 3101 ND2 ASN D 27 -20.067 -20.698 -15.228 1.00 85.89 N ANISOU 3101 ND2 ASN D 27 10363 14864 7408 -2572 995 -515 N ATOM 3102 N ILE D 28 -24.713 -20.263 -16.954 1.00 93.68 N ANISOU 3102 N ILE D 28 9294 16753 9548 -2541 1173 -2273 N ATOM 3103 CA ILE D 28 -25.587 -21.406 -16.711 1.00 98.28 C ANISOU 3103 CA ILE D 28 9770 17813 9758 -3345 1375 -2152 C ATOM 3104 C ILE D 28 -24.789 -22.702 -16.746 1.00106.88 C ANISOU 3104 C ILE D 28 11762 18472 10375 -3774 1209 -1172 C ATOM 3105 O ILE D 28 -25.102 -23.655 -16.020 1.00122.58 O ANISOU 3105 O ILE D 28 13905 20904 11765 -4656 1399 -920 O ATOM 3106 CB ILE D 28 -26.743 -21.419 -17.729 1.00 99.95 C ANISOU 3106 CB ILE D 28 9517 17936 10521 -3107 1184 -2531 C ATOM 3107 CG1 ILE D 28 -27.547 -20.120 -17.640 1.00103.93 C ANISOU 3107 CG1 ILE D 28 9103 18840 11544 -2624 1231 -3610 C ATOM 3108 CG2 ILE D 28 -27.655 -22.617 -17.500 1.00105.08 C ANISOU 3108 CG2 ILE D 28 10052 19096 10780 -4006 1392 -2399 C ATOM 3109 CD1 ILE D 28 -28.753 -20.080 -18.558 1.00106.76 C ANISOU 3109 CD1 ILE D 28 8928 19150 12488 -2369 982 -4107 C ATOM 3110 N PHE D 29 -23.743 -22.759 -17.563 1.00 88.84 N ANISOU 3110 N PHE D 29 10096 15335 8326 -3196 823 -646 N ATOM 3111 CA PHE D 29 -22.918 -23.945 -17.714 1.00 86.33 C ANISOU 3111 CA PHE D 29 10601 14521 7678 -3429 552 176 C ATOM 3112 C PHE D 29 -21.499 -23.652 -17.242 1.00 97.98 C ANISOU 3112 C PHE D 29 12513 15729 8986 -3172 474 448 C ATOM 3113 O PHE D 29 -21.119 -22.502 -17.007 1.00 81.50 O ANISOU 3113 O PHE D 29 10143 13731 7093 -2754 605 68 O ATOM 3114 CB PHE D 29 -22.921 -24.431 -19.169 1.00 82.42 C ANISOU 3114 CB PHE D 29 10417 13297 7603 -2991 147 495 C ATOM 3115 CG PHE D 29 -24.296 -24.714 -19.702 1.00 96.22 C ANISOU 3115 CG PHE D 29 11743 15247 9570 -3196 161 227 C ATOM 3116 CD1 PHE D 29 -25.051 -23.705 -20.279 1.00 86.11 C ANISOU 3116 CD1 PHE D 29 9842 14029 8846 -2707 169 -412 C ATOM 3117 CD2 PHE D 29 -24.841 -25.984 -19.614 1.00 93.86 C ANISOU 3117 CD2 PHE D 29 11685 15048 8928 -3890 100 593 C ATOM 3118 CE1 PHE D 29 -26.318 -23.958 -20.762 1.00 89.64 C ANISOU 3118 CE1 PHE D 29 9850 14668 9540 -2864 137 -722 C ATOM 3119 CE2 PHE D 29 -26.108 -26.244 -20.098 1.00 92.41 C ANISOU 3119 CE2 PHE D 29 11072 15085 8954 -4110 117 320 C ATOM 3120 CZ PHE D 29 -26.848 -25.231 -20.670 1.00 92.68 C ANISOU 3120 CZ PHE D 29 10419 15216 9580 -3577 148 -361 C ATOM 3121 N ASP D 30 -20.717 -24.717 -17.102 1.00 95.46 N ANISOU 3121 N ASP D 30 12895 15052 8323 -3419 198 1085 N ATOM 3122 CA ASP D 30 -19.366 -24.594 -16.575 1.00 99.54 C ANISOU 3122 CA ASP D 30 13821 15337 8661 -3230 69 1327 C ATOM 3123 C ASP D 30 -18.468 -23.847 -17.552 1.00 80.97 C ANISOU 3123 C ASP D 30 11490 12445 6829 -2370 -93 1269 C ATOM 3124 O ASP D 30 -18.592 -23.991 -18.772 1.00 92.72 O ANISOU 3124 O ASP D 30 13039 13501 8690 -1994 -287 1342 O ATOM 3125 CB ASP D 30 -18.785 -25.977 -16.287 1.00120.80 C ANISOU 3125 CB ASP D 30 17273 17689 10936 -3637 -334 1963 C ATOM 3126 CG ASP D 30 -19.789 -26.902 -15.633 1.00135.76 C ANISOU 3126 CG ASP D 30 19287 19992 12305 -4593 -273 2132 C ATOM 3127 OD1 ASP D 30 -20.901 -27.047 -16.181 1.00141.35 O ANISOU 3127 OD1 ASP D 30 19652 20883 13173 -4762 -139 1965 O ATOM 3128 OD2 ASP D 30 -19.468 -27.486 -14.578 1.00139.39 O ANISOU 3128 OD2 ASP D 30 20208 20583 12169 -5223 -388 2431 O ATOM 3129 N VAL D 31 -17.561 -23.038 -17.005 1.00 72.49 N ANISOU 3129 N VAL D 31 10386 11422 5736 -2123 -7 1135 N ATOM 3130 CA VAL D 31 -16.562 -22.369 -17.826 1.00 67.72 C ANISOU 3130 CA VAL D 31 9861 10353 5515 -1452 -149 1115 C ATOM 3131 C VAL D 31 -15.566 -23.399 -18.340 1.00 68.59 C ANISOU 3131 C VAL D 31 10522 9948 5589 -1310 -525 1575 C ATOM 3132 O VAL D 31 -15.205 -24.350 -17.633 1.00 88.56 O ANISOU 3132 O VAL D 31 13431 12459 7758 -1651 -731 1886 O ATOM 3133 CB VAL D 31 -15.865 -21.261 -17.019 1.00 93.56 C ANISOU 3133 CB VAL D 31 12950 13849 8748 -1299 30 841 C ATOM 3134 CG1 VAL D 31 -14.881 -20.504 -17.889 1.00 93.27 C ANISOU 3134 CG1 VAL D 31 12983 13385 9072 -719 -91 804 C ATOM 3135 CG2 VAL D 31 -16.895 -20.311 -16.431 1.00 70.33 C ANISOU 3135 CG2 VAL D 31 9436 11449 5838 -1424 356 294 C ATOM 3136 N ASP D 32 -15.121 -23.222 -19.585 1.00 80.37 N ANISOU 3136 N ASP D 32 12082 11012 7441 -820 -663 1582 N ATOM 3137 CA ASP D 32 -14.225 -24.196 -20.199 1.00 92.35 C ANISOU 3137 CA ASP D 32 14027 12088 8975 -624 -1015 1882 C ATOM 3138 C ASP D 32 -12.793 -24.028 -19.700 1.00 96.12 C ANISOU 3138 C ASP D 32 14626 12513 9381 -422 -1109 1871 C ATOM 3139 O ASP D 32 -12.238 -24.926 -19.059 1.00107.95 O ANISOU 3139 O ASP D 32 16451 13915 10651 -562 -1412 2086 O ATOM 3140 CB ASP D 32 -14.285 -24.075 -21.724 1.00 83.02 C ANISOU 3140 CB ASP D 32 12854 10550 8138 -243 -1083 1836 C ATOM 3141 CG ASP D 32 -13.738 -25.300 -22.428 1.00 84.95 C ANISOU 3141 CG ASP D 32 13489 10398 8389 -99 -1451 2080 C ATOM 3142 OD1 ASP D 32 -14.457 -26.319 -22.493 1.00 86.81 O ANISOU 3142 OD1 ASP D 32 13933 10519 8533 -343 -1664 2309 O ATOM 3143 OD2 ASP D 32 -12.590 -25.245 -22.917 1.00 88.18 O ANISOU 3143 OD2 ASP D 32 13978 10631 8895 244 -1539 1999 O ATOM 3144 N ILE D 33 -12.176 -22.884 -19.992 1.00 95.32 N ANISOU 3144 N ILE D 33 14293 12445 9479 -110 -914 1614 N ATOM 3145 CA ILE D 33 -10.792 -22.611 -19.621 1.00 90.73 C ANISOU 3145 CA ILE D 33 13744 11851 8880 91 -974 1537 C ATOM 3146 C ILE D 33 -10.717 -21.223 -19.001 1.00 83.17 C ANISOU 3146 C ILE D 33 12484 11182 7933 85 -672 1275 C ATOM 3147 O ILE D 33 -11.336 -20.277 -19.500 1.00 93.34 O ANISOU 3147 O ILE D 33 13557 12500 9406 159 -483 1083 O ATOM 3148 CB ILE D 33 -9.845 -22.712 -20.837 1.00 88.52 C ANISOU 3148 CB ILE D 33 13518 11288 8826 469 -1082 1462 C ATOM 3149 CG1 ILE D 33 -9.929 -24.101 -21.472 1.00109.29 C ANISOU 3149 CG1 ILE D 33 16440 13615 11470 535 -1428 1654 C ATOM 3150 CG2 ILE D 33 -8.410 -22.402 -20.433 1.00 64.96 C ANISOU 3150 CG2 ILE D 33 10464 8372 5845 651 -1122 1294 C ATOM 3151 CD1 ILE D 33 -9.111 -24.247 -22.735 1.00120.81 C ANISOU 3151 CD1 ILE D 33 17902 14877 13121 881 -1490 1491 C ATOM 3152 N MET D 34 -9.961 -21.102 -17.911 1.00 91.77 N ANISOU 3152 N MET D 34 13593 12437 8838 13 -701 1251 N ATOM 3153 CA MET D 34 -9.740 -19.822 -17.253 1.00 86.29 C ANISOU 3153 CA MET D 34 12646 11995 8145 27 -465 992 C ATOM 3154 C MET D 34 -8.245 -19.601 -17.064 1.00 74.46 C ANISOU 3154 C MET D 34 11179 10432 6682 231 -575 928 C ATOM 3155 O MET D 34 -7.455 -20.548 -17.028 1.00 75.36 O ANISOU 3155 O MET D 34 11493 10386 6755 314 -867 1053 O ATOM 3156 CB MET D 34 -10.451 -19.746 -15.896 1.00 79.05 C ANISOU 3156 CB MET D 34 11657 11469 6910 -350 -331 948 C ATOM 3157 CG MET D 34 -11.862 -20.307 -15.883 1.00 76.95 C ANISOU 3157 CG MET D 34 11350 11368 6519 -680 -243 1006 C ATOM 3158 SD MET D 34 -12.657 -20.155 -14.271 1.00 86.37 S ANISOU 3158 SD MET D 34 12392 13180 7245 -1244 12 849 S ATOM 3159 CE MET D 34 -12.757 -18.375 -14.104 1.00 80.89 C ANISOU 3159 CE MET D 34 11196 12724 6814 -935 299 290 C ATOM 3160 N GLY D 35 -7.866 -18.336 -16.940 1.00 62.51 N ANISOU 3160 N GLY D 35 9455 9030 5267 321 -391 690 N ATOM 3161 CA GLY D 35 -6.466 -18.006 -16.776 1.00 61.08 C ANISOU 3161 CA GLY D 35 9236 8840 5132 470 -459 581 C ATOM 3162 C GLY D 35 -6.285 -16.590 -16.281 1.00 65.18 C ANISOU 3162 C GLY D 35 9565 9521 5679 455 -277 349 C ATOM 3163 O GLY D 35 -7.246 -15.907 -15.921 1.00 67.54 O ANISOU 3163 O GLY D 35 9757 9947 5957 364 -135 233 O ATOM 3164 N TRP D 36 -5.026 -16.153 -16.273 1.00 71.59 N ANISOU 3164 N TRP D 36 10307 10335 6558 553 -310 226 N ATOM 3165 CA TRP D 36 -4.656 -14.838 -15.772 1.00 71.79 C ANISOU 3165 CA TRP D 36 10197 10474 6605 525 -203 20 C ATOM 3166 C TRP D 36 -3.741 -14.132 -16.761 1.00 56.55 C ANISOU 3166 C TRP D 36 8209 8440 4837 553 -151 -98 C ATOM 3167 O TRP D 36 -2.816 -14.738 -17.311 1.00 62.48 O ANISOU 3167 O TRP D 36 8921 9187 5633 613 -198 -117 O ATOM 3168 CB TRP D 36 -3.963 -14.938 -14.407 1.00 68.03 C ANISOU 3168 CB TRP D 36 9708 10183 5956 487 -312 -22 C ATOM 3169 CG TRP D 36 -4.876 -15.353 -13.297 1.00 71.31 C ANISOU 3169 CG TRP D 36 10218 10778 6097 304 -313 62 C ATOM 3170 CD1 TRP D 36 -5.121 -16.625 -12.867 1.00 67.25 C ANISOU 3170 CD1 TRP D 36 9930 10257 5364 169 -495 296 C ATOM 3171 CD2 TRP D 36 -5.668 -14.491 -12.471 1.00 61.55 C ANISOU 3171 CD2 TRP D 36 8865 9786 4733 173 -135 -126 C ATOM 3172 NE1 TRP D 36 -6.017 -16.608 -11.825 1.00 63.94 N ANISOU 3172 NE1 TRP D 36 9555 10110 4627 -131 -385 298 N ATOM 3173 CE2 TRP D 36 -6.367 -15.309 -11.563 1.00 63.82 C ANISOU 3173 CE2 TRP D 36 9280 10293 4675 -105 -136 -6 C ATOM 3174 CE3 TRP D 36 -5.852 -13.106 -12.411 1.00 61.53 C ANISOU 3174 CE3 TRP D 36 8677 9836 4865 248 -12 -419 C ATOM 3175 CZ2 TRP D 36 -7.237 -14.790 -10.607 1.00 66.18 C ANISOU 3175 CZ2 TRP D 36 9445 10962 4739 -326 70 -227 C ATOM 3176 CZ3 TRP D 36 -6.717 -12.592 -11.461 1.00 63.71 C ANISOU 3176 CZ3 TRP D 36 8816 10413 4977 133 122 -665 C ATOM 3177 CH2 TRP D 36 -7.399 -13.432 -10.572 1.00 66.05 C ANISOU 3177 CH2 TRP D 36 9162 11025 4909 -159 206 -596 C ATOM 3178 N TYR D 37 -4.007 -12.846 -16.976 1.00 56.51 N ANISOU 3178 N TYR D 37 8205 8364 4902 480 -82 -215 N ATOM 3179 CA TYR D 37 -3.175 -11.977 -17.793 1.00 56.93 C ANISOU 3179 CA TYR D 37 8286 8326 5019 353 -48 -304 C ATOM 3180 C TYR D 37 -2.750 -10.772 -16.966 1.00 69.73 C ANISOU 3180 C TYR D 37 9855 10007 6632 280 -83 -471 C ATOM 3181 O TYR D 37 -3.486 -10.318 -16.086 1.00 81.49 O ANISOU 3181 O TYR D 37 11322 11526 8115 358 -132 -558 O ATOM 3182 CB TYR D 37 -3.918 -11.491 -19.046 1.00 66.89 C ANISOU 3182 CB TYR D 37 9765 9297 6352 261 -71 -240 C ATOM 3183 CG TYR D 37 -4.300 -12.577 -20.026 1.00 74.82 C ANISOU 3183 CG TYR D 37 10852 10214 7362 310 -44 -86 C ATOM 3184 CD1 TYR D 37 -5.361 -13.433 -19.767 1.00 67.79 C ANISOU 3184 CD1 TYR D 37 9955 9306 6498 463 -86 24 C ATOM 3185 CD2 TYR D 37 -3.613 -12.728 -21.223 1.00 82.27 C ANISOU 3185 CD2 TYR D 37 11881 11123 8255 153 32 -77 C ATOM 3186 CE1 TYR D 37 -5.716 -14.420 -20.663 1.00 68.63 C ANISOU 3186 CE1 TYR D 37 10161 9297 6618 507 -102 169 C ATOM 3187 CE2 TYR D 37 -3.962 -13.712 -22.127 1.00 65.15 C ANISOU 3187 CE2 TYR D 37 9797 8873 6086 216 41 28 C ATOM 3188 CZ TYR D 37 -5.015 -14.553 -21.842 1.00 66.00 C ANISOU 3188 CZ TYR D 37 9921 8897 6259 418 -51 166 C ATOM 3189 OH TYR D 37 -5.367 -15.534 -22.738 1.00 67.82 O ANISOU 3189 OH TYR D 37 10258 9013 6497 482 -81 275 O ATOM 3190 N ARG D 38 -1.560 -10.249 -17.254 1.00 64.67 N ANISOU 3190 N ARG D 38 9170 9421 5980 107 -52 -560 N ATOM 3191 CA ARG D 38 -1.078 -9.039 -16.605 1.00 65.05 C ANISOU 3191 CA ARG D 38 9210 9479 6025 -10 -121 -705 C ATOM 3192 C ARG D 38 -0.550 -8.069 -17.651 1.00 62.73 C ANISOU 3192 C ARG D 38 9099 9025 5709 -363 -130 -714 C ATOM 3193 O ARG D 38 -0.018 -8.474 -18.689 1.00 70.99 O ANISOU 3193 O ARG D 38 10149 10135 6690 -564 5 -677 O ATOM 3194 CB ARG D 38 0.019 -9.336 -15.568 1.00 68.38 C ANISOU 3194 CB ARG D 38 9389 10184 6409 45 -123 -824 C ATOM 3195 CG ARG D 38 1.369 -9.717 -16.154 1.00 64.87 C ANISOU 3195 CG ARG D 38 8740 9929 5978 -85 -38 -934 C ATOM 3196 CD ARG D 38 2.478 -9.504 -15.137 1.00 70.86 C ANISOU 3196 CD ARG D 38 9268 10903 6752 -69 -122 -1128 C ATOM 3197 NE ARG D 38 3.770 -9.988 -15.613 1.00 80.02 N ANISOU 3197 NE ARG D 38 10109 12320 7976 -134 -61 -1355 N ATOM 3198 CZ ARG D 38 4.300 -11.157 -15.268 1.00 95.26 C ANISOU 3198 CZ ARG D 38 11817 14382 9994 154 -204 -1484 C ATOM 3199 NH1 ARG D 38 3.651 -11.961 -14.439 1.00 98.52 N ANISOU 3199 NH1 ARG D 38 12392 14663 10378 437 -417 -1314 N ATOM 3200 NH2 ARG D 38 5.481 -11.520 -15.749 1.00106.26 N ANISOU 3200 NH2 ARG D 38 12834 16046 11495 132 -170 -1820 N ATOM 3201 N GLN D 39 -0.709 -6.778 -17.369 1.00 69.36 N ANISOU 3201 N GLN D 39 10122 9660 6573 -477 -317 -784 N ATOM 3202 CA GLN D 39 -0.241 -5.711 -18.247 1.00 90.10 C ANISOU 3202 CA GLN D 39 13052 12062 9121 -918 -426 -752 C ATOM 3203 C GLN D 39 0.695 -4.805 -17.458 1.00111.81 C ANISOU 3203 C GLN D 39 15732 14907 11842 -1095 -502 -895 C ATOM 3204 O GLN D 39 0.251 -4.060 -16.578 1.00 68.79 O ANISOU 3204 O GLN D 39 10346 9304 6487 -908 -732 -1006 O ATOM 3205 CB GLN D 39 -1.409 -4.915 -18.827 1.00 87.99 C ANISOU 3205 CB GLN D 39 13214 11287 8931 -914 -759 -687 C ATOM 3206 CG GLN D 39 -0.974 -3.669 -19.582 1.00 83.71 C ANISOU 3206 CG GLN D 39 13140 10399 8266 -1429 -1024 -620 C ATOM 3207 CD GLN D 39 -1.782 -3.434 -20.841 1.00 90.30 C ANISOU 3207 CD GLN D 39 14476 10765 9068 -1598 -1288 -448 C ATOM 3208 OE1 GLN D 39 -2.752 -4.141 -21.112 1.00 95.96 O ANISOU 3208 OE1 GLN D 39 15143 11408 9911 -1264 -1281 -416 O ATOM 3209 NE2 GLN D 39 -1.380 -2.440 -21.623 1.00 94.02 N ANISOU 3209 NE2 GLN D 39 15480 10900 9345 -2169 -1560 -324 N ATOM 3210 N ALA D 40 1.985 -4.874 -17.773 1.00126.48 N ANISOU 3210 N ALA D 40 17423 17054 13580 -1454 -309 -948 N ATOM 3211 CA ALA D 40 2.951 -3.988 -17.151 1.00137.10 C ANISOU 3211 CA ALA D 40 18702 18499 14892 -1706 -384 -1084 C ATOM 3212 C ALA D 40 2.791 -2.571 -17.704 1.00141.96 C ANISOU 3212 C ALA D 40 19847 18682 15411 -2160 -687 -986 C ATOM 3213 O ALA D 40 2.331 -2.386 -18.834 1.00150.71 O ANISOU 3213 O ALA D 40 21348 19509 16407 -2441 -769 -814 O ATOM 3214 CB ALA D 40 4.371 -4.490 -17.398 1.00141.92 C ANISOU 3214 CB ALA D 40 18906 19599 15419 -1988 -90 -1250 C ATOM 3215 N PRO D 41 3.150 -1.552 -16.922 1.00127.53 N ANISOU 3215 N PRO D 41 18102 16740 13612 -2250 -929 -1085 N ATOM 3216 CA PRO D 41 3.038 -0.173 -17.416 1.00127.18 C ANISOU 3216 CA PRO D 41 18649 16198 13476 -2705 -1344 -986 C ATOM 3217 C PRO D 41 3.984 0.068 -18.583 1.00119.59 C ANISOU 3217 C PRO D 41 17886 15357 12195 -3543 -1184 -855 C ATOM 3218 O PRO D 41 5.175 -0.244 -18.511 1.00115.53 O ANISOU 3218 O PRO D 41 16954 15372 11571 -3848 -829 -990 O ATOM 3219 CB PRO D 41 3.415 0.676 -16.197 1.00131.20 C ANISOU 3219 CB PRO D 41 19098 16666 14087 -2594 -1587 -1167 C ATOM 3220 CG PRO D 41 4.230 -0.237 -15.337 1.00127.98 C ANISOU 3220 CG PRO D 41 18055 16852 13722 -2357 -1200 -1328 C ATOM 3221 CD PRO D 41 3.637 -1.601 -15.532 1.00127.44 C ANISOU 3221 CD PRO D 41 17718 16991 13710 -1941 -912 -1285 C ATOM 3222 N GLY D 42 3.442 0.627 -19.664 1.00119.58 N ANISOU 3222 N GLY D 42 18526 14880 12028 -3944 -1472 -630 N ATOM 3223 CA GLY D 42 4.205 0.868 -20.868 1.00124.21 C ANISOU 3223 CA GLY D 42 19411 15580 12204 -4864 -1319 -480 C ATOM 3224 C GLY D 42 4.487 -0.356 -21.709 1.00115.72 C ANISOU 3224 C GLY D 42 17969 15024 10975 -4959 -755 -513 C ATOM 3225 O GLY D 42 5.032 -0.217 -22.811 1.00121.25 O ANISOU 3225 O GLY D 42 18915 15880 11273 -5766 -577 -429 O ATOM 3226 N LYS D 43 4.136 -1.548 -21.235 1.00 99.59 N ANISOU 3226 N LYS D 43 15378 13257 9204 -4208 -492 -648 N ATOM 3227 CA LYS D 43 4.379 -2.785 -21.958 1.00 89.29 C ANISOU 3227 CA LYS D 43 13704 12408 7812 -4184 -31 -732 C ATOM 3228 C LYS D 43 3.053 -3.453 -22.298 1.00 80.34 C ANISOU 3228 C LYS D 43 12765 10928 6833 -3654 -156 -562 C ATOM 3229 O LYS D 43 2.027 -3.215 -21.654 1.00 80.57 O ANISOU 3229 O LYS D 43 12952 10542 7118 -3137 -498 -489 O ATOM 3230 CB LYS D 43 5.262 -3.741 -21.145 1.00 83.78 C ANISOU 3230 CB LYS D 43 12193 12336 7303 -3792 320 -1070 C ATOM 3231 CG LYS D 43 6.509 -3.086 -20.570 1.00 89.04 C ANISOU 3231 CG LYS D 43 12577 13339 7917 -4181 385 -1296 C ATOM 3232 CD LYS D 43 7.666 -4.068 -20.486 1.00 98.29 C ANISOU 3232 CD LYS D 43 12963 15234 9149 -4109 787 -1719 C ATOM 3233 CE LYS D 43 7.298 -5.301 -19.680 1.00107.09 C ANISOU 3233 CE LYS D 43 13686 16395 10609 -3202 748 -1819 C ATOM 3234 NZ LYS D 43 8.410 -6.291 -19.657 1.00118.56 N ANISOU 3234 NZ LYS D 43 14410 18463 12174 -3061 996 -2288 N ATOM 3235 N GLU D 44 3.087 -4.296 -23.326 1.00 80.40 N ANISOU 3235 N GLU D 44 12720 11153 6677 -3804 134 -552 N ATOM 3236 CA GLU D 44 1.880 -4.957 -23.793 1.00 95.96 C ANISOU 3236 CA GLU D 44 14890 12805 8764 -3385 21 -383 C ATOM 3237 C GLU D 44 1.456 -6.059 -22.825 1.00 72.71 C ANISOU 3237 C GLU D 44 11430 10030 6165 -2567 111 -494 C ATOM 3238 O GLU D 44 2.233 -6.527 -21.989 1.00 74.28 O ANISOU 3238 O GLU D 44 11114 10638 6470 -2350 297 -711 O ATOM 3239 CB GLU D 44 2.094 -5.537 -25.191 1.00107.09 C ANISOU 3239 CB GLU D 44 16418 14410 9860 -3821 298 -357 C ATOM 3240 CG GLU D 44 2.449 -4.501 -26.246 1.00125.19 C ANISOU 3240 CG GLU D 44 19341 16537 11690 -4780 204 -199 C ATOM 3241 CD GLU D 44 1.320 -3.524 -26.513 1.00134.10 C ANISOU 3241 CD GLU D 44 21292 16822 12838 -4834 -437 135 C ATOM 3242 OE1 GLU D 44 0.146 -3.893 -26.297 1.00134.80 O ANISOU 3242 OE1 GLU D 44 21422 16536 13258 -4159 -696 209 O ATOM 3243 OE2 GLU D 44 1.606 -2.385 -26.938 1.00142.30 O ANISOU 3243 OE2 GLU D 44 22940 17563 13566 -5568 -727 293 O ATOM 3244 N ARG D 45 0.198 -6.470 -22.953 1.00 76.72 N ANISOU 3244 N ARG D 45 12653 11249 5247 -2622 -739 1290 N ATOM 3245 CA ARG D 45 -0.342 -7.515 -22.097 1.00 71.92 C ANISOU 3245 CA ARG D 45 11650 10679 4995 -2031 -539 945 C ATOM 3246 C ARG D 45 0.249 -8.871 -22.473 1.00 85.06 C ANISOU 3246 C ARG D 45 12921 12851 6545 -1939 13 787 C ATOM 3247 O ARG D 45 0.582 -9.131 -23.632 1.00103.96 O ANISOU 3247 O ARG D 45 15407 15524 8568 -2186 207 841 O ATOM 3248 CB ARG D 45 -1.868 -7.551 -22.204 1.00 72.36 C ANISOU 3248 CB ARG D 45 11937 10331 5224 -1649 -896 776 C ATOM 3249 CG ARG D 45 -2.558 -8.383 -21.133 1.00 79.16 C ANISOU 3249 CG ARG D 45 12422 11194 6459 -1126 -784 470 C ATOM 3250 CD ARG D 45 -4.068 -8.201 -21.175 1.00 79.63 C ANISOU 3250 CD ARG D 45 12658 10895 6705 -801 -1175 290 C ATOM 3251 NE ARG D 45 -4.455 -6.802 -21.016 1.00 79.89 N ANISOU 3251 NE ARG D 45 13035 10508 6813 -848 -1732 333 N ATOM 3252 CZ ARG D 45 -5.708 -6.385 -20.861 1.00 77.54 C ANISOU 3252 CZ ARG D 45 12845 9878 6738 -522 -2166 107 C ATOM 3253 NH1 ARG D 45 -6.703 -7.262 -20.839 1.00 66.38 N ANISOU 3253 NH1 ARG D 45 11198 8548 5476 -183 -2060 -139 N ATOM 3254 NH2 ARG D 45 -5.967 -5.092 -20.724 1.00 75.29 N ANISOU 3254 NH2 ARG D 45 12888 9176 6545 -531 -2744 105 N ATOM 3255 N GLU D 46 0.387 -9.736 -21.470 1.00 78.60 N ANISOU 3255 N GLU D 46 11678 12150 6034 -1577 228 572 N ATOM 3256 CA GLU D 46 0.923 -11.074 -21.665 1.00 78.53 C ANISOU 3256 CA GLU D 46 11294 12530 6015 -1399 639 366 C ATOM 3257 C GLU D 46 0.102 -12.068 -20.856 1.00 71.89 C ANISOU 3257 C GLU D 46 10273 11520 5521 -917 607 149 C ATOM 3258 O GLU D 46 -0.615 -11.700 -19.923 1.00 76.71 O ANISOU 3258 O GLU D 46 10926 11854 6368 -758 377 150 O ATOM 3259 CB GLU D 46 2.403 -11.159 -21.264 1.00 87.40 C ANISOU 3259 CB GLU D 46 12022 14055 7130 -1579 936 369 C ATOM 3260 CG GLU D 46 2.691 -10.690 -19.847 1.00100.97 C ANISOU 3260 CG GLU D 46 13592 15613 9158 -1521 795 423 C ATOM 3261 CD GLU D 46 4.124 -10.951 -19.427 1.00113.47 C ANISOU 3261 CD GLU D 46 14735 17588 10793 -1635 1061 380 C ATOM 3262 OE1 GLU D 46 4.657 -12.029 -19.764 1.00116.69 O ANISOU 3262 OE1 GLU D 46 14813 18333 11192 -1469 1349 154 O ATOM 3263 OE2 GLU D 46 4.721 -10.075 -18.766 1.00121.55 O ANISOU 3263 OE2 GLU D 46 15730 18568 11885 -1870 941 539 O ATOM 3264 N LEU D 47 0.216 -13.339 -21.231 1.00 66.76 N ANISOU 3264 N LEU D 47 9422 11062 4881 -703 824 -52 N ATOM 3265 CA LEU D 47 -0.473 -14.421 -20.540 1.00 73.33 C ANISOU 3265 CA LEU D 47 10099 11744 6017 -328 773 -212 C ATOM 3266 C LEU D 47 0.422 -14.957 -19.428 1.00 74.28 C ANISOU 3266 C LEU D 47 9858 12002 6362 -222 893 -267 C ATOM 3267 O LEU D 47 1.542 -15.410 -19.690 1.00 77.95 O ANISOU 3267 O LEU D 47 10078 12764 6776 -238 1101 -377 O ATOM 3268 CB LEU D 47 -0.845 -15.537 -21.516 1.00 61.40 C ANISOU 3268 CB LEU D 47 8619 10275 4435 -147 829 -400 C ATOM 3269 CG LEU D 47 -1.381 -16.835 -20.906 1.00 59.72 C ANISOU 3269 CG LEU D 47 8247 9915 4530 177 751 -544 C ATOM 3270 CD1 LEU D 47 -2.719 -16.606 -20.222 1.00 57.20 C ANISOU 3270 CD1 LEU D 47 8036 9300 4398 239 514 -455 C ATOM 3271 CD2 LEU D 47 -1.492 -17.922 -21.965 1.00 68.41 C ANISOU 3271 CD2 LEU D 47 9383 11060 5550 349 774 -764 C ATOM 3272 N VAL D 48 -0.070 -14.901 -18.192 1.00 74.53 N ANISOU 3272 N VAL D 48 9845 11847 6627 -111 747 -218 N ATOM 3273 CA VAL D 48 0.697 -15.406 -17.057 1.00 72.91 C ANISOU 3273 CA VAL D 48 9361 11723 6620 -25 789 -239 C ATOM 3274 C VAL D 48 0.530 -16.913 -16.924 1.00 74.26 C ANISOU 3274 C VAL D 48 9404 11849 6963 226 765 -375 C ATOM 3275 O VAL D 48 1.495 -17.678 -17.040 1.00 75.71 O ANISOU 3275 O VAL D 48 9374 12174 7219 333 838 -514 O ATOM 3276 CB VAL D 48 0.285 -14.681 -15.763 1.00 55.37 C ANISOU 3276 CB VAL D 48 7174 9364 4501 -48 636 -131 C ATOM 3277 CG1 VAL D 48 0.957 -15.325 -14.560 1.00 64.85 C ANISOU 3277 CG1 VAL D 48 8144 10621 5877 36 632 -133 C ATOM 3278 CG2 VAL D 48 0.639 -13.210 -15.848 1.00 56.35 C ANISOU 3278 CG2 VAL D 48 7437 9473 4501 -282 571 -17 C ATOM 3279 N ALA D 49 -0.698 -17.361 -16.681 1.00 68.46 N ANISOU 3279 N ALA D 49 8787 10912 6313 319 620 -352 N ATOM 3280 CA ALA D 49 -0.970 -18.779 -16.509 1.00 72.35 C ANISOU 3280 CA ALA D 49 9219 11289 6979 490 510 -422 C ATOM 3281 C ALA D 49 -2.426 -19.046 -16.852 1.00 70.58 C ANISOU 3281 C ALA D 49 9157 10895 6763 507 388 -405 C ATOM 3282 O ALA D 49 -3.276 -18.156 -16.769 1.00 66.98 O ANISOU 3282 O ALA D 49 8795 10415 6237 424 364 -345 O ATOM 3283 CB ALA D 49 -0.658 -19.242 -15.081 1.00 73.51 C ANISOU 3283 CB ALA D 49 9239 11395 7298 495 401 -324 C ATOM 3284 N SER D 50 -2.699 -20.289 -17.241 1.00 61.83 N ANISOU 3284 N SER D 50 8068 9655 5769 633 263 -489 N ATOM 3285 CA SER D 50 -4.047 -20.735 -17.555 1.00 55.41 C ANISOU 3285 CA SER D 50 7373 8673 5008 629 109 -472 C ATOM 3286 C SER D 50 -4.202 -22.177 -17.101 1.00 60.52 C ANISOU 3286 C SER D 50 7994 9133 5866 673 -118 -442 C ATOM 3287 O SER D 50 -3.237 -22.944 -17.083 1.00 58.01 O ANISOU 3287 O SER D 50 7627 8763 5652 811 -197 -538 O ATOM 3288 CB SER D 50 -4.352 -20.619 -19.054 1.00 65.71 C ANISOU 3288 CB SER D 50 8850 9947 6171 703 117 -621 C ATOM 3289 OG SER D 50 -3.505 -21.466 -19.812 1.00 73.88 O ANISOU 3289 OG SER D 50 9873 11004 7193 871 125 -819 O ATOM 3290 N ILE D 51 -5.427 -22.539 -16.730 1.00 66.28 N ANISOU 3290 N ILE D 51 8749 9762 6672 543 -262 -318 N ATOM 3291 CA ILE D 51 -5.738 -23.889 -16.273 1.00 65.08 C ANISOU 3291 CA ILE D 51 8626 9396 6707 476 -544 -210 C ATOM 3292 C ILE D 51 -7.093 -24.289 -16.840 1.00 70.84 C ANISOU 3292 C ILE D 51 9422 10000 7491 393 -696 -199 C ATOM 3293 O ILE D 51 -8.042 -23.498 -16.817 1.00 70.89 O ANISOU 3293 O ILE D 51 9357 10160 7419 289 -583 -180 O ATOM 3294 CB ILE D 51 -5.725 -23.992 -14.733 1.00 64.02 C ANISOU 3294 CB ILE D 51 8401 9342 6583 241 -576 42 C ATOM 3295 CG1 ILE D 51 -6.129 -25.398 -14.279 1.00 60.92 C ANISOU 3295 CG1 ILE D 51 8102 8693 6352 71 -937 229 C ATOM 3296 CG2 ILE D 51 -6.621 -22.929 -14.106 1.00 57.10 C ANISOU 3296 CG2 ILE D 51 7397 8751 5549 58 -367 119 C ATOM 3297 CD1 ILE D 51 -5.960 -25.629 -12.794 1.00 68.75 C ANISOU 3297 CD1 ILE D 51 9071 9754 7298 -205 -1017 512 C ATOM 3298 N THR D 52 -7.178 -25.508 -17.366 1.00 75.87 N ANISOU 3298 N THR D 52 10190 10347 8292 464 -998 -248 N ATOM 3299 CA THR D 52 -8.408 -26.015 -17.946 1.00 66.52 C ANISOU 3299 CA THR D 52 9079 9002 7196 375 -1205 -238 C ATOM 3300 C THR D 52 -9.229 -26.741 -16.883 1.00 75.07 C ANISOU 3300 C THR D 52 10096 10035 8394 3 -1409 68 C ATOM 3301 O THR D 52 -8.804 -26.912 -15.738 1.00 92.93 O ANISOU 3301 O THR D 52 12308 12363 10639 -175 -1411 274 O ATOM 3302 CB THR D 52 -8.103 -26.939 -19.124 1.00 63.99 C ANISOU 3302 CB THR D 52 8958 8379 6976 640 -1469 -476 C ATOM 3303 OG1 THR D 52 -7.442 -28.119 -18.650 1.00 66.35 O ANISOU 3303 OG1 THR D 52 9333 8405 7474 684 -1796 -441 O ATOM 3304 CG2 THR D 52 -7.204 -26.235 -20.130 1.00 66.54 C ANISOU 3304 CG2 THR D 52 9318 8868 7097 937 -1213 -769 C ATOM 3305 N ASP D 53 -10.429 -27.180 -17.270 1.00 73.24 N ANISOU 3305 N ASP D 53 9866 9704 8257 -159 -1596 113 N ATOM 3306 CA ASP D 53 -11.292 -27.910 -16.349 1.00 86.12 C ANISOU 3306 CA ASP D 53 11414 11342 9966 -608 -1788 430 C ATOM 3307 C ASP D 53 -10.708 -29.259 -15.951 1.00 94.11 C ANISOU 3307 C ASP D 53 12654 11960 11142 -717 -2220 619 C ATOM 3308 O ASP D 53 -11.113 -29.817 -14.925 1.00 97.86 O ANISOU 3308 O ASP D 53 13109 12463 11611 -1167 -2376 970 O ATOM 3309 CB ASP D 53 -12.676 -28.104 -16.971 1.00 92.85 C ANISOU 3309 CB ASP D 53 12188 12173 10917 -761 -1926 411 C ATOM 3310 CG ASP D 53 -12.608 -28.610 -18.397 1.00104.82 C ANISOU 3310 CG ASP D 53 13957 13297 12573 -442 -2202 164 C ATOM 3311 OD1 ASP D 53 -11.711 -28.164 -19.144 1.00108.75 O ANISOU 3311 OD1 ASP D 53 14587 13756 12979 -45 -2070 -99 O ATOM 3312 OD2 ASP D 53 -13.448 -29.455 -18.772 1.00115.53 O ANISOU 3312 OD2 ASP D 53 15377 14412 14108 -614 -2554 230 O ATOM 3313 N GLY D 54 -9.770 -29.793 -16.730 1.00 86.08 N ANISOU 3313 N GLY D 54 11856 10593 10255 -324 -2445 381 N ATOM 3314 CA GLY D 54 -9.136 -31.053 -16.399 1.00 78.64 C ANISOU 3314 CA GLY D 54 11147 9210 9522 -328 -2952 479 C ATOM 3315 C GLY D 54 -8.031 -30.907 -15.374 1.00 76.36 C ANISOU 3315 C GLY D 54 10838 8997 9179 -310 -2891 581 C ATOM 3316 O GLY D 54 -7.885 -31.751 -14.485 1.00 83.37 O ANISOU 3316 O GLY D 54 11881 9633 10164 -579 -3285 877 O ATOM 3317 N GLY D 55 -7.245 -29.839 -15.486 1.00 77.05 N ANISOU 3317 N GLY D 55 10760 9408 9108 -26 -2446 360 N ATOM 3318 CA GLY D 55 -6.173 -29.593 -14.543 1.00 72.09 C ANISOU 3318 CA GLY D 55 10081 8875 8434 8 -2376 428 C ATOM 3319 C GLY D 55 -4.856 -29.234 -15.200 1.00 84.90 C ANISOU 3319 C GLY D 55 11626 10549 10082 501 -2226 31 C ATOM 3320 O GLY D 55 -3.872 -28.946 -14.512 1.00 92.70 O ANISOU 3320 O GLY D 55 12528 11639 11056 571 -2157 35 O ATOM 3321 N SER D 56 -4.824 -29.248 -16.530 1.00 93.35 N ANISOU 3321 N SER D 56 12711 11590 11166 819 -2173 -320 N ATOM 3322 CA SER D 56 -3.606 -28.908 -17.253 1.00 88.92 C ANISOU 3322 CA SER D 56 12029 11193 10565 1235 -1975 -723 C ATOM 3323 C SER D 56 -3.322 -27.416 -17.134 1.00 78.81 C ANISOU 3323 C SER D 56 10553 10379 9014 1158 -1420 -694 C ATOM 3324 O SER D 56 -4.204 -26.583 -17.365 1.00 81.73 O ANISOU 3324 O SER D 56 10924 10924 9205 979 -1167 -585 O ATOM 3325 CB SER D 56 -3.728 -29.310 -18.721 1.00 85.60 C ANISOU 3325 CB SER D 56 11696 10684 10143 1542 -2048 -1102 C ATOM 3326 OG SER D 56 -3.819 -30.717 -18.858 1.00 89.68 O ANISOU 3326 OG SER D 56 12406 10717 10949 1685 -2640 -1201 O ATOM 3327 N THR D 57 -2.086 -27.080 -16.774 1.00 70.58 N ANISOU 3327 N THR D 57 9344 9507 7968 1299 -1290 -806 N ATOM 3328 CA THR D 57 -1.669 -25.700 -16.586 1.00 63.55 C ANISOU 3328 CA THR D 57 8287 9006 6853 1202 -843 -763 C ATOM 3329 C THR D 57 -0.559 -25.348 -17.567 1.00 70.84 C ANISOU 3329 C THR D 57 9046 10197 7674 1461 -602 -1126 C ATOM 3330 O THR D 57 0.235 -26.205 -17.968 1.00 77.34 O ANISOU 3330 O THR D 57 9784 10955 8646 1767 -784 -1444 O ATOM 3331 CB THR D 57 -1.185 -25.455 -15.151 1.00 63.00 C ANISOU 3331 CB THR D 57 8135 8973 6829 1041 -873 -525 C ATOM 3332 OG1 THR D 57 -0.117 -26.360 -14.843 1.00 70.25 O ANISOU 3332 OG1 THR D 57 8996 9711 7983 1267 -1186 -673 O ATOM 3333 CG2 THR D 57 -2.322 -25.664 -14.162 1.00 62.42 C ANISOU 3333 CG2 THR D 57 8193 8780 6742 703 -1020 -158 C ATOM 3334 N ASN D 58 -0.514 -24.074 -17.949 1.00 71.50 N ANISOU 3334 N ASN D 58 9077 10598 7492 1322 -217 -1092 N ATOM 3335 CA ASN D 58 0.509 -23.562 -18.858 1.00 87.37 C ANISOU 3335 CA ASN D 58 10921 12964 9314 1426 74 -1362 C ATOM 3336 C ASN D 58 1.010 -22.239 -18.297 1.00 87.84 C ANISOU 3336 C ASN D 58 10865 13280 9232 1183 345 -1170 C ATOM 3337 O ASN D 58 0.287 -21.238 -18.324 1.00 92.14 O ANISOU 3337 O ASN D 58 11560 13843 9605 956 462 -959 O ATOM 3338 CB ASN D 58 -0.041 -23.386 -20.274 1.00 96.04 C ANISOU 3338 CB ASN D 58 12180 14154 10157 1441 200 -1507 C ATOM 3339 CG ASN D 58 1.046 -23.097 -21.290 1.00107.88 C ANISOU 3339 CG ASN D 58 13500 16089 11402 1519 495 -1818 C ATOM 3340 OD1 ASN D 58 1.602 -24.012 -21.898 1.00112.83 O ANISOU 3340 OD1 ASN D 58 14004 16797 12071 1822 429 -2207 O ATOM 3341 ND2 ASN D 58 1.356 -21.819 -21.480 1.00110.66 N ANISOU 3341 ND2 ASN D 58 13830 16742 11473 1231 803 -1663 N ATOM 3342 N TYR D 59 2.239 -22.233 -17.789 1.00 81.91 N ANISOU 3342 N TYR D 59 9847 12695 8578 1248 388 -1267 N ATOM 3343 CA TYR D 59 2.830 -21.054 -17.176 1.00 82.92 C ANISOU 3343 CA TYR D 59 9855 13033 8616 1017 581 -1093 C ATOM 3344 C TYR D 59 3.776 -20.357 -18.146 1.00 79.92 C ANISOU 3344 C TYR D 59 9282 13089 7994 924 907 -1261 C ATOM 3345 O TYR D 59 4.333 -20.977 -19.055 1.00100.45 O ANISOU 3345 O TYR D 59 11714 15910 10542 1114 995 -1597 O ATOM 3346 CB TYR D 59 3.592 -21.422 -15.900 1.00 80.18 C ANISOU 3346 CB TYR D 59 9334 12601 8531 1090 388 -1055 C ATOM 3347 CG TYR D 59 2.738 -22.037 -14.816 1.00 73.30 C ANISOU 3347 CG TYR D 59 8667 11364 7820 1067 75 -820 C ATOM 3348 CD1 TYR D 59 2.577 -23.414 -14.729 1.00 68.18 C ANISOU 3348 CD1 TYR D 59 8087 10421 7395 1269 -272 -908 C ATOM 3349 CD2 TYR D 59 2.101 -21.242 -13.873 1.00 70.66 C ANISOU 3349 CD2 TYR D 59 8459 10998 7391 821 102 -522 C ATOM 3350 CE1 TYR D 59 1.801 -23.981 -13.736 1.00 75.01 C ANISOU 3350 CE1 TYR D 59 9157 10988 8356 1140 -565 -633 C ATOM 3351 CE2 TYR D 59 1.323 -21.800 -12.877 1.00 69.94 C ANISOU 3351 CE2 TYR D 59 8520 10686 7368 733 -132 -309 C ATOM 3352 CZ TYR D 59 1.176 -23.169 -12.813 1.00 78.44 C ANISOU 3352 CZ TYR D 59 9676 11491 8636 850 -456 -329 C ATOM 3353 OH TYR D 59 0.402 -23.730 -11.823 1.00 60.99 O ANISOU 3353 OH TYR D 59 7637 9094 6445 659 -697 -56 O ATOM 3354 N ALA D 60 3.953 -19.056 -17.938 1.00 68.69 N ANISOU 3354 N ALA D 60 7884 11808 6406 610 1068 -1036 N ATOM 3355 CA ALA D 60 4.930 -18.298 -18.699 1.00 72.35 C ANISOU 3355 CA ALA D 60 8159 12711 6621 392 1360 -1107 C ATOM 3356 C ALA D 60 6.333 -18.543 -18.151 1.00 82.23 C ANISOU 3356 C ALA D 60 8961 14222 8060 475 1405 -1287 C ATOM 3357 O ALA D 60 6.518 -18.936 -16.996 1.00 97.67 O ANISOU 3357 O ALA D 60 10839 15952 10320 626 1173 -1251 O ATOM 3358 CB ALA D 60 4.602 -16.805 -18.665 1.00 65.90 C ANISOU 3358 CB ALA D 60 7582 11869 5589 -8 1411 -772 C ATOM 3359 N ASP D 61 7.332 -18.305 -19.004 1.00 84.85 N ANISOU 3359 N ASP D 61 8984 15069 8186 352 1699 -1490 N ATOM 3360 CA ASP D 61 8.717 -18.529 -18.605 1.00 98.41 C ANISOU 3360 CA ASP D 61 10181 17120 10091 440 1758 -1732 C ATOM 3361 C ASP D 61 9.174 -17.564 -17.519 1.00 98.47 C ANISOU 3361 C ASP D 61 10139 17057 10217 163 1683 -1429 C ATOM 3362 O ASP D 61 10.104 -17.888 -16.772 1.00112.49 O ANISOU 3362 O ASP D 61 11557 18906 12279 313 1572 -1580 O ATOM 3363 CB ASP D 61 9.640 -18.416 -19.820 1.00115.03 C ANISOU 3363 CB ASP D 61 11906 19915 11884 306 2151 -2036 C ATOM 3364 CG ASP D 61 9.281 -19.395 -20.920 1.00124.87 C ANISOU 3364 CG ASP D 61 13180 21280 12984 623 2219 -2418 C ATOM 3365 OD1 ASP D 61 8.657 -20.433 -20.613 1.00122.34 O ANISOU 3365 OD1 ASP D 61 13027 20510 12947 1047 1897 -2550 O ATOM 3366 OD2 ASP D 61 9.624 -19.127 -22.091 1.00129.82 O ANISOU 3366 OD2 ASP D 61 13678 22459 13188 417 2574 -2578 O ATOM 3367 N SER D 62 8.544 -16.394 -17.411 1.00 86.39 N ANISOU 3367 N SER D 62 8971 15359 8494 -208 1684 -1037 N ATOM 3368 CA SER D 62 8.931 -15.408 -16.411 1.00 87.25 C ANISOU 3368 CA SER D 62 9080 15370 8699 -465 1566 -772 C ATOM 3369 C SER D 62 8.338 -15.686 -15.036 1.00 85.15 C ANISOU 3369 C SER D 62 9011 14630 8711 -238 1235 -652 C ATOM 3370 O SER D 62 8.785 -15.081 -14.056 1.00 92.14 O ANISOU 3370 O SER D 62 9852 15442 9717 -360 1096 -512 O ATOM 3371 CB SER D 62 8.521 -14.006 -16.870 1.00107.20 C ANISOU 3371 CB SER D 62 11942 17871 10916 -937 1616 -439 C ATOM 3372 OG SER D 62 7.117 -13.912 -17.036 1.00119.83 O ANISOU 3372 OG SER D 62 14014 19088 12428 -858 1477 -307 O ATOM 3373 N VAL D 63 7.348 -16.576 -14.936 1.00 83.89 N ANISOU 3373 N VAL D 63 9071 14176 8628 47 1097 -695 N ATOM 3374 CA VAL D 63 6.723 -16.907 -13.662 1.00 82.44 C ANISOU 3374 CA VAL D 63 9074 13621 8628 188 813 -560 C ATOM 3375 C VAL D 63 6.695 -18.402 -13.389 1.00 86.73 C ANISOU 3375 C VAL D 63 9547 14000 9408 534 610 -735 C ATOM 3376 O VAL D 63 6.120 -18.824 -12.384 1.00 78.27 O ANISOU 3376 O VAL D 63 8659 12640 8441 595 364 -591 O ATOM 3377 CB VAL D 63 5.296 -16.328 -13.568 1.00 60.65 C ANISOU 3377 CB VAL D 63 6716 10616 5710 84 766 -348 C ATOM 3378 CG1 VAL D 63 5.317 -14.817 -13.749 1.00 70.35 C ANISOU 3378 CG1 VAL D 63 8077 11901 6754 -230 829 -183 C ATOM 3379 CG2 VAL D 63 4.385 -16.986 -14.593 1.00 70.56 C ANISOU 3379 CG2 VAL D 63 8124 11809 6876 205 825 -437 C ATOM 3380 N LYS D 64 7.294 -19.221 -14.251 1.00 96.23 N ANISOU 3380 N LYS D 64 10501 15383 10680 751 675 -1053 N ATOM 3381 CA LYS D 64 7.309 -20.660 -14.029 1.00 89.35 C ANISOU 3381 CA LYS D 64 9597 14277 10076 1112 373 -1252 C ATOM 3382 C LYS D 64 8.141 -21.001 -12.799 1.00 86.61 C ANISOU 3382 C LYS D 64 9093 13799 10018 1220 60 -1249 C ATOM 3383 O LYS D 64 9.239 -20.473 -12.604 1.00 97.79 O ANISOU 3383 O LYS D 64 10180 15478 11497 1165 142 -1342 O ATOM 3384 CB LYS D 64 7.863 -21.382 -15.257 1.00 98.64 C ANISOU 3384 CB LYS D 64 10504 15712 11263 1377 487 -1691 C ATOM 3385 CG LYS D 64 7.849 -22.898 -15.147 1.00110.51 C ANISOU 3385 CG LYS D 64 12015 16899 13075 1799 80 -1951 C ATOM 3386 CD LYS D 64 8.459 -23.546 -16.379 1.00126.97 C ANISOU 3386 CD LYS D 64 13791 19295 15157 2121 192 -2489 C ATOM 3387 CE LYS D 64 8.499 -25.059 -16.243 1.00137.41 C ANISOU 3387 CE LYS D 64 15141 20224 16842 2592 -327 -2797 C ATOM 3388 NZ LYS D 64 9.140 -25.704 -17.423 1.00146.56 N ANISOU 3388 NZ LYS D 64 15960 21719 18006 2985 -245 -3430 N ATOM 3389 N GLY D 65 7.607 -21.891 -11.962 1.00 83.73 N ANISOU 3389 N GLY D 65 8974 13021 9818 1334 -330 -1120 N ATOM 3390 CA GLY D 65 8.250 -22.274 -10.727 1.00 94.18 C ANISOU 3390 CA GLY D 65 10261 14143 11378 1404 -713 -1057 C ATOM 3391 C GLY D 65 7.922 -21.395 -9.539 1.00 94.91 C ANISOU 3391 C GLY D 65 10561 14180 11319 1096 -721 -683 C ATOM 3392 O GLY D 65 8.123 -21.821 -8.396 1.00103.45 O ANISOU 3392 O GLY D 65 11757 15028 12520 1101 -1089 -544 O ATOM 3393 N ARG D 66 7.424 -20.182 -9.775 1.00 82.68 N ANISOU 3393 N ARG D 66 9087 12827 9500 837 -371 -535 N ATOM 3394 CA ARG D 66 7.040 -19.260 -8.713 1.00 70.25 C ANISOU 3394 CA ARG D 66 7707 11223 7763 591 -381 -260 C ATOM 3395 C ARG D 66 5.530 -19.187 -8.530 1.00 79.67 C ANISOU 3395 C ARG D 66 9233 12306 8731 458 -327 -57 C ATOM 3396 O ARG D 66 5.030 -19.349 -7.413 1.00 84.06 O ANISOU 3396 O ARG D 66 9982 12753 9206 355 -505 135 O ATOM 3397 CB ARG D 66 7.593 -17.862 -9.008 1.00 71.14 C ANISOU 3397 CB ARG D 66 7668 11593 7767 405 -126 -269 C ATOM 3398 CG ARG D 66 9.100 -17.802 -9.167 1.00 79.33 C ANISOU 3398 CG ARG D 66 8297 12839 9006 459 -134 -466 C ATOM 3399 CD ARG D 66 9.492 -16.569 -9.957 1.00 85.52 C ANISOU 3399 CD ARG D 66 8939 13922 9635 198 178 -464 C ATOM 3400 NE ARG D 66 8.824 -15.375 -9.450 1.00 85.29 N ANISOU 3400 NE ARG D 66 9216 13781 9409 -49 175 -215 N ATOM 3401 CZ ARG D 66 8.712 -14.238 -10.128 1.00 86.38 C ANISOU 3401 CZ ARG D 66 9425 14029 9364 -313 351 -129 C ATOM 3402 NH1 ARG D 66 9.219 -14.139 -11.348 1.00 91.23 N ANISOU 3402 NH1 ARG D 66 9831 14928 9904 -435 600 -225 N ATOM 3403 NH2 ARG D 66 8.086 -13.202 -9.587 1.00 84.54 N ANISOU 3403 NH2 ARG D 66 9487 13629 9004 -462 246 37 N ATOM 3404 N PHE D 67 4.792 -18.940 -9.609 1.00 85.23 N ANISOU 3404 N PHE D 67 9990 13077 9315 442 -89 -110 N ATOM 3405 CA PHE D 67 3.341 -18.858 -9.550 1.00 75.16 C ANISOU 3405 CA PHE D 67 8957 11735 7866 341 -40 24 C ATOM 3406 C PHE D 67 2.737 -20.249 -9.671 1.00 68.21 C ANISOU 3406 C PHE D 67 8178 10654 7083 426 -227 47 C ATOM 3407 O PHE D 67 3.234 -21.094 -10.421 1.00 61.53 O ANISOU 3407 O PHE D 67 7243 9725 6411 620 -312 -126 O ATOM 3408 CB PHE D 67 2.793 -17.957 -10.660 1.00 74.98 C ANISOU 3408 CB PHE D 67 8977 11818 7694 287 213 -40 C ATOM 3409 CG PHE D 67 3.102 -16.494 -10.478 1.00 74.78 C ANISOU 3409 CG PHE D 67 8955 11904 7553 140 304 -4 C ATOM 3410 CD1 PHE D 67 3.869 -16.051 -9.411 1.00 77.28 C ANISOU 3410 CD1 PHE D 67 9205 12249 7908 81 195 51 C ATOM 3411 CD2 PHE D 67 2.610 -15.558 -11.372 1.00 67.67 C ANISOU 3411 CD2 PHE D 67 8167 11033 6513 53 428 -18 C ATOM 3412 CE1 PHE D 67 4.149 -14.708 -9.250 1.00 71.20 C ANISOU 3412 CE1 PHE D 67 8468 11528 7056 -61 210 80 C ATOM 3413 CE2 PHE D 67 2.884 -14.213 -11.214 1.00 64.76 C ANISOU 3413 CE2 PHE D 67 7858 10687 6062 -101 412 30 C ATOM 3414 CZ PHE D 67 3.653 -13.788 -10.152 1.00 64.73 C ANISOU 3414 CZ PHE D 67 7776 10703 6113 -157 303 74 C ATOM 3415 N THR D 68 1.660 -20.482 -8.925 1.00 63.65 N ANISOU 3415 N THR D 68 7779 10022 6385 266 -308 242 N ATOM 3416 CA THR D 68 0.945 -21.754 -8.944 1.00 64.59 C ANISOU 3416 CA THR D 68 8032 9935 6573 238 -526 340 C ATOM 3417 C THR D 68 -0.536 -21.462 -9.127 1.00 75.44 C ANISOU 3417 C THR D 68 9485 11411 7765 77 -362 415 C ATOM 3418 O THR D 68 -1.201 -20.999 -8.194 1.00 80.90 O ANISOU 3418 O THR D 68 10205 12277 8258 -124 -298 546 O ATOM 3419 CB THR D 68 1.188 -22.549 -7.660 1.00 68.27 C ANISOU 3419 CB THR D 68 8622 10253 7066 104 -870 562 C ATOM 3420 OG1 THR D 68 2.589 -22.813 -7.516 1.00 84.08 O ANISOU 3420 OG1 THR D 68 10519 12137 9289 305 -1080 442 O ATOM 3421 CG2 THR D 68 0.430 -23.868 -7.701 1.00 72.36 C ANISOU 3421 CG2 THR D 68 9327 10515 7654 -4 -1163 718 C ATOM 3422 N ILE D 69 -1.051 -21.724 -10.322 1.00 78.98 N ANISOU 3422 N ILE D 69 9947 11786 8274 179 -303 293 N ATOM 3423 CA ILE D 69 -2.457 -21.491 -10.624 1.00 73.14 C ANISOU 3423 CA ILE D 69 9247 11125 7417 61 -192 322 C ATOM 3424 C ILE D 69 -3.240 -22.768 -10.351 1.00 67.08 C ANISOU 3424 C ILE D 69 8579 10198 6711 -105 -436 498 C ATOM 3425 O ILE D 69 -2.758 -23.881 -10.597 1.00 78.07 O ANISOU 3425 O ILE D 69 10061 11308 8294 -21 -716 509 O ATOM 3426 CB ILE D 69 -2.639 -21.010 -12.078 1.00 81.20 C ANISOU 3426 CB ILE D 69 10268 12138 8445 227 -41 116 C ATOM 3427 CG1 ILE D 69 -4.087 -20.578 -12.325 1.00 71.87 C ANISOU 3427 CG1 ILE D 69 9103 11036 7167 136 33 112 C ATOM 3428 CG2 ILE D 69 -2.217 -22.085 -13.071 1.00 81.54 C ANISOU 3428 CG2 ILE D 69 10354 11973 8654 408 -185 -10 C ATOM 3429 CD1 ILE D 69 -4.325 -19.987 -13.697 1.00 64.91 C ANISOU 3429 CD1 ILE D 69 8285 10119 6259 269 121 -58 C ATOM 3430 N SER D 70 -4.445 -22.607 -9.812 1.00 58.58 N ANISOU 3430 N SER D 70 7472 9311 5475 -354 -360 621 N ATOM 3431 CA SER D 70 -5.325 -23.726 -9.513 1.00 69.30 C ANISOU 3431 CA SER D 70 8902 10583 6846 -632 -570 841 C ATOM 3432 C SER D 70 -6.762 -23.262 -9.707 1.00 74.54 C ANISOU 3432 C SER D 70 9417 11514 7392 -771 -376 790 C ATOM 3433 O SER D 70 -7.023 -22.087 -9.979 1.00 83.04 O ANISOU 3433 O SER D 70 10367 12797 8388 -616 -134 576 O ATOM 3434 CB SER D 70 -5.087 -24.253 -8.094 1.00 77.52 C ANISOU 3434 CB SER D 70 10029 11669 7756 -943 -746 1140 C ATOM 3435 OG SER D 70 -5.292 -23.233 -7.132 1.00 86.87 O ANISOU 3435 OG SER D 70 11084 13268 8655 -1066 -480 1136 O ATOM 3436 N ARG D 71 -7.700 -24.194 -9.564 1.00 73.42 N ANISOU 3436 N ARG D 71 9286 11352 7257 -1075 -533 982 N ATOM 3437 CA ARG D 71 -9.106 -23.862 -9.743 1.00 75.48 C ANISOU 3437 CA ARG D 71 9335 11903 7440 -1221 -373 909 C ATOM 3438 C ARG D 71 -9.963 -24.870 -8.995 1.00 78.14 C ANISOU 3438 C ARG D 71 9641 12367 7680 -1737 -516 1230 C ATOM 3439 O ARG D 71 -9.490 -25.920 -8.554 1.00 76.54 O ANISOU 3439 O ARG D 71 9669 11899 7514 -1964 -825 1530 O ATOM 3440 CB ARG D 71 -9.490 -23.823 -11.226 1.00 77.51 C ANISOU 3440 CB ARG D 71 9617 11925 7907 -949 -420 687 C ATOM 3441 CG ARG D 71 -9.472 -25.174 -11.916 1.00 84.34 C ANISOU 3441 CG ARG D 71 10689 12362 8995 -988 -774 804 C ATOM 3442 CD ARG D 71 -9.892 -25.046 -13.370 1.00 83.29 C ANISOU 3442 CD ARG D 71 10591 12048 9009 -717 -807 555 C ATOM 3443 NE ARG D 71 -11.285 -24.629 -13.506 1.00 85.84 N ANISOU 3443 NE ARG D 71 10691 12625 9301 -855 -708 488 N ATOM 3444 CZ ARG D 71 -11.881 -24.381 -14.668 1.00 80.50 C ANISOU 3444 CZ ARG D 71 10025 11834 8726 -660 -755 278 C ATOM 3445 NH1 ARG D 71 -11.205 -24.504 -15.802 1.00 77.58 N ANISOU 3445 NH1 ARG D 71 9898 11142 8436 -351 -860 129 N ATOM 3446 NH2 ARG D 71 -13.153 -24.007 -14.697 1.00 80.57 N ANISOU 3446 NH2 ARG D 71 9785 12087 8742 -773 -707 191 N ATOM 3447 N ASP D 72 -11.242 -24.527 -8.859 1.00 80.88 N ANISOU 3447 N ASP D 72 9692 13131 7906 -1939 -322 1159 N ATOM 3448 CA ASP D 72 -12.251 -25.400 -8.270 1.00 84.73 C ANISOU 3448 CA ASP D 72 10066 13853 8274 -2509 -403 1450 C ATOM 3449 C ASP D 72 -13.431 -25.439 -9.231 1.00 87.80 C ANISOU 3449 C ASP D 72 10240 14275 8845 -2486 -407 1277 C ATOM 3450 O ASP D 72 -14.189 -24.469 -9.326 1.00 81.85 O ANISOU 3450 O ASP D 72 9142 13925 8031 -2338 -135 959 O ATOM 3451 CB ASP D 72 -12.678 -24.902 -6.888 1.00 93.11 C ANISOU 3451 CB ASP