HEADER RNA 01-NOV-24 9E7D TITLE CRYSTAL STRUCTURE OF HIV-1 RRE SLII A31C MUTANT IN COMPLEX WITH FAB TITLE 2 BL3-6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: REV RESPONSE ELEMENT SLIIC; COMPND 3 CHAIN: R, C; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: BL3-6 FAB HEAVY CHAIN; COMPND 8 CHAIN: H, A; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: BL3-6 FAB LIGHT CHAIN; COMPND 12 CHAIN: L, B; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 4 ORGANISM_TAXID: 11676; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 7 ORGANISM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 10 MOL_ID: 3; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HIV-1, REPLICATION, FAB, CHAPERONE, REV RESPONSE ELEMENT, RNA EXPDTA X-RAY DIFFRACTION AUTHOR M.OJHA,D.KOIRALA REVDAT 1 28-MAY-25 9E7D 0 JRNL AUTH M.OJHA,D.KOIRALA JRNL TITL CRYSTAL STRUCTURE OF HIV-1 RRE SLII A31C MUTANT IN COMPLEX JRNL TITL 2 WITH FAB BL3-6 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.11 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) : 3.11 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.20 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 73.6 REMARK 3 NUMBER OF REFLECTIONS : 20060 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.250 REMARK 3 R VALUE (WORKING SET) : 0.246 REMARK 3 FREE R VALUE : 0.329 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800 REMARK 3 FREE R VALUE TEST SET COUNT : 962 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 34.2000 - 5.9300 0.99 3679 191 0.2043 0.2799 REMARK 3 2 5.9300 - 4.7100 0.99 3693 178 0.2280 0.2904 REMARK 3 3 4.7100 - 4.1200 0.94 3478 174 0.2382 0.3552 REMARK 3 4 4.1200 - 3.8100 0.88 2572 125 0.2702 0.3662 REMARK 3 5 3.4800 - 3.4700 0.22 34 1 0.2730 0.6438 REMARK 3 6 3.4700 - 3.2700 0.77 2878 151 0.3081 0.3792 REMARK 3 7 3.2700 - 3.1100 0.75 2764 142 0.3002 0.3727 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) : 0.497 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.736 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.50 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 : 0.010 10254 REMARK 3 ANGLE : 1.364 14620 REMARK 3 CHIRALITY : 0.063 1758 REMARK 3 PLANARITY : 0.012 1326 REMARK 3 DIHEDRAL : 17.802 4156 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 34 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 1 THROUGH 10 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.8641 -1.3703 -5.9659 REMARK 3 T TENSOR REMARK 3 T11: 0.8696 T22: 0.8081 REMARK 3 T33: 1.5892 T12: -0.3094 REMARK 3 T13: 0.0515 T23: 0.5216 REMARK 3 L TENSOR REMARK 3 L11: 1.4412 L22: 0.6873 REMARK 3 L33: 1.2253 L12: 0.8321 REMARK 3 L13: 0.3744 L23: -0.2730 REMARK 3 S TENSOR REMARK 3 S11: 0.0924 S12: -0.6539 S13: -1.1104 REMARK 3 S21: -0.0530 S22: 0.0201 S23: -0.4428 REMARK 3 S31: 0.3689 S32: 0.1690 S33: 0.3061 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 11 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.1293 -14.4671 -11.2076 REMARK 3 T TENSOR REMARK 3 T11: 1.2907 T22: 1.0563 REMARK 3 T33: 2.1247 T12: -0.1853 REMARK 3 T13: 0.4513 T23: 0.2674 REMARK 3 L TENSOR REMARK 3 L11: 1.2498 L22: 1.4222 REMARK 3 L33: 1.5053 L12: -0.8156 REMARK 3 L13: -0.7078 L23: 1.4525 REMARK 3 S TENSOR REMARK 3 S11: -0.0756 S12: -0.7098 S13: -1.3139 REMARK 3 S21: 0.2148 S22: -0.0379 S23: 0.0751 REMARK 3 S31: 0.0106 S32: 0.2570 S33: 0.2185 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 26 THROUGH 35 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.3273 -22.0815 -3.1348 REMARK 3 T TENSOR REMARK 3 T11: 1.1979 T22: 1.0216 REMARK 3 T33: 2.2183 T12: 0.1909 REMARK 3 T13: 0.5823 T23: 0.6851 REMARK 3 L TENSOR REMARK 3 L11: 1.0437 L22: 0.0655 REMARK 3 L33: 0.6506 L12: -0.2077 REMARK 3 L13: -0.8240 L23: 0.1706 REMARK 3 S TENSOR REMARK 3 S11: -0.3575 S12: -1.0665 S13: -1.5021 REMARK 3 S21: 0.4499 S22: 0.0605 S23: 0.2978 REMARK 3 S31: 0.1169 S32: -0.0360 S33: 0.1373 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 36 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.7944 3.4877 -0.5717 REMARK 3 T TENSOR REMARK 3 T11: 0.1448 T22: 0.4425 REMARK 3 T33: 1.4080 T12: -0.4606 REMARK 3 T13: 0.2600 T23: 0.6230 REMARK 3 L TENSOR REMARK 