HEADER IMMUNE SYSTEM 22-MAY-24 9BX5 TITLE HUMAN FAB 8C1 IN COMPLEX WITH OSPCA PEPTIDE P4 (RESIDUES 141-144) COMPND MOL_ID: 1; COMPND 2 MOLECULE: 8C1 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 8C1 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: P4 PEPTIDE FROM OUTER SURFACE PROTEIN C; COMPND 11 CHAIN: P; COMPND 12 FRAGMENT: RESIDUES 141-144; COMPND 13 SYNONYM: PC,P23; COMPND 14 ENGINEERED: YES 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; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: BORRELIELLA BURGDORFERI; SOURCE 13 ORGANISM_TAXID: 224326; SOURCE 14 STRAIN: B31; SOURCE 15 GENE: OSPC, BB_B19; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI B; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 37762 KEYWDS HUMAN FAB, PEPTIDE OF OUTER SURFACE PROTEIN C TYPE A (OSPCA), IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.J.RUDOLPH,N.MANTIS REVDAT 1 27-AUG-25 9BX5 0 JRNL AUTH M.J.RUDOLPH,N.MANTIS JRNL TITL HUMAN FAB 8C1 IN COMPLEX WITH OSPCA PEPTIDE P4 (RESIDUES JRNL TITL 2 141-144) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.57 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) : 1.57 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 62886 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.143 REMARK 3 R VALUE (WORKING SET) : 0.142 REMARK 3 FREE R VALUE : 0.170 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 3082 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 38.9000 - 4.4000 0.99 2925 149 0.1506 0.1576 REMARK 3 2 4.4000 - 3.4900 1.00 2786 162 0.1314 0.1608 REMARK 3 3 3.4900 - 3.0500 1.00 2768 148 0.1404 0.1789 REMARK 3 4 3.0500 - 2.7700 1.00 2756 138 0.1501 0.1717 REMARK 3 5 2.7700 - 2.5700 1.00 2760 123 0.1492 0.1727 REMARK 3 6 2.5700 - 2.4200 1.00 2726 149 0.1400 0.1503 REMARK 3 7 2.4200 - 2.3000 1.00 2725 144 0.1330 0.1696 REMARK 3 8 2.3000 - 2.2000 1.00 2724 151 0.1320 0.1748 REMARK 3 9 2.2000 - 2.1200 1.00 2703 144 0.1286 0.1482 REMARK 3 10 2.1200 - 2.0400 1.00 2741 129 0.1358 0.1720 REMARK 3 11 2.0400 - 1.9800 1.00 2694 152 0.1402 0.1682 REMARK 3 12 1.9800 - 1.9200 1.00 2724 130 0.1421 0.1670 REMARK 3 13 1.9200 - 1.8700 1.00 2691 156 0.1412 0.1806 REMARK 3 14 1.8700 - 1.8300 1.00 2687 133 0.1396 0.1776 REMARK 3 15 1.8300 - 1.7800 1.00 2701 148 0.1422 0.1608 REMARK 3 16 1.7800 - 1.7500 1.00 2732 136 0.1419 0.1602 REMARK 3 17 1.7500 - 1.7100 1.00 2705 131 0.1469 0.2364 REMARK 3 18 1.7100 - 1.6800 1.00 2683 139 0.1482 0.1925 REMARK 3 19 1.6800 - 1.6500 1.00 2696 113 0.1514 0.1993 REMARK 3 20 1.6500 - 1.6200 1.00 2674 155 0.1559 0.1970 REMARK 3 21 1.6200 - 1.5900 0.99 2698 117 0.1534 0.1934 REMARK 3 22 1.5900 - 1.5700 0.94 2505 135 0.1610 0.1942 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) : 0.112 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.132 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 13.52 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.26 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 : 0.008 3411 REMARK 3 ANGLE : 1.074 4646 REMARK 3 CHIRALITY : 0.063 530 REMARK 3 PLANARITY : 0.009 594 REMARK 3 DIHEDRAL : 6.764 473 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 20 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 