HEADER SPLICING/IMMUNE SYSTEM 13-MAR-24 8YOR TITLE COMPLEX OF HARSWHEP AND A-HARSWHEP FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: A-HARSWHEP FAB-LIGHT CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: A-HARSWHEP FAB-HEAVY CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HISTIDINE--TRNA LIGASE, CYTOPLASMIC; COMPND 11 CHAIN: E, F; COMPND 12 SYNONYM: HISTIDYL-TRNA SYNTHETASE,HISRS,HARSWHEP; COMPND 13 EC: 6.1.1.21; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: HARS1, HARS, HRS; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NRP2, LUNG INFLAMMATION, HIS-TRNA SYNTHETASE SPLICE VARIANT, KEYWDS 2 SPLICING, SPLICING-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR L.ZHAI REVDAT 1 12-FEB-25 8YOR 0 JRNL AUTH Z.LITING,X.ZHIWEN JRNL TITL HUMAN HARS SPLICE VARIANT THERAPEUTIC TARGETS NRP2 TO JRNL TITL 2 SUPPRESS LUNG INFLAMMATION AND FIBROSIS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 89.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 3 NUMBER OF REFLECTIONS : 59716 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.229 REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.273 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 2974 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 10.0000 - 6.3448 0.95 2742 131 0.2413 0.2460 REMARK 3 2 6.3448 - 5.0362 0.98 2785 133 0.2114 0.2290 REMARK 3 3 5.0362 - 4.3996 0.99 2766 146 0.1769 0.2095 REMARK 3 4 4.3996 - 3.9974 0.92 2594 113 0.1797 0.2342 REMARK 3 5 3.9974 - 3.7108 0.95 2703 113 0.2023 0.2319 REMARK 3 6 3.7108 - 3.4920 0.98 2711 148 0.2073 0.2702 REMARK 3 7 3.4920 - 3.3172 0.98 2703 170 0.2137 0.2754 REMARK 3 8 3.3172 - 3.1728 0.98 2744 149 0.2278 0.2780 REMARK 3 9 3.1728 - 3.0506 0.99 2732 157 0.2379 0.2836 REMARK 3 10 3.0506 - 2.9453 0.99 2759 137 0.2471 0.2888 REMARK 3 11 2.9453 - 2.8532 0.98 2727 161 0.2522 0.3112 REMARK 3 12 2.8532 - 2.7717 0.92 2529 152 0.2644 0.3311 REMARK 3 13 2.7717 - 2.6987 0.92 2569 130 0.2514 0.3256 REMARK 3 14 2.6987 - 2.6329 0.97 2731 124 0.2539 0.3136 REMARK 3 15 2.6329 - 2.5730 0.97 2721 132 0.2619 0.3020 REMARK 3 16 2.5730 - 2.5182 0.97 2697 142 0.2646 0.3259 REMARK 3 17 2.5182 - 2.4679 0.98 2688 152 0.2684 0.3066 REMARK 3 18 2.4679 - 2.4213 0.98 2727 127 0.2776 0.3023 REMARK 3 19 2.4213 - 2.3780 0.97 2708 161 0.2865 0.3380 REMARK 3 20 2.3780 - 2.3377 0.98 2716 137 0.2954 0.3827 REMARK 3 21 2.3377 - 2.3000 0.98 2690 159 0.2767 0.3201 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) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.640 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 7516 REMARK 3 ANGLE : 0.641 10193 REMARK 3 CHIRALITY : 0.023 1154 REMARK 3 PLANARITY : 0.004 1308 REMARK 3 DIHEDRAL : 11.105 2725 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 