HEADER IMMUNE SYSTEM/ANTIGEN 23-MAY-24 9BYF TITLE FAB 212-55 IN COMPLEX WITH OSPA COMPND MOL_ID: 1; COMPND 2 MOLECULE: 221-55 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 221-55 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: OUTER SURFACE PROTEIN A; COMPND 11 CHAIN: A; COMPND 12 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: OSPA, BB_A15; 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 9BYF 0 JRNL AUTH M.J.RUDOLPH,N.MANTIS JRNL TITL FAB 212-55 IN COMPLEX WITH OSPA JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.85 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) : 2.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.73 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 24562 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.233 REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.288 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150 REMARK 3 FREE R VALUE TEST SET COUNT : 1264 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 47.7300 - 5.9200 0.99 2739 128 0.2312 0.2885 REMARK 3 2 5.9200 - 4.7000 0.99 2649 137 0.2034 0.2665 REMARK 3 3 4.7000 - 4.1100 1.00 2581 166 0.1786 0.2332 REMARK 3 4 4.1100 - 3.7300 1.00 2611 134 0.2111 0.2627 REMARK 3 5 3.7300 - 3.4600 1.00 2606 125 0.2307 0.2757 REMARK 3 6 3.4600 - 3.2600 0.99 2570 142 0.2687 0.3549 REMARK 3 7 3.2600 - 3.1000 0.99 2553 142 0.2778 0.3313 REMARK 3 8 3.1000 - 2.9600 1.00 2581 147 0.2905 0.3626 REMARK 3 9 2.9600 - 2.8500 0.94 2408 143 0.3031 0.3222 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.386 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 50.82 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.43 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 4781 REMARK 3 ANGLE : 0.446 6480 REMARK 3 CHIRALITY : 0.041 749 REMARK 3 PLANARITY : 0.004 828 REMARK 3 DIHEDRAL : 4.179 661 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 152 THROUGH 175 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.2934 -13.8660 45.3138 REMARK 3 T TENSOR REMARK 3 T11: 0.2124 T22: 0.1361 REMARK 3 T33: 0.8367 T12: -0.0423 REMARK 3 T13: 0.0550 T23: 0.1241 REMARK 3 L TENSOR REMARK 3 L11: 3.2432 L22: 4.1148 REMARK 3 L33: 5.7962 L12: 1.9094 REMARK 3 L13: 2.8286 L23: 2.7682 REMARK 3 S TENSOR REMARK 3 S11: -0.1174 S12: 0.1116 S13: 0.3503 REMARK 3 S21: -0.1496 S22: -0.1656 S23: 0.6359 REMARK 3 S31: -0.0013 S32: -0.2878 S33: 0.3541 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 176 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.7453 -13.1042 32.0471 REMARK 3 T TENSOR REMARK 3 T11: 0.3903 T22: 0.2919 REMARK 3 T33: 0.7846 T12: -0.3607 REMARK 3 T13: 0.0372 T23: -0.1006 REMARK 3 L TENSOR REMARK 3 L11: 1.3473 L22: 3.5498 REMARK 3 L33: 0.9931 L12: 1.2362 REMARK 3 L13: -0.2469 L23: 1.0364 REMARK 3 S TENSOR REMARK 3 S11: -0.4201 S12: 0.4131 S13: -0.1214 REMARK 3 S21: -0.8260 S22: 0.2144 S23: 0.0511 REMARK 3 S31: -0.4884 S32: 0.1048 S33: 0.0612 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 108 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.3480 -6.8075 113.9239 REMARK 3 T TENSOR REMARK 3 T11: 1.5442 T22: 1.9354 REMARK 3 T33: 0.7781 T12: -0.6892 REMARK 3 T13: 