134 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.1394 63.5429 35.3370 REMARK 3 T TENSOR REMARK 3 T11: 0.1278 T22: 0.0808 REMARK 3 T33: 0.0902 T12: 0.0136 REMARK 3 T13: -0.0390 T23: -0.0197 REMARK 3 L TENSOR REMARK 3 L11: 1.1503 L22: 6.6216 REMARK 3 L33: 3.7992 L12: -0.6812 REMARK 3 L13: 0.7334 L23: -4.5863 REMARK 3 S TENSOR REMARK 3 S11: -0.0143 S12: -0.0892 S13: 0.1808 REMARK 3 S21: -0.0155 S22: 0.0346 S23: 0.2642 REMARK 3 S31: -0.0332 S32: -0.0900 S33: -0.0046 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 156 THROUGH 168 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.6092 69.0387 29.1312 REMARK 3 T TENSOR REMARK 3 T11: 0.1556 T22: 0.1341 REMARK 3 T33: 0.1829 T12: 0.0542 REMARK 3 T13: -0.0327 T23: 0.0216 REMARK 3 L TENSOR REMARK 3 L11: 2.4865 L22: 6.5443 REMARK 3 L33: 1.1142 L12: -2.1797 REMARK 3 L13: 0.3492 L23: -1.6149 REMARK 3 S TENSOR REMARK 3 S11: 0.1079 S12: 0.0899 S13: 0.0924 REMARK 3 S21: -0.0365 S22: -0.0881 S23: 0.2099 REMARK 3 S31: -0.1263 S32: -0.2756 S33: -0.0427 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 169 THROUGH 193 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.3849 63.6023 30.5637 REMARK 3 T TENSOR REMARK 3 T11: 0.1119 T22: 0.1183 REMARK 3 T33: 0.1562 T12: 0.0202 REMARK 3 T13: -0.0387 T23: 0.0371 REMARK 3 L TENSOR REMARK 3 L11: 1.6070 L22: 6.8502 REMARK 3 L33: 3.2151 L12: 0.1578 REMARK 3 L13: -0.2970 L23: -3.2854 REMARK 3 S TENSOR REMARK 3 S11: 0.0476 S12: 0.0884 S13: 0.2304 REMARK 3 S21: -0.2626 S22: -0.2298 S23: -0.2237 REMARK 3 S31: 0.0569 S32: 0.0140 S33: 0.2072 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 194 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.2510 71.9881 38.8464 REMARK 3 T TENSOR REMARK 3 T11: 0.2120 T22: 0.1182 REMARK 3 T33: 0.1877 T12: 0.0367 REMARK 3 T13: -0.0313 T23: -0.0338 REMARK 3 L TENSOR REMARK 3 L11: 2.3582 L22: 5.1500 REMARK 3 L33: 2.9473 L12: -0.5067 REMARK 3 L13: 0.1461 L23: -1.4251 REMARK 3 S TENSOR REMARK 3 S11: -0.0448 S12: -0.2301 S13: 0.4193 REMARK 3 S21: 0.6853 S22: 0.1392 S23: 0.2562 REMARK 3 S31: -0.5637 S32: -0.2111 S33: -0.0981 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 141 THROUGH 144 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.4335 22.2793 17.0580 REMARK 3 T TENSOR REMARK 3 T11: 0.1662 T22: 0.1266 REMARK 3 T33: 0.1825 T12: -0.0303 REMARK 3 T13: 0.0380 T23: 0.0151 REMARK 3 L TENSOR REMARK 3 L11: 5.0579 L22: 9.7729 REMARK 3 L33: 6.9176 L12: -6.2380 REMARK 3 L13: -4.2549 L23: 2.6364 REMARK 3 S TENSOR REMARK 3 S11: -0.3005 S12: -0.2664 S13: -0.7328 REMARK 3 S21: 0.0987 S22: 0.2169 S23: 0.5007 REMARK 3 S31: 0.2866 S32: 0.0414 S33: 0.0920 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.4759 39.8605 8.9596 REMARK 3 T TENSOR REMARK 3 T11: 0.1028 T22: 0.1923 REMARK 3 T33: 0.0714 T12: -0.0467 REMARK 3 T13: -0.0125 T23: 0.0442 REMARK 3 L TENSOR REMARK 3 L11: 2.1368 L22: 6.2352 REMARK 3 L33: 1.2419 L12: 0.0817 REMARK 3 L13: 0.1912 L23: -1.2693 REMARK 3 S TENSOR REMARK 3 S11: -0.2448 S12: 0.3076 S13: 0.1800 REMARK 3 S21: -0.3832 S22: 0.1860 S23: -0.4217 REMARK 3 S31: -0.0245 S32: 0.0878 S33: 0.2622 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.1403 27.3483 8.2979 REMARK 3 T TENSOR REMARK 3 T11: 0.1020 T22: 