HEADER IMMUNE SYSTEM 27-JUN-24 9CFD TITLE FAB 8C1 IN COMPLEX WITH OSPCA PEPTIDE P15 (RESIDUES 132-146) COMPND MOL_ID: 1; COMPND 2 MOLECULE: MONOCLONAL 8C1 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MONOCLONAL 8C1 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: OUTER SURFACE PROTEIN C; COMPND 11 CHAIN: P; COMPND 12 FRAGMENT: RESIDUES 132-146; COMPND 13 SYNONYM: PC,P23; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: BORRELIELLA BURGDORFERI B31; SOURCE 14 ORGANISM_TAXID: 224326 KEYWDS ANTI-OSPA ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.J.RUDOLPH,N.MANTIS REVDAT 1 27-AUG-25 9CFD 0 JRNL AUTH M.J.RUDOLPH,N.MANTIS JRNL TITL FAB 8C1 IN COMPLEX WITH OSPCA PEPTIDE P15 (RESIDUES 132-146) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.64 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.09 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 56248 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.162 REMARK 3 R VALUE (WORKING SET) : 0.161 REMARK 3 FREE R VALUE : 0.189 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 2878 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 46.0900 - 4.5200 0.99 2597 154 0.1760 0.1982 REMARK 3 2 4.5100 - 3.5900 0.99 2559 130 0.1440 0.1746 REMARK 3 3 3.5900 - 3.1300 1.00 2557 134 0.1534 0.1887 REMARK 3 4 3.1300 - 2.8500 1.00 2558 134 0.1627 0.1922 REMARK 3 5 2.8500 - 2.6400 1.00 2579 133 0.1533 0.1517 REMARK 3 6 2.6400 - 2.4900 1.00 2549 148 0.1545 0.1855 REMARK 3 7 2.4900 - 2.3600 1.00 2543 138 0.1502 0.1785 REMARK 3 8 2.3600 - 2.2600 1.00 2554 143 0.1557 0.1963 REMARK 3 9 2.2600 - 2.1700 1.00 2516 138 0.1428 0.1568 REMARK 3 10 2.1700 - 2.1000 1.00 2540 150 0.1469 0.1781 REMARK 3 11 2.1000 - 2.0300 1.00 2580 115 0.1508 0.1763 REMARK 3 12 2.0300 - 1.9700 1.00 2531 147 0.1618 0.1793 REMARK 3 13 1.9700 - 1.9200 1.00 2579 126 0.1621 0.1930 REMARK 3 14 1.9200 - 1.8800 1.00 2521 164 0.1632 0.2048 REMARK 3 15 1.8800 - 1.8300 1.00 2515 137 0.1719 0.2044 REMARK 3 16 1.8300 - 1.7900 1.00 2552 145 0.1632 0.2029 REMARK 3 17 1.7900 - 1.7600 1.00 2536 126 0.1760 0.2025 REMARK 3 18 1.7600 - 1.7200 1.00 2585 106 0.1946 0.2471 REMARK 3 19 1.7200 - 1.6900 1.00 2540 144 0.2139 0.2633 REMARK 3 20 1.6900 - 1.6700 1.00 2469 151 0.2379 0.2867 REMARK 3 21 1.6700 - 1.6400 0.93 2410 115 0.2694 0.3124 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) : 0.178 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.231 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.94 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.13 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 : 0.018 3524 REMARK 3 ANGLE : 1.410 4800 REMARK 3 CHIRALITY : 0.092 547 REMARK 3 PLANARITY : 0.012 610 REMARK 3 DIHEDRAL : 6.477 483 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 134 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.7737 -41.3796 -13.8189 REMARK 3 T TENSOR REMARK 3 T11: 0.1798 T22: 0.3062 REMARK 3 T33: 0.2701 