33 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 24 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.2068 -12.0388 -31.9561 REMARK 3 T TENSOR REMARK 3 T11: 0.4310 T22: 0.4376 REMARK 3 T33: 0.2316 T12: -0.0259 REMARK 3 T13: 0.0763 T23: 0.0680 REMARK 3 L TENSOR REMARK 3 L11: 6.2026 L22: 1.6652 REMARK 3 L33: 2.1822 L12: 1.5953 REMARK 3 L13: 0.0556 L23: 0.6576 REMARK 3 S TENSOR REMARK 3 S11: -0.0473 S12: -0.7513 S13: 0.0735 REMARK 3 S21: 0.3335 S22: 0.0160 S23: 0.1909 REMARK 3 S31: -0.0481 S32: -0.1900 S33: -0.0710 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.7174 -20.3236 -38.4382 REMARK 3 T TENSOR REMARK 3 T11: 0.3694 T22: 0.3679 REMARK 3 T33: 0.2145 T12: -0.0461 REMARK 3 T13: 0.0260 T23: 0.0657 REMARK 3 L TENSOR REMARK 3 L11: 1.7729 L22: 1.5668 REMARK 3 L33: 1.2470 L12: 0.2677 REMARK 3 L13: 0.0438 L23: 0.1048 REMARK 3 S TENSOR REMARK 3 S11: 0.0855 S12: -0.3352 S13: -0.0936 REMARK 3 S21: 0.3679 S22: -0.0475 S23: 0.0267 REMARK 3 S31: 0.1296 S32: -0.1994 S33: -0.0376 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.7622 0.1121 -35.1738 REMARK 3 T TENSOR REMARK 3 T11: 0.3856 T22: 0.2866 REMARK 3 T33: 0.1915 T12: -0.0689 REMARK 3 T13: -0.0006 T23: -0.0419 REMARK 3 L TENSOR REMARK 3 L11: 4.6046 L22: 6.5830 REMARK 3 L33: 0.0017 L12: 5.3429 REMARK 3 L13: -0.0484 L23: -0.0744 REMARK 3 S TENSOR REMARK 3 S11: 0.1275 S12: -0.5551 S13: -0.0705 REMARK 3 S21: 0.1234 S22: -0.2322 S23: -0.2251 REMARK 3 S31: -0.4820 S32: -0.0617 S33: 0.1031 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 153 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.2828 16.9983 -49.7026 REMARK 3 T TENSOR REMARK 3 T11: 0.4020 T22: 0.2411 REMARK 3 T33: 0.4018 T12: 0.0379 REMARK 3 T13: -0.0746 T23: -0.1368 REMARK 3 L TENSOR REMARK 3 L11: 2.0852 L22: 3.3521 REMARK 3 L33: 2.3359 L12: -0.0278 REMARK 3 L13: 1.1739 L23: -1.2451 REMARK 3 S TENSOR REMARK 3 S11: -0.0958 S12: -0.2364 S13: 0.5201 REMARK 3 S21: 0.0609 S22: -0.0413 S23: 0.0844 REMARK 3 S31: -0.3623 S32: -0.3351 S33: 0.1167 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 154 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.1522 17.9326 -48.0384 REMARK 3 T TENSOR REMARK 3 T11: 0.4789 T22: 0.3310 REMARK 3 T33: 0.4456 T12: 0.0492 REMARK 3 T13: -0.0929 T23: -0.1697 REMARK 3 L TENSOR REMARK 3 L11: 1.8620 L22: 0.3014 REMARK 3 L33: 2.2066 L12: 0.6313 REMARK 3 L13: -0.0439 L23: 0.1580 REMARK 3 S TENSOR REMARK 3 S11: -0.1820 S12: -0.2001 S13: 0.6262 REMARK 3 S21: 0.2605 S22: -0.0311 S23: 0.0996 REMARK 3 S31: -0.5321 S32: -0.2029 S33: 0.2112 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 201 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.7676 22.8278 -43.9327 REMARK 3 T TENSOR REMARK 3 T11: 0.5783 T22: 0.3293 