Browse entries in the PDBbind-CN Database
HEADER TRANSCRIPTION/DNA 27-JAN-12 3VOK TITLE X-RAY CRYSTAL STRUCTURE OF WILD TYPE HRTR IN THE APO FORM WITH THE TITLE 2 TARGET DNA. COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 5'-D(*AP*TP*GP*AP*CP*AP*CP*TP*GP*TP*GP*TP*CP*AP*T)-3'; COMPND 7 CHAIN: U; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS; SOURCE 3 ORGANISM_TAXID: 272623; SOURCE 4 STRAIN: IL1403; SOURCE 5 GENE: L53789, LL0661, YGFC; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-3A; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES KEYWDS HEME, SENSOR PROTEIN, TETR SUPERFAMILY, DNA-BINDING COMPLEX, KEYWDS 2 TRANSCRIPTION-DNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR H.SAWAI,H.SUGIMOTO,Y.SHIRO,S.AONO REVDAT 3 22-NOV-17 3VOK 1 REMARK REVDAT 2 12-SEP-12 3VOK 1 JRNL REVDAT 1 25-JUL-12 3VOK 0 JRNL AUTH H.SAWAI,M.YAMANAKA,H.SUGIMOTO,Y.SHIRO,S.AONO JRNL TITL STRUCTURAL BASIS FOR THE TRANSCRIPTIONAL REGULATION OF HEME JRNL TITL 2 HOMEOSTASIS IN LACTOCOCCUS LACTIS. JRNL REF J.BIOL.CHEM. V. 287 30755 2012 JRNL REFN ISSN 0021-9258 JRNL PMID 22798069 JRNL DOI 10.1074/JBC.M112.370916 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.7_650 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.87 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 3 NUMBER OF REFLECTIONS : 20763 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.204 REMARK 3 R VALUE (WORKING SET) : 0.202 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150 REMARK 3 FREE R VALUE TEST SET COUNT : 1070 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 23.8719 - 3.9929 0.98 2686 131 0.1915 0.2008 REMARK 3 2 3.9929 - 3.1716 0.99 2556 132 0.1897 0.2208 REMARK 3 3 3.1716 - 2.7714 0.99 2481 159 0.2216 0.2895 REMARK 3 4 2.7714 - 2.5183 0.98 2464 123 0.2335 0.2837 REMARK 3 5 2.5183 - 2.3380 0.98 2440 131 0.2218 0.2811 REMARK 3 6 2.3380 - 2.2002 0.96 2398 138 0.2007 0.2584 REMARK 3 7 2.2002 - 2.0901 0.95 2333 134 0.1951 0.2282 REMARK 3 8 2.0901 - 1.9992 0.94 2335 122 0.1889 0.2214 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.83 REMARK 3 K_SOL : 0.37 REMARK 3 B_SOL : 44.00 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.800 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.25 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.47370 REMARK 3 B22 (A**2) : 2.47370 REMARK 3 B33 (A**2) : -4.94740 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 1925 REMARK 3 ANGLE : 1.106 2671 REMARK 3 CHIRALITY : 0.071 286 REMARK 3 PLANARITY : 0.005 280 REMARK 3 DIHEDRAL : 20.349 738 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 2:27) REMARK 3 ORIGIN FOR THE GROUP (A): 34.3766 47.9828 4.1551 REMARK 3 T TENSOR REMARK 3 T11: 0.4642 T22: 0.3592 REMARK 3 T33: 0.3223 T12: -0.1201 REMARK 3 T13: -0.1024 T23: -0.0290 REMARK 3 L TENSOR REMARK 3 L11: 0.3224 L22: 0.7563 REMARK 3 L33: 0.2315 L12: 0.3115 REMARK 3 L13: -0.0449 L23: 0.2582 REMARK 3 S TENSOR REMARK 3 S11: 0.1106 S12: -0.1612 S13: 0.0018 REMARK 3 S21: 0.1116 S22: 0.0090 S23: 0.0668 REMARK 3 S31: 0.0462 S32: 0.0992 S33: -0.0424 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 28:34) REMARK 3 ORIGIN FOR THE GROUP (A): 26.6805 49.5298 -11.0317 REMARK 3 T TENSOR REMARK 3 T11: 0.5527 T22: 0.3319 REMARK 3 T33: 0.3692 T12: -0.1488 REMARK 3 T13: -0.1564 T23: 0.0909 REMARK 3 L TENSOR REMARK 3 L11: 0.0011 L22: 0.1181 REMARK 3 L33: 0.0032 L12: 0.0096 REMARK 3 L13: 0.0009 L23: 0.0117 REMARK 3 S TENSOR REMARK 3 S11: -0.0624 S12: 0.0321 S13: 0.0228 REMARK 3 S21: -0.0536 S22: 0.0178 S23: 0.0316 REMARK 3 S31: -0.0371 S32: -0.0131 S33: 0.0185 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 35:70) REMARK 3 ORIGIN FOR THE GROUP (A): 34.5561 48.0849 -3.0229 REMARK 3 T TENSOR REMARK 3 T11: 0.4302 T22: 0.2703 REMARK 3 T33: 0.3491 T12: -0.1477 REMARK 3 T13: -0.1234 T23: 0.0380 REMARK 3 L TENSOR REMARK 3 L11: 0.1450 L22: 0.0658 REMARK 3 L33: 0.0816 L12: 0.0460 REMARK 3 L13: 0.0318 L23: 0.0308 REMARK 3 S TENSOR REMARK 3 S11: -0.0389 S12: 0.0323 S13: 0.0381 REMARK 3 S21: -0.0629 S22: 0.0362 S23: -0.0429 REMARK 3 S31: 0.0044 S32: 0.0869 S33: 0.0113 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 71:99) REMARK 3 ORIGIN FOR THE GROUP (A): 15.8376 22.7628 -1.8844 REMARK 3 T TENSOR REMARK 3 T11: 0.2846 T22: 0.1955 REMARK 3 T33: 0.2246 T12: 0.0095 REMARK 3 T13: -0.0017 T23: -0.0156 REMARK 3 L TENSOR REMARK 3 L11: 0.5827 L22: 0.1904 REMARK 3 L33: 0.3966 L12: 0.2273 REMARK 3 L13: -0.0022 L23: -0.1939 REMARK 3 S TENSOR REMARK 3 S11: 0.0531 S12: -0.1725 S13: -0.1393 REMARK 3 S21: 0.2587 S22: -0.0400 S23: 0.0005 REMARK 3 S31: -0.0909 S32: -0.0357 S33: -0.0208 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 100:113) REMARK 3 ORIGIN FOR THE GROUP (A): 18.1492 40.3027 -4.0382 REMARK 3 T TENSOR REMARK 3 T11: 0.4147 T22: 0.2440 REMARK 3 T33: 0.3289 T12: -0.0937 REMARK 3 T13: -0.0657 T23: -0.0202 REMARK 3 L TENSOR REMARK 3 L11: 0.1145 L22: 0.1131 REMARK 3 L33: 0.0901 L12: 0.0821 REMARK 3 L13: 0.0388 L23: 0.0927 REMARK 3 S TENSOR REMARK 3 S11: -0.0317 S12: -0.0215 S13: 0.0367 REMARK 3 S21: 0.1172 S22: -0.0566 S23: 0.0115 REMARK 3 S31: -0.0527 S32: -0.0155 S33: 0.0368 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 114:138) REMARK 3 ORIGIN FOR THE GROUP (A): 29.6581 34.2016 -14.1192 REMARK 3 T TENSOR REMARK 3 T11: 0.4178 T22: 0.5333 REMARK 3 T33: 0.3139 T12: -0.0766 REMARK 3 T13: -0.0876 T23: -0.0091 REMARK 3 L TENSOR REMARK 3 L11: 0.0473 L22: 0.0818 REMARK 3 L33: 0.2134 L12: -0.0101 REMARK 3 L13: 0.0874 L23: 0.0341 REMARK 3 S TENSOR REMARK 3 S11: -0.0592 S12: 0.0942 S13: -0.0392 REMARK 3 S21: -0.0676 S22: 0.0615 S23: -0.0104 REMARK 3 S31: -0.1934 S32: 0.0725 S33: 0.0109 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 139:157) REMARK 3 ORIGIN FOR THE GROUP (A): 15.5494 29.3675 -13.4047 REMARK 3 T TENSOR REMARK 3 T11: 0.1692 T22: 0.1817 REMARK 3 T33: 0.2136 T12: 0.0105 REMARK 3 T13: -0.0254 T23: 0.0137 REMARK 3 L TENSOR REMARK 3 L11: 0.4992 L22: 0.0499 REMARK 3 L33: 0.5440 L12: 0.1599 REMARK 3 L13: 0.0741 L23: 0.0377 REMARK 3 S TENSOR REMARK 3 S11: -0.0176 S12: 0.0391 S13: -0.0294 REMARK 3 S21: -0.0429 S22: -0.0112 S23: -0.0748 REMARK 3 S31: -0.1183 S32: 0.1451 S33: 0.0256 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 158:178) REMARK 3 ORIGIN FOR THE GROUP (A): 5.4954 28.4442 -9.8270 REMARK 3 T TENSOR REMARK 3 T11: 0.2050 T22: 0.2236 REMARK 3 T33: 0.2633 T12: 0.0607 REMARK 3 T13: -0.0038 T23: -0.0222 REMARK 3 L TENSOR REMARK 3 L11: 0.3351 L22: 0.1143 REMARK 3 L33: 0.1511 L12: -0.1662 REMARK 3 L13: -0.0311 L23: -0.0048 REMARK 3 S TENSOR REMARK 3 S11: -0.0397 S12: -0.0319 S13: -0.0168 REMARK 3 S21: 0.0386 S22: 0.0313 S23: 0.1028 REMARK 3 S31: -0.0907 S32: -0.1414 S33: 0.0255 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 179:189) REMARK 3 ORIGIN FOR THE GROUP (A): 1.2336 13.9852 -22.5451 REMARK 3 T TENSOR REMARK 3 T11: 0.1669 T22: 0.1901 REMARK 3 T33: 0.2607 T12: 0.0163 REMARK 3 T13: -0.0505 T23: 0.0269 REMARK 3 L TENSOR REMARK 3 L11: 0.0616 L22: 0.0139 REMARK 3 L33: 0.0841 L12: -0.0040 REMARK 3 L13: 0.0033 L23: -0.0076 REMARK 3 S TENSOR REMARK 3 S11: -0.0290 S12: -0.0390 S13: 0.1038 REMARK 3 S21: 0.0163 S22: -0.0035 S23: -0.0494 REMARK 3 S31: -0.0081 S32: -0.0178 S33: 0.0224 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN U REMARK 3 ORIGIN FOR THE GROUP (A): 36.7486 64.6365 -18.1634 REMARK 3 T TENSOR REMARK 3 T11: 0.6523 T22: 0.4340 REMARK 3 T33: 0.1782 T12: -0.1720 REMARK 3 T13: -0.6310 T23: 0.2025 REMARK 3 L TENSOR REMARK 3 L11: 0.0490 L22: 0.1410 REMARK 3 L33: 0.2277 L12: -0.0791 REMARK 3 L13: 0.0102 L23: -0.0558 REMARK 3 S TENSOR REMARK 3 S11: 0.1689 S12: -0.0061 S13: 0.0238 REMARK 3 S21: -0.0113 S22: 0.2342 S23: -0.0262 REMARK 3 S31: -0.0295 S32: 0.0808 S33: 0.3937 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 3VOK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-FEB-12. REMARK 100 THE DEPOSITION ID IS D_1000095304. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-JAN-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.3 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21224 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 21.50 REMARK 200 R MERGE (I) : 0.07900 REMARK 200 R SYM (I) : 0.07900 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 41.5840 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 21.80 REMARK 200 R MERGE FOR SHELL (I) : 0.51300 REMARK 200 R SYM FOR SHELL (I) : 0.51300 REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.622 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.3.0 REMARK 200 STARTING MODEL: 1QPI REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M SODIUM CITRATE, 0.1M PIPES, PH REMARK 280 7.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+1/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+5/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.46333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.23167 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 54.34750 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 18.11583 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 90.57917 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.46333 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 36.23167 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 18.11583 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 54.34750 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 90.57917 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, U REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -36.23167 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 MET A 1 REMARK 465 PRO A 125 REMARK 465 GLN A 126 REMARK 465 SER A 127 REMARK 465 SER A 128 REMARK 465 ALA A 129 REMARK 465 THR A 130 REMARK 465 VAL A 131 REMARK 465 PRO A 132 REMARK 465 ALA A 133 REMARK 465 SER A 134 REMARK 465 GLU A 135 REMARK 465 ASN A 136 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 DG U 3 C3' - C2' - C1' ANGL. DEV. = -5.9 DEGREES REMARK 500 DG U 3 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES REMARK 500 DA U 6 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES REMARK 500 DG U 9 C1' - O4' - C4' ANGL. DEV. = -7.4 DEGREES REMARK 500 DG U 9 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 999 REMARK 999 SEQUENCE REMARK 999 CHAIN U HAS MICROHETEROGENEITY AT POSITION 8(DT/DA) DBREF 3VOK A 1 189 UNP Q9CHR1 Q9CHR1_LACLA 1 189 DBREF 3VOK U 1 15 PDB 3VOK 3VOK 1 15 SEQADV 3VOK DA U 8 PDB 3VOK DT 8 MICROHETEROGENEITY SEQRES 1 A 189 MET PRO LYS SER THR TYR PHE SER LEU SER ASP GLU LYS SEQRES 2 A 189 ARG ASN ARG VAL TYR ASP ALA CYS LEU ASN GLU PHE GLN SEQRES 3 A 189 THR HIS SER PHE HIS GLU ALA LYS ILE MET HIS ILE VAL SEQRES 4 A 189 LYS ALA LEU ASP ILE PRO ARG GLY SER PHE TYR GLN TYR SEQRES 5 A 189 PHE GLU ASP LEU LYS ASP ALA TYR PHE TYR VAL LEU SER SEQRES 6 A 189 GLN GLU THR LEU GLU ILE HIS ASP LEU PHE PHE ASN LEU SEQRES 7 A 189 LEU LYS ASP ASN SER ILE GLU GLU SER LEU ASP LYS TYR SEQRES 8 A 189 LYS TYR LEU LEU LEU GLU ASN LEU ILE ASP SER PRO GLN SEQRES 9 A 189 TYR LYS LEU TYR LYS TYR ARG PHE LEU ASP TRP THR TYR SEQRES 10 A 189 GLU LEU GLU ARG ASP TRP LYS PRO GLN SER SER ALA THR SEQRES 11 A 189 VAL PRO ALA SER GLU ASN ASP ASN PRO ILE SER GLN VAL SEQRES 12 A 189 LEU LYS SER VAL VAL HIS ASN LEU VAL TYR ARG LEU PHE SEQRES 13 A 189 SER GLU ASN TRP THR GLU LYS THR PHE ILE GLU ASN TYR SEQRES 14 A 189 ASP LYS GLU ILE LYS LEU VAL THR GLU GLY LEU LEU ASN SEQRES 15 A 189 TYR ILE THR ASP ARG LYS ASN SEQRES 1 U 15 DA DT DG DA DC DA DC DT DG DT DG DT DC SEQRES 2 U 15 DA DT FORMUL 3 HOH *81(H2 O) HELIX 1 1 LYS A 3 SER A 8 1 6 HELIX 2 2 ASP A 11 HIS A 28 1 18 HELIX 3 3 LYS A 34 LEU A 42 1 9 HELIX 4 4 PRO A 45 TYR A 52 1 8 HELIX 5 5 ASP A 55 THR A 68 1 14 HELIX 6 6 ILE A 71 LEU A 79 1 9 HELIX 7 7 SER A 83 ILE A 100 1 18 HELIX 8 8 GLN A 104 ASP A 114 1 11 HELIX 9 9 THR A 116 TRP A 123 1 8 HELIX 10 10 ASN A 138 GLU A 158 1 21 HELIX 11 11 THR A 161 GLU A 178 1 18 HELIX 12 12 LEU A 181 ILE A 184 1 4 CRYST1 97.870 97.870 108.695 90.00 90.00 120.00 P 65 2 2 12 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 0.010218 0.005899 0.000000 0.00000 SCALE2 0.000000 0.011798 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009200 0.00000 ATOM 1 N PRO A 2 39.397 41.288 -1.429 1.00 40.86 N ANISOU 1 N PRO A 2 5973 4888 4663 -978 -1376 -291 N ATOM 2 CA PRO A 2 40.018 42.532 -0.969 1.00 39.82 C ANISOU 2 CA PRO A 2 5826 4798 4507 -1000 -1340 -338 C ATOM 3 C PRO A 2 41.502 42.337 -0.689 1.00 48.87 C ANISOU 3 C PRO A 2 6944 5982 5644 -984 -1368 -384 C ATOM 4 O PRO A 2 41.950 41.195 -0.587 1.00 48.95 O ANISOU 4 O PRO A 2 6947 5987 5664 -956 -1421 -372 O ATOM 5 CB PRO A 2 39.273 42.831 0.334 1.00 42.63 C ANISOU 5 CB PRO A 2 6195 5170 4832 -1018 -1326 -307 C ATOM 6 CG PRO A 2 37.946 42.186 0.152 1.00 42.48 C ANISOU 6 CG PRO A 2 6199 5107 4833 -1016 -1330 -250 C ATOM 7 CD PRO A 2 38.207 40.936 -0.638 1.00 44.34 C ANISOU 7 CD PRO A 2 6437 5316 5096 -985 -1378 -235 C ATOM 8 N LYS A 3 42.242 43.441 -0.597 1.00 52.14 N ANISOU 8 N LYS A 3 7338 6429 6043 -1003 -1334 -438 N ATOM 9 CA LYS A 3 43.672 43.433 -0.282 1.00 49.86 C ANISOU 9 CA LYS A 3 7017 6180 5749 -992 -1356 -491 C ATOM 10 C LYS A 3 43.980 43.319 1.210 1.00 60.40 C ANISOU 10 C LYS A 3 8347 7556 7046 -991 -1387 -480 C ATOM 11 O LYS A 3 43.159 43.670 2.065 1.00 53.61 O ANISOU 11 O LYS A 3 7510 6703 6154 -1011 -1369 -447 O ATOM 12 CB LYS A 3 44.355 44.674 -0.863 1.00 45.59 C ANISOU 12 CB LYS A 3 6457 5655 5209 -1016 -1303 -557 C ATOM 13 CG LYS A 3 44.252 44.775 -2.386 1.00 50.77 C ANISOU 13 CG LYS A 3 7123 6270 5897 -1021 -1277 -574 C ATOM 14 CD LYS A 3 45.031 45.976 -2.903 1.00 53.23 C ANISOU 14 CD LYS A 3 7420 6598 6205 -1048 -1224 -642 C ATOM 15 CE LYS A 3 45.087 46.000 -4.423 1.00 57.23 C ANISOU 15 CE LYS A 3 7942 7065 6737 -1057 -1201 -663 C ATOM 16 NZ LYS A 3 45.993 47.084 -4.902 1.00 62.11 N ANISOU 16 NZ LYS A 3 8548 7700 7351 -1085 -1150 -735 N ATOM 17 N SER A 4 45.175 42.830 1.518 1.00 66.27 N ANISOU 17 N SER A 4 9061 8325 7794 -969 -1434 -511 N ATOM 18 CA SER A 4 45.600 42.679 2.902 1.00 68.08 C ANISOU 18 CA SER A 4 9288 8594 7985 -968 -1475 -503 C ATOM 19 C SER A 4 45.355 43.959 3.695 1.00 62.75 C ANISOU 19 C SER A 4 8622 7955 7266 -1008 -1424 -519 C ATOM 20 O SER A 4 44.896 43.912 4.836 1.00 65.02 O ANISOU 20 O SER A 4 8935 8259 7511 -1022 -1435 -484 O ATOM 21 CB SER A 4 47.079 42.292 2.962 1.00 81.58 C ANISOU 21 CB SER A 4 10954 10328 9715 -942 -1525 -553 C ATOM 22 OG SER A 4 47.869 43.174 2.179 1.00 91.63 O ANISOU 22 OG SER A 4 12193 11613 11010 -954 -1481 -626 O ATOM 23 N THR A 5 45.652 45.102 3.082 1.00 59.92 N ANISOU 23 N THR A 5 8246 7606 6917 -1029 -1366 -572 N ATOM 24 CA THR A 5 45.512 46.379 3.767 1.00 60.30 C ANISOU 24 CA THR A 5 8297 7686 6927 -1067 -1313 -595 C ATOM 25 C THR A 5 44.055 46.666 4.141 1.00 56.53 C ANISOU 25 C THR A 5 7858 7187 6433 -1091 -1275 -543 C ATOM 26 O THR A 5 43.800 47.449 5.057 1.00 51.57 O ANISOU 26 O THR A 5 7239 6586 5768 -1122 -1243 -548 O ATOM 27 CB THR A 5 46.104 47.551 2.947 1.00 71.32 C ANISOU 27 CB THR A 5 9669 9089 8340 -1086 -1255 -662 C ATOM 28 OG1 THR A 5 45.270 47.814 1.817 1.00 86.74 O ANISOU 28 OG1 THR A 5 11641 10995 10321 -1092 -1213 -647 O ATOM 29 CG2 THR A 5 47.515 47.221 2.465 1.00 68.39 C ANISOU 29 CG2 THR A 5 9256 8733 7996 -1065 -1286 -720 C ATOM 30 N TYR A 6 43.104 46.039 3.440 1.00 46.15 N ANISOU 30 N TYR A 6 6564 5824 5147 -1078 -1278 -496 N ATOM 31 CA TYR A 6 41.690 46.133 3.820 1.00 42.95 C ANISOU 31 CA TYR A 6 6191 5394 4734 -1096 -1249 -445 C ATOM 32 C TYR A 6 41.489 45.462 5.181 1.00 51.49 C ANISOU 32 C TYR A 6 7294 6496 5773 -1100 -1285 -407 C ATOM 33 O TYR A 6 40.904 46.041 6.103 1.00 49.01 O ANISOU 33 O TYR A 6 6998 6197 5427 -1133 -1249 -399 O ATOM 34 CB TYR A 6 40.759 45.500 2.760 1.00 34.66 C ANISOU 34 CB TYR A 6 5156 4288 3727 -1080 -1252 -405 C ATOM 35 CG TYR A 6 39.341 45.282 3.265 1.00 42.63 C ANISOU 35 CG TYR A 6 6193 5270 4734 -1093 -1237 -350 C ATOM 36 CD1 TYR A 6 38.465 46.353 3.426 1.00 41.96 C ANISOU 36 CD1 TYR A 6 6114 5177 4653 -1125 -1175 -352 C ATOM 37 CD2 TYR A 6 38.887 44.009 3.604 1.00 39.81 C ANISOU 37 CD2 TYR A 6 5856 4895 4375 -1076 -1282 -298 C ATOM 38 CE1 TYR A 6 37.175 46.160 3.910 1.00 40.92 C ANISOU 38 CE1 TYR A 6 6002 5020 4526 -1139 -1156 -308 C ATOM 39 CE2 TYR A 6 37.598 43.807 4.085 1.00 38.79 C ANISOU 39 CE2 TYR A 6 5752 4741 4246 -1092 -1263 -252 C ATOM 40 CZ TYR A 6 36.751 44.888 4.239 1.00 32.54 C ANISOU 40 CZ TYR A 6 4961 3942 3461 -1124 -1199 -260 C ATOM 41 OH TYR A 6 35.474 44.687 4.709 1.00 41.91 O ANISOU 41 OH TYR A 6 6167 5102 4654 -1142 -1176 -221 O ATOM 42 N PHE A 7 42.001 44.244 5.305 1.00 49.42 N ANISOU 42 N PHE A 7 7034 6233 5512 -1068 -1354 -386 N ATOM 43 CA PHE A 7 41.844 43.467 6.530 1.00 61.47 C ANISOU 43 CA PHE A 7 8589 7772 6996 -1071 -1398 -344 C ATOM 44 C PHE A 7 42.639 44.034 7.719 1.00 62.62 C ANISOU 44 C PHE A 7 8733 7974 7088 -1093 -1407 -373 C ATOM 45 O PHE A 7 42.326 43.748 8.874 1.00 70.20 O ANISOU 45 O PHE A 7 9726 8947 7999 -1112 -1424 -341 O ATOM 46 CB PHE A 7 42.223 42.004 6.284 1.00 59.59 C ANISOU 46 CB PHE A 7 8353 7512 6778 -1028 -1475 -313 C ATOM 47 CG PHE A 7 41.399 41.331 5.218 1.00 57.91 C ANISOU 47 CG PHE A 7 8146 7244 6611 -1009 -1470 -280 C ATOM 48 CD1 PHE A 7 40.074 40.999 5.453 1.00 52.08 C ANISOU 48 CD1 PHE A 7 7444 6476 5870 -1023 -1451 -226 C ATOM 49 CD2 PHE A 7 41.956 41.012 3.987 1.00 55.23 C ANISOU 49 CD2 PHE A 7 7780 6885 6321 -980 -1485 -305 C ATOM 50 CE1 PHE A 7 39.319 40.375 4.481 1.00 50.81 C ANISOU 50 CE1 PHE A 7 7288 6266 5753 -1007 -1450 -197 C ATOM 51 CE2 PHE A 7 41.205 40.383 3.011 1.00 55.04 C ANISOU 51 CE2 PHE A 7 7765 6811 6336 -966 -1483 -275 C ATOM 52 CZ PHE A 7 39.884 40.066 3.256 1.00 52.19 C ANISOU 52 CZ PHE A 7 7437 6421 5971 -978 -1468 -221 C ATOM 53 N SER A 8 43.655 44.841 7.430 1.00 66.54 N ANISOU 53 N SER A 8 9191 8501 7591 -1094 -1394 -436 N ATOM 54 CA SER A 8 44.487 45.430 8.476 1.00 70.93 C ANISOU 54 CA SER A 8 9739 9111 8099 -1115 -1404 -471 C ATOM 55 C SER A 8 43.850 46.692 9.061 1.00 71.50 C ANISOU 55 C SER A 8 9826 9202 8138 -1166 -1326 -487 C ATOM 56 O SER A 8 44.371 47.280 10.014 1.00 62.12 O ANISOU 56 O SER A 8 8639 8060 6905 -1193 -1323 -515 O ATOM 57 CB SER A 8 45.881 45.751 7.933 1.00 73.28 C ANISOU 57 CB SER A 8 9986 9433 8423 -1096 -1422 -538 C ATOM 58 OG SER A 8 46.502 44.589 7.409 1.00 81.81 O ANISOU 58 OG SER A 8 11048 10495 9541 -1050 -1491 -530 O ATOM 59 N LEU A 9 42.726 47.107 8.483 1.00 63.52 N ANISOU 59 N LEU A 9 8826 8154 7154 -1179 -1264 -470 N ATOM 60 CA LEU A 9 41.979 48.254 8.994 1.00 60.35 C ANISOU 60 CA LEU A 9 8437 7760 6734 -1225 -1187 -482 C ATOM 61 C LEU A 9 41.478 48.007 10.422 1.00 50.09 C ANISOU 61 C LEU A 9 7178 6479 5375 -1257 -1191 -450 C ATOM 62 O LEU A 9 41.188 46.875 10.799 1.00 45.26 O ANISOU 62 O LEU A 9 6596 5854 4749 -1244 -1241 -400 O ATOM 63 CB LEU A 9 40.786 48.563 8.080 1.00 58.93 C ANISOU 63 CB LEU A 9 8260 7528 6604 -1226 -1133 -463 C ATOM 64 CG LEU A 9 40.911 49.687 7.046 1.00 54.29 C ANISOU 64 CG LEU A 9 7644 6928 6055 -1230 -1079 -508 C ATOM 65 CD1 LEU A 9 42.245 49.628 6.342 1.00 61.15 C ANISOU 65 CD1 LEU A 9 8482 7815 6936 -1205 -1112 -552 C ATOM 66 CD2 LEU A 9 39.767 49.638 6.037 1.00 43.57 C ANISOU 66 CD2 LEU A 9 6293 5511 4750 -1221 -1054 -476 C ATOM 67 N SER A 10 41.360 49.079 11.201 1.00 51.21 N ANISOU 67 N SER A 10 7324 6650 5482 -1303 -1134 -481 N ATOM 68 CA SER A 10 40.713 49.003 12.505 1.00 45.58 C ANISOU 68 CA SER A 10 6655 5949 4713 -1346 -1118 -455 C ATOM 69 C SER A 10 39.287 48.493 12.315 1.00 49.94 C ANISOU 69 C SER A 10 7232 6448 5293 -1349 -1091 -403 C ATOM 70 O SER A 10 38.695 48.656 11.230 1.00 43.41 O ANISOU 70 O SER A 10 6384 5580 4530 -1329 -1062 -399 O ATOM 71 CB SER A 10 40.679 50.386 13.158 1.00 54.34 C ANISOU 71 CB SER A 10 7761 7090 5796 -1397 -1043 -503 C ATOM 72 OG SER A 10 39.872 51.285 12.407 1.00 50.95 O ANISOU 72 OG SER A 10 7311 6626 5422 -1405 -965 -519 O ATOM 73 N ASP A 11 38.748 47.836 13.342 1.00 40.31 N ANISOU 73 N ASP A 11 6060 5229 4027 -1374 -1103 -363 N ATOM 74 CA ASP A 11 37.369 47.357 13.279 1.00 44.30 C ANISOU 74 CA ASP A 11 6589 5686 4558 -1383 -1071 -318 C ATOM 75 C ASP A 11 36.438 48.480 12.846 1.00 42.64 C ANISOU 75 C ASP A 11 6355 5450 4398 -1406 -979 -344 C ATOM 76 O ASP A 11 35.551 48.270 12.017 1.00 43.71 O ANISOU 76 O ASP A 11 6478 5535 4594 -1388 -963 -322 O ATOM 77 CB ASP A 11 36.903 46.782 14.620 1.00 52.19 C ANISOU 77 CB ASP A 11 7647 6693 5489 -1424 -1075 -284 C ATOM 78 CG ASP A 11 37.327 45.337 14.817 1.00 68.58 C ANISOU 78 CG ASP A 11 9754 8764 7537 -1394 -1168 -234 C ATOM 79 OD1 ASP A 11 37.914 44.748 13.882 1.00 65.84 O ANISOU 79 OD1 ASP A 11 9379 8405 7230 -1339 -1226 -227 O ATOM 80 OD2 ASP A 11 37.060 44.785 15.908 1.00 78.52 O ANISOU 80 OD2 ASP A 11 11070 10030 8735 -1427 -1182 -202 O ATOM 81 N GLU A 12 36.653 49.675 13.399 1.00 33.20 N ANISOU 81 N GLU A 12 5149 4285 3179 -1445 -923 -392 N ATOM 82 CA GLU A 12 35.820 50.824 13.065 1.00 35.76 C ANISOU 82 CA GLU A 12 5450 4584 3554 -1468 -836 -421 C ATOM 83 C GLU A 12 35.873 51.192 11.569 1.00 44.93 C ANISOU 83 C GLU A 12 6569 5714 4790 -1426 -836 -432 C ATOM 84 O GLU A 12 34.838 51.317 10.914 1.00 43.57 O ANISOU 84 O GLU A 12 6385 5491 4679 -1420 -804 -416 O ATOM 85 CB GLU A 12 36.218 52.034 13.904 1.00 42.24 C ANISOU 85 CB GLU A 12 6266 5447 4334 -1516 -780 -474 C ATOM 86 CG GLU A 12 35.222 53.173 13.823 1.00 59.02 C ANISOU 86 CG GLU A 12 8374 7544 6510 -1547 -684 -501 C ATOM 87 CD GLU A 12 35.833 54.455 13.291 1.00 76.42 C ANISOU 87 CD GLU A 12 10538 9760 8737 -1547 -648 -557 C ATOM 88 OE1 GLU A 12 35.297 55.004 12.301 1.00 73.11 O ANISOU 88 OE1 GLU A 12 10090 9297 8390 -1529 -616 -562 O ATOM 89 OE2 GLU A 12 36.838 54.921 13.874 1.00 88.41 O ANISOU 89 OE2 GLU A 12 12058 11332 10203 -1565 -651 -595 O ATOM 90 N LYS A 13 37.078 51.382 11.045 1.00 43.72 N ANISOU 90 N LYS A 13 6394 5588 4631 -1400 -872 -461 N ATOM 91 CA LYS A 13 37.260 51.836 9.661 1.00 40.35 C ANISOU 91 CA LYS A 13 5933 5134 4263 -1369 -867 -479 C ATOM 92 C LYS A 13 36.847 50.773 8.642 1.00 36.86 C ANISOU 92 C LYS A 13 5493 4647 3865 -1326 -915 -433 C ATOM 93 O LYS A 13 36.289 51.092 7.592 1.00 37.79 O ANISOU 93 O LYS A 13 5596 4721 4040 -1312 -896 -430 O ATOM 94 CB LYS A 13 38.717 52.256 9.429 1.00 49.12 C ANISOU 94 CB LYS A 13 7022 6289 5353 -1358 -890 -528 C ATOM 95 CG LYS A 13 39.046 52.659 7.999 1.00 63.96 C ANISOU 95 CG LYS A 13 8875 8142 7285 -1330 -887 -549 C ATOM 96 CD LYS A 13 38.142 53.767 7.491 1.00 60.78 C ANISOU 96 CD LYS A 13 8464 7701 6929 -1348 -815 -560 C ATOM 97 CE LYS A 13 38.487 54.121 6.063 1.00 56.30 C ANISOU 97 CE LYS A 13 7880 7106 6406 -1324 -817 -577 C ATOM 98 NZ LYS A 13 37.451 55.009 5.488 1.00 60.27 N ANISOU 98 NZ LYS A 13 8381 7559 6961 -1336 -763 -573 N ATOM 99 N ARG A 14 37.136 49.513 8.956 1.00 38.18 N ANISOU 99 N ARG A 14 5680 4823 4004 -1306 -980 -398 N ATOM 100 CA ARG A 14 36.812 48.401 8.082 1.00 39.20 C ANISOU 100 CA ARG A 14 5813 4912 4171 -1266 -1029 -355 C ATOM 101 C ARG A 14 35.297 48.255 7.971 1.00 47.10 C ANISOU 101 C ARG A 14 6825 5861 5210 -1277 -994 -318 C ATOM 102 O ARG A 14 34.763 47.994 6.891 1.00 44.72 O ANISOU 102 O ARG A 14 6514 5516 4963 -1253 -1002 -299 O ATOM 103 CB ARG A 14 37.444 47.109 8.606 1.00 39.79 C ANISOU 103 CB ARG A 14 5909 5006 4205 -1245 -1104 -326 C ATOM 104 CG ARG A 14 37.386 45.934 7.635 1.00 44.05 C ANISOU 104 CG ARG A 14 6447 5508 4782 -1201 -1160 -291 C ATOM 105 CD ARG A 14 38.318 44.799 8.077 1.00 52.34 C ANISOU 105 CD ARG A 14 7509 6580 5799 -1175 -1239 -274 C ATOM 106 NE ARG A 14 37.764 44.026 9.185 1.00 56.93 N ANISOU 106 NE ARG A 14 8132 7160 6338 -1192 -1257 -228 N ATOM 107 CZ ARG A 14 38.128 44.157 10.461 1.00 67.79 C ANISOU 107 CZ ARG A 14 9532 8575 7649 -1222 -1264 -232 C ATOM 108 NH1 ARG A 14 39.067 45.030 10.814 1.00 58.21 N ANISOU 108 NH1 ARG A 14 8300 7409 6409 -1235 -1257 -281 N ATOM 109 NH2 ARG A 14 37.553 43.403 11.389 1.00 66.53 N ANISOU 109 NH2 ARG A 14 9419 8408 7451 -1241 -1279 -187 N ATOM 110 N ASN A 15 34.604 48.434 9.090 1.00 42.81 N ANISOU 110 N ASN A 15 6301 5324 4640 -1317 -953 -311 N ATOM 111 CA ASN A 15 33.147 48.419 9.076 1.00 44.98 C ANISOU 111 CA ASN A 15 6581 5552 4959 -1333 -910 -286 C ATOM 112 C ASN A 15 32.543 49.596 8.322 1.00 37.58 C ANISOU 112 C ASN A 15 5611 4582 4084 -1339 -853 -312 C ATOM 113 O ASN A 15 31.547 49.437 7.615 1.00 41.30 O ANISOU 113 O ASN A 15 6072 5002 4616 -1327 -846 -289 O ATOM 114 CB ASN A 15 32.585 48.335 10.499 1.00 53.23 C ANISOU 114 CB ASN A 15 7657 6610 5958 -1381 -873 -278 C ATOM 115 CG ASN A 15 32.361 46.908 10.945 1.00 60.82 C ANISOU 115 CG ASN A 15 8656 7563 6889 -1374 -923 -226 C ATOM 116 OD1 ASN A 15 31.222 46.436 11.006 1.00 73.92 O ANISOU 116 OD1 ASN A 15 10327 9182 8578 -1384 -901 -197 O ATOM 117 ND2 ASN A 15 33.446 46.200 11.238 1.00 57.52 N ANISOU 117 ND2 ASN A 15 8257 7180 6418 -1355 -990 -216 N ATOM 118 N ARG A 16 33.131 50.781 8.458 1.00 35.67 N ANISOU 118 N ARG A 16 5353 4369 3831 -1357 -815 -360 N ATOM 119 CA ARG A 16 32.682 51.908 7.637 1.00 40.30 C ANISOU 119 CA ARG A 16 5912 4922 4479 -1357 -770 -384 C ATOM 120 C ARG A 16 32.863 51.642 6.138 1.00 35.55 C ANISOU 120 C ARG A 16 5299 4288 3921 -1315 -813 -371 C ATOM 121 O ARG A 16 31.970 51.936 5.343 1.00 34.65 O ANISOU 121 O ARG A 16 5173 4122 3870 -1307 -799 -359 O ATOM 122 CB ARG A 16 33.391 53.215 8.019 1.00 46.03 C ANISOU 122 CB ARG A 16 6623 5683 5181 -1384 -722 -440 C ATOM 123 CG ARG A 16 32.917 53.808 9.335 1.00 61.16 C ANISOU 123 CG ARG A 16 8547 7618 7074 -1435 -657 -461 C ATOM 124 CD ARG A 16 33.548 55.162 9.608 1.00 61.05 C ANISOU 124 CD ARG A 16 8517 7634 7046 -1461 -606 -518 C ATOM 125 NE ARG A 16 33.173 56.145 8.599 1.00 64.02 N ANISOU 125 NE ARG A 16 8866 7967 7491 -1452 -573 -535 N ATOM 126 CZ ARG A 16 34.028 56.712 7.754 1.00 68.87 C ANISOU 126 CZ ARG A 16 9469 8589 8111 -1434 -584 -561 C ATOM 127 NH1 ARG A 16 35.319 56.392 7.803 1.00 68.05 N ANISOU 127 NH1 ARG A 16 9370 8534 7952 -1423 -625 -578 N ATOM 128 NH2 ARG A 16 33.594 57.601 6.865 1.00 66.49 N ANISOU 128 NH2 ARG A 16 9150 8241 7871 -1429 -555 -571 N ATOM 129 N VAL A 17 34.022 51.103 5.758 1.00 35.84 N ANISOU 129 N VAL A 17 5339 4353 3925 -1289 -867 -376 N ATOM 130 CA VAL A 17 34.320 50.854 4.345 1.00 35.16 C ANISOU 130 CA VAL A 17 5247 4240 3874 -1254 -904 -371 C ATOM 131 C VAL A 17 33.373 49.795 3.792 1.00 39.89 C ANISOU 131 C VAL A 17 5855 4791 4510 -1232 -939 -318 C ATOM 132 O VAL A 17 32.754 49.977 2.737 1.00 35.06 O ANISOU 132 O VAL A 17 5238 4132 3950 -1221 -939 -306 O ATOM 133 CB VAL A 17 35.791 50.397 4.134 1.00 32.88 C ANISOU 133 CB VAL A 17 4957 3992 3546 -1233 -952 -392 C ATOM 134 CG1 VAL A 17 35.997 49.867 2.722 1.00 29.82 C ANISOU 134 CG1 VAL A 17 4567 3571 3190 -1200 -991 -381 C ATOM 135 CG2 VAL A 17 36.757 51.542 4.416 1.00 40.30 C ANISOU 135 CG2 VAL A 17 5881 4972 4458 -1253 -917 -450 C ATOM 136 N TYR A 18 33.258 48.685 4.515 1.00 33.76 N ANISOU 136 N TYR A 18 5096 4026 3706 -1228 -969 -287 N ATOM 137 CA TYR A 18 32.370 47.612 4.101 1.00 30.93 C ANISOU 137 CA TYR A 18 4748 3624 3379 -1210 -1000 -238 C ATOM 138 C TYR A 18 30.914 48.058 3.969 1.00 31.66 C ANISOU 138 C TYR A 18 4832 3669 3530 -1226 -958 -224 C ATOM 139 O TYR A 18 30.271 47.783 2.962 1.00 36.02 O ANISOU 139 O TYR A 18 5379 4175 4133 -1207 -977 -201 O ATOM 140 CB TYR A 18 32.446 46.412 5.053 1.00 33.11 C ANISOU 140 CB TYR A 18 5048 3919 3612 -1209 -1034 -207 C ATOM 141 CG TYR A 18 31.589 45.265 4.546 1.00 37.10 C ANISOU 141 CG TYR A 18 5565 4379 4153 -1189 -1066 -159 C ATOM 142 CD1 TYR A 18 32.081 44.362 3.606 1.00 37.22 C ANISOU 142 CD1 TYR A 18 5582 4382 4179 -1152 -1124 -143 C ATOM 143 CD2 TYR A 18 30.275 45.108 4.982 1.00 42.36 C ANISOU 143 CD2 TYR A 18 6236 5012 4845 -1210 -1034 -133 C ATOM 144 CE1 TYR A 18 31.287 43.313 3.127 1.00 31.76 C ANISOU 144 CE1 TYR A 18 4899 3648 3520 -1136 -1152 -101 C ATOM 145 CE2 TYR A 18 29.483 44.081 4.513 1.00 36.25 C ANISOU 145 CE2 TYR A 18 5470 4197 4106 -1194 -1062 -93 C ATOM 146 