HEADER IMMUNE SYSTEM 06-SEP-22 8GSI TITLE STRUCTURE OF THE COBOLIMAB FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NANOBODY; COMPND 11 CHAIN: F; COMPND 12 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_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: CAMELUS BACTRIANUS; SOURCE 14 ORGANISM_TAXID: 9837; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COBOLIMAB, TIM-3. IMMUME CHECKPOINT, CANCER IMMUNOTHERAPY, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.S.HEO,S.B.CHOI REVDAT 1 06-SEP-23 8GSI 0 JRNL AUTH Y.S.HEO,S.B.CHOI JRNL TITL CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF COBOLIMAB, AN JRNL TITL 2 INVESTIGATIONAL ANTIBODY TARGETING TIM-3 FOR JRNL TITL 3 IMMUNE-ONCOLOGY. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.02 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20_4459 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) : 2.02 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.83 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 46864 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2344 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 29.8300 - 5.1900 1.00 2772 147 0.1820 0.2156 REMARK 3 2 5.1800 - 4.1200 1.00 2682 141 0.1560 0.1731 REMARK 3 3 4.1200 - 3.6000 1.00 2638 139 0.1745 0.2146 REMARK 3 4 3.6000 - 3.2700 1.00 2645 139 0.1842 0.2460 REMARK 3 5 3.2700 - 3.0400 1.00 2623 138 0.2058 0.2139 REMARK 3 6 3.0400 - 2.8600 1.00 2625 138 0.2191 0.2467 REMARK 3 7 2.8600 - 2.7100 1.00 2583 136 0.2261 0.2634 REMARK 3 8 2.7100 - 2.6000 1.00 2609 137 0.2249 0.3007 REMARK 3 9 2.6000 - 2.5000 1.00 2607 138 0.2253 0.2127 REMARK 3 10 2.5000 - 2.4100 1.00 2610 137 0.2365 0.3144 REMARK 3 11 2.4100 - 2.3400 1.00 2582 136 0.2450 0.3244 REMARK 3 12 2.3400 - 2.2700 1.00 2599 137 0.2461 0.2952 REMARK 3 13 2.2700 - 2.2100 1.00 2607 137 0.2412 0.2639 REMARK 3 14 2.2100 - 2.1500 1.00 2597 136 0.2352 0.3212 REMARK 3 15 2.1500 - 2.1100 1.00 2589 137 0.2458 0.2726 REMARK 3 16 2.1100 - 2.0600 1.00 2547 134 0.2567 0.2975 REMARK 3 17 2.0600 - 2.0200 1.00 2605 137 0.3003 0.3324 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) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.660 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.76 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.6216 59.4574 78.6331 REMARK 3 T TENSOR REMARK 3 T11: 0.5936 T22: 0.4970 REMARK 3 T33: 0.5192 T12: -0.0907 REMARK 3 T13: 0.1654 T23: -0.1307 REMARK 3 L TENSOR REMARK 3 L11: 7.1917 L22: 1.5910 REMARK 3 L33: 3.4242 L12: -1.0663 REMARK 3 L13: 0.3379 L23: -0.5510 REMARK 3 S TENSOR REMARK 3 S11: -0.4258 S12: -0.3333 S13: -0.4059 REMARK 3 S21: 0.4415 S22: 0.5347 S23: -0.0432 REMARK 3 S31: -0.4321 S32: 0.3323 S33: -0.1126 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 19 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.8779 67.0176 72.9870 REMARK 3 T TENSOR REMARK 3 T11: 0.6902 T22: 0.4740 REMARK 3 T33: 0.7260 T12: -0.2014 REMARK 3 T13: 0.3266 T23: -0.2783 REMARK 3 L TENSOR REMARK 3 L11: 4.4653 L22: 3.4793 REMARK 3 L33: 1.8129 L12: -0.7049 REMARK 3 L13: -2.2262 L23: -1.3631 