HEADER IMMUNE SYSTEM 29-MAR-24 9B88 TITLE ANTI-OSPC FAB 8C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF MONOCLONAL 8C1 FAB; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN OF MONOCLONAL 8C1 FAB; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 OTHER_DETAILS: LIGHT CHAIN OF MONOCLONAL SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.J.RUDOLPH,N.MANTIS REVDAT 1 09-APR-25 9B88 0 JRNL AUTH M.J.RUDOLPH,N.MANTIS JRNL TITL STRUCTURE OF ANTI-OSPC FAB 8C1. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.73 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.88 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.420 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 47233 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.153 REMARK 3 R VALUE (WORKING SET) : 0.151 REMARK 3 FREE R VALUE : 0.176 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150 REMARK 3 FREE R VALUE TEST SET COUNT : 2432 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 45.8800 - 4.4500 1.00 2689 155 0.1670 0.1748 REMARK 3 2 4.4500 - 3.5300 1.00 2663 133 0.1286 0.1555 REMARK 3 3 3.5300 - 3.0800 1.00 2662 142 0.1428 0.1515 REMARK 3 4 3.0800 - 2.8000 1.00 2662 133 0.1585 0.1769 REMARK 3 5 2.8000 - 2.6000 1.00 2621 145 0.1524 0.1760 REMARK 3 6 2.6000 - 2.4500 1.00 2627 152 0.1562 0.1780 REMARK 3 7 2.4500 - 2.3300 1.00 2622 147 0.1468 0.1813 REMARK 3 8 2.3300 - 2.2200 1.00 2651 145 0.1463 0.1797 REMARK 3 9 2.2200 - 2.1400 1.00 2611 157 0.1364 0.2007 REMARK 3 10 2.1400 - 2.0600 1.00 2635 129 0.1569 0.1725 REMARK 3 11 2.0600 - 2.0000 1.00 2629 131 0.1492 0.1823 REMARK 3 12 2.0000 - 1.9400 1.00 2632 147 0.1463 0.1813 REMARK 3 13 1.9400 - 1.8900 1.00 2597 149 0.1453 0.1820 REMARK 3 14 1.8900 - 1.8500 1.00 2631 146 0.1566 0.2108 REMARK 3 15 1.8500 - 1.8000 1.00 2605 153 0.1760 0.2251 REMARK 3 16 1.8000 - 1.7700 1.00 2622 132 0.1895 0.2257 REMARK 3 17 1.7700 - 1.7300 1.00 2642 136 0.2170 0.2414 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) : 0.175 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.512 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.62 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 : 0.013 3421 REMARK 3 ANGLE : 1.126 4652 REMARK 3 CHIRALITY : 0.072 527 REMARK 3 PLANARITY : 0.009 588 REMARK 3 DIHEDRAL : 6.323 469 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 20 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.8696 67.2244 33.6809 REMARK 3 T TENSOR REMARK 3 T11: 0.1695 T22: 0.1230 REMARK 3 T33: 0.1746 T12: -0.0142 REMARK 3 T13: 0.0216 T23: 0.0269 REMARK 3 L TENSOR REMARK 3 L11: 1.5639 L22: 2.3216 REMARK 3 L33: 4.8919 L12: -0.7098 REMARK 3 L13: -0.9246 L23: 2.0516 REMARK 3 S TENSOR REMARK 3 S11: 0.0057 S12: -0.0872 S13: 0.0960 REMARK 3 S21: -0.0527 S22: 0.1123 S23: -0.1177 REMARK 3 S31: -0.1894 S32: 0.2972 S33: -0.1550 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.3333 63.7356 21.4295 REMARK 3 T TENSOR REMARK 3 T11: 0.2288 T22: 0.2164 REMARK 3 T33: 0.1785 T12: 0.0018 REMARK 3 T13: 0.0342 T23: 0.0590 REMARK 3 L TENSOR REMARK 3 L11: 3.7338 L22: 3.2790 REMARK 3 