HEADER IMMUNE SYSTEM/TOXIN 11-AUG-25 9PZI TITLE CRYSTAL STRUCTURE OF SYNTHETIC ANTIBODY COP-2 IN COMPLEX WITH THE C- TITLE 2 TERMINAL DOMAIN OF CLOSTRIDIUM PERFRINGENS ENTEROTOXIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: COP-2 LIGHT CHAIN; COMPND 3 CHAIN: C, A, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: COP-2 HEAVY CHAIN; COMPND 7 CHAIN: D, B, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HEAT-LABILE ENTEROTOXIN B CHAIN; COMPND 11 CHAIN: G, I, H; COMPND 12 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 192-319); COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PERFRINGENS; SOURCE 15 ORGANISM_TAXID: 1502; SOURCE 16 GENE: CPE; SOURCE 17 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 18 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS ENTEROTOXIN, SYNTHETIC ANTIBODY, TOXIN, IMMUNE SYSTEM-TOXIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.J.VECCHIO,C.P.OGBU,S.KAPOOR REVDAT 1 20-AUG-25 9PZI 0 SPRSDE 20-AUG-25 9PZI 9MXI JRNL AUTH C.P.OGBU,S.KAPOOR,A.J.VECCHIO JRNL TITL CRYSTAL STRUCTURE OF SYNTHETIC ANTIBODY, COP-2, IN COMPLEX JRNL TITL 2 WITH THE C-TERMINAL DOMAIN OF CLOSTRIDIUM PERFRINGENS JRNL TITL 3 ENTEROTOXIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.74 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 80904 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910 REMARK 3 FREE R VALUE TEST SET COUNT : 3974 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 29.7400 - 7.5500 1.00 2858 105 0.1627 0.2218 REMARK 3 2 7.5500 - 6.0100 0.98 2736 134 0.1860 0.2130 REMARK 3 3 6.0100 - 5.2600 1.00 2778 144 0.1619 0.1954 REMARK 3 4 5.2600 - 4.7800 1.00 2786 128 0.1291 0.1657 REMARK 3 5 4.7800 - 4.4400 1.00 2776 126 0.1238 0.1598 REMARK 3 6 4.4400 - 4.1700 1.00 2814 122 0.1336 0.1475 REMARK 3 7 4.1700 - 3.9700 1.00 2777 113 0.1490 0.2223 REMARK 3 8 3.9700 - 3.7900 0.98 2719 146 0.1622 0.1931 REMARK 3 9 3.7900 - 3.6500 0.99 2722 155 0.1679 0.2022 REMARK 3 10 3.6500 - 3.5200 0.99 2692 181 0.1778 0.1996 REMARK 3 11 3.5200 - 3.4100 0.99 2748 131 0.1805 0.2187 REMARK 3 12 3.4100 - 3.3200 0.99 2728 134 0.1854 0.2389 REMARK 3 13 3.3200 - 3.2300 0.99 2794 135 0.1885 0.2541 REMARK 3 14 3.2300 - 3.1500 1.00 2729 138 0.1980 0.2429 REMARK 3 15 3.1500 - 3.0800 1.00 2802 139 0.1971 0.2839 REMARK 3 16 3.0800 - 3.0100 1.00 2739 136 0.2177 0.2684 REMARK 3 17 3.0100 - 2.9500 1.00 2804 118 0.2216 0.2981 REMARK 3 18 2.9500 - 2.9000 1.00 2732 140 0.2147 0.2352 REMARK 3 19 2.9000 - 2.8400 1.00 2781 122 0.2076 0.2620 REMARK 3 20 2.8400 - 2.8000 1.00 2765 163 0.2001 0.2482 REMARK 3 21 2.8000 - 2.7500 1.00 2757 141 0.2121 0.2472 REMARK 3 22 2.7500 - 2.7100 1.00 2740 155 0.2118 0.2609 REMARK 3 23 2.7100 - 2.6700 0.99 2709 174 0.2248 0.2844 REMARK 3 24 2.6700 - 2.6300 0.97 2662 159 0.2400 0.2897 REMARK 3 25 2.6300 - 2.6000 0.98 2670 159 0.2516 0.3070 REMARK 3 26 2.6000 - 2.5600 0.98 2706 154 0.2683 0.3167 REMARK 3 27 2.5600 - 2.5300 0.98 2665 150 0.2649 0.3330 REMARK 3 28 2.5300 - 2.5000 0.99 2742 172 0.2723 0.3403 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 : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.270 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.06 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.67 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 : 0.015 13116 REMARK 3 ANGLE : 1.450 17865 REMARK 3 CHIRALITY : 0.072 2010 REMARK 3 PLANARITY : 0.012 2267 REMARK 3 DIHEDRAL : 7.494 1805 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 53 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN C AND RESID 2:50 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.480 59.244 -40.137 REMARK 3 T TENSOR REMARK 3 T11: 0.3731 T22: 0.5410 REMARK 3 T33: 0.3171 T12: -0.0302 REMARK 3 T13: 0.0228 T23: -0.0193 REMARK 3 L TENSOR REMARK 3 L11: 1.7267 L22: 6.7982 REMARK 3 L33: 1.4329 L12: 0.2134 REMARK 3 L13: 0.4804 L23: -0.1613 REMARK 3 S TENSOR REMARK 3 S11: -0.1267 S12: 0.2160 S13: 0.1395 REMARK 3 S21: -0.3833 S22: 0.3558 S23: 0.0916 REMARK 3 S31: -0.1654 S32: 0.0895 S33: -0.1617 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN C AND RESID 51:63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.657 66.138 -31.628 REMARK 3 T TENSOR REMARK 3 T11: 0.3269 T22: 0.4207 REMARK 3 T33: 0.3006 T12: -0.0068 REMARK 3 T13: 0.0261 T23: 0.0050 REMARK 3 L TENSOR REMARK 3 L11: 2.1523 L22: 3.0280 REMARK 3 L33: 2.9263 L12: 0.3858 REMARK 3 L13: 0.0532 L23: -0.7011 REMARK 3 S TENSOR REMARK 3 S11: -0.0438 S12: 0.1715 S13: 0.2714 REMARK 3 S21: 0.2391 S22: 0.1480 S23: 0.0591 REMARK 3 S31: -0.4594 S32: -0.1987 S33: -0.0576 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN C AND RESID 64:86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.616 55.892 -26.140 REMARK 3 T TENSOR REMARK 3 T11: 0.4339 T22: 0.3877 REMARK 3 T33: 0.3949 T12: -0.0091 REMARK 3 T13: 0.0176 T23: 0.0041 REMARK 3 L TENSOR REMARK 3 L11: 4.0913 L22: 2.9321 REMARK 3 L33: 3.5510 L12: -0.5558 REMARK 3 L13: 1.1147 L23: 1.8771 REMARK 3 S TENSOR REMARK 3 S11: 0.2414 S12: -0.2641 S13: -0.6676 REMARK 3 S21: 0.4522 S22: -0.2019 S23: -0.4583 REMARK 3 S31: 0.7382 S32: 0.0462 S33: -0.0739 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN C AND RESID 87:127 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.110 61.593 -33.231 REMARK 3 T TENSOR REMARK 3 T11: 0.3366 T22: 0.4471 REMARK 3 T33: 0.3103 T12: -0.0281 REMARK 3 T13: 0.0298 T23: 0.0106 REMARK 3 L TENSOR REMARK 3 L11: 2.2540 L22: 1.7922 REMARK 3 L33: 1.9646 L12: 0.0001 REMARK 3 L13: 0.6598 L23: 1.2390 REMARK 3 S TENSOR REMARK 3 S11: 0.0783 S12: 0.4475 S13: -0.0161 REMARK 3 S21: -0.1268 S22: -0.1327 S23: -0.1050 REMARK 3 S31: -0.1830 S32: 0.0405 S33: 0.0323 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN C AND RESID 128:139 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.955 41.649 -41.385 REMARK 3 T TENSOR REMARK 3 T11: 0.4122 T22: 0.3898 REMARK 3 T33: 0.3911 T12: -0.0340 REMARK 3 T13: 0.0411 T23: -0.0499 REMARK 3 L TENSOR REMARK 3 L11: 0.8968 L22: 7.8860 REMARK 3 L33: 2.2962 L12: 1.5081 REMARK 3 L13: 1.2168 L23: 4.0094 REMARK 3 S TENSOR REMARK 3 S11: 0.1174 S12: -0.2345 S13: -0.5242 REMARK 3 S21: -0.3587 S22: -0.2420 S23: 0.0531 REMARK 3 S31: -0.4385 S32: -0.1908 S33: 0.1089 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN C AND RESID 140:154 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.971 28.044 -29.399 REMARK 3 T TENSOR REMARK 3 T11: 0.6756 T22: 0.8938 REMARK 3 T33: 1.0051 T12: -0.2346 REMARK 3 T13: 0.2662 T23: -0.1386 REMARK 3 L TENSOR REMARK 3 L11: 4.7121 L22: 0.6649 REMARK 3 L33: 1.5998 L12: -1.5739 REMARK 3 L13: -1.0921 L23: 0.8154 REMARK 3 S TENSOR REMARK 3 S11: -1.2068 S12: -0.6539 S13: -0.7763 REMARK 3 S21: 0.3705 S22: 0.4288 S23: -0.1062 REMARK 3 S31: 1.2270 S32: -0.8579 S33: 0.6205 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: ( CHAIN C AND RESID 155:176 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.247 33.941 -40.264 REMARK 3 T TENSOR REMARK 3 T11: 0.5346 T22: 0.5308 REMARK 3 T33: 0.7154 T12: -0.0644 REMARK 3 T13: 0.0725 T23: -0.2056 REMARK 3 L TENSOR REMARK 3 L11: 7.7309 L22: 1.1582 REMARK 3 L33: 1.3849 L12: 1.3918 REMARK 3 L13: -1.5046 L23: -0.6507 REMARK 3 S TENSOR REMARK 3 S11: 0.4188 S12: 0.1276 S13: -0.1263 REMARK 3 S21: 0.1340 S22: -0.3858 S23: 0.6512 REMARK 3 S31: 0.0441 S32: -0.1177 S33: 0.0318 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: ( CHAIN C AND RESID 177:189 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.294 35.375 -42.209 REMARK 3 T TENSOR REMARK 3 T11: 0.7548 T22: 0.8467 REMARK 3 T33: 0.8605 T12: 0.0442 REMARK 3 T13: -0.0141 T23: -0.1758 REMARK 3 L TENSOR REMARK 3 L11: 6.8597 L22: 3.2980 REMARK 3 L33: 4.9441 L12: 0.9093 REMARK 3 L13: 0.5305 L23: 0.5658 REMARK 3 S TENSOR REMARK 3 S11: 0.4071 S12: 1.1648 S13: 0.3932 REMARK 3 S21: -0.7985 S22: -0.5226 S23: 1.1843 REMARK 3 S31: 0.6954 S32: -0.6758 S33: -0.0323 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: ( CHAIN C AND RESID 190:212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.903 35.998 -34.979 REMARK 3 T TENSOR REMARK 3 T11: 0.5121 T22: 0.5689 REMARK 3 T33: 0.6794 T12: -0.0477 REMARK 3 T13: 0.0723 T23: -0.1973 REMARK 3 L TENSOR REMARK 3 L11: 1.4756 L22: 1.7463 REMARK 3 L33: 1.0334 L12: 1.5527 REMARK 3 L13: -0.9022 L23: -0.8778 REMARK 3 S TENSOR REMARK 3 S11: 0.1109 S12: -0.9567 S13: -0.2480 REMARK 3 S21: 0.1603 S22: -0.2638 S23: 0.3575 REMARK 3 S31: 0.0306 S32: -0.1755 S33: 0.1317 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: ( CHAIN C AND RESID 213:223 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.270 26.381 -41.396 REMARK 3 T TENSOR REMARK 3 T11: 0.6518 T22: 0.7565 REMARK 3 T33: 1.3136 T12: -0.1380 REMARK 3 T13: 0.0344 T23: -0.2955 REMARK 3 L TENSOR REMARK 3 L11: 5.3942 L22: 1.5186 REMARK 3 L33: 0.0990 L12: 1.7509 REMARK 3 L13: 0.1493 L23: 0.0097 REMARK 3 S TENSOR REMARK 3 S11: -0.5530 S12: 0.0895 S13: -1.1804 REMARK 3 S21: -0.2432 S22: 0.2046 S23: 0.6016 REMARK 3 S31: 0.5579 S32: -0.7489 S33: 0.2713 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: ( CHAIN C AND RESID 224:237 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.223 25.554 -44.026 REMARK 3 T TENSOR REMARK 3 T11: 0.5492 T22: 0.5374 REMARK 3 T33: 0.8499 T12: -0.0474 REMARK 3 T13: 0.0609 T23: -0.2630 REMARK 3 L TENSOR REMARK 3 L11: 8.5007 L22: 3.6289 REMARK 3 L33: 4.3717 L12: 2.9016 REMARK 3 L13: -3.3047 L23: -1.8169 REMARK 3 S TENSOR REMARK 3 S11: -0.4772 S12: 0.9764 S13: -0.9892 REMARK 3 S21: 0.2107 S22: 0.2482 S23: 0.2381 REMARK 3 S31: 0.6610 S32: -0.8340 S33: 0.3971 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: ( CHAIN D AND RESID 4:43 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.652 58.674 -15.328 REMARK 3 T TENSOR REMARK 3 T11: 0.3940 T22: 0.4458 REMARK 3 T33: 0.2782 T12: -0.0269 REMARK 3 T13: 0.0939 T23: -0.0767 REMARK 3 L TENSOR REMARK 3 L11: 1.7169 L22: 3.1221 REMARK 3 L33: 4.9820 L12: 1.4456 REMARK 3 L13: 2.3333 L23: 0.0090 REMARK 3 S TENSOR REMARK 3 S11: 0.1148 S12: -0.3727 S13: -0.3732 REMARK 3 S21: 0.3568 S22: -0.0682 S23: 0.1766 REMARK 3 S31: 0.5337 S32: -0.3184 S33: -0.0442 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: ( CHAIN D AND RESID 44:93 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.890 67.871 -17.845 REMARK 3 T TENSOR REMARK 3 T11: 0.3032 T22: 0.3692 REMARK 3 T33: 0.2386 T12: 0.0168 REMARK 3 T13: 0.0302 T23: -0.0137 REMARK 3 L TENSOR REMARK 3 L11: 2.3178 L22: 2.3183 REMARK 3 L33: 1.5892 L12: 0.2481 REMARK 3 L13: -0.2762 L23: 0.1991 REMARK 3 S TENSOR REMARK 3 S11: -0.0329 S12: 0.2302 S13: 0.0664 REMARK 3 S21: -0.0385 S22: 0.0194 S23: 0.1103 REMARK 3 S31: -0.3390 S32: -0.1649 S33: 0.0085 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: ( CHAIN D AND RESID 94:117 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.086 67.107 -15.152 REMARK 3 T TENSOR REMARK 3 T11: 0.3829 T22: 0.3712 REMARK 3 T33: 0.3051 T12: -0.0218 REMARK 3 T13: 0.0462 T23: -0.0100 REMARK 3 L TENSOR REMARK 3 L11: 3.2704 L22: 4.2163 REMARK 3 L33: 0.9944 L12: -0.1354 REMARK 3 L13: -1.3592 L23: 1.3760 REMARK 3 S TENSOR REMARK 3 S11: -0.1172 S12: 0.3119 S13: 0.2615 REMARK 3 S21: -0.1283 S22: -0.2761 S23: 0.2413 REMARK 3 S31: -0.2593 S32: -0.4233 S33: 0.3283 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: ( CHAIN D AND RESID 118:158 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.619 62.639 -20.869 REMARK 3 T TENSOR REMARK 3 T11: 0.3679 T22: 0.3483 REMARK 3 T33: 0.3033 T12: 0.0252 REMARK 3 T13: 0.0570 T23: -0.0612 REMARK 3 L TENSOR REMARK 3 L11: 2.5587 L22: 2.2774 REMARK 3 L33: 1.2976 L12: 0.9540 REMARK 3 L13: 0.1693 L23: 0.0956 REMARK 3 S TENSOR REMARK 3 S11: -0.0183 S12: -0.2425 S13: -0.3040 REMARK 3 S21: 0.0298 S22: -0.1253 S23: -0.0287 REMARK 3 S31: 0.0780 S32: -0.1837 S33: 0.0524 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: ( CHAIN D AND RESID 159:173 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.203 26.923 -25.897 REMARK 3 T TENSOR REMARK 3 T11: 0.6118 T22: 0.6592 REMARK 3 T33: 0.9705 T12: -0.1274 REMARK 3 T13: 0.1714 T23: 0.1106 REMARK 3 L TENSOR REMARK 3 L11: 8.3874 L22: 8.9289 REMARK 3 L33: 6.6316 L12: -4.8617 REMARK 3 L13: 0.4833 L23: 2.2847 REMARK 3 S TENSOR REMARK 3 S11: 0.7799 S12: -0.8664 S13: -0.8207 REMARK 3 S21: 0.0173 S22: -0.2389 S23: 0.3172 REMARK 3 S31: 0.7979 S32: -0.6384 S33: -0.4318 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: ( CHAIN D AND RESID 174:242 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.729 35.749 -23.214 REMARK 3 T TENSOR REMARK 3 T11: 0.5779 T22: 0.7209 REMARK 3 T33: 0.5694 T12: -0.0370 REMARK 3 T13: 0.0810 T23: 0.0225 REMARK 3 L TENSOR REMARK 3 L11: 3.2019 L22: 4.0487 REMARK 3 L33: 3.5696 L12: 0.0076 REMARK 3 L13: -0.5092 L23: 1.4225 REMARK 3 S TENSOR REMARK 3 S11: -0.1726 S12: -1.0112 S13: -0.5016 REMARK 3 S21: 0.7990 S22: 0.0742 S23: 0.1602 REMARK 3 S31: 0.5992 S32: 0.3527 S33: 0.1008 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: ( CHAIN D AND RESID 243:252 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.155 31.797 -15.789 REMARK 3 T TENSOR REMARK 3 T11: 1.0923 T22: 1.0960 REMARK 3 T33: 1.1575 T12: 0.0273 REMARK 3 T13: 0.3504 T23: 0.2995 REMARK 3 L TENSOR REMARK 3 L11: 0.8923 L22: 1.6572 REMARK 3 L33: 0.6992 L12: -0.5918 REMARK 3 L13: 0.3353 L23: 0.6587 REMARK 3 S TENSOR REMARK 3 S11: -0.0939 S12: -0.7053 S13: -0.4368 REMARK 3 S21: 0.4763 S22: -0.3184 S23: 0.0086 REMARK 3 S31: 0.1525 S32: 0.4094 S33: 0.2179 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: ( CHAIN A AND RESID 2:50 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.595 31.375 -53.107 REMARK 3 T TENSOR REMARK 3 T11: 0.3713 T22: 0.3261 REMARK 3 T33: 0.4969 T12: -0.0302 REMARK 3 T13: -0.0645 T23: -0.0521 REMARK 3 L TENSOR REMARK 3 L11: 2.1558 L22: 3.0729 REMARK 3 L33: 4.9402 L12: -1.0148 REMARK 3 L13: -0.8313 L23: -1.9448 REMARK 3 S TENSOR REMARK 3 S11: 0.0488 S12: -0.1275 S13: 0.4222 REMARK 3 S21: 0.4989 S22: 0.1910 S23: 0.1562 REMARK 3 S31: -0.4726 S32: -0.3303 S33: -0.0796 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: ( CHAIN A AND RESID 51:100 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.078 22.539 -56.823 REMARK 3 T TENSOR REMARK 3 T11: 0.2707 T22: 0.2632 REMARK 3 T33: 0.3697 T12: -0.0049 REMARK 3 T13: -0.0402 T23: -0.0051 REMARK 3 L TENSOR REMARK 3 L11: 3.0550 L22: 4.5548 REMARK 3 L33: 1.3189 L12: -0.2179 REMARK 3 L13: -0.7746 L23: -0.3383 REMARK 3 S TENSOR REMARK 3 S11: -0.0248 S12: -0.1357 S13: 0.2881 REMARK 3 S21: 0.1779 S22: -0.1136 S23: -0.0876 REMARK 3 S31: 0.0625 S32: 0.1214 S33: 0.1408 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: ( CHAIN A AND RESID 101:127 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.704 22.994 -55.917 REMARK 3 T TENSOR REMARK 3 T11: 0.3070 T22: 0.2617 REMARK 3 T33: 0.4406 T12: 0.0256 REMARK 3 T13: -0.0136 T23: 0.0103 REMARK 3 L TENSOR REMARK 3 L11: 0.4625 L22: 3.1569 REMARK 3 L33: 2.8927 L12: 0.0296 REMARK 3 L13: 0.2681 L23: -1.1040 REMARK 3 S TENSOR REMARK 3 S11: 0.0146 S12: -0.0660 S13: -0.0552 REMARK 3 S21: -0.0851 S22: -0.2656 S23: 0.0247 REMARK 3 S31: 0.2695 S32: 0.2339 S33: 0.1359 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: ( CHAIN A AND RESID 128:139 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.356 41.264 -68.049 REMARK 3 T TENSOR REMARK 3 T11: 0.3581 T22: 0.3207 REMARK 3 T33: 0.5040 T12: 0.0176 REMARK 3 T13: -0.0353 T23: 0.0318 REMARK 3 L TENSOR REMARK 3 L11: 0.6477 L22: 5.4166 REMARK 3 L33: 3.9319 L12: -1.9006 REMARK 3 L13: 1.5463 L23: -4.5358 REMARK 3 S TENSOR REMARK 3 S11: 0.1799 S12: 0.2685 S13: -0.2855 REMARK 3 S21: 0.2879 S22: 0.2409 S23: 0.5288 REMARK 3 S31: 0.2276 S32: -0.2993 S33: -0.5738 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: ( CHAIN A AND RESID 140:176 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.621 40.852 -80.454 REMARK 3 T TENSOR REMARK 3 T11: 0.4299 T22: 0.6783 REMARK 3 T33: 0.5843 T12: -0.0188 REMARK 3 T13: -0.0356 T23: 0.1927 REMARK 3 L TENSOR REMARK 3 L11: 5.8035 L22: 1.9645 REMARK 3 L33: 1.6903 L12: 1.2359 REMARK 3 L13: 1.2129 L23: 0.1374 REMARK 3 S TENSOR REMARK 3 S11: -0.2120 S12: 0.6798 S13: 0.1766 REMARK 3 S21: -0.0664 S22: 0.1852 S23: 0.5421 REMARK 3 S31: -0.0512 S32: -0.3936 S33: 0.0126 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: ( CHAIN A AND RESID 177:189 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.776 44.578 -74.811 REMARK 3 T TENSOR REMARK 3 T11: 0.5636 T22: 0.6751 REMARK 3 T33: 0.8715 T12: 0.0631 REMARK 3 T13: -0.0132 T23: 0.1745 REMARK 3 L TENSOR REMARK 3 L11: 3.6573 L22: 3.5893 