REMARK 3 T33: 0.6106 T12: -0.0270 REMARK 3 T13: -0.1454 T23: -0.1089 REMARK 3 L TENSOR REMARK 3 L11: 3.9473 L22: 5.6582 REMARK 3 L33: 6.9091 L12: -1.0348 REMARK 3 L13: 3.3471 L23: -2.8176 REMARK 3 S TENSOR REMARK 3 S11: -0.2804 S12: 0.1500 S13: 1.0408 REMARK 3 S21: 0.0294 S22: -0.6229 S23: 0.0880 REMARK 3 S31: -0.9200 S32: 0.6423 S33: 0.8479 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.6557 -18.9733 -60.5925 REMARK 3 T TENSOR REMARK 3 T11: 0.1936 T22: 0.2644 REMARK 3 T33: 0.1760 T12: -0.0164 REMARK 3 T13: -0.0156 T23: 0.0468 REMARK 3 L TENSOR REMARK 3 L11: 0.4219 L22: 5.3180 REMARK 3 L33: 0.7442 L12: -1.0451 REMARK 3 L13: -0.1162 L23: -0.3330 REMARK 3 S TENSOR REMARK 3 S11: 0.1290 S12: 0.2481 S13: 0.0261 REMARK 3 S21: -0.2811 S22: -0.1805 S23: -0.0781 REMARK 3 S31: -0.0138 S32: -0.0382 S33: 0.0586 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.9588 -19.8183 -54.1206 REMARK 3 T TENSOR REMARK 3 T11: 0.2125 T22: 0.3410 REMARK 3 T33: 0.2973 T12: -0.0288 REMARK 3 T13: 0.0218 T23: 0.1095 REMARK 3 L TENSOR REMARK 3 L11: 2.4502 L22: 3.3347 REMARK 3 L33: 3.2351 L12: -0.2841 REMARK 3 L13: 0.0808 L23: 1.6892 REMARK 3 S TENSOR REMARK 3 S11: -0.1659 S12: -0.1367 S13: 0.0871 REMARK 3 S21: 0.2188 S22: 0.1394 S23: 0.4072 REMARK 3 S31: 0.1124 S32: -0.4513 S33: 0.0351 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 74 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.2754 -15.6130 -59.6111 REMARK 3 T TENSOR REMARK 3 T11: 0.2032 T22: 0.3146 REMARK 3 T33: 0.2190 T12: -0.0488 REMARK 3 T13: 0.0297 T23: 0.0397 REMARK 3 L TENSOR REMARK 3 L11: 2.2072 L22: 5.6227 REMARK 3 L33: 1.1293 L12: -1.1503 REMARK 3 L13: -0.0491 L23: 0.1059 REMARK 3 S TENSOR REMARK 3 S11: -0.2232 S12: -0.1450 S13: -0.1389 REMARK 3 S21: 0.0613 S22: 0.1288 S23: 0.6033 REMARK 3 S31: -0.1060 S32: -0.1481 S33: 0.1080 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 99 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.9779 -11.5803 -56.5374 REMARK 3 T TENSOR REMARK 3 T11: 0.2597 T22: 0.2847 REMARK 3 T33: 0.2646 T12: 0.0073 REMARK 3 T13: 0.0494 T23: 0.0534 REMARK 3 L TENSOR REMARK 3 L11: 0.7273 L22: 0.7918 REMARK 3 L33: 0.4303 L12: 0.0485 REMARK 3 L13: 0.1205 L23: 0.4747 REMARK 3 S TENSOR REMARK 3 S11: -0.1117 S12: -0.0196 S13: 0.0327 REMARK 3 S21: 0.0936 S22: 0.2039 S23: 0.1354 REMARK 3 S31: -0.0132 S32: -0.1632 S33: -0.0971 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 134 THROUGH 154 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.9616 14.8628 -55.2387 REMARK 3 T TENSOR REMARK 3 T11: 0.3273 T22: 0.2995 REMARK 3 T33: 0.4804 T12: 0.0060 REMARK 3 T13: -0.0415 T23: -0.1206 REMARK 3 L TENSOR REMARK 3 L11: 0.5792 L22: 3.9010 REMARK 3 L33: 3.1721 L12: -0.8326 REMARK 3 L13: -0.7936 L23: -1.2537 REMARK 3 