CZ TYR A 18 29.996 43.182 3.586 1.00 38.37 C ANISOU 146 CZ TYR A 18 5743 4456 4382 -1156 -1122 -75 C ATOM 147 OH TYR A 18 29.204 42.165 3.112 1.00 40.72 O ANISOU 147 OH TYR A 18 6048 4712 4714 -1142 -1148 -36 O ATOM 148 N ASP A 19 30.389 48.715 5.000 1.00 32.16 N ANISOU 148 N ASP A 19 4892 3741 3587 -1262 -901 -238 N ATOM 149 CA ASP A 19 29.003 49.178 4.981 1.00 37.71 C ANISOU 149 CA ASP A 19 5579 4395 4352 -1279 -856 -231 C ATOM 150 C ASP A 19 28.715 50.111 3.794 1.00 32.43 C ANISOU 150 C ASP A 19 4888 3688 3747 -1267 -847 -244 C ATOM 151 O ASP A 19 27.608 50.135 3.254 1.00 38.39 O ANISOU 151 O ASP A 19 5628 4390 4568 -1262 -843 -225 O ATOM 152 CB ASP A 19 28.655 49.851 6.319 1.00 41.74 C ANISOU 152 CB ASP A 19 6090 4927 4843 -1325 -788 -255 C ATOM 153 CG ASP A 19 28.661 48.860 7.495 1.00 45.42 C ANISOU 153 CG ASP A 19 6588 5420 5251 -1344 -796 -234 C ATOM 154 OD1 ASP A 19 28.517 47.644 7.255 1.00 52.31 O ANISOU 154 OD1 ASP A 19 7477 6278 6120 -1322 -845 -194 O ATOM 155 OD2 ASP A 19 28.809 49.299 8.657 1.00 45.25 O ANISOU 155 OD2 ASP A 19 6579 5432 5184 -1383 -753 -257 O ATOM 156 N ALA A 20 29.723 50.881 3.392 1.00 33.81 N ANISOU 156 N ALA A 20 5059 3888 3900 -1263 -846 -277 N ATOM 157 CA ALA A 20 29.609 51.751 2.225 1.00 34.21 C ANISOU 157 CA ALA A 20 5098 3903 3999 -1253 -843 -288 C ATOM 158 C ALA A 20 29.531 50.954 0.924 1.00 33.47 C ANISOU 158 C ALA A 20 5014 3774 3929 -1220 -903 -256 C ATOM 159 O ALA A 20 28.736 51.271 0.025 1.00 32.74 O ANISOU 159 O ALA A 20 4915 3629 3895 -1213 -910 -242 O ATOM 160 CB ALA A 20 30.790 52.727 2.182 1.00 36.91 C ANISOU 160 CB ALA A 20 5438 4282 4304 -1262 -822 -335 C ATOM 161 N CYS A 21 30.369 49.931 0.796 1.00 32.46 N ANISOU 161 N CYS A 21 4902 3674 3757 -1201 -950 -247 N ATOM 162 CA CYS A 21 30.281 49.075 -0.385 1.00 33.93 C ANISOU 162 CA CYS A 21 5100 3828 3964 -1173 -1004 -218 C ATOM 163 C CYS A 21 28.918 48.414 -0.391 1.00 30.14 C ANISOU 163 C CYS A 21 4616 3303 3531 -1170 -1014 -176 C ATOM 164 O CYS A 21 28.244 48.367 -1.412 1.00 34.63 O ANISOU 164 O CYS A 21 5185 3824 4148 -1159 -1037 -157 O ATOM 165 CB CYS A 21 31.396 48.024 -0.391 1.00 31.92 C ANISOU 165 CB CYS A 21 4859 3610 3660 -1154 -1049 -217 C ATOM 166 SG CYS A 21 33.066 48.754 -0.556 1.00 33.96 S ANISOU 166 SG CYS A 21 5114 3918 3872 -1156 -1041 -273 S ATOM 167 N LEU A 22 28.508 47.909 0.768 1.00 31.78 N ANISOU 167 N LEU A 22 4823 3526 3724 -1182 -998 -164 N ATOM 168 CA LEU A 22 27.246 47.194 0.873 1.00 31.51 C ANISOU 168 CA LEU A 22 4786 3451 3734 -1183 -1002 -128 C ATOM 169 C LEU A 22 26.111 48.117 0.453 1.00 32.06 C ANISOU 169 C LEU A 22 4832 3472 3879 -1192 -973 -132 C ATOM 170 O LEU A 22 25.223 47.718 -0.302 1.00 34.37 O ANISOU 170 O LEU A 22 5118 3716 4226 -1180 -999 -105 O ATOM 171 CB LEU A 22 27.024 46.687 2.303 1.00 32.40 C ANISOU 171 CB LEU A 22 4907 3590 3813 -1204 -976 -122 C ATOM 172 CG LEU A 22 25.661 46.046 2.576 1.00 37.42 C ANISOU 172 CG LEU A 22 5539 4185 4495 -1213 -966 -92 C ATOM 173 CD1 LEU A 22 25.481 44.797 1.721 1.00 34.48 C ANISOU 173 CD1 LEU A 22 5177 3785 4137 -1184 -1026 -54 C ATOM 174 CD2 LEU A 22 25.486 45.733 4.066 1.00 36.74 C ANISOU 174 CD2 LEU A 22 5467 4125 4367 -1245 -928 -92 C ATOM 175 N ASN A 23 26.164 49.361 0.917 1.00 37.29 N ANISOU 175 N ASN A 23 5478 4143 4546 -1214 -921 -166 N ATOM 176 CA ASN A 23 25.122 50.322 0.593 1.00 42.15 C ANISOU 176 CA ASN A 23 6067 4709 5240 -1222 -892 -172 C ATOM 177 C ASN A 23 25.041 50.626 -0.901 1.00 41.98 C ANISOU 177 C ASN A 23 6049 4645 5258 -1200 -935 -161 C ATOM 178 O ASN A 23 23.953 50.706 -1.470 1.00 40.97 O ANISOU 178 O ASN A 23 5903 4461 5201 -1194 -948 -142 O ATOM 179 CB ASN A 23 25.298 51.610 1.389 1.00 43.97 C ANISOU 179 CB ASN A 23 6282 4959 5466 -1251 -825 -215 C ATOM 180 CG ASN A 23 24.262 52.652 1.035 1.00 57.21 C ANISOU 180 CG ASN A 23 7928 6579 7230 -1257 -797 -224 C ATOM 181 OD1 ASN A 23 23.125 52.594 1.506 1.00 59.71 O ANISOU 181 OD1 ASN A 23 8220 6863 7605 -1269 -769 -219 O ATOM 182 ND2 ASN A 23 24.644 53.609 0.191 1.00 62.98 N ANISOU 182 ND2 ASN A 23 8660 7295 7976 -1249 -804 -238 N ATOM 183 N GLU A 24 26.194 50.802 -1.532 1.00 36.13 N ANISOU 183 N GLU A 24 5329 3929 4470 -1190 -957 -174 N ATOM 184 CA GLU A 24 26.237 51.033 -2.965 1.00 32.72 C ANISOU 184 CA GLU A 24 4911 3460 4061 -1175 -999 -164 C ATOM 185 C GLU A 24 25.594 49.873 -3.736 1.00 32.29 C ANISOU 185 C GLU A 24 4865 3370 4033 -1155 -1056 -122 C ATOM 186 O GLU A 24 24.838 50.091 -4.673 1.00 37.94 O ANISOU 186 O GLU A 24 5580 4033 4803 -1149 -1084 -104 O ATOM 187 CB GLU A 24 27.679 51.233 -3.433 1.00 34.96 C ANISOU 187 CB GLU A 24 5220 3782 4283 -1172 -1008 -189 C ATOM 188 CG GLU A 24 27.819 51.384 -4.950 1.00 36.05 C ANISOU 188 CG GLU A 24 5382 3883 4433 -1163 -1049 -180 C ATOM 189 CD GLU A 24 27.387 52.766 -5.458 1.00 40.38 C ANISOU 189 CD GLU A 24 5929 4390 5025 -1174 -1030 -190 C ATOM 190 OE1 GLU A 24 26.908 53.585 -4.649 1.00 35.00 O ANISOU 190 OE1 GLU A 24 5221 3705 4373 -1187 -983 -205 O ATOM 191 OE2 GLU A 24 27.534 53.033 -6.666 1.00 37.95 O ANISOU 191 OE2 GLU A 24 5648 4050 4720 -1173 -1060 -184 O ATOM 192 N PHE A 25 25.900 48.640 -3.343 1.00 31.17 N ANISOU 192 N PHE A 25 4734 3257 3854 -1146 -1076 -107 N ATOM 193 CA PHE A 25 25.374 47.471 -4.062 1.00 37.65 C ANISOU 193 CA PHE A 25 5564 4046 4695 -1129 -1128 -70 C ATOM 194 C PHE A 25 23.926 47.140 -3.710 1.00 31.58 C ANISOU 194 C PHE A 25 4771 3237 3991 -1132 -1122 -45 C ATOM 195 O PHE A 25 23.252 46.426 -4.446 1.00 35.91 O ANISOU 195 O PHE A 25 5321 3747 4574 -1120 -1164 -16 O ATOM 196 CB PHE A 25 26.290 46.250 -3.882 1.00 40.37 C ANISOU 196 CB PHE A 25 5929 4430 4980 -1115 -1155 -63 C ATOM 197 CG PHE A 25 27.679 46.467 -4.418 1.00 36.25 C ANISOU 197 CG PHE A 25 5425 3940 4407 -1110 -1166 -90 C ATOM 198 CD1 PHE A 25 27.866 46.907 -5.721 1.00 40.17 C ANISOU 198 CD1 PHE A 25 5939 4410 4915 -1108 -1188 -95 C ATOM 199 CD2 PHE A 25 28.790 46.274 -3.613 1.00 29.20 C ANISOU 199 CD2 PHE A 25 4536 3103 3457 -1110 -1154 -112 C ATOM 200 CE1 PHE A 25 29.139 47.128 -6.225 1.00 39.09 C ANISOU 200 CE1 PHE A 25 5820 4300 4734 -1108 -1191 -125 C ATOM 201 CE2 PHE A 25 30.069 46.499 -4.103 1.00 33.19 C ANISOU 201 CE2 PHE A 25 5051 3636 3923 -1106 -1161 -143 C ATOM 202 CZ PHE A 25 30.245 46.928 -5.415 1.00 44.67 C ANISOU 202 CZ PHE A 25 6521 5062 5389 -1106 -1176 -151 C ATOM 203 N GLN A 26 23.431 47.672 -2.602 1.00 33.57 N ANISOU 203 N GLN A 26 4999 3495 4260 -1152 -1068 -60 N ATOM 204 CA GLN A 26 22.008 47.528 -2.331 1.00 40.10 C ANISOU 204 CA GLN A 26 5797 4278 5161 -1159 -1055 -46 C ATOM 205 C GLN A 26 21.224 48.431 -3.285 1.00 37.59 C ANISOU 205 C GLN A 26 5459 3902 4921 -1154 -1070 -45 C ATOM 206 O GLN A 26 20.066 48.176 -3.586 1.00 42.30 O ANISOU 206 O GLN A 26 6034 4450 5590 -1150 -1087 -26 O ATOM 207 CB GLN A 26 21.689 47.861 -0.870 1.00 44.74 C ANISOU 207 CB GLN A 26 6365 4886 5747 -1187 -986 -68 C ATOM 208 CG GLN A 26 22.184 46.807 0.122 1.00 46.04 C ANISOU 208 CG GLN A 26 6554 5097 5842 -1195 -978 -59 C ATOM 209 CD GLN A 26 22.126 47.279 1.563 1.00 54.51 C ANISOU 209 CD GLN A 26 7621 6199 6894 -1229 -909 -86 C ATOM 210 OE1 GLN A 26 22.166 48.480 1.836 1.00 60.19 O ANISOU 210 OE1 GLN A 26 8322 6921 7627 -1245 -864 -118 O ATOM 211 NE2 GLN A 26 22.036 46.333 2.497 1.00 47.07 N ANISOU 211 NE2 GLN A 26 6696 5275 5913 -1244 -898 -72 N ATOM 212 N THR A 27 21.848 49.525 -3.699 1.00 35.24 N ANISOU 212 N THR A 27 5168 3609 4611 -1155 -1063 -66 N ATOM 213 CA THR A 27 21.184 50.510 -4.545 1.00 39.02 C ANISOU 213 CA THR A 27 5633 4032 5160 -1152 -1078 -65 C ATOM 214 C THR A 27 21.593 50.522 -6.023 1.00 41.12 C ANISOU 214 C THR A 27 5935 4276 5414 -1137 -1141 -47 C ATOM 215 O THR A 27 21.021 51.257 -6.825 1.00 45.41 O ANISOU 215 O THR A 27 6475 4768 6013 -1134 -1165 -39 O ATOM 216 CB THR A 27 21.364 51.914 -3.930 1.00 43.56 C ANISOU 216 CB THR A 27 6190 4614 5746 -1169 -1018 -102 C ATOM 217 OG1 THR A 27 22.757 52.156 -3.718 1.00 39.95 O ANISOU 217 OG1 THR A 27 5761 4214 5203 -1175 -1000 -125 O ATOM 218 CG2 THR A 27 20.669 51.975 -2.582 1.00 47.90 C ANISOU 218 CG2 THR A 27 6702 5170 6326 -1189 -954 -119 C ATOM 219 N HIS A 28 22.586 49.723 -6.385 1.00 40.10 N ANISOU 219 N HIS A 28 6369 4205 4664 -1397 -1574 871 N ATOM 220 CA HIS A 28 23.132 49.765 -7.736 1.00 40.58 C ANISOU 220 CA HIS A 28 6441 4268 4708 -1419 -1579 880 C ATOM 221 C HIS A 28 23.486 48.380 -8.237 1.00 40.19 C ANISOU 221 C HIS A 28 6390 4230 4650 -1431 -1554 876 C ATOM 222 O HIS A 28 24.132 47.610 -7.526 1.00 35.04 O ANISOU 222 O HIS A 28 5733 3583 3999 -1428 -1530 872 O ATOM 223 CB HIS A 28 24.422 50.597 -7.777 1.00 44.14 C ANISOU 223 CB HIS A 28 6905 4715 5150 -1426 -1585 891 C ATOM 224 CG HIS A 28 24.226 52.047 -7.469 1.00 48.58 C ANISOU 224 CG HIS A 28 7473 5267 5719 -1417 -1611 897 C ATOM 225 ND1 HIS A 28 23.987 52.511 -6.195 1.00 49.38 N ANISOU 225 ND1 HIS A 28 7567 5362 5834 -1397 -1614 893 N ATOM 226 CD2 HIS A 28 24.238 53.138 -8.272 1.00 49.01 C ANISOU 226 CD2 HIS A 28 7540 5315 5767 -1426 -1637 906 C ATOM 227 CE1 HIS A 28 23.857 53.827 -6.225 1.00 51.18 C ANISOU 227 CE1 HIS A 28 7802 5581 6064 -1394 -1639 900 C ATOM 228 NE2 HIS A 28 24.006 54.231 -7.473 1.00 47.49 N ANISOU 228 NE2 HIS A 28 7347 5113 5585 -1411 -1654 908 N ATOM 229 N SER A 29 23.119 48.092 -9.481 1.00 36.53 N ANISOU 229 N SER A 29 5933 3770 4177 -1447 -1560 878 N ATOM 230 CA SER A 29 23.623 46.909 -10.166 1.00 40.72 C ANISOU 230 CA SER A 29 6466 4311 4697 -1462 -1538 876 C ATOM 231 C SER A 29 25.125 47.113 -10.303 1.00 38.40 C ANISOU 231 C SER A 29 6182 4017 4391 -1473 -1529 885 C ATOM 232 O SER A 29 25.617 48.233 -10.140 1.00 37.57 O ANISOU 232 O SER A 29 6085 3905 4285 -1472 -1545 893 O ATOM 233 CB SER A 29 22.983 46.758 -11.555 1.00 48.13 C ANISOU 233 CB SER A 29 7411 5252 5626 -1478 -1550 878 C ATOM 234 OG SER A 29 23.508 47.707 -12.479 1.00 43.92 O ANISOU 234 OG SER A 29 6894 4713 5079 -1492 -1569 890 O ATOM 235 N PHE A 30 25.861 46.034 -10.543 1.00 32.80 N ANISOU 235 N PHE A 30 5473 3317 3674 -1484 -1504 884 N ATOM 236 CA PHE A 30 27.298 46.153 -10.737 1.00 40.58 C ANISOU 236 CA PHE A 30 6468 4303 4649 -1496 -1494 892 C ATOM 237 C PHE A 30 27.632 47.191 -11.804 1.00 37.55 C ANISOU 237 C PHE A 30 6100 3912 4253 -1510 -1516 903 C ATOM 238 O PHE A 30 28.597 47.952 -11.667 1.00 40.17 O ANISOU 238 O PHE A 30 6441 4239 4583 -1513 -1520 911 O ATOM 239 CB PHE A 30 27.937 44.808 -11.090 1.00 35.89 C ANISOU 239 CB PHE A 30 5872 3719 4047 -1508 -1465 889 C ATOM 240 CG PHE A 30 29.412 44.911 -11.384 1.00 39.09 C ANISOU 240 CG PHE A 30 6287 4124 4443 -1521 -1455 897 C ATOM 241 CD1 PHE A 30 30.310 45.189 -10.370 1.00 43.04 C ANISOU 241 CD1 PHE A 30 6784 4620 4949 -1512 -1447 899 C ATOM 242 CD2 PHE A 30 29.891 44.761 -12.675 1.00 49.61 C ANISOU 242 CD2 PHE A 30 7633 5459 5760 -1543 -1453 903 C ATOM 243 CE1 PHE A 30 31.666 45.299 -10.634 1.00 52.28 C ANISOU 243 CE1 PHE A 30 7963 5790 6113 -1524 -1438 906 C ATOM 244 CE2 PHE A 30 31.245 44.868 -12.947 1.00 51.52 C ANISOU 244 CE2 PHE A 30 7883 5699 5994 -1555 -1442 911 C ATOM 245 CZ PHE A 30 32.135 45.142 -11.924 1.00 45.80 C ANISOU 245 CZ PHE A 30 7153 4970 5276 -1546 -1435 912 C ATOM 246 N HIS A 31 26.840 47.238 -12.869 1.00 37.49 N ANISOU 246 N HIS A 31 6099 3905 4239 -1520 -1530 904 N ATOM 247 CA HIS A 31 27.113 48.208 -13.923 1.00 41.22 C ANISOU 247 CA HIS A 31 6589 4372 4700 -1535 -1551 915 C ATOM 248 C HIS A 31 26.786 49.659 -13.554 1.00 45.99 C ANISOU 248 C HIS A 31 7197 4965 5311 -1524 -1579 920 C ATOM 249 O HIS A 31 27.408 50.579 -14.079 1.00 50.61 O ANISOU 249 O HIS A 31 7797 5545 5889 -1533 -1593 930 O ATOM 250 CB HIS A 31 26.434 47.803 -15.237 1.00 54.70 C ANISOU 250 CB HIS A 31 8304 6082 6397 -1550 -1558 915 C ATOM 251 CG HIS A 31 27.104 46.651 -15.912 1.00 69.37 C ANISOU 251 CG HIS A 31 10166 7949 8243 -1566 -1532 914 C ATOM 252 ND1 HIS A 31 26.404 45.631 -16.519 1.00 84.28 N ANISOU 252 ND1 HIS A 31 12051 9844 10127 -1573 -1524 908 N ATOM 253 CD2 HIS A 31 28.416 46.348 -16.059 1.00 77.06 C ANISOU 253 CD2 HIS A 31 11146 8925 9207 -1578 -1513 919 C ATOM 254 CE1 HIS A 31 27.256 44.753 -17.018 1.00 89.48 C ANISOU 254 CE1 HIS A 31 12715 10510 10775 -1588 -1501 909 C ATOM 255 NE2 HIS A 31 28.483 45.164 -16.752 1.00 85.46 N ANISOU 255 NE2 HIS A 31 12211 9998 10263 -1591 -1493 915 N ATOM 256 N GLU A 32 25.802 49.865 -12.682 1.00 46.58 N ANISOU 256 N GLU A 32 7259 5037 5401 -1505 -1588 913 N ATOM 257 CA GLU A 32 25.468 51.209 -12.214 1.00 48.19 C ANISOU 257 CA GLU A 32 7465 5231 5614 -1493 -1614 917 C ATOM 258 C GLU A 32 26.377 51.657 -11.059 1.00 44.74 C ANISOU 258 C GLU A 32 7025 4790 5183 -1482 -1607 920 C ATOM 259 O GLU A 32 26.512 52.850 -10.799 1.00 39.79 O ANISOU 259 O GLU A 32 6404 4155 4560 -1476 -1626 926 O ATOM 260 CB GLU A 32 24.016 51.286 -11.730 1.00 58.08 C ANISOU 260 CB GLU A 32 8705 6481 6881 -1476 -1627 909 C ATOM 261 CG GLU A 32 22.942 50.848 -12.707 1.00 70.67 C ANISOU 261 CG GLU A 32 10300 8079 8473 -1484 -1636 905 C ATOM 262 CD GLU A 32 21.573 50.706 -12.030 1.00 77.38 C ANISOU 262 CD GLU A 32 11134 8927 9341 -1466 -1642 895 C ATOM 263 OE1 GLU A 32 20.608 51.325 -12.529 1.00 86.18 O ANISOU 263 OE1 GLU A 32 12250 10035 10459 -1465 -1667 896 O ATOM 264 OE2 GLU A 32 21.462 49.982 -11.003 1.00 53.28 O ANISOU 264 OE2 GLU A 32 8067 5878 6299 -1453 -1621 886 O ATOM 265 N ALA A 33 26.981 50.703 -10.355 1.00 37.43 N ANISOU 265 N ALA A 33 6091 3871 4260 -1478 -1580 914 N ATOM 266 CA ALA A 33 27.795 51.029 -9.192 1.00 36.11 C ANISOU 266 CA ALA A 33 5920 3700 4100 -1466 -1572 915 C ATOM 267 C ALA A 33 29.078 51.752 -9.595 1.00 39.13 C ANISOU 267 C ALA A 33 6316 4078 4472 -1478 -1576 927 C ATOM 268 O ALA A 33 29.672 51.461 -10.627 1.00 42.59 O ANISOU 268 O ALA A 33 6765 4521 4898 -1497 -1570 932 O ATOM 269 CB ALA A 33 28.111 49.770 -8.373 1.00 37.46 C ANISOU 269 CB ALA A 33 6079 3879 4276 -1460 -1542 906 C ATOM 270 N LYS A 34 29.511 52.697 -8.775 1.00 40.48 N ANISOU 270 N LYS A 34 6489 4242 4651 -1467 -1586 931 N ATOM 271 CA LYS A 34 30.737 53.417 -9.085 1.00 39.04 C ANISOU 271 CA LYS A 34 6318 4055 4460 -1478 -1590 942 C ATOM 272 C LYS A 34 31.641 53.591 -7.868 1.00 36.57 C ANISOU 272 C LYS A 34 6001 3738 4155 -1466 -1581 942 C ATOM 273 O LYS A 34 31.179 53.880 -6.755 1.00 34.66 O ANISOU 273 O LYS A 34 5751 3492 3926 -1447 -1585 937 O ATOM 274 CB LYS A 34 30.424 54.785 -9.700 1.00 36.30 C ANISOU 274 CB LYS A 34 5983 3699 4110 -1482 -1621 950 C ATOM 275 CG LYS A 34 29.502 54.750 -10.910 1.00 42.01 C ANISOU 275 CG LYS A 34 6712 4424 4825 -1493 -1634 951 C ATOM 276 CD LYS A 34 30.177 54.153 -12.142 1.00 44.01 C ANISOU 276 CD LYS A 34 6977 4683 5063 -1516 -1622 955 C ATOM 277 CE LYS A 34 29.124 53.789 -13.185 1.00 53.47 C ANISOU 277 CE LYS A 34 8178 5885 6254 -1525 -1631 953 C ATOM 278 NZ LYS A 34 29.701 53.106 -14.370 1.00 58.46 N ANISOU 278 NZ LYS A 34 8821 6522 6871 -1547 -1617 956 N ATOM 279 N ILE A 35 32.940 53.424 -8.090 1.00 37.35 N ANISOU 279 N ILE A 35 5588 3887 4718 -1629 -1262 465 N ATOM 280 CA ILE A 35 33.917 53.660 -7.033 1.00 34.17 C ANISOU 280 CA ILE A 35 5157 3496 4331 -1618 -1259 452 C ATOM 281 C ILE A 35 33.777 55.072 -6.492 1.00 38.09 C ANISOU 281 C ILE A 35 5643 3980 4851 -1632 -1277 457 C ATOM 282 O ILE A 35 33.840 55.286 -5.281 1.00 38.43 O ANISOU 282 O ILE A 35 5669 4021 4912 -1618 -1286 447 O ATOM 283 CB ILE A 35 35.346 53.417 -7.524 1.00 33.33 C ANISOU 283 CB ILE A 35 5036 3416 4213 -1623 -1236 446 C ATOM 284 CG1 ILE A 35 35.593 51.912 -7.675 1.00 41.59 C ANISOU 284 CG1 ILE A 35 6087 4476 5240 -1602 -1218 434 C ATOM 285 CG2 ILE A 35 36.361 54.049 -6.569 1.00 32.62 C ANISOU 285 CG2 ILE A 35 4917 3337 4142 -1620 -1235 436 C ATOM 286 CD1 ILE A 35 36.871 51.575 -8.440 1.00 47.70 C ANISOU 286 CD1 ILE A 35 6851 5274 5998 -1609 -1194 429 C ATOM 287 N MET A 36 33.569 56.032 -7.392 1.00 35.14 N ANISOU 287 N MET A 36 5278 3596 4478 -1660 -1283 475 N ATOM 288 CA MET A 36 33.452 57.427 -6.994 1.00 41.89 C ANISOU 288 CA MET A 36 6123 4437 5356 -1675 -1300 481 C ATOM 289 C MET A 36 32.340 57.608 -5.964 1.00 43.00 C ANISOU 289 C MET A 36 6266 4558 5516 -1660 -1322 477 C ATOM 290 O MET A 36 32.474 58.400 -5.034 1.00 39.93 O ANISOU 290 O MET A 36 5860 4163 5149 -1659 -1333 471 O ATOM 291 CB MET A 36 33.227 58.334 -8.217 1.00 43.43 C ANISOU 291 CB MET A 36 6332 4623 5548 -1707 -1305 503 C ATOM 292 CG MET A 36 33.192 59.822 -7.876 1.00 53.01 C ANISOU 292 CG MET A 36 7535 5821 6787 -1724 -1322 511 C ATOM 293 SD MET A 36 33.263 60.909 -9.329 1.00 67.68 S ANISOU 293 SD MET A 36 9404 7671 8639 -1764 -1325 537 S ATOM 294 CE MET A 36 34.953 60.660 -9.865 1.00 56.68 C ANISOU 294 CE MET A 36 7995 6312 7230 -1774 -1296 532 C ATOM 295 N HIS A 37 31.249 56.862 -6.120 1.00 37.89 N ANISOU 295 N HIS A 37 5638 3899 4858 -1650 -1327 479 N ATOM 296 CA HIS A 37 30.142 56.915 -5.161 1.00 42.83 C ANISOU 296 CA HIS A 37 6267 4507 5500 -1635 -1346 474 C ATOM 297 C HIS A 37 30.556 56.509 -3.745 1.00 46.46 C ANISOU 297 C HIS A 37 6706 4976 5969 -1610 -1345 454 C ATOM 298 O HIS A 37 30.248 57.192 -2.763 1.00 47.81 O ANISOU 298 O HIS A 37 6866 5138 6162 -1606 -1361 448 O ATOM 299 CB HIS A 37 29.018 55.978 -5.595 1.00 46.85 C ANISOU 299 CB HIS A 37 6801 5006 5993 -1626 -1349 478 C ATOM 300 CG HIS A 37 28.360 56.362 -6.879 1.00 50.74 C ANISOU 300 CG HIS A 37 7316 5486 6476 -1648 -1354 497 C ATOM 301 ND1 HIS A 37 27.397 55.580 -7.479 1.00 47.37 N ANISOU 301 ND1 HIS A 37 6912 5052 6033 -1645 -1355 503 N ATOM 302 CD2 HIS A 37 28.515 57.447 -7.676 1.00 54.90 C ANISOU 302 CD2 HIS A 37 7844 6006 7007 -1676 -1359 513 C ATOM 303 CE1 HIS A 37 26.990 56.164 -8.593 1.00 49.55 C ANISOU 303 CE1 HIS A 37 7203 5320 6303 -1666 -1359 521 C ATOM 304 NE2 HIS A 37 27.654 57.299 -8.734 1.00 48.27 N ANISOU 304 NE2 HIS A 37 7028 5161 6153 -1680 -1359 528 N ATOM 305 N ILE A 38 31.220 55.361 -3.646 1.00 37.75 N ANISOU 305 N ILE A 38 5599 3892 4851 -1593 -1327 444 N ATOM 306 CA ILE A 38 31.616 54.808 -2.363 1.00 33.81 C ANISOU 306 CA ILE A 38 5083 3405 4359 -1568 -1325 426 C ATOM 307 C ILE A 38 32.592 55.732 -1.633 1.00 41.25 C ANISOU 307 C ILE A 38 5999 4356 5320 -1573 -1327 418 C ATOM 308 O ILE A 38 32.435 55.981 -0.432 1.00 40.65 O ANISOU 308 O ILE A 38 5908 4277 5259 -1560 -1338 408 O ATOM 309 CB ILE A 38 32.226 53.387 -2.529 1.00 27.74 C ANISOU 309 CB ILE A 38 4316 2655 3570 -1550 -1305 417 C ATOM 310 CG1 ILE A 38 31.159 52.390 -3.018 1.00 30.94 C ANISOU 310 CG1 ILE A 38 4747 3051 3959 -1542 -1306 422 C ATOM 311 CG2 ILE A 38 32.855 52.911 -1.233 1.00 31.59 C ANISOU 311 CG2 ILE A 38 4782 3156 4065 -1526 -1302 400 C ATOM 312 CD1 ILE A 38 31.722 51.235 -3.844 1.00 27.97 C ANISOU 312 CD1 ILE A 38 4379 2689 3560 -1536 -1285 420 C ATOM 313 N VAL A 39 33.592 56.249 -2.344 1.00 42.86 N ANISOU 313 N VAL A 39 6193 4570 5520 -1591 -1315 424 N ATOM 314 CA VAL A 39 34.577 57.114 -1.683 1.00 42.58 C ANISOU 314 CA VAL A 39 6132 4545 5502 -1596 -1316 417 C ATOM 315 C VAL A 39 33.985 58.462 -1.262 1.00 44.19 C ANISOU 315 C VAL A 39 6332 4728 5730 -1610 -1337 421 C ATOM 316 O VAL A 39 34.398 59.021 -0.254 1.00 48.01 O ANISOU 316 O VAL A 39 6795 5215 6232 -1605 -1343 411 O ATOM 317 CB VAL A 39 35.879 57.313 -2.507 1.00 50.66 C ANISOU 317 CB VAL A 39 7145 5586 6516 -1612 -1297 420 C ATOM 318 CG1 VAL A 39 36.705 56.031 -2.506 1.00 52.09 C ANISOU 318 CG1 VAL A 39 7320 5790 6679 -1593 -1276 408 C ATOM 319 CG2 VAL A 39 35.576 57.765 -3.917 1.00 46.72 C ANISOU 319 CG2 VAL A 39 6665 5078 6007 -1639 -1296 439 C ATOM 320 N LYS A 40 33.013 58.968 -2.017 1.00 45.48 N ANISOU 320 N LYS A 40 6515 4871 5894 -1626 -1349 437 N ATOM 321 CA LYS A 40 32.352 60.220 -1.651 1.00 52.04 C ANISOU 321 CA LYS A 40 7343 5680 6749 -1638 -1371 441 C ATOM 322 C LYS A 40 31.505 60.052 -0.394 1.00 55.90 C ANISOU 322 C LYS A 40 7828 6160 7251 -1616 -1386 428 C ATOM 323 O LYS A 40 31.366 60.975 0.407 1.00 55.20 O ANISOU 323 O LYS A 40 7724 6066 7183 -1611 -1395 422 O ATOM 324 CB LYS A 40 31.481 60.741 -2.793 1.00 53.03 C ANISOU 324 CB LYS A 40 7491 5787 6871 -1655 -1378 461 C ATOM 325 CG LYS A 40 32.248 61.413 -3.916 1.00 58.92 C ANISOU 325 CG LYS A 40 8237 6536 7611 -1684 -1370 476 C ATOM 326 CD LYS A 40 31.291 62.042 -4.924 1.00 66.34 C ANISOU 326 CD LYS A 40 9194 7465 8547 -1688 -1373 496 C ATOM 327 CE LYS A 40 32.028 62.817 -6.009 1.00 69.20 C ANISOU 327 CE LYS A 40 9557 7831 8905 -1717 -1367 512 C ATOM 328 NZ LYS A 40 31.100 63.288 -7.087 1.00 67.40 N ANISOU 328 NZ LYS A 40 9348 7593 8669 -1722 -1370 532 N ATOM 329 N ALA A 41 30.940 58.863 -0.220 1.00 53.90 N ANISOU 329 N ALA A 41 7587 5909 6983 -1596 -1382 423 N ATOM 330 CA ALA A 41 30.101 58.596 0.934 1.00 41.44 C ANISOU 330 CA ALA A 41 6006 4323 5414 -1577 -1395 412 C ATOM 331 C ALA A 41 30.951 58.472 2.189 1.00 45.76 C ANISOU 331 C ALA A 41 6528 4889 5970 -1561 -1391 394 C ATOM 332 O ALA A 41 30.542 58.894 3.268 1.00 56.01 O ANISOU 332 O ALA A 41 7815 6180 7285 -1553 -1405 383 O ATOM 333 CB ALA A 41 29.268 57.321 0.712 1.00 48.30 C ANISOU 333 CB ALA A 41 6896 5191 6264 -1561 -1391 413 C ATOM 334 N LEU A 42 32.135 57.882 2.035 1.00 39.16 N ANISOU 334 N LEU A 42 5682 4074 5121 -1556 -1372 389 N ATOM 335 CA LEU A 42 33.077 57.696 3.129 1.00 41.92 C ANISOU 335 CA LEU A 42 6007 4444 5477 -1541 -1366 373 C ATOM 336 C LEU A 42 33.881 58.966 3.377 1.00 45.63 C ANISOU 336 C LEU A 42 6455 4916 5966 -1557 -1370 371 C ATOM 337 O LEU A 42 34.568 59.084 4.386 1.00 43.94 O ANISOU 337 O LEU A 42 6219 4716 5762 -1547 -1370 357 O ATOM 338 CB LEU A 42 34.058 56.571 2.780 1.00 44.53 C ANISOU 338 CB LEU A 42 6335 4796 5787 -1530 -1345 370 C ATOM 339 CG LEU A 42 33.509 55.146 2.777 1.00 42.87 C ANISOU 339 CG LEU A 42 6141 4588 5559 -1509 -1339 368 C ATOM 340 CD1 LEU A 42 34.445 54.206 2.027 1.00 40.09 C ANISOU 340 CD1 LEU A 42 5790 4254 5187 -1505 -1317 368 C ATOM 341 CD2 LEU A 42 33.290 54.686 4.211 1.00 35.45 C ANISOU 341 CD2 LEU A 42 5189 3653 4625 -1485 -1347 353 C ATOM 342 N ASP A 43 33.810 59.893 2.431 1.00 46.72 N ANISOU 342 N ASP A 43 6601 5041 6109 -1582 -1373 385 N ATOM 343 CA ASP A 43 34.680 61.074 2.430 1.00 56.22 C ANISOU 343 CA ASP A 43 7786 6247 7328 -1601 -1374 385 C ATOM 344 C ASP A 43 36.155 60.697 2.638 1.00 53.69 C ANISOU 344 C ASP A 43 7445 5955 7001 -1595 -1356 376 C ATOM 345 O ASP A 43 36.811 61.194 3.548 1.00 48.88 O ANISOU 345 O ASP A 43 6812 5354 6407 -1592 -1359 364 O ATOM 346 CB ASP A 43 34.218 62.115 3.459 1.00 52.39 C ANISOU 346 CB ASP A 43 7288 5749 6870 -1602 -1395 377 C ATOM 347 CG ASP A 43 34.844 63.488 3.228 1.00 59.66 C ANISOU 347 CG ASP A 43 8196 6664 7809 -1626 -1399 382 C ATOM 348 OD1 ASP A 43 35.054 63.869 2.054 1.00 62.91 O ANISOU 348 OD1 ASP A 43 8617 7071 8215 -1647 -1394 398 O ATOM 349 OD2 ASP A 43 35.122 64.188 4.225 1.00 57.35 O ANISOU 349 OD2 ASP A 43 7882 6374 7536 -1621 -1406 369 O ATOM 350 N ILE A 44 36.653 59.787 1.804 1.00 47.24 N ANISOU 350 N ILE A 44 6635 5151 6161 -1593 -1337 380 N ATOM 351 CA ILE A 44 38.071 59.459 1.765 1.00 41.57 C ANISOU 351 CA ILE A 44 5900 4460 5437 -1591 -1319 373 C ATOM 352 C ILE A 44 38.581 59.655 0.342 1.00 39.84 C ANISOU 352 C ILE A 44 5689 4244 5204 -1614 -1305 387 C ATOM 353 O ILE A 44 37.791 59.663 -0.604 1.00 43.02 O ANISOU 353 O ILE A 44 6115 4632 5598 -1626 -1308 402 O ATOM 354 CB ILE A 44 38.359 58.011 2.223 1.00 43.32 C ANISOU 354 CB ILE A 44 6119 4698 5642 -1563 -1306 361 C ATOM 355 CG1 ILE A 44 37.822 56.985 1.225 1.00 45.29 C ANISOU 355 CG1 ILE A 44 6394 4945 5869 -1559 -1297 370 C ATOM 356 CG2 ILE A 44 37.775 57.744 3.611 1.00 48.47 C ANISOU 356 CG2 ILE A 44 6765 5347 6305 -1540 -1320 348 C ATOM 357 CD1 ILE A 44 38.046 55.560 1.689 1.00 42.82 C ANISOU 357 CD1 ILE A 44 6080 4647 5544 -1531 -1287 359 C ATOM 358 N PRO A 45 39.901 59.826 0.183 1.00 42.28 N ANISOU 358 N PRO A 45 5978 4573 5511 -1621 -1290 383 N ATOM 359 CA PRO A 45 40.465 59.990 -1.162 1.00 44.12 C ANISOU 359 CA PRO A 45 6219 4814 5731 -1644 -1276 396 C ATOM 360 C PRO A 45 40.304 58.738 -2.020 1.00 37.82 C ANISOU 360 C PRO A 45 5439 4023 4907 -1635 -1261 399 C ATOM 361 O PRO A 45 40.302 57.604 -1.528 1.00 40.45 O ANISOU 361 O PRO A 45 5772 4365 5231 -1610 -1255 387 O ATOM 362 CB PRO A 45 41.947 60.304 -0.899 1.00 51.87 C ANISOU 362 CB PRO A 45 7172 5818 6717 -1648 -1263 386 C ATOM 363 CG PRO A 45 42.214 59.827 0.486 1.00 51.73 C ANISOU 363 CG PRO A 45 7136 5811 6709 -1621 -1266 367 C ATOM 364 CD PRO A 45 40.922 59.915 1.241 1.00 45.62 C ANISOU 364 CD PRO A 45 6373 5015 5946 -1610 -1287 366 C ATOM 365 N ARG A 46 40.151 58.964 -3.316 1.00 43.75 N ANISOU 365 N ARG A 46 6207 4770 5646 -1658 -1255 415 N ATOM 366 CA ARG A 46 39.910 57.903 -4.290 1.00 43.45 C ANISOU 366 CA ARG A 46 6189 4737 5583 -1654 -1242 419 C ATOM 367 C ARG A 46 41.000 56.830 -4.268 1.00 42.52 C ANISOU 367 C ARG A 46 6058 4646 5451 -1637 -1220 405 C ATOM 368 O ARG A 46 40.714 55.625 -4.344 1.00 35.66 O ANISOU 368 O ARG A 46 5201 3782 4568 -1618 -1212 400 O ATOM 369 CB ARG A 46 39.792 58.533 -5.682 1.00 50.72 C ANISOU 369 CB ARG A 46 7125 5652 6493 -1685 -1239 439 C ATOM 370 CG ARG A 46 39.487 57.562 -6.791 1.00 46.03 C ANISOU 370 CG ARG A 46 6554 5063 5874 -1686 -1226 445 C ATOM 371 CD ARG A 46 39.415 58.257 -8.175 1.00 42.39 C ANISOU 371 CD ARG A 46 6107 4598 5402 -1719 -1224 465 C ATOM 372 NE ARG A 46 39.242 57.218 -9.178 1.00 38.77 N ANISOU 372 NE ARG A 46 5667 4148 4917 -1717 -1209 468 N ATOM 373 CZ ARG A 46 38.112 56.522 -9.305 1.00 53.59 C ANISOU 373 CZ ARG A 46 7566 6010 6785 -1705 -1216 471 C ATOM 374 NH1 ARG A 46 37.077 56.807 -8.527 1.00 63.96 N ANISOU 374 NH1 ARG A 46 8885 7301 8114 -1696 -1238 472 N ATOM 375 NH2 ARG A 46 38.000 55.557 -10.209 1.00 46.85 N ANISOU 375 NH2 ARG A 46 6728 5165 5907 -1703 -1202 471 N ATOM 376 N GLY A 47 42.251 57.267 -4.150 1.00 41.22 N ANISOU 376 N GLY A 47 5869 4500 5291 -1645 -1209 399 N ATOM 377 CA GLY A 47 43.371 56.349 -4.017 1.00 39.51 C ANISOU 377 CA GLY A 47 5637 4311 5065 -1629 -1189 384 C ATOM 378 C GLY A 47 43.231 55.311 -2.912 1.00 38.57 C ANISOU 378 C GLY A 47 5512 4195 4948 -1594 -1191 368 C ATOM 379 O GLY A 47 43.747 54.201 -3.043 1.00 37.78 O ANISOU 379 O GLY A 47 5410 4111 4835 -1577 -1176 358 O ATOM 380 N SER A 48 42.553 55.664 -1.817 1.00 38.89 N ANISOU 380 N SER A 48 5550 4220 5005 -1584 -1211 365 N ATOM 381 CA SER A 48 42.333 54.724 -0.718 1.00 40.36 C ANISOU 381 CA SER A 48 5732 4409 5194 -1552 -1215 352 C ATOM 382 C SER A 48 41.504 53.502 -1.112 1.00 44.77 C ANISOU 382 C SER A 48 6314 4960 5735 -1537 -1212 354 C ATOM 383 O SER A 48 41.750 52.388 -0.631 1.00 44.57 O ANISOU 383 O SER A 48 6286 4946 5705 -1512 -1205 342 O ATOM 384 CB SER A 48 41.680 55.422 0.486 1.00 53.11 C ANISOU 384 CB SER A 48 7341 6009 6830 -1547 -1237 349 C ATOM 385 OG SER A 48 42.549 56.379 1.066 1.00 52.83 O ANISOU 385 OG SER A 48 7279 5983 6811 -1556 -1240 343 O ATOM 386 N PHE A 49 40.505 53.695 -1.965 1.00 40.89 N ANISOU 386 N PHE A 49 5848 4451 5237 -1551 -1218 368 N ATOM 387 CA PHE A 49 39.699 52.548 -2.383 1.00 36.29 C ANISOU 387 CA PHE A 49 5289 3862 4638 -1538 -1215 370 C ATOM 388 C PHE A 49 40.594 51.468 -2.981 1.00 31.03 C ANISOU 388 C PHE A 49 4620 3216 3954 -1529 -1192 362 C ATOM 389 O PHE A 49 40.434 50.276 -2.705 1.00 37.39 O ANISOU 389 O PHE A 49 5430 4024 4751 -1505 -1187 354 O ATOM 390 CB PHE A 49 38.635 52.947 -3.405 1.00 28.60 C ANISOU 390 CB PHE A 49 4341 2868 3657 -1558 -1222 387 C ATOM 391 CG PHE A 49 37.827 51.778 -3.899 1.00 33.61 C ANISOU 391 CG PHE A 49 5000 3496 4274 -1546 -1219 389 C ATOM 392 CD1 PHE A 49 36.632 51.444 -3.290 1.00 35.46 C ANISOU 392 CD1 PHE A 49 5248 3713 4513 -1532 -1234 389 C ATOM 393 CD2 PHE A 49 38.287 50.990 -4.941 1.00 34.89 C ANISOU 393 CD2 PHE A 49 5170 3671 4415 -1548 -1199 388 C ATOM 394 CE1 PHE A 49 35.892 50.365 -3.728 1.00 39.20 C ANISOU 394 CE1 PHE A 49 5743 4180 4970 -1521 -1231 390 C ATOM 395 CE2 PHE A 49 37.551 49.907 -5.385 1.00 36.08 C ANISOU 395 CE2 PHE A 49 5343 3816 4551 -1537 -1196 389 C ATOM 396 CZ PHE A 49 36.354 49.596 -4.775 1.00 36.45 C ANISOU 396 CZ PHE A 49 5403 3844 4602 -1524 -1212 390 C ATOM 397 N TYR A 50 41.543 51.899 -3.803 