REMARK 3 L33: 3.6394 L12: -1.0431 REMARK 3 L13: 1.0358 L23: -1.3289 REMARK 3 S TENSOR REMARK 3 S11: -0.0800 S12: 0.3363 S13: 0.7810 REMARK 3 S21: -0.1521 S22: 0.4685 S23: 0.5358 REMARK 3 S31: -0.8626 S32: -0.9397 S33: -0.5382 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: ( CHAIN A AND RESID 190:212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.141 37.889 -76.960 REMARK 3 T TENSOR REMARK 3 T11: 0.5045 T22: 0.4843 REMARK 3 T33: 0.6918 T12: -0.0499 REMARK 3 T13: -0.0312 T23: 0.1596 REMARK 3 L TENSOR REMARK 3 L11: 8.7603 L22: 0.2216 REMARK 3 L33: 2.2148 L12: 0.2621 REMARK 3 L13: 2.0420 L23: -0.1573 REMARK 3 S TENSOR REMARK 3 S11: 0.0828 S12: 0.3340 S13: -0.3990 REMARK 3 S21: -0.0728 S22: 0.1260 S23: 0.0598 REMARK 3 S31: 0.0337 S32: -0.2559 S33: -0.3244 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: ( CHAIN A AND RESID 213:237 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.410 49.415 -82.493 REMARK 3 T TENSOR REMARK 3 T11: 0.5164 T22: 0.8723 REMARK 3 T33: 0.8764 T12: -0.0427 REMARK 3 T13: -0.1712 T23: 0.3545 REMARK 3 L TENSOR REMARK 3 L11: 3.9899 L22: 1.0484 REMARK 3 L33: 2.3673 L12: 0.0941 REMARK 3 L13: 2.2549 L23: 0.8569 REMARK 3 S TENSOR REMARK 3 S11: -0.5796 S12: 0.8460 S13: 1.1627 REMARK 3 S21: -0.5859 S22: 0.3442 S23: 1.1722 REMARK 3 S31: -0.6726 S32: -0.5591 S33: 0.2723 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: ( CHAIN B AND RESID 4:158 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.960 9.202 -59.739 REMARK 3 T TENSOR REMARK 3 T11: 0.3609 T22: 0.2307 REMARK 3 T33: 0.5505 T12: -0.0410 REMARK 3 T13: -0.0622 T23: -0.0018 REMARK 3 L TENSOR REMARK 3 L11: 2.4552 L22: 2.5940 REMARK 3 L33: 2.0626 L12: -0.4608 REMARK 3 L13: 0.9136 L23: -1.1013 REMARK 3 S TENSOR REMARK 3 S11: 0.0097 S12: 0.0126 S13: -0.1219 REMARK 3 S21: -0.1485 S22: 0.1443 S23: 0.6398 REMARK 3 S31: 0.1110 S32: -0.2106 S33: -0.1130 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: ( CHAIN B AND RESID 159:173 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.896 32.790 -88.582 REMARK 3 T TENSOR REMARK 3 T11: 0.7854 T22: 1.1947 REMARK 3 T33: 0.6716 T12: -0.1449 REMARK 3 T13: -0.1769 T23: -0.0639 REMARK 3 L TENSOR REMARK 3 L11: 3.0998 L22: 1.7791 REMARK 3 L33: 1.0549 L12: -2.0605 REMARK 3 L13: -0.4225 L23: 0.9205 REMARK 3 S TENSOR REMARK 3 S11: 0.0680 S12: 0.6280 S13: -0.4554 REMARK 3 S21: -0.5517 S22: -0.4112 S23: 0.7985 REMARK 3 S31: 0.0019 S32: -0.6038 S33: 0.2555 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: ( CHAIN B AND RESID 174:252 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.920 26.923 -83.271 REMARK 3 T TENSOR REMARK 3 T11: 0.5876 T22: 0.6436 REMARK 3 T33: 0.7665 T12: -0.1585 REMARK 3 T13: -0.0847 T23: -0.0747 REMARK 3 L TENSOR REMARK 3 L11: 3.8253 L22: 3.7837 REMARK 3 L33: 2.5798 L12: 0.2572 REMARK 3 L13: 0.4933 L23: -1.1659 REMARK 3 S TENSOR REMARK 3 S11: -0.3135 S12: 0.8090 S13: -1.0402 REMARK 3 S21: -0.9201 S22: 0.3277 S23: -0.0166 REMARK 3 S31: 0.5947 S32: -0.0190 S33: -0.0956 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: ( CHAIN E AND RESID 2:50 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.857 56.174 -71.222 REMARK 3 T TENSOR REMARK 3 T11: 0.3418 T22: 0.4512 REMARK 3 T33: 0.3360 T12: 0.0115 REMARK 3 T13: 0.0156 T23: 0.1265 REMARK 3 L TENSOR REMARK 3 L11: 1.0863 L22: 3.5552 REMARK 3 L33: 4.7167 L12: 0.4007 REMARK 3 L13: -0.7561 L23: 0.7689 REMARK 3 S TENSOR REMARK 3 S11: -0.2488 S12: -0.1757 S13: 0.1191 REMARK 3 S21: 0.0660 S22: -0.1145 S23: 0.0697 REMARK 3 S31: 0.3939 S32: -0.2266 S33: 0.3425 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: ( CHAIN E AND RESID 51:63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.460 60.796 -81.238 REMARK 3 T TENSOR REMARK 3 T11: 0.3316 T22: 0.3003 REMARK 3 T33: 0.2844 T12: -0.0128 REMARK 3 T13: 0.0139 T23: 0.0514 REMARK 3 L TENSOR REMARK 3 L11: 3.3410 L22: 3.6029 REMARK 3 L33: 2.7156 L12: -0.7370 REMARK 3 L13: -0.8609 L23: 0.3543 REMARK 3 S TENSOR REMARK 3 S11: 0.1859 S12: 0.0904 S13: -0.0282 REMARK 3 S21: -0.6169 S22: 0.0360 S23: -0.3508 REMARK 3 S31: -0.0483 S32: 0.2761 S33: -0.1309 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: ( CHAIN E AND RESID 64:127 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.545 64.447 -75.752 REMARK 3 T TENSOR REMARK 3 T11: 0.3237 T22: 0.3354 REMARK 3 T33: 0.3295 T12: 0.0083 REMARK 3 T13: 0.0178 T23: 0.0341 REMARK 3 L TENSOR REMARK 3 L11: 2.3087 L22: 1.1645 REMARK 3 L33: 4.0108 L12: 0.3073 REMARK 3 L13: 0.4187 L23: -1.0382 REMARK 3 S TENSOR REMARK 3 S11: 0.0495 S12: -0.2103 S13: -0.1508 REMARK 3 S21: 0.0704 S22: 0.1172 S23: -0.0319 REMARK 3 S31: -0.0808 S32: 0.0937 S33: -0.1695 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: ( CHAIN E AND RESID 128:139 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.032 63.677 -55.039 REMARK 3 T TENSOR REMARK 3 T11: 0.4600 T22: 0.5152 REMARK 3 T33: 0.3888 T12: 0.0084 REMARK 3 T13: 0.0531 T23: 0.0048 REMARK 3 L TENSOR REMARK 3 L11: 1.3361 L22: 1.0684 REMARK 3 L33: 2.9214 L12: -0.8453 REMARK 3 L13: -1.9051 L23: 1.5748 REMARK 3 S TENSOR REMARK 3 S11: -0.0686 S12: -0.2655 S13: -0.1142 REMARK 3 S21: -0.0848 S22: -0.1835 S23: 0.0488 REMARK 3 S31: 0.5000 S32: -0.5683 S33: 0.4267 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: ( CHAIN E AND RESID 140:154 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.454 82.186 -49.626 REMARK 3 T TENSOR REMARK 3 T11: 0.6061 T22: 1.7612 REMARK 3 T33: 0.7607 T12: 0.9204 REMARK 3 T13: -0.2181 T23: -0.2602 REMARK 3 L TENSOR REMARK 3 L11: 1.7843 L22: 1.2662 REMARK 3 L33: 0.0530 L12: 0.6834 REMARK 3 L13: 0.1752 L23: -0.0981 REMARK 3 S TENSOR REMARK 3 S11: -0.0297 S12: 0.0125 S13: 0.6276 REMARK 3 S21: -0.0884 S22: -0.0585 S23: 0.6802 REMARK 3 S31: -0.4031 S32: -0.5509 S33: -0.2813 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: ( CHAIN E AND RESID 155:176 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.209 68.997 -48.825 REMARK 3 T TENSOR REMARK 3 T11: 0.5133 T22: 1.5775 REMARK 3 T33: 0.1911 T12: 0.2632 REMARK 3 T13: -0.1265 T23: 0.0754 REMARK 3 L TENSOR REMARK 3 L11: 4.1739 L22: 1.5431 REMARK 3 L33: 0.2451 L12: -0.3443 REMARK 3 L13: -0.3815 L23: 0.3424 REMARK 3 S TENSOR REMARK 3 S11: 0.3577 S12: -0.4695 S13: -0.4059 REMARK 3 S21: -0.3444 S22: -0.2162 S23: -0.0142 REMARK 3 S31: -0.5624 S32: -2.0304 S33: -0.0378 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: ( CHAIN E AND RESID 177:189 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.312 66.756 -48.860 REMARK 3 T TENSOR REMARK 3 T11: 0.6728 T22: 1.9297 REMARK 3 T33: 0.5563 T12: 0.0615 REMARK 3 T13: 0.0905 T23: 0.2541 REMARK 3 L TENSOR REMARK 3 L11: 3.2844 L22: 1.9535 REMARK 3 L33: 5.4472 L12: 1.4538 REMARK 3 L13: -4.2261 L23: -1.6767 REMARK 3 S TENSOR REMARK 3 S11: 0.3017 S12: -0.7242 S13: -0.2893 REMARK 3 S21: 0.6682 S22: 0.2651 S23: 0.7911 REMARK 3 S31: 0.0020 S32: -2.6537 S33: -0.0578 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: ( CHAIN E AND RESID 190:212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.858 72.306 -53.247 REMARK 3 T TENSOR REMARK 3 T11: 0.5573 T22: 1.6040 REMARK 3 T33: 0.4226 T12: 0.2713 REMARK 3 T13: 0.0165 T23: 0.0616 REMARK 3 L TENSOR REMARK 3 L11: 2.7101 L22: 1.5107 REMARK 3 L33: 0.2560 L12: -1.8845 REMARK 3 L13: -0.5128 L23: 0.4812 REMARK 3 S TENSOR REMARK 3 S11: 0.1638 S12: -0.2660 S13: 0.5617 REMARK 3 S21: 0.2446 S22: 0.0764 S23: 0.0799 REMARK 3 S31: -0.5257 S32: -1.7363 S33: -0.0614 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: ( CHAIN E AND RESID 213:237 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.368 70.913 -40.689 REMARK 3 T TENSOR REMARK 3 T11: 0.6891 T22: 1.9729 REMARK 3 T33: 0.2417 T12: 0.5070 REMARK 3 T13: 0.1634 T23: -0.1018 REMARK 3 L TENSOR REMARK 3 L11: 4.1159 L22: 0.5992 REMARK 3 L33: 2.0640 L12: -0.4043 REMARK 3 L13: -2.7484 L23: 0.7117 REMARK 3 S TENSOR REMARK 3 S11: 0.2367 S12: -1.3167 S13: -0.3486 REMARK 3 S21: 0.6085 S22: 0.0180 S23: 0.1532 REMARK 3 S31: -1.0851 S32: -2.0148 S33: 0.1808 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: ( CHAIN F AND RESID 4:163 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.323 73.808 -85.503 REMARK 3 T TENSOR REMARK 3 T11: 0.3653 T22: 0.3320 REMARK 3 T33: 0.2939 T12: 0.0607 REMARK 3 T13: -0.0046 T23: 0.0771 