HEADER IMMUNE SYSTEM 31-JUL-25 9PUK TITLE NEUTRALIZING MONOCLONAL ANTIBODY FAB FRAGMENT FOR HUMAN LEPTIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUTRALIZING MONOCLONAL ANTIBODY FAB FRAGMENT FOR HUMAN COMPND 3 LEPTIN, HEAVY CHAIN; COMPND 4 CHAIN: A, C; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NEUTRALIZING MONOCLONAL ANTIBODY FAB FRAGMENT FOR HUMAN COMPND 8 LEPTIN, LIGHT CHAIN; COMPND 9 CHAIN: B, D; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK293F KEYWDS ANTIBODY, FAB, LEPTIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR D.R.TOMCHICK,R.M.WYNN,P.E.SCHERER REVDAT 1 05-NOV-25 9PUK 0 JRNL AUTH X.N.SUN,S.CHEN,S.ZHAO,J.B.FUNCKE,M.VIROSTEK,L.PEDERSEN,C.LI, JRNL AUTH 2 C.JOUNG,Q.LIN,Y.LI,A.COBB,M.Y.WANG,K.MIN,L.MAYA-RAMOS, JRNL AUTH 3 G.DEGASPERI,J.LIU,N.ZHANG,Z.AN,D.R.TOMCHICK,R.M.WYNN,D.Y.OH, JRNL AUTH 4 P.E.SCHERER JRNL TITL LEPTIN AS A KEY DRIVER FOR ORGAN FIBROGENESIS. JRNL REF SCI ADV V. 11 Y7904 2025 JRNL REFN ESSN 2375-2548 JRNL PMID 41124259 JRNL DOI 10.1126/SCIADV.ADY7904 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.33 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 3 NUMBER OF REFLECTIONS : 15683 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.273 REMARK 3 R VALUE (WORKING SET) : 0.267 REMARK 3 FREE R VALUE : 0.320 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.050 REMARK 3 FREE R VALUE TEST SET COUNT : 1576 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 49.3300 - 7.3300 1.00 1475 169 0.2831 0.3246 REMARK 3 2 7.3300 - 5.8200 1.00 1399 155 0.2996 0.3655 REMARK 3 3 5.8200 - 5.0900 1.00 1375 155 0.2577 0.2868 REMARK 3 4 5.0900 - 4.6200 1.00 1359 151 0.2293 0.2887 REMARK 3 5 4.6200 - 4.2900 1.00 1366 153 0.2285 0.2792 REMARK 3 6 4.2900 - 4.0400 1.00 1343 150 0.2433 0.2954 REMARK 3 7 4.0400 - 3.8400 1.00 1360 144 0.2671 0.2918 REMARK 3 8 3.8400 - 3.6700 1.00 1327 156 0.2764 0.3571 REMARK 3 9 3.6700 - 3.5300 1.00 1349 145 0.2933 0.3644 REMARK 3 10 3.5300 - 3.4100 0.87 1162 137 0.3017 0.3542 REMARK 3 11 3.4100 - 3.3000 0.45 592 61 0.3157 0.3823 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) : 0.478 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.018 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 47.74 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.28 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 6400 REMARK 3 ANGLE : 0.536 8718 REMARK 3 CHIRALITY : 0.046 984 REMARK 3 PLANARITY : 0.005 1114 REMARK 3 DIHEDRAL : 11.802 2258 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 21 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.6244 21.3031 -26.5766 REMARK 3 T TENSOR REMARK 3 T11: 0.6251 T22: 0.6085 REMARK 3 T33: 0.7082 T12: 0.0085 REMARK 3 T13: -0.0597 T23: -0.0618 REMARK 3 L TENSOR REMARK 3 L11: 0.9265 L22: 2.0467 REMARK 3 L33: 1.5127 L12: 0.1833 REMARK 3 L13: 0.0762 L23: 0.2016 REMARK 3 S TENSOR REMARK 3 S11: -0.4533 S12: 0.8879 S13: -0.3809 REMARK 3 S21: -0.4266 S22: 0.0107 S23: 0.1105 REMARK 3 S31: 0.1590 S32: -0.0581 S33: 0.2163 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 100 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.2558 29.7756 -22.7839 REMARK 3 T TENSOR REMARK 3 T11: 0.5552 T22: 0.4540 REMARK 3 T33: 0.3523 T12: 0.0852 REMARK 3 T13: -0.1025 T23: 0.0822 REMARK 3 L TENSOR REMARK 3 L11: 0.2683 L22: 1.5438 REMARK 3 L33: 0.3762 L12: -0.5500 REMARK 3 L13: -0.1142 L23: -0.2086 REMARK 3 S TENSOR REMARK 3 S11: 0.1150 S12: 0.0729 S13: -0.2389 REMARK 3 S21: -0.3398 S22: 0.3640 S23: 0.5887 REMARK 3 S31: -0.5465 S32: -0.3093 S33: -0.1000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 154 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.4982 54.9363 -13.4356 REMARK 3 T TENSOR REMARK 3 T11: -0.6298 T22: 1.2935 REMARK 3 T33: 0.2797 T12: -0.1240 REMARK 3 T13: 0.4507 T23: 0.3140 REMARK 3 L TENSOR REMARK 3 L11: 0.5356 L22: 0.3884 REMARK 3 L33: 0.5517 L12: -0.0803 REMARK 3 L13: -0.2881 L23: 0.1540 REMARK 3 S TENSOR REMARK 3 S11: 0.0019 S12: -0.2996 S13: 0.3351 REMARK 3 S21: 0.4899 S22: 0.0060 S23: -0.0823 REMARK 3 S31: -0.1629 S32: -0.1937 S33: -0.1814 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 155 THROUGH 184 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.9465 45.8690 -14.8702 REMARK 3 T TENSOR REMARK 3 T11: 0.4207 T22: 0.3644 REMARK 3 T33: 0.2645 T12: 0.0355 REMARK 3 T13: -0.0802 T23: 0.1531 REMARK 3 L TENSOR REMARK 3 L11: 2.1874 L22: 2.2229 REMARK 3 L33: 1.0436 L12: 0.1994 REMARK 3 L13: -0.0921 L23: 0.4726 REMARK 3 S TENSOR REMARK 3 S11: 0.0056 S12: -0.3134 S13: -0.1552 REMARK 3 S21: 0.2458 S22: 0.2622 S23: 0.4295 REMARK 3 S31: 0.3612 S32: 0.3501 S33: -0.0728 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 185 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.2893 52.5139 -16.5324 REMARK 3 T TENSOR REMARK 3 T11: 0.3129 T22: 0.7015 REMARK 3 T33: 0.3694 T12: -0.0746 REMARK 3 T13: 0.0292 T23: 0.0299 REMARK 3 L TENSOR REMARK 3 L11: 2.3351 L22: 1.4457 REMARK 3 L33: 2.1921 L12: 0.6340 REMARK 3 L13: 1.0851 L23: 0.2159 REMARK 3 S TENSOR REMARK 3 S11: 0.0093 S12: -0.2460 S13: 0.7877 REMARK 3 S21: -0.0075 S22: -0.3567 S23: 0.2923 REMARK 3 S31: -0.5621 S32: 0.2851 S33: 0.1632 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 50 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.6284 16.1454 -4.0859 REMARK 3 T TENSOR REMARK 3 T11: 0.8518 T22: 0.5905 REMARK 3 T33: 1.0002 T12: -0.0554 REMARK 3 T13: 0.0607 T23: -0.0262 REMARK 3 L TENSOR REMARK 3 L11: 0.8365 L22: 0.3741 REMARK 3 L33: 1.0338 L12: 0.3861 REMARK 3 L13: 0.1578 L23: 0.2590 REMARK 3 S TENSOR REMARK 3 S11: -0.3550 S12: -0.2263 S13: -0.4405 REMARK 3 S21: 0.4142 S22: 0.2328 S23: 1.1091 REMARK 3 S31: 0.2010 S32: 0.3881 S33: 0.0815 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 51 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.9382 12.3292 -5.2759 REMARK 3 T TENSOR REMARK 3 T11: 1.2681 T22: 1.5642 REMARK 3 T33: 1.2788 T12: 0.1766 REMARK 3 T13: -0.5444 T23: -0.2869 REMARK 3 L TENSOR REMARK 3 L11: 0.4062 L22: 0.0631 REMARK 3 L33: 0.2575 L12: -0.1546 REMARK 3 L13: -0.3270 L23: 0.1269 REMARK 3 S TENSOR REMARK 3 S11: -0.1146 S12: 0.4941 S13: -0.9185 REMARK 3 S21: -0.0171 S22: -0.0393 S23: 0.2192 REMARK 3 S31: 0.5181 S32: -0.4584 S33: -0.0258 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 77 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.1617 10.4253 -0.0028 REMARK 3 T TENSOR REMARK 3 T11: 1.1789 T22: -0.0077 REMARK 3 T33: 1.5279 T12: 0.1133 REMARK 3 T13: -0.3293 T23: 0.2614 REMARK 3 L TENSOR REMARK 3 L11: 0.3157 L22: 1.0366 REMARK 3 L33: 0.2975 L12: 0.2861 REMARK 3 L13: -0.1487 L23: -0.5497 REMARK 3 S TENSOR REMARK 3 S11: -0.2603 S12: -0.2067 S13: 0.0612 REMARK 3 S21: 0.3743 S22: 0.1396 S23: -0.3981 REMARK 3 S31: 0.1020 S32: -0.1461 S33: -0.1960 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 105 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.3559 16.5361 -7.9814 REMARK 3 T TENSOR REMARK 3 T11: 0.5508 T22: 0.3439 REMARK 