L33: 6.7536 L12: -1.6781 REMARK 3 L13: -3.1541 L23: 3.2176 REMARK 3 S TENSOR REMARK 3 S11: 0.0233 S12: 0.2944 S13: 0.2014 REMARK 3 S21: -0.3030 S22: -0.0128 S23: -0.0492 REMARK 3 S31: -0.1656 S32: 0.0569 S33: -0.1212 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.8463 56.5508 29.0743 REMARK 3 T TENSOR REMARK 3 T11: 0.1280 T22: 0.1221 REMARK 3 T33: 0.1478 T12: 0.0090 REMARK 3 T13: 0.0000 T23: 0.0091 REMARK 3 L TENSOR REMARK 3 L11: 2.8168 L22: 2.7859 REMARK 3 L33: 3.8832 L12: 0.2252 REMARK 3 L13: 0.9100 L23: 1.1125 REMARK 3 S TENSOR REMARK 3 S11: 0.1121 S12: 0.0044 S13: -0.0289 REMARK 3 S21: 0.0480 S22: 0.0211 S23: 0.1001 REMARK 3 S31: 0.2350 S32: -0.1458 S33: -0.0644 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 64 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.1929 59.8452 21.6082 REMARK 3 T TENSOR REMARK 3 T11: 0.2096 T22: 0.2037 REMARK 3 T33: 0.1669 T12: 0.0363 REMARK 3 T13: -0.0341 T23: 0.0146 REMARK 3 L TENSOR REMARK 3 L11: 4.4596 L22: 2.9509 REMARK 3 L33: 3.4649 L12: 0.9044 REMARK 3 L13: -1.3920 L23: -0.1719 REMARK 3 S TENSOR REMARK 3 S11: -0.0338 S12: 0.6544 S13: 0.0732 REMARK 3 S21: -0.3364 S22: -0.0178 S23: 0.0674 REMARK 3 S31: -0.1668 S32: -0.5984 S33: 0.0051 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 65 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.5984 67.3987 23.9847 REMARK 3 T TENSOR REMARK 3 T11: 0.1981 T22: 0.1989 REMARK 3 T33: 0.2368 T12: 0.0331 REMARK 3 T13: -0.0156 T23: 0.0559 REMARK 3 L TENSOR REMARK 3 L11: 2.7563 L22: 4.8597 REMARK 3 L33: 6.0157 L12: 1.8067 REMARK 3 L13: -3.6400 L23: -1.2689 REMARK 3 S TENSOR REMARK 3 S11: 0.0716 S12: 0.6088 S13: 0.5242 REMARK 3 S21: -0.2349 S22: 0.0638 S23: 0.1350 REMARK 3 S31: -0.2905 S32: -0.3222 S33: -0.1785 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.6629 62.5307 36.1505 REMARK 3 T TENSOR REMARK 3 T11: 0.1522 T22: 0.1381 REMARK 3 T33: 0.1692 T12: -0.0019 REMARK 3 T13: 0.0126 T23: 0.0138 REMARK 3 L TENSOR REMARK 3 L11: 0.6715 L22: 1.5843 REMARK 3 L33: 2.3391 L12: 0.1753 REMARK 3 L13: 0.5180 L23: 0.9567 REMARK 3 S TENSOR REMARK 3 S11: -0.0059 S12: 0.0157 S13: 0.0806 REMARK 3 S21: 0.0038 S22: 0.0353 S23: 0.0311 REMARK 3 S31: -0.0507 S32: -0.0615 S33: -0.0309 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 121 THROUGH 135 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.7125 60.3270 61.8890 REMARK 3 T TENSOR REMARK 3 T11: 0.2738 T22: 0.4291 REMARK 3 T33: 0.3390 T12: 0.0941 REMARK 3 T13: -0.0305 T23: 0.0651 REMARK 3 L TENSOR REMARK 3 L11: 1.6636 L22: 3.3300 REMARK 3 L33: 2.2566 L12: 0.0769 REMARK 3 L13: -1.1495 L23: 2.0966 REMARK 3 S TENSOR REMARK 3 S11: -0.3837 S12: -0.8387 S13: -0.7599 REMARK 3 S21: 1.0903 S22: 0.4100 S23: -0.0973 REMARK 3 S31: 0.1540 S32: 0.7848 S33: -0.1087 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 136 THROUGH 189 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.6773 60.5979 52.4214 REMARK 3 T TENSOR REMARK 3 T11: 0.1339 T22: 0.1543 REMARK 3 T33: 0.1897 T12: 0.0004 REMARK 3 T13: 0.0272 T23: -0.0088 REMARK 3 L TENSOR REMARK 3 L11: 2.8488 L22: 0.7243 REMARK 3 L33: 