T12: 0.0253 REMARK 3 T13: -0.0120 T23: -0.0695 REMARK 3 L TENSOR REMARK 3 L11: 2.0018 L22: 3.6915 REMARK 3 L33: 6.3209 L12: 1.4711 REMARK 3 L13: -0.5993 L23: -4.3145 REMARK 3 S TENSOR REMARK 3 S11: 0.0189 S12: 0.4533 S13: -0.2846 REMARK 3 S21: -0.2962 S22: -0.0500 S23: -0.2408 REMARK 3 S31: 0.3626 S32: 0.2511 S33: 0.0842 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 156 THROUGH 177 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.4984 -41.0706 -10.8717 REMARK 3 T TENSOR REMARK 3 T11: 0.0913 T22: 0.2782 REMARK 3 T33: 0.2130 T12: 0.0756 REMARK 3 T13: 0.0037 T23: -0.0408 REMARK 3 L TENSOR REMARK 3 L11: 1.7123 L22: 5.2148 REMARK 3 L33: 4.0741 L12: 0.6445 REMARK 3 L13: 0.7791 L23: -2.2203 REMARK 3 S TENSOR REMARK 3 S11: 0.1374 S12: 0.2578 S13: -0.1631 REMARK 3 S21: 0.2263 S22: 0.0421 S23: -0.0451 REMARK 3 S31: -0.4507 S32: 0.1308 S33: -0.0643 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 178 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.8113 -36.3073 -20.2575 REMARK 3 T TENSOR REMARK 3 T11: 0.2395 T22: 0.4226 REMARK 3 T33: 0.2400 T12: 0.0403 REMARK 3 T13: 0.0025 T23: -0.0168 REMARK 3 L TENSOR REMARK 3 L11: 2.3868 L22: 6.5885 REMARK 3 L33: 3.9667 L12: 0.6245 REMARK 3 L13: 0.3416 L23: -2.2109 REMARK 3 S TENSOR REMARK 3 S11: -0.0152 S12: 0.5824 S13: 0.0734 REMARK 3 S21: -0.7412 S22: 0.1328 S23: 0.3461 REMARK 3 S31: -0.0161 S32: -0.0564 S33: -0.1857 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 132 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.4296 -39.7216 37.1471 REMARK 3 T TENSOR REMARK 3 T11: 0.3567 T22: 0.4515 REMARK 3 T33: 0.2375 T12: 0.0712 REMARK 3 T13: 0.0045 T23: 0.0334 REMARK 3 L TENSOR REMARK 3 L11: 2.2306 L22: 3.9937 REMARK 3 L33: 5.1619 L12: -1.8825 REMARK 3 L13: -2.0689 L23: 2.5798 REMARK 3 S TENSOR REMARK 3 S11: -0.1783 S12: -0.6270 S13: 0.1857 REMARK 3 S21: 0.1049 S22: 0.2015 S23: 0.2467 REMARK 3 S31: -0.3770 S32: -0.5615 S33: 0.0369 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.3262 -24.7906 15.8407 REMARK 3 T TENSOR REMARK 3 T11: 0.2496 T22: 0.1822 REMARK 3 T33: 0.2042 T12: 0.0879 REMARK 3 T13: 0.0186 T23: -0.0461 REMARK 3 L TENSOR REMARK 3 L11: 1.4923 L22: 3.2259 REMARK 3 L33: 5.9803 L12: 1.4294 REMARK 3 L13: -0.0558 L23: -3.4438 REMARK 3 S TENSOR REMARK 3 S11: 0.0191 S12: -0.1864 S13: 0.3311 REMARK 3 S21: 0.1652 S22: 0.1328 S23: 0.2688 REMARK 3 S31: -0.4124 S32: -0.2540 S33: -0.3156 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.2208 -28.6679 28.4370 REMARK 3 T TENSOR REMARK 3 T11: 0.2905 T22: 0.3130 REMARK 3 T33: 0.1907 T12: 0.1031 REMARK 3 T13: 0.0202 T23: -0.0443 REMARK 3 L TENSOR REMARK 3 L11: 2.0672 L22: 2.4088 REMARK 3 L33: 9.2621 L12: 1.5348 REMARK 3 L13: -3.2904 L23: -4.6767 REMARK 3 S TENSOR REMARK 3 S11: -0.1509 S12: -0.0089 S13: 0.0459 REMARK 3 S21: 0.2559 S22: 0.1843 S23: -0.0365 REMARK 3 S31: -0.5608 S32: -0.6679 S33: -0.1691 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 33 