Browse entries in the PDBbind-CN Database
HEADER DNA BINDING PROTEIN/DNA 05-JUL-13 4LJR TITLE STRUCTURAL INSIGHTS INTO THE UNIQUE SINGLE-STRANDED DNA BINDING MODE TITLE 2 OF DNA PROCESSING PROTEIN A FROM HELICOBACTER PYLORI COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA PROCESSING CHAIN A; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SINGLE-STRANDED DNA; COMPND 7 CHAIN: C, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI; SOURCE 3 ORGANISM_TAXID: 85962; SOURCE 4 STRAIN: 26695; SOURCE 5 GENE: HP0333, HP_0333; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES KEYWDS DNA PROCESSING A DOMAIN, ROSSMANN FOLD, SSDNA BINDING, COMPLEX, KEYWDS 2 NATURAL RECOMBINATION MEDIATING PROTEIN, DNA BINDING PROTEIN-DNA KEYWDS 3 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.WANG REVDAT 4 12-NOV-14 4LJR 1 KEYWDS REVDAT 3 02-APR-14 4LJR 1 JRNL REVDAT 2 29-JAN-14 4LJR 1 JRNL REVDAT 1 01-JAN-14 4LJR 0 JRNL AUTH W.WANG,J.DING,Y.ZHANG,Y.HU,D.C.WANG JRNL TITL STRUCTURAL INSIGHTS INTO THE UNIQUE SINGLE-STRANDED JRNL TITL 2 DNA-BINDING MODE OF HELICOBACTER PYLORI DPRA. JRNL REF NUCLEIC ACIDS RES. V. 42 3478 2014 JRNL REFN ISSN 0305-1048 JRNL PMID 24369431 JRNL DOI 10.1093/NAR/GKT1334 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.16 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 80.5 REMARK 3 NUMBER OF REFLECTIONS : 34988 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.196 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030 REMARK 3 FREE R VALUE TEST SET COUNT : 1759 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 33.1604 - 4.2298 0.91 3014 156 0.1711 0.1985 REMARK 3 2 4.2298 - 3.3583 0.95 3051 175 0.1576 0.1816 REMARK 3 3 3.3583 - 2.9341 0.96 3049 172 0.1857 0.2389 REMARK 3 4 2.9341 - 2.6660 0.93 2931 159 0.1971 0.2589 REMARK 3 5 2.6660 - 2.4750 0.89 2831 172 0.2006 0.2463 REMARK 3 6 2.4750 - 2.3291 0.83 2647 120 0.1896 0.2140 REMARK 3 7 2.3291 - 2.2125 0.65 2044 103 0.2712 0.3759 REMARK 3 8 2.2125 - 2.1162 0.78 2469 118 0.1938 0.2382 REMARK 3 9 2.1162 - 2.0347 0.77 2423 132 0.1992 0.2440 REMARK 3 10 2.0347 - 1.9645 0.76 2397 122 0.2092 0.2753 REMARK 3 11 1.9645 - 1.9031 0.64 2000 111 0.3552 0.4481 REMARK 3 12 1.9031 - 1.8487 0.67 2098 108 0.2564 0.2936 REMARK 3 13 1.8487 - 1.8000 0.71 2275 111 0.2683 0.3342 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.20 REMARK 3 SHRINKAGE RADIUS : 0.95 REMARK 3 K_SOL : 0.35 REMARK 3 B_SOL : 43.50 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.720 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.77830 REMARK 3 B22 (A**2) : 7.00780 REMARK 3 B33 (A**2) : -4.22950 REMARK 3 B12 (A**2) : -0.00000 REMARK 3 B13 (A**2) : 1.35590 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 : 0.004 3530 REMARK 3 ANGLE : 0.870 4804 REMARK 3 CHIRALITY : 0.059 564 REMARK 3 PLANARITY : 0.004 593 REMARK 3 DIHEDRAL : 13.933 1360 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 19 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain 'A' and (resseq 5:18) REMARK 3 ORIGIN FOR THE GROUP (A): 18.7643 -8.0199 2.4677 REMARK 3 T TENSOR REMARK 3 T11: 0.1151 T22: 0.1092 REMARK 3 T33: 0.1670 T12: 0.0099 REMARK 3 T13: -0.0037 T23: -0.0360 REMARK 3 L TENSOR REMARK 3 L11: 0.4476 L22: 0.4270 REMARK 3 L33: 0.3704 L12: 0.2560 REMARK 3 L13: 0.0526 L23: -0.1123 REMARK 3 S TENSOR REMARK 3 S11: 0.0444 S12: -0.0082 S13: -0.1419 REMARK 3 S21: -0.0068 S22: -0.1342 S23: -0.1252 REMARK 3 S31: 0.0965 S32: -0.1158 S33: 0.0011 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain 'A' and (resseq 19:41) REMARK 3 ORIGIN FOR THE GROUP (A): 7.3728 -5.8618 6.2797 REMARK 3 T TENSOR REMARK 3 T11: 0.1211 T22: 0.0936 REMARK 3 T33: 0.1926 T12: -0.0099 REMARK 3 T13: 0.0088 T23: -0.0324 REMARK 3 L TENSOR REMARK 3 L11: 0.1479 L22: 0.2112 REMARK 3 L33: 1.1938 L12: -0.0931 REMARK 3 L13: -0.3887 L23: 0.1736 REMARK 3 S TENSOR REMARK 3 S11: 0.0043 S12: 0.1941 S13: -0.0812 REMARK 3 S21: -0.0862 S22: -0.1223 S23: -0.0131 REMARK 3 S31: 0.1404 S32: -0.4792 S33: 0.0063 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain 'A' and (resseq 42:71) REMARK 3 ORIGIN FOR THE GROUP (A): 16.3744 -4.6630 27.4294 REMARK 3 T TENSOR REMARK 3 T11: 0.2094 T22: 0.3980 REMARK 3 T33: 0.1409 T12: -0.0146 REMARK 3 T13: -0.0344 T23: 0.0103 REMARK 3 L TENSOR REMARK 3 L11: 0.7097 L22: 0.3773 REMARK 3 L33: 0.3264 L12: 0.0299 REMARK 3 L13: 0.2955 L23: 0.2786 REMARK 3 S TENSOR REMARK 3 S11: -0.0893 S12: -0.6978 S13: -0.0024 REMARK 3 S21: 0.2098 S22: -0.0133 S23: 0.1053 REMARK 3 S31: 0.1160 S32: 0.1369 S33: -0.0048 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain 'A' and (resseq 72:109) REMARK 3 ORIGIN FOR THE GROUP (A): 19.3208 -4.8264 16.0887 REMARK 3 T TENSOR REMARK 3 T11: 0.0906 T22: 0.1041 REMARK 3 T33: 0.1115 T12: 0.0011 REMARK 3 T13: -0.0167 T23: -0.0141 REMARK 3 L TENSOR REMARK 3 L11: 0.2958 L22: 0.1317 REMARK 3 L33: 0.2141 L12: 0.0549 REMARK 3 L13: 0.0752 L23: 0.0095 REMARK 3 S TENSOR REMARK 3 S11: -0.0189 S12: -0.2066 S13: 0.0619 REMARK 3 S21: -0.0378 S22: -0.0736 S23: -0.0457 REMARK 3 S31: 0.0647 S32: 0.0468 S33: -0.0263 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: chain 'A' and (resseq 110:122) REMARK 3 ORIGIN FOR THE GROUP (A): 26.7858 -7.8129 14.1504 REMARK 3 T TENSOR REMARK 3 T11: 0.1213 T22: 0.2102 REMARK 3 T33: 0.2172 T12: 0.0186 REMARK 3 T13: -0.0204 T23: 0.0331 REMARK 3 L TENSOR REMARK 3 L11: 0.7367 L22: 0.4393 REMARK 3 L33: 1.0068 L12: -0.2925 REMARK 3 L13: -0.3939 L23: -0.3388 REMARK 3 S TENSOR REMARK 3 S11: -0.1609 S12: -0.2248 S13: -0.3476 REMARK 3 S21: -0.1202 S22: -0.0188 S23: -0.1980 REMARK 3 S31: 0.3590 S32: 0.4254 S33: 0.0759 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: chain 'A' and (resseq 123:136) REMARK 3 ORIGIN FOR THE GROUP (A): 18.5746 0.3630 3.6128 REMARK 3 T TENSOR REMARK 3 T11: 0.1036 T22: -0.3573 REMARK 3 T33: 0.2240 T12: 0.0526 REMARK 3 T13: -0.0047 T23: 0.0312 REMARK 3 L TENSOR REMARK 3 L11: 0.0870 L22: 0.2815 REMARK 3 L33: 0.0921 L12: -0.1424 REMARK 3 L13: 0.0077 L23: 0.0112 REMARK 3 S TENSOR REMARK 3 S11: -0.0658 S12: 0.1940 S13: -0.0220 REMARK 3 S21: -0.2177 S22: -0.0668 S23: -0.1236 REMARK 3 S31: 0.0659 S32: 0.2380 S33: -0.0342 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: chain 'A' and (resseq 137:163) REMARK 3 ORIGIN FOR THE GROUP (A): 11.4373 4.4069 18.0184 REMARK 3 T TENSOR REMARK 3 T11: 0.1294 T22: 0.1022 REMARK 3 T33: 0.2003 T12: 0.0481 REMARK 3 T13: -0.0246 T23: -0.1042 REMARK 3 L TENSOR REMARK 3 L11: 0.2114 L22: 0.4545 REMARK 3 L33: 0.6360 L12: -0.0234 REMARK 3 L13: 0.3153 L23: 0.1567 REMARK 3 S TENSOR REMARK 3 S11: -0.0005 S12: -0.4587 S13: 0.1757 REMARK 3 S21: -0.0299 S22: -0.1160 S23: 0.0018 REMARK 3 S31: -0.0474 S32: -0.4865 S33: 0.0455 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: chain 'A' and (resseq 164:182) REMARK 3 ORIGIN FOR THE GROUP (A): 4.6217 4.7229 22.3252 REMARK 3 T TENSOR REMARK 3 T11: 0.1985 T22: 0.2954 REMARK 3 T33: 0.2042 T12: 0.0296 REMARK 3 T13: -0.0478 T23: -0.1154 REMARK 3 L TENSOR REMARK 3 L11: 0.3545 L22: 0.4141 REMARK 3 L33: 0.2988 L12: 0.1959 REMARK 3 L13: 0.2314 L23: -0.0019 REMARK 3 S TENSOR REMARK 3 S11: 0.0636 S12: -0.3261 S13: 0.2029 REMARK 3 S21: -0.1299 S22: -0.0738 S23: 0.1977 REMARK 3 S31: -0.0571 S32: 0.1189 S33: 0.0146 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: chain 'A' and (resseq 183:197) REMARK 3 ORIGIN FOR THE GROUP (A): 11.5667 9.8239 34.7415 REMARK 3 T TENSOR REMARK 3 T11: 0.2877 T22: 0.6050 REMARK 3 T33: -0.1622 T12: 0.1202 REMARK 3 T13: 0.0187 T23: -0.5059 REMARK 3 L TENSOR REMARK 3 L11: 0.1221 L22: 0.0346 REMARK 3 L33: 0.0301 L12: -0.0221 REMARK 3 L13: -0.0040 L23: 0.0063 REMARK 3 S TENSOR REMARK 3 S11: -0.0056 S12: 0.0350 S13: 0.1004 REMARK 3 S21: -0.0688 S22: -0.0113 S23: 0.0177 REMARK 3 S31: -0.1571 S32: -0.0332 S33: 0.0567 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: chain 'A' and (resseq 198:217) REMARK 3 ORIGIN FOR THE GROUP (A): 4.5931 -5.6950 32.7980 REMARK 3 T TENSOR REMARK 3 T11: 0.2051 T22: 0.5807 REMARK 3 T33: 0.1792 T12: -0.0426 REMARK 3 T13: 0.1071 T23: 0.0844 REMARK 3 L TENSOR REMARK 3 L11: 0.6456 L22: 0.9255 REMARK 3 L33: 0.4967 L12: 0.3225 REMARK 3 L13: 0.3893 L23: 0.2596 REMARK 3 S TENSOR REMARK 3 S11: 0.0115 S12: -0.8087 S13: -0.1287 REMARK 3 S21: 0.4731 S22: -0.1987 S23: 0.1387 REMARK 3 S31: 0.2051 S32: -0.3330 S33: 0.0030 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: chain 'B' and (resseq 5:18) REMARK 3 ORIGIN FOR THE GROUP (A): 5.3099 17.7433 77.1581 REMARK 3 T TENSOR REMARK 3 T11: 0.2242 T22: 0.1443 REMARK 3 T33: 0.1858 T12: -0.0048 REMARK 3 T13: 0.0305 T23: -0.0467 REMARK 3 L TENSOR REMARK 3 L11: 0.7953 L22: 0.3993 REMARK 3 L33: 0.4034 L12: -0.1343 REMARK 3 L13: -0.0152 L23: -0.0197 REMARK 3 S TENSOR REMARK 3 S11: 0.0297 S12: -0.0926 S13: 0.1125 REMARK 3 S21: 0.2209 S22: -0.0910 S23: 0.1439 REMARK 3 S31: -0.0620 S32: -0.0539 S33: 0.0288 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: chain 'B' and (resseq 19:41) REMARK 3 ORIGIN FOR THE GROUP (A): -3.7325 15.7987 69.4853 REMARK 3 T TENSOR REMARK 3 T11: 0.1324 T22: 0.2669 REMARK 3 T33: 0.2947 T12: 0.0150 REMARK 3 T13: 0.0379 T23: -0.0611 REMARK 3 L TENSOR REMARK 3 L11: 0.1951 L22: 1.0093 REMARK 3 L33: 0.7230 L12: 0.0998 REMARK 3 L13: -0.2320 L23: -0.0853 REMARK 3 S TENSOR REMARK 3 S11: 0.0989 S12: 0.1772 S13: 0.0155 REMARK 3 S21: 0.1206 S22: -0.1505 S23: 0.4703 REMARK 3 S31: -0.0681 S32: -0.4823 S33: 0.0604 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: chain 'B' and (resseq 42:71) REMARK 3 ORIGIN FOR THE GROUP (A): 11.9252 15.5890 52.8251 REMARK 3 T TENSOR REMARK 3 T11: 0.2196 T22: 0.2863 REMARK 3 T33: 0.1026 T12: 0.0571 REMARK 3 T13: 0.0294 T23: -0.0229 REMARK 3 L TENSOR REMARK 3 L11: 0.4095 L22: 0.3207 REMARK 3 L33: 0.1732 L12: 0.2265 REMARK 3 L13: 0.1359 L23: 0.2321 REMARK 3 S TENSOR REMARK 3 S11: -0.1167 S12: 0.4963 S13: 0.0720 REMARK 3 S21: -0.1565 S22: 0.1528 S23: -0.0890 REMARK 3 S31: -0.2028 S32: 0.1260 S33: -0.0379 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: chain 'B' and (resseq 72:150) REMARK 3 ORIGIN FOR THE GROUP (A): 9.3669 13.0311 67.4689 REMARK 3 T TENSOR REMARK 3 T11: 0.1634 T22: 0.1416 REMARK 3 T33: 0.1552 T12: 0.0019 REMARK 3 T13: 0.0249 T23: -0.0255 REMARK 3 L TENSOR REMARK 3 L11: 0.6048 L22: 0.7493 REMARK 3 L33: 0.7702 L12: -0.2974 REMARK 3 L13: -0.1350 L23: 0.3205 REMARK 3 S TENSOR REMARK 3 S11: -0.0095 S12: 0.0650 S13: -0.0873 REMARK 3 S21: 0.0422 S22: -0.0431 S23: 0.0604 REMARK 3 S31: 0.0095 S32: 0.0018 S33: 0.0156 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: chain 'B' and (resseq 151:182) REMARK 3 ORIGIN FOR THE GROUP (A): 1.9312 5.9726 53.5137 REMARK 3 T TENSOR REMARK 3 T11: 0.2788 T22: 0.4085 REMARK 3 T33: 0.2926 T12: -0.0383 REMARK 3 T13: 0.0622 T23: -0.1544 REMARK 3 L TENSOR REMARK 3 L11: 0.5237 L22: 0.3699 REMARK 3 L33: 0.3705 L12: -0.0788 REMARK 3 L13: 0.2538 L23: -0.3235 REMARK 3 S TENSOR REMARK 3 S11: -0.2338 S12: 0.3464 S13: -0.2324 REMARK 3 S21: 0.0818 S22: -0.2273 S23: 0.2848 REMARK 3 S31: 0.1395 S32: -0.4121 S33: 0.0768 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: chain 'B' and (resseq 183:197) REMARK 3 ORIGIN FOR THE GROUP (A): 10.1213 1.1329 44.1097 REMARK 3 T TENSOR REMARK 3 T11: 0.3428 T22: 0.6506 REMARK 3 T33: 0.2108 T12: 0.0277 REMARK 3 T13: 0.0300 T23: -0.2268 REMARK 3 L TENSOR REMARK 3 L11: 0.3812 L22: 0.6069 REMARK 3 L33: 0.0289 L12: -0.2537 REMARK 3 L13: 0.0052 L23: -0.1021 REMARK 3 S TENSOR REMARK 3 S11: 0.0626 S12: -0.0563 S13: -0.1421 REMARK 3 S21: 0.1714 S22: -0.0175 S23: 0.2155 REMARK 3 S31: 0.2963 S32: 0.1258 S33: 0.0654 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: chain 'B' and (resseq 198:217) REMARK 3 ORIGIN FOR THE GROUP (A): 2.4817 16.7135 43.7065 REMARK 3 T TENSOR REMARK 3 T11: 0.4869 T22: 0.6861 REMARK 3 T33: 0.1610 T12: 0.0979 REMARK 3 T13: -0.1306 T23: -0.0422 REMARK 3 L TENSOR REMARK 3 L11: 0.4020 L22: 0.2620 REMARK 3 L33: 0.0128 L12: -0.0528 REMARK 3 L13: -0.0304 L23: -0.0206 REMARK 3 S TENSOR REMARK 3 S11: -0.0191 S12: 0.6027 S13: 0.0824 REMARK 3 S21: -0.3062 S22: -0.1530 S23: 0.0963 REMARK 3 S31: -0.1916 S32: -0.1545 S33: 0.0413 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: chain 'C' REMARK 3 ORIGIN FOR THE GROUP (A): 16.2698 -2.6786 65.9996 REMARK 3 T TENSOR REMARK 3 T11: 0.4442 T22: 0.3396 REMARK 3 T33: 0.2877 T12: 0.0785 REMARK 3 T13: 0.0012 T23: -0.0165 REMARK 3 L TENSOR REMARK 3 L11: 0.0709 L22: 0.5468 REMARK 3 L33: 0.8408 L12: -0.1590 REMARK 3 L13: -0.1285 L23: -0.0943 REMARK 3 S TENSOR REMARK 3 S11: 0.0285 S12: 0.3070 S13: -0.2900 REMARK 3 S21: -0.1424 S22: -0.3033 S23: 0.1548 REMARK 3 S31: 0.1992 S32: 0.1124 S33: 0.1142 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: chain 'D' REMARK 3 ORIGIN FOR THE GROUP (A): 21.6497 10.3830 13.4934 REMARK 3 T TENSOR REMARK 3 T11: 1.4381 T22: 1.0847 REMARK 3 T33: 0.8295 T12: -0.2622 REMARK 3 T13: -0.0064 T23: -0.2711 REMARK 3 L TENSOR REMARK 3 L11: 0.1714 L22: 0.2988 REMARK 3 L33: 0.7235 L12: 0.0638 REMARK 3 L13: -0.1997 L23: 0.2828 REMARK 3 S TENSOR REMARK 3 S11: -0.0126 S12: -0.0108 S13: 0.0605 REMARK 3 S21: -0.0343 S22: -0.0241 S23: -0.0272 REMARK 3 S31: -0.0556 S32: 0.0010 S33: 0.0135 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 4LJR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-13. REMARK 100 THE RCSB ID CODE IS RCSB080716. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-NOV-11 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.2 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-17A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36291 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 40.510 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 83.6 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASES REMARK 200 STARTING MODEL: PDB ENTRY 4LJL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 100 MM NAAC, PH 5.2, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 20.25500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 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: 3050 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20330 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LEU A 218 REMARK 465 GLU A 219 REMARK 465 HIS A 220 REMARK 465 HIS A 221 REMARK 465 HIS A 222 REMARK 465 HIS A 223 REMARK 465 HIS A 224 REMARK 465 HIS A 225 REMARK 465 LEU B 218 REMARK 465 GLU B 219 REMARK 465 HIS B 220 REMARK 465 HIS B 221 REMARK 465 HIS B 222 REMARK 465 HIS B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 DT C 7 REMARK 465 DT C 8 REMARK 465 DT C 9 REMARK 465 DT C 10 REMARK 465 DT C 11 REMARK 465 DT C 12 REMARK 465 DT C 13 REMARK 465 DT C 14 REMARK 465 DT C 15 REMARK 465 DT C 16 REMARK 465 DT C 17 REMARK 465 DT C 18 REMARK 465 DT C 19 REMARK 465 DT C 20 REMARK 465 DT C 21 REMARK 465 DT C 22 REMARK 465 DT C 23 REMARK 465 DT C 24 REMARK 465 DT C 25 REMARK 465 DT C 26 REMARK 465 DT C 27 REMARK 465 DT C 28 REMARK 465 DT C 29 REMARK 465 DT C 30 REMARK 465 DT C 31 REMARK 465 DT C 32 REMARK 465 DT C 33 REMARK 465 DT C 34 REMARK 465 DT C 35 REMARK 465 DT D 6 REMARK 465 DT D 7 REMARK 465 DT D 8 REMARK 465 DT D 9 REMARK 465 DT D 10 REMARK 465 DT D 11 REMARK 465 DT D 12 REMARK 465 DT D 13 REMARK 465 DT D 14 REMARK 465 DT D 15 REMARK 465 DT D 16 REMARK 465 DT D 17 REMARK 465 DT D 18 REMARK 465 DT D 19 REMARK 465 DT D 20 REMARK 465 DT D 21 REMARK 465 DT D 22 REMARK 465 DT D 23 REMARK 465 DT D 24 REMARK 465 DT D 25 REMARK 465 DT D 26 REMARK 465 DT D 27 REMARK 465 DT D 28 REMARK 465 DT D 29 REMARK 465 DT D 30 REMARK 465 DT D 31 REMARK 465 DT D 32 REMARK 465 DT D 33 REMARK 465 DT D 34 REMARK 465 DT D 35 REMARK 465 DT D 36 REMARK 465 DT D 37 REMARK 465 DT D 38 REMARK 465 DT D 39 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 461 O HOH A 467 1.87 REMARK 500 O HOH A 481 O HOH A 489 1.93 REMARK 500 O HOH A 445 O HOH A 448 2.03 REMARK 500 O HOH B 408 O HOH B 436 2.05 REMARK 500 O HOH B 446 O HOH B 454 2.09 REMARK 500 O HOH A 375 O HOH A 404 2.09 REMARK 500 O HOH A 453 O HOH A 465 2.12 REMARK 500 O HOH A 347 O HOH A 396 2.16 REMARK 500 O HOH A 344 O HOH A 451 2.16 REMARK 500 OD2 ASP A 85 O HOH A 423 2.16 REMARK 500 O HOH B 304 O HOH B 476 2.18 REMARK 500 O HOH A 373 O HOH A 395 2.18 REMARK 500 O LEU A 161 O HOH A 478 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 DT C 1 P DT C 1 OP3 -0.128 REMARK 500 REMARK 500 REMARK: NULL 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 DT C 2 O4' - C4' - C3' ANGL. DEV. = -3.4 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 12 -155.40 -126.96 REMARK 500 ASP A 132 28.52 48.52 REMARK 500 ASN A 187 8.03 58.16 REMARK 500 LYS A 216 26.99 -77.60 REMARK 500 SER B 12 -158.86 -129.11 REMARK 500 LYS B 162 61.26 37.76 REMARK 500 ASN B 187 30.07 76.50 REMARK 500 SER B 189 70.62 -155.78 REMARK 500 ASN B 206 111.96 -160.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 411 DISTANCE = 6.23 ANGSTROMS REMARK 525 HOH A 444 DISTANCE = 6.49 ANGSTROMS REMARK 525 HOH A 460 DISTANCE = 5.61 ANGSTROMS REMARK 525 HOH B 406 DISTANCE = 6.18 ANGSTROMS REMARK 525 HOH B 424 DISTANCE = 5.77 ANGSTROMS REMARK 525 HOH B 438 DISTANCE = 7.33 ANGSTROMS REMARK 525 HOH B 477 DISTANCE = 7.96 ANGSTROMS REMARK 525 HOH C 110 DISTANCE = 7.35 ANGSTROMS REMARK 525 HOH C 112 DISTANCE = 6.30 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4LJK RELATED DB: PDB REMARK 900 RELATED ID: 4LJL RELATED DB: PDB DBREF 4LJR A 5 217 UNP O25100 O25100_HELPY 5 217 DBREF 4LJR B 5 217 UNP O25100 O25100_HELPY 5 217 DBREF 4LJR C 1 35 PDB 4LJR 4LJR 1 35 DBREF 4LJR D 5 39 PDB 4LJR 4LJR 5 39 SEQADV 4LJR LEU A 218 UNP O25100 EXPRESSION TAG SEQADV 4LJR GLU A 219 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS A 220 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS A 221 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS A 222 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS A 223 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS A 224 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS A 225 UNP O25100 EXPRESSION TAG SEQADV 4LJR LEU B 218 UNP O25100 EXPRESSION TAG SEQADV 4LJR GLU B 219 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS B 220 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS B 221 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS B 222 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS B 223 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS B 224 UNP O25100 EXPRESSION TAG SEQADV 4LJR HIS B 225 UNP O25100 EXPRESSION TAG SEQRES 1 A 221 MET LYS SER HIS PHE GLN TYR SER THR LEU GLU ASN ILE SEQRES 2 A 221 PRO LYS ALA PHE ASP ILE LEU LYS ASP PRO PRO LYS LYS SEQRES 3 A 221 LEU TYR CYS VAL GLY ASP THR LYS LEU LEU ASP THR PRO SEQRES 4 A 221 LEU LYS VAL ALA ILE ILE GLY THR ARG ARG PRO THR PRO SEQRES 5 A 221 TYR SER LYS GLN HIS THR ILE THR LEU ALA ARG GLU LEU SEQRES 6 A 221 ALA LYS ASN GLY ALA VAL ILE VAL SER GLY GLY ALA LEU SEQRES 7 A 221 GLY VAL ASP ILE ILE ALA GLN GLU ASN ALA LEU PRO LYS SEQRES 8 A 221 THR ILE MET LEU SER PRO CYS SER LEU ASP PHE ILE TYR SEQRES 9 A 221 PRO THR ASN ASN HIS LYS VAL ILE GLN GLU ILE ALA GLN SEQRES 10 A 221 ASN GLY LEU ILE LEU SER GLU TYR GLU LYS ASP PHE MET SEQRES 11 A 221 PRO ILE LYS GLY SER PHE LEU ALA ARG ASN ARG LEU VAL SEQRES 12 A 221 ILE ALA LEU SER ASP VAL VAL ILE ILE PRO GLN ALA ASP SEQRES 13 A 221 LEU LYS SER GLY SER MET SER SER ALA ARG LEU ALA GLN SEQRES 14 A 221 LYS TYR GLN LYS PRO LEU PHE VAL LEU PRO GLN ARG LEU SEQRES 15 A 221 ASN GLU SER ASP GLY THR ASN GLU LEU LEU GLU LYS GLY SEQRES 16 A 221 GLN ALA GLN GLY ILE PHE ASN ILE GLN ASN PHE ILE ASN SEQRES 17 A 221 THR LEU LEU LYS ASP LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 1 B 221 MET LYS SER HIS PHE GLN TYR SER THR LEU GLU ASN ILE SEQRES 2 B 221 PRO LYS ALA PHE ASP ILE LEU LYS ASP PRO PRO LYS LYS SEQRES 3 B 221 LEU TYR CYS VAL GLY ASP THR LYS LEU LEU ASP THR PRO SEQRES 4 B 221 LEU LYS VAL ALA ILE ILE GLY THR ARG ARG PRO THR PRO SEQRES 5 B 221 TYR SER LYS GLN HIS THR ILE THR LEU ALA ARG GLU LEU SEQRES 6 B 221 ALA LYS ASN GLY ALA VAL ILE VAL SER GLY GLY ALA LEU SEQRES 7 B 221 GLY VAL ASP ILE ILE ALA GLN GLU ASN ALA LEU PRO LYS SEQRES 8 B 221 THR ILE MET LEU SER PRO CYS SER LEU ASP PHE ILE TYR SEQRES 9 B 221 PRO THR ASN ASN HIS LYS VAL ILE GLN GLU ILE ALA GLN SEQRES 10 B 221 ASN GLY LEU ILE LEU SER GLU TYR GLU LYS ASP PHE MET SEQRES 11 B 221 PRO ILE LYS GLY SER PHE LEU ALA ARG ASN ARG LEU VAL SEQRES 12 B 221 ILE ALA LEU SER ASP VAL VAL ILE ILE PRO GLN ALA ASP SEQRES 13 B 221 LEU LYS SER GLY SER MET SER SER ALA ARG LEU ALA GLN SEQRES 14 B 221 LYS TYR GLN LYS PRO LEU PHE VAL LEU PRO GLN ARG LEU SEQRES 15 B 221 ASN GLU SER ASP GLY THR ASN GLU LEU LEU GLU LYS GLY SEQRES 16 B 221 GLN ALA GLN GLY ILE PHE ASN ILE GLN ASN PHE ILE ASN SEQRES 17 B 221 THR LEU LEU LYS ASP LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 1 C 35 DT DT DT DT DT DT DT DT DT DT DT DT DT SEQRES 2 C 35 DT DT DT DT DT DT DT DT DT DT DT DT DT SEQRES 3 C 35 DT DT DT DT DT DT DT DT DT SEQRES 1 D 35 DT DT DT DT DT DT DT DT DT DT DT DT DT SEQRES 2 D 35 DT DT DT DT DT DT DT DT DT DT DT DT DT SEQRES 3 D 35 DT DT DT DT DT DT DT DT DT FORMUL 5 HOH *385(H2 O) HELIX 1 1 PRO A 18 LEU A 24 5 7 HELIX 2 2 THR A 37 THR A 42 5 6 HELIX 3 3 THR A 55 ASN A 72 1 18 HELIX 4 4 GLY A 83 LEU A 93 1 11 HELIX 5 5 PRO A 109 ASN A 111 5 3 HELIX 6 6 ASN A 112 GLY A 123 1 12 HELIX 7 7 ILE A 136 SER A 151 1 16 HELIX 8 8 SER A 163 TYR A 175 1 13 HELIX 9 9 SER A 189 LYS A 198 1 10 HELIX 10 10 ASN A 206 LYS A 216 1 11 HELIX 11 11 PRO B 18 LEU B 24 5 7 HELIX 12 12 THR B 37 THR B 42 5 6 HELIX 13 13 THR B 55 ASN B 72 1 18 HELIX 14 14 GLY B 83 LEU B 93 1 11 HELIX 15 15 PRO B 109 ASN B 111 5 3 HELIX 16 16 ASN B 112 GLY B 123 1 12 HELIX 17 17 ILE B 136 SER B 151 1 16 HELIX 18 18 SER B 163 TYR B 175 1 13 HELIX 19 19 SER B 189 LYS B 198 1 10 HELIX 20 20 ASN B 206 ASP B 217 1 12 SHEET 1 A 9 SER A 12 THR A 13 0 SHEET 2 A 9 TYR A 32 GLY A 35 -1 O CYS A 33 N SER A 12 SHEET 3 A 9 LEU A 124 SER A 127 -1 O SER A 127 N TYR A 32 SHEET 4 A 9 THR A 96 LEU A 99 1 N MET A 98 O LEU A 126 SHEET 5 A 9 VAL A 75 SER A 78 1 N ILE A 76 O ILE A 97 SHEET 6 A 9 LYS A 45 ILE A 48 1 N VAL A 46 O VAL A 77 SHEET 7 A 9 VAL A 153 ILE A 156 1 O ILE A 155 N ALA A 47 SHEET 8 A 9 LEU A 179 VAL A 181 1 O PHE A 180 N ILE A 156 SHEET 9 A 9 GLN A 202 GLY A 203 1 O GLN A 202 N LEU A 179 SHEET 1 B 9 SER B 12 THR B 13 0 SHEET 2 B 9 TYR B 32 GLY B 35 -1 O CYS B 33 N SER B 12 SHEET 3 B 9 LEU B 124 SER B 127 -1 O SER B 127 N TYR B 32 SHEET 4 B 9 THR B 96 SER B 100 1 N SER B 100 O LEU B 126 SHEET 5 B 9 VAL B 75 SER B 78 1 N ILE B 76 O ILE B 97 SHEET 6 B 9 LYS B 45 ILE B 48 1 N VAL B 46 O VAL B 75 SHEET 7 B 9 VAL B 153 ILE B 156 1 O ILE B 155 N ALA B 47 SHEET 8 B 9 LEU B 179 VAL B 181 1 O PHE B 180 N ILE B 156 SHEET 9 B 9 GLN B 202 GLY B 203 1 O GLN B 202 N VAL B 181 CISPEP 1 LEU A 93 PRO A 94 0 2.59 CISPEP 2 TYR A 108 PRO A 109 0 0.73 CISPEP 3 LEU B 93 PRO B 94 0 2.38 CISPEP 4 TYR B 108 PRO B 109 0 -4.44 CRYST1 37.400 40.510 154.680 90.00 92.18 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.026738 0.000000 0.001018 0.00000 SCALE2 0.000000 0.024685 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006470 0.00000 ATOM 1 N MET A 5 30.898 1.893 6.375 1.00 31.14 N ANISOU 1 N MET A 5 3710 3530 4593 224 -275 251 N ATOM 2 CA MET A 5 31.331 0.512 6.534 1.00 24.19 C ANISOU 2 CA MET A 5 2812 2611 3766 211 -266 284 C ATOM 3 C MET A 5 30.473 -0.438 5.704 1.00 24.86 C ANISOU 3 C MET A 5 2900 2702 3842 231 -224 224 C ATOM 4 O MET A 5 29.243 -0.434 5.803 1.00 18.62 O ANISOU 4 O MET A 5 2129 1951 2995 219 -220 165 O ATOM 5 CB MET A 5 31.282 0.099 8.003 1.00 23.72 C ANISOU 5 CB MET A 5 2760 2549 3702 147 -308 318 C ATOM 6 CG MET A 5 31.872 -1.274 8.262 1.00 23.40 C ANISOU 6 CG MET A 5 2701 2464 3727 130 -307 365 C ATOM 7 SD MET A 5 31.840 -1.759 10.003 1.00 23.90 S ANISOU 7 SD MET A 5 2773 2525 3781 48 -361 413 S ATOM 8 CE MET A 5 32.724 -3.313 9.886 1.00 16.94 C ANISOU 8 CE MET A 5 1862 1578 2996 51 -353 473 C ATOM 9 N LYS A 6 31.129 -1.259 4.892 1.00 20.12 N ANISOU 9 N LYS A 6 2281 2063 3300 262 -191 241 N ATOM 10 CA LYS A 6 30.422 -2.204 4.040 1.00 21.57 C ANISOU 10 CA LYS A 6 2469 2246 3479 281 -149 186 C ATOM 11 C LYS A 6 30.075 -3.448 4.836 1.00 18.55 C ANISOU 11 C LYS A 6 2090 1846 3114 238 -159 193 C ATOM 12 O LYS A 6 30.858 -3.891 5.669 1.00 15.12 O ANISOU 12 O LYS A 6 1643 1376 2727 211 -185 256 O ATOM 13 CB LYS A 6 31.264 -2.557 2.811 1.00 27.55 C ANISOU 13 CB LYS A 6 3215 2984 4267 320 -102 189 C ATOM 14 CG LYS A 6 31.664 -1.335 1.990 1.00 33.35 C ANISOU 14 CG LYS A 6 3958 3756 4959 346 -89 181 C ATOM 15 CD LYS A 6 31.502 -1.563 0.494 1.00 41.98 C ANISOU 15 CD LYS A 6 5057 4860 6033 384 -39 134 C ATOM 16 CE LYS A 6 32.579 -2.480 -0.054 1.00 45.52 C ANISOU 16 CE LYS A 6 5495 5282 6518 388 -5 157 C ATOM 17 NZ LYS A 6 32.391 -2.730 -1.510 1.00 47.82 N ANISOU 17 NZ LYS A 6 5796 5584 6789 423 41 110 N ATOM 18 N SER A 7 28.891 -4.001 4.595 1.00 19.34 N ANISOU 18 N SER A 7 2207 1970 3172 229 -141 130 N ATOM 19 CA SER A 7 28.441 -5.170 5.338 1.00 18.74 C ANISOU 19 CA SER A 7 2136 1879 3105 185 -151 132 C ATOM 20 C SER A 7 28.863 -6.466 4.662 1.00 19.67 C ANISOU 20 C SER A 7 2243 1943 3285 204 -117 137 C ATOM 21 O SER A 7 29.104 -7.473 5.338 1.00 21.31 O ANISOU 21 O SER A 7 2447 2114 3535 172 -131 173 O ATOM 22 CB SER A 7 26.922 -5.164 5.455 1.00 20.13 C ANISOU 22 CB SER A 7 2333 2109 3206 161 -149 63 C ATOM 23 OG SER A 7 26.347 -5.373 4.180 1.00 12.78 O ANISOU 23 OG SER A 7 1407 1189 2258 198 -108 2 O ATOM 24 N HIS A 8 28.951 -6.431 3.333 1.00 18.22 N ANISOU 24 N HIS A 8 2059 1756 3109 254 -73 101 N ATOM 25 CA HIS A 8 29.154 -7.629 2.522 1.00 21.59 C ANISOU 25 CA HIS A 8 2482 2138 3584 276 -31 85 C ATOM 26 C HIS A 8 28.024 -8.643 2.720 1.00 18.04 C ANISOU 26 C HIS A 8 2052 1695 3107 240 -28 40 C ATOM 27 O HIS A 8 28.185 -9.831 2.445 1.00 20.72 O ANISOU 27 O HIS A 8 2391 1987 3494 241 -5 38 O ATOM 28 CB HIS A 8 30.511 -8.269 2.817 1.00 25.22 C ANISOU 28 CB HIS A 8 2916 2530 4137 283 -33 158 C ATOM 29 CG HIS A 8 31.675 -7.370 2.537 1.00 31.94 C ANISOU 29 CG HIS A 8 3753 3403 4979 300 -30 196 C ATOM 30 ND1 HIS A 8 32.401 -6.760 3.536 1.00 34.33 N ANISOU 30 ND1 HIS A 8 4044 3715 5286 272 -73 257 N ATOM 31 CD2 HIS A 8 32.233 -6.973 1.369 1.00 36.10 C ANISOU 31 CD2 HIS A 8 4281 3952 5485 334 9 177 C ATOM 32 CE1 HIS A 8 33.362 -6.031 2.996 1.00 37.13 C ANISOU 32 CE1 HIS A 8 4390 4092 5625 289 -58 273 C ATOM 33 NE2 HIS A 8 33.282 -6.142 1.683 1.00 38.94 N ANISOU 33 NE2 HIS A 8 4628 4329 5840 327 -10 227 N ATOM 34 N PHE A 9 26.875 -8.167 3.193 1.00 16.63 N ANISOU 34 N PHE A 9 1890 1574 2855 209 -49 2 N ATOM 35 CA PHE A 9 25.709 -9.027 3.368 1.00 13.08 C ANISOU 35 CA PHE A 9 1458 1141 2373 173 -47 -43 C ATOM 36 C PHE A 9 25.153 -9.465 2.015 1.00 18.13 C ANISOU 36 C PHE A 9 2108 1784 2996 203 -1 -110 C ATOM 37 O PHE A 9 25.138 -8.690 1.061 1.00 17.61 O ANISOU 37 O PHE A 9 2042 1743 2904 243 21 -140 O ATOM 38 CB PHE A 9 24.590 -8.295 4.123 1.00 15.38 C ANISOU 38 CB PHE A 9 1759 1499 2585 136 -76 -71 C ATOM 39 CG PHE A 9 24.901 -7.983 5.561 1.00 21.87 C ANISOU 39 CG PHE A 9 2577 2325 3408 93 -122 -16 C ATOM 40 CD1 PHE A 9 25.889 -8.666 6.245 1.00 21.82 C ANISOU 40 CD1 PHE A 9 2560 2262 3467 73 -141 54 C ATOM 41 CD2 PHE A 9 24.186 -6.999 6.229 1.00 19.10 C ANISOU 41 CD2 PHE A 9 2233 2033 2991 70 -146 -35 C ATOM 42 CE1 PHE A 9 26.166 -8.372 7.570 1.00 20.80 C ANISOU 42 CE1 PHE A 9 2430 2139 3334 27 -186 106 C ATOM 43 CE2 PHE A 9 24.456 -6.696 7.554 1.00 19.58 C ANISOU 43 CE2 PHE A 9 2294 2099 3046 26 -187 12 C ATOM 44 CZ PHE A 9 25.448 -7.384 8.224 1.00 19.40 C ANISOU 44 CZ PHE A 9 2264 2024 3085 2 -208 84 C ATOM 45 N GLN A 10 24.692 -10.709 1.933 1.00 17.25 N ANISOU 45 N GLN A 10 2007 1647 2898 180 13 -133 N ATOM 46 CA GLN A 10 23.952 -11.157 0.763 1.00 20.90 C ANISOU 46 CA GLN A 10 2486 2121 3333 196 51 -202 C ATOM 47 C GLN A 10 22.476 -11.032 1.092 1.00 18.67 C ANISOU 47 C GLN A 10 2216 1903 2975 157 34 -251 C ATOM 48 O GLN A 10 21.949 -11.846 1.837 1.00 18.16 O ANISOU 48 O GLN A 10 2159 1833 2910 110 17 -249 O ATOM 49 CB GLN A 10 24.282 -12.613 0.413 1.00 26.47 C ANISOU 49 CB GLN A 10 3198 2759 4099 194 78 -204 C ATOM 50 CG GLN A 10 25.689 -12.848 -0.134 1.00 31.83 C ANISOU 50 CG GLN A 10 3862 3373 4857 240 107 -167 C ATOM 51 CD GLN A 10 25.894 -14.278 -0.624 1.00 42.19 C ANISOU 51 CD GLN A 10 5184 4618 6226 243 142 -182 C ATOM 52 OE1 GLN A 10 24.935 -14.984 -0.953 1.00 43.39 O ANISOU 52 OE1 GLN A 10 5359 4778 6347 219 153 -236 O ATOM 53 NE2 GLN A 10 27.149 -14.710 -0.673 1.00 46.22 N ANISOU 53 NE2 GLN A 10 5677 5061 6824 271 158 -134 N ATOM 54 N TYR A 11 21.812 -10.014 0.551 1.00 13.11 N ANISOU 54 N TYR A 11 1514 1260 2209 176 36 -293 N ATOM 55 CA TYR A 11 20.426 -9.771 0.926 1.00 17.47 C ANISOU 55 CA TYR A 11 2071 1877 2691 142 19 -336 C ATOM 56 C TYR A 11 19.452 -9.880 -0.237 1.00 10.80 C ANISOU 56 C TYR A 11 1237 1067 1800 155 44 -406 C ATOM 57 O TYR A 11 19.823 -9.714 -1.401 1.00 14.07 O ANISOU 57 O TYR A 11 1655 1471 2219 196 73 -424 O ATOM 58 CB TYR A 11 20.274 -8.425 1.640 1.00 12.51 C ANISOU 58 CB TYR A 11 1431 1296 2024 143 -12 -322 C ATOM 59 CG TYR A 11 20.685 -7.229 0.816 1.00 12.50 C ANISOU 59 CG TYR A 11 1425 1312 2013 196 -2 -326 C ATOM 60 CD1 TYR A 11 21.988 -6.756 0.858 1.00 15.92 C ANISOU 60 CD1 TYR A 11 1850 1708 2492 224 -4 -273 C ATOM 61 CD2 TYR A 11 19.770 -6.570 0.013 1.00 15.79 C ANISOU 61 CD2 TYR A 11 1844 1783 2374 216 6 -380 C ATOM 62 CE1 TYR A 11 22.377 -5.663 0.115 1.00 17.87 C ANISOU 62 CE1 TYR A 11 2092 1970 2729 269 3 -274 C ATOM 63 CE2 TYR A 11 20.146 -5.476 -0.751 1.00 18.73 C ANISOU 63 CE2 TYR A 11 2213 2169 2736 262 12 -380 C ATOM 64 CZ TYR A 11 21.454 -5.024 -0.686 1.00 21.50 C ANISOU 64 CZ TYR A 11 2557 2482 3132 288 11 -327 C ATOM 65 OH TYR A 11 21.857 -3.936 -1.422 1.00 24.33 O ANISOU 65 OH TYR A 11 2912 2853 3481 330 16 -324 O ATOM 66 N SER A 12 18.202 -10.151 0.113 1.00 12.04 N ANISOU 66 N SER A 12 1397 1268 1909 115 32 -443 N ATOM 67 CA SER A 12 17.109 -10.304 -0.833 1.00 10.90 C ANISOU 67 CA SER A 12 1261 1165 1716 114 48 -508 C ATOM 68 C SER A 12 15.943 -9.381 -0.441 1.00 13.20 C ANISOU 68 C SER A 12 1539 1535 1941 102 25 -536 C ATOM 69 O SER A 12 16.139 -8.358 0.224 1.00 14.83 O ANISOU 69 O SER A 12 1733 1763 2139 111 4 -512 O ATOM 70 CB SER A 12 16.648 -11.760 -0.809 1.00 22.40 C ANISOU 70 CB SER A 12 2732 2595 3185 72 57 -527 C ATOM 71 OG SER A 12 15.786 -12.058 -1.883 1.00 23.18 O ANISOU 71 OG SER A 12 2841 2721 3245 73 77 -587 O ATOM 72 N THR A 13 14.731 -9.742 -0.859 1.00 18.37 N ANISOU 72 N THR A 13 2195 2232 2551 80 29 -588 N ATOM 73 CA THR A 13 13.519 -9.029 -0.458 1.00 20.74 C ANISOU 73 CA THR A 13 2480 2607 2794 64 9 -618 C ATOM 74 C THR A 13 12.531 -9.988 0.192 1.00 17.28 C ANISOU 74 C THR A 13 2040 2187 2336 3 1 -637 C ATOM 75 O THR A 13 12.531 -11.185 -0.099 1.00 22.39 O ANISOU 75 O THR A 13 2705 2800 3004 -22 14 -645 O ATOM 76 CB THR A 13 12.794 -8.379 -1.661 1.00 21.38 C ANISOU 76 CB THR A 13 2556 2737 2830 96 17 -665 C ATOM 77 OG1 THR A 13 12.583 -9.360 -2.677 1.00 18.99 O ANISOU 77 OG1 THR A 13 2271 2418 2528 88 40 -697 O ATOM 78 CG2 THR A 13 13.602 -7.242 -2.250 1.00 24.82 C ANISOU 78 CG2 THR A 13 2990 3166 3275 153 21 -647 C ATOM 79 N LEU A 14 11.681 -9.454 1.065 1.00 21.76 N ANISOU 79 N LEU A 14 2590 2811 2865 -22 -18 -646 N ATOM 80 CA LEU A 14 10.581 -10.223 1.628 1.00 19.07 C ANISOU 80 CA LEU A 14 2245 2504 2498 -80 -25 -669 C ATOM 81 C LEU A 14 9.559 -10.483 0.534 1.00 18.99 C ANISOU 81 C LEU A 14 2232 2532 2452 -79 -14 -724 C ATOM 82 O LEU A 14 9.286 -9.610 -0.289 1.00 21.44 O ANISOU 82 O LEU A 14 2532 2876 2738 -38 -11 -749 O ATOM 83 CB LEU A 14 9.917 -9.471 2.781 1.00 18.69 C ANISOU 83 CB LEU A 14 2174 2513 2414 -103 -44 -669 C ATOM 84 CG LEU A 14 10.721 -9.340 4.072 1.00 16.79 C ANISOU 84 CG LEU A 14 1938 2245 2197 -123 -60 -616 C ATOM 85 CD1 LEU A 14 9.949 -8.488 5.085 1.00 13.45 C ANISOU 85 CD1 LEU A 14 1494 1886 1729 -143 -73 -628 C ATOM 86 CD2 LEU A 14 11.019 -10.713 4.644 1.00 19.72 C ANISOU 86 CD2 LEU A 14 2325 2569 2599 -176 -63 -586 C ATOM 87 N GLU A 15 8.998 -11.686 0.524 1.00 21.82 N ANISOU 87 N GLU A 15 2599 2883 2807 -128 -11 -741 N ATOM 88 CA GLU A 15 7.981 -12.035 -0.453 1.00 26.18 C ANISOU 88 CA GLU A 15 3150 3472 3324 -137 -3 -793 C ATOM 89 C GLU A 15 6.697 -11.271 -0.168 1.00 28.00 C ANISOU 89 C GLU A 15 3348 3790 3502 -147 -18 -823 C ATOM 90 O GLU A 15 6.040 -10.775 -1.084 1.00 29.50 O ANISOU 90 O GLU A 15 3526 4024 3659 -124 -17 -859 O ATOM 91 CB GLU A 15 7.715 -13.534 -0.428 1.00 31.10 C ANISOU 91 CB GLU A 15 3794 4063 3960 -192 2 -801 C ATOM 92 CG GLU A 15 6.655 -13.976 -1.415 1.00 36.27 C ANISOU 92 CG GLU A 15 4449 4754 4576 -210 7 -854 C ATOM 93 CD GLU A 15 6.508 -15.475 -1.465 1.00 38.69 C ANISOU 93 CD GLU A 15 4782 5019 4901 -263 14 -862 C ATOM 94 OE1 GLU A 15 6.008 -15.985 -2.488 1.00 42.33 O ANISOU 94 OE1 GLU A 15 5257 5485 5342 -271 23 -903 O ATOM 95 OE2 GLU A 15 6.895 -16.142 -0.482 1.00 39.39 O ANISOU 95 OE2 GLU A 15 4878 5067 5021 -297 7 -827 O ATOM 96 N ASN A 16 6.352 -11.177 1.112 1.00 26.88 N ANISOU 96 N ASN A 16 3190 3673 3350 -182 -31 -808 N ATOM 97 CA ASN A 16 5.184 -10.423 1.532 1.00 27.89 C ANISOU 97 CA ASN A 16 3282 3882 3432 -191 -40 -836 C ATOM 98 C ASN A 16 5.524 -9.390 2.608 1.00 24.26 C ANISOU 98 C ASN A 16 2809 3436 2972 -176 -49 -811 C ATOM 99 O ASN A 16 6.319 -9.663 3.509 1.00 23.71 O ANISOU 99 O ASN A 16 2754 3325 2928 -196 -53 -770 O ATOM 100 CB ASN A 16 4.096 -11.376 2.038 1.00 32.22 C ANISOU 100 CB ASN A 16 3821 4466 3956 -260 -44 -855 C ATOM 101 CG ASN A 16 3.695 -12.410 0.999 1.00 36.88 C ANISOU 101 CG ASN A 16 4426 5044 4543 -281 -37 -883 C ATOM 102 OD1 ASN A 16 2.945 -12.111 0.067 1.00 34.47 O ANISOU 102 OD1 ASN A 16 4107 4782 4209 -264 -37 -920 O ATOM 103 ND2 ASN A 16 4.191 -13.635 1.157 1.00 37.40 N ANISOU 103 ND2 ASN A 16 4522 5049 4640 -318 -33 -864 N ATOM 104 N ILE A 17 4.925 -8.205 2.505 1.00 22.06 N ANISOU 104 N ILE A 17 2502 3213 2665 -142 -53 -834 N ATOM 105 CA ILE A 17 5.031 -7.216 3.566 1.00 22.75 C ANISOU 105 CA ILE A 17 2576 3321 2746 -133 -60 -821 C ATOM 106 C ILE A 17 4.224 -7.716 4.757 1.00 22.63 C ANISOU 106 C ILE A 17 2546 3346 2706 -199 -61 -828 C ATOM 107 O ILE A 17 3.054 -8.068 4.609 1.00 23.59 O ANISOU 107 O ILE A 17 2645 3521 2799 -226 -59 -863 O ATOM 108 CB ILE A 17 4.462 -5.848 3.146 1.00 21.39 C ANISOU 108 CB ILE A 17 2376 3200 2552 -81 -62 -850 C ATOM 109 CG1 ILE A 17 4.981 -5.430 1.770 1.00 24.62 C ANISOU 109 CG1 ILE A 17 2796 3583 2976 -23 -61 -851 C ATOM 110 CG2 ILE A 17 4.775 -4.787 4.205 1.00 17.67 C ANISOU 110 CG2 ILE A 17 1898 2736 2079 -68 -67 -835 C ATOM 111 CD1 ILE A 17 6.483 -5.276 1.692 1.00 29.84 C ANISOU 111 CD1 ILE A 17 3487 4173 3676 6 -60 -807 C ATOM 112 N PRO A 18 4.844 -7.761 5.945 1.00 23.30 N ANISOU 112 N PRO A 18 2644 3409 2801 -227 -67 -792 N ATOM 113 CA PRO A 18 4.115 -8.183 7.147 1.00 24.74 C ANISOU 113 CA PRO A 18 2813 3632 2954 -293 -68 -795 C ATOM 114 C PRO A 18 2.864 -7.339 7.365 1.00 23.81 C ANISOU 114 C PRO A 18 2656 3597 2794 -287 -61 -842 C ATOM 115 O PRO A 18 2.911 -6.117 7.227 1.00 24.04 O ANISOU 115 O PRO A 18 2673 3640 2821 -233 -59 -852 O ATOM 116 CB PRO A 18 5.119 -7.925 8.272 1.00 25.82 C ANISOU 116 CB PRO A 18 2971 3734 3107 -307 -77 -749 C ATOM 117 CG PRO A 18 6.453 -7.996 7.609 1.00 24.32 C ANISOU 117 CG PRO A 18 2808 3467 2965 -267 -82 -712 C ATOM 118 CD PRO A 18 6.251 -7.433 6.235 1.00 22.28 C ANISOU 118 CD PRO A 18 2540 3217 2708 -204 -73 -744 C ATOM 119 N LYS A 19 1.758 -7.997 7.699 1.00 23.53 N ANISOU 119 N LYS A 19 2554 3136 3250 -490 61 -639 N ATOM 120 CA LYS A 19 0.482 -7.318 7.916 1.00 26.76 C ANISOU 120 CA LYS A 19 2853 3733 3581 -465 26 -672 C ATOM 121 C LYS A 19 0.544 -6.251 9.016 1.00 20.44 C ANISOU 121 C LYS A 19 2038 2906 2821 -375 1 -607 C ATOM 122 O LYS A 19 -0.283 -5.341 9.039 1.00 25.13 O ANISOU 122 O LYS A 19 2552 3641 3357 -300 -32 -609 O ATOM 123 CB LYS A 19 -0.621 -8.333 8.239 1.00 36.04 C ANISOU 123 CB LYS A 19 3983 5018 4695 -618 42 -766 C ATOM 124 CG LYS A 19 -1.554 -8.679 7.080 1.00 45.30 C ANISOU 124 CG LYS A 19 5081 6373 5758 -663 36 -852 C ATOM 125 CD LYS A 19 -0.872 -9.540 6.033 1.00 50.86 C ANISOU 125 CD LYS A 19 5859 6996 6471 -713 68 -871 C ATOM 126 CE LYS A 19 -1.884 -10.383 5.260 1.00 55.01 C ANISOU 126 CE LYS A 19 6327 7682 6893 -834 80 -980 C ATOM 127 NZ LYS A 19 -2.951 -9.570 4.605 1.00 58.08 N ANISOU 127 NZ LYS A 19 6586 8304 7178 -762 34 -1016 N ATOM 128 N ALA A 20 1.519 -6.351 9.918 1.00 17.82 N ANISOU 128 N ALA A 20 1786 2399 2586 -379 18 -549 N ATOM 129 CA ALA A 20 1.627 -5.380 11.008 1.00 16.71 C ANISOU 129 CA ALA A 20 1639 2224 2487 -305 -3 -489 C ATOM 130 C ALA A 20 1.769 -3.968 10.446 1.00 17.26 C ANISOU 130 C ALA A 20 1686 2335 2539 -148 -32 -437 C ATOM 131 O ALA A 20 1.345 -2.994 11.063 1.00 20.46 O ANISOU 131 O ALA A 20 2052 2790 2930 -75 -55 -409 O ATOM 132 CB ALA A 20 2.812 -5.718 11.933 1.00 17.88 C ANISOU 132 CB ALA A 20 1880 2172 2741 -327 20 -434 C ATOM 133 N PHE A 21 2.353 -3.866 9.255 1.00 14.74 N ANISOU 133 N PHE A 21 1395 1992 2216 -97 -26 -425 N ATOM 134 CA PHE A 21 2.603 -2.569 8.639 1.00 14.95 C ANISOU 134 CA PHE A 21 1418 2037 2226 51 -45 -373 C ATOM 135 C PHE A 21 1.364 -1.965 7.982 1.00 17.53 C ANISOU 135 C PHE A 21 1653 2568 2439 115 -73 -411 C ATOM 136 O PHE A 21 1.368 -0.792 7.599 1.00 20.86 O ANISOU 136 O PHE A 21 2070 3024 2832 248 -88 -369 O ATOM 137 CB PHE A 21 3.746 -2.686 7.637 1.00 16.90 C ANISOU 137 CB PHE A 21 1734 2174 2512 83 -25 -343 C ATOM 138 CG PHE A 21 5.064 -3.043 8.276 1.00 15.68 C ANISOU 138 CG PHE A 21 1666 1825 2467 52 0 -294 C ATOM 139 CD1 PHE A 21 5.476 -2.410 9.433 1.00 20.43 C ANISOU 139 CD1 PHE A 21 2289 2346 3127 84 -5 -239 C ATOM 140 CD2 PHE A 21 5.876 -4.015 7.728 1.00 22.69 C ANISOU 140 CD2 PHE A 21 2612 2617 3392 -7 29 -302 C ATOM 141 CE1 PHE A 21 6.683 -2.739 10.031 1.00 15.27 C ANISOU 141 CE1 PHE A 21 1707 1529 2567 59 16 -196 C ATOM 142 CE2 PHE A 21 7.086 -4.342 8.311 1.00 16.00 C ANISOU 142 CE2 PHE A 21 1838 1602 2637 -25 51 -257 C ATOM 143 CZ PHE A 21 7.491 -3.702 9.463 1.00 16.84 C ANISOU 143 CZ PHE A 21 1959 1640 2801 8 43 -204 C ATOM 144 N ASP A 22 0.307 -2.763 7.865 1.00 16.46 N ANISOU 144 N ASP A 22 1447 2571 2234 21 -78 -493 N ATOM 145 CA ASP A 22 -0.930 -2.293 7.254 1.00 20.08 C ANISOU 145 CA ASP A 22 1806 3246 2576 74 -106 -538 C ATOM 146 C ASP A 22 -1.529 -1.102 8.000 1.00 21.34 C ANISOU 146 C ASP A 22 1921 3481 2707 180 -132 -503 C ATOM 147 O ASP A 22 -2.346 -0.372 7.445 1.00 20.29 O ANISOU 147 O ASP A 22 1720 3510 2479 277 -157 -516 O ATOM 148 CB ASP A 22 -1.969 -3.417 7.169 1.00 26.56 C ANISOU 148 CB ASP A 22 2555 4207 3330 -67 -103 -638 C ATOM 149 CG ASP A 22 -1.678 -4.401 6.051 1.00 33.52 C ANISOU 149 CG ASP A 22 3462 5076 4197 -144 -82 -686 C ATOM 150 OD1 ASP A 22 -0.850 -4.077 5.173 1.00 36.72 O ANISOU 150 OD1 ASP A 22 3922 5405 4625 -66 -78 -644 O ATOM 151 OD2 ASP A 22 -2.283 -5.495 6.048 1.00 33.35 O ANISOU 151 OD2 ASP A 22 3411 5121 4139 -286 -67 -766 O ATOM 152 N ILE A 23 -1.132 -0.908 9.254 1.00 18.60 N ANISOU 152 N ILE A 23 1613 3020 2435 166 -126 -459 N ATOM 153 CA ILE A 23 -1.720 0.155 10.070 1.00 24.05 C ANISOU 153 CA ILE A 23 2266 3773 3099 256 -147 -427 C ATOM 154 C ILE A 23 -1.137 1.515 9.699 1.00 26.17 C ANISOU 154 C ILE A 23 2584 3986 3372 420 -151 -350 C ATOM 155 O ILE A 23 -1.651 2.556 10.104 1.00 24.68 O ANISOU 155 O ILE A 23 2371 3862 3142 524 -167 -321 O ATOM 156 CB ILE A 23 -1.481 -0.064 11.581 1.00 23.64 C ANISOU 156 CB ILE A 23 2244 3613 3126 185 -138 -405 C ATOM 157 CG1 ILE A 23 0.013 -0.007 11.902 1.00 23.66 C ANISOU 157 CG1 ILE A 23 2356 3390 3243 191 -116 -335 C ATOM 158 CG2 ILE A 23 -2.099 -1.379 12.058 1.00 19.39 C ANISOU 158 CG2 ILE A 23 1666 3122 2579 21 -127 -481 C ATOM 159 CD1 ILE A 23 0.315 -0.056 13.394 1.00 27.02 C ANISOU 159 CD1 ILE A 23 2813 3709 3743 144 -111 -305 C ATOM 160 N LEU A 24 -0.050 1.504 8.940 1.00 25.83 N ANISOU 160 N LEU A 24 2616 3819 3377 444 -133 -316 N ATOM 161 CA LEU A 24 0.685 2.735 8.670 1.00 30.63 C ANISOU 161 CA LEU A 24 3291 4342 4003 581 -127 -240 C ATOM 162 C LEU A 24 0.021 3.569 7.583 1.00 30.07 C ANISOU 162 C LEU A 24 3185 4416 3824 714 -141 -244 C ATOM 163 O LEU A 24 -0.658 3.037 6.705 1.00 29.27 O ANISOU 163 O LEU A 24 3020 4451 3648 693 -153 -304 O ATOM 164 CB LEU A 24 2.135 2.424 8.277 1.00 26.80 C ANISOU 164 CB LEU A 24 2899 3673 3610 555 -99 -202 C ATOM 165 CG LEU A 24 3.007 1.691 9.298 1.00 24.08 C ANISOU 165 CG LEU A 24 2604 3169 3376 448 -82 -186 C ATOM 166 CD1 LEU A 24 4.302 1.195 8.647 1.00 18.61 C ANISOU 166 CD1 LEU A 24 1986 2334 2753 421 -56 -165 C ATOM 167 CD2 LEU A 24 3.313 2.577 10.498 1.00 26.17 C ANISOU 167 CD2 LEU A 24 2900 3354 3689 493 -83 -128 C ATOM 168 N LYS A 25 0.216 4.883 7.645 1.00 35.34 N ANISOU 168 N LYS A 25 3933 5019 4475 800 -130 -171 N ATOM 169 CA LYS A 25 -0.270 5.750 6.580 1.00 43.45 C ANISOU 169 CA LYS A 25 4987 6123 5400 883 -129 -158 C ATOM 170 C LYS A 25 0.359 5.326 5.257 1.00 44.28 C ANISOU 170 C LYS A 25 5108 6210 5507 899 -121 -170 C ATOM 171 O LYS A 25 -0.342 5.004 4.296 1.00 42.70 O ANISOU 171 O LYS A 25 4847 6158 5220 925 -137 -221 O ATOM 172 CB LYS A 25 0.051 7.218 6.868 1.00 47.44 C ANISOU 172 CB LYS A 25 5598 6526 5902 928 -106 -83 C ATOM 173 CG LYS A 25 -0.492 8.163 5.804 1.00 52.55 C ANISOU 173 CG LYS A 25 6275 7256 6434 1018 -103 -74 C ATOM 174 CD LYS A 25 -2.011 8.029 5.680 1.00 55.92 C ANISOU 174 CD LYS A 25 6612 7894 6740 1056 -132 -129 C ATOM 175 CE LYS A 25 -2.558 8.749 4.447 1.00 58.32 C ANISOU 175 CE LYS A 25 6937 8301 6921 1152 -131 -130 C ATOM 176 NZ LYS A 25 -2.236 8.032 3.180 1.00 58.46 N ANISOU 176 NZ LYS A 25 6932 8353 6928 1156 -137 -161 N ATOM 177 N ASP A 26 1.688 5.319 5.223 1.00 41.38 N ANISOU 177 N ASP A 26 4823 5663 5236 877 -93 -124 N ATOM 178 CA ASP A 26 2.428 4.863 4.050 1.00 41.32 C ANISOU 178 CA ASP A 26 4841 5613 5245 885 -80 -132 C ATOM 179 C ASP A 26 3.246 3.627 4.397 1.00 37.01 C ANISOU 179 C ASP A 26 4287 4972 4803 804 -72 -159 C ATOM 180 O ASP A 26 4.413 3.738 4.762 1.00 38.01 O ANISOU 180 O ASP A 26 4493 4927 5022 780 -47 -108 O ATOM 181 CB ASP A 26 3.349 5.967 3.521 1.00 46.82 C ANISOU 181 CB ASP A 26 5653 6179 5959 906 -49 -60 C ATOM 182 CG ASP A 26 2.598 7.045 2.754 1.00 57.59 C ANISOU 182 CG ASP A 26 7036 7642 7206 989 -53 -50 C ATOM 183 OD1 ASP A 26 1.510 7.460 3.209 1.00 59.79 O ANISOU 183 OD1 ASP A 26 7275 8033 7410 1023 -71 -63 O ATOM 184 OD2 ASP A 26 3.096 7.478 1.690 1.00 63.00 O ANISOU 184 OD2 ASP A 26 7775 8292 7868 1019 -36 -30 O ATOM 185 N PRO A 27 2.624 2.442 4.310 1.00 35.57 N ANISOU 185 N PRO A 27 4040 4876 4598 692 -84 -230 N ATOM 186 CA PRO A 27 3.348 1.191 4.571 1.00 33.25 C ANISOU 186 CA PRO A 27 3778 4467 4390 552 -65 -250 C ATOM 187 C PRO A 27 4.412 0.935 3.516 1.00 30.47 C ANISOU 187 C PRO A 27 3493 4012 4073 560 -41 -232 C ATOM 188 O PRO A 27 4.200 1.263 2.351 1.00 32.14 O ANISOU 188 O PRO A 27 3696 4298 4218 632 -44 -241 O ATOM 189 CB PRO A 27 2.253 0.124 4.480 1.00 37.40 C ANISOU 189 CB PRO A 27 4220 5137 4852 446 -80 -337 C ATOM 190 CG PRO A 27 1.129 0.773 3.735 1.00 39.39 C ANISOU 190 CG PRO A 27 4396 5587 4982 540 -107 -366 C ATOM 191 CD PRO A 27 1.185 2.218 4.104 1.00 36.37 C ANISOU 191 CD PRO A 27 4037 5189 4592 684 -113 -298 C ATOM 192 N PRO A 28 5.545 0.346 3.918 1.00 22.86 N ANISOU 192 N PRO A 28 2593 2883 3211 490 -16 -207 N ATOM 193 CA PRO A 28 6.616 0.068 2.954 1.00 22.91 C ANISOU 193 CA PRO A 28 2662 2787 3254 496 10 -189 C ATOM 194 C PRO A 28 6.092 -0.802 1.823 1.00 22.32 C ANISOU 194 C PRO A 28 2556 2810 3115 450 8 -254 C ATOM 195 O PRO A 28 5.310 -1.716 2.073 1.00 24.25 O ANISOU 195 O PRO A 28 2751 3134 3329 352 0 -317 O ATOM 196 CB PRO A 28 7.657 -0.691 3.785 1.00 21.00 C ANISOU 196 CB PRO A 28 2474 2385 3120 407 32 -168 C ATOM 197 CG PRO A 28 6.920 -1.200 4.988 1.00 21.10 C ANISOU 197 CG PRO A 28 2443 2437 3135 324 18 -199 C ATOM 198 CD PRO A 28 5.801 -0.240 5.244 1.00 17.36 C ANISOU 198 CD PRO A 28 1906 2100 2588 396 -11 -203 C ATOM 199 N LYS A 29 6.496 -0.512 0.592 1.00 27.78 N ANISOU 199 N LYS A 29 3278 3498 3781 518 19 -243 N ATOM 200 CA LYS A 29 5.996 -1.267 -0.548 1.00 29.05 C ANISOU 200 CA LYS A 29 3408 3756 3874 481 16 -305 C ATOM 201 C LYS A 29 6.915 -2.442 -0.815 1.00 23.98 C ANISOU 201 C LYS A 29 2823 2991 3297 383 48 -316 C ATOM 202 O LYS A 29 6.542 -3.402 -1.481 1.00 29.02 O ANISOU 202 O LYS A 29 3445 3686 3894 308 52 -377 O ATOM 203 CB LYS A 29 5.905 -0.379 -1.792 1.00 38.66 C ANISOU 203 CB LYS A 29 4629 5039 5020 608 12 -289 C ATOM 204 CG LYS A 29 5.131 0.911 -1.587 1.00 42.73 C ANISOU 204 CG LYS A 29 5108 5661 5468 732 -12 -266 C ATOM 205 CD LYS A 29 4.781 1.562 -2.916 1.00 47.52 C ANISOU 205 CD LYS A 29 5708 6369 5979 849 -18 -268 C ATOM 206 CE LYS A 29 4.204 2.958 -2.713 1.00 50.34 C ANISOU 206 CE LYS A 29 6053 6801 6272 993 -32 -230 C ATOM 207 NZ LYS A 29 2.990 2.956 -1.853 1.00 49.90 N ANISOU 207 NZ LYS A 29 5908 6887 6164 974 -65 -267 N ATOM 208 N LYS A 30 8.121 -2.356 -0.270 1.00 16.23 N ANISOU 208 N LYS A 30 1910 1842 2415 385 71 -258 N ATOM 209 CA LYS A 30 9.152 -3.344 -0.511 1.00 16.90 C ANISOU 209 CA LYS A 30 2058 1798 2566 316 103 -256 C ATOM 210 C LYS A 30 10.090 -3.362 0.688 1.00 14.28 C ANISOU 210 C LYS A 30 1770 1321 2335 293 117 -206 C ATOM 211 O LYS A 30 10.444 -2.314 1.218 1.00 16.84 O ANISOU 211 O LYS A 30 2102 1606 2689 366 111 -152 O ATOM 212 CB LYS A 30 9.922 -2.974 -1.778 1.00 23.65 C ANISOU 212 CB LYS A 30 2959 2610 3418 391 121 -229 C ATOM 213 CG LYS A 30 10.532 -4.147 -2.507 1.00 29.79 C ANISOU 213 CG LYS A 30 3781 3322 4216 321 150 -255 C ATOM 214 CD LYS A 30 10.965 -3.730 -3.905 1.00 36.36 C ANISOU 214 CD LYS A 30 4641 4154 5018 400 162 -241 C ATOM 215 CE LYS A 30 11.739 -4.837 -4.602 1.00 42.91 C ANISOU 215 CE LYS A 30 5527 4900 5879 340 196 -257 C ATOM 216 NZ LYS A 30 12.319 -4.368 -5.893 1.00 45.24 N ANISOU 216 NZ LYS A 30 5856 5176 6156 421 211 -235 N ATOM 217 N LEU A 31 10.477 -4.551 1.132 1.00 13.82 N ANISOU 217 N LEU A 31 1743 1186 2323 193 137 -225 N ATOM 218 CA LEU A 31 11.389 -4.665 2.264 1.00 13.28 C ANISOU 218 CA LEU A 31 1715 985 2345 173 150 -180 C ATOM 219 C LEU A 31 12.545 -5.591 1.920 1.00 14.01 C ANISOU 219 C LEU A 31 1873 1052 2399 122 159 -148 C ATOM 220 O LEU A 31 12.344 -6.690 1.413 1.00 17.14 O ANISOU 220 O LEU A 31 2286 1418 2808 61 186 -199 O ATOM 221 CB LEU A 31 10.651 -5.162 3.512 1.00 10.62 C ANISOU 221 CB LEU A 31 1350 677 2010 92 138 -207 C ATOM 222 CG LEU A 31 9.745 -4.166 4.234 1.00 11.05 C ANISOU 222 CG LEU A 31 1342 824 2031 134 105 -201 C ATOM 223 CD1 LEU A 31 8.934 -4.871 5.319 1.00 15.34 C ANISOU 223 CD1 LEU A 31 1856 1405 2567 38 98 -241 C ATOM 224 CD2 LEU A 31 10.542 -3.002 4.833 1.00 12.94 C ANISOU 224 CD2 LEU A 31 1606 1006 2306 213 98 -124 C ATOM 225 N TYR A 32 13.759 -5.135 2.191 1.00 12.15 N ANISOU 225 N TYR A 32 1671 843 2102 145 134 -81 N ATOM 226 CA TYR A 32 14.946 -5.950 1.951 1.00 9.86 C ANISOU 226 CA TYR A 32 1426 546 1773 118 127 -63 C ATOM 227 C TYR A 32 15.335 -6.663 3.232 1.00 11.65 C ANISOU 227 C TYR A 32 1660 777 1990 71 120 -50 C ATOM 228 O TYR A 32 15.168 -6.110 4.319 1.00 10.18 O ANISOU 228 O TYR A 32 1445 610 1812 73 114 -36 O ATOM 229 CB TYR A 32 16.075 -5.065 1.437 1.00 11.14 C ANISOU 229 CB TYR A 32 1594 730 1907 164 116 -26 C ATOM 230 CG TYR A 32 15.668 -4.430 0.144 1.00 11.11 C ANISOU 230 CG TYR A 32 1599 730 1892 218 114 -39 C ATOM 231 CD1 TYR A 32 14.977 -3.229 0.134 1.00 17.18 C ANISOU 231 CD1 TYR A 32 2346 1525 2657 275 107 -35 C ATOM 232 CD2 TYR A 32 15.925 -5.057 -1.072 1.00 16.81 C ANISOU 232 CD2 TYR A 32 2340 1426 2620 220 131 -54 C ATOM 233 CE1 TYR A 32 14.575 -2.656 -1.038 1.00 17.16 C ANISOU 233 CE1 TYR A 32 2338 1530 2649 340 113 -47 C ATOM 234 CE2 TYR A 32 15.514 -4.483 -2.262 1.00 18.35 C ANISOU 234 CE2 TYR A 32 2531 1624 2819 278 142 -68 C ATOM 235 CZ TYR A 32 14.840 -3.279 -2.231 1.00 21.76 C ANISOU 235 CZ TYR A 32 2938 2089 3239 342 132 -64 C ATOM 236 OH TYR A 32 14.421 -2.679 -3.401 1.00 25.32 O ANISOU 236 OH TYR A 32 3382 2560 3679 417 140 -78 O ATOM 237 N CYS A 33 15.823 -7.893 3.104 1.00 12.63 N ANISOU 237 N CYS A 33 1808 875 2118 35 133 -58 N ATOM 238 CA CYS A 33 16.026 -8.752 4.267 1.00 14.49 C ANISOU 238 CA CYS A 33 2044 1101 2361 -4 141 -54 C ATOM 239 C CYS A 33 17.298 -9.576 4.181 1.00 12.63 C ANISOU 239 C CYS A 33 1822 844 2132 -2 161 -37 C ATOM 240 O CYS A 33 17.698 -10.023 3.105 1.00 12.86 O ANISOU 240 O CYS A 33 1874 854 2157 2 171 -43 O ATOM 241 CB CYS A 33 14.829 -9.702 4.427 1.00 13.16 C ANISOU 241 CB CYS A 33 1902 918 2181 -66 136 -95 C ATOM 242 SG CYS A 33 14.575 -10.791 2.981 1.00 19.90 S ANISOU 242 SG CYS A 33 2788 1735 3037 -105 161 -138 S ATOM 243 N VAL A 34 17.937 -9.770 5.329 1.00 13.84 N ANISOU 243 N VAL A 34 1961 1000 2297 -3 168 -18 N ATOM 244 CA VAL A 34 18.960 -10.789 5.467 1.00 15.77 C ANISOU 244 CA VAL A 34 2227 1219 2544 -6 187 -10 C ATOM 245 C VAL A 34 18.737 -11.512 6.796 1.00 15.32 C ANISOU 245 C VAL A 34 2181 1152 2488 -31 187 -12 C ATOM 246 O VAL A 34 18.485 -10.879 7.817 1.00 13.48 O ANISOU 246 O VAL A 34 1919 942 2261 -28 176 -4 O ATOM 247 CB VAL A 34 20.385 -10.206 5.372 1.00 14.84 C ANISOU 247 CB VAL A 34 2083 1116 2442 33 197 20 C ATOM 248 CG1 VAL A 34 20.574 -9.052 6.351 1.00 9.96 C ANISOU 248 CG1 VAL A 34 1415 532 1837 48 187 39 C ATOM 249 CG2 VAL A 34 21.411 -11.296 5.631 1.00 18.15 C ANISOU 249 CG2 VAL A 34 2525 1507 2864 33 217 28 C ATOM 250 N GLY A 35 18.797 -12.839 6.775 1.00 20.66 N ANISOU 250 N GLY A 35 2902 1793 3157 -58 202 -24 N ATOM 251 CA GLY A 35 18.632 -13.616 7.988 1.00 21.00 C ANISOU 251 CA GLY A 35 2962 1819 3196 -81 206 -26 C ATOM 252 C GLY A 35 17.334 -14.400 8.013 1.00 23.78 C ANISOU 252 C GLY A 35 3343 2156 3534 -139 207 -60 C ATOM 253 O GLY A 35 16.748 -14.685 6.969 1.00 21.67 O ANISOU 253 O GLY A 35 3092 1883 3260 -165 211 -85 O ATOM 254 N ASP A 36 16.880 -14.721 9.220 1.00 21.82 N ANISOU 254 N ASP A 36 3100 1906 3285 -162 205 -63 N ATOM 255 CA ASP A 36 15.738 -15.599 9.437 1.00 21.12 C ANISOU 255 CA ASP A 36 3037 1804 3183 -225 214 -96 C ATOM 256 C ASP A 36 14.400 -14.882 9.302 1.00 17.95 C ANISOU 256 C ASP A 36 2607 1438 2777 -259 191 -121 C ATOM 257 O ASP A 36 13.911 -14.291 10.268 1.00 21.10 O ANISOU 257 O ASP A 36 2981 1860 3177 -261 174 -116 O ATOM 258 CB ASP A 36 15.840 -16.203 10.841 1.00 23.42 C ANISOU 258 CB ASP A 36 3345 2081 3474 -234 224 -88 C ATOM 259 CG ASP A 36 14.823 -17.292 11.083 1.00 26.50 C ANISOU 259 CG ASP A 36 3767 2454 3847 -301 250 -123 C ATOM 260 OD1 ASP A 36 14.017 -17.559 10.172 1.00 28.64 O ANISOU 260 OD1 ASP A 36 4044 2733 4105 -346 261 -159 O ATOM 261 OD2 ASP A 36 14.829 -17.877 12.188 1.00 26.14 O ANISOU 261 OD2 ASP A 36 3743 2393 3797 -311 265 -120 O ATOM 262 N THR A 37 13.793 -14.958 8.122 1.00 18.05 N ANISOU 262 N THR A 37 2622 1456 2781 -288 192 -151 N ATOM 263 CA THR A 37 12.519 -14.283 7.881 1.00 16.50 C ANISOU 263 CA THR A 37 2394 1298 2577 -323 169 -182 C ATOM 264 C THR A 37 11.372 -14.886 8.693 1.00 18.25 C ANISOU 264 C THR A 37 2611 1537 2786 -393 175 -215 C ATOM 265 O THR A 37 10.318 -14.274 8.822 1.00 20.43 O ANISOU 265 O THR A 37 2850 1853 3061 -427 167 -244 O ATOM 266 CB THR A 37 12.114 -14.318 6.399 1.00 16.28 C ANISOU 266 CB THR A 37 2367 1275 2543 -346 178 -219 C ATOM 267 OG1 THR A 37 11.846 -15.668 6.013 1.00 23.71 O ANISOU 267 OG1 THR A 37 3342 2201 3466 -406 213 -255 O ATOM 268 CG2 THR A 37 13.216 -13.751 5.526 1.00 20.38 C ANISOU 268 CG2 THR A 37 2894 1782 3070 -275 167 -184 C ATOM 269 N LYS A 38 11.571 -16.088 9.225 1.00 19.70 N ANISOU 269 N LYS A 38 2832 1691 2962 -420 210 -221 N ATOM 270 CA LYS A 38 10.519 -16.753 9.988 1.00 23.03 C ANISOU 270 CA LYS A 38 3257 2130 3365 -489 228 -256 C ATOM 271 C LYS A 38 10.258 -16.074 11.327 1.00 20.45 C ANISOU 271 C LYS A 38 2901 1819 3049 -473 203 -234 C ATOM 272 O LYS A 38 9.227 -16.313 11.959 1.00 23.08 O ANISOU 272 O LYS A 38 3221 2180 3368 -528 210 -263 O ATOM 273 CB LYS A 38 10.855 -18.228 10.210 1.00 29.53 C ANISOU 273 CB LYS A 38 4142 2910 4167 -518 284 -267 C ATOM 274 CG LYS A 38 10.985 -19.031 8.927 1.00 33.37 C ANISOU 274 CG LYS A 38 4666 3381 4632 -546 318 -295 C ATOM 275 CD LYS A 38 9.726 -18.928 8.083 1.00 38.38 C ANISOU 275 CD LYS A 38 5272 4071 5241 -615 315 -352 C ATOM 276 CE LYS A 38 9.857 -19.738 6.803 1.00 41.67 C ANISOU 276 CE LYS A 38 5729 4475 5631 -646 350 -383 C ATOM 277 NZ LYS A 38 8.672 -19.582 5.914 1.00 43.01 N ANISOU 277 NZ LYS A 38 5875 4708 5761 -735 381 -462 N ATOM 278 N LEU A 39 11.194 -15.236 11.764 1.00 18.45 N ANISOU 278 N LEU A 39 2639 1556 2817 -401 179 -185 N ATOM 279 CA LEU A 39 11.039 -14.513 13.023 1.00 21.43 C ANISOU 279 CA LEU A 39 2991 1949 3201 -382 158 -163 C ATOM 280 C LEU A 39 9.816 -13.604 12.967 1.00 21.56 C ANISOU 280 C LEU A 39 2962 2017 3211 -410 132 -185 C ATOM 281 O LEU A 39 9.214 -13.288 13.991 1.00 22.77 O ANISOU 281 O LEU A 39 3096 2193 3364 -424 121 -185 O ATOM 282 CB LEU A 39 12.293 -13.689 13.335 1.00 16.57 C ANISOU 282 CB LEU A 39 2369 1328 2600 -304 147 -116 C ATOM 283 CG LEU A 39 13.516 -14.474 13.802 1.00 16.45 C ANISOU 283 CG LEU A 39 2386 1275 2590 -275 166 -92 C ATOM 284 CD1 LEU A 39 14.676 -13.531 14.062 1.00 12.66 C ANISOU 284 CD1 LEU A 39 1879 807 2123 -207 157 -55 C ATOM 285 CD2 LEU A 39 13.179 -15.249 15.059 1.00 17.20 C ANISOU 285 CD2 LEU A 39 2501 1353 2680 -305 177 -97 C ATOM 286 N LEU A 40 9.457 -13.193 11.756 1.00 21.31 N ANISOU 286 N LEU A 40 2913 2008 3175 -419 122 -206 N ATOM 287 CA LEU A 40 8.298 -12.338 