D 72 10863 15594 8920 -2859 -100 1506 C ATOM 3452 CG ASP D 72 -13.553 -25.899 -6.152 1.00105.17 C ANISOU 3452 CG ASP D 72 12304 17420 10237 -3580 -181 1897 C ATOM 3453 OD1 ASP D 72 -13.712 -27.035 -6.645 1.00110.90 O ANISOU 3453 OD1 ASP D 72 13241 17718 11178 -3819 -551 2178 O ATOM 3454 OD2 ASP D 72 -14.081 -25.545 -5.077 1.00108.79 O ANISOU 3454 OD2 ASP D 72 12484 18559 10293 -3933 111 1919 O ATOM 3455 N ASN D 73 -13.580 -26.557 -9.947 1.00 99.53 N ANISOU 3455 N ASN D 73 11936 15305 10577 -2602 -772 1456 N ATOM 3456 CA ASN D 73 -14.624 -26.662 -10.961 1.00 95.10 C ANISOU 3456 CA ASN D 73 11218 14689 10225 -2556 -848 1292 C ATOM 3457 C ASN D 73 -16.024 -26.583 -10.367 1.00112.29 C ANISOU 3457 C ASN D 73 12933 17486 12245 -3017 -658 1324 C ATOM 3458 O ASN D 73 -16.977 -26.284 -11.096 1.00119.21 O ANISOU 3458 O ASN D 73 13549 18470 13276 -2904 -633 1073 O ATOM 3459 CB ASN D 73 -14.465 -27.967 -11.744 1.00 81.93 C ANISOU 3459 CB ASN D 73 9899 12388 8840 -2614 -1337 1482 C ATOM 3460 CG ASN D 73 -13.134 -28.056 -12.464 1.00 80.29 C ANISOU 3460 CG ASN D 73 10063 11648 8794 -2099 -1507 1336 C ATOM 3461 OD1 ASN D 73 -12.563 -27.042 -12.866 1.00 82.69 O ANISOU 3461 OD1 ASN D 73 10339 12021 9059 -1657 -1250 1039 O ATOM 3462 ND2 ASN D 73 -12.632 -29.274 -12.631 1.00 95.61 N ANISOU 3462 ND2 ASN D 73 12341 13069 10917 -2168 -1969 1530 N ATOM 3463 N ALA D 74 -16.172 -26.842 -9.067 1.00131.39 N ANISOU 3463 N ALA D 74 15225 20352 14343 -3547 -528 1612 N ATOM 3464 CA ALA D 74 -17.490 -26.776 -8.445 1.00136.79 C ANISOU 3464 CA ALA D 74 15392 21766 14814 -4040 -286 1616 C ATOM 3465 C ALA D 74 -17.988 -25.338 -8.363 1.00130.67 C ANISOU 3465 C ALA D 74 14145 21564 13938 -3642 132 1070 C ATOM 3466 O ALA D 74 -19.146 -25.051 -8.690 1.00134.03 O ANISOU 3466 O ALA D 74 14115 22361 14451 -3658 233 798 O ATOM 3467 CB ALA D 74 -17.448 -27.415 -7.057 1.00142.85 C ANISOU 3467 CB ALA D 74 16185 22916 15176 -4759 -245 2082 C ATOM 3468 N LYS D 75 -17.126 -24.418 -7.933 1.00118.03 N ANISOU 3468 N LYS D 75 12646 20016 12185 -3264 323 880 N ATOM 3469 CA LYS D 75 -17.494 -23.020 -7.765 1.00105.51 C ANISOU 3469 CA LYS D 75 10679 18901 10508 -2857 631 348 C ATOM 3470 C LYS D 75 -17.108 -22.152 -8.955 1.00100.82 C ANISOU 3470 C LYS D 75 10269 17802 10238 -2164 502 -9 C ATOM 3471 O LYS D 75 -17.425 -20.959 -8.958 1.00100.08 O ANISOU 3471 O LYS D 75 9922 17967 10137 -1781 637 -464 O ATOM 3472 CB LYS D 75 -16.852 -22.456 -6.492 1.00100.98 C ANISOU 3472 CB LYS D 75 10105 18723 9539 -2901 882 340 C ATOM 3473 CG LYS D 75 -17.171 -23.242 -5.230 1.00114.00 C ANISOU 3473 CG LYS D 75 11625 20930 10761 -3641 1019 720 C ATOM 3474 CD LYS D 75 -16.525 -22.607 -4.009 1.00125.75 C ANISOU 3474 CD LYS D 75 13143 22808 11828 -3636 1250 665 C ATOM 3475 CE LYS D 75 -15.017 -22.500 -4.172 1.00128.76 C ANISOU 3475 CE LYS D 75 14083 22488 12353 -3282 1028 810 C ATOM 3476 NZ LYS D 75 -14.372 -21.858 -2.993 1.00133.99 N ANISOU 3476 NZ LYS D 75 14791 23492 12628 -3265 1205 749 N ATOM 3477 N ASN D 76 -16.439 -22.720 -9.958 1.00107.35 N ANISOU 3477 N ASN D 76 11536 17928 11326 -2007 215 173 N ATOM 3478 CA ASN D 76 -15.963 -21.981 -11.128 1.00103.20 C ANISOU 3478 CA ASN D 76 11248 16936 11028 -1442 94 -93 C ATOM 3479 C ASN D 76 -15.111 -20.784 -10.707 1.00105.98 C ANISOU 3479 C ASN D 76 11679 17348 11239 -1104 254 -293 C ATOM 3480 O ASN D 76 -15.379 -19.632 -11.054 1.00112.75 O ANISOU 3480 O ASN D 76 12431 18257 12151 -738 269 -664 O ATOM 3481 CB ASN D 76 -17.130 -21.547 -12.019 1.00101.36 C ANISOU 3481 CB ASN D 76 10756 16751 11004 -1242 2 -429 C ATOM 3482 CG ASN D 76 -17.704 -22.694 -12.826 1.00103.42 C ANISOU 3482 CG ASN D 76 11086 16723 11485 -1465 -260 -239 C ATOM 3483 OD1 ASN D 76 -18.880 -23.032 -12.698 1.00105.22 O ANISOU 3483 OD1 ASN D 76 10928 17285 11765 -1747 -268 -275 O ATOM 3484 ND2 ASN D 76 -16.872 -23.300 -13.665 1.00 99.69 N ANISOU 3484 ND2 ASN D 76 11083 15653 11143 -1337 -489 -68 N ATOM 3485 N THR D 77 -14.068 -21.084 -9.938 1.00 91.44 N ANISOU 3485 N THR D 77 10050 15459 9234 -1242 307 -34 N ATOM 3486 CA THR D 77 -13.143 -20.084 -9.429 1.00 80.63 C ANISOU 3486 CA THR D 77 8778 14125 7731 -992 424 -161 C ATOM 3487 C THR D 77 -11.718 -20.539 -9.707 1.00 67.08 C ANISOU 3487 C THR D 77 7468 11930 6092 -919 295 82 C ATOM 3488 O THR D 77 -11.409 -21.727 -9.591 1.00 76.89 O ANISOU 3488 O THR D 77 8867 12980 7369 -1171 153 395 O ATOM 3489 CB THR D 77 -13.335 -19.861 -7.921 1.00 91.16 C ANISOU 3489 CB THR D 77 9866 16043 8726 -1247 647 -159 C ATOM 3490 OG1 THR D 77 -14.722 -19.634 -7.642 1.00 98.13 O ANISOU 3490 OG1 THR D 77 10283 17479 9523 -1361 792 -412 O ATOM 3491 CG2 THR D 77 -12.527 -18.663 -7.446 1.00 86.36 C ANISOU 3491 CG2 THR D 77 9337 15468 8008 -934 724 -375 C ATOM 3492 N VAL D 78 -10.857 -19.596 -10.082 1.00 63.16 N ANISOU 3492 N VAL D 78 7127 11240 5632 -582 308 -77 N ATOM 3493 CA VAL D 78 -9.445 -19.870 -10.320 1.00 72.73 C ANISOU 3493 CA VAL D 78 8626 12102 6907 -489 229 77 C ATOM 3494 C VAL D 78 -8.616 -19.104 -9.301 1.00 78.05 C ANISOU 3494 C VAL D 78 9302 12938 7416 -458 331 64 C ATOM 3495 O VAL D 78 -8.914 -17.948 -8.982 1.00 58.37 O ANISOU 3495 O VAL D 78 6691 10661 4827 -322 422 -173 O ATOM 3496 CB VAL D 78 -9.014 -19.505 -11.755 1.00 72.48 C ANISOU 3496 CB VAL D 78 8779 11724 7037 -196 155 -59 C ATOM 3497 CG1 VAL D 78 -9.418 -20.603 -12.711 1.00 89.98 C ANISOU 3497 CG1 VAL D 78 11085 13690 9411 -230 -4 8 C ATOM 3498 CG2 VAL D 78 -9.618 -18.174 -12.175 1.00 70.55 C ANISOU 3498 CG2 VAL D 78 8470 11559 6778 8 180 -338 C ATOM 3499 N TYR D 79 -7.570 -19.754 -8.797 1.00 79.66 N ANISOU 3499 N TYR D 79 9652 13006 7610 -557 256 290 N ATOM 3500 CA TYR D 79 -6.692 -19.185 -7.785 1.00 73.09 C ANISOU 3500 CA TYR D 79 8846 12291 6635 -555 300 312 C ATOM 3501 C TYR D 79 -5.273 -19.118 -8.330 1.00 76.95 C ANISOU 3501 C TYR D 79 9493 12457 7288 -361 215 325 C ATOM 3502 O TYR D 79 -4.746 -20.122 -8.821 1.00 84.13 O ANISOU 3502 O TYR D 79 10502 13104 8360 -350 72 439 O ATOM 3503 CB TYR D 79 -6.728 -20.015 -6.499 1.00 60.82 C ANISOU 3503 CB TYR D 79 7301 10922 4885 -901 248 579 C ATOM 3504 CG TYR D 79 -8.121 -20.245 -5.959 1.00 63.63 C ANISOU 3504 CG TYR D 79 7451 11696 5030 -1196 367 598 C ATOM 3505 CD1 TYR D 79 -8.731 -19.306 -5.138 1.00 77.91 C ANISOU 3505 CD1 TYR D 79 9033 14001 6568 -1208 579 374 C ATOM 3506 CD2 TYR D 79 -8.826 -21.400 -6.270 1.00 65.39 C ANISOU 3506 CD2 TYR D 79 7677 11847 5322 -1468 255 809 C ATOM 3507 CE1 TYR D 79 -10.004 -19.510 -4.641 1.00 80.66 C ANISOU 3507 CE1 TYR D 79 9102 14846 6697 -1488 733 336 C ATOM 3508 CE2 TYR D 79 -10.101 -21.613 -5.778 1.00 73.92 C ANISOU 3508 CE2 TYR D 79 8509 13379 6198 -1805 385 837 C ATOM 3509 CZ TYR D 79 -10.684 -20.665 -4.965 1.00 75.84 C ANISOU 3509 CZ TYR D 79 8468 14197 6151 -1816 653 588 C ATOM 3510 OH TYR D 79 -11.952 -20.871 -4.472 1.00 84.62 O ANISOU 3510 OH TYR D 79 9246 15870 7035 -2160 826 561 O ATOM 3511 N LEU D 80 -4.661 -17.941 -8.245 1.00 69.23 N ANISOU 3511 N LEU D 80 8515 11515 6275 -211 280 183 N ATOM 3512 CA LEU D 80 -3.276 -17.729 -8.659 1.00 68.69 C ANISOU 3512 CA LEU D 80 8523 11248 6329 -87 238 187 C ATOM 3513 C LEU D 80 -2.453 -17.474 -7.399 1.00 81.08 C ANISOU 3513 C LEU D 80 10091 12910 7806 -156 186 264 C ATOM 3514 O LEU D 80 -2.368 -16.345 -6.913 1.00 91.69 O ANISOU 3514 O LEU D 80 11422 14374 9044 -119 222 152 O ATOM 3515 CB LEU D 80 -3.160 -16.570 -9.646 1.00 67.69 C ANISOU 3515 CB LEU D 80 8433 11054 6231 57 298 18 C ATOM 3516 CG LEU D 80 -1.746 -16.263 -10.150 1.00 52.75 C ANISOU 3516 CG LEU D 80 6567 9056 4421 103 302 26 C ATOM 3517 CD1 LEU D 80 -1.191 -17.429 -10.957 1.00 53.09 C ANISOU 3517 CD1 LEU D 80 6590 8983 4600 160 293 47 C ATOM 3518 CD2 LEU D 80 -1.723 -14.980 -10.967 1.00 52.42 C ANISOU 3518 CD2 LEU D 80 6613 8967 4336 127 321 -70 C ATOM 3519 N ALA D 81 -1.849 -18.535 -6.871 1.00 79.11 N ANISOU 3519 N ALA D 81 9885 12564 7610 -246 37 445 N ATOM 3520 CA ALA D 81 -1.019 -18.439 -5.672 1.00 67.62 C ANISOU 3520 CA ALA D 81 8462 11155 6074 -320 -79 541 C ATOM 3521 C ALA D 81 0.363 -17.950 -6.082 1.00 74.00 C ANISOU 3521 C ALA D 81 9219 11829 7069 -155 -116 450 C ATOM 3522 O ALA D 81 1.187 -18.720 -6.580 1.00 83.85 O ANISOU 3522 O ALA D 81 10429 12898 8532 -59 -231 455 O ATOM 3523 CB ALA D 81 -0.947 -19.783 -4.957 1.00 67.69 C ANISOU 3523 CB ALA D 81 8582 11063 6075 -502 -316 792 C ATOM 3524 N MET D 82 0.619 -16.661 -5.878 1.00 90.01 N ANISOU 3524 N MET D 82 11221 13957 9020 -124 -42 340 N ATOM 3525 CA MET D 82 1.892 -16.057 -6.245 1.00 85.68 C ANISOU 3525 CA MET D 82 10598 13335 8623 -55 -66 279 C ATOM 3526 C MET D 82 2.861 -16.141 -5.073 1.00 88.15 C ANISOU 3526 C MET D 82 10903 13641 8950 -97 -260 357 C ATOM 3527 O MET D 82 2.501 -15.819 -3.937 1.00 94.74 O ANISOU 3527 O MET D 82 11834 14585 9579 -181 -325 396 O ATOM 3528 CB MET D 82 1.693 -14.601 -6.669 1.00 76.74 C ANISOU 3528 CB MET D 82 9497 12239 7423 -50 19 158 C ATOM 3529 CG MET D 82 0.762 -14.426 -7.860 1.00 79.59 C ANISOU 3529 CG MET D 82 9903 12566 7769 -6 143 82 C ATOM 3530 SD MET D 82 0.665 -12.724 -8.451 1.00 81.23 S ANISOU 3530 SD MET D 82 10228 12702 7931 -22 100 -24 S ATOM 3531 CE MET D 82 -0.109 -11.914 -7.055 1.00 76.46 C ANISOU 3531 CE MET D 82 9679 12198 7175 44 -29 -164 C ATOM 3532 N ALA D 83 4.085 -16.582 -5.353 1.00 82.44 N ANISOU 3532 N ALA D 83 10045 12819 8459 -26 -363 344 N ATOM 3533 CA ALA D 83 5.135 -16.681 -4.351 1.00 80.94 C ANISOU 3533 CA ALA D 83 9821 12587 8348 -37 -606 394 C ATOM 3534 C ALA D 83 6.428 -16.112 -4.916 1.00 75.98 C ANISOU 3534 C ALA D 83 8948 11987 7934 9 -584 272 C ATOM 3535 O ALA D 83 6.659 -16.147 -6.128 1.00 91.44 O ANISOU 3535 O ALA D 83 10745 14001 9999 60 -404 163 O ATOM 3536 CB ALA D 83 5.353 -18.131 -3.897 1.00 62.03 C ANISOU 3536 CB ALA D 83 7479 10023 6066 4 -882 501 C ATOM 3537 N SER D 84 7.268 -15.588 -4.021 1.00 70.12 N ANISOU 3537 N SER D 84 8170 11245 7227 -41 -769 291 N ATOM 3538 CA SER D 84 8.536 -14.960 -4.396 1.00 72.86 C ANISOU 3538 CA SER D 84 8247 11664 7774 -70 -772 196 C ATOM 3539 C SER D 84 8.310 -13.833 -5.404 1.00 69.83 C ANISOU 3539 C SER D 84 7846 11384 7302 -209 -516 166 C ATOM 3540 O SER D 84 8.933 -13.781 -6.466 1.00 70.63 O ANISOU 3540 O SER D 84 7707 11619 7509 -254 -349 89 O ATOM 3541 CB SER D 84 9.525 -15.996 -4.938 1.00 65.75 C ANISOU 3541 CB SER D 84 7030 10780 7173 93 -836 60 C ATOM 3542 OG SER D 84 10.696 -15.372 -5.436 1.00101.01 O ANISOU 3542 OG SER D 84 11147 15431 11802 21 -760 -59 O ATOM 3543 N LEU D 85 7.404 -12.923 -5.056 1.00 77.27 N ANISOU 3543 N LEU D 85 9052 12278 8029 -283 -514 211 N ATOM 3544 CA LEU D 85 7.034 -11.841 -5.959 1.00 79.90 C ANISOU 3544 CA LEU D 85 9467 12614 8277 -409 -386 202 C ATOM 3545 C LEU D 85 8.208 -10.894 -6.178 1.00 85.62 C ANISOU 3545 C LEU D 85 10049 13372 9110 -628 -459 235 C ATOM 3546 O LEU D 85 8.895 -10.504 -5.229 1.00 78.75 O ANISOU 3546 O LEU D 85 9150 12460 8311 -673 -683 248 O ATOM 3547 CB LEU D 85 5.831 -11.081 -5.406 1.00 67.62 C ANISOU 3547 CB LEU D 85 8203 10974 6516 -370 -465 168 C ATOM 3548 CG LEU D 85 4.483 -11.780 -5.592 1.00 71.07 C ANISOU 3548 CG LEU D 85 8737 11444 6823 -238 -324 131 C ATOM 3549 CD1 LEU D 85 3.381 -11.048 -4.849 1.00 64.73 C ANISOU 3549 CD1 LEU D 85 8119 10656 5821 -168 -406 14 C ATOM 3550 CD2 LEU D 85 4.149 -11.886 -7.070 1.00 90.67 C ANISOU 3550 CD2 LEU D 85 11204 13912 9337 -256 -139 128 C ATOM 3551 N LYS D 86 8.432 -10.529 -7.433 1.00 86.00 N ANISOU 3551 N LYS D 86 10017 13514 9146 -805 -283 263 N ATOM 3552 CA LYS D 86 9.501 -9.641 -7.848 1.00 76.29 C ANISOU 3552 CA LYS D 86 8635 12380 7974 -1126 -311 341 C ATOM 3553 C LYS D 86 8.940 -8.294 -8.286 1.00 82.24 C ANISOU 3553 C LYS D 86 9724 12947 8575 -1361 -436 459 C ATOM 3554 O LYS D 86 7.771 -8.194 -8.673 1.00 83.90 O ANISOU 3554 O LYS D 86 10208 13022 8650 -1249 -417 438 O ATOM 3555 CB LYS D 86 10.296 -10.264 -9.004 1.00 70.47 C ANISOU 3555 CB LYS D 86 7524 11972 7280 -1225 -15 287 C ATOM 3556 CG LYS D 86 10.909 -11.617 -8.687 1.00 71.07 C ANISOU 3556 CG LYS D 86 7252 12191 7562 -937 27 104 C ATOM 3557 CD LYS D 86 11.606 -12.198 -9.907 1.00 73.08 C ANISOU 3557 CD LYS D 86 7111 12821 7835 -972 327 -53 C ATOM 3558 CE LYS D 86 12.191 -13.569 -9.612 1.00 88.85 C ANISOU 3558 CE LYS D 86 8769 14899 10089 -605 272 -308 C ATOM 3559 NZ LYS D 86 12.856 -14.155 -10.808 1.00 99.80 N ANISOU 3559 NZ LYS D 86 9726 16705 11487 -565 562 -569 N ATOM 3560 N PRO D 87 9.745 -7.229 -8.234 1.00 87.81 N ANISOU 3560 N PRO D 87 10430 13611 9325 -1697 -628 582 N ATOM 3561 CA PRO D 87 9.262 -5.927 -8.723 1.00 90.55 C ANISOU 3561 CA PRO D 87 11155 13702 9549 -1954 -854 718 C ATOM 3562 C PRO D 87 8.943 -5.918 -10.208 1.00 94.49 C ANISOU 3562 C PRO D 87 11730 14305 9868 -2169 -635 829 C ATOM 3563 O PRO D 87 8.271 -4.990 -10.675 1.00 99.14 O ANISOU 3563 O PRO D 87 12713 14614 10342 -2312 -869 932 O ATOM 3564 CB PRO D 87 10.417 -4.972 -8.388 1.00 87.74 C ANISOU 3564 CB PRO D 87 10725 13309 9304 -2342 -1115 865 C ATOM 3565 CG PRO D 87 11.616 -5.853 -8.249 1.00 88.75 C ANISOU 3565 CG PRO D 87 10319 13819 9584 -2367 -873 814 C ATOM 3566 CD PRO D 87 11.103 -7.137 -7.672 1.00 82.37 C ANISOU 3566 CD PRO D 87 9419 13057 8822 -1864 -725 605 C ATOM 3567 N GLU D 88 9.405 -6.915 -10.967 1.00 96.93 N ANISOU 3567 N GLU D 88 11693 14994 10141 -2179 -238 785 N ATOM 3568 CA GLU D 88 9.011 -7.018 -12.367 1.00 94.46 C ANISOU 3568 CA GLU D 88 11478 14814 9600 -2341 -12 851 C ATOM 3569 C GLU D 88 7.553 -7.437 -12.507 