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*** HYDROLASE/LIGASE 18-JAN-12 4DDG ***elNémo ID: 22012115434913873Job options:ID = 22012115434913873 JOBID = HYDROLASE/LIGASE 18-JAN-12 4DDG USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = on DORMSD = on NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER HYDROLASE/LIGASE 18-JAN-12 4DDG TITLE CRYSTAL STRUCTURE OF HUMAN OTUB1/UBCH5B~UB/UB COMPND MOL_ID: 1; COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D2, UBIQUITIN THIOESTERASE COMPND 3 OTUB1; COMPND 4 CHAIN: A, B, C, J, K, L; COMPND 5 SYNONYM: UBIQUITIN CARRIER PROTEIN D2, UBIQUITIN-CONJUGATING ENZYME COMPND 6 E2(17)KB 2, UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 2, UBIQUITIN- COMPND 7 PROTEIN LIGASE D2, DEUBIQUITINATING ENZYME OTUB1, OTU DOMAIN- COMPND 8 CONTAINING UBIQUITIN ALDEHYDE-BINDING PROTEIN 1, OTUBAIN-1, HOTU1, COMPND 9 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE OTUB1; COMPND 10 EC: 6.3.2.19, 3.4.19.12; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 2; COMPND 13 MOLECULE: POLYUBIQUITIN-C; COMPND 14 CHAIN: D, E, F, G, H, I, M, N, O, P, Q, R; COMPND 15 SYNONYM: UBIQUITIN; COMPND 16 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: E2, HSPC263, OTB1, OTU1, OTUB1, UBC4, UBC5B, UBCH4, UBCH5B, SOURCE 6 UBE2D2; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: UBC; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS INHIBITION, HYDROLASE-LIGASE COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR Y.C.JUANG,M.SANCHES,F.SICHERI REVDAT 4 15-NOV-17 4DDG 1 REMARK REVDAT 3 02-AUG-17 4DDG 1 SOURCE REVDAT 2 23-MAY-12 4DDG 1 ATOM HELIX REMARK SHEET REVDAT 1 22-FEB-12 4DDG 0 JRNL AUTH Y.C.JUANG,M.C.LANDRY,M.SANCHES,V.VITTAL,C.C.LEUNG, JRNL AUTH 2 D.F.CECCARELLI,A.R.MATEO,J.N.PRUNEDA,D.Y.MAO,R.K.SZILARD, JRNL AUTH 3 S.ORLICKY,M.MUNRO,P.S.BRZOVIC,R.E.KLEVIT,F.SICHERI, JRNL AUTH 4 D.DUROCHER JRNL TITL OTUB1 CO-OPTS LYS48-LINKED UBIQUITIN RECOGNITION TO SUPPRESS JRNL TITL 2 E2 ENZYME FUNCTION. JRNL REF MOL.CELL V. 45 384 2012 JRNL REFN ISSN 1097-2765 JRNL PMID 22325355 JRNL DOI 10.1016/J.MOLCEL.2012.01.011 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743) 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 : MLHL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.12 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 60385 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.236 REMARK 3 R VALUE (WORKING SET) : 0.233 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 3053 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 49.1268 - 9.2236 0.95 2612 129 0.1772 0.1684 REMARK 3 2 9.2236 - 7.3289 1.00 2659 133 0.1738 0.1991 REMARK 3 3 7.3289 - 6.4047 1.00 2607 171 0.2021 0.2688 REMARK 3 4 6.4047 - 5.8202 1.00 2627 147 0.2507 0.3206 REMARK 3 5 5.8202 - 5.4036 1.00 2654 140 0.2416 0.2714 REMARK 3 6 5.4036 - 5.0853 1.00 2610 138 0.2183 0.2733 REMARK 3 7 5.0853 - 4.8309 1.00 2598 145 0.2116 0.2576 REMARK 3 8 4.8309 - 4.6207 1.00 2591 141 0.1986 0.2747 REMARK 3 9 4.6207 - 4.4430 1.00 2641 125 0.2075 0.2526 REMARK 3 10 4.4430 - 4.2898 1.00 2635 130 0.2122 0.2698 REMARK 3 11 4.2898 - 4.1557 1.00 2564 138 0.2261 0.3140 REMARK 3 12 4.1557 - 4.0370 1.00 2619 135 0.2450 0.2774 REMARK 3 13 4.0370 - 3.9307 1.00 2607 154 0.2465 0.3017 REMARK 3 14 3.9307 - 3.8349 0.99 2564 141 0.2818 0.3376 REMARK 3 15 3.8349 - 3.7477 1.00 2588 143 0.2748 0.3567 REMARK 3 16 3.7477 - 3.6680 1.00 2621 145 0.2930 0.3455 REMARK 3 17 3.6680 - 3.5946 1.00 2610 126 0.3216 0.4092 REMARK 3 18 3.5946 - 3.5268 1.00 2582 139 0.3247 0.3750 REMARK 3 19 3.5268 - 3.4639 1.00 2601 124 0.3282 0.4114 REMARK 3 20 3.4639 - 3.4052 0.99 2597 128 0.3697 0.4129 REMARK 3 21 3.4052 - 3.3502 1.00 2578 145 0.3718 0.4259 REMARK 3 22 3.3502 - 3.2987 0.99 2567 136 0.3765 0.3961 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.86 REMARK 3 K_SOL : 0.31 REMARK 3 B_SOL : 110.3 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.260 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) : -4.77940 REMARK 3 B22 (A**2) : 3.13020 REMARK 3 B33 (A**2) : 1.64920 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -2.56620 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 27126 REMARK 3 ANGLE : 0.938 36660 REMARK 3 CHIRALITY : 0.070 4032 REMARK 3 PLANARITY : 0.005 4782 REMARK 3 DIHEDRAL : 16.511 10326 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 24 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ -1:147) REMARK 3 ORIGIN FOR THE GROUP (A): -58.9105 -14.4602 9.1567 REMARK 3 T TENSOR REMARK 3 T11: 0.9419 T22: 1.6336 REMARK 3 T33: 0.4728 T12: 0.1492 REMARK 3 T13: 0.1658 T23: 0.0061 REMARK 3 L TENSOR REMARK 3 L11: 4.0807 L22: 4.9080 REMARK 3 L33: 3.3389 L12: -0.5462 REMARK 3 L13: 0.3255 L23: 0.9439 REMARK 3 S TENSOR REMARK 3 S11: -0.4190 S12: -0.8663 S13: -0.2664 REMARK 3 S21: 0.5422 S22: 0.5825 S23: -0.4760 REMARK 3 S31: 0.4796 S32: 1.8712 S33: -0.2026 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271) REMARK 3 ORIGIN FOR THE GROUP (A): -22.9339 9.8754 17.1484 REMARK 3 T TENSOR REMARK 3 T11: 1.9324 T22: 1.0264 REMARK 3 T33: 1.8534 T12: 0.3414 REMARK 3 T13: -1.6001 T23: -0.2334 REMARK 3 L TENSOR REMARK 3 L11: 0.4574 L22: 0.6582 REMARK 3 L33: 0.2849 L12: -0.3889 REMARK 3 L13: 0.2519 L23: -0.4136 REMARK 3 S TENSOR REMARK 3 S11: -1.0755 S12: -0.8252 S13: 1.4552 REMARK 3 S21: 1.0662 S22: -0.0036 S23: -0.6423 REMARK 3 S31: -1.5783 S32: -0.1924 S33: -0.4898 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ -1:147) REMARK 3 ORIGIN FOR THE GROUP (A): -36.0794 -9.0058 -9.4012 REMARK 3 T TENSOR REMARK 3 T11: 0.1894 T22: 0.3064 REMARK 3 T33: 0.2552 T12: -0.0208 REMARK 3 T13: -0.0578 T23: 0.0251 REMARK 3 L TENSOR REMARK 3 L11: 3.0780 L22: 5.1069 REMARK 3 L33: 4.0853 L12: -0.5796 REMARK 3 L13: 0.4705 L23: 0.1521 REMARK 3 S TENSOR REMARK 3 S11: -0.2898 S12: -0.1099 S13: 0.2845 REMARK 3 S21: 0.5541 S22: -0.2047 S23: -0.2387 REMARK 3 S31: 0.1862 S32: 0.1770 S33: 0.5010 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1025:1271) REMARK 3 ORIGIN FOR THE GROUP (A): -54.3319 13.8772 -42.3539 REMARK 3 T TENSOR REMARK 3 T11: 0.4201 T22: 0.4143 REMARK 3 T33: 0.7802 T12: 0.1292 REMARK 3 T13: 0.1367 T23: 0.3035 REMARK 3 L TENSOR REMARK 3 L11: 2.3740 L22: 1.5529 REMARK 3 L33: 3.3143 L12: 0.0549 REMARK 3 L13: -0.3174 L23: -0.5322 REMARK 3 S TENSOR REMARK 3 S11: 0.0598 S12: 0.2840 S13: 0.8090 REMARK 3 S21: 0.3717 S22: 0.4770 S23: 0.5065 REMARK 3 S31: -0.9640 S32: -0.5032 S33: -0.2843 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ -1:147) REMARK 3 ORIGIN FOR THE GROUP (A): -70.4904 41.0497 20.0663 REMARK 3 T TENSOR REMARK 3 T11: 0.4495 T22: 0.3232 REMARK 3 T33: 0.1768 T12: -0.0327 REMARK 3 T13: 0.4084 T23: 0.3431 REMARK 3 L TENSOR REMARK 3 L11: 3.3648 L22: 3.1954 REMARK 3 L33: 3.8301 L12: -0.0770 REMARK 3 L13: -0.9824 L23: 0.3238 REMARK 3 S TENSOR REMARK 3 S11: 0.2069 S12: -0.2358 S13: -0.2104 REMARK 3 S21: -0.2764 S22: 0.0882 S23: 0.0213 REMARK 3 S31: 0.3718 S32: 0.2477 S33: -0.0352 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 1025:1271) REMARK 3 ORIGIN FOR THE GROUP (A): -45.2023 55.8861 -10.6272 REMARK 3 T TENSOR REMARK 3 T11: 0.3769 T22: 0.3228 REMARK 3 T33: 0.0702 T12: 0.0108 REMARK 3 T13: 0.1025 T23: 0.0232 REMARK 3 L TENSOR REMARK 3 L11: 3.4590 L22: 2.1460 REMARK 3 L33: 3.1508 L12: 0.6662 REMARK 3 L13: 0.2895 L23: -0.3961 REMARK 3 S TENSOR REMARK 3 S11: -0.4352 S12: 0.3382 S13: -0.5676 REMARK 3 S21: -0.0313 S22: 0.1473 S23: -0.1456 REMARK 3 S31: -0.1264 S32: 0.0008 S33: 0.2978 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): -1.9547 -6.9973 21.3419 REMARK 3 T TENSOR REMARK 3 T11: 1.1241 T22: 1.5070 REMARK 3 T33: 2.3957 T12: 0.0984 REMARK 3 T13: -0.4724 T23: 0.8255 REMARK 3 L TENSOR REMARK 3 L11: 2.9494 L22: 2.0690 REMARK 3 L33: 3.7310 L12: -1.1823 REMARK 3 L13: 0.6937 L23: 0.7830 REMARK 3 S TENSOR REMARK 3 S11: -1.1612 S12: -0.0634 S13: 0.9771 REMARK 3 S21: 0.2854 S22: -0.8336 S23: -1.6717 REMARK 3 S31: -1.2501 S32: 1.0278 S33: 1.1179 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): -56.1234 -3.5318 -63.2212 REMARK 3 T TENSOR REMARK 3 T11: 0.2464 T22: 0.7711 REMARK 3 T33: 0.5682 T12: 0.0024 REMARK 3 T13: 0.1207 T23: 0.1695 REMARK 3 L TENSOR REMARK 3 L11: 4.1383 L22: 2.7618 REMARK 3 L33: 3.9570 L12: 0.6512 REMARK 3 L13: 1.7296 L23: -0.1012 REMARK 3 S TENSOR REMARK 3 S11: -0.1268 S12: 0.4125 S13: -0.9753 REMARK 3 S21: -0.3865 S22: -0.1439 S23: -0.6125 REMARK 3 S31: 0.5277 S32: 1.4668 S33: 0.3010 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): -31.1846 35.1420 -21.2524 REMARK 3 T TENSOR REMARK 3 T11: 1.0833 T22: 1.5423 REMARK 3 T33: 1.3303 T12: 0.2070 REMARK 3 T13: 0.4293 T23: -0.4930 REMARK 3 L TENSOR REMARK 3 L11: 1.1608 L22: 2.1124 REMARK 3 L33: 3.7189 L12: 0.1223 REMARK 3 L13: -0.5518 L23: 1.9358 REMARK 3 S TENSOR REMARK 3 S11: 0.0978 S12: 0.9546 S13: -1.1516 REMARK 3 S21: -0.2420 S22: -0.0184 S23: -0.9743 REMARK 3 S31: 1.1829 S32: 1.0309 S33: 0.2848 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'G' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): -31.3618 -12.9096 26.6998 REMARK 3 T TENSOR REMARK 3 T11: 1.1977 T22: 2.4350 REMARK 3 T33: 1.0369 T12: 0.7024 REMARK 3 T13: -0.0969 T23: -0.1644 REMARK 3 L TENSOR REMARK 3 L11: 3.4597 L22: 2.2868 REMARK 3 L33: 0.1409 L12: 1.2149 REMARK 3 L13: -0.6522 L23: -0.0546 REMARK 3 S TENSOR REMARK 3 S11: -0.7744 S12: -1.9095 S13: -0.5916 REMARK 3 S21: 1.0345 S22: 0.2460 S23: -0.2977 REMARK 3 S31: -0.7385 S32: -1.5042 S33: 0.0758 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): -98.1222 47.7609 41.5723 REMARK 3 T TENSOR REMARK 3 T11: 0.1259 T22: 0.7978 REMARK 3 T33: 0.3539 T12: 0.0235 REMARK 3 T13: -0.1548 T23: -0.0938 REMARK 3 L TENSOR REMARK 3 L11: 1.6924 L22: 3.6849 REMARK 3 L33: 4.8960 L12: 0.4790 REMARK 3 L13: 0.4395 L23: -0.1495 REMARK 3 S TENSOR REMARK 3 S11: 0.1682 S12: -0.4019 S13: 0.3535 REMARK 3 S21: -0.0156 S22: -0.2645 S23: 0.0404 REMARK 3 S31: 0.7237 S32: -0.3778 S33: -0.0191 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'I' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): -92.0553 -15.4750 -6.5831 REMARK 3 T TENSOR REMARK 3 T11: 0.3589 T22: 0.5334 REMARK 3 T33: 0.9240 T12: -0.2197 REMARK 3 T13: 0.2470 T23: -0.1681 REMARK 3 L TENSOR REMARK 3 L11: 5.2007 L22: 2.5706 REMARK 3 L33: 2.9649 L12: 0.4020 REMARK 3 L13: -2.0017 L23: 0.9270 REMARK 3 S TENSOR REMARK 3 S11: -0.5086 S12: -0.1912 S13: -1.7469 REMARK 3 S21: -0.0422 S22: -0.2682 S23: 0.5953 REMARK 3 S31: 0.8081 S32: -0.2966 S33: 0.4323 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'J' AND (RESSEQ -1:147) REMARK 3 ORIGIN FOR THE GROUP (A): 9.8367 -13.3747 -80.2532 REMARK 3 T TENSOR REMARK 3 T11: 0.4471 T22: 1.3932 REMARK 3 T33: 1.1017 T12: 0.1171 REMARK 3 T13: 0.0701 T23: 0.2691 REMARK 3 L TENSOR REMARK 3 L11: 3.5900 L22: 3.8721 REMARK 3 L33: 2.1568 L12: 0.9315 REMARK 3 L13: 0.7416 L23: -0.3553 REMARK 3 S TENSOR REMARK 3 S11: 0.0085 S12: 0.0968 S13: -0.1019 REMARK 3 S21: -0.0482 S22: -0.2311 S23: 0.0552 REMARK 3 S31: 0.0100 S32: -0.5721 S33: 0.1969 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'K' AND (RESSEQ -1:147) REMARK 3 ORIGIN FOR THE GROUP (A): -13.0959 -8.5163 -61.5791 REMARK 3 T TENSOR REMARK 3 T11: 0.4178 T22: 0.6658 REMARK 3 T33: 0.5706 T12: 0.0522 REMARK 3 T13: -0.1560 T23: 0.0719 REMARK 3 L TENSOR REMARK 3 L11: 2.5507 L22: 4.7121 REMARK 3 L33: 3.7965 L12: 0.2475 REMARK 3 L13: 0.9859 L23: -0.2889 REMARK 3 S TENSOR REMARK 3 S11: -0.3027 S12: -0.1047 S13: 0.4058 REMARK 3 S21: -0.1071 S22: -0.0958 S23: -0.4224 REMARK 3 S31: -0.7795 S32: 0.0552 S33: 0.3695 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'J' AND (RESSEQ 1025:1271) REMARK 3 ORIGIN FOR THE GROUP (A): -26.9404 10.6581 -87.4801 REMARK 3 T TENSOR REMARK 3 T11: 0.7401 T22: 0.4566 REMARK 3 T33: 0.5977 T12: -0.1225 REMARK 3 T13: -0.3361 T23: 0.1184 REMARK 3 L TENSOR REMARK 3 L11: 2.2311 L22: 4.1969 REMARK 3 L33: 3.0654 L12: -0.6458 REMARK 3 L13: -0.6011 L23: 0.0221 REMARK 3 S TENSOR REMARK 3 S11: -0.1486 S12: 0.1742 S13: 0.4181 REMARK 3 S21: -0.3245 S22: -0.0793 S23: -0.2555 REMARK 3 S31: -0.7100 S32: 0.4860 S33: 0.2204 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'K' AND (RESSEQ 1025:1271) REMARK 3 ORIGIN FOR THE GROUP (A): 4.8728 13.3960 -27.3988 REMARK 3 T TENSOR REMARK 3 T11: 0.2054 T22: 1.3101 REMARK 3 T33: 1.9997 T12: 0.0083 REMARK 3 T13: -0.8520 T23: -0.7413 REMARK 3 L TENSOR REMARK 3 L11: 1.1821 L22: 1.1696 REMARK 3 L33: 2.0293 L12: 0.6002 REMARK 3 L13: 0.3648 L23: -0.3797 REMARK 3 S TENSOR REMARK 3 S11: -0.4755 S12: -0.5348 S13: 1.2691 REMARK 3 S21: 0.2594 S22: -0.0378 S23: -0.7963 REMARK 3 S31: -0.5607 S32: 0.8415 S33: -2.2680 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESSEQ -1:147) REMARK 3 ORIGIN FOR THE GROUP (A): 21.5250 41.5020 -93.1211 REMARK 3 T TENSOR REMARK 3 T11: 0.4329 T22: 1.3269 REMARK 3 T33: 1.2664 T12: -0.1012 REMARK 3 T13: 0.0871 T23: -0.4034 REMARK 3 L TENSOR REMARK 3 L11: 2.9624 L22: 3.4864 REMARK 3 L33: 3.6670 L12: 0.3984 REMARK 3 L13: -1.2620 L23: -1.5030 REMARK 3 S TENSOR REMARK 3 S11: -0.0964 S12: 0.2017 S13: 0.4343 REMARK 3 S21: -0.4078 S22: -0.0979 S23: 0.1691 REMARK 3 S31: 0.1852 S32: -0.5454 S33: 0.0982 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESSEQ 1025:1271) REMARK 3 ORIGIN FOR THE GROUP (A): -4.0500 56.3017 -61.9920 REMARK 3 T TENSOR REMARK 3 T11: 0.3013 T22: 0.4407 REMARK 3 T33: 0.1486 T12: -0.0186 REMARK 3 T13: 0.0032 T23: -0.1350 REMARK 3 L TENSOR REMARK 3 L11: 2.9861 L22: 2.9704 REMARK 3 L33: 2.4779 L12: -0.4222 REMARK 3 L13: 0.2713 L23: 0.1775 REMARK 3 S TENSOR REMARK 3 S11: -0.4380 S12: -0.3978 S13: -0.3993 REMARK 3 S21: 0.2289 S22: 0.3170 S23: -0.3195 REMARK 3 S31: -0.3312 S32: 0.2766 S33: 0.0830 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'M' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): -47.1965 -7.0626 -92.1962 REMARK 3 T TENSOR REMARK 3 T11: 1.1272 T22: 0.7074 REMARK 3 T33: 0.8545 T12: -0.1738 REMARK 3 T13: -0.1982 T23: -0.2381 REMARK 3 L TENSOR REMARK 3 L11: 4.4789 L22: 1.6485 REMARK 3 L33: 3.2077 L12: 0.6505 REMARK 3 L13: -0.6803 L23: -1.0844 REMARK 3 S TENSOR REMARK 3 S11: -0.8028 S12: -0.5462 S13: 0.1312 REMARK 3 S21: 0.1359 S22: -0.1253 S23: 0.4774 REMARK 3 S31: 0.5436 S32: -0.5721 S33: 0.8372 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'N' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): 6.9972 -4.6255 -7.2317 REMARK 3 T TENSOR REMARK 3 T11: 0.4776 T22: 1.6826 REMARK 3 T33: 1.5323 T12: 0.1036 REMARK 3 T13: -0.3664 T23: -0.4340 REMARK 3 L TENSOR REMARK 3 L11: 1.8357 L22: 0.9924 REMARK 3 L33: 2.3652 L12: 0.4300 REMARK 3 L13: 0.4348 L23: -0.2124 REMARK 3 S TENSOR REMARK 3 S11: -0.1334 S12: -0.4520 S13: -0.8932 REMARK 3 S21: 0.0405 S22: -0.5350 S23: 0.2396 REMARK 3 S31: -0.0706 S32: -1.2376 S33: -0.2957 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'O' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): -18.0514 35.1583 -52.1277 REMARK 3 T TENSOR REMARK 3 T11: 1.0656 T22: 1.4918 REMARK 3 T33: 1.3305 T12: -0.0351 REMARK 3 T13: 0.4237 T23: 0.4972 REMARK 3 L TENSOR REMARK 3 L11: 1.9495 L22: 3.0763 REMARK 3 L33: 4.2498 L12: 0.0930 REMARK 3 L13: -0.0782 L23: -1.2824 REMARK 3 S TENSOR REMARK 3 S11: 0.0980 S12: -1.6565 S13: -1.4953 REMARK 3 S21: 0.5155 S22: -0.1893 S23: 0.7928 REMARK 3 S31: 1.4231 S32: -0.4887 S33: 0.1002 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'P' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): -17.7606 -11.2334 -97.5855 REMARK 3 T TENSOR REMARK 3 T11: 0.6757 T22: 0.8090 REMARK 3 T33: 0.8103 T12: 0.0025 REMARK 3 T13: 0.0015 T23: 0.2399 REMARK 3 L TENSOR REMARK 3 L11: 4.7753 L22: 3.2471 REMARK 3 L33: 2.7322 L12: -0.6057 REMARK 3 L13: 1.2368 L23: 0.0320 REMARK 3 S TENSOR REMARK 3 S11: 0.3415 S12: -0.5625 S13: -1.1439 REMARK 3 S21: -0.5090 S22: -0.1719 S23: -0.1326 REMARK 3 S31: 0.0438 S32: 1.1875 S33: -0.0963 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'Q' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): 49.3083 47.2202-114.8069 REMARK 3 T TENSOR REMARK 3 T11: 0.3084 T22: 0.9125 REMARK 3 T33: 0.7586 T12: -0.3418 REMARK 3 T13: -0.3720 T23: 0.3104 REMARK 3 L TENSOR REMARK 3 L11: 1.0545 L22: 2.0616 REMARK 3 L33: 4.5475 L12: -0.5268 REMARK 3 L13: 0.7334 L23: 0.7660 REMARK 3 S TENSOR REMARK 3 S11: -0.1528 S12: 0.7491 S13: 0.7884 REMARK 3 S21: -0.1670 S22: 0.1941 S23: 0.2822 REMARK 3 S31: 0.4024 S32: -0.4081 S33: 0.0718 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'R' AND (RESSEQ 1:76) REMARK 3 ORIGIN FOR THE GROUP (A): 42.9515 -14.7086 -64.1468 REMARK 3 T TENSOR REMARK 3 T11: 0.5016 T22: 0.5736 REMARK 3 T33: 0.9028 T12: 0.0060 REMARK 3 T13: 0.1770 T23: 0.0414 REMARK 3 L TENSOR REMARK 3 L11: 4.8175 L22: 4.0405 REMARK 3 L33: 3.2463 L12: 0.7614 REMARK 3 L13: -1.8775 L23: -0.8993 REMARK 3 S TENSOR REMARK 3 S11: -0.6080 S12: 0.1884 S13: -1.8303 REMARK 3 S21: 0.1067 S22: 0.0333 S23: -0.3532 REMARK 3 S31: 0.4703 S32: -0.2867 S33: 0.4716 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 4 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'G' REMARK 3 SELECTION : CHAIN 'H' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: CHAIN 'G' REMARK 3 SELECTION : CHAIN 'I' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: CHAIN 'G' REMARK 3 SELECTION : CHAIN 'Q' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: CHAIN 'G' REMARK 3 SELECTION : CHAIN 'P' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: CHAIN 'G' REMARK 3 SELECTION : CHAIN 'R' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'B' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 1191 REMARK 3 RMSD : 0.003 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'C' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 1191 REMARK 3 RMSD : 0.003 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'J' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 1191 REMARK 3 RMSD : 0.002 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'K' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 1191 REMARK 3 RMSD : 0.002 REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'L' AND (RESSEQ 1:150 ) AND (NOT REMARK 3 ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 1191 REMARK 3 RMSD : 0.003 REMARK 3 NCS GROUP : 3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'B' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 2026 REMARK 3 RMSD : 0.002 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'C' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 2026 REMARK 3 RMSD : 0.002 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'J' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 2026 REMARK 3 RMSD : 0.001 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'K' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 2026 REMARK 3 RMSD : 0.002 REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 SELECTION : CHAIN 'L' AND (RESSEQ 1025:1271 ) AND REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D) REMARK 3 ATOM PAIRS NUMBER : 2026 REMARK 3 RMSD : 0.002 REMARK 3 NCS GROUP : 4 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'D' REMARK 3 SELECTION : CHAIN 'E' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: CHAIN 'D' REMARK 3 SELECTION : CHAIN 'F' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: CHAIN 'D' REMARK 3 SELECTION : CHAIN 'N' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: CHAIN 'D' REMARK 3 SELECTION : CHAIN 'M' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: CHAIN 'D' REMARK 3 SELECTION : CHAIN 'O' REMARK 3 ATOM PAIRS NUMBER : 601 REMARK 3 RMSD : 0.001 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4DDG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-12. REMARK 100 THE DEPOSITION ID IS D_1000070190. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-DEC-11 REMARK 200 TEMPERATURE (KELVIN) : 198.25 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CLSI REMARK 200 BEAMLINE : 08ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949 REMARK 200 MONOCHROMATOR : ACCEL/BRUKER DOUBLE CRYSTAL REMARK 200 MONOCHROMATOR (DCM) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60387 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.299 REMARK 200 RESOLUTION RANGE LOW (A) : 49.290 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.50 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 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: PDB ENTRY 2ESK AND 2ZFY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.28 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG1500, 0.1 M SPG, PH 7.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 52.46400 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 300 REMARK: THE BIOLOGICAL COMPLEX DEFINED BY THE AUTHOR CONSISTS OF: REMARK 300 COMPLEX 1: CHAIN H, CHAIN E, RESIDUES 1 TO 147 OF CHAIN C, REMARK 300 AND RESIDUES 1025-1271 OF CHAIN B; REMARK 300 COMPLEX 2: CHAIN G, CHAIN D, RESIDUES 1 TO 147 OF CHAIN B, REMARK 300 AND RESIDUES 1025-1271 OF CHAIN A; REMARK 300 COMPLEX 3: CHAIN I, CHAIN F, RESIDUES 1 TO 147 OF CHAIN A, REMARK 300 AND RESIDUES 1025-1271 OF CHAIN C; REMARK 300 COMPLEX 4: CHAIN Q, CHAIN N, RESIDUES 1 TO 147 OF CHAIN L, REMARK 300 AND RESIDUES 1025-1271 OF CHAIN K; REMARK 300 COMPLEX 5: CHAIN P, CHAIN M, RESIDUES 1 TO 147 OF CHAIN K, REMARK 300 AND RESIDUES 1025-1271 OF CHAIN J; REMARK 300 COMPLEX 6: CHAIN R, CHAIN O, RESIDUES 1 TO 147 OF CHAIN J, REMARK 300 AND RESIDUES 1025-1271 OF CHAIN L 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 13330 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 63270 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 13140 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 63600 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L, M, N, O, P, Q, R 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 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 OG SER L 85 O GLY Q 76 1.85 REMARK 500 OG SER C 85 O GLY H 76 1.93 REMARK 500 NZ LYS A 1188 OE1 GLN N 31 2.05 REMARK 500 OE1 GLU B 1195 NH2 ARG E 42 2.16 REMARK 500 OE1 GLU K 1195 NH2 ARG N 42 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO A1250 C - N - CA ANGL. DEV. = -9.1 DEGREES REMARK 500 PRO C1250 C - N - CA ANGL. DEV. = -9.1 DEGREES REMARK 500 PRO J1250 C - N - CA ANGL. DEV. = -9.0 DEGREES REMARK 500 PRO K1250 C - N - CA ANGL. DEV. = -9.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 HIS A 75 138.76 -176.39 REMARK 500 ARG A 90 -85.09 -123.27 REMARK 500 PRO A 113 -175.96 -67.54 REMARK 500 THR A 129 -69.25 -96.91 REMARK 500 TYR A1026 -37.50 -38.74 REMARK 500 GLU A1150 -70.15 -57.32 REMARK 500 GLN A1206 -61.18 -94.80 REMARK 500 VAL A1208 -59.79 -128.69 REMARK 500 CYS A1212 -3.90 70.26 REMARK 500 ASP A1237 -82.11 -128.44 REMARK 500 HIS B 75 138.82 -176.36 REMARK 500 ARG B 90 -85.11 -123.20 REMARK 500 PRO B 113 -175.95 -67.65 REMARK 500 THR B 129 -69.23 -96.96 REMARK 500 SER B 150 -78.49 -86.41 REMARK 500 ALA B1025 -58.29 -25.91 REMARK 500 GLU B1150 -70.12 -57.34 REMARK 500 GLN B1206 -61.07 -94.84 REMARK 500 VAL B1208 -59.80 -128.62 REMARK 500 CYS B1212 -3.94 70.27 REMARK 500 ASP B1237 -82.18 -128.45 REMARK 500 HIS C 75 138.78 -176.41 REMARK 500 ARG C 90 -85.15 -123.22 REMARK 500 PRO C 113 -175.98 -67.51 REMARK 500 THR C 129 -69.25 -96.93 REMARK 500 GLU C1150 -70.12 -57.27 REMARK 500 GLN C1206 -61.10 -94.86 REMARK 500 VAL C1208 -59.82 -128.70 REMARK 500 CYS C1212 -3.88 70.27 REMARK 500 ASP C1237 -82.22 -128.38 REMARK 500 ARG D 72 -72.95 -55.92 REMARK 500 ARG E 72 -72.91 -55.85 REMARK 500 ARG F 72 -73.05 -55.82 REMARK 500 HIS J 75 138.69 -176.39 REMARK 500 ARG J 90 -85.09 -123.25 REMARK 500 PRO J 113 -175.93 -67.64 REMARK 500 THR J 129 -69.22 -96.95 REMARK 500 SER J 150 -86.18 -85.10 REMARK 500 ALA J1025 -57.21 -18.89 REMARK 500 GLU J1150 -70.04 -57.33 REMARK 500 GLN J1206 -61.10 -94.84 REMARK 500 VAL J1208 -59.74 -128.69 REMARK 500 CYS J1212 -3.91 70.34 REMARK 500 ASP J1237 -82.11 -128.36 REMARK 500 HIS K 75 138.75 -176.42 REMARK 500 ARG K 90 -85.10 -123.26 REMARK 500 PRO K 113 -175.96 -67.71 REMARK 500 THR K 129 -69.27 -96.89 REMARK 500 SER K 150 -83.90 -85.31 REMARK 500 ALA K1025 -57.58 -20.84 REMARK 500 REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 PHE A 1249 PRO A 1250 115.25 REMARK 500 PHE B 1249 PRO B 1250 115.29 REMARK 500 PHE C 1249 PRO C 1250 115.28 REMARK 500 PHE J 1249 PRO J 1250 115.25 REMARK 500 PHE K 1249 PRO K 1250 115.28 REMARK 500 PHE L 1249 PRO L 1250 115.25 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4DDI RELATED DB: PDB DBREF 4DDG A 1 147 UNP P62837 UB2D2_HUMAN 1 147 DBREF 4DDG A 1025 1271 UNP Q96FW1 OTUB1_HUMAN 25 271 DBREF 4DDG B 1 147 UNP P62837 UB2D2_HUMAN 1 147 DBREF 4DDG B 1025 1271 UNP Q96FW1 OTUB1_HUMAN 25 271 DBREF 4DDG C 1 147 UNP P62837 UB2D2_HUMAN 1 147 DBREF 4DDG C 1025 1271 UNP Q96FW1 OTUB1_HUMAN 25 271 DBREF 4DDG D 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG E 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG F 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG G 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG H 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG I 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG J 1 147 UNP P62837 UB2D2_HUMAN 1 147 DBREF 4DDG J 1025 1271 UNP Q96FW1 OTUB1_HUMAN 25 271 DBREF 4DDG K 1 147 UNP P62837 UB2D2_HUMAN 1 147 DBREF 4DDG K 1025 1271 UNP Q96FW1 OTUB1_HUMAN 25 271 DBREF 4DDG L 1 147 UNP P62837 UB2D2_HUMAN 1 147 DBREF 4DDG L 1025 1271 UNP Q96FW1 OTUB1_HUMAN 25 271 DBREF 4DDG M 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG N 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG O 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG P 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG Q 1 76 UNP P0CG48 UBC_HUMAN 1 76 DBREF 4DDG R 1 76 UNP P0CG48 UBC_HUMAN 1 76 SEQADV 4DDG GLY A -1 UNP P62837 EXPRESSION TAG SEQADV 4DDG ALA A 0 UNP P62837 EXPRESSION TAG SEQADV 4DDG SER A 85 UNP P62837 CYS 85 CONFLICT SEQADV 4DDG GLY A 148 UNP Q96FW1 LINKER SEQADV 4DDG GLY A 149 UNP Q96FW1 LINKER SEQADV 4DDG SER A 150 UNP Q96FW1 LINKER SEQADV 4DDG SER A 1091 UNP Q96FW1 CYS 91 CONFLICT SEQADV 4DDG GLY B -1 UNP P62837 EXPRESSION TAG SEQADV 4DDG ALA B 0 UNP P62837 EXPRESSION TAG SEQADV 4DDG SER B 85 UNP P62837 CYS 85 CONFLICT SEQADV 4DDG GLY B 148 UNP Q96FW1 LINKER SEQADV 4DDG GLY B 149 UNP Q96FW1 LINKER SEQADV 4DDG SER B 150 UNP Q96FW1 LINKER SEQADV 4DDG SER B 1091 UNP Q96FW1 CYS 91 CONFLICT SEQADV 4DDG GLY C -1 UNP P62837 EXPRESSION TAG SEQADV 4DDG ALA C 0 UNP P62837 EXPRESSION TAG SEQADV 4DDG SER C 85 UNP P62837 CYS 85 CONFLICT SEQADV 4DDG GLY C 148 UNP Q96FW1 LINKER SEQADV 4DDG GLY C 149 UNP Q96FW1 LINKER SEQADV 4DDG SER C 150 UNP Q96FW1 LINKER SEQADV 4DDG SER C 1091 UNP Q96FW1 CYS 91 CONFLICT SEQADV 4DDG GLY J -1 UNP P62837 EXPRESSION TAG SEQADV 4DDG ALA J 0 UNP P62837 EXPRESSION TAG SEQADV 4DDG SER J 85 UNP P62837 CYS 85 CONFLICT SEQADV 4DDG GLY J 148 UNP Q96FW1 LINKER SEQADV 4DDG GLY J 149 UNP Q96FW1 LINKER SEQADV 4DDG SER J 150 UNP Q96FW1 LINKER SEQADV 4DDG SER J 1091 UNP Q96FW1 CYS 91 CONFLICT SEQADV 4DDG GLY K -1 UNP P62837 EXPRESSION TAG SEQADV 4DDG ALA K 0 UNP P62837 EXPRESSION TAG SEQADV 4DDG SER K 85 UNP P62837 CYS 85 CONFLICT SEQADV 4DDG GLY K 148 UNP Q96FW1 LINKER SEQADV 4DDG GLY K 149 UNP Q96FW1 LINKER SEQADV 4DDG SER K 150 UNP Q96FW1 LINKER SEQADV 4DDG SER K 1091 UNP Q96FW1 CYS 91 CONFLICT SEQADV 4DDG GLY L -1 UNP P62837 EXPRESSION TAG SEQADV 4DDG ALA L 0 UNP P62837 EXPRESSION TAG SEQADV 4DDG SER L 85 UNP P62837 CYS 85 CONFLICT SEQADV 4DDG GLY L 148 UNP Q96FW1 LINKER SEQADV 4DDG GLY L 149 UNP Q96FW1 LINKER SEQADV 4DDG SER L 150 UNP Q96FW1 LINKER SEQADV 4DDG SER L 1091 UNP Q96FW1 CYS 91 CONFLICT SEQRES 1 A 399 GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN SEQRES 2 A 399 ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY SEQRES 3 A 399 PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE SEQRES 4 A 399 MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE SEQRES 5 A 399 PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS SEQRES 6 A 399 PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO SEQRES 7 A 399 ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU SEQRES 8 A 399 ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL SEQRES 9 A 399 LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO SEQRES 10 A 399 ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS SEQRES 11 A 399 THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP SEQRES 12 A 399 THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU SEQRES 13 A 399 ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE SEQRES 14 A 399 ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SEQRES 15 A 399 SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE SEQRES 16 A 399 TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER SEQRES 17 A 399 TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR SEQRES 18 A 399 ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP SEQRES 19 A 399 ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA SEQRES 20 A 399 LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU SEQRES 21 A 399 PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU SEQRES 22 A 399 ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU SEQRES 23 A 399 LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU SEQRES 24 A 399 VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN SEQRES 25 A 399 ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY SEQRES 26 A 399 ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO SEQRES 27 A 399 MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU SEQRES 28 A 399 ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET SEQRES 29 A 399 ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE SEQRES 30 A 399 PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG SEQRES 31 A 399 PRO GLY HIS TYR ASP ILE LEU TYR LYS SEQRES 1 B 399 GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN SEQRES 2 B 399 ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY SEQRES 3 B 399 PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE SEQRES 4 B 399 MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE SEQRES 5 B 399 PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS SEQRES 6 B 399 PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO SEQRES 7 B 399 ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU SEQRES 8 B 399 ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL SEQRES 9 B 399 LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO SEQRES 10 B 399 ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS SEQRES 11 B 399 THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP SEQRES 12 B 399 THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU SEQRES 13 B 399 ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE SEQRES 14 B 399 ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SEQRES 15 B 399 SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE SEQRES 16 B 399 TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER SEQRES 17 B 399 TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR SEQRES 18 B 399 ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP SEQRES 19 B 399 ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA SEQRES 20 B 399 LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU SEQRES 21 B 399 PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU SEQRES 22 B 399 ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU SEQRES 23 B 399 LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU SEQRES 24 B 399 VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN SEQRES 25 B 399 ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY SEQRES 26 B 399 ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO SEQRES 27 B 399 MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU SEQRES 28 B 399 ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET SEQRES 29 B 399 ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE SEQRES 30 B 399 PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG SEQRES 31 B 399 PRO GLY HIS TYR ASP ILE LEU TYR LYS SEQRES 1 C 399 GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN SEQRES 2 C 399 ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY SEQRES 3 C 399 PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE SEQRES 4 C 399 MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE SEQRES 5 C 399 PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS SEQRES 6 C 399 PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO SEQRES 7 C 399 ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU SEQRES 8 C 399 ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL SEQRES 9 C 399 LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO SEQRES 10 C 399 ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS SEQRES 11 C 399 THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP SEQRES 12 C 399 THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU SEQRES 13 C 399 ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE SEQRES 14 C 399 ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SEQRES 15 C 399 SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE SEQRES 16 C 399 TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER SEQRES 17 C 399 TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR SEQRES 18 C 399 ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP SEQRES 19 C 399 ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA SEQRES 20 C 399 LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU SEQRES 21 C 399 PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU SEQRES 22 C 399 ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU SEQRES 23 C 399 LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU SEQRES 24 C 399 VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN SEQRES 25 C 399 ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY SEQRES 26 C 399 ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO SEQRES 27 C 399 MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU SEQRES 28 C 399 ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET SEQRES 29 C 399 ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE SEQRES 30 C 399 PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG SEQRES 31 C 399 PRO GLY HIS TYR ASP ILE LEU TYR LYS SEQRES 1 D 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 D 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 