0.2729 T23: -0.0484 REMARK 3 L TENSOR REMARK 3 L11: 3.3137 L22: 3.4072 REMARK 3 L33: 3.9489 L12: -0.1929 REMARK 3 L13: 1.9150 L23: 1.7985 REMARK 3 S TENSOR REMARK 3 S11: -0.2102 S12: -0.1194 S13: 0.4667 REMARK 3 S21: 1.4651 S22: 0.3186 S23: 1.2322 REMARK 3 S31: 0.1608 S32: 0.6622 S33: -0.2208 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 109 THROUGH 203 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.5336 -7.2677 97.6091 REMARK 3 T TENSOR REMARK 3 T11: 0.3971 T22: 0.8570 REMARK 3 T33: 0.9197 T12: -0.1495 REMARK 3 T13: 0.1085 T23: -0.2375 REMARK 3 L TENSOR REMARK 3 L11: 3.8416 L22: 2.6659 REMARK 3 L33: 4.9737 L12: 1.1125 REMARK 3 L13: 2.4413 L23: 0.9763 REMARK 3 S TENSOR REMARK 3 S11: 0.2176 S12: -1.0800 S13: 0.2398 REMARK 3 S21: 0.3743 S22: -0.3486 S23: -0.1558 REMARK 3 S31: -0.1781 S32: -0.0545 S33: 0.2641 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 273 ) REMARK 3 ORIGIN FOR THE GROUP (A): -54.3012 -19.1393 87.9937 REMARK 3 T TENSOR REMARK 3 T11: 0.1678 T22: 0.7470 REMARK 3 T33: 0.8410 T12: -0.0543 REMARK 3 T13: 0.0956 T23: -0.1890 REMARK 3 L TENSOR REMARK 3 L11: 4.1942 L22: 0.9012 REMARK 3 L33: 1.9829 L12: 1.5870 REMARK 3 L13: -1.8905 L23: -0.5298 REMARK 3 S TENSOR REMARK 3 S11: 0.1528 S12: -0.2202 S13: -0.2369 REMARK 3 S21: 0.2512 S22: -0.1168 S23: 0.6632 REMARK 3 S31: -0.0285 S32: -0.3127 S33: -0.0935 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.4506 -34.6900 63.3645 REMARK 3 T TENSOR REMARK 3 T11: 0.2331 T22: 0.3257 REMARK 3 T33: 0.9164 T12: -0.0280 REMARK 3 T13: 0.2038 T23: -0.0365 REMARK 3 L TENSOR REMARK 3 L11: 2.4465 L22: 2.5838 REMARK 3 L33: 5.6022 L12: -0.6475 REMARK 3 L13: 1.9590 L23: -0.9671 REMARK 3 S TENSOR REMARK 3 S11: 0.2906 S12: -0.0097 S13: -0.4288 REMARK 3 S21: 0.0207 S22: -0.1668 S23: 0.1803 REMARK 3 S31: 0.2708 S32: 0.4924 S33: -0.1763 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.1850 -28.4039 72.9870 REMARK 3 T TENSOR REMARK 3 T11: 0.1023 T22: 0.3817 REMARK 3 T33: 0.8224 T12: -0.0624 REMARK 3 T13: 0.1846 T23: 0.1589 REMARK 3 L TENSOR REMARK 3 L11: 2.1122 L22: 0.2700 REMARK 3 L33: 1.3368 L12: 0.6073 REMARK 3 L13: -0.2833 L23: 0.0852 REMARK 3 S TENSOR REMARK 3 S11: -0.1410 S12: -0.4132 S13: -0.3852 REMARK 3 S21: 0.0919 S22: -0.0299 S23: 0.2556 REMARK 3 S31: 0.2512 S32: -0.0525 S33: 0.2654 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 61 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.9067 -32.4036 69.5136 REMARK 3 T TENSOR REMARK 3 T11: 0.3242 T22: 0.2934 REMARK 3 T33: 0.8404 T12: -0.0233 REMARK 3 T13: 0.2125 T23: 0.0103 REMARK 3 L TENSOR REMARK 3 L11: 2.5132 L22: 2.5818 REMARK 3 L33: 7.0110 L12: 1.4005 REMARK 3 L13: 1.8087 L23: -0.2499 REMARK 3 S TENSOR REMARK 3 S11: -0.0882 S12: 0.0905 S13: -0.4798 REMARK 3 S21: 0.2752 S22: -0.1105 S23: 0.2508 REMARK 3 S31: 0.8585 S32: -0.2930 S33: 0.0594 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.4711 -25.8557 70.2746 REMARK 3 T TENSOR REMARK 3 T11: 0.3111 T22: 0.2818 REMARK 3 T33: 1.0711 T12: 0.0003 REMARK 3 T13: 0.1063 T23: 0.0466 REMARK 3 L TENSOR REMARK 3 L11: 1.7405 L22: 0.9093 REMARK 3 L33: 2.4318 L12: 0.5200 REMARK 3 L13: 0.9663 L23: 1.4898 REMARK 3 S