1.00 73.10 C ANISOU 3569 C GLU D 88 9067 11876 6830 -1968 -25 739 C ATOM 3570 O GLU D 88 6.913 -7.120 -13.516 1.00 74.34 O ANISOU 3570 O GLU D 88 9494 11955 6797 -2097 -26 823 O ATOM 3571 CB GLU D 88 9.916 -8.009 -13.103 1.00104.64 C ANISOU 3571 CB GLU D 88 12279 16622 10858 -2392 412 743 C ATOM 3572 CG GLU D 88 11.354 -7.542 -13.298 1.00118.99 C ANISOU 3572 CG GLU D 88 13725 18806 12682 -2858 498 843 C ATOM 3573 CD GLU D 88 12.220 -7.740 -12.067 1.00127.61 C ANISOU 3573 CD GLU D 88 14484 19912 14090 -2710 356 735 C ATOM 3574 OE1 GLU D 88 11.681 -8.114 -11.004 1.00127.28 O ANISOU 3574 OE1 GLU D 88 14583 19561 14215 -2292 156 629 O ATOM 3575 OE2 GLU D 88 13.446 -7.524 -12.164 1.00129.97 O ANISOU 3575 OE2 GLU D 88 14369 20562 14451 -3040 439 758 O ATOM 3576 N ASP D 89 7.013 -8.139 -11.512 1.00 72.79 N ANISOU 3576 N ASP D 89 8984 11741 6931 -1546 -56 566 N ATOM 3577 CA ASP D 89 5.633 -8.605 -11.545 1.00 67.98 C ANISOU 3577 CA ASP D 89 8576 10977 6275 -1223 -52 451 C ATOM 3578 C ASP D 89 4.622 -7.505 -11.252 1.00 63.50 C ANISOU 3578 C ASP D 89 8391 10068 5668 -1176 -392 439 C ATOM 3579 O ASP D 89 3.420 -7.791 -11.208 1.00 60.85 O ANISOU 3579 O ASP D 89 8175 9637 5309 -907 -410 306 O ATOM 3580 CB ASP D 89 5.441 -9.752 -10.550 1.00 75.71 C ANISOU 3580 CB ASP D 89 9369 12020 7378 -881 21 308 C ATOM 3581 CG ASP D 89 6.262 -10.974 -10.903 1.00 83.67 C ANISOU 3581 CG ASP D 89 10033 13286 8472 -821 265 248 C ATOM 3582 OD1 ASP D 89 6.943 -10.953 -11.950 1.00 88.70 O ANISOU 3582 OD1 ASP D 89 10519 14135 9046 -1017 447 264 O ATOM 3583 OD2 ASP D 89 6.226 -11.956 -10.134 1.00 84.07 O ANISOU 3583 OD2 ASP D 89 9967 13337 8640 -584 247 168 O ATOM 3584 N THR D 90 5.069 -6.269 -11.047 1.00 70.36 N ANISOU 3584 N THR D 90 9434 10748 6550 -1420 -699 546 N ATOM 3585 CA THR D 90 4.167 -5.153 -10.770 1.00 75.16 C ANISOU 3585 CA THR D 90 10416 10980 7160 -1326 -1123 470 C ATOM 3586 C THR D 90 3.357 -4.852 -12.024 1.00 66.36 C ANISOU 3586 C THR D 90 9588 9702 5926 -1403 -1204 531 C ATOM 3587 O THR D 90 3.865 -4.268 -12.984 1.00 89.57 O ANISOU 3587 O THR D 90 12697 12582 8752 -1816 -1288 777 O ATOM 3588 CB THR D 90 4.954 -3.929 -10.318 1.00 68.77 C ANISOU 3588 CB THR D 90 9758 9951 6419 -1599 -1510 584 C ATOM 3589 OG1 THR D 90 5.715 -4.253 -9.148 1.00 94.22 O ANISOU 3589 OG1 THR D 90 12719 13327 9753 -1516 -1456 518 O ATOM 3590 CG2 THR D 90 4.009 -2.780 -9.999 1.00 70.12 C ANISOU 3590 CG2 THR D 90 10329 9685 6629 -1422 -2038 427 C ATOM 3591 N ALA D 91 2.089 -5.252 -12.018 1.00 67.61 N ANISOU 3591 N ALA D 91 9797 9805 6088 -1040 -1193 320 N ATOM 3592 CA ALA D 91 1.209 -5.045 -13.159 1.00 71.49 C ANISOU 3592 CA ALA D 91 10557 10117 6491 -1051 -1313 340 C ATOM 3593 C ALA D 91 -0.231 -5.200 -12.693 1.00 66.52 C ANISOU 3593 C ALA D 91 9932 9398 5946 -593 -1428 18 C ATOM 3594 O ALA D 91 -0.499 -5.580 -11.551 1.00 72.23 O ANISOU 3594 O ALA D 91 10430 10278 6737 -324 -1332 -190 O ATOM 3595 CB ALA D 91 1.527 -6.022 -14.295 1.00 76.81 C ANISOU 3595 CB ALA D 91 11102 11069 7015 -1221 -904 484 C ATOM 3596 N VAL D 92 -1.157 -4.896 -13.596 1.00 76.18 N ANISOU 3596 N VAL D 92 11404 10398 7142 -534 -1644 -23 N ATOM 3597 CA VAL D 92 -2.580 -5.106 -13.353 1.00 79.85 C ANISOU 3597 CA VAL D 92 11807 10834 7697 -117 -1733 -352 C ATOM 3598 C VAL D 92 -2.940 -6.483 -13.894 1.00 61.08 C ANISOU 3598 C VAL D 92 9210 8733 5263 -68 -1303 -323 C ATOM 3599 O VAL D 92 -2.871 -6.725 -15.102 1.00 80.29 O ANISOU 3599 O VAL D 92 11796 11120 7589 -249 -1246 -152 O ATOM 3600 CB VAL D 92 -3.434 -4.009 -13.997 1.00 66.50 C ANISOU 3600 CB VAL D 92 10499 8702 6067 -28 -2302 -461 C ATOM 3601 CG1 VAL D 92 -4.902 -4.396 -13.958 1.00 65.94 C ANISOU 3601 CG1 VAL D 92 10274 8682 6099 390 -2334 -816 C ATOM 3602 CG2 VAL D 92 -3.217 -2.690 -13.280 1.00 69.41 C ANISOU 3602 CG2 VAL D 92 11080 8749 6545 18 -2818 -577 C ATOM 3603 N TYR D 93 -3.322 -7.387 -12.999 1.00 69.32 N ANISOU 3603 N TYR D 93 9922 10062 6355 148 -1030 -483 N ATOM 3604 CA TYR D 93 -3.617 -8.765 -13.368 1.00 65.12 C ANISOU 3604 CA TYR D 93 9190 9751 5801 178 -682 -445 C ATOM 3605 C TYR D 93 -5.088 -8.889 -13.744 1.00 67.38 C ANISOU 3605 C TYR D 93 9473 9981 6148 404 -807 -658 C ATOM 3606 O TYR D 93 -5.971 -8.561 -12.944 1.00 64.19 O ANISOU 3606 O TYR D 93 8933 9641 5815 638 -933 -933 O ATOM 3607 CB TYR D 93 -3.257 -9.714 -12.226 1.00 67.63 C ANISOU 3607 CB TYR D 93 9201 10363 6131 216 -397 -445 C ATOM 3608 CG TYR D 93 -1.769 -9.952 -12.099 1.00 65.65 C ANISOU 3608 CG TYR D 93 8894 10190 5860 10 -244 -238 C ATOM 3609 CD1 TYR D 93 -0.926 -8.964 -11.606 1.00 57.73 C ANISOU 3609 CD1 TYR D 93 7969 9106 4859 -109 -406 -188 C ATOM 3610 CD2 TYR D 93 -1.206 -11.163 -12.478 1.00 71.19 C ANISOU 3610 CD2 TYR D 93 9445 11037 6566 -47 18 -130 C ATOM 3611 CE1 TYR D 93 0.435 -9.176 -11.492 1.00 59.43 C ANISOU 3611 CE1 TYR D 93 8070 9427 5083 -304 -275 -23 C ATOM 3612 CE2 TYR D 93 0.153 -11.385 -12.367 1.00 67.35 C ANISOU 3612 CE2 TYR D 93 8838 10655 6095 -188 135 -14 C ATOM 3613 CZ TYR D 93 0.968 -10.389 -11.874 1.00 67.59 C ANISOU 3613 CZ TYR D 93 8905 10648 6130 -328 5 45 C ATOM 3614 OH TYR D 93 2.322 -10.607 -11.762 1.00 76.17 O ANISOU 3614 OH TYR D 93 9811 11874 7258 -475 113 138 O ATOM 3615 N TYR D 94 -5.344 -9.354 -14.963 1.00 72.41 N ANISOU 3615 N TYR D 94 10233 10534 6745 340 -776 -565 N ATOM 3616 CA TYR D 94 -6.691 -9.522 -15.487 1.00 66.16 C ANISOU 3616 CA TYR D 94 9446 9663 6030 530 -927 -747 C ATOM 3617 C TYR D 94 -7.067 -10.996 -15.493 1.00 66.96 C ANISOU 3617 C TYR D 94 9292 9995 6155 554 -617 -733 C ATOM 3618 O TYR D 94 -6.222 -11.865 -15.733 1.00 72.75 O ANISOU 3618 O TYR D 94 9994 10827 6822 412 -363 -550 O ATOM 3619 CB TYR D 94 -6.807 -8.958 -16.906 1.00 59.28 C ANISOU 3619 CB TYR D 94 8964 8476 5083 427 -1207 -647 C ATOM 3620 CG TYR D 94 -6.432 -7.499 -17.031 1.00 61.76 C ANISOU 3620 CG TYR D 94 9621 8475 5369 325 -1615 -592 C ATOM 3621 CD1 TYR D 94 -7.375 -6.501 -16.829 1.00 70.40 C ANISOU 3621 CD1 TYR D 94 10835 9293 6622 577 -2106 -858 C ATOM 3622 CD2 TYR D 94 -5.137 -7.121 -17.360 1.00 65.46 C ANISOU 3622 CD2 TYR D 94 10284 8921 5667 -32 -1553 -291 C ATOM 3623 CE1 TYR D 94 -7.038 -5.166 -16.946 1.00 74.84 C ANISOU 3623 CE1 TYR D 94 11771 9477 7188 482 -2590 -802 C ATOM 3624 CE2 TYR D 94 -4.791 -5.788 -17.479 1.00 77.23 C ANISOU 3624 CE2 TYR D 94 12126 10086 7132 -203 -1985 -187 C ATOM 3625 CZ TYR D 94 -5.745 -4.816 -17.272 1.00 79.82 C ANISOU 3625 CZ TYR D 94 12639 10055 7633 57 -2536 -431 C ATOM 3626 OH TYR D 94 -5.404 -3.488 -17.388 1.00 85.52 O ANISOU 3626 OH TYR D 94 13768 10367 8359 -113 -3071 -323 O ATOM 3627 N CYS D 95 -8.340 -11.271 -15.232 1.00 64.80 N ANISOU 3627 N CYS D 95 8822 9808 5990 732 -677 -949 N ATOM 3628 CA CYS D 95 -8.877 -12.622 -15.269 1.00 66.26 C ANISOU 3628 CA CYS D 95 8793 10166 6218 709 -474 -921 C ATOM 3629 C CYS D 95 -9.583 -12.855 -16.598 1.00 66.55 C ANISOU 3629 C CYS D 95 8995 9996 6296 752 -643 -948 C ATOM 3630 O CYS D 95 -10.259 -11.963 -17.119 1.00 75.77 O ANISOU 3630 O CYS D 95 10309 10965 7517 881 -960 -1104 O ATOM 3631 CB CYS D 95 -9.847 -12.857 -14.110 1.00 61.14 C ANISOU 3631 CB CYS D 95 7773 9829 5627 790 -403 -1117 C ATOM 3632 SG CYS D 95 -10.563 -14.515 -14.047 1.00 84.31 S ANISOU 3632 SG CYS D 95 10456 12967 8610 648 -215 -1017 S ATOM 3633 N ALA D 96 -9.420 -14.057 -17.145 1.00 55.29 N ANISOU 3633 N ALA D 96 7569 8583 4856 663 -489 -815 N ATOM 3634 CA ALA D 96 -10.039 -14.428 -18.407 1.00 56.00 C ANISOU 3634 CA ALA D 96 7828 8487 4961 698 -645 -842 C ATOM 3635 C ALA D 96 -10.714 -15.784 -18.263 1.00 62.80 C ANISOU 3635 C ALA D 96 8463 9452 5945 679 -564 -845 C ATOM 3636 O ALA D 96 -10.344 -16.599 -17.414 1.00 67.16 O ANISOU 3636 O ALA D 96 8826 10172 6518 580 -369 -740 O ATOM 3637 CB ALA D 96 -9.017 -14.466 -19.550 1.00 56.20 C ANISOU 3637 CB ALA D 96 8182 8385 4787 588 -600 -691 C ATOM 3638 N ALA D 97 -11.713 -16.017 -19.110 1.00 59.26 N ANISOU 3638 N ALA D 97 8067 8866 5584 747 -773 -946 N ATOM 3639 CA ALA D 97 -12.481 -17.251 -19.048 1.00 60.71 C ANISOU 3639 CA ALA D 97 8049 9109 5911 690 -772 -942 C ATOM 3640 C ALA D 97 -13.157 -17.488 -20.390 1.00 70.89 C ANISOU 3640 C ALA D 97 9548 10147 7242 766 -1034 -1019 C ATOM 3641 O ALA D 97 -13.583 -16.539 -21.052 1.00 71.84 O ANISOU 3641 O ALA D 97 9843 10107 7344 885 -1275 -1141 O ATOM 3642 CB ALA D 97 -13.523 -17.200 -17.925 1.00 58.76 C ANISOU 3642 CB ALA D 97 7377 9152 5796 659 -746 -1063 C ATOM 3643 N VAL D 98 -13.247 -18.757 -20.780 1.00 67.27 N ANISOU 3643 N VAL D 98 9104 9613 6841 699 -1048 -951 N ATOM 3644 CA VAL D 98 -13.917 -19.171 -22.007 1.00 63.07 C ANISOU 3644 CA VAL D 98 8766 8844 6354 765 -1317 -1033 C ATOM 3645 C VAL D 98 -15.121 -20.014 -21.616 1.00 69.62 C ANISOU 3645 C VAL D 98 9278 9734 7441 669 -1442 -1063 C ATOM 3646 O VAL D 98 -14.965 -21.091 -21.028 1.00 77.09 O ANISOU 3646 O VAL D 98 10088 10742 8460 504 -1353 -921 O ATOM 3647 CB VAL D 98 -12.979 -19.955 -22.938 1.00 73.52 C ANISOU 3647 CB VAL D 98 10402 10017 7514 784 -1281 -981 C ATOM 3648 CG1 VAL D 98 -13.729 -20.417 -24.179 1.00 62.09 C ANISOU 3648 CG1 VAL D 98 9174 8330 6089 857 -1586 -1091 C ATOM 3649 CG2 VAL D 98 -11.777 -19.105 -23.319 1.00 76.64 C ANISOU 3649 CG2 VAL D 98 11044 10460 7617 799 -1111 -945 C ATOM 3650 N ALA D 99 -16.317 -19.529 -21.939 1.00 56.57 N ANISOU 3650 N ALA D 99 6941 10226 4327 -136 14 -420 N ATOM 3651 CA ALA D 99 -17.556 -20.221 -21.612 1.00 75.64 C ANISOU 3651 CA ALA D 99 9198 12970 6572 -306 311 -595 C ATOM 3652 C ALA D 99 -18.422 -20.316 -22.858 1.00 58.00 C ANISOU 3652 C ALA D 99 6532 10953 4553 -106 385 -669 C ATOM 3653 O ALA D 99 -18.698 -19.300 -23.505 1.00 58.22 O ANISOU 3653 O ALA D 99 6395 10945 4782 224 293 -776 O ATOM 3654 CB ALA D 99 -18.314 -19.503 -20.490 1.00 62.30 C ANISOU 3654 CB ALA D 99 7548 11457 4664 -329 551 -932 C ATOM 3655 N TYR D 100 -18.852 -21.542 -23.191 1.00 57.57 N ANISOU 3655 N TYR D 100 6342 11079 4455 -321 487 -603 N ATOM 3656 CA TYR D 100 -19.686 -21.784 -24.356 1.00 68.86 C ANISOU 3656 CA TYR D 100 7369 12720 6076 -164 559 -663 C ATOM 3657 C TYR D 100 -21.147 -21.951 -23.951 1.00 80.38 C ANISOU 3657 C TYR D 100 8566 14574 7401 -245 901 -1011 C ATOM 3658 O TYR D 100 -21.444 -22.434 -22.854 1.00 77.49 O ANISOU 3658 O TYR D 100 8361 14375 6706 -618 1114 -1117 O ATOM 3659 CB TYR D 100 -19.222 -23.039 -25.105 1.00 70.36 C ANISOU 3659 CB TYR D 100 7516 12875 6342 -325 433 -413 C ATOM 3660 CG TYR D 100 -17.809 -22.954 -25.637 1.00 52.00 C ANISOU 3660 CG TYR D 100 5305 10273 4179 -266 123 -214 C ATOM 3661 CD1 TYR D 100 -17.495 -22.111 -26.695 1.00 67.28 C ANISOU 3661 CD1 TYR D 100 7095 12169 6299 -52 11 -183 C ATOM 3662 CD2 TYR D 100 -16.792 -23.725 -25.091 1.00 51.55 C ANISOU 3662 CD2 TYR D 100 5507 10001 4078 -469 -94 -103 C ATOM 3663 CE1 TYR D 100 -16.206 -22.032 -27.188 1.00 72.37 C ANISOU 3663 CE1 TYR D 100 7794 12667 7036 -102 -211 -81 C ATOM 3664 CE2 TYR D 100 -15.500 -23.654 -25.578 1.00 63.00 C ANISOU 3664 CE2 TYR D 100 6957 11269 5709 -414 -365 -55 C ATOM 3665 CZ TYR D 100 -15.213 -22.806 -26.626 1.00 67.02 C ANISOU 3665 CZ TYR D 100 7262 11845 6357 -260 -372 -62 C ATOM 3666 OH TYR D 100 -13.928 -22.733 -27.113 1.00 66.49 O ANISOU 3666 OH TYR D 100 7150 11699 6415 -307 -581 -90 O ATOM 3667 N PRO D 101 -22.077 -21.556 -24.811 1.00 89.68 N ANISOU 3667 N PRO D 101 9347 15921 8807 52 940 -1230 N ATOM 3668 CA PRO D 101 -23.503 -21.719 -24.512 1.00 81.02 C ANISOU 3668 CA PRO D 101 7887 15263 7636 -4 1267 -1678 C ATOM 3669 C PRO D 101 -23.927 -23.175 -24.681 1.00 77.72 C ANISOU 3669 C PRO D 101 7392 15088 7051 -399 1459 -1549 C ATOM 3670 O PRO D 101 -23.125 -24.053 -24.994 1.00 80.35 O ANISOU 3670 O PRO D 101 7958 15212 7360 -580 1288 -1137 O ATOM 3671 CB PRO D 101 -24.191 -20.814 -25.544 1.00 94.22 C ANISOU 3671 CB PRO D 101 9196 16909 9694 512 1083 -1926 C ATOM 3672 CG PRO D 101 -23.094 -19.982 -26.156 1.00 94.14 C ANISOU 3672 CG PRO D 101 9477 16431 9862 759 668 -1590 C ATOM 3673 CD PRO D 101 -21.862 -20.813 -26.062 1.00 88.65 C ANISOU 3673 CD PRO D 101 9107 15577 8999 430 642 -1127 C ATOM 3674 N ASP D 102 -25.218 -23.418 -24.467 1.00 81.89 N ANISOU 3674 N ASP D 102 7561 16074 7480 -532 1790 -1969 N ATOM 3675 CA ASP D 102 -25.769 -24.750 -24.670 1.00 81.10 C ANISOU 3675 CA ASP D 102 7430 16108 7276 -922 1901 -1841 C ATOM 3676 C ASP D 102 -25.830 -25.069 -26.157 1.00 83.53 C ANISOU 3676 C ASP D 102 7496 16304 7937 -603 1702 -1639 C ATOM 3677 O ASP D 102 -26.198 -24.220 -26.973 1.00 91.38 O ANISOU 3677 O ASP D 102 8196 17263 9260 -129 1581 -1821 O ATOM 3678 CB ASP D 102 -27.163 -24.853 -24.056 1.00 79.73 C ANISOU 3678 CB ASP D 102 7051 16186 7056 -1164 2140 -2302 C ATOM 3679 CG ASP D 102 -27.651 -26.286 -23.954 1.00 95.20 C ANISOU 3679 CG ASP D 102 9142 18220 8811 -1706 2214 -2132 C ATOM 3680 OD1 ASP D 102 -26.837 -27.210 -24.166 1.00 98.68 O ANISOU 3680 OD1 ASP D 102 9890 18492 9112 -1926 2060 -1667 O ATOM 3681 OD2 ASP D 102 -28.848 -26.489 -23.664 1.00107.42 O ANISOU 3681 OD2 ASP D 102 10473 20016 10325 -1922 2393 -2500 O ATOM 3682 N ILE D 103 -25.484 -26.308 -26.501 1.00 83.15 N ANISOU 3682 N ILE D 103 7599 16184 7811 -882 1620 -1282 N ATOM 3683 CA ILE D 103 -25.372 -26.752 -27.890 1.00 74.48 C ANISOU 3683 CA ILE D 103 6332 14947 7020 -643 1410 -1059 C ATOM 3684 C ILE D 103 -24.468 -25.775 -28.634 1.00 73.23 C ANISOU 3684 C ILE D 103 6137 14595 7091 -232 1179 -929 C ATOM 3685 O ILE D 103 -24.935 -25.061 -29.533 1.00 70.12 O ANISOU 3685 O ILE D 103 5491 