HEADER IMMUNE SYSTEM 30-MAY-24 9C24 TITLE FAB F946 IN COMPLEX WITH OSPCB COMPND MOL_ID: 1; COMPND 2 MOLECULE: F946 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: F946 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: OUTER SURFACE PROTEIN C; COMPND 11 CHAIN: C, D; COMPND 12 FRAGMENT: RESIDUES 38-202; COMPND 13 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; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI B; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 37762 KEYWDS FAB-ANTIGEN COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.J.RUDOLPH,N.MANTIS REVDAT 1 27-AUG-25 9C24 0 JRNL AUTH M.J.RUDOLPH,N.MANTIS JRNL TITL FAB F946 IN COMPLEX WITH OSPCB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.91 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 35013 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.237 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.288 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820 REMARK 3 FREE R VALUE TEST SET COUNT : 1688 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 48.9100 - 6.4200 0.99 2995 137 0.2110 0.2417 REMARK 3 2 6.4100 - 5.0900 1.00 2887 136 0.2185 0.2762 REMARK 3 3 5.0900 - 4.4500 1.00 2855 146 0.1778 0.2357 REMARK 3 4 4.4500 - 4.0400 1.00 2811 161 0.1973 0.2561 REMARK 3 5 4.0400 - 3.7500 1.00 2796 141 0.2202 0.2997 REMARK 3 6 3.7500 - 3.5300 1.00 2816 141 0.2582 0.3011 REMARK 3 7 3.5300 - 3.3600 1.00 2785 140 0.2855 0.3277 REMARK 3 8 3.3600 - 3.2100 1.00 2794 139 0.2887 0.3595 REMARK 3 9 3.2100 - 3.0900 1.00 2791 138 0.2775 0.3617 REMARK 3 10 3.0900 - 2.9800 1.00 2781 144 0.3176 0.3718 REMARK 3 11 2.9800 - 2.8900 0.96 2654 142 0.3297 0.3899 REMARK 3 12 2.8900 - 2.8000 0.85 2360 123 0.3780 0.4133 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) : 0.490 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.450 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.003 8813 REMARK 3 ANGLE : 0.718 11938 REMARK 3 CHIRALITY : 0.042 1393 REMARK 3 PLANARITY : 0.006 1495 REMARK 3 DIHEDRAL : 6.934 1187 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 32 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.8865 41.2206 -33.8012 REMARK 3 T TENSOR REMARK 3 T11: 0.2615 T22: 0.4028 REMARK 3 T33: 0.4046 T12: -0.0332 REMARK 3 T13: 0.0563 T23: 0.0418 REMARK 3 L TENSOR REMARK 3 L11: 4.2826 L22: 4.5882 REMARK 3 L33: 2.2955 L12: -1.2914 REMARK 3 L13: -0.3566 L23: 1.3410 REMARK 3 S TENSOR REMARK 3 S11: 0.1375 S12: 0.3476 S13: 0.1810 REMARK 3 S21: -0.0488 S22: -0.1085 S23: 0.5884 REMARK 3 S31: -0.1461 S32: -0.3421 S33: -0.0116 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 120 THROUGH 153 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.1290 47.0272 -6.6873 REMARK 3 T TENSOR REMARK 3 T11: 0.9225 T22: 0.8753 REMARK 3 T33: 1.1494 T12: 0.0532 REMARK 3 T13: 0.4483 T23: -0.0870 REMARK 3 L TENSOR REMARK 3 L11: 5.6765 L22: 7.0819 REMARK 3 L33: 3.6061 L12: -1.3702 REMARK 3 L13: -0.8435 L23: 0.4299 REMARK 3 S TENSOR REMARK 3 S11: -0.4750 S12: -1.0177 S13: -0.6503 REMARK 3 S21: 2.1306 S22: -0.0267 S23: 0.1361 REMARK 3 S31: -0.3094 S32: -0.6812 S33: 0.4768 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 154 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.6832 46.1889 -11.3174 REMARK 3 T TENSOR REMARK 3 T11: 1.1608 T22: 0.5668 REMARK 3 T33: 0.8370 T12: 0.0437 REMARK 3 T13: 0.3553 T23: -0.0173 REMARK 3 L TENSOR REMARK 3 L11: 9.6337 L22: 7.2635 REMARK 3 L33: 8.8204 L12: -1.5950 REMARK 3 L13: 2.7955 L23: -1.5212 REMARK 3 S TENSOR REMARK 3 S11: 0.0178 S12: -0.6908 S13: 0.2045 REMARK 3 S21: 2.5208 S22: -0.2545 S23: 0.8010 REMARK 3 S31: -0.4268 S32: -0.4864 S33: 0.2030 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 165 THROUGH 187 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.3972 40.9788 -8.1908 REMARK 3 T TENSOR REMARK 3 T11: 1.2201 T22: 0.6666 REMARK 3 T33: 1.0430 T12: 0.0072 REMARK 3 T13: 0.5469 T23: -0.0676 REMARK 3 L TENSOR REMARK 3 L11: 4.6651 L22: 2.3744 REMARK 3 L33: 3.1986 L12: -0.3022 REMARK 3 L13: 0.1880 L23: 0.2358 REMARK 3 S TENSOR REMARK 3 S11: -0.0408 S12: -0.2428 S13: 0.2103 REMARK 3 S21: 1.7982 S22: -0.0605 S23: 0.8944 REMARK 3 S31: 0.1140 S32: -0.0182 S33: 0.1619 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 188 THROUGH 205 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.1546 