0.2083 REMARK 3 T33: 0.0767 T12: -0.0305 REMARK 3 T13: 0.0239 T23: -0.0414 REMARK 3 L TENSOR REMARK 3 L11: 2.2577 L22: 5.0425 REMARK 3 L33: 2.4066 L12: 1.5075 REMARK 3 L13: -0.2142 L23: -2.1909 REMARK 3 S TENSOR REMARK 3 S11: -0.2193 S12: 0.5730 S13: -0.2839 REMARK 3 S21: -0.1443 S22: 0.2154 S23: -0.2733 REMARK 3 S31: 0.0462 S32: 0.1455 S33: 0.0802 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 33 THROUGH 57 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.7815 34.9567 13.3099 REMARK 3 T TENSOR REMARK 3 T11: 0.0503 T22: 0.1094 REMARK 3 T33: 0.0536 T12: -0.0043 REMARK 3 T13: -0.0122 T23: 0.0518 REMARK 3 L TENSOR REMARK 3 L11: 2.7418 L22: 3.8509 REMARK 3 L33: 1.8503 L12: 0.5408 REMARK 3 L13: -0.0148 L23: 0.2811 REMARK 3 S TENSOR REMARK 3 S11: -0.1206 S12: 0.2673 S13: 0.1410 REMARK 3 S21: -0.0571 S22: 0.0804 S23: 0.2121 REMARK 3 S31: -0.1079 S32: -0.0396 S33: 0.0512 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 58 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.0547 35.3617 5.8070 REMARK 3 T TENSOR REMARK 3 T11: -0.0019 T22: 0.2989 REMARK 3 T33: 0.1234 T12: -0.0158 REMARK 3 T13: -0.1688 T23: 0.1587 REMARK 3 L TENSOR REMARK 3 L11: 2.6332 L22: 2.0173 REMARK 3 L33: 0.6853 L12: 0.2698 REMARK 3 L13: -0.1376 L23: 0.2213 REMARK 3 S TENSOR REMARK 3 S11: -0.3462 S12: 0.9916 S13: -0.0232 REMARK 3 S21: -0.9626 S22: 0.2920 S23: 0.3301 REMARK 3 S31: -0.1280 S32: -0.1300 S33: -0.0250 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 77 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.6730 42.6301 5.7854 REMARK 3 T TENSOR REMARK 3 T11: 0.1498 T22: 0.2689 REMARK 3 T33: 0.1336 T12: -0.0888 REMARK 3 T13: -0.0551 T23: 0.1302 REMARK 3 L TENSOR REMARK 3 L11: 0.9786 L22: 5.8485 REMARK 3 L33: 1.3010 L12: -0.2097 REMARK 3 L13: 0.6690 L23: -0.4637 REMARK 3 S TENSOR REMARK 3 S11: -0.3365 S12: 0.5880 S13: 0.2865 REMARK 3 S21: -0.4949 S22: 0.3958 S23: 0.1968 REMARK 3 S31: -0.2107 S32: 0.1221 S33: -0.0421 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 92 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.9724 41.4901 14.1948 REMARK 3 T TENSOR REMARK 3 T11: 0.0877 T22: 0.1070 REMARK 3 T33: 0.0852 T12: -0.0275 REMARK 3 T13: -0.0298 T23: 0.0728 REMARK 3 L TENSOR REMARK 3 L11: 0.7716 L22: 0.6015 REMARK 3 L33: 0.5670 L12: 0.7790 REMARK 3 L13: 0.1260 L23: 0.4984 REMARK 3 S TENSOR REMARK 3 S11: -0.1408 S12: 0.2868 S13: 0.1447 REMARK 3 S21: -0.1076 S22: 0.1235 S23: 0.1422 REMARK 3 S31: -0.1383 S32: 0.0400 S33: -0.0483 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 121 THROUGH 146 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.7068 66.7754 27.8627 REMARK 3 T TENSOR REMARK 3 T11: 0.1230 T22: 0.0657 REMARK 3 T33: 0.1474 T12: -0.0001 REMARK 3 T13: -0.0295 T23: 0.0044 REMARK 3 L TENSOR REMARK 3 L11: 2.8141 L22: 2.9328 REMARK 3 L33: 4.0948 L12: 0.3793 REMARK 3 L13: 0.9486 L23: 0.2039 REMARK 3 S TENSOR REMARK 3 S11: -0.1396 S12: -0.1549 S13: 0.3350 REMARK 3 S21: -0.0013 S22: 0.0128 S23: 0.0442 REMARK 3 S31: -0.6004 S32: -0.0264 S33: 0.0918 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 147 THROUGH 189 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.8546 58.9106 26.1060 REMARK 3 T TENSOR REMARK 3 T11: 0.1080 T22: 0.0505 