11.537 1.00 15.90 C ANISOU 287 CA LEU A 40 2167 1372 2502 -454 133 -255 C ATOM 288 C LEU A 40 6.994 -13.032 11.905 1.00 17.46 C ANISOU 288 C LEU A 40 2341 1616 2676 -546 154 -316 C ATOM 289 O LEU A 40 5.950 -12.392 11.970 1.00 19.23 O ANISOU 289 O LEU A 40 2500 1906 2899 -585 158 -366 O ATOM 290 CB LEU A 40 8.237 -11.888 10.076 1.00 18.61 C ANISOU 290 CB LEU A 40 2484 1723 2863 -454 155 -295 C ATOM 291 CG LEU A 40 9.364 -10.955 9.638 1.00 17.77 C ANISOU 291 CG LEU A 40 2386 1584 2783 -358 141 -240 C ATOM 292 CD1 LEU A 40 9.338 -10.779 8.128 1.00 16.20 C ANISOU 292 CD1 LEU A 40 2172 1379 2603 -358 165 -281 C ATOM 293 CD2 LEU A 40 9.254 -9.614 10.340 1.00 15.15 C ANISOU 293 CD2 LEU A 40 2007 1268 2481 -305 125 -216 C ATOM 294 N ASP A 41 7.054 -14.338 12.138 1.00 19.33 N ANISOU 294 N ASP A 41 2624 1829 2890 -580 169 -318 N ATOM 295 CA ASP A 41 5.858 -15.090 12.502 1.00 21.92 C ANISOU 295 CA ASP A 41 2940 2206 3182 -667 200 -376 C ATOM 296 C ASP A 41 5.758 -15.313 14.010 1.00 24.03 C ANISOU 296 C ASP A 41 3219 2458 3453 -657 183 -342 C ATOM 297 O ASP A 41 4.841 -15.979 14.491 1.00 25.47 O ANISOU 297 O ASP A 41 3400 2674 3603 -723 211 -383 O ATOM 298 CB ASP A 41 5.817 -16.425 11.762 1.00 22.85 C ANISOU 298 CB ASP A 41 3105 2311 3264 -722 246 -414 C ATOM 299 CG ASP A 41 5.741 -16.253 10.253 1.00 32.46 C ANISOU 299 CG ASP A 41 4309 3556 4467 -747 265 -460 C ATOM 300 OD1 ASP A 41 5.213 -15.216 9.789 1.00 33.76 O ANISOU 300 OD1 ASP A 41 4408 3784 4634 -754 252 -494 O ATOM 301 OD2 ASP A 41 6.208 -17.159 9.532 1.00 36.56 O ANISOU 301 OD2 ASP A 41 4881 4040 4972 -758 293 -465 O ATOM 302 N THR A 42 6.709 -14.761 14.754 1.00 18.73 N ANISOU 302 N THR A 42 2556 1766 2796 -119 -6 627 N ATOM 303 CA THR A 42 6.710 -14.903 16.201 1.00 21.70 C ANISOU 303 CA THR A 42 2896 2203 3148 -136 23 766 C ATOM 304 C THR A 42 5.450 -14.264 16.781 1.00 20.62 C ANISOU 304 C THR A 42 2729 2039 3066 -189 61 762 C ATOM 305 O THR A 42 5.123 -13.131 16.452 1.00 22.28 O ANISOU 305 O THR A 42 2930 2197 3337 -227 33 666 O ATOM 306 CB THR A 42 7.977 -14.275 16.814 1.00 22.85 C ANISOU 306 CB THR A 42 3017 2437 3229 -141 -15 842 C ATOM 307 OG1 THR A 42 9.136 -14.875 16.218 1.00 23.35 O ANISOU 307 OG1 THR A 42 3102 2513 3255 -93 -44 828 O ATOM 308 CG2 THR A 42 8.011 -14.482 18.320 1.00 18.85 C ANISOU 308 CG2 THR A 42 2472 2083 2608 -146 27 953 C ATOM 309 N PRO A 43 4.727 -15.003 17.633 1.00 27.21 N ANISOU 309 N PRO A 43 3546 2910 3882 -195 126 850 N ATOM 310 CA PRO A 43 3.468 -14.501 18.197 1.00 30.42 C ANISOU 310 CA PRO A 43 3916 3311 4331 -246 180 823 C ATOM 311 C PRO A 43 3.638 -13.200 18.981 1.00 28.45 C ANISOU 311 C PRO A 43 3623 3207 3980 -270 163 695 C ATOM 312 O PRO A 43 2.796 -12.309 18.858 1.00 25.20 O ANISOU 312 O PRO A 43 3192 2762 3620 -304 159 561 O ATOM 313 CB PRO A 43 3.033 -15.628 19.139 1.00 30.71 C ANISOU 313 CB PRO A 43 3940 3416 4313 -240 257 959 C ATOM 314 CG PRO A 43 3.659 -16.850 18.574 1.00 31.47 C ANISOU 314 CG PRO A 43 4083 3490 4383 -180 215 966 C ATOM 315 CD PRO A 43 4.983 -16.402 18.014 1.00 28.08 C ANISOU 315 CD PRO A 43 3670 3070 3928 -154 148 936 C ATOM 316 N LEU A 44 4.702 -13.104 19.774 1.00 26.76 N ANISOU 316 N LEU A 44 3392 3148 3627 -252 148 733 N ATOM 317 CA LEU A 44 4.949 -11.925 20.602 1.00 25.53 C ANISOU 317 CA LEU A 44 3191 3143 3366 -270 130 617 C ATOM 318 C LEU A 44 6.195 -11.162 20.155 1.00 20.18 C ANISOU 318 C LEU A 44 2523 2482 2664 -259 50 561 C ATOM 319 O LEU A 44 7.314 -11.664 20.266 1.00 19.79 O ANISOU 319 O LEU A 44 2485 2488 2547 -225 30 654 O ATOM 320 CB LEU A 44 5.073 -12.321 22.077 1.00 26.71 C ANISOU 320 CB LEU A 44 3304 3487 3360 -263 183 691 C ATOM 321 CG LEU A 44 5.422 -11.222 23.086 1.00 23.81 C ANISOU 321 CG LEU A 44 2884 3301 2863 -276 167 583 C ATOM 322 CD1 LEU A 44 4.392 -10.102 23.045 1.00 25.03 C ANISOU 322 CD1 LEU A 44 3006 3432 3074 -317 167 411 C ATOM 323 CD2 LEU A 44 5.545 -11.788 24.491 1.00 26.03 C ANISOU 323 CD2 LEU A 44 3134 3768 2987 -266 222 677 C ATOM 324 N LYS A 45 5.990 -9.952 19.647 1.00 23.07 N ANISOU 324 N LYS A 45 2881 2797 3086 -288 3 410 N ATOM 325 CA LYS A 45 7.089 -9.101 19.216 1.00 24.88 C ANISOU 325 CA LYS A 45 3116 3040 3298 -287 -73 344 C ATOM 326 C LYS A 45 7.183 -7.894 20.137 1.00 22.46 C ANISOU 326 C LYS A 45 2757 2878 2899 -308 -92 217 C ATOM 327 O LYS A 45 6.214 -7.153 20.302 1.00 19.01 O ANISOU 327 O LYS A 45 2295 2429 2500 -339 -85 101 O ATOM 328 CB LYS A 45 6.893 -8.659 17.762 1.00 23.37 C ANISOU 328 CB LYS A 45 2966 2660 3253 -304 -125 276 C ATOM 329 CG LYS A 45 6.724 -9.817 16.778 1.00 25.77 C ANISOU 329 CG LYS A 45 3320 2812 3659 -283 -109 387 C ATOM 330 CD LYS A 45 6.754 -9.325 15.347 1.00 21.15 C ANISOU 330 CD LYS A 45 2776 2061 3197 -298 -168 321 C ATOM 331 CE LYS A 45 6.423 -10.441 14.367 1.00 23.81 C ANISOU 331 CE LYS A 45 3153 2338 3557 -244 -122 361 C ATOM 332 NZ LYS A 45 5.098 -11.068 14.657 1.00 22.82 N ANISOU 332 NZ LYS A 45 3026 2186 3456 -243 -62 372 N ATOM 333 N VAL A 46 8.349 -7.712 20.750 1.00 21.77 N ANISOU 333 N VAL A 46 2649 2929 2692 -289 -118 237 N ATOM 334 CA VAL A 46 8.555 -6.635 21.714 1.00 20.71 C ANISOU 334 CA VAL A 46 2461 2949 2458 -303 -137 124 C ATOM 335 C VAL A 46 9.650 -5.678 21.254 1.00 18.79 C ANISOU 335 C VAL A 46 2218 2709 2212 -309 -220 46 C ATOM 336 O VAL A 46 10.770 -6.093 20.989 1.00 19.12 O ANISOU 336 O VAL A 46 2279 2765 2221 -284 -245 125 O ATOM 337 CB VAL A 46 8.949 -7.201 23.088 1.00 22.38 C ANISOU 337 CB VAL A 46 2638 3356 2509 -277 -93 209 C ATOM 338 CG1 VAL A 46 9.150 -6.077 24.107 1.00 21.42 C ANISOU 338 CG1 VAL A 46 2457 3401 2281 -289 -113 84 C ATOM 339 CG2 VAL A 46 7.892 -8.185 23.574 1.00 26.46 C ANISOU 339 CG2 VAL A 46 3154 3875 3023 -276 -8 298 C ATOM 340 N ALA A 47 9.317 -4.396 21.162 1.00 19.52 N ANISOU 340 N ALA A 47 2288 2788 2342 -344 -262 -112 N ATOM 341 CA ALA A 47 10.311 -3.371 20.861 1.00 18.43 C ANISOU 341 CA ALA A 47 2142 2665 2195 -357 -341 -196 C ATOM 342 C ALA A 47 11.026 -2.913 22.127 1.00 19.84 C ANISOU 342 C ALA A 47 2264 3050 2224 -344 -348 -231 C ATOM 343 O ALA A 47 10.389 -2.579 23.135 1.00 21.89 O ANISOU 343 O ALA A 47 2476 3418 2421 -349 -318 -294 O ATOM 344 CB ALA A 47 9.667 -2.186 20.164 1.00 14.10 C ANISOU 344 CB ALA A 47 1597 2000 1760 -400 -392 -348 C ATOM 345 N ILE A 48 12.351 -2.910 22.082 1.00 16.79 N ANISOU 345 N ILE A 48 1880 2722 1779 -326 -388 -192 N ATOM 346 CA ILE A 48 13.137 -2.337 23.164 1.00 20.07 C ANISOU 346 CA ILE A 48 2241 3322 2062 -315 -410 -241 C ATOM 347 C ILE A 48 14.020 -1.284 22.535 1.00 19.88 C ANISOU 347 C ILE A 48 2215 3262 2076 -339 -493 -334 C ATOM 348 O ILE A 48 14.897 -1.594 21.719 1.00 21.31 O ANISOU 348 O ILE A 48 2430 3379 2287 -332 -521 -271 O ATOM 349 CB ILE A 48 13.975 -3.384 23.919 1.00 18.59 C ANISOU 349 CB ILE A 48 2048 3268 1747 -267 -378 -100 C ATOM 350 CG1 ILE A 48 13.068 -4.495 24.470 1.00 20.51 C ANISOU 350 CG1 ILE A 48 2299 3532 1962 -249 -295 6 C ATOM 351 CG2 ILE A 48 14.769 -2.723 25.041 1.00 21.59 C ANISOU 351 CG2 ILE A 48 2370 3842 1990 -255 -405 -162 C ATOM 352 CD1 ILE A 48 13.809 -5.563 25.229 1.00 23.36 C ANISOU 352 CD1 ILE A 48 2659 4016 2200 -202 -265 152 C ATOM 353 N ILE A 49 13.768 -0.035 22.905 1.00 17.54 N ANISOU 353 N ILE A 49 1878 3007 1781 -368 -532 -486 N ATOM 354 CA ILE A 49 14.433 1.104 22.296 1.00 18.45 C ANISOU 354 CA ILE A 49 1999 3057 1955 -394 -605 -578 C ATOM 355 C ILE A 49 14.752 2.092 23.394 1.00 20.56 C ANISOU 355 C ILE A 49 2230 3417 2163 -372 -600 -645 C ATOM 356 O ILE A 49 14.131 2.068 24.462 1.00 25.03 O ANISOU 356 O ILE A 49 2745 4118 2649 -366 -570 -691 O ATOM 357 CB ILE A 49 13.523 1.806 21.269 1.00 22.57 C ANISOU 357 CB ILE A 49 2582 3351 2643 -415 -609 -615 C ATOM 358 CG1 ILE A 49 12.240 2.283 21.950 1.00 26.39 C ANISOU 358 CG1 ILE A 49 3037 3851 3139 -419 -577 -699 C ATOM 359 CG2 ILE A 49 13.207 0.881 20.096 1.00 19.55 C ANISOU 359 CG2 ILE A 49 2240 2846 2341 -435 -611 -554 C ATOM 360 CD1 ILE A 49 11.539 3.389 21.206 1.00 30.02 C ANISOU 360 CD1 ILE A 49 3560 4129 3718 -426 -576 -711 C ATOM 361 N GLY A 50 15.711 2.970 23.141 1.00 20.24 N ANISOU 361 N GLY A 50 2217 3311 2161 -364 -628 -648 N ATOM 362 CA GLY A 50 16.049 3.967 24.134 1.00 24.42 C ANISOU 362 CA GLY A 50 2711 3919 2647 -348 -626 -712 C ATOM 363 C GLY A 50 17.333 4.712 23.857 1.00 24.97 C ANISOU 363 C GLY A 50 2806 3942 2740 -345 -658 -695 C ATOM 364 O GLY A 50 17.891 4.659 22.759 1.00 20.82 O ANISOU 364 O GLY A 50 2334 3297 2280 -359 -682 -638 O ATOM 365 N THR A 51 17.791 5.406 24.889 1.00 25.41 N ANISOU 365 N THR A 51 2818 4099 2737 -327 -655 -746 N ATOM 366 CA THR A 51 18.968 6.256 24.831 1.00 26.44 C ANISOU 366 CA THR A 51 2961 4203 2884 -327 -682 -746 C ATOM 367 C THR A 51 20.214 5.526 24.340 1.00 24.64 C ANISOU 367 C THR A 51 2748 3984 2629 -318 -699 -669 C ATOM 368 O THR A 51 20.417 4.347 24.626 1.00 24.36 O ANISOU 368 O THR A 51 2689 4054 2510 -296 -683 -620 O ATOM 369 CB THR A 51 19.257 6.849 26.221 1.00 27.36 C ANISOU 369 CB THR A 51 3012 4465 2920 -303 -671 -814 C ATOM 370 OG1 THR A 51 20.469 7.609 26.182 1.00 29.30 O ANISOU 370 OG1 THR A 51 3265 4690 3178 -303 -698 -813 O ATOM 371 CG2 THR A 51 19.404 5.736 27.242 1.00 25.80 C ANISOU 371 CG2 THR A 51 2758 4463 2581 -270 -642 -791 C ATOM 372 N ARG A 52 21.046 6.247 23.600 1.00 23.92 N ANISOU 372 N ARG A 52 2698 3787 2603 -337 -728 -651 N ATOM 373 CA ARG A 52 22.325 5.722 23.147 1.00 26.55 C ANISOU 373 CA ARG A 52 3043 4126 2920 -329 -744 -591 C ATOM 374 C ARG A 52 23.341 5.720 24.292 1.00 27.97 C ANISOU 374 C ARG A 52 3166 4462 3001 -296 -739 -609 C ATOM 375 O ARG A 52 24.425 5.152 24.179 1.00 29.66 O ANISOU 375 O ARG A 52 3376 4716 3178 -280 -745 -562 O ATOM 376 CB ARG A 52 22.832 6.539 21.956 1.00 29.02 C ANISOU 376 CB ARG A 52 3417 4279 3328 -367 -775 -562 C ATOM 377 CG ARG A 52 21.916 6.446 20.741 1.00 37.16 C ANISOU 377 CG ARG A 52 4512 5166 4443 -404 -775 -520 C ATOM 378 CD ARG A 52 22.520 7.079 19.492 1.00 43.31 C ANISOU 378 CD ARG A 52 5323 5858 5275 -444 -783 -499 C ATOM 379 NE ARG A 52 22.311 8.524 19.432 1.00 48.37 N ANISOU 379 NE ARG A 52 5954 6480 5945 -469 -776 -561 N ATOM 380 CZ ARG A 52 21.167 9.102 19.075 1.00 52.44 C ANISOU 380 CZ ARG A 52 6483 6940 6503 -486 -752 -591 C ATOM 381 NH1 ARG A 52 21.072 10.426 19.042 1.00 51.69 N ANISOU 381 NH1 ARG A 52 6372 6826 6440 -493 -753 -652 N ATOM 382 NH2 ARG A 52 20.115 8.359 18.756 1.00 55.12 N ANISOU 382 NH2 ARG A 52 6844 7241 6856 -490 -727 -564 N ATOM 383 N ARG A 53 22.973 6.338 25.407 1.00 25.81 N ANISOU 383 N ARG A 53 2847 4277 2683 -285 -726 -678 N ATOM 384 CA ARG A 53 23.877 6.421 26.551 1.00 31.59 C ANISOU 384 CA ARG A 53 3525 5158 3322 -254 -720 -699 C ATOM 385 C ARG A 53 23.208 5.990 27.852 1.00 30.71 C ANISOU 385 C ARG A 53 3355 5211 3103 -224 -686 -727 C ATOM 386 O ARG A 53 22.978 6.811 28.740 1.00 29.30 O ANISOU 386 O ARG A 53 3136 5092 2903 -218 -680 -802 O ATOM 387 CB ARG A 53 24.437 7.837 26.674 1.00 34.47 C ANISOU 387 CB ARG A 53 3888 5474 3734 -270 -744 -756 C ATOM 388 CG ARG A 53 25.316 8.230 25.498 1.00 41.04 C ANISOU 388 CG ARG A 53 4774 6173 4648 -300 -776 -715 C ATOM 389 CD ARG A 53 25.403 9.738 25.317 1.00 49.91 C ANISOU 389 CD ARG A 53 5893 7238 5833 -326 -793 -780 C ATOM 390 NE ARG A 53 25.713 10.084 23.930 1.00 57.54 N ANISOU 390 NE ARG A 53 6903 8081 6880 -362 -810 -750 N ATOM 391 CZ ARG A 53 24.795 10.338 22.998 1.00 60.57 C ANISOU 391 CZ ARG A 53 7328 8351 7335 -391 -809 -741 C ATOM 392 NH1 ARG A 53 23.506 10.298 23.308 1.00 60.95 N ANISOU 392 NH1 ARG A 53 7376 8390 7392 -387 -791 -765 N ATOM 393 NH2 ARG A 53 25.163 10.638 21.758 1.00 59.48 N ANISOU 393 NH2 ARG A 53 7229 8114 7255 -426 -822 -707 N ATOM 394 N PRO A 54 22.895 4.690 27.967 1.00 27.16 N ANISOU 394 N PRO A 54 2899 4839 2580 -206 -663 -659 N ATOM 395 CA PRO A 54 22.237 4.183 29.174 1.00 22.23 C ANISOU 395 CA PRO A 54 2224 4380 1842 -180 -627 -664 C ATOM 396 C PRO A 54 23.193 4.117 30.362 1.00 24.99 C ANISOU 396 C PRO A 54 2525 4886 2084 -142 -620 -658 C ATOM 397 O PRO A 54 24.386 3.868 30.192 1.00 28.76 O ANISOU 397 O PRO A 54 3011 5364 2551 -126 -636 -611 O ATOM 398 CB PRO A 54 21.808 2.771 28.772 1.00 24.31 C ANISOU 398 CB PRO A 54 2509 4663 2064 -173 -609 -563 C ATOM 399 CG PRO A 54 22.793 2.370 27.716 1.00 27.64 C ANISOU 399 CG PRO A 54 2975 4987 2540 -174 -635 -494 C ATOM 400 CD PRO A 54 23.093 3.635 26.957 1.00 27.25 C ANISOU 400 CD PRO A 54 2954 4789 2613 -208 -668 -566 C ATOM 401 N THR A 55 22.655 4.340 31.554 1.00 25.05 N ANISOU 401 N THR A 55 2480 5024 2014 -126 -595 -709 N ATOM 402 CA THR A 55 23.407 4.178 32.790 1.00 27.11 C ANISOU 402 CA THR A 55 2691 5447 2161 -87 -584 -698 C ATOM 403 C THR A 55 23.623 2.692 33.029 1.00 28.58 C ANISOU 403 C THR A 55 2886 5723 2249 -55 -562 -570 C ATOM 404 O THR A 55 22.916 1.869 32.465 1.00 26.39 O ANISOU 404 O THR A 55 2641 5410 1976 -64 -547 -503 O ATOM 405 CB THR A 55 22.595 4.711 33.976 1.00 29.04 C ANISOU 405 CB THR A 55 2877 5812 2346 -80 -558 -780 C ATOM 406 OG1 THR A 55 21.289 4.121 33.938 1.00 29.71 O ANISOU 406 OG1 THR A 55 2964 5916 2408 -93 -527 -763 O ATOM 407 CG2 THR A 55 22.458 6.221 33.890 1.00 30.76 C ANISOU 407 CG2 THR A 55 3082 5946 2659 -102 -580 -903 C ATOM 408 N PRO A 56 24.592 2.341 33.881 1.00 31.28 N ANISOU 408 N PRO A 56 3202 6177 2505 -16 -560 -529 N ATOM 409 CA PRO A 56 24.774 0.934 34.257 1.00 33.72 C ANISOU 409 CA PRO A 56 3522 6569 2720 20 -537 -397 C ATOM 410 C PRO A 56 23.479 0.288 34.758 1.00 33.23 C ANISOU 410 C PRO A 56 3453 6585 2588 19 -493 -357 C ATOM 411 O PRO A 56 23.240 -0.885 34.477 1.00 33.27 O ANISOU 411 O PRO A 56 3494 6581 2566 31 -474 -237 O ATOM 412 CB PRO A 56 25.797 1.013 35.392 1.00 33.67 C ANISOU 412 CB PRO A 56 3475 6687 2632 59 -541 -399 C ATOM 413 CG PRO A 56 26.584 2.241 35.089 1.00 34.10 C ANISOU 413 CG PRO A 56 3516 6675 2763 43 -577 -502 C ATOM 414 CD PRO A 56 25.590 3.217 34.517 1.00 32.81 C ANISOU 414 CD PRO A 56 3359 6417 2691 -2 -580 -598 C ATOM 415 N TYR A 57 22.662 1.043 35.491 1.00 31.08 N ANISOU 415 N TYR A 57 3136 6384 2290 5 -477 -453 N ATOM 416 CA TYR A 57 21.375 0.547 35.975 1.00 31.21 C ANISOU 416 CA TYR A 57 3140 6477 2241 -3 -432 -430 C ATOM 417 C TYR A 57 20.457 0.115 34.834 1.00 31.88 C ANISOU 417 C TYR A 57 3273 6445 2393 -35 -426 -397 C ATOM 418 O TYR A 57 19.905 -0.985 34.850 1.00 32.57 O ANISOU 418 O TYR A 57 3385 6562 2427 -28 -391 -285 O ATOM 419 CB TYR A 57 20.673 1.614 36.823 1.00 31.66 C ANISOU 419 CB TYR A 57 3136 6612 2281 -16 -421 -565 C ATOM 420 CG TYR A 57 19.194 1.365 37.042 1.00 32.40 C ANISOU 420 CG TYR A 57 3218 6752 2342 -39 -378 -577 C ATOM 421 CD1 TYR A 57 18.757 0.391 37.928 1.00 33.23 C ANISOU 421 CD1 TYR A 57 3313 6988 2324 -22 -329 -483 C ATOM 422 CD2 TYR A 57 18.237 2.115 36.370 1.00 30.76 C ANISOU 422 CD2 TYR A 57 3010 6446 2231 -79 -383 -682 C ATOM 423 CE1 TYR A 57 17.405 0.165 38.137 1.00 30.40 C ANISOU 423 CE1 TYR A 57 2943 6673 1933 -47 -283 -493 C ATOM 424 CE2 TYR A 57 16.880 1.898 36.575 1.00 28.70 C ANISOU 424 CE2 TYR A 57 2735 6229 1942 -102 -342 -703 C ATOM 425 CZ TYR A 57 16.473 0.920 37.455 1.00 30.51 C ANISOU 425 CZ TYR A 57 2953 6600 2041 -87 -290 -609 C ATOM 426 OH TYR A 57 15.127 0.704 37.658 1.00 33.93 O ANISOU 426 OH TYR A 57 3373 7076 2442 -114 -242 -629 O ATOM 427 N SER A 58 20.282 0.994 33.854 1.00 28.89 N ANISOU 427 N SER A 58 2911 5929 2139 -70 -458 -489 N ATOM 428 CA SER A 58 19.381 0.712 32.743 1.00 29.27 C ANISOU 428 CA SER A 58 3001 5858 2262 -104 -458 -476 C ATOM 429 C SER A 58 19.910 -0.425 31.885 1.00 30.73 C ANISOU 429 C SER A 58 3242 5977 2459 -90 -466 -336 C ATOM 430 O SER A 58 19.154 -1.287 31.448 1.00 32.07 O ANISOU 430 O SER A 58 3440 6124 2620 -98 -444 -256 O ATOM 431 CB SER A 58 19.164 1.962 31.899 1.00 26.89 C ANISOU 431 CB SER A 58 2708 5403 2104 -142 -494 -601 C ATOM 432 OG SER A 58 18.651 3.012 32.693 1.00 28.70 O ANISOU 432 OG SER A 58 2887 5681 2334 -148 -485 -724 O ATOM 433 N LYS A 59 21.215 -0.426 31.645 1.00 29.11 N ANISOU 433 N LYS A 59 3048 5737 2275 -69 -495 -306 N ATOM 434 CA LYS A 59 21.840 -1.504 30.890 1.00 28.24 C ANISOU 434 CA LYS A 59 2985 5565 2178 -49 -502 -177 C ATOM 435 C LYS A 59 21.573 -2.852 31.560 1.00 29.29 C ANISOU 435 C LYS A 59 3127 5793 2208 -14 -458 -35 C ATOM 436 O LYS A 59 21.179 -3.821 30.907 1.00 28.77 O ANISOU 436 O LYS A 59 3104 5666 2162 -11 -443 72 O ATOM 437 CB LYS A 59 23.343 -1.260 30.767 1.00 33.46 C ANISOU 437 CB LYS A 59 3647 6203 2864 -29 -535 -180 C ATOM 438 CG LYS A 59 24.103 -2.370 30.064 1.00 39.50 C ANISOU 438 CG LYS A 59 4454 6909 3646 -4 -542 -55 C ATOM 439 CD LYS A 59 25.534 -1.945 29.767 1.00 45.56 C ANISOU 439 CD LYS A 59 5220 7637 4453 5 -577 -85 C ATOM 440 CE LYS A 59 26.315 -3.068 29.098 1.00 52.06 C ANISOU 440 CE LYS A 59 6079 8405 5295 33 -583 30 C ATOM 441 NZ LYS A 59 27.714 -2.661 28.774 1.00 54.88 N ANISOU 441 NZ LYS A 59 6433 8729 5691 37 -615 -4 N ATOM 442 N GLN A 60 21.784 -2.901 32.870 1.00 28.26 N ANISOU 442 N GLN A 60 2959 5803 1977 14 -435 -30 N ATOM 443 CA GLN A 60 21.606 -4.124 33.637 1.00 27.66 C ANISOU 443 CA GLN A 60 2893 5809 1808 47 -391 106 C ATOM 444 C GLN A 60 20.220 -4.734 33.420 1.00 30.70 C ANISOU 444 C GLN A 60 3301 6179 2183 26 -345 166 C ATOM 445 O GLN A 60 20.087 -5.929 33.165 1.00 30.18 O ANISOU 445 O GLN A 60 3280 6071 2118 44 -319 308 O ATOM 446 CB GLN A 60 21.851 -3.839 35.123 1.00 32.92 C ANISOU 446 CB GLN A 60 3507 6632 2370 69 -375 73 C ATOM 447 CG GLN A 60 21.504 -4.974 36.059 1.00 37.98 C ANISOU 447 CG GLN A 60 4155 7361 2913 96 -327 200 C ATOM 448 CD GLN A 60 21.647 -4.580 37.523 1.00 42.06 C ANISOU 448 CD GLN A 60 4617 8038 3327 111 -315 153 C ATOM 449 OE1 GLN A 60 22.209 -3.534 37.847 1.00 41.59 O ANISOU 449 OE1 GLN A 60 4514 8019 3270 112 -346 36 O ATOM 450 NE2 GLN A 60 21.130 -5.415 38.412 1.00 43.71 N ANISOU 450 NE2 GLN A 60 4829 8331 3450 124 -269 247 N ATOM 451 N HIS A 61 19.184 -3.909 33.502 1.00 32.68 N ANISOU 451 N HIS A 61 3524 6456 2437 -13 -335 53 N ATOM 452 CA HIS A 61 17.820 -4.415 33.393 1.00 24.96 C ANISOU 452 CA HIS A 61 2563 5479 1441 -38 -285 97 C ATOM 453 C HIS A 61 17.353 -4.589 31.958 1.00 28.59 C ANISOU 453 C HIS A 61 3071 5792 2001 -66 -304 114 C ATOM 454 O HIS A 61 16.450 -5.382 31.688 1.00 28.40 O ANISOU 454 O HIS A 61 3081 5680 2028 -75 -245 200 O ATOM 455 CB HIS A 61 16.872 -3.520 34.170 1.00 28.54 C ANISOU 455 CB HIS A 61 2962 6031 1850 -67 -262 -38 C ATOM 456 CG HIS A 61 17.194 -3.453 35.628 1.00 34.53 C ANISOU 456 CG HIS A 61 3674 6943 2504 -40 -239 -42 C ATOM 457 ND1 HIS A 61 17.063 -4.540 36.464 1.00 37.31 N ANISOU 457 ND1 HIS A 61 4035 7374 2765 -16 -187 95 N ATOM 458 CD2 HIS A 61 17.670 -2.443 36.393 1.00 36.63 C ANISOU 458 CD2 HIS A 61 3882 7287 2748 -33 -264 -162 C ATOM 459 CE1 HIS A 61 17.427 -4.198 37.687 1.00 39.82 C ANISOU 459 CE1 HIS A 61 4304 7823 3002 3 -184 56 C ATOM 460 NE2 HIS A 61 17.800 -2.931 37.671 1.00 39.78 N ANISOU 460 NE2 HIS A 61 4256 7824 3034 -5 -229 -99 N ATOM 461 N THR A 62 17.962 -3.842 31.042 1.00 25.06 N ANISOU 461 N THR A 62 2628 5241 1652 -80 -367 29 N ATOM 462 CA THR A 62 17.723 -4.047 29.618 1.00 23.75 C ANISOU 462 CA THR A 62 2514 4866 1643 -102 -377 52 C ATOM 463 C THR A 62 18.188 -5.446 29.231 1.00 26.49 C ANISOU 463 C THR A 62 2912 5158 1996 -64 -357 235 C ATOM 464 O THR A 62 17.532 -6.140 28.454 1.00 23.66 O ANISOU 464 O THR A 62 2599 4651 1739 -73 -323 307 O ATOM 465 CB THR A 62 18.456 -2.999 28.767 1.00 21.22 C ANISOU 465 CB THR A 62 2187 4471 1404 -125 -454 -62 C ATOM 466 OG1 THR A 62 17.926 -1.698 29.051 1.00 23.09 O ANISOU 466 OG1 THR A 62 2382 4731 1661 -162 -474 -233 O ATOM 467 CG2 THR A 62 18.283 -3.295 27.277 1.00 19.84 C ANISOU 467 CG2 THR A 62 2070 4080 1387 -145 -462 -26 C ATOM 468 N ILE A 63 19.316 -5.865 29.797 1.00 28.45 N ANISOU 468 N ILE A 63 3149 5511 2148 -20 -376 304 N ATOM 469 CA ILE A 63 19.837 -7.201 29.540 1.00 24.86 C ANISOU 469 CA ILE A 63 2738 4996 1710 21 -359 467 C ATOM 470 C ILE A 63 18.880 -8.286 30.036 1.00 31.14 C ANISOU 470 C ILE A 63 3557 5812 2464 31 -290 596 C ATOM 471 O ILE A 63 18.509 -9.191 29.282 1.00 34.98 O ANISOU 471 O ILE A 63 4090 6177 3025 35 -268 704 O ATOM 472 CB ILE A 63 21.221 -7.386 30.175 1.00 25.46 C ANISOU 472 CB ILE A 63 2800 5123 1750 65 -377 484 C ATOM 473 CG1 ILE A 63 22.276 -6.646 29.349 1.00 24.50 C ANISOU 473 CG1 ILE A 63 2676 4932 1703 57 -436 399 C ATOM 474 CG2 ILE A 63 21.559 -8.861 30.303 1.00 26.12 C ANISOU 474 CG2 ILE A 63 2922 5170 1834 108 -349 644 C ATOM 475 CD1 ILE A 63 23.614 -6.530 30.034 1.00 29.75 C ANISOU 475 CD1 ILE A 63 3315 5662 2326 91 -455 382 C ATOM 476 N THR A 64 18.463 -8.180 31.294 1.00 28.14 N ANISOU 476 N THR A 64 3143 5567 1982 31 -251 580 N ATOM 477 CA THR A 64 17.509 -9.126 31.864 1.00 32.34 C ANISOU 477 CA THR A 64 3691 6121 2474 31 -178 692 C ATOM 478 C THR A 64 16.222 -9.191 31.032 1.00 29.02 C ANISOU 478 C THR A 64 3297 5573 2157 -10 -139 688 C ATOM 479 O THR A 64 15.743 -10.277 30.699 1.00 27.84 O ANISOU 479 O THR A 64 3190 5329 2060 -4 -97 817 O ATOM 480 CB THR A 64 17.169 -8.778 33.325 1.00 34.49 C ANISOU 480 CB THR A 64 3914 6562 2627 27 -144 645 C ATOM 481 OG1 THR A 64 18.381 -8.598 34.068 1.00 37.91 O ANISOU 481 OG1 THR A 64 4322 7072 3011 63 -180 622 O ATOM 482 CG2 THR A 64 16.352 -9.890 33.967 1.00 38.82 C ANISOU 482 CG2 THR A 64 4484 7127 3141 29 -70 776 C ATOM 483 N LEU A 65 15.666 -8.032 30.694 1.00 28.82 N ANISOU 483 N LEU A 65 3247 5505 2199 -52 -152 525 N ATOM 484 CA LEU A 65 14.424 -7.990 29.919 1.00 29.22 C ANISOU 484 CA LEU A 65 3318 5395 2387 -92 -115 489 C ATOM 485 C LEU A 65 14.571 -8.710 28.582 1.00 27.39 C ANISOU 485 C LEU A 65 3146 4964 2296 -84 -128 573 C ATOM 486 O LEU A 65 13.732 -9.534 28.216 1.00 27.40 O ANISOU 486 O LEU A 65 3182 4860 2370 -91 -78 657 O ATOM 487 CB LEU A 65 13.949 -6.548 29.715 1.00 29.53 C ANISOU 487 CB LEU A 65 3322 5417 2482 -133 -143 292 C ATOM 488 CG LEU A 65 13.244 -5.886 30.903 1.00 36.75 C ANISOU 488 CG LEU A 65 4177 6490 3297 -152 -110 193 C ATOM 489 CD1 LEU A 65 13.220 -4.372 30.758 1.00 32.70 C ANISOU 489 CD1 LEU A 65 3622 5979 2823 -181 -166 -8 C ATOM 490 CD2 LEU A 65 11.836 -6.444 31.060 1.00 37.99 C ANISOU 490 CD2 LEU A 65 4341 6607 3487 -176 -29 232 C ATOM 491 N ALA A 66 15.647 -8.406 27.863 1.00 28.61 N ANISOU 491 N ALA A 66 3312 5071 2488 -70 -194 550 N ATOM 492 CA ALA A 66 15.898 -9.010 26.559 1.00 26.97 C ANISOU 492 CA ALA A 66 3156 4684 2409 -62 -212 616 C ATOM 493 C ALA A 66 16.111 -10.518 26.649 1.00 23.89 C ANISOU 493 C ALA A 66 2800 4278 1997 -19 -182 802 C ATOM 494 O ALA A 66 15.469 -11.288 25.937 1.00 28.04 O ANISOU 494 O ALA A 66 3365 4660 2627 -22 -151 874 O ATOM 495 CB ALA A 66 17.100 -8.344 25.889 1.00 26.25 C ANISOU 495 CB ALA A 66 3061 4572 2341 -57 -288 550 C ATOM 496 N ARG A 67 17.020 -10.933 27.522 1.00 25.42 N ANISOU 496 N ARG A 67 2979 4619 2062 22 -195 877 N ATOM 497 CA ARG A 67 17.344 -12.347 27.698 1.00 28.96 C ANISOU 497 CA ARG A 67 3458 5058 2487 66 -176 1051 C ATOM 498 C ARG A 67 16.118 -13.180 28.087 1.00 30.51 C ANISOU 498 C ARG A 67 3673 5227 2693 53 -100 1143 C ATOM 499 O ARG A 67 15.842 -14.216 27.482 1.00 31.31 O ANISOU 499 O ARG A 67 3815 5178 2902 65 -79 1229 O ATOM 500 CB ARG A 67 18.441 -12.502 28.756 1.00 33.18 C ANISOU 500 CB ARG A 67 3968 5707 2931 103 -193 1048 C ATOM 501 CG ARG A 67 19.325 -13.729 28.581 1.00 39.97 C ANISOU 501 CG ARG A 67 4862 6478 3849 149 -203 1138 C ATOM 502 CD ARG A 67 20.276 -13.885 29.764 1.00 47.97 C ANISOU 502 CD ARG A 67 5851 7616 4761 181 -216 1143 C ATOM 503 NE ARG A 67 19.551 -13.856 31.034 1.00 53.40 N ANISOU 503 NE ARG A 67 6514 8431 5342 169 -172 1161 N ATOM 504 CZ ARG A 67 19.770 -12.975 32.006 1.00 57.57 C ANISOU 504 CZ ARG A 67 6996 9118 5761 164 -180 1082 C ATOM 505 NH1 ARG A 67 20.710 -12.049 31.869 1.00 61.60 N ANISOU 505 NH1 ARG A 67 7477 9670 6257 170 -232 981 N ATOM 506 NH2 ARG A 67 19.055 -13.024 33.122 1.00 56.25 N ANISOU 506 NH2 ARG A 67 6809 9062 5502 152 -135 1099 N ATOM 507 N GLU A 68 15.387 -12.716 29.094 1.00 28.88 N ANISOU 507 N GLU A 68 3432 5148 2392 27 -58 1099 N ATOM 508 CA GLU A 68 14.211 -13.430 29.583 1.00 32.25 C ANISOU 508 CA GLU A 68 3868 5573 2813 8 19 1181 C ATOM 509 C GLU A 68 13.068 -13.480 28.567 1.00 33.56 C ANISOU 509 C GLU A 68 4059 5549 3143 -29 52 1148 C ATOM 510 O GLU A 68 12.421 -14.515 28.409 1.00 36.91 O ANISOU 510 O GLU A 68 4514 5890 3619 -29 98 1265 O ATOM 511 CB GLU A 68 13.729 -12.822 30.900 1.00 41.43 C ANISOU 511 CB GLU A 68 4982 6924 3837 -15 56 1118 C ATOM 512 CG GLU A 68 14.667 -13.076 32.070 1.00 54.57 C ANISOU 512 CG GLU A 68 6626 8716 5391 23 38 1143 C ATOM 513 CD GLU A 68 14.923 -14.555 32.301 1.00 63.12 C ANISOU 513 CD GLU A 68 7750 9718 6514 56 53 1284 C ATOM 514 OE1 GLU A 68 13.960 -15.283 32.630 1.00 66.63 O ANISOU 514 OE1 GLU A 68 8209 10137 6969 37 114 1359 O ATOM 515 OE2 GLU A 68 16.086 -14.990 32.147 1.00 64.80 O ANISOU 515 OE2 GLU A 68 7979 9892 6750 97 4 1312 O ATOM 516 N LEU A 69 12.814 -12.367 27.886 1.00 28.94 N ANISOU 516 N LEU A 69 3461 4895 2642 -60 24 990 N ATOM 517 CA LEU A 69 11.772 -12.331 26.864 1.00 31.31 C ANISOU 517 CA LEU A 69 3785 5011 3101 -93 46 948 C ATOM 518 C LEU A 69 12.098 -13.328 25.760 1.00 30.61 C ANISOU 518 C LEU A 69 3750 4756 3126 -66 29 1058 C ATOM 519 O LEU A 69 11.253 -14.131 25.371 1.00 32.88 O ANISOU 519 O LEU A 69 4065 4928 3498 -73 73 1131 O ATOM 520 CB LEU A 69 11.610 -10.922 26.290 1.00 33.92 C ANISOU 520 CB LEU A 69 4095 5294 3499 -127 4 761 C ATOM 521 CG LEU A 69 10.691 -9.983 27.073 1.00 35.80 C ANISOU 521 CG LEU A 69 4284 5627 3692 -165 34 631 C ATOM 522 CD1 LEU A 69 10.872 -8.543 26.626 1.00 33.96 C ANISOU 522 CD1 LEU A 69 4028 5371 3504 -190 -27 451 C ATOM 523 CD2 LEU A 69 9.246 -10.419 26.914 1.00 35.06 C ANISOU 523 CD2 LEU A 69 4199 5441 3681 -195 102 647 C ATOM 524 N ALA A 70 13.335 -13.283 25.274 1.00 27.60 N ANISOU 524 N ALA A 70 3380 4365 2743 -34 -34 1066 N ATOM 525 CA ALA A 70 13.790 -14.220 24.254 1.00 33.01 C ANISOU 525 CA ALA A 70 4110 4908 3524 -3 -55 1165 C ATOM 526 C ALA A 70 13.721 -15.657 24.761 1.00 35.94 C ANISOU 526 C ALA A 70 4502 5282 3873 30 -17 1322 C ATOM 527 O ALA A 70 13.369 -16.568 24.013 1.00 35.50 O ANISOU 527 O ALA A 70 4483 5060 3946 39 -3 1347 O ATOM 528 CB ALA A 70 15.204 -13.881 23.804 1.00 33.16 C ANISOU 528 CB ALA A 70 4126 4946 3526 24 -128 1137 C ATOM 529 N LYS A 71 14.061 -15.854 26.031 1.00 37.00 N ANISOU 529 N LYS A 71 4613 5568 3879 45 -3 1350 N ATOM 530 CA LYS A 71 13.992 -17.176 26.643 1.00 40.53 C ANISOU 530 CA LYS A 71 5079 5991 4328 68 29 1434 C ATOM 531 C LYS A 71 12.557 -17.705 26.621 1.00 42.28 C ANISOU 531 C LYS A 71 5315 6137 4613 37 95 1477 C ATOM 532 O LYS A 71 12.329 -18.899 26.444 1.00 44.96 O ANISOU 532 O LYS A 71 5687 6367 5029 50 110 1530 O ATOM 533 CB LYS A 71 14.522 -17.126 28.079 1.00 43.29 C ANISOU 533 CB LYS A 71 5398 6526 4523 83 31 1452 C ATOM 534 CG LYS A 71 14.708 -18.487 28.735 1.00 46.37 C ANISOU 534 CG LYS A 71 5811 6898 4909 109 45 1543 C ATOM 535 CD LYS A 71 15.070 -18.340 30.207 1.00 50.70 C ANISOU 535 CD LYS A 71 6330 7632 5303 116 52 1560 C ATOM 536 CE LYS A 71 15.025 -19.682 30.930 1.00 55.72 C ANISOU 536 CE LYS A 71 6991 8253 5929 131 72 1662 C ATOM 537 NZ LYS A 71 15.196 -19.526 32.403 1.00 58.44 N ANISOU 537 NZ LYS A 71 7308 8776 6123 132 86 1681 N ATOM 538 N ASN A 72 11.593 -16.805 26.787 1.00 34.38 N ANISOU 538 N ASN A 72 4236 4919 3909 -192 -89 72 N ATOM 539 CA ASN A 72 10.183 -17.182 26.792 1.00 39.85 C ANISOU 539 CA ASN A 72 4945 5613 4583 -220 -87 50 C ATOM 540 C ASN A 72 9.522 -17.174 25.410 1.00 43.62 C ANISOU 540 C ASN A 72 5473 6005 5097 -211 -80 33 C ATOM 541 O ASN A 72 8.299 -17.262 25.300 1.00 47.07 O ANISOU 541 O ASN A 72 5920 6440 5525 -233 -81 2 O ATOM 542 CB ASN A 72 9.397 -16.295 27.762 1.00 44.43 C ANISOU 542 CB ASN A 72 5470 6271 5140 -250 -105 -17 C ATOM 543 CG ASN A 72 9.604 -16.690 29.212 1.00 48.89 C ANISOU 543 CG ASN A 72 5994 6927 5653 -271 -109 6 C ATOM 544 OD1 ASN A 72 8.748 -17.334 29.819 1.00 52.75 O ANISOU 544 OD1 ASN A 72 6483 7455 6105 -299 -106 12 O ATOM 545 ND2 ASN A 72 10.747 -16.312 29.773 1.00 48.23 N ANISOU 545 ND2 ASN A 72 5878 6880 5568 -258 -116 19 N ATOM 546 N GLY A 73 10.331 -17.056 24.363 1.00 42.94 N ANISOU 546 N GLY A 73 5416 5851 5050 -178 -73 51 N ATOM 547 CA GLY A 73 9.841 -17.213 23.006 1.00 38.75 C ANISOU 547 CA GLY A 73 4938 5236 4551 -167 -64 46 C ATOM 548 C GLY A 73 9.404 -15.948 22.291 1.00 32.76 C ANISOU 548 C GLY A 73 4171 4448 3826 -166 -78 -21 C ATOM 549 O GLY A 73 8.848 -16.020 21.199 1.00 32.35 O ANISOU 549 O GLY A 73 4162 4332 3798 -160 -73 -30 O ATOM 550 N ALA A 74 9.635 -14.791 22.898 1.00 31.15 N ANISOU 550 N ALA A 74 3916 4293 3627 -170 -96 -67 N ATOM 551 CA ALA A 74 9.320 -13.533 22.234 1.00 26.36 C ANISOU 551 CA ALA A 74 3300 3658 3057 -167 -112 -129 C ATOM 552 C ALA A 74 10.496 -13.116 21.361 1.00 22.77 C ANISOU 552 C ALA A 74 2860 3152 2642 -135 -108 -109 C ATOM 553 O ALA A 74 11.625 -13.560 21.578 1.00 23.68 O ANISOU 553 O ALA A 74 2973 3273 2751 -118 -98 -59 O ATOM 554 CB ALA A 74 9.012 -12.456 23.248 1.00 25.26 C ANISOU 554 CB ALA A 74 3099 3591 2907 -186 -134 -191 C ATOM 555 N VAL A 75 10.231 -12.271 20.373 1.00 18.20 N ANISOU 555 N VAL A 75 2295 2521 2101 -128 -117 -147 N ATOM 556 CA VAL A 75 11.314 -11.708 19.566 1.00 21.00 C ANISOU 556 CA VAL A 75 2657 2830 2493 -101 -116 -135 C ATOM 557 C VAL A 75 11.444 -10.226 19.883 1.00 22.42 C ANISOU 557 C VAL A 75 2789 3037 2694 -106 -141 -195 C ATOM 558 O VAL A 75 10.442 -9.513 19.951 1.00 20.05 O ANISOU 558 O VAL A 75 2473 2745 2400 -123 -158 -254 O ATOM 559 CB VAL A 75 11.098 -11.930 18.048 1.00 21.07 C ANISOU 559 CB VAL A 75 2724 2751 2531 -85 -104 -124 C ATOM 560 CG1 VAL A 75 9.763 -11.374 17.601 1.00 22.14 C ANISOU 560 CG1 VAL A 75 2867 2865 2679 -102 -119 -180 C ATOM 561 CG2 VAL A 75 12.224 -11.281 17.241 1.00 23.65 C ANISOU 561 CG2 VAL A 75 3055 3036 2895 -60 -104 -112 C ATOM 562 N ILE A 76 12.679 -9.776 20.099 1.00 19.17 N ANISOU 562 N ILE A 76 2351 2639 2293 -92 -144 -179 N ATOM 563 CA ILE A 76 12.952 -8.374 20.387 1.00 15.94 C ANISOU 563 CA ILE A 76 1896 2252 1907 -95 -168 -231 C ATOM 564 C ILE A 76 13.156 -7.602 19.090 1.00 17.54 C ANISOU 564 C ILE A 76 2124 2383 2159 -80 -173 -245 C ATOM 565 O ILE A 76 13.933 -8.009 18.240 1.00 15.91 O ANISOU 565 O ILE A 76 1950 2127 1966 -59 -156 -199 O ATOM 566 CB ILE A 76 14.214 -8.215 21.264 1.00 17.37 C ANISOU 566 CB ILE A 76 2036 2486 2077 -89 -171 -208 C ATOM 567 CG1 ILE A 76 14.031 -8.930 22.611 1.00 21.19 C ANISOU 567 CG1 ILE A 76 2493 3047 2511 -106 -168 -195 C ATOM 568 CG2 ILE A 76 14.560 -6.732 21.450 1.00 19.53 C ANISOU 568 CG2 ILE A 76 2266 2775 2380 -93 -196 -262 C ATOM 569 CD1 ILE A 76 12.708 -8.668 23.271 1.00 27.34 C ANISOU 569 CD1 ILE A 76 3251 3868 3269 -134 -181 -251 C ATOM 570 N VAL A 77 12.443 -6.493 18.944 1.00 15.40 N ANISOU 570 N VAL A 77 1835 2105 1910 -91 -196 -309 N ATOM 571 CA VAL A 77 12.582 -5.630 17.788 1.00 15.86 C ANISOU 571 CA VAL A 77 1912 2099 2016 -80 -205 -327 C ATOM 572 C VAL A 77 13.282 -4.339 18.184 1.00 16.62 C ANISOU 572 C VAL A 77 1961 2218 2136 -80 -228 -361 C ATOM 573 O VAL A 77 12.914 -3.699 19.166 1.00 20.09 O ANISOU 573 O VAL A 77 2355 2713 2567 -97 -248 -410 O ATOM 574 CB VAL A 77 11.204 -5.280 17.192 1.00 17.40 C ANISOU 574 CB VAL A 77 2126 2259 2224 -91 -217 -374 C ATOM 575 CG1 VAL A 77 11.370 -4.591 15.838 1.00 16.37 C ANISOU 575 CG1 VAL A 77 2025 2054 2140 -77 -223 -379 C ATOM 576 CG2 VAL A 77 10.360 -6.541 17.054 1.00 17.02 C ANISOU 576 CG2 VAL A 77 2116 2203 2146 -97 -197 -348 C ATOM 577 N SER A 78 14.293 -3.951 17.417 1.00 11.45 N ANISOU 577 N SER A 78 1316 1522 1512 -63 -225 -337 N ATOM 578 CA SER A 78 14.926 -2.669 17.656 1.00 13.49 C ANISOU 578 CA SER A 78 1533 1792 1799 -65 -248 -370 C ATOM 579 C SER A 78 15.598 -2.126 16.393 1.00 13.12 C ANISOU 579 C SER A 78 1513 1678 1796 -50 -248 -354 C ATOM 580 O SER A 78 15.386 -2.647 15.292 1.00 11.55 O ANISOU 580 O SER A 78 1363 1420 1605 -39 -232 -326 O ATOM 581 CB SER A 78 15.902 -2.770 18.828 1.00 15.91 C ANISOU 581 CB SER A 78 1795 2167 2082 -67 -248 -353 C ATOM 582 OG SER A 78 16.206 -1.483 19.339 1.00 18.86 O ANISOU 582 OG SER A 78 2121 2567 2478 -76 -275 -401 O ATOM 583 N GLY A 79 16.379 -1.063 16.553 1.00 15.67 N ANISOU 583 N GLY A 79 1801 2009 2146 -50 -266 -372 N ATOM 584 CA GLY A 79 16.970 -0.354 15.435 1.00 15.05 C ANISOU 584 CA GLY A 79 1739 1870 2110 -40 -270 -363 C ATOM 585 C GLY A 79 18.478 -0.473 15.318 1.00 18.56 C ANISOU 585 C GLY A 79 2176 2318 2559 -25 -256 -312 C ATOM 586 O GLY A 79 19.082 0.165 14.457 1.00 19.30 O ANISOU 586 O GLY A 79 2278 2367 2687 -19 -260 -303 O ATOM 587 N GLY A 80 19.088 -1.290 16.173 1.00 17.60 N ANISOU 587 N GLY A 80 2038 2247 2403 -21 -241 -277 N ATOM 588 CA GLY A 80 20.523 -1.522 16.130 1.00 15.18 C ANISOU 588 CA GLY A 80 1722 1948 2098 -6 -226 -225 C ATOM 589 C GLY A 80 21.406 -0.359 16.558 1.00 17.40 C ANISOU 589 C GLY A 80 1954 2253 2403 -12 -248 -247 C ATOM 590 O GLY A 80 22.617 -0.377 16.322 1.00 16.68 O ANISOU 590 O GLY A 80 1856 2159 2322 0 -238 -206 O ATOM 591 N ALA A 81 20.806 0.654 17.173 1.00 17.00 N ANISOU 591 N ALA A 81 1870 2227 2364 -32 -279 -311 N ATOM 592 CA ALA A 81 21.530 1.860 17.581 1.00 16.82 C ANISOU 592 CA ALA A 81 1801 2224 2368 -41 -304 -340 C ATOM 593 C ALA A 81 22.503 1.614 18.738 1.00 11.36 C ANISOU 593 C ALA A 81 1064 1603 1649 -42 -302 -319 C ATOM 594 O ALA A 81 22.410 0.605 19.432 1.00 16.33 O ANISOU 594 O ALA A 81 1693 2274 2237 -39 -286 -295 O ATOM 595 CB ALA A 81 20.547 2.957 17.960 1.00 18.07 C ANISOU 595 CB ALA A 81 1934 2387 2543 -60 -337 -417 C ATOM 596 N LEU A 82 23.435 2.543 18.933 1.00 17.76 N ANISOU 596 N LEU A 82 1839 2426 2485 -46 -319 -329 N ATOM 597 CA LEU A 82 24.303 2.517 20.104 1.00 19.32 C ANISOU 597 CA LEU A 82 1988 2694 2660 -51 -323 -321 C ATOM 598 C LEU A 82 23.429 2.538 21.353 1.00 19.61 C ANISOU 598 C LEU A 82 1993 2792 2664 -68 -339 -369 C ATOM 599 O LEU A 82 22.347 3.133 21.347 1.00 21.75 O ANISOU 599 O LEU A 82 2265 3051 2946 -81 -357 -427 O ATOM 600 CB LEU A 82 25.231 3.736 20.115 1.00 23.42 C ANISOU 600 CB LEU A 82 2471 3213 3216 -58 -346 -339 C ATOM 601 CG LEU A 82 26.072 4.017 18.863 1.00 26.47 C ANISOU 601 CG LEU A 82 2880 3537 3640 -46 -336 -301 C ATOM 602 CD1 LEU A 82 26.976 5.226 19.061 1.00 24.07 C ANISOU 602 CD1 LEU A 82 2533 3242 3369 -57 -361 -321 C ATOM 603 CD2 LEU A 82 26.896 2.802 18.468 1.00 31.62 C ANISOU 603 CD2 LEU A 82 3557 4186 4272 -23 -300 -224 C ATOM 604 N GLY A 83 23.899 1.899 22.419 1.00 21.09 N ANISOU 604 N GLY A 83 2153 3048 2812 -69 -332 -346 N ATOM 605 CA GLY A 83 23.214 1.951 23.699 1.00 23.56 C ANISOU 605 CA GLY A 83 2431 3430 3091 -88 -347 -391 C ATOM 606 C GLY A 83 22.127 0.911 23.876 1.00 20.74 C ANISOU 606 C GLY A 83 2102 3083 2696 -89 -331 -384 C ATOM 607 O GLY A 83 22.344 -0.278 23.632 1.00 21.41 O ANISOU 607 O GLY A 83 2218 3160 2759 -74 -303 -323 O ATOM 608 N VAL A 84 20.952 1.366 24.305 1.00 17.98 N ANISOU 608 N VAL A 84 1756 2736 2339 -103 -338 -435 N ATOM 609 CA VAL A 84 19.834 0.478 24.621 1.00 18.74 C ANISOU 609 CA VAL A 84 1866 2854 2398 -109 -328 -440 C ATOM 610 C VAL A 84 19.502 -0.538 23.515 1.00 20.11 C ANISOU 610 C VAL A 84 2091 2976 2574 -96 -308 -399 C ATOM 611 O VAL A 84 19.355 -1.731 23.789 1.00 18.26 O ANISOU 611 O VAL A 84 1874 2761 2302 -92 -287 -357 O ATOM 612 CB VAL A 84 18.566 1.285 24.988 1.00 21.74 C ANISOU 612 CB VAL A 84 2268 3211 2780 -117 -322 -482 C ATOM 613 CG1 VAL A 84 17.364 0.364 25.129 1.00 21.53 C ANISOU 613 CG1 VAL A 84 2260 3198 2722 -123 -311 -486 C ATOM 614 CG2 VAL A 84 18.791 2.083 26.270 1.00 20.03 C ANISOU 614 CG2 VAL A 84 2028 3031 2550 -123 -322 -498 C ATOM 615 N ASP A 85 19.375 -0.062 22.276 1.00 21.57 N ANISOU 615 N ASP A 85 2309 3086 2803 -86 -309 -405 N ATOM 616 CA ASP A 85 19.028 -0.927 21.145 1.00 18.43 C ANISOU 616 CA ASP A 85 1970 2624 2408 -72 -285 -363 C ATOM 617 C ASP A 85 19.943 -2.145 21.091 1.00 19.94 C ANISOU 617 C ASP A 85 2181 2820 2576 -54 -256 -285 C ATOM 618 O ASP A 85 19.492 -3.290 21.166 1.00 18.52 O ANISOU 618 O ASP A 85 2028 2644 2365 -51 -236 -253 O ATOM 619 CB ASP A 85 19.161 -0.169 19.815 1.00 18.80 C ANISOU 619 CB ASP A 85 2044 2593 2506 -63 -290 -370 C ATOM 620 CG ASP A 85 18.005 0.786 19.541 1.00 25.83 C ANISOU 620 CG ASP A 85 2933 3458 3422 -76 -315 -439 C ATOM 621 OD1 ASP A 85 17.358 1.269 20.499 1.00 27.18 O ANISOU 621 OD1 ASP A 85 3070 3677 3581 -92 -333 -492 O ATOM 622 OD2 ASP A 85 17.755 1.065 18.343 1.00 27.19 O ANISOU 622 OD2 ASP A 85 3142 3561 3628 -69 -314 -438 O ATOM 623 N ILE A 86 21.240 -1.887 20.969 1.00 19.18 N ANISOU 623 N ILE A 86 2069 2722 2495 -42 -254 -255 N ATOM 624 CA ILE A 86 22.203 -2.939 20.658 1.00 18.74 C ANISOU 624 CA ILE A 86 2035 2657 2428 -20 -226 -180 C ATOM 625 C ILE A 86 22.484 -3.827 21.867 1.00 20.45 C ANISOU 625 C ILE A 86 2227 2944 2597 -23 -218 -150 C ATOM 626 O ILE A 86 22.856 -4.989 21.724 1.00 24.62 O ANISOU 626 O ILE A 86 2782 3466 3107 -6 -194 -90 O ATOM 627 CB ILE A 86 23.502 -2.341 20.086 1.00 15.55 C ANISOU 627 CB ILE A 86 1621 2229 2058 -7 -226 -157 C ATOM 628 CG1 ILE A 86 24.276 -3.387 19.265 1.00 12.26 C ANISOU 628 CG1 ILE A 86 1242 1774 1640 20 -193 -84 C ATOM 629 CG2 ILE A 86 24.328 -1.698 21.193 1.00 17.63 C ANISOU 629 CG2 ILE A 86 1824 2558 2316 -17 -245 -171 C ATOM 630 CD1 ILE A 86 23.624 -3.709 17.923 1.00 8.81 C ANISOU 630 CD1 ILE A 86 866 1262 1222 30 -178 -77 C ATOM 631 N ILE A 87 22.287 -3.284 23.063 1.00 23.11 N ANISOU 631 N ILE A 87 2516 3348 2916 -43 -240 -192 N ATOM 632 CA ILE A 87 22.325 -4.104 24.265 1.00 23.58 C ANISOU 632 CA ILE A 87 2554 3480 2927 -50 -235 -170 C ATOM 633 C ILE A 87 21.176 -5.109 24.232 1.00 21.84 C ANISOU 633 C ILE A 87 2369 3251 2677 -55 -221 -161 C ATOM 634 O ILE A 87 21.383 -6.307 24.417 1.00 22.80 O ANISOU 634 O ILE A 87 2509 3382 2770 -45 -201 -105 O ATOM 635 CB ILE A 87 22.249 -3.238 25.537 1.00 24.73 C ANISOU 635 CB ILE A 87 2640 3701 3058 -73 -263 -224 C ATOM 636 CG1 ILE A 87 23.498 -2.361 25.644 1.00 24.57 C ANISOU 636 CG1 ILE A 87 2582 3692 3062 -69 -277 -225 C ATOM 637 CG2 ILE A 87 22.110 -4.103 26.781 1.00 23.38 C ANISOU 637 CG2 ILE A 87 2448 3605 2831 -84 -259 -204 C ATOM 638 CD1 ILE A 87 23.404 -1.303 26.742 1.00 21.38 C ANISOU 638 CD1 ILE A 87 2120 3351 2652 -92 -307 -289 C ATOM 639 N ALA A 88 19.966 -4.619 23.981 1.00 18.75 N ANISOU 639 N ALA A 88 1988 2841 2296 -69 -232 -216 N ATOM 640 CA ALA A 88 18.789 -5.476 23.946 1.00 17.23 C ANISOU 640 CA ALA A 88 1827 2641 2078 -77 -220 -214 C ATOM 641 C ALA A 88 18.901 -6.532 22.855 1.00 17.29 C ANISOU 641 C ALA A 88 1894 2582 2092 -56 -192 -155 C ATOM 642 O ALA A 88 18.588 -7.703 23.075 1.00 18.90 O ANISOU 642 O ALA A 88 2121 2795 2264 -55 -175 -117 O ATOM 643 CB ALA A 88 17.519 -4.642 23.757 1.00 16.98 C ANISOU 643 CB ALA A 88 1794 2595 2061 -94 -238 -287 C ATOM 644 N GLN A 89 19.345 -6.120 21.672 1.00 15.75 N ANISOU 644 N GLN A 89 1726 2322 1939 -39 -188 -148 N ATOM 645 CA GLN A 89 19.408 -7.043 20.552 1.00 16.08 C ANISOU 645 CA GLN A 89 1825 2298 1989 -18 -162 -98 C ATOM 646 C GLN A 89 20.484 -8.108 20.736 1.00 16.87 C ANISOU 646 C GLN A 89 1931 2408 2070 2 -140 -26 C ATOM 647 O GLN A 89 20.261 -9.267 20.395 1.00 22.85 O ANISOU 647 O GLN A 89 2729 3140 2811 12 -118 16 O ATOM 648 CB GLN A 89 19.584 -6.290 19.231 1.00 15.65 C ANISOU 648 CB GLN A 89 1794 2171 1981 -7 -163 -111 C ATOM 649 CG GLN A 89 18.481 -5.265 18.980 1.00 14.75 C ANISOU 649 CG GLN A 89 1676 2039 1887 -25 -186 -180 C ATOM 650 CD GLN A 89 18.198 -5.047 17.507 1.00 15.61 C ANISOU 650 CD GLN A 89 1833 2067 2032 -14 -181 -181 C ATOM 651 OE1 GLN A 89 18.383 -3.952 16.980 1.00 19.87 O ANISOU 651 OE1 GLN A 89 2363 2579 2608 -15 -197 -211 O ATOM 652 NE2 GLN A 89 17.741 -6.096 16.832 1.00 19.03 N ANISOU 652 NE2 GLN A 89 2317 2461 2454 -6 -159 -148 N ATOM 653 N GLU A 90 21.644 -7.735 21.270 1.00 16.77 N ANISOU 653 N GLU A 90 1879 2433 2060 8 -146 -11 N ATOM 654 CA GLU A 90 22.681 -8.739 21.484 1.00 19.94 C ANISOU 654 CA GLU A 90 2284 2847 2444 29 -127 58 C ATOM 655 C GLU A 90 22.224 -9.770 22.501 1.00 23.39 C ANISOU 655 C GLU A 90 2717 3334 2834 18 -122 80 C ATOM 656 O GLU A 90 22.510 -10.961 22.365 1.00 24.41 O ANISOU 656 O GLU A 90 2876 3450 2949 35 -100 138 O ATOM 657 CB GLU A 90 24.005 -8.121 21.935 1.00 23.84 C ANISOU 657 CB GLU A 90 2732 3378 2949 35 -136 68 C ATOM 658 CG GLU A 90 25.094 -9.164 22.102 1.00 29.39 C ANISOU 658 CG GLU A 90 3438 4091 3637 59 -116 140 C ATOM 659 CD GLU A 90 26.364 -8.609 22.704 1.00 34.36 C ANISOU 659 CD GLU A 90 4016 4767 4271 64 -127 151 C ATOM 660 OE1 GLU A 90 26.362 -7.446 23.166 1.00 34.28 O ANISOU 660 OE1 GLU A 90 3966 4789 4271 45 -151 100 O ATOM 661 OE2 GLU A 90 27.370 -9.346 22.713 1.00 41.14 O ANISOU 661 OE2 GLU A 90 4876 5630 5125 86 -111 209 O ATOM 662 N ASN A 91 21.503 -9.315 23.520 1.00 23.78 N ANISOU 662 N ASN A 91 2732 3443 2862 -9 -142 34 N ATOM 663 CA ASN A 91 21.094 -10.219 24.581 1.00 21.32 C ANISOU 663 CA ASN A 91 2411 3187 2502 -22 -139 54 C ATOM 664 C ASN A 91 19.852 -11.045 24.255 1.00 25.67 C ANISOU 664 C ASN A 91 3007 3710 3038 -31 -127 56 C ATOM 665 O ASN A 91 19.510 -11.977 24.982 1.00 25.96 O ANISOU 665 O ASN A 91 3046 3782 3037 -40 -121 83 O ATOM 666 CB ASN A 91 20.970 -9.467 25.906 1.00 22.19 C ANISOU 666 CB ASN A 91 2461 3381 2588 -48 -164 10 C ATOM 667 CG ASN A 91 22.328 -9.160 26.511 1.00 25.36 C ANISOU 667 CG ASN A 91 2820 3826 2989 -39 -171 32 C ATOM 668 OD1 ASN A 91 22.921 -10.010 27.170 1.00 29.44 O ANISOU 668 OD1 ASN A 91 3328 4380 3477 -32 -163 84 O ATOM 669 ND2 ASN A 91 22.842 -7.960 26.257 1.00 24.78 N ANISOU 669 ND2 ASN A 91 2721 3745 2949 -37 -186 -4 N ATOM 670 N ALA A 92 19.202 -10.718 23.141 1.00 21.96 N ANISOU 670 N ALA A 92 2573 3174 2598 -28 -124 29 N ATOM 671 CA ALA A 92 18.038 -11.468 22.674 1.00 21.08 C ANISOU 671 CA ALA A 92 2506 3026 2476 -35 -113 30 C ATOM 672 C ALA A 92 18.396 -12.482 21.594 1.00 20.49 C ANISOU 672 C ALA A 92 2488 2882 2415 -9 -86 87 C ATOM 673 O ALA A 92 17.582 -13.338 21.267 1.00 22.70 O ANISOU 673 O ALA A 92 2809 3134 2683 -13 -74 101 O ATOM 674 CB ALA A 92 16.945 -10.519 22.162 1.00 17.76 C ANISOU 674 CB ALA A 92 2090 2580 2078 -51 -127 -39 C ATOM 675 N LEU A 93 19.603 -12.383 21.041 1.00 23.95 N ANISOU 675 N LEU A 93 2930 3293 2878 17 -78 119 N ATOM 676 CA LEU A 93 20.042 -13.300 19.986 1.00 27.09 C ANISOU 676 CA LEU A 93 3379 3624 3288 45 -52 172 C ATOM 677 C LEU A 93 19.736 -14.755 20.331 1.00 30.13 C ANISOU 677 C LEU A 93 3792 4013 3641 46 -36 220 C ATOM 678 O LEU A 93 19.915 -15.174 21.473 1.00 30.11 O ANISOU 678 O LEU A 93 3761 4071 3607 37 -40 240 O ATOM 679 CB LEU A 93 21.539 -13.129 19.691 1.00 22.65 C ANISOU 679 CB LEU A 93 2805 3054 2748 72 -44 207 C ATOM 680 CG LEU A 93 21.923 -11.927 18.823 1.00 19.31 C ANISOU 680 CG LEU A 93 2375 2596 2365 79 -52 175 C ATOM 681 CD1 LEU A 93 23.413 -11.631 18.902 1.00 24.07 C ANISOU 681 CD1 LEU A 93 2949 3215 2983 98 -49 205 C ATOM 682 CD2 LEU A 93 21.480 -12.143 17.380 1.00 23.54 C ANISOU 682 CD2 LEU A 93 2969 3051 2925 90 -36 176 C ATOM 683 N PRO A 94 19.289 -15.536 19.336 1.00 29.22 N ANISOU 683 N PRO A 94 3735 3832 3535 57 -17 240 N ATOM 684 CA PRO A 94 19.117 -15.138 17.937 1.00 27.29 C ANISOU 684 CA PRO A 94 3529 3516 3326 69 -10 222 C ATOM 685 C PRO A 94 17.707 -14.639 17.638 1.00 25.94 C ANISOU 685 C PRO A 94 3369 3328 3157 44 -22 166 C ATOM 686 O PRO A 94 17.390 -14.366 16.481 1.00 23.45 O ANISOU 686 O PRO A 94 3089 2953 2869 50 -18 150 O ATOM 687 CB PRO A 94 19.342 -16.450 17.198 1.00 30.61 C ANISOU 687 CB PRO A 94 4003 3882 3746 92 17 278 C ATOM 688 CG PRO A 94 18.745 -17.468 18.126 1.00 31.82 C ANISOU 688 CG PRO A 94 4159 4069 3861 77 19 300 C ATOM 689 CD PRO A 94 18.999 -16.968 19.527 1.00 29.02 C ANISOU 689 CD PRO A 94 3743 3799 3484 59 -1 288 C ATOM 690 N LYS A 95 16.866 -14.521 18.658 1.00 27.95 N ANISOU 690 N LYS A 95 3597 3639 3386 15 -38 136 N ATOM 691 CA LYS A 95 15.493 -14.083 18.428 1.00 23.53 C ANISOU 691 CA LYS A 95 3045 3067 2827 -8 -50 82 C ATOM 692 C LYS A 95 15.375 -12.567 18.440 1.00 18.66 C ANISOU 692 C LYS A 95 2391 2464 2234 -18 -73 19 C ATOM 693 O LYS A 95 14.839 -11.981 19.375 1.00 19.64 O ANISOU 693 O LYS A 95 2474 2644 2343 -41 -92 -23 O ATOM 694 CB LYS A 95 14.553 -14.698 19.466 1.00 32.41 C ANISOU 694 CB LYS A 95 4159 4243 3911 -35 -54 77 C ATOM 695 CG LYS A 95 14.363 -16.191 19.293 1.00 39.51 C ANISOU 695 CG LYS A 95 5104 5116 4791 -30 -32 132 C ATOM 696 CD LYS A 95 12.902 -16.577 19.406 1.00 46.46 C ANISOU 696 CD LYS A 95 6002 5999 5652 -58 -35 108 C ATOM 697 CE LYS A 95 12.685 -18.006 18.944 1.00 51.73 C ANISOU 697 CE LYS A 95 6724 6622 6309 -51 -13 160 C ATOM 698 NZ LYS A 95 13.087 -18.197 17.519 1.00 55.42 N ANISOU 698 NZ LYS A 95 7242 7007 6809 -23 2 178 N ATOM 699 N THR A 96 15.871 -11.925 17.392 1.00 18.46 N ANISOU 699 N THR A 96 2381 2387 2246 -1 -73 13 N ATOM 700 CA THR A 96 15.822 -10.476 17.340 1.00 15.23 C ANISOU 700 CA THR A 96 1939 1985 1864 -10 -96 -43 C ATOM 701 C THR A 96 15.756 -9.970 15.903 1.00 16.98 C ANISOU 701 C THR A 96 2196 2131 2124 2 -95 -54 C ATOM 702 O THR A 96 16.362 -10.545 14.997 1.00 18.85 O ANISOU 702 O THR A 96 2471 2319 2371 25 -74 -11 O ATOM 703 CB THR A 96 17.008 -9.853 18.105 1.00 20.68 C ANISOU 703 CB THR A 96 2578 2723 2556 -4 -106 -38 C ATOM 704 OG1 THR A 96 16.742 -8.469 18.379 1.00 20.88 O ANISOU 704 OG1 THR A 96 2564 2770 2601 -20 -133 -101 O ATOM 705 CG2 THR A 96 18.308 -10.010 17.330 1.00 16.42 C ANISOU 705 CG2 THR A 96 2055 2145 2039 25 -89 10 C ATOM 706 N ILE A 97 14.979 -8.908 15.706 1.00 15.35 N ANISOU 706 N ILE A 97 1978 1918 1938 -13 -117 -114 N ATOM 707 CA ILE A 97 14.794 -8.294 14.400 1.00 13.51 C ANISOU 707 CA ILE A 97 1775 1617 1742 -5 -120 -130 C ATOM 708 C ILE A 97 15.255 -6.844 14.446 1.00 13.16 C ANISOU 708 C ILE A 97 1691 1580 1728 -8 -144 -169 C ATOM 709 O ILE A 97 14.785 -6.058 15.271 1.00 17.06 O ANISOU 709 O ILE A 97 2143 2117 2221 -26 -168 -219 O ATOM 710 CB ILE A 97 13.319 -8.298 13.979 1.00 13.97 C ANISOU 710 CB ILE A 97 1859 1649 1800 -21 -128 -168 C ATOM 711 CG1 ILE A 97 12.778 -9.725 13.897 1.00 14.96 C ANISOU 711 CG1 ILE A 97 2026 1764 1896 -21 -106 -132 C ATOM 712 CG2 ILE A 97 13.137 -7.561 12.645 1.00 13.06 C ANISOU 712 CG2 ILE A 97 1772 1466 1723 -14 -135 -187 C ATOM 713 CD1 ILE A 97 11.269 -9.776 13.650 1.00 14.07 C ANISOU 713 CD1 ILE A 97 1931 1635 1778 -40 -115 -170 C ATOM 714 N MET A 98 16.176 -6.494 13.560 1.00 12.48 N ANISOU 714 N MET A 98 1619 1453 1671 10 -138 -147 N ATOM 715 CA MET A 98 16.653 -5.123 13.451 1.00 14.21 C ANISOU 715 CA MET A 98 1806 1670 1924 7 -160 -179 C ATOM 716 C MET A 98 16.067 -4.438 12.216 1.00 14.20 C ANISOU 716 C MET A 98 1835 1603 1956 6 -170 -205 C ATOM 717 O MET A 98 16.058 -5.013 11.133 1.00 16.81 O ANISOU 717 O MET A 98 2215 1881 2292 19 -152 -174 O ATOM 718 CB MET A 98 18.181 -5.098 13.357 1.00 18.39 C ANISOU 718 CB MET A 98 2323 2203 2463 25 -149 -135 C ATOM 719 CG MET A 98 18.750 -3.721 13.068 1.00 20.19 C ANISOU 719 CG MET A 98 2524 2419 2729 22 -170 -162 C ATOM 720 SD MET A 98 20.549 -3.732 12.948 1.00 18.10 S ANISOU 720 SD MET A 98 2243 2161 2474 42 -154 -109 S ATOM 721 CE MET A 98 20.835 -2.074 12.336 1.00 19.39 C ANISOU 721 CE MET A 98 2386 2293 2686 34 -182 -147 C ATOM 722 N LEU A 99 15.575 -3.214 12.393 1.00 14.73 N ANISOU 722 N LEU A 99 1873 1675 2047 -9 -201 -262 N ATOM 723 CA LEU A 99 15.148 -2.379 11.271 1.00 16.99 C ANISOU 723 CA LEU A 99 2182 1902 2371 -10 -215 -287 C ATOM 724 C LEU A 99 16.238 -1.341 11.035 1.00 14.07 C ANISOU 724 C LEU A 99 1789 1524 2035 -5 -227 -286 C ATOM 725 O LEU A 99 16.515 -0.504 11.891 1.00 10.71 O ANISOU 725 O LEU A 99 1314 1138 1617 -15 -248 -318 O ATOM 726 CB LEU A 99 13.815 -1.680 11.577 1.00 17.97 C ANISOU 726 CB LEU A 99 2292 2034 2504 -29 -244 -354 C ATOM 727 CG LEU A 99 12.514 -2.493 11.596 1.00 21.67 C ANISOU 727 CG LEU A 99 2785 2500 2946 -37 -237 -365 C ATOM 728 CD1 LEU A 99 12.153 -2.983 10.194 1.00 23.02 C ANISOU 728 CD1 LEU A 99 3018 2603 3127 -28 -223 -340 C ATOM 729 CD2 LEU A 99 12.589 -3.658 12.565 1.00 26.29 C ANISOU 729 CD2 LEU A 99 3365 3139 3487 -38 -217 -336 C ATOM 730 N SER A 100 16.859 -1.396 9.867 1.00 17.84 N ANISOU 730 N SER A 100 2300 1949 2531 9 -213 -250 N ATOM 731 CA SER A 100 18.021 -0.571 9.568 1.00 13.31 C ANISOU 731 CA SER A 100 1706 1365 1985 14 -219 -237 C ATOM 732 C SER A 100 17.652 0.798 8.988 1.00 12.98 C ANISOU 732 C SER A 100 1659 1286 1985 3 -250 -280 C ATOM 733 O SER A 100 16.675 0.917 8.234 1.00 14.57 O ANISOU 733 O SER A 100 1892 1446 2197 -1 -257 -299 O ATOM 734 CB SER A 100 18.932 -1.310 8.584 1.00 13.09 C ANISOU 734 CB SER A 100 1716 1301 1955 35 -186 -174 C ATOM 735 OG SER A 100 20.109 -0.558 8.336 1.00 16.82 O ANISOU 735 OG SER A 100 2168 1770 2453 39 -190 -159 O ATOM 736 N PRO A 101 18.429 1.836 9.346 1.00 14.02 N ANISOU 736 N PRO A 101 1750 1435 2143 -3 -269 -295 N ATOM 737 CA PRO A 101 18.248 3.179 8.787 1.00 13.43 C ANISOU 737 CA PRO A 101 1669 1323 2112 -14 -299 -330 C ATOM 738 C PRO A 101 19.010 3.333 7.478 1.00 14.97 C ANISOU 738 C PRO A 101 1894 1470 2323 -3 -283 -284 C ATOM 739 O PRO A 101 19.018 4.412 6.901 1.00 16.69 O ANISOU 739 O PRO A 101 2105 1687 2550 -7 -289 -281 O ATOM 740 CB PRO A 101 18.868 4.076 9.855 1.00 13.18 C ANISOU 740 CB PRO A 101 1578 1338 2093 -24 -322 -359 C ATOM 741 CG PRO A 101 20.000 3.242 10.406 1.00 13.80 C ANISOU 741 CG PRO A 101 1642 1458 2142 -13 -295 -309 C ATOM 742 CD PRO A 101 19.466 1.817 10.401 1.00 13.43 C ANISOU 742 CD PRO A 101 1631 1418 2056 -2 -266 -281 C ATOM 743 N CYS A 102 19.656 2.263 7.026 1.00 16.21 N ANISOU 743 N CYS A 102 2081 1614 2464 13 -251 -231 N ATOM 744 CA CYS A 102 20.359 2.287 5.746 1.00 15.62 C ANISOU 744 CA CYS A 102 2039 1491 2405 23 -235 -190 C ATOM 745 C CYS A 102 20.119 0.998 4.966 1.00 13.88 C ANISOU 745 C CYS A 102 1871 1250 2153 39 -198 -148 C ATOM 746 O CYS A 102 19.451 0.082 5.453 1.00 12.39 O ANISOU 746 O CYS A 102 1694 1073 1939 42 -190 -153 O ATOM 747 CB CYS A 102 21.852 2.517 5.967 1.00 17.46 C ANISOU 747 CB CYS A 102 2241 1747 2646 29 -226 -157 C ATOM 748 SG CYS A 102 22.608 1.292 7.047 1.00 18.11 S ANISOU 748 SG CYS A 102 2303 1892 2686 44 -197 -120 S ATOM 749 N SER A 103 20.615 0.955 3.733 1.00 13.13 N ANISOU 749 N SER A 103 1804 1140 2046 45 -170 -108 N ATOM 750 CA SER A 103 20.534 -0.254 2.925 1.00 14.30 C ANISOU 750 CA SER A 103 1998 1278 2156 59 -128 -68 C ATOM 751 C SER A 103 21.414 -1.341 3.539 1.00 14.76 C ANISOU 751 C SER A 103 2059 1327 2222 83 -117 -34 C ATOM 752 O SER A 103 22.344 -1.052 4.305 1.00 13.47 O ANISOU 752 O SER A 103 1853 1197 2067 85 -122 -26 O ATOM 753 CB SER A 103 20.889 0.022 1.454 1.00 13.27 C ANISOU 753 CB SER A 103 1893 1140 2010 60 -98 -41 C ATOM 754 OG SER A 103 22.080 0.778 1.344 1.00 15.16 O ANISOU 754 OG SER A 103 2111 1371 2279 61 -109 -27 O ATOM 755 N LEU A 104 21.092 -2.591 3.228 1.00 13.41 N ANISOU 755 N LEU A 104 1925 1154 2017 95 -85 -8 N ATOM 756 CA LEU A 104 21.733 -3.734 3.864 1.00 12.51 C ANISOU 756 CA LEU A 104 1810 1056 1885 115 -65 29 C ATOM 757 C LEU A 104 23.156 -3.999 3.378 1.00 13.84 C ANISOU 757 C LEU A 104 1978 1222 2057 136 -39 79 C ATOM 758 O LEU A 104 23.820 -4.905 3.883 1.00 14.56 O ANISOU 758 O LEU A 104 2063 1341 2127 153 -16 113 O ATOM 759 CB LEU A 104 20.858 -4.983 3.713 1.00 12.45 C ANISOU 759 CB LEU A 104 1847 1035 1850 122 -47 37 C ATOM 760 CG LEU A 104 19.488 -4.890 4.395 1.00 8.83 C ANISOU 760 CG LEU A 104 1383 591 1383 102 -70 -9 C ATOM 761 CD1 LEU A 104 18.668 -6.125 4.054 1.00 9.97 C ANISOU 761 CD1 LEU A 104 1562 729 1498 104 -45 4 C ATOM 762 CD2 LEU A 104 19.637 -4.730 5.892 1.00 10.45 C ANISOU 762 CD2 LEU A 104 1534 860 1576 93 -84 -25 C ATOM 763 N ASP A 105 23.618 -3.218 2.405 1.00 12.13 N ANISOU 763 N ASP A 105 1769 980 1860 133 -39 83 N ATOM 764 CA ASP A 105 25.014 -3.282 1.995 1.00 14.49 C ANISOU 764 CA ASP A 105 2060 1281 2165 150 -19 126 C ATOM 765 C ASP A 105 25.905 -2.458 2.930 1.00 15.38 C ANISOU 765 C ASP A 105 2111 1433 2298 143 -36 122 C ATOM 766 O ASP A 105 27.128 -2.507 2.840 1.00 15.11 O ANISOU 766 O ASP A 105 2060 1414 2268 155 -19 157 O ATOM 767 CB ASP A 105 25.183 -2.863 0.525 1.00 16.40 C ANISOU 767 CB ASP A 105 2337 1516 2379 142 -16 124 C ATOM 768 CG ASP A 105 24.454 -1.575 0.180 1.00 19.02 C ANISOU 768 CG ASP A 105 2660 1842 2723 117 -28 87 C ATOM 769 OD1 ASP A 105 23.743 -1.023 1.045 1.00 17.56 O ANISOU 769 OD1 ASP A 105 2446 1662 2564 102 -57 52 O ATOM 770 OD2 ASP A 105 24.580 -1.120 -0.979 1.00 18.76 O ANISOU 770 OD2 ASP A 105 2650 1804 2673 112 -16 89 O ATOM 771 N PHE A 106 25.274 -1.699 3.825 1.00 13.26 N ANISOU 771 N PHE A 106 1811 1190 2039 121 -69 76 N ATOM 772 CA PHE A 106 25.987 -0.853 4.779 1.00 17.13 C ANISOU 772 CA PHE A 106 2242 1725 2543 110 -90 63 C ATOM 773 C PHE A 106 25.773 -1.354 6.206 1.00 17.88 C ANISOU 773 C PHE A 106 2305 1876 2611 109 -95 51 C ATOM 774 O PHE A 106 24.696 -1.853 6.545 1.00 15.87 O ANISOU 774 O PHE A 106 2068 1624 2338 105 -99 30 O ATOM 775 CB PHE A 106 25.470 0.590 4.712 1.00 17.84 C ANISOU 775 CB PHE A 106 2314 1800 2666 85 -129 15 C ATOM 776 CG PHE A 106 25.998 1.389 3.556 1.00 20.28 C ANISOU 776 CG PHE A 106 2634 2066 3005 81 -131 28 C ATOM 777 CD1 PHE A 106 27.353 1.453 3.297 1.00 21.37 C ANISOU 777 CD1 PHE A 106 2756 2213 3150 91 -114 68 C ATOM 778 CD2 PHE A 106 25.126 2.091 2.733 1.00 20.34 C ANISOU 778 CD2 PHE A 106 2668 2025 3034 68 -151 0 C ATOM 779 CE1 PHE A 106 27.832 2.193 2.245 1.00 23.99 C ANISOU 779 CE1 PHE A 106 3098 2509 3509 85 -115 81 C ATOM 780 CE2 PHE A 106 25.599 2.837 1.676 1.00 22.71 C ANISOU 780 CE2 