40.3640 6.0879 REMARK 3 T TENSOR REMARK 3 T11: 2.7478 T22: 1.0410 REMARK 3 T33: 0.8745 T12: 0.0146 REMARK 3 T13: 0.0991 T23: -0.1541 REMARK 3 L TENSOR REMARK 3 L11: 4.6443 L22: 0.1794 REMARK 3 L33: 4.8122 L12: 0.5356 REMARK 3 L13: -4.5059 L23: -0.6231 REMARK 3 S TENSOR REMARK 3 S11: -0.3878 S12: -1.7549 S13: 0.7147 REMARK 3 S21: 2.5983 S22: -0.6374 S23: -0.4053 REMARK 3 S31: -0.3987 S32: 1.1265 S33: 0.8373 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 206 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.7932 51.8256 -9.0414 REMARK 3 T TENSOR REMARK 3 T11: 1.3809 T22: 0.7343 REMARK 3 T33: 1.2126 T12: 0.0306 REMARK 3 T13: 0.5386 T23: -0.1289 REMARK 3 L TENSOR REMARK 3 L11: 6.6390 L22: 4.3141 REMARK 3 L33: 4.1218 L12: -0.2683 REMARK 3 L13: 0.7923 L23: 0.5109 REMARK 3 S TENSOR REMARK 3 S11: -0.0095 S12: -0.6145 S13: 1.3038 REMARK 3 S21: 2.0807 S22: -0.5555 S23: 1.0414 REMARK 3 S31: -0.0096 S32: -0.3457 S33: 0.3592 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID -1 THROUGH 12 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.2292 19.3323 -28.9415 REMARK 3 T TENSOR REMARK 3 T11: 0.6342 T22: 0.6295 REMARK 3 T33: 1.0868 T12: -0.3008 REMARK 3 T13: 0.3461 T23: -0.2361 REMARK 3 L TENSOR REMARK 3 L11: 5.0511 L22: 4.5777 REMARK 3 L33: 3.2518 L12: -0.5092 REMARK 3 L13: -0.0105 L23: 0.3352 REMARK 3 S TENSOR REMARK 3 S11: -0.2885 S12: 0.8055 S13: -0.8380 REMARK 3 S21: 0.5897 S22: 0.0783 S23: 0.8541 REMARK 3 S31: 0.4896 S32: -1.0796 S33: 0.1022 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 13 THROUGH 23 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.8232 13.1560 -24.8458 REMARK 3 T TENSOR REMARK 3 T11: 1.2636 T22: 0.4822 REMARK 3 T33: 0.8699 T12: -0.2498 REMARK 3 T13: 0.4300 T23: -0.0254 REMARK 3 L TENSOR REMARK 3 L11: 4.9743 L22: 4.7285 REMARK 3 L33: 4.2835 L12: -1.9983 REMARK 3 L13: -0.5879 L23: -3.8517 REMARK 3 S TENSOR REMARK 3 S11: -0.9841 S12: 0.4524 S13: -1.1750 REMARK 3 S21: 1.4561 S22: -0.1691 S23: 0.6508 REMARK 3 S31: 1.7397 S32: -0.2334 S33: 0.5718 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 24 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.5229 22.0843 -28.5646 REMARK 3 T TENSOR REMARK 3 T11: 0.4198 T22: 0.3629 REMARK 3 T33: 0.4989 T12: -0.1373 REMARK 3 T13: 0.0775 T23: -0.0583 REMARK 3 L TENSOR REMARK 3 L11: 3.5072 L22: 7.1179 REMARK 3 L33: 4.9406 L12: -1.5597 REMARK 3 L13: -2.0625 L23: 1.3516 REMARK 3 S TENSOR REMARK 3 S11: -0.1731 S12: -0.0156 S13: -0.5424 REMARK 3 S21: 0.8166 S22: 0.1021 S23: 0.4185 REMARK 3 S31: 0.9407 S32: -0.3052 S33: 0.0529 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 100 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.3818 34.1258 -2.1185 REMARK 3 T TENSOR REMARK 3 T11: 1.5592 T22: 0.7510 REMARK 3 T33: 0.9459 T12: -0.1053 REMARK 3 T13: 1.2961 T23: 0.0573 REMARK 3 L TENSOR REMARK 3 L11: 1.4542 L22: 0.7332 REMARK 3 L33: 0.3661 L12: 0.6979 REMARK 3 L13: 0.2768 L23: -0.1302 REMARK 3 S TENSOR REMARK 3 S11: -1.5972 S12: -0.6398 S13: 0.5215 REMARK 3 S21: 1.9196 S22: 0.3123 S23: 1.4942 REMARK 3 S31: 0.2354 S32: -0.1992 S33: 0.0943 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 127 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.3513 30.0872 -2.8069 REMARK 3 T TENSOR REMARK 3 T11: 1.7491 T22: 1.1235 REMARK 3 T33: 1.3774 T12: -0.2151 REMARK 3 T13: 0.8623 T23: 0.0694 REMARK 3 L TENSOR REMARK 3 L11: 4.0672 L22: 3.8581 REMARK 3 L33: 5.5494 L12: -1.2500 REMARK 3 L13: 1.8369 L23: 3.3606 REMARK 3 S TENSOR REMARK 3 S11: 0.1279 S12: -1.2593 S13: -0.9235 REMARK 3 S21: -0.7058 S22: -0.9280 S23: -0.7064 REMARK 3 S31: 1.1933 S32: -0.8131 S33: 0.7621 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 148 THROUGH 186 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.6797 35.4429 -4.4491 REMARK 3 T TENSOR REMARK 3 T11: 1.6760 T22: 0.9776 REMARK 3 T33: 1.2550 T12: -0.3165 REMARK 3 T13: 0.8860 T23: -0.1307 REMARK 3 L TENSOR REMARK 3 L11: 4.7413 L22: 1.4657 REMARK 3 L33: 0.8315 L12: -0.9391 REMARK 3 L13: 1.2957 L23: 0.4213 REMARK 3 S TENSOR REMARK 3 S11: -0.2692 S12: -1.2731 S13: 0.5262 REMARK 3 S21: -0.5957 S22: 0.0178 S23: 0.5091 REMARK 3 S31: 0.3047 S32: -0.1270 S33: 0.1340 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 187 THROUGH 208 ) REMARK 3 ORIGIN FOR THE GROUP (A): -48.8008 