S TENSOR REMARK 3 S11: -0.5571 S12: -0.2621 S13: 1.7101 REMARK 3 S21: 0.0721 S22: -0.0148 S23: -0.2980 REMARK 3 S31: -0.7256 S32: 0.5933 S33: 0.6247 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 155 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.9151 6.1239 -59.0062 REMARK 3 T TENSOR REMARK 3 T11: 0.3223 T22: 0.2179 REMARK 3 T33: 0.2602 T12: -0.0128 REMARK 3 T13: -0.0093 T23: -0.0597 REMARK 3 L TENSOR REMARK 3 L11: 4.7291 L22: 0.3032 REMARK 3 L33: 1.5692 L12: -0.2512 REMARK 3 L13: 1.1072 L23: -0.7141 REMARK 3 S TENSOR REMARK 3 S11: -0.0250 S12: -0.0352 S13: 0.0921 REMARK 3 S21: -0.0689 S22: 0.1060 S23: -0.0522 REMARK 3 S31: -0.0536 S32: 0.0600 S33: -0.0717 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 213 THROUGH 224 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.2261 11.7847 -66.6419 REMARK 3 T TENSOR REMARK 3 T11: 0.4635 T22: 0.3684 REMARK 3 T33: 0.4107 T12: -0.0581 REMARK 3 T13: -0.0720 T23: 0.0732 REMARK 3 L TENSOR REMARK 3 L11: 5.1738 L22: 1.8569 REMARK 3 L33: 4.6697 L12: -1.1909 REMARK 3 L13: 1.7931 L23: 1.2512 REMARK 3 S TENSOR REMARK 3 S11: -0.2187 S12: 0.7379 S13: 0.9769 REMARK 3 S21: -0.5990 S22: 0.1810 S23: -0.6531 REMARK 3 S31: -0.8216 S32: 0.4546 S33: -0.0786 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 11 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.1164 -45.5206 -52.5608 REMARK 3 T TENSOR REMARK 3 T11: 0.7407 T22: 0.5912 REMARK 3 T33: 0.4291 T12: -0.1823 REMARK 3 T13: -0.1350 T23: 0.1061 REMARK 3 L TENSOR REMARK 3 L11: 7.0017 L22: 9.5321 REMARK 3 L33: 3.1788 L12: -5.2176 REMARK 3 L13: 0.6014 L23: 0.2136 REMARK 3 S TENSOR REMARK 3 S11: 0.6191 S12: 0.9828 S13: -0.7753 REMARK 3 S21: -1.1565 S22: -0.6620 S23: 0.7567 REMARK 3 S31: 0.8772 S32: -0.1484 S33: -0.0183 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 31 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.6206 -42.1271 -43.8822 REMARK 3 T TENSOR REMARK 3 T11: 0.5658 T22: 0.4388 REMARK 3 T33: 0.4125 T12: -0.1757 REMARK 3 T13: -0.0028 T23: 0.1366 REMARK 3 L TENSOR REMARK 3 L11: 3.3516 L22: 3.7279 REMARK 3 L33: 2.9600 L12: -1.6504 REMARK 3 L13: -0.1738 L23: 0.4112 REMARK 3 S TENSOR REMARK 3 S11: -0.0294 S12: -0.6544 S13: -0.4163 REMARK 3 S21: -0.1075 S22: 0.2773 S23: 0.5742 REMARK 3 S31: 0.2474 S32: 0.0555 S33: -0.1222 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.4286 -6.9023 -36.5324 REMARK 3 T TENSOR REMARK 3 T11: 0.4812 T22: 0.5540 REMARK 3 T33: 0.3168 T12: -0.1724 REMARK 3 T13: -0.0755 T23: -0.0166 REMARK 3 L TENSOR REMARK 3 L11: 2.4903 L22: 1.5030 REMARK 3 L33: 0.7465 L12: 0.1796 REMARK 3 L13: 0.4130 L23: -0.4800 REMARK 3 S TENSOR REMARK 3 S11: 0.3001 S12: -0.8311 S13: -0.0448 REMARK 3 S21: 0.6140 S22: -0.2435 S23: -0.2671 REMARK 3 S31: -0.5470 S32: 0.5513