REMARK 3 L TENSOR REMARK 3 L11: 3.5424 L22: 1.3786 REMARK 3 L33: 2.5557 L12: -1.4920 REMARK 3 L13: -0.8325 L23: 0.2108 REMARK 3 S TENSOR REMARK 3 S11: -0.1001 S12: -0.0832 S13: 0.0604 REMARK 3 S21: 0.0312 S22: 0.1677 S23: 0.0633 REMARK 3 S31: -0.2897 S32: -0.3707 S33: -0.0957 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: ( CHAIN F AND RESID 164:184 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.795 82.255 -52.894 REMARK 3 T TENSOR REMARK 3 T11: 1.4118 T22: 1.3809 REMARK 3 T33: 0.3569 T12: 1.0040 REMARK 3 T13: -0.5517 T23: -0.1804 REMARK 3 L TENSOR REMARK 3 L11: 2.5502 L22: 1.2069 REMARK 3 L33: 3.4897 L12: 1.6228 REMARK 3 L13: 2.5901 L23: 1.2026 REMARK 3 S TENSOR REMARK 3 S11: -0.0473 S12: -0.8220 S13: 0.2101 REMARK 3 S21: 0.6625 S22: 0.1476 S23: 0.0117 REMARK 3 S31: -0.7236 S32: -1.1267 S33: 0.3960 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: ( CHAIN F AND RESID 185:252 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.998 83.803 -60.139 REMARK 3 T TENSOR REMARK 3 T11: 1.1338 T22: 0.7107 REMARK 3 T33: 0.5964 T12: 0.3901 REMARK 3 T13: -0.1847 T23: -0.0417 REMARK 3 L TENSOR REMARK 3 L11: 4.2676 L22: 0.3112 REMARK 3 L33: 4.1514 L12: 0.2282 REMARK 3 L13: 1.1554 L23: 0.1281 REMARK 3 S TENSOR REMARK 3 S11: -0.7792 S12: -0.2783 S13: 1.0281 REMARK 3 S21: 0.2422 S22: 0.4110 S23: -0.0080 REMARK 3 S31: -2.4441 S32: -1.1618 S33: 0.2279 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: ( CHAIN G AND RESID 201:210 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.280 62.977 -101.675 REMARK 3 T TENSOR REMARK 3 T11: 0.4372 T22: 0.4226 REMARK 3 T33: 0.4481 T12: 0.0393 REMARK 3 T13: 0.0108 T23: -0.0182 REMARK 3 L TENSOR REMARK 3 L11: 4.1483 L22: 2.3065 REMARK 3 L33: 2.1395 L12: -0.7130 REMARK 3 L13: 0.6266 L23: 1.2038 REMARK 3 S TENSOR REMARK 3 S11: -0.1083 S12: -0.1517 S13: -0.5459 REMARK 3 S21: 1.1868 S22: -0.6143 S23: -0.6567 REMARK 3 S31: -0.4252 S32: 0.9396 S33: 0.4640 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: ( CHAIN G AND RESID 211:227 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.270 71.580 -118.223 REMARK 3 T TENSOR REMARK 3 T11: 0.4746 T22: 0.3443 REMARK 3 T33: 0.3223 T12: 0.0679 REMARK 3 T13: 0.0016 T23: -0.0121 REMARK 3 L TENSOR REMARK 3 L11: 3.5378 L22: 2.8048 REMARK 3 L33: 4.1626 L12: 0.5793 REMARK 3 L13: 0.0200 L23: -1.5025 REMARK 3 S TENSOR REMARK 3 S11: -0.0218 S12: 0.4409 S13: 0.1716 REMARK 3 S21: -0.7006 S22: -0.3842 S23: -0.1405 REMARK 3 S31: -0.0477 S32: 0.7043 S33: 0.2009 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: ( CHAIN G AND RESID 228:284 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.593 65.748 -105.224 REMARK 3 T TENSOR REMARK 3 T11: 0.3387 T22: 0.3419 REMARK 3 T33: 0.3326 T12: 0.0364 REMARK 3 T13: 0.0343 T23: 0.0209 REMARK 3 L TENSOR REMARK 3 L11: 1.3160 L22: 2.5685 REMARK 3 L33: 3.3636 L12: -0.3381 REMARK 3 L13: 0.6585 L23: 0.1012 REMARK 3 S TENSOR REMARK 3 S11: 0.1102 S12: 0.0886 S13: -0.0855 REMARK 3 S21: -0.1501 S22: 0.0117 S23: 0.0660 REMARK 3 S31: 0.1324 S32: -0.1630 S33: -0.1156 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: ( CHAIN G AND RESID 285:322 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.101 65.145 -109.879 REMARK 3 T TENSOR REMARK 3 T11: 0.3836 T22: 0.3443 REMARK 3 T33: 0.3206 T12: 0.0237 REMARK 3 T13: 0.0105 T23: -0.0297 REMARK 3 L TENSOR REMARK 3 L11: 2.2719 L22: 1.9686 REMARK 3 L33: 3.5704 L12: 0.1611 REMARK 3 L13: 0.0329 L23: -0.4769 REMARK 3 S TENSOR REMARK 3 S11: 0.0064 S12: 0.0555 S13: -0.1482 REMARK 3 S21: -0.2535 S22: 0.0144 S23: -0.0389 REMARK 3 S31: 0.3404 S32: -0.1023 S33: -0.0141 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: ( CHAIN I AND RESID 200:217 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.086 94.865 -96.473 REMARK 3 T TENSOR REMARK 3 T11: 0.4597 T22: 0.5646 REMARK 3 T33: 0.4444 T12: -0.0747 REMARK 3 T13: -0.0605 T23: 0.0587 REMARK 3 L TENSOR REMARK 3 L11: 2.2166 L22: 7.5644 REMARK 3 L33: 1.4517 L12: 1.7094 REMARK 3 L13: 0.2741 L23: -0.3742 REMARK 3 S TENSOR REMARK 3 S11: -0.1205 S12: -0.1012 S13: 0.1467 REMARK 3 S21: 0.0126 S22: -0.0634 S23: -0.5858 REMARK 3 S31: 0.1217 S32: 0.3190 S33: 0.0832 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: ( CHAIN I AND RESID 218:227 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.877 83.740 -90.910 REMARK 3 T TENSOR REMARK 3 T11: 0.5241 T22: 0.4578 REMARK 3 T33: 0.4576 T12: 0.0051 REMARK 3 T13: -0.1129 T23: 0.1007 REMARK 3 L TENSOR REMARK 3 L11: 5.9132 L22: 1.6341 REMARK 3 L33: 3.5411 L12: 1.9590 REMARK 3 L13: -1.2695 L23: -0.9043 REMARK 3 S TENSOR REMARK 3 S11: 0.2983 S12: -0.7404 S13: -0.0967 REMARK 3 S21: 1.4153 S22: -0.3215 S23: 0.4242 REMARK 3 S31: -0.0023 S32: -0.2942 S33: 0.1270 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: ( CHAIN I AND RESID 228:284 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.107 97.328 -96.780 REMARK 3 T TENSOR REMARK 3 T11: 0.3772 T22: 0.3131 REMARK 3 T33: 0.3699 T12: -0.0240 REMARK 3 T13: -0.0302 T23: -0.0058 REMARK 3 L TENSOR REMARK 3 L11: 2.1202 L22: 3.1486 REMARK 3 L33: 2.6236 L12: 0.4767 REMARK 3 L13: -0.2435 L23: -1.0500 REMARK 3 S TENSOR REMARK 3 S11: 0.1146 S12: -0.1632 S13: 0.1092 REMARK 3 S21: 0.1945 S22: -0.1694 S23: 0.3054 REMARK 3 S31: 0.0273 S32: -0.0253 S33: 0.0766 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: ( CHAIN I AND RESID 285:321 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.686 94.404 -93.538 REMARK 3 T TENSOR REMARK 3 T11: 0.4505 T22: 0.3147 REMARK 3 T33: 0.3740 T12: -0.0303 REMARK 3 T13: -0.0086 T23: 0.0435 REMARK 3 L TENSOR REMARK 3 L11: 2.7420 L22: 2.7030 REMARK 3 L33: 2.9701 L12: 0.3102 REMARK 3 L13: -0.6209 L23: -0.7293 REMARK 3 S TENSOR REMARK 3 S11: 0.0770 S12: -0.1933 S13: 0.3226 REMARK 3 S21: 0.3871 S22: -0.1576 S23: 0.1953 REMARK 3 S31: -0.2761 S32: 0.0666 S33: 0.0542 REMARK 3 TLS GROUP : 50 REMARK 3 SELECTION: ( CHAIN H AND RESID 197:204 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.892 78.525 -71.542 REMARK 3 T TENSOR REMARK 3 T11: 1.1281 T22: 0.7523 REMARK 3 T33: 0.8089 T12: 0.0907 REMARK 3 T13: -0.1382 T23: 0.0504 REMARK 3 L TENSOR REMARK 3 L11: 5.9828 L22: 7.2123 REMARK 3 L33: 1.0756 L12: 0.3313 REMARK 3 L13: 0.8103 L23: -1.5516 REMARK 3 S TENSOR REMARK 3 S11: 0.2455 S12: -1.3515 S13: -0.7520 REMARK 3 S21: 2.1341 S22: 0.5013 S23: -0.9165 REMARK 3 S31: 0.2243 S32: -0.0085 S33: -0.6271 REMARK 3 TLS GROUP : 51 REMARK 3 SELECTION: ( CHAIN H AND RESID 205:227 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.814 93.204 -100.353 REMARK 3 T TENSOR REMARK 3 T11: 0.4492 T22: 0.3214 REMARK 3 T33: 0.4755 T12: 0.0748 REMARK 3 T13: 0.1000 T23: 0.0011 REMARK 3 L TENSOR REMARK 3 L11: 3.7206 L22: 3.8006 REMARK 3 L33: 5.7023 L12: -0.1318 REMARK 3 L13: -0.1499 L23: -1.5042 REMARK 3 S TENSOR REMARK 3 S11: 0.0163 S12: 0.2949 S13: 0.4803 REMARK 3 S21: -0.0842 S22: 0.0920 S23: -0.0798 REMARK 3 S31: -0.4064 S32: -0.4262 S33: -0.2624 REMARK 3 TLS GROUP : 52 REMARK 3 SELECTION: ( CHAIN H AND RESID 228:302 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.792 85.632 -92.848 REMARK 3 T TENSOR REMARK 3 T11: 0.4017 T22: 0.2788 REMARK 3 T33: 0.3603 T12: 0.0147 REMARK 3 T13: 0.0464 T23: -0.0335 REMARK 3 L TENSOR REMARK 3 L11: 1.5403 L22: 2.6147 REMARK 3 L33: 2.9098 L12: 0.0289 REMARK 3 L13: -0.9458 L23: -0.3881 REMARK 3 S TENSOR REMARK 3 S11: 0.1627 S12: -0.1079 S13: 0.2236 REMARK 3 S21: 0.0382 S22: -0.0309 S23: -0.1304 REMARK 3 S31: -0.2079 S32: 0.1361 S33: -0.1130 REMARK 3 TLS GROUP : 53 REMARK 3 SELECTION: ( CHAIN H AND RESID 303:322 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.943 94.957 -90.855 REMARK 3 T TENSOR REMARK 3 T11: 0.5232 T22: 0.2945 REMARK 3 T33: 0.5706 T12: -0.0474 REMARK 3 T13: 0.1342 T23: -0.0627 REMARK 3 L TENSOR REMARK 3 L11: 2.5344 L22: 1.7459 REMARK 3 L33: 7.4006 L12: -0.7181 REMARK 3 L13: -1.5529 L23: 0.0378 REMARK 3 S TENSOR REMARK 3 S11: 0.1150 S12: -0.6021 S13: 0.1588 REMARK 3 S21: 0.2316 S22: -0.2989 S23: 0.1795 REMARK 3 S31: -0.9884 S32: 0.3475 S33: 0.2054 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: TLS, NCS AND SECONDARY STRUCTURE REMARK 3 RESTRAINTS REMARK 4 REMARK 4 9PZI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000298526. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-FEB-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033167 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81028 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 29.740 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : 0.06600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.9600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.53500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.690 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM SODIUM CHLORIDE, 1.75 M REMARK 280 AMMONIUM SULFATE, AND 100 MM SODIUM CACODYLATE PH 6.6, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z+1/2 REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 36.20066 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 99.26000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 54.50433 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 36.20066 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 99.26000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 54.50433 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: H REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 39.07368 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -109.00866 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24900 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: I REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 36.20066 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -99.26000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 54.50433 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5610 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24740 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 308 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET C -22 REMARK 465 LYS C -21 REMARK 465 LYS C -20 REMARK 465 ASN C -19 REMARK 465 ILE C -18 REMARK 465 ALA C -17 REMARK 465 PHE C -16 REMARK 465 LEU C -15 REMARK 465 LEU C -14 REMARK 465 ALA C -13 REMARK 465 SER C -12 REMARK 465 MET C -11 REMARK 465 PHE C -10 REMARK 465 VAL C -9 REMARK 465 PHE C -8 REMARK 465 SER C -7 REMARK 465 ILE C -6 REMARK 465 ALA C -5 REMARK 465 THR C -4 REMARK 465 ASN C -3 REMARK 465 ALA C -2 REMARK 465 TYR C -1 REMARK 465 ALA C 0 REMARK 465 SER C 1 REMARK 465 GLY C 238 REMARK 465 GLU C 239 REMARK 465 CYS C 240 REMARK 465 MET D -22 REMARK 465 LYS D -21 REMARK 465 LYS D -20 REMARK 465 ASN D -19 REMARK 465 ILE D -18 REMARK 465 ALA D -17 REMARK 465 PHE D -16 REMARK 465 LEU D -15 REMARK 465 LEU D -14 REMARK 465 ALA D -13 REMARK 465 SER D -12 REMARK 465 MET D -11 REMARK 465 PHE D -10 REMARK 465 VAL D -9 REMARK 465 PHE D -8 REMARK 465 SER D -7 REMARK 465 ILE D -6 REMARK 465 ALA D -5 REMARK 465 THR D -4 REMARK 465 ASN D -3 REMARK 465 ALA D -2 REMARK 465 TYR D -1 REMARK 465 ALA D 0 REMARK 465 GLU D 1 REMARK 465 ILE D 2 REMARK 465 SER D 3 REMARK 465 LYS D 168 REMARK 465 SER D 169 REMARK 465 THR D 170 REMARK 465 SER D 171 REMARK 465 GLY D 172 REMARK 465 LYS D 253 REMARK 465 SER D 254 REMARK 465 CYS D 255 REMARK 465 ASP D 256 REMARK 465 LYS D 257 REMARK 465 THR D 258 REMARK 465 HIS D 259 REMARK 465 THR D 260 REMARK 465 MET A -22 REMARK 465 LYS A -21 REMARK 465 LYS A -20 REMARK 465 ASN A -19 REMARK 465 ILE A -18 REMARK 465 ALA A -17 REMARK 465 PHE A -16 REMARK 465 LEU A -15 REMARK 465 LEU A -14 REMARK 465 ALA A -13 REMARK 465 SER A -12 REMARK 465 MET A -11 REMARK 465 PHE A -10 REMARK 465 VAL A -9 REMARK 465 PHE A -8 REMARK 465 SER A -7 REMARK 465 ILE A -6 REMARK 465 ALA A -5 REMARK 465 THR A -4 REMARK 465 ASN A -3 REMARK 465 ALA A -2 REMARK 465 TYR A -1 REMARK 465 ALA A 0 REMARK 465 GLY A 238 REMARK 465 GLU A 239 REMARK 465 CYS A 240 REMARK 465 MET B -22 REMARK 465 LYS B -21 REMARK 465 LYS B -20 REMARK 465 ASN B -19 REMARK 465 ILE B -18 REMARK 465 ALA B -17 REMARK 465 PHE B -16 REMARK 465 LEU B -15 REMARK 465 LEU B -14 REMARK 465 ALA B -13 REMARK 465 SER B -12 REMARK 465 MET B -11 REMARK 465 PHE B -10 REMARK 465 VAL B -9 REMARK 465 PHE B -8 REMARK 465 SER B -7 REMARK 465 ILE B -6 REMARK 465 ALA B -5 REMARK 465 THR B -4 REMARK 465 ASN B -3 REMARK 465 ALA B -2 REMARK 465 TYR B -1 REMARK 465 ALA B 0 REMARK 465 GLU B 1 REMARK 465 ILE B 2 REMARK 465 SER B 3 REMARK 465 SER B 167 REMARK 465 LYS B 168 REMARK 465 SER B 169 REMARK 465 THR B 170 REMARK 465 SER B 171 REMARK 465 GLY B 172 REMARK 465 LYS B 253 REMARK 465 SER B 254 REMARK 465 CYS B 255 REMARK 465 ASP B 256 REMARK 465 LYS B 257 REMARK 465 THR B 258 REMARK 465 HIS B 259 REMARK 465 THR B 260 REMARK 465 MET E -22 REMARK 465 LYS E -21 REMARK 465 LYS E -20 REMARK 465 ASN E -19 REMARK 465 ILE E -18 REMARK 465 ALA E -17 REMARK 465 PHE E -16 REMARK 465 LEU E -15 REMARK 465 LEU E -14 REMARK 465 ALA E -13 REMARK 465 SER E -12 REMARK 465 MET E -11 REMARK 465 PHE E -10 REMARK 465 VAL E -9 REMARK 465 PHE E -8 REMARK 465 SER E -7 REMARK 465 ILE E -6 REMARK 465 ALA E -5 REMARK 465 THR E -4 REMARK 465 ASN E -3 REMARK 465 ALA E -2 REMARK 465 TYR E -1 REMARK 465 ALA E 0 REMARK 465 GLY E 238 REMARK 465 GLU E 239 REMARK 465 CYS E 240 REMARK 465 MET F -22 REMARK 465 LYS F -21 REMARK 465 LYS F -20 REMARK 465 ASN F -19 REMARK 465 ILE F -18 REMARK 465 ALA F -17 REMARK 465 PHE F -16 REMARK 465 LEU F -15 REMARK 465 LEU F -14 REMARK 465 ALA F -13 REMARK 465 SER F -12 REMARK 465 MET F -11 REMARK 465 PHE F -10 REMARK 465 VAL F -9 REMARK 465 PHE F -8 REMARK 465 SER F -7 REMARK 465 ILE F -6 REMARK 465 ALA F -5 REMARK 465 THR F -4 REMARK 465 ASN F -3 REMARK 465 ALA F -2 REMARK 465 TYR F -1 REMARK 465 ALA F 0 REMARK 465 GLU F 1 REMARK 465 ILE F 2 REMARK 465 SER F 3 REMARK 465 LYS F 168 REMARK 465 SER F 169 REMARK 465 THR F 170 REMARK 465 SER F 171 REMARK 465 GLY F 172 REMARK 465 LYS F 253 REMARK 465 SER F 254 REMARK 465 CYS F 255 REMARK 465 ASP F 256 REMARK 465 LYS F 257 REMARK 465 THR F 258 REMARK 465 HIS F 259 REMARK 465 THR F 260 REMARK 465 MET G 191 REMARK 465 SER G 192 REMARK 465 THR G 193 REMARK 465 ASP G 194 REMARK 465 ILE G 195 REMARK 465 GLU G 196 REMARK 465 LYS G 197 REMARK 465 GLU G 198 REMARK 465 ILE G 199 REMARK 465 LEU G 200 REMARK 465 PRO G 323 REMARK 465 ARG G 324 REMARK 465 MET I 191 REMARK 465 SER I 192 REMARK 465 THR I 193 REMARK 465 ASP I 194 REMARK 465 ILE I 195 REMARK 465 GLU I 196 REMARK 465 LYS I 197 REMARK 465 GLU I 198 REMARK 465 VAL I 322 REMARK 465 PRO I 323 REMARK 465 ARG I 324 REMARK 465 MET H 191 REMARK 465 SER H 192 REMARK 465 THR H 193 REMARK 465 ASP H 194 REMARK 465 ILE H 195 REMARK 465 GLU H 196 REMARK 465 PRO H 323 REMARK 465 ARG H 324 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER A 1 OG REMARK 470 SER E 1 OG REMARK 470 LYS F 248 CG CD CE NZ REMARK 470 LYS F 249 CG CD CE NZ REMARK 470 VAL F 250 CG1 CG2 REMARK 470 GLU F 251 CG CD OE1 OE2 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 HH11 ARG B 45 O HOH B 301 1.33 REMARK 500 HG SER A 203 O HOH A 302 1.45 REMARK 500 HE ARG A 168 O HOH A 307 1.53 REMARK 500 HE21 GLN C 52 O HOH C 301 1.53 REMARK 500 O HIS A 215 HE ARG A 237 1.54 REMARK 500 HG1 THR G 212 O HOH G 401 1.54 REMARK 500 O HOH G 436 O HOH G 438 1.85 REMARK 500 O HOH C 334 O HOH C 336 2.01 REMARK 500 OD1 ASN A 184 O HOH A 301 2.03 REMARK 500 OG SER A 203 O HOH A 302 2.04 REMARK 500 O HOH C 323 O HOH C 337 2.08 REMARK 500 NH1 ARG B 45 O HOH B 301 2.12 REMARK 500 O HOH G 439 O HOH H 434 2.13 REMARK 500 O HOH C 316 O HOH C 340 2.15 REMARK 500 O PHE E 108 O HOH E 301 2.15 REMARK 500 O HOH E 319 O HOH E 332 2.18 REMARK 500 OG SER D 56 O HOH D 301 2.18 REMARK 500 O SER E 234 O HOH E 302 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH H 437 O HOH H 437 2553 1.87 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 VAL C 159 CB VAL C 159 CG2 0.129 REMARK 500 LYS C 171 CG LYS C 171 CD 0.267 REMARK 500 LYS C 171 CD LYS C 171 CE 0.388 REMARK 500 LYS C 171 CE LYS C 171 NZ 0.380 REMARK 500 LYS C 195 CD LYS C 195 CE 0.314 REMARK 500 LYS C 195 CE LYS C 195 NZ 0.273 REMARK 500 SER D 227 CB SER D 227 OG 0.098 REMARK 500 LYS B 69 CD LYS B 69 CE 0.254 REMARK 500 THR B 232 CB THR B 232 CG2 0.353 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 VAL C 159 CG1 - CB - CG2 ANGL. DEV. = 19.4 DEGREES REMARK 500 CYS C 160 CA - CB - SG ANGL. DEV. = 8.4 DEGREES REMARK 500 LYS C 171 CD - CE - NZ ANGL. DEV. = -29.0 DEGREES REMARK 500 LYS C 195 CD - CE - NZ ANGL. DEV. = -34.0 DEGREES REMARK 500 