HEADER IMMUNE SYSTEM/ANTIGEN 29-MAY-24 9C1S TITLE FAB F946 IN COMPLEX WITH OSPC TYPE A 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 SYNONYM: PC; 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, BB_B19; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI B; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 37762 KEYWDS FAB-ANTIGEN COMPLEX, IMMUNE SYSTEM, IMMUNE SYSTEM-ANTIGEN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.J.RUDOLPH,N.MANTIS REVDAT 1 27-AUG-25 9C1S 0 JRNL AUTH M.J.RUDOLPH,N.MANTIS JRNL TITL FAB F946 IN COMPLEX WITH OSPC TYPE A JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.60 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.57 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2 REMARK 3 NUMBER OF REFLECTIONS : 42076 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 2083 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 47.5700 - 6.4000 0.99 2949 151 0.1726 0.1974 REMARK 3 2 6.4000 - 5.0800 1.00 2844 147 0.1728 0.2114 REMARK 3 3 5.0800 - 4.4400 1.00 2784 146 0.1438 0.1774 REMARK 3 4 4.4400 - 4.0400 1.00 2825 114 0.1541 0.2350 REMARK 3 5 4.0400 - 3.7500 1.00 2750 163 0.1793 0.2463 REMARK 3 6 3.7500 - 3.5300 1.00 2742 160 0.1978 0.2261 REMARK 3 7 3.5300 - 3.3500 1.00 2721 174 0.2136 0.2650 REMARK 3 8 3.3500 - 3.2000 1.00 2727 155 0.2159 0.2737 REMARK 3 9 3.2000 - 3.0800 1.00 2768 132 0.2283 0.3084 REMARK 3 10 3.0800 - 2.9700 1.00 2749 125 0.2420 0.3428 REMARK 3 11 2.9700 - 2.8800 0.99 2721 136 0.2588 0.3627 REMARK 3 12 2.8800 - 2.8000 0.97 2632 126 0.2585 0.3248 REMARK 3 13 2.8000 - 2.7300 0.95 2614 131 0.2669 0.3321 REMARK 3 14 2.7300 - 2.6600 0.92 2479 130 0.2621 0.3115 REMARK 3 15 2.6600 - 2.6000 0.61 1688 93 0.2516 0.3305 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) : 0.345 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.269 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.04 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 9133 REMARK 3 ANGLE : 0.561 12382 REMARK 3 CHIRALITY : 0.040 1435 REMARK 3 PLANARITY : 0.004 1563 REMARK 3 DIHEDRAL : 5.181 1236 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 28 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.6625 6.4345 22.9382 REMARK 3 T TENSOR REMARK 3 T11: 0.2839 T22: 0.2337 REMARK 3 T33: 0.3217 T12: -0.0278 REMARK 3 T13: 0.0047 T23: 0.0135 REMARK 3 L TENSOR REMARK 3 L11: 2.1989 L22: 3.2060 REMARK 3 L33: 2.4570 L12: 0.2905 REMARK 3 L13: 0.4215 L23: -0.1166 REMARK 3 S TENSOR REMARK 3 S11: -0.0701 S12: -0.1028 S13: -0.2187 REMARK 3 S21: 0.0006 S22: 0.2358 S23: 0.5339 REMARK 3 S31: 0.1483 S32: -0.2635 S33: -0.1050 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 120 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.7253 3.2228 -10.8487 REMARK 3 T TENSOR REMARK 3 T11: 0.4134 T22: 0.3719 REMARK 3 T33: 0.4298 T12: 0.1358 REMARK 3 T13: -0.1457 T23: -0.1359 REMARK 3 L TENSOR REMARK 3 L11: 3.5882 L22: 3.7964 REMARK 3 L33: 5.1971 L12: 1.8679 REMARK 3 L13: -1.1395 L23: -0.1659 REMARK 3 S TENSOR REMARK 3 S11: 0.1642 S12: 0.2752 S13: -0.3662 REMARK 3 S21: -0.3078 S22: 0.1064 S23: -0.2341 REMARK 3 S31: 0.5791 S32: 0.5699 S33: -0.1303 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 