Browse entries in the PDBbind-CN Database
HEADER RNA BINDING PROTEIN 17-APR-18 6GC5 TITLE MOLECULAR BASIS FOR AU-RICH ELEMENT RECOGNITION AND DIMERIZATION BY TITLE 2 THE HUR C-TERMINAL RRM COMPND MOL_ID: 1; COMPND 2 MOLECULE: ELAV-LIKE PROTEIN 1; COMPND 3 CHAIN: A, B, C, D; COMPND 4 SYNONYM: HU-ANTIGEN R,HUR; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: AU-RICH RNA; COMPND 8 CHAIN: E, F, G, H; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ELAVL1, HUR; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606 KEYWDS ELAV, HUR, RRM3, DIMER, RRM, RNA BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR N.RIPIN,F.H.ALLAIN REVDAT 3 27-FEB-19 6GC5 1 JRNL REVDAT 2 13-FEB-19 6GC5 1 JRNL REVDAT 1 30-JAN-19 6GC5 0 JRNL AUTH N.RIPIN,J.BOUDET,M.M.DUSZCZYK,A.HINNIGER,M.FALLER,M.KREPL, JRNL AUTH 2 A.GADI,R.J.SCHNEIDER,J.SPONER,N.C.MEISNER-KOBER,F.H.ALLAIN JRNL TITL MOLECULAR BASIS FOR AU-RICH ELEMENT RECOGNITION AND JRNL TITL 2 DIMERIZATION BY THE HUR C-TERMINAL RRM. JRNL REF PROC. NATL. ACAD. SCI. V. 116 2935 2019 JRNL REF 2 U.S.A. JRNL REFN ESSN 1091-6490 JRNL PMID 30718402 JRNL DOI 10.1073/PNAS.1808696116 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.95 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0 REMARK 3 NUMBER OF REFLECTIONS : 35638 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.202 REMARK 3 R VALUE (WORKING SET) : 0.201 REMARK 3 FREE R VALUE : 0.231 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1784 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 0.0000 - 4.4674 0.97 2791 147 0.2089 0.2240 REMARK 3 2 4.4674 - 3.5459 0.96 2661 141 0.1685 0.2070 REMARK 3 3 3.5459 - 3.0976 0.98 2691 141 0.1953 0.1989 REMARK 3 4 3.0976 - 2.8144 0.98 2706 143 0.2032 0.2172 REMARK 3 5 2.8144 - 2.6127 0.98 2676 140 0.1976 0.2615 REMARK 3 6 2.6127 - 2.4586 0.98 2683 142 0.1897 0.2515 REMARK 3 7 2.4586 - 2.3355 0.97 2666 140 0.1928 0.2315 REMARK 3 8 2.3355 - 2.2338 0.91 2449 130 0.2022 0.2544 REMARK 3 9 2.2338 - 2.1478 0.96 2620 138 0.2044 0.2723 REMARK 3 10 2.1478 - 2.0737 0.97 2651 139 0.2010 0.2634 REMARK 3 11 2.0737 - 2.0088 0.96 2564 135 0.2256 0.2506 REMARK 3 12 2.0088 - 1.9514 0.95 2625 139 0.2640 0.3140 REMARK 3 13 1.9514 - 1.9000 0.77 2071 109 0.4235 0.4698 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.20 REMARK 3 SHRINKAGE RADIUS : 0.95 REMARK 3 K_SOL : 0.34 REMARK 3 B_SOL : 53.92 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.990 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) : -9.77890 REMARK 3 B22 (A**2) : 17.02580 REMARK 3 B33 (A**2) : -7.24690 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 2.02320 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 : 0.015 2831 REMARK 3 ANGLE : 1.216 3753 REMARK 3 CHIRALITY : 0.090 434 REMARK 3 PLANARITY : 0.006 423 REMARK 3 DIHEDRAL : 12.004 959 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 23 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 243:275) REMARK 3 ORIGIN FOR THE GROUP (A): 219.9190 36.2599 39.8626 REMARK 3 T TENSOR REMARK 3 T11: 0.2854 T22: 0.2378 REMARK 3 T33: 0.3103 T12: -0.0352 REMARK 3 T13: -0.0142 T23: -0.0154 REMARK 3 L TENSOR REMARK 3 L11: 0.7553 L22: 0.4478 REMARK 3 L33: 0.4110 L12: 0.5576 REMARK 3 L13: 0.0719 L23: -0.0761 REMARK 3 S TENSOR REMARK 3 S11: 0.1506 S12: 0.0590 S13: -0.0754 REMARK 3 S21: -0.0071 S22: -0.0281 S23: -0.0775 REMARK 3 S31: 0.0026 S32: 0.0581 S33: -0.1246 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 276:286) REMARK 3 ORIGIN FOR THE GROUP (A): 235.0160 40.4375 41.0334 REMARK 3 T TENSOR REMARK 3 T11: 0.2963 T22: 0.3271 REMARK 3 T33: 0.4255 T12: -0.0802 REMARK 3 T13: 0.0276 T23: 0.0242 REMARK 3 L TENSOR REMARK 3 L11: 0.2147 L22: 2.2483 REMARK 3 L33: 1.2133 L12: 0.3112 REMARK 3 L13: -0.4608 L23: -1.1304 REMARK 3 S TENSOR REMARK 3 S11: 0.1439 S12: -0.0352 S13: 0.1544 REMARK 3 S21: -0.0653 S22: -0.2880 S23: -0.6403 REMARK 3 S31: -0.1570 S32: 0.2658 S33: 0.1339 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 287:305) REMARK 3 ORIGIN FOR THE GROUP (A): 211.6046 37.8384 43.0310 REMARK 3 T TENSOR REMARK 3 T11: 0.3063 T22: 0.2543 REMARK 3 T33: 0.3392 T12: 0.0056 REMARK 3 T13: 0.0318 T23: 0.0104 REMARK 3 L TENSOR REMARK 3 L11: 0.8014 L22: 0.6133 REMARK 3 L33: 1.6447 L12: -0.4768 REMARK 3 L13: 0.1788 L23: 0.1291 REMARK 3 S TENSOR REMARK 3 S11: 0.0779 S12: -0.0068 S13: 0.3359 REMARK 3 S21: -0.1188 S22: 0.0250 S23: 0.2838 REMARK 3 S31: -0.3029 S32: -0.4949 S33: -0.0724 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 306:321) REMARK 3 ORIGIN FOR THE GROUP (A): 219.5108 33.3919 49.0948 REMARK 3 T TENSOR REMARK 3 T11: 0.2703 T22: 0.1793 REMARK 3 T33: 0.3139 T12: -0.0006 REMARK 3 T13: 0.0172 T23: -0.0100 REMARK 3 L TENSOR REMARK 3 L11: 1.4078 L22: 0.1393 REMARK 3 L33: 2.0455 L12: 0.2890 REMARK 3 L13: -0.0462 L23: -0.4211 REMARK 3 S TENSOR REMARK 3 S11: 0.1634 S12: -0.2891 S13: -0.6688 REMARK 3 S21: 0.2089 S22: -0.2220 S23: -0.2035 REMARK 3 S31: 0.5195 S32: 0.3837 S33: 0.0644 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 243:256) REMARK 3 ORIGIN FOR THE GROUP (A): 216.2110 30.7612 18.4162 REMARK 3 T TENSOR REMARK 3 T11: 0.2602 T22: 0.5991 REMARK 3 T33: 0.2311 T12: 0.0240 REMARK 3 T13: -0.0368 T23: 0.0372 REMARK 3 L TENSOR REMARK 3 L11: 1.0419 L22: 0.5656 REMARK 3 L33: 0.9027 L12: 0.2842 REMARK 3 L13: -0.8888 L23: -0.3735 REMARK 3 S TENSOR REMARK 3 S11: 0.1779 S12: 0.7278 S13: 0.0272 REMARK 3 S21: -0.1162 S22: -0.2281 S23: -0.1285 REMARK 3 S31: 0.2579 S32: 0.4917 S33: -0.0327 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 257:267) REMARK 3 ORIGIN FOR THE GROUP (A): 215.7720 36.4257 26.3701 REMARK 3 T TENSOR REMARK 3 T11: 0.3736 T22: 0.4408 REMARK 3 T33: 0.2898 T12: -0.0521 REMARK 3 T13: -0.0163 T23: -0.0190 REMARK 3 L TENSOR REMARK 3 L11: 8.3479 L22: 1.4658 REMARK 3 L33: 1.7832 L12: -0.4347 REMARK 3 L13: -0.8401 L23: -0.6696 REMARK 3 S TENSOR REMARK 3 S11: 0.2875 S12: 0.9532 S13: 0.8850 REMARK 3 S21: -0.3980 S22: 0.0486 S23: -0.2285 REMARK 3 S31: -0.7179 S32: 0.5364 S33: -0.2188 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 268:286) REMARK 3 ORIGIN FOR THE GROUP (A): 220.9597 28.2290 22.1981 REMARK 3 T TENSOR REMARK 3 T11: 0.3180 T22: 0.8623 REMARK 3 T33: 0.2287 T12: 0.1668 REMARK 3 T13: -0.0068 T23: -0.0535 REMARK 3 L TENSOR REMARK 3 L11: 1.1749 L22: 0.4178 REMARK 3 L33: 0.4426 L12: 0.5953 REMARK 3 L13: -0.7223 L23: -0.3539 REMARK 3 S TENSOR REMARK 3 S11: 0.1790 S12: 0.4219 S13: 0.0439 REMARK 3 S21: -0.1298 S22: -0.0133 S23: -0.1844 REMARK 3 S31: 0.4316 S32: 1.0574 S33: 0.1057 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 287:294) REMARK 3 ORIGIN FOR THE GROUP (A): 212.1278 28.2858 24.1994 REMARK 3 T TENSOR REMARK 3 T11: 0.3273 T22: 0.4247 REMARK 3 T33: 0.2978 T12: 0.0212 REMARK 3 T13: -0.0153 T23: 0.0585 REMARK 3 L TENSOR REMARK 3 L11: 0.4881 L22: 0.2537 REMARK 3 L33: 1.6941 L12: 0.3339 REMARK 3 L13: 0.2573 L23: -0.0227 REMARK 3 S TENSOR REMARK 3 S11: 0.1222 S12: 0.1020 S13: -0.0875 REMARK 3 S21: -0.0950 S22: 0.1788 S23: 0.0636 REMARK 3 S31: 0.2794 S32: 0.2825 S33: -0.3760 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 295:305) REMARK 3 ORIGIN FOR THE GROUP (A): 204.0524 35.2285 23.0813 REMARK 3 T TENSOR REMARK 3 T11: 0.2887 T22: 0.3857 REMARK 3 T33: 0.2690 T12: -0.0241 REMARK 3 T13: -0.0753 T23: 0.0015 REMARK 3 L TENSOR REMARK 3 L11: 2.4721 L22: 4.6454 REMARK 3 L33: 1.4334 L12: 1.1489 REMARK 3 L13: -1.4270 L23: 0.9062 REMARK 3 S TENSOR REMARK 3 S11: -0.0124 S12: -0.2249 S13: -0.2628 REMARK 3 S21: 0.6014 S22: -0.2208 S23: 0.2484 REMARK 3 S31: 0.1034 S32: -0.7397 S33: 0.1076 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 306:322) REMARK 3 ORIGIN FOR THE GROUP (A): 212.6023 34.4067 14.8296 REMARK 3 T TENSOR REMARK 3 T11: 0.3384 T22: 0.5693 REMARK 3 T33: 0.2767 T12: -0.0334 REMARK 3 T13: -0.0801 T23: 0.0695 REMARK 3 L TENSOR REMARK 3 L11: 2.3029 L22: 0.1830 REMARK 3 L33: 1.3362 L12: 0.1906 REMARK 3 L13: -0.3540 L23: 0.0247 REMARK 3 S TENSOR REMARK 3 S11: 0.1960 S12: 0.7739 S13: 0.3591 REMARK 3 S21: -0.0965 S22: 0.1007 S23: 0.2202 REMARK 3 S31: 0.3335 S32: 0.3650 S33: -0.1810 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 243:256) REMARK 3 ORIGIN FOR THE GROUP (A): 195.2095 38.1126 5.2872 REMARK 3 T TENSOR REMARK 3 T11: 0.3183 T22: 0.4313 REMARK 3 T33: 0.2985 T12: -0.0184 REMARK 3 T13: -0.0000 T23: 0.0307 REMARK 3 L TENSOR REMARK 3 L11: 1.1854 L22: 1.2829 REMARK 3 L33: 0.2141 L12: -0.3766 REMARK 3 L13: -0.1473 L23: -0.4365 REMARK 3 S TENSOR REMARK 3 S11: 0.3627 S12: 0.3126 S13: 0.0056 REMARK 3 S21: -0.3240 S22: -0.1986 S23: -0.1102 REMARK 3 S31: -0.2376 S32: -0.2966 S33: -0.2303 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 257:267) REMARK 3 ORIGIN FOR THE GROUP (A): 188.7954 33.4322 10.6968 REMARK 3 T TENSOR REMARK 3 T11: 0.3466 T22: 0.3543 REMARK 3 T33: 0.3365 T12: -0.0493 REMARK 3 T13: 0.0143 T23: -0.0273 REMARK 3 L TENSOR REMARK 3 L11: 2.1554 L22: 1.5770 REMARK 3 L33: 1.8845 L12: 1.0436 REMARK 3 L13: -0.8618 L23: 0.8107 REMARK 3 S TENSOR REMARK 3 S11: -0.1397 S12: 0.3405 S13: -0.2924 REMARK 3 S21: -0.2203 S22: -0.0552 S23: -0.1784 REMARK 3 S31: 0.3970 S32: -0.1340 S33: 0.1217 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 268:275) REMARK 3 ORIGIN FOR THE GROUP (A): 187.6721 40.9462 11.0902 REMARK 3 T TENSOR REMARK 3 T11: 0.3051 T22: 0.3556 REMARK 3 T33: 0.3280 T12: 0.0608 REMARK 3 T13: -0.0065 T23: 0.0432 REMARK 3 L TENSOR REMARK 3 L11: 1.8252 L22: 4.3359 REMARK 3 L33: 1.9673 L12: 0.5326 REMARK 3 L13: 0.6531 L23: -2.5028 REMARK 3 S TENSOR REMARK 3 S11: 0.1543 S12: 0.2926 S13: 0.3921 REMARK 3 S21: 0.3759 S22: -0.1578 S23: 0.2402 REMARK 3 S31: -0.6578 S32: -0.2229 S33: 0.0172 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 276:286) REMARK 3 ORIGIN FOR THE GROUP (A): 190.7052 41.7153 -6.2492 REMARK 3 T TENSOR REMARK 3 T11: 0.4630 T22: 0.4859 REMARK 3 T33: 0.3137 T12: 0.0420 REMARK 3 T13: -0.0620 T23: 0.1000 REMARK 3 L TENSOR REMARK 3 L11: 1.1133 L22: 1.0333 REMARK 3 L33: 0.4770 L12: -0.3799 REMARK 3 L13: -0.6065 L23: 0.5701 REMARK 3 S TENSOR REMARK 3 S11: -0.0822 S12: 0.0743 S13: -0.1423 REMARK 3 S21: -0.5215 S22: 0.2325 S23: 0.4087 REMARK 3 S31: 0.5025 S32: 0.1792 S33: -0.0138 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 287:294) REMARK 3 ORIGIN FOR THE GROUP (A): 192.7134 41.6388 12.4605 REMARK 3 T TENSOR REMARK 3 T11: 0.3340 T22: 0.2391 REMARK 3 T33: 0.3440 T12: 0.0194 REMARK 3 T13: 0.0005 T23: 0.0100 REMARK 3 L TENSOR REMARK 3 L11: 0.9937 L22: 0.3136 REMARK 3 L33: 1.6617 L12: -0.0584 REMARK 3 L13: -0.6678 L23: 0.6217 REMARK 3 S TENSOR REMARK 3 S11: 0.2597 S12: -0.2157 S13: 0.4016 REMARK 3 S21: 0.1705 S22: -0.2091 S23: 0.0566 REMARK 3 S31: -0.8210 S32: -0.1988 S33: -0.1010 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 295:305) REMARK 3 ORIGIN FOR THE GROUP (A): 197.5764 35.4649 19.0596 REMARK 3 T TENSOR REMARK 3 T11: 0.3439 T22: 0.3609 REMARK 3 T33: 0.2791 T12: -0.0164 REMARK 3 T13: -0.0141 T23: 0.0247 REMARK 3 L TENSOR REMARK 3 L11: 2.3282 L22: 0.6805 REMARK 3 L33: 0.4744 L12: -0.4860 REMARK 3 L13: -0.8165 L23: -0.1044 REMARK 3 S TENSOR REMARK 3 S11: -0.0358 S12: -0.6897 S13: 0.0431 REMARK 3 S21: 0.1824 S22: -0.0192 S23: 0.2167 REMARK 3 S31: -0.2796 S32: 0.4010 S33: -0.0494 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 306:321) REMARK 3 ORIGIN FOR THE GROUP (A): 200.6480 33.7151 7.6652 REMARK 3 T TENSOR REMARK 3 T11: 0.2908 T22: 0.2793 REMARK 3 T33: 0.2553 T12: -0.0144 REMARK 3 T13: -0.0261 T23: 0.0238 REMARK 3 L TENSOR REMARK 3 L11: 1.9069 L22: 0.1579 REMARK 3 L33: 3.6529 L12: -0.2722 REMARK 3 L13: 0.0698 L23: -0.5733 REMARK 3 S TENSOR REMARK 3 S11: 0.1430 S12: 0.1719 S13: -0.3610 REMARK 3 S21: -0.1124 S22: -0.0169 S23: -0.1586 REMARK 3 S31: 0.6873 S32: 0.1054 S33: -0.0858 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 242:256) REMARK 3 ORIGIN FOR THE GROUP (A): 171.0565 31.9889 14.4437 REMARK 3 T TENSOR REMARK 3 T11: 0.3654 T22: 0.4878 REMARK 3 T33: 0.3304 T12: -0.0253 REMARK 3 T13: 0.0026 T23: -0.0480 REMARK 3 L TENSOR REMARK 3 L11: 4.4240 L22: 3.0559 REMARK 3 L33: 0.7524 L12: -2.2159 REMARK 3 L13: 0.4360 L23: -0.3857 REMARK 3 S TENSOR REMARK 3 S11: 0.2206 S12: 1.1102 S13: -0.2250 REMARK 3 S21: -0.0703 S22: -0.2555 S23: 0.3869 REMARK 3 S31: -0.3057 S32: -0.0729 S33: -0.0003 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 257:267) REMARK 3 ORIGIN FOR THE GROUP (A): 178.9493 37.4431 14.5761 REMARK 3 T TENSOR REMARK 3 T11: 0.3005 T22: 0.3568 REMARK 3 T33: 0.3402 T12: 0.0332 REMARK 3 T13: 0.0012 T23: 0.0566 REMARK 3 L TENSOR REMARK 3 L11: 1.1205 L22: 1.2939 REMARK 3 L33: 4.3374 L12: 0.9318 REMARK 3 L13: -0.1832 L23: 1.0555 REMARK 3 S TENSOR REMARK 3 S11: 0.0473 S12: 0.2573 S13: 0.5343 REMARK 3 S21: 0.1244 S22: -0.1120 S23: 0.0715 REMARK 3 S31: -0.3468 S32: -0.4254 S33: 0.0716 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 268:275) REMARK 3 ORIGIN FOR THE GROUP (A): 179.9494 30.2591 13.9065 REMARK 3 T TENSOR REMARK 3 T11: 0.2809 T22: 0.4310 REMARK 3 T33: 0.3121 T12: 0.0124 REMARK 3 T13: 0.0505 T23: -0.0504 REMARK 3 L TENSOR REMARK 3 L11: 2.4355 L22: 2.8915 REMARK 3 L33: 2.7299 L12: 0.2576 REMARK 3 L13: -2.4026 L23: 0.4878 REMARK 3 S TENSOR REMARK 3 S11: 0.0906 S12: 0.5876 S13: -0.5151 REMARK 3 S21: -0.1179 S22: -0.0846 S23: -0.2018 REMARK 3 S31: 0.3513 S32: -0.3028 S33: 0.1419 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 276:286) REMARK 3 ORIGIN FOR THE GROUP (A): 166.9516 29.4206 4.6724 REMARK 3 T TENSOR REMARK 3 T11: 0.3219 T22: 1.1302 REMARK 3 T33: 0.2091 T12: 0.0113 REMARK 3 T13: -0.0496 T23: -0.3544 REMARK 3 L TENSOR REMARK 3 L11: 0.1350 L22: 0.3013 REMARK 3 L33: 0.9680 L12: -0.1986 REMARK 3 L13: 0.3482 L23: -0.4905 REMARK 3 S TENSOR REMARK 3 S11: 0.0558 S12: 0.1388 S13: -0.0497 REMARK 3 S21: -0.1336 S22: 0.1054 S23: 0.0005 REMARK 3 S31: -0.0117 S32: 0.0675 S33: 0.4573 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 287:305) REMARK 3 ORIGIN FOR THE GROUP (A): 176.3898 32.8616 22.5373 REMARK 3 T TENSOR REMARK 3 T11: 0.2927 T22: 0.3887 REMARK 3 T33: 0.2973 T12: -0.0107 REMARK 3 T13: 0.0418 T23: -0.0079 REMARK 3 L TENSOR REMARK 3 L11: 0.4749 L22: 0.5608 REMARK 3 L33: 1.0868 L12: 0.0358 REMARK 3 L13: -0.3411 L23: -0.5225 REMARK 3 S TENSOR REMARK 3 S11: 0.0265 S12: 0.0222 S13: -0.1723 REMARK 3 S21: 0.0660 S22: -0.1734 S23: -0.0001 REMARK 3 S31: 0.0432 S32: -0.0803 S33: 0.1137 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 306:322) REMARK 3 ORIGIN FOR THE GROUP (A): 167.1860 36.2204 18.5975 REMARK 3 T TENSOR REMARK 3 T11: 0.2541 T22: 0.3469 REMARK 3 T33: 0.2851 T12: 0.0367 REMARK 3 T13: 0.0637 T23: -0.0078 REMARK 3 L TENSOR REMARK 3 L11: 1.1624 L22: 5.5189 REMARK 3 L33: 0.9797 L12: -1.6053 REMARK 3 L13: 0.6926 L23: -1.4077 REMARK 3 S TENSOR REMARK 3 S11: -0.0335 S12: 0.3852 S13: 0.3530 REMARK 3 S21: 0.2213 S22: -0.2968 S23: -0.4219 REMARK 3 S31: -0.2159 S32: -0.3521 S33: 0.2718 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 6GC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-APR-18. REMARK 100 THE DEPOSITION ID IS D_1200009322. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-OCT-14 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35681 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 77.950 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.04556 REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 15.2300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 REMARK 200 COMPLETENESS FOR SHELL (%) : 81.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.66830 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3HI9 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM TRIS (PH8), 100 MM NACL, 10% REMARK 280 (W/V) GLYCEROL, 1MM TCEP PRECIPITANT: 2 M AMMONIUM SULFATE, 0.1 REMARK 280 M BIS-TRIS WELL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 75.64350 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.12900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 75.64350 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.12900 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 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 APPLY THE FOLLOWING TO CHAINS: A, B, E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1260 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 4970 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 4490 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1050 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 4920 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 4660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H 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 GLY A 237 REMARK 465 ALA A 238 REMARK 465 MET A 239 REMARK 465 GLY A 240 REMARK 465 SER A 241 REMARK 465 SER A 242 REMARK 465 ASN A 322 REMARK 465 LYS A 323 REMARK 465 SER A 324 REMARK 465 HIS A 325 REMARK 465 LYS A 326 REMARK 465 GLY B 237 REMARK 465 ALA B 238 REMARK 465 MET B 239 REMARK 465 GLY B 240 REMARK 465 SER B 241 REMARK 465 SER B 242 REMARK 465 PHE B 279 REMARK 465 ASN B 280 REMARK 465 THR B 281 REMARK 465 ASN B 282 REMARK 465 LYS B 323 REMARK 465 SER B 324 REMARK 465 HIS B 325 REMARK 465 LYS B 326 REMARK 465 GLY C 237 REMARK 465 ALA C 238 REMARK 465 MET C 239 REMARK 465 GLY C 240 REMARK 465 SER C 241 REMARK 465 SER C 242 REMARK 465 ASN C 322 REMARK 465 LYS C 323 REMARK 465 SER C 324 REMARK 465 HIS C 325 REMARK 465 LYS C 326 REMARK 465 GLY D 237 REMARK 465 ALA D 238 REMARK 465 MET D 239 REMARK 465 GLY D 240 REMARK 465 SER D 241 REMARK 465 ASN D 280 REMARK 465 THR D 281 REMARK 465 ASN D 282 REMARK 465 LYS D 283 REMARK 465 LYS D 323 REMARK 465 SER D 324 REMARK 465 HIS D 325 REMARK 465 LYS D 326 REMARK 465 U E 6 REMARK 465 A E 7 REMARK 465 U E 8 REMARK 465 U E 9 REMARK 465 U E 10 REMARK 465 U E 11 REMARK 465 A F 1 REMARK 465 U F 5 REMARK 465 U F 6 REMARK 465 A F 7 REMARK 465 U F 8 REMARK 465 U F 9 REMARK 465 U F 10 REMARK 465 U F 11 REMARK 465 A G -2 REMARK 465 U G -1 REMARK 465 U G 0 REMARK 465 U G 5 REMARK 465 U G 6 REMARK 465 U G 7 REMARK 465 U G 8 REMARK 465 A H 1 REMARK 465 U H 5 REMARK 465 U H 6 REMARK 465 A H 7 REMARK 465 U H 8 REMARK 465 U H 9 REMARK 465 U H 10 REMARK 465 U H 11 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ASP A 256 OD1 OD2 REMARK 470 GLU A 257 CD OE1 OE2 REMARK 470 LYS A 274 CE NZ REMARK 470 ASN A 282 OD1 ND2 REMARK 470 ARG A 309 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 312 CG OD1 OD2 REMARK 470 LYS A 313 CG CD CE NZ REMARK 470 GLN B 253 CG CD OE1 NE2 REMARK 470 ASP B 254 CG OD1 OD2 REMARK 470 ASP B 256 OD1 OD2 REMARK 470 GLN B 262 CD OE1 NE2 REMARK 470 LYS B 274 NZ REMARK 470 LYS B 283 CG CD CE NZ REMARK 470 GLU B 296 CG CD OE1 OE2 REMARK 470 ARG B 309 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 312 CG OD1 OD2 REMARK 470 LYS B 313 CG CD CE NZ REMARK 470 LYS C 283 CE NZ REMARK 470 LYS C 285 CE NZ REMARK 470 GLU C 296 CG CD OE1 OE2 REMARK 470 MET C 300 CE REMARK 470 ARG C 309 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 312 CG OD1 OD2 REMARK 470 LYS C 313 CE NZ REMARK 470 SER D 242 OG REMARK 470 GLN D 253 CG CD OE1 NE2 REMARK 470 ASP D 254 CG OD1 OD2 REMARK 470 GLU D 257 OE1 OE2 REMARK 470 ILE D 259 CD1 REMARK 470 GLN D 262 CD OE1 NE2 REMARK 470 MET D 263 SD CE REMARK 470 LYS D 274 CD CE NZ REMARK 470 PHE D 279 C O CB CG CD1 CD2 CE1 REMARK 470 PHE D 279 CE2 CZ REMARK 470 GLU D 296 CG CD OE1 OE2 REMARK 470 ARG D 309 CG CD NE CZ NH1 NH2 REMARK 470 ASP D 312 CG OD1 OD2 REMARK 470 LYS D 313 NZ REMARK 470 ASN D 322 OD1 ND2 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 A E 1 C6 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 F 101 O HOH F 102 1.89 REMARK 500 O HOH B 439 O HOH C 440 1.98 REMARK 500 O3' U F 4 O HOH F 101 1.99 REMARK 500 O HOH A 435 O HOH B 431 2.01 REMARK 500 O HOH A 401 O HOH B 406 2.06 REMARK 500 O HOH C 432 O HOH C 448 2.09 REMARK 500 O HOH D 424 O HOH D 430 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 437 O HOH A 439 4856 1.92 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 ASN A 250 29.60 83.07 REMARK 500 ASN A 282 14.57 57.46 REMARK 500 ASN B 250 30.49 87.25 REMARK 500 ASN B 272 146.05 -170.34 REMARK 500 ASN C 250 27.41 82.14 REMARK 500 ASN D 250 32.29 90.59 REMARK 500 ASN D 272 142.40 -170.21 REMARK 500 REMARK 500 REMARK: NULL DBREF 6GC5 A 241 326 UNP Q15717 ELAV1_HUMAN 241 326 DBREF 6GC5 B 241 326 UNP Q15717 ELAV1_HUMAN 241 326 DBREF 6GC5 C 241 326 UNP Q15717 ELAV1_HUMAN 241 326 DBREF 6GC5 D 241 326 UNP Q15717 ELAV1_HUMAN 241 326 DBREF 6GC5 E 1 11 PDB 6GC5 6GC5 1 11 DBREF 6GC5 F 1 11 PDB 6GC5 6GC5 1 11 DBREF 6GC5 G -2 8 PDB 6GC5 6GC5 -2 8 DBREF 6GC5 H 1 11 PDB 6GC5 6GC5 1 11 SEQADV 6GC5 GLY A 237 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 ALA A 238 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 MET A 239 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 GLY A 240 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 GLY B 237 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 ALA B 238 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 MET B 239 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 GLY B 240 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 GLY C 237 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 ALA C 238 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 MET C 239 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 GLY C 240 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 GLY D 237 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 ALA D 238 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 MET D 239 UNP Q15717 EXPRESSION TAG SEQADV 6GC5 GLY D 240 UNP Q15717 EXPRESSION TAG SEQRES 1 A 90 GLY ALA MET GLY SER SER GLY TRP CYS ILE PHE ILE TYR SEQRES 2 A 90 ASN LEU GLY GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN SEQRES 3 A 90 MET PHE GLY PRO PHE GLY ALA VAL THR ASN VAL LYS VAL SEQRES 4 A 90 ILE ARG ASP PHE ASN THR ASN LYS CYS LYS GLY PHE GLY SEQRES 5 A 90 PHE VAL THR MET THR ASN TYR GLU GLU ALA ALA MET ALA SEQRES 6 A 90 ILE ALA SER LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE SEQRES 7 A 90 LEU GLN VAL SER PHE LYS THR ASN LYS SER HIS LYS SEQRES 1 B 90 GLY ALA MET GLY SER SER GLY TRP CYS ILE PHE ILE TYR SEQRES 2 B 90 ASN LEU GLY GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN SEQRES 3 B 90 MET PHE GLY PRO PHE GLY ALA VAL THR ASN VAL LYS VAL SEQRES 4 B 90 ILE ARG ASP PHE ASN THR ASN LYS CYS LYS GLY PHE GLY SEQRES 5 B 90 PHE VAL THR MET THR ASN TYR GLU GLU ALA ALA MET ALA SEQRES 6 B 90 ILE ALA SER LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE SEQRES 7 B 90 LEU GLN VAL SER PHE LYS THR ASN LYS SER HIS LYS SEQRES 1 C 90 GLY ALA MET GLY SER SER GLY TRP CYS ILE PHE ILE TYR SEQRES 2 C 90 ASN LEU GLY GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN SEQRES 3 C 90 MET PHE GLY PRO PHE GLY ALA VAL THR ASN VAL LYS VAL SEQRES 4 C 90 ILE ARG ASP PHE ASN THR ASN LYS CYS LYS GLY PHE GLY SEQRES 5 C 90 PHE VAL THR MET THR ASN TYR GLU GLU ALA ALA MET ALA SEQRES 6 C 90 ILE ALA SER LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE SEQRES 7 C 90 LEU GLN VAL SER PHE LYS THR ASN LYS SER HIS LYS SEQRES 1 D 90 GLY ALA MET GLY SER SER GLY TRP CYS ILE PHE ILE TYR SEQRES 2 D 90 ASN LEU GLY GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN SEQRES 3 D 90 MET PHE GLY PRO PHE GLY ALA VAL THR ASN VAL LYS VAL SEQRES 4 D 90 ILE ARG ASP PHE ASN THR ASN LYS CYS LYS GLY PHE GLY SEQRES 5 D 90 PHE VAL THR MET THR ASN TYR GLU GLU ALA ALA MET ALA SEQRES 6 D 90 ILE ALA SER LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE SEQRES 7 D 90 LEU GLN VAL SER PHE LYS THR ASN LYS SER HIS LYS SEQRES 1 E 11 A U U U U U A U U U U SEQRES 1 F 11 A U U U U U A U U U U SEQRES 1 G 11 A U U U U U A U U U U SEQRES 1 H 11 A U U U U U A U U U U FORMUL 9 HOH *191(H2 O) HELIX 1 AA1 ASP A 256 GLY A 265 1 10 HELIX 2 AA2 PRO A 266 GLY A 268 5 3 HELIX 3 AA3 ASN A 294 ASN A 306 1 13 HELIX 4 AA4 ASP B 256 GLY B 265 1 10 HELIX 5 AA5 PRO B 266 GLY B 268 5 3 HELIX 6 AA6 ASN B 294 ASN B 306 1 13 HELIX 7 AA7 ASP C 256 GLY C 265 1 10 HELIX 8 AA8 PRO C 266 GLY C 268 5 3 HELIX 9 AA9 ASN C 294 ASN C 306 1 13 HELIX 10 AB1 ASP D 256 GLY D 265 1 10 HELIX 11 AB2 PRO D 266 GLY D 268 5 3 HELIX 12 AB3 ASN D 294 ASN D 306 1 13 SHEET 1 AA1 4 VAL A 270 ARG A 277 0 SHEET 2 AA1 4 CYS A 284 MET A 292 -1 O THR A 291 N ASN A 272 SHEET 3 AA1 4 TRP A 244 TYR A 249 -1 N ILE A 246 O VAL A 290 SHEET 4 AA1 4 GLN A 316 PHE A 319 -1 O SER A 318 N PHE A 247 SHEET 1 AA2 2 ARG A 309 LEU A 310 0 SHEET 2 AA2 2 LYS A 313 ILE A 314 -1 O LYS A 313 N LEU A 310 SHEET 1 AA3 4 VAL B 270 VAL B 275 0 SHEET 2 AA3 4 PHE B 287 MET B 292 -1 O THR B 291 N THR B 271 SHEET 3 AA3 4 TRP B 244 TYR B 249 -1 N ILE B 246 O VAL B 290 SHEET 4 AA3 4 GLN B 316 PHE B 319 -1 O SER B 318 N PHE B 247 SHEET 1 AA4 2 ARG B 309 LEU B 310 0 SHEET 2 AA4 2 LYS B 313 ILE B 314 -1 O LYS B 313 N LEU B 310 SHEET 1 AA5 4 VAL C 270 ARG C 277 0 SHEET 2 AA5 4 CYS C 284 MET C 292 -1 O THR C 291 N ASN C 272 SHEET 3 AA5 4 TRP C 244 TYR C 249 -1 N TRP C 244 O MET C 292 SHEET 4 AA5 4 GLN C 316 PHE C 319 -1 O SER C 318 N PHE C 247 SHEET 1 AA6 2 ARG C 309 LEU C 310 0 SHEET 2 AA6 2 LYS C 313 ILE C 314 -1 O LYS C 313 N LEU C 310 SHEET 1 AA7 4 VAL D 270 VAL D 275 0 SHEET 2 AA7 4 PHE D 287 MET D 292 -1 O THR D 291 N ASN D 272 SHEET 3 AA7 4 TRP D 244 TYR D 249 -1 N ILE D 246 O VAL D 290 SHEET 4 AA7 4 GLN D 316 PHE D 319 -1 O SER D 318 N PHE D 247 SHEET 1 AA8 2 ARG D 309 LEU D 310 0 SHEET 2 AA8 2 LYS D 313 ILE D 314 -1 O LYS D 313 N LEU D 310 CRYST1 151.287 40.258 106.496 90.00 132.95 90.00 C 1 2 1 16 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 0.006610 0.000000 0.006154 0.00000 SCALE2 0.000000 0.024840 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012829 0.00000 ATOM 1 N GLY A 243 211.337 47.594 37.591 1.00 44.14 N ANISOU 1 N GLY A 243 5713 5054 6006 -297 342 162 N ATOM 2 CA GLY A 243 210.572 46.659 38.404 1.00 45.31 C ANISOU 2 CA GLY A 243 5857 5205 6152 -305 316 144 C ATOM 3 C GLY A 243 211.096 46.479 39.832 1.00 44.86 C ANISOU 3 C GLY A 243 5816 5138 6089 -346 332 95 C ATOM 4 O GLY A 243 211.560 47.423 40.476 1.00 47.19 O ANISOU 4 O GLY A 243 6122 5407 6402 -370 384 78 O ATOM 5 N TRP A 244 211.020 45.250 40.325 1.00 35.73 N ANISOU 5 N TRP A 244 4664 4006 4907 -360 283 75 N ATOM 6 CA TRP A 244 211.363 44.935 41.699 1.00 32.43 C ANISOU 6 CA TRP A 244 4259 3585 4479 -407 285 37 C ATOM 7 C TRP A 244 212.742 44.286 41.719 1.00 35.11 C ANISOU 7 C TRP A 244 4609 3947 4786 -422 249 13 C ATOM 8 O TRP A 244 213.016 43.313 40.995 1.00 33.38 O ANISOU 8 O TRP A 244 4383 3752 4546 -400 195 16 O ATOM 9 CB TRP A 244 210.312 44.007 42.263 1.00 34.19 C ANISOU 9 CB TRP A 244 4476 3817 4699 -417 250 38 C ATOM 10 CG TRP A 244 208.963 44.607 42.163 1.00 41.31 C ANISOU 10 CG TRP A 244 5360 4698 5637 -398 284 63 C ATOM 11 CD1 TRP A 244 208.014 44.376 41.187 1.00 40.14 C ANISOU 11 CD1 TRP A 244 5193 4558 5500 -357 260 103 C ATOM 12 CD2 TRP A 244 208.406 45.584 43.045 1.00 42.29 C ANISOU 12 CD2 TRP A 244 5480 4790 5797 -419 351 50 C ATOM 13 NE1 TRP A 244 206.886 45.136 41.442 1.00 41.92 N ANISOU 13 NE1 TRP A 244 5399 4758 5771 -349 305 119 N ATOM 14 CE2 TRP A 244 207.104 45.889 42.579 1.00 41.36 C ANISOU 14 CE2 TRP A 244 5336 4660 5718 -385 365 83 C ATOM 15 CE3 TRP A 244 208.877 46.227 44.205 1.00 44.95 C ANISOU 15 CE3 TRP A 244 5832 5109 6137 -467 403 10 C ATOM 16 CZ2 TRP A 244 206.268 46.806 43.214 1.00 46.57 C ANISOU 16 CZ2 TRP A 244 5981 5286 6429 -390 430 76 C ATOM 17 CZ3 TRP A 244 208.037 47.138 44.854 1.00 47.85 C ANISOU 17 CZ3 TRP A 244 6188 5444 6548 -479 471 -2 C ATOM 18 CH2 TRP A 244 206.747 47.417 44.351 1.00 49.59 C ANISOU 18 CH2 TRP A 244 6379 5648 6815 -437 485 29 C ATOM 19 N CYS A 245 213.625 44.866 42.518 1.00 33.01 N ANISOU 19 N CYS A 245 4354 3671 4516 -461 283 -11 N ATOM 20 CA CYS A 245 215.006 44.440 42.539 1.00 27.18 C ANISOU 20 CA CYS A 245 3620 2952 3754 -475 255 -30 C ATOM 21 C CYS A 245 215.195 43.451 43.669 1.00 30.63 C ANISOU 21 C CYS A 245 4062 3400 4177 -518 211 -48 C ATOM 22 O CYS A 245 214.805 43.723 44.806 1.00 30.18 O ANISOU 22 O CYS A 245 4014 3332 4121 -564 234 -58 O ATOM 23 CB CYS A 245 215.927 45.640 42.725 1.00 33.34 C ANISOU 23 CB CYS A 245 4410 3721 4537 -497 312 -40 C ATOM 24 SG CYS A 245 217.704 45.251 42.345 1.00 45.02 S ANISOU 24 SG CYS A 245 5885 5230 5992 -501 283 -57 S ATOM 25 N ILE A 246 215.778 42.295 43.343 1.00 26.48 N ANISOU 25 N ILE A 246 3527 2894 3639 -505 147 -53 N ATOM 26 CA ILE A 246 216.039 41.220 44.290 1.00 27.91 C ANISOU 26 CA ILE A 246 3710 3084 3813 -543 90 -62 C ATOM 27 C ILE A 246 217.556 41.088 44.525 1.00 30.55 C ANISOU 27 C ILE A 246 4038 3427 4142 -563 73 -76 C ATOM 28 O ILE A 246 218.346 41.036 43.572 1.00 29.56 O ANISOU 28 O ILE A 246 3900 3311 4020 -526 68 -82 O ATOM 29 CB ILE A 246 215.488 39.869 43.794 1.00 26.19 C ANISOU 29 CB ILE A 246 3482 2873 3596 -513 20 -54 C ATOM 30 CG1 ILE A 246 213.973 39.965 43.559 1.00 28.36 C ANISOU 30 CG1 ILE A 246 3759 3143 3874 -495 33 -35 C ATOM 31 CG2 ILE A 246 215.848 38.725 44.821 1.00 24.63 C ANISOU 31 CG2 ILE A 246 3284 2678 3396 -556 -47 -57 C ATOM 32 CD1 ILE A 246 213.375 38.813 42.726 1.00 26.69 C ANISOU 32 CD1 ILE A 246 3540 2941 3662 -457 -27 -25 C ATOM 33 N PHE A 247 217.952 41.037 45.796 1.00 27.75 N ANISOU 33 N PHE A 247 3690 3073 3779 -626 64 -81 N ATOM 34 CA PHE A 247 219.333 40.765 46.228 1.00 26.20 C ANISOU 34 CA PHE A 247 3485 2887 3581 -655 36 -87 C ATOM 35 C PHE A 247 219.565 39.264 46.526 1.00 26.44 C ANISOU 35 C PHE A 247 3501 2922 3623 -660 -54 -80 C ATOM 36 O PHE A 247 218.746 38.611 47.182 1.00 28.05 O ANISOU 36 O PHE A 247 3712 3123 3823 -687 -90 -69 O ATOM 37 CB PHE A 247 219.617 41.613 47.477 1.00 28.09 C ANISOU 37 CB PHE A 247 3742 3128 3803 -731 76 -92 C ATOM 38 CG PHE A 247 220.935 41.338 48.133 1.00 30.77 C ANISOU 38 CG PHE A 247 4072 3482 4138 -777 43 -91 C ATOM 39 CD1 PHE A 247 222.127 41.735 47.538 1.00 28.59 C ANISOU 39 CD1 PHE A 247 3782 3214 3868 -756 57 -97 C ATOM 40 CD2 PHE A 247 220.987 40.704 49.364 1.00 33.47 C ANISOU 40 CD2 PHE A 247 4417 3832 4468 -846 -5 -80 C ATOM 41 CE1 PHE A 247 223.347 41.496 48.170 1.00 29.30 C ANISOU 41 CE1 PHE A 247 3857 3318 3956 -800 24 -93 C ATOM 42 CE2 PHE A 247 222.198 40.454 49.994 1.00 33.41 C ANISOU 42 CE2 PHE A 247 4397 3839 4459 -892 -42 -71 C ATOM 43 CZ PHE A 247 223.378 40.863 49.411 1.00 28.97 C ANISOU 43 CZ PHE A 247 3818 3283 3907 -868 -26 -77 C ATOM 44 N ILE A 248 220.669 38.706 46.023 1.00 26.46 N ANISOU 44 N ILE A 248 3480 2930 3644 -633 -90 -87 N ATOM 45 CA ILE A 248 220.973 37.296 46.250 1.00 22.14 C ANISOU 45 CA ILE A 248 2914 2378 3121 -632 -176 -80 C ATOM 46 C ILE A 248 222.404 37.229 46.780 1.00 29.10 C ANISOU 46 C ILE A 248 3775 3267 4017 -664 -199 -78 C ATOM 47 O ILE A 248 223.336 37.724 46.130 1.00 28.58 O ANISOU 47 O ILE A 248 3694 3210 3956 -637 -168 -94 O ATOM 48 CB ILE A 248 220.941 36.438 44.980 1.00 29.94 C ANISOU 48 CB ILE A 248 3884 3360 4133 -559 -207 -95 C ATOM 49 CG1 ILE A 248 219.601 36.555 44.227 1.00 33.30 C ANISOU 49 CG1 ILE A 248 4326 3783 4543 -523 -183 -94 C ATOM 50 CG2 ILE A 248 221.202 34.981 45.356 1.00 25.84 C ANISOU 50 CG2 ILE A 248 3347 2825 3648 -562 -297 -88 C ATOM 51 CD1 ILE A 248 219.419 37.844 43.423 1.00 32.57 C ANISOU 51 CD1 ILE A 248 4242 3701 4432 -498 -103 -99 C ATOM 52 N TYR A 249 222.571 36.609 47.937 1.00 25.98 N ANISOU 52 N TYR A 249 3378 2869 3626 -723 -256 -56 N ATOM 53 CA TYR A 249 223.893 36.412 48.519 1.00 25.02 C ANISOU 53 CA TYR A 249 3231 2754 3521 -758 -292 -45 C ATOM 54 C TYR A 249 224.195 34.912 48.649 1.00 23.05 C ANISOU 54 C TYR A 249 2953 2485 3320 -746 -390 -29 C ATOM 55 O TYR A 249 223.283 34.082 48.816 1.00 24.58 O ANISOU 55 O TYR A 249 3157 2664 3519 -746 -436 -17 O ATOM 56 CB TYR A 249 224.011 37.107 49.881 1.00 28.90 C ANISOU 56 CB TYR A 249 3743 3262 3976 -854 -274 -26 C ATOM 57 CG TYR A 249 225.412 36.972 50.451 1.00 32.18 C ANISOU 57 CG TYR A 249 4130 3688 4408 -894 -312 -9 C ATOM 58 CD1 TYR A 249 226.418 37.869 50.089 1.00 32.49 C ANISOU 58 CD1 TYR A 249 4159 3743 4443 -887 -261 -23 C ATOM 59 CD2 TYR A 249 225.741 35.919 51.298 1.00 36.94 C ANISOU 59 CD2 TYR A 249 4714 4287 5034 -939 -403 26 C ATOM 60 CE1 TYR A 249 227.713 37.741 50.589 1.00 37.54 C ANISOU 60 CE1 TYR A 249 4769 4396 5099 -924 -297 -4 C ATOM 61 CE2 TYR A 249 227.041 35.784 51.813 1.00 36.73 C ANISOU 61 CE2 TYR A 249 4656 4271 5028 -976 -442 50 C ATOM 62 CZ TYR A 249 228.015 36.699 51.444 1.00 41.97 C ANISOU 62 CZ TYR A 249 5309 4952 5686 -967 -388 33 C ATOM 63 OH TYR A 249 229.300 36.566 51.923 1.00 46.72 O ANISOU 63 OH TYR A 249 5875 5566 6309 -1003 -427 58 O ATOM 64 N ASN A 250 225.494 34.592 48.622 1.00 29.10 N ANISOU 64 N ASN A 250 3681 3251 4124 -739 -423 -26 N ATOM 65 CA ASN A 250 226.041 33.231 48.569 1.00 28.98 C ANISOU 65 CA ASN A 250 3627 3211 4172 -714 -512 -16 C ATOM 66 C ASN A 250 226.132 32.562 47.173 1.00 32.95 C ANISOU 66 C ASN A 250 4106 3694 4719 -618 -515 -55 C ATOM 67 O ASN A 250 226.058 31.334 47.038 1.00 35.34 O ANISOU 67 O ASN A 250 4389 3966 5073 -591 -584 -53 O ATOM 68 CB ASN A 250 225.428 32.301 49.606 1.00 29.88 C ANISOU 68 CB ASN A 250 3751 3309 4293 -768 -593 25 C ATOM 69 CG ASN A 250 226.336 32.123 50.816 1.00 36.43 C ANISOU 69 CG ASN A 250 4560 4145 5136 -846 -650 69 C ATOM 70 OD1 ASN A 250 227.552 32.339 50.735 1.00 33.15 O ANISOU 70 OD1 ASN A 250 4111 3737 4748 -840 -648 69 O ATOM 71 ND2 ASN A 250 225.759 31.725 51.932 1.00 35.50 N ANISOU 71 ND2 ASN A 250 4461 4029 4998 -923 -701 110 N ATOM 72 N LEU A 251 226.305 33.376 46.140 1.00 32.30 N ANISOU 72 N LEU A 251 4025 3631 4616 -573 -439 -91 N ATOM 73 CA LEU A 251 226.732 32.858 44.844 1.00 32.39 C ANISOU 73 CA LEU A 251 4006 3635 4666 -495 -435 -134 C ATOM 74 C LEU A 251 228.186 32.425 44.986 1.00 33.24 C ANISOU 74 C LEU A 251 4060 3738 4832 -488 -471 -136 C ATOM 75 O LEU A 251 228.914 33.022 45.755 1.00 33.16 O ANISOU 75 O LEU A 251 4041 3745 4812 -538 -465 -112 O ATOM 76 CB LEU A 251 226.625 33.961 43.787 1.00 29.44 C ANISOU 76 CB LEU A 251 3647 3291 4248 -463 -345 -164 C ATOM 77 CG LEU A 251 225.220 34.534 43.548 1.00 29.17 C ANISOU 77 CG LEU A 251 3659 3262 4161 -465 -303 -158 C ATOM 78 CD1 LEU A 251 225.288 35.721 42.594 1.00 27.50 C ANISOU 78 CD1 LEU A 251 3458 3078 3912 -442 -220 -178 C ATOM 79 CD2 LEU A 251 224.215 33.459 43.056 1.00 27.18 C ANISOU 79 CD2 LEU A 251 3415 2987 3924 -429 -346 -166 C ATOM 80 N GLY A 252 228.621 31.427 44.228 1.00 37.06 N ANISOU 80 N GLY A 252 4505 4199 5377 -429 -503 -168 N ATOM 81 CA GLY A 252 230.042 31.075 44.230 1.00 39.32 C ANISOU 81 CA GLY A 252 4732 4482 5728 -413 -528 -177 C ATOM 82 C GLY A 252 230.945 32.084 43.519 1.00 38.53 C ANISOU 82 C GLY A 252 4613 4423 5604 -397 -451 -209 C ATOM 83 O GLY A 252 230.476 32.962 42.789 1.00 37.71 O ANISOU 83 O GLY A 252 4540 4347 5440 -386 -378 -231 O ATOM 84 N GLN A 253 232.254 31.946 43.707 1.00 35.38 N ANISOU 84 N GLN A 253 4159 4028 5256 -396 -469 -209 N ATOM 85 CA GLN A 253 233.231 32.861 43.111 1.00 35.59 C ANISOU 85 CA GLN A 253 4162 4098 5263 -387 -401 -236 C ATOM 86 C GLN A 253 233.230 32.901 41.578 1.00 36.13 C ANISOU 86 C GLN A 253 4221 4185 5324 -321 -342 -302 C ATOM 87 O GLN A 253 233.590 33.919 40.971 1.00 34.52 O ANISOU 87 O GLN A 253 4021 4024 5071 -323 -270 -321 O ATOM 88 CB GLN A 253 234.639 32.475 43.592 1.00 37.00 C ANISOU 88 CB GLN A 253 4272 4273 5512 -393 -443 -223 C ATOM 89 CG GLN A 253 234.737 32.371 45.114 0.78 41.22 C ANISOU 89 CG GLN A 253 4812 4795 6056 -467 -511 -152 C ATOM 90 CD GLN A 253 234.764 33.728 45.785 0.33 45.78 C ANISOU 90 CD GLN A 253 5429 5414 6552 -541 -462 -120 C ATOM 91 OE1 GLN A 253 235.719 34.485 45.619 0.56 47.86 O ANISOU 91 OE1 GLN A 253 5668 5712 6802 -551 -420 -127 O ATOM 92 NE2 GLN A 253 233.714 34.048 46.547 0.93 49.08 N ANISOU 92 NE2 GLN A 253 5906 5828 6915 -594 -465 -88 N ATOM 93 N ASP A 254 232.870 31.786 40.955 1.00 35.09 N ANISOU 93 N ASP A 254 4075 4021 5238 -269 -372 -338 N ATOM 94 CA ASP A 254 232.839 31.700 39.494 1.00 36.71 C ANISOU 94 CA ASP A 254 4271 4245 5433 -214 -320 -405 C ATOM 95 C ASP A 254 231.415 31.828 38.940 1.00 34.99 C ANISOU 95 C ASP A 254 4113 4028 5154 -208 -297 -409 C ATOM 96 O ASP A 254 231.134 31.422 37.804 1.00 33.52 O ANISOU 96 O ASP A 254 3924 3847 4964 -166 -275 -461 O ATOM 97 CB ASP A 254 233.432 30.369 39.030 1.00 41.61 C ANISOU 97 CB ASP A 254 4832 4829 6147 -158 -360 -454 C ATOM 98 CG ASP A 254 234.915 30.254 39.331 1.00 50.35 C ANISOU 98 CG ASP A 254 5868 5939 7322 -153 -373 -458 C ATOM 99 OD1 ASP A 254 235.675 31.183 38.974 1.00 54.48 O ANISOU 99 OD1 ASP A 254 6376 6514 7811 -163 -313 -472 O ATOM 100 OD2 ASP A 254 235.310 29.232 39.931 1.00 51.49 O ANISOU 100 OD2 ASP A 254 5972 6035 7558 -141 -447 -445 O ATOM 101 N ALA A 255 230.508 32.375 39.732 1.00 34.36 N ANISOU 101 N ALA A 255 4085 3944 5026 -252 -303 -357 N ATOM 102 CA ALA A 255 229.131 32.511 39.256 1.00 33.33 C ANISOU 102 CA ALA A 255 4006 3815 4844 -247 -284 -355 C ATOM 103 C ALA A 255 229.082 33.464 38.062 1.00 33.54 C ANISOU 103 C ALA A 255 4044 3888 4810 -232 -204 -383 C ATOM 104 O ALA A 255 229.860 34.414 37.982 1.00 32.42 O ANISOU 104 O ALA A 255 3893 3780 4647 -248 -157 -383 O ATOM 105 CB ALA A 255 228.226 33.010 40.365 1.00 30.24 C ANISOU 105 CB ALA A 255 3660 3413 4415 -299 -298 -297 C ATOM 106 N ASP A 256 228.152 33.220 37.144 1.00 30.07 N ANISOU 106 N ASP A 256 3628 3452 4343 -207 -191 -404 N ATOM 107 CA ASP A 256 227.936 34.127 36.019 1.00 32.43 C ANISOU 107 CA ASP A 256 3945 3798 4581 -202 -123 -419 C ATOM 108 C ASP A 256 226.440 34.405 35.885 1.00 32.84 C ANISOU 108 C ASP A 256 4046 3845 4586 -210 -118 -387 C ATOM 109 O ASP A 256 225.643 33.781 36.583 1.00 34.80 O ANISOU 109 O ASP A 256 4313 4059 4852 -217 -167 -363 O ATOM 110 CB ASP A 256 228.461 33.485 34.735 1.00 39.60 C ANISOU 110 CB ASP A 256 4819 4726 5502 -162 -106 -486 C ATOM 111 CG ASP A 256 227.741 32.193 34.398 1.00 41.13 C ANISOU 111 CG ASP A 256 5016 4887 5724 -133 -152 -513 C ATOM 112 N GLU A 257 226.064 35.319 34.985 1.00 29.96 N ANISOU 112 N GLU A 257 3701 3517 4165 -213 -63 -383 N ATOM 113 CA GLU A 257 224.677 35.727 34.819 1.00 33.96 C ANISOU 113 CA GLU A 257 4249 4022 4631 -221 -55 -347 C ATOM 114 C GLU A 257 223.772 34.510 34.631 1.00 34.65 C ANISOU 114 C GLU A 257 4345 4086 4734 -201 -106 -358 C ATOM 115 O GLU A 257 222.634 34.447 35.158 1.00 33.08 O ANISOU 115 O GLU A 257 4175 3866 4528 -212 -129 -320 O ATOM 116 CB GLU A 257 224.527 36.701 33.633 1.00 36.94 C ANISOU 116 CB GLU A 257 4636 4444 4953 -223 3 -345 C ATOM 117 CG GLU A 257 224.859 38.149 33.997 1.00 42.17 C ANISOU 117 CG GLU A 257 5311 5119 5594 -252 51 -309 C ATOM 118 N GLY A 258 224.288 33.538 33.892 1.00 29.98 N ANISOU 118 N GLY A 258 3727 3498 4166 -172 -121 -413 N ATOM 119 CA GLY A 258 223.521 32.344 33.573 1.00 31.92 C ANISOU 119 CA GLY A 258 3981 3721 4427 -154 -166 -432 C ATOM 120 C GLY A 258 222.824 31.755 34.795 1.00 32.32 C ANISOU 120 C GLY A 258 4048 3724 4509 -166 -227 -394 C ATOM 121 O GLY A 258 221.659 31.342 34.719 1.00 28.21 O ANISOU 121 O GLY A 258 3554 3193 3972 -168 -253 -376 O ATOM 122 N ILE A 259 223.505 31.724 35.934 1.00 29.99 N ANISOU 122 N ILE A 259 3737 3404 4253 -181 -252 -377 N ATOM 123 CA ILE A 259 222.899 31.080 37.088 1.00 29.25 C ANISOU 123 CA ILE A 259 3657 3269 4187 -200 -314 -342 C ATOM 124 C ILE A 259 221.690 31.867 37.620 1.00 26.88 C ANISOU 124 C ILE A 259 3398 2976 3840 -233 -299 -289 C ATOM 125 O ILE A 259 220.710 31.279 38.077 1.00 26.88 O ANISOU 125 O ILE A 259 3417 2955 3841 -244 -342 -266 O ATOM 126 CB ILE A 259 223.916 30.784 38.227 1.00 30.78 C ANISOU 126 CB ILE A 259 3823 3437 4434 -218 -353 -331 C ATOM 127 CG1 ILE A 259 223.240 29.885 39.276 1.00 32.25 C ANISOU 127 CG1 ILE A 259 4023 3582 4649 -241 -429 -296 C ATOM 128 CG2 ILE A 259 224.399 32.049 38.869 1.00 31.59 C ANISOU 128 CG2 ILE A 259 3930 3563 4511 -253 -310 -301 C ATOM 129 CD1 ILE A 259 222.726 28.563 