3 L11: 1.9872 L22: 0.0793 REMARK 3 L33: 0.8271 L12: 0.2194 REMARK 3 L13: 0.4919 L23: 0.2425 REMARK 3 S TENSOR REMARK 3 S11: 0.1224 S12: -0.8749 S13: -1.2717 REMARK 3 S21: -0.1294 S22: -0.2265 S23: 0.2959 REMARK 3 S31: 0.6796 S32: -0.2578 S33: -0.0128 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.1611 78.6651 -46.3291 REMARK 3 T TENSOR REMARK 3 T11: 1.8700 T22: 1.6760 REMARK 3 T33: 2.5200 T12: -0.0396 REMARK 3 T13: 0.6510 T23: 0.3292 REMARK 3 L TENSOR REMARK 3 L11: 1.1735 L22: 0.0490 REMARK 3 L33: 0.3791 L12: -0.2351 REMARK 3 L13: -0.6392 L23: 0.1170 REMARK 3 S TENSOR REMARK 3 S11: 0.1397 S12: 0.4080 S13: 0.6291 REMARK 3 S21: -0.3788 S22: -0.1283 S23: -0.4469 REMARK 3 S31: 0.2020 S32: 0.3771 S33: -0.1885 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 31 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.1448 81.5992 -42.9546 REMARK 3 T TENSOR REMARK 3 T11: 1.2053 T22: 1.0198 REMARK 3 T33: 1.1593 T12: -0.3610 REMARK 3 T13: 0.0667 T23: 0.4341 REMARK 3 L TENSOR REMARK 3 L11: 1.3630 L22: 0.4615 REMARK 3 L33: 0.5990 L12: -0.6990 REMARK 3 L13: -0.6492 L23: 0.2372 REMARK 3 S TENSOR REMARK 3 S11: 0.1718 S12: 0.2617 S13: 1.4369 REMARK 3 S21: -0.0839 S22: 0.2835 S23: -0.8411 REMARK 3 S31: -0.6674 S32: 0.7834 S33: -0.0059 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 3 THROUGH 20 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.6955 19.7674 -25.8644 REMARK 3 T TENSOR REMARK 3 T11: 0.0180 T22: 0.0620 REMARK 3 T33: 0.6650 T12: -0.0084 REMARK 3 T13: 0.1605 T23: 0.2869 REMARK 3 L TENSOR REMARK 3 L11: 4.9566 L22: 3.3446 REMARK 3 L33: 2.1252 L12: 0.7255 REMARK 3 L13: -0.8928 L23: -2.6520 REMARK 3 S TENSOR REMARK 3 S11: 0.0499 S12: -0.2781 S13: 0.3431 REMARK 3 S21: -0.1444 S22: 0.3179 S23: 0.3177 REMARK 3 S31: -0.2966 S32: 0.3355 S33: -0.4951 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 21 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.6087 17.3531 -14.1502 REMARK 3 T TENSOR REMARK 3 T11: 0.1418 T22: 0.2639 REMARK 3 T33: 0.5038 T12: -0.2016 REMARK 3 T13: -0.1037 T23: 0.3786 REMARK 3 L TENSOR REMARK 3 L11: 3.1412 L22: 1.4130 REMARK 3 L33: 1.8411 L12: 0.7122 REMARK 3 L13: -1.2627 L23: 0.2943 REMARK 3 S TENSOR REMARK 3 S11: 0.0751 S12: -0.4201 S13: -0.1449 REMARK 3 S21: 0.1117 S22: -0.0462 S23: 0.0835 REMARK 3 S31: -0.0379 S32: 0.1488 S33: 0.0139 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 37 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.9817 16.0000 -22.7422 REMARK 3 T TENSOR REMARK 3 T11: -0.2278 T22: -0.0669 REMARK 3 T33: 0.4177 T12: 0.1102 REMARK 3 T13: 0.0791 T23: 0.1212 REMARK 3 L TENSOR REMARK 3 L11: 1.3390 L22: 0.8006 REMARK 3 L33: 0.6448 L12: -0.7245 REMARK 3 L13: 0.0864 L23: 0.1041 REMARK 3 S TENSOR REMARK 3 S11: -0.0198 S12: 0.1837 S13: -0.1188 REMARK 3 S21: -0.1312 S22: -0.2141 S23: 0.1697 REMARK 3 S31: -0.0098 S32: -0.0539 S33: -0.1612 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 68 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.9005 10.7395 -21.0911 REMARK 3 T TENSOR REMARK 3 T11: 0.0119 T22: 0.1176 REMARK 3 T33: 0.5806 T12: 0.0774 REMARK 3 T13: -0.0993 T23: 0.0671 REMARK 3 L TENSOR REMARK 3 L11: 2.1371 L22: 0.8535 REMARK 3 L33: 2.0419 L12: -0.2756 REMARK 3 L13: 0.1628 L23: 0.6871 REMARK 3 S TENSOR REMARK 3 S11: 0.0869 S12: 0.0524 S13: -0.3203 REMARK 3 S21: 0.0149 S22: -0.0716 S23: -0.1572 REMARK 3 S31: 0.1406 S32: 0.2713 S33: -0.1016 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 87 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.3579 17.5400 -28.9697 REMARK 3 T TENSOR REMARK 3 T11: 0.3112 T22: 0.0632 REMARK 3 T33: 0.4661 T12: -0.1485 REMARK 3 T13: 0.0249 T23: 0.1773 REMARK 3 L TENSOR REMARK 3 L11: 3.7455 L22: 3.0032 REMARK 3 L33: 4.0346 L12: -1.0788 REMARK 3 L13: -0.1355 L23: 1.7050 REMARK 3 S TENSOR REMARK 3 S11: 0.1101 S12: -0.0204 S13: -0.3552 REMARK 3 S21: -0.5671 S22: 0.1833 S23: 0.0623 REMARK 3 S31: 0.3635 S32: 0.0250 S33: -0.1821 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 103 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.6557 24.4051 -9.7628 REMARK 3 T TENSOR REMARK 3 T11: 0.0539 T22: 0.2142 REMARK 3 T33: 0.3472 T12: 0.1033 REMARK 3 T13: 0.1576 T23: 0.3122 REMARK 3 L TENSOR