0 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.9222 27.1533 16.6916 REMARK 3 T TENSOR REMARK 3 T11: 0.2986 T22: 0.1999 REMARK 3 T33: 0.3438 T12: -0.0152 REMARK 3 T13: -0.0801 T23: 0.0175 REMARK 3 L TENSOR REMARK 3 L11: 2.4432 L22: 3.7495 REMARK 3 L33: 5.0392 L12: -0.4810 REMARK 3 L13: -0.5800 L23: 0.2225 REMARK 3 S TENSOR REMARK 3 S11: -0.2497 S12: 0.0708 S13: 0.1607 REMARK 3 S21: -0.0060 S22: 0.2143 S23: 0.3946 REMARK 3 S31: -0.0926 S32: -0.1954 S33: 0.0067 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 60 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.4040 33.3801 20.0855 REMARK 3 T TENSOR REMARK 3 T11: 0.5404 T22: 0.2171 REMARK 3 T33: 0.4653 T12: 0.0821 REMARK 3 T13: -0.0620 T23: -0.0546 REMARK 3 L TENSOR REMARK 3 L11: 5.3024 L22: 0.8500 REMARK 3 L33: 6.2759 L12: 1.1985 REMARK 3 L13: -4.5717 L23: -0.4259 REMARK 3 S TENSOR REMARK 3 S11: 0.3261 S12: 0.4820 S13: 0.4700 REMARK 3 S21: 0.0412 S22: -0.0962 S23: 0.5898 REMARK 3 S31: -1.4619 S32: -0.4168 S33: -0.2514 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 74 THROUGH 100 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.5080 23.6528 16.2912 REMARK 3 T TENSOR REMARK 3 T11: 0.3496 T22: 0.1997 REMARK 3 T33: 0.3375 T12: 0.0693 REMARK 3 T13: -0.0811 T23: -0.0458 REMARK 3 L TENSOR REMARK 3 L11: 5.5237 L22: 3.9578 REMARK 3 L33: 7.7810 L12: 3.8822 REMARK 3 L13: -3.3079 L23: -3.2195 REMARK 3 S TENSOR REMARK 3 S11: -0.1513 S12: -0.0190 S13: 0.1708 REMARK 3 S21: -0.3440 S22: 0.1733 S23: 0.2075 REMARK 3 S31: 0.3229 S32: -0.1243 S33: 0.0087 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 101 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.4049 29.1791 -5.3226 REMARK 3 T TENSOR REMARK 3 T11: 0.4647 T22: 0.4388 REMARK 3 T33: 0.2406 T12: -0.1756 REMARK 3 T13: -0.0326 T23: 0.0422 REMARK 3 L TENSOR REMARK 3 L11: 1.6195 L22: 2.7239 REMARK 3 L33: 5.3555 L12: -0.3295 REMARK 3 L13: 0.6352 L23: 3.5542 REMARK 3 S TENSOR REMARK 3 S11: -0.0934 S12: 0.4892 S13: 0.2472 REMARK 3 S21: -0.6154 S22: 0.8275 S23: -0.2845 REMARK 3 S31: 0.0040 S32: -0.1951 S33: -0.6074 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 112 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.5982 4.9899 -21.1480 REMARK 3 T TENSOR REMARK 3 T11: 0.4933 T22: 0.5072 REMARK 3 T33: 0.4440 T12: 0.0381 REMARK 3 T13: -0.0329 T23: -0.1550 REMARK 3 L TENSOR REMARK 3 L11: 4.6738 L22: 4.6101 REMARK 3 L33: 3.5907 L12: 1.5879 REMARK 3 L13: 1.5204 L23: 0.0783 REMARK 3 S TENSOR REMARK 3 S11: 0.2506 S12: 0.6173 S13: -0.8345 REMARK 3 S21: -0.2409 S22: 0.3516 S23: -0.4921 REMARK 3 S31: 0.4565 S32: 0.3617 S33: -0.5639 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 127 THROUGH 161 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.2899 17.4823 -14.4909 REMARK 3 T TENSOR REMARK 3 T11: 0.3100 T22: 0.2655 REMARK 3 T33: 0.2554 T12: -0.0194 REMARK 3 T13: 0.0390 T23: -0.0206 REMARK 3 L TENSOR REMARK 3 L11: 3.7354 L22: 2.2369 REMARK 3 L33: 2.3885 L12: 0.7936 REMARK 3 L13: 1.8821 L23: 1.2231 REMARK 3 S TENSOR REMARK 3 S11: 0.0591 S12: 0.2958 S13: -0.1184 REMARK 3 S21: 0.0270 S22: 0.0205 S23: 0.0636 REMARK 3 S31: -0.0919 S32: 0.0892 S33: -0.0421 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 