38.695 1.00 34.99 C ANISOU 129 CD1 ILE A 259 4369 3899 5027 -209 -478 -324 C ATOM 130 N LEU A 260 221.767 33.194 37.571 1.00 24.59 N ANISOU 130 N LEU A 260 3118 2715 3512 -248 -238 -270 N ATOM 131 CA LEU A 260 220.670 34.004 38.062 1.00 24.93 C ANISOU 131 CA LEU A 260 3194 2760 3521 -275 -216 -225 C ATOM 132 C LEU A 260 219.500 33.808 37.128 1.00 26.16 C ANISOU 132 C LEU A 260 3366 2926 3649 -255 -214 -222 C ATOM 133 O LEU A 260 218.347 33.683 37.567 1.00 26.07 O ANISOU 133 O LEU A 260 3376 2903 3628 -269 -233 -191 O ATOM 134 CB LEU A 260 221.064 35.474 38.142 1.00 24.31 C ANISOU 134 CB LEU A 260 3120 2702 3416 -293 -150 -210 C ATOM 135 CG LEU A 260 222.135 35.727 39.219 1.00 29.76 C ANISOU 135 CG LEU A 260 3797 3384 4128 -325 -153 -207 C ATOM 136 CD1 LEU A 260 222.573 37.165 39.185 1.00 26.42 C ANISOU 136 CD1 LEU A 260 3380 2980 3677 -343 -86 -197 C ATOM 137 CD2 LEU A 260 221.585 35.375 40.586 1.00 30.76 C ANISOU 137 CD2 LEU A 260 3938 3485 4265 -365 -194 -177 C ATOM 138 N TRP A 261 219.781 33.737 35.821 1.00 24.02 N ANISOU 138 N TRP A 261 3084 2679 3362 -227 -192 -254 N ATOM 139 CA TRP A 261 218.644 33.509 34.895 1.00 22.71 C ANISOU 139 CA TRP A 261 2935 2528 3165 -215 -195 -247 C ATOM 140 C TRP A 261 217.990 32.170 35.168 1.00 24.23 C ANISOU 140 C TRP A 261 3134 2692 3379 -210 -261 -253 C ATOM 141 O TRP A 261 216.765 32.062 35.191 1.00 28.90 O ANISOU 141 O TRP A 261 3746 3283 3953 -218 -276 -222 O ATOM 142 CB TRP A 261 219.115 33.528 33.429 1.00 23.03 C ANISOU 142 CB TRP A 261 2963 2605 3180 -195 -165 -285 C ATOM 143 CG TRP A 261 219.486 34.889 32.893 1.00 27.13 C ANISOU 143 CG TRP A 261 3482 3161 3666 -203 -102 -270 C ATOM 144 CD1 TRP A 261 220.741 35.304 32.533 1.00 28.14 C ANISOU 144 CD1 TRP A 261 3589 3311 3793 -201 -67 -300 C ATOM 145 CD2 TRP A 261 218.592 35.987 32.578 1.00 25.63 C ANISOU 145 CD2 TRP A 261 3312 2987 3441 -215 -68 -219 C ATOM 146 NE1 TRP A 261 220.689 36.594 32.060 1.00 28.55 N ANISOU 146 NE1 TRP A 261 3648 3391 3808 -215 -16 -270 N ATOM 147 CE2 TRP A 261 219.400 37.034 32.077 1.00 26.99 C ANISOU 147 CE2 TRP A 261 3475 3188 3593 -222 -16 -220 C ATOM 148 CE3 TRP A 261 217.204 36.165 32.648 1.00 27.53 C ANISOU 148 CE3 TRP A 261 3572 3221 3669 -221 -78 -172 C ATOM 149 CZ2 TRP A 261 218.860 38.256 31.664 1.00 31.16 C ANISOU 149 CZ2 TRP A 261 4016 3732 4093 -234 23 -172 C ATOM 150 CZ3 TRP A 261 216.668 37.392 32.245 1.00 29.47 C ANISOU 150 CZ3 TRP A 261 3825 3482 3891 -229 -37 -126 C ATOM 151 CH2 TRP A 261 217.497 38.421 31.763 1.00 29.98 C ANISOU 151 CH2 TRP A 261 3883 3569 3940 -236 11 -125 C ATOM 152 N GLN A 262 218.792 31.133 35.349 1.00 22.99 N ANISOU 152 N GLN A 262 2958 2512 3267 -198 -301 -291 N ATOM 153 CA GLN A 262 218.223 29.809 35.562 1.00 29.43 C ANISOU 153 CA GLN A 262 3780 3294 4108 -194 -368 -298 C ATOM 154 C GLN A 262 217.393 29.759 36.848 1.00 27.85 C ANISOU 154 C GLN A 262 3598 3071 3912 -227 -404 -246 C ATOM 155 O GLN A 262 216.382 29.059 36.900 1.00 25.64 O ANISOU 155 O GLN A 262 3336 2780 3627 -233 -445 -232 O ATOM 156 CB GLN A 262 219.313 28.761 35.741 1.00 32.98 C ANISOU 156 CB GLN A 262 4200 3710 4619 -176 -408 -342 C ATOM 157 CG GLN A 262 220.004 28.246 34.512 1.00 43.24 C ANISOU 157 CG GLN A 262 5478 5020 5930 -142 -392 -408 C ATOM 158 CD GLN A 262 221.148 27.302 34.913 1.00 49.72 C ANISOU 158 CD GLN A 262 6262 5799 6829 -123 -432 -446 C ATOM 159 OE1 GLN A 262 222.324 27.697 34.909 1.00 55.85 O ANISOU 159 OE1 GLN A 262 7007 6586 7628 -114 -403 -468 O ATOM 160 NE2 GLN A 262 220.800 26.065 35.309 1.00 42.91 N ANISOU 160 NE2 GLN A 262 5402 4888 6013 -119 -501 -449 N ATOM 161 N MET A 263 217.873 30.432 37.896 1.00 26.65 N ANISOU 161 N MET A 263 3443 2915 3770 -253 -392 -222 N ATOM 162 CA MET A 263 217.181 30.399 39.183 1.00 28.03 C ANISOU 162 CA MET A 263 3633 3073 3944 -293 -422 -179 C ATOM 163 C MET A 263 215.880 31.194 39.187 1.00 27.44 C ANISOU 163 C MET A 263 3582 3018 3826 -308 -387 -144 C ATOM 164 O MET A 263 214.884 30.724 39.718 1.00 23.74 O ANISOU 164 O MET A 263 3128 2541 3353 -329 -423 -119 O ATOM 165 CB MET A 263 218.078 30.908 40.319 1.00 30.22 C ANISOU 165 CB MET A 263 3901 3345 4239 -326 -417 -166 C ATOM 166 CG MET A 263 219.171 29.938 40.689 1.00 31.64 C ANISOU 166 CG MET A 263 4054 3496 4473 -322 -473 -184 C ATOM 167 SD MET A 263 220.091 30.438 42.170 1.00 38.24 S ANISOU 167 SD MET A 263 4878 4328 5323 -376 -481 -155 S ATOM 168 CE MET A 263 220.518 32.109 41.785 1.00 22.54 C ANISOU 168 CE MET A 263 2893 2377 3294 -375 -383 -162 C ATOM 169 N PHE A 264 215.881 32.385 38.591 1.00 22.05 N ANISOU 169 N PHE A 264 2901 2362 3116 -298 -320 -140 N ATOM 170 CA PHE A 264 214.724 33.282 38.716 1.00 23.44 C ANISOU 170 CA PHE A 264 3092 2549 3263 -311 -283 -103 C ATOM 171 C PHE A 264 213.765 33.189 37.529 1.00 27.84 C ANISOU 171 C PHE A 264 3655 3125 3796 -286 -278 -95 C ATOM 172 O PHE A 264 212.548 33.384 37.668 1.00 25.31 O ANISOU 172 O PHE A 264 3344 2808 3462 -295 -276 -61 O ATOM 173 CB PHE A 264 215.230 34.698 38.917 1.00 26.04 C ANISOU 173 CB PHE A 264 3421 2888 3585 -320 -215 -95 C ATOM 174 CG PHE A 264 215.789 34.925 40.301 1.00 26.98 C ANISOU 174 CG PHE A 264 3541 2993 3719 -361 -217 -91 C ATOM 175 CD1 PHE A 264 217.116 34.648 40.591 1.00 24.54 C ANISOU 175 CD1 PHE A 264 3217 2678 3430 -366 -233 -113 C ATOM 176 CD2 PHE A 264 214.958 35.350 41.320 1.00 24.67 C ANISOU 176 CD2 PHE A 264 3261 2693 3419 -399 -205 -65 C ATOM 177 CE1 PHE A 264 217.621 34.851 41.861 1.00 23.47 C ANISOU 177 CE1 PHE A 264 3081 2533 3303 -412 -239 -104 C ATOM 178 CE2 PHE A 264 215.448 35.545 42.597 1.00 21.60 C ANISOU 178 CE2 PHE A 264 2875 2296 3035 -447 -206 -63 C ATOM 179 CZ PHE A 264 216.766 35.296 42.870 1.00 21.71 C ANISOU 179 CZ PHE A 264 2877 2307 3065 -455 -225 -79 C ATOM 180 N GLY A 265 214.319 32.859 36.362 1.00 27.98 N ANISOU 180 N GLY A 265 3665 3158 3808 -258 -277 -126 N ATOM 181 CA GLY A 265 213.508 32.653 35.162 1.00 25.58 C ANISOU 181 CA GLY A 265 3367 2878 3475 -242 -279 -121 C ATOM 182 C GLY A 265 212.237 31.820 35.375 1.00 27.47 C ANISOU 182 C GLY A 265 3619 3108 3710 -251 -328 -99 C ATOM 183 O GLY A 265 211.174 32.190 34.888 1.00 26.84 O ANISOU 183 O GLY A 265 3545 3048 3606 -252 -316 -65 O ATOM 184 N PRO A 266 212.332 30.661 36.058 1.00 27.43 N ANISOU 184 N PRO A 266 3616 3075 3730 -260 -387 -114 N ATOM 185 CA PRO A 266 211.098 29.866 36.140 1.00 27.00 C ANISOU 185 CA PRO A 266 3576 3017 3666 -272 -433 -93 C ATOM 186 C PRO A 266 209.965 30.511 36.938 1.00 28.78 C ANISOU 186 C PRO A 266 3807 3247 3881 -296 -420 -42 C ATOM 187 O PRO A 266 208.831 30.010 36.848 1.00 27.47 O ANISOU 187 O PRO A 266 3649 3088 3701 -306 -451 -19 O ATOM 188 CB PRO A 266 211.557 28.553 36.794 1.00 29.28 C ANISOU 188 CB PRO A 266 3865 3269 3991 -280 -501 -117 C ATOM 189 CG PRO A 266 213.052 28.466 36.421 1.00 25.37 C ANISOU 189 CG PRO A 266 3353 2764 3523 -256 -488 -166 C ATOM 190 CD PRO A 266 213.517 29.897 36.515 1.00 28.81 C ANISOU 190 CD PRO A 266 3781 3222 3944 -257 -419 -153 C ATOM 191 N PHE A 267 210.248 31.591 37.671 1.00 25.39 N ANISOU 191 N PHE A 267 3372 2816 3458 -308 -373 -28 N ATOM 192 CA PHE A 267 209.222 32.257 38.495 1.00 29.18 C ANISOU 192 CA PHE A 267 3854 3299 3934 -333 -351 11 C ATOM 193 C PHE A 267 208.367 33.349 37.826 1.00 32.03 C ANISOU 193 C PHE A 267 4209 3680 4282 -318 -299 44 C ATOM 194 O PHE A 267 207.311 33.754 38.355 1.00 28.61 O ANISOU 194 O PHE A 267 3771 3248 3850 -333 -285 75 O ATOM 195 CB PHE A 267 209.832 32.771 39.818 1.00 24.69 C ANISOU 195 CB PHE A 267 3286 2715 3382 -364 -331 7 C ATOM 196 CG PHE A 267 210.311 31.659 40.712 1.00 26.92 C ANISOU 196 CG PHE A 267 3573 2978 3679 -392 -395 -6 C ATOM 197 CD1 PHE A 267 209.403 30.935 41.490 1.00 29.47 C ANISOU 197 CD1 PHE A 267 3903 3296 3997 -426 -441 14 C ATOM 198 CD2 PHE A 267 211.658 31.297 40.742 1.00 24.06 C ANISOU 198 CD2 PHE A 267 3204 2601 3338 -385 -413 -35 C ATOM 199 CE1 PHE A 267 209.830 29.890 42.302 1.00 28.63 C ANISOU 199 CE1 PHE A 267 3801 3171 3907 -457 -508 10 C ATOM 200 CE2 PHE A 267 212.098 30.271 41.571 1.00 28.37 C ANISOU 200 CE2 PHE A 267 3749 3124 3905 -411 -478 -39 C ATOM 201 CZ PHE A 267 211.178 29.550 42.343 1.00 30.13 C ANISOU 201 CZ PHE A 267 3983 3341 4123 -448 -528 -15 C ATOM 202 N GLY A 268 208.803 33.845 36.681 1.00 29.45 N ANISOU 202 N GLY A 268 3877 3369 3944 -291 -270 39 N ATOM 203 CA GLY A 268 208.044 34.880 36.018 1.00 27.31 C ANISOU 203 CA GLY A 268 3597 3114 3666 -279 -228 78 C ATOM 204 C GLY A 268 208.973 35.751 35.197 1.00 29.15 C ANISOU 204 C GLY A 268 3825 3358 3892 -262 -184 69 C ATOM 205 O GLY A 268 210.161 35.422 35.032 1.00 30.70 O ANISOU 205 O GLY A 268 4023 3554 4086 -257 -188 29 O ATOM 206 N ALA A 269 208.455 36.885 34.736 1.00 26.91 N ANISOU 206 N ALA A 269 3532 3081 3611 -254 -141 109 N ATOM 207 CA ALA A 269 209.231 37.799 33.904 1.00 27.68 C ANISOU 207 CA ALA A 269 3625 3192 3701 -243 -100 111 C ATOM 208 C ALA A 269 210.430 38.385 34.666 1.00 26.55 C ANISOU 208 C ALA A 269 3485 3029 3574 -250 -64 81 C ATOM 209 O ALA A 269 210.293 39.005 35.721 1.00 29.65 O ANISOU 209 O ALA A 269 3878 3395 3992 -263 -36 87 O ATOM 210 CB ALA A 269 208.368 38.891 33.358 1.00 26.24 C ANISOU 210 CB ALA A 269 3431 3014 3526 -236 -69 169 C ATOM 211 N VAL A 270 211.608 38.172 34.090 1.00 27.21 N ANISOU 211 N VAL A 270 3569 3128 3641 -246 -64 46 N ATOM 212 CA VAL A 270 212.871 38.698 34.579 1.00 26.33 C ANISOU 212 CA VAL A 270 3457 3007 3541 -253 -33 18 C ATOM 213 C VAL A 270 213.433 39.604 33.469 1.00 26.70 C ANISOU 213 C VAL A 270 3498 3079 3567 -246 6 27 C ATOM 214 O VAL A 270 213.546 39.181 32.301 1.00 25.83 O ANISOU 214 O VAL A 270 3384 3002 3427 -239 -9 19 O ATOM 215 CB VAL A 270 213.860 37.544 34.864 1.00 27.36 C ANISOU 215 CB VAL A 270 3586 3136 3672 -253 -71 -34 C ATOM 216 CG1 VAL A 270 215.256 38.093 35.244 1.00 24.88 C ANISOU 216 CG1 VAL A 270 3266 2819 3367 -261 -40 -60 C ATOM 217 CG2 VAL A 270 213.303 36.604 35.978 1.00 28.97 C ANISOU 217 CG2 VAL A 270 3796 3315 3895 -267 -118 -37 C ATOM 218 N THR A 271 213.740 40.852 33.794 1.00 24.43 N ANISOU 218 N THR A 271 3211 2776 3294 -254 55 45 N ATOM 219 CA THR A 271 214.209 41.771 32.752 1.00 28.93 C ANISOU 219 CA THR A 271 3777 3369 3845 -253 89 63 C ATOM 220 C THR A 271 215.720 41.964 32.753 1.00 32.26 C ANISOU 220 C THR A 271 4196 3803 4258 -262 110 23 C ATOM 221 O THR A 271 216.304 42.374 31.751 1.00 32.45 O ANISOU 221 O THR A 271 4215 3860 4256 -265 127 23 O ATOM 222 CB THR A 271 213.521 43.136 32.861 1.00 31.08 C ANISOU 222 CB THR A 271 4048 3617 4142 -256 130 116 C ATOM 223 OG1 THR A 271 213.619 43.601 34.203 1.00 32.87 O ANISOU 223 OG1 THR A 271 4282 3804 4403 -267 156 106 O ATOM 224 CG2 THR A 271 212.041 43.001 32.513 1.00 27.95 C ANISOU 224 CG2 THR A 271 3646 3219 3754 -244 108 163 C ATOM 225 N ASN A 272 216.362 41.640 33.865 1.00 30.27 N ANISOU 225 N ASN A 272 3946 3531 4025 -270 105 -10 N ATOM 226 CA ASN A 272 217.775 41.970 34.020 1.00 32.68 C ANISOU 226 CA ASN A 272 4245 3844 4327 -282 129 -41 C ATOM 227 C ASN A 272 218.352 41.166 35.167 1.00 31.73 C ANISOU 227 C ASN A 272 4122 3705 4227 -291 101 -75 C ATOM 228 O ASN A 272 217.654 40.922 36.158 1.00 28.65 O ANISOU 228 O ASN A 272 3742 3288 3856 -301 85 -65 O ATOM 229 CB ASN A 272 217.902 43.460 34.343 1.00 36.78 C ANISOU 229 CB ASN A 272 4773 4345 4856 -299 183 -12 C ATOM 230 CG ASN A 272 219.351 43.905 34.520 1.00 46.96 C ANISOU 230 CG ASN A 272 6058 5646 6140 -316 209 -38 C ATOM 231 OD1 ASN A 272 220.046 44.199 33.543 1.00 47.67 O ANISOU 231 OD1 ASN A 272 6138 5769 6204 -315 224 -44 O ATOM 232 ND2 ASN A 272 219.810 43.959 35.772 1.00 50.68 N ANISOU 232 ND2 ASN A 272 6534 6093 6631 -337 213 -54 N ATOM 233 N VAL A 273 219.612 40.753 35.034 1.00 27.09 N ANISOU 233 N VAL A 273 3520 3135 3638 -290 94 -114 N ATOM 234 CA VAL A 273 220.354 40.114 36.128 1.00 28.27 C ANISOU 234 CA VAL A 273 3661 3268 3812 -303 67 -140 C ATOM 235 C VAL A 273 221.767 40.665 36.157 1.00 33.20 C ANISOU 235 C VAL A 273 4271 3908 4435 -316 96 -160 C ATOM 236 O VAL A 273 222.286 41.160 35.145 1.00 32.25 O ANISOU 236 O VAL A 273 4142 3818 4292 -308 126 -167 O ATOM 237 CB VAL A 273 220.447 38.547 36.019 1.00 24.65 C ANISOU 237 CB VAL A 273 3188 2808 3369 -283 6 -173 C ATOM 238 CG1 VAL A 273 219.059 37.899 35.838 1.00 25.09 C ANISOU 238 CG1 VAL A 273 3258 2854 3422 -272 -27 -155 C ATOM 239 CG2 VAL A 273 221.386 38.106 34.881 1.00 27.58 C ANISOU 239 CG2 VAL A 273 3536 3211 3733 -261 8 -215 C ATOM 240 N LYS A 274 222.429 40.557 37.302 1.00 28.94 N ANISOU 240 N LYS A 274 3728 3352 3916 -340 84 -167 N ATOM 241 CA LYS A 274 223.772 41.101 37.378 1.00 29.45 C ANISOU 241 CA LYS A 274 3777 3433 3979 -356 110 -182 C ATOM 242 C LYS A 274 224.561 40.407 38.460 1.00 28.99 C ANISOU 242 C LYS A 274 3702 3363 3949 -376 71 -195 C ATOM 243 O LYS A 274 224.098 40.301 39.598 1.00 27.21 O ANISOU 243 O LYS A 274 3492 3112 3734 -404 52 -177 O ATOM 244 CB LYS A 274 223.709 42.601 37.666 1.00 32.34 C ANISOU 244 CB LYS A 274 4165 3794 4329 -386 168 -154 C ATOM 245 CG LYS A 274 225.085 43.260 37.946 1.00 35.59 C ANISOU 245 CG LYS A 274 4565 4221 4737 -413 196 -164 C ATOM 246 CD LYS A 274 225.879 43.466 36.665 1.00 40.91 C ANISOU 246 CD LYS A 274 5217 4935 5390 -395 218 -182 C ATOM 247 N VAL A 275 225.744 39.916 38.118 1.00 26.30 N ANISOU 247 N VAL A 275 3327 3041 3623 -363 58 -226 N ATOM 248 CA VAL A 275 226.614 39.350 39.150 1.00 25.78 C ANISOU 248 CA VAL A 275 3241 2964 3591 -384 19 -230 C ATOM 249 C VAL A 275 227.629 40.433 39.537 1.00 29.83 C ANISOU 249 C VAL A 275 3749 3494 4090 -421 61 -223 C ATOM 250 O VAL A 275 228.218 41.078 38.662 1.00 28.84 O ANISOU 250 O VAL A 275 3615 3399 3945 -411 104 -236 O ATOM 251 CB VAL A 275 227.300 38.033 38.624 1.00 34.38 C ANISOU 251 CB VAL A 275 4287 4056 4719 -346 -26 -269 C ATOM 252 CG1 VAL A 275 228.408 37.558 39.540 1.00 33.62 C ANISOU 252 CG1 VAL A 275 4158 3951 4665 -365 -65 -269 C ATOM 253 CG2 VAL A 275 226.254 36.924 38.417 1.00 28.47 C ANISOU 253 CG2 VAL A 275 3548 3284 3986 -318 -73 -274 C ATOM 254 N ILE A 276 227.846 40.663 40.828 1.00 28.25 N ANISOU 254 N ILE A 276 3625 3443 3665 -600 213 -114 N ATOM 255 CA ILE A 276 228.842 41.662 41.209 1.00 29.62 C ANISOU 255 CA ILE A 276 3755 3560 3939 -671 222 -95 C ATOM 256 C ILE A 276 230.216 41.009 41.382 1.00 29.84 C ANISOU 256 C ILE A 276 3677 3598 4063 -708 204 -52 C ATOM 257 O ILE A 276 230.348 39.998 42.063 1.00 30.62 O ANISOU 257 O ILE A 276 3741 3739 4154 -723 133 -67 O ATOM 258 CB ILE A 276 228.426 42.427 42.487 1.00 35.09 C ANISOU 258 CB ILE A 276 4493 4218 4620 -748 157 -150 C ATOM 259 CG1 ILE A 276 227.034 43.059 42.295 1.00 36.35 C ANISOU 259 CG1 ILE A 276 4746 4364 4702 -694 198 -173 C ATOM 260 CG2 ILE A 276 229.472 43.473 42.876 1.00 35.44 C ANISOU 260 CG2 ILE A 276 4512 4195 4757 -843 153 -128 C ATOM 261 CD1 ILE A 276 226.864 43.809 40.970 1.00 37.91 C ANISOU 261 CD1 ILE A 276 4965 4536 4904 -630 297 -124 C ATOM 262 N ARG A 277 231.236 41.579 40.752 1.00 27.46 N ANISOU 262 N ARG A 277 3317 3255 3861 -718 273 14 N ATOM 263 CA ARG A 277 232.569 40.970 40.768 1.00 33.28 C ANISOU 263 CA ARG A 277 3932 3998 4714 -737 278 84 C ATOM 264 C ARG A 277 233.555 41.943 41.327 1.00 31.89 C ANISOU 264 C ARG A 277 3681 3776 4660 -845 241 124 C ATOM 265 O ARG A 277 233.380 43.151 41.206 1.00 30.15 O ANISOU 265 O ARG A 277 3511 3504 4440 -879 266 112 O ATOM 266 CB ARG A 277 233.047 40.660 39.343 1.00 33.90 C ANISOU 266 CB ARG A 277 3998 4060 4821 -643 421 155 C ATOM 267 CG ARG A 277 232.181 39.650 38.632 1.00 36.87 C ANISOU 267 CG ARG A 277 4468 4470 5069 -547 460 127 C ATOM 268 CD ARG A 277 232.609 39.529 37.153 1.00 42.58 C ANISOU 268 CD ARG A 277 5226 5152 5799 -461 615 194 C ATOM 269 NE ARG A 277 231.575 38.807 36.434 1.00 46.72 N ANISOU 269 NE ARG A 277 5884 5697 6170 -391 634 159 N ATOM 270 CZ ARG A 277 231.380 37.504 36.554 1.00 47.88 C ANISOU 270 CZ ARG A 277 6057 5880 6254 -362 611 144 C ATOM 271 NH1 ARG A 277 232.190 36.800 37.335 1.00 49.35 N ANISOU 271 NH1 ARG A 277 6138 6086 6526 -383 581 165 N ATOM 272 NH2 ARG A 277 230.389 36.908 35.889 1.00 43.27 N ANISOU 272 NH2 ARG A 277 5607 5310 5523 -317 614 115 N ATOM 273 N ASP A 278 234.637 41.415 41.867 1.00 33.55 N ANISOU 273 N ASP A 278 3766 4001 4980 -899 184 185 N ATOM 274 CA ASP A 278 235.786 42.240 42.163 1.00 33.78 C ANISOU 274 CA ASP A 278 3696 3987 5153 -1004 154 258 C ATOM 275 C ASP A 278 236.466 42.577 40.843 1.00 35.61 C ANISOU 275 C ASP A 278 3871 4183 5478 -937 311 346 C ATOM 276 O ASP A 278 236.891 41.677 40.128 1.00 34.86 O ANISOU 276 O ASP A 278 3717 4105 5424 -845 403 408 O ATOM 277 CB ASP A 278 236.742 41.448 43.046 1.00 37.47 C ANISOU 277 CB ASP A 278 4027 4489 5722 -1073 44 321 C ATOM 278 CG ASP A 278 237.933 42.268 43.486 1.00 43.89 C ANISOU 278 CG ASP A 278 4726 5261 6690 -1208 -23 410 C ATOM 279 OD1 ASP A 278 238.564 42.914 42.621 1.00 44.96 O ANISOU 279 OD1 ASP A 278 4801 5355 6927 -1194 82 485 O ATOM 280 OD2 ASP A 278 238.220 42.274 44.695 1.00 46.96 O ANISOU 280 OD2 ASP A 278 5094 5656 7094 -1335 -186 407 O ATOM 281 N PHE A 279 236.599 43.865 40.525 1.00 33.09 N ANISOU 281 N PHE A 279 3579 3802 5191 -981 352 355 N ATOM 282 CA PHE A 279 237.133 44.265 39.223 1.00 33.71 C ANISOU 282 CA PHE A 279 3628 3838 5344 -911 515 432 C ATOM 283 C PHE A 279 238.554 43.751 38.999 1.00 38.92 C ANISOU 283 C PHE A 279 4105 4495 6187 -912 562 567 C ATOM 284 O PHE A 279 238.918 43.406 37.878 1.00 38.25 O ANISOU 284 O PHE A 279 4001 4390 6142 -805 721 633 O ATOM 285 CB PHE A 279 237.081 45.783 39.039 1.00 31.29 C ANISOU 285 CB PHE A 279 3378 3462 5049 -972 542 421 C ATOM 286 CG PHE A 279 237.680 46.270 37.737 1.00 32.03 C ANISOU 286 CG PHE A 279 3443 3504 5223 -908 711 503 C ATOM 287 CD1 PHE A 279 236.928 46.318 36.565 1.00 32.92 C ANISOU 287 CD1 PHE A 279 3676 3601 5231 -784 840 476 C ATOM 288 CD2 PHE A 279 239.014 46.678 37.685 1.00 34.31 C ANISOU 288 CD2 PHE A 279 3584 3755 5698 -976 736 616 C ATOM 289 CE1 PHE A 279 237.513 46.772 35.343 1.00 32.22 C ANISOU 289 CE1 PHE A 279 3579 3455 5211 -725 1005 554 C ATOM 290 CE2 PHE A 279 239.588 47.120 36.507 1.00 34.23 C ANISOU 290 CE2 PHE A 279 3547 3690 5769 -915 904 697 C ATOM 291 CZ PHE A 279 238.835 47.183 35.329 1.00 38.31 C ANISOU 291 CZ PHE A 279 4203 4184 6168 -787 1045 661 C ATOM 292 N ASN A 280 239.351 43.690 40.059 1.00 37.69 N ANISOU 292 N ASN A 280 3822 4355 6143 -1032 426 618 N ATOM 293 CA ASN A 280 240.744 43.313 39.906 1.00 44.26 C ANISOU 293 CA ASN A 280 4453 5183 7179 -1043 463 772 C ATOM 294 C ASN A 280 241.070 41.813 39.902 1.00 47.63 C ANISOU 294 C ASN A 280 4794 5661 7644 -953 491 829 C ATOM 295 O ASN A 280 242.184 41.423 39.533 1.00 53.37 O ANISOU 295 O ASN A 280 5356 6375 8546 -920 574 974 O ATOM 296 CB ASN A 280 241.618 44.112 40.879 1.00 45.67 C ANISOU 296 CB ASN A 280 4517 5343 7493 -1227 310 836 C ATOM 297 CG ASN A 280 241.544 45.613 40.605 1.00 45.25 C ANISOU 297 CG ASN A 280 4539 5219 7436 -1301 336 812 C ATOM 298 OD1 ASN A 280 241.962 46.081 39.544 1.00 43.29 O ANISOU 298 OD1 ASN A 280 4258 4925 7265 -1241 494 878 O ATOM 299 ND2 ASN A 280 240.964 46.369 41.546 1.00 41.77 N ANISOU 299 ND2 ASN A 280 4219 4759 6893 -1424 196 713 N ATOM 300 N THR A 281 240.110 40.972 40.268 1.00 41.15 N ANISOU 300 N THR A 281 4081 4889 6664 -905 437 725 N ATOM 301 CA THR A 281 240.301 39.521 40.187 1.00 41.46 C ANISOU 301 CA THR A 281 4071 4968 6714 -809 480 767 C ATOM 302 C THR A 281 239.320 38.897 39.208 1.00 41.63 C ANISOU 302 C THR A 281 4263 4988 6567 -666 612 689 C ATOM 303 O THR A 281 239.478 37.749 38.816 1.00 44.87 O ANISOU 303 O THR A 281 4668 5408 6972 -567 699 727 O ATOM 304 CB THR A 281 240.127 38.821 41.564 1.00 44.21 C ANISOU 304 CB THR A 281 4391 5379 7029 -885 288 727 C ATOM 305 OG1 THR A 281 238.768 38.935 42.002 1.00 44.33 O ANISOU 305 OG1 THR A 281 4585 5416 6843 -899 207 568 O ATOM 306 CG2 THR A 281 241.036 39.450 42.603 1.00 45.56 C ANISOU 306 CG2 THR A 281 4420 5548 7344 -1050 125 802 C ATOM 307 N ASN A 282 238.312 39.673 38.821 1.00 36.21 N ANISOU 307 N ASN A 282 3731 4285 5742 -663 622 587 N ATOM 308 CA ASN A 282 237.140 39.181 38.087 1.00 37.49 C ANISOU 308 CA ASN A 282 4070 4455 5717 -562 687 500 C ATOM 309 C ASN A 282 236.345 38.074 38.761 1.00 40.06 C ANISOU 309 C ASN A 282 4455 4845 5923 -548 589 422 C ATOM 310 O ASN A 282 235.504 37.449 38.134 1.00 42.94 O ANISOU 310 O ASN A 282 4949 5217 6147 -468 641 371 O ATOM 311 CB ASN A 282 237.488 38.755 36.658 1.00 42.70 C ANISOU 311 CB ASN A 282 4777 5066 6383 -438 892 568 C ATOM 312 CG ASN A 282 237.966 39.922 35.797 1.00 44.71 C ANISOU 312 CG ASN A 282 5025 5251 6713 -435 1009 624 C ATOM 313 N LYS A 283 236.574 37.847 40.048 1.00 40.86 N ANISOU 313 N LYS A 283 4470 4986 6070 -635 440 413 N ATOM 314 CA LYS A 283 235.757 36.872 40.771 1.00 39.35 C ANISOU 314 CA LYS A 283 4341 4852 5759 -628 343 331 C ATOM 315 C LYS A 283 234.455 37.497 41.281 1.00 35.78 C ANISOU 315 C LYS A 283 4014 4413 5166 -674 249 210 C ATOM 316 O LYS A 283 234.413 38.680 41.637 1.00 33.77 O ANISOU 316 O LYS A 283 3766 4130 4934 -751 204 191 O ATOM 317 CB LYS A 283 236.519 36.275 41.959 1.00 41.59 C ANISOU 317 CB LYS A 283 4492 5170 6141 -697 222 376 C ATOM 318 CG LYS A 283 237.842 35.602 41.619 1.00 47.80 C ANISOU 318 CG LYS A 283 5124 5945 7092 -651 309 519 C ATOM 319 CD LYS A 283 237.649 34.542 40.529 1.00 54.79 C ANISOU 319 CD LYS A 283 6088 6817 7911 -505 477 532 C ATOM 320 CE LYS A 283 238.374 33.243 40.897 1.00 60.94 C ANISOU 320 CE LYS A 283 6766 7617 8770 -461 489 614 C ATOM 321 NZ LYS A 283 238.409 32.276 39.757 1.00 64.16 N ANISOU 321 NZ LYS A 283 7259 7987 9133 -319 686 650 N ATOM 322 N CYS A 284 233.417 36.679 41.371 1.00 33.31 N ANISOU 322 N CYS A 284 3800 4141 4717 -628 222 136 N ATOM 323 CA CYS A 284 232.164 37.122 41.975 1.00 32.91 C ANISOU 323 CA CYS A 284 3850 4107 4549 -663 137 36 C ATOM 324 C CYS A 284 232.412 37.383 43.446 1.00 33.25 C ANISOU 324 C CYS A 284 3849 4155 4630 -774 -2 10 C ATOM 325 O CYS A 284 233.009 36.551 44.132 1.00 35.59 O ANISOU 325 O CYS A 284 4070 4479 4972 -800 -68 36 O ATOM 326 CB CYS A 284 231.080 36.052 41.811 1.00 32.72 C ANISOU 326 CB CYS A 284 3919 4127 4387 -598 130 -21 C ATOM 327 SG CYS A 284 229.459 36.471 42.569 1.00 31.67 S ANISOU 327 SG CYS A 284 3891 4014 4127 -627 40 -123 S ATOM 328 N LYS A 285 231.960 38.527 43.941 1.00 30.51 N ANISOU 328 N LYS A 285 3559 3773 4259 -840 -43 -36 N ATOM 329 CA LYS A 285 232.072 38.820 45.375 1.00 32.45 C ANISOU 329 CA LYS A 285 3813 4007 4509 -955 -175 -72 C ATOM 330 C LYS A 285 231.050 38.079 46.261 1.00 35.84 C ANISOU 330 C LYS A 285 4323 4471 4821 -950 -248 -154 C ATOM 331 O LYS A 285 231.030 38.256 47.475 1.00 37.33 O ANISOU 331 O LYS A 285 4550 4642 4990 -1040 -350 -192 O ATOM 332 CB LYS A 285 231.988 40.325 45.611 1.00 39.05 C ANISOU 332 CB LYS A 285 4711 4774 5353 -1031 -177 -91 C ATOM 333 CG LYS A 285 233.267 41.055 45.225 1.00 44.98 C ANISOU 333 CG LYS A 285 5363 5485 6243 -1090 -156 -4 C ATOM 334 CD LYS A 285 233.266 42.511 45.677 1.00 53.36 C ANISOU 334 CD LYS A 285 6500 6468 7306 -1193 -180 -26 C ATOM 335 CE LYS A 285 232.133 43.306 45.030 1.00 58.50 C ANISOU 335 CE LYS A 285 7272 7086 7868 -1118 -74 -79 C ATOM 336 NZ LYS A 285 232.203 44.771 45.363 1.00 63.27 N ANISOU 336 NZ LYS A 285 7958 7600 8479 -1209 -71 -93 N ATOM 337 N GLY A 286 230.218 37.246 45.652 1.00 31.94 N ANISOU 337 N GLY A 286 3866 4021 4248 -850 -195 -179 N ATOM 338 CA GLY A 286 229.307 36.400 46.395 1.00 33.95 C ANISOU 338 CA GLY A 286 4181 4315 4405 -839 -256 -243 C ATOM 339 C GLY A 286 227.850 36.776 46.235 1.00 33.36 C ANISOU 339 C GLY A 286 4210 4235 4229 -795 -221 -299 C ATOM 340 O GLY A 286 226.979 36.081 46.734 1.00 32.59 O ANISOU 340 O GLY A 286 4158 4169 4054 -777 -256 -345 O ATOM 341 N PHE A 287 227.577 37.887 45.557 1.00 29.45 N ANISOU 341 N PHE A 287 4492 2817 3879 -687 633 -486 N ATOM 342 CA PHE A 287 226.196 38.360 45.463 1.00 30.36 C ANISOU 342 CA PHE A 287 4631 2837 4069 -651 648 -458 C ATOM 343 C PHE A 287 225.874 38.938 44.093 1.00 29.05 C ANISOU 343 C PHE A 287 4525 2571 3942 -650 649 -356 C ATOM 344 O PHE A 287 226.785 39.219 43.276 1.00 26.05 O ANISOU 344 O PHE A 287 4169 2185 3544 -681 647 -314 O ATOM 345 CB PHE A 287 225.861 39.348 46.579 1.00 28.01 C ANISOU 345 CB PHE A 287 4313 2479 3849 -608 688 -526 C ATOM 346 CG PHE A 287 226.703 40.600 46.574 1.00 33.88 C ANISOU 346 CG PHE A 287 5074 3152 4648 -615 709 -536 C ATOM 347 CD1 PHE A 287 227.889 40.656 47.307 1.00 36.02 C ANISOU 347 CD1 PHE A 287 5308 3488 4889 -643 708 -599 C ATOM 348 CD2 PHE A 287 226.302 41.730 45.874 1.00 33.42 C ANISOU 348 CD2 PHE A 287 5069 2957 4671 -593 729 -479 C ATOM 349 CE1 PHE A 287 228.674 41.801 47.319 1.00 33.92 C ANISOU 349 CE1 PHE A 287 5058 3154 4676 -664 726 -612 C ATOM 350 CE2 PHE A 287 227.080 42.893 45.884 1.00 37.10 C ANISOU 350 CE2 PHE A 287 5557 3353 5188 -610 745 -488 C ATOM 351 CZ PHE A 287 228.277 42.927 46.615 1.00 33.59 C ANISOU 351 CZ PHE A 287 5074 2974 4716 -653 744 -559 C ATOM 352 N GLY A 288 224.576 39.093 43.859 1.00 25.95 N ANISOU 352 N GLY A 288 4148 2115 3597 -605 651 -311 N ATOM 353 CA GLY A 288 224.053 39.541 42.587 1.00 28.71 C ANISOU 353 CA GLY A 288 4524 2421 3963 -559 626 -189 C ATOM 354 C GLY A 288 222.665 40.124 42.776 1.00 30.77 C ANISOU 354 C GLY A 288 4750 2655 4286 -457 620 -159 C ATOM 355 O GLY A 288 222.116 40.132 43.906 1.00 27.69 O ANISOU 355 O GLY A 288 4310 2289 3923 -424 638 -233 O ATOM 356 N PHE A 289 222.124 40.640 41.673 1.00 26.24 N ANISOU 356 N PHE A 289 4202 2038 3730 -398 596 -51 N ATOM 357 CA PHE A 289 220.826 41.302 41.672 1.00 24.96 C ANISOU 357 CA PHE A 289 4011 1849 3623 -284 587 -12 C ATOM 358 C PHE A 289 220.023 40.809 40.495 1.00 29.74 C ANISOU 358 C PHE A 289 4593 2525 4181 -237 516 97 C ATOM 359 O PHE A 289 220.587 40.549 39.429 1.00 26.52 O ANISOU 359 O PHE A 289 4233 2119 3724 -273 491 164 O ATOM 360 CB PHE A 289 220.983 42.805 41.531 1.00 24.63 C ANISOU 360 CB PHE A 289 4047 1643 3667 -236 636 7 C ATOM 361 CG PHE A 289 221.736 43.413 42.654 1.00 30.07 C ANISOU 361 CG PHE A 289 4764 2249 4412 -280 700 -105 C ATOM 362 CD1 PHE A 289 221.166 43.517 43.908 1.00 30.70 C ANISOU 362 CD1 PHE A 289 4791 2349 4523 -232 719 -198 C ATOM 363 CD2 PHE A 289 223.047 43.813 42.480 1.00 34.81 C ANISOU 363 CD2 PHE A 289 5436 2765 5025 -374 740 -123 C ATOM 364 CE1 PHE A 289 221.867 44.036 44.960 1.00 35.69 C ANISOU 364 CE1 PHE A 289 5450 2911 5199 -268 771 -310 C ATOM 365 CE2 PHE A 289 223.752 44.339 43.546 1.00 37.20 C ANISOU 365 CE2 PHE A 289 5736 3035 5365 -411 774 -232 C ATOM 366 CZ PHE A 289 223.165 44.448 44.779 1.00 33.90 C ANISOU 366 CZ PHE A 289 5284 2616 4982 -360 794 -328 C ATOM 367 N VAL A 290 218.712 40.715 40.670 1.00 24.57 N ANISOU 367 N VAL A 290 3862 1934 3539 -154 484 113 N ATOM 368 CA VAL A 290 217.836 40.299 39.572 1.00 22.74 C ANISOU 368 CA VAL A 290 3597 1776 3266 -101 408 210 C ATOM 369 C VAL A 290 216.668 41.272 39.622 1.00 31.75 C ANISOU 369 C VAL A 290 4708 2886 4470 33 412 240 C ATOM 370 O VAL A 290 216.247 41.669 40.710 1.00 29.74 O ANISOU 370 O VAL A 290 4411 2624 4265 73 452 171 O ATOM 371 CB VAL A 290 217.330 38.849 39.873 1.00 35.42 C ANISOU 371 CB VAL A 290 5112 3540 4808 -153 352 185 C ATOM 372 CG1 VAL A 290 216.079 38.475 39.080 1.00 33.55 C ANISOU 372 CG1 VAL A 290 4805 3396 4547 -89 272 261 C ATOM 373 CG2 VAL A 290 218.454 37.842 39.684 1.00 30.07 C ANISOU 373 CG2 VAL A 290 4477 2893 4055 -268 337 163 C ATOM 374 N THR A 291 216.123 41.652 38.476 1.00 28.23 N ANISOU 374 N THR A 291 4282 2429 4017 115 369 340 N ATOM 375 CA THR A 291 214.971 42.546 38.444 1.00 28.69 C ANISOU 375 CA THR A 291 4311 2468 4124 260 363 372 C ATOM 376 C THR A 291 213.787 41.796 37.828 1.00 28.90 C ANISOU 376 C THR A 291 4233 2646 4102 311 276 426 C ATOM 377 O THR A 291 213.909 41.246 36.731 1.00 25.74 O ANISOU 377 O THR A 291 3851 2287 3641 288 216 494 O ATOM 378 CB THR A 291 215.301 43.801 37.599 1.00 34.34 C ANISOU 378 CB THR A 291 5149 3026 4873 333 387 448 C ATOM 379 OG1 THR A 291 216.415 44.496 38.186 1.00 36.13 O ANISOU 379 OG1 THR A 291 5469 3109 5150 268 466 394 O ATOM 380 CG2 THR A 291 214.111 44.722 37.488 1.00 34.30 C ANISOU 380 CG2 THR A 291 5126 2999 4909 501 375 486 C ATOM 381 N MET A 292 212.668 41.756 38.550 1.00 27.99 N ANISOU 381 N MET A 292 4004 2622 4011 376 269 390 N ATOM 382 CA MET A 292 211.455 41.069 38.109 1.00 26.83 C ANISOU 382 CA MET A 292 3736 2633 3827 418 188 430 C ATOM 383 C MET A 292 210.316 42.066 38.008 1.00 30.06 C ANISOU 383 C MET A 292 4100 3045 4275 591 182 462 C ATOM 384 O MET A 292 210.209 42.983 38.814 1.00 31.97 O ANISOU 384 O MET A 292 4358 3214 4574 666 245 417 O ATOM 385 CB MET A 292 211.089 39.904 39.052 1.00 26.08 C ANISOU 385 CB MET A 292 3521 2678 3710 323 180 363 C ATOM 386 CG MET A 292 212.080 38.736 38.951 1.00 27.94 C ANISOU 386 CG MET A 292 3800 2930 3888 165 162 344 C ATOM 387 SD MET A 292 211.629 37.317 39.946 1.00 27.83 S ANISOU 387 SD MET A 292 3666 3067 3841 53 146 282 S ATOM 388 CE MET A 292 210.338 36.575 38.919 1.00 24.99 C ANISOU 388 CE MET A 292 3197 2857 3442 73 30 355 C ATOM 389 N THR A 293 209.459 41.878 37.012 1.00 30.08 N ANISOU 389 N THR A 293 4050 3138 4243 662 101 535 N ATOM 390 CA THR A 293 208.464 42.880 36.670 1.00 31.59 C ANISOU 390 CA THR A 293 4218 3327 4458 845 86 578 C ATOM 391 C THR A 293 207.283 42.865 37.646 1.00 33.36 C ANISOU 391 C THR A 293 4286 3682 4709 914 93 524 C ATOM 392 O THR A 293 206.709 43.900 37.971 1.00 37.68 O ANISOU 392 O THR A 293 4830 4192 5296 1064 123 517 O ATOM 393 CB THR A 293 207.945 42.589 35.253 1.00 34.71 C ANISOU 393 CB THR A 293 4598 3796 4796 898 -12 671 C ATOM 394 OG1 THR A 293 209.067 42.500 34.368 1.00 36.51 O ANISOU 394 OG1 THR A 293 4964 3921 4989 828 -16 721 O ATOM 395 CG2 THR A 293 206.945 43.669 34.779 1.00 33.04 C ANISOU 395 CG2 THR A 293 4375 3579 4599 1106 -35 724 C ATOM 396 N ASN A 294 206.917 41.676 38.101 1.00 32.09 N ANISOU 396 N ASN A 294 3997 3675 4521 805 66 488 N ATOM 397 CA ASN A 294 205.663 41.503 38.828 1.00 32.47 C ANISOU 397 CA ASN A 294 3871 3886 4579 862 62 455 C ATOM 398 C ASN A 294 205.931 41.229 40.313 1.00 30.87 C ANISOU 398 C ASN A 294 3630 3696 4401 782 143 363 C ATOM 399 O ASN A 294 206.663 40.304 40.641 1.00 29.56 O ANISOU 399 O ASN A 294 3486 3532 4213 623 153 333 O ATOM 400 CB ASN A 294 204.881 40.373 38.178 1.00 34.32 C ANISOU 400 CB ASN A 294 3977 4300 4764 801 -36 492 C ATOM 401 CG ASN A 294 204.472 40.721 36.754 1.00 39.85 C ANISOU 401 CG ASN A 294 4701 5006 5435 908 -120 576 C ATOM 402 OD1 ASN A 294 203.884 41.773 36.528 1.00 39.93 O ANISOU 402 OD1 ASN A 294 4711 4994 5465 1084 -118 603 O ATOM 403 ND2 ASN A 294 204.844 39.882 35.788 1.00 39.63 N ANISOU 403 ND2 ASN A 294 4708 4995 5354 813 -195 617 N ATOM 404 N TYR A 295 205.335 42.035 41.193 1.00 35.47 N ANISOU 404 N TYR A 295 4161 4292 5023 904 199 320 N ATOM 405 CA TYR A 295 205.628 41.952 42.636 1.00 35.41 C ANISOU 405 CA TYR A 295 4134 4284 5036 855 283 229 C ATOM 406 C TYR A 295 205.376 40.540 43.169 1.00 32.39 C ANISOU 406 C TYR A 295 3628 4064 4616 702 271 208 C ATOM 407 O TYR A 295 206.200 39.990 43.901 1.00 30.20 O ANISOU 407 O TYR A 295 3395 3750 4329 578 315 156 O ATOM 408 CB TYR A 295 204.813 42.984 43.455 1.00 39.12 C ANISOU 408 CB TYR A 295 4546 4777 5542 1031 334 187 C ATOM 409 CG TYR A 295 205.207 43.003 44.927 1.00 43.44 C ANISOU 409 CG TYR A 295 5091 5308 6105 994 423 90 C ATOM 410 CD1 TYR A 295 206.334 43.700 45.359 1.00 42.59 C ANISOU 410 CD1 TYR A 295 5141 5008 6031 985 481 35 C ATOM 411 CD2 TYR A 295 204.475 42.303 45.874 1.00 51.65 C ANISOU 411 CD2 TYR A 295 5973 6528 7123 963 447 53 C ATOM 412 CE1 TYR A 295 206.712 43.712 46.698 1.00 46.76 C ANISOU 412 CE1 TYR A 295 5670 5527 6568 957 555 -60 C ATOM 413 CE2 TYR A 295 204.851 42.306 47.216 1.00 54.67 C ANISOU 413 CE2 TYR A 295 6360 6902 7511 936 529 -34 C ATOM 414 CZ TYR A 295 205.970 43.009 47.622 1.00 52.99 C ANISOU 414 CZ TYR A 295 6306 6498 7328 938 579 -94 C ATOM 415 OH TYR A 295 206.340 43.012 48.955 1.00 56.19 O ANISOU 415 OH TYR A 295 6715 6900 7733 919 654 -187 O ATOM 416 N GLU A 296 204.235 39.953 42.811 1.00 33.85 N ANISOU 416 N GLU A 296 3659 4426 4777 709 210 248 N ATOM 417 CA GLU A 296 203.889 38.641 43.344 1.00 36.74 C ANISOU 417 CA GLU A 296 3904 4944 5111 561 200 234 C ATOM 418 C GLU A 296 204.851 37.549 42.890 1.00 32.69 C ANISOU 418 C GLU A 296 3481 4379 4560 380 160 245 C ATOM 419 O GLU A 296 205.130 36.599 43.632 1.00 30.68 O ANISOU 419 O GLU A 296 3205 4167 4282 244 185 211 O ATOM 420 CB GLU A 296 202.460 38.257 42.964 1.00 42.81 C ANISOU 420 CB GLU A 296 4485 5915 5866 596 135 276 C ATOM 421 CG GLU A 296 201.425 39.335 43.303 1.00 54.35 C ANISOU 421 CG GLU A 296 5846 7450 7356 797 165 268 C ATOM 422 CD GLU A 296 201.479 40.514 42.327 1.00 63.23 C ANISOU 422 CD GLU A 296 7071 8456 8497 967 132 308 C ATOM 423 OE1 GLU A 296 202.061 40.358 41.223 1.00 62.85 O ANISOU 423 OE1 GLU A 296 7130 8317 8433 924 71 358 O ATOM 424 OE2 GLU A 296 200.947 41.595 42.667 1.00 67.63 O ANISOU 424 OE2 GLU A 296 7609 9010 9080 1149 168 291 O ATOM 425 N GLU A 297 205.332 37.664 41.653 1.00 29.06 N ANISOU 425 N GLU A 297 3123 3833 4087 386 98 298 N ATOM 426 CA GLU A 297 206.262 36.668 41.133 1.00 27.82 C ANISOU 426 CA GLU A 297 3056 3628 3885 234 55 308 C ATOM 427 C GLU A 297 207.638 36.816 41.790 1.00 26.52 C ANISOU 427 C GLU A 297 3031 3320 3726 173 132 253 C ATOM 428 O GLU A 297 208.298 35.810 42.092 1.00 25.42 O ANISOU 428 O GLU A 297 2926 3183 3549 34 130 226 O ATOM 429 CB GLU A 297 206.375 36.793 39.607 1.00 27.93 C ANISOU 429 CB GLU A 297 3136 3602 3874 272 -31 381 C ATOM 430 CG GLU A 297 205.105 36.318 38.890 1.00 28.99 C ANISOU 430 CG GLU A 297 3130 3898 3988 296 -127 428 C ATOM 431 CD GLU A 297 205.113 36.589 37.377 1.00 35.97 C ANISOU 431 CD GLU A 297 4076 4748 4843 368 -213 500 C ATOM 432 OE1 GLU A 297 205.957 37.367 36.871 1.00 36.79 O ANISOU 432 OE1 GLU A 297 4325 4705 4950 428 -188 524 O ATOM 433 OE2 GLU A 297 204.257 36.008 36.686 1.00 39.52 O ANISOU 433 OE2 GLU A 297 4426 5325 5263 361 -307 533 O ATOM 434 N ALA A 298 208.069 38.063 42.001 1.00 26.81 N ANISOU 434 N ALA A 298 3149 3230 3807 279 194 233 N ATOM 435 CA ALA A 298 209.298 38.333 42.764 1.00 25.88 C ANISOU 435 CA ALA A 298 3145 2984 3703 229 271 168 C ATOM 436 C ALA A 298 209.209 37.758 44.176 1.00 26.41 C ANISOU 436 C ALA A 298 3143 3128 3764 165 327 93 C ATOM 437 O ALA A 298 210.192 37.207 44.703 1.00 25.83 O ANISOU 437 O ALA A 298 3137 3012 3667 59 357 44 O ATOM 438 CB ALA A 298 209.550 39.845 42.861 1.00 27.95 C ANISOU 438 CB ALA A 298 3490 3106 4024 360 326 154 C ATOM 439 N ALA A 299 208.044 37.929 44.816 1.00 26.97 N ANISOU 439 N ALA A 299 3080 3316 3853 240 347 83 N ATOM 440 CA ALA A 299 207.884 37.420 46.182 1.00 27.71 C ANISOU 440 CA ALA A 299 3102 3493 3935 189 408 19 C ATOM 441 C ALA A 299 207.943 35.898 46.176 1.00 28.99 C ANISOU 441 C ALA A 299 3228 3745 4040 24 367 34 C ATOM 442 O ALA A 299 208.517 35.294 47.081 1.00 25.92 O ANISOU 442 O ALA A 299 2867 3357 3625 -64 412 -17 O ATOM 443 CB ALA A 299 206.558 37.914 46.821 1.00 32.71 C ANISOU 443 CB ALA A 299 3585 4252 4592 310 438 12 C ATOM 444 N AMET A 300 207.334 35.284 45.170 0.46 28.38 N ANISOU 444 N AMET A 300 3096 3744 3943 -13 280 103 N ATOM 445 N BMET A 300 207.352 35.275 45.168 0.54 28.31 N ANISOU 445 N BMET A 300 3089 3734 3934 -15 280 103 N ATOM 446 CA AMET A 300 207.393 33.832 45.068 0.46 27.66 C ANISOU 446 CA AMET A 300 2988 3722 3799 -172 231 118 C ATOM 447 CA BMET A 300 207.385 33.822 45.057 0.54 27.66 C ANISOU 447 CA BMET A 300 2987 3723 3799 -173 229 119 C ATOM 448 C AMET A 300 208.833 33.363 44.883 0.46 26.81 C ANISOU 448 C AMET A 300 3039 3492 3654 -265 226 94 C ATOM 449 C BMET A 300 208.814 33.329 44.840 0.54 26.81 C ANISOU 449 C BMET A 300 3038 3495 3653 -267 222 97 C ATOM 450 O AMET A 300 209.264 32.392 45.516 0.46 26.15 O ANISOU 450 O AMET A 300 2979 3426 3529 -378 240 64 O ATOM 451 O BMET A 300 209.215 32.300 45.397 0.54 26.12 O ANISOU 451 O BMET A 300 2973 3429 3522 -385 229 71 O ATOM 452 CB AMET A 300 206.536 33.325 43.908 0.46 29.21 C ANISOU 452 CB AMET A 300 3109 4009 3982 -191 126 190 C ATOM 453 CB BMET A 300 206.509 33.348 43.893 0.54 29.27 C ANISOU 453 CB BMET A 300 3114 4018 3990 -188 125 191 C ATOM 454 CG AMET A 300 206.532 31.821 43.797 0.46 25.27 C ANISOU 454 CG AMET A 300 2598 3573 3431 -359 67 203 C ATOM 455 CG BMET A 300 205.017 33.542 44.082 0.54 28.80 C ANISOU 455 CG BMET A 300 2870 4118 3955 -122 118 214 C ATOM 456 SD AMET A 300 205.911 31.107 45.326 0.46 44.25 S ANISOU 456 SD AMET A 300 4885 6101 5829 -443 138 170 S ATOM 457 SD BMET A 300 204.376 32.470 45.386 0.54 34.90 S ANISOU 457 SD BMET A 300 3512 5041 4709 -247 165 190 S ATOM 458 CE AMET A 300 204.367 32.006 45.501 0.46 37.68 C ANISOU 458 CE AMET A 300 3855 5414 5046 -305 158 192 C ATOM 459 CE BMET A 300 205.451 31.056 45.225 0.54 40.64 C ANISOU 459 CE BMET A 300 4372 5694 5377 -440 123 185 C ATOM 460 N ALA A 301 209.580 34.048 44.020 1.00 25.22 N ANISOU 460 N ALA A 301 2948 3170 3463 -213 209 111 N ATOM 461 CA ALA A 301 210.992 33.676 43.784 1.00 26.81 C ANISOU 461 CA ALA A 301 3294 3266 3626 -292 208 88 C ATOM 462 C ALA A 301 211.793 33.793 45.080 1.00 27.22 C ANISOU 462 C ALA A 301 3391 3270 3681 -317 298 4 C ATOM 463 O ALA A 301 212.563 32.903 45.430 1.00 27.27 O ANISOU 463 O ALA A 301 3454 3270 3636 -416 298 -29 O ATOM 464 CB ALA A 301 211.631 34.570 42.708 1.00 24.56 C ANISOU 464 CB ALA A 301 3110 2864 3358 -223 192 124 C ATOM 465 N ILE A 302 211.617 34.920 45.767 1.00 23.96 N ANISOU 465 N ILE A 302 2960 2821 3325 -215 368 -33 N ATOM 466 CA ILE A 302 212.281 35.156 47.049 1.00 27.16 C ANISOU 466 CA ILE A 302 3399 3186 3735 -221 452 -122 C ATOM 467 C ILE A 302 211.977 34.048 48.066 1.00 28.14 C ANISOU 467 C ILE A 302 3458 3421 3812 -303 471 -152 C ATOM 468 O ILE A 302 212.893 33.453 48.655 1.00 26.66 O ANISOU 468 O ILE A 302 3339 3210 3582 -379 494 -203 O ATOM 469 CB ILE A 302 211.905 36.541 47.630 1.00 26.68 C ANISOU 469 CB ILE A 302 3316 3081 3742 -84 516 -158 C ATOM 470 CG1 ILE A 302 212.538 37.640 46.778 1.00 29.94 C ANISOU 470 CG1 ILE A 302 3833 3345 4197 -23 511 -140 C ATOM 471 CG2 ILE A 302 212.341 36.675 49.115 1.00 24.35 C ANISOU 471 CG2 ILE A 302 3029 2778 3444 -83 598 -257 C ATOM 472 CD1 ILE A 302 211.953 39.030 47.046 1.00 33.87 C ANISOU 472 CD1 ILE A 302 4316 3791 4762 128 551 -154 C ATOM 473 N ALA A 303 210.694 33.755 48.254 1.00 27.31 N ANISOU 473 N ALA A 303 3221 3444 3711 -289 461 -116 N ATOM 474 CA ALA A 303 210.289 32.733 49.229 1.00 30.36 C ANISOU 474 CA ALA A 303 3538 3941 4055 -371 486 -131 C ATOM 475 C ALA A 303 210.757 31.337 48.851 1.00 29.59 C ANISOU 475 C ALA A 303 3497 3853 3892 -515 427 -108 C ATOM 476 O ALA A 303 211.078 30.533 49.724 1.00 29.53 O ANISOU 476 O ALA A 303 3511 3873 3838 -591 458 -141 O ATOM 477 CB ALA A 303 208.748 32.740 49.451 1.00 29.31 C ANISOU 477 CB ALA A 303 3235 3957 3942 -331 489 -91 C ATOM 478 N SER A 304 210.809 31.036 47.552 1.00 24.16 N ANISOU 478 N SER A 304 2843 3141 3196 -547 339 -52 N ATOM 479 CA SER A 304 211.200 29.697 47.145 1.00 25.75 C ANISOU 479 CA SER A 304 3104 3349 3332 -674 273 -32 C ATOM 480 C SER A 304 212.717 29.514 47.207 1.00 27.14 C ANISOU 480 C SER A 304 3430 3418 3464 -706 285 -83 C ATOM 481 O SER A 304 213.190 28.402 47.455 1.00 28.83 O ANISOU 481 O SER A 304 3703 3638 3612 -800 265 -97 O ATOM 482 CB SER A 304 210.707 29.379 45.712 1.00 28.73 C ANISOU 482 CB SER A 304 3465 3746 3705 -693 166 40 C ATOM 483 OG SER A 304 209.273 29.264 45.688 1.00 37.47 O ANISOU 483 OG SER A 304 4421 4978 4840 -691 143 84 O ATOM 484 N LEU A 305 213.472 30.579 46.941 1.00 25.56 N ANISOU 484 N LEU A 305 3293 3121 3296 -628 315 -108 N ATOM 485 CA LEU A 305 214.930 30.442 46.835 1.00 26.95 C ANISOU 485 CA LEU A 305 3601 3209 3432 -660 319 -152 C ATOM 486 C LEU A 305 215.669 30.768 48.140 