SER D 227 CB - CA - C ANGL. DEV. = 13.9 DEGREES REMARK 500 SER A 228 CB - CA - C ANGL. DEV. = -13.4 DEGREES REMARK 500 SER A 228 N - CA - CB ANGL. DEV. = 9.2 DEGREES REMARK 500 LYS B 69 CA - CB - CG ANGL. DEV. = 19.3 DEGREES REMARK 500 THR B 232 OG1 - CB - CG2 ANGL. DEV. = -19.6 DEGREES REMARK 500 THR B 232 CA - CB - CG2 ANGL. DEV. = -17.2 DEGREES REMARK 500 LEU E 151 CA - CB - CG ANGL. DEV. = 14.8 DEGREES REMARK 500 GLN F 39 N - CA - CB ANGL. DEV. = 15.1 DEGREES REMARK 500 GLN F 39 CA - CB - CG ANGL. DEV. = 18.0 DEGREES REMARK 500 LYS F 102 CD - CE - NZ ANGL. DEV. = -14.0 DEGREES REMARK 500 LYS F 156 CA - CB - CG ANGL. DEV. = 13.8 DEGREES REMARK 500 ASP H 292 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER C 55 -130.01 47.96 REMARK 500 ALA C 76 -43.63 76.27 REMARK 500 ASN C 164 67.69 63.58 REMARK 500 ASN D 130 -149.40 -123.01 REMARK 500 SER D 227 21.72 -78.25 REMARK 500 ASN D 243 27.89 49.78 REMARK 500 SER A 55 -128.76 48.11 REMARK 500 ALA A 76 -44.13 76.25 REMARK 500 ASN A 164 69.60 62.50 REMARK 500 LYS B 69 -147.40 -152.01 REMARK 500 ASN B 130 -144.90 -124.32 REMARK 500 HIS B 133 19.32 58.80 REMARK 500 ASP B 183 67.58 62.07 REMARK 500 THR B 230 -64.42 -100.03 REMARK 500 ASP E 2 79.33 -101.78 REMARK 500 SER E 55 -129.05 47.25 REMARK 500 ALA E 76 -41.08 74.88 REMARK 500 SER E 147 -162.22 -111.42 REMARK 500 SER E 149 12.83 -65.79 REMARK 500 SER E 153 3.55 34.67 REMARK 500 ASN E 164 67.13 61.16 REMARK 500 ALA F 118 164.73 178.53 REMARK 500 ASN F 130 -147.22 -118.00 REMARK 500 SER F 166 -78.96 -128.99 REMARK 500 ASP F 183 71.42 61.19 REMARK 500 SER F 227 3.35 -66.96 REMARK 500 THR F 230 -60.83 -95.35 REMARK 500 LYS F 245 72.10 -150.72 REMARK 500 PHE G 268 -4.23 76.33 REMARK 500 PHE I 268 -3.92 73.78 REMARK 500 VAL I 282 -50.27 -122.47 REMARK 500 ILE H 199 65.64 60.44 REMARK 500 PHE H 268 -10.03 66.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG C 168 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 341 DISTANCE = 5.87 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9IHC RELATED DB: PDB REMARK 900 RELATED ID: EMD-52864 RELATED DB: EMDB DBREF 9PZI C -22 240 PDB 9PZI 9PZI -22 240 DBREF 9PZI D -22 260 PDB 9PZI 9PZI -22 260 DBREF 9PZI A -22 240 PDB 9PZI 9PZI -22 240 DBREF 9PZI B -22 260 PDB 9PZI 9PZI -22 260 DBREF 9PZI E -22 240 PDB 9PZI 9PZI -22 240 DBREF 9PZI F -22 260 PDB 9PZI 9PZI -22 260 DBREF 9PZI G 192 319 UNP P01558 ELTB_CLOPF 192 319 DBREF 9PZI I 192 319 UNP P01558 ELTB_CLOPF 192 319 DBREF 9PZI H 192 319 UNP P01558 ELTB_CLOPF 192 319 SEQADV 9PZI MET G 191 UNP P01558 INITIATING METHIONINE SEQADV 9PZI GLY G 320 UNP P01558 EXPRESSION TAG SEQADV 9PZI LEU G 321 UNP P01558 EXPRESSION TAG SEQADV 9PZI VAL G 322 UNP P01558 EXPRESSION TAG SEQADV 9PZI PRO G 323 UNP P01558 EXPRESSION TAG SEQADV 9PZI ARG G 324 UNP P01558 EXPRESSION TAG SEQADV 9PZI MET I 191 UNP P01558 INITIATING METHIONINE SEQADV 9PZI GLY I 320 UNP P01558 EXPRESSION TAG SEQADV 9PZI LEU I 321 UNP P01558 EXPRESSION TAG SEQADV 9PZI VAL I 322 UNP P01558 EXPRESSION TAG SEQADV 9PZI PRO I 323 UNP P01558 EXPRESSION TAG SEQADV 9PZI ARG I 324 UNP P01558 EXPRESSION TAG SEQADV 9PZI MET H 191 UNP P01558 INITIATING METHIONINE SEQADV 9PZI GLY H 320 UNP P01558 EXPRESSION TAG SEQADV 9PZI LEU H 321 UNP P01558 EXPRESSION TAG SEQADV 9PZI VAL H 322 UNP P01558 EXPRESSION TAG SEQADV 9PZI PRO H 323 UNP P01558 EXPRESSION TAG SEQADV 9PZI ARG H 324 UNP P01558 EXPRESSION TAG SEQRES 1 C 239 MET LYS LYS ASN ILE ALA PHE LEU LEU ALA SER MET PHE SEQRES 2 C 239 VAL PHE SER ILE ALA THR ASN ALA TYR ALA SER ASP ILE SEQRES 3 C 239 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 4 C 239 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SER SEQRES 5 C 239 VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 6 C 239 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SER LEU SEQRES 7 C 239 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER ARG SER SEQRES 8 C 239 GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN PRO SEQRES 9 C 239 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER TYR GLU SEQRES 10 C 239 TRP ALA PRO VAL THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 11 C 239 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 12 C 239 PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SER SEQRES 13 C 239 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 14 C 239 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 15 C 239 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 16 C 239 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 17 C 239 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 18 C 239 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 19 C 239 ASN ARG GLY GLU CYS SEQRES 1 D 260 MET LYS LYS ASN ILE ALA PHE LEU LEU ALA SER MET PHE SEQRES 2 D 260 VAL PHE SER ILE ALA THR ASN ALA TYR ALA GLU ILE SER SEQRES 3 D 260 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 4 D 260 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 5 D 260 PHE ASN PHE SER SER SER SER ILE HIS TRP VAL ARG GLN SEQRES 6 D 260 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 7 D 260 SER TYR SER GLY TYR THR SER TYR ALA ASP SER VAL LYS SEQRES 8 D 260 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 9 D 260 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 10 D 260 ALA VAL TYR TYR CYS ALA ARG TYR TRP SER TRP TYR ASN SEQRES 11 D 260 SER SER HIS TYR ILE TYR SER ALA LEU ASP TYR TRP GLY SEQRES 12 D 260 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS SEQRES 13 D 260 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 14 D 260 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 15 D 260 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 16 D 260 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 17 D 260 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 18 D 260 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 19 D 260 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 20 D 260 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 A 239 MET LYS LYS ASN ILE ALA PHE LEU LEU ALA SER MET PHE SEQRES 2 A 239 VAL PHE SER ILE ALA THR ASN ALA TYR ALA SER ASP ILE SEQRES 3 A 239 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 4 A 239 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SER SEQRES 5 A 239 VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 6 A 239 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SER LEU SEQRES 7 A 239 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER ARG SER SEQRES 8 A 239 GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN PRO SEQRES 9 A 239 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER TYR GLU SEQRES 10 A 239 TRP ALA PRO VAL THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 11 A 239 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 12 A 239 PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SER SEQRES 13 A 239 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 14 A 239 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 15 A 239 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 16 A 239 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 17 A 239 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 18 A 239 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 19 A 239 ASN ARG GLY GLU CYS SEQRES 1 B 260 MET LYS LYS ASN ILE ALA PHE LEU LEU ALA SER MET PHE SEQRES 2 B 260 VAL PHE SER ILE ALA THR ASN ALA TYR ALA GLU ILE SER SEQRES 3 B 260 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 4 B 260 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 5 B 260 PHE ASN PHE SER SER SER SER ILE HIS TRP VAL ARG GLN SEQRES 6 B 260 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 7 B 260 SER TYR SER GLY TYR THR SER TYR ALA ASP SER VAL LYS SEQRES 8 B 260 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 9 B 260 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 10 B 260 ALA VAL TYR TYR CYS ALA ARG TYR TRP SER TRP TYR ASN SEQRES 11 B 260 SER SER HIS TYR ILE TYR SER ALA LEU ASP TYR TRP GLY SEQRES 12 B 260 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS SEQRES 13 B 260 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 14 B 260 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 15 B 260 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 