162 THROUGH 172 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.8993 21.5842 -5.7310 REMARK 3 T TENSOR REMARK 3 T11: 0.4399 T22: 0.5114 REMARK 3 T33: 0.5144 T12: -0.0671 REMARK 3 T13: -0.0137 T23: -0.0017 REMARK 3 L TENSOR REMARK 3 L11: 4.6209 L22: 3.9258 REMARK 3 L33: 2.4130 L12: 4.1349 REMARK 3 L13: 2.8890 L23: 2.2607 REMARK 3 S TENSOR REMARK 3 S11: 0.2870 S12: -0.6108 S13: -0.3401 REMARK 3 S21: -0.3972 S22: -0.4402 S23: -0.7143 REMARK 3 S31: -0.0848 S32: 1.2409 S33: 0.0665 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 173 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.8726 14.4055 -22.3040 REMARK 3 T TENSOR REMARK 3 T11: 0.3652 T22: 0.3771 REMARK 3 T33: 0.2604 T12: 0.0835 REMARK 3 T13: -0.0303 T23: -0.0256 REMARK 3 L TENSOR REMARK 3 L11: 5.1330 L22: 7.4052 REMARK 3 L33: 6.6539 L12: 3.9132 REMARK 3 L13: 2.2860 L23: 1.7713 REMARK 3 S TENSOR REMARK 3 S11: -0.1745 S12: 0.5140 S13: 0.0887 REMARK 3 S21: -1.0097 S22: -0.0632 S23: 0.3395 REMARK 3 S31: -0.3079 S32: 0.0956 S33: 0.1939 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.8224 40.4496 65.1947 REMARK 3 T TENSOR REMARK 3 T11: 0.3023 T22: 0.2308 REMARK 3 T33: 0.2798 T12: 0.0151 REMARK 3 T13: -0.0220 T23: 0.0248 REMARK 3 L TENSOR REMARK 3 L11: 1.0425 L22: 1.6358 REMARK 3 L33: 2.1755 L12: -0.0048 REMARK 3 L13: -0.5805 L23: 0.5694 REMARK 3 S TENSOR REMARK 3 S11: -0.0905 S12: 0.1763 S13: 0.0666 REMARK 3 S21: -0.0324 S22: 0.1280 S23: 0.2098 REMARK 3 S31: -0.0035 S32: -0.1888 S33: -0.0754 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 120 THROUGH 225 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.7418 44.0740 97.5524 REMARK 3 T TENSOR REMARK 3 T11: 0.3205 T22: 0.2790 REMARK 3 T33: 0.3346 T12: -0.0187 REMARK 3 T13: 0.0977 T23: 0.0607 REMARK 3 L TENSOR REMARK 3 L11: 4.2117 L22: 2.3354 REMARK 3 L33: 4.6469 L12: -0.5019 REMARK 3 L13: 2.1165 L23: 0.1049 REMARK 3 S TENSOR REMARK 3 S11: 0.1771 S12: -0.2825 S13: 0.3599 REMARK 3 S21: 0.2458 S22: -0.2764 S23: -0.1802 REMARK 3 S31: -0.3894 S32: 0.2767 S33: 0.0893 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 16 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.7880 16.3712 75.3862 REMARK 3 T TENSOR REMARK 3 T11: 0.2644 T22: 0.2232 REMARK 3 T33: 0.3796 T12: -0.0414 REMARK 3 T13: 0.0742 T23: -0.0477 REMARK 3 L TENSOR REMARK 3 L11: 9.3083 L22: 4.3576 REMARK 3 L33: 7.2602 L12: -1.8412 REMARK 3 L13: 5.5644 L23: -2.3815 REMARK 3 S TENSOR REMARK 3 S11: -0.0363 S12: -0.3229 S13: -0.3760 REMARK 3 S21: -0.1750 S22: 0.2148 S23: 0.5367 REMARK 3 S31: 0.7003 S32: -0.3920 S33: -0.0135 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 17 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.7333 19.9952 69.0147 REMARK 3 T TENSOR REMARK 3 T11: 0.3127 T22: 0.1839 REMARK 3 T33: 0.2676 T12: 0.0294 REMARK 3 T13: 0.0497 T23: -0.0041 REMARK 3 L TENSOR REMARK 3 L11: 3.2757 L22: 3.3788 REMARK 3 L33: 3.3613 L12: 0.2486 REMARK 3 L13: 0.5563 L23: -1.1805 REMARK 3 S TENSOR REMARK 3 S11: -0.0121 S12: -0.1157 S13: -0.4516 REMARK 3 S21: 0.1327 S22: 0.0010 S23: -0.0490 REMARK 3 S31: 0.1774 S32: -0.1045 S33: 0.0099 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 68 