1.00 28.99 C ANISOU 486 C LEU A 305 3890 3436 3689 -646 407 -242 C ATOM 487 O LEU A 305 216.786 30.313 48.334 1.00 26.90 O ANISOU 487 O LEU A 305 3716 3134 3372 -691 411 -288 O ATOM 488 CB LEU A 305 215.490 31.321 45.712 1.00 26.46 C ANISOU 488 CB LEU A 305 3599 3056 3397 -605 298 -124 C ATOM 489 CG LEU A 305 215.002 30.869 44.328 1.00 26.86 C ANISOU 489 CG LEU A 305 3644 3134 3427 -620 202 -41 C ATOM 490 CD1 LEU A 305 215.298 31.955 43.277 1.00 27.24 C ANISOU 490 CD1 LEU A 305 3735 3102 3512 -541 194 -1 C ATOM 491 CD2 LEU A 305 215.660 29.554 43.960 1.00 26.63 C ANISOU 491 CD2 LEU A 305 3692 3116 3311 -716 140 -42 C ATOM 492 N ASN A 306 215.080 31.597 48.991 1.00 26.29 N ANISOU 492 N ASN A 306 3837 2107 4047 -331 295 -215 N ATOM 493 CA ASN A 306 215.756 32.018 50.213 1.00 28.31 C ANISOU 493 CA ASN A 306 4049 2502 4206 -357 239 -64 C ATOM 494 C ASN A 306 215.894 30.807 51.128 1.00 29.54 C ANISOU 494 C ASN A 306 4269 2530 4423 -349 172 122 C ATOM 495 O ASN A 306 214.903 30.164 51.477 1.00 30.19 O ANISOU 495 O ASN A 306 4442 2502 4526 -450 177 163 O ATOM 496 CB ASN A 306 215.015 33.162 50.922 1.00 27.50 C ANISOU 496 CB ASN A 306 3938 2572 3940 -520 269 -75 C ATOM 497 CG ASN A 306 215.763 33.653 52.160 1.00 30.90 C ANISOU 497 CG ASN A 306 4322 3161 4256 -557 212 65 C ATOM 498 OD1 ASN A 306 216.932 33.990 52.084 1.00 24.61 O ANISOU 498 OD1 ASN A 306 3449 2452 3449 -470 178 87 O ATOM 499 ND2 ASN A 306 215.091 33.669 53.306 1.00 28.34 N ANISOU 499 ND2 ASN A 306 4040 2888 3841 -693 200 165 N ATOM 500 N GLY A 307 217.121 30.483 51.504 1.00 25.27 N ANISOU 500 N GLY A 307 3679 2011 3911 -230 109 242 N ATOM 501 CA GLY A 307 217.364 29.340 52.355 1.00 25.83 C ANISOU 501 CA GLY A 307 3804 1962 4046 -201 43 435 C ATOM 502 C GLY A 307 217.637 28.083 51.573 1.00 28.52 C ANISOU 502 C GLY A 307 4210 2058 4570 -47 37 421 C ATOM 503 O GLY A 307 217.897 27.035 52.154 1.00 31.52 O ANISOU 503 O GLY A 307 4647 2303 5028 4 -16 580 O ATOM 504 N TYR A 308 217.582 28.177 50.245 1.00 27.29 N ANISOU 504 N TYR A 308 4048 1840 4481 31 93 230 N ATOM 505 CA TYR A 308 217.812 27.019 49.397 1.00 33.56 C ANISOU 505 CA TYR A 308 4911 2396 5445 180 98 183 C ATOM 506 C TYR A 308 219.313 26.871 49.067 1.00 36.40 C ANISOU 506 C TYR A 308 5178 2793 5857 407 66 215 C ATOM 507 O TYR A 308 220.059 27.849 49.067 1.00 36.46 O ANISOU 507 O TYR A 308 5058 3025 5769 436 60 203 O ATOM 508 CB TYR A 308 217.023 27.196 48.102 1.00 37.30 C ANISOU 508 CB TYR A 308 5413 2806 5952 149 175 -44 C ATOM 509 CG TYR A 308 217.005 25.964 47.234 1.00 42.21 C ANISOU 509 CG TYR A 308 6133 3163 6740 262 188 -115 C ATOM 510 CD1 TYR A 308 216.099 24.938 47.483 1.00 46.96 C ANISOU 510 CD1 TYR A 308 6881 3582 7380 166 171 -71 C ATOM 511 CD2 TYR A 308 217.882 25.822 46.164 1.00 42.28 C ANISOU 511 CD2 TYR A 308 6091 3162 6812 454 203 -228 C ATOM 512 CE1 TYR A 308 216.069 23.798 46.695 1.00 49.35 C ANISOU 512 CE1 TYR A 308 7282 3757 7710 250 147 -137 C ATOM 513 CE2 TYR A 308 217.855 24.678 45.364 1.00 44.73 C ANISOU 513 CE2 TYR A 308 6501 3362 7135 538 186 -290 C ATOM 514 CZ TYR A 308 216.940 23.673 45.640 1.00 48.82 C ANISOU 514 CZ TYR A 308 7171 3716 7660 435 158 -247 C ATOM 515 OH TYR A 308 216.884 22.531 44.872 1.00 51.91 O ANISOU 515 OH TYR A 308 7678 3977 8068 507 138 -312 O ATOM 516 N ARG A 309 219.746 25.662 48.737 1.00 39.52 N ANISOU 516 N ARG A 309 5641 2972 6403 568 49 248 N ATOM 517 CA ARG A 309 221.177 25.402 48.563 1.00 38.72 C ANISOU 517 CA ARG A 309 5451 2910 6350 799 15 309 C ATOM 518 C ARG A 309 221.639 25.628 47.113 1.00 44.62 C ANISOU 518 C ARG A 309 6135 3674 7145 943 68 103 C ATOM 519 O ARG A 309 220.940 25.285 46.160 1.00 45.90 O ANISOU 519 O ARG A 309 6377 3681 7381 931 123 -65 O ATOM 520 CB ARG A 309 221.500 23.986 49.012 1.00 41.70 C ANISOU 520 CB ARG A 309 5929 3049 6864 927 -32 466 C ATOM 521 N LEU A 310 222.791 26.269 46.961 1.00 39.37 N ANISOU 521 N LEU A 310 5317 3222 6419 1060 52 117 N ATOM 522 CA LEU A 310 223.459 26.387 45.675 1.00 38.59 C ANISOU 522 CA LEU A 310 5137 3161 6362 1227 91 -43 C ATOM 523 C LEU A 310 224.919 26.039 45.948 1.00 42.19 C ANISOU 523 C LEU A 310 5490 3702 6837 1446 39 97 C ATOM 524 O LEU A 310 225.599 26.726 46.727 1.00 39.99 O ANISOU 524 O LEU A 310 5095 3657 6442 1416 -9 231 O ATOM 525 CB LEU A 310 223.340 27.798 45.110 1.00 35.76 C ANISOU 525 CB LEU A 310 4668 3041 5877 1120 130 -183 C ATOM 526 CG LEU A 310 224.200 28.033 43.844 1.00 38.55 C ANISOU 526 CG LEU A 310 4905 3490 6251 1291 162 -324 C ATOM 527 CD1 LEU A 310 223.656 27.245 42.650 1.00 37.48 C ANISOU 527 CD1 LEU A 310 4888 3220 6132 1318 214 -475 C ATOM 528 CD2 LEU A 310 224.270 29.506 43.481 1.00 38.84 C ANISOU 528 CD2 LEU A 310 4819 3790 6149 1182 184 -412 C ATOM 529 N GLY A 311 225.384 24.951 45.344 1.00 45.28 N ANISOU 529 N GLY A 311 5928 3907 7371 1664 48 72 N ATOM 530 CA GLY A 311 226.683 24.405 45.682 1.00 49.97 C ANISOU 530 CA GLY A 311 6441 4544 7999 1894 -1 228 C ATOM 531 C GLY A 311 226.680 23.909 47.124 1.00 55.63 C ANISOU 531 C GLY A 311 7213 5212 8714 1847 -70 482 C ATOM 532 O GLY A 311 225.796 23.150 47.537 1.00 57.69 O ANISOU 532 O GLY A 311 7638 5228 9053 1764 -73 525 O ATOM 533 N ASP A 312 227.670 24.339 47.899 1.00 55.95 N ANISOU 533 N ASP A 312 7109 5496 8655 1891 -128 657 N ATOM 534 CA ASP A 312 227.746 23.957 49.309 1.00 55.18 C ANISOU 534 CA ASP A 312 7037 5398 8532 1840 -198 912 C ATOM 535 C ASP A 312 227.233 25.069 50.218 1.00 49.32 C ANISOU 535 C ASP A 312 6252 4870 7616 1566 -221 963 C ATOM 536 O ASP A 312 227.465 25.038 51.428 1.00 50.40 O ANISOU 536 O ASP A 312 6362 5104 7685 1506 -283 1174 O ATOM 537 CB ASP A 312 229.193 23.605 49.694 1.00 58.95 C ANISOU 537 CB ASP A 312 7379 6013 9005 2070 -253 1102 C ATOM 538 N LYS A 313 226.553 26.053 49.638 1.00 41.86 N ANISOU 538 N LYS A 313 5302 4005 6599 1405 -169 770 N ATOM 539 CA LYS A 313 226.156 27.228 50.397 1.00 42.11 C ANISOU 539 CA LYS A 313 5287 4253 6459 1165 -182 793 C ATOM 540 C LYS A 313 224.632 27.418 50.455 1.00 40.50 C ANISOU 540 C LYS A 313 5220 3921 6248 948 -138 690 C ATOM 541 O LYS A 313 223.899 26.926 49.602 1.00 45.12 O ANISOU 541 O LYS A 313 5907 4296 6940 965 -85 545 O ATOM 542 CB LYS A 313 226.829 28.469 49.819 1.00 42.52 C ANISOU 542 CB LYS A 313 5185 4578 6393 1156 -166 685 C ATOM 543 N ILE A 314 224.167 28.124 51.476 1.00 33.00 N ANISOU 543 N ILE A 314 4266 3110 5162 744 -159 766 N ATOM 544 CA ILE A 314 222.738 28.403 51.629 1.00 29.91 C ANISOU 544 CA ILE A 314 3984 2642 4739 536 -117 683 C ATOM 545 C ILE A 314 222.435 29.788 51.103 1.00 31.20 C ANISOU 545 C ILE A 314 4088 2980 4787 421 -65 508 C ATOM 546 O ILE A 314 223.002 30.787 51.584 1.00 27.75 O ANISOU 546 O ILE A 314 3551 2782 4212 359 -88 545 O ATOM 547 CB ILE A 314 222.327 28.293 53.128 1.00 34.02 C ANISOU 547 CB ILE A 314 4544 3206 5177 383 -168 876 C ATOM 548 CG1 ILE A 314 222.607 26.889 53.664 1.00 41.21 C ANISOU 548 CG1 ILE A 314 5520 3931 6207 496 -222 1068 C ATOM 549 CG2 ILE A 314 220.862 28.689 53.338 1.00 28.80 C ANISOU 549 CG2 ILE A 314 3977 2509 4457 165 -122 793 C ATOM 550 CD1 ILE A 314 221.538 25.872 53.368 1.00 46.25 C ANISOU 550 CD1 ILE A 314 6324 4271 6979 466 -195 1030 C ATOM 551 N LEU A 315 221.559 29.884 50.092 1.00 26.06 N ANISOU 551 N LEU A 315 3497 2216 4188 389 5 317 N ATOM 552 CA LEU A 315 221.261 31.199 49.518 1.00 23.96 C ANISOU 552 CA LEU A 315 3176 2107 3822 294 58 155 C ATOM 553 C LEU A 315 220.545 32.113 50.484 1.00 26.69 C ANISOU 553 C LEU A 315 3539 2583 4018 85 62 188 C ATOM 554 O LEU A 315 219.695 31.664 51.255 1.00 26.08 O ANISOU 554 O LEU A 315 3551 2422 3936 -21 55 265 O ATOM 555 CB LEU A 315 220.385 31.070 48.251 1.00 23.04 C ANISOU 555 CB LEU A 315 3119 1850 3788 298 133 -46 C ATOM 556 CG LEU A 315 221.007 30.252 47.110 1.00 32.43 C ANISOU 556 CG LEU A 315 4295 2911 5118 502 145 -126 C ATOM 557 CD1 LEU A 315 219.936 30.027 46.016 1.00 35.16 C ANISOU 557 CD1 LEU A 315 4718 3109 5534 466 218 -314 C ATOM 558 CD2 LEU A 315 222.249 30.969 46.535 1.00 31.91 C ANISOU 558 CD2 LEU A 315 4077 3041 5006 620 137 -165 C ATOM 559 N GLN A 316 220.856 33.397 50.408 1.00 23.63 N ANISOU 559 N GLN A 316 3072 2398 3508 24 76 123 N ATOM 560 CA GLN A 316 220.073 34.401 51.109 1.00 29.50 C ANISOU 560 CA GLN A 316 3843 3254 4110 -167 100 104 C ATOM 561 C GLN A 316 219.445 35.244 50.011 1.00 27.98 C ANISOU 561 C GLN A 316 3651 3071 3908 -198 178 -97 C ATOM 562 O GLN A 316 220.160 35.831 49.190 1.00 26.00 O ANISOU 562 O GLN A 316 3319 2906 3653 -127 189 -181 O ATOM 563 CB GLN A 316 220.975 35.281 51.990 1.00 28.65 C ANISOU 563 CB GLN A 316 3654 3375 3857 -225 51 197 C ATOM 564 CG GLN A 316 221.651 34.540 53.129 1.00 31.76 C ANISOU 564 CG GLN A 316 4028 3799 4238 -202 -30 411 C ATOM 565 CD GLN A 316 222.757 35.369 53.788 1.00 32.83 C ANISOU 565 CD GLN A 316 4060 4182 4234 -240 -82 493 C ATOM 566 OE1 GLN A 316 222.713 36.602 53.768 1.00 33.55 O ANISOU 566 OE1 GLN A 316 4130 4412 4205 -350 -57 401 O ATOM 567 NE2 GLN A 316 223.762 34.693 54.345 1.00 34.48 N ANISOU 567 NE2 GLN A 316 4203 4443 4456 -149 -156 668 N ATOM 568 N VAL A 317 218.121 35.261 49.940 1.00 25.99 N ANISOU 568 N VAL A 317 3483 2737 3656 -297 233 -169 N ATOM 569 CA VAL A 317 217.448 36.001 48.884 1.00 25.55 C ANISOU 569 CA VAL A 317 3424 2691 3593 -320 310 -348 C ATOM 570 C VAL A 317 216.417 36.945 49.489 1.00 27.06 C ANISOU 570 C VAL A 317 3658 2966 3656 -481 354 -378 C ATOM 571 O VAL A 317 215.600 36.516 50.309 1.00 29.01 O ANISOU 571 O VAL A 317 3974 3169 3880 -571 351 -307 O ATOM 572 CB VAL A 317 216.729 35.028 47.894 1.00 23.97 C ANISOU 572 CB VAL A 317 3278 2301 3530 -264 349 -437 C ATOM 573 CG1 VAL A 317 216.111 35.809 46.720 1.00 23.97 C ANISOU 573 CG1 VAL A 317 3255 2336 3517 -280 428 -618 C ATOM 574 CG2 VAL A 317 217.690 33.959 47.419 1.00 24.24 C ANISOU 574 CG2 VAL A 317 3291 2226 3695 -96 308 -402 C ATOM 575 N SER A 318 216.438 38.213 49.077 1.00 25.04 N ANISOU 575 N SER A 318 3365 2831 3318 -514 395 -481 N ATOM 576 CA SER A 318 215.523 39.188 49.679 1.00 29.24 C ANISOU 576 CA SER A 318 3941 3445 3722 -649 441 -513 C ATOM 577 C SER A 318 215.363 40.389 48.764 1.00 30.62 C ANISOU 577 C SER A 318 4087 3690 3858 -649 505 -658 C ATOM 578 O SER A 318 216.178 40.579 47.872 1.00 28.26 O ANISOU 578 O SER A 318 3721 3411 3604 -563 497 -710 O ATOM 579 CB SER A 318 216.116 39.672 51.003 1.00 29.55 C ANISOU 579 CB SER A 318 3976 3611 3639 -726 389 -400 C ATOM 580 OG SER A 318 217.468 40.080 50.804 1.00 30.25 O ANISOU 580 OG SER A 318 3988 3793 3714 -669 344 -383 O ATOM 581 N PHE A 319 214.342 41.223 48.976 1.00 30.01 N ANISOU 581 N PHE A 319 4006 3697 3697 -666 540 -618 N ATOM 582 CA PHE A 319 214.272 42.496 48.220 1.00 31.89 C ANISOU 582 CA PHE A 319 4157 4023 3938 -608 542 -586 C ATOM 583 C PHE A 319 215.472 43.388 48.537 1.00 32.01 C ANISOU 583 C PHE A 319 4151 4114 3896 -638 513 -592 C ATOM 584 O PHE A 319 215.815 43.558 49.702 1.00 32.74 O ANISOU 584 O PHE A 319 4297 4256 3886 -736 506 -585 O ATOM 585 CB PHE A 319 212.994 43.273 48.536 1.00 34.39 C ANISOU 585 CB PHE A 319 4467 4370 4230 -644 564 -526 C ATOM 586 CG PHE A 319 211.769 42.720 47.878 1.00 35.97 C ANISOU 586 CG PHE A 319 4655 4532 4481 -599 570 -511 C ATOM 587 CD1 PHE A 319 211.604 42.804 46.510 1.00 35.54 C ANISOU 587 CD1 PHE A 319 4533 4469 4499 -542 557 -516 C ATOM 588 CD2 PHE A 319 210.776 42.144 48.628 1.00 34.85 C ANISOU 588 CD2 PHE A 319 4572 4374 4294 -645 599 -505 C ATOM 589 CE1 PHE A 319 210.458 42.294 45.899 1.00 38.56 C ANISOU 589 CE1 PHE A 319 4908 4833 4911 -528 567 -511 C ATOM 590 CE2 PHE A 319 209.634 41.646 48.032 1.00 36.98 C ANISOU 590 CE2 PHE A 319 4828 4624 4598 -613 601 -495 C ATOM 591 CZ PHE A 319 209.471 41.715 46.663 1.00 36.76 C ANISOU 591 CZ PHE A 319 4733 4592 4643 -559 589 -500 C ATOM 592 N LYS A 320 216.106 43.955 47.510 1.00 33.02 N ANISOU 592 N LYS A 320 4205 4266 4075 -571 485 -595 N ATOM 593 CA LYS A 320 217.290 44.796 47.710 1.00 39.75 C ANISOU 593 CA LYS A 320 5032 5201 4871 -603 458 -602 C ATOM 594 C LYS A 320 217.008 45.972 48.651 1.00 42.69 C ANISOU 594 C LYS A 320 5432 5613 5174 -682 460 -547 C ATOM 595 O LYS A 320 215.934 46.571 48.595 1.00 43.51 O ANISOU 595 O LYS A 320 5546 5675 5312 -654 459 -503 O ATOM 596 CB LYS A 320 217.819 45.346 46.380 1.00 40.30 C ANISOU 596 CB LYS A 320 5020 5284 5007 -530 430 -602 C ATOM 597 CG LYS A 320 219.054 46.240 46.530 1.00 39.94 C ANISOU 597 CG LYS A 320 4942 5334 4899 -572 408 -609 C ATOM 598 CD LYS A 320 219.344 46.972 45.226 1.00 41.93 C ANISOU 598 CD LYS A 320 5126 5590 5216 -520 383 -594 C ATOM 599 CE LYS A 320 220.756 47.535 45.190 1.00 41.67 C ANISOU 599 CE LYS A 320 5043 5667 5124 -555 363 -620 C ATOM 600 NZ LYS A 320 221.029 48.456 46.324 1.00 41.64 N ANISOU 600 NZ LYS A 320 5090 5709 5021 -640 364 -577 N ATOM 601 N THR A 321 217.976 46.289 49.506 1.00 43.16 N ANISOU 601 N THR A 321 5509 5757 5134 -764 439 -547 N ATOM 602 CA THR A 321 217.863 47.421 50.433 1.00 49.13 C ANISOU 602 CA THR A 321 6293 6540 5834 -835 433 -501 C ATOM 603 C THR A 321 218.322 48.708 49.766 1.00 50.44 C ANISOU 603 C THR A 321 6425 6705 6035 -780 410 -484 C ATOM 604 O THR A 321 219.239 48.675 48.942 1.00 52.96 O ANISOU 604 O THR A 321 6689 7066 6367 -760 400 -507 O ATOM 605 CB THR A 321 218.736 47.206 51.675 1.00 53.79 C ANISOU 605 CB THR A 321 6913 7237 6288 -958 399 -484 C ATOM 606 OG1 THR A 321 220.058 46.808 51.267 1.00 59.79 O ANISOU 606 OG1 THR A 321 7623 8095 6999 -958 353 -502 O ATOM 607 CG2 THR A 321 218.143 46.142 52.549 1.00 55.84 C ANISOU 607 CG2 THR A 321 7236 7493 6489 -1016 397 -473 C TER 608 THR A 321 ATOM 609 N GLY B 243 207.345 22.426 29.278 1.00 47.80 N ANISOU 609 N GLY B 243 6736 5599 5828 -169 -663 -955 N ATOM 610 CA GLY B 243 207.219 23.771 28.742 1.00 44.29 C ANISOU 610 CA GLY B 243 6247 5227 5355 -257 -732 -892 C ATOM 611 C GLY B 243 207.023 23.822 27.228 1.00 40.17 C ANISOU 611 C GLY B 243 5673 4892 4697 -187 -762 -951 C ATOM 612 O GLY B 243 206.910 22.788 26.558 1.00 44.50 O ANISOU 612 O GLY B 243 6250 5490 5167 -72 -748 -1085 O ATOM 613 N TRP B 244 206.978 25.039 26.694 1.00 33.46 N ANISOU 613 N TRP B 244 4711 4170 3831 -260 -749 -805 N ATOM 614 CA TRP B 244 206.758 25.285 25.269 1.00 36.39 C ANISOU 614 CA TRP B 244 4984 4760 4083 -209 -734 -791 C ATOM 615 C TRP B 244 208.043 25.746 24.627 1.00 34.94 C ANISOU 615 C TRP B 244 4649 4825 3803 -141 -703 -672 C ATOM 616 O TRP B 244 208.635 26.755 25.042 1.00 32.49 O ANISOU 616 O TRP B 244 4263 4542 3540 -219 -687 -513 O ATOM 617 CB TRP B 244 205.693 26.354 25.096 1.00 36.97 C ANISOU 617 CB TRP B 244 5035 4798 4213 -335 -734 -698 C ATOM 618 CG TRP B 244 204.435 25.936 25.728 1.00 40.39 C ANISOU 618 CG TRP B 244 5610 4991 4745 -403 -762 -807 C ATOM 619 CD1 TRP B 244 203.985 26.261 26.983 1.00 39.82 C ANISOU 619 CD1 TRP B 244 5577 4712 4842 -493 -703 -744 C ATOM 620 CD2 TRP B 244 203.471 25.045 25.167 1.00 43.92 C ANISOU 620 CD2 TRP B 244 6098 5433 5156 -357 -743 -937 C ATOM 621 NE1 TRP B 244 202.773 25.639 27.222 1.00 41.24 N ANISOU 621 NE1 TRP B 244 5749 4820 5098 -470 -593 -785 N ATOM 622 CE2 TRP B 244 202.434 24.897 26.123 1.00 45.39 C ANISOU 622 CE2 TRP B 244 6292 5448 5506 -418 -621 -895 C ATOM 623 CE3 TRP B 244 203.373 24.377 23.943 1.00 46.98 C ANISOU 623 CE3 TRP B 244 6465 5992 5394 -261 -760 -1046 C ATOM 624 CZ2 TRP B 244 201.308 24.098 25.879 1.00 48.10 C ANISOU 624 CZ2 TRP B 244 6641 5778 5859 -416 -542 -953 C ATOM 625 CZ3 TRP B 244 202.245 23.588 23.703 1.00 50.56 C ANISOU 625 CZ3 TRP B 244 6963 6381 5868 -285 -686 -1092 C ATOM 626 CH2 TRP B 244 201.232 23.458 24.668 1.00 48.65 C ANISOU 626 CH2 TRP B 244 6739 5964 5780 -372 -584 -1045 C ATOM 627 N CYS B 245 208.476 24.988 23.628 1.00 36.40 N ANISOU 627 N CYS B 245 4793 5184 3853 -1 -687 -755 N ATOM 628 CA CYS B 245 209.731 25.253 22.952 1.00 32.61 C ANISOU 628 CA CYS B 245 4174 4945 3272 85 -653 -659 C ATOM 629 C CYS B 245 209.586 26.237 21.772 1.00 29.73 C ANISOU 629 C CYS B 245 3676 4799 2821 67 -632 -543 C ATOM 630 O CYS B 245 208.740 26.061 20.898 1.00 32.58 O ANISOU 630 O CYS B 245 4044 5225 3111 82 -638 -611 O ATOM 631 CB CYS B 245 210.350 23.945 22.460 1.00 37.38 C ANISOU 631 CB CYS B 245 4799 5629 3774 253 -632 -800 C ATOM 632 SG CYS B 245 212.094 24.155 22.078 1.00 41.80 S ANISOU 632 SG CYS B 245 5203 6428 4250 359 -588 -676 S ATOM 633 N ILE B 246 210.422 27.269 21.780 1.00 27.84 N ANISOU 633 N ILE B 246 3315 4674 2588 30 -605 -365 N ATOM 634 CA ILE B 246 210.425 28.315 20.786 1.00 26.19 C ANISOU 634 CA ILE B 246 2972 4664 2313 9 -574 -225 C ATOM 635 C ILE B 246 211.737 28.241 20.019 1.00 28.16 C ANISOU 635 C ILE B 246 3097 5160 2442 128 -538 -175 C ATOM 636 O ILE B 246 212.806 28.127 20.628 1.00 29.52 O ANISOU 636 O ILE B 246 3245 5332 2641 152 -529 -138 O ATOM 637 CB ILE B 246 210.343 29.711 21.422 1.00 25.94 C ANISOU 637 CB ILE B 246 2897 4559 2401 -143 -554 -44 C ATOM 638 CG1 ILE B 246 209.085 29.786 22.321 1.00 30.64 C ANISOU 638 CG1 ILE B 246 3624 4885 3132 -264 -582 -90 C ATOM 639 CG2 ILE B 246 210.300 30.788 20.317 1.00 26.77 C ANISOU 639 CG2 ILE B 246 2861 4872 2439 -153 -510 109 C ATOM 640 CD1 ILE B 246 209.078 30.968 23.266 1.00 33.23 C ANISOU 640 CD1 ILE B 246 3946 5078 3600 -422 -554 57 C ATOM 641 N PHE B 247 211.629 28.285 18.694 1.00 30.35 N ANISOU 641 N PHE B 247 3296 5652 2585 199 -517 -173 N ATOM 642 CA PHE B 247 212.768 28.260 17.756 1.00 28.95 C ANISOU 642 CA PHE B 247 2993 5731 2275 316 -474 -123 C ATOM 643 C PHE B 247 212.999 29.681 17.245 1.00 35.64 C ANISOU 643 C PHE B 247 3697 6732 3113 253 -437 85 C ATOM 644 O PHE B 247 212.042 30.388 16.873 1.00 36.79 O ANISOU 644 O PHE B 247 3827 6881 3271 179 -438 148 O ATOM 645 CB PHE B 247 212.433 27.334 16.573 1.00 29.31 C ANISOU 645 CB PHE B 247 3055 5916 2166 431 -469 -271 C ATOM 646 CG PHE B 247 213.407 27.398 15.425 1.00 35.09 C ANISOU 646 CG PHE B 247 3658 6927 2748 544 -419 -219 C ATOM 647 CD1 PHE B 247 214.725 27.016 15.596 1.00 36.46 C ANISOU 647 CD1 PHE B 247 3787 7163 2904 639 -385 -206 C ATOM 648 CD2 PHE B 247 212.990 27.806 14.158 1.00 41.76 C ANISOU 648 CD2 PHE B 247 4423 7978 3466 559 -404 -182 C ATOM 649 CE1 PHE B 247 215.626 27.060 14.512 1.00 40.01 C ANISOU 649 CE1 PHE B 247 4116 7870 3216 747 -332 -158 C ATOM 650 CE2 PHE B 247 213.890 27.850 13.062 1.00 43.93 C ANISOU 650 CE2 PHE B 247 4580 8517 3594 665 -353 -136 C ATOM 651 CZ PHE B 247 215.188 27.474 13.235 1.00 37.40 C ANISOU 651 CZ PHE B 247 3715 7740 2756 759 -315 -129 C ATOM 652 N ILE B 248 214.273 30.087 17.228 1.00 33.61 N ANISOU 652 N ILE B 248 3331 6602 2838 286 -399 198 N ATOM 653 CA ILE B 248 214.671 31.441 16.851 1.00 29.68 C ANISOU 653 CA ILE B 248 2695 6239 2343 224 -352 402 C ATOM 654 C ILE B 248 215.769 31.364 15.798 1.00 34.66 C ANISOU 654 C ILE B 248 3196 7142 2832 352 -307 446 C ATOM 655 O ILE B 248 216.868 30.906 16.083 1.00 36.65 O ANISOU 655 O ILE B 248 3421 7435 3071 421 -297 433 O ATOM 656 CB ILE B 248 215.254 32.224 18.061 1.00 37.77 C ANISOU 656 CB ILE B 248 3705 7137 3508 102 -341 519 C ATOM 657 CG1 ILE B 248 214.204 32.321 19.195 1.00 33.99 C ANISOU 657 CG1 ILE B 248 3362 6375 3177 -32 -378 476 C ATOM 658 CG2 ILE B 248 215.680 33.634 17.625 1.00 34.14 C ANISOU 658 CG2 ILE B 248 3103 6815 3052 35 -276 727 C ATOM 659 CD1 ILE B 248 214.372 31.291 20.343 1.00 28.45 C ANISOU 659 CD1 ILE B 248 2784 5486 2540 -24 -428 341 C ATOM 660 N TYR B 249 215.476 31.818 14.588 1.00 37.63 N ANISOU 660 N TYR B 249 3489 7708 3101 385 -278 506 N ATOM 661 CA TYR B 249 216.449 31.790 13.498 1.00 36.10 C ANISOU 661 CA TYR B 249 3172 7781 2764 505 -230 551 C ATOM 662 C TYR B 249 216.997 33.200 13.225 1.00 40.78 C ANISOU 662 C TYR B 249 3618 8501 3377 445 -171 776 C ATOM 663 O TYR B 249 216.303 34.210 13.419 1.00 43.78 O ANISOU 663 O TYR B 249 3985 8808 3839 327 -160 891 O ATOM 664 CB TYR B 249 215.796 31.218 12.238 1.00 38.01 C ANISOU 664 CB TYR B 249 3420 8174 2847 592 -234 451 C ATOM 665 CG TYR B 249 216.769 31.060 11.111 1.00 43.03 C ANISOU 665 CG TYR B 249 3945 9077 3326 721 -181 474 C ATOM 666 CD1 TYR B 249 217.675 30.017 11.109 1.00 46.09 C ANISOU 666 CD1 TYR B 249 4354 9499 3660 842 -165 362 C ATOM 667 CD2 TYR B 249 216.818 31.970 10.061 1.00 49.91 C ANISOU 667 CD2 TYR B 249 4688 10168 4108 727 -138 620 C ATOM 668 CE1 TYR B 249 218.605 29.871 10.087 1.00 51.65 C ANISOU 668 CE1 TYR B 249 4956 10444 4224 963 -107 386 C ATOM 669 CE2 TYR B 249 217.749 31.826 9.029 1.00 53.10 C ANISOU 669 CE2 TYR B 249 4990 10819 4366 846 -85 644 C ATOM 670 CZ TYR B 249 218.640 30.769 9.058 1.00 56.58 C ANISOU 670 CZ TYR B 249 5458 11283 4756 962 -70 522 C ATOM 671 OH TYR B 249 219.583 30.588 8.054 1.00 66.89 O ANISOU 671 OH TYR B 249 6668 12826 5922 1085 -9 541 O ATOM 672 N ASN B 250 218.241 33.242 12.741 1.00 44.50 N ANISOU 672 N ASN B 250 3977 9160 3771 530 -126 838 N ATOM 673 CA ASN B 250 218.928 34.460 12.311 1.00 44.66 C ANISOU 673 CA ASN B 250 3847 9337 3786 498 -59 1041 C ATOM 674 C ASN B 250 219.654 35.171 13.451 1.00 48.57 C ANISOU 674 C ASN B 250 4312 9721 4422 384 -43 1150 C ATOM 675 O ASN B 250 219.789 36.393 13.449 1.00 53.56 O ANISOU 675 O ASN B 250 4859 10381 5109 289 11 1318 O ATOM 676 CB ASN B 250 217.994 35.409 11.552 1.00 45.76 C ANISOU 676 CB ASN B 250 3940 9543 3904 445 -32 1153 C ATOM 677 CG ASN B 250 218.516 35.753 10.168 1.00 49.68 C ANISOU 677 CG ASN B 250 4298 10328 4249 543 26 1246 C ATOM 678 OD1 ASN B 250 219.600 35.308 9.777 1.00 51.37 O ANISOU 678 OD1 ASN B 250 4452 10690 4378 647 51 1225 O ATOM 679 ND2 ASN B 250 217.756 36.546 9.427 1.00 52.44 N ANISOU 679 ND2 ASN B 250 4595 10744 4584 510 56 1347 N ATOM 680 N LEU B 251 220.117 34.398 14.430 1.00 44.57 N ANISOU 680 N LEU B 251 3875 9090 3972 391 -85 1054 N ATOM 681 CA LEU B 251 221.035 34.922 15.436 1.00 46.49 C ANISOU 681 CA LEU B 251 4070 9278 4314 299 -73 1148 C ATOM 682 C LEU B 251 222.344 35.167 14.705 1.00 51.02 C ANISOU 682 C LEU B 251 4487 10101 4798 385 -15 1249 C ATOM 683 O LEU B 251 222.601 34.543 13.684 1.00 52.86 O ANISOU 683 O LEU B 251 4683 10501 4899 536 0 1196 O ATOM 684 CB LEU B 251 221.252 33.904 16.552 1.00 45.10 C ANISOU 684 CB LEU B 251 3997 8942 4197 310 -134 1021 C ATOM 685 CG LEU B 251 219.986 33.557 17.339 1.00 43.91 C ANISOU 685 CG LEU B 251 4011 8534 4138 229 -192 909 C ATOM 686 CD1 LEU B 251 220.296 32.454 18.358 1.00 42.06 C ANISOU 686 CD1 LEU B 251 3871 8163 3947 265 -246 786 C ATOM 687 CD2 LEU B 251 219.474 34.805 18.021 1.00 43.99 C ANISOU 687 CD2 LEU B 251 4030 8409 4277 38 -173 1026 C ATOM 688 N GLY B 252 223.164 36.078 15.206 1.00 51.06 N ANISOU 688 N GLY B 252 4398 10133 4870 286 22 1390 N ATOM 689 CA GLY B 252 224.438 36.329 14.572 1.00 52.86 C ANISOU 689 CA GLY B 252 4471 10594 5020 361 77 1490 C ATOM 690 C GLY B 252 225.465 35.313 15.023 1.00 53.45 C ANISOU 690 C GLY B 252 4533 10705 5071 459 46 1421 C ATOM 691 O GLY B 252 225.222 34.525 15.945 1.00 53.00 O ANISOU 691 O GLY B 252 4585 10481 5070 450 -16 1310 O ATOM 692 N GLN B 253 226.624 35.342 14.371 1.00 52.75 N ANISOU 692 N GLN B 253 4305 10836 4900 555 95 1495 N ATOM 693 CA GLN B 253 227.705 34.423 14.680 1.00 50.75 C ANISOU 693 CA GLN B 253 4014 10649 4619 666 81 1455 C ATOM 694 C GLN B 253 228.181 34.592 16.115 1.00 49.46 C ANISOU 694 C GLN B 253 3857 10363 4572 538 39 1493 C ATOM 695 O GLN B 253 228.633 33.631 16.737 1.00 48.93 O ANISOU 695 O GLN B 253 3818 10260 4515 609 -1 1424 O ATOM 696 CB GLN B 253 228.880 34.611 13.685 1.00 48.88 C ANISOU 696 CB GLN B 253 3688 10607 4276 762 154 1537 C ATOM 697 N ASP B 254 228.087 35.803 16.658 1.00 52.19 N ANISOU 697 N ASP B 254 4206 10621 5003 343 56 1596 N ATOM 698 CA ASP B 254 228.561 36.025 18.031 1.00 54.38 C ANISOU 698 CA ASP B 254 4493 10789 5380 200 19 1629 C ATOM 699 C ASP B 254 227.458 35.933 19.079 1.00 55.80 C ANISOU 699 C ASP B 254 4792 10743 5667 78 -43 1554 C ATOM 700 O ASP B 254 227.686 36.248 20.252 1.00 57.44 O ANISOU 700 O ASP B 254 5015 10851 5960 -71 -72 1583 O ATOM 701 CB ASP B 254 229.295 37.364 18.166 1.00 59.00 C ANISOU 701 CB ASP B 254 5051 11371 5994 53 58 1767 C ATOM 702 N ALA B 255 226.266 35.501 18.663 1.00 52.54 N ANISOU 702 N ALA B 255 4502 10218 5242 132 -61 1445 N ATOM 703 CA ALA B 255 225.149 35.362 19.598 1.00 46.74 C ANISOU 703 CA ALA B 255 3929 9223 4605 23 -114 1356 C ATOM 704 C ALA B 255 225.469 34.492 20.809 1.00 47.22 C ANISOU 704 C ALA B 255 4059 9168 4715 18 -183 1279 C ATOM 705 O ALA B 255 226.196 33.500 20.730 1.00 50.63 O ANISOU 705 O ALA B 255 4461 9689 5088 168 -202 1233 O ATOM 706 CB ALA B 255 223.908 34.833 18.897 1.00 45.63 C ANISOU 706 CB ALA B 255 3900 9007 4429 107 -128 1240 C ATOM 707 N ASP B 256 224.902 34.865 21.947 1.00 44.28 N ANISOU 707 N ASP B 256 3781 8590 4452 -154 -215 1268 N ATOM 708 CA ASP B 256 225.144 34.162 23.190 1.00 45.52 C ANISOU 708 CA ASP B 256 4006 8630 4661 -183 -281 1209 C ATOM 709 C ASP B 256 223.798 33.992 23.881 1.00 42.65 C ANISOU 709 C ASP B 256 3823 7996 4385 -271 -321 1104 C ATOM 710 O ASP B 256 222.817 34.631 23.502 1.00 44.84 O ANISOU 710 O ASP B 256 4151 8190 4695 -339 -291 1107 O ATOM 711 CB ASP B 256 226.056 34.990 24.086 1.00 52.48 C ANISOU 711 CB ASP B 256 4796 9557 5589 -352 -276 1330 C ATOM 712 CG ASP B 256 225.282 36.025 24.900 1.00 54.94 C ANISOU 712 CG ASP B 256 5188 9675 6011 -589 -263 1357 C ATOM 713 N GLU B 257 223.756 33.127 24.883 1.00 42.18 N ANISOU 713 N GLU B 257 4230 7764 4032 -993 220 -957 N ATOM 714 CA GLU B 257 222.520 32.821 25.602 1.00 42.70 C ANISOU 714 CA GLU B 257 4440 7578 4207 -860 46 -1033 C ATOM 715 C GLU B 257 221.937 34.076 26.271 1.00 42.99 C ANISOU 715 C GLU B 257 4661 7268 4404 -990 59 -870 C ATOM 716 O GLU B 257 220.703 34.285 26.337 1.00 42.91 O ANISOU 716 O GLU B 257 4821 7064 4418 -879 -18 -797 O ATOM 717 CB GLU B 257 222.810 31.725 26.638 1.00 42.94 C ANISOU 717 CB GLU B 257 4323 7604 4389 -795 -79 -1271 C ATOM 718 CG GLU B 257 222.722 30.279 26.092 1.00 44.82 C ANISOU 718 CG GLU B 257 4417 8026 4586 -573 -148 -1469 C ATOM 719 CD GLU B 257 223.942 29.813 25.285 1.00 53.89 C ANISOU 719 CD GLU B 257 5353 9497 5625 -585 -20 -1567 C ATOM 720 OE1 GLU B 257 225.032 30.434 25.401 1.00 59.11 O ANISOU 720 OE1 GLU B 257 5934 10250 6276 -774 104 -1478 O ATOM 721 OE2 GLU B 257 223.807 28.802 24.540 1.00 52.50 O ANISOU 721 OE2 GLU B 257 5071 9485 5391 -406 -41 -1762 O ATOM 722 N GLY B 258 222.836 34.894 26.796 1.00 40.28 N ANISOU 722 N GLY B 258 4263 6839 4201 -1226 159 -843 N ATOM 723 CA GLY B 258 222.489 36.197 27.332 1.00 39.44 C ANISOU 723 CA GLY B 258 4292 6390 4304 -1384 215 -735 C ATOM 724 C GLY B 258 221.458 36.921 26.477 1.00 39.54 C ANISOU 724 C GLY B 258 4480 6248 4294 -1301 274 -449 C ATOM 725 O GLY B 258 220.476 37.444 26.998 1.00 39.94 O ANISOU 725 O GLY B 258 4685 5996 4496 -1265 228 -421 O ATOM 726 N ILE B 259 221.652 36.951 25.163 1.00 41.36 N ANISOU 726 N ILE B 259 4667 6725 4324 -1255 378 -223 N ATOM 727 CA ILE B 259 220.737 37.729 24.324 1.00 42.18 C ANISOU 727 CA ILE B 259 4894 6736 4396 -1182 445 124 C ATOM 728 C ILE B 259 219.316 37.154 24.314 1.00 39.02 C ANISOU 728 C ILE B 259 4630 6304 3892 -937 275 78 C ATOM 729 O ILE B 259 218.336 37.901 24.371 1.00 40.07 O ANISOU 729 O ILE B 259 4904 6167 4155 -894 280 278 O ATOM 730 CB ILE B 259 221.264 37.980 22.874 1.00 51.23 C ANISOU 730 CB ILE B 259 5922 8241 5300 -1186 609 443 C ATOM 731 CG1 ILE B 259 220.349 38.954 22.135 1.00 54.65 C ANISOU 731 CG1 ILE B 259 6449 8564 5750 -1127 692 888 C ATOM 732 CG2 ILE B 259 221.309 36.705 22.076 1.00 53.62 C ANISOU 732 CG2 ILE B 259 6127 9033 5215 -994 528 269 C ATOM 733 CD1 ILE B 259 219.954 40.150 22.966 1.00 60.41 C ANISOU 733 CD1 ILE B 259 7299 8721 6934 -1259 753 1012 C ATOM 734 N LEU B 260 219.215 35.831 24.261 1.00 37.61 N ANISOU 734 N LEU B 260 4389 6376 3527 -780 131 -187 N ATOM 735 CA LEU B 260 217.923 35.151 24.336 1.00 36.48 C ANISOU 735 CA LEU B 260 4336 6194 3329 -564 -45 -276 C ATOM 736 C LEU B 260 217.240 35.409 25.680 1.00 35.64 C ANISOU 736 C LEU B 260 4352 5694 3496 -572 -135 -359 C ATOM 737 O LEU B 260 216.053 35.733 25.723 1.00 31.07 O ANISOU 737 O LEU B 260 3907 4934 2966 -463 -191 -235 O ATOM 738 CB LEU B 260 218.092 33.643 24.110 1.00 37.39 C ANISOU 738 CB LEU B 260 4314 6597 3297 -420 -167 -585 C ATOM 739 CG LEU B 260 218.636 33.189 22.744 1.00 38.75 C ANISOU 739 CG LEU B 260 4342 7226 3154 -366 -95 -605 C ATOM 740 CD1 LEU B 260 218.714 31.658 22.706 1.00 36.06 C ANISOU 740 CD1 LEU B 260 3855 7060 2788 -219 -220 -991 C ATOM 741 CD2 LEU B 260 217.727 33.694 21.607 1.00 38.88 C ANISOU 741 CD2 LEU B 260 4426 7426 2919 -267 -80 -337 C ATOM 742 N TRP B 261 217.981 35.292 26.788 1.00 28.79 N ANISOU 742 N TRP B 261 3417 4735 2789 -696 -145 -564 N ATOM 743 CA TRP B 261 217.373 35.566 28.090 1.00 31.63 C ANISOU 743 CA TRP B 261 3860 4805 3353 -703 -220 -664 C ATOM 744 C TRP B 261 216.836 36.985 28.117 1.00 32.53 C ANISOU 744 C TRP B 261 4125 4591 3642 -785 -108 -465 C ATOM 745 O TRP B 261 215.736 37.244 28.613 1.00 29.63 O ANISOU 745 O TRP B 261 3880 3998 3380 -684 -166 -444 O ATOM 746 CB TRP B 261 218.405 35.443 29.233 1.00 35.84 C ANISOU 746 CB TRP B 261 4260 5370 3990 -861 -224 -890 C ATOM 747 CG TRP B 261 218.784 34.074 29.627 1.00 36.03 C ANISOU 747 CG TRP B 261 4114 5630 3947 -762 -345 -1068 C ATOM 748 CD1 TRP B 261 220.016 33.485 29.467 1.00 36.96 C ANISOU 748 CD1 TRP B 261 4037 5996 4010 -829 -311 -1160 C ATOM 749 CD2 TRP B 261 217.968 33.118 30.302 1.00 34.61 C ANISOU 749 CD2 TRP B 261 3906 5443 3801 -575 -506 -1147 C ATOM 750 NE1 TRP B 261 220.001 32.216 29.993 1.00 36.73 N ANISOU 750 NE1 TRP B 261 3859 6090 4006 -685 -438 -1283 N ATOM 751 CE2 TRP B 261 218.748 31.964 30.512 1.00 35.51 C ANISOU 751 CE2 TRP B 261 3824 5730 3939 -507 -530 -1214 C ATOM 752 CE3 TRP B 261 216.645 33.132 30.770 1.00 36.73 C ANISOU 752 CE3 TRP B 261 4294 5532 4130 -435 -601 -1104 C ATOM 753 CZ2 TRP B 261 218.258 30.825 31.139 1.00 34.90 C ANISOU 753 CZ2 TRP B 261 3704 5564 3994 -300 -588 -1143 C ATOM 754 CZ3 TRP B 261 216.157 32.003 31.411 1.00 37.65 C ANISOU 754 CZ3 TRP B 261 4337 5633 4334 -250 -691 -1074 C ATOM 755 CH2 TRP B 261 216.955 30.861 31.577 1.00 34.23 C ANISOU 755 CH2 TRP B 261 3738 5302 3965 -190 -661 -1063 C ATOM 756 N GLN B 262 217.639 37.920 27.615 1.00 33.27 N ANISOU 756 N GLN B 262 4190 4638 3813 -969 67 -309 N ATOM 757 CA GLN B 262 217.251 39.322 27.655 1.00 38.66 C ANISOU 757 CA GLN B 262 4976 4945 4769 -1065 203 -110 C ATOM 758 C GLN B 262 216.024 39.611 26.800 1.00 34.39 C ANISOU 758 C GLN B 262 4554 4335 4179 -876 206 220 C ATOM 759 O GLN B 262 215.238 40.493 27.132 1.00 35.54 O ANISOU 759 O GLN B 262 4806 4120 4579 -861 257 333 O ATOM 760 CB GLN B 262 218.399 40.219 27.199 1.00 45.33 C ANISOU 760 CB GLN B 262 5721 5745 5757 -1305 402 42 C ATOM 761 CG GLN B 262 219.529 40.318 28.222 1.00 50.68 C ANISOU 761 CG GLN B 262 6279 6392 6584 -1541 416 -282 C ATOM 762 N MET B 263 215.891 38.903 25.683 1.00 34.30 N ANISOU 762 N MET B 263 4498 4687 3846 -735 160 363 N ATOM 763 CA MET B 263 214.728 39.112 24.812 1.00 35.12 C ANISOU 763 CA MET B 263 4676 4824 3842 -551 141 681 C ATOM 764 C MET B 263 213.450 38.437 25.323 1.00 32.36 C ANISOU 764 C MET B 263 4421 4408 3465 -347 -52 536 C ATOM 765 O MET B 263 212.369 38.991 25.148 1.00 33.83 O ANISOU 765 O MET B 263 4699 4420 3735 -234 -51 774 O ATOM 766 CB MET B 263 214.993 38.636 23.386 1.00 36.67 C ANISOU 766 CB MET B 263 4761 5513 3658 -472 157 861 C ATOM 767 CG MET B 263 215.948 39.536 22.603 1.00 40.66 C ANISOU 767 CG MET B 263 5164 6108 4177 -630 380 1195 C ATOM 768 SD MET B 263 215.954 39.110 20.842 1.00 53.81 S ANISOU 768 SD MET B 263 6683 8444 5317 -487 404 1476 S ATOM 769 CE MET B 263 216.483 37.400 20.936 1.00 48.30 C ANISOU 769 CE MET B 263 5895 8127 4328 -418 234 903 C ATOM 770 N PHE B 264 213.564 37.223 25.859 1.00 29.65 N ANISOU 770 N PHE B 264 4027 4220 3018 -289 -209 193 N ATOM 771 CA PHE B 264 212.369 36.428 26.228 1.00 31.46 C ANISOU 771 CA PHE B 264 4302 4428 3223 -90 -396 84 C ATOM 772 C PHE B 264 211.927 36.585 27.700 1.00 33.30 C ANISOU 772 C PHE B 264 4601 4345 3706 -94 -442 -78 C ATOM 773 O PHE B 264 210.725 36.494 28.041 1.00 29.69 O ANISOU 773 O PHE B 264 4216 3755 3311 58 -535 -37 O ATOM 774 CB PHE B 264 212.561 34.951 25.844 1.00 29.85 C ANISOU 774 CB PHE B 264 3967 4564 2810 11 -538 -152 C ATOM 775 CG PHE B 264 212.477 34.704 24.346 1.00 32.05 C ANISOU 775 CG PHE B 264 4182 5209 2789 90 -537 -32 C ATOM 776 CD1 PHE B 264 213.570 34.934 23.531 1.00 33.28 C ANISOU 776 CD1 PHE B 264 4245 5627 2771 -18 -400 34 C ATOM 777 CD2 PHE B 264 211.299 34.277 23.758 1.00 32.90 C ANISOU 777 CD2 PHE B 264 4296 5438 2766 268 -671 14 C ATOM 778 CE1 PHE B 264 213.493 34.724 22.148 1.00 38.43 C ANISOU 778 CE1 PHE B 264 4810 6705 3086 65 -391 137 C ATOM 779 CE2 PHE B 264 211.206 34.079 22.379 1.00 33.24 C ANISOU 779 CE2 PHE B 264 4251 5901 2478 339 -678 95 C ATOM 780 CZ PHE B 264 212.308 34.296 21.574 1.00 41.34 C ANISOU 780 CZ PHE B 264 5181 7232 3294 243 -535 153 C ATOM 781 N GLY B 265 212.901 36.816 28.564 1.00 29.03 N ANISOU 781 N GLY B 265 4013 3733 3285 -266 -378 -265 N ATOM 782 CA GLY B 265 212.651 36.989 29.989 1.00 28.77 C ANISOU 782 CA GLY B 265 4001 3505 3427 -289 -411 -458 C ATOM 783 C GLY B 265 211.553 37.999 30.276 1.00 31.72 C ANISOU 783 C GLY B 265 4517 3541 3994 -228 -355 -329 C ATOM 784 O GLY B 265 210.697 37.746 31.113 1.00 29.03 O ANISOU 784 O GLY B 265 4202 3127 3701 -107 -444 -420 O ATOM 785 N PRO B 266 211.556 39.151 29.579 1.00 32.80 N ANISOU 785 N PRO B 266 4724 3468 4269 -300 -196 -88 N ATOM 786 CA PRO B 266 210.521 40.134 29.921 1.00 31.22 C ANISOU 786 CA PRO B 266 4638 2899 4326 -231 -125 27 C ATOM 787 C PRO B 266 209.086 39.652 29.646 1.00 27.70 C ANISOU 787 C PRO B 266 4255 2487 3785 27 -253 196 C ATOM 788 O PRO B 266 208.151 40.280 30.157 1.00 28.69 O ANISOU 788 O PRO B 266 4456 2329 4115 116 -217 239 O ATOM 789 CB PRO B 266 210.891 41.351 29.052 1.00 33.59 C ANISOU 789 CB PRO B 266 4953 2984 4826 -349 79 334 C ATOM 790 CG PRO B 266 212.391 41.207 28.845 1.00 33.80 C ANISOU 790 CG PRO B 266 4868 3203 4772 -565 137 225 C ATOM 791 CD PRO B 266 212.573 39.718 28.672 1.00 31.75 C ANISOU 791 CD PRO B 266 4542 3383 4140 -464 -47 82 C ATOM 792 N PHE B 267 208.912 38.544 28.935 1.00 30.33 N ANISOU 792 N PHE B 267 4535 3151 3839 143 -399 245 N ATOM 793 CA PHE B 267 207.558 38.110 28.529 1.00 33.65 C ANISOU 793 CA PHE B 267 4986 3623 4176 369 -527 412 C ATOM 794 C PHE B 267 206.890 37.106 29.466 1.00 35.10 C ANISOU 794 C PHE B 267 5135 3850 4351 496 -696 201 C ATOM 795 O PHE B 267 205.689 36.875 29.386 1.00 31.58 O ANISOU 795 O PHE B 267 4710 3377 3912 670 -791 321 O ATOM 796 CB PHE B 267 207.563 37.538 27.111 1.00 25.91 C ANISOU 796 CB PHE B 267 3942 2990 2912 434 -594 580 C ATOM 797 CG PHE B 267 207.722 38.587 26.036 1.00 29.12 C ANISOU 797 CG PHE B 267 4365 3397 3302 391 -437 953 C ATOM 798 CD1 PHE B 267 206.618 39.267 25.533 1.00 30.78 C ANISOU 798 CD1 PHE B 267 4619 3502 3573 528 -414 1314 C ATOM 799 CD2 PHE B 267 208.982 38.885 25.515 1.00 30.80 C ANISOU 799 CD2 PHE B 267 4516 3737 3448 221 -307 990 C ATOM 800 CE1 PHE B 267 206.762 40.240 24.546 1.00 34.21 C ANISOU 800 CE1 PHE B 267 5028 3955 4016 503 -258 1740 C ATOM 801 CE2 PHE B 267 209.132 39.856 24.540 1.00 35.96 C ANISOU 801 CE2 PHE B 267 5148 4405 4108 186 -147 1401 C ATOM 802 CZ PHE B 267 208.020 40.530 24.045 1.00 35.96 C ANISOU 802 CZ PHE B 267 5182 4303 4177 331 -122 1795 C ATOM 803 N GLY B 268 207.655 36.492 30.350 1.00 29.59 N ANISOU 803 N GLY B 268 3361 3983 3899 -1134 394 359 N ATOM 804 CA GLY B 268 207.084 35.465 31.200 1.00 29.42 C ANISOU 804 CA GLY B 268 3565 3744 3870 -1035 264 267 C ATOM 805 C GLY B 268 208.176 34.525 31.671 1.00 31.46 C ANISOU 805 C GLY B 268 3810 4229 3913 -830 153 116 C ATOM 806 O GLY B 268 209.388 34.818 31.471 1.00 31.00 O ANISOU 806 O GLY B 268 3555 4490 3733 -803 193 86 O ATOM 807 N ALA B 269 207.763 33.421 32.297 1.00 28.34 N ANISOU 807 N ALA B 269 3615 3673 3479 -688 18 30 N ATOM 808 CA ALA B 269 208.710 32.488 32.929 1.00 28.66 C ANISOU 808 CA ALA B 269 3655 3891 3342 -499 -88 -103 C ATOM 809 C ALA B 269 209.448 31.745 31.831 1.00 26.03 C ANISOU 809 C ALA B 269 3265 3821 2803 -240 -154 -134 C ATOM 810 O ALA B 269 208.830 31.191 30.918 1.00 25.72 O ANISOU 810 O ALA B 269 3337 3701 2735 -117 -206 -108 O ATOM 811 CB ALA B 269 207.980 31.483 33.839 1.00 27.04 C ANISOU 811 CB ALA B 269 3688 3422 3164 -410 -211 -174 C ATOM 812 N VAL B 270 210.773 31.770 31.897 1.00 27.46 N ANISOU 812 N VAL B 270 3266 4325 2842 -170 -143 -188 N ATOM 813 CA VAL B 270 211.601 31.125 30.882 1.00 26.63 C ANISOU 813 CA VAL B 270 3085 4493 2542 69 -189 -223 C ATOM 814 C VAL B 270 212.401 30.083 31.642 1.00 28.06 C ANISOU 814 C VAL B 270 3286 4792 2584 272 -295 -339 C ATOM 815 O VAL B 270 213.013 30.420 32.660 1.00 28.81 O ANISOU 815 O VAL B 270 3287 4976 2685 178 -276 -369 O ATOM 816 CB VAL B 270 212.558 32.150 30.188 1.00 27.70 C ANISOU 816 CB VAL B 270 2958 4934 2631 -25 -68 -169 C ATOM 817 CG1 VAL B 270 213.620 31.436 29.355 1.00 30.00 C ANISOU 817 CG1 VAL B 270 3154 5538 2708 228 -115 -226 C ATOM 818 CG2 VAL B 270 211.755 33.147 29.325 1.00 25.13 C ANISOU 818 CG2 VAL B 270 2604 4499 2444 -210 39 -36 C ATOM 819 N THR B 271 212.409 28.827 31.195 1.00 29.13 N ANISOU 819 N THR B 271 3537 4931 2598 542 -401 -401 N ATOM 820 CA THR B 271 213.110 27.796 31.983 1.00 34.96 C ANISOU 820 CA THR B 271 4300 5757 3227 742 -500 -498 C ATOM 821 C THR B 271 214.398 27.323 31.355 1.00 37.21 C ANISOU 821 C THR B 271 4429 6384 3324 956 -509 -543 C ATOM 822 O THR B 271 215.166 26.607 31.987 1.00 40.09 O ANISOU 822 O THR B 271 4763 6872 3598 1112 -573 -606 O ATOM 823 CB THR B 271 212.254 26.557 32.285 1.00 35.57 C ANISOU 823 CB THR B 271 4633 5565 3316 910 -619 -553 C ATOM 824 OG1 THR B 271 211.740 26.011 31.065 1.00 38.21 O ANISOU 824 OG1 THR B 271 5071 5844 3605 1046 -639 -552 O ATOM 825 CG2 THR B 271 211.064 26.922 33.210 1.00 44.85 C ANISOU 825 CG2 THR B 271 5967 6398 4677 706 -623 -521 C ATOM 826 N ASN B 272 214.656 27.727 30.120 1.00 34.01 N ANISOU 826 N ASN B 272 3919 6138 2864 964 -442 -505 N ATOM 827 CA ASN B 272 215.885 27.288 29.461 1.00 37.66 C ANISOU 827 CA ASN B 272 4231 6927 3150 1168 -442 -550 C ATOM 828 C ASN B 272 216.106 28.046 28.154 1.00 38.58 C ANISOU 828 C ASN B 272 4212 7217 3230 1104 -347 -490 C ATOM 829 O ASN B 272 215.148 28.386 27.486 1.00 35.30 O ANISOU 829 O ASN B 272 3883 6638 2890 1005 -319 -430 O ATOM 830 CB ASN B 272 215.801 25.782 29.188 1.00 42.48 C ANISOU 830 CB ASN B 272 5001 7477 3663 1467 -543 -635 C ATOM 831 CG ASN B 272 217.030 25.240 28.445 1.00 51.55 C ANISOU 831 CG ASN B 272 6007 8943 4635 1695 -533 -685 C ATOM 832 OD1 ASN B 272 217.135 25.362 27.217 1.00 55.08 O ANISOU 832 OD1 ASN B 272 6407 9507 5016 1732 -484 -674 O ATOM 833 ND2 ASN B 272 217.951 24.622 29.188 1.00 50.98 N ANISOU 833 ND2 ASN B 272 5864 8979 4528 1832 -565 -729 N ATOM 834 N VAL B 273 217.367 28.312 27.802 1.00 35.00 N ANISOU 834 N VAL B 273 3540 7098 2660 1158 -298 -500 N ATOM 835 CA VAL B 273 217.695 28.911 26.519 1.00 36.50 C ANISOU 835 CA VAL B 273 3594 7482 2792 1129 -213 -451 C ATOM 836 C VAL B 273 218.945 28.207 26.043 1.00 40.57 C ANISOU 836 C VAL B 273 3991 8300 3125 1373 -229 -522 C ATOM 837 O VAL B 273 219.765 27.749 26.858 1.00 36.02 O ANISOU 837 O VAL B 273 3353 7839 2492 1481 -271 -576 O ATOM 838 CB VAL B 273 218.001 30.426 26.624 1.00 42.17 C ANISOU 838 CB VAL B 273 4113 8315 3594 857 -93 -363 C ATOM 839 CG1 VAL B 273 216.893 31.156 27.399 1.00 39.94 C ANISOU 839 CG1 VAL B 273 3932 7731 3514 603 -65 -300 C ATOM 840 CG2 VAL B 273 219.364 30.641 27.283 1.00 48.37 C ANISOU 840 CG2 VAL B 273 4693 9385 4299 872 -73 -401 C ATOM 841 N LYS B 274 219.096 28.126 24.733 1.00 36.74 N ANISOU 841 N LYS B 274 3466 7946 2547 1455 -193 -517 N ATOM 842 CA LYS B 274 220.243 27.455 24.146 1.00 43.03 C ANISOU 842 CA LYS B 274 4155 9023 3173 1688 -194 -586 C ATOM 843 C LYS B 274 