THROUGH 57 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.9076 -34.7533 23.1364 REMARK 3 T TENSOR REMARK 3 T11: 0.1278 T22: 0.1540 REMARK 3 T33: 0.1548 T12: 0.0275 REMARK 3 T13: -0.0065 T23: 0.0033 REMARK 3 L TENSOR REMARK 3 L11: 3.0902 L22: 3.0005 REMARK 3 L33: 2.7335 L12: -0.2927 REMARK 3 L13: 2.2985 L23: -1.9671 REMARK 3 S TENSOR REMARK 3 S11: 0.0216 S12: -0.0948 S13: 0.1022 REMARK 3 S21: 0.0151 S22: -0.0498 S23: -0.1197 REMARK 3 S31: 0.1622 S32: 0.1773 S33: -0.0278 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 58 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.0925 -28.3357 25.9889 REMARK 3 T TENSOR REMARK 3 T11: 0.2561 T22: 0.2028 REMARK 3 T33: 0.2079 T12: 0.0185 REMARK 3 T13: -0.0377 T23: -0.0105 REMARK 3 L TENSOR REMARK 3 L11: 3.4600 L22: 5.2744 REMARK 3 L33: 3.5466 L12: -1.3846 REMARK 3 L13: 1.2954 L23: -0.3449 REMARK 3 S TENSOR REMARK 3 S11: -0.0550 S12: -0.2193 S13: 0.5777 REMARK 3 S21: 0.4663 S22: 0.0485 S23: -0.4896 REMARK 3 S31: -0.8602 S32: 0.2810 S33: -0.0487 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 77 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.5005 -25.0789 17.5657 REMARK 3 T TENSOR REMARK 3 T11: 0.2438 T22: 0.1725 REMARK 3 T33: 0.1923 T12: -0.0058 REMARK 3 T13: -0.0255 T23: 0.0028 REMARK 3 L TENSOR REMARK 3 L11: 7.7828 L22: 1.9234 REMARK 3 L33: 3.7102 L12: 1.0996 REMARK 3 L13: -4.7911 L23: -1.0938 REMARK 3 S TENSOR REMARK 3 S11: 0.0866 S12: -0.3976 S13: 0.2374 REMARK 3 S21: 0.3450 S22: -0.1780 S23: -0.2277 REMARK 3 S31: -0.7253 S32: 0.4815 S33: -0.0825 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 92 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.9801 -30.2035 14.1232 REMARK 3 T TENSOR REMARK 3 T11: 0.1765 T22: 0.2002 REMARK 3 T33: 0.1782 T12: 0.0149 REMARK 3 T13: 0.0059 T23: -0.0107 REMARK 3 L TENSOR REMARK 3 L11: 0.4608 L22: 1.8096 REMARK 3 L33: 4.6431 L12: -0.2003 REMARK 3 L13: 0.5185 L23: -2.5077 REMARK 3 S TENSOR REMARK 3 S11: -0.0107 S12: -0.1573 S13: 0.0527 REMARK 3 S21: 0.1973 S22: 0.0121 S23: -0.0096 REMARK 3 S31: -0.2662 S32: 0.0777 S33: -0.0501 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 121 THROUGH 146 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.5620 -29.0242 -7.7755 REMARK 3 T TENSOR REMARK 3 T11: 0.1724 T22: 0.2413 REMARK 3 T33: 0.2070 T12: 0.0116 REMARK 3 T13: 0.0236 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 7.8532 L22: 6.7893 REMARK 3 L33: 1.1732 L12: 5.2919 REMARK 3 L13: 1.0105 L23: 0.5038 REMARK 3 S TENSOR REMARK 3 S11: -0.3408 S12: 0.6186 S13: 0.2696 REMARK 3 S21: -0.3851 S22: 0.2204 S23: 0.4503 REMARK 3 S31: -0.0387 S32: 0.0488 S33: 0.1002 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 147 THROUGH 189 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.3710 -31.7990 -1.3410 REMARK 3 T TENSOR REMARK 3 T11: 0.1694 T22: 0.1626 REMARK 3 T33: 0.2135 T12: 0.0098 REMARK 3 T13: 0.0342 T23: 0.0125 REMARK 3 L TENSOR REMARK 3 L11: 3.8947 L22: 