REMARK 3 L11: 7.2011 L22: 4.8928 REMARK 3 L33: 4.3355 L12: 2.3782 REMARK 3 L13: -3.5887 L23: -1.5537 REMARK 3 S TENSOR REMARK 3 S11: 0.1039 S12: -0.5961 S13: -0.1133 REMARK 3 S21: 0.3704 S22: -0.1166 S23: 0.1227 REMARK 3 S31: -0.1056 S32: 0.1588 S33: -0.1493 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 116 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.7675 25.5851 -44.0156 REMARK 3 T TENSOR REMARK 3 T11: 0.3522 T22: 0.1134 REMARK 3 T33: 0.2166 T12: 0.1595 REMARK 3 T13: -0.0127 T23: 0.0038 REMARK 3 L TENSOR REMARK 3 L11: 1.2327 L22: 0.9492 REMARK 3 L33: 1.8129 L12: -0.8037 REMARK 3 L13: -0.6036 L23: -0.3843 REMARK 3 S TENSOR REMARK 3 S11: 0.0216 S12: 0.1112 S13: -0.0670 REMARK 3 S21: -0.2003 S22: -0.0485 S23: -0.0498 REMARK 3 S31: 0.2917 S32: 0.0681 S33: -0.1047 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 137 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.0756 43.5338 -55.5319 REMARK 3 T TENSOR REMARK 3 T11: 0.6729 T22: 0.3339 REMARK 3 T33: 0.2638 T12: 0.3092 REMARK 3 T13: 0.0289 T23: 0.2602 REMARK 3 L TENSOR REMARK 3 L11: 0.9219 L22: 1.2885 REMARK 3 L33: 2.0900 L12: 0.1157 REMARK 3 L13: 0.3959 L23: -0.1497 REMARK 3 S TENSOR REMARK 3 S11: -0.0404 S12: 0.3194 S13: 0.3116 REMARK 3 S21: -0.2611 S22: 0.0994 S23: 0.3485 REMARK 3 S31: -0.3104 S32: -0.1384 S33: -0.0745 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 158 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.4011 38.5571 -47.1815 REMARK 3 T TENSOR REMARK 3 T11: 0.1412 T22: -0.1097 REMARK 3 T33: 0.0963 T12: 0.2925 REMARK 3 T13: -0.0305 T23: 0.1039 REMARK 3 L TENSOR REMARK 3 L11: 1.1230 L22: 0.7618 REMARK 3 L33: 0.7654 L12: 0.2401 REMARK 3 L13: -0.1969 L23: 0.2661 REMARK 3 S TENSOR REMARK 3 S11: 0.2524 S12: 0.1407 S13: 0.0064 REMARK 3 S21: -0.1749 S22: -0.0313 S23: 0.0812 REMARK 3 S31: -0.0920 S32: -0.0750 S33: 0.2877 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 201 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.8416 41.5055 -53.7390 REMARK 3 T TENSOR REMARK 3 T11: 0.6837 T22: 0.3518 REMARK 3 T33: 0.2638 T12: 0.0862 REMARK 3 T13: -0.1126 T23: 0.2072 REMARK 3 L TENSOR REMARK 3 L11: 2.1848 L22: 3.3031 REMARK 3 L33: 1.2504 L12: 1.2594 REMARK 3 L13: -0.6153 L23: -0.4404 REMARK 3 S TENSOR REMARK 3 S11: -0.0187 S12: 0.5060 S13: -0.1262 REMARK 3 S21: -0.2778 S22: -0.2723 S23: -0.4246 REMARK 3 S31: -0.0470 S32: 0.0898 S33: 0.1548 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.5062 33.8212 -25.9523 REMARK 3 T TENSOR REMARK 3 T11: 0.4427 T22: 0.6511 REMARK 3 T33: 0.3407 T12: -0.1569 REMARK 3 T13: -0.1671 T23: 0.2633 REMARK 3 L TENSOR REMARK 3 L11: 7.7915 L22: 3.6405 REMARK 3 L33: 2.3958 L12: 4.1541 REMARK 3 L13: -1.0266 L23: 0.7286 REMARK 3 S TENSOR REMARK 3 S11: 0.0412 S12: 0.0557 S13: -0.4501 REMARK 3 S21: -0.3561 S22: -0.2045 S23: -0.2038 REMARK 3 S31: -0.1604 S32: -0.1141 S33: 0.3633 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 27 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.6971 33.7675 -21.1482 REMARK 3 T TENSOR REMARK 3 T11: -0.0611 T22: 0.0260 REMARK 3 T33: 0.5256 T12: 0.5781 REMARK 3 T13: 0.2363 T23: 0.1912 REMARK 3 L TENSOR REMARK 3 L11: 0.8027 L22: 0.8910 REMARK 3 L33: 0.5102 L12: -0.6478 REMARK 3 L13: -0.1563 L23: 0.2670 REMARK 3 S TENSOR REMARK 3 S11: -0.0300 S12: -0.1056 S13: -0.0338 REMARK 3 S21: 0.0468 S22: 0.1549 S23: 0.2412 REMARK 3 S31: -0.2581 S32: -0.1801 S33: 0.4006 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 115 THROUGH 189 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.2443 37.8490 -54.0852 REMARK 3 T TENSOR REMARK 3 T11: 0.5200 T22: 0.0242 REMARK 3 T33: 0.4012 T12: 0.2129 REMARK 3 T13: -0.2479 T23: 0.3726 REMARK 3 L TENSOR REMARK 3 L11: 0.2701 L22: 0.1363 REMARK 3 L33: 1.1632 L12: -0.0661 REMARK 3 L13: 0.1411 L23: 0.3367 REMARK 3 S TENSOR REMARK 3 S11: 0.0981 S12: 0.2223 S13: -0.0216 REMARK 3 S21: -0.2681 S22: -0.1464 S23: 0.1859 REMARK 3 S31: 0.1738 S32: 0.1692 S33: 0.0131 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 190 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.7859 42.9726 -60.7789 REMARK 3 T TENSOR REMARK 3 T11: 1.0084 T22: 0.7490 REMARK 3 T33: 0.4544 T12: 0.1276 REMARK 3 T13: -0.3214 T23: 