2.2516 L12: -0.4816 REMARK 3 L13: -0.0049 L23: -0.5532 REMARK 3 S TENSOR REMARK 3 S11: -0.0951 S12: -0.0931 S13: -0.2109 REMARK 3 S21: 0.0632 S22: 0.0385 S23: 0.0712 REMARK 3 S31: 0.0154 S32: 0.2498 S33: 0.0440 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 190 THROUGH 204 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.3288 66.0467 49.4335 REMARK 3 T TENSOR REMARK 3 T11: 0.1134 T22: 0.2257 REMARK 3 T33: 0.1362 T12: -0.0514 REMARK 3 T13: 0.0236 T23: -0.0025 REMARK 3 L TENSOR REMARK 3 L11: 5.9604 L22: 2.0902 REMARK 3 L33: 1.6801 L12: -2.2952 REMARK 3 L13: 0.3408 L23: -0.4432 REMARK 3 S TENSOR REMARK 3 S11: -0.1621 S12: 0.0436 S13: 0.0493 REMARK 3 S21: 0.2262 S22: 0.0430 S23: -0.1178 REMARK 3 S31: -0.1754 S32: 0.4010 S33: 0.0641 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 205 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.9395 69.7050 52.9263 REMARK 3 T TENSOR REMARK 3 T11: 0.2092 T22: 0.3246 REMARK 3 T33: 0.2417 T12: -0.0629 REMARK 3 T13: 0.0207 T23: 0.0012 REMARK 3 L TENSOR REMARK 3 L11: 2.5254 L22: 7.1141 REMARK 3 L33: 7.3132 L12: -3.8299 REMARK 3 L13: 3.4896 L23: -3.7585 REMARK 3 S TENSOR REMARK 3 S11: -0.4088 S12: -0.1276 S13: 0.4237 REMARK 3 S21: 0.3412 S22: 0.1331 S23: -0.1845 REMARK 3 S31: -0.6616 S32: 0.7062 S33: 0.2445 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.5408 37.8243 31.1780 REMARK 3 T TENSOR REMARK 3 T11: 0.1780 T22: 0.1203 REMARK 3 T33: 0.1858 T12: 0.0155 REMARK 3 T13: -0.0147 T23: -0.0160 REMARK 3 L TENSOR REMARK 3 L11: 2.6723 L22: 2.4027 REMARK 3 L33: 3.8473 L12: 0.2665 REMARK 3 L13: 0.6760 L23: 0.0173 REMARK 3 S TENSOR REMARK 3 S11: -0.0176 S12: -0.0012 S13: -0.2002 REMARK 3 S21: 0.1833 S22: 0.0818 S23: -0.0800 REMARK 3 S31: 0.2212 S32: 0.1199 S33: -0.0306 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 38 THROUGH 53 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.3436 46.8352 32.5859 REMARK 3 T TENSOR REMARK 3 T11: 0.1624 T22: 0.1922 REMARK 3 T33: 0.1933 T12: -0.0035 REMARK 3 T13: -0.0238 T23: -0.0122 REMARK 3 L TENSOR REMARK 3 L11: 2.5208 L22: 5.0641 REMARK 3 L33: 5.7942 L12: 0.4740 REMARK 3 L13: -0.5352 L23: 1.6799 REMARK 3 S TENSOR REMARK 3 S11: 0.1781 S12: -0.1300 S13: -0.0240 REMARK 3 S21: 0.3471 S22: 0.0321 S23: -0.4939 REMARK 3 S31: -0.0809 S32: 0.5218 S33: -0.2172 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 54 THROUGH 80 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.0596 36.8579 26.8867 REMARK 3 T TENSOR REMARK 3 T11: 0.1844 T22: 0.2409 REMARK 3 T33: 0.2404 T12: 0.0576 REMARK 3 T13: -0.0215 T23: -0.0796 REMARK 3 L TENSOR REMARK 3 L11: 3.0974 L22: 2.8469 REMARK 3 L33: 3.6197 L12: 0.6231 REMARK 3 L13: 0.3459 L23: -0.2307 REMARK 3 S TENSOR REMARK 3 S11: 0.0309 S12: 0.1317 S13: -0.1943 REMARK 3 S21: 0.0338 S22: 0.0980 S23: -0.4270 REMARK 3 S31: 0.0841 S32: 0.4926 S33: -0.1022 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 81 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.8393 43.3994 32.6295 REMARK 3 T TENSOR REMARK 3 T11: 0.1497 T22: 0.1536 REMARK 3 T33: 0.1548 T12: -0.0068 REMARK 3 T13: -0.0089 T23: -0.0238 REMARK 3 L TENSOR REMARK 3 L11: 2.1411 L22: 2.7651 REMARK 3 L33: 3.3309 L12: 0.3315 REMARK 3 L13: 0.0297 L23: 0.1981 REMARK 3 S TENSOR REMARK 3 S11: 0.0061 S12: 0.0207 S13: -0.1574 REMARK 3 S21: 0.1067 S22: 0.0752 S23: -0.2067 REMARK 3 S31: -0.0025 S32: 0.4106 S33: -0.0337 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 107 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.5248 43.0645 54.7468 REMARK 3 T TENSOR REMARK 3 T11: 0.2160 T22: 0.2690 REMARK 3 T33: 0.2665 T12: 0.0207 REMARK 3 T13: -0.0275 T23: 0.0049 REMARK 3 L TENSOR REMARK 3 L11: 1.4558 L22: 1.0879 REMARK 3 L33: 3.6343 L12: 0.3573 REMARK 3 L13: 2.1882 L23: 0.7525 REMARK 3 S TENSOR REMARK 3 S11: 0.4356 S12: 0.0350 S13: -0.2972 REMARK 3 S21: 0.0281 S22: -0.0327 S23: -0.2118 REMARK 3 S31: 0.5610 S32: 0.1700 S33: -0.4184 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 124 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 48.7431 70.6068 65.5515 REMARK 3 T TENSOR REMARK 3 T11: 0.5184 T22: 0.2755 REMARK 3 T33: 0.2849 T12: -0.0526 REMARK 3 T13: -0.0665 T23: -0.0436 REMARK 3 L TENSOR REMARK 3 L11: 4.5040 L22: 2.5121 REMARK 3 L33: 6.7012 L12: -1.0930 REMARK 3 L13: 1.6614 L23: 0.0465 REMARK 3 S TENSOR REMARK 3 S11: -0.1913 S12: 0.0184 S13: 0.7819 REMARK 3 S21: -0.1967 S22: -0.1117 S23: -0.5124 REMARK 3 S31: -1.6640 S32: 0.2155 S33: 0.2433 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 135 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.7368 49.5750 63.7641 REMARK 3 T TENSOR REMARK 3 T11: 0.1907 T22: 0.3124 REMARK 3 T33: 0.2579 T12: -0.0325 REMARK 3 T13: -0.0239 T23: 0.0878 REMARK 3 L TENSOR REMARK 3 L11: 1.3914 L22: 4.5404 REMARK 3 L33: 4.0531 L12: -0.0167 REMARK 3 L13: 0.8761 L23: 3.1269 REMARK 3 S TENSOR REMARK 3 S11: 0.2063 S12: -0.2932 S13: -0.2081 REMARK 3 S21: 0.1882 S22: 0.0050 S23: -0.0673 REMARK 3 S31: 0.4209 S32: -0.1361 S33: -0.1416 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 156 THROUGH 168 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.6309 55.0968 70.2107 REMARK 3 T TENSOR REMARK 3 T11: 0.2135 T22: 0.4748 REMARK 3 T33: 0.2655 T12: -0.0584 REMARK 3 T13: -0.0003 T23: 0.0510 REMARK 3 L TENSOR REMARK 3 L11: 1.6119 L22: 2.0160 REMARK 3 L33: 4.6856 L12: 1.0714 REMARK 3 L13: 1.4218 L23: 1.6048 REMARK 3 S TENSOR REMARK 3 S11: 0.2722 S12: -0.6772 S13: -0.1530 REMARK 3 S21: 0.3173 S22: -0.0709 S23: -0.0271 REMARK 3 S31: -0.0275 S32: -0.2998 S33: -0.0784 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 169 THROUGH 186 ) REMARK 3 ORIGIN FOR THE GROUP (A): 45.2807 49.8657 55.1078 REMARK 3 T TENSOR REMARK 3 T11: 0.1744 T22: 0.2666 REMARK 3 T33: 0.2100 T12: -0.0309 REMARK 3 T13: 0.0147 T23: 0.0251 REMARK 3 L TENSOR REMARK 3 L11: 2.1476 L22: 5.5636 REMARK 3 L33: 6.2545 L12: -0.5755 REMARK 3 L13: 0.5686 L23: 4.5342 REMARK 3 S TENSOR REMARK 3 S11: 0.1322 S12: 0.0205 S13: -0.0446 REMARK 3 S21: -0.2434 S22: 0.3034 S23: -0.2507 REMARK 3 S31: -0.0543 S32: 0.5170 S33: -0.2792 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 187 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): 48.8151 55.6789 72.7169 