0.6667 REMARK 3 L33: 1.2666 L12: 0.8600 REMARK 3 L13: -0.3461 L23: -0.1375 REMARK 3 S TENSOR REMARK 3 S11: -0.0961 S12: 0.0695 S13: -0.3603 REMARK 3 S21: -0.0405 S22: 0.0556 S23: -0.0572 REMARK 3 S31: 0.0523 S32: -0.1321 S33: 0.0395 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 190 THROUGH 204 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.3768 -25.9400 0.3465 REMARK 3 T TENSOR REMARK 3 T11: 0.1999 T22: 0.2237 REMARK 3 T33: 0.2190 T12: 0.0300 REMARK 3 T13: 0.0301 T23: 0.0032 REMARK 3 L TENSOR REMARK 3 L11: 8.3047 L22: 4.2619 REMARK 3 L33: 1.8803 L12: 5.1968 REMARK 3 L13: 2.9379 L23: 2.0209 REMARK 3 S TENSOR REMARK 3 S11: -0.2522 S12: -0.2221 S13: 0.1347 REMARK 3 S21: -0.2453 S22: 0.1040 S23: 0.1514 REMARK 3 S31: -0.2191 S32: -0.2053 S33: 0.0829 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 205 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.3422 -21.9923 -2.8777 REMARK 3 T TENSOR REMARK 3 T11: 0.2428 T22: 0.3128 REMARK 3 T33: 0.3214 T12: 0.0719 REMARK 3 T13: 0.0136 T23: 0.0011 REMARK 3 L TENSOR REMARK 3 L11: 7.1892 L22: 6.3645 REMARK 3 L33: 4.9871 L12: 3.1679 REMARK 3 L13: 2.2838 L23: 0.4069 REMARK 3 S TENSOR REMARK 3 S11: -0.2193 S12: -0.2960 S13: 0.9697 REMARK 3 S21: -0.1038 S22: -0.0755 S23: 0.3419 REMARK 3 S31: -0.3157 S32: -0.8618 S33: 0.2484 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.9828 -54.2084 18.7040 REMARK 3 T TENSOR REMARK 3 T11: 0.1825 T22: 0.1836 REMARK 3 T33: 0.2185 T12: 0.0360 REMARK 3 T13: -0.0045 T23: 0.0253 REMARK 3 L TENSOR REMARK 3 L11: 2.6535 L22: 2.4293 REMARK 3 L33: 4.8683 L12: 0.0777 REMARK 3 L13: 2.1305 L23: 0.7539 REMARK 3 S TENSOR REMARK 3 S11: 0.0260 S12: 0.0251 S13: -0.1346 REMARK 3 S21: -0.0771 S22: 0.0215 S23: 0.0066 REMARK 3 S31: 0.0597 S32: -0.0374 S33: -0.0483 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 38 THROUGH 53 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.8668 -45.5273 17.3191 REMARK 3 T TENSOR REMARK 3 T11: 0.1589 T22: 0.1704 REMARK 3 T33: 0.1631 T12: 0.0404 REMARK 3 T13: -0.0397 T23: 0.0011 REMARK 3 L TENSOR REMARK 3 L11: 3.3412 L22: 6.9199 REMARK 3 L33: 7.5845 L12: 0.6282 REMARK 3 L13: -1.3448 L23: -2.3155 REMARK 3 S TENSOR REMARK 3 S11: 0.1128 S12: 0.0281 S13: 0.0272 REMARK 3 S21: -0.4715 S22: 0.1603 S23: 0.5406 REMARK 3 S31: -0.3620 S32: -0.6910 S33: -0.2823 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 54 THROUGH 80 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.4777 -55.5185 23.0403 REMARK 3 T TENSOR REMARK 3 T11: 0.1613 T22: 0.2470 REMARK 3 T33: 0.2473 T12: -0.0255 REMARK 3 T13: -0.0126 T23: 0.0767 REMARK 3 L TENSOR REMARK 3 L11: 4.0215 L22: 3.3504 REMARK 3 L33: 4.6137 L12: -0.8496 REMARK 3 L13: 1.2778 L23: 1.0368 REMARK 3 S TENSOR REMARK 3 S11: 0.0906 S12: -0.2204 S13: -0.3105 REMARK 3 S21: -0.0418 S22: -0.0426 S23: 0.5019 REMARK 3 S31: 0.0385 S32: -0.6267 S33: -0.0520 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 81 