0.1242 REMARK 3 L TENSOR REMARK 3 L11: 3.6601 L22: 2.4061 REMARK 3 L33: 5.1855 L12: -0.9899 REMARK 3 L13: -2.9266 L23: 3.2586 REMARK 3 S TENSOR REMARK 3 S11: 0.6553 S12: 0.4674 S13: 0.1483 REMARK 3 S21: -0.8069 S22: -0.4047 S23: 0.2561 REMARK 3 S31: -0.7567 S32: -0.7078 S33: -0.0693 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 20 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.5354 39.6963 -31.9793 REMARK 3 T TENSOR REMARK 3 T11: 0.5416 T22: 0.5415 REMARK 3 T33: 0.3380 T12: -0.4775 REMARK 3 T13: 0.2106 T23: 0.0558 REMARK 3 L TENSOR REMARK 3 L11: 5.4377 L22: 4.5372 REMARK 3 L33: 4.3407 L12: -2.8820 REMARK 3 L13: -0.1138 L23: 2.4684 REMARK 3 S TENSOR REMARK 3 S11: 0.2512 S12: -0.3336 S13: -0.5433 REMARK 3 S21: 0.6275 S22: -0.3982 S23: 0.3925 REMARK 3 S31: -0.2242 S32: -0.0326 S33: -0.1447 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 21 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): -50.7956 48.6213 -39.4323 REMARK 3 T TENSOR REMARK 3 T11: 0.1920 T22: 0.4443 REMARK 3 T33: 0.1058 T12: -0.0923 REMARK 3 T13: -0.0011 T23: 0.0660 REMARK 3 L TENSOR REMARK 3 L11: 3.4394 L22: 1.9799 REMARK 3 L33: 1.1691 L12: -1.6726 REMARK 3 L13: 0.6096 L23: 0.7899 REMARK 3 S TENSOR REMARK 3 S11: 0.1526 S12: 0.3320 S13: -0.1691 REMARK 3 S21: 0.0576 S22: -0.2933 S23: 0.1933 REMARK 3 S31: -0.1995 S32: -0.3823 S33: -0.0920 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.1605 51.4123 -30.0193 REMARK 3 T TENSOR REMARK 3 T11: -0.0446 T22: 0.1560 REMARK 3 T33: 0.0483 T12: 0.2982 REMARK 3 T13: 0.4147 T23: 0.0247 REMARK 3 L TENSOR REMARK 3 L11: 1.4940 L22: 0.5673 REMARK 3 L33: 0.6056 L12: -0.4185 REMARK 3 L13: -0.4237 L23: 0.2855 REMARK 3 S TENSOR REMARK 3 S11: 0.1184 S12: -0.0397 S13: 0.1727 REMARK 3 S21: -0.0884 S22: 0.0526 S23: -0.1287 REMARK 3 S31: -0.0537 S32: 0.0270 S33: 0.1900 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.6270 45.7756 -38.7898 REMARK 3 T TENSOR REMARK 3 T11: 0.1527 T22: 0.2947 REMARK 3 T33: 0.1498 T12: -0.3278 REMARK 3 T13: 0.2201 T23: -0.1253 REMARK 3 L TENSOR REMARK 3 L11: 3.5052 L22: 0.5259 REMARK 3 L33: 1.8327 L12: -0.3693 REMARK 3 L13: 0.4258 L23: -0.2711 REMARK 3 S TENSOR REMARK 3 S11: 0.0292 S12: 0.1995 S13: 0.0837 REMARK 3 S21: 0.0338 S22: -0.0416 S23: 0.0305 REMARK 3 S31: -0.0195 S32: -0.1179 S33: -0.2376 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.1060 43.9028 -27.6976 REMARK 3 T TENSOR REMARK 3 T11: 0.1781 T22: 0.4490 REMARK 3 T33: 0.3269 T12: -0.1722 REMARK 3 T13: 0.2258 T23: -0.0169 REMARK 3 L TENSOR REMARK 3 L11: 1.9889 L22: 1.4819 REMARK 3 L33: 2.6599 L12: -0.9886 REMARK 3 L13: -1.6319 L23: 1.1686 REMARK 3 S TENSOR REMARK 3 S11: -0.2857 S12: -0.0549 S13: 0.1208 REMARK 3 S21: 0.0158 S22: -0.0485 S23: -0.0945 REMARK 3 S31: 0.5240 S32: 0.1556 S33: -0.1005 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): -53.8593 60.2406 -31.6090 REMARK 3 T TENSOR REMARK 3 T11: 0.6006 T22: 0.5071 REMARK 3 T33: 0.2500 T12: -0.2678 REMARK 3 T13: -0.1376 T23: 0.0100 REMARK 3 L TENSOR REMARK 3 L11: 3.8130 L22: 3.0487 REMARK 3 L33: 4.1097 L12: -0.1572 REMARK 3 L13: 0.5342 L23: 2.1923 REMARK 3 S TENSOR REMARK 3 S11: -0.0950 S12: 0.7751 S13: -0.0215 REMARK 3 S21: -0.7216 S22: -0.1542 S23: 0.0616 REMARK 3 S31: -0.7487 S32: -0.0178 S33: 0.4314 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 116 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): -42.9083 27.9934 -18.0022 REMARK 3 T TENSOR REMARK 3 T11: 0.1996 T22: 0.5399 REMARK 3 T33: 0.0884 T12: -0.1536 REMARK 3 T13: 0.0551 T23: -0.0075 REMARK 3 L TENSOR REMARK 3 L11: 0.7156 L22: 0.7917 REMARK 3 L33: 0.1671 L12: -0.3443 REMARK 3 L13: -0.2793 L23: 0.1474 REMARK 3 S TENSOR REMARK 3 S11: 0.0715 S12: -0.2705 S13: -0.0992 REMARK 3 S21: -0.0430 S22: -0.0586 S23: -0.2042 REMARK 3 S31: 0.1281 S32: -0.0618 S33: -0.0640 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): -48.7535 23.9205 2.9552 REMARK 3 T TENSOR REMARK 3 T11: 0.4695 T22: 0.6592 REMARK 3 T33: 0.1416 T12: 0.0106 REMARK 3 T13: 0.0278 T23: 0.2601 REMARK 3 L TENSOR REMARK 3 L11: 1.2630 L22: 1.8103 REMARK 3 L33: 0.2241 L12: 0.5221 REMARK 3 L13: -0.2862 L23: -0.3034 REMARK 3 S TENSOR REMARK 3 S11: 0.1403 S12: -0.5863 S13: -0.1396 REMARK 3 