1.00 31.78 N ANISOU 397 N TYR A 50 4706 3325 4043 -1548 -1178 364 N ATOM 398 CA TYR A 50 42.425 50.966 -4.505 1.00 31.69 C ANISOU 398 CA TYR A 50 4691 3335 4014 -1542 -1155 357 C ATOM 399 C TYR A 50 43.451 50.330 -3.589 1.00 42.21 C ANISOU 399 C TYR A 50 5999 4687 5353 -1518 -1146 339 C ATOM 400 O TYR A 50 44.077 49.329 -3.947 1.00 41.33 O ANISOU 400 O TYR A 50 5884 4590 5228 -1505 -1129 329 O ATOM 401 CB TYR A 50 43.119 51.656 -5.674 1.00 35.52 C ANISOU 401 CB TYR A 50 5174 3832 4491 -1571 -1141 365 C ATOM 402 CG TYR A 50 42.161 52.018 -6.778 1.00 43.07 C ANISOU 402 CG TYR A 50 6156 4771 5436 -1594 -1146 383 C ATOM 403 CD1 TYR A 50 41.795 51.085 -7.742 1.00 47.71 C ANISOU 403 CD1 TYR A 50 6766 5361 6003 -1592 -1135 385 C ATOM 404 CD2 TYR A 50 41.615 53.290 -6.852 1.00 48.16 C ANISOU 404 CD2 TYR A 50 6806 5399 6092 -1617 -1162 397 C ATOM 405 CE1 TYR A 50 40.908 51.419 -8.763 1.00 44.18 C ANISOU 405 CE1 TYR A 50 6343 4899 5544 -1613 -1140 401 C ATOM 406 CE2 TYR A 50 40.730 53.631 -7.857 1.00 47.16 C ANISOU 406 CE2 TYR A 50 6704 5258 5956 -1637 -1168 415 C ATOM 407 CZ TYR A 50 40.381 52.696 -8.811 1.00 46.54 C ANISOU 407 CZ TYR A 50 6646 5182 5855 -1636 -1157 417 C ATOM 408 OH TYR A 50 39.507 53.054 -9.815 1.00 41.60 O ANISOU 408 OH TYR A 50 6044 4542 5219 -1657 -1163 434 O ATOM 409 N GLN A 51 43.619 50.901 -2.400 1.00 40.31 N ANISOU 409 N GLN A 51 5740 4445 5131 -1511 -1159 334 N ATOM 410 CA GLN A 51 44.452 50.243 -1.406 1.00 43.10 C ANISOU 410 CA GLN A 51 6072 4815 5491 -1485 -1154 317 C ATOM 411 C GLN A 51 43.694 49.077 -0.806 1.00 46.58 C ANISOU 411 C GLN A 51 6525 5247 5927 -1457 -1161 312 C ATOM 412 O GLN A 51 44.295 48.078 -0.407 1.00 47.73 O ANISOU 412 O GLN A 51 6661 5406 6070 -1434 -1152 300 O ATOM 413 CB GLN A 51 44.863 51.212 -0.304 1.00 33.13 C ANISOU 413 CB GLN A 51 4785 3555 4248 -1487 -1166 313 C ATOM 414 CG GLN A 51 45.641 52.413 -0.802 1.00 42.68 C ANISOU 414 CG GLN A 51 5980 4772 5464 -1515 -1161 317 C ATOM 415 CD GLN A 51 46.569 52.965 0.267 1.00 57.26 C ANISOU 415 CD GLN A 51 7797 6633 7328 -1510 -1165 306 C ATOM 416 OE1 GLN A 51 46.178 53.811 1.081 1.00 57.04 O ANISOU 416 OE1 GLN A 51 7763 6594 7316 -1514 -1182 307 O ATOM 417 NE2 GLN A 51 47.804 52.478 0.276 1.00 53.64 N ANISOU 417 NE2 GLN A 51 7317 6198 6865 -1501 -1148 294 N ATOM 418 N TYR A 52 42.375 49.234 -0.696 1.00 34.33 N ANISOU 418 N TYR A 52 4995 3673 4378 -1459 -1177 322 N ATOM 419 CA TYR A 52 41.521 48.204 -0.103 1.00 33.00 C ANISOU 419 CA TYR A 52 4840 3494 4206 -1435 -1184 319 C ATOM 420 C TYR A 52 41.085 47.116 -1.085 1.00 43.16 C ANISOU 420 C TYR A 52 6149 4776 5473 -1430 -1173 321 C ATOM 421 O TYR A 52 40.871 45.961 -0.698 1.00 38.42 O ANISOU 421 O TYR A 52 5555 4176 4869 -1406 -1172 315 O ATOM 422 CB TYR A 52 40.301 48.847 0.576 1.00 35.80 C ANISOU 422 CB TYR A 52 5203 3826 4572 -1438 -1207 326 C ATOM 423 CG TYR A 52 40.659 49.977 1.527 1.00 38.57 C ANISOU 423 CG TYR A 52 5533 4180 4943 -1444 -1219 322 C ATOM 424 CD1 TYR A 52 41.797 49.914 2.325 1.00 42.93 C ANISOU 424 CD1 TYR A 52 6057 4751 5502 -1432 -1213 310 C ATOM 425 CD2 TYR A 52 39.866 51.114 1.614 1.00 40.03 C ANISOU 425 CD2 TYR A 52 5724 4348 5140 -1462 -1235 331 C ATOM 426 CE1 TYR A 52 42.127 50.957 3.196 1.00 48.04 C ANISOU 426 CE1 TYR A 52 6683 5401 6167 -1438 -1224 306 C ATOM 427 CE2 TYR A 52 40.185 52.156 2.476 1.00 47.24 C ANISOU 427 CE2 TYR A 52 6615 5262 6071 -1468 -1246 327 C ATOM 428 CZ TYR A 52 41.315 52.073 3.266 1.00 52.53 C ANISOU 428 CZ TYR A 52 7259 5952 6748 -1456 -1240 314 C ATOM 429 OH TYR A 52 41.623 53.108 4.123 1.00 54.85 O ANISOU 429 OH TYR A 52 7533 6248 7060 -1462 -1251 310 O ATOM 430 N PHE A 53 40.928 47.495 -2.352 1.00 40.53 N ANISOU 430 N PHE A 53 5830 4440 5129 -1454 -1166 332 N ATOM 431 CA PHE A 53 40.415 46.581 -3.358 1.00 34.92 C ANISOU 431 CA PHE A 53 5144 3725 4400 -1452 -1157 335 C ATOM 432 C PHE A 53 41.177 46.687 -4.673 1.00 38.62 C ANISOU 432 C PHE A 53 5612 4208 4855 -1472 -1138 337 C ATOM 433 O PHE A 53 41.664 47.756 -5.044 1.00 43.52 O ANISOU 433 O PHE A 53 6222 4834 5478 -1495 -1136 343 O ATOM 434 CB PHE A 53 38.927 46.856 -3.627 1.00 35.68 C ANISOU 434 CB PHE A 53 5267 3797 4495 -1462 -1173 348 C ATOM 435 CG PHE A 53 38.066 46.805 -2.395 1.00 37.25 C ANISOU 435 CG PHE A 53 5466 3981 4706 -1446 -1192 347 C ATOM 436 CD1 PHE A 53 37.640 45.588 -1.884 1.00 34.78 C ANISOU 436 CD1 PHE A 53 5162 3665 4389 -1420 -1193 340 C ATOM 437 CD2 PHE A 53 37.683 47.973 -1.755 1.00 33.97 C ANISOU 437 CD2 PHE A 53 5044 3556 4307 -1457 -1209 352 C ATOM 438 CE1 PHE A 53 36.845 45.534 -0.745 1.00 40.29 C ANISOU 438 CE1 PHE A 53 5860 4350 5097 -1406 -1211 339 C ATOM 439 CE2 PHE A 53 36.896 47.930 -0.624 1.00 38.59 C ANISOU 439 CE2 PHE A 53 5630 4129 4904 -1442 -1227 350 C ATOM 440 CZ PHE A 53 36.476 46.709 -0.112 1.00 38.37 C ANISOU 440 CZ PHE A 53 5610 4099 4870 -1417 -1227 344 C ATOM 441 N GLU A 54 41.245 45.568 -5.387 1.00 45.07 N ANISOU 441 N GLU A 54 6440 5030 5655 -1463 -1123 332 N ATOM 442 CA GLU A 54 41.783 45.535 -6.743 1.00 45.40 C ANISOU 442 CA GLU A 54 6486 5084 5679 -1481 -1104 333 C ATOM 443 C GLU A 54 41.040 46.516 -7.644 1.00 44.36 C ANISOU 443 C GLU A 54 6373 4941 5543 -1512 -1111 352 C ATOM 444 O GLU A 54 41.649 47.361 -8.302 1.00 48.34 O ANISOU 444 O GLU A 54 6869 5455 6044 -1536 -1104 357 O ATOM 445 CB GLU A 54 41.665 44.123 -7.320 1.00 57.47 C ANISOU 445 CB GLU A 54 8028 6615 7191 -1465 -1091 325 C ATOM 446 CG GLU A 54 42.818 43.732 -8.219 1.00 66.36 C ANISOU 446 CG GLU A 54 9144 7765 8304 -1470 -1066 316 C ATOM 447 CD GLU A 54 44.149 43.850 -7.501 1.00 70.56 C ANISOU 447 CD GLU A 54 9644 8317 8848 -1459 -1059 303 C ATOM 448 OE1 GLU A 54 44.331 43.167 -6.466 1.00 65.81 O ANISOU 448 OE1 GLU A 54 9033 7716 8257 -1432 -1063 292 O ATOM 449 OE2 GLU A 54 45.002 44.639 -7.959 1.00 74.84 O ANISOU 449 OE2 GLU A 54 10171 8875 9389 -1479 -1049 304 O ATOM 450 N ASP A 55 39.718 46.390 -7.662 1.00 46.77 N ANISOU 450 N ASP A 55 6701 5224 5846 -1511 -1126 361 N ATOM 451 CA ASP A 55 38.840 47.201 -8.504 1.00 46.68 C ANISOU 451 CA ASP A 55 6709 5198 5828 -1538 -1135 379 C ATOM 452 C ASP A 55 37.424 47.083 -7.948 1.00 42.95 C ANISOU 452 C ASP A 55 6256 4701 5363 -1528 -1155 385 C ATOM 453 O ASP A 55 37.231 46.496 -6.887 1.00 39.11 O ANISOU 453 O ASP A 55 5763 4210 4885 -1503 -1162 376 O ATOM 454 CB ASP A 55 38.883 46.717 -9.958 1.00 50.73 C ANISOU 454 CB ASP A 55 7238 5718 6317 -1551 -1118 382 C ATOM 455 CG ASP A 55 38.705 45.209 -10.081 1.00 56.03 C ANISOU 455 CG ASP A 55 7921 6392 6976 -1528 -1108 371 C ATOM 456 OD1 ASP A 55 38.095 44.595 -9.175 1.00 46.67 O ANISOU 456 OD1 ASP A 55 6739 5194 5798 -1505 -1119 366 O ATOM 457 OD2 ASP A 55 39.174 44.637 -11.088 1.00 58.90 O ANISOU 457 OD2 ASP A 55 8288 6769 7321 -1533 -1089 366 O ATOM 458 N LEU A 56 36.436 47.624 -8.656 1.00 38.89 N ANISOU 458 N LEU A 56 5763 4171 4844 -1548 -1166 401 N ATOM 459 CA LEU A 56 35.045 47.519 -8.218 1.00 42.16 C ANISOU 459 CA LEU A 56 6194 4562 5263 -1540 -1185 407 C ATOM 460 C LEU A 56 34.581 46.069 -8.080 1.00 43.80 C ANISOU 460 C LEU A 56 6415 4767 5461 -1516 -1180 397 C ATOM 461 O LEU A 56 33.866 45.725 -7.145 1.00 39.77 O ANISOU 461 O LEU A 56 5907 4244 4959 -1498 -1193 394 O ATOM 462 CB LEU A 56 34.108 48.231 -9.189 1.00 41.75 C ANISOU 462 CB LEU A 56 6164 4495 5206 -1566 -1195 425 C ATOM 463 CG LEU A 56 33.147 49.312 -8.673 1.00 50.87 C ANISOU 463 CG LEU A 56 7323 5628 6378 -1575 -1219 436 C ATOM 464 CD1 LEU A 56 31.913 49.374 -9.573 1.00 38.91 C ANISOU 464 CD1 LEU A 56 5835 4095 4852 -1589 -1229 451 C ATOM 465 CD2 LEU A 56 32.745 49.153 -7.195 1.00 36.75 C ANISOU 465 CD2 LEU A 56 5525 3831 4608 -1551 -1233 427 C ATOM 466 N LYS A 57 34.978 45.228 -9.029 1.00 39.81 N ANISOU 466 N LYS A 57 5917 4273 4936 -1516 -1162 393 N ATOM 467 CA LYS A 57 34.549 43.837 -9.044 1.00 36.33 C ANISOU 467 CA LYS A 57 5491 3830 4485 -1494 -1156 385 C ATOM 468 C LYS A 57 35.015 43.119 -7.784 1.00 34.61 C ANISOU 468 C LYS A 57 5255 3616 4278 -1465 -1156 370 C ATOM 469 O LYS A 57 34.291 42.297 -7.224 1.00 33.32 O ANISOU 469 O LYS A 57 5102 3442 4116 -1445 -1164 366 O ATOM 470 CB LYS A 57 35.090 43.129 -10.290 1.00 38.10 C ANISOU 470 CB LYS A 57 5721 4067 4686 -1501 -1135 380 C ATOM 471 CG LYS A 57 34.370 41.830 -10.635 1.00 49.74 C ANISOU 471 CG LYS A 57 7217 5535 6148 -1486 -1131 376 C ATOM 472 CD LYS A 57 35.029 41.151 -11.838 1.00 56.71 C ANISOU 472 CD LYS A 57 8104 6434 7009 -1492 -1108 369 C ATOM 473 CE LYS A 57 36.393 40.587 -11.450 1.00 67.83 C ANISOU 473 CE LYS A 57 9488 7862 8421 -1475 -1091 351 C ATOM 474 NZ LYS A 57 37.372 40.623 -12.574 1.00 76.11 N ANISOU 474 NZ LYS A 57 10531 8933 9455 -1490 -1070 347 N ATOM 475 N ASP A 58 36.227 43.431 -7.337 1.00 35.93 N ANISOU 475 N ASP A 58 5397 3800 4454 -1461 -1148 362 N ATOM 476 CA ASP A 58 36.760 42.857 -6.101 1.00 34.56 C ANISOU 476 CA ASP A 58 5205 3633 4292 -1434 -1149 348 C ATOM 477 C ASP A 58 35.782 43.117 -4.944 1.00 33.22 C ANISOU 477 C ASP A 58 5038 3446 4137 -1425 -1171 352 C ATOM 478 O ASP A 58 35.398 42.191 -4.221 1.00 34.20 O ANISOU 478 O ASP A 58 5167 3565 4263 -1401 -1176 346 O ATOM 479 CB ASP A 58 38.144 43.462 -5.795 1.00 34.72 C ANISOU 479 CB ASP A 58 5197 3674 4322 -1437 -1140 341 C ATOM 480 CG ASP A 58 38.818 42.831 -4.575 1.00 44.30 C ANISOU 480 CG ASP A 58 6390 4897 5546 -1409 -1140 327 C ATOM 481 OD1 ASP A 58 38.180 41.999 -3.894 1.00 41.09 O ANISOU 481 OD1 ASP A 58 5991 4479 5141 -1388 -1148 324 O ATOM 482 OD2 ASP A 58 39.992 43.184 -4.294 1.00 47.46 O ANISOU 482 OD2 ASP A 58 6765 5314 5953 -1409 -1132 320 O ATOM 483 N ALA A 59 35.383 44.381 -4.785 1.00 31.07 N ANISOU 483 N ALA A 59 4765 3165 3876 -1443 -1185 362 N ATOM 484 CA ALA A 59 34.480 44.786 -3.710 1.00 37.68 C ANISOU 484 CA ALA A 59 5602 3987 4728 -1436 -1207 365 C ATOM 485 C ALA A 59 33.097 44.172 -3.890 1.00 32.97 C ANISOU 485 C ALA A 59 5032 3371 4124 -1432 -1216 371 C ATOM 486 O ALA A 59 32.445 43.788 -2.920 1.00 33.73 O ANISOU 486 O ALA A 59 5129 3458 4227 -1415 -1228 368 O ATOM 487 CB ALA A 59 34.379 46.306 -3.644 1.00 31.96 C ANISOU 487 CB ALA A 59 4870 3256 4016 -1459 -1219 375 C ATOM 488 N TYR A 60 32.643 44.104 -5.134 1.00 31.59 N ANISOU 488 N TYR A 60 4878 3191 3935 -1448 -1211 380 N ATOM 489 CA TYR A 60 31.339 43.525 -5.436 1.00 33.47 C ANISOU 489 CA TYR A 60 5141 3411 4164 -1445 -1219 386 C ATOM 490 C TYR A 60 31.286 42.050 -5.040 1.00 33.41 C ANISOU 490 C TYR A 60 5138 3405 4150 -1419 -1212 375 C ATOM 491 O TYR A 60 30.356 41.616 -4.343 1.00 31.81 O ANISOU 491 O TYR A 60 4945 3189 3951 -1406 -1225 375 O ATOM 492 CB TYR A 60 31.003 43.702 -6.930 1.00 32.00 C ANISOU 492 CB TYR A 60 4975 3223 3962 -1468 -1213 397 C ATOM 493 CG TYR A 60 29.640 43.192 -7.323 1.00 30.54 C ANISOU 493 CG TYR A 60 4816 3019 3767 -1468 -1222 403 C ATOM 494 CD1 TYR A 60 28.509 43.553 -6.608 1.00 35.81 C ANISOU 494 CD1 TYR A 60 5490 3669 4446 -1465 -1242 409 C ATOM 495 CD2 TYR A 60 29.475 42.376 -8.433 1.00 32.83 C ANISOU 495 CD2 TYR A 60 5125 3311 4037 -1471 -1210 404 C ATOM 496 CE1 TYR A 60 27.254 43.099 -6.973 1.00 32.79 C ANISOU 496 CE1 TYR A 60 5132 3271 4057 -1466 -1251 415 C ATOM 497 CE2 TYR A 60 28.229 41.928 -8.806 1.00 33.89 C ANISOU 497 CE2 TYR A 60 5284 3430 4164 -1472 -1218 410 C ATOM 498 CZ TYR A 60 27.122 42.292 -8.077 1.00 35.63 C ANISOU 498 CZ TYR A 60 5510 3632 4396 -1469 -1239 416 C ATOM 499 OH TYR A 60 25.874 41.836 -8.447 1.00 31.09 O ANISOU 499 OH TYR A 60 4959 3042 3813 -1470 -1247 421 O ATOM 500 N PHE A 61 32.283 41.285 -5.485 1.00 29.86 N ANISOU 500 N PHE A 61 4683 2972 3690 -1411 -1193 366 N ATOM 501 CA PHE A 61 32.334 39.851 -5.199 1.00 32.99 C ANISOU 501 CA PHE A 61 5084 3369 4080 -1386 -1186 355 C ATOM 502 C PHE A 61 32.531 39.609 -3.706 1.00 35.92 C ANISOU 502 C PHE A 61 5439 3742 4467 -1363 -1195 347 C ATOM 503 O PHE A 61 32.007 38.636 -3.156 1.00 34.72 O ANISOU 503 O PHE A 61 5295 3583 4315 -1344 -1199 344 O ATOM 504 CB PHE A 61 33.447 39.159 -5.996 1.00 36.09 C ANISOU 504 CB PHE A 61 5471 3780 4462 -1383 -1163 345 C ATOM 505 CG PHE A 61 33.097 38.909 -7.446 1.00 40.07 C ANISOU 505 CG PHE A 61 5996 4283 4947 -1399 -1153 350 C ATOM 506 CD1 PHE A 61 31.838 39.226 -7.937 1.00 40.17 C ANISOU 506 CD1 PHE A 61 6031 4277 4953 -1413 -1165 363 C ATOM 507 CD2 PHE A 61 34.021 38.339 -8.310 1.00 43.80 C ANISOU 507 CD2 PHE A 61 6465 4771 5406 -1399 -1132 341 C ATOM 508 CE1 PHE A 61 31.504 38.985 -9.275 1.00 38.72 C ANISOU 508 CE1 PHE A 61 5867 4093 4751 -1429 -1156 367 C ATOM 509 CE2 PHE A 61 33.698 38.101 -9.646 1.00 44.61 C ANISOU 509 CE2 PHE A 61 6587 4873 5490 -1415 -1122 345 C ATOM 510 CZ PHE A 61 32.436 38.419 -10.123 1.00 37.64 C ANISOU 510 CZ PHE A 61 5727 3973 4601 -1430 -1135 358 C ATOM 511 N TYR A 62 33.275 40.495 -3.044 1.00 32.79 N ANISOU 511 N TYR A 62 5019 3355 4084 -1366 -1198 345 N ATOM 512 CA TYR A 62 33.445 40.339 -1.605 1.00 31.68 C ANISOU 512 CA TYR A 62 4862 3217 3957 -1346 -1207 339 C ATOM 513 C TYR A 62 32.096 40.465 -0.908 1.00 33.73 C ANISOU 513 C TYR A 62 5135 3458 4223 -1343 -1227 345 C ATOM 514 O TYR A 62 31.691 39.580 -0.146 1.00 34.27 O ANISOU 514 O TYR A 62 5207 3522 4292 -1323 -1232 341 O ATOM 515 CB TYR A 62 34.464 41.327 -1.030 1.00 32.91 C ANISOU 515 CB TYR A 62 4990 3386 4126 -1351 -1207 335 C ATOM 516 CG TYR A 62 34.703 41.112 0.454 1.00 40.11 C ANISOU 516 CG TYR A 62 5885 4303 5051 -1330 -1216 327 C ATOM 517 CD1 TYR A 62 35.321 39.954 0.912 1.00 43.25 C ANISOU 517 CD1 TYR A 62 6275 4710 5447 -1305 -1208 317 C ATOM 518 CD2 TYR A 62 34.310 42.063 1.396 1.00 37.64 C ANISOU 518 CD2 TYR A 62 5563 3986 4754 -1334 -1233 330 C ATOM 519 CE1 TYR A 62 35.546 39.740 2.266 1.00 48.29 C ANISOU 519 CE1 TYR A 62 6898 5353 6096 -1286 -1217 311 C ATOM 520 CE2 TYR A 62 34.537 41.859 2.767 1.00 43.21 C ANISOU 520 CE2 TYR A 62 6252 4696 5469 -1315 -1241 322 C ATOM 521 CZ TYR A 62 35.158 40.693 3.189 1.00 49.84 C ANISOU 521 CZ TYR A 62 7085 5546 6305 -1292 -1233 314 C ATOM 522 OH TYR A 62 35.389 40.468 4.535 1.00 46.99 O ANISOU 522 OH TYR A 62 6709 5192 5954 -1274 -1242 308 O ATOM 523 N VAL A 63 31.384 41.549 -1.189 1.00 31.37 N ANISOU 523 N VAL A 63 4843 3149 3929 -1364 -1238 355 N ATOM 524 CA VAL A 63 30.054 41.748 -0.614 1.00 31.13 C ANISOU 524 CA VAL A 63 4824 3101 3904 -1364 -1257 361 C ATOM 525 C VAL A 63 29.115 40.589 -0.931 1.00 39.20 C ANISOU 525 C VAL A 63 5870 4111 4914 -1354 -1257 362 C ATOM 526 O VAL A 63 28.377 40.116 -0.060 1.00 33.30 O ANISOU 526 O VAL A 63 5127 3355 4170 -1340 -1267 360 O ATOM 527 CB VAL A 63 29.414 43.076 -1.088 1.00 29.62 C ANISOU 527 CB VAL A 63 4638 2898 3718 -1389 -1268 372 C ATOM 528 CG1 VAL A 63 27.928 43.109 -0.705 1.00 29.15 C ANISOU 528 CG1 VAL A 63 4594 2818 3662 -1388 -1286 377 C ATOM 529 CG2 VAL A 63 30.164 44.271 -0.488 1.00 32.58 C ANISOU 529 CG2 VAL A 63 4988 3280 4109 -1397 -1273 370 C ATOM 530 N LEU A 64 29.124 40.127 -2.178 1.00 30.30 N ANISOU 530 N LEU A 64 4759 2983 3771 -1362 -1244 365 N ATOM 531 CA LEU A 64 28.293 38.974 -2.518 1.00 32.86 C ANISOU 531 CA LEU A 64 5105 3296 4083 -1352 -1243 365 C ATOM 532 C LEU A 64 28.677 37.739 -1.720 1.00 30.25 C ANISOU 532 C LEU A 64 4770 2972 3753 -1325 -1238 355 C ATOM 533 O LEU A 64 27.806 37.007 -1.237 1.00 34.07 O ANISOU 533 O LEU A 64 5265 3444 4235 -1313 -1246 355 O ATOM 534 CB LEU A 64 28.353 38.647 -4.017 1.00 31.60 C ANISOU 534 CB LEU A 64 4962 3138 3906 -1365 -1229 368 C ATOM 535 CG LEU A 64 27.685 39.635 -4.982 1.00 38.49 C ANISOU 535 CG LEU A 64 5847 4002 4774 -1392 -1235 381 C ATOM 536 CD1 LEU A 64 27.759 39.094 -6.412 1.00 35.96 C ANISOU 536 CD1 LEU A 64 5544 3685 4435 -1402 -1221 383 C ATOM 537 CD2 LEU A 64 26.228 39.881 -4.584 1.00 36.63 C ANISOU 537 CD2 LEU A 64 5627 3747 4544 -1395 -1255 389 C ATOM 538 N SER A 65 29.972 37.478 -1.609 1.00 31.95 N ANISOU 538 N SER A 65 4966 3203 3969 -1316 -1225 346 N ATOM 539 CA SER A 65 30.401 36.264 -0.929 1.00 42.26 C ANISOU 539 CA SER A 65 6267 4514 5275 -1290 -1220 336 C ATOM 540 C SER A 65 30.037 36.365 0.547 1.00 42.11 C ANISOU 540 C SER A 65 6238 4492 5269 -1277 -1236 336 C ATOM 541 O SER A 65 29.769 35.363 1.200 1.00 43.43 O ANISOU 541 O SER A 65 6410 4655 5436 -1258 -1239 333 O ATOM 542 CB SER A 65 31.903 36.012 -1.123 1.00 40.86 C ANISOU 542 CB SER A 65 6071 4357 5098 -1283 -1203 327 C ATOM 543 OG SER A 65 32.683 36.989 -0.458 1.00 47.62 O ANISOU 543 OG SER A 65 6902 5225 5967 -1286 -1206 325 O ATOM 544 N GLN A 66 30.020 37.583 1.074 1.00 35.68 N ANISOU 544 N GLN A 66 5412 3680 4467 -1288 -1247 339 N ATOM 545 CA GLN A 66 29.698 37.766 2.479 1.00 40.28 C ANISOU 545 CA GLN A 66 5983 4261 5061 -1277 -1262 337 C ATOM 546 C GLN A 66 28.195 37.709 2.742 1.00 44.04 C ANISOU 546 C GLN A 66 6478 4719 5537 -1280 -1277 344 C ATOM 547 O GLN A 66 27.764 37.158 3.749 1.00 41.61 O ANISOU 547 O GLN A 66 6170 4408 5231 -1265 -1286 342 O ATOM 548 CB GLN A 66 30.273 39.090 2.990 1.00 34.68 C ANISOU 548 CB GLN A 66 5251 3560 4365 -1288 -1268 337 C ATOM 549 CG GLN A 66 31.793 39.110 3.030 1.00 35.90 C ANISOU 549 CG GLN A 66 5383 3735 4523 -1282 -1254 329 C ATOM 550 CD GLN A 66 32.351 38.142 4.057 1.00 53.49 C ANISOU 550 CD GLN A 66 7598 5971 6753 -1256 -1253 320 C ATOM 551 OE1 GLN A 66 32.948 37.119 3.712 1.00 58.88 O ANISOU 551 OE1 GLN A 66 8283 6660 7429 -1243 -1241 315 O ATOM 552 NE2 GLN A 66 32.161 38.466 5.329 1.00 49.49 N ANISOU 552 NE2 GLN A 66 7080 5467 6257 -1249 -1267 319 N ATOM 553 N GLU A 67 27.412 38.351 1.879 1.00 32.66 N ANISOU 553 N GLU A 67 5052 3267 4092 -1300 -1281 352 N ATOM 554 CA GLU A 67 25.974 38.507 2.117 1.00 31.91 C ANISOU 554 CA GLU A 67 4972 3154 3998 -1305 -1297 358 C ATOM 555 C GLU A 67 25.030 37.432 1.575 1.00 41.62 C ANISOU 555 C GLU A 67 6227 4371 5215 -1300 -1295 362 C ATOM 556 O GLU A 67 23.939 37.248 2.110 1.00 39.26 O ANISOU 556 O GLU A 67 5939 4061 4918 -1297 -1308 364 O ATOM 557 CB GLU A 67 25.505 39.884 1.624 1.00 28.78 C ANISOU 557 CB GLU A 67 4577 2751 3608 -1328 -1305 366 C ATOM 558 CG GLU A 67 26.281 41.069 2.226 1.00 27.83 C ANISOU 558 CG GLU A 67 4432 2641 3503 -1335 -1309 363 C ATOM 559 CD GLU A 67 26.132 41.183 3.748 1.00 36.69 C ANISOU 559 CD GLU A 67 5538 3765 4636 -1321 -1321 357 C ATOM 560 OE1 GLU A 67 25.136 40.690 4.315 1.00 40.54 O ANISOU 560 OE1 GLU A 67 6036 4243 5123 -1313 -1331 357 O ATOM 561 OE2 GLU A 67 27.022 41.773 4.372 1.00 35.65 O ANISOU 561 OE2 GLU A 67 5385 3646 4516 -1320 -1321 351 O ATOM 562 N THR A 68 25.442 36.725 0.524 1.00 35.33 N ANISOU 562 N THR A 68 5441 3577 4405 -1300 -1280 361 N ATOM 563 CA THR A 68 24.504 35.897 -0.222 1.00 31.18 C ANISOU 563 CA THR A 68 4941 3038 3867 -1301 -1279 365 C ATOM 564 C THR A 68 24.931 34.435 -0.260 1.00 37.69 C ANISOU 564 C THR A 68 5771 3865 4683 -1282 -1267 358 C ATOM 565 O THR A 68 26.085 34.100 0.033 1.00 40.42 O ANISOU 565 O THR A 68 6101 4224 5031 -1269 -1257 350 O ATOM 566 CB THR A 68 24.258 36.395 -1.690 1.00 29.33 C ANISOU 566 CB THR A 68 4721 2799 3622 -1324 -1274 372 C ATOM 567 OG1 THR A 68 25.437 36.233 -2.482 1.00 35.58 O ANISOU 567 OG1 THR A 68 5506 3604 4407 -1326 -1256 368 O ATOM 568 CG2 THR A 68 23.819 37.864 -1.722 1.00 37.06 C ANISOU 568 CG2 THR A 68 5697 3774 4611 -1344 -1286 380 C ATOM 569 N LEU A 69 23.980 33.579 -0.630 1.00 34.28 N ANISOU 569 N LEU A 69 5362 3421 4242 -1279 -1269 360 N ATOM 570 CA LEU A 69 24.209 32.151 -0.786 1.00 36.09 C ANISOU 570 CA LEU A 69 5600 3649 4463 -1262 -1258 354 C ATOM 571 C LEU A 69 24.046 31.793 -2.251 1.00 35.23 C ANISOU 571 C LEU A 69 5510 3536 4340 -1273 -1247 355 C ATOM 572 O LEU A 69 23.434 32.540 -3.015 1.00 37.92 O ANISOU 572 O LEU A 69 5861 3871 4676 -1293 -1251 362 O ATOM 573 CB LEU A 69 23.166 31.362 0.013 1.00 37.69 C ANISOU 573 CB LEU A 69 5815 3839 4667 -1250 -1270 356 C ATOM 574 CG LEU A 69 23.076 31.608 1.510 1.00 45.88 C ANISOU 574 CG LEU A 69 6837 4879 5716 -1239 -1283 356 C ATOM 575 CD1 LEU A 69 21.851 30.899 2.085 1.00 45.31 C ANISOU 575 CD1 LEU A 69 6780 4793 5642 -1232 -1295 359 C ATOM 576 CD2 LEU A 69 24.343 31.133 2.181 1.00 53.82 C ANISOU 576 CD2 LEU A 69 7823 5898 6727 -1220 -1275 348 C ATOM 577 N GLU A 70 24.607 30.659 -2.656 1.00 36.90 N ANISOU 577 N GLU A 70 5726 3751 4544 -1260 -1233 347 N ATOM 578 CA GLU A 70 24.398 30.164 -4.011 1.00 33.97 C ANISOU 578 CA GLU A 70 5374 3376 4157 -1269 -1222 346 C ATOM 579 C GLU A 70 23.175 29.241 -4.026 1.00 35.68 C ANISOU 579 C GLU A 70 5613 3575 4368 -1264 -1229 349 C ATOM 580 O GLU A 70 23.149 28.224 -3.342 1.00 35.47 O ANISOU 580 O GLU A 70 5588 3544 4344 -1245 -1230 344 O ATOM 581 CB GLU A 70 25.632 29.410 -4.506 1.00 41.00 C ANISOU 581 CB GLU A 70 6256 4278 5043 -1258 -1202 335 C ATOM 582 CG GLU A 70 26.924 30.211 -4.446 1.00 43.33 C ANISOU 582 CG GLU A 70 6527 4592 5345 -1262 -1194 331 C ATOM 583 CD GLU A 70 26.848 31.511 -5.234 1.00 45.05 C ANISOU 583 CD GLU A 70 6745 4814 5559 -1288 -1195 339 C ATOM 584 OE1 GLU A 70 26.845 31.452 -6.474 1.00 46.14 O ANISOU 584 OE1 GLU A 70 6894 4953 5682 -1302 -1184 339 O ATOM 585 OE2 GLU A 70 26.782 32.592 -4.607 1.00 46.04 O ANISOU 585 OE2 GLU A 70 6858 4940 5694 -1296 -1206 345 O ATOM 586 N ILE A 71 22.151 29.601 -4.783 1.00 30.01 N ANISOU 586 N ILE A 71 4453 3378 3573 37 -252 -357 N ATOM 587 CA ILE A 71 20.937 28.789 -4.787 1.00 32.54 C ANISOU 587 CA ILE A 71 4739 3699 3926 64 -199 -348 C ATOM 588 C ILE A 71 21.181 27.364 -5.305 1.00 28.38 C ANISOU 588 C ILE A 71 4133 3173 3478 67 -220 -321 C ATOM 589 O ILE A 71 20.454 26.442 -4.959 1.00 30.90 O ANISOU 589 O ILE A 71 4431 3492 3817 76 -193 -297 O ATOM 590 CB ILE A 71 19.764 29.479 -5.527 1.00 34.85 C ANISOU 590 CB ILE A 71 5023 3988 4232 101 -141 -386 C ATOM 591 CG1 ILE A 71 20.044 29.610 -7.023 1.00 35.68 C ANISOU 591 CG1 ILE A 71 5062 4094 4399 114 -157 -410 C ATOM 592 CG2 ILE A 71 19.492 30.848 -4.898 1.00 34.75 C ANISOU 592 CG2 ILE A 71 5094 3968 4144 101 -116 -412 C ATOM 593 CD1 ILE A 71 18.831 30.053 -7.819 1.00 37.67 C ANISOU 593 CD1 ILE A 71 5290 4348 4676 149 -101 -436 C ATOM 594 N HIS A 72 22.217 27.181 -6.116 1.00 26.20 N ANISOU 594 N HIS A 72 3812 2897 3246 59 -268 -324 N ATOM 595 CA HIS A 72 22.625 25.833 -6.507 1.00 38.04 C ANISOU 595 CA HIS A 72 5241 4393 4819 60 -292 -298 C ATOM 596 C HIS A 72 22.834 24.983 -5.255 1.00 34.88 C ANISOU 596 C HIS A 72 4863 3991 4400 40 -308 -246 C ATOM 597 O HIS A 72 22.292 23.879 -5.144 1.00 27.01 O ANISOU 597 O HIS A 72 3829 2986 3446 49 -290 -222 O ATOM 598 CB HIS A 72 23.905 25.868 -7.359 1.00 38.75 C ANISOU 598 CB HIS A 72 5290 4487 4945 50 -347 -307 C ATOM 599 CG HIS A 72 24.528 24.522 -7.581 1.00 45.68 C ANISOU 599 CG HIS A 72 6104 5358 5894 49 -377 -279 C ATOM 600 ND1 HIS A 72 25.388 23.939 -6.673 1.00 45.65 N ANISOU 600 ND1 HIS A 72 6112 5351 5881 26 -419 -231 N ATOM 601 CD2 HIS A 72 24.419 23.644 -8.610 1.00 41.39 C ANISOU 601 CD2 HIS A 72 5484 4809 5434 67 -370 -292 C ATOM 602 CE1 HIS A 72 25.779 22.762 -7.130 1.00 42.18 C ANISOU 602 CE1 HIS A 72 5606 4901 5520 34 -436 -215 C ATOM 603 NE2 HIS A 72 25.205 22.558 -8.302 1.00 43.48 N ANISOU 603 NE2 HIS A 72 5718 5063 5741 58 -406 -254 N ATOM 604 N ASP A 73 23.602 25.518 -4.303 1.00 35.35 N ANISOU 604 N ASP A 73 4981 4057 4392 9 -342 -227 N ATOM 605 CA ASP A 73 23.961 24.792 -3.093 1.00 39.82 C ANISOU 605 CA ASP A 73 5569 4627 4934 -17 -366 -172 C ATOM 606 C ASP A 73 22.768 24.525 -2.189 1.00 35.28 C ANISOU 606 C ASP A 73 5025 4055 4323 -13 -316 -156 C ATOM 607 O ASP A 73 22.693 23.481 -1.543 1.00 31.43 O ANISOU 607 O ASP A 73 4522 3568 3853 -22 -322 -108 O ATOM 608 CB ASP A 73 25.049 25.548 -2.304 1.00 43.04 C ANISOU 608 CB ASP A 73 6036 5048 5268 -56 -414 -158 C ATOM 609 CG ASP A 73 26.352 25.680 -3.084 1.00 52.51 C ANISOU 609 CG ASP A 73 7200 6250 6503 -65 -471 -161 C ATOM 610 OD1 ASP A 73 26.503 24.994 -4.116 1.00 53.53 O ANISOU 610 OD1 ASP A 73 7255 6370 6715 -42 -477 -168 O ATOM 611 OD2 ASP A 73 27.225 26.469 -2.667 1.00 58.47 O ANISOU 611 OD2 ASP A 73 8001 7017 7200 -96 -510 -158 O ATOM 612 N LEU A 74 21.850 25.479 -2.107 1.00 30.67 N ANISOU 612 N LEU A 74 4487 3476 3691 1 -266 -194 N ATOM 613 CA LEU A 74 20.644 25.265 -1.322 1.00 32.80 C ANISOU 613 CA LEU A 74 4781 3753 3928 9 -213 -182 C ATOM 614 C LEU A 74 19.931 24.008 -1.825 1.00 34.80 C ANISOU 614 C LEU A 74 4964 3998 4261 30 -190 -163 C ATOM 615 O LEU A 74 19.397 23.229 -1.045 1.00 24.19 O ANISOU 615 O LEU A 74 3620 2660 2912 23 -175 -124 O ATOM 616 CB LEU A 74 19.704 26.469 -1.440 1.00 26.77 C ANISOU 616 CB LEU A 74 4062 2991 3119 31 -157 -232 C ATOM 617 CG LEU A 74 19.974 27.720 -0.608 1.00 43.93 C ANISOU 617 CG LEU A 74 6324 5171 5197 10 -157 -252 C ATOM 618 CD1 LEU A 74 21.458 28.025 -0.506 1.00 59.77 C ANISOU 618 CD1 LEU A 74 8349 7177 7184 -26 -226 -244 C ATOM 619 CD2 LEU A 74 19.216 28.892 -1.191 1.00 30.92 C ANISOU 619 CD2 LEU A 74 4697 3513 3536 41 -109 -307 C ATOM 620 N PHE A 75 19.910 23.808 -3.135 1.00 27.25 N ANISOU 620 N PHE A 75 3945 3029 3379 54 -189 -190 N ATOM 621 CA PHE A 75 19.167 22.666 -3.655 1.00 26.80 C ANISOU 621 CA PHE A 75 3823 2964 3396 72 -165 -178 C ATOM 622 C PHE A 75 19.908 21.359 -3.450 1.00 25.97 C ANISOU 622 C PHE A 75 3678 2845 3346 56 -208 -131 C ATOM 623 O PHE A 75 19.334 20.369 -3.013 1.00 22.40 O ANISOU 623 O PHE A 75 3206 2387 2918 54 -193 -95 O ATOM 624 CB PHE A 75 18.859 22.813 -5.149 1.00 24.93 C ANISOU 624 CB PHE A 75 3530 2722 3220 98 -147 -224 C ATOM 625 CG PHE A 75 18.118 21.627 -5.715 1.00 21.93 C ANISOU 625 CG PHE A 75 3084 2332 2915 112 -124 -215 C ATOM 626 CD1 PHE A 75 16.786 21.408 -5.386 1.00 21.43 C ANISOU 626 CD1 PHE A 75 3025 2278 2841 123 -70 -206 C ATOM 627 CD2 PHE A 75 18.762 20.715 -6.531 1.00 27.82 C ANISOU 627 CD2 PHE A 75 3765 3062 3742 111 -155 -215 C ATOM 628 CE1 PHE A 75 16.096 20.309 -5.890 1.00 23.02 C ANISOU 628 CE1 PHE A 75 3166 2471 3109 131 -49 -196 C ATOM 629 CE2 PHE A 75 18.076 19.612 -7.042 1.00 31.70 C ANISOU 629 CE2 PHE A 75 4200 3542 4303 120 -133 -210 C ATOM 630 CZ PHE A 75 16.745 19.416 -6.720 1.00 27.39 C ANISOU 630 CZ PHE A 75 3659 3005 3744 128 -81 -200 C ATOM 631 N PHE A 76 21.185 21.342 -3.795 1.00 22.80 N ANISOU 631 N PHE A 76 3258 2436 2968 45 -263 -130 N ATOM 632 CA PHE A 76 21.923 20.088 -3.720 1.00 26.23 C ANISOU 632 CA PHE A 76 3646 2853 3466 35 -303 -86 C ATOM 633 C PHE A 76 22.140 19.651 -2.285 1.00 26.12 C ANISOU 633 C PHE A 76 3670 2846 3410 7 -323 -23 C ATOM 634 O PHE A 76 22.216 18.454 -2.001 1.00 28.55 O ANISOU 634 O PHE A 76 3942 3137 3770 2 -337 24 O ATOM 635 CB PHE A 76 23.216 20.153 -4.524 1.00 26.72 C ANISOU 635 CB PHE A 76 3673 2910 3571 34 -353 -100 C ATOM 636 CG PHE A 76 23.001 19.938 -5.988 1.00 31.60 C ANISOU 636 CG PHE A 76 4227 3518 4263 60 -336 -148 C ATOM 637 CD1 PHE A 76 22.845 18.659 -6.494 1.00 39.21 C ANISOU 637 CD1 PHE A 76 5126 4458 5315 72 -332 -138 C ATOM 638 CD2 PHE A 76 22.896 21.011 -6.854 1.00 38.33 C ANISOU 638 CD2 PHE A 76 5084 4385 5096 71 -323 -201 C ATOM 639 CE1 PHE A 76 22.616 18.454 -7.851 1.00 41.84 C ANISOU 639 CE1 PHE A 76 5400 4786 5712 92 -315 -186 C ATOM 640 CE2 PHE A 76 22.673 20.809 -8.209 1.00 43.67 C ANISOU 640 CE2 PHE A 76 5699 5059 5836 91 -307 -243 C ATOM 641 CZ PHE A 76 22.534 19.535 -8.704 1.00 41.88 C ANISOU 641 CZ PHE A 76 5409 4812 5692 100 -303 -237 C ATOM 642 N ASN A 77 22.212 20.616 -1.370 1.00 25.83 N ANISOU 642 N ASN A 77 3705 2832 3277 -14 -324 -21 N ATOM 643 CA ASN A 77 22.196 20.273 0.039 1.00 33.61 C ANISOU 643 CA ASN A 77 4730 3832 4209 -44 -334 36 C ATOM 644 C ASN A 77 20.884 19.576 0.459 1.00 35.59 C ANISOU 644 C ASN A 77 4973 4084 4466 -35 -284 57 C ATOM 645 O ASN A 77 20.922 18.627 1.229 1.00 30.00 O ANISOU 645 O ASN A 77 4254 3374 3768 -53 -299 117 O ATOM 646 CB ASN A 77 22.543 21.489 0.923 1.00 36.73 C ANISOU 646 CB ASN A 77 5208 4255 4495 -71 -342 28 C ATOM 647 CG ASN A 77 24.020 21.898 0.794 1.00 42.95 C ANISOU 647 CG ASN A 77 6000 5045 5274 -93 -406 32 C ATOM 648 OD1 ASN A 77 24.865 21.094 0.392 1.00 40.59 O ANISOU 648 OD1 ASN A 77 5646 4733 5045 -93 -449 61 O ATOM 649 ND2 ASN A 77 24.328 23.149 1.130 1.00 40.99 N ANISOU 649 ND2 ASN A 77 5817 4813 4943 -112 -411 4 N ATOM 650 N LEU A 78 19.735 20.005 -0.075 