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.3610 -43.8433 4.3383 REMARK 3 T TENSOR REMARK 3 T11: 0.1330 T22: 0.1960 REMARK 3 T33: 0.1881 T12: 0.0283 REMARK 3 T13: 0.0142 T23: -0.0046 REMARK 3 L TENSOR REMARK 3 L11: 1.6287 L22: 0.2930 REMARK 3 L33: 2.5446 L12: -0.4125 REMARK 3 L13: 1.6368 L23: -0.5590 REMARK 3 S TENSOR REMARK 3 S11: 0.0519 S12: 0.0359 S13: -0.1389 REMARK 3 S21: 0.0017 S22: 0.0419 S23: 0.0850 REMARK 3 S31: 0.0025 S32: -0.1229 S33: -0.1272 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 9CFD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000285401. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-MAY-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56365 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640 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 (%) : 99.5 REMARK 200 DATA REDUNDANCY : 19.30 REMARK 200 R MERGE (I) : 0.08900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1 REMARK 200 DATA REDUNDANCY IN SHELL : 11.70 REMARK 200 R MERGE FOR SHELL (I) : 1.04100 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 (%): 47.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS- PH 7.0, 200 MM LI2SO4, REMARK 280 AND 2.0 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.56267 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.78133 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.67200 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 11.89067 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.45333 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: 6240 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19600 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 129 REMARK 465 LYS H 130 REMARK 465 SER H 131 REMARK 465 THR H 132 REMARK 465 SER H 133 REMARK 465 SER H 216 REMARK 465 CYS H 217 REMARK 465 ASP H 218 REMARK 465 LYS H 219 REMARK 465 THR H 220 REMARK 465 HIS H 221 REMARK 465 CYS L 219 REMARK 465 GLY P 146 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 HZ1 LYS L 195 O HOH L 404 1.47 REMARK 500 HD22 ASN L 142 O1 SO4 L 301 1.59 REMARK 500 O PRO H 41 O HOH H 401 1.94 REMARK 500 NZ LYS H 65 O1 SO4 H 302 2.00 REMARK 500 O HOH H 411 O HOH H 458 2.00 REMARK 500 O HOH L 413 O HOH L 540 2.01 REMARK 500 O HOH H 446 O HOH H 567 2.06 REMARK 500 O HOH H 550 O HOH H 555 2.07 REMARK 500 O HOH H 566 O HOH L 470 2.08 REMARK 500 OG1 THR H 192 O HOH H 402 2.08 REMARK 500 OE2 GLU L 148 O HOH L 401 2.09 REMARK 500 O3 SO4 H 301 O HOH H 403 2.15 REMARK 500 OD2 ASP L 1 O HOH L 402 2.16 REMARK 500 O HOH L 420 O HOH L 504 2.19 REMARK 500 O HOH L 541 O HOH L 549 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 NZ LYS L 79 O4 SO4 L 301 3545 2.11 REMARK 500 O HOH H 518 O HOH H 572 5554 2.14 REMARK 500 O HOH H 571 O HOH H 572 5554 2.15 REMARK 500 O HOH L 409 O HOH L 431 4544 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 GLN L 6 CB GLN L 6 CG -0.181 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 CYS H 141 CA - CB - SG ANGL. DEV. = 9.3 DEGREES REMARK 500 CYS H 197 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 CYS L 94 CA - CB - SG ANGL. DEV. = 8.