REMARK 3 S TENSOR REMARK 3 S11: 0.2634 S12: -0.6721 S13: 0.7467 REMARK 3 S21: 0.4782 S22: 0.0452 S23: 0.0270 REMARK 3 S31: -0.7768 S32: 0.1733 S33: -0.2242 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 62 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.3664 61.4645 74.7568 REMARK 3 T TENSOR REMARK 3 T11: 0.5514 T22: 0.4640 REMARK 3 T33: 0.5331 T12: -0.1651 REMARK 3 T13: 0.2131 T23: -0.2216 REMARK 3 L TENSOR REMARK 3 L11: 3.6043 L22: 1.1561 REMARK 3 L33: 1.1020 L12: 1.1103 REMARK 3 L13: -1.8751 L23: -0.8176 REMARK 3 S TENSOR REMARK 3 S11: 0.4455 S12: -0.7361 S13: 0.7578 REMARK 3 S21: 0.2088 S22: -0.0785 S23: -0.0495 REMARK 3 S31: -0.4464 S32: 0.2735 S33: -0.3142 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 114 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.6251 33.6298 68.8182 REMARK 3 T TENSOR REMARK 3 T11: 0.3621 T22: 0.3963 REMARK 3 T33: 0.3776 T12: -0.1374 REMARK 3 T13: 0.0373 T23: -0.0816 REMARK 3 L TENSOR REMARK 3 L11: 3.5609 L22: 9.6709 REMARK 3 L33: 2.1092 L12: -3.7548 REMARK 3 L13: -1.2420 L23: 2.3349 REMARK 3 S TENSOR REMARK 3 S11: -0.0894 S12: 0.0335 S13: 0.0790 REMARK 3 S21: 0.4078 S22: 0.1805 S23: -0.9178 REMARK 3 S31: 0.1782 S32: -0.1260 S33: -0.0974 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.1459 24.8076 71.7949 REMARK 3 T TENSOR REMARK 3 T11: 0.5978 T22: 0.3671 REMARK 3 T33: 0.4351 T12: -0.1434 REMARK 3 T13: 0.1193 T23: -0.0829 REMARK 3 L TENSOR REMARK 3 L11: 2.6483 L22: 5.9050 REMARK 3 L33: 0.8761 L12: -2.9588 REMARK 3 L13: -0.9018 L23: 2.1308 REMARK 3 S TENSOR REMARK 3 S11: -0.3962 S12: 0.1598 S13: -0.6449 REMARK 3 S21: 1.1689 S22: -0.0633 S23: 0.4364 REMARK 3 S31: 0.7003 S32: -0.2591 S33: 0.4403 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 34 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.7531 59.4914 54.0068 REMARK 3 T TENSOR REMARK 3 T11: 0.4238 T22: 0.3695 REMARK 3 T33: 0.4773 T12: -0.1082 REMARK 3 T13: 0.1736 T23: -0.1187 REMARK 3 L TENSOR REMARK 3 L11: 1.9348 L22: 3.5183 REMARK 3 L33: 2.0737 L12: 0.2920 REMARK 3 L13: 0.1021 L23: -0.4434 REMARK 3 S TENSOR REMARK 3 S11: 0.1668 S12: 0.1297 S13: 0.2856 REMARK 3 S21: -0.5722 S22: -0.0203 S23: -0.6488 REMARK 3 S31: -0.4407 S32: 0.1442 S33: -0.1189 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 35 THROUGH 77 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.0929 58.6337 63.3149 REMARK 3 T TENSOR REMARK 3 T11: 0.4028 T22: 0.3133 REMARK 3 T33: 0.4778 T12: -0.1162 REMARK 3 T13: 0.1352 T23: -0.1091 REMARK 3 L TENSOR REMARK 3 L11: 3.9919 L22: 3.6308 REMARK 3 L33: 2.7468 L12: 0.1138 REMARK 3 L13: 1.0909 L23: 1.6997 REMARK 3 S TENSOR REMARK 3 S11: 0.2152 S12: -0.1787 S13: -0.0542 REMARK 3 S21: 0.2591 S22: -0.1109 S23: -0.3460 REMARK 3 S31: -0.0068 S32: 0.0813 S33: -0.1200 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.3125 45.8329 58.4705 REMARK 3 T TENSOR REMARK 3 T11: 0.3450 T22: 0.3288 REMARK 3 T33: 0.3303 T12: -0.0682 REMARK 3 T13: 0.1496 T23: -0.0830 REMARK 3 L TENSOR REMARK 3 L11: 1.7910 L22: 3.5155 REMARK 3 L33: 1.4749 L12: 0.8836 REMARK 3 L13: 0.2339 L23: 0.5268 REMARK 3 S