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.3410 21.4660 71.1487 REMARK 3 T TENSOR REMARK 3 T11: 0.3619 T22: 0.2712 REMARK 3 T33: 0.3532 T12: -0.0225 REMARK 3 T13: 0.0607 T23: -0.0202 REMARK 3 L TENSOR REMARK 3 L11: 0.9660 L22: 4.2243 REMARK 3 L33: 5.9290 L12: -0.7687 REMARK 3 L13: 0.6554 L23: -3.1531 REMARK 3 S TENSOR REMARK 3 S11: -0.1364 S12: -0.0552 S13: 0.0108 REMARK 3 S21: -0.0969 S22: 0.0583 S23: 0.2190 REMARK 3 S31: 0.3065 S32: 0.0733 S33: 0.0207 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 100 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.0012 18.1317 91.7253 REMARK 3 T TENSOR REMARK 3 T11: 0.5326 T22: 0.3170 REMARK 3 T33: 0.2921 T12: 0.0556 REMARK 3 T13: 0.1059 T23: 0.1050 REMARK 3 L TENSOR REMARK 3 L11: 0.1997 L22: 0.9824 REMARK 3 L33: 3.2856 L12: -0.3084 REMARK 3 L13: -0.5567 L23: 1.7955 REMARK 3 S TENSOR REMARK 3 S11: -0.3849 S12: -0.3389 S13: 0.0669 REMARK 3 S21: 0.3487 S22: 0.4568 S23: 0.3221 REMARK 3 S31: 0.7380 S32: -0.3227 S33: 0.0361 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 112 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.4196 43.3924 107.8304 REMARK 3 T TENSOR REMARK 3 T11: 0.4046 T22: 0.3272 REMARK 3 T33: 0.4205 T12: -0.0812 REMARK 3 T13: 0.0497 T23: 0.0546 REMARK 3 L TENSOR REMARK 3 L11: 5.6389 L22: 2.8814 REMARK 3 L33: 4.1637 L12: -2.9404 REMARK 3 L13: -1.2408 L23: 0.0936 REMARK 3 S TENSOR REMARK 3 S11: 0.1808 S12: -0.0199 S13: 0.9842 REMARK 3 S21: 0.0109 S22: 0.0534 S23: -0.3612 REMARK 3 S31: -0.3548 S32: -0.1593 S33: -0.1936 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 127 THROUGH 161 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.0831 30.4990 103.0420 REMARK 3 T TENSOR REMARK 3 T11: 0.2589 T22: 0.2147 REMARK 3 T33: 0.2967 T12: -0.0486 REMARK 3 T13: -0.0063 T23: 0.0265 REMARK 3 L TENSOR REMARK 3 L11: 4.6143 L22: 2.9990 REMARK 3 L33: 3.4263 L12: -3.0822 REMARK 3 L13: -2.0897 L23: 1.1205 REMARK 3 S TENSOR REMARK 3 S11: -0.0693 S12: -0.1028 S13: -0.2039 REMARK 3 S21: 0.1303 S22: -0.0637 S23: 0.1743 REMARK 3 S31: 0.3613 S32: -0.0126 S33: 0.1894 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 162 THROUGH 210 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.3832 31.8363 106.0296 REMARK 3 T TENSOR REMARK 3 T11: 0.3308 T22: 0.2318 REMARK 3 T33: 0.2017 T12: -0.0020 REMARK 3 T13: -0.0015 T23: 0.0573 REMARK 3 L TENSOR REMARK 3 L11: 3.4549 L22: 2.5205 REMARK 3 L33: 3.6141 L12: -1.2054 REMARK 3 L13: -2.3812 L23: 1.4759 REMARK 3 S TENSOR REMARK 3 S11: 0.0660 S12: -0.0612 S13: -0.1985 REMARK 3 S21: 0.0736 S22: -0.2398 S23: 0.0798 REMARK 3 S31: -0.0343 S32: 0.0689 S33: 0.0738 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 41 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.2675 24.1377 48.8445 REMARK 3 T TENSOR REMARK 3 T11: 0.4427 T22: 0.8626 REMARK 3 T33: 0.3384 T12: -0.0050 REMARK 3 T13: -0.0141 T23: -0.1805 REMARK 3 L TENSOR REMARK 3 L11: 2.4018 L22: 2.5799 REMARK 3 L33: 1.4129 L12: 0.8089 REMARK 3 L13: 0.0179 L23: 0.3188 REMARK 3 S TENSOR REMARK 3 S11: 0.3989 S12: -0.9369 S13: 0.2564 REMARK 3 S21: 0.1734 S22: 0.0684 S23: -0.5814 REMARK 3 S31: 0.1950 S32: 0.6130 S33: -0.3099 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 87 