PHE A 106 2979 2303 3348 61 -149 14 C ATOM 781 CZ PHE A 106 26.959 2.887 1.428 1.00 27.29 C ANISOU 781 CZ PHE A 106 3544 2878 3948 70 -135 55 C ATOM 782 N ILE A 107 26.796 -1.217 7.042 1.00 14.67 N ANISOU 782 N ILE A 107 1853 1517 2203 111 -96 66 N ATOM 783 CA ILE A 107 26.637 -1.426 8.479 1.00 17.00 C ANISOU 783 CA ILE A 107 2110 1872 2476 105 -108 48 C ATOM 784 C ILE A 107 26.576 -0.073 9.187 1.00 17.11 C ANISOU 784 C ILE A 107 2075 1912 2513 80 -146 0 C ATOM 785 O ILE A 107 27.429 0.779 8.968 1.00 21.55 O ANISOU 785 O ILE A 107 2614 2473 3103 76 -155 3 O ATOM 786 CB ILE A 107 27.790 -2.280 9.060 1.00 20.89 C ANISOU 786 CB ILE A 107 2583 2407 2949 125 -85 97 C ATOM 787 CG1 ILE A 107 27.665 -3.730 8.579 1.00 21.29 C ANISOU 787 CG1 ILE A 107 2680 2436 2974 149 -50 139 C ATOM 788 CG2 ILE A 107 27.779 -2.237 10.580 1.00 20.51 C ANISOU 788 CG2 ILE A 107 2486 2425 2882 114 -102 78 C ATOM 789 CD1 ILE A 107 28.625 -4.685 9.247 1.00 22.09 C ANISOU 789 CD1 ILE A 107 2763 2578 3052 169 -28 185 C ATOM 790 N TYR A 108 25.546 0.139 10.002 1.00 16.27 N ANISOU 790 N TYR A 108 1956 1829 2398 64 -168 -47 N ATOM 791 CA TYR A 108 25.458 1.349 10.819 1.00 16.43 C ANISOU 791 CA TYR A 108 1928 1879 2437 42 -205 -98 C ATOM 792 C TYR A 108 24.735 1.075 12.134 1.00 15.29 C ANISOU 792 C TYR A 108 1758 1789 2263 32 -217 -131 C ATOM 793 O TYR A 108 23.659 0.480 12.130 1.00 17.00 O ANISOU 793 O TYR A 108 2001 1997 2461 31 -212 -143 O ATOM 794 CB TYR A 108 24.746 2.492 10.080 1.00 16.98 C ANISOU 794 CB TYR A 108 2009 1900 2543 27 -231 -141 C ATOM 795 CG TYR A 108 24.746 3.774 10.893 1.00 22.19 C ANISOU 795 CG TYR A 108 2617 2587 3225 5 -269 -193 C ATOM 796 CD1 TYR A 108 23.768 4.017 11.858 1.00 22.76 C ANISOU 796 CD1 TYR A 108 2668 2691 3287 -9 -291 -247 C ATOM 797 CD2 TYR A 108 25.747 4.719 10.727 1.00 25.56 C ANISOU 797 CD2 TYR A 108 3018 3010 3684 -1 -281 -188 C ATOM 798 CE1 TYR A 108 23.787 5.181 12.621 1.00 28.08 C ANISOU 798 CE1 TYR A 108 3295 3392 3983 -27 -326 -297 C ATOM 799 CE2 TYR A 108 25.774 5.881 11.480 1.00 28.57 C ANISOU 799 CE2 TYR A 108 3352 3415 4087 -21 -316 -236 C ATOM 800 CZ TYR A 108 24.795 6.111 12.422 1.00 30.39 C ANISOU 800 CZ TYR A 108 3563 3676 4308 -33 -339 -292 C ATOM 801 OH TYR A 108 24.837 7.272 13.163 1.00 32.65 O ANISOU 801 OH TYR A 108 3803 3985 4617 -51 -374 -342 O ATOM 802 N PRO A 109 25.300 1.538 13.263 1.00 13.34 N ANISOU 802 N PRO A 109 1457 1600 2013 22 -233 -146 N ATOM 803 CA PRO A 109 26.551 2.304 13.365 1.00 15.39 C ANISOU 803 CA PRO A 109 1679 1873 2295 20 -242 -135 C ATOM 804 C PRO A 109 27.769 1.395 13.299 1.00 16.11 C ANISOU 804 C PRO A 109 1771 1981 2369 42 -211 -69 C ATOM 805 O PRO A 109 27.673 0.231 13.684 1.00 12.83 O ANISOU 805 O PRO A 109 1367 1588 1918 55 -190 -40 O ATOM 806 CB PRO A 109 26.456 2.946 14.749 1.00 16.60 C ANISOU 806 CB PRO A 109 1778 2089 2442 1 -270 -181 C ATOM 807 CG PRO A 109 25.610 1.976 15.545 1.00 15.59 C ANISOU 807 CG PRO A 109 1655 1997 2270 2 -262 -187 C ATOM 808 CD PRO A 109 24.609 1.430 14.564 1.00 16.77 C ANISOU 808 CD PRO A 109 1862 2091 2420 10 -248 -183 C ATOM 809 N THR A 110 28.896 1.933 12.838 1.00 21.86 N ANISOU 809 N THR A 110 2127 3303 2877 -275 -396 -53 N ATOM 810 CA THR A 110 30.116 1.152 12.639 1.00 20.36 C ANISOU 810 CA THR A 110 1819 3214 2704 -241 -388 -13 C ATOM 811 C THR A 110 30.531 0.335 13.857 1.00 21.30 C ANISOU 811 C THR A 110 1866 3413 2815 -184 -407 50 C ATOM 812 O THR A 110 30.883 -0.834 13.732 1.00 19.51 O ANISOU 812 O THR A 110 1556 3253 2605 -122 -391 107 O ATOM 813 CB THR A 110 31.296 2.050 12.244 1.00 21.93 C ANISOU 813 CB THR A 110 1977 3455 2902 -255 -374 -17 C ATOM 814 OG1 THR A 110 31.043 2.619 10.956 1.00 29.37 O ANISOU 814 OG1 THR A 110 2968 4342 3850 -293 -347 -58 O ATOM 815 CG2 THR A 110 32.574 1.230 12.189 1.00 25.24 C ANISOU 815 CG2 THR A 110 2263 3997 3330 -200 -357 39 C ATOM 816 N ASN A 111 30.483 0.951 15.032 1.00 22.01 N ANISOU 816 N ASN A 111 1987 3494 2882 -189 -434 47 N ATOM 817 CA ASN A 111 30.945 0.309 16.263 1.00 20.89 C ANISOU 817 CA ASN A 111 1782 3431 2723 -136 -452 108 C ATOM 818 C ASN A 111 30.112 -0.881 16.720 1.00 20.86 C ANISOU 818 C ASN A 111 1781 3422 2724 -91 -456 152 C ATOM 819 O ASN A 111 30.533 -1.633 17.595 1.00 22.14 O ANISOU 819 O ASN A 111 1884 3652 2877 -26 -460 222 O ATOM 820 CB ASN A 111 31.042 1.335 17.391 1.00 24.56 C ANISOU 820 CB ASN A 111 2271 3923 3140 -170 -474 100 C ATOM 821 CG ASN A 111 32.093 2.389 17.122 1.00 23.74 C ANISOU 821 CG ASN A 111 2128 3879 3012 -210 -468 88 C ATOM 822 OD1 ASN A 111 32.901 2.253 16.202 1.00 26.68 O ANISOU 822 OD1 ASN A 111 2454 4265 3421 -198 -451 87 O ATOM 823 ND2 ASN A 111 32.087 3.450 17.922 1.00 26.80 N ANISOU 823 ND2 ASN A 111 2532 4305 3344 -257 -481 79 N ATOM 824 N ASN A 112 28.930 -1.046 16.135 1.00 17.15 N ANISOU 824 N ASN A 112 1379 2870 2266 -122 -454 118 N ATOM 825 CA ASN A 112 28.072 -2.179 16.456 1.00 18.38 C ANISOU 825 CA ASN A 112 1537 3014 2433 -87 -460 166 C ATOM 826 C ASN A 112 28.215 -3.316 15.453 1.00 21.47 C ANISOU 826 C ASN A 112 1860 3426 2871 -42 -433 221 C ATOM 827 O ASN A 112 27.379 -4.212 15.398 1.00 18.91 O ANISOU 827 O ASN A 112 1544 3060 2582 -23 -436 268 O ATOM 828 CB ASN A 112 26.604 -1.744 16.533 1.00 17.94 C ANISOU 828 CB ASN A 112 1595 2856 2366 -144 -471 105 C ATOM 829 CG ASN A 112 26.297 -0.941 17.782 1.00 20.83 C ANISOU 829 CG ASN A 112 2011 3203 2700 -145 -483 85 C ATOM 830 OD1 ASN A 112 27.146 -0.801 18.666 1.00 23.30 O ANISOU 830 OD1 ASN A 112 2276 3580 2997 -117 -495 117 O ATOM 831 ND2 ASN A 112 25.072 -0.425 17.873 1.00 24.59 N ANISOU 831 ND2 ASN A 112 2571 3618 3153 -183 -474 53 N ATOM 832 N HIS A 113 29.277 -3.290 14.660 1.00 22.56 N ANISOU 832 N HIS A 113 1928 3619 3026 -14 -400 227 N ATOM 833 CA HIS A 113 29.377 -4.222 13.540 1.00 19.77 C ANISOU 833 CA HIS A 113 1578 3210 2723 43 -332 244 C ATOM 834 C HIS A 113 29.344 -5.692 13.961 1.00 17.67 C ANISOU 834 C HIS A 113 1348 2865 2500 169 -269 326 C ATOM 835 O HIS A 113 28.742 -6.521 13.281 1.00 16.76 O ANISOU 835 O HIS A 113 1351 2593 2424 188 -207 300 O ATOM 836 CB HIS A 113 30.607 -3.922 12.669 1.00 20.12 C ANISOU 836 CB HIS A 113 1554 3318 2773 69 -288 236 C ATOM 837 CG HIS A 113 31.912 -4.114 13.372 1.00 23.85 C ANISOU 837 CG HIS A 113 1893 3928 3239 162 -282 326 C ATOM 838 ND1 HIS A 113 32.594 -5.316 13.365 1.00 22.99 N ANISOU 838 ND1 HIS A 113 1761 3808 3167 309 -203 412 N ATOM 839 CD2 HIS A 113 32.672 -3.261 14.101 1.00 22.99 C ANISOU 839 CD2 HIS A 113 1778 3870 3087 121 -316 307 C ATOM 840 CE1 HIS A 113 33.706 -5.195 14.063 1.00 25.04 C ANISOU 840 CE1 HIS A 113 1934 4180 3401 352 -211 465 C ATOM 841 NE2 HIS A 113 33.777 -3.954 14.521 1.00 27.36 N ANISOU 841 NE2 HIS A 113 2252 4499 3645 230 -280 394 N ATOM 842 N LYS A 114 29.988 -6.027 15.073 1.00 21.52 N ANISOU 842 N LYS A 114 1737 3462 2979 256 -282 425 N ATOM 843 CA LYS A 114 30.009 -7.422 15.500 1.00 23.86 C ANISOU 843 CA LYS A 114 2063 3685 3316 386 -213 513 C ATOM 844 C LYS A 114 28.602 -7.945 15.793 1.00 21.60 C ANISOU 844 C LYS A 114 1898 3258 3052 351 -218 500 C ATOM 845 O LYS A 114 28.199 -8.987 15.270 1.00 22.19 O ANISOU 845 O LYS A 114 2079 3175 3177 396 -140 499 O ATOM 846 CB LYS A 114 30.924 -7.624 16.714 1.00 28.50 C ANISOU 846 CB LYS A 114 2514 4432 3882 487 -232 628 C ATOM 847 CG LYS A 114 31.014 -9.072 17.164 1.00 35.55 C ANISOU 847 CG LYS A 114 3436 5255 4818 636 -150 731 C ATOM 848 CD LYS A 114 31.895 -9.228 18.398 1.00 42.71 C ANISOU 848 CD LYS A 114 4275 6279 5673 693 -160 800 C ATOM 849 CE LYS A 114 31.126 -9.843 19.568 1.00 47.55 C ANISOU 849 CE LYS A 114 4934 6852 6281 722 -169 854 C ATOM 850 NZ LYS A 114 30.126 -8.907 20.162 1.00 48.96 N ANISOU 850 NZ LYS A 114 5151 7037 6416 589 -260 781 N ATOM 851 N VAL A 115 27.850 -7.230 16.624 1.00 20.03 N ANISOU 851 N VAL A 115 1684 3113 2814 270 -306 490 N ATOM 852 CA VAL A 115 26.485 -7.654 16.924 1.00 17.11 C ANISOU 852 CA VAL A 115 1418 2621 2462 232 -314 482 C ATOM 853 C VAL A 115 25.588 -7.633 15.694 1.00 18.88 C ANISOU 853 C VAL A 115 1771 2692 2711 141 -290 378 C ATOM 854 O VAL A 115 24.792 -8.545 15.497 1.00 14.60 O ANISOU 854 O VAL A 115 1331 2002 2213 150 -245 379 O ATOM 855 CB VAL A 115 25.842 -6.824 18.057 1.00 18.76 C ANISOU 855 CB VAL A 115 1585 2925 2617 167 -414 493 C ATOM 856 CG1 VAL A 115 24.366 -7.176 18.205 1.00 19.08 C ANISOU 856 CG1 VAL A 115 1736 2836 2678 115 -419 479 C ATOM 857 CG2 VAL A 115 26.579 -7.061 19.362 1.00 24.91 C ANISOU 857 CG2 VAL A 115 2286 3814 3364 258 -418 577 C ATOM 858 N ILE A 116 25.716 -6.602 14.864 1.00 16.69 N ANISOU 858 N ILE A 116 1488 2451 2403 51 -319 291 N ATOM 859 CA ILE A 116 24.864 -6.493 13.685 1.00 17.37 C ANISOU 859 CA ILE A 116 1688 2410 2500 -36 -302 191 C ATOM 860 C ILE A 116 25.134 -7.658 12.743 1.00 18.28 C ANISOU 860 C ILE A 116 1883 2392 2670 37 -201 183 C ATOM 861 O ILE A 116 24.207 -8.241 12.170 1.00 14.28 O ANISOU 861 O ILE A 116 1493 1741 2193 1 -172 137 O ATOM 862 CB ILE A 116 25.057 -5.157 12.958 1.00 18.15 C ANISOU 862 CB ILE A 116 1760 2581 2554 -132 -343 108 C ATOM 863 CG1 ILE A 116 24.471 -4.020 13.801 1.00 19.91 C ANISOU 863 CG1 ILE A 116 1942 2898 2724 -221 -439 99 C ATOM 864 CG2 ILE A 116 24.373 -5.193 11.601 1.00 12.56 C ANISOU 864 CG2 ILE A 116 1165 1749 1857 -196 -309 13 C ATOM 865 CD1 ILE A 116 24.761 -2.648 13.258 1.00 16.76 C ANISOU 865 CD1 ILE A 116 1550 2539 2279 -278 -443 11 C ATOM 866 N GLN A 117 26.409 -8.006 12.610 1.00 19.88 N ANISOU 866 N GLN A 117 2021 2647 2885 140 -148 230 N ATOM 867 CA GLN A 117 26.812 -9.182 11.851 1.00 22.31 C ANISOU 867 CA GLN A 117 2398 2835 3242 234 -43 239 C ATOM 868 C GLN A 117 26.142 -10.446 12.388 1.00 19.62 C ANISOU 868 C GLN A 117 2138 2365 2952 289 1 292 C ATOM 869 O GLN A 117 25.645 -11.266 11.616 1.00 18.60 O ANISOU 869 O GLN A 117 2131 2074 2863 289 64 247 O ATOM 870 CB GLN A 117 28.337 -9.328 11.873 1.00 29.23 C ANISOU 870 CB GLN A 117 3171 3816 4119 351 5 306 C ATOM 871 CG GLN A 117 28.830 -10.752 11.681 1.00 41.05 C ANISOU 871 CG GLN A 117 4718 5210 5668 492 116 367 C ATOM 872 CD GLN A 117 28.682 -11.233 10.255 1.00 53.02 C ANISOU 872 CD GLN A 117 6360 6576 7209 488 193 282 C ATOM 873 OE1 GLN A 117 29.133 -10.575 9.317 1.00 56.81 O ANISOU 873 OE1 GLN A 117 6825 7095 7664 455 196 221 O ATOM 874 NE2 GLN A 117 28.044 -12.388 10.081 1.00 58.89 N ANISOU 874 NE2 GLN A 117 7229 7146 8000 519 257 278 N ATOM 875 N GLU A 118 26.117 -10.596 13.711 1.00 23.51 N ANISOU 875 N GLU A 118 2563 2927 3441 333 -31 385 N ATOM 876 CA GLU A 118 25.459 -11.742 14.338 1.00 21.81 C ANISOU 876 CA GLU A 118 2415 2596 3275 385 10 448 C ATOM 877 C GLU A 118 23.950 -11.738 14.093 1.00 19.99 C ANISOU 877 C GLU A 118 2295 2241 3058 264 -21 377 C ATOM 878 O GLU A 118 23.333 -12.792 13.926 1.00 17.67 O ANISOU 878 O GLU A 118 2104 1790 2819 279 38 381 O ATOM 879 CB GLU A 118 25.759 -11.788 15.843 1.00 24.07 C ANISOU 879 CB GLU A 118 2596 3005 3545 459 -24 567 C ATOM 880 CG GLU A 118 27.246 -11.954 16.166 1.00 29.76 C ANISOU 880 CG GLU A 118 3201 3853 4254 591 11 652 C ATOM 881 CD GLU A 118 27.552 -11.813 17.649 1.00 38.83 C ANISOU 881 CD GLU A 118 4231 5153 5369 653 -39 760 C ATOM 882 OE1 GLU A 118 26.665 -11.371 18.410 1.00 36.98 O ANISOU 882 OE1 GLU A 118 3998 4943 5110 582 -113 758 O ATOM 883 OE2 GLU A 118 28.684 -12.149 18.055 1.00 46.59 O ANISOU 883 OE2 GLU A 118 5120 6237 6346 776 -5 848 O ATOM 884 N ILE A 119 23.353 -10.555 14.078 1.00 14.54 N ANISOU 884 N ILE A 119 1583 1623 2317 144 -111 315 N ATOM 885 CA ILE A 119 21.934 -10.449 13.759 1.00 15.10 C ANISOU 885 CA ILE A 119 1750 1595 2393 26 -143 247 C ATOM 886 C ILE A 119 21.677 -10.918 12.328 1.00 13.99 C ANISOU 886 C ILE A 119 1724 1310 2281 -10 -85 152 C ATOM 887 O ILE A 119 20.786 -11.727 12.087 1.00 18.38 O ANISOU 887 O ILE A 119 2383 1722 2880 -41 -55 131 O ATOM 888 CB ILE A 119 21.414 -9.015 13.955 1.00 12.52 C ANISOU 888 CB ILE A 119 1377 1380 2000 -87 -245 201 C ATOM 889 CG1 ILE A 119 21.527 -8.616 15.427 1.00 19.31 C ANISOU 889 CG1 ILE A 119 2138 2370 2828 -55 -304 289 C ATOM 890 CG2 ILE A 119 19.972 -8.890 13.458 1.00 13.43 C ANISOU 890 CG2 ILE A 119 1589 1397 2116 -205 -272 128 C ATOM 891 CD1 ILE A 119 21.382 -7.132 15.681 1.00 18.87 C ANISOU 891 CD1 ILE A 119 2021 2446 2701 -144 -396 249 C ATOM 892 N ALA A 120 22.466 -10.417 11.382 1.00 14.07 N ANISOU 892 N ALA A 120 1717 1362 2266 -8 -70 94 N ATOM 893 CA ALA A 120 22.366 -10.862 9.999 1.00 16.31 C ANISOU 893 CA ALA A 120 2107 1522 2567 -27 -10 5 C ATOM 894 C ALA A 120 22.489 -12.373 9.901 1.00 18.88 C ANISOU 894 C ALA A 120 2516 1697 2960 64 87 39 C ATOM 895 O ALA A 120 21.836 -13.000 9.075 1.00 20.32 O ANISOU 895 O ALA A 120 2818 1733 3169 22 125 -32 O ATOM 896 CB ALA A 120 23.421 -10.182 9.122 1.00 14.23 C ANISOU 896 CB ALA A 120 1796 1340 2269 -7 6 -38 C ATOM 897 N GLN A 121 23.312 -12.959 10.765 1.00 16.91 N ANISOU 897 N GLN A 121 2205 1484 2736 189 128 148 N ATOM 898 CA GLN A 121 23.592 -14.385 10.697 1.00 17.67 C ANISOU 898 CA GLN A 121 2377 1441 2897 296 235 193 C ATOM 899 C GLN A 121 22.535 -15.271 11.362 1.00 25.19 C ANISOU 899 C GLN A 121 3401 2266 3902 277 247 230 C ATOM 900 O GLN A 121 22.180 -16.320 10.826 1.00 25.45 O ANISOU 900 O GLN A 121 3555 2126 3988 287 321 201 O ATOM 901 CB GLN A 121 24.972 -14.682 11.286 1.00 35.07 C ANISOU 901 CB GLN A 121 4482 3740 5104 452 285 303 C ATOM 902 CG GLN A 121 25.368 -16.138 11.217 1.00 44.54 C ANISOU 902 CG GLN A 121 5757 4800 6367 581 407 360 C ATOM 903 CD GLN A 121 26.852 -16.317 10.960 1.00 53.81 C ANISOU 903 CD GLN A 121 6867 6046 7532 721 477 413 C ATOM 904 OE1 GLN A 121 27.565 -15.350 10.686 1.00 55.97 O ANISOU 904 OE1 GLN A 121 7044 6465 7755 709 435 395 O ATOM 905 NE2 GLN A 121 27.324 -17.557 11.042 1.00 58.53 N ANISOU 905 NE2 GLN A 121 7516 6541 8181 857 589 483 N ATOM 906 N ASN A 122 22.029 -14.851 12.514 1.00 20.83 N ANISOU 906 N ASN A 122 2781 1799 3336 248 176 293 N ATOM 907 CA ASN A 122 21.132 -15.701 13.289 1.00 21.74 C ANISOU 907 CA ASN A 122 2947 1809 3504 247 192 352 C ATOM 908 C ASN A 122 19.762 -15.091 13.582 1.00 20.65 C ANISOU 908 C ASN A 122 2821 1677 3347 107 103 315 C ATOM 909 O ASN A 122 18.826 -15.807 13.924 1.00 20.11 O ANISOU 909 O ASN A 122 2818 1495 3328 77 119 338 O ATOM 910 CB ASN A 122 21.806 -16.120 14.595 1.00 29.70 C ANISOU 910 CB ASN A 122 3866 2895 4524 382 217 497 C ATOM 911 CG ASN A 122 23.227 -16.585 14.385 1.00 35.46 C ANISOU 911 CG ASN A 122 4560 3654 5261 528 298 547 C ATOM 912 OD1 ASN A 122 23.465 -17.652 13.821 1.00 36.60 O ANISOU 912 OD1 ASN A 122 4795 3651 5458 596 401 546 O ATOM 913 ND2 ASN A 122 24.184 -15.781 14.833 1.00 38.12 N ANISOU 913 ND2 ASN A 122 4761 4181 5542 577 254 590 N ATOM 914 N GLY A 123 19.652 -13.773 13.458 1.00 13.67 N ANISOU 914 N GLY A 123 1560 1100 2534 106 201 17 N ATOM 915 CA GLY A 123 18.368 -13.104 13.589 1.00 14.89 C ANISOU 915 CA GLY A 123 1707 1270 2679 96 158 7 C ATOM 916 C GLY A 123 17.909 -12.638 12.219 1.00 12.73 C ANISOU 916 C GLY A 123 1474 984 2380 104 148 2 C ATOM 917 O GLY A 123 18.066 -13.352 11.230 1.00 17.45 O ANISOU 917 O GLY A 123 2117 1555 2957 121 171 0 O ATOM 918 N LEU A 124 17.387 -11.423 12.154 1.00 15.32 N ANISOU 918 N LEU A 124 1785 1329 2708 92 112 1 N ATOM 919 CA LEU A 124 16.860 -10.876 10.911 1.00 14.34 C ANISOU 919 CA LEU A 124 1699 1193 2557 98 98 -3 C ATOM 920 C LEU A 124 17.069 -9.366 10.875 1.00 12.62 C ANISOU 920 C LEU A 124 1451 992 2350 85 73 5 C ATOM 921 O LEU A 124 16.835 -8.676 11.864 1.00 15.82 O ANISOU 921 O LEU A 124 1808 1427 2777 69 44 6 O ATOM 922 CB LEU A 124 15.360 -11.169 10.808 1.00 13.58 C ANISOU 922 CB LEU A 124 1622 1097 2439 98 71 -18 C ATOM 923 CG LEU A 124 14.587 -10.562 9.633 1.00 14.08 C ANISOU 923 CG LEU A 124 1726 1151 2475 102 49 -24 C ATOM 924 CD1 LEU A 124 14.942 -11.258 8.320 1.00 12.92 C ANISOU 924 CD1 LEU A 124 1640 967 2300 123 77 -26 C ATOM 925 CD2 LEU A 124 13.086 -10.642 9.884 1.00 16.23 C ANISOU 925 CD2 LEU A 124 1996 1432 2736 97 17 -37 C ATOM 926 N ILE A 125 17.532 -8.855 9.742 1.00 9.47 N ANISOU 926 N ILE A 125 1082 577 1938 93 82 11 N ATOM 927 CA ILE A 125 17.603 -7.417 9.541 1.00 11.58 C ANISOU 927 CA ILE A 125 1328 858 2212 83 57 18 C ATOM 928 C ILE A 125 16.725 -7.074 8.348 1.00 11.60 C ANISOU 928 C ILE A 125 1382 846 2180 89 40 10 C ATOM 929 O ILE A 125 16.789 -7.748 7.318 1.00 12.01 O ANISOU 929 O ILE A 125 1489 868 2205 106 62 7 O ATOM 930 CB ILE A 125 19.030 -6.932 9.211 1.00 10.33 C ANISOU 930 CB ILE A 125 1159 692 2073 85 84 35 C ATOM 931 CG1 ILE A 125 20.060 -7.522 10.177 1.00 13.88 C ANISOU 931 CG1 ILE A 125 1571 1148 2555 83 112 43 C ATOM 932 CG2 ILE A 125 19.084 -5.416 9.234 1.00 14.38 C ANISOU 932 CG2 ILE A 125 1641 1223 2599 71 53 42 C ATOM 933 CD1 ILE A 125 21.476 -6.961 9.985 1.00 12.88 C ANISOU 933 CD1 ILE A 125 1423 1017 2454 83 137 62 C ATOM 934 N LEU A 126 15.914 -6.029 8.492 1.00 11.24 N ANISOU 934 N LEU A 126 1317 820 2132 77 -2 7 N ATOM 935 CA LEU A 126 15.082 -5.535 7.411 1.00 15.36 C ANISOU 935 CA LEU A 126 1883 1331 2622 80 -21 1 C ATOM 936 C LEU A 126 15.453 -4.102 7.089 1.00 12.85 C ANISOU 936 C LEU A 126 1549 1021 2311 72 -39 12 C ATOM 937 O LEU A 126 15.872 -3.349 7.976 1.00 13.25 O ANISOU 937 O LEU A 126 1543 1099 2394 58 -57 19 O ATOM 938 CB LEU A 126 13.611 -5.584 7.817 1.00 13.29 C ANISOU 938 CB LEU A 126 1612 1085 2351 73 -59 -12 C ATOM 939 CG LEU A 126 13.041 -6.949 8.172 1.00 13.31 C ANISOU 939 CG LEU A 126 1629 1081 2349 80 -46 -23 C ATOM 940 CD1 LEU A 126 11.561 -6.815 8.516 1.00 14.97 C ANISOU 940 CD1 LEU A 126 1825 1309 2554 73 -87 -34 C ATOM 941 CD2 LEU A 126 13.274 -7.934 7.016 1.00 12.52 C ANISOU 941 CD2 LEU A 126 1598 941 2220 101 -11 -26 C ATOM 942 N SER A 127 15.273 -3.723 5.826 1.00 14.01 N ANISOU 942 N SER A 127 1749 1147 2429 79 -37 12 N ATOM 943 CA SER A 127 15.457 -2.333 5.399 1.00 10.89 C ANISOU 943 CA SER A 127 1345 757 2035 71 -57 21 C ATOM 944 C SER A 127 14.459 -1.928 4.315 1.00 13.74 C ANISOU 944 C SER A 127 1758 1103 2358 74 -75 14 C ATOM 945 O SER A 127 14.083 -2.728 3.455 1.00 13.36 O ANISOU 945 O SER A 127 1771 1028 2279 88 -56 6 O ATOM 946 CB SER A 127 16.878 -2.095 4.889 1.00 11.37 C ANISOU 946 CB SER A 127 1413 799 2107 77 -22 37 C ATOM 947 OG SER A 127 17.036 -0.776 4.438 1.00 14.05 O ANISOU 947 OG SER A 127 1748 1142 2448 70 -40 46 O ATOM 948 N GLU A 128 14.045 -0.668 4.349 1.00 11.47 N ANISOU 948 N GLU A 128 1446 836 2075 61 -113 17 N ATOM 949 CA GLU A 128 13.201 -0.107 3.292 1.00 12.46 C ANISOU 949 CA GLU A 128 1617 950 2168 62 -131 13 C ATOM 950 C GLU A 128 14.036 0.313 2.082 1.00 18.19 C ANISOU 950 C GLU A 128 2394 1643 2876 70 -100 24 C ATOM 951 O GLU A 128 13.498 0.575 1.011 1.00 18.62 O ANISOU 951 O GLU A 128 2500 1677 2899 74 -99 21 O ATOM 952 CB GLU A 128 12.447 1.111 3.823 1.00 18.36 C ANISOU 952 CB GLU A 128 2315 1733 2927 45 -190 13 C ATOM 953 CG GLU A 128 10.966 1.107 3.533 1.00 22.70 C ANISOU 953 CG GLU A 128 2881 2290 3453 43 -226 1 C ATOM 954 CD GLU A 128 10.235 2.217 4.269 1.00 23.04 C ANISOU 954 CD GLU A 128 2869 2375 3509 29 -292 1 C ATOM 955 OE1 GLU A 128 9.300 2.800 3.687 1.00 26.22 O ANISOU 955 OE1 GLU A 128 3290 2783 3891 27 -327 -3 O ATOM 956 OE2 GLU A 128 10.593 2.504 5.431 1.00 19.04 O ANISOU 956 OE2 GLU A 128 2303 1897 3033 21 -310 5 O ATOM 957 N TYR A 129 15.352 0.358 2.254 1.00 12.82 N ANISOU 957 N TYR A 129 1697 957 2218 72 -73 37 N ATOM 958 CA TYR A 129 16.243 0.916 1.232 1.00 15.70 C ANISOU 958 CA TYR A 129 2098 1295 2572 79 -49 50 C ATOM 959 C TYR A 129 17.074 -0.126 0.495 1.00 15.50 C ANISOU 959 C TYR A 129 2123 1234 2533 99 -5 52 C ATOM 960 O TYR A 129 17.755 -0.948 1.112 1.00 17.39 O ANISOU 960 O TYR A 129 2334 1477 2796 104 17 54 O ATOM 961 CB TYR A 129 17.140 1.974 1.870 1.00 10.91 C ANISOU 961 CB TYR A 129 1429 711 2007 66 -58 67 C ATOM 962 CG TYR A 129 16.340 2.861 2.795 1.00 13.61 C ANISOU 962 CG TYR A 129 1713 1093 2367 47 -112 63 C ATOM 963 CD1 TYR A 129 15.458 3.808 2.288 1.00 15.03 C ANISOU 963 CD1 TYR A 129 1907 1278 2527 40 -148 60 C ATOM 964 CD2 TYR A 129 16.432 2.719 4.171 1.00 13.19 C ANISOU 964 CD2 TYR A 129 1590 1072 2349 38 -131 61 C ATOM 965 CE1 TYR A 129 14.704 4.606 3.128 1.00 16.21 C ANISOU 965 CE1 TYR A 129 2001 1466 2690 25 -206 56 C ATOM 966 CE2 TYR A 129 15.687 3.512 5.018 1.00 15.33 C ANISOU 966 CE2 TYR A 129 1811 1380 2634 24 -186 57 C ATOM 967 CZ TYR A 129 14.824 4.448 4.494 1.00 19.54 C ANISOU 967 CZ TYR A 129 2358 1921 3147 18 -225 55 C ATOM 968 OH TYR A 129 14.083 5.239 5.337 1.00 17.87 O ANISOU 968 OH TYR A 129 2095 1747 2947 5 -286 52 O ATOM 969 N GLU A 130 17.026 -0.076 -0.833 1.00 15.98 N ANISOU 969 N GLU A 130 2255 1260 2556 111 4 52 N ATOM 970 CA GLU A 130 17.622 -1.134 -1.653 1.00 15.73 C ANISOU 970 CA GLU A 130 2271 1195 2511 133 28 50 C ATOM 971 C GLU A 130 19.138 -1.257 -1.575 1.00 15.22 C ANISOU 971 C GLU A 130 2170 1127 2484 139 64 67 C ATOM 972 O GLU A 130 19.660 -2.339 -1.311 1.00 15.36 O ANISOU 972 O GLU A 130 2175 1143 2517 149 91 66 O ATOM 973 CB GLU A 130 17.208 -0.998 -3.121 1.00 18.63 C ANISOU 973 CB GLU A 130 2718 1526 2835 145 15 44 C ATOM 974 CG GLU A 130 17.874 -2.036 -4.020 1.00 19.89 C ANISOU 974 CG GLU A 130 2901 1655 3001 166 28 41 C ATOM 975 CD GLU A 130 17.452 -1.923 -5.475 1.00 28.35 C ANISOU 975 CD GLU A 130 4027 2692 4052 175 -2 33 C ATOM 976 OE1 GLU A 130 17.749 -2.856 -6.249 1.00 30.77 O ANISOU 976 OE1 GLU A 130 4336 2978 4377 192 15 27 O ATOM 977 OE2 GLU A 130 16.829 -0.907 -5.845 1.00 29.45 O ANISOU 977 OE2 GLU A 130 4187 2843 4161 162 -28 34 O ATOM 978 N LYS A 131 19.841 -0.156 -1.823 1.00 14.93 N ANISOU 978 N LYS A 131 2118 1091 2463 131 69 85 N ATOM 979 CA LYS A 131 21.292 -0.203 -2.004 1.00 17.05 C ANISOU 979 CA LYS A 131 2360 1353 2764 139 111 105 C ATOM 980 C LYS A 131 21.878 1.200 -1.951 1.00 15.28 C ANISOU 980 C LYS A 131 2104 1138 2562 125 107 125 C ATOM 981 O LYS A 131 21.182 2.170 -2.218 1.00 14.14 O ANISOU 981 O LYS A 131 1979 995 2398 114 74 123 O ATOM 982 CB LYS A 131 21.623 -0.823 -3.361 1.00 21.96 C ANISOU 982 CB LYS A 131 3037 1940 3368 160 134 106 C ATOM 983 CG LYS A 131 21.069 -0.017 -4.518 1.00 28.81 C ANISOU 983 CG LYS A 131 3958 2785 4203 159 105 104 C ATOM 984 CD LYS A 131 21.318 -0.684 -5.861 1.00 35.57 C ANISOU 984 CD LYS A 131 4858 3609 5049 179 126 103 C ATOM 985 CE LYS A 131 20.753 0.171 -6.994 1.00 37.63 C ANISOU 985 CE LYS A 131 5164 3847 5287 176 92 102 C ATOM 986 NZ LYS A 131 21.000 -0.426 -8.339 1.00 40.91 N ANISOU 986 NZ LYS A 131 5611 4234 5700 195 121 102 N ATOM 987 N ASP A 132 23.157 1.294 -1.595 1.00 19.01 N ANISOU 987 N ASP A 132 2527 1617 3078 126 142 146 N ATOM 988 CA ASP A 132 23.887 2.565 -1.573 1.00 17.67 C ANISOU 988 CA ASP A 132 2322 1455 2937 115 143 168 C ATOM 989 C ASP A 132 23.138 3.679 -0.854 1.00 18.98 C ANISOU 989 C ASP A 132 2457 1647 3107 93 93 164 C ATOM 990 O ASP A 132 23.311 4.856 -1.164 1.00 19.09 O ANISOU 990 O ASP A 132 2465 1661 3127 84 80 178 O ATOM 991 CB ASP A 132 24.243 2.993 -2.998 1.00 20.15 C ANISOU 991 CB ASP A 132 2688 1737 3231 125 159 181 C ATOM 992 CG ASP A 132 24.999 1.920 -3.749 1.00 23.51 C ANISOU 992 CG ASP A 132 3137 2140 3656 148 210 187 C ATOM 993 OD1 ASP A 132 25.963 1.366 -3.182 1.00 26.28 O ANISOU 993 OD1 ASP A 132 3443 2501 4042 155 250 199 O ATOM 994 OD2 ASP A 132 24.619 1.617 -4.898 1.00 27.47 O ANISOU 994 OD2 ASP A 132 3700 2615 4124 161 211 180 O ATOM 995 N PHE A 133 22.304 3.305 0.111 1.00 12.73 N ANISOU 995 N PHE A 133 1641 880 2315 86 66 146 N ATOM 996 CA PHE A 133 21.528 4.280 0.872 1.00 13.15 C ANISOU 996 CA PHE A 133 1656 964 2377 66 17 141 C ATOM 997 C PHE A 133 22.139 4.465 2.252 1.00 16.42 C ANISOU 997 C PHE A 133 1983 1411 2844 55 9 148 C ATOM 998 O PHE A 133 22.047 3.586 3.109 1.00 16.18 O ANISOU 998 O PHE A 133 1927 1394 2826 56 13 138 O ATOM 999 CB PHE A 133 20.072 3.833 1.013 1.00 12.84 C ANISOU 999 CB PHE A 133 1644 932 2303 64 -13 117 C ATOM 1000 CG PHE A 133 19.130 4.941 1.421 1.00 16.29 C ANISOU 1000 CG PHE A 133 2053 1396 2740 47 -66 112 C ATOM 1001 CD1 PHE A 133 19.082 5.383 2.730 1.00 18.65 C ANISOU 1001 CD1 PHE A 133 2275 1735 3078 32 -101 112 C ATOM 1002 CD2 PHE A 133 18.292 5.534 0.488 1.00 21.05 C ANISOU 1002 CD2 PHE A 133 2707 1986 3305 45 -83 108 C ATOM 1003 CE1 PHE A 133 18.218 6.395 3.108 1.00 19.48 C ANISOU 1003 CE1 PHE A 133 2352 1868 3183 18 -156 108 C ATOM 1004 CE2 PHE A 133 17.429 6.548 0.858 1.00 17.23 C ANISOU 1004 CE2 PHE A 133 2192 1530 2823 29 -135 104 C ATOM 1005 CZ PHE A 133 17.391 6.979 2.171 1.00 16.70 C ANISOU 1005 CZ PHE A 133 2046 1504 2794 16 -175 104 C ATOM 1006 N MET A 134 22.764 5.611 2.460 1.00 15.30 N ANISOU 1006 N MET A 134 1798 1281 2736 45 -4 166 N ATOM 1007 CA MET A 134 23.412 5.900 3.729 1.00 16.83 C ANISOU 1007 CA MET A 134 1908 1504 2982 34 -16 175 C ATOM 1008 C MET A 134 22.401 6.474 4.699 1.00 19.39 C ANISOU 1008 C MET A 134 2192 1864 3310 18 -77 161 C ATOM 1009 O MET A 134 21.413 7.067 4.273 1.00 17.62 O ANISOU 1009 O MET A 134 1996 1643 3057 13 -111 153 O ATOM 1010 CB MET A 134 24.550 6.890 3.507 1.00 20.40 C ANISOU 1010 CB MET A 134 2328 1953 3470 31 -5 201 C ATOM 1011 CG MET A 134 25.678 6.312 2.675 1.00 25.51 C ANISOU 1011 CG MET A 134 3001 2569 4122 47 57 218 C ATOM 1012 SD MET A 134 27.240 7.035 3.139 1.00 51.21 S ANISOU 1012 SD MET A 134 6181 5833 7443 43 75 250 S ATOM 1013 CE MET A 134 26.887 8.730 2.719 1.00 12.22 C ANISOU 1013 CE MET A 134 1241 900 2503 30 30 261 C ATOM 1014 N PRO A 135 22.635 6.292 6.010 1.00 18.00 N ANISOU 1014 N PRO A 135 1952 1716 3171 10 -92 159 N ATOM 1015 CA PRO A 135 21.718 6.850 7.006 1.00 19.04 C ANISOU 1015 CA PRO A 135 2041 1884 3309 -4 -154 148 C ATOM 1016 C PRO A 135 21.577 8.347 6.798 1.00 18.39 C ANISOU 1016 C PRO A 135 1940 1813 3232 -14 -197 158 C ATOM 1017 O PRO A 135 22.550 9.014 6.449 1.00 19.88 O ANISOU 1017 O PRO A 135 2115 1992 3445 -15 -182 178 O ATOM 1018 CB PRO A 135 22.425 6.572 8.338 1.00 16.41 C ANISOU 1018 CB PRO A 135 1641 1573 3022 -11 -155 151 C ATOM 1019 CG PRO A 135 23.381 5.466 8.055 1.00 20.01 C ANISOU 1019 CG PRO A 135 2114 2003 3484 2 -91 158 C ATOM 1020 CD PRO A 135 23.803 5.642 6.627 1.00 15.81 C ANISOU 1020 CD PRO A 135 1636 1438 2932 14 -55 170 C ATOM 1021 N ILE A 136 20.369 8.854 6.991 1.00 21.54 N ANISOU 1021 N ILE A 136 2340 2233 3610 -22 -251 145 N ATOM 1022 CA ILE A 136 20.102 10.278 6.898 1.00 24.14 C ANISOU 1022 CA ILE A 136 2650 2578 3943 -32 -300 153 C ATOM 1023 C ILE A 136 18.953 10.535 7.869 1.00 26.36 C ANISOU 1023 C ILE A 136 2954 2897 4164 -35 -334 132 C ATOM 1024 O ILE A 136 18.209 9.613 8.198 1.00 23.64 O ANISOU 1024 O ILE A 136 2619 2557 3804 -32 -334 116 O ATOM 1025 CB ILE A 136 19.771 10.702 5.439 1.00 16.63 C ANISOU 1025 CB ILE A 136 1767 1598 2952 -28 -288 156 C ATOM 1026 CG1 ILE A 136 20.053 12.195 5.221 1.00 18.52 C ANISOU 1026 CG1 ILE A 136 1985 1845 3206 -38 -321 173 C ATOM 1027 CG2 ILE A 136 18.349 10.307 5.054 1.00 20.53 C ANISOU 1027 CG2 ILE A 136 2308 2092 3399 -26 -308 135 C ATOM 1028 CD1 ILE A 136 19.864 12.650 3.769 1.00 20.92 C ANISOU 1028 CD1 ILE A 136 2357 2117 3473 -36 -304 179 C ATOM 1029 N LYS A 137 18.828 11.765 8.356 1.00 27.15 N ANISOU 1029 N LYS A 137 3681 2595 4039 362 -173 -361 N ATOM 1030 CA LYS A 137 17.847 12.068 9.396 1.00 30.91 C ANISOU 1030 CA LYS A 137 4113 3114 4518 389 -220 -421 C ATOM 1031 C LYS A 137 16.481 11.433 9.129 1.00 27.41 C ANISOU 1031 C LYS A 137 3664 2701 4049 398 -228 -432 C ATOM 1032 O LYS A 137 15.935 10.745 9.987 1.00 26.28 O ANISOU 1032 O LYS A 137 3489 2599 3896 394 -231 -449 O ATOM 1033 CB LYS A 137 17.722 13.580 9.611 1.00 39.34 C ANISOU 1033 CB LYS A 137 5169 4173 5606 430 -272 -478 C ATOM 1034 CG LYS A 137 18.260 14.431 8.470 1.00 46.45 C ANISOU 1034 CG LYS A 137 6112 5019 6517 436 -266 -459 C ATOM 1035 CD LYS A 137 18.137 15.912 8.800 1.00 54.07 C ANISOU 1035 CD LYS A 137 7067 5977 7502 477 -324 -517 C ATOM 1036 CE LYS A 137 18.843 16.247 10.111 1.00 57.56 C ANISOU 1036 CE LYS A 137 7473 6433 7965 477 -341 -544 C ATOM 1037 NZ LYS A 137 18.698 17.677 10.494 1.00 59.28 N ANISOU 1037 NZ LYS A 137 7680 6646 8199 520 -402 -605 N ATOM 1038 N GLY A 138 15.954 11.644 7.927 1.00 29.99 N ANISOU 1038 N GLY A 138 4021 3006 4367 410 -229 -422 N ATOM 1039 CA GLY A 138 14.652 11.119 7.551 1.00 30.92 C ANISOU 1039 CA GLY A 138 4135 3149 4465 421 -240 -434 C ATOM 1040 C GLY A 138 14.531 9.605 7.569 1.00 31.18 C ANISOU 1040 C GLY A 138 4173 3198 4478 384 -199 -390 C ATOM 1041 O GLY A 138 13.442 9.069 7.772 1.00 28.03 O ANISOU 1041 O GLY A 138 3755 2832 4064 391 -211 -411 O ATOM 1042 N SER A 139 15.638 8.902 7.355 1.00 27.77 N ANISOU 1042 N SER A 139 3767 2743 4042 346 -151 -332 N ATOM 1043 CA SER A 139 15.590 7.441 7.350 1.00 18.65 C ANISOU 1043 CA SER A 139 2621 1600 2864 312 -117 -290 C ATOM 1044 C SER A 139 15.581 6.876 8.769 1.00 18.04 C ANISOU 1044 C SER A 139 2508 1558 2786 300 -122 -306 C ATOM 1045 O SER A 139 15.005 5.822 9.014 1.00 14.47 O ANISOU 1045 O SER A 139 2054 1127 2316 283 -112 -295 O ATOM 1046 CB SER A 139 16.721 6.832 6.508 1.00 20.91 C ANISOU 1046 CB SER A 139 2950 1856 3137 281 -69 -228 C ATOM 1047 OG SER A 139 17.986 6.950 7.135 1.00 16.97 O ANISOU 1047 OG SER A 139 2447 1351 2649 268 -60 -218 O ATOM 1048 N PHE A 140 16.218 7.578 9.701 1.00 18.26 N ANISOU 1048 N PHE A 140 2511 1592 2836 309 -139 -334 N ATOM 1049 CA PHE A 140 16.153 7.201 11.110 1.00 20.65 C ANISOU 1049 CA PHE A 140 2777 1931 3140 303 -148 -360 C ATOM 1050 C PHE A 140 14.719 7.268 11.614 1.00 20.86 C ANISOU 1050 C PHE A 140 2768 2001 3156 332 -177 -419 C ATOM 1051 O PHE A 140 14.229 6.341 12.253 1.00 19.55 O ANISOU 1051 O PHE A 140 2588 1865 2974 317 -166 -423 O ATOM 1052 CB PHE A 140 17.037 8.113 11.964 1.00 23.58 C ANISOU 1052 CB PHE A 140 3123 2298 3536 314 -167 -387 C ATOM 1053 CG PHE A 140 18.507 7.912 11.741 1.00 22.27 C ANISOU 1053 CG PHE A 140 2981 2099 3380 285 -139 -337 C ATOM 1054 CD1 PHE A 140 19.178 6.867 12.356 1.00 22.28 C ANISOU 1054 CD1 PHE A 140 2981 2110 3374 252 -118 -304 C ATOM 1055 CD2 PHE A 140 19.220 8.765 10.918 1.00 26.38 C ANISOU 1055 CD2 PHE A 140 3524 2583 3917 292 -136 -325 C ATOM 1056 CE1 PHE A 140 20.525 6.675 12.157 1.00 18.66 C ANISOU 1056 CE1 PHE A 140 2538 1629 2924 229 -98 -265 C ATOM 1057 CE2 PHE A 140 20.576 8.575 10.715 1.00 27.77 C ANISOU 1057 CE2 PHE A 140 3717 2736 4100 268 -111 -285 C ATOM 1058 CZ PHE A 140 21.228 7.526 11.340 1.00 22.10 C ANISOU 1058 CZ PHE A 140 2991 2032 3375 238 -94 -257 C ATOM 1059 N LEU A 141 14.051 8.376 11.326 1.00 23.14 N ANISOU 1059 N LEU A 141 3042 2299 3453 373 -215 -469 N ATOM 1060 CA LEU A 141 12.653 8.529 11.706 1.00 27.50 C ANISOU 1060 CA LEU A 141 3554 2903 3991 408 -246 -535 C ATOM 1061 C LEU A 141 11.784 7.509 10.985 1.00 23.32 C ANISOU 1061 C LEU A 141 3043 2378 3441 394 -227 -509 C ATOM 1062 O LEU A 141 10.884 6.915 11.582 1.00 22.91 O ANISOU 1062 O LEU A 141 2959 2375 3371 398 -227 -543 O ATOM 1063 CB LEU A 141 12.165 9.939 11.390 1.00 34.47 C ANISOU 1063 CB LEU A 141 4423 3792 4883 459 -297 -592 C ATOM 1064 CG LEU A 141 12.901 11.056 12.127 1.00 40.60 C ANISOU 1064 CG LEU A 141 5181 4567 5679 479 -325 -627 C ATOM 1065 CD1 LEU A 141 12.279 12.412 11.803 1.00 41.09 C ANISOU 1065 CD1 LEU A 141 5232 4637 5744 532 -383 -687 C ATOM 1066 CD2 LEU A 141 12.889 10.791 13.625 1.00 40.53 C ANISOU 1066 CD2 LEU A 141 5123 4614 5663 480 -328 -669 C ATOM 1067 N ALA A 142 12.068 7.293 9.704 1.00 18.95 N ANISOU 1067 N ALA A 142 2537 1775 2887 376 -208 -451 N ATOM 1068 CA ALA A 142 11.254 6.394 8.898 1.00 18.44 C ANISOU 1068 CA ALA A 142 2493 1710 2805 364 -193 -425 C ATOM 1069 C ALA A 142 11.305 4.978 9.454 1.00 18.49 C ANISOU 1069 C ALA A 142 2504 1728 2795 323 -159 -392 C ATOM 1070 O ALA A 142 10.276 4.323 9.596 1.00 19.58 O ANISOU 1070 O ALA A 142 2628 1894 2917 323 -160 -412 O ATOM 1071 CB ALA A 142 11.705 6.409 7.450 1.00 16.61 C ANISOU 1071 CB ALA A 142 2313 1427 2572 351 -174 -370 C ATOM 1072 N ARG A 143 12.504 4.495 9.766 1.00 15.95 N ANISOU 1072 N ARG A 143 2203 1384 2474 288 -130 -345 N ATOM 1073 CA ARG A 143 12.611 3.135 10.278 1.00 12.97 C ANISOU 1073 CA ARG A 143 1837 1013 2077 247 -103 -310 C ATOM 1074 C ARG A 143 12.047 3.044 11.692 1.00 14.52 C ANISOU 1074 C ARG A 143 1990 1257 2271 255 -115 -370 C ATOM 1075 O ARG A 143 11.599 1.988 12.121 1.00 15.88 O ANISOU 1075 O ARG A 143 2169 1443 2422 226 -100 -365 O ATOM 1076 CB ARG A 143 14.049 2.583 10.167 1.00 14.35 C ANISOU 1076 CB ARG A 143 2045 1159 2248 211 -74 -247 C ATOM 1077 CG ARG A 143 15.070 3.143 11.142 1.00 13.00 C ANISOU 1077 CG ARG A 143 1853 990 2095 213 -80 -261 C ATOM 1078 CD ARG A 143 14.976 2.464 12.519 1.00 16.85 C ANISOU 1078 CD ARG A 143 2320 1505 2576 195 -81 -278 C ATOM 1079 NE ARG A 143 16.279 2.389 13.171 1.00 21.55 N ANISOU 1079 NE ARG A 143 2916 2091 3181 176 -74 -257 N ATOM 1080 CZ ARG A 143 16.923 3.434 13.677 1.00 27.96 C ANISOU 1080 CZ ARG A 143 3701 2902 4019 198 -90 -287 C ATOM 1081 NH1 ARG A 143 16.388 4.644 13.603 1.00 33.01 N ANISOU 1081 NH1 ARG A 143 4315 3552 4675 238 -116 -339 N ATOM 1082 NH2 ARG A 143 18.104 3.272 14.252 1.00 26.81 N ANISOU 1082 NH2 ARG A 143 3555 2749 3883 179 -85 -266 N ATOM 1083 N ASN A 144 12.044 4.157 12.413 1.00 17.22 N ANISOU 1083 N ASN A 144 2288 1628 2628 292 -142 -432 N ATOM 1084 CA ASN A 144 11.459 4.152 13.744 1.00 19.52 C ANISOU 1084 CA ASN A 144 2529 1984 2905 306 -150 -504 C ATOM 1085 C ASN A 144 9.975 3.788 13.709 1.00 20.60 C ANISOU 1085 C ASN A 144 2634 2177 3016 323 -158 -561 C ATOM 1086 O ASN A 144 9.472 3.127 14.616 1.00 21.37 O ANISOU 1086 O ASN A 144 2660 2336 3123 324 -189 -653 O ATOM 1087 CB ASN A 144 11.682 5.487 14.450 1.00 21.47 C ANISOU 1087 CB ASN A 144 2729 2260 3166 349 -184 -567 C ATOM 1088 CG ASN A 144 13.093 5.636 14.980 1.00 25.94 C ANISOU 1088 CG ASN A 144 3310 2793 3754 328 -176 -534 C ATOM 1089 OD1 ASN A 144 13.880 4.686 14.965 1.00 24.32 O ANISOU 1089 OD1 ASN A 144 3142 2553 3547 284 -146 -470 O ATOM 1090 ND2 ASN A 144 13.423 6.832 15.459 1.00 26.38 N ANISOU 1090 ND2 ASN A 144 3336 2861 3827 361 -207 -579 N ATOM 1091 N ARG A 145 9.284 4.196 12.649 1.00 14.91 N ANISOU 1091 N ARG A 145 1921 1447 2298 347 -172 -559 N ATOM 1092 CA ARG A 145 7.873 3.879 12.507 1.00 16.55 C ANISOU 1092 CA ARG A 145 2081 1713 2495 372 -200 -631 C ATOM 1093 C ARG A 145 7.681 2.389 12.287 1.00 17.84 C ANISOU 1093 C ARG A 145 2261 1853 2663 327 -195 -613 C ATOM 1094 O ARG A 145 6.700 1.808 12.753 1.00 21.43 O ANISOU 1094 O ARG A 145 2640 2390 3113 336 -227 -721 O ATOM 1095 CB ARG A 145 7.240 4.677 11.357 1.00 22.70 C ANISOU 1095 CB ARG A 145 2878 2475 3270 403 -212 -618 C ATOM 1096 CG ARG A 145 7.152 3.950 10.009 1.00 22.53 C ANISOU 1096 CG ARG A 145 2917 2389 3253 376 -198 -545 C ATOM 1097 CD ARG A 145 6.843 4.960 8.910 1.00 23.81 C ANISOU 1097 CD ARG A 145 3089 2529 3429 414 -234 -552 C ATOM 1098 NE ARG A 145 6.579 4.352 7.611 1.00 24.02 N ANISOU 1098 NE ARG A 145 3163 2509 3452 395 -225 -497 N ATOM 1099 CZ ARG A 145 7.522 3.876 6.802 1.00 28.95 C ANISOU 1099 CZ ARG A 145 3846 3073 4082 356 -194 -414 C ATOM 1100 NH1 ARG A 145 8.800 3.925 7.165 1.00 24.69 N ANISOU 1100 NH1 ARG A 145 3322 2509 3550 333 -170 -378 N ATOM 1101 NH2 ARG A 145 7.184 3.349 5.634 1.00 25.83 N ANISOU 1101 NH2 ARG A 145 3486 2650 3679 343 -187 -374 N ATOM 1102 N LEU A 146 8.619 1.770 11.577 1.00 12.89 N ANISOU 1102 N LEU A 146 1731 1140 2028 272 -143 -483 N ATOM 1103 CA LEU A 146 8.546 0.340 11.335 1.00 11.03 C ANISOU 1103 CA LEU A 146 1529 869 1795 215 -140 -443 C ATOM 1104 C LEU A 146 8.758 -0.467 12.618 1.00 12.98 C ANISOU 1104 C LEU A 146 1734 1135 2065 172 -166 -503 C ATOM 1105 O LEU A 146 8.113 -1.495 12.812 1.00 18.78 O ANISOU 1105 O LEU A 146 2448 1883 2804 114 -195 -550 O ATOM 1106 CB LEU A 146 9.549 -0.086 10.252 1.00 13.34 C ANISOU 1106 CB LEU A 146 1910 1099 2059 175 -81 -309 C ATOM 1107 CG LEU A 146 9.410 0.589 8.885 1.00 12.62 C ANISOU 1107 CG LEU A 146 1828 987 1982 209 -91 -293 C ATOM 1108 CD1 LEU A 146 10.434 0.018 7.889 1.00 13.52 C ANISOU 1108 CD1 LEU A 146 1988 1059 2089 178 -63 -210 C ATOM 1109 CD2 LEU A 146 7.981 0.495 8.321 1.00 13.02 C ANISOU 1109 CD2 LEU A 146 1866 1054 2025 228 -109 -327 C ATOM 1110 N VAL A 147 9.666 -0.018 13.483 1.00 11.39 N ANISOU 1110 N VAL A 147 1521 941 1867 178 -155 -505 N ATOM 1111 CA VAL A 147 9.910 -0.723 14.740 1.00 11.03 C ANISOU 1111 CA VAL A 147 1433 925 1832 122 -172 -570 C ATOM 1112 C VAL A 147 8.624 -0.754 15.561 1.00 15.29 C ANISOU 1112 C VAL A 147 1848 1678 2284 103 -186 -666 C ATOM 1113 O VAL A 147 8.213 -1.798 16.065 1.00 15.41 O ANISOU 1113 O VAL A 147 1827 1814 2213 -4 -174 -610 O ATOM 1114 CB VAL A 147 11.045 -0.067 15.555 1.00 11.95 C ANISOU 1114 CB VAL A 147 1548 1037 1954 142 -158 -552 C ATOM 1115 CG1 VAL A 147 11.064 -0.592 16.989 1.00 11.01 C ANISOU 1115 CG1 VAL A 147 1361 1016 1808 82 -171 -627 C ATOM 1116 CG2 VAL A 147 12.388 -0.302 14.888 1.00 14.32 C ANISOU 1116 CG2 VAL A 147 1954 1257 2230 113 -106 -389 C ATOM 1117 N ILE A 148 7.980 0.399 15.668 1.00 14.53 N ANISOU 1117 N ILE A 148 1684 1647 2191 203 -204 -788 N ATOM 1118 CA ILE A 148 6.757 0.516 16.445 1.00 15.01 C ANISOU 1118 CA ILE A 148 1615 1937 2152 195 -208 -869 C ATOM 1119 C ILE A 148 5.597 -0.263 15.798 1.00 16.99 C ANISOU 1119 C ILE A 148 1841 2265 2347 141 -209 -834 C ATOM 1120 O ILE A 148 4.919 -1.046 16.463 1.00 17.54 O ANISOU 1120 O ILE A 148 1836 2508 2319 48 -196 -814 O ATOM 1121 CB ILE A 148 6.386 1.992 16.684 1.00 18.96 C ANISOU 1121 CB ILE A 148 2053 2478 2673 327 -233 -1015 C ATOM 1122 CG1 ILE A 148 7.519 2.717 17.424 1.00 18.58 C ANISOU 1122 CG1 ILE A 148 2023 2371 2664 356 -234 -1009 C ATOM 1123 CG2 ILE A 148 5.085 2.103 17.469 1.00 28.15 C ANISOU 1123 CG2 ILE A 148 3075 3889 3731 324 -236 -1104 C ATOM 1124 CD1 ILE A 148 8.006 2.009 18.678 1.00 18.29 C ANISOU 1124 CD1 ILE A 148 1952 2429 2570 274 -214 -1006 C ATOM 1125 N ALA A 149 5.385 -0.070 14.503 1.00 17.11 N ANISOU 1125 N ALA A 149 1924 2151 2426 195 -225 -824 N ATOM 1126 CA ALA A 149 4.299 -0.766 13.809 1.00 22.04 C ANISOU 1126 CA ALA A 149 2532 2837 3007 151 -231 -793 C ATOM 1127 C ALA A 149 4.420 -2.285 13.917 1.00 19.17 C ANISOU 1127 C ALA A 149 2198 2497 2589 4 -210 -663 C ATOM 1128 O ALA A 149 3.425 -2.987 14.071 1.00 18.52 O ANISOU 1128 O ALA A 149 2049 2562 2424 -71 -209 -649 O ATOM 1129 CB ALA A 149 4.242 -0.346 12.343 1.00 18.67 C ANISOU 1129 CB ALA A 149 2194 2235 2664 233 -253 -791 C ATOM 1130 N LEU A 150 5.646 -2.793 13.834 1.00 19.28 N ANISOU 1130 N LEU A 150 2313 2364 2649 -37 -197 -569 N ATOM 1131 CA LEU A 150 5.865 -4.236 13.853 1.00 18.89 C ANISOU 1131 CA LEU A 150 2311 2311 2557 -169 -184 -442 C ATOM 1132 C LEU A 150 5.683 -4.855 15.238 1.00 21.90 C ANISOU 1132 C LEU A 150 2608 2879 2833 -272 -169 -431 C ATOM 1133 O LEU A 150 5.437 -6.056 15.363 1.00 20.34 O ANISOU 1133 O LEU A 150 2420 2736 2571 -391 -164 -342 O ATOM 1134 CB LEU A 150 7.254 -4.572 13.302 1.00 16.58 C ANISOU 1134 CB LEU A 150 2152 1799 2348 -173 -176 -349 C ATOM 1135 CG LEU A 150 7.591 -6.055 13.119 1.00 16.90 C ANISOU 1135 CG LEU A 150 2267 1797 2359 -295 -170 -213 C ATOM 1136 CD1 LEU A 150 6.690 -6.691 12.058 1.00 17.43 C ANISOU 1136 CD1 LEU A 150 2362 1851 2408 -324 -184 -168 C ATOM 1137 CD2 LEU A 150 9.048 -6.211 12.720 1.00 13.48 C ANISOU 1137 CD2 LEU A 150 1951 1159 2011 -281 -162 -142 C ATOM 1138 N SER A 151 5.792 -4.034 16.275 1.00 21.31 N ANISOU 1138 N SER A 151 2456 2902 2741 -227 -165 -521 N ATOM 1139 CA SER A 151 5.856 -4.543 17.641 1.00 19.02 C ANISOU 1139 CA SER A 151 2102 2766 2359 -318 -149 -509 C ATOM 1140 C SER A 151 4.500 -4.530 18.328 1.00 22.28 C ANISOU 1140 C SER A 151 2378 3425 2663 -350 -144 -579 C ATOM 1141 O SER A 151 3.674 -3.659 18.069 1.00 27.90 O ANISOU 1141 O SER A 151 3021 4200 3382 -263 -154 -681 O ATOM 1142 CB SER A 151 6.853 -3.719 18.453 1.00 17.85 C ANISOU 1142 CB SER A 151 1952 2580 2250 -256 -147 -562 C ATOM 1143 OG SER A 151 8.132 -3.752 17.827 1.00 19.78 O ANISOU 1143 OG SER A 151 2318 2603 2596 -231 -149 -497 O ATOM 1144 N ASP A 152 4.278 -5.509 19.199 1.00 24.85 N ANISOU 1144 N ASP A 152 2666 3889 2889 -478 -129 -523 N ATOM 1145 CA ASP A 152 3.018 -5.633 19.925 1.00 25.47 C ANISOU 1145 CA ASP A 152 2611 4213 2852 -530 -118 -577 C ATOM 1146 C ASP A 152 3.084 -4.835 21.219 1.00 26.13 C ANISOU 1146 C ASP A 152 2602 4433 2891 -489 -107 -677 C ATOM 1147 O ASP A 152 2.093 -4.246 21.648 1.00 28.51 O ANISOU 1147 O ASP A 152 2784 4911 3137 -452 -102 -781 O ATOM 1148 CB ASP A 152 2.724 -7.103 20.232 1.00 23.98 C ANISOU 1148 CB ASP A 152 2432 4108 2572 -696 -107 -464 C ATOM 1149 CG ASP A 152 2.542 -7.933 18.977 1.00 29.06 C ANISOU 1149 CG ASP A 152 3162 4631 3249 -741 -122 -368 C ATOM 1150 OD1 ASP A 152 1.692 -7.570 18.136 1.00 27.81 O ANISOU 1150 OD1 ASP A 152 2972 4480 3113 -686 -133 -414 O ATOM 1151 OD2 ASP A 152 3.263 -8.938 18.825 1.00 28.32 O ANISOU 1151 OD2 ASP A 152 3169 4430 3161 -826 -126 -249 O ATOM 1152 N VAL A 153 4.265 -4.827 21.828 1.00 25.50 N ANISOU 1152 N VAL A 153 2580 4272 2837 -495 -104 -647 N ATOM 1153 CA VAL A 153 4.522 -4.087 23.051 1.00 25.98 C ANISOU 1153 CA VAL A 153 2573 4435 2864 -454 -98 -733 C ATOM 1154 C VAL A 153 5.823 -3.306 22.894 1.00 25.98 C ANISOU 1154 C VAL A 153 2654 4240 2976 -357 -113 -749 C ATOM 1155 O VAL A 153 6.746 -3.766 22.226 1.00 23.83 O ANISOU 1155 O VAL A 153 2496 3779 2778 -374 -119 -657 O ATOM 1156 CB VAL A 153 4.648 -5.037 24.250 1.00 27.16 C ANISOU 1156 CB VAL A 153 2702 4715 2905 -589 -80 -672 C ATOM 1157 CG1 VAL A 153 5.001 -4.264 25.501 1.00 22.73 C ANISOU 1157 CG1 VAL A 153 2080 4244 2311 -542 -75 -759 C ATOM 1158 CG2 VAL A 153 3.355 -5.815 24.444 1.00 29.14 C ANISOU 1158 CG2 VAL A 153 2868 5164 3038 -695 -62 -654 C ATOM 1159 N VAL A 154 5.894 -2.126 23.502 1.00 23.57 N ANISOU 1159 N VAL A 154 2290 3982 2684 -255 -119 -866 N ATOM 1160 CA VAL A 154 7.067 -1.264 23.375 1.00 18.86 C ANISOU 1160 CA VAL A 154 1762 3209 2195 -159 -136 -893 C ATOM 1161 C VAL A 154 7.673 -0.948 24.743 1.00 22.43 C ANISOU 1161 C VAL A 154 2178 3734 2608 -161 -135 -934 C ATOM 1162 O VAL A 154 7.002 -0.395 25.618 1.00 22.28 O ANISOU 1162 O VAL A 154 2055 3892 2516 -132 -132 -1033 O ATOM 1163 CB VAL A 154 6.726 0.061 22.651 1.00 17.55 C ANISOU 1163 CB VAL A 154 1579 2983 2105 -10 -158 -1003 C ATOM 1164 CG1 VAL A 154 7.915 1.016 22.684 1.00 21.79 C ANISOU 1164 CG1 VAL A 154 2177 3358 2744 84 -176 -1039 C ATOM 1165 CG2 VAL A 154 6.288 -0.209 21.216 1.00 20.17 C ANISOU 1165 CG2 VAL A 154 1965 3209 2488 0 -163 -958 C ATOM 1166 N ILE A 155 8.935 -1.323 24.926 1.00 16.87 N ANISOU 1166 N ILE A 155 1562 2896 1952 -195 -138 -859 N ATOM 1167 CA ILE A 155 9.647 -1.023 26.159 1.00 20.50 C ANISOU 1167 CA ILE A 155 2002 3399 2388 -193 -143 -892 C ATOM 1168 C ILE A 155 10.690 0.061 25.929 1.00 19.27 C ANISOU 1168 C ILE A 155 1898 3071 2352 -79 -165 -941 C ATOM 1169 O ILE A 155 11.548 -0.070 25.052 1.00 19.75 O ANISOU 1169 O ILE A 155 2057 2934 2515 -67 -171 -875 O ATOM 1170 CB ILE A 155 10.343 -2.275 26.728 1.00 21.05 C ANISOU 1170 CB ILE A 155 2126 3459 2412 -322 -135 -774 C ATOM 1171 CG1 ILE A 155 9.307 -3.361 27.034 1.00 20.80 C ANISOU 1171 CG1 ILE A 155 2046 3604 2254 -445 -115 -723 C ATOM 1172 CG2 ILE A 155 11.155 -1.918 27.975 1.00 25.80 C ANISOU 1172 CG2 ILE A 155 2716 4089 2997 -313 -145 -810 C ATOM 1173 CD1 ILE A 155 9.925 -4.698 27.395 1.00 21.73 C ANISOU 1173 CD1 ILE A 155 2234 3694 2329 -578 -113 -594 C ATOM 1174 N ILE A 156 10.612 1.131 26.720 1.00 19.76 N ANISOU 1174 N ILE A 156 1894 3211 2402 4 -178 -1059 N ATOM 1175 CA ILE A 156 11.640 2.164 26.706 1.00 17.06 C ANISOU 1175 CA ILE A 156 1596 2721 2165 102 -203 -1108 C ATOM 1176 C ILE A 156 12.318 2.226 28.079 1.00 19.73 C ANISOU 1176 C ILE A 156 1912 3122 2461 80 -210 -1129 C ATOM 1177 O ILE A 156 11.825 2.894 28.985 1.00 24.11 O ANISOU 1177 O ILE A 156 2383 3824 2954 124 -217 -1231 O ATOM 1178 CB ILE A 156 11.054 3.546 26.344 1.00 18.95 C ANISOU 1178 CB ILE A 156 1791 2965 2445 239 -224 -1239 C ATOM 1179 CG1 ILE A 156 10.313 3.483 25.001 1.00 23.94 C ANISOU 1179 CG1 ILE A 156 2443 3542 3111 263 -220 -1222 C ATOM 1180 CG2 ILE A 156 12.156 4.591 26.299 1.00 21.16 C ANISOU 1180 CG2 ILE A 156 2124 3079 2838 328 -251 -1258 C ATOM 1181 CD1 ILE A 156 9.631 4.785 24.610 1.00 20.98 C ANISOU 1181 CD1 ILE A 156 2026 3172 2774 382 -247 -1299 C ATOM 1182 N PRO A 157 13.440 1.509 28.241 1.00 19.71 N ANISOU 1182 N PRO A 157 1985 3011 2491 12 -211 -1032 N ATOM 1183 CA PRO A 157 14.172 1.448 29.515 1.00 21.27 C ANISOU 1183 CA PRO A 157 2175 3255 2652 -17 -222 -1038 C ATOM 1184 C PRO A 157 14.596 2.823 30.027 1.00 25.46 C ANISOU 1184 C PRO A 157 2679 3762 3232 98 -250 -1155 C ATOM 1185 O PRO A 157 14.398 3.127 31.206 1.00 28.11 O ANISOU 1185 O PRO A 157 2950 4240 3490 104 -257 -1223 O ATOM 1186 CB PRO A 157 15.408 0.614 29.161 1.00 24.51 C ANISOU 1186 CB PRO A 157 2689 3491 3131 -80 -224 -917 C ATOM 1187 CG PRO A 157 14.946 -0.259 28.050 1.00 21.35 C ANISOU 1187 CG PRO A 157 2331 3046 2736 -136 -204 -828 C ATOM 1188 CD PRO A 157 14.013 0.595 27.240 1.00 21.16 C ANISOU 1188 CD PRO A 157 2267 3036 2737 -47 -201 -907 C ATOM 1189 N GLN A 158 15.173 3.639 29.151 1.00 24.04 N ANISOU 1189 N GLN A 158 2552 3403 3179 187 -267 -1177 N ATOM 1190 CA GLN A 158 15.656 4.964 29.527 1.00 21.90 C ANISOU 1190 CA GLN A 158 2269 3083 2971 292 -295 -1253 C ATOM 1191 C GLN A 158 15.632 5.898 28.318 1.00 24.03 C ANISOU 1191 C GLN A 158 2573 3218 3341 364 -303 -1201 C ATOM 1192 O GLN A 158 15.950 5.483 27.206 1.00 21.05 O ANISOU 1192 O GLN A 158 2266 2709 3022 340 -288 -1112 O ATOM 1193 CB GLN A 158 17.082 4.874 30.093 1.00 26.25 C ANISOU 1193 CB GLN A 158 2874 3525 3575 270 -311 -1210 C ATOM 1194 CG GLN A 158 17.639 6.204 30.570 1.00 28.99 C ANISOU 1194 CG GLN A 158 3206 3833 3978 353 -338 -1226 C ATOM 1195 CD GLN A 158 19.122 6.162 30.886 1.00 25.99 C ANISOU 1195 CD GLN A 158 2885 3325 3665 334 -352 -1164 C ATOM 1196 OE1 GLN A 158 19.788 7.197 30.903 1.00 30.34 O ANISOU 1196 OE1 GLN A 158 3448 3806 4274 378 -374 -1138 O ATOM 1197 NE2 GLN A 158 19.646 4.970 31.146 1.00 19.77 N ANISOU 1197 NE2 GLN A 158 2136 2516 2860 252 -345 -1133 N ATOM 1198 N ALA A 159 15.263 7.158 28.535 1.00 30.11 N ANISOU 1198 N ALA A 159 3299 4028 4114 434 -333 -1241 N ATOM 1199 CA ALA A 159 15.195 8.123 27.442 1.00 29.29 C ANISOU 1199 CA ALA A 159 3239 3821 4068 470 -350 -1183 C ATOM 1200 C ALA A 159 15.095 9.569 27.919 1.00 28.59 C ANISOU 1200 C ALA A 159 3122 3763 3980 529 -394 -1227 C ATOM 1201 O ALA A 159 14.420 9.866 28.912 1.00 29.33 O ANISOU 1201 O ALA A 159 3131 3999 4013 562 -414 -1325 O ATOM 1202 CB ALA A 159 14.024 7.795 26.520 1.00 24.28 C ANISOU 1202 CB ALA A 159 2590 3226 3410 472 -337 -1190 C ATOM 1203 N ASP A 160 15.759 10.466 27.196 1.00 29.52 N ANISOU 1203 N ASP A 160 3309 3755 4151 533 -404 -1152 N ATOM 1204 CA ASP A 160 15.657 11.898 27.471 1.00 34.20 C ANISOU 1204 CA ASP A 160 3888 4361 4745 582 -446 -1189 C ATOM 1205 C ASP A 160 14.398 12.488 26.847 1.00 36.78 C ANISOU 1205 C ASP A 160 4190 4739 5046 620 -465 -1226 C ATOM 1206 O ASP A 160 13.697 11.827 26.077 1.00 35.27 O ANISOU 1206 O ASP A 160 4001 4557 4844 606 -443 -1211 O ATOM 1207 CB ASP A 160 16.876 12.653 26.928 1.00 36.28 C ANISOU 1207 CB ASP A 160 4234 4491 5061 562 -438 -1096 C ATOM 1208 CG ASP A 160 18.162 12.290 27.644 1.00 40.72 C ANISOU 1208 CG ASP A 160 4814 5010 5649 532 -430 -1066 C ATOM 1209 OD1 ASP A 160 18.288 12.619 28.843 1.00 42.52 O ANISOU 1209 OD1 ASP A 160 4992 5299 5863 561 -464 -1140 O ATOM 1210 OD2 ASP A 160 19.056 11.694 27.001 1.00 43.29 O ANISOU 1210 OD2 ASP A 160 5198 5245 6006 484 -394 -974 O ATOM 1211 N LEU A 161 14.121 13.743 27.185 1.00 39.49 N ANISOU 1211 N LEU A 161 4511 5111 5381 669 -509 -1276 N ATOM 1212 CA LEU A 161 13.036 14.481 26.557 1.00 45.95 C ANISOU 1212 CA LEU A 161 5316 5962 6182 708 -535 -1308 C ATOM 1213 C LEU A 161 13.463 14.940 25.169 1.00 47.66 C ANISOU 1213 C LEU A 161 5606 6051 6452 697 -537 -1234 C ATOM 1214 O LEU A 161 14.647 15.151 24.917 1.00 48.70 O ANISOU 1214 O LEU A 161 5784 6087 6632 674 -538 -1182 O ATOM 1215 CB LEU A 161 12.639 15.686 27.413 1.00 48.71 C ANISOU 1215 CB LEU A 161 5613 6387 6506 770 -592 -1397 C ATOM 1216 CG LEU A 161 11.780 15.396 28.644 1.00 51.54 C ANISOU 1216 CG LEU A 161 5862 6922 6796 804 -612 -1509 C ATOM 1217 CD1 LEU A 161 11.724 16.603 29.574 1.00 51.76 C ANISOU 1217 CD1 LEU A 161 5853 7005 6808 862 -668 -1583 C ATOM 1218 CD2 LEU A 161 10.383 14.970 28.220 1.00 52.80 C ANISOU 1218 CD2 LEU A 161 5967 7186 6909 817 -609 -1554 C ATOM 1219 N LYS A 162 12.493 15.089 24.273 1.00 48.39 N ANISOU 1219 N LYS A 162 5696 6156 6534 716 -549 -1245 N ATOM 1220 CA LYS A 162 12.756 15.561 22.918 1.00 48.83 C ANISOU 1220 CA LYS A 162 5807 6111 6634 714 -565 -1196 C ATOM 1221 C LYS A 162 13.703 14.630 22.158 1.00 47.06 C ANISOU 1221 C LYS A 162 5646 5789 6446 651 -511 -1093 C ATOM 1222 O LYS A 162 14.472 15.080 21.310 1.00 49.43 O ANISOU 1222 O LYS A 162 5994 5998 6788 639 -518 -1043 O ATOM 1223 CB LYS A 162 13.331 16.982 22.942 1.00 51.90 C ANISOU 1223 CB LYS A 162 6208 6458 7055 751 -624 -1222 C ATOM 1224 CG LYS A 162 12.626 17.942 23.897 1.00 56.26 C ANISOU 1224 CG LYS A 162 6699 7104 7573 815 -681 -1325 C ATOM 1225 CD LYS A 162 11.160 18.145 23.528 1.00 61.25 C ANISOU 1225 CD LYS A 162 7292 7813 8165 858 -707 -1382 C ATOM 1226 CE LYS A 162 10.479 19.116 24.489 1.00 61.93 C ANISOU 1226 CE LYS A 162 7315 8000 8215 924 -767 -1486 C ATOM 1227 NZ LYS A 162 9.037 19.317 24.165 1.00 60.01 N ANISOU 1227 NZ LYS A 162 7028 7843 7932 968 -795 -1547 N ATOM 1228 N SER A 163 13.647 13.337 22.465 1.00 41.36 N ANISOU 1228 N SER A 163 4921 5090 5703 611 -458 -1063 N ATOM 1229 CA SER A 163 14.497 12.350 21.801 1.00 31.53 C ANISOU 1229 CA SER A 163 3735 3760 4486 553 -409 -967 C ATOM 1230 C SER A 163 13.700 11.528 20.796 1.00 32.74 C ANISOU 1230 C SER A 163 3907 3908 4625 536 -380 -933 C ATOM 1231 O SER A 163 12.474 11.617 20.752 1.00 38.05 O ANISOU 1231 O SER A 163 4542 4652 5264 566 -393 -986 O ATOM 1232 CB SER A 163 15.137 11.419 22.831 1.00 32.15 C ANISOU 1232 CB SER A 163 3808 3854 4552 518 -373 -951 C ATOM 1233 OG SER A 163 14.147 10.778 23.619 1.00 32.67 O ANISOU 1233 OG SER A 163 3814 4029 4568 529 -368 -1020 O ATOM 1234 N GLY A 164 14.398 10.729 19.991 1.00 29.59 N ANISOU 1234 N GLY A 164 3547 4516 3180 63 -286 -1226 N ATOM 1235 CA GLY A 164 13.741 9.842 19.047 1.00 30.87 C ANISOU 1235 CA GLY A 164 3778 4593 3358 117 -327 -1162 C ATOM 1236 C GLY A 164 12.871 8.840 19.783 1.00 30.93 C ANISOU 1236 C GLY A 164 3744 4643 3366 147 -332 -1154 C ATOM 1237 O GLY A 164 11.787 8.483 19.325 1.00 32.70 O ANISOU 1237 O GLY A 164 4003 4779 3645 181 -373 -1138 O ATOM 1238 N SER A 165 13.348 8.394 20.941 1.00 29.16 N ANISOU 1238 N SER A 165 3444 4555 3081 132 -291 -1165 N ATOM 1239 CA SER A 165 12.585 7.478 21.775 1.00 29.41 C ANISOU 1239 CA SER A 165 3428 4642 3106 152 -291 -1160 C ATOM 1240 C SER A 165 11.208 8.056 22.075 1.00 29.66 C ANISOU 1240 C SER A 165 3437 4604 3228 147 -312 -1223 C ATOM 1241 O SER A 165 10.209 7.341 22.050 1.00 32.18 O ANISOU 1241 O SER A 165 3760 4889 3576 179 -340 -1201 O ATOM 1242 CB SER A 165 13.324 7.195 23.080 1.00 29.51 C ANISOU 1242 CB SER A 165 3357 4812 3044 121 -243 -1176 C ATOM 1243 OG SER A 165 14.532 6.501 22.837 1.00 29.66 O ANISOU 1243 OG SER A 165 3391 4897 2982 133 -227 -1113 O ATOM 1244 N MET A 166 11.158 9.355 22.347 1.00 28.16 N ANISOU 1244 N MET A 166 3221 4391 3085 107 -301 -1301 N ATOM 1245 CA MET A 166 9.897 10.005 22.693 1.00 31.28 C ANISOU 1245 CA MET A 166 3587 4725 3573 101 -317 -1371 C ATOM 1246 C MET A 166 8.963 10.096 21.489 1.00 32.03 C ANISOU 1246 C MET A 166 3757 4662 3750 136 -377 -1347 C ATOM 1247 O MET A 166 7.747 9.937 21.620 1.00 27.42 O ANISOU 1247 O MET A 166 3159 4028 3231 156 -401 -1366 O ATOM 1248 CB MET A 166 10.143 11.384 23.307 1.00 32.55 C ANISOU 1248 CB MET A 166 3702 4903 3763 50 -291 -1465 C ATOM 1249 CG MET A 166 10.807 11.319 24.682 1.00 31.87 C ANISOU 1249 CG MET A 166 3531 4974 3604 11 -235 -1501 C ATOM 1250 SD MET A 166 9.859 10.323 25.856 1.00 40.88 S ANISOU 1250 SD MET A 166 4599 6203 4730 23 -218 -1509 S ATOM 1251 CE MET A 166 8.443 11.380 26.142 1.00 58.51 C ANISOU 1251 CE MET A 166 6800 8346 7087 15 -229 -1600 C ATOM 1252 N SER A 167 9.537 10.340 20.316 1.00 31.86 N ANISOU 1252 N SER A 167 3815 4563 3726 143 -400 -1305 N ATOM 1253 CA SER A 167 8.762 10.330 19.081 1.00 32.35 C ANISOU 1253 CA SER A 167 3959 4476 3856 176 -460 -1269 C ATOM 1254 C SER A 167 8.156 8.953 18.864 1.00 28.60 C ANISOU 1254 C SER A 167 3506 3997 3364 225 -484 -1201 C ATOM 1255 O SER A 167 6.991 8.829 18.488 1.00 29.21 O ANISOU 1255 O SER A 167 3605 3980 3514 251 -528 -1198 O ATOM 1256 CB SER A 167 9.637 10.700 17.881 1.00 35.45 C ANISOU 1256 CB SER A 167 4437 4806 4228 171 -475 -1227 C ATOM 1257 OG SER A 167 10.140 12.018 17.998 1.00 44.60 O ANISOU 1257 OG SER A 167 5581 5955 5409 123 -460 -1287 O ATOM 1258 N SER A 168 8.956 7.918 19.096 1.00 27.60 N ANISOU 1258 N SER A 168 3373 3970 3144 238 -457 -1145 N ATOM 1259 CA SER A 168 8.480 6.548 18.964 1.00 27.32 C ANISOU 1259 CA SER A 168 3356 3941 3085 283 -479 -1078 C ATOM 1260 C SER A 168 7.403 6.249 20.001 1.00 23.98 C ANISOU 1260 C SER A 168 2860 3557 2696 283 -476 -1115 C ATOM 1261 O SER A 168 6.450 5.516 19.733 1.00 19.96 O ANISOU 1261 O SER A 168 2371 2995 2219 317 -514 -1080 O ATOM 1262 CB SER A 168 9.640 5.578 19.116 1.00 25.31 C ANISOU 1262 CB SER A 168 3100 3792 2723 293 -449 -1019 C ATOM 1263 OG SER A 168 10.618 5.836 18.118 1.00 26.88 O ANISOU 1263 OG SER A 168 3366 3956 2891 294 -449 -986 O ATOM 1264 N