220.576 28.093 22.807 1.00 46.90 C ANISOU 843 C LYS B 274 4504 9711 3606 1639 -105 -537 C ATOM 844 O LYS B 274 219.697 28.282 21.985 1.00 46.81 O ANISOU 844 O LYS B 274 4583 9590 3614 1569 -87 -493 O ATOM 845 CB LYS B 274 219.897 25.990 23.918 1.00 42.66 C ANISOU 845 CB LYS B 274 4297 8787 3123 1924 -271 -666 C ATOM 846 CG LYS B 274 220.994 25.195 23.256 1.00 50.58 C ANISOU 846 CG LYS B 274 5200 9990 4029 2155 -263 -726 C ATOM 847 CD LYS B 274 221.826 24.469 24.285 1.00 51.51 C ANISOU 847 CD LYS B 274 5274 10172 4124 2320 -311 -780 C ATOM 848 CE LYS B 274 222.360 23.185 23.656 1.00 55.13 C ANISOU 848 CE LYS B 274 5760 10673 4515 2599 -339 -852 C ATOM 849 N VAL B 275 221.847 28.411 22.576 1.00 45.13 N ANISOU 849 N VAL B 275 4057 9772 3319 1673 -59 -536 N ATOM 850 CA VAL B 275 222.283 28.826 21.245 1.00 46.68 C ANISOU 850 CA VAL B 275 4129 10138 3470 1656 -4 -496 C ATOM 851 C VAL B 275 223.017 27.648 20.626 1.00 45.30 C ANISOU 851 C VAL B 275 3961 10048 3204 1918 -53 -577 C ATOM 852 O VAL B 275 223.866 27.044 21.267 1.00 45.78 O ANISOU 852 O VAL B 275 3971 10198 3225 2066 -96 -630 O ATOM 853 CB VAL B 275 223.216 30.056 21.318 1.00 48.65 C ANISOU 853 CB VAL B 275 4148 10605 3732 1483 56 -425 C ATOM 854 CG1 VAL B 275 223.916 30.307 19.975 1.00 48.42 C ANISOU 854 CG1 VAL B 275 4010 10753 3633 1502 77 -396 C ATOM 855 CG2 VAL B 275 222.417 31.287 21.788 1.00 44.93 C ANISOU 855 CG2 VAL B 275 3669 10011 3392 1197 129 -334 C ATOM 856 N ILE B 276 222.657 27.284 19.404 1.00 43.32 N ANISOU 856 N ILE B 276 3777 9764 2919 1972 -45 -584 N ATOM 857 CA ILE B 276 223.251 26.117 18.780 1.00 42.56 C ANISOU 857 CA ILE B 276 3707 9720 2743 2208 -81 -666 C ATOM 858 C ILE B 276 224.531 26.539 18.091 1.00 44.24 C ANISOU 858 C ILE B 276 3713 10225 2873 2219 -52 -646 C ATOM 859 O ILE B 276 224.558 27.521 17.349 1.00 47.75 O ANISOU 859 O ILE B 276 4056 10772 3315 2059 1 -573 O ATOM 860 CB ILE B 276 222.304 25.436 17.765 1.00 45.99 C ANISOU 860 CB ILE B 276 4321 9983 3169 2255 -88 -696 C ATOM 861 CG1 ILE B 276 221.015 25.030 18.484 1.00 44.97 C ANISOU 861 CG1 ILE B 276 4420 9540 3127 2228 -135 -709 C ATOM 862 CG2 ILE B 276 222.988 24.196 17.174 1.00 50.46 C ANISOU 862 CG2 ILE B 276 4912 10605 3654 2492 -116 -788 C ATOM 863 CD1 ILE B 276 221.298 24.094 19.653 1.00 46.73 C ANISOU 863 CD1 ILE B 276 4715 9668 3374 2396 -202 -782 C ATOM 864 N ARG B 277 225.585 25.795 18.356 1.00 46.16 N ANISOU 864 N ARG B 277 3903 10589 3048 2402 -91 -702 N ATOM 865 CA ARG B 277 226.904 26.113 17.817 1.00 49.14 C ANISOU 865 CA ARG B 277 4105 11232 3333 2420 -76 -686 C ATOM 866 C ARG B 277 227.513 24.916 17.134 1.00 51.85 C ANISOU 866 C ARG B 277 4485 11627 3588 2650 -96 -764 C ATOM 867 O ARG B 277 227.202 23.769 17.439 1.00 51.20 O ANISOU 867 O ARG B 277 4544 11399 3511 2820 -137 -832 O ATOM 868 CB ARG B 277 227.838 26.568 18.951 1.00 53.04 C ANISOU 868 CB ARG B 277 4477 11865 3809 2377 -96 -660 C ATOM 869 CG ARG B 277 227.416 27.877 19.616 1.00 54.88 C ANISOU 869 CG ARG B 277 4658 12067 4128 2116 -61 -583 C ATOM 870 CD ARG B 277 228.391 28.279 20.715 1.00 59.38 C ANISOU 870 CD ARG B 277 5123 12772 4667 2061 -75 -568 C ATOM 871 NE ARG B 277 228.109 29.634 21.179 1.00 62.45 N ANISOU 871 NE ARG B 277 5458 13128 5141 1783 -24 -495 N ATOM 872 CZ ARG B 277 227.352 29.945 22.227 1.00 69.54 C ANISOU 872 CZ ARG B 277 6408 13881 6134 1662 -19 -483 C ATOM 873 NH1 ARG B 277 226.791 29.000 22.979 1.00 68.78 N ANISOU 873 NH1 ARG B 277 6417 13662 6053 1801 -69 -541 N ATOM 874 NH2 ARG B 277 227.166 31.221 22.537 1.00 75.09 N ANISOU 874 NH2 ARG B 277 7063 14541 6927 1397 39 -414 N ATOM 875 N ASP B 278 228.426 25.204 16.220 1.00 50.61 N ANISOU 875 N ASP B 278 4204 11673 3351 2649 -65 -751 N ATOM 876 CA ASP B 278 229.201 24.192 15.536 1.00 56.69 C ANISOU 876 CA ASP B 278 4981 12527 4031 2849 -67 -820 C ATOM 877 C ASP B 278 230.313 23.621 16.440 1.00 58.22 C ANISOU 877 C ASP B 278 5126 12825 4169 2997 -105 -843 C ATOM 878 O ASP B 278 230.331 22.423 16.750 1.00 56.82 O ANISOU 878 O ASP B 278 5057 12552 3978 3187 -136 -906 O ATOM 879 CB ASP B 278 229.806 24.850 14.304 1.00 58.44 C ANISOU 879 CB ASP B 278 5076 12937 4191 2770 -15 -790 C ATOM 880 CG ASP B 278 230.885 24.033 13.687 1.00 66.02 C ANISOU 880 CG ASP B 278 5999 14032 5052 2949 -5 -851 C ATOM 881 OD1 ASP B 278 230.536 23.191 12.830 1.00 66.45 O ANISOU 881 OD1 ASP B 278 6153 14011 5083 3050 15 -917 O ATOM 882 OD2 ASP B 278 232.065 24.257 14.045 1.00 56.90 O ANISOU 882 OD2 ASP B 278 4721 13054 3843 2975 -9 -831 O ATOM 883 N LYS B 283 231.215 28.869 16.849 1.00 67.41 N ANISOU 883 N LYS B 283 5837 14358 5418 2148 9 -535 N ATOM 884 CA LYS B 283 230.377 29.893 16.228 1.00 66.42 C ANISOU 884 CA LYS B 283 5714 14154 5368 1943 54 -466 C ATOM 885 C LYS B 283 228.910 29.451 16.102 1.00 63.43 C ANISOU 885 C LYS B 283 5473 13563 5063 1956 52 -479 C ATOM 886 O LYS B 283 228.615 28.302 15.752 1.00 61.99 O ANISOU 886 O LYS B 283 5383 13320 4849 2143 28 -551 O ATOM 887 CB LYS B 283 230.925 30.280 14.854 1.00 69.21 C ANISOU 887 CB LYS B 283 5985 14652 5660 1923 89 -442 C ATOM 888 N CYS B 284 227.996 30.376 16.360 1.00 59.88 N ANISOU 888 N CYS B 284 5050 12986 4716 1749 85 -407 N ATOM 889 CA CYS B 284 226.588 30.043 16.346 1.00 57.28 C ANISOU 889 CA CYS B 284 4856 12449 4458 1740 88 -410 C ATOM 890 C CYS B 284 226.162 29.625 14.942 1.00 59.14 C ANISOU 890 C CYS B 284 5136 12687 4647 1804 105 -421 C ATOM 891 O CYS B 284 226.617 30.211 13.958 1.00 59.20 O ANISOU 891 O CYS B 284 5048 12832 4612 1736 136 -376 O ATOM 892 CB CYS B 284 225.756 31.241 16.782 1.00 57.02 C ANISOU 892 CB CYS B 284 4831 12290 4545 1484 134 -313 C ATOM 893 SG CYS B 284 224.014 30.905 16.655 1.00 59.75 S ANISOU 893 SG CYS B 284 5349 12388 4965 1457 147 -299 S ATOM 894 N LYS B 285 225.291 28.619 14.853 1.00 57.75 N ANISOU 894 N LYS B 285 5119 12347 4478 1925 85 -483 N ATOM 895 CA LYS B 285 224.846 28.091 13.559 1.00 60.02 C ANISOU 895 CA LYS B 285 5477 12615 4712 1982 101 -508 C ATOM 896 C LYS B 285 223.750 28.949 12.944 1.00 59.30 C ANISOU 896 C LYS B 285 5412 12449 4671 1779 144 -408 C ATOM 897 O LYS B 285 223.257 28.653 11.849 1.00 61.04 O ANISOU 897 O LYS B 285 5691 12656 4845 1785 159 -412 O ATOM 898 CB LYS B 285 224.329 26.655 13.696 1.00 62.12 C ANISOU 898 CB LYS B 285 5936 12702 4965 2174 59 -616 C ATOM 899 CG LYS B 285 225.401 25.587 13.816 1.00 64.15 C ANISOU 899 CG LYS B 285 6178 13046 5150 2404 24 -714 C ATOM 900 CD LYS B 285 224.751 24.208 13.877 1.00 64.94 C ANISOU 900 CD LYS B 285 6489 12932 5253 2569 -14 -810 C ATOM 901 CE LYS B 285 225.765 23.091 13.666 1.00 65.57 C ANISOU 901 CE LYS B 285 6562 13100 5253 2794 -31 -900 C ATOM 902 NZ LYS B 285 225.175 21.731 13.877 1.00 66.58 N ANISOU 902 NZ LYS B 285 6899 13002 5397 2952 -71 -989 N ATOM 903 N GLY B 286 223.355 30.005 13.641 1.00 52.86 N ANISOU 903 N GLY B 286 4556 11580 3948 1591 167 -314 N ATOM 904 CA GLY B 286 222.309 30.863 13.123 1.00 52.51 C ANISOU 904 CA GLY B 286 4531 11457 3962 1392 211 -198 C ATOM 905 C GLY B 286 220.979 30.756 13.859 1.00 49.76 C ANISOU 905 C GLY B 286 4348 10860 3698 1327 205 -175 C ATOM 906 O GLY B 286 220.069 31.526 13.590 1.00 48.34 O ANISOU 906 O GLY B 286 4183 10602 3583 1147 243 -59 O ATOM 907 N PHE B 287 220.850 29.806 14.775 1.00 35.91 N ANISOU 907 N PHE B 287 3936 6515 3193 305 45 -309 N ATOM 908 CA PHE B 287 219.573 29.636 15.479 1.00 34.44 C ANISOU 908 CA PHE B 287 3830 6125 3130 288 9 -184 C ATOM 909 C PHE B 287 219.733 29.225 16.936 1.00 36.82 C ANISOU 909 C PHE B 287 4131 6383 3476 373 -4 -182 C ATOM 910 O PHE B 287 220.842 28.921 17.401 1.00 38.36 O ANISOU 910 O PHE B 287 4269 6697 3608 464 3 -281 O ATOM 911 CB PHE B 287 218.665 28.646 14.735 1.00 37.66 C ANISOU 911 CB PHE B 287 4341 6399 3570 318 -79 -153 C ATOM 912 CG PHE B 287 219.291 27.299 14.474 1.00 39.81 C ANISOU 912 CG PHE B 287 4650 6692 3783 466 -152 -268 C ATOM 913 CD1 PHE B 287 219.140 26.263 15.381 1.00 40.93 C ANISOU 913 CD1 PHE B 287 4857 6728 3967 579 -221 -270 C ATOM 914 CD2 PHE B 287 220.008 27.062 13.315 1.00 42.79 C ANISOU 914 CD2 PHE B 287 5005 7193 4061 495 -154 -373 C ATOM 915 CE1 PHE B 287 219.703 25.019 15.139 1.00 40.41 C ANISOU 915 CE1 PHE B 287 4841 6668 3846 725 -293 -375 C ATOM 916 CE2 PHE B 287 220.581 25.813 13.065 1.00 41.12 C ANISOU 916 CE2 PHE B 287 4834 6997 3792 646 -222 -485 C ATOM 917 CZ PHE B 287 220.421 24.794 13.976 1.00 38.46 C ANISOU 917 CZ PHE B 287 4572 6542 3501 765 -293 -485 C ATOM 918 N GLY B 288 218.622 29.242 17.672 1.00 32.25 N ANISOU 918 N GLY B 288 3609 5643 3002 340 -22 -67 N ATOM 919 CA GLY B 288 218.648 28.745 19.024 1.00 30.81 C ANISOU 919 CA GLY B 288 3439 5403 2863 414 -45 -57 C ATOM 920 C GLY B 288 217.230 28.511 19.510 1.00 36.65 C ANISOU 920 C GLY B 288 4259 5956 3711 376 -87 70 C ATOM 921 O GLY B 288 216.265 28.636 18.727 1.00 33.64 O ANISOU 921 O GLY B 288 3922 5496 3364 305 -104 144 O ATOM 922 N PHE B 289 217.116 28.152 20.785 1.00 29.96 N ANISOU 922 N PHE B 289 3426 5050 2909 421 -105 96 N ATOM 923 CA PHE B 289 215.825 27.748 21.366 1.00 33.08 C ANISOU 923 CA PHE B 289 3895 5278 3394 395 -154 209 C ATOM 924 C PHE B 289 215.602 28.380 22.728 1.00 35.86 C ANISOU 924 C PHE B 289 4211 5612 3803 359 -101 270 C ATOM 925 O PHE B 289 216.557 28.636 23.490 1.00 33.14 O ANISOU 925 O PHE B 289 3808 5360 3425 395 -60 210 O ATOM 926 CB PHE B 289 215.733 26.211 21.505 1.00 32.48 C ANISOU 926 CB PHE B 289 3914 5112 3314 500 -266 182 C ATOM 927 CG PHE B 289 215.883 25.476 20.195 1.00 32.78 C ANISOU 927 CG PHE B 289 4006 5151 3296 542 -325 121 C ATOM 928 CD1 PHE B 289 217.135 25.124 19.726 1.00 33.71 C ANISOU 928 CD1 PHE B 289 4094 5389 3325 642 -328 -13 C ATOM 929 CD2 PHE B 289 214.769 25.167 19.418 1.00 32.00 C ANISOU 929 CD2 PHE B 289 3983 4945 3229 479 -375 195 C ATOM 930 CE1 PHE B 289 217.291 24.468 18.495 1.00 32.81 C ANISOU 930 CE1 PHE B 289 4030 5283 3154 683 -378 -78 C ATOM 931 CE2 PHE B 289 214.913 24.502 18.187 1.00 31.41 C ANISOU 931 CE2 PHE B 289 3964 4872 3098 512 -428 134 C ATOM 932 CZ PHE B 289 216.169 24.169 17.722 1.00 34.69 C ANISOU 932 CZ PHE B 289 4352 5402 3425 614 -427 -3 C ATOM 933 N VAL B 290 214.335 28.596 23.050 1.00 28.40 N ANISOU 933 N VAL B 290 3300 4553 2939 288 -105 387 N ATOM 934 CA VAL B 290 213.950 29.072 24.380 1.00 28.94 C ANISOU 934 CA VAL B 290 3344 4587 3065 257 -64 451 C ATOM 935 C VAL B 290 212.767 28.231 24.825 1.00 27.81 C ANISOU 935 C VAL B 290 3275 4306 2983 252 -140 541 C ATOM 936 O VAL B 290 211.931 27.854 24.013 1.00 30.51 O ANISOU 936 O VAL B 290 3669 4581 3342 222 -191 591 O ATOM 937 CB VAL B 290 213.553 30.564 24.324 1.00 31.41 C ANISOU 937 CB VAL B 290 3603 4922 3409 154 36 511 C ATOM 938 CG1 VAL B 290 212.776 30.995 25.572 1.00 29.61 C ANISOU 938 CG1 VAL B 290 3368 4630 3253 116 70 597 C ATOM 939 CG2 VAL B 290 214.810 31.431 24.086 1.00 31.79 C ANISOU 939 CG2 VAL B 290 3581 5112 3385 143 114 422 C ATOM 940 N THR B 291 212.693 27.907 26.101 1.00 27.69 N ANISOU 940 N THR B 291 3268 4257 2995 274 -152 562 N ATOM 941 CA THR B 291 211.537 27.175 26.619 1.00 28.87 C ANISOU 941 CA THR B 291 3484 4287 3198 251 -221 655 C ATOM 942 C THR B 291 210.803 28.052 27.618 1.00 31.65 C ANISOU 942 C THR B 291 3789 4625 3613 179 -152 741 C ATOM 943 O THR B 291 211.410 28.536 28.585 1.00 29.67 O ANISOU 943 O THR B 291 3489 4426 3357 191 -94 712 O ATOM 944 CB THR B 291 211.993 25.844 27.295 1.00 33.65 C ANISOU 944 CB THR B 291 4158 4851 3776 339 -314 612 C ATOM 945 OG1 THR B 291 212.585 25.006 26.297 1.00 39.57 O ANISOU 945 OG1 THR B 291 4963 5604 4468 415 -381 531 O ATOM 946 CG2 THR B 291 210.818 25.088 27.961 1.00 33.21 C ANISOU 946 CG2 THR B 291 4176 4675 3766 298 -386 712 C ATOM 947 N MET B 292 209.505 28.274 27.378 1.00 30.11 N ANISOU 947 N MET B 292 3605 4367 3470 106 -156 846 N ATOM 948 CA MET B 292 208.681 29.050 28.296 1.00 32.38 C ANISOU 948 CA MET B 292 3848 4638 3815 47 -95 930 C ATOM 949 C MET B 292 207.549 28.222 28.905 1.00 33.29 C ANISOU 949 C MET B 292 4010 4672 3967 16 -165 1020 C ATOM 950 O MET B 292 206.921 27.408 28.236 1.00 33.91 O ANISOU 950 O MET B 292 4149 4694 4041 0 -248 1057 O ATOM 951 CB MET B 292 208.114 30.286 27.588 1.00 32.33 C ANISOU 951 CB MET B 292 3795 4650 3839 -13 -20 980 C ATOM 952 CG MET B 292 209.190 31.242 27.116 1.00 28.89 C ANISOU 952 CG MET B 292 3315 4297 3364 -5 58 901 C ATOM 953 SD MET B 292 208.580 32.793 26.413 1.00 30.02 S ANISOU 953 SD MET B 292 3418 4450 3539 -75 147 962 S ATOM 954 CE MET B 292 207.886 33.617 27.862 1.00 27.28 C ANISOU 954 CE MET B 292 3034 4078 3254 -102 222 1030 C ATOM 955 N THR B 293 207.270 28.455 30.177 1.00 30.34 N ANISOU 955 N THR B 293 3609 4298 3623 -3 -131 1057 N ATOM 956 CA THR B 293 206.313 27.618 30.912 1.00 31.64 C ANISOU 956 CA THR B 293 3814 4398 3808 -39 -199 1135 C ATOM 957 C THR B 293 204.887 27.806 30.426 1.00 35.23 C ANISOU 957 C THR B 293 4259 4825 4302 -112 -208 1243 C ATOM 958 O THR B 293 204.120 26.846 30.277 1.00 36.88 O ANISOU 958 O THR B 293 4527 4979 4506 -148 -298 1300 O ATOM 959 CB THR B 293 206.391 27.974 32.390 1.00 27.62 C ANISOU 959 CB THR B 293 3264 3912 3317 -48 -147 1145 C ATOM 960 OG1 THR B 293 207.759 27.834 32.792 1.00 29.07 O ANISOU 960 OG1 THR B 293 3450 4137 3460 21 -139 1045 O ATOM 961 CG2 THR B 293 205.494 27.058 33.253 1.00 31.99 C ANISOU 961 CG2 THR B 293 3861 4412 3881 -91 -220 1222 C ATOM 962 N ASN B 294 204.513 29.055 30.197 1.00 31.86 N ANISOU 962 N ASN B 294 3760 4436 3910 -138 -116 1275 N ATOM 963 CA ASN B 294 203.099 29.350 30.021 1.00 32.31 C ANISOU 963 CA ASN B 294 3788 4481 4009 -200 -113 1385 C ATOM 964 C ASN B 294 202.747 29.560 28.534 1.00 31.12 C ANISOU 964 C ASN B 294 3643 4327 3856 -216 -130 1407 C ATOM 965 O ASN B 294 203.322 30.424 27.865 1.00 31.00 O ANISOU 965 O ASN B 294 3602 4342 3837 -195 -70 1363 O ATOM 966 CB ASN B 294 202.702 30.549 30.893 1.00 35.98 C ANISOU 966 CB ASN B 294 4172 4981 4516 -212 -6 1420 C ATOM 967 CG ASN B 294 202.888 30.263 32.392 1.00 44.06 C ANISOU 967 CG ASN B 294 5191 6011 5540 -211 4 1410 C ATOM 968 OD1 ASN B 294 202.450 29.220 32.885 1.00 49.87 O ANISOU 968 OD1 ASN B 294 5966 6719 6265 -238 -75 1447 O ATOM 969 ND2 ASN B 294 203.567 31.169 33.109 1.00 43.01 N ANISOU 969 ND2 ASN B 294 5017 5914 5412 -187 97 1360 N ATOM 970 N TYR B 295 201.813 28.769 28.016 1.00 39.47 N ANISOU 970 N TYR B 295 5341 5414 4243 -1335 239 442 N ATOM 971 CA TYR B 295 201.495 28.851 26.578 1.00 44.09 C ANISOU 971 CA TYR B 295 5596 6105 5052 -1279 211 271 C ATOM 972 C TYR B 295 201.193 30.279 26.104 1.00 32.97 C ANISOU 972 C TYR B 295 4037 4879 3610 -1094 106 120 C ATOM 973 O TYR B 295 201.685 30.715 25.058 1.00 31.74 O ANISOU 973 O TYR B 295 3758 4736 3566 -972 -72 84 O ATOM 974 CB TYR B 295 200.343 27.910 26.202 1.00 53.12 C ANISOU 974 CB TYR B 295 6537 7325 6323 -1451 477 127 C ATOM 975 CG TYR B 295 199.823 28.177 24.813 1.00 62.73 C ANISOU 975 CG TYR B 295 7418 8708 7708 -1398 428 -77 C ATOM 976 CD1 TYR B 295 200.362 27.537 23.703 1.00 63.43 C ANISOU 976 CD1 TYR B 295 7406 8721 7975 -1434 342 -80 C ATOM 977 CD2 TYR B 295 198.795 29.092 24.610 1.00 70.93 C ANISOU 977 CD2 TYR B 295 8249 9973 8728 -1314 462 -265 C ATOM 978 CE1 TYR B 295 199.868 27.798 22.416 1.00 67.22 C ANISOU 978 CE1 TYR B 295 7614 9367 8559 -1402 280 -266 C ATOM 979 CE2 TYR B 295 198.304 29.364 23.342 1.00 72.97 C ANISOU 979 CE2 TYR B 295 8214 10394 9118 -1256 372 -430 C ATOM 980 CZ TYR B 295 198.838 28.718 22.252 1.00 71.45 C ANISOU 980 CZ TYR B 295 7957 10143 9049 -1307 273 -429 C ATOM 981 OH TYR B 295 198.319 29.015 21.013 1.00 74.81 O ANISOU 981 OH TYR B 295 8126 10744 9554 -1265 169 -591 O ATOM 982 N GLU B 296 200.369 31.002 26.851 1.00 34.25 N ANISOU 982 N GLU B 296 4215 5167 3632 -1077 240 28 N ATOM 983 CA GLU B 296 200.008 32.383 26.512 1.00 36.19 C ANISOU 983 CA GLU B 296 4319 5563 3867 -893 172 -107 C ATOM 984 C GLU B 296 201.219 33.317 26.453 1.00 34.41 C ANISOU 984 C GLU B 296 4241 5255 3579 -723 -84 -10 C ATOM 985 O GLU B 296 201.297 34.181 25.580 1.00 32.20 O ANISOU 985 O GLU B 296 3814 5042 3377 -559 -209 -86 O ATOM 986 CB GLU B 296 198.961 32.949 27.504 1.00 37.09 C ANISOU 986 CB GLU B 296 4450 5781 3862 -925 409 -221 C ATOM 987 N GLU B 297 202.157 33.175 27.398 1.00 31.89 N ANISOU 987 N GLU B 297 4216 4787 3115 -763 -165 155 N ATOM 988 CA GLU B 297 203.295 34.074 27.433 1.00 30.48 C ANISOU 988 CA GLU B 297 4161 4528 2891 -619 -398 221 C ATOM 989 C GLU B 297 204.257 33.722 26.282 1.00 28.46 C ANISOU 989 C GLU B 297 3812 4156 2847 -560 -588 277 C ATOM 990 O GLU B 297 204.859 34.600 25.667 1.00 27.91 O ANISOU 990 O GLU B 297 3701 4066 2837 -410 -733 242 O ATOM 991 CB GLU B 297 203.986 33.979 28.811 1.00 31.81 C ANISOU 991 CB GLU B 297 4664 4585 2839 -697 -457 374 C ATOM 992 CG GLU B 297 203.140 34.605 29.948 1.00 33.87 C ANISOU 992 CG GLU B 297 5061 4953 2854 -754 -256 288 C ATOM 993 CD GLU B 297 203.753 34.447 31.318 1.00 44.06 C ANISOU 993 CD GLU B 297 6721 6149 3870 -864 -315 438 C ATOM 994 OE1 GLU B 297 204.576 33.523 31.504 1.00 41.82 O ANISOU 994 OE1 GLU B 297 6575 5719 3595 -927 -472 636 O ATOM 995 OE2 GLU B 297 203.411 35.252 32.222 1.00 49.55 O ANISOU 995 OE2 GLU B 297 7577 6910 4339 -891 -207 359 O ATOM 996 N ALA B 298 204.386 32.436 25.985 1.00 28.69 N ANISOU 996 N ALA B 298 3813 4088 3001 -688 -553 352 N ATOM 997 CA ALA B 298 205.166 31.992 24.820 1.00 31.01 C ANISOU 997 CA ALA B 298 4000 4262 3523 -667 -667 371 C ATOM 998 C ALA B 298 204.589 32.592 23.540 1.00 31.89 C ANISOU 998 C ALA B 298 3881 4522 3714 -577 -658 197 C ATOM 999 O ALA B 298 205.311 33.137 22.723 1.00 27.30 O ANISOU 999 O ALA B 298 3275 3879 3217 -468 -790 180 O ATOM 1000 CB ALA B 298 205.136 30.478 24.733 1.00 30.81 C ANISOU 1000 CB ALA B 298 3959 4121 3627 -843 -560 448 C ATOM 1001 N ALA B 299 203.268 32.483 23.371 1.00 30.34 N ANISOU 1001 N ALA B 299 3519 4517 3493 -627 -501 68 N ATOM 1002 CA ALA B 299 202.597 33.119 22.239 1.00 30.03 C ANISOU 1002 CA ALA B 299 3259 4645 3505 -529 -530 -84 C ATOM 1003 C ALA B 299 202.874 34.628 22.175 1.00 32.08 C ANISOU 1003 C ALA B 299 3557 4940 3693 -312 -652 -104 C ATOM 1004 O ALA B 299 203.138 35.174 21.097 1.00 32.15 O ANISOU 1004 O ALA B 299 3500 4958 3758 -201 -766 -143 O ATOM 1005 CB ALA B 299 201.076 32.837 22.270 1.00 28.40 C ANISOU 1005 CB ALA B 299 2844 4643 3303 -609 -356 -226 C ATOM 1006 N AMET B 300 202.819 35.306 23.317 0.51 29.31 N ANISOU 1006 N AMET B 300 3332 4596 3209 -262 -613 -80 N ATOM 1007 N BMET B 300 202.845 35.293 23.318 0.49 29.36 N ANISOU 1007 N BMET B 300 3341 4598 3216 -263 -615 -77 N ATOM 1008 CA AMET B 300 203.139 36.731 23.326 0.51 28.94 C ANISOU 1008 CA AMET B 300 3333 4554 3109 -69 -700 -105 C ATOM 1009 CA BMET B 300 203.115 36.721 23.348 0.49 29.32 C ANISOU 1009 CA BMET B 300 3381 4605 3156 -71 -696 -106 C ATOM 1010 C AMET B 300 204.566 36.980 22.829 0.51 28.92 C ANISOU 1010 C AMET B 300 3452 4369 3169 1 -877 -26 C ATOM 1011 C BMET B 300 204.566 37.036 22.916 0.49 28.82 C ANISOU 1011 C BMET B 300 3448 4356 3146 5 -875 -26 C ATOM 1012 O AMET B 300 204.799 37.849 21.983 0.51 28.80 O ANISOU 1012 O AMET B 300 3393 4350 3199 149 -955 -70 O ATOM 1013 O BMET B 300 204.815 37.993 22.180 0.49 28.57 O ANISOU 1013 O BMET B 300 3386 4320 3150 160 -951 -69 O ATOM 1014 CB AMET B 300 203.002 37.327 24.730 0.51 33.35 C ANISOU 1014 CB AMET B 300 4048 5119 3504 -68 -612 -101 C ATOM 1015 CB BMET B 300 202.832 37.257 24.753 0.49 33.99 C ANISOU 1015 CB BMET B 300 4110 5219 3585 -81 -588 -111 C ATOM 1016 CG AMET B 300 203.297 38.840 24.754 0.51 34.25 C ANISOU 1016 CG AMET B 300 4204 5228 3582 123 -668 -150 C ATOM 1017 CG BMET B 300 202.232 38.646 24.767 0.49 37.84 C ANISOU 1017 CG BMET B 300 4517 5809 4053 90 -538 -222 C ATOM 1018 SD AMET B 300 202.116 39.790 23.741 0.51 41.20 S ANISOU 1018 SD AMET B 300 4803 6279 4573 310 -622 -286 S ATOM 1019 SD BMET B 300 200.664 38.689 25.627 0.49 63.29 S ANISOU 1019 SD BMET B 300 7625 9188 7233 19 -263 -350 S ATOM 1020 CE AMET B 300 200.570 39.231 24.451 0.51 59.91 C ANISOU 1020 CE AMET B 300 7017 8810 6935 181 -382 -386 C ATOM 1021 CE BMET B 300 201.027 37.626 27.017 0.49 39.66 C ANISOU 1021 CE BMET B 300 4917 6098 4053 -225 -161 -245 C ATOM 1022 N ALA B 301 205.521 36.234 23.377 1.00 28.72 N ANISOU 1022 N ALA B 301 3578 4176 3159 -102 -934 92 N ATOM 1023 CA ALA B 301 206.925 36.453 23.023 1.00 27.41 C ANISOU 1023 CA ALA B 301 3505 3812 3099 -44 -1091 154 C ATOM 1024 C ALA B 301 207.054 36.245 21.512 1.00 30.03 C ANISOU 1024 C ALA B 301 3708 4114 3589 -26 -1106 98 C ATOM 1025 O ALA B 301 207.666 37.041 20.806 1.00 28.86 O ANISOU 1025 O ALA B 301 3577 3893 3497 90 -1174 64 O ATOM 1026 CB ALA B 301 207.844 35.497 23.785 1.00 25.56 C ANISOU 1026 CB ALA B 301 3406 3397 2907 -163 -1166 301 C ATOM 1027 N ILE B 302 206.449 35.177 21.015 1.00 29.84 N ANISOU 1027 N ILE B 302 3570 4145 3624 -158 -1022 79 N ATOM 1028 CA ILE B 302 206.560 34.860 19.604 1.00 29.52 C ANISOU 1028 CA ILE B 302 3434 4078 3702 -184 -1025 15 C ATOM 1029 C ILE B 302 205.918 35.919 18.713 1.00 30.78 C ANISOU 1029 C ILE B 302 3512 4398 3786 -41 -1057 -86 C ATOM 1030 O ILE B 302 206.496 36.305 17.699 1.00 30.28 O ANISOU 1030 O ILE B 302 3482 4250 3771 14 -1111 -111 O ATOM 1031 CB ILE B 302 205.908 33.534 19.280 1.00 28.93 C ANISOU 1031 CB ILE B 302 3245 4055 3690 -372 -914 -15 C ATOM 1032 CG1 ILE B 302 206.703 32.391 19.897 1.00 27.48 C ANISOU 1032 CG1 ILE B 302 3151 3657 3634 -509 -882 106 C ATOM 1033 CG2 ILE B 302 205.760 33.371 17.758 1.00 30.88 C ANISOU 1033 CG2 ILE B 302 3394 4341 3998 -409 -914 -121 C ATOM 1034 CD1 ILE B 302 205.948 31.060 19.907 1.00 28.83 C ANISOU 1034 CD1 ILE B 302 3229 3869 3857 -704 -726 87 C ATOM 1035 N ALA B 303 204.730 36.389 19.077 1.00 29.51 N ANISOU 1035 N ALA B 303 3245 4449 3518 20 -1017 -140 N ATOM 1036 CA ALA B 303 204.023 37.364 18.248 1.00 27.03 C ANISOU 1036 CA ALA B 303 2827 4286 3156 174 -1069 -214 C ATOM 1037 C ALA B 303 204.753 38.693 18.281 1.00 31.06 C ANISOU 1037 C ALA B 303 3471 4692 3638 366 -1135 -184 C ATOM 1038 O ALA B 303 204.706 39.466 17.322 1.00 33.10 O ANISOU 1038 O ALA B 303 3724 4971 3883 495 -1199 -206 O ATOM 1039 CB ALA B 303 202.579 37.545 18.712 1.00 25.23 C ANISOU 1039 CB ALA B 303 2419 4286 2883 201 -1000 -286 C ATOM 1040 N SER B 304 205.474 38.931 19.371 1.00 28.50 N ANISOU 1040 N SER B 304 3284 4244 3301 372 -1121 -131 N ATOM 1041 CA SER B 304 206.141 40.216 19.587 1.00 34.02 C ANISOU 1041 CA SER B 304 4103 4843 3979 535 -1158 -127 C ATOM 1042 C SER B 304 207.537 40.291 18.974 1.00 37.14 C ANISOU 1042 C SER B 304 4625 5007 4481 540 -1224 -100 C ATOM 1043 O SER B 304 207.967 41.362 18.543 1.00 40.31 O ANISOU 1043 O SER B 304 5094 5323 4898 662 -1203 -119 O ATOM 1044 CB SER B 304 206.225 40.524 21.090 1.00 39.69 C ANISOU 1044 CB SER B 304 4914 5552 4613 524 -1116 -111 C ATOM 1045 OG SER B 304 204.909 40.693 21.626 1.00 48.48 O ANISOU 1045 OG SER B 304 5917 6858 5645 536 -1008 -165 O ATOM 1046 N LEU B 305 208.235 39.158 18.945 1.00 32.97 N ANISOU 1046 N LEU B 305 4119 4350 4058 384 -1239 -55 N ATOM 1047 CA LEU B 305 209.650 39.104 18.547 1.00 31.10 C ANISOU 1047 CA LEU B 305 3979 3856 3983 365 -1280 -39 C ATOM 1048 C LEU B 305 209.873 38.567 17.128 1.00 33.44 C ANISOU 1048 C LEU B 305 4251 4074 4380 294 -1242 -77 C ATOM 1049 O LEU B 305 210.943 38.757 16.554 1.00 34.13 O ANISOU 1049 O LEU B 305 4416 3944 4606 297 -1233 -98 O ATOM 1050 CB LEU B 305 210.462 38.267 19.532 1.00 29.54 C ANISOU 1050 CB LEU B 305 3825 3514 3885 251 -1332 44 C ATOM 1051 CG LEU B 305 210.538 38.719 20.996 1.00 35.76 C ANISOU 1051 CG LEU B 305 4697 4336 4554 283 -1392 89 C ATOM 1052 CD1 LEU B 305 211.157 37.616 21.879 1.00 32.18 C ANISOU 1052 CD1 LEU B 305 4289 3765 4173 149 -1471 208 C ATOM 1053 CD2 LEU B 305 211.326 40.027 21.142 1.00 39.33 C ANISOU 1053 CD2 LEU B 305 5228 4692 5023 392 -1363 29 C ATOM 1054 N ASN B 306 208.885 37.885 16.556 1.00 32.18 N ANISOU 1054 N ASN B 306 3252 5097 3877 -756 -479 1281 N ATOM 1055 CA ASN B 306 209.037 37.506 15.166 1.00 35.14 C ANISOU 1055 CA ASN B 306 3579 5726 4045 -700 -571 1342 C ATOM 1056 C ASN B 306 209.160 38.786 14.359 1.00 38.50 C ANISOU 1056 C ASN B 306 3797 6263 4568 -742 -483 1585 C ATOM 1057 O ASN B 306 208.313 39.677 14.469 1.00 37.31 O ANISOU 1057 O ASN B 306 3552 5978 4644 -819 -408 1764 O ATOM 1058 CB ASN B 306 207.850 36.680 14.649 1.00 34.76 C ANISOU 1058 CB ASN B 306 3597 5680 3929 -708 -689 1356 C ATOM 1059 CG ASN B 306 208.098 36.135 13.238 1.00 35.07 C ANISOU 1059 CG ASN B 306 3596 6010 3717 -646 -793 1371 C ATOM 1060 OD1 ASN B 306 209.207 35.679 12.932 1.00 37.27 O ANISOU 1060 OD1 ASN B 306 3903 6453 3805 -562 -826 1245 O ATOM 1061 ND2 ASN B 306 207.077 36.186 12.377 1.00 33.27 N ANISOU 1061 ND2 ASN B 306 3294 5864 3482 -685 -843 1519 N ATOM 1062 N GLY B 307 210.211 38.888 13.552 1.00 40.67 N ANISOU 1062 N GLY B 307 3996 6781 4676 -688 -489 1599 N ATOM 1063 CA GLY B 307 210.387 40.053 12.705 1.00 39.68 C ANISOU 1063 CA GLY B 307 3670 6784 4624 -725 -411 1844 C ATOM 1064 C GLY B 307 211.262 41.118 13.325 1.00 45.31 C ANISOU 1064 C GLY B 307 4300 7416 5499 -768 -264 1870 C ATOM 1065 O GLY B 307 211.571 42.135 12.698 1.00 50.36 O ANISOU 1065 O GLY B 307 4773 8147 6213 -803 -183 2069 O ATOM 1066 N TYR B 308 211.693 40.878 14.556 1.00 43.95 N ANISOU 1066 N TYR B 308 4239 7083 5377 -768 -227 1668 N ATOM 1067 CA TYR B 308 212.553 41.821 15.247 1.00 47.65 C ANISOU 1067 CA TYR B 308 4634 7479 5990 -818 -87 1652 C ATOM 1068 C TYR B 308 213.936 41.890 14.580 1.00 48.87 C ANISOU 1068 C TYR B 308 4715 7903 5951 -767 -85 1631 C ATOM 1069 O TYR B 308 214.523 40.866 14.224 1.00 46.40 O ANISOU 1069 O TYR B 308 4484 7777 5370 -670 -192 1485 O ATOM 1070 CB TYR B 308 212.700 41.428 16.719 1.00 51.87 C ANISOU 1070 CB TYR B 308 5304 7821 6585 -826 -62 1424 C ATOM 1071 CG TYR B 308 213.594 42.357 17.513 1.00 59.94 C ANISOU 1071 CG TYR B 308 6250 8778 7746 -886 82 1375 C ATOM 1072 CD1 TYR B 308 213.172 43.637 17.852 1.00 65.19 C ANISOU 1072 CD1 TYR B 308 6797 9259 8713 -995 226 1512 C ATOM 1073 CD2 TYR B 308 214.856 41.952 17.931 1.00 62.47 C ANISOU 1073 CD2 TYR B 308 6612 9223 7900 -834 77 1184 C ATOM 1074 CE1 TYR B 308 213.987 44.494 18.581 1.00 67.93 C ANISOU 1074 CE1 TYR B 308 7071 9545 9196 -1063 364 1448 C ATOM 1075 CE2 TYR B 308 215.673 42.799 18.665 1.00 65.25 C ANISOU 1075 CE2 TYR B 308 6887 9534 8372 -900 210 1128 C ATOM 1076 CZ TYR B 308 215.236 44.067 18.985 1.00 68.43 C ANISOU 1076 CZ TYR B 308 7175 9751 9077 -1021 353 1253 C ATOM 1077 OH TYR B 308 216.053 44.907 19.708 1.00 70.66 O ANISOU 1077 OH TYR B 308 7376 9991 9481 -1098 489 1178 O ATOM 1078 N ARG B 309 214.461 43.097 14.412 1.00 51.84 N ANISOU 1078 N ARG B 309 4934 8296 6466 -834 42 1773 N ATOM 1079 CA ARG B 309 215.799 43.241 13.849 1.00 56.65 C ANISOU 1079 CA ARG B 309 5461 9160 6902 -800 57 1756 C ATOM 1080 C ARG B 309 216.821 43.191 14.973 1.00 59.38 C ANISOU 1080 C ARG B 309 5862 9457 7244 -802 117 1530 C ATOM 1081 O ARG B 309 216.935 44.131 15.756 1.00 60.84 O ANISOU 1081 O ARG B 309 5988 9468 7661 -898 252 1542 O ATOM 1082 CB ARG B 309 215.933 44.545 13.056 1.00 60.66 C ANISOU 1082 CB ARG B 309 5766 9731 7550 -876 165 2030 C ATOM 1083 N LEU B 310 217.539 42.077 15.073 1.00 60.32 N ANISOU 1083 N LEU B 310 6092 9728 7101 -695 17 1318 N ATOM 1084 CA LEU B 310 218.614 41.958 16.044 1.00 59.40 C ANISOU 1084 CA LEU B 310 6012 9621 6936 -680 62 1110 C ATOM 1085 C LEU B 310 219.883 42.375 15.326 1.00 64.35 C ANISOU 1085 C LEU B 310 6506 10520 7422 -666 99 1143 C ATOM 1086 O LEU B 310 220.269 41.750 14.334 1.00 63.46 O ANISOU 1086 O LEU B 310 6388 10658 7066 -572 3 1144 O ATOM 1087 CB LEU B 310 218.735 40.520 16.559 1.00 56.94 C ANISOU 1087 CB LEU B 310 5887 9325 6423 -560 -63 875 C ATOM 1088 CG LEU B 310 219.718 40.255 17.713 1.00 54.72 C ANISOU 1088 CG LEU B 310 5661 9043 6087 -531 -29 656 C ATOM 1089 CD1 LEU B 310 219.528 41.239 18.870 1.00 53.10 C ANISOU 1089 CD1 LEU B 310 5408 8615 6151 -663 112 652 C ATOM 1090 CD2 LEU B 310 219.619 38.812 18.222 1.00 51.04 C ANISOU 1090 CD2 LEU B 310 5387 8550 5455 -409 -155 462 C ATOM 1091 N GLY B 311 220.525 43.432 15.819 1.00 68.55 N ANISOU 1091 N GLY B 311 6927 11011 8109 -764 240 1162 N ATOM 1092 CA GLY B 311 221.675 44.000 15.136 1.00 72.05 C ANISOU 1092 CA GLY B 311 7222 11699 8454 -779 294 1223 C ATOM 1093 C GLY B 311 221.223 44.516 13.784 1.00 73.59 C ANISOU 1093 C GLY B 311 7296 11999 8664 -803 289 1497 C ATOM 1094 O GLY B 311 220.624 45.591 13.701 1.00 76.33 O ANISOU 1094 O GLY B 311 7545 12184 9275 -913 392 1702 O ATOM 1095 N ASP B 312 221.480 43.745 12.730 1.00 70.44 N ANISOU 1095 N ASP B 312 6901 11876 7988 -697 170 1503 N ATOM 1096 CA ASP B 312 220.962 44.081 11.405 1.00 72.36 C ANISOU 1096 CA ASP B 312 7033 12255 8206 -709 143 1760 C ATOM 1097 C ASP B 312 220.444 42.848 10.650 1.00 72.56 C ANISOU 1097 C ASP B 312 7154 12430 7987 -589 -24 1705 C ATOM 1098 O ASP B 312 220.521 42.779 9.423 1.00 76.87 O ANISOU 1098 O ASP B 312 7606 13236 8364 -557 -78 1832 O ATOM 1099 CB ASP B 312 222.018 44.821 10.574 1.00 74.86 C ANISOU 1099 CB ASP B 312 7167 12837 8439 -743 210 1890 C ATOM 1100 N LYS B 313 219.920 41.878 11.396 1.00 66.02 N ANISOU 1100 N LYS B 313 6508 11439 7139 -530 -104 1514 N ATOM 1101 CA LYS B 313 219.320 40.681 10.818 1.00 60.74 C ANISOU 1101 CA LYS B 313 5947 10856 6275 -431 -257 1440 C ATOM 1102 C LYS B 313 217.886 40.600 11.313 1.00 56.16 C ANISOU 1102 C LYS B 313 5458 9986 5894 -480 -273 1490 C ATOM 1103 O LYS B 313 217.600 41.030 12.432 1.00 59.22 O ANISOU 1103 O LYS B 313 5889 10104 6507 -547 -192 1460 O ATOM 1104 CB LYS B 313 220.100 39.435 11.249 1.00 59.84 C ANISOU 1104 CB LYS B 313 5979 10823 5933 -301 -346 1144 C ATOM 1105 N ILE B 314 216.994 40.044 10.500 1.00 49.07 N ANISOU 1105 N ILE B 314 4582 9156 4906 -452 -376 1555 N ATOM 1106 CA ILE B 314 215.578 39.944 10.871 1.00 49.35 C ANISOU 1106 CA ILE B 314 4692 8944 5116 -501 -399 1613 C ATOM 1107 C ILE B 314 215.275 38.587 11.498 1.00 43.28 C ANISOU 1107 C ILE B 314 4134 8066 4244 -426 -508 1363 C ATOM 1108 O ILE B 314 215.340 37.558 10.827 1.00 43.09 O ANISOU 1108 O ILE B 314 4174 8213 3986 -340 -628 1254 O ATOM 1109 CB ILE B 314 214.652 40.123 9.641 1.00 48.30 C ANISOU 1109 CB ILE B 314 4453 8946 4951 -524 -450 1839 C ATOM 1110 CG1 ILE B 314 214.877 41.488 8.985 1.00 53.04 C ANISOU 1110 CG1 ILE B 314 4839 9647 5669 -597 -340 2125 C ATOM 1111 CG2 ILE B 314 213.185 39.948 10.046 1.00 47.04 C ANISOU 1111 CG2 ILE B 314 4371 8544 4958 -571 -479 1883 C ATOM 1112 CD1 ILE B 314 214.519 42.670 9.870 1.00 53.83 C ANISOU 1112 CD1 ILE B 314 4889 9446 6120 -701 -193 2253 C ATOM 1113 N LEU B 315 214.940 38.560 12.783 1.00 38.74 N ANISOU 1113 N LEU B 315 3667 7208 3844 -461 -466 1268 N ATOM 1114 CA LEU B 315 214.728 37.267 13.419 1.00 37.25 C ANISOU 1114 CA LEU B 315 3678 6915 3559 -390 -565 1042 C ATOM 1115 C LEU B 315 213.475 36.576 12.926 1.00 39.24 C ANISOU 1115 C LEU B 315 3999 7125 3785 -395 -670 1072 C ATOM 1116 O LEU B 315 212.459 37.221 12.625 1.00 39.80 O ANISOU 1116 O LEU B 315 3988 7126 4008 -479 -642 1267 O ATOM 1117 CB LEU B 315 214.611 37.402 14.938 1.00 41.66 C ANISOU 1117 CB LEU B 315 4328 7196 4306 -434 -495 944 C ATOM 1118 CG LEU B 315 215.801 37.963 15.721 1.00 43.17 C ANISOU 1118 CG LEU B 315 4475 7397 4532 -439 -393 864 C ATOM 1119 CD1 LEU B 315 215.537 37.755 17.213 1.00 48.37 C ANISOU 1119 CD1 LEU B 315 5252 7803 5324 -467 -359 731 C ATOM 1120 CD2 LEU B 315 217.077 37.275 15.294 1.00 39.77 C ANISOU 1120 CD2 LEU B 315 4062 7219 3831 -317 -452 719 C ATOM 1121 N GLN B 316 213.541 35.247 12.856 1.00 39.46 N ANISOU 1121 N GLN B 316 4177 7191 3624 -303 -788 877 N ATOM 1122 CA GLN B 316 212.324 34.454 12.704 1.00 36.80 C ANISOU 1122 CA GLN B 316 3943 6755 3285 -320 -884 855 C ATOM 1123 C GLN B 316 212.066 33.733 14.022 1.00 35.73 C ANISOU 1123 C GLN B 316 3994 6352 3229 -311 -899 688 C ATOM 1124 O GLN B 316 212.948 33.059 14.543 1.00 35.50 O ANISOU 1124 O GLN B 316 4068 6325 3095 -221 -920 504 O ATOM 1125 CB GLN B 316 212.484 33.446 11.575 1.00 41.61 C ANISOU 1125 CB GLN B 316 4582 7599 3629 -235 -1008 755 C ATOM 1126 CG GLN B 316 212.751 34.093 10.211 1.00 45.16 C ANISOU 1126 CG GLN B 316 4838 8357 3966 -242 -1002 921 C ATOM 1127 CD GLN B 316 213.316 33.107 9.203 1.00 49.94 C ANISOU 1127 CD GLN B 316 5478 9173 4323 -137 -1081 753 C ATOM 1128 OE1 GLN B 316 213.113 31.895 9.321 1.00 50.12 O ANISOU 1128 OE1 GLN B 316 5671 9085 4286 -77 -1155 546 O ATOM 1129 NE2 GLN B 316 214.048 33.624 8.212 1.00 48.62 N ANISOU 1129 NE2 GLN B 316 5170 9219 4085 -115 -1022 822 N ATOM 1130 N VAL B 317 210.875 33.888 14.591 1.00 33.12 N ANISOU 1130 N VAL B 317 3702 5799 3085 -401 -884 758 N ATOM 1131 CA VAL B 317 210.602 33.294 15.908 1.00 30.24 C ANISOU 1131 CA VAL B 317 3500 5184 2807 -406 -887 620 C ATOM 1132 C VAL B 317 209.292 32.572 15.815 1.00 31.93 C ANISOU 1132 C VAL B 317 3808 5279 3043 -449 -972 618 C ATOM 1133 O VAL B 317 208.357 33.102 15.216 1.00 32.50 O ANISOU 1133 O VAL B 317 3782 5370 3197 -526 -967 784 O ATOM 1134 CB VAL B 317 210.507 34.374 17.010 1.00 32.10 C ANISOU 1134 CB VAL B 317 3676 5237 3285 -493 -753 696 C ATOM 1135 CG1 VAL B 317 210.220 33.721 18.358 1.00 29.63 C ANISOU 1135 CG1 VAL B 317 3524 4698 3038 -499 -761 556 C ATOM 1136 CG2 VAL B 317 211.803 35.162 17.082 1.00 31.46 C ANISOU 1136 CG2 VAL B 317 3486 5278 3189 -468 -661 699 C ATOM 1137 N SER B 318 209.234 31.345 16.332 1.00 29.98 N ANISOU 1137 N SER B 318 3747 4926 2719 -398 -1052 438 N ATOM 1138 CA SER B 318 208.032 30.530 16.146 1.00 30.20 C ANISOU 1138 CA SER B 318 3871 4856 2746 -443 -1143 417 C ATOM 1139 C SER B 318 208.035 29.331 17.066 1.00 30.62 C ANISOU 1139 C SER B 318 4133 4729 2771 -399 -1200 233 C ATOM 1140 O SER B 318 209.082 29.001 17.616 1.00 31.07 O ANISOU 1140 O SER B 318 4257 4787 2761 -307 -1189 113 O ATOM 1141 CB SER B 318 207.976 30.033 14.695 1.00 41.17 C ANISOU 1141 CB SER B 318 5223 6475 3944 -405 -1238 406 C ATOM 1142 OG SER B 318 209.163 29.324 14.353 1.00 42.45 O ANISOU 1142 OG SER B 318 5441 6781 3906 -276 -1285 241 O ATOM 1143 N PHE B 319 206.883 28.680 17.271 1.00 29.76 N ANISOU 1143 N PHE B 319 4125 4466 2716 -465 -1259 217 N ATOM 1144 CA PHE B 319 206.891 27.434 18.047 1.00 38.13 C ANISOU 1144 CA PHE B 319 5391 5358 3741 -421 -1321 49 C ATOM 1145 C PHE B 319 207.780 26.418 17.338 1.00 39.10 C ANISOU 1145 C PHE B 319 5594 5611 3650 -287 -1406 -117 C ATOM 1146 O PHE B 319 207.636 26.218 16.133 1.00 31.55 O ANISOU 1146 O PHE B 319 4586 4823 2576 -278 -1466 -123 O ATOM 1147 CB PHE B 319 205.487 26.833 18.245 1.00 37.22 C ANISOU 1147 CB PHE B 319 5366 5071 3704 -522 -1377 57 C ATOM 1148 CG PHE B 319 204.652 27.563 19.270 1.00 37.20 C ANISOU 1148 CG PHE B 319 5329 4892 3913 -637 -1296 173 C ATOM 1149 CD1 PHE B 319 205.012 27.561 20.611 1.00 36.05 C ANISOU 1149 CD1 PHE B 319 5257 4593 3848 -627 -1240 126 C ATOM 1150 CD2 PHE B 319 203.494 28.242 18.886 1.00 38.93 C ANISOU 1150 CD2 PHE B 319 5435 5112 4244 -752 -1278 327 C ATOM 1151 CE1 PHE B 319 204.252 28.243 21.557 1.00 35.09 C ANISOU 1151 CE1 PHE B 319 5094 4324 3914 -734 -1161 217 C ATOM 1152 CE2 PHE B 319 202.732 28.924 19.835 1.00 34.38 C ANISOU 1152 CE2 PHE B 319 4821 4375 3867 -851 -1198 423 C ATOM 1153 CZ PHE B 319 203.107 28.912 21.160 1.00 31.66 C ANISOU 1153 CZ PHE B 319 4550 3880 3598 -844 -1141 360 C ATOM 1154 N LYS B 320 208.692 25.782 18.075 1.00 36.71 N ANISOU 1154 N LYS B 320 5409 5243 3294 -180 -1410 -251 N ATOM 1155 CA LYS B 320 209.531 24.739 17.466 1.00 37.23 C ANISOU 1155 CA LYS B 320 5563 5413 3172 -38 -1490 -422 C ATOM 1156 C LYS B 320 208.704 23.636 16.814 1.00 43.20 C ANISOU 1156 C LYS B 320 6429 6113 3870 -58 -1597 -515 C ATOM 1157 O LYS B 320 207.721 23.146 17.394 1.00 47.68 O ANISOU 1157 O LYS B 320 7106 6468 4543 -140 -1622 -514 O ATOM 1158 CB LYS B 320 210.457 24.097 18.509 1.00 36.60 C ANISOU 1158 CB LYS B 320 5611 5227 3067 80 -1484 -542 C ATOM 1159 CG LYS B 320 211.294 22.938 17.931 1.00 41.09 C ANISOU 1159 CG LYS B 320 6281 5874 3456 241 -1566 -727 C ATOM 1160 CD LYS B 320 212.173 22.274 18.993 1.00 43.29 C ANISOU 1160 CD LYS B 320 6664 6040 3743 358 -1536 -814 C ATOM 1161 CE LYS B 320 213.213 21.347 18.351 1.00 44.99 C ANISOU 1161 CE LYS B 320 6878 6349 3869 500 -1519 -936 C ATOM 1162 NZ LYS B 320 212.591 20.462 17.323 1.00 43.38 N ANISOU 1162 NZ LYS B 320 6723 6131 3629 485 -1582 -1016 N ATOM 1163 N THR B 321 209.107 23.237 15.613 1.00 40.86 N ANISOU 1163 N THR B 321 6102 6018 3406 11 -1657 -604 N ATOM 1164 CA THR B 321 208.532 22.071 14.964 1.00 46.50 C ANISOU 1164 CA THR B 321 6928 6697 4044 10 -1758 -742 C ATOM 1165 C THR B 321 209.430 20.852 15.106 1.00 51.33 C ANISOU 1165 C THR B 321 7644 7241 4618 146 -1736 -917 C ATOM 1166 O THR B 321 210.595 20.968 15.481 1.00 50.52 O ANISOU 1166 O THR B 321 7520 7183 4492 256 -1677 -937 O ATOM 1167 CB THR B 321 208.325 22.320 13.463 1.00 53.73 C ANISOU 1167 CB THR B 321 7693 7886 4837 -23 -1784 -720 C ATOM 1168 OG1 THR B 321 209.502 22.928 12.922 1.00 55.48 O ANISOU 1168 OG1 THR B 321 7774 8340 4968 56 -1718 -687 O ATOM 1169 CG2 THR B 321 207.126 23.226 13.240 1.00 56.59 C ANISOU 1169 CG2 THR B 321 7934 8270 5296 -183 -1771 -524 C ATOM 1170 N ASN B 322 208.896 19.679 14.789 1.00 57.74 N ANISOU 1170 N ASN B 322 8564 7944 5430 136 -1785 -1041 N ATOM 1171 CA ASN B 322 209.702 18.461 14.796 1.00 66.42 C ANISOU 1171 CA ASN B 322 9766 8970 6501 270 -1777 -1204 C ATOM 1172 C ASN B 322 210.548 18.316 13.533 1.00 70.80 C ANISOU 1172 C ASN B 322 10211 9773 6918 339 -1757 -1280 C ATOM 1173 O ASN B 322 210.771 19.284 12.801 1.00 72.87 O ANISOU 1173 O ASN B 322 10311 10272 7105 302 -1731 -1185 O ATOM 1174 CB ASN B 322 208.814 17.231 14.990 1.00 71.52 C ANISOU 1174 CB ASN B 322 10583 9376 7216 230 -1837 -1310 C ATOM 1175 CG ASN B 322 207.902 17.361 16.197 1.00 76.49 C ANISOU 1175 CG ASN B 322 11322 9753 7987 134 -1855 -1218 C ATOM 1176 OD1 ASN B 322 206.774 17.849 16.088 1.00 80.86 O ANISOU 1176 OD1 ASN B 322 11844 10294 8585 -17 -1884 -1130 O ATOM 1177 ND2 ASN B 322 208.386 16.927 17.355 1.00 75.28 N ANISOU 1177 ND2 ASN B 322 11293 9408 7903 217 -1837 -1228 N TER 1178 ASN B 322 ATOM 1179 N GLY C 243 190.579 47.890 18.355 1.00 52.86 N ANISOU 1179 N GLY C 243 6721 7078 6286 -517 579 457 N ATOM 1180 CA GLY C 243 191.245 46.665 18.763 1.00 50.07 C ANISOU 1180 CA GLY C 243 6308 6747 5972 -647 457 418 C ATOM 1181 C GLY C 243 192.600 46.505 18.087 1.00 45.56 C ANISOU 1181 C GLY C 243 5745 6094 5472 -696 446 406 C ATOM 1182 O GLY C 243 193.159 47.471 17.591 1.00 51.57 O ANISOU 1182 O GLY C 243 6572 6759 6262 -651 539 420 O ATOM 1183 N TRP C 244 193.125 45.284 18.063 1.00 36.99 N ANISOU 1183 N TRP C 244 4587 5042 4426 -786 338 385 N ATOM 1184 CA TRP C 244 194.455 45.001 17.511 1.00 36.26 C ANISOU 1184 CA TRP C 244 4493 4871 4412 -844 323 376 C ATOM 1185 C TRP C 244 194.405 44.419 16.091 1.00 33.84 C ANISOU 1185 C TRP C 244 4140 4624 4093 -764 307 403 C ATOM 1186 O TRP C 244 193.779 43.369 15.846 1.00 32.16 O ANISOU 1186 O TRP C 244 3847 4520 3851 -759 217 398 O ATOM 1187 CB TRP C 244 195.159 44.026 18.441 1.00 36.71 C ANISOU 1187 CB TRP C 244 4501 4916 4529 -999 217 336 C ATOM 1188 CG TRP C 244 195.265 44.587 19.830 1.00 43.50 C ANISOU 1188 CG TRP C 244 5417 5723 5389 -1076 226 305 C ATOM 1189 CD1 TRP C 244 194.384 44.400 20.881 1.00 45.17 C ANISOU 1189 CD1 TRP C 244 5618 6004 5539 -1096 194 294 C ATOM 1190 CD2 TRP C 244 196.289 45.461 20.313 1.00 45.77 C ANISOU 1190 CD2 TRP C 244 5783 5871 5737 -1137 271 280 C ATOM 1191 NE1 TRP C 244 194.824 45.103 21.982 1.00 46.08 N ANISOU 1191 NE1 TRP C 244 5811 6037 5659 -1164 216 257 N ATOM 1192 CE2 TRP C 244 195.984 45.765 21.657 1.00 50.53 C ANISOU 1192 CE2 TRP C 244 6428 6469 6300 -1193 258 244 C ATOM 1193 CE3 TRP C 244 197.433 46.025 19.735 1.00 52.77 C ANISOU 1193 CE3 TRP C 244 6707 6633 6712 -1148 323 287 C ATOM 1194 CZ2 TRP C 244 196.791 46.595 22.437 1.00 55.87 C ANISOU 1194 CZ2 TRP