D 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 D 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 D 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 D 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 E 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 E 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 E 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 E 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 E 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 E 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 F 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 F 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 F 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 F 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 F 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 F 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 G 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 G 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 G 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 G 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 G 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 G 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 H 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 H 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 H 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 H 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 H 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 H 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 I 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 I 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 I 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 I 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 I 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 I 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 J 399 GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN SEQRES 2 J 399 ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY SEQRES 3 J 399 PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE SEQRES 4 J 399 MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE SEQRES 5 J 399 PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS SEQRES 6 J 399 PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO SEQRES 7 J 399 ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU SEQRES 8 J 399 ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL SEQRES 9 J 399 LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO SEQRES 10 J 399 ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS SEQRES 11 J 399 THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP SEQRES 12 J 399 THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU SEQRES 13 J 399 ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE SEQRES 14 J 399 ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SEQRES 15 J 399 SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE SEQRES 16 J 399 TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER SEQRES 17 J 399 TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR SEQRES 18 J 399 ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP SEQRES 19 J 399 ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA SEQRES 20 J 399 LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU SEQRES 21 J 399 PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU SEQRES 22 J 399 ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU SEQRES 23 J 399 LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU SEQRES 24 J 399 VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN SEQRES 25 J 399 ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY SEQRES 26 J 399 ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO SEQRES 27 J 399 MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU SEQRES 28 J 399 ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET SEQRES 29 J 399 ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE SEQRES 30 J 399 PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG SEQRES 31 J 399 PRO GLY HIS TYR ASP ILE LEU TYR LYS SEQRES 1 K 399 GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN SEQRES 2 K 399 ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY SEQRES 3 K 399 PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE SEQRES 4 K 399 MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE SEQRES 5 K 399 PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS SEQRES 6 K 399 PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO SEQRES 7 K 399 ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU SEQRES 8 K 399 ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL SEQRES 9 K 399 LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO SEQRES 10 K 399 ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS SEQRES 11 K 399 THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP SEQRES 12 K 399 THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU SEQRES 13 K 399 ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE SEQRES 14 K 399 ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SEQRES 15 K 399 SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE SEQRES 16 K 399 TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER SEQRES 17 K 399 TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR SEQRES 18 K 399 ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP SEQRES 19 K 399 ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA SEQRES 20 K 399 LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU SEQRES 21 K 399 PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU SEQRES 22 K 399 ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU SEQRES 23 K 399 LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU SEQRES 24 K 399 VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN SEQRES 25 K 399 ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY SEQRES 26 K 399 ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO SEQRES 27 K 399 MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU SEQRES 28 K 399 ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET SEQRES 29 K 399 ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE SEQRES 30 K 399 PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG SEQRES 31 K 399 PRO GLY HIS TYR ASP ILE LEU TYR LYS SEQRES 1 L 399 GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN SEQRES 2 L 399 ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY SEQRES 3 L 399 PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE SEQRES 4 L 399 MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE SEQRES 5 L 399 PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS SEQRES 6 L 399 PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO SEQRES 7 L 399 ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU SEQRES 8 L 399 ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL SEQRES 9 L 399 LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO SEQRES 10 L 399 ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS SEQRES 11 L 399 THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP SEQRES 12 L 399 THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU SEQRES 13 L 399 ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE SEQRES 14 L 399 ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SEQRES 15 L 399 SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE SEQRES 16 L 399 TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER SEQRES 17 L 399 TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR SEQRES 18 L 399 ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP SEQRES 19 L 399 ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA SEQRES 20 L 399 LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU SEQRES 21 L 399 PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU SEQRES 22 L 399 ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU SEQRES 23 L 399 LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU SEQRES 24 L 399 VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN SEQRES 25 L 399 ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY SEQRES 26 L 399 ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO SEQRES 27 L 399 MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU SEQRES 28 L 399 ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET SEQRES 29 L 399 ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE SEQRES 30 L 399 PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG SEQRES 31 L 399 PRO GLY HIS TYR ASP ILE LEU TYR LYS SEQRES 1 M 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 M 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 M 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 M 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 M 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 M 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 N 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 N 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 N 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 N 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 N 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 N 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 O 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 O 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 O 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 O 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 O 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 O 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 P 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 P 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 P 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 P 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 P 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 P 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 Q 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 Q 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 Q 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 Q 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 Q 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 Q 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 R 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 R 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 R 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 R 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 R 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 R 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY HELIX 1 1 GLY A -1 ASP A 16 1 18 HELIX 2 2 LEU A 86 ARG A 90 5 5 HELIX 3 3 THR A 98 ASP A 112 1 15 HELIX 4 4 VAL A 120 ASP A 130 1 11 HELIX 5 5 ASP A 130 ALA A 146 1 17 HELIX 6 6 SER A 150 ASN A 1045 1 22 HELIX 7 7 VAL A 1056 TYR A 1061 1 6 HELIX 8 8 ASP A 1065 TYR A 1079 1 15 HELIX 9 9 ASN A 1090 LEU A 1104 1 15 HELIX 10 10 ASP A 1107 GLN A 1128 1 22 HELIX 11 11 THR A 1131 LYS A 1151 1 21 HELIX 12 12 SER A 1154 ASN A 1163 1 10 HELIX 13 13 ASP A 1164 GLU A 1186 1 23 HELIX 14 14 GLU A 1186 GLU A 1191 1 6 HELIX 15 15 HIS A 1192 ILE A 1194 5 3 HELIX 16 16 THR A 1199 VAL A 1208 1 10 HELIX 17 17 ASP A 1216 SER A 1228 1 13 HELIX 18 18 ALA B 0 ASP B 16 1 17 HELIX 19 19 LEU B 86 ARG B 90 5 5 HELIX 20 20 THR B 98 ASP B 112 1 15 HELIX 21 21 VAL B 120 ASP B 130 1 11 HELIX 22 22 ASP B 130 ALA B 146 1 17 HELIX 23 23 SER B 150 ASN B 1045 1 22 HELIX 24 24 VAL B 1056 TYR B 1061 1 6 HELIX 25 25 ASP B 1065 TYR B 1079 1 15 HELIX 26 26 ASN B 1090 LEU B 1104 1 15 HELIX 27 27 ASP B 1107 GLN B 1128 1 22 HELIX 28 28 THR B 1131 LYS B 1151 1 21 HELIX 29 29 SER B 1154 ASN B 1163 1 10 HELIX 30 30 ASP B 1164 GLU B 1186 1 23 HELIX 31 31 GLU B 1186 GLU B 1191 1 6 HELIX 32 32 HIS B 1192 ILE B 1194 5 3 HELIX 33 33 THR B 1199 VAL B 1208 1 10 HELIX 34 34 ASP B 1216 SER B 1228 1 13 HELIX 35 35 ALA C 0 ASP C 16 1 17 HELIX 36 36 LEU C 86 ARG C 90 5 5 HELIX 37 37 THR C 98 ASP C 112 1 15 HELIX 38 38 VAL C 120 ASP C 130 1 11 HELIX 39 39 ASP C 130 ALA C 146 1 17 HELIX 40 40 SER C 150 ASN C 1045 1 22 HELIX 41 41 VAL C 1056 TYR C 1061 1 6 HELIX 42 42 ASP C 1065 TYR C 1079 1 15 HELIX 43 43 ASN C 1090 LEU C 1104 1 15 HELIX 44 44 ASP C 1107 GLN C 1128 1 22 HELIX 45 45 THR C 1131 LYS C 1151 1 21 HELIX 46 46 SER C 1154 ASN C 1163 1 10 HELIX 47 47 ASP C 1164 GLU C 1186 1 23 HELIX 48 48 GLU C 1186 GLU C 1191 1 6 HELIX 49 49 HIS C 1192 ILE C 1194 5 3 HELIX 50 50 THR C 1199 VAL C 1208 1 10 HELIX 51 51 ASP C 1216 SER C 1228 1 13 HELIX 52 52 THR D 22 GLY D 35 1 14 HELIX 53 53 PRO D 37 ASP D 39 5 3 HELIX 54 54 THR E 22 GLY E 35 1 14 HELIX 55 55 PRO E 37 ASP E 39 5 3 HELIX 56 56 THR F 22 GLY F 35 1 14 HELIX 57 57 PRO F 37 ASP F 39 5 3 HELIX 58 58 THR G 22 GLY G 35 1 14 HELIX 59 59 PRO G 37 ASP G 39 5 3 HELIX 60 60 THR G 55 ASN G 60 5 6 HELIX 61 61 THR H 22 GLY H 35 1 14 HELIX 62 62 PRO H 37 ASP H 39 5 3 HELIX 63 63 THR H 55 ASN H 60 5 6 HELIX 64 64 THR I 22 GLY I 35 1 14 HELIX 65 65 PRO I 37 ASP I 39 5 3 HELIX 66 66 THR I 55 ASN I 60 5 6 HELIX 67 67 ALA J 0 ASP J 16 1 17 HELIX 68 68 LEU J 86 ARG J 90 5 5 HELIX 69 69 THR J 98 ASP J 112 1 15 HELIX 70 70 VAL J 120 ASP J 130 1 11 HELIX 71 71 ASP J 130 ALA J 146 1 17 HELIX 72 72 SER J 150 ASN J 1045 1 22 HELIX 73 73 VAL J 1056 TYR J 1061 1 6 HELIX 74 74 ASP J 1065 TYR J 1079 1 15 HELIX 75 75 ASN J 1090 LEU J 1104 1 15 HELIX 76 76 ASP J 1107 GLN J 1128 1 22 HELIX 77 77 THR J 1131 LYS J 1151 1 21 HELIX 78 78 SER J 1154 ASN J 1163 1 10 HELIX 79 79 ASP J 1164 GLU J 1186 1 23 HELIX 80 80 GLU J 1186 GLU J 1191 1 6 HELIX 81 81 HIS J 1192 ILE J 1194 5 3 HELIX 82 82 THR J 1199 VAL J 1208 1 10 HELIX 83 83 ASP J 1216 SER J 1228 1 13 HELIX 84 84 ALA K 0 ASP K 16 1 17 HELIX 85 85 LEU K 86 ARG K 90 5 5 HELIX 86 86 THR K 98 ASP K 112 1 15 HELIX 87 87 VAL K 120 ASP K 130 1 11 HELIX 88 88 ASP K 130 ALA K 146 1 17 HELIX 89 89 SER K 150 ASN K 1045 1 22 HELIX 90 90 VAL K 1056 TYR K 1061 1 6 HELIX 91 91 ASP K 1065 TYR K 1079 1 15 HELIX 92 92 ASN K 1090 LEU K 1104 1 15 HELIX 93 93 ASP K 1107 GLN K 1128 1 22 HELIX 94 94 THR K 1131 LYS K 1151 1 21 HELIX 95 95 SER K 1154 ASN K 1163 1 10 HELIX 96 96 ASP K 1164 GLU K 1186 1 23 HELIX 97 97 GLU K 1186 GLU K 1191 1 6 HELIX 98 98 HIS K 1192 ILE K 1194 5 3 HELIX 99 99 THR K 1199 VAL K 1208 1 10 HELIX 100 100 ASP K 1216 SER K 1228 1 13 HELIX 101 101 ALA L 0 ASP L 16 1 17 HELIX 102 102 LEU L 86 ARG L 90 5 5 HELIX 103 103 THR L 98 ASP L 112 1 15 HELIX 104 104 VAL L 120 ASP L 130 1 11 HELIX 105 105 ASP L 130 ALA L 146 1 17 HELIX 106 106 ALA L 1025 ASN L 1045 1 21 HELIX 107 107 VAL L 1056 TYR L 1061 1 6 HELIX 108 108 ASP L 1065 TYR L 1079 1 15 HELIX 109 109 ASN L 1090 LEU L 1104 1 15 HELIX 110 110 ASP L 1107 GLN L 1128 1 22 HELIX 111 111 THR L 1131 LYS L 1151 1 21 HELIX 112 112 SER L 1154 ASN L 1163 1 10 HELIX 113 113 ASP L 1164 GLU L 1186 1 23 HELIX 114 114 GLU L 1186 GLU L 1191 1 6 HELIX 115 115 HIS L 1192 ILE L 1194 5 3 HELIX 116 116 THR L 1199 VAL L 1208 1 10 HELIX 117 117 ASP L 1216 SER L 1228 1 13 HELIX 118 118 THR M 22 GLY M 35 1 14 HELIX 119 119 PRO M 37 ASP M 39 5 3 HELIX 120 120 THR N 22 GLY N 35 1 14 HELIX 121 121 PRO N 37 ASP N 39 5 3 HELIX 122 122 THR O 22 GLY O 35 1 14 HELIX 123 123 PRO O 37 ASP O 39 5 3 HELIX 124 124 THR P 22 GLY P 35 1 14 HELIX 125 125 PRO P 37 ASP P 39 5 3 HELIX 126 126 THR P 55 ASN P 60 5 6 HELIX 127 127 THR Q 22 GLY Q 35 1 14 HELIX 128 128 PRO Q 37 ASP Q 39 5 3 HELIX 129 129 THR Q 55 ASN Q 60 5 6 HELIX 130 130 THR R 22 GLY R 35 1 14 HELIX 131 131 PRO R 37 ASP R 39 5 3 HELIX 132 132 THR R 55 ASN R 60 5 6 SHEET 1 A 4 CYS A 21 VAL A 26 0 SHEET 2 A 4 ASP A 29 MET A 38 -1 O THR A 36 N SER A 22 SHEET 3 A 4 VAL A 49 HIS A 55 -1 O PHE A 50 N ILE A 37 SHEET 4 A 4 LYS A 66 PHE A 69 -1 O LYS A 66 N HIS A 55 SHEET 1 B 6 LEU A1052 GLU A1053 0 SHEET 2 B 6 TYR A1081 ARG A1083 -1 O ILE A1082 N LEU A1052 SHEET 3 B 6 HIS A1265 TYR A1270 -1 O ILE A1268 N ARG A1083 SHEET 4 B 6 TYR A1258 ARG A1262 -1 N ARG A1262 O HIS A1265 SHEET 5 B 6 GLN A1232 TYR A1235 1 N GLU A1234 O LEU A1259 SHEET 6 B 6 PRO A1246 ILE A1248 -1 O HIS A1247 N VAL A1233 SHEET 1 C 4 CYS B 21 VAL B 26 0 SHEET 2 C 4 ASP B 29 MET B 38 -1 O THR B 36 N SER B 22 SHEET 3 C 4 VAL B 49 HIS B 55 -1 O PHE B 50 N ILE B 37 SHEET 4 C 4 LYS B 66 PHE B 69 -1 O LYS B 66 N HIS B 55 SHEET 1 D 6 LEU B1052 GLU B1053 0 SHEET 2 D 6 TYR B1081 ARG B1083 -1 O ILE B1082 N LEU B1052 SHEET 3 D 6 HIS B1265 TYR B1270 -1 O ILE B1268 N ARG B1083 SHEET 4 D 6 TYR B1258 ARG B1262 -1 N ARG B1262 O HIS B1265 SHEET 5 D 6 GLN B1232 TYR B1235 1 N GLU B1234 O LEU B1259 SHEET 6 D 6 PRO B1246 ILE B1248 -1 O HIS B1247 N VAL B1233 SHEET 1 E 4 CYS C 21 VAL C 26 0 SHEET 2 E 4 ASP C 29 MET C 38 -1 O THR C 36 N SER C 22 SHEET 3 E 4 VAL C 49 HIS C 55 -1 O PHE C 50 N ILE C 37 SHEET 4 E 4 LYS C 66 PHE C 69 -1 O LYS C 66 N HIS C 55 SHEET 1 F 6 LEU C1052 GLU C1053 0 SHEET 2 F 6 TYR C1081 ARG C1083 -1 O ILE C1082 N LEU C1052 SHEET 3 F 6 HIS C1265 TYR C1270 -1 O ILE C1268 N ARG C1083 SHEET 4 F 6 TYR C1258 ARG C1262 -1 N ARG C1262 O HIS C1265 SHEET 5 F 6 GLN C1232 TYR C1235 1 N GLU C1234 O LEU C1259 SHEET 6 F 6 PRO C1246 ILE C1248 -1 O HIS C1247 N VAL C1233 SHEET 1 G 5 THR D 12 GLU D 16 0 SHEET 2 G 5 GLN D 2 THR D 7 -1 N VAL D 5 O ILE D 13 SHEET 3 G 5 THR D 66 LEU D 71 1 O LEU D 67 N PHE D 4 SHEET 4 G 5 GLN D 41 PHE D 45 -1 N ARG D 42 O VAL D 70 SHEET 5 G 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45 SHEET 1 H 5 THR E 12 GLU E 16 0 SHEET 2 H 5 GLN E 2 THR E 7 -1 N VAL E 5 O ILE E 13 SHEET 3 H 5 THR E 66 LEU E 71 1 O LEU E 67 N PHE E 4 SHEET 4 H 5 GLN E 41 PHE E 45 -1 N ARG E 42 O VAL E 70 SHEET 5 H 5 LYS E 48 GLN E 49 -1 O LYS E 48 N PHE E 45 SHEET 1 I 5 THR F 12 GLU F 16 0 SHEET 2 I 5 GLN F 2 THR F 7 -1 N VAL F 5 O ILE F 13 SHEET 3 I 5 THR F 66 LEU F 71 1 O LEU F 67 N PHE F 4 SHEET 4 I 5 GLN F 41 PHE F 45 -1 N ARG F 42 O VAL F 70 SHEET 5 I 5 LYS F 48 GLN F 49 -1 O LYS F 48 N PHE F 45 SHEET 1 J 5 THR G 12 GLU G 16 0 SHEET 2 J 5 GLN G 2 LYS G 6 -1 N VAL G 5 O ILE G 13 SHEET 3 J 5 THR G 66 LEU G 71 1 O LEU G 67 N PHE G 4 SHEET 4 J 5 GLN G 41 PHE G 45 -1 N ARG G 42 O VAL G 70 SHEET 5 J 5 LYS G 48 GLN G 49 -1 O LYS G 48 N PHE G 45 SHEET 1 K 5 THR H 12 GLU H 16 0 SHEET 2 K 5 GLN H 2 LYS H 6 -1 N VAL H 5 O ILE H 13 SHEET 3 K 5 THR H 66 LEU H 71 1 O LEU H 67 N PHE H 4 SHEET 4 K 5 GLN H 41 PHE H 45 -1 N ARG H 42 O VAL H 70 SHEET 5 K 5 LYS H 48 GLN H 49 -1 O LYS H 48 N PHE H 45 SHEET 1 L 5 THR I 12 GLU I 16 0 SHEET 2 L 5 GLN I 2 LYS I 6 -1 N VAL I 5 O ILE I 13 SHEET 3 L 5 THR I 66 LEU I 71 1 O LEU I 67 N PHE I 4 SHEET 4 L 5 GLN I 41 PHE I 45 -1 N ARG I 42 O VAL I 70 SHEET 5 L 5 LYS I 48 GLN I 49 -1 O LYS I 48 N PHE I 45 SHEET 1 M 4 CYS J 21 VAL J 26 0 SHEET 2 M 4 ASP J 29 MET J 38 -1 O THR J 36 N SER J 22 SHEET 3 M 4 VAL J 49 HIS J 55 -1 O PHE J 50 N ILE J 37 SHEET 4 M 4 LYS J 66 PHE J 69 -1 O LYS J 66 N HIS J 55 SHEET 1 N 6 LEU J1052 GLU J1053 0 SHEET 2 N 6 TYR J1081 ARG J1083 -1 O ILE J1082 N LEU J1052 SHEET 3 N 6 HIS J1265 TYR J1270 -1 O ILE J1268 N ARG J1083 SHEET 4 N 6 TYR J1258 ARG J1262 -1 N ARG J1262 O HIS J1265 SHEET 5 N 6 GLN J1232 TYR J1235 1 N GLU J1234 O LEU J1259 SHEET 6 N 6 PRO J1246 ILE J1248 -1 O HIS J1247 N VAL J1233 SHEET 1 O 4 CYS K 21 VAL K 26 0 SHEET 2 O 4 ASP K 29 MET K 38 -1 O THR K 36 N SER K 22 SHEET 3 O 4 VAL K 49 HIS K 55 -1 O PHE K 50 N ILE K 37 SHEET 4 O 4 LYS K 66 PHE K 69 -1 O LYS K 66 N HIS K 55 SHEET 1 P 6 LEU K1052 GLU K1053 0 SHEET 2 P 6 TYR K1081 ARG K1083 -1 O ILE K1082 N LEU K1052 SHEET 3 P 6 HIS K1265 TYR K1270 -1 O ILE K1268 N ARG K1083 SHEET 4 P 6 TYR K1258 ARG K1262 -1 N ARG K1262 O HIS K1265 SHEET 5 P 6 GLN K1232 TYR K1235 1 N GLU K1234 O LEU K1259 SHEET 6 P 6 PRO K1246 ILE K1248 -1 O HIS K1247 N VAL K1233 SHEET 1 Q 4 CYS L 21 VAL L 26 0 SHEET 2 Q 4 ASP L 29 MET L 38 -1 O THR L 36 N SER L 22 SHEET 3 Q 4 VAL L 49 HIS L 55 -1 O PHE L 50 N ILE L 37 SHEET 4 Q 4 LYS L 66 PHE L 69 -1 O LYS L 66 N HIS L 55 SHEET 1 R 6 LEU L1052 GLU L1053 0 SHEET 2 R 6 TYR L1081 ARG L1083 -1 O ILE L1082 N LEU L1052 SHEET 3 R 6 HIS L1265 TYR L1270 -1 O ILE L1268 N ARG L1083 SHEET 4 R 6 TYR L1258 ARG L1262 -1 N ARG L1262 O HIS L1265 SHEET 5 R 6 GLN L1232 TYR L1235 1 N GLU L1234 O LEU L1259 SHEET 6 R 6 PRO L1246 ILE L1248 -1 O HIS L1247 N VAL L1233 SHEET 1 S 5 THR M 12 GLU M 16 0 SHEET 2 S 5 GLN M 2 THR M 7 -1 N VAL M 5 O ILE M 13 SHEET 3 S 5 THR M 66 LEU M 71 1 O LEU M 67 N PHE M 4 SHEET 4 S 5 GLN M 41 PHE M 45 -1 N ARG M 42 O VAL M 70 SHEET 5 S 5 LYS M 48 GLN M 49 -1 O LYS M 48 N PHE M 45 SHEET 1 T 5 THR N 12 GLU N 16 0 SHEET 2 T 5 GLN N 2 THR N 7 -1 N VAL N 5 O ILE N 13 SHEET 3 T 5 THR N 66 LEU N 71 1 O LEU N 67 N PHE N 4 SHEET 4 T 5 GLN N 41 PHE N 45 -1 N ARG N 42 O VAL N 70 SHEET 5 T 5 LYS N 48 GLN N 49 -1 O LYS N 48 N PHE N 45 SHEET 1 U 5 THR O 12 GLU O 16 0 SHEET 2 U 5 GLN O 2 THR O 7 -1 N VAL O 5 O ILE O 13 SHEET 3 U 5 THR O 66 LEU O 71 1 O LEU O 67 N PHE O 4 SHEET 4 U 5 GLN O 41 PHE O 45 -1 N ARG O 42 O VAL O 70 SHEET 5 U 5 LYS O 48 GLN O 49 -1 O LYS O 48 N PHE O 45 SHEET 1 V 5 THR P 12 GLU P 16 0 SHEET 2 V 5 GLN P 2 LYS P 6 -1 N VAL P 5 O ILE P 13 SHEET 3 V 5 THR P 66 LEU P 71 1 O LEU P 67 N PHE P 4 SHEET 4 V 5 GLN P 41 PHE P 45 -1 N ARG P 42 O VAL P 70 SHEET 5 V 5 LYS P 48 GLN P 49 -1 O LYS P 48 N PHE P 45 SHEET 1 W 5 THR Q 12 GLU Q 16 0 SHEET 2 W 5 GLN Q 2 LYS Q 6 -1 N VAL Q 5 O ILE Q 13 SHEET 3 W 5 THR Q 66 LEU Q 71 1 O LEU Q 67 N PHE Q 4 SHEET 4 W 5 GLN Q 41 PHE Q 45 -1 N ARG Q 42 O VAL Q 70 SHEET 5 W 5 LYS Q 48 GLN Q 49 -1 O LYS Q 48 N PHE Q 45 SHEET 1 X 5 THR R 12 GLU R 16 0 SHEET 2 X 5 GLN R 2 LYS R 6 -1 N VAL R 5 O ILE R 13 SHEET 3 X 5 THR R 66 LEU R 71 1 O LEU R 67 N PHE R 4 SHEET 4 X 5 GLN R 41 PHE R 45 -1 N ARG R 42 O VAL R 70 SHEET 5 X 5 LYS R 48 GLN R 49 -1 O LYS R 48 N PHE R 45 SSBOND 1 CYS A 21 CYS A 107 1555 1555 2.04 SSBOND 2 CYS B 21 CYS B 107 1555 1555 2.04 SSBOND 3 CYS C 21 CYS C 107 1555 1555 2.04 SSBOND 4 CYS J 21 CYS J 107 1555 1555 2.04 SSBOND 5 CYS K 21 CYS K 107 1555 1555 2.04 SSBOND 6 CYS L 21 CYS L 107 1555 1555 2.04 CISPEP 1 TYR A 60 PRO A 61 0 -7.60 CISPEP 2 TYR B 60 PRO B 61 0 -7.60 CISPEP 3 TYR C 60 PRO C 61 0 -7.59 CISPEP 4 TYR J 60 PRO J 61 0 -7.69 CISPEP 5 TYR K 60 PRO K 61 0 -7.62 CISPEP 6 TYR L 60 PRO L 61 0 -7.60 CRYST1 134.566 104.928 148.479 90.00 104.19 90.00 P 1 21 1 24 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 0.007431 0.000000 0.001879 0.00000 SCALE2 0.000000 0.009530 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006947 0.00000 ATOM 10 N MET A 1 3.991 -63.855 28.189 1.00166.74 N ANISOU 10 N MET A 1 22393 21339 19622 -5805 242 -1636 N ATOM 11 CA MET A 1 4.561 -63.863 26.845 1.00166.40 C ANISOU 11 CA MET A 1 22187 21570 19469 -5440 288 -1897 C ATOM 12 C MET A 1 4.590 -65.284 26.305 1.00146.71 C ANISOU 12 C MET A 1 19489 19655 16600 -5162 452 -1814 C ATOM 13 O MET A 1 4.486 -65.499 25.097 1.00135.55 O ANISOU 13 O MET A 1 17875 18657 14972 -4958 492 -2029 O ATOM 14 CB MET A 1 5.975 -63.279 26.837 1.00169.21 C ANISOU 14 CB MET A 1 22717 21506 20068 -5135 258 -1902 C ATOM 15 CG MET A 1 6.234 -62.244 27.913 1.00142.20 C ANISOU 15 CG MET A 1 19563 17415 17051 -5337 89 -1808 C ATOM 16 SD MET A 1 6.289 -63.009 29.542 1.00245.91 S ANISOU 16 SD MET A 1 32911 30341 30183 -5476 62 -1351 S ATOM 17 CE MET A 1 7.409 -64.372 29.228 1.00179.33 C ANISOU 17 CE MET A 1 24381 22226 21529 -5002 236 -1212 C ATOM 18 N ALA A 2 4.738 -66.247 27.212 1.00141.63 N ANISOU 18 N ALA A 2 18918 19023 15872 -5139 533 -1506 N ATOM 19 CA ALA A 2 4.669 -67.659 26.861 1.00136.49 C ANISOU 19 CA ALA A 2 18088 18877 14894 -4896 685 -1410 C ATOM 20 C ALA A 2 3.309 -67.979 26.246 1.00106.45 C ANISOU 20 C ALA A 2 13978 15599 10871 -5077 710 -1582 C ATOM 21 O ALA A 2 3.227 -68.593 25.181 1.00 98.93 O ANISOU 21 O ALA A 2 12800 15110 9677 -4810 758 -1709 O ATOM 22 CB ALA A 2 4.923 -68.520 28.088 1.00105.01 C ANISOU 22 CB ALA A 2 14256 14765 10877 -4905 748 -1088 C ATOM 23 N LEU A 3 2.246 -67.547 26.920 1.00129.59 N ANISOU 23 N LEU A 3 16895 18446 13897 -5535 671 -1581 N ATOM 24 CA LEU A 3 0.889 -67.768 26.430 1.00133.68 C ANISOU 24 CA LEU A 3 17082 19433 14279 -5773 692 -1759 C ATOM 25 C LEU A 3 0.680 -67.095 25.078 1.00119.79 C ANISOU 25 C LEU A 3 15135 17871 12507 -5703 565 -2134 C ATOM 26 O LEU A 3 0.190 -67.724 24.133 1.00141.49 O ANISOU 26 O LEU A 3 17577 21165 15016 -5546 574 -2296 O ATOM 27 CB LEU A 3 -0.144 -67.250 27.432 1.00135.00 C ANISOU 27 CB LEU A 3 17299 19384 14609 -6329 691 -1680 C ATOM 28 CG LEU A 3 -1.610 -67.465 27.035 1.00132.46 C ANISOU 28 CG LEU A 3 16592 19530 14206 -6643 736 -1860 C ATOM 29 CD1 LEU A 3 -2.148 -68.778 27.599 1.00112.60 C ANISOU 29 CD1 LEU A 3 13913 17409 11462 -6651 952 -1658 C ATOM 30 CD2 LEU A 3 -2.478 -66.285 27.455 1.00148.58 C ANISOU 30 CD2 LEU A 3 18687 21231 16535 -7201 651 -1943 C ATOM 31 N LYS A 4 1.053 -65.818 24.996 1.00106.70 N ANISOU 31 N LYS A 4 13668 15769 11103 -5801 432 -2283 N ATOM 32 CA LYS A 4 0.927 -65.072 23.746 1.00138.95 C ANISOU 32 CA LYS A 4 17628 19998 15170 -5728 303 -2673 C ATOM 33 C LYS A 4 1.600 -65.832 22.604 1.00134.43 C ANISOU 33 C LYS A 4 16945 19861 14270 -5205 359 -2735 C ATOM 34 O LYS A 4 1.016 -66.016 21.524 1.00115.29 O ANISOU 34 O LYS A 4 14266 17919 11620 -5120 290 -2990 O ATOM 35 CB LYS A 4 1.528 -63.668 23.879 1.00133.62 C ANISOU 35 CB LYS A 4 17224 18727 14817 -5800 185 -2805 C ATOM 36 CG LYS A 4 1.600 -62.912 22.557 1.00157.36 C ANISOU 36 CG LYS A 4 20151 21873 17767 -5648 73 -3231 C ATOM 37 CD LYS A 4 2.223 -61.529 22.709 1.00163.28 C ANISOU 37 CD LYS A 4 21162 22020 18859 -5689 -24 -3386 C ATOM 38 CE LYS A 4 1.244 -60.535 23.310 1.00176.64 C ANISOU 38 CE LYS A 4 22899 23329 20886 -6217 -175 -3504 C ATOM 39 NZ LYS A 4 1.790 -59.147 23.292 1.00172.53 N ANISOU 39 NZ LYS A 4 22610 22238 20705 -6218 -294 -3724 N ATOM 40 N ARG A 5 2.820 -66.295 22.869 1.00106.31 N ANISOU 40 N ARG A 5 13580 16124 10688 -4864 477 -2488 N ATOM 41 CA ARG A 5 3.592 -67.056 21.895 1.00103.75 C ANISOU 41 CA ARG A 5 13208 16136 10077 -4368 567 -2469 C ATOM 42 C ARG A 5 2.866 -68.324 21.462 1.00 82.13 C ANISOU 42 C ARG A 5 10188 14000 7019 -4244 609 -2425 C ATOM 43 O ARG A 5 2.790 -68.622 20.271 1.00125.39 O ANISOU 43 O ARG A 5 15515 19907 12220 -3971 572 -2586 O ATOM 44 CB ARG A 5 4.970 -67.407 22.459 1.00118.03 C ANISOU 44 CB ARG A 5 15258 17598 11989 -4096 701 -2175 C ATOM 45 CG ARG A 5 5.675 -68.542 21.733 1.00 92.23 C ANISOU 45 CG ARG A 5 11943 14664 8437 -3629 841 -2037 C ATOM 46 CD ARG A 5 6.431 -68.079 20.503 1.00 81.24 C ANISOU 46 CD ARG A 5 10598 13354 6915 -3310 873 -2210 C ATOM 47 NE ARG A 5 7.288 -69.145 19.993 1.00 75.81 N ANISOU 47 NE ARG A 5 9934 12859 6010 -2879 1038 -1994 N ATOM 48 CZ ARG A 5 8.488 -68.950 19.460 1.00104.71 C ANISOU 48 CZ ARG A 5 13740 16372 9672 -2583 1174 -1951 C ATOM 49 NH1 ARG A 5 9.193 -69.985 19.025 1.00 83.66 N ANISOU 49 NH1 ARG A 5 11099 13868 6820 -2223 1332 -1724 N ATOM 50 NH2 ARG A 5 8.983 -67.720 19.366 1.00106.23 N ANISOU 50 NH2 ARG A 5 14051 16244 10070 -2648 1166 -2136 N ATOM 51 N ILE A 6 2.335 -69.064 22.431 1.00110.97 N ANISOU 51 N ILE A 6 13776 17686 10700 -4428 684 -2211 N ATOM 52 CA ILE A 6 1.566 -70.268 22.128 1.00 96.76 C ANISOU 52 CA ILE A 6 11676 16445 8644 -4324 734 -2185 C ATOM 53 C ILE A 6 0.408 -69.948 21.178 1.00108.00 C ANISOU 53 C ILE A 6 12767 18306 9961 -4472 579 -2530 C ATOM 54 O ILE A 6 0.166 -70.677 20.204 1.00113.01 O ANISOU 54 O ILE A 6 13169 19449 10322 -4174 539 -2622 O ATOM 55 CB ILE A 6 1.054 -70.955 23.414 1.00 79.89 C ANISOU 55 CB ILE A 6 9524 14258 6574 -4568 859 -1946 C ATOM 56 CG1 ILE A 6 2.233 -71.456 24.248 1.00 85.61 C ANISOU 56 CG1 ILE A 6 10555 14620 7352 -4353 977 -1631 C ATOM 57 CG2 ILE A 6 0.121 -72.113 23.085 1.00104.31 C ANISOU 57 CG2 ILE A 6 12247 17946 9438 -4484 918 -1977 C ATOM 58 CD1 ILE A 6 1.827 -72.167 25.519 1.00124.58 C ANISOU 58 CD1 ILE A 6 15528 19512 12294 -4549 1099 -1405 C ATOM 59 N HIS A 7 -0.285 -68.842 21.443 1.00128.31 N ANISOU 59 N HIS A 7 15326 20661 12765 -4922 469 -2725 N ATOM 60 CA HIS A 7 -1.354 -68.397 20.552 1.00106.31 C ANISOU 60 CA HIS A 7 12230 18232 9932 -5105 288 -3099 C ATOM 61 C HIS A 7 -0.839 -68.120 19.140 1.00129.93 C ANISOU 61 C HIS A 7 15232 21449 12688 -4720 151 -3351 C ATOM 62 O HIS A 7 -1.477 -68.506 18.152 1.00126.56 O ANISOU 62 O HIS A 7 14507 21556 12025 -4587 18 -3568 O ATOM 63 CB HIS A 7 -2.070 -67.168 21.116 1.00148.90 C ANISOU 63 CB HIS A 7 17661 23249 15666 -5669 196 -3261 C ATOM 64 CG HIS A 7 -3.161 -67.500 22.087 1.00156.44 C ANISOU 64 CG HIS A 7 18431 24247 16762 -6119 295 -3133 C ATOM 65 ND1 HIS A 7 -3.226 -66.952 23.350 1.00165.80 N ANISOU 65 ND1 HIS A 7 19864 24910 18222 -6512 377 -2924 N ATOM 66 CD2 HIS A 7 -4.237 -68.316 21.977 1.00120.82 C ANISOU 66 CD2 HIS A 7 13509 20248 12150 -6237 340 -3180 C ATOM 67 CE1 HIS A 7 -4.289 -67.420 23.978 1.00147.94 C ANISOU 67 CE1 HIS A 7 17375 22841 15995 -6866 496 -2833 C ATOM 68 NE2 HIS A 7 -4.919 -68.250 23.166 1.00154.80 N ANISOU 68 NE2 HIS A 7 17820 24340 16657 -6710 486 -2999 N ATOM 69 N LYS A 8 0.314 -67.462 19.045 1.00131.02 N ANISOU 69 N LYS A 8 15707 21195 12878 -4531 183 -3323 N ATOM 70 CA LYS A 8 0.915 -67.206 17.735 1.00123.43 C ANISOU 70 CA LYS A 8 14808 20439 11652 -4145 108 -3531 C ATOM 71 C LYS A 8 1.213 -68.509 16.990 1.00101.13 C ANISOU 71 C LYS A 8 11875 18111 8438 -3660 170 -3371 C ATOM 72 O LYS A 8 0.937 -68.628 15.790 1.00150.02 O ANISOU 72 O LYS A 8 17928 24758 14316 -3430 26 -3591 O ATOM 73 CB LYS A 8 2.193 -66.370 17.866 1.00 88.80 C ANISOU 73 CB LYS A 8 10788 15537 7415 -4010 200 -3490 C ATOM 74 CG LYS A 8 1.996 -65.003 18.514 1.00153.25 C ANISOU 74 CG LYS A 8 19088 23164 15975 -4425 113 -3665 C ATOM 75 CD LYS A 8 3.306 -64.221 18.562 1.00131.99 C ANISOU 75 CD LYS A 8 16713 20000 13438 -4227 205 -3648 C ATOM 76 CE LYS A 8 3.668 -63.639 17.201 1.00157.96 C ANISOU 76 CE LYS A 8 20041 23501 16477 -3946 157 -3994 C ATOM 77 NZ LYS A 8 3.024 -62.316 16.956 1.00141.69 N ANISOU 77 NZ LYS A 8 17981 21256 14598 -4250 -43 -4434 N ATOM 78 N GLU A 9 1.763 -69.487 17.704 1.00120.54 N ANISOU 78 N GLU A 9 14413 20470 10917 -3500 363 -2991 N ATOM 79 CA GLU A 9 2.105 -70.771 17.097 1.00122.34 C ANISOU 79 CA GLU A 9 14571 21086 10825 -3033 434 -2801 C ATOM 80 C GLU A 9 0.854 -71.483 16.598 1.00106.31 C ANISOU 80 C GLU A 9 12137 19648 8606 -3038 287 -2946 C ATOM 81 O GLU A 9 0.862 -72.082 15.520 1.00147.94 O ANISOU 81 O GLU A 9 17307 25359 13546 -2652 200 -2987 O ATOM 82 CB GLU A 9 2.881 -71.669 18.071 1.00 82.21 C ANISOU 82 CB GLU A 9 9648 15733 5854 -2904 657 -2397 C ATOM 83 CG GLU A 9 4.240 -71.120 18.496 1.00143.62 C ANISOU 83 CG GLU A 9 17786 22959 13825 -2829 794 -2238 C ATOM 84 CD GLU A 9 5.308 -72.197 18.619 1.00131.05 C ANISOU 84 CD GLU A 9 16339 21287 12167 -2447 982 -1895 C ATOM 85 OE1 GLU A 9 5.149 -73.267 17.996 1.00115.82 O ANISOU 85 OE1 GLU A 9 14280 19759 9967 -2134 996 -1810 O ATOM 86 OE2 GLU A 9 6.308 -71.973 19.339 1.00 93.09 O ANISOU 86 OE2 GLU A 9 11767 16002 7601 -2455 1101 -1719 O ATOM 87 N LEU A 10 -0.219 -71.412 17.378 1.00 91.75 N ANISOU 87 N LEU A 10 10062 17819 6980 -3474 259 -3016 N ATOM 88 CA LEU A 10 -1.475 -72.029 16.967 1.00101.45 C ANISOU 88 CA LEU A 10 10841 19608 8097 -3527 129 -3185 C ATOM 89 C LEU A 10 -2.033 -71.340 15.724 1.00123.25 C ANISOU 89 C LEU A 10 13428 22704 10698 -3522 -159 -3596 C ATOM 90 O LEU A 10 -2.591 -71.992 14.834 1.00120.02 O ANISOU 90 O LEU A 10 12717 22844 10038 -3277 -322 -3725 O ATOM 91 CB LEU A 10 -2.491 -71.998 18.106 1.00108.72 C ANISOU 91 CB LEU A 10 11555 20443 9310 -4048 208 -3173 C ATOM 92 CG LEU A 10 -3.789 -72.760 17.840 1.00 99.03 C ANISOU 92 CG LEU A 10 9806 19796 8024 -4118 135 -3321 C ATOM 93 CD1 LEU A 10 -3.492 -74.188 17.406 1.00 98.32 C ANISOU 93 CD1 LEU A 10 9604 20089 7662 -3572 189 -3139 C ATOM 94 CD2 LEU A 10 -4.677 -72.743 19.073 1.00135.23 C ANISOU 94 CD2 LEU A 10 14234 24255 12894 -4646 297 -3253 C ATOM 95 N ASN A 11 -1.870 -70.020 15.664 1.00157.86 N ANISOU 95 N ASN A 11 18004 26749 15227 -3775 -240 -3816 N ATOM 96 CA ASN A 11 -2.237 -69.260 14.473 1.00133.41 C ANISOU 96 CA ASN A 11 14819 23911 11957 -3747 -518 -4238 C ATOM 97 C ASN A 11 -1.477 -69.735 13.236 1.00123.82 C ANISOU 97 C ASN A 11 13734 23032 10281 -3146 -574 -4215 C ATOM 98 O ASN A 11 -2.074 -69.960 12.183 1.00141.20 O ANISOU 98 O ASN A 11 15697 25757 12196 -2968 -825 -4458 O ATOM 99 CB ASN A 11 -2.010 -67.762 14.695 1.00154.21 C ANISOU 99 CB ASN A 11 17707 26040 14844 -4074 -557 -4462 C ATOM 100 CG ASN A 11 -3.048 -67.144 15.611 1.00170.72 C ANISOU 100 CG ASN A 11 19627 27884 17355 -4704 -594 -4583 C ATOM 101 OD1 ASN A 11 -4.221 -67.513 15.574 1.00175.93 O ANISOU 101 OD1 ASN A 11 19881 28903 18060 -4938 -702 -4718 O ATOM 102 ND2 ASN A 11 -2.620 -66.195 16.439 1.00162.91 N ANISOU 102 ND2 ASN A 11 18939 26270 16690 -4981 -502 -4526 N ATOM 103 N ASP A 12 -0.161 -69.889 13.370 1.00164.41 N ANISOU 103 N ASP A 12 19249 27868 15352 -2840 -346 -3912 N ATOM 104 CA ASP A 12 0.665 -70.367 12.259 1.00175.54 C ANISOU 104 CA ASP A 12 20832 29542 16324 -2278 -337 -3817 C ATOM 105 C ASP A 12 0.283 -71.778 11.819 1.00148.28 C ANISOU 105 C ASP A 12 17134 26600 12606 -1927 -399 -3646 C ATOM 106 O ASP A 12 0.203 -72.061 10.623 1.00140.81 O ANISOU 106 O ASP A 12 16144 26032 11324 -1554 -574 -3718 O ATOM 107 CB ASP A 12 2.154 -70.318 12.619 1.00209.11 C ANISOU 107 CB ASP A 12 25496 33327 20630 -2068 -35 -3494 C ATOM 108 CG ASP A 12 3.028 -71.012 11.584 1.00195.91 C ANISOU 108 CG ASP A 12 24006 31906 18524 -1497 42 -3299 C ATOM 109 OD1 ASP A 12 3.209 -70.455 10.482 1.00142.12 O ANISOU 109 OD1 ASP A 12 17309 25194 11496 -1286 -63 -3466 O ATOM 110 OD2 ASP A 12 3.546 -72.113 11.879 1.00196.27 O ANISOU 110 OD2 ASP A 12 24099 31924 18551 -1243 215 -2918 O ATOM 111 N LEU A 13 0.054 -72.662 12.786 1.00159.88 N ANISOU 111 N LEU A 13 18457 27997 14291 -2014 -251 -3384 N ATOM 112 CA LEU A 13 -0.288 -74.046 12.482 1.00132.55 C ANISOU 112 CA LEU A 13 14755 24970 10637 -1668 -286 -3218 C ATOM 113 C LEU A 13 -1.659 -74.131 11.825 1.00125.93 C ANISOU 113 C LEU A 13 13447 24702 9699 -1751 -608 -3566 C ATOM 114 O LEU A 13 -1.917 -75.028 11.023 1.00142.57 O ANISOU 114 O LEU A 13 15367 27280 11523 -1350 -761 -3542 O ATOM 115 CB LEU A 13 -0.249 -74.903 13.750 1.00105.73 C ANISOU 115 CB LEU A 13 11315 21347 7513 -1770 -38 -2908 C ATOM 116 CG LEU A 13 -0.390 -76.415 13.557 1.00124.91 C ANISOU 116 CG LEU A 13 13555 