REMARK 3 T33: 0.1113 T12: -0.0044 REMARK 3 T13: -0.0254 T23: 0.0389 REMARK 3 L TENSOR REMARK 3 L11: 2.0301 L22: 1.6026 REMARK 3 L33: 2.5076 L12: 0.1532 REMARK 3 L13: -0.1151 L23: 0.3886 REMARK 3 S TENSOR REMARK 3 S11: -0.0788 S12: -0.0155 S13: 0.0679 REMARK 3 S21: -0.0142 S22: 0.0432 S23: 0.0309 REMARK 3 S31: -0.0826 S32: -0.0379 S33: 0.0471 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 190 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.6752 63.0832 23.5493 REMARK 3 T TENSOR REMARK 3 T11: 0.1228 T22: 0.1068 REMARK 3 T33: 0.1395 T12: -0.0440 REMARK 3 T13: 0.0012 T23: 0.0359 REMARK 3 L TENSOR REMARK 3 L11: 4.0012 L22: 3.3959 REMARK 3 L33: 6.0871 L12: 1.7102 REMARK 3 L13: 1.8892 L23: 1.9106 REMARK 3 S TENSOR REMARK 3 S11: -0.0592 S12: -0.0140 S13: 0.0625 REMARK 3 S21: -0.0769 S22: 0.1565 S23: -0.2448 REMARK 3 S31: -0.4490 S32: 0.4400 S33: -0.1204 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.6654 34.0662 32.5679 REMARK 3 T TENSOR REMARK 3 T11: 0.0647 T22: 0.0881 REMARK 3 T33: 0.0536 T12: -0.0032 REMARK 3 T13: 0.0172 T23: 0.0134 REMARK 3 L TENSOR REMARK 3 L11: 2.0308 L22: 1.1067 REMARK 3 L33: 1.1499 L12: 0.6002 REMARK 3 L13: 0.6451 L23: 0.2234 REMARK 3 S TENSOR REMARK 3 S11: 0.0336 S12: -0.2264 S13: 0.0790 REMARK 3 S21: 0.0731 S22: -0.1157 S23: 0.0443 REMARK 3 S31: -0.0062 S32: -0.0748 S33: 0.0704 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 38 THROUGH 53 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.9606 33.3225 27.5175 REMARK 3 T TENSOR REMARK 3 T11: 0.0606 T22: 0.0760 REMARK 3 T33: 0.0577 T12: 0.0065 REMARK 3 T13: -0.0081 T23: 0.0158 REMARK 3 L TENSOR REMARK 3 L11: 3.5115 L22: 2.9787 REMARK 3 L33: 1.8949 L12: 1.8269 REMARK 3 L13: -0.6977 L23: -0.5380 REMARK 3 S TENSOR REMARK 3 S11: 0.0563 S12: -0.1473 S13: -0.1098 REMARK 3 S21: 0.0427 S22: -0.0974 S23: -0.2200 REMARK 3 S31: 0.0175 S32: 0.1565 S33: 0.0474 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 54 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.0890 23.5732 32.3443 REMARK 3 T TENSOR REMARK 3 T11: 0.1202 T22: 0.0935 REMARK 3 T33: 0.1362 T12: 0.0089 REMARK 3 T13: -0.0204 T23: 0.0431 REMARK 3 L TENSOR REMARK 3 L11: 5.8948 L22: 2.9421 REMARK 3 L33: 4.4265 L12: 0.8991 REMARK 3 L13: 1.3795 L23: 1.3171 REMARK 3 S TENSOR REMARK 3 S11: 0.2238 S12: -0.0165 S13: -0.2762 REMARK 3 S21: 0.1437 S22: -0.0483 S23: -0.3756 REMARK 3 S31: 0.3383 S32: 0.2923 S33: -0.2198 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 67 THROUGH 95 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.5647 32.4571 35.5864 REMARK 3 T TENSOR REMARK 3 T11: 0.0737 T22: 0.0989 REMARK 3 T33: 0.0734 T12: 0.0032 REMARK 3 T13: 0.0050 T23: 0.0116 REMARK 3 L TENSOR REMARK 3 L11: 2.5403 L22: 1.2315 REMARK 3 L33: 2.1626 L12: 1.0739 REMARK 3 L13: 0.9602 L23: -0.0696 REMARK 3 S TENSOR REMARK 3 S11: 0.1262 S12: -0.2716 S13: -0.1641 REMARK 3 S21: 0.1632 S22: -0.1271 S23: -0.0641 REMARK 3 S31: 0.0882 S32: 0.0768 S33: -0.0110 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 96 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.4003 41.8872 32.4826 REMARK 3 T TENSOR REMARK 3 T11: 0.0793 T22: 0.1043 REMARK 3 T33: 0.0926 T12: -0.0028 REMARK 3 T13: 0.0070 T23: -0.0031 REMARK 3 L TENSOR