S21: 0.7101 S22: 0.1022 S23: 0.3023 REMARK 3 S31: 0.0441 S32: 0.0452 S33: -0.1152 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 158 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): -50.7218 26.6539 -6.7701 REMARK 3 T TENSOR REMARK 3 T11: 0.0520 T22: 0.5104 REMARK 3 T33: 0.1629 T12: -0.4460 REMARK 3 T13: 0.0055 T23: 0.3231 REMARK 3 L TENSOR REMARK 3 L11: 0.7961 L22: 0.5025 REMARK 3 L33: 0.4547 L12: 0.1673 REMARK 3 L13: -0.1489 L23: 0.1683 REMARK 3 S TENSOR REMARK 3 S11: 0.0722 S12: -0.0631 S13: -0.1202 REMARK 3 S21: -0.0174 S22: 0.0561 S23: 0.1138 REMARK 3 S31: -0.0018 S32: 0.1015 S33: 0.2217 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 201 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.5115 16.6365 -4.9161 REMARK 3 T TENSOR REMARK 3 T11: 0.4991 T22: 0.7101 REMARK 3 T33: 0.3656 T12: -0.1212 REMARK 3 T13: -0.2447 T23: 0.4345 REMARK 3 L TENSOR REMARK 3 L11: 1.3088 L22: 1.8804 REMARK 3 L33: 1.0258 L12: 0.1200 REMARK 3 L13: -0.6292 L23: 0.5450 REMARK 3 S TENSOR REMARK 3 S11: -0.2475 S12: -0.1312 S13: -0.1898 REMARK 3 S21: 0.4034 S22: 0.2399 S23: 0.0301 REMARK 3 S31: 0.0162 S32: -0.0008 S33: 0.0611 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.7948 59.5198 -9.9488 REMARK 3 T TENSOR REMARK 3 T11: 0.5992 T22: 0.6091 REMARK 3 T33: 0.3223 T12: -0.3063 REMARK 3 T13: -0.3889 T23: -0.0042 REMARK 3 L TENSOR REMARK 3 L11: 2.3891 L22: 3.1560 REMARK 3 L33: 0.6663 L12: 1.3165 REMARK 3 L13: 0.0225 L23: 0.4820 REMARK 3 S TENSOR REMARK 3 S11: -0.0554 S12: -0.2936 S13: -0.0206 REMARK 3 S21: 0.2914 S22: 0.0896 S23: -0.3230 REMARK 3 S31: 0.1114 S32: 0.1665 S33: 0.0323 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 27 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.3861 58.1268 -15.6012 REMARK 3 T TENSOR REMARK 3 T11: 0.7069 T22: 0.2506 REMARK 3 T33: 0.2015 T12: -0.4531 REMARK 3 T13: -0.1506 T23: 0.1634 REMARK 3 L TENSOR REMARK 3 L11: 0.6687 L22: 1.2830 REMARK 3 L33: 0.0538 L12: -0.3135 REMARK 3 L13: 0.1614 L23: -0.1547 REMARK 3 S TENSOR REMARK 3 S11: -0.1012 S12: -0.0730 S13: 0.1806 REMARK 3 S21: 0.3030 S22: -0.1670 S23: -0.0677 REMARK 3 S31: -0.1551 S32: 0.0965 S33: -0.2381 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 115 THROUGH 189 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.8036 31.2298 2.2892 REMARK 3 T TENSOR REMARK 3 T11: 0.5562 T22: 0.8777 REMARK 3 T33: -0.0379 T12: -0.3669 REMARK 3 T13: 0.0091 T23: 0.1742 REMARK 3 L TENSOR REMARK 3 L11: 0.2498 L22: 0.2305 REMARK 3 L33: 0.5251 L12: -0.1219 REMARK 3 L13: -0.0843 L23: 0.2095 REMARK 3 S TENSOR REMARK 3 S11: 0.2038 S12: -0.0935 S13: -0.0032 REMARK 3 S21: 0.0411 S22: 0.0490 S23: -0.1748 REMARK 3 S31: -0.0441 S32: 0.4488 S33: 0.8695 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 190 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.1722 31.2007 12.2540 REMARK 3 T TENSOR REMARK 3 T11: 0.9020 T22: 0.9453 REMARK 3 T33: 0.2984 T12: -0.2449 REMARK 3 T13: -0.0686 T23: 0.2566 REMARK 3 L TENSOR REMARK 3 L11: 3.7946 L22: 6.5996 REMARK 3 L33: 2.8743 L12: -3.5908 REMARK 3 L13: 2.2307 L23: -0.1019 REMARK 3 S TENSOR REMARK 3 S11: -0.1210 S12: -0.4701 S13: -0.1322 REMARK 3 S21: 0.6929 S22: 0.2788 S23: 0.1933 REMARK 3 S31: 0.5106 S32: 0.4273 S33: -0.2796 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "A" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "H" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "B" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "L" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9E7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000289650. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-OCT-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0-6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21022 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 34.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 1.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.11 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 1.44600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM NITRATE, 20% PEG 3,350, REMARK 280 PH 6.