TENSOR REMARK 3 S11: 0.1716 S12: -0.3811 S13: -0.3496 REMARK 3 S21: 0.2670 S22: 0.0437 S23: -0.2383 REMARK 3 S31: 0.3022 S32: 0.0258 S33: -0.2505 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 119 THROUGH 143 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.6118 -30.9856 41.3674 REMARK 3 T TENSOR REMARK 3 T11: 0.1918 T22: 0.2348 REMARK 3 T33: 0.7763 T12: -0.0828 REMARK 3 T13: 0.1318 T23: -0.1531 REMARK 3 L TENSOR REMARK 3 L11: 0.3960 L22: 1.4817 REMARK 3 L33: 1.1371 L12: 0.7599 REMARK 3 L13: -0.0668 L23: -0.2935 REMARK 3 S TENSOR REMARK 3 S11: 0.0380 S12: 0.0677 S13: -0.5399 REMARK 3 S21: -0.2816 S22: 0.0017 S23: -0.6220 REMARK 3 S31: -0.1520 S32: 0.3015 S33: -0.0154 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 144 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.1887 -27.1002 45.4031 REMARK 3 T TENSOR REMARK 3 T11: 0.1500 T22: 0.2757 REMARK 3 T33: 1.1691 T12: -0.1039 REMARK 3 T13: 0.0004 T23: -0.0349 REMARK 3 L TENSOR REMARK 3 L11: 1.5105 L22: 0.7737 REMARK 3 L33: 0.6708 L12: 0.9022 REMARK 3 L13: 0.3174 L23: 0.2093 REMARK 3 S TENSOR REMARK 3 S11: -0.1099 S12: 0.1712 S13: -0.0562 REMARK 3 S21: 0.0397 S22: -0.0575 S23: -0.4867 REMARK 3 S31: -0.0385 S32: 0.0951 S33: 0.1029 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 198 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.0601 -33.3853 43.3799 REMARK 3 T TENSOR REMARK 3 T11: 0.2432 T22: 0.3343 REMARK 3 T33: 1.1829 T12: 0.0560 REMARK 3 T13: 0.1123 T23: 0.0045 REMARK 3 L TENSOR REMARK 3 L11: 5.2872 L22: 0.2287 REMARK 3 L33: 0.1827 L12: 0.8413 REMARK 3 L13: -0.4615 L23: -0.1914 REMARK 3 S TENSOR REMARK 3 S11: 0.0960 S12: -0.0733 S13: 0.2400 REMARK 3 S21: -0.3898 S22: -0.1602 S23: -0.5635 REMARK 3 S31: -0.0298 S32: 0.2432 S33: 0.0450 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 210 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.5773 -36.3847 41.0067 REMARK 3 T TENSOR REMARK 3 T11: 0.2515 T22: 0.3475 REMARK 3 T33: 0.6034 T12: -0.1943 REMARK 3 T13: 0.0640 T23: -0.1323 REMARK 3 L TENSOR REMARK 3 L11: 3.6532 L22: 3.8341 REMARK 3 L33: 2.5226 L12: -1.1115 REMARK 3 L13: 1.0839 L23: 0.2594 REMARK 3 S TENSOR REMARK 3 S11: 0.1122 S12: 0.5335 S13: -0.1203 REMARK 3 S21: -0.2646 S22: 0.1587 S23: -0.5957 REMARK 3 S31: 0.0415 S32: 0.3756 S33: -0.0552 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.5285 -6.0318 67.4441 REMARK 3 T TENSOR REMARK 3 T11: -0.0059 T22: 0.2172 REMARK 3 T33: 0.6746 T12: 0.0231 REMARK 3 T13: 0.0431 T23: 0.0924 REMARK 3 L TENSOR REMARK 3 L11: 0.4981 L22: 0.1194 REMARK 3 L33: 2.2026 L12: -0.2178 REMARK 3 L13: -1.0153 L23: 0.3860 REMARK 3 S TENSOR REMARK 3 S11: 0.0655 S12: -0.3876 S13: 0.1747 REMARK 3 S21: -0.0468 S22: 0.0235 S23: -0.0221 REMARK 3 S31: -0.2339 S32: 0.1503 S33: 0.1759 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.0444 -8.9092 74.3876 REMARK 3 T TENSOR REMARK 3 T11: 0.1501 T22: 0.2871 REMARK 3 T33: 0.9090 T12: 0.0377 REMARK 3 T13: 0.1072 T23: -0.0614 REMARK 3 L TENSOR REMARK 3 L11: 2.7378 L22: 0.7936 REMARK 3 L33: 2.0126 L12: -1.4357 REMARK 3 L13: -1.6404 L23: 1.0687 REMARK 3 S TENSOR REMARK 3 S11: 0.2670 S12: 0.1511 S13: 0.9588 REMARK 3 S21: -0.0052 S22: -0.0950 S23: 0.0778 REMARK 3 S31: -0.3605 S32: -0.0523 S33: -0.2084 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 40 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.4324 -12.9205 77.2958 REMARK 3 T TENSOR REMARK 3 T11: 0.0956 T22: 0.4653 REMARK 3 T33: 0.8903 T12: -0.0296 REMARK 3 T13: -0.0101 T23: -0.0819 REMARK 3 L TENSOR REMARK 3 L11: 1.9442 L22: 0.8193 REMARK 3 L33: 1.6156 L12: 0.5161 REMARK 3 L13: -0.9537 L23: -0.2593 REMARK 3 S TENSOR REMARK 3 S11: 0.1703 S12: -0.3825 S13: 0.1818 REMARK 3 S21: 0.1705 S22: -0.2451 S23: -0.0961 REMARK 3 S31: -0.1219 S32: -0.0541 S33: 0.1582 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 77 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.1050 -11.7888 67.4291 REMARK 3 T TENSOR REMARK 3 T11: 0.1865 T22: 0.2043 REMARK 3 T33: 0.9815 T12: 0.0324 REMARK 3 T13: -0.0777 T23: -0.0003 REMARK 3 L TENSOR REMARK 3 L11: 0.4387 L22: 1.0437 REMARK 3 L33: 0.4082 L12: 0.0232 REMARK 3 L13: -0.2474 L23: 0.2187 REMARK 3 S TENSOR REMARK 3 S11: -0.0793 S12: -0.0386 S13: -0.3809 REMARK 3 S21: 0.2428 S22: -0.0480 S23: 0.0428 REMARK 3 S31: 0.0708 S32: 0.0393 S33: -0.0003 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 115 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.3397 -16.9633 37.9570 REMARK 3 T TENSOR REMARK 3 T11: 0.1900 T22: 0.4137 REMARK 3 T33: 0.9045 T12: -0.0965 REMARK 3 T13: 0.0242 T23: -0.0564 REMARK 3 L TENSOR REMARK 3 L11: 2.4457 L22: 3.8886 REMARK 3 L33: 1.8575 L12: 2.8361 REMARK 3 L13: 0.8554 L23: 0.0155 REMARK 3 S TENSOR REMARK 3 S11: -0.3113 S12: 0.2480 S13: 0.0986 REMARK 3 S21: -0.6631 S22: 0.4658 S23: -0.0521 REMARK 3 S31: 0.0805 S32: -0.2079 S33: 0.0157 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 9BYF 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_1000284368. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-MAR-20 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 : 24587 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850 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 (%) : 99.6 REMARK 200 DATA REDUNDANCY : 9.900 REMARK 200 R MERGE (I) : 0.35300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 2.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 10.10 REMARK 200 R MERGE FOR SHELL (I) : 1.91100 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 (%): 64.28 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.5, 23% PEG 3350, AND REMARK 280 200 MM NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2 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,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y+1/2,-Z REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 50.56000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 81.20800 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 50.56000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 81.20800 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 50.56000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 81.20800 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 50.56000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 81.20800 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6100 