29.5952 4.2491 REMARK 3 T TENSOR REMARK 3 T11: 1.3807 T22: 1.5115 REMARK 3 T33: 1.3433 T12: -0.0925 REMARK 3 T13: 0.6647 T23: 0.1448 REMARK 3 L TENSOR REMARK 3 L11: 3.0357 L22: 5.1164 REMARK 3 L33: 1.5666 L12: -1.8536 REMARK 3 L13: 0.7557 L23: 1.0085 REMARK 3 S TENSOR REMARK 3 S11: -0.2172 S12: -0.4575 S13: -0.8522 REMARK 3 S21: -0.6184 S22: 0.3344 S23: -0.2729 REMARK 3 S31: 0.6892 S32: -1.4019 S33: -0.0633 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.8567 4.5728 -71.6841 REMARK 3 T TENSOR REMARK 3 T11: 0.2526 T22: 0.3421 REMARK 3 T33: 0.3954 T12: 0.0342 REMARK 3 T13: 0.1046 T23: 0.0165 REMARK 3 L TENSOR REMARK 3 L11: 2.6741 L22: 3.2437 REMARK 3 L33: 6.9747 L12: 1.0508 REMARK 3 L13: 2.9848 L23: 0.7723 REMARK 3 S TENSOR REMARK 3 S11: 0.0688 S12: -0.2237 S13: -0.1491 REMARK 3 S21: -0.2250 S22: 0.0187 S23: 0.0184 REMARK 3 S31: -0.2200 S32: -0.6639 S33: -0.0798 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.5271 7.7773 -87.5333 REMARK 3 T TENSOR REMARK 3 T11: 0.5710 T22: 0.4699 REMARK 3 T33: 0.4328 T12: 0.0649 REMARK 3 T13: 0.1243 T23: 0.0034 REMARK 3 L TENSOR REMARK 3 L11: 1.8993 L22: 0.8139 REMARK 3 L33: 3.2504 L12: 0.8627 REMARK 3 L13: 0.3560 L23: -0.0728 REMARK 3 S TENSOR REMARK 3 S11: -0.0088 S12: 0.4354 S13: 0.0470 REMARK 3 S21: -0.5284 S22: 0.3365 S23: -0.1099 REMARK 3 S31: -0.1551 S32: 0.0950 S33: -0.3435 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 194 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.7023 6.3909-105.0918 REMARK 3 T TENSOR REMARK 3 T11: 0.9311 T22: 1.0368 REMARK 3 T33: 0.9896 T12: -0.1206 REMARK 3 T13: 0.4491 T23: -0.0391 REMARK 3 L TENSOR REMARK 3 L11: 1.6879 L22: 6.3516 REMARK 3 L33: 4.4867 L12: 1.3160 REMARK 3 L13: 1.1420 L23: -2.6535 REMARK 3 S TENSOR REMARK 3 S11: 0.0323 S12: 1.6526 S13: -0.8297 REMARK 3 S21: -0.2299 S22: 0.0598 S23: -1.0784 REMARK 3 S31: -0.6650 S32: 0.6030 S33: -0.1385 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 195 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.4612 0.8246-111.2593 REMARK 3 T TENSOR REMARK 3 T11: 0.9558 T22: 1.3438 REMARK 3 T33: 1.1166 T12: -0.2090 REMARK 3 T13: 0.3459 T23: -0.1720 REMARK 3 L TENSOR REMARK 3 L11: 7.5073 L22: 2.9166 REMARK 3 L33: 1.3246 L12: -3.4839 REMARK 3 L13: 0.0681 L23: 1.2492 REMARK 3 S TENSOR REMARK 3 S11: 0.0436 S12: 0.4593 S13: -1.3288 REMARK 3 S21: -1.0855 S22: -0.6546 S23: -0.2374 REMARK 3 S31: 0.6595 S32: 1.7237 S33: 0.6534 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.3402 28.2240 -77.9945 REMARK 3 T TENSOR REMARK 3 T11: 1.0345 T22: 0.4708 REMARK 3 T33: 0.6567 T12: 0.0582 REMARK 3 T13: 0.2277 T23: 0.0608 REMARK 3 L TENSOR REMARK 3 L11: 2.6758 L22: 2.7396 REMARK 3 L33: 7.6756 L12: 0.2294 REMARK 3 L13: 0.5787 L23: -0.5669 REMARK 3 S TENSOR REMARK 3 S11: -0.0614 S12: 0.3983 S13: 1.1033 REMARK 3 S21: -1.0861 S22: 0.1776 S23: -0.4415 REMARK 3 S31: -1.7430 S32: -0.1935 S33: -0.1348 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 74 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.2999 19.8836 -94.0984 REMARK 3 T TENSOR REMARK 3 T11: 1.8784 T22: 0.6755 REMARK 3 T33: 0.5636 T12: -0.0375 REMARK 3 T13: 0.0823 T23: 0.1172 REMARK 3 L TENSOR REMARK 3 L11: 1.3666 L22: 0.3026 REMARK 3 L33: 3.6020 L12: 0.3102 REMARK 3 L13: 0.0810 L23: 0.5050 REMARK 3 S TENSOR REMARK 3 S11: -0.4050 S12: 0.6817 S13: 0.3764 REMARK 3 S21: -1.4428 S22: 0.4555 S23: 0.0950 REMARK 3 S31: -0.0792 S32: -0.2401 S33: -0.0658 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 127 THROUGH 208 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.1933 17.7550-112.1010 REMARK 3 T TENSOR REMARK 3 T11: 2.2988 T22: 1.1050 REMARK 3 T33: 0.6483 T12: -0.2288 REMARK 3 T13: 0.0723 T23: 0.1278 REMARK 3 L TENSOR REMARK 3 L11: 1.5454 L22: 1.6335 REMARK 3 L33: 4.1558 L12: -1.6442 REMARK 3 L13: 1.2947 L23: -0.9005 REMARK 3 S TENSOR REMARK 3 S11: -0.1280 S12: 0.3585 S13: 0.1164 REMARK 3 S21: -1.6673 S22: 0.2569 S23: -0.0059 REMARK 3 S31: -0.5917 S32: -0.1946 S33: -0.2124 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 40 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.0514 18.7304 -49.9559 REMARK 3 T TENSOR REMARK 3 T11: 0.4073 T22: 0.7026 REMARK 3 T33: 0.7694 T12: 0.0679 REMARK 3 T13: 0.1841 T23: 0.0286 REMARK 3 L TENSOR REMARK 3 L11: 5.7605 L22: 2.0088 REMARK 3 L33: 4.5260 L12: -1.7173 REMARK 3 L13: -5.0735 L23: 1.2081 REMARK 3 S TENSOR REMARK 3 S11: 0.4126 S12: 0.2479 S13: 0.5726 REMARK 3 S21: 0.2288 S22: 0.5362 S23: 1.4769 REMARK 3 S31: 0.6999 S32: -0.7086 S33: -0.8099 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 49 THROUGH 93 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.1867 24.6470 -43.3291 REMARK 3 T TENSOR REMARK 3 T11: 0.4182 T22: 0.5915 REMARK 3 T33: 1.1623 T12: 0.0461 REMARK 3 T13: 0.0127 T23: -0.1255 REMARK 3 L TENSOR REMARK 3 L11: 2.3599 L22: 2.4761 REMARK 3 L33: 2.2264 L12: 0.5403 REMARK 3 L13: 1.7210 L23: 0.9013 REMARK 3 S TENSOR REMARK 3 S11: 0.4957 S12: -0.0361 S13: 2.0121 REMARK 3 S21: 0.3120 S22: -0.3584 S23: -0.7220 REMARK 3 S31: 0.0375 S32: 0.4974 S33: -0.0964 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 94 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.4137 15.8516 -35.6853 REMARK 3 T TENSOR REMARK 3 T11: 0.5097 T22: 0.6149 REMARK 3 T33: 0.3803 T12: -0.0155 REMARK 3 T13: -0.0735 T23: -0.0572 REMARK 3 L TENSOR REMARK 3 L11: 7.0537 L22: 6.1336 REMARK 3 L33: 6.4212 L12: 1.2964 REMARK 3 L13: 4.9574 L23: 0.5273 REMARK 3 S TENSOR REMARK 3 S11: 0.4480 S12: -2.0985 S13: -0.1204 REMARK 3 S21: 0.5471 S22: -0.3693 S23: -0.4608 REMARK 3 S31: 0.6721 S32: -0.3310 S33: -0.0130 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 114 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.4187 9.1131 -45.9551 REMARK 3 T TENSOR REMARK 3 T11: 0.7866 T22: 1.2136 REMARK 3 T33: 0.8643 T12: -0.3167 REMARK 3 T13: -0.3289 T23: -0.0079 REMARK 3 L TENSOR REMARK 3 L11: 4.2118 L22: 9.4514 REMARK 3 L33: 2.1862 L12: -1.2310 REMARK 3 L13: 2.8355 L23: 0.7473 REMARK 3 S TENSOR REMARK 3 S11: 0.9952 S12: -0.8111 S13: -1.6810 REMARK 3 S21: 0.0669 S22: -0.0911 S23: 1.9035 REMARK 3 S31: 1.3060 S32: -2.3752 S33: -0.7452 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 121 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.2482 9.3104 -39.6149 REMARK 3 T TENSOR REMARK 3 T11: 0.6693 T22: 0.6163 REMARK 3 T33: 0.8888 T12: 0.1677 REMARK 3 T13: -0.1878 T23: -0.1379 REMARK 3 L TENSOR REMARK 3 L11: 7.3244 L22: 4.0718 REMARK 3 L33: 6.2984 L12: -1.9586 REMARK 3 L13: 3.9530 L23: -0.4576 REMARK 3 S TENSOR REMARK 3 S11: 0.8985 S12: 0.0785 S13: -1.0748 REMARK 3 S21: 0.5927 S22: -0.1147 S23: -0.8981 REMARK 3 S31: 1.3130 S32: 0.8313 S33: -0.7917 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 156 THROUGH 170 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.8177 13.1228 -47.3829 REMARK 3 T TENSOR REMARK 3 T11: 0.6316 T22: 0.7009 REMARK 3 T33: 1.1184 T12: 0.0074 REMARK 3 T13: 0.0744 T23: -0.0677 REMARK 3 L TENSOR REMARK 3 L11: 1.8580 L22: 3.2037 REMARK 3 L33: 8.8762 L12: -0.9736 REMARK 3 L13: 1.7591 L23: 3.4904 REMARK 3 S TENSOR REMARK 3 S11: 0.7644 S12: 0.9145 S13: -1.0795 REMARK 3 S21: -0.1213 S22: 0.1677 S23: -1.0228 REMARK 3 S31: 1.5079 S32: 0.1303 S33: -0.8237 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 171 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.4210 14.1439 -52.6241 REMARK 3 T TENSOR REMARK 3 T11: 0.3437 T22: 0.5427 REMARK 3 T33: 0.3939 T12: 0.0785 REMARK 3 T13: 0.0473 T23: -0.0571 REMARK 3 L TENSOR REMARK 3 L11: 3.7998 L22: 2.4938 REMARK 3 L33: 5.8219 L12: -0.7926 REMARK 3 L13: 4.8413 L23: -0.6942 REMARK 3 S TENSOR REMARK 3 S11: 1.2050 S12: 0.7217 S13: -0.6357 REMARK 3 S21: 0.0971 S22: -0.5391 S23: -0.3182 REMARK 3 S31: 0.5660 S32: -0.0307 S33: -0.5290 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 41 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.8592 28.0509 -46.1110 REMARK 3 T TENSOR REMARK 3 T11: 0.3321 T22: 0.5789 REMARK 3 T33: 0.6044 T12: 0.0010 REMARK 3 T13: 0.0867 T23: -0.1270 REMARK 3 L TENSOR REMARK 3 L11: 2.8997 L22: 3.3571 REMARK 3 L33: 3.7376 L12: -2.2013 REMARK 3 L13: 3.6279 L23: -2.6950 REMARK 3 S TENSOR REMARK 3 S11: -0.1681 S12: -0.0384 S13: 0.9334 REMARK 3 S21: -0.4058 S22: -0.3745 S23: -0.8695 REMARK 3 S31: 0.4455 S32: 0.2852 S33: 0.3767 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 76 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.4077 26.2011 -36.8831 REMARK 3 T TENSOR REMARK 3 T11: 0.4210 T22: 0.9082 REMARK 3 T33: 1.0416 T12: -0.0435 REMARK 3 T13: 0.0211 T23: -0.1579 REMARK 3 L TENSOR REMARK 3 L11: 2.7971 L22: 3.9206 REMARK 3 L33: 4.7673 L12: -2.3407 REMARK 3 L13: 3.3270 