REMARK 3 L11: 1.4806 L22: 2.1379 REMARK 3 L33: 1.0015 L12: 1.7677 REMARK 3 L13: 1.0980 L23: 1.1312 REMARK 3 S TENSOR REMARK 3 S11: 0.1049 S12: -0.1724 S13: 0.0628 REMARK 3 S21: 0.1512 S22: -0.1482 S23: 0.0207 REMARK 3 S31: 0.0269 S32: -0.1065 S33: 0.0400 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 119 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.3324 73.1420 27.5071 REMARK 3 T TENSOR REMARK 3 T11: 0.1571 T22: 0.0817 REMARK 3 T33: 0.2174 T12: -0.0079 REMARK 3 T13: -0.0147 T23: 0.0265 REMARK 3 L TENSOR REMARK 3 L11: 3.0294 L22: 4.5047 REMARK 3 L33: 7.9016 L12: 0.5150 REMARK 3 L13: -0.8356 L23: -2.0763 REMARK 3 S TENSOR REMARK 3 S11: 0.1097 S12: 0.1008 S13: 0.5075 REMARK 3 S21: -0.1027 S22: -0.0699 S23: -0.2455 REMARK 3 S31: -0.5613 S32: 0.4791 S33: 0.0436 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 9BX5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000284314. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-APR-24 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 EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63082 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570 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 (%) : 99.8 REMARK 200 DATA REDUNDANCY : 12.30 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 51.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60 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 (%): 48.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM SODIUM NITRATE AND 20% PEG REMARK 280 3,350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21 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,-Z+1/2 REMARK 290 4555 -X+1/2,-Y,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.82850 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.55100 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.82850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 47.55100 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4560 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P 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 H 691 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 LYS H 130 REMARK 465 SER H 131 REMARK 465 THR H 132 REMARK 465 SER H 133 REMARK 465 LYS H 215 REMARK 465 SER H 216 REMARK 465 CYS H 217 REMARK 465 ASP H 218 REMARK 465 LYS H 219 REMARK 465 THR H 220 REMARK 465 HIS H 221 REMARK 465 GLY L 217 REMARK 465 GLU L 218 REMARK 465 CYS L 219 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 HH21 ARG H 82 O HOH H 405 1.60 REMARK 500 OD2 ASP L 75 O HOH L 401 1.71 REMARK 500 OE1 GLU H 1 O HOH H 401 1.85 REMARK 500 O HOH L 624 O HOH L 677 1.87 REMARK 500 O HOH L 438 O HOH L 589 1.87 REMARK 500 O HOH L 401 O HOH L 453 1.91 REMARK 500 OD2 ASP L 190 O HOH L 402 1.93 REMARK 500 O HOH H 518 O HOH L 439 1.93 REMARK 500 O HOH H 625 O HOH H 696 2.01 REMARK 500 O HOH H 413 O HOH H 645 2.03 REMARK 500 O HOH H 406 O HOH H 627 2.03 REMARK 500 O HOH H 424 O HOH H 618 2.03 REMARK 500 O HOH H 483 O HOH H 607 2.03 REMARK 500 O HOH L 402 O HOH L 479 2.05 REMARK 500 O HOH H 518 O HOH H 624 2.09 REMARK 500 O HOH H 525 O HOH H 579 2.10 REMARK 500 O HOH H 618 O HOH H 666 2.11 REMARK 500 O HOH L 453 O HOH L 634 2.13 REMARK 500 O HOH H 432 O HOH H 666 