14197 6957 125 1089 -1053 O ATOM 3686 CB ILE D 103 -26.751 -26.865 -28.563 1.00 69.53 C ANISOU 3686 CB ILE D 103 5440 14353 6623 -503 1452 -1301 C ATOM 3687 CG1 ILE D 103 -27.778 -27.469 -27.602 1.00 65.46 C ANISOU 3687 CG1 ILE D 103 4942 14069 5861 -931 1708 -1556 C ATOM 3688 CG2 ILE D 103 -26.661 -27.708 -29.827 1.00 58.11 C ANISOU 3688 CG2 ILE D 103 3968 12735 5378 -426 1257 -1029 C ATOM 3689 CD1 ILE D 103 -27.472 -28.886 -27.179 1.00 65.38 C ANISOU 3689 CD1 ILE D 103 5210 14092 5538 -1475 1712 -1267 C ATOM 3690 N PRO D 104 -23.181 -25.701 -28.300 1.00 69.22 N ANISOU 3690 N PRO D 104 5989 13779 6532 -301 968 -677 N ATOM 3691 CA PRO D 104 -22.332 -24.653 -28.875 1.00 59.72 C ANISOU 3691 CA PRO D 104 4863 12312 5517 -8 721 -577 C ATOM 3692 C PRO D 104 -21.951 -24.934 -30.321 1.00 65.88 C ANISOU 3692 C PRO D 104 5479 13048 6504 87 536 -398 C ATOM 3693 O PRO D 104 -21.597 -26.057 -30.690 1.00 62.94 O ANISOU 3693 O PRO D 104 5057 12707 6150 -80 488 -268 O ATOM 3694 CB PRO D 104 -21.098 -24.670 -27.965 1.00 52.45 C ANISOU 3694 CB PRO D 104 4339 11139 4451 -185 591 -421 C ATOM 3695 CG PRO D 104 -21.014 -26.087 -27.506 1.00 52.60 C ANISOU 3695 CG PRO D 104 4486 11182 4317 -536 589 -312 C ATOM 3696 CD PRO D 104 -22.436 -26.569 -27.368 1.00 54.89 C ANISOU 3696 CD PRO D 104 4558 11820 4478 -683 891 -491 C ATOM 3697 N THR D 105 -22.029 -23.890 -31.142 1.00 68.47 N ANISOU 3697 N THR D 105 5751 13290 6975 330 386 -414 N ATOM 3698 CA THR D 105 -21.554 -23.942 -32.518 1.00 49.03 C ANISOU 3698 CA THR D 105 3209 10797 4622 321 202 -246 C ATOM 3699 C THR D 105 -20.126 -23.436 -32.658 1.00 64.97 C ANISOU 3699 C THR D 105 5468 12633 6584 192 13 -98 C ATOM 3700 O THR D 105 -19.565 -23.503 -33.757 1.00 88.91 O ANISOU 3700 O THR D 105 8434 15712 9635 63 -102 -4 O ATOM 3701 CB THR D 105 -22.475 -23.126 -33.433 1.00 61.32 C ANISOU 3701 CB THR D 105 4651 12334 6314 557 60 -325 C ATOM 3702 OG1 THR D 105 -22.445 -21.749 -33.039 1.00 70.98 O ANISOU 3702 OG1 THR D 105 6110 13314 7546 738 -141 -404 O ATOM 3703 CG2 THR D 105 -23.904 -23.640 -33.352 1.00 75.87 C ANISOU 3703 CG2 THR D 105 6166 14408 8252 695 252 -563 C ATOM 3704 N TYR D 106 -19.537 -22.930 -31.573 1.00 61.30 N ANISOU 3704 N TYR D 106 5262 12002 6025 181 -1 -112 N ATOM 3705 CA TYR D 106 -18.170 -22.414 -31.537 1.00 58.51 C ANISOU 3705 CA TYR D 106 5128 11488 5613 46 -164 -21 C ATOM 3706 C TYR D 106 -17.972 -21.232 -32.481 1.00 59.62 C ANISOU 3706 C TYR D 106 5396 11529 5727 28 -374 68 C ATOM 3707 O TYR D 106 -16.846 -20.950 -32.905 1.00 67.50 O ANISOU 3707 O TYR D 106 6495 12512 6641 -213 -485 135 O ATOM 3708 CB TYR D 106 -17.153 -23.523 -31.828 1.00 56.89 C ANISOU 3708 CB TYR D 106 4788 11377 5450 -164 -198 -24 C ATOM 3709 CG TYR D 106 -17.307 -24.715 -30.910 1.00 63.39 C ANISOU 3709 CG TYR D 106 5612 12189 6285 -194 -145 -68 C ATOM 3710 CD1 TYR D 106 -17.911 -25.884 -31.353 1.00 76.99 C ANISOU 3710 CD1 TYR D 106 7102 14071 8081 -228 -95 -84 C ATOM 3711 CD2 TYR D 106 -16.869 -24.662 -29.592 1.00 61.97 C ANISOU 3711 CD2 TYR D 106 5728 11809 6007 -237 -190 -73 C ATOM 3712 CE1 TYR D 106 -18.061 -26.973 -30.514 1.00 82.50 C ANISOU 3712 CE1 TYR D 106 7904 14705 8738 -341 -131 -86 C ATOM 3713 CE2 TYR D 106 -17.016 -25.747 -28.746 1.00 73.99 C ANISOU 3713 CE2 TYR D 106 7374 13269 7470 -367 -225 -71 C ATOM 3714 CZ TYR D 106 -17.612 -26.899 -29.212 1.00 76.31 C ANISOU 3714 CZ TYR D 106 7475 13698 7819 -437 -214 -68 C ATOM 3715 OH TYR D 106 -17.760 -27.979 -28.373 1.00 79.44 O ANISOU 3715 OH TYR D 106 8092 13982 8109 -647 -330 -30 O ATOM 3716 N PHE D 107 -19.056 -20.536 -32.812 1.00 62.41 N ANISOU 3716 N PHE D 107 5761 11809 6141 243 -474 33 N ATOM 3717 CA PHE D 107 -19.015 -19.282 -33.554 1.00 69.38 C ANISOU 3717 CA PHE D 107 6910 12466 6983 229 -818 134 C ATOM 3718 C PHE D 107 -19.720 -18.224 -32.720 1.00 76.37 C ANISOU 3718 C PHE D 107 7964 13096 7958 576 -985 -29 C ATOM 3719 O PHE D 107 -20.887 -18.398 -32.351 1.00 84.22 O ANISOU 3719 O PHE D 107 8720 14175 9107 873 -887 -281 O ATOM 3720 CB PHE D 107 -19.684 -19.419 -34.924 1.00 86.45 C ANISOU 3720 CB PHE D 107 8959 14699 9189 188 -960 199 C ATOM 3721 CG PHE D 107 -18.826 -20.090 -35.960 1.00 86.69 C ANISOU 3721 CG PHE D 107 8889 14969 9081 -228 -885 330 C ATOM 3722 CD1 PHE D 107 -18.717 -21.469 -36.003 1.00 83.25 C ANISOU 3722 CD1 PHE D 107 8077 14836 8718 -276 -593 246 C ATOM 3723 CD2 PHE D 107 -18.139 -19.341 -36.900 1.00 87.65 C ANISOU 3723 CD2 PHE D 107 9298 15028 8978 -617 -1135 495 C ATOM 3724 CE1 PHE D 107 -17.931 -22.089 -36.958 1.00 70.52 C ANISOU 3724 CE1 PHE D 107 6294 13483 7018 -626 -541 248 C ATOM 3725 CE2 PHE D 107 -17.353 -19.954 -37.858 1.00 74.16 C ANISOU 3725 CE2 PHE D 107 7427 13643 7108 -1064 -1015 508 C ATOM 3726 CZ PHE D 107 -17.249 -21.329 -37.886 1.00 69.61 C ANISOU 3726 CZ PHE D 107 6390 13391 6667 -1029 -713 346 C ATOM 3727 N ASP D 108 -19.014 -17.138 -32.417 1.00 75.94 N ANISOU 3727 N ASP D 108 8282 12762 7811 525 -1239 55 N ATOM 3728 CA ASP D 108 -19.571 -16.050 -31.618 1.00 77.02 C ANISOU 3728 CA ASP D 108 8586 12623 8055 874 -1468 -149 C ATOM 3729 C ASP D 108 -19.067 -14.738 -32.200 1.00 80.76 C ANISOU 3729 C ASP D 108 9545 12696 8446 761 -2008 45 C ATOM 3730 O ASP D 108 -17.891 -14.398 -32.044 1.00 88.43 O ANISOU 3730 O ASP D 108 10795 13587 9215 454 -2035 244 O ATOM 3731 CB ASP D 108 -19.182 -16.187 -30.145 1.00 76.43 C ANISOU 3731 CB ASP D 108 8510 12608 7922 924 -1179 -282 C ATOM 3732 CG ASP D 108 -20.031 -15.321 -29.229 1.00 84.40 C ANISOU 3732 CG ASP D 108 9517 13482 9067 1319 -1294 -647 C ATOM 3733 OD1 ASP D 108 -20.470 -14.234 -29.659 1.00 90.81 O ANISOU 3733 OD1 ASP D 108 10492 13984 10027 1561 -1771 -743 O ATOM 3734 OD2 ASP D 108 -20.259 -15.731 -28.072 1.00 93.95 O ANISOU 3734 OD2 ASP D 108 10575 14894 10229 1362 -947 -875 O ATOM 3735 N TYR D 109 -19.954 -14.009 -32.873 1.00 68.79 N ANISOU 3735 N TYR D 109 8154 10906 7078 980 -2488 -26 N ATOM 3736 CA TYR D 109 -19.628 -12.712 -33.445 1.00 77.46 C ANISOU 3736 CA TYR D 109 9825 11522 8084 848 -3151 172 C ATOM 3737 C TYR D 109 -19.873 -11.567 -32.471 1.00 84.55 C ANISOU 3737 C TYR D 109 10937 12037 9151 1252 -3517 -78 C ATOM 3738 O TYR D 109 -19.792 -10.401 -32.870 1.00104.81 O ANISOU 3738 O TYR D 109 14021 14102 11700 1228 -4209 38 O ATOM 3739 CB TYR D 109 -20.429 -12.489 -34.729 1.00 79.20 C ANISOU 3739 CB TYR D 109 10176 11535 8380 854 -3645 239 C ATOM 3740 CG TYR D 109 -20.276 -13.605 -35.738 1.00 71.88 C ANISOU 3740 CG TYR D 109 9014 11002 7294 471 -3296 442 C ATOM 3741 CD1 TYR D 109 -19.151 -13.685 -36.547 1.00 76.36 C ANISOU 3741 CD1 TYR D 109 9849 11691 7474 -204 -3258 797 C ATOM 3742 CD2 TYR D 109 -21.257 -14.577 -35.882 1.00 75.92 C ANISOU 3742 CD2 TYR D 109 9007 11806 8032 754 -2998 223 C ATOM 3743 CE1 TYR D 109 -19.005 -14.703 -37.470 1.00 66.01 C ANISOU 3743 CE1 TYR D 109 8269 10779 6030 -545 -2941 896 C ATOM 3744 CE2 TYR D 109 -21.120 -15.599 -36.803 1.00 65.01 C ANISOU 3744 CE2 TYR D 109 7408 10769 6525 428 -2710 389 C ATOM 3745 CZ TYR D 109 -19.993 -15.656 -37.594 1.00 64.33 C ANISOU 3745 CZ TYR D 109 7570 10794 6078 -200 -2689 709 C ATOM 3746 OH TYR D 109 -19.852 -16.671 -38.513 1.00 71.37 O ANISOU 3746 OH TYR D 109 8194 12067 6857 -516 -2406 790 O ATOM 3747 N ASP D 110 -20.168 -11.873 -31.210 1.00 78.76 N ANISOU 3747 N ASP D 110 9849 11521 8554 1578 -3107 -427 N ATOM 3748 CA ASP D 110 -20.421 -10.868 -30.185 1.00 79.36 C ANISOU 3748 CA ASP D 110 10034 11324 8795 1972 -3375 -763 C ATOM 3749 C ASP D 110 -19.320 -10.782 -29.142 1.00 73.00 C ANISOU 3749 C ASP D 110 9394 10567 7777 1778 -3074 -639 C ATOM 3750 O ASP D 110 -18.906 -9.678 -28.781 1.00 74.17 O ANISOU 3750 O ASP D 110 9936 10329 7918 1847 -3491 -623 O ATOM 3751 CB ASP D 110 -21.756 -11.154 -29.487 1.00 94.60 C ANISOU 3751 CB ASP D 110 11404 13510 11030 2477 -3160 -1396 C ATOM 3752 CG ASP D 110 -22.087 -10.130 -28.421 1.00105.68 C ANISOU 3752 CG ASP D 110 12822 14707 12626 2903 -3419 -1882 C ATOM 3753 OD1 ASP D 110 -22.368 -8.966 -28.778 1.00112.06 O ANISOU 3753 OD1 ASP D 110 13928 14993 13658 3198 -4197 -2015 O ATOM 3754 OD2 ASP D 110 -22.069 -10.489 -27.225 1.00107.63 O ANISOU 3754 OD2 ASP D 110 12808 15294 12790 2919 -2891 -2147 O ATOM 3755 N SER D 111 -18.830 -11.920 -28.647 1.00 77.74 N ANISOU 3755 N SER D 111 9736 11587 8216 1540 -2428 -555 N ATOM 3756 CA SER D 111 -17.769 -11.920 -27.650 1.00 82.44 C ANISOU 3756 CA SER D 111 10495 12200 8627 1359 -2188 -450 C ATOM 3757 C SER D 111 -16.748 -13.033 -27.844 1.00 75.29 C ANISOU 3757 C SER D 111 9514 11570 7522 922 -1798 -159 C ATOM 3758 O SER D 111 -15.846 -13.162 -27.010 1.00 68.12 O ANISOU 3758 O SER D 111 8719 10670 6494 781 -1626 -103 O ATOM 3759 CB SER D 111 -18.366 -12.021 -26.235 1.00 90.62 C ANISOU 3759 CB SER D 111 11299 13404 9730 1647 -1884 -873 C ATOM 3760 OG SER D 111 -19.166 -10.890 -25.938 1.00103.94 O ANISOU 3760 OG SER D 111 13010 14844 11638 2084 -2282 -1267 O ATOM 3761 N ASP D 112 -16.859 -13.835 -28.907 1.00 68.52 N ANISOU 3761 N ASP D 112 8458 10922 6654 729 -1699 -23 N ATOM 3762 CA ASP D 112 -15.926 -14.927 -29.195 1.00 75.03 C ANISOU 3762 CA ASP D 112 9137 12016 7354 360 -1400 144 C ATOM 3763 C ASP D 112 -15.848 -15.928 -28.044 1.00 74.57 C ANISOU 3763 C ASP D 112 8890 12145 7300 407 -1022 12 C ATOM 3764 O ASP D 112 -14.817 -16.574 -27.837 1.00 87.70 O ANISOU 3764 O ASP D 112 10548 13881 8894 172 -912 88 O ATOM 3765 CB ASP D 112 -14.531 -14.391 -29.539 1.00 77.51 C ANISOU 3765 CB ASP D 112 9743 12223 7483 -28 -1568 352 C ATOM 3766 CG ASP D 112 -13.677 -15.411 -30.270 1.00 78.42 C ANISOU 3766 CG ASP D 112 9613 12664 7519 -414 -1360 404 C ATOM 3767 OD1 ASP D 112 -14.208 -16.484 -30.625 1.00 74.01 O ANISOU 3767 OD1 ASP D 112 8711 12350 7060 -357 -1151 336 O ATOM 3768 OD2 ASP D 112 -12.477 -15.142 -30.486 1.00 78.17 O ANISOU 3768 OD2 ASP D 112 9700 12665 7337 -778 -1413 456 O ATOM 3769 N ASN D 113 -16.942 -16.065 -27.292 1.00 71.80 N ANISOU 3769 N ASN D 113 8390 11874 7016 673 -863 -229 N ATOM 3770 CA ASN D 113 -17.018 -16.921 -26.108 1.00 65.57 C ANISOU 3770 CA ASN D 113 7532 11246 6136 616 -542 -347 C ATOM 3771 C ASN D 113 -15.903 -16.629 -25.109 1.00 70.93 C ANISOU 3771 C ASN D 113 8526 11732 6691 501 -585 -273 C ATOM 3772 O ASN D 113 -15.517 -17.505 -24.330 1.00 69.77 O ANISOU 3772 O ASN D 113 8431 11639 6440 326 -436 -256 O ATOM 3773 CB ASN D 113 -17.006 -18.403 -26.492 1.00 58.28 C ANISOU 3773 CB ASN D 113 6380 10563 5202 407 -342 -261 C ATOM 3774 CG ASN D 113 -18.149 -18.771 -27.413 1.00 69.36 C ANISOU 3774 CG ASN D 113 7459 12174 6722 515 -270 -341 C ATOM 3775 OD1 ASN D 113 -17.935 -19.198 -28.546 1.00 60.20 O ANISOU 3775 OD1 ASN D 113 6167 11079 5626 417 -338 -196 O ATOM 3776 ND2 ASN D 113 -19.376 -18.602 -26.931 1.00 73.89 N ANISOU 3776 ND2 ASN D 113 7867 12886 7320 702 -127 -629 N ATOM 3777 N PHE D 114 -15.386 -15.404 -25.117 1.00 81.01 N ANISOU 3777 N PHE D 114 10060 12746 7976 580 -849 -224 N ATOM 3778 CA PHE D 114 -14.273 -15.000 -24.270 1.00 55.90 C ANISOU 3778 CA PHE D 114 7183 9363 4696 480 -927 -152 C ATOM 3779 C PHE D 114 -14.721 -13.844 -23.390 1.00 77.18 C ANISOU 3779 C PHE D 114 10065 11877 7385 739 -1030 -341 C ATOM 3780 O PHE D 114 -15.325 -12.883 -23.880 1.00 69.80 O ANISOU 3780 O PHE D 114 9150 10806 6565 968 -1284 -432 O ATOM 3781 CB PHE D 114 -13.066 -14.588 -25.119 1.00 57.09 C ANISOU 3781 CB PHE D 114 7471 9391 4829 251 -1156 61 C ATOM 3782 CG PHE D 114 -11.753 -14.683 -24.400 1.00 54.11 C ANISOU 3782 CG PHE D 114 7269 8905 4386 76 -1181 100 C ATOM 3783 CD1 PHE D 114 -11.304 -13.643 -23.604 1.00 56.98 C ANISOU 3783 CD1 PHE D 114 7956 9007 4688 144 -1333 104 C ATOM 3784 CD2 PHE D 114 -10.960 -15.810 -24.532 1.00 57.74 C ANISOU 3784 CD2 PHE D 114 7555 9501 4883 -127 -1110 87 C ATOM 3785 CE1 PHE D 114 -10.092 -13.731 -22.946 1.00 54.67 C ANISOU 3785 CE1 PHE D 114 7815 8603 4354 -5 -1380 119 C ATOM 3786 CE2 PHE D 114 -9.749 -15.904 -23.878 1.00 64.67 C ANISOU 3786 CE2 PHE D 114 8565 10248 5757 -245 -1210 49 C ATOM 3787 CZ PHE D 114 -9.314 -14.863 -23.085 1.00 53.17 C ANISOU 3787 CZ PHE D 114 7436 8543 4223 -193 -1329 78 C ATOM 3788 N TYR D 115 -14.426 -13.933 -22.095 1.00 58.90 N ANISOU 3788 N TYR D 115 7905 9532 4942 701 -895 -428 N ATOM 3789 CA TYR D 115 -14.861 -12.934 -21.131 1.00 78.15 C ANISOU 3789 CA TYR D 115 10473 11864 7359 931 -943 -689 C ATOM 3790 C TYR D 115 -13.695 -12.546 -20.235 1.00 79.86 C ANISOU 3790 C TYR D 115 11053 11837 7454 817 -1036 -565 C ATOM 3791 O TYR D 115 -12.906 -13.401 -19.821 1.00 71.15 O ANISOU 3791 O TYR D 115 10053 10741 6240 560 -937 -412 O ATOM 3792 CB TYR D 115 -16.034 -13.456 -20.294 1.00 79.63 C ANISOU 3792 CB TYR D 115 10423 12385 7447 957 -589 -1054 C ATOM 3793 CG TYR D 115 -17.180 -13.973 -21.134 1.00 80.81 C ANISOU 3793 CG TYR D 115 10170 12813 7720 1045 -465 -1209 C ATOM 3794 CD1 TYR D 115 -17.256 -15.314 -21.492 1.00 76.21 C ANISOU 3794 CD1 TYR D 115 9441 12457 7059 777 -235 -1043 C ATOM 3795 CD2 TYR D 115 -18.179 -13.119 -21.582 1.00 78.19 C ANISOU 3795 CD2 TYR D 115 9614 12479 7617 1420 -647 -1547 C ATOM 3796 CE1 TYR D 115 -18.298 -15.790 -22.266 1.00 66.81 C ANISOU 3796 CE1 TYR D 115 7882 11522 5982 852 -120 -1180 C ATOM 3797 CE2 TYR D 115 -19.226 -13.587 -22.356 1.00 74.04 C ANISOU 3797 CE2 TYR D 115 8708 12194 7231 1519 -566 -1717 C ATOM 3798 CZ TYR D 115 -19.280 -14.922 -22.695 1.00 72.04 C ANISOU 3798 CZ TYR D 115 8307 12201 6865 1220 -267 -1517 C ATOM 3799 OH TYR D 115 -20.319 -15.393 -23.465 1.00 76.11 O ANISOU 3799 OH TYR D 115 8442 12957 7518 1313 -182 -1683 O ATOM 3800 N TRP D 116 -13.591 -11.254 -19.943 1.00 85.49 N ANISOU 3800 N TRP D 116 11972 12295 8215 1028 -1295 -655 N ATOM 3801 CA TRP D 116 -12.503 -10.697 -19.152 1.00 83.11 C ANISOU 3801 CA TRP D 116 12026 11731 7819 952 -1429 -545 C ATOM 3802 C TRP D 116 -13.011 -10.277 -17.777 1.00 92.67 C ANISOU 3802 C TRP D 116 13312 12970 8929 1102 -1304 -877 C ATOM 3803 O TRP D 116 -14.170 -10.497 -17.414 1.00106.95 O ANISOU 3803 O TRP D 116 14858 15066 10713 1206 -1067 -1232 O ATOM 3804 CB TRP D 116 -11.863 -9.510 -19.876 1.00 78.86 C ANISOU 3804 CB TRP D 116 11735 10860 7368 994 -1860 -365 C ATOM 3805 CG TRP D 116 -11.080 -9.885 -21.092 1.00 84.43 C ANISOU 3805 CG TRP D 116 12418 11595 8068 685 -1941 -63 C ATOM 3806 CD1 TRP D 116 -11.548 -9.992 -22.369 1.00 61.60 C ANISOU 3806 CD1 TRP D 116 9372 8795 5239 633 -2031 20 C ATOM 3807 CD2 TRP D 116 -9.683 -10.195 -21.149 1.00 77.77 C ANISOU 3807 CD2 TRP D 116 11674 10730 7143 355 -1941 120 C ATOM 3808 NE1 TRP D 116 -10.529 -10.352 -23.217 1.00 66.06 N ANISOU 3808 NE1 TRP D 116 9932 9443 5724 244 -2041 240 N ATOM 3809 CE2 TRP D 116 -9.373 -10.483 -22.493 1.00 70.03 C ANISOU 3809 CE2 TRP D 116 10550 9899 6161 83 -1984 262 C ATOM 3810 CE3 TRP D 116 -8.664 -10.259 -20.194 1.00 75.33 C ANISOU 3810 CE3 TRP D 116 11541 10305 6774 260 -1926 125 C ATOM 3811 CZ2 TRP D 116 -8.089 -10.830 -22.905 1.00 70.82 C ANISOU 3811 CZ2 TRP D 116 10602 10101 6205 -288 -1975 328 C ATOM 3812 CZ3 TRP D 116 -7.389 -10.604 -20.605 1.00 80.03 C ANISOU 3812 CZ3 TRP D 116 12103 10943 7361 -54 -1970 207 C ATOM 3813 CH2 TRP D 116 -7.113 -10.885 -21.949 1.00 57.34 C ANISOU 3813 CH2 TRP D 116 9012 8284 4492 -328 -1976 269 C ATOM 3814 N GLY D 117 -12.113 -9.659 -17.007 1.00 79.25 N ANISOU 3814 N GLY D 117 11949 11010 7152 1076 -1449 -803 N ATOM 3815 CA GLY D 117 -12.454 -9.104 -15.715 1.00 68.79 C ANISOU 3815 CA GLY D 117 10733 9691 5714 1198 -1370 -1125 C ATOM 3816 C GLY D 117 -12.060 -7.640 -15.633 1.00 72.05 C ANISOU 3816 C GLY D 117 11394 9728 6254 1462 -1781 -1160 C ATOM 3817 O GLY D 117 -11.473 -7.079 -16.561 1.00 84.38 O ANISOU 3817 O GLY D 117 13106 11015 7940 1470 -2134 -886 O ATOM 3818 N GLN D 118 -12.394 -7.038 -14.490 1.00 78.76 N ANISOU 3818 N GLN D 118 12306 10587 7032 1620 -1739 -1520 N ATOM 3819 CA GLN D 118 -12.098 -5.623 -14.288 1.00 88.89 C ANISOU 3819 CA GLN D 118 13834 11489 8450 1909 -2174 -1612 C ATOM 3820 C GLN D 118 -10.598 -5.387 -14.148 1.00 89.45 C ANISOU 3820 C GLN D 118 14337 11220 8432 1684 -2362 -1167 C ATOM 3821 O GLN D 118 -10.022 -4.553 -14.856 1.00 81.23 O ANISOU 3821 O GLN D 118 13523 9836 7505 1720 -2787 -934 O ATOM 3822 CB GLN D 118 -12.844 -5.103 -13.059 1.00106.87 C ANISOU 3822 CB GLN D 118 16002 13928 10677 2130 -2048 -2202 C ATOM 3823 N GLY D 119 -9.950 -6.111 -13.240 1.00 94.98 N ANISOU 3823 N GLY D 119 15179 11999 8910 1409 -2091 -1062 N ATOM 3824 CA GLY D 119 -8.513 -5.936 -13.029 1.00 87.00 C ANISOU 3824 CA GLY D 119 14523 10682 7850 1219 -2278 -729 C ATOM 3825 C GLY D 119 -8.222 -5.603 -11.580 1.00 89.27 C ANISOU 3825 C GLY D 119 15083 10868 7970 1225 -2233 -882 C ATOM 3826 O GLY D 119 -8.879 -4.770 -10.956 1.00 85.68 O ANISOU 3826 O GLY D 119 14626 10411 7517 1484 -2274 -1233 O ATOM 3827 N THR D 120 -7.216 -6.279 -11.032 1.00 78.89 N ANISOU 3827 N THR D 120 13995 9458 6522 943 -2189 -664 N ATOM 3828 CA THR D 120 -6.741 -6.032 -9.677 1.00 93.60 C ANISOU 3828 CA THR D 120 16199 11165 8200 881 -2200 -734 C ATOM 3829 C THR D 120 -5.274 -5.633 -9.732 1.00 78.29 C ANISOU 3829 C THR D 120 14537 8853 6357 813 -2522 -460 C ATOM 3830 O THR D 120 -4.472 -6.293 -10.402 1.00 66.86 O ANISOU 3830 O THR D 120 13021 7373 5008 626 -2597 -246 O ATOM 3831 CB THR D 120 -6.921 -7.264 -8.784 1.00115.23 C ANISOU 3831 CB THR D 120 19044 14090 10649 548 -1927 -762 C ATOM 3832 OG1 THR D 120 -6.296 -8.400 -9.394 1.00124.31 O ANISOU 3832 OG1 THR D 120 20156 15202 11873 327 -1988 -488 O ATOM 3833 CG2 THR D 120 -8.398 -7.555 -8.565 1.00123.57 C ANISOU 3833 CG2 THR D 120 19827 15591 11533 526 -1554 -1114 C ATOM 3834 N GLN D 121 -4.930 -4.556 -9.032 1.00 79.02 N ANISOU 3834 N GLN D 121 14899 8695 6430 959 -2713 -531 N ATOM 3835 CA GLN D 121 -3.562 -4.061 -9.022 1.00 81.55 C ANISOU 3835 CA GLN D 121 15480 8677 6828 879 -3015 -313 C ATOM 3836 C GLN D 121 -2.692 -4.911 -8.105 1.00 87.07 C ANISOU 3836 C GLN D 121 16406 9264 7414 649 -3007 -242 C ATOM 3837 O GLN D 121 -3.081 -5.237 -6.980 1.00 92.96 O ANISOU 3837 O GLN D 121 17344 10043 7933 589 -2866 -368 O ATOM 3838 CB GLN D 121 -3.525 -2.601 -8.571 1.00 92.27 C ANISOU 3838 CB GLN D 121 17081 9768 8210 1121 -3273 -411 C ATOM 3839 CG GLN D 121 -2.140 -1.972 -8.595 1.00 97.38 C ANISOU 3839 CG GLN D 121 18005 10080 8917 1002 -3590 -193 C ATOM 3840 CD GLN D 121 -1.667 -1.648 -9.999 1.00114.61 C ANISOU 3840 CD GLN D 121 20088 12238 11220 837 -3788 21 C ATOM 3841 OE1 GLN D 121 -2.315 -0.895 -10.725 1.00121.07 O ANISOU 3841 OE1 GLN D 121 20897 13010 12095 961 -3971 25 O ATOM 3842 NE2 GLN D 121 -0.532 -2.217 -10.388 1.00120.21 N ANISOU 3842 NE2 GLN D 121 20730 12984 11961 523 -3792 152 N ATOM 3843 N VAL D 122 -1.508 -5.269 -8.596 1.00 76.39 N ANISOU 3843 N VAL D 122 15031 7783 6210 486 -3193 -86 N ATOM 3844 CA VAL D 122 -0.514 -6.008 -7.826 1.00 66.47 C ANISOU 3844 CA VAL D 122 13989 6320 4946 322 -3351 -64 C ATOM 3845 C VAL D 122 0.795 -5.240 -7.929 1.00 94.40 C ANISOU 3845 C VAL D 122 17588 9609 8671 300 -3612 -26 C ATOM 3846 O VAL D 122 1.387 -5.156 -9.013 1.00109.05 O ANISOU 3846 O VAL D 122 19197 11567 10670 189 -3696 -5 O ATOM 3847 CB VAL D 122 -0.342 -7.451 -8.321 1.00 65.26 C ANISOU 3847 CB VAL D 122 13614 6287 4894 152 -3350 -58 C ATOM 3848 CG1 VAL D 122 0.833 -8.112 -7.618 1.00 66.17 C ANISOU 3848 CG1 VAL D 122 13891 6085 5164 38 -3638 -90 C ATOM 3849 CG2 VAL D 122 -1.618 -8.246 -8.093 1.00 90.23 C ANISOU 3849 CG2 VAL D 122 16750 9685 7848 94 -3073 -80 C ATOM 3850 N THR D 123 1.247 -4.677 -6.812 1.00 99.36 N ANISOU 3850 N THR D 123 18515 9949 9288 349 -3705 -44 N ATOM 3851 CA THR D 123 2.466 -3.881 -6.765 1.00 92.64 C ANISOU 3851 CA THR D 123 17725 8854 8621 315 -3918 -30 C ATOM 3852 C THR D 123 3.472 -4.555 -5.845 1.00 81.07 C ANISOU 3852 C THR D 123 16400 7113 7288 237 -4093 -89 C ATOM 3853 O THR D 123 3.123 -4.973 -4.736 1.00 82.54 O ANISOU 3853 O THR D 123 16856 7152 7352 239 -4059 -88 O ATOM 3854 CB THR D 123 2.179 -2.456 -6.284 1.00 89.04 C ANISOU 3854 CB THR D 123 17516 8230 8083 484 -3958 -15 C ATOM 3855 OG1 THR D 123 1.125 -1.887 -7.071 1.00100.04 O ANISOU 3855 OG1 THR D 123 18819 9806 9387 616 -3906 2 O ATOM 3856 CG2 THR D 123 3.422 -1.589 -6.418 1.00 89.31 C ANISOU 3856 CG2 THR D 123 17603 8042 8290 380 -4170 21 C ATOM 3857 N VAL D 124 4.714 -4.664 -6.310 1.00 79.04 N ANISOU 3857 N VAL D 124 15964 6801 7267 136 -4305 -165 N ATOM 3858 CA VAL D 124 5.803 -5.271 -5.554 1.00 72.75 C ANISOU 3858 CA VAL D 124 15239 5712 6690 126 -4569 -263 C ATOM 3859 C VAL D 124 6.932 -4.251 -5.485 1.00 93.96 C ANISOU 3859 C VAL D 124 17941 8263 9498 106 -4727 -302 C ATOM 3860 O VAL D 124 7.564 -3.948 -6.504 1.00114.13 O ANISOU 3860 O VAL D 124 20163 11061 12141 -51 -4741 -412 O ATOM 3861 CB VAL D 124 6.289 -6.582 -6.185 1.00 68.80 C ANISOU 3861 CB VAL D 124 14356 5340 6444 68 -4707 -437 C ATOM 3862 CG1 VAL D 124 7.409 -7.185 -5.355 1.00 70.63 C ANISOU 3862 CG1 VAL D 124 14621 5243 6971 145 -5043 -537 C ATOM 3863 CG2 VAL D 124 5.136 -7.566 -6.326 1.00 68.13 C ANISOU 3863 CG2 VAL D 124 14281 5390 6215 49 -4560 -366 C ATOM 3864 N SER D 125 7.187 -3.725 -4.292 1.00109.48 N ANISOU 3864 N SER D 125 20285 9873 11439 203 -4825 -232 N ATOM 3865 CA SER D 125 8.207 -2.710 -4.081 1.00113.78 C ANISOU 3865 CA SER D 125 20897 10260 12074 195 -4980 -235 C ATOM 3866 C SER D 125 9.477 -3.331 -3.510 1.00119.35 C ANISOU 3866 C SER D 125 21489 10812 13048 250 -5270 -336 C ATOM 3867 O SER D 125 9.461 -4.415 -2.922 1.00127.91 O ANISOU 3867 O SER D 125 22625 11758 14217 335 -5410 -329 O ATOM 3868 CB SER D 125 7.692 -1.614 -3.144 1.00109.47 C ANISOU 3868 CB SER D 125 20791 9444 11359 297 -4914 -146 C ATOM 3869 OG SER D 125 7.311 -2.152 -1.889 1.00107.37 O ANISOU 3869 OG SER D 125 20804 8983 11009 360 -4895 -148 O ATOM 3870 N SER D 126 10.586 -2.621 -3.692 1.00124.88 N ANISOU 3870 N SER D 126 22017 11556 13878 181 -5378 -439 N ATOM 3871 CA SER D 126 11.879 -3.077 -3.197 1.00126.25 C ANISOU 3871 CA SER D 126 21961 11653 14354 260 -5638 -628 C ATOM 3872 C SER D 126 12.064 -2.706 -1.729 1.00121.50 C ANISOU 3872 C SER D 126 21840 10677 13647 450 -5853 -393 C ATOM 3873 O SER D 126 12.972 -3.204 -1.063 1.00116.66 O ANISOU 3873 O SER D 126 21137 9947 13241 572 -6138 -480 O ATOM 3874 CB SER D 126 13.014 -2.487 -4.037 1.00126.63 C ANISOU 3874 CB SER D 126 21551 11992 14571 30 -5597 -933 C ATOM 3875 OG SER D 126 12.911 -2.892 -5.391 1.00125.71 O ANISOU 3875 OG SER D 126 20952 12319 14494 -215 -5399 -1181 O TER 3876 SER D 126 HETATM 3877 N SAR B 1 -7.339 -16.001 -82.459 1.00109.28 N HETATM 3878 CA SAR B 1 -7.260 -16.858 -81.289 1.00 98.44 C HETATM 3879 C SAR B 1 -8.601 -17.236 -80.610 1.00 79.60 C HETATM 3880 O SAR B 1 -9.695 -17.004 -81.204 1.00 90.34 O HETATM 3881 CN SAR B 1 -6.900 -16.649 -83.671 1.00117.99 C ATOM 3882 N ARG B 2 -8.528 -17.796 -79.406 1.00124.92 N ANISOU 3882 N ARG B 2 15410 19491 12563 821 230 -3517 N ATOM 3883 CA ARG B 2 -9.728 -18.155 -78.660 1.00104.42 C ANISOU 3883 CA ARG B 2 13014 16648 10013 714 53 -3285 C ATOM 3884 C ARG B 2 -10.308 -16.924 -77.968 1.00 77.46 C ANISOU 3884 C ARG B 2 9110 13618 6704 569 -325 -2896 C ATOM 3885 O ARG B 2 -9.581 -15.986 -77.641 1.00 66.63 O ANISOU 3885 O ARG B 2 7262 12573 5482 785 -381 -2764 O ATOM 3886 CB ARG B 2 -9.423 -19.248 -77.633 1.00107.28 C ANISOU 3886 CB ARG B 2 13576 16585 10602 1427 277 -3200 C ATOM 3887 CG ARG B 2 -10.666 -19.892 -77.040 1.00104.71 C ANISOU 3887 CG ARG B 2 13599 15772 10414 1258 158 -2914 C ATOM 3888 CD ARG B 2 -10.347 -20.730 -75.818 1.00 92.05 C ANISOU 3888 CD ARG B 2 12050 13862 9063 2005 306 -2745 C ATOM 3889 NE ARG B 2 -11.563 -21.268 -75.216 1.00 89.73 N ANISOU 3889 NE ARG B 2 12061 13129 8901 1834 169 -2456 N ATOM 3890 CZ ARG B 2 -11.596 -21.957 -74.082 1.00107.06 C ANISOU 3890 CZ ARG B 2 14327 15030 11322 2368 224 -2233 C ATOM 3891 NH1 ARG B 2 -10.475 -22.195 -73.416 1.00121.52 N ANISOU 3891 NH1 ARG B 2 15915 16985 13271 3093 397 -2220 N ATOM 3892 NH2 ARG B 2 -12.751 -22.406 -73.611 1.00111.66 N ANISOU 3892 NH2 ARG B 2 15191 15223 12013 2159 92 -1973 N ATOM 3893 N VAL B 3 -11.619 -16.934 -77.747 1.00 73.39 N ANISOU 3893 N VAL B 3 8730 12866 6290 163 -524 -2556 N ATOM 3894 CA VAL B 3 -12.340 -15.811 -77.158 1.00 72.20 C ANISOU 3894 CA VAL B 3 8183 12964 6288 -19 -779 -2136 C ATOM 3895 C VAL B 3 -12.923 -16.275 -75.830 1.00 75.73 C ANISOU 3895 C VAL B 3 8739 13051 6983 341 -798 -1805 C ATOM 3896 O VAL B 3 -13.895 -17.042 -75.806 1.00 88.89 O ANISOU 3896 O VAL B 3 10753 14285 8737 116 -831 -1618 O ATOM 3897 CB VAL B 3 -13.439 -15.287 -78.092 1.00 75.27 C ANISOU 3897 CB VAL B 3 8558 13297 6744 -812 -928 -1826 C ATOM 3898 CG1 VAL B 3 -14.175 -14.123 -77.455 1.00 55.60 C ANISOU 3898 CG1 VAL B 3 5702 10829 4595 -879 -993 -1286 C ATOM 3899 CG2 VAL B 3 -12.843 -14.878 -79.431 1.00 83.40 C ANISOU 3899 CG2 VAL B 3 9552 14369 7767 -1100 -805 -1975 C ATOM 3900 N TYR B 4 -12.334 -15.815 -74.723 1.00 68.95 N ANISOU 3900 N TYR B 4 7603 12388 6208 848 -785 -1722 N ATOM 3901 CA TYR B 4 -12.834 -16.131 -73.384 1.00 60.33 C ANISOU 3901 CA TYR B 4 6596 11006 5321 1170 -802 -1401 C ATOM 3902 C TYR B 4 -13.786 -15.017 -72.957 1.00 60.38 C ANISOU 3902 C TYR B 4 6373 11099 5468 844 -905 -998 C ATOM 3903 O TYR B 4 -13.455 -14.130 -72.168 1.00 74.45 O ANISOU 3903 O TYR B 4 7902 13135 7249 1009 -881 -902 O ATOM 3904 CB TYR B 4 -11.682 -16.305 -72.401 1.00 63.38 C ANISOU 3904 CB TYR B 4 6844 11559 5676 1823 -724 -1486 C ATOM 3905 CG TYR B 4 -12.111 -16.787 -71.030 1.00 69.96 C ANISOU 3905 CG TYR B 4 7815 12087 6681 2151 -736 -1180 C ATOM 3906 CD1 TYR B 4 -12.299 -18.139 -70.777 1.00 76.37 C ANISOU 3906 CD1 TYR B 4 8987 12416 7615 2436 -647 -1163 C ATOM 3907 CD2 TYR B 4 -12.322 -15.891 -69.988 1.00 61.15 C ANISOU 3907 CD2 TYR B 4 6509 11138 5587 2152 -798 -916 C ATOM 3908 CE1 TYR B 4 -12.690 -18.586 -69.528 1.00 76.84 C ANISOU 3908 CE1 TYR B 4 9162 12207 7826 2729 -669 -873 C ATOM 3909 CE2 TYR B 4 -12.714 -16.328 -68.737 1.00 67.37 C ANISOU 3909 CE2 TYR B 4 7454 11647 6499 2411 -797 -645 C ATOM 3910 CZ TYR B 4 -12.896 -17.676 -68.512 1.00 75.36 C ANISOU 3910 CZ TYR B 4 8772 12219 7641 2708 -758 -615 C ATOM 3911 OH TYR B 4 -13.285 -18.117 -67.268 1.00 70.96 O ANISOU 3911 OH TYR B 4 8362 11397 7205 2960 -768 -335 O ATOM 3912 N TYR B 5 -14.998 -15.072 -73.505 1.00 51.79 N ANISOU 3912 N TYR B 5 5392 9785 4499 339 -987 -724 N ATOM 3913 CA TYR B 5 -16.009 -14.044 -73.288 1.00 49.54 C ANISOU 3913 CA TYR B 5 4859 9540 4423 2 -1019 -249 C ATOM 3914 C TYR B 5 -16.746 -14.193 -71.964 1.00 59.79 C ANISOU 3914 C TYR B 5 6265 10477 5975 250 -947 136 C ATOM 3915 O TYR B 5 -17.622 -13.372 -71.669 1.00 74.41 O ANISOU 3915 O TYR B 5 7936 12281 8056 33 -880 581 O ATOM 3916 CB TYR B 5 -17.016 -14.064 -74.441 1.00 42.29 C ANISOU 3916 CB TYR B 5 3941 8582 3545 -674 -1156 5 C ATOM 3917 CG TYR B 5 -17.593 -15.434 -74.706 1.00 51.35 C ANISOU 3917 CG TYR B 5 5537 9307 4665 -831 -1235 12 C ATOM 3918 CD1 TYR B 5 -18.730 -15.870 -74.040 1.00 50.89 