L23: -1.5194 REMARK 3 S TENSOR REMARK 3 S11: 0.3642 S12: -1.1132 S13: 0.4514 REMARK 3 S21: 0.1152 S22: 0.2122 S23: -0.7128 REMARK 3 S31: 0.4281 S32: -0.0490 S33: -0.2981 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 121 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.6041 39.2109 -37.5519 REMARK 3 T TENSOR REMARK 3 T11: 0.4013 T22: 0.7355 REMARK 3 T33: 2.1355 T12: -0.0960 REMARK 3 T13: 0.0485 T23: -0.2978 REMARK 3 L TENSOR REMARK 3 L11: 3.7004 L22: 1.0335 REMARK 3 L33: 3.3414 L12: -0.1961 REMARK 3 L13: 3.3909 L23: -0.7264 REMARK 3 S TENSOR REMARK 3 S11: -0.3654 S12: -0.3510 S13: 2.0607 REMARK 3 S21: -0.0059 S22: 0.3097 S23: -0.8031 REMARK 3 S31: -0.5162 S32: 0.2208 S33: 0.1731 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 152 THROUGH 170 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.9773 33.7246 -25.5843 REMARK 3 T TENSOR REMARK 3 T11: 0.5126 T22: 1.1622 REMARK 3 T33: 1.0551 T12: -0.0092 REMARK 3 T13: -0.0883 T23: -0.4897 REMARK 3 L TENSOR REMARK 3 L11: 0.2780 L22: 8.6048 REMARK 3 L33: 3.3478 L12: -1.1881 REMARK 3 L13: 0.3891 L23: -1.3491 REMARK 3 S TENSOR REMARK 3 S11: -0.2801 S12: -1.5559 S13: 1.4883 REMARK 3 S21: 0.8052 S22: 0.6960 S23: -1.4417 REMARK 3 S31: -0.3506 S32: 1.2831 S33: -0.2933 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 171 THROUGH 202 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.7753 33.9434 -40.6766 REMARK 3 T TENSOR REMARK 3 T11: 0.3427 T22: 0.6779 REMARK 3 T33: 0.7772 T12: -0.1223 REMARK 3 T13: 0.1452 T23: -0.3058 REMARK 3 L TENSOR REMARK 3 L11: 8.6625 L22: 4.1107 REMARK 3 L33: 8.3209 L12: 3.7790 REMARK 3 L13: 5.9093 L23: 2.6519 REMARK 3 S TENSOR REMARK 3 S11: 0.4585 S12: -0.9349 S13: 1.6553 REMARK 3 S21: 0.2280 S22: -0.3885 S23: -0.4095 REMARK 3 S31: 0.1016 S32: -0.0163 S33: 0.1922 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 9C24 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_1000284587. 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 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 : 35099 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 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 (%) : 98.8 REMARK 200 DATA REDUNDANCY : 11.20 REMARK 200 R MERGE (I) : 0.12400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.9 REMARK 200 DATA REDUNDANCY IN SHELL : 7.30 REMARK 200 R MERGE FOR SHELL (I) : 0.76300 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 (%): 54.53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 210 MM CALCIUM CHLORIDE AND 18% PEG REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 38.89700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.33550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.22950 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 94.33550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.89700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.22950 REMARK 290 SMTRY3 4 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 15030 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 48430 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER H 137 REMARK 465 SER H 138 REMARK 465 LYS H 139 REMARK 465 SER H 140 REMARK 465 THR H 141 REMARK 465 SER H 142 REMARK 465 GLY H 143 REMARK 465 GLY H 144 REMARK 465 THR H 201 REMARK 465 GLN H 202 REMARK 465 ASP H 218 REMARK 465 LYS H 219 REMARK 465 ARG H 220 REMARK 465 VAL H 221 REMARK 465 GLU H 222 REMARK 465 PRO H 223 REMARK 465 LYS H 224 REMARK 465 SER H 225 REMARK 465 CYS H 226 REMARK 465 ASP H 227 REMARK 465 LYS H 228 REMARK 465 THR H 229 REMARK 465 HIS H 230 REMARK 465 ARG L 106 REMARK 465 ASP L 149 REMARK 465 ASN L 150 REMARK 465 ALA L 151 REMARK 465 VAL L 203 REMARK 465 ARG L 209 REMARK 465 GLY L 210 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER A 138 REMARK 465 LYS A 139 REMARK 465 SER A 140 REMARK 465 THR A 141 REMARK 465 SER A 142 REMARK 465 GLY A 143 REMARK 465 GLY A 144 REMARK 465 GLY A 200 REMARK 465 THR A 201 REMARK 465 GLN A 202 REMARK 465 THR A 203 REMARK 465 LYS A 219 REMARK 465 ARG A 220 REMARK 465 VAL A 221 REMARK 465 GLU A 222 REMARK 465 PRO A 223 REMARK 465 LYS A 224 REMARK 465 SER A 225 REMARK 465 CYS A 226 REMARK 465 ASP A 227 REMARK 465 LYS A 228 REMARK 465 THR A 229 REMARK 465 HIS A 230 REMARK 465 ASP B -1 REMARK 465 PRO B 139 REMARK 465 ARG B 209 REMARK 465 