24125 9781 -1357 -15 -2696 C ATOM 117 CD1 LEU A 13 0.695 -76.950 12.630 1.00137.87 C ANISOU 117 CD1 LEU A 13 15491 25803 11089 -781 12 -2466 C ATOM 118 CD2 LEU A 13 -0.345 -77.122 14.898 1.00106.90 C ANISOU 118 CD2 LEU A 13 11265 21576 7774 -1505 242 -2445 C ATOM 119 N ALA A 14 -2.534 -73.189 12.168 1.00144.53 N ANISOU 119 N ALA A 14 15607 26996 12311 -2272 -723 -3888 N ATOM 120 CA ALA A 14 -3.864 -73.134 11.572 1.00153.39 C ANISOU 120 CA ALA A 14 16247 28626 13406 -2426 -1043 -4269 C ATOM 121 C ALA A 14 -3.832 -72.517 10.171 1.00134.15 C ANISOU 121 C ALA A 14 13886 26402 10684 -2175 -1338 -4548 C ATOM 122 O ALA A 14 -4.679 -72.823 9.331 1.00130.61 O ANISOU 122 O ALA A 14 13096 26387 10143 -2026 -1615 -4742 O ATOM 123 CB ALA A 14 -4.817 -72.364 12.474 1.00171.47 C ANISOU 123 CB ALA A 14 18309 30708 16135 -3103 -1029 -4480 C ATOM 124 N ARG A 15 -2.850 -71.651 9.930 1.00164.11 N ANISOU 124 N ARG A 15 18138 29797 14419 -2098 -1246 -4522 N ATOM 125 CA ARG A 15 -2.694 -70.996 8.632 1.00147.90 C ANISOU 125 CA ARG A 15 16245 27805 12145 -1832 -1453 -4722 C ATOM 126 C ARG A 15 -2.456 -72.000 7.500 1.00164.20 C ANISOU 126 C ARG A 15 18322 30249 13819 -1209 -1565 -4528 C ATOM 127 O ARG A 15 -3.175 -72.004 6.501 1.00144.36 O ANISOU 127 O ARG A 15 15603 28095 11152 -1059 -1878 -4758 O ATOM 128 CB ARG A 15 -1.555 -69.974 8.680 1.00168.51 C ANISOU 128 CB ARG A 15 19350 29917 14758 -1839 -1266 -4698 C ATOM 129 CG ARG A 15 -1.042 -69.541 7.316 1.00191.65 C ANISOU 129 CG ARG A 15 22551 32915 17351 -1435 -1382 -4784 C ATOM 130 CD ARG A 15 -0.114 -68.338 7.419 1.00189.23 C ANISOU 130 CD ARG A 15 22652 32140 17106 -1530 -1209 -4875 C ATOM 131 NE ARG A 15 -0.774 -67.107 6.991 1.00233.90 N ANISOU 131 NE ARG A 15 28265 37748 22860 -1794 -1449 -5354 N ATOM 132 CZ ARG A 15 -1.454 -66.299 7.799 1.00226.44 C ANISOU 132 CZ ARG A 15 27165 36550 22320 -2328 -1507 -5622 C ATOM 133 NH1 ARG A 15 -2.021 -65.200 7.317 1.00204.67 N ANISOU 133 NH1 ARG A 15 24393 33711 19662 -2523 -1730 -6044 N ATOM 134 NH2 ARG A 15 -1.568 -66.590 9.089 1.00211.56 N ANISOU 134 NH2 ARG A 15 25168 34465 20749 -2672 -1340 -5454 N ATOM 135 N ASP A 16 -1.447 -72.846 7.670 1.00214.77 N ANISOU 135 N ASP A 16 24981 36534 20088 -852 -1315 -4095 N ATOM 136 CA ASP A 16 -1.136 -73.881 6.692 1.00215.62 C ANISOU 136 CA ASP A 16 25146 36917 19863 -262 -1389 -3841 C ATOM 137 C ASP A 16 -1.287 -75.250 7.326 1.00197.17 C ANISOU 137 C ASP A 16 22585 34750 17582 -117 -1285 -3559 C ATOM 138 O ASP A 16 -0.303 -75.842 7.770 1.00177.38 O ANISOU 138 O ASP A 16 20355 31957 15086 81 -998 -3170 O ATOM 139 CB ASP A 16 0.286 -73.717 6.162 1.00237.73 C ANISOU 139 CB ASP A 16 28490 39378 22460 84 -1171 -3548 C ATOM 140 CG ASP A 16 0.358 -72.787 4.974 1.00246.97 C ANISOU 140 CG ASP A 16 29860 40599 23378 195 -1354 -3795 C ATOM 141 OD1 ASP A 16 -0.595 -72.788 4.166 1.00229.96 O ANISOU 141 OD1 ASP A 16 27450 38848 21078 258 -1704 -4065 O ATOM 142 OD2 ASP A 16 1.364 -72.058 4.846 1.00237.14 O ANISOU 142 OD2 ASP A 16 29022 38999 22082 222 -1144 -3732 O ATOM 143 N PRO A 17 -2.526 -75.756 7.376 1.00169.00 N ANISOU 143 N PRO A 17 18499 31640 14073 -217 -1514 -3769 N ATOM 144 CA PRO A 17 -2.752 -77.004 8.104 1.00156.15 C ANISOU 144 CA PRO A 17 16621 30198 12512 -120 -1398 -3556 C ATOM 145 C PRO A 17 -2.110 -78.201 7.416 1.00178.09 C ANISOU 145 C PRO A 17 19562 33080 15026 535 -1384 -3186 C ATOM 146 O PRO A 17 -2.328 -78.412 6.222 1.00161.01 O ANISOU 146 O PRO A 17 17356 31205 12615 903 -1655 -3238 O ATOM 147 CB PRO A 17 -4.277 -77.144 8.098 1.00156.65 C ANISOU 147 CB PRO A 17 16052 30771 12699 -365 -1680 -3927 C ATOM 148 CG PRO A 17 -4.761 -76.297 6.944 1.00164.49 C ANISOU 148 CG PRO A 17 16998 31904 13598 -356 -2012 -4259 C ATOM 149 CD PRO A 17 -3.636 -75.420 6.468 1.00146.35 C ANISOU 149 CD PRO A 17 15284 29181 11142 -247 -1906 -4161 C ATOM 150 N PRO A 18 -1.316 -78.978 8.166 1.00210.59 N ANISOU 150 N PRO A 18 23883 36923 19210 676 -1074 -2810 N ATOM 151 CA PRO A 18 -0.845 -80.279 7.684 1.00178.10 C ANISOU 151 CA PRO A 18 19859 32899 14912 1265 -1056 -2460 C ATOM 152 C PRO A 18 -1.995 -81.275 7.710 1.00190.62 C ANISOU 152 C PRO A 18 20890 35069 16469 1406 -1273 -2602 C ATOM 153 O PRO A 18 -2.734 -81.324 8.695 1.00178.60 O ANISOU 153 O PRO A 18 19018 33646 15196 1024 -1198 -2769 O ATOM 154 CB PRO A 18 0.225 -80.670 8.711 1.00159.97 C ANISOU 154 CB PRO A 18 17898 30077 12807 1241 -648 -2091 C ATOM 155 CG PRO A 18 0.571 -79.392 9.432 1.00157.86 C ANISOU 155 CG PRO A 18 17830 29391 12758 723 -474 -2213 C ATOM 156 CD PRO A 18 -0.699 -78.612 9.451 1.00182.65 C ANISOU 156 CD PRO A 18 20568 32894 15935 306 -724 -2678 C ATOM 157 N ALA A 19 -2.150 -82.056 6.647 1.00208.98 N ANISOU 157 N ALA A 19 23132 37718 18553 1940 -1521 -2523 N ATOM 158 CA ALA A 19 -3.215 -83.043 6.599 1.00189.75 C ANISOU 158 CA ALA A 19 20137 35850 16109 2142 -1755 -2662 C ATOM 159 C ALA A 19 -2.826 -84.271 7.406 1.00188.80 C ANISOU 159 C ALA A 19 20039 35587 16109 2379 -1484 -2341 C ATOM 160 O ALA A 19 -3.665 -84.887 8.061 1.00166.49 O ANISOU 160 O ALA A 19 16755 32922 13581 2272 -1442 -2451 O ATOM 161 CB ALA A 19 -3.525 -83.425 5.164 1.00184.04 C ANISOU 161 CB ALA A 19 19332 35466 15129 2649 -2133 -2688 C ATOM 162 N GLN A 20 -1.547 -84.622 7.353 1.00184.85 N ANISOU 162 N GLN A 20 20078 34682 15473 2683 -1256 -1932 N ATOM 163 CA GLN A 20 -1.068 -85.814 8.037 1.00165.30 C ANISOU 163 CA GLN A 20 17689 31920 13195 2936 -986 -1602 C ATOM 164 C GLN A 20 -0.857 -85.627 9.543 1.00141.33 C ANISOU 164 C GLN A 20 14705 28418 10577 2445 -594 -1571 C ATOM 165 O GLN A 20 -1.317 -86.449 10.333 1.00136.13 O ANISOU 165 O GLN A 20 13774 27770 10178 2435 -465 -1571 O ATOM 166 CB GLN A 20 0.207 -86.338 7.374 1.00193.50 C ANISOU 166 CB GLN A 20 21803 35217 16503 3450 -901 -1167 C ATOM 167 CG GLN A 20 0.513 -87.787 7.706 1.00222.12 C ANISOU 167 CG GLN A 20 25448 38687 20261 3874 -763 -864 C ATOM 168 CD GLN A 20 1.570 -88.379 6.800 1.00227.10 C ANISOU 168 CD GLN A 20 26552 39133 20604 4436 -763 -445 C ATOM 169 OE1 GLN A 20 2.717 -88.566 7.204 1.00220.30 O ANISOU 169 OE1 GLN A 20 26120 37704 19878 4445 -439 -118 O ATOM 170 NE2 GLN A 20 1.186 -88.681 5.564 1.00205.02 N ANISOU 170 NE2 GLN A 20 23666 36687 17544 4861 -1112 -445 N ATOM 171 N CYS A 21 -0.174 -84.556 9.944 1.00153.91 N ANISOU 171 N CYS A 21 16647 29607 12223 2058 -411 -1552 N ATOM 172 CA CYS A 21 0.046 -84.313 11.374 1.00134.71 C ANISOU 172 CA CYS A 21 14296 26724 10165 1598 -82 -1514 C ATOM 173 C CYS A 21 -0.325 -82.912 11.863 1.00119.20 C ANISOU 173 C CYS A 21 12291 24650 8351 972 -72 -1786 C ATOM 174 O CYS A 21 0.341 -81.929 11.548 1.00123.28 O ANISOU 174 O CYS A 21 13132 24940 8767 853 -64 -1788 O ATOM 175 CB CYS A 21 1.483 -84.661 11.790 1.00110.20 C ANISOU 175 CB CYS A 21 11707 23046 7119 1764 216 -1124 C ATOM 176 SG CYS A 21 2.798 -84.181 10.642 1.00253.69 S ANISOU 176 SG CYS A 21 30408 40931 25053 2059 208 -872 S ATOM 177 N SER A 22 -1.373 -82.852 12.679 1.00150.16 N ANISOU 177 N SER A 22 15819 28704 12531 574 -45 -2003 N ATOM 178 CA SER A 22 -1.843 -81.603 13.257 1.00127.30 C ANISOU 178 CA SER A 22 12863 25676 9830 -48 -28 -2245 C ATOM 179 C SER A 22 -1.942 -81.757 14.765 1.00136.66 C ANISOU 179 C SER A 22 14049 26532 11342 -427 275 -2153 C ATOM 180 O SER A 22 -1.999 -82.868 15.286 1.00141.09 O ANISOU 180 O SER A 22 14513 27123 11972 -230 426 -2008 O ATOM 181 CB SER A 22 -3.218 -81.242 12.698 1.00126.86 C ANISOU 181 CB SER A 22 12285 26156 9760 -240 -324 -2639 C ATOM 182 OG SER A 22 -4.206 -82.127 13.201 1.00130.08 O ANISOU 182 OG SER A 22 12213 26869 10343 -274 -276 -2712 O ATOM 183 N ALA A 23 -1.968 -80.628 15.462 1.00116.33 N ANISOU 183 N ALA A 23 11603 23640 8958 -957 355 -2243 N ATOM 184 CA ALA A 23 -2.077 -80.634 16.912 1.00 94.45 C ANISOU 184 CA ALA A 23 8881 20546 6460 -1351 619 -2150 C ATOM 185 C ALA A 23 -2.852 -79.413 17.370 1.00106.45 C ANISOU 185 C ALA A 23 10279 21993 8175 -1976 581 -2385 C ATOM 186 O ALA A 23 -3.035 -78.458 16.613 1.00115.20 O ANISOU 186 O ALA A 23 11362 23179 9229 -2096 366 -2607 O ATOM 187 CB ALA A 23 -0.704 -80.661 17.548 1.00114.52 C ANISOU 187 CB ALA A 23 11943 22513 9058 -1258 824 -1840 C ATOM 188 N GLY A 24 -3.315 -79.445 18.613 1.00 97.61 N ANISOU 188 N GLY A 24 9101 20714 7271 -2373 790 -2338 N ATOM 189 CA GLY A 24 -4.122 -78.360 19.132 1.00125.40 C ANISOU 189 CA GLY A 24 12507 24139 11000 -2990 780 -2522 C ATOM 190 C GLY A 24 -4.426 -78.547 20.597 1.00 95.16 C ANISOU 190 C GLY A 24 8722 20083 7351 -3363 1062 -2372 C ATOM 191 O GLY A 24 -4.284 -79.649 21.124 1.00143.04 O ANISOU 191 O GLY A 24 14780 26208 13363 -3135 1249 -2202 O ATOM 192 N PRO A 25 -4.862 -77.469 21.257 1.00 95.68 N ANISOU 192 N PRO A 25 8852 19882 7620 -3933 1090 -2437 N ATOM 193 CA PRO A 25 -5.128 -77.441 22.698 1.00120.62 C ANISOU 193 CA PRO A 25 12137 22770 10924 -4344 1349 -2267 C ATOM 194 C PRO A 25 -6.244 -78.386 23.120 1.00106.36 C ANISOU 194 C PRO A 25 9887 21411 9116 -4445 1545 -2312 C ATOM 195 O PRO A 25 -7.192 -78.621 22.368 1.00104.18 O ANISOU 195 O PRO A 25 9101 21638 8846 -4434 1444 -2559 O ATOM 196 CB PRO A 25 -5.545 -75.988 22.945 1.00121.24 C ANISOU 196 CB PRO A 25 12297 22550 11220 -4913 1262 -2387 C ATOM 197 CG PRO A 25 -6.040 -75.509 21.627 1.00139.85 C ANISOU 197 CG PRO A 25 14338 25239 13561 -4869 982 -2721 C ATOM 198 CD PRO A 25 -5.164 -76.178 20.619 1.00112.53 C ANISOU 198 CD PRO A 25 10953 21957 9847 -4219 858 -2691 C ATOM 199 N VAL A 26 -6.126 -78.910 24.334 1.00109.06 N ANISOU 199 N VAL A 26 10417 21571 9448 -4542 1822 -2089 N ATOM 200 CA VAL A 26 -7.147 -79.774 24.891 1.00100.42 C ANISOU 200 CA VAL A 26 8943 20867 8344 -4666 2076 -2121 C ATOM 201 C VAL A 26 -8.123 -78.915 25.672 1.00103.34 C ANISOU 201 C VAL A 26 9226 21147 8892 -5365 2213 -2151 C ATOM 202 O VAL A 26 -7.785 -78.369 26.729 1.00121.37 O ANISOU 202 O VAL A 26 11940 22964 11212 -5679 2334 -1936 O ATOM 203 CB VAL A 26 -6.537 -80.802 25.852 1.00 98.11 C ANISOU 203 CB VAL A 26 8931 20433 7913 -4417 2327 -1880 C ATOM 204 CG1 VAL A 26 -7.631 -81.625 26.511 1.00122.69 C ANISOU 204 CG1 VAL A 26 11667 23947 11003 -4579 2637 -1930 C ATOM 205 CG2 VAL A 26 -5.549 -81.694 25.115 1.00135.99 C ANISOU 205 CG2 VAL A 26 13833 25267 12570 -3738 2208 -1828 C ATOM 206 N GLY A 27 -9.332 -78.796 25.135 1.00108.08 N ANISOU 206 N GLY A 27 9266 22184 9615 -5609 2179 -2412 N ATOM 207 CA GLY A 27 -10.371 -78.023 25.781 1.00129.89 C ANISOU 207 CA GLY A 27 11878 24893 12582 -6301 2326 -2453 C ATOM 208 C GLY A 27 -9.909 -76.616 26.089 1.00139.03 C ANISOU 208 C GLY A 27 13508 25440 13877 -6670 2186 -2364 C ATOM 209 O GLY A 27 -9.469 -75.877 25.208 1.00108.70 O ANISOU 209 O GLY A 27 9753 21458 10089 -6558 1872 -2511 O ATOM 210 N ASP A 28 -9.993 -76.265 27.365 1.00161.82 N ANISOU 210 N ASP A 28 16756 27918 16810 -7044 2399 -2114 N ATOM 211 CA ASP A 28 -9.626 -74.942 27.838 1.00153.68 C ANISOU 211 CA ASP A 28 16195 26259 15937 -7402 2283 -1995 C ATOM 212 C ASP A 28 -8.118 -74.717 27.829 1.00150.47 C ANISOU 212 C ASP A 28 16296 25440 15434 -7064 2128 -1841 C ATOM 213 O ASP A 28 -7.658 -73.603 27.583 1.00124.06 O ANISOU 213 O ASP A 28 13212 21684 12243 -7173 1904 -1882 O ATOM 214 CB ASP A 28 -10.152 -74.744 29.262 1.00195.99 C ANISOU 214 CB ASP A 28 21896 31222 21348 -7706 2490 -1727 C ATOM 215 CG ASP A 28 -10.313 -73.286 29.630 1.00225.16 C ANISOU 215 CG ASP A 28 25920 34341 25290 -8125 2358 -1666 C ATOM 216 OD1 ASP A 28 -10.888 -72.530 28.817 1.00217.59 O ANISOU 216 OD1 ASP A 28 24700 33426 24547 -8318 2186 -1919 O ATOM 217 OD2 ASP A 28 -9.865 -72.895 30.728 1.00229.18 O ANISOU 217 OD2 ASP A 28 26955 34338 25784 -8220 2403 -1371 O ATOM 218 N ASP A 29 -7.347 -75.773 28.084 1.00201.04 N ANISOU 218 N ASP A 29 22862 31909 21616 -6597 2229 -1681 N ATOM 219 CA ASP A 29 -5.932 -75.591 28.420 1.00163.64 C ANISOU 219 CA ASP A 29 18679 26670 16828 -6312 2123 -1474 C ATOM 220 C ASP A 29 -5.051 -75.252 27.222 1.00134.62 C ANISOU 220 C ASP A 29 15050 22927 13172 -5911 1838 -1616 C ATOM 221 O ASP A 29 -4.989 -76.000 26.248 1.00190.19 O ANISOU 221 O ASP A 29 21810 30370 20083 -5493 1777 -1753 O ATOM 222 CB ASP A 29 -5.384 -76.817 29.159 1.00157.28 C ANISOU 222 CB ASP A 29 18050 25908 15802 -5981 2322 -1265 C ATOM 223 CG ASP A 29 -4.072 -76.529 29.867 1.00175.48 C ANISOU 223 CG ASP A 29 20941 27631 18103 -5846 2241 -1024 C ATOM 224 OD1 ASP A 29 -3.688 -75.344 29.952 1.00160.27 O ANISOU 224 OD1 ASP A 29 19284 25255 16356 -6059 2067 -990 O ATOM 225 OD2 ASP A 29 -3.432 -77.485 30.353 1.00194.82 O ANISOU 225 OD2 ASP A 29 23568 30063 20393 -5526 2341 -886 O ATOM 226 N MET A 30 -4.365 -74.118 27.313 1.00 90.76 N ANISOU 226 N MET A 30 9860 16853 7770 -6031 1672 -1576 N ATOM 227 CA MET A 30 -3.480 -73.662 26.249 1.00109.21 C ANISOU 227 CA MET A 30 12289 19083 10123 -5687 1440 -1705 C ATOM 228 C MET A 30 -2.127 -74.364 26.262 1.00112.82 C ANISOU 228 C MET A 30 13029 19384 10454 -5170 1458 -1518 C ATOM 229 O MET A 30 -1.479 -74.493 25.224 1.00100.86 O ANISOU 229 O MET A 30 11487 17976 8859 -4769 1344 -1608 O ATOM 230 CB MET A 30 -3.277 -72.148 26.337 1.00125.38 C ANISOU 230 CB MET A 30 14594 20628 12415 -6007 1274 -1766 C ATOM 231 CG MET A 30 -4.286 -71.354 25.539 1.00152.68 C ANISOU 231 CG MET A 30 17730 24285 15998 -6313 1130 -2092 C ATOM 232 SD MET A 30 -4.271 -71.846 23.804 1.00136.32 S ANISOU 232 SD MET A 30 15286 22793 13715 -5830 956 -2401 S ATOM 233 CE MET A 30 -5.973 -72.367 23.591 1.00159.46 C ANISOU 233 CE MET A 30 17595 26340 16653 -6136 1009 -2610 C ATOM 234 N PHE A 31 -1.703 -74.810 27.438 1.00 95.14 N ANISOU 234 N PHE A 31 11071 16886 8193 -5190 1601 -1259 N ATOM 235 CA PHE A 31 -0.381 -75.402 27.593 1.00 78.88 C ANISOU 235 CA PHE A 31 9302 14595 6074 -4761 1607 -1082 C ATOM 236 C PHE A 31 -0.403 -76.913 27.417 1.00 84.85 C ANISOU 236 C PHE A 31 9870 15751 6616 -4375 1748 -1047 C ATOM 237 O PHE A 31 0.640 -77.564 27.448 1.00121.53 O ANISOU 237 O PHE A 31 14715 20245 11217 -3996 1762 -917 O ATOM 238 CB PHE A 31 0.209 -75.043 28.957 1.00112.02 C ANISOU 238 CB PHE A 31 13933 18257 10373 -4958 1627 -843 C ATOM 239 CG PHE A 31 0.531 -73.586 29.112 1.00106.12 C ANISOU 239 CG PHE A 31 13428 17022 9872 -5223 1456 -853 C ATOM 240 CD1 PHE A 31 -0.477 -72.655 29.282 1.00100.99 C ANISOU 240 CD1 PHE A 31 12699 16328 9344 -5703 1425 -942 C ATOM 241 CD2 PHE A 31 1.843 -73.149 29.088 1.00123.71 C ANISOU 241 CD2 PHE A 31 15946 18818 12241 -4993 1333 -782 C ATOM 242 CE1 PHE A 31 -0.188 -71.315 29.430 1.00117.72 C ANISOU 242 CE1 PHE A 31 15051 17962 11714 -5927 1257 -963 C ATOM 243 CE2 PHE A 31 2.143 -71.808 29.233 1.00120.44 C ANISOU 243 CE2 PHE A 31 15735 17949 12079 -5206 1176 -812 C ATOM 244 CZ PHE A 31 1.125 -70.889 29.403 1.00 99.39 C ANISOU 244 CZ PHE A 31 13014 15224 9526 -5662 1129 -904 C ATOM 245 N HIS A 32 -1.598 -77.466 27.234 1.00100.01 N ANISOU 245 N HIS A 32 11393 18169 8438 -4475 1853 -1173 N ATOM 246 CA HIS A 32 -1.752 -78.896 27.003 1.00 82.45 C ANISOU 246 CA HIS A 32 8936 16357 6035 -4093 1981 -1179 C ATOM 247 C HIS A 32 -2.381 -79.120 25.633 1.00 85.16 C ANISOU 247 C HIS A 32 8825 17215 6317 -3887 1870 -1414 C ATOM 248 O HIS A 32 -3.542 -78.778 25.410 1.00117.97 O ANISOU 248 O HIS A 32 12622 21682 10518 -4197 1861 -1598 O ATOM 249 CB HIS A 32 -2.604 -79.527 28.108 1.00128.44 C ANISOU 249 CB HIS A 32 14667 22351 11782 -4342 2233 -1121 C ATOM 250 CG HIS A 32 -2.729 -81.019 28.011 1.00104.77 C ANISOU 250 CG HIS A 32 11463 19689 8654 -3915 2359 -1137 C ATOM 251 ND1 HIS A 32 -2.106 -81.762 27.034 1.00149.68 N ANISOU 251 ND1 HIS A 32 17069 25532 14269 -3377 2270 -1169 N ATOM 252 CD2 HIS A 32 -3.409 -81.902 28.781 1.00106.20 C ANISOU 252 CD2 HIS A 32 11534 19988 8828 -3902 2526 -1120 C ATOM 253 CE1 HIS A 32 -2.399 -83.041 27.200 1.00149.12 C ANISOU 253 CE1 HIS A 32 16835 25657 14165 -3063 2375 -1175 C ATOM 254 NE2 HIS A 32 -3.187 -83.152 28.254 1.00110.04 N ANISOU 254 NE2 HIS A 32 11859 20701 9250 -3370 2538 -1162 N ATOM 255 N TRP A 33 -1.602 -79.689 24.718 1.00102.19 N ANISOU 255 N TRP A 33 11005 19449 8375 -3368 1775 -1400 N ATOM 256 CA TRP A 33 -2.073 -79.982 23.370 1.00 99.91 C ANISOU 256 CA TRP A 33 10336 19645 7980 -3089 1629 -1595 C ATOM 257 C TRP A 33 -2.068 -81.473 23.098 1.00108.31 C ANISOU 257 C TRP A 33 11215 21037 8900 -2601 1711 -1551 C ATOM 258 O TRP A 33 -1.299 -82.225 23.692 1.00120.57 O ANISOU 258 O TRP A 33 13030 22352 10430 -2369 1842 -1359 O ATOM 259 CB TRP A 33 -1.198 -79.306 22.313 1.00 84.17 C ANISOU 259 CB TRP A 33 8535 17495 5952 -2859 1423 -1620 C ATOM 260 CG TRP A 33 -1.320 -77.817 22.235 1.00 96.59 C ANISOU 260 CG TRP A 33 10205 18834 7660 -3265 1293 -1753 C ATOM 261 CD1 TRP A 33 -1.754 -76.973 23.215 1.00110.40 C ANISOU 261 CD1 TRP A 33 12046 20303 9598 -3796 1348 -1754 C ATOM 262 CD2 TRP A 33 -1.001 -76.995 21.108 1.00 84.84 C ANISOU 262 CD2 TRP A 33 8755 17358 6123 -3159 1087 -1909 C ATOM 263 NE1 TRP A 33 -1.720 -75.674 22.769 1.00113.90 N ANISOU 263 NE1 TRP A 33 12571 20554 10151 -4021 1178 -1912 N ATOM 264 CE2 TRP A 33 -1.261 -75.661 21.479 1.00 97.87 C ANISOU 264 CE2 TRP A 33 10506 18711 7969 -3636 1022 -2027 C ATOM 265 CE3 TRP A 33 -0.520 -77.257 19.822 1.00 85.24 C ANISOU 265 CE3 TRP A 33 8788 17638 5964 -2698 956 -1956 C ATOM 266 CZ2 TRP A 33 -1.056 -74.594 20.610 1.00117.01 C ANISOU 266 CZ2 TRP A 33 12997 21066 10397 -3659 834 -2229 C ATOM 267 CZ3 TRP A 33 -0.315 -76.196 18.963 1.00 86.07 C ANISOU 267 CZ3 TRP A 33 8973 17700 6028 -2727 780 -2139 C ATOM 268 CH2 TRP A 33 -0.583 -74.881 19.359 1.00108.18 C ANISOU 268 CH2 TRP A 33 11857 20207 9038 -3202 722 -2293 C ATOM 269 N GLN A 34 -2.932 -81.888 22.182 1.00101.53 N ANISOU 269 N GLN A 34 9898 20715 7963 -2436 1609 -1747 N ATOM 270 CA GLN A 34 -2.931 -83.254 21.695 1.00 91.19 C ANISOU 270 CA GLN A 34 8387 19732 6528 -1903 1628 -1726 C ATOM 271 C GLN A 34 -2.622 -83.239 20.208 1.00 93.21 C ANISOU 271 C GLN A 34 8577 20198 6642 -1487 1361 -1785 C ATOM 272 O GLN A 34 -3.238 -82.499 19.441 1.00 94.47 O ANISOU 272 O GLN A 34 8500 20614 6780 -1641 1156 -1998 O ATOM 273 CB GLN A 34 -4.279 -83.926 21.946 1.00 95.35 C ANISOU 273 CB GLN A 34 8384 20761 7084 -2009 1744 -1903 C ATOM 274 CG GLN A 34 -4.263 -85.424 21.693 1.00129.83 C ANISOU 274 CG GLN A 34 12565 25403 11361 -1452 1805 -1874 C ATOM 275 CD GLN A 34 -5.651 -86.023 21.608 1.00157.57 C ANISOU 275 CD GLN A 34 15446 29506 14918 -1489 1866 -2110 C ATOM 276 OE1 GLN A 34 -6.580 -85.402 21.086 1.00173.80 O ANISOU 276 OE1 GLN A 34 17109 31890 17035 -1754 1722 -2331 O ATOM 277 NE2 GLN A 34 -5.803 -87.238 22.124 1.00154.87 N ANISOU 277 NE2 GLN A 34 14984 29297 14564 -1224 2080 -2085 N ATOM 278 N ALA A 35 -1.655 -84.054 19.806 1.00108.56 N ANISOU 278 N ALA A 35 10751 22017 8478 -966 1360 -1593 N ATOM 279 CA ALA A 35 -1.280 -84.158 18.405 1.00 91.75 C ANISOU 279 CA ALA A 35 8621 20075 6163 -522 1131 -1589 C ATOM 280 C ALA A 35 -1.849 -85.429 17.801 1.00 95.27 C ANISOU 280 C ALA A 35 8701 20988 6508 -52 1060 -1635 C ATOM 281 O ALA A 35 -1.770 -86.502 18.393 1.00111.63 O ANISOU 281 O ALA A 35 10760 23019 8636 158 1235 -1533 O ATOM 282 CB ALA A 35 0.228 -84.138 18.260 1.00100.76 C ANISOU 282 CB ALA A 35 10283 20738 7262 -261 1180 -1316 C ATOM 283 N THR A 36 -2.435 -85.299 16.620 1.00130.82 N ANISOU 283 N THR A 36 12903 25938 10866 127 785 -1809 N ATOM 284 CA THR A 36 -2.887 -86.467 15.884 1.00127.01 C ANISOU 284 CA THR A 36 12086 25893 10277 648 653 -1841 C ATOM 285 C THR A 36 -2.010 -86.613 14.656 1.00112.01 C ANISOU 285 C THR A 36 10474 23964 8121 1163 450 -1667 C ATOM 286 O THR A 36 -2.114 -85.819 13.721 1.00151.28 O ANISOU 286 O THR A 36 15438 29122 12920 1141 203 -1788 O ATOM 287 CB THR A 36 -4.348 -86.313 15.435 1.00125.81 C ANISOU 287 CB THR A 36 11302 26345 10154 493 450 -2189 C ATOM 288 OG1 THR A 36 -5.202 -86.253 16.586 1.00157.40 O ANISOU 288 OG1 THR A 36 15020 30390 14393 9 689 -2326 O ATOM 289 CG2 THR A 36 -4.760 -87.488 14.566 1.00118.55 C ANISOU 289 CG2 THR A 36 10032 25883 9127 1094 257 -2224 C ATOM 290 N ILE A 37 -1.146 -87.622 14.653 1.00101.72 N ANISOU 290 N ILE A 37 9443 22421 6786 1622 558 -1386 N ATOM 291 CA ILE A 37 -0.300 -87.860 13.491 1.00106.56 C ANISOU 291 CA ILE A 37 10352 22991 7146 2127 401 -1169 C ATOM 292 C ILE A 37 -0.601 -89.206 12.827 1.00106.52 C ANISOU 292 C ILE A 37 10121 23300 7050 2746 257 -1105 C ATOM 293 O ILE A 37 -0.681 -90.247 13.482 1.00106.58 O ANISOU 293 O ILE A 37 10035 23231 7230 2920 419 -1049 O ATOM 294 CB ILE A 37 1.217 -87.668 13.796 1.00 98.11 C ANISOU 294 CB ILE A 37 9890 21288 6101 2142 620 -845 C ATOM 295 CG1 ILE A 37 1.907 -88.983 14.157 1.00104.59 C ANISOU 295 CG1 ILE A 37 10899 21815 7024 2543 792 -577 C ATOM 296 CG2 ILE A 37 1.418 -86.630 14.892 1.00 94.09 C ANISOU 296 CG2 ILE A 37 9535 20416 5800 1532 811 -914 C ATOM 297 CD1 ILE A 37 3.398 -88.834 14.366 1.00148.74 C ANISOU 297 CD1 ILE A 37 17044 26800 12671 2565 988 -267 C ATOM 298 N MET A 38 -0.809 -89.155 11.517 1.00121.88 N ANISOU 298 N MET A 38 11981 25613 8716 3087 -67 -1133 N ATOM 299 CA MET A 38 -1.196 -90.331 10.757 1.00121.92 C ANISOU 299 CA MET A 38 11742 25965 8618 3698 -282 -1090 C ATOM 300 C MET A 38 0.030 -91.089 10.284 1.00121.42 C ANISOU 300 C MET A 38 12183 25531 8422 4225 -221 -670 C ATOM 301 O MET A 38 1.028 -90.485 9.883 1.00122.66 O ANISOU 301 O MET A 38 12815 25387 8404 4205 -169 -454 O ATOM 302 CB MET A 38 -2.043 -89.929 9.548 1.00126.90 C ANISOU 302 CB MET A 38 12036 27191 8990 3833 -713 -1324 C ATOM 303 CG MET A 38 -3.424 -90.557 9.526 1.00131.60 C ANISOU 303 CG MET A 38 11927 28344 9730 3932 -902 -1631 C ATOM 304 SD MET A 38 -4.599 -89.695 10.584 1.00132.25 S ANISOU 304 SD MET A 38 11508 28608 10131 3132 -758 -2051 S ATOM 305 CE MET A 38 -4.977 -88.266 9.571 1.00145.33 C ANISOU 305 CE MET A 38 13111 30567 11541 2852 -1135 -2315 C ATOM 306 N GLY A 39 -0.043 -92.413 10.341 1.00134.88 N ANISOU 306 N GLY A 39 13777 27241 10232 4692 -209 -558 N ATOM 307 CA GLY A 39 1.011 -93.238 9.787 1.00135.53 C ANISOU 307 CA GLY A 39 14302 26990 10205 5235 -189 -156 C ATOM 308 C GLY A 39 1.138 -92.934 8.311 1.00144.82 C ANISOU 308 C GLY A 39 15620 28444 10963 5582 -520 -36 C ATOM 309 O GLY A 39 0.171 -93.067 7.557 1.00143.94 O ANISOU 309 O GLY A 39 15103 28891 10695 5813 -877 -237 O ATOM 310 N PRO A 40 2.338 -92.518 7.889 1.00136.71 N ANISOU 310 N PRO A 40 15163 27036 9743 5618 -404 285 N ATOM 311 CA PRO A 40 2.590 -92.150 6.495 1.00141.02 C ANISOU 311 CA PRO A 40 15940 27815 9825 5926 -668 430 C ATOM 312 C PRO A 40 2.455 -93.371 5.605 1.00145.68 C ANISOU 312 C PRO A 40 16507 28593 10252 6651 -929 648 C ATOM 313 O PRO A 40 2.821 -94.464 6.028 1.00145.55 O ANISOU 313 O PRO A 40 16577 28248 10479 6937 -775 859 O ATOM 314 CB PRO A 40 4.051 -91.688 6.518 1.00158.74 C ANISOU 314 CB PRO A 40 18817 29491 12007 5810 -350 781 C ATOM 315 CG PRO A 40 4.356 -91.407 7.958 1.00130.97 C ANISOU 315 CG PRO A 40 15306 25535 8922 5286 9 691 C ATOM 316 CD PRO A 40 3.542 -92.383 8.722 1.00131.58 C ANISOU 316 CD PRO A 40 14969 25719 9307 5367 -3 525 C ATOM 317 N ASN A 41 1.926 -93.198 4.401 1.00133.06 N ANISOU 317 N ASN A 41 14797 27508 8254 6958 -1342 583 N ATOM 318 CA ASN A 41 1.902 -94.300 3.453 1.00138.75 C ANISOU 318 CA ASN A 41 15569 28342 8807 7669 -1609 836 C ATOM 319 C ASN A 41 3.330 -94.631 3.043 1.00139.94 C ANISOU 319 C ASN A 41 16414 27845 8911 7888 -1340 1361 C ATOM 320 O ASN A 41 4.223 -93.790 3.163 1.00154.60 O ANISOU 320 O ASN A 41 18658 29302 10779 7498 -1041 1473 O ATOM 321 CB ASN A 41 1.028 -93.968 2.244 1.00144.63 C ANISOU 321 CB ASN A 41 16053 29561 9339 7803 -2041 594 C ATOM 322 CG ASN A 41 -0.432 -93.795 2.616 1.00169.68 C ANISOU 322 CG ASN A 41 18470 33364 12635 7613 -2318 74 C ATOM 323 OD1 ASN A 41 -0.753 -93.221 3.657 1.00165.44 O ANISOU 323 OD1 ASN A 41 17680 32897 12282 7097 -2146 -190 O ATOM 324 ND2 ASN A 41 -1.324 -94.310 1.778 1.00166.22 N ANISOU 324 ND2 ASN A 41 17668 33338 12152 7992 -2720 -82 N ATOM 325 N ASP A 42 3.535 -95.859 2.577 1.00161.98 N ANISOU 325 N ASP A 42 19333 30508 11703 8493 -1438 1669 N ATOM 326 CA ASP A 42 4.867 -96.417 2.347 1.00161.91 C ANISOU 326 CA ASP A 42 19944 29846 11728 8722 -1157 2189 C ATOM 327 C ASP A 42 5.661 -96.534 3.643 1.00155.85 C ANISOU 327 C ASP A 42 19372 28601 11242 8466 -737 2330 C ATOM 328 O ASP A 42 6.891 -96.589 3.617 1.00154.38 O ANISOU 328 O ASP A 42 19701 27819 11138 8420 -418 2699 O ATOM 329 CB ASP A 42 5.667 -95.596 1.327 1.00192.40 C ANISOU 329 CB ASP A 42 24275 33479 15351 8562 -1066 2378 C ATOM 330 CG ASP A 42 5.092 -95.676 -0.070 1.00240.64 C ANISOU 330 CG ASP A 42 30338 39959 21137 8909 -1468 2342 C ATOM 331 OD1 ASP A 42 4.421 -96.682 -0.381 1.00259.42 O ANISOU 331 OD1 ASP A 42 32473 42570 23522 9396 -1765 2338 O ATOM 332 OD2 ASP A 42 5.320 -94.736 -0.862 1.00237.74 O ANISOU 332 OD2 ASP A 42 30178 39634 20518 8700 -1492 2309 O ATOM 333 N SER A 43 4.960 -96.553 4.772 1.00143.52 N ANISOU 333 N SER A 43 17360 27130 10042 8142 -663 1952 N ATOM 334 CA SER A 43 5.570 -96.978 6.024 1.00128.47 C ANISOU 334 CA SER A 43 15566 24635 8611 7897 -267 1997 C ATOM 335 C SER A 43 5.054 -98.360 6.391 1.00131.14 C ANISOU 335 C SER A 43 15624 24951 9251 8318 -342 1942 C ATOM 336 O SER A 43 4.153 -98.884 5.735 1.00140.15 O ANISOU 336 O SER A 43 16422 26565 10263 8750 -697 1834 O ATOM 337 CB SER A 43 5.244 -95.990 7.146 1.00122.97 C ANISOU 337 CB SER A 43 14626 23964 8133 7182 -70 1615 C ATOM 338 OG SER A 43 5.862 -94.737 6.916 1.00172.20 O ANISOU 338 OG SER A 43 21155 30113 14160 6796 45 1670 O ATOM 339 N PRO A 44 5.621 -98.959 7.448 1.00128.11 N ANISOU 339 N PRO A 44 15376 24022 9278 8207 -20 1994 N ATOM 340 CA PRO A 44 4.942-100.059 8.134 1.00129.65 C ANISOU 340 CA PRO A 44 15202 24249 9809 8439 -30 1774 C ATOM 341 C PRO A 44 3.789 -99.498 8.955 1.00127.59 C ANISOU 341 C PRO A 44 14371 24447 9660 7978 -25 1261 C ATOM 342 O PRO A 44 2.812-100.193 9.239 1.00149.38 O ANISOU 342 O PRO A 44 16650 27526 12580 8175 -123 984 O ATOM 343 CB PRO A 44 6.029-100.615 9.054 1.00126.50 C ANISOU 343 CB PRO A 44 15196 23096 9772 8344 335 1964 C ATOM 344 CG PRO A 44 7.311-100.212 8.411 1.00125.74 C ANISOU 344 CG PRO A 44 15693 22575 9507 8337 449 2418 C ATOM 345 CD PRO A 44 7.037 -98.861 7.839 1.00124.59 C ANISOU 345 CD PRO A 44 15486 22867 8984 8009 335 2324 C ATOM 346 N TYR A 45 3.918 -98.224 9.314 1.00123.19 N ANISOU 346 N TYR A 45 13871 23910 9024 7365 102 1144 N ATOM 347 CA TYR A 45 2.980 -97.559 10.206 1.00120.73 C ANISOU 347 CA TYR A 45 13113 23919 8838 6827 168 709 C ATOM 348 C TYR A 45 1.753 -97.092 9.444 1.00125.95 C ANISOU 348 C TYR A 45 13274 25310 9270 6852 -183 429 C ATOM 349 O TYR A 45 0.840 -96.503 10.023 1.00123.31 O ANISOU 349 O TYR A 45 12518 25308 9026 6411 -165 63 O ATOM 350 CB TYR A 45 3.654 -96.361 10.875 1.00114.94 C ANISOU 350 CB TYR A 45 12671 22866 8136 6180 420 715 C ATOM 351 CG TYR A 45 4.995 -96.686 11.485 1.00111.64 C ANISOU 351 CG TYR A 45 12769 21720 7928 6140 726 1011 C ATOM 352 CD1 TYR A 45 5.093 -97.136 12.795 1.00109.01 C ANISOU 352 CD1 TYR A 45 12418 21068 7931 5931 974 887 C ATOM 353 CD2 TYR A 45 6.166 -96.541 10.751 1.00149.62 C ANISOU 353 CD2 TYR A 45 18082 26168 12599 6304 769 1405 C ATOM 354 CE1 TYR A 45 6.322 -97.435 13.354 1.00114.15 C ANISOU 354 CE1 TYR A 45 13520 21053 8799 5887 1215 1126 C ATOM 355 CE2 TYR A 45 7.396 -96.838 11.303 1.00126.57 C ANISOU 355 CE2 TYR A 45 15593 22575 9921 6243 1048 1662 C ATOM 356 CZ TYR A 45 7.468 -97.284 12.603 1.00106.34 C ANISOU 356 CZ TYR A 45 12986 19700 7717 6034 1250 1510 C ATOM 357 OH TYR A 45 8.692 -97.580 13.156 1.00104.09 O ANISOU 357 OH TYR A 45 13110 18744 7694 5965 1491 1735 O ATOM 358 N GLN A 46 1.749 -97.349 8.140 1.00128.96 N ANISOU 358 N GLN A 46 13718 25926 9353 7363 -510 610 N ATOM 359 CA GLN A 46 0.640 -96.972 7.275 1.00133.26 C ANISOU 359 CA GLN A 46 13807 27170 9658 7461 -916 351 C ATOM 360 C GLN A 46 -0.680 -97.503 7.811 1.00135.75 C ANISOU 360 C GLN A 46 13410 27924 10243 7463 -989 -56 C ATOM 361 O GLN A 46 -0.787 -98.672 8.186 1.00137.52 O ANISOU 361 O GLN A 46 13504 28033 10715 7827 -909 -37 O ATOM 362 CB GLN A 46 0.881 -97.494 5.859 1.00143.54 C ANISOU 362 CB GLN A 46 15314 28611 10613 8143 -1272 652 C ATOM 363 CG GLN A 46 -0.336 -97.462 4.956 1.00144.57 C ANISOU 363 CG GLN A 46 14908 29480 10540 8403 -1765 375 C ATOM 364 CD GLN A 46 -0.053 -98.051 3.593 1.00158.58 C ANISOU 364 CD GLN A 46 16939 31364 11952 9123 -2137 709 C ATOM 365 OE1 GLN A 46 1.063 -97.953 3.082 1.00184.66 O ANISOU 365 OE1 GLN A 46 20883 34282 14997 9270 -2042 1137 O ATOM 366 NE2 GLN A 46 -1.061 -98.675 2.995 1.00156.47 N ANISOU 366 NE2 GLN A 46 16167 31621 11664 9581 -2560 525 N ATOM 367 N GLY A 47 -1.679 -96.630 7.860 1.00136.10 N ANISOU 367 N GLY A 47 12992 28458 10260 7037 -1118 -437 N ATOM 368 CA GLY A 47 -3.014 -97.016 8.277 1.00139.13 C ANISOU 368 CA GLY A 47 12642 29328 10894 6990 -1184 -843 C ATOM 369 C GLY A 47 -3.259 -96.770 9.748 1.00134.86 C ANISOU 369 C GLY A 47 11953 28613 10674 6389 -758 -1054 C ATOM 370 O GLY A 47 -4.394 -96.815 10.217 1.00136.86 O ANISOU 370 O GLY A 47 11599 29276 11126 6172 -735 -1414 O ATOM 371 N GLY A 48 -2.183 -96.503 10.479 1.00133.77 N ANISOU 371 N GLY A 48 12372 27870 10583 6114 -420 -824 N ATOM 372 CA GLY A 48 -2.279 -96.295 11.909 1.00131.82 C ANISOU 372 CA GLY A 48 12085 27400 10599 5575 -26 -974 C ATOM 373 C GLY A 48 -2.501 -94.840 12.260 1.00126.47 C ANISOU 373 C GLY A 48 11400 26777 9875 4859 32 -1137 C ATOM 374 O GLY A 48 -2.198 -93.949 11.468 1.00126.01 O ANISOU 374 O GLY A 48 11545 26756 9579 4771 -167 -1069 O ATOM 375 N VAL A 49 -3.040 -94.604 13.452 1.00120.14 N ANISOU 375 N VAL A 49 10378 25977 9291 4356 309 -1353 N ATOM 376 CA VAL A 49 -3.227 -93.247 13.946 1.00117.02 C ANISOU 376 CA VAL A 49 10012 25549 8900 3651 397 -1487 C ATOM 377 C VAL A 49 -2.577 -93.105 15.315 1.00114.17 C ANISOU 377 C VAL A 49 10021 24658 8700 3262 787 -1383 C ATOM 378 O VAL A 49 -2.943 -93.794 16.268 1.00123.08 O ANISOU 378 O VAL A 49 10983 25781 10003 3218 1031 -1478 O ATOM 379 CB VAL A 49 -4.710 -92.865 14.040 1.00120.47 C ANISOU 379 CB VAL A 49 9770 26564 9437 3308 316 -1878 C ATOM 380 CG1 VAL A 49 -4.857 -91.473 14.631 1.00117.33 C ANISOU 380 CG1 VAL A 49 9457 26046 9077 2563 426 -1990 C ATOM 381 CG2 VAL A 49 -5.357 -92.936 12.669 1.00125.76 C ANISOU 381 CG2 VAL A 49 10055 27774 9952 3676 -128 -2015 C ATOM 382 N PHE A 50 -1.608 -92.200 15.401 1.00111.97 N ANISOU 382 N PHE A 50 10243 23947 8352 2994 836 -1199 N ATOM 383 CA PHE A 50 -0.796 -92.061 16.597 1.00103.03 C ANISOU 383 CA PHE A 50 9524 22260 7361 2691 1145 -1062 C ATOM 384 C PHE A 50 -1.060 -90.743 17.311 1.00106.48 C ANISOU 384 C PHE A 50 9983 22621 7853 1993 1236 -1190 C ATOM 385 O PHE A 50 -1.046 -89.674 16.694 1.00 99.91 O ANISOU 385 O PHE A 50 9196 21850 6916 1784 1068 -1229 O ATOM 386 CB PHE A 50 0.684 -92.188 16.241 1.00100.38 C ANISOU 386 CB PHE A 50 9768 21401 6970 2972 1160 -716 C ATOM 387 CG PHE A 50 1.041 -93.510 15.622 1.00103.08 C ANISOU 387 CG PHE A 50 10164 21715 7288 3646 1093 -543 C ATOM 388 CD1 PHE A 50 0.933 -93.703 14.255 1.00106.64 C ANISOU 388 CD1 PHE A 50 10530 22461 7527 4092 806 -467 C ATOM 389 CD2 PHE A 50 1.480 -94.560 16.409 1.00119.02 C ANISOU 389 CD2 PHE A 50 12334 23400 9488 3844 1300 -459 C ATOM 390 CE1 PHE A 50 1.258 -94.918 13.689 1.00109.53 C ANISOU 390 CE1 PHE A 50 10969 22767 7878 4726 730 -279 C ATOM 391 CE2 PHE A 50 1.808 -95.776 15.847 1.00109.24 C ANISOU 391 CE2 PHE A 50 11157 22087 8260 4469 1234 -302 C ATOM 392 CZ PHE A 50 1.697 -95.955 14.485 1.00113.61 C ANISOU 392 CZ PHE A 50 11634 22916 8618 4913 950 -196 C ATOM 393 N PHE A 51 -1.307 -90.828 18.615 1.00 98.89 N ANISOU 393 N PHE A 51 9009 21518 7046 1647 1500 -1259 N ATOM 394 CA PHE A 51 -1.580 -89.647 19.421 1.00 96.70 C ANISOU 394 CA PHE A 51 8780 21124 6836 987 1601 -1350 C ATOM 395 C PHE A 51 -0.362 -89.223 20.218 1.00103.89 C ANISOU 395 C PHE A 51 10262 21398 7813 793 1745 -1130 C ATOM 396 O PHE A 51 0.400 -90.055 20.709 1.00107.90 O ANISOU 396 O PHE A 51 11040 21584 8375 1042 1878 -976 O ATOM 397 CB PHE A 51 -2.748 -89.889 20.371 1.00 98.89 C ANISOU 397 CB PHE A 51 8667 21693 7215 668 1803 -1563 C ATOM 398 CG PHE A 51 -4.056 -90.116 19.676 1.00114.15 C ANISOU 398 CG PHE A 51 9958 24270 9144 744 1669 -1824 C ATOM 399 CD1 PHE A 51 -4.559 -89.172 18.798 1.00125.48 C ANISOU 399 CD1 PHE A 51 11171 25975 10533 558 1408 -1966 C ATOM 400 CD2 PHE A 51 -4.789 -91.265 19.912 1.00126.43 C ANISOU 400 CD2 PHE A 51 11112 26166 10759 1001 1798 -1956 C ATOM 401 CE1 PHE A 51 -5.763 -89.376 18.160 1.00110.54 C ANISOU 401 CE1 PHE A 51 8656 24679 8664 618 1250 -2230 C ATOM 402 CE2 PHE A 51 -5.994 -91.472 19.279 1.00112.58 C ANISOU 402 CE2 PHE A 51 8716 25016 9043 1074 1665 -2213 C ATOM 403 CZ PHE A 51 -6.480 -90.527 18.402 1.00115.34 C ANISOU 403 CZ PHE A 51 8837 25631 9358 875 1379 -2348 C ATOM 404 N LEU A 52 -0.184 -87.914 20.340 1.00112.19 N ANISOU 404 N LEU A 52 11481 22262 8883 352 1700 -1136 N ATOM 405 CA LEU A 52 0.888 -87.352 21.140 1.00 93.04 C ANISOU 405 CA LEU A 52 9545 19251 6555 118 1810 -959 C ATOM 406 C LEU A 52 0.283 -86.388 22.147 1.00 86.71 C ANISOU 406 C LEU A 52 8715 18387 5844 -505 1897 -1070 C ATOM 407 O LEU A 52 -0.788 -85.823 21.920 1.00 92.75 O ANISOU 407 O LEU A 52 9135 19509 6598 -788 1831 -1267 O ATOM 408 CB LEU A 52 1.897 -86.609 20.258 1.00 86.91 C ANISOU 408 CB LEU A 52 9069 18221 5731 227 1669 -822 C ATOM 409 CG LEU A 52 2.903 -87.366 19.384 1.00 83.51 C ANISOU 409 CG LEU A 52 8855 17652 5223 784 1627 -606 C ATOM 410 CD1 LEU A 52 2.233 -88.171 18.287 1.00108.61 C ANISOU 410 CD1 LEU A 52 11703 21333 8230 1233 1473 -670 C ATOM 411 CD2 LEU A 52 3.892 -86.389 18.771 1.00113.57 C ANISOU 411 CD2 LEU A 52 12984 21171 8997 745 1567 -481 C ATOM 412 N THR A 53 0.964 -86.222 23.270 1.00 94.86 N ANISOU 412 N THR A 53 10121 18903 7017 -713 2013 -932 N ATOM 413 CA THR A 53 0.633 -85.166 24.208 1.00101.51 C ANISOU 413 CA THR A 53 11061 19547 7962 -1281 2053 -966 C ATOM 414 C THR A 53 1.790 -84.181 24.235 1.00 90.31 C ANISOU 414 C THR A 53 10052 17629 6631 -1395 1972 -829 C ATOM 415 O THR A 53 2.969 -84.569 24.154 1.00 93.52 O ANISOU 415 O THR A 53 10753 17691 7090 -1097 1972 -661 O ATOM 416 CB THR A 53 0.331 -85.700 25.624 1.00 93.08 C ANISOU 416 CB THR A 53 10086 18298 6982 -1459 2229 -933 C ATOM 417 OG1 THR A 53 1.322 -86.666 25.996 1.00120.71 O ANISOU 417 OG1 THR A 53 13876 21468 10519 -1100 2284 -790 O ATOM 418 CG2 THR A 53 -1.047 -86.355 25.671 1.00 98.71 C ANISOU 418 CG2 THR A 53 10331 19540 7634 -1491 2341 -1114 C ATOM 419 N ILE A 54 1.434 -82.906 24.327 1.00 81.88 N ANISOU 419 N ILE A 54 8978 16550 5583 -1837 1919 -916 N ATOM 420 CA ILE A 54 2.378 -81.807 24.268 1.00 87.58 C ANISOU 420 CA ILE A 54 10026 16828 6423 -1966 1822 -837 C ATOM 421 C ILE A 54 2.144 -80.882 25.453 1.00106.58 C ANISOU 421 C ILE A 54 12599 18932 8965 -2489 1852 -826 C ATOM 422 O ILE A 54 1.073 -80.297 25.585 1.00109.64 O ANISOU 422 O ILE A 54 12777 19523 9360 -2860 1842 -963 O ATOM 423 CB ILE A 54 2.178 -80.997 22.977 1.00 75.90 C ANISOU 423 CB ILE A 54 8393 15559 4886 -1936 1650 -983 C ATOM 424 CG1 ILE A 54 2.437 -81.876 21.755 1.00 78.35 C ANISOU 424 CG1 ILE A 54 8583 16165 5021 -1396 1595 -961 C ATOM 425 CG2 ILE A 54 3.070 -79.767 22.964 1.00 87.97 C ANISOU 425 CG2 ILE A 54 10235 16637 6553 -2097 1577 -942 C ATOM 426 CD1 ILE A 54 1.979 -81.257 20.460 1.00 93.98 C ANISOU 426 CD1 ILE A 54 10357 18489 6864 -1342 1405 -1143 C ATOM 427 N HIS A 55 3.142 -80.759 26.317 1.00 86.24 N ANISOU 427 N HIS A 55 10398 15860 6508 -2522 1876 -657 N ATOM 428 CA HIS A 55 3.051 -79.845 27.447 1.00116.11 C ANISOU 428 CA HIS A 55 14398 19301 10416 -2977 1864 -610 C ATOM 429 C HIS A 55 4.059 -78.715 27.310 1.00102.32 C ANISOU 429 C HIS A 55 12919 17090 8868 -3034 1725 -561 C ATOM 430 O HIS A 55 5.274 -78.929 27.365 1.00116.80 O ANISOU 430 O HIS A 55 14982 18597 10800 -2787 1712 -436 O ATOM 431 CB HIS A 55 3.222 -80.587 28.775 1.00115.23 C ANISOU 431 CB HIS A 55 14498 19011 10274 -3015 1979 -476 C ATOM 432 CG HIS A 55 2.037 -81.418 29.152 1.00103.44 C ANISOU 432 CG HIS A 55 12748 17866 8690 -3044 2102 -545 C ATOM 433 ND1 HIS A 55 1.910 -82.742 28.791 1.00 77.26 N ANISOU 433 ND1 HIS A 55 9244 14806 5304 -2633 2177 -581 N ATOM 434 CD2 HIS A 55 0.916 -81.108 29.846 1.00123.55 C ANISOU 434 CD2 HIS A 55 15188 20548 11207 -3442 2183 -586 C ATOM 435 CE1 HIS A 55 0.766 -83.214 29.253 1.00130.43 C ANISOU 435 CE1 HIS A 55 15751 21833 11974 -2767 2303 -660 C ATOM 436 NE2 HIS A 55 0.143 -82.243 29.896 1.00154.84 N ANISOU 436 NE2 HIS A 55 18885 24859 15088 -3262 2317 -658 N ATOM 437 N PHE A 56 3.536 -77.510 27.104 1.00 88.37 N ANISOU 437 N PHE A 56 11097 15295 7186 -3361 1629 -679 N ATOM 438 CA PHE A 56 4.358 -76.318 27.012 1.00 87.71 C ANISOU 438 CA PHE A 56 11239 14776 7312 -3444 1503 -675 C ATOM 439 C PHE A 56 4.772 -75.882 28.404 1.00 93.81 C ANISOU 439 C PHE A 56 12333 15057 8253 -3699 1471 -519 C ATOM 440 O PHE A 56 3.918 -75.669 29.267 1.00113.37 O ANISOU 440 O PHE A 56 14831 17537 10708 -4060 1492 -495 O ATOM 441 CB PHE A 56 3.581 -75.184 26.341 1.00105.48 C ANISOU 441 CB PHE A 56 13325 17151 9603 -3708 1397 -889 C ATOM 442 CG PHE A 56 3.277 -75.430 24.893 1.00 96.18 C ANISOU 442 CG PHE A 56 11865 16430 8250 -3445 1365 -1066 C ATOM 443 CD1 PHE A 56 4.202 -75.107 23.915 1.00 95.21 C ANISOU 443 CD1 PHE A 56 11828 16226 8121 -3145 1314 -1100 C ATOM 444 CD2 PHE A 56 2.064 -75.972 24.507 1.00114.20 C ANISOU 444 CD2 PHE A 56 13791 19234 10368 -3494 1384 -1200 C ATOM 445 CE1 PHE A 56 3.926 -75.326 22.580 1.00 91.18 C ANISOU 445 CE1 PHE A 56 11100 16146 7397 -2887 1264 -1247 C ATOM 446 CE2 PHE A 56 1.781 -76.191 23.170 1.00 99.49 C ANISOU 446 CE2 PHE A 56 11671 17799 8331 -3229 1304 -1366 C ATOM 447 CZ PHE A 56 2.714 -75.868 22.208 1.00110.13 C ANISOU 447 CZ PHE A 56 13154 19060 9629 -2921 1234 -1382 C ATOM 448 N PRO A 57 6.086 -75.756 28.630 1.00 72.16 N ANISOU 448 N PRO A 57 9841 11895 5683 -3514 1418 -404 N ATOM 449 CA PRO A 57 6.600 -75.264 29.910 1.00111.69 C ANISOU 449 CA PRO A 57 15159 16405 10874 -3718 1325 -265 C ATOM 450 C PRO A 57 6.081 -73.860 30.189 1.00109.46 C ANISOU 450 C PRO A 57 14943 15899 10746 -4113 1202 -327 C ATOM 451 O PRO A 57 5.887 -73.087 29.252 1.00 87.41 O ANISOU 451 O PRO A 57 12012 13183 8017 -4139 1159 -495 O ATOM 452 CB PRO A 57 8.110 -75.214 29.678 1.00134.59 C ANISOU 452 CB PRO A 57 18202 18950 13986 -3417 1277 -201 C ATOM 453 CG PRO A 57 8.359 -76.207 28.603 1.00120.03 C ANISOU 453 CG PRO A 57 16178 17440 11989 -3031 1407 -224 C ATOM 454 CD PRO A 57 7.167 -76.127 27.703 1.00 97.04 C ANISOU 454 CD PRO A 57 12987 15020 8865 -3096 1446 -388 C ATOM 455 N THR A 58 5.863 -73.550 31.463 1.00129.04 N ANISOU 455 N THR A 58 17655 18099 13276 -4407 1137 -194 N ATOM 456 CA THR A 58 5.403 -72.228 31.874 1.00107.06 C ANISOU 456 CA THR A 58 14991 15021 10667 -4790 1008 -209 C ATOM 457 C THR A 58 6.287 -71.093 31.343 1.00126.05 C ANISOU 457 C THR A 58 17461 17049 13382 -4698 855 -305 C ATOM 458 O THR A 58 5.808 -69.984 31.108 1.00133.46 O ANISOU 458 O THR A 58 18385 17859 14465 -4939 769 -426 O ATOM 459 CB THR A 58 5.291 -72.135 33.410 1.00144.92 C ANISOU 459 CB THR A 58 20107 19500 15456 -5052 940 11 C ATOM 460 OG1 THR A 58 5.284 -70.755 33.806 1.00185.17 O ANISOU 460 OG1 THR A 58 25395 24147 20813 -5326 755 33 O ATOM 461 CG2 THR A 58 6.460 -72.838 34.071 1.00139.95 C ANISOU 461 CG2 THR A 58 19689 18641 14844 -4770 881 153 C ATOM 462 N ASP A 59 7.573 -71.380 31.160 1.00136.42 N ANISOU 462 N ASP A 59 18838 18180 14815 -4352 836 -265 N ATOM 463 CA ASP A 59 8.476 -70.448 30.507 1.00104.73 C ANISOU 463 CA ASP A 59 14829 13885 11076 -4205 758 -379 C ATOM 464 C ASP A 59 8.739 -70.895 29.072 1.00122.22 C ANISOU 464 C ASP A 59 16810 16470 13156 -3883 905 -517 C ATOM 465 O ASP A 59 9.404 -71.897 28.825 1.00150.83 O ANISOU 465 O ASP A 59 20401 20213 16694 -3578 1012 -429 O ATOM 466 CB ASP A 59 9.789 -70.328 31.276 1.00131.58 C ANISOU 466 CB ASP A 59 18443 16797 14755 -4062 641 -242 C ATOM 467 CG ASP A 59 10.385 -71.679 31.644 1.00173.80 C ANISOU 467 CG ASP A 59 23821 22233 19982 -3824 719 -94 C ATOM 468 OD1 ASP A 59 9.619 -72.658 31.693 1.00206.94 O ANISOU 468 OD1 ASP A 59 27946 26810 23872 -3840 839 -59 O ATOM 469 OD2 ASP A 59 11.613 -71.754 31.874 1.00159.33 O ANISOU 469 OD2 ASP A 59 22068 20084 18385 -3623 661 -32 O ATOM 470 N TYR A 60 8.182 -70.162 28.123 1.00124.75 N ANISOU 470 N TYR A 60 16985 16971 13445 -3954 900 -734 N ATOM 471 CA TYR A 60 8.250 -70.543 26.724 1.00 84.11 C ANISOU 471 CA TYR A 60 11634 12229 8095 -3667 1015 -870 C ATOM 472 C TYR A 60 8.498 -69.256 25.924 1.00111.58 C ANISOU 472 C TYR A 60 15107 15566 11722 -3672 956 -1102 C ATOM 473 O TYR A 60 8.142 -68.179 26.391 1.00174.68 O ANISOU 473 O TYR A 60 23184 23262 19923 -3963 823 -1194 O ATOM 474 CB TYR A 60 6.937 -71.242 26.358 1.00 84.40 C ANISOU 474 CB TYR A 60 11443 12807 7820 -3760 1064 -938 C ATOM 475 CG TYR A 60 6.938 -71.899 25.001 1.00 96.10 C ANISOU 475 CG TYR A 60 12720 14758 9037 -3421 1152 -1034 C ATOM 476 CD1 TYR A 60 7.471 -73.171 24.814 1.00 92.49 C ANISOU 476 CD1 TYR A 60 12242 14470 8430 -3075 1275 -870 C ATOM 477 CD2 TYR A 60 6.421 -71.239 23.899 1.00139.65 C ANISOU 477 CD2 TYR A 60 18084 20531 14448 -3436 1093 -1290 C ATOM 478 CE1 TYR A 60 7.483 -73.762 23.563 1.00104.24 C ANISOU 478 CE1 TYR A 60 13576 16363 9666 -2745 1338 -924 C ATOM 479 CE2 TYR A 60 6.429 -71.816 22.655 1.00 87.86 C ANISOU 479 CE2 TYR A 60 11369 14405 7609 -3108 1142 -1364 C ATOM 480 CZ TYR A 60 6.958 -73.074 22.485 1.00 74.38 C ANISOU 480 CZ TYR A 60 9656 12853 5751 -2758 1265 -1164 C ATOM 481 OH TYR A 60 6.959 -73.637 21.233 1.00 92.52 O ANISOU 481 OH TYR A 60 11828 15565 7760 -2416 1295 -1209 O ATOM 482 N PRO A 61 9.162 -69.339 24.758 1.00 86.26 N ANISOU 482 N PRO A 61 11829 12533 8414 -3342 1061 -1191 N ATOM 483 CA PRO A 61 9.870 -70.436 24.085 1.00 90.40 C ANISOU 483 CA PRO A 61 12304 13296 8747 -2951 1227 -1062 C ATOM 484 C PRO A 61 11.149 -70.922 24.792 1.00101.30 C ANISOU 484 C PRO A 61 13831 14302 10358 -2785 1298 -825 C ATOM 485 O PRO A 61 11.701 -71.916 24.336 1.00138.59 O ANISOU 485 O PRO A 61 18525 19181 14950 -2490 1439 -693 O ATOM 486 CB PRO A 61 10.203 -69.854 22.722 1.00110.51 C ANISOU 486 CB PRO A 61 14799 16012 11179 -2743 1292 -1259 C ATOM 487 CG PRO A 61 10.211 -68.388 22.901 1.00137.37 C ANISOU 487 CG PRO A 61 18274 19074 14845 -2964 1182 -1467 C ATOM 488 CD PRO A 61 9.146 -68.116 23.933 1.00135.31 C ANISOU 488 CD PRO A 61 18023 18699 14692 -3371 1013 -1470 C ATOM 489 N PHE A 62 11.634 -70.231 25.822 1.00101.60 N ANISOU 489 N PHE A 62 14015 13847 10743 -2956 1189 -779 N ATOM 490 CA PHE A 62 12.972 -70.502 26.369 1.00 83.93 C ANISOU 490 CA PHE A 62 11880 11227 8782 -2789 1226 -610 C ATOM 491 C PHE A 62 13.306 -71.962 26.669 1.00101.99 C ANISOU 491 C PHE A 62 14178 13619 10955 -2609 1314 -397 C ATOM 492 O PHE A 62 14.470 -72.363 26.567 1.00114.12 O ANISOU 492 O PHE A 62 15736 14968 12657 -2384 1415 -289 O ATOM 493 CB PHE A 62 13.209 -69.708 27.650 1.00 91.10 C ANISOU 493 CB PHE A 62 12942 11627 10045 -3023 1023 -573 C ATOM 494 CG PHE A 62 12.987 -68.245 27.492 1.00 98.75 C ANISOU 494 CG PHE A 62 13927 12388 11205 -3189 917 -776 C ATOM 495 CD1 PHE A 62 13.338 -67.600 26.313 1.00 74.50 C ANISOU 495 CD1 PHE A 62 10760 9409 8138 -3026 1038 -976 C ATOM 496 CD2 PHE A 62 12.422 -67.512 28.509 1.00177.10 C ANISOU 496 CD2 PHE A 62 23985 22015 21292 -3500 700 -769 C ATOM 497 CE1 PHE A 62 13.124 -66.250 26.176 1.00109.84 C ANISOU 497 CE1 PHE A 62 15258 13675 12800 -3167 937 -1201 C ATOM 498 CE2 PHE A 62 12.203 -66.168 28.381 1.00197.76 C ANISOU 498 CE2 PHE A 62 26631 24393 24116 -3648 591 -960 C ATOM 499 CZ PHE A 62 12.559 -65.530 27.206 1.00191.23 C ANISOU 499 CZ PHE A 62 25691 23653 23315 -3476 706 -1197 C ATOM 500 N LYS A 63 12.307 -72.754 27.051 1.00 95.55 N ANISOU 500 N LYS A 63 13339 13085 9882 -2712 1287 -347 N ATOM 501 CA LYS A 63 12.489 -74.190 27.202 1.00 77.93 C ANISOU 501 CA LYS A 63 11103 11003 7505 -2510 1382 -190 C ATOM 502 C LYS A 63 11.632 -74.915 26.173 1.00 87.44 C ANISOU 502 C LYS A 63 12127 12760 8335 -2361 1492 -244 C ATOM 503 O LYS A 63 10.560 -74.440 25.806 1.00131.60 O ANISOU 503 O LYS A 63 17602 18640 13762 -2530 1444 -395 O ATOM 504 CB LYS A 63 12.069 -74.640 28.610 1.00 97.89 C ANISOU 504 CB LYS A 63 13756 13404 10032 -2716 1268 -93 C ATOM 505 CG LYS A 63 13.071 -74.373 29.704 1.00107.98 C ANISOU 505 CG LYS A 63 15226 14158 11643 -2767 1133 6 C ATOM 506 CD LYS A 63 12.455 -74.737 31.044 1.00135.28 C ANISOU 506 CD LYS A 63 18841 17561 14999 -2989 1010 88 C ATOM 507 CE LYS A 63 13.497 -74.822 32.127 1.00151.01 C ANISOU 507 CE LYS A 63 21027 19090 17259 -2968 852 193 C ATOM 508 NZ LYS A 63 14.230 -73.542 32.266 1.00180.26 N ANISOU 508 NZ LYS A 63 24778 22372 21342 -3039 700 159 N ATOM 509 N PRO A 64 12.106 -76.079 25.711 1.00 85.64 N ANISOU 509 N PRO A 64 11872 12670 7997 -2041 1623 -124 N ATOM 510 CA PRO A 64 11.390 -76.845 24.687 1.00 83.52 C ANISOU 510 CA PRO A 64 11434 12915 7385 -1833 1704 -156 C ATOM 511 C PRO A 64 10.127 -77.482 25.246 1.00 93.76 C ANISOU 511 C PRO A 64 12618 14520 8485 -1977 1660 -196 C ATOM 512 O PRO A 64 10.075 -77.778 26.440 1.00118.41 O ANISOU 512 O PRO A 64 15847 17446 11698 -2135 1626 -128 O ATOM 513 CB PRO A 64 12.392 -77.931 24.301 1.00 73.15 C ANISOU 513 CB PRO A 64 10179 11526 6088 -1464 1844 28 C ATOM 514 CG PRO A 64 13.239 -78.109 25.507 1.00 97.86 C ANISOU 514 CG PRO A 64 13474 14180 9527 -1548 1812 139 C ATOM 515 CD PRO A 64 13.339 -76.760 26.154 1.00111.94 C ANISOU 515 CD PRO A 64 15329 15656 11547 -1859 1682 48 C ATOM 516 N PRO A 65 9.113 -77.687 24.394 1.00 89.11 N ANISOU 516 N PRO A 65 11808 14425 7623 -1922 1661 -315 N ATOM 517 CA PRO A 65 7.891 -78.380 24.819 1.00 92.75 C ANISOU 517 CA PRO A 65 12099 15235 7909 -2033 1659 -366 C ATOM 518 C PRO A 65 8.174 -79.846 25.125 1.00 95.21 C ANISOU 518 C PRO A 65 12432 15586 8156 -1747 1760 -225 C ATOM 519 O PRO A 65 9.064 -80.443 24.514 1.00 95.37 O ANISOU 519 O PRO A 65 12520 15530 8187 -1397 1824 -109 O ATOM 520 CB PRO A 65 6.974 -78.257 23.599 1.00102.40 C ANISOU 520 CB PRO A 65 13048 16965 8893 -1960 1617 -538 C ATOM 521 CG PRO A 65 7.896 -78.033 22.445 1.00 65.75 C ANISOU 521 CG PRO A 65 8482 12287 4213 -1652 1635 -507 C ATOM 522 CD PRO A 65 9.041 -77.241 22.993 1.00 67.27 C ANISOU 522 CD PRO A 65 8931 11932 4697 -1759 1656 -427 C ATOM 523 N LYS A 66 7.439 -80.413 26.076 1.00 86.87 N ANISOU 523 N LYS A 66 11336 14632 7039 -1900 1788 -235 N ATOM 524 CA LYS A 66 7.589 -81.828 26.392 1.00 92.14 C ANISOU 524 CA LYS A 66 12014 15360 7635 -1625 1885 -151 C ATOM 525 C LYS A 66 6.598 -82.615 25.555 1.00 84.31 C ANISOU 525 C LYS A 66 10704 14926 6406 -1411 1929 -247 C ATOM 526 O LYS A 66 5.391 -82.434 25.679 1.00104.85 O ANISOU 526 O LYS A 66 13075 17868 8895 -1640 1928 -385 O ATOM 527 CB LYS A 66 7.361 -82.090 27.885 1.00108.96 C ANISOU 527 CB LYS A 66 14289 17320 9791 -1866 1907 -126 C ATOM 528 CG LYS A 66 8.534 -81.700 28.780 1.00 97.32 C ANISOU 528 CG LYS A 66 13145 15274 8557 -1956 1832 -10 C ATOM 529 CD LYS A 66 8.235 -80.443 29.583 1.00141.77 C ANISOU 529 CD LYS A 66 18894 20695 14278 -2394 1723 -27 C ATOM 530 CE LYS A 66 7.112 -80.681 30.583 1.00177.47 C ANISOU 530 CE LYS A 66 23405 25413 18612 -2673 1775 -57 C ATOM 531 NZ LYS A 66 6.796 -79.458 31.375 1.00146.77 N ANISOU 531 NZ LYS A 66 19668 21289 14808 -3106 1667 -34 N ATOM 532 N VAL A 67 7.105 -83.481 24.686 1.00 87.13 N ANISOU 532 N VAL A 67 11036 15366 6705 -972 1963 -169 N ATOM 533 CA VAL A 67 6.244 -84.178 23.742 1.00 95.08 C ANISOU 533 CA VAL A 67 11735 16895 7495 -708 1958 -254 C ATOM 534 C VAL A 67 6.408 -85.687 23.845 1.00 87.25 C ANISOU 534 C VAL A 67 10735 15946 6470 -321 2048 -177 C ATOM 535 O VAL A 67 7.530 -86.193 23.853 1.00 68.88 O ANISOU 535 O VAL A 67 8650 13260 4260 -80 2091 -13 O ATOM 536 CB VAL A 67 6.555 -83.756 22.300 1.00 69.94 C ANISOU 536 CB VAL A 67 8511 13850 4212 -480 1875 -240 C ATOM 537 CG1 VAL A 67 5.576 -84.402 21.345 1.00 84.63 C ANISOU 537 CG1 VAL A 67 10038 16271 5845 -217 1808 -344 C ATOM 538 CG2 VAL A 67 6.507 -82.244 22.168 1.00106.32 C ANISOU 538 CG2 VAL A 67 13156 18368 8871 -832 1789 -344 C ATOM 539 N ALA A 68 5.292 -86.408 23.916 1.00 83.07 N ANISOU 539 N ALA A 68 9916 15816 5829 -259 2074 -306 N ATOM 540 CA ALA A 68 5.379 -87.866 23.999 1.00 73.87 C ANISOU 540 CA ALA A 68 8722 14722 4624 137 2167 -269 C ATOM 541 C ALA A 68 4.211 -88.623 23.358 1.00103.75 C ANISOU 541 C ALA A 68 12092 19069 8260 378 2151 -413 C ATOM 542 O ALA A 68 3.071 -88.170 23.395 1.00103.65 O ANISOU 542 O ALA A 68 11778 19403 8201 112 2121 -585 O ATOM 543 CB ALA A 68 5.566 -88.300 25.446 1.00 99.50 C ANISOU 543 CB ALA A 68 12160 17688 7957 -25 2284 -273 C ATOM 544 N PHE A 69 4.511 -89.780 22.776 1.00 78.98 N ANISOU 544 N PHE A 69 8932 15992 5083 886 2162 -339 N ATOM 545 CA PHE A 69 3.485 -90.643 22.208 1.00 82.76 C ANISOU 545 CA PHE A 69 9010 16989 5446 1192 2137 -474 C ATOM 546 C PHE A 69 2.664 -91.315 23.304 1.00 84.27 C ANISOU 546 C PHE A 69 9018 17349 5650 1076 2308 -646 C ATOM 547 O PHE A 69 3.219 -91.987 24.173 1.00 83.37 O ANISOU 547 O PHE A 69 9150 16912 5616 1147 2435 -602 O ATOM 548 CB PHE A 69 4.123 -91.742 21.356 1.00 96.67 C ANISOU 548 CB PHE A 69 10856 18668 7204 1797 2089 -317 C ATOM 549 CG PHE A 69 4.557 -91.289 19.991 1.00 84.58 C ANISOU 549 CG PHE A 69 9387 17187 5562 2010 1922 -172 C ATOM 550 CD1 PHE A 69 5.772 -90.655 19.811 1.00 88.02 C ANISOU 550 CD1 PHE A 69 10208 17176 6058 1938 1935 35 C ATOM 551 CD2 PHE A 69 3.762 -91.524 18.885 1.00 88.12 C ANISOU 551 CD2 PHE A 69 9504 18141 5837 2300 1754 -249 C ATOM 552 CE1 PHE A 69 6.176 -90.245 18.554 1.00 92.19 C ANISOU 552 CE1 PHE A 69 10816 17771 6440 2139 1819 170 C ATOM 553 CE2 PHE A 69 4.164 -91.117 17.625 1.00108.69 C ANISOU 553 CE2 PHE A 69 12205 20812 8280 2512 1592 -114 C ATOM 554 CZ PHE A 69 5.372 -90.478 17.461 1.00 86.16 C ANISOU 554 CZ PHE A 69 9765 17519 5454 2429 1643 100 C ATOM 555 N THR A 70 1.346 -91.136 23.261 1.00 86.93 N ANISOU 555 N THR A 70 8927 18174 5928 889 2309 -852 N ATOM 556 CA THR A 70 0.447 -91.919 24.107 1.00 95.92 C ANISOU 556 CA THR A 70 9832 19508 7105 847 2476 -1018 C ATOM 557 C THR A 70 0.183 -93.295 23.493 1.00 92.95 C ANISOU 557 C THR A 70 9177 19469 6669 1450 2500 -1093 C ATOM 558 O THR A 70 0.027 -94.287 24.204 1.00124.35 O ANISOU 558 O THR A 70 13144 23403 10702 1606 2659 -1172 O ATOM 559 CB THR A 70 -0.883 -91.190 24.386 1.00 91.49 C ANISOU 559 CB THR A 70 8903 19310 6549 371 2505 -1202 C ATOM 560 OG1 THR A 70 -1.073 -90.143 23.425 1.00 91.28 O ANISOU 560 OG1 THR A 70 8725 19510 6448 221 2324 -1228 O ATOM 561 CG2 THR A 70 -0.876 -90.584 25.782 1.00133.35 C ANISOU 561 CG2 THR A 70 14497 24225 11943 -148 2629 -1161 C ATOM 562 N THR A 71 0.141 -93.341 22.165 1.00 94.48 N ANISOU 562 N THR A 71 9189 19902 6807 1791 2290 -1059 N ATOM 563 CA THR A 71 -0.030 -94.590 21.425 1.00112.48 C ANISOU 563 CA THR A 71 11250 22399 9090 2413 2221 -1080 C ATOM 564 C THR A 71 1.288 -95.364 21.374 1.00104.32 C ANISOU 564 C THR A 71 10679 20827 8131 2820 2228 -845 C ATOM 565 O THR A 71 2.329 -94.791 21.058 1.00 93.48 O ANISOU 565 O THR A 71 9692 19061 6764 2769 2150 -620 O ATOM 566 CB THR A 71 -0.501 -94.306 19.978 1.00100.58 C ANISOU 566 CB THR A 71 9431 21304 7480 2638 1934 -1098 C ATOM 567 OG1 THR A 71 -1.704 -93.524 20.004 1.00132.53 O ANISOU 567 OG1 THR A 71 13038 25821 11498 2219 1907 -1336 O ATOM 568 CG2 THR A 71 -0.759 -95.601 19.224 1.00116.39 C ANISOU 568 CG2 THR A 71 11183 23548 9490 3304 1829 -1118 C ATOM 569 N ARG A 72 1.256 -96.656 21.688 1.00 98.80 N ANISOU 569 N ARG A 72 9935 20094 7509 3214 2335 -906 N ATOM 570 CA ARG A 72 2.475 -97.457 21.630 1.00 97.92 C ANISOU 570 CA ARG A 72 10251 19444 7510 3601 2337 -697 C ATOM 571 C ARG A 72 2.919 -97.613 20.182 1.00 99.29 C ANISOU 571 C ARG A 72 10474 19612 7641 4050 2105 -472 C ATOM 572 O ARG A 72 2.090 -97.725 19.279 1.00132.83 O ANISOU 572 O ARG A 72 14335 24349 11786 4287 1941 -551 O ATOM 573 CB ARG A 72 2.286 -98.825 22.288 1.00100.66 C ANISOU 573 CB ARG A 72 10536 19750 7960 3940 2497 -852 C ATOM 574 CG ARG A 72 3.512 -99.294 23.073 1.00141.98 C ANISOU 574 CG ARG A 72 16290 24318 13338 3974 2602 -736 C ATOM 575 CD ARG A 72 3.564-100.809 23.222 1.00147.12 C ANISOU 575 CD ARG A 72 16934 24850 14116 4512 2674 -836 C ATOM 576 NE ARG A 72 2.467-101.336 24.028 1.00176.10 N ANISOU 576 NE ARG A 72 20258 28919 17732 4481 2868 -1174 N ATOM 577 CZ ARG A 72 2.543-101.561 25.335 1.00193.59 C ANISOU 577 CZ ARG A 72 22654 30961 19939 4252 3079 -1340 C ATOM 578 NH1 ARG A 72 3.670-101.302 25.987 1.00211.90 N ANISOU 578 NH1 ARG A 72 25480 32704 22326 4039 3081 -1209 N ATOM 579 NH2 ARG A 72 1.494-102.043 25.992 1.00137.34 N ANISOU 579 NH2 ARG A 72 15198 24251 12733 4240 3290 -1643 N ATOM 580 N ILE A 73 4.230 -97.607 19.960 1.00 97.07 N ANISOU 580 N ILE A 73 10666 18784 7433 4155 2090 -189 N ATOM 581 CA ILE A 73 4.765 -97.671 18.604 1.00101.82 C ANISOU 581 CA ILE A 73 11397 19336 7955 4543 1905 79 C ATOM 582 C ILE A 73 6.114 -98.389 18.564 1.00 97.89 C ANISOU 582 C ILE A 73 11371 18193 7631 4836 1970 361 C ATOM 583 O ILE A 73 6.928 -98.260 19.479 1.00114.40 O ANISOU 583 O ILE A 73 13773 19804 9890 4565 2120 397 O ATOM 584 CB ILE A 73 4.883 -96.255 17.985 1.00 96.24 C ANISOU 584 CB ILE A 73 10740 18751 7075 4199 1795 165 C ATOM 585 CG1 ILE A 73 5.321 -96.330 16.525 1.00 98.42 C ANISOU 585 CG1 ILE A 73 11142 19063 7189 4620 1608 428 C ATOM 586 CG2 ILE A 73 5.837 -95.386 18.788 1.00 91.49 C ANISOU 586 CG2 ILE A 73 10515 17659 6587 3723 1939 256 C ATOM 587 CD1 ILE A 73 5.401 -94.980 15.855 1.00 96.92 C ANISOU 587 CD1 ILE A 73 11002 19031 6794 4327 1502 474 C ATOM 588 N TYR A 74 6.339 -99.158 17.506 1.00101.27 N ANISOU 588 N TYR A 74 11849 18602 8029 5389 1842 563 N ATOM 589 CA TYR A 74 7.589 -99.888 17.346 1.00101.59 C ANISOU 589 CA TYR A 74 12329 18016 8252 5687 1904 861 C ATOM 590 C TYR A 74 8.537 -99.062 16.499 1.00100.05 C ANISOU 590 C TYR A 74 12458 17603 7953 5596 1874 1198 C ATOM 591 O TYR A 74 8.264 -98.800 15.328 1.00112.59 O ANISOU 591 O TYR A 74 13969 19519 9289 5816 1706 1328 O ATOM 592 CB TYR A 74 7.327-101.236 16.678 1.00106.83 C ANISOU 592 CB TYR A 74 12902 18732 8957 6363 1793 924 C ATOM 593 CG TYR A 74 8.486-102.205 16.746 1.00115.91 C ANISOU 593 CG TYR A 74 14478 19192 10372 6671 1883 1170 C ATOM 594 CD1 TYR A 74 8.702-102.977 17.882 1.00114.03 C ANISOU 594 CD1 TYR A 74 14324 18595 10406 6652 2036 983 C ATOM 595 CD2 TYR A 74 9.347-102.367 15.669 1.00128.30 C ANISOU 595 CD2 TYR A 74 16374 20463 11911 6979 1817 1584 C ATOM 596 CE1 TYR A 74 9.752-103.873 17.946 1.00117.12 C ANISOU 596 CE1 TYR A 74 15098 18326 11076 6918 2101 1180 C ATOM 597 CE2 TYR A 74 10.401-103.259 15.724 1.00115.98 C ANISOU 597 CE2 TYR A 74 15200 18237 10631 7234 1910 1821 C ATOM 598 CZ TYR A 74 10.599-104.008 16.865 1.00110.35 C ANISOU 598 CZ TYR A 74 14546 17154 10229 7197 2042 1605 C ATOM 599 OH TYR A 74 11.643-104.899 16.928 1.00127.08 O ANISOU 599 OH TYR A 74 17043 18581 12661 7433 2119 1812 O ATOM 600 N HIS A 75 9.662 -98.677 17.085 1.00 96.68 N ANISOU 600 N HIS A 75 12390 16627 7717 5287 2037 1330 N ATOM 601 CA HIS A 75 10.556 -97.714 16.461 1.00 94.85 C ANISOU 601 CA HIS A 75 12429 16202 7407 5097 2070 1599 C ATOM 602 C HIS A 75 11.790 -97.548 17.330 1.00 91.69 C ANISOU 602 C HIS A 75 12367 15147 7325 4791 2261 1695 C ATOM 603 O HIS A 75 11.681 -97.484 18.553 1.00131.46 O ANISOU 603 O HIS A 75 17358 20063 12530 4479 2325 1458 O ATOM 604 CB HIS A 75 9.844 -96.366 16.340 1.00 92.86 C ANISOU 604 CB HIS A 75 11945 16428 6908 4701 1992 1419 C ATOM 605 CG HIS A 75 10.567 -95.372 15.489 1.00 96.29 C ANISOU 605 CG HIS A 75 12604 16792 7189 4585 2005 1652 C ATOM 606 ND1 HIS A 75 11.709 -94.723 15.906 1.00100.76 N ANISOU 606 ND1 HIS A 75 13467 16871 7945 4260 2180 1786 N ATOM 607 CD2 HIS A 75 10.302 -94.905 14.246 1.00117.36 C ANISOU 607 CD2 HIS A 75 15236 19835 9522 4758 1866 1754 C ATOM 608 CE1 HIS A 75 12.121 -93.907 14.955 1.00121.72 C ANISOU 608 CE1 HIS A 75 16255 19602 10392 4241 2185 1962 C ATOM 609 NE2 HIS A 75 11.285 -93.997 13.937 1.00 95.25 N ANISOU 609 NE2 HIS A 75 12726 16770 6696 4539 1992 1946 N ATOM 610 N PRO A 76 12.970 -97.471 16.700 1.00 92.00 N ANISOU 610 N PRO A 76 12743 14769 7445 4872 2351 2044 N ATOM 611 CA PRO A 76 14.250 -97.394 17.415 1.00 90.42 C ANISOU 611 CA PRO A 76 12843 13910 7603 4616 2526 2157 C ATOM 612 C PRO A 76 14.437 -96.104 18.211 1.00 90.51 C ANISOU 612 C PRO A 76 12826 13893 7673 4039 2578 1995 C ATOM 613 O PRO A 76 15.196 -96.086 19.181 1.00120.82 O ANISOU 613 O PRO A 76 16811 17267 11830 3781 2664 1952 O ATOM 614 CB PRO A 76 15.283 -97.471 16.286 1.00103.48 C ANISOU 614 CB PRO A 76 14799 15266 9254 4845 2622 2590 C ATOM 615 CG PRO A 76 14.553 -97.010 15.073 1.00 93.83 C ANISOU 615 CG PRO A 76 13447 14623 7582 5045 2492 2662 C ATOM 616 CD PRO A 76 13.161 -97.525 15.242 1.00 95.19 C ANISOU 616 CD PRO A 76 13263 15306 7601 5239 2295 2364 C ATOM 617 N ASN A 77 13.780 -95.034 17.789 1.00 93.53 N ANISOU 617 N ASN A 77 13028 14746 7764 3850 2504 1902 N ATOM 618 CA ASN A 77 13.909 -93.744 18.460 1.00 81.49 C ANISOU 618 CA ASN A 77 11477 13193 6291 3328 2534 1754 C ATOM 619 C ASN A 77 12.788 -93.392 19.438 1.00 78.88 C ANISOU 619 C ASN A 77 10880 13196 5895 3028 2442 1398 C ATOM 620 O ASN A 77 12.774 -92.301 20.003 1.00109.51 O ANISOU 620 O ASN A 77 14736 17069 9803 2601 2441 1276 O ATOM 621 CB ASN A 77 14.104 -92.636 17.433 1.00 93.21 C ANISOU 621 CB ASN A 77 12993 14873 7548 3250 2546 1882 C ATOM 622 CG ASN A 77 15.328 -92.862 16.579 1.00110.15 C ANISOU 622 CG ASN A 77 15439 16649 9764 3472 2700 2256 C ATOM 623 OD1 ASN A 77 15.224 -93.104 15.376 1.00 85.26 O ANISOU 623 OD1 ASN A 77 12339 13724 6333 3818 2673 2455 O ATOM 624 ND2 ASN A 77 16.501 -92.800 17.199 1.00138.73 N ANISOU 624 ND2 ASN A 77 19258 19696 13758 3271 2861 2362 N ATOM 625 N ILE A 78 11.838 -94.303 19.623 1.00 82.79 N ANISOU 625 N ILE A 78 11172 13982 6305 3256 2376 1240 N ATOM 626 CA ILE A 78 10.748 -94.077 20.568 1.00 79.95 C ANISOU 626 CA ILE A 78 10556 13945 5877 2976 2337 920 C ATOM 627 C ILE A 78 10.553 -95.290 21.473 1.00 81.17 C ANISOU 627 C ILE A 78 10703 13968 6169 3137 2388 782 C ATOM 628 O ILE A 78 10.211 -96.372 20.996 1.00140.82 O ANISOU 628 O ILE A 78 18161 21654 13688 3580 2366 792 O ATOM 629 CB ILE A 78 9.417 -93.804 19.834 1.00 90.07 C ANISOU 629 CB ILE A 78 11469 15903 6851 3047 2213 774 C ATOM 630 CG1 ILE A 78 9.627 -92.883 18.630 1.00 82.07 C ANISOU 630 CG1 ILE A 78 10488 15047 5648 3053 2135 921 C ATOM 631 CG2 ILE A 78 8.397 -93.214 20.786 1.00108.58 C ANISOU 631 CG2 ILE A 78 13569 18542 9143 2622 2212 480 C ATOM 632 CD1 ILE A 78 8.405 -92.752 17.751 1.00 84.83 C ANISOU 632 CD1 ILE A 78 10486 16045 5700 3198 1964 784 C ATOM 633 N ASN A 79 10.769 -95.116 22.776 1.00 85.95 N ANISOU 633 N ASN A 79 11419 14317 6922 2799 2445 642 N ATOM 634 CA ASN A 79 10.574 -96.210 23.731 1.00 84.90 C ANISOU 634 CA ASN A 79 11306 14072 6881 2924 2501 467 C ATOM 635 C ASN A 79 9.099 -96.473 24.005 1.00107.54 C ANISOU 635 C ASN A 79 13814 17521 9525 2933 2515 200 C ATOM 636 O ASN A 79 8.265 -95.595 23.798 1.00137.67 O ANISOU 636 O ASN A 79 17390 21763 13157 2683 2478 122 O ATOM 637 CB ASN A 79 11.318 -95.941 25.044 1.00 91.25 C ANISOU 637 CB ASN A 79 12374 14417 7881 2569 2531 401 C ATOM 638 CG ASN A 79 10.939 -94.612 25.677 1.00102.97 C ANISOU 638 CG ASN A 79 13808 16054 9260 2046 2502 309 C ATOM 639 OD1 ASN A 79 10.007 -93.942 25.235 1.00126.24 O ANISOU 639 OD1 ASN A 79 16504 19467 11996 1921 2478 254 O ATOM 640 ND2 ASN A 79 11.665 -94.227 26.723 1.00133.43 N ANISOU 640 ND2 ASN A 79 17908 19502 13286 1742 2482 288 N ATOM 641 N SER A 80 8.780 -97.676 24.475 1.00150.75 N ANISOU 641 N SER A 80 19239 23005 15034 3213 2580 43 N ATOM 642 CA SER A 80 7.398 -98.015 24.812 1.00156.36 C ANISOU 642 CA SER A 80 19585 24267 15559 3229 2643 -230 C ATOM 643 C SER A 80 6.907 -97.183 26.003 1.00139.78 C ANISOU 643 C SER A 80 17472 22288 13350 2677 2721 -399 C ATOM 644 O SER A 80 5.719 -97.188 26.334 1.00153.33 O ANISOU 644 O SER A 80 18877 24484 14899 2560 2807 -607 O ATOM 645 CB SER A 80 7.250 -99.511 25.084 1.00139.45 C ANISOU 645 CB SER A 80 17416 22073 13497 3678 2720 -377 C ATOM 646 OG SER A 80 8.267 -99.970 25.957 1.00203.83 O ANISOU 646 OG SER A 80 25959 29645 21844 3652 2762 -379 O ATOM 647 N ASN A 81 7.835 -96.472 26.634 1.00 81.87 N ANISOU 647 N ASN A 81 10475 14507 6125 2341 2691 -298 N ATOM 648 CA ASN A 81 7.508 -95.462 27.623 1.00105.38 C ANISOU 648 CA ASN A 81 13496 17539 9004 1803 2714 -383 C ATOM 649 C ASN A 81 6.858 -94.247 26.951 1.00 85.93 C ANISOU 649 C ASN A 81 10796 15434 6420 1529 2652 -338 C ATOM 650 O ASN A 81 6.072 -93.527 27.570 1.00111.59 O ANISOU 650 O ASN A 81 13933 18925 9540 1129 2694 -448 O ATOM 651 CB ASN A 81 8.773 -95.047 28.382 1.00183.19 C ANISOU 651 CB ASN A 81 23766 26788 19050 1577 2649 -278 C ATOM 652 CG ASN A 81 8.474 -94.235 29.629 1.00181.58 C ANISOU 652 CG ASN A 81 23671 26580 18740 1080 2656 -374 C ATOM 653 OD1 ASN A 81 7.399 -94.358 30.223 1.00129.33 O ANISOU 653 OD1 ASN A 81 16893 20342 11905 945 2768 -545 O ATOM 654 ND2 ASN A 81 9.430 -93.404 30.039 1.00144.79 N ANISOU 654 ND2 ASN A 81 19285 21489 14242 811 2542 -255 N ATOM 655 N GLY A 82 7.186 -94.029 25.679 1.00 94.82 N ANISOU 655 N GLY A 82 11864 16585 7580 1745 2553 -177 N ATOM 656 CA GLY A 82 6.557 -92.981 24.894 1.00 83.37 C ANISOU 656 CA GLY A 82 10180 15498 6001 1554 2470 -171 C ATOM 657 C GLY A 82 7.425 -91.777 24.558 1.00 96.21 C ANISOU 657 C GLY A 82 12026 16821 7709 1314 2384 -3 C ATOM 658 O GLY A 82 7.011 -90.900 23.795 1.00 83.48 O ANISOU 658 O GLY A 82 10254 15474 5991 1192 2302 -7 O ATOM 659 N SER A 83 8.625 -91.734 25.128 1.00119.64 N ANISOU 659 N SER A 83 15343 19236 10879 1249 2399 119 N ATOM 660 CA SER A 83 9.538 -90.607 24.958 1.00 80.35 C ANISOU 660 CA SER A 83 10569 13929 6032 1015 2343 260 C ATOM 661 C SER A 83 10.177 -90.572 23.569 1.00 89.63 C ANISOU 661 C SER A 83 11776 15068 7210 1318 2323 456 C ATOM 662 O SER A 83 10.678 -91.587 23.084 1.00 83.53 O ANISOU 662 O SER A 83 11083 14158 6495 1715 2360 584 O ATOM 663 CB SER A 83 10.627 -90.660 26.032 1.00 96.46 C ANISOU 663 CB SER A 83 12933 15397 8322 870 2354 312 C ATOM 664 OG SER A 83 10.067 -90.926 27.306 1.00127.32 O ANISOU 664 OG SER A 83 16860 19346 12171 670 2375 143 O ATOM 665 N ILE A 84 10.167 -89.398 22.937 1.00106.75 N ANISOU 665 N ILE A 84 13905 17348 9309 1133 2270 481 N ATOM 666 CA ILE A 84 10.745 -89.226 21.603 1.00 80.79 C ANISOU 666 CA ILE A 84 10673 14066 5958 1392 2266 663 C ATOM 667 C ILE A 84 12.198 -88.765 21.698 1.00 70.93 C ANISOU 667 C ILE A 84 9719 12267 4964 1306 2344 847 C ATOM 668 O ILE A 84 12.515 -87.842 22.447 1.00 94.77 O ANISOU 668 O ILE A 84 12817 15054 8139 939 2332 786 O ATOM 669 CB ILE A 84 9.940 -88.216 20.772 1.00 71.63 C ANISOU 669 CB ILE A 84 9307 13353 4555 1267 2167 556 C ATOM 670 CG1 ILE A 84 8.459 -88.600 20.763 1.00103.55 C ANISOU 670 CG1 ILE A 84 12998 17944 8400 1290 2087 344 C ATOM 671 CG2 ILE A 84 10.489 -88.131 19.358 1.00 81.27 C ANISOU 671 CG2 ILE A 84 10612 14633 5634 1579 2164 739 C ATOM 672 CD1 ILE A 84 7.541 -87.498 20.277 1.00100.11 C ANISOU 672 CD1 ILE A 84 12332 17914 7790 1035 1969 165 C ATOM 673 N SER A 85 13.078 -89.413 20.940 1.00 88.10 N ANISOU 673 N SER A 85 12047 14227 7199 1647 2426 1080 N ATOM 674 CA SER A 85 14.520 -89.247 21.132 1.00 70.48 C ANISOU 674 CA SER A 85 10070 11430 5278 1587 2538 1261 C ATOM 675 C SER A 85 15.261 -88.269 20.217 1.00 95.29 C ANISOU 675 C SER A 85 13302 14500 8405 1547 2625 1409 C ATOM 676 O SER A 85 16.488 -88.174 20.289 1.00135.37 O ANISOU 676 O SER A 85 18554 19119 13761 1513 2753 1572 O ATOM 677 CB SER A 85 15.222 -90.601 21.113 1.00141.02 C ANISOU 677 CB SER A 85 19160 20030 14392 1919 2618 1435 C ATOM 678 OG SER A 85 16.505 -90.475 21.699 1.00 69.35 O ANISOU 678 OG SER A 85 10281 10375 5695 1760 2702 1534 O ATOM 679 N LEU A 86 14.543 -87.565 19.350 1.00 86.32 N ANISOU 679 N LEU A 86 12036 13813 6950 1555 2565 1339 N ATOM 680 CA LEU A 86 15.176 -86.530 18.534 1.00136.74 C ANISOU 680 CA LEU A 86 18509 20165 13281 1497 2655 1425 C ATOM 681 C LEU A 86 15.547 -85.335 19.414 1.00108.11 C ANISOU 681 C LEU A 86 14894 16269 9913 1065 2654 1282 C ATOM 682 O LEU A 86 14.806 -84.982 20.333 1.00114.26 O ANISOU 682 O LEU A 86 15559 17126 10729 790 2520 1068 O ATOM 683 CB LEU A 86 14.275 -86.108 17.370 1.00 99.46 C ANISOU 683 CB LEU A 86 13659 16008 8125 1633 2556 1348 C ATOM 684 CG LEU A 86 12.958 -85.389 17.669 1.00 88.53 C ANISOU 684 CG LEU A 86 12023 15035 6581 1368 2365 1029 C ATOM 685 CD1 LEU A 86 13.125 -83.881 17.586 1.00143.21 C ANISOU 685 CD1 LEU A 86 18966 21926 13521 1053 2367 892 C ATOM 686 CD2 LEU A 86 11.880 -85.855 16.712 1.00127.91 C ANISOU 686 CD2 LEU A 86 16817 20552 11230 1634 2199 959 C ATOM 687 N ASP A 87 16.689 -84.712 19.133 1.00 84.22 N ANISOU 687 N ASP A 87 12002 12925 7071 1013 2811 1407 N ATOM 688 CA ASP A 87 17.272 -83.744 20.068 1.00145.12 C ANISOU 688 CA ASP A 87 19733 20275 15132 654 2809 1301 C ATOM 689 C ASP A 87 16.939 -82.258 19.869 1.00 90.30 C ANISOU 689 C ASP A 87 12715 13493 8103 410 2759 1107 C ATOM 690 O ASP A 87 17.493 -81.407 20.565 1.00115.64 O ANISOU 690 O ASP A 87 15942 16377 11621 150 2755 1031 O ATOM 691 CB ASP A 87 18.784 -83.954 20.223 1.00144.27 C ANISOU 691 CB ASP A 87 19767 19630 15417 682 2999 1505 C ATOM 692 CG ASP A 87 19.465 -84.271 18.914 1.00159.86 C ANISOU 692 CG ASP A 87 21852 21631 17257 982 3232 1766 C ATOM 693 OD1 ASP A 87 18.862 -84.006 17.851 1.00162.21 O ANISOU 693 OD1 ASP A 87 22132 22362 17139 1140 3234 1762 O ATOM 694 OD2 ASP A 87 20.606 -84.779 18.949 1.00173.34 O ANISOU 694 OD2 ASP A 87 23671 22922 19270 1052 3410 1978 O ATOM 695 N ILE A 88 16.053 -81.934 18.932 1.00 85.66 N ANISOU 695 N ILE A 88 12041 13387 7120 501 2699 1010 N ATOM 696 CA ILE A 88 15.521 -80.571 18.880 1.00107.62 C ANISOU 696 CA ILE A 88 14737 16325 9828 239 2602 763 C ATOM 697 C ILE A 88 14.542 -80.393 20.042 1.00 82.14 C ANISOU 697 C ILE A 88 11391 13132 6686 -71 2398 565 C ATOM 698 O ILE A 88 14.123 -79.280 20.363 1.00 66.67 O ANISOU 698 O ILE A 88 9379 11175 4776 -361 2297 367 O ATOM 699 CB ILE A 88 14.826 -80.243 17.537 1.00 81.89 C ANISOU 699 CB ILE A 88 11419 13579 6117 409 2565 677 C ATOM 700 CG1 ILE A 88 13.303 -80.353 17.662 1.00 93.53 C ANISOU 700 CG1 ILE A 88 12684 15492 7363 314 2329 461 C ATOM 701 CG2 ILE A 88 15.363 -81.137 16.422 1.00 97.94 C ANISOU 701 CG2 ILE A 88 13572 15721 7919 828 2716 946 C ATOM 702 CD1 ILE A 88 12.555 -79.947 16.420 1.00103.95 C ANISOU 702 CD1 ILE A 88 13913 17309 8273 443 2226 319 C ATOM 703 N LEU A 89 14.188 -81.512 20.667 1.00 75.14 N ANISOU 703 N LEU A 89 10478 12260 5812 -2 2354 624 N ATOM 704 CA LEU A 89 13.359 -81.504 21.861 1.00 67.19 C ANISOU 704 CA LEU A 89 9395 11261 4873 -283 2211 479 C ATOM 705 C LEU A 89 14.184 -81.437 23.145 1.00101.41 C ANISOU 705 C LEU A 89 13874 15073 9584 -475 2203 530 C ATOM 706 O LEU A 89 13.619 -81.268 24.229 1.00 76.23 O ANISOU 706 O LEU A 89 10678 11834 6451 -739 2085 428 O ATOM 707 CB LEU A 89 12.466 -82.748 21.903 1.00 67.88 C ANISOU 707 CB LEU A 89 9362 11677 4752 -102 2178 478 C ATOM 708 CG LEU A 89 11.213 -82.751 21.030 1.00 67.58 C ANISOU 708 CG LEU A 89 9094 12222 4363 -20 2093 341 C ATOM 709 CD1 LEU A 89 10.477 -84.076 21.166 1.00 81.99 C ANISOU 709 CD1 LEU A 89 10780 14317 6055 195 2081 346 C ATOM 710 CD2 LEU A 89 10.303 -81.595 21.402 1.00 95.90 C ANISOU 710 CD2 LEU A 89 12555 15954 7928 -422 1973 110 C ATOM 711 N ARG A 90 15.506 -81.589 23.043 1.00 82.23 N ANISOU 711 N ARG A 90 11575 12258 7410 -348 2324 690 N ATOM 712 CA ARG A 90 16.324 -81.517 24.251 1.00 95.20 C ANISOU 712 CA ARG A 90 13329 13406 9435 -524 2274 715 C ATOM 713 C ARG A 90 17.436 -80.464 24.233 1.00111.50 C ANISOU 713 C ARG A 90 15439 15095 11830 -637 2326 731 C ATOM 714 O ARG A 90 17.237 -79.339 24.691 1.00108.93 O ANISOU 714 O ARG A 90 15096 14688 11606 -895 2211 594 O ATOM 715 CB ARG A 90 16.957 -82.888 24.507 1.00 77.44 C ANISOU 715 CB ARG A 90 11170 10944 7311 -300 2342 865 C ATOM 716 CG ARG A 90 16.032 -84.062 24.230 1.00117.45 C ANISOU 716 CG ARG A 90 16177 16381 12066 -74 2345 868 C ATOM 717 CD ARG A 90 16.782 -85.257 23.648 1.00105.78 C ANISOU 717 CD ARG A 90 14781 14758 10652 281 2486 1067 C ATOM 718 NE ARG A 90 17.356 -86.125 24.675 1.00 94.07 N ANISOU 718 NE ARG A 90 13414 12889 9439 283 2452 1085 N ATOM 719 CZ ARG A 90 18.600 -86.019 25.130 1.00135.99 C ANISOU 719 CZ ARG A 90 18831 17694 15144 202 2477 1159 C ATOM 720 NH1 ARG A 90 19.408 -85.081 24.653 1.00153.30 N ANISOU 720 NH1 ARG A 90 21015 19713 17520 117 2570 1233 N ATOM 721 NH2 ARG A 90 19.036 -86.855 26.063 1.00108.47 N ANISOU 