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 APPLY THE FOLLOWING TO CHAINS: R, H, L 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, A, B 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 GLU H 1 REMARK 465 ILE H 2 REMARK 465 ASP H 229 REMARK 465 LYS H 230 REMARK 465 THR H 231 REMARK 465 HIS H 232 REMARK 465 THR H 233 REMARK 465 GLU A 1 REMARK 465 ILE A 2 REMARK 465 ASP A 229 REMARK 465 LYS A 230 REMARK 465 THR A 231 REMARK 465 HIS A 232 REMARK 465 THR A 233 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 NE2 GLN A 85 OD1 ASN A 87 2.08 REMARK 500 O PRO L 9 OG1 THR L 103 2.12 REMARK 500 OE1 GLU B 106 OH TYR B 174 2.15 REMARK 500 O2 C R 53 OG SER H 60 2.15 REMARK 500 N2 G C 11 O2 C C 41 2.18 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 G R 39 C4 - N9 - C1' ANGL. DEV. = 8.2 DEGREES REMARK 500 A R 52 C8 - N9 - C4 ANGL. DEV. = -2.9 DEGREES REMARK 500 G C 24 O4' - C1' - N9 ANGL. DEV. = 4.5 DEGREES REMARK 500 G C 24 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES REMARK 500 G C 24 N9 - C4 - C5 ANGL. DEV. = 2.8 DEGREES REMARK 500 SER H 55 C - N - CA ANGL. DEV. = 18.3 DEGREES REMARK 500 CYS L 215 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 SER A 55 C - N - CA ANGL. DEV. = 17.9 DEGREES REMARK 500 CYS B 215 CA - CB - SG ANGL. DEV. = 7.9 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 VAL H 51 -57.52 -123.03 REMARK 500 TYR H 57 -17.24 67.99 REMARK 500 SER H 88 62.51 39.51 REMARK 500 SER H 108 24.13 -141.03 REMARK 500 SER H 139 -176.09 -178.72 REMARK 500 LYS H 141 -7.55 80.23 REMARK 500 THR H 172 -37.42 -132.89 REMARK 500 SER L 31 -120.90 51.53 REMARK 500 ALA L 52 -17.17 65.42 REMARK 500 ALA L 85 -175.57 -176.14 REMARK 500 ASN L 153 -5.50 72.30 REMARK 500 VAL A 51 -53.80 -122.46 REMARK 500 TYR A 57 -19.18 67.57 REMARK 500 SER A 88 62.73 39.36 REMARK 500 SER A 108 32.37 -142.26 REMARK 500 SER A 139 -179.01 -178.33 REMARK 500 LYS A 141 -6.46 81.04 REMARK 500 THR A 172 -38.42 -132.36 REMARK 500 SER B 31 -124.34 52.98 REMARK 500 ALA B 52 -14.31 68.09 REMARK 500 ASN B 153 -4.29 72.84 REMARK 500 REMARK 500 REMARK: NULL DBREF 9E7D R 1 72 GB 902798 U26942.1 7174 7241 DBREF 9E7D C 1 72 GB 902798 U26942.1 7174 7241 DBREF 9E7D H 1 233 PDB 9E7D 9E7D 1 233 DBREF 9E7D L 1 215 PDB 9E7D 9E7D 1 215 DBREF 9E7D A 1 233 PDB 9E7D 9E7D 1 233 DBREF 9E7D B 1 215 PDB 9E7D 9E7D 1 215 SEQADV 9E7D G R 1 GB 902798 A 7174 CONFLICT SEQADV 9E7D C R 31 GB 902798 A 7204 ENGINEERED MUTATION SEQADV 9E7D G R 49 GB 902798 U 7222 CONFLICT SEQADV 9E7D A R 50 GB 902798 U 7223 CONFLICT SEQADV 9E7D A R 52 GB 902798 INSERTION SEQADV 9E7D C R 53 GB 902798 INSERTION SEQADV 9E7D A R 54 GB 902798 INSERTION SEQADV 9E7D C R 55 GB 902798 INSERTION SEQADV 9E7D C R 72 GB 902798 A 7241 CONFLICT SEQADV 9E7D G C 1 GB 902798 A 7174 CONFLICT SEQADV 9E7D C C 31 GB 902798 A 7204 ENGINEERED MUTATION SEQADV 9E7D G C 49 GB 902798 U 7222 CONFLICT SEQADV 9E7D A C 50 GB 902798 U 7223 CONFLICT SEQADV 9E7D A C 52 GB 902798 INSERTION SEQADV 9E7D C C 53 GB 902798 INSERTION SEQADV 9E7D A C 54 GB 902798 INSERTION SEQADV 9E7D C C 55 GB 902798 INSERTION SEQADV 9E7D C C 72 GB 902798 A 7241 CONFLICT SEQRES 1 R 72 G G C A C U A U G G G C G SEQRES 2 R 72 C A G C G U C A A U G A C SEQRES 3 R 72 G C U G C C G G U A C A G SEQRES 4 R 72 G C C A G A C A A G A A A SEQRES 5 R 72 C A C U U G U C U G A U A SEQRES 6 R 72 U A G U G C C SEQRES 1 C 72 G G C A C U A U G G G C G SEQRES 2 C 72 C A G C G U C A A U G A C SEQRES 3 C 72 G C U G C C G G U A C A G SEQRES 4 C 72 G C C A G A C A A G A A A SEQRES 5 C 72 C A C U U G U C U G A U A SEQRES 6 C 72 U A G U G C C SEQRES 1 H 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 233 ALA SER GLY PHE TYR ILE SER TYR SER SER ILE HIS TRP SEQRES 4 H 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 233 SER ILE SER PRO TYR SER GLY SER THR TYR TYR ALA ASP SEQRES 6 H 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLN GLY TYR SEQRES 9 H 233 ARG ARG ARG SER GLY ARG GLY PHE ASP TYR TRP GLY GLN SEQRES 10 H 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 L 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 215 SER TYR SER PHE PRO SER THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL 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 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 