ALA A 169 7.561 6.825 21.186 1.00 24.41 N ANISOU 1264 N ALA A 169 2829 3705 2741 242 -431 -1185 N ATOM 1265 CA ALA A 169 6.570 6.661 22.241 1.00 23.94 C ANISOU 1265 CA ALA A 169 2693 3690 2711 235 -421 -1230 C ATOM 1266 C ALA A 169 5.223 7.247 21.817 1.00 24.79 C ANISOU 1266 C ALA A 169 2813 3671 2934 247 -463 -1268 C ATOM 1267 O ALA A 169 4.174 6.675 22.098 1.00 25.84 O ANISOU 1267 O ALA A 169 2923 3794 3102 266 -481 -1264 O ATOM 1268 CB ALA A 169 7.058 7.300 23.537 1.00 26.37 C ANISOU 1268 CB ALA A 169 2913 4119 2987 185 -363 -1305 C ATOM 1269 N ARG A 170 5.254 8.388 21.140 1.00 23.40 N ANISOU 1269 N ARG A 170 2674 3396 2819 236 -481 -1305 N ATOM 1270 CA ARG A 170 4.019 8.995 20.663 1.00 29.85 C ANISOU 1270 CA ARG A 170 3507 4083 3752 249 -527 -1340 C ATOM 1271 C ARG A 170 3.397 8.140 19.564 1.00 26.65 C ANISOU 1271 C ARG A 170 3180 3575 3370 296 -587 -1259 C ATOM 1272 O ARG A 170 2.176 8.039 19.460 1.00 28.96 O ANISOU 1272 O ARG A 170 3467 3796 3741 316 -623 -1268 O ATOM 1273 CB ARG A 170 4.254 10.431 20.192 1.00 35.96 C ANISOU 1273 CB ARG A 170 4304 4773 4584 223 -538 -1396 C ATOM 1274 CG ARG A 170 4.436 11.417 21.340 1.00 45.42 C ANISOU 1274 CG ARG A 170 5418 6047 5792 178 -489 -1496 C ATOM 1275 CD ARG A 170 4.548 12.854 20.852 1.00 55.57 C ANISOU 1275 CD ARG A 170 6729 7237 7147 154 -508 -1553 C ATOM 1276 NE ARG A 170 5.906 13.378 20.990 1.00 63.53 N ANISOU 1276 NE ARG A 170 7740 8312 8088 116 -471 -1561 N ATOM 1277 CZ ARG A 170 6.772 13.500 19.987 1.00 66.78 C ANISOU 1277 CZ ARG A 170 8227 8678 8467 114 -488 -1507 C ATOM 1278 NH1 ARG A 170 6.424 13.142 18.757 1.00 68.48 N ANISOU 1278 NH1 ARG A 170 8528 8781 8710 146 -541 -1441 N ATOM 1279 NH2 ARG A 170 7.985 13.987 20.214 1.00 65.65 N ANISOU 1279 NH2 ARG A 170 8076 8605 8263 76 -451 -1518 N ATOM 1280 N LEU A 171 4.241 7.506 18.756 1.00 25.47 N ANISOU 1280 N LEU A 171 3103 3421 3153 314 -597 -1181 N ATOM 1281 CA LEU A 171 3.756 6.569 17.749 1.00 23.54 C ANISOU 1281 CA LEU A 171 2935 3091 2916 359 -651 -1099 C ATOM 1282 C LEU A 171 3.083 5.370 18.401 1.00 18.44 C ANISOU 1282 C LEU A 171 2249 2507 2252 382 -652 -1069 C ATOM 1283 O LEU A 171 2.062 4.893 17.924 1.00 19.96 O ANISOU 1283 O LEU A 171 2471 2616 2498 412 -701 -1038 O ATOM 1284 CB LEU A 171 4.896 6.080 16.857 1.00 29.87 C ANISOU 1284 CB LEU A 171 3816 3894 3638 373 -651 -1026 C ATOM 1285 CG LEU A 171 5.191 6.889 15.599 1.00 36.60 C ANISOU 1285 CG LEU A 171 4756 4628 4522 368 -684 -1016 C ATOM 1286 CD1 LEU A 171 6.292 6.212 14.790 1.00 32.18 C ANISOU 1286 CD1 LEU A 171 4269 4086 3874 385 -678 -941 C ATOM 1287 CD2 LEU A 171 3.921 7.032 14.774 1.00 39.11 C ANISOU 1287 CD2 LEU A 171 5125 4795 4938 391 -754 -1007 C ATOM 1288 N ALA A 172 3.679 4.870 19.476 1.00 20.46 N ANISOU 1288 N ALA A 172 2438 2906 2430 366 -600 -1073 N ATOM 1289 CA ALA A 172 3.108 3.754 20.206 1.00 19.44 C ANISOU 1289 CA ALA A 172 2264 2847 2276 379 -598 -1045 C ATOM 1290 C ALA A 172 1.724 4.124 20.733 1.00 20.36 C ANISOU 1290 C ALA A 172 2323 2930 2483 373 -610 -1103 C ATOM 1291 O ALA A 172 0.782 3.343 20.616 1.00 25.50 O ANISOU 1291 O ALA A 172 2980 3547 3164 399 -645 -1066 O ATOM 1292 CB ALA A 172 4.022 3.344 21.344 1.00 17.92 C ANISOU 1292 CB ALA A 172 2005 2817 1988 354 -539 -1050 C ATOM 1293 N GLN A 173 1.598 5.322 21.291 1.00 20.69 N ANISOU 1293 N GLN A 173 2310 2980 2572 339 -581 -1194 N ATOM 1294 CA GLN A 173 0.299 5.794 21.781 1.00 22.98 C ANISOU 1294 CA GLN A 173 2542 3235 2956 333 -589 -1260 C ATOM 1295 C GLN A 173 -0.718 5.913 20.641 1.00 28.92 C ANISOU 1295 C GLN A 173 3357 3823 3807 368 -659 -1237 C ATOM 1296 O GLN A 173 -1.852 5.450 20.759 1.00 26.79 O ANISOU 1296 O GLN A 173 3065 3524 3590 385 -686 -1230 O ATOM 1297 CB GLN A 173 0.452 7.120 22.530 1.00 29.28 C ANISOU 1297 CB GLN A 173 3274 4066 3785 292 -546 -1367 C ATOM 1298 CG GLN A 173 1.118 6.961 23.890 1.00 32.25 C ANISOU 1298 CG GLN A 173 3568 4610 4075 255 -477 -1400 C ATOM 1299 CD GLN A 173 1.521 8.278 24.515 1.00 37.64 C ANISOU 1299 CD GLN A 173 4202 5325 4775 213 -435 -1499 C ATOM 1300 OE1 GLN A 173 0.675 9.095 24.876 1.00 36.94 O ANISOU 1300 OE1 GLN A 173 4066 5199 4769 203 -432 -1581 O ATOM 1301 NE2 GLN A 173 2.825 8.490 24.648 1.00 42.84 N ANISOU 1301 NE2 GLN A 173 4870 6053 5356 189 -403 -1494 N ATOM 1302 N LYS A 174 -0.294 6.509 19.531 1.00 28.58 N ANISOU 1302 N LYS A 174 3395 3677 3788 375 -692 -1221 N ATOM 1303 CA LYS A 174 -1.152 6.675 18.368 1.00 26.90 C ANISOU 1303 CA LYS A 174 3252 3304 3664 403 -763 -1195 C ATOM 1304 C LYS A 174 -1.737 5.336 17.924 1.00 24.03 C ANISOU 1304 C LYS A 174 2929 2914 3288 442 -805 -1109 C ATOM 1305 O LYS A 174 -2.909 5.257 17.553 1.00 26.01 O ANISOU 1305 O LYS A 174 3188 3070 3624 462 -855 -1104 O ATOM 1306 CB LYS A 174 -0.374 7.330 17.219 1.00 24.77 C ANISOU 1306 CB LYS A 174 3073 2945 3392 401 -788 -1174 C ATOM 1307 CG LYS A 174 -1.181 7.569 15.947 1.00 26.14 C ANISOU 1307 CG LYS A 174 3329 2948 3655 425 -866 -1145 C ATOM 1308 CD LYS A 174 -0.247 7.833 14.765 1.00 31.96 C ANISOU 1308 CD LYS A 174 4168 3620 4355 424 -887 -1098 C ATOM 1309 CE LYS A 174 -0.985 7.880 13.435 1.00 35.77 C ANISOU 1309 CE LYS A 174 4744 3938 4909 448 -969 -1053 C ATOM 1310 NZ LYS A 174 -1.851 9.088 13.327 1.00 41.64 N ANISOU 1310 NZ LYS A 174 5457 4597 5766 430 -984 -1088 N ATOM 1311 N TYR A 175 -0.917 4.290 17.976 1.00 18.08 N ANISOU 1311 N TYR A 175 2198 2243 2430 452 -787 -1042 N ATOM 1312 CA TYR A 175 -1.316 2.964 17.516 1.00 26.24 C ANISOU 1312 CA TYR A 175 3277 3253 3440 489 -828 -955 C ATOM 1313 C TYR A 175 -1.699 2.018 18.659 1.00 30.99 C ANISOU 1313 C TYR A 175 3800 3971 4004 486 -801 -947 C ATOM 1314 O TYR A 175 -1.866 0.812 18.452 1.00 30.31 O ANISOU 1314 O TYR A 175 3744 3891 3881 513 -829 -872 O ATOM 1315 CB TYR A 175 -0.207 2.358 16.656 1.00 25.57 C ANISOU 1315 CB TYR A 175 3281 3165 3270 509 -836 -879 C ATOM 1316 CG TYR A 175 -0.008 3.094 15.346 1.00 25.84 C ANISOU 1316 CG TYR A 175 3407 3068 3342 515 -875 -869 C ATOM 1317 CD1 TYR A 175 -1.092 3.416 14.540 1.00 30.16 C ANISOU 1317 CD1 TYR A 175 4000 3472 3988 531 -940 -866 C ATOM 1318 CD2 TYR A 175 1.258 3.482 14.927 1.00 23.73 C ANISOU 1318 CD2 TYR A 175 3182 2821 3013 503 -848 -863 C ATOM 1319 CE1 TYR A 175 -0.919 4.094 13.342 1.00 34.22 C ANISOU 1319 CE1 TYR A 175 4601 3865 4535 532 -979 -855 C ATOM 1320 CE2 TYR A 175 1.443 4.158 13.736 1.00 24.24 C ANISOU 1320 CE2 TYR A 175 3333 2770 3109 503 -883 -852 C ATOM 1321 CZ TYR A 175 0.350 4.463 12.947 1.00 35.68 C ANISOU 1321 CZ TYR A 175 4829 4076 4653 517 -950 -847 C ATOM 1322 OH TYR A 175 0.526 5.136 11.759 1.00 40.18 O ANISOU 1322 OH TYR A 175 5486 4529 5251 513 -989 -834 O ATOM 1323 N GLN A 176 -1.846 2.577 19.856 1.00 27.14 N ANISOU 1323 N GLN A 176 3213 3573 3525 452 -750 -1025 N ATOM 1324 CA GLN A 176 -2.272 1.810 21.026 1.00 30.12 C ANISOU 1324 CA GLN A 176 3509 4065 3871 440 -721 -1027 C ATOM 1325 C GLN A 176 -1.428 0.564 21.255 1.00 32.51 C ANISOU 1325 C GLN A 176 3828 4466 4060 448 -709 -951 C ATOM 1326 O GLN A 176 -1.957 -0.505 21.568 1.00 37.32 O ANISOU 1326 O GLN A 176 4422 5109 4651 459 -725 -903 O ATOM 1327 CB GLN A 176 -3.753 1.428 20.923 1.00 38.57 C ANISOU 1327 CB GLN A 176 4565 5065 5024 458 -767 -1017 C ATOM 1328 CG GLN A 176 -4.708 2.516 21.385 1.00 45.36 C ANISOU 1328 CG GLN A 176 5355 5892 5986 439 -756 -1114 C ATOM 1329 CD GLN A 176 -6.164 2.125 21.211 1.00 47.55 C ANISOU 1329 CD GLN A 176 5619 6097 6351 460 -803 -1100 C ATOM 1330 OE1 GLN A 176 -6.496 0.942 21.102 1.00 46.89 O ANISOU 1330 OE1 GLN A 176 5555 6022 6238 479 -832 -1025 O ATOM 1331 NE2 GLN A 176 -7.041 3.121 21.175 1.00 47.30 N ANISOU 1331 NE2 GLN A 176 5553 5989 6430 456 -815 -1173 N ATOM 1332 N LYS A 177 -0.117 0.707 21.079 1.00 24.12 N ANISOU 1332 N LYS A 177 2795 3445 2924 442 -682 -939 N ATOM 1333 CA LYS A 177 0.827 -0.344 21.420 1.00 22.55 C ANISOU 1333 CA LYS A 177 2599 3351 2618 446 -662 -878 C ATOM 1334 C LYS A 177 1.202 -0.154 22.877 1.00 24.21 C ANISOU 1334 C LYS A 177 2709 3712 2778 401 -598 -932 C ATOM 1335 O LYS A 177 1.771 0.872 23.226 1.00 24.42 O ANISOU 1335 O LYS A 177 2704 3772 2802 370 -557 -998 O ATOM 1336 CB LYS A 177 2.086 -0.202 20.573 1.00 24.43 C ANISOU 1336 CB LYS A 177 2909 3568 2804 458 -659 -846 C ATOM 1337 CG LYS A 177 1.823 -0.140 19.081 1.00 26.24 C ANISOU 1337 CG LYS A 177 3243 3646 3083 495 -717 -805 C ATOM 1338 CD LYS A 177 1.417 -1.491 18.556 1.00 27.66 C ANISOU 1338 CD LYS A 177 3476 3790 3245 537 -767 -718 C ATOM 1339 CE LYS A 177 1.559 -1.539 17.043 1.00 26.98 C ANISOU 1339 CE LYS A 177 3503 3573 3174 572 -816 -668 C ATOM 1340 NZ LYS A 177 1.353 -2.916 16.531 1.00 31.53 N ANISOU 1340 NZ LYS A 177 4138 4124 3720 614 -862 -581 N ATOM 1341 N PRO A 178 0.880 -1.132 23.736 1.00 24.85 N ANISOU 1341 N PRO A 178 2741 3884 2818 394 -591 -904 N ATOM 1342 CA PRO A 178 1.189 -0.968 25.161 1.00 26.39 C ANISOU 1342 CA PRO A 178 2840 4225 2961 346 -531 -955 C ATOM 1343 C PRO A 178 2.636 -0.526 25.394 1.00 24.41 C ANISOU 1343 C PRO A 178 2587 4051 2639 325 -487 -972 C ATOM 1344 O PRO A 178 3.575 -1.037 24.775 1.00 22.61 O ANISOU 1344 O PRO A 178 2415 3819 2355 348 -499 -910 O ATOM 1345 CB PRO A 178 0.926 -2.360 25.735 1.00 26.33 C ANISOU 1345 CB PRO A 178 2813 4294 2899 350 -544 -889 C ATOM 1346 CG PRO A 178 -0.140 -2.920 24.832 1.00 26.13 C ANISOU 1346 CG PRO A 178 2842 4148 2940 392 -608 -838 C ATOM 1347 CD PRO A 178 0.236 -2.427 23.456 1.00 25.35 C ANISOU 1347 CD PRO A 178 2834 3921 2876 426 -640 -823 C ATOM 1348 N LEU A 179 2.802 0.427 26.303 1.00 25.74 N ANISOU 1348 N LEU A 179 2683 4289 2806 279 -436 -1057 N ATOM 1349 CA LEU A 179 4.070 1.110 26.493 1.00 23.11 C ANISOU 1349 CA LEU A 179 2344 4013 2423 254 -396 -1088 C ATOM 1350 C LEU A 179 4.541 0.960 27.941 1.00 23.25 C ANISOU 1350 C LEU A 179 2277 4193 2365 206 -343 -1117 C ATOM 1351 O LEU A 179 3.813 1.305 28.879 1.00 21.91 O ANISOU 1351 O LEU A 179 2035 4071 2217 174 -317 -1180 O ATOM 1352 CB LEU A 179 3.877 2.582 26.128 1.00 26.46 C ANISOU 1352 CB LEU A 179 2772 4355 2925 241 -388 -1169 C ATOM 1353 CG LEU A 179 5.053 3.543 25.991 1.00 30.92 C ANISOU 1353 CG LEU A 179 3347 4935 3465 218 -358 -1205 C ATOM 1354 CD1 LEU A 179 6.060 3.051 24.953 1.00 23.26 C ANISOU 1354 CD1 LEU A 179 2459 3932 2448 248 -379 -1125 C ATOM 1355 CD2 LEU A 179 4.509 4.912 25.602 1.00 33.56 C ANISOU 1355 CD2 LEU A 179 3687 5167 3897 209 -365 -1283 C ATOM 1356 N PHE A 180 5.743 0.417 28.115 1.00 20.73 N ANISOU 1356 N PHE A 180 1964 3956 1956 202 -329 -1070 N ATOM 1357 CA PHE A 180 6.327 0.180 29.436 1.00 24.83 C ANISOU 1357 CA PHE A 180 2411 4630 2395 157 -285 -1086 C ATOM 1358 C PHE A 180 7.704 0.821 29.552 1.00 25.62 C ANISOU 1358 C PHE A 180 2506 4782 2446 133 -249 -1105 C ATOM 1359 O PHE A 180 8.470 0.865 28.579 1.00 26.21 O ANISOU 1359 O PHE A 180 2643 4803 2512 161 -266 -1069 O ATOM 1360 CB PHE A 180 6.449 -1.318 29.708 1.00 26.33 C ANISOU 1360 CB PHE A 180 2602 4884 2516 172 -307 -996 C ATOM 1361 CG PHE A 180 5.139 -2.040 29.721 1.00 31.63 C ANISOU 1361 CG PHE A 180 3271 5517 3228 189 -341 -970 C ATOM 1362 CD1 PHE A 180 4.565 -2.490 28.542 1.00 32.11 C ANISOU 1362 CD1 PHE A 180 3405 5452 3342 242 -395 -916 C ATOM 1363 CD2 PHE A 180 4.477 -2.272 30.915 1.00 30.21 C ANISOU 1363 CD2 PHE A 180 3017 5430 3032 149 -319 -997 C ATOM 1364 CE1 PHE A 180 3.357 -3.157 28.560 1.00 32.11 C ANISOU 1364 CE1 PHE A 180 3403 5418 3381 256 -428 -889 C ATOM 1365 CE2 PHE A 180 3.272 -2.939 30.935 1.00 30.97 C ANISOU 1365 CE2 PHE A 180 3107 5494 3165 162 -349 -971 C ATOM 1366 CZ PHE A 180 2.711 -3.382 29.758 1.00 31.14 C ANISOU 1366 CZ PHE A 180 3200 5388 3242 216 -405 -916 C ATOM 1367 N VAL A 181 8.023 1.303 30.747 1.00 27.27 N ANISOU 1367 N VAL A 181 2645 5080 2638 81 -193 -1144 N ATOM 1368 CA VAL A 181 9.297 1.953 30.994 1.00 25.37 C ANISOU 1368 CA VAL A 181 2392 4876 2372 52 -153 -1149 C ATOM 1369 C VAL A 181 9.892 1.427 32.299 1.00 26.02 C ANISOU 1369 C VAL A 181 2409 5077 2399 13 -113 -1115 C ATOM 1370 O VAL A 181 9.166 0.925 33.162 1.00 26.04 O ANISOU 1370 O VAL A 181 2367 5136 2392 -5 -105 -1118 O ATOM 1371 CB VAL A 181 9.121 3.481 31.095 1.00 24.46 C ANISOU 1371 CB VAL A 181 2254 4727 2311 22 -128 -1250 C ATOM 1372 CG1 VAL A 181 8.408 4.020 29.858 1.00 25.04 C ANISOU 1372 CG1 VAL A 181 2388 4672 2453 58 -173 -1287 C ATOM 1373 CG2 VAL A 181 8.336 3.832 32.346 1.00 29.71 C ANISOU 1373 CG2 VAL A 181 2839 5455 2993 -20 -93 -1315 C ATOM 1374 N LEU A 182 11.210 1.524 32.438 1.00 24.60 N ANISOU 1374 N LEU A 182 2226 4935 2185 -2 -92 -1082 N ATOM 1375 CA LEU A 182 11.862 1.196 33.700 1.00 29.59 C ANISOU 1375 CA LEU A 182 2794 5673 2774 -46 -57 -1059 C ATOM 1376 C LEU A 182 11.634 2.322 34.683 1.00 31.34 C ANISOU 1376 C LEU A 182 2951 5939 3017 -102 -18 -1146 C ATOM 1377 O LEU A 182 11.636 3.489 34.295 1.00 31.00 O ANISOU 1377 O LEU A 182 2918 5847 3014 -109 -10 -1211 O ATOM 1378 CB LEU A 182 13.370 1.020 33.524 1.00 29.40 C ANISOU 1378 CB LEU A 182 2783 5670 2715 -45 -51 -1003 C ATOM 1379 CG LEU A 182 13.939 -0.258 32.912 1.00 32.47 C ANISOU 1379 CG LEU A 182 3218 6045 3074 0 -80 -905 C ATOM 1380 CD1 LEU A 182 15.452 -0.225 33.030 1.00 30.74 C ANISOU 1380 CD1 LEU A 182 2988 5866 2827 -13 -63 -870 C ATOM 1381 CD2 LEU A 182 13.377 -1.489 33.601 1.00 29.03 C ANISOU 1381 CD2 LEU A 182 2761 5652 2616 3 -89 -854 C ATOM 1382 N PRO A 183 11.439 1.978 35.966 1.00 38.65 N ANISOU 1382 N PRO A 183 3662 7099 3926 641 -238 -2003 N ATOM 1383 CA PRO A 183 11.395 3.016 36.995 1.00 36.03 C ANISOU 1383 CA PRO A 183 3348 6751 3590 644 -238 -2009 C ATOM 1384 C PRO A 183 12.738 3.728 37.037 1.00 30.44 C ANISOU 1384 C PRO A 183 2672 6021 2872 622 -222 -2007 C ATOM 1385 O PRO A 183 13.775 3.070 36.985 1.00 30.67 O ANISOU 1385 O PRO A 183 2686 6056 2909 600 -213 -2003 O ATOM 1386 CB PRO A 183 11.179 2.222 38.288 1.00 35.47 C ANISOU 1386 CB PRO A 183 3230 6703 3545 642 -244 -2013 C ATOM 1387 CG PRO A 183 10.576 0.924 37.851 1.00 34.95 C ANISOU 1387 CG PRO A 183 3124 6664 3493 648 -253 -2010 C ATOM 1388 CD PRO A 183 11.189 0.633 36.511 1.00 37.35 C ANISOU 1388 CD PRO A 183 3443 6963 3786 638 -245 -2002 C ATOM 1389 N GLN A 184 12.710 5.053 37.130 1.00 31.25 N ANISOU 1389 N GLN A 184 2817 6098 2957 628 -219 -2011 N ATOM 1390 CA GLN A 184 13.915 5.865 37.055 1.00 30.43 C ANISOU 1390 CA GLN A 184 2750 5971 2842 609 -204 -2010 C ATOM 1391 C GLN A 184 13.889 6.971 38.105 1.00 31.80 C ANISOU 1391 C GLN A 184 2943 6128 3012 612 -203 -2018 C ATOM 1392 O GLN A 184 12.824 7.449 38.491 1.00 32.18 O ANISOU 1392 O GLN A 184 2994 6175 3058 633 -214 -2024 O ATOM 1393 CB GLN A 184 14.031 6.492 35.665 1.00 30.99 C ANISOU 1393 CB GLN A 184 2865 6023 2888 612 -199 -2006 C ATOM 1394 CG GLN A 184 14.244 5.501 34.542 1.00 33.58 C ANISOU 1394 CG GLN A 184 3179 6365 3217 606 -197 -1998 C ATOM 1395 CD GLN A 184 15.682 5.044 34.445 1.00 36.24 C ANISOU 1395 CD GLN A 184 3511 6702 3558 577 -184 -1992 C ATOM 1396 OE1 GLN A 184 16.509 5.349 35.309 1.00 35.13 O ANISOU 1396 OE1 GLN A 184 3373 6554 3423 561 -176 -1995 O ATOM 1397 NE2 GLN A 184 15.991 4.313 33.388 1.00 29.39 N ANISOU 1397 NE2 GLN A 184 2637 5842 2688 571 -181 -1986 N ATOM 1398 N ARG A 185 15.065 7.385 38.560 1.00 34.69 N ANISOU 1398 N ARG A 185 3323 6481 3376 591 -191 -2019 N ATOM 1399 CA ARG A 185 15.145 8.453 39.543 1.00 36.68 C ANISOU 1399 CA ARG A 185 3595 6716 3625 592 -189 -2027 C ATOM 1400 C ARG A 185 14.733 9.790 38.955 1.00 40.00 C ANISOU 1400 C ARG A 185 4067 7109 4021 606 -189 -2030 C ATOM 1401 O ARG A 185 14.691 9.963 37.735 1.00 41.34 O ANISOU 1401 O ARG A 185 4264 7270 4175 609 -186 -2025 O ATOM 1402 CB ARG A 185 16.557 8.564 40.109 1.00 37.96 C ANISOU 1402 CB ARG A 185 3761 6871 3792 565 -176 -2027 C ATOM 1403 CG ARG A 185 16.981 7.373 40.919 1.00 36.90 C ANISOU 1403 CG ARG A 185 3576 6763 3682 551 -176 -2026 C ATOM 1404 CD ARG A 185 18.305 7.644 41.593 1.00 35.78 C ANISOU 1404 CD ARG A 185 3439 6611 3543 526 -164 -2027 C ATOM 1405 NE ARG A 185 18.690 6.546 42.466 1.00 36.76 N ANISOU 1405 NE ARG A 185 3515 6760 3691 513 -164 -2027 N ATOM 1406 CZ ARG A 185 19.936 6.320 42.861 1.00 42.99 C ANISOU 1406 CZ ARG A 185 4297 7550 4488 488 -153 -2025 C ATOM 1407 NH1 ARG A 185 20.913 7.114 42.447 1.00 43.06 N ANISOU 1407 NH1 ARG A 185 4345 7535 4482 474 -141 -2024 N ATOM 1408 NH2 ARG A 185 20.205 5.297 43.658 1.00 47.07 N ANISOU 1408 NH2 ARG A 185 4768 8090 5026 478 -155 -2025 N ATOM 1409 N LEU A 186 14.439 10.732 39.842 1.00 38.94 N ANISOU 1409 N LEU A 186 3948 6963 3885 614 -191 -2039 N ATOM 1410 CA LEU A 186 14.093 12.092 39.463 1.00 43.36 C ANISOU 1410 CA LEU A 186 4557 7495 4423 626 -190 -2043 C ATOM 1411 C LEU A 186 15.225 12.735 38.667 1.00 49.49 C ANISOU 1411 C LEU A 186 5376 8247 5180 608 -175 -2038 C ATOM 1412 O LEU A 186 16.398 12.422 38.876 1.00 48.34 O ANISOU 1412 O LEU A 186 5224 8102 5041 585 -164 -2036 O ATOM 1413 CB LEU A 186 13.827 12.917 40.719 1.00 42.51 C ANISOU 1413 CB LEU A 186 4454 7379 4318 633 -193 -2054 C ATOM 1414 CG LEU A 186 12.762 14.001 40.609 1.00 44.29 C ANISOU 1414 CG LEU A 186 4710 7588 4529 657 -200 -2060 C ATOM 1415 CD1 LEU A 186 11.446 13.369 40.193 1.00 40.51 C ANISOU 1415 CD1 LEU A 186 4209 7129 4055 680 -215 -2058 C ATOM 1416 CD2 LEU A 186 12.619 14.745 41.929 1.00 47.60 C ANISOU 1416 CD2 LEU A 186 5131 8001 4954 661 -203 -2071 C ATOM 1417 N ASN A 187 14.864 13.634 37.756 1.00 51.99 N ANISOU 1417 N ASN A 187 5736 8543 5475 620 -174 -2038 N ATOM 1418 CA ASN A 187 15.841 14.385 36.967 1.00 53.67 C ANISOU 1418 CA ASN A 187 5994 8730 5667 605 -161 -2034 C ATOM 1419 C ASN A 187 16.793 13.522 36.143 1.00 52.72 C ANISOU 1419 C ASN A 187 5866 8618 5548 585 -152 -2024 C ATOM 1420 O ASN A 187 17.753 14.027 35.562 1.00 57.12 O ANISOU 1420 O ASN A 187 6456 9156 6091 570 -140 -2021 O ATOM 1421 CB ASN A 187 16.621 15.369 37.846 1.00 56.34 C ANISOU 1421 CB ASN A 187 6356 9048 6003 592 -152 -2041 C ATOM 1422 CG ASN A 187 15.770 16.539 38.300 1.00 60.23 C ANISOU 1422 CG ASN A 187 6874 9523 6486 612 -158 -2051 C ATOM 1423 OD1 ASN A 187 14.795 16.902 37.640 1.00 60.63 O ANISOU 1423 OD1 ASN A 187 6943 9569 6525 633 -166 -2051 O ATOM 1424 ND2 ASN A 187 16.133 17.137 39.432 1.00 61.30 N ANISOU 1424 ND2 ASN A 187 7012 9650 6627 606 -155 -2060 N ATOM 1425 N GLU A 188 16.529 12.221 36.102 1.00 49.61 N ANISOU 1425 N GLU A 188 5426 8253 5172 586 -158 -2020 N ATOM 1426 CA GLU A 188 17.199 11.338 35.157 1.00 49.60 C ANISOU 1426 CA GLU A 188 5415 8261 5170 571 -152 -2010 C ATOM 1427 C GLU A 188 16.122 10.643 34.327 1.00 47.59 C ANISOU 1427 C GLU A 188 5144 8024 4916 591 -164 -2006 C ATOM 1428 O GLU A 188 14.988 10.481 34.785 1.00 48.78 O ANISOU 1428 O GLU A 188 5273 8186 5075 611 -176 -2011 O ATOM 1429 CB GLU A 188 18.091 10.317 35.871 1.00 52.09 C ANISOU 1429 CB GLU A 188 5689 8595 5508 550 -147 -2008 C ATOM 1430 CG GLU A 188 17.438 8.960 36.123 1.00 53.84 C ANISOU 1430 CG GLU A 188 5857 8849 5752 556 -158 -2007 C ATOM 1431 CD GLU A 188 18.296 8.042 36.982 1.00 52.25 C ANISOU 1431 CD GLU A 188 5616 8665 5572 535 -154 -2006 C ATOM 1432 OE1 GLU A 188 17.844 6.913 37.292 1.00 48.29 O ANISOU 1432 OE1 GLU A 188 5068 8190 5090 538 -162 -2005 O ATOM 1433 OE2 GLU A 188 19.418 8.454 37.353 1.00 49.76 O ANISOU 1433 OE2 GLU A 188 5315 8337 5255 515 -142 -2007 O ATOM 1434 N SER A 189 16.473 10.251 33.107 1.00 43.37 N ANISOU 1434 N SER A 189 4618 7490 4371 585 -159 -1998 N ATOM 1435 CA SER A 189 15.511 9.650 32.188 1.00 41.24 C ANISOU 1435 CA SER A 189 4336 7235 4099 603 -169 -1995 C ATOM 1436 C SER A 189 14.225 10.473 32.148 1.00 38.85 C ANISOU 1436 C SER A 189 4053 6923 3785 631 -180 -2000 C ATOM 1437 O SER A 189 13.138 9.963 32.435 1.00 36.73 O ANISOU 1437 O SER A 189 3755 6673 3529 649 -193 -2003 O ATOM 1438 CB SER A 189 15.207 8.207 32.593 1.00 39.53 C ANISOU 1438 CB SER A 189 4062 7051 3908 603 -177 -1994 C ATOM 1439 OG SER A 189 14.662 7.483 31.500 1.00 40.16 O ANISOU 1439 OG SER A 189 4130 7144 3984 613 -183 -1988 O ATOM 1440 N ASP A 190 14.360 11.747 31.792 1.00 38.82 N ANISOU 1440 N ASP A 190 4099 6891 3758 634 -174 -2002 N ATOM 1441 CA ASP A 190 13.244 12.688 31.831 1.00 42.06 C ANISOU 1441 CA ASP A 190 4533 7289 4157 658 -183 -2008 C ATOM 1442 C ASP A 190 12.077 12.268 30.941 1.00 40.35 C ANISOU 1442 C ASP A 190 4309 7087 3937 681 -195 -2005 C ATOM 1443 O ASP A 190 10.911 12.421 31.316 1.00 38.97 O ANISOU 1443 O ASP A 190 4124 6917 3765 704 -207 -2010 O ATOM 1444 CB ASP A 190 13.719 14.097 31.462 1.00 43.81 C ANISOU 1444 CB ASP A 190 4813 7478 4355 655 -173 -2009 C ATOM 1445 CG ASP A 190 14.421 14.799 32.616 1.00 47.18 C ANISOU 1445 CG ASP A 190 5250 7890 4786 641 -166 -2016 C ATOM 1446 OD1 ASP A 190 14.782 14.123 33.603 1.00 50.10 O ANISOU 1446 OD1 ASP A 190 5583 8275 5178 630 -166 -2018 O ATOM 1447 OD2 ASP A 190 14.612 16.030 32.537 1.00 47.61 O ANISOU 1447 OD2 ASP A 190 5349 7916 4822 642 -160 -2019 O ATOM 1448 N GLY A 191 12.393 11.734 29.766 1.00 37.17 N ANISOU 1448 N GLY A 191 3908 6688 3525 676 -191 -1997 N ATOM 1449 CA GLY A 191 11.376 11.332 28.815 1.00 34.60 C ANISOU 1449 CA GLY A 191 3576 6375 3194 696 -201 -1994 C ATOM 1450 C GLY A 191 10.468 10.250 29.357 1.00 31.53 C ANISOU 1450 C GLY A 191 3135 6017 2829 709 -215 -1997 C ATOM 1451 O GLY A 191 9.245 10.374 29.296 1.00 33.36 O ANISOU 1451 O GLY A 191 3362 6254 3060 733 -227 -2000 O ATOM 1452 N THR A 192 11.061 9.192 29.902 1.00 30.49 N ANISOU 1452 N THR A 192 2963 5904 2719 692 -212 -1995 N ATOM 1453 CA THR A 192 10.277 8.067 30.402 1.00 32.55 C ANISOU 1453 CA THR A 192 3171 6194 3002 702 -224 -1997 C ATOM 1454 C THR A 192 9.499 8.424 31.666 1.00 32.80 C ANISOU 1454 C THR A 192 3189 6227 3045 715 -234 -2005 C ATOM 1455 O THR A 192 8.398 7.924 31.875 1.00 32.68 O ANISOU 1455 O THR A 192 3146 6230 3040 734 -247 -2008 O ATOM 1456 CB THR A 192 11.137 6.813 30.650 1.00 32.68 C ANISOU 1456 CB THR A 192 3148 6231 3039 680 -219 -1993 C ATOM 1457 OG1 THR A 192 12.068 7.061 31.710 1.00 32.84 O ANISOU 1457 OG1 THR A 192 3167 6243 3069 660 -211 -1995 O ATOM 1458 CG2 THR A 192 11.888 6.427 29.378 1.00 31.65 C ANISOU 1458 CG2 THR A 192 3029 6099 2898 667 -211 -1985 C ATOM 1459 N ASN A 193 10.066 9.285 32.507 1.00 34.66 N ANISOU 1459 N ASN A 193 3446 6445 3279 706 -227 -2009 N ATOM 1460 CA ASN A 193 9.344 9.736 33.694 1.00 35.32 C ANISOU 1460 CA ASN A 193 3521 6529 3371 719 -235 -2018 C ATOM 1461 C ASN A 193 8.126 10.594 33.349 1.00 34.74 C ANISOU 1461 C ASN A 193 3473 6445 3283 747 -245 -2022 C ATOM 1462 O ASN A 193 7.103 10.534 34.030 1.00 37.76 O ANISOU 1462 O ASN A 193 3834 6838 3675 765 -257 -2028 O ATOM 1463 CB ASN A 193 10.274 10.447 34.680 1.00 36.88 C ANISOU 1463 CB ASN A 193 3734 6710 3571 702 -225 -2022 C ATOM 1464 CG ASN A 193 11.034 9.473 35.561 1.00 37.49 C ANISOU 1464 CG ASN A 193 3769 6805 3671 681 -221 -2021 C ATOM 1465 OD1 ASN A 193 10.655 8.309 35.685 1.00 38.09 O ANISOU 1465 OD1 ASN A 193 3802 6907 3764 684 -229 -2020 O ATOM 1466 ND2 ASN A 193 12.109 9.945 36.183 1.00 39.86 N ANISOU 1466 ND2 ASN A 193 4083 7092 3971 661 -210 -2023 N ATOM 1467 N GLU A 194 8.233 11.386 32.288 1.00 34.27 N ANISOU 1467 N GLU A 194 3457 6365 3199 750 -240 -2019 N ATOM 1468 CA GLU A 194 7.089 12.149 31.807 1.00 35.44 C ANISOU 1468 CA GLU A 194 3630 6503 3332 776 -249 -2022 C ATOM 1469 C GLU A 194 5.982 11.222 31.324 1.00 37.35 C ANISOU 1469 C GLU A 194 3839 6770 3582 795 -262 -2021 C ATOM 1470 O GLU A 194 4.799 11.512 31.494 1.00 38.10 O ANISOU 1470 O GLU A 194 3931 6869 3676 819 -275 -2026 O ATOM 1471 CB GLU A 194 7.479 13.089 30.668 1.00 36.40 C ANISOU 1471 CB GLU A 194 3805 6600 3426 774 -240 -2018 C ATOM 1472 CG GLU A 194 6.264 13.625 29.927 1.00 41.92 C ANISOU 1472 CG GLU A 194 4524 7294 4110 802 -250 -2020 C ATOM 1473 CD GLU A 194 6.621 14.456 28.715 1.00 51.13 C ANISOU 1473 CD GLU A 194 5741 8438 5248 801 -242 -2015 C ATOM 1474 OE1 GLU A 194 7.208 15.543 28.893 1.00 53.60 O ANISOU 1474 OE1 GLU A 194 6093 8725 5548 792 -233 -2018 O ATOM 1475 OE2 GLU A 194 6.307 14.023 27.582 1.00 55.15 O ANISOU 1475 OE2 GLU A 194 6250 8956 5749 808 -245 -2010 O ATOM 1476 N LEU A 195 6.367 10.118 30.694 1.00 30.77 N ANISOU 1476 N LEU A 195 2981 5955 2756 785 -260 -2014 N ATOM 1477 CA LEU A 195 5.386 9.135 30.257 1.00 30.70 C ANISOU 1477 CA LEU A 195 2937 5971 2756 802 -273 -2013 C ATOM 1478 C LEU A 195 4.642 8.581 31.474 1.00 35.32 C ANISOU 1478 C LEU A 195 3479 6576 3364 811 -284 -2019 C ATOM 1479 O LEU A 195 3.417 8.461 31.464 1.00 32.49 O ANISOU 1479 O LEU A 195 3106 6228 3008 835 -298 -2022 O ATOM 1480 CB LEU A 195 6.061 8.009 29.472 1.00 30.55 C ANISOU 1480 CB LEU A 195 2898 5968 2743 786 -268 -2005 C ATOM 1481 CG LEU A 195 6.693 8.398 28.132 1.00 35.12 C ANISOU 1481 CG LEU A 195 3515 6532 3298 779 -258 -1999 C ATOM 1482 CD1 LEU A 195 7.416 7.210 27.519 1.00 37.12 C ANISOU 1482 CD1 LEU A 195 3742 6802 3560 762 -253 -1992 C ATOM 1483 CD2 LEU A 195 5.640 8.938 27.159 1.00 36.75 C ANISOU 1483 CD2 LEU A 195 3745 6732 3485 804 -266 -1999 C ATOM 1484 N LEU A 196 5.391 8.260 32.527 1.00 33.80 N ANISOU 1484 N LEU A 196 3266 6388 3188 792 -279 -2020 N ATOM 1485 CA LEU A 196 4.797 7.771 33.767 1.00 36.03 C ANISOU 1485 CA LEU A 196 3509 6689 3493 799 -288 -2026 C ATOM 1486 C LEU A 196 3.890 8.816 34.398 1.00 36.84 C ANISOU 1486 C LEU A 196 3629 6780 3590 819 -296 -2034 C ATOM 1487 O LEU A 196 2.772 8.511 34.809 1.00 41.21 O ANISOU 1487 O LEU A 196 4157 7349 4153 839 -310 -2038 O ATOM 1488 CB LEU A 196 5.881 7.375 34.771 1.00 36.52 C ANISOU 1488 CB LEU A 196 3550 6755 3571 774 -280 -2026 C ATOM 1489 CG LEU A 196 6.633 6.073 34.508 1.00 36.53 C ANISOU 1489 CG LEU A 196 3518 6776 3587 754 -275 -2020 C ATOM 1490 CD1 LEU A 196 7.743 5.887 35.538 1.00 35.64 C ANISOU 1490 CD1 LEU A 196 3391 6663 3487 730 -265 -2020 C ATOM 1491 CD2 LEU A 196 5.666 4.898 34.528 1.00 36.36 C ANISOU 1491 CD2 LEU A 196 3449 6784 3583 768 -288 -2020 C ATOM 1492 N GLU A 197 4.384 10.046 34.484 1.00 36.84 N ANISOU 1492 N GLU A 197 3672 6751 3573 815 -288 -2036 N ATOM 1493 CA GLU A 197 3.630 11.130 35.101 1.00 35.82 C ANISOU 1493 CA GLU A 197 3564 6609 3437 832 -294 -2045 C ATOM 1494 C GLU A 197 2.284 11.326 34.408 1.00 37.39 C ANISOU 1494 C GLU A 197 3769 6810 3626 861 -307 -2046 C ATOM 1495 O GLU A 197 1.272 11.579 35.056 1.00 39.82 O ANISOU 1495 O GLU A 197 4067 7123 3940 880 -318 -2053 O ATOM 1496 CB GLU A 197 4.429 12.438 35.071 1.00 39.17 C ANISOU 1496 CB GLU A 197 4039 7001 3843 822 -282 -2046 C ATOM 1497 CG GLU A 197 3.764 13.574 35.849 1.00 41.09 C ANISOU 1497 CG GLU A 197 4302 7229 4081 838 -287 -2056 C ATOM 1498 CD GLU A 197 4.621 14.825 35.930 1.00 47.66 C ANISOU 1498 CD GLU A 197 5182 8030 4896 825 -275 -2058 C ATOM 1499 OE1 GLU A 197 5.573 14.952 35.134 1.00 49.76 O ANISOU 1499 OE1 GLU A 197 5473 8284 5151 809 -263 -2052 O ATOM 1500 OE2 GLU A 197 4.342 15.683 36.795 1.00 51.35 O ANISOU 1500 OE2 GLU A 197 5661 8486 5363 832 -277 -2067 O ATOM 1501 N LYS A 198 2.273 11.193 33.089 1.00 33.68 N ANISOU 1501 N LYS A 198 2845 6688 3265 321 36 -1346 N ATOM 1502 CA LYS A 198 1.060 11.448 32.321 1.00 31.23 C ANISOU 1502 CA LYS A 198 2527 6281 3057 308 33 -1432 C ATOM 1503 C LYS A 198 0.226 10.190 32.100 1.00 34.21 C ANISOU 1503 C LYS A 198 2919 6632 3447 250 152 -1345 C ATOM 1504 O LYS A 198 -0.775 10.216 31.387 1.00 39.83 O ANISOU 1504 O LYS A 198 3627 7254 4251 237 161 -1393 O ATOM 1505 CB LYS A 198 1.406 12.122 30.993 1.00 33.20 C ANISOU 1505 CB LYS A 198 2831 6359 3424 343 -80 -1468 C ATOM 1506 CG LYS A 198 2.042 13.495 31.168 1.00 36.91 C ANISOU 1506 CG LYS A 198 3298 6806 3921 401 -181 -1542 C ATOM 1507 CD LYS A 198 2.461 14.096 29.837 1.00 41.80 C ANISOU 1507 CD LYS A 198 4047 7156 4681 425 -224 -1492 C ATOM 1508 CE LYS A 198 3.028 15.493 30.024 1.00 48.80 C ANISOU 1508 CE LYS A 198 4961 7956 5624 477 -280 -1511 C ATOM 1509 NZ LYS A 198 3.536 16.060 28.744 1.00 50.10 N ANISOU 1509 NZ LYS A 198 5259 7875 5903 482 -317 -1443 N ATOM 1510 N GLY A 199 0.637 9.093 32.726 1.00 37.86 N ANISOU 1510 N GLY A 199 3397 7171 3819 212 240 -1212 N ATOM 1511 CA GLY A 199 -0.092 7.841 32.627 1.00 40.62 C ANISOU 1511 CA GLY A 199 3756 7501 4176 152 353 -1116 C ATOM 1512 C GLY A 199 -0.086 7.270 31.222 1.00 38.52 C ANISOU 1512 C GLY A 199 3543 7053 4039 151 343 -1041 C ATOM 1513 O GLY A 199 -1.006 6.557 30.830 1.00 41.35 O ANISOU 1513 O GLY A 199 3899 7357 4455 115 413 -1008 O ATOM 1514 N GLN A 200 0.961 7.579 30.464 1.00 36.99 N ANISOU 1514 N GLN A 200 3400 6764 3890 192 260 -1012 N ATOM 1515 CA GLN A 200 1.069 7.126 29.080 1.00 34.81 C ANISOU 1515 CA GLN A 200 3184 6304 3740 192 246 -944 C ATOM 1516 C GLN A 200 1.883 5.845 28.951 1.00 34.54 C ANISOU 1516 C GLN A 200 3188 6243 3693 167 299 -766 C ATOM 1517 O GLN A 200 1.932 5.232 27.886 1.00 34.19 O ANISOU 1517 O GLN A 200 3188 6052 3753 158 308 -689 O ATOM 1518 CB GLN A 200 1.673 8.225 28.215 1.00 35.04 C ANISOU 1518 CB GLN A 200 3258 6221 3836 242 126 -1019 C ATOM 1519 CG GLN A 200 0.853 9.498 28.217 1.00 39.28 C ANISOU 1519 CG GLN A 200 3762 6762 4399 263 60 -1191 C ATOM 1520 CD GLN A 200 1.574 10.645 27.552 1.00 41.38 C ANISOU 1520 CD GLN A 200 4083 6935 4706 306 -63 -1264 C ATOM 1521 OE1 GLN A 200 2.798 10.734 27.601 1.00 42.33 O ANISOU 1521 OE1 GLN A 200 4243 7055 4787 330 -101 -1217 O ATOM 1522 NE2 GLN A 200 0.818 11.529 26.918 1.00 45.64 N ANISOU 1522 NE2 GLN A 200 4629 7392 5321 312 -125 -1380 N ATOM 1523 N ALA A 201 2.521 5.447 30.044 1.00 34.49 N ANISOU 1523 N ALA A 201 3166 6378 3560 153 331 -699 N ATOM 1524 CA ALA A 201 3.238 4.183 30.096 1.00 30.18 C ANISOU 1524 CA ALA A 201 2653 5827 2988 120 381 -525 C ATOM 1525 C ALA A 201 3.108 3.570 31.480 1.00 32.55 C ANISOU 1525 C ALA A 201 2930 6293 3144 70 457 -465 C ATOM 1526 O ALA A 201 2.905 4.280 32.467 1.00 34.19 O ANISOU 1526 O ALA A 201 3100 6633 3256 77 451 -556 O ATOM 1527 CB ALA A 201 4.697 4.387 29.748 1.00 31.81 C ANISOU 1527 CB ALA A 201 2894 5998 3193 163 306 -470 C ATOM 1528 N GLN A 202 3.215 2.248 31.547 1.00 32.34 N ANISOU 1528 N GLN A 202 2933 6248 3107 17 524 -311 N ATOM 1529 CA GLN A 202 3.253 1.546 32.818 1.00 32.28 C ANISOU 1529 CA GLN A 202 2928 6376 2960 -39 587 -225 C ATOM 1530 C GLN A 202 4.698 1.241 33.186 1.00 28.33 C ANISOU 1530 C GLN A 202 2465 5914 2385 -29 543 -102 C ATOM 1531 O GLN A 202 5.550 1.040 32.312 1.00 27.63 O ANISOU 1531 O GLN A 202 2402 5722 2374 2 495 -33 O ATOM 1532 CB GLN A 202 2.461 0.242 32.741 1.00 35.10 C ANISOU 1532 CB GLN A 202 3303 6684 3347 -110 681 -125 C ATOM 1533 CG GLN A 202 1.024 0.398 32.275 1.00 44.86 C ANISOU 1533 CG GLN A 202 4504 7869 4673 -120 728 -228 C ATOM 1534 CD GLN A 202 0.282 -0.923 32.268 1.00 53.85 C ANISOU 1534 CD GLN A 202 5659 8967 5836 -190 821 -125 C ATOM 1535 OE1 GLN A 202 0.601 -1.829 33.041 1.00 58.69 O ANISOU 1535 OE1 GLN A 202 6304 9638 6358 -244 864 -4 O ATOM 1536 NE2 GLN A 202 -0.704 -1.047 31.387 1.00 54.52 N ANISOU 1536 NE2 GLN A 202 5726 8943 6046 -189 848 -170 N ATOM 1537 N GLY A 203 4.980 1.207 34.482 1.00 28.66 N ANISOU 1537 N GLY A 203 2511 6099 2278 -57 558 -72 N ATOM 1538 CA GLY A 203 6.310 0.863 34.938 1.00 32.82 C ANISOU 1538 CA GLY A 203 3079 6662 2729 -53 514 56 C ATOM 1539 C GLY A 203 6.484 -0.636 35.075 1.00 31.12 C ANISOU 1539 C GLY A 203 2919 6401 2506 -120 560 244 C ATOM 1540 O GLY A 203 5.528 -1.358 35.365 1.00 36.82 O ANISOU 1540 O GLY A 203 3647 7126 3217 -184 640 268 O ATOM 1541 N ILE A 204 7.706 -1.105 34.852 1.00 25.62 N ANISOU 1541 N ILE A 204 2261 5653 1822 -105 506 376 N ATOM 1542 CA ILE A 204 8.054 -2.496 35.099 1.00 26.57 C ANISOU 1542 CA ILE A 204 2440 5723 1933 -164 527 560 C ATOM 1543 C ILE A 204 8.668 -2.628 36.493 1.00 35.08 C ANISOU 1543 C ILE A 204 3560 6914 2855 -196 508 630 C ATOM 1544 O ILE A 204 9.860 -2.383 36.679 1.00 38.19 O ANISOU 1544 O ILE A 204 3977 7312 3221 -159 430 682 O ATOM 1545 CB ILE A 204 9.061 -3.016 34.058 1.00 27.69 C ANISOU 1545 CB ILE A 204 2604 5722 2193 -131 472 671 C ATOM 1546 CG1 ILE A 204 8.418 -3.039 32.669 1.00 30.36 C ANISOU 1546 CG1 ILE A 204 2917 5928 2690 -111 495 613 C ATOM 1547 CG2 ILE A 204 9.561 -4.401 34.456 1.00 28.23 C ANISOU 1547 CG2 ILE A 204 2737 5737 2253 -186 473 855 C ATOM 1548 CD1 ILE A 204 9.421 -3.082 31.516 1.00 29.76 C ANISOU 1548 CD1 ILE A 204 2849 5722 2736 -58 434 668 C ATOM 1549 N PHE A 205 7.853 -3.015 37.469 1.00 36.27 N ANISOU 1549 N PHE A 205 3727 7147 2907 -265 577 631 N ATOM 1550 CA PHE A 205 8.325 -3.100 38.850 1.00 40.67 C ANISOU 1550 CA PHE A 205 4333 7812 3308 -302 562 686 C ATOM 1551 C PHE A 205 8.805 -4.504 39.204 1.00 42.73 C ANISOU 1551 C PHE A 205 4671 8008 3554 -363 558 877 C ATOM 1552 O PHE A 205 9.396 -4.720 40.261 1.00 46.24 O ANISOU 1552 O PHE A 205 5174 8510 3884 -393 528 950 O ATOM 1553 CB PHE A 205 7.247 -2.605 39.821 1.00 41.70 C ANISOU 1553 CB PHE A 205 4439 8080 3324 -342 634 569 C ATOM 1554 CG PHE A 205 6.847 -1.175 39.586 1.00 44.13 C ANISOU 1554 CG PHE A 205 4672 8445 3648 -277 622 373 C ATOM 1555 CD1 PHE A 205 7.576 -0.137 40.146 1.00 41.56 C ANISOU 1555 CD1 PHE A 205 4344 8199 3249 -227 555 301 C ATOM 1556 CD2 PHE A 205 5.759 -0.866 38.786 1.00 46.35 C ANISOU 1556 CD2 PHE A 205 4893 8688 4032 -263 669 258 C ATOM 1557 CE1 PHE A 205 7.223 1.180 39.915 1.00 41.28 C ANISOU 1557 CE1 PHE A 205 4240 8202 3240 -164 534 117 C ATOM 1558 CE2 PHE A 205 5.398 0.453 38.556 1.00 44.16 C ANISOU 1558 CE2 PHE A 205 4550 8447 3782 -201 644 75 C ATOM 1559 CZ PHE A 205 6.133 1.474 39.120 1.00 40.87 C ANISOU 1559 CZ PHE A 205 4128 8110 3293 -151 576 4 C ATOM 1560 N ASN A 206 8.561 -5.450 38.305 1.00 43.45 N ANISOU 1560 N ASN A 206 4769 7970 3769 -379 582 953 N ATOM 1561 CA ASN A 206 9.030 -6.820 38.478 1.00 42.25 C ANISOU 1561 CA ASN A 206 4689 7731 3635 -428 569 1126 C ATOM 1562 C ASN A 206 9.114 -7.535 37.136 1.00 42.95 C ANISOU 1562 C ASN A 206 4770 7648 3900 -407 561 1180 C ATOM 1563 O ASN A 206 8.093 -7.838 36.520 1.00 41.32 O ANISOU 1563 O ASN A 206 4540 7394 3767 -427 629 1137 O ATOM 1564 CB ASN A 206 8.122 -7.591 39.439 1.00 42.74 C ANISOU 1564 CB ASN A 206 4788 7853 3596 -521 649 1165 C ATOM 1565 CG ASN A 206 8.709 -8.928 39.842 1.00 43.50 C ANISOU 1565 CG ASN A 206 4969 7874 3686 -571 621 1341 C ATOM 1566 OD1 ASN A 206 8.679 -9.889 39.072 1.00 42.51 O ANISOU 1566 OD1 ASN A 206 4858 7614 3680 -580 623 1416 O ATOM 1567 ND2 ASN A 206 9.252 -8.996 41.053 1.00 46.26 N ANISOU 1567 ND2 ASN A 206 5378 8303 3897 -604 588 1401 N ATOM 1568 N ILE A 207 10.339 -7.798 36.692 1.00 44.08 N ANISOU 1568 N ILE A 207 4936 7695 4117 -366 478 1270 N ATOM 1569 CA ILE A 207 10.594 -8.316 35.351 1.00 44.46 C ANISOU 1569 CA ILE A 207 4974 7579 4340 -332 460 1306 C ATOM 1570 C ILE A 207 9.933 -9.672 35.085 1.00 43.10 C ANISOU 1570 C ILE A 207 4837 7305 4234 -390 511 1380 C ATOM 1571 O ILE A 207 9.265 -9.851 34.067 1.00 38.05 O ANISOU 1571 O ILE A 207 4173 6578 3707 -383 549 1333 O ATOM 1572 CB ILE A 207 12.113 -8.376 35.059 1.00 45.02 C ANISOU 1572 CB ILE A 207 5063 7567 4475 -279 360 1389 C ATOM 1573 CG1 ILE A 207 12.706 -6.967 35.111 1.00 46.03 C ANISOU 1573 CG1 ILE A 207 5152 7781 4557 -213 310 1300 C ATOM 1574 CG2 ILE A 207 12.384 -9.018 33.711 1.00 40.46 C ANISOU 1574 CG2 ILE A 207 4479 6812 4080 -249 345 1426 C ATOM 1575 CD1 ILE A 207 14.205 -6.919 34.924 1.00 47.31 C ANISOU 1575 CD1 ILE A 207 5332 7867 4776 -161 212 1369 C ATOM 1576 N GLN A 208 10.108 -10.617 36.004 1.00 43.17 N ANISOU 1576 N GLN A 208 4908 7322 4171 -449 508 1490 N ATOM 1577 CA GLN A 208 9.503 -11.940 35.858 1.00 46.71 C ANISOU 1577 CA GLN A 208 5396 7681 4670 -507 552 1561 C ATOM 1578 C GLN A 208 7.977 -11.854 35.821 1.00 46.51 C ANISOU 1578 C GLN A 208 5342 7707 4623 -551 658 1471 C ATOM 1579 O GLN A 208 7.331 -12.538 35.028 1.00 45.12 O ANISOU 1579 O GLN A 208 5164 7426 4551 -565 697 1469 O ATOM 1580 CB GLN A 208 9.965 -12.882 36.975 1.00 49.53 C ANISOU 1580 CB GLN A 208 5830 8052 4937 -564 526 1691 C ATOM 1581 CG GLN A 208 11.462 -13.188 36.948 1.00 52.86 C ANISOU 1581 CG GLN A 208 6286 8390 5408 -522 419 1786 C ATOM 1582 CD GLN A 208 12.325 -11.951 37.174 1.00 55.33 C ANISOU 1582 CD GLN A 208 6570 8779 5673 -463 357 1737 C ATOM 1583 OE1 GLN A 208 12.010 -11.102 38.013 1.00 54.46 O ANISOU 1583 OE1 GLN A 208 6451 8817 5424 -476 379 1676 O ATOM 1584 NE2 GLN A 208 13.416 -11.843 36.418 1.00 55.12 N ANISOU 1584 NE2 GLN A 208 6529 8649 5764 -396 281 1756 N ATOM 1585 N ASN A 209 7.410 -11.011 36.681 1.00 45.75 N ANISOU 1585 N ASN A 209 5220 7767 4394 -570 701 1391 N ATOM 1586 CA ASN A 209 5.969 -10.771 36.697 1.00 47.10 C ANISOU 1586 CA ASN A 209 5352 7997 4547 -605 801 1287 C ATOM 1587 C ASN A 209 5.483 -10.205 35.375 1.00 44.04 C ANISOU 1587 C ASN A 209 4904 7531 4299 -550 813 1175 C ATOM 1588 O ASN A 209 4.562 -10.738 34.752 1.00 39.91 O ANISOU 1588 O ASN A 209 4372 6930 3860 -574 871 1153 O ATOM 1589 CB ASN A 209 5.599 -9.796 37.817 1.00 48.17 C ANISOU 1589 CB ASN A 209 5464 8316 4524 -620 833 1200 C ATOM 1590 CG ASN A 209 5.314 -10.492 39.127 1.00 55.47 C ANISOU 1590 CG ASN A 209 6444 9324 5307 -706 876 1279 C ATOM 1591 OD1 ASN A 209 5.507 -11.702 39.255 1.00 58.44 O ANISOU 1591 OD1 ASN A 209 6883 9624 5699 -752 871 1409 O ATOM 1592 ND2 ASN A 209 4.853 -9.730 40.113 1.00 56.18 N ANISOU 1592 ND2 ASN A 209 6515 9572 5258 -727 917 1196 N ATOM 1593 N PHE A 210 6.107 -9.103 34.974 1.00 44.34 N ANISOU 1593 N PHE A 210 4902 7589 4356 -478 756 1103 N ATOM 1594 CA PHE A 210 5.803 -8.423 33.725 1.00 37.19 C ANISOU 1594 CA PHE A 210 3946 6609 3576 -420 752 995 C ATOM 1595 C PHE A 210 5.731 -9.417 32.575 1.00 36.94 C ANISOU 1595 C PHE A 210 3939 6398 3699 -422 752 1051 C ATOM 1596 O PHE A 210 4.763 -9.438 31.817 1.00 32.56 O ANISOU 1596 O PHE A 210 3362 5779 3231 -425 800 975 O ATOM 1597 CB PHE A 210 6.866 -7.349 33.463 1.00 37.14 C ANISOU 1597 CB PHE A 210 3914 6627 3571 -343 670 956 C ATOM 1598 CG PHE A 210 6.877 -6.821 32.055 1.00 33.87 C ANISOU 1598 CG PHE A 210 3467 6101 3301 -281 645 879 C ATOM 1599 CD1 PHE A 210 5.838 -6.036 31.584 1.00 35.01 C ANISOU 1599 CD1 PHE A 210 3564 6254 3485 -265 683 729 C ATOM 1600 CD2 PHE A 210 7.946 -7.088 31.213 1.00 32.61 C ANISOU 1600 CD2 PHE A 210 3327 5823 3242 -238 579 952 C ATOM 1601 CE1 PHE A 210 5.852 -5.543 30.288 1.00 32.14 C ANISOU 1601 CE1 PHE A 210 3182 5774 3254 -212 654 657 C ATOM 1602 CE2 PHE A 210 7.969 -6.596 29.912 1.00 32.13 C ANISOU 1602 CE2 PHE A 210 3244 5653 3309 -186 556 880 C ATOM 1603 CZ PHE A 210 6.922 -5.821 29.453 1.00 28.50 C ANISOU 1603 CZ PHE A 210 2748 5198 2883 -176 593 733 C ATOM 1604 N ILE A 211 6.755 -10.254 32.462 1.00 39.70 N ANISOU 1604 N ILE A 211 4336 6662 4085 -418 695 1179 N ATOM 1605 CA ILE A 211 6.829 -11.223 31.378 1.00 44.60 C ANISOU 1605 CA ILE A 211 4984 7110 4851 -414 684 1227 C ATOM 1606 C ILE A 211 5.695 -12.244 31.422 1.00 46.45 C ANISOU 1606 C ILE A 211 5243 7306 5101 -483 760 1241 C ATOM 1607 O ILE A 211 5.030 -12.479 30.412 1.00 46.91 O ANISOU 1607 O ILE A 211 5293 7263 5269 -479 787 1187 O ATOM 1608 CB ILE A 211 8.188 -11.931 31.356 1.00 47.10 C ANISOU 1608 CB ILE A 211 5343 7347 5205 -394 603 1352 C ATOM 1609 CG1 ILE A 211 9.283 -10.919 31.011 1.00 43.30 C ANISOU 1609 CG1 ILE A 211 4831 6874 4746 -318 531 1329 C ATOM 1610 CG2 ILE A 211 8.173 -13.067 30.346 1.00 49.93 C ANISOU 1610 CG2 ILE A 211 5733 7535 5704 -396 597 1393 C ATOM 1611 CD1 ILE A 211 10.672 -11.469 31.099 1.00 40.56 C ANISOU 1611 CD1 ILE A 211 4515 6461 4434 -294 451 1441 C ATOM 1612 N ASN A 212 5.469 -12.842 32.589 1.00 46.46 N ANISOU 1612 N ASN A 212 5276 7389 4990 -547 794 1313 N ATOM 1613 CA ASN A 212 4.372 -13.792 32.738 1.00 48.23 C ANISOU 1613 CA ASN A 212 5521 7589 5215 -617 872 1331 C ATOM 1614 C ASN A 212 3.023 -13.174 32.392 1.00 44.63 C ANISOU 1614 C ASN A 212 5010 7166 4783 -625 953 1198 C ATOM 1615 O ASN A 212 2.147 -13.845 31.854 1.00 46.59 O ANISOU 1615 O ASN A 212 5262 7336 5107 -656 1005 1184 O ATOM 1616 CB ASN A 212 4.338 -14.381 34.149 1.00 53.42 C ANISOU 1616 CB ASN A 212 6222 8345 5729 -688 898 1424 C ATOM 1617 CG ASN A 212 5.361 -15.477 34.342 1.00 58.93 C ANISOU 1617 CG ASN A 212 6989 8961 6440 -699 831 1568 C ATOM 1618 OD1 ASN A 212 6.361 -15.545 33.623 1.00 61.33 O ANISOU 1618 OD1 ASN A 212 7298 9167 6838 -642 752 1596 O ATOM 1619 ND2 ASN A 212 5.114 -16.350 35.309 1.00 61.54 N ANISOU 1619 ND2 ASN A 212 7371 9329 6682 -772 861 1658 N ATOM 1620 N THR A 213 2.866 -11.892 32.697 1.00 42.70 N ANISOU 1620 N THR A 213 4711 7034 4478 -593 959 1096 N ATOM 1621 CA THR A 213 1.643 -11.178 32.356 1.00 44.21 C ANISOU 1621 CA THR A 213 4841 7252 4703 -587 1024 957 C ATOM 1622 C THR A 213 1.489 -10.987 30.846 1.00 41.71 C ANISOU 1622 C THR A 213 4507 6790 4552 -538 1001 888 C ATOM 1623 O THR A 213 0.377 -11.049 30.325 1.00 43.83 O ANISOU 1623 O THR A 213 4748 7012 4893 -552 1059 816 O ATOM 1624 CB THR A 213 1.561 -9.820 33.070 1.00 46.97 C ANISOU 1624 CB THR A 213 5139 7759 4950 -560 1025 853 C ATOM 1625 OG1 THR A 213 1.583 -10.027 34.487 1.00 50.46 O ANISOU 1625 OG1 THR A 213 5602 8339 5232 -615 1054 908 O ATOM 1626 CG2 THR A 213 0.275 -9.095 32.693 1.00 45.56 C ANISOU 1626 CG2 THR A 213 4892 7596 4822 -547 1084 705 C ATOM 1627 N LEU A 214 2.596 -10.755 30.143 1.00 40.22 N ANISOU 1627 N LEU A 214 4334 6526 4423 -481 917 909 N ATOM 1628 CA LEU A 214 2.542 -10.668 28.686 1.00 39.37 C ANISOU 1628 CA LEU A 214 4223 6270 4465 -441 890 852 C ATOM 1629 C LEU A 214 2.198 -12.029 28.103 1.00 42.05 C ANISOU 1629 C LEU A 214 4608 6484 4886 -483 911 913 C ATOM 1630 O LEU A 214 1.350 -12.141 27.219 1.00 40.96 O ANISOU 1630 O LEU A 214 4460 6261 4842 -490 942 841 O ATOM 1631 CB LEU A 214 3.871 -10.187 28.097 1.00 36.53 C ANISOU 1631 CB LEU A 214 3874 5860 4147 -374 797 871 C ATOM 1632 CG LEU A 214 4.219 -8.699 28.170 1.00 37.64 C ANISOU 1632 CG LEU A 214 3968 6083 4252 -316 761 778 C ATOM 1633 CD1 LEU A 214 5.592 -8.452 27.565 1.00 34.40 C ANISOU 1633 CD1 LEU A 214 3574 5606 3891 -257 674 822 C ATOM 1634 CD2 LEU A 214 3.176 -7.862 27.463 1.00 35.89 C ANISOU 1634 CD2 LEU A 214 3704 5832 4102 -297 790 628 C ATOM 1635 N LEU A 215 2.861 -13.064 28.610 1.00 45.25 N ANISOU 1635 N LEU A 215 5064 6876 5253 -512 889 1043 N ATOM 1636 CA LEU A 215 2.652 -14.419 28.119 1.00 50.29 C ANISOU 1636 CA LEU A 215 5750 7397 5959 -549 897 1104 C ATOM 1637 C LEU A 215 1.193 -14.853 28.228 1.00 56.25 C ANISOU 1637 C LEU A 215 6493 8163 6717 -612 992 1062 C ATOM 1638 O LEU A 215 0.664 -15.492 27.318 1.00 56.36 O ANISOU 1638 O LEU A 215 6521 8068 6823 -627 1004 1037 O ATOM 1639 CB LEU A 215 3.551 -15.410 28.860 1.00 53.67 C ANISOU 1639 CB LEU A 215 6231 7825 6335 -572 860 1249 C ATOM 1640 CG LEU A 215 5.062 -15.222 28.717 1.00 56.52 C ANISOU 1640 CG LEU A 215 6605 8153 6715 -510 764 1306 C ATOM 1641 CD1 LEU A 215 5.798 -16.403 29.330 1.00 59.47 C ANISOU 1641 CD1 LEU A 215 7033 8498 7063 -538 729 1442 C ATOM 1642 CD2 LEU A 215 5.448 -15.051 27.257 1.00 54.46 C ANISOU 1642 CD2 LEU A 215 6339 7762 6591 -449 714 1250 C ATOM 1643 N LYS A 216 0.543 -14.503 29.335 1.00 62.50 N ANISOU 1643 N LYS A 216 7255 9088 7403 -649 1059 1051 N ATOM 1644 CA LYS A 216 -0.840 -14.921 29.563 1.00 69.72 C ANISOU 1644 CA LYS A 216 8150 10023 8318 -708 1157 1019 C ATOM 1645 C LYS A 216 -1.844 -14.090 28.763 1.00 73.13 C ANISOU 1645 C LYS A 216 8518 10429 8839 -681 1195 876 C ATOM 1646 O LYS A 216 -3.000 -13.944 29.160 1.00 75.29 O ANISOU 1646 O LYS A 216 8746 10764 9099 -710 1278 826 O ATOM 1647 CB LYS A 216 -1.190 -14.891 31.057 1.00 73.04 C ANISOU 1647 CB LYS A 216 8562 10600 8590 -759 1217 1060 C ATOM 1648 CG LYS A 216 -1.438 -13.503 31.631 1.00 75.18 C ANISOU 1648 CG LYS A 216 8768 11011 8786 -729 1234 960 C ATOM 1649 CD LYS A 216 -2.529 -13.552 32.694 1.00 78.52 C ANISOU 1649 CD LYS A 216 9161 11562 9112 -789 1332 945 C ATOM 1650 CE LYS A 216 -2.805 -12.181 33.293 1.00 80.81 C ANISOU 1650 CE LYS A 216 9384 11999 9321 -759 1345 831 C ATOM 1651 NZ LYS A 216 -1.704 -11.719 34.184 1.00 82.34 N ANISOU 1651 NZ LYS A 216 9605 12298 9382 -748 1287 871 N ATOM 1652 N ASP A 217 -1.397 -13.550 27.633 1.00 74.63 N ANISOU 1652 N ASP A 217 8704 10528 9124 -622 1132 813 N ATOM 1653 CA ASP A 217 -2.265 -12.779 26.752 1.00 74.56 C ANISOU 1653 CA ASP A 217 8642 10473 9215 -593 1153 679 C ATOM 1654 C ASP A 217 -2.284 -13.393 25.358 1.00 72.02 C ANISOU 1654 C ASP A 217 8344 10015 9005 -594 1111 671 C ATOM 1655 O ASP A 217 -1.610 -14.391 25.102 1.00 71.13 O ANISOU 1655 O ASP A 217 8286 9845 8894 -608 1065 768 O ATOM 1656 CB ASP A 217 -1.804 -11.322 26.680 1.00 76.69 C ANISOU 1656 CB ASP A 217 8870 10791 9475 -521 1104 598 C ATOM 1657 CG ASP A 217 -1.929 -10.600 28.013 1.00 79.31 C ANISOU 1657 CG ASP A 217 9162 11298 9676 -522 1133 588 C ATOM 1658 OD1 ASP A 217 -2.073 -11.278 29.052 1.00 81.63 O ANISOU 1658 OD1 ASP A 217 9472 11675 9870 -578 1180 667 O ATOM 1659 OD2 ASP A 217 -1.878 -9.351 28.023 1.00 78.72 O ANISOU 1659 OD2 ASP A 217 9042 11280 9590 -468 1105 497 O TER 1660 ASP A 217 ATOM 1661 N MET B 5 18.196 8.092 77.720 1.00 30.25 N ANISOU 1661 N MET B 5 4431 3664 3397 -138 -119 46 N ATOM 1662 CA MET B 5 18.627 9.481 77.773 1.00 25.66 C ANISOU 1662 CA MET B 5 3850 3087 2811 -148 -145 33 C ATOM 1663 C MET B 5 17.494 10.404 78.189 1.00 22.88 C ANISOU 1663 C MET B 5 3508 2712 2475 -161 -102 -19 C ATOM 1664 O MET B 5 16.484 10.510 77.492 1.00 27.83 O ANISOU 1664 O MET B 5 4101 3323 3150 -145 -74 -44 O ATOM 1665 CB MET B 5 19.176 9.928 76.416 1.00 28.04 C ANISOU 1665 CB MET B 5 4099 3401 3154 -123 -185 49 C ATOM 1666 CG MET B 5 19.508 11.412 76.357 1.00 30.01 C ANISOU 1666 CG MET B 5 4343 3647 3414 -134 -208 37 C ATOM 1667 SD MET B 5 20.339 11.900 74.829 1.00 32.13 S ANISOU 1667 SD MET B 5 4550 3936 3723 -105 -257 71 S ATOM 1668 CE MET B 5 21.794 10.855 74.887 1.00 66.60 C ANISOU 1668 CE MET B 5 8920 8338 8048 -101 -301 126 C ATOM 1669 N LYS B 6 17.676 11.077 79.320 1.00 24.28 N ANISOU 1669 N LYS B 6 3729 2888 2607 -188 -100 -36 N ATOM 1670 CA LYS B 6 16.713 12.057 79.802 1.00 25.05 C ANISOU 1670 CA LYS B 6 3839 2963 2715 -200 -62 -89 C ATOM 1671 C LYS B 6 16.759 13.335 78.971 1.00 26.85 C ANISOU 1671 C LYS B 6 4032 3176 2994 -189 -84 -106 C ATOM 1672 O LYS B 6 17.838 13.832 78.628 1.00 23.85 O ANISOU 1672 O LYS B 6 3642 2805 2614 -191 -136 -82 O ATOM 1673 CB LYS B 6 16.977 12.383 81.275 1.00 23.78 C ANISOU 1673 CB LYS B 6 3738 2810 2486 -230 -56 -107 C ATOM 1674 CG LYS B 6 16.542 11.290 82.232 1.00 29.70 C ANISOU 1674 CG LYS B 6 4525 3571 3188 -240 -14 -97 C ATOM 1675 CD LYS B 6 16.994 11.594 83.652 1.00 36.08 C ANISOU 1675 CD LYS B 6 5393 4400 3918 -267 -18 -108 C ATOM 1676 CE LYS B 6 16.323 10.679 84.658 1.00 40.23 C ANISOU 1676 CE LYS B 6 5955 4935 4396 -276 36 -102 C ATOM 1677 NZ LYS B 6 16.708 11.024 86.058 1.00 45.82 N ANISOU 1677 NZ LYS B 6 6721 5670 5019 -299 34 -116 N ATOM 1678 N SER B 7 15.584 13.867 78.651 1.00 20.44 N ANISOU 1678 N SER B 7 3199 2340 2228 -178 -45 -145 N ATOM 1679 CA SER B 7 15.497 15.091 77.875 1.00 18.27 C ANISOU 1679 CA SER B 7 2891 2045 2005 -166 -61 -159 C ATOM 1680 C SER B 7 15.652 16.336 78.738 1.00 20.16 C ANISOU 1680 C SER B 7 3164 2264 2232 -189 -64 -195 C ATOM 1681 O SER B 7 16.238 17.335 78.304 1.00 22.45 O ANISOU 1681 O SER B 7 3439 2541 2551 -189 -100 -189 O ATOM 1682 CB SER B 7 14.148 15.154 77.165 1.00 20.91 C ANISOU 1682 CB SER B 7 3186 2364 2396 -140 -19 -185 C ATOM 1683 OG SER B 7 13.108 15.192 78.122 1.00 17.30 O ANISOU 1683 OG SER B 7 2756 1891 1926 -153 36 -230 O ATOM 1684 N HIS B 8 15.118 16.265 79.955 1.00 19.43 N ANISOU 1684 N HIS B 8 3117 2168 2098 -208 -25 -232 N ATOM 1685 CA HIS B 8 14.952 17.421 80.832 1.00 20.95 C ANISOU 1685 CA HIS B 8 3342 2338 2279 -226 -15 -284 C ATOM 1686 C HIS B 8 14.025 18.473 80.241 1.00 23.62 C ANISOU 1686 C HIS B 8 3649 2638 2689 -206 9 -320 C ATOM 1687 O HIS B 8 14.069 19.644 80.630 1.00 24.12 O ANISOU 1687 O HIS B 8 3727 2673 2765 -216 4 -358 O ATOM 1688 CB HIS B 8 16.296 18.027 81.239 1.00 25.05 C ANISOU 1688 CB HIS B 8 3886 2864 2770 -250 -72 -274 C ATOM 1689 CG HIS B 8 17.167 17.080 82.004 1.00 28.22 C ANISOU 1689 CG HIS B 8 4324 3305 3095 -269 -94 -244 C ATOM 1690 ND1 HIS B 8 16.762 16.483 83.176 1.00 30.23 N ANISOU 1690 ND1 HIS B 8 4623 3577 3284 -282 -58 -262 N ATOM 1691 CD2 HIS B 8 18.412 16.609 81.750 1.00 32.42 C ANISOU 1691 CD2 HIS B 8 4849 3863 3606 -274 -148 -192 C ATOM 1692 CE1 HIS B 8 17.723 15.689 83.619 1.00 35.82 C ANISOU 1692 CE1 HIS B 8 5355 4320 3935 -294 -90 -221 C ATOM 1693 NE2 HIS B 8 18.734 15.749 82.772 1.00 34.82 N ANISOU 1693 NE2 HIS B 8 5196 4199 3835 -289 -145 -180 N ATOM 1694 N PHE B 9 13.181 18.048 79.302 1.00 21.62 N ANISOU 1694 N PHE B 9 3349 2382 2482 -178 33 -310 N ATOM 1695 CA PHE B 9 12.165 18.928 78.744 1.00 20.38 C ANISOU 1695 CA PHE B 9 3159 2194 2391 -155 60 -342 C ATOM 1696 C PHE B 9 11.145 19.274 79.819 1.00 20.13 C ANISOU 1696 C PHE B 9 3158 2146 2346 -162 118 -404 C ATOM 1697 O PHE B 9 10.789 18.436 80.648 1.00 25.57 O ANISOU 1697 O PHE B 9 3875 2854 2984 -176 154 -413 O ATOM 1698 CB PHE B 9 11.430 18.261 77.575 1.00 20.03 C ANISOU 1698 CB PHE B 9 3058 2160 2392 -123 74 -321 C ATOM 1699 CG PHE B 9 12.286 18.012 76.371 1.00 19.62 C ANISOU 1699 CG PHE B 9 2968 2127 2360 -107 22 -265 C ATOM 1700 CD1 PHE B 9 13.470 18.705 76.184 1.00 20.57 C ANISOU 1700 CD1 PHE B 9 3093 2244 2479 -116 -29 -238 C ATOM 1701 CD2 PHE B 9 11.894 17.091 75.413 1.00 22.06 C ANISOU 1701 CD2 PHE B 9 3234 2459 2689 -82 25 -243 C ATOM 1702 CE1 PHE B 9 14.255 18.475 75.065 1.00 21.91 C ANISOU 1702 CE1 PHE B 9 3225 2437 2664 -99 -73 -184 C ATOM 1703 CE2 PHE B 9 12.672 16.856 74.294 1.00 24.96 C ANISOU 1703 CE2 PHE B 9 3566 2849 3069 -64 -20 -195 C ATOM 1704 CZ PHE B 9 13.856 17.551 74.123 1.00 22.42 C ANISOU 1704 CZ PHE B 9 3248 2527 2742 -71 -68 -164 C ATOM 1705 N GLN B 10 10.689 20.519 79.806 1.00 23.26 N ANISOU 1705 N GLN B 10 3549 2504 2786 -153 128 -444 N ATOM 1706 CA GLN B 10 9.539 20.917 80.600 1.00 27.86 C ANISOU 1706 CA GLN B 10 4146 3069 3370 -150 189 -506 C ATOM 1707 C GLN B 10 8.340 20.822 79.676 1.00 22.93 C ANISOU 1707 C GLN B 10 3466 2437 2811 -115 222 -508 C ATOM 1708 O GLN B 10 8.253 21.557 78.695 1.00 23.21 O ANISOU 1708 O GLN B 10 3460 2449 2910 -90 202 -497 O ATOM 1709 CB GLN B 10 9.700 22.352 81.107 1.00 30.54 C ANISOU 1709 CB GLN B 10 4509 3367 3726 -156 181 -554 C ATOM 1710 CG GLN B 10 11.021 22.612 81.809 1.00 33.55 C ANISOU 1710 CG GLN B 10 4938 3754 4056 -190 133 -551 C ATOM 1711 CD GLN B 10 11.094 23.992 82.440 1.00 36.01 C ANISOU 1711 CD GLN B 10 5276 4022 4383 -200 130 -610 C ATOM 1712 OE1 GLN B 10 11.106 24.124 83.665 1.00 42.32 O ANISOU 1712 OE1 GLN B 10 6126 4829 5125 -221 147 -660 O ATOM 1713 NE2 GLN B 10 11.155 25.026 81.607 1.00 26.98 N ANISOU 1713 NE2 GLN B 10 4100 2833 3320 -184 107 -606 N ATOM 1714 N TYR B 11 7.423 19.905 79.966 1.00 19.89 N ANISOU 1714 N TYR B 11 3075 2072 2411 -113 273 -518 N ATOM 1715 CA TYR B 11 6.286 19.708 79.069 1.00 17.79 C ANISOU 1715 CA TYR B 11 2749 1803 2206 -82 301 -521 C ATOM 1716 C TYR B 11 4.944 19.819 79.768 1.00 20.24 C ANISOU 1716 C TYR B 11 3059 2107 2524 -76 373 -575 C ATOM 1717 O TYR B 11 4.850 19.710 80.984 1.00 20.06 O ANISOU 1717 O TYR B 11 3083 2090 2447 -99 408 -604 O ATOM 1718 CB TYR B 11 6.388 18.394 78.279 1.00 17.45 C ANISOU 1718 CB TYR B 11 2675 1793 2163 -78 287 -473 C ATOM 1719 CG TYR B 11 6.583 17.135 79.091 1.00 20.79 C ANISOU 1719 CG TYR B 11 3133 2243 2523 -106 306 -460 C ATOM 1720 CD1 TYR B 11 7.858 16.709 79.439 1.00 20.24 C ANISOU 1720 CD1 TYR B 11 3103 2190 2398 -129 264 -424 C ATOM 1721 CD2 TYR B 11 5.501 16.358 79.487 1.00 20.52 C ANISOU 1721 CD2 TYR B 11 3090 2218 2489 -110 365 -478 C ATOM 1722 CE1 TYR B 11 8.056 15.561 80.157 1.00 14.77 C ANISOU 1722 CE1 TYR B 11 2442 1520 1650 -151 280 -405 C ATOM 1723 CE2 TYR B 11 5.688 15.201 80.215 1.00 20.76 C ANISOU 1723 CE2 TYR B 11 3153 2269 2466 -136 384 -458 C ATOM 1724 CZ TYR B 11 6.975 14.806 80.542 1.00 20.79 C ANISOU 1724 CZ TYR B 11 3198 2288 2415 -155 340 -420 C ATOM 1725 OH TYR B 11 7.194 13.661 81.262 1.00 19.01 O ANISOU 1725 OH TYR B 11 3004 2081 2137 -177 357 -394 O ATOM 1726 N SER B 12 3.906 20.057 78.977 1.00 18.74 N ANISOU 1726 N SER B 12 2813 1908 2402 -45 394 -587 N ATOM 1727 CA SER B 12 2.572 20.249 79.519 1.00 18.43 C ANISOU 1727 CA SER B 12 2762 1861 2381 -34 463 -638 C ATOM 1728 C SER B 12 1.622 19.331 78.775 1.00 19.43 C ANISOU 1728 C SER B 12 2829 2008 2545 -19 486 -625 C ATOM 1729 O SER B 12 2.044 18.350 78.172 1.00 16.58 O ANISOU 1729 O SER B 12 2452 1670 2176 -26 457 -583 O ATOM 1730 CB SER B 12 2.139 21.710 79.347 1.00 28.56 C ANISOU 1730 CB SER B 12 4029 3103 3720 -6 467 -676 C ATOM 1731 OG SER B 12 0.902 21.964 79.996 1.00 36.81 O ANISOU 1731 OG SER B 12 5067 4141 4779 5 536 -730 O ATOM 1732 N THR B 13 0.338 19.658 78.812 1.00 21.47 N ANISOU 1732 N THR B 13 3051 2258 2847 2 538 -665 N ATOM 1733 CA THR B 13 -0.671 18.884 78.114 1.00 22.20 C ANISOU 1733 CA THR B 13 3081 2370 2983 16 561 -661 C ATOM 1734 C THR B 13 -1.426 19.815 77.184 1.00 18.11 C ANISOU 1734 C THR B 13 2503 1835 2541 60 556 -677 C ATOM 1735 O THR B 13 -1.640 20.979 77.518 1.00 24.56 O ANISOU 1735 O THR B 13 3331 2622 3378 77 569 -709 O ATOM 1736 CB THR B 13 -1.662 18.257 79.115 1.00 34.00 C ANISOU 1736 CB THR B 13 4582 3878 4458 -3 637 -693 C ATOM 1737 OG1 THR B 13 -0.936 17.516 80.103 1.00 42.80 O ANISOU 1737 OG1 THR B 13 5760 5008 5497 -42 644 -676 O ATOM 1738 CG2 THR B 13 -2.634 17.330 78.411 1.00 34.93 C ANISOU 1738 CG2 THR B 13 4634 4016 4624 4 658 -687 C ATOM 1739 N LEU B 14 -1.821 19.317 76.015 1.00 16.15 N ANISOU 1739 N LEU B 14 2192 1606 2337 81 535 -655 N ATOM 1740 CA LEU B 14 -2.687 20.092 75.131 1.00 24.50 C ANISOU 1740 CA LEU B 14 3186 2656 3467 127 534 -668 C ATOM 1741 C LEU B 