1.00 29.87 N ANISOU 650 N LEU A 78 4249 3362 3740 -7 -226 12 N ATOM 651 CA LEU A 78 18.472 19.286 0.187 1.00 23.53 C ANISOU 651 CA LEU A 78 3429 2561 2951 3 -178 32 C ATOM 652 C LEU A 78 18.491 17.850 -0.331 1.00 21.94 C ANISOU 652 C LEU A 78 3154 2330 2852 8 -193 63 C ATOM 653 O LEU A 78 17.970 16.932 0.319 1.00 22.54 O ANISOU 653 O LEU A 78 3219 2406 2941 -2 -184 112 O ATOM 654 CB LEU A 78 17.272 20.030 -0.424 1.00 20.91 C ANISOU 654 CB LEU A 78 3102 2237 2605 33 -115 -22 C ATOM 655 CG LEU A 78 16.866 21.323 0.308 1.00 27.16 C ANISOU 655 CG LEU A 78 3970 3054 3293 31 -82 -47 C ATOM 656 CD1 LEU A 78 15.806 22.103 -0.518 1.00 28.66 C ANISOU 656 CD1 LEU A 78 4156 3248 3486 68 -23 -102 C ATOM 657 CD2 LEU A 78 16.332 20.991 1.694 1.00 33.72 C ANISOU 657 CD2 LEU A 78 4839 3910 4062 9 -64 -1 C ATOM 658 N LEU A 79 19.086 17.669 -1.507 1.00 26.21 N ANISOU 658 N LEU A 79 3645 2848 3466 24 -214 32 N ATOM 659 CA LEU A 79 19.105 16.375 -2.184 1.00 25.83 C ANISOU 659 CA LEU A 79 3525 2767 3522 34 -224 47 C ATOM 660 C LEU A 79 19.899 15.339 -1.418 1.00 28.08 C ANISOU 660 C LEU A 79 3798 3035 3838 12 -271 115 C ATOM 661 O LEU A 79 19.664 14.134 -1.559 1.00 25.73 O ANISOU 661 O LEU A 79 3453 2709 3616 14 -272 144 O ATOM 662 CB LEU A 79 19.716 16.519 -3.581 1.00 33.28 C ANISOU 662 CB LEU A 79 4423 3694 4528 53 -238 -5 C ATOM 663 CG LEU A 79 18.907 16.250 -4.850 1.00 45.08 C ANISOU 663 CG LEU A 79 5864 5178 6085 77 -200 -53 C ATOM 664 CD1 LEU A 79 19.862 15.781 -5.936 1.00 42.86 C ANISOU 664 CD1 LEU A 79 5526 4875 5886 85 -234 -77 C ATOM 665 CD2 LEU A 79 17.784 15.222 -4.665 1.00 30.85 C ANISOU 665 CD2 LEU A 79 4036 3364 4319 77 -165 -26 C ATOM 666 N LYS A 80 20.854 15.798 -0.618 1.00 26.90 N ANISOU 666 N LYS A 80 3687 2901 3632 -11 -312 143 N ATOM 667 CA LYS A 80 21.634 14.870 0.192 1.00 32.38 C ANISOU 667 CA LYS A 80 4369 3583 4350 -35 -360 217 C ATOM 668 C LYS A 80 20.728 14.185 1.219 1.00 34.17 C ANISOU 668 C LYS A 80 4609 3819 4557 -52 -338 273 C ATOM 669 O LYS A 80 21.018 13.082 1.681 1.00 33.74 O ANISOU 669 O LYS A 80 4524 3744 4552 -65 -367 337 O ATOM 670 CB LYS A 80 22.782 15.597 0.909 1.00 34.82 C ANISOU 670 CB LYS A 80 4722 3917 4590 -62 -408 238 C ATOM 671 CG LYS A 80 23.850 16.192 -0.012 1.00 34.78 C ANISOU 671 CG LYS A 80 4701 3907 4606 -51 -440 195 C ATOM 672 CD LYS A 80 24.902 16.968 0.805 1.00 47.30 C ANISOU 672 CD LYS A 80 6337 5522 6112 -85 -486 220 C ATOM 673 CE LYS A 80 25.956 17.632 -0.084 1.00 54.26 C ANISOU 673 CE LYS A 80 7205 6403 7009 -77 -519 179 C ATOM 674 NZ LYS A 80 26.909 18.492 0.695 1.00 56.97 N ANISOU 674 NZ LYS A 80 7602 6778 7267 -114 -562 199 N ATOM 675 N ASP A 81 19.699 14.906 1.646 1.00 25.67 N ANISOU 675 N ASP A 81 3578 2773 3402 -53 -290 252 N ATOM 676 CA ASP A 81 18.776 14.466 2.706 1.00 27.71 C ANISOU 676 CA ASP A 81 3857 3052 3619 -71 -264 301 C ATOM 677 C ASP A 81 17.333 14.064 2.362 1.00 30.96 C ANISOU 677 C ASP A 81 4246 3460 4057 -53 -205 287 C ATOM 678 O ASP A 81 16.579 13.706 3.258 1.00 28.30 O ANISOU 678 O ASP A 81 3924 3144 3684 -69 -184 331 O ATOM 679 CB ASP A 81 18.703 15.565 3.771 1.00 41.95 C ANISOU 679 CB ASP A 81 5738 4902 5297 -94 -254 300 C ATOM 680 CG ASP A 81 19.901 15.565 4.670 1.00 49.08 C ANISOU 680 CG ASP A 81 6666 5820 6162 -131 -313 351 C ATOM 681 OD1 ASP A 81 20.296 14.464 5.114 1.00 57.91 O ANISOU 681 OD1 ASP A 81 7750 6924 7327 -149 -349 422 O ATOM 682 OD2 ASP A 81 20.450 16.655 4.921 1.00 49.48 O ANISOU 682 OD2 ASP A 81 6768 5893 6138 -143 -325 323 O ATOM 683 N ASN A 82 16.925 14.191 1.101 1.00 27.41 N ANISOU 683 N ASN A 82 3761 2992 3661 -21 -178 228 N ATOM 684 CA ASN A 82 15.501 14.138 0.726 1.00 26.25 C ANISOU 684 CA ASN A 82 3601 2854 3520 -4 -117 205 C ATOM 685 C ASN A 82 15.388 13.607 -0.692 1.00 22.35 C ANISOU 685 C ASN A 82 3042 2324 3124 20 -111 166 C ATOM 686 O ASN A 82 16.319 13.765 -1.473 1.00 25.32 O ANISOU 686 O ASN A 82 3398 2681 3541 29 -142 134 O ATOM 687 CB ASN A 82 14.881 15.559 0.678 1.00 27.89 C ANISOU 687 CB ASN A 82 3856 3097 3643 12 -72 150 C ATOM 688 CG ASN A 82 14.860 16.281 2.023 1.00 30.41 C ANISOU 688 CG ASN A 82 4248 3455 3853 -9 -66 172 C ATOM 689 OD1 ASN A 82 13.921 16.138 2.798 1.00 27.46 O ANISOU 689 OD1 ASN A 82 3891 3107 3435 -17 -30 199 O ATOM 690 ND2 ASN A 82 15.849 17.137 2.254 1.00 24.61 N ANISOU 690 ND2 ASN A 82 3554 2726 3069 -19 -98 155 N ATOM 691 N SER A 83 14.240 13.033 -1.053 1.00 20.04 N ANISOU 691 N SER A 83 2717 2029 2868 27 -70 164 N ATOM 692 CA SER A 83 13.995 12.644 -2.435 1.00 23.15 C ANISOU 692 CA SER A 83 3054 2397 3345 46 -58 119 C ATOM 693 C SER A 83 13.987 13.893 -3.328 1.00 21.56 C ANISOU 693 C SER A 83 2862 2215 3113 69 -38 48 C ATOM 694 O SER A 83 13.901 15.024 -2.836 1.00 20.47 O ANISOU 694 O SER A 83 2777 2108 2892 73 -23 35 O ATOM 695 CB SER A 83 12.637 11.944 -2.571 1.00 23.23 C ANISOU 695 CB SER A 83 3034 2410 3382 46 -13 132 C ATOM 696 OG SER A 83 11.580 12.849 -2.301 1.00 23.93 O ANISOU 696 OG SER A 83 3155 2543 3394 55 39 117 O ATOM 697 N ILE A 84 14.128 13.687 -4.637 1.00 18.65 N ANISOU 697 N ILE A 84 2443 1827 2814 83 -39 3 N ATOM 698 CA ILE A 84 14.048 14.798 -5.590 1.00 18.13 C ANISOU 698 CA ILE A 84 2378 1782 2729 103 -20 -61 C ATOM 699 C ILE A 84 12.737 15.556 -5.443 1.00 18.54 C ANISOU 699 C ILE A 84 2453 1870 2721 114 38 -72 C ATOM 700 O ILE A 84 12.731 16.774 -5.433 1.00 17.91 O ANISOU 700 O ILE A 84 2411 1814 2582 126 52 -101 O ATOM 701 CB ILE A 84 14.123 14.289 -7.027 1.00 21.50 C ANISOU 701 CB ILE A 84 2739 2190 3241 111 -21 -104 C ATOM 702 CG1 ILE A 84 15.478 13.638 -7.248 1.00 26.93 C ANISOU 702 CG1 ILE A 84 3402 2842 3988 105 -75 -99 C ATOM 703 CG2 ILE A 84 13.897 15.442 -8.046 1.00 27.55 C ANISOU 703 CG2 ILE A 84 3501 2984 3984 129 2 -164 C ATOM 704 CD1 ILE A 84 15.535 12.845 -8.504 1.00 35.22 C ANISOU 704 CD1 ILE A 84 4385 3867 5129 109 -75 -135 C ATOM 705 N GLU A 85 11.628 14.832 -5.315 1.00 18.29 N ANISOU 705 N GLU A 85 2399 1843 2708 110 73 -48 N ATOM 706 CA GLU A 85 10.334 15.496 -5.168 1.00 20.14 C ANISOU 706 CA GLU A 85 2649 2114 2889 123 130 -55 C ATOM 707 C GLU A 85 10.240 16.304 -3.881 1.00 23.54 C ANISOU 707 C GLU A 85 3149 2570 3224 122 143 -33 C ATOM 708 O GLU A 85 9.756 17.431 -3.878 1.00 21.44 O ANISOU 708 O GLU A 85 2914 2331 2902 141 177 -61 O ATOM 709 CB GLU A 85 9.185 14.485 -5.211 1.00 21.72 C ANISOU 709 CB GLU A 85 2810 2316 3126 115 162 -27 C ATOM 710 CG GLU A 85 9.091 13.683 -6.503 1.00 24.44 C ANISOU 710 CG GLU A 85 3087 2639 3562 113 158 -53 C ATOM 711 CD GLU A 85 9.836 12.365 -6.395 1.00 26.08 C ANISOU 711 CD GLU A 85 3268 2800 3841 92 114 -24 C ATOM 712 OE1 GLU A 85 9.392 11.355 -6.995 1.00 20.83 O ANISOU 712 OE1 GLU A 85 2554 2115 3246 82 121 -24 O ATOM 713 OE2 GLU A 85 10.863 12.342 -5.684 1.00 24.99 O ANISOU 713 OE2 GLU A 85 3160 2645 3691 86 74 -1 O ATOM 714 N GLU A 86 10.678 15.714 -2.777 1.00 22.12 N ANISOU 714 N GLU A 86 2993 2383 3027 100 115 18 N ATOM 715 CA GLU A 86 10.633 16.412 -1.506 1.00 21.61 C ANISOU 715 CA GLU A 86 2996 2347 2869 93 125 39 C ATOM 716 C GLU A 86 11.592 17.584 -1.513 1.00 28.44 C ANISOU 716 C GLU A 86 3906 3213 3687 98 102 2 C ATOM 717 O GLU A 86 11.279 18.650 -0.969 1.00 21.48 O ANISOU 717 O GLU A 86 3078 2357 2727 106 131 -15 O ATOM 718 CB GLU A 86 10.950 15.464 -0.339 1.00 25.51 C ANISOU 718 CB GLU A 86 3501 2836 3356 61 96 107 C ATOM 719 CG GLU A 86 10.878 16.170 1.012 1.00 27.99 C ANISOU 719 CG GLU A 86 3884 3187 3565 48 107 128 C ATOM 720 CD GLU A 86 9.439 16.489 1.418 1.00 53.39 C ANISOU 720 CD GLU A 86 7114 6441 6730 60 174 129 C ATOM 721 OE1 GLU A 86 9.252 17.255 2.387 1.00 62.55 O ANISOU 721 OE1 GLU A 86 8332 7634 7799 56 196 130 O ATOM 722 OE2 GLU A 86 8.499 15.969 0.770 1.00 54.12 O ANISOU 722 OE2 GLU A 86 7158 6533 6872 72 206 129 O ATOM 723 N SER A 87 12.760 17.399 -2.130 1.00 19.01 N ANISOU 723 N SER A 87 2690 1990 2542 94 51 -11 N ATOM 724 CA SER A 87 13.711 18.507 -2.241 1.00 18.80 C ANISOU 724 CA SER A 87 2702 1965 2476 96 25 -46 C ATOM 725 C SER A 87 13.075 19.665 -3.010 1.00 21.22 C ANISOU 725 C SER A 87 3016 2287 2761 124 68 -103 C ATOM 726 O SER A 87 13.190 20.816 -2.622 1.00 21.55 O ANISOU 726 O SER A 87 3113 2342 2734 129 77 -125 O ATOM 727 CB SER A 87 15.003 18.067 -2.948 1.00 18.55 C ANISOU 727 CB SER A 87 2634 1904 2509 90 -33 -52 C ATOM 728 OG SER A 87 15.702 17.094 -2.170 1.00 24.97 O ANISOU 728 OG SER A 87 3444 2703 3341 65 -75 4 O ATOM 729 N LEU A 88 12.393 19.356 -4.104 1.00 18.36 N ANISOU 729 N LEU A 88 2597 1921 2458 142 93 -125 N ATOM 730 CA LEU A 88 11.795 20.425 -4.885 1.00 17.79 C ANISOU 730 CA LEU A 88 2525 1864 2371 168 131 -172 C ATOM 731 C LEU A 88 10.686 21.121 -4.102 1.00 21.60 C ANISOU 731 C LEU A 88 3051 2373 2783 182 188 -168 C ATOM 732 O LEU A 88 10.516 22.337 -4.196 1.00 22.43 O ANISOU 732 O LEU A 88 3190 2488 2844 200 211 -201 O ATOM 733 CB LEU A 88 11.270 19.870 -6.198 1.00 17.39 C ANISOU 733 CB LEU A 88 2400 1810 2397 179 145 -191 C ATOM 734 CG LEU A 88 12.391 19.577 -7.199 1.00 17.59 C ANISOU 734 CG LEU A 88 2385 1814 2484 172 96 -216 C ATOM 735 CD1 LEU A 88 11.874 18.690 -8.309 1.00 17.14 C ANISOU 735 CD1 LEU A 88 2255 1754 2505 173 109 -228 C ATOM 736 CD2 LEU A 88 12.996 20.867 -7.757 1.00 22.87 C ANISOU 736 CD2 LEU A 88 3075 2490 3125 183 84 -259 C ATOM 737 N ASP A 89 9.954 20.350 -3.307 1.00 23.48 N ANISOU 737 N ASP A 89 3288 2623 3010 173 210 -126 N ATOM 738 CA ASP A 89 8.898 20.919 -2.469 1.00 24.26 C ANISOU 738 CA ASP A 89 3427 2752 3041 185 266 -118 C ATOM 739 C ASP A 89 9.453 21.916 -1.429 1.00 23.58 C ANISOU 739 C ASP A 89 3420 2671 2866 178 260 -127 C ATOM 740 O ASP A 89 8.991 23.069 -1.334 1.00 23.88 O ANISOU 740 O ASP A 89 3498 2722 2855 201 300 -159 O ATOM 741 CB ASP A 89 8.075 19.803 -1.832 1.00 31.30 C ANISOU 741 CB ASP A 89 4296 3657 3940 171 286 -67 C ATOM 742 CG ASP A 89 6.775 20.312 -1.208 1.00 42.81 C ANISOU 742 CG ASP A 89 5778 5151 5338 189 354 -61 C ATOM 743 OD1 ASP A 89 6.255 21.339 -1.669 1.00 36.81 O ANISOU 743 OD1 ASP A 89 5025 4401 4558 219 392 -100 O ATOM 744 OD2 ASP A 89 6.270 19.677 -0.266 1.00 47.07 O ANISOU 744 OD2 ASP A 89 6324 5709 5850 173 368 -17 O ATOM 745 N LYS A 90 10.491 21.514 -0.713 1.00 23.32 N ANISOU 745 N LYS A 90 3413 2629 2818 147 209 -100 N ATOM 746 CA LYS A 90 11.116 22.374 0.302 1.00 22.74 C ANISOU 746 CA LYS A 90 3416 2563 2660 132 196 -106 C ATOM 747 C LYS A 90 11.828 23.560 -0.329 1.00 27.28 C ANISOU 747 C LYS A 90 4017 3124 3225 144 180 -158 C ATOM 748 O LYS A 90 11.899 24.644 0.252 1.00 23.67 O ANISOU 748 O LYS A 90 3625 2674 2696 145 195 -183 O ATOM 749 CB LYS A 90 12.142 21.578 1.116 1.00 26.13 C ANISOU 749 CB LYS A 90 3857 2988 3084 92 138 -58 C ATOM 750 CG LYS A 90 11.512 20.571 2.103 1.00 24.29 C ANISOU 750 CG LYS A 90 3618 2776 2837 73 152 1 C ATOM 751 CD LYS A 90 12.572 19.819 2.920 1.00 25.91 C ANISOU 751 CD LYS A 90 3832 2977 3037 32 91 55 C ATOM 752 CE LYS A 90 11.887 18.874 3.921 1.00 31.89 C ANISOU 752 CE LYS A 90 4583 3757 3776 11 106 117 C ATOM 753 NZ LYS A 90 12.847 17.955 4.563 1.00 37.01 N ANISOU 753 NZ LYS A 90 5225 4398 4441 -27 45 178 N ATOM 754 N TYR A 91 12.371 23.340 -1.520 1.00 23.25 N ANISOU 754 N TYR A 91 3455 2591 2786 150 149 -175 N ATOM 755 CA TYR A 91 13.249 24.313 -2.154 1.00 19.67 C ANISOU 755 CA TYR A 91 3019 2125 2331 154 120 -216 C ATOM 756 C TYR A 91 12.554 25.629 -2.437 1.00 22.17 C ANISOU 756 C TYR A 91 3365 2446 2611 184 168 -261 C ATOM 757 O TYR A 91 13.142 26.699 -2.226 1.00 21.98 O ANISOU 757 O TYR A 91 3395 2415 2540 180 155 -288 O ATOM 758 CB TYR A 91 13.791 23.738 -3.450 1.00 20.87 C ANISOU 758 CB TYR A 91 3101 2260 2571 157 85 -226 C ATOM 759 CG TYR A 91 14.875 24.558 -4.140 1.00 23.07 C ANISOU 759 CG TYR A 91 3387 2526 2853 155 44 -260 C ATOM 760 CD1 TYR A 91 15.938 25.106 -3.423 1.00 22.39 C ANISOU 760 CD1 TYR A 91 3357 2437 2714 131 3 -257 C ATOM 761 CD2 TYR A 91 14.851 24.739 -5.517 1.00 21.06 C ANISOU 761 CD2 TYR A 91 3079 2268 2656 173 44 -293 C ATOM 762 CE1 TYR A 91 16.956 25.818 -4.083 1.00 27.91 C ANISOU 762 CE1 TYR A 91 4059 3128 3419 126 -37 -285 C ATOM 763 CE2 TYR A 91 15.857 25.444 -6.184 1.00 23.35 C ANISOU 763 CE2 TYR A 91 3370 2550 2951 168 5 -321 C ATOM 764 CZ TYR A 91 16.907 25.980 -5.452 1.00 27.57 C ANISOU 764 CZ TYR A 91 3961 3080 3433 145 -36 -316 C ATOM 765 OH TYR A 91 17.906 26.667 -6.114 1.00 26.15 O ANISOU 765 OH TYR A 91 3781 2895 3259 138 -77 -341 O ATOM 766 N LYS A 92 11.323 25.576 -2.944 1.00 22.73 N ANISOU 766 N LYS A 92 3400 2528 2708 213 222 -267 N ATOM 767 CA LYS A 92 10.649 26.838 -3.256 1.00 23.40 C ANISOU 767 CA LYS A 92 3509 2616 2767 245 269 -305 C ATOM 768 C LYS A 92 10.546 27.707 -2.005 1.00 22.33 C ANISOU 768 C LYS A 92 3458 2485 2540 243 294 -314 C ATOM 769 O LYS A 92 10.732 28.915 -2.085 1.00 23.33 O ANISOU 769 O LYS A 92 3629 2599 2636 255 302 -352 O ATOM 770 CB LYS A 92 9.253 26.614 -3.866 1.00 22.35 C ANISOU 770 CB LYS A 92 3323 2500 2670 276 327 -303 C ATOM 771 CG LYS A 92 8.328 25.777 -2.978 1.00 39.87 C ANISOU 771 CG LYS A 92 5538 4741 4869 272 363 -264 C ATOM 772 CD LYS A 92 7.025 25.406 -3.673 1.00 30.56 C ANISOU 772 CD LYS A 92 4297 3581 3733 297 413 -255 C ATOM 773 CE LYS A 92 6.499 24.073 -3.169 1.00 34.32 C ANISOU 773 CE LYS A 92 4742 4072 4225 278 419 -208 C ATOM 774 NZ LYS A 92 5.091 23.820 -3.560 1.00 33.14 N ANISOU 774 NZ LYS A 92 4545 3948 4097 300 476 -195 N ATOM 775 N TYR A 93 10.240 27.108 -0.850 1.00 25.74 N ANISOU 775 N TYR A 93 3914 2935 2930 226 307 -281 N ATOM 776 CA TYR A 93 10.090 27.897 0.379 1.00 22.56 C ANISOU 776 CA TYR A 93 3593 2543 2436 221 335 -292 C ATOM 777 C TYR A 93 11.428 28.444 0.847 1.00 29.25 C ANISOU 777 C TYR A 93 4500 3376 3239 188 281 -306 C ATOM 778 O TYR A 93 11.513 29.572 1.305 1.00 28.44 O ANISOU 778 O TYR A 93 4463 3267 3076 191 298 -341 O ATOM 779 CB TYR A 93 9.378 27.107 1.502 1.00 27.76 C ANISOU 779 CB TYR A 93 4260 3233 3056 208 365 -251 C ATOM 780 CG TYR A 93 8.064 26.559 1.002 1.00 29.37 C ANISOU 780 CG TYR A 93 4401 3452 3304 238 416 -236 C ATOM 781 CD1 TYR A 93 7.040 27.416 0.601 1.00 28.55 C ANISOU 781 CD1 TYR A 93 4297 3354 3198 281 479 -267 C ATOM 782 CD2 TYR A 93 7.857 25.187 0.883 1.00 26.42 C ANISOU 782 CD2 TYR A 93 3969 3088 2981 223 401 -189 C ATOM 783 CE1 TYR A 93 5.843 26.921 0.098 1.00 30.53 C ANISOU 783 CE1 TYR A 93 4487 3624 3490 306 525 -249 C ATOM 784 CE2 TYR A 93 6.673 24.691 0.376 1.00 28.93 C ANISOU 784 CE2 TYR A 93 4230 3422 3340 245 445 -174 C ATOM 785 CZ TYR A 93 5.667 25.565 -0.014 1.00 35.39 C ANISOU 785 CZ TYR A 93 5046 4250 4151 286 507 -204 C ATOM 786 OH TYR A 93 4.483 25.065 -0.518 1.00 35.18 O ANISOU 786 OH TYR A 93 4960 4244 4164 306 549 -185 O ATOM 787 N LEU A 94 12.474 27.633 0.728 1.00 26.72 N ANISOU 787 N LEU A 94 4153 3049 2951 156 215 -277 N ATOM 788 CA LEU A 94 13.842 28.062 1.047 1.00 25.45 C ANISOU 788 CA LEU A 94 4037 2877 2757 122 155 -283 C ATOM 789 C LEU A 94 14.322 29.228 0.153 1.00 28.84 C ANISOU 789 C LEU A 94 4479 3282 3197 137 143 -332 C ATOM 790 O LEU A 94 14.950 30.174 0.638 1.00 26.70 O ANISOU 790 O LEU A 94 4275 3004 2867 119 128 -356 O ATOM 791 CB LEU A 94 14.777 26.865 0.897 1.00 27.69 C ANISOU 791 CB LEU A 94 4272 3157 3091 93 91 -238 C ATOM 792 CG LEU A 94 16.216 26.890 1.398 1.00 43.01 C ANISOU 792 CG LEU A 94 6244 5095 5002 51 22 -222 C ATOM 793 CD1 LEU A 94 16.296 27.429 2.815 1.00 43.34 C ANISOU 793 CD1 LEU A 94 6369 5157 4941 21 30 -217 C ATOM 794 CD2 LEU A 94 16.790 25.467 1.327 1.00 37.45 C ANISOU 794 CD2 LEU A 94 5481 4390 4359 32 -26 -168 C ATOM 795 N LEU A 95 14.054 29.146 -1.152 1.00 24.19 N ANISOU 795 N LEU A 95 3826 2683 2683 165 148 -346 N ATOM 796 CA LEU A 95 14.330 30.259 -2.059 1.00 24.74 C ANISOU 796 CA LEU A 95 3901 2733 2766 182 144 -389 C ATOM 797 C LEU A 95 13.655 31.558 -1.591 1.00 27.81 C ANISOU 797 C LEU A 95 4358 3115 3096 203 197 -426 C ATOM 798 O LEU A 95 14.298 32.613 -1.519 1.00 30.97 O ANISOU 798 O LEU A 95 4810 3496 3459 193 179 -456 O ATOM 799 CB LEU A 95 13.856 29.931 -3.479 1.00 22.74 C ANISOU 799 CB LEU A 95 3565 2478 2597 210 154 -395 C ATOM 800 CG LEU A 95 14.702 28.940 -4.256 1.00 23.76 C ANISOU 800 CG LEU A 95 3628 2606 2793 193 98 -376 C ATOM 801 CD1 LEU A 95 14.010 28.626 -5.600 1.00 22.54 C ANISOU 801 CD1 LEU A 95 3394 2456 2713 220 121 -386 C ATOM 802 CD2 LEU A 95 16.102 29.504 -4.451 1.00 27.68 C ANISOU 802 CD2 LEU A 95 4148 3091 3279 168 37 -390 C ATOM 803 N LEU A 96 12.364 31.490 -1.276 1.00 27.52 N ANISOU 803 N LEU A 96 4317 3091 3048 232 264 -424 N ATOM 804 CA LEU A 96 11.652 32.701 -0.851 1.00 30.44 C ANISOU 804 CA LEU A 96 4746 3452 3367 258 322 -460 C ATOM 805 C LEU A 96 12.218 33.267 0.448 1.00 37.40 C ANISOU 805 C LEU A 96 5721 4332 4158 227 313 -474 C ATOM 806 O LEU A 96 12.380 34.479 0.582 1.00 33.17 O ANISOU 806 O LEU A 96 5245 3772 3585 232 325 -515 O ATOM 807 CB LEU A 96 10.158 32.446 -0.682 1.00 29.69 C ANISOU 807 CB LEU A 96 4628 3378 3276 295 397 -451 C ATOM 808 CG LEU A 96 9.334 32.237 -1.955 1.00 31.64 C ANISOU 808 CG LEU A 96 4793 3628 3602 332 423 -447 C ATOM 809 CD1 LEU A 96 7.957 31.803 -1.562 1.00 31.72 C ANISOU 809 CD1 LEU A 96 4782 3666 3606 358 490 -427 C ATOM 810 CD2 LEU A 96 9.294 33.513 -2.813 1.00 31.01 C ANISOU 810 CD2 LEU A 96 4720 3523 3541 361 435 -485 C ATOM 811 N GLU A 97 12.498 32.385 1.405 1.00 32.79 N ANISOU 811 N GLU A 97 5148 3772 3539 192 293 -438 N ATOM 812 CA GLU A 97 13.078 32.777 2.685 1.00 37.10 C ANISOU 812 CA GLU A 97 5777 4324 3995 153 280 -445 C ATOM 813 C GLU A 97 14.393 33.536 2.506 1.00 36.15 C ANISOU 813 C GLU A 97 5698 4180 3859 122 220 -467 C ATOM 814 O GLU A 97 14.683 34.476 3.249 1.00 38.53 O ANISOU 814 O GLU A 97 6079 4473 4086 104 225 -499 O ATOM 815 CB GLU A 97 13.286 31.537 3.567 1.00 37.66 C ANISOU 815 CB GLU A 97 5837 4429 4045 116 255 -390 C ATOM 816 CG GLU A 97 14.373 31.672 4.616 1.00 58.68 C ANISOU 816 CG GLU A 97 8563 7100 6632 60 207 -381 C ATOM 817 CD GLU A 97 14.635 30.361 5.350 1.00 73.33 C ANISOU 817 CD GLU A 97 10393 8987 8481 23 175 -317 C ATOM 818 OE1 GLU A 97 15.639 30.280 6.091 1.00 75.64 O ANISOU 818 OE1 GLU A 97 10722 9292 8725 -26 123 -297 O ATOM 819 OE2 GLU A 97 13.838 29.410 5.181 1.00 75.62 O ANISOU 819 OE2 GLU A 97 10626 9291 8816 43 200 -284 O ATOM 820 N ASN A 98 15.200 33.115 1.541 1.00 30.46 N ANISOU 820 N ASN A 98 4921 3449 3202 115 162 -452 N ATOM 821 CA ASN A 98 16.476 33.781 1.275 1.00 33.11 C ANISOU 821 CA ASN A 98 5285 3766 3528 85 102 -468 C ATOM 822 C ASN A 98 16.422 35.011 0.364 1.00 41.82 C ANISOU 822 C ASN A 98 6399 4837 4652 112 114 -515 C ATOM 823 O ASN A 98 17.083 36.023 0.620 1.00 38.08 O ANISOU 823 O ASN A 98 5990 4345 4133 91 93 -545 O ATOM 824 CB ASN A 98 17.489 32.781 0.744 1.00 35.32 C ANISOU 824 CB ASN A 98 5504 4054 3862 61 31 -428 C ATOM 825 CG ASN A 98 18.063 31.913 1.834 1.00 47.96 C ANISOU 825 CG ASN A 98 7119 5679 5423 17 -4 -383 C ATOM 826 OD1 ASN A 98 19.042 32.288 2.482 1.00 48.79 O ANISOU 826 OD1 ASN A 98 7277 5789 5473 -26 -48 -380 O ATOM 827 ND2 ASN A 98 17.457 30.744 2.049 1.00 33.36 N ANISOU 827 ND2 ASN A 98 5224 3848 3601 25 13 -343 N ATOM 828 N LEU A 99 15.654 34.906 -0.713 1.00 33.69 N ANISOU 828 N LEU A 99 5305 3802 3693 156 144 -519 N ATOM 829 CA LEU A 99 15.650 35.927 -1.762 1.00 37.19 C ANISOU 829 CA LEU A 99 5740 4218 4171 181 147 -553 C ATOM 830 C LEU A 99 14.761 37.131 -1.459 1.00 40.97 C ANISOU 830 C LEU A 99 6276 4675 4616 213 213 -594 C ATOM 831 O LEU A 99 15.085 38.266 -1.803 1.00 42.67 O ANISOU 831 O LEU A 99 6527 4860 4826 216 206 -626 O ATOM 832 CB LEU A 99 15.220 35.311 -3.104 1.00 36.18 C ANISOU 832 CB LEU A 99 5514 4099 4134 211 150 -538 C ATOM 833 CG LEU A 99 16.065 34.185 -3.695 1.00 43.08 C ANISOU 833 CG LEU A 99 6320 4989 5059 187 90 -506 C ATOM 834 CD1 LEU A 99 15.390 33.621 -4.948 1.00 37.48 C ANISOU 834 CD1 LEU A 99 5519 4290 4432 218 108 -499 C ATOM 835 CD2 LEU A 99 17.465 34.657 -4.011 1.00 44.14 C ANISOU 835 CD2 LEU A 99 6469 5112 5189 153 21 -514 C ATOM 836 N ILE A 100 13.614 36.858 -0.852 1.00 34.33 N ANISOU 836 N ILE A 100 5243 3517 4283 -931 -481 -328 N ATOM 837 CA ILE A 100 12.564 37.851 -0.662 1.00 41.42 C ANISOU 837 CA ILE A 100 6146 4409 5183 -920 -477 -365 C ATOM 838 C ILE A 100 12.520 38.332 0.784 1.00 49.78 C ANISOU 838 C ILE A 100 7246 5453 6217 -929 -481 -379 C ATOM 839 O ILE A 100 12.643 39.526 1.063 1.00 42.71 O ANISOU 839 O ILE A 100 6363 4542 5321 -927 -508 -385 O ATOM 840 CB ILE A 100 11.187 37.318 -1.086 1.00 39.29 C ANISOU 840 CB ILE A 100 5855 4153 4920 -909 -437 -399 C ATOM 841 CG1 ILE A 100 11.173 37.036 -2.591 1.00 47.36 C ANISOU 841 CG1 ILE A 100 6836 5189 5968 -898 -436 -387 C ATOM 842 CG2 ILE A 100 10.098 38.305 -0.709 1.00 43.05 C ANISOU 842 CG2 ILE A 100 6339 4621 5396 -899 -432 -440 C ATOM 843 CD1 ILE A 100 11.833 38.115 -3.447 1.00 41.45 C ANISOU 843 CD1 ILE A 100 6077 4434 5239 -893 -477 -367 C ATOM 844 N ASP A 101 12.351 37.381 1.696 1.00 43.05 N ANISOU 844 N ASP A 101 6412 4604 5342 -941 -455 -384 N ATOM 845 CA ASP A 101 12.084 37.657 3.112 1.00 54.34 C ANISOU 845 CA ASP A 101 7879 6023 6745 -951 -449 -404 C ATOM 846 C ASP A 101 13.320 38.075 3.908 1.00 59.66 C ANISOU 846 C ASP A 101 8583 6682 7404 -965 -485 -375 C ATOM 847 O ASP A 101 13.295 38.076 5.140 1.00 78.13 O ANISOU 847 O ASP A 101 10955 9013 9717 -978 -480 -384 O ATOM 848 CB ASP A 101 11.431 36.447 3.776 1.00 60.90 C ANISOU 848 CB ASP A 101 8719 6862 7556 -961 -407 -420 C ATOM 849 CG ASP A 101 10.124 36.075 3.128 1.00 66.96 C ANISOU 849 CG ASP A 101 9460 7644 8337 -948 -370 -453 C ATOM 850 OD1 ASP A 101 9.448 36.993 2.618 1.00 68.17 O ANISOU 850 OD1 ASP A 101 9599 7796 8507 -933 -375 -477 O ATOM 851 OD2 ASP A 101 9.779 34.872 3.120 1.00 74.42 O ANISOU 851 OD2 ASP A 101 10399 8602 9276 -953 -338 -455 O ATOM 852 N SER A 102 14.414 38.369 3.208 1.00 56.81 N ANISOU 852 N SER A 102 8209 6318 7057 -964 -518 -341 N ATOM 853 CA SER A 102 15.681 38.714 3.855 1.00 50.77 C ANISOU 853 CA SER A 102 7469 5540 6279 -977 -553 -311 C ATOM 854 C SER A 102 16.161 40.135 3.512 1.00 52.03 C ANISOU 854 C SER A 102 7629 5688 6453 -971 -593 -304 C ATOM 855 O SER A 102 15.657 40.760 2.581 1.00 51.87 O ANISOU 855 O SER A 102 7585 5669 6453 -957 -596 -316 O ATOM 856 CB SER A 102 16.760 37.689 3.487 1.00 47.65 C ANISOU 856 CB SER A 102 7065 5153 5889 -985 -560 -271 C ATOM 857 OG SER A 102 17.445 38.059 2.300 1.00 47.58 O ANISOU 857 OG SER A 102 7028 5147 5905 -978 -585 -248 O ATOM 858 N PRO A 103 17.112 40.663 4.305 1.00 56.05 N ANISOU 858 N PRO A 103 8166 6183 6947 -983 -623 -287 N ATOM 859 CA PRO A 103 17.767 41.958 4.066 1.00 53.41 C ANISOU 859 CA PRO A 103 7834 5836 6623 -980 -664 -275 C ATOM 860 C PRO A 103 18.642 41.982 2.804 1.00 48.33 C ANISOU 860 C PRO A 103 7163 5199 6004 -977 -687 -243 C ATOM 861 O PRO A 103 19.104 43.052 2.410 1.00 45.72 O ANISOU 861 O PRO A 103 6830 4859 5685 -974 -719 -234 O ATOM 862 CB PRO A 103 18.629 42.161 5.325 1.00 56.06 C ANISOU 862 CB PRO A 103 8208 6159 6934 -996 -684 -262 C ATOM 863 CG PRO A 103 18.826 40.806 5.881 1.00 59.55 C ANISOU 863 CG PRO A 103 8659 6609 7359 -1008 -663 -250 C ATOM 864 CD PRO A 103 17.571 40.043 5.563 1.00 56.36 C ANISOU 864 CD PRO A 103 8238 6218 6958 -999 -619 -278 C ATOM 865 N GLN A 104 18.907 40.812 2.221 1.00 42.50 N ANISOU 865 N GLN A 104 6402 4474 5271 -978 -671 -225 N ATOM 866 CA GLN A 104 19.742 40.701 1.021 1.00 46.22 C ANISOU 866 CA GLN A 104 6844 4953 5764 -977 -690 -195 C ATOM 867 C GLN A 104 18.911 40.820 -0.258 1.00 39.87 C ANISOU 867 C GLN A 104 6006 4159 4984 -962 -676 -209 C ATOM 868 O GLN A 104 19.416 40.615 -1.356 1.00 39.05 O ANISOU 868 O GLN A 104 5874 4065 4898 -961 -685 -188 O ATOM 869 CB GLN A 104 20.503 39.370 1.001 1.00 52.41 C ANISOU 869 CB GLN A 104 7621 5746 6545 -986 -682 -168 C ATOM 870 CG GLN A 104 21.632 39.264 2.011 1.00 59.85 C ANISOU 870 CG GLN A 104 8593 6679 7470 -1001 -704 -145 C ATOM 871 CD GLN A 104 21.143 38.918 3.408 1.00 59.21 C ANISOU 871 CD GLN A 104 8546 6591 7360 -1009 -686 -163 C ATOM 872 OE1 GLN A 104 20.154 38.201 3.578 1.00 52.83 O ANISOU 872 OE1 GLN A 104 7737 5791 6546 -1006 -650 -184 O ATOM 873 NE2 GLN A 104 21.840 39.428 4.414 1.00 51.08 N ANISOU 873 NE2 GLN A 104 7548 5547 6313 -1019 -711 -153 N ATOM 874 N TYR A 105 17.633 41.132 -0.100 1.00 39.36 N ANISOU 874 N TYR A 105 5942 4094 4918 -951 -655 -245 N ATOM 875 CA TYR A 105 16.723 41.201 -1.226 1.00 41.83 C ANISOU 875 CA TYR A 105 6224 4417 5252 -936 -640 -262 C ATOM 876 C TYR A 105 17.320 41.970 -2.404 1.00 38.02 C ANISOU 876 C TYR A 105 5720 3934 4792 -933 -671 -241 C ATOM 877 O TYR A 105 17.316 41.476 -3.532 1.00 32.59 O ANISOU 877 O TYR A 105 5001 3260 4121 -929 -664 -231 O ATOM 878 CB TYR A 105 15.412 41.853 -0.797 1.00 42.74 C ANISOU 878 CB TYR A 105 6348 4526 5364 -925 -624 -304 C ATOM 879 CG TYR A 105 14.516 42.202 -1.953 1.00 45.08 C ANISOU 879 CG TYR A 105 6614 4829 5684 -909 -617 -322 C ATOM 880 CD1 TYR A 105 13.719 41.233 -2.554 1.00 41.65 C ANISOU 880 CD1 TYR A 105 6155 4412 5258 -902 -582 -335 C ATOM 881 CD2 TYR A 105 14.458 43.499 -2.446 1.00 48.54 C ANISOU 881 CD2 TYR A 105 7050 5256 6138 -900 -647 -326 C ATOM 882 CE1 TYR A 105 12.896 41.545 -3.622 1.00 42.58 C ANISOU 882 CE1 TYR A 105 6244 4537 5397 -886 -576 -351 C ATOM 883 CE2 TYR A 105 13.640 43.819 -3.517 1.00 46.23 C ANISOU 883 CE2 TYR A 105 6730 4969 5866 -885 -642 -341 C ATOM 884 CZ TYR A 105 12.862 42.838 -4.098 1.00 47.82 C ANISOU 884 CZ TYR A 105 6906 5189 6075 -878 -607 -354 C ATOM 885 OH TYR A 105 12.041 43.146 -5.156 1.00 58.59 O ANISOU 885 OH TYR A 105 8243 6559 7460 -863 -603 -370 O ATOM 886 N LYS A 106 17.848 43.164 -2.151 1.00 30.70 N ANISOU 886 N LYS A 106 4810 2990 3864 -935 -707 -235 N ATOM 887 CA LYS A 106 18.327 43.992 -3.255 1.00 38.26 C ANISOU 887 CA LYS A 106 5750 3946 4841 -932 -737 -217 C ATOM 888 C LYS A 106 19.573 43.411 -3.893 1.00 35.10 C ANISOU 888 C LYS A 106 5334 3555 4446 -944 -751 -179 C ATOM 889 O LYS A 106 19.754 43.517 -5.099 1.00 33.63 O ANISOU 889 O LYS A 106 5121 3378 4279 -941 -759 -166 O ATOM 890 CB LYS A 106 18.567 45.443 -2.823 1.00 42.95 C ANISOU 890 CB LYS A 106 6367 4519 5433 -933 -772 -220 C ATOM 891 CG LYS A 106 17.300 46.248 -2.637 1.00 47.47 C ANISOU 891 CG LYS A 106 6945 5082 6010 -918 -764 -259 C ATOM 892 CD LYS A 106 16.454 46.272 -3.910 1.00 46.90 C ANISOU 892 CD LYS A 106 6840 5019 5960 -903 -754 -270 C ATOM 893 CE LYS A 106 17.170 46.937 -5.085 1.00 52.01 C ANISOU 893 CE LYS A 106 7470 5665 6625 -905 -787 -243 C ATOM 894 NZ LYS A 106 17.442 48.395 -4.871 1.00 56.18 N ANISOU 894 NZ LYS A 106 8017 6171 7155 -905 -825 -243 N ATOM 895 N LEU A 107 20.432 42.797 -3.083 1.00 35.36 N ANISOU 895 N LEU A 107 5383 3587 4464 -957 -753 -161 N ATOM 896 CA LEU A 107 21.626 42.135 -3.614 1.00 31.54 C ANISOU 896 CA LEU A 107 4884 3113 3987 -968 -765 -126 C ATOM 897 C LEU A 107 21.270 41.009 -4.597 1.00 29.87 C ANISOU 897 C LEU A 107 4638 2923 3789 -963 -736 -125 C ATOM 898 O LEU A 107 21.889 40.878 -5.649 1.00 29.59 O ANISOU 898 O LEU A 107 4577 2897 3769 -966 -747 -104 O ATOM 899 CB LEU A 107 22.484 41.580 -2.477 1.00 39.01 C ANISOU 899 CB LEU A 107 5855 4054 4913 -981 -770 -111 C ATOM 900 CG LEU A 107 23.820 42.228 -2.077 1.00 43.20 C ANISOU 900 CG LEU A 107 6403 4572 5438 -993 -810 -85 C ATOM 901 CD1 LEU A 107 24.012 43.676 -2.557 1.00 26.35 C ANISOU 901 CD1 LEU A 107 4270 2427 3315 -992 -842 -83 C ATOM 902 CD2 LEU A 107 24.019 42.115 -0.574 1.00 30.52 C ANISOU 902 CD2 LEU A 107 4834 2954 3808 -1001 -811 -88 C ATOM 903 N TYR A 108 20.292 40.186 -4.233 1.00 30.40 N ANISOU 903 N TYR A 108 4705 2997 3849 -957 -699 -148 N ATOM 904 CA TYR A 108 19.888 39.066 -5.071 1.00 27.87 C ANISOU 904 CA TYR A 108 4354 2696 3541 -952 -669 -149 C ATOM 905 C TYR A 108 19.213 39.574 -6.344 1.00 26.30 C ANISOU 905 C TYR A 108 4125 2505 3362 -941 -667 -159 C ATOM 906 O TYR A 108 19.401 39.017 -7.431 1.00 29.31 O ANISOU 906 O TYR A 108 4476 2903 3759 -941 -661 -147 O ATOM 907 CB TYR A 108 18.928 38.150 -4.306 1.00 29.77 C ANISOU 907 CB TYR A 108 4604 2940 3767 -949 -629 -173 C ATOM 908 CG TYR A 108 19.581 37.198 -3.312 1.00 33.63 C ANISOU 908 CG TYR