721 NH2 ARG A 90 15449 13885 11881 207 2410 1137 N ATOM 722 N SER A 91 18.592 -80.817 23.676 1.00 90.25 N ANISOU 722 N SER A 91 12795 12174 9320 -441 2512 899 N ATOM 723 CA SER A 91 19.754 -79.928 23.746 1.00 84.66 C ANISOU 723 CA SER A 91 12093 11082 8991 -541 2593 913 C ATOM 724 C SER A 91 19.856 -78.901 22.627 1.00 78.14 C ANISOU 724 C SER A 91 11218 10437 8035 -502 2745 869 C ATOM 725 O SER A 91 20.464 -77.842 22.792 1.00 87.93 O ANISOU 725 O SER A 91 12423 11439 9548 -641 2767 785 O ATOM 726 CB SER A 91 21.050 -80.746 23.838 1.00 94.98 C ANISOU 726 CB SER A 91 13456 11991 10641 -409 2738 1103 C ATOM 727 OG SER A 91 21.075 -81.783 22.874 1.00100.90 O ANISOU 727 OG SER A 91 14256 12919 11163 -110 2918 1289 O ATOM 728 N GLN A 92 19.245 -79.217 21.493 1.00 87.54 N ANISOU 728 N GLN A 92 12405 12057 8798 -294 2834 907 N ATOM 729 CA GLN A 92 19.389 -78.407 20.287 1.00 84.69 C ANISOU 729 CA GLN A 92 12037 11907 8235 -198 2998 876 C ATOM 730 C GLN A 92 18.250 -77.411 20.088 1.00 98.89 C ANISOU 730 C GLN A 92 13760 14045 9770 -352 2829 611 C ATOM 731 O GLN A 92 18.145 -76.774 19.038 1.00109.27 O ANISOU 731 O GLN A 92 15075 15614 10830 -261 2921 533 O ATOM 732 CB GLN A 92 19.628 -79.285 19.051 1.00 95.37 C ANISOU 732 CB GLN A 92 13469 13483 9285 149 3207 1104 C ATOM 733 CG GLN A 92 20.988 -79.993 19.088 1.00 88.11 C ANISOU 733 CG GLN A 92 12633 12146 8697 268 3441 1373 C ATOM 734 CD GLN A 92 21.362 -80.660 17.775 1.00129.20 C ANISOU 734 CD GLN A 92 17959 17519 13613 599 3691 1637 C ATOM 735 OE1 GLN A 92 21.214 -80.078 16.698 1.00129.44 O ANISOU 735 OE1 GLN A 92 18025 17860 13295 712 3803 1620 O ATOM 736 NE2 GLN A 92 21.864 -81.888 17.859 1.00144.36 N ANISOU 736 NE2 GLN A 92 19963 19218 15668 762 3773 1884 N ATOM 737 N TRP A 93 17.394 -77.286 21.093 1.00 60.89 N ANISOU 737 N TRP A 93 8895 9233 5009 -591 2587 470 N ATOM 738 CA TRP A 93 16.226 -76.431 20.965 1.00 61.25 C ANISOU 738 CA TRP A 93 8860 9578 4835 -772 2421 226 C ATOM 739 C TRP A 93 16.583 -74.948 21.010 1.00 75.81 C ANISOU 739 C TRP A 93 10705 11205 6893 -957 2413 46 C ATOM 740 O TRP A 93 17.124 -74.454 21.997 1.00 93.71 O ANISOU 740 O TRP A 93 12999 13053 9555 -1139 2348 32 O ATOM 741 CB TRP A 93 15.240 -76.751 22.084 1.00105.55 C ANISOU 741 CB TRP A 93 14426 15221 10457 -998 2205 162 C ATOM 742 CG TRP A 93 14.161 -75.738 22.244 1.00 80.85 C ANISOU 742 CG TRP A 93 11221 12258 7239 -1279 2034 -77 C ATOM 743 CD1 TRP A 93 14.153 -74.672 23.096 1.00 96.07 C ANISOU 743 CD1 TRP A 93 13189 13875 9440 -1580 1908 -194 C ATOM 744 CD2 TRP A 93 12.921 -75.694 21.535 1.00 80.84 C ANISOU 744 CD2 TRP A 93 11087 12750 6877 -1291 1954 -230 C ATOM 745 NE1 TRP A 93 12.986 -73.965 22.959 1.00 95.78 N ANISOU 745 NE1 TRP A 93 13069 14083 9241 -1795 1774 -400 N ATOM 746 CE2 TRP A 93 12.210 -74.575 22.007 1.00 77.28 C ANISOU 746 CE2 TRP A 93 10601 12244 6516 -1634 1799 -440 C ATOM 747 CE3 TRP A 93 12.341 -76.494 20.548 1.00 89.03 C ANISOU 747 CE3 TRP A 93 12022 14261 7543 -1039 1979 -213 C ATOM 748 CZ2 TRP A 93 10.949 -74.234 21.524 1.00 97.14 C ANISOU 748 CZ2 TRP A 93 12968 15158 8783 -1763 1682 -646 C ATOM 749 CZ3 TRP A 93 11.093 -76.156 20.069 1.00 93.50 C ANISOU 749 CZ3 TRP A 93 12424 15249 7853 -1145 1841 -427 C ATOM 750 CH2 TRP A 93 10.409 -75.035 20.556 1.00 95.16 C ANISOU 750 CH2 TRP A 93 12586 15391 8179 -1519 1701 -647 C ATOM 751 N SER A 94 16.277 -74.251 19.920 1.00 75.68 N ANISOU 751 N SER A 94 10665 11480 6609 -887 2463 -105 N ATOM 752 CA SER A 94 16.313 -72.792 19.879 1.00 66.49 C ANISOU 752 CA SER A 94 9492 10185 5587 -1061 2425 -350 C ATOM 753 C SER A 94 14.934 -72.212 20.193 1.00106.40 C ANISOU 753 C SER A 94 14477 15429 10522 -1329 2164 -588 C ATOM 754 O SER A 94 13.914 -72.832 19.894 1.00 94.92 O ANISOU 754 O SER A 94 12948 14372 8745 -1310 2070 -607 O ATOM 755 CB SER A 94 16.794 -72.304 18.509 1.00117.89 C ANISOU 755 CB SER A 94 16037 16893 11862 -836 2640 -415 C ATOM 756 OG SER A 94 16.468 -70.935 18.314 1.00119.59 O ANISOU 756 OG SER A 94 16234 17102 12103 -990 2562 -727 O ATOM 757 N PRO A 95 14.897 -71.014 20.794 1.00 88.15 N ANISOU 757 N PRO A 95 12176 12818 8496 -1582 2048 -772 N ATOM 758 CA PRO A 95 13.640 -70.302 21.052 1.00 77.85 C ANISOU 758 CA PRO A 95 10821 11630 7127 -1872 1820 -1004 C ATOM 759 C PRO A 95 12.949 -69.857 19.764 1.00 92.16 C ANISOU 759 C PRO A 95 12569 13882 8567 -1798 1811 -1248 C ATOM 760 O PRO A 95 11.779 -69.474 19.790 1.00 89.04 O ANISOU 760 O PRO A 95 12093 13676 8063 -2022 1624 -1445 O ATOM 761 CB PRO A 95 14.093 -69.078 21.852 1.00 82.10 C ANISOU 761 CB PRO A 95 11425 11663 8104 -2081 1734 -1116 C ATOM 762 CG PRO A 95 15.383 -69.484 22.463 1.00 83.65 C ANISOU 762 CG PRO A 95 11676 11482 8626 -1959 1846 -891 C ATOM 763 CD PRO A 95 16.041 -70.350 21.437 1.00105.67 C ANISOU 763 CD PRO A 95 14448 14520 11180 -1626 2104 -747 C ATOM 764 N ALA A 96 13.676 -69.890 18.655 1.00 88.57 N ANISOU 764 N ALA A 96 12155 13580 7917 -1497 2010 -1239 N ATOM 765 CA ALA A 96 13.139 -69.446 17.377 1.00 75.01 C ANISOU 765 CA ALA A 96 10413 12284 5804 -1388 1993 -1481 C ATOM 766 C ALA A 96 12.389 -70.564 16.652 1.00101.06 C ANISOU 766 C ALA A 96 13632 16116 8651 -1202 1940 -1393 C ATOM 767 O ALA A 96 11.787 -70.339 15.604 1.00123.92 O ANISOU 767 O ALA A 96 16487 19424 11171 -1106 1862 -1594 O ATOM 768 CB ALA A 96 14.256 -68.909 16.502 1.00 97.58 C ANISOU 768 CB ALA A 96 13380 15081 8615 -1143 2247 -1517 C ATOM 769 N LEU A 97 12.436 -71.767 17.215 1.00 94.72 N ANISOU 769 N LEU A 97 12802 15300 7889 -1136 1965 -1110 N ATOM 770 CA LEU A 97 11.773 -72.920 16.615 1.00100.12 C ANISOU 770 CA LEU A 97 13393 16450 8198 -925 1914 -1007 C ATOM 771 C LEU A 97 10.275 -72.940 16.898 1.00104.64 C ANISOU 771 C LEU A 97 13760 17317 8680 -1170 1661 -1203 C ATOM 772 O LEU A 97 9.809 -72.398 17.900 1.00106.23 O ANISOU 772 O LEU A 97 13919 17283 9160 -1527 1555 -1303 O ATOM 773 CB LEU A 97 12.409 -74.223 17.102 1.00101.20 C ANISOU 773 CB LEU A 97 13580 16435 8437 -741 2048 -654 C ATOM 774 CG LEU A 97 13.898 -74.406 16.802 1.00 99.61 C ANISOU 774 CG LEU A 97 13553 15947 8349 -501 2322 -419 C ATOM 775 CD1 LEU A 97 14.365 -75.798 17.221 1.00 83.53 C ANISOU 775 CD1 LEU A 97 11552 13785 6400 -324 2415 -97 C ATOM 776 CD2 LEU A 97 14.180 -74.153 15.329 1.00104.32 C ANISOU 776 CD2 LEU A 97 14231 16849 8555 -220 2444 -450 C ATOM 777 N THR A 98 9.528 -73.587 16.011 1.00102.11 N ANISOU 777 N THR A 98 13309 17512 7977 -973 1565 -1245 N ATOM 778 CA THR A 98 8.081 -73.660 16.133 1.00118.56 C ANISOU 778 CA THR A 98 15137 19938 9971 -1187 1337 -1448 C ATOM 779 C THR A 98 7.662 -75.089 16.459 1.00108.16 C ANISOU 779 C THR A 98 13682 18828 8587 -1042 1341 -1242 C ATOM 780 O THR A 98 8.366 -76.038 16.120 1.00 97.81 O ANISOU 780 O THR A 98 12469 17529 7164 -684 1469 -985 O ATOM 781 CB THR A 98 7.384 -73.211 14.828 1.00112.24 C ANISOU 781 CB THR A 98 14229 19620 8798 -1087 1163 -1737 C ATOM 782 OG1 THR A 98 6.852 -74.350 14.144 1.00143.55 O ANISOU 782 OG1 THR A 98 18038 24069 12438 -786 1078 -1652 O ATOM 783 CG2 THR A 98 8.366 -72.498 13.915 1.00139.75 C ANISOU 783 CG2 THR A 98 17947 23027 12123 -872 1282 -1781 C ATOM 784 N ILE A 99 6.523 -75.236 17.127 1.00105.06 N ANISOU 784 N ILE A 99 13062 18578 8276 -1323 1218 -1356 N ATOM 785 CA ILE A 99 5.975 -76.555 17.434 1.00104.07 C ANISOU 785 CA ILE A 99 12761 18698 8083 -1193 1226 -1220 C ATOM 786 C ILE A 99 5.637 -77.317 16.145 1.00104.27 C ANISOU 786 C ILE A 99 12640 19246 7731 -782 1132 -1233 C ATOM 787 O ILE A 99 5.593 -78.548 16.129 1.00102.23 O ANISOU 787 O ILE A 99 12309 19144 7391 -499 1172 -1056 O ATOM 788 CB ILE A 99 4.740 -76.446 18.371 1.00 89.31 C ANISOU 788 CB ILE A 99 10653 16915 6365 -1614 1145 -1367 C ATOM 789 CG1 ILE A 99 4.825 -77.459 19.517 1.00118.64 C ANISOU 789 CG1 ILE A 99 14390 20466 10222 -1624 1283 -1145 C ATOM 790 CG2 ILE A 99 3.438 -76.591 17.594 1.00114.40 C ANISOU 790 CG2 ILE A 99 13468 20672 9325 -1619 961 -1612 C ATOM 791 CD1 ILE A 99 4.492 -78.878 19.118 1.00111.39 C ANISOU 791 CD1 ILE A 99 13286 19930 9106 -1257 1303 -1054 C ATOM 792 N SER A 100 5.417 -76.577 15.059 1.00105.15 N ANISOU 792 N SER A 100 12726 19617 7609 -728 990 -1449 N ATOM 793 CA SER A 100 5.174 -77.189 13.758 1.00101.36 C ANISOU 793 CA SER A 100 12157 19557 6799 -309 851 -1441 C ATOM 794 C SER A 100 6.441 -77.892 13.270 1.00105.50 C ANISOU 794 C SER A 100 12981 19807 7299 131 1019 -1079 C ATOM 795 O SER A 100 6.387 -79.032 12.798 1.00149.95 O ANISOU 795 O SER A 100 18560 25608 12804 493 986 -896 O ATOM 796 CB SER A 100 4.706 -76.139 12.742 1.00119.18 C ANISOU 796 CB SER A 100 14362 22077 8843 -368 641 -1768 C ATOM 797 OG SER A 100 4.303 -76.741 11.524 1.00132.80 O ANISOU 797 OG SER A 100 15971 24215 10272 16 447 -1775 O ATOM 798 N LYS A 101 7.578 -77.210 13.402 1.00116.14 N ANISOU 798 N LYS A 101 14626 20734 8767 83 1209 -985 N ATOM 799 CA LYS A 101 8.871 -77.788 13.045 1.00110.60 C ANISOU 799 CA LYS A 101 14211 19726 8085 418 1419 -643 C ATOM 800 C LYS A 101 9.108 -79.092 13.795 1.00 89.97 C ANISOU 800 C LYS A 101 11588 16951 5646 544 1523 -371 C ATOM 801 O LYS A 101 9.560 -80.075 13.210 1.00111.57 O ANISOU 801 O LYS A 101 14421 19678 8291 909 1572 -123 O ATOM 802 CB LYS A 101 10.014 -76.809 13.331 1.00108.14 C ANISOU 802 CB LYS A 101 14148 19003 7936 273 1642 -621 C ATOM 803 CG LYS A 101 10.144 -75.667 12.329 1.00161.65 C ANISOU 803 CG LYS A 101 21028 25887 14503 289 1612 -833 C ATOM 804 CD LYS A 101 11.571 -75.122 12.312 1.00166.29 C ANISOU 804 CD LYS A 101 21886 26088 15208 331 1916 -697 C ATOM 805 CE LYS A 101 11.705 -73.910 11.403 1.00182.92 C ANISOU 805 CE LYS A 101 24099 28293 17109 333 1919 -950 C ATOM 806 NZ LYS A 101 11.241 -74.192 10.018 1.00168.35 N ANISOU 806 NZ LYS A 101 22283 26803 14878 617 1749 -972 N ATOM 807 N VAL A 102 8.793 -79.090 15.086 1.00 81.17 N ANISOU 807 N VAL A 102 10369 15704 4767 233 1552 -426 N ATOM 808 CA VAL A 102 8.890 -80.286 15.915 1.00 86.47 C ANISOU 808 CA VAL A 102 11019 16241 5595 319 1635 -230 C ATOM 809 C VAL A 102 7.990 -81.384 15.364 1.00 91.43 C ANISOU 809 C VAL A 102 11419 17299 6021 606 1491 -229 C ATOM 810 O VAL A 102 8.403 -82.542 15.222 1.00 78.65 O ANISOU 810 O VAL A 102 9869 15618 4395 943 1560 3 O ATOM 811 CB VAL A 102 8.461 -79.997 17.367 1.00 72.82 C ANISOU 811 CB VAL A 102 9202 14373 4094 -106 1653 -340 C ATOM 812 CG1 VAL A 102 8.613 -81.242 18.225 1.00 91.78 C ANISOU 812 CG1 VAL A 102 11614 16626 6634 3 1747 -157 C ATOM 813 CG2 VAL A 102 9.265 -78.847 17.945 1.00 73.90 C ANISOU 813 CG2 VAL A 102 9537 14057 4484 -397 1737 -362 C ATOM 814 N LEU A 103 6.754 -81.003 15.051 1.00 82.73 N ANISOU 814 N LEU A 103 10026 16654 4754 472 1289 -504 N ATOM 815 CA LEU A 103 5.767 -81.951 14.552 1.00 83.10 C ANISOU 815 CA LEU A 103 9774 17202 4597 725 1132 -561 C ATOM 816 C LEU A 103 6.236 -82.666 13.290 1.00 93.32 C ANISOU 816 C LEU A 103 11189 18613 5655 1248 1077 -360 C ATOM 817 O LEU A 103 6.279 -83.895 13.257 1.00113.18 O ANISOU 817 O LEU A 103 13672 21195 8138 1585 1103 -180 O ATOM 818 CB LEU A 103 4.425 -81.262 14.318 1.00 96.70 C ANISOU 818 CB LEU A 103 11146 19422 6175 462 915 -925 C ATOM 819 CG LEU A 103 3.280 -81.802 15.174 1.00101.11 C ANISOU 819 CG LEU A 103 11338 20265 6816 256 904 -1070 C ATOM 820 CD1 LEU A 103 3.736 -81.985 16.616 1.00 82.33 C ANISOU 820 CD1 LEU A 103 9118 17412 4751 9 1136 -925 C ATOM 821 CD2 LEU A 103 2.081 -80.873 15.102 1.00131.15 C ANISOU 821 CD2 LEU A 103 14825 24375 10629 -143 719 -1428 C ATOM 822 N LEU A 104 6.598 -81.914 12.255 1.00108.51 N ANISOU 822 N LEU A 104 13270 20555 7403 1329 1008 -385 N ATOM 823 CA LEU A 104 7.072 -82.569 11.035 1.00 98.95 C ANISOU 823 CA LEU A 104 12217 19435 5945 1812 965 -162 C ATOM 824 C LEU A 104 8.477 -83.149 11.192 1.00 88.51 C ANISOU 824 C LEU A 104 11251 17600 4779 1995 1236 214 C ATOM 825 O LEU A 104 8.935 -83.916 10.347 1.00136.43 O ANISOU 825 O LEU A 104 17467 23687 10681 2400 1242 464 O ATOM 826 CB LEU A 104 6.957 -81.677 9.789 1.00116.95 C ANISOU 826 CB LEU A 104 14560 21938 7936 1869 801 -310 C ATOM 827 CG LEU A 104 7.180 -80.170 9.867 1.00130.57 C ANISOU 827 CG LEU A 104 16401 23489 9722 1500 846 -533 C ATOM 828 CD1 LEU A 104 8.211 -79.737 8.839 1.00138.62 C ANISOU 828 CD1 LEU A 104 17777 24323 10570 1695 955 -386 C ATOM 829 CD2 LEU A 104 5.859 -79.459 9.630 1.00118.18 C ANISOU 829 CD2 LEU A 104 14505 22385 8014 1285 556 -946 C ATOM 830 N SER A 105 9.152 -82.796 12.280 1.00 88.78 N ANISOU 830 N SER A 105 11414 17185 5134 1696 1449 254 N ATOM 831 CA SER A 105 10.418 -83.434 12.603 1.00 96.45 C ANISOU 831 CA SER A 105 12658 17685 6303 1833 1699 580 C ATOM 832 C SER A 105 10.134 -84.869 13.033 1.00 93.68 C ANISOU 832 C SER A 105 12203 17397 5992 2088 1692 719 C ATOM 833 O SER A 105 10.845 -85.798 12.645 1.00101.42 O ANISOU 833 O SER A 105 13364 18217 6955 2435 1792 1013 O ATOM 834 CB SER A 105 11.151 -82.672 13.708 1.00 82.01 C ANISOU 834 CB SER A 105 10952 15407 4801 1455 1892 554 C ATOM 835 OG SER A 105 12.528 -83.001 13.728 1.00172.01 O ANISOU 835 OG SER A 105 22620 26369 16367 1574 2135 845 O ATOM 836 N ILE A 106 9.076 -85.042 13.824 1.00 92.24 N ANISOU 836 N ILE A 106 11731 17460 5857 1918 1590 503 N ATOM 837 CA ILE A 106 8.633 -86.372 14.250 1.00 84.28 C ANISOU 837 CA ILE A 106 10576 16594 4854 2166 1587 566 C ATOM 838 C ILE A 106 8.017 -87.159 13.088 1.00 87.60 C ANISOU 838 C ILE A 106 10849 17497 4940 2645 1399 610 C ATOM 839 O ILE A 106 8.331 -88.341 12.886 1.00115.86 O ANISOU 839 O ILE A 106 14513 21043 8467 3067 1448 840 O ATOM 840 CB ILE A 106 7.610 -86.279 15.405 1.00 86.52 C ANISOU 840 CB ILE A 106 10567 17045 5262 1822 1557 300 C ATOM 841 CG1 ILE A 106 8.200 -85.504 16.584 1.00 77.91 C ANISOU 841 CG1 ILE A 106 9645 15485 4471 1374 1707 275 C ATOM 842 CG2 ILE A 106 7.178 -87.662 15.857 1.00 82.93 C ANISOU 842 CG2 ILE A 106 9957 16744 4808 2095 1592 336 C ATOM 843 CD1 ILE A 106 7.175 -85.109 17.622 1.00 76.95 C ANISOU 843 CD1 ILE A 106 9282 15514 4442 960 1668 20 C ATOM 844 N CYS A 107 7.141 -86.499 12.332 1.00 89.95 N ANISOU 844 N CYS A 107 10931 18246 5001 2597 1170 383 N ATOM 845 CA CYS A 107 6.527 -87.099 11.147 1.00 96.77 C ANISOU 845 CA CYS A 107 11643 19612 5514 3050 932 395 C ATOM 846 C CYS A 107 7.609 -87.586 10.185 1.00111.15 C ANISOU 846 C CYS A 107 13840 21184 7209 3469 997 767 C ATOM 847 O CYS A 107 7.464 -88.636 9.556 1.00113.02 O ANISOU 847 O CYS A 107 14061 21635 7245 3963 892 939 O ATOM 848 CB CYS A 107 5.603 -86.108 10.429 1.00116.97 C ANISOU 848 CB CYS A 107 13966 22625 7853 2885 666 79 C ATOM 849 SG CYS A 107 4.091 -85.611 11.312 1.00167.52 S ANISOU 849 SG CYS A 107 19851 29465 14336 2423 547 -375 S ATOM 850 N SER A 108 8.687 -86.812 10.074 1.00101.10 N ANISOU 850 N SER A 108 12897 19463 6052 3272 1177 893 N ATOM 851 CA SER A 108 9.838 -87.214 9.272 1.00116.46 C ANISOU 851 CA SER A 108 15216 21107 7927 3585 1314 1263 C ATOM 852 C SER A 108 10.565 -88.384 9.925 1.00 95.07 C ANISOU 852 C SER A 108 12663 18023 5434 3790 1526 1562 C ATOM 853 O SER A 108 11.037 -89.296 9.244 1.00109.53 O ANISOU 853 O SER A 108 14690 19784 7143 4227 1554 1878 O ATOM 854 CB SER A 108 10.804 -86.042 9.086 1.00131.18 C ANISOU 854 CB SER A 108 17345 22617 9882 3283 1492 1280 C ATOM 855 OG SER A 108 12.018 -86.464 8.491 1.00129.06 O ANISOU 855 OG SER A 108 17422 22007 9608 3521 1696 1651 O ATOM 856 N LEU A 109 10.650 -88.354 11.252 1.00105.04 N ANISOU 856 N LEU A 109 13862 19033 7017 3478 1669 1461 N ATOM 857 CA LEU A 109 11.306 -89.420 12.001 1.00105.82 C ANISOU 857 CA LEU A 109 14106 18764 7337 3639 1868 1691 C ATOM 858 C LEU A 109 10.605 -90.765 11.804 1.00107.22 C ANISOU 858 C LEU A 109 14143 19261 7334 4128 1747 1757 C ATOM 859 O LEU A 109 11.220 -91.821 11.968 1.00103.50 O ANISOU 859 O LEU A 109 13846 18428 7053 4393 1857 1999 O ATOM 860 CB LEU A 109 11.377 -89.065 13.488 1.00 85.54 C ANISOU 860 CB LEU A 109 11471 15924 5107 3197 1997 1513 C ATOM 861 CG LEU A 109 12.184 -90.011 14.378 1.00 84.09 C ANISOU 861 CG LEU A 109 11463 15247 5241 3271 2195 1699 C ATOM 862 CD1 LEU A 109 13.608 -90.140 13.859 1.00 92.02 C ANISOU 862 CD1 LEU A 109 12836 15799 6327 3423 2413 2067 C ATOM 863 CD2 LEU A 109 12.174 -89.532 15.818 1.00 97.76 C ANISOU 863 CD2 LEU A 109 13123 16725 7296 2798 2254 1482 C ATOM 864 N LEU A 110 9.324 -90.733 11.449 1.00109.72 N ANISOU 864 N LEU A 110 14107 20155 7426 4203 1480 1500 N ATOM 865 CA LEU A 110 8.614 -91.981 11.169 1.00 98.58 C ANISOU 865 CA LEU A 110 12490 18996 5969 4655 1306 1512 C ATOM 866 C LEU A 110 9.051 -92.670 9.874 1.00105.98 C ANISOU 866 C LEU A 110 13671 19971 6626 5230 1216 1865 C ATOM 867 O LEU A 110 9.396 -93.851 9.888 1.00127.29 O ANISOU 867 O LEU A 110 16488 22408 9467 5602 1259 2090 O ATOM 868 CB LEU A 110 7.098 -91.774 11.183 1.00104.18 C ANISOU 868 CB LEU A 110 12695 20323 6565 4562 1047 1122 C ATOM 869 CG LEU A 110 6.467 -91.591 12.565 1.00 96.95 C ANISOU 869 CG LEU A 110 11500 19384 5955 4108 1142 813 C ATOM 870 CD1 LEU A 110 4.993 -91.933 12.516 1.00 99.92 C ANISOU 870 CD1 LEU A 110 11349 20343 6272 4180 924 503 C ATOM 871 CD2 LEU A 110 7.182 -92.434 13.611 1.00110.44 C ANISOU 871 CD2 LEU A 110 13398 20555 8008 4120 1382 948 C ATOM 872 N CYS A 111 9.035 -91.941 8.757 1.00139.87 N ANISOU 872 N CYS A 111 18057 24564 10522 5305 1084 1909 N ATOM 873 CA CYS A 111 9.405 -92.519 7.464 1.00126.89 C ANISOU 873 CA CYS A 111 16655 22933 8626 5814 972 2238 C ATOM 874 C CYS A 111 10.881 -92.879 7.438 1.00141.07 C ANISOU 874 C CYS A 111 18926 24060 10614 5880 1292 2665 C ATOM 875 O CYS A 111 11.290 -93.842 6.789 1.00145.44 O ANISOU 875 O CYS A 111 19712 24471 11078 6354 1283 3017 O ATOM 876 CB CYS A 111 9.121 -91.547 6.317 1.00123.11 C ANISOU 876 CB CYS A 111 16156 22747 7872 5734 765 2111 C ATOM 877 SG CYS A 111 7.512 -90.741 6.351 1.00175.93 S ANISOU 877 SG CYS A 111 22298 30143 14405 5484 418 1561 S ATOM 878 N ASP A 112 11.681 -92.087 8.143 1.00135.97 N ANISOU 878 N ASP A 112 18412 22991 10260 5394 1565 2629 N ATOM 879 CA ASP A 112 13.127 -92.253 8.121 1.00146.33 C ANISOU 879 CA ASP A 112 20127 23679 11792 5375 1882 2992 C ATOM 880 C ASP A 112 13.705 -92.242 9.529 1.00131.03 C ANISOU 880 C ASP A 112 18219 21296 10272 5035 2143 2952 C ATOM 881 O ASP A 112 14.087 -91.189 10.039 1.00121.24 O ANISOU 881 O ASP A 112 16962 19874 9231 4557 2262 2784 O ATOM 882 CB ASP A 112 13.771 -91.151 7.284 1.00174.31 C ANISOU 882 CB ASP A 112 23847 27135 15249 5143 1960 3019 C ATOM 883 CG ASP A 112 15.197 -91.473 6.899 1.00206.91 C ANISOU 883 CG ASP A 112 28372 30721 19522 5228 2264 3435 C ATOM 884 OD1 ASP A 112 16.109 -91.200 7.708 1.00194.71 O ANISOU 884 OD1 ASP A 112 26927 28712 18343 4911 2543 3482 O ATOM 885 OD2 ASP A 112 15.403 -92.000 5.786 1.00228.49 O ANISOU 885 OD2 ASP A 112 31308 33493 22014 5603 2219 3713 O ATOM 886 N PRO A 113 13.772 -93.421 10.163 1.00124.56 N ANISOU 886 N PRO A 113 17427 20247 9655 5267 2196 3069 N ATOM 887 CA PRO A 113 14.297 -93.565 11.526 1.00 96.54 C ANISOU 887 CA PRO A 113 13876 16193 6614 4930 2379 2969 C ATOM 888 C PRO A 113 15.793 -93.284 11.614 1.00 96.35 C ANISOU 888 C PRO A 113 14197 15575 6838 4752 2698 3258 C ATOM 889 O PRO A 113 16.418 -92.913 10.620 1.00129.48 O ANISOU 889 O PRO A 113 18623 19751 10822 4851 2810 3524 O ATOM 890 CB PRO A 113 14.008 -95.031 11.861 1.00102.21 C ANISOU 890 CB PRO A 113 14539 16764 7531 5288 2297 3001 C ATOM 891 CG PRO A 113 13.892 -95.702 10.553 1.00127.28 C ANISOU 891 CG PRO A 113 17842 20134 10384 5840 2170 3295 C ATOM 892 CD PRO A 113 13.286 -94.703 9.626 1.00156.02 C ANISOU 892 CD PRO A 113 21380 24362 13539 5817 2008 3207 C ATOM 893 N ASN A 114 16.358 -93.474 12.801 1.00113.63 N ANISOU 893 N ASN A 114 16400 17277 9497 4479 2831 3182 N ATOM 894 CA ASN A 114 17.716 -93.023 13.075 1.00106.94 C ANISOU 894 CA ASN A 114 15784 15888 8959 4209 3115 3365 C ATOM 895 C ASN A 114 18.524 -93.994 13.940 1.00131.95 C ANISOU 895 C ASN A 114 19079 18418 12639 4201 3233 3462 C ATOM 896 O ASN A 114 18.738 -93.741 15.125 1.00156.27 O ANISOU 896 O ASN A 114 22072 21239 16063 3848 3250 3238 O ATOM 897 CB ASN A 114 17.649 -91.658 13.756 1.00108.35 C ANISOU 897 CB ASN A 114 15809 16152 9208 3705 3132 3069 C ATOM 898 CG ASN A 114 18.887 -90.831 13.525 1.00154.15 C ANISOU 898 CG ASN A 114 21802 21620 15149 3488 3410 3255 C ATOM 899 OD1 ASN A 114 19.986 -91.367 13.378 1.00161.66 O ANISOU 899 OD1 ASN A 114 22978 22095 16350 3574 3632 3565 O ATOM 900 ND2 ASN A 114 18.718 -89.514 13.485 1.00163.32 N ANISOU 900 ND2 ASN A 114 22833 22985 16237 3167 3367 3019 N ATOM 901 N PRO A 115 18.984 -95.108 13.353 1.00119.69 N ANISOU 901 N PRO A 115 17747 16591 11139 4593 3297 3793 N ATOM 902 CA PRO A 115 19.740 -96.142 14.071 1.00116.98 C ANISOU 902 CA PRO A 115 17543 15613 11290 4628 3390 3883 C ATOM 903 C PRO A 115 21.143 -95.703 14.476 1.00145.43 C ANISOU 903 C PRO A 115 21309 18632 15314 4278 3662 4027 C ATOM 904 O PRO A 115 21.966 -96.547 14.826 1.00129.32 O ANISOU 904 O PRO A 115 19433 16013 13691 4322 3770 4176 O ATOM 905 CB PRO A 115 19.806 -97.306 13.089 1.00108.52 C ANISOU 905 CB PRO A 115 16682 14448 10101 5167 3379 4239 C ATOM 906 CG PRO A 115 18.884 -96.943 11.967 1.00136.80 C ANISOU 906 CG PRO A 115 20185 18699 13095 5436 3215 4277 C ATOM 907 CD PRO A 115 18.837 -95.458 11.930 1.00122.90 C ANISOU 907 CD PRO A 115 18314 17250 11132 5041 3269 4117 C ATOM 908 N ASP A 116 21.426 -94.414 14.351 1.00180.13 N ANISOU 908 N ASP A 116 25655 23170 19615 3958 3774 3986 N ATOM 909 CA ASP A 116 22.710 -93.856 14.740 1.00234.08 C ANISOU 909 CA ASP A 116 32573 29507 26861 3608 4030 4081 C ATOM 910 C ASP A 116 22.759 -93.719 16.254 1.00217.07 C ANISOU 910 C ASP A 116 30252 27100 25125 3251 3914 3726 C ATOM 911 O ASP A 116 23.599 -94.323 16.923 1.00198.11 O ANISOU 911 O ASP A 116 27933 24134 23206 3161 3983 3767 O ATOM 912 CB ASP A 116 22.914 -92.491 14.078 1.00266.51 C ANISOU 912 CB ASP A 116 36662 33897 30703 3423 4181 4116 C ATOM 913 CG ASP A 116 24.291 -91.916 14.337 1.00270.80 C ANISOU 913 CG ASP A 116 37266 33946 31678 3101 4486 4239 C ATOM 914 OD1 ASP A 116 25.272 -92.687 14.316 1.00282.61 O ANISOU 914 OD1 ASP A 116 38930 34908 33540 3154 4679 4517 O ATOM 915 OD2 ASP A 116 24.395 -90.690 14.561 1.00237.75 O ANISOU 915 OD2 ASP A 116 32945 29893 27498 2795 4532 4051 O ATOM 916 N ASP A 117 21.843 -92.911 16.777 1.00183.24 N ANISOU 916 N ASP A 117 25744 23235 20643 3045 3726 3380 N ATOM 917 CA ASP A 117 21.736 -92.652 18.204 1.00143.50 C ANISOU 917 CA ASP A 117 20570 18048 15907 2705 3586 3042 C ATOM 918 C ASP A 117 20.387 -93.183 18.669 1.00166.47 C ANISOU 918 C ASP A 117 23330 21348 18571 2834 3335 2773 C ATOM 919 O ASP A 117 19.424 -92.426 18.799 1.00210.22 O ANISOU 919 O ASP A 117 28687 27356 23831 2692 3202 2544 O ATOM 920 CB ASP A 117 21.825 -91.148 18.458 1.00199.12 C ANISOU 920 CB ASP A 117 27489 25226 22941 2323 3603 2882 C ATOM 921 CG ASP A 117 22.756 -90.801 19.602 1.00213.03 C ANISOU 921 CG ASP A 117 29235 26481 25225 1966 3622 2770 C ATOM 922 OD1 ASP A 117 23.654 -91.613 19.908 1.00207.56 O ANISOU 922 OD1 ASP A 117 28658 25278 24928 2002 3704 2897 O ATOM 923 OD2 ASP A 117 22.585 -89.718 20.198 1.00219.28 O ANISOU 923 OD2 ASP A 117 29897 27372 26047 1653 3535 2549 O ATOM 924 N PRO A 118 20.309 -94.503 18.886 1.00113.93 N ANISOU 924 N PRO A 118 16750 14501 12040 3109 3287 2798 N ATOM 925 CA PRO A 118 19.069 -95.216 19.202 1.00 96.94 C ANISOU 925 CA PRO A 118 14451 12712 9669 3313 3097 2568 C ATOM 926 C PRO A 118 18.609 -95.027 20.634 1.00 91.09 C ANISOU 926 C PRO A 118 13583 11984 9041 3002 2968 2200 C ATOM 927 O PRO A 118 19.425 -95.053 21.554 1.00121.20 O ANISOU 927 O PRO A 118 17499 15326 13226 2772 2987 2139 O ATOM 928 CB PRO A 118 19.447 -96.688 18.988 1.00124.60 C ANISOU 928 CB PRO A 118 18124 15855 13362 3708 3131 2740 C ATOM 929 CG PRO A 118 20.905 -96.701 18.574 1.00137.37 C ANISOU 929 CG PRO A 118 19988 16898 15308 3666 3346 3080 C ATOM 930 CD PRO A 118 21.473 -95.391 18.985 1.00117.37 C ANISOU 930 CD PRO A 118 17400 14291 12903 3204 3421 3013 C ATOM 931 N LEU A 119 17.306 -94.857 20.818 1.00 93.17 N ANISOU 931 N LEU A 119 13626 12789 8984 2994 2835 1959 N ATOM 932 CA LEU A 119 16.710 -94.875 22.146 1.00 94.66 C ANISOU 932 CA LEU A 119 13715 13041 9211 2756 2731 1630 C ATOM 933 C LEU A 119 16.450 -96.306 22.606 1.00 96.61 C ANISOU 933 C LEU A 119 13994 13173 9542 3057 2704 1521 C ATOM 934 O LEU A 119 16.494 -96.612 23.797 1.00124.05 O ANISOU 934 O LEU A 119 17517 16447 13171 2900 2662 1304 O ATOM 935 CB LEU A 119 15.408 -94.085 22.142 1.00 87.82 C ANISOU 935 CB LEU A 119 12589 12794 7984 2594 2638 1428 C ATOM 936 CG LEU A 119 14.783 -93.874 23.513 1.00 73.09 C ANISOU 936 CG LEU A 119 10642 11014 6117 2276 2564 1126 C ATOM 937 CD1 LEU A 119 15.778 -93.181 24.426 1.00107.42 C ANISOU 937 CD1 LEU A 119 15165 14887 10762 1903 2556 1119 C ATOM 938 CD2 LEU A 119 13.511 -93.061 23.377 1.00 89.68 C ANISOU 938 CD2 LEU A 119 12480 13706 7890 2097 2498 965 C ATOM 939 N VAL A 120 16.172 -97.177 21.644 1.00111.59 N ANISOU 939 N VAL A 120 15873 15202 11324 3510 2716 1665 N ATOM 940 CA VAL A 120 15.868 -98.574 21.922 1.00105.39 C ANISOU 940 CA VAL A 120 15100 14327 10618 3868 2692 1559 C ATOM 941 C VAL A 120 16.835 -99.458 21.151 1.00134.28 C ANISOU 941 C VAL A 120 19002 17507 14513 4226 2764 1875 C ATOM 942 O VAL A 120 16.594 -99.780 19.984 1.00118.67 O ANISOU 942 O VAL A 120 17008 15725 12356 4594 2758 2096 O ATOM 943 CB VAL A 120 14.431 -98.935 21.518 1.00103.28 C ANISOU 943 CB VAL A 120 14536 14701 10005 4143 2612 1404 C ATOM 944 CG1 VAL A 120 14.112-100.365 21.925 1.00109.91 C ANISOU 944 CG1 VAL A 120 15368 15439 10954 4513 2603 1244 C ATOM 945 CG2 VAL A 120 13.445 -97.968 22.150 1.00101.14 C ANISOU 945 CG2 VAL A 120 14015 14914 9499 3754 2566 1134 C ATOM 946 N PRO A 121 17.945 -99.834 21.801 1.00112.92 N ANISOU 946 N PRO A 121 16529 14159 12215 4109 2822 1903 N ATOM 947 CA PRO A 121 19.067-100.564 21.198 1.00109.86 C ANISOU 947 CA PRO A 121 16404 13193 12146 4341 2922 2222 C ATOM 948 C PRO A 121 18.636-101.795 20.401 1.00123.53 C ANISOU 948 C PRO A 121 18166 14971 13800 4914 2895 2345 C ATOM 949 O PRO A 121 19.155-102.020 19.305 1.00147.92 O ANISOU 949 O PRO A 121 21414 17888 16903 5163 2971 2725 O ATOM 950 CB PRO A 121 19.890-100.993 22.416 1.00120.93 C ANISOU 950 CB PRO A 121 17960 14003 13987 4128 2913 2038 C ATOM 951 CG PRO A 121 19.590 -99.966 23.446 1.00118.71 C ANISOU 951 CG PRO A 121 17547 13946 13614 3668 2838 1758 C ATOM 952 CD PRO A 121 18.147 -99.608 23.241 1.00107.88 C ANISOU 952 CD PRO A 121 15915 13312 11765 3734 2774 1605 C ATOM 953 N GLU A 122 17.698-102.569 20.936 1.00129.99 N ANISOU 953 N GLU A 122 18837 16023 14529 5131 2794 2034 N ATOM 954 CA GLU A 122 17.280-103.803 20.279 1.00125.35 C ANISOU 954 CA GLU A 122 18258 15449 13922 5709 2749 2108 C ATOM 955 C GLU A 122 16.584-103.547 18.946 1.00110.50 C ANISOU 955 C GLU A 122 16231 14098 11655 6006 2689 2337 C ATOM 956 O GLU A 122 16.950-104.141 17.931 1.00125.62 O ANISOU 956 O GLU A 122 18317 15813 13598 6398 2694 2679 O ATOM 957 CB GLU A 122 16.389-104.645 21.198 1.00123.31 C ANISOU 957 CB GLU A 122 17835 15365 13653 5871 2678 1676 C ATOM 958 CG GLU A 122 15.822-105.907 20.548 1.00152.00 C ANISOU 958 CG GLU A 122 21414 19068 17270 6505 2615 1698 C ATOM 959 CD GLU A 122 16.844-107.026 20.397 1.00187.29 C ANISOU 959 CD GLU A 122 26225 22772 22162 6804 2651 1885 C ATOM 960 OE1 GLU A 122 16.443-108.139 19.994 1.00198.88 O ANISOU 960 OE1 GLU A 122 27678 24209 23678 7339 2589 1875 O ATOM 961 OE2 GLU A 122 18.042-106.805 20.678 1.00168.24 O ANISOU 961 OE2 GLU A 122 24083 19778 20065 6510 2735 2035 O ATOM 962 N ILE A 123 15.587-102.666 18.952 1.00143.57 N ANISOU 962 N ILE A 123 20118 18947 15484 5816 2620 2152 N ATOM 963 CA ILE A 123 14.869-102.309 17.730 1.00102.15 C ANISOU 963 CA ILE A 123 14705 14255 9852 6054 2522 2312 C ATOM 964 C ILE A 123 15.844-101.731 16.713 1.00102.40 C ANISOU 964 C ILE A 123 15004 14061 9842 6021 2608 2753 C ATOM 965 O ILE A 123 15.736-101.989 15.515 1.00114.19 O ANISOU 965 O ILE A 123 16556 15708 11121 6409 2545 3038 O ATOM 966 CB ILE A 123 13.732-101.293 17.992 1.00 99.36 C ANISOU 966 CB ILE A 123 13988 14593 9171 5745 2443 2017 C ATOM 967 CG1 ILE A 123 12.665-101.899 18.905 1.00107.04 C ANISOU 967 CG1 ILE A 123 14671 15858 10140 5799 2398 1601 C ATOM 968 CG2 ILE A 123 13.086-100.859 16.688 1.00117.97 C ANISOU 968 CG2 ILE A 123 16187 17495 11143 5965 2314 2169 C ATOM 969 CD1 ILE A 123 11.478-100.982 19.140 1.00115.17 C ANISOU 969 CD1 ILE A 123 15326 17560 10872 5497 2339 1326 C ATOM 970 N ALA A 124 16.802-100.955 17.205 1.00115.19 N ANISOU 970 N ALA A 124 16785 15320 11661 5567 2753 2809 N ATOM 971 CA ALA A 124 17.839-100.401 16.346 1.00125.02 C ANISOU 971 CA ALA A 124 18284 16306 12912 5496 2899 3214 C ATOM 972 C ALA A 124 18.604-101.524 15.663 1.00120.21 C ANISOU 972 C ALA A 124 17978 15191 12504 5914 2972 3590 C ATOM 973 O ALA A 124 18.859-101.468 14.460 1.00130.46 O ANISOU 973 O ALA A 124 19440 16543 13587 6155 3014 3970 O ATOM 974 CB ALA A 124 18.786 -99.542 17.148 1.00133.48 C ANISOU 974 CB ALA A 124 19440 17008 14270 4959 3046 3166 C ATOM 975 N ARG A 125 18.958-102.543 16.439 1.00146.16 N ANISOU 975 N ARG A 125 21363 17978 16194 5999 2982 3481 N ATOM 976 CA ARG A 125 19.701-103.680 15.913 1.00133.79 C ANISOU 976 CA ARG A 125 20099 15839 14896 6377 3048 3815 C ATOM 977 C ARG A 125 18.889-104.403 14.846 1.00138.20 C ANISOU 977 C ARG A 125 20629 16740 15140 6981 2892 3980 C ATOM 978 O ARG A 125 19.410-104.734 13.780 1.00142.05 O ANISOU 978 O ARG A 125 21383 17012 15578 7277 2949 4434 O ATOM 979 CB ARG A 125 20.070-104.648 17.040 1.00137.30 C ANISOU 979 CB ARG A 125 20618 15725 15824 6362 3044 3566 C ATOM 980 CG ARG A 125 21.085-105.712 16.641 1.00138.94 C ANISOU 980 CG ARG A 125 21178 15183 16432 6634 3144 3907 C ATOM 981 CD ARG A 125 21.288-106.721 17.759 1.00147.30 C ANISOU 981 CD ARG A 125 22288 15741 17937 6661 3095 3581 C ATOM 982 NE ARG A 125 20.084-107.510 17.999 1.00176.72 N ANISOU 982 NE ARG A 125 25812 19842 21491 7060 2914 3251 N ATOM 983 CZ ARG A 125 19.853-108.702 17.458 1.00202.35 C ANISOU 983 CZ ARG A 125 29157 22913 24814 7627 2839 3362 C ATOM 984 NH1 ARG A 125 20.747-109.248 16.646 1.00205.71 N ANISOU 984 NH1 ARG A 125 29919 22769 25474 7852 2924 3824 N ATOM 985 NH2 ARG A 125 18.728-109.347 17.731 1.00196.91 N ANISOU 985 NH2 ARG A 125 28227 22608 23980 7973 2689 3016 N ATOM 986 N ILE A 126 17.613-104.634 15.140 1.00181.99 N ANISOU 986 N ILE A 126 25846 22826 20477 7159 2697 3616 N ATOM 987 CA ILE A 126 16.715-105.321 14.214 1.00131.89 C ANISOU 987 CA ILE A 126 19389 16868 13856 7746 2501 3699 C ATOM 988 C ILE A 126 16.596-104.558 12.897 1.00132.99 C ANISOU 988 C ILE A 126 19567 17425 13538 7842 2451 4034 C ATOM 989 O ILE A 126 16.732-105.138 11.824 1.00139.69 O ANISOU 989 O ILE A 126 20617 18198 14263 8309 2384 4409 O ATOM 990 CB ILE A 126 15.304-105.511 14.821 1.00131.18 C ANISOU 990 CB ILE A 126 18852 17370 13621 7834 2329 3200 C ATOM 991 CG1 ILE A 126 15.382-106.237 16.171 1.00130.34 C ANISOU 991 CG1 ILE A 126 18725 16898 13901 7735 2393 2834 C ATOM 992 CG2 ILE A 126 14.398-106.254 13.851 1.00136.20 C ANISOU 992 CG2 ILE A 126 19327 18398 14023 8467 2105 3272 C ATOM 993 CD1 ILE A 126 15.973-107.628 16.102 1.00134.93 C ANISOU 993 CD1 ILE A 126 19580 16832 14857 8176 2404 2975 C ATOM 994 N TYR A 127 16.353-103.256 12.990 1.00117.31 N ANISOU 994 N TYR A 127 17413 15865 11295 7405 2475 3894 N ATOM 995 CA TYR A 127 16.196-102.407 11.814 1.00118.15 C ANISOU 995 CA TYR A 127 17545 16413 10934 7449 2423 4134 C ATOM 996 C TYR A 127 17.474-102.351 10.988 1.00146.02 C ANISOU 996 C TYR A 127 21529 19464 14489 7492 2633 4673 C ATOM 997 O TYR A 127 17.438-102.396 9.754 1.00132.97 O ANISOU 997 O TYR A 127 20039 18007 12478 7842 2562 5018 O ATOM 998 CB TYR A 127 15.798-100.993 12.240 1.00113.16 C ANISOU 998 CB TYR A 127 16666 16223 10107 6914 2438 3836 C ATOM 999 CG TYR A 127 15.680-100.011 11.096 1.00113.89 C ANISOU 999 CG TYR A 127 16795 16759 9720 6908 2393 4022 C ATOM 1000 CD1 TYR A 127 16.771 -99.259 10.682 1.00119.79 C ANISOU 1000 CD1 TYR A 127 17845 17231 10438 6668 2631 4325 C ATOM 1001 CD2 TYR A 127 14.475 -99.829 10.436 1.00121.17 C ANISOU 1001 CD2 TYR A 127 17434 18385 10220 7142 2116 3868 C ATOM 1002 CE1 TYR A 127 16.669 -98.358 9.639 1.00131.52 C ANISOU 1002 CE1 TYR A 127 19387 19134 11452 6676 2605 4467 C ATOM 1003 CE2 TYR A 127 14.360 -98.931 9.392 1.00152.25 C ANISOU 1003 CE2 TYR A 127 21420 22733 13696 7143 2049 4001 C ATOM 1004 CZ TYR A 127 15.460 -98.198 8.997 1.00136.43 C ANISOU 1004 CZ TYR A 127 19755 20447 11635 6916 2300 4298 C ATOM 1005 OH TYR A 127 15.352 -97.302 7.961 1.00117.33 O ANISOU 1005 OH TYR A 127 17408 18449 8724 6929 2248 4403 O ATOM 1006 N LYS A 128 18.601-102.237 11.679 1.00169.96 N ANISOU 1006 N LYS A 128 24758 21879 17940 7125 2892 4742 N ATOM 1007 CA LYS A 128 19.891-102.097 11.020 1.00169.49 C ANISOU 1007 CA LYS A 128 25094 21336 17968 7069 3158 5234 C ATOM 1008 C LYS A 128 20.313-103.396 10.334 1.00172.56 C ANISOU 1008 C LYS A 128 25806 21268 18489 7589 3161 5651 C ATOM 1009 O LYS A 128 20.965-103.368 9.291 1.00171.09 O ANISOU 1009 O LYS A 128 25916 20939 18152 7701 3294 6094 O ATOM 1010 CB LYS A 128 20.952-101.643 12.025 1.00157.87 C ANISOU 1010 CB LYS A 128 23679 19327 16977 6520 3413 5148 C ATOM 1011 CG LYS A 128 22.183-101.024 11.392 1.00172.66 C ANISOU 1011 CG LYS A 128 25840 20879 18884 6307 3733 5571 C ATOM 1012 CD LYS A 128 22.723 -99.887 12.244 1.00184.69 C ANISOU 1012 CD LYS A 128 27222 22320 20632 5697 3895 5334 C ATOM 1013 CE LYS A 128 23.845 -99.151 11.530 1.00196.82 C ANISOU 1013 CE LYS A 128 28985 23648 22152 5495 4236 5722 C ATOM 1014 NZ LYS A 128 24.212 -97.889 12.229 1.00184.75 N ANISOU 1014 NZ LYS A 128 27266 22162 20769 4949 4357 5463 N ATOM 1015 N THR A 129 19.925-104.530 10.915 1.00169.43 N ANISOU 1015 N THR A 129 25333 20657 18388 7864 3012 5452 N ATOM 1016 CA THR A 129 20.297-105.830 10.355 1.00144.85 C ANISOU 1016 CA THR A 129 22525 17047 15466 8377 2993 5814 C ATOM 1017 C THR A 129 19.204-106.444 9.474 1.00141.80 C ANISOU 1017 C THR A 129 22024 17156 14697 8985 2674 5842 C ATOM 1018 O THR A 129 19.367-106.539 8.258 1.00146.21 O ANISOU 1018 O THR A 129 22742 17816 14993 9132 2635 6138 O ATOM 1019 CB THR A 129 20.730-106.831 11.452 1.00140.49 C ANISOU 1019 CB THR A 129 22018 15820 15543 8344 3038 5603 C