3 T33: 0.7989 T12: -0.0625 REMARK 3 T13: 0.1098 T23: -0.1103 REMARK 3 L TENSOR REMARK 3 L11: 0.4849 L22: 1.8836 REMARK 3 L33: 2.2708 L12: -0.7106 REMARK 3 L13: -0.8146 L23: 0.2604 REMARK 3 S TENSOR REMARK 3 S11: -0.3782 S12: -0.2766 S13: -0.6249 REMARK 3 S21: 0.2397 S22: 0.0684 S23: 1.0556 REMARK 3 S31: 0.0839 S32: -0.3446 S33: 0.1512 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 106 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.5208 33.2954 5.2993 REMARK 3 T TENSOR REMARK 3 T11: 0.5125 T22: 0.7400 REMARK 3 T33: 0.3788 T12: 0.0260 REMARK 3 T13: -0.0223 T23: 0.1202 REMARK 3 L TENSOR REMARK 3 L11: 3.6207 L22: 2.7107 REMARK 3 L33: 2.0878 L12: -1.5086 REMARK 3 L13: -2.4264 L23: 0.0241 REMARK 3 S TENSOR REMARK 3 S11: -0.6626 S12: -0.1392 S13: -0.6773 REMARK 3 S21: -0.1399 S22: -0.3826 S23: 0.1055 REMARK 3 S31: 0.6206 S32: -0.0521 S33: 0.1645 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.6191 60.7841 -11.9089 REMARK 3 T TENSOR REMARK 3 T11: 0.6812 T22: 0.7581 REMARK 3 T33: 0.5433 T12: 0.5688 REMARK 3 T13: 0.2334 T23: 0.3667 REMARK 3 L TENSOR REMARK 3 L11: 0.6407 L22: 3.7848 REMARK 3 L33: 0.6463 L12: -0.5723 REMARK 3 L13: 0.6398 L23: -0.8402 REMARK 3 S TENSOR REMARK 3 S11: 0.5279 S12: 0.9525 S13: 0.3576 REMARK 3 S21: -1.2099 S22: -0.4025 S23: 0.4741 REMARK 3 S31: -0.6499 S32: -0.4440 S33: -0.1183 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 135 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.8245 49.6193 -0.2409 REMARK 3 T TENSOR REMARK 3 T11: 0.6031 T22: 0.6655 REMARK 3 T33: 0.2857 T12: -0.0757 REMARK 3 T13: 0.0301 T23: 0.0386 REMARK 3 L TENSOR REMARK 3 L11: 2.5940 L22: 2.0042 REMARK 3 L33: 0.9616 L12: 0.2432 REMARK 3 L13: -0.7389 L23: 0.0236 REMARK 3 S TENSOR REMARK 3 S11: 0.1661 S12: 0.7568 S13: 0.3258 REMARK 3 S21: 0.8057 S22: 0.0077 S23: 0.2627 REMARK 3 S31: 0.3542 S32: -0.6721 S33: -0.0552 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 156 THROUGH 176 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.7382 47.2491 -2.5186 REMARK 3 T TENSOR REMARK 3 T11: 0.5202 T22: 0.8855 REMARK 3 T33: 0.3745 T12: 0.1260 REMARK 3 T13: 0.2218 T23: 0.0411 REMARK 3 L TENSOR REMARK 3 L11: 0.9450 L22: 1.3081 REMARK 3 L33: 0.9617 L12: 0.5776 REMARK 3 L13: 0.6699 L23: 1.0244 REMARK 3 S TENSOR REMARK 3 S11: -0.0814 S12: 0.7300 S13: -0.3491 REMARK 3 S21: 0.3098 S22: 0.3680 S23: 0.2165 REMARK 3 S31: 0.3876 S32: -0.6757 S33: 0.2195 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 177 THROUGH 192 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.3925 58.3595 -8.1956 REMARK 3 T TENSOR REMARK 3 T11: 1.0643 T22: 0.6975 REMARK 3 T33: 0.2662 T12: 0.1965 REMARK 3 T13: -0.1377 T23: -0.0027 REMARK 3 L TENSOR REMARK 3 L11: 2.3262 L22: 1.0408 REMARK 3 L33: 2.8458 L12: 0.9033 REMARK 3 L13: -1.7808 L23: 0.3416 REMARK 3 S TENSOR REMARK 3 S11: 0.4184 S12: -0.1694 S13: 0.6061 REMARK 3 S21: 0.2187 S22: 0.1844 S23: 0.0921 REMARK 3 S31: -1.1754 S32: -1.0351 S33: 0.2367 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 193 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.4714 57.5791 3.3834 REMARK 3 T TENSOR REMARK 3 T11: 1.0547 T22: 0.8591 REMARK 3 T33: 0.3200 T12: 0.1372 REMARK 3 T13: 0.0261 T23: -0.2563 REMARK 3 L TENSOR REMARK 3 L11: 2.3664 L22: 3.0535 REMARK 3 L33: 1.3006 L12: 0.2562 REMARK 3 L13: -0.5373 L23: -1.1816 REMARK 3 S TENSOR REMARK 3 S11: 0.3624 S12: -0.1008 S13: 0.4999 REMARK 3 S21: 0.3189 S22: -0.2060 S23: 0.3264 REMARK 3 S31: -0.6553 S32: -1.4631 