14 -4.020 20.330 75.838 1.00 25.56 C ANISOU 1741 C LEU B 14 3301 2783 3626 134 606 -722 C ATOM 1742 O LEU B 14 -4.495 19.466 76.577 1.00 25.42 O ANISOU 1742 O LEU B 14 3293 2782 3583 107 654 -738 O ATOM 1743 CB LEU B 14 -2.917 19.370 73.801 1.00 20.51 C ANISOU 1743 CB LEU B 14 2615 2183 2994 146 499 -640 C ATOM 1744 CG LEU B 14 -1.746 19.270 72.826 1.00 22.29 C ANISOU 1744 CG LEU B 14 2842 2421 3206 153 427 -587 C ATOM 1745 CD1 LEU B 14 -2.213 18.614 71.535 1.00 16.98 C ANISOU 1745 CD1 LEU B 14 2099 1786 2569 178 400 -573 C ATOM 1746 CD2 LEU B 14 -1.145 20.639 72.542 1.00 21.47 C ANISOU 1746 CD2 LEU B 14 2751 2288 3119 176 393 -571 C ATOM 1747 N GLU B 15 -4.625 21.497 75.623 1.00 22.12 N ANISOU 1747 N GLU B 15 2839 2323 3243 173 616 -746 N ATOM 1748 CA GLU B 15 -5.840 21.825 76.359 1.00 26.91 C ANISOU 1748 CA GLU B 15 3430 2922 3873 183 687 -800 C ATOM 1749 C GLU B 15 -6.966 20.892 75.928 1.00 27.47 C ANISOU 1749 C GLU B 15 3432 3027 3978 187 717 -806 C ATOM 1750 O GLU B 15 -7.877 20.610 76.699 1.00 29.67 O ANISOU 1750 O GLU B 15 3702 3314 4257 177 782 -842 O ATOM 1751 CB GLU B 15 -6.225 23.300 76.208 1.00 32.76 C ANISOU 1751 CB GLU B 15 4156 3624 4669 227 690 -826 C ATOM 1752 CG GLU B 15 -6.953 23.649 74.927 1.00 35.83 C ANISOU 1752 CG GLU B 15 4463 4018 5132 277 668 -812 C ATOM 1753 CD GLU B 15 -7.350 25.112 74.882 1.00 37.41 C ANISOU 1753 CD GLU B 15 4652 4174 5389 322 676 -835 C ATOM 1754 OE1 GLU B 15 -8.223 25.469 74.061 1.00 41.78 O ANISOU 1754 OE1 GLU B 15 5136 4733 6007 367 675 -834 O ATOM 1755 OE2 GLU B 15 -6.791 25.904 75.672 1.00 27.99 O ANISOU 1755 OE2 GLU B 15 3518 2941 4177 312 682 -856 O ATOM 1756 N ASN B 16 -6.886 20.409 74.693 1.00 29.52 N ANISOU 1756 N ASN B 16 3642 3310 4265 201 667 -772 N ATOM 1757 CA ASN B 16 -7.698 19.278 74.251 1.00 31.83 C ANISOU 1757 CA ASN B 16 3877 3639 4580 194 683 -774 C ATOM 1758 C ASN B 16 -7.159 18.644 72.973 1.00 28.87 C ANISOU 1758 C ASN B 16 3470 3290 4211 201 615 -733 C ATOM 1759 O ASN B 16 -6.275 19.196 72.316 1.00 30.10 O ANISOU 1759 O ASN B 16 3638 3439 4360 220 558 -701 O ATOM 1760 CB ASN B 16 -9.181 19.646 74.112 1.00 37.77 C ANISOU 1760 CB ASN B 16 4558 4396 5397 226 728 -814 C ATOM 1761 CG ASN B 16 -9.406 20.865 73.248 1.00 39.22 C ANISOU 1761 CG ASN B 16 4701 4566 5634 282 696 -811 C ATOM 1762 OD1 ASN B 16 -8.587 21.193 72.389 1.00 39.15 O ANISOU 1762 OD1 ASN B 16 4696 4556 5623 300 632 -772 O ATOM 1763 ND2 ASN B 16 -10.528 21.548 73.472 1.00 36.74 N ANISOU 1763 ND2 ASN B 16 4347 4243 5369 313 742 -849 N ATOM 1764 N ILE B 17 -7.694 17.476 72.636 1.00 23.51 N ANISOU 1764 N ILE B 17 2748 2639 3545 185 622 -737 N ATOM 1765 CA ILE B 17 -7.219 16.701 71.498 1.00 18.72 C ANISOU 1765 CA ILE B 17 2113 2062 2940 189 563 -707 C ATOM 1766 C ILE B 17 -7.606 17.364 70.182 1.00 23.55 C ANISOU 1766 C ILE B 17 2656 2692 3600 243 519 -701 C ATOM 1767 O ILE B 17 -8.775 17.650 69.956 1.00 24.41 O ANISOU 1767 O ILE B 17 2704 2810 3761 268 544 -730 O ATOM 1768 CB ILE B 17 -7.789 15.272 71.538 1.00 21.29 C ANISOU 1768 CB ILE B 17 2408 2407 3275 156 586 -720 C ATOM 1769 CG1 ILE B 17 -7.530 14.639 72.909 1.00 28.06 C ANISOU 1769 CG1 ILE B 17 3330 3246 4085 105 637 -721 C ATOM 1770 CG2 ILE B 17 -7.191 14.413 70.425 1.00 21.60 C ANISOU 1770 CG2 ILE B 17 2425 2473 3309 159 523 -695 C ATOM 1771 CD1 ILE B 17 -6.063 14.612 73.302 1.00 31.08 C ANISOU 1771 CD1 ILE B 17 3793 3616 4401 85 604 -684 C ATOM 1772 N PRO B 18 -6.618 17.630 69.313 1.00 25.86 N ANISOU 1772 N PRO B 18 2957 2994 3875 263 455 -660 N ATOM 1773 CA PRO B 18 -6.948 18.214 68.014 1.00 23.88 C ANISOU 1773 CA PRO B 18 2641 2768 3664 316 412 -647 C ATOM 1774 C PRO B 18 -7.981 17.378 67.266 1.00 27.41 C ANISOU 1774 C PRO B 18 3009 3257 4149 326 410 -673 C ATOM 1775 O PRO B 18 -8.028 16.150 67.401 1.00 20.58 O ANISOU 1775 O PRO B 18 2142 2406 3272 291 418 -686 O ATOM 1776 CB PRO B 18 -5.604 18.212 67.287 1.00 22.74 C ANISOU 1776 CB PRO B 18 2523 2636 3480 322 347 -597 C ATOM 1777 CG PRO B 18 -4.613 18.398 68.396 1.00 27.44 C ANISOU 1777 CG PRO B 18 3205 3192 4029 284 361 -585 C ATOM 1778 CD PRO B 18 -5.162 17.577 69.536 1.00 25.12 C ANISOU 1778 CD PRO B 18 2933 2888 3725 241 421 -622 C ATOM 1779 N LYS B 19 -8.811 18.065 66.490 1.00 34.80 N ANISOU 1779 N LYS B 19 2718 5208 5297 552 216 -683 N ATOM 1780 CA LYS B 19 -9.922 17.447 65.786 1.00 33.53 C ANISOU 1780 CA LYS B 19 2427 5141 5173 522 149 -705 C ATOM 1781 C LYS B 19 -9.474 16.332 64.847 1.00 26.66 C ANISOU 1781 C LYS B 19 1562 4308 4261 446 42 -733 C ATOM 1782 O LYS B 19 -10.168 15.325 64.688 1.00 26.94 O ANISOU 1782 O LYS B 19 1519 4392 4326 355 23 -776 O ATOM 1783 CB LYS B 19 -10.676 18.517 64.997 1.00 38.86 C ANISOU 1783 CB LYS B 19 3041 5865 5860 653 91 -652 C ATOM 1784 CG LYS B 19 -11.870 18.013 64.216 1.00 46.45 C ANISOU 1784 CG LYS B 19 3864 6923 6864 634 16 -668 C ATOM 1785 CD LYS B 19 -12.256 19.030 63.151 1.00 52.56 C ANISOU 1785 CD LYS B 19 4609 7734 7625 762 -72 -609 C ATOM 1786 CE LYS B 19 -13.732 18.948 62.806 1.00 58.25 C ANISOU 1786 CE LYS B 19 5174 8539 8420 770 -100 -613 C ATOM 1787 NZ LYS B 19 -14.103 19.985 61.805 1.00 61.19 N ANISOU 1787 NZ LYS B 19 5524 8940 8786 894 -180 -551 N ATOM 1788 N ALA B 20 -8.321 16.515 64.214 1.00 26.65 N ANISOU 1788 N ALA B 20 1658 4279 4188 483 -24 -706 N ATOM 1789 CA ALA B 20 -7.832 15.543 63.246 1.00 22.86 C ANISOU 1789 CA ALA B 20 1197 3829 3660 422 -125 -726 C ATOM 1790 C ALA B 20 -7.742 14.133 63.834 1.00 29.31 C ANISOU 1790 C ALA B 20 2010 4632 4495 266 -80 -788 C ATOM 1791 O ALA B 20 -7.842 13.142 63.108 1.00 29.89 O ANISOU 1791 O ALA B 20 2065 4743 4548 195 -151 -816 O ATOM 1792 CB ALA B 20 -6.487 15.981 62.688 1.00 21.66 C ANISOU 1792 CB ALA B 20 1184 3623 3424 477 -177 -676 C ATOM 1793 N PHE B 21 -7.555 14.037 65.146 1.00 25.62 N ANISOU 1793 N PHE B 21 1605 4085 4045 206 41 -790 N ATOM 1794 CA PHE B 21 -7.315 12.736 65.763 1.00 27.09 C ANISOU 1794 CA PHE B 21 1835 4229 4229 57 90 -830 C ATOM 1795 C PHE B 21 -8.595 11.925 65.956 1.00 28.67 C ANISOU 1795 C PHE B 21 1892 4498 4503 -24 116 -896 C ATOM 1796 O PHE B 21 -8.543 10.723 66.198 1.00 29.57 O ANISOU 1796 O PHE B 21 2030 4592 4611 -148 136 -934 O ATOM 1797 CB PHE B 21 -6.561 12.892 67.090 1.00 27.16 C ANISOU 1797 CB PHE B 21 1988 4118 4214 17 204 -800 C ATOM 1798 CG PHE B 21 -5.177 13.456 66.933 1.00 24.21 C ANISOU 1798 CG PHE B 21 1776 3663 3759 67 174 -732 C ATOM 1799 CD1 PHE B 21 -4.191 12.736 66.272 1.00 25.33 C ANISOU 1799 CD1 PHE B 21 2003 3783 3840 24 105 -720 C ATOM 1800 CD2 PHE B 21 -4.859 14.705 67.441 1.00 24.46 C ANISOU 1800 CD2 PHE B 21 1876 3641 3777 154 220 -681 C ATOM 1801 CE1 PHE B 21 -2.920 13.250 66.117 1.00 25.53 C ANISOU 1801 CE1 PHE B 21 2167 3736 3798 68 81 -657 C ATOM 1802 CE2 PHE B 21 -3.586 15.225 67.287 1.00 21.90 C ANISOU 1802 CE2 PHE B 21 1696 3244 3382 194 193 -619 C ATOM 1803 CZ PHE B 21 -2.616 14.493 66.624 1.00 24.93 C ANISOU 1803 CZ PHE B 21 2152 3610 3711 151 123 -607 C ATOM 1804 N ASP B 22 -9.743 12.581 65.837 1.00 30.47 N ANISOU 1804 N ASP B 22 2016 4782 4779 47 115 -886 N ATOM 1805 CA ASP B 22 -11.015 11.938 66.163 1.00 31.03 C ANISOU 1805 CA ASP B 22 1987 4892 4910 -23 151 -922 C ATOM 1806 C ASP B 22 -11.489 10.925 65.115 1.00 33.07 C ANISOU 1806 C ASP B 22 2191 5218 5157 -83 49 -951 C ATOM 1807 O ASP B 22 -12.524 10.289 65.285 1.00 37.62 O ANISOU 1807 O ASP B 22 2685 5830 5780 -148 69 -982 O ATOM 1808 CB ASP B 22 -12.090 12.990 66.467 1.00 33.98 C ANISOU 1808 CB ASP B 22 2265 5300 5347 73 194 -898 C ATOM 1809 CG ASP B 22 -11.696 13.905 67.624 1.00 38.73 C ANISOU 1809 CG ASP B 22 2936 5823 5957 120 314 -874 C ATOM 1810 OD1 ASP B 22 -10.740 13.566 68.360 1.00 38.49 O ANISOU 1810 OD1 ASP B 22 3017 5712 5896 54 378 -885 O ATOM 1811 OD2 ASP B 22 -12.337 14.962 67.800 1.00 37.04 O ANISOU 1811 OD2 ASP B 22 2671 5623 5779 221 346 -842 O ATOM 1812 N ILE B 23 -10.718 10.765 64.044 1.00 33.57 N ANISOU 1812 N ILE B 23 2307 5293 5155 -64 -57 -938 N ATOM 1813 CA ILE B 23 -11.020 9.759 63.032 1.00 31.99 C ANISOU 1813 CA ILE B 23 2083 5143 4930 -128 -150 -965 C ATOM 1814 C ILE B 23 -10.563 8.370 63.484 1.00 30.20 C ANISOU 1814 C ILE B 23 1932 4862 4681 -270 -106 -1006 C ATOM 1815 O ILE B 23 -11.078 7.353 63.020 1.00 30.76 O ANISOU 1815 O ILE B 23 1977 4963 4750 -349 -143 -1038 O ATOM 1816 CB ILE B 23 -10.340 10.090 61.690 1.00 31.81 C ANISOU 1816 CB ILE B 23 2106 5143 4836 -54 -274 -933 C ATOM 1817 CG1 ILE B 23 -8.821 10.038 61.840 1.00 31.85 C ANISOU 1817 CG1 ILE B 23 2248 5074 4780 -61 -262 -919 C ATOM 1818 CG2 ILE B 23 -10.772 11.458 61.183 1.00 34.74 C ANISOU 1818 CG2 ILE B 23 2422 5559 5221 91 -321 -884 C ATOM 1819 CD1 ILE B 23 -8.075 10.517 60.616 1.00 32.78 C ANISOU 1819 CD1 ILE B 23 2424 5204 4827 24 -370 -881 C ATOM 1820 N LEU B 24 -9.595 8.333 64.392 1.00 28.67 N ANISOU 1820 N LEU B 24 1840 4585 4470 -303 -26 -1002 N ATOM 1821 CA LEU B 24 -8.982 7.073 64.814 1.00 27.05 C ANISOU 1821 CA LEU B 24 1734 4313 4232 -428 14 -1027 C ATOM 1822 C LEU B 24 -9.935 6.191 65.615 1.00 27.63 C ANISOU 1822 C LEU B 24 1771 4378 4349 -529 94 -1067 C ATOM 1823 O LEU B 24 -10.788 6.694 66.351 1.00 27.26 O ANISOU 1823 O LEU B 24 1650 4345 4364 -510 163 -1072 O ATOM 1824 CB LEU B 24 -7.728 7.351 65.637 1.00 23.00 C ANISOU 1824 CB LEU B 24 1339 3709 3692 -434 80 -1004 C ATOM 1825 CG LEU B 24 -6.627 8.123 64.911 1.00 22.10 C ANISOU 1825 CG LEU B 24 1275 3591 3530 -344 8 -965 C ATOM 1826 CD1 LEU B 24 -5.701 8.776 65.910 1.00 20.21 C ANISOU 1826 CD1 LEU B 24 1168 3247 3265 -316 87 -910 C ATOM 1827 CD2 LEU B 24 -5.868 7.204 63.957 1.00 23.69 C ANISOU 1827 CD2 LEU B 24 1553 3781 3665 -390 -74 -967 C ATOM 1828 N LYS B 25 -9.779 4.877 65.478 1.00 30.51 N ANISOU 1828 N LYS B 25 2197 4715 4681 -631 88 -1092 N ATOM 1829 CA LYS B 25 -10.648 3.940 66.179 1.00 37.88 C ANISOU 1829 CA LYS B 25 3108 5637 5648 -727 159 -1129 C ATOM 1830 C LYS B 25 -10.375 3.943 67.679 1.00 35.59 C ANISOU 1830 C LYS B 25 2893 5260 5370 -768 289 -1127 C ATOM 1831 O LYS B 25 -11.201 3.484 68.468 1.00 35.50 O ANISOU 1831 O LYS B 25 2853 5238 5396 -827 366 -1154 O ATOM 1832 CB LYS B 25 -10.526 2.522 65.608 1.00 43.81 C ANISOU 1832 CB LYS B 25 3916 6376 6353 -817 120 -1151 C ATOM 1833 CG LYS B 25 -9.258 1.772 65.980 1.00 46.05 C ANISOU 1833 CG LYS B 25 4366 6561 6571 -869 154 -1135 C ATOM 1834 CD LYS B 25 -9.452 0.273 65.747 1.00 51.63 C ANISOU 1834 CD LYS B 25 5119 7248 7249 -964 152 -1160 C ATOM 1835 CE LYS B 25 -8.132 -0.488 65.736 1.00 54.60 C ANISOU 1835 CE LYS B 25 5658 7537 7552 -994 157 -1132 C ATOM 1836 NZ LYS B 25 -7.395 -0.390 67.031 1.00 56.34 N ANISOU 1836 NZ LYS B 25 5983 7665 7760 -1005 251 -1106 N ATOM 1837 N ASP B 26 -9.214 4.466 68.061 1.00 34.24 N ANISOU 1837 N ASP B 26 2822 5024 5164 -739 312 -1094 N ATOM 1838 CA ASP B 26 -8.866 4.624 69.468 1.00 36.15 C ANISOU 1838 CA ASP B 26 3148 5178 5409 -770 430 -1084 C ATOM 1839 C ASP B 26 -8.013 5.878 69.626 1.00 36.27 C ANISOU 1839 C ASP B 26 3195 5169 5418 -687 436 -1044 C ATOM 1840 O ASP B 26 -6.789 5.798 69.715 1.00 32.42 O ANISOU 1840 O ASP B 26 2824 4615 4879 -700 430 -1016 O ATOM 1841 CB ASP B 26 -8.125 3.387 69.987 1.00 40.86 C ANISOU 1841 CB ASP B 26 3894 5684 5948 -865 466 -1083 C ATOM 1842 CG ASP B 26 -7.849 3.450 71.486 1.00 45.74 C ANISOU 1842 CG ASP B 26 4611 6208 6562 -901 584 -1071 C ATOM 1843 OD1 ASP B 26 -8.529 4.223 72.198 1.00 45.56 O ANISOU 1843 OD1 ASP B 26 4530 6191 6589 -876 654 -1078 O ATOM 1844 OD2 ASP B 26 -6.949 2.718 71.953 1.00 45.58 O ANISOU 1844 OD2 ASP B 26 4735 6103 6482 -949 605 -1049 O ATOM 1845 N PRO B 27 -8.667 7.050 69.641 1.00 33.34 N ANISOU 1845 N PRO B 27 2720 4848 5098 -595 447 -1036 N ATOM 1846 CA PRO B 27 -7.957 8.331 69.684 1.00 29.72 C ANISOU 1846 CA PRO B 27 2282 4375 4635 -497 450 -997 C ATOM 1847 C PRO B 27 -7.266 8.513 71.022 1.00 29.33 C ANISOU 1847 C PRO B 27 2360 4216 4568 -536 564 -975 C ATOM 1848 O PRO B 27 -7.724 7.967 72.027 1.00 31.02 O ANISOU 1848 O PRO B 27 2605 4385 4797 -615 656 -997 O ATOM 1849 CB PRO B 27 -9.081 9.367 69.531 1.00 32.32 C ANISOU 1849 CB PRO B 27 2479 4777 5024 -394 451 -993 C ATOM 1850 CG PRO B 27 -10.269 8.598 69.005 1.00 37.90 C ANISOU 1850 CG PRO B 27 3079 5558 5764 -436 408 -1029 C ATOM 1851 CD PRO B 27 -10.126 7.229 69.587 1.00 35.70 C ANISOU 1851 CD PRO B 27 2880 5221 5462 -573 456 -1060 C ATOM 1852 N PRO B 28 -6.175 9.282 71.042 1.00 27.43 N ANISOU 1852 N PRO B 28 2248 3910 4264 -465 539 -908 N ATOM 1853 CA PRO B 28 -5.473 9.534 72.303 1.00 26.49 C ANISOU 1853 CA PRO B 28 2280 3676 4109 -492 630 -872 C ATOM 1854 C PRO B 28 -6.366 10.343 73.236 1.00 27.25 C ANISOU 1854 C PRO B 28 2328 3768 4258 -460 739 -882 C ATOM 1855 O PRO B 28 -7.005 11.301 72.802 1.00 23.40 O ANISOU 1855 O PRO B 28 1740 3342 3808 -356 723 -877 O ATOM 1856 CB PRO B 28 -4.260 10.356 71.869 1.00 26.97 C ANISOU 1856 CB PRO B 28 2452 3693 4102 -404 561 -799 C ATOM 1857 CG PRO B 28 -4.675 10.999 70.579 1.00 29.09 C ANISOU 1857 CG PRO B 28 2606 4059 4388 -297 466 -796 C ATOM 1858 CD PRO B 28 -5.607 10.038 69.913 1.00 27.23 C ANISOU 1858 CD PRO B 28 2230 3917 4200 -353 429 -862 C ATOM 1859 N LYS B 29 -6.428 9.945 74.501 1.00 34.03 N ANISOU 1859 N LYS B 29 3261 4552 5118 -547 852 -897 N ATOM 1860 CA LYS B 29 -7.258 10.649 75.467 1.00 38.53 C ANISOU 1860 CA LYS B 29 3800 5105 5735 -525 972 -909 C ATOM 1861 C LYS B 29 -6.547 11.908 75.948 1.00 33.14 C ANISOU 1861 C LYS B 29 3241 4348 5003 -439 993 -845 C ATOM 1862 O LYS B 29 -7.184 12.888 76.338 1.00 35.44 O ANISOU 1862 O LYS B 29 3492 4643 5329 -368 1061 -841 O ATOM 1863 CB LYS B 29 -7.606 9.733 76.642 1.00 41.75 C ANISOU 1863 CB LYS B 29 4266 5451 6148 -648 1077 -943 C ATOM 1864 CG LYS B 29 -8.479 8.547 76.251 1.00 43.54 C ANISOU 1864 CG LYS B 29 4405 5735 6402 -713 1039 -991 C ATOM 1865 CD LYS B 29 -8.726 7.615 77.429 1.00 40.94 C ANISOU 1865 CD LYS B 29 4175 5328 6053 -816 1124 -1012 C ATOM 1866 CE LYS B 29 -9.588 6.431 77.014 1.00 38.11 C ANISOU 1866 CE LYS B 29 3734 5025 5720 -875 1091 -1059 C ATOM 1867 NZ LYS B 29 -9.009 5.695 75.854 1.00 34.53 N ANISOU 1867 NZ LYS B 29 3272 4614 5235 -890 974 -1059 N ATOM 1868 N LYS B 30 -5.221 11.870 75.913 1.00 26.75 N ANISOU 1868 N LYS B 30 2581 3469 4114 -448 937 -794 N ATOM 1869 CA LYS B 30 -4.402 13.014 76.294 1.00 28.64 C ANISOU 1869 CA LYS B 30 2948 3636 4300 -376 943 -731 C ATOM 1870 C LYS B 30 -3.158 13.101 75.419 1.00 25.51 C ANISOU 1870 C LYS B 30 2623 3229 3842 -339 822 -679 C ATOM 1871 O LYS B 30 -2.612 12.077 75.001 1.00 24.23 O ANISOU 1871 O LYS B 30 2481 3069 3658 -404 764 -684 O ATOM 1872 CB LYS B 30 -3.973 12.904 77.757 1.00 34.65 C ANISOU 1872 CB LYS B 30 3865 4281 5021 -455 1044 -719 C ATOM 1873 CG LYS B 30 -5.107 12.952 78.747 1.00 41.23 C ANISOU 1873 CG LYS B 30 4655 5106 5907 -489 1181 -763 C ATOM 1874 CD LYS B 30 -4.582 13.081 80.167 1.00 45.88 C ANISOU 1874 CD LYS B 30 5424 5570 6440 -550 1275 -741 C ATOM 1875 CE LYS B 30 -3.647 14.271 80.301 1.00 47.11 C ANISOU 1875 CE LYS B 30 5705 5662 6532 -474 1247 -675 C ATOM 1876 NZ LYS B 30 -3.527 14.714 81.717 1.00 49.15 N ANISOU 1876 NZ LYS B 30 6112 5813 6751 -512 1359 -662 N ATOM 1877 N LEU B 31 -2.712 14.322 75.146 1.00 19.65 N ANISOU 1877 N LEU B 31 1922 2472 3073 -235 792 -628 N ATOM 1878 CA LEU B 31 -1.463 14.530 74.433 1.00 21.06 C ANISOU 1878 CA LEU B 31 2183 2628 3192 -198 693 -573 C ATOM 1879 C LEU B 31 -0.567 15.494 75.198 1.00 22.17 C ANISOU 1879 C LEU B 31 2477 2670 3278 -173 723 -515 C ATOM 1880 O LEU B 31 -0.986 16.593 75.569 1.00 25.73 O ANISOU 1880 O LEU B 31 2932 3108 3738 -104 778 -504 O ATOM 1881 CB LEU B 31 -1.723 15.041 73.014 1.00 25.11 C ANISOU 1881 CB LEU B 31 2587 3232 3721 -91 599 -568 C ATOM 1882 CG LEU B 31 -2.312 14.044 72.008 1.00 23.38 C ANISOU 1882 CG LEU B 31 2235 3110 3537 -118 533 -616 C ATOM 1883 CD1 LEU B 31 -2.781 14.763 70.755 1.00 18.44 C ANISOU 1883 CD1 LEU B 31 1500 2575 2930 -1 452 -611 C ATOM 1884 CD2 LEU B 31 -1.305 12.953 71.649 1.00 20.10 C ANISOU 1884 CD2 LEU B 31 1893 2666 3077 -196 472 -608 C ATOM 1885 N TYR B 32 0.662 15.067 75.451 1.00 17.26 N ANISOU 1885 N TYR B 32 1982 1976 2599 -231 690 -477 N ATOM 1886 CA TYR B 32 1.628 15.907 76.135 1.00 17.01 C ANISOU 1886 CA TYR B 32 2100 1852 2512 -218 704 -419 C ATOM 1887 C TYR B 32 2.401 16.683 75.085 1.00 16.57 C ANISOU 1887 C TYR B 32 2054 1813 2430 -126 612 -369 C ATOM 1888 O TYR B 32 2.564 16.213 73.960 1.00 19.53 O ANISOU 1888 O TYR B 32 2362 2247 2813 -105 531 -373 O ATOM 1889 CB TYR B 32 2.536 15.053 77.017 1.00 17.35 C ANISOU 1889 CB TYR B 32 2271 1810 2513 -330 714 -402 C ATOM 1890 CG TYR B 32 1.694 14.222 77.955 1.00 15.99 C ANISOU 1890 CG TYR B 32 2083 1625 2366 -421 806 -456 C ATOM 1891 CD1 TYR B 32 1.226 12.973 77.574 1.00 16.28 C ANISOU 1891 CD1 TYR B 32 2035 1714 2437 -482 795 -504 C ATOM 1892 CD2 TYR B 32 1.315 14.716 79.191 1.00 21.13 C ANISOU 1892 CD2 TYR B 32 2807 2213 3008 -445 909 -461 C ATOM 1893 CE1 TYR B 32 0.420 12.221 78.417 1.00 18.72 C ANISOU 1893 CE1 TYR B 32 2328 2011 2772 -568 885 -554 C ATOM 1894 CE2 TYR B 32 0.508 13.975 80.045 1.00 20.73 C ANISOU 1894 CE2 TYR B 32 2745 2150 2982 -528 1003 -511 C ATOM 1895 CZ TYR B 32 0.066 12.725 79.648 1.00 22.09 C ANISOU 1895 CZ TYR B 32 2828 2375 3191 -590 990 -558 C ATOM 1896 OH TYR B 32 -0.737 11.978 80.484 1.00 28.73 O ANISOU 1896 OH TYR B 32 3658 3202 4057 -676 1087 -608 O ATOM 1897 N CYS B 33 2.849 17.881 75.440 1.00 16.50 N ANISOU 1897 N CYS B 33 2132 1748 2388 -72 630 -325 N ATOM 1898 CA CYS B 33 3.460 18.772 74.462 1.00 14.98 C ANISOU 1898 CA CYS B 33 1948 1570 2174 24 556 -279 C ATOM 1899 C CYS B 33 4.624 19.574 75.017 1.00 16.68 C ANISOU 1899 C CYS B 33 2315 1689 2332 22 555 -217 C ATOM 1900 O CYS B 33 4.641 19.960 76.187 1.00 17.90 O ANISOU 1900 O CYS B 33 2562 1771 2466 -15 627 -211 O ATOM 1901 CB CYS B 33 2.414 19.748 73.923 1.00 13.87 C ANISOU 1901 CB CYS B 33 1708 1493 2070 138 573 -294 C ATOM 1902 SG CYS B 33 1.646 20.739 75.238 1.00 23.38 S ANISOU 1902 SG CYS B 33 2960 2640 3284 155 703 -303 S ATOM 1903 N VAL B 34 5.589 19.832 74.152 1.00 18.44 N ANISOU 1903 N VAL B 34 2565 1913 2529 62 473 -172 N ATOM 1904 CA VAL B 34 6.629 20.800 74.436 1.00 19.66 C ANISOU 1904 CA VAL B 34 2844 1991 2636 80 463 -112 C ATOM 1905 C VAL B 34 6.828 21.612 73.162 1.00 14.59 C ANISOU 1905 C VAL B 34 2163 1391 1989 190 402 -84 C ATOM 1906 O VAL B 34 6.903 21.053 72.061 1.00 17.11 O ANISOU 1906 O VAL B 34 2407 1772 2321 212 335 -90 O ATOM 1907 CB VAL B 34 7.943 20.132 74.888 1.00 21.33 C ANISOU 1907 CB VAL B 34 3156 2134 2812 -12 426 -75 C ATOM 1908 CG1 VAL B 34 8.452 19.163 73.836 1.00 25.43 C ANISOU 1908 CG1 VAL B 34 3617 2701 3342 -21 347 -72 C ATOM 1909 CG2 VAL B 34 8.991 21.186 75.192 1.00 20.95 C ANISOU 1909 CG2 VAL B 34 3231 2010 2719 3 413 -14 C ATOM 1910 N GLY B 35 6.870 22.932 73.304 1.00 17.71 N ANISOU 1910 N GLY B 35 2615 1750 2364 258 429 -55 N ATOM 1911 CA GLY B 35 7.059 23.802 72.161 1.00 20.02 C ANISOU 1911 CA GLY B 35 2886 2072 2647 364 379 -25 C ATOM 1912 C GLY B 35 5.820 24.579 71.760 1.00 20.96 C ANISOU 1912 C GLY B 35 2919 2249 2796 471 410 -50 C ATOM 1913 O GLY B 35 4.913 24.798 72.562 1.00 27.41 O ANISOU 1913 O GLY B 35 3718 3060 3636 471 488 -80 O ATOM 1914 N ASP B 36 5.789 24.976 70.494 1.00 22.52 N ANISOU 1914 N ASP B 36 3063 2502 2994 564 348 -35 N ATOM 1915 CA ASP B 36 4.816 25.925 69.970 1.00 21.66 C ANISOU 1915 CA ASP B 36 2887 2439 2904 685 362 -42 C ATOM 1916 C ASP B 36 3.530 25.247 69.493 1.00 24.96 C ANISOU 1916 C ASP B 36 3145 2961 3379 708 350 -98 C ATOM 1917 O ASP B 36 3.442 24.788 68.361 1.00 24.49 O ANISOU 1917 O ASP B 36 3007 2973 3325 738 272 -106 O ATOM 1918 CB ASP B 36 5.463 26.714 68.829 1.00 26.40 C ANISOU 1918 CB ASP B 36 3519 3042 3469 774 297 6 C ATOM 1919 CG ASP B 36 4.517 27.699 68.186 1.00 33.35 C ANISOU 1919 CG ASP B 36 4336 3970 4365 908 300 5 C ATOM 1920 OD1 ASP B 36 3.477 28.014 68.800 1.00 34.11 O ANISOU 1920 OD1 ASP B 36 4384 4078 4497 936 367 -23 O ATOM 1921 OD2 ASP B 36 4.827 28.166 67.066 1.00 35.04 O ANISOU 1921 OD2 ASP B 36 4549 4210 4555 976 235 35 O ATOM 1922 N THR B 37 2.528 25.199 70.365 1.00 25.64 N ANISOU 1922 N THR B 37 3184 3053 3506 692 430 -137 N ATOM 1923 CA THR B 37 1.271 24.525 70.049 1.00 25.24 C ANISOU 1923 CA THR B 37 2974 3098 3516 700 428 -193 C ATOM 1924 C THR B 37 0.476 25.234 68.955 1.00 26.35 C ANISOU 1924 C THR B 37 3011 3319 3681 834 383 -191 C ATOM 1925 O THR B 37 -0.514 24.700 68.459 1.00 24.22 O ANISOU 1925 O THR B 37 2598 3142 3461 850 357 -233 O ATOM 1926 CB THR B 37 0.374 24.378 71.295 1.00 25.24 C ANISOU 1926 CB THR B 37 2950 3081 3559 654 537 -234 C ATOM 1927 OG1 THR B 37 -0.032 25.675 71.741 1.00 23.21 O ANISOU 1927 OG1 THR B 37 2729 2784 3304 740 609 -214 O ATOM 1928 CG2 THR B 37 1.120 23.661 72.416 1.00 26.21 C ANISOU 1928 CG2 THR B 37 3183 3122 3653 520 580 -235 C ATOM 1929 N LYS B 38 0.902 26.434 68.571 1.00 28.89 N ANISOU 1929 N LYS B 38 3404 3606 3966 930 372 -141 N ATOM 1930 CA LYS B 38 0.214 27.152 67.502 1.00 29.34 C ANISOU 1930 CA LYS B 38 3376 3734 4039 1064 324 -132 C ATOM 1931 C LYS B 38 0.419 26.486 66.141 1.00 29.12 C ANISOU 1931 C LYS B 38 3284 3782 3997 1074 207 -135 C ATOM 1932 O LYS B 38 -0.318 26.752 65.193 1.00 30.88 O ANISOU 1932 O LYS B 38 3413 4081 4240 1156 151 -139 O ATOM 1933 CB LYS B 38 0.648 28.617 67.455 1.00 34.73 C ANISOU 1933 CB LYS B 38 4167 4349 4681 1140 341 -78 C ATOM 1934 CG LYS B 38 0.070 29.465 68.576 1.00 41.67 C ANISOU 1934 CG LYS B 38 5080 5174 5579 1152 447 -81 C ATOM 1935 CD LYS B 38 -1.457 29.483 68.522 1.00 51.17 C ANISOU 1935 CD LYS B 38 6129 6455 6858 1205 470 -123 C ATOM 1936 CE LYS B 38 -2.045 30.293 69.673 1.00 56.30 C ANISOU 1936 CE LYS B 38 6816 7049 7527 1214 582 -130 C ATOM 1937 NZ LYS B 38 -3.535 30.385 69.608 1.00 59.90 N ANISOU 1937 NZ LYS B 38 7118 7579 8064 1268 605 -169 N ATOM 1938 N LEU B 39 1.409 25.606 66.050 1.00 24.20 N ANISOU 1938 N LEU B 39 2720 3133 3341 978 169 -132 N ATOM 1939 CA LEU B 39 1.673 24.902 64.801 1.00 23.57 C ANISOU 1939 CA LEU B 39 2596 3115 3243 978 67 -136 C ATOM 1940 C LEU B 39 0.525 23.965 64.428 1.00 23.19 C ANISOU 1940 C LEU B 39 2391 3171 3248 958 34 -197 C ATOM 1941 O LEU B 39 0.384 23.577 63.273 1.00 26.08 O ANISOU 1941 O LEU B 39 2697 3607 3604 985 -55 -206 O ATOM 1942 CB LEU B 39 2.990 24.127 64.883 1.00 16.98 C ANISOU 1942 CB LEU B 39 1860 2223 2368 877 47 -119 C ATOM 1943 CG LEU B 39 4.268 24.965 64.867 1.00 20.09 C ANISOU 1943 CG LEU B 39 2398 2530 2707 899 49 -54 C ATOM 1944 CD1 LEU B 39 5.490 24.097 65.146 1.00 19.28 C ANISOU 1944 CD1 LEU B 39 2374 2371 2579 790 38 -40 C ATOM 1945 CD2 LEU B 39 4.419 25.698 63.535 1.00 27.71 C ANISOU 1945 CD2 LEU B 39 3365 3524 3637 1006 -19 -21 C ATOM 1946 N LEU B 40 -0.302 23.612 65.406 1.00 20.67 N ANISOU 1946 N LEU B 40 2009 2862 2984 907 106 -239 N ATOM 1947 CA LEU B 40 -1.418 22.703 65.154 1.00 25.06 C ANISOU 1947 CA LEU B 40 2411 3514 3598 875 83 -300 C ATOM 1948 C LEU B 40 -2.511 23.359 64.312 1.00 31.76 C ANISOU 1948 C LEU B 40 3133 4453 4480 998 37 -305 C ATOM 1949 O LEU B 40 -3.414 22.684 63.822 1.00 31.62 O ANISOU 1949 O LEU B 40 2979 4529 4506 986 -9 -351 O ATOM 1950 CB LEU B 40 -1.995 22.180 66.470 1.00 25.60 C ANISOU 1950 CB LEU B 40 2450 3561 3717 786 184 -342 C ATOM 1951 CG LEU B 40 -1.048 21.261 67.237 1.00 22.53 C ANISOU 1951 CG LEU B 40 2165 3097 3298 653 216 -345 C ATOM 1952 CD1 LEU B 40 -1.472 21.084 68.699 1.00 18.86 C ANISOU 1952 CD1 LEU B 40 1715 2583 2867 580 332 -371 C ATOM 1953 CD2 LEU B 40 -0.929 19.920 66.539 1.00 21.01 C ANISOU 1953 CD2 LEU B 40 1923 2957 3103 575 143 -379 C ATOM 1954 N ASP B 41 -2.421 24.676 64.146 1.00 32.54 N ANISOU 1954 N ASP B 41 3281 4524 4559 1115 47 -258 N ATOM 1955 CA ASP B 41 -3.434 25.422 63.408 1.00 37.96 C ANISOU 1955 CA ASP B 41 3898 5254 5273 1183 12 -235 C ATOM 1956 C ASP B 41 -3.007 25.700 61.974 1.00 38.55 C ANISOU 1956 C ASP B 41 4018 5341 5288 1212 -94 -194 C ATOM 1957 O ASP B 41 -3.757 26.289 61.196 1.00 38.10 O ANISOU 1957 O ASP B 41 3912 5320 5242 1268 -137 -175 O ATOM 1958 CB ASP B 41 -3.750 26.736 64.117 1.00 38.35 C ANISOU 1958 CB ASP B 41 3991 5238 5341 1246 97 -203 C ATOM 1959 CG ASP B 41 -4.318 26.520 65.498 1.00 43.97 C ANISOU 1959 CG ASP B 41 4657 5937 6111 1220 214 -245 C ATOM 1960 OD1 ASP B 41 -5.026 25.509 65.691 1.00 47.78 O ANISOU 1960 OD1 ASP B 41 5016 6491 6646 1168 219 -302 O ATOM 1961 OD2 ASP B 41 -4.051 27.353 66.390 1.00 44.63 O ANISOU 1961 OD2 ASP B 41 4835 5936 6184 1240 302 -225 O ATOM 1962 N THR B 42 -1.797 25.278 61.629 1.00 33.36 N ANISOU 1962 N THR B 42 4706 3885 4085 731 -192 354 N ATOM 1963 CA THR B 42 -1.293 25.459 60.277 1.00 34.25 C ANISOU 1963 CA THR B 42 4855 4039 4121 756 -207 421 C ATOM 1964 C THR B 42 -2.207 24.754 59.283 1.00 35.51 C ANISOU 1964 C THR B 42 5021 4254 4217 790 -216 418 C ATOM 1965 O THR B 42 -2.518 23.572 59.444 1.00 37.87 O ANISOU 1965 O THR B 42 5314 4583 4490 819 -189 344 O ATOM 1966 CB THR B 42 0.140 24.935 60.133 1.00 32.51 C ANISOU 1966 CB THR B 42 4661 3847 3844 777 -177 408 C ATOM 1967 OG1 THR B 42 0.968 25.537 61.137 1.00 36.82 O ANISOU 1967 OG1 THR B 42 5198 4339 4454 744 -169 402 O ATOM 1968 CG2 THR B 42 0.691 25.271 58.755 1.00 32.56 C ANISOU 1968 CG2 THR B 42 4701 3909 3762 785 -191 493 C ATOM 1969 N PRO B 43 -2.651 25.490 58.255 1.00 36.26 N ANISOU 1969 N PRO B 43 5124 4367 4286 781 -255 501 N ATOM 1970 CA PRO B 43 -3.598 24.998 57.250 1.00 36.94 C ANISOU 1970 CA PRO B 43 5211 4509 4315 804 -272 510 C ATOM 1971 C PRO B 43 -3.134 23.696 56.604 1.00 39.78 C ANISOU 1971 C PRO B 43 5581 4954 4578 847 -240 467 C ATOM 1972 O PRO B 43 -3.888 22.721 56.568 1.00 39.99 O ANISOU 1972 O PRO B 43 5596 5009 4590 880 -227 405 O ATOM 1973 CB PRO B 43 -3.610 26.123 56.215 1.00 40.11 C ANISOU 1973 CB PRO B 43 5626 4926 4690 768 -320 623 C ATOM 1974 CG PRO B 43 -3.278 27.344 57.003 1.00 39.26 C ANISOU 1974 CG PRO B 43 5510 4739 4669 729 -336 660 C ATOM 1975 CD PRO B 43 -2.275 26.893 58.019 1.00 36.89 C ANISOU 1975 CD PRO B 43 5211 4415 4391 738 -291 595 C ATOM 1976 N LEU B 44 -1.904 23.685 56.101 1.00 38.79 N ANISOU 1976 N LEU B 44 5476 4877 4387 845 -226 500 N ATOM 1977 CA LEU B 44 -1.371 22.509 55.425 1.00 35.07 C ANISOU 1977 CA LEU B 44 5003 4505 3817 880 -195 463 C ATOM 1978 C LEU B 44 -0.335 21.786 56.278 1.00 30.17 C ANISOU 1978 C LEU B 44 4385 3870 3207 911 -153 393 C ATOM 1979 O LEU B 44 0.743 22.311 56.543 1.00 26.56 O ANISOU 1979 O LEU B 44 3945 3392 2755 893 -144 422 O ATOM 1980 CB LEU B 44 -0.761 22.894 54.077 1.00 35.60 C ANISOU 1980 CB LEU B 44 5082 4669 3777 839 -206 547 C ATOM 1981 CG LEU B 44 -0.223 21.729 53.245 1.00 36.00 C ANISOU 1981 CG LEU B 44 5113 4851 3713 851 -172 505 C ATOM 1982 CD1 LEU B 44 -1.332 20.727 52.955 1.00 37.47 C ANISOU 1982 CD1 LEU B 44 5271 5077 3888 889 -173 443 C ATOM 1983 CD2 LEU B 44 0.402 22.229 51.953 1.00 35.45 C ANISOU 1983 CD2 LEU B 44 5047 4884 3537 780 -174 582 C ATOM 1984 N LYS B 45 -0.678 20.577 56.707 1.00 30.72 N ANISOU 1984 N LYS B 45 4438 3951 3283 956 -129 299 N ATOM 1985 CA LYS B 45 0.257 19.727 57.428 1.00 27.48 C ANISOU 1985 CA LYS B 45 4027 3536 2878 986 -95 224 C ATOM 1986 C LYS B 45 0.669 18.584 56.509 1.00 31.96 C ANISOU 1986 C LYS B 45 4576 4227 3340 1029 -80 191 C ATOM 1987 O LYS B 45 -0.185 17.863 55.988 1.00 36.32 O ANISOU 1987 O LYS B 45 5107 4834 3861 1048 -83 158 O ATOM 1988 CB LYS B 45 -0.389 19.181 58.705 1.00 24.12 C ANISOU 1988 CB LYS B 45 3588 3044 2533 970 -82 137 C ATOM 1989 CG LYS B 45 -0.913 20.258 59.646 1.00 28.40 C ANISOU 1989 CG LYS B 45 4126 3496 3167 906 -100 164 C ATOM 1990 CD LYS B 45 -1.497 19.661 60.908 1.00 29.88 C ANISOU 1990 CD LYS B 45 4289 3652 3414 859 -92 95 C ATOM 1991 CE LYS B 45 -2.075 20.742 61.817 1.00 31.30 C ANISOU 1991 CE LYS B 45 4447 3763 3681 801 -109 122 C ATOM 1992 NZ LYS B 45 -3.210 21.465 61.181 1.00 27.97 N ANISOU 1992 NZ LYS B 45 4025 3333 3268 809 -136 170 N ATOM 1993 N VAL B 46 1.974 18.429 56.297 1.00 27.96 N ANISOU 1993 N VAL B 46 4063 3774 2788 1010 -54 183 N ATOM 1994 CA VAL B 46 2.483 17.378 55.421 1.00 29.14 C ANISOU 1994 CA VAL B 46 4157 4049 2866 977 -15 111 C ATOM 1995 C VAL B 46 3.404 16.438 56.182 1.00 26.47 C ANISOU 1995 C VAL B 46 3791 3694 2575 989 22 5 C ATOM 1996 O VAL B 46 4.371 16.871 56.801 1.00 25.06 O ANISOU 1996 O VAL B 46 3622 3460 2438 972 33 9 O ATOM 1997 CB VAL B 46 3.242 17.965 54.215 1.00 28.55 C ANISOU 1997 CB VAL B 46 4069 4073 2705 894 -1 171 C ATOM 1998 CG1 VAL B 46 3.677 16.860 53.260 1.00 27.20 C ANISOU 1998 CG1 VAL B 46 3836 4038 2458 859 40 91 C ATOM 1999 CG2 VAL B 46 2.379 18.980 53.498 1.00 33.93 C ANISOU 1999 CG2 VAL B 46 4785 4763 3345 879 -45 285 C ATOM 2000 N ALA B 47 3.097 15.149 56.141 1.00 25.22 N ANISOU 2000 N ALA B 47 3595 3578 2410 1018 38 -90 N ATOM 2001 CA ALA B 47 3.932 14.164 56.803 1.00 24.78 C ANISOU 2001 CA ALA B 47 3485 3487 2444 978 46 -165 C ATOM 2002 C ALA B 47 5.063 13.757 55.875 1.00 22.96 C ANISOU 2002 C ALA B 47 3200 3362 2163 917 87 -207 C ATOM 2003 O ALA B 47 4.833 13.476 54.703 1.00 25.68 O ANISOU 2003 O ALA B 47 3512 3810 2436 887 99 -210 O ATOM 2004 CB ALA B 47 3.111 12.950 57.194 1.00 24.83 C ANISOU 2004 CB ALA B 47 3448 3462 2526 941 10 -196 C ATOM 2005 N ILE B 48 6.290 13.744 56.386 1.00 13.07 N ANISOU 2005 N ILE B 48 1935 2081 950 889 106 -238 N ATOM 2006 CA ILE B 48 7.401 13.172 55.623 1.00 18.77 C ANISOU 2006 CA ILE B 48 2595 2891 1645 822 143 -293 C ATOM 2007 C ILE B 48 8.045 12.072 56.443 1.00 22.64 C ANISOU 2007 C ILE B 48 3038 3312 2250 779 134 -356 C ATOM 2008 O ILE B 48 8.699 12.333 57.450 1.00 21.86 O ANISOU 2008 O ILE B 48 2957 3135 2214 778 129 -357 O ATOM 2009 CB ILE B 48 8.450 14.217 55.222 1.00 19.98 C ANISOU 2009 CB ILE B 48 2774 3104 1713 807 183 -264 C ATOM 2010 CG1 ILE B 48 7.793 15.347 54.426 1.00 21.13 C ANISOU 2010 CG1 ILE B 48 2963 3290 1775 791 167 -150 C ATOM 2011 CG2 ILE B 48 9.553 13.572 54.402 1.00 20.39 C ANISOU 2011 CG2 ILE B 48 2755 3250 1743 730 220 -326 C ATOM 2012 CD1 ILE B 48 8.775 16.359 53.875 1.00 24.59 C ANISOU 2012 CD1 ILE B 48 3406 3765 2174 713 183 -83 C ATOM 2013 N ILE B 49 7.825 10.836 56.016 1.00 22.64 N ANISOU 2013 N ILE B 49 2986 3340 2276 738 131 -399 N ATOM 2014 CA ILE B 49 8.305 9.667 56.731 1.00 22.88 C ANISOU 2014 CA ILE B 49 2983 3308 2403 690 122 -441 C ATOM 2015 C ILE B 49 9.005 8.762 55.736 1.00 24.71 C ANISOU 2015 C ILE B 49 3159 3615 2614 644 152 -496 C ATOM 2016 O ILE B 49 8.794 8.879 54.528 1.00 28.81 O ANISOU 2016 O ILE B 49 3661 4233 3053 640 171 -500 O ATOM 2017 CB ILE B 49 7.143 8.879 57.356 1.00 23.08 C ANISOU 2017 CB ILE B 49 3011 3272 2486 684 85 -423 C ATOM 2018 CG1 ILE B 49 6.134 8.496 56.270 1.00 25.85 C ANISOU 2018 CG1 ILE B 49 3344 3693 2783 698 81 -424 C ATOM 2019 CG2 ILE B 49 6.474 9.691 58.450 1.00 23.98 C ANISOU 2019 CG2 ILE B 49 3177 3306 2628 713 54 -369 C ATOM 2020 CD1 ILE B 49 4.875 7.850 56.794 1.00 28.76 C ANISOU 2020 CD1 ILE B 49 3721 4013 3196 696 46 -403 C ATOM 2021 N GLY B 50 9.829 7.852 56.239 1.00 25.21 N ANISOU 2021 N GLY B 50 3198 3633 2746 605 156 -530 N ATOM 2022 CA GLY B 50 10.540 6.933 55.372 1.00 22.36 C ANISOU 2022 CA GLY B 50 2789 3333 2374 568 178 -580 C ATOM 2023 C GLY B 50 11.629 6.140 56.065 1.00 24.81 C ANISOU 2023 C GLY B 50 3077 3599 2750 548 173 -614 C ATOM 2024 O GLY B 50 11.769 6.177 57.288 1.00 22.89 O ANISOU 2024 O GLY B 50 2852 3284 2561 563 145 -601 O ATOM 2025 N THR B 51 12.405 5.423 55.262 1.00 26.11 N ANISOU 2025 N THR B 51 3194 3827 2901 523 188 -664 N ATOM 2026 CA THR B 51 13.485 4.584 55.756 1.00 25.10 C ANISOU 2026 CA THR B 51 3026 3688 2823 515 170 -711 C ATOM 2027 C THR B 51 14.474 5.341 56.638 1.00 23.84 C ANISOU 2027 C THR B 51 2893 3469 2695 512 183 -701 C ATOM 2028 O THR B 51 14.719 6.533 56.456 1.00 21.27 O ANISOU 2028 O THR B 51 2604 3140 2339 505 224 -675 O ATOM 2029 CB THR B 51 14.258 3.932 54.592 1.00 27.32 C ANISOU 2029 CB THR B 51 3246 4057 3077 484 191 -769 C ATOM 2030 OG1 THR B 51 15.362 3.181 55.111 1.00 23.67 O ANISOU 2030 OG1 THR B 51 2743 3584 2668 474 170 -818 O ATOM 2031 CG2 THR B 51 14.787 4.997 53.640 1.00 31.61 C ANISOU 2031 CG2 THR B 51 3803 4656 3553 456 249 -760 C ATOM 2032 N ARG B 52 15.039 4.631 57.603 1.00 22.81 N ANISOU 2032 N ARG B 52 2744 3297 2625 517 146 -724 N ATOM 2033 CA ARG B 52 16.061 5.200 58.459 1.00 22.93 C ANISOU 2033 CA ARG B 52 2778 3260 2676 514 153 -720 C ATOM 2034 C ARG B 52 17.433 5.210 57.786 1.00 29.94 C ANISOU 2034 C ARG B 52 3627 4196 3553 486 187 -768 C ATOM 2035 O ARG B 52 18.391 5.751 58.330 1.00 28.20 O ANISOU 2035 O ARG B 52 3418 3940 3356 481 199 -769 O ATOM 2036 CB ARG B 52 16.118 4.440 59.781 1.00 30.61 C ANISOU 2036 CB ARG B 52 3746 4175 3711 525 96 -723 C ATOM 2037 CG ARG B 52 14.849 4.584 60.609 1.00 27.22 C ANISOU 2037 CG ARG B 52 3359 3694 3289 548 63 -671 C ATOM 2038 CD ARG B 52 15.000 3.923 61.966 1.00 36.38 C ANISOU 2038 CD ARG B 52 4519 4804 4499 551 12 -670 C ATOM 2039 NE ARG B 52 15.143 2.479 61.847 1.00 40.90 N ANISOU 2039 NE ARG B 52 5039 5411 5090 544 -23 -718 N ATOM 2040 CZ ARG B 52 15.962 1.747 62.594 1.00 39.17 C ANISOU 2040 CZ ARG B 52 4792 5176 4914 535 -55 -748 C ATOM 2041 NH1 ARG B 52 16.025 0.436 62.409 1.00 38.88 N ANISOU 2041 NH1 ARG B 52 4704 5173 4896 529 -88 -794 N ATOM 2042 NH2 ARG B 52 16.716 2.325 63.522 1.00 37.67 N ANISOU 2042 NH2 ARG B 52 4624 4937 4752 532 -57 -733 N ATOM 2043 N ARG B 53 17.518 4.616 56.600 1.00 32.99 N ANISOU 2043 N ARG B 53 3966 4665 3904 466 200 -808 N ATOM 2044 CA ARG B 53 18.771 4.576 55.850 1.00 33.50 C ANISOU 2044 CA ARG B 53 3985 4790 3953 433 231 -858 C ATOM 2045 C ARG B 53 18.574 5.058 54.411 1.00 27.92 C ANISOU 2045 C ARG B 53 3269 4177 3164 409 278 -861 C ATOM 2046 O ARG B 53 18.656 4.269 53.466 1.00 25.66 O ANISOU 2046 O ARG B 53 2931 3961 2859 385 280 -900 O ATOM 2047 CB ARG B 53 19.359 3.162 55.853 1.00 36.69 C ANISOU 2047 CB ARG B 53 4314 5222 4404 421 191 -928 C ATOM 2048 CG ARG B 53 19.647 2.590 57.234 1.00 42.67 C ANISOU 2048 CG ARG B 53 5071 5907 5237 439 139 -934 C ATOM 2049 CD ARG B 53 20.619 3.461 58.017 1.00 49.86 C ANISOU 2049 CD ARG B 53 6009 6764 6171 438 153 -920 C ATOM 2050 NE ARG B 53 20.800 2.976 59.383 1.00 54.92 N ANISOU 2050 NE ARG B 53 6654 7336 6878 453 101 -917 N ATOM 2051 CZ ARG B 53 21.429 3.650 60.342 1.00 57.15 C ANISOU 2051 CZ ARG B 53 6967 7557 7189 458 100 -895 C ATOM 2052 NH1 ARG B 53 21.940 4.848 60.087 1.00 58.91 N ANISOU 2052 NH1 ARG B 53 7221 7775 7386 453 150 -876 N ATOM 2053 NH2 ARG B 53 21.540 3.131 61.559 1.00 57.11 N ANISOU 2053 NH2 ARG B 53 6963 7499 7237 467 50 -892 N ATOM 2054 N PRO B 54 18.308 6.359 54.238 1.00 23.46 N ANISOU 2054 N PRO B 54 2734 3638 2540 416 305 -832 N ATOM 2055 CA PRO B 54 18.098 6.905 52.892 1.00 21.65 C ANISOU 2055 CA PRO B 54 2482 3530 2212 388 341 -837 C ATOM 2056 C PRO B 54 19.381 6.903 52.081 1.00 24.14 C ANISOU 2056 C PRO B 54 2737 3935 2499 337 373 -894 C ATOM 2057 O PRO B 54 20.466 7.052 52.637 1.00 27.08 O ANISOU 2057 O PRO B 54 3098 4278 2913 330 379 -920 O ATOM 2058 CB PRO B 54 17.666 8.348 53.166 1.00 27.02 C ANISOU 2058 CB PRO B 54 3218 4208 2841 408 357 -784 C ATOM 2059 CG PRO B 54 18.216 8.659 54.519 1.00 26.73 C ANISOU 2059 CG PRO B 54 3212 4064 2879 434 344 -777 C ATOM 2060 CD PRO B 54 18.123 7.381 55.284 1.00 24.59 C ANISOU 2060 CD PRO B 54 2937 3704 2701 446 303 -786 C ATOM 2061 N THR B 55 19.252 6.727 50.772 1.00 24.78 N ANISOU 2061 N THR B 55 2778 4126 2512 297 394 -911 N ATOM 2062 CA THR B 55 20.376 6.896 49.870 1.00 23.13 C ANISOU 2062 CA THR B 55 2512 4017 2260 235 431 -958 C ATOM 2063 C THR B 55 20.664 8.384 49.797 1.00 23.29 C ANISOU 2063 C THR B 55 2563 4078 2207 213 471 -918 C ATOM 2064 O THR B 55 19.828 9.194 50.200 1.00 27.85 O ANISOU 2064 O THR B 55 3200 4625 2754 245 468 -855 O ATOM 2065 CB THR B 55 20.009 6.428 48.459 1.00 26.03 C ANISOU 2065 CB THR B 55 2836 4492 2562 194 443 -974 C ATOM 2066 OG1 THR B 55 18.870 7.168 48.007 1.00 22.95 O ANISOU 2066 OG1 THR B 55 2490 4138 2091 200 451 -907 O ATOM 2067 CG2 THR B 55 19.670 4.949 48.456 1.00 32.81 C ANISOU 2067 CG2 THR B 55 3662 5318 3485 213 405 -1012 C ATOM 2068 N PRO B 56 21.848 8.756 49.293 1.00 25.17 N ANISOU 2068 N PRO B 56 2759 4387 2417 154 508 -954 N ATOM 2069 CA PRO B 56 22.127 10.170 49.034 1.00 26.62 C ANISOU 2069 CA PRO B 56 2969 4630 2515 114 550 -907 C ATOM 2070 C PRO B 56 21.055 10.770 48.132 1.00 27.08 C ANISOU 2070 C PRO B 56 3059 4764 2464 93 560 -834 C ATOM 2071 O PRO B 56 20.654 11.916 48.324 1.00 30.35 O ANISOU 2071 O PRO B 56 3530 5184 2819 94 570 -759 O ATOM 2072 CB PRO B 56 23.468 10.125 48.304 1.00 32.19 C ANISOU 2072 CB PRO B 56 3609 5418 3204 37 586 -965 C ATOM 2073 CG PRO B 56 24.143 8.922 48.862 1.00 34.98 C ANISOU 2073 CG PRO B 56 3916 5706 3669 63 556 -1045 C ATOM 2074 CD PRO B 56 23.044 7.915 49.112 1.00 29.44 C ANISOU 2074 CD PRO B 56 3229 4944 3011 121 509 -1036 C ATOM 2075 N TYR B 57 20.593 9.993 47.159 1.00 25.08 N ANISOU 2075 N TYR B 57 2772 4569 2187 74 552 -852 N ATOM 2076 CA TYR B 57 19.512 10.429 46.281 1.00 26.88 C ANISOU 2076 CA TYR B 57 3030 4865 2320 57 553 -783 C ATOM 2077 C TYR B 57 18.265 10.842 47.070 1.00 26.96 C ANISOU 2077 C TYR B 57 3111 4798 2334 128 521 -716 C ATOM 2078 O TYR B 57 17.761 11.955 46.918 1.00 28.77 O ANISOU 2078 O TYR B 57 3391 5057 2483 116 527 -632 O ATOM 2079 CB TYR B 57 19.163 9.320 45.287 1.00 32.79 C ANISOU 2079 CB TYR B 57 3727 5667 3065 39 542 -826 C ATOM 2080 CG TYR B 57 17.849 9.524 44.571 1.00 34.17 C ANISOU 2080 CG TYR B 57 3933 5883 3166 42 529 -762 C ATOM 2081 CD1 TYR B 57 17.750 10.408 43.507 1.00 35.27 C ANISOU 2081 CD1 TYR B 57 4085 6124 3192 -25 552 -701 C ATOM 2082 CD2 TYR B 57 16.707 8.832 44.959 1.00 29.59 C ANISOU 2082 CD2 TYR B 57 3372 5239 2633 108 491 -757 C ATOM 2083 CE1 TYR B 57 16.553 10.601 42.851 1.00 36.88 C ANISOU 2083 CE1 TYR B 57 4319 6362 3331 -22 535 -639 C ATOM 2084 CE2 TYR B 57 15.505 9.016 44.306 1.00 29.27 C ANISOU 2084 CE2 TYR B 57 3358 5236 2529 111 477 -702 C ATOM 2085 CZ TYR B 57 15.435 9.903 43.251 1.00 32.82 C ANISOU 2085 CZ TYR B 57 3819 5786 2866 48 498 -643 C ATOM 2086 OH TYR B 57 14.246 10.097 42.592 1.00 31.24 O ANISOU 2086 OH TYR B 57 3646 5620 2604 50 479 -584 O ATOM 2087 N SER B 58 17.763 9.938 47.905 1.00 26.25 N ANISOU 2087 N SER B 58 3024 4609 2339 196 484 -747 N ATOM 2088 CA SER B 58 16.544 10.212 48.659 1.00 24.76 C ANISOU 2088 CA SER B 58 2897 4345 2164 262 452 -693 C ATOM 2089 C SER B 58 16.746 11.355 49.643 1.00 24.88 C ANISOU 2089 C SER B 58 2967 4309 2179 289 456 -648 C ATOM 2090 O SER B 58 15.854 12.180 49.848 1.00 25.88 O ANISOU 2090 O SER B 58 3149 4427 2259 319 442 -575 O ATOM 2091 CB SER B 58 16.059 8.952 49.379 1.00 26.83 C ANISOU 2091 CB SER B 58 3151 4508 2534 316 411 -733 C ATOM 2092 OG SER B 58 15.815 7.911 48.449 1.00 24.34 O ANISOU 2092 OG SER B 58 2788 4246 2215 293 406 -768 O ATOM 2093 N LYS B 59 17.932 11.410 50.237 1.00 26.15 N ANISOU 2093 N LYS B 59 3109 4436 2391 280 472 -692 N ATOM 2094 CA LYS B 59 18.267 12.477 51.169 1.00 26.86 C ANISOU 2094 CA LYS B 59 3243 4478 2483 303 480 -658 C ATOM 2095 C LYS B 59 18.196 13.863 50.522 1.00 29.16 C ANISOU 2095 C LYS B 59 3568 4864 2648 258 508 -572 C ATOM 2096 O LYS B 59 17.574 14.773 51.068 1.00 29.91 O ANISOU 2096 O LYS B 59 3725 4929 2712 299 493 -496 O ATOM 2097 CB LYS B 59 19.650 12.244 51.785 1.00 24.53 C ANISOU 2097 CB LYS B 59 2915 4140 2266 292 494 -724 C ATOM 2098 CG LYS B 59 20.069 13.322 52.772 1.00 29.91 C ANISOU 2098 CG LYS B 59 3638 4769 2958 316 503 -697 C ATOM 2099 CD LYS B 59 21.389 12.977 53.449 1.00 34.78 C ANISOU 2099 CD LYS B 59 4220 5329 3667 310 509 -766 C ATOM 2100 CE LYS B 59 21.752 14.012 54.508 1.00 42.15 C ANISOU 2100 CE LYS B 59 5196 6196 4622 342 513 -743 C ATOM 2101 NZ LYS B 59 23.103 13.763 55.085 1.00 44.08 N ANISOU 2101 NZ LYS B 59 5404 6392 4951 326 520 -808 N ATOM 2102 N GLN B 60 18.825 14.033 49.364 1.00 29.57 N ANISOU 2102 N GLN B 60 3583 5025 2627 170 543 -571 N ATOM 2103 CA GLN B 60 18.860 15.360 48.756 1.00 29.77 C ANISOU 2103 CA GLN B 60 3644 5131 2535 107 565 -471 C ATOM 2104 C GLN B 60 17.463 15.881 48.418 1.00 27.96 C ANISOU 2104 C GLN B 60 3473 4915 2235 128 531 -365 C ATOM 2105 O GLN B 60 17.166 17.048 48.638 1.00 27.91 O ANISOU 2105 O GLN B 60 3533 4851 2222 122 504 -247 O ATOM 2106 CB GLN B 60 19.806 15.425 47.550 1.00 35.50 C ANISOU 2106 CB GLN B 60 4322 5964 3203 0 606 -487 C ATOM 2107 CG GLN B 60 19.589 14.367 46.486 1.00 41.44 C ANISOU 2107 CG GLN B 60 5021 6774 3951 -23 603 -541 C ATOM 2108 CD GLN B 60 20.553 14.521 45.316 1.00 43.64 C ANISOU 2108 CD GLN B 60 5253 7158 4169 -127 643 -556 C ATOM 2109 OE1 GLN B 60 21.628 13.915 45.293 1.00 46.93 O ANISOU 2109 OE1 GLN B 60 5609 7585 4638 -149 664 -647 O ATOM 2110 NE2 GLN B 60 20.172 15.339 44.342 1.00 40.17 N ANISOU 2110 NE2 GLN B 60 4843 6795 3623 -191 647 -464 N ATOM 2111 N HIS B 61 16.593 15.009 47.928 1.00 28.37 N ANISOU 2111 N HIS B 61 3509 4973 2298 151 508 -390 N ATOM 2112 CA HIS B 61 15.242 15.430 47.581 1.00 28.40 C ANISOU 2112 CA HIS B 61 3563 4984 2243 174 471 -298 C ATOM 2113 C HIS B 61 14.324 15.589 48.800 1.00 29.46 C ANISOU 2113 C HIS B 61 3751 5012 2429 278 430 -268 C ATOM 2114 O HIS B 61 13.404 16.405 48.789 1.00 27.41 O ANISOU 2114 O HIS B 61 3553 4712 2152 293 390 -158 O ATOM 2115 CB HIS B 61 14.642 14.491 46.538 1.00 31.61 C ANISOU 2115 CB HIS B 61 3931 5442 2637 155 464 -334 C ATOM 2116 CG HIS B 61 15.366 14.522 45.229 1.00 35.03 C ANISOU 2116 CG HIS B 61 4322 5984 3002 56 498 -341 C ATOM 2117 ND1 HIS B 61 15.633 15.694 44.559 1.00 34.57 N ANISOU 2117 ND1 HIS B 61 4296 5990 2851 -19 509 -246 N ATOM 2118 CD2 HIS B 61 15.890 13.526 44.474 1.00 31.35 C ANISOU 2118 CD2 HIS B 61 3788 5570 2554 20 518 -427 C ATOM 2119 CE1 HIS B 61 16.286 15.422 43.441 1.00 34.61 C ANISOU 2119 CE1 HIS B 61 4253 6083 2816 -98 539 -280 C ATOM 2120 NE2 HIS B 61 16.452 14.115 43.368 1.00 34.88 N ANISOU 2120 NE2 HIS B 61 4224 6115 2915 -73 545 -391 N ATOM 2121 N THR B 62 14.582 14.826 49.856 1.00 28.28 N ANISOU 2121 N THR B 62 3585 4772 2389 339 426 -355 N ATOM 2122 CA THR B 62 13.836 15.006 51.089 1.00 23.90 C ANISOU 2122 CA THR B 62 3084 4089 1909 431 385 -328 C ATOM 2123 C THR B 62 14.134 16.401 51.624 1.00 25.53 C ANISOU 2123 C THR B 62 3350 4203 2146 414 365 -220 C ATOM 2124 O THR B 62 13.242 17.099 52.101 1.00 24.57 O ANISOU 2124 O THR B 62 3290 3993 2051 455 321 -133 O ATOM 2125 CB THR B 62 14.223 13.961 52.141 1.00 21.37 C ANISOU 2125 CB THR B 62 2733 3675 1710 481 380 -434 C ATOM 2126 OG1 THR B 62 13.818 12.666 51.686 1.00 23.95 O ANISOU 2126 OG1 THR B 62 3012 4005 2082 469 368 -493 O ATOM 2127 CG2 THR B 62 13.544 14.265 53.491 1.00 20.56 C ANISOU 2127 CG2 THR B 62 2693 3442 1678 573 342 -405 C ATOM 2128 N ILE B 63 15.397 16.804 51.521 1.00 29.25 N ANISOU 2128 N ILE B 63 3802 4697 2616 353 398 -230 N ATOM 2129 CA ILE B 63 15.816 18.130 51.959 1.00 32.01 C ANISOU 2129 CA ILE B 63 4202 4967 2991 328 384 -133 C ATOM 2130 C ILE B 63 15.075 19.223 51.192 1.00 33.46 C ANISOU 2130 C ILE B 63 4437 5174 3102 289 358 4 C ATOM 2131 O ILE B 63 14.574 20.178 51.782 1.00 34.79 O ANISOU 2131 O ILE B 63 4669 5239 3312 316 317 98 O ATOM 2132 CB ILE B 63 17.339 18.312 51.810 1.00 30.88 C ANISOU 2132 CB ILE B 63 4020 4866 2847 258 430 -174 C ATOM 2133 CG1 ILE B 63 18.072 17.493 52.873 1.00 25.42 C ANISOU 2133 CG1 ILE B 63 3295 4109 2255 308 441 -290 C ATOM 2134 CG2 ILE B 63 17.723 19.786 51.909 1.00 32.16 C ANISOU 2134 CG2 ILE B 63 4235 4976 3009 212 420 -58 C ATOM 2135 CD1 ILE B 63 19.573 17.559 52.762 1.00 33.57 C ANISOU 2135 CD1 ILE B 63 4280 5180 3293 246 486 -345 C ATOM 2136 N THR B 64 14.995 19.079 49.876 1.00 34.53 N ANISOU 2136 N THR B 64 4545 5444 3130 225 379 13 N ATOM 2137 CA THR B 64 14.294 20.066 49.062 1.00 33.28 C ANISOU 2137 CA THR B 64 4434 5315 2895 183 351 143 C ATOM 2138 C THR B 64 12.790 20.106 49.363 1.00 33.96 C ANISOU 2138 C THR B 64 4566 5335 3003 259 294 195 C ATOM 2139 O THR B 64 12.211 21.184 49.508 1.00 33.20 O ANISOU 2139 O THR B 64 4530 5168 2915 265 251 310 O ATOM 2140 CB THR B 64 14.548 19.846 47.559 1.00 35.04 C ANISOU 2140 CB THR B 64 4617 5704 2992 93 386 137 C ATOM 2141 OG1 THR B 64 15.943 20.033 47.287 1.00 36.97 O ANISOU 2141 OG1 THR B 64 4828 6003 3217 14 437 104 O ATOM 2142 CG2 THR B 64 13.738 20.837 46.730 1.00 33.01 C ANISOU 2142 CG2 THR B 64 4414 5473 2656 53 349 276 C ATOM 2143 N LEU B 65 12.165 18.936 49.473 1.00 35.01 N ANISOU 2143 N LEU B 65 4667 5487 3148 318 295 108 N ATOM 2144 CA LEU B 65 10.739 18.865 49.793 1.00 33.53 C ANISOU 2144 CA LEU B 65 4515 5239 2985 392 245 144 C ATOM 2145 C LEU B 65 10.416 19.552 51.120 1.00 30.90 C ANISOU 2145 C LEU B 65 4240 4744 2758 457 206 191 C ATOM 2146 O LEU B 65 9.477 20.344 51.206 1.00 29.66 O ANISOU 2146 O LEU B 65 4134 4527 2607 481 159 287 O ATOM 2147 CB LEU B 65 10.261 17.413 49.819 1.00 33.53 C ANISOU 2147 CB LEU B 65 4468 5279 2991 445 258 28 C ATOM 2148 CG LEU B 65 10.094 16.720 48.466 1.00 37.24 C ANISOU 2148 CG LEU B 65 4889 5905 3354 397 283 -8 C ATOM 2149 CD1 LEU B 65 9.990 15.208 48.631 1.00 35.63 C ANISOU 2149 CD1 LEU B 65 4626 5706 3207 433 298 -141 C ATOM 2150 CD2 LEU B 65 8.875 17.272 47.743 1.00 39.62 C ANISOU 2150 CD2 LEU B 65 5230 6232 3591 395 240 93 C ATOM 2151 N ALA B 66 11.199 19.245 52.150 1.00 29.91 N ANISOU 2151 N ALA B 66 4102 4547 2715 485 224 122 N ATOM 2152 CA ALA B 66 10.971 19.789 53.482 1.00 28.44 C ANISOU 2152 CA ALA B 66 3965 4211 2632 546 191 151 C ATOM 2153 C ALA B 66 11.156 21.305 53.516 1.00 32.44 C ANISOU 2153 C ALA B 66 4525 4660 3143 508 169 275 C ATOM 2154 O ALA B 66 10.312 22.031 54.041 1.00 31.57 O ANISOU 2154 O ALA B 66 4466 4454 3074 550 123 349 O ATOM 2155 CB ALA B 66 11.898 19.124 54.485 1.00 21.81 C ANISOU 2155 CB ALA B 66 3097 3318 1870 573 217 49 C ATOM 2156 N ARG B 67 12.269 21.777 52.964 1.00 29.68 N ANISOU 2156 N ARG B 67 4159 4367 2750 429 201 293 N ATOM 2157 CA ARG B 67 12.565 23.206 52.969 1.00 35.32 C ANISOU 2157 CA ARG B 67 4921 5031 3468 386 182 408 C ATOM 2158 C ARG B 67 11.523 23.992 52.183 1.00 37.05 C ANISOU 2158 C ARG B 67 5182 5268 3628 370 139 525 C ATOM 2159 O ARG B 67 10.973 24.981 52.670 1.00 39.47 O ANISOU 2159 O ARG B 67 5543 5474 3981 395 94 615 O ATOM 2160 CB ARG B 67 13.961 23.476 52.402 1.00 40.21 C ANISOU 2160 CB ARG B 67 5511 5725 4043 295 230 399 C ATOM 2161 CG ARG B 67 15.079 22.836 53.199 1.00 48.84 C ANISOU 2161 CG ARG B 67 6563 6792 5200 307 268 289 C ATOM 2162 CD ARG B 67 16.452 23.159 52.624 1.00 58.59 C ANISOU 2162 CD ARG B 67 7768 8101 6393 215 315 280 C ATOM 2163 NE ARG B 67 16.787 24.576 52.740 1.00 66.07 N ANISOU 2163 NE ARG B 67 8765 8988 7350 174 299 392 N ATOM 2164 CZ ARG B 67 17.066 25.189 53.888 1.00 70.05 C ANISOU 2164 CZ ARG B 67 9302 9365 7949 209 281 412 C ATOM 2165 NH1 ARG B 67 17.035 24.515 55.032 1.00 68.85 N ANISOU 2165 NH1 ARG B 67 9142 9131 7886 286 276 331 N ATOM 2166 NH2 ARG B 67 17.365 26.482 53.892 1.00 72.16 N ANISOU 2166 NH2 ARG B 67 9612 9586 8220 166 268 514 N ATOM 2167 N GLU B 68 11.245 23.543 50.967 1.00 37.01 N ANISOU 2167 N GLU B 68 5150 5390 3523 328 151 522 N ATOM 2168 CA GLU B 68 10.337 24.268 50.093 1.00 41.46 C ANISOU 2168 CA GLU B 68 5751 5984 4020 303 110 634 C ATOM 2169 C GLU B 68 8.908 24.277 50.624 1.00 41.08 C ANISOU 2169 C GLU B 68 5735 5850 4022 391 54 661 C ATOM 2170 O GLU B 68 8.178 25.245 50.429 1.00 43.36 O ANISOU 2170 O GLU B 68 6073 6095 4307 391 4 771 O ATOM 2171 CB GLU B 68 10.396 23.708 48.673 1.00 46.27 C ANISOU 2171 CB GLU B 68 6319 6755 4506 237 137 616 C ATOM 2172 CG GLU B 68 11.706 23.996 47.963 1.00 52.99 C ANISOU 2172 CG GLU B 68 7146 7695 5292 134 186 618 C ATOM 2173 CD GLU B 68 12.030 25.478 47.929 1.00 58.82 C ANISOU 2173 CD GLU B 68 7940 8379 6031 82 161 746 C ATOM 2174 OE1 GLU B 68 11.211 26.257 47.392 1.00 58.82 O ANISOU 2174 OE1 GLU B 68 7985 8373 5991 69 113 858 O ATOM 2175 OE2 GLU B 68 13.101 25.864 48.447 1.00 61.01 O ANISOU 2175 OE2 GLU B 68 8215 8616 6351 56 189 733 O ATOM 2176 N LEU B 69 8.509 23.205 51.299 1.00 35.41 N ANISOU 2176 N LEU B 69 4992 5106 3355 464 62 561 N ATOM 2177 CA LEU B 69 7.176 23.162 51.878 1.00 37.09 C ANISOU 2177 CA LEU B 69 5235 5237 3621 547 14 576 C ATOM 2178 C LEU B 69 7.086 24.139 53.044 1.00 37.94 C ANISOU 2178 C LEU B 69 5393 5194 3829 586 -19 631 C ATOM 2179 O LEU B 69 6.088 24.839 53.199 1.00 40.19 O ANISOU 2179 O LEU B 69 5720 5411 4140 620 -70 707 O ATOM 2180 CB LEU B 69 6.799 21.742 52.301 1.00 35.90 C ANISOU 2180 CB LEU B 69 5044 5099 3497 610 33 453 C ATOM 2181 CG LEU B 69 6.251 20.886 51.160 1.00 34.12 C ANISOU 2181 CG LEU B 69 4781 5004 3180 594 42 420 C ATOM 2182 CD1 LEU B 69 5.933 19.479 51.634 1.00 32.93 C ANISOU 2182 CD1 LEU B 69 4591 4859 3062 656 61 296 C ATOM 2183 CD2 LEU B 69 5.013 21.546 50.573 1.00 32.49 C ANISOU 2183 CD2 LEU B 69 4612 4797 2937 602 -12 519 C ATOM 2184 N ALA B 70 8.145 24.198 53.847 1.00 41.50 N ANISOU 2184 N ALA B 70 5839 5593 4337 581 10 591 N ATOM 2185 CA ALA B 70 8.215 25.154 54.947 1.00 40.13 C ANISOU 2185 CA ALA B 70 5711 5281 4257 610 -16 639 C ATOM 2186 C ALA B 70 8.179 26.581 54.413 1.00 42.97 C ANISOU 2186 C ALA B 70 6112 5622 4590 560 -49 773 C ATOM 2187 O ALA B 70 7.439 27.424 54.916 1.00 44.57 O ANISOU 2187 O ALA B 70 6360 5725 4849 597 -97 844 O ATOM 2188 CB ALA B 70 9.470 24.923 55.779 1.00 42.32 C ANISOU 2188 CB ALA B 70 5969 5522 4589 604 24 570 C ATOM 2189 N LYS B 71 8.982 26.850 53.388 1.00 46.45 N ANISOU 2189 N LYS B 71 6540 6161 4949 473 -23 807 N ATOM 2190 CA LYS B 71 8.965 28.156 52.744 1.00 50.86 C ANISOU 2190 CA LYS B 71 7138 6715 5470 415 -55 937 C ATOM 2191 C LYS B 71 7.541 28.509 52.322 1.00 50.52 C ANISOU 2191 C LYS B 71 7126 6657 5411 447 -115 1013 C ATOM 2192 O LYS B 71 7.092 29.638 52.497 1.00 52.27 O ANISOU 2192 O LYS B 71 7371 6787 5704 421 -169 1076 O ATOM 2193 CB LYS B 71 9.901 28.177 51.531 1.00 54.62 C ANISOU 2193 CB LYS B 71 7590 7324 5840 312 -16 952 C ATOM 2194 CG LYS B 71 9.787 29.441 50.695 1.00 59.62 C ANISOU 2194 CG LYS B 71 8266 7968 6418 245 -51 1092 C ATOM 2195 CD LYS B 71 10.686 29.394 49.469 1.00 63.13 C ANISOU 2195 CD LYS B 71 8685 8552 6748 139 -9 1102 C ATOM 2196 CE LYS B 71 12.152 29.479 49.854 1.00 65.13 C ANISOU 2196 CE LYS B 71 8917 8806 7025 93 46 1056 C ATOM 2197 NZ LYS B 71 13.020 29.629 48.653 1.00 67.86 N ANISOU 2197 NZ LYS B 71 9243 9281 7260 -20 85 1078 N ATOM 2198 N ASN B 72 6.829 27.529 51.777 1.00 46.36 N ANISOU 2198 N ASN B 72 6518 5936 5162 545 111 20 N ATOM 2199 CA ASN B 72 5.460 27.743 51.322 1.00 45.19 C ANISOU 2199 CA ASN B 72 6379 5813 4980 633 52 -10 C ATOM 2200 C ASN B 72 4.433 27.722 52.457 1.00 48.71 C ANISOU 2200 C ASN B 72 6774 6246 5489 632 17 -54 C ATOM 2201 O ASN B 72 3.235 27.562 52.217 1.00 48.34 O ANISOU 2201 O ASN B 72 6701 6233 5433 696 -37 -101 O ATOM 2202 CB ASN B 72 5.088 26.725 50.241 1.00 44.62 C ANISOU 2202 CB ASN B 72 6273 5815 4866 684 16 -59 C ATOM 2203 CG ASN B 72 5.685 27.069 48.888 1.00 45.27 C ANISOU 2203 CG ASN B 72 6428 5914 4857 726 39 -14 C ATOM 2204 OD1 ASN B 72 4.998 27.591 48.013 1.00 47.09 O ANISOU 2204 OD1 ASN B 72 6711 6164 5017 813 6 -7 O ATOM 2205 ND2 ASN B 72 6.969 26.782 48.712 1.00 40.06 N ANISOU 2205 ND2 ASN B 72 5774 5251 4197 667 97 18 N ATOM 2206 N GLY B 73 4.911 27.878 53.689 1.00 49.54 N ANISOU 2206 N GLY B 73 6863 6304 5656 560 47 -42 N ATOM 2207 CA GLY B 73 4.038 27.984 54.847 1.00 47.96 C ANISOU 2207 CA GLY B 73 6626 6085 5512 554 25 -75 C ATOM 2208 C GLY B 73 3.378 26.692 55.301 1.00 44.56 C ANISOU 2208 C GLY B 73 6102 5698 5132 542 -2 -146 C ATOM 2209 O GLY B 73 2.361 26.720 55.999 1.00 45.21 O ANISOU 2209 O GLY B 73 6150 5780 5250 558 -26 -183 O ATOM 2210 N ALA B 74 3.948 25.557 54.913 1.00 36.92 N ANISOU 2210 N ALA B 74 5095 4765 4170 513 6 -167 N ATOM 2211 CA ALA B 74 3.440 24.267 55.373 1.00 34.45 C ANISOU 2211 CA ALA B 74 4698 4481 3910 492 -10 -232 C ATOM 2212 C ALA B 74 4.191 23.812 56.627 1.00 30.11 C ANISOU 2212 C ALA B 74 4122 3899 3421 411 27 -223 C ATOM 2213 O ALA B 74 5.324 24.233 56.858 1.00 30.26 O ANISOU 2213 O ALA B 74 4175 3887 3433 370 63 -174 O ATOM 2214 CB ALA B 74 3.569 23.229 54.272 1.00 31.88 C ANISOU 2214 CB ALA B 74 4345 4209 3559 511 -25 -267 C ATOM 2215 N VAL B 75 3.558 22.967 57.439 1.00 26.48 N ANISOU 2215 N VAL B 75 3601 3444 3018 390 20 -270 N ATOM 2216 CA VAL B 75 4.246 22.357 58.577 1.00 25.89 C ANISOU 2216 CA VAL B 75 3502 3343 2993 322 53 -264 C ATOM 2217 C VAL B 75 4.548 20.886 58.287 1.00 25.64 C ANISOU 2217 C VAL B 75 3421 3338 2983 301 56 -300 C ATOM 2218 O VAL B 75 3.709 20.154 57.756 1.00 24.93 O ANISOU 2218 O VAL B 75 3291 3281 2902 327 30 -354 O ATOM 2219 CB VAL B 75 3.457 22.501 59.902 1.00 27.95 C ANISOU 2219 CB VAL B 75 3742 3578 3301 307 55 -281 C ATOM 2220 CG1 VAL B 75 2.076 21.874 59.776 1.00 32.43 C ANISOU 2220 CG1 VAL B 75 4253 4176 3895 337 29 -344 C ATOM 2221 CG2 VAL B 75 4.234 21.879 61.070 1.00 23.99 C ANISOU 2221 CG2 VAL B 75 3226 3050 2840 245 88 -270 C ATOM 2222 N ILE B 76 5.759 20.465 58.623 1.00 20.89 N ANISOU 2222 N ILE B 76 2822 2722 2391 255 85 -275 N ATOM 2223 CA ILE B 76 6.202 19.108 58.330 1.00 20.52 C ANISOU 2223 CA ILE B 76 2738 2696 2363 238 91 -304 C ATOM 2224 C ILE B 76 5.999 18.237 59.562 1.00 23.25 C ANISOU 2224 C ILE B 76 3048 3018 2769 199 105 -325 C ATOM 2225 O ILE B 76 6.498 18.565 60.637 1.00 23.10 O ANISOU 2225 O ILE B 76 3043 2967 2766 167 125 -294 O ATOM 2226 CB ILE B 76 7.694 19.087 57.940 1.00 20.98 C ANISOU 2226 CB ILE B 76 2818 2757 2397 216 117 -266 C ATOM 2227 CG1 ILE B 76 7.919 19.890 56.655 1.00 23.68 C ANISOU 2227 CG1 ILE B 76 3201 3121 2674 253 113 -241 C ATOM 2228 CG2 ILE B 76 8.187 17.653 57.773 1.00 20.14 C ANISOU 