REMARK 3 T TENSOR REMARK 3 T11: 0.2214 T22: 0.4361 REMARK 3 T33: 0.2423 T12: -0.0884 REMARK 3 T13: -0.0088 T23: 0.0616 REMARK 3 L TENSOR REMARK 3 L11: 2.3967 L22: 4.2942 REMARK 3 L33: 4.0832 L12: 0.7499 REMARK 3 L13: 1.1276 L23: 1.5012 REMARK 3 S TENSOR REMARK 3 S11: 0.3198 S12: -0.5141 S13: -0.0588 REMARK 3 S21: 0.6966 S22: -0.2037 S23: -0.5023 REMARK 3 S31: 0.0785 S32: -0.0066 S33: -0.1268 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 9B88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-24. REMARK 100 THE DEPOSITION ID IS D_1000282858. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-OCT-23 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 : NSLS-II 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) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54544 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730 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 (%) : 99.0 REMARK 200 DATA REDUNDANCY : 19.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 44.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRI-SODIUM CITRATE PH 3.5 AND REMARK 280 2.4 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.18333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.59167 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 35.38750 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 11.79583 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 58.97917 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 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 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 THR A 132 REMARK 465 SER A 216 REMARK 465 CYS A 217 REMARK 465 ASP A 218 REMARK 465 LYS A 219 REMARK 465 THR A 220 REMARK 465 HIS A 221 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 SG CYS B 139 HG CYS B 199 1.09 REMARK 500 HH12 ARG B 147 O HOH B 406 1.55 REMARK 500 O HOH B 553 O HOH B 566 1.79 REMARK 500 OE2 GLU B 170 O HOH B 401 1.90 REMARK 500 O HOH A 525 O HOH B 515 1.93 REMARK 500 O HOH A 596 O HOH A 630 1.95 REMARK 500 O HOH A 601 O HOH A 603 1.97 REMARK 500 O HOH B 520 O HOH B 581 1.98 REMARK 500 O HOH A 550 O HOH A 555 1.98 REMARK 500 O HOH B 552 O HOH B 598 2.00 REMARK 500 O HOH A 592 O HOH A 598 2.02 REMARK 500 O HOH A 650 O HOH A 673 2.02 REMARK 500 OG1 THR B 134 O HOH B 402 2.03 REMARK 500 OE1 GLU B 128 O HOH B 403 2.03 REMARK 500 O PRO A 127 O HOH A 401 2.03 REMARK 500 O HOH A 656 O HOH B 596 2.05 REMARK 500 O HOH A 676 O HOH B 625 2.06 REMARK 500 O HOH A 644 O HOH A 654 2.08 REMARK 500 O HOH A 426 O HOH A 630 2.08 REMARK 500 O HOH A 604 O HOH A 643 2.08 REMARK 500 O HOH A 429 O HOH A 617 2.09 REMARK 500 O HOH A 636 O HOH B 582 2.11 REMARK 500 O HOH B 458 O HOH B 575 2.12 REMARK 500 O4 SO4 A 304 O HOH A 402 2.13 REMARK 500 O HOH B 618 O HOH B 622 2.17 REMARK 500 O3 SO4 A 305 O HOH A 403 2.19 REMARK 500 O1 SO4 A 305 O HOH A 404 2.19 REMARK 500 O HOH A 411 O HOH A 627 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 HZ3 LYS B 193 O1 SO4 A 304 1556 1.49 REMARK 500 O HOH B 570 O HOH B 605 4664 1.97 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 