S33: -0.0383 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.9627 18.6484 -11.4499 REMARK 3 T TENSOR REMARK 3 T11: 0.7140 T22: 0.8262 REMARK 3 T33: 0.8054 T12: -0.2395 REMARK 3 T13: -0.2374 T23: 0.4580 REMARK 3 L TENSOR REMARK 3 L11: 1.7138 L22: 0.7314 REMARK 3 L33: 2.6161 L12: 0.3876 REMARK 3 L13: 0.7551 L23: 1.0698 REMARK 3 S TENSOR REMARK 3 S11: 0.0397 S12: -1.4693 S13: -1.1371 REMARK 3 S21: 0.2040 S22: -0.2239 S23: -0.4729 REMARK 3 S31: 0.7843 S32: -1.5316 S33: -0.7139 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 129 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.1040 48.5473 -22.0002 REMARK 3 T TENSOR REMARK 3 T11: 0.1338 T22: 0.3500 REMARK 3 T33: 0.2120 T12: 0.0383 REMARK 3 T13: 0.0289 T23: 0.0958 REMARK 3 L TENSOR REMARK 3 L11: 2.4559 L22: 1.4507 REMARK 3 L33: 1.8994 L12: -0.7297 REMARK 3 L13: 0.2763 L23: 0.7558 REMARK 3 S TENSOR REMARK 3 S11: -0.0420 S12: -0.2295 S13: 0.1959 REMARK 3 S21: 0.1331 S22: 0.2125 S23: 0.2378 REMARK 3 S31: 0.0952 S32: -0.6290 S33: -0.0409 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.0879 12.5984 -33.8542 REMARK 3 T TENSOR REMARK 3 T11: 0.8033 T22: 0.2727 REMARK 3 T33: 1.0008 T12: -0.1440 REMARK 3 T13: 0.0691 T23: 0.0034 REMARK 3 L TENSOR REMARK 3 L11: 0.6110 L22: 0.2081 REMARK 3 L33: 0.8175 L12: -0.3378 REMARK 3 L13: -0.0956 L23: 0.1163 REMARK 3 S TENSOR REMARK 3 S11: -0.4768 S12: 0.4399 S13: -0.4469 REMARK 3 S21: -0.9944 S22: 0.5660 S23: 0.0634 REMARK 3 S31: 0.1206 S32: 0.0662 S33: -0.0524 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 95 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.9171 17.9265 -32.4477 REMARK 3 T TENSOR REMARK 3 T11: 0.8868 T22: 0.2370 REMARK 3 T33: 0.6516 T12: -0.1461 REMARK 3 T13: 0.0070 T23: -0.1647 REMARK 3 L TENSOR REMARK 3 L11: 0.6347 L22: 0.3050 REMARK 3 L33: 0.4199 L12: 0.3311 REMARK 3 L13: -0.3058 L23: 0.0518 REMARK 3 S TENSOR REMARK 3 S11: -0.1782 S12: -0.0688 S13: -0.6873 REMARK 3 S21: 0.0665 S22: 0.0668 S23: -0.7191 REMARK 3 S31: 0.6773 S32: 0.1824 S33: -0.1874 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 119 THROUGH 192 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.4985 49.7704 -30.8545 REMARK 3 T TENSOR REMARK 3 T11: 0.1546 T22: 0.1899 REMARK 3 T33: 0.1632 T12: -0.0841 REMARK 3 T13: -0.1063 T23: -0.1462 REMARK 3 L TENSOR REMARK 3 L11: 2.3680 L22: 2.0186 REMARK 3 L33: 3.3604 L12: 0.0218 REMARK 3 L13: -0.2531 L23: -0.2503 REMARK 3 S TENSOR REMARK 3 S11: -0.0381 S12: -0.4741 S13: -0.0810 REMARK 3 S21: 0.2596 S22: -0.0202 S23: -0.3757 REMARK 3 S31: 0.6736 S32: 0.3647 S33: -0.0323 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 193 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.5789 54.0988 -39.4015 REMARK 3 T TENSOR REMARK 3 T11: 0.3675 T22: 0.1304 REMARK 3 T33: 0.0992 T12: -0.1034 REMARK 3 T13: 0.1320 T23: 0.2593 REMARK 3 L TENSOR REMARK 3 L11: 1.3698 L22: 2.5615 REMARK 3 L33: 2.2178 L12: -0.7399 REMARK 3 L13: -0.2303 L23: 0.4120 REMARK 3 S TENSOR REMARK 3 S11: 0.1965 S12: -0.0741 S13: 0.3608 REMARK 3 S21: -0.9630 S22: -0.1736 S23: -0.5247 REMARK 3 S31: -0.2472 S32: 0.7420 S33: -0.0382 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 2 through 100 or REMARK 3 resid 108 through 222)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 2 through 100 or REMARK 3 resid 108 through 135 or resid 143 REMARK 3 through 222)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "B" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "D" and (resid 3 through 57 or REMARK 3 resid 60 through 213)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9PUK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000298454. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-JUN-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17545 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 21.40 REMARK 200 R MERGE (I) : 0.16400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 7.60 REMARK 200 R MERGE FOR SHELL (I) : 1.43900 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.91 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: FAB AT 25 MG/ML IN 20 MM HEPES, PH REMARK 280 7.4, 75 MM NACL VERSUS 1.0 M LITHIUM CHLORIDE, 0.1 M CITRATE PH REMARK 280 4.0, 20% (W/V) PEG 6,000., VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 35.10750 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 103.97050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.10750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 103.97050 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: DIMERIC 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC 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 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 GLN A 1 REMARK 465 PRO A 102 REMARK 465 SER A 103 REMARK 465 SER A 104 REMARK 465 TYR A 105 REMARK 465 TYR A 106 REMARK 465 TYR A 107 REMARK 465 SER A 136 REMARK 465 SER A 137 REMARK 465 LYS A 138 REMARK 465 SER A 139 REMARK 465 THR A 140 REMARK 465 SER A 141 REMARK 465 GLY A 142 REMARK 465 LYS A 223 REMARK 465 SER A 224 REMARK 465 CYS A 225 REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 SER B 58 REMARK 465 GLY B 59 REMARK 465 GLY B 112 REMARK 465 GLN B 113 REMARK 465 ALA B 214 REMARK 465 GLU B 215 REMARK 465 CYS B 216 REMARK 465 SER B 217 REMARK 465 GLN C 1 REMARK 465 VAL C 101 REMARK 465 PRO C 102 REMARK 465 SER C 103 REMARK 465 SER C 104 REMARK 465 TYR C 105 REMARK 465 SER C 224 REMARK 465 CYS C 225 REMARK 465 GLN D 1 REMARK 465 GLY D 112 REMARK 465 GLN D 113 REMARK 465 ALA D 214 REMARK 465 GLU D 215 REMARK 465 CYS D 216 REMARK 465 SER D 217 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN B 28 -90.40 -116.74 REMARK 500 ALA B 31 1.14 80.52 REMARK 500 ASP B 53 -27.42 77.79 REMARK 500 THR B 54 1.74 -151.77 REMARK 500 ALA B 86 173.47 178.41 REMARK 500 PRO B 146 -164.83 -73.58 REMARK 500 ASN B 175 -5.02 79.64 REMARK 500 LYS B 176 -154.89 -85.21 REMARK 500 THR C 140 31.36 -83.53 REMARK 500 ASP C 153 70.16 52.93 REMARK 500 ASN D 28 -90.50 -116.88 REMARK 500 ASP D 53 -28.05 76.29 REMARK 500 THR D 54 0.43 -150.57 REMARK 500 ALA D 86 173.19 178.11 REMARK 500 PRO D 146 -164.83 -72.94 REMARK 500 ASN D 175 -6.37 78.90 REMARK 500 LYS D 176 -154.82 -86.35 REMARK 500 REMARK 500 REMARK: NULL DBREF 9PUK A 1 225 PDB 9PUK 9PUK 1 225 DBREF 9PUK B 1 217 PDB 9PUK 9PUK 1 217 DBREF 9PUK C 1 225 PDB 9PUK 9PUK 1 225 DBREF 9PUK D 1 217 PDB 9PUK 9PUK 1 217 SEQRES 1 A 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 A 225 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 225 GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 A 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 A 225 PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE GLN SEQRES 6 A 225 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 A 225 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 A 225 ALA VAL TYR TYR CYS ALA ARG SER GLN VAL PRO SER SER SEQRES 9 A 225 TYR TYR TYR GLY MET ASP VAL TRP GLY GLN GLY