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.4216 34.8092 47.3238 REMARK 3 T TENSOR REMARK 3 T11: 0.5819 T22: 0.9682 REMARK 3 T33: 0.7025 T12: -0.2469 REMARK 3 T13: 0.1728 T23: -0.1805 REMARK 3 L TENSOR REMARK 3 L11: 4.7636 L22: 4.3026 REMARK 3 L33: 2.5851 L12: -0.7460 REMARK 3 L13: 0.4843 L23: 0.4254 REMARK 3 S TENSOR REMARK 3 S11: 0.2253 S12: -0.4930 S13: 0.5055 REMARK 3 S21: 0.1822 S22: 0.0918 S23: -1.0011 REMARK 3 S31: -0.6405 S32: 1.0385 S33: -0.2075 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 141 THROUGH 170 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.0519 34.5474 57.6911 REMARK 3 T TENSOR REMARK 3 T11: 0.6073 T22: 1.8777 REMARK 3 T33: 1.2954 T12: -0.3215 REMARK 3 T13: 0.0847 T23: -0.5822 REMARK 3 L TENSOR REMARK 3 L11: 1.3173 L22: 0.2882 REMARK 3 L33: 2.8743 L12: 0.1002 REMARK 3 L13: -1.8949 L23: 0.0635 REMARK 3 S TENSOR REMARK 3 S11: 0.5924 S12: -0.1998 S13: -0.0460 REMARK 3 S21: 0.0142 S22: 0.1301 S23: -1.3015 REMARK 3 S31: -0.2376 S32: 0.7248 S33: -0.1325 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 171 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.5725 33.4373 52.1273 REMARK 3 T TENSOR REMARK 3 T11: 0.4940 T22: 0.3602 REMARK 3 T33: 0.3177 T12: -0.0365 REMARK 3 T13: 0.0594 T23: -0.1436 REMARK 3 L TENSOR REMARK 3 L11: 8.0314 L22: 5.3742 REMARK 3 L33: 5.0707 L12: 2.2886 REMARK 3 L13: 1.9614 L23: 1.2181 REMARK 3 S TENSOR REMARK 3 S11: 0.0315 S12: 0.3671 S13: 1.0173 REMARK 3 S21: -0.1138 S22: 0.2916 S23: -0.4383 REMARK 3 S31: -0.5439 S32: 0.6171 S33: -0.4280 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 40 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.2305 19.7655 45.8100 REMARK 3 T TENSOR REMARK 3 T11: 0.5698 T22: 0.5277 REMARK 3 T33: 0.2588 T12: 0.1169 REMARK 3 T13: -0.0476 T23: -0.0768 REMARK 3 L TENSOR REMARK 3 L11: 5.2637 L22: 2.3666 REMARK 3 L33: 2.6898 L12: -0.0408 REMARK 3 L13: -0.8208 L23: -0.0324 REMARK 3 S TENSOR REMARK 3 S11: 0.2097 S12: 0.1892 S13: -0.8131 REMARK 3 S21: 0.0256 S22: -0.1521 S23: -0.1191 REMARK 3 S31: 0.3737 S32: 0.6045 S33: -0.1474 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 76 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.9779 15.5157 47.5497 REMARK 3 T TENSOR REMARK 3 T11: 0.7321 T22: 1.3244 REMARK 3 T33: 0.6065 T12: 0.1666 REMARK 3 T13: -0.1966 T23: -0.0941 REMARK 3 L TENSOR REMARK 3 L11: 4.1020 L22: 4.6111 REMARK 3 L33: 3.2048 L12: 0.4875 REMARK 3 L13: -0.6938 L23: 0.2884 REMARK 3 S TENSOR REMARK 3 S11: 0.2789 S12: -0.4098 S13: -0.7163 REMARK 3 S21: 0.3703 S22: -0.2635 S23: -1.2217 REMARK 3 S31: 0.7347 S32: 1.6853 S33: -0.0408 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 141 THROUGH 158 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.6574 14.0459 44.9318 REMARK 3 T TENSOR REMARK 3 T11: 0.3942 T22: 2.0474 REMARK 3 T33: 1.1117 T12: 0.5042 REMARK 3 T13: 0.0086 T23: -0.1863 REMARK 3 L TENSOR REMARK 3 L11: 2.1426 L22: 0.3306 REMARK 3 L33: 0.0862 L12: 0.2457 REMARK 3 L13: 0.0057 L23: -0.1439 REMARK 3 S TENSOR REMARK 3 S11: -0.0920 S12: -0.2349 S13: 0.1306 REMARK 3 S21: 0.0888 S22: -0.0261 S23: -0.4807 REMARK 3 S31: 0.0560 S32: 0.0487 S33: 0.0275 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 