TENSOR REMARK 3 S11: 0.1603 S12: -0.1591 S13: 0.2178 REMARK 3 S21: 0.0909 S22: -0.1115 S23: -0.1390 REMARK 3 S31: -0.0868 S32: -0.1303 S33: -0.0525 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 135 THROUGH 203 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.1920 36.9215 55.3727 REMARK 3 T TENSOR REMARK 3 T11: 0.3687 T22: 0.5085 REMARK 3 T33: 0.3206 T12: -0.0773 REMARK 3 T13: 0.0916 T23: -0.0598 REMARK 3 L TENSOR REMARK 3 L11: 4.1767 L22: 1.7534 REMARK 3 L33: 2.8216 L12: -0.2294 REMARK 3 L13: -3.9365 L23: -0.0331 REMARK 3 S TENSOR REMARK 3 S11: 0.0531 S12: 1.0210 S13: 0.1417 REMARK 3 S21: -0.1915 S22: -0.0085 S23: -0.1737 REMARK 3 S31: 0.0264 S32: -0.8637 S33: -0.0924 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 204 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.6566 28.6189 50.2621 REMARK 3 T TENSOR REMARK 3 T11: 0.5440 T22: 0.9696 REMARK 3 T33: 0.4764 T12: -0.3106 REMARK 3 T13: 0.1190 T23: -0.2300 REMARK 3 L TENSOR REMARK 3 L11: 5.3516 L22: 2.4410 REMARK 3 L33: 1.9655 L12: 1.6149 REMARK 3 L13: -3.1873 L23: -2.0647 REMARK 3 S TENSOR REMARK 3 S11: -0.5350 S12: 0.9371 S13: -0.4242 REMARK 3 S21: -0.4041 S22: 0.2481 S23: 0.1633 REMARK 3 S31: 0.6540 S32: -1.8040 S33: 0.2175 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 3 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.4153 47.9022 95.4713 REMARK 3 T TENSOR REMARK 3 T11: 0.6513 T22: 0.7027 REMARK 3 T33: 0.5535 T12: -0.1384 REMARK 3 T13: 0.2004 T23: -0.1656 REMARK 3 L TENSOR REMARK 3 L11: 9.9114 L22: 8.0784 REMARK 3 L33: 6.5391 L12: -4.4092 REMARK 3 L13: 1.7359 L23: -2.5017 REMARK 3 S TENSOR REMARK 3 S11: -0.2702 S12: -0.5421 S13: -1.1003 REMARK 3 S21: 1.1032 S22: 0.3872 S23: 1.5547 REMARK 3 S31: 0.6017 S32: -1.0753 S33: -0.2851 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 19 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.7292 49.4285 97.4842 REMARK 3 T TENSOR REMARK 3 T11: 1.0855 T22: 0.7575 REMARK 3 T33: 0.2791 T12: 0.0397 REMARK 3 T13: 0.0175 T23: -0.1546 REMARK 3 L TENSOR REMARK 3 L11: 3.7926 L22: 2.5123 REMARK 3 L33: 1.9918 L12: 0.0829 REMARK 3 L13: 1.4908 L23: -1.7724 REMARK 3 S TENSOR REMARK 3 S11: 0.2091 S12: -0.5113 S13: 0.0101 REMARK 3 S21: 1.3917 S22: -0.0211 S23: 0.2405 REMARK 3 S31: 1.7656 S32: -0.2574 S33: -0.0263 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 27 THROUGH 34 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.2162 44.9850 97.0904 REMARK 3 T TENSOR REMARK 3 T11: 1.0706 T22: 1.0734 REMARK 3 T33: 0.6377 T12: 0.1522 REMARK 3 T13: -0.2910 T23: -0.2978 REMARK 3 L TENSOR REMARK 3 L11: 3.7076 L22: 4.8319 REMARK 3 L33: 7.2315 L12: -1.6848 REMARK 3 L13: -3.2852 L23: 4.0378 REMARK 3 S TENSOR REMARK 3 S11: -1.0123 S12: -1.1938 S13: 0.4375 REMARK 3 S21: 1.7368 S22: 0.0483 S23: -1.0305 REMARK 3 S31: -0.2250 S32: 0.0912 S33: 0.7623 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 35 THROUGH 46 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.7344 40.6655 86.0957 REMARK 3 T TENSOR REMARK 3 T11: 0.8998 T22: 0.8034 REMARK 3 T33: 0.7340 T12: -0.3350 REMARK 3 T13: 0.3059 T23: -0.1911 