THR MET SEQRES 10 A 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 A 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 A 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 A 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 A 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 A 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 A 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 A 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 A 225 PRO LYS SER CYS SEQRES 1 B 217 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 B 217 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY GLY ASN SEQRES 3 B 217 SER ASN ILE GLY ALA GLY TYR HIS VAL HIS TRP TYR GLN SEQRES 4 B 217 GLN LEU PRO GLY ALA ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 B 217 ASP THR ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 B 217 GLY SER GLN SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 B 217 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 B 217 SER TYR ASP ARG SER ARG GLY GLY TRP PHE PHE GLY GLY SEQRES 9 B 217 GLY THR GLN LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 B 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 B 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU VAL SER ASP SEQRES 12 B 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 B 217 GLY SER PRO VAL LYS VAL GLY VAL GLU THR THR LYS PRO SEQRES 14 B 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 B 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 B 217 TYR SER CYS ARG VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 B 217 LYS THR VAL ALA PRO ALA GLU CYS SER SEQRES 1 C 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 C 225 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 C 225 GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 C 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 C 225 PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE GLN SEQRES 6 C 225 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 C 225 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 C 225 ALA VAL TYR TYR CYS ALA ARG SER GLN VAL PRO SER SER SEQRES 9 C 225 TYR TYR TYR GLY MET ASP VAL TRP GLY GLN GLY THR MET SEQRES 10 C 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 C 225 PRO LYS SER CYS SEQRES 1 D 217 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 D 217 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY GLY ASN SEQRES 3 D 217 SER ASN ILE GLY ALA GLY TYR HIS VAL HIS TRP TYR GLN SEQRES 4 D 217 GLN LEU PRO GLY ALA ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 D 217 ASP THR ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 D 217 GLY SER GLN SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 D 217 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 D 217 SER TYR ASP ARG SER ARG GLY GLY TRP PHE PHE GLY GLY SEQRES 9 D 217 GLY THR GLN LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 D 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 D 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU VAL SER ASP SEQRES 12 D 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 D 217 GLY SER PRO VAL LYS VAL GLY VAL GLU THR THR LYS PRO SEQRES 14 D 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 D 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 D 217 TYR SER CYS ARG VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 D 217 LYS THR VAL ALA PRO ALA GLU CYS SER HELIX 1 AA1 ARG A 87 THR A 91 5 5 HELIX 2 AA2 SER A 165 