2.13 REMARK 500 O HOH H 489 O HOH L 409 2.13 REMARK 500 O HOH L 690 O HOH L 693 2.14 REMARK 500 O HOH L 583 O HOH L 690 2.14 REMARK 500 O HOH H 665 O HOH H 712 2.15 REMARK 500 O HOH L 648 O HOH L 683 2.16 REMARK 500 O HOH L 574 O HOH L 607 2.18 REMARK 500 OD2 ASP H 209 O HOH H 402 2.18 REMARK 500 O HOH L 443 O HOH L 692 2.18 REMARK 500 OD2 ASP H 66 O HOH H 403 2.19 REMARK 500 O HOH L 607 O HOH L 639 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 H 604 O HOH L 452 3575 1.90 REMARK 500 O HOH H 528 O HOH L 636 3565 1.96 REMARK 500 O HOH H 656 O HOH L 436 3565 1.97 REMARK 500 OD2 ASP H 55 NZ LYS L 174 3465 1.99 REMARK 500 O HOH H 523 O HOH H 601 2555 2.04 REMARK 500 O HOH L 735 O HOH L 752 3565 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 MET H 34 CA - CB - CG ANGL. DEV. = -15.6 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER H 85 64.40 36.87 REMARK 500 SER H 85 64.40 39.28 REMARK 500 SER H 99 -130.28 49.95 REMARK 500 VAL L 56 -49.13 73.93 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 L 762 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH L 763 DISTANCE = 6.05 ANGSTROMS REMARK 525 HOH L 764 DISTANCE = 6.33 ANGSTROMS REMARK 525 HOH L 765 DISTANCE = 6.45 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9B88 RELATED DB: PDB DBREF 9BX5 H 1 221 PDB 9BX5 9BX5 1 221 DBREF 9BX5 L 1 219 PDB 9BX5 9BX5 1 219 DBREF 9BX5 P 141 144 UNP Q07337 OSPC_BORBU 141 144 SEQRES 1 H 221 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 221 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 H 221 TYR THR PHE SER ASN SER TRP MET ASN TRP VAL LYS GLN SEQRES 4 H 221 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ARG ILE TYR SEQRES 5 H 221 PRO GLY ASP GLY ASP THR ASN TYR ASN GLY LYS PHE LYS SEQRES 6 H 221 ASP LYS ALA THR LEU THR THR ASP LYS SER SER SER THR SEQRES 7 H 221 ALA TYR MET ARG LEU SER SER LEU THR SER VAL ASP SER SEQRES 8 H 221 ALA VAL TYR PHE CYS ALA ARG SER LEU PHE ASP TYR TRP SEQRES 9 H 221 GLY GLN GLY THR THR LEU THR VAL SER SER ALA SER THR SEQRES 10 H 221 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 H 221 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 H 221 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 H 221 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 H 221 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 H 221 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 H 221 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 H 221 ASP LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 L 219 ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SER VAL SEQRES 2 L 219 THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 L 219 GLN SER LEU LEU ASP SER ASP GLY LYS THR TYR LEU ILE SEQRES 4 L 219 TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5 L 219 ILE TYR LEU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 L 219 TYR CYS CYS GLN GLY THR HIS PHE PRO PHE THR PHE GLY SEQRES 9 L 219 VAL GLY THR LYS LEU GLU LEU LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 P 4 LYS HIS THR ASP HET CL H 301 1 HET CL L 301 1 HET CL L 302 1 HET CL L 303 1 HET EDO L 304 4 HETNAM CL CHLORIDE ION HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 4 CL 4(CL 1-) FORMUL 8 EDO C2 H6 O2 