ATOM 1020 OG1 THR A 129 19.614-107.149 12.292 1.00135.73 O ANISOU 1020 OG1 THR A 129 21038 15594 14940 8431 2817 5053 O ATOM 1021 CG2 THR A 129 21.853-106.245 12.302 1.00164.76 C ANISOU 1021 CG2 THR A 129 25178 18396 19026 7727 3310 5552 C ATOM 1022 N ASP A 130 18.096-106.859 10.087 1.00173.75 N ANISOU 1022 N ASP A 130 25704 21558 18754 9180 2440 5394 N ATOM 1023 CA ASP A 130 17.006-107.500 9.351 1.00167.58 C ANISOU 1023 CA ASP A 130 24747 21249 17678 9796 2117 5379 C ATOM 1024 C ASP A 130 15.774-106.598 9.243 1.00155.73 C ANISOU 1024 C ASP A 130 22789 20666 15715 9686 1911 5025 C ATOM 1025 O ASP A 130 15.024-106.434 10.207 1.00151.96 O ANISOU 1025 O ASP A 130 21919 20488 15330 9459 1866 4515 O ATOM 1026 CB ASP A 130 16.627-108.820 10.029 1.00160.40 C ANISOU 1026 CB ASP A 130 23722 20049 17173 10157 2009 5109 C ATOM 1027 CG ASP A 130 15.469-109.522 9.345 1.00175.74 C ANISOU 1027 CG ASP A 130 25410 22482 18880 10783 1669 5028 C ATOM 1028 OD1 ASP A 130 15.257-109.296 8.136 1.00195.15 O ANISOU 1028 OD1 ASP A 130 27917 25292 20938 10943 1513 5282 O ATOM 1029 OD2 ASP A 130 14.778-110.312 10.022 1.00173.42 O ANISOU 1029 OD2 ASP A 130 24841 22234 18817 11041 1563 4646 O ATOM 1030 N ARG A 131 15.541-106.064 8.047 1.00158.00 N ANISOU 1030 N ARG A 131 23139 21395 15499 9869 1778 5300 N ATOM 1031 CA ARG A 131 14.475-105.089 7.821 1.00136.01 C ANISOU 1031 CA ARG A 131 19956 19453 12267 9723 1580 4993 C ATOM 1032 C ARG A 131 13.112-105.762 7.697 1.00146.59 C ANISOU 1032 C ARG A 131 20859 21327 13510 10190 1225 4686 C ATOM 1033 O ARG A 131 12.088-105.177 8.047 1.00138.67 O ANISOU 1033 O ARG A 131 19392 20941 12355 9982 1094 4249 O ATOM 1034 CB ARG A 131 14.770-104.258 6.570 1.00137.77 C ANISOU 1034 CB ARG A 131 20429 19948 11968 9750 1559 5373 C ATOM 1035 CG ARG A 131 13.847-103.068 6.376 1.00135.20 C ANISOU 1035 CG ARG A 131 19742 20419 11208 9490 1390 5043 C ATOM 1036 CD ARG A 131 14.142-101.972 7.386 1.00128.45 C ANISOU 1036 CD ARG A 131 18771 19513 10519 8766 1646 4745 C ATOM 1037 NE ARG A 131 15.447-101.350 7.169 1.00139.53 N ANISOU 1037 NE ARG A 131 20600 20478 11936 8464 1975 5103 N ATOM 1038 CZ ARG A 131 15.648-100.276 6.411 1.00144.68 C ANISOU 1038 CZ ARG A 131 21378 21428 12167 8297 2026 5236 C ATOM 1039 NH1 ARG A 131 16.870 -99.777 6.275 1.00130.40 N ANISOU 1039 NH1 ARG A 131 19859 19158 10527 7933 2363 5441 N ATOM 1040 NH2 ARG A 131 14.629 -99.697 5.789 1.00128.01 N ANISOU 1040 NH2 ARG A 131 18994 20023 9620 8364 1737 5001 N ATOM 1041 N GLU A 132 13.112-106.983 7.173 1.00191.71 N ANISOU 1041 N GLU A 132 26720 26789 19333 10822 1074 4926 N ATOM 1042 CA GLU A 132 11.916-107.811 7.094 1.00195.41 C ANISOU 1042 CA GLU A 132 26770 27666 19809 11336 752 4643 C ATOM 1043 C GLU A 132 11.207-107.847 8.439 1.00191.44 C ANISOU 1043 C GLU A 132 25800 27338 19601 11025 831 4033 C ATOM 1044 O GLU A 132 10.063-107.405 8.565 1.00190.46 O ANISOU 1044 O GLU A 132 25169 27911 19286 10938 666 3639 O ATOM 1045 CB GLU A 132 12.296-109.233 6.678 1.00208.66 C ANISOU 1045 CB GLU A 132 28711 28783 21786 11782 699 4859 C ATOM 1046 CG GLU A 132 11.169-110.250 6.790 1.00227.69 C ANISOU 1046 CG GLU A 132 30689 31478 24343 12261 425 4505 C ATOM 1047 CD GLU A 132 10.268-110.264 5.574 1.00237.80 C ANISOU 1047 CD GLU A 132 31747 33377 25228 12604 41 4522 C ATOM 1048 OE1 GLU A 132 9.673-109.214 5.255 1.00244.74 O ANISOU 1048 OE1 GLU A 132 32373 34925 25694 12448 -90 4413 O ATOM 1049 OE2 GLU A 132 10.161-111.328 4.930 1.00244.06 O ANISOU 1049 OE2 GLU A 132 32621 33973 26137 13022 -148 4634 O ATOM 1050 N LYS A 133 11.906-108.382 9.437 1.00142.73 N ANISOU 1050 N LYS A 133 19814 20522 13892 10853 1086 3961 N ATOM 1051 CA LYS A 133 11.366-108.525 10.782 1.00139.48 C ANISOU 1051 CA LYS A 133 19051 20189 13756 10577 1194 3413 C ATOM 1052 C LYS A 133 10.891-107.187 11.334 1.00133.69 C ANISOU 1052 C LYS A 133 18022 19972 12802 9929 1267 3096 C ATOM 1053 O LYS A 133 9.853-107.118 11.985 1.00132.54 O ANISOU 1053 O LYS A 133 17411 20301 12649 9815 1224 2637 O ATOM 1054 CB LYS A 133 12.412-109.134 11.721 1.00138.20 C ANISOU 1054 CB LYS A 133 19234 19196 14080 10418 1457 3428 C ATOM 1055 CG LYS A 133 11.830-109.750 12.989 1.00142.81 C ANISOU 1055 CG LYS A 133 19519 19788 14954 10377 1521 2889 C ATOM 1056 CD LYS A 133 12.747-109.549 14.194 1.00132.90 C ANISOU 1056 CD LYS A 133 18508 17969 14020 9840 1793 2762 C ATOM 1057 CE LYS A 133 14.113-110.190 13.993 1.00164.48 C ANISOU 1057 CE LYS A 133 23048 21076 18373 9965 1907 3160 C ATOM 1058 NZ LYS A 133 14.059-111.677 14.016 1.00178.59 N ANISOU 1058 NZ LYS A 133 24912 22461 20485 10561 1831 3111 N ATOM 1059 N TYR A 134 11.648-106.127 11.066 1.00130.40 N ANISOU 1059 N TYR A 134 17875 19453 12218 9508 1393 3346 N ATOM 1060 CA TYR A 134 11.284-104.798 11.549 1.00125.11 C ANISOU 1060 CA TYR A 134 16972 19206 11359 8893 1458 3074 C ATOM 1061 C TYR A 134 9.948-104.346 10.982 1.00126.50 C ANISOU 1061 C TYR A 134 16677 20225 11160 9000 1187 2843 C ATOM 1062 O TYR A 134 9.054-103.950 11.726 1.00124.10 O ANISOU 1062 O TYR A 134 15958 20337 10857 8697 1185 2413 O ATOM 1063 CB TYR A 134 12.361-103.764 11.207 1.00129.37 C ANISOU 1063 CB TYR A 134 17887 19486 11783 8501 1631 3400 C ATOM 1064 CG TYR A 134 11.944-102.335 11.498 1.00117.59 C ANISOU 1064 CG TYR A 134 16165 18453 10061 7935 1653 3147 C ATOM 1065 CD1 TYR A 134 12.013-101.819 12.789 1.00126.97 C ANISOU 1065 CD1 TYR A 134 17249 19515 11477 7390 1824 2835 C ATOM 1066 CD2 TYR A 134 11.484-101.501 10.485 1.00118.56 C ANISOU 1066 CD2 TYR A 134 16195 19119 9735 7957 1485 3216 C ATOM 1067 CE1 TYR A 134 11.635-100.516 13.061 1.00108.69 C ANISOU 1067 CE1 TYR A 134 14746 17573 8977 6884 1835 2620 C ATOM 1068 CE2 TYR A 134 11.104-100.198 10.748 1.00114.65 C ANISOU 1068 CE2 TYR A 134 15501 19000 9060 7444 1498 2967 C ATOM 1069 CZ TYR A 134 11.183 -99.712 12.037 1.00115.99 C ANISOU 1069 CZ TYR A 134 15573 19005 9492 6910 1678 2681 C ATOM 1070 OH TYR A 134 10.807 -98.416 12.306 1.00114.18 O ANISOU 1070 OH TYR A 134 15166 19108 9109 6411 1684 2450 O ATOM 1071 N ASN A 135 9.827-104.398 9.661 1.00130.72 N ANISOU 1071 N ASN A 135 17288 21004 11373 9420 956 3137 N ATOM 1072 CA ASN A 135 8.599-104.001 8.989 1.00132.87 C ANISOU 1072 CA ASN A 135 17122 22075 11290 9564 644 2930 C ATOM 1073 C ASN A 135 7.412-104.833 9.455 1.00135.35 C ANISOU 1073 C ASN A 135 16902 22742 11781 9843 500 2523 C ATOM 1074 O ASN A 135 6.341-104.295 9.741 1.00134.28 O ANISOU 1074 O ASN A 135 16269 23203 11547 9601 410 2126 O ATOM 1075 CB ASN A 135 8.761-104.098 7.470 1.00137.96 C ANISOU 1075 CB ASN A 135 18002 22861 11556 10057 387 3348 C ATOM 1076 CG ASN A 135 9.592-102.962 6.897 1.00135.77 C ANISOU 1076 CG ASN A 135 18113 22509 10963 9719 508 3644 C ATOM 1077 OD1 ASN A 135 10.114-102.125 7.630 1.00130.41 O ANISOU 1077 OD1 ASN A 135 17526 21626 10398 9131 784 3551 O ATOM 1078 ND2 ASN A 135 9.725-102.937 5.575 1.00157.88 N ANISOU 1078 ND2 ASN A 135 21151 25482 13356 10110 301 4002 N ATOM 1079 N ARG A 136 7.612-106.145 9.546 1.00156.68 N ANISOU 1079 N ARG A 136 19706 25057 14770 10343 498 2612 N ATOM 1080 CA ARG A 136 6.554-107.051 9.990 1.00155.52 C ANISOU 1080 CA ARG A 136 19062 25202 14825 10671 396 2223 C ATOM 1081 C ARG A 136 6.073-106.726 11.404 1.00151.03 C ANISOU 1081 C ARG A 136 18177 24760 14449 10128 646 1739 C ATOM 1082 O ARG A 136 4.874-106.533 11.636 1.00151.64 O ANISOU 1082 O ARG A 136 17692 25463 14462 10045 562 1346 O ATOM 1083 CB ARG A 136 7.023-108.505 9.904 1.00163.11 C ANISOU 1083 CB ARG A 136 20267 25605 16100 11289 386 2412 C ATOM 1084 CG ARG A 136 6.126-109.493 10.632 1.00162.64 C ANISOU 1084 CG ARG A 136 19752 25708 16336 11573 388 1966 C ATOM 1085 CD ARG A 136 6.406-110.920 10.195 1.00168.77 C ANISOU 1085 CD ARG A 136 20717 26043 17364 12332 264 2168 C ATOM 1086 NE ARG A 136 7.836-111.198 10.111 1.00173.28 N ANISOU 1086 NE ARG A 136 21978 25764 18097 12334 424 2619 N ATOM 1087 CZ ARG A 136 8.597-111.529 11.149 1.00176.65 C ANISOU 1087 CZ ARG A 136 22675 25567 18876 12072 723 2533 C ATOM 1088 NH1 ARG A 136 8.062-111.621 12.361 1.00163.06 N ANISOU 1088 NH1 ARG A 136 20632 23992 17332 11802 897 2020 N ATOM 1089 NH2 ARG A 136 9.890-111.763 10.975 1.00165.53 N ANISOU 1089 NH2 ARG A 136 21863 23394 17637 12070 848 2958 N ATOM 1090 N ILE A 137 7.014-106.661 12.339 1.00133.34 N ANISOU 1090 N ILE A 137 16299 21925 12440 9755 949 1776 N ATOM 1091 CA ILE A 137 6.693-106.354 13.729 1.00131.45 C ANISOU 1091 CA ILE A 137 15857 21736 12351 9237 1188 1364 C ATOM 1092 C ILE A 137 6.001-105.005 13.843 1.00126.66 C ANISOU 1092 C ILE A 137 14943 21707 11476 8681 1172 1162 C ATOM 1093 O ILE A 137 4.974-104.884 14.507 1.00125.41 O ANISOU 1093 O ILE A 137 14329 21998 11323 8479 1215 762 O ATOM 1094 CB ILE A 137 7.952-106.329 14.615 1.00125.33 C ANISOU 1094 CB ILE A 137 15574 20215 11831 8892 1462 1480 C ATOM 1095 CG1 ILE A 137 8.554-107.727 14.739 1.00128.91 C ANISOU 1095 CG1 ILE A 137 16296 20061 12623 9384 1503 1581 C ATOM 1096 CG2 ILE A 137 7.609-105.814 15.998 1.00121.02 C ANISOU 1096 CG2 ILE A 137 14851 19778 11352 8315 1669 1084 C ATOM 1097 CD1 ILE A 137 9.835-107.750 15.539 1.00125.76 C ANISOU 1097 CD1 ILE A 137 16372 18900 12508 9061 1735 1693 C ATOM 1098 N ALA A 138 6.568-103.999 13.189 1.00123.47 N ANISOU 1098 N ALA A 138 14796 21275 10844 8436 1125 1440 N ATOM 1099 CA ALA A 138 6.024-102.646 13.229 1.00120.27 C ANISOU 1099 CA ALA A 138 14158 21342 10195 7904 1098 1267 C ATOM 1100 C ALA A 138 4.594-102.619 12.712 1.00123.81 C ANISOU 1100 C ALA A 138 14017 22563 10463 8085 844 992 C ATOM 1101 O ALA A 138 3.735-101.924 13.257 1.00128.49 O ANISOU 1101 O ALA A 138 14228 23579 11013 7653 881 656 O ATOM 1102 CB ALA A 138 6.895-101.701 12.431 1.00118.45 C ANISOU 1102 CB ALA A 138 14315 20952 9738 7733 1073 1618 C ATOM 1103 N ARG A 139 4.343-103.391 11.657 1.00131.52 N ANISOU 1103 N ARG A 139 14914 23705 11351 8724 578 1140 N ATOM 1104 CA ARG A 139 2.998-103.500 11.114 1.00135.78 C ANISOU 1104 CA ARG A 139 14853 24971 11764 8970 294 871 C ATOM 1105 C ARG A 139 2.066-104.148 12.123 1.00136.80 C ANISOU 1105 C ARG A 139 14492 25323 12164 8953 434 439 C ATOM 1106 O ARG A 139 0.923-103.724 12.272 1.00137.59 O ANISOU 1106 O ARG A 139 14041 26023 12215 8730 372 90 O ATOM 1107 CB ARG A 139 2.991-104.278 9.796 1.00141.90 C ANISOU 1107 CB ARG A 139 15677 25835 12404 9719 -50 1141 C ATOM 1108 CG ARG A 139 2.849-103.395 8.566 1.00143.33 C ANISOU 1108 CG ARG A 139 15881 26420 12159 9735 -362 1297 C ATOM 1109 CD ARG A 139 2.714-104.222 7.298 1.00150.16 C ANISOU 1109 CD ARG A 139 16762 27428 12863 10513 -745 1546 C ATOM 1110 NE ARG A 139 3.891-105.051 7.052 1.00151.38 N ANISOU 1110 NE ARG A 139 17518 26883 13115 10909 -643 2013 N ATOM 1111 CZ ARG A 139 4.949-104.654 6.353 1.00162.49 C ANISOU 1111 CZ ARG A 139 19516 27946 14275 10910 -615 2476 C ATOM 1112 NH1 ARG A 139 5.977-105.476 6.180 1.00179.85 N ANISOU 1112 NH1 ARG A 139 22232 29487 16617 11254 -499 2897 N ATOM 1113 NH2 ARG A 139 4.982-103.436 5.826 1.00148.98 N ANISOU 1113 NH2 ARG A 139 17881 26542 12183 10562 -686 2509 N ATOM 1114 N GLU A 140 2.550-105.174 12.818 1.00134.85 N ANISOU 1114 N GLU A 140 14442 24591 12205 9176 636 450 N ATOM 1115 CA GLU A 140 1.728-105.829 13.832 1.00136.09 C ANISOU 1115 CA GLU A 140 14177 24938 12594 9171 818 29 C ATOM 1116 C GLU A 140 1.379-104.882 14.977 1.00131.26 C ANISOU 1116 C GLU A 140 13426 24482 11964 8410 1087 -252 C ATOM 1117 O GLU A 140 0.237-104.848 15.440 1.00135.20 O ANISOU 1117 O GLU A 140 13380 25500 12489 8255 1151 -625 O ATOM 1118 CB GLU A 140 2.406-107.098 14.350 1.00137.56 C ANISOU 1118 CB GLU A 140 14667 24521 13080 9565 978 84 C ATOM 1119 CG GLU A 140 2.181-108.302 13.453 1.00183.86 C ANISOU 1119 CG GLU A 140 20408 30409 19043 10393 723 177 C ATOM 1120 CD GLU A 140 3.341-109.274 13.472 1.00218.75 C ANISOU 1120 CD GLU A 140 25392 34030 23694 10781 792 468 C ATOM 1121 OE1 GLU A 140 3.518-110.005 12.477 1.00246.55 O ANISOU 1121 OE1 GLU A 140 29021 37421 27234 11419 541 735 O ATOM 1122 OE2 GLU A 140 4.078-109.309 14.481 1.00203.52 O ANISOU 1122 OE2 GLU A 140 23803 31592 21935 10449 1081 432 O ATOM 1123 N TRP A 141 2.367-104.109 15.419 1.00125.88 N ANISOU 1123 N TRP A 141 13233 23347 11247 7940 1244 -60 N ATOM 1124 CA TRP A 141 2.176-103.151 16.501 1.00126.98 C ANISOU 1124 CA TRP A 141 13331 23553 11364 7220 1473 -268 C ATOM 1125 C TRP A 141 1.198-102.064 16.089 1.00121.13 C ANISOU 1125 C TRP A 141 12169 23445 10412 6873 1332 -424 C ATOM 1126 O TRP A 141 0.403-101.584 16.898 1.00120.04 O ANISOU 1126 O TRP A 141 11713 23617 10282 6418 1486 -718 O ATOM 1127 CB TRP A 141 3.506-102.512 16.910 1.00116.94 C ANISOU 1127 CB TRP A 141 12664 21653 10114 6844 1611 -3 C ATOM 1128 CG TRP A 141 4.285-103.295 17.922 1.00114.83 C ANISOU 1128 CG TRP A 141 12738 20796 10097 6878 1837 -12 C ATOM 1129 CD1 TRP A 141 4.449-104.649 17.966 1.00122.26 C ANISOU 1129 CD1 TRP A 141 13734 21483 11237 7415 1856 -29 C ATOM 1130 CD2 TRP A 141 5.000-102.767 19.047 1.00110.12 C ANISOU 1130 CD2 TRP A 141 12475 19780 9584 6357 2048 -28 C ATOM 1131 NE1 TRP A 141 5.229-104.995 19.045 1.00116.25 N ANISOU 1131 NE1 TRP A 141 13326 20169 10673 7247 2069 -72 N ATOM 1132 CE2 TRP A 141 5.578-103.857 19.722 1.00111.17 C ANISOU 1132 CE2 TRP A 141 12854 19428 9956 6603 2178 -68 C ATOM 1133 CE3 TRP A 141 5.209-101.475 19.544 1.00117.79 C ANISOU 1133 CE3 TRP A 141 13563 20729 10465 5724 2118 -21 C ATOM 1134 CZ2 TRP A 141 6.352-103.697 20.869 1.00121.42 C ANISOU 1134 CZ2 TRP A 141 14501 20248 11385 6229 2354 -109 C ATOM 1135 CZ3 TRP A 141 5.978-101.319 20.681 1.00147.00 C ANISOU 1135 CZ3 TRP A 141 17603 23947 14302 5372 2293 -40 C ATOM 1136 CH2 TRP A 141 6.539-102.425 21.332 1.00125.94 C ANISOU 1136 CH2 TRP A 141 15168 20828 11854 5622 2400 -87 C ATOM 1137 N THR A 142 1.273-101.673 14.823 1.00122.60 N ANISOU 1137 N THR A 142 12375 23808 10400 7079 1039 -222 N ATOM 1138 CA THR A 142 0.335-100.701 14.290 1.00123.35 C ANISOU 1138 CA THR A 142 12061 24508 10298 6809 846 -394 C ATOM 1139 C THR A 142 -1.066-101.296 14.342 1.00128.18 C ANISOU 1139 C THR A 142 11971 25728 11004 7002 779 -760 C ATOM 1140 O THR A 142 -1.995-100.671 14.849 1.00127.81 O ANISOU 1140 O THR A 142 11511 26085 10967 6539 863 -1060 O ATOM 1141 CB THR A 142 0.698-100.303 12.849 1.00124.95 C ANISOU 1141 CB THR A 142 12444 24798 10233 7086 514 -118 C ATOM 1142 OG1 THR A 142 2.051 -99.832 12.811 1.00120.93 O ANISOU 1142 OG1 THR A 142 12577 23709 9663 6931 631 230 O ATOM 1143 CG2 THR A 142 -0.227 -99.211 12.344 1.00125.63 C ANISOU 1143 CG2 THR A 142 12139 25481 10116 6757 301 -336 C ATOM 1144 N GLN A 143 -1.190-102.523 13.837 1.00133.00 N ANISOU 1144 N GLN A 143 12450 26373 11710 7688 643 -728 N ATOM 1145 CA GLN A 143 -2.448-103.268 13.824 1.00138.43 C ANISOU 1145 CA GLN A 143 12450 27612 12535 7987 576 -1072 C ATOM 1146 C GLN A 143 -3.083-103.372 15.203 1.00137.41 C ANISOU 1146 C GLN A 143 12026 27595 12587 7582 964 -1421 C ATOM 1147 O GLN A 143 -4.308-103.336 15.338 1.00140.56 O ANISOU 1147 O GLN A 143 11778 28579 13050 7466 977 -1761 O ATOM 1148 CB GLN A 143 -2.216-104.677 13.279 1.00169.76 C ANISOU 1148 CB GLN A 143 16457 31409 16634 8813 430 -947 C ATOM 1149 CG GLN A 143 -2.374-104.811 11.776 1.00167.33 C ANISOU 1149 CG GLN A 143 16045 31379 16153 9357 -44 -767 C ATOM 1150 CD GLN A 143 -3.785-105.203 11.378 1.00199.60 C ANISOU 1150 CD GLN A 143 19320 36194 20326 9644 -275 -1125 C ATOM 1151 OE1 GLN A 143 -4.622-105.501 12.230 1.00189.98 O ANISOU 1151 OE1 GLN A 143 17610 35249 19326 9482 -35 -1500 O ATOM 1152 NE2 GLN A 143 -4.054-105.204 10.077 1.00209.06 N ANISOU 1152 NE2 GLN A 143 20367 37720 21346 10076 -742 -1015 N ATOM 1153 N LYS A 144 -2.248-103.514 16.225 1.00136.61 N ANISOU 1153 N LYS A 144 12400 26938 12567 7368 1280 -1338 N ATOM 1154 CA LYS A 144 -2.746-103.652 17.586 1.00132.61 C ANISOU 1154 CA LYS A 144 11714 26496 12177 7001 1661 -1640 C ATOM 1155 C LYS A 144 -3.085-102.304 18.212 1.00128.67 C ANISOU 1155 C LYS A 144 11170 26159 11558 6195 1804 -1731 C ATOM 1156 O LYS A 144 -4.249-101.998 18.470 1.00130.81 O ANISOU 1156 O LYS A 144 10891 26968 11842 5909 1886 -2021 O ATOM 1157 CB LYS A 144 -1.738-104.410 18.459 1.00130.60 C ANISOU 1157 CB LYS A 144 11989 25584 12047 7125 1908 -1548 C ATOM 1158 CG LYS A 144 -1.537-105.861 18.037 1.00175.71 C ANISOU 1158 CG LYS A 144 17704 31119 17938 7913 1821 -1527 C ATOM 1159 CD LYS A 144 -0.568-106.596 18.951 1.00169.00 C ANISOU 1159 CD LYS A 144 17370 29605 17237 7997 2060 -1485 C ATOM 1160 CE LYS A 144 -0.506-108.073 18.589 1.00192.29 C ANISOU 1160 CE LYS A 144 20271 32388 20400 8783 1987 -1521 C ATOM 1161 NZ LYS A 144 0.467-108.826 19.430 1.00183.61 N ANISOU 1161 NZ LYS A 144 19688 30605 19471 8884 2191 -1504 N ATOM 1162 N TYR A 145 -2.059-101.496 18.444 1.00123.25 N ANISOU 1162 N TYR A 145 11056 24992 10781 5832 1835 -1479 N ATOM 1163 CA TYR A 145 -2.209-100.284 19.242 1.00121.23 C ANISOU 1163 CA TYR A 145 10866 24749 10447 5077 2003 -1543 C ATOM 1164 C TYR A 145 -2.773 -99.053 18.520 1.00118.91 C ANISOU 1164 C TYR A 145 10322 24840 10019 4722 1785 -1568 C ATOM 1165 O TYR A 145 -3.554 -98.298 19.098 1.00118.46 O ANISOU 1165 O TYR A 145 9996 25060 9953 4176 1914 -1763 O ATOM 1166 CB TYR A 145 -0.885 -99.973 19.939 1.00113.92 C ANISOU 1166 CB TYR A 145 10628 23130 9526 4838 2139 -1305 C ATOM 1167 CG TYR A 145 -0.268-101.215 20.546 1.00114.68 C ANISOU 1167 CG TYR A 145 10991 22814 9768 5218 2303 -1295 C ATOM 1168 CD1 TYR A 145 -0.792-101.779 21.700 1.00138.79 C ANISOU 1168 CD1 TYR A 145 13898 25957 12880 5116 2594 -1566 C ATOM 1169 CD2 TYR A 145 0.822-101.834 19.951 1.00133.52 C ANISOU 1169 CD2 TYR A 145 13781 24721 12230 5682 2174 -1023 C ATOM 1170 CE1 TYR A 145 -0.240-102.920 22.254 1.00117.70 C ANISOU 1170 CE1 TYR A 145 11478 22906 10336 5475 2730 -1601 C ATOM 1171 CE2 TYR A 145 1.380-102.973 20.494 1.00145.27 C ANISOU 1171 CE2 TYR A 145 15512 25798 13884 6023 2308 -1038 C ATOM 1172 CZ TYR A 145 0.847-103.511 21.644 1.00128.88 C ANISOU 1172 CZ TYR A 145 13286 23820 11863 5925 2573 -1345 C ATOM 1173 OH TYR A 145 1.406-104.644 22.182 1.00131.83 O ANISOU 1173 OH TYR A 145 13916 23776 12396 6273 2693 -1399 O ATOM 1174 N ALA A 146 -2.384 -98.853 17.265 1.00136.13 N ANISOU 1174 N ALA A 146 12607 27031 12086 5027 1457 -1373 N ATOM 1175 CA ALA A 146 -2.749 -97.630 16.546 1.00135.65 C ANISOU 1175 CA ALA A 146 12407 27266 11869 4699 1228 -1396 C ATOM 1176 C ALA A 146 -4.077 -97.687 15.791 1.00141.06 C ANISOU 1176 C ALA A 146 12391 28661 12544 4835 987 -1669 C ATOM 1177 O ALA A 146 -4.570 -96.658 15.335 1.00157.35 O ANISOU 1177 O ALA A 146 14259 31019 14507 4491 811 -1774 O ATOM 1178 CB ALA A 146 -1.630 -97.227 15.595 1.00133.63 C ANISOU 1178 CB ALA A 146 12657 26675 11443 4895 1013 -1059 C ATOM 1179 N MET A 147 -4.641 -98.880 15.639 1.00137.78 N ANISOU 1179 N MET A 147 11587 28512 12251 5345 962 -1801 N ATOM 1180 CA MET A 147 -5.842 -99.050 14.817 1.00135.06 C ANISOU 1180 CA MET A 147 10545 28844 11929 5569 682 -2055 C ATOM 1181 C MET A 147 -7.179 -99.103 15.564 1.00138.04 C ANISOU 1181 C MET A 147 10236 29713 12499 5231 903 -2450 C ATOM 1182 O MET A 147 -8.221 -99.337 14.952 1.00143.45 O ANISOU 1182 O MET A 147 10266 30974 13264 5421 690 -2696 O ATOM 1183 CB MET A 147 -5.680-100.241 13.871 1.00139.58 C ANISOU 1183 CB MET A 147 11057 29469 12508 6416 409 -1944 C ATOM 1184 CG MET A 147 -4.440-100.124 12.999 1.00137.53 C ANISOU 1184 CG MET A 147 11450 28775 12030 6730 184 -1530 C ATOM 1185 SD MET A 147 -4.756-100.249 11.237 1.00143.27 S ANISOU 1185 SD MET A 147 11960 29939 12536 7334 -407 -1454 S ATOM 1186 CE MET A 147 -5.142-101.989 11.080 1.00182.28 C ANISOU 1186 CE MET A 147 16555 34989 17712 8165 -478 -1513 C TER 3227 LYS A1271 CONECT 176 849 CONECT 849 176 CONECT 3403 4076 CONECT 4076 3403 CONECT 6630 7303 CONECT 7303 6630 CONECT1346914142 CONECT1414213469 CONECT1669617369 CONECT1736916696 CONECT1992320596 CONECT2059619923 MASTER 838 0 0 132 120 0 0 626568 18 12 258 END A second structure was input as follows:HEADER LIGASE 17-DEC-15 5FER TITLE COMPLEX OF TRIM25 RING WITH UBCH5-UB COMPND MOL_ID: 1; COMPND 2 MOLECULE: E3 UBIQUITIN/ISG15 LIGASE TRIM25; COMPND 3 CHAIN: A, D; COMPND 4 SYNONYM: ESTROGEN-RESPONSIVE FINGER PROTEIN,RING FINGER PROTEIN 147, COMPND 5 RING-TYPE E3 UBIQUITIN TRANSFERASE,TRIPARTITE MOTIF-CONTAINING COMPND 6 PROTEIN 25,UBIQUITIN/ISG15-CONJUGATING ENZYME TRIM25,ZINC FINGER COMPND 7 PROTEIN 147; COMPND 8 EC: 6.3.2.-,2.3.2.27; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D1; COMPND 12 CHAIN: B, E; COMPND 13 SYNONYM: (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME D1,E2 COMPND 14 UBIQUITIN-CONJUGATING ENZYME D1,STIMULATOR OF FE TRANSPORT,SFT,UBC4/5 COMPND 15 HOMOLOG,UBCH5,UBIQUITIN CARRIER PROTEIN D1,UBIQUITIN-CONJUGATING COMPND 16 ENZYME E2(17)KB 1,UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 1,UBIQUITIN- COMPND 17 PROTEIN LIGASE D1; COMPND 18 EC: 2.3.2.23,2.3.2.24; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 3; COMPND 21 MOLECULE: UBIQUITIN-40S RIBOSOMAL PROTEIN S27A; COMPND 22 CHAIN: C, F; COMPND 23 SYNONYM: UBIQUITIN CARBOXYL EXTENSION PROTEIN 80 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: TRIM25, EFP, RNF147, ZNF147; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: UBE2D1, SFT, UBC5A, UBCH5, UBCH5A; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 17 ORGANISM_COMMON: BOVINE; SOURCE 18 ORGANISM_TAXID: 9913 KEYWDS E3 LIGASE, UBIQUITIN, LIGASE EXPDTA X-RAY DIFFRACTION AUTHOR K.RITTINGER,M.G.KOLIOPOULOS,D.ESPOSITO REVDAT 4 20-FEB-19 5FER 1 REMARK LINK REVDAT 3 13-SEP-17 5FER 1 REMARK REVDAT 2 15-JUN-16 5FER 1 JRNL REVDAT 1 18-MAY-16 5FER 0 JRNL AUTH M.G.KOLIOPOULOS,D.ESPOSITO,E.CHRISTODOULOU,I.A.TAYLOR, JRNL AUTH 2 K.RITTINGER JRNL TITL FUNCTIONAL ROLE OF TRIM E3 LIGASE OLIGOMERIZATION AND JRNL TITL 2 REGULATION OF CATALYTIC ACTIVITY. JRNL REF EMBO J. V. 35 1204 2016 JRNL REFN ESSN 1460-2075 JRNL PMID 27154206 JRNL DOI 10.15252/EMBJ.201593741 REMARK 2 REMARK 2 RESOLUTION. 2.34 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.30 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 30000 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.229 REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.273 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890 REMARK 3 FREE R VALUE TEST SET COUNT : 1468 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 30.2978 - 5.0345 1.00 3046 161 0.1790 0.2272 REMARK 3 2 5.0345 - 3.9989 1.00 2915 151 0.1770 0.2143 REMARK 3 3 3.9989 - 3.4943 1.00 2883 147 0.2091 0.2672 REMARK 3 4 3.4943 - 3.1752 1.00 2869 145 0.2459 0.3070 REMARK 3 5 3.1752 - 2.9478 0.99 2821 163 0.2688 0.3163 REMARK 3 6 2.9478 - 2.7741 0.99 2807 131 0.2911 0.3022 REMARK 3 7 2.7741 - 2.6353 0.99 2811 136 0.3087 0.3684 REMARK 3 8 2.6353 - 2.5206 0.99 2789 167 0.3365 0.4033 REMARK 3 9 2.5206 - 2.4236 0.99 2786 134 0.3428 0.3737 REMARK 3 10 2.4236 - 2.3400 0.99 2805 133 0.3685 0.3674 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.820 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) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 4879 REMARK 3 ANGLE : 0.539 6630 REMARK 3 CHIRALITY : 0.041 740 REMARK 3 PLANARITY : 0.006 862 REMARK 3 DIHEDRAL : 12.639 2990 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 5FER COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-15. REMARK 100 THE DEPOSITION ID IS D_1000216462. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-MAY-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.2829 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 : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30000 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340 REMARK 200 RESOLUTION RANGE LOW (A) : 30.280 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 12.80 REMARK 200 R MERGE (I) : 0.13900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.7500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.91800 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: SAD REMARK 200 SOFTWARE USED: AUTOSOL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 20000 AND 100 MM TRIS PH 8.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 30.24000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.21500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.85000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.21500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.24000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.85000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5630 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 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 -2 REMARK 465 PRO A -1 REMARK 465 GLY A 0 REMARK 465 ASP A 80 REMARK 465 LEU A 81 REMARK 465 ALA A 82 REMARK 465 GLY B -2 REMARK 465 PRO B -1 REMARK 465 GLY B 0 REMARK 465 ALA B 146 REMARK 465 MET B 147 REMARK 465 GLY D -2 REMARK 465 PRO D -1 REMARK 465 GLY D 0 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 GLY E -2 REMARK 465 PRO E -1 REMARK 465 GLY E 0 REMARK 465 MET E 147 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 NZ LYS B 85 O GLY C 76 1.27 REMARK 500 NZ LYS E 85 O GLY F 76 1.41 REMARK 500 CE LYS E 85 O GLY F 76 1.56 REMARK 500 OH TYR E 134 O HOH E 201 2.02 REMARK 500 O TYR E 74 O HOH E 201 2.03 REMARK 500 OH TYR E 45 O HOH E 201 2.05 REMARK 500 CE LYS B 85 O GLY C 76 2.15 REMARK 500 OD2 ASP B 87 O HOH B 201 2.19 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 GLU A 3 21.08 -76.50 REMARK 500 SER A 46 -136.50 61.70 REMARK 500 PRO B 17 77.30 21.11 REMARK 500 ARG B 90 -108.86 -137.17 REMARK 500 ASP B 130 81.07 -158.87 REMARK 500 VAL C 17 -169.68 -129.61 REMARK 500 GLN C 62 -169.60 -114.67 REMARK 500 SER D 46 -149.58 58.75 REMARK 500 ARG E 90 -98.16 -139.33 REMARK 500 ASP E 130 82.69 -159.18 REMARK 500 VAL F 17 -168.17 -129.30 REMARK 500 GLN F 62 -155.09 -115.57 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 101 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 13 SG REMARK 620 2 CYS A 16 SG 99.7 REMARK 620 3 CYS A 33 SG 107.8 97.5 REMARK 620 4 CYS A 36 SG 120.3 105.6 120.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 102 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 28 SG REMARK 620 2 HIS A 30 ND1 114.7 REMARK 620 3 CYS A 50 SG 101.4 112.4 REMARK 620 4 CYS A 53 SG 109.4 108.1 110.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN D 102 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS D 13 SG REMARK 620 2 CYS D 16 SG 112.6 REMARK 620 3 CYS D 33 SG 103.2 106.2 REMARK 620 4 CYS D 36 SG 113.7 108.9 111.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN D 101 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS D 28 SG REMARK 620 2 HIS D 30 ND1 112.5 REMARK 620 3 CYS D 50 SG 102.7 109.8 REMARK 620 4 CYS D 53 SG 110.2 109.1 112.5 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY F 76 and LYS E REMARK 800 85 DBREF 5FER A 1 82 UNP Q14258 TRI25_HUMAN 1 82 DBREF 5FER B 1 147 UNP P51668 UB2D1_HUMAN 1 147 DBREF 5FER C 1 76 UNP P62992 RS27A_BOVIN 1 76 DBREF 5FER D 1 82 UNP Q14258 TRI25_HUMAN 1 82 DBREF 5FER E 1 147 UNP P51668 UB2D1_HUMAN 1 147 DBREF 5FER F 1 76 UNP P62992 RS27A_BOVIN 1 76 SEQADV 5FER GLY A -2 UNP Q14258 EXPRESSION TAG SEQADV 5FER PRO A -1 UNP Q14258 EXPRESSION TAG SEQADV 5FER GLY A 0 UNP Q14258 EXPRESSION TAG SEQADV 5FER GLY B -2 UNP P51668 EXPRESSION TAG SEQADV 5FER PRO B -1 UNP P51668 EXPRESSION TAG SEQADV 5FER GLY B 0 UNP P51668 EXPRESSION TAG SEQADV 5FER ARG B 22 UNP P51668 SER 22 ENGINEERED MUTATION SEQADV 5FER LYS B 85 UNP P51668 CYS 85 ENGINEERED MUTATION SEQADV 5FER GLY D -2 UNP Q14258 EXPRESSION TAG SEQADV 5FER PRO D -1 UNP Q14258 EXPRESSION TAG SEQADV 5FER GLY D 0 UNP Q14258 EXPRESSION TAG SEQADV 5FER GLY E -2 UNP P51668 EXPRESSION TAG SEQADV 5FER PRO E -1 UNP P51668 EXPRESSION TAG SEQADV 5FER GLY E 0 UNP P51668 EXPRESSION TAG SEQADV 5FER ARG E 22 UNP P51668 SER 22 ENGINEERED MUTATION SEQADV 5FER LYS E 85 UNP P51668 CYS 85 ENGINEERED MUTATION SEQRES 1 A 85 GLY PRO GLY MET ALA GLU LEU CYS PRO LEU ALA GLU GLU SEQRES 2 A 85 LEU SER CYS SER ILE CYS LEU GLU PRO PHE LYS GLU PRO SEQRES 3 A 85 VAL THR THR PRO CYS GLY HIS ASN PHE CYS GLY SER CYS SEQRES 4 A 85 LEU ASN GLU THR TRP ALA VAL GLN GLY SER PRO TYR LEU SEQRES 5 A 85 CYS PRO GLN CYS ARG ALA VAL TYR GLN ALA ARG PRO GLN SEQRES 6 A 85 LEU HIS LYS ASN THR VAL LEU CYS ASN VAL VAL GLU GLN SEQRES 7 A 85 PHE LEU GLN ALA ASP LEU ALA SEQRES 1 B 150 GLY PRO GLY MET ALA LEU LYS ARG ILE GLN LYS GLU LEU SEQRES 2 B 150 SER ASP LEU GLN ARG ASP PRO PRO ALA HIS CYS ARG ALA SEQRES 3 B 150 GLY PRO VAL GLY ASP ASP LEU PHE HIS TRP GLN ALA THR SEQRES 4 B 150 ILE MET GLY PRO PRO ASP SER ALA TYR GLN GLY GLY VAL SEQRES 5 B 150 PHE PHE LEU THR VAL HIS PHE PRO THR ASP TYR PRO PHE SEQRES 6 B 150 LYS PRO PRO LYS ILE ALA PHE THR THR LYS ILE TYR HIS SEQRES 7 B 150 PRO ASN ILE ASN SER ASN GLY SER ILE LYS LEU ASP ILE SEQRES 8 B 150 LEU ARG SER GLN TRP SER PRO ALA LEU THR VAL SER LYS SEQRES 9 B 150 VAL LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN SEQRES 10 B 150 PRO ASP ASP PRO LEU VAL PRO ASP ILE ALA GLN ILE TYR SEQRES 11 B 150 LYS SER ASP LYS GLU LYS TYR ASN ARG HIS ALA ARG GLU SEQRES 12 B 150 TRP THR GLN LYS TYR ALA MET SEQRES 1 C 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 C 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 C 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 C 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 C 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 C 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 1 D 85 GLY PRO GLY MET ALA GLU LEU CYS PRO LEU ALA GLU GLU SEQRES 2 D 85 LEU SER CYS SER ILE CYS LEU GLU PRO PHE LYS GLU PRO SEQRES 3 D 85 VAL THR THR PRO CYS GLY HIS ASN PHE CYS GLY SER CYS SEQRES 4 D 85 LEU ASN GLU THR TRP ALA VAL GLN GLY SER PRO TYR LEU SEQRES 5 D 85 CYS PRO GLN CYS ARG ALA VAL TYR GLN ALA ARG PRO GLN SEQRES 6 D 85 LEU HIS LYS ASN THR VAL LEU CYS ASN VAL VAL GLU GLN SEQRES 7 D 85 PHE LEU GLN ALA ASP LEU ALA SEQRES 1 E 150 GLY PRO GLY MET ALA LEU LYS ARG ILE GLN LYS GLU LEU SEQRES 2 E 150 SER ASP LEU GLN ARG ASP PRO PRO ALA HIS CYS ARG ALA SEQRES 3 E 150 GLY PRO VAL GLY ASP ASP LEU PHE HIS TRP GLN ALA THR SEQRES 4 E 150 ILE MET GLY PRO PRO ASP SER ALA TYR GLN GLY GLY VAL SEQRES 5 E 150 PHE PHE LEU THR VAL HIS PHE PRO THR ASP TYR PRO PHE SEQRES 6 E 150 LYS PRO PRO LYS ILE ALA PHE THR THR LYS ILE TYR HIS SEQRES 7 E 150 PRO ASN ILE ASN SER ASN GLY SER ILE LYS LEU ASP ILE SEQRES 8 E 150 LEU ARG SER GLN TRP SER PRO ALA LEU THR VAL SER LYS SEQRES 9 E 150 VAL LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN SEQRES 10 E 150 PRO ASP ASP PRO LEU VAL PRO ASP ILE ALA GLN ILE TYR SEQRES 11 E 150 LYS SER ASP LYS GLU LYS TYR ASN ARG HIS ALA ARG GLU SEQRES 12 E 150 TRP THR GLN LYS TYR ALA MET SEQRES 1 F 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 F 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 F 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 F 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 F 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 F 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY HET ZN A 101 1 HET ZN A 102 1 HET ZN D 101 1 HET ZN D 102 1 HETNAM ZN ZINC ION FORMUL 7 ZN 4(ZN 2+) FORMUL 11 HOH *68(H2 O) HELIX 1 AA1 PRO A 6 LEU A 11 1 6 HELIX 2 AA2 GLY A 34 GLN A 44 1 11 HELIX 3 AA3 ASN A 66 ALA A 79 1 14 HELIX 4 AA4 ALA B 2 ASP B 16 1 15 HELIX 5 AA5 LEU B 86 ARG B 90 5 5 HELIX 6 AA6 THR B 98 CYS B 111 1 14 HELIX 7 AA7 VAL B 120 ASP B 130 1 11 HELIX 8 AA8 ASP B 130 TYR B 145 1 16 HELIX 9 AA9 THR C 22 GLY C 35 1 14 HELIX 10 AB1 PRO C 37 ASP C 39 5 3 HELIX 11 AB2 LEU C 56 ASN C 60 5 5 HELIX 12 AB3 LEU D 4 LEU D 11 1 8 HELIX 13 AB4 GLY D 34 VAL D 43 1 10 HELIX 14 AB5 ASN D 66 ALA D 82 1 17 HELIX 15 AB6 ALA E 2 ASP E 16 1 15 HELIX 16 AB7 LEU E 86 ARG E 90 5 5 HELIX 17 AB8 THR E 98 CYS E 111 1 14 HELIX 18 AB9 VAL E 120 ASP E 130 1 11 HELIX 19 AC1 ASP E 130 TYR E 145 1 16 HELIX 20 AC2 THR F 22 GLY F 35 1 14 HELIX 21 AC3 PRO F 37 ASP F 39 5 3 SHEET 1 AA1 2 PRO A 23 THR A 25 0 SHEET 2 AA1 2 ASN A 31 CYS A 33 -1 O PHE A 32 N VAL A 24 SHEET 1 AA2 2 TYR A 48 LEU A 49 0 SHEET 2 AA2 2 VAL A 56 TYR A 57 -1 O TYR A 57 N TYR A 48 SHEET 1 AA3 4 CYS B 21 GLY B 24 0 SHEET 2 AA3 4 HIS B 32 MET B 38 -1 O THR B 36 N ARG B 22 SHEET 3 AA3 4 VAL B 49 HIS B 55 -1 O VAL B 54 N TRP B 33 SHEET 4 AA3 4 LYS B 66 PHE B 69 -1 O LYS B 66 N HIS B 55 SHEET 1 AA4 5 THR C 12 GLU C 16 0 SHEET 2 AA4 5 GLN C 2 LYS C 6 -1 N ILE C 3 O LEU C 15 SHEET 3 AA4 5 THR C 66 LEU C 71 1 O LEU C 67 N PHE C 4 SHEET 4 AA4 5 GLN C 41 PHE C 45 -1 N ILE C 44 O HIS C 68 SHEET 5 AA4 5 LYS C 48 GLN C 49 -1 O LYS C 48 N PHE C 45 SHEET 1 AA5 2 PRO D 23 THR D 25 0 SHEET 2 AA5 2 ASN D 31 CYS D 33 -1 O PHE D 32 N VAL D 24 SHEET 1 AA6 2 TYR D 48 LEU D 49 0 SHEET 2 AA6 2 VAL D 56 TYR D 57 -1 O TYR D 57 N TYR D 48 SHEET 1 AA7 4 CYS E 21 PRO E 25 0 SHEET 2 AA7 4 HIS E 32 MET E 38 -1 O GLN E 34 N GLY E 24 SHEET 3 AA7 4 VAL E 49 HIS E 55 -1 O VAL E 54 N TRP E 33 SHEET 4 AA7 4 LYS E 66 PHE E 69 -1 O ALA E 68 N THR E 53 SHEET 1 AA8 5 THR F 12 GLU F 16 0 SHEET 2 AA8 5 GLN F 2 LYS F 6 -1 N ILE F 3 O LEU F 15 SHEET 3 AA8 5 THR F 66 LEU F 71 1 O LEU F 67 N LYS F 6 SHEET 4 AA8 5 GLN F 41 PHE F 45 -1 N ILE F 44 O HIS F 68 SHEET 5 AA8 5 LYS F 48 GLN F 49 -1 O LYS F 48 N PHE F 45 LINK SG CYS A 13 ZN L ZN A 101 1555 1555 2.48 LINK SG CYS A 16 ZN L ZN A 101 1555 1555 2.33 LINK SG CYS A 28 ZN L ZN A 102 1555 1555 2.27 LINK ND1 HIS A 30 ZN L ZN A 102 1555 1555 2.07 LINK SG CYS A 33 ZN L ZN A 101 1555 1555 2.35 LINK SG CYS A 36 ZN L ZN A 101 1555 1555 2.35 LINK SG CYS A 50 ZN L ZN A 102 1555 1555 2.35 LINK SG CYS A 53 ZN L ZN A 102 1555 1555 2.33 LINK SG CYS D 13 ZN L ZN D 102 1555 1555 2.41 LINK SG CYS D 16 ZN L ZN D 102 1555 1555 2.33 LINK SG CYS D 28 ZN L ZN D 101 1555 1555 2.28 LINK ND1 HIS D 30 ZN L ZN D 101 1555 1555 2.06 LINK SG CYS D 33 ZN L ZN D 102 1555 1555 2.31 LINK SG CYS D 36 ZN L ZN D 102 1555 1555 2.34 LINK SG CYS D 50 ZN L ZN D 101 1555 1555 2.38 LINK SG CYS D 53 ZN L ZN D 101 1555 1555 2.27 CISPEP 1 TYR B 60 PRO B 61 0 3.01 CISPEP 2 TYR E 60 PRO E 61 0 1.00 SITE 1 AC1 5 CYS A 13 CYS A 16 LYS A 21 CYS A 33 SITE 2 AC1 5 CYS A 36 SITE 1 AC2 4 CYS A 28 HIS A 30 CYS A 50 CYS A 53 SITE 1 AC3 4 CYS D 28 HIS D 30 CYS D 50 CYS D 53 SITE 1 AC4 4 CYS D 13 CYS D 16 CYS D 33 CYS D 36 SITE 1 AC5 13 HIS E 75 ASN E 77 ILE