GLY B 210 REMARK 465 GLU B 211 REMARK 465 CYS B 212 REMARK 465 LYS C 38 REMARK 465 GLY C 39 REMARK 465 ASN C 115 REMARK 465 GLY C 116 REMARK 465 ALA C 165 REMARK 465 GLY C 166 REMARK 465 SER C 201 REMARK 465 PRO C 202 REMARK 465 LYS D 38 REMARK 465 GLY D 39 REMARK 465 PRO D 40 REMARK 465 ASN D 115 REMARK 465 GLY D 116 REMARK 465 SER D 117 REMARK 465 GLY D 166 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 OE1 GLN H 181 OG SER H 187 2.01 REMARK 500 O ASP L 183 OH TYR L 190 2.12 REMARK 500 O GLU C 132 OG1 THR C 136 2.14 REMARK 500 OE1 GLU C 44 O HOH C 301 2.19 REMARK 500 OE1 GLN A 181 OG SER A 187 2.19 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 ILE L 0 C - N - CA ANGL. DEV. = 16.3 DEGREES REMARK 500 GLU L 141 C - N - CA ANGL. DEV. = 16.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN H 33 157.54 65.33 REMARK 500 LEU H 102 -137.60 52.65 REMARK 500 PRO H 157 144.39 -38.28 REMARK 500 SER H 166 -118.51 49.80 REMARK 500 SER L 28 -131.96 56.33 REMARK 500 ALA L 48 18.87 54.12 REMARK 500 ALA L 49 -6.62 73.12 REMARK 500 SER L 75 -163.86 62.41 REMARK 500 PRO L 93 38.42 -88.62 REMARK 500 SER A 15 -0.76 71.11 REMARK 500 ASN A 33 153.90 73.79 REMARK 500 LEU A 102 -142.11 61.60 REMARK 500 PRO A 212 45.69 -84.14 REMARK 500 SER B 28 -135.90 45.81 REMARK 500 ALA B 48 18.69 53.98 REMARK 500 ALA B 49 -6.39 72.76 REMARK 500 THR B 67 -1.22 77.29 REMARK 500 LYS C 47 -5.74 74.56 REMARK 500 ASP C 83 0.82 -69.48 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 PHE H 156 PRO H 157 -111.34 REMARK 500 LYS C 47 LYS C 48 148.11 REMARK 500 ASP C 168 LYS C 169 137.44 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 321 DISTANCE = 6.53 ANGSTROMS DBREF 9C24 H 1 230 PDB 9C24 9C24 1 230 DBREF 9C24 L -1 212 PDB 9C24 9C24 -1 212 DBREF 9C24 A 1 230 PDB 9C24 9C24 1 230 DBREF 9C24 B -1 212 PDB 9C24 9C24 -1 212 DBREF 9C24 C 38 202 UNP Q44977 OSPC2_BORBG 38 202 DBREF 9C24 D 38 202 UNP Q44977 OSPC2_BORBG 38 202 SEQRES 1 H 230 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 230 PRO SER GLY THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 230 ALA SER ILE SER VAL GLY ASN TRP TRP SER TRP VAL ARG SEQRES 4 H 230 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU PHE SEQRES 5 H 230 TYR HIS SER GLY LYS THR ASN TYR ASN PRO SER LEU LYS SEQRES 6 H 230 SER ARG VAL THR ILE SER VAL ASP LYS SER LYS ASN GLN SEQRES 7 H 230 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 H 230 ALA VAL TYR TYR CYS ALA ARG SER ASP LEU LEU THR GLY SEQRES 9 H 230 TYR PHE PRO TYR TYR PHE ASP TYR TRP GLY GLN GLY THR SEQRES 10 H 230 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 230 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 230 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 230 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 230 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 230 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 230 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 230 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 H 230 GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 L 214 ASP ILE GLN LEU THR GLN SER PRO SER PHE LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN GLY ILE SER SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN ARG LEU SEQRES 8 L 214 ASN SER TYR PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 230 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 A 230 PRO SER GLY THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 A 230 ALA SER ILE SER VAL GLY ASN TRP TRP SER TRP VAL ARG SEQRES 4 A 230 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU PHE SEQRES 5 A 230 TYR HIS SER GLY LYS THR ASN TYR ASN PRO SER LEU LYS SEQRES 6 A 230 SER ARG VAL THR ILE SER VAL ASP LYS SER LYS ASN GLN SEQRES 7 A 230 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 A 230 ALA VAL TYR TYR CYS ALA ARG SER ASP LEU LEU THR GLY SEQRES 9 A 230 TYR PHE PRO TYR TYR PHE ASP TYR TRP GLY GLN GLY THR SEQRES 10 A 230 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 A 230 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 A 230 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 A 230 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 A 230 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 A 230 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 