159 THROUGH 169 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.0471 12.7523 36.4644 REMARK 3 T TENSOR REMARK 3 T11: 0.4829 T22: 1.7858 REMARK 3 T33: 1.0995 T12: 0.1950 REMARK 3 T13: -0.2191 T23: -0.3030 REMARK 3 L TENSOR REMARK 3 L11: 3.3791 L22: 3.4266 REMARK 3 L33: 2.5129 L12: 2.0133 REMARK 3 L13: -2.1391 L23: 0.3328 REMARK 3 S TENSOR REMARK 3 S11: 0.3418 S12: -0.4859 S13: -0.8952 REMARK 3 S21: 0.2604 S22: -0.2148 S23: -1.3381 REMARK 3 S31: 0.2713 S32: 0.6286 S33: -0.2809 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 170 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.7217 13.6513 39.2352 REMARK 3 T TENSOR REMARK 3 T11: 0.6078 T22: 0.3881 REMARK 3 T33: 0.2906 T12: 0.1425 REMARK 3 T13: 0.0743 T23: -0.0789 REMARK 3 L TENSOR REMARK 3 L11: 5.0755 L22: 2.4400 REMARK 3 L33: 3.8915 L12: -1.4634 REMARK 3 L13: 1.0289 L23: 0.3158 REMARK 3 S TENSOR REMARK 3 S11: 0.6307 S12: -0.3029 S13: -0.1478 REMARK 3 S21: -0.1066 S22: -0.1698 S23: -0.3279 REMARK 3 S31: 0.7819 S32: 0.4571 S33: -0.3625 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 9C1S 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_1000284550. 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 : 42767 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550 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 (%) : 99.9 REMARK 200 DATA REDUNDANCY : 11.50 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1 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 (%): 53.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM AMMONIUM NITRATE AND 20% 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 39.90750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.48400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.57050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.48400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.90750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.57050 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: 14810 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 50440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 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 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 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 ASP L -1 REMARK 465 SER A 140 REMARK 465 THR A 141 REMARK 465 SER A 142 REMARK 465 GLY A 143 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 GLU B 211 REMARK 465 CYS B 212 REMARK 465 LYS C 38 REMARK 465 GLY C 39 REMARK 465 PRO C 40 REMARK 465 GLY C 146 REMARK 465 LYS C 147 REMARK 465 GLY C 169 REMARK 465 LYS D 38 REMARK 465 GLY D 39 REMARK 465 LYS D 80 REMARK 465 LEU D 87 REMARK 465 ASP D 88 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 33 151.71 68.91 REMARK 500 LEU H 102 -138.77 57.55 REMARK 500 SER L 28 -122.35 66.95 REMARK 500 ALA L 49 -5.75 73.16 REMARK 500 ASN A 33 153.12 69.60 REMARK 500 LEU A 102 -129.27 57.92 REMARK 500 SER B 28 -131.29 59.62 REMARK 500 ALA B 48 28.42 47.92 REMARK 500 ALA B 49 -5.69 73.04 REMARK 500 ASN D 85 -3.23 73.80 REMARK 500 REMARK 500 REMARK: NULL DBREF 9C1S H 1 230 PDB 9C1S 9C1S 1 230 DBREF 9C1S L -1 212 PDB 9C1S 9C1S -1 212 DBREF 9C1S A 1 230 PDB 9C1S 9C1S 1 230 