2228 CG2 ILE B 76 2673 2667 2314 200 124 -297 C ATOM 2229 CD1 ILE B 76 7.098 19.410 55.499 1.00 27.43 C ANISOU 2229 CD1 ILE B 76 3662 3639 3120 306 81 -286 C ATOM 2230 N VAL B 77 5.276 17.131 59.400 1.00 19.15 N ANISOU 2230 N VAL B 77 2483 2512 2280 203 95 -378 N ATOM 2231 CA VAL B 77 4.988 16.224 60.511 1.00 20.16 C ANISOU 2231 CA VAL B 77 2581 2613 2467 168 115 -397 C ATOM 2232 C VAL B 77 5.741 14.909 60.358 1.00 19.47 C ANISOU 2232 C VAL B 77 2476 2523 2398 147 129 -411 C ATOM 2233 O VAL B 77 5.678 14.255 59.312 1.00 21.90 O ANISOU 2233 O VAL B 77 2765 2859 2698 165 114 -447 O ATOM 2234 CB VAL B 77 3.480 15.915 60.609 1.00 21.23 C ANISOU 2234 CB VAL B 77 2675 2755 2638 179 102 -452 C ATOM 2235 CG1 VAL B 77 3.190 15.018 61.808 1.00 23.68 C ANISOU 2235 CG1 VAL B 77 2960 3030 3005 138 134 -465 C ATOM 2236 CG2 VAL B 77 2.683 17.196 60.693 1.00 20.09 C ANISOU 2236 CG2 VAL B 77 2544 2616 2473 210 84 -444 C ATOM 2237 N SER B 78 6.448 14.501 61.403 1.00 19.84 N ANISOU 2237 N SER B 78 2531 2539 2469 114 155 -385 N ATOM 2238 CA SER B 78 7.181 13.247 61.328 1.00 19.13 C ANISOU 2238 CA SER B 78 2428 2442 2398 101 169 -397 C ATOM 2239 C SER B 78 7.408 12.663 62.719 1.00 12.66 C ANISOU 2239 C SER B 78 1614 1581 1614 71 196 -380 C ATOM 2240 O SER B 78 6.863 13.160 63.697 1.00 17.42 O ANISOU 2240 O SER B 78 2227 2164 2230 60 205 -366 O ATOM 2241 CB SER B 78 8.502 13.451 60.581 1.00 18.61 C ANISOU 2241 CB SER B 78 2380 2400 2293 109 167 -370 C ATOM 2242 OG SER B 78 8.981 12.229 60.060 1.00 17.93 O ANISOU 2242 OG SER B 78 2274 2320 2218 112 172 -397 O ATOM 2243 N GLY B 79 8.211 11.610 62.804 1.00 19.83 N ANISOU 2243 N GLY B 79 2520 2477 2537 64 208 -380 N ATOM 2244 CA GLY B 79 8.433 10.929 64.063 1.00 15.24 C ANISOU 2244 CA GLY B 79 1949 1855 1985 45 233 -364 C ATOM 2245 C GLY B 79 9.828 11.065 64.646 1.00 18.11 C ANISOU 2245 C GLY B 79 2336 2215 2328 43 236 -321 C ATOM 2246 O GLY B 79 10.175 10.349 65.577 1.00 18.72 O ANISOU 2246 O GLY B 79 2427 2263 2424 37 252 -308 O ATOM 2247 N GLY B 80 10.626 11.976 64.105 1.00 18.80 N ANISOU 2247 N GLY B 80 2429 2334 2381 49 222 -301 N ATOM 2248 CA GLY B 80 11.974 12.204 64.605 1.00 18.76 C ANISOU 2248 CA GLY B 80 2435 2333 2360 45 222 -268 C ATOM 2249 C GLY B 80 12.924 11.018 64.491 1.00 18.04 C ANISOU 2249 C GLY B 80 2333 2241 2279 55 227 -274 C ATOM 2250 O GLY B 80 13.971 10.985 65.145 1.00 18.82 O ANISOU 2250 O GLY B 80 2437 2341 2374 56 226 -252 O ATOM 2251 N ALA B 81 12.571 10.044 63.661 1.00 18.96 N ANISOU 2251 N ALA B 81 2433 2359 2412 67 230 -309 N ATOM 2252 CA ALA B 81 13.418 8.864 63.463 1.00 16.20 C ANISOU 2252 CA ALA B 81 2076 2006 2074 82 235 -320 C ATOM 2253 C ALA B 81 14.710 9.187 62.734 1.00 16.25 C ANISOU 2253 C ALA B 81 2068 2055 2052 94 229 -311 C ATOM 2254 O ALA B 81 14.801 10.188 62.028 1.00 18.61 O ANISOU 2254 O ALA B 81 2363 2386 2321 89 225 -303 O ATOM 2255 CB ALA B 81 12.664 7.791 62.697 1.00 14.64 C ANISOU 2255 CB ALA B 81 1864 1797 1901 90 239 -367 C ATOM 2256 N LEU B 82 15.701 8.315 62.896 1.00 17.12 N ANISOU 2256 N LEU B 82 2171 2164 2171 110 232 -312 N ATOM 2257 CA LEU B 82 16.897 8.351 62.065 1.00 23.64 C ANISOU 2257 CA LEU B 82 2974 3032 2977 124 232 -315 C ATOM 2258 C LEU B 82 16.503 8.387 60.583 1.00 20.85 C ANISOU 2258 C LEU B 82 2609 2708 2603 133 234 -343 C ATOM 2259 O LEU B 82 15.456 7.872 60.196 1.00 21.87 O ANISOU 2259 O LEU B 82 2742 2821 2745 137 231 -375 O ATOM 2260 CB LEU B 82 17.742 7.108 62.333 1.00 34.40 C ANISOU 2260 CB LEU B 82 4328 4383 4358 151 235 -325 C ATOM 2261 CG LEU B 82 19.244 7.189 62.067 1.00 41.46 C ANISOU 2261 CG LEU B 82 5195 5320 5238 166 234 -319 C ATOM 2262 CD1 LEU B 82 19.881 8.233 62.969 1.00 42.59 C ANISOU 2262 CD1 LEU B 82 5335 5476 5373 146 225 -286 C ATOM 2263 CD2 LEU B 82 19.886 5.830 62.289 1.00 45.31 C ANISOU 2263 CD2 LEU B 82 5678 5791 5746 203 234 -336 C ATOM 2264 N GLY B 83 17.341 8.993 59.752 1.00 19.79 N ANISOU 2264 N GLY B 83 2461 2619 2438 136 241 -335 N ATOM 2265 CA GLY B 83 17.108 8.969 58.317 1.00 17.81 C ANISOU 2265 CA GLY B 83 2206 2402 2159 152 244 -361 C ATOM 2266 C GLY B 83 16.124 9.997 57.806 1.00 15.04 C ANISOU 2266 C GLY B 83 1874 2060 1780 145 237 -354 C ATOM 2267 O GLY B 83 16.227 11.180 58.106 1.00 20.04 O ANISOU 2267 O GLY B 83 2521 2697 2399 126 240 -318 O ATOM 2268 N VAL B 84 15.164 9.539 57.012 1.00 19.77 N ANISOU 2268 N VAL B 84 2474 2663 2374 164 225 -394 N ATOM 2269 CA VAL B 84 14.216 10.437 56.358 1.00 19.14 C ANISOU 2269 CA VAL B 84 2410 2600 2262 170 212 -394 C ATOM 2270 C VAL B 84 13.525 11.404 57.322 1.00 17.29 C ANISOU 2270 C VAL B 84 2192 2338 2039 147 205 -365 C ATOM 2271 O VAL B 84 13.497 12.610 57.086 1.00 18.89 O ANISOU 2271 O VAL B 84 2416 2553 2209 145 206 -334 O ATOM 2272 CB VAL B 84 13.148 9.644 55.586 1.00 24.34 C ANISOU 2272 CB VAL B 84 3060 3264 2925 194 192 -453 C ATOM 2273 CG1 VAL B 84 12.001 10.555 55.179 1.00 25.09 C ANISOU 2273 CG1 VAL B 84 3168 3372 2994 205 170 -457 C ATOM 2274 CG2 VAL B 84 13.770 8.959 54.377 1.00 25.33 C ANISOU 2274 CG2 VAL B 84 3176 3426 3021 224 196 -484 C ATOM 2275 N ASP B 85 12.961 10.869 58.397 1.00 16.48 N ANISOU 2275 N ASP B 85 2084 2195 1982 132 202 -373 N ATOM 2276 CA ASP B 85 12.270 11.693 59.397 1.00 20.01 C ANISOU 2276 CA ASP B 85 2546 2616 2441 113 198 -350 C ATOM 2277 C ASP B 85 13.069 12.927 59.825 1.00 18.00 C ANISOU 2277 C ASP B 85 2310 2365 2164 96 206 -300 C ATOM 2278 O ASP B 85 12.633 14.064 59.635 1.00 18.62 O ANISOU 2278 O ASP B 85 2409 2448 2219 96 201 -281 O ATOM 2279 CB ASP B 85 11.959 10.865 60.649 1.00 21.26 C ANISOU 2279 CB ASP B 85 2700 2730 2648 96 205 -355 C ATOM 2280 CG ASP B 85 10.734 9.976 60.492 1.00 26.03 C ANISOU 2280 CG ASP B 85 3288 3317 3285 99 201 -404 C ATOM 2281 OD1 ASP B 85 10.391 9.598 59.347 1.00 26.02 O ANISOU 2281 OD1 ASP B 85 3272 3341 3275 118 189 -444 O ATOM 2282 OD2 ASP B 85 10.119 9.649 61.536 1.00 26.38 O ANISOU 2282 OD2 ASP B 85 3335 3323 3366 82 212 -403 O ATOM 2283 N ILE B 86 14.236 12.702 60.417 1.00 18.34 N ANISOU 2283 N ILE B 86 2347 2405 2217 83 218 -280 N ATOM 2284 CA ILE B 86 14.977 13.793 61.046 1.00 20.36 C ANISOU 2284 CA ILE B 86 2614 2658 2463 60 223 -241 C ATOM 2285 C ILE B 86 15.614 14.732 60.019 1.00 20.03 C ANISOU 2285 C ILE B 86 2580 2647 2385 58 236 -221 C ATOM 2286 O ILE B 86 15.837 15.910 60.296 1.00 18.57 O ANISOU 2286 O ILE B 86 2412 2454 2188 37 241 -192 O ATOM 2287 CB ILE B 86 16.042 13.262 62.045 1.00 16.05 C ANISOU 2287 CB ILE B 86 2055 2104 1940 50 226 -232 C ATOM 2288 CG1 ILE B 86 16.435 14.347 63.056 1.00 16.69 C ANISOU 2288 CG1 ILE B 86 2149 2173 2021 24 223 -202 C ATOM 2289 CG2 ILE B 86 17.250 12.699 61.310 1.00 19.26 C ANISOU 2289 CG2 ILE B 86 2434 2543 2339 61 237 -240 C ATOM 2290 CD1 ILE B 86 15.333 14.670 64.048 1.00 14.29 C ANISOU 2290 CD1 ILE B 86 1870 1834 1728 19 214 -198 C ATOM 2291 N ILE B 87 15.906 14.216 58.831 1.00 19.42 N ANISOU 2291 N ILE B 87 2491 2602 2287 79 244 -238 N ATOM 2292 CA ILE B 87 16.393 15.064 57.751 1.00 18.48 C ANISOU 2292 CA ILE B 87 2385 2512 2125 81 263 -218 C ATOM 2293 C ILE B 87 15.326 16.097 57.400 1.00 19.55 C ANISOU 2293 C ILE B 87 2558 2638 2233 90 253 -205 C ATOM 2294 O ILE B 87 15.615 17.286 57.286 1.00 20.75 O ANISOU 2294 O ILE B 87 2736 2784 2363 75 268 -169 O ATOM 2295 CB ILE B 87 16.722 14.239 56.499 1.00 20.10 C ANISOU 2295 CB ILE B 87 2576 2756 2306 110 272 -244 C ATOM 2296 CG1 ILE B 87 18.025 13.465 56.710 1.00 21.63 C ANISOU 2296 CG1 ILE B 87 2733 2964 2520 104 288 -251 C ATOM 2297 CG2 ILE B 87 16.820 15.150 55.284 1.00 21.24 C ANISOU 2297 CG2 ILE B 87 2748 2928 2395 122 291 -223 C ATOM 2298 CD1 ILE B 87 18.197 12.282 55.780 1.00 23.23 C ANISOU 2298 CD1 ILE B 87 2919 3195 2714 138 291 -290 C ATOM 2299 N ALA B 88 14.092 15.629 57.233 1.00 23.34 N ANISOU 2299 N ALA B 88 3039 3115 2716 116 228 -236 N ATOM 2300 CA ALA B 88 12.976 16.495 56.871 1.00 22.01 C ANISOU 2300 CA ALA B 88 2900 2942 2522 137 211 -232 C ATOM 2301 C ALA B 88 12.650 17.473 57.985 1.00 23.97 C ANISOU 2301 C ALA B 88 3167 3152 2788 113 209 -205 C ATOM 2302 O ALA B 88 12.412 18.657 57.740 1.00 22.67 O ANISOU 2302 O ALA B 88 3038 2979 2595 119 210 -177 O ATOM 2303 CB ALA B 88 11.748 15.663 56.531 1.00 24.58 C ANISOU 2303 CB ALA B 88 3208 3276 2856 167 183 -283 C ATOM 2304 N GLN B 89 12.640 16.985 59.219 1.00 22.14 N ANISOU 2304 N GLN B 89 2917 2895 2601 90 206 -212 N ATOM 2305 CA GLN B 89 12.301 17.855 60.331 1.00 22.10 C ANISOU 2305 CA GLN B 89 2930 2856 2610 71 203 -191 C ATOM 2306 C GLN B 89 13.370 18.934 60.531 1.00 21.30 C ANISOU 2306 C GLN B 89 2850 2745 2497 43 221 -151 C ATOM 2307 O GLN B 89 13.041 20.105 60.711 1.00 25.84 O ANISOU 2307 O GLN B 89 3458 3300 3061 39 220 -129 O ATOM 2308 CB GLN B 89 12.037 17.050 61.608 1.00 17.85 C ANISOU 2308 CB GLN B 89 2373 2295 2115 57 199 -208 C ATOM 2309 CG GLN B 89 10.914 16.032 61.444 1.00 17.73 C ANISOU 2309 CG GLN B 89 2336 2280 2120 77 188 -249 C ATOM 2310 CD GLN B 89 10.252 15.664 62.747 1.00 22.89 C ANISOU 2310 CD GLN B 89 2985 2902 2810 64 190 -257 C ATOM 2311 OE1 GLN B 89 10.351 14.528 63.210 1.00 28.85 O ANISOU 2311 OE1 GLN B 89 3724 3645 3593 57 199 -272 O ATOM 2312 NE2 GLN B 89 9.555 16.624 63.343 1.00 16.10 N ANISOU 2312 NE2 GLN B 89 2144 2025 1948 62 187 -246 N ATOM 2313 N GLU B 90 14.644 18.561 60.470 1.00 21.98 N ANISOU 2313 N GLU B 90 2915 2847 2588 23 237 -145 N ATOM 2314 CA GLU B 90 15.684 19.564 60.659 1.00 24.58 C ANISOU 2314 CA GLU B 90 3256 3170 2915 -11 257 -114 C ATOM 2315 C GLU B 90 15.610 20.637 59.579 1.00 27.08 C ANISOU 2315 C GLU B 90 3610 3487 3192 -5 275 -87 C ATOM 2316 O GLU B 90 15.816 21.818 59.851 1.00 27.52 O ANISOU 2316 O GLU B 90 3694 3515 3246 -29 286 -59 O ATOM 2317 CB GLU B 90 17.086 18.954 60.683 1.00 27.32 C ANISOU 2317 CB GLU B 90 3564 3540 3276 -30 272 -117 C ATOM 2318 CG GLU B 90 18.165 20.028 60.821 1.00 30.43 C ANISOU 2318 CG GLU B 90 3960 3928 3673 -72 294 -92 C ATOM 2319 CD GLU B 90 19.577 19.474 60.935 1.00 35.33 C ANISOU 2319 CD GLU B 90 4532 4578 4312 -91 307 -101 C ATOM 2320 OE1 GLU B 90 19.815 18.325 60.512 1.00 31.43 O ANISOU 2320 OE1 GLU B 90 4010 4114 3819 -66 306 -122 O ATOM 2321 OE2 GLU B 90 20.454 20.199 61.454 1.00 40.86 O ANISOU 2321 OE2 GLU B 90 5221 5272 5031 -130 317 -92 O ATOM 2322 N ASN B 91 15.315 20.225 58.350 1.00 25.75 N ANISOU 2322 N ASN B 91 3444 3348 2990 29 278 -95 N ATOM 2323 CA ASN B 91 15.263 21.176 57.244 1.00 24.97 C ANISOU 2323 CA ASN B 91 3390 3253 2845 44 297 -65 C ATOM 2324 C ASN B 91 13.944 21.937 57.171 1.00 25.21 C ANISOU 2324 C ASN B 91 3463 3261 2854 77 274 -60 C ATOM 2325 O ASN B 91 13.799 22.863 56.378 1.00 31.77 O ANISOU 2325 O ASN B 91 4341 4086 3644 95 286 -30 O ATOM 2326 CB ASN B 91 15.586 20.485 55.918 1.00 21.58 C ANISOU 2326 CB ASN B 91 2952 2870 2379 72 311 -75 C ATOM 2327 CG ASN B 91 17.052 20.119 55.803 1.00 22.91 C ANISOU 2327 CG ASN B 91 3087 3059 2558 40 346 -70 C ATOM 2328 OD1 ASN B 91 17.875 20.938 55.398 1.00 28.25 O ANISOU 2328 OD1 ASN B 91 3781 3734 3219 15 386 -36 O ATOM 2329 ND2 ASN B 91 17.389 18.891 56.172 1.00 25.75 N ANISOU 2329 ND2 ASN B 91 3398 3438 2949 41 335 -104 N ATOM 2330 N ALA B 92 12.990 21.550 58.016 1.00 22.69 N ANISOU 2330 N ALA B 92 3127 2929 2564 86 242 -88 N ATOM 2331 CA ALA B 92 11.693 22.219 58.073 1.00 22.60 C ANISOU 2331 CA ALA B 92 3146 2901 2542 119 217 -90 C ATOM 2332 C ALA B 92 11.622 23.213 59.232 1.00 27.23 C ANISOU 2332 C ALA B 92 3755 3440 3152 92 219 -70 C ATOM 2333 O ALA B 92 10.676 23.998 59.333 1.00 30.32 O ANISOU 2333 O ALA B 92 4176 3810 3533 118 204 -66 O ATOM 2334 CB ALA B 92 10.585 21.198 58.187 1.00 26.33 C ANISOU 2334 CB ALA B 92 3582 3391 3032 148 186 -139 C ATOM 2335 N LEU B 93 12.630 23.182 60.097 1.00 28.25 N ANISOU 2335 N LEU B 93 3868 3555 3312 44 235 -62 N ATOM 2336 CA LEU B 93 12.656 24.040 61.278 1.00 30.81 C ANISOU 2336 CA LEU B 93 4210 3836 3659 16 234 -51 C ATOM 2337 C LEU B 93 12.541 25.512 60.907 1.00 31.20 C ANISOU 2337 C LEU B 93 4318 3852 3685 19 246 -16 C ATOM 2338 O LEU B 93 13.124 25.954 59.918 1.00 33.46 O ANISOU 2338 O LEU B 93 4629 4141 3943 16 271 11 O ATOM 2339 CB LEU B 93 13.929 23.800 62.098 1.00 29.78 C ANISOU 2339 CB LEU B 93 4052 3705 3559 -34 246 -50 C ATOM 2340 CG LEU B 93 13.979 22.529 62.946 1.00 24.85 C ANISOU 2340 CG LEU B 93 3382 3096 2964 -36 231 -79 C ATOM 2341 CD1 LEU B 93 15.401 22.254 63.410 1.00 25.79 C ANISOU 2341 CD1 LEU B 93 3472 3226 3102 -74 241 -78 C ATOM 2342 CD2 LEU B 93 13.031 22.633 64.136 1.00 26.27 C ANISOU 2342 CD2 LEU B 93 3571 3250 3160 -29 212 -93 C ATOM 2343 N PRO B 94 11.799 26.281 61.717 1.00 28.35 N ANISOU 2343 N PRO B 94 3984 3453 3334 25 232 -17 N ATOM 2344 CA PRO B 94 11.156 25.785 62.938 1.00 25.35 C ANISOU 2344 CA PRO B 94 3578 3070 2985 26 210 -48 C ATOM 2345 C PRO B 94 9.772 25.172 62.714 1.00 26.25 C ANISOU 2345 C PRO B 94 3675 3206 3095 75 187 -77 C ATOM 2346 O PRO B 94 9.166 24.715 63.685 1.00 27.32 O ANISOU 2346 O PRO B 94 3787 3337 3256 75 176 -102 O ATOM 2347 CB PRO B 94 11.006 27.054 63.771 1.00 25.31 C ANISOU 2347 CB PRO B 94 3615 3015 2988 13 210 -36 C ATOM 2348 CG PRO B 94 10.740 28.107 62.735 1.00 21.56 C ANISOU 2348 CG PRO B 94 3193 2520 2479 39 219 -6 C ATOM 2349 CD PRO B 94 11.610 27.734 61.554 1.00 25.40 C ANISOU 2349 CD PRO B 94 3673 3035 2944 30 241 13 C ATOM 2350 N LYS B 95 9.279 25.161 61.478 1.00 24.36 N ANISOU 2350 N LYS B 95 3444 2988 2823 116 179 -76 N ATOM 2351 CA LYS B 95 7.922 24.682 61.219 1.00 29.82 C ANISOU 2351 CA LYS B 95 4114 3702 3513 164 152 -111 C ATOM 2352 C LYS B 95 7.811 23.170 61.090 1.00 28.05 C ANISOU 2352 C LYS B 95 3834 3516 3309 161 146 -149 C ATOM 2353 O LYS B 95 7.557 22.646 60.006 1.00 27.93 O ANISOU 2353 O LYS B 95 3805 3534 3272 191 135 -166 O ATOM 2354 CB LYS B 95 7.322 25.368 59.990 1.00 38.08 C ANISOU 2354 CB LYS B 95 5197 4759 4512 219 138 -100 C ATOM 2355 CG LYS B 95 6.748 26.732 60.308 1.00 44.38 C ANISOU 2355 CG LYS B 95 6047 5517 5300 242 133 -80 C ATOM 2356 CD LYS B 95 5.791 27.205 59.238 1.00 50.85 C ANISOU 2356 CD LYS B 95 6893 6353 6076 314 107 -82 C ATOM 2357 CE LYS B 95 5.123 28.495 59.674 1.00 55.13 C ANISOU 2357 CE LYS B 95 7482 6851 6612 344 99 -67 C ATOM 2358 NZ LYS B 95 6.133 29.488 60.135 1.00 56.47 N ANISOU 2358 NZ LYS B 95 7706 6965 6786 298 132 -21 N ATOM 2359 N THR B 96 7.993 22.472 62.206 1.00 26.37 N ANISOU 2359 N THR B 96 3592 3294 3136 128 154 -162 N ATOM 2360 CA THR B 96 7.908 21.018 62.200 1.00 22.37 C ANISOU 2360 CA THR B 96 3038 2810 2653 123 153 -196 C ATOM 2361 C THR B 96 7.284 20.507 63.491 1.00 19.04 C ANISOU 2361 C THR B 96 2594 2369 2271 108 157 -216 C ATOM 2362 O THR B 96 7.493 21.080 64.557 1.00 17.49 O ANISOU 2362 O THR B 96 2418 2146 2082 89 166 -198 O ATOM 2363 CB THR B 96 9.293 20.382 61.997 1.00 20.74 C ANISOU 2363 CB THR B 96 2821 2614 2446 94 170 -182 C ATOM 2364 OG1 THR B 96 9.140 18.998 61.659 1.00 22.60 O ANISOU 2364 OG1 THR B 96 3017 2872 2698 101 167 -216 O ATOM 2365 CG2 THR B 96 10.144 20.520 63.254 1.00 20.61 C ANISOU 2365 CG2 THR B 96 2808 2571 2450 55 183 -163 C ATOM 2366 N ILE B 97 6.500 19.440 63.380 1.00 17.74 N ANISOU 2366 N ILE B 97 2391 2220 2131 117 154 -255 N ATOM 2367 CA ILE B 97 5.878 18.793 64.533 1.00 16.45 C ANISOU 2367 CA ILE B 97 2206 2037 2006 101 168 -274 C ATOM 2368 C ILE B 97 6.330 17.340 64.572 1.00 18.25 C ANISOU 2368 C ILE B 97 2408 2268 2260 82 181 -289 C ATOM 2369 O ILE B 97 6.182 16.606 63.596 1.00 20.86 O ANISOU 2369 O ILE B 97 2713 2620 2592 94 172 -317 O ATOM 2370 CB ILE B 97 4.341 18.796 64.448 1.00 17.80 C ANISOU 2370 CB ILE B 97 2350 2217 2195 125 159 -314 C ATOM 2371 CG1 ILE B 97 3.802 20.211 64.241 1.00 22.80 C ANISOU 2371 CG1 ILE B 97 3010 2850 2801 157 141 -303 C ATOM 2372 CG2 ILE B 97 3.735 18.162 65.698 1.00 16.42 C ANISOU 2372 CG2 ILE B 97 2156 2020 2061 103 185 -329 C ATOM 2373 CD1 ILE B 97 2.293 20.255 64.015 1.00 24.08 C ANISOU 2373 CD1 ILE B 97 3139 3031 2980 191 125 -348 C ATOM 2374 N MET B 98 6.897 16.937 65.699 1.00 16.00 N ANISOU 2374 N MET B 98 2132 1959 1990 57 200 -272 N ATOM 2375 CA MET B 98 7.337 15.562 65.906 1.00 16.15 C ANISOU 2375 CA MET B 98 2134 1970 2032 43 214 -281 C ATOM 2376 C MET B 98 6.324 14.818 66.773 1.00 16.12 C ANISOU 2376 C MET B 98 2117 1943 2067 34 237 -302 C ATOM 2377 O MET B 98 5.834 15.365 67.749 1.00 16.94 O ANISOU 2377 O MET B 98 2235 2029 2172 29 249 -292 O ATOM 2378 CB MET B 98 8.707 15.564 66.584 1.00 14.74 C ANISOU 2378 CB MET B 98 1977 1782 1842 29 219 -247 C ATOM 2379 CG MET B 98 9.167 14.212 67.063 1.00 14.88 C ANISOU 2379 CG MET B 98 1988 1785 1881 22 234 -250 C ATOM 2380 SD MET B 98 10.872 14.251 67.675 1.00 18.12 S ANISOU 2380 SD MET B 98 2415 2197 2273 16 229 -216 S ATOM 2381 CE MET B 98 10.939 12.681 68.534 1.00 21.11 C ANISOU 2381 CE MET B 98 2798 2546 2678 20 249 -219 C ATOM 2382 N LEU B 99 6.002 13.581 66.403 1.00 15.42 N ANISOU 2382 N LEU B 99 2000 1849 2008 29 248 -334 N ATOM 2383 CA LEU B 99 5.212 12.706 67.266 1.00 13.33 C ANISOU 2383 CA LEU B 99 1727 1554 1786 12 281 -349 C ATOM 2384 C LEU B 99 6.144 11.645 67.832 1.00 14.74 C ANISOU 2384 C LEU B 99 1925 1705 1972 1 300 -329 C ATOM 2385 O LEU B 99 6.709 10.846 67.091 1.00 16.47 O ANISOU 2385 O LEU B 99 2133 1928 2197 5 293 -342 O ATOM 2386 CB LEU B 99 4.059 12.049 66.496 1.00 15.88 C ANISOU 2386 CB LEU B 99 2003 1884 2146 10 282 -406 C ATOM 2387 CG LEU B 99 2.822 12.878 66.120 1.00 22.84 C ANISOU 2387 CG LEU B 99 2856 2791 3032 24 266 -437 C ATOM 2388 CD1 LEU B 99 2.008 13.255 67.355 1.00 24.62 C ANISOU 2388 CD1 LEU B 99 3085 2995 3274 13 297 -430 C ATOM 2389 CD2 LEU B 99 3.203 14.118 65.327 1.00 25.09 C ANISOU 2389 CD2 LEU B 99 3157 3109 3265 55 226 -420 C ATOM 2390 N SER B 100 6.312 11.650 69.147 1.00 16.01 N ANISOU 2390 N SER B 100 2117 1837 2129 -6 323 -298 N ATOM 2391 CA SER B 100 7.315 10.819 69.802 1.00 16.39 C ANISOU 2391 CA SER B 100 2194 1862 2173 -5 335 -271 C ATOM 2392 C SER B 100 6.787 9.432 70.130 1.00 16.37 C ANISOU 2392 C SER B 100 2191 1817 2212 -17 374 -285 C ATOM 2393 O SER B 100 5.645 9.286 70.547 1.00 14.64 O ANISOU 2393 O SER B 100 1963 1579 2021 -34 406 -300 O ATOM 2394 CB SER B 100 7.805 11.492 71.088 1.00 18.38 C ANISOU 2394 CB SER B 100 2485 2105 2392 -1 337 -231 C ATOM 2395 OG SER B 100 8.750 10.671 71.747 1.00 22.84 O ANISOU 2395 OG SER B 100 3078 2650 2949 9 344 -207 O ATOM 2396 N PRO B 101 7.629 8.404 69.958 1.00 16.46 N ANISOU 2396 N PRO B 101 2212 1813 2230 -9 376 -280 N ATOM 2397 CA PRO B 101 7.246 7.035 70.315 1.00 19.90 C ANISOU 2397 CA PRO B 101 2659 2198 2705 -20 417 -288 C ATOM 2398 C PRO B 101 7.455 6.768 71.805 1.00 21.43 C ANISOU 2398 C PRO B 101 2905 2352 2884 -15 449 -243 C ATOM 2399 O PRO B 101 7.178 5.665 72.271 1.00 25.97 O ANISOU 2399 O PRO B 101 3503 2876 3487 -23 490 -239 O ATOM 2400 CB PRO B 101 8.226 6.192 69.500 1.00 20.31 C ANISOU 2400 CB PRO B 101 2706 2251 2761 -3 398 -297 C ATOM 2401 CG PRO B 101 9.455 7.028 69.468 1.00 19.42 C ANISOU 2401 CG PRO B 101 2601 2179 2599 20 360 -269 C ATOM 2402 CD PRO B 101 8.987 8.462 69.390 1.00 20.99 C ANISOU 2402 CD PRO B 101 2786 2413 2775 11 342 -268 C ATOM 2403 N CYS B 102 7.960 7.765 72.528 1.00 20.90 N ANISOU 2403 N CYS B 102 2862 2307 2772 -1 429 -211 N ATOM 2404 CA CYS B 102 8.203 7.650 73.963 1.00 21.46 C ANISOU 2404 CA CYS B 102 2987 2350 2815 12 452 -169 C ATOM 2405 C CYS B 102 7.669 8.882 74.680 1.00 18.94 C ANISOU 2405 C CYS B 102 2677 2049 2470 7 452 -160 C ATOM 2406 O CYS B 102 7.233 9.834 74.045 1.00 21.73 O ANISOU 2406 O CYS B 102 2995 2435 2826 -4 431 -182 O ATOM 2407 CB CYS B 102 9.701 7.471 74.258 1.00 21.19 C ANISOU 2407 CB CYS B 102 2980 2325 2744 46 419 -141 C ATOM 2408 SG CYS B 102 10.786 8.821 73.706 1.00 20.78 S ANISOU 2408 SG CYS B 102 2902 2339 2657 55 356 -143 S ATOM 2409 N SER B 103 7.693 8.860 76.006 1.00 17.84 N ANISOU 2409 N SER B 103 2587 1887 2302 18 476 -127 N ATOM 2410 CA SER B 103 7.274 10.025 76.776 1.00 20.81 C ANISOU 2410 CA SER B 103 2978 2281 2649 19 475 -120 C ATOM 2411 C SER B 103 8.303 11.129 76.574 1.00 21.94 C ANISOU 2411 C SER B 103 3116 2466 2755 33 415 -117 C ATOM 2412 O SER B 103 9.425 10.864 76.130 1.00 20.92 O ANISOU 2412 O SER B 103 2981 2351 2618 46 381 -112 O ATOM 2413 CB SER B 103 7.105 9.677 78.259 1.00 17.24 C ANISOU 2413 CB SER B 103 2587 1796 2168 32 517 -86 C ATOM 2414 OG SER B 103 8.216 8.949 78.758 1.00 22.19 O ANISOU 2414 OG SER B 103 3257 2409 2765 63 504 -55 O ATOM 2415 N LEU B 104 7.917 12.364 76.877 1.00 18.51 N ANISOU 2415 N LEU B 104 2681 2049 2301 29 404 -122 N ATOM 2416 CA LEU B 104 8.732 13.527 76.542 1.00 17.21 C ANISOU 2416 CA LEU B 104 2508 1920 2113 33 353 -125 C ATOM 2417 C LEU B 104 9.904 13.747 77.483 1.00 15.02 C ANISOU 2417 C LEU B 104 2266 1649 1791 54 325 -104 C ATOM 2418 O LEU B 104 10.719 14.641 77.259 1.00 19.78 O ANISOU 2418 O LEU B 104 2859 2278 2379 52 284 -109 O ATOM 2419 CB LEU B 104 7.864 14.787 76.485 1.00 19.20 C ANISOU 2419 CB LEU B 104 2750 2181 2363 24 352 -141 C ATOM 2420 CG LEU B 104 6.846 14.814 75.335 1.00 12.57 C ANISOU 2420 CG LEU B 104 1865 1349 1563 10 361 -169 C ATOM 2421 CD1 LEU B 104 5.974 16.052 75.459 1.00 13.09 C ANISOU 2421 CD1 LEU B 104 1929 1422 1623 12 360 -183 C ATOM 2422 CD2 LEU B 104 7.559 14.778 73.991 1.00 12.47 C ANISOU 2422 CD2 LEU B 104 1821 1358 1559 7 327 -178 C ATOM 2423 N ASP B 105 9.980 12.942 78.539 1.00 17.55 N ANISOU 2423 N ASP B 105 2629 1947 2092 74 348 -82 N ATOM 2424 CA ASP B 105 11.113 13.001 79.447 1.00 17.90 C ANISOU 2424 CA ASP B 105 2707 2003 2091 103 316 -65 C ATOM 2425 C ASP B 105 12.302 12.201 78.914 1.00 17.55 C ANISOU 2425 C ASP B 105 2646 1969 2053 119 287 -61 C ATOM 2426 O ASP B 105 13.383 12.212 79.507 1.00 19.81 O ANISOU 2426 O ASP B 105 2948 2272 2306 146 251 -54 O ATOM 2427 CB ASP B 105 10.716 12.505 80.840 1.00 18.29 C ANISOU 2427 CB ASP B 105 2819 2025 2106 128 351 -39 C ATOM 2428 CG ASP B 105 10.017 11.159 80.802 1.00 23.57 C ANISOU 2428 CG ASP B 105 3502 2652 2803 126 409 -24 C ATOM 2429 OD1 ASP B 105 9.538 10.767 79.718 1.00 28.18 O ANISOU 2429 OD1 ASP B 105 4042 3228 3437 99 424 -42 O ATOM 2430 OD2 ASP B 105 9.929 10.495 81.856 1.00 24.83 O ANISOU 2430 OD2 ASP B 105 3719 2784 2932 151 440 5 O ATOM 2431 N PHE B 106 12.104 11.513 77.793 1.00 20.12 N ANISOU 2431 N PHE B 106 2937 2287 2420 104 301 -71 N ATOM 2432 CA PHE B 106 13.185 10.758 77.159 1.00 18.84 C ANISOU 2432 CA PHE B 106 2755 2137 2268 120 277 -73 C ATOM 2433 C PHE B 106 13.483 11.250 75.745 1.00 19.78 C ANISOU 2433 C PHE B 106 2816 2287 2412 97 255 -97 C ATOM 2434 O PHE B 106 12.601 11.757 75.050 1.00 20.12 O ANISOU 2434 O PHE B 106 2838 2331 2476 70 269 -113 O ATOM 2435 CB PHE B 106 12.849 9.267 77.101 1.00 19.13 C ANISOU 2435 CB PHE B 106 2809 2131 2328 132 315 -63 C ATOM 2436 CG PHE B 106 12.766 8.605 78.446 1.00 22.55 C ANISOU 2436 CG PHE B 106 3307 2529 2731 163 340 -30 C ATOM 2437 CD1 PHE B 106 13.789 8.738 79.367 1.00 22.48 C ANISOU 2437 CD1 PHE B 106 3330 2539 2673 204 304 -13 C ATOM 2438 CD2 PHE B 106 11.656 7.848 78.787 1.00 23.75 C ANISOU 2438 CD2 PHE B 106 3490 2632 2903 152 402 -19 C ATOM 2439 CE1 PHE B 106 13.713 8.119 80.602 1.00 26.68 C ANISOU 2439 CE1 PHE B 106 3930 3040 3168 240 326 20 C ATOM 2440 CE2 PHE B 106 11.571 7.228 80.015 1.00 24.99 C ANISOU 2440 CE2 PHE B 106 3715 2753 3028 181 433 17 C ATOM 2441 CZ PHE B 106 12.600 7.367 80.928 1.00 27.47 C ANISOU 2441 CZ PHE B 106 4067 3085 3284 229 394 38 C ATOM 2442 N ILE B 107 14.734 11.092 75.329 1.00 20.03 N ANISOU 2442 N ILE B 107 2824 2345 2440 111 223 -101 N ATOM 2443 CA ILE B 107 15.141 11.392 73.963 1.00 22.93 C ANISOU 2443 CA ILE B 107 3142 2743 2828 93 209 -121 C ATOM 2444 C ILE B 107 15.343 10.094 73.204 1.00 24.20 C ANISOU 2444 C ILE B 107 3288 2894 3012 108 221 -128 C ATOM 2445 O ILE B 107 16.137 9.248 73.615 1.00 26.20 O ANISOU 2445 O ILE B 107 3553 3143 3259 140 212 -120 O ATOM 2446 CB ILE B 107 16.474 12.148 73.914 1.00 24.49 C ANISOU 2446 CB ILE B 107 3314 2982 3009 93 169 -126 C ATOM 2447 CG1 ILE B 107 16.366 13.476 74.662 1.00 23.70 C ANISOU 2447 CG1 ILE B 107 3230 2888 2887 76 154 -124 C ATOM 2448 CG2 ILE B 107 16.894 12.374 72.454 1.00 24.84 C ANISOU 2448 CG2 ILE B 107 3311 3055 3072 75 166 -142 C ATOM 2449 CD1 ILE B 107 15.565 14.513 73.918 1.00 18.95 C ANISOU 2449 CD1 ILE B 107 2617 2285 2296 43 166 -131 C ATOM 2450 N TYR B 108 14.619 9.937 72.104 1.00 21.87 N ANISOU 2450 N TYR B 108 2969 2596 2744 89 239 -147 N ATOM 2451 CA TYR B 108 14.827 8.804 71.212 1.00 23.38 C ANISOU 2451 CA TYR B 108 3142 2782 2959 101 247 -163 C ATOM 2452 C TYR B 108 14.558 9.196 69.762 1.00 19.50 C ANISOU 2452 C TYR B 108 2612 2317 2479 82 244 -189 C ATOM 2453 O TYR B 108 13.560 9.854 69.467 1.00 18.04 O ANISOU 2453 O TYR B 108 2423 2133 2299 61 252 -198 O ATOM 2454 CB TYR B 108 13.945 7.607 71.590 1.00 23.80 C ANISOU 2454 CB TYR B 108 3224 2782 3038 106 283 -163 C ATOM 2455 CG TYR B 108 14.068 6.516 70.563 1.00 21.99 C ANISOU 2455 CG TYR B 108 2974 2543 2837 114 291 -188 C ATOM 2456 CD1 TYR B 108 15.047 5.535 70.676 1.00 22.86 C ANISOU 2456 CD1 TYR B 108 3095 2644 2948 149 285 -182 C ATOM 2457 CD2 TYR B 108 13.258 6.505 69.435 1.00 21.29 C ANISOU 2457 CD2 TYR B 108 2856 2460 2773 92 299 -221 C ATOM 2458 CE1 TYR B 108 15.187 4.556 69.716 1.00 22.29 C ANISOU 2458 CE1 TYR B 108 3006 2562 2901 159 291 -209 C ATOM 2459 CE2 TYR B 108 13.396 5.537 68.470 1.00 21.92 C ANISOU 2459 CE2 TYR B 108 2918 2535 2877 101 303 -250 C ATOM 2460 CZ TYR B 108 14.357 4.562 68.613 1.00 26.87 C ANISOU 2460 CZ TYR B 108 3558 3147 3505 134 301 -244 C ATOM 2461 OH TYR B 108 14.494 3.591 67.650 1.00 27.87 O ANISOU 2461 OH TYR B 108 3668 3265 3655 145 305 -277 O ATOM 2462 N PRO B 109 15.458 8.805 68.848 1.00 20.36 N ANISOU 2462 N PRO B 109 2693 2453 2590 95 233 -202 N ATOM 2463 CA PRO B 109 16.723 8.115 69.117 1.00 18.91 C ANISOU 2463 CA PRO B 109 2506 2278 2401 126 220 -196 C ATOM 2464 C PRO B 109 17.778 9.076 69.656 1.00 17.63 C ANISOU 2464 C PRO B 109 2333 2151 2214 126 193 -182 C ATOM 2465 O PRO B 109 17.744 10.260 69.341 1.00 17.92 O ANISOU 2465 O PRO B 109 2356 2212 2241 98 187 -181 O ATOM 2466 CB PRO B 109 17.140 7.610 67.736 1.00 20.58 C ANISOU 2466 CB PRO B 109 2682 2513 2623 134 221 -223 C ATOM 2467 CG PRO B 109 16.544 8.599 66.784 1.00 19.85 C ANISOU 2467 CG PRO B 109 2572 2446 2524 106 223 -234 C ATOM 2468 CD PRO B 109 15.253 9.058 67.412 1.00 14.77 C ANISOU 2468 CD PRO B 109 1954 1773 1885 85 233 -227 C ATOM 2469 N THR B 110 18.714 8.572 70.454 1.00 19.73 N ANISOU 2469 N THR B 110 2606 2419 2471 157 176 -173 N ATOM 2470 CA THR B 110 19.715 9.437 71.069 1.00 17.66 C ANISOU 2470 CA THR B 110 2329 2192 2189 157 146 -167 C ATOM 2471 C THR B 110 20.613 10.148 70.060 1.00 17.01 C ANISOU 2471 C THR B 110 2193 2160 2110 137 137 -183 C ATOM 2472 O THR B 110 21.081 11.254 70.318 1.00 19.66 O ANISOU 2472 O THR B 110 2514 2519 2436 114 122 -182 O ATOM 2473 CB THR B 110 20.592 8.675 72.075 1.00 21.10 C ANISOU 2473 CB THR B 110 2779 2626 2612 205 123 -159 C ATOM 2474 OG1 THR B 110 21.305 7.634 71.399 1.00 26.08 O ANISOU 2474 OG1 THR B 110 3385 3266 3257 237 123 -173 O ATOM 2475 CG2 THR B 110 19.729 8.072 73.156 1.00 19.91 C ANISOU 2475 CG2 THR B 110 2690 2423 2451 224 138 -136 C ATOM 2476 N ASN B 111 20.857 9.517 68.918 1.00 15.59 N ANISOU 2476 N ASN B 111 1986 1994 1943 146 151 -198 N ATOM 2477 CA ASN B 111 21.695 10.120 67.883 1.00 16.92 C ANISOU 2477 CA ASN B 111 2106 2209 2112 128 152 -211 C ATOM 2478 C ASN B 111 21.089 11.403 67.353 1.00 21.96 C ANISOU 2478 C ASN B 111 2748 2852 2743 83 165 -204 C ATOM 2479 O ASN B 111 21.789 12.256 66.815 1.00 24.19 O ANISOU 2479 O ASN B 111 3002 3168 3023 59 168 -206 O ATOM 2480 CB ASN B 111 21.905 9.144 66.733 1.00 23.13 C ANISOU 2480 CB ASN B 111 2871 3007 2908 150 169 -231 C ATOM 2481 CG ASN B 111 22.409 7.804 67.202 1.00 34.37 C ANISOU 2481 CG ASN B 111 4300 4418 4342 200 159 -237 C ATOM 2482 OD1 ASN B 111 21.653 7.009 67.770 1.00 42.48 O ANISOU 2482 OD1 ASN B 111 5369 5396 5375 218 163 -230 O ATOM 2483 ND2 ASN B 111 23.691 7.540 66.973 1.00 32.27 N ANISOU 2483 ND2 ASN B 111 3990 4192 4078 224 148 -252 N ATOM 2484 N ASN B 112 19.778 11.538 67.506 1.00 22.04 N ANISOU 2484 N ASN B 112 2796 2827 2752 74 174 -197 N ATOM 2485 CA ASN B 112 19.090 12.735 67.050 1.00 12.75 C ANISOU 2485 CA ASN B 112 1629 1651 1567 41 183 -190 C ATOM 2486 C ASN B 112 18.872 13.761 68.166 1.00 13.24 C ANISOU 2486 C ASN B 112 1714 1696 1620 21 170 -175 C ATOM 2487 O ASN B 112 18.093 14.695 68.014 1.00 17.39 O ANISOU 2487 O ASN B 112 2258 2209 2139 1 176 -168 O ATOM 2488 CB ASN B 112 17.760 12.344 66.396 1.00 19.63 C ANISOU 2488 CB ASN B 112 2516 2500 2441 45 198 -198 C ATOM 2489 CG ASN B 112 17.955 11.656 65.052 1.00 24.31 C ANISOU 2489 CG ASN B 112 3086 3115 3035 60 209 -218 C ATOM 2490 OD1 ASN B 112 19.003 11.796 64.420 1.00 23.05 O ANISOU 2490 OD1 ASN B 112 2900 2991 2868 60 212 -220 O ATOM 2491 ND2 ASN B 112 16.936 10.922 64.600 1.00 20.06 N ANISOU 2491 ND2 ASN B 112 2557 2559 2507 71 217 -237 N ATOM 2492 N HIS B 113 19.579 13.612 69.285 1.00 19.75 N ANISOU 2492 N HIS B 113 2540 2522 2443 32 150 -173 N ATOM 2493 CA HIS B 113 19.298 14.481 70.427 1.00 19.84 C ANISOU 2493 CA HIS B 113 2578 2516 2443 19 136 -164 C ATOM 2494 C HIS B 113 19.391 15.973 70.086 1.00 20.47 C ANISOU 2494 C HIS B 113 2654 2603 2520 -21 137 -162 C ATOM 2495 O HIS B 113 18.560 16.759 70.528 1.00 20.18 O ANISOU 2495 O HIS B 113 2649 2542 2476 -34 138 -155 O ATOM 2496 CB HIS B 113 20.148 14.123 71.658 1.00 26.19 C ANISOU 2496 CB HIS B 113 3384 3328 3238 43 107 -166 C ATOM 2497 CG HIS B 113 21.585 14.534 71.553 1.00 40.48 C ANISOU 2497 CG HIS B 113 5148 5180 5054 33 85 -181 C ATOM 2498 ND1 HIS B 113 22.478 13.912 70.713 1.00 48.85 N ANISOU 2498 ND1 HIS B 113 6162 6271 6126 45 89 -192 N ATOM 2499 CD2 HIS B 113 22.283 15.493 72.209 1.00 48.00 C ANISOU 2499 CD2 HIS B 113 6087 6148 6002 13 61 -192 C ATOM 2500 CE1 HIS B 113 23.670 14.478 70.844 1.00 52.83 C ANISOU 2500 CE1 HIS B 113 6624 6813 6638 30 70 -209 C ATOM 2501 NE2 HIS B 113 23.577 15.436 71.744 1.00 52.28 N ANISOU 2501 NE2 HIS B 113 6572 6733 6560 9 51 -210 N ATOM 2502 N LYS B 114 20.380 16.369 69.286 1.00 21.57 N ANISOU 2502 N LYS B 114 2756 2773 2666 -40 140 -168 N ATOM 2503 CA LYS B 114 20.530 17.795 68.976 1.00 15.94 C ANISOU 2503 CA LYS B 114 2044 2059 1953 -82 148 -163 C ATOM 2504 C LYS B 114 19.347 18.387 68.202 1.00 19.87 C ANISOU 2504 C LYS B 114 2574 2533 2442 -89 169 -149 C ATOM 2505 O LYS B 114 18.845 19.456 68.559 1.00 23.28 O ANISOU 2505 O LYS B 114 3036 2940 2869 -108 168 -142 O ATOM 2506 CB LYS B 114 21.848 18.093 68.256 1.00 19.48 C ANISOU 2506 CB LYS B 114 2445 2543 2414 -106 157 -171 C ATOM 2507 CG LYS B 114 23.086 17.970 69.135 1.00 22.09 C ANISOU 2507 CG LYS B 114 2736 2899 2756 -107 129 -191 C ATOM 2508 CD LYS B 114 24.341 18.387 68.368 1.00 27.71 C ANISOU 2508 CD LYS B 114 3394 3649 3488 -139 145 -203 C ATOM 2509 CE LYS B 114 25.572 18.413 69.260 1.00 34.31 C ANISOU 2509 CE LYS B 114 4182 4515 4341 -143 113 -232 C ATOM 2510 NZ LYS B 114 25.950 17.053 69.734 1.00 38.19 N ANISOU 2510 NZ LYS B 114 4655 5030 4827 -87 85 -244 N ATOM 2511 N VAL B 115 18.901 17.700 67.153 1.00 19.37 N ANISOU 2511 N VAL B 115 2506 2478 2375 -71 186 -149 N ATOM 2512 CA VAL B 115 17.760 18.186 66.382 1.00 22.77 C ANISOU 2512 CA VAL B 115 2965 2894 2794 -69 199 -140 C ATOM 2513 C VAL B 115 16.469 18.101 67.197 1.00 15.79 C ANISOU 2513 C VAL B 115 2111 1978 1910 -55 191 -142 C ATOM 2514 O VAL B 115 15.624 18.989 67.129 1.00 20.81 O ANISOU 2514 O VAL B 115 2774 2595 2538 -59 193 -136 O ATOM 2515 CB VAL B 115 17.594 17.437 65.043 1.00 17.90 C ANISOU 2515 CB VAL B 115 2333 2299 2170 -49 214 -147 C ATOM 2516 CG1 VAL B 115 16.303 17.869 64.352 1.00 20.98 C ANISOU 2516 CG1 VAL B 115 2751 2676 2544 -37 218 -145 C ATOM 2517 CG2 VAL B 115 18.796 17.692 64.137 1.00 22.36 C ANISOU 2517 CG2 VAL B 115 2872 2896 2729 -64 232 -143 C ATOM 2518 N ILE B 116 16.322 17.035 67.975 1.00 16.11 N ANISOU 2518 N ILE B 116 2149 2012 1960 -36 184 -151 N ATOM 2519 CA ILE B 116 15.124 16.882 68.791 1.00 14.83 C ANISOU 2519 CA ILE B 116 2013 1821 1800 -25 185 -152 C ATOM 2520 C ILE B 116 15.025 18.019 69.807 1.00 18.26 C ANISOU 2520 C ILE B 116 2475 2237 2225 -40 175 -144 C ATOM 2521 O ILE B 116 13.948 18.568 70.015 1.00 17.49 O ANISOU 2521 O ILE B 116 2401 2121 2125 -38 180 -144 O ATOM 2522 CB ILE B 116 15.037 15.494 69.454 1.00 16.00 C ANISOU 2522 CB ILE B 116 2161 1959 1960 -4 188 -158 C ATOM 2523 CG1 ILE B 116 14.811 14.422 68.379 1.00 19.75 C ANISOU 2523 CG1 ILE B 116 2614 2441 2447 10 200 -173 C ATOM 2524 CG2 ILE B 116 13.897 15.452 70.488 1.00 16.94 C ANISOU 2524 CG2 ILE B 116 2310 2046 2079 1 197 -156 C ATOM 2525 CD1 ILE B 116 14.780 13.025 68.934 1.00 19.89 C ANISOU 2525 CD1 ILE B 116 2636 2441 2480 30 207 -178 C ATOM 2526 N GLN B 117 16.151 18.401 70.411 1.00 16.78 N ANISOU 2526 N GLN B 117 2282 2060 2035 -53 160 -143 N ATOM 2527 CA GLN B 117 16.164 19.574 71.286 1.00 16.16 C ANISOU 2527 CA GLN B 117 2228 1965 1949 -70 148 -142 C ATOM 2528 C GLN B 117 15.732 20.836 70.535 1.00 16.32 C ANISOU 2528 C GLN B 117 2263 1971 1967 -89 157 -135 C ATOM 2529 O GLN B 117 15.012 21.668 71.077 1.00 21.96 O ANISOU 2529 O GLN B 117 3010 2660 2675 -91 156 -134 O ATOM 2530 CB GLN B 117 17.550 19.802 71.889 1.00 21.47 C ANISOU 2530 CB GLN B 117 2881 2655 2621 -84 125 -150 C ATOM 2531 CG GLN B 117 18.002 18.747 72.877 1.00 24.00 C ANISOU 2531 CG GLN B 117 3198 2986 2936 -56 108 -155 C ATOM 2532 CD GLN B 117 19.447 18.948 73.299 1.00 34.56 C ANISOU 2532 CD GLN B 117 4505 4351 4275 -66 80 -171 C ATOM 2533 OE1 GLN B 117 20.331 18.175 72.922 1.00 37.50 O ANISOU 2533 OE1 GLN B 117 4840 4753 4657 -55 74 -176 O ATOM 2534 NE2 GLN B 117 19.695 19.996 74.082 1.00 39.22 N ANISOU 2534 NE2 GLN B 117 5107 4934 4860 -86 60 -183 N ATOM 2535 N GLU B 118 16.181 20.983 69.291 1.00 14.09 N ANISOU 2535 N GLU B 118 1963 1705 1687 -100 169 -128 N ATOM 2536 CA GLU B 118 15.831 22.160 68.509 1.00 16.61 C ANISOU 2536 CA GLU B 118 2304 2008 1999 -114 182 -116 C ATOM 2537 C GLU B 118 14.339 22.184 68.176 1.00 19.08 C ANISOU 2537 C GLU B 118 2641 2306 2303 -85 186 -115 C ATOM 2538 O GLU B 118 13.726 23.248 68.141 1.00 20.60 O ANISOU 2538 O GLU B 118 2865 2474 2487 -85 187 -108 O ATOM 2539 CB GLU B 118 16.686 22.263 67.242 1.00 21.49 C ANISOU 2539 CB GLU B 118 2902 2648 2616 -129 200 -106 C ATOM 2540 CG GLU B 118 18.132 22.665 67.516 1.00 30.72 C ANISOU 2540 CG GLU B 118 4046 3827 3799 -167 200 -109 C ATOM 2541 CD GLU B 118 19.041 22.509 66.301 1.00 47.14 C ANISOU 2541 CD GLU B 118 6095 5936 5879 -181 225 -102 C ATOM 2542 OE1 GLU B 118 18.537 22.182 65.204 1.00 50.17 O ANISOU 2542 OE1 GLU B 118 6486 6330 6245 -159 241 -92 O ATOM 2543 OE2 GLU B 118 20.268 22.711 66.448 1.00 54.34 O ANISOU 2543 OE2 GLU B 118 6974 6863 6808 -213 229 -109 O ATOM 2544 N ILE B 119 13.755 21.009 67.964 1.00 15.42 N ANISOU 2544 N ILE B 119 2159 1857 1843 -60 187 -126 N ATOM 2545 CA ILE B 119 12.317 20.914 67.734 1.00 19.22 C ANISOU 2545 CA ILE B 119 2651 2330 2323 -34 189 -135 C ATOM 2546 C ILE B 119 11.525 21.291 68.992 1.00 18.30 C ANISOU 2546 C ILE B 119 2557 2188 2210 -30 186 -140 C ATOM 2547 O ILE B 119 10.539 22.010 68.902 1.00 16.63 O ANISOU 2547 O ILE B 119 2364 1962 1994 -16 186 -142 O ATOM 2548 CB ILE B 119 11.899 19.510 67.246 1.00 16.01 C ANISOU 2548 CB ILE B 119 2214 1941 1926 -16 194 -152 C ATOM 2549 CG1 ILE B 119 12.589 19.180 65.923 1.00 18.87 C ANISOU 2549 CG1 ILE B 119 2557 2332 2280 -13 197 -151 C ATOM 2550 CG2 ILE B 119 10.388 19.428 67.070 1.00 17.47 C ANISOU 2550 CG2 ILE B 119 2401 2121 2118 7 195 -170 C ATOM 2551 CD1 ILE B 119 12.349 17.765 65.451 1.00 20.92 C ANISOU 2551 CD1 ILE B 119 2790 2608 2552 3 200 -173 C ATOM 2552 N ALA B 120 11.957 20.815 70.159 1.00 18.65 N ANISOU 2552 N ALA B 120 2601 2227 2259 -37 184 -142 N ATOM 2553 CA ALA B 120 11.270 21.165 71.400 1.00 22.42 C ANISOU 2553 CA ALA B 120 3104 2682 2733 -31 185 -146 C ATOM 2554 C ALA B 120 11.341 22.671 71.630 1.00 25.91 C ANISOU 2554 C ALA B 120 3575 3104 3164 -42 176 -142 C ATOM 2555 O ALA B 120 10.389 23.275 72.122 1.00 26.46 O ANISOU 2555 O ALA B 120 3668 3154 3230 -29 179 -148 O ATOM 2556 CB ALA B 120 11.858 20.411 72.591 1.00 19.96 C ANISOU 2556 CB ALA B 120 2795 2371 2418 -31 182 -146 C ATOM 2557 N GLN B 121 12.471 23.271 71.263 1.00 23.97 N ANISOU 2557 N GLN B 121 3329 2860 2917 -67 167 -134 N ATOM 2558 CA GLN B 121 12.679 24.704 71.457 1.00 26.76 C ANISOU 2558 CA GLN B 121 3713 3187 3266 -85 162 -131 C ATOM 2559 C GLN B 121 11.885 25.568 70.470 1.00 25.84 C ANISOU 2559 C GLN B 121 3620 3055 3145 -72 170 -120 C ATOM 2560 O GLN B 121 11.215 26.519 70.876 1.00 32.92 O ANISOU 2560 O GLN B 121 4550 3921 4037 -63 168 -123 O ATOM 2561 CB GLN B 121 14.171 25.045 71.366 1.00 32.29 C ANISOU 2561 CB GLN B 121 4400 3894 3974 -122 155 -128 C ATOM 2562 CG GLN B 121 15.023 24.444 72.474 1.00 37.76 C ANISOU 2562 CG GLN B 121 5075 4605 4669 -129 137 -143 C ATOM 2563 CD GLN B 121 16.519 24.575 72.205 1.00 41.55 C ANISOU 2563 CD GLN B 121 5523 5103 5162 -163 130 -147 C ATOM 2564 OE1 GLN B 121 16.956 25.420 71.418 1.00 43.23 O ANISOU 2564 OE1 GLN B 121 5736 5305 5384 -192 143 -139 O ATOM 2565 NE2 GLN B 121 17.308 23.727 72.854 1.00 37.70 N ANISOU 2565 NE2 GLN B 121 5008 4643 4675 -157 112 -160 N ATOM 2566 N ASN B 122 11.957 25.234 69.183 1.00 23.06 N ANISOU 2566 N ASN B 122 3251 2721 2790 -66 179 -109 N ATOM 2567 CA ASN B 122 11.416 26.095 68.126 1.00 18.12 C ANISOU 2567 CA ASN B 122 2652 2081 2150 -50 185 -94 C ATOM 2568 C ASN B 122 10.239 25.496 67.353 1.00 19.72 C ANISOU 2568 C ASN B 122 2842 2305 2345 -7 182 -103 C ATOM 2569 O ASN B 122 9.519 26.209 66.651 1.00 21.19 O ANISOU 2569 O ASN B 122 3054 2481 2516 21 180 -96 O ATOM 2570 CB ASN B 122 12.522 26.493 67.145 1.00 24.57 C ANISOU 2570 CB ASN B 122 3472 2902 2962 -76 199 -72 C ATOM 2571 CG ASN B 122 13.722 27.098 67.838 1.00 34.25 C ANISOU 2571 CG ASN B 122 4701 4110 4204 -124 201 -71 C ATOM 2572 OD1 ASN B 122 14.857 26.671 67.623 1.00 41.87 O ANISOU 2572 OD1 ASN B 122 5633 5097 5177 -152 208 -71 O ATOM 2573 ND2 ASN B 122 13.480 28.093 68.681 1.00 31.48 N ANISOU 2573 ND2 ASN B 122 4384 3720 3857 -132 194 -77 N ATOM 2574 N GLY B 123 10.057 24.186 67.474 1.00 20.16 N ANISOU 2574 N GLY B 123 2860 2388 2412 -1 182 -120 N ATOM 2575 CA GLY B 123 8.945 23.512 66.831 1.00 21.10 C ANISOU 2575 CA GLY B 123 2958 2528 2532 33 178 -139 C ATOM 2576 C GLY B 123 7.965 23.016 67.877 1.00 16.42 C ANISOU 2576 C GLY B 123 2352 1929 1959 42 181 -162 C ATOM 2577 O GLY B 123 7.680 23.714 68.850 1.00 19.60 O ANISOU 2577 O GLY B 123 2777 2307 2361 41 182 -161 O ATOM 2578 N LEU B 124 7.463 21.802 67.690 1.00 17.08 N ANISOU 2578 N LEU B 124 2400 2033 2059 50 185 -184 N ATOM 2579 CA LEU B 124 6.525 21.202 68.636 1.00 12.51 C ANISOU 2579 CA LEU B 124 1805 1446 1502 54 198 -205 C ATOM 2580 C LEU B 124 6.716 19.695 68.686 1.00 12.48 C ANISOU 2580 C LEU B 124 1770 1452 1519 42 210 -217 C ATOM 2581 O LEU B 124 6.817 19.051 67.638 1.00 18.83 O ANISOU 2581 O LEU B 124 2551 2277 2327 48 205 -228 O ATOM 2582 CB LEU B 124 5.082 21.493 68.205 1.00 15.45 C ANISOU 2582 CB LEU B 124 2163 1827 1881 85 192 -231 C ATOM 2583 CG LEU B 124 3.939 20.840 69.001 1.00 14.64 C ANISOU 2583 CG LEU B 124 2033 1721 1808 88 213 -259 C ATOM 2584 CD1 LEU B 124 3.873 21.355 70.441 1.00 16.70 C ANISOU 2584 CD1 LEU B 124 2323 1957 2065 79 230 -248 C ATOM 2585 CD2 LEU B 124 2.589 21.060 68.288 1.00 13.78 C ANISOU 2585 CD2 LEU B 124 1894 1632 1709 121 201 -294 C ATOM 2586 N ILE B 125 6.760 19.135 69.891 1.00 14.93 N ANISOU 2586 N ILE B 125 2086 1745 1840 29 229 -214 N ATOM 2587 CA ILE B 125 6.768 17.686 70.060 1.00 14.33 C ANISOU 2587 CA ILE B 125 1989 1668 1787 21 247 -224 C ATOM 2588 C ILE B 125 5.549 17.242 70.862 1.00 13.58 C ANISOU 2588 C ILE B 125 1886 1557 1716 22 276 -241 C ATOM 2589 O ILE B 125 5.245 17.813 71.910 1.00 17.79 O ANISOU 2589 O ILE B 125 2443 2076 2240 23 287 -233 O ATOM 2590 CB ILE B 125 8.048 17.186 70.767 1.00 16.24 C ANISOU 2590 CB ILE B 125 2248 1902 2020 9 248 -200 C ATOM 2591 CG1 ILE B 125 9.299 17.849 70.174 1.00 16.69 C ANISOU 2591 CG1 ILE B 125 2311 1975 2056 4 224 -184 C ATOM 2592 CG2 ILE B 125 8.158 15.663 70.671 1.00 13.95 C ANISOU 2592 CG2 ILE B 125 1941 1607 1753 7 264 -209 C ATOM 2593 CD1 ILE B 125 10.602 17.320 70.761 1.00 17.47 C ANISOU 2593 CD1 ILE B 125 2415 2076 2149 -4 219 -169 C ATOM 2594 N LEU B 126 4.851 16.225 70.360 1.00 14.83 N ANISOU 2594 N LEU B 126 2010 1719 1908 19 290 -269 N ATOM 2595 CA LEU B 126 3.699 15.654 71.058 1.00 16.34 C ANISOU 2595 CA LEU B 126 2185 1893 2130 11 327 -289 C ATOM 2596 C LEU B 126 3.957 14.202 71.418 1.00 15.86 C ANISOU 2596 C LEU B 126 2124 1809 2094 -7 357 -287 C ATOM 2597 O LEU B 126 4.683 13.501 70.716 1.00 15.61 O ANISOU 2597 O LEU B 126 2085 1780 2065 -8 344 -288 O ATOM 2598 CB LEU B 126 2.451 15.712 70.180 1.00 15.86 C ANISOU 2598 CB LEU B 126 2076 1852 2096 20 321 -334 C ATOM 2599 CG LEU B 126 1.996 17.092 69.708 1.00 17.38 C ANISOU 2599 CG LEU B 126 2270 2068 2267 48 290 -340 C ATOM 2600 CD1 LEU B 126 0.834 16.935 68.742 1.00 17.97 C ANISOU 2600 CD1 LEU B 126 2292 2169 2369 64 277 -391 C ATOM 2601 CD2 LEU B 126 1.593 17.963 70.899 1.00 15.60 C ANISOU 2601 CD2 LEU B 126 2070 1826 2030 53 307 -327 C ATOM 2602 N SER B 127 3.345 13.748 72.508 1.00 16.94 N ANISOU 2602 N SER B 127 2272 1919 2246 -18 401 -283 N ATOM 2603 CA SER B 127 3.449 12.353 72.906 1.00 15.05 C ANISOU 2603 CA SER B 127 2039 1646 2032 -35 439 -279 C ATOM 2604 C SER B 127 2.156 11.874 73.551 1.00 16.52 C ANISOU 2604 C SER B 127 2211 1810 2257 -54 494 -297 C ATOM 2605 O SER B 127 1.479 12.636 74.245 1.00 20.22 O ANISOU 2605 O SER B 127 2684 2282 2716 -50 511 -297 O ATOM 2606 CB SER B 127 4.605 12.144 73.884 1.00 19.16 C ANISOU 2606 CB SER B 127 2615 2148 2516 -26 441 -233 C ATOM 2607 OG SER B 127 4.661 10.788 74.285 1.00 19.65 O ANISOU 2607 OG SER B 127 2692 2172 2601 -35 480 -224 O ATOM 2608 N GLU B 128 1.831 10.603 73.328 1.00 15.53 N ANISOU 2608 N GLU B 128 2067 1658 2177 -76 527 -316 N ATOM 2609 CA GLU B 128 0.647 9.985 73.918 1.00 18.37 C ANISOU 2609 CA GLU B 128 2410 1989 2583 -103 591 -335 C ATOM 2610 C GLU B 128 0.957 9.463 75.324 1.00 18.50 C ANISOU 2610 C GLU B 128 2490 1960 2580 -107 644 -286 C ATOM 2611 O GLU B 128 0.052 9.100 76.078 1.00 20.50 O ANISOU 2611 O GLU B 128 2744 2188 2859 -128 707 -289 O ATOM 2612 CB GLU B 128 0.161 8.842 73.010 1.00 21.15 C ANISOU 2612 CB GLU B 128 2714 2326 2997 -130 603 -382 C ATOM 2613 CG GLU B 128 -1.256 8.369 73.260 1.00 25.85 C ANISOU 2613 CG GLU B 128 3265 2904 3655 -165 662 -422 C ATOM 2614 CD GLU B 128 -1.746 7.394 72.202 1.00 23.16 C ANISOU 2614 CD GLU B 128 2866 2556 3378 -192 661 -482 C ATOM 2615 OE1 GLU B 128 -2.888 6.915 72.328 1.00 22.34 O ANISOU 2615 OE1 GLU B 128 2717 2436 3335 -228 709 -524 O ATOM 2616 OE2 GLU B 128 -0.996 7.102 71.243 1.00 22.85 O ANISOU 2616 OE2 GLU B 128 2825 2527 3329 -178 614 -491 O ATOM 2617 N TYR B 129 2.238 9.449 75.681 1.00 17.67 N ANISOU 2617 N TYR B 129 2438 1850 2427 -83 618 -243 N ATOM 2618 CA TYR B 129 2.690 8.863 76.941 1.00 21.82 C ANISOU 2618 CA TYR B 129 3031 2336 2924 -75 658 -194 C ATOM 2619 C TYR B 129 3.211 9.914 77.919 1.00 19.39 C ANISOU 2619 C TYR B 129 2769 2047 2550 -47 638 -161 C ATOM 2620 O TYR B 129 4.048 10.746 77.561 1.00 16.16 O ANISOU 2620 O TYR B 129 2359 1673 2109 -27 577 -158 O ATOM 2621 CB TYR B 129 3.755 7.806 76.652 1.00 21.35 C ANISOU 2621 CB TYR B 129 2997 2251 2864 -65 645 -176 C ATOM 2622 CG TYR B 129 3.362 6.941 75.483 1.00 17.57 C ANISOU 2622 CG TYR B 129 2468 1760 2447 -90 649 -219 C ATOM 2623 CD1 TYR B 129 2.451 5.908 75.640 1.00 20.74 C ANISOU 2623 CD1 TYR B 129 2862 2114 2905 -124 715 -235 C ATOM 2624 CD2 TYR B 129 3.869 7.184 74.210 1.00 19.61 C ANISOU 2624 CD2 TYR B 129 2686 2056 2708 -82 590 -247 C ATOM 2625 CE1 TYR B 129 2.072 5.126 74.568 1.00 22.48 C ANISOU 2625 CE1 TYR B 129 3034 2324 3185 -149 715 -284 C ATOM 2626 CE2 TYR B 129 3.491 6.413 73.137 1.00 20.60 C ANISOU 2626 CE2 TYR B 129 2767 2175 2885 -101 590 -292 C ATOM 2627 CZ TYR B 129 2.593 5.382 73.322 1.00 22.00 C ANISOU 2627 CZ TYR B 129 2935 2304 3121 -134 650 -314 C ATOM 2628 OH TYR B 129 2.217 4.600 72.250 1.00 21.77 O ANISOU 2628 OH TYR B 129 2860 2267 3146 -155 647 -367 O ATOM 2629 N GLU B 130 2.713 9.864 79.152 1.00 19.14 N ANISOU 2629 N GLU B 130 2778 1992 2500 -46 692 -137 N ATOM 2630 CA GLU B 130 2.984 10.906 80.140 1.00 18.60 C ANISOU 2630 CA GLU B 130 2752 1944 2371 -19 677 -115 C ATOM 2631 C GLU B 130 4.440 10.967 80.593 1.00 20.75 C ANISOU 2631 C GLU B 130 3076 2222 2586 15 630 -80 C ATOM 2632 O GLU B 130 5.069 12.028 80.536 1.00 18.90 O ANISOU 2632 O GLU B 130 2841 2021 2318 31 574 -84 O ATOM 2633 CB GLU B 130 2.082 10.760 81.371 1.00 21.81 C ANISOU 2633 CB GLU B 130 3194 2326 2768 -23 752 -99 C ATOM 2634 CG GLU B 130 2.304 11.882 82.394 1.00 21.87 C ANISOU 2634 CG GLU B 130 3245 2356 2709 8 736 -84 C ATOM 2635 CD GLU B 130 1.491 11.723 83.677 1.00 28.11 C ANISOU 2635 CD GLU B 130 4079 3125 3478 10 814 -65 C ATOM 2636 OE1 GLU B 130 1.047 12.753 84.227 1.00 31.25 O ANISOU 2636 OE1 GLU B 130 4482 3545 3847 22 815 -76 O ATOM 2637 OE2 GLU B 130 1.317 10.581 84.150 1.00 31.26 O ANISOU 2637 OE2 GLU B 130 4512 3481 3885 1 876 -38 O ATOM 2638 N LYS B 131 4.972 9.837 81.047 1.00 21.64 N ANISOU 2638 N LYS B 131 3233 2300 2689 27 653 -48 N ATOM 2639 CA LYS B 131 6.305 9.828 81.638 1.00 19.98 C ANISOU 2639 CA LYS B 131 3074 2098 2421 67 610 -17 C ATOM 2640 C LYS B 131 6.864 8.419 81.765 1.00 24.89 C ANISOU 2640 C LYS B 131 3731 2678 3046 83 630 12 C ATOM 2641 O LYS B 131 6.128 7.434 81.689 1.00 21.42 O ANISOU 2641 O LYS B 131 3296 2194 2648 61 692 15 O ATOM 2642 CB LYS B 131 6.258 10.483 83.019 1.00 24.92 C ANISOU 2642 CB LYS B 131 3756 2729 2983 94 621 5 C ATOM 2643 CG LYS B 131 5.421 9.707 84.023 1.00 27.19 C ANISOU 2643 CG LYS B 131 4096 2973 3264 93 705 34 C ATOM 2644 CD LYS B 131 5.266 10.469 85.333 1.00 28.84 C ANISOU 2644 CD LYS B 131 4358 3194 3405 120 717 50 C ATOM 2645 CE LYS B 131 4.517 9.642 86.366 1.00 32.57 C ANISOU 2645 CE LYS B 131 4891 3622 3862 123 809 85 C ATOM 2646 NZ LYS B 131 4.322 10.419 87.626 1.00 35.38 N ANISOU 2646 NZ LYS B 131 5301 3995 4147 153 823 97 N ATOM 2647 N ASP B 132 8.174 8.334 81.956 1.00 25.72 N ANISOU 2647 N ASP B 132 3863 2798 3110 122 578 30 N ATOM 2648 CA ASP B 132 8.825 7.062 82.232 1.00 27.72 C ANISOU 2648 CA ASP B 132 4162 3014 3355 152 590 61 C ATOM 2649 C ASP B 132 8.392 5.981 81.252 1.00 27.40 C ANISOU 2649 C ASP B 132 4092 2935 3385 122 624 46 C ATOM 2650 O ASP B 132 8.220 4.821 81.632 1.00 27.14 O ANISOU 2650 O ASP B 132 4104 2845 3362 129 676 72 O ATOM 2651 CB ASP B 132 8.520 6.622 83.666 1.00 30.73 C ANISOU 2651 CB ASP B 132 4628 3358 3688 179 644 106 C ATOM 2652 CG ASP B 132 9.540 5.635 84.202 1.00 37.55 C ANISOU 2652 CG ASP B 132 5557 4197 4515 234 632 145 C ATOM 2653 OD1 ASP B 132 10.710 5.690 83.768 1.00 34.43 O ANISOU 2653 OD1 ASP B 132 5140 3833 4107 263 562 135 O ATOM 2654 OD2 ASP B 132 9.171 4.806 85.062 1.00 41.92 O ANISOU 2654 OD2 ASP B 132 6182 4698 5048 251 694 186 O ATOM 2655 N PHE B 133 8.227 6.364 79.990 1.00 24.31 N ANISOU 2655 N PHE B 133 3627 2573 3039 91 596 3 N ATOM 2656 CA PHE B 133 7.820 5.420 78.958 1.00 23.82 C ANISOU 2656 CA PHE B 133 3529 2481 3042 62 620 -22 C ATOM 2657 C PHE B 133 8.839 5.390 77.828 1.00 24.08 C ANISOU 2657 C PHE B 133 3520 2546 3083 75 558 -44 C ATOM 2658 O PHE B 133 8.882 6.297 76.994 1.00 23.65 O ANISOU 2658 O PHE B 133 3412 2540 3034 61 517 -73 O ATOM 2659 CB PHE B 133 6.437 5.777 78.408 1.00 20.64 C ANISOU 2659 CB PHE B 133 3071 2080 2690 13 653 -61 C ATOM 2660 CG PHE B 133 5.831 4.698 77.558 1.00 23.41 C ANISOU 2660 CG PHE B 133 3391 2394 3111 -20 687 -92 C ATOM 2661 CD1 PHE B 133 6.106 4.627 76.199 1.00 25.47 C ANISOU 2661 CD1 PHE B 133 3596 2680 3403 -27 644 -132 C ATOM 2662 CD2 PHE B 133 5.012 3.737 78.121 1.00 22.98 C ANISOU 2662 CD2 PHE B 133 3365 2275 3091 -44 765 -82 C ATOM 2663 CE1 PHE B 133 5.559 3.620 75.417 1.00 26.16 C ANISOU 2663 CE1 PHE B 133 3653 2732 3553 -56 672 -168 C ATOM 2664 CE2 PHE B 133 4.460 2.735 77.343 1.00 24.26 C ANISOU 2664 CE2 PHE B 133 3496 2398 3323 -79 797 -116 C ATOM 2665 CZ PHE B 133 4.737 2.676 75.991 1.00 22.13 C ANISOU 2665 CZ PHE B 133 3169 2157 3083 -84 747 -162 C ATOM 2666 N MET B 134 9.672 4.355 77.818 1.00 19.63 N ANISOU 2666 N MET B 134 2985 1955 2517 105 553 -27 N ATOM 2667 CA MET B 134 10.622 4.159 76.732 1.00 21.14 C ANISOU 2667 CA MET B 134 3138 2175 2721 119 504 -50 C ATOM 2668 C MET B 134 9.922 3.559 75.517 1.00 20.98 C ANISOU 2668 C MET B 134 3071 2137 2764 83 524 -92 C ATOM 2669 O MET B 134 8.933 2.847 75.663 1.00 21.31 O ANISOU 2669 O MET B 134 3124 2127 2846 55 580 -98 O ATOM 2670 CB MET B 134 11.759 3.252 77.189 1.00 25.03 C ANISOU 2670 CB MET B 134 3677 2645 3187 172 490 -20 C ATOM 2671 CG MET B 134 12.723 3.906 78.175 1.00 21.58 C ANISOU 2671 CG MET B 134 3271 2244 2684 216 447 10 C ATOM 2672 SD MET B 134 13.841 5.076 77.381 1.00 35.93 S ANISOU 2672 SD MET B 134 5020 4146 4485 219 369 -19 S ATOM 2673 CE MET B 134 14.895 3.961 76.457 1.00 41.33 C ANISOU 2673 CE MET B 134 5684 4828 5193 252 347 -32 C ATOM 2674 N PRO B 135 10.452 3.834 74.309 1.00 18.65 N ANISOU 2674 N PRO B 135 2722 1885 2478 83 479 -125 N ATOM 2675 CA PRO B 135 9.852 3.298 73.083 1.00 20.53 C ANISOU 2675 CA PRO B 135 2915 2115 2770 55 488 -172 C ATOM 2676 C PRO B 135 9.791 1.775 73.097 1.00 26.14 C ANISOU 2676 C PRO B 135 3655 2757 3519 59 527 -173 C ATOM 2677 O PRO B 135 10.713 1.109 73.578 1.00 25.98 O ANISOU 2677 O PRO B 135 3680 2714 3479 99 523 -143 O ATOM 2678 CB PRO B 135 10.813 3.756 71.970 1.00 19.04 C ANISOU 2678 CB PRO B 135 2684 1986 2566 72 432 -193 C ATOM 2679 CG PRO B 135 11.723 4.770 72.585 1.00 20.60 C ANISOU 2679 CG PRO B 135 2892 2225 2709 94 396 -162 C ATOM 2680 CD PRO B 135 11.742 4.497 74.065 1.00 19.93 C ANISOU 2680 CD PRO B 135 2868 2103 2600 113 420 -119 C ATOM 2681 N ILE B 136 8.716 1.236 72.539 1.00 25.39 N ANISOU 2681 N ILE B 136 3535 2631 3481 19 562 -213 N ATOM 2682 CA ILE B 136 8.530 -0.201 72.450 1.00 28.04 C ANISOU 2682 CA ILE B 136 3895 2894 3864 13 604 -223 C ATOM 2683 C ILE B 136 7.807 -0.482 71.141 1.00 28.71 C ANISOU 2683 C ILE B 136 3917 2986 4005 -23 600 -293 C ATOM 2684 O ILE B 136 7.213 0.425 70.557 1.00 27.34 O ANISOU 2684 O ILE B 136 3691 2866 3832 -44 577 -325 O ATOM 2685 CB ILE B 136 7.694 -0.727 73.639 1.00 32.54 C ANISOU 2685 CB ILE B 136 4518 3394 4453 -10 677 -191 C ATOM 2686 CG1 ILE B 136 7.883 -2.234 73.817 1.00 35.73 C ANISOU 2686 CG1 ILE B 136 4974 3711 4891 -1 720 -181 C ATOM 2687 CG2 ILE B 136 6.224 -0.365 73.467 1.00 32.59 C ANISOU 2687 CG2 ILE B 136 4477 3402 4505 -68 712 -230 C ATOM 2688 CD1 ILE B 136 9.093 -2.600 74.650 1.00 41.44 C ANISOU 2688 CD1 ILE B 136 5770 4415 5560 63 708 -121 C ATOM 2689 N LYS B 137 7.866 -1.725 70.675 1.00 28.68 N ANISOU 2689 N LYS B 137 3922 2928 4045 -25 620 -318 N ATOM 2690 CA LYS B 137 7.255 -2.090 69.397 1.00 29.76 C ANISOU 2690 CA LYS B 137 4001 3072 4233 -54 611 -392 C ATOM 2691 C LYS B 137 5.862 -1.481 69.230 1.00 24.93 C ANISOU 2691 C LYS B 137 3338 2482 3654 -104 625 -432 C ATOM 2692 O LYS B 137 5.557 -0.871 68.209 1.00 21.77 O ANISOU 2692 O LYS B 137 2878 2142 3253 -109 583 -480 O ATOM 2693 CB LYS B 137 7.178 -3.608 69.249 1.00 31.07 C ANISOU 2693 CB LYS B 137 4196 3154 4457 -64 650 -415 C ATOM 2694 CG LYS B 137 6.524 -4.054 67.952 1.00 33.72 C ANISOU 2694 CG LYS B 137 4471 3493 4848 -94 639 -500 C ATOM 2695 CD LYS B 137 6.246 -5.548 67.954 1.00 40.98 C ANISOU 2695 CD LYS B 137 5420 4315 5836 -116 690 -526 C ATOM 2696 CE LYS B 137 5.272 -5.920 66.849 1.00 45.42 C ANISOU 2696 CE LYS B 137 5916 4878 6464 -162 686 -620 C ATOM 2697 NZ LYS B 137 5.706 -5.381 65.531 1.00 48.02 N ANISOU 2697 NZ LYS B 137 6192 5293 6758 -132 613 -667 N ATOM 2698 N GLY B 138 5.023 -1.639 70.246 1.00 25.83 N ANISOU 2698 N GLY B 138 3474 2547 3793 -137 685 -410 N ATOM 2699 CA GLY B 138 3.672 -1.112 70.191 1.00 26.91 C ANISOU 2699 CA GLY B 138 3556 2702 3965 -183 705 -449 C ATOM 2700 C GLY B 138 3.596 0.403 70.091 1.00 28.96 C ANISOU 2700 C GLY B 138 3784 3046 4175 -167 658 -443 C ATOM 2701 O GLY B 138 2.700 0.940 69.429 1.00 24.85 O ANISOU 2701 O GLY B 138 3200 2567 3676 -188 641 -495 O ATOM 2702 N SER B 139 4.526 1.103 70.738 1.00 24.53 N ANISOU 2702 N SER B 139 3264 2509 3546 -129 635 -382 N ATOM 2703 CA SER B 139 4.480 2.566 70.741 1.00 19.25 C ANISOU 2703 CA SER B 139 2574 1910 2831 -116 596 -372 C ATOM 2704 C SER B 139 4.892 3.204 69.404 1.00 23.01 C ANISOU 2704 C SER B 139 3004 2453 3286 -97 529 -407 C ATOM 2705 O SER B 139 4.424 4.294 69.072 1.00 20.74 O ANISOU 2705 O SER B 139 2684 2217 2981 -96 502 -421 O ATOM 2706 CB SER B 139 5.276 3.156 71.913 1.00 19.54 C ANISOU 2706 CB SER B 139 2668 1950 2806 -87 595 -303 C ATOM 2707 OG SER B 139 6.671 2.982 71.769 1.00 23.18 O ANISOU 2707 OG SER B 139 3157 2421 3229 -47 557 -277 O ATOM 2708 N PHE B 140 5.756 2.536 68.642 1.00 20.77 N ANISOU 2708 N PHE B 140 2723 2168 3000 -77 506 -418 N ATOM 2709 CA PHE B 140 6.109 3.024 67.313 1.00 18.80 C ANISOU 2709 CA PHE B 140 2433 1979 2729 -58 451 -452 C ATOM 2710 C PHE B 140 4.897 2.965 66.403 1.00 17.57 C ANISOU 2710 C PHE B 140 2221 1840 2616 -83 446 -522 C ATOM 2711 O PHE B 140 4.602 3.913 65.680 1.00 19.21 O ANISOU 2711 O PHE B 140 2394 2105 2799 -72 407 -543 O ATOM 2712 CB PHE B 140 7.240 2.202 66.679 1.00 16.95 C ANISOU 2712 CB PHE B 140 2211 1739 2488 -31 434 -457 C ATOM 2713 CG PHE B 140 8.573 2.408 67.318 1.00 