C 244 7187 7023 7019 -1263 281 203 C ATOM 1195 CZ3 TRP C 244 198.235 46.854 20.514 1.00 56.60 C ANISOU 1195 CZ3 TRP C 244 7262 6989 7256 -1221 348 254 C ATOM 1196 CH2 TRP C 244 197.908 47.127 21.850 1.00 54.07 C ANISOU 1196 CH2 TRP C 244 6985 6667 6889 -1279 321 207 C ATOM 1197 N CYS C 245 195.086 45.082 15.170 1.00 35.62 N ANISOU 1197 N CYS C 245 4417 4776 4344 -703 392 430 N ATOM 1198 CA CYS C 245 195.039 44.684 13.775 1.00 34.83 C ANISOU 1198 CA CYS C 245 4293 4730 4211 -608 394 457 C ATOM 1199 C CYS C 245 196.122 43.649 13.426 1.00 31.54 C ANISOU 1199 C CYS C 245 3831 4287 3866 -690 330 434 C ATOM 1200 O CYS C 245 197.297 43.830 13.743 1.00 30.28 O ANISOU 1200 O CYS C 245 3692 4013 3800 -773 355 429 O ATOM 1201 CB CYS C 245 195.192 45.917 12.893 1.00 35.55 C ANISOU 1201 CB CYS C 245 4461 4761 4286 -484 530 511 C ATOM 1202 SG CYS C 245 194.763 45.552 11.200 1.00 42.21 S ANISOU 1202 SG CYS C 245 5289 5706 5043 -333 534 550 S ATOM 1203 N ILE C 246 195.707 42.587 12.741 1.00 30.05 N ANISOU 1203 N ILE C 246 3579 4201 3640 -660 249 421 N ATOM 1204 CA ILE C 246 196.552 41.468 12.328 1.00 25.47 C ANISOU 1204 CA ILE C 246 2946 3612 3118 -725 184 395 C ATOM 1205 C ILE C 246 196.620 41.405 10.798 1.00 30.55 C ANISOU 1205 C ILE C 246 3612 4289 3708 -598 224 416 C ATOM 1206 O ILE C 246 195.585 41.443 10.139 1.00 29.16 O ANISOU 1206 O ILE C 246 3435 4214 3431 -485 212 425 O ATOM 1207 CB ILE C 246 195.948 40.156 12.854 1.00 26.48 C ANISOU 1207 CB ILE C 246 2976 3835 3249 -799 44 353 C ATOM 1208 CG1 ILE C 246 195.868 40.236 14.394 1.00 26.47 C ANISOU 1208 CG1 ILE C 246 2961 3809 3288 -916 12 341 C ATOM 1209 CG2 ILE C 246 196.756 38.936 12.374 1.00 27.89 C ANISOU 1209 CG2 ILE C 246 3097 4007 3495 -860 -24 323 C ATOM 1210 CD1 ILE C 246 195.169 39.051 15.021 1.00 29.36 C ANISOU 1210 CD1 ILE C 246 3227 4268 3659 -982 -112 316 C ATOM 1211 N PHE C 247 197.837 41.332 10.248 1.00 31.13 N ANISOU 1211 N PHE C 247 3705 4275 3846 -614 273 426 N ATOM 1212 CA PHE C 247 198.073 41.190 8.796 1.00 30.38 C ANISOU 1212 CA PHE C 247 3638 4206 3701 -497 318 445 C ATOM 1213 C PHE C 247 198.313 39.713 8.457 1.00 30.44 C ANISOU 1213 C PHE C 247 3575 4260 3729 -547 212 391 C ATOM 1214 O PHE C 247 199.070 38.994 9.166 1.00 27.81 O ANISOU 1214 O PHE C 247 3189 3870 3506 -684 158 363 O ATOM 1215 CB PHE C 247 199.312 42.030 8.427 1.00 28.89 C ANISOU 1215 CB PHE C 247 3512 3881 3586 -480 453 498 C ATOM 1216 CG PHE C 247 199.760 41.930 6.971 1.00 32.29 C ANISOU 1216 CG PHE C 247 3978 4320 3972 -361 522 529 C ATOM 1217 CD1 PHE C 247 198.950 42.373 5.941 1.00 30.82 C ANISOU 1217 CD1 PHE C 247 3839 4223 3649 -197 565 560 C ATOM 1218 CD2 PHE C 247 201.025 41.457 6.657 1.00 32.10 C ANISOU 1218 CD2 PHE C 247 3943 4208 4043 -409 553 534 C ATOM 1219 CE1 PHE C 247 199.382 42.307 4.604 1.00 32.66 C ANISOU 1219 CE1 PHE C 247 4116 4467 3827 -78 634 590 C ATOM 1220 CE2 PHE C 247 201.476 41.395 5.315 1.00 33.14 C ANISOU 1220 CE2 PHE C 247 4117 4344 4129 -290 632 566 C ATOM 1221 CZ PHE C 247 200.645 41.813 4.301 1.00 30.70 C ANISOU 1221 CZ PHE C 247 3862 4133 3669 -124 671 592 C ATOM 1222 N ILE C 248 197.635 39.246 7.412 1.00 28.64 N ANISOU 1222 N ILE C 248 3346 4138 3398 -438 174 373 N ATOM 1223 CA ILE C 248 197.817 37.891 6.908 1.00 28.12 C ANISOU 1223 CA ILE C 248 3224 4116 3343 -464 80 315 C ATOM 1224 C ILE C 248 198.226 37.959 5.421 1.00 32.03 C ANISOU 1224 C ILE C 248 3785 4622 3764 -330 153 328 C ATOM 1225 O ILE C 248 197.542 38.576 4.602 1.00 29.32 O ANISOU 1225 O ILE C 248 3496 4346 3296 -187 193 357 O ATOM 1226 CB ILE C 248 196.522 37.066 7.021 1.00 30.27 C ANISOU 1226 CB ILE C 248 3425 4519 3557 -460 -60 263 C ATOM 1227 CG1 ILE C 248 196.011 37.034 8.477 1.00 31.09 C ANISOU 1227 CG1 ILE C 248 3468 4625 3722 -575 -120 260 C ATOM 1228 CG2 ILE C 248 196.733 35.645 6.490 1.00 26.29 C ANISOU 1228 CG2 ILE C 248 2862 4050 3078 -489 -160 194 C ATOM 1229 CD1 ILE C 248 195.019 38.156 8.798 1.00 29.42 C ANISOU 1229 CD1 ILE C 248 3295 4450 3434 -502 -72 305 C ATOM 1230 N TYR C 249 199.368 37.363 5.100 1.00 27.15 N ANISOU 1230 N TYR C 249 3161 3931 3223 -373 177 316 N ATOM 1231 CA TYR C 249 199.828 37.253 3.722 1.00 27.93 C ANISOU 1231 CA TYR C 249 3320 4039 3255 -252 244 323 C ATOM 1232 C TYR C 249 199.845 35.792 3.291 1.00 28.99 C ANISOU 1232 C TYR C 249 3401 4224 3391 -279 135 237 C ATOM 1233 O TYR C 249 200.036 34.884 4.108 1.00 29.33 O ANISOU 1233 O TYR C 249 3358 4243 3543 -418 42 192 O ATOM 1234 CB TYR C 249 201.220 37.883 3.553 1.00 28.12 C ANISOU 1234 CB TYR C 249 3391 3922 3371 -257 394 391 C ATOM 1235 CG TYR C 249 201.668 37.881 2.109 1.00 30.58 C ANISOU 1235 CG TYR C 249 3774 4245 3601 -112 486 413 C ATOM 1236 CD1 TYR C 249 201.304 38.922 1.260 1.00 32.36 C ANISOU 1236 CD1 TYR C 249 4085 4506 3704 50 590 479 C ATOM 1237 CD2 TYR C 249 202.405 36.817 1.582 1.00 32.52 C ANISOU 1237 CD2 TYR C 249 4002 4471 3885 -131 471 369 C ATOM 1238 CE1 TYR C 249 201.677 38.924 -0.074 1.00 33.73 C ANISOU 1238 CE1 TYR C 249 4331 4701 3786 193 677 504 C ATOM 1239 CE2 TYR C 249 202.789 36.807 0.229 1.00 35.46 C ANISOU 1239 CE2 TYR C 249 4449 4858 4165 14 562 387 C ATOM 1240 CZ TYR C 249 202.418 37.876 -0.583 1.00 34.68 C ANISOU 1240 CZ TYR C 249 4440 4801 3935 177 665 456 C ATOM 1241 OH TYR C 249 202.764 37.913 -1.918 1.00 34.33 O ANISOU 1241 OH TYR C 249 4478 4782 3784 331 761 482 O ATOM 1242 N ASN C 250 199.660 35.593 1.983 1.00 31.94 N ANISOU 1242 N ASN C 250 3831 4665 3639 -139 149 218 N ATOM 1243 CA ASN C 250 199.549 34.291 1.344 1.00 32.00 C ANISOU 1243 CA ASN C 250 3808 4733 3618 -130 48 126 C ATOM 1244 C ASN C 250 198.178 33.639 1.406 1.00 34.29 C ANISOU 1244 C ASN C 250 4040 5150 3837 -124 -117 53 C ATOM 1245 O ASN C 250 198.062 32.413 1.359 1.00 37.25 O ANISOU 1245 O ASN C 250 4351 5552 4250 -179 -233 -33 O ATOM 1246 CB ASN C 250 200.642 33.321 1.785 1.00 35.72 C ANISOU 1246 CB ASN C 250 4216 5106 4250 -265 34 94 C ATOM 1247 CG ASN C 250 201.824 33.299 0.815 1.00 37.47 C ANISOU 1247 CG ASN C 250 4505 5255 4476 -196 161 117 C ATOM 1248 OD1 ASN C 250 201.662 33.576 -0.376 1.00 36.30 O ANISOU 1248 OD1 ASN C 250 4445 5163 4185 -38 218 121 O ATOM 1249 ND2 ASN C 250 203.013 32.992 1.324 1.00 40.55 N ANISOU 1249 ND2 ASN C 250 4855 5522 5032 -308 209 139 N ATOM 1250 N LEU C 251 197.136 34.464 1.495 1.00 32.25 N ANISOU 1250 N LEU C 251 3801 4965 3488 -56 -126 90 N ATOM 1251 CA LEU C 251 195.792 34.012 1.157 1.00 34.57 C ANISOU 1251 CA LEU C 251 4060 5390 3683 1 -264 34 C ATOM 1252 C LEU C 251 195.754 33.622 -0.325 1.00 35.94 C ANISOU 1252 C LEU C 251 4303 5634 3719 142 -279 -15 C ATOM 1253 O LEU C 251 196.545 34.126 -1.128 1.00 35.60 O ANISOU 1253 O LEU C 251 4355 5554 3617 234 -149 26 O ATOM 1254 CB LEU C 251 194.793 35.129 1.429 1.00 32.74 C ANISOU 1254 CB LEU C 251 3848 5213 3380 66 -241 102 C ATOM 1255 CG LEU C 251 194.656 35.596 2.883 1.00 32.16 C ANISOU 1255 CG LEU C 251 3719 5084 3415 -54 -228 145 C ATOM 1256 CD1 LEU C 251 193.666 36.758 2.966 1.00 29.24 C ANISOU 1256 CD1 LEU C 251 3381 4767 2961 36 -187 213 C ATOM 1257 CD2 LEU C 251 194.208 34.437 3.788 1.00 32.23 C ANISOU 1257 CD2 LEU C 251 3605 5115 3525 -190 -377 80 C ATOM 1258 N GLY C 252 194.847 32.724 -0.698 1.00 38.19 N ANISOU 1258 N GLY C 252 4540 6017 3952 161 -436 -103 N ATOM 1259 CA GLY C 252 194.690 32.349 -2.100 1.00 39.16 C ANISOU 1259 CA GLY C 252 4734 6218 3926 300 -470 -162 C ATOM 1260 C GLY C 252 193.927 33.416 -2.889 1.00 40.42 C ANISOU 1260 C GLY C 252 4979 6472 3908 469 -430 -100 C ATOM 1261 O GLY C 252 193.309 34.303 -2.309 1.00 40.12 O ANISOU 1261 O GLY C 252 4924 6447 3872 472 -405 -24 O ATOM 1262 N GLN C 253 193.950 33.341 -4.217 1.00 40.59 N ANISOU 1262 N GLN C 253 5093 6560 3771 616 -424 -130 N ATOM 1263 CA GLN C 253 193.281 34.371 -5.010 1.00 41.39 C ANISOU 1263 CA GLN C 253 5276 6752 3697 785 -380 -59 C ATOM 1264 C GLN C 253 191.767 34.279 -4.828 1.00 44.51 C ANISOU 1264 C GLN C 253 5600 7260 4053 797 -544 -83 C ATOM 1265 O GLN C 253 191.045 35.264 -5.012 1.00 42.28 O ANISOU 1265 O GLN C 253 5347 7037 3680 894 -513 -1 O ATOM 1266 CB GLN C 253 193.699 34.294 -6.486 1.00 48.12 C ANISOU 1266 CB GLN C 253 6252 7655 4377 946 -332 -81 C ATOM 1267 CG GLN C 253 193.500 32.929 -7.103 0.99 53.27 C ANISOU 1267 CG GLN C 253 6890 8364 4985 946 -491 -230 C ATOM 1268 CD GLN C 253 193.906 32.876 -8.564 0.35 54.40 C ANISOU 1268 CD GLN C 253 7169 8562 4938 1115 -439 -256 C ATOM 1269 OE1 GLN C 253 194.960 33.385 -8.955 0.64 55.81 O ANISOU 1269 OE1 GLN C 253 7434 8674 5095 1174 -258 -186 O ATOM 1270 NE2 GLN C 253 193.065 32.260 -9.380 1.00 54.17 N ANISOU 1270 NE2 GLN C 253 7158 8653 4771 1198 -600 -356 N ATOM 1271 N ASP C 254 191.292 33.098 -4.439 1.00 44.43 N ANISOU 1271 N ASP C 254 5488 7270 4125 695 -715 -189 N ATOM 1272 CA ASP C 254 189.857 32.877 -4.249 1.00 49.02 C ANISOU 1272 CA ASP C 254 5983 7950 4693 697 -882 -215 C ATOM 1273 C ASP C 254 189.432 33.024 -2.772 1.00 44.90 C ANISOU 1273 C ASP C 254 5344 7380 4336 557 -896 -168 C ATOM 1274 O ASP C 254 188.287 32.757 -2.421 1.00 49.47 O ANISOU 1274 O ASP C 254 5831 8024 4943 536 -1028 -183 O ATOM 1275 CB ASP C 254 189.455 31.516 -4.828 1.00 54.59 C ANISOU 1275 CB ASP C 254 6645 8715 5383 690 -1073 -358 C ATOM 1276 CG ASP C 254 189.618 31.460 -6.350 1.00 63.00 C ANISOU 1276 CG ASP C 254 7835 9853 6247 854 -1077 -408 C ATOM 1277 OD1 ASP C 254 189.241 32.454 -7.021 1.00 60.92 O ANISOU 1277 OD1 ASP C 254 7657 9663 5829 1000 -1019 -329 O ATOM 1278 OD2 ASP C 254 190.135 30.439 -6.874 1.00 66.32 O ANISOU 1278 OD2 ASP C 254 8275 10259 6665 841 -1132 -521 O ATOM 1279 N ALA C 255 190.349 33.479 -1.923 1.00 36.37 N ANISOU 1279 N ALA C 255 4271 6188 3360 468 -758 -108 N ATOM 1280 CA ALA C 255 190.026 33.740 -0.519 1.00 37.92 C ANISOU 1280 CA ALA C 255 4378 6338 3691 346 -752 -58 C ATOM 1281 C ALA C 255 188.843 34.693 -0.354 1.00 44.52 C ANISOU 1281 C ALA C 255 5205 7245 4467 422 -752 21 C ATOM 1282 O ALA C 255 188.697 35.676 -1.093 1.00 42.82 O ANISOU 1282 O ALA C 255 5079 7067 4125 560 -668 87 O ATOM 1283 CB ALA C 255 191.223 34.292 0.217 1.00 39.18 C ANISOU 1283 CB ALA C 255 4571 6370 3943 265 -594 1 C ATOM 1284 N ASP C 256 188.007 34.406 0.639 1.00 44.17 N ANISOU 1284 N ASP C 256 5047 7214 4520 334 -839 22 N ATOM 1285 CA ASP C 256 186.914 35.300 0.986 1.00 47.95 C ANISOU 1285 CA ASP C 256 5505 7743 4970 389 -826 104 C ATOM 1286 C ASP C 256 186.890 35.528 2.503 1.00 43.34 C ANISOU 1286 C ASP C 256 4855 7090 4521 261 -779 148 C ATOM 1287 O ASP C 256 187.572 34.835 3.254 1.00 42.76 O ANISOU 1287 O ASP C 256 4737 6947 4563 127 -791 109 O ATOM 1288 CB ASP C 256 185.586 34.736 0.498 1.00 56.23 C ANISOU 1288 CB ASP C 256 6477 8909 5978 446 -1000 67 C ATOM 1289 CG ASP C 256 185.256 33.406 1.136 1.00 64.37 C ANISOU 1289 CG ASP C 256 7374 9938 7145 318 -1152 -13 C ATOM 1290 OD1 ASP C 256 186.117 32.874 1.880 1.00 65.57 O ANISOU 1290 OD1 ASP C 256 7499 10004 7410 189 -1123 -42 O ATOM 1291 OD2 ASP C 256 184.144 32.884 0.881 1.00 70.23 O ANISOU 1291 OD2 ASP C 256 8033 10763 7888 346 -1303 -43 O ATOM 1292 N GLU C 257 186.118 36.518 2.924 1.00 39.51 N ANISOU 1292 N GLU C 257 5013 6053 3946 -751 -70 -376 N ATOM 1293 CA GLU C 257 186.054 36.938 4.311 1.00 40.54 C ANISOU 1293 CA GLU C 257 5084 6069 4250 -667 -115 -301 C ATOM 1294 C GLU C 257 185.847 35.705 5.230 1.00 36.27 C ANISOU 1294 C GLU C 257 4555 5410 3816 -709 -53 -417 C ATOM 1295 O GLU C 257 186.372 35.628 6.356 1.00 38.28 O ANISOU 1295 O GLU C 257 4799 5523 4222 -652 -25 -374 O ATOM 1296 CB GLU C 257 184.912 37.962 4.447 1.00 39.99 C ANISOU 1296 CB GLU C 257 4936 6109 4151 -637 -273 -220 C ATOM 1297 CG GLU C 257 185.321 39.451 4.273 1.00 46.71 C ANISOU 1297 CG GLU C 257 5768 6971 5008 -542 -329 -45 C ATOM 1298 CD GLU C 257 185.565 39.921 2.824 1.00 55.55 C ANISOU 1298 CD GLU C 257 6948 8214 5945 -561 -341 15 C ATOM 1299 OE1 GLU C 257 184.998 39.331 1.857 1.00 56.76 O ANISOU 1299 OE1 GLU C 257 7126 8509 5931 -648 -363 -67 O ATOM 1300 OE2 GLU C 257 186.332 40.917 2.665 1.00 54.87 O ANISOU 1300 OE2 GLU C 257 6887 8087 5873 -499 -323 145 O ATOM 1301 N GLY C 258 185.091 34.729 4.729 1.00 33.54 N ANISOU 1301 N GLY C 258 4237 5127 3382 -818 -28 -562 N ATOM 1302 CA GLY C 258 184.756 33.539 5.495 1.00 33.86 C ANISOU 1302 CA GLY C 258 4306 5053 3505 -877 40 -677 C ATOM 1303 C GLY C 258 185.985 32.817 6.009 1.00 36.38 C ANISOU 1303 C GLY C 258 4687 5172 3964 -826 168 -673 C ATOM 1304 O GLY C 258 185.982 32.271 7.125 1.00 38.22 O ANISOU 1304 O GLY C 258 4936 5267 4320 -813 190 -671 O ATOM 1305 N ILE C 259 187.055 32.827 5.217 1.00 31.64 N ANISOU 1305 N ILE C 259 4119 4558 3346 -795 250 -666 N ATOM 1306 CA ILE C 259 188.253 32.109 5.616 1.00 33.31 C ANISOU 1306 CA ILE C 259 4369 4586 3702 -733 372 -673 C ATOM 1307 C ILE C 259 188.922 32.796 6.813 1.00 30.55 C ANISOU 1307 C ILE C 259 3967 4147 3492 -611 317 -521 C ATOM 1308 O ILE C 259 189.435 32.132 7.709 1.00 30.52 O ANISOU 1308 O ILE C 259 3980 3989 3626 -561 360 -505 O ATOM 1309 CB ILE C 259 189.269 31.881 4.437 1.00 41.01 C ANISOU 1309 CB ILE C 259 5377 5569 4635 -742 496 -736 C ATOM 1310 CG1 ILE C 259 190.351 30.884 4.857 1.00 46.29 C ANISOU 1310 CG1 ILE C 259 6075 6034 5480 -678 631 -777 C ATOM 1311 CG2 ILE C 259 189.965 33.167 4.020 1.00 36.42 C ANISOU 1311 CG2 ILE C 259 4756 5075 4007 -680 454 -618 C ATOM 1312 CD1 ILE C 259 189.847 29.486 5.127 1.00 49.93 C ANISOU 1312 CD1 ILE C 259 6604 6368 6000 -741 716 -901 C ATOM 1313 N LEU C 260 188.897 34.123 6.820 1.00 29.50 N ANISOU 1313 N LEU C 260 3774 4113 3321 -569 222 -409 N ATOM 1314 CA LEU C 260 189.505 34.897 7.882 1.00 28.32 C ANISOU 1314 CA LEU C 260 3568 3906 3287 -476 177 -282 C ATOM 1315 C LEU C 260 188.702 34.677 9.161 1.00 30.28 C ANISOU 1315 C LEU C 260 3800 4105 3601 -494 111 -268 C ATOM 1316 O LEU C 260 189.275 34.395 10.216 1.00 27.14 O ANISOU 1316 O LEU C 260 3396 3597 3318 -447 123 -219 O ATOM 1317 CB LEU C 260 189.596 36.362 7.501 1.00 27.91 C ANISOU 1317 CB LEU C 260 3468 3960 3177 -444 113 -182 C ATOM 1318 CG LEU C 260 190.642 36.652 6.394 1.00 31.43 C ANISOU 1318 CG LEU C 260 3937 4437 3567 -429 196 -179 C ATOM 1319 CD1 LEU C 260 190.586 38.125 6.024 1.00 28.43 C ANISOU 1319 CD1 LEU C 260 3532 4150 3121 -408 132 -67 C ATOM 1320 CD2 LEU C 260 192.082 36.290 6.864 1.00 31.80 C ANISOU 1320 CD2 LEU C 260 3965 4366 3752 -358 292 -175 C ATOM 1321 N TRP C 261 187.370 34.725 9.052 1.00 27.69 N ANISOU 1321 N TRP C 261 3464 3864 3194 -572 46 -321 N ATOM 1322 CA TRP C 261 186.546 34.407 10.222 1.00 30.19 C ANISOU 1322 CA TRP C 261 3771 4135 3564 -617 5 -338 C ATOM 1323 C TRP C 261 186.821 33.016 10.780 1.00 31.86 C ANISOU 1323 C TRP C 261 4065 4194 3846 -643 92 -392 C ATOM 1324 O TRP C 261 186.934 32.854 11.995 1.00 32.01 O ANISOU 1324 O TRP C 261 4089 4123 3949 -632 77 -337 O ATOM 1325 CB TRP C 261 185.036 34.506 9.923 1.00 30.33 C ANISOU 1325 CB TRP C 261 3758 4278 3489 -709 -64 -422 C ATOM 1326 CG TRP C 261 184.518 35.892 9.719 1.00 32.34 C ANISOU 1326 CG TRP C 261 3919 4660 3709 -672 -173 -352 C ATOM 1327 CD1 TRP C 261 184.032 36.432 8.535 1.00 35.28 C ANISOU 1327 CD1 TRP C 261 4263 5179 3962 -675 -230 -356 C ATOM 1328 CD2 TRP C 261 184.398 36.918 10.698 1.00 31.56 C ANISOU 1328 CD2 TRP C 261 3743 4550 3696 -628 -236 -265 C ATOM 1329 NE1 TRP C 261 183.640 37.733 8.738 1.00 33.64 N ANISOU 1329 NE1 TRP C 261 3971 5032 3779 -616 -327 -262 N ATOM 1330 CE2 TRP C 261 183.847 38.056 10.058 1.00 31.73 C ANISOU 1330 CE2 TRP C 261 3695 4691 3669 -591 -322 -218 C ATOM 1331 CE3 TRP C 261 184.681 36.987 12.072 1.00 32.91 C ANISOU 1331 CE3 TRP C 261 3900 4627 3978 -623 -226 -225 C ATOM 1332 CZ2 TRP C 261 183.581 39.251 10.741 1.00 33.38 C ANISOU 1332 CZ2 TRP C 261 3818 4905 3960 -544 -383 -143 C ATOM 1333 CZ3 TRP C 261 184.410 38.170 12.749 1.00 33.90 C ANISOU 1333 CZ3 TRP C 261 3938 4780 4165 -597 -285 -164 C ATOM 1334 CH2 TRP C 261 183.874 39.288 12.079 1.00 35.65 C ANISOU 1334 CH2 TRP C 261 4088 5099 4359 -555 -354 -128 C ATOM 1335 N GLN C 262 186.896 32.010 9.909 1.00 28.81 N ANISOU 1335 N GLN C 262 3750 3776 3422 -686 186 -499 N ATOM 1336 CA GLN C 262 187.175 30.646 10.367 1.00 33.38 C ANISOU 1336 CA GLN C 262 4420 4179 4085 -702 285 -549 C ATOM 1337 C GLN C 262 188.535 30.520 11.023 1.00 33.34 C ANISOU 1337 C GLN C 262 4417 4035 4215 -576 314 -437 C ATOM 1338 O GLN C 262 188.703 29.774 11.989 1.00 31.30 O ANISOU 1338 O GLN C 262 4211 3633 4047 -561 334 -399 O ATOM 1339 CB GLN C 262 187.179 29.663 9.205 1.00 35.80 C ANISOU 1339 CB GLN C 262 4795 4466 4343 -766 406 -696 C ATOM 1340 CG GLN C 262 185.847 29.159 8.775 1.00 39.57 C ANISOU 1340 CG GLN C 262 5299 5024 4710 -917 417 -844 C ATOM 1341 CD GLN C 262 186.001 28.269 7.574 1.00 47.69 C ANISOU 1341 CD GLN C 262 6389 6046 5685 -988 549 -997 C ATOM 1342 OE1 GLN C 262 186.086 28.749 6.441 1.00 51.93 O ANISOU 1342 OE1 GLN C 262 6891 6731 6107 -1007 541 -1033 O ATOM 1343 NE2 GLN C 262 186.097 26.964 7.812 1.00 49.20 N ANISOU 1343 NE2 GLN C 262 6677 6054 5961 -1030 681 -1084 N ATOM 1344 N MET C 263 189.540 31.190 10.467 1.00 29.21 N ANISOU 1344 N MET C 263 3838 3556 3703 -489 321 -387 N ATOM 1345 CA MET C 263 190.867 31.020 11.051 1.00 29.29 C ANISOU 1345 CA MET C 263 3829 3451 3848 -368 349 -298 C ATOM 1346 C MET C 263 191.017 31.720 12.397 1.00 28.21 C ANISOU 1346 C MET C 263 3635 3322 3762 -324 246 -162 C ATOM 1347 O MET C 263 191.671 31.188 13.310 1.00 28.75 O ANISOU 1347 O MET C 263 3713 3276 3933 -258 246 -89 O ATOM 1348 CB MET C 263 191.962 31.513 10.090 1.00 29.57 C ANISOU 1348 CB MET C 263 3813 3534 3886 -301 403 -303 C ATOM 1349 CG MET C 263 192.061 30.662 8.851 1.00 30.93 C ANISOU 1349 CG MET C 263 4044 3679 4027 -346 531 -445 C ATOM 1350 SD MET C 263 193.464 31.223 7.860 1.00 45.12 S ANISOU 1350 SD MET C 263 5780 5524 5837 -278 611 -456 S ATOM 1351 CE MET C 263 193.107 32.950 7.704 1.00 30.09 C ANISOU 1351 CE MET C 263 3818 3812 3804 -301 492 -357 C ATOM 1352 N PHE C 264 190.467 32.924 12.514 1.00 27.15 N ANISOU 1352 N PHE C 264 3436 3320 3558 -358 161 -127 N ATOM 1353 CA PHE C 264 190.726 33.724 13.724 1.00 27.97 C ANISOU 1353 CA PHE C 264 3473 3445 3710 -328 82 -15 C ATOM 1354 C PHE C 264 189.690 33.627 14.824 1.00 28.18 C ANISOU 1354 C PHE C 264 3519 3466 3723 -413 23 -8 C ATOM 1355 O PHE C 264 190.019 33.764 16.011 1.00 27.16 O ANISOU 1355 O PHE C 264 3367 3310 3640 -402 -19 75 O ATOM 1356 CB PHE C 264 190.963 35.182 13.364 1.00 25.44 C ANISOU 1356 CB PHE C 264 3064 3246 3357 -305 45 28 C ATOM 1357 CG PHE C 264 192.284 35.384 12.680 1.00 25.83 C ANISOU 1357 CG PHE C 264 3082 3293 3440 -221 107 45 C ATOM 1358 CD1 PHE C 264 192.398 35.217 11.311 1.00 26.52 C ANISOU 1358 CD1 PHE C 264 3204 3407 3467 -228 175 -28 C ATOM 1359 CD2 PHE C 264 193.420 35.655 13.430 1.00 25.71 C ANISOU 1359 CD2 PHE C 264 2999 3257 3513 -147 103 121 C ATOM 1360 CE1 PHE C 264 193.624 35.358 10.670 1.00 27.04 C ANISOU 1360 CE1 PHE C 264 3240 3471 3563 -167 250 -31 C ATOM 1361 CE2 PHE C 264 194.634 35.799 12.818 1.00 27.03 C ANISOU 1361 CE2 PHE C 264 3124 3428 3719 -78 168 116 C ATOM 1362 CZ PHE C 264 194.758 35.645 11.428 1.00 28.16 C ANISOU 1362 CZ PHE C 264 3305 3587 3808 -88 250 37 C ATOM 1363 N GLY C 265 188.444 33.412 14.418 1.00 26.76 N ANISOU 1363 N GLY C 265 3373 3326 3469 -510 21 -104 N ATOM 1364 CA GLY C 265 187.342 33.259 15.360 1.00 29.30 C ANISOU 1364 CA GLY C 265 3712 3648 3773 -614 -17 -131 C ATOM 1365 C GLY C 265 187.630 32.293 16.514 1.00 30.48 C ANISOU 1365 C GLY C 265 3941 3662 3976 -629 2 -80 C ATOM 1366 O GLY C 265 187.305 32.585 17.666 1.00 29.67 O ANISOU 1366 O GLY C 265 3825 3573 3877 -685 -46 -36 O ATOM 1367 N PRO C 266 188.178 31.104 16.217 1.00 27.24 N ANISOU 1367 N PRO C 266 3623 3117 3610 -588 76 -88 N ATOM 1368 CA PRO C 266 188.445 30.162 17.311 1.00 30.89 C ANISOU 1368 CA PRO C 266 4176 3435 4127 -590 88 -14 C ATOM 1369 C PRO C 266 189.391 30.671 18.400 1.00 30.08 C ANISOU 1369 C PRO C 266 4017 3342 4072 -514 13 140 C ATOM 1370 O PRO C 266 189.355 30.124 19.502 1.00 31.85 O ANISOU 1370 O PRO C 266 4308 3488 4304 -549 -9 215 O ATOM 1371 CB PRO C 266 189.041 28.952 16.591 1.00 29.32 C ANISOU 1371 CB PRO C 266 4064 3084 3994 -525 189 -47 C ATOM 1372 CG PRO C 266 188.316 28.986 15.240 1.00 29.36 C ANISOU 1372 CG PRO C 266 4063 3168 3923 -593 246 -207 C ATOM 1373 CD PRO C 266 188.262 30.448 14.898 1.00 28.07 C ANISOU 1373 CD PRO C 266 3772 3192 3703 -575 164 -189 C ATOM 1374 N PHE C 267 190.162 31.718 18.132 1.00 26.90 N ANISOU 1374 N PHE C 267 3495 3040 3685 -432 -23 182 N ATOM 1375 CA PHE C 267 191.147 32.234 19.104 1.00 28.54 C ANISOU 1375 CA PHE C 267 3630 3281 3935 -367 -89 310 C ATOM 1376 C PHE C 267 190.586 33.311 20.045 1.00 32.89 C ANISOU 1376 C PHE C 267 4114 3953 4430 -466 -157 328 C ATOM 1377 O PHE C 267 191.198 33.627 21.055 1.00 27.28 O ANISOU 1377 O PHE C 267 3359 3278 3730 -457 -211 422 O ATOM 1378 CB PHE C 267 192.399 32.771 18.401 1.00 29.24 C ANISOU 1378 CB PHE C 267 3620 3410 4078 -238 -74 334 C ATOM 1379 CG PHE C 267 193.260 31.683 17.797 1.00 31.55 C ANISOU 1379 CG PHE C 267 3955 3574 4458 -124 -7 334 C ATOM 1380 CD1 PHE C 267 194.193 31.007 18.572 1.00 32.99 C ANISOU 1380 CD1 PHE C 267 4140 3669 4727 -26 -35 443 C ATOM 1381 CD2 PHE C 267 193.122 31.324 16.455 1.00 28.29 C ANISOU 1381 CD2 PHE C 267 3577 3130 4044 -117 84 221 C ATOM 1382 CE1 PHE C 267 194.963 29.991 18.025 1.00 31.95 C ANISOU 1382 CE1 PHE C 267 4037 3399 4703 91 34 436 C ATOM 1383 CE2 PHE C 267 193.897 30.319 15.910 1.00 29.63 C ANISOU 1383 CE2 PHE C 267 3780 3170 4307 -22 165 199 C ATOM 1384 CZ PHE C 267 194.819 29.647 16.692 1.00 30.72 C ANISOU 1384 CZ PHE C 267 3914 3200 4557 90 144 305 C ATOM 1385 N GLY C 268 189.426 33.881 19.734 1.00 29.46 N ANISOU 1385 N GLY C 268 3865 3858 3472 -623 -309 -108 N ATOM 1386 CA GLY C 268 188.856 34.864 20.654 1.00 28.87 C ANISOU 1386 CA GLY C 268 4106 3613 3250 -593 -165 -161 C ATOM 1387 C GLY C 268 187.975 35.873 19.936 1.00 30.52 C ANISOU 1387 C GLY C 268 4311 3814 3470 -333 4 -172 C ATOM 1388 O GLY C 268 187.587 35.654 18.792 1.00 29.72 O ANISOU 1388 O GLY C 268 3940 3872 3481 -183 7 -141 O ATOM 1389 N ALA C 269 187.648 36.970 20.610 1.00 29.12 N ANISOU 1389 N ALA C 269 4451 3440 3175 -284 140 -213 N ATOM 1390 CA ALA C 269 186.793 37.998 20.018 1.00 30.87 C ANISOU 1390 CA ALA C 269 4679 3621 3430 -29 313 -209 C ATOM 1391 C ALA C 269 187.396 38.615 18.763 1.00 26.99 C ANISOU 1391 C ALA C 269 4077 3147 3031 12 196 -122 C ATOM 1392 O ALA C 269 188.474 39.219 18.814 1.00 27.22 O ANISOU 1392 O ALA C 269 4287 3033 3023 -134 61 -76 O ATOM 1393 CB ALA C 269 186.485 39.110 21.031 1.00 30.08 C ANISOU 1393 CB ALA C 269 4998 3255 3176 12 484 -278 C ATOM 1394 N VAL C 270 186.676 38.498 17.653 1.00 27.46 N ANISOU 1394 N VAL C 270 3851 3376 3208 203 240 -79 N ATOM 1395 CA VAL C 270 187.072 39.127 16.378 1.00 27.47 C ANISOU 1395 CA VAL C 270 3747 3410 3278 271 159 14 C ATOM 1396 C VAL C 270 185.987 40.139 15.997 1.00 31.27 C ANISOU 1396 C VAL C 270 4236 3834 3812 511 321 41 C ATOM 1397 O VAL C 270 184.822 39.804 16.021 1.00 28.19 O ANISOU 1397 O VAL C 270 3696 3531 3484 659 447 33 O ATOM 1398 CB VAL C 270 187.226 38.076 15.252 1.00 30.32 C ANISOU 1398 CB VAL C 270 3783 4019 3718 276 42 56 C ATOM 1399 CG1 VAL C 270 187.563 38.754 13.880 1.00 24.59 C ANISOU 1399 CG1 VAL C 270 2969 3341 3032 359 -16 160 C ATOM 1400 CG2 VAL C 270 188.319 37.057 15.623 1.00 26.49 C ANISOU 1400 CG2 VAL C 270 3273 3575 3219 60 -99 43 C ATOM 1401 N THR C 271 186.347 41.383 15.708 1.00 28.79 N ANISOU 1401 N THR C 271 4088 3358 3494 545 315 92 N ATOM 1402 CA THR C 271 185.320 42.381 15.423 1.00 32.68 C ANISOU 1402 CA THR C 271 4594 3764 4059 778 475 127 C ATOM 1403 C THR C 271 185.226 42.706 13.936 1.00 32.96 C ANISOU 1403 C THR C 271 4394 3928 4200 878 388 256 C ATOM 1404 O THR C 271 184.238 43.262 13.494 1.00 31.46 O ANISOU 1404 O THR C 271 4109 3730 4114 1074 490 319 O ATOM 1405 CB THR C 271 185.569 43.691 16.178 1.00 36.59 C ANISOU 1405 CB THR C 271 5479 3943 4481 781 551 92 C ATOM 1406 OG1 THR C 271 186.938 44.085 15.971 1.00 34.91 O ANISOU 1406 OG1 THR C 271 5399 3644 4221 582 340 146 O ATOM 1407 CG2 THR C 271 185.284 43.533 17.716 1.00 33.74 C ANISOU 1407 CG2 THR C 271 5413 3423 3984 743 708 -46 C ATOM 1408 N ASN C 272 186.257 42.379 13.171 1.00 28.85 N ANISOU 1408 N ASN C 272 3785 3518 3656 747 207 313 N ATOM 1409 CA ASN C 272 186.248 42.750 11.752 1.00 36.82 C ANISOU 1409 CA ASN C 272 4621 4643 4725 830 131 441 C ATOM 1410 C ASN C 272 187.246 41.921 10.962 1.00 31.44 C ANISOU 1410 C ASN C 272 3803 4144 4000 704 -17 480 C ATOM 1411 O ASN C 272 188.297 41.556 11.505 1.00 27.46 O ANISOU 1411 O ASN C 272 3386 3599 3449 533 -80 455 O ATOM 1412 CB ASN C 272 186.606 44.227 11.605 1.00 38.02 C ANISOU 1412 CB ASN C 272 4958 4589 4897 858 128 526 C ATOM 1413 CG ASN C 272 186.565 44.683 10.159 1.00 46.82 C ANISOU 1413 CG ASN C 272 5903 5820 6066 940 51 678 C ATOM 1414 OD1 ASN C 272 185.502 45.013 9.628 1.00 46.89 O ANISOU 1414 OD1 ASN C 272 5790 5862 6162 1108 106 735 O ATOM 1415 ND2 ASN C 272 187.719 44.686 9.512 1.00 48.20 N ANISOU 1415 ND2 ASN C 272 6059 6058 6195 818 -74 766 N ATOM 1416 N VAL C 273 186.948 41.624 9.697 1.00 27.10 N ANISOU 1416 N VAL C 273 3055 3782 3462 784 -70 552 N ATOM 1417 CA VAL C 273 187.966 40.993 8.831 1.00 26.58 C ANISOU 1417 CA VAL C 273 2900 3865 3332 696 -170 598 C ATOM 1418 C VAL C 273 187.893 41.695 7.489 1.00 28.74 C ANISOU 1418 C VAL C 273 3113 4211 3596 787 -207 737 C ATOM 1419 O VAL C 273 186.849 42.265 7.153 1.00 31.86 O ANISOU 1419 O VAL C 273 3467 4593 4046 915 -188 783 O ATOM 1420 CB VAL C 273 187.740 39.445 8.637 1.00 28.12 C ANISOU 1420 CB VAL C 273 2945 4247 3493 675 -208 504 C ATOM 1421 CG1 VAL C 273 187.589 38.742 10.005 1.00 27.96 C ANISOU 1421 CG1 VAL C 273 2966 4162 3494 592 -172 379 C ATOM 1422 CG2 VAL C 273 186.535 39.141 7.715 1.00 32.37 C ANISOU 1422 CG2 VAL C 273 3337 4926 4038 804 -243 525 C ATOM 1423 N LYS C 274 188.984 41.683 6.730 1.00 32.38 N ANISOU 1423 N LYS C 274 3559 4744 3999 724 -253 829 N ATOM 1424 CA LYS C 274 188.978 42.336 5.410 1.00 33.79 C ANISOU 1424 CA LYS C 274 3694 5005 4140 799 -285 977 C ATOM 1425 C LYS C 274 189.876 41.577 4.468 1.00 31.79 C ANISOU 1425 C LYS C 274 3377 4924 3776 764 -296 1019 C ATOM 1426 O LYS C 274 191.029 41.345 4.793 1.00 27.64 O ANISOU 1426 O LYS C 274 2866 4373 3262 665 -275 1046 O ATOM 1427 CB LYS C 274 189.507 43.773 5.530 1.00 37.29 C ANISOU 1427 CB LYS C 274 4248 5274 4646 776 -291 1115 C ATOM 1428 CG LYS C 274 189.753 44.515 4.179 1.00 46.99 C ANISOU 1428 CG LYS C 274 5433 6587 5836 823 -330 1307 C ATOM 1429 CD LYS C 274 188.472 45.037 3.550 1.00 50.14 C ANISOU 1429 CD LYS C 274 5781 7007 6263 959 -355 1353 C ATOM 1430 CE LYS C 274 188.800 45.797 2.250 1.00 54.40 C ANISOU 1430 CE LYS C 274 6295 7624 6750 980 -409 1559 C ATOM 1431 NZ LYS C 274 187.844 45.482 1.151 1.00 54.63 N ANISOU 1431 NZ LYS C 274 6234 7818 6703 1065 -471 1598 N ATOM 1432 N VAL C 275 189.373 41.215 3.289 1.00 30.68 N ANISOU 1432 N VAL C 275 3180 4948 3530 844 -329 1041 N ATOM 1433 CA VAL C 275 190.232 40.608 2.278 1.00 35.35 C ANISOU 1433 CA VAL C 275 3761 5690 3982 838 -302 1085 C ATOM 1434 C VAL C 275 190.521 41.675 1.224 1.00 36.78 C ANISOU 1434 C VAL C 275 3964 5904 4105 876 -304 1285 C ATOM 1435 O VAL C 275 189.605 42.337 0.793 1.00 36.24 O ANISOU 1435 O VAL C 275 3896 5831 4043 936 -372 1343 O ATOM 1436 CB VAL C 275 189.521 39.383 1.642 1.00 38.25 C ANISOU 1436 CB VAL C 275 4111 6203 4219 885 -352 961 C ATOM 1437 CG1 VAL C 275 190.255 38.890 0.430 1.00 38.75 C ANISOU 1437 CG1 VAL C 275 4223 6408 4094 913 -305 1003 C ATOM 1438 CG2 VAL C 275 189.396 38.237 2.682 1.00 41.43 C ANISOU 1438 CG2 VAL C 275 4478 6577 4688 832 -353 781 C ATOM 1439 N ILE C 276 191.782 41.875 0.843 1.00 34.06 N ANISOU 1439 N ILE C 276 3983 5461 3497 968 -40 1091 N ATOM 1440 CA ILE C 276 192.103 42.935 -0.106 1.00 32.74 C ANISOU 1440 CA ILE C 276 3794 5351 3294 884 -70 1033 C ATOM 1441 C ILE C 276 192.040 42.331 -1.508 1.00 35.23 C ANISOU 1441 C ILE C 276 4326 5528 3531 809 -174 1014 C ATOM 1442 O ILE C 276 192.673 41.311 -1.776 1.00 33.62 O ANISOU 1442 O ILE C 276 4275 5291 3206 894 -154 965 O ATOM 1443 CB ILE C 276 193.516 43.524 0.139 1.00 39.81 C ANISOU 1443 CB ILE C 276 4610 6453 4062 1011 58 911 C ATOM 1444 CG1 ILE C 276 193.620 44.098 1.569 1.00 37.89 C ANISOU 1444 CG1 ILE C 276 4146 6364 3886 1096 160 913 C ATOM 1445 CG2 ILE C 276 193.875 44.589 -0.952 1.00 35.87 C ANISOU 1445 CG2 ILE C 276 4111 5994 3525 919 41 851 C ATOM 1446 CD1 ILE C 276 192.554 45.163 1.859 1.00 38.13 C ANISOU 1446 CD1 ILE C 276 4008 6379 4100 961 121 992 C ATOM 1447 N ARG C 277 191.261 42.952 -2.382 1.00 35.57 N ANISOU 1447 N ARG C 277 4381 5492 3643 654 -287 1054 N ATOM 1448 CA ARG C 277 190.990 42.418 -3.716 1.00 38.76 C ANISOU 1448 CA ARG C 277 4983 5758 3986 567 -408 1045 C ATOM 1449 C ARG C 277 191.428 43.385 -4.803 1.00 40.36 C ANISOU 1449 C ARG C 277 5214 6016 4103 509 -430 996 C ATOM 1450 O ARG C 277 191.569 44.588 -4.572 1.00 42.87 O ANISOU 1450 O ARG C 277 5382 6442 4464 491 -378 997 O ATOM 1451 CB ARG C 277 189.490 42.173 -3.906 1.00 41.59 C ANISOU 1451 CB ARG C 277 5351 5946 4505 428 -551 1143 C ATOM 1452 CG ARG C 277 188.902 41.106 -2.986 1.00 45.16 C ANISOU 1452 CG ARG C 277 5802 6299 5057 464 -535 1199 C ATOM 1453 CD ARG C 277 187.528 40.612 -3.433 1.00 46.69 C ANISOU 1453 CD ARG C 277 6051 6299 5392 325 -682 1264 C ATOM 1454 NE ARG C 277 187.198 39.373 -2.735 1.00 49.72 N ANISOU 1454 NE ARG C 277 6484 6571 5838 375 -644 1296 N ATOM 1455 CZ ARG C 277 186.653 39.319 -1.517 1.00 53.04 C ANISOU 1455 CZ ARG C 277 6775 6980 6396 399 -579 1371 C ATOM 1456 NH1 ARG C 277 186.366 40.439 -0.856 1.00 51.10 N ANISOU 1456 NH1 ARG C 277 6337 6834 6244 373 -551 1414 N ATOM 1457 NH2 ARG C 277 186.393 38.141 -0.953 1.00 54.19 N ANISOU 1457 NH2 ARG C 277 6988 7012 6589 450 -533 1403 N ATOM 1458 N ASP C 278 191.620 42.849 -6.000 1.00 37.29 N ANISOU 1458 N ASP C 278 5023 5548 3596 477 -503 955 N ATOM 1459 CA ASP C 278 191.818 43.690 -7.165 1.00 38.54 C ANISOU 1459 CA ASP C 278 5239 5727 3676 405 -545 929 C ATOM 1460 C ASP C 278 190.409 43.875 -7.687 1.00 35.53 C ANISOU 1460 C ASP C 278 4867 5217 3417 257 -714 1023 C ATOM 1461 O ASP C 278 189.732 42.897 -7.965 1.00 36.90 O ANISOU 1461 O ASP C 278 5148 5255 3617 215 -819 1043 O ATOM 1462 CB ASP C 278 192.702 42.975 -8.177 1.00 42.91 C ANISOU 1462 CB ASP C 278 6005 6261 4036 448 -539 836 C ATOM 1463 CG ASP C 278 193.038 43.841 -9.382 1.00 54.61 C ANISOU 1463 CG ASP C 278 7561 7773 5415 390 -558 806 C ATOM 1464 OD1 ASP C 278 192.194 44.669 -9.797 1.00 58.62 O ANISOU 1464 OD1 ASP C 278 8024 8248 6002 282 -650 880 O ATOM 1465 OD2 ASP C 278 194.155 43.690 -9.919 1.00 61.40 O ANISOU 1465 OD2 ASP C 278 8527 8688 6115 456 -477 710 O ATOM 1466 N PHE C 279 189.949 45.117 -7.785 1.00 34.49 N ANISOU 1466 N PHE C 279 4613 5122 3368 181 -739 1076 N ATOM 1467 CA PHE C 279 188.575 45.367 -8.215 1.00 40.26 C ANISOU 1467 CA PHE C 279 5331 5739 4228 47 -905 1166 C ATOM 1468 C PHE C 279 188.226 44.708 -9.563 1.00 42.98 C ANISOU 1468 C PHE C 279 5890 5966 4474 -17 -1058 1149 C ATOM 1469 O PHE C 279 187.115 44.196 -9.751 1.00 41.97 O ANISOU 1469 O PHE C 279 5789 5711 4446 -100 -1201 1194 O ATOM 1470 CB PHE C 279 188.281 46.868 -8.273 1.00 38.30 C ANISOU 1470 CB PHE C 279 4936 5555 4060 -14 -900 1221 C ATOM 1471 CG PHE C 279 186.875 47.193 -8.751 1.00 38.10 C ANISOU 1471 CG PHE C 279 4892 5419 4167 -145 -1078 1313 C ATOM 1472 CD1 PHE C 279 185.808 47.196 -7.860 1.00 37.24 C ANISOU 1472 CD1 PHE C 279 4631 5254 4265 -197 -1122 1387 C ATOM 1473 CD2 PHE C 279 186.634 47.488 -10.073 1.00 37.54 C ANISOU 1473 CD2 PHE C 279 4952 5302 4009 -209 -1198 1323 C ATOM 1474 CE1 PHE C 279 184.515 47.494 -8.295 1.00 40.34 C ANISOU 1474 CE1 PHE C 279 4995 5546 4788 -315 -1288 1462 C ATOM 1475 CE2 PHE C 279 185.354 47.786 -10.519 1.00 39.53 C ANISOU 1475 CE2 PHE C 279 5181 5461 4376 -318 -1370 1401 C ATOM 1476 CZ PHE C 279 184.291 47.793 -9.618 1.00 40.88 C ANISOU 1476 CZ PHE C 279 5190 5576 4767 -372 -1416 1468 C ATOM 1477 N ASN C 280 189.159 44.735 -10.505 1.00 45.42 N ANISOU 1477 N ASN C 280 6346 6318 4591 19 -1026 1077 N ATOM 1478 CA ASN C 280 188.856 44.293 -11.858 1.00 47.87 C ANISOU 1478 CA ASN C 280 6856 6537 4793 -43 -1170 1057 C ATOM 1479 C ASN C 280 188.955 42.804 -12.131 1.00 49.50 C ANISOU 1479 C ASN C 280 7230 6650 4929 -18 -1212 993 C ATOM 1480 O ASN C 280 188.444 42.329 -13.141 1.00 51.97 O ANISOU 1480 O ASN C 280 7688 6869 5189 -84 -1356 977 O ATOM 1481 CB ASN C 280 189.727 45.020 -12.866 1.00 50.31 C ANISOU 1481 CB ASN C 280 7266 6925 4926 -26 -1123 1014 C ATOM 1482 CG ASN C 280 189.430 46.484 -12.921 1.00 50.35 C ANISOU 1482 CG ASN C 280 7142 6988 5001 -73 -1114 1087 C ATOM 1483 OD1 ASN C 280 188.395 46.898 -13.438 1.00 51.81 O ANISOU 1483 OD1 ASN C 280 7325 7109 5253 -165 -1262 1163 O ATOM 1484 ND2 ASN C 280 190.350 47.289 -12.410 1.00 44.41 N ANISOU 1484 ND2 ASN C 280 6281 6357 4235 -10 -939 1060 N ATOM 1485 N THR C 281 189.641 42.062 -11.274 1.00 43.79 N ANISOU 1485 N THR C 281 6491 5951 4196 82 -1087 949 N ATOM 1486 CA THR C 281 189.665 40.627 -11.476 1.00 45.00 C ANISOU 1486 CA THR C 281 6795 5998 4304 105 -1120 896 C ATOM 1487 C THR C 281 188.803 40.011 -10.406 1.00 45.88 C ANISOU 1487 C THR C 281 6803 6024 4605 94 -1132 956 C ATOM 1488 O THR C 281 188.493 38.821 -10.445 1.00 46.44 O ANISOU 1488 O THR C 281 6972 5975 4700 91 -1172 933 O ATOM 1489 CB THR C 281 191.083 40.053 -11.397 1.00 46.52 C ANISOU 1489 CB THR C 281 7079 6262 4336 235 -973 799 C ATOM 1490 OG1 THR C 281 191.646 40.375 -10.123 1.00 45.23 O ANISOU 1490 OG1 THR C 281 6752 6207 4225 335 -820 811 O ATOM 1491 CG2 THR C 281 191.959 40.632 -12.526 1.00 48.79 C ANISOU 1491 CG2 THR C 281 7480 6623 4433 240 -950 732 C ATOM 1492 N ASN C 282 188.396 40.856 -9.466 1.00 47.72 N ANISOU 1492 N ASN C 282 6837 6315 4980 85 -1092 1032 N ATOM 1493 CA ASN C 282 187.767 40.402 -8.228 1.00 52.75 C ANISOU 1493 CA ASN C 282 7352 6900 5789 99 -1056 1092 C ATOM 1494 C ASN C 282 188.509 39.228 -7.584 1.00 50.75 C ANISOU 1494 C ASN C 282 7168 6636 5478 225 -937 1048 C ATOM 1495 O ASN C 282 187.898 38.351 -6.979 1.00 53.51 O ANISOU 1495 O ASN C 282 7514 6875 5941 225 -940 1084 O ATOM 1496 CB ASN C 282 186.277 40.079 -8.432 1.00 60.63 C ANISOU 1496 CB ASN C 282 8341 7739 6957 -32 -1215 1149 C ATOM 1497 CG ASN C 282 185.505 40.077 -7.124 1.00 65.29 C ANISOU 1497 CG ASN C 282 8757 8295 7753 -39 -1172 1231 C ATOM 1498 OD1 ASN C 282 185.684 40.956 -6.275 1.00 64.51 O ANISOU 1498 OD1 ASN C 282 8494 8309 7707 -3 -1081 1273 O ATOM 1499 ND2 ASN C 282 184.666 39.074 -6.942 1.00 69.96 N ANISOU 1499 ND2 ASN C 282 9385 8730 8465 -84 -1225 1248 N ATOM 1500 N LYS C 283 189.835 39.219 -7.714 1.00 45.22 N ANISOU 1500 N LYS C 283 6529 6047 4605 336 -827 970 N ATOM 1501 CA LYS C 283 190.662 38.255 -6.993 1.00 45.27 C ANISOU 1501 CA LYS C 283 6578 6073 4551 479 -699 930 C ATOM 1502 C LYS C 283 191.338 38.900 -5.777 1.00 40.22 C ANISOU 1502 C LYS C 283 5764 5598 3919 595 -550 939 C ATOM 1503 O LYS C 283 191.675 40.083 -5.793 1.00 37.31 O ANISOU 1503 O LYS C 283 5286 5357 3533 586 -517 928 O ATOM 1504 CB LYS C 283 191.720 37.644 -7.913 1.00 48.33 C ANISOU 1504 CB LYS C 283 7153 6468 4741 539 -674 823 C ATOM 1505 CG LYS C 283 191.134 36.851 -9.070 1.00 53.43 C ANISOU 1505 CG LYS C 283 7981 6954 5366 440 -812 796 C ATOM 1506 CD LYS C 283 190.155 35.798 -8.550 1.00 59.03 C ANISOU 1506 CD LYS C 283 8700 7501 6230 409 -854 848 C ATOM 1507 N CYS C 284 191.543 38.102 -4.738 1.00 39.46 N ANISOU 1507 N CYS C 284 5646 5498 3848 709 -458 956 N ATOM 1508 CA CYS C 284 192.313 38.526 -3.568 1.00 35.79 C ANISOU 1508 CA CYS C 284 5035 5201 3363 847 -314 946 C ATOM 1509 C CYS C 284 193.771 38.732 -3.961 1.00 37.26 C ANISOU 1509 C CYS C 284 5267 5526 3363 952 -227 829 C ATOM 1510 O CYS C 284 194.343 37.890 -4.655 1.00 39.77 O ANISOU 1510 O CYS C 284 5757 5791 3563 991 -229 763 O ATOM 1511 CB CYS C 284 192.201 37.464 -2.475 1.00 34.17 C ANISOU 1511 CB CYS C 284 4833 4944 3205 957 -242 994 C ATOM 1512 SG CYS C 284 193.245 37.745 -1.031 1.00 36.35 S ANISOU 1512 SG CYS C 284 4956 5433 3422 1161 -70 970 S ATOM 1513 N LYS C 285 194.376 39.842 -3.532 1.00 34.83 N ANISOU 1513 N LYS C 285 4803 5393 3038 995 -146 793 N ATOM 1514 CA LYS C 285 195.781 40.122 -3.884 1.00 38.42 C ANISOU 1514 CA LYS C 285 5282 5985 3332 1091 -51 668 C ATOM 1515 C LYS C 285 196.789 39.335 -3.035 1.00 42.18 C ANISOU 1515 C LYS C 285 5760 6547 3719 1286 67 608 C ATOM 1516 O LYS C 285 198.007 39.535 -3.151 1.00 42.49 O ANISOU 1516 O LYS C 285 5794 6714 3636 1385 157 494 O ATOM 1517 CB LYS C 285 196.079 41.620 -3.772 1.00 40.67 C ANISOU 1517 CB LYS C 285 5392 6419 3641 1062 2 637 C ATOM 1518 CG LYS C 285 195.174 42.514 -4.641 1.00 45.79 C ANISOU 1518 CG LYS C 285 6035 6995 4367 883 -106 697 C ATOM 1519 CD LYS C 285 195.769 43.918 -4.809 1.00 49.64 C ANISOU 1519 CD LYS C 285 6396 7622 4841 867 -29 641 C ATOM 1520 N GLY C 286 196.284 38.463 -2.165 1.00 32.91 N ANISOU 1520 N GLY C 286 4588 5305 2612 1345 72 684 N ATOM 1521 CA GLY C 286 197.146 37.584 -1.388 1.00 33.25 C ANISOU 1521 CA GLY C 286 4656 5409 2567 1539 174 646 C ATOM 1522 C GLY C 286 197.186 37.928 0.096 1.00 40.72 C ANISOU 1522 C GLY C 286 5413 6492 3567 1653 260 681 C ATOM 1523 O GLY C 286 197.847 37.254 0.882 1.00 39.44 O ANISOU 1523 O GLY C 286 5254 6396 3335 1830 343 661 O ATOM 1524 N PHE C 287 196.499 38.990 0.490 1.00 29.90 N ANISOU 1524 N PHE C 287 3566 3226 4568 424 -307 954 N ATOM 1525 CA PHE C 287 196.568 39.409 1.890 1.00 29.99 C ANISOU 1525 CA PHE C 287 3657 3117 4619 368 -306 957 C ATOM 1526 C PHE C 287 195.273 39.991 2.406 1.00 29.50 C ANISOU 1526 C PHE C 287 3660 3034 4514 550 -241 888 C ATOM 1527 O PHE C 287 194.357 40.345 1.645 1.00 30.86 O ANISOU 1527 O PHE C 287 3842 3210 4673 763 -207 904 O ATOM 1528 CB PHE C 287 197.756 40.363 2.155 1.00 29.54 C ANISOU 1528 CB PHE C 287 3792 2875 4559 197 -278 944 C ATOM 1529 CG PHE C 287 197.708 41.649 1.378 1.00 31.98 C ANISOU 1529 CG PHE C 287 4301 2983 4866 303 -200 977 C ATOM 1530 CD1 PHE C 287 198.230 41.707 0.087 1.00 34.53 C ANISOU 1530 CD1 PHE C 287 4629 3318 5172 305 -202 1019 C ATOM 1531 CD2 PHE C 287 197.207 42.818 1.951 1.00 29.89 C ANISOU 1531 CD2 PHE C 287 4236 2556 4565 380 -109 913 C ATOM 1532 CE1 PHE C 287 198.221 42.894 -0.639 1.00 38.12 C ANISOU 1532 CE1 PHE C 287 5286 3614 5583 389 -129 1024 C ATOM 1533 CE2 PHE C 287 197.189 44.015 1.230 1.00 36.66 C ANISOU 1533 CE2 PHE C 287 5298 3209 5420 482 -26 952 C ATOM 1534 CZ PHE C 287 197.695 44.053 -0.076 1.00 39.07 C ANISOU 1534 CZ PHE C 287 5607 3533 5703 479 -51 1004 C ATOM 1535 N GLY C 288 195.178 40.047 3.729 1.00 25.98 N ANISOU 1535 N GLY C 288 3250 2589 4032 465 -225 798 N ATOM 1536 CA GLY C 288 193.969 40.513 4.374 1.00 24.01 C ANISOU 1536 CA GLY C 288 3047 2336 3738 618 -165 718 C ATOM 1537 C GLY C 288 194.318 40.909 5.812 1.00 26.31 C ANISOU 1537 C GLY C 288 3443 2564 3991 467 -140 623 C ATOM 1538 O GLY C 288 195.497 40.845 6.225 1.00 23.95 O ANISOU 1538 O GLY C 288 3176 2228 3695 253 -170 622 O ATOM 1539 N PHE C 289 193.297 41.334 6.560 1.00 28.01 N ANISOU 1539 N PHE C 289 3705 2776 4163 580 -85 536 N ATOM 1540 CA PHE C 289 193.481 41.884 7.908 1.00 29.00 C ANISOU 1540 CA PHE C 289 3947 2830 4243 464 -46 434 C ATOM 1541 C PHE C 289 192.391 41.367 8.799 1.00 30.43 C ANISOU 1541 C PHE C 289 4025 3155 4380 533 -37 354 C ATOM 1542 O PHE C 289 191.277 41.172 8.336 1.00 26.88 O ANISOU 1542 O PHE C 289 3494 2789 3929 728 -23 355 O ATOM 1543 CB PHE C 289 193.337 43.405 7.880 1.00 29.20 C ANISOU 1543 CB PHE C 289 4211 2628 4256 550 49 394 C ATOM 1544 CG PHE C 289 194.375 44.085 7.031 1.00 34.25 C ANISOU 1544 CG PHE C 289 4987 3094 4932 480 65 463 C ATOM 1545 CD1 PHE C 289 195.643 44.321 7.543 1.00 33.78 C ANISOU 1545 CD1 PHE C 289 5007 2957 4871 234 60 435 C ATOM 1546 CD2 PHE C 289 194.094 44.465 