A 108 5112 3426 4238 -961 -623 -159 C ATOM 909 CD1 TYR A 108 20.422 36.181 -3.743 1.00 38.78 C ANISOU 909 CD1 TYR A 108 5747 4090 4899 -968 -622 -133 C ATOM 910 CD2 TYR A 108 19.306 37.286 -1.945 1.00 35.70 C ANISOU 910 CD2 TYR A 108 5410 3676 4477 -965 -618 -173 C ATOM 911 CE1 TYR A 108 21.004 35.294 -2.836 1.00 35.65 C ANISOU 911 CE1 TYR A 108 5368 3689 4486 -979 -618 -120 C ATOM 912 CE2 TYR A 108 19.872 36.399 -1.038 1.00 35.03 C ANISOU 912 CE2 TYR A 108 5344 3589 4375 -977 -613 -159 C ATOM 913 CZ TYR A 108 20.717 35.409 -1.494 1.00 36.76 C ANISOU 913 CZ TYR A 108 5546 3817 4603 -983 -614 -132 C ATOM 914 OH TYR A 108 21.294 34.535 -0.610 1.00 38.86 O ANISOU 914 OH TYR A 108 5831 4079 4853 -994 -612 -118 O ATOM 915 N LYS A 109 18.419 40.627 -6.201 1.00 29.19 N ANISOU 915 N LYS A 109 4503 2860 3729 -931 -674 -182 N ATOM 916 CA LYS A 109 17.720 41.199 -7.342 1.00 30.57 C ANISOU 916 CA LYS A 109 4654 3041 3923 -919 -675 -194 C ATOM 917 C LYS A 109 18.700 41.557 -8.459 1.00 29.20 C ANISOU 917 C LYS A 109 4459 2871 3763 -926 -704 -163 C ATOM 918 O LYS A 109 18.529 41.143 -9.593 1.00 33.72 O ANISOU 918 O LYS A 109 5001 3460 4351 -923 -694 -159 O ATOM 919 CB LYS A 109 16.910 42.428 -6.920 1.00 41.03 C ANISOU 919 CB LYS A 109 5997 4349 5246 -909 -686 -220 C ATOM 920 CG LYS A 109 16.114 43.057 -8.072 1.00 39.10 C ANISOU 920 CG LYS A 109 5728 4107 5021 -895 -689 -234 C ATOM 921 CD LYS A 109 15.150 44.101 -7.548 1.00 51.94 C ANISOU 921 CD LYS A 109 7371 5716 6646 -883 -694 -266 C ATOM 922 CE LYS A 109 14.363 44.768 -8.667 1.00 60.13 C ANISOU 922 CE LYS A 109 8387 6756 7705 -869 -701 -279 C ATOM 923 NZ LYS A 109 13.359 45.728 -8.111 1.00 67.48 N ANISOU 923 NZ LYS A 109 9333 7670 8636 -855 -704 -314 N ATOM 924 N TYR A 110 19.740 42.314 -8.131 1.00 29.92 N ANISOU 924 N TYR A 110 4569 2950 3851 -937 -739 -142 N ATOM 925 CA TYR A 110 20.690 42.736 -9.151 1.00 31.95 C ANISOU 925 CA TYR A 110 4809 3210 4120 -945 -768 -114 C ATOM 926 C TYR A 110 21.512 41.578 -9.680 1.00 35.38 C ANISOU 926 C TYR A 110 5220 3664 4560 -956 -758 -90 C ATOM 927 O TYR A 110 21.919 41.580 -10.839 1.00 35.30 O ANISOU 927 O TYR A 110 5184 3665 4564 -960 -767 -75 O ATOM 928 CB TYR A 110 21.612 43.821 -8.606 1.00 33.43 C ANISOU 928 CB TYR A 110 5022 3378 4300 -955 -807 -99 C ATOM 929 CG TYR A 110 20.892 45.109 -8.315 1.00 37.17 C ANISOU 929 CG TYR A 110 5514 3834 4774 -945 -823 -120 C ATOM 930 CD1 TYR A 110 20.205 45.791 -9.315 1.00 44.27 C ANISOU 930 CD1 TYR A 110 6397 4734 5689 -935 -829 -129 C ATOM 931 CD2 TYR A 110 20.910 45.652 -7.048 1.00 39.00 C ANISOU 931 CD2 TYR A 110 5780 4047 4990 -946 -832 -130 C ATOM 932 CE1 TYR A 110 19.545 46.985 -9.040 1.00 43.67 C ANISOU 932 CE1 TYR A 110 6339 4640 5615 -925 -844 -149 C ATOM 933 CE2 TYR A 110 20.267 46.835 -6.764 1.00 39.28 C ANISOU 933 CE2 TYR A 110 5832 4066 5026 -937 -846 -150 C ATOM 934 CZ TYR A 110 19.583 47.499 -7.760 1.00 46.42 C ANISOU 934 CZ TYR A 110 6720 4970 5948 -926 -853 -160 C ATOM 935 OH TYR A 110 18.943 48.676 -7.448 1.00 52.34 O ANISOU 935 OH TYR A 110 7486 5701 6700 -916 -868 -182 O ATOM 936 N ARG A 111 21.763 40.597 -8.818 1.00 40.94 N ANISOU 936 N ARG A 111 5934 4369 5251 -960 -741 -88 N ATOM 937 CA ARG A 111 22.511 39.401 -9.194 1.00 35.57 C ANISOU 937 CA ARG A 111 5233 3705 4576 -969 -730 -68 C ATOM 938 C ARG A 111 21.768 38.570 -10.240 1.00 37.44 C ANISOU 938 C ARG A 111 5436 3963 4828 -961 -699 -78 C ATOM 939 O ARG A 111 22.382 37.919 -11.096 1.00 33.10 O ANISOU 939 O ARG A 111 4858 3428 4289 -968 -697 -60 O ATOM 940 CB ARG A 111 22.779 38.554 -7.943 1.00 42.54 C ANISOU 940 CB ARG A 111 6139 4583 5442 -974 -718 -67 C ATOM 941 CG ARG A 111 23.744 37.409 -8.147 1.00 51.58 C ANISOU 941 CG ARG A 111 7267 5739 6592 -984 -714 -44 C ATOM 942 CD ARG A 111 24.303 36.950 -6.806 1.00 64.98 C ANISOU 942 CD ARG A 111 8994 7425 8271 -991 -717 -37 C ATOM 943 NE ARG A 111 24.911 35.615 -6.796 1.00 71.19 N ANISOU 943 NE ARG A 111 9767 8220 9059 -997 -705 -22 N ATOM 944 CZ ARG A 111 25.101 34.824 -7.853 1.00 71.02 C ANISOU 944 CZ ARG A 111 9711 8218 9057 -998 -692 -13 C ATOM 945 NH1 ARG A 111 24.746 35.195 -9.083 1.00 69.00 N ANISOU 945 NH1 ARG A 111 9427 7974 8817 -993 -690 -17 N ATOM 946 NH2 ARG A 111 25.663 33.637 -7.670 1.00 70.96 N ANISOU 946 NH2 ARG A 111 9695 8216 9050 -1003 -683 -1 N ATOM 947 N PHE A 112 20.445 38.539 -10.126 1.00 27.63 N ANISOU 947 N PHE A 112 4194 2721 3584 -948 -673 -107 N ATOM 948 CA PHE A 112 19.610 37.851 -11.104 1.00 33.35 C ANISOU 948 CA PHE A 112 4886 3464 4321 -939 -644 -120 C ATOM 949 C PHE A 112 19.248 38.687 -12.339 1.00 38.77 C ANISOU 949 C PHE A 112 5551 4155 5023 -933 -657 -122 C ATOM 950 O PHE A 112 19.262 38.187 -13.461 1.00 42.33 O ANISOU 950 O PHE A 112 5971 4625 5489 -934 -647 -116 O ATOM 951 CB PHE A 112 18.367 37.281 -10.429 1.00 31.31 C ANISOU 951 CB PHE A 112 4637 3207 4055 -928 -607 -151 C ATOM 952 CG PHE A 112 18.653 36.050 -9.633 1.00 34.64 C ANISOU 952 CG PHE A 112 5066 3631 4464 -934 -586 -147 C ATOM 953 CD1 PHE A 112 18.703 34.814 -10.261 1.00 38.52 C ANISOU 953 CD1 PHE A 112 5530 4141 4966 -936 -561 -141 C ATOM 954 CD2 PHE A 112 18.905 36.125 -8.279 1.00 36.74 C ANISOU 954 CD2 PHE A 112 5368 3882 4711 -940 -591 -147 C ATOM 955 CE1 PHE A 112 18.983 33.680 -9.545 1.00 42.23 C ANISOU 955 CE1 PHE A 112 6008 4612 5426 -942 -543 -135 C ATOM 956 CE2 PHE A 112 19.191 34.988 -7.548 1.00 41.27 C ANISOU 956 CE2 PHE A 112 5950 4457 5273 -946 -573 -142 C ATOM 957 CZ PHE A 112 19.230 33.764 -8.187 1.00 39.13 C ANISOU 957 CZ PHE A 112 5652 4203 5013 -947 -549 -135 C ATOM 958 N LEU A 113 18.904 39.950 -12.121 1.00 30.80 N ANISOU 958 N LEU A 113 4560 3129 4012 -928 -679 -132 N ATOM 959 CA LEU A 113 18.471 40.813 -13.218 1.00 33.23 C ANISOU 959 CA LEU A 113 4852 3439 4334 -921 -693 -136 C ATOM 960 C LEU A 113 19.643 41.415 -13.999 1.00 40.72 C ANISOU 960 C LEU A 113 5793 4388 5290 -936 -728 -105 C ATOM 961 O LEU A 113 19.542 41.614 -15.208 1.00 41.35 O ANISOU 961 O LEU A 113 5848 4479 5383 -936 -734 -99 O ATOM 962 CB LEU A 113 17.555 41.915 -12.698 1.00 31.70 C ANISOU 962 CB LEU A 113 4681 3227 4138 -909 -702 -162 C ATOM 963 CG LEU A 113 16.252 41.451 -12.060 1.00 35.06 C ANISOU 963 CG LEU A 113 5111 3653 4558 -894 -667 -197 C ATOM 964 CD1 LEU A 113 15.434 42.655 -11.697 1.00 36.98 C ANISOU 964 CD1 LEU A 113 5372 3878 4802 -882 -680 -222 C ATOM 965 CD2 LEU A 113 15.476 40.548 -13.008 1.00 33.57 C ANISOU 965 CD2 LEU A 113 4888 3486 4381 -886 -635 -208 C ATOM 966 N ASP A 114 20.740 41.746 -13.316 1.00 35.88 N ANISOU 966 N ASP A 114 4959 5392 3283 -499 -1078 111 N ATOM 967 CA ASP A 114 21.914 42.216 -14.046 1.00 38.72 C ANISOU 967 CA ASP A 114 5345 5760 3608 -564 -1070 105 C ATOM 968 C ASP A 114 23.133 41.401 -13.740 1.00 45.99 C ANISOU 968 C ASP A 114 6211 6708 4555 -598 -1043 86 C ATOM 969 O ASP A 114 23.866 41.694 -12.808 1.00 56.97 O ANISOU 969 O ASP A 114 7607 8090 5950 -608 -1039 90 O ATOM 970 CB ASP A 114 22.211 43.653 -13.641 1.00 46.34 C ANISOU 970 CB ASP A 114 6385 6691 4529 -578 -1089 126 C ATOM 971 CG ASP A 114 21.029 44.561 -13.858 1.00 60.18 C ANISOU 971 CG ASP A 114 8198 8414 6253 -542 -1118 146 C ATOM 972 OD1 ASP A 114 20.815 44.988 -15.017 1.00 61.55 O ANISOU 972 OD1 ASP A 114 8407 8588 6392 -563 -1128 147 O ATOM 973 OD2 ASP A 114 20.312 44.832 -12.870 1.00 56.98 O ANISOU 973 OD2 ASP A 114 7805 7987 5860 -492 -1132 160 O ATOM 974 N TRP A 115 23.421 40.464 -14.618 1.00 37.95 N ANISOU 974 N TRP A 115 5146 5723 3552 -620 -1026 64 N ATOM 975 CA TRP A 115 24.553 39.588 -14.461 1.00 34.47 C ANISOU 975 CA TRP A 115 4649 5312 3136 -652 -1000 42 C ATOM 976 C TRP A 115 24.906 39.295 -15.905 1.00 36.08 C ANISOU 976 C TRP A 115 4844 5543 3321 -693 -990 26 C ATOM 977 O TRP A 115 24.021 39.075 -16.724 1.00 38.98 O ANISOU 977 O TRP A 115 5212 5914 3686 -676 -998 25 O ATOM 978 CB TRP A 115 24.119 38.316 -13.726 1.00 39.02 C ANISOU 978 CB TRP A 115 5155 5900 3770 -608 -989 32 C ATOM 979 CG TRP A 115 25.236 37.431 -13.216 1.00 44.47 C ANISOU 979 CG TRP A 115 5789 6615 4493 -629 -965 12 C ATOM 980 CD1 TRP A 115 25.665 36.259 -13.771 1.00 44.98 C ANISOU 980 CD1 TRP A 115 5794 6715 4584 -645 -945 -14 C ATOM 981 CD2 TRP A 115 26.051 37.642 -12.048 1.00 37.59 C ANISOU 981 CD2 TRP A 115 4916 5734 3631 -635 -959 15 C ATOM 982 NE1 TRP A 115 26.688 35.730 -13.029 1.00 42.16 N ANISOU 982 NE1 TRP A 115 5397 6371 4251 -659 -928 -27 N ATOM 983 CE2 TRP A 115 26.946 36.555 -11.965 1.00 38.04 C ANISOU 983 CE2 TRP A 115 4910 5824 3721 -654 -936 -10 C ATOM 984 CE3 TRP A 115 26.100 38.636 -11.061 1.00 35.23 C ANISOU 984 CE3 TRP A 115 4664 5405 3318 -625 -972 35 C ATOM 985 CZ2 TRP A 115 27.886 36.432 -10.939 1.00 37.87 C ANISOU 985 CZ2 TRP A 115 4869 5802 3716 -663 -925 -15 C ATOM 986 CZ3 TRP A 115 27.039 38.515 -10.040 1.00 38.01 C ANISOU 986 CZ3 TRP A 115 4997 5757 3686 -635 -961 31 C ATOM 987 CH2 TRP A 115 27.921 37.419 -9.989 1.00 34.48 C ANISOU 987 CH2 TRP A 115 4486 5343 3272 -654 -938 6 C ATOM 988 N THR A 116 26.189 39.286 -16.217 1.00 46.18 N ANISOU 988 N THR A 116 6115 6844 4588 -748 -973 12 N ATOM 989 CA THR A 116 26.637 39.055 -17.573 1.00 50.49 C ANISOU 989 CA THR A 116 6654 7417 5112 -792 -963 -4 C ATOM 990 C THR A 116 27.668 37.954 -17.523 1.00 52.51 C ANISOU 990 C THR A 116 6841 7710 5398 -816 -936 -31 C ATOM 991 O THR A 116 28.179 37.630 -16.451 1.00 52.05 O ANISOU 991 O THR A 116 6754 7653 5369 -807 -927 -35 O ATOM 992 CB THR A 116 27.288 40.318 -18.150 1.00 51.47 C ANISOU 992 CB THR A 116 6845 7533 5179 -844 -970 7 C ATOM 993 OG1 THR A 116 28.289 40.780 -17.242 1.00 61.51 O ANISOU 993 OG1 THR A 116 8126 8797 6446 -868 -964 11 O ATOM 994 CG2 THR A 116 26.248 41.411 -18.330 1.00 47.69 C ANISOU 994 CG2 THR A 116 6437 7017 4666 -821 -999 33 C ATOM 995 N TYR A 117 27.972 37.375 -18.677 1.00 45.53 N ANISOU 995 N TYR A 117 5931 6858 4509 -844 -923 -51 N ATOM 996 CA TYR A 117 29.028 36.375 -18.767 1.00 43.82 C ANISOU 996 CA TYR A 117 5653 6681 4317 -871 -898 -79 C ATOM 997 C TYR A 117 30.343 36.889 -18.162 1.00 44.08 C ANISOU 997 C TYR A 117 5695 6718 4336 -912 -888 -80 C ATOM 998 O TYR A 117 31.142 36.103 -17.656 1.00 41.76 O ANISOU 998 O TYR A 117 5349 6446 4073 -918 -870 -99 O ATOM 999 CB TYR A 117 29.252 35.955 -20.227 1.00 47.49 C ANISOU 999 CB TYR A 117 6103 7177 4763 -904 -888 -98 C ATOM 1000 CG TYR A 117 30.364 34.946 -20.394 1.00 44.09 C ANISOU 1000 CG TYR A 117 5610 6789 4355 -932 -862 -129 C ATOM 1001 CD1 TYR A 117 30.238 33.657 -19.890 1.00 47.15 C ANISOU 1001 CD1 TYR A 117 5930 7190 4794 -899 -852 -146 C ATOM 1002 CD2 TYR A 117 31.545 35.282 -21.042 1.00 53.24 C ANISOU 1002 CD2 TYR A 117 6776 7972 5480 -992 -848 -140 C ATOM 1003 CE1 TYR A 117 31.259 32.727 -20.034 1.00 51.61 C ANISOU 1003 CE1 TYR A 117 6438 7793 5379 -922 -830 -175 C ATOM 1004 CE2 TYR A 117 32.570 34.361 -21.189 1.00 55.75 C ANISOU 1004 CE2 TYR A 117 7035 8330 5817 -1016 -825 -169 C ATOM 1005 CZ TYR A 117 32.419 33.084 -20.686 1.00 55.61 C ANISOU 1005 CZ TYR A 117 6952 8325 5852 -980 -816 -187 C ATOM 1006 OH TYR A 117 33.433 32.161 -20.829 1.00 69.28 O ANISOU 1006 OH TYR A 117 8626 10096 7602 -1002 -795 -217 O ATOM 1007 N GLU A 118 30.563 38.203 -18.213 1.00 40.27 N ANISOU 1007 N GLU A 118 5280 6213 3808 -940 -900 -60 N ATOM 1008 CA GLU A 118 31.767 38.793 -17.635 1.00 50.11 C ANISOU 1008 CA GLU A 118 6541 7461 5039 -980 -892 -58 C ATOM 1009 C GLU A 118 31.858 38.423 -16.160 1.00 60.28 C ANISOU 1009 C GLU A 118 7799 8736 6368 -945 -890 -57 C ATOM 1010 O GLU A 118 32.856 37.864 -15.695 1.00 66.31 O ANISOU 1010 O GLU A 118 8519 9523 7153 -963 -872 -74 O ATOM 1011 CB GLU A 118 31.744 40.315 -17.772 1.00 62.95 C ANISOU 1011 CB GLU A 118 8250 9056 6612 -1005 -911 -32 C ATOM 1012 CG GLU A 118 32.873 41.006 -17.012 1.00 76.79 C ANISOU 1012 CG GLU A 118 10022 10803 8349 -1042 -907 -27 C ATOM 1013 CD GLU A 118 32.556 42.448 -16.630 1.00 83.95 C ANISOU 1013 CD GLU A 118 11012 11668 9219 -1043 -932 4 C ATOM 1014 OE1 GLU A 118 31.465 42.946 -16.986 1.00 83.04 O ANISOU 1014 OE1 GLU A 118 10939 11526 9085 -1015 -952 21 O ATOM 1015 OE2 GLU A 118 33.403 43.083 -15.962 1.00 89.10 O ANISOU 1015 OE2 GLU A 118 11685 12311 9857 -1070 -931 11 O ATOM 1016 N LEU A 119 30.800 38.741 -15.426 1.00 47.67 N ANISOU 1016 N LEU A 119 6227 7104 4782 -895 -909 -36 N ATOM 1017 CA LEU A 119 30.733 38.408 -14.016 1.00 41.09 C ANISOU 1017 CA LEU A 119 5368 6256 3987 -856 -909 -32 C ATOM 1018 C LEU A 119 30.712 36.894 -13.824 1.00 45.44 C ANISOU 1018 C LEU A 119 5840 6834 4591 -831 -892 -56 C ATOM 1019 O LEU A 119 31.413 36.359 -12.966 1.00 40.60 O ANISOU 1019 O LEU A 119 5189 6231 4008 -830 -880 -67 O ATOM 1020 CB LEU A 119 29.509 39.069 -13.378 1.00 36.93 C ANISOU 1020 CB LEU A 119 4885 5687 3457 -806 -933 -5 C ATOM 1021 CG LEU A 119 29.503 40.603 -13.378 1.00 40.83 C ANISOU 1021 CG LEU A 119 5463 6150 3902 -824 -953 20 C ATOM 1022 CD1 LEU A 119 28.105 41.162 -13.149 1.00 38.93 C ANISOU 1022 CD1 LEU A 119 5263 5873 3654 -773 -979 43 C ATOM 1023 CD2 LEU A 119 30.480 41.167 -12.338 1.00 39.46 C ANISOU 1023 CD2 LEU A 119 5305 5965 3724 -845 -951 26 C ATOM 1024 N GLU A 120 29.918 36.195 -14.630 1.00 44.76 N ANISOU 1024 N GLU A 120 5730 6760 4517 -811 -892 -64 N ATOM 1025 CA GLU A 120 29.837 34.744 -14.493 1.00 44.32 C ANISOU 1025 CA GLU A 120 5602 6729 4511 -787 -878 -86 C ATOM 1026 C GLU A 120 31.212 34.072 -14.600 1.00 47.29 C ANISOU 1026 C GLU A 120 5930 7141 4897 -827 -855 -114 C ATOM 1027 O GLU A 120 31.545 33.203 -13.793 1.00 54.62 O ANISOU 1027 O GLU A 120 6809 8078 5867 -809 -845 -127 O ATOM 1028 CB GLU A 120 28.880 34.146 -15.522 1.00 53.23 C ANISOU 1028 CB GLU A 120 6714 7867 5644 -768 -882 -93 C ATOM 1029 CG GLU A 120 28.492 32.715 -15.215 1.00 65.52 C ANISOU 1029 CG GLU A 120 8202 9438 7254 -731 -873 -110 C ATOM 1030 CD GLU A 120 27.570 32.620 -14.019 1.00 80.18 C ANISOU 1030 CD GLU A 120 10056 11266 9141 -676 -885 -92 C ATOM 1031 OE1 GLU A 120 26.347 32.793 -14.206 1.00 82.94 O ANISOU 1031 OE1 GLU A 120 10425 11598 9489 -641 -901 -78 O ATOM 1032 OE2 GLU A 120 28.066 32.384 -12.893 1.00 85.28 O ANISOU 1032 OE2 GLU A 120 10681 11908 9812 -666 -879 -94 O ATOM 1033 N ARG A 121 32.005 34.479 -15.590 1.00 44.81 N ANISOU 1033 N ARG A 121 5632 6847 4546 -881 -847 -123 N ATOM 1034 CA ARG A 121 33.325 33.890 -15.804 1.00 46.74 C ANISOU 1034 CA ARG A 121 5832 7130 4796 -921 -825 -150 C ATOM 1035 C ARG A 121 34.210 34.003 -14.570 1.00 54.42 C ANISOU 1035 C ARG A 121 6795 8098 5784 -926 -819 -150 C ATOM 1036 O ARG A 121 34.848 33.033 -14.158 1.00 53.49 O ANISOU 1036 O ARG A 121 6620 8003 5700 -923 -804 -173 O ATOM 1037 CB ARG A 121 34.038 34.549 -16.991 1.00 53.60 C ANISOU 1037 CB ARG A 121 6731 8019 5616 -981 -819 -155 C ATOM 1038 CG ARG A 121 35.257 33.763 -17.467 1.00 63.38 C ANISOU 1038 CG ARG A 121 7917 9305 6861 -1020 -795 -187 C ATOM 1039 CD ARG A 121 36.219 34.609 -18.295 1.00 72.74 C ANISOU 1039 CD ARG A 121 9135 10509 7995 -1085 -788 -189 C ATOM 1040 NE ARG A 121 35.525 35.556 -19.162 1.00 80.06 N ANISOU 1040 NE ARG A 121 10124 11416 8878 -1097 -803 -168 N ATOM 1041 CZ ARG A 121 35.463 36.863 -18.930 1.00 86.16 C ANISOU 1041 CZ ARG A 121 10964 12159 9614 -1113 -818 -141 C ATOM 1042 NH1 ARG A 121 36.063 37.376 -17.863 1.00 84.94 N ANISOU 1042 NH1 ARG A 121 10822 11990 9462 -1120 -819 -132 N ATOM 1043 NH2 ARG A 121 34.807 37.658 -19.766 1.00 89.09 N ANISOU 1043 NH2 ARG A 121 11390 12513 9946 -1121 -832 -124 N ATOM 1044 N ASP A 122 34.256 35.198 -13.992 1.00 53.18 N ANISOU 1044 N ASP A 122 6695 7911 5600 -934 -831 -126 N ATOM 1045 CA ASP A 122 35.144 35.460 -12.871 1.00 49.17 C ANISOU 1045 CA ASP A 122 6185 7398 5101 -944 -827 -125 C ATOM 1046 C ASP A 122 34.580 35.017 -11.520 1.00 47.15 C ANISOU 1046 C ASP A 122 5909 7119 4889 -888 -833 -117 C ATOM 1047 O ASP A 122 35.332 34.800 -10.572 1.00 49.38 O ANISOU 1047 O ASP A 122 6168 7403 5191 -890 -826 -123 O ATOM 1048 CB ASP A 122 35.529 36.942 -12.839 1.00 49.13 C ANISOU 1048 CB ASP A 122 6250 7372 5047 -981 -838 -103 C ATOM 1049 CG ASP A 122 36.265 37.374 -14.092 1.00 56.30 C ANISOU 1049 CG ASP A 122 7175 8306 5911 -1042 -830 -111 C ATOM 1050 OD1 ASP A 122 36.798 36.491 -14.800 1.00 54.94 O ANISOU 1050 OD1 ASP A 122 6952 8173 5749 -1062 -811 -138 O ATOM 1051 OD2 ASP A 122 36.309 38.590 -14.373 1.00 58.01 O ANISOU 1051 OD2 ASP A 122 7456 8503 6082 -1071 -842 -91 O ATOM 1052 N TRP A 123 33.263 34.869 -11.431 1.00 41.42 N ANISOU 1052 N TRP A 123 5190 6370 4176 -839 -847 -103 N ATOM 1053 CA TRP A 123 32.641 34.529 -10.154 1.00 46.53 C ANISOU 1053 CA TRP A 123 5824 6995 4862 -786 -854 -93 C ATOM 1054 C TRP A 123 32.929 33.080 -9.745 1.00 54.86 C ANISOU 1054 C TRP A 123 6804 8073 5968 -767 -838 -118 C ATOM 1055 O TRP A 123 32.864 32.159 -10.567 1.00 54.33 O ANISOU 1055 O TRP A 123 6696 8033 5915 -770 -828 -138 O ATOM 1056 CB TRP A 123 31.136 34.825 -10.189 1.00 40.56 C ANISOU 1056 CB TRP A 123 5097 6209 4104 -740 -873 -71 C ATOM 1057 CG TRP A 123 30.364 34.355 -8.981 1.00 42.32 C ANISOU 1057 CG TRP A 123 5300 6412 4367 -682 -879 -61 C ATOM 1058 CD1 TRP A 123 29.436 33.348 -8.946 1.00 43.24 C ANISOU 1058 CD1 TRP A 123 5376 6533 4521 -639 -879 -66 C ATOM 1059 CD2 TRP A 123 30.426 34.886 -7.648 1.00 35.71 C ANISOU 1059 CD2 TRP A 123 4484 5547 3536 -662 -887 -45 C ATOM 1060 NE1 TRP A 123 28.930 33.217 -7.678 1.00 43.50 N ANISOU 1060 NE1 TRP A 123 5403 6544 4582 -595 -885 -54 N ATOM 1061 CE2 TRP A 123 29.521 34.145 -6.861 1.00 39.44 C ANISOU 1061 CE2 TRP A 123 4925 6009 4050 -606 -890 -41 C ATOM 1062 CE3 TRP A 123 31.169 35.908 -7.040 1.00 37.84 C ANISOU 1062 CE3 TRP A 123 4796 5801 3782 -685 -891 -33 C ATOM 1063 CZ2 TRP A 123 29.333 34.393 -5.497 1.00 40.80 C ANISOU 1063 CZ2 TRP A 123 5108 6157 4239 -573 -896 -25 C ATOM 1064 CZ3 TRP A 123 30.983 36.151 -5.679 1.00 45.85 C ANISOU 1064 CZ3 TRP A 123 5821 6789 4813 -652 -899 -18 C ATOM 1065 CH2 TRP A 123 30.070 35.398 -4.927 1.00 45.77 C ANISOU 1065 CH2 TRP A 123 5779 6770 4843 -596 -901 -15 C ATOM 1066 N LYS A 124 33.265 32.907 -8.470 1.00 58.66 N ANISOU 1066 N LYS A 124 7269 8543 6475 -748 -836 -116 N ATOM 1067 CA LYS A 124 33.558 31.601 -7.884 1.00 76.07 C ANISOU 1067 CA LYS A 124 9408 10765 8729 -727 -824 -137 C ATOM 1068 C LYS A 124 32.394 31.095 -7.024 1.00 79.29 C ANISOU 1068 C LYS A 124 9803 11150 9174 -666 -833 -124 C ATOM 1069 O LYS A 124 32.575 30.723 -5.862 1.00 80.84 O ANISOU 1069 O LYS A 124 9978 11338 9401 -643 -831 -124 O ATOM 1070 CB LYS A 124 34.848 31.660 -7.052 1.00 78.57 C ANISOU 1070 CB LYS A 124 9712 11090 9052 -751 -814 -147 C ATOM 1071 CG LYS A 124 34.868 32.717 -5.934 1.00 79.84 C ANISOU 1071 CG LYS A 124 9919 11215 9200 -742 -826 -122 C ATOM 1072 CD LYS A 124 35.002 34.144 -6.478 1.00 84.10 C ANISOU 1072 CD LYS A 124 10527 11741 9685 -779 -836 -103 C ATOM 1073 CE LYS A 124 35.544 35.123 -5.428 1.00 84.73 C ANISOU 1073 CE LYS A 124 10646 11796 9751 -787 -844 -87 C ATOM 1074 NZ LYS A 124 34.668 35.278 -4.228 1.00 80.48 N ANISOU 1074 NZ LYS A 124 10123 11222 9233 -733 -858 -66 N ATOM 1075 N ASP A 137 27.090 19.291 -14.188 1.00 64.59 N ANISOU 1075 N ASP A 137 7510 9468 7563 -517 -813 -298 N ATOM 1076 CA ASP A 137 27.501 18.973 -15.555 1.00 73.53 C ANISOU 1076 CA ASP A 137 8631 10629 8678 -546 -807 -322 C ATOM 1077 C ASP A 137 26.636 17.870 -16.170 1.00 72.27 C ANISOU 1077 C ASP A 137 8440 10476 8544 -523 -814 -333 C ATOM 1078 O ASP A 137 27.045 17.189 -17.110 1.00 88.72 O ANISOU 1078 O ASP A 137 10498 12585 10627 -540 -808 -358 O ATOM 1079 CB ASP A 137 28.983 18.580 -15.597 1.00 82.72 C ANISOU 1079 CB ASP A 137 9767 11820 9841 -577 -791 -351 C ATOM 1080 CG ASP A 137 29.449 18.178 -16.995 1.00 90.62 C ANISOU 1080 CG ASP A 137 10753 12853 10825 -606 -784 -377 C ATOM 1081 OD1 ASP A 137 30.354 17.320 -17.094 1.00 96.41 O ANISOU 1081 OD1 ASP A 137 11446 13612 11574 -617 -773 -407 O ATOM 1082 OD2 ASP A 137 28.911 18.712 -17.991 1.00 83.38 O ANISOU 1082 OD2 ASP A 137 9864 11937 9878 -617 -789 -369 O ATOM 1083 N ASN A 138 25.431 17.699 -15.643 1.00 49.53 N ANISOU 1083 N ASN A 138 5560 7573 5686 -484 -827 -313 N ATOM 1084 CA ASN A 138 24.519 16.705 -16.181 1.00 42.21 C ANISOU 1084 CA ASN A 138 4605 6651 4784 -462 -835 -320 C ATOM 1085 C ASN A 138 23.203 17.366 -16.619 1.00 33.25 C ANISOU 1085 C ASN A 138 3505 5499 3632 -445 -850 -295 C ATOM 1086 O ASN A 138 22.916 18.489 -16.222 1.00 31.48 O ANISOU 1086 O ASN A 138 3321 5255 3383 -442 -855 -270 O ATOM 1087 CB ASN A 138 24.296 15.594 -15.151 1.00 44.05 C ANISOU 1087 CB ASN A 138 4795 6875 5065 -430 -836 -323 C ATOM 1088 CG ASN A 138 23.462 16.047 -13.983 1.00 49.41 C ANISOU 1088 CG ASN A 138 5491 7525 5757 -398 -845 -293 C ATOM 1089 OD1 ASN A 138 22.238 16.001 -14.041 1.00 56.79 O ANISOU 1089 OD1 ASN A 138 6430 8447 6699 -372 -857 -276 O ATOM 1090 ND2 ASN A 138 24.119 16.494 -12.912 1.00 52.18 N ANISOU 1090 ND2 ASN A 138 5851 7866 6109 -400 -839 -286 N ATOM 1091 N PRO A 139 22.424 16.686 -17.465 1.00 27.39 N ANISOU 1091 N PRO A 139 2753 3603 4049 425 -64 -39 N ATOM 1092 CA PRO A 139 21.171 17.237 -18.001 1.00 30.98 C ANISOU 1092 CA PRO A 139 3265 4031 4474 404 -64 -47 C ATOM 1093 C PRO A 139 20.184 17.639 -16.908 1.00 28.09 C ANISOU 1093 C PRO A 139 2943 3623 4106 395 -93 -14 C ATOM 1094 O PRO A 139 19.481 18.626 -17.064 1.00 28.18 O ANISOU 1094 O PRO A 139 2999 3629 4079 363 -99 -6 O ATOM 1095 CB PRO A 139 20.583 16.070 -18.790 1.00 30.28 C ANISOU 1095 CB PRO A 139 3177 3915 4414 442 -47 -86 C ATOM 1096 CG PRO A 139 21.742 15.192 -19.102 1.00 40.13 C ANISOU 1096 CG PRO A 139 4364 5189 5693 474 -29 -110 C ATOM 1097 CD PRO A 139 22.710 15.338 -17.979 1.00 27.09 C ANISOU 1097 CD PRO A 139 2679 3557 4056 475 -47 -74 C ATOM 1098 N ILE A 140 20.125 16.876 -15.822 1.00 23.51 N ANISOU 1098 N ILE A 140 2351 3015 3566 422 -112 5 N ATOM 1099 CA ILE A 140 19.148 17.134 -14.769 1.00 30.88 C ANISOU 1099 CA ILE A 140 3322 3914 4498 415 -140 32 C ATOM 1100 C ILE A 140 19.447 18.457 -14.108 1.00 28.88 C ANISOU 1100 C ILE A 140 3081 3684 4208 372 -155 62 C ATOM 1101 O ILE A 140 18.571 19.291 -13.899 1.00 21.59 O ANISOU 1101 O ILE A 140 2203 2745 3256 349 -167 71 O ATOM 1102 CB ILE A 140 19.175 16.024 -13.719 1.00 34.03 C ANISOU 1102 CB ILE A 140 3699 4286 4947 449 -158 50 C ATOM 1103 CG1 ILE A 140 18.600 14.740 -14.320 1.00 41.77 C ANISOU 1103 CG1 ILE A 140 4680 5228 5963 488 -147 21 C ATOM 1104 CG2 ILE A 140 18.420 16.455 -12.456 1.00 37.32 C ANISOU 1104 CG2 ILE A 140 4144 4683 5355 433 -189 84 C ATOM 1105 CD1 ILE A 140 18.972 13.502 -13.560 1.00 49.04 C ANISOU 1105 CD1 ILE A 140 5569 6125 6939 527 -160 34 C ATOM 1106 N SER A 141 20.716 18.643 -13.785 1.00 23.38 N ANISOU 1106 N SER A 141 2344 3028 3513 363 -154 75 N ATOM 1107 CA SER A 141 21.180 19.861 -13.176 1.00 23.30 C ANISOU 1107 CA SER A 141 2340 3044 3468 319 -166 101 C ATOM 1108 C SER A 141 20.946 21.077 -14.070 1.00 22.63 C ANISOU 1108 C SER A 141 2293 2970 3335 278 -155 91 C ATOM 1109 O SER A 141 20.475 22.113 -13.592 1.00 19.45 O ANISOU 1109 O SER A 141 1930 2557 2905 247 -171 108 O ATOM 1110 CB SER A 141 22.682 19.728 -12.844 1.00 32.37 C ANISOU 1110 CB SER A 141 3431 4243 4627 316 -162 113 C ATOM 1111 OG SER A 141 23.145 20.854 -12.125 1.00 48.71 O ANISOU 1111 OG SER A 141 5505 6338 6665 271 -175 139 O ATOM 1112 N GLN A 142 21.291 20.954 -15.352 1.00 21.24 N ANISOU 1112 N GLN A 142 2105 2817 3149 279 -129 65 N ATOM 1113 CA GLN A 142 21.161 22.072 -16.304 1.00 25.88 C ANISOU 1113 CA GLN A 142 2726 3419 3690 238 -119 59 C ATOM 1114 C GLN A 142 19.700 22.459 -16.508 1.00 23.07 C ANISOU 1114 C GLN A 142 2428 3018 3318 238 -128 56 C ATOM 1115 O GLN A 142 19.345 23.633 -16.601 1.00 19.82 O ANISOU 1115 O GLN A 142 2058 2601 2871 203 -137 68 O ATOM 1116 CB GLN A 142 21.775 21.689 -17.662 1.00 25.49 C ANISOU 1116 CB GLN A 142 2645 3406 3632 241 -88 28 C ATOM 1117 CG GLN A 142 23.296 21.525 -17.636 1.00 25.99 C ANISOU 1117 CG GLN A 142 2648 3527 3700 235 -77 29 C ATOM 1118 CD GLN A 142 24.014 22.850 -17.453 1.00 33.73 C ANISOU 1118 CD GLN A 142 3635 4544 4638 177 -83 53 C ATOM 1119 OE1 GLN A 142 23.426 23.925 -17.622 1.00 25.43 O ANISOU 1119 OE1 GLN A 142 2634 3475 3551 140 -91 65 O ATOM 1120 NE2 GLN A 142 25.291 22.785 -17.119 1.00 34.33 N ANISOU 1120 NE2 GLN A 142 3659 4670 4716 168 -79 61 N ATOM 1121 N VAL A 143 18.844 21.458 -16.614 1.00 15.80 N ANISOU 1121 N VAL A 143 1513 2066 2426 277 -126 39 N ATOM 1122 CA VAL A 143 17.427 21.753 -16.761 1.00 16.55 C ANISOU 1122 CA VAL A 143 1660 2123 2506 279 -136 35 C ATOM 1123 C VAL A 143 16.819 22.424 -15.522 1.00 19.84 C ANISOU 1123 C VAL A 143 2108 2514 2917 268 -165 62 C ATOM 1124 O VAL A 143 16.164 23.464 -15.636 1.00 17.94 O ANISOU 1124 O VAL A 143 1912 2261 2644 246 -174 68 O ATOM 1125 CB VAL A 143 16.631 20.514 -17.164 1.00 19.61 C ANISOU 1125 CB VAL A 143 2044 2485 2921 319 -127 10 C ATOM 1126 CG1 VAL A 143 15.097 20.782 -17.014 1.00 17.05 C ANISOU 1126 CG1 VAL A 143 1771 2124 2583 323 -142 11 C ATOM 1127 CG2 VAL A 143 16.993 20.125 -18.595 1.00 17.62 C ANISOU 1127 CG2 VAL A 143 1773 2258 2662 323 -97 -23 C ATOM 1128 N LEU A 144 17.044 21.849 -14.343 1.00 18.14 N ANISOU 1128 N LEU A 144 1870 2292 2731 284 -180 77 N ATOM 1129 CA LEU A 144 16.508 22.468 -13.138 1.00 18.81 C ANISOU 1129 CA LEU A 144 1980 2360 2808 271 -207 99 C ATOM 1130 C LEU A 144 17.070 23.864 -12.959 1.00 21.43 C ANISOU 1130 C LEU A 144 2327 2709 3105 227 -213 114 C ATOM 1131 O LEU A 144 16.348 24.790 -12.604 1.00 16.85 O ANISOU 1131 O LEU A 144 1790 2111 2503 211 -228 120 O ATOM 1132 CB LEU A 144 16.846 21.626 -11.904 1.00 21.25 C ANISOU 1132 CB LEU A 144 2254 2669 3152 290 -222 117 C ATOM 1133 CG LEU A 144 15.770 20.731 -11.279 1.00 35.77 C ANISOU 1133 CG LEU A 144 4101 4474 5015 319 -236 118 C ATOM 1134 CD1 LEU A 144 14.514 20.580 -12.113 1.00 28.37 C ANISOU 1134 CD1 LEU A 144 3201 3511 4068 332 -229 95 C ATOM 1135 CD2 LEU A 144 16.335 19.383 -10.873 1.00 31.74 C ANISOU 1135 CD2 LEU A 144 3546 3964 4551 349 -236 125 C ATOM 1136 N LYS A 145 18.374 24.007 -13.187 1.00 20.27 N ANISOU 1136 N LYS A 145 2146 2600 2955 208 -201 119 N ATOM 1137 CA LYS A 145 19.021 25.298 -13.013 1.00 23.69 C ANISOU 1137 CA LYS A 145 2593 3053 3356 160 -206 134 C ATOM 1138 C LYS A 145 18.332 26.344 -13.895 1.00 21.64 C ANISOU 1138 C LYS A 145 2387 2775 3060 138 -204 127 C ATOM 1139 O LYS A 145 17.989 27.430 -13.426 1.00 19.45 O ANISOU 1139 O LYS A 145 2149 2480 2761 112 -221 139 O ATOM 1140 CB LYS A 145 20.511 25.211 -13.350 1.00 24.99 C ANISOU 1140 CB LYS A 145 2708 3268 3518 143 -190 136 C ATOM 1141 CG LYS A 145 21.255 26.535 -13.171 1.00 38.30 C ANISOU 1141 CG LYS A 145 4406 4977 5168 86 -195 153 C ATOM 1142 CD LYS A 145 22.639 26.475 -13.812 1.00 41.61 C ANISOU 1142 CD LYS A 145 4779 5453 5578 66 -175 151 C ATOM 1143 CE LYS A 145 22.527 26.494 -15.323 1.00 52.31 C ANISOU 1143 CE LYS A 145 6144 6817 6916 63 -153 131 C ATOM 1144 NZ LYS A 145 23.752 26.001 -16.004 1.00 55.04 N ANISOU 1144 NZ LYS A 145 6432 7221 7261 61 -130 120 N ATOM 1145 N SER A 146 18.126 26.008 -15.176 1.00 17.17 N ANISOU 1145 N SER A 146 1822 2213 2488 149 -184 109 N ATOM 1146 CA SER A 146 17.492 26.919 -16.142 1.00 20.28 C ANISOU 1146 CA SER A 146 2263 2594 2848 130 -182 105 C ATOM 1147 C SER A 146 16.108 27.365 -15.715 1.00 19.24 C ANISOU 1147 C SER A 146 2182 2417 2710 142 -202 107 C ATOM 1148 O SER A 146 15.756 28.554 -15.757 1.00 21.83 O ANISOU 1148 O SER A 146 2555 2727 3011 117 -214 118 O ATOM 1149 CB SER A 146 17.343 26.194 -17.508 1.00 22.89 C ANISOU 1149 CB SER A 146 2580 2939 3178 148 -157 82 C ATOM 1150 OG SER A 146 18.614 25.838 -18.005 1.00 36.98 O ANISOU 1150 OG SER A 146 4316 4769 4964 136 -136 76 O ATOM 1151 N VAL A 147 15.298 26.390 -15.335 1.00 19.06 N ANISOU 1151 N VAL A 147 2152 2375 2713 182 -206 97 N ATOM 1152 CA VAL A 147 13.902 26.660 -15.002 1.00 14.49 C ANISOU 1152 CA VAL A 147 1616 1762 2128 199 -223 94 C ATOM 1153 C VAL A 147 13.788 27.475 -13.717 1.00 17.92 C ANISOU 1153 C VAL A 147 2069 2182 2557 184 -248 110 C ATOM 1154 O VAL A 147 12.968 28.383 -13.625 1.00 19.66 O ANISOU 1154 O VAL A 147 2334 2378 2757 