18.54 C ANISOU 2713 CG PHE B 140 2454 1946 2642 2 422 -398 C ATOM 2714 CD1 PHE B 140 9.269 3.592 67.135 1.00 16.29 C ANISOU 2714 CD1 PHE B 140 2162 1722 2305 21 384 -375 C ATOM 2715 CD2 PHE B 140 9.138 1.415 68.102 1.00 20.24 C ANISOU 2715 CD2 PHE B 140 2717 2106 2867 16 449 -368 C ATOM 2716 CE1 PHE B 140 10.502 3.778 67.723 1.00 19.84 C ANISOU 2716 CE1 PHE B 140 2641 2181 2718 49 371 -330 C ATOM 2717 CE2 PHE B 140 10.367 1.596 68.684 1.00 19.98 C ANISOU 2717 CE2 PHE B 140 2716 2085 2791 53 432 -321 C ATOM 2718 CZ PHE B 140 11.050 2.775 68.499 1.00 16.75 C ANISOU 2718 CZ PHE B 140 2289 1740 2334 67 391 -305 C ATOM 2719 N LEU B 141 4.201 1.836 66.435 1.00 18.65 N ANISOU 2719 N LEU B 141 2347 1923 2815 -114 484 -560 N ATOM 2720 CA LEU B 141 3.039 1.641 65.579 1.00 24.39 C ANISOU 2720 CA LEU B 141 3012 2663 3591 -139 477 -638 C ATOM 2721 C LEU B 141 1.892 2.567 65.985 1.00 22.74 C ANISOU 2721 C LEU B 141 2770 2481 3391 -158 485 -647 C ATOM 2722 O LEU B 141 1.198 3.117 65.128 1.00 21.88 O ANISOU 2722 O LEU B 141 2607 2423 3283 -153 448 -698 O ATOM 2723 CB LEU B 141 2.609 0.169 65.583 1.00 29.51 C ANISOU 2723 CB LEU B 141 3659 3240 4314 -175 521 -679 C ATOM 2724 CG LEU B 141 3.705 -0.813 65.138 1.00 35.71 C ANISOU 2724 CG LEU B 141 4478 3995 5094 -151 513 -677 C ATOM 2725 CD1 LEU B 141 3.125 -2.198 64.888 1.00 38.62 C ANISOU 2725 CD1 LEU B 141 4836 4294 5542 -188 550 -735 C ATOM 2726 CD2 LEU B 141 4.441 -0.312 63.897 1.00 37.46 C ANISOU 2726 CD2 LEU B 141 4680 4290 5265 -109 447 -698 C ATOM 2727 N ALA B 142 1.715 2.759 67.291 1.00 20.90 N ANISOU 2727 N ALA B 142 2570 2215 3157 -173 531 -596 N ATOM 2728 CA ALA B 142 0.718 3.697 67.799 1.00 20.20 C ANISOU 2728 CA ALA B 142 2455 2151 3070 -185 542 -598 C ATOM 2729 C ALA B 142 1.026 5.124 67.332 1.00 20.44 C ANISOU 2729 C ALA B 142 2477 2252 3036 -145 482 -584 C ATOM 2730 O ALA B 142 0.152 5.834 66.830 1.00 17.27 O ANISOU 2730 O ALA B 142 2027 1894 2639 -141 457 -624 O ATOM 2731 CB ALA B 142 0.678 3.639 69.318 1.00 20.64 C ANISOU 2731 CB ALA B 142 2561 2159 3123 -200 603 -539 C ATOM 2732 N ARG B 143 2.278 5.532 67.524 1.00 19.85 N ANISOU 2732 N ARG B 143 2452 2188 2904 -115 460 -527 N ATOM 2733 CA ARG B 143 2.773 6.836 67.087 1.00 19.18 C ANISOU 2733 CA ARG B 143 2369 2160 2758 -81 409 -507 C ATOM 2734 C ARG B 143 2.476 7.092 65.608 1.00 22.28 C ANISOU 2734 C ARG B 143 2717 2604 3147 -64 360 -561 C ATOM 2735 O ARG B 143 2.085 8.200 65.220 1.00 17.74 O ANISOU 2735 O ARG B 143 2125 2073 2543 -44 329 -567 O ATOM 2736 CB ARG B 143 4.286 6.901 67.334 1.00 20.76 C ANISOU 2736 CB ARG B 143 2619 2357 2910 -59 396 -452 C ATOM 2737 CG ARG B 143 4.960 8.217 66.956 1.00 23.97 C ANISOU 2737 CG ARG B 143 3034 2814 3258 -32 352 -425 C ATOM 2738 CD ARG B 143 5.389 8.260 65.491 1.00 24.48 C ANISOU 2738 CD ARG B 143 3076 2921 3305 -11 311 -453 C ATOM 2739 NE ARG B 143 6.421 7.282 65.154 1.00 23.83 N ANISOU 2739 NE ARG B 143 3005 2825 3223 -4 312 -451 N ATOM 2740 CZ ARG B 143 7.706 7.406 65.471 1.00 24.34 C ANISOU 2740 CZ ARG B 143 3100 2892 3255 11 306 -407 C ATOM 2741 NH1 ARG B 143 8.122 8.457 66.166 1.00 23.35 N ANISOU 2741 NH1 ARG B 143 2997 2779 3096 14 300 -364 N ATOM 2742 NH2 ARG B 143 8.575 6.472 65.109 1.00 26.53 N ANISOU 2742 NH2 ARG B 143 3383 3161 3537 22 306 -411 N ATOM 2743 N ASN B 144 2.676 6.069 64.785 1.00 21.98 N ANISOU 2743 N ASN B 144 2662 2557 3132 -67 354 -600 N ATOM 2744 CA ASN B 144 2.490 6.205 63.346 1.00 25.24 C ANISOU 2744 CA ASN B 144 3037 3019 3532 -44 306 -653 C ATOM 2745 C ASN B 144 1.076 6.660 63.001 1.00 25.18 C ANISOU 2745 C ASN B 144 2975 3042 3549 -47 291 -709 C ATOM 2746 O ASN B 144 0.887 7.509 62.125 1.00 25.99 O ANISOU 2746 O ASN B 144 3062 3201 3614 -13 244 -726 O ATOM 2747 CB ASN B 144 2.830 4.900 62.612 1.00 25.86 C ANISOU 2747 CB ASN B 144 3107 3078 3639 -49 306 -695 C ATOM 2748 CG ASN B 144 4.320 4.570 62.647 1.00 27.18 C ANISOU 2748 CG ASN B 144 3322 3234 3772 -30 306 -648 C ATOM 2749 OD1 ASN B 144 5.144 5.393 63.048 1.00 21.67 O ANISOU 2749 OD1 ASN B 144 2655 2553 3026 -13 299 -589 O ATOM 2750 ND2 ASN B 144 4.667 3.359 62.218 1.00 28.91 N ANISOU 2750 ND2 ASN B 144 3541 3425 4020 -33 314 -679 N ATOM 2751 N ARG B 145 0.084 6.102 63.691 1.00 23.22 N ANISOU 2751 N ARG B 145 2700 2758 3365 -86 332 -737 N ATOM 2752 CA ARG B 145 -1.309 6.467 63.437 1.00 19.78 C ANISOU 2752 CA ARG B 145 2202 2353 2962 -91 321 -797 C ATOM 2753 C ARG B 145 -1.561 7.947 63.714 1.00 19.27 C ANISOU 2753 C ARG B 145 2144 2327 2850 -60 300 -764 C ATOM 2754 O ARG B 145 -2.375 8.576 63.042 1.00 22.75 O ANISOU 2754 O ARG B 145 2541 2816 3286 -35 260 -809 O ATOM 2755 CB ARG B 145 -2.278 5.590 64.249 1.00 21.65 C ANISOU 2755 CB ARG B 145 2406 2538 3281 -146 382 -829 C ATOM 2756 CG ARG B 145 -2.733 6.172 65.584 1.00 22.17 C ANISOU 2756 CG ARG B 145 2487 2585 3352 -162 430 -785 C ATOM 2757 CD ARG B 145 -3.416 5.094 66.419 1.00 21.95 C ANISOU 2757 CD ARG B 145 2445 2494 3402 -220 506 -803 C ATOM 2758 NE ARG B 145 -4.104 5.596 67.608 1.00 23.46 N ANISOU 2758 NE ARG B 145 2637 2673 3604 -238 557 -777 N ATOM 2759 CZ ARG B 145 -3.488 6.079 68.684 1.00 24.62 C ANISOU 2759 CZ ARG B 145 2850 2800 3705 -227 583 -699 C ATOM 2760 NH1 ARG B 145 -2.167 6.158 68.707 1.00 21.88 N ANISOU 2760 NH1 ARG B 145 2567 2445 3300 -200 559 -641 N ATOM 2761 NH2 ARG B 145 -4.192 6.500 69.730 1.00 23.89 N ANISOU 2761 NH2 ARG B 145 2757 2699 3622 -241 631 -682 N ATOM 2762 N LEU B 146 -0.853 8.502 64.694 1.00 19.26 N ANISOU 2762 N LEU B 146 2198 2304 2814 -59 322 -689 N ATOM 2763 CA LEU B 146 -0.990 9.923 65.022 1.00 21.12 C ANISOU 2763 CA LEU B 146 2450 2569 3006 -31 304 -656 C ATOM 2764 C LEU B 146 -0.364 10.811 63.943 1.00 18.36 C ANISOU 2764 C LEU B 146 2117 2267 2592 16 246 -643 C ATOM 2765 O LEU B 146 -0.878 11.888 63.639 1.00 21.93 O ANISOU 2765 O LEU B 146 2562 2754 3018 48 215 -648 O ATOM 2766 CB LEU B 146 -0.362 10.241 66.384 1.00 18.39 C ANISOU 2766 CB LEU B 146 2161 2186 2640 -43 343 -584 C ATOM 2767 CG LEU B 146 -0.791 9.436 67.618 1.00 21.66 C ANISOU 2767 CG LEU B 146 2580 2548 3101 -84 410 -577 C ATOM 2768 CD1 LEU B 146 -0.004 9.897 68.851 1.00 24.41 C ANISOU 2768 CD1 LEU B 146 2994 2871 3409 -81 433 -504 C ATOM 2769 CD2 LEU B 146 -2.297 9.507 67.892 1.00 19.68 C ANISOU 2769 CD2 LEU B 146 2273 2303 2901 -102 436 -626 C ATOM 2770 N VAL B 147 0.759 10.370 63.382 1.00 15.65 N ANISOU 2770 N VAL B 147 1801 1922 2223 21 234 -625 N ATOM 2771 CA VAL B 147 1.375 11.104 62.280 1.00 14.04 C ANISOU 2771 CA VAL B 147 1614 1762 1959 62 187 -614 C ATOM 2772 C VAL B 147 0.396 11.176 61.120 1.00 18.77 C ANISOU 2772 C VAL B 147 2165 2406 2559 91 146 -681 C ATOM 2773 O VAL B 147 0.170 12.240 60.541 1.00 21.49 O ANISOU 2773 O VAL B 147 2517 2789 2859 131 110 -677 O ATOM 2774 CB VAL B 147 2.661 10.424 61.784 1.00 14.10 C ANISOU 2774 CB VAL B 147 1647 1765 1947 62 187 -596 C ATOM 2775 CG1 VAL B 147 3.131 11.063 60.479 1.00 15.77 C ANISOU 2775 CG1 VAL B 147 1869 2025 2099 103 145 -596 C ATOM 2776 CG2 VAL B 147 3.756 10.506 62.848 1.00 17.44 C ANISOU 2776 CG2 VAL B 147 2116 2153 2357 45 216 -529 C ATOM 2777 N ILE B 148 -0.190 10.033 60.790 1.00 16.49 N ANISOU 2777 N ILE B 148 1831 2113 2323 71 150 -746 N ATOM 2778 CA ILE B 148 -1.122 9.946 59.666 1.00 21.84 C ANISOU 2778 CA ILE B 148 2456 2837 3006 98 105 -823 C ATOM 2779 C ILE B 148 -2.375 10.772 59.912 1.00 29.33 C ANISOU 2779 C ILE B 148 3367 3810 3968 114 91 -849 C ATOM 2780 O ILE B 148 -2.786 11.565 59.062 1.00 33.73 O ANISOU 2780 O ILE B 148 3915 4418 4483 166 40 -870 O ATOM 2781 CB ILE B 148 -1.522 8.488 59.383 1.00 26.83 C ANISOU 2781 CB ILE B 148 3041 3449 3703 64 116 -895 C ATOM 2782 CG1 ILE B 148 -0.319 7.696 58.863 1.00 25.18 C ANISOU 2782 CG1 ILE B 148 2866 3226 3474 64 118 -881 C ATOM 2783 CG2 ILE B 148 -2.690 8.431 58.401 1.00 26.01 C ANISOU 2783 CG2 ILE B 148 2870 3395 3616 88 68 -987 C ATOM 2784 CD1 ILE B 148 0.506 8.425 57.821 1.00 29.45 C ANISOU 2784 CD1 ILE B 148 3442 3815 3931 117 76 -855 C ATOM 2785 N ALA B 149 -2.975 10.588 61.085 1.00 27.88 N ANISOU 2785 N ALA B 149 3164 3590 3839 74 138 -847 N ATOM 2786 CA ALA B 149 -4.184 11.316 61.456 1.00 31.10 C ANISOU 2786 CA ALA B 149 3531 4019 4266 86 133 -874 C ATOM 2787 C ALA B 149 -3.996 12.832 61.414 1.00 29.16 C ANISOU 2787 C ALA B 149 3328 3800 3953 138 103 -824 C ATOM 2788 O ALA B 149 -4.855 13.553 60.913 1.00 30.06 O ANISOU 2788 O ALA B 149 3412 3957 4055 183 63 -859 O ATOM 2789 CB ALA B 149 -4.672 10.872 62.838 1.00 28.82 C ANISOU 2789 CB ALA B 149 3227 3682 4040 32 202 -867 C ATOM 2790 N LEU B 150 -2.875 13.316 61.942 1.00 25.43 N ANISOU 2790 N LEU B 150 2926 3298 3438 134 122 -744 N ATOM 2791 CA LEU B 150 -2.640 14.755 62.000 1.00 19.62 C ANISOU 2791 CA LEU B 150 2236 2575 2644 175 101 -694 C ATOM 2792 C LEU B 150 -2.365 15.357 60.623 1.00 21.00 C ANISOU 2792 C LEU B 150 2429 2793 2756 231 45 -696 C ATOM 2793 O LEU B 150 -2.670 16.520 60.384 1.00 25.02 O ANISOU 2793 O LEU B 150 2960 3322 3226 277 17 -680 O ATOM 2794 CB LEU B 150 -1.488 15.082 62.958 1.00 20.61 C ANISOU 2794 CB LEU B 150 2428 2658 2747 150 136 -615 C ATOM 2795 CG LEU B 150 -1.163 16.563 63.158 1.00 22.50 C ANISOU 2795 CG LEU B 150 2718 2897 2933 181 122 -563 C ATOM 2796 CD1 LEU B 150 -2.383 17.305 63.681 1.00 18.05 C ANISOU 2796 CD1 LEU B 150 2131 2341 2386 202 121 -585 C ATOM 2797 CD2 LEU B 150 0.022 16.735 64.112 1.00 21.86 C ANISOU 2797 CD2 LEU B 150 2693 2776 2836 150 154 -497 C ATOM 2798 N SER B 151 -1.793 14.566 59.717 1.00 24.95 N ANISOU 2798 N SER B 151 2779 3983 2718 261 -71 -1311 N ATOM 2799 CA SER B 151 -1.323 15.103 58.442 1.00 27.37 C ANISOU 2799 CA SER B 151 3038 4376 2984 290 -222 -1264 C ATOM 2800 C SER B 151 -2.402 15.118 57.366 1.00 32.91 C ANISOU 2800 C SER B 151 3569 5249 3686 265 -249 -1420 C ATOM 2801 O SER B 151 -3.281 14.257 57.347 1.00 38.76 O ANISOU 2801 O SER B 151 4227 6033 4468 186 -114 -1567 O ATOM 2802 CB SER B 151 -0.103 14.318 57.950 1.00 31.14 C ANISOU 2802 CB SER B 151 3582 4791 3459 234 -177 -1170 C ATOM 2803 OG SER B 151 0.923 14.336 58.934 1.00 33.87 O ANISOU 2803 OG SER B 151 4085 4979 3804 257 -159 -1016 O ATOM 2804 N ASP B 152 -2.326 16.103 56.473 1.00 27.19 N ANISOU 2804 N ASP B 152 2792 4621 2919 331 -429 -1384 N ATOM 2805 CA ASP B 152 -3.253 16.198 55.347 1.00 28.45 C ANISOU 2805 CA ASP B 152 2790 4948 3073 312 -475 -1517 C ATOM 2806 C ASP B 152 -2.754 15.408 54.140 1.00 28.10 C ANISOU 2806 C ASP B 152 2703 4957 3016 239 -448 -1532 C ATOM 2807 O ASP B 152 -3.546 14.887 53.355 1.00 28.47 O ANISOU 2807 O ASP B 152 2627 5115 3075 177 -403 -1676 O ATOM 2808 CB ASP B 152 -3.468 17.659 54.954 1.00 34.81 C ANISOU 2808 CB ASP B 152 3551 5837 3837 420 -686 -1473 C ATOM 2809 CG ASP B 152 -4.052 18.488 56.082 1.00 40.37 C ANISOU 2809 CG ASP B 152 4289 6499 4549 500 -721 -1472 C ATOM 2810 OD1 ASP B 152 -5.210 18.224 56.472 1.00 44.40 O ANISOU 2810 OD1 ASP B 152 4723 7055 5094 477 -630 -1612 O ATOM 2811 OD2 ASP B 152 -3.363 19.413 56.567 1.00 39.96 O ANISOU 2811 OD2 ASP B 152 4339 6372 4471 588 -842 -1333 O ATOM 2812 N VAL B 153 -1.436 15.345 53.992 1.00 30.15 N ANISOU 2812 N VAL B 153 3066 5139 3251 250 -479 -1383 N ATOM 2813 CA VAL B 153 -0.794 14.632 52.891 1.00 32.66 C ANISOU 2813 CA VAL B 153 3362 5497 3550 193 -456 -1376 C ATOM 2814 C VAL B 153 0.358 13.823 53.458 1.00 28.05 C ANISOU 2814 C VAL B 153 2914 4762 2982 156 -346 -1267 C ATOM 2815 O VAL B 153 0.984 14.242 54.428 1.00 28.19 O ANISOU 2815 O VAL B 153 3050 4660 3001 205 -368 -1138 O ATOM 2816 CB VAL B 153 -0.227 15.612 51.848 1.00 36.46 C ANISOU 2816 CB VAL B 153 3816 6069 3970 264 -651 -1275 C ATOM 2817 CG1 VAL B 153 0.589 14.867 50.803 1.00 36.76 C ANISOU 2817 CG1 VAL B 153 3849 6135 3982 214 -620 -1247 C ATOM 2818 CG2 VAL B 153 -1.352 16.397 51.188 1.00 40.51 C ANISOU 2818 CG2 VAL B 153 4187 6739 4468 298 -764 -1382 C ATOM 2819 N VAL B 154 0.635 12.666 52.866 1.00 27.54 N ANISOU 2819 N VAL B 154 2835 4700 2930 72 -230 -1320 N ATOM 2820 CA VAL B 154 1.747 11.842 53.323 1.00 27.03 C ANISOU 2820 CA VAL B 154 2894 4495 2883 34 -122 -1218 C ATOM 2821 C VAL B 154 2.768 11.583 52.216 1.00 25.84 C ANISOU 2821 C VAL B 154 2751 4377 2691 30 -161 -1141 C ATOM 2822 O VAL B 154 2.458 10.977 51.185 1.00 28.07 O ANISOU 2822 O VAL B 154 2944 4756 2964 -23 -126 -1252 O ATOM 2823 CB VAL B 154 1.258 10.513 53.906 1.00 29.82 C ANISOU 2823 CB VAL B 154 3249 4779 3301 -68 87 -1339 C ATOM 2824 CG1 VAL B 154 2.412 9.761 54.543 1.00 24.07 C ANISOU 2824 CG1 VAL B 154 2658 3893 2595 -97 192 -1220 C ATOM 2825 CG2 VAL B 154 0.172 10.774 54.934 1.00 30.16 C ANISOU 2825 CG2 VAL B 154 3269 4809 3380 -61 127 -1422 C ATOM 2826 N ILE B 155 3.988 12.061 52.439 1.00 25.81 N ANISOU 2826 N ILE B 155 2854 4292 2661 87 -236 -948 N ATOM 2827 CA ILE B 155 5.076 11.850 51.496 1.00 27.67 C ANISOU 2827 CA ILE B 155 3109 4548 2856 91 -271 -848 C ATOM 2828 C ILE B 155 6.025 10.798 52.046 1.00 28.34 C ANISOU 2828 C ILE B 155 3307 4486 2975 40 -124 -776 C ATOM 2829 O ILE B 155 6.545 10.943 53.155 1.00 28.84 O ANISOU 2829 O ILE B 155 3483 4413 3061 61 -104 -662 O ATOM 2830 CB ILE B 155 5.863 13.152 51.243 1.00 29.05 C ANISOU 2830 CB ILE B 155 3316 4744 2977 192 -472 -665 C ATOM 2831 CG1 ILE B 155 4.921 14.267 50.787 1.00 31.14 C ANISOU 2831 CG1 ILE B 155 3473 5144 3213 247 -625 -728 C ATOM 2832 CG2 ILE B 155 6.970 12.920 50.232 1.00 30.29 C ANISOU 2832 CG2 ILE B 155 3484 4934 3090 197 -504 -560 C ATOM 2833 CD1 ILE B 155 5.628 15.571 50.502 1.00 33.96 C ANISOU 2833 CD1 ILE B 155 3855 5527 3522 344 -831 -552 C ATOM 2834 N ILE B 156 6.244 9.738 51.272 1.00 27.20 N ANISOU 2834 N ILE B 156 3134 4368 2832 -24 -22 -843 N ATOM 2835 CA ILE B 156 7.185 8.691 51.650 1.00 29.01 C ANISOU 2835 CA ILE B 156 3464 4466 3092 -72 117 -776 C ATOM 2836 C ILE B 156 8.296 8.622 50.602 1.00 31.74 C ANISOU 2836 C ILE B 156 3822 4853 3387 -46 66 -668 C ATOM 2837 O ILE B 156 8.179 7.904 49.607 1.00 35.33 O ANISOU 2837 O ILE B 156 4211 5386 3826 -88 119 -770 O ATOM 2838 CB ILE B 156 6.486 7.317 51.802 1.00 28.92 C ANISOU 2838 CB ILE B 156 3423 4425 3142 -178 310 -954 C ATOM 2839 CG1 ILE B 156 5.362 7.401 52.842 1.00 31.03 C ANISOU 2839 CG1 ILE B 156 3671 4660 3458 -202 363 -1055 C ATOM 2840 CG2 ILE B 156 7.485 6.247 52.202 1.00 28.92 C ANISOU 2840 CG2 ILE B 156 3528 4282 3176 -224 451 -880 C ATOM 2841 CD1 ILE B 156 4.627 6.096 53.073 1.00 26.33 C ANISOU 2841 CD1 ILE B 156 3042 4033 2929 -309 547 -1223 C ATOM 2842 N PRO B 157 9.371 9.398 50.813 1.00 29.44 N ANISOU 2842 N PRO B 157 3611 4510 3065 27 -43 -459 N ATOM 2843 CA PRO B 157 10.469 9.528 49.843 1.00 29.47 C ANISOU 2843 CA PRO B 157 3622 4561 3014 66 -115 -329 C ATOM 2844 C PRO B 157 11.091 8.192 49.448 1.00 29.83 C ANISOU 2844 C PRO B 157 3696 4563 3073 6 40 -353 C ATOM 2845 O PRO B 157 11.327 7.955 48.260 1.00 29.84 O ANISOU 2845 O PRO B 157 3639 4671 3028 8 23 -379 O ATOM 2846 CB PRO B 157 11.486 10.391 50.587 1.00 27.31 C ANISOU 2846 CB PRO B 157 3457 4185 2733 136 -218 -98 C ATOM 2847 CG PRO B 157 10.661 11.197 51.537 1.00 30.77 C ANISOU 2847 CG PRO B 157 3900 4595 3194 161 -279 -129 C ATOM 2848 CD PRO B 157 9.560 10.278 51.981 1.00 30.38 C ANISOU 2848 CD PRO B 157 3815 4530 3199 80 -117 -334 C ATOM 2849 N GLN B 158 11.351 7.334 50.426 1.00 25.30 N ANISOU 2849 N GLN B 158 3212 3837 2562 -46 188 -344 N ATOM 2850 CA GLN B 158 11.957 6.027 50.167 1.00 29.17 C ANISOU 2850 CA GLN B 158 3740 4268 3076 -104 343 -364 C ATOM 2851 C GLN B 158 11.613 5.083 51.311 1.00 32.98 C ANISOU 2851 C GLN B 158 4281 4607 3641 -181 513 -437 C ATOM 2852 O GLN B 158 11.595 5.497 52.466 1.00 30.74 O ANISOU 2852 O GLN B 158 4066 4226 3389 -168 505 -365 O ATOM 2853 CB GLN B 158 13.479 6.154 50.041 1.00 28.34 C ANISOU 2853 CB GLN B 158 3721 4103 2943 -53 305 -143 C ATOM 2854 CG GLN B 158 14.218 4.817 49.982 1.00 30.29 C ANISOU 2854 CG GLN B 158 4026 4260 3222 -106 472 -140 C ATOM 2855 CD GLN B 158 15.721 4.957 50.185 1.00 27.92 C ANISOU 2855 CD GLN B 158 3827 3871 2911 -58 446 98 C ATOM 2856 OE1 GLN B 158 16.298 6.026 49.974 1.00 22.20 O ANISOU 2856 OE1 GLN B 158 3110 3189 2138 18 291 258 O ATOM 2857 NE2 GLN B 158 16.359 3.876 50.609 1.00 28.05 N ANISOU 2857 NE2 GLN B 158 3921 3760 2975 -104 598 127 N ATOM 2858 N ALA B 159 11.344 3.820 50.995 1.00 32.37 N ANISOU 2858 N ALA B 159 4181 4519 3599 -260 665 -577 N ATOM 2859 CA ALA B 159 11.006 2.847 52.029 1.00 30.86 C ANISOU 2859 CA ALA B 159 4040 4195 3491 -339 832 -648 C ATOM 2860 C ALA B 159 11.145 1.403 51.555 1.00 32.77 C ANISOU 2860 C ALA B 159 4279 4405 3768 -417 990 -752 C ATOM 2861 O ALA B 159 11.035 1.117 50.365 1.00 38.62 O ANISOU 2861 O ALA B 159 4948 5255 4470 -422 978 -842 O ATOM 2862 CB ALA B 159 9.599 3.097 52.543 1.00 30.71 C ANISOU 2862 CB ALA B 159 3953 4215 3502 -370 836 -798 C ATOM 2863 N ASP B 160 11.382 0.499 52.500 1.00 36.10 N ANISOU 2863 N ASP B 160 4781 4674 4263 -476 1137 -739 N ATOM 2864 CA ASP B 160 11.407 -0.931 52.218 1.00 46.33 C ANISOU 2864 CA ASP B 160 6078 5918 5607 -557 1299 -849 C ATOM 2865 C ASP B 160 10.020 -1.524 52.416 1.00 49.95 C ANISOU 2865 C ASP B 160 6459 6400 6121 -643 1385 -1064 C ATOM 2866 O ASP B 160 9.185 -0.945 53.108 1.00 51.50 O ANISOU 2866 O ASP B 160 6627 6609 6331 -643 1352 -1098 O ATOM 2867 CB ASP B 160 12.388 -1.647 53.147 1.00 49.12 C ANISOU 2867 CB ASP B 160 6556 6091 6018 -581 1416 -721 C ATOM 2868 CG ASP B 160 13.831 -1.316 52.843 1.00 53.36 C ANISOU 2868 CG ASP B 160 7167 6599 6509 -509 1355 -516 C ATOM 2869 OD1 ASP B 160 14.184 -1.213 51.650 1.00 54.61 O ANISOU 2869 OD1 ASP B 160 7279 6863 6606 -471 1295 -518 O ATOM 2870 OD2 ASP B 160 14.615 -1.162 53.805 1.00 54.93 O ANISOU 2870 OD2 ASP B 160 7467 6671 6733 -490 1367 -349 O ATOM 2871 N LEU B 161 9.782 -2.682 51.807 1.00 54.92 N ANISOU 2871 N LEU B 161 7054 7033 6780 -715 1495 -1206 N ATOM 2872 CA LEU B 161 8.541 -3.417 52.019 1.00 56.35 C ANISOU 2872 CA LEU B 161 7167 7217 7025 -808 1592 -1403 C ATOM 2873 C LEU B 161 8.430 -3.859 53.473 1.00 56.87 C ANISOU 2873 C LEU B 161 7301 7127 7179 -857 1693 -1357 C ATOM 2874 O LEU B 161 9.432 -3.931 54.186 1.00 55.90 O ANISOU 2874 O LEU B 161 7289 6882 7070 -838 1738 -1204 O ATOM 2875 CB LEU B 161 8.460 -4.629 51.088 1.00 59.28 C ANISOU 2875 CB LEU B 161 7501 7598 7425 -869 1651 -1518 C ATOM 2876 CG LEU B 161 7.921 -4.369 49.679 1.00 61.06 C ANISOU 2876 CG LEU B 161 7618 8000 7582 -854 1565 -1647 C ATOM 2877 CD1 LEU B 161 7.987 -5.630 48.831 1.00 61.85 C ANISOU 2877 CD1 LEU B 161 7702 8082 7714 -909 1617 -1731 C ATOM 2878 CD2 LEU B 161 6.495 -3.840 49.749 1.00 62.52 C ANISOU 2878 CD2 LEU B 161 7694 8285 7775 -877 1505 -1773 C ATOM 2879 N LYS B 162 7.208 -4.155 53.905 1.00 58.19 N ANISOU 2879 N LYS B 162 7401 7301 7409 -920 1712 -1472 N ATOM 2880 CA LYS B 162 6.938 -4.546 55.287 1.00 59.55 C ANISOU 2880 CA LYS B 162 7621 7341 7663 -968 1787 -1430 C ATOM 2881 C LYS B 162 7.789 -3.768 56.293 1.00 59.31 C ANISOU 2881 C LYS B 162 7702 7227 7607 -903 1783 -1258 C ATOM 2882 O LYS B 162 8.581 -4.344 57.040 1.00 63.24 O ANISOU 2882 O LYS B 162 8300 7577 8153 -921 1849 -1144 O ATOM 2883 CB LYS B 162 7.103 -6.060 55.478 1.00 61.82 C ANISOU 2883 CB LYS B 162 7940 7501 8046 -1060 1893 -1449 C ATOM 2884 CG LYS B 162 8.514 -6.588 55.269 1.00 62.26 C ANISOU 2884 CG LYS B 162 8097 7460 8100 -1040 1929 -1331 C ATOM 2885 CD LYS B 162 8.633 -8.039 55.713 1.00 63.74 C ANISOU 2885 CD LYS B 162 8327 7501 8391 -1130 2034 -1347 C ATOM 2886 CE LYS B 162 7.898 -8.971 54.767 1.00 65.51 C ANISOU 2886 CE LYS B 162 8460 7784 8649 -1206 2062 -1511 C ATOM 2887 NZ LYS B 162 8.515 -8.947 53.412 1.00 65.16 N ANISOU 2887 NZ LYS B 162 8399 7825 8533 -1159 2019 -1526 N ATOM 2888 N SER B 163 7.616 -2.451 56.307 1.00 53.09 N ANISOU 2888 N SER B 163 6896 6529 6746 -826 1681 -1229 N ATOM 2889 CA SER B 163 8.352 -1.595 57.225 1.00 47.27 C ANISOU 2889 CA SER B 163 6258 5715 5987 -754 1616 -1038 C ATOM 2890 C SER B 163 7.388 -0.701 57.993 1.00 41.29 C ANISOU 2890 C SER B 163 5467 4998 5224 -727 1557 -1068 C ATOM 2891 O SER B 163 6.187 -0.703 57.729 1.00 41.33 O ANISOU 2891 O SER B 163 5365 5100 5238 -758 1560 -1229 O ATOM 2892 CB SER B 163 9.357 -0.735 56.459 1.00 48.06 C ANISOU 2892 CB SER B 163 6385 5868 6007 -660 1470 -896 C ATOM 2893 OG SER B 163 8.693 0.167 55.589 1.00 48.81 O ANISOU 2893 OG SER B 163 6378 6126 6040 -612 1332 -968 O ATOM 2894 N GLY B 164 7.915 0.063 58.942 1.00 35.57 N ANISOU 2894 N GLY B 164 4834 4198 4483 -666 1502 -911 N ATOM 2895 CA GLY B 164 7.105 1.027 59.660 1.00 36.70 C ANISOU 2895 CA GLY B 164 4956 4380 4611 -623 1431 -925 C ATOM 2896 C GLY B 164 6.480 2.006 58.686 1.00 37.71 C ANISOU 2896 C GLY B 164 4977 4675 4676 -564 1279 -994 C ATOM 2897 O GLY B 164 5.323 2.396 58.836 1.00 38.88 O ANISOU 2897 O GLY B 164 5042 4903 4826 -564 1258 -1109 O ATOM 2898 N SER B 165 7.250 2.396 57.674 1.00 36.91 N ANISOU 2898 N SER B 165 4874 4630 4519 -514 1174 -921 N ATOM 2899 CA SER B 165 6.771 3.309 56.645 1.00 32.85 C ANISOU 2899 CA SER B 165 4260 4278 3942 -458 1023 -974 C ATOM 2900 C SER B 165 5.583 2.721 55.896 1.00 31.22 C ANISOU 2900 C SER B 165 3921 4185 3756 -525 1078 -1191 C ATOM 2901 O SER B 165 4.624 3.425 55.594 1.00 32.13 O ANISOU 2901 O SER B 165 3940 4419 3847 -499 992 -1281 O ATOM 2902 CB SER B 165 7.892 3.638 55.655 1.00 36.17 C ANISOU 2902 CB SER B 165 4704 4736 4305 -403 923 -853 C ATOM 2903 OG SER B 165 9.047 4.109 56.331 1.00 40.38 O ANISOU 2903 OG SER B 165 5360 5157 4824 -348 875 -645 O ATOM 2904 N MET B 166 5.655 1.429 55.594 1.00 34.63 N ANISOU 2904 N MET B 166 4348 4577 4234 -612 1217 -1273 N ATOM 2905 CA MET B 166 4.580 0.746 54.882 1.00 38.40 C ANISOU 2905 CA MET B 166 4706 5149 4737 -686 1276 -1480 C ATOM 2906 C MET B 166 3.341 0.647 55.755 1.00 38.84 C ANISOU 2906 C MET B 166 4711 5201 4847 -732 1344 -1591 C ATOM 2907 O MET B 166 2.219 0.828 55.283 1.00 43.52 O ANISOU 2907 O MET B 166 5185 5914 5437 -749 1312 -1736 O ATOM 2908 CB MET B 166 5.025 -0.646 54.437 1.00 41.84 C ANISOU 2908 CB MET B 166 5163 5523 5213 -767 1411 -1533 C ATOM 2909 CG MET B 166 5.966 -0.627 53.249 1.00 38.62 C ANISOU 2909 CG MET B 166 4765 5166 4745 -728 1345 -1476 C ATOM 2910 SD MET B 166 5.180 0.113 51.803 1.00 52.49 S ANISOU 2910 SD MET B 166 6377 7140 6426 -692 1197 -1596 S ATOM 2911 CE MET B 166 3.797 -0.998 51.561 1.00 84.42 C ANISOU 2911 CE MET B 166 10314 11224 10537 -812 1319 -1848 C ATOM 2912 N SER B 167 3.557 0.345 57.030 1.00 36.77 N ANISOU 2912 N SER B 167 4536 4802 4633 -752 1439 -1521 N ATOM 2913 CA SER B 167 2.486 0.378 58.017 1.00 39.80 C ANISOU 2913 CA SER B 167 4886 5177 5061 -781 1498 -1596 C ATOM 2914 C SER B 167 1.755 1.713 57.927 1.00 39.74 C ANISOU 2914 C SER B 167 4809 5291 5000 -699 1351 -1613 C ATOM 2915 O SER B 167 0.525 1.762 57.903 1.00 43.54 O ANISOU 2915 O SER B 167 5183 5858 5500 -726 1363 -1752 O ATOM 2916 CB SER B 167 3.057 0.183 59.422 1.00 37.96 C ANISOU 2916 CB SER B 167 4777 4784 4864 -783 1583 -1470 C ATOM 2917 OG SER B 167 2.065 0.404 60.409 1.00 41.73 O ANISOU 2917 OG SER B 167 5225 5261 5370 -791 1618 -1521 O ATOM 2918 N SER B 168 2.525 2.794 57.863 1.00 35.88 N ANISOU 2918 N SER B 168 4379 4807 4447 -599 1209 -1468 N ATOM 2919 CA SER B 168 1.958 4.134 57.772 1.00 37.17 C ANISOU 2919 CA SER B 168 4489 5076 4559 -512 1055 -1467 C ATOM 2920 C SER B 168 1.202 4.335 56.460 1.00 35.93 C ANISOU 2920 C SER B 168 4192 5087 4373 -516 977 -1602 C ATOM 2921 O SER B 168 0.172 5.004 56.426 1.00 32.25 O ANISOU 2921 O SER B 168 3636 4723 3897 -490 913 -1686 O ATOM 2922 CB SER B 168 3.052 5.190 57.919 1.00 39.13 C ANISOU 2922 CB SER B 168 4836 5283 4748 -409 915 -1273 C ATOM 2923 OG SER B 168 3.697 5.085 59.177 1.00 41.98 O ANISOU 2923 OG SER B 168 5327 5492 5133 -402 977 -1149 O ATOM 2924 N ALA B 169 1.728 3.769 55.378 1.00 38.50 N ANISOU 2924 N ALA B 169 4500 5445 4683 -547 982 -1619 N ATOM 2925 CA ALA B 169 1.045 3.833 54.092 1.00 39.04 C ANISOU 2925 CA ALA B 169 4438 5671 4723 -561 918 -1752 C ATOM 2926 C ALA B 169 -0.322 3.167 54.186 1.00 36.70 C ANISOU 2926 C ALA B 169 4036 5423 4485 -646 1017 -1944 C ATOM 2927 O ALA B 169 -1.291 3.636 53.594 1.00 37.48 O ANISOU 2927 O ALA B 169 4017 5657 4566 -638 944 -2053 O ATOM 2928 CB ALA B 169 1.885 3.175 53.006 1.00 38.97 C ANISOU 2928 CB ALA B 169 4443 5674 4691 -585 930 -1742 C ATOM 2929 N ARG B 170 -0.390 2.067 54.928 1.00 39.36 N ANISOU 2929 N ARG B 170 4413 5647 4894 -730 1183 -1980 N ATOM 2930 CA ARG B 170 -1.644 1.350 55.129 1.00 44.71 C ANISOU 2930 CA ARG B 170 4997 6348 5642 -818 1274 -2128 C ATOM 2931 C ARG B 170 -2.649 2.226 55.877 1.00 46.09 C ANISOU 2931 C ARG B 170 5117 6577 5816 -775 1237 -2162 C ATOM 2932 O ARG B 170 -3.836 2.236 55.553 1.00 46.54 O ANISOU 2932 O ARG B 170 5052 6733 5896 -807 1218 -2281 O ATOM 2933 CB ARG B 170 -1.393 0.042 55.887 1.00 51.19 C ANISOU 2933 CB ARG B 170 5888 7011 6551 -907 1420 -2089 C ATOM 2934 CG ARG B 170 -2.652 -0.664 56.382 1.00 60.99 C ANISOU 2934 CG ARG B 170 7050 8246 7877 -996 1496 -2188 C ATOM 2935 CD ARG B 170 -2.300 -1.866 57.258 1.00 68.68 C ANISOU 2935 CD ARG B 170 8106 9057 8933 -1076 1630 -2135 C ATOM 2936 NE ARG B 170 -3.397 -2.261 58.144 1.00 75.62 N ANISOU 2936 NE ARG B 170 8937 9914 9882 -1137 1701 -2192 N ATOM 2937 CZ ARG B 170 -4.111 -3.376 58.011 1.00 79.17 C ANISOU 2937 CZ ARG B 170 9325 10347 10409 -1248 1777 -2292 C ATOM 2938 NH1 ARG B 170 -3.850 -4.224 57.025 1.00 79.41 N ANISOU 2938 NH1 ARG B 170 9336 10379 10458 -1309 1794 -2349 N ATOM 2939 NH2 ARG B 170 -5.087 -3.648 58.869 1.00 81.43 N ANISOU 2939 NH2 ARG B 170 9571 10616 10752 -1296 1838 -2336 N ATOM 2940 N LEU B 171 -2.161 2.964 56.872 1.00 44.90 N ANISOU 2940 N LEU B 171 5062 6354 5645 -701 1211 -2036 N ATOM 2941 CA LEU B 171 -2.998 3.877 57.647 1.00 42.96 C ANISOU 2941 CA LEU B 171 4783 6148 5393 -644 1163 -2045 C ATOM 2942 C LEU B 171 -3.461 5.064 56.804 1.00 39.67 C ANISOU 2942 C LEU B 171 4275 5882 4914 -564 988 -2072 C ATOM 2943 O LEU B 171 -4.610 5.496 56.900 1.00 38.47 O ANISOU 2943 O LEU B 171 4023 5822 4770 -553 963 -2169 O ATOM 2944 CB LEU B 171 -2.244 4.380 58.880 1.00 42.84 C ANISOU 2944 CB LEU B 171 4906 6005 5366 -579 1160 -1883 C ATOM 2945 CG LEU B 171 -1.898 3.327 59.935 1.00 45.18 C ANISOU 2945 CG LEU B 171 5292 6151 5725 -650 1333 -1849 C ATOM 2946 CD1 LEU B 171 -0.829 3.836 60.897 1.00 42.52 C ANISOU 2946 CD1 LEU B 171 5108 5686 5362 -582 1305 -1663 C ATOM 2947 CD2 LEU B 171 -3.150 2.898 60.688 1.00 47.06 C ANISOU 2947 CD2 LEU B 171 5459 6398 6025 -705 1428 -1945 C ATOM 2948 N ALA B 172 -2.557 5.592 55.986 1.00 37.04 N ANISOU 2948 N ALA B 172 3976 5575 4521 -507 866 -1981 N ATOM 2949 CA ALA B 172 -2.886 6.699 55.098 1.00 35.25 C ANISOU 2949 CA ALA B 172 3667 5491 4234 -434 693 -1995 C ATOM 2950 C ALA B 172 -4.056 6.309 54.211 1.00 38.06 C ANISOU 2950 C ALA B 172 3868 5984 4609 -497 708 -2180 C ATOM 2951 O ALA B 172 -5.015 7.063 54.062 1.00 39.23 O ANISOU 2951 O ALA B 172 3918 6243 4745 -461 627 -2249 O ATOM 2952 CB ALA B 172 -1.688 7.070 54.251 1.00 32.97 C ANISOU 2952 CB ALA B 172 3432 5209 3885 -384 583 -1874 C ATOM 2953 N GLN B 173 -3.973 5.124 53.620 1.00 40.51 N ANISOU 2953 N GLN B 173 4158 6286 4949 -593 809 -2262 N ATOM 2954 CA GLN B 173 -5.058 4.628 52.790 1.00 45.46 C ANISOU 2954 CA GLN B 173 4643 7031 5598 -666 832 -2442 C ATOM 2955 C GLN B 173 -6.333 4.492 53.617 1.00 48.89 C ANISOU 2955 C GLN B 173 5004 7478 6093 -704 912 -2545 C ATOM 2956 O GLN B 173 -7.383 5.009 53.240 1.00 50.02 O ANISOU 2956 O GLN B 173 5026 7749 6231 -692 845 -2641 O ATOM 2957 CB GLN B 173 -4.678 3.296 52.141 1.00 44.83 C ANISOU 2957 CB GLN B 173 4573 6913 5547 -764 935 -2500 C ATOM 2958 CG GLN B 173 -3.680 3.439 50.995 1.00 46.96 C ANISOU 2958 CG GLN B 173 4871 7225 5746 -729 847 -2445 C ATOM 2959 CD GLN B 173 -3.170 2.106 50.482 1.00 50.47 C ANISOU 2959 CD GLN B 173 5348 7604 6224 -814 951 -2473 C ATOM 2960 OE1 GLN B 173 -2.055 1.694 50.800 1.00 54.84 O ANISOU 2960 OE1 GLN B 173 6019 8042 6777 -810 1010 -2371 O ATOM 2961 NE2 GLN B 173 -3.983 1.428 49.679 1.00 48.63 N ANISOU 2961 NE2 GLN B 173 5011 7440 6025 -891 965 -2598 N ATOM 2962 N LYS B 174 -6.232 3.815 54.756 1.00 49.21 N ANISOU 2962 N LYS B 174 5121 7381 6197 -748 1040 -2497 N ATOM 2963 CA LYS B 174 -7.390 3.602 55.618 1.00 46.47 C ANISOU 2963 CA LYS B 174 4715 7027 5916 -788 1112 -2555 C ATOM 2964 C LYS B 174 -8.103 4.904 55.969 1.00 43.60 C ANISOU 2964 C LYS B 174 4294 6760 5513 -691 1019 -2573 C ATOM 2965 O LYS B 174 -9.329 4.972 55.942 1.00 47.09 O ANISOU 2965 O LYS B 174 4618 7288 5986 -715 1019 -2674 O ATOM 2966 CB LYS B 174 -6.993 2.870 56.900 1.00 45.76 C ANISOU 2966 CB LYS B 174 4735 6768 5882 -827 1243 -2467 C ATOM 2967 CG LYS B 174 -8.153 2.670 57.857 1.00 48.41 C ANISOU 2967 CG LYS B 174 5018 7097 6279 -864 1316 -2516 C ATOM 2968 CD LYS B 174 -7.735 1.914 59.098 1.00 50.20 C ANISOU 2968 CD LYS B 174 5355 7161 6558 -904 1441 -2426 C ATOM 2969 CE LYS B 174 -8.939 1.594 59.962 1.00 54.91 C ANISOU 2969 CE LYS B 174 5888 7758 7215 -951 1517 -2482 C ATOM 2970 NZ LYS B 174 -8.554 0.837 61.185 1.00 58.55 N ANISOU 2970 NZ LYS B 174 6455 8065 7725 -992 1635 -2394 N ATOM 2971 N TYR B 175 -7.332 5.935 56.298 1.00 39.02 N ANISOU 2971 N TYR B 175 3802 6153 4870 -582 926 -2455 N ATOM 2972 CA TYR B 175 -7.907 7.212 56.712 1.00 38.02 C ANISOU 2972 CA TYR B 175 3643 6091 4713 -480 816 -2434 C ATOM 2973 C TYR B 175 -7.917 8.258 55.597 1.00 35.17 C ANISOU 2973 C TYR B 175 3217 5859 4287 -406 629 -2429 C ATOM 2974 O TYR B 175 -7.925 9.460 55.859 1.00 34.66 O ANISOU 2974 O TYR B 175 3167 5819 4181 -301 505 -2361 O ATOM 2975 CB TYR B 175 -7.206 7.746 57.965 1.00 38.07 C ANISOU 2975 CB TYR B 175 3792 5971 4703 -404 816 -2287 C ATOM 2976 CG TYR B 175 -7.443 6.894 59.192 1.00 39.00 C ANISOU 2976 CG TYR B 175 3955 5981 4881 -465 993 -2300 C ATOM 2977 CD1 TYR B 175 -8.627 6.992 59.909 1.00 41.57 C ANISOU 2977 CD1 TYR B 175 4205 6350 5239 -466 1051 -2384 C ATOM 2978 CD2 TYR B 175 -6.484 5.988 59.631 1.00 39.57 C ANISOU 2978 CD2 TYR B 175 4142 5913 4979 -520 1102 -2224 C ATOM 2979 CE1 TYR B 175 -8.850 6.215 61.028 1.00 43.31 C ANISOU 2979 CE1 TYR B 175 4472 6466 5520 -524 1190 -2357 C ATOM 2980 CE2 TYR B 175 -6.699 5.204 60.751 1.00 43.17 C ANISOU 2980 CE2 TYR B 175 4642 6266 5496 -578 1249 -2212 C ATOM 2981 CZ TYR B 175 -7.886 5.324 61.446 1.00 45.53 C ANISOU 2981 CZ TYR B 175 4871 6603 5827 -580 1284 -2269 C ATOM 2982 OH TYR B 175 -8.115 4.555 62.563 1.00 50.15 O ANISOU 2982 OH TYR B 175 5499 7085 6470 -637 1410 -2234 O ATOM 2983 N GLN B 176 -7.926 7.786 54.355 1.00 41.14 N ANISOU 2983 N GLN B 176 3902 6695 5035 -462 608 -2503 N ATOM 2984 CA GLN B 176 -8.096 8.653 53.190 1.00 45.70 C ANISOU 2984 CA GLN B 176 4394 7414 5557 -409 441 -2521 C ATOM 2985 C GLN B 176 -7.136 9.841 53.150 1.00 43.41 C ANISOU 2985 C GLN B 176 4189 7107 5199 -291 284 -2359 C ATOM 2986 O GLN B 176 -7.541 10.961 52.836 1.00 46.14 O ANISOU 2986 O GLN B 176 4475 7549 5509 -211 139 -2352 O ATOM 2987 CB GLN B 176 -9.544 9.149 53.095 1.00 51.58 C ANISOU 2987 CB GLN B 176 4992 8289 6318 -399 403 -2645 C ATOM 2988 CG GLN B 176 -10.568 8.044 52.867 1.00 57.39 C ANISOU 2988 CG GLN B 176 5618 9072 7117 -519 530 -2813 C ATOM 2989 CD GLN B 176 -11.965 8.579 52.595 1.00 61.63 C ANISOU 2989 CD GLN B 176 5998 9754 7666 -509 475 -2930 C ATOM 2990 OE1 GLN B 176 -12.155 9.775 52.372 1.00 64.38 O ANISOU 2990 OE1 GLN B 176 6311 10182 7970 -413 329 -2896 O ATOM 2991 NE2 GLN B 176 -12.952 7.690 52.615 1.00 60.60 N ANISOU 2991 NE2 GLN B 176 5771 9656 7599 -609 589 -3067 N ATOM 2992 N LYS B 177 -5.869 9.591 53.470 1.00 38.20 N ANISOU 2992 N LYS B 177 3667 6322 4525 -282 309 -2226 N ATOM 2993 CA LYS B 177 -4.824 10.601 53.328 1.00 34.32 C ANISOU 2993 CA LYS B 177 3260 5809 3973 -182 161 -2062 C ATOM 2994 C LYS B 177 -4.002 10.304 52.077 1.00 36.62 C ANISOU 2994 C LYS B 177 3548 6143 4223 -202 112 -2031 C ATOM 2995 O LYS B 177 -3.374 9.250 51.978 1.00 38.23 O ANISOU 2995 O LYS B 177 3807 6274 4445 -270 224 -2025 O ATOM 2996 CB LYS B 177 -3.908 10.624 54.559 1.00 28.07 C ANISOU 2996 CB LYS B 177 2627 4848 3189 -149 209 -1916 C ATOM 2997 CG LYS B 177 -4.630 10.867 55.894 1.00 29.22 C ANISOU 2997 CG LYS B 177 2792 4940 3370 -126 268 -1937 C ATOM 2998 CD LYS B 177 -5.551 12.073 55.816 1.00 30.44 C ANISOU 2998 CD LYS B 177 2858 5207 3502 -43 135 -1979 C ATOM 2999 CE LYS B 177 -6.324 12.279 57.116 1.00 35.16 C ANISOU 2999 CE LYS B 177 3469 5761 4131 -18 202 -2011 C ATOM 3000 NZ LYS B 177 -5.528 12.996 58.157 1.00 38.41 N ANISOU 3000 NZ LYS B 177 4026 6050 4517 69 152 -1857 N ATOM 3001 N PRO B 178 -3.999 11.235 51.114 1.00 37.57 N ANISOU 3001 N PRO B 178 3605 6383 4286 -139 -55 -2009 N ATOM 3002 CA PRO B 178 -3.293 10.991 49.853 1.00 40.95 C ANISOU 3002 CA PRO B 178 4018 6873 4668 -154 -105 -1986 C ATOM 3003 C PRO B 178 -1.803 10.718 50.061 1.00 36.22 C ANISOU 3003 C PRO B 178 3561 6150 4051 -139 -83 -1823 C ATOM 3004 O PRO B 178 -1.135 11.441 50.810 1.00 33.49 O ANISOU 3004 O PRO B 178 3313 5717 3693 -67 -144 -1674 O ATOM 3005 CB PRO B 178 -3.505 12.293 49.071 1.00 41.22 C ANISOU 3005 CB PRO B 178 3975 7041 4644 -68 -305 -1954 C ATOM 3006 CG PRO B 178 -3.827 13.313 50.101 1.00 40.45 C ANISOU 3006 CG PRO B 178 3909 6902 4557 12 -372 -1895 C ATOM 3007 CD PRO B 178 -4.584 12.584 51.169 1.00 40.30 C ANISOU 3007 CD PRO B 178 3896 6811 4606 -46 -208 -1993 C ATOM 3008 N LEU B 179 -1.309 9.667 49.410 1.00 34.05 N ANISOU 3008 N LEU B 179 3295 5865 3776 -208 6 -1855 N ATOM 3009 CA LEU B 179 0.096 9.288 49.457 1.00 32.19 C ANISOU 3009 CA LEU B 179 3182 5525 3525 -201 37 -1711 C ATOM 3010 C LEU B 179 0.864 9.875 48.280 1.00 34.47 C ANISOU 3010 C LEU B 179 3454 5905 3737 -145 -105 -1620 C ATOM 3011 O LEU B 179 0.320 10.043 47.189 1.00 37.31 O ANISOU 3011 O LEU B 179 3703 6413 4063 -150 -175 -1712 O ATOM 3012 CB LEU B 179 0.240 7.764 49.419 1.00 35.00 C ANISOU 3012 CB LEU B 179 3562 5812 3925 -305 220 -1795 C ATOM 3013 CG LEU B 179 0.080 6.953 50.705 1.00 41.71 C ANISOU 3013 CG LEU B 179 4481 6515 4851 -364 386 -1816 C ATOM 3014 CD1 LEU B 179 -0.176 5.490 50.383 1.00 41.77 C ANISOU 3014 CD1 LEU B 179 4462 6502 4905 -477 546 -1952 C ATOM 3015 CD2 LEU B 179 1.314 7.099 51.583 1.00 42.61 C ANISOU 3015 CD2 LEU B 179 4747 6479 4966 -321 397 -1626 C ATOM 3016 N PHE B 180 2.138 10.167 48.508 1.00 29.15 N ANISOU 3016 N PHE B 180 2892 5146 3038 -92 -147 -1434 N ATOM 3017 CA PHE B 180 3.048 10.587 47.448 1.00 28.52 C ANISOU 3017 CA PHE B 180 2810 5137 2888 -43 -263 -1326 C ATOM 3018 C PHE B 180 4.433 10.012 47.708 1.00 29.61 C ANISOU 3018 C PHE B 180 3075 5149 3027 -46 -193 -1180 C ATOM 3019 O PHE B 180 4.851 9.887 48.858 1.00 24.01 O ANISOU 3019 O PHE B 180 2471 4293 2358 -44 -129 -1096 O ATOM 3020 CB PHE B 180 3.135 12.109 47.381 1.00 29.87 C ANISOU 3020 CB PHE B 180 2967 5368 3016 59 -464 -1208 C ATOM 3021 CG PHE B 180 1.901 12.768 46.845 1.00 32.43 C ANISOU 3021 CG PHE B 180 3155 5841 3326 73 -558 -1335 C ATOM 3022 CD1 PHE B 180 1.726 12.935 45.482 1.00 29.75 C ANISOU 3022 CD1 PHE B 180 2711 5660 2933 76 -643 -1386 C ATOM 3023 CD2 PHE B 180 0.921 13.234 47.705 1.00 31.90 C ANISOU 3023 CD2 PHE B 180 3063 5759 3300 86 -563 -1401 C ATOM 3024 CE1 PHE B 180 0.587 13.552 44.985 1.00 35.85 C ANISOU 3024 CE1 PHE B 180 3402 6482 3739 96 -676 -1434 C ATOM 3025 CE2 PHE B 180 -0.213 13.851 47.218 1.00 36.48 C ANISOU 3025 CE2 PHE B 180 3516 6476 3870 101 -651 -1514 C ATOM 3026 CZ PHE B 180 -0.383 14.011 45.856 1.00 37.45 C ANISOU 3026 CZ PHE B 180 3580 6666 3984 109 -678 -1495 C ATOM 3027 N VAL B 181 5.152 9.663 46.646 1.00 29.02 N ANISOU 3027 N VAL B 181 2990 5132 2905 -47 -204 -1148 N ATOM 3028 CA VAL B 181 6.486 9.102 46.804 1.00 30.54 C ANISOU 3028 CA VAL B 181 3294 5213 3095 -46 -138 -1008 C ATOM 3029 C VAL B 181 7.474 9.726 45.828 1.00 30.06 C ANISOU 3029 C VAL B 181 3232 5232 2958 23 -271 -860 C ATOM 3030 O VAL B 181 7.076 10.429 44.898 1.00 29.96 O ANISOU 3030 O VAL B 181 3122 5369 2892 59 -399 -890 O ATOM 3031 CB VAL B 181 6.478 7.575 46.600 1.00 30.22 C ANISOU 3031 CB VAL B 181 3262 5129 3090 -140 48 -1130 C ATOM 3032 CG1 VAL B 181 5.435 6.927 47.508 1.00 31.20 C ANISOU 3032 CG1 VAL B 181 3376 5186 3293 -215 178 -1280 C ATOM 3033 CG2 VAL B 181 6.215 7.235 45.140 1.00 34.16 C ANISOU 3033 CG2 VAL B 181 3660 5782 3536 -160 28 -1245 C ATOM 3034 N LEU B 182 8.762 9.484 46.061 1.00 27.98 N ANISOU 3034 N LEU B 182 3074 4868 2690 43 -242 -695 N ATOM 3035 CA LEU B 182 9.800 9.829 45.091 1.00 31.45 C ANISOU 3035 CA LEU B 182 3513 5377 3059 99 -336 -555 C ATOM 3036 C LEU B 182 9.950 8.680 44.111 1.00 29.63 C ANISOU 3036 C LEU B 182 3249 5202 2807 47 -224 -660 C ATOM 3037 O LEU B 182 9.797 7.521 44.491 1.00 33.48 O ANISOU 3037 O LEU B 182 3771 5603 3347 -26 -57 -762 O ATOM 3038 CB LEU B 182 11.146 10.051 45.780 1.00 32.09 C ANISOU 3038 CB LEU B 182 3721 5324 3147 143 -351 -324 C ATOM 3039 CG LEU B 182 11.434 11.363 46.505 1.00 33.46 C ANISOU 3039 CG LEU B 182 3942 5451 3320 218 -505 -156 C ATOM 3040 CD1 LEU B 182 12.827 11.320 47.117 1.00 31.32 C ANISOU 3040 CD1 LEU B 182 3799 5041 3060 246 -493 62 C ATOM 3041 CD2 LEU B 182 11.299 12.538 45.554 1.00 33.22 C ANISOU 3041 CD2 LEU B 182 3821 5578 3222 287 -701 -109 C ATOM 3042 N PRO B 183 10.239 8.993 42.839 1.00 33.81 N ANISOU 3042 N PRO B 183 3266 6501 3079 58 212 -1721 N ATOM 3043 CA PRO B 183 10.610 7.947 41.884 1.00 31.52 C ANISOU 3043 CA PRO B 183 2998 6205 2773 110 176 -1734 C ATOM 3044 C PRO B 183 11.861 7.215 42.362 1.00 31.16 C ANISOU 3044 C PRO B 183 3013 6159 2668 171 154 -1713 C ATOM 3045 O PRO B 183 12.821 7.854 42.799 1.00 31.58 O ANISOU 3045 O PRO B 183 3050 6237 2713 189 142 -1684 O ATOM 3046 CB PRO B 183 10.915 8.735 40.605 1.00 34.06 C ANISOU 3046 CB PRO B 183 3237 6560 3145 123 139 -1728 C ATOM 3047 CG PRO B 183 10.131 9.999 40.743 1.00 31.43 C ANISOU 3047 CG PRO B 183 2838 6239 2863 58 163 -1729 C ATOM 3048 CD PRO B 183 10.165 10.321 42.208 1.00 33.48 C ANISOU 3048 CD PRO B 183 3133 6491 3097 31 199 -1714 C ATOM 3049 N GLN B 184 11.845 5.888 42.286 1.00 32.04 N ANISOU 3049 N GLN B 184 3193 6244 2739 202 147 -1729 N ATOM 3050 CA GLN B 184 12.962 5.086 42.771 1.00 32.21 C ANISOU 3050 CA GLN B 184 3277 6261 2701 257 127 -1712 C ATOM 3051 C GLN B 184 13.293 3.964 41.796 1.00 31.13 C ANISOU 3051 C GLN B 184 3167 6111 2549 309 89 -1728 C ATOM 3052 O GLN B 184 12.408 3.412 41.144 1.00 31.45 O ANISOU 3052 O GLN B 184 3213 6130 2605 297 89 -1762 O ATOM 3053 CB GLN B 184 12.647 4.497 44.150 1.00 33.25 C ANISOU 3053 CB GLN B 184 3487 6366 2779 241 166 -1713 C ATOM 3054 CG GLN B 184 12.409 5.529 45.247 1.00 33.64 C ANISOU 3054 CG GLN B 184 3524 6425 2833 197 205 -1696 C ATOM 3055 CD GLN B 184 13.689 6.152 45.769 1.00 34.15 C ANISOU 3055 CD GLN B 184 3578 6517 2880 228 183 -1663 C ATOM 3056 OE1 GLN B 184 14.771 5.928 45.230 1.00 33.78 O ANISOU 3056 OE1 GLN B 184 3522 6488 2826 280 140 -1652 O ATOM 3057 NE2 GLN B 184 13.570 6.931 46.844 1.00 32.41 N ANISOU 3057 NE2 GLN B 184 3360 6301 2653 197 213 -1650 N ATOM 3058 N ARG B 185 14.574 3.627 41.705 1.00 35.78 N ANISOU 3058 N ARG B 185 3773 6713 3108 367 55 -1707 N ATOM 3059 CA ARG B 185 15.019 2.555 40.827 1.00 36.77 C ANISOU 3059 CA ARG B 185 3930 6827 3216 422 18 -1719 C ATOM 3060 C ARG B 185 14.488 1.197 41.270 1.00 39.58 C ANISOU 3060 C ARG B 185 4370 7141 3526 425 27 -1746 C ATOM 3061 O ARG B 185 14.066 1.020 42.413 1.00 41.81 O ANISOU 3061 O ARG B 185 4697 7409 3779 396 63 -1747 O ATOM 3062 CB ARG B 185 16.546 2.516 40.756 1.00 41.91 C ANISOU 3062 CB ARG B 185 4578 7501 3843 483 -15 -1690 C ATOM 3063 CG ARG B 185 17.162 3.681 40.005 1.00 41.26 C ANISOU 3063 CG ARG B 185 4407 7461 3807 494 -32 -1670 C ATOM 3064 CD ARG B 185 18.678 3.581 39.979 1.00 41.98 C ANISOU 3064 CD ARG B 185 4497 7579 3876 555 -62 -1646 C ATOM 3065 NE ARG B 185 19.276 4.687 39.238 1.00 43.64 N ANISOU 3065 NE ARG B 185 4618 7832 4129 568 -77 -1630 N ATOM 3066 CZ ARG B 185 20.577 4.954 39.217 1.00 49.35 C ANISOU 3066 CZ ARG B 185 5315 8589 4846 614 -99 -1610 C ATOM 3067 NH1 ARG B 185 21.421 4.197 39.905 1.00 49.80 N ANISOU 3067 NH1 ARG B 185 5427 8641 4855 651 -109 -1603 N ATOM 3068 NH2 ARG B 185 21.033 5.982 38.513 1.00 49.88 N ANISOU 3068 NH2 ARG B 185 5299 8698 4955 624 -111 -1599 N ATOM 3069 N LEU B 186 14.515 0.242 40.349 1.00 39.29 N ANISOU 3069 N LEU B 186 4357 7087 3485 463 -6 -1769 N ATOM 3070 CA LEU B 186 14.129 -1.129 40.641 1.00 41.79 C ANISOU 3070 CA LEU B 186 4753 7366 3761 474 -6 -1799 C ATOM 3071 C LEU B 186 15.042 -1.684 41.731 1.00 45.68 C ANISOU 3071 C LEU B 186 5308 7858 4190 505 -3 -1774 C ATOM 3072 O LEU B 186 16.263 -1.627 41.604 1.00 44.52 O ANISOU 3072 O LEU B 186 5155 7731 4028 551 -31 -1746 O ATOM 3073 CB LEU B 186 14.252 -1.972 39.370 1.00 44.18 C ANISOU 3073 CB LEU B 186 5064 7652 4069 520 -52 -1824 C ATOM 3074 CG LEU B 186 13.318 -3.168 39.188 1.00 44.36 C ANISOU 3074 CG LEU B 186 5141 7632 4084 516 -58 -1876 C ATOM 3075 CD1 LEU B 186 11.869 -2.729 39.299 1.00 44.44 C ANISOU 3075 CD1 LEU B 186 5122 7629 4134 448 -23 -1910 C ATOM 3076 CD2 LEU B 186 13.573 -3.836 37.846 1.00 43.80 C ANISOU 3076 CD2 LEU B 186 5072 7547 4023 567 -111 -1897 C ATOM 3077 N ASN B 187 14.451 -2.193 42.810 1.00 47.53 N ANISOU 3077 N ASN B 187 5601 8071 4388 479 33 -1786 N ATOM 3078 CA ASN B 187 15.214 -2.844 43.878 1.00 50.54 C ANISOU 3078 CA ASN B 187 6051 8449 4702 509 37 -1766 C ATOM 3079 C ASN B 187 15.956 -1.892 44.819 1.00 52.66 C ANISOU 3079 C ASN B 187 6304 8746 4957 502 51 -1723 C ATOM 3080 O ASN B 187 17.004 -2.247 45.354 1.00 57.04 O ANISOU 3080 O ASN B 187 6895 9309 5467 543 34 -1701 O ATOM 3081 CB ASN B 187 16.219 -3.849 43.296 1.00 52.67 C ANISOU 3081 CB ASN B 187 6354 8715 4944 577 -13 -1765 C ATOM 3082 CG ASN B 187 15.551 -5.008 42.580 1.00 54.01 C ANISOU 3082 CG ASN B 187 6558 8848 5113 591 -30 -1811 C ATOM 3083 OD1 ASN B 187 14.650 -5.649 43.117 1.00 54.37 O ANISOU 3083 OD1 ASN B 187 6649 8868 5141 567 -3 -1842 O ATOM 3084 ND2 ASN B 187 15.995 -5.284 41.357 1.00 58.94 N ANISOU 3084 ND2 ASN B 187 7162 9474 5761 632 -76 -1820 N ATOM 3085 N GLU B 188 15.426 -0.690 45.022 1.00 49.74 N ANISOU 3085 N GLU B 188 5881 8391 4626 453 80 -1715 N ATOM 3086 CA GLU B 188 16.049 0.267 45.935 1.00 51.73 C ANISOU 3086 CA GLU B 188 6118 8667 4869 444 92 -1682 C ATOM 3087 C GLU B 188 15.077 0.734 47.007 1.00 52.51 C ANISOU 3087 C GLU B 188 6235 8757 4961 388 149 -1683 C ATOM 3088 O GLU B 188 15.476 1.171 48.090 1.00 54.53 O ANISOU 3088 O GLU B 188 6512 9021 5186 385 165 -1660 O ATOM 3089 CB GLU B 188 16.578 1.480 45.174 1.00 52.84 C ANISOU 3089 CB GLU B 188 6167 8843 5068 445 68 -1666 C ATOM 3090 CG GLU B 188 17.942 1.280 44.549 1.00 52.06 C ANISOU 3090 CG GLU B 188 6051 8765 4963 508 20 -1650 C ATOM 3091 CD GLU B 188 18.713 2.581 44.431 1.00 52.48 C ANISOU 3091 CD GLU B 188 6026 8860 5053 510 7 -1627 C ATOM 3092 OE1 GLU B 188 18.135 3.644 44.737 1.00 51.21 O ANISOU 3092 OE1 GLU B 188 5823 8710 4926 462 33 -1625 O ATOM 3093 OE2 GLU B 188 19.899 2.542 44.042 1.00 53.13 O ANISOU 3093 OE2 GLU B 188 6088 8966 5132 561 -28 -1614 O ATOM 3094 N SER B 189 13.795 0.638 46.687 1.00 48.62 N ANISOU 3094 N SER B 189 5732 8245 4498 346 179 -1712 N ATOM 3095 CA SER B 189 12.743 1.096 47.570 1.00 40.66 C ANISOU 3095 CA SER B 189 4732 7227 3492 289 240 -1717 C ATOM 3096 C SER B 189 11.497 0.313 47.196 1.00 41.15 C ANISOU 3096 C SER B 189 4809 7260 3566 263 267 -1761 C ATOM 3097 O SER B 189 10.564 0.858 46.613 1.00 40.79 O ANISOU 3097 O SER B 189 4707 7214 3579 218 282 -1783 O ATOM 3098 CB SER B 189 12.517 2.594 47.364 1.00 37.62 C ANISOU 3098 CB SER B 189 4263 6865 3168 249 247 -1705 C ATOM 3099 OG SER B 189 11.703 3.151 48.380 1.00 41.05 O ANISOU 3099 OG SER B 189 4707 7291 3598 199 306 -1702 O ATOM 3100 N ASP B 190 11.501 -0.978 47.517 1.00 43.03 N ANISOU 3100 N ASP B 190 5122 7476 3752 290 270 -1777 N ATOM 3101 CA ASP B 190 10.422 -1.874 47.116 1.00 45.63 C ANISOU 3101 CA ASP B 190 5468 7777 4093 273 289 -1827 C ATOM 3102 C ASP B 190 9.084 -1.435 47.700 1.00 45.47 C ANISOU 3102 C ASP B 190 5434 7746 4098 205 363 -1845 C ATOM 3103 O ASP B 190 8.029 -1.666 47.104 1.00 46.37 O ANISOU 3103 O ASP B 190 5519 7841 4257 170 379 -1892 O ATOM 3104 CB ASP B 190 10.729 -3.315 47.534 1.00 48.67 C ANISOU 3104 CB ASP B 190 5940 8142 4412 317 284 -1839 C ATOM 3105 CG ASP B 190 11.977 -3.869 46.862 1.00 50.04 C ANISOU 3105 CG ASP B 190 6126 8322 4566 384 212 -1826 C ATOM 3106 OD1 ASP B 190 12.300 -3.433 45.737 1.00 45.46 O ANISOU 3106 OD1 ASP B 190 5486 7753 4032 395 167 -1827 O ATOM 3107 OD2 ASP B 190 12.634 -4.748 47.462 1.00 52.26 O ANISOU 3107 OD2 ASP B 190 6476 8598 4783 426 204 -1815 O ATOM 3108 N GLY B 191 9.138 -0.800 48.866 1.00 41.29 N ANISOU 3108 N GLY B 191 4923 7225 3541 186 409 -1811 N ATOM 3109 CA GLY B 191 7.945 -0.326 49.535 1.00 43.51 C ANISOU 3109 CA GLY B 191 5194 7495 3843 124 488 -1820 C ATOM 3110 C GLY B 191 7.213 0.736 48.744 1.00 42.49 C ANISOU 3110 C GLY B 191 4972 7374 3799 71 490 -1835 C ATOM 3111 O GLY B 191 6.015 0.611 48.500 1.00 45.73 O ANISOU 3111 O GLY B 191 5357 7765 4253 23 533 -1875 O ATOM 3112 N THR B 192 7.927 1.783 48.340 1.00 39.07 N ANISOU 3112 N THR B 192 4484 6968 3393 80 446 -1805 N ATOM 3113 CA THR B 192 7.301 2.887 47.618 1.00 38.57 C ANISOU 3113 CA THR B 192 4331 6917 3408 32 446 -1814 C ATOM 3114 C THR B 192 6.946 2.475 46.199 1.00 35.13 C ANISOU 3114 C THR B 192 3852 6476 3019 36 405 -1855 C ATOM 3115 O THR B 192 5.918 2.882 45.665 1.00 32.72 O ANISOU 3115 O THR B 192 3491 6165 2775 -14 425 -1886 O ATOM 3116 CB THR B 192 8.191 4.148 47.595 1.00 35.08 C ANISOU 3116 CB THR B 192 3839 6506 2982 42 412 -1773 C ATOM 3117 OG1 THR B 192 9.480 3.818 47.071 1.00 36.21 O ANISOU 3117 OG1 THR B 192 3990 6666 3102 105 346 -1756 O ATOM 3118 CG2 THR B 192 8.348 4.714 49.005 1.00 31.85 C ANISOU 3118 CG2 THR B 192 3466 6098 2537 30 455 -1740 C ATOM 3119 N ASN B 193 7.796 1.655 45.592 1.00 35.70 N ANISOU 3119 N ASN B 193 3952 6548 3063 95 347 -1857 N ATOM 3120 CA ASN B 193 7.528 1.176 44.241 1.00 36.74 C ANISOU 3120 CA ASN B 193 4054 6672 3233 108 302 -1896 C ATOM 3121 C ASN B 193 6.262 0.326 44.160 1.00 38.48 C ANISOU 3121 C ASN B 193 4293 6857 3471 73 336 -1958 C ATOM 3122 O ASN B 193 5.512 0.408 43.189 1.00 42.23 O ANISOU 3122 O ASN B 193 4717 7323 4004 49 321 -1999 O ATOM 3123 CB ASN B 193 8.736 0.425 43.680 1.00 38.52 C ANISOU 3123 CB ASN B 193 4313 6902 3422 183 237 -1883 C ATOM 3124 CG ASN B 193 9.755 1.355 43.050 1.00 40.96 C ANISOU 3124 CG ASN B 193 4566 7245 3751 211 194 -1844 C ATOM 3125 OD1 ASN B 193 9.421 2.465 42.633 1.00 41.68 O ANISOU 3125 OD1 ASN B 193 4584 7356 3895 177 198 -1838 O ATOM 3126 ND2 ASN B 193 11.004 0.906 42.973 1.00 41.48 N ANISOU 3126 ND2 ASN B 193 4664 7320 3777 272 153 -1819 N ATOM 3127 N GLU B 194 6.028 -0.491 45.179 1.00 42.07 N ANISOU 3127 N GLU B 194 4817 7291 3878 71 382 -1967 N ATOM 3128 CA GLU B 194 4.791 -1.259 45.268 1.00 45.93 C ANISOU 3128 CA GLU B 194 5319 7742 4389 32 429 -2029 C ATOM 3129 C GLU B 194 3.577 -0.341 45.358 1.00 45.26 C ANISOU 3129 C GLU B 194 5171 7653 4372 -48 491 -2047 C ATOM 3130 O GLU B 194 2.540 -0.611 44.755 1.00 45.02 O ANISOU 3130 O GLU B 194 5108 7596 4401 -87 504 -2109 O ATOM 3131 CB GLU B 194 4.818 -2.207 46.467 1.00 51.27 C ANISOU 3131 CB GLU B 194 6081 8401 4998 45 481 -2028 C ATOM 3132 CG GLU B 194 3.452 -2.780 46.817 1.00 56.24 C ANISOU 3132 CG GLU B 194 6717 8991 5659 -11 560 -2088 C ATOM 3133 CD GLU B 194 3.543 -4.101 47.551 1.00 61.37 C ANISOU 3133 CD GLU B 194 7455 9570 6294 17 572 -2047 C ATOM 3134 OE1 GLU B 194 4.011 -5.085 46.937 1.00 65.46 O ANISOU 3134 OE1 GLU B 194 8004 10063 6806 66 505 -2061 O ATOM 3135 OE2 GLU B 194 3.151 -4.155 48.737 1.00 61.71 O ANISOU 3135 OE2 GLU B 194 7536 9578 6331 -9 650 -1998 O ATOM 3136 N LEU B 195 3.705 0.739 46.119 1.00 44.80 N ANISOU 3136 N LEU B 195 5094 7617 4309 -72 529 -1996 N ATOM 3137 CA LEU B 195 2.637 1.725 46.208 1.00 43.27 C ANISOU 3137 CA LEU B 195 4836 7421 4182 -145 586 -2005 C ATOM 3138 C LEU B 195 2.333 2.274 44.819 1.00 42.85 C ANISOU 3138 C LEU B 195 4701 7379 4202 -160 533 -2033 C ATOM 3139 O LEU B 195 1.175 2.417 44.429 1.00 42.74 O ANISOU 3139 O LEU B 195 4640 7345 4256 -217 566 -2080 O ATOM 3140 CB LEU B 195 3.020 2.859 47.162 1.00 44.93 C ANISOU 3140 CB LEU B 195 5042 7653 4374 -157 615 -1942 C ATOM 3141 CG LEU B 195 3.122 2.483 48.639 1.00 44.35 C ANISOU 3141 CG LEU B 195 5049 7568 4234 -151 679 -1913 C ATOM 3142 CD1 LEU B 195 3.647 3.651 49.457 1.00 42.76 C ANISOU 3142 CD1 LEU B 195 4844 7388 4016 -153 687 -1855 C ATOM 3143 CD2 LEU B 195 1.770 2.018 49.161 1.00 46.37 C ANISOU 3143 CD2 LEU B 195 5315 7785 4517 -209 778 -1948 C ATOM 3144 N LEU B 196 3.384 2.572 44.067 1.00 40.51 N ANISOU 3144 N LEU B 196 4387 7112 3893 -109 455 -2004 N ATOM 3145 CA LEU B 196 3.215 3.031 42.700 1.00 38.91 C ANISOU 3145 CA LEU B 196 4113 6922 3750 -111 402 -2024 C ATOM 3146 C LEU B 196 2.588 1.941 41.842 1.00 38.88 C ANISOU 3146 C LEU B 196 4120 6884 3768 -105 376 -2094 C ATOM 3147 O LEU B 196 1.660 2.203 41.086 1.00 41.93 O ANISOU 3147 O LEU B 196 4450 7259 4221 -145 374 -2138 O ATOM 3148 CB LEU B 196 4.552 3.467 42.099 1.00 35.86 C ANISOU 3148 CB LEU B 196 3712 6572 3343 -50 333 -1977 C ATOM 3149 CG LEU B 196 5.112 4.810 42.566 1.00 37.42 C ANISOU 3149 CG LEU B 196 3869 6803 3546 -62 342 -1921 C ATOM 3150 CD1 LEU B 196 6.447 5.088 41.889 1.00 37.84 C ANISOU 3150 CD1 LEU B 196 3905 6886 3585 1 277 -1884 C ATOM 3151 CD2 LEU B 196 4.118 5.928 42.286 1.00 36.36 C ANISOU 3151 CD2 LEU B 196 3654 6677 3483 -129 370 -1934 C ATOM 3152 N GLU B 197 3.092 0.717 41.960 1.00 39.29 N ANISOU 3152 N GLU B 197 4244 6916 3768 -55 351 -2106 N ATOM 3153 CA GLU B 197 2.626 -0.370 41.104 1.00 39.43 C ANISOU 3153 CA GLU B 197 4278 6894 3808 -41 310 -2174 C ATOM 3154 C GLU B 197 1.134 -0.639 41.269 1.00 43.00 C ANISOU 3154 C GLU B 197 4713 7303 4322 -112 366 -2247 C ATOM 3155 O GLU B 197 0.459 -1.026 40.315 1.00 42.93 O ANISOU 3155 O GLU B 197 4681 7255 4377 -124 325 -2303 O ATOM 3156 CB GLU B 197 3.423 -1.653 41.353 1.00 40.22 C ANISOU 3156 CB GLU B 197 4463 6977 3840 24 278 -2174 C ATOM 3157 CG GLU B 197 3.061 -2.776 40.394 1.00 45.75 C ANISOU 3157 CG GLU B 197 5183 7633 4566 47 220 -2243 C ATOM 3158 CD GLU B 197 3.949 -3.992 40.551 1.00 53.37 C ANISOU 3158 CD GLU B 197 6228 8584 5465 116 182 -2239 C ATOM 3159 OE1 GLU B 197 4.528 -4.161 41.644 1.00 54.98 O ANISOU 3159 OE1 GLU B 197 6482 8803 5606 131 221 -2199 O ATOM 3160 OE2 GLU B 197 4.071 -4.775 39.579 1.00 55.82 O ANISOU 3160 OE2 GLU B 197 6554 8866 5788 157 112 -2275 O ATOM 3161 N LYS B 198 0.619 -0.432 42.476 1.00 41.37 N ANISOU 3161 N LYS B 198 4888 7382 3450 464 -561 -1633 N ATOM 3162 CA LYS B 198 -0.793 -0.698 42.744 1.00 42.99 C ANISOU 3162 CA LYS B 198 5036 7582 3716 493 -595 -1696 C ATOM 3163 C LYS B 198 -1.660 0.554 42.634 1.00 46.26 C ANISOU 3163 C LYS B 198 5482 8018 4076 544 -667 -1658 C ATOM 3164 O LYS B 198 -2.864 0.508 42.886 1.00 47.52 O ANISOU 3164 O LYS B 198 5602 8173 4283 573 -701 -1703 O ATOM 3165 CB LYS B 198 -0.972 -1.373 44.106 1.00 43.08 C ANISOU 3165 CB LYS B 198 5007 7493 3869 464 -557 -1728 C ATOM 3166 CG LYS B 198 -0.227 -2.696 44.223 1.00 42.50 C ANISOU 3166 CG LYS B 198 4891 7396 3859 415 -489 -1766 C ATOM 3167 CD LYS B 198 -0.427 -3.340 45.581 1.00 46.19 C ANISOU 3167 CD LYS B 198 5318 7766 4467 388 -454 -1788 C ATOM 3168 CE LYS B 198 0.403 -4.606 45.719 1.00 46.76 C ANISOU 3168 CE LYS B 198 5351 7812 4602 338 -387 -1814 C ATOM 3169 NZ LYS B 198 0.252 -5.227 47.065 1.00 49.90 N ANISOU 3169 NZ LYS B 198 5710 8114 5135 310 -352 -1824 N ATOM 3170 N GLY B 199 -1.047 1.664 42.237 1.00 46.93 N ANISOU 3170 N GLY B 199 5638 8129 4064 555 -691 -1574 N ATOM 3171 CA GLY B 199 -1.764 2.917 42.079 1.00 48.71 C ANISOU 3171 CA GLY B 199 5898 8377 4232 603 -762 -1524 C ATOM 3172 C GLY B 199 -2.290 3.461 43.393 1.00 49.28 C ANISOU 3172 C GLY B 199 5976 8359 4391 609 -779 -1510 C ATOM 3173 O GLY B 199 -3.272 4.201 43.424 1.00 51.67 O ANISOU 3173 O GLY B 199 6280 8670 4683 651 -837 -1501 O ATOM 3174 N GLN B 200 -1.623 3.093 44.481 1.00 46.84 N ANISOU 3174 N GLN B 200 5668 7963 4165 567 -727 -1507 N ATOM 3175 CA GLN B 200 -2.025 3.509 45.818 1.00 43.27 C ANISOU 3175 CA GLN B 200 5219 7418 3802 567 -735 -1496 C ATOM 3176 C GLN B 200 -1.280 4.766 46.255 1.00 42.07 C ANISOU 3176 C GLN B 200 5145 7230 3610 567 -751 -1397 C ATOM 3177 O GLN B 200 -1.589 5.360 47.287 1.00 40.63 O ANISOU 3177 O GLN B 200 4977 6977 3483 574 -768 -1375 O ATOM 3178 CB GLN B 200 -1.764 2.380 46.809 1.00 41.07 C ANISOU 3178 CB GLN B 200 4897 7063 3645 522 -670 -1546 C ATOM 3179 CG GLN B 200 -2.494 1.098 46.475 1.00 42.34 C ANISOU 3179 CG GLN B 200 4977 7251 3858 521 -651 -1639 C ATOM 3180 CD GLN B 200 -2.081 -0.046 47.372 1.00 44.17 C ANISOU 3180 CD GLN B 200 5167 7411 4206 474 -584 -1674 C ATOM 3181 OE1 GLN B 200 -1.036 0.004 48.017 1.00 42.76 O ANISOU 3181 OE1 GLN B 200 5023 7174 4051 435 -544 -1631 O ATOM 3182 NE2 GLN B 200 -2.903 -1.088 47.419 1.00 48.76 N ANISOU 3182 NE2 GLN B 200 5672 7995 4860 476 -572 -1749 N ATOM 3183 N ALA B 201 -0.288 5.158 45.465 1.00 43.28 N ANISOU 3183 N ALA B 201 5346 7432 3666 560 -745 -1336 N ATOM 3184 CA ALA B 201 0.448 6.388 45.713 1.00 37.28 C ANISOU 3184 CA ALA B 201 4659 6649 2855 563 -764 -1233 C ATOM 3185 C ALA B 201 0.750 7.084 44.393 1.00 36.59 C ANISOU 3185 C ALA B 201 4613 6655 2636 589 -796 -1168 C ATOM 3186 O ALA B 201 0.739 6.463 43.328 1.00 36.26 O ANISOU 3186 O ALA B 201 4547 6689 2542 592 -787 -1205 O ATOM 3187 CB ALA B 201 1.737 6.099 46.479 1.00 34.15 C ANISOU 3187 CB ALA B 201 4289 6186 2499 511 -701 -1206 C ATOM 3188 N GLN B 202 1.006 8.383 44.466 