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28760 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A 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 443 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 451 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 404 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 SER H 136 REMARK 465 SER H 137 REMARK 465 LYS H 138 REMARK 465 SER H 139 REMARK 465 THR H 140 REMARK 465 SER H 141 REMARK 465 GLY H 142 REMARK 465 SER H 224 REMARK 465 CYS H 225 REMARK 465 ASP H 226 REMARK 465 LYS H 227 REMARK 465 THR H 228 REMARK 465 HIS H 229 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 LYS A 18 REMARK 465 GLN A 19 REMARK 465 ASN A 20 REMARK 465 VAL A 21 REMARK 465 SER A 22 REMARK 465 SER A 23 REMARK 465 LEU A 24 REMARK 465 ASP A 25 REMARK 465 GLU A 26 REMARK 465 LYS A 27 REMARK 465 ASN A 28 REMARK 465 SER A 29 REMARK 465 VAL A 30 REMARK 465 SER A 31 REMARK 465 VAL A 32 REMARK 465 ASP A 33 REMARK 465 LEU A 34 REMARK 465 PRO A 35 REMARK 465 GLY A 36 REMARK 465 GLU A 37 REMARK 465 MET A 38 REMARK 465 LYS A 39 REMARK 465 VAL A 40 REMARK 465 LEU A 41 REMARK 465 VAL A 42 REMARK 465 SER A 43 REMARK 465 LYS A 44 REMARK 465 GLU A 45 REMARK 465 LYS A 46 REMARK 465 ASN A 47 REMARK 465 LYS A 48 REMARK 465 ASP A 49 REMARK 465 GLY A 50 REMARK 465 LYS A 51 REMARK 465 TYR A 52 REMARK 465 ASP A 53 REMARK 465 LEU A 54 REMARK 465 ILE A 55 REMARK 465 ALA A 56 REMARK 465 THR A 57 REMARK 465 VAL A 58 REMARK 465 ASP A 59 REMARK 465 LYS A 60 REMARK 465 LEU A 61 REMARK 465 GLU A 62 REMARK 465 LEU A 63 REMARK 465 LYS A 64 REMARK 465 GLY A 65 REMARK 465 THR A 66 REMARK 465 SER A 67 REMARK 465 ASP A 68 REMARK 465 LYS A 69 REMARK 465 ASN A 70 REMARK 465 ASN A 71 REMARK 465 GLY A 72 REMARK 465 SER A 73 REMARK 465 GLY A 74 REMARK 465 VAL A 75 REMARK 465 LEU A 76 REMARK 465 GLU A 77 REMARK 465 GLY A 78 REMARK 465 VAL A 79 REMARK 465 LYS A 80 REMARK 465 ALA A 81 REMARK 465 ASP A 82 REMARK 465 LYS A 83 REMARK 465 SER A 84 REMARK 465 LYS A 85 REMARK 465 VAL A 86 REMARK 465 LYS A 87 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 OH TYR L 92 O HOH L 401 2.12 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 THR L 52 -3.23 66.33 REMARK 500 SER L 53 -37.76 -131.27 REMARK 500 PHE L 84 56.68 -90.14 REMARK 500 GLU A 104 -23.66 -144.03 REMARK 500 VAL A 110 -59.99 -121.64 REMARK 500 ASP A 118 49.62 -86.60 REMARK 500 ALA A 173 -8.82 -59.85 REMARK 500 GLU A 174 -63.71 -93.19 REMARK 500 ASN A 241 61.51 60.71 REMARK 500 REMARK 500 REMARK: NULL DBREF 9BYF H 1 229 PDB 9BYF 9BYF 1 229 DBREF 9BYF L 1 215 PDB 9BYF 9BYF 1 215 DBREF 9BYF A 18 273 UNP P0CL66 OSPA_BORBU 18 273 SEQRES 1 H 229 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 229 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 229 PHE THR PHE ARG ASN TYR TRP MET ASP TRP VAL ARG GLN SEQRES 4 H 229 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ASN ILE LYS SEQRES 5 H 229 GLN ASP GLY SER VAL LYS TYR TYR VAL ASP SER VAL GLU SEQRES 6 H 229 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 229 LEU PHE LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 229 ALA VAL TYR TYR CYS ALA ARG ASP GLY TYR