ALA A 167 5 3 HELIX 3 AA3 SER A 196 GLY A 199 5 4 HELIX 4 AA4 LYS A 210 ASN A 213 5 4 HELIX 5 AA5 GLN B 81 GLU B 85 5 5 HELIX 6 AA6 SER B 126 ALA B 132 1 7 HELIX 7 AA7 THR B 186 HIS B 193 1 8 HELIX 8 AA8 ARG C 87 THR C 91 5 5 HELIX 9 AA9 LYS C 138 GLY C 142 5 5 HELIX 10 AB1 SER C 165 ALA C 167 5 3 HELIX 11 AB2 SER C 196 GLY C 199 5 4 HELIX 12 AB3 LYS C 210 ASN C 213 5 4 HELIX 13 AB4 ILE D 29 TYR D 33 5 5 HELIX 14 AB5 GLN D 81 GLU D 85 5 5 HELIX 15 AB6 SER D 126 ALA D 132 1 7 HELIX 16 AB7 THR D 186 HIS D 193 1 8 SHEET 1 AA1 4 LEU A 4 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 ALA A 24 -1 O LYS A 23 N VAL A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O MET A 81 N VAL A 20 SHEET 4 AA1 4 VAL A 68 ASP A 73 -1 N THR A 69 O GLU A 82 SHEET 1 AA2 6 GLU A 10 LYS A 12 0 SHEET 2 AA2 6 THR A 116 VAL A 120 1 O THR A 119 N LYS A 12 SHEET 3 AA2 6 ALA A 92 GLN A 100 -1 N ALA A 92 O VAL A 118 SHEET 4 AA2 6 TYR A 32 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 52 -1 O ILE A 51 N ILE A 34 SHEET 6 AA2 6 THR A 57 TYR A 60 -1 O THR A 57 N ILE A 52 SHEET 1 AA3 4 GLU A 10 LYS A 12 0 SHEET 2 AA3 4 THR A 116 VAL A 120 1 O THR A 119 N LYS A 12 SHEET 3 AA3 4 ALA A 92 GLN A 100 -1 N ALA A 92 O VAL A 118 SHEET 4 AA3 4 VAL A 111 TRP A 112 -1 O VAL A 111 N ARG A 98 SHEET 1 AA4 4 SER A 129 LEU A 133 0 SHEET 2 AA4 4 THR A 144 TYR A 154 -1 O LYS A 152 N SER A 129 SHEET 3 AA4 4 TYR A 185 PRO A 194 -1 O TYR A 185 N TYR A 154 SHEET 4 AA4 4 VAL A 172 THR A 174 -1 N HIS A 173 O VAL A 190 SHEET 1 AA5 4 SER A 129 LEU A 133 0 SHEET 2 AA5 4 THR A 144 TYR A 154 -1 O LYS A 152 N SER A 129 SHEET 3 AA5 4 TYR A 185 PRO A 194 -1 O TYR A 185 N TYR A 154 SHEET 4 AA5 4 VAL A 178 LEU A 179 -1 N VAL A 178 O SER A 186 SHEET 1 AA6 3 THR A 160 TRP A 163 0 SHEET 2 AA6 3 ILE A 204 HIS A 209 -1 O ASN A 206 N SER A 162 SHEET 3 AA6 3 THR A 214 LYS A 219 -1 O VAL A 216 N VAL A 207 SHEET 1 AA7 5 SER B 9 GLY B 12 0 SHEET 2 AA7 5 THR B 106 VAL B 110 1 O THR B 109 N VAL B 10 SHEET 3 AA7 5 ALA B 86 ASP B 94 -1 N ALA B 86 O LEU B 108 SHEET 4 AA7 5 VAL B 35 GLN B 40 -1 N GLN B 40 O ASP B 87 SHEET 5 AA7 5 LYS B 47 ILE B 50 -1 O ILE B 50 N TRP B 37 SHEET 1 AA8 4 SER B 9 GLY B 12 0 SHEET 2 AA8 4 THR B 106 VAL B 110 1 O THR B 109 N VAL B 10 SHEET 3 AA8 4 ALA B 86 ASP B 94 -1 N ALA B 86 O LEU B 108 SHEET 4 AA8 4 GLY B 99 PHE B 102 -1 O PHE B 101 N SER B 92 SHEET 1 AA9 3 VAL B 18 THR B 23 0 SHEET 2 AA9 3 SER B 72 ILE B 77 -1 O ILE B 77 N VAL B 18 SHEET 3 AA9 3 PHE B 64 SER B 69 -1 N SER B 69 O SER B 72 SHEET 1 AB1 4 SER B 119 PHE B 123 0 SHEET 2 AB1 4 ALA B 135 PHE B 144 -1 O LEU B 140 N THR B 121 SHEET 3 AB1 4 TYR B 177 LEU B 185 -1 O SER B 181 N CYS B 139 SHEET 4 AB1 4 VAL B 164 THR B 166 -1 N GLU B 165 O TYR B 182 SHEET 1 AB2 4 SER B 119 PHE B 123 0 SHEET 2 AB2 4 ALA B 135 PHE B 144 -1 O LEU B 140 N THR B 121 SHEET 3 AB2 4 TYR B 177 LEU B 185 -1 O SER B 181 N CYS B 139 SHEET 4 AB2 4 SER B 170 LYS B 171 -1 N SER B 170 O ALA B 178 SHEET 1 AB3 4 SER B 158 VAL B 160 0 SHEET 2 AB3 4 THR B 150 ALA B 155 -1 N ALA B 155 O SER B 158 SHEET 3 AB3 4 TYR B 196 HIS B 202 -1 O ARG B 199 N ALA B 152 SHEET 4 AB3 4 SER B 205 VAL B 211 -1 O VAL B 207 N VAL B 200 SHEET 1 AB4 4 LEU C 4 GLN C 6 0 SHEET 2 AB4 4 VAL C 18 ALA C 24 -1 O LYS C 23 N VAL C 5 SHEET 3 AB4 4 THR C 78 LEU C 83 -1 O MET C 81 N VAL C 20 SHEET 4 AB4 4 VAL C 68 ASP C 73 -1 N THR C 69 O GLU C 82 SHEET 1 AB5 6 GLU C 10 LYS C 12 0 SHEET 2 AB5 6 THR C 116 VAL C 120 1 O THR C 119 N LYS