C ANISOU 3918 CD1 TYR B 5 5619 8857 4859 -881 -1271 479 C ATOM 3919 CD2 TYR B 5 -16.997 -16.296 -75.616 1.00 63.48 C ANISOU 3919 CD2 TYR B 5 7397 10807 5916 -944 -1225 -452 C ATOM 3920 CE1 TYR B 5 -19.256 -17.122 -74.275 1.00 59.44 C ANISOU 3920 CE1 TYR B 5 7143 9553 5889 -1066 -1342 482 C ATOM 3921 CE2 TYR B 5 -17.517 -17.550 -75.857 1.00 67.54 C ANISOU 3921 CE2 TYR B 5 8405 10887 6370 -1138 -1237 -475 C ATOM 3922 CZ TYR B 5 -18.648 -17.957 -75.185 1.00 66.58 C ANISOU 3922 CZ TYR B 5 8407 10411 6481 -1212 -1318 -8 C ATOM 3923 OH TYR B 5 -19.171 -19.205 -75.422 1.00 76.32 O ANISOU 3923 OH TYR B 5 10159 11212 7626 -1449 -1332 -32 O ATOM 3924 N HIS B 6 -16.421 -15.205 -71.167 1.00 72.49 N ANISOU 3924 N HIS B 6 8157 11817 7570 704 -922 8 N ATOM 3925 CA HIS B 6 -17.134 -15.433 -69.923 1.00 67.73 C ANISOU 3925 CA HIS B 6 7694 10855 7185 918 -861 363 C ATOM 3926 C HIS B 6 -16.775 -14.359 -68.897 1.00 68.62 C ANISOU 3926 C HIS B 6 7609 11174 7288 1107 -717 447 C ATOM 3927 O HIS B 6 -15.678 -13.797 -68.933 1.00 75.92 O ANISOU 3927 O HIS B 6 8352 12513 7981 1230 -701 147 O ATOM 3928 CB HIS B 6 -16.800 -16.815 -69.371 1.00 64.09 C ANISOU 3928 CB HIS B 6 7575 10076 6698 1353 -871 204 C ATOM 3929 CG HIS B 6 -16.925 -17.910 -70.383 1.00 52.06 C ANISOU 3929 CG HIS B 6 6346 8325 5110 1177 -924 9 C ATOM 3930 ND1 HIS B 6 -18.133 -18.276 -70.937 1.00 52.32 N ANISOU 3930 ND1 HIS B 6 6557 8072 5249 687 -1017 284 N ATOM 3931 CD2 HIS B 6 -15.994 -18.718 -70.942 1.00 53.38 C ANISOU 3931 CD2 HIS B 6 6691 8490 5100 1386 -855 -416 C ATOM 3932 CE1 HIS B 6 -17.940 -19.262 -71.794 1.00 62.93 C ANISOU 3932 CE1 HIS B 6 8238 9244 6429 543 -1013 -12 C ATOM 3933 NE2 HIS B 6 -16.651 -19.550 -71.816 1.00 59.76 N ANISOU 3933 NE2 HIS B 6 7857 8974 5875 990 -874 -451 N ATOM 3934 N PRO B 7 -17.697 -14.045 -67.970 1.00 72.60 N ANISOU 3934 N PRO B 7 8176 11387 8024 1091 -580 864 N ATOM 3935 CA PRO B 7 -17.447 -13.066 -66.905 1.00 67.04 C ANISOU 3935 CA PRO B 7 7414 10784 7274 1200 -364 941 C ATOM 3936 C PRO B 7 -16.214 -13.402 -66.072 1.00 70.76 C ANISOU 3936 C PRO B 7 7969 11476 7441 1596 -420 624 C ATOM 3937 O PRO B 7 -15.398 -12.523 -65.795 1.00 75.52 O ANISOU 3937 O PRO B 7 8433 12458 7804 1574 -350 461 O ATOM 3938 CB PRO B 7 -18.714 -13.151 -66.049 1.00 58.74 C ANISOU 3938 CB PRO B 7 6540 9236 6544 1180 -190 1434 C ATOM 3939 CG PRO B 7 -19.764 -13.623 -66.983 1.00 65.46 C ANISOU 3939 CG PRO B 7 7349 9868 7655 886 -313 1729 C ATOM 3940 CD PRO B 7 -19.076 -14.562 -67.928 1.00 71.75 C ANISOU 3940 CD PRO B 7 8212 10823 8226 908 -588 1314 C HETATM 3941 N NH2 B 8 -16.084 -14.667 -65.685 1.00 37.62 N TER 3942 NH2 B 8 HETATM 3943 C1 NAG A1401 -20.421 -8.969 -91.256 1.00 93.29 C HETATM 3944 C2 NAG A1401 -21.228 -10.044 -91.986 1.00 97.75 C HETATM 3945 C3 NAG A1401 -20.718 -10.207 -93.416 1.00102.22 C HETATM 3946 C4 NAG A1401 -20.701 -8.863 -94.132 1.00 95.40 C HETATM 3947 C5 NAG A1401 -19.918 -7.840 -93.314 1.00 99.75 C HETATM 3948 C6 NAG A1401 -19.961 -6.451 -93.907 1.00 93.61 C HETATM 3949 C7 NAG A1401 -22.197 -11.817 -90.584 1.00102.45 C HETATM 3950 C8 NAG A1401 -23.452 -10.995 -90.573 1.00108.79 C HETATM 3951 N2 NAG A1401 -21.169 -11.312 -91.275 1.00 98.01 N HETATM 3952 O3 NAG A1401 -21.553 -11.121 -94.117 1.00108.97 O HETATM 3953 O4 NAG A1401 -20.095 -9.001 -95.412 1.00 95.10 O HETATM 3954 O5 NAG A1401 -20.474 -7.743 -91.994 1.00101.74 O HETATM 3955 O6 NAG A1401 -19.227 -5.526 -93.118 1.00 88.71 O HETATM 3956 O7 NAG A1401 -22.118 -12.890 -89.995 1.00 97.84 O HETATM 3957 C24 OLC A1402 -5.231 -13.630 -37.853 1.00 90.28 C HETATM 3958 C3 OLC A1402 -1.842 -16.721 -43.430 1.00 80.62 C HETATM 3959 C2 OLC A1402 -2.056 -16.732 -41.918 1.00 84.23 C HETATM 3960 C21 OLC A1402 -4.323 -14.377 -40.050 1.00103.93 C HETATM 3961 C1 OLC A1402 -2.871 -15.507 -41.511 1.00 94.52 C HETATM 3962 C22 OLC A1402 -5.413 -14.612 -39.007 1.00102.24 C HETATM 3963 O19 OLC A1402 -2.709 -14.475 -42.071 1.00 97.68 O HETATM 3964 O25 OLC A1402 -6.179 -13.901 -36.857 1.00 71.46 O HETATM 3965 O23 OLC A1402 -6.670 -14.414 -39.592 1.00102.18 O HETATM 3966 O20 OLC A1402 -3.813 -15.607 -40.480 1.00101.82 O HETATM 3967 C9 OLC A1403 -23.116 -27.317 -55.711 1.00 66.87 C HETATM 3968 C8 OLC A1403 -23.579 -27.014 -54.288 1.00 68.76 C HETATM 3969 C24 OLC A1403 -25.061 -33.403 -43.801 1.00 92.33 C HETATM 3970 C7 OLC A1403 -22.681 -27.746 -53.293 1.00 65.07 C HETATM 3971 C6 OLC A1403 -23.309 -27.696 -51.902 1.00 73.44 C HETATM 3972 C5 OLC A1403 -22.698 -28.793 -51.034 1.00 76.08 C HETATM 3973 C4 OLC A1403 -23.335 -28.764 -49.646 1.00 81.39 C HETATM 3974 C3 OLC A1403 -22.778 -29.915 -48.813 1.00 77.96 C HETATM 3975 C2 OLC A1403 -23.556 -30.031 -47.504 1.00 73.82 C HETATM 3976 C21 OLC A1403 -22.931 -32.624 -44.838 1.00 91.72 C HETATM 3977 C1 OLC A1403 -22.964 -31.168 -46.673 1.00 92.62 C HETATM 3978 C22 OLC A1403 -23.634 -32.938 -43.519 1.00 89.45 C HETATM 3979 O19 OLC A1403 -22.033 -31.773 -47.087 1.00105.04 O HETATM 3980 O25 OLC A1403 -25.519 -34.178 -42.727 1.00 90.45 O HETATM 3981 O23 OLC A1403 -22.938 -33.951 -42.849 1.00 87.11 O HETATM 3982 O20 OLC A1403 -23.518 -31.501 -45.432 1.00 97.04 O HETATM 3983 C24 OLC A1404 -27.605 -24.515 -35.522 1.00 98.32 C HETATM 3984 C3 OLC A1404 -26.174 -22.453 -42.284 1.00 73.80 C HETATM 3985 C2 OLC A1404 -26.330 -23.664 -41.367 1.00 74.77 C HETATM 3986 C21 OLC A1404 -26.845 -24.213 -37.882 1.00 90.00 C HETATM 3987 C1 OLC A1404 -26.790 -23.196 -39.988 1.00 85.31 C HETATM 3988 C22 OLC A1404 -27.788 -23.696 -36.798 1.00 90.96 C HETATM 3989 O19 OLC A1404 -26.579 -22.083 -39.642 1.00 89.18 O HETATM 3990 O25 OLC A1404 -28.047 -23.769 -34.422 1.00107.53 O HETATM 3991 O23 OLC A1404 -27.496 -22.352 -36.536 1.00 88.93 O HETATM 3992 O20 OLC A1404 -27.461 -24.073 -39.130 1.00 87.81 O HETATM 3993 C24 OLC A1405 -10.258 -37.754 -37.281 1.00100.24 C HETATM 3994 C21 OLC A1405 -11.385 -36.618 -39.196 1.00 87.60 C HETATM 3995 C1 OLC A1405 -12.351 -35.468 -40.996 1.00 91.13 C HETATM 3996 C22 OLC A1405 -10.048 -36.853 -38.496 1.00101.21 C HETATM 3997 O19 OLC A1405 -12.460 -34.351 -41.378 1.00 90.04 O HETATM 3998 O25 OLC A1405 -9.016 -38.055 -36.705 1.00 97.04 O HETATM 3999 O23 OLC A1405 -9.161 -37.469 -39.387 1.00110.99 O HETATM 4000 O20 OLC A1405 -11.173 -35.880 -40.365 1.00 91.26 O HETATM 4001 C24 OLC A1406 -27.217 -34.855 -47.587 1.00 97.50 C HETATM 4002 C6 OLC A1406 -28.330 -30.120 -54.687 1.00 82.99 C HETATM 4003 C5 OLC A1406 -28.785 -31.570 -54.542 1.00 85.46 C HETATM 4004 C4 OLC A1406 -28.040 -32.231 -53.385 1.00 89.49 C HETATM 4005 C3 OLC A1406 -28.654 -31.797 -52.055 1.00 94.53 C HETATM 4006 C2 OLC A1406 -27.610 -31.040 -51.238 1.00102.83 C HETATM 4007 C21 OLC A1406 -28.722 -33.041 -48.414 1.00 95.15 C HETATM 4008 C1 OLC A1406 -27.773 -31.371 -49.756 1.00103.88 C HETATM 4009 C22 OLC A1406 -28.095 -33.676 -47.175 1.00101.37 C HETATM 4010 O19 OLC A1406 -27.945 -30.501 -48.970 1.00101.18 O HETATM 4011 O25 OLC A1406 -26.230 -35.061 -46.614 1.00 90.71 O HETATM 4012 O23 OLC A1406 -27.310 -32.722 -46.515 1.00107.17 O HETATM 4013 O20 OLC A1406 -27.714 -32.699 -49.321 1.00100.43 O HETATM 4014 C10 OLC A1407 -4.471 -17.363 -48.670 1.00 92.58 C HETATM 4015 C9 OLC A1407 -5.113 -16.895 -47.621 1.00 84.55 C HETATM 4016 C11 OLC A1407 -4.478 -18.862 -48.959 1.00 92.98 C HETATM 4017 C8 OLC A1407 -5.110 -15.397 -47.327 1.00 79.40 C HETATM 4018 C12 OLC A1407 -3.595 -19.149 -50.171 1.00 90.90 C HETATM 4019 C7 OLC A1407 -3.671 -14.887 -47.320 1.00 74.96 C HETATM 4020 C6 OLC A1407 -3.673 -13.377 -47.098 1.00 72.41 C HETATM 4021 C5 OLC A1407 -3.483 -13.081 -45.612 1.00 67.37 C HETATM 4022 C4 OLC A1407 -3.665 -11.585 -45.367 1.00 74.73 C HETATM 4023 C3 OLC A1407 -2.869 -11.168 -44.132 1.00 79.77 C HETATM 4024 C1 CLR A1408 -36.196 -3.424 -44.005 1.00 91.34 C HETATM 4025 C2 CLR A1408 -36.844 -3.829 -42.682 1.00 83.43 C HETATM 4026 C3 CLR A1408 -37.568 -5.148 -42.831 1.00 81.91 C HETATM 4027 C4 CLR A1408 -36.601 -6.228 -43.274 1.00 84.43 C HETATM 4028 C5 CLR A1408 -35.834 -5.840 -44.518 1.00 93.11 C HETATM 4029 C6 CLR A1408 -35.731 -6.684 -45.535 1.00 96.67 C HETATM 4030 C7 CLR A1408 -34.993 -6.412 -46.808 1.00 97.03 C HETATM 4031 C8 CLR A1408 -34.047 -5.221 -46.695 1.00 92.88 C HETATM 4032 C9 CLR A1408 -34.747 -4.072 -45.954 1.00 90.38 C HETATM 4033 C10 CLR A1408 -35.180 -4.462 -44.510 1.00 94.64 C HETATM 4034 C11 CLR A1408 -33.938 -2.769 -45.999 1.00 88.30 C HETATM 4035 C12 CLR A1408 -33.481 -2.386 -47.405 1.00 91.00 C HETATM 4036 C13 CLR A1408 -32.682 -3.515 -48.069 1.00 94.67 C HETATM 4037 C14 CLR A1408 -33.613 -4.744 -48.087 1.00 89.98 C HETATM 4038 C15 CLR A1408 -32.909 -5.723 -49.035 1.00 89.72 C HETATM 4039 C16 CLR A1408 -32.188 -4.829 -50.060 1.00 90.84 C HETATM 4040 C17 CLR A1408 -32.385 -3.376 -49.583 1.00 96.09 C HETATM 4041 C18 CLR A1408 -31.395 -3.795 -47.275 1.00 94.85 C HETATM 4042 C19 CLR A1408 -33.977 -4.505 -43.549 1.00101.51 C HETATM 4043 C20 CLR A1408 -31.238 -2.456 -50.047 1.00 95.66 C HETATM 4044 C21 CLR A1408 -31.482 -0.979 -49.748 1.00 86.40 C HETATM 4045 C22 CLR A1408 -30.934 -2.654 -51.542 1.00 96.96 C HETATM 4046 C23 CLR A1408 -31.965 -2.075 -52.503 1.00100.51 C HETATM 4047 C24 CLR A1408 -31.355 -1.607 -53.821 1.00103.41 C HETATM 4048 C25 CLR A1408 -30.423 -2.586 -54.519 1.00102.68 C HETATM 4049 C26 CLR A1408 -30.920 -2.938 -55.910 1.00 98.90 C HETATM 4050 C27 CLR A1408 -29.000 -2.055 -54.579 1.00100.78 C HETATM 4051 O1 CLR A1408 -38.174 -5.519 -41.590 1.00 83.78 O HETATM 4052 O HOH A1501 -20.432 -9.309 -61.537 1.00 94.63 O HETATM 4053 O HOH A1502 -22.494 -15.962 -68.394 1.00 60.58 O HETATM 4054 O HOH A1503 -20.525 -13.608 -79.394 1.00 73.27 O HETATM 4055 O HOH A1504 -22.039 -20.166 -73.179 1.00 58.45 O HETATM 4056 O HOH A1505 -18.683 -14.751 -49.879 1.00 47.63 O HETATM 4057 O HOH A1506 -18.912 -23.919 -59.831 1.00 46.54 O HETATM 4058 O HOH A1507 -4.965 -21.782 -24.976 1.00 24.26 O HETATM 4059 O HOH A1508 -19.601 -37.807 -30.992 1.00 77.35 O HETATM 4060 O HOH A1509 -22.597 -29.011 -75.053 1.00 63.09 O HETATM 4061 O HOH A1510 -20.740 -33.411 -21.670 1.00 50.82 O HETATM 4062 O HOH A1511 -0.904 -19.701 -30.999 1.00 51.97 O HETATM 4063 O HOH A1512 -16.745 -38.755 -35.911 1.00 59.10 O HETATM 4064 O HOH A1513 -3.644 -24.530 -39.571 1.00 59.61 O HETATM 4065 O HOH A1514 -0.058 -8.902 -66.174 1.00 59.79 O HETATM 4066 O HOH A1515 -26.409 -3.627 -78.630 1.00 59.89 O HETATM 4067 O HOH D 201 -1.186 -5.504 -25.024 1.00 54.47 O HETATM 4068 O HOH D 202 -22.993 -14.359 -32.824 1.00 29.13 O HETATM 4069 O HOH D 203 -9.812 -9.596 -26.473 1.00 81.80 O HETATM 4070 O HOH D 204 -13.410 -27.564 -26.634 1.00 61.52 O HETATM 4071 O HOH D 205 -23.789 -18.334 -21.977 1.00 80.93 O HETATM 4072 O HOH B 101 -13.559 -18.682 -78.447 1.00 71.32 O CONECT 63 2577 CONECT 735 1354 CONECT 1326 3943 CONECT 1354 735 CONECT 2577 63 CONECT 3074 3632 CONECT 3632 3074 CONECT 3877 3878 3881 CONECT 3878 3877 3879 CONECT 3879 3878 3880 3882 CONECT 3880 3879 CONECT 3881 3877 CONECT 3882 3879 CONECT 3936 3941 CONECT 3941 3936 CONECT 3943 1326 3944 3954 CONECT 3944 3943 3945 3951 CONECT 3945 3944 3946 3952 CONECT 3946 3945 3947 3953 CONECT 3947 3946 3948 3954 CONECT 3948 3947 3955 CONECT 3949 3950 3951 3956 CONECT 3950 3949 CONECT 3951 3944 3949 CONECT 3952 3945 CONECT 3953 3946 CONECT 3954 3943 3947 CONECT 3955 3948 CONECT 3956 3949 CONECT 3957 3962 3964 CONECT 3958 3959 CONECT 3959 3958 3961 CONECT 3960 3962 3966 CONECT 3961 3959 3963 3966 CONECT 3962 3957 3960 3965 CONECT 3963 3961 CONECT 3964 3957 CONECT 3965 3962 CONECT 3966 3960 3961 CONECT 3967 3968 CONECT 3968 3967 3970 CONECT 3969 3978 3980 CONECT 3970 3968 3971 CONECT 3971 3970 3972 CONECT 3972 3971 3973 CONECT 3973 3972 3974 CONECT 3974 3973 3975 CONECT 3975 3974 3977 CONECT 3976 3978 3982 CONECT 3977 3975 3979 3982 CONECT 3978 3969 3976 3981 CONECT 3979 3977 CONECT 3980 3969 CONECT 3981 3978 CONECT 3982 3976 3977 CONECT 3983 3988 3990 CONECT 3984 3985 CONECT 3985 3984 3987 CONECT 3986 3988 3992 CONECT 3987 3985 3989 3992 CONECT 3988 3983 3986 3991 CONECT 3989 3987 CONECT 3990 3983 CONECT 3991 3988 CONECT 3992 3986 3987 CONECT 3993 3996 3998 CONECT 3994 3996 4000 CONECT 3995 3997 4000 CONECT 3996 3993 3994 3999 CONECT 3997 3995 CONECT 3998 3993 CONECT 3999 3996 CONECT 4000 3994 3995 CONECT 4001 4009 4011 CONECT 4002 4003 CONECT 4003 4002 4004 CONECT 4004 4003 4005 CONECT 4005 4004 4006 CONECT 4006 4005 4008 CONECT 4007 4009 4013 CONECT 4008 4006 4010 4013 CONECT 4009 4001 4007 4012 CONECT 4010 4008 CONECT 4011 4001 CONECT 4012 4009 CONECT 4013 4007 4008 CONECT 4014 4015 4016 CONECT 4015 4014 4017 CONECT 4016 4014 4018 CONECT 4017 4015 4019 CONECT 4018 4016 CONECT 4019 4017 4020 CONECT 4020 4019 4021 CONECT 4021 4020 4022 CONECT 4022 4021 4023 CONECT 4023 4022 CONECT 4024 4025 4033 CONECT 4025 4024 4026 CONECT 4026 4025 4027 4051 CONECT 4027 4026 4028 CONECT 4028 4027 4029 4033 CONECT 4029 4028 4030 CONECT 4030 4029 4031 CONECT 4031 4030 4032 4037 CONECT 4032 4031 4033 4034 CONECT 4033 4024 4028 4032 4042 CONECT 4034 4032 4035 CONECT 4035 4034 4036 CONECT 4036 4035 4037 4040 4041 CONECT 4037 4031 4036 4038 CONECT 4038 4037 4039 CONECT 4039 4038 4040 CONECT 4040 4036 4039 4043 CONECT 4041 4036 CONECT 4042 4033 CONECT 4043 4040 4044 4045 CONECT 4044 4043 CONECT 4045 4043 4046 CONECT 4046 4045 4047 CONECT 4047 4046 4048 CONECT 4048 4047 4049 4050 CONECT 4049 4048 CONECT 4050 4048 CONECT 4051 4026 MASTER 502 0 10 16 18 0 0 6 4069 3 124 44 END