A 230 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 A 230 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 A 230 GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 B 214 ASP ILE GLN LEU THR GLN SER PRO SER PHE LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 214 GLN GLY ILE SER SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 B 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN ARG LEU SEQRES 8 B 214 ASN SER TYR PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 C 165 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 C 165 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 C 165 ALA LEU LEU SER SER ILE ASP GLU LEU ALA LYS ALA ILE SEQRES 4 C 165 GLY LYS LYS ILE LYS ASN ASP GLY SER LEU GLY ASP GLU SEQRES 5 C 165 ALA ASN HIS ASN GLU SER LEU LEU ALA GLY ALA TYR THR SEQRES 6 C 165 ILE SER THR LEU ILE THR GLN LYS LEU SER LYS LEU ASN SEQRES 7 C 165 GLY SER GLU GLY LEU LYS GLU LYS ILE ALA ALA ALA LYS SEQRES 8 C 165 LYS CYS SER GLU GLU PHE SER THR LYS LEU LYS ASP ASN SEQRES 9 C 165 HIS ALA GLN LEU GLY ILE GLN GLY VAL THR ASP GLU ASN SEQRES 10 C 165 ALA LYS LYS ALA ILE LEU LYS ALA ASN ALA ALA GLY LYS SEQRES 11 C 165 ASP LYS GLY VAL GLU GLU LEU GLU LYS LEU SER GLY SER SEQRES 12 C 165 LEU GLU SER LEU SER LYS ALA ALA LYS GLU MET LEU ALA SEQRES 13 C 165 ASN SER VAL LYS GLU LEU THR SER PRO SEQRES 1 D 165 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 D 165 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 D 165 ALA LEU LEU SER SER ILE ASP GLU LEU ALA LYS ALA ILE SEQRES 4 D 165 GLY LYS LYS ILE LYS ASN ASP GLY SER LEU GLY ASP GLU SEQRES 5 D 165 ALA ASN HIS ASN GLU SER LEU LEU ALA GLY ALA TYR THR SEQRES 6 D 165 ILE SER THR LEU ILE THR GLN LYS LEU SER LYS LEU ASN SEQRES 7 D 165 GLY SER GLU GLY LEU LYS GLU LYS ILE ALA ALA ALA LYS SEQRES 8 D 165 LYS CYS SER GLU GLU PHE SER THR LYS LEU LYS ASP ASN SEQRES 9 D 165 HIS ALA GLN LEU GLY ILE GLN GLY VAL THR ASP GLU ASN SEQRES 10 D 165 ALA LYS LYS ALA ILE LEU LYS ALA ASN ALA ALA GLY LYS SEQRES 11 D 165 ASP LYS GLY VAL GLU GLU LEU GLU LYS LEU SER GLY SER SEQRES 12 D 165 LEU GLU SER LEU SER LYS ALA ALA LYS GLU MET LEU ALA SEQRES 13 D 165 ASN SER VAL LYS GLU LEU THR SER PRO FORMUL 7 HOH *72(H2 O) HELIX 1 AA1 THR H 87 THR H 91 5 5 HELIX 2 AA2 GLN L 77 PHE L 81 5 5 HELIX 3 AA3 SER L 119 LYS L 124 1 6 HELIX 4 AA4 LYS L 181 HIS L 187 1 7 HELIX 5 AA5 PRO A 62 SER A 66 5 5 HELIX 6 AA6 THR A 87 THR A 91 5 5 HELIX 7 AA7 SER A 166 ALA A 168 5 3 HELIX 8 AA8 PRO A 195 LEU A 199 5 5 HELIX 9 AA9 GLN B 77 PHE B 81 5 5 HELIX 10 AB1 SER B 119 LYS B 124 1 6 HELIX 11 AB2 LYS B 181 GLU B 185 1 5 HELIX 12 AB3 ASN C 41 SER C 46 1 6 HELIX 13 AB4 LYS C 48 ALA C 75 1 28 HELIX 14 AB5 ASN C 93 LYS C 113 1 21 HELIX 15 AB6 LEU C 120 ASP C 140 1 21 HELIX 16 AB7 ASN C 141 GLY C 146 1 6 HELIX 17 AB8 THR C 151 LYS C 156 1 6 HELIX 18 AB9 GLY C 170 LEU C 199 1 30 HELIX 19 AC1 LEU D 42 LYS D 74 1 33 HELIX 20 AC2 ASN D 93 LYS D 113 1 21 HELIX 21 AC3 LEU D 120 ASP D 140 1 21 HELIX 22 AC4 ASN D 141 GLY D 146 1 6 HELIX 23 AC5 THR D 151 LEU D 160 1 10 HELIX 24 AC6 GLY D 170 SER D 201 1 32 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA1 4 GLN H 78 LEU H 83 -1 O LEU H 83 N LEU H 18 SHEET 4 AA1 4 VAL H 68 ASP H 73 -1 N ASP H 73 O GLN H 78 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 117 VAL H 121 1 O THR H 120 N VAL H 12 SHEET 3 AA2 6 ALA H 92 ASP H 100 -1 N TYR H 94 O THR H 117 SHEET 4 AA2 6 TRP H 34 GLN H 40 -1 N VAL H 38 O TYR H 95 SHEET 5 AA2 6 GLU H 47 TYR H 53 -1 O GLU H 47 N ARG H 39 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O ASN H 59 N GLU H 51 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 117 VAL H 121 1 O THR H 120 N VAL H 12 SHEET 3 AA3 4 ALA H 92 ASP H 100 -1 N TYR H 94 O THR H 117 SHEET 4 AA3 4 TYR H 109 TRP H 113 -1 O TYR H 109 N ASP H 100 SHEET 1 AA4 4 SER H 130 LEU H 134 0 SHEET 2 AA4 4 ALA H 146 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA4 4 TYR H 186 VAL H 194 -1 O VAL H 194 N ALA H 146 SHEET 4 AA4 4 VAL H 173 THR H 175 -1 N HIS H 174 O VAL H 191 SHEET 1 AA5 4 SER H 130 LEU H 134 0 SHEET 2 AA5 4 ALA H 146 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA5 4 TYR H 186 VAL H 194 -1 O VAL H 194 N ALA H 146 SHEET 4 AA5 4 VAL H 179 LEU H 180 -1 N VAL H 179 O SER H 187 SHEET 1 AA6 