A 99 -134.95 54.42 REMARK 500 SER A 128 -159.64 -161.64 REMARK 500 ASP A 145 63.01 62.02 REMARK 500 VAL B 56 -50.16 72.11 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 A 674 DISTANCE = 5.86 ANGSTROMS REMARK 525 HOH A 675 DISTANCE = 6.08 ANGSTROMS REMARK 525 HOH A 676 DISTANCE = 6.24 ANGSTROMS REMARK 525 HOH B 624 DISTANCE = 5.89 ANGSTROMS REMARK 525 HOH B 625 DISTANCE = 6.09 ANGSTROMS DBREF 9B88 A 1 221 PDB 9B88 9B88 1 221 DBREF 9B88 B 1 219 PDB 9B88 9B88 1 219 SEQRES 1 A 221 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 A 221 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 A 221 TYR THR PHE SER ASN SER TRP MET ASN TRP VAL LYS GLN SEQRES 4 A 221 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ARG ILE TYR SEQRES 5 A 221 PRO GLY ASP GLY ASP THR ASN TYR ASN GLY LYS PHE LYS SEQRES 6 A 221 ASP LYS ALA THR LEU THR THR ASP LYS SER SER SER THR SEQRES 7 A 221 ALA TYR MET ARG LEU SER SER LEU THR SER VAL ASP SER SEQRES 8 A 221 ALA VAL TYR PHE CYS ALA ARG SER LEU PHE ASP TYR TRP SEQRES 9 A 221 GLY GLN GLY THR THR LEU THR VAL SER SER ALA SER THR SEQRES 10 A 221 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 A 221 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 A 221 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 A 221 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 A 221 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 A 221 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 A 221 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 A 221 ASP LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 B 219 ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SER VAL SEQRES 2 B 219 THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 B 219 GLN SER LEU LEU ASP SER ASP GLY LYS THR TYR LEU ILE SEQRES 4 B 219 TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5 B 219 ILE TYR LEU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 B 219 ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 B 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 B 219 TYR CYS CYS GLN GLY THR HIS PHE PRO PHE THR PHE GLY SEQRES 9 B 219 VAL GLY THR LYS LEU GLU LEU LYS ARG THR VAL ALA ALA SEQRES 10 B 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 B 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 B 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 B 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 B 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 B 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 B 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 B 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET EDO A 301 4 HET EDO A 302 4 HET SO4 A 303 5 HET SO4 A 304 5 HET SO4 A 305 5 HET SO4 A 306 5 HET CL A 307 1 HET SO4 B 301 5 HET CL B 302 1 HETNAM EDO 1,2-ETHANEDIOL HETNAM SO4 SULFATE ION HETNAM CL CHLORIDE ION HETSYN EDO ETHYLENE GLYCOL FORMUL 3 EDO 2(C2 H6 O2) FORMUL 5 SO4 5(O4 S 2-) FORMUL 9 CL 2(CL 1-) FORMUL 12 HOH *501(H2 O) HELIX 1 AA1 THR A 28 SER A 32 5 5 HELIX 2 AA2 GLY A 62 LYS A 65 5 4 HELIX 3 AA3 THR A 87 SER A 91 5 5 HELIX 4 AA4 SER A 157 