E 78 ILE E 84 SITE 2 AC5 13 LEU E 86 ASP E 117 PRO E 118 LEU E 119 SITE 3 AC5 13 VAL E 120 ILE E 123 TYR E 134 ARG F 74 SITE 4 AC5 13 GLY F 75 CRYST1 60.480 71.700 160.430 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.016534 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013947 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006233 0.00000 ATOM 2992 N MET E 1 7.237 -64.918 27.585 1.00 58.60 N ATOM 2993 CA MET E 1 5.950 -65.249 28.182 1.00 74.77 C ATOM 2994 C MET E 1 5.206 -66.254 27.299 1.00 66.04 C ATOM 2995 O MET E 1 5.283 -66.192 26.073 1.00 58.79 O ATOM 2996 CB MET E 1 5.123 -63.980 28.397 1.00 73.76 C ATOM 2997 CG MET E 1 4.107 -64.071 29.523 1.00 75.41 C ATOM 2998 SD MET E 1 4.299 -62.718 30.698 1.00 83.33 S ATOM 2999 CE MET E 1 4.342 -61.315 29.586 1.00 75.54 C ATOM 3000 N ALA E 2 4.473 -67.168 27.940 1.00 60.02 N ATOM 3001 CA ALA E 2 4.046 -68.389 27.266 1.00 56.04 C ATOM 3002 C ALA E 2 2.879 -68.161 26.309 1.00 58.57 C ATOM 3003 O ALA E 2 2.850 -68.749 25.222 1.00 56.07 O ATOM 3004 CB ALA E 2 3.672 -69.450 28.301 1.00 51.18 C ATOM 3005 N LEU E 3 1.909 -67.327 26.693 1.00 57.90 N ATOM 3006 CA LEU E 3 0.659 -67.256 25.939 1.00 57.36 C ATOM 3007 C LEU E 3 0.882 -66.761 24.514 1.00 58.12 C ATOM 3008 O LEU E 3 0.238 -67.247 23.575 1.00 56.57 O ATOM 3009 CB LEU E 3 -0.344 -66.363 26.668 1.00 61.48 C ATOM 3010 CG LEU E 3 -1.703 -66.178 25.983 1.00 59.18 C ATOM 3011 CD1 LEU E 3 -2.383 -67.520 25.749 1.00 57.16 C ATOM 3012 CD2 LEU E 3 -2.599 -65.249 26.790 1.00 62.38 C ATOM 3013 N LYS E 4 1.793 -65.799 24.329 1.00 53.95 N ATOM 3014 CA LYS E 4 2.024 -65.242 22.997 1.00 56.54 C ATOM 3015 C LYS E 4 2.574 -66.298 22.045 1.00 54.40 C ATOM 3016 O LYS E 4 2.135 -66.394 20.892 1.00 52.56 O ATOM 3017 CB LYS E 4 2.979 -64.051 23.075 1.00 57.10 C ATOM 3018 CG LYS E 4 2.329 -62.723 23.468 1.00 62.75 C ATOM 3019 CD LYS E 4 1.837 -62.746 24.907 1.00 78.09 C ATOM 3020 CE LYS E 4 2.950 -63.175 25.847 1.00 69.13 C ATOM 3021 NZ LYS E 4 2.444 -63.911 27.040 1.00 59.76 N1+ ATOM 3022 N ARG E 5 3.542 -67.093 22.511 1.00 51.06 N ATOM 3023 CA ARG E 5 4.080 -68.171 21.691 1.00 51.69 C ATOM 3024 C ARG E 5 2.996 -69.175 21.319 1.00 51.05 C ATOM 3025 O ARG E 5 2.947 -69.655 20.179 1.00 50.20 O ATOM 3026 CB ARG E 5 5.228 -68.859 22.431 1.00 50.33 C ATOM 3027 CG ARG E 5 5.612 -70.232 21.904 1.00 52.39 C ATOM 3028 CD ARG E 5 6.304 -70.164 20.558 1.00 45.66 C ATOM 3029 NE ARG E 5 6.678 -71.499 20.092 1.00 56.36 N ATOM 3030 CZ ARG E 5 7.878 -72.041 20.270 1.00 48.06 C ATOM 3031 NH1 ARG E 5 8.832 -71.363 20.893 1.00 44.57 N1+ ATOM 3032 NH2 ARG E 5 8.125 -73.261 19.814 1.00 56.90 N ATOM 3033 N ILE E 6 2.102 -69.488 22.261 1.00 52.55 N ATOM 3034 CA ILE E 6 1.010 -70.412 21.983 1.00 49.20 C ATOM 3035 C ILE E 6 0.063 -69.825 20.942 1.00 52.37 C ATOM 3036 O ILE E 6 -0.416 -70.532 20.047 1.00 51.20 O ATOM 3037 CB ILE E 6 0.274 -70.770 23.288 1.00 53.70 C ATOM 3038 CG1 ILE E 6 1.223 -71.470 24.259 1.00 52.72 C ATOM 3039 CG2 ILE E 6 -0.936 -71.642 23.005 1.00 49.99 C ATOM 3040 CD1 ILE E 6 0.609 -71.761 25.606 1.00 56.39 C ATOM 3041 N GLN E 7 -0.219 -68.524 21.044 1.00 58.04 N ATOM 3042 CA GLN E 7 -1.124 -67.877 20.099 1.00 55.60 C ATOM 3043 C GLN E 7 -0.574 -67.933 18.680 1.00 47.84 C ATOM 3044 O GLN E 7 -1.301 -68.254 17.731 1.00 48.86 O ATOM 3045 CB GLN E 7 -1.372 -66.427 20.520 1.00 53.80 C ATOM 3046 CG GLN E 7 -2.176 -66.265 21.803 1.00 61.95 C ATOM 3047 CD GLN E 7 -2.084 -64.863 22.380 1.00 69.13 C ATOM 3048 OE1 GLN E 7 -1.225 -64.070 21.985 1.00 71.69 O ATOM 3049 NE2 GLN E 7 -2.966 -64.548 23.322 1.00 68.31 N ATOM 3050 N LYS E 8 0.714 -67.622 18.515 1.00 44.50 N ATOM 3051 CA LYS E 8 1.289 -67.594 17.175 1.00 46.50 C ATOM 3052 C LYS E 8 1.378 -68.993 16.577 1.00 56.58 C ATOM 3053 O LYS E 8 1.138 -69.172 15.377 1.00 56.54 O ATOM 3054 CB LYS E 8 2.663 -66.928 17.199 1.00 51.71 C ATOM 3055 CG LYS E 8 3.192 -66.629 15.812 1.00 56.29 C ATOM 3056 CD LYS E 8 4.297 -65.597 15.841 1.00 61.70 C ATOM 3057 CE LYS E 8 4.433 -64.930 14.480 1.00 68.42 C ATOM 3058 NZ LYS E 8 4.517 -65.935 13.383 1.00 71.84 N1+ ATOM 3059 N GLU E 9 1.721 -69.992 17.395 1.00 55.07 N ATOM 3060 CA GLU E 9 1.711 -71.368 16.904 1.00 51.67 C ATOM 3061 C GLU E 9 0.325 -71.760 16.408 1.00 54.03 C ATOM 3062 O GLU E 9 0.189 -72.409 15.365 1.00 54.35 O ATOM 3063 CB GLU E 9 2.174 -72.333 17.994 1.00 48.04 C ATOM 3064 CG GLU E 9 3.652 -72.268 18.332 1.00 51.96 C ATOM 3065 CD GLU E 9 4.111 -73.475 19.130 1.00 55.46 C ATOM 3066 OE1 GLU E 9 3.680 -74.601 18.802 1.00 51.70 O ATOM 3067 OE2 GLU E 9 4.888 -73.302 20.093 1.00 53.51 O1- ATOM 3068 N LEU E 10 -0.717 -71.366 17.142 1.00 51.88 N ATOM 3069 CA LEU E 10 -2.076 -71.717 16.741 1.00 57.12 C ATOM 3070 C LEU E 10 -2.481 -70.995 15.462 1.00 54.96 C ATOM 3071 O LEU E 10 -3.104 -71.596 14.577 1.00 52.89 O ATOM 3072 CB LEU E 10 -3.052 -71.395 17.872 1.00 56.35 C ATOM 3073 CG LEU E 10 -4.523 -71.711 17.593 1.00 60.01 C ATOM 3074 CD1 LEU E 10 -4.718 -73.199 17.331 1.00 58.21 C ATOM 3075 CD2 LEU E 10 -5.392 -71.247 18.751 1.00 55.99 C ATOM 3076 N SER E 11 -2.134 -69.709 15.341 1.00 55.52 N ATOM 3077 CA SER E 11 -2.518 -68.949 14.154 1.00 61.35 C ATOM 3078 C SER E 11 -1.815 -69.475 12.909 1.00 62.76 C ATOM 3079 O SER E 11 -2.429 -69.583 11.843 1.00 62.55 O ATOM 3080 CB SER E 11 -2.212 -67.466 14.357 1.00 63.77 C ATOM 3081 OG SER E 11 -0.815 -67.219 14.285 1.00 72.73 O ATOM 3082 N ASP E 12 -0.527 -69.806 13.025 1.00 63.90 N ATOM 3083 CA ASP E 12 0.168 -70.440 11.908 1.00 67.92 C ATOM 3084 C ASP E 12 -0.383 -71.833 11.640 1.00 65.54 C ATOM 3085 O ASP E 12 -0.391 -72.287 10.488 1.00 57.65 O ATOM 3086 CB ASP E 12 1.672 -70.506 12.187 1.00 69.11 C ATOM 3087 CG ASP E 12 2.277 -69.140 12.462 1.00 78.22 C ATOM 3088 OD1 ASP E 12 1.657 -68.118 12.092 1.00 83.14 O ATOM 3089 OD2 ASP E 12 3.381 -69.088 13.047 1.00 76.22 O1- ATOM 3090 N LEU E 13 -0.852 -72.523 12.682 1.00 60.85 N ATOM 3091 CA LEU E 13 -1.453 -73.837 12.498 1.00 58.62 C ATOM 3092 C LEU E 13 -2.808 -73.738 11.818 1.00 67.98 C ATOM 3093 O LEU E 13 -3.201 -74.644 11.078 1.00 74.87 O ATOM 3094 CB LEU E 13 -1.578 -74.537 13.854 1.00 61.23 C ATOM 3095 CG LEU E 13 -1.688 -76.058 13.884 1.00 63.89 C ATOM 3096 CD1 LEU E 13 -0.475 -76.695 13.236 1.00 58.91 C ATOM 3097 CD2 LEU E 13 -1.834 -76.524 15.319 1.00 68.90 C ATOM 3098 N GLN E 14 -3.540 -72.648 12.057 1.00 63.71 N ATOM 3099 CA GLN E 14 -4.821 -72.436 11.396 1.00 62.77 C ATOM 3100 C GLN E 14 -4.643 -71.908 9.978 1.00 67.55 C ATOM 3101 O GLN E 14 -5.419 -72.254 9.084 1.00 73.25 O ATOM 3102 CB GLN E 14 -5.683 -71.476 12.215 1.00 55.13 C ATOM 3103 CG GLN E 14 -6.154 -72.042 13.546 1.00 51.85 C ATOM 3104 CD GLN E 14 -6.677 -70.969 14.482 1.00 58.76 C ATOM 3105 OE1 GLN E 14 -6.479 -69.775 14.248 1.00 65.65 O ATOM 3106 NE2 GLN E 14 -7.347 -71.389 15.549 1.00 53.92 N ATOM 3107 N ARG E 15 -3.626 -71.067 9.760 1.00 69.59 N ATOM 3108 CA ARG E 15 -3.381 -70.537 8.421 1.00 69.83 C ATOM 3109 C ARG E 15 -2.972 -71.641 7.456 1.00 75.18 C ATOM 3110 O ARG E 15 -3.297 -71.581 6.266 1.00 77.98 O ATOM 3111 CB ARG E 15 -2.305 -69.452 8.474 1.00 66.83 C ATOM 3112 CG ARG E 15 -2.045 -68.775 7.137 1.00 77.12 C ATOM 3113 CD ARG E 15 -3.305 -68.105 6.608 1.00 87.57 C ATOM 3114 NE ARG E 15 -3.195 -67.761 5.193 1.00 89.47 N ATOM 3115 CZ ARG E 15 -2.704 -66.617 4.731 1.00 88.88 C ATOM 3116 NH1 ARG E 15 -2.643 -66.397 3.424 1.00 86.36 N1+ ATOM 3117 NH2 ARG E 15 -2.267 -65.691 5.574 1.00 83.09 N ATOM 3118 N ASP E 16 -2.266 -72.652 7.945 1.00 82.61 N ATOM 3119 CA ASP E 16 -1.868 -73.789 7.130 1.00 85.16 C ATOM 3120 C ASP E 16 -2.028 -75.081 7.920 1.00 86.44 C ATOM 3121 O ASP E 16 -1.313 -75.299 8.907 1.00 84.18 O ATOM 3122 CB ASP E 16 -0.428 -73.638 6.651 1.00 83.61 C ATOM 3123 CG ASP E 16 0.111 -74.913 6.031 1.00 90.72 C ATOM 3124 OD1 ASP E 16 0.621 -75.772 6.784 1.00 94.96 O1- ATOM 3125 OD2 ASP E 16 0.019 -75.058 4.793 1.00 95.91 O ATOM 3126 N PRO E 17 -2.947 -75.956 7.525 1.00 88.75 N ATOM 3127 CA PRO E 17 -3.117 -77.221 8.236 1.00 83.45 C ATOM 3128 C PRO E 17 -2.127 -78.259 7.743 1.00 82.84 C ATOM 3129 O PRO E 17 -2.150 -78.640 6.564 1.00 80.14 O ATOM 3130 CB PRO E 17 -4.567 -77.623 7.904 1.00 86.31 C ATOM 3131 CG PRO E 17 -5.079 -76.580 6.912 1.00 86.93 C ATOM 3132 CD PRO E 17 -3.890 -75.831 6.410 1.00 80.67 C ATOM 3133 N PRO E 18 -1.234 -78.731 8.608 1.00 79.58 N ATOM 3134 CA PRO E 18 -0.301 -79.784 8.196 1.00 71.51 C ATOM 3135 C PRO E 18 -1.029 -81.099 7.963 1.00 72.70 C ATOM 3136 O PRO E 18 -2.026 -81.412 8.618 1.00 74.98 O ATOM 3137 CB PRO E 18 0.668 -79.882 9.380 1.00 69.36 C ATOM 3138 CG PRO E 18 -0.115 -79.392 10.548 1.00 68.67 C ATOM 3139 CD PRO E 18 -1.026 -78.322 10.009 1.00 71.78 C ATOM 3140 N ALA E 19 -0.510 -81.873 7.008 1.00 64.73 N ATOM 3141 CA ALA E 19 -1.167 -83.116 6.616 1.00 66.64 C ATOM 3142 C ALA E 19 -1.102 -84.184 7.699 1.00 70.93 C ATOM 3143 O ALA E 19 -1.928 -85.102 7.692 1.00 72.52 O ATOM 3144 CB ALA E 19 -0.548 -83.649 5.324 1.00 71.27 C ATOM 3145 N HIS E 20 -0.153 -84.083 8.628 1.00 73.57 N ATOM 3146 CA HIS E 20 0.099 -85.153 9.580 1.00 71.67 C ATOM 3147 C HIS E 20 -0.722 -85.046 10.860 1.00 69.78 C ATOM 3148 O HIS E 20 -0.718 -85.994 11.655 1.00 66.09 O ATOM 3149 CB HIS E 20 1.589 -85.197 9.941 1.00 65.75 C ATOM 3150 CG HIS E 20 2.092 -83.945 10.590 1.00 67.86 C ATOM 3151 ND1 HIS E 20 2.696 -82.930 9.881 1.00 65.41 N ATOM 3152 CD2 HIS E 20 2.091 -83.549 11.887 1.00 61.01 C ATOM 3153 CE1 HIS E 20 3.042 -81.960 10.709 1.00 65.77 C ATOM 3154 NE2 HIS E 20 2.686 -82.312 11.933 1.00 61.26 N ATOM 3155 N CYS E 21 -1.426 -83.939 11.086 1.00 66.83 N ATOM 3156 CA CYS E 21 -2.136 -83.773 12.348 1.00 63.65 C ATOM 3157 C CYS E 21 -3.191 -82.682 12.206 1.00 67.44 C ATOM 3158 O CYS E 21 -3.321 -82.038 11.161 1.00 66.48 O ATOM 3159 CB CYS E 21 -1.168 -83.445 13.486 1.00 65.11 C ATOM 3160 SG CYS E 21 -0.469 -81.779 13.404 1.00 75.27 S ATOM 3161 N ARG E 22 -3.957 -82.500 13.281 1.00 62.53 N ATOM 3162 CA ARG E 22 -4.882 -81.384 13.446 1.00 61.50 C ATOM 3163 C ARG E 22 -4.954 -81.090 14.933 1.00 58.42 C ATOM 3164 O ARG E 22 -5.276 -81.982 15.723 1.00 68.13 O ATOM 3165 CB ARG E 22 -6.271 -81.712 12.895 1.00 69.68 C ATOM 3166 CG ARG E 22 -7.371 -80.822 13.474 1.00 75.48 C ATOM 3167 CD ARG E 22 -8.651 -81.606 13.724 1.00 80.93 C ATOM 3168 NE ARG E 22 -9.500 -80.964 14.726 1.00 84.63 N ATOM 3169 CZ ARG E 22 -9.444 -81.219 16.032 1.00 85.23 C ATOM 3170 NH1 ARG E 22 -8.575 -82.104 16.503 1.00 74.57 N1+ ATOM 3171 NH2 ARG E 22 -10.254 -80.585 16.871 1.00 78.76 N ATOM 3172 N ALA E 23 -4.649 -79.856 15.321 1.00 62.18 N ATOM 3173 CA ALA E 23 -4.591 -79.495 16.728 1.00 66.48 C ATOM 3174 C ALA E 23 -5.340 -78.191 16.962 1.00 66.14 C ATOM 3175 O ALA E 23 -5.539 -77.387 16.049 1.00 70.81 O ATOM 3176 CB ALA E 23 -3.143 -79.365 17.217 1.00 62.53 C ATOM 3177 N GLY E 24 -5.746 -77.996 18.213 1.00 62.49 N ATOM 3178 CA GLY E 24 -6.456 -76.808 18.621 1.00 62.69 C ATOM 3179 C GLY E 24 -6.855 -76.880 20.080 1.00 63.39 C ATOM 3180 O GLY E 24 -6.876 -77.958 20.686 1.00 69.73 O ATOM 3181 N PRO E 25 -7.173 -75.737 20.677 1.00 65.69 N ATOM 3182 CA PRO E 25 -7.562 -75.722 22.092 1.00 67.46 C ATOM 3183 C PRO E 25 -8.889 -76.430 22.308 1.00 69.26 C ATOM 3184 O PRO E 25 -9.646 -76.714 21.373 1.00 68.45 O ATOM 3185 CB PRO E 25 -7.659 -74.229 22.421 1.00 64.26 C ATOM 3186 CG PRO E 25 -7.925 -73.574 21.107 1.00 61.80 C ATOM 3187 CD PRO E 25 -7.186 -74.388 20.083 1.00 61.29 C ATOM 3188 N VAL E 26 -9.168 -76.723 23.576 1.00 68.34 N ATOM 3189 CA VAL E 26 -10.407 -77.400 23.946 1.00 75.20 C ATOM 3190 C VAL E 26 -11.540 -76.406 24.152 1.00 78.41 C ATOM 3191 O VAL E 26 -12.625 -76.556 23.583 1.00 74.44 O ATOM 3192 CB VAL E 26 -10.184 -78.273 25.202 1.00 77.36 C ATOM 3193 CG1 VAL E 26 -9.553 -79.603 24.819 1.00 66.55 C ATOM 3194 CG2 VAL E 26 -9.315 -77.547 26.221 1.00 69.10 C ATOM 3195 N GLY E 27 -11.310 -75.372 24.957 1.00 78.23 N ATOM 3196 CA GLY E 27 -12.312 -74.351 25.184 1.00 75.78 C ATOM 3197 C GLY E 27 -11.739 -72.955 25.098 1.00 79.59 C ATOM 3198 O GLY E 27 -11.240 -72.543 24.044 1.00 79.00 O ATOM 3199 N ASP E 28 -11.804 -72.212 26.199 1.00 85.56 N ATOM 3200 CA ASP E 28 -11.244 -70.871 26.247 1.00 84.72 C ATOM 3201 C ASP E 28 -9.772 -70.858 26.623 1.00 85.46 C ATOM 3202 O ASP E 28 -9.073 -69.889 26.308 1.00 87.21 O ATOM 3203 CB ASP E 28 -12.024 -70.010 27.245 1.00 90.55 C ATOM 3204 CG ASP E 28 -13.519 -70.053 27.010 1.00 99.65 C ATOM 3205 OD1 ASP E 28 -13.936 -70.158 25.837 1.00100.59 O ATOM 3206 OD2 ASP E 28 -14.276 -69.986 28.003 1.00104.94 O1- ATOM 3207 N ASP E 29 -9.283 -71.906 27.281 1.00 80.83 N ATOM 3208 CA ASP E 29 -7.903 -71.969 27.746 1.00 75.68 C ATOM 3209 C ASP E 29 -7.031 -72.508 26.618 1.00 75.98 C ATOM 3210 O ASP E 29 -7.158 -73.674 26.227 1.00 75.82 O ATOM 3211 CB ASP E 29 -7.798 -72.848 28.990 1.00 79.04 C ATOM 3212 CG ASP E 29 -6.515 -72.609 29.764 1.00 81.46 C ATOM 3213 OD1 ASP E 29 -5.608 -71.934 29.234 1.00 80.34 O ATOM 3214 OD2 ASP E 29 -6.415 -73.107 30.906 1.00 81.66 O1- ATOM 3215 N LEU E 30 -6.147 -71.660 26.093 1.00 75.69 N ATOM 3216 CA LEU E 30 -5.210 -72.084 25.060 1.00 75.25 C ATOM 3217 C LEU E 30 -4.029 -72.864 25.622 1.00 67.65 C ATOM 3218 O LEU E 30 -3.211 -73.361 24.841 1.00 63.87 O ATOM 3219 CB LEU E 30 -4.705 -70.872 24.268 1.00 67.43 C ATOM 3220 CG LEU E 30 -5.725 -70.171 23.364 1.00 67.17 C ATOM 3221 CD1 LEU E 30 -6.490 -69.092 24.120 1.00 73.10 C ATOM 3222 CD2 LEU E 30 -5.048 -69.601 22.123 1.00 63.19 C ATOM 3223 N PHE E 31 -3.920 -72.981 26.945 1.00 62.29 N ATOM 3224 CA PHE E 31 -2.897 -73.819 27.556 1.00 67.57 C ATOM 3225 C PHE E 31 -3.263 -75.297 27.546 1.00 62.94 C ATOM 3226 O PHE E 31 -2.423 -76.126 27.912 1.00 60.25 O ATOM 3227 CB PHE E 31 -2.624 -73.360 28.990 1.00 65.34 C ATOM 3228 CG PHE E 31 -1.817 -72.094 29.082 1.00 68.23 C ATOM 3229 CD1 PHE E 31 -2.437 -70.856 29.012 1.00 70.17 C ATOM 3230 CD2 PHE E 31 -0.441 -72.143 29.233 1.00 62.47 C ATOM 3231 CE1 PHE E 31 -1.695 -69.688 29.096 1.00 63.75 C ATOM 3232 CE2 PHE E 31 0.304 -70.981 29.319 1.00 61.30 C ATOM 3233 CZ PHE E 31 -0.324 -69.750 29.250 1.00 65.74 C ATOM 3234 N HIS E 32 -4.489 -75.640 27.152 1.00 66.62 N ATOM 3235 CA HIS E 32 -4.924 -77.028 27.032 1.00 65.49 C ATOM 3236 C HIS E 32 -5.459 -77.234 25.622 1.00 60.88 C ATOM 3237 O HIS E 32 -6.408 -76.556 25.214 1.00 63.32 O ATOM 3238 CB HIS E 32 -5.993 -77.374 28.069 1.00 64.44 C ATOM 3239 CG HIS E 32 -5.552 -77.174 29.487 1.00 71.42 C ATOM 3240 ND1 HIS E 32 -5.522 -75.936 30.092 1.00 78.71 N ATOM 3241 CD2 HIS E 32 -5.117 -78.058 30.416 1.00 72.80 C ATOM 3242 CE1 HIS E 32 -5.089 -76.066 31.333 1.00 79.35 C ATOM 3243 NE2 HIS E 32 -4.836 -77.341 31.556 1.00 85.04 N ATOM 3244 N TRP E 33 -4.852 -78.159 24.886 1.00 58.20 N ATOM 3245 CA TRP E 33 -5.230 -78.437 23.512 1.00 56.17 C ATOM 3246 C TRP E 33 -5.637 -79.896 23.357 1.00 60.18 C ATOM 3247 O TRP E 33 -5.342 -80.745 24.203 1.00 61.39 O ATOM 3248 CB TRP E 33 -4.087 -78.142 22.530 1.00 60.73 C ATOM 3249 CG TRP E 33 -3.767 -76.694 22.340 1.00 55.52 C ATOM 3250 CD1 TRP E 33 -4.109 -75.658 23.156 1.00 58.38 C ATOM 3251 CD2 TRP E 33 -3.037 -76.119 21.249 1.00 55.12 C ATOM 3252 NE1 TRP E 33 -3.633 -74.474 22.644 1.00 54.78 N ATOM 3253 CE2 TRP E 33 -2.975 -74.731 21.473 1.00 58.57 C ATOM 3254 CE3 TRP E 33 -2.433 -76.647 20.102 1.00 53.26 C ATOM 3255 CZ2 TRP E 33 -2.326 -73.862 20.596 1.00 59.22 C ATOM 3256 CZ3 TRP E 33 -1.793 -75.785 19.234 1.00 61.17 C ATOM 3257 CH2 TRP E 33 -1.743 -74.408 19.485 1.00 61.96 C ATOM 3258 N GLN E 34 -6.313 -80.172 22.249 1.00 61.59 N ATOM 3259 CA GLN E 34 -6.611 -81.524 21.804 1.00 63.38 C ATOM 3260 C GLN E 34 -6.083 -81.687 20.387 1.00 63.39 C ATOM 3261 O GLN E 34 -6.421 -80.895 19.500 1.00 71.56 O ATOM 3262 CB GLN E 34 -8.111 -81.814 21.842 1.00 70.23 C ATOM 3263 CG GLN E 34 -8.508 -83.059 21.066 1.00 67.28 C ATOM 3264 CD GLN E 34 -10.005 -83.287 21.043 1.00 70.26 C ATOM 3265 OE1 GLN E 34 -10.700 -83.019 22.025 1.00 72.49 O ATOM 3266 NE2 GLN E 34 -10.514 -83.774 19.918 1.00 72.84 N ATOM 3267 N ALA E 35 -5.255 -82.703 20.180 1.00 61.00 N ATOM 3268 CA ALA E 35 -4.656 -82.962 18.882 1.00 58.56 C ATOM 3269 C ALA E 35 -5.082 -84.336 18.384 1.00 59.80 C ATOM 3270 O ALA E 35 -5.480 -85.207 19.160 1.00 66.11 O ATOM 3271 CB ALA E 35 -3.128 -82.877 18.948 1.00 60.23 C ATOM 3272 N THR E 36 -4.989 -84.519 17.070 1.00 56.76 N ATOM 3273 CA THR E 36 -5.275 -85.799 16.439 1.00 62.08 C ATOM 3274 C THR E 36 -4.267 -86.028 15.322 1.00 66.50 C ATOM 3275 O THR E 36 -4.103 -85.173 14.447 1.00 72.04 O ATOM 3276 CB THR E 36 -6.711 -85.856 15.889 1.00 66.83 C ATOM 3277 OG1 THR E 36 -6.833 -86.948 14.970 1.00 71.61 O ATOM 3278 CG2 THR E 36 -7.082 -84.561 15.186 1.00 67.29 C ATOM 3279 N ILE E 37 -3.586 -87.171 15.364 1.00 62.03 N ATOM 3280 CA ILE E 37 -2.569 -87.507 14.379 1.00 64.36 C ATOM 3281 C ILE E 37 -3.010 -88.754 13.629 1.00 63.63 C ATOM 3282 O ILE E 37 -3.751 -89.591 14.156 1.00 69.02 O ATOM 3283 CB ILE E 37 -1.181 -87.720 15.021 1.00 64.03 C ATOM 3284 CG1 ILE E 37 -1.194 -88.937 15.944 1.00 62.58 C ATOM 3285 CG2 ILE E 37 -0.752 -86.477 15.789 1.00 58.66 C ATOM 3286 CD1 ILE E 37 0.141 -89.229 16.592 1.00 59.13 C ATOM 3287 N MET E 38 -2.551 -88.871 12.389 1.00 64.67 N ATOM 3288 CA MET E 38 -2.851 -90.022 11.554 1.00 61.58 C ATOM 3289 C MET E 38 -1.678 -90.989 11.566 1.00 68.69 C ATOM 3290 O MET E 38 -0.514 -90.571 11.591 1.00 72.97 O ATOM 3291 CB MET E 38 -3.166 -89.593 10.121 1.00 71.47 C ATOM 3292 CG MET E 38 -4.401 -88.721 9.992 1.00 77.38 C ATOM 3293 SD MET E 38 -5.467 -89.244 8.635 1.00 94.07 S ATOM 3294 CE MET E 38 -5.889 -90.906 9.158 1.00 64.82 C ATOM 3295 N GLY E 39 -1.990 -92.280 11.553 1.00 64.87 N ATOM 3296 CA GLY E 39 -0.974 -93.302 11.529 1.00 60.43 C ATOM 3297 C GLY E 39 -0.184 -93.282 10.240 1.00 64.28 C ATOM 3298 O GLY E 39 -0.666 -92.835 9.195 1.00 70.59 O ATOM 3299 N PRO E 40 1.059 -93.754 10.295 1.00 67.13 N ATOM 3300 CA PRO E 40 1.867 -93.828 9.084 1.00 62.13 C ATOM 3301 C PRO E 40 1.188 -94.692 8.038 1.00 64.24 C ATOM 3302 O PRO E 40 0.393 -95.590 8.370 1.00 67.28 O ATOM 3303 CB PRO E 40 3.179 -94.454 9.574 1.00 64.89 C ATOM 3304 CG PRO E 40 3.256 -94.044 11.010 1.00 64.52 C ATOM 3305 CD PRO E 40 1.838 -94.080 11.506 1.00 62.41 C ATOM 3306 N PRO E 41 1.482 -94.460 6.756 1.00 74.48 N ATOM 3307 CA PRO E 41 0.678 -95.073 5.688 1.00 74.64 C ATOM 3308 C PRO E 41 0.962 -96.551 5.452 1.00 74.65 C ATOM 3309 O PRO E 41 0.082 -97.278 4.988 1.00 87.45 O ATOM 3310 CB PRO E 41 1.050 -94.237 4.457 1.00 69.33 C ATOM 3311 CG PRO E 41 2.447 -93.798 4.731 1.00 79.73 C ATOM 3312 CD PRO E 41 2.522 -93.568 6.220 1.00 77.53 C ATOM 3313 N ASP E 42 2.175 -97.002 5.736 1.00 70.62 N ATOM 3314 CA ASP E 42 2.590 -98.380 5.477 1.00 75.81 C ATOM 3315 C ASP E 42 3.098 -98.991 6.778 1.00 75.27 C ATOM 3316 O ASP E 42 4.304 -99.191 6.951 1.00 73.12 O ATOM 3317 CB ASP E 42 3.663 -98.435 4.374 1.00 75.49 C ATOM 3318 CG ASP E 42 3.107 -98.144 2.993 1.00 85.74 C ATOM 3319 OD1 ASP E 42 2.027 -97.526 2.897 1.00 87.04 O ATOM 3320 OD2 ASP E 42 3.758 -98.532 1.998 1.00 88.40 O1- ATOM 3321 N SER E 43 2.184 -99.302 7.690 1.00 70.96 N ATOM 3322 CA SER E 43 2.571 -99.808 9.001 1.00 72.15 C ATOM 3323 C SER E 43 1.384-100.536 9.621 1.00 68.62 C ATOM 3324 O SER E 43 0.387-100.827 8.953 1.00 72.44 O ATOM 3325 CB SER E 43 3.059 -98.672 9.902 1.00 62.35 C ATOM 3326 OG SER E 43 2.015 -97.754 10.174 1.00 62.44 O ATOM 3327 N ALA E 44 1.499-100.832 10.914 1.00 67.56 N ATOM 3328 CA ALA E 44 0.404-101.423 11.666 1.00 63.00 C ATOM 3329 C ALA E 44 -0.628-100.393 12.099 1.00 64.64 C ATOM 3330 O ALA E 44 -1.686-100.777 12.614 1.00 63.70 O ATOM 3331 CB ALA E 44 0.952-102.155 12.892 1.00 62.02 C ATOM 3332 N TYR E 45 -0.356 -99.103 11.897 1.00 61.97 N ATOM 3333 CA TYR E 45 -1.252 -98.026 12.303 1.00 59.53 C ATOM 3334 C TYR E 45 -1.908 -97.343 11.107 1.00 60.93 C ATOM 3335 O TYR E 45 -2.288 -96.173 11.191 1.00 62.05 O ATOM 3336 CB TYR E 45 -0.500 -97.000 13.148 1.00 61.16 C ATOM 3337 CG TYR E 45 0.352 -97.608 14.233 1.00 61.72 C ATOM 3338 CD1 TYR E 45 -0.177 -97.862 15.491 1.00 60.21 C ATOM 3339 CD2 TYR E 45 1.684 -97.925 14.001 1.00 56.06 C ATOM 3340 CE1 TYR E 45 0.595 -98.417 16.485 1.00 57.45 C ATOM 3341 CE2 TYR E 45 2.462 -98.476 14.989 1.00 53.92 C ATOM 3342 CZ TYR E 45 1.914 -98.721 16.226 1.00 54.42 C ATOM 3343 OH TYR E 45 2.691 -99.270 17.208 1.00 50.89 O ATOM 3344 N GLN E 46 -2.039 -98.061 9.992 1.00 65.38 N ATOM 3345 CA GLN E 46 -2.655 -97.500 8.797 1.00 64.12 C ATOM 3346 C GLN E 46 -4.083 -97.055 9.076 1.00 66.26 C ATOM 3347 O GLN E 46 -4.829 -97.704 9.818 1.00 73.58 O ATOM 3348 CB GLN E 46 -2.657 -98.516 7.659 1.00 66.50 C ATOM 3349 CG GLN E 46 -1.286 -98.944 7.202 1.00 69.92 C ATOM 3350 CD GLN E 46 -1.336 -99.994 6.105 1.00 76.44 C ATOM 3351 OE1 GLN E 46 -2.369-100.188 5.465 1.00 83.42 O ATOM 3352 NE2 GLN E 46 -0.217-100.677 5.886 1.00 76.98 N ATOM 3353 N GLY E 47 -4.459 -95.937 8.472 1.00 63.36 N ATOM 3354 CA GLY E 47 -5.779 -95.375 8.650 1.00 60.37 C ATOM 3355 C GLY E 47 -6.178 -95.030 10.070 1.00 74.74 C ATOM 3356 O GLY E 47 -7.316 -94.579 10.273 1.00 73.50 O ATOM 3357 N GLY E 48 -5.320 -95.217 11.067 1.00 66.89 N ATOM 3358 CA GLY E 48 -5.711 -94.918 12.431 1.00 56.48 C ATOM 3359 C GLY E 48 -5.753 -93.427 12.702 1.00 61.61 C ATOM 3360 O GLY E 48 -5.007 -92.637 12.125 1.00 64.60 O ATOM 3361 N VAL E 49 -6.657 -93.040 13.593 1.00 57.82 N ATOM 3362 CA VAL E 49 -6.832 -91.657 14.015 1.00 59.49 C ATOM 3363 C VAL E 49 -6.663 -91.647 15.522 1.00 62.51 C ATOM 3364 O VAL E 49 -7.520 -92.161 16.253 1.00 70.90 O ATOM 3365 CB VAL E 49 -8.197 -91.102 13.601 1.00 65.71 C ATOM 3366 CG1 VAL E 49 -8.386 -89.712 14.155 1.00 59.99 C ATOM 3367 CG2 VAL E 49 -8.328 -91.108 12.082 1.00 57.89 C ATOM 3368 N PHE E 50 -5.559 -91.080 15.990 1.00 61.62 N ATOM 3369 CA PHE E 50 -5.174 -91.130 17.395 1.00 59.43 C ATOM 3370 C PHE E 50 -5.318 -89.741 17.999 1.00 57.40 C ATOM 3371 O PHE E 50 -4.725 -88.781 17.498 1.00 63.83 O ATOM 3372 CB PHE E 50 -3.741 -91.643 17.547 1.00 59.52 C ATOM 3373 CG PHE E 50 -3.507 -92.980 16.905 1.00 53.79 C ATOM 3374 CD1 PHE E 50 -3.138 -93.071 15.570 1.00 49.46 C ATOM 3375 CD2 PHE E 50 -3.654 -94.150 17.636 1.00 52.26 C ATOM 3376 CE1 PHE E 50 -2.924 -94.306 14.977 1.00 58.03 C ATOM 3377 CE2 PHE E 50 -3.440 -95.386 17.051 1.00 49.93 C ATOM 3378 CZ PHE E 50 -3.074 -95.465 15.720 1.00 54.15 C ATOM 3379 N PHE E 51 -6.098 -89.643 19.065 1.00 51.49 N ATOM 3380 CA PHE E 51 -6.292 -88.389 19.780 1.00 54.88 C ATOM 3381 C PHE E 51 -5.232 -88.237 20.864 1.00 59.89 C ATOM 3382 O PHE E 51 -4.782 -89.220 21.461 1.00 63.23 O ATOM 3383 CB PHE E 51 -7.687 -88.330 20.406 1.00 59.06 C ATOM 3384 CG PHE E 51 -8.810 -88.229 19.405 1.00 64.81 C ATOM 3385 CD1 PHE E 51 -9.153 -89.315 18.612 1.00 60.16 C ATOM 3386 CD2 PHE E 51 -9.535 -87.054 19.273 1.00 67.25 C ATOM 3387 CE1 PHE E 51 -10.186 -89.224 17.696 1.00 59.53 C ATOM 3388 CE2 PHE E 51 -10.569 -86.959 18.364 1.00 62.33 C ATOM 3389 CZ PHE E 51 -10.896 -88.045 17.573 1.00 66.06 C ATOM 3390 N LEU E 52 -4.829 -86.991 21.113 1.00 59.11 N ATOM 3391 CA LEU E 52 -3.839 -86.689 22.137 1.00 50.28 C ATOM 3392 C LEU E 52 -4.258 -85.440 22.896 1.00 57.64 C ATOM 3393 O LEU E 52 -5.076 -84.646 22.429 1.00 64.39 O ATOM 3394 CB LEU E 52 -2.437 -86.486 21.543 1.00 53.28 C ATOM 3395 CG LEU E 52 -1.765 -87.668 20.839 1.00 55.15 C ATOM 3396 CD1 LEU E 52 -2.110 -87.698 19.358 1.00 54.67 C ATOM 3397 CD2 LEU E 52 -0.259 -87.622 21.043 1.00 54.49 C ATOM 3398 N THR E 53 -3.673 -85.274 24.080 1.00 57.10 N ATOM 3399 CA THR E 53 -3.894 -84.110 24.924 1.00 56.90 C ATOM 3400 C THR E 53 -2.588 -83.336 25.050 1.00 58.66 C ATOM 3401 O THR E 53 -1.535 -83.928 25.313 1.00 66.28 O ATOM 3402 CB THR E 53 -4.396 -84.517 26.312 1.00 61.69 C ATOM 3403 OG1 THR E 53 -5.659 -85.180 26.188 1.00 74.43 O ATOM 3404 CG2 THR E 53 -4.557 -83.297 27.211 1.00 49.04 C ATOM 3405 N VAL E 54 -2.656 -82.021 24.855 1.00 57.45 N ATOM 3406 CA VAL E 54 -1.497 -81.145 24.953 1.00 52.48 C ATOM 3407 C VAL E 54 -1.749 -80.155 26.078 1.00 52.73 C ATOM 3408 O VAL E 54 -2.739 -79.416 26.050 1.00 59.93 O ATOM 3409 CB VAL E 54 -1.221 -80.412 23.629 1.00 49.16 C ATOM 3410 CG1 VAL E 54 0.036 -79.573 23.745 1.00 45.94 C ATOM 3411 CG2 VAL E 54 -1.102 -81.409 22.485 1.00 43.58 C ATOM 3412 N HIS E 55 -0.858 -80.141 27.063 1.00 53.18 N ATOM 3413 CA HIS E 55 -0.959 -79.254 28.217 1.00 59.35 C ATOM 3414 C HIS E 55 0.315 -78.422 28.288 1.00 59.79 C ATOM 3415 O HIS E 55 1.393 -78.954 28.575 1.00 56.44 O ATOM 3416 CB HIS E 55 -1.173 -80.052 29.503 1.00 58.62 C ATOM 3417 CG HIS E 55 -1.242 -79.206 30.734 1.00 63.43 C ATOM 3418 ND1 HIS E 55 -1.573 -77.867 30.704 1.00 72.92 N ATOM 3419 CD2 HIS E 55 -1.019 -79.506 32.038 1.00 67.81 C ATOM 3420 CE1 HIS E 55 -1.554 -77.382 31.931 1.00 70.50 C ATOM 3421 NE2 HIS E 55 -1.222 -78.355 32.759 1.00 75.45 N ATOM 3422 N PHE E 56 0.189 -77.129 28.029 1.00 57.22 N ATOM 3423 CA PHE E 56 1.347 -76.245 28.040 1.00 49.97 C ATOM 3424 C PHE E 56 1.628 -75.765 29.459 1.00 53.47 C ATOM 3425 O PHE E 56 0.705 -75.317 30.146 1.00 62.91 O ATOM 3426 CB PHE E 56 1.118 -75.043 27.132 1.00 53.60 C ATOM 3427 CG PHE E 56 0.902 -75.398 25.694 1.00 51.05 C ATOM 3428 CD1 PHE E 56 1.976 -75.493 24.824 1.00 51.73 C ATOM 3429 CD2 PHE E 56 -0.374 -75.617 25.202 1.00 55.83 C ATOM 3430 CE1 PHE E 56 1.783 -75.810 23.497 1.00 47.14 C ATOM 3431 CE2 PHE E 56 -0.572 -75.937 23.872 1.00 53.81 C ATOM 3432 CZ PHE E 56 0.505 -76.032 23.020 1.00 46.43 C ATOM 3433 N PRO E 57 2.870 -75.839 29.922 1.00 56.05 N ATOM 3434 CA PRO E 57 3.209 -75.244 31.219 1.00 56.06 C ATOM 3435 C PRO E 57 3.227 -73.725 31.137 1.00 59.84 C ATOM 3436 O PRO E 57 3.141 -73.123 30.064 1.00 57.10 O ATOM 3437 CB PRO E 57 4.601 -75.806 31.516 1.00 52.91 C ATOM 3438 CG PRO E 57 5.170 -76.116 30.168 1.00 51.70 C ATOM 3439 CD PRO E 57 4.011 -76.546 29.317 1.00 49.20 C ATOM 3440 N THR E 58 3.342 -73.099 32.310 1.00 57.60 N ATOM 3441 CA THR E 58 3.363 -71.642 32.367 1.00 62.55 C ATOM 3442 C THR E 58 4.664 -71.056 31.837 1.00 56.84 C ATOM 3443 O THR E 58 4.684 -69.890 31.428 1.00 58.54 O ATOM 3444 CB THR E 58 3.131 -71.166 33.803 1.00 63.06 C ATOM 3445 OG1 THR E 58 4.197 -71.636 34.642 1.00 65.94 O ATOM 3446 CG2 THR E 58 1.802 -71.693 34.333 1.00 63.03 C ATOM 3447 N ASP E 59 5.750 -71.832 31.831 1.00 57.51 N ATOM 3448 CA ASP E 59 7.043 -71.372 31.347 1.00 54.37 C ATOM 3449 C ASP E 59 7.358 -71.885 29.946 1.00 53.41 C ATOM 3450 O ASP E 59 8.531 -71.989 29.573 1.00 54.02 O ATOM 3451 CB ASP E 59 8.145 -71.774 32.327 1.00 51.43 C ATOM 3452 CG ASP E 59 7.934 -73.163 32.906 1.00 59.44 C ATOM 3453 OD1 ASP E 59 7.219 -73.971 32.278 1.00 67.61 O ATOM 3454 OD2 ASP E 59 8.488 -73.447 33.989 1.00 61.92 O1- ATOM 3455 N TYR E 60 6.334 -72.216 29.163 1.00 50.90 N ATOM 3456 CA TYR E 60 6.495 -72.594 27.764 1.00 49.79 C ATOM 3457 C TYR E 60 7.047 -71.395 26.988 1.00 50.20 C ATOM 3458 O TYR E 60 6.691 -70.257 27.287 1.00 55.39 O ATOM 3459 CB TYR E 60 5.151 -73.061 27.195 1.00 46.73 C ATOM 3460 CG TYR E 60 5.194 -73.614 25.789 1.00 43.47 C ATOM 3461 CD1 TYR E 60 5.623 -74.912 25.546 1.00 45.49 C ATOM 3462 CD2 TYR E 60 4.786 -72.844 24.708 1.00 48.32 C ATOM 3463 CE1 TYR E 60 5.659 -75.426 24.261 1.00 44.04 C ATOM 3464 CE2 TYR E 60 4.814 -73.348 23.420 1.00 47.56 C ATOM 3465 CZ TYR E 60 5.252 -74.639 23.202 1.00 43.61 C ATOM 3466 OH TYR E 60 5.284 -75.140 21.921 1.00 47.43 O ATOM 3467 N PRO E 61 7.922 -71.634 25.993 1.00 51.37 N ATOM 3468 CA PRO E 61 8.439 -72.919 25.508 1.00 47.30 C ATOM 3469 C PRO E 61 9.770 -73.331 26.128 1.00 46.52 C ATOM 3470 O PRO E 61 10.437 -74.221 25.594 1.00 42.04 O ATOM 3471 CB PRO E 61 8.609 -72.656 24.014 1.00 45.62 C ATOM 3472 CG PRO E 61 9.043 -71.228 23.968 1.00 49.40 C ATOM 3473 CD PRO E 61 8.365 -70.523 25.132 1.00 47.15 C ATOM 3474 N PHE E 62 10.156 -72.699 27.235 1.00 39.82 N ATOM 3475 CA PHE E 62 11.408 -73.061 27.884 1.00 38.70 C ATOM 3476 C PHE E 62 11.308 -74.389 28.626 1.00 46.76 C ATOM 3477 O PHE E 62 12.341 -74.998 28.926 1.00 46.23 O ATOM 3478 CB PHE E 62 11.846 -71.936 28.822 1.00 46.30 C ATOM 3479 CG PHE E 62 11.870 -70.586 28.157 1.00 47.38 C ATOM 3480 CD1 PHE E 62 12.908 -70.235 27.312 1.00 43.19 C ATOM 3481 CD2 PHE E 62 10.840 -69.681 28.360 1.00 45.74 C ATOM 3482 CE1 PHE E 62 12.921 -69.002 26.686 1.00 46.27 C ATOM 3483 CE2 PHE E 62 10.852 -68.443 27.740 1.00 48.33 C ATOM 3484 CZ PHE E 62 11.895 -68.107 26.903 1.00 45.45 C ATOM 3485 N LYS E 63 10.094 -74.851 28.921 1.00 51.63 N ATOM 3486 CA LYS E 63 9.844 -76.191 29.410 1.00 46.88 C ATOM 3487 C LYS E 63 8.913 -76.906 28.442 1.00 48.36 C ATOM 3488 O LYS E 63 8.010 -76.280 27.880 1.00 43.98 O ATOM 3489 CB LYS E 63 9.218 -76.169 30.817 1.00 52.35 C ATOM 3490 CG LYS E 63 10.138 -75.624 31.900 1.00 55.38 C ATOM 3491 CD LYS E 63 11.358 -76.513 32.089 1.00 62.00 C ATOM 3492 CE LYS E 63 12.263 -75.974 33.185 1.00 64.90 C ATOM 3493 NZ LYS E 63 13.468 -76.822 33.388 1.00 67.42 N1+ ATOM 3494 N PRO E 64 9.103 -78.206 28.221 1.00 48.55 N ATOM 3495 CA PRO E 64 8.325 -78.915 27.192 1.00 49.06 C ATOM 3496 C PRO E 64 6.867 -79.052 27.584 1.00 51.61 C ATOM 3497 O PRO E 64 6.525 -79.043 28.780 1.00 54.66 O ATOM 3498 CB PRO E 64 9.008 -80.294 27.124 1.00 47.58 C ATOM 3499 CG PRO E 64 9.595 -80.464 28.477 1.00 49.09 C ATOM 3500 CD PRO E 64 10.021 -79.102 28.941 1.00 47.77 C ATOM 3501 N PRO E 65 5.977 -79.192 26.609 1.00 52.41 N ATOM 3502 CA PRO E 65 4.568 -79.433 26.916 1.00 49.46 C ATOM 3503 C PRO E 65 4.315 -80.897 27.234 1.00 58.08 C ATOM 3504 O PRO E 65 4.963 -81.799 26.701 1.00 54.19 O ATOM 3505 CB PRO E 65 3.855 -79.021 25.627 1.00 53.06 C ATOM 3506 CG PRO E 65 4.856 -79.326 24.556 1.00 45.12 C ATOM 3507 CD PRO E 65 6.209 -79.040 25.162 1.00 48.10 C ATOM 3508 N LYS E 66 3.354 -81.119 28.125 1.00 56.39 N ATOM 3509 CA LYS E 66 2.964 -82.468 28.510 1.00 46.33 C ATOM 3510 C LYS E 66 1.981 -83.011 27.485 1.00 51.83 C ATOM 3511 O LYS E 66 0.879 -82.477 27.322 1.00 54.33 O ATOM 3512 CB LYS E 66 2.354 -82.464 29.909 1.00 58.42 C ATOM 3513 CG LYS E 66 1.919 -83.828 30.414 1.00 54.83 C ATOM 3514 CD LYS E 66 1.193 -83.703 31.747 1.00 68.13 C ATOM 3515 CE LYS E 66 0.374 -84.943 32.059 1.00 80.59 C ATOM 3516 NZ LYS E 66 -0.575 -84.710 33.186 1.00 79.02 N1+ ATOM 3517 N ILE E 67 2.382 -84.069 26.784 1.00 54.99 N ATOM 3518 CA ILE E 67 1.602 -84.649 25.699 1.00 44.88 C ATOM 3519 C ILE E 67 1.370 -86.123 26.003 1.00 57.22 C ATOM 3520 O ILE E 67 2.320 -86.857 26.293 1.00 63.48 O ATOM 3521 CB ILE E 67 2.316 -84.481 24.346 1.00 49.52 C ATOM 3522 CG1 ILE E 67 2.540 -82.996 24.050 1.00 54.27 C ATOM 3523 CG2 ILE E 67 1.522 -85.152 23.233 1.00 49.24 C ATOM 3524 CD1 ILE E 67 3.275 -82.736 22.763 1.00 47.77 C ATOM 3525 N ALA E 68 0.112 -86.547 25.926 1.00 59.14 N ATOM 3526 CA ALA E 68 -0.261 -87.922 26.218 1.00 52.51 C ATOM 3527 C ALA E 68 -1.393 -88.362 25.304 1.00 51.54 C ATOM 3528 O ALA E 68 -2.287 -87.574 24.986 1.00 56.05 O ATOM 3529 CB ALA E 68 -0.685 -88.088 27.685 1.00 50.51 C ATOM 3530 N PHE E 69 -1.346 -89.624 24.882 1.00 57.42 N ATOM 3531 CA PHE E 69 -2.424 -90.196 24.089 1.00 53.33 C ATOM 3532 C PHE E 69 -3.682 -90.364 24.933 1.00 65.05 C ATOM 3533 O PHE E 69 -3.619 -90.731 26.108 1.00 57.56 O ATOM 3534 CB PHE E 69 -2.014 -91.556 23.526 1.00 55.62 C ATOM 3535 CG PHE E 69 -1.128 -91.483 22.319 1.00 58.73 C ATOM 3536 CD1 PHE E 69 0.231 -91.252 22.449 1.00 57.92 C ATOM 3537 CD2 PHE E 69 -1.652 -91.675 21.051 1.00 49.98 C ATOM 3538 CE1 PHE E 69 1.047 -91.196 21.331 1.00 49.60 C ATOM 3539 CE2 PHE E 69 -0.842 -91.619 19.931 1.00 53.71 C ATOM 3540 CZ PHE E 69 0.509 -91.381 20.074 1.00 47.45 C ATOM 3541 N THR E 70 -4.831 -90.086 24.320 1.00 67.61 N ATOM 3542 CA THR E 70 -6.118 -90.499 24.874 1.00 56.25 C ATOM 3543 C THR E 70 -6.684 -91.722 24.171 1.00 62.89 C ATOM 3544 O THR E 70 -7.367 -92.528 24.806 1.00 67.26 O ATOM 3545 CB THR E 70 -7.133 -89.353 24.800 1.00 55.41 C ATOM 3546 OG1 THR E 70 -7.212 -88.865 23.455 1.00 63.83 O ATOM 3547 CG2 THR E 70 -6.724 -88.220 25.723 1.00 45.76 C ATOM 3548 N THR E 71 -6.410 -91.874 22.878 1.00 59.96 N ATOM 3549 CA THR E 71 -6.697 -93.120 22.187 1.00 58.32 C ATOM 3550 C THR E 71 -5.719 -94.196 22.647 1.00 66.12 C ATOM 3551 O THR E 71 -4.535 -93.923 22.873 1.00 67.63 O ATOM 3552 CB THR E 71 -6.593 -92.925 20.673 1.00 61.11 C ATOM 3553 OG1 THR E 71 -7.441 -91.844 20.270 1.00 66.28 O ATOM 3554 CG2 THR E 71 -7.002 -94.190 19.930 1.00 58.03 C ATOM 3555 N LYS E 72 -6.216 -95.420 22.794 1.00 71.76 N ATOM 3556 CA LYS E 72 -5.376 -96.533 23.211 1.00 67.37 C ATOM 3557 C LYS E 72 -4.546 -97.006 22.026 1.00 59.32 C ATOM 3558 O LYS E 72 -5.062 -97.147 20.912 1.00 67.59 O ATOM 3559 CB LYS E 72 -6.227 -97.678 23.766 1.00 72.94 C ATOM 3560 CG LYS E 72 -7.160 -97.274 24.908 1.00 72.83 C ATOM 3561 CD LYS E 72 -8.506 -96.787 24.385 1.00 75.50 C ATOM 3562 CE LYS E 72 -9.201 -95.865 25.374 1.00 81.92 C ATOM 3563 NZ LYS E 72 -10.402 -95.228 24.763 1.00 69.07 N1+ ATOM 3564 N ILE E 73 -3.258 -97.232 22.259 1.00 59.67 N ATOM 3565 CA ILE E 73 -2.319 -97.568 21.194 1.00 55.88 C ATOM 3566 C ILE E 73 -1.353 -98.625 21.708 1.00 55.09 C ATOM 3567 O ILE E 73 -0.946 -98.596 22.874 1.00 61.68 O ATOM 3568 CB ILE E 73 -1.578 -96.314 20.687 1.00 58.14 C ATOM 3569 CG1 ILE E 73 -0.686 -96.648 19.489 1.00 55.15 C ATOM 3570 CG2 ILE E 73 -0.776 -95.669 21.808 1.00 56.22 C ATOM 3571 CD1 ILE E 73 -0.048 -95.430 18.865 1.00 47.66 C ATOM 3572 N TYR E 74 -1.008 -99.573 20.840 1.00 51.69 N ATOM 3573 CA TYR E 74 -0.111-100.675 21.185 1.00 51.05 C ATOM 3574 C TYR E 74 1.300-100.245 20.815 1.00 54.47 C ATOM 3575 O TYR E 74 1.664-100.237 19.638 1.00 54.50 O ATOM 3576 CB TYR E 74 -0.533-101.943 20.451 1.00 55.58 C ATOM 3577 CG TYR E 74 0.120-103.212 20.949 1.00 54.48 C ATOM 3578 CD1 TYR E 74 -0.399-103.897 22.046 1.00 55.15 C ATOM 3579 CD2 TYR E 74 1.236-103.739 20.316 1.00 52.89 C ATOM 3580 CE1 TYR E 74 0.188-105.060 22.503 1.00 55.88 C ATOM 3581 CE2 TYR E 74 1.830-104.906 20.767 1.00 55.09 C ATOM 3582 CZ TYR E 74 1.301-105.561 21.867 1.00 55.34 C ATOM 3583 OH TYR E 74 1.874-106.723 22.332 1.00 55.16 O ATOM 3584 N HIS E 75 2.108 -99.872 21.813 1.00 45.97 N ATOM 3585 CA HIS E 75 3.457 -99.389 21.540 1.00 48.65 C ATOM 3586 C HIS E 75 4.349 -99.604 22.753 1.00 49.90 C ATOM 3587 O HIS E 75 3.892 -99.406 23.886 1.00 52.07 O ATOM 3588 CB HIS E 75 3.450 -97.904 21.159 1.00 49.97 C ATOM 3589 CG HIS E 75 4.712 -97.443 20.500 1.00 45.86 C ATOM 3590 ND1 HIS E 75 5.749 -96.863 21.196 1.00 49.83 N ATOM 3591 CD2 