5.721 1.00 34.42 C ANISOU 1546 CD2 PHE C 289 5052 3044 4983 655 86 552 C ATOM 1547 CE1 PHE C 289 196.616 44.922 6.776 1.00 35.57 C ANISOU 1547 CE1 PHE C 289 5354 3032 5129 151 81 488 C ATOM 1548 CE2 PHE C 289 195.070 45.071 4.938 1.00 37.66 C ANISOU 1548 CE2 PHE C 289 5592 3293 5422 579 107 618 C ATOM 1549 CZ PHE C 289 196.336 45.293 5.472 1.00 34.97 C ANISOU 1549 CZ PHE C 289 5330 2872 5086 319 107 582 C ATOM 1550 N VAL C 290 192.678 41.197 10.083 1.00 27.21 N ANISOU 1550 N VAL C 290 3626 2783 3930 378 -41 279 N ATOM 1551 CA VAL C 290 191.598 40.869 11.016 1.00 24.32 C ANISOU 1551 CA VAL C 290 3191 2535 3513 442 -17 192 C ATOM 1552 C VAL C 290 191.813 41.757 12.233 1.00 29.82 C ANISOU 1552 C VAL C 290 4045 3126 4159 347 35 85 C ATOM 1553 O VAL C 290 192.948 42.105 12.560 1.00 27.49 O ANISOU 1553 O VAL C 290 3841 2743 3862 168 25 81 O ATOM 1554 CB VAL C 290 191.691 39.389 11.418 1.00 29.19 C ANISOU 1554 CB VAL C 290 3612 3357 4122 334 -84 215 C ATOM 1555 CG1 VAL C 290 190.818 39.098 12.583 1.00 28.87 C ANISOU 1555 CG1 VAL C 290 3527 3423 4020 344 -53 119 C ATOM 1556 CG2 VAL C 290 191.333 38.498 10.221 1.00 28.17 C ANISOU 1556 CG2 VAL C 290 3319 3340 4044 437 -122 303 C ATOM 1557 N THR C 291 190.743 42.181 12.883 1.00 27.20 N ANISOU 1557 N THR C 291 3747 2802 3785 464 96 -10 N ATOM 1558 CA THR C 291 190.903 42.939 14.121 1.00 31.46 C ANISOU 1558 CA THR C 291 4421 3261 4271 365 147 -123 C ATOM 1559 C THR C 291 190.384 42.118 15.304 1.00 31.08 C ANISOU 1559 C THR C 291 4254 3395 4162 304 133 -193 C ATOM 1560 O THR C 291 189.257 41.605 15.254 1.00 26.21 O ANISOU 1560 O THR C 291 3522 2903 3532 443 143 -211 O ATOM 1561 CB THR C 291 190.167 44.276 14.042 1.00 33.77 C ANISOU 1561 CB THR C 291 4887 3386 4559 540 243 -191 C ATOM 1562 OG1 THR C 291 190.681 45.020 12.929 1.00 37.19 O ANISOU 1562 OG1 THR C 291 5445 3641 5046 594 264 -115 O ATOM 1563 CG2 THR C 291 190.320 45.089 15.360 1.00 30.36 C ANISOU 1563 CG2 THR C 291 4596 2866 4074 430 305 -323 C ATOM 1564 N MET C 292 191.214 41.976 16.344 1.00 27.90 N ANISOU 1564 N MET C 292 3873 3016 3714 95 111 -233 N ATOM 1565 CA MET C 292 190.795 41.230 17.536 1.00 29.11 C ANISOU 1565 CA MET C 292 3930 3335 3796 26 101 -294 C ATOM 1566 C MET C 292 190.853 42.142 18.737 1.00 28.30 C ANISOU 1566 C MET C 292 3964 3161 3629 -52 159 -423 C ATOM 1567 O MET C 292 191.767 42.940 18.865 1.00 28.56 O ANISOU 1567 O MET C 292 4128 3060 3663 -164 172 -447 O ATOM 1568 CB MET C 292 191.678 39.992 17.773 1.00 26.16 C ANISOU 1568 CB MET C 292 3429 3102 3409 -145 14 -217 C ATOM 1569 CG MET C 292 191.589 38.957 16.648 1.00 26.27 C ANISOU 1569 CG MET C 292 3293 3201 3486 -78 -39 -97 C ATOM 1570 SD MET C 292 192.465 37.396 16.903 1.00 28.25 S ANISOU 1570 SD MET C 292 3390 3619 3725 -246 -131 -4 S ATOM 1571 CE MET C 292 191.465 36.707 18.260 1.00 28.80 C ANISOU 1571 CE MET C 292 3390 3849 3705 -253 -95 -83 C ATOM 1572 N THR C 293 189.895 42.011 19.634 1.00 28.32 N ANISOU 1572 N THR C 293 3931 3258 3572 -5 197 -512 N ATOM 1573 CA THR C 293 189.774 42.965 20.716 1.00 30.15 C ANISOU 1573 CA THR C 293 4294 3418 3745 -50 263 -647 C ATOM 1574 C THR C 293 190.862 42.804 21.771 1.00 32.88 C ANISOU 1574 C THR C 293 4657 3811 4027 -290 228 -680 C ATOM 1575 O THR C 293 191.349 43.792 22.321 1.00 33.34 O ANISOU 1575 O THR C 293 4855 3752 4058 -379 272 -769 O ATOM 1576 CB THR C 293 188.407 42.787 21.408 1.00 30.39 C ANISOU 1576 CB THR C 293 4263 3560 3723 65 312 -739 C ATOM 1577 OG1 THR C 293 187.384 42.742 20.402 1.00 31.69 O ANISOU 1577 OG1 THR C 293 4372 3731 3938 290 332 -706 O ATOM 1578 CG2 THR C 293 188.142 43.931 22.381 1.00 35.59 C ANISOU 1578 CG2 THR C 293 5069 4122 4331 56 393 -887 C ATOM 1579 N ASN C 294 191.230 41.561 22.064 1.00 33.82 N ANISOU 1579 N ASN C 294 4633 4102 4113 -391 153 -611 N ATOM 1580 CA ASN C 294 192.118 41.277 23.204 1.00 35.35 C ANISOU 1580 CA ASN C 294 4822 4387 4222 -597 116 -644 C ATOM 1581 C ASN C 294 193.554 40.924 22.772 1.00 33.83 C ANISOU 1581 C ASN C 294 4607 4195 4050 -741 36 -552 C ATOM 1582 O ASN C 294 193.783 39.941 22.058 1.00 29.95 O ANISOU 1582 O ASN C 294 4000 3777 3601 -725 -29 -430 O ATOM 1583 CB ASN C 294 191.524 40.159 24.063 1.00 34.16 C ANISOU 1583 CB ASN C 294 4544 4438 3997 -612 99 -642 C ATOM 1584 CG ASN C 294 190.130 40.501 24.553 1.00 37.27 C ANISOU 1584 CG ASN C 294 4950 4849 4361 -484 180 -748 C ATOM 1585 OD1 ASN C 294 189.920 41.539 25.184 1.00 43.49 O ANISOU 1585 OD1 ASN C 294 5855 5554 5115 -487 243 -871 O ATOM 1586 ND2 ASN C 294 189.161 39.673 24.198 1.00 38.14 N ANISOU 1586 ND2 ASN C 294 4943 5061 4489 -368 185 -708 N ATOM 1587 N TYR C 295 194.506 41.722 23.243 1.00 34.77 N ANISOU 1587 N TYR C 295 4815 4649 3747 -448 107 -693 N ATOM 1588 CA TYR C 295 195.911 41.567 22.875 1.00 35.97 C ANISOU 1588 CA TYR C 295 4934 4928 3806 -519 34 -667 C ATOM 1589 C TYR C 295 196.410 40.120 22.952 1.00 33.59 C ANISOU 1589 C TYR C 295 4545 4799 3419 -435 8 -466 C ATOM 1590 O TYR C 295 197.031 39.614 22.002 1.00 30.11 O ANISOU 1590 O TYR C 295 4099 4312 3028 -433 -50 -360 O ATOM 1591 CB TYR C 295 196.793 42.468 23.754 1.00 43.34 C ANISOU 1591 CB TYR C 295 5842 6052 4572 -643 33 -855 C ATOM 1592 CG TYR C 295 198.129 42.747 23.112 1.00 52.75 C ANISOU 1592 CG TYR C 295 7026 7279 5736 -745 -39 -875 C ATOM 1593 CD1 TYR C 295 198.257 43.725 22.130 1.00 53.31 C ANISOU 1593 CD1 TYR C 295 7173 7119 5963 -825 -52 -958 C ATOM 1594 CD2 TYR C 295 199.256 42.012 23.457 1.00 59.02 C ANISOU 1594 CD2 TYR C 295 7732 8334 6358 -753 -87 -794 C ATOM 1595 CE1 TYR C 295 199.477 43.982 21.528 1.00 58.09 C ANISOU 1595 CE1 TYR C 295 7767 7750 6554 -914 -109 -967 C ATOM 1596 CE2 TYR C 295 200.483 42.262 22.855 1.00 61.57 C ANISOU 1596 CE2 TYR C 295 8044 8686 6664 -846 -150 -808 C ATOM 1597 CZ TYR C 295 200.588 43.249 21.894 1.00 61.94 C ANISOU 1597 CZ TYR C 295 8169 8497 6869 -927 -160 -897 C ATOM 1598 OH TYR C 295 201.806 43.503 21.297 1.00 66.36 O ANISOU 1598 OH TYR C 295 8713 9080 7420 -1016 -215 -903 O ATOM 1599 N GLU C 296 196.148 39.479 24.095 1.00 32.44 N ANISOU 1599 N GLU C 296 4326 4855 3147 -363 58 -410 N ATOM 1600 CA GLU C 296 196.570 38.099 24.394 1.00 33.11 C ANISOU 1600 CA GLU C 296 4310 5125 3146 -271 59 -208 C ATOM 1601 C GLU C 296 196.011 37.056 23.418 1.00 34.02 C ANISOU 1601 C GLU C 296 4424 5049 3454 -170 59 -30 C ATOM 1602 O GLU C 296 196.704 36.105 23.002 1.00 31.74 O ANISOU 1602 O GLU C 296 4078 4821 3160 -137 30 118 O ATOM 1603 CB GLU C 296 196.173 37.734 25.850 1.00 35.63 C ANISOU 1603 CB GLU C 296 4552 5676 3309 -197 135 -182 C ATOM 1604 N GLU C 297 194.753 37.228 23.041 1.00 31.72 N ANISOU 1604 N GLU C 297 4190 4524 3338 -122 94 -50 N ATOM 1605 CA GLU C 297 194.163 36.355 22.032 1.00 30.87 C ANISOU 1605 CA GLU C 297 4082 4221 3428 -37 86 81 C ATOM 1606 C GLU C 297 194.740 36.615 20.634 1.00 27.24 C ANISOU 1606 C GLU C 297 3677 3616 3056 -97 1 64 C ATOM 1607 O GLU C 297 194.980 35.680 19.856 1.00 27.74 O ANISOU 1607 O GLU C 297 3707 3636 3198 -48 -28 187 O ATOM 1608 CB GLU C 297 192.642 36.501 22.050 1.00 30.10 C ANISOU 1608 CB GLU C 297 4019 3930 3489 30 143 56 C ATOM 1609 CG GLU C 297 192.070 36.137 23.432 1.00 29.22 C ANISOU 1609 CG GLU C 297 3843 3968 3290 104 237 96 C ATOM 1610 CD GLU C 297 190.560 36.305 23.551 1.00 37.74 C ANISOU 1610 CD GLU C 297 4952 4865 4523 171 302 71 C ATOM 1611 OE1 GLU C 297 189.953 37.136 22.833 1.00 35.14 O ANISOU 1611 OE1 GLU C 297 4708 4320 4323 135 279 -33 O ATOM 1612 OE2 GLU C 297 189.977 35.617 24.409 1.00 40.68 O ANISOU 1612 OE2 GLU C 297 5254 5317 4884 266 384 166 O ATOM 1613 N ALA C 298 194.962 37.882 20.308 1.00 27.45 N ANISOU 1613 N ALA C 298 3785 3566 3079 -197 -30 -86 N ATOM 1614 CA ALA C 298 195.575 38.219 19.037 1.00 26.66 C ANISOU 1614 CA ALA C 298 3735 3347 3047 -251 -101 -95 C ATOM 1615 C ALA C 298 196.944 37.558 18.934 1.00 33.99 C ANISOU 1615 C ALA C 298 4602 4452 3859 -278 -147 -7 C ATOM 1616 O ALA C 298 197.274 36.970 17.897 1.00 29.79 O ANISOU 1616 O ALA C 298 4068 3850 3402 -251 -192 84 O ATOM 1617 CB ALA C 298 195.706 39.728 18.882 1.00 28.73 C ANISOU 1617 CB ALA C 298 4079 3521 3318 -359 -108 -263 C ATOM 1618 N ALA C 299 197.746 37.676 20.002 1.00 27.61 N ANISOU 1618 N ALA C 299 3743 3884 2864 -329 -137 -40 N ATOM 1619 CA ALA C 299 199.069 37.055 20.045 1.00 27.69 C ANISOU 1619 CA ALA C 299 3681 4090 2749 -352 -177 49 C ATOM 1620 C ALA C 299 198.963 35.540 19.900 1.00 27.01 C ANISOU 1620 C ALA C 299 3519 4037 2709 -234 -157 248 C ATOM 1621 O ALA C 299 199.729 34.938 19.139 1.00 26.35 O ANISOU 1621 O ALA C 299 3410 3955 2646 -231 -198 342 O ATOM 1622 CB ALA C 299 199.813 37.433 21.360 1.00 31.39 C ANISOU 1622 CB ALA C 299 4090 4840 2995 -416 -166 -27 C ATOM 1623 N MET C 300 198.009 34.906 20.588 1.00 27.24 N ANISOU 1623 N MET C 300 3504 4075 2769 -136 -88 314 N ATOM 1624 CA MET C 300 197.824 33.461 20.397 1.00 27.04 C ANISOU 1624 CA MET C 300 3400 4043 2832 -22 -53 501 C ATOM 1625 C MET C 300 197.515 33.079 18.926 1.00 28.17 C ANISOU 1625 C MET C 300 3582 3945 3176 4 -93 532 C ATOM 1626 O MET C 300 198.069 32.101 18.389 1.00 27.36 O ANISOU 1626 O MET C 300 3424 3856 3116 43 -103 652 O ATOM 1627 CB MET C 300 196.744 32.897 21.345 1.00 27.22 C ANISOU 1627 CB MET C 300 3368 4089 2887 82 41 568 C ATOM 1628 CG MET C 300 197.306 32.703 22.783 1.00 44.82 C ANISOU 1628 CG MET C 300 5507 6628 4894 98 88 621 C ATOM 1629 SD MET C 300 196.029 32.316 23.990 1.00 79.39 S ANISOU 1629 SD MET C 300 9833 11050 9283 216 206 679 S ATOM 1630 N ALA C 301 196.631 33.856 18.300 1.00 25.32 N ANISOU 1630 N ALA C 301 3311 3375 2934 -12 -112 421 N ATOM 1631 CA ALA C 301 196.286 33.650 16.906 1.00 24.57 C ANISOU 1631 CA ALA C 301 3255 3073 3008 12 -157 428 C ATOM 1632 C ALA C 301 197.553 33.810 16.022 1.00 29.56 C ANISOU 1632 C ALA C 301 3908 3738 3585 -55 -230 433 C ATOM 1633 O ALA C 301 197.821 32.976 15.178 1.00 26.04 O ANISOU 1633 O ALA C 301 3432 3247 3213 -14 -253 513 O ATOM 1634 CB ALA C 301 195.202 34.633 16.484 1.00 24.38 C ANISOU 1634 CB ALA C 301 3320 2852 3090 2 -165 308 C ATOM 1635 N ILE C 302 198.327 34.867 16.248 1.00 25.95 N ANISOU 1635 N ILE C 302 3496 3360 3004 -158 -259 342 N ATOM 1636 CA ILE C 302 199.511 35.157 15.425 1.00 25.86 C ANISOU 1636 CA ILE C 302 3507 3370 2947 -228 -322 342 C ATOM 1637 C ILE C 302 200.552 34.048 15.565 1.00 26.55 C ANISOU 1637 C ILE C 302 3504 3626 2959 -205 -325 476 C ATOM 1638 O ILE C 302 201.089 33.543 14.569 1.00 29.90 O ANISOU 1638 O ILE C 302 3922 4006 3432 -191 -361 541 O ATOM 1639 CB ILE C 302 200.111 36.549 15.807 1.00 28.07 C ANISOU 1639 CB ILE C 302 3838 3703 3124 -350 -338 206 C ATOM 1640 CG1 ILE C 302 199.199 37.686 15.327 1.00 27.94 C ANISOU 1640 CG1 ILE C 302 3917 3479 3221 -372 -333 88 C ATOM 1641 CG2 ILE C 302 201.578 36.753 15.284 1.00 24.43 C ANISOU 1641 CG2 ILE C 302 3371 3327 2585 -430 -391 221 C ATOM 1642 CD1 ILE C 302 199.439 38.998 16.096 1.00 29.68 C ANISOU 1642 CD1 ILE C 302 4171 3742 3364 -480 -313 -65 C ATOM 1643 N ALA C 303 200.826 33.635 16.803 1.00 25.94 N ANISOU 1643 N ALA C 303 3348 3749 2759 -193 -282 526 N ATOM 1644 CA ALA C 303 201.858 32.626 17.027 1.00 24.94 C ANISOU 1644 CA ALA C 303 3124 3799 2551 -168 -276 667 C ATOM 1645 C ALA C 303 201.407 31.243 16.539 1.00 29.45 C ANISOU 1645 C ALA C 303 3637 4281 3271 -54 -238 808 C ATOM 1646 O ALA C 303 202.232 30.392 16.181 1.00 28.41 O ANISOU 1646 O ALA C 303 3444 4211 3139 -30 -240 922 O ATOM 1647 CB ALA C 303 202.215 32.563 18.540 1.00 25.80 C ANISOU 1647 CB ALA C 303 3154 4172 2478 -172 -235 694 C ATOM 1648 N SER C 304 200.098 30.993 16.571 1.00 27.89 N ANISOU 1648 N SER C 304 3447 3939 3209 18 -195 797 N ATOM 1649 CA SER C 304 199.585 29.678 16.203 1.00 29.69 C ANISOU 1649 CA SER C 304 3605 4074 3600 124 -147 913 C ATOM 1650 C SER C 304 199.409 29.553 14.677 1.00 30.58 C ANISOU 1650 C SER C 304 3767 3989 3862 129 -203 872 C ATOM 1651 O SER C 304 199.581 28.470 14.112 1.00 32.12 O ANISOU 1651 O SER C 304 3900 4143 4162 187 -186 958 O ATOM 1652 CB SER C 304 198.245 29.420 16.909 1.00 31.62 C ANISOU 1652 CB SER C 304 3823 4252 3938 201 -72 920 C ATOM 1653 OG SER C 304 198.437 29.570 18.322 1.00 39.39 O ANISOU 1653 OG SER C 304 4761 5444 4760 202 -20 956 O ATOM 1654 N LEU C 305 199.057 30.655 14.020 1.00 21.86 N ANISOU 1654 N LEU C 305 2768 2767 2771 75 -263 741 N ATOM 1655 CA LEU C 305 198.753 30.598 12.575 1.00 23.46 C ANISOU 1655 CA LEU C 305 3014 2796 3104 94 -317 699 C ATOM 1656 C LEU C 305 199.913 30.959 11.650 1.00 28.08 C ANISOU 1656 C LEU C 305 3640 3411 3618 34 -384 692 C ATOM 1657 O LEU C 305 199.874 30.643 10.461 1.00 25.79 O ANISOU 1657 O LEU C 305 3361 3022 3415 65 -422 686 O ATOM 1658 CB LEU C 305 197.584 31.513 12.228 1.00 26.06 C ANISOU 1658 CB LEU C 305 3425 2966 3511 94 -338 583 C ATOM 1659 CG LEU C 305 196.238 31.070 12.844 1.00 30.50 C ANISOU 1659 CG LEU C 305 3947 3451 4191 169 -276 585 C ATOM 1660 CD1 LEU C 305 195.210 32.174 12.698 1.00 27.96 C ANISOU 1660 CD1 LEU C 305 3709 3000 3915 155 -292 472 C ATOM 1661 CD2 LEU C 305 195.699 29.790 12.193 1.00 29.96 C ANISOU 1661 CD2 LEU C 305 3802 3282 4299 258 -259 637 C ATOM 1662 N ASN C 306 200.895 31.692 12.155 1.00 28.91 N ANISOU 1662 N ASN C 306 3991 3400 3595 -184 -469 507 N ATOM 1663 CA ASN C 306 202.038 32.050 11.307 1.00 29.06 C ANISOU 1663 CA ASN C 306 3943 3484 3615 -22 -407 424 C ATOM 1664 C ASN C 306 202.755 30.779 10.922 1.00 27.46 C ANISOU 1664 C ASN C 306 3892 3122 3421 135 -435 371 C ATOM 1665 O ASN C 306 202.984 29.930 11.766 1.00 25.89 O ANISOU 1665 O ASN C 306 3786 2804 3247 184 -486 428 O ATOM 1666 CB ASN C 306 203.005 32.965 12.053 1.00 29.36 C ANISOU 1666 CB ASN C 306 3809 3675 3670 47 -371 466 C ATOM 1667 CG ASN C 306 204.149 33.457 11.161 1.00 29.58 C ANISOU 1667 CG ASN C 306 3738 3816 3686 182 -305 400 C ATOM 1668 OD1 ASN C 306 203.929 33.879 10.015 1.00 25.79 O ANISOU 1668 OD1 ASN C 306 3240 3380 3179 166 -259 338 O ATOM 1669 ND2 ASN C 306 205.364 33.412 11.691 1.00 27.44 N ANISOU 1669 ND2 ASN C 306 3387 3618 3421 311 -300 422 N ATOM 1670 N GLY C 307 203.093 30.634 9.638 1.00 30.20 N ANISOU 1670 N GLY C 307 4271 3467 3737 228 -399 263 N ATOM 1671 CA GLY C 307 203.836 29.475 9.175 1.00 29.21 C ANISOU 1671 CA GLY C 307 4297 3196 3603 417 -417 193 C ATOM 1672 C GLY C 307 202.914 28.323 8.852 1.00 35.14 C ANISOU 1672 C GLY C 307 5296 3708 4348 325 -484 149 C ATOM 1673 O GLY C 307 203.358 27.263 8.419 1.00 34.61 O ANISOU 1673 O GLY C 307 5411 3469 4270 469 -507 75 O ATOM 1674 N TYR C 308 201.611 28.535 9.053 1.00 33.11 N ANISOU 1674 N TYR C 308 5049 3445 4086 81 -516 192 N ATOM 1675 CA TYR C 308 200.630 27.479 8.807 1.00 38.39 C ANISOU 1675 CA TYR C 308 5942 3905 4738 -65 -589 164 C ATOM 1676 C TYR C 308 200.341 27.267 7.318 1.00 35.94 C ANISOU 1676 C TYR C 308 5712 3577 4366 -74 -575 15 C ATOM 1677 O TYR C 308 200.158 28.219 6.573 1.00 35.04 O ANISOU 1677 O TYR C 308 5440 3663 4212 -100 -515 -21 O ATOM 1678 CB TYR C 308 199.319 27.766 9.542 1.00 44.96 C ANISOU 1678 CB TYR C 308 6733 4787 5563 -330 -630 274 C ATOM 1679 CG TYR C 308 198.344 26.620 9.433 1.00 52.16 C ANISOU 1679 CG TYR C 308 7871 5493 6453 -514 -716 269 C ATOM 1680 CD1 TYR C 308 198.474 25.503 10.243 1.00 57.95 C ANISOU 1680 CD1 TYR C 308 8797 5991 7231 -514 -786 335 C ATOM 1681 CD2 TYR C 308 197.308 26.645 8.505 1.00 55.75 C ANISOU 1681 CD2 TYR C 308 8351 5993 6838 -697 -728 203 C ATOM 1682 CE1 TYR C 308 197.597 24.440 10.150 1.00 63.43 C ANISOU 1682 CE1 TYR C 308 9718 6477 7906 -710 -871 336 C ATOM 1683 CE2 TYR C 308 196.425 25.584 8.399 1.00 61.38 C ANISOU 1683 CE2 TYR C 308 9274 6525 7522 -899 -814 196 C ATOM 1684 CZ TYR C 308 196.573 24.485 9.229 1.00 65.95 C ANISOU 1684 CZ TYR C 308 10058 6848 8153 -915 -887 263 C ATOM 1685 OH TYR C 308 195.701 23.420 9.142 1.00 71.55 O ANISOU 1685 OH TYR C 308 10994 7357 8835 -1145 -978 264 O ATOM 1686 N ARG C 309 200.295 26.013 6.889 1.00 37.66 N ANISOU 1686 N ARG C 309 6187 3551 4573 -52 -631 -70 N ATOM 1687 CA ARG C 309 200.094 25.719 5.475 1.00 45.12 C ANISOU 1687 CA ARG C 309 7225 4472 5446 -46 -624 -231 C ATOM 1688 C ARG C 309 198.610 25.732 5.074 1.00 48.56 C ANISOU 1688 C ARG C 309 7690 4936 5825 -350 -666 -240 C ATOM 1689 O ARG C 309 197.868 24.825 5.442 1.00 53.36 O ANISOU 1689 O ARG C 309 8492 5349 6436 -530 -751 -217 O ATOM 1690 CB ARG C 309 200.721 24.368 5.121 1.00 50.40 C ANISOU 1690 CB ARG C 309 8181 4858 6113 126 -666 -343 C ATOM 1691 N LEU C 310 198.196 26.760 4.324 1.00 44.49 N ANISOU 1691 N LEU C 310 6978 4677 5251 -407 -607 -263 N ATOM 1692 CA LEU C 310 196.826 26.899 3.822 1.00 43.77 C ANISOU 1692 CA LEU C 310 6868 4684 5079 -668 -634 -270 C ATOM 1693 C LEU C 310 196.792 26.747 2.297 1.00 47.63 C ANISOU 1693 C LEU C 310 7400 5221 5475 -632 -614 -439 C ATOM 1694 O LEU C 310 197.410 27.529 1.572 1.00 44.19 O ANISOU 1694 O LEU C 310 6809 4966 5016 -467 -531 -483 O ATOM 1695 CB LEU C 310 196.241 28.267 4.199 1.00 41.07 C ANISOU 1695 CB LEU C 310 6258 4623 4722 -756 -579 -144 C ATOM 1696 CG LEU C 310 194.890 28.603 3.548 1.00 44.67 C ANISOU 1696 CG LEU C 310 6643 5260 5070 -976 -586 -143 C ATOM 1697 CD1 LEU C 310 193.767 27.724 4.112 1.00 45.00 C ANISOU 1697 CD1 LEU C 310 6819 5197 5081 -1247 -689 -87 C ATOM 1698 CD2 LEU C 310 194.541 30.082 3.709 1.00 46.02 C ANISOU 1698 CD2 LEU C 310 6553 5715 5217 -973 -507 -38 C ATOM 1699 N GLY C 311 196.053 25.758 1.808 1.00 53.31 N ANISOU 1699 N GLY C 311 8326 5794 6135 -801 -692 -531 N ATOM 1700 CA GLY C 311 196.153 25.388 0.409 1.00 56.62 C ANISOU 1700 CA GLY C 311 8834 6216 6464 -745 -686 -719 C ATOM 1701 C GLY C 311 197.574 24.902 0.189 1.00 58.39 C ANISOU 1701 C GLY C 311 9172 6284 6729 -423 -658 -819 C ATOM 1702 O GLY C 311 198.059 24.025 0.901 1.00 59.21 O ANISOU 1702 O GLY C 311 9476 6119 6903 -346 -707 -808 O ATOM 1703 N ASP C 312 198.269 25.484 -0.776 1.00 60.11 N ANISOU 1703 N ASP C 312 9253 6689 6895 -222 -577 -902 N ATOM 1704 CA ASP C 312 199.652 25.086 -1.011 1.00 58.61 C ANISOU 1704 CA ASP C 312 9135 6412 6722 105 -543 -988 C ATOM 1705 C ASP C 312 200.640 26.184 -0.608 1.00 52.67 C ANISOU 1705 C ASP C 312 8112 5877 6022 293 -450 -872 C ATOM 1706 O ASP C 312 201.800 26.149 -1.007 1.00 55.99 O ANISOU 1706 O ASP C 312 8502 6347 6425 566 -401 -930 O ATOM 1707 CB ASP C 312 199.856 24.679 -2.477 1.00 61.40 C ANISOU 1707 CB ASP C 312 9575 6796 6957 221 -530 -1194 C ATOM 1708 N LYS C 313 200.183 27.142 0.201 1.00 45.86 N ANISOU 1708 N LYS C 313 7059 5151 5214 146 -430 -708 N ATOM 1709 CA LYS C 313 201.030 28.258 0.611 1.00 38.71 C ANISOU 1709 CA LYS C 313 5908 4446 4355 276 -348 -600 C ATOM 1710 C LYS C 313 201.226 28.332 2.113 1.00 36.65 C ANISOU 1710 C LYS C 313 5628 4100 4196 251 -373 -456 C ATOM 1711 O LYS C 313 200.379 27.884 2.875 1.00 41.65 O ANISOU 1711 O LYS C 313 6371 4593 4862 70 -442 -397 O ATOM 1712 CB LYS C 313 200.452 29.581 0.118 1.00 39.93 C ANISOU 1712 CB LYS C 313 5828 4874 4469 161 -282 -541 C ATOM 1713 CG LYS C 313 200.394 29.696 -1.412 1.00 42.26 C ANISOU 1713 CG LYS C 313 6087 5319 4653 213 -241 -664 C ATOM 1714 CD LYS C 313 199.506 30.858 -1.818 1.00 44.69 C ANISOU 1714 CD LYS C 313 6204 5862 4913 61 -191 -587 C ATOM 1715 N ILE C 314 202.341 28.924 2.520 1.00 32.56 N ANISOU 1715 N ILE C 314 4958 3698 3716 423 -318 -396 N ATOM 1716 CA ILE C 314 202.656 29.141 3.924 1.00 32.16 C ANISOU 1716 CA ILE C 314 4852 3621 3749 416 -332 -262 C ATOM 1717 C ILE C 314 202.226 30.539 4.336 1.00 32.04 C ANISOU 1717 C ILE C 314 4616 3805 3752 273 -287 -151 C ATOM 1718 O ILE C 314 202.765 31.561 3.869 1.00 31.87 O ANISOU 1718 O ILE C 314 4411 3985 3713 334 -212 -141 O ATOM 1719 CB ILE C 314 204.158 28.974 4.158 1.00 37.07 C ANISOU 1719 CB ILE C 314 5426 4275 4382 682 -302 -261 C ATOM 1720 CG1 ILE C 314 204.588 27.557 3.755 1.00 41.69 C ANISOU 1720 CG1 ILE C 314 6257 4645 4939 866 -343 -374 C ATOM 1721 CG2 ILE C 314 204.514 29.276 5.619 1.00 35.10 C ANISOU 1721 CG2 ILE C 314 5092 4038 4206 669 -315 -122 C ATOM 1722 CD1 ILE C 314 206.084 27.376 3.664 1.00 46.26 C ANISOU 1722 CD1 ILE C 314 6776 5311 5490 1176 -301 -394 C ATOM 1723 N LEU C 315 201.229 30.591 5.217 1.00 30.45 N ANISOU 1723 N LEU C 315 4440 3548 3581 81 -334 -65 N ATOM 1724 CA LEU C 315 200.738 31.865 5.707 1.00 26.74 C ANISOU 1724 CA LEU C 315 3793 3247 3122 -38 -296 36 C ATOM 1725 C LEU C 315 201.795 32.650 6.422 1.00 25.46 C ANISOU 1725 C LEU C 315 3481 3185 3007 65 -253 101 C ATOM 1726 O LEU C 315 202.575 32.091 7.180 1.00 28.77 O ANISOU 1726 O LEU C 315 3940 3527 3467 167 -282 123 O ATOM 1727 CB LEU C 315 199.610 31.624 6.704 1.00 28.72 C ANISOU 1727 CB LEU C 315 4101 3427 3386 -228 -360 124 C ATOM 1728 CG LEU C 315 198.350 31.021 6.111 1.00 38.35 C ANISOU 1728 CG LEU C 315 5434 4594 4542 -399 -408 86 C ATOM 1729 CD1 LEU C 315 197.338 30.829 7.249 1.00 41.26 C ANISOU 1729 CD1 LEU C 315 5828 4932 4917 -585 -471 201 C ATOM 1730 CD2 LEU C 315 197.785 31.920 5.007 1.00 40.46 C ANISOU 1730 CD2 LEU C 315 5581 5059 4734 -444 -346 52 C ATOM 1731 N GLN C 316 201.792 33.959 6.229 1.00 25.57 N ANISOU 1731 N GLN C 316 3331 3373 3012 30 -187 138 N ATOM 1732 CA GLN C 316 202.543 34.835 7.117 1.00 26.36 C ANISOU 1732 CA GLN C 316 3298 3563 3155 56 -159 212 C ATOM 1733 C GLN C 316 201.561 35.665 7.940 1.00 29.08 C ANISOU 1733 C GLN C 316 3598 3944 3508 -98 -164 294 C ATOM 1734 O GLN C 316 200.727 36.382 7.387 1.00 27.17 O ANISOU 1734 O GLN C 316 3320 3777 3227 -178 -128 303 O ATOM 1735 CB GLN C 316 203.483 35.724 6.311 1.00 29.37 C ANISOU 1735 CB GLN C 316 3538 4103 3516 141 -81 193 C ATOM 1736 CG GLN C 316 204.390 34.929 5.380 1.00 27.67 C ANISOU 1736 CG GLN C 316 3353 3895 3267 314 -70 107 C ATOM 1737 CD GLN C 316 205.042 35.816 4.331 1.00 30.98 C ANISOU 1737 CD GLN C 316 3626 4501 3643 368 11 95 C ATOM 1738 OE1 GLN C 316 205.063 37.038 4.483 1.00 34.70 O ANISOU 1738 OE1 GLN C 316 3978 5080 4128 281 57 163 O ATOM 1739 NE2 GLN C 316 205.567 35.209 3.262 1.00 28.33 N ANISOU 1739 NE2 GLN C 316 3309 4205 3249 512 30 11 N ATOM 1740 N VAL C 317 201.625 35.531 9.261 1.00 26.72 N ANISOU 1740 N VAL C 317 3303 3603 3246 -125 -208 358 N ATOM 1741 CA VAL C 317 200.662 36.211 10.126 1.00 28.26 C ANISOU 1741 CA VAL C 317 3464 3839 3433 -251 -219 431 C ATOM 1742 C VAL C 317 201.420 37.030 11.148 1.00 27.73 C ANISOU 1742 C VAL C 317 3296 3840 3398 -230 -205 474 C ATOM 1743 O VAL C 317 202.379 36.532 11.758 1.00 25.14 O ANISOU 1743 O VAL C 317 2960 3490 3101 -153 -232 480 O ATOM 1744 CB VAL C 317 199.720 35.202 10.843 1.00 23.10 C ANISOU 1744 CB VAL C 317 2920 3085 2773 -341 -298 476 C ATOM 1745 CG1 VAL C 317 198.681 35.947 11.721 1.00 23.07 C ANISOU 1745 CG1 VAL C 317 2859 3169 2737 -456 -305 557 C ATOM 1746 CG2 VAL C 317 199.024 34.283 9.812 1.00 25.03 C ANISOU 1746 CG2 VAL C 317 3283 3247 2978 -389 -324 421 C ATOM 1747 N SER C 318 201.015 38.283 11.342 1.00 26.19 N ANISOU 1747 N SER C 318 3032 3731 3188 -293 -163 501 N ATOM 1748 CA SER C 318 201.782 39.138 12.272 1.00 30.05 C ANISOU 1748 CA SER C 318 3437 4279 3700 -291 -152 523 C ATOM 1749 C SER C 318 200.960 40.352 12.656 1.00 30.75 C ANISOU 1749 C SER C 318 3505 4417 3760 -366 -123 552 C ATOM 1750 O SER C 318 199.976 40.637 11.988 1.00 27.69 O ANISOU 1750 O SER C 318 3144 4044 3334 -394 -95 559 O ATOM 1751 CB SER C 318 203.069 39.598 11.596 1.00 31.24 C ANISOU 1751 CB SER C 318 3510 4491 3868 -229 -103 487 C ATOM 1752 OG SER C 318 202.767 40.253 10.368 1.00 33.53 O ANISOU 1752 OG SER C 318 3790 4814 4135 -240 -38 467 O ATOM 1753 N PHE C 319 201.325 41.056 13.735 1.00 28.21 N ANISOU 1753 N PHE C 319 3141 4130 3446 -390 -130 567 N ATOM 1754 CA PHE C 319 200.662 42.331 14.039 1.00 30.30 C ANISOU 1754 CA PHE C 319 3408 4426 3678 -435 -95 578 C ATOM 1755 C PHE C 319 200.931 43.290 12.882 1.00 32.70 C ANISOU 1755 C PHE C 319 3701 4736 3986 -431 -17 558 C ATOM 1756 O PHE C 319 202.052 43.338 12.357 1.00 33.99 O ANISOU 1756 O PHE C 319 3818 4914 4184 -418 4 534 O ATOM 1757 CB PHE C 319 201.194 42.976 15.333 1.00 34.10 C ANISOU 1757 CB PHE C 319 3856 4936 4163 -463 -116 574 C ATOM 1758 CG PHE C 319 200.706 42.348 16.608 1.00 36.03 C ANISOU 1758 CG PHE C 319 4104 5203 4382 -469 -183 610 C ATOM 1759 CD1 PHE C 319 199.358 42.405 16.972 1.00 37.68 C ANISOU 1759 CD1 PHE C 319 4347 5438 4531 -484 -194 650 C ATOM 1760 CD2 PHE C 319 201.607 41.779 17.498 1.00 37.97 C ANISOU 1760 CD2 PHE C 319 4303 5474 4649 -457 -234 616 C ATOM 1761 CE1 PHE C 319 198.925 41.862 18.173 1.00 40.64 C ANISOU 1761 CE1 PHE C 319 4710 5859 4873 -496 -255 697 C ATOM 1762 CE2 PHE C 319 201.168 41.231 18.702 1.00 37.82 C ANISOU 1762 CE2 PHE C 319 4281 5490 4601 -463 -294 663 C ATOM 1763 CZ PHE C 319 199.836 41.273 19.040 1.00 40.20 C ANISOU 1763 CZ PHE C 319 4615 5812 4846 -488 -306 705 C ATOM 1764 N LYS C 320 199.897 44.024 12.465 1.00 37.54 N ANISOU 1764 N LYS C 320 4351 5357 4555 -436 27 579 N ATOM 1765 CA LYS C 320 200.020 44.977 11.353 1.00 37.77 C ANISOU 1765 CA LYS C 320 4381 5390 4581 -427 105 580 C ATOM 1766 C LYS C 320 201.093 46.020 11.651 1.00 41.55 C ANISOU 1766 C LYS C 320 4845 5845 5097 -469 132 565 C ATOM 1767 O LYS C 320 201.202 46.517 12.776 1.00 41.55 O ANISOU 1767 O LYS C 320 4865 5825 5098 -504 106 553 O ATOM 1768 CB LYS C 320 198.690 45.699 11.066 1.00 35.10 C ANISOU 1768 CB LYS C 320 4089 5073 4175 -403 149 619 C ATOM 1769 CG LYS C 320 198.717 46.577 9.786 1.00 35.43 C ANISOU 1769 CG LYS C 320 4135 5121 4204 -378 234 640 C ATOM 1770 CD LYS C 320 197.458 47.406 9.607 1.00 35.04 C ANISOU 1770 CD LYS C 320 4133 5102 4077 -327 283 691 C ATOM 1771 CE LYS C 320 197.441 48.158 8.248 1.00 41.95 C ANISOU 1771 CE LYS C 320 5010 5996 4934 -290 368 730 C ATOM 1772 NZ LYS C 320 198.602 49.118 8.156 1.00 42.55 N ANISOU 1772 NZ LYS C 320 5108 5985 5075 -332 407 727 N ATOM 1773 N THR C 321 201.864 46.348 10.621 1.00 43.62 N ANISOU 1773 N THR C 321 5070 6125 5380 -475 180 566 N ATOM 1774 CA THR C 321 202.864 47.398 10.679 1.00 46.31 C ANISOU 1774 CA THR C 321 5395 6454 5747 -547 211 566 C ATOM 1775 C THR C 321 202.219 48.760 10.448 1.00 46.55 C ANISOU 1775 C THR C 321 5517 6413 5758 -565 273 597 C ATOM 1776 O THR C 321 201.354 48.896 9.578 1.00 49.37 O ANISOU 1776 O THR C 321 5904 6775 6081 -504 320 634 O ATOM 1777 CB THR C 321 203.926 47.154 9.607 1.00 47.60 C ANISOU 1777 CB THR C 321 5468 6693 5926 -545 240 572 C ATOM 1778 OG1 THR C 321 203.314 47.176 8.312 1.00 46.79 O ANISOU 1778 OG1 THR C 321 5375 6608 5795 -490 296 599 O ATOM 1779 CG2 THR C 321 204.552 45.792 9.819 1.00 50.63 C ANISOU 1779 CG2 THR C 321 5781 7139 6319 -488 184 540 C TER 1780 THR C 321 ATOM 1781 N SER D 242 181.646 19.660 19.697 1.00 70.71 N ANISOU 1781 N SER D 242 8347 8727 9792 -1024 -12 -1595 N ATOM 1782 CA SER D 242 182.270 20.477 20.737 1.00 68.66 C ANISOU 1782 CA SER D 242 8321 8336 9433 -1114 23 -1390 C ATOM 1783 C SER D 242 181.876 21.947 20.584 1.00 68.13 C ANISOU 1783 C SER D 242 8395 8350 9141 -1125 40 -1260 C ATOM 1784 O SER D 242 181.811 22.468 19.465 1.00 74.72 O ANISOU 1784 O SER D 242 9147 9423 9818 -1087 9 -1303 O ATOM 1785 CB SER D 242 183.792 20.338 20.689 1.00 66.03 C ANISOU 1785 CB SER D 242 8000 8055 9033 -1142 -29 -1355 C ATOM 1786 N GLY D 243 181.620 22.609 21.710 1.00 57.13 N ANISOU 1786 N GLY D 243 7221 6770 7715 -1137 88 -1077 N ATOM 1787 CA GLY D 243 181.189 23.996 21.704 1.00 49.31 C ANISOU 1787 CA GLY D 243 6380 5813 6543 -1121 99 -931 C ATOM 1788 C GLY D 243 179.695 24.161 21.956 1.00 43.92 C ANISOU 1788 C GLY D 243 5715 5059 5913 -1056 177 -912 C ATOM 1789 O GLY D 243 178.934 23.200 21.902 1.00 47.85 O ANISOU 1789 O GLY D 243 6063 5513 6604 -1027 216 -1023 O ATOM 1790 N TRP D 244 179.278 25.395 22.211 1.00 36.04 N ANISOU 1790 N TRP D 244 4881 4038 4776 -1032 195 -769 N ATOM 1791 CA TRP D 244 177.885 25.707 22.533 1.00 36.14 C ANISOU 1791 CA TRP D 244 4929 3976 4827 -962 280 -724 C ATOM 1792 C TRP D 244 177.123 26.321 21.354 1.00 32.07 C ANISOU 1792 C TRP D 244 4298 3655 4234 -923 256 -757 C ATOM 1793 O TRP D 244 177.474 27.389 20.862 1.00 35.17 O ANISOU 1793 O TRP D 244 4755 4154 4456 -929 212 -665 O ATOM 1794 CB TRP D 244 177.831 26.634 23.744 1.00 34.75 C ANISOU 1794 CB TRP D 244 5026 3623 4552 -929 318 -557 C ATOM 1795 CG TRP D 244 178.605 26.061 24.906 1.00 37.93 C ANISOU 1795 CG TRP D 244 5557 3866 4989 -934 323 -525 C ATOM 1796 CD1 TRP D 244 179.913 26.334 25.250 1.00 38.84 C ANISOU 1796 CD1 TRP D 244 5786 3949 5022 -986 219 -499 C ATOM 1797 CD2 TRP D 244 178.137 25.102 25.851 1.00 39.60 C ANISOU 1797 CD2 TRP D 244 5776 3933 5338 -875 433 -500 C ATOM 1798 NE1 TRP D 244 180.272 25.601 26.354 1.00 41.65 N ANISOU 1798 NE1 TRP D 244 6235 4163 5427 -953 244 -477 N ATOM 1799 CE2 TRP D 244 179.188 24.836 26.754 1.00 42.34 C ANISOU 1799 CE2 TRP D 244 6263 4182 5642 -879 389 -459 C ATOM 1800 CE3 TRP D 244 176.910 24.445 26.044 1.00 43.18 C ANISOU 1800 CE3 TRP D 244 6116 4320 5970 -812 572 -487 C ATOM 1801 CZ2 TRP D 244 179.069 23.947 27.820 1.00 45.59 C ANISOU 1801 CZ2 TRP D 244 6720 4456 6145 -808 486 -391 C ATOM 1802 CZ3 TRP D 244 176.784 23.560 27.105 1.00 45.54 C ANISOU 1802 CZ3 TRP D 244 6443 4463 6399 -752 686 -403 C ATOM 1803 CH2 TRP D 244 177.859 23.313 27.975 1.00 45.73 C ANISOU 1803 CH2 TRP D 244 6621 4414 6340 -744 647 -348 C ATOM 1804 N CYS D 245 176.054 25.655 20.964 1.00 29.69 N ANISOU 1804 N CYS D 245 3819 3379 4084 -876 282 -874 N ATOM 1805 CA CYS D 245 175.255 26.044 19.810 1.00 30.00 C ANISOU 1805 CA CYS D 245 3719 3617 4064 -816 236 -943 C ATOM 1806 C CYS D 245 174.106 26.988 20.171 1.00 31.47 C ANISOU 1806 C CYS D 245 4002 3725 4230 -757 304 -811 C ATOM 1807 O CYS D 245 173.257 26.681 21.033 1.00 35.52 O ANISOU 1807 O CYS D 245 4534 4048 4913 -729 404 -775 O ATOM 1808 CB CYS D 245 174.709 24.793 19.147 1.00 29.92 C ANISOU 1808 CB CYS D 245 3437 3667 4265 -786 186 -1184 C ATOM 1809 SG CYS D 245 173.839 25.112 17.598 1.00 40.46 S ANISOU 1809 SG CYS D 245 4575 5296 5503 -679 75 -1331 S ATOM 1810 N ILE D 246 174.083 28.128 19.492 1.00 29.69 N ANISOU 1810 N ILE D 246 3824 3649 3808 -728 263 -722 N ATOM 1811 CA ILE D 246 173.126 29.203 19.723 1.00 30.63 C ANISOU 1811 CA ILE D 246 4044 3710 3885 -669 312 -586 C ATOM 1812 C ILE D 246 172.223 29.302 18.487 1.00 31.13 C ANISOU 1812 C ILE D 246 3911 3992 3925 -588 250 -671 C ATOM 1813 O ILE D 246 172.717 29.280 17.359 1.00 29.16 O ANISOU 1813 O ILE D 246 3550 3993 3536 -567 160 -735 O ATOM 1814 CB ILE D 246 173.870 30.535 19.910 1.00 31.46 C ANISOU 1814 CB ILE D 246 4353 3792 3809 -693 295 -397 C ATOM 1815 CG1 ILE D 246 174.813 30.457 21.131 1.00 32.20 C ANISOU 1815 CG1 ILE D 246 4640 3675 3919 -757 313 -346 C ATOM 1816 CG2 ILE D 246 172.899 31.678 20.100 1.00 26.77 C ANISOU 1816 CG2 ILE D 246 3855 3130 3185 -623 336 -268 C ATOM 1817 CD1 ILE D 246 175.768 31.687 21.257 1.00 31.54 C ANISOU 1817 CD1 ILE D 246 4719 3546 3718 -798 251 -197 C ATOM 1818 N PHE D 247 170.908 29.370 18.716 1.00 28.05 N ANISOU 1818 N PHE D 247 3471 3516 3670 -525 300 -671 N ATOM 1819 CA PHE D 247 169.878 29.576 17.690 1.00 29.08 C ANISOU 1819 CA PHE D 247 3427 3822 3800 -432 230 -743 C ATOM 1820 C PHE D 247 169.548 31.084 17.605 1.00 29.19 C ANISOU 1820 C PHE D 247 3585 3861 3647 -381 253 -532 C ATOM 1821 O PHE D 247 169.429 31.776 18.644 1.00 28.60 O ANISOU 1821 O PHE D 247 3707 3571 3588 -393 352 -377 O ATOM 1822 CB PHE D 247 168.645 28.734 18.090 1.00 30.34 C ANISOU 1822 CB PHE D 247 3423 3829 4275 -402 276 -853 C ATOM 1823 CG PHE D 247 167.411 28.984 17.269 1.00 34.13 C ANISOU 1823 CG PHE D 247 3726 4428 4813 -302 203 -922 C ATOM 1824 CD1 PHE D 247 167.314 28.514 15.962 1.00 33.34 C ANISOU 1824 CD1 PHE D 247 3406 4587 4675 -238 28 -1140 C ATOM 1825 CD2 PHE D 247 166.311 29.626 17.829 1.00 32.99 C ANISOU 1825 CD2 PHE D 247 3624 4140 4772 -251 303 -788 C ATOM 1826 CE1 PHE D 247 166.130 28.703 15.217 1.00 35.42 C ANISOU 1826 CE1 PHE D 247 3494 4963 5003 -128 -69 -1226 C ATOM 1827 CE2 PHE D 247 165.143 29.833 17.090 1.00 36.95 C ANISOU 1827 CE2 PHE D 247 3944 4742 5355 -156 226 -853 C ATOM 1828 CZ PHE D 247 165.059 29.366 15.786 1.00 36.21 C ANISOU 1828 CZ PHE D 247 3630 4904 5225 -97 30 -1075 C ATOM 1829 N ILE D 248 169.466 31.614 16.385 1.00 30.17 N ANISOU 1829 N ILE D 248 3617 4248 3599 -307 159 -523 N ATOM 1830 CA ILE D 248 169.034 32.993 16.180 1.00 30.64 C ANISOU 1830 CA ILE D 248 3770 4333 3540 -245 173 -317 C ATOM 1831 C ILE D 248 167.841 32.998 15.235 1.00 36.35 C ANISOU 1831 C ILE D 248 4299 5239 4272 -119 94 -402 C ATOM 1832 O ILE D 248 167.918 32.422 14.147 1.00 33.99 O ANISOU 1832 O ILE D 248 3822 5208 3884 -53 -24 -562 O ATOM 1833 CB ILE D 248 170.103 33.870 15.520 1.00 34.00 C ANISOU 1833 CB ILE D 248 4267 4921 3733 -252 142 -143 C ATOM 1834 CG1 ILE D 248 171.406 33.831 16.319 1.00 34.42 C ANISOU 1834 CG1 ILE D 248 4475 4811 3790 -378 182 -82 C ATOM 1835 CG2 ILE D 248 169.599 35.309 15.342 1.00 31.76 C ANISOU 1835 CG2 ILE D 248 4064 4624 3381 -186 160 90 C ATOM 1836 CD1 ILE D 248 172.264 32.639 15.984 1.00 37.92 C ANISOU 1836 CD1 ILE D 248 4809 5380 4219 -424 141 -256 C ATOM 1837 N TYR D 249 166.760 33.663 15.637 1.00 32.49 N ANISOU 1837 N TYR D 249 3844 4617 3883 -67 147 -307 N ATOM 1838 CA TYR D 249 165.573 33.820 14.794 1.00 34.08 C ANISOU 1838 CA TYR D 249 3868 4974 4108 61 63 -363 C ATOM 1839 C TYR D 249 165.298 35.302 14.518 1.00 34.68 C ANISOU 1839 C TYR D 249 4048 5090 4038 135 78 -114 C ATOM 1840 O TYR D 249 165.561 36.169 15.362 1.00 37.53 O ANISOU 1840 O TYR D 249 4616 5238 4407 86 181 75 O ATOM 1841 CB TYR D 249 164.350 33.130 15.412 1.00 37.23 C ANISOU 1841 CB TYR D 249 4139 5179 4826 72 107 -489 C ATOM 1842 CG TYR D 249 163.131 33.181 14.512 1.00 41.90 C ANISOU 1842 CG TYR D 249 4510 5926 5484 202 -14 -584 C ATOM 1843 CD1 TYR D 249 162.834 32.125 13.643 1.00 43.29 C ANISOU 1843 CD1 TYR D 249 4424 6274 5749 253 -183 -867 C ATOM 1844 CD2 TYR D 249 162.293 34.291 14.508 1.00 43.65 C ANISOU 1844 CD2 TYR D 249 4777 6120 5688 286 19 -410 C ATOM 1845 CE1 TYR D 249 161.727 32.175 12.798 1.00 45.87 C ANISOU 1845 CE1 TYR D 249 4540 6750 6138 388 -332 -981 C ATOM 1846 CE2 TYR D 249 161.175 34.345 13.671 1.00 48.62 C ANISOU 1846 CE2 TYR D 249 5195 6897 6380 414 -109 -498 C ATOM 1847 CZ TYR D 249 160.906 33.288 12.819 1.00 49.84 C ANISOU 1847 CZ TYR D 249 5092 7230 6613 466 -292 -786 C ATOM 1848 OH TYR D 249 159.801 33.351 11.988 1.00 55.49 O ANISOU 1848 OH TYR D 249 5592 8095 7395 608 -452 -896 O ATOM 1849 N ASN D 250 164.801 35.567 13.312 1.00 36.35 N ANISOU 1849 N ASN D 250 4112 5581 4120 267 -40 -125 N ATOM 1850 CA ASN D 250 164.531 36.908 12.776 1.00 40.75 C ANISOU 1850 CA ASN D 250 4721 6236 4528 365 -47 122 C ATOM 1851 C ASN D 250 165.680 37.539 12.017 1.00 44.53 C ANISOU 1851 C ASN D 250 5259 6925 4735 381 -60 315 C ATOM 1852 O ASN D 250 165.867 38.759 12.032 1.00 46.82 O ANISOU 1852 O ASN D 250 5661 7156 4972 394 -7 595 O ATOM 1853 CB ASN D 250 163.963 37.876 13.812 1.00 40.34 C ANISOU 1853 CB ASN D 250 4829 5869 4629 341 74 300 C ATOM 1854 CG ASN D 250 162.442 38.012 13.706 1.00 43.35 C ANISOU 1854 CG ASN D 250 5079 6231 5161 454 50 257 C ATOM 1855 OD1 ASN D 250 161.842 37.716 12.657 1.00 42.26 O ANISOU 1855 OD1 ASN D 250 4739 6349 4969 570 -87 149 O ATOM 1856 ND2 ASN D 250 161.815 38.459 14.790 1.00 41.04 N ANISOU 1856 ND2 ASN D 250 4896 5642 5054 438 175 331 N ATOM 1857 N LEU D 251 166.459 36.689 11.360 1.00 46.98 N ANISOU 1857 N LEU D 251 5478 7471 4901 386 -124 172 N ATOM 1858 CA LEU D 251 167.348 37.128 10.301 1.00 44.83 C ANISOU 1858 CA LEU D 251 5185 7511 4339 468 -144 339 C ATOM 1859 C LEU D 251 166.489 37.515 9.099 1.00 49.87 C ANISOU 1859 C LEU D 251 5682 8474 4793 688 -250 374 C ATOM 1860 O LEU D 251 165.416 36.962 8.903 1.00 48.34 O ANISOU 1860 O LEU D 251 5355 8329 4683 770 -361 141 O ATOM 1861 CB LEU D 251 168.265 35.976 9.928 1.00 44.41 C ANISOU 1861 CB LEU D 251 5053 7637 4184 446 -187 126 C ATOM 1862 CG LEU D 251 169.093 35.515 11.117 1.00 40.57 C ANISOU 1862 CG LEU D 251 4695 6837 3882 240 -98 83 C ATOM 1863 CD1 LEU D 251 169.976 34.353 10.728 1.00 37.63 C ANISOU 1863 CD1 LEU D 251 4231 6636 3429 226 -144 -133 C ATOM 1864 CD2 LEU D 251 169.908 36.694 11.601 1.00 44.85 C ANISOU 1864 CD2 LEU D 251 5414 7206 4421 150 10 415 C ATOM 1865 N GLY D 252 166.962 38.458 8.292 1.00 52.75 N ANISOU 1865 N GLY D 252 6061 9059 4923 793 -220 675 N ATOM 1866 CA GLY D 252 166.184 38.922 7.158 1.00 55.34 C ANISOU 1866 CA GLY D 252 6271 9714 5043 1027 -314 755 C ATOM 1867 C GLY D 252 166.331 37.983 5.982 1.00 56.74 C ANISOU 1867 C GLY D 252 6284 10341 4935 1212 -453 512 C ATOM 1868 O GLY D 252 167.110 37.020 6.022 1.00 56.37 O ANISOU 1868 O GLY D 252 6215 10344 4859 1150 -461 303 O ATOM 1869 N GLN D 253 165.587 38.267 4.922 1.00 58.52 N ANISOU 1869 N GLN D 253 6394 10902 4939 1460 -573 529 N ATOM 1870 CA GLN D 253 165.619 37.434 3.735 1.00 60.28 C ANISOU 1870 CA GLN D 253 6461 11590 4852 1692 -740 267 C ATOM 1871 C GLN D 253 166.996 37.475 3.082 1.00 59.61 C ANISOU 1871 C GLN D 253 6405 11802 4443 1763 -635 450 C ATOM 1872 O GLN D 253 167.399 36.510 2.438 1.00 60.52 O ANISOU 1872 O GLN D 253 6426 12214 4355 1884 -733 168 O ATOM 1873 CB GLN D 253 164.540 37.880 2.740 1.00 55.79 C ANISOU 1873 CB GLN D 253 5779 11337 4083 1973 -898 285 C ATOM 1874 N ASP D 254 167.718 38.582 3.244 1.00 60.89 N ANISOU 1874 N ASP D 254 6679 11873 4583 1695 -438 915 N ATOM 1875 CA ASP D 254 169.027 38.715 2.583 1.00 65.87 C ANISOU 1875 CA ASP D 254 7308 12787 4934 1773 -311 1154 C ATOM 1876 C ASP D 254 170.204 38.448 3.521 1.00 63.72 C ANISOU 1876 C ASP D 254 7130 12196 4885 1496 -172 1181 C ATOM 1877 O ASP D 254 171.357 38.707 3.167 1.00 67.91 O ANISOU 1877 O ASP D 254 7660 12867 5276 1510 -33 1441 O ATOM 1878 CB ASP D 254 169.183 40.092 1.925 1.00 69.97 C ANISOU 1878 CB ASP D 254 7837 13475 5274 1921 -182 1696 C ATOM 1879 N ALA D 255 169.910 37.918 4.705 1.00 54.32 N ANISOU 1879 N ALA D 255 6008 10588 4043 1259 -206 924 N ATOM 1880 CA ALA D 255 170.943 37.641 5.700 1.00 53.33 C ANISOU 1880 CA ALA D 255 5983 10140 4140 1002 -99 925 C ATOM 1881 C ALA D 255 172.029 36.739 5.114 1.00 55.18 C ANISOU 1881 C ALA D 255 6139 10659 4166 1060 -89 789 C ATOM 1882 O ALA D 255 171.762 35.916 4.240 1.00 53.43 O ANISOU 1882 O ALA D 255 5793 10797 3710 1259 -213 509 O ATOM 1883 CB ALA D 255 170.332 36.997 6.953 1.00 48.57 C ANISOU 1883 CB ALA D 255 5446 9124 3885 803 -152 624 C ATOM 1884 N ASP D 256 173.257 36.902 5.589 1.00 54.61 N ANISOU 1884 N ASP D 256 6131 10426 4191 897 45 974 N ATOM 1885 CA ASP D 256 174.342 36.011 5.204 1.00 54.02 C ANISOU 1885 CA ASP D 256 5986 10563 3974 923 70 839 C ATOM 1886 C ASP D 256 175.247 35.710 6.402 1.00 51.35 C ANISOU 1886 C ASP D 256 5746 9823 3941 640 135 810 C ATOM 1887 O ASP D 256 175.071 36.269 7.495 1.00 48.52 O ANISOU 1887 O ASP D 256 5518 9046 3871 444 161 911 O ATOM 1888 CB ASP D 256 175.142 36.561 4.010 1.00 60.90 C ANISOU 1888 CB ASP D 256 6771 11860 4507 1133 189 1179 C ATOM 1889 CG ASP D 256 175.833 37.881 4.310 1.00 65.56 C ANISOU 1889 CG ASP D 256 7419 12241 5250 1015 366 1702 C ATOM 1890 OD1 ASP D 256 175.998 38.230 5.498 1.00 66.56 O ANISOU 1890 OD1 ASP D 256 7663 11891 5736 753 386 1749 O ATOM 1891 OD2 ASP D 256 176.222 38.573 3.347 1.00 70.98 O ANISOU 1891 OD2 ASP D 256 8022 13181 5768 1187 475 2036 O ATOM 1892 N GLU D 257 176.188 34.794 6.219 1.00 34.47 N ANISOU 1892 N GLU D 257 3369 5915 3812 301 -25 1103 N ATOM 1893 CA GLU D 257 177.036 34.378 7.335 1.00 36.67 C ANISOU 1893 CA GLU D 257 3771 6008 4155 227 5 994 C ATOM 1894 C GLU D 257 177.797 35.561 7.940 1.00 38.50 C ANISOU 1894 C GLU D 257 4097 5979 4553 310 -26 1039 C ATOM 1895 O GLU D 257 178.064 35.603 9.160 1.00 38.84 O ANISOU 1895 O GLU D 257 4218 5876 4662 304 -14 938 O ATOM 1896 CB GLU D 257 177.975 33.243 6.906 1.00 43.05 C ANISOU 1896 CB GLU D 257 4630 6832 4893 77 35 969 C ATOM 1897 CG GLU D 257 177.244 31.906 6.738 1.00 50.09 C ANISOU 1897 CG GLU D 257 5498 7923 5610 -39 86 871 C ATOM 1898 CD GLU D 257 178.166 30.774 6.312 1.00 50.76 C ANISOU 1898 CD GLU D 257 5664 7998 5626 -159 118 839 C ATOM 1899 N GLY D 258 178.127 36.533 7.098 1.00 37.60 N ANISOU 1899 N GLY D 258 3993 5803 4490 369 -63 1189 N ATOM 1900 CA GLY D 258 178.867 37.690 7.566 1.00 40.30 C ANISOU 1900 CA GLY D 258 4452 5894 4967 413 -82 1236 C ATOM 1901 C GLY D 258 178.158 38.400 8.721 1.00 39.06 C ANISOU 1901 C GLY D 258 4330 5621 4890 544 -83 1162 C ATOM 1902 O GLY D 258 178.788 38.816 9.686 1.00 38.21 O ANISOU 1902 O GLY D 258 4326 5318 4875 521 -72 1104 O ATOM 1903 N ILE D 259 176.842 38.544 8.647 1.00 40.46 N ANISOU 1903 N ILE D 259 4409 5937 5026 680 -94 1149 N ATOM 1904 CA ILE D 259 176.162 39.260 9.713 1.00 42.26 C ANISOU 1904 CA ILE D 259 4657 6067 5331 819 -87 1062 C ATOM 1905 C ILE D 259 176.240 38.480 11.038 1.00 37.97 C ANISOU 1905 C ILE D 259 4134 5508 4782 705 -33 877 C ATOM 1906 O ILE D 259 176.346 39.086 12.104 1.00 38.50 O ANISOU 1906 O ILE D 259 4289 5400 4941 742 -17 803 O ATOM 1907 CB ILE D 259 174.717 39.679 9.351 1.00 49.94 C ANISOU 1907 CB ILE D 259 5494 7216 6263 1024 -116 1074 C ATOM 1908 CG1 ILE D 259 174.306 40.924 10.156 1.00 52.65 C ANISOU 1908 CG1 ILE D 259 5910 7368 6725 1227 -123 1042 C ATOM 1909 CG2 ILE D 259 173.725 38.539 9.577 1.00 49.97 C ANISOU 1909 CG2 ILE D 259 5326 7523 6137 960 -77 929 C ATOM 1910 N LEU D 260 176.254 37.145 10.967 1.00 33.82 N ANISOU 1910 N LEU D 260 3562 5147 4142 556 -7 807 N ATOM 1911 CA LEU D 260 176.332 36.342 12.189 1.00 32.78 C ANISOU 1911 CA LEU D 260 3490 4988 3978 439 35 644 C ATOM 1912 C LEU D 260 177.704 36.463 12.799 1.00 31.79 C ANISOU 1912 C LEU D 260 3509 4631 3939 365 20 644 C ATOM 1913 O LEU D 260 177.825 36.617 14.004 1.00 28.80 O ANISOU 1913 O LEU D 260 3211 4129 3603 343 34 544 O ATOM 1914 CB LEU D 260 175.969 34.864 11.970 1.00 32.32 C ANISOU 1914 CB LEU D 260 3393 5135 3751 293 69 568 C ATOM 1915 CG LEU D 260 174.486 34.683 11.610 1.00 32.76 C ANISOU 1915 CG LEU D 260 3286 5466 3695 330 95 520 C ATOM 1916 CD1 LEU D 260 174.231 33.204 11.353 1.00 34.89 C ANISOU 1916 CD1 LEU D 260 3558 5920 3781 139 140 445 C ATOM 1917 CD2 LEU D 260 173.616 35.162 12.739 1.00 36.04 C ANISOU 1917 CD2 LEU D 260 3669 5887 4136 395 127 386 C ATOM 1918 N TRP D 261 178.746 36.406 11.970 1.00 29.21 N ANISOU 1918 N TRP D 261 3202 4268 3629 317 -6 749 N ATOM 1919 CA TRP D 261 180.094 36.562 12.514 1.00 29.48 C ANISOU 1919 CA TRP D 261 3338 4126 3737 247 -24 738 C ATOM 1920 C TRP D 261 180.245 37.957 13.129 1.00 33.11 C ANISOU 1920 C TRP D 261 3873 4385 4322 311 -28 756 C ATOM 1921 O TRP D 261 180.889 38.135 14.175 1.00 33.00 O ANISOU 1921 O TRP D 261 3947 4232 4359 256 -31 681 O ATOM 1922 CB TRP D 261 181.152 36.440 11.408 1.00 31.78 C ANISOU 1922 CB TRP D 261 3606 4444 4024 188 -43 840 C ATOM 1923 CG TRP D 261 181.423 35.060 10.854 1.00 34.14 C ANISOU 1923 CG TRP D 261 3867 4892 4213 112 -35 810 C ATOM 1924 CD1 TRP D 261 181.091 34.594 9.598 1.00 38.77 C ANISOU 1924 CD1 TRP D 261 4372 5645 4713 97 -21 879 C ATOM 1925 CD2 TRP D 261 182.121 33.991 11.505 1.00 29.92 C ANISOU 1925 CD2 TRP D 261 3393 4340 3635 49 -45 705 C ATOM 1926 NE1 TRP D 261 181.537 33.299 9.446 1.00 36.61 N ANISOU 1926 NE1 TRP D 261 4114 5447 4350 22 -8 813 N ATOM 1927 CE2 TRP D 261 182.165 32.909 10.588 1.00 33.42 C ANISOU 1927 CE2 TRP D 261 3802 4926 3971 7 -28 711 C ATOM 1928 CE3 TRP D 261 182.721 33.849 12.755 1.00 27.80 C ANISOU 1928 CE3 TRP D 261 3217 3947 3399 31 -73 611 C ATOM 1929 CZ2 TRP D 261 182.780 31.698 10.905 1.00 34.34 C ANISOU 1929 CZ2 TRP D 261 3991 5039 4018 -29 -37 622 C ATOM 1930 CZ3 TRP D 261 183.334 32.639 13.066 1.00 32.69 C ANISOU 1930 CZ3 TRP D 261 3898 4579 3944 -2 -96 533 C ATOM 1931 CH2 TRP D 261 183.345 31.572 12.144 1.00 34.33 C ANISOU 1931 CH2 TRP D 261 4087 4908 4050 -21 -77 538 C ATOM 1932 N GLN D 262 179.678 38.959 12.460 1.00 32.42 N ANISOU 1932 N GLN D 262 3770 4274 4275 428 -33 859 N ATOM 1933 CA GLN D 262 179.839 40.342 12.910 1.00 35.56 C ANISOU 1933 CA GLN D 262 4281 4448 4783 495 -32 888 C ATOM 1934 C GLN D 262 179.123 40.568 14.235 1.00 35.21 C ANISOU 1934 C GLN D 262 4268 4336 4774 555 -1 747 C ATOM 1935 O GLN D 262 179.582 41.329 15.091 1.00 35.20 O ANISOU 1935 O GLN D 262 4386 4135 4852 534 13 704 O ATOM 1936 CB GLN D 262 179.337 41.334 11.853 1.00 39.86 C ANISOU 1936 CB GLN D 262 4837 4963 5344 634 -55 1039 C ATOM 1937 CG GLN D 262 180.381 41.655 10.784 1.00 48.89 C ANISOU 1937 CG GLN D 262 6037 6059 6480 534 -74 1182 C ATOM 1938 N MET D 263 177.982 39.913 14.385 1.00 33.37 N ANISOU 1938 N MET D 263 3924 4286 4470 611 17 666 N ATOM 1939 CA MET D 263 177.204 40.058 15.615 1.00 36.39 C ANISOU 1939 CA MET D 263 4315 4646 4866 652 59 511 C ATOM 1940 C MET D 263 177.802 39.277 16.783 1.00 32.63 C ANISOU 1940 C MET D 263 3915 4125 4356 479 75 384 C ATOM 1941 O MET D 263 177.841 39.780 17.906 1.00 34.96 O ANISOU 1941 O MET D 263 4297 4282 4703 466 102 287 O ATOM 1942 CB MET D 263 175.742 39.653 15.405 1.00 37.40 C ANISOU 1942 CB MET D 263 4281 5022 4909 749 81 446 C ATOM 1943 CG MET D 263 174.848 40.783 14.907 1.00 50.56 C ANISOU 1943 CG MET D 263 5888 6691 6633 994 65 505 C ATOM 1944 N PHE D 264 178.278 38.062 16.534 1.00 27.05 N ANISOU 1944 N PHE D 264 3194 3526 3557 353 56 382 N ATOM 1945 CA PHE D 264 178.721 37.216 17.640 1.00 28.34 C ANISOU 1945 CA PHE D 264 3449 3655 3663 214 57 264 C ATOM 1946 C PHE D 264 180.213 37.291 17.972 1.00 30.93 C ANISOU 1946 C PHE D 264 3876 3833 4043 133 8 291 C ATOM 1947 O PHE D 264 180.612 37.153 19.136 1.00 27.59 O ANISOU 1947 O PHE D 264 3551 3319 3613 55 -2 197 O ATOM 1948 CB PHE D 264 178.307 35.788 17.377 1.00 25.35 C ANISOU 1948 CB PHE D 264 3040 3459 3132 130 65 220 C ATOM 1949 CG PHE D 264 176.842 35.563 17.626 1.00 27.82 C ANISOU 1949 CG PHE D 264 3276 3936 3358 138 125 117 C ATOM 1950 CD1 PHE D 264 175.920 35.753 16.598 1.00 27.55 C ANISOU 1950 CD1 PHE D 264 3084 4084 3300 236 140 170 C ATOM 1951 CD2 PHE D 264 176.384 35.208 18.887 1.00 28.96 C ANISOU 1951 CD2 PHE D 264 3497 4074 3434 42 165 -38 C ATOM 1952 CE1 PHE D 264 174.600 35.581 16.808 1.00 27.62 C ANISOU 1952 CE1 PHE D 264 2986 4286 3221 244 194 62 C ATOM 1953 CE2 PHE D 264 175.038 35.019 19.123 1.00 27.00 C ANISOU 1953 CE2 PHE D 264 3156 4010 3092 27 233 -154 C ATOM 1954 CZ PHE D 264 174.142 35.199 18.083 1.00 29.45 C ANISOU 1954 CZ PHE D 264 3282 4526 3382 131 248 -111 C ATOM 1955 N GLY D 265 181.021 37.503 16.935 1.00 28.30 N ANISOU 1955 N GLY D 265 3505 3499 3748 143 -22 413 N ATOM 1956 CA GLY D 265 182.471 37.587 17.089 1.00 28.75 C ANISOU 1956 CA GLY D 265 3610 3470 3843 63 -66 431 C ATOM 1957 C GLY D 265 182.954 38.489 18.213 1.00 25.91 C ANISOU 1957 C GLY D 265 3349 2937 3558 18 -65 372 C ATOM 1958 O GLY D 265 183.917 38.134 18.911 1.00 28.78 O ANISOU 1958 O GLY D 265 3757 3274 3906 -70 -109 316 O ATOM 1959 N PRO D 266 182.336 39.680 18.376 1.00 26.99 N ANISOU 1959 N PRO D 266 3526 2956 3772 83 -21 383 N ATOM 1960 CA PRO D 266 182.799 40.586 19.444 1.00 27.88 C ANISOU 1960 CA PRO D 266 3756 2890 3949 21 -7 319 C ATOM 1961 C PRO D 266 182.677 40.001 20.850 1.00 28.02 C ANISOU 1961 C PRO D 266 3832 2901 3916 -50 -11 173 C ATOM 1962 O PRO D 266 183.336 40.513 21.775 1.00 27.79 O ANISOU 1962 O PRO D 266 3893 2753 3914 -142 -16 113 O ATOM 1963 CB PRO D 266 181.906 41.832 19.284 1.00 29.18 C ANISOU 1963 CB PRO D 266 3967 2929 4191 146 49 349 C ATOM 1964 CG PRO D 266 181.523 41.803 17.781 1.00 40.39 C ANISOU 1964 CG PRO D 266 5296 4451 5601 252 37 491 C ATOM 1965 CD PRO D 266 181.348 40.328 17.492 1.00 27.84 C ANISOU 1965 CD PRO D 266 3587 3079 3910 222 11 467 C ATOM 1966 N PHE D 267 181.898 38.929 21.010 1.00 26.58 N ANISOU 1966 N PHE D 267 3612 2846 3640 -35 -9 115 N ATOM 1967 CA PHE D 267 181.683 38.368 22.366 1.00 30.93 C ANISOU 1967 CA PHE D 267 4251 3383 4117 -123 -8 -24 C ATOM 1968 C PHE D 267 182.658 37.265 22.774 1.00 31.44 C ANISOU 1968 C PHE D 267 4371 3483 4092 -218 -92 -44 C ATOM 1969 O PHE D 267 182.719 36.895 23.941 1.00 30.19 O ANISOU 1969 O PHE D 267 4319 3285 3866 -303 -112 -142 O ATOM 1970 CB PHE D 267 180.242 37.873 22.526 1.00 29.94 C ANISOU 1970 CB PHE D 267 4092 3371 3915 -91 53 -104 C ATOM 1971 CG PHE D 267 179.241 38.976 22.466 1.00 31.55 C ANISOU 1971 CG PHE D 267 4244 3544 4199 26 127 -127 C ATOM 1972 CD1 PHE D 267 178.920 39.705 23.611 1.00 31.54 C ANISOU 1972 CD1 PHE D 267 4320 3430 4235 7 180 -246 C ATOM 1973 CD2 PHE D 267 178.632 39.305 21.258 1.00 28.04 C ANISOU 1973 CD2 PHE D 267 3679 3183 3790 171 140 -31 C ATOM 1974 CE1 PHE D 267 178.001 40.742 23.556 1.00 29.99 C ANISOU 1974 CE1 PHE D 267 4082 3197 4117 153 248 -278 C ATOM 1975 CE2 PHE D 267 177.728 40.342 21.188 1.00 29.47 C ANISOU 1975 CE2 PHE D 267 3820 3332 4045 323 191 -49 C ATOM 1976 CZ PHE D 267 177.402 41.064 22.355 1.00 30.50 C ANISOU 1976 CZ PHE D 267 4029 3341 4219 326 248 -179 C ATOM 1977 N GLY D 268 183.429 36.739 21.827 1.00 31.44 N ANISOU 1977 N GLY D 268 3650 4500 3797 -134 546 378 N ATOM 1978 CA GLY D 268 184.335 35.664 22.178 1.00 32.37 C ANISOU 1978 CA GLY D 268 3727 4557 4016 -99 360 349 C ATOM 1979 C GLY D 268 184.567 34.707 21.037 1.00 33.17 C ANISOU 1979 C GLY D 268 3745 4652 4206 30 335 265 C ATOM 1980 O GLY D 268 184.163 34.980 19.901 1.00 33.55 O ANISOU 1980 O GLY D 268 3757 4775 4216 85 453 215 O ATOM 1981 N ALA D 269 185.215 33.585 21.334 1.00 32.20 N ANISOU 1981 N ALA D 269 3600 4442 4193 84 190 255 N ATOM 1982 CA ALA D 269 185.636 32.666 20.280 1.00 30.09 C ANISOU 1982 CA ALA D 269 3252 4143 4036 201 194 160 C ATOM 1983 C ALA D 269 184.386 32.093 19.647 1.00 29.47 C ANISOU 1983 C ALA D 269 3244 4054 3899 184 246 114 C ATOM 1984 O ALA D 269 183.511 31.585 20.354 1.00 29.86 O ANISOU 1984 O ALA D 269 3402 4027 3917 115 198 162 O ATOM 1985 CB ALA D 269 186.513 31.544 20.848 1.00 30.43 C ANISOU 1985 CB ALA D 269 3271 4068 4224 276 48 186 C ATOM 1986 N VAL D 270 184.312 32.202 18.323 1.00 26.92 N ANISOU 1986 N VAL D 270 2857 3818 3552 239 350 13 N ATOM 1987 CA VAL D 270 183.225 31.628 17.511 1.00 24.87 C ANISOU 1987 CA VAL D 270 2625 3600 3224 221 389 -71 C ATOM 1988 C VAL D 270 183.852 30.631 16.508 1.00 27.25 C ANISOU 1988 C VAL D 270 2876 3851 3624 294 415 -211 C ATOM 1989 O VAL D 270 184.865 30.941 15.856 1.00 28.66 O ANISOU 1989 O VAL D 270 2977 4058 3854 375 475 -254 O ATOM 1990 CB VAL D 270 182.482 32.712 16.737 1.00 26.04 C ANISOU 1990 CB VAL D 270 2750 3937 3208 224 495 -64 C ATOM 1991 CG1 VAL D 270 181.436 32.076 15.802 1.00 26.35 C ANISOU 1991 CG1 VAL D 270 2778 4071 3160 207 506 -173 C ATOM 1992 CG2 VAL D 270 181.833 33.745 17.682 1.00 27.41 C ANISOU 1992 CG2 VAL D 270 2976 4138 3300 156 516 73 C ATOM 1993 N THR D 271 183.310 29.417 16.429 1.00 26.97 N ANISOU 1993 N THR D 271 2894 3719 3636 255 396 -291 N ATOM 1994 CA THR D 271 183.941 28.384 15.602 1.00 30.57 C ANISOU 1994 CA THR D 271 3324 4084 4208 311 449 -429 C ATOM 1995 C THR D 271 183.140 28.031 14.373 1.00 34.75 C ANISOU 1995 C THR D 271 3851 4727 4627 256 529 -601 C ATOM 1996 O THR D 271 183.627 27.300 13.527 1.00 33.59 O ANISOU 1996 O THR D 271 3692 4525 4547 284 606 -741 O ATOM 1997 CB THR D 271 184.223 27.071 16.339 1.00 33.99 C ANISOU 1997 CB THR D 271 3824 4272 4818 324 410 -416 C ATOM 1998 OG1 THR D 271 183.033 26.645 17.021 1.00 35.48 O ANISOU 1998 OG1 THR D 271 4121 4406 4956 208 384 -394 O ATOM 1999 CG2 THR D 271 185.358 27.258 17.351 1.00 32.36 C ANISOU 1999 CG2 THR D 271 3586 3977 4733 420 314 -261 C ATOM 2000 N ASN D 272 181.918 28.538 14.279 1.00 36.63 N ANISOU 2000 N ASN D 272 4094 5131 4692 176 514 -596 N ATOM 2001 CA ASN D 272 181.067 28.181 13.156 1.00 38.60 C ANISOU 2001 CA ASN D 272 4320 5537 4809 112 557 -766 C ATOM 2002 C ASN D 272 179.841 29.068 13.158 1.00 36.60 C ANISOU 2002 C ASN D 272 4029 5509 4367 69 520 -703 C ATOM 2003 O ASN D 272 179.319 29.416 14.233 1.00 32.16 O ANISOU 2003 O ASN D 272 3496 4899 3825 28 474 -572 O ATOM 2004 CB ASN D 272 180.655 26.716 13.273 1.00 39.46 C ANISOU 2004 CB ASN D 272 4487 5481 5025 3 576 -914 C ATOM 2005 CG ASN D 272 179.816 26.256 12.108 1.00 46.61 C ANISOU 2005 CG ASN D 272 5356 6562 5791 -100 620 -1135 C ATOM 2006 OD1 ASN D 272 180.343 25.884 11.052 1.00 47.16 O ANISOU 2006 OD1 ASN D 272 5417 6659 5842 -81 698 -1285 O ATOM 2007 ND2 ASN D 272 178.497 26.261 12.292 1.00 46.02 N ANISOU 2007 ND2 ASN D 272 5253 6616 5616 -221 575 -1171 N ATOM 2008 N VAL D 273 179.387 29.462 11.971 1.00 33.12 N ANISOU 2008 N VAL D 273 3527 5319 3738 90 546 -782 N ATOM 2009 CA VAL D 273 178.082 30.112 11.863 1.00 33.11 C ANISOU 2009 CA VAL D 273 3462 5557 3561 62 504 -735 C ATOM 2010 C VAL D 273 177.394 29.548 10.633 1.00 33.70 C ANISOU 2010 C VAL D 273 3472 5857 3477 1 491 -940 C ATOM 2011 O VAL D 273 178.058 29.105 9.708 1.00 32.13 O ANISOU 2011 O VAL D 273 3292 5665 3250 19 542 -1077 O ATOM 2012 CB VAL D 273 178.185 31.650 11.721 1.00 30.40 C ANISOU 2012 CB VAL D 273 3096 5362 3092 200 544 -543 C ATOM 2013 CG1 VAL D 273 179.082 32.235 12.834 1.00 32.80 C ANISOU 2013 CG1 VAL D 273 3463 5453 3546 238 575 -382 C ATOM 2014 CG2 VAL D 273 178.691 32.034 10.344 1.00 32.21 C ANISOU 2014 CG2 VAL D 273 3309 5760 3168 311 610 -595 C ATOM 2015 N LYS D 274 176.067 29.574 10.624 1.00 35.90 N ANISOU 2015 N LYS D 274 3665 6329 3647 -78 427 -971 N ATOM 2016 CA LYS D 274 175.327 29.026 9.506 1.00 40.78 C ANISOU 2016 CA LYS D 274 4195 7206 4094 -162 389 -1187 C ATOM 2017 C LYS D 274 173.971 29.692 9.394 1.00 42.46 C ANISOU 2017 C LYS D 274 4262 7734 4137 -158 304 -1126 C ATOM 2018 O LYS D 274 173.216 29.768 10.366 1.00 38.01 O ANISOU 2018 O LYS D 274 3663 7107 3671 -221 281 -1051 O ATOM 2019 CB LYS D 274 175.149 27.512 9.664 1.00 46.75 C ANISOU 2019 CB LYS D 274 4984 7787 4992 -365 414 -1434 C ATOM 2020 CG LYS D 274 174.613 26.806 8.395 1.00 54.49 C ANISOU 2020 CG LYS D 274 5890 9017 5797 -490 402 -1722 C ATOM 2021 N VAL D 275 173.660 30.167 8.198 1.00 37.83 N ANISOU 2021 N VAL D 275 3590 7491 3291 -73 261 -1152 N ATOM 2022 CA VAL D 275 172.341 30.694 7.912 1.00 37.64 C ANISOU 2022 CA VAL D 275 3392 7823 3087 -50 160 -1109 C ATOM 2023 C VAL D 275 171.602 29.571 7.222 1.00 43.77 C ANISOU 2023 C VAL D 275 4059 8798 3772 -254 82 -1426 C ATOM 2024 O VAL D 275 172.123 28.975 6.265 1.00 43.12 O ANISOU 2024 O VAL D 275 4028 8770 3585 -303 100 -1621 O ATOM 2025 CB VAL D 275 172.459 31.948 6.989 1.00 49.60 C ANISOU 2025 CB VAL D 275 4885 9618 4343 195 160 -919 C ATOM 2026 CG1 VAL D 275 171.096 32.353 6.422 1.00 50.08 C ANISOU 2026 CG1 VAL D 275 4737 10119 4173 244 31 -896 C ATOM 2027 CG2 VAL D 275 173.112 33.111 7.757 1.00 45.55 C ANISOU 2027 CG2 VAL D 275 4476 8889 3940 367 276 -622 C ATOM 2028 N ILE D 276 170.396 29.270 7.695 1.00 48.11 N ANISOU 2028 N ILE D 276 3741 10372 4165 171 -137 -2497 N ATOM 2029 CA ILE D 276 169.626 28.158 7.159 1.00 43.48 C ANISOU 2029 CA ILE D 276 3170 9774 3575 194 -158 -2499 C ATOM 2030 C ILE D 276 168.770 28.651 5.996 1.00 48.13 C ANISOU 2030 C ILE D 276 3788 10371 4126 180 -161 -2479 C ATOM 2031 O ILE D 276 168.058 29.641 6.123 1.00 45.48 O ANISOU 2031 O ILE D 276 3465 10039 3776 168 -155 -2449 O ATOM 2032 CB ILE D 276 168.730 27.510 8.243 1.00 43.45 C ANISOU 2032 CB ILE D 276 3169 9745 3596 217 -171 -2485 C ATOM 2033 CG1 ILE D 276 169.600 26.985 9.396 1.00 44.53 C ANISOU 2033 CG1 ILE D 276 3277 9871 3771 231 -167 -2506 C ATOM 2034 CG2 ILE D 276 167.858 26.412 7.627 1.00 45.52 C ANISOU 2034 CG2 ILE D 276 3457 9993 3845 231 -197 -2483 C ATOM 2035 CD1 ILE D 276 170.615 25.936 8.974 1.00 50.51 C ANISOU 2035 CD1 ILE D 276 4024 10631 4538 244 -174 -2544 C ATOM 2036 N ARG D 277 168.853 27.965 4.860 1.00 51.09 N ANISOU 2036 N ARG D 277 4178 10750 4482 186 -174 -2495 N ATOM 2037 CA ARG D 277 168.151 28.393 3.647 1.00 55.12 C ANISOU 2037 CA ARG D 277 4719 11271 4956 172 -178 -2479 C ATOM 2038 C ARG D 277 167.244 27.315 3.077 1.00 56.97 C ANISOU 2038 C ARG D 277 4987 11484 5176 188 -209 -2478 C ATOM 2039 O ARG D 277 167.499 26.128 3.234 1.00 58.70 O ANISOU 2039 O ARG D 277 5214 11682 5408 209 -229 -2499 O ATOM 2040 CB ARG D 277 169.157 28.816 2.567 1.00 59.05 C ANISOU 2040 CB ARG D 277 5212 11797 5429 158 -164 -2499 C ATOM 2041 CG ARG D 277 169.728 30.204 2.784 1.00 62.18 C ANISOU 2041 CG ARG D 277 5591 12216 5818 128 -137 -2489 C ATOM 2042 CD ARG D 277 171.023 30.400 2.020 1.00 63.95 C ANISOU 2042 CD ARG D 277 5795 12480 6024 116 -123 -2513 C ATOM 2043 NE ARG D 277 171.512 31.762 2.206 1.00 66.08 N ANISOU 2043 NE ARG D 277 6057 12770 6280 79 -101 -2500 N ATOM 2044 CZ ARG D 277 172.680 32.079 2.758 1.00 73.52 C ANISOU 2044 CZ ARG D 277 6968 13737 7229 63 -87 -2514 C ATOM 2045 NH1 ARG D 277 173.511 31.132 3.188 1.00 73.59 N ANISOU 2045 NH1 ARG D 277 6942 13759 7260 85 -90 -2542 N ATOM 2046 NH2 ARG D 277 173.020 33.356 2.879 1.00 77.49 N ANISOU 2046 NH2 ARG D 277 7477 14255 7712 25 -70 -2500 N ATOM 2047 N ASP D 278 166.171 27.747 2.422 1.00 59.89 N ANISOU 2047 N ASP D 278 5381 11858 5516 175 -216 -2450 N ATOM 2048 CA ASP D 278 165.336 26.868 1.610 1.00 60.44 C ANISOU 2048 CA ASP D 278 5492 11911 5562 180 -250 -2445 C ATOM 2049 C ASP D 278 166.183 26.197 0.510 1.00 58.44 C ANISOU 2049 C ASP D 278 5262 11651 5291 190 -262 -2481 C ATOM 2050 O ASP D 278 166.812 26.883 -0.306 1.00 56.76 O ANISOU 2050 O ASP D 278 5043 11463 5059 181 -242 -2490 O ATOM 2051 CB ASP D 278 164.248 27.712 0.957 1.00 67.81 C ANISOU 2051 CB ASP D 278 6441 12863 6463 161 -250 -2410 C ATOM 2052 CG ASP D 278 163.091 26.884 0.441 1.00 78.45 C ANISOU 2052 CG ASP D 278 7828 14194 7785 159 -290 -2392 C ATOM 2053 OD1 ASP D 278 162.912 25.740 0.918 1.00 80.93 O ANISOU 2053 OD1 ASP D 278 8158 14481 8112 170 -320 -2397 O ATOM 2054 OD2 ASP D 278 162.348 27.393 -0.431 1.00 81.87 O ANISOU 2054 OD2 ASP D 278 8280 14641 8184 143 -295 -2369 O ATOM 2055 N PHE D 279 166.211 24.866 0.490 1.00 54.93 N ANISOU 2055 N PHE D 279 4849 11173 4849 210 -296 -2500 N ATOM 2056 CA PHE D 279 166.938 24.143 -0.564 1.00 58.04 C ANISOU 2056 CA PHE D 279 5276 11558 5219 229 -314 -2534 C ATOM 2057 N CYS D 284 166.748 32.551 2.594 1.00 60.21 N ANISOU 2057 N CYS D 284 5410 11952 5517 101 -137 -2393 N ATOM 2058 CA CYS D 284 166.904 32.406 4.066 1.00 57.67 C ANISOU 2058 CA CYS D 284 5070 11614 5229 116 -136 -2392 C ATOM 2059 C CYS D 284 165.571 32.104 4.741 1.00 54.30 C ANISOU 2059 C CYS D 284 4646 11179 4805 140 -152 -2364 C ATOM 2060 O CYS D 284 164.523 32.678 4.397 1.00 55.00 O ANISOU 2060 O CYS D 284 4754 11279 4865 140 -156 -2333 O ATOM 2061 CB CYS D 284 167.556 33.629 4.741 1.00 57.65 C ANISOU 2061 CB CYS D 284 5073 11608 5224 96 -119 -2386 C ATOM 2062 SG CYS D 284 167.752 33.507 6.621 1.00 61.96 S ANISOU 2062 SG CYS D 284 5605 12129 5808 116 -121 -2386 S ATOM 2063 N LYS D 285 165.596 31.193 5.703 1.00 54.48 N ANISOU 2063 N LYS D 285 4649 11191 4860 161 -161 -2374 N ATOM 2064 CA LYS D 285 164.353 30.820 6.381 1.00 53.05 C ANISOU 2064 CA LYS D 285 4466 11014 4679 185 -175 -2346 C ATOM 2065 C LYS D 285 163.997 31.721 7.562 1.00 52.55 C ANISOU 2065 C LYS D 285 4400 10951 4615 199 -168 -2321 C ATOM 2066 O LYS D 285 162.946 31.559 8.172 1.00 51.56 O ANISOU 2066 O LYS D 285 4267 10841 4482 222 -178 -2293 O ATOM 2067 CB LYS D 285 164.388 29.358 6.829 1.00 54.00 C ANISOU 2067 CB LYS D 285 4572 11119 4825 202 -191 -2364 C ATOM 2068 CG LYS D 285 164.471 28.366 5.693 1.00 55.20 C ANISOU 2068 CG LYS D 285 4743 11264 4967 197 -209 -2384 C ATOM 2069 CD LYS D 285 164.253 26.957 6.220 1.00 59.65 C ANISOU 2069 CD LYS D 285 5309 11806 5550 214 -233 -2394 C ATOM 2070 CE LYS D 285 164.585 25.911 5.162 1.00 63.26 C ANISOU 2070 CE LYS D 285 5798 12242 5997 213 -257 -2420 C ATOM 2071 NZ LYS D 285 164.402 24.522 5.676 1.00 65.94 N ANISOU 2071 NZ LYS D 285 6153 12549 6350 228 -288 -2429 N ATOM 2072 N GLY D 286 164.861 32.673 7.888 1.00 47.84 N ANISOU 2072 N GLY D 286 3814 10341 4022 185 -154 -2328 N ATOM 2073 CA GLY D 286 164.604 33.522 9.028 1.00 49.33 C ANISOU 2073 CA GLY D 286 4015 10521 4207 202 -152 -2306 C ATOM 2074 C GLY D 286 165.505 33.219 10.225 1.00 51.04 C ANISOU 2074 C GLY D 286 4217 10716 4461 208 -149 -2327 C ATOM 2075 O GLY D 286 165.550 34.002 11.169 1.00 48.64 O ANISOU 2075 O GLY D 286 3933 10395 4153 219 -148 -2315 O ATOM 2076 N PHE D 287 166.212 32.090 10.196 1.00 36.75 N ANISOU 2076 N PHE D 287 3856 6002 4105 -16 326 -865 N ATOM 2077 CA PHE D 287 167.038 31.683 11.337 1.00 36.97 C ANISOU 2077 CA PHE D 287 3942 5919 4187 -34 357 -823 C ATOM 2078 C PHE D 287 168.381 31.090 10.965 1.00 37.51 C ANISOU 2078 C PHE D 287 4082 5890 4280 -19 372 -813 C ATOM 2079 O PHE D 287 168.653 30.767 9.793 1.00 35.26 O ANISOU 2079 O PHE D 287 3812 5611 3974 -6 365 -852 O ATOM 2080 CB PHE D 287 166.275 30.714 12.256 1.00 41.46 C ANISOU 2080 CB PHE D 287 4498 6468 4788 -126 375 -842 C ATOM 2081 CG PHE D 287 165.897 29.404 11.603 1.00 42.59 C ANISOU 2081 CG PHE D 287 4648 6599 4935 -208 374 -912 C ATOM 2082 CD1 PHE D 287 164.672 29.262 10.948 1.00 45.95 C ANISOU 2082 CD1 PHE D 287 5010 7127 5324 -255 348 -967 C ATOM 2083 CD2 PHE D 287 166.745 28.308 11.670 1.00 38.85 C ANISOU 2083 CD2 PHE D 287 4248 6013 4500 -241 403 -920 C ATOM 2084 CE1 PHE D 287 164.300 28.042 10.357 1.00 44.34 C ANISOU 2084 CE1 PHE D 287 4820 6909 5117 -345 345 -1036 C ATOM 2085 CE2 PHE D 287 166.389 27.088 11.103 1.00 37.67 C ANISOU 2085 CE2 PHE D 287 4121 5840 4353 -320 409 -988 C ATOM 2086 CZ PHE D 287 165.155 26.955 10.432 1.00 41.66 C ANISOU 2086 CZ PHE D 287 4567 6445 4816 -378 378 -1050 C ATOM 2087 N GLY D 288 169.222 30.945 11.988 1.00 34.78 N ANISOU 2087 N GLY D 288 3779 5457 3978 -19 396 -757 N ATOM 2088 CA GLY D 288 170.582 30.493 11.801 1.00 29.61 C ANISOU 2088 CA GLY D 288 3185 4714 3351 7 415 -726 C ATOM 2089 C GLY D 288 171.163 30.047 13.138 1.00 28.86 C ANISOU 2089 C GLY D 288 3124 4536 3306 -22 441 -669 C ATOM 2090 O GLY D 288 170.465 30.028 14.151 1.00 28.63 O ANISOU 2090 O GLY D 288 3075 4515 3287 -66 445 -664 O ATOM 2091 N PHE D 289 172.427 29.653 13.121 1.00 28.71 N ANISOU 2091 N PHE D 289 3152 4440 3316 4 461 -624 N ATOM 2092 CA PHE D 289 173.075 29.077 14.286 1.00 28.41 C ANISOU 2092 CA PHE D 289 3145 4324 3326 -22 487 -564 C ATOM 2093 C PHE D 289 174.496 29.578 14.358 1.00 32.96 C ANISOU 2093 C PHE D 289 3746 4866 3913 38 487 -481 C ATOM 2094 O PHE D 289 175.122 29.815 13.326 1.00 32.19 O ANISOU 2094 O PHE D 289 3655 4776 3801 93 483 -479 O ATOM 2095 CB PHE D 289 173.128 27.552 14.165 1.00 29.41 C ANISOU 2095 CB PHE D 289 3309 4377 3487 -68 527 -596 C ATOM 2096 CG PHE D 289 171.777 26.915 14.105 1.00 32.12 C ANISOU 2096 CG PHE D 289 3632 4748 3824 -143 528 -676 C ATOM 2097 CD1 PHE D 289 171.059 26.677 15.271 1.00 32.08 C ANISOU 2097 CD1 PHE D 289 3610 4741 3839 -203 535 -669 C ATOM 2098 CD2 PHE D 289 171.210 26.585 12.884 1.00 32.48 C ANISOU 2098 CD2 PHE D 289 3674 4827 3839 -157 520 -756 C ATOM 2099 CE1 PHE D 289 169.800 26.100 15.221 1.00 36.41 C ANISOU 2099 CE1 PHE D 289 4132 5321 4382 -277 536 -737 C ATOM 2100 CE2 PHE D 289 169.942 26.015 12.824 1.00 31.48 C ANISOU 2100 CE2 PHE D 289 3523 4735 3702 -238 515 -827 C ATOM 2101 CZ PHE D 289 169.240 25.770 13.995 1.00 34.77 C ANISOU 2101 CZ PHE D 289 3916 5150 4143 -298 523 -815 C ATOM 2102 N VAL D 290 175.013 29.670 15.580 1.00 31.65 N ANISOU 2102 N VAL D 290 3590 4664 3771 23 491 -410 N ATOM 2103 CA VAL D 290 176.407 30.034 15.780 1.00 31.33 C ANISOU 2103 CA VAL D 290 3568 4593 3743 65 488 -320 C ATOM 2104 C VAL D 290 176.900 29.085 16.842 1.00 33.09 C ANISOU 2104 C VAL D 290 3813 4748 4011 28 517 -265 C ATOM 2105 O VAL D 290 176.153 28.710 17.735 1.00 32.78 O ANISOU 2105 O VAL D 290 3773 4701 3982 -28 525 -282 O ATOM 2106 CB VAL D 290 176.490 31.491 16.285 1.00 36.74 C ANISOU 2106 CB VAL D 290 4241 5325 4395 81 450 -279 C ATOM 2107 CG1 VAL D 290 177.861 31.831 16.814 1.00 38.98 C ANISOU 2107 CG1 VAL D 290 4540 5578 4692 98 441 -177 C ATOM 2108 CG2 VAL D 290 176.079 32.433 15.165 1.00 35.42 C ANISOU 2108 CG2 VAL D 290 4052 5221 4184 129 427 -324 C ATOM 2109 N THR D 291 178.151 28.677 16.761 1.00 29.98 N ANISOU 2109 N THR D 291 3437 4308 3646 61 536 -194 N ATOM 2110 CA THR D 291 178.723 27.854 17.798 1.00 31.67 C ANISOU 2110 CA THR D 291 3668 4463 3900 35 563 -125 C ATOM 2111 C THR D 291 179.852 28.627 18.462 1.00 31.19 C ANISOU 2111 C THR D 291 3598 4415 3836 53 535 -16 C ATOM 2112 O THR D 291 180.734 29.127 17.782 1.00 30.07 O ANISOU 2112 O THR D 291 3449 4288 3688 105 524 26 O ATOM 2113 CB THR D 291 179.333 26.566 17.205 1.00 36.64 C ANISOU 2113 CB THR D 291 4327 5024 4569 61 618 -116 C ATOM 2114 OG1 THR D 291 178.292 25.782 16.620 1.00 38.73 O ANISOU 2114 OG1 THR D 291 4609 5272 4834 30 642 -220 O ATOM 2115 CG2 THR D 291 180.045 25.753 18.308 1.00 39.08 C ANISOU 2115 CG2 THR D 291 4651 5276 4923 46 649 -26 C ATOM 2116 N MET D 292 179.826 28.707 19.787 1.00 30.42 N ANISOU 2116 N MET D 292 3504 4313 3742 6 524 31 N ATOM 2117 CA MET D 292 180.866 29.420 20.515 1.00 31.96 C ANISOU 2117 CA MET D 292 3693 4523 3927 7 492 134 C ATOM 2118 C MET D 292 181.515 28.474 21.513 1.00 32.82 C ANISOU 2118 C MET D 292 3809 4588 4074 -16 516 218 C ATOM 2119 O MET D 292 180.838 27.680 22.128 1.00 33.60 O ANISOU 2119 O MET D 292 3920 4655 4191 -55 544 190 O ATOM 2120 CB MET D 292 180.245 30.613 21.240 1.00 31.73 C ANISOU 2120 CB MET D 292 3667 4538 3851 -31 449 117 C ATOM 2121 CG MET D 292 179.664 31.666 20.288 1.00 30.81 C ANISOU 2121 CG MET D 292 3544 4469 3695 1 426 49 C ATOM 2122 SD MET D 292 179.228 33.183 21.158 1.00 31.50 S ANISOU 2122 SD MET D 292 3648 4595 3723 -29 384 52 S ATOM 2123 CE MET D 292 180.837 33.763 21.772 1.00 34.05 C ANISOU 2123 CE MET D 292 3983 4913 4039 -41 348 178 C ATOM 2124 N THR D 293 182.812 28.611 21.716 1.00 32.52 N ANISOU 2124 N THR D 293 3757 4553 4045 6 505 328 N ATOM 2125 CA THR D 293 183.567 27.664 22.526 1.00 33.74 C ANISOU 2125 CA THR D 293 3910 4672 4237 -2 532 423 C ATOM 2126 C THR D 293 183.305 27.782 24.012 1.00 32.11 C ANISOU 2126 C THR D 293 3711 4473 4014 -70 509 457 C ATOM 2127 O THR D 293 183.212 26.786 24.713 1.00 33.94 O ANISOU 2127 O THR D 293 3952 4666 4276 -90 545 482 O ATOM 2128 CB THR D 293 185.067 27.881 22.292 1.00 37.61 C ANISOU 2128 CB THR D 293 4373 5181 4738 42 521 542 C ATOM 2129 OG1 THR D 293 185.308 27.905 20.881 1.00 35.77 O ANISOU 2129 OG1 THR D 293 4134 4945 4511 110 541 510 O ATOM 2130 CG2 THR D 293 185.880 26.775 22.942 1.00 39.45 C ANISOU 2130 CG2 THR D 293 4597 5378 5013 53 560 648 C ATOM 2131 N ASN D 294 183.191 29.009 24.500 1.00 30.71 N ANISOU 2131 N ASN D 294 3538 4343 3787 -105 454 459 N ATOM 2132 CA ASN D 294 183.162 29.233 25.937 1.00 30.04 C ANISOU 2132 CA ASN D 294 3466 4270 3677 -169 428 507 C ATOM 2133 C ASN D 294 181.773 29.590 26.451 1.00 30.29 C ANISOU 2133 C ASN D 294 3526 4306 3677 -212 426 413 C ATOM 2134 O ASN D 294 181.172 30.577 26.034 1.00 31.17 O ANISOU 2134 O ASN D 294 3646 4445 3751 -208 404 346 O ATOM 2135 CB ASN D 294 184.158 30.325 26.286 1.00 29.60 C ANISOU 2135 CB ASN D 294 3406 4260 3582 -187 369 592 C ATOM 2136 CG ASN D 294 185.572 29.949 25.889 1.00 40.55 C ANISOU 2136 CG ASN D 294 4754 5652 5000 -147 371 704 C ATOM 2137 OD1 ASN D 294 186.090 28.896 26.300 1.00 45.92 O ANISOU 2137 OD1 ASN D 294 5418 6309 5719 -137 403 777 O ATOM 2138 ND2 ASN D 294 186.192 30.781 25.055 1.00 40.70 N ANISOU 2138 ND2 ASN D 294 4757 5703 5006 -117 343 721 N ATOM 2139 N TYR D 295 181.267 28.780 27.369 1.00 30.69 N ANISOU 2139 N TYR D 295 3588 4330 3744 -250 454 413 N ATOM 2140 CA TYR D 295 179.891 28.925 27.816 1.00 32.84 C ANISOU 2140 CA TYR D 295 3878 4605 3994 -285 464 326 C ATOM 2141 C TYR D 295 179.565 30.345 28.279 1.00 34.26 C ANISOU 2141 C TYR D 295 4083 4827 4107 -310 421 309 C ATOM 2142 O TYR D 295 178.489 30.885 27.966 1.00 35.08 O ANISOU 2142 O TYR D 295 4193 4949 4188 -305 425 222 O ATOM 2143 CB TYR D 295 179.582 27.919 28.930 1.00 36.50 C ANISOU 2143 CB TYR D 295 4352 5036 4480 -327 497 353 C ATOM 2144 CG TYR D 295 178.117 27.927 29.326 1.00 37.79 C ANISOU 2144 CG TYR D 295 4527 5203 4629 -361 517 266 C ATOM 2145 CD1 TYR D 295 177.201 27.092 28.704 1.00 38.56 C ANISOU 2145 CD1 TYR D 295 4611 5277 4764 -356 559 188 C ATOM 2146 CD2 TYR D 295 177.648 28.776 30.322 1.00 45.25 C ANISOU 2146 CD2 TYR D 295 5498 6177 5519 -398 494 265 C ATOM 2147 CE1 TYR D 295 175.830 27.097 29.067 1.00 40.99 C ANISOU 2147 CE1 TYR D 295 4918 5597 5058 -390 577 115 C ATOM 2148 CE2 TYR D 295 176.283 28.781 30.695 1.00 45.98 C ANISOU 2148 CE2 TYR D 295 5595 6277 5599 -422 519 193 C ATOM 2149 CZ TYR D 295 175.388 27.942 30.057 1.00 45.06 C ANISOU 2149 CZ TYR D 295 5452 6145 5523 -418 559 122 C ATOM 2150 OH TYR D 295 174.042 27.948 30.390 1.00 47.31 O ANISOU 2150 OH TYR D 295 5732 6448 5798 -443 582 58 O ATOM 2151 N GLU D 296 180.467 30.951 29.045 1.00 31.58 N ANISOU 2151 N GLU D 296 3761 4504 3734 -338 381 393 N ATOM 2152 CA GLU D 296 180.173 32.263 29.627 1.00 34.57 C ANISOU 2152 CA GLU D 296 4182 4911 4044 -370 345 378 C ATOM 2153 C GLU D 296 180.135 33.343 28.536 1.00 31.25 C ANISOU 2153 C GLU D 296 3762 4513 3601 -330 324 332 C ATOM 2154 O GLU D 296 179.391 34.326 28.648 1.00 31.51 O ANISOU 2154 O GLU D 296 3828 4560 3586 -334 317 277 O ATOM 2155 CB GLU D 296 181.188 32.641 30.730 1.00 38.30 C ANISOU 2155 CB GLU D 296 4679 5395 4477 -424 302 480 C ATOM 2156 N GLU D 297 180.957 33.175 27.499 1.00 28.83 N ANISOU 2156 N GLU D 297 3420 4208 3326 -286 318 359 N ATOM 2157 CA GLU D 297 180.913 34.108 26.370 1.00 27.51 C ANISOU 2157 CA GLU D 297 3249 4062 3141 -242 303 316 C ATOM 2158 C GLU D 297 179.627 33.940 25.563 1.00 26.55 C ANISOU 2158 C GLU D 297 3114 3945 3031 -204 337 207 C ATOM 2159 O GLU D 297 179.049 34.916 25.063 1.00 28.04 O ANISOU 2159 O GLU D 297 3313 4157 3184 -181 329 153 O ATOM 2160 CB GLU D 297 182.149 33.915 25.468 1.00 27.25 C ANISOU 2160 CB GLU D 297 3180 4033 3140 -202 292 379 C ATOM 2161 CG GLU D 297 183.449 34.256 26.212 1.00 27.85 C ANISOU 2161 CG GLU D 297 3260 4123 3199 -243 250 496 C ATOM 2162 CD GLU D 297 184.718 34.078 25.394 1.00 36.68 C ANISOU 2162 CD GLU D 297 4335 5252 4349 -203 242 575 C ATOM 2163 OE1 GLU D 297 184.743 33.304 24.425 1.00 35.68 O ANISOU 2163 OE1 GLU D 297 4176 5110 4269 -142 280 555 O ATOM 2164 OE2 GLU D 297 185.720 34.728 25.739 1.00 44.95 O ANISOU 2164 OE2 GLU D 297 5381 6325 5371 -235 197 661 O ATOM 2165 N ALA D 298 179.212 32.692 25.385 1.00 26.05 N ANISOU 2165 N ALA D 298 3025 3858 3014 -199 376 179 N ATOM 2166 CA ALA D 298 177.958 32.403 24.697 1.00 32.10 C ANISOU 2166 CA ALA D 298 3774 4633 3790 -179 405 79 C ATOM 2167 C ALA D 298 176.799 33.041 25.470 1.00 31.38 C ANISOU 2167 C ALA D 298 3704 4563 3658 -207 407 33 C ATOM 2168 O ALA D 298 175.914 33.663 24.886 1.00 27.54 O ANISOU 2168 O ALA D 298 3207 4109 3147 -181 410 -34 O ATOM 2169 CB ALA D 298 177.750 30.892 24.584 1.00 31.09 C ANISOU 2169 CB ALA D 298 3627 4467 3717 -187 447 63 C ATOM 2170 N ALA D 299 176.837 32.899 26.792 1.00 28.15 N ANISOU 2170 N ALA D 299 3321 4138 3237 -257 409 75 N ATOM 2171 CA ALA D 299 175.821 33.495 27.648 1.00 31.04 C ANISOU 2171 CA ALA D 299 3714 4519 3559 -281 417 42 C ATOM 2172 C ALA D 299 175.788 35.020 27.503 1.00 31.24 C ANISOU 2172 C ALA D 299 3775 4571 3526 -259 393 32 C ATOM 2173 O ALA D 299 174.698 35.620 27.426 1.00 28.20 O ANISOU 2173 O ALA D 299 3394 4210 3111 -240 410 -26 O ATOM 2174 CB ALA D 299 176.038 33.083 29.114 1.00 30.23 C ANISOU 2174 CB ALA D 299 3643 4393 3449 -338 422 98 C ATOM 2175 N AMET D 300 176.963 35.644 27.469 0.57 28.79 N ANISOU 2175 N AMET D 300 3489 4254 3197 -262 355 92 N ATOM 2176 N BMET D 300 176.954 35.660 27.478 0.43 29.12 N ANISOU 2176 N BMET D 300 3532 4296 3238 -262 355 92 N ATOM 2177 CA AMET D 300 177.012 37.088 27.286 0.57 30.39 C ANISOU 2177 CA AMET D 300 3733 4472 3344 -245 334 85 C ATOM 2178 CA BMET D 300 176.995 37.110 27.311 0.43 30.34 C ANISOU 2178 CA BMET D 300 3727 4464 3335 -246 334 84 C ATOM 2179 C AMET D 300 176.405 37.484 25.937 0.57 30.65 C ANISOU 2179 C AMET D 300 3732 4532 3382 -178 344 20 C ATOM 2180 C BMET D 300 176.464 37.527 25.928 0.43 30.55 C ANISOU 2180 C BMET D 300 3720 4519 3368 -178 342 22 C ATOM 2181 O AMET D 300 175.651 38.459 25.832 0.57 29.33 O ANISOU 2181 O AMET D 300 3589 4384 3173 -152 354 -21 O ATOM 2182 O BMET D 300 175.808 38.562 25.793 0.43 29.48 O ANISOU 2182 O BMET D 300 3611 4400 3188 -151 349 -14 O ATOM 2183 CB AMET D 300 178.454 37.608 27.357 0.57 31.09 C ANISOU 2183 CB AMET D 300 3844 4551 3416 -267 288 165 C ATOM 2184 CB BMET D 300 178.418 37.660 27.511 0.43 31.29 C ANISOU 2184 CB BMET D 300 3877 4575 3436 -274 288 166 C ATOM 2185 CG AMET D 300 178.520 39.132 27.358 0.57 29.12 C ANISOU 2185 CG AMET D 300 3656 4306 3104 -266 267 161 C ATOM 2186 CG BMET D 300 178.970 37.585 28.936 0.43 32.64 C ANISOU 2186 CG BMET D 300 4093 4730 3580 -347 268 232 C ATOM 2187 SD AMET D 300 177.278 39.784 28.523 0.57 42.15 S ANISOU 2187 SD AMET D 300 5377 5946 4691 -288 298 113 S ATOM 2188 SD BMET D 300 178.138 38.619 30.158 0.43 40.14 S ANISOU 2188 SD BMET D 300 5134 5670 4448 -385 277 203 S ATOM 2189 CE AMET D 300 177.831 39.033 30.051 0.57 42.65 C ANISOU 2189 CE AMET D 300 5467 5989 4748 -373 284 180 C ATOM 2190 CE BMET D 300 177.493 39.924 29.115 0.43 42.87 C ANISOU 2190 CE BMET D 300 5500 6028 4762 -319 289 136 C ATOM 2191 N ALA D 301 176.753 36.731 24.903 1.00 31.56 N ANISOU 2191 N ALA D 301 3794 4652 3545 -149 345 13 N ATOM 2192 CA ALA D 301 176.237 37.025 23.565 1.00 32.07 C ANISOU 2192 CA ALA D 301 3825 4749 3612 -88 352 -46 C ATOM 2193 C ALA D 301 174.692 36.933 23.552 1.00 29.59 C ANISOU 2193 C ALA D 301 3489 4465 3289 -77 384 -122 C ATOM 2194 O ALA D 301 174.009 37.837 23.079 1.00 26.80 O ANISOU 2194 O ALA D 301 3135 4146 2901 -35 388 -159 O ATOM 2195 CB ALA D 301 176.850 36.091 22.522 1.00 28.13 C ANISOU 2195 CB ALA D 301 3281 4244 3163 -62 353 -42 C ATOM 2196 N ILE D 302 174.161 35.832 24.064 1.00 26.49 N ANISOU 2196 N ILE D 302 3076 4061 2928 -113 407 -138 N ATOM 2197 CA ILE D 302 172.722 35.639 24.130 1.00 28.74 C ANISOU 2197 CA ILE D 302 3332 4379 3208 -113 437 -200 C ATOM 2198 C ILE D 302 172.042 36.784 24.899 1.00 32.98 C ANISOU 2198 C ILE D 302 3907 4934 3690 -104 447 -202 C ATOM 2199 O ILE D 302 171.045 37.338 24.420 1.00 30.55 O ANISOU 2199 O ILE D 302 3575 4674 3360 -64 463 -246 O ATOM 2200 CB ILE D 302 172.368 34.265 24.762 1.00 26.63 C ANISOU 2200 CB ILE D 302 3046 4088 2984 -166 461 -205 C ATOM 2201 CG1 ILE D 302 172.829 33.142 23.846 1.00 28.07 C ANISOU 2201 CG1 ILE D 302 3197 4251 3218 -165 463 -217 C ATOM 2202 CG2 ILE D 302 170.833 34.150 25.105 1.00 28.73 C ANISOU 2202 CG2 ILE D 302 3282 4393 3240 -178 493 -257 C ATOM 2203 CD1 ILE D 302 172.815 31.785 24.497 1.00 29.51 C ANISOU 2203 CD1 ILE D 302 3377 4391 3446 -217 489 -205 C ATOM 2204 N ALA D 303 172.571 37.148 26.078 1.00 30.76 N ANISOU 2204 N ALA D 303 3686 4617 3382 -140 442 -152 N ATOM 2205 CA ALA D 303 171.913 38.201 26.887 1.00 34.18 C ANISOU 2205 CA ALA D 303 4173 5058 3758 -134 461 -156 C ATOM 2206 C ALA D 303 171.979 39.566 26.205 1.00 32.45 C ANISOU 2206 C ALA D 303 3981 4853 3495 -77 452 -164 C ATOM 2207 O ALA D 303 171.057 40.381 26.321 1.00 31.68 O ANISOU 2207 O ALA D 303 3901 4778 3358 -40 482 -190 O ATOM 2208 CB ALA D 303 172.523 38.292 28.339 1.00 29.74 C ANISOU 2208 CB ALA D 303 3682 4450 3167 -193 454 -102 C ATOM 2209 N SER D 304 173.067 39.809 25.477 1.00 28.85 N ANISOU 2209 N SER D 304 3528 4385 3048 -67 416 -138 N ATOM 2210 CA SER D 304 173.218 41.083 24.784 1.00 32.62 C ANISOU 2210 CA SER D 304 4034 4872 3487 -16 408 -141 C ATOM 2211 C SER D 304 172.388 41.189 23.494 1.00 34.70 C ANISOU 2211 C SER D 304 4233 5191 3760 54 422 -193 C ATOM 2212 O SER D 304 171.906 42.269 23.164 1.00 36.50 O ANISOU 2212 O SER D 304 4482 5439 3948 107 437 -207 O ATOM 2213 CB SER D 304 174.697 41.348 24.480 1.00 36.17 C ANISOU 2213 CB SER D 304 4508 5294 3942 -33 364 -87 C ATOM 2214 OG SER D 304 175.435 41.295 25.696 1.00 46.15 O ANISOU 2214 OG SER D 304 5827 6518 5189 -103 347 -33 O ATOM 2215 N LEU D 305 172.220 40.077 22.779 1.00 30.94 N ANISOU 2215 N LEU D 305 3683 4739 3332 54 418 -220 N ATOM 2216 CA LEU D 305 171.578 40.086 21.458 1.00 30.56 C ANISOU 2216 CA LEU D 305 3572 4749 3290 111 422 -267 C ATOM 2217 C LEU D 305 170.080 39.698 21.463 1.00 34.14 C ANISOU 2217 C LEU D 305 3970 5257 3744 118 452 -318 C ATOM 2218 O LEU D 305 169.331 40.066 20.557 1.00 35.13 O ANISOU 2218 O LEU D 305 4049 5443 3854 171 457 -350 O ATOM 2219 CB LEU D 305 172.345 39.172 20.492 1.00 29.25 C ANISOU 2219 CB LEU D 305 3366 4578 3168 107 399 -270 C ATOM 2220 CG LEU D 305 173.788 39.612 20.184 1.00 32.62 C ANISOU 2220 CG LEU D 305 3829 4970 3597 115 369 -216 C ATOM 2221 CD1 LEU D 305 174.550 38.515 19.371 1.00 28.31 C ANISOU 2221 CD1 LEU D 305 3246 4412 3098 112 358 -212 C ATOM 2222 CD2 LEU D 305 173.779 40.944 19.431 1.00 34.35 C ANISOU 2222 CD2 LEU D 305 4063 5214 3774 177 363 -217 C ATOM 2223 N ASN D 306 169.671 38.890 22.429 1.00 30.19 N ANISOU 2223 N ASN D 306 3947 3231 4292 294 -165 95 N ATOM 2224 CA ASN D 306 168.272 38.506 22.517 1.00 30.82 C ANISOU 2224 CA ASN D 306 4080 3562 4068 355 24 -89 C ATOM 2225 C ASN D 306 167.434 39.745 22.784 1.00 34.70 C ANISOU 2225 C ASN D 306 4684 4029 4470 491 -25 -127 C ATOM 2226 O ASN D 306 167.585 40.392 23.826 1.00 33.84 O ANISOU 2226 O ASN D 306 4822 3669 4367 534 -214 -159 O ATOM 2227 CB ASN D 306 168.039 37.486 23.630 1.00 26.86 C ANISOU 2227 CB ASN D 306 3768 3019 3418 297 41 -248 C ATOM 2228 CG ASN D 306 166.603 36.962 23.623 1.00 30.83 C ANISOU 2228 CG ASN D 306 4258 3783 3674 349 274 -400 C ATOM 2229 OD1 ASN D 306 166.060 36.626 22.560 1.00 28.96 O ANISOU 2229 OD1 ASN D 306 3804 3801 3400 353 431 -397 O ATOM 2230 ND2 ASN D 306 165.962 36.939 24.804 1.00 29.02 N ANISOU 2230 ND2 ASN D 306 4271 3467 3286 405 290 -520 N ATOM 2231 N GLY D 307 166.574 40.097 21.832 1.00 39.31 N ANISOU 2231 N GLY D 307 5109 4854 4973 573 126 -122 N ATOM 2232 CA GLY D 307 165.803 41.322 21.934 1.00 40.65 C ANISOU 2232 CA GLY D 307 5349 5010 5086 710 90 -136 C ATOM 2233 C GLY D 307 166.439 42.497 21.201 1.00 45.99 C ANISOU 2233 C GLY D 307 5928 5586 5958 751 -35 46 C ATOM 2234 O GLY D 307 165.893 43.598 21.197 1.00 55.01 O ANISOU 2234 O GLY D 307 7120 6703 7078 866 -85 52 O ATOM 2235 N TYR D 308 167.586 42.274 20.571 1.00 39.10 N ANISOU 2235 N TYR D 308 4911 4649 5295 667 -68 211 N ATOM 2236 CA TYR D 308 168.261 43.328 19.813 1.00 45.23 C ANISOU 2236 CA TYR D 308 5564 5320 6301 704 -149 427 C ATOM 2237 C TYR D 308 167.527 43.543 18.486 1.00 46.20 C ANISOU 2237 C TYR D 308 5523 5728 6304 800 48 467 C ATOM 2238 O TYR D 308 167.057 42.587 17.882 1.00 45.25 O ANISOU 2238 O TYR D 308 5324 5850 6020 791 229 394 O ATOM 2239 CB TYR D 308 169.716 42.936 19.538 1.00 50.72 C ANISOU 2239 CB TYR D 308 6131 5851 7291 598 -196 622 C ATOM 2240 CG TYR D 308 170.491 43.912 18.683 1.00 61.58 C ANISOU 2240 CG TYR D 308 7336 7109 8953 635 -227 892 C ATOM 2241 CD1 TYR D 308 171.097 45.033 19.242 1.00 66.88 C ANISOU 2241 CD1 TYR D 308 8059 7454 9898 632 -503 1009 C ATOM 2242 CD2 TYR D 308 170.640 43.701 17.316 1.00 67.50 C ANISOU 2242 CD2 TYR D 308 7891 8050 9705 685 15 1043 C ATOM 2243 CE1 TYR D 308 171.817 45.923 18.461 1.00 71.10 C ANISOU 2243 CE1 TYR D 308 8410 7863 10740 661 -523 1284 C ATOM 2244 CE2 TYR D 308 171.361 44.586 16.527 1.00 71.91 C ANISOU 2244 CE2 TYR D 308 8298 8492 10533 736 29 1321 C ATOM 2245 CZ TYR D 308 171.945 45.693 17.103 1.00 73.91 C ANISOU 2245 CZ TYR D 308 8560 8427 11095 715 -232 1449 C ATOM 2246 OH TYR D 308 172.658 46.566 16.312 1.00 76.74 O ANISOU 2246 OH TYR D 308 8741 8657 11760 762 -206 1750 O ATOM 2247 N ARG D 309 167.445 44.790 18.030 1.00 47.37 N ANISOU 2247 N ARG D 309 5636 5825 6537 895 -14 584 N ATOM 2248 CA ARG D 309 166.749 45.100 16.778 1.00 50.78 C ANISOU 2248 CA ARG D 309 5945 6500 6848 1003 140 629 C ATOM 2249 C ARG D 309 167.702 45.060 15.576 1.00 53.60 C ANISOU 2249 C ARG D 309 6146 6866 7356 1011 250 872 C ATOM 2250 O ARG D 309 168.618 45.875 15.478 1.00 58.33 O ANISOU 2250 O ARG D 309 6688 7249 8228 1011 165 1087 O ATOM 2251 CB