A 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 A 233 ALA SER GLY PHE TYR ILE SER TYR SER SER ILE HIS TRP SEQRES 4 A 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 A 233 SER ILE SER PRO TYR SER GLY SER THR TYR TYR ALA ASP SEQRES 6 A 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 A 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 A 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLN GLY TYR SEQRES 9 A 233 ARG ARG ARG SER GLY ARG GLY PHE ASP TYR TRP GLY GLN SEQRES 10 A 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 A 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 B 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 B 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 B 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 B 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 B 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 B 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 B 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 B 215 SER TYR SER PHE PRO SER THR PHE GLY GLN GLY THR LYS SEQRES 9 B 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS HELIX 1 AA1 TYR H 31 SER H 35 5 5 HELIX 2 AA2 ASP H 65 LYS H 68 5 4 HELIX 3 AA3 THR H 77 LYS H 79 5 3 HELIX 4 AA4 ARG H 90 THR H 94 5 5 HELIX 5 AA5 TYR H 104 GLY H 109 1 6 HELIX 6 AA6 SER H 199 LEU H 201 5 3 HELIX 7 AA7 LYS H 213 ASN H 216 5 4 HELIX 8 AA8 GLN L 80 PHE L 84 5 5 HELIX 9 AA9 SER L 122 SER L 128 1 7 HELIX 10 AB1 LYS L 184 LYS L 189 1 6 HELIX 11 AB2 TYR A 31 SER A 35 5 5 HELIX 12 AB3 ASP A 65 LYS A 68 5 4 HELIX 13 AB4 ARG A 90 THR A 94 5 5 HELIX 14 AB5 TYR A 104 GLY A 109 1 6 HELIX 15 AB6 SER A 199 GLY A 202 5 4 HELIX 16 AB7 LYS A 213 ASN A 216 5 4 HELIX 17 AB8 GLN B 80 PHE B 84 5 5 HELIX 18 AB9 SER B 122 SER B 128 1 7 HELIX 19 AC1 LYS B 184 LYS B 189 1 6 SHEET 1 AA1 4 GLN H 6 SER H 10 0 SHEET 2 AA1 4 LEU H 21 SER H 28 -1 O SER H 28 N GLN H 6 SHEET 3 AA1 4 THR H 81 MET H 86 -1 O LEU H 84 N LEU H 23 SHEET 4 AA1 4 THR H 72 ASP H 76 -1 N THR H 72 O GLN H 85 SHEET 1 AA2 6 LEU H 14 VAL H 15 0 SHEET 2 AA2 6 THR H 119 VAL H 123 1 O THR H 122 N VAL H 15 SHEET 3 AA2 6 ALA H 95 GLN H 102 -1 N ALA H 95 O VAL H 121 SHEET 4 AA2 6 ILE H 37 GLN H 42 -1 N VAL H 40 O TYR H 98 SHEET 5 AA2 6 LEU H 48 ILE H 54 -1 O GLU H 49 N ARG H 41 SHEET 6 AA2 6 THR H 61 TYR H 63 -1 O TYR H 62 N SER H 53 SHEET 1 AA3 4 LEU H 14 VAL H 15 0 SHEET 2 AA3 4 THR H 119 VAL H 123 1 O THR H 122 N VAL H 15 SHEET 3 AA3 4 ALA H 95 GLN H 102 -1 N ALA H 95 O VAL H 121 SHEET 4 AA3 4 PHE H 112 TRP H 115 -1 O TYR H 114 N ARG H 101 SHEET 1 AA4 4 SER H 132 LEU H 136 0 SHEET 2 AA4 4 THR H 147 TYR H 157 -1 O LYS H 155 N SER H 132 SHEET 3 AA4 4 TYR H 188 PRO H 197 -1 O LEU H 190 N VAL H 154 SHEET 4 AA4 4 VAL H 175 THR H 177 -1 N HIS H 176 O VAL H 193 SHEET 1 AA5 4 THR H 143 SER H 144 0 SHEET 2 AA5 4 THR H 147 TYR H 157 -1 O THR H 147 N SER H 144 SHEET 3 AA5 4 TYR H 188 PRO H 197 -1 O LEU H 190 N VAL H 154 SHEET 4 AA5 4 VAL H 181 LEU H 182 -1 N VAL H 181 O SER H 189 SHEET 1 AA6 3 THR H 163 TRP H 166 0 SHEET 2 AA6 3 TYR H 206 HIS H 212 -1 O ASN H 211 N THR H 163 SHEET 3 AA6 3 THR H 217 VAL H 223 -1 O VAL H 219 N VAL H 210 SHEET 1 AA7 4 MET L 5 SER L 8 0 SHEET 2 AA7 4 VAL L 20 ALA L 26 -1 O THR L 23 N SER L 8 SHEET 3 AA7 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AA7 4 PHE L 63 SER L 64 -1 N SER L 64 O THR L 75 SHEET 1 AA8 4 MET L 5 SER L 8 0 SHEET 2 AA8 4 VAL L 20 ALA L 26 -1 O THR L 23 N SER L 8 SHEET 3 AA8 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AA8 4 ARG L 67 SER L 68 -1 N SER L 68 O ASP L 71 SHEET 1 AA9 5 SER L 11 ALA L 14 0 SHEET 2 AA9 5 THR L 103 ILE L 107 1 O LYS L 104 N LEU L 12 SHEET 3 AA9 5 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA9 5 VAL L 34 GLN L 39 -1 N GLN L 39 O THR L 86 SHEET 5 AA9 5 LYS L 46 LEU L 47 -1 O LYS L 46 N GLN L 38 SHEET 1 AB1 4 SER L 11 ALA L 14 0 SHEET 2 AB1 4 THR L 103 ILE L 107 1 O LYS L 104 N LEU L 12 SHEET 3 AB1 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AB1 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AB2 2 ILE L 49 TYR L 50 0 SHEET 2 AB2 2 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AB3 4 SER L 115 PHE L 119 0 SHEET 2 AB3 4 