SER GLY TYR SEQRES 9 H 229 ASP SER VAL GLY PHE ASP ILE TRP GLY GLN GLY THR MET SEQRES 10 H 229 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 229 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 229 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 229 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 229 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 229 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 229 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 229 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 H 229 PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 L 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SER ASP THR SEQRES 5 L 215 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 215 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 215 TYR GLY SER SER PRO TYR THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 256 LYS GLN ASN VAL SER SER LEU ASP GLU LYS ASN SER VAL SEQRES 2 A 256 SER VAL ASP LEU PRO GLY GLU MET LYS VAL LEU VAL SER SEQRES 3 A 256 LYS GLU LYS ASN LYS ASP GLY LYS TYR ASP LEU ILE ALA SEQRES 4 A 256 THR VAL ASP LYS LEU GLU LEU LYS GLY THR SER ASP LYS SEQRES 5 A 256 ASN ASN GLY SER GLY VAL LEU GLU GLY VAL LYS ALA ASP SEQRES 6 A 256 LYS SER LYS VAL LYS LEU THR ILE SER ASP ASP LEU GLY SEQRES 7 A 256 GLN THR THR LEU GLU VAL PHE LYS GLU ASP GLY LYS THR SEQRES 8 A 256 LEU VAL SER LYS LYS VAL THR SER LYS ASP LYS SER SER SEQRES 9 A 256 THR GLU GLU LYS PHE ASN GLU LYS GLY GLU VAL SER GLU SEQRES 10 A 256 LYS ILE ILE THR ARG ALA ASP GLY THR ARG LEU GLU TYR SEQRES 11 A 256 THR GLY ILE LYS SER ASP GLY SER GLY LYS ALA LYS GLU SEQRES 12 A 256 VAL LEU LYS GLY TYR VAL LEU GLU GLY THR LEU THR ALA SEQRES 13 A 256 GLU LYS THR THR LEU VAL VAL LYS GLU GLY THR VAL THR SEQRES 14 A 256 LEU SER LYS ASN ILE SER LYS SER GLY GLU VAL SER VAL SEQRES 15 A 256 GLU LEU ASN ASP THR ASP SER SER ALA ALA THR LYS LYS SEQRES 16 A 256 THR ALA ALA TRP ASN SER GLY THR SER THR LEU THR ILE SEQRES 17 A 256 THR VAL ASN SER LYS LYS THR LYS ASP LEU VAL PHE THR SEQRES 18 A 256 LYS GLU ASN THR ILE THR VAL GLN GLN TYR ASP SER ASN SEQRES 19 A 256 GLY THR LYS LEU GLU GLY SER ALA VAL GLU ILE THR LYS SEQRES 20 A 256 LEU ASP GLU ILE LYS ASN ALA LEU LYS HET EDO H 301 4 HET CL H 302 1 HET CL H 303 1 HET CL H 304 1 HET CL L 301 1 HET CL L 302 1 HET CL L 303 1 HET CL L 304 1 HET CL A 301 1 HETNAM EDO 1,2-ETHANEDIOL HETNAM CL CHLORIDE ION HETSYN EDO ETHYLENE GLYCOL FORMUL 4 EDO C2 H6 O2 FORMUL 5 CL 8(CL 1-) FORMUL 13 HOH *116(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 ARG H 87 THR H 91 5 5 HELIX 3 AA3 SER H 165 ALA H 167 5 3 HELIX 4 AA4 SER H 196 LEU H 198 5 3 HELIX 5 AA5 GLU L 80 PHE L 84 5 5 HELIX 6 AA6 SER L 122 LYS L 127 1 6 HELIX 7 AA7 LYS L 184 LYS L 189 1 6 HELIX 8 AA8 LYS A 264 LEU A 272 1 9 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA1 4 SER H 78 MET H 83 -1 O LEU H 79 N CYS H 22 SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AA2 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 116 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA2 6 LYS H 58 TYR H 60 -1 O TYR H 59 N ASN H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AA3 