ALA A 159 5 3 HELIX 5 AA5 SER A 188 LEU A 190 5 3 HELIX 6 AA6 LYS A 202 ASN A 205 5 4 HELIX 7 AA7 GLU B 84 LEU B 88 5 5 HELIX 8 AA8 SER B 126 SER B 132 1 7 HELIX 9 AA9 SER B 187 HIS B 194 1 8 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O LEU A 83 N VAL A 18 SHEET 4 AA1 4 ALA A 68 ASP A 73 -1 N THR A 71 O TYR A 80 SHEET 1 AA2 6 GLU A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 108 VAL A 112 1 O THR A 111 N GLU A 10 SHEET 3 AA2 6 ALA A 92 ARG A 98 -1 N ALA A 92 O LEU A 110 SHEET 4 AA2 6 MET A 34 ARG A 40 -1 N ASN A 35 O ALA A 97 SHEET 5 AA2 6 GLY A 44 ILE A 51 -1 O GLU A 46 N LYS A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O ASN A 59 N ARG A 50 SHEET 1 AA3 4 SER A 121 LEU A 125 0 SHEET 2 AA3 4 THR A 136 TYR A 146 -1 O LEU A 142 N PHE A 123 SHEET 3 AA3 4 TYR A 177 PRO A 186 -1 O TYR A 177 N TYR A 146 SHEET 4 AA3 4 VAL A 164 THR A 166 -1 N HIS A 165 O VAL A 182 SHEET 1 AA4 4 SER A 121 LEU A 125 0 SHEET 2 AA4 4 THR A 136 TYR A 146 -1 O LEU A 142 N PHE A 123 SHEET 3 AA4 4 TYR A 177 PRO A 186 -1 O TYR A 177 N TYR A 146 SHEET 4 AA4 4 VAL A 170 LEU A 171 -1 N VAL A 170 O SER A 178 SHEET 1 AA5 3 THR A 152 TRP A 155 0 SHEET 2 AA5 3 ILE A 196 HIS A 201 -1 O ASN A 198 N SER A 154 SHEET 3 AA5 3 THR A 206 ARG A 211 -1 O VAL A 208 N VAL A 199 SHEET 1 AA6 4 MET B 4 THR B 7 0 SHEET 2 AA6 4 ALA B 19 SER B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA6 4 ASP B 75 ILE B 80 -1 O LEU B 78 N ILE B 21 SHEET 4 AA6 4 PHE B 67 SER B 72 -1 N THR B 68 O LYS B 79 SHEET 1 AA7 6 THR B 10 THR B 14 0 SHEET 2 AA7 6 THR B 107 LYS B 112 1 O GLU B 110 N LEU B 11 SHEET 3 AA7 6 GLY B 89 GLN B 95 -1 N GLY B 89 O LEU B 109 SHEET 4 AA7 6 LEU B 38 GLN B 43 -1 N LEU B 41 O TYR B 92 SHEET 5 AA7 6 LYS B 50 TYR B 54 -1 O LEU B 52 N TRP B 40 SHEET 6 AA7 6 LYS B 58 LEU B 59 -1 O LYS B 58 N TYR B 54 SHEET 1 AA8 4 THR B 10 THR B 14 0 SHEET 2 AA8 4 THR B 107 LYS B 112 1 O GLU B 110 N LEU B 11 SHEET 3 AA8 4 GLY B 89 GLN B 95 -1 N GLY B 89 O LEU B 109 SHEET 4 AA8 4 THR B 102 PHE B 103 -1 O THR B 102 N GLN B 95 SHEET 1 AA9 4 SER B 119 PHE B 123 0 SHEET 2 AA9 4 ALA B 135 PHE B 144 -1 O LEU B 140 N PHE B 121 SHEET 3 AA9 4 TYR B 178 LEU B 186 -1 O LEU B 184 N VAL B 137 SHEET 4 AA9 4 SER B 164 VAL B 168 -1 N GLN B 165 O THR B 183 SHEET 1 AB1 4 ALA B 158 LEU B 159 0 SHEET 2 AB1 4 LYS B 150 VAL B 155 -1 N VAL B 155 O ALA B 158 SHEET 3 AB1 4 VAL B 196 THR B 202 -1 O GLU B 200 N GLN B 152 SHEET 4 AB1 4 VAL B 210 ASN B 215 -1 O VAL B 210 N VAL B 201 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.15 SSBOND 2 CYS A 141 CYS A 197 1555 1555 2.08 SSBOND 3 CYS B 23 CYS B 93 1555 1555 2.15 SSBOND 4 CYS B 139 CYS B 199 1555 1555 2.10 CISPEP 1 PHE A 147 PRO A 148 0 -8.71 CISPEP 2 GLU A 149 PRO A 150 0 -1.33 CISPEP 3 THR B 7 PRO B 8 0 -10.15 CISPEP 4 PHE B 99 PRO B 100 0 -5.96 CISPEP 5 TYR B 145 PRO B 146 0 3.20 CRYST1 105.962 105.962 70.775 90.00 90.00 120.00 P 65 6 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 0.009437 0.005449 0.000000 0.00000 SCALE2 0.000000 0.010897 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014129 0.00000