REMARK 3 L TENSOR REMARK 3 L11: 7.2661 L22: 9.1817 REMARK 3 L33: 4.1187 L12: 0.3256 REMARK 3 L13: 1.0412 L23: -1.3744 REMARK 3 S TENSOR REMARK 3 S11: -0.0615 S12: -0.6604 S13: -1.8964 REMARK 3 S21: 0.6135 S22: -0.3497 S23: 0.9711 REMARK 3 S31: 1.5252 S32: -1.6600 S33: 0.4742 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 47 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.7969 50.1354 84.8323 REMARK 3 T TENSOR REMARK 3 T11: 0.3932 T22: 0.3961 REMARK 3 T33: 0.3604 T12: 0.0017 REMARK 3 T13: -0.0384 T23: -0.1464 REMARK 3 L TENSOR REMARK 3 L11: 2.7003 L22: 7.7032 REMARK 3 L33: 9.0934 L12: -3.2779 REMARK 3 L13: -2.8626 L23: -1.1919 REMARK 3 S TENSOR REMARK 3 S11: -0.0146 S12: 0.2915 S13: 0.0951 REMARK 3 S21: 0.5283 S22: 0.5383 S23: -1.1539 REMARK 3 S31: 0.2455 S32: 0.4651 S33: -0.5036 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 62 THROUGH 84 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.6848 53.2131 90.3927 REMARK 3 T TENSOR REMARK 3 T11: 0.4974 T22: 0.5082 REMARK 3 T33: 0.2892 T12: 0.0070 REMARK 3 T13: 0.0459 T23: -0.0899 REMARK 3 L TENSOR REMARK 3 L11: 7.6626 L22: 4.4845 REMARK 3 L33: 9.1945 L12: -0.3831 REMARK 3 L13: 2.8312 L23: 1.1020 REMARK 3 S TENSOR REMARK 3 S11: -0.1924 S12: 0.1540 S13: 0.0813 REMARK 3 S21: 0.2844 S22: 0.2595 S23: -0.1783 REMARK 3 S31: 0.4270 S32: 0.3602 S33: -0.1425 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 85 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.4090 47.0506 87.5846 REMARK 3 T TENSOR REMARK 3 T11: 0.6573 T22: 0.6102 REMARK 3 T33: 0.3968 T12: -0.1653 REMARK 3 T13: 0.1258 T23: -0.1221 REMARK 3 L TENSOR REMARK 3 L11: 7.4016 L22: 8.0878 REMARK 3 L33: 3.4730 L12: -2.6022 REMARK 3 L13: -4.2864 L23: 4.1057 REMARK 3 S TENSOR REMARK 3 S11: -0.3537 S12: -0.0255 S13: -0.5697 REMARK 3 S21: 1.0085 S22: -0.1583 S23: 1.0054 REMARK 3 S31: 0.9765 S32: -0.8031 S33: 0.5143 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 100 THROUGH 122 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.8938 41.7394 89.9797 REMARK 3 T TENSOR REMARK 3 T11: 0.8963 T22: 0.4772 REMARK 3 T33: 0.3890 T12: -0.0200 REMARK 3 T13: -0.0513 T23: -0.0454 REMARK 3 L TENSOR REMARK 3 L11: 2.1895 L22: 5.9421 REMARK 3 L33: 5.4729 L12: -1.6415 REMARK 3 L13: -3.1008 L23: 1.9340 REMARK 3 S TENSOR REMARK 3 S11: -0.6403 S12: -0.5064 S13: -0.9851 REMARK 3 S21: 1.2043 S22: 0.2458 S23: 0.2162 REMARK 3 S31: 1.4966 S32: -0.0525 S33: 0.4173 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8GSI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-SEP-22. REMARK 100 THE DEPOSITION ID IS D_1300032042. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-MAR-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PAL/PLS REMARK 200 BEAMLINE : 5C (4A) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46872 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 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: MOLREP REMARK 200 STARTING MODEL: 5GGS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE PH 6.5 40% V/V REMARK 280 MPD 5% W/V PEG 8000, EVAPORATION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 