179 -262 111 O ATOM 1155 CB VAL A 147 13.147 25.320 -14.845 1.00 19.10 C ANISOU 1155 CB VAL A 147 2182 2335 2741 241 -221 79 C ATOM 1156 CG1 VAL A 147 11.764 25.528 -14.268 1.00 21.36 C ANISOU 1156 CG1 VAL A 147 2503 2593 3020 257 -240 78 C ATOM 1157 CG2 VAL A 147 13.073 24.628 -16.234 1.00 15.56 C ANISOU 1157 CG2 VAL A 147 1723 1897 2292 254 -195 58 C ATOM 1158 N VAL A 148 14.600 27.121 -12.722 1.00 18.58 N ANISOU 1158 N VAL A 148 2117 2281 2660 179 -253 121 N ATOM 1159 CA VAL A 148 14.576 27.807 -11.426 1.00 18.98 C ANISOU 1159 CA VAL A 148 2181 2326 2706 162 -276 134 C ATOM 1160 C VAL A 148 15.110 29.228 -11.586 1.00 19.86 C ANISOU 1160 C VAL A 148 2321 2436 2787 118 -280 142 C ATOM 1161 O VAL A 148 14.541 30.193 -11.065 1.00 21.60 O ANISOU 1161 O VAL A 148 2582 2634 2993 107 -298 143 O ATOM 1162 CB VAL A 148 15.389 27.036 -10.355 1.00 23.46 C ANISOU 1162 CB VAL A 148 2698 2917 3299 164 -281 146 C ATOM 1163 CG1 VAL A 148 15.634 27.920 -9.078 1.00 22.98 C ANISOU 1163 CG1 VAL A 148 2646 2860 3227 135 -302 160 C ATOM 1164 CG2 VAL A 148 14.672 25.742 -10.000 1.00 23.89 C ANISOU 1164 CG2 VAL A 148 2734 2962 3383 205 -284 141 C ATOM 1165 N HIS A 149 16.200 29.357 -12.325 1.00 19.80 N ANISOU 1165 N HIS A 149 2295 2456 2773 93 -263 147 N ATOM 1166 CA HIS A 149 16.758 30.685 -12.582 1.00 24.83 C ANISOU 1166 CA HIS A 149 2962 3094 3380 45 -266 158 C ATOM 1167 C HIS A 149 15.733 31.596 -13.250 1.00 27.66 C ANISOU 1167 C HIS A 149 3380 3414 3715 45 -273 154 C ATOM 1168 O HIS A 149 15.603 32.773 -12.904 1.00 21.87 O ANISOU 1168 O HIS A 149 2688 2657 2964 19 -289 161 O ATOM 1169 CB HIS A 149 18.007 30.579 -13.475 1.00 29.12 C ANISOU 1169 CB HIS A 149 3472 3679 3915 19 -244 162 C ATOM 1170 CG HIS A 149 18.832 31.829 -13.502 1.00 51.57 C ANISOU 1170 CG HIS A 149 6334 6531 6728 -38 -248 177 C ATOM 1171 ND1 HIS A 149 18.570 32.879 -14.358 1.00 61.81 N ANISOU 1171 ND1 HIS A 149 7680 7808 7996 -66 -250 182 N ATOM 1172 CD2 HIS A 149 19.912 32.200 -12.771 1.00 63.16 C ANISOU 1172 CD2 HIS A 149 7780 8027 8191 -76 -252 189 C ATOM 1173 CE1 HIS A 149 19.453 33.841 -14.156 1.00 63.59 C ANISOU 1173 CE1 HIS A 149 7915 8045 8201 -120 -255 197 C ATOM 1174 NE2 HIS A 149 20.281 33.453 -13.200 1.00 60.30 N ANISOU 1174 NE2 HIS A 149 7454 7659 7797 -127 -255 200 N ATOM 1175 N ASN A 150 14.996 31.046 -14.209 1.00 18.29 N ANISOU 1175 N ASN A 150 2199 2221 2530 74 -263 142 N ATOM 1176 CA ASN A 150 13.966 31.824 -14.918 1.00 25.79 C ANISOU 1176 CA ASN A 150 3202 3138 3457 79 -270 140 C ATOM 1177 C ASN A 150 12.779 32.238 -14.010 1.00 28.05 C ANISOU 1177 C ASN A 150 3524 3387 3746 102 -294 135 C ATOM 1178 O ASN A 150 12.240 33.345 -14.114 1.00 23.78 O ANISOU 1178 O ASN A 150 3034 2816 3187 93 -308 138 O ATOM 1179 CB ASN A 150 13.476 31.032 -16.134 1.00 21.02 C ANISOU 1179 CB ASN A 150 2589 2545 2854 105 -251 128 C ATOM 1180 CG ASN A 150 12.428 31.777 -16.945 1.00 25.02 C ANISOU 1180 CG ASN A 150 3146 3024 3335 111 -259 129 C ATOM 1181 OD1 ASN A 150 12.674 32.888 -17.411 1.00 23.75 O ANISOU 1181 OD1 ASN A 150 3020 2855 3151 78 -264 144 O ATOM 1182 ND2 ASN A 150 11.262 31.153 -17.143 1.00 27.16 N ANISOU 1182 ND2 ASN A 150 3421 3285 3611 151 -259 114 N ATOM 1183 N LEU A 151 12.378 31.346 -13.120 1.00 17.78 N ANISOU 1183 N LEU A 151 2198 2091 2468 132 -299 126 N ATOM 1184 CA LEU A 151 11.329 31.649 -12.146 1.00 21.75 C ANISOU 1184 CA LEU A 151 2724 2568 2971 151 -320 118 C ATOM 1185 C LEU A 151 11.761 32.789 -11.217 1.00 23.09 C ANISOU 1185 C LEU A 151 2915 2726 3131 119 -338 125 C ATOM 1186 O LEU A 151 10.977 33.710 -10.920 1.00 22.00 O ANISOU 1186 O LEU A 151 2822 2558 2981 124 -355 118 O ATOM 1187 CB LEU A 151 11.010 30.408 -11.307 1.00 20.11 C ANISOU 1187 CB LEU A 151 2478 2375 2788 180 -322 112 C ATOM 1188 CG LEU A 151 10.106 29.377 -12.005 1.00 28.55 C ANISOU 1188 CG LEU A 151 3539 3444 3865 217 -312 99 C ATOM 1189 CD1 LEU A 151 10.263 27.988 -11.421 1.00 19.60 C ANISOU 1189 CD1 LEU A 151 2358 2327 2761 236 -308 98 C ATOM 1190 CD2 LEU A 151 8.648 29.813 -11.948 1.00 26.65 C ANISOU 1190 CD2 LEU A 151 3336 3180 3608 241 -327 87 C ATOM 1191 N VAL A 152 13.003 32.718 -10.761 1.00 22.24 N ANISOU 1191 N VAL A 152 2777 2644 3030 88 -333 136 N ATOM 1192 CA VAL A 152 13.571 33.731 -9.852 1.00 23.85 C ANISOU 1192 CA VAL A 152 2996 2843 3224 51 -347 142 C ATOM 1193 C VAL A 152 13.734 35.076 -10.582 1.00 24.99 C ANISOU 1193 C VAL A 152 3191 2960 3344 18 -350 148 C ATOM 1194 O VAL A 152 13.463 36.139 -10.021 1.00 28.20 O ANISOU 1194 O VAL A 152 3638 3336 3740 3 -368 144 O ATOM 1195 CB VAL A 152 14.928 33.256 -9.269 1.00 25.30 C ANISOU 1195 CB VAL A 152 3127 3069 3418 23 -339 154 C ATOM 1196 CG1 VAL A 152 15.670 34.411 -8.537 1.00 26.31 C ANISOU 1196 CG1 VAL A 152 3272 3196 3529 -26 -351 160 C ATOM 1197 CG2 VAL A 152 14.727 32.059 -8.329 1.00 27.43 C ANISOU 1197 CG2 VAL A 152 3351 3359 3712 54 -343 152 C ATOM 1198 N TYR A 153 14.172 35.019 -11.840 1.00 23.28 N ANISOU 1198 N TYR A 153 2973 2753 3118 6 -334 157 N ATOM 1199 CA TYR A 153 14.271 36.209 -12.683 1.00 25.04 C ANISOU 1199 CA TYR A 153 3245 2951 3317 -25 -337 168 C ATOM 1200 C TYR A 153 12.928 36.942 -12.767 1.00 30.03 C ANISOU 1200 C TYR A 153 3934 3533 3942 2 -356 160 C ATOM 1201 O TYR A 153 12.853 38.160 -12.575 1.00 28.77 O ANISOU 1201 O TYR A 153 3823 3337 3771 -20 -372 164 O ATOM 1202 CB TYR A 153 14.733 35.822 -14.084 1.00 22.02 C ANISOU 1202 CB TYR A 153 2848 2595 2926 -34 -316 177 C ATOM 1203 CG TYR A 153 14.998 37.004 -15.001 1.00 27.25 C ANISOU 1203 CG TYR A 153 3555 3238 3560 -75 -319 195 C ATOM 1204 CD1 TYR A 153 16.269 37.530 -15.127 1.00 33.20 C ANISOU 1204 CD1 TYR A 153 4302 4015 4299 -133 -313 211 C ATOM 1205 CD2 TYR A 153 13.974 37.583 -15.733 1.00 30.28 C ANISOU 1205 CD2 TYR A 153 3988 3584 3931 -58 -328 198 C ATOM 1206 CE1 TYR A 153 16.524 38.604 -15.968 1.00 40.08 C ANISOU 1206 CE1 TYR A 153 5215 4869 5143 -175 -317 230 C ATOM 1207 CE2 TYR A 153 14.216 38.664 -16.574 1.00 35.61 C ANISOU 1207 CE2 TYR A 153 4707 4240 4581 -96 -334 219 C ATOM 1208 CZ TYR A 153 15.491 39.167 -16.681 1.00 39.48 C ANISOU 1208 CZ TYR A 153 5192 4752 5058 -157 -328 235 C ATOM 1209 OH TYR A 153 15.743 40.234 -17.515 1.00 45.30 O ANISOU 1209 OH TYR A 153 5972 5470 5768 -200 -335 259 O ATOM 1210 N ARG A 154 11.868 36.191 -13.050 1.00 20.01 N ANISOU 1210 N ARG A 154 2659 2262 2681 51 -353 148 N ATOM 1211 CA ARG A 154 10.516 36.744 -13.080 1.00 24.40 C ANISOU 1211 CA ARG A 154 3261 2779 3231 85 -371 138 C ATOM 1212 C ARG A 154 10.027 37.205 -11.709 1.00 31.03 C ANISOU 1212 C ARG A 154 4115 3598 4077 95 -392 122 C ATOM 1213 O ARG A 154 9.330 38.224 -11.592 1.00 30.42 O ANISOU 1213 O ARG A 154 4087 3480 3991 104 -410 116 O ATOM 1214 CB ARG A 154 9.537 35.728 -13.681 1.00 31.63 C ANISOU 1214 CB ARG A 154 4159 3708 4151 131 -361 128 C ATOM 1215 CG ARG A 154 9.633 35.623 -15.192 1.00 36.47 C ANISOU 1215 CG ARG A 154 4777 4331 4750 126 -346 139 C ATOM 1216 CD ARG A 154 8.602 34.619 -15.700 1.00 41.26 C ANISOU 1216 CD ARG A 154 5367 4951 5360 170 -337 125 C ATOM 1217 NE ARG A 154 9.076 33.284 -15.443 1.00 41.03 N ANISOU 1217 NE ARG A 154 5282 4956 5351 177 -320 116 N ATOM 1218 CZ ARG A 154 8.315 32.206 -15.303 1.00 29.83 C ANISOU 1218 CZ ARG A 154 3839 3548 3945 214 -315 100 C ATOM 1219 NH1 ARG A 154 6.998 32.264 -15.389 1.00 28.27 N ANISOU 1219 NH1 ARG A 154 3666 3338 3739 246 -326 90 N ATOM 1220 NH2 ARG A 154 8.907 31.062 -15.070 1.00 27.75 N ANISOU 1220 NH2 ARG A 154 3529 3312 3704 216 -301 96 N ATOM 1221 N LEU A 155 10.386 36.463 -10.670 1.00 28.31 N ANISOU 1221 N LEU A 155 3727 3283 3748 95 -390 116 N ATOM 1222 CA LEU A 155 10.028 36.864 -9.309 1.00 26.15 C ANISOU 1222 CA LEU A 155 3461 2999 3477 99 -408 100 C ATOM 1223 C LEU A 155 10.497 38.298 -9.061 1.00 28.84 C ANISOU 1223 C LEU A 155 3846 3306 3805 60 -422 102 C ATOM 1224 O LEU A 155 9.747 39.135 -8.559 1.00 32.15 O ANISOU 1224 O LEU A 155 4304 3691 4220 73 -440 86 O ATOM 1225 CB LEU A 155 10.643 35.908 -8.276 1.00 28.85 C ANISOU 1225 CB LEU A 155 3746 3382 3834 92 -404 100 C ATOM 1226 CG LEU A 155 10.753 36.395 -6.819 1.00 32.06 C ANISOU 1226 CG LEU A 155 4151 3792 4240 75 -420 89 C ATOM 1227 CD1 LEU A 155 9.391 36.437 -6.163 1.00 30.36 C ANISOU 1227 CD1 LEU A 155 3950 3564 4022 115 -436 66 C ATOM 1228 CD2 LEU A 155 11.697 35.509 -6.009 1.00 31.92 C ANISOU 1228 CD2 LEU A 155 4074 3820 4234 57 -414 100 C ATOM 1229 N PHE A 156 11.736 38.586 -9.438 1.00 24.13 N ANISOU 1229 N PHE A 156 3244 2720 3203 12 -412 121 N ATOM 1230 CA PHE A 156 12.272 39.931 -9.259 1.00 32.90 C ANISOU 1230 CA PHE A 156 4399 3799 4302 -33 -424 125 C ATOM 1231 C PHE A 156 11.737 40.949 -10.268 1.00 39.80 C ANISOU 1231 C PHE A 156 5337 4623 5164 -30 -433 133 C ATOM 1232 O PHE A 156 11.273 42.017 -9.879 1.00 35.69 O ANISOU 1232 O PHE A 156 4866 4055 4640 -31 -453 122 O ATOM 1233 CB PHE A 156 13.798 39.906 -9.272 1.00 30.49 C ANISOU 1233 CB PHE A 156 4065 3528 3992 -89 -411 143 C ATOM 1234 CG PHE A 156 14.399 39.389 -7.992 1.00 32.62 C ANISOU 1234 CG PHE A 156 4287 3837 4271 -102 -411 137 C ATOM 1235 CD1 PHE A 156 14.187 40.062 -6.788 1.00 32.83 C ANISOU 1235 CD1 PHE A 156 4332 3848 4296 -112 -429 119 C ATOM 1236 CD2 PHE A 156 15.169 38.237 -7.986 1.00 31.09 C ANISOU 1236 CD2 PHE A 156 4029 3697 4086 -103 -394 148 C ATOM 1237 CE1 PHE A 156 14.734 39.582 -5.593 1.00 28.06 C ANISOU 1237 CE1 PHE A 156 3680 3285 3696 -126 -429 115 C ATOM 1238 CE2 PHE A 156 15.727 37.759 -6.808 1.00 32.69 C ANISOU 1238 CE2 PHE A 156 4187 3938 4297 -114 -395 146 C ATOM 1239 CZ PHE A 156 15.508 38.436 -5.604 1.00 28.42 C ANISOU 1239 CZ PHE A 156 3663 3385 3751 -128 -413 131 C ATOM 1240 N SER A 157 11.780 40.608 -11.553 1.00 31.57 N ANISOU 1240 N SER A 157 4291 3589 4115 -27 -419 150 N ATOM 1241 CA SER A 157 11.456 41.567 -12.610 1.00 30.99 C ANISOU 1241 CA SER A 157 4274 3474 4027 -34 -428 166 C ATOM 1242 C SER A 157 9.969 41.924 -12.667 1.00 39.92 C ANISOU 1242 C SER A 157 5444 4563 5159 21 -445 152 C ATOM 1243 O SER A 157 9.596 43.008 -13.109 1.00 38.25 O ANISOU 1243 O SER A 157 5290 4302 4940 18 -462 160 O ATOM 1244 CB SER A 157 11.932 41.052 -13.977 1.00 35.46 C ANISOU 1244 CB SER A 157 4821 4072 4582 -48 -407 188 C ATOM 1245 OG SER A 157 11.227 39.882 -14.362 1.00 30.63 O ANISOU 1245 OG SER A 157 4173 3488 3977 0 -395 178 O ATOM 1246 N GLU A 158 9.126 40.982 -12.268 1.00 34.94 N ANISOU 1246 N GLU A 158 4524 4076 4676 814 -179 -282 N ATOM 1247 CA GLU A 158 7.695 41.199 -12.204 1.00 37.50 C ANISOU 1247 CA GLU A 158 4820 4430 4997 850 -171 -277 C ATOM 1248 C GLU A 158 7.150 41.479 -10.803 1.00 39.44 C ANISOU 1248 C GLU A 158 5068 4685 5233 882 -153 -292 C ATOM 1249 O GLU A 158 5.942 41.602 -10.614 1.00 40.71 O ANISOU 1249 O GLU A 158 5205 4874 5391 913 -144 -289 O ATOM 1250 CB GLU A 158 6.967 40.053 -12.904 1.00 38.69 C ANISOU 1250 CB GLU A 158 4926 4623 5152 832 -169 -264 C ATOM 1251 CG GLU A 158 7.484 39.873 -14.317 1.00 44.71 C ANISOU 1251 CG GLU A 158 5687 5378 5922 807 -187 -252 C ATOM 1252 CD GLU A 158 6.821 38.733 -15.050 1.00 58.27 C ANISOU 1252 CD GLU A 158 7359 7136 7644 788 -188 -242 C ATOM 1253 OE1 GLU A 158 5.722 38.307 -14.625 1.00 56.39 O ANISOU 1253 OE1 GLU A 158 7087 6932 7406 802 -175 -243 O ATOM 1254 OE2 GLU A 158 7.404 38.267 -16.054 1.00 62.95 O ANISOU 1254 OE2 GLU A 158 7950 7728 8242 759 -201 -236 O ATOM 1255 N ASN A 159 8.038 41.554 -9.817 1.00 40.19 N ANISOU 1255 N ASN A 159 5190 4759 5321 875 -149 -308 N ATOM 1256 CA ASN A 159 7.620 41.798 -8.435 1.00 40.79 C ANISOU 1256 CA ASN A 159 5269 4845 5385 906 -134 -324 C ATOM 1257 C ASN A 159 6.473 40.891 -7.968 1.00 43.79 C ANISOU 1257 C ASN A 159 5605 5275 5758 916 -114 -315 C ATOM 1258 O ASN A 159 5.473 41.361 -7.411 1.00 41.79 O ANISOU 1258 O ASN A 159 5342 5040 5498 956 -103 -318 O ATOM 1259 CB ASN A 159 7.261 43.278 -8.231 1.00 48.34 C ANISOU 1259 CB ASN A 159 6250 5777 6341 952 -138 -335 C ATOM 1260 CG ASN A 159 8.454 44.196 -8.417 1.00 62.58 C ANISOU 1260 CG ASN A 159 8098 7527 8152 944 -155 -346 C ATOM 1261 OD1 ASN A 159 8.538 44.934 -9.402 1.00 68.67 O ANISOU 1261 OD1 ASN A 159 8882 8273 8936 947 -168 -337 O ATOM 1262 ND2 ASN A 159 9.387 44.155 -7.469 1.00 70.80 N ANISOU 1262 ND2 ASN A 159 9163 8551 9187 933 -153 -366 N ATOM 1263 N TRP A 160 6.633 39.585 -8.187 1.00 33.05 N ANISOU 1263 N TRP A 160 4219 3936 4401 878 -108 -304 N ATOM 1264 CA TRP A 160 5.641 38.597 -7.777 1.00 32.32 C ANISOU 1264 CA TRP A 160 4083 3890 4309 880 -88 -294 C ATOM 1265 C TRP A 160 5.457 38.558 -6.275 1.00 33.21 C ANISOU 1265 C TRP A 160 4198 4017 4405 904 -67 -304 C ATOM 1266 O TRP A 160 6.415 38.718 -5.523 1.00 30.10 O ANISOU 1266 O TRP A 160 3833 3602 4001 900 -67 -318 O ATOM 1267 CB TRP A 160 6.094 37.192 -8.195 1.00 28.09 C ANISOU 1267 CB TRP A 160 3524 3366 3782 831 -87 -284 C ATOM 1268 CG TRP A 160 5.922 36.853 -9.649 1.00 32.44 C ANISOU 1268 CG TRP A 160 4056 3921 4348 808 -103 -272 C ATOM 1269 CD1 TRP A 160 5.250 37.570 -10.590 1.00 37.02 C ANISOU 1269 CD1 TRP A 160 4630 4503 4934 829 -115 -266 C ATOM 1270 CD2 TRP A 160 6.419 35.678 -10.310 1.00 29.08 C ANISOU 1270 CD2 TRP A 160 3614 3502 3934 762 -107 -264 C ATOM 1271 NE1 TRP A 160 5.298 36.915 -11.802 1.00 35.32 N ANISOU 1271 NE1 TRP A 160 4395 4296 4730 799 -128 -257 N ATOM 1272 CE2 TRP A 160 6.014 35.753 -11.655 1.00 34.34 C ANISOU 1272 CE2 TRP A 160 4263 4174 4611 758 -124 -256 C ATOM 1273 CE3 TRP A 160 7.170 34.571 -9.886 1.00 31.86 C ANISOU 1273 CE3 TRP A 160 3962 3856 4288 726 -98 -263 C ATOM 1274 CZ2 TRP A 160 6.334 34.764 -12.592 1.00 33.20 C ANISOU 1274 CZ2 TRP A 160 4099 4037 4478 719 -133 -250 C ATOM 1275 CZ3 TRP A 160 7.490 33.589 -10.810 1.00 28.79 C ANISOU 1275 CZ3 TRP A 160 3555 3471 3912 686 -107 -256 C ATOM 1276 CH2 TRP A 160 7.072 33.694 -12.155 1.00 31.02 C ANISOU 1276 CH2 TRP A 160 3821 3760 4205 683 -125 -250 C ATOM 1277 N THR A 161 4.234 38.279 -5.845 1.00 32.96 N ANISOU 1277 N THR A 161 4130 4022 4371 929 -49 -296 N ATOM 1278 CA THR A 161 3.989 37.881 -4.462 1.00 36.98 C ANISOU 1278 CA THR A 161 4630 4555 4865 947 -25 -299 C ATOM 1279 C THR A 161 4.493 36.455 -4.252 1.00 40.27 C ANISOU 1279 C THR A 161 5028 4986 5287 905 -13 -288 C ATOM 1280 O THR A 161 4.745 35.733 -5.215 1.00 31.70 O ANISOU 1280 O THR A 161 3928 3898 4218 866 -22 -278 O ATOM 1281 CB THR A 161 2.514 37.915 -4.134 1.00 39.32 C ANISOU 1281 CB THR A 161 4891 4890 5160 983 -8 -289 C ATOM 1282 OG1 THR A 161 1.822 36.976 -4.971 1.00 35.56 O ANISOU 1282 OG1 THR A 161 4369 4438 4702 959 -5 -270 O ATOM 1283 CG2 THR A 161 1.962 39.335 -4.372 1.00 38.12 C ANISOU 1283 CG2 THR A 161 4757 4725 5003 1027 -19 -299 C ATOM 1284 N GLU A 162 4.672 36.058 -3.000 1.00 36.24 N ANISOU 1284 N GLU A 162 4518 4489 4761 914 7 -290 N ATOM 1285 CA GLU A 162 5.069 34.688 -2.707 1.00 38.15 C ANISOU 1285 CA GLU A 162 4740 4747 5008 879 22 -277 C ATOM 1286 C GLU A 162 4.080 33.680 -3.306 1.00 39.44 C ANISOU 1286 C GLU A 162 4852 4940 5193 861 33 -255 C ATOM 1287 O GLU A 162 4.487 32.692 -3.913 1.00 32.04 O ANISOU 1287 O GLU A 162 3900 4001 4273 819 30 -246 O ATOM 1288 CB GLU A 162 5.225 34.488 -1.200 1.00 44.07 C ANISOU 1288 CB GLU A 162 5495 5514 5736 901 46 -281 C ATOM 1289 CG GLU A 162 6.281 35.403 -0.589 1.00 46.50 C ANISOU 1289 CG GLU A 162 5852 5792 6022 915 33 -306 C ATOM 1290 CD GLU A 162 6.808 34.888 0.740 1.00 58.43 C ANISOU 1290 CD GLU A 162 7369 7318 7512 922 53 -309 C ATOM 1291 OE1 GLU A 162 7.927 35.294 1.124 1.00 56.72 O ANISOU 1291 OE1 GLU A 162 7190 7078 7282 919 41 -329 O ATOM 1292 OE2 GLU A 162 6.112 34.072 1.391 1.00 58.87 O ANISOU 1292 OE2 GLU A 162 7391 7411 7565 931 80 -291 O ATOM 1293 N LYS A 163 2.784 33.945 -3.169 1.00 29.39 N ANISOU 1293 N LYS A 163 3550 3694 3921 894 44 -249 N ATOM 1294 CA LYS A 163 1.784 33.041 -3.732 1.00 30.96 C ANISOU 1294 CA LYS A 163 3697 3922 4143 879 54 -230 C ATOM 1295 C LYS A 163 1.959 32.852 -5.246 1.00 32.82 C ANISOU 1295 C LYS A 163 3927 4143 4400 845 28 -229 C ATOM 1296 O LYS A 163 1.819 31.740 -5.765 1.00 30.74 O ANISOU 1296 O LYS A 163 3630 3892 4158 810 32 -218 O ATOM 1297 CB LYS A 163 0.364 33.536 -3.436 1.00 37.20 C ANISOU 1297 CB LYS A 163 4460 4743 4932 923 66 -224 C ATOM 1298 CG LYS A 163 -0.721 32.673 -4.075 1.00 45.64 C ANISOU 1298 CG LYS A 163 5473 5842 6027 908 74 -207 C ATOM 1299 CD LYS A 163 -2.096 33.311 -3.966 1.00 62.46 C ANISOU 1299 CD LYS A 163 7578 7999 8154 952 81 -203 C ATOM 1300 CE LYS A 163 -3.160 32.456 -4.640 1.00 63.96 C ANISOU 1300 CE LYS A 163 7710 8219 8372 936 87 -188 C ATOM 1301 NZ LYS A 163 -3.165 31.056 -4.119 1.00 70.43 N ANISOU 1301 NZ LYS A 163 8496 9056 9209 906 111 -172 N ATOM 1302 N THR A 164 2.222 33.947 -5.954 1.00 31.34 N ANISOU 1302 N THR A 164 3769 3931 4207 857 4 -241 N ATOM 1303 CA THR A 164 2.402 33.892 -7.408 1.00 31.27 C ANISOU 1303 CA THR A 164 3757 3909 4213 830 -21 -240 C ATOM 1304 C THR A 164 3.642 33.069 -7.751 1.00 23.10 C ANISOU 1304 C THR A 164 2736 2855 3186 782 -29 -241 C ATOM 1305 O THR A 164 3.621 32.254 -8.680 1.00 21.72 O ANISOU 1305 O THR A 164 2536 2686 3029 749 -37 -235 O ATOM 1306 CB THR A 164 2.505 35.314 -8.013 1.00 34.49 C ANISOU 1306 CB THR A 164 4199 4294 4614 856 -43 -250 C ATOM 1307 OG1 THR A 164 1.253 35.996 -7.828 1.00 37.36 O ANISOU 1307 OG1 THR A 164 4545 4678 4973 901 -36 -249 O ATOM 1308 CG2 THR A 164 2.821 35.257 -9.499 1.00 29.53 C ANISOU 1308 CG2 THR A 164 3569 3652 3997 830 -68 -248 C ATOM 1309 N PHE A 165 4.717 33.258 -6.989 1.00 22.66 N ANISOU 1309 N PHE A 165 2718 2777 3115 778 -26 -249 N ATOM 1310 CA PHE A 165 5.941 32.514 -7.269 1.00 29.99 C ANISOU 1310 CA PHE A 165 3660 3685 4048 734 -33 -250 C ATOM 1311 C PHE A 165 5.681 31.027 -7.060 1.00 29.77 C ANISOU 1311 C PHE A 165 3593 3683 4036 705 -15 -236 C ATOM 1312 O PHE A 165 6.076 30.186 -7.877 1.00 24.60 O ANISOU 1312 O PHE A 165 2926 3025 3398 666 -23 -232 O ATOM 1313 CB PHE A 165 7.099 33.006 -6.390 1.00 22.59 C ANISOU 1313 CB PHE A 165 2769 2723 3092 738 -34 -263 C ATOM 1314 CG PHE A 165 8.342 32.142 -6.456 1.00 25.12 C ANISOU 1314 CG PHE A 165 3102 3028 3414 695 -36 -262 C ATOM 1315 CD1 PHE A 165 9.309 32.360 -7.435 1.00 24.04 C ANISOU 1315 CD1 PHE A 165 2990 2862 3282 668 -60 -267 C ATOM 1316 CD2 PHE A 165 8.568 31.146 -5.510 1.00 26.44 C ANISOU 1316 CD2 PHE A 165 3257 3210 3578 683 -14 -256 C ATOM 1317 CE1 PHE A 165 10.455 31.581 -7.493 1.00 22.74 C ANISOU 1317 CE1 PHE A 165 2836 2685 3119 630 -63 -267 C ATOM 1318 CE2 PHE A 165 9.702 30.347 -5.571 1.00 26.16 C ANISOU 1318 CE2 PHE A 165 3232 3162 3545 645 -16 -254 C ATOM 1319 CZ PHE A 165 10.655 30.568 -6.553 1.00 25.92 C ANISOU 1319 CZ PHE A 165 3226 3102 3518 618 -41 -261 C ATOM 1320 N ILE A 166 5.007 30.707 -5.964 1.00 27.66 N ANISOU 1320 N ILE A 166 3305 3441 3764 726 12 -229 N ATOM 1321 CA ILE A 166 4.730 29.318 -5.633 1.00 29.29 C ANISOU 1321 CA ILE A 166 3472 3669 3987 702 34 -213 C ATOM 1322 C ILE A 166 3.851 28.682 -6.715 1.00 30.61 C ANISOU 1322 C ILE A 166 3595 3853 4183 683 28 -205 C ATOM 1323 O ILE A 166 4.109 27.565 -7.158 1.00 26.48 O ANISOU 1323 O ILE A 166 3051 3331 3680 644 29 -199 O ATOM 1324 CB ILE A 166 4.082 29.192 -4.245 1.00 31.36 C ANISOU 1324 CB ILE A 166 3720 3958 4239 733 66 -204 C ATOM 1325 CG1 ILE A 166 5.092 29.547 -3.142 1.00 27.92 C ANISOU 1325 CG1 ILE A 166 3325 3509 3775 746 73 -213 C ATOM 1326 CG2 ILE A 166 3.601 27.780 -4.010 1.00 28.14 C ANISOU 1326 CG2 ILE A 166 3265 3573 3853 710 90 -184 C ATOM 1327 CD1 ILE A 166 4.421 29.768 -1.772 1.00 28.52 C ANISOU 1327 CD1 ILE A 166 3393 3612 3832 789 100 -207 C ATOM 1328 N GLU A 167 2.827 29.400 -7.164 1.00 25.81 N ANISOU 1328 N GLU A 167 2972 3259 3576 711 21 -207 N ATOM 1329 CA GLU A 167 1.944 28.848 -8.205 1.00 26.66 C ANISOU 1329 CA GLU A 167 3034 3385 3709 695 13 -202 C ATOM 1330 C GLU A 167 2.674 28.554 -9.508 1.00 26.50 C ANISOU 1330 C GLU A 167 3022 3346 3700 659 -14 -209 C ATOM 1331 O GLU A 167 2.481 27.490 -10.112 1.00 24.14 O ANISOU 1331 O GLU A 167 2688 3057 3425 626 -15 -206 O ATOM 1332 CB GLU A 167 0.742 29.765 -8.462 1.00 28.37 C ANISOU 1332 CB GLU A 167 3236 3621 3923 736 9 -204 C ATOM 1333 CG GLU A 167 -0.185 29.858 -7.273 1.00 41.50 C ANISOU 1333 CG GLU A 167 4879 5310 5580 770 38 -194 C ATOM 1334 CD GLU A 167 -1.308 30.865 -7.477 1.00 53.60 C ANISOU 1334 CD GLU A 167 6401 6859 7106 814 33 -196 C ATOM 1335 OE1 GLU A 167 -1.136 31.813 -8.280 1.00 55.55 O ANISOU 1335 OE1 GLU A 167 6673 7090 7345 826 8 -207 O ATOM 1336 OE2 GLU A 167 -2.360 30.702 -6.829 1.00 62.89 O ANISOU 1336 OE2 GLU A 167 7543 8065 8285 837 55 -186 O ATOM 1337 N ASN A 168 3.525 29.480 -9.936 1.00 24.92 N ANISOU 1337 N ASN A 168 2868 3119 3483 663 -35 -220 N ATOM 1338 CA ASN A 168 4.285 29.283 -11.180 1.00 22.34 C ANISOU 1338 CA ASN A 168 2551 2775 3163 632 -61 -225 C ATOM 1339 C ASN A 168 5.362 28.198 -11.040 1.00 20.60 C ANISOU 1339 C ASN A 168 2337 2540 2949 589 -57 -224 C ATOM 1340 O ASN A 168 5.550 27.368 -11.936 1.00 21.53 O ANISOU 1340 O ASN A 168 2436 2660 3084 556 -68 -224 O ATOM 1341 CB ASN A 168 4.895 30.612 -11.624 1.00 21.01 C ANISOU 1341 CB ASN A 168 2428 2580 2976 650 -82 -233 C ATOM 1342 CG ASN A 168 3.857 31.519 -12.267 1.00 31.29 C ANISOU 1342 CG ASN A 168 3718 3895 4276 685 -93 -233 C ATOM 1343 OD1 ASN A 168 3.165 31.107 -13.192 1.00 35.37 O ANISOU 1343 OD1 ASN A 168 4199 4432 4807 677 -103 -231 O ATOM 1344 ND2 ASN A 168 3.706 32.722 -11.744 1.00 31.16 N ANISOU 1344 ND2 ASN A 168 3728 3867 4243 723 -92 -236 N ATOM 1345 N TYR A 169 6.054 28.211 -9.908 1.00 21.04 N ANISOU 1345 N TYR A 169 2419 2585 2991 592 -41 -223 N ATOM 1346 CA TYR A 169 7.032 27.168 -9.580 1.00 19.61 C ANISOU 1346 CA TYR A 169 2243 2393 2814 555 -33 -220 C ATOM 1347 C TYR A 169 6.367 25.778 -9.641 1.00 25.11 C ANISOU 1347 C TYR A 169 2889 3113 3540 531 -17 -209 C ATOM 1348 O TYR A 169 6.875 24.851 -10.281 1.00 20.44 O ANISOU 1348 O TYR A 169 2287 2514 2964 493 -25 -209 O ATOM 1349 CB TYR A 169 7.602 27.445 -8.186 1.00 20.99 C ANISOU 1349 CB TYR A 169 2447 2561 2969 572 -15 -219 C ATOM 1350 CG TYR A 169 8.656 26.461 -7.685 1.00 18.81 C ANISOU 1350 CG TYR A 169 2179 2274 2692 540 -4 -215 C ATOM 1351 CD1 TYR A 169 8.285 25.234 -7.148 1.00 17.75 C ANISOU 1351 CD1 TYR A 169 2010 2159 2574 525 21 -201 C ATOM 1352 CD2 TYR A 169 10.018 26.788 -7.699 1.00 17.28 C ANISOU 1352 CD2 TYR A 169 2030 2053 2483 527 -18 -225 C ATOM 1353 CE1 TYR A 169 9.235 24.342 -6.666 1.00 21.06 C ANISOU 1353 CE1 TYR A 169 2438 2570 2993 499 32 -196 C ATOM 1354 CE2 TYR A 169 10.973 25.893 -7.215 1.00 21.93 C ANISOU 1354 CE2 TYR A 169 2626 2634 3070 500 -8 -220 C ATOM 1355 CZ TYR A 169 10.574 24.677 -6.701 1.00 18.68 C ANISOU 1355 CZ TYR A 169 2180 2243 2674 487 17 -206 C ATOM 1356 OH TYR A 169 11.512 23.784 -6.213 1.00 20.23 O ANISOU 1356 OH TYR A 169 2384 2432 2869 462 29 -200 O ATOM 1357 N ASP A 170 5.217 25.642 -8.988 1.00 23.22 N ANISOU 1357 N ASP A 170 2616 2899 3307 553 4 -200 N ATOM 1358 CA ASP A 170 4.510 24.356 -8.977 1.00 23.60 C ANISOU 1358 CA ASP A 170 2613 2968 3386 531 22 -189 C ATOM 1359 C ASP A 170 4.194 23.859 -10.392 1.00 21.98 C ANISOU 1359 C ASP A 170 2379 2767 3206 505 -1 -196 C ATOM 1360 O ASP A 170 4.440 22.695 -10.705 1.00 22.92 O ANISOU 1360 O ASP A 170 2476 2884 3349 468 2 -194 O ATOM 1361 CB ASP A 170 3.223 24.450 -8.141 1.00 27.63 C ANISOU 1361 CB ASP A 170 3090 3507 3900 563 47 -177 C ATOM 1362 CG ASP A 170 3.495 24.473 -6.642 1.00 26.29 C ANISOU 1362 CG ASP A 170 2937 3340 3712 583 76 -167 C ATOM 1363 OD1 ASP A 170 4.661 24.306 -6.233 1.00 24.60 O ANISOU 1363 OD1 ASP A 170 2756 3106 3484 569 77 -168 O ATOM 1364 OD2 ASP A 170 2.535 24.640 -5.863 1.00 27.81 O ANISOU 1364 OD2 ASP A 170 3108 3556 3903 614 98 -157 O ATOM 1365 N LYS A 171 3.641 24.733 -11.238 1.00 21.48 N ANISOU 1365 N LYS A 171 2314 2709 3137 525 -22 -205 N ATOM 1366 CA LYS A 171 3.262 24.341 -12.595 1.00 26.13 C ANISOU 1366 CA LYS A 171 2874 3307 3746 505 -45 -213 C ATOM 1367 C LYS A 171 4.475 23.941 -13.421 1.00 21.55 C ANISOU 1367 C LYS A 171 2318 2705 3166 470 -66 -222 C ATOM 1368 O LYS A 171 4.463 22.922 -14.086 1.00 22.85 O ANISOU 1368 O LYS A 171 2454 2874 3354 439 -72 -226 O ATOM 1369 CB LYS A 171 2.521 25.479 -13.323 1.00 22.36 C ANISOU 1369 CB LYS A 171 2397 2842 3257 539 -64 -220 C ATOM 1370 CG LYS A 171 1.128 25.788 -12.757 1.00 31.54 C ANISOU 1370 CG LYS A 171 3527 4033 4425 572 -47 -213 C ATOM 1371 CD LYS A 171 0.388 26.802 -13.630 1.00 33.36 C ANISOU 1371 CD LYS A 171 3754 4276 4647 603 -68 -220 C ATOM 1372 CE LYS A 171 -0.444 27.784 -12.813 1.00 47.12 C ANISOU 1372 CE LYS A 171 5499 6031 6373 650 -53 -214 C ATOM 1373 NZ LYS A 171 -1.347 27.104 -11.830 1.00 61.65 N ANISOU 1373 NZ LYS A 171 7300 7896 8230 655 -23 -202 N ATOM 1374 N GLU A 172 5.516 24.761 -13.385 1.00 19.70 N ANISOU 1374 N GLU A 172 2134 2445 2904 477 -77 -225 N ATOM 1375 CA GLU A 172 6.673 24.535 -14.252 1.00 18.34 C ANISOU 1375 CA GLU A 172 1986 2253 2730 448 -98 -232 C ATOM 1376 C GLU A 172 7.535 23.369 -13.760 1.00 20.07 C ANISOU 1376 C GLU A 172 2207 2461 2960 412 -85 -228 C ATOM 1377 O GLU A 172 8.115 22.636 -14.569 1.00 19.73 O ANISOU 1377 O GLU A 172 2159 2410 2927 379 -98 -234 O ATOM 1378 CB GLU A 172 7.462 25.850 -14.409 1.00 20.10 C ANISOU 1378 CB GLU A 172 2261 2453 2924 467 -114 -235 C ATOM 1379 CG GLU A 172 6.598 26.909 -15.166 1.00 20.49 C ANISOU 1379 CG GLU A 172 2304 2513 2966 500 -130 -238 C ATOM 1380 CD GLU A 172 7.194 28.319 -15.181 1.00 29.02 C ANISOU 1380 CD GLU A 172 3433 3570 4022 525 -142 -239 C ATOM 1381 OE1 GLU A 172 8.427 28.456 -15.064 1.00 30.65 O ANISOU 1381 OE1 GLU A 172 3677 3749 4218 510 -147 -241 O ATOM 1382 OE2 GLU A 172 6.411 29.287 -15.331 1.00 28.02 O ANISOU 1382 OE2 GLU A 172 3306 3452 3889 561 -146 -239 O ATOM 1383 N ILE A 173 7.600 23.176 -12.440 1.00 21.65 N ANISOU 1383 N ILE A 173 2412 2660 3155 419 -57 -218 N ATOM 1384 CA ILE A 173 8.333 22.030 -11.889 1.00 22.21 C ANISOU 1384 CA ILE A 173 2481 2721 3236 388 -41 -212 C ATOM 1385 C ILE A 173 7.540 20.732 -12.147 1.00 18.19 C ANISOU 1385 C ILE A 173 1918 2229 2764 364 -30 -208 C ATOM 1386 O ILE A 173 8.118 19.660 -12.384 1.00 21.16 O ANISOU 1386 O ILE A 173 2285 2596 3157 329 -29 -208 O ATOM 1387 CB ILE A 173 8.696 22.232 -10.366 1.00 29.21 C ANISOU 1387 CB ILE A 173 3391 3604 4104 405 -14 -202 C ATOM 1388 CG1 ILE A 173 9.714 23.369 -10.190 1.00 23.03 C ANISOU 1388 CG1 ILE A 173 2663 2798 3289 420 -28 -210 C ATOM 1389 CG2 ILE A 173 9.233 20.955 -9.737 1.00 26.27 C ANISOU 1389 CG2 ILE A 173 3009 3228 3745 377 7 -191 C ATOM 1390 CD1 ILE A 173 11.080 23.147 -10.840 1.00 33.72 C ANISOU 1390 CD1 ILE A 173 4047 4128 4638 389 -47 -217 C ATOM 1391 N LYS A 174 6.214 20.823 -12.145 1.00 20.06 N ANISOU 1391 N LYS A 174 2116 2490 3015 383 -23 -205 N ATOM 1392 CA LYS A 174 5.389 19.652 -12.454 1.00 20.34 C ANISOU 1392 CA LYS A 174 2098 2541 3090 360 -15 -204 C ATOM 1393 C LYS A 174 5.563 19.265 -13.918 1.00 20.78 C ANISOU 1393 C LYS A 174 2141 2595 3160 334 -46 -221 C ATOM 1394 O LYS A 174 5.660 18.081 -14.264 1.00 21.38 O ANISOU 1394 O LYS A 174 2190 2668 3265 300 -45 -224 O ATOM 1395 CB LYS A 174 3.903 19.921 -12.125 1.00 21.92 C ANISOU 1395 CB LYS A 174 2258 2769 3301 388 -2 -198 C ATOM 1396 CG LYS A 174 2.963 18.746 -12.416 1.00 36.71 C ANISOU 1396 CG LYS A 174 4070 4658 5219 365 7 -196 C ATOM 1397 CD LYS A 174 1.517 19.118 -12.046 1.00 55.82 C ANISOU 1397 CD LYS A 174 6454 7108 7649 396 21 -189 C ATOM 1398 CE LYS A 174 0.627 17.889 -11.842 1.00 69.11 C ANISOU 1398 CE LYS A 174 8076 8804 9377 375 43 -180 C ATOM 1399 NZ LYS A 174 0.151 17.292 -13.125 1.00 76.85 N ANISOU 1399 NZ LYS A 174 9017 9793 10390 350 19 -199 N ATOM 1400 N LEU A 175 5.624 20.269 -14.786 1.00 19.52 N ANISOU 1400 N LEU A 175 2001 2435 2979 351 -73 -232 N ATOM 1401 CA LEU A 175 5.895 20.027 -16.193 1.00 19.14 C ANISOU 1401 CA LEU A 175 1947 2387 2938 331 -104 -248 C ATOM 1402 C LEU A 175 7.235 19.334 -16.345 1.00 21.90 C ANISOU 1402 C LEU A 175 2322 2713 3287 297 -108 -250 C ATOM 1403 O LEU A 175 7.338 18.339 -17.057 1.00 23.54 O ANISOU 1403 O LEU A 175 2505 2922 3518 267 -118 -260 O ATOM 1404 CB LEU A 175 5.869 21.348 -16.992 1.00 21.26 C ANISOU 1404 CB LEU A 175 2241 2659 3179 360 -130 -255 C ATOM 1405 CG LEU A 175 5.904 21.233 -18.518 1.00 30.57 C ANISOU 1405 CG LEU A 175 3407 3846 4361 349 -162 -270 C ATOM 1406 CD1 LEU A 175 5.247 22.459 -19.143 1.00 30.11 C ANISOU 1406 CD1 LEU A 175 3354 3804 4285 386 -179 -273 C ATOM 1407 CD2 LEU A 175 7.336 21.043 -19.042 1.00 20.67 C ANISOU 1407 CD2 LEU A 175 2190 2569 3095 324 -177 -274 C ATOM 1408 N VAL A 176 8.256 19.864 -15.682 1.00 20.50 N ANISOU 1408 N VAL A 176 2191 2514 3082 303 -102 -243 N ATOM 1409 CA VAL A 176 9.585 19.255 -15.717 1.00 18.46 C ANISOU 1409 CA VAL A 176 1959 2234 2821 273 -105 -243 C ATOM 1410 C VAL A 176 9.611 17.840 -15.123 1.00 20.52 C ANISOU 1410 C VAL A 176 2193 2493 3110 244 -81 -236 C ATOM 1411 O VAL A 176 10.183 16.937 -15.705 1.00 21.48 O ANISOU 1411 O VAL A 176 2308 2606 3247 212 -90 -243 O ATOM 1412 CB VAL A 176 10.627 20.111 -14.981 1.00 23.64 C ANISOU 1412 CB VAL A 176 2669 2869 3444 286 -101 -237 C ATOM 1413 CG1 VAL A 176 11.942 19.335 -14.850 1.00 23.55 C ANISOU 1413 CG1 VAL A 176 2679 2837 3431 254 -98 -236 C ATOM 1414 CG2 VAL A 176 10.859 21.394 -15.734 1.00 25.55 C ANISOU 1414 CG2 VAL A 176 2941 3106 3662 307 -126 -244 C ATOM 1415 N THR A 177 8.987 17.628 -13.971 1.00 19.81 N ANISOU 1415 N THR A 177 2086 2411 3029 256 -51 -222 N ATOM 1416 CA THR A 177 9.158 16.337 -13.309 1.00 20.32 C ANISOU 1416 CA THR A 177 2131 2471 3120 230 -26 -211 C ATOM 1417 C THR A 177 8.373 15.231 -14.014 1.00 20.57 C ANISOU 1417 C THR A 177 2108 2511 3194 205 -28 -218 C ATOM 1418 O THR A 177 8.876 14.112 -14.192 1.00 21.11 O ANISOU 1418 O THR A 177 2167 2569 3286 172 -25 -220 O ATOM 1419 CB THR A 177 8.781 16.395 -11.815 1.00 24.23 C ANISOU 1419 CB THR A 177 2624 2973 3611 251 10 -191 C ATOM 1420 OG1 THR A 177 7.445 16.842 -11.686 1.00 25.89 O ANISOU 1420 OG1 THR A 177 2803 3205 3828 277 16 -188 O ATOM 1421 CG2 THR A 177 9.668 17.383 -11.101 1.00 22.41 C ANISOU 1421 CG2 THR A 177 2446 2731 3338 273 11 -188 C ATOM 1422 N GLU A 178 7.132 15.524 -14.392 1.00 18.21 N ANISOU 1422 N GLU A 178 1774 2234 2909 221 -34 -224 N ATOM 1423 CA GLU A 178 6.314 14.513 -15.060 1.00 19.51 C ANISOU 1423 CA GLU A 178 1886 2411 3118 198 -37 -234 C ATOM 1424 C GLU A 178 6.398 14.551 -16.594 1.00 21.98 C ANISOU 1424 C GLU A 178 2192 2727 3432 186 -76 -259 C ATOM 1425 O GLU A 178 5.986 13.606 -17.265 1.00 21.22 O ANISOU 1425 O GLU A 178 2055 2636 3371 162 -84 -273 O ATOM 1426 CB GLU A 178 4.861 14.589 -14.566 1.00 29.43 C ANISOU 1426 CB GLU A 178 3098 3691 4394 218 -19 -225 C ATOM 1427 CG GLU A 178 4.710 14.478 -13.011 1.00 35.15 C ANISOU 1427 CG GLU A 178 3824 4415 5118 231 22 -198 C ATOM 1428 CD GLU A 178 5.161 13.121 -12.399 1.00 32.89 C ANISOU 1428 CD GLU A 178 3523 4112 4860 200 49 -184 C ATOM 1429 OE1 GLU A 178 5.321 12.115 -13.122 1.00 34.20 O ANISOU 1429 OE1 GLU A 178 3666 4269 5059 165 39 -195 O ATOM 1430 OE2 GLU A 178 5.352 13.063 -11.166 1.00 42.26 O ANISOU 1430 OE2 GLU A 178 4722 5297 6039 211 80 -161 O ATOM 1431 N GLY A 179 6.943 15.637 -17.138 1.00 22.40 N ANISOU 1431 N GLY A 179 2402 2647 3463 181 -587 195 N ATOM 1432 CA GLY A 179 7.239 15.741 -18.564 1.00 18.21 C ANISOU 1432 CA GLY A 179 1870 2101 2948 175 -576 222 C ATOM 1433 C GLY A 179 6.239 16.574 -19.356 1.00 21.47 C ANISOU 1433 C GLY A 179 2280 2504 3373 175 -575 224 C ATOM 1434 O GLY A 179 5.040 16.556 -19.101 1.00 18.86 O ANISOU 1434 O GLY A 179 1955 2186 3024 178 -574 212 O ATOM 1435 N LEU A 180 6.747 17.270 -20.356 1.00 17.23 N ANISOU 1435 N LEU A 180 1735 1945 2865 170 -576 241 N ATOM 1436 CA LEU A 180 5.953 18.217 -21.133 1.00 19.38 C ANISOU 1436 CA LEU A 180 2002 2205 3155 171 -577 244 C ATOM 1437 C LEU A 180 4.838 17.499 -21.862 1.00 18.56 C ANISOU 1437 C LEU A 180 1912 2116 3025 169 -559 256 C ATOM 1438 O LEU A 180 3.682 17.958 -21.905 1.00 19.20 O ANISOU 1438 O LEU A 180 1993 2201 3102 172 -560 246 O ATOM 1439 CB LEU A 180 6.874 18.919 -22.135 1.00 25.72 C ANISOU 1439 CB LEU A 180 2795 2983 3993 165 -578 264 C ATOM 1440 CG LEU A 180 6.314 19.881 -23.195 1.00 33.98 C ANISOU 1440 CG LEU A 180 3836 4013 5062 164 -578 275 C ATOM 1441 CD1 LEU A 180 5.218 20.715 -22.625 1.00 56.50 C ANISOU 1441 CD1 LEU A 180 6685 6865 7915 171 -589 251 C ATOM 1442 CD2 LEU A 180 7.450 20.771 -23.672 1.00 41.36 C ANISOU 1442 CD2 LEU A 180 4757 4921 6035 160 -586 286 C ATOM 1443 N LEU A 181 5.165 16.354 -22.446 1.00 19.80 N ANISOU 1443 N LEU A 181 2078 2282 3163 163 -542 277 N ATOM 1444 CA LEU A 181 4.151 15.659 -23.233 1.00 21.94 C ANISOU 1444 CA LEU A 181 2361 2566 3409 160 -525 289 C ATOM 1445 C LEU A 181 3.016 15.147 -22.333 1.00 24.42 C ANISOU 1445 C LEU A 181 2684 2903 3690 164 -524 269 C ATOM 1446 O LEU A 181 1.846 15.237 -22.687 1.00 24.48 O ANISOU 1446 O LEU A 181 2695 2918 3687 165 -519 267 O ATOM 1447 CB LEU A 181 4.776 14.530 -24.084 1.00 17.60 C ANISOU 1447 CB LEU A 181 1821 2020 2847 152 -507 316 C ATOM 1448 CG LEU A 181 5.710 15.059 -25.182 1.00 21.38 C ANISOU 1448 CG LEU A 181 2290 2476 3357 147 -506 339 C ATOM 1449 CD1 LEU A 181 6.441 13.904 -25.901 1.00 24.06 C ANISOU 1449 CD1 LEU A 181 2639 2821 3684 141 -489 364 C ATOM 1450 CD2 LEU A 181 4.951 15.920 -26.208 1.00 29.08 C ANISOU 1450 CD2 LEU A 181 3260 3439 4348 146 -504 348 C ATOM 1451 N ASN A 182 3.357 14.593 -21.176 1.00 20.79 N ANISOU 1451 N ASN A 182 2228 2457 3215 168 -529 254 N ATOM 1452 CA ASN A 182 2.323 14.202 -20.206 1.00 21.54 C ANISOU 1452 CA ASN A 182 2330 2574 3281 173 -530 232 C ATOM 1453 C ASN A 182 1.472 15.390 -19.760 1.00 23.24 C ANISOU 1453 C ASN A 182 2536 2785 3509 179 -545 210 C ATOM 1454 O ASN A 182 0.281 15.240 -19.449 1.00 28.45 O ANISOU 1454 O ASN A 182 3201 3461 4147 183 -542 198 O ATOM 1455 CB ASN A 182 2.964 13.540 -18.980 1.00 24.02 C ANISOU 1455 CB ASN A 182 2647 2900 3579 175 -536 219 C ATOM 1456 CG ASN A 182 3.389 12.102 -19.254 1.00 33.30 C ANISOU 1456 CG ASN A 182 3836 4088 4730 170 -519 237 C ATOM 1457 OD1 ASN A 182 3.210 11.585 -20.358 1.00 29.57 O ANISOU 1457 OD1 ASN A 182 3371 3614 4250 164 -503 260 O ATOM 1458 ND2 ASN A 182 3.936 11.451 -18.249 1.00 39.18 N ANISOU 1458 ND2 ASN A 182 4584 4843 5459 172 -522 228 N ATOM 1459 N TYR A 183 2.089 16.567 -19.718 1.00 25.63 N ANISOU 1459 N TYR A 183 2826 3066 3848 182 -559 205 N ATOM 1460 CA TYR A 183 1.388 17.795 -19.332 1.00 27.63 C ANISOU 1460 CA TYR A 183 3070 3312 4117 189 -574 184 C ATOM 1461 C TYR A 183 0.313 18.180 -20.349 1.00 29.56 C ANISOU 1461 C TYR A 183 3316 3554 4363 188 -566 194 C ATOM 1462 O TYR A 183 -0.776 18.607 -19.990 1.00 25.43 O ANISOU 1462 O TYR A 183 2792 3039 3833 194 -570 177 O ATOM 1463 CB TYR A 183 2.380 18.954 -19.208 1.00 32.18 C ANISOU 1463 CB TYR A 183 3631 3862 4733 190 -591 179 C ATOM 1464 CG TYR A 183 1.942 20.047 -18.252 1.00 38.95 C ANISOU 1464 CG TYR A 183 4479 4715 5603 199 -610 150 C ATOM 1465 CD1 TYR A 183 2.148 19.909 -16.873 1.00 38.21 C ANISOU 1465 CD1 TYR A 183 4386 4634 5500 205 -621 126 C ATOM 1466 CD2 TYR A 183 1.334 21.213 -18.718 1.00 30.15 C ANISOU 1466 CD2 TYR A 183 3357 3586 4511 203 -616 146 C ATOM 1467 CE1 TYR A 183 1.754 20.896 -15.981 1.00 43.51 C ANISOU 1467 CE1 TYR A 183 5049 5301 6182 213 -638 98 C ATOM 1468 CE2 TYR A 183 0.934 22.220 -17.828 1.00 32.60 C ANISOU 1468 CE2 TYR A 183 3661 3893 4835 211 -634 119 C ATOM 1469 CZ TYR A 183 1.145 22.047 -16.459 1.00 43.25 C ANISOU 1469 CZ TYR A 183 5009 5253 6172 216 -645 95 C ATOM 1470 OH TYR A 183 0.762 23.009 -15.549 1.00 35.29 O ANISOU 1470 OH TYR A 183 3994 4242 5175 225 -662 67 O ATOM 1471 N ILE A 184 0.655 18.060 -21.625 1.00 18.18 N ANISOU 1471 N ILE A 184 1874 2101 2931 181 -555 221 N ATOM 1472 CA ILE A 184 -0.189 18.541 -22.717 1.00 20.99 C ANISOU 1472 CA ILE A 184 2230 2451 3295 180 -548 233 C ATOM 1473 C ILE A 184 -1.277 17.581 -23.197 1.00 21.08 C ANISOU 1473 C ILE A 184 2254 2484 3272 177 -530 242 C ATOM 1474 O ILE A 184 -2.328 18.007 -23.678 1.00 21.70 O ANISOU 1474 O ILE A 184 2332 2565 3349 179 -528 241 O ATOM 1475 CB ILE A 184 0.696 18.907 -23.927 1.00 34.25 C ANISOU 1475 CB ILE A 184 3903 4107 5002 173 -544 259 C ATOM 1476 CG1 ILE A 184 1.745 19.920 -23.499 1.00 48.69 C ANISOU 1476 CG1 ILE A 184 5719 5914 6867 176 -562 251 C ATOM 1477 CG2 ILE A 184 -0.144 19.487 -25.055 1.00 51.45 C ANISOU 1477 CG2 ILE A 184 6079 6278 7190 173 -538 271 C ATOM 1478 CD1 ILE A 184 2.526 20.483 -24.662 1.00 66.40 C ANISOU 1478 CD1 ILE A 184 7954 8134 9141 170 -560 274 C ATOM 1479 N THR A 185 -0.996 16.283 -23.122 1.00 22.10 N ANISOU 1479 N THR A 185 2394 2629 3374 172 -518 251 N ATOM 1480 CA THR A 185 -1.914 15.286 -23.661 1.00 23.13 C ANISOU 1480 CA THR A 185 2538 2779 3472 167 -500 262 C ATOM 1481 C THR A 185 -2.062 14.121 -22.702 1.00 23.74 C ANISOU 1481 C THR A 185 2626 2879 3513 167 -495 251 C ATOM 1482 O THR A 185 -1.144 13.808 -21.951 1.00 23.65 O ANISOU 1482 O THR A 185 2615 2869 3503 168 -501 245 O ATOM 1483 CB THR A 185 -1.471 14.739 -25.054 1.00 28.56 C ANISOU 1483 CB THR A 185 3230 3459 4161 158 -484 293 C ATOM 1484 OG1 THR A 185 -2.452 13.816 -25.539 1.00 25.59 O ANISOU 1484 OG1 THR A 185 2866 3102 3753 154 -467 302 O ATOM 1485 CG2 THR A 185 -0.129 13.999 -24.976 1.00 19.67 C ANISOU 1485 CG2 THR A 185 2107 2329 3036 154 -480 305 C ATOM 1486 N ASP A 186 -3.224 13.485 -22.758 1.00 22.29 N ANISOU 1486 N ASP A 186 2453 2717 3299 166 -485 249 N ATOM 1487 CA ASP A 186 -3.481 12.243 -22.036 1.00 28.44 C ANISOU 1487 CA ASP A 186 3244 3519 4041 164 -477 243 C ATOM 1488 C ASP A 186 -2.953 11.028 -22.812 1.00 29.32 C ANISOU 1488 C ASP A 186 3368 3634 4137 155 -459 269 C ATOM 1489 O ASP A 186 -2.868 9.921 -22.276 1.00 26.12 O ANISOU 1489 O ASP A 186 2975 3246 3705 153 -452 267 O ATOM 1490 CB ASP A 186 -4.995 12.086 -21.799 1.00 23.50 C ANISOU 1490 CB ASP A 186 2625 2916 3389 166 -473 231 C ATOM 1491 CG ASP A 186 -5.547 13.111 -20.823 1.00 25.21 C ANISOU 1491 CG ASP A 186 2830 3133 3615 176 -490 203 C ATOM 1492 OD1 ASP A 186 -4.760 13.669 -20.044 1.00 30.94 O ANISOU 1492 OD1 ASP A 186 3548 3848 4359 182 -505 190 O ATOM 1493 OD2 ASP A 186 -6.783 13.342 -20.834 1.00 34.16 O ANISOU 1493 OD2 ASP A 186 3965 4279 4736 179 -489 195 O ATOM 1494 N ARG A 187 -2.582 11.222 -24.073 1.00 21.84 N ANISOU 1494 N ARG A 187 2418 2671 3207 150 -452 292 N ATOM 1495 CA ARG A 187 -2.061 10.101 -24.850 1.00 22.45 C ANISOU 1495 CA ARG A 187 2507 2751 3271 142 -435 316 C ATOM 1496 C ARG A 187 -0.745 9.666 -24.256 1.00 28.52 C ANISOU 1496 C ARG A 187 3276 3515 4044 143 -439 316 C ATOM 1497 O ARG A 187 0.029 10.496 -23.807 1.00 30.18 O ANISOU 1497 O ARG A 187 3475 3711 4282 147 -453 308 O ATOM 1498 CB ARG A 187 -1.827 10.493 -26.310 1.00 20.67 C ANISOU 1498 CB ARG A 187 2278 2509 3067 137 -427 340 C ATOM 1499 CG ARG A 187 -3.075 10.736 -27.098 1.00 28.81 C ANISOU 1499 CG ARG A 187 3311 3546 4091 135 -420 345 C ATOM 1500 CD ARG A 187 -2.723 10.999 -28.546 1.00 29.39 C ANISOU 1500 CD ARG A 187 3381 3604 4183 130 -411 371 C ATOM 1501 NE ARG A 187 -3.913 10.993 -29.392 1.00 23.87 N ANISOU 1501 NE ARG A 187 2685 2912 3471 127 -401 378 N ATOM 1502 CZ ARG A 187 -3.883 11.157 -30.710 1.00 29.38 C ANISOU 1502 CZ ARG A 187 3382 3601 4181 121 -392 400 C ATOM 1503 NH1 ARG A 187 -2.721 11.360 -31.336 1.00 26.04 N ANISOU 1503 NH1 ARG A 187 2953 3159 3781 119 -392 417 N ATOM 1504 NH2 ARG A 187 -5.017 11.123 -31.395 1.00 23.79 N ANISOU 1504 NH2 ARG A 187 2677 2903 3460 119 -383 406 N ATOM 1505 N LYS A 188 -0.473 8.368 -24.307 1.00 26.95 N ANISOU 1505 N LYS A 188 3092 3328 3820 138 -425 327 N ATOM 1506 CA LYS A 188 0.685 7.800 -23.628 1.00 40.73 C ANISOU 1506 CA LYS A 188 4838 5072 5564 139 -428 326 C ATOM 1507 C LYS A 188 1.787 7.478 -24.612 1.00 39.16 C ANISOU 1507 C LYS A 188 4641 4860 5379 134 -419 352 C ATOM 1508 O LYS A 188 1.522 7.207 -25.780 1.00 42.61 O ANISOU 1508 O LYS A 188 5082 5294 5812 128 -406 372 O ATOM 1509 CB LYS A 188 0.289 6.543 -22.855 1.00 42.87 C ANISOU 1509 CB LYS A 188 5125 5367 5796 138 -420 319 C ATOM 1510 CG LYS A 188 -0.709 6.809 -21.736 1.00 48.25 C ANISOU 1510 CG LYS A 188 5806 6065 6464 144 -430 293 C ATOM 1511 CD LYS A 188 -0.218 7.912 -20.802 1.00 61.03 C ANISOU 1511 CD LYS A 188 7408 7672 8107 152 -451 272 C ATOM 1512 CE LYS A 188 0.051 7.380 -19.396 1.00 71.55 C ANISOU 1512 CE LYS A 188 8745 9019 9422 156 -458 254 C ATOM 1513 NZ LYS A 188 -1.168 6.783 -18.767 1.00 73.20 N ANISOU 1513 NZ LYS A 188 8964 9253 9597 157 -453 241 N ATOM 1514 N ASN A 189 3.027 7.547 -24.134 1.00 53.06 N ANISOU 1514 N ASN A 189 6395 6611 7154 137 -427 351 N ATOM 1515 CA ASN A 189 4.205 7.277 -24.953 1.00 64.62 C ANISOU 1515 CA ASN A 189 7858 8062 8633 133 -420 374 C ATOM 1516 C ASN A 189 4.078 5.994 -25.773 1.00 64.36 C ANISOU 1516 C ASN A 189 7842 8039 8574 126 -399 395 C ATOM 1517 O ASN A 189 4.199 6.021 -26.998 1.00 71.33 O ANISOU 1517 O ASN A 189 8725 8913 9466 121 -389 416 O ATOM 1518 CB ASN A 189 5.460 7.213 -24.075 1.00 64.50 C ANISOU 1518 CB ASN A 189 7838 8043 8628 137 -431 368 C ATOM 1519 CG ASN A 189 6.736 7.480 -24.858 1.00 69.64 C ANISOU 1519 CG ASN A 189 8480 8675 9306 134 -430 388 C ATOM 1520 OD1 ASN A 189 7.808 7.668 -24.275 1.00 72.90 O ANISOU 1520 OD1 ASN A 189 8885 9081 9733 137 -440 384 O ATOM 1521 ND2 ASN A 189 6.623 7.516 -26.188 1.00 61.92 N ANISOU 1521 ND2 ASN A 189 7503 7689 8335 129 -418 409 N TER 1522 ASN A 189 ATOM 1523 O5' DA U 1 48.642 55.187 2.584 1.00 57.83 O ANISOU 1523 O5' DA U 1 8818 6516 6639 -805 -3391 502 O ATOM 1524 C5' DA U 1 48.931 56.032 3.700 1.00 51.85 C ANISOU 1524 C5' DA U 1 8050 5792 5858 -795 -3373 480 C ATOM 1525 C4' DA U 1 48.790 57.490 3.312 1.00 48.17 C ANISOU 1525 C4' DA U 1 7575 5355 5372 -820 -3331 490 C ATOM 1526 O4' DA U 1 49.835 57.826 2.359 1.00 44.41 O ANISOU 1526 O4' DA U 1 7076 4922 4876 -813 -3322 443 O ATOM 1527 C3' DA U 1 47.480 57.879 2.628 1.00 46.14 C ANISOU 1527 C3' DA U 1 7336 5062 5133 -862 -3312 560 C ATOM 1528 O3' DA U 1 47.155 59.201 3.065 1.00 49.77 O ANISOU 1528 O3' DA U 1 7794 5543 5574 -878 -3277 574 O ATOM 1529 C2' DA U 1 47.850 57.836 1.137 1.00 48.51 C ANISOU 1529 C2' DA U 1 7629 5370 5433 -871 -3309 552 C ATOM 1530 C1' DA U 1 49.286 58.360 1.165 1.00 46.88 C ANISOU 1530 C1' DA U 1 7394 5225 5193 -845 -3300 479 C ATOM 1531 N9 DA U 1 50.187 57.923 0.096 1.00 50.37 N ANISOU 1531 N9 DA U 1 7820 5688 5630 -832 -3311 440 N ATOM 1532 C8 DA U 1 50.894 58.708 -0.779 1.00 49.44 C ANISOU 1532 C8 DA U 1 7681 5614 5489 -837 -3288 408 C ATOM 1533 N7 DA U 1 51.642 58.017 -1.617 1.00 47.81 N ANISOU 1533 N7 DA U 1 7463 5419 5283 -822 -3305 374 N ATOM 1534 C5 DA U 1 51.428 56.695 -1.263 1.00 44.12 C ANISOU 1534 C5 DA U 1 7012 4912 4841 -804 -3343 384 C ATOM 1535 C6 DA U 1 51.928 55.463 -1.759 1.00 51.02 C ANISOU 1535 C6 DA U 1 7885 5773 5726 -782 -3376 362 C ATOM 1536 N6 DA U 1 52.798 55.354 -2.769 1.00 50.94 N ANISOU 1536 N6 DA U 1 7856 5794 5705 -773 -3378 322 N ATOM 1537 N1 DA U 1 51.498 54.321 -1.175 1.00 52.91 N ANISOU 1537 N1 DA U 1 8145 5968 5990 -770 -3409 381 N ATOM 1538 C2 DA U 1 50.627 54.409 -0.162 1.00 51.49 C ANISOU 1538 C2 DA U 1 7983 5759 5822 -780 -3408 419 C ATOM 1539 N3 DA U 1 50.086 55.501 0.380 1.00 46.82 N ANISOU 1539 N3 DA U 1 7392 5176 5221 -801 -3378 443 N ATOM 1540 C4 DA U 1 50.530 56.624 -0.212 1.00 44.03 C ANISOU 1540 C4 DA U 1 7021 4866 4844 -811 -3346 424 C ATOM 1541 P DT U 2 45.675 59.797 2.851 1.00 59.39 P ANISOU 1541 P DT U 2 9030 6729 6808 -921 -3253 648 P ATOM 1542 OP1 DT U 2 45.463 60.860 3.855 1.00 61.08 O ANISOU 1542 OP1 DT U 2 9244 6963 7002 -923 -3228 652 O ATOM 1543 OP2 DT U 2 44.730 58.659 2.767 1.00 63.51 O ANISOU 1543 OP2 DT U 2 9570 7197 7365 -933 -3280 694 O ATOM 1544 O5' DT U 2 45.761 60.516 1.432 1.00 58.32 O ANISOU 1544 O5' DT U 2 8888 6608 6664 -944 -3228 654 O ATOM 1545 C5' DT U 2 46.442 61.751 1.337 1.00 45.26 C ANISOU 1545 C5' DT U 2 7218 5002 4976 -943 -3197 621 C ATOM 1546 C4' DT U 2 46.473 62.183 -0.111 1.00 51.64 C ANISOU 1546 C4' DT U 2 8022 5817 5781 -965 -3179 629 C ATOM 1547 O4' DT U 2 47.323 61.267 -0.837 1.00 44.92 O ANISOU 1547 O4' DT U 2 7161 4971 4934 -944 -3205 592 O ATOM 1548 C3' DT U 2 45.120 62.154 -0.828 1.00 53.13 C ANISOU 1548 C3' DT U 2 8229 5962 5996 -1003 -3171 701 C ATOM 1549 O3' DT U 2 44.972 63.328 -1.615 1.00 69.65 O ANISOU 1549 O3' DT U 2 10319 8073 8073 -1028 -3135 714 O ATOM 1550 C2' DT U 2 45.226 60.914 -1.719 1.00 57.12 C ANISOU 1550 C2' DT U 2 8737 6440 6524 -998 -3202 701 C ATOM 1551 C1' DT U 2 46.703 60.980 -2.074 1.00 57.62 C ANISOU 1551 C1' DT U 2 8780 6551 6562 -969 -3205 631 C ATOM 1552 N1 DT U 2 47.341 59.726 -2.551 1.00 58.83 N ANISOU 1552 N1 DT U 2 8929 6696 6727 -945 -3240 602 N ATOM 1553 C2 DT U 2 48.433 59.865 -3.373 1.00 51.29 C ANISOU 1553 C2 DT U 2 7955 5780 5753 -931 -3236 552 C ATOM 1554 O2 DT U 2 48.850 60.951 -3.724 1.00 50.57 O ANISOU 1554 O2 DT U 2 7850 5729 5637 -940 -3206 532 O ATOM 1555 N3 DT U 2 48.999 58.684 -3.766 1.00 45.87 N ANISOU 1555 N3 DT U 2 7266 5086 5077 -908 -3269 525 N ATOM 1556 C4 DT U 2 48.585 57.410 -3.416 1.00 43.39 C ANISOU 1556 C4 DT U 2 6968 4727 4790 -899 -3305 544 C ATOM 1557 O4 DT U 2 49.161 56.407 -3.808 1.00 51.16 O ANISOU 1557 O4 DT U 2 7950 5707 5782 -877 -3334 517 O ATOM 1558 C5 DT U 2 47.443 57.333 -2.536 1.00 50.33 C ANISOU 1558 C5 DT U 2 7868 5567 5690 -916 -3307 596 C ATOM 1559 C7 DT U 2 46.924 55.989 -2.102 1.00 45.30 C ANISOU 1559 C7 DT U 2 7249 4880 5083 -909 -3344 617 C ATOM 1560 C6 DT U 2 46.877 58.485 -2.148 1.00 46.12 C ANISOU 1560 C6 DT U 2 7335 5043 5146 -938 -3274 622 C ATOM 1561 P DG U 3 43.768 64.356 -1.326 1.00 70.97 P ANISOU 1561 P DG U 3 10496 8227 8240 -1061 -3104 770 P ATOM 1562 OP1 DG U 3 43.627 64.490 0.146 1.00 67.16 O ANISOU 1562 OP1 DG U 3 10017 7748 7751 -1047 -3106 767 O ATOM 1563 OP2 DG U 3 42.611 63.945 -2.150 1.00 77.77 O ANISOU 1563 OP2 DG U 3 11370 9048 9133 -1094 -3106 829 O ATOM 1564 O5' DG U 3 44.302 65.730 -1.943 1.00 89.96 O ANISOU 1564 O5' DG U 3 12893 10675 10613 -1071 -3066 749 O ATOM 1565 C5' DG U 3 45.678 65.874 -2.293 1.00 89.53 C ANISOU 1565 C5' DG U 3 12820 10664 10534 -1048 -3067 683 C ATOM 1566 C4' DG U 3 45.820 66.007 -3.796 1.00 88.33 C ANISOU 1566 C4' DG U 3 12665 10516 10381 -1064 -3057 686 C ATOM 1567 O4' DG U 3 46.263 64.756 -4.385 1.00 87.41 O ANISOU 1567 O4' DG U 3 12543 10386 10281 -1047 -3090 668 O ATOM 1568 C3' DG U 3 44.521 66.314 -4.523 1.00 94.25 C ANISOU 1568 C3' DG U 3 13430 11231 11150 -1103 -3040 755 C ATOM 1569 O3' DG U 3 44.860 66.849 -5.776 1.00 97.84 O ANISOU 1569 O3' DG U 3 13880 11705 11592 -1116 -3021 747 O ATOM 1570 C2' DG U 3 43.964 64.912 -4.724 1.00 91.35 C ANISOU 1570 C2' DG U 3 13071 10818 10818 -1102 -3075 783 C ATOM 1571 C1' DG U 3 45.247 64.292 -5.259 1.00 83.46 C ANISOU 1571 C1' DG U 3 12058 9843 9809 -1073 -3095 724 C ATOM 1572 N9 DG U 3 45.254 62.834 -5.310 1.00 65.99 N ANISOU 1572 N9 DG U 3 9851 7599 7623 -1058 -3135 723 N ATOM 1573 C8 DG U 3 44.309 61.959 -4.831 1.00 64.14 C ANISOU 1573 C8 DG U 3 9632 7318 7421 -1066 -3158 765 C ATOM 1574 N7 DG U 3 44.617 60.704 -5.037 1.00 66.84 N ANISOU 1574 N7 DG U 3 9976 7639 7779 -1048 -3193 751 N ATOM 1575 C5 DG U 3 45.845 60.766 -5.692 1.00 55.23 C ANISOU 1575 C5 DG U 3 8489 6208 6287 -1025 -3194 696 C ATOM 1576 C6 DG U 3 46.675 59.731 -6.171 1.00 54.14 C ANISOU 1576 C6 DG U 3 8346 6072 6153 -999 -3224 657 C ATOM 1577 O6 DG U 3 46.471 58.507 -6.102 1.00 61.22 O ANISOU 1577 O6 DG U 3 9253 6933 7073 -990 -3258 666 O ATOM 1578 N1 DG U 3 47.831 60.243 -6.770 1.00 52.18 N ANISOU 1578 N1 DG U 3 8076 5875 5876 -984 -3211 603 N ATOM 1579 C2 DG U 3 48.145 61.574 -6.894 1.00 55.14 C ANISOU 1579 C2 DG U 3 8437 6290 6222 -995 -3174 588 C ATOM 1580 N2 DG U 3 49.301 61.887 -7.506 1.00 56.87 N ANISOU 1580 N2 DG U 3 8634 6559 6417 -980 -3166 532 N ATOM 1581 N3 DG U 3 47.371 62.551 -6.451 1.00 59.14 N ANISOU 1581 N3 DG U 3 8953 6793 6725 -1019 -3146 625 N ATOM 1582 C4 DG U 3 46.246 62.066 -5.867 1.00 55.87 C ANISOU 1582 C4 DG U 3 8558 6331 6339 -1032 -3158 678 C ATOM 1583 P DA U 4 44.542 68.383 -6.114 1.00147.09 P ANISOU 1583 P DA U 4 20120 17962 17807 -1143 -2977 764 P ATOM 1584 OP1 DA U 4 44.930 69.198 -4.942 1.00145.08 O ANISOU 1584 OP1 DA U 4 19861 17736 17526 -1132 -2961 737 O ATOM 1585 OP2 DA U 4 43.161 68.455 -6.644 1.00146.65 O ANISOU 1585 OP2 DA U 4 20078 17867 17774 -1178 -2967 834 O ATOM 1586 O5' DA U 4 45.540 68.706 -7.316 1.00 65.40 O ANISOU 1586 O5' DA U 4 9759 7650 7439 -1141 -2966 722 O ATOM 1587 C5' DA U 4 46.913 68.381 -7.164 1.00 68.49 C ANISOU 1587 C5' DA U 4 10131 8081 7813 -1109 -2981 651 C ATOM 1588 C4' DA U 4 47.440 67.665 -8.396 1.00 80.96 C ANISOU 1588 C4' DA U 4 11700 9663 9398 -1103 -2997 632 C ATOM 1589 O4' DA U 4 47.152 66.243 -8.334 1.00 89.14 O ANISOU 1589 O4' DA U 4 12744 10661 10466 -1089 -3036 647 O ATOM 1590 C3' DA U 4 46.881 68.149 -9.731 1.00 84.46 C ANISOU 1590 C3' DA U 4 12152 10095 9844 -1133 -2976 669 C ATOM 1591 O3' DA U 4 48.002 68.288 -10.608 1.00 86.35 O ANISOU 1591 O3' DA U 4 12373 10376 10062 -1122 -2972 615 O ATOM 1592 C2' DA U 4 45.891 67.042 -10.122 1.00 83.58 C ANISOU 1592 C2' DA U 4 12058 9928 9771 -1142 -3002 722 C ATOM 1593 C1' DA U 4 46.561 65.799 -9.545 1.00 83.11 C ANISOU 1593 C1' DA U 4 11990 9866 9722 -1107 -3041 685 C ATOM 1594 N9 DA U 4 45.717 64.652 -9.185 1.00 75.66 N ANISOU 1594 N9 DA U 4 11063 8871 8814 -1108 -3072 725 N ATOM 1595 C8 DA U 4 44.530 64.656 -8.499 1.00 72.06 C ANISOU 1595 C8 DA U 4 10622 8378 8379 -1128 -3070 779 C ATOM 1596 N7 DA U 4 44.018 63.461 -8.296 1.00 65.94 N ANISOU 1596 N7 DA U 4 9858 7563 7635 -1125 -3103 801 N ATOM 1597 C5 DA U 4 44.940 62.606 -8.880 1.00 66.43 C ANISOU 1597 C5 DA U 4 9912 7632 7695 -1100 -3128 760 C ATOM 1598 C6 DA U 4 44.992 61.200 -9.002 1.00 59.06 C ANISOU 1598 C6 DA U 4 8985 6669 6786 -1084 -3167 757 C ATOM 1599 N6 DA U 4 44.049 60.374 -8.520 1.00 56.01 N ANISOU 1599 N6 DA U 4 8615 6236 6432 -1095 -3190 798 N ATOM 1600 N1 DA U 4 46.062 60.674 -9.644 1.00 55.45 N ANISOU 1600 N1 DA U 4 8516 6232 6318 -1058 -3183 708 N ATOM 1601 C2 DA U 4 47.005 61.488 -10.130 1.00 54.01 C ANISOU 1601 C2 DA U 4 8315 6100 6105 -1050 -3161 665 C ATOM 1602 N3 DA U 4 47.065 62.820 -10.072 1.00 64.70 N ANISOU 1602 N3 DA U 4 9662 7487 7435 -1064 -3124 662 N ATOM 1603 C4 DA U 4 45.994 63.321 -9.427 1.00 70.01 C ANISOU 1603 C4 DA U 4 10349 8135 8118 -1088 -3109 712 C ATOM 1604 P DC U 5 47.797 68.741 -12.136 1.00137.63 P ANISOU 1604 P DC U 5 18870 16870 16552 -1146 -2952 635 P ATOM 1605 OP1 DC U 5 48.553 69.995 -12.346 1.00136.09 O ANISOU 1605 OP1 DC U 5 18662 16727 16320 -1153 -2919 594 O ATOM 1606 OP2 DC U 5 46.350 68.690 -12.440 1.00138.99 O ANISOU 1606 OP2 DC U 5 19068 16991 16752 -1176 -2948 712 O ATOM 1607 O5' DC U 5 48.512 67.577 -12.963 1.00110.58 O ANISOU 1607 O5' DC U 5 15433 13447 13135 -1124 -2983 603 O ATOM 1608 C5' DC U 5 48.411 66.244 -12.476 1.00109.74 C ANISOU 1608 C5' DC U 5 15332 13311 13055 -1103 -3023 606 C ATOM 1609 C4' DC U 5 48.758 65.262 -13.572 1.00103.96 C ANISOU 1609 C4' DC U 5 14597 12570 12334 -1092 -3047 594 C ATOM 1610 O4' DC U 5 48.096 63.998 -13.316 1.00 96.74 O ANISOU 1610 O4' DC U 5 13699 11603 11454 -1086 -3082 628 O ATOM 1611 C3' DC U 5 48.275 65.701 -14.943 1.00104.99 C ANISOU 1611 C3' DC U 5 14737 12691 12465 -1119 -3028 627 C ATOM 1612 O3' DC U 5 49.112 65.140 -15.937 1.00107.91 O ANISOU 1612 O3' DC U 5 15093 13079 12829 -1102 -3043 588 O ATOM 1613 C2' DC U 5 46.862 65.129 -14.994 1.00100.23 C ANISOU 1613 C2' DC U 5 14161 12024 11899 -1141 -3041 700 C ATOM 1614 C1' DC U 5 47.002 63.829 -14.203 1.00 90.50 C ANISOU 1614 C1' DC U 5 12930 10769 10687 -1115 -3081 688 C ATOM 1615 N1 DC U 5 45.786 63.502 -13.398 1.00 69.93 N ANISOU 1615 N1 DC U 5 10343 8115 8110 -1132 -3090 744 N ATOM 1616 C2 DC U 5 45.486 62.171 -13.103 1.00 58.49 C ANISOU 1616 C2 DC U 5 8906 6627 6691 -1121 -3128 756 C ATOM 1617 O2 DC U 5 46.240 61.286 -13.523 1.00 55.64 O ANISOU 1617 O2 DC U 5 8539 6270 6331 -1096 -3155 721 O ATOM 1618 N3 DC U 5 44.377 61.894 -12.363 1.00 64.25 N ANISOU 1618 N3 DC U 5 9650 7316 7446 -1138 -3136 805 N ATOM 1619 C4 DC U 5 43.593 62.892 -11.934 1.00 62.19 C ANISOU 1619 C4 DC U 5 9392 7054 7182 -1165 -3106 841 C ATOM 1620 N4 DC U 5 42.509 62.587 -11.213 1.00 53.97 N ANISOU 1620 N4 DC U 5 8362 5977 6166 -1182 -3114 887 N ATOM 1621 C5 DC U 5 43.885 64.257 -12.230 1.00 61.61 C ANISOU 1621 C5 DC U 5 9310 7020 7080 -1175 -3067 830 C ATOM 1622 C6 DC U 5 44.979 64.511 -12.956 1.00 66.00 C ANISOU 1622 C6 DC U 5 9853 7615 7611 -1158 -3060 782 C ATOM 1623 P DA U 6 49.059 65.695 -17.442 1.00115.56 P ANISOU 1623 P DA U 6 16063 14057 13787 -1122 -3022 599 P ATOM 1624 OP1 DA U 6 50.404 66.202 -17.788 1.00119.61 O ANISOU 1624 OP1 DA U 6 16547 14634 14266 -1107 -3009 527 O ATOM 1625 OP2 DA U 6 47.873 66.576 -17.560 1.00109.87 O ANISOU 1625 OP2 DA U 6 15363 13309 13072 -1160 -2993 662 O ATOM 1626 O5' DA U 6 48.772 64.388 -18.309 1.00 86.00 O ANISOU 1626 O5' DA U 6 12333 10273 10070 -1116 -3056 618 O ATOM 1627 C5' DA U 6 49.369 63.146 -17.953 1.00 83.42 C ANISOU 1627 C5' DA U 6 11999 9942 9754 -1083 -3094 585 C ATOM 1628 C4' DA U 6 48.537 62.018 -18.536 1.00 77.00 C ANISOU 1628 C4' DA U 6 11211 9070 8976 -1089 -3124 631 C ATOM 1629 O4' DA U 6 47.440 61.676 -17.644 1.00 69.45 O ANISOU 1629 O4' DA U 6 10275 8066 8048 -1104 -3135 682 O ATOM 1630 C3' DA U 6 47.891 62.386 -19.866 1.00 78.35 C ANISOU 1630 C3' DA U 6 11395 9225 9151 -1118 -3109 670 C ATOM 1631 O3' DA U 6 47.914 61.267 -20.743 1.00 83.49 O ANISOU 1631 O3' DA U 6 12056 9849 9819 -1108 -3140 672 O ATOM 1632 C2' DA U 6 46.472 62.770 -19.451 1.00 74.53 C ANISOU 1632 C2' DA U 6 10932 8698 8690 -1154 -3096 740 C ATOM 1633 C1' DA U 6 46.222 61.735 -18.362 1.00 68.17 C ANISOU 1633 C1' DA U 6 10134 7860 7908 -1139 -3129 746 C ATOM 1634 N9 DA U 6 45.116 62.068 -17.462 1.00 60.05 N ANISOU 1634 N9 DA U 6 9117 6803 6896 -1164 -3119 796 N ATOM 1635 C8 DA U 6 44.664 63.317 -17.131 1.00 59.25 C ANISOU 1635 C8 DA U 6 9014 6716 6783 -1187 -3082 817 C ATOM 1636 N7 DA U 6 43.650 63.311 -16.295 1.00 62.54 N ANISOU 1636 N7 DA U 6 9440 7101 7219 -1206 -3082 861 N ATOM 1637 C5 DA U 6 43.419 61.959 -16.059 1.00 59.98 C ANISOU 1637 C5 DA U 6 9125 6739 6923 -1195 -3122 868 C ATOM 1638 C6 DA U 6 42.468 61.276 -15.259 1.00 49.99 C ANISOU 1638 C6 DA U 6 7873 5432 5690 -1207 -3142 907 C ATOM 1639 N6 DA U 6 41.536 61.894 -14.512 1.00 46.60 N ANISOU 1639 N6 DA U 6 7445 4993 5267 -1232 -3124 946 N ATOM 1640 N1 DA U 6 42.522 59.930 -15.256 1.00 48.41 N ANISOU 1640 N1 DA U 6 7681 5201 5511 -1193 -3182 902 N ATOM 1641 C2 DA U 6 43.443 59.297 -16.003 1.00 49.19 C ANISOU 1641 C2 DA U 6 7777 5310 5603 -1167 -3201 863 C ATOM 1642 N3 DA U 6 44.379 59.830 -16.792 1.00 52.16 N ANISOU 1642 N3 DA U 6 8140 5727 5951 -1153 -3186 824 N ATOM 1643 C4 DA U 6 44.314 61.177 -16.772 1.00 54.88 C ANISOU 1643 C4 DA U 6 8476 6102 6274 -1169 -3145 829 C ATOM 1644 P DC U 7 47.545 61.451 -22.297 1.00102.80 P ANISOU 1644 P DC U 7 14511 12284 12266 -1129 -3131 697 P ATOM 1645 OP1 DC U 7 48.651 60.884 -23.100 1.00109.05 O ANISOU 1645 OP1 DC U 7 15290 13104 13042 -1100 -3148 644 O ATOM 1646 OP2 DC U 7 47.086 62.847 -22.498 1.00 92.46 O ANISOU 1646 OP2 DC U 7 13201 10989 10941 -1160 -3088 722 O ATOM 1647 O5' DC U 7 46.276 60.516 -22.488 1.00 98.47 O ANISOU 1647 O5' DC U 7 13992 11666 11759 -1150 -3157 759 O ATOM 1648 C5' DC U 7 45.230 60.688 -21.570 1.00 94.23 C ANISOU 1648 C5' DC U 7 13465 11097 11241 -1173 -3152 806 C ATOM 1649 C4' DC U 7 44.553 59.365 -21.321 1.00 86.21 C ANISOU 1649 C4' DC U 7 12468 10026 10263 -1175 -3192 834 C ATOM 1650 O4' DC U 7 44.008 59.377 -19.987 1.00 80.60 O ANISOU 1650 O4' DC U 7 11760 9300 9565 -1181 -3193 854 O ATOM 1651 C3' DC U 7 43.413 59.123 -22.292 1.00 82.44 C ANISOU 1651 C3' DC U 7 12009 9503 9810 -1211 -3197 889 C ATOM 1652 O3' DC U 7 43.579 57.873 -22.927 1.00 83.85 O ANISOU 1652 O3' DC U 7 12200 9654 10006 -1197 -3235 881 O ATOM 1653 C2' DC U 7 42.135 59.175 -21.462 1.00 81.39 C ANISOU 1653 C2' DC U 7 11885 9335 9705 -1243 -3195 944 C ATOM 1654 C1' DC U 7 42.600 59.301 -20.017 1.00 75.40 C ANISOU 1654 C1' DC U 7 11117 8596 8937 -1221 -3193 918 C ATOM 1655 N1 DC U 7 42.029 60.489 -19.319 1.00 59.26 N ANISOU 1655 N1 DC U 7 9066 6566 6885 -1244 -3158 943 N ATOM 1656 C2 DC U 7 41.046 60.253 -18.358 1.00 57.91 C ANISOU 1656 C2 DC U 7 8901 6364 6738 -1262 -3165 981 C ATOM 1657 O2 DC U 7 40.713 59.080 -18.138 1.00 58.06 O ANISOU 1657 O2 DC U 7 8931 6346 6784 -1260 -3200 992 O ATOM 1658 N3 DC U 7 40.496 61.304 -17.704 1.00 58.98 N ANISOU 1658 N3 DC U 7 9030 6512 6866 -1282 -3133 1004 N ATOM 1659 C4 DC U 7 40.892 62.546 -17.980 1.00 57.33 C ANISOU 1659 C4 DC U 7 8812 6343 6628 -1285 -3096 991 C ATOM 1660 N4 DC U 7 40.311 63.541 -17.295 1.00 54.03 N ANISOU 1660 N4 DC U 7 8389 5935 6203 -1304 -3067 1015 N ATOM 1661 C5 DC U 7 41.894 62.808 -18.971 1.00 59.52 C ANISOU 1661 C5 DC U 7 9084 6652 6880 -1267 -3088 952 C ATOM 1662 C6 DC U 7 42.434 61.759 -19.613 1.00 53.43 C ANISOU 1662 C6 DC U 7 8315 5869 6115 -1247 -3119 928 C ATOM 1663 P A DT U 8 42.886 57.596 -24.350 0.50102.68 P ANISOU 1663 P A DT U 8 14601 12008 12407 -1222 -3242 916 P ATOM 1664 OP1A DT U 8 43.456 56.345 -24.898 0.50103.55 O ANISOU 1664 OP1A DT U 8 14720 12101 12524 -1195 -3281 889 O ATOM 1665 OP2A DT U 8 42.947 58.848 -25.138 0.50 99.58 O ANISOU 1665 OP2A DT U 8 14199 11648 11990 -1238 -3202 919 O ATOM 1666 O5'A DT U 8 41.350 57.346 -23.976 0.50 79.38 O ANISOU 1666 O5'A DT U 8 11663 9004 9492 -1265 -3249 982 O ATOM 1667 C5'A DT U 8 40.991 56.246 -23.147 0.50 76.29 C ANISOU 1667 C5'A DT U 8 11283 8576 9128 -1261 -3284 992 C ATOM 1668 C4'A DT U 8 39.564 56.382 -22.647 0.50 72.46 C ANISOU 1668 C4'A DT U 8 10803 8058 8672 -1305 -3280 1050 C ATOM 1669 O4'A DT U 8 39.465 57.503 -21.736 0.50 69.20 O ANISOU 1669 O4'A DT U 8 10374 7674 8243 -1311 -3245 1055 O ATOM 1670 C3'A DT U 8 38.506 56.612 -23.725 0.50 73.64 C ANISOU 1670 C3'A DT U 8 10957 8184 8837 -1348 -3272 1098 C ATOM 1671 O3'A DT U 8 37.556 55.561 -23.629 0.50 77.16 O ANISOU 1671 O3'A DT U 8 11417 8580 9320 -1371 -3306 1133 O ATOM 1672 C2'A DT U 8 37.890 57.969 -23.378 0.50 70.28 C ANISOU 1672 C2'A DT U 8 10517 7782 8402 -1375 -3230 1125 C ATOM 1673 C1'A DT U 8 38.195 58.089 -21.889 0.50 68.22 C ANISOU 1673 C1'A DT U 8 10248 7535 8135 -1357 -3226 1108 C ATOM 1674 N1 A DT U 8 38.275 59.486 -21.387 0.50 67.02 N ANISOU 1674 N1 A DT U 8 10082 7423 7958 -1361 -3183 1107 N ATOM 1675 C2 A DT U 8 37.536 59.842 -20.279 0.50 63.81 C ANISOU 1675 C2 A DT U 8 9669 7013 7562 -1378 -3172 1133 C ATOM 1676 O2 A DT U 8 36.810 59.064 -19.685 0.50 62.57 O ANISOU 1676 O2 A DT U 8 9517 6824 7433 -1391 -3196 1158 O ATOM 1677 N3 A DT U 8 37.683 61.152 -19.896 0.50 64.94 N ANISOU 1677 N3 A DT U 8 9800 7193 7679 -1380 -3132 1129 N ATOM 1678 C4 A DT U 8 38.478 62.114 -20.497 0.50 68.25 C ANISOU 1678 C4 A DT U 8 10214 7652 8066 -1368 -3103 1101 C ATOM 1679 O4 A DT U 8 38.540 63.267 -20.077 0.50 66.34 O ANISOU 1679 O4 A DT U 8 9963 7441 7802 -1372 -3068 1099 O ATOM 1680 C5 A DT U 8 39.223 61.670 -21.652 0.50 71.97 C ANISOU 1680 C5 A DT U 8 10691 8127 8529 -1352 -3116 1074 C ATOM 1681 C7 A DT U 8 40.121 62.623 -22.392 1.00 81.07 C ANISOU 1681 C7 A DT U 8 11835 9323 9645 -1339 -3086 1041 C ATOM 1682 C6 A DT U 8 39.087 60.394 -22.038 0.50 68.03 C ANISOU 1682 C6 A DT U 8 10203 7591 8054 -1348 -3155 1078 C ATOM 1683 P B DA U 8 42.887 57.596 -24.351 0.50102.69 P ANISOU 1683 P B DA U 8 14601 12008 12407 -1222 -3242 916 P ATOM 1684 OP1B DA U 8 43.473 56.355 -24.907 0.50103.55 O ANISOU 1684 OP1B DA U 8 14719 12102 12523 -1195 -3281 889 O ATOM 1685 OP2B DA U 8 42.929 58.854 -25.130 0.50 99.56 O ANISOU 1685 OP2B DA U 8 14195 11644 11987 -1238 -3202 920 O ATOM 1686 O5'B DA U 8 41.358 57.318 -23.974 0.50 79.40 O ANISOU 1686 O5'B DA U 8 11666 9006 9495 -1264 -3250 981 O ATOM 1687 C5'B DA U 8 41.032 56.218 -23.133 0.50 77.00 C ANISOU 1687 C5'B DA U 8 11373 8666 9218 -1259 -3285 990 C ATOM 1688 C4'B DA U 8 39.596 56.317 -22.655 0.50 72.91 C ANISOU 1688 C4'B DA U 8 10859 8113 8728 -1303 -3282 1049 C ATOM 1689 O4'B DA U 8 39.473 57.428 -21.735 0.50 69.20 O ANISOU 1689 O4'B DA U 8 10375 7673 8245 -1310 -3247 1054 O ATOM 1690 C3'B DA U 8 38.565 56.548 -23.757 0.50 73.95 C ANISOU 1690 C3'B DA U 8 10998 8224 8877 -1345 -3274 1095 C ATOM 1691 O3'B DA U 8 37.555 55.562 -23.630 0.50 77.16 O ANISOU 1691 O3'B DA U 8 11416 8580 9320 -1371 -3306 1133 O ATOM 1692 C2'B DA U 8 38.017 57.948 -23.486 0.50 71.38 C ANISOU 1692 C2'B DA U 8 10658 7924 8540 -1372 -3230 1120 C ATOM 1693 C1'B DA U 8 38.269 58.110 -21.993 0.50 68.64 C ANISOU 1693 C1'B DA U 8 10303 7591 8187 -1355 -3225 1106 C ATOM 1694 N9 B DA U 8 38.442 59.496 -21.584 0.50 67.48 N ANISOU 1694 N9 B DA U 8 10141 7486 8014 -1357 -3182 1101 N ATOM 1695 C8 B DA U 8 39.286 60.422 -22.126 0.50 68.31 C ANISOU 1695 C8 B DA U 8 10238 7632 8085 -1343 -3154 1070 C ATOM 1696 N7 B DA U 8 39.223 61.594 -21.540 0.50 70.68 N ANISOU 1696 N7 B DA U 8 10527 7961 8367 -1350 -3118 1073 N ATOM 1697 C5 B DA U 8 38.270 61.425 -20.549 0.50 67.97 C ANISOU 1697 C5 B DA U 8 10184 7595 8047 -1370 -3124 1108 C ATOM 1698 C6 B DA U 8 37.739 62.297 -19.577 0.50 63.70 C ANISOU 1698 C6 B DA U 8 9634 7067 7501 -1384 -3097 1128 C ATOM 1699 N6 B DA U 8 38.105 63.575 -19.433 0.50 66.11 N ANISOU 1699 N6 B DA U 8 9931 7411 7776 -1382 -3059 1115 N ATOM 1700 N1 B DA U 8 36.805 61.794 -18.754 0.50 57.35 N ANISOU 1700 N1 B DA U 8 8831 6235 6725 -1402 -3113 1161 N ATOM 1701 C2 B DA U 8 36.427 60.517 -18.886 0.50 52.78 C ANISOU 1701 C2 B DA U 8 8262 5617 6176 -1406 -3152 1174 C ATOM 1702 N3 B DA U 8 36.849 59.606 -19.755 0.50 60.94 N ANISOU 1702 N3 B DA U 8 9306 6632 7217 -1394 -3179 1158 N ATOM 1703 C4 B DA U 8 37.779 60.133 -20.563 0.50 65.18 C ANISOU 1703 C4 B DA U 8 9841 7199 7726 -1375 -3163 1125 C ATOM 1704 P DG U 9 36.632 55.179 -24.888 1.00 62.23 P ANISOU 1704 P DG U 9 9537 6655 7453 -1407 -3320 1172 P ATOM 1705 OP1 DG U 9 36.440 53.713 -24.878 1.00 68.72 O ANISOU 1705 OP1 DG U 9 10377 7431 8302 -1405 -3368 1175 O ATOM 1706 OP2 DG U 9 37.192 55.844 -26.093 1.00 68.00 O ANISOU 1706 OP2 DG U 9 10265 7413 8158 -1399 -3299 1154 O ATOM 1707 O5' DG U 9 35.268 55.976 -24.608 1.00 81.40 O ANISOU 1707 O5' DG U 9 11952 9081 9896 -1457 -3295 1226 O ATOM 1708 C5' DG U 9 34.489 55.634 -23.480 1.00 73.63 C ANISOU 1708 C5' DG U 9 10963 8078 8935 -1475 -3306 1252 C ATOM 1709 C4' DG U 9 33.632 56.781 -22.966 1.00 63.29 C ANISOU 1709 C4' DG U 9 9634 6790 7624 -1505 -3270 1285 C ATOM 1710 O4' DG U 9 34.444 57.836 -22.424 1.00 60.56 O ANISOU 1710 O4' DG U 9 9278 6487 7245 -1480 -3235 1255 O ATOM 1711 C3' DG U 9 32.734 57.525 -23.939 1.00 53.87 C ANISOU 1711 C3' DG U 9 8431 5603 6435 -1545 -3248 1322 C ATOM 1712 O3' DG U 9 31.533 56.811 -24.043 1.00 48.48 O ANISOU 1712 O3' DG U 9 7747 4886 5788 -1583 -3273 1365 O ATOM 1713 C2' DG U 9 32.449 58.811 -23.180 1.00 57.22 C ANISOU 1713 C2' DG U 9 8835 6063 6843 -1554 -3207 1333 C ATOM 1714 C1' DG U 9 33.494 58.807 -22.070 1.00 55.38 C ANISOU 1714 C1' DG U 9 8605 5846 6591 -1513 -3205 1292 C ATOM 1715 N9 DG U 9 34.125 60.110 -21.953 1.00 52.65 N ANISOU 1715 N9 DG U 9 8251 5544 6211 -1498 -3163 1270 N ATOM 1716 C8 DG U 9 35.289 60.559 -22.524 1.00 55.79 C ANISOU 1716 C8 DG U 9 8652 5969 6577 -1468 -3149 1229 C ATOM 1717 N7 DG U 9 35.560 61.799 -22.208 1.00 56.05 N ANISOU 1717 N7 DG U 9 8674 6039 6583 -1465 -3110 1221 N ATOM 1718 C5 DG U 9 34.505 62.187 -21.385 1.00 53.62 C ANISOU 1718 C5 DG U 9 8356 5728 6289 -1492 -3099 1258 C ATOM 1719 C6 DG U 9 34.230 63.417 -20.738 1.00 48.22 C ANISOU 1719 C6 DG U 9 7659 5073 5588 -1501 -3061 1268 C ATOM 1720 O6 DG U 9 34.896 64.455 -20.761 1.00 49.75 O ANISOU 1720 O6 DG U 9 7850 5301 5750 -1488 -3029 1245 O ATOM 1721 N1 DG U 9 33.041 63.371 -20.010 1.00 50.83 N ANISOU 1721 N1 DG U 9 7979 5391 5942 -1529 -3063 1309 N ATOM 1722 C2 DG U 9 32.220 62.269 -19.907 1.00 54.10 C ANISOU 1722 C2 DG U 9 8395 5771 6392 -1548 -3097 1337 C ATOM 1723 N2 DG U 9 31.112 62.388 -19.159 1.00 60.97 N ANISOU 1723 N2 DG U 9 9249 6637 7278 -1573 -3094 1374 N ATOM 1724 N3 DG U 9 32.467 61.117 -20.506 1.00 50.76 N ANISOU 1724 N3 DG U 9 7984 5316 5984 -1541 -3133 1328 N ATOM 1725 C4 DG U 9 33.616 61.152 -21.222 1.00 52.51 C ANISOU 1725 C4 DG U 9 8218 5549 6184 -1513 -3131 1289 C ATOM 1726 P DT U 10 30.346 57.334 -24.998 1.00 50.13 P ANISOU 1726 P DT U 10 7942 5096 6009 -1630 -3260 1410 P ATOM 1727 OP1 DT U 10 29.441 56.183 -25.263 1.00 50.69 O ANISOU 1727 OP1 DT U 10 8018 5125 6116 -1660 -3300 1440 O ATOM 1728 OP2 DT U 10 30.952 58.050 -26.140 1.00 49.96 O ANISOU 1728 OP2 DT U 10 7924 5096 5963 -1619 -3237 1392 O ATOM 1729 O5' DT U 10 29.541 58.365 -24.070 1.00 59.66 O ANISOU 1729 O5' DT U 10 9123 6332 7214 -1652 -3227 1438 O ATOM 1730 C5' DT U 10 29.016 57.928 -22.799 1.00 52.92 C ANISOU 1730 C5' DT U 10 8261 5467 6378 -1659 -3241 1453 C ATOM 1731 C4' DT U 10 28.146 59.009 -22.176 1.00 50.06 C ANISOU 1731 C4' DT U 10 7871 5137 6012 -1682 -3207 1483 C ATOM 1732 O4' DT U 10 28.969 60.137 -21.755 1.00 49.81 O ANISOU 1732 O4' DT U 10 7837 5141 5945 -1654 -3169 1454 O ATOM 1733 C3' DT U 10 27.077 59.564 -23.112 1.00 49.34 C ANISOU 1733 C3' DT U 10 7761 5057 5930 -1721 -3193 1522 C ATOM 1734 O3' DT U 10 25.801 59.394 -22.514 1.00 47.99 O ANISOU 1734 O3' DT U 10 7566 4884 5783 -1754 -3201 1565 O ATOM 1735 C2' DT U 10 27.428 61.038 -23.318 1.00 53.34 C ANISOU 1735 C2' DT U 10 8258 5605 6403 -1712 -3145 1511 C ATOM 1736 C1' DT U 10 28.395 61.356 -22.187 1.00 48.61 C ANISOU 1736 C1' DT U 10 7668 5022 5782 -1675 -3132 1476 C ATOM 1737 N1 DT U 10 29.539 62.250 -22.544 1.00 50.89 N ANISOU 1737 N1 DT U 10 7966 5337 6034 -1646 -3102 1438 N ATOM 1738 C2 DT U 10 29.584 63.505 -21.984 1.00 51.12 C ANISOU 1738 C2 DT U 10 7983 5403 6039 -1642 -3062 1436 C ATOM 1739 O2 DT U 10 28.705 63.905 -21.244 1.00 55.09 O ANISOU 1739 O2 DT U 10 8466 5916 6548 -1659 -3051 1465 O ATOM 1740 N3 DT U 10 30.683 64.259 -22.331 1.00 48.04 N ANISOU 1740 N3 DT U 10 7602 5036 5615 -1616 -3037 1400 N ATOM 1741 C4 DT U 10 31.716 63.871 -23.176 1.00 54.83 C ANISOU 1741 C4 DT U 10 8481 5890 6464 -1593 -3048 1366 C ATOM 1742 O4 DT U 10 32.661 64.610 -23.439 1.00 54.55 O ANISOU 1742 O4 DT U 10 8450 5881 6397 -1571 -3024 1334 O ATOM 1743 C5 DT U 10 31.600 62.535 -23.723 1.00 54.60 C ANISOU 1743 C5 DT U 10 8462 5822 6461 -1596 -3090 1370 C ATOM 1744 C7 DT U 10 32.651 61.991 -24.647 1.00 52.83 C ANISOU 1744 C7 DT U 10 8257 5591 6226 -1570 -3106 1334 C ATOM 1745 C6 DT U 10 30.536 61.799 -23.380 1.00 47.77 C ANISOU 1745 C6 DT U 10 7591 4931 5629 -1623 -3115 1405 C ATOM 1746 P DG U 11 24.470 59.561 -23.389 1.00 57.87 P ANISOU 1746 P DG U 11 8794 6141 7053 -1799 -3201 1612 P ATOM 1747 OP1 DG U 11 23.396 58.766 -22.751 1.00 57.38 O ANISOU 1747 OP1 DG U 11 8715 6063 7023 -1827 -3229 1648 O ATOM 1748 OP2 DG U 11 24.813 59.287 -24.808 1.00 56.95 O ANISOU 1748 OP2 DG U 11 8694 6008 6936 -1801 -3212 1602 O ATOM 1749 O5' DG U 11 24.134 61.112 -23.264 1.00 58.15 O ANISOU 1749 O5' DG U 11 8804 6226 7065 -1802 -3152 1623 O ATOM 1750 C5' DG U 11 23.904 61.688 -21.995 1.00 58.25 C ANISOU 1750 C5' DG U 11 8799 6263 7068 -1795 -3132 1629 C ATOM 1751 C4' DG U 11 23.769 63.190 -22.157 1.00 62.73 C ANISOU 1751 C4' DG U 11 9351 6876 7609 -1794 -3085 1634 C ATOM 1752 O4' DG U 11 25.065 63.753 -22.461 1.00 59.78 O ANISOU 1752 O4' DG U 11 9000 6509 7204 -1763 -3064 1591 O ATOM 1753 C3' DG U 11 22.833 63.660 -23.271 1.00 67.85 C ANISOU 1753 C3' DG U 11 9977 7540 8262 -1823 -3074 1668 C ATOM 1754 O3' DG U 11 22.042 64.692 -22.692 1.00 73.37 O ANISOU 1754 O3' DG U 11 10646 8281 8951 -1829 -3042 1694 O ATOM 1755 C2' DG U 11 23.791 64.137 -24.366 1.00 60.16 C ANISOU 1755 C2' DG U 11 9025 6568 7265 -1807 -3058 1637 C ATOM 1756 C1' DG U 11 24.923 64.687 -23.510 1.00 60.74 C ANISOU 1756 C1' DG U 11 9115 6654 7310 -1772 -3036 1597 C ATOM 1757 N9 DG U 11 26.239 64.800 -24.129 1.00 53.29 N ANISOU 1757 N9 DG U 11 8198 5705 6343 -1745 -3030 1555 N ATOM 1758 C8 DG U 11 26.866 63.905 -24.965 1.00 48.76 C ANISOU 1758 C8 DG U 11 7648 5102 5778 -1737 -3058 1535 C ATOM 1759 N7 DG U 11 28.058 64.292 -25.328 1.00 51.56 N ANISOU 1759 N7 DG U 11 8021 5464 6104 -1708 -3043 1496 N ATOM 1760 C5 DG U 11 28.235 65.514 -24.679 1.00 49.88 C ANISOU 1760 C5 DG U 11 7799 5288 5865 -1699 -3003 1489 C ATOM 1761 C6 DG U 11 29.328 66.416 -24.689 1.00 47.97 C ANISOU 1761 C6 DG U 11 7568 5072 5587 -1672 -2973 1453 C ATOM 1762 O6 DG U 11 30.413 66.313 -25.283 1.00 55.07 O ANISOU 1762 O6 DG U 11 8485 5969 6469 -1649 -2974 1418 O ATOM 1763 N1 DG U 11 29.080 67.538 -23.900 1.00 49.62 N ANISOU 1763 N1 DG U 11 7764 5312 5778 -1672 -2938 1460 N ATOM 1764 C2 DG U 11 27.924 67.763 -23.186 1.00 47.10 C ANISOU 1764 C2 DG U 11 7422 5002 5473 -1693 -2933 1497 C ATOM 1765 N2 DG U 11 27.869 68.898 -22.472 1.00 53.69 N ANISOU 1765 N2 DG U 11 8247 5868 6284 -1687 -2898 1498 N ATOM 1766 N3 DG U 11 26.896 66.930 -23.168 1.00 51.60 N ANISOU 1766 N3 DG U 11 7978 5552 6076 -1717 -2961 1531 N ATOM 1767 C4 DG U 11 27.122 65.834 -23.935 1.00 50.59 C ANISOU 1767 C4 DG U 11 7865 5391 5967 -1720 -2995 1525 C ATOM 1768 P DT U 12 21.027 65.552 -23.590 1.00 86.93 P ANISOU 1768 P DT U 12 12334 10030 10664 -1851 -3019 1729 P ATOM 1769 OP1 DT U 12 19.776 65.726 -22.822 1.00 85.26 O ANISOU 1769 OP1 DT U 12 12086 9844 10465 -1866 -3015 1772 O ATOM 1770 OP2 DT U 12 20.969 64.941 -24.939 1.00 88.72 O ANISOU 1770 OP2 DT U 12 12570 10233 10906 -1869 -3042 1733 O ATOM 1771 O5' DT U 12 21.738 66.979 -23.672 1.00100.25 O ANISOU 1771 O5' DT U 12 14028 11751 12311 -1827 -2972 1705 O ATOM 1772 C5' DT U 12 22.275 67.489 -22.459 1.00100.79 C ANISOU 1772 C5' DT U 12 14103 11834 12361 -1802 -2952 1685 C ATOM 1773 C4' DT U 12 22.761 68.918 -22.604 1.00100.13 C ANISOU 1773 C4' DT U 12 14022 11784 12239 -1784 -2906 1669 C ATOM 1774 O4' DT U 12 24.071 68.959 -23.226 1.00 95.50 O ANISOU 1774 O4' DT U 12 13468 11184 11634 -1767 -2903 1626 O ATOM 1775 C3' DT U 12 21.892 69.811 -23.471 1.00 95.04 C ANISOU 1775 C3' DT U 12 13355 11171 11586 -1799 -2880 1700 C ATOM 1776 O3' DT U 12 22.127 71.136 -23.042 1.00 95.30 O ANISOU 1776 O3' DT U 12 13387 11239 11584 -1779 -2837 1691 O ATOM 1777 C2' DT U 12 22.490 69.549 -24.850 1.00 87.02 C ANISOU 1777 C2' DT U 12 12359 10136 10569 -1804 -2890 1681 C ATOM 1778 C1' DT U 12 23.971 69.585 -24.492 1.00 76.81 C ANISOU 1778 C1' DT U 12 11098 8830 9254 -1775 -2885 1631 C ATOM 1779 N1 DT U 12 24.894 68.856 -25.406 1.00 58.22 N ANISOU 1779 N1 DT U 12 8771 6445 6903 -1770 -2907 1602 N ATOM 1780 C2 DT U 12 26.163 69.363 -25.553 1.00 57.26 C ANISOU 1780 C2 DT U 12 8674 6329 6752 -1745 -2888 1560 C ATOM 1781 O2 DT U 12 26.532 70.370 -24.987 1.00 59.10 O ANISOU 1781 O2 DT U 12 8908 6589 6959 -1730 -2855 1548 O ATOM 1782 N3 DT U 12 26.984 68.657 -26.392 1.00 59.88 N ANISOU 1782 N3 DT U 12 9029 6637 7087 -1736 -2909 1535 N ATOM 1783 C4 DT U 12 26.665 67.509 -27.086 1.00 65.24 C ANISOU 1783 C4 DT U 12 9712 7283 7794 -1750 -2947 1546 C ATOM 1784 O4 DT U 12 27.477 66.948 -27.819 1.00 67.52 O ANISOU 1784 O4 DT U 12 10022 7553 8081 -1738 -2963 1521 O ATOM 1785 C5 DT U 12 25.315 67.024 -26.892 1.00 63.96 C ANISOU 1785 C5 DT U 12 9525 7114 7663 -1780 -2965 1590 C ATOM 1786 C7 DT U 12 24.872 65.779 -27.605 1.00 62.54 C ANISOU 1786 C7 DT U 12 9350 6899 7516 -1799 -3008 1605 C ATOM 1787 C6 DT U 12 24.499 67.708 -26.067 1.00 57.30 C ANISOU 1787 C6 DT U 12 8656 6297 6817 -1788 -2945 1616 C ATOM 1788 P DC U 13 20.955 72.233 -23.104 1.00 95.04 P ANISOU 1788 P DC U 13 13321 11251 11539 -1783 -2803 1732 P ATOM 1789 OP1 DC U 13 20.283 72.256 -21.787 1.00 97.27 O ANISOU 1789 OP1 DC U 13 13583 11547 11826 -1777 -2801 1754 O ATOM 1790 OP2 DC U 13 20.167 71.997 -24.339 1.00 93.27 O ANISOU 1790 OP2 DC U 13 13080 11027 11331 -1806 -2814 1761 O ATOM 1791 O5' DC U 13 21.752 73.601 -23.282 1.00 94.65 O ANISOU 1791 O5' DC U 13 13290 11227 11448 -1761 -2758 1706 O ATOM 1792 C5' DC U 13 23.117 73.649 -22.876 1.00 88.34 C ANISOU 1792 C5' DC U 13 12522 10412 10630 -1743 -2755 1659 C ATOM 1793 C4' DC U 13 23.854 74.676 -23.710 1.00 85.42 C ANISOU 1793 C4' DC U 13 12170 10058 10227 -1734 -2722 1636 C ATOM 1794 O4' DC U 13 24.708 74.029 -24.691 1.00 82.54 O ANISOU 1794 O4' DC U 13 11827 9666 9868 -1737 -2743 1608 O ATOM 1795 C3' DC U 13 22.937 75.576 -24.525 1.00 87.45 C ANISOU 1795 C3' DC U 13 12407 10346 10473 -1741 -2694 1669 C ATOM 1796 O3' DC U 13 23.636 76.760 -24.791 1.00 93.71 O ANISOU 1796 O3' DC U 13 13218 11159 11228 -1726 -2655 1646 O ATOM 1797 C2' DC U 13 22.770 74.771 -25.805 1.00 79.39 C ANISOU 1797 C2' DC U 13 11386 9304 9475 -1762 -2722 1675 C ATOM 1798 C1' DC U 13 24.216 74.318 -25.988 1.00 78.86 C ANISOU 1798 C1' DC U 13 11353 9209 9402 -1752 -2735 1627 C ATOM 1799 N1 DC U 13 24.342 73.113 -26.855 1.00 73.46 N ANISOU 1799 N1 DC U 13 10677 8491 8745 -1765 -2774 1623 N ATOM 1800 C2 DC U 13 25.584 72.767 -27.409 1.00 69.27 C ANISOU 1800 C2 DC U 13 10176 7940 8205 -1754 -2783 1583 C ATOM 1801 O2 DC U 13 26.579 73.465 -27.164 1.00 74.29 O ANISOU 1801 O2 DC U 13 10829 8587 8810 -1734 -2759 1551 O ATOM 1802 N3 DC U 13 25.660 71.667 -28.198 1.00 56.83 N ANISOU 1802 N3 DC U 13 8608 6333 6653 -1763 -2819 1581 N ATOM 1803 C4 DC U 13 24.572 70.937 -28.440 1.00 61.68 C ANISOU 1803 C4 DC U 13 9203 6935 7299 -1787 -2845 1617 C ATOM 1804 N4 DC U 13 24.698 69.859 -29.228 1.00 63.70 N ANISOU 1804 N4 DC U 13 9470 7157 7575 -1796 -2880 1613 N ATOM 1805 C5 DC U 13 23.300 71.281 -27.888 1.00 61.33 C ANISOU 1805 C5 DC U 13 9126 6912 7264 -1801 -2836 1658 C ATOM 1806 C6 DC U 13 23.232 72.365 -27.111 1.00 64.20 C ANISOU 1806 C6 DC U 13 9481 7308 7604 -1788 -2801 1660 C ATOM 1807 P DA U 14 22.886 78.175 -24.727 1.00 88.17 P ANISOU 1807 P DA U 14 12502 10501 10498 -1715 -2608 1674 P ATOM 1808 OP1 DA U 14 22.804 78.585 -23.307 1.00 93.94 O ANISOU 1808 OP1 DA U 14 13231 11245 11218 -1698 -2594 1676 O ATOM 1809 OP2 DA U 14 21.654 78.076 -25.543 1.00 79.79 O ANISOU 1809 OP2 DA U 14 11412 9451 9452 -1729 -2612 1718 O ATOM 1810 O5' DA U 14 23.911 79.158 -25.447 1.00 86.84 O ANISOU 1810 O5' DA U 14 12361 10341 10292 -1706 -2576 1641 O ATOM 1811 C5' DA U 14 25.287 79.034 -25.109 1.00 78.57 C ANISOU 1811 C5' DA U 14 11343 9277 9232 -1697 -2581 1594 C ATOM 1812 C4' DA U 14 26.135 79.313 -26.334 1.00 74.98 C ANISOU 1812 C4' DA U 14 10910 8820 8760 -1700 -2571 1568 C ATOM 1813 O4' DA U 14 26.211 78.136 -27.178 1.00 70.38 O ANISOU 1813 O4' DA U 14 10326 8208 8206 -1714 -2610 1566 O ATOM 1814 C3' DA U 14 25.599 80.431 -27.220 1.00 72.34 C ANISOU 1814 C3' DA U 14 10571 8514 8402 -1700 -2534 1589 C ATOM 1815 O3' DA U 14 26.695 81.122 -27.776 1.00 70.10 O ANISOU 1815 O3' DA U 14 10314 8235 8086 -1694 -2510 1555 O ATOM 1816 C2' DA U 14 24.813 79.685 -28.292 1.00 69.79 C ANISOU 1816 C2' DA U 14 10229 8180 8107 -1718 -2559 1616 C ATOM 1817 C1' DA U 14 25.639 78.412 -28.442 1.00 66.28 C ANISOU 1817 C1' DA U 14 9799 7698 7686 -1725 -2601 1587 C ATOM 1818 N9 DA U 14 24.847 77.255 -28.845 1.00 59.20 N ANISOU 1818 N9 DA U 14 8885 6781 6829 -1743 -2640 1612 N ATOM 1819 C8 DA U 14 23.518 77.032 -28.603 1.00 53.51 C ANISOU 1819 C8 DA U 14 8133 6069 6130 -1754 -2649 1656 C ATOM 1820 N7 DA U 14 23.082 75.892 -29.079 1.00 51.16 N ANISOU 1820 N7 DA U 14 7826 5746 5866 -1772 -2688 1670 N ATOM 1821 C5 DA U 14 24.199 75.335 -29.685 1.00 51.78 C ANISOU 1821 C5 DA U 14 7932 5798 5944 -1770 -2705 1633 C ATOM 1822 C6 DA U 14 24.402 74.130 -30.390 1.00 54.88 C ANISOU 1822 C6 DA U 14 8334 6156 6362 -1781 -2745 1626 C ATOM 1823 N6 DA U 14 23.441 73.221 -30.610 1.00 49.45 N ANISOU 1823 N6 DA U 14 7628 5452 5709 -1802 -2777 1657 N ATOM 1824 N1 DA U 14 25.645 73.891 -30.858 1.00 53.69 N ANISOU 1824 N1 DA U 14 8213 5988 6200 -1769 -2750 1586 N ATOM 1825 C2 DA U 14 26.617 74.785 -30.646 1.00 52.92 C ANISOU 1825 C2 DA U 14 8132 5907 6067 -1750 -2718 1555 C ATOM 1826 N3 DA U 14 26.548 75.946 -30.006 1.00 51.90 N ANISOU 1826 N3 DA U 14 7999 5809 5913 -1742 -2681 1558 N ATOM 1827 C4 DA U 14 25.299 76.160 -29.547 1.00 55.78 C ANISOU 1827 C4 DA U 14 8463 6316 6417 -1751 -2676 1597 C ATOM 1828 P DT U 15 26.454 82.430 -28.670 1.00 77.34 P ANISOU 1828 P DT U 15 11235 9180 8969 -1691 -2465 1567 P ATOM 1829 OP1 DT U 15 27.490 83.422 -28.307 1.00 80.94 O ANISOU 1829 OP1 DT U 15 11719 9650 9386 -1678 -2432 1534 O ATOM 1830 OP2 DT U 15 25.013 82.771 -28.607 1.00 78.87 O ANISOU 1830 OP2 DT U 15 11401 9395 9170 -1689 -2452 1617 O ATOM 1831 O5' DT U 15 26.731 81.919 -30.155 1.00 58.94 O ANISOU 1831 O5' DT U 15 8911 6837 6648 -1703 -2482 1559 O ATOM 1832 C5' DT U 15 27.988 81.330 -30.445 1.00 58.60 C ANISOU 1832 C5' DT U 15 8889 6773 6603 -1703 -2502 1518 C ATOM 1833 C4' DT U 15 27.834 80.532 -31.719 1.00 60.65 C ANISOU 1833 C4' DT U 15 9146 7016 6884 -1716 -2528 1524 C ATOM 1834 O4' DT U 15 26.866 79.482 -31.483 1.00 51.26 O ANISOU 1834 O4' DT U 15 7933 5809 5736 -1727 -2564 1553 O ATOM 1835 C3' DT U 15 27.282 81.328 -32.898 1.00 54.09 C ANISOU 1835 C3' DT U 15 8311 6205 6036 -1720 -2501 1545 C ATOM 1836 O3' DT U 15 28.350 81.654 -33.786 1.00 59.78 O ANISOU 1836 O3' DT U 15 9057 6927 6731 -1716 -2488 1513 O ATOM 1837 C2' DT U 15 26.251 80.390 -33.542 1.00 44.48 C ANISOU 1837 C2' DT U 15 7071 4973 4855 -1734 -2534 1578 C ATOM 1838 C1' DT U 15 26.443 79.088 -32.758 1.00 45.94 C ANISOU 1838 C1' DT U 15 7253 5127 5074 -1739 -2578 1568 C ATOM 1839 N1 DT U 15 25.226 78.244 -32.603 1.00 48.51 N ANISOU 1839 N1 DT U 15 7552 5443 5438 -1754 -2608 1606 N ATOM 1840 C2 DT U 15 25.298 76.952 -33.068 1.00 50.35 C ANISOU 1840 C2 DT U 15 7787 5643 5702 -1765 -2652 1603 C ATOM 1841 O2 DT U 15 26.308 76.508 -33.585 1.00 47.05 O ANISOU 1841 O2 DT U 15 7392 5206 5280 -1760 -2664 1571 O ATOM 1842 N3 DT U 15 24.148 76.218 -32.900 1.00 46.40 N ANISOU 1842 N3 DT U 15 7260 5134 5234 -1781 -2679 1639 N ATOM 1843 C4 DT U 15 22.960 76.648 -32.335 1.00 42.99 C ANISOU 1843 C4 DT U 15 6799 4726 4808 -1785 -2666 1678 C ATOM 1844 O4 DT U 15 21.977 75.920 -32.244 1.00 45.60 O ANISOU 1844 O4 DT U 15 7107 5049 5169 -1800 -2693 1710 O ATOM 1845 C5 DT U 15 22.962 78.014 -31.862 1.00 52.67 C ANISOU 1845 C5 DT U 15 8025 5988 6000 -1768 -2619 1680 C ATOM 1846 C7 DT U 15 21.727 78.588 -31.229 1.00 53.43 C ANISOU 1846 C7 DT U 15 8091 6114 6096 -1763 -2600 1722 C ATOM 1847 C6 DT U 15 24.080 78.740 -32.012 1.00 47.37 C ANISOU 1847 C6 DT U 15 7380 5321 5295 -1754 -2593 1644 C TER 1848 DT U 15 HETATM 1849 O HOH A 201 6.805 11.338 -7.508 1.00 24.59 O HETATM 1850 O HOH A 202 8.656 11.853 -15.523 1.00 26.07 O HETATM 1851 O HOH A 203 10.983 28.743 -15.678 1.00 26.23 O HETATM 1852 O HOH A 204 -0.123 11.425 -21.028 1.00 26.24 O HETATM 1853 O HOH A 205 5.845 10.717 -9.972 1.00 26.80 O HETATM 1854 O HOH A 206 4.000 17.069 -16.623 1.00 27.68 O HETATM 1855 O HOH A 207 5.188 20.840 -8.890 1.00 28.20 O HETATM 1856 O HOH A 208 7.752 18.063 -5.276 1.00 29.27 O HETATM 1857 O HOH A 209 11.743 24.617 2.963 1.00 29.41 O HETATM 1858 O HOH A 210 24.074 42.273 -6.614 1.00 29.51 O HETATM 1859 O HOH A 211 -1.986 13.812 -19.155 1.00 29.74 O HETATM 1860 O HOH A 212 24.696 43.231 -10.651 1.00 30.00 O HETATM 1861 O HOH A 213 17.359 30.562 -16.932 1.00 31.04 O HETATM 1862 O HOH A 214 24.315 45.074 -6.614 1.00 31.20 O HETATM 1863 O HOH A 215 2.333 24.534 -3.436 1.00 31.64 O HETATM 1864 O HOH A 216 4.014 22.397 -0.673 1.00 31.92 O HETATM 1865 O HOH A 217 23.651 28.979 -7.655 1.00 32.54 O HETATM 1866 O HOH A 218 18.214 12.169 -2.990 1.00 35.87 O HETATM 1867 O HOH A 219 5.204 11.104 -15.710 1.00 36.21 O HETATM 1868 O HOH A 220 1.657 15.798 -15.718 1.00 36.42 O HETATM 1869 O HOH A 221 6.423 22.049 -6.755 1.00 36.73 O HETATM 1870 O HOH A 222 12.454 12.525 1.145 1.00 36.81 O HETATM 1871 O HOH A 223 23.629 16.249 -3.495 1.00 37.65 O HETATM 1872 O HOH A 224 0.100 25.850 -9.517 1.00 37.73 O HETATM 1873 O HOH A 225 0.189 25.840 -6.776 1.00 38.19 O HETATM 1874 O HOH A 226 -0.208 22.157 -12.902 1.00 38.83 O HETATM 1875 O HOH A 227 6.169 18.398 -9.364 1.00 38.88 O HETATM 1876 O HOH A 228 -1.386 19.410 -17.287 1.00 38.88 O HETATM 1877 O HOH A 229 15.169 33.968 -17.841 1.00 39.05 O HETATM 1878 O HOH A 230 -8.560 11.550 -21.826 1.00 39.81 O HETATM 1879 O HOH A 231 1.456 22.429 -2.126 1.00 40.21 O HETATM 1880 O HOH A 232 27.927 53.951 -0.042 1.00 40.27 O HETATM 1881 O HOH A 233 9.778 40.284 -5.925 1.00 40.32 O HETATM 1882 O HOH A 234 3.784 29.281 -15.182 1.00 41.24 O HETATM 1883 O HOH A 235 2.115 38.588 -8.195 1.00 41.38 O HETATM 1884 O HOH A 236 6.287 20.308 -4.833 1.00 42.23 O HETATM 1885 O HOH A 237 35.719 46.164 -11.694 1.00 42.63 O HETATM 1886 O HOH A 238 7.975 17.079 -7.909 1.00 43.20 O HETATM 1887 O HOH A 239 -5.129 14.399 -17.497 1.00 43.24 O HETATM 1888 O HOH A 240 22.447 24.826 2.224 1.00 43.25 O HETATM 1889 O HOH A 241 26.168 43.095 6.767 1.00 43.78 O HETATM 1890 O HOH A 242 9.229 30.685 2.501 1.00 44.43 O HETATM 1891 O HOH A 243 3.718 21.182 -3.941 1.00 44.67 O HETATM 1892 O HOH A 244 30.020 53.644 5.826 1.00 44.72 O HETATM 1893 O HOH A 245 16.973 33.281 -16.323 1.00 44.80 O HETATM 1894 O HOH A 246 36.637 39.551 -4.110 1.00 45.10 O HETATM 1895 O HOH A 247 0.444 22.998 -10.284 1.00 45.39 O HETATM 1896 O HOH A 248 44.078 48.116 -6.572 1.00 45.49 O HETATM 1897 O HOH A 249 10.348 39.494 -16.791 1.00 45.99 O HETATM 1898 O HOH A 250 20.712 34.695 1.882 1.00 46.20 O HETATM 1899 O HOH A 251 21.883 43.303 2.002 1.00 47.14 O HETATM 1900 O HOH A 252 26.051 29.028 -0.852 1.00 47.67 O HETATM 1901 O HOH A 253 34.734 42.372 6.436 1.00 47.75 O HETATM 1902 O HOH A 254 25.281 44.652 -13.822 1.00 47.94 O HETATM 1903 O HOH A 255 38.971 41.715 -9.009 1.00 48.15 O HETATM 1904 O HOH A 256 15.248 36.225 -18.835 1.00 48.47 O HETATM 1905 O HOH A 257 19.991 29.814 -16.323 1.00 48.74 O HETATM 1906 O HOH A 258 -1.222 16.335 -16.940 1.00 48.95 O HETATM 1907 O HOH A 259 22.629 13.519 -3.366 1.00 49.23 O HETATM 1908 O HOH A 260 -3.113 9.435 -19.527 1.00 49.42 O HETATM 1909 O HOH A 261 47.600 42.700 -1.097 1.00 50.24 O HETATM 1910 O HOH A 262 44.508 57.779 -0.009 1.00 50.47 O HETATM 1911 O HOH A 263 18.206 29.426 4.760 1.00 51.31 O HETATM 1912 O HOH A 264 45.801 53.226 -4.446 1.00 51.46 O HETATM 1913 O HOH A 265 42.038 56.683 3.756 1.00 52.30 O HETATM 1914 O HOH A 266 14.096 23.218 4.122 1.00 52.42 O HETATM 1915 O HOH A 267 5.919 14.537 -7.900 1.00 52.88 O HETATM 1916 O HOH A 268 27.412 52.803 -15.923 1.00 54.70 O HETATM 1917 O HOH A 269 5.909 16.143 -3.355 1.00 54.70 O HETATM 1918 O HOH A 270 29.877 46.130 8.827 1.00 56.02 O HETATM 1919 O HOH A 271 3.130 20.072 -7.463 1.00 56.15 O HETATM 1920 O HOH A 272 40.445 53.709 13.633 1.00 57.00 O HETATM 1921 O HOH A 273 24.933 26.675 2.000 1.00 58.07 O HETATM 1922 O HOH A 274 18.720 45.435 4.079 1.00 61.58 O HETATM 1923 O HOH U 101 28.517 76.433 -34.689 1.00 42.88 O HETATM 1924 O HOH U 102 49.485 53.728 -4.117 1.00 51.20 O HETATM 1925 O HOH U 103 35.006 64.688 -25.142 1.00 52.61 O HETATM 1926 O HOH U 104 28.543 60.217 -18.810 1.00 53.13 O HETATM 1927 O HOH U 105 29.111 77.524 -29.827 1.00 54.66 O HETATM 1928 O HOH U 106 26.528 63.982 -19.909 1.00 56.04 O HETATM 1929 O HOH U 107 37.060 63.367 -24.088 1.00 56.56 O MASTER 433 0 0 12 0 0 0 6 1927 2 0 17 END
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Related entries of code: 3vok
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
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Protein Sequence Similarity
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Complexes with the same small molecule ligand
PDB Code
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Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
3vok
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
transcriptional regulator heme-regulated transporter regulator (HrtR)
Ligand Name
15-mer DNA
EC.Number
E.C.-.-.-.-
Resolution
2(Å)
Affinity (Kd/Ki/IC50)
Kd=0.2nM
Release Year
2012
Protein/NA Sequence
Check fasta file
Primary Reference
(2012) J.Biol.Chem. Vol. 287: pp. 30755-30768
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q9CHR1
Entrez Gene ID
No matched NCBI Entrez Gene ID found!
ASD
Information of known allosteric effects of PDB entries
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