ARG D 309 166.076 46.473 16.867 1.00 51.89 C ANISOU 2251 CB ARG D 309 6141 6594 6981 1121 37 631 C ATOM 2252 N LEU D 310 167.480 44.109 14.671 1.00 48.87 N ANISOU 2252 N LEU D 310 5487 6496 6586 1029 443 847 N ATOM 2253 CA LEU D 310 168.288 43.982 13.465 1.00 50.54 C ANISOU 2253 CA LEU D 310 5597 6731 6873 1082 605 1073 C ATOM 2254 C LEU D 310 167.445 44.386 12.261 1.00 56.23 C ANISOU 2254 C LEU D 310 6323 7664 7379 1238 706 1086 C ATOM 2255 O LEU D 310 166.607 43.608 11.799 1.00 58.49 O ANISOU 2255 O LEU D 310 6650 8171 7401 1271 773 925 O ATOM 2256 CB LEU D 310 168.782 42.544 13.289 1.00 45.71 C ANISOU 2256 CB LEU D 310 4972 6189 6207 1012 743 1041 C ATOM 2257 CG LEU D 310 169.570 42.293 11.988 1.00 48.22 C ANISOU 2257 CG LEU D 310 5226 6540 6555 1107 967 1272 C ATOM 2258 CD1 LEU D 310 170.828 43.144 11.920 1.00 49.30 C ANISOU 2258 CD1 LEU D 310 5239 6416 7076 1111 974 1590 C ATOM 2259 CD2 LEU D 310 169.917 40.814 11.849 1.00 47.55 C ANISOU 2259 CD2 LEU D 310 5160 6533 6373 1055 1100 1204 C ATOM 2260 N GLY D 311 167.681 45.589 11.745 1.00 57.76 N ANISOU 2260 N GLY D 311 6478 7770 7697 1334 693 1283 N ATOM 2261 CA GLY D 311 166.808 46.163 10.740 1.00 58.73 C ANISOU 2261 CA GLY D 311 6631 8064 7621 1489 738 1288 C ATOM 2262 C GLY D 311 165.425 46.408 11.328 1.00 59.72 C ANISOU 2262 C GLY D 311 6805 8300 7586 1494 598 1037 C ATOM 2263 O GLY D 311 165.266 47.218 12.245 1.00 61.23 O ANISOU 2263 O GLY D 311 7012 8354 7899 1468 452 1002 O ATOM 2264 N ASP D 312 164.423 45.703 10.813 1.00 57.51 N ANISOU 2264 N ASP D 312 6554 8248 7048 1538 637 870 N ATOM 2265 CA ASP D 312 163.047 45.915 11.262 1.00 61.61 C ANISOU 2265 CA ASP D 312 7077 8874 7460 1558 532 665 C ATOM 2266 C ASP D 312 162.516 44.715 12.045 1.00 60.67 C ANISOU 2266 C ASP D 312 6955 8833 7264 1446 536 443 C ATOM 2267 O ASP D 312 161.304 44.529 12.172 1.00 64.16 O ANISOU 2267 O ASP D 312 7367 9400 7610 1467 499 282 O ATOM 2268 CB ASP D 312 162.124 46.227 10.072 1.00 63.94 C ANISOU 2268 CB ASP D 312 7377 9340 7579 1706 522 660 C ATOM 2269 N LYS D 313 163.420 43.899 12.576 1.00 55.22 N ANISOU 2269 N LYS D 313 6282 8055 6645 1326 582 450 N ATOM 2270 CA LYS D 313 162.986 42.741 13.335 1.00 53.89 C ANISOU 2270 CA LYS D 313 6120 7946 6410 1218 596 256 C ATOM 2271 C LYS D 313 163.700 42.652 14.677 1.00 46.47 C ANISOU 2271 C LYS D 313 5238 6808 5611 1104 554 242 C ATOM 2272 O LYS D 313 164.828 43.111 14.821 1.00 44.30 O ANISOU 2272 O LYS D 313 4978 6347 5506 1078 515 398 O ATOM 2273 CB LYS D 313 163.188 41.458 12.531 1.00 59.94 C ANISOU 2273 CB LYS D 313 6882 8838 7055 1190 685 228 C ATOM 2274 CG LYS D 313 162.632 41.518 11.115 1.00 65.05 C ANISOU 2274 CG LYS D 313 7538 9642 7535 1324 692 252 C ATOM 2275 CD LYS D 313 162.029 40.189 10.697 1.00 68.04 C ANISOU 2275 CD LYS D 313 7931 10167 7756 1294 689 94 C ATOM 2276 CE LYS D 313 160.587 40.070 11.194 1.00 70.74 C ANISOU 2276 CE LYS D 313 8186 10599 8094 1267 588 -90 C ATOM 2277 N ILE D 314 163.021 42.074 15.660 1.00 38.24 N ANISOU 2277 N ILE D 314 4233 5785 4511 1045 553 65 N ATOM 2278 CA ILE D 314 163.619 41.847 16.968 1.00 38.49 C ANISOU 2278 CA ILE D 314 4375 5625 4624 950 504 27 C ATOM 2279 C ILE D 314 164.145 40.422 17.037 1.00 35.48 C ANISOU 2279 C ILE D 314 3982 5277 4221 827 572 -20 C ATOM 2280 O ILE D 314 163.389 39.452 16.916 1.00 36.43 O ANISOU 2280 O ILE D 314 4059 5560 4221 797 652 -149 O ATOM 2281 CB ILE D 314 162.617 42.102 18.104 1.00 42.54 C ANISOU 2281 CB ILE D 314 4985 6107 5069 989 495 -120 C ATOM 2282 CG1 ILE D 314 162.174 43.570 18.086 1.00 43.95 C ANISOU 2282 CG1 ILE D 314 5195 6226 5278 1123 421 -70 C ATOM 2283 CG2 ILE D 314 163.250 41.744 19.442 1.00 39.84 C ANISOU 2283 CG2 ILE D 314 4819 5556 4761 908 438 -169 C ATOM 2284 CD1 ILE D 314 161.344 43.983 19.273 1.00 50.54 C ANISOU 2284 CD1 ILE D 314 6173 6978 6052 1198 428 -186 C ATOM 2285 N LEU D 315 165.458 40.302 17.202 1.00 34.37 N ANISOU 2285 N LEU D 315 3865 4965 4230 755 529 99 N ATOM 2286 CA LEU D 315 166.116 39.007 17.241 1.00 32.38 C ANISOU 2286 CA LEU D 315 3599 4718 3985 644 591 81 C ATOM 2287 C LEU D 315 165.677 38.202 18.433 1.00 28.78 C ANISOU 2287 C LEU D 315 3244 4239 3452 560 583 -96 C ATOM 2288 O LEU D 315 165.523 38.730 19.518 1.00 31.51 O ANISOU 2288 O LEU D 315 3724 4437 3812 569 493 -146 O ATOM 2289 CB LEU D 315 167.637 39.187 17.354 1.00 36.39 C ANISOU 2289 CB LEU D 315 4095 4995 4736 587 525 267 C ATOM 2290 CG LEU D 315 168.286 39.860 16.145 1.00 40.16 C ANISOU 2290 CG LEU D 315 4457 5467 5335 672 587 497 C ATOM 2291 CD1 LEU D 315 169.810 39.826 16.267 1.00 42.53 C ANISOU 2291 CD1 LEU D 315 4693 5528 5937 603 554 704 C ATOM 2292 CD2 LEU D 315 167.846 39.140 14.893 1.00 44.70 C ANISOU 2292 CD2 LEU D 315 4983 6291 5709 741 766 475 C ATOM 2293 N GLN D 316 165.528 36.904 18.224 1.00 31.25 N ANISOU 2293 N GLN D 316 3516 4680 3678 489 679 -183 N ATOM 2294 CA GLN D 316 165.311 35.983 19.315 1.00 31.81 C ANISOU 2294 CA GLN D 316 3676 4711 3699 396 693 -320 C ATOM 2295 C GLN D 316 166.550 35.110 19.334 1.00 31.50 C ANISOU 2295 C GLN D 316 3639 4572 3757 290 684 -259 C ATOM 2296 O GLN D 316 166.877 34.481 18.333 1.00 31.00 O ANISOU 2296 O GLN D 316 3478 4617 3683 283 766 -213 O ATOM 2297 CB GLN D 316 164.057 35.152 19.064 1.00 34.96 C ANISOU 2297 CB GLN D 316 3998 5326 3958 394 801 -463 C ATOM 2298 CG GLN D 316 162.816 36.003 18.777 1.00 42.96 C ANISOU 2298 CG GLN D 316 4949 6452 4921 510 815 -494 C ATOM 2299 CD GLN D 316 161.633 35.190 18.297 1.00 43.25 C ANISOU 2299 CD GLN D 316 4856 6686 4892 503 882 -602 C ATOM 2300 OE1 GLN D 316 161.665 33.956 18.326 1.00 44.93 O ANISOU 2300 OE1 GLN D 316 5044 6942 5084 406 921 -670 O ATOM 2301 NE2 GLN D 316 160.574 35.880 17.856 1.00 41.54 N ANISOU 2301 NE2 GLN D 316 4546 6569 4668 605 875 -612 N ATOM 2302 N VAL D 317 167.284 35.114 20.442 1.00 27.41 N ANISOU 2302 N VAL D 317 3250 3826 3338 222 572 -249 N ATOM 2303 CA VAL D 317 168.588 34.449 20.470 1.00 27.41 C ANISOU 2303 CA VAL D 317 3230 3690 3496 125 533 -157 C ATOM 2304 C VAL D 317 168.583 33.586 21.713 1.00 30.32 C ANISOU 2304 C VAL D 317 3754 3958 3810 32 489 -286 C ATOM 2305 O VAL D 317 168.247 34.068 22.787 1.00 29.82 O ANISOU 2305 O VAL D 317 3875 3762 3695 57 393 -355 O ATOM 2306 CB VAL D 317 169.758 35.473 20.563 1.00 27.54 C ANISOU 2306 CB VAL D 317 3238 3447 3779 133 369 37 C ATOM 2307 CG1 VAL D 317 171.100 34.756 20.607 1.00 23.65 C ANISOU 2307 CG1 VAL D 317 2685 2794 3506 34 333 154 C ATOM 2308 CG2 VAL D 317 169.692 36.500 19.415 1.00 29.95 C ANISOU 2308 CG2 VAL D 317 3409 3834 4137 245 423 182 C ATOM 2309 N SER D 318 168.930 32.316 21.567 1.00 29.20 N ANISOU 2309 N SER D 318 3565 3869 3660 -59 565 -318 N ATOM 2310 CA SER D 318 168.863 31.403 22.702 1.00 30.42 C ANISOU 2310 CA SER D 318 3870 3942 3747 -146 542 -440 C ATOM 2311 C SER D 318 169.730 30.178 22.468 1.00 32.17 C ANISOU 2311 C SER D 318 4026 4148 4049 -251 575 -414 C ATOM 2312 O SER D 318 170.084 29.912 21.331 1.00 32.62 O ANISOU 2312 O SER D 318 3924 4314 4154 -235 669 -334 O ATOM 2313 CB SER D 318 167.413 30.952 22.901 1.00 34.55 C ANISOU 2313 CB SER D 318 4411 4659 4057 -121 686 -599 C ATOM 2314 OG SER D 318 166.903 30.363 21.702 1.00 34.45 O ANISOU 2314 OG SER D 318 4212 4889 3990 -118 815 -622 O ATOM 2315 N PHE D 319 170.065 29.413 23.510 1.00 29.44 N ANISOU 2315 N PHE D 319 3822 3662 3704 -340 508 -480 N ATOM 2316 CA PHE D 319 170.727 28.125 23.270 1.00 28.22 C ANISOU 2316 CA PHE D 319 3599 3519 3606 -437 561 -476 C ATOM 2317 C PHE D 319 169.800 27.207 22.480 1.00 27.08 C ANISOU 2317 C PHE D 319 3350 3649 3290 -437 752 -583 C ATOM 2318 O PHE D 319 168.626 27.050 22.846 1.00 32.68 O ANISOU 2318 O PHE D 319 4105 4471 3842 -427 817 -710 O ATOM 2319 CB PHE D 319 171.147 27.413 24.550 1.00 26.65 C ANISOU 2319 CB PHE D 319 3586 3125 3417 -532 450 -539 C ATOM 2320 CG PHE D 319 172.343 28.014 25.231 1.00 27.24 C ANISOU 2320 CG PHE D 319 3754 2879 3716 -557 200 -424 C ATOM 2321 CD1 PHE D 319 173.602 27.947 24.649 1.00 31.02 C ANISOU 2321 CD1 PHE D 319 4063 3243 4479 -596 144 -253 C ATOM 2322 CD2 PHE D 319 172.222 28.587 26.484 1.00 27.72 C ANISOU 2322 CD2 PHE D 319 4088 2728 3718 -533 15 -479 C ATOM 2323 CE1 PHE D 319 174.719 28.482 25.294 1.00 29.72 C ANISOU 2323 CE1 PHE D 319 3953 2748 4592 -633 -127 -129 C ATOM 2324 CE2 PHE D 319 173.326 29.132 27.135 1.00 32.34 C ANISOU 2324 CE2 PHE D 319 4783 2976 4527 -559 -284 -381 C ATOM 2325 CZ PHE D 319 174.586 29.074 26.534 1.00 35.58 C ANISOU 2325 CZ PHE D 319 4975 3265 5278 -622 -371 -201 C ATOM 2326 N LYS D 320 170.333 26.607 21.417 1.00 31.58 N ANISOU 2326 N LYS D 320 3790 4302 3906 -438 836 -522 N ATOM 2327 CA LYS D 320 169.592 25.674 20.567 1.00 32.27 C ANISOU 2327 CA LYS D 320 3810 4612 3841 -432 964 -623 C ATOM 2328 C LYS D 320 168.983 24.579 21.417 1.00 35.38 C ANISOU 2328 C LYS D 320 4275 5022 4147 -536 978 -777 C ATOM 2329 O LYS D 320 169.616 24.083 22.351 1.00 35.18 O ANISOU 2329 O LYS D 320 4343 4836 4187 -621 922 -780 O ATOM 2330 CB LYS D 320 170.500 25.050 19.477 1.00 38.63 C ANISOU 2330 CB LYS D 320 4541 5439 4699 -404 1047 -531 C ATOM 2331 CG LYS D 320 169.762 24.083 18.525 1.00 36.70 C ANISOU 2331 CG LYS D 320 4292 5367 4286 -362 1094 -623 C ATOM 2332 CD LYS D 320 170.717 23.422 17.523 1.00 38.48 C ANISOU 2332 CD LYS D 320 4514 5575 4533 -295 1174 -524 C ATOM 2333 CE LYS D 320 169.932 22.592 16.482 1.00 39.66 C ANISOU 2333 CE LYS D 320 4725 5833 4510 -210 1139 -593 C ATOM 2334 NZ LYS D 320 168.884 21.721 17.130 1.00 33.24 N ANISOU 2334 NZ LYS D 320 3928 5042 3658 -324 1025 -751 N ATOM 2335 N THR D 321 167.736 24.241 21.104 1.00 34.43 N ANISOU 2335 N THR D 321 4116 5035 3930 -504 977 -845 N ATOM 2336 CA THR D 321 167.043 23.124 21.732 1.00 38.98 C ANISOU 2336 CA THR D 321 4723 5593 4496 -576 946 -913 C ATOM 2337 C THR D 321 166.948 21.961 20.761 1.00 44.40 C ANISOU 2337 C THR D 321 5349 6346 5174 -590 919 -932 C ATOM 2338 O THR D 321 167.158 22.130 19.555 1.00 45.40 O ANISOU 2338 O THR D 321 5437 6546 5265 -509 922 -895 O ATOM 2339 CB THR D 321 165.617 23.520 22.180 1.00 42.28 C ANISOU 2339 CB THR D 321 5121 6059 4884 -534 957 -943 C ATOM 2340 OG1 THR D 321 164.943 24.204 21.108 1.00 42.76 O ANISOU 2340 OG1 THR D 321 5080 6249 4919 -442 948 -929 O ATOM 2341 CG2 THR D 321 165.687 24.416 23.404 1.00 41.97 C ANISOU 2341 CG2 THR D 321 5212 5916 4819 -513 993 -944 C ATOM 2342 N ASN D 322 166.670 20.770 21.278 1.00 52.25 N ANISOU 2342 N ASN D 322 6357 7308 6189 -685 905 -992 N ATOM 2343 CA ASN D 322 166.426 19.614 20.410 1.00 59.55 C ANISOU 2343 CA ASN D 322 7233 8300 7095 -712 880 -1047 C ATOM 2344 C ASN D 322 165.015 19.616 19.820 1.00 62.59 C ANISOU 2344 C ASN D 322 7516 8821 7445 -695 866 -1126 C ATOM 2345 O ASN D 322 164.848 19.711 18.600 1.00 65.34 O ANISOU 2345 O ASN D 322 7833 9271 7721 -623 842 -1153 O ATOM 2346 CB ASN D 322 166.696 18.306 21.153 1.00 61.12 C ANISOU 2346 CB ASN D 322 7468 8417 7340 -835 879 -1091 C ATOM 2347 CG ASN D 322 168.177 18.059 21.373 1.00 61.98 C ANISOU 2347 CG ASN D 322 7651 8414 7483 -862 892 -1043 C TER 2348 ASN D 322 ATOM 2349 P A E 1 233.007 35.690 55.315 1.00 62.82 P ATOM 2350 OP1 A E 1 231.987 36.272 56.243 1.00 52.75 O ATOM 2351 OP2 A E 1 232.824 34.320 54.782 1.00 64.90 O ATOM 2352 O5' A E 1 233.340 36.703 54.136 1.00 43.50 O ATOM 2353 C5' A E 1 232.311 37.221 53.299 1.00 46.45 C ATOM 2354 C4' A E 1 232.715 38.536 52.684 1.00 46.40 C ATOM 2355 O4' A E 1 233.707 38.301 51.643 1.00 46.02 O ATOM 2356 C3' A E 1 231.593 39.325 52.016 1.00 47.25 C ATOM 2357 O3' A E 1 231.891 40.718 52.121 1.00 47.39 O ATOM 2358 C2' A E 1 231.734 38.901 50.562 1.00 45.13 C ATOM 2359 O2' A E 1 231.132 39.778 49.636 1.00 40.36 O ATOM 2360 C1' A E 1 233.254 38.888 50.439 1.00 46.93 C ATOM 2361 N9 A E 1 233.774 38.104 49.324 0.74 47.15 N ATOM 2362 C8 A E 1 233.495 36.805 48.971 1.00 49.09 C ATOM 2363 N7 A E 1 234.155 36.414 47.905 1.00 48.13 N ATOM 2364 C5 A E 1 234.922 37.523 47.561 1.00 46.94 C ATOM 2365 C6 A E 1 235.841 37.760 46.523 0.00 47.07 C ATOM 2366 N6 A E 1 236.179 36.862 45.601 1.00 46.20 N ATOM 2367 N1 A E 1 236.428 38.973 46.458 0.70 48.29 N ATOM 2368 C2 A E 1 236.107 39.894 47.377 1.00 48.06 C ATOM 2369 N3 A E 1 235.253 39.795 48.391 0.56 47.31 N ATOM 2370 C4 A E 1 234.691 38.572 48.424 1.00 46.24 C ATOM 2371 P U E 2 231.145 41.631 53.207 1.00 50.64 P ATOM 2372 OP1 U E 2 231.702 43.001 53.081 1.00 53.27 O ATOM 2373 OP2 U E 2 231.239 40.929 54.514 1.00 51.23 O ATOM 2374 O5' U E 2 229.641 41.611 52.699 1.00 49.55 O ATOM 2375 C5' U E 2 229.298 42.093 51.412 1.00 42.76 C ATOM 2376 C4' U E 2 227.837 42.421 51.343 1.00 40.21 C ATOM 2377 O4' U E 2 227.078 41.195 51.481 1.00 36.66 O ATOM 2378 C3' U E 2 227.348 43.359 52.434 1.00 40.27 C ATOM 2379 O3' U E 2 226.403 44.258 51.887 1.00 44.50 O ATOM 2380 C2' U E 2 226.664 42.432 53.438 1.00 38.80 C ATOM 2381 O2' U E 2 225.605 43.031 54.157 1.00 36.92 O ATOM 2382 C1' U E 2 226.161 41.297 52.548 1.00 39.94 C ATOM 2383 N1 U E 2 226.133 39.993 53.223 1.00 41.02 N ATOM 2384 C2 U E 2 224.943 39.322 53.366 1.00 40.06 C ATOM 2385 O2 U E 2 223.872 39.758 52.972 1.00 37.72 O ATOM 2386 N3 U E 2 225.073 38.111 54.000 1.00 43.28 N ATOM 2387 C4 U E 2 226.247 37.541 54.487 1.00 41.55 C ATOM 2388 O4 U E 2 226.196 36.436 55.027 1.00 41.66 O ATOM 2389 C5 U E 2 227.441 38.305 54.292 1.00 38.42 C ATOM 2390 C6 U E 2 227.330 39.477 53.676 1.00 40.80 C ATOM 2391 P U E 3 226.854 45.748 51.514 1.00 44.66 P ATOM 2392 OP1 U E 3 228.290 45.692 51.157 1.00 43.77 O ATOM 2393 OP2 U E 3 226.420 46.621 52.625 1.00 48.07 O ATOM 2394 O5' U E 3 225.990 46.072 50.227 1.00 43.09 O ATOM 2395 C5' U E 3 226.359 45.593 48.940 1.00 41.94 C ATOM 2396 C4' U E 3 225.200 45.724 47.999 1.00 39.02 C ATOM 2397 O4' U E 3 224.205 44.715 48.353 1.00 37.00 O ATOM 2398 C3' U E 3 224.487 47.064 48.082 1.00 37.57 C ATOM 2399 O3' U E 3 223.951 47.408 46.811 1.00 38.64 O ATOM 2400 C2' U E 3 223.346 46.788 49.064 1.00 38.19 C ATOM 2401 O2' U E 3 222.239 47.640 48.911 1.00 38.71 O ATOM 2402 C1' U E 3 222.995 45.334 48.743 1.00 33.84 C ATOM 2403 N1 U E 3 222.467 44.574 49.898 1.00 38.22 N ATOM 2404 C2 U E 3 221.115 44.282 49.939 1.00 37.21 C ATOM 2405 O2 U E 3 220.318 44.661 49.092 1.00 34.52 O ATOM 2406 N3 U E 3 220.719 43.564 51.036 1.00 36.97 N ATOM 2407 C4 U E 3 221.503 43.095 52.071 1.00 39.98 C ATOM 2408 O4 U E 3 220.963 42.449 52.983 1.00 41.38 O ATOM 2409 C5 U E 3 222.893 43.423 51.957 1.00 36.48 C ATOM 2410 C6 U E 3 223.310 44.138 50.901 1.00 37.42 C ATOM 2411 P U E 4 224.598 48.614 45.962 1.00 43.51 P ATOM 2412 OP1 U E 4 225.593 49.258 46.826 1.00 39.35 O ATOM 2413 OP2 U E 4 223.484 49.427 45.434 1.00 46.78 O ATOM 2414 O5' U E 4 225.325 47.853 44.754 1.00 49.14 O ATOM 2415 C5' U E 4 226.500 47.067 44.972 1.00 48.79 C ATOM 2416 C4' U E 4 227.379 47.027 43.740 1.00 49.43 C ATOM 2417 O4' U E 4 226.627 46.445 42.631 1.00 46.62 O ATOM 2418 C3' U E 4 227.866 48.389 43.245 1.00 48.31 C ATOM 2419 O3' U E 4 229.154 48.233 42.637 1.00 44.00 O ATOM 2420 C2' U E 4 226.828 48.745 42.177 1.00 49.04 C ATOM 2421 O2' U E 4 227.276 49.670 41.206 1.00 52.66 O ATOM 2422 C1' U E 4 226.540 47.374 41.565 1.00 48.42 C ATOM 2423 N1 U E 4 225.195 47.236 40.968 1.00 56.27 N ATOM 2424 C2 U E 4 225.093 47.004 39.600 1.00 60.96 C ATOM 2425 O2 U E 4 226.073 46.968 38.861 1.00 56.89 O ATOM 2426 N3 U E 4 223.799 46.841 39.142 1.00 61.77 N ATOM 2427 C4 U E 4 222.637 46.868 39.896 1.00 66.46 C ATOM 2428 O4 U E 4 221.533 46.705 39.354 1.00 71.43 O ATOM 2429 C5 U E 4 222.843 47.088 41.296 1.00 63.28 C ATOM 2430 C6 U E 4 224.082 47.249 41.768 1.00 57.89 C ATOM 2431 P U E 5 230.454 48.087 43.569 1.00 54.89 P ATOM 2432 OP1 U E 5 229.975 47.786 44.954 1.00 58.30 O ATOM 2433 OP2 U E 5 231.279 49.307 43.351 1.00 51.20 O ATOM 2434 O5' U E 5 231.186 46.804 42.963 1.00 52.50 O ATOM 2435 C5' U E 5 231.898 46.877 41.741 1.00 48.64 C ATOM 2436 C4' U E 5 231.404 45.853 40.759 1.00 49.59 C ATOM 2437 O4' U E 5 230.040 46.182 40.353 1.00 48.40 O ATOM 2438 C3' U E 5 232.170 45.768 39.441 1.00 51.88 C ATOM 2439 O3' U E 5 233.366 45.008 39.535 1.00 50.88 O ATOM 2440 C2' U E 5 231.127 45.176 38.502 1.00 50.90 C ATOM 2441 O2' U E 5 230.936 43.786 38.763 1.00 48.74 O ATOM 2442 C1' U E 5 229.876 45.926 38.974 1.00 51.09 C ATOM 2443 N1 U E 5 229.743 47.220 38.279 1.00 50.37 N ATOM 2444 C2 U E 5 229.500 47.123 36.931 1.00 48.10 C ATOM 2445 O2 U E 5 229.372 46.055 36.366 1.00 49.34 O ATOM 2446 N3 U E 5 229.407 48.317 36.276 1.00 47.06 N ATOM 2447 C4 U E 5 229.543 49.572 36.821 1.00 47.13 C ATOM 2448 O4 U E 5 229.428 50.534 36.059 1.00 47.86 O ATOM 2449 C5 U E 5 229.805 49.602 38.238 1.00 47.79 C ATOM 2450 C6 U E 5 229.900 48.445 38.909 1.00 48.09 C TER 2451 U E 5 ATOM 2452 P U F 2 220.553 26.073 6.542 1.00 69.88 P ATOM 2453 OP1 U F 2 221.525 26.932 7.276 1.00 64.20 O ATOM 2454 OP2 U F 2 219.847 26.615 5.341 1.00 70.03 O ATOM 2455 O5' U F 2 219.510 25.417 7.556 1.00 60.20 O ATOM 2456 C5' U F 2 219.615 25.646 8.958 1.00 54.38 C ATOM 2457 C4' U F 2 218.288 25.475 9.656 1.00 50.79 C ATOM 2458 O4' U F 2 217.619 26.756 9.729 1.00 51.40 O ATOM 2459 C3' U F 2 217.314 24.515 8.989 1.00 47.57 C ATOM 2460 O3' U F 2 216.579 23.827 9.988 1.00 42.82 O ATOM 2461 C2' U F 2 216.365 25.444 8.234 1.00 47.57 C ATOM 2462 O2' U F 2 215.073 24.908 8.055 1.00 47.44 O ATOM 2463 C1' U F 2 216.334 26.668 9.141 1.00 48.03 C ATOM 2464 N1 U F 2 216.081 27.939 8.441 1.00 47.34 N ATOM 2465 C2 U F 2 215.077 28.767 8.902 1.00 45.55 C ATOM 2466 O2 U F 2 214.344 28.474 9.820 1.00 42.47 O ATOM 2467 N3 U F 2 214.928 29.952 8.228 1.00 48.28 N ATOM 2468 C4 U F 2 215.680 30.380 7.152 1.00 47.14 C ATOM 2469 O4 U F 2 215.425 31.478 6.659 1.00 44.08 O ATOM 2470 C5 U F 2 216.721 29.484 6.741 1.00 50.37 C ATOM 2471 C6 U F 2 216.883 28.324 7.385 1.00 52.63 C ATOM 2472 P U F 3 216.716 22.235 10.150 1.00 52.58 P ATOM 2473 OP1 U F 3 218.133 21.892 9.890 1.00 50.08 O ATOM 2474 OP2 U F 3 215.655 21.610 9.324 1.00 52.56 O ATOM 2475 O5' U F 3 216.382 22.021 11.691 1.00 47.99 O ATOM 2476 C5' U F 3 217.249 22.530 12.696 1.00 46.89 C ATOM 2477 C4' U F 3 216.544 22.587 14.022 1.00 42.04 C ATOM 2478 O4' U F 3 215.656 23.737 14.015 1.00 35.74 O ATOM 2479 C3' U F 3 215.679 21.373 14.323 1.00 40.34 C ATOM 2480 O3' U F 3 215.701 21.081 15.721 1.00 42.16 O ATOM 2481 C2' U F 3 214.278 21.818 13.921 1.00 33.33 C ATOM 2482 O2' U F 3 213.256 21.180 14.636 1.00 35.83 O ATOM 2483 C1' U F 3 214.321 23.320 14.208 1.00 35.99 C ATOM 2484 N1 U F 3 213.480 24.128 13.310 1.00 41.37 N ATOM 2485 C2 U F 3 212.278 24.620 13.788 1.00 39.57 C ATOM 2486 O2 U F 3 211.858 24.394 14.916 1.00 41.84 O ATOM 2487 N3 U F 3 211.558 25.362 12.883 1.00 40.66 N ATOM 2488 C4 U F 3 211.917 25.668 11.583 1.00 40.02 C ATOM 2489 O4 U F 3 211.156 26.366 10.927 1.00 36.79 O ATOM 2490 C5 U F 3 213.183 25.143 11.147 1.00 40.88 C ATOM 2491 C6 U F 3 213.905 24.407 12.019 1.00 43.23 C ATOM 2492 P U F 4 216.181 19.631 16.220 1.00 43.76 P ATOM 2493 OP1 U F 4 216.807 18.951 15.047 1.00 44.09 O ATOM 2494 OP2 U F 4 215.039 18.983 16.886 1.00 37.22 O ATOM 2495 O5' U F 4 217.292 19.996 17.296 1.00 53.50 O ATOM 2496 C5' U F 4 218.482 20.672 16.909 1.00 54.72 C ATOM 2497 C4' U F 4 219.538 20.542 17.968 1.00 55.29 C ATOM 2498 O4' U F 4 219.229 21.459 19.062 1.00 53.01 O ATOM 2499 C3' U F 4 219.638 19.155 18.593 1.00 56.69 C ATOM 2500 O3' U F 4 220.993 18.896 18.957 1.00 58.61 O ATOM 2501 C2' U F 4 218.784 19.294 19.852 1.00 56.20 C ATOM 2502 O2' U F 4 219.093 18.375 20.874 1.00 58.92 O ATOM 2503 C1' U F 4 219.087 20.732 20.266 1.00 53.20 C ATOM 2504 N1 U F 4 218.019 21.380 21.070 1.00 54.31 N ATOM 2505 C2 U F 4 218.403 21.910 22.285 1.00 50.86 C ATOM 2506 O2 U F 4 219.554 21.842 22.669 1.00 51.93 O ATOM 2507 N3 U F 4 217.418 22.528 23.015 1.00 45.79 N ATOM 2508 C4 U F 4 216.089 22.654 22.662 1.00 46.87 C ATOM 2509 O4 U F 4 215.311 23.238 23.421 1.00 45.03 O ATOM 2510 C5 U F 4 215.758 22.082 21.386 1.00 49.87 C ATOM 2511 C6 U F 4 216.707 21.481 20.649 1.00 53.08 C TER 2512 U F 4 ATOM 2513 P U G 1 205.318 37.001 -5.935 1.00 52.15 P ATOM 2514 OP1 U G 1 206.519 37.304 -5.102 1.00 49.29 O ATOM 2515 OP2 U G 1 204.524 35.775 -5.661 1.00 55.10 O ATOM 2516 O5' U G 1 204.368 38.270 -6.021 1.00 40.60 O ATOM 2517 C5' U G 1 203.650 38.730 -4.877 1.00 45.01 C ATOM 2518 C4' U G 1 203.000 40.062 -5.136 1.00 42.06 C ATOM 2519 O4' U G 1 201.907 39.889 -6.084 1.00 42.21 O ATOM 2520 C3' U G 1 202.390 40.747 -3.919 1.00 39.61 C ATOM 2521 O3' U G 1 202.532 42.159 -4.059 1.00 34.57 O ATOM 2522 C2' U G 1 200.915 40.381 -4.037 1.00 39.10 C ATOM 2523 O2' U G 1 200.046 41.238 -3.343 1.00 38.46 O ATOM 2524 C1' U G 1 200.745 40.492 -5.551 1.00 44.28 C ATOM 2525 N1 U G 1 199.548 39.815 -6.108 1.00 49.92 N ATOM 2526 C2 U G 1 199.392 38.437 -6.030 1.00 54.56 C ATOM 2527 O2 U G 1 200.193 37.690 -5.495 1.00 58.61 O ATOM 2528 N3 U G 1 198.247 37.947 -6.609 1.00 54.81 N ATOM 2529 C4 U G 1 197.249 38.659 -7.254 1.00 60.45 C ATOM 2530 O4 U G 1 196.257 38.070 -7.729 1.00 64.19 O ATOM 2531 C5 U G 1 197.488 40.075 -7.301 1.00 57.70 C ATOM 2532 C6 U G 1 198.597 40.586 -6.750 1.00 54.32 C ATOM 2533 P U G 2 203.756 42.910 -3.362 1.00 42.37 P ATOM 2534 OP1 U G 2 203.660 44.347 -3.723 1.00 46.19 O ATOM 2535 OP2 U G 2 204.988 42.153 -3.710 1.00 38.53 O ATOM 2536 O5' U G 2 203.424 42.719 -1.813 1.00 36.60 O ATOM 2537 C5' U G 2 202.154 43.093 -1.290 1.00 36.15 C ATOM 2538 C4' U G 2 202.260 43.370 0.176 1.00 36.40 C ATOM 2539 O4' U G 2 202.515 42.108 0.843 1.00 36.98 O ATOM 2540 C3' U G 2 203.413 44.293 0.549 1.00 39.67 C ATOM 2541 O3' U G 2 203.033 45.160 1.600 1.00 41.46 O ATOM 2542 C2' U G 2 204.517 43.350 1.024 1.00 37.42 C ATOM 2543 O2' U G 2 205.363 43.891 2.011 1.00 39.82 O ATOM 2544 C1' U G 2 203.729 42.167 1.564 1.00 35.30 C ATOM 2545 N1 U G 2 204.425 40.875 1.402 1.00 39.16 N ATOM 2546 C2 U G 2 204.586 40.126 2.553 1.00 38.56 C ATOM 2547 O2 U G 2 204.166 40.526 3.636 1.00 37.96 O ATOM 2548 N3 U G 2 205.229 38.919 2.378 1.00 33.91 N ATOM 2549 C4 U G 2 205.707 38.414 1.178 1.00 36.34 C ATOM 2550 O4 U G 2 206.258 37.312 1.163 1.00 33.87 O ATOM 2551 C5 U G 2 205.508 39.254 0.024 1.00 37.61 C ATOM 2552 C6 U G 2 204.891 40.433 0.176 1.00 38.43 C ATOM 2553 P U G 3 202.706 46.699 1.288 1.00 47.77 P ATOM 2554 OP1 U G 3 202.080 46.744 -0.053 1.00 45.71 O ATOM 2555 OP2 U G 3 203.949 47.470 1.533 1.00 46.87 O ATOM 2556 O5' U G 3 201.619 47.052 2.400 1.00 47.60 O ATOM 2557 C5' U G 3 200.262 46.651 2.242 1.00 46.46 C ATOM 2558 C4' U G 3 199.528 46.698 3.558 1.00 46.15 C ATOM 2559 O4' U G 3 199.946 45.566 4.376 1.00 39.51 O ATOM 2560 C3' U G 3 199.789 47.949 4.379 1.00 45.85 C ATOM 2561 O3' U G 3 198.601 48.323 5.066 1.00 53.41 O ATOM 2562 C2' U G 3 200.848 47.508 5.381 1.00 41.61 C ATOM 2563 O2' U G 3 200.818 48.223 6.598 1.00 47.69 O ATOM 2564 C1' U G 3 200.514 46.026 5.585 1.00 38.41 C ATOM 2565 N1 U G 3 201.691 45.173 5.887 1.00 38.92 N ATOM 2566 C2 U G 3 201.839 44.733 7.185 1.00 37.51 C ATOM 2567 O2 U G 3 201.048 45.030 8.058 1.00 40.93 O ATOM 2568 N3 U G 3 202.945 43.954 7.437 1.00 36.80 N ATOM 2569 C4 U G 3 203.898 43.566 6.521 1.00 38.55 C ATOM 2570 O4 U G 3 204.831 42.854 6.901 1.00 37.50 O ATOM 2571 C5 U G 3 203.692 44.059 5.186 1.00 34.49 C ATOM 2572 C6 U G 3 202.620 44.821 4.923 1.00 37.57 C ATOM 2573 P A G 4 197.890 49.721 4.728 1.00 55.93 P ATOM 2574 OP1 A G 4 198.624 50.320 3.584 1.00 58.77 O ATOM 2575 OP2 A G 4 197.812 50.488 6.009 1.00 54.59 O ATOM 2576 O5' A G 4 196.439 49.272 4.262 1.00 78.31 O ATOM 2577 C5' A G 4 196.115 49.180 2.884 1.00 80.43 C ATOM 2578 C4' A G 4 194.654 49.457 2.655 1.00 82.97 C ATOM 2579 O4' A G 4 193.880 48.289 3.034 1.00 83.26 O ATOM 2580 C3' A G 4 194.068 50.596 3.483 1.00 85.24 C ATOM 2581 O3' A G 4 194.255 51.869 2.885 1.00 86.29 O ATOM 2582 C2' A G 4 192.606 50.198 3.634 1.00 85.07 C ATOM 2583 O2' A G 4 191.878 50.513 2.452 1.00 87.01 O ATOM 2584 C1' A G 4 192.720 48.680 3.737 1.00 83.30 C ATOM 2585 N9 A G 4 192.857 48.220 5.131 1.00 81.36 N ATOM 2586 C8 A G 4 194.010 48.190 5.875 1.00 79.77 C ATOM 2587 N7 A G 4 193.855 47.705 7.080 1.00 78.78 N ATOM 2588 C5 A G 4 192.509 47.376 7.133 1.00 80.56 C ATOM 2589 C6 A G 4 191.721 46.812 8.154 1.00 79.49 C ATOM 2590 N6 A G 4 192.202 46.473 9.351 1.00 77.26 N ATOM 2591 N1 A G 4 190.409 46.608 7.891 1.00 82.96 N ATOM 2592 C2 A G 4 189.942 46.955 6.680 1.00 84.02 C ATOM 2593 N3 A G 4 190.586 47.492 5.640 1.00 82.60 N ATOM 2594 C4 A G 4 191.883 47.680 5.934 1.00 81.22 C TER 2595 A G 4 ATOM 2596 P U H 2 157.781 28.598 10.864 1.00 65.93 P ATOM 2597 OP1 U H 2 157.411 27.192 10.547 1.00 62.98 O ATOM 2598 OP2 U H 2 156.726 29.561 11.289 1.00 58.92 O ATOM 2599 O5' U H 2 159.016 28.637 11.881 1.00 58.68 O ATOM 2600 C5' U H 2 160.230 27.950 11.589 1.00 55.51 C ATOM 2601 C4' U H 2 161.042 27.708 12.838 1.00 50.64 C ATOM 2602 O4' U H 2 161.276 28.982 13.500 1.00 48.19 O ATOM 2603 C3' U H 2 160.388 26.793 13.871 1.00 46.32 C ATOM 2604 O3' U H 2 161.377 25.956 14.463 1.00 41.81 O ATOM 2605 C2' U H 2 159.841 27.771 14.923 1.00 44.25 C ATOM 2606 O2' U H 2 159.756 27.242 16.230 1.00 43.27 O ATOM 2607 C1' U H 2 160.847 28.913 14.847 1.00 48.54 C ATOM 2608 N1 U H 2 160.291 30.238 15.221 1.00 50.03 N ATOM 2609 C2 U H 2 160.848 30.922 16.303 1.00 48.14 C ATOM 2610 O2 U H 2 161.751 30.501 17.001 1.00 44.75 O ATOM 2611 N3 U H 2 160.285 32.142 16.560 1.00 50.97 N ATOM 2612 C4 U H 2 159.255 32.755 15.869 1.00 52.61 C ATOM 2613 O4 U H 2 158.858 33.870 16.239 1.00 51.33 O ATOM 2614 C5 U H 2 158.745 31.997 14.760 1.00 50.13 C ATOM 2615 C6 U H 2 159.267 30.799 14.484 1.00 50.06 C ATOM 2616 P U H 3 161.443 24.392 14.098 1.00 45.94 P ATOM 2617 OP1 U H 3 161.022 24.256 12.684 1.00 46.05 O ATOM 2618 OP2 U H 3 160.698 23.656 15.148 1.00 38.19 O ATOM 2619 O5' U H 3 162.996 24.058 14.233 1.00 45.83 O ATOM 2620 C5' U H 3 163.950 24.569 13.308 1.00 35.84 C ATOM 2621 C4' U H 3 165.345 24.445 13.876 1.00 36.05 C ATOM 2622 O4' U H 3 165.548 25.512 14.844 1.00 32.48 O ATOM 2623 C3' U H 3 165.610 23.137 14.612 1.00 38.13 C ATOM 2624 O3' U H 3 166.959 22.738 14.422 1.00 44.61 O ATOM 2625 C2' U H 3 165.403 23.503 16.077 1.00 34.91 C ATOM 2626 O2' U H 3 166.149 22.716 16.972 1.00 39.66 O ATOM 2627 C1' U H 3 165.840 24.965 16.117 1.00 32.35 C ATOM 2628 N1 U H 3 165.127 25.788 17.141 1.00 37.64 N ATOM 2629 C2 U H 3 165.787 26.139 18.324 1.00 36.31 C ATOM 2630 O2 U H 3 166.919 25.783 18.578 1.00 37.90 O ATOM 2631 N3 U H 3 165.066 26.900 19.223 1.00 35.78 N ATOM 2632 C4 U H 3 163.768 27.366 19.052 1.00 38.53 C ATOM 2633 O4 U H 3 163.256 28.070 19.935 1.00 35.67 O ATOM 2634 C5 U H 3 163.140 26.965 17.818 1.00 40.01 C ATOM 2635 C6 U H 3 163.828 26.218 16.931 1.00 41.96 C ATOM 2636 P U H 4 167.310 21.315 13.756 1.00 44.75 P ATOM 2637 OP1 U H 4 166.054 20.735 13.231 1.00 45.09 O ATOM 2638 OP2 U H 4 168.084 20.542 14.755 1.00 44.47 O ATOM 2639 O5' U H 4 168.248 21.744 12.551 1.00 39.53 O ATOM 2640 C5' U H 4 167.770 22.629 11.538 1.00 40.92 C ATOM 2641 C4' U H 4 168.695 22.639 10.339 1.00 44.60 C ATOM 2642 O4' U H 4 169.866 23.463 10.647 1.00 44.22 O ATOM 2643 C3' U H 4 169.233 21.267 9.935 1.00 49.51 C ATOM 2644 O3' U H 4 169.390 21.212 8.512 1.00 56.03 O ATOM 2645 C2' U H 4 170.606 21.233 10.611 1.00 49.59 C ATOM 2646 O2' U H 4 171.543 20.356 10.007 1.00 52.60 O ATOM 2647 C1' U H 4 171.042 22.693 10.491 1.00 45.07 C ATOM 2648 N1 U H 4 172.037 23.113 11.519 1.00 45.76 N ATOM 2649 C2 U H 4 173.284 23.605 11.097 1.00 44.45 C ATOM 2650 O2 U H 4 173.584 23.761 9.920 1.00 43.03 O ATOM 2651 N3 U H 4 174.159 23.940 12.110 1.00 41.27 N ATOM 2652 C4 U H 4 173.924 23.811 13.468 1.00 42.40 C ATOM 2653 O4 U H 4 174.784 24.147 14.279 1.00 41.82 O ATOM 2654 C5 U H 4 172.637 23.278 13.817 1.00 43.97 C ATOM 2655 C6 U H 4 171.762 22.948 12.857 1.00 45.07 C TER 2656 U H 4 HETATM 2657 O HOH A 401 205.307 36.510 34.463 1.00 49.20 O HETATM 2658 O HOH A 402 203.049 43.964 37.439 1.00 53.25 O HETATM 2659 O HOH A 403 227.085 29.105 46.363 1.00 37.79 O HETATM 2660 O HOH A 404 221.345 38.754 53.342 1.00 42.33 O HETATM 2661 O HOH A 405 219.265 38.418 51.725 1.00 45.50 O HETATM 2662 O HOH A 406 208.281 42.482 31.871 1.00 32.62 O HETATM 2663 O HOH A 407 207.882 39.118 37.215 1.00 29.89 O HETATM 2664 O HOH A 408 229.676 31.964 52.265 1.00 48.75 O HETATM 2665 O HOH A 409 219.160 43.596 38.314 1.00 42.49 O HETATM 2666 O HOH A 410 242.593 48.077 37.918 1.00 27.78 O HETATM 2667 O HOH A 411 212.242 30.549 52.112 1.00 27.31 O HETATM 2668 O HOH A 412 238.490 38.415 44.642 1.00 53.29 O HETATM 2669 O HOH A 413 217.960 42.716 51.160 1.00 31.67 O HETATM 2670 O HOH A 414 205.964 32.748 40.499 1.00 38.28 O HETATM 2671 O HOH A 415 211.042 44.138 35.355 1.00 42.33 O HETATM 2672 O HOH A 416 223.474 31.787 54.137 1.00 34.79 O HETATM 2673 O HOH A 417 206.089 30.378 37.169 1.00 41.98 O HETATM 2674 O HOH A 418 211.873 34.940 32.864 1.00 25.52 O HETATM 2675 O HOH A 419 216.749 33.997 55.559 1.00 38.90 O HETATM 2676 O HOH A 420 215.123 45.998 34.003 1.00 43.81 O HETATM 2677 O HOH A 421 203.573 44.098 40.346 1.00 44.96 O HETATM 2678 O HOH A 422 230.264 34.244 53.264 1.00 50.70 O HETATM 2679 O HOH A 423 220.771 41.614 32.494 1.00 42.95 O HETATM 2680 O HOH A 424 212.633 26.881 49.846 1.00 47.01 O HETATM 2681 O HOH A 425 207.659 27.191 44.457 1.00 57.77 O HETATM 2682 O HOH A 426 225.937 28.688 53.731 1.00 46.21 O HETATM 2683 O HOH A 427 228.023 37.255 33.948 1.00 47.38 O HETATM 2684 O HOH A 428 222.884 38.199 30.822 1.00 55.39 O HETATM 2685 O HOH A 429 226.867 40.124 35.344 1.00 37.15 O HETATM 2686 O HOH A 430 218.821 32.286 54.082 1.00 33.99 O HETATM 2687 O HOH A 431 231.386 29.176 41.536 1.00 48.05 O HETATM 2688 O HOH A 432 244.945 45.036 39.929 1.00 55.52 O HETATM 2689 O HOH A 433 221.448 35.848 56.776 1.00 45.66 O HETATM 2690 O HOH A 434 223.099 34.453 57.684 1.00 54.47 O HETATM 2691 O HOH A 435 204.532 38.676 32.560 1.00 51.95 O HETATM 2692 O HOH A 436 245.531 47.086 37.788 1.00 41.36 O HETATM 2693 O HOH A 437 242.633 44.261 35.911 1.00 47.72 O HETATM 2694 O HOH A 438 209.034 44.762 30.863 1.00 50.75 O HETATM 2695 O HOH A 439 213.971 25.425 43.417 1.00 47.45 O HETATM 2696 O HOH A 440 224.971 29.498 55.976 1.00 53.37 O HETATM 2697 O HOH A 441 210.744 25.775 42.646 1.00 50.57 O HETATM 2698 O HOH B 401 217.143 24.352 31.516 1.00 54.88 O HETATM 2699 O HOH B 402 231.473 26.379 17.005 1.00 59.86 O HETATM 2700 O HOH B 403 234.138 23.639 15.360 1.00 50.26 O HETATM 2701 O HOH B 404 207.939 27.969 35.369 1.00 30.62 O HETATM 2702 O HOH B 405 208.998 26.646 13.959 1.00 34.88 O HETATM 2703 O HOH B 406 205.089 34.502 34.066 1.00 47.61 O HETATM 2704 O HOH B 407 212.051 41.591 24.973 1.00 48.13 O HETATM 2705 O HOH B 408 211.126 30.876 13.554 1.00 36.63 O HETATM 2706 O HOH B 409 214.222 36.248 8.293 1.00 41.74 O HETATM 2707 O HOH B 410 203.854 38.516 28.429 1.00 44.25 O HETATM 2708 O HOH B 411 203.869 39.811 14.812 1.00 32.28 O HETATM 2709 O HOH B 412 214.979 25.493 25.221 1.00 38.71 O HETATM 2710 O HOH B 413 221.074 38.507 14.486 1.00 58.45 O HETATM 2711 O HOH B 414 222.683 34.710 11.007 1.00 60.57 O HETATM 2712 O HOH B 415 198.727 30.180 28.819 1.00 50.88 O HETATM 2713 O HOH B 416 206.011 40.339 13.239 1.00 42.63 O HETATM 2714 O HOH B 417 200.848 27.131 32.210 1.00 53.87 O HETATM 2715 O HOH B 418 218.162 23.400 25.619 1.00 48.70 O HETATM 2716 O HOH B 419 206.047 31.326 30.214 1.00 26.01 O HETATM 2717 O HOH B 420 215.556 42.492 29.059 1.00 45.06 O HETATM 2718 O HOH B 421 208.968 25.586 31.186 1.00 42.84 O HETATM 2719 O HOH B 422 217.688 39.598 7.810 1.00 52.38 O HETATM 2720 O HOH B 423 207.244 22.623 22.632 1.00 49.81 O HETATM 2721 O HOH B 424 205.359 26.201 14.416 1.00 51.07 O HETATM 2722 O HOH B 425 212.053 29.793 10.950 1.00 46.36 O HETATM 2723 O HOH B 426 222.446 30.635 30.193 1.00 53.41 O HETATM 2724 O HOH B 427 206.830 23.672 20.129 1.00 46.76 O HETATM 2725 O HOH B 428 200.528 26.576 29.467 1.00 44.33 O HETATM 2726 O HOH B 429 213.108 23.438 30.774 1.00 50.28 O HETATM 2727 O HOH B 430 205.796 19.587 13.941 1.00 56.17 O HETATM 2728 O HOH B 431 205.441 39.831 31.186 1.00 42.76 O HETATM 2729 O HOH B 432 220.530 24.074 27.838 1.00 64.88 O HETATM 2730 O HOH B 433 210.316 36.832 10.424 1.00 42.33 O HETATM 2731 O HOH B 434 203.771 24.166 31.628 1.00 57.40 O HETATM 2732 O HOH B 435 219.405 27.287 29.943 1.00 46.58 O HETATM 2733 O HOH B 436 205.899 37.334 9.681 1.00 59.09 O HETATM 2734 O HOH B 437 204.703 31.832 35.989 1.00 56.70 O HETATM 2735 O HOH B 438 211.013 18.046 18.749 1.00 60.75 O HETATM 2736 O HOH B 439 208.504 33.933 10.108 1.00 51.19 O HETATM 2737 O HOH B 440 207.072 35.354 9.071 1.00 55.41 O HETATM 2738 O HOH B 441 207.235 30.133 11.299 1.00 47.20 O HETATM 2739 O HOH B 442 211.777 36.767 8.125 1.00 51.83 O HETATM 2740 O HOH C 401 190.730 46.080 22.377 1.00 53.35 O HETATM 2741 O HOH C 402 194.005 40.121 -9.906 1.00 42.94 O HETATM 2742 O HOH C 403 186.291 48.421 -13.618 1.00 36.42 O HETATM 2743 O HOH C 404 185.191 43.821 -8.032 1.00 56.66 O HETATM 2744 O HOH C 405 203.378 42.953 10.136 1.00 38.69 O HETATM 2745 O HOH C 406 202.385 38.652 8.309 1.00 40.71 O HETATM 2746 O HOH C 407 184.985 42.664 21.495 1.00 33.18 O HETATM 2747 O HOH C 408 205.236 32.415 3.390 1.00 32.19 O HETATM 2748 O HOH C 409 204.383 37.032 13.431 1.00 26.86 O HETATM 2749 O HOH C 410 203.281 33.356 -2.482 1.00 49.21 O HETATM 2750 O HOH C 411 188.559 36.774 -3.545 1.00 50.30 O HETATM 2751 O HOH C 412 204.481 35.929 -2.622 1.00 49.88 O HETATM 2752 O HOH C 413 204.892 30.149 15.675 1.00 33.15 O HETATM 2753 O HOH C 414 185.296 35.441 17.334 1.00 22.87 O HETATM 2754 O HOH C 415 190.392 44.424 10.283 1.00 43.79 O HETATM 2755 O HOH C 416 205.724 32.678 14.296 1.00 27.35 O HETATM 2756 O HOH C 417 190.307 39.086 20.878 1.00 25.54 O HETATM 2757 O HOH C 418 196.643 30.026 0.640 1.00 50.39 O HETATM 2758 O HOH C 419 182.899 44.467 11.376 1.00 55.34 O HETATM 2759 O HOH C 420 202.394 51.324 8.678 1.00 62.43 O HETATM 2760 O HOH C 421 193.053 31.851 22.238 1.00 48.28 O HETATM 2761 O HOH C 422 188.310 44.692 18.544 1.00 43.13 O HETATM 2762 O HOH C 423 181.706 43.444 14.853 1.00 44.96 O HETATM 2763 O HOH C 424 186.686 46.627 14.611 1.00 46.28 O HETATM 2764 O HOH C 425 196.666 47.401 15.909 1.00 53.59 O HETATM 2765 O HOH C 426 187.245 36.422 23.675 1.00 48.94 O HETATM 2766 O HOH C 427 182.487 39.834 7.034 1.00 42.19 O HETATM 2767 O HOH C 428 184.158 42.321 8.889 1.00 45.97 O HETATM 2768 O HOH C 429 205.707 33.115 0.024 1.00 49.33 O HETATM 2769 O HOH C 430 198.892 46.005 15.057 1.00 45.56 O HETATM 2770 O HOH C 431 195.036 40.534 26.679 1.00 56.13 O HETATM 2771 O HOH C 432 193.065 30.983 0.991 1.00 51.79 O HETATM 2772 O HOH C 433 205.535 32.425 7.895 1.00 37.74 O HETATM 2773 O HOH C 434 204.497 29.591 0.487 1.00 41.65 O HETATM 2774 O HOH C 435 187.428 43.000 26.177 1.00 47.75 O HETATM 2775 O HOH C 436 195.500 30.894 -5.232 1.00 61.67 O HETATM 2776 O HOH C 437 193.913 44.068 25.189 1.00 47.21 O HETATM 2777 O HOH C 438 184.654 30.439 3.175 1.00 66.12 O HETATM 2778 O HOH C 439 198.166 51.015 10.644 1.00 55.41 O HETATM 2779 O HOH C 440 208.535 32.592 11.565 1.00 43.60 O HETATM 2780 O HOH C 441 186.024 38.886 25.106 1.00 45.16 O HETATM 2781 O HOH C 442 204.390 34.857 15.063 1.00 31.59 O HETATM 2782 O HOH C 443 185.871 46.988 -16.312 1.00 42.97 O HETATM 2783 O HOH C 444 206.288 30.884 1.327 1.00 49.72 O HETATM 2784 O HOH C 445 207.091 32.385 5.573 1.00 42.82 O HETATM 2785 O HOH C 446 181.868 45.184 16.214 1.00 59.79 O HETATM 2786 O HOH C 447 183.747 45.031 20.939 1.00 57.14 O HETATM 2787 O HOH C 448 191.106 30.262 0.992 1.00 54.10 O HETATM 2788 O HOH D 401 188.288 27.854 25.749 1.00 44.39 O HETATM 2789 O HOH D 402 160.764 38.395 18.011 1.00 40.60 O HETATM 2790 O HOH D 403 187.829 28.024 20.210 1.00 31.41 O HETATM 2791 O HOH D 404 165.654 23.714 7.856 1.00 43.45 O HETATM 2792 O HOH D 405 187.390 33.971 23.830 1.00 46.54 O HETATM 2793 O HOH D 406 168.405 40.305 26.589 1.00 27.22 O HETATM 2794 O HOH D 407 181.878 37.795 26.310 1.00 41.08 O HETATM 2795 O HOH D 408 165.519 32.124 20.214 1.00 46.57 O HETATM 2796 O HOH D 409 183.310 31.481 23.035 1.00 25.68 O HETATM 2797 O HOH D 410 164.062 22.671 19.049 1.00 44.92 O HETATM 2798 O HOH D 411 170.050 19.900 18.773 1.00 54.21 O HETATM 2799 O HOH D 412 183.574 25.871 19.604 1.00 41.78 O HETATM 2800 O HOH D 413 170.633 25.822 4.818 1.00 41.28 O HETATM 2801 O HOH D 414 163.264 36.245 24.601 1.00 32.62 O HETATM 2802 O HOH D 415 176.796 24.311 11.213 1.00 51.77 O HETATM 2803 O HOH D 416 185.144 26.661 27.712 1.00 56.26 O HETATM 2804 O HOH D 417 184.015 24.093 24.574 1.00 54.96 O HETATM 2805 O HOH D 418 167.091 27.429 25.184 1.00 38.67 O HETATM 2806 O HOH D 419 182.194 24.146 15.954 1.00 47.35 O HETATM 2807 O HOH D 420 182.730 26.512 28.315 1.00 46.57 O HETATM 2808 O HOH D 421 176.578 26.544 14.448 1.00 39.55 O HETATM 2809 O HOH D 422 182.547 29.402 30.340 1.00 50.15 O HETATM 2810 O HOH D 423 172.531 24.247 22.535 1.00 51.78 O HETATM 2811 O HOH D 424 163.613 38.279 21.692 1.00 38.84 O HETATM 2812 O HOH D 425 177.636 42.665 18.381 1.00 48.64 O HETATM 2813 O HOH D 426 157.230 34.030 10.753 1.00 59.32 O HETATM 2814 O HOH D 427 162.259 25.369 21.755 1.00 48.13 O HETATM 2815 O HOH D 428 161.549 32.560 5.650 1.00 61.57 O HETATM 2816 O HOH D 429 181.217 28.783 9.427 1.00 55.00 O HETATM 2817 O HOH D 430 162.780 36.347 22.283 1.00 51.97 O HETATM 2818 O HOH D 431 167.489 25.631 26.438 1.00 53.82 O HETATM 2819 O HOH D 432 161.626 23.259 23.436 1.00 56.92 O HETATM 2820 O HOH D 433 188.141 25.316 19.033 1.00 50.06 O HETATM 2821 O HOH D 434 182.835 37.441 28.593 1.00 49.78 O HETATM 2822 O HOH D 435 181.285 40.794 26.144 1.00 62.09 O HETATM 2823 O HOH D 436 179.068 44.154 20.382 1.00 56.17 O HETATM 2824 O HOH E 101 233.990 44.006 37.261 1.00 45.92 O HETATM 2825 O HOH E 102 228.672 47.788 33.876 1.00 42.74 O HETATM 2826 O HOH E 103 223.361 42.276 55.428 1.00 53.55 O HETATM 2827 O HOH E 104 223.202 50.385 42.927 1.00 66.33 O HETATM 2828 O HOH E 105 230.014 50.790 41.350 1.00 44.12 O HETATM 2829 O HOH E 106 228.602 34.875 55.128 1.00 57.91 O HETATM 2830 O HOH E 107 218.268 42.821 54.235 1.00 55.97 O HETATM 2831 O HOH F 101 222.550 19.214 17.761 1.00 36.96 O HETATM 2832 O HOH F 102 223.096 17.707 18.760 1.00 48.25 O HETATM 2833 O HOH F 103 221.541 23.626 7.415 1.00 69.84 O HETATM 2834 O HOH F 104 221.423 18.028 22.323 1.00 50.35 O HETATM 2835 O HOH G 101 206.885 36.044 -1.064 1.00 46.36 O HETATM 2836 O HOH G 102 192.737 48.991 10.641 1.00 57.16 O HETATM 2837 O HOH G 103 204.283 39.341 6.277 1.00 37.76 O HETATM 2838 O HOH G 104 199.742 44.039 -4.195 1.00 46.96 O HETATM 2839 O HOH H 101 166.055 27.697 21.565 1.00 29.63 O HETATM 2840 O HOH H 102 162.873 31.561 19.439 1.00 36.37 O HETATM 2841 O HOH H 103 160.388 28.577 19.784 1.00 51.32 O HETATM 2842 O HOH H 104 163.031 29.926 22.180 1.00 45.94 O HETATM 2843 O HOH H 105 170.625 19.147 14.260 1.00 52.04 O HETATM 2844 O HOH H 106 163.801 27.383 22.798 1.00 34.32 O HETATM 2845 O HOH H 107 172.551 21.286 7.274 1.00 61.05 O HETATM 2846 O HOH H 108 161.654 23.320 18.354 1.00 54.37 O HETATM 2847 O HOH H 109 160.189 25.973 19.516 1.00 58.00 O MASTER 797 0 0 12 24 0 0 6 2815 8 0 32 END
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Related entries of code: 6gc5
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
4ed5
RCSB PDB
PDBbind
11aa, >4ED5_2|Chains... *
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
6gc5
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
HuR C-terminal RRM3
Ligand Name
short ARE motifs derived from the c-fos 3鈥 UTR
EC.Number
E.C.-.-.-.-
Resolution
1.9(Å)
Affinity (Kd/Ki/IC50)
Kd=0.65uM
Release Year
2019
Protein/NA Sequence
Check fasta file
Primary Reference
(2019) Proc. Natl. Acad. Sci. U.S.A. Vol. 116: pp. 2935-2944
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):
Q15717
Entrez Gene ID
NCBI Entrez Gene ID:
1994
ASD
Information of known allosteric effects of PDB entries
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