DBREF 9C1S B -1 212 PDB 9C1S 9C1S -1 212 DBREF 9C1S C 38 201 UNP Q07337 OSPC_BORBU 38 201 DBREF 9C1S D 38 201 UNP Q07337 OSPC_BORBU 38 201 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 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 C 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 C 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 C 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 C 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 C 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 C 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 C 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 C 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 C 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 C 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 C 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 C 164 SER VAL LYS GLU LEU THR SER PRO SEQRES 1 D 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 D 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 D 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 D 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 D 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 D 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 D 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 D 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 D 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 D 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 D 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 D 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 D 164 SER VAL LYS GLU LEU THR SER PRO FORMUL 7 HOH *233(H2 O) HELIX 1 AA1 THR H 87 THR H 91 5 5 HELIX 2 AA2 SER H 166 ALA H 168 5 3 HELIX 3 AA3 SER H 197 LEU H 199 5 3 HELIX 4 AA4 LYS H 211 ASN H 214 5 4 HELIX 5 AA5 GLN L 77 PHE L 81 5 5 HELIX 6 AA6 SER L 119 SER L 125 1 7 HELIX 7 AA7 LYS L 181 LYS L 186 1 6 HELIX 8 AA8 THR A 87 THR A 91 5 5 HELIX 9 AA9 SER A 166 ALA A 168 5 3 HELIX 10 AB1 SER A 197 LEU A 199 5 3 HELIX 11 AB2 LYS A 211 ASN A 214 5 4 HELIX 12 AB3 GLN B 77 PHE B 81 5 5 HELIX 13 AB4 SER B 119 LYS B 124 1 6 HELIX 14 AB5 LYS B 181 GLU B 185 1 5 HELIX 15 AB6 LEU C 42 ALA C 76 1 35 HELIX 16 AB7 ASN C 94 LEU C 115 1 22 HELIX 17 AB8 LEU C 120 LYS C 141 1 22 HELIX 18 AB9 THR C 151 LEU C 160 1 10 HELIX 19 AC1 GLU C 171 THR C 199 1 29 HELIX 20 AC2 ASN D 41 ALA D 76 1 36 HELIX 21 AC3 ASN D 94 GLY D 114 1 21 HELIX 22 AC4 LEU D 120 LYS D 141 1 22 HELIX 23 AC5 HIS D 142 LEU D 145 5 4 HELIX 24 AC6 THR D 151 ILE D 159 1 9 HELIX 25 AC7 GLY D 169 GLU D 197 1 29 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 PHE H 52 -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 THR H 145 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA4 4 TYR H 186 PRO H 195 -1 O TYR H 186 N TYR H 155 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 THR H 145 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA5 4 TYR H 186 PRO H 195 -1 O TYR H 186 N TYR H 155 SHEET 4 AA5 4 VAL H 179 LEU H 180 -1 N VAL H 179 O SER H 187 SHEET 1 AA6 3 THR H 161 TRP H 164 0 SHEET 2 AA6 3 ILE H 205 HIS H 210 -1 O ASN H 207 N SER H 163 SHEET 3 AA6 3 THR H 215 ARG H 220 -1 O THR H 215 N HIS H 