THR L 130 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AB3 4 TYR L 174 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AB3 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB4 4 ALA L 154 LEU L 155 0 SHEET 2 AB4 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB4 4 VAL L 192 THR L 198 -1 O ALA L 194 N LYS L 150 SHEET 4 AB4 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AB5 4 GLN A 6 SER A 10 0 SHEET 2 AB5 4 LEU A 21 SER A 28 -1 O SER A 28 N GLN A 6 SHEET 3 AB5 4 THR A 81 MET A 86 -1 O LEU A 84 N LEU A 23 SHEET 4 AB5 4 PHE A 71 ASP A 76 -1 N ASP A 76 O THR A 81 SHEET 1 AB6 6 GLY A 13 VAL A 15 0 SHEET 2 AB6 6 THR A 119 VAL A 123 1 O THR A 122 N GLY A 13 SHEET 3 AB6 6 ALA A 95 GLN A 102 -1 N ALA A 95 O VAL A 121 SHEET 4 AB6 6 ILE A 37 GLN A 42 -1 N GLN A 42 O VAL A 96 SHEET 5 AB6 6 LEU A 48 ILE A 54 -1 O GLU A 49 N ARG A 41 SHEET 6 AB6 6 THR A 61 TYR A 63 -1 O TYR A 62 N SER A 53 SHEET 1 AB7 4 GLY A 13 VAL A 15 0 SHEET 2 AB7 4 THR A 119 VAL A 123 1 O THR A 122 N GLY A 13 SHEET 3 AB7 4 ALA A 95 GLN A 102 -1 N ALA A 95 O VAL A 121 SHEET 4 AB7 4 PHE A 112 TRP A 115 -1 O TYR A 114 N ARG A 101 SHEET 1 AB8 4 SER A 132 LEU A 136 0 SHEET 2 AB8 4 THR A 147 TYR A 157 -1 O LYS A 155 N SER A 132 SHEET 3 AB8 4 TYR A 188 PRO A 197 -1 O LEU A 190 N VAL A 154 SHEET 4 AB8 4 VAL A 175 THR A 177 -1 N HIS A 176 O VAL A 193 SHEET 1 AB9 4 THR A 143 SER A 144 0 SHEET 2 AB9 4 THR A 147 TYR A 157 -1 O THR A 147 N SER A 144 SHEET 3 AB9 4 TYR A 188 PRO A 197 -1 O LEU A 190 N VAL A 154 SHEET 4 AB9 4 VAL A 181 LEU A 182 -1 N VAL A 181 O SER A 189 SHEET 1 AC1 3 THR A 163 TRP A 166 0 SHEET 2 AC1 3 ILE A 207 HIS A 212 -1 O ASN A 209 N SER A 165 SHEET 3 AC1 3 THR A 217 LYS A 222 -1 O VAL A 219 N VAL A 210 SHEET 1 AC2 4 MET B 5 SER B 8 0 SHEET 2 AC2 4 VAL B 20 ALA B 26 -1 O THR B 23 N SER B 8 SHEET 3 AC2 4 ASP B 71 ILE B 76 -1 O PHE B 72 N CYS B 24 SHEET 4 AC2 4 PHE B 63 SER B 68 -1 N SER B 68 O ASP B 71 SHEET 1 AC3 6 SER B 11 ALA B 14 0 SHEET 2 AC3 6 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 12 SHEET 3 AC3 6 THR B 86 GLN B 91 -1 N TYR B 87 O THR B 103 SHEET 4 AC3 6 VAL B 34 GLN B 39 -1 N GLN B 39 O THR B 86 SHEET 5 AC3 6 LYS B 46 TYR B 50 -1 O LEU B 48 N TRP B 36 SHEET 6 AC3 6 SER B 54 LEU B 55 -1 O SER B 54 N TYR B 50 SHEET 1 AC4 4 SER B 11 ALA B 14 0 SHEET 2 AC4 4 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 12 SHEET 3 AC4 4 THR B 86 GLN B 91 -1 N TYR B 87 O THR B 103 SHEET 4 AC4 4 THR B 98 PHE B 99 -1 O THR B 98 N GLN B 91 SHEET 1 AC5 4 SER B 115 PHE B 119 0 SHEET 2 AC5 4 THR B 130 PHE B 140 -1 O VAL B 134 N PHE B 119 SHEET 3 AC5 4 TYR B 174 SER B 183 -1 O LEU B 182 N ALA B 131 SHEET 4 AC5 4 SER B 160 VAL B 164 -1 N GLN B 161 O THR B 179 SHEET 1 AC6 4 ALA B 154 LEU B 155 0 SHEET 2 AC6 4 LYS B 146 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AC6 4 VAL B 192 THR B 198 -1 O ALA B 194 N LYS B 150 SHEET 4 AC6 4 VAL B 206 ASN B 211 -1 O VAL B 206 N VAL B 197 SSBOND 1 CYS H 25 CYS H 99 1555 1555 2.07 SSBOND 2 CYS H 152 CYS H 208 1555 1555 2.02 SSBOND 3 CYS L 24 CYS L 89 1555 1555 2.06 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.05 SSBOND 5 CYS A 25 CYS A 99 1555 1555 2.08 SSBOND 6 CYS A 152 CYS A 208 1555 1555 2.02 SSBOND 7 CYS B 24 CYS B 89 1555 1555 2.07 SSBOND 8 CYS B 135 CYS B 195 1555 1555 2.03 CISPEP 1 PHE H 158 PRO H 159 0 -0.53 CISPEP 2 GLU H 160 PRO H 161 0 -3.31 CISPEP 3 SER L 8 PRO L 9 0 -2.98 CISPEP 4 PHE L 95 PRO L 96 0 -1.02 CISPEP 5 TYR L 141 PRO L 142 0 2.00 CISPEP 6 PHE A 158 PRO A 159 0 -3.68 CISPEP 7 GLU A 160 PRO A 161 0 -1.39 CISPEP 8 SER B 8 PRO B 9 0 -1.10 CISPEP 9 PHE B 95 PRO B 96 0 1.31 CISPEP 10 TYR B 141 PRO B 142 0 -0.69 CRYST1 72.874 75.871 83.516 63.17 71.85 77.75 P 1 2 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 0.013722 -0.002979 -0.003585 0.00000 SCALE2 0.000000 0.013487 -0.006150 0.00000 SCALE3 0.000000 0.000000 0.013849 0.00000 MTRIX1 1 -0.409132 -0.766828 -0.494556 0.77247 1 MTRIX2 1 -0.759280 -0.014492 0.650602 5.00105 1 MTRIX3 1 -0.506067 0.641689 -0.576308 -93.87157 1 MTRIX1 2 -0.402747 -0.768307 -0.497492 1.07667 1 MTRIX2 2 -0.762444 -0.019121 0.646771 5.04060 1 MTRIX3 2 -0.506432 0.639795 -0.578091 -93.92321 1