1.00 36.54 N ANISOU 3188 N GLN B 202 4666 6640 2579 610 -835 -1069 N ATOM 3189 CA GLN B 202 1.360 9.162 43.291 1.00 40.98 C ANISOU 3189 CA GLN B 202 5271 7280 3020 635 -865 -989 C ATOM 3190 C GLN B 202 2.821 9.589 43.385 1.00 39.35 C ANISOU 3190 C GLN B 202 5124 7052 2776 606 -827 -899 C ATOM 3191 O GLN B 202 3.312 9.904 44.469 1.00 38.91 O ANISOU 3191 O GLN B 202 5092 6913 2777 585 -811 -866 O ATOM 3192 CB GLN B 202 0.456 10.387 43.183 1.00 46.50 C ANISOU 3192 CB GLN B 202 5990 7990 3688 687 -943 -933 C ATOM 3193 CG GLN B 202 0.793 11.317 42.039 1.00 55.03 C ANISOU 3193 CG GLN B 202 7117 9141 4650 715 -977 -835 C ATOM 3194 CD GLN B 202 -0.211 12.443 41.898 1.00 62.24 C ANISOU 3194 CD GLN B 202 8042 10064 5542 767 -1056 -786 C ATOM 3195 OE1 GLN B 202 -1.388 12.286 42.233 1.00 64.14 O ANISOU 3195 OE1 GLN B 202 8241 10294 5835 789 -1089 -851 O ATOM 3196 NE2 GLN B 202 0.249 13.590 41.409 1.00 64.52 N ANISOU 3196 NE2 GLN B 202 8385 10370 5757 786 -1085 -666 N ATOM 3197 N GLY B 203 3.514 9.592 42.251 1.00 39.41 N ANISOU 3197 N GLY B 203 5154 7132 2689 604 -813 -860 N ATOM 3198 CA GLY B 203 4.914 9.969 42.235 1.00 42.26 C ANISOU 3198 CA GLY B 203 5569 7477 3011 577 -774 -772 C ATOM 3199 C GLY B 203 5.110 11.470 42.176 1.00 38.06 C ANISOU 3199 C GLY B 203 5099 6937 2426 606 -820 -643 C ATOM 3200 O GLY B 203 4.319 12.179 41.556 1.00 36.83 O ANISOU 3200 O GLY B 203 4947 6826 2221 651 -880 -611 O ATOM 3201 N ILE B 204 6.158 11.956 42.836 1.00 33.89 N ANISOU 3201 N ILE B 204 4617 6347 1913 582 -792 -565 N ATOM 3202 CA ILE B 204 6.556 13.352 42.713 1.00 35.99 C ANISOU 3202 CA ILE B 204 4944 6601 2130 605 -826 -428 C ATOM 3203 C ILE B 204 7.598 13.478 41.606 1.00 40.42 C ANISOU 3203 C ILE B 204 5539 7220 2597 596 -795 -356 C ATOM 3204 O ILE B 204 8.761 13.135 41.801 1.00 41.69 O ANISOU 3204 O ILE B 204 5719 7357 2763 557 -734 -335 O ATOM 3205 CB ILE B 204 7.137 13.902 44.030 1.00 35.09 C ANISOU 3205 CB ILE B 204 4863 6384 2085 585 -816 -372 C ATOM 3206 CG1 ILE B 204 6.071 13.877 45.128 1.00 35.32 C ANISOU 3206 CG1 ILE B 204 4861 6352 2206 598 -850 -437 C ATOM 3207 CG2 ILE B 204 7.657 15.317 43.831 1.00 35.22 C ANISOU 3207 CG2 ILE B 204 4942 6384 2057 606 -845 -221 C ATOM 3208 CD1 ILE B 204 6.598 14.221 46.512 1.00 34.03 C ANISOU 3208 CD1 ILE B 204 4724 6087 2120 576 -836 -404 C ATOM 3209 N PHE B 205 7.173 13.958 40.441 1.00 46.46 N ANISOU 3209 N PHE B 205 6310 8063 3279 633 -834 -319 N ATOM 3210 CA PHE B 205 8.066 14.064 39.288 1.00 48.58 C ANISOU 3210 CA PHE B 205 6609 8395 3454 628 -806 -255 C ATOM 3211 C PHE B 205 8.597 15.482 39.085 1.00 50.87 C ANISOU 3211 C PHE B 205 6961 8665 3704 647 -831 -101 C ATOM 3212 O PHE B 205 9.438 15.725 38.218 1.00 55.74 O ANISOU 3212 O PHE B 205 7609 9320 4250 642 -805 -29 O ATOM 3213 CB PHE B 205 7.377 13.553 38.021 1.00 48.84 C ANISOU 3213 CB PHE B 205 6608 8532 3416 653 -825 -317 C ATOM 3214 CG PHE B 205 7.058 12.086 38.058 1.00 48.93 C ANISOU 3214 CG PHE B 205 6560 8567 3466 630 -790 -460 C ATOM 3215 CD1 PHE B 205 8.019 11.147 37.717 1.00 47.52 C ANISOU 3215 CD1 PHE B 205 6375 8408 3273 591 -720 -495 C ATOM 3216 CD2 PHE B 205 5.800 11.645 38.434 1.00 49.05 C ANISOU 3216 CD2 PHE B 205 6524 8577 3536 646 -825 -557 C ATOM 3217 CE1 PHE B 205 7.731 9.796 37.755 1.00 45.89 C ANISOU 3217 CE1 PHE B 205 6111 8215 3111 569 -688 -623 C ATOM 3218 CE2 PHE B 205 5.506 10.295 38.471 1.00 50.06 C ANISOU 3218 CE2 PHE B 205 6594 8719 3709 624 -791 -684 C ATOM 3219 CZ PHE B 205 6.473 9.369 38.130 1.00 48.07 C ANISOU 3219 CZ PHE B 205 6335 8485 3446 586 -723 -716 C ATOM 3220 N ASN B 206 8.097 16.413 39.888 1.00 48.74 N ANISOU 3220 N ASN B 206 6706 8329 3484 667 -879 -50 N ATOM 3221 CA ASN B 206 8.629 17.767 39.916 1.00 51.75 C ANISOU 3221 CA ASN B 206 7143 8666 3852 680 -900 98 C ATOM 3222 C ASN B 206 8.243 18.470 41.206 1.00 52.48 C ANISOU 3222 C ASN B 206 7244 8661 4033 687 -935 127 C ATOM 3223 O ASN B 206 7.076 18.777 41.434 1.00 53.71 O ANISOU 3223 O ASN B 206 7378 8813 4215 720 -993 96 O ATOM 3224 CB ASN B 206 8.164 18.582 38.711 1.00 54.04 C ANISOU 3224 CB ASN B 206 7448 9024 4061 722 -950 167 C ATOM 3225 CG ASN B 206 8.802 19.956 38.665 1.00 57.37 C ANISOU 3225 CG ASN B 206 7926 9396 4475 731 -965 324 C ATOM 3226 OD1 ASN B 206 8.274 20.920 39.223 1.00 56.06 O ANISOU 3226 OD1 ASN B 206 7773 9173 4355 753 -1016 380 O ATOM 3227 ND2 ASN B 206 9.954 20.051 38.010 1.00 59.40 N ANISOU 3227 ND2 ASN B 206 8217 9671 4681 711 -918 396 N ATOM 3228 N ILE B 207 9.240 18.729 42.041 1.00 55.72 N ANISOU 3228 N ILE B 207 7688 8991 4491 656 -899 187 N ATOM 3229 CA ILE B 207 9.012 19.221 43.393 1.00 56.30 C ANISOU 3229 CA ILE B 207 7769 8965 4657 657 -921 203 C ATOM 3230 C ILE B 207 8.308 20.578 43.452 1.00 56.75 C ANISOU 3230 C ILE B 207 7846 8989 4728 699 -993 291 C ATOM 3231 O ILE B 207 7.457 20.800 44.312 1.00 56.74 O ANISOU 3231 O ILE B 207 7827 8939 4791 716 -1032 257 O ATOM 3232 CB ILE B 207 10.331 19.270 44.188 1.00 55.78 C ANISOU 3232 CB ILE B 207 7739 8821 4633 615 -865 261 C ATOM 3233 CG1 ILE B 207 10.965 17.877 44.227 1.00 54.66 C ANISOU 3233 CG1 ILE B 207 7573 8706 4488 571 -793 165 C ATOM 3234 CG2 ILE B 207 10.091 19.807 45.591 1.00 54.83 C ANISOU 3234 CG2 ILE B 207 7629 8597 4608 617 -890 278 C ATOM 3235 CD1 ILE B 207 12.302 17.832 44.921 1.00 53.05 C ANISOU 3235 CD1 ILE B 207 7402 8433 4321 527 -734 218 C ATOM 3236 N GLN B 208 8.653 21.480 42.537 1.00 57.23 N ANISOU 3236 N GLN B 208 7941 9073 4732 715 -1008 403 N ATOM 3237 CA GLN B 208 8.060 22.815 42.550 1.00 55.11 C ANISOU 3237 CA GLN B 208 7691 8767 4481 751 -1073 496 C ATOM 3238 C GLN B 208 6.588 22.794 42.138 1.00 50.52 C ANISOU 3238 C GLN B 208 7071 8244 3881 794 -1135 430 C ATOM 3239 O GLN B 208 5.769 23.518 42.704 1.00 48.30 O ANISOU 3239 O GLN B 208 6785 7915 3652 820 -1188 448 O ATOM 3240 CB GLN B 208 8.840 23.779 41.654 1.00 60.80 C ANISOU 3240 CB GLN B 208 8457 9492 5150 754 -1071 633 C ATOM 3241 CG GLN B 208 8.445 25.236 41.856 1.00 68.27 C ANISOU 3241 CG GLN B 208 9428 10375 6137 782 -1130 742 C ATOM 3242 CD GLN B 208 8.586 26.070 40.596 1.00 76.07 C ANISOU 3242 CD GLN B 208 10441 11407 7053 802 -1151 841 C ATOM 3243 OE1 GLN B 208 8.349 27.279 40.610 1.00 79.06 O ANISOU 3243 OE1 GLN B 208 10841 11737 7461 822 -1195 936 O ATOM 3244 NE2 GLN B 208 8.965 25.426 39.495 1.00 77.97 N ANISOU 3244 NE2 GLN B 208 10680 11742 7203 798 -1118 817 N ATOM 3245 N ASN B 209 6.259 21.969 41.147 1.00 45.10 N ANISOU 3245 N ASN B 209 6356 7660 3121 800 -1127 354 N ATOM 3246 CA ASN B 209 4.878 21.826 40.694 1.00 47.13 C ANISOU 3246 CA ASN B 209 6572 7977 3358 838 -1182 282 C ATOM 3247 C ASN B 209 4.028 21.073 41.705 1.00 48.11 C ANISOU 3247 C ASN B 209 6650 8070 3559 836 -1188 158 C ATOM 3248 O ASN B 209 2.838 21.349 41.865 1.00 50.86 O ANISOU 3248 O ASN B 209 6972 8418 3933 869 -1243 125 O ATOM 3249 CB ASN B 209 4.825 21.127 39.335 1.00 48.42 C ANISOU 3249 CB ASN B 209 6718 8256 3425 843 -1168 236 C ATOM 3250 CG ASN B 209 4.981 22.092 38.181 1.00 52.66 C ANISOU 3250 CG ASN B 209 7288 8838 3883 868 -1196 349 C ATOM 3251 OD1 ASN B 209 4.086 22.230 37.349 1.00 58.36 O ANISOU 3251 OD1 ASN B 209 7991 9628 4554 903 -1242 333 O ATOM 3252 ND2 ASN B 209 6.115 22.781 38.135 1.00 52.05 N ANISOU 3252 ND2 ASN B 209 7260 8719 3798 851 -1169 466 N ATOM 3253 N PHE B 210 4.650 20.112 42.378 1.00 45.86 N ANISOU 3253 N PHE B 210 6354 7758 3312 796 -1130 89 N ATOM 3254 CA PHE B 210 4.003 19.389 43.461 1.00 42.12 C ANISOU 3254 CA PHE B 210 5840 7241 2921 787 -1128 -23 C ATOM 3255 C PHE B 210 3.537 20.377 44.525 1.00 40.56 C ANISOU 3255 C PHE B 210 5658 6952 2802 808 -1172 27 C ATOM 3256 O PHE B 210 2.372 20.379 44.922 1.00 40.91 O ANISOU 3256 O PHE B 210 5669 6986 2890 834 -1214 -35 O ATOM 3257 CB PHE B 210 4.969 18.361 44.055 1.00 40.25 C ANISOU 3257 CB PHE B 210 5600 6977 2716 736 -1054 -80 C ATOM 3258 CG PHE B 210 4.503 17.765 45.354 1.00 42.62 C ANISOU 3258 CG PHE B 210 5868 7210 3114 722 -1045 -175 C ATOM 3259 CD1 PHE B 210 3.423 16.898 45.388 1.00 44.73 C ANISOU 3259 CD1 PHE B 210 6077 7506 3410 731 -1055 -302 C ATOM 3260 CD2 PHE B 210 5.153 18.066 46.540 1.00 44.72 C ANISOU 3260 CD2 PHE B 210 6162 7382 3447 701 -1026 -137 C ATOM 3261 CE1 PHE B 210 2.992 16.350 46.584 1.00 44.44 C ANISOU 3261 CE1 PHE B 210 6011 7405 3471 717 -1045 -388 C ATOM 3262 CE2 PHE B 210 4.730 17.520 47.740 1.00 46.81 C ANISOU 3262 CE2 PHE B 210 6399 7585 3803 688 -1018 -225 C ATOM 3263 CZ PHE B 210 3.648 16.660 47.761 1.00 46.82 C ANISOU 3263 CZ PHE B 210 6341 7614 3835 696 -1026 -350 C ATOM 3264 N ILE B 211 4.450 21.234 44.966 1.00 40.90 N ANISOU 3264 N ILE B 211 5750 6927 2864 796 -1163 140 N ATOM 3265 CA ILE B 211 4.146 22.205 46.011 1.00 43.20 C ANISOU 3265 CA ILE B 211 6058 7121 3234 813 -1200 195 C ATOM 3266 C ILE B 211 3.063 23.196 45.587 1.00 48.51 C ANISOU 3266 C ILE B 211 6725 7807 3900 861 -1272 240 C ATOM 3267 O ILE B 211 2.085 23.404 46.309 1.00 47.96 O ANISOU 3267 O ILE B 211 6633 7697 3894 884 -1311 199 O ATOM 3268 CB ILE B 211 5.408 22.961 46.449 1.00 43.30 C ANISOU 3268 CB ILE B 211 6125 7058 3270 789 -1173 318 C ATOM 3269 CG1 ILE B 211 6.314 22.029 47.255 1.00 42.55 C ANISOU 3269 CG1 ILE B 211 6031 6925 3209 743 -1107 264 C ATOM 3270 CG2 ILE B 211 5.037 24.179 47.284 1.00 42.66 C ANISOU 3270 CG2 ILE B 211 6062 6882 3264 812 -1219 394 C ATOM 3271 CD1 ILE B 211 7.756 22.433 47.237 1.00 45.05 C ANISOU 3271 CD1 ILE B 211 6398 7203 3517 712 -1063 374 C ATOM 3272 N ASN B 212 3.238 23.801 44.416 1.00 52.67 N ANISOU 3272 N ASN B 212 7273 8389 4351 875 -1290 324 N ATOM 3273 CA ASN B 212 2.248 24.736 43.891 1.00 56.11 C ANISOU 3273 CA ASN B 212 7703 8844 4772 920 -1358 371 C ATOM 3274 C ASN B 212 0.845 24.135 43.892 1.00 58.26 C ANISOU 3274 C ASN B 212 7921 9160 5054 947 -1393 251 C ATOM 3275 O ASN B 212 -0.104 24.758 44.365 1.00 59.88 O ANISOU 3275 O ASN B 212 8113 9326 5311 977 -1443 254 O ATOM 3276 CB ASN B 212 2.629 25.197 42.482 1.00 60.10 C ANISOU 3276 CB ASN B 212 8233 9422 5181 929 -1364 456 C ATOM 3277 CG ASN B 212 3.925 25.979 42.457 1.00 60.32 C ANISOU 3277 CG ASN B 212 8315 9396 5208 905 -1335 588 C ATOM 3278 OD1 ASN B 212 4.386 26.471 43.487 1.00 61.74 O ANISOU 3278 OD1 ASN B 212 8515 9477 5465 890 -1326 636 O ATOM 3279 ND2 ASN B 212 4.519 26.101 41.277 1.00 60.07 N ANISOU 3279 ND2 ASN B 212 8305 9427 5092 903 -1320 646 N ATOM 3280 N THR B 213 0.726 22.920 43.367 1.00 56.57 N ANISOU 3280 N THR B 213 7675 9024 4797 935 -1364 144 N ATOM 3281 CA THR B 213 -0.551 22.217 43.336 1.00 56.01 C ANISOU 3281 CA THR B 213 7548 8994 4740 956 -1390 22 C ATOM 3282 C THR B 213 -1.153 22.069 44.731 1.00 55.74 C ANISOU 3282 C THR B 213 7491 8875 4812 956 -1397 -44 C ATOM 3283 O THR B 213 -2.350 22.286 44.922 1.00 55.37 O ANISOU 3283 O THR B 213 7415 8824 4800 989 -1445 -83 O ATOM 3284 CB THR B 213 -0.411 20.824 42.703 1.00 56.10 C ANISOU 3284 CB THR B 213 7527 9085 4704 933 -1345 -86 C ATOM 3285 OG1 THR B 213 -0.107 20.961 41.309 1.00 57.55 O ANISOU 3285 OG1 THR B 213 7725 9357 4784 942 -1348 -36 O ATOM 3286 CG2 THR B 213 -1.702 20.033 42.862 1.00 54.02 C ANISOU 3286 CG2 THR B 213 7202 8846 4477 949 -1366 -218 C ATOM 3287 N LEU B 214 -0.322 21.696 45.701 1.00 52.11 N ANISOU 3287 N LEU B 214 7045 8350 4406 921 -1349 -57 N ATOM 3288 CA LEU B 214 -0.778 21.577 47.081 1.00 53.07 C ANISOU 3288 CA LEU B 214 7150 8384 4629 919 -1351 -115 C ATOM 3289 C LEU B 214 -1.394 22.888 47.558 1.00 57.09 C ANISOU 3289 C LEU B 214 7675 8830 5185 957 -1410 -37 C ATOM 3290 O LEU B 214 -2.404 22.890 48.264 1.00 56.01 O ANISOU 3290 O LEU B 214 7510 8656 5115 978 -1439 -98 O ATOM 3291 CB LEU B 214 0.372 21.171 48.006 1.00 48.30 C ANISOU 3291 CB LEU B 214 6568 7714 4068 875 -1293 -114 C ATOM 3292 CG LEU B 214 0.729 19.687 48.101 1.00 45.59 C ANISOU 3292 CG LEU B 214 6194 7400 3729 835 -1231 -229 C ATOM 3293 CD1 LEU B 214 1.823 19.470 49.140 1.00 43.65 C ANISOU 3293 CD1 LEU B 214 5975 7076 3534 794 -1180 -217 C ATOM 3294 CD2 LEU B 214 -0.496 18.864 48.448 1.00 44.85 C ANISOU 3294 CD2 LEU B 214 6039 7313 3688 845 -1241 -363 C ATOM 3295 N LEU B 215 -0.783 24.000 47.162 1.00 58.73 N ANISOU 3295 N LEU B 215 7929 9023 5363 963 -1426 99 N ATOM 3296 CA LEU B 215 -1.244 25.317 47.583 1.00 59.69 C ANISOU 3296 CA LEU B 215 8068 9078 5534 994 -1477 186 C ATOM 3297 C LEU B 215 -2.581 25.679 46.940 1.00 64.57 C ANISOU 3297 C LEU B 215 8655 9746 6131 1038 -1538 169 C ATOM 3298 O LEU B 215 -3.392 26.388 47.536 1.00 64.80 O ANISOU 3298 O LEU B 215 8676 9720 6224 1067 -1581 181 O ATOM 3299 CB LEU B 215 -0.195 26.381 47.258 1.00 57.28 C ANISOU 3299 CB LEU B 215 7816 8742 5206 984 -1472 338 C ATOM 3300 CG LEU B 215 1.219 26.070 47.744 1.00 54.70 C ANISOU 3300 CG LEU B 215 7522 8370 4890 939 -1410 368 C ATOM 3301 CD1 LEU B 215 2.076 27.320 47.701 1.00 55.58 C ANISOU 3301 CD1 LEU B 215 7683 8422 5014 932 -1413 522 C ATOM 3302 CD2 LEU B 215 1.174 25.503 49.148 1.00 52.81 C ANISOU 3302 CD2 LEU B 215 7272 8055 4738 924 -1388 286 C ATOM 3303 N LYS B 216 -2.805 25.187 45.725 1.00 68.61 N ANISOU 3303 N LYS B 216 9150 10362 6557 1044 -1542 140 N ATOM 3304 CA LYS B 216 -4.044 25.457 45.003 1.00 74.31 C ANISOU 3304 CA LYS B 216 9842 11142 7251 1085 -1599 122 C ATOM 3305 C LYS B 216 -5.277 25.069 45.816 1.00 77.00 C ANISOU 3305 C LYS B 216 10137 11453 7668 1105 -1622 14 C ATOM 3306 O LYS B 216 -6.211 25.859 45.958 1.00 77.68 O ANISOU 3306 O LYS B 216 10213 11515 7787 1141 -1675 39 O ATOM 3307 CB LYS B 216 -4.054 24.726 43.657 1.00 78.83 C ANISOU 3307 CB LYS B 216 10399 11831 7722 1084 -1591 83 C ATOM 3308 CG LYS B 216 -3.440 25.508 42.504 1.00 83.04 C ANISOU 3308 CG LYS B 216 10970 12411 8169 1089 -1602 204 C ATOM 3309 CD LYS B 216 -2.063 26.041 42.858 1.00 85.88 C ANISOU 3309 CD LYS B 216 11382 12709 8540 1058 -1564 308 C ATOM 3310 CE LYS B 216 -1.321 26.552 41.631 1.00 89.56 C ANISOU 3310 CE LYS B 216 11884 13229 8915 1057 -1561 412 C ATOM 3311 NZ LYS B 216 -0.993 25.457 40.673 1.00 90.48 N ANISOU 3311 NZ LYS B 216 11988 13446 8945 1042 -1524 344 N ATOM 3312 N ASP B 217 -5.272 23.851 46.348 1.00 78.99 N ANISOU 3312 N ASP B 217 10359 11704 7950 1081 -1580 -106 N ATOM 3313 CA ASP B 217 -6.409 23.341 47.108 1.00 80.63 C ANISOU 3313 CA ASP B 217 10520 11884 8232 1096 -1593 -218 C ATOM 3314 C ASP B 217 -6.391 23.843 48.550 1.00 79.52 C ANISOU 3314 C ASP B 217 10394 11627 8194 1096 -1593 -204 C ATOM 3315 O ASP B 217 -6.482 25.044 48.803 1.00 79.85 O ANISOU 3315 O ASP B 217 10462 11616 8261 1118 -1630 -109 O ATOM 3316 CB ASP B 217 -6.416 21.811 47.087 1.00 82.28 C ANISOU 3316 CB ASP B 217 10688 12135 8441 1068 -1544 -350 C ATOM 3317 CG ASP B 217 -6.022 21.247 45.735 1.00 85.83 C ANISOU 3317 CG ASP B 217 11134 12690 8789 1057 -1527 -355 C ATOM 3318 OD1 ASP B 217 -4.823 20.957 45.540 1.00 85.37 O ANISOU 3318 OD1 ASP B 217 11104 12641 8693 1022 -1480 -323 O ATOM 3319 OD2 ASP B 217 -6.908 21.096 44.866 1.00 88.31 O ANISOU 3319 OD2 ASP B 217 11417 13076 9060 1084 -1561 -391 O TER 3320 ASP B 217 ATOM 3321 OP3 DT C 1 22.577 -7.345 60.499 1.00111.78 O ANISOU 3321 OP3 DT C 1 15143 14297 13033 1504 283 -23 O ATOM 3322 P DT C 1 22.328 -6.084 61.231 1.00110.52 P ANISOU 3322 P DT C 1 14940 14169 12885 1404 231 52 P ATOM 3323 OP1 DT C 1 20.901 -5.740 61.049 1.00109.66 O ANISOU 3323 OP1 DT C 1 14834 14011 12821 1341 163 -92 O ATOM 3324 OP2 DT C 1 23.359 -5.114 60.803 1.00110.10 O ANISOU 3324 OP2 DT C 1 14853 14254 12725 1443 215 193 O ATOM 3325 O5' DT C 1 22.561 -6.382 62.786 1.00 49.40 O ANISOU 3325 O5' DT C 1 7191 6349 5231 1328 280 137 O ATOM 3326 C5' DT C 1 23.676 -5.836 63.481 1.00 42.41 C ANISOU 3326 C5' DT C 1 6272 5529 4312 1315 301 318 C ATOM 3327 C4' DT C 1 23.214 -5.297 64.821 1.00 34.98 C ANISOU 3327 C4' DT C 1 5318 4527 3445 1194 285 360 C ATOM 3328 O4' DT C 1 22.721 -3.944 64.652 1.00 32.74 O ANISOU 3328 O4' DT C 1 5013 4302 3126 1136 207 369 O ATOM 3329 C3' DT C 1 22.075 -6.084 65.468 1.00 33.61 C ANISOU 3329 C3' DT C 1 5176 4205 3388 1135 302 230 C ATOM 3330 O3' DT C 1 22.316 -6.233 66.869 1.00 29.66 O ANISOU 3330 O3' DT C 1 4677 3638 2953 1070 342 316 O ATOM 3331 C2' DT C 1 20.842 -5.221 65.193 1.00 32.63 C ANISOU 3331 C2' DT C 1 5043 4079 3278 1071 224 132 C ATOM 3332 C1' DT C 1 21.461 -3.832 65.278 1.00 31.43 C ANISOU 3332 C1' DT C 1 4858 4039 3048 1046 179 273 C ATOM 3333 N1 DT C 1 20.698 -2.751 64.600 1.00 32.75 N ANISOU 3333 N1 DT C 1 5013 4259 3170 1025 97 216 N ATOM 3334 C2 DT C 1 20.308 -1.671 65.356 1.00 33.38 C ANISOU 3334 C2 DT C 1 5082 4339 3263 934 55 269 C ATOM 3335 O2 DT C 1 20.567 -1.575 66.540 1.00 36.71 O ANISOU 3335 O2 DT C 1 5502 4716 3728 868 81 358 O ATOM 3336 N3 DT C 1 19.615 -0.708 64.668 1.00 34.15 N ANISOU 3336 N3 DT C 1 5173 4487 3313 926 -18 214 N ATOM 3337 C4 DT C 1 19.280 -0.724 63.329 1.00 34.37 C ANISOU 3337 C4 DT C 1 5206 4568 3286 999 -54 114 C ATOM 3338 O4 DT C 1 18.654 0.194 62.804 1.00 31.57 O ANISOU 3338 O4 DT C 1 4848 4257 2889 990 -121 73 O ATOM 3339 C5 DT C 1 19.722 -1.887 62.592 1.00 35.04 C ANISOU 3339 C5 DT C 1 5303 4649 3361 1090 -8 62 C ATOM 3340 C7 DT C 1 19.417 -2.009 61.127 1.00 33.25 C ANISOU 3340 C7 DT C 1 5089 4474 3071 1175 -44 -48 C ATOM 3341 C6 DT C 1 20.401 -2.833 63.254 1.00 36.33 C ANISOU 3341 C6 DT C 1 5474 4761 3569 1099 66 116 C ATOM 3342 P DT C 2 22.925 -7.606 67.440 1.00 36.52 P ANISOU 3342 P DT C 2 5578 4429 3868 1115 434 338 P ATOM 3343 OP1 DT C 2 24.401 -7.488 67.424 1.00 31.30 O ANISOU 3343 OP1 DT C 2 4892 3870 3130 1180 463 500 O ATOM 3344 OP2 DT C 2 22.268 -8.728 66.733 1.00 45.31 O ANISOU 3344 OP2 DT C 2 6735 5466 5015 1163 460 177 O ATOM 3345 O5' DT C 2 22.377 -7.661 68.938 1.00 51.25 O ANISOU 3345 O5' DT C 2 7458 6179 5835 1007 453 350 O ATOM 3346 C5' DT C 2 22.725 -6.629 69.816 1.00 46.36 C ANISOU 3346 C5' DT C 2 6811 5599 5205 937 425 481 C ATOM 3347 C4' DT C 2 21.527 -5.935 70.429 1.00 36.47 C ANISOU 3347 C4' DT C 2 5560 4282 4015 827 379 422 C ATOM 3348 O4' DT C 2 22.064 -5.088 71.466 1.00 29.67 O ANISOU 3348 O4' DT C 2 4685 3446 3142 763 367 570 O ATOM 3349 C3' DT C 2 20.817 -4.915 69.558 1.00 32.41 C ANISOU 3349 C3' DT C 2 5023 3836 3457 811 299 358 C ATOM 3350 O3' DT C 2 19.691 -4.391 70.286 1.00 32.25 O ANISOU 3350 O3' DT C 2 5007 3742 3505 712 268 306 O ATOM 3351 C2' DT C 2 21.949 -3.897 69.427 1.00 29.22 C ANISOU 3351 C2' DT C 2 4588 3563 2951 827 270 520 C ATOM 3352 C1' DT C 2 22.459 -3.863 70.870 1.00 28.81 C ANISOU 3352 C1' DT C 2 4542 3464 2940 765 303 643 C ATOM 3353 N1 DT C 2 23.935 -3.729 71.090 1.00 28.93 N ANISOU 3353 N1 DT C 2 4534 3568 2889 801 325 813 N ATOM 3354 C2 DT C 2 24.396 -2.632 71.790 1.00 30.19 C ANISOU 3354 C2 DT C 2 4677 3779 3014 733 289 947 C ATOM 3355 O2 DT C 2 23.666 -1.756 72.212 1.00 27.97 O ANISOU 3355 O2 DT C 2 4405 3472 2749 650 243 935 O ATOM 3356 N3 DT C 2 25.756 -2.595 71.975 1.00 29.18 N ANISOU 3356 N3 DT C 2 4522 3734 2830 766 310 1098 N ATOM 3357 C4 DT C 2 26.682 -3.526 71.540 1.00 31.17 C ANISOU 3357 C4 DT C 2 4760 4025 3057 865 365 1129 C ATOM 3358 O4 DT C 2 27.880 -3.402 71.756 1.00 31.12 O ANISOU 3358 O4 DT C 2 4722 4102 3002 889 380 1270 O ATOM 3359 C5 DT C 2 26.137 -4.654 70.828 1.00 29.43 C ANISOU 3359 C5 DT C 2 4567 3743 2873 938 405 984 C ATOM 3360 C7 DT C 2 27.048 -5.726 70.313 1.00 30.56 C ANISOU 3360 C7 DT C 2 4707 3916 2988 1054 469 1005 C ATOM 3361 C6 DT C 2 24.811 -4.703 70.643 1.00 28.18 C ANISOU 3361 C6 DT C 2 4436 3500 2769 900 381 834 C ATOM 3362 P DT C 3 18.475 -3.670 69.512 1.00 27.87 P ANISOU 3362 P DT C 3 4437 3208 2945 688 194 182 P ATOM 3363 OP1 DT C 3 17.285 -3.715 70.389 1.00 31.10 O ANISOU 3363 OP1 DT C 3 4856 3505 3456 599 195 104 O ATOM 3364 OP2 DT C 3 18.410 -4.226 68.142 1.00 28.01 O ANISOU 3364 OP2 DT C 3 4454 3267 2923 776 185 78 O ATOM 3365 O5' DT C 3 18.948 -2.150 69.402 1.00 30.36 O ANISOU 3365 O5' DT C 3 4731 3639 3166 669 131 303 O ATOM 3366 C5' DT C 3 18.888 -1.295 70.537 1.00 30.11 C ANISOU 3366 C5' DT C 3 4704 3586 3152 581 117 397 C ATOM 3367 C4' DT C 3 19.624 -0.007 70.229 1.00 32.62 C ANISOU 3367 C4' DT C 3 5007 4025 3361 581 65 521 C ATOM 3368 O4' DT C 3 21.039 -0.201 70.426 1.00 33.04 O ANISOU 3368 O4' DT C 3 5051 4136 3366 615 102 663 O ATOM 3369 C3' DT C 3 19.499 0.451 68.782 1.00 30.29 C ANISOU 3369 C3' DT C 3 4698 3829 2984 647 14 463 C ATOM 3370 O3' DT C 3 18.414 1.363 68.699 1.00 26.28 O ANISOU 3370 O3' DT C 3 4193 3315 2478 599 -47 398 O ATOM 3371 C2' DT C 3 20.850 1.100 68.461 1.00 31.49 C ANISOU 3371 C2' DT C 3 4834 4102 3027 679 7 616 C ATOM 3372 C1' DT C 3 21.725 0.776 69.675 1.00 29.52 C ANISOU 3372 C1' DT C 3 4587 3820 2811 642 58 746 C ATOM 3373 N1 DT C 3 23.079 0.213 69.404 1.00 29.15 N ANISOU 3373 N1 DT C 3 4519 3840 2716 712 103 842 N ATOM 3374 C2 DT C 3 24.153 0.698 70.127 1.00 32.18 C ANISOU 3374 C2 DT C 3 4889 4274 3063 679 110 1009 C ATOM 3375 O2 DT C 3 24.051 1.582 70.964 1.00 30.82 O ANISOU 3375 O2 DT C 3 4728 4090 2892 592 79 1081 O ATOM 3376 N3 DT C 3 25.362 0.113 69.828 1.00 31.61 N ANISOU 3376 N3 DT C 3 4791 4269 2951 752 154 1091 N ATOM 3377 C4 DT C 3 25.595 -0.892 68.909 1.00 31.78 C ANISOU 3377 C4 DT C 3 4806 4305 2962 857 194 1023 C ATOM 3378 O4 DT C 3 26.717 -1.349 68.722 1.00 33.21 O ANISOU 3378 O4 DT C 3 4964 4550 3105 923 235 1110 O ATOM 3379 C5 DT C 3 24.430 -1.363 68.197 1.00 28.94 C ANISOU 3379 C5 DT C 3 4471 3883 2640 884 184 846 C ATOM 3380 C7 DT C 3 24.568 -2.449 67.171 1.00 30.80 C ANISOU 3380 C7 DT C 3 4714 4124 2865 994 223 759 C ATOM 3381 C6 DT C 3 23.243 -0.801 68.477 1.00 32.94 C ANISOU 3381 C6 DT C 3 4996 4330 3191 810 138 764 C ATOM 3382 P DT C 4 17.634 1.575 67.311 1.00 28.49 P ANISOU 3382 P DT C 4 4464 3647 2716 656 -102 264 P ATOM 3383 OP1 DT C 4 18.555 1.207 66.205 1.00 27.29 O ANISOU 3383 OP1 DT C 4 4304 3582 2484 753 -91 282 O ATOM 3384 OP2 DT C 4 17.016 2.916 67.341 1.00 25.37 O ANISOU 3384 OP2 DT C 4 4073 3285 2282 610 -168 275 O ATOM 3385 O5' DT C 4 16.471 0.481 67.360 1.00 27.65 O ANISOU 3385 O5' DT C 4 4356 3430 2719 649 -81 93 O ATOM 3386 C5' DT C 4 16.716 -0.879 67.061 1.00 28.23 C ANISOU 3386 C5' DT C 4 4434 3460 2831 701 -27 30 C ATOM 3387 C4' DT C 4 15.484 -1.708 67.372 1.00 30.84 C ANISOU 3387 C4' DT C 4 4768 3675 3277 662 -11 -122 C ATOM 3388 O4' DT C 4 15.171 -1.641 68.787 1.00 31.24 O ANISOU 3388 O4' DT C 4 4826 3634 3410 571 19 -77 O ATOM 3389 C3' DT C 4 14.202 -1.282 66.666 1.00 33.03 C ANISOU 3389 C3' DT C 4 5027 3963 3561 655 -78 -262 C ATOM 3390 O3' DT C 4 13.431 -2.454 66.480 1.00 35.74 O ANISOU 3390 O3' DT C 4 5370 4221 3988 656 -53 -411 O ATOM 3391 C2' DT C 4 13.555 -0.355 67.692 1.00 29.61 C ANISOU 3391 C2' DT C 4 4588 3496 3167 564 -100 -222 C ATOM 3392 C1' DT C 4 13.878 -1.100 68.986 1.00 29.04 C ANISOU 3392 C1' DT C 4 4535 3321 3180 512 -23 -165 C ATOM 3393 N1 DT C 4 13.936 -0.268 70.228 1.00 29.74 N ANISOU 3393 N1 DT C 4 4634 3382 3284 434 -20 -51 N ATOM 3394 C2 DT C 4 12.841 -0.200 71.070 1.00 27.31 C ANISOU 3394 C2 DT C 4 4326 2984 3067 358 -16 -109 C ATOM 3395 O2 DT C 4 11.790 -0.771 70.863 1.00 27.50 O ANISOU 3395 O2 DT C 4 4334 2951 3164 346 -15 -251 O ATOM 3396 N3 DT C 4 13.015 0.580 72.177 1.00 24.66 N ANISOU 3396 N3 DT C 4 4010 2626 2732 294 -12 7 N ATOM 3397 C4 DT C 4 14.147 1.284 72.532 1.00 28.39 C ANISOU 3397 C4 DT C 4 4502 3157 3127 291 -16 170 C ATOM 3398 O4 DT C 4 14.202 1.954 73.551 1.00 28.28 O ANISOU 3398 O4 DT C 4 4511 3114 3119 228 -15 262 O ATOM 3399 C5 DT C 4 15.259 1.172 71.622 1.00 27.04 C ANISOU 3399 C5 DT C 4 4322 3084 2868 367 -21 224 C ATOM 3400 C7 DT C 4 16.542 1.895 71.915 1.00 25.64 C ANISOU 3400 C7 DT C 4 4156 2982 2604 365 -26 400 C ATOM 3401 C6 DT C 4 15.101 0.411 70.532 1.00 27.10 C ANISOU 3401 C6 DT C 4 4312 3113 2872 437 -21 114 C ATOM 3402 P DT C 5 12.718 -2.744 65.071 1.00 36.16 P ANISOU 3402 P DT C 5 5413 4311 4015 715 -105 -572 P ATOM 3403 OP1 DT C 5 12.454 -4.198 64.993 1.00 37.10 O ANISOU 3403 OP1 DT C 5 5549 4338 4210 724 -53 -682 O ATOM 3404 OP2 DT C 5 13.507 -2.076 64.011 1.00 34.01 O ANISOU 3404 OP2 DT C 5 5143 4164 3614 797 -145 -511 O ATOM 3405 O5' DT C 5 11.327 -1.951 65.180 1.00 40.88 O ANISOU 3405 O5' DT C 5 5978 4901 4652 655 -170 -659 O ATOM 3406 C5' DT C 5 10.236 -2.443 65.963 1.00 38.14 C ANISOU 3406 C5' DT C 5 5616 4446 4427 576 -150 -752 C ATOM 3407 C4' DT C 5 8.905 -2.177 65.274 1.00 35.46 C ANISOU 3407 C4' DT C 5 5241 4125 4108 569 -220 -903 C ATOM 3408 O4' DT C 5 8.619 -0.754 65.247 1.00 30.35 O ANISOU 3408 O4' DT C 5 4577 3553 3401 562 -285 -851 O ATOM 3409 C3' DT C 5 8.846 -2.610 63.816 1.00 38.34 C ANISOU 3409 C3' DT C 5 5606 4547 4415 651 -262 -1012 C ATOM 3410 O3' DT C 5 7.518 -2.949 63.450 1.00 42.87 O ANISOU 3410 O3' DT C 5 6146 5089 5055 624 -301 -1181 O ATOM 3411 C2' DT C 5 9.295 -1.355 63.078 1.00 37.04 C ANISOU 3411 C2' DT C 5 5442 4509 4123 709 -326 -937 C ATOM 3412 C1' DT C 5 8.616 -0.277 63.913 1.00 31.84 C ANISOU 3412 C1' DT C 5 4760 3846 3491 639 -355 -897 C ATOM 3413 N1 DT C 5 9.345 1.013 63.874 1.00 30.69 N ANISOU 3413 N1 DT C 5 4631 3790 3238 661 -385 -755 N ATOM 3414 C2 DT C 5 8.764 2.126 63.303 1.00 33.12 C ANISOU 3414 C2 DT C 5 4927 4174 3481 681 -462 -778 C ATOM 3415 O2 DT C 5 7.647 2.137 62.811 1.00 34.97 O ANISOU 3415 O2 DT C 5 5131 4412 3742 685 -513 -910 O ATOM 3416 N3 DT C 5 9.550 3.248 63.335 1.00 33.59 N ANISOU 3416 N3 DT C 5 5012 4307 3442 696 -479 -637 N ATOM 3417 C4 DT C 5 10.826 3.361 63.858 1.00 33.52 C ANISOU 3417 C4 DT C 5 5032 4309 3395 689 -431 -480 C ATOM 3418 O4 DT C 5 11.443 4.420 63.835 1.00 38.23 O ANISOU 3418 O4 DT C 5 5649 4974 3901 696 -453 -362 O ATOM 3419 C5 DT C 5 11.377 2.156 64.429 1.00 32.53 C ANISOU 3419 C5 DT C 5 4911 4108 3341 674 -354 -465 C ATOM 3420 C7 DT C 5 12.753 2.151 65.030 1.00 33.58 C ANISOU 3420 C7 DT C 5 5067 4251 3441 669 -299 -300 C ATOM 3421 C6 DT C 5 10.620 1.053 64.407 1.00 31.15 C ANISOU 3421 C6 DT C 5 4719 3856 3261 663 -333 -601 C ATOM 3422 P DT C 6 7.250 -4.156 62.424 1.00 54.13 P ANISOU 3422 P DT C 6 7582 6492 6492 668 -305 -1334 P ATOM 3423 OP1 DT C 6 7.308 -5.422 63.187 1.00 53.53 O ANISOU 3423 OP1 DT C 6 7528 6293 6517 621 -219 -1359 O ATOM 3424 OP2 DT C 6 8.131 -3.959 61.251 1.00 55.38 O ANISOU 3424 OP2 DT C 6 7769 6748 6524 773 -334 -1300 O ATOM 3425 O5' DT C 6 5.746 -3.913 61.939 1.00 86.25 O ANISOU 3425 O5' DT C 6 11597 10573 10601 639 -383 -1493 O ATOM 3426 C5' DT C 6 5.441 -2.857 61.036 1.00 87.56 C ANISOU 3426 C5' DT C 6 11742 10851 10676 691 -475 -1511 C ATOM 3427 C4' DT C 6 4.335 -3.281 60.087 1.00 90.73 C ANISOU 3427 C4' DT C 6 12111 11262 11099 701 -540 -1697 C ATOM 3428 O4' DT C 6 4.853 -4.255 59.141 1.00 92.67 O ANISOU 3428 O4' DT C 6 12400 11506 11305 766 -530 -1758 O ATOM 3429 C3' DT C 6 3.128 -3.930 60.764 1.00 91.58 C ANISOU 3429 C3' DT C 6 12173 11275 11348 605 -525 -1814 C ATOM 3430 O3' DT C 6 1.915 -3.400 60.233 1.00 91.01 O ANISOU 3430 O3' DT C 6 12042 11256 11283 598 -613 -1929 O ATOM 3431 C2' DT C 6 3.289 -5.412 60.433 1.00 93.70 C ANISOU 3431 C2' DT C 6 12476 11467 11659 607 -479 -1906 C ATOM 3432 C1' DT C 6 3.957 -5.346 59.063 1.00 94.49 C ANISOU 3432 C1' DT C 6 12615 11656 11631 718 -525 -1916 C ATOM 3433 N1 DT C 6 4.708 -6.589 58.672 1.00 95.59 N ANISOU 3433 N1 DT C 6 12817 11742 11761 759 -468 -1938 N ATOM 3434 C2 DT C 6 4.099 -7.507 57.843 1.00 97.00 C ANISOU 3434 C2 DT C 6 13003 11892 11959 767 -496 -2101 C ATOM 3435 O2 DT C 6 2.970 -7.364 57.406 1.00 98.18 O ANISOU 3435 O2 DT C 6 13105 12062 12137 740 -569 -2230 O ATOM 3436 N3 DT C 6 4.868 -8.605 57.543 1.00 97.26 N ANISOU 3436 N3 DT C 6 13105 11872 11975 809 -436 -2107 N ATOM 3437 C4 DT C 6 6.155 -8.872 57.980 1.00 97.00 C ANISOU 3437 C4 DT C 6 13125 11819 11910 847 -352 -1968 C ATOM 3438 O4 DT C 6 6.767 -9.887 57.658 1.00 97.83 O ANISOU 3438 O4 DT C 6 13293 11878 12000 891 -301 -1984 O ATOM 3439 C5 DT C 6 6.731 -7.871 58.843 1.00 95.64 C ANISOU 3439 C5 DT C 6 12932 11685 11721 833 -331 -1802 C ATOM 3440 C7 DT C 6 8.123 -8.047 59.382 1.00 94.83 C ANISOU 3440 C7 DT C 6 12875 11572 11584 870 -247 -1641 C ATOM 3441 C6 DT C 6 5.991 -6.796 59.141 1.00 95.11 C ANISOU 3441 C6 DT C 6 12805 11663 11668 789 -389 -1796 C TER 3442 DT C 6 ATOM 3443 OP3 DT D 5 24.349 9.644 9.916 1.00132.00 O ANISOU 3443 OP3 DT D 5 19943 16370 13838 -2649 -16 -2652 O ATOM 3444 P DT D 5 24.201 11.070 10.272 1.00132.73 P ANISOU 3444 P DT D 5 20048 16445 13940 -2652 -30 -2659 P ATOM 3445 OP1 DT D 5 23.619 11.752 9.097 1.00132.41 O ANISOU 3445 OP1 DT D 5 20037 16383 13891 -2646 -32 -2650 O ATOM 3446 OP2 DT D 5 25.500 11.520 10.815 1.00133.55 O ANISOU 3446 OP2 DT D 5 20137 16549 14055 -2672 -24 -2660 O ATOM 3447 O5' DT D 5 23.141 11.187 11.460 1.00 90.44 O ANISOU 3447 O5' DT D 5 14683 11097 8582 -2637 -48 -2678 O ATOM 3448 C5' DT D 5 23.514 11.756 12.711 1.00 91.23 C ANISOU 3448 C5' DT D 5 14772 11199 8693 -2645 -56 -2690 C ATOM 3449 C4' DT D 5 22.260 12.222 13.424 1.00 90.58 C ANISOU 3449 C4' DT D 5 14693 11115 8609 -2630 -72 -2709 C ATOM 3450 O4' DT D 5 21.310 11.133 13.442 1.00 89.11 O ANISOU 3450 O4' DT D 5 14499 10948 8410 -2618 -72 -2716 O ATOM 3451 C3' DT D 5 22.442 12.645 14.876 1.00 89.66 C ANISOU 3451 C3' DT D 5 14563 11003 8500 -2638 -81 -2725 C ATOM 3452 O3' DT D 5 22.496 14.066 14.936 1.00 88.70 O ANISOU 3452 O3' DT D 5 14458 10857 8388 -2643 -86 -2730 O ATOM 3453 C2' DT D 5 21.211 12.092 15.600 1.00 89.88 C ANISOU 3453 C2' DT D 5 14584 11046 8519 -2624 -88 -2743 C ATOM 3454 C1' DT D 5 20.438 11.315 14.533 1.00 89.99 C ANISOU 3454 C1' DT D 5 14604 11068 8521 -2612 -83 -2738 C ATOM 3455 N1 DT D 5 19.973 9.968 14.972 1.00 89.75 N ANISOU 3455 N1 DT D 5 14563 11060 8477 -2612 -74 -2747 N ATOM 3456 C2 DT D 5 18.629 9.762 15.201 1.00 91.30 C ANISOU 3456 C2 DT D 5 14756 11270 8663 -2604 -78 -2770 C ATOM 3457 O2 DT D 5 17.788 10.634 15.066 1.00 92.00 O ANISOU 3457 O2 DT D 5 14846 11354 8754 -2591 -92 -2783 O ATOM 3458 N3 DT D 5 18.307 8.487 15.600 1.00 91.53 N ANISOU 3458 N3 DT D 5 14782 11316 8677 -2612 -64 -2778 N ATOM 3459 C4 DT D 5 19.174 7.423 15.785 1.00 90.13 C ANISOU 3459 C4 DT D 5 14610 11142 8494 -2620 -48 -2764 C ATOM 3460 O4 DT D 5 18.787 6.313 16.145 1.00 88.79 O ANISOU 3460 O4 DT D 5 14446 10982 8308 -2626 -33 -2772 O ATOM 3461 C5 DT D 5 20.563 7.711 15.525 1.00 89.28 C ANISOU 3461 C5 DT D 5 14501 11023 8399 -2621 -49 -2740 C ATOM 3462 C7 DT D 5 21.597 6.637 15.690 1.00 88.37 C ANISOU 3462 C7 DT D 5 14386 10912 8277 -2621 -35 -2724 C ATOM 3463 C6 DT D 5 20.893 8.951 15.135 1.00 89.01 C ANISOU 3463 C6 DT D 5 14465 10974 8379 -2620 -61 -2734 C TER 3464 DT D 5 HETATM 3465 O HOH A 301 14.258 0.654 6.924 1.00 17.50 O HETATM 3466 O HOH A 302 28.220 -4.736 1.242 1.00 16.16 O HETATM 3467 O HOH A 303 18.956 -3.398 1.529 1.00 15.23 O HETATM 3468 O HOH A 304 11.292 -0.042 0.031 1.00 21.69 O HETATM 3469 O HOH A 305 23.415 4.675 17.009 1.00 18.90 O HETATM 3470 O HOH A 306 12.733 2.977 7.014 1.00 17.53 O HETATM 3471 O HOH A 307 19.628 2.731 21.570 1.00 20.15 O HETATM 3472 O HOH A 308 31.233 -4.174 17.289 1.00 22.16 O HETATM 3473 O HOH A 309 9.174 -6.975 -0.255 1.00 23.13 O HETATM 3474 O HOH A 310 30.072 3.697 15.283 1.00 22.87 O HETATM 3475 O HOH A 311 -2.393 -5.443 11.005 1.00 25.96 O HETATM 3476 O HOH A 312 5.973 -15.117 21.083 1.00 28.57 O HETATM 3477 O HOH A 313 22.784 3.182 -6.260 1.00 20.09 O HETATM 3478 O HOH A 314 5.800 -17.954 -3.556 1.00 26.02 O HETATM 3479 O HOH A 315 25.080 -12.597 4.133 1.00 31.28 O HETATM 3480 O HOH A 316 11.075 10.225 7.171 1.00 33.91 O HETATM 3481 O HOH A 317 13.553 -9.023 -5.179 1.00 34.99 O HETATM 3482 O HOH A 318 18.253 2.342 -2.618 1.00 26.58 O HETATM 3483 O HOH A 319 7.095 -6.456 -1.945 1.00 29.96 O HETATM 3484 O HOH A 320 16.523 -17.152 14.398 1.00 30.31 O HETATM 3485 O HOH A 321 23.110 -1.437 9.848 1.00 25.83 O HETATM 3486 O HOH A 322 26.250 -6.071 0.421 1.00 21.41 O HETATM 3487 O HOH A 323 -2.741 -0.467 15.983 1.00 26.01 O HETATM 3488 O HOH A 324 19.207 5.376 34.707 1.00 32.51 O HETATM 3489 O HOH A 325 22.060 -2.228 7.256 1.00 31.00 O HETATM 3490 O HOH A 326 20.967 9.908 23.087 1.00 34.18 O HETATM 3491 O HOH A 327 25.596 -4.810 22.645 1.00 30.00 O HETATM 3492 O HOH A 328 0.449 -3.402 13.800 1.00 29.17 O HETATM 3493 O HOH A 329 3.791 5.759 7.640 1.00 32.78 O HETATM 3494 O HOH A 330 13.982 2.762 16.763 1.00 33.04 O HETATM 3495 O HOH A 331 11.163 3.435 17.089 1.00 24.87 O HETATM 3496 O HOH A 332 25.039 6.770 -1.934 1.00 32.00 O HETATM 3497 O HOH A 333 10.006 -14.207 2.430 1.00 35.60 O HETATM 3498 O HOH A 334 10.739 5.823 33.962 1.00 34.26 O HETATM 3499 O HOH A 335 8.308 -16.527 1.199 1.00 37.66 O HETATM 3500 O HOH A 336 25.549 -5.776 -2.131 1.00 37.58 O HETATM 3501 O HOH A 337 -4.589 5.122 14.681 1.00 40.47 O HETATM 3502 O HOH A 338 21.310 1.575 13.257 1.00 23.86 O HETATM 3503 O HOH A 339 4.722 -12.176 7.526 1.00 43.27 O HETATM 3504 O HOH A 340 3.084 -10.431 16.601 1.00 31.90 O HETATM 3505 O HOH A 341 9.922 6.588 37.607 1.00 28.30 O HETATM 3506 O HOH A 342 15.354 5.696 20.013 1.00 53.57 O HETATM 3507 O HOH A 343 4.798 -10.357 10.242 1.00 40.78 O HETATM 3508 O HOH A 344 15.172 1.416 -2.314 1.00 27.95 O HETATM 3509 O HOH A 345 29.058 -5.181 18.398 1.00 27.56 O HETATM 3510 O HOH A 346 21.548 -14.340 2.854 1.00 30.24 O HETATM 3511 O HOH A 347 27.986 -3.510 20.338 1.00 39.51 O HETATM 3512 O HOH A 348 7.963 14.530 34.368 1.00 40.61 O HETATM 3513 O HOH A 349 17.447 11.666 20.202 1.00 44.98 O HETATM 3514 O HOH A 350 7.963 -13.027 3.602 1.00 28.66 O HETATM 3515 O HOH A 351 22.245 -14.875 7.149 1.00 27.97 O HETATM 3516 O HOH A 352 10.185 13.933 33.445 1.00 38.68 O HETATM 3517 O HOH A 353 0.074 2.727 24.209 1.00 33.72 O HETATM 3518 O HOH A 354 26.582 0.618 22.741 1.00 27.33 O HETATM 3519 O HOH A 355 0.159 -6.003 14.687 1.00 30.94 O HETATM 3520 O HOH A 356 1.713 6.932 36.328 1.00 43.69 O HETATM 3521 O HOH A 357 2.928 -12.308 13.176 1.00 35.65 O HETATM 3522 O HOH A 358 33.672 -5.293 18.140 1.00 33.40 O HETATM 3523 O HOH A 359 29.990 -8.294 7.745 1.00 56.48 O HETATM 3524 O HOH A 360 12.616 6.846 4.251 1.00 37.75 O HETATM 3525 O HOH A 361 -0.722 -4.562 20.680 1.00 38.20 O HETATM 3526 O HOH A 362 32.333 -9.898 13.296 1.00 36.57 O HETATM 3527 O HOH A 363 3.030 -8.952 10.958 1.00 32.68 O HETATM 3528 O HOH A 364 15.825 15.327 28.942 1.00 46.25 O HETATM 3529 O HOH A 365 12.775 -19.217 13.118 1.00 37.33 O HETATM 3530 O HOH A 366 3.306 -8.975 13.583 1.00 30.33 O HETATM 3531 O HOH A 367 2.753 -7.694 0.348 1.00 36.48 O HETATM 3532 O HOH A 368 23.709 2.903 37.300 1.00 36.36 O HETATM 3533 O HOH A 369 25.792 -2.213 -3.210 1.00 46.45 O HETATM 3534 O HOH A 370 35.889 -2.885 15.739 1.00 32.09 O HETATM 3535 O HOH A 371 -6.996 5.777 19.885 1.00 50.02 O HETATM 3536 O HOH A 372 13.018 12.469 35.832 1.00 37.63 O HETATM 3537 O HOH A 373 2.841 -14.065 10.623 1.00 36.27 O HETATM 3538 O HOH A 374 12.301 -8.015 38.421 1.00 49.64 O HETATM 3539 O HOH A 375 25.616 -6.800 26.690 1.00 42.95 O HETATM 3540 O HOH A 376 20.429 -7.603 37.587 1.00 40.15 O HETATM 3541 O HOH A 377 15.217 1.272 -5.129 1.00 34.22 O HETATM 3542 O HOH A 378 16.770 13.028 31.165 1.00 45.30 O HETATM 3543 O HOH A 379 6.928 -11.291 5.796 1.00 34.12 O HETATM 3544 O HOH A 380 12.277 -0.068 -2.775 1.00 36.24 O HETATM 3545 O HOH A 381 0.487 -5.381 27.638 1.00 40.19 O HETATM 3546 O HOH A 382 2.895 -7.002 15.386 1.00 30.62 O HETATM 3547 O HOH A 383 21.367 -8.265 -3.345 1.00 47.97 O HETATM 3548 O HOH A 384 5.048 7.905 6.461 1.00 41.17 O HETATM 3549 O HOH A 385 3.070 -7.596 31.475 1.00 36.51 O HETATM 3550 O HOH A 386 13.732 -6.552 -6.168 1.00 42.85 O HETATM 3551 O HOH A 387 -2.592 -2.601 19.553 1.00 47.69 O HETATM 3552 O HOH A 388 29.729 -15.856 10.728 1.00 46.62 O HETATM 3553 O HOH A 389 -1.085 -7.571 12.839 1.00 44.31 O HETATM 3554 O HOH A 390 25.171 -13.196 6.654 1.00 46.17 O HETATM 3555 O HOH A 391 3.712 -4.239 -2.079 1.00 40.46 O HETATM 3556 O HOH A 392 -2.198 11.264 27.557 1.00 40.07 O HETATM 3557 O HOH A 393 24.002 -3.859 -3.011 1.00 40.60 O HETATM 3558 O HOH A 394 10.491 -16.948 17.187 1.00 44.69 O HETATM 3559 O HOH A 395 1.468 -15.648 10.035 1.00 39.38 O HETATM 3560 O HOH A 396 27.938 -4.295 22.347 1.00 45.93 O HETATM 3561 O HOH A 397 -0.226 -7.097 25.854 1.00 36.92 O HETATM 3562 O HOH A 398 16.136 16.919 30.896 1.00 44.49 O HETATM 3563 O HOH A 399 25.584 6.166 16.114 1.00 35.50 O HETATM 3564 O HOH A 400 14.702 -4.343 -5.696 1.00 50.07 O HETATM 3565 O HOH A 401 8.683 2.392 0.950 1.00 32.96 O HETATM 3566 O HOH A 402 -1.178 -3.700 28.527 1.00 51.02 O HETATM 3567 O HOH A 403 3.108 -2.091 36.498 1.00 46.45 O HETATM 3568 O HOH A 404 26.593 -4.999 26.288 1.00 58.09 O HETATM 3569 O HOH A 405 3.464 10.653 24.311 1.00 46.17 O HETATM 3570 O HOH A 406 5.475 -18.135 7.095 1.00 40.63 O HETATM 3571 O HOH A 407 29.994 -4.226 -0.622 1.00 28.59 O HETATM 3572 O HOH A 408 11.332 -8.514 -6.771 1.00 37.08 O HETATM 3573 O HOH A 409 16.007 -18.853 16.240 1.00 48.54 O HETATM 3574 O HOH A 410 2.568 -6.271 33.763 1.00 59.97 O HETATM 3575 O HOH A 411 26.645 1.628 42.120 1.00 50.93 O HETATM 3576 O HOH A 412 23.478 -8.882 -1.825 1.00 32.38 O HETATM 3577 O HOH A 413 12.919 -20.106 34.034 1.00 49.76 O HETATM 3578 O HOH A 414 8.072 -14.421 6.824 1.00 30.66 O HETATM 3579 O HOH A 415 25.188 -4.458 32.741 1.00 35.25 O HETATM 3580 O HOH A 416 17.744 -7.162 36.249 1.00 32.05 O HETATM 3581 O HOH A 417 -5.684 -1.807 20.367 1.00 42.74 O HETATM 3582 O HOH A 418 7.011 14.685 16.689 1.00 44.01 O HETATM 3583 O HOH A 419 1.499 13.656 26.144 1.00 48.88 O HETATM 3584 O HOH A 420 25.382 -2.554 34.132 1.00 37.61 O HETATM 3585 O HOH A 421 25.636 -15.193 17.598 1.00 46.48 O HETATM 3586 O HOH A 422 17.410 18.417 32.463 1.00 51.52 O HETATM 3587 O HOH A 423 16.807 2.888 17.661 1.00 34.60 O HETATM 3588 O HOH A 424 -3.369 4.644 23.417 1.00 38.26 O HETATM 3589 O HOH A 425 12.224 -18.411 32.666 1.00 53.29 O HETATM 3590 O HOH A 426 3.807 -15.212 -2.085 1.00 40.79 O HETATM 3591 O HOH A 427 5.977 10.299 16.307 1.00 51.17 O HETATM 3592 O HOH A 428 20.809 3.531 14.319 1.00 43.23 O HETATM 3593 O HOH A 429 24.430 -6.506 33.712 1.00 43.92 O HETATM 3594 O HOH A 430 21.970 3.935 45.453 1.00 45.50 O HETATM 3595 O HOH A 431 28.264 -0.535 20.998 1.00 33.91 O HETATM 3596 O HOH A 432 28.043 -0.257 37.819 1.00 48.04 O HETATM 3597 O HOH A 433 -4.736 5.884 12.062 1.00 48.57 O HETATM 3598 O HOH A 434 1.635 -17.880 11.530 1.00 49.12 O HETATM 3599 O HOH A 435 28.994 -0.330 35.545 1.00 49.28 O HETATM 3600 O HOH A 436 22.121 1.929 46.896 1.00 57.61 O HETATM 3601 O HOH A 437 1.451 -0.430 0.187 1.00 42.60 O HETATM 3602 O HOH A 438 21.975 -8.150 34.036 1.00 28.10 O HETATM 3603 O HOH A 439 2.141 -4.878 0.147 1.00 40.86 O HETATM 3604 O HOH A 440 2.664 -2.851 1.452 1.00 43.69 O HETATM 3605 O HOH A 441 7.795 17.938 18.510 1.00 45.74 O HETATM 3606 O HOH A 442 27.726 -0.587 33.080 1.00 40.43 O HETATM 3607 O HOH A 443 10.026 -2.949 42.102 1.00 43.44 O HETATM 3608 O HOH A 444 10.067 19.062 16.745 1.00 40.68 O HETATM 3609 O HOH A 445 1.370 4.599 34.414 1.00 46.98 O HETATM 3610 O HOH A 446 11.289 -18.531 15.154 1.00 46.45 O HETATM 3611 O HOH A 447 20.942 9.014 40.456 1.00 45.98 O HETATM 3612 O HOH A 448 2.433 3.298 35.545 1.00 40.77 O HETATM 3613 O HOH A 449 -2.762 2.207 24.437 1.00 43.70 O HETATM 3614 O HOH A 450 31.360 -7.702 11.750 1.00 41.71 O HETATM 3615 O HOH A 451 15.856 3.376 -1.717 1.00 45.98 O HETATM 3616 O HOH A 452 22.957 -16.168 17.962 1.00 47.57 O HETATM 3617 O HOH A 453 7.437 17.152 31.110 1.00 49.05 O HETATM 3618 O HOH A 454 16.684 -13.167 36.270 1.00 44.83 O HETATM 3619 O HOH A 455 16.377 -14.328 3.616 1.00 36.78 O HETATM 3620 O HOH A 456 15.796 -9.047 37.631 1.00 34.42 O HETATM 3621 O HOH A 457 18.956 -13.981 3.917 1.00 40.50 O HETATM 3622 O HOH A 458 0.459 2.189 27.246 1.00 41.12 O HETATM 3623 O HOH A 459 11.778 -12.754 39.797 1.00 44.47 O HETATM 3624 O HOH A 460 11.418 19.643 19.095 1.00 44.38 O HETATM 3625 O HOH A 461 22.109 -18.521 17.431 1.00 52.47 O HETATM 3626 O HOH A 462 4.361 -4.257 34.735 1.00 44.30 O HETATM 3627 O HOH A 463 18.116 16.350 33.958 1.00 54.57 O HETATM 3628 O HOH A 464 0.378 -11.022 20.277 1.00 46.53 O HETATM 3629 O HOH A 465 8.551 18.957 31.216 1.00 41.71 O HETATM 3630 O HOH A 466 0.533 -6.772 29.955 1.00 43.06 O HETATM 3631 O HOH A 467 21.167 -19.641 16.269 1.00 39.27 O HETATM 3632 O HOH A 468 15.843 -11.426 37.622 1.00 59.13 O HETATM 3633 O HOH A 469 -3.227 -1.012 4.691 1.00 25.69 O HETATM 3634 O HOH A 470 27.690 3.456 23.360 1.00 39.07 O HETATM 3635 O HOH A 471 -1.068 -8.652 -0.013 1.00 40.94 O HETATM 3636 O HOH A 472 8.581 -16.961 5.176 1.00 62.95 O HETATM 3637 O HOH A 473 3.341 -18.857 -3.874 1.00 40.62 O HETATM 3638 O HOH A 474 15.641 18.035 11.277 1.00 48.04 O HETATM 3639 O HOH A 475 2.037 -11.332 4.903 1.00 43.33 O HETATM 3640 O HOH A 476 1.820 15.686 37.856 1.00 54.30 O HETATM 3641 O HOH A 477 0.369 -7.404 1.664 1.00 54.74 O HETATM 3642 O HOH A 478 16.383 15.224 23.576 1.00 48.25 O HETATM 3643 O HOH A 479 7.007 -19.583 10.959 1.00 42.60 O HETATM 3644 O HOH A 480 6.063 11.426 23.707 1.00 50.49 O HETATM 3645 O HOH A 481 16.539 8.557 22.162 1.00 58.10 O HETATM 3646 O HOH A 482 8.138 -20.729 3.304 1.00 49.41 O HETATM 3647 O HOH A 483 33.183 3.406 9.810 1.00 46.19 O HETATM 3648 O HOH A 484 0.072 -6.099 4.145 1.00 56.52 O HETATM 3649 O HOH A 485 2.440 6.978 10.994 1.00 51.08 O HETATM 3650 O HOH A 486 4.779 -20.108 5.839 1.00 45.83 O HETATM 3651 O HOH A 487 25.678 7.795 34.378 1.00 43.21 O HETATM 3652 O HOH A 488 28.059 -12.255 4.306 1.00 47.17 O HETATM 3653 O HOH A 489 17.842 7.851 20.929 1.00 59.74 O HETATM 3654 O HOH A 490 3.029 -18.361 14.991 1.00 48.41 O HETATM 3655 O HOH A 491 26.751 -9.897 -1.586 1.00 54.99 O HETATM 3656 O HOH A 492 24.720 6.128 36.468 1.00 50.06 O HETATM 3657 O HOH A 493 25.897 8.820 8.391 1.00 45.06 O HETATM 3658 O HOH B 301 13.128 8.162 59.115 1.00 16.22 O HETATM 3659 O HOH B 302 5.313 12.993 77.640 1.00 16.97 O HETATM 3660 O HOH B 303 2.985 9.356 71.009 1.00 18.33 O HETATM 3661 O HOH B 304 -6.415 3.250 63.779 1.00 34.49 O HETATM 3662 O HOH B 305 13.822 14.196 81.477 1.00 21.26 O HETATM 3663 O HOH B 306 10.090 24.897 74.328 1.00 26.11 O HETATM 3664 O HOH B 307 11.270 6.790 65.945 1.00 24.46 O HETATM 3665 O HOH B 308 11.763 9.183 67.488 1.00 23.73 O HETATM 3666 O HOH B 309 11.560 15.893 81.453 1.00 25.64 O HETATM 3667 O HOH B 310 12.035 11.931 71.603 1.00 28.99 O HETATM 3668 O HOH B 311 -0.148 3.458 72.680 1.00 23.95 O HETATM 3669 O HOH B 312 11.981 22.398 77.842 1.00 28.87 O HETATM 3670 O HOH B 313 1.611 7.028 70.395 1.00 24.64 O HETATM 3671 O HOH B 314 -9.226 27.648 73.064 1.00 26.44 O HETATM 3672 O HOH B 315 -14.914 14.893 68.017 1.00 30.59 O HETATM 3673 O HOH B 316 -6.386 4.034 66.886 1.00 31.14 O HETATM 3674 O HOH B 317 -6.368 28.412 74.751 1.00 25.65 O HETATM 3675 O HOH B 318 16.631 4.714 43.408 1.00 38.69 O HETATM 3676 O HOH B 319 -4.971 26.156 77.485 1.00 32.93 O HETATM 3677 O HOH B 320 -4.697 16.588 75.712 1.00 24.68 O HETATM 3678 O HOH B 321 0.297 -0.446 69.017 1.00 27.88 O HETATM 3679 O HOH B 322 15.424 5.942 64.400 1.00 25.31 O HETATM 3680 O HOH B 323 4.752 -3.606 72.255 1.00 33.49 O HETATM 3681 O HOH B 324 6.961 24.532 75.635 1.00 31.73 O HETATM 3682 O HOH B 325 10.459 0.944 60.618 1.00 31.03 O HETATM 3683 O HOH B 326 -5.207 19.096 79.117 1.00 35.13 O HETATM 3684 O HOH B 327 13.422 -1.958 49.071 1.00 45.04 O HETATM 3685 O HOH B 328 -0.060 25.956 55.497 1.00 36.26 O HETATM 3686 O HOH B 329 8.744 25.983 70.062 1.00 33.37 O HETATM 3687 O HOH B 330 12.775 24.997 85.547 1.00 39.66 O HETATM 3688 O HOH B 331 20.053 10.459 60.324 1.00 32.80 O HETATM 3689 O HOH B 332 20.605 15.830 65.884 1.00 23.69 O HETATM 3690 O HOH B 333 9.608 4.524 40.931 1.00 30.62 O HETATM 3691 O HOH B 334 19.205 19.171 48.548 1.00 34.70 O HETATM 3692 O HOH B 335 21.768 6.589 54.807 1.00 32.39 O HETATM 3693 O HOH B 336 -9.830 12.083 72.673 1.00 33.15 O HETATM 3694 O HOH B 337 -2.157 10.248 45.635 1.00 43.72 O HETATM 3695 O HOH B 338 11.646 1.485 55.156 1.00 27.67 O HETATM 3696 O HOH B 339 -1.389 2.146 64.731 1.00 33.80 O HETATM 3697 O HOH B 340 2.586 12.739 86.966 1.00 37.43 O HETATM 3698 O HOH B 341 5.289 7.685 61.103 1.00 46.10 O HETATM 3699 O HOH B 342 13.193 22.965 75.673 1.00 35.13 O HETATM 3700 O HOH B 343 -2.063 9.581 79.434 1.00 35.65 O HETATM 3701 O HOH B 344 17.032 5.722 46.629 1.00 40.70 O HETATM 3702 O HOH B 345 17.664 7.179 80.376 1.00 33.66 O HETATM 3703 O HOH B 346 -13.819 3.400 67.735 1.00 29.50 O HETATM 3704 O HOH B 347 22.106 7.673 45.631 1.00 29.66 O HETATM 3705 O HOH B 348 17.009 20.343 78.106 1.00 41.94 O HETATM 3706 O HOH B 349 12.236 -4.218 50.892 1.00 38.59 O HETATM 3707 O HOH B 350 7.552 29.454 63.802 1.00 41.53 O HETATM 3708 O HOH B 351 -12.918 12.182 51.060 1.00 37.81 O HETATM 3709 O HOH B 352 12.081 -0.353 75.848 1.00 43.58 O HETATM 3710 O HOH B 353 23.724 7.616 70.836 1.00 37.58 O HETATM 3711 O HOH B 354 7.721 23.683 77.816 1.00 41.69 O HETATM 3712 O HOH B 355 -1.903 1.003 67.397 1.00 36.06 O HETATM 3713 O HOH B 356 -4.491 20.843 58.683 1.00 45.58 O HETATM 3714 O HOH B 357 8.105 -2.806 44.232 1.00 43.28 O HETATM 3715 O HOH B 358 7.480 25.342 80.053 1.00 33.17 O HETATM 3716 O HOH B 359 -2.457 12.862 82.813 1.00 50.45 O HETATM 3717 O HOH B 360 3.901 23.644 74.844 1.00 38.07 O HETATM 3718 O HOH B 361 0.143 10.054 86.495 1.00 37.51 O HETATM 3719 O HOH B 362 -6.932 19.531 64.014 1.00 27.03 O HETATM 3720 O HOH B 363 14.434 21.864 78.726 1.00 38.99 O HETATM 3721 O HOH B 364 22.769 4.892 69.280 1.00 38.72 O HETATM 3722 O HOH B 365 20.165 11.331 80.708 1.00 38.92 O HETATM 3723 O HOH B 366 23.370 18.543 73.064 1.00 37.28 O HETATM 3724 O HOH B 367 -4.159 6.759 74.414 1.00 42.90 O HETATM 3725 O HOH B 368 7.140 27.368 65.267 1.00 39.25 O HETATM 3726 O HOH B 369 15.951 7.187 75.260 1.00 49.21 O HETATM 3727 O HOH B 370 18.305 5.957 71.097 1.00 41.02 O HETATM 3728 O HOH B 371 -3.516 24.477 69.263 1.00 38.83 O HETATM 3729 O HOH B 372 -5.856 22.950 61.380 1.00 48.57 O HETATM 3730 O HOH B 373 -3.131 23.648 74.428 1.00 43.48 O HETATM 3731 O HOH B 374 1.187 4.189 39.559 1.00 44.97 O HETATM 3732 O HOH B 375 -2.731 2.211 69.278 1.00 44.92 O HETATM 3733 O HOH B 376 -10.268 16.600 73.864 1.00 37.35 O HETATM 3734 O HOH B 377 1.994 -4.253 37.552 1.00 41.32 O HETATM 3735 O HOH B 378 1.993 0.173 72.925 1.00 30.52 O HETATM 3736 O HOH B 379 -7.878 13.903 60.276 1.00 32.14 O HETATM 3737 O HOH B 380 14.383 13.067 83.761 1.00 41.03 O HETATM 3738 O HOH B 381 1.117 1.285 74.604 1.00 51.78 O HETATM 3739 O HOH B 382 -2.519 3.324 71.378 1.00 41.77 O HETATM 3740 O HOH B 383 10.851 13.294 36.549 1.00 33.61 O HETATM 3741 O HOH B 384 10.267 12.480 73.385 1.00 38.53 O HETATM 3742 O HOH B 385 16.341 18.833 45.106 1.00 43.02 O HETATM 3743 O HOH B 386 -6.269 15.304 53.339 1.00 40.22 O HETATM 3744 O HOH B 387 8.087 5.233 39.133 1.00 42.24 O HETATM 3745 O HOH B 388 11.723 30.050 69.218 1.00 48.24 O HETATM 3746 O HOH B 389 13.338 0.264 56.250 1.00 40.56 O HETATM 3747 O HOH B 390 -0.305 8.674 82.609 1.00 42.33 O HETATM 3748 O HOH B 391 -1.436 3.560 38.328 1.00 50.45 O HETATM 3749 O HOH B 392 14.280 1.443 50.936 1.00 44.39 O HETATM 3750 O HOH B 393 11.223 2.854 59.383 1.00 56.43 O HETATM 3751 O HOH B 394 4.982 22.887 77.290 1.00 45.14 O HETATM 3752 O HOH B 395 7.986 -8.318 50.661 1.00 50.92 O HETATM 3753 O HOH B 396 -1.482 15.492 82.955 1.00 43.06 O HETATM 3754 O HOH B 397 -4.586 20.357 64.539 1.00 42.39 O HETATM 3755 O HOH B 398 10.086 1.980 57.490 1.00 52.32 O HETATM 3756 O HOH B 399 18.903 16.026 60.379 1.00 43.01 O HETATM 3757 O HOH B 400 9.050 4.840 44.616 1.00 45.46 O HETATM 3758 O HOH B 401 17.003 0.018 59.115 1.00 41.76 O HETATM 3759 O HOH B 402 17.339 5.361 74.237 1.00 43.64 O HETATM 3760 O HOH B 403 20.230 14.604 63.215 1.00 41.32 O HETATM 3761 O HOH B 404 -3.232 27.145 75.824 1.00 37.83 O HETATM 3762 O HOH B 405 11.863 25.966 87.905 1.00 49.13 O HETATM 3763 O HOH B 406 25.113 -0.534 42.804 1.00 44.23 O HETATM 3764 O HOH B 407 -2.321 25.989 51.739 1.00 52.55 O HETATM 3765 O HOH B 408 0.987 6.808 40.454 1.00 47.78 O HETATM 3766 O HOH B 409 -5.337 2.362 68.283 1.00 44.49 O HETATM 3767 O HOH B 410 -4.327 24.484 79.297 1.00 46.01 O HETATM 3768 O HOH B 411 -2.669 9.800 76.453 1.00 24.30 O HETATM 3769 O HOH B 412 7.821 0.786 77.392 1.00 39.45 O HETATM 3770 O HOH B 413 -4.487 8.530 76.165 1.00 37.22 O HETATM 3771 O HOH B 414 -6.171 4.734 74.502 1.00 43.04 O HETATM 3772 O HOH B 415 8.393 30.216 68.713 1.00 45.98 O HETATM 3773 O HOH B 416 17.772 17.908 75.919 1.00 39.83 O HETATM 3774 O HOH B 417 20.035 22.437 62.637 1.00 62.12 O HETATM 3775 O HOH B 418 18.526 -2.110 40.244 1.00 34.13 O HETATM 3776 O HOH B 419 9.353 6.232 59.852 1.00 59.26 O HETATM 3777 O HOH B 420 -3.215 8.226 47.260 1.00 51.72 O HETATM 3778 O HOH B 421 1.234 15.446 83.622 1.00 32.76 O HETATM 3779 O HOH B 422 -11.782 14.492 62.127 1.00 50.30 O HETATM 3780 O HOH B 423 5.646 23.764 79.346 1.00 57.32 O HETATM 3781 O HOH B 424 18.508 30.769 50.029 1.00 48.40 O HETATM 3782 O HOH B 425 -2.986 21.983 79.755 1.00 45.18 O HETATM 3783 O HOH B 426 20.716 12.258 62.681 1.00 44.92 O HETATM 3784 O HOH B 427 -11.654 8.515 57.830 1.00 41.69 O HETATM 3785 O HOH B 428 16.078 22.977 48.276 1.00 47.68 O HETATM 3786 O HOH B 429 -12.563 7.460 60.356 1.00 55.83 O HETATM 3787 O HOH B 430 9.599 2.464 80.206 1.00 33.78 O HETATM 3788 O HOH B 431 15.807 1.235 53.375 1.00 32.81 O HETATM 3789 O HOH B 432 3.656 29.568 65.060 1.00 42.65 O HETATM 3790 O HOH B 433 -6.967 6.883 50.060 1.00 41.96 O HETATM 3791 O HOH B 434 -9.057 27.285 48.203 1.00 47.72 O HETATM 3792 O HOH B 435 -5.522 21.533 71.323 1.00 43.71 O HETATM 3793 O HOH B 436 2.582 7.935 39.819 1.00 47.43 O HETATM 3794 O HOH B 437 -6.456 28.064 47.705 1.00 54.21 O HETATM 3795 O HOH B 438 21.253 30.885 49.509 1.00 42.27 O HETATM 3796 O HOH B 439 15.774 24.657 50.091 1.00 52.75 O HETATM 3797 O HOH B 440 -3.776 23.370 71.730 1.00 57.06 O HETATM 3798 O HOH B 441 11.832 -2.025 43.470 1.00 45.73 O HETATM 3799 O HOH B 442 -4.143 6.921 50.713 1.00 35.13 O HETATM 3800 O HOH B 443 -5.824 3.573 44.211 1.00 43.16 O HETATM 3801 O HOH B 444 -14.500 13.441 49.534 1.00 41.17 O HETATM 3802 O HOH B 445 20.557 14.008 81.917 1.00 53.66 O HETATM 3803 O HOH B 446 8.361 7.867 61.263 1.00 35.86 O HETATM 3804 O HOH B 447 18.183 13.281 41.105 1.00 36.30 O HETATM 3805 O HOH B 448 10.898 -8.333 52.971 1.00 41.44 O HETATM 3806 O HOH B 449 9.875 29.320 67.032 1.00 46.90 O HETATM 3807 O HOH B 450 -5.590 -0.057 54.674 1.00 48.72 O HETATM 3808 O HOH B 451 24.954 17.295 72.053 1.00 58.57 O HETATM 3809 O HOH B 452 11.584 10.011 83.841 1.00 33.12 O HETATM 3810 O HOH B 453 14.308 1.503 58.362 1.00 44.38 O HETATM 3811 O HOH B 454 8.457 5.950 62.081 1.00 44.80 O HETATM 3812 O HOH B 455 2.753 -2.647 74.190 1.00 36.21 O HETATM 3813 O HOH B 456 11.366 20.349 40.727 1.00 54.26 O HETATM 3814 O HOH B 457 20.514 21.552 70.049 1.00 35.81 O HETATM 3815 O HOH B 458 18.261 1.099 49.012 1.00 59.93 O HETATM 3816 O HOH B 459 -9.591 20.737 67.546 1.00 39.39 O HETATM 3817 O HOH B 460 20.503 18.299 56.523 1.00 39.97 O HETATM 3818 O HOH B 461 23.934 17.090 75.666 1.00 50.67 O HETATM 3819 O HOH B 462 11.397 30.486 65.563 1.00 44.82 O HETATM 3820 O HOH B 463 20.556 21.663 54.649 1.00 38.40 O HETATM 3821 O HOH B 464 11.411 4.009 82.150 1.00 53.98 O HETATM 3822 O HOH B 465 6.569 26.714 74.611 1.00 51.77 O HETATM 3823 O HOH B 466 2.187 28.556 57.894 1.00 39.64 O HETATM 3824 O HOH B 467 -0.317 29.703 74.628 1.00 39.34 O HETATM 3825 O HOH B 468 -1.528 30.842 64.778 1.00 53.44 O HETATM 3826 O HOH B 469 6.122 28.580 72.177 1.00 46.98 O HETATM 3827 O HOH B 470 -4.914 -0.337 61.895 1.00 41.41 O HETATM 3828 O HOH B 471 18.756 0.713 52.263 1.00 48.79 O HETATM 3829 O HOH B 472 18.895 -5.393 40.785 1.00 41.68 O HETATM 3830 O HOH B 473 -0.227 29.297 63.005 1.00 46.25 O HETATM 3831 O HOH B 474 19.213 17.936 44.030 1.00 49.42 O HETATM 3832 O HOH B 475 -0.450 27.287 76.089 1.00 44.10 O HETATM 3833 O HOH B 476 -4.846 1.782 64.124 1.00 58.02 O HETATM 3834 O HOH B 477 27.571 0.443 43.722 1.00 53.15 O HETATM 3835 O HOH C 101 25.887 2.919 72.553 1.00 37.29 O HETATM 3836 O HOH C 102 17.353 4.490 65.354 1.00 32.30 O HETATM 3837 O HOH C 103 17.498 -4.012 65.193 1.00 38.97 O HETATM 3838 O HOH C 104 16.109 -1.932 63.610 1.00 42.17 O HETATM 3839 O HOH C 105 27.328 0.742 71.383 1.00 38.38 O HETATM 3840 O HOH C 106 13.445 5.188 65.286 1.00 36.32 O HETATM 3841 O HOH C 107 27.999 -3.320 67.427 1.00 37.19 O HETATM 3842 O HOH C 108 26.834 -5.370 66.639 1.00 32.91 O HETATM 3843 O HOH C 109 18.691 1.241 60.382 1.00 44.92 O HETATM 3844 O HOH C 110 29.926 -8.393 60.369 1.00 44.37 O HETATM 3845 O HOH C 111 25.040 -7.518 60.897 1.00 38.07 O HETATM 3846 O HOH C 112 29.455 -6.431 61.667 1.00 43.52 O HETATM 3847 O HOH C 113 30.004 -3.221 68.651 1.00 43.24 O HETATM 3848 O HOH C 114 0.184 -6.181 56.212 1.00 55.50 O HETATM 3849 O HOH C 115 23.673 -10.754 64.869 1.00 54.25 O MASTER 679 0 0 20 18 0 0 6 3845 4 0 40 END
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Related entries of code: 4ljr
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Protein Sequence Similarity
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
4ljr
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
DNA processing protein A from Helicobacter pylori, HpDprA(5-225)
Ligand Name
35-bp single-stranded DNA
EC.Number
E.C.-.-.-.-
Resolution
1.8(Å)
Affinity (Kd/Ki/IC50)
Kd=30.6nM
Release Year
2014
Protein/NA Sequence
Check fasta file
Primary Reference
(2014) Nucleic Acids Res. Vol. 42: pp. 3478-3491
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):
O25100
Entrez Gene ID
No matched NCBI Entrez Gene ID found!
ASD
Information of known allosteric effects of PDB entries
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