2 THR H 161 TRP H 164 0 SHEET 2 AA6 2 CYS H 206 ASN H 209 -1 O ASN H 209 N THR H 161 SHEET 1 AA7 4 LEU L 2 GLN L 4 0 SHEET 2 AA7 4 VAL L 17 ALA L 23 -1 O ARG L 22 N THR L 3 SHEET 3 AA7 4 GLU L 68 ILE L 73 -1 O PHE L 69 N CYS L 21 SHEET 4 AA7 4 PHE L 60 GLY L 64 -1 N SER L 61 O THR L 72 SHEET 1 AA8 6 PHE L 8 SER L 12 0 SHEET 2 AA8 6 THR L 100 LYS L 105 1 O LYS L 105 N ALA L 11 SHEET 3 AA8 6 ALA L 82 ARG L 88 -1 N ALA L 82 O LEU L 102 SHEET 4 AA8 6 LEU L 31 GLN L 36 -1 N GLN L 36 O THR L 83 SHEET 5 AA8 6 LYS L 43 TYR L 47 -1 O LYS L 43 N GLN L 35 SHEET 6 AA8 6 THR L 51 LEU L 52 -1 O THR L 51 N TYR L 47 SHEET 1 AA9 4 SER L 112 PHE L 116 0 SHEET 2 AA9 4 THR L 127 ASN L 135 -1 O ASN L 135 N SER L 112 SHEET 3 AA9 4 SER L 172 SER L 180 -1 O LEU L 179 N ALA L 128 SHEET 4 AA9 4 GLU L 159 VAL L 161 -1 N SER L 160 O SER L 174 SHEET 1 AB1 3 GLN L 145 LYS L 147 0 SHEET 2 AB1 3 TYR L 190 GLU L 193 -1 O ALA L 191 N LYS L 147 SHEET 3 AB1 3 LYS L 205 PHE L 207 -1 O PHE L 207 N TYR L 190 SHEET 1 AB2 4 GLN A 3 SER A 7 0 SHEET 2 AB2 4 LEU A 18 SER A 25 -1 O THR A 23 N GLN A 5 SHEET 3 AB2 4 GLN A 78 LEU A 83 -1 O LEU A 83 N LEU A 18 SHEET 4 AB2 4 VAL A 68 ASP A 73 -1 N ASP A 73 O GLN A 78 SHEET 1 AB3 6 LEU A 11 VAL A 12 0 SHEET 2 AB3 6 THR A 117 VAL A 121 1 O THR A 120 N VAL A 12 SHEET 3 AB3 6 ALA A 92 ASP A 100 -1 N TYR A 94 O THR A 117 SHEET 4 AB3 6 TRP A 34 GLN A 40 -1 N VAL A 38 O TYR A 95 SHEET 5 AB3 6 GLU A 47 PHE A 52 -1 O GLU A 47 N ARG A 39 SHEET 6 AB3 6 THR A 58 TYR A 60 -1 O ASN A 59 N GLU A 51 SHEET 1 AB4 4 LEU A 11 VAL A 12 0 SHEET 2 AB4 4 THR A 117 VAL A 121 1 O THR A 120 N VAL A 12 SHEET 3 AB4 4 ALA A 92 ASP A 100 -1 N TYR A 94 O THR A 117 SHEET 4 AB4 4 TYR A 109 TRP A 113 -1 O TYR A 109 N ASP A 100 SHEET 1 AB5 4 SER A 130 LEU A 134 0 SHEET 2 AB5 4 ALA A 146 TYR A 155 -1 O LYS A 153 N SER A 130 SHEET 3 AB5 4 TYR A 186 VAL A 194 -1 O VAL A 194 N ALA A 146 SHEET 4 AB5 4 VAL A 173 THR A 175 -1 N HIS A 174 O VAL A 191 SHEET 1 AB6 4 SER A 130 LEU A 134 0 SHEET 2 AB6 4 ALA A 146 TYR A 155 -1 O LYS A 153 N SER A 130 SHEET 3 AB6 4 TYR A 186 VAL A 194 -1 O VAL A 194 N ALA A 146 SHEET 4 AB6 4 VAL A 179 LEU A 180 -1 N VAL A 179 O SER A 187 SHEET 1 AB7 2 VAL A 160 TRP A 164 0 SHEET 2 AB7 2 CYS A 206 HIS A 210 -1 O ASN A 209 N THR A 161 SHEET 1 AB8 4 LEU B 2 GLN B 4 0 SHEET 2 AB8 4 VAL B 17 ALA B 23 -1 O ARG B 22 N THR B 3 SHEET 3 AB8 4 GLU B 68 ILE B 73 -1 O PHE B 69 N CYS B 21 SHEET 4 AB8 4 PHE B 60 SER B 65 -1 N SER B 61 O THR B 72 SHEET 1 AB9 6 PHE B 8 SER B 10 0 SHEET 2 AB9 6 THR B 100 GLU B 103 1 O GLU B 103 N LEU B 9 SHEET 3 AB9 6 THR B 83 ARG B 88 -1 N TYR B 84 O THR B 100 SHEET 4 AB9 6 LEU B 31 GLN B 36 -1 N TYR B 34 O TYR B 85 SHEET 5 AB9 6 LYS B 43 TYR B 47 -1 O ILE B 46 N TRP B 33 SHEET 6 AB9 6 THR B 51 LEU B 52 -1 O THR B 51 N TYR B 47 SHEET 1 AC1 4 SER B 112 PHE B 116 0 SHEET 2 AC1 4 THR B 127 PHE B 137 -1 O LEU B 133 N PHE B 114 SHEET 3 AC1 4 TYR B 171 SER B 180 -1 O LEU B 177 N VAL B 130 SHEET 4 AC1 4 SER B 157 VAL B 161 -1 N SER B 160 O SER B 174 SHEET 1 AC2 4 LEU B 152 GLN B 153 0 SHEET 2 AC2 4 LYS B 143 VAL B 148 -1 N TRP B 146 O GLN B 153 SHEET 3 AC2 4 TYR B 190 THR B 195 -1 O ALA B 191 N LYS B 147 SHEET 4 AC2 4 VAL B 203 PHE B 207 -1 O VAL B 203 N VAL B 194 SHEET 1 AC3 2 LYS C 78 ILE C 80 0 SHEET 2 AC3 2 LEU C 86 ASP C 88 -1 O GLY C 87 N LYS C 79 SHEET 1 AC4 2 LYS D 78 ILE D 80 0 SHEET 2 AC4 2 LEU D 86 ASP D 88 -1 O GLY D 87 N LYS D 79 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 150 CYS H 206 1555 1555 2.03 SSBOND 3 CYS L 21 CYS L 86 1555 1555 2.03 SSBOND 4 CYS L 132 CYS L 192 1555 1555 2.04 SSBOND 5 CYS A 22 CYS A 96 1555 1555 2.04 SSBOND 6 CYS A 150 CYS A 206 1555 1555 2.04 SSBOND 7 CYS B 21 CYS B 86 1555 1555 2.04 SSBOND 8 CYS B 132 CYS B 192 1555 1555 2.04 CISPEP 1 PHE H 106 PRO H 107 0 -6.49 CISPEP 2 ASP L -1 ILE L 0 0 4.28 CISPEP 3 TYR L 92 PRO L 93 0 12.40 CISPEP 4 TYR L 138 PRO L 139 0 -10.47 CISPEP 5 ARG L 140 GLU L 141 0 3.07 CISPEP 6 PHE A 106 PRO A 107 0 -6.83 CISPEP 7 PHE A 156 PRO A 157 0 -3.51 CISPEP 8 TYR B 92 PRO B 93 0 -1.44 CRYST1 77.794 96.459 188.671 90.00 90.00 90.00 P 21 21 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 0.012854 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010367 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005300 0.00000