C 12 SHEET 3 AB5 6 ALA C 92 SER C 99 -1 N ALA C 92 O VAL C 118 SHEET 4 AB5 6 ALA C 33 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AB5 6 LEU C 45 ILE C 52 -1 O ILE C 51 N ILE C 34 SHEET 6 AB5 6 THR C 57 TYR C 60 -1 O ASN C 59 N GLY C 50 SHEET 1 AB6 4 GLU C 10 LYS C 12 0 SHEET 2 AB6 4 THR C 116 VAL C 120 1 O THR C 119 N LYS C 12 SHEET 3 AB6 4 ALA C 92 SER C 99 -1 N ALA C 92 O VAL C 118 SHEET 4 AB6 4 VAL C 111 TRP C 112 -1 O VAL C 111 N ARG C 98 SHEET 1 AB7 4 SER C 129 LEU C 133 0 SHEET 2 AB7 4 THR C 144 TYR C 154 -1 O LYS C 152 N SER C 129 SHEET 3 AB7 4 TYR C 185 PRO C 194 -1 O TYR C 185 N TYR C 154 SHEET 4 AB7 4 VAL C 172 THR C 174 -1 N HIS C 173 O VAL C 190 SHEET 1 AB8 4 SER C 129 LEU C 133 0 SHEET 2 AB8 4 THR C 144 TYR C 154 -1 O LYS C 152 N SER C 129 SHEET 3 AB8 4 TYR C 185 PRO C 194 -1 O TYR C 185 N TYR C 154 SHEET 4 AB8 4 VAL C 178 LEU C 179 -1 N VAL C 178 O SER C 186 SHEET 1 AB9 3 THR C 160 TRP C 163 0 SHEET 2 AB9 3 ILE C 204 HIS C 209 -1 O ASN C 206 N SER C 162 SHEET 3 AB9 3 THR C 214 LYS C 219 -1 O VAL C 216 N VAL C 207 SHEET 1 AC1 5 SER D 9 GLY D 12 0 SHEET 2 AC1 5 THR D 106 VAL D 110 1 O THR D 109 N VAL D 10 SHEET 3 AC1 5 ALA D 86 ASP D 94 -1 N ALA D 86 O LEU D 108 SHEET 4 AC1 5 VAL D 35 GLN D 40 -1 N GLN D 40 O ASP D 87 SHEET 5 AC1 5 LYS D 47 ILE D 50 -1 O ILE D 50 N TRP D 37 SHEET 1 AC2 4 SER D 9 GLY D 12 0 SHEET 2 AC2 4 THR D 106 VAL D 110 1 O THR D 109 N VAL D 10 SHEET 3 AC2 4 ALA D 86 ASP D 94 -1 N ALA D 86 O LEU D 108 SHEET 4 AC2 4 GLY D 99 PHE D 102 -1 O PHE D 101 N SER D 92 SHEET 1 AC3 3 VAL D 18 THR D 23 0 SHEET 2 AC3 3 SER D 72 ILE D 77 -1 O LEU D 75 N ILE D 20 SHEET 3 AC3 3 PHE D 64 SER D 69 -1 N SER D 67 O SER D 74 SHEET 1 AC4 4 SER D 119 PHE D 123 0 SHEET 2 AC4 4 ALA D 135 PHE D 144 -1 O LEU D 140 N THR D 121 SHEET 3 AC4 4 TYR D 177 LEU D 185 -1 O SER D 181 N CYS D 139 SHEET 4 AC4 4 VAL D 164 THR D 166 -1 N GLU D 165 O TYR D 182 SHEET 1 AC5 4 SER D 119 PHE D 123 0 SHEET 2 AC5 4 ALA D 135 PHE D 144 -1 O LEU D 140 N THR D 121 SHEET 3 AC5 4 TYR D 177 LEU D 185 -1 O SER D 181 N CYS D 139 SHEET 4 AC5 4 SER D 170 LYS D 171 -1 N SER D 170 O ALA D 178 SHEET 1 AC6 4 SER D 158 PRO D 159 0 SHEET 2 AC6 4 THR D 150 ALA D 155 -1 N ALA D 155 O SER D 158 SHEET 3 AC6 4 TYR D 196 HIS D 202 -1 O ARG D 199 N ALA D 152 SHEET 4 AC6 4 SER D 205 VAL D 211 -1 O VAL D 207 N VAL D 200 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS A 149 CYS A 205 1555 1555 2.02 SSBOND 3 CYS B 22 CYS B 90 1555 1555 2.03 SSBOND 4 CYS B 139 CYS B 198 1555 1555 2.04 SSBOND 5 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 6 CYS C 149 CYS C 205 1555 1555 2.03 SSBOND 7 CYS D 22 CYS D 90 1555 1555 2.03 SSBOND 8 CYS D 139 CYS D 198 1555 1555 2.04 CISPEP 1 PHE A 155 PRO A 156 0 -5.06 CISPEP 2 GLU A 157 PRO A 158 0 -6.13 CISPEP 3 TYR B 145 PRO B 146 0 0.80 CISPEP 4 PHE C 155 PRO C 156 0 -5.16 CISPEP 5 GLU C 157 PRO C 158 0 -6.27 CISPEP 6 TYR D 145 PRO D 146 0 0.60 CRYST1 70.215 207.941 72.823 90.00 90.00 90.00 P 21 21 2 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 0.014242 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004809 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013732 0.00000 MTRIX1 1 -0.992497 0.108855 0.055677 1.03645 1 MTRIX2 1 0.110512 0.993492 0.027598 -4.90386 1 MTRIX3 1 -0.052311 0.033544 -0.998067 -36.90779 1 MTRIX1 2 -0.994462 0.089393 0.055270 1.82679 1 MTRIX2 2 0.091046 0.995449 0.028148 -4.59995 1 MTRIX3 2 -0.052502 0.033025 -0.998075 -37.17300 1