92.24500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 92.24500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.15000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.65000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.15000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.65000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 92.24500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.15000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.65000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 92.24500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.15000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 59.65000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 B 345 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 GLU B 1 REMARK 465 GLY B 190 REMARK 465 THR B 191 REMARK 465 GLN B 192 REMARK 465 ASP B 217 REMARK 465 LYS B 218 REMARK 465 THR B 219 REMARK 465 HIS B 220 REMARK 465 HIS B 221 REMARK 465 HIS B 222 REMARK 465 HIS B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 MET F 1 REMARK 465 GLN F 2 REMARK 465 LEU F 123 REMARK 465 GLU F 124 REMARK 465 HIS F 125 REMARK 465 HIS F 126 REMARK 465 HIS F 127 REMARK 465 HIS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH B 417 O HOH B 425 1.85 REMARK 500 N TYR B 194 O HOH B 301 1.90 REMARK 500 O HOH B 394 O HOH B 429 1.95 REMARK 500 O HOH F 229 O HOH F 231 2.07 REMARK 500 O SER B 128 O HOH B 302 2.08 REMARK 500 OG1 THR A 206 O HOH A 301 2.08 REMARK 500 OE1 GLU A 105 OH TYR A 173 2.09 REMARK 500 O HOH A 355 O HOH A 383 2.10 REMARK 500 O HOH A 352 O HOH A 360 2.12 REMARK 500 OD2 ASP B 34 O HOH B 303 2.13 REMARK 500 O HOH B 302 O HOH B 338 2.15 REMARK 500 OG SER A 91 O HOH A 302 2.17 REMARK 500 O HOH B 390 O HOH B 430 2.17 REMARK 500 O HOH A 367 O HOH A 388 2.18 REMARK 500 OG SER B 156 O HOH B 304 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH B 394 O HOH B 421 3555 2.19 REMARK 500 O HOH B 333 O HOH B 380 3455 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA A 51 -7.02 73.73 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ILE A 29 ARG A 30 -115.68 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 B 439 DISTANCE = 6.22 ANGSTROMS DBREF 8GSI A 1 214 PDB 8GSI 8GSI 1 214 DBREF 8GSI B 1 225 PDB 8GSI 8GSI 1 225 DBREF 8GSI F 1 130 PDB 8GSI 8GSI 1 130 SEQRES 1 A 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 A 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 A 214 GLN SER ILE ARG ARG TYR LEU ASN TRP TYR HIS GLN LYS SEQRES 4 A 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 A 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 A 214 GLN PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SER SEQRES 8 A 214 HIS SER ALA PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 A 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 A 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 A 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 A 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 A 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 A 