16 B 260 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 17 B 260 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 18 B 260 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 19 B 260 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 20 B 260 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 E 239 MET LYS LYS ASN ILE ALA PHE LEU LEU ALA SER MET PHE SEQRES 2 E 239 VAL PHE SER ILE ALA THR ASN ALA TYR ALA SER ASP ILE SEQRES 3 E 239 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 4 E 239 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SER SEQRES 5 E 239 VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 6 E 239 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SER LEU SEQRES 7 E 239 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER ARG SER SEQRES 8 E 239 GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN PRO SEQRES 9 E 239 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER TYR GLU SEQRES 10 E 239 TRP ALA PRO VAL THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 11 E 239 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 12 E 239 PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SER SEQRES 13 E 239 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 14 E 239 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 15 E 239 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 16 E 239 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 17 E 239 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 18 E 239 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 19 E 239 ASN ARG GLY GLU CYS SEQRES 1 F 260 MET LYS LYS ASN ILE ALA PHE LEU LEU ALA SER MET PHE SEQRES 2 F 260 VAL PHE SER ILE ALA THR ASN ALA TYR ALA GLU ILE SER SEQRES 3 F 260 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 4 F 260 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 5 F 260 PHE ASN PHE SER SER SER SER ILE HIS TRP VAL ARG GLN SEQRES 6 F 260 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 7 F 260 SER TYR SER GLY TYR THR SER TYR ALA ASP SER VAL LYS SEQRES 8 F 260 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 9 F 260 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 10 F 260 ALA VAL TYR TYR CYS ALA ARG TYR TRP SER TRP TYR ASN SEQRES 11 F 260 SER SER HIS TYR ILE TYR SER ALA LEU ASP TYR TRP GLY SEQRES 12 F 260 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS SEQRES 13 F 260 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 14 F 260 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 15 F 260 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 16 F 260 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 17 F 260 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 18 F 260 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 19 F 260 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 20 F 260 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 G 134 MET SER THR ASP ILE GLU LYS GLU ILE LEU ASP LEU ALA SEQRES 2 G 134 ALA ALA THR GLU ARG LEU ASN LEU THR ASP ALA LEU ASN SEQRES 3 G 134 SER ASN PRO ALA GLY ASN LEU TYR ASP TRP ARG SER SER SEQRES 4 G 134 ASN SER TYR PRO TRP THR GLN LYS LEU ASN LEU HIS LEU SEQRES 5 G 134 THR ILE THR ALA THR GLY GLN LYS TYR ARG ILE LEU ALA SEQRES 6 G 134 SER LYS ILE VAL ASP PHE ASN ILE TYR SER ASN ASN PHE SEQRES 7 G 134 ASN ASN LEU VAL LYS LEU GLU GLN SER LEU GLY ASP GLY SEQRES 8 G 134 VAL LYS ASP HIS TYR VAL ASP ILE SER LEU ASP ALA GLY SEQRES 9 G 134 GLN TYR VAL LEU VAL MET LYS ALA ASN SER SER TYR SER SEQRES 10 G 134 GLY ASN TYR PRO TYR SER ILE LEU PHE GLN LYS PHE GLY SEQRES 11 G 134 LEU VAL PRO ARG SEQRES 1 I 134 MET SER THR ASP ILE GLU LYS GLU ILE LEU ASP LEU ALA SEQRES 2 I 134 ALA ALA THR GLU ARG LEU ASN LEU THR ASP ALA LEU ASN SEQRES 3 I 134 SER ASN PRO ALA GLY ASN LEU TYR ASP TRP ARG SER SER SEQRES 4 I 134 ASN SER TYR PRO TRP THR GLN LYS LEU ASN LEU HIS LEU SEQRES 5 I 134 THR ILE THR ALA THR GLY GLN LYS TYR ARG ILE LEU ALA SEQRES 6 I 134 SER LYS ILE VAL ASP PHE ASN ILE TYR SER ASN ASN PHE SEQRES 7 I 134 ASN ASN LEU VAL LYS LEU GLU GLN SER LEU GLY ASP GLY SEQRES 8 I 134 VAL LYS ASP HIS TYR VAL ASP ILE SER LEU ASP ALA GLY SEQRES 9 I 134 GLN TYR VAL LEU VAL MET LYS ALA ASN SER SER TYR SER SEQRES 10 I 134 GLY ASN TYR PRO TYR SER ILE LEU PHE GLN LYS PHE GLY SEQRES 11 I 134 LEU VAL PRO ARG SEQRES 1 H 134 MET SER THR ASP ILE GLU LYS GLU ILE LEU ASP LEU ALA SEQRES 2 H 134 ALA ALA THR GLU ARG LEU ASN LEU THR ASP ALA LEU ASN SEQRES 3 H 134 SER ASN PRO ALA GLY ASN LEU TYR ASP TRP ARG SER SER SEQRES 4 H 134 ASN SER TYR PRO TRP THR GLN LYS LEU ASN LEU HIS LEU SEQRES 5 H 134 THR ILE THR ALA THR GLY GLN LYS TYR ARG ILE LEU ALA SEQRES 6 H 134 SER LYS ILE VAL ASP PHE ASN ILE TYR SER ASN ASN PHE SEQRES 7 H 134 ASN ASN LEU VAL LYS LEU GLU GLN SER LEU GLY ASP GLY SEQRES 8 H 134 VAL LYS ASP HIS TYR VAL ASP ILE SER LEU ASP ALA GLY SEQRES 9 H 134 GLN TYR VAL LEU VAL MET LYS ALA ASN SER SER TYR SER SEQRES 10 H 134 GLY ASN TYR PRO TYR SER ILE LEU PHE GLN LYS PHE GLY SEQRES 11 H 134 LEU VAL PRO ARG FORMUL 10 HOH *323(H2 O) HELIX 1 AA1 GLN C 104 PHE C 108 5 5 HELIX 2 AA2 SER C 147 LYS C 152 1 6 HELIX 3 AA3 LYS C 209 HIS C 215 1 7 HELIX 4 AA4 ASN D 54 SER D 57 5 4 HELIX 5 AA5 THR D 100 LYS D 102 5 3 HELIX 6 AA6 ARG D 113 THR D 117 5 5 HELIX 7 AA7 SER D 195 ALA D 197 5 3 HELIX 8 AA8 LYS D 240 ASN D 243 5 4 HELIX 9 AA9 GLN A 104 PHE A 108 5 5 HELIX 10 AB1 SER A 147 SER A 153 1 7 HELIX 11 AB2 LYS A 209 HIS A 215 1 7 HELIX 12 AB3 ASN B 54 SER B 57 5 4 HELIX 13 AB4 ARG B 113 THR B 117 5 5 HELIX 14 AB5 SER B 195 ALA B 197 5 3 HELIX 15 AB6 SER B 226 LEU B 228 5 3 HELIX 16 AB7 LYS B 240 ASN B 243 5 4 HELIX 17 AB8 GLN E 104 PHE E 108 5 5 HELIX 18 AB9 SER E 147 SER E 153 5 7 HELIX 19 AC1 LYS E 209 HIS E 215 1 7 HELIX 20 AC2 ASN F 54 SER F 57 5 4 HELIX 21 AC3 THR F 100 LYS F 102 5 3 HELIX 22 AC4 ARG F 113 THR F 117 5 5 HELIX 23 AC5 SER F 195 ALA F 197 5 3 HELIX 24 AC6 SER F 226 GLY F 229 5 4 HELIX 25 AC7 HIS F 239 ASN F 243 5 5 HELIX 26 AC8 LEU G 211 SER G 217 1 7 HELIX 27 AC9 LEU I 211 SER I 217 1 7 HELIX 28 AD1 LEU H 211 SER H 217 1 7 SHEET 1 AA1 4 MET C 5 SER C 8 0 SHEET 2 AA1 4 VAL C 44 ALA C 50 -1 O THR C 47 N SER C 8 SHEET 3 AA1 4 ASP C 95 ILE C 100 -1 O LEU C 98 N ILE C 46 SHEET 4 AA1 4 PHE C 87 SER C 92 -1 N SER C 90 O THR C 97 SHEET 1 AA2 6 SER C 11 SER C 39 0 SHEET 2 AA2 6 THR C 128 LYS C 133 1 O GLU C 131 N LEU C 12 SHEET 3 AA2 6 ALA C 109 GLN C 115 -1 N ALA C 109 O VAL C 130 SHEET 4 AA2 6 VAL C 58 GLN C 63 -1 N TYR C 61 O TYR C 112 SHEET 5 AA2 6 LYS C 70 TYR C 74 -1 O LEU C 72 N TRP C 60 SHEET 6 AA2 6 SER C 78 LEU C 79 -1 O SER C 78 N TYR C 74 SHEET 1 AA3 4 SER C 11 SER C 39 0 SHEET 2 AA3 4 THR C 128 LYS C 133 1 O GLU C 131 N LEU C 12 SHEET 3 AA3 4 ALA C 109 GLN C 115 -1 N ALA C 109 O VAL C 130 SHEET 4 AA3 4 THR C 123 PHE C 124 -1 O THR C 123 N GLN C 115 SHEET 1 AA4 4 SER C 140 PHE C 144 0 SHEET 2 AA4 4 THR C 155 PHE C 165 -1 O LEU C 161 N PHE C 142 SHEET 3 AA4 4 TYR C 199 SER C 208 -1 O TYR C 199 N PHE C 165 SHEET 4 AA4 4 SER C 185 VAL C 189 -1 N GLN C 186 O THR C 204 SHEET 1 AA5 4 ALA C 179 LEU C 180 0 SHEET 2 AA5 4 LYS C 171 VAL C 176 -1 N VAL C 176 O ALA C 179 SHEET 3 AA5 4 VAL C 217 THR C 223 -1 O GLU C 221 N GLN C 173 SHEET 4 AA5 4 VAL C 231 ASN C 236 -1 O VAL C 231 N VAL C 222 SHEET 1 AA6 4 GLN D 6 SER D 10 0 SHEET 2 AA6 4 LEU D 44 SER D 51 -1 O SER D 51 N GLN D 6 SHEET 3 AA6 4 THR D 104 MET D 109 -1 O MET D 109 N LEU D 44 SHEET 4 AA6 4 PHE D 94 ASP D 99 -1 N THR D 95 O GLN D 108 SHEET 1 AA7 6 GLY D 13 VAL D 38 0 SHEET 2 AA7 6 THR D 146 VAL D 150 1 O THR D 149 N GLY D 13 SHEET 3 AA7 6 ALA D 118 TRP D 128 -1 N TYR D 120 O THR D 146 SHEET 4 AA7 6 SER D 59 GLN D 65 -1 N VAL D 63 O TYR D 121 SHEET 5 AA7 6 GLU D 72 SER D 78 -1 O ALA D 75 N TRP D 62 SHEET 6 AA7 6 THR D 84 TYR D 86 -1 O SER D 85 N SER D 76 SHEET 1 AA8 4 GLY D 13 VAL D 38 0 SHEET 2 AA8 4 THR D 146 VAL D 150 1 O THR D 149 N GLY D 13 SHEET 3 AA8 4 ALA D 118 TRP D 128 -1 N TYR D 120 O THR D 146 SHEET 4 AA8 4 TYR D 136 TRP D 142 -1 O ALA D 138 N TRP D 126 SHEET 1 AA9 4 SER D 159 LEU D 163 0 SHEET 2 AA9 4 THR D 174 TYR D 184 -1 O LEU D 180 N PHE D 161 SHEET 3 AA9 4 TYR D 215 PRO D 224 -1 O LEU D 217 N VAL D 181 SHEET 4 AA9 4 VAL D 202 THR D 204 -1 N HIS D 203 O VAL D 220 SHEET 1 AB1 4 SER D 