HIS E 75 5.100 -97.481 19.204 1.00 47.95 C ATOM 3592 CE1 HIS E 75 6.724 -96.561 20.356 1.00 50.33 C ATOM 3593 NE2 HIS E 75 6.355 -96.925 19.140 1.00 53.92 N ATOM 3594 N PRO E 76 5.613-100.000 22.555 1.00 48.90 N ATOM 3595 CA PRO E 76 6.497-100.248 23.707 1.00 47.00 C ATOM 3596 C PRO E 76 6.817 -99.009 24.523 1.00 49.71 C ATOM 3597 O PRO E 76 7.211 -99.137 25.686 1.00 50.54 O ATOM 3598 CB PRO E 76 7.771-100.821 23.061 1.00 47.16 C ATOM 3599 CG PRO E 76 7.362-101.249 21.675 1.00 51.52 C ATOM 3600 CD PRO E 76 6.272-100.306 21.273 1.00 46.27 C ATOM 3601 N ASN E 77 6.675 -97.818 23.946 1.00 48.69 N ATOM 3602 CA ASN E 77 7.037 -96.579 24.621 1.00 42.37 C ATOM 3603 C ASN E 77 5.819 -95.759 25.036 1.00 47.32 C ATOM 3604 O ASN E 77 5.975 -94.612 25.465 1.00 47.59 O ATOM 3605 CB ASN E 77 7.958 -95.752 23.721 1.00 46.00 C ATOM 3606 CG ASN E 77 9.186 -96.527 23.278 1.00 48.31 C ATOM 3607 OD1 ASN E 77 9.371 -96.802 22.092 1.00 49.09 O ATOM 3608 ND2 ASN E 77 10.035 -96.880 24.234 1.00 49.75 N ATOM 3609 N ILE E 78 4.615 -96.312 24.907 1.00 50.58 N ATOM 3610 CA ILE E 78 3.376 -95.646 25.302 1.00 53.49 C ATOM 3611 C ILE E 78 2.585 -96.614 26.174 1.00 48.11 C ATOM 3612 O ILE E 78 2.208 -97.695 25.709 1.00 50.50 O ATOM 3613 CB ILE E 78 2.537 -95.211 24.088 1.00 51.57 C ATOM 3614 CG1 ILE E 78 3.413 -94.498 23.056 1.00 49.88 C ATOM 3615 CG2 ILE E 78 1.395 -94.309 24.523 1.00 51.04 C ATOM 3616 CD1 ILE E 78 2.757 -94.339 21.710 1.00 43.19 C ATOM 3617 N ASN E 79 2.328 -96.227 27.423 1.00 49.37 N ATOM 3618 CA ASN E 79 1.682 -97.129 28.360 1.00 53.70 C ATOM 3619 C ASN E 79 0.161 -97.044 28.228 1.00 53.99 C ATOM 3620 O ASN E 79 -0.382 -96.332 27.382 1.00 62.01 O ATOM 3621 CB ASN E 79 2.140 -96.849 29.792 1.00 47.38 C ATOM 3622 CG ASN E 79 1.854 -95.429 30.240 1.00 52.09 C ATOM 3623 OD1 ASN E 79 1.029 -94.730 29.653 1.00 57.87 O ATOM 3624 ND2 ASN E 79 2.532 -95.002 31.297 1.00 52.06 N ATOM 3625 N SER E 80 -0.542 -97.793 29.087 1.00 52.17 N ATOM 3626 CA SER E 80 -1.998 -97.839 29.037 1.00 51.29 C ATOM 3627 C SER E 80 -2.638 -96.508 29.409 1.00 55.57 C ATOM 3628 O SER E 80 -3.775 -96.248 29.001 1.00 55.93 O ATOM 3629 CB SER E 80 -2.519 -98.946 29.957 1.00 54.42 C ATOM 3630 OG SER E 80 -2.087 -98.738 31.290 1.00 65.10 O ATOM 3631 N ASN E 81 -1.947 -95.671 30.175 1.00 57.31 N ATOM 3632 CA ASN E 81 -2.451 -94.342 30.508 1.00 55.65 C ATOM 3633 C ASN E 81 -2.196 -93.322 29.406 1.00 56.52 C ATOM 3634 O ASN E 81 -2.560 -92.153 29.574 1.00 54.94 O ATOM 3635 CB ASN E 81 -1.825 -93.854 31.817 1.00 55.27 C ATOM 3636 CG ASN E 81 -2.235 -94.697 33.009 1.00 66.62 C ATOM 3637 OD1 ASN E 81 -1.660 -95.752 33.267 1.00 70.51 O ATOM 3638 ND2 ASN E 81 -3.236 -94.225 33.746 1.00 61.73 N ATOM 3639 N GLY E 82 -1.591 -93.730 28.293 1.00 53.12 N ATOM 3640 CA GLY E 82 -1.274 -92.821 27.212 1.00 57.45 C ATOM 3641 C GLY E 82 0.002 -92.026 27.387 1.00 59.23 C ATOM 3642 O GLY E 82 0.335 -91.226 26.502 1.00 56.30 O ATOM 3643 N SER E 83 0.726 -92.213 28.492 1.00 47.70 N ATOM 3644 CA SER E 83 1.967 -91.487 28.705 1.00 44.76 C ATOM 3645 C SER E 83 3.003 -91.886 27.665 1.00 47.70 C ATOM 3646 O SER E 83 3.134 -93.062 27.313 1.00 48.41 O ATOM 3647 CB SER E 83 2.503 -91.754 30.113 1.00 51.93 C ATOM 3648 OG SER E 83 1.605 -91.290 31.104 1.00 56.78 O ATOM 3649 N ILE E 84 3.743 -90.895 27.169 1.00 52.08 N ATOM 3650 CA ILE E 84 4.763 -91.089 26.144 1.00 47.62 C ATOM 3651 C ILE E 84 6.121 -90.847 26.784 1.00 50.21 C ATOM 3652 O ILE E 84 6.411 -89.733 27.240 1.00 56.30 O ATOM 3653 CB ILE E 84 4.559 -90.145 24.953 1.00 51.54 C ATOM 3654 CG1 ILE E 84 3.096 -90.142 24.510 1.00 50.94 C ATOM 3655 CG2 ILE E 84 5.481 -90.533 23.801 1.00 44.31 C ATOM 3656 CD1 ILE E 84 2.774 -89.041 23.522 1.00 51.61 C ATOM 3657 N LYS E 85 6.958 -91.880 26.813 1.00 43.52 N ATOM 3658 CA LYS E 85 8.321 -91.739 27.319 1.00 53.63 C ATOM 3659 C LYS E 85 9.224 -91.450 26.128 1.00 50.34 C ATOM 3660 O LYS E 85 9.640 -92.362 25.407 1.00 44.17 O ATOM 3661 CB LYS E 85 8.754 -92.982 28.088 1.00 48.00 C ATOM 3662 CG LYS E 85 9.839 -92.704 29.122 1.00 49.12 C ATOM 3663 CD LYS E 85 10.012 -93.861 30.098 1.00 48.90 C ATOM 3664 CE LYS E 85 10.594 -95.084 29.419 1.00 45.48 C ATOM 3665 NZ LYS E 85 11.878 -94.776 28.730 1.00 53.37 N1+ ATOM 3666 N LEU E 86 9.515 -90.169 25.911 1.00 52.33 N ATOM 3667 CA LEU E 86 10.241 -89.696 24.741 1.00 47.64 C ATOM 3668 C LEU E 86 11.200 -88.599 25.175 1.00 49.33 C ATOM 3669 O LEU E 86 10.835 -87.729 25.971 1.00 50.20 O ATOM 3670 CB LEU E 86 9.267 -89.182 23.670 1.00 40.57 C ATOM 3671 CG LEU E 86 9.826 -88.666 22.346 1.00 48.15 C ATOM 3672 CD1 LEU E 86 10.646 -89.736 21.648 1.00 50.12 C ATOM 3673 CD2 LEU E 86 8.681 -88.205 21.460 1.00 42.77 C ATOM 3674 N ASP E 87 12.423 -88.634 24.635 1.00 42.39 N ATOM 3675 CA ASP E 87 13.484 -87.772 25.155 1.00 49.76 C ATOM 3676 C ASP E 87 13.223 -86.299 24.857 1.00 47.08 C ATOM 3677 O ASP E 87 13.518 -85.433 25.690 1.00 47.25 O ATOM 3678 CB ASP E 87 14.842 -88.202 24.585 1.00 49.24 C ATOM 3679 CG ASP E 87 14.915 -88.072 23.076 1.00 50.23 C ATOM 3680 OD1 ASP E 87 13.855 -88.105 22.413 1.00 50.72 O ATOM 3681 OD2 ASP E 87 16.039 -87.936 22.549 1.00 63.79 O1- ATOM 3682 N ILE E 88 12.671 -85.985 23.680 1.00 42.08 N ATOM 3683 CA ILE E 88 12.398 -84.595 23.336 1.00 44.49 C ATOM 3684 C ILE E 88 11.295 -83.985 24.185 1.00 47.23 C ATOM 3685 O ILE E 88 11.097 -82.766 24.141 1.00 51.44 O ATOM 3686 CB ILE E 88 12.026 -84.445 21.849 1.00 46.12 C ATOM 3687 CG1 ILE E 88 10.734 -85.201 21.542 1.00 49.73 C ATOM 3688 CG2 ILE E 88 13.168 -84.923 20.960 1.00 48.45 C ATOM 3689 CD1 ILE E 88 10.260 -85.044 20.118 1.00 47.18 C ATOM 3690 N LEU E 89 10.575 -84.795 24.957 1.00 47.58 N ATOM 3691 CA LEU E 89 9.580 -84.293 25.892 1.00 49.38 C ATOM 3692 C LEU E 89 10.140 -84.094 27.294 1.00 52.18 C ATOM 3693 O LEU E 89 9.389 -83.729 28.203 1.00 54.63 O ATOM 3694 CB LEU E 89 8.379 -85.245 25.948 1.00 47.88 C ATOM 3695 CG LEU E 89 7.606 -85.402 24.636 1.00 53.42 C ATOM 3696 CD1 LEU E 89 6.544 -86.484 24.757 1.00 53.17 C ATOM 3697 CD2 LEU E 89 6.982 -84.078 24.226 1.00 50.81 C ATOM 3698 N ARG E 90 11.438 -84.324 27.490 1.00 57.66 N ATOM 3699 CA ARG E 90 12.060 -84.130 28.796 1.00 54.20 C ATOM 3700 C ARG E 90 13.434 -83.487 28.666 1.00 51.55 C ATOM 3701 O ARG E 90 13.548 -82.264 28.529 1.00 59.63 O ATOM 3702 CB ARG E 90 12.183 -85.462 29.542 1.00 63.86 C ATOM 3703 CG ARG E 90 10.864 -86.077 29.982 1.00 73.72 C ATOM 3704 CD ARG E 90 10.502 -87.273 29.119 1.00 67.65 C ATOM 3705 NE ARG E 90 11.602 -88.231 29.027 1.00 71.36 N ATOM 3706 CZ ARG E 90 11.875 -89.147 29.951 1.00 74.82 C ATOM 3707 NH1 ARG E 90 11.127 -89.236 31.043 1.00 68.87 N1+ ATOM 3708 NH2 ARG E 90 12.895 -89.977 29.782 1.00 74.25 N ATOM 3709 N SER E 91 14.485 -84.310 28.708 1.00 52.47 N ATOM 3710 CA SER E 91 15.841 -83.779 28.757 1.00 53.92 C ATOM 3711 C SER E 91 16.273 -83.211 27.410 1.00 46.56 C ATOM 3712 O SER E 91 16.998 -82.213 27.359 1.00 54.89 O ATOM 3713 CB SER E 91 16.812 -84.867 29.215 1.00 52.18 C ATOM 3714 OG SER E 91 16.734 -86.002 28.371 1.00 55.53 O ATOM 3715 N GLN E 92 15.843 -83.832 26.314 1.00 47.00 N ATOM 3716 CA GLN E 92 16.228 -83.398 24.976 1.00 49.90 C ATOM 3717 C GLN E 92 15.261 -82.381 24.385 1.00 45.05 C ATOM 3718 O GLN E 92 15.196 -82.239 23.157 1.00 45.58 O ATOM 3719 CB GLN E 92 16.361 -84.609 24.050 1.00 46.48 C ATOM 3720 CG GLN E 92 17.488 -85.545 24.441 1.00 52.37 C ATOM 3721 CD GLN E 92 18.843 -84.866 24.402 1.00 56.20 C ATOM 3722 OE1 GLN E 92 19.397 -84.611 23.332 1.00 48.73 O ATOM 3723 NE2 GLN E 92 19.388 -84.569 25.578 1.00 50.10 N ATOM 3724 N TRP E 93 14.510 -81.669 25.223 1.00 51.99 N ATOM 3725 CA TRP E 93 13.591 -80.656 24.730 1.00 43.20 C ATOM 3726 C TRP E 93 14.352 -79.437 24.222 1.00 38.76 C ATOM 3727 O TRP E 93 15.386 -79.052 24.774 1.00 39.87 O ATOM 3728 CB TRP E 93 12.618 -80.244 25.835 1.00 47.42 C ATOM 3729 CG TRP E 93 11.863 -78.986 25.532 1.00 41.57 C ATOM 3730 CD1 TRP E 93 12.053 -77.764 26.106 1.00 45.33 C ATOM 3731 CD2 TRP E 93 10.809 -78.824 24.576 1.00 40.43 C ATOM 3732 NE1 TRP E 93 11.177 -76.850 25.571 1.00 42.94 N ATOM 3733 CE2 TRP E 93 10.402 -77.474 24.630 1.00 39.13 C ATOM 3734 CE3 TRP E 93 10.164 -79.685 23.685 1.00 40.94 C ATOM 3735 CZ2 TRP E 93 9.384 -76.967 23.827 1.00 41.95 C ATOM 3736 CZ3 TRP E 93 9.155 -79.178 22.887 1.00 43.65 C ATOM 3737 CH2 TRP E 93 8.774 -77.836 22.964 1.00 41.52 C ATOM 3738 N SER E 94 13.834 -78.829 23.155 1.00 45.16 N ATOM 3739 CA SER E 94 14.389 -77.600 22.614 1.00 45.60 C ATOM 3740 C SER E 94 13.281 -76.556 22.513 1.00 39.57 C ATOM 3741 O SER E 94 12.189 -76.862 22.007 1.00 44.15 O ATOM 3742 CB SER E 94 15.026 -77.831 21.239 1.00 42.10 C ATOM 3743 OG SER E 94 15.345 -76.596 20.622 1.00 39.39 O ATOM 3744 N PRO E 95 13.516 -75.325 22.975 1.00 39.03 N ATOM 3745 CA PRO E 95 12.480 -74.287 22.830 1.00 39.97 C ATOM 3746 C PRO E 95 12.182 -73.932 21.383 1.00 42.92 C ATOM 3747 O PRO E 95 11.126 -73.349 21.112 1.00 46.38 O ATOM 3748 CB PRO E 95 13.071 -73.093 23.593 1.00 38.82 C ATOM 3749 CG PRO E 95 14.538 -73.341 23.622 1.00 41.75 C ATOM 3750 CD PRO E 95 14.701 -74.831 23.692 1.00 41.44 C ATOM 3751 N ALA E 96 13.068 -74.269 20.444 1.00 33.78 N ATOM 3752 CA ALA E 96 12.799 -74.038 19.030 1.00 38.15 C ATOM 3753 C ALA E 96 11.824 -75.053 18.446 1.00 43.23 C ATOM 3754 O ALA E 96 11.382 -74.876 17.306 1.00 45.71 O ATOM 3755 CB ALA E 96 14.099 -74.055 18.229 1.00 40.48 C ATOM 3756 N LEU E 97 11.483 -76.099 19.190 1.00 42.81 N ATOM 3757 CA LEU E 97 10.489 -77.058 18.731 1.00 39.11 C ATOM 3758 C LEU E 97 9.088 -76.471 18.864 1.00 49.50 C ATOM 3759 O LEU E 97 8.763 -75.812 19.857 1.00 45.98 O ATOM 3760 CB LEU E 97 10.592 -78.359 19.531 1.00 40.76 C ATOM 3761 CG LEU E 97 11.680 -79.356 19.129 1.00 48.92 C ATOM 3762 CD1 LEU E 97 11.790 -80.478 20.154 1.00 37.44 C ATOM 3763 CD2 LEU E 97 11.404 -79.924 17.742 1.00 40.30 C ATOM 3764 N THR E 98 8.262 -76.710 17.852 1.00 46.50 N ATOM 3765 CA THR E 98 6.867 -76.306 17.864 1.00 46.33 C ATOM 3766 C THR E 98 5.982 -77.534 18.016 1.00 56.10 C ATOM 3767 O THR E 98 6.422 -78.671 17.815 1.00 49.32 O ATOM 3768 CB THR E 98 6.494 -75.548 16.584 1.00 50.73 C ATOM 3769 OG1 THR E 98 6.706 -76.392 15.446 1.00 50.39 O ATOM 3770 CG2 THR E 98 7.343 -74.291 16.441 1.00 47.37 C ATOM 3771 N VAL E 99 4.722 -77.289 18.382 1.00 46.29 N ATOM 3772 CA VAL E 99 3.779 -78.384 18.597 1.00 48.73 C ATOM 3773 C VAL E 99 3.604 -79.197 17.322 1.00 46.07 C ATOM 3774 O VAL E 99 3.491 -80.427 17.365 1.00 50.58 O ATOM 3775 CB VAL E 99 2.436 -77.834 19.113 1.00 50.03 C ATOM 3776 CG1 VAL E 99 1.401 -78.947 19.208 1.00 47.09 C ATOM 3777 CG2 VAL E 99 2.634 -77.177 20.461 1.00 49.51 C ATOM 3778 N SER E 100 3.587 -78.528 16.167 1.00 48.18 N ATOM 3779 CA SER E 100 3.503 -79.247 14.903 1.00 50.62 C ATOM 3780 C SER E 100 4.707 -80.157 14.708 1.00 46.17 C ATOM 3781 O SER E 100 4.565 -81.293 14.240 1.00 50.32 O ATOM 3782 CB SER E 100 3.383 -78.260 13.739 1.00 58.58 C ATOM 3783 OG SER E 100 3.296 -78.940 12.499 1.00 58.98 O ATOM 3784 N LYS E 101 5.901 -79.683 15.078 1.00 49.16 N ATOM 3785 CA LYS E 101 7.099 -80.506 14.937 1.00 47.41 C ATOM 3786 C LYS E 101 7.089 -81.670 15.919 1.00 44.30 C ATOM 3787 O LYS E 101 7.501 -82.784 15.572 1.00 40.49 O ATOM 3788 CB LYS E 101 8.351 -79.651 15.131 1.00 37.72 C ATOM 3789 CG LYS E 101 8.631 -78.700 13.988 1.00 44.99 C ATOM 3790 CD LYS E 101 8.897 -79.460 12.701 1.00 43.89 C ATOM 3791 CE LYS E 101 9.322 -78.521 11.585 1.00 52.67 C ATOM 3792 NZ LYS E 101 9.679 -79.262 10.345 1.00 46.67 N1+ ATOM 3793 N VAL E 102 6.617 -81.434 17.144 1.00 47.32 N ATOM 3794 CA VAL E 102 6.572 -82.501 18.139 1.00 43.20 C ATOM 3795 C VAL E 102 5.572 -83.575 17.730 1.00 44.29 C ATOM 3796 O VAL E 102 5.865 -84.773 17.814 1.00 52.62 O ATOM 3797 CB VAL E 102 6.247 -81.924 19.529 1.00 49.69 C ATOM 3798 CG1 VAL E 102 6.133 -83.043 20.551 1.00 44.03 C ATOM 3799 CG2 VAL E 102 7.311 -80.926 19.946 1.00 47.30 C ATOM 3800 N LEU E 103 4.380 -83.172 17.283 1.00 50.62 N ATOM 3801 CA LEU E 103 3.379 -84.150 16.858 1.00 47.09 C ATOM 3802 C LEU E 103 3.880 -84.967 15.676 1.00 46.02 C ATOM 3803 O LEU E 103 3.609 -86.172 15.584 1.00 46.13 O ATOM 3804 CB LEU E 103 2.072 -83.444 16.501 1.00 46.87 C ATOM 3805 CG LEU E 103 1.289 -82.840 17.668 1.00 56.60 C ATOM 3806 CD1 LEU E 103 0.021 -82.162 17.169 1.00 59.88 C ATOM 3807 CD2 LEU E 103 0.962 -83.915 18.692 1.00 52.52 C ATOM 3808 N LEU E 104 4.611 -84.332 14.763 1.00 45.96 N ATOM 3809 CA LEU E 104 5.203 -85.070 13.656 1.00 47.63 C ATOM 3810 C LEU E 104 6.327 -85.972 14.142 1.00 44.91 C ATOM 3811 O LEU E 104 6.519 -87.071 13.606 1.00 47.81 O ATOM 3812 CB LEU E 104 5.709 -84.101 12.592 1.00 48.47 C ATOM 3813 CG LEU E 104 6.351 -84.719 11.352 1.00 46.15 C ATOM 3814 CD1 LEU E 104 5.384 -85.659 10.657 1.00 43.45 C ATOM 3815 CD2 LEU E 104 6.797 -83.613 10.417 1.00 54.08 C ATOM 3816 N SER E 105 7.073 -85.530 15.156 1.00 47.99 N ATOM 3817 CA SER E 105 8.087 -86.385 15.764 1.00 40.58 C ATOM 3818 C SER E 105 7.452 -87.615 16.403 1.00 45.35 C ATOM 3819 O SER E 105 7.984 -88.724 16.298 1.00 46.21 O ATOM 3820 CB SER E 105 8.888 -85.593 16.793 1.00 44.09 C ATOM 3821 OG SER E 105 9.565 -84.507 16.183 1.00 48.29 O ATOM 3822 N ILE E 106 6.312 -87.433 17.073 1.00 44.78 N ATOM 3823 CA ILE E 106 5.609 -88.562 17.682 1.00 41.56 C ATOM 3824 C ILE E 106 5.112 -89.520 16.615 1.00 47.77 C ATOM 3825 O ILE E 106 5.074 -90.738 16.830 1.00 49.05 O ATOM 3826 CB ILE E 106 4.460 -88.052 18.577 1.00 40.97 C ATOM 3827 CG1 ILE E 106 5.019 -87.193 19.714 1.00 46.17 C ATOM 3828 CG2 ILE E 106 3.664 -89.212 19.153 1.00 40.28 C ATOM 3829 CD1 ILE E 106 3.960 -86.621 20.624 1.00 44.68 C ATOM 3830 N CYS E 107 4.738 -89.000 15.443 1.00 46.40 N ATOM 3831 CA ACYS E 107 4.298 -89.870 14.358 0.52 47.95 C ATOM 3832 CA BCYS E 107 4.295 -89.869 14.360 0.48 48.16 C ATOM 3833 C CYS E 107 5.401 -90.831 13.936 1.00 41.54 C ATOM 3834 O CYS E 107 5.156 -92.028 13.748 1.00 44.22 O ATOM 3835 CB ACYS E 107 3.827 -89.035 13.167 0.52 50.38 C ATOM 3836 CB BCYS E 107 3.824 -89.029 13.173 0.48 49.84 C ATOM 3837 SG ACYS E 107 2.300 -88.107 13.450 0.52 48.77 S ATOM 3838 SG BCYS E 107 3.052 -89.974 11.844 0.48 51.32 S ATOM 3839 N SER E 108 6.632 -90.323 13.790 1.00 46.58 N ATOM 3840 CA SER E 108 7.749 -91.173 13.391 1.00 46.14 C ATOM 3841 C SER E 108 8.159 -92.144 14.490 1.00 54.88 C ATOM 3842 O SER E 108 8.861 -93.122 14.207 1.00 40.90 O ATOM 3843 CB SER E 108 8.947 -90.316 12.989 1.00 47.53 C ATOM 3844 OG SER E 108 9.440 -89.585 14.097 1.00 45.47 O ATOM 3845 N LEU E 109 7.747 -91.890 15.735 1.00 54.79 N ATOM 3846 CA LEU E 109 8.053 -92.810 16.823 1.00 47.79 C ATOM 3847 C LEU E 109 7.285 -94.118 16.683 1.00 51.62 C ATOM 3848 O LEU E 109 7.751 -95.163 17.152 1.00 52.16 O ATOM 3849 CB LEU E 109 7.749 -92.147 18.166 1.00 45.98 C ATOM 3850 CG LEU E 109 7.918 -92.965 19.446 1.00 53.44 C ATOM 3851 CD1 LEU E 109 9.357 -93.426 19.607 1.00 43.19 C ATOM 3852 CD2 LEU E 109 7.463 -92.165 20.661 1.00 48.04 C ATOM 3853 N LEU E 110 6.122 -94.084 16.027 1.00 54.50 N ATOM 3854 CA LEU E 110 5.271 -95.269 15.952 1.00 50.93 C ATOM 3855 C LEU E 110 5.963 -96.409 15.216 1.00 49.15 C ATOM 3856 O LEU E 110 5.884 -97.568 15.640 1.00 58.57 O ATOM 3857 CB LEU E 110 3.948 -94.920 15.276 1.00 51.01 C ATOM 3858 CG LEU E 110 3.183 -93.754 15.904 1.00 49.98 C ATOM 3859 CD1 LEU E 110 1.842 -93.557 15.215 1.00 56.62 C ATOM 3860 CD2 LEU E 110 2.996 -93.980 17.394 1.00 50.93 C ATOM 3861 N CYS E 111 6.651 -96.105 14.117 1.00 52.42 N ATOM 3862 CA CYS E 111 7.344 -97.117 13.332 1.00 52.84 C ATOM 3863 C CYS E 111 8.819 -97.232 13.691 1.00 54.34 C ATOM 3864 O CYS E 111 9.551 -97.973 13.026 1.00 58.08 O ATOM 3865 CB CYS E 111 7.194 -96.820 11.842 1.00 60.10 C ATOM 3866 SG CYS E 111 5.486 -96.733 11.314 1.00 70.42 S ATOM 3867 N ASP E 112 9.271 -96.519 14.716 1.00 55.12 N ATOM 3868 CA ASP E 112 10.653 -96.599 15.184 1.00 53.27 C ATOM 3869 C ASP E 112 10.651 -96.567 16.706 1.00 56.37 C ATOM 3870 O ASP E 112 11.047 -95.574 17.326 1.00 56.23 O ATOM 3871 CB ASP E 112 11.495 -95.464 14.599 1.00 54.17 C ATOM 3872 CG ASP E 112 12.953 -95.545 15.001 1.00 62.83 C ATOM 3873 OD1 ASP E 112 13.451 -96.673 15.209 1.00 63.35 O ATOM 3874 OD2 ASP E 112 13.596 -94.479 15.111 1.00 57.61 O1- ATOM 3875 N PRO E 113 10.201 -97.641 17.344 1.00 53.34 N ATOM 3876 CA PRO E 113 10.208 -97.694 18.807 1.00 52.77 C ATOM 3877 C PRO E 113 11.576 -98.091 19.339 1.00 53.09 C ATOM 3878 O PRO E 113 12.460 -98.539 18.606 1.00 57.06 O ATOM 3879 CB PRO E 113 9.157 -98.763 19.118 1.00 50.34 C ATOM 3880 CG PRO E 113 9.261 -99.700 17.959 1.00 54.91 C ATOM 3881 CD PRO E 113 9.618 -98.862 16.754 1.00 47.94 C ATOM 3882 N ASN E 114 11.739 -97.913 20.649 1.00 56.97 N ATOM 3883 CA ASN E 114 12.956 -98.312 21.349 1.00 51.77 C ATOM 3884 C ASN E 114 12.612 -99.450 22.298 1.00 59.97 C ATOM 3885 O ASN E 114 12.299 -99.215 23.475 1.00 60.85 O ATOM 3886 CB ASN E 114 13.567 -97.132 22.109 1.00 53.09 C ATOM 3887 CG ASN E 114 14.895 -97.480 22.753 1.00 60.80 C ATOM 3888 OD1 ASN E 114 15.487 -98.519 22.466 1.00 59.45 O ATOM 3889 ND2 ASN E 114 15.375 -96.599 23.627 1.00 59.63 N ATOM 3890 N PRO E 115 12.647-100.705 21.840 1.00 62.96 N ATOM 3891 CA PRO E 115 12.300-101.829 22.721 1.00 61.94 C ATOM 3892 C PRO E 115 13.365-102.172 23.747 1.00 59.08 C ATOM 3893 O PRO E 115 13.107-103.009 24.622 1.00 64.55 O ATOM 3894 CB PRO E 115 12.101-102.987 21.734 1.00 62.68 C ATOM 3895 CG PRO E 115 13.021-102.652 20.605 1.00 56.82 C ATOM 3896 CD PRO E 115 13.005-101.152 20.483 1.00 57.14 C ATOM 3897 N ASP E 116 14.552-101.562 23.665 1.00 62.48 N ATOM 3898 CA ASP E 116 15.622-101.883 24.603 1.00 63.24 C ATOM 3899 C ASP E 116 15.479-101.138 25.925 1.00 63.59 C ATOM 3900 O ASP E 116 15.887-101.661 26.968 1.00 62.90 O ATOM 3901 CB ASP E 116 16.978-101.575 23.961 1.00 63.44 C ATOM 3902 CG ASP E 116 17.184-102.320 22.658 1.00 72.81 C ATOM 3903 OD1 ASP E 116 16.755-103.489 22.569 1.00 79.51 O ATOM 3904 OD2 ASP E 116 17.766-101.732 21.719 1.00 76.05 O1- ATOM 3905 N ASP E 117 14.915 -99.930 25.904 1.00 65.61 N ATOM 3906 CA ASP E 117 14.567 -99.179 27.112 1.00 65.46 C ATOM 3907 C ASP E 117 13.084 -98.844 27.021 1.00 59.56 C ATOM 3908 O ASP E 117 12.710 -97.734 26.616 1.00 59.74 O ATOM 3909 CB ASP E 117 15.416 -97.916 27.262 1.00 55.41 C ATOM 3910 CG ASP E 117 15.056 -97.117 28.503 1.00 70.19 C ATOM 3911 OD1 ASP E 117 14.604 -97.727 29.495 1.00 65.52 O ATOM 3912 OD2 ASP E 117 15.220 -95.878 28.479 1.00 79.28 O1- ATOM 3913 N PRO E 118 12.207 -99.783 27.382 1.00 58.08 N ATOM 3914 CA PRO E 118 10.778 -99.597 27.103 1.00 56.54 C ATOM 3915 C PRO E 118 9.984 -99.029 28.266 1.00 51.76 C ATOM 3916 O PRO E 118 10.429 -99.054 29.417 1.00 53.32 O ATOM 3917 CB PRO E 118 10.322-101.020 26.772 1.00 58.48 C ATOM 3918 CG PRO E 118 11.173-101.873 27.667 1.00 52.45 C ATOM 3919 CD PRO E 118 12.502-101.153 27.837 1.00 52.42 C ATOM 3920 N LEU E 119 8.790 -98.523 27.962 1.00 55.45 N ATOM 3921 CA LEU E 119 7.824 -98.141 28.983 1.00 51.09 C ATOM 3922 C LEU E 119 6.873 -99.282 29.322 1.00 53.87 C ATOM 3923 O LEU E 119 6.439 -99.397 30.473 1.00 54.05 O ATOM 3924 CB LEU E 119 7.033 -96.914 28.524 1.00 47.23 C ATOM 3925 CG LEU E 119 6.032 -96.308 29.512 1.00 52.12 C ATOM 3926 CD1 LEU E 119 6.710 -95.970 30.829 1.00 39.64 C ATOM 3927 CD2 LEU E 119 5.377 -95.073 28.913 1.00 53.99 C ATOM 3928 N VAL E 120 6.548-100.124 28.346 1.00 51.91 N ATOM 3929 CA VAL E 120 5.757-101.330 28.551 1.00 52.39 C ATOM 3930 C VAL E 120 6.655-102.528 28.247 1.00 53.66 C ATOM 3931 O VAL E 120 6.927-102.811 27.070 1.00 54.75 O ATOM 3932 CB VAL E 120 4.500-101.342 27.670 1.00 55.97 C ATOM 3933 CG1 VAL E 120 3.576-102.476 28.095 1.00 46.65 C ATOM 3934 CG2 VAL E 120 3.790-100.001 27.742 1.00 49.36 C ATOM 3935 N PRO E 121 7.134-103.255 29.261 1.00 53.44 N ATOM 3936 CA PRO E 121 8.123-104.308 28.987 1.00 57.34 C ATOM 3937 C PRO E 121 7.575-105.471 28.178 1.00 55.91 C ATOM 3938 O PRO E 121 8.270-105.980 27.292 1.00 55.06 O ATOM 3939 CB PRO E 121 8.559-104.751 30.395 1.00 59.99 C ATOM 3940 CG PRO E 121 8.150-103.631 31.304 1.00 56.01 C ATOM 3941 CD PRO E 121 6.906-103.069 30.702 1.00 55.40 C ATOM 3942 N ASP E 122 6.344-105.913 28.459 1.00 54.72 N ATOM 3943 CA ASP E 122 5.814-107.087 27.770 1.00 60.34 C ATOM 3944 C ASP E 122 5.553-106.807 26.295 1.00 55.67 C ATOM 3945 O ASP E 122 5.701-107.707 25.463 1.00 56.44 O ATOM 3946 CB ASP E 122 4.540-107.575 28.457 1.00 56.79 C ATOM 3947 CG ASP E 122 3.462-106.511 28.510 1.00 68.60 C ATOM 3948 OD1 ASP E 122 3.544-105.627 29.392 1.00 76.79 O ATOM 3949 OD2 ASP E 122 2.534-106.559 27.683 1.00 69.92 O1- ATOM 3950 N ILE E 123 5.166-105.576 25.951 1.00 59.05 N ATOM 3951 CA ILE E 123 4.992-105.223 24.546 1.00 53.37 C ATOM 3952 C ILE E 123 6.339-105.186 23.833 1.00 55.69 C ATOM 3953 O ILE E 123 6.468-105.653 22.696 1.00 55.04 O ATOM 3954 CB ILE E 123 4.240-103.882 24.416 1.00 54.41 C ATOM 3955 CG1 ILE E 123 2.792-104.037 24.881 1.00 52.26 C ATOM 3956 CG2 ILE E 123 4.289-103.368 22.990 1.00 46.99 C ATOM 3957 CD1 ILE E 123 1.979-102.776 24.762 1.00 50.55 C ATOM 3958 N ALA E 124 7.363-104.645 24.497 1.00 58.20 N ATOM 3959 CA ALA E 124 8.699-104.635 23.911 1.00 55.71 C ATOM 3960 C ALA E 124 9.258-106.042 23.757 1.00 56.18 C ATOM 3961 O ALA E 124 9.997-106.314 22.805 1.00 59.83 O ATOM 3962 CB ALA E 124 9.641-103.790 24.765 1.00 53.49 C ATOM 3963 N GLN E 125 8.925-106.945 24.682 1.00 58.87 N ATOM 3964 CA GLN E 125 9.400-108.322 24.579 1.00 60.34 C ATOM 3965 C GLN E 125 8.830-109.008 23.344 1.00 53.42 C ATOM 3966 O GLN E 125 9.546-109.726 22.638 1.00 57.53 O ATOM 3967 CB GLN E 125 9.039-109.096 25.848 1.00 57.74 C ATOM 3968 CG GLN E 125 9.309-110.586 25.770 1.00 59.72 C ATOM 3969 CD GLN E 125 10.763-110.907 25.499 1.00 58.94 C ATOM 3970 OE1 GLN E 125 11.656-110.136 25.850 1.00 64.27 O ATOM 3971 NE2 GLN E 125 11.008-112.051 24.869 1.00 69.92 N ATOM 3972 N ILE E 126 7.542-108.794 23.064 1.00 53.96 N ATOM 3973 CA ILE E 126 6.935-109.353 21.860 1.00 61.39 C ATOM 3974 C ILE E 126 7.574-108.751 20.613 1.00 62.45 C ATOM 3975 O ILE E 126 7.784-109.443 19.609 1.00 60.48 O ATOM 3976 CB ILE E 126 5.409-109.139 21.877 1.00 57.35 C ATOM 3977 CG1 ILE E 126 4.770-109.964 22.997 1.00 54.81 C ATOM 3978 CG2 ILE E 126 4.789-109.495 20.534 1.00 55.25 C ATOM 3979 CD1 ILE E 126 3.257-109.882 23.031 1.00 57.51 C ATOM 3980 N TYR E 127 7.906-107.456 20.664 1.00 61.67 N ATOM 3981 CA TYR E 127 8.532-106.790 19.525 1.00 59.76 C ATOM 3982 C TYR E 127 9.876-107.411 19.168 1.00 58.84 C ATOM 3983 O TYR E 127 10.241-107.463 17.988 1.00 60.73 O ATOM 3984 CB TYR E 127 8.701-105.298 19.826 1.00 58.52 C ATOM 3985 CG TYR E 127 9.259-104.475 18.684 1.00 62.02 C ATOM 3986 CD1 TYR E 127 10.629-104.286 18.534 1.00 62.23 C ATOM 3987 CD2 TYR E 127 8.415-103.877 17.759 1.00 61.20 C ATOM 3988 CE1 TYR E 127 11.140-103.533 17.494 1.00 62.46 C ATOM 3989 CE2 TYR E 127 8.916-103.123 16.714 1.00 58.46 C ATOM 3990 CZ TYR E 127 10.279-102.952 16.586 1.00 63.73 C ATOM 3991 OH TYR E 127 10.778-102.200 15.546 1.00 67.02 O ATOM 3992 N LYS E 128 10.623-107.890 20.166 1.00 57.07 N ATOM 3993 CA LYS E 128 11.959-108.425 19.941 1.00 63.93 C ATOM 3994 C LYS E 128 11.952-109.900 19.546 1.00 63.51 C ATOM 3995 O LYS E 128 12.780-110.324 18.731 1.00 65.92 O ATOM 3996 CB LYS E 128 12.817-108.233 21.196 1.00 60.25 C ATOM 3997 CG LYS E 128 13.027-106.781 21.584 1.00 57.83 C ATOM 3998 CD LYS E 128 13.757-106.665 22.910 1.00 69.90 C ATOM 3999 CE LYS E 128 15.102-107.371 22.866 1.00 78.97 C ATOM 4000 NZ LYS E 128 16.010-106.781 21.843 1.00 77.96 N1+ ATOM 4001 N SER E 129 11.041-110.694 20.109 1.00 57.48 N ATOM 4002 CA SER E 129 11.020-112.132 19.863 1.00 61.96 C ATOM 4003 C SER E 129 10.043-112.553 18.773 1.00 63.96 C ATOM 4004 O SER E 129 10.179-113.660 18.244 1.00 66.77 O ATOM 4005 CB SER E 129 10.676-112.884 21.156 1.00 66.88 C ATOM 4006 OG SER E 129 9.451-112.430 21.702 1.00 69.46 O ATOM 4007 N ASP E 130 9.073-111.711 18.428 1.00 66.90 N ATOM 4008 CA ASP E 130 8.122-112.041 17.375 1.00 66.68 C ATOM 4009 C ASP E 130 7.470-110.775 16.829 1.00 64.01 C ATOM 4010 O ASP E 130 6.365-110.410 17.237 1.00 63.26 O ATOM 4011 CB ASP E 130 7.058-113.009 17.902 1.00 63.64 C ATOM 4012 CG ASP E 130 6.249-113.650 16.793 1.00 70.52 C ATOM 4013 OD1 ASP E 130 6.673-113.569 15.619 1.00 75.66 O ATOM 4014 OD2 ASP E 130 5.195-114.249 17.095 1.00 77.87 O1- ATOM 4015 N LYS E 131 8.157-110.095 15.902 1.00 59.92 N ATOM 4016 CA LYS E 131 7.655-108.823 15.396 1.00 64.55 C ATOM 4017 C LYS E 131 6.376-109.000 14.589 1.00 66.80 C ATOM 4018 O LYS E 131 5.552-108.079 14.529 1.00 63.24 O ATOM 4019 CB LYS E 131 8.732-108.129 14.558 1.00 57.76 C ATOM 4020 CG LYS E 131 8.449-106.663 14.282 1.00 64.02 C ATOM 4021 CD LYS E 131 9.612-105.995 13.574 1.00 65.67 C ATOM 4022 CE LYS E 131 9.358-104.513 13.363 1.00 64.96 C ATOM 4023 NZ LYS E 131 10.488-103.860 12.641 1.00 68.60 N1+ ATOM 4024 N GLU E 132 6.186-110.170 13.975 1.00 64.91 N ATOM 4025 CA GLU E 132 4.952-110.435 13.242 1.00 63.80 C ATOM 4026 C GLU E 132 3.758-110.447 14.188 1.00 63.22 C ATOM 4027 O GLU E 132 2.713-109.850 13.902 1.00 62.48 O ATOM 4028 CB GLU E 132 5.063-111.760 12.491 1.00 68.43 C ATOM 4029 CG GLU E 132 6.419-111.981 11.846 1.00 78.89 C ATOM 4030 CD GLU E 132 6.809-110.850 10.914 1.00 84.64 C ATOM 4031 OE1 GLU E 132 6.109-110.649 9.900 1.00 89.44 O ATOM 4032 OE2 GLU E 132 7.809-110.159 11.202 1.00 89.17 O1- ATOM 4033 N LYS E 133 3.896-111.134 15.324 1.00 60.40 N ATOM 4034 CA LYS E 133 2.856-111.099 16.344 1.00 62.95 C ATOM 4035 C LYS E 133 2.663-109.686 16.884 1.00 62.95 C ATOM 4036 O LYS E 133 1.539-109.291 17.211 1.00 61.70 O ATOM 4037 CB LYS E 133 3.206-112.066 17.473 1.00 65.07 C ATOM 4038 CG LYS E 133 2.133-112.228 18.537 1.00 67.10 C ATOM 4039 CD LYS E 133 2.477-113.375 19.477 1.00 69.90 C ATOM 4040 CE LYS E 133 1.401-113.570 20.535 1.00 72.18 C ATOM 4041 NZ LYS E 133 1.334-112.418 21.479 1.00 68.53 N1+ ATOM 4042 N TYR E 134 3.750-108.917 16.975 1.00 65.33 N ATOM 4043 CA TYR E 134 3.647-107.522 17.398 1.00 59.56 C ATOM 4044 C TYR E 134 2.847-106.707 16.391 1.00 59.36 C ATOM 4045 O TYR E 134 1.977-105.914 16.772 1.00 61.18 O ATOM 4046 CB TYR E 134 5.047-106.934 17.577 1.00 59.29 C ATOM 4047 CG TYR E 134 5.090-105.441 17.826 1.00 56.88 C ATOM 4048 CD1 TYR E 134 5.039-104.929 19.118 1.00 61.62 C ATOM 4049 CD2 TYR E 134 5.201-104.546 16.767 1.00 60.72 C ATOM 4050 CE1 TYR E 134 5.087-103.568 19.345 1.00 59.36 C ATOM 4051 CE2 TYR E 134 5.244-103.190 16.985 1.00 57.11 C ATOM 4052 CZ TYR E 134 5.195-102.708 18.273 1.00 61.30 C ATOM 4053 OH TYR E 134 5.248-101.352 18.480 1.00 54.86 O ATOM 4054 N ASN E 135 3.133-106.887 15.098 1.00 57.57 N ATOM 4055 CA ASN E 135 2.431-106.127 14.071 1.00 59.65 C ATOM 4056 C ASN E 135 0.939-106.417 14.086 1.00 60.51 C ATOM 4057 O ASN E 135 0.119-105.496 13.988 1.00 59.49 O ATOM 4058 CB ASN E 135 3.025-106.425 12.695 1.00 57.92 C ATOM 4059 CG ASN E 135 4.369-105.767 12.485 1.00 60.69 C ATOM 4060 OD1 ASN E 135 4.614-104.667 12.980 1.00 60.42 O ATOM 4061 ND2 ASN E 135 5.256-106.437 11.756 1.00 65.40 N ATOM 4062 N ARG E 136 0.565-107.691 14.213 1.00 60.19 N ATOM 4063 CA ARG E 136 -0.854-108.040 14.223 1.00 55.19 C ATOM 4064 C ARG E 136 -1.547-107.480 15.458 1.00 56.63 C ATOM 4065 O ARG E 136 -2.700-107.035 15.381 1.00 60.05 O ATOM 4066 CB ARG E 136 -1.025-109.554 14.148 1.00 62.09 C ATOM 4067 CG ARG E 136 -0.352-110.188 12.944 1.00 63.90 C ATOM 4068 CD ARG E 136 -0.942-111.553 12.644 1.00 68.52 C ATOM 4069 NE ARG E 136 -1.002-112.397 13.830 1.00 59.95 N ATOM 4070 CZ ARG E 136 -0.019-113.209 14.220 1.00 70.06 C ATOM 4071 NH1 ARG E 136 1.103-113.282 13.520 1.00 67.95 N1+ ATOM 4072 NH2 ARG E 136 -0.163-113.944 15.317 1.00 74.06 N ATOM 4073 N HIS E 137 -0.868-107.494 16.607 1.00 56.92 N ATOM 4074 CA HIS E 137 -1.445-106.904 17.809 1.00 65.58 C ATOM 4075 C HIS E 137 -1.659-105.405 17.634 1.00 60.43 C ATOM 4076 O HIS E 137 -2.693-104.865 18.044 1.00 65.51 O ATOM 4077 CB HIS E 137 -0.551-107.179 19.021 1.00 66.39 C ATOM 4078 CG HIS E 137 -0.720-108.548 19.598 1.00 69.26 C ATOM 4079 ND1 HIS E 137 -1.825-109.335 19.349 1.00 70.13 N ATOM 4080 CD2 HIS E 137 0.076-109.273 20.423 1.00 61.80 C ATOM 4081 CE1 HIS E 137 -1.699-110.483 19.991 1.00 72.89 C ATOM 4082 NE2 HIS E 137 -0.557-110.469 20.651 1.00 68.16 N ATOM 4083 N ALA E 138 -0.691-104.719 17.019 1.00 59.25 N ATOM 4084 CA ALA E 138 -0.846-103.288 16.785 1.00 61.34 C ATOM 4085 C ALA E 138 -1.876-103.017 15.695 1.00 60.57 C ATOM 4086 O ALA E 138 -2.646-102.055 15.795 1.00 61.41 O ATOM 4087 CB ALA E 138 0.504-102.665 16.428 1.00 54.31 C ATOM 4088 N ARG E 139 -1.907-103.851 14.652 1.00 61.78 N ATOM 4089 CA ARG E 139 -2.948-103.727 13.633 1.00 57.08 C ATOM 4090 C ARG E 139 -4.332-103.928 14.235 1.00 63.94 C ATOM 4091 O ARG E 139 -5.272-103.192 13.910 1.00 68.28 O ATOM 4092 CB ARG E 139 -2.719-104.730 12.499 1.00 61.79 C ATOM 4093 CG ARG E 139 -1.547-104.409 11.592 1.00 67.18 C ATOM 4094 CD ARG E 139 -1.499-105.331 10.382 1.00 63.76 C ATOM 4095 NE ARG E 139 -2.629-105.106 9.486 1.00 81.79 N ATOM 4096 CZ ARG E 139 -2.639-104.208 8.510 1.00 88.06 C ATOM 4097 NH1 ARG E 139 -1.575-103.441 8.296 1.00 72.09 N1+ ATOM 4098 NH2 ARG E 139 -3.712-104.069 7.743 1.00 83.58 N ATOM 4099 N GLU E 140 -4.475-104.920 15.116 1.00 65.37 N ATOM 4100 CA GLU E 140 -5.764-105.168 15.747 1.00 60.61 C ATOM 4101 C GLU E 140 -6.176-104.002 16.640 1.00 66.78 C ATOM 4102 O GLU E 140 -7.348-103.600 16.639 1.00 66.95 O ATOM 4103 CB GLU E 140 -5.709-106.469 16.546 1.00 65.85 C ATOM 4104 CG GLU E 140 -6.890-106.678 17.482 1.00 77.40 C ATOM 4105 CD GLU E 140 -6.720-107.892 18.375 1.00 84.68 C ATOM 4106 OE1 GLU E 140 -7.412-108.903 18.146 1.00 89.86 O ATOM 4107 OE2 GLU E 140 -5.882-107.835 19.305 1.00 78.44 O1- ATOM 4108 N TRP E 141 -5.233-103.445 17.403 1.00 65.91 N ATOM 4109 CA TRP E 141 -5.571-102.345 18.304 1.00 62.08 C ATOM 4110 C TRP E 141 -5.975-101.092 17.539 1.00 67.29 C ATOM 4111 O TRP E 141 -6.774-100.293 18.038 1.00 66.66 O ATOM 4112 CB TRP E 141 -4.402-102.039 19.235 1.00 63.11 C ATOM 4113 CG TRP E 141 -4.338-102.940 20.432 1.00 66.88 C ATOM 4114 CD1 TRP E 141 -4.602-104.277 20.468 1.00 67.04 C ATOM 4115 CD2 TRP E 141 -4.009-102.557 21.774 1.00 61.28 C ATOM 4116 NE1 TRP E 141 -4.447-104.754 21.744 1.00 64.20 N ATOM 4117 CE2 TRP E 141 -4.084-103.720 22.568 1.00 64.33 C ATOM 4118 CE3 TRP E 141 -3.652-101.348 22.382 1.00 61.08 C ATOM 4119 CZ2 TRP E 141 -3.815-103.711 23.935 1.00 65.36 C ATOM 4120 CZ3 TRP E 141 -3.385-101.342 23.739 1.00 64.23 C ATOM 4121 CH2 TRP E 141 -3.470-102.515 24.500 1.00 68.69 C ATOM 4122 N THR E 142 -5.436-100.897 16.330 1.00 70.41 N ATOM 4123 CA THR E 142 -5.817 -99.729 15.543 1.00 72.27 C ATOM 4124 C THR E 142 -7.239 -99.857 15.017 1.00 70.62 C ATOM 4125 O THR E 142 -7.977 -98.865 14.959 1.00 71.01 O ATOM 4126 CB THR E 142 -4.831 -99.525 14.395 1.00 70.44 C ATOM 4127 OG1 THR E 142 -4.686-100.748 13.664 1.00 78.32 O ATOM 4128 CG2 THR E 142 -3.476 -99.103 14.931 1.00 57.45 C ATOM 4129 N GLN E 143 -7.649-101.069 14.627 1.00 72.83 N ATOM 4130 CA GLN E 143 -9.032-101.271 14.203 1.00 69.40 C ATOM 4131 C GLN E 143 -10.008-101.057 15.353 1.00 76.53 C ATOM 4132 O GLN E 143 -11.118-100.555 15.138 1.00 79.83 O ATOM 4133 CB GLN E 143 -9.201-102.670 13.610 1.00 65.21 C ATOM 4134 CG GLN E 143 -10.643-103.030 13.270 1.00 83.20 C ATOM 4135 CD GLN E 143 -10.777-104.412 12.670 1.00 84.47 C ATOM 4136 OE1 GLN E 143 -9.838-104.941 12.078 1.00 90.18 O ATOM 4137 NE2 GLN E 143 -11.957-105.010 12.820 1.00 80.79 N ATOM 4138 N LYS E 144 -9.608-101.412 16.575 1.00 73.05 N ATOM 4139 CA LYS E 144 -10.497-101.334 17.725 1.00 67.56 C ATOM 4140 C LYS E 144 -10.380-100.023 18.491 1.00 70.79 C ATOM 4141 O LYS E 144 -11.341 -99.637 19.167 1.00 68.97 O ATOM 4142 CB LYS E 144 -10.221-102.498 18.687 1.00 71.57 C ATOM 4143 CG LYS E 144 -10.905-103.818 18.325 1.00 81.02 C ATOM 4144 CD LYS E 144 -10.382-104.406 17.018 1.00 78.93 C ATOM 4145 CE LYS E 144 -10.918-105.806 16.778 1.00 82.03 C ATOM 4146 NZ LYS E 144 -10.377-106.782 17.761 1.00 75.33 N1+ ATOM 4147 N TYR E 145 -9.239 -99.334 18.396 1.00 66.93 N ATOM 4148 CA TYR E 145 -8.948 -98.155 19.216 1.00 68.50 C ATOM 4149 C TYR E 145 -9.083 -98.459 20.706 1.00 75.57 C ATOM 4150 O TYR E 145 -9.462 -97.590 21.494 1.00 81.77 O ATOM 4151 CB TYR E 145 -9.839 -96.964 18.838 1.00 65.52 C ATOM 4152 CG TYR E 145 -9.518 -96.339 17.503 1.00 73.34 C ATOM 4153 CD1 TYR E 145 -8.267 -96.488 16.925 1.00 71.63 C ATOM 4154 CD2 TYR E 145 -10.474 -95.596 16.820 1.00 80.05 C ATOM 4155 CE1 TYR E 145 -7.973 -95.914 15.704 1.00 75.22 C ATOM 4156 CE2 TYR E 145 -10.193 -95.022 15.596 1.00 70.46 C ATOM 4157 CZ TYR E 145 -8.940 -95.184 15.044 1.00 68.80 C ATOM 4158 OH TYR E 145 -8.655 -94.611 13.827 1.00 73.35 O ATOM 4159 N ALA E 146 -8.775 -99.691 21.102 1.00 69.28 N ATOM 4160 CA ALA E 146 -8.915-100.111 22.490 1.00 68.22 C ATOM 4161 C ALA E 146 -8.075-101.352 22.772 1.00 70.06 C ATOM 4162 O ALA E 146 -8.514-102.259 23.479 1.00 75.19 O ATOM 4163 CB ALA E 146 -10.377-100.375 22.823 1.00 69.43 C TER 4164 ALA E 146 HETATM 4816 O HOH E 201 3.419-100.523 18.661 1.00 30.00 O HETATM 4817 O HOH E 202 2.765 -88.328 27.990 1.00 30.00 O HETATM 4818 O HOH E 203 6.479 -83.061 28.246 1.00 52.50 O HETATM 4819 O HOH E 204 7.478 -79.874 9.264 1.00 51.75 O HETATM 4820 O HOH E 205 9.309 -93.791 11.799 1.00 46.79 O HETATM 4821 O HOH E 206 1.006 -99.736 24.114 1.00 51.54 O HETATM 4822 O HOH E 207 13.521-102.125 15.185 1.00 63.54 O HETATM 4823 O HOH E 208 -2.308 -99.510 18.383 1.00 53.32 O HETATM 4824 O HOH E 209 13.719 -96.221 31.708 1.00 50.96 O HETATM 4825 O HOH E 210 2.818 -75.539 16.166 1.00 50.02 O HETATM 4826 O HOH E 211 16.372 -76.804 26.372 1.00 47.81 O HETATM 4827 O HOH E 212 6.817 -65.471 23.683 1.00 41.72 O HETATM 4828 O HOH E 213 4.599 -87.163 28.885 1.00 30.00 O HETATM 4829 O HOH E 214 6.827 -62.862 31.419 1.00 71.61 O CONECT 94 4767 CONECT 114 4767 CONECT 208 4768 CONECT 219 4768 CONECT 247 4767 CONECT 263 4767 CONECT 373 4768 CONECT 395 4768 CONECT 2456 4770 CONECT 2476 4770 CONECT 2570 4769 CONECT 2581 4769 CONECT 2609 4770 CONECT 2625 4770 CONECT 2735 4769 CONECT 2757 4769 CONECT 4767 94 114 247 263 CONECT 4768 208 219 373 395 CONECT 4769 2570 2581 2735 2757 CONECT 4770 2456 2476 2609 2625 MASTER 336 0 4 21 26 0 9 6 4829 6 20 50 END If you find results from this site helpful for your research, please cite one of our papers:
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