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 A 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 A 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 A 214 PHE ASN ARG GLY GLU CYS SEQRES 1 B 225 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA ALA SER SEQRES 3 B 225 GLY PHE THR PHE SER SER TYR ASP MET SER TRP VAL ARG SEQRES 4 B 225 GLN ALA PRO GLY LYS GLY LEU ASP TRP VAL SER THR ILE SEQRES 5 B 225 SER GLY GLY GLY THR TYR THR TYR TYR GLN ASP SER VAL SEQRES 6 B 225 LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN SEQRES 7 B 225 THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP SEQRES 8 B 225 THR ALA VAL TYR TYR CYS ALA SER MET ASP TYR TRP GLY SEQRES 9 B 225 GLN GLY THR THR VAL THR VAL SER SER ALA SER THR LYS SEQRES 10 B 225 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 11 B 225 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 12 B 225 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 13 B 225 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 B 225 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 15 B 225 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 16 B 225 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 17 B 225 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS SEQRES 18 B 225 HIS HIS HIS HIS SEQRES 1 F 130 MET GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 F 130 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 F 130 GLY ARG THR ILE SER SER TYR ALA MET SER TRP PHE ARG SEQRES 4 F 130 GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA THR ALA SEQRES 5 F 130 ARG ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER VAL SEQRES 6 F 130 GLN GLY ARG PHE THR VAL SER ARG ASP ASN ALA LYS ASN SEQRES 7 F 130 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 F 130 THR ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR PHE SEQRES 9 F 130 TYR SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 F 130 VAL THR VAL SER SER LEU GLU HIS HIS HIS HIS HIS HIS FORMUL 4 HOH *278(H2 O) HELIX 1 AA1 GLN A 79 PHE A 83 5 5 HELIX 2 AA2 SER A 121 SER A 127 1 7 HELIX 3 AA3 LYS A 183 GLU A 187 1 5 HELIX 4 AA4 SER B 26 TYR B 33 5 8 HELIX 5 AA5 ASP B 63 LYS B 66 5 4 HELIX 6 AA6 ASN B 75 LYS B 77 5 3 HELIX 7 AA7 ARG B 88 THR B 92 5 5 HELIX 8 AA8 SER B 156 ALA B 158 5 3 HELIX 9 AA9 SER B 187 LEU B 189 5 3 HELIX 10 AB1 LYS B 201 ASN B 204 5 4 HELIX 11 AB2 ASN F 75 LYS F 77 5 3 HELIX 12 AB3 LYS F 88 THR F 92 5 5 SHEET 1 AA1 4 MET A 4 SER A 7 0 SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AA1 4 ASP A 70 ILE A 75 -1 O LEU A 73 N ILE A 21 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74 SHEET 1 AA2 6 SER A 10 ALA A 13 0 SHEET 2 AA2 6 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11 SHEET 3 AA2 6 VAL A 85 GLN A 90 -1 N TYR A 86 O THR A 102 SHEET 4 AA2 6 LEU A 33 GLN A 38 -1 N ASN A 34 O GLN A 89 SHEET 5 AA2 6 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 AA2 6 THR A 53 LEU A 54 -1 O THR A 53 N TYR A 49 SHEET 1 AA3 4 SER A 10 ALA A 13 0 SHEET 2 AA3 4 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11 SHEET 3 AA3 4 VAL A 85 