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER H 99 -135.55 56.29 REMARK 500 ASP H 145 62.97 61.05 REMARK 500 VAL L 56 -49.60 77.79 REMARK 500 ASN L 143 62.38 61.56 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH L 561 DISTANCE = 5.94 ANGSTROMS DBREF 9CFD H 1 221 PDB 9CFD 9CFD 1 221 DBREF 9CFD L 1 219 PDB 9CFD 9CFD 1 219 DBREF 9CFD P 132 146 UNP Q07337 OSPC_BORBU 132 146 SEQRES 1 H 221 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 221 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 H 221 TYR THR PHE SER ASN SER TRP MET ASN TRP VAL LYS GLN SEQRES 4 H 221 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ARG ILE TYR SEQRES 5 H 221 PRO GLY ASP GLY ASP THR ASN TYR ASN GLY LYS PHE LYS SEQRES 6 H 221 ASP LYS ALA THR LEU THR THR ASP LYS SER SER SER THR SEQRES 7 H 221 ALA TYR MET ARG LEU SER SER LEU THR SER VAL ASP SER SEQRES 8 H 221 ALA VAL TYR PHE CYS ALA ARG SER LEU PHE ASP TYR TRP SEQRES 9 H 221 GLY GLN GLY THR THR LEU THR VAL SER SER ALA SER THR SEQRES 10 H 221 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 H 221 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 H 221 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 H 221 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 H 221 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 H 221 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 H 221 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 H 221 ASP LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 L 219 ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SER VAL SEQRES 2 L 219 THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 L 219 GLN SER LEU LEU ASP SER ASP GLY LYS THR TYR LEU ILE SEQRES 4 L 219 TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5 L 219 ILE TYR LEU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 L 219 TYR CYS CYS GLN GLY THR HIS PHE PRO PHE THR PHE GLY SEQRES 9 L 219 VAL GLY THR LYS LEU GLU LEU LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 P 15 GLU THR PHE THR ASN LYS LEU LYS GLU LYS HIS THR ASP SEQRES 2 P 15 LEU GLY HET SO4 H 301 5 HET SO4 H 302 5 HET CL H 303 1 HET CL H 304 1 HET CL H 305 1 HET CL H 306 1 HET CL H 307 1 HET SO4 L 301 5 HET CL L 302 1 HET CL L 303 1 HETNAM SO4 SULFATE ION HETNAM CL CHLORIDE ION FORMUL 4 SO4 3(O4 S 2-) FORMUL 6 CL 7(CL 1-) FORMUL 14 HOH *377(H2 O) HELIX 1 AA1 THR H 28 SER H 32 5 5 HELIX 2 AA2 GLY H 62 LYS H 65 5 4 HELIX 3 AA3 LYS H 74 SER H 76 5 3 HELIX 4 AA4 THR H 87 SER H 91 5 5 HELIX 5 AA5 SER H 157 ALA H 159 5 3 HELIX 6 AA6 SER H 188 LEU H 190 5 3 HELIX 7 AA7 LYS H 202 ASN H 205 5 4 HELIX 8 AA8 GLU L 84 LEU L 88 5 5 HELIX 9 AA9 SER L 126 GLY L 133 1 8 HELIX 10 AB1 LYS L 188 HIS L 194 1 7 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O MET H 81 N ILE H 20 SHEET 4 AA1 