159 LEU D 163 0 SHEET 2 AB1 4 THR D 174 TYR D 184 -1 O LEU D 180 N PHE D 161 SHEET 3 AB1 4 TYR D 215 PRO D 224 -1 O LEU D 217 N VAL D 181 SHEET 4 AB1 4 VAL D 208 LEU D 209 -1 N VAL D 208 O SER D 216 SHEET 1 AB2 3 THR D 190 TRP D 193 0 SHEET 2 AB2 3 TYR D 233 HIS D 239 -1 O ASN D 238 N THR D 190 SHEET 3 AB2 3 THR D 244 VAL D 250 -1 O VAL D 250 N TYR D 233 SHEET 1 AB3 4 MET A 5 SER A 8 0 SHEET 2 AB3 4 VAL A 44 ALA A 50 -1 O THR A 47 N SER A 8 SHEET 3 AB3 4 ASP A 95 ILE A 100 -1 O LEU A 98 N ILE A 46 SHEET 4 AB3 4 PHE A 87 SER A 92 -1 N SER A 90 O THR A 97 SHEET 1 AB4 6 SER A 11 SER A 39 0 SHEET 2 AB4 6 THR A 128 LYS A 133 1 O GLU A 131 N LEU A 12 SHEET 3 AB4 6 ALA A 109 GLN A 115 -1 N TYR A 111 O THR A 128 SHEET 4 AB4 6 VAL A 58 GLN A 63 -1 N GLN A 63 O THR A 110 SHEET 5 AB4 6 LYS A 70 TYR A 74 -1 O LEU A 72 N TRP A 60 SHEET 6 AB4 6 SER A 78 LEU A 79 -1 O SER A 78 N TYR A 74 SHEET 1 AB5 4 SER A 11 SER A 39 0 SHEET 2 AB5 4 THR A 128 LYS A 133 1 O GLU A 131 N LEU A 12 SHEET 3 AB5 4 ALA A 109 GLN A 115 -1 N TYR A 111 O THR A 128 SHEET 4 AB5 4 THR A 123 PHE A 124 -1 O THR A 123 N GLN A 115 SHEET 1 AB6 4 SER A 140 PHE A 144 0 SHEET 2 AB6 4 THR A 155 PHE A 165 -1 O LEU A 161 N PHE A 142 SHEET 3 AB6 4 TYR A 199 SER A 208 -1 O LEU A 207 N ALA A 156 SHEET 4 AB6 4 SER A 185 VAL A 189 -1 N GLN A 186 O THR A 204 SHEET 1 AB7 4 ALA A 179 LEU A 180 0 SHEET 2 AB7 4 LYS A 171 VAL A 176 -1 N VAL A 176 O ALA A 179 SHEET 3 AB7 4 VAL A 217 THR A 223 -1 O THR A 223 N LYS A 171 SHEET 4 AB7 4 VAL A 231 ASN A 236 -1 O VAL A 231 N VAL A 222 SHEET 1 AB8 4 GLN B 6 SER B 10 0 SHEET 2 AB8 4 LEU B 44 SER B 51 -1 O SER B 51 N GLN B 6 SHEET 3 AB8 4 THR B 104 MET B 109 -1 O MET B 109 N LEU B 44 SHEET 4 AB8 4 PHE B 94 ASP B 99 -1 N THR B 95 O GLN B 108 SHEET 1 AB9 6 LEU B 14 VAL B 38 0 SHEET 2 AB9 6 THR B 146 VAL B 150 1 O THR B 149 N VAL B 38 SHEET 3 AB9 6 ALA B 118 TRP B 128 -1 N ALA B 118 O VAL B 148 SHEET 4 AB9 6 SER B 59 GLN B 65 -1 N VAL B 63 O TYR B 121 SHEET 5 AB9 6 LEU B 71 SER B 78 -1 O GLU B 72 N ARG B 64 SHEET 6 AB9 6 THR B 84 TYR B 86 -1 O SER B 85 N SER B 76 SHEET 1 AC1 4 LEU B 14 VAL B 38 0 SHEET 2 AC1 4 THR B 146 VAL B 150 1 O THR B 149 N VAL B 38 SHEET 3 AC1 4 ALA B 118 TRP B 128 -1 N ALA B 118 O VAL B 148 SHEET 4 AC1 4 TYR B 136 TRP B 142 -1 O ALA B 138 N TRP B 126 SHEET 1 AC2 4 SER B 159 LEU B 163 0 SHEET 2 AC2 4 THR B 174 TYR B 184 -1 O LEU B 180 N PHE B 161 SHEET 3 AC2 4 TYR B 215 PRO B 224 -1 O LEU B 217 N VAL B 181 SHEET 4 AC2 4 VAL B 202 THR B 204 -1 N HIS B 203 O VAL B 220 SHEET 1 AC3 4 SER B 159 LEU B 163 0 SHEET 2 AC3 4 THR B 174 TYR B 184 -1 O LEU B 180 N PHE B 161 SHEET 3 AC3 4 TYR B 215 PRO B 224 -1 O LEU B 217 N VAL B 181 SHEET 4 AC3 4 VAL B 208 LEU B 209 -1 N VAL B 208 O SER B 216 SHEET 1 AC4 3 THR B 190 TRP B 193 0 SHEET 2 AC4 3 TYR B 233 HIS B 239 -1 O ASN B 238 N THR B 190 SHEET 3 AC4 3 THR B 244 VAL B 250 -1 O VAL B 250 N TYR B 233 SHEET 1 AC5 4 MET E 5 SER E 8 0 SHEET 2 AC5 4 VAL E 44 ALA E 50 -1 O THR E 47 N SER E 8 SHEET 3 AC5 4 ASP E 95 ILE E 100 -1 O PHE E 96 N CYS E 48 SHEET 4 AC5 4 PHE E 87 SER E 92 -1 N SER E 90 O THR E 97 SHEET 1 AC6 6 SER E 11 SER E 39 0 SHEET 2 AC6 6 THR E 128 LYS E 133 1 O GLU E 131 N LEU E 12 SHEET 3 AC6 6 ALA E 109 GLN E 115 -1 N TYR E 111 O THR E 128 SHEET 4 AC6 6 VAL E 58 GLN E 63 -1 N GLN E 63 O THR E 110 SHEET 5 AC6 6 PRO E 69 TYR E 74 -1 O LYS E 70 N GLN E 62 SHEET 6 AC6 6 SER E 78 LEU E 79 -1 O SER E 78 N TYR E 74 SHEET 1 AC7 4 SER E 11 SER E 39 0 SHEET 2 AC7 4 THR E 128 LYS E 133 1 O GLU E 131 N LEU E 12 SHEET 3 AC7 4 ALA E 109 GLN E 115 -1 N TYR E 111 O THR E 128 SHEET 4 AC7 4 THR E 123 PHE E 124 -1 O THR E 123 N GLN E 115 SHEET 1 AC8 4 SER E 140 PHE E 144 0 SHEET 2 AC8 4 THR E 155 PHE E 165 -1 O LEU E 161 N PHE E 142 SHEET 3 AC8 4 TYR E 199 SER E 208 -1 O TYR E 199 N PHE E 165 SHEET 4 AC8 4 SER E 185 VAL E 189 -1 N SER E 188 O SER E 202 SHEET 1 AC9 4 ALA E 179 LEU E 180 0 SHEET 2 AC9 4 LYS E 171 VAL E 176 -1 N VAL E 176 O ALA E 179 SHEET 3 AC9 4 VAL E 217 THR E 223 -1 O GLU E 221 N GLN E 173 SHEET 4 AC9 4 VAL E 231 ASN E 236 -1 O PHE E 235 N TYR E 218 SHEET 1 AD1 4 GLN F 6 SER F 10 0 SHEET 2 AD1 4 LEU F 44 SER F 51 -1 O SER F 47 N SER F 10 SHEET 3 AD1 4 THR F 104 MET F 109 -1 O MET F 109 N LEU F 44 SHEET 4 AD1 4 PHE F 94 ASP F 99 -1 N THR F 95 O GLN F 108 SHEET 1 AD2 6 GLY F 13 VAL F 38 0 SHEET 2 AD2 6 THR F 146 VAL F 150 1 O THR F 149 N GLY F 13 SHEET 3 AD2 6 ALA F 118 TRP F 128 -1 N TYR F 120 O THR F 146 SHEET 4 AD2 6 SER F 59 GLN F 65 -1 N VAL F 63 O TYR F 121 SHEET 5 AD2 6 LEU F 71 SER F 78 -1 O VAL F 74 N TRP F 62 SHEET 6 AD2 6 THR F 84 TYR F 86 -1 O SER F 85 N SER F 76 SHEET 1 AD3 4 GLY F 13 VAL F 38 0 SHEET 2 AD3 4 THR F 146 VAL F 150 1 O THR F 149 N GLY F 13 SHEET 3 AD3 4 ALA F 118 TRP F 128 -1 N TYR F 120 O THR F 146 SHEET 4 AD3 4 TYR F 136 TRP F 142 -1 O TYR F 141 N ARG F 124 SHEET 1 AD4 4 SER F 159 LEU F 163 0 SHEET 2 AD4 4 THR F 174 TYR F 184 -1 O GLY F 178 N LEU F 163 SHEET 3 AD4 4 TYR F 215 PRO F 224 -1 O LEU F 217 N VAL F 181 SHEET 4 AD4 4 VAL F 202 THR F 204 -1 N HIS F 203 O VAL F 220 SHEET 1 AD5 4 SER F 159 LEU F 163 0 SHEET 2 AD5 4 THR F 174 TYR F 184 -1 O GLY F 178 N LEU F 163 SHEET 3 AD5 4 TYR F 215 PRO F 224 -1 O LEU F 217 N VAL F 181 SHEET 4 AD5 4 VAL F 208 LEU F 209 -1 N VAL F 208 O SER F 216 SHEET 1 AD6 3 THR F 190 TRP F 193 0 SHEET 2 AD6 3 TYR F 233 ASN F 238 -1 O ASN F 238 N THR F 190 SHEET 3 AD6 3 LYS F 249 VAL F 250 -1 O VAL F 250 N TYR F 233 SHEET 1 AD7 5 ALA G 205 ASN G 210 0 SHEET 2 AD7 5 LEU G 238 ILE G 244 1 O HIS G 241 N GLU G 207 SHEET 3 AD7 5 GLY G 294 ALA G 302 -1 O LEU G 298 N LEU G 240 SHEET 4 AD7 5 VAL G 259 ASN G 266 -1 N ASP G 260 O LYS G 301 SHEET 5 AD7 5 LEU G 271 SER G 277 -1 O LEU G 274 N ILE G 263 SHEET 1 AD8 4 LEU G 223 ARG G 227 0 SHEET 2 AD8 4 SER G 313 LYS G 318 -1 O ILE G 314 N TRP G 226 SHEET 3 AD8 4 GLN G 249 ALA G 255 -1 N LEU G 254 O LEU G 315 SHEET 4 AD8 4 HIS G 285 LEU G 291 -1 O ILE G 289 N TYR G 251 SHEET 1 AD9 5 ALA I 205 ASN I 210 0 SHEET 2 AD9 5 LEU I 238 ILE I 244 1 O HIS I 241 N GLU I 207 SHEET 3 AD9 5 GLY I 294 ALA I 302 -1 O LEU I 298 N LEU I 240 SHEET 4 AD9 5 VAL I 259 ASN I 266 -1 N ASP I 260 O LYS I 301 SHEET 5 AD9 5 LEU I 271 SER I 277 -1 O LEU I 274 N ILE I 263 SHEET 1 AE1 4 LEU I 223 ARG I 227 0 SHEET 2 AE1 4 SER I 313 LYS I 318 -1 O PHE I 316 N TYR I 224 SHEET 3 AE1 4 GLN I 249 ALA I 255 -1 N LEU I 254 O LEU I 315 SHEET 4 AE1 4 HIS I 285 LEU I 291 -1 O ILE I 289 N TYR I 251 SHEET 1 AE2 5 ALA H 205 ASN H 210 0 SHEET 2 AE2 5 LEU H 238 ILE H 244 1 O HIS H 241 N GLU H 207 SHEET 3 AE2 5 GLY H 294 ALA H 302 -1 O LEU H 298 N LEU H 240 SHEET 4 AE2 5 VAL H 259 ASN H 266 -1 N ASN H 262 O VAL H 299 SHEET 5 AE2 5 LEU H 271 SER H 277 -1 O SER H 277 N PHE H 261 SHEET 1 AE3 4 LEU H 223 ARG H 227 0 SHEET 2 AE3 4 SER H 313 LYS H 318 -1 O PHE H 316 N TYR H 224 SHEET 3 AE3 4 GLN H 249 ALA H 255 -1 N LEU H 254 O LEU H 315 SHEET 4 AE3 4 HIS H 285 LEU H 291 -1 O ILE H 289 N TYR H 251 SHEET 1 AE4 2 TYR H 232 PRO H 233 0 SHEET 2 AE4 2 ASN H 309 TYR H 310 -1 O TYR H 310 N TYR H 232 SSBOND 1 CYS C 48 CYS C 113 1555 1555 2.18 SSBOND 2 CYS C 160 CYS C 220 1555 1555 2.06 SSBOND 3 CYS D 48 CYS D 122 1555 1555 2.09 SSBOND 4 CYS D 179 CYS D 235 1555 1555 2.04 SSBOND 5 CYS A 48 CYS A 113 1555 1555 2.11 SSBOND 6 CYS A 160 CYS A 220 1555 1555 2.05 SSBOND 7 CYS B 48 CYS B 122 1555 1555 2.10 SSBOND 8 CYS B 179 CYS B 235 1555 1555 2.06 SSBOND 9 CYS E 48 CYS E 113 1555 1555 2.12 SSBOND 10 CYS E 160 CYS E 220 1555 1555 2.06 SSBOND 11 CYS F 48 CYS F 122 1555 1555 2.09 SSBOND 12 CYS F 179 CYS F 235 1555 1555 2.04 CISPEP 1 SER C 8 PRO C 9 0 -9.49 CISPEP 2 TYR C 166 PRO C 167 0 -2.94 CISPEP 3 PHE D 185 PRO D 186 0 1.05 CISPEP 4 GLU D 187 PRO D 188 0 2.98 CISPEP 5 SER A 8 PRO A 9 0 -8.24 CISPEP 6 TYR A 166 PRO A 167 0 -2.67 CISPEP 7 PHE B 185 PRO B 186 0 -1.04 CISPEP 8 GLU B 187 PRO B 188 0 2.70 CISPEP 9 SER E 8 PRO E 9 0 -10.25 CISPEP 10 TYR E 166 PRO E 167 0 -3.18 CISPEP 11 PHE F 185 PRO F 186 0 -0.12 CISPEP 12 GLU F 187 PRO F 188 0 3.44 CRYST1 111.475 198.520 115.800 90.00 109.72 90.00 I 1 2 1 12 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008971 0.000000 0.003215 0.00000 SCALE2 0.000000 0.005037 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009174 0.00000