GLN A 90 -1 N TYR A 86 O THR A 102 SHEET 4 AA3 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AA4 4 SER A 114 PHE A 118 0 SHEET 2 AA4 4 THR A 129 PHE A 139 -1 O LEU A 135 N PHE A 116 SHEET 3 AA4 4 TYR A 173 SER A 182 -1 O LEU A 181 N ALA A 130 SHEET 4 AA4 4 SER A 159 VAL A 163 -1 N SER A 162 O SER A 176 SHEET 1 AA5 4 ALA A 153 LEU A 154 0 SHEET 2 AA5 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 AA5 4 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147 SHEET 4 AA5 4 VAL A 205 ASN A 210 -1 O LYS A 207 N CYS A 194 SHEET 1 AA6 4 LEU B 4 SER B 7 0 SHEET 2 AA6 4 LEU B 18 ALA B 24 -1 O SER B 21 N SER B 7 SHEET 3 AA6 4 THR B 79 MET B 84 -1 O LEU B 82 N LEU B 20 SHEET 4 AA6 4 PHE B 69 ASP B 74 -1 N SER B 72 O TYR B 81 SHEET 1 AA7 6 GLY B 10 VAL B 12 0 SHEET 2 AA7 6 THR B 107 VAL B 111 1 O THR B 108 N GLY B 10 SHEET 3 AA7 6 ALA B 93 SER B 99 -1 N TYR B 95 O THR B 107 SHEET 4 AA7 6 MET B 35 GLN B 40 -1 N VAL B 38 O TYR B 96 SHEET 5 AA7 6 LEU B 46 ILE B 52 -1 O ASP B 47 N ARG B 39 SHEET 6 AA7 6 THR B 59 TYR B 61 -1 O TYR B 60 N THR B 51 SHEET 1 AA8 4 GLY B 10 VAL B 12 0 SHEET 2 AA8 4 THR B 107 VAL B 111 1 O THR B 108 N GLY B 10 SHEET 3 AA8 4 ALA B 93 SER B 99 -1 N TYR B 95 O THR B 107 SHEET 4 AA8 4 TYR B 102 TRP B 103 -1 O TYR B 102 N SER B 99 SHEET 1 AA9 4 SER B 120 LEU B 124 0 SHEET 2 AA9 4 THR B 135 TYR B 145 -1 O GLY B 139 N LEU B 124 SHEET 3 AA9 4 TYR B 176 PRO B 185 -1 O LEU B 178 N VAL B 142 SHEET 4 AA9 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AB1 4 SER B 120 LEU B 124 0 SHEET 2 AB1 4 THR B 135 TYR B 145 -1 O GLY B 139 N LEU B 124 SHEET 3 AB1 4 TYR B 176 PRO B 185 -1 O LEU B 178 N VAL B 142 SHEET 4 AB1 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AB2 3 THR B 151 TRP B 154 0 SHEET 2 AB2 3 ILE B 195 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AB2 3 THR B 205 LYS B 210 -1 O VAL B 207 N VAL B 198 SHEET 1 AB3 4 GLN F 4 SER F 8 0 SHEET 2 AB3 4 LEU F 19 SER F 26 -1 O SER F 22 N SER F 8 SHEET 3 AB3 4 THR F 79 MET F 84 -1 O VAL F 80 N CYS F 23 SHEET 4 AB3 4 PHE F 69 ASP F 74 -1 N SER F 72 O TYR F 81 SHEET 1 AB4 6 GLY F 11 VAL F 13 0 SHEET 2 AB4 6 THR F 116 VAL F 120 1 O THR F 119 N VAL F 13 SHEET 3 AB4 6 ALA F 93 ILE F 99 -1 N TYR F 95 O THR F 116 SHEET 4 AB4 6 MET F 35 GLN F 40 -1 N PHE F 38 O TYR F 96 SHEET 5 AB4 6 GLU F 47 ALA F 52 -1 O ALA F 52 N MET F 35 SHEET 6 AB4 6 ALA F 59 TYR F 61 -1 O PHE F 60 N THR F 51 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.07 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.04 SSBOND 3 CYS A 214 CYS B 216 1555 1555 2.05 SSBOND 4 CYS B 22 CYS B 97 1555 1555 2.05 SSBOND 5 CYS B 140 CYS B 196 1555 1555 2.04 SSBOND 6 CYS F 23 CYS F 97 1555 1555 2.05 CISPEP 1 SER A 7 PRO A 8 0 -20.18 CISPEP 2 ALA A 94 PRO A 95 0 -3.33 CISPEP 3 TYR A 140 PRO A 141 0 1.27 CISPEP 4 PHE B 146 PRO B 147 0 -5.98 CISPEP 5 GLU B 148 PRO B 149 0 -5.33 CRYST1 64.300 119.300 184.490 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015552 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008382 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005420 0.00000