4 ALA H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 108 VAL H 112 1 O THR H 111 N GLU H 10 SHEET 3 AA2 6 ALA H 92 ARG H 98 -1 N ALA H 92 O LEU H 110 SHEET 4 AA2 6 MET H 34 ARG H 40 -1 N ASN H 35 O ALA H 97 SHEET 5 AA2 6 GLY H 44 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O ASN H 59 N ARG H 50 SHEET 1 AA3 4 GLU H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 108 VAL H 112 1 O THR H 111 N GLU H 10 SHEET 3 AA3 4 ALA H 92 ARG H 98 -1 N ALA H 92 O LEU H 110 SHEET 4 AA3 4 TYR H 103 TRP H 104 -1 O TYR H 103 N ARG H 98 SHEET 1 AA4 4 SER H 121 LEU H 125 0 SHEET 2 AA4 4 THR H 136 TYR H 146 -1 O LYS H 144 N SER H 121 SHEET 3 AA4 4 TYR H 177 PRO H 186 -1 O VAL H 185 N ALA H 137 SHEET 4 AA4 4 VAL H 164 THR H 166 -1 N HIS H 165 O VAL H 182 SHEET 1 AA5 4 SER H 121 LEU H 125 0 SHEET 2 AA5 4 THR H 136 TYR H 146 -1 O LYS H 144 N SER H 121 SHEET 3 AA5 4 TYR H 177 PRO H 186 -1 O VAL H 185 N ALA H 137 SHEET 4 AA5 4 VAL H 170 LEU H 171 -1 N VAL H 170 O SER H 178 SHEET 1 AA6 3 THR H 152 TRP H 155 0 SHEET 2 AA6 3 ILE H 196 HIS H 201 -1 O ASN H 198 N SER H 154 SHEET 3 AA6 3 THR H 206 ARG H 211 -1 O VAL H 208 N VAL H 199 SHEET 1 AA7 4 MET L 4 THR L 7 0 SHEET 2 AA7 4 ALA L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AA7 4 ASP L 75 ILE L 80 -1 O ILE L 80 N ALA L 19 SHEET 4 AA7 4 PHE L 67 SER L 72 -1 N THR L 68 O LYS L 79 SHEET 1 AA8 6 THR L 10 THR L 14 0 SHEET 2 AA8 6 THR L 107 LYS L 112 1 O GLU L 110 N LEU L 11 SHEET 3 AA8 6 GLY L 89 GLN L 95 -1 N GLY L 89 O LEU L 109 SHEET 4 AA8 6 LEU L 38 GLN L 43 -1 N GLN L 43 O VAL L 90 SHEET 5 AA8 6 LYS L 50 TYR L 54 -1 O LEU L 52 N TRP L 40 SHEET 6 AA8 6 LYS L 58 LEU L 59 -1 O LYS L 58 N TYR L 54 SHEET 1 AA9 4 THR L 10 THR L 14 0 SHEET 2 AA9 4 THR L 107 LYS L 112 1 O GLU L 110 N LEU L 11 SHEET 3 AA9 4 GLY L 89 GLN L 95 -1 N GLY L 89 O LEU L 109 SHEET 4 AA9 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AB1 4 SER L 119 PHE L 123 0 SHEET 2 AB1 4 THR L 134 PHE L 144 -1 O LEU L 140 N PHE L 121 SHEET 3 AB1 4 TYR L 178 SER L 187 -1 O LEU L 184 N VAL L 137 SHEET 4 AB1 4 SER L 164 VAL L 168 -1 N SER L 167 O SER L 181 SHEET 1 AB2 4 ALA L 158 LEU L 159 0 SHEET 2 AB2 4 LYS L 150 VAL L 155 -1 N VAL L 155 O ALA L 158 SHEET 3 AB2 4 VAL L 196 THR L 202 -1 O GLU L 200 N GLN L 152 SHEET 4 AB2 4 VAL L 210 ASN L 215 -1 O VAL L 210 N VAL L 201 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.10 SSBOND 2 CYS H 141 CYS H 197 1555 1555 2.09 SSBOND 3 CYS L 23 CYS L 93 1555 1555 2.14 SSBOND 4 CYS L 139 CYS L 199 1555 1555 2.10 CISPEP 1 PHE H 147 PRO H 148 0 -10.08 CISPEP 2 GLU H 149 PRO H 150 0 -2.08 CISPEP 3 THR L 7 PRO L 8 0 -2.97 CISPEP 4 PHE L 99 PRO L 100 0 -2.43 CISPEP 5 TYR L 145 PRO L 146 0 -0.32 CRYST1 106.440 106.440 71.344 90.00 90.00 120.00 P 65 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.009395 0.005424 0.000000 0.00000 SCALE2 0.000000 0.010848 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014017 0.00000