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 116 SHEET 4 AA3 4 ILE H 111 TRP H 112 -1 O ILE H 111 N ARG H 98 SHEET 1 AA4 4 SER H 129 LEU H 133 0 SHEET 2 AA4 4 THR H 144 TYR H 154 -1 O LEU H 150 N PHE H 131 SHEET 3 AA4 4 TYR H 185 PRO H 194 -1 O VAL H 191 N LEU H 147 SHEET 4 AA4 4 VAL H 172 THR H 174 -1 N HIS H 173 O VAL H 190 SHEET 1 AA5 4 SER H 129 LEU H 133 0 SHEET 2 AA5 4 THR H 144 TYR H 154 -1 O LEU H 150 N PHE H 131 SHEET 3 AA5 4 TYR H 185 PRO H 194 -1 O VAL H 191 N LEU H 147 SHEET 4 AA5 4 VAL H 178 LEU H 179 -1 N VAL H 178 O SER H 186 SHEET 1 AA6 3 THR H 160 TRP H 163 0 SHEET 2 AA6 3 ILE H 204 HIS H 209 -1 O ASN H 206 N SER H 162 SHEET 3 AA6 3 THR H 214 ARG H 219 -1 O LYS H 218 N CYS H 205 SHEET 1 AA7 3 LEU L 4 SER L 7 0 SHEET 2 AA7 3 ALA L 19 VAL L 29 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 3 PHE L 63 ILE L 76 -1 O LEU L 74 N LEU L 21 SHEET 1 AA8 5 THR L 10 LEU L 13 0 SHEET 2 AA8 5 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 11 SHEET 3 AA8 5 VAL L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA8 5 LEU L 34 GLN L 39 -1 N ALA L 35 O GLN L 90 SHEET 5 AA8 5 ARG L 46 SER L 50 -1 O ARG L 46 N GLN L 38 SHEET 1 AA9 4 SER L 115 PHE L 119 0 SHEET 2 AA9 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AA9 4 TYR L 174 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AA9 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB1 4 LEU L 155 GLN L 156 0 SHEET 2 AB1 4 LYS L 146 VAL L 151 -1 N TRP L 149 O GLN L 156 SHEET 3 AB1 4 VAL L 192 THR L 198 -1 O ALA L 194 N LYS L 150 SHEET 4 AB1 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AB211 THR A 89 ILE A 90 0 SHEET 2 AB211 THR A 97 PHE A 102 -1 O THR A 98 N THR A 89 SHEET 3 AB211 LEU A 109 THR A 115 -1 O LYS A 113 N LEU A 99 SHEET 4 AB211 SER A 121 PHE A 126 -1 O GLU A 124 N LYS A 112 SHEET 5 AB211 VAL A 132 THR A 138 -1 O SER A 133 N LYS A 125 SHEET 6 AB211 ARG A 144 THR A 148 -1 O LEU A 145 N ILE A 137 SHEET 7 AB211 GLY A 156 VAL A 161 -1 O LYS A 157 N THR A 148 SHEET 8 AB211 VAL A 166 LEU A 171 -1 O LEU A 167 N GLU A 160 SHEET 9 AB211 LYS A 175 GLU A 182 -1 O THR A 177 N THR A 170 SHEET 10 AB211 VAL A 185 SER A 192 -1 O LEU A 187 N VAL A 180 SHEET 11 AB211 VAL A 197 ASP A 203 -1 O SER A 198 N ASN A 190 SHEET 1 AB3 5 LYS A 212 ASN A 217 0 SHEET 2 AB3 5 THR A 222 VAL A 227 -1 O THR A 226 N THR A 213 SHEET 3 AB3 5 LYS A 230 THR A 238 -1 O LYS A 230 N VAL A 227 SHEET 4 AB3 5 THR A 242 GLN A 247 -1 O GLN A 246 N ASP A 234 SHEET 5 AB3 5 VAL A 260 GLU A 261 -1 O VAL A 260 N VAL A 245 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 149 CYS H 205 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 89 1555 1555 2.03 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.03 CISPEP 1 PHE H 155 PRO H 156 0 -3.30 CISPEP 2 GLU H 157 PRO H 158 0 -1.12 CISPEP 3 SER L 7 PRO L 8 0 -2.12 CISPEP 4 SER L 95 PRO L 96 0 -1.67 CISPEP 5 TYR L 141 PRO L 142 0 2.15 CRYST1 101.120 162.416 126.785 90.00 90.00 90.00 C 2 2 2 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 0.009889 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006157 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007887 0.00000