210 SHEET 1 AA7 4 LEU L 2 SER L 5 0 SHEET 2 AA7 4 VAL L 17 ALA L 23 -1 O THR L 20 N SER L 5 SHEET 3 AA7 4 GLU L 68 ILE L 73 -1 O LEU L 71 N ILE L 19 SHEET 4 AA7 4 PHE L 60 SER L 63 -1 N SER L 61 O THR L 72 SHEET 1 AA8 6 PHE L 8 ALA L 11 0 SHEET 2 AA8 6 THR L 100 ILE L 104 1 O GLU L 103 N LEU L 9 SHEET 3 AA8 6 THR L 83 ARG L 88 -1 N TYR L 84 O THR L 100 SHEET 4 AA8 6 LEU L 31 GLN L 36 -1 N TYR L 34 O TYR L 85 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 PHE L 137 -1 O LEU L 133 N PHE L 114 SHEET 3 AA9 4 TYR L 171 SER L 180 -1 O LEU L 173 N LEU L 134 SHEET 4 AA9 4 SER L 157 VAL L 161 -1 N SER L 160 O SER L 174 SHEET 1 AB1 4 ALA L 151 LEU L 152 0 SHEET 2 AB1 4 LYS L 143 VAL L 148 -1 N VAL L 148 O ALA L 151 SHEET 3 AB1 4 VAL L 189 THR L 195 -1 O GLU L 193 N GLN L 145 SHEET 4 AB1 4 VAL L 203 ASN L 208 -1 O VAL L 203 N VAL L 194 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 SER A 71 O SER A 80 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 THR A 145 TYR A 155 -1 O LEU A 151 N PHE A 132 SHEET 3 AB5 4 TYR A 186 PRO A 195 -1 O LEU A 188 N VAL A 152 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 THR A 145 TYR A 155 -1 O LEU A 151 N PHE A 132 SHEET 3 AB6 4 TYR A 186 PRO A 195 -1 O LEU A 188 N VAL A 152 SHEET 4 AB6 4 VAL A 179 LEU A 180 -1 N VAL A 179 O SER A 187 SHEET 1 AB7 3 THR A 161 TRP A 164 0 SHEET 2 AB7 3 ILE A 205 HIS A 210 -1 O ASN A 207 N SER A 163 SHEET 3 AB7 3 THR A 215 ARG A 220 -1 O VAL A 217 N VAL A 208 SHEET 1 AB8 4 LEU B 2 SER B 5 0 SHEET 2 AB8 4 VAL B 17 ALA B 23 -1 O THR B 20 N SER B 5 SHEET 3 AB8 4 GLU B 68 ILE B 73 -1 O LEU B 71 N ILE B 19 SHEET 4 AB8 4 PHE B 60 SER B 63 -1 N SER B 61 O THR B 72 SHEET 1 AB9 6 PHE B 8 ALA B 11 0 SHEET 2 AB9 6 THR B 100 ILE B 104 1 O GLU B 103 N LEU B 9 SHEET 3 AB9 6 ALA B 82 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 LEU B 45 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 179 N ALA B 128 SHEET 4 AC1 4 SER B 157 VAL B 161 -1 N GLN B 158 O THR B 176 SHEET 1 AC2 4 ALA B 151 LEU B 152 0 SHEET 2 AC2 4 LYS B 143 VAL B 148 -1 N VAL B 148 O ALA B 151 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 LYS B 205 N CYS B 192 SHEET 1 AC3 2 LYS C 79 ILE C 81 0 SHEET 2 AC3 2 LEU C 87 THR C 89 -1 O ASP C 88 N LYS C 80 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 2.04 SSBOND 4 CYS L 132 CYS L 192 1555 1555 2.04 SSBOND 5 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 6 CYS A 150 CYS A 206 1555 1555 2.03 SSBOND 7 CYS B 21 CYS B 86 1555 1555 2.03 SSBOND 8 CYS B 132 CYS B 192 1555 1555 2.03 CISPEP 1 PHE H 106 PRO H 107 0 -6.19 CISPEP 2 PHE H 156 PRO H 157 0 -5.59 CISPEP 3 GLU H 158 PRO H 159 0 -0.49 CISPEP 4 SER L 5 PRO L 6 0 -3.54 CISPEP 5 TYR L 92 PRO L 93 0 13.05 CISPEP 6 TYR L 138 PRO L 139 0 3.63 CISPEP 7 PHE A 106 PRO A 107 0 -8.38 CISPEP 8 PHE A 156 PRO A 157 0 -3.41 CISPEP 9 GLU A 158 PRO A 159 0 -4.07 CISPEP 10 SER B 5 PRO B 6 0 -3.17 CISPEP 11 TYR B 92 PRO B 93 0 14.32 CISPEP 12 TYR B 138 PRO B 139 0 3.23 CRYST1 79.815 95.141 182.968 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 0.012529 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010511 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005465 0.00000