FORMUL 9 HOH *693(H2 O) HELIX 1 AA1 THR H 28 SER H 32 5 5 HELIX 2 AA2 GLY H 62 LYS H 65 5 4 HELIX 3 AA3 LYS H 74 SER H 76 5 3 HELIX 4 AA4 THR H 87 SER H 91 5 5 HELIX 5 AA5 SER H 157 ALA H 159 5 3 HELIX 6 AA6 SER H 188 LEU H 190 5 3 HELIX 7 AA7 LYS H 202 ASN H 205 5 4 HELIX 8 AA8 GLU L 84 LEU L 88 5 5 HELIX 9 AA9 SER L 126 GLY L 133 1 8 HELIX 10 AB1 LYS L 188 GLU L 192 1 5 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O MET H 81 N ILE H 20 SHEET 4 AA1 4 ALA H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 108 VAL H 112 1 O THR H 109 N GLU H 10 SHEET 3 AA2 6 ALA H 92 ARG H 98 -1 N ALA H 92 O LEU H 110 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N ASN H 35 O ALA H 97 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O ASN H 59 N ARG H 50 SHEET 1 AA3 4 SER H 121 LEU H 125 0 SHEET 2 AA3 4 THR H 136 TYR H 146 -1 O LEU H 142 N PHE H 123 SHEET 3 AA3 4 TYR H 177 PRO H 186 -1 O LEU H 179 N VAL H 143 SHEET 4 AA3 4 VAL H 164 THR H 166 -1 N HIS H 165 O VAL H 182 SHEET 1 AA4 4 SER H 121 LEU H 125 0 SHEET 2 AA4 4 THR H 136 TYR H 146 -1 O LEU H 142 N PHE H 123 SHEET 3 AA4 4 TYR H 177 PRO H 186 -1 O LEU H 179 N VAL H 143 SHEET 4 AA4 4 VAL H 170 LEU H 171 -1 N VAL H 170 O SER H 178 SHEET 1 AA5 3 THR H 152 TRP H 155 0 SHEET 2 AA5 3 ILE H 196 HIS H 201 -1 O ASN H 198 N SER H 154 SHEET 3 AA5 3 THR H 206 ARG H 211 -1 O VAL H 208 N VAL H 199 SHEET 1 AA6 4 MET L 4 THR L 7 0 SHEET 2 AA6 4 ALA L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AA6 4 ASP L 75 ILE L 80 -1 O PHE L 76 N CYS L 23 SHEET 4 AA6 4 PHE L 67 SER L 72 -1 N THR L 68 O LYS L 79 SHEET 1 AA7 6 THR L 10 VAL L 13 0 SHEET 2 AA7 6 THR L 107 LEU L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AA7 6 GLY L 89 GLN L 95 -1 N GLY L 89 O LEU L 109 SHEET 4 AA7 6 LEU L 38 GLN L 43 -1 N LEU L 41 O TYR L 92 SHEET 5 AA7 6 PRO L 49 TYR L 54 -1 O LEU L 52 N TRP L 40 SHEET 6 AA7 6 LYS L 58 LEU L 59 -1 O LYS L 58 N TYR L 54 SHEET 1 AA8 4 THR L 10 VAL L 13 0 SHEET 2 AA8 4 THR L 107 LEU L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AA8 4 GLY L 89 GLN L 95 -1 N GLY L 89 O LEU L 109 SHEET 4 AA8 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AA9 4 SER L 119 PHE L 123 0 SHEET 2 AA9 4 THR L 134 PHE L 144 -1 O LEU L 140 N PHE L 121 SHEET 3 AA9 4 TYR L 178 SER L 187 -1 O LEU L 180 N LEU L 141 SHEET 4 AA9 4 SER L 164 VAL L 168 -1 N SER L 167 O SER L 181 SHEET 1 AB1 4 ALA L 158 LEU L 159 0 SHEET 2 AB1 4 LYS L 150 VAL L 155 -1 N VAL L 155 O ALA L 158 SHEET 3 AB1 4 VAL L 196 THR L 202 -1 O GLU L 200 N GLN L 152 SHEET 4 AB1 4 VAL L 210 ASN L 215 -1 O VAL L 210 N VAL L 201 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.08 SSBOND 2 CYS H 141 CYS H 197 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 93 1555 1555 2.09 SSBOND 4 CYS L 139 CYS L 199 1555 1555 2.01 CISPEP 1 PHE H 147 PRO H 148 0 -8.10 CISPEP 2 GLU H 149 PRO H 150 0 -0.43 CISPEP 3 THR L 7 PRO L 8 0 -14.15 CISPEP 4 PHE L 99 PRO L 100 0 -2.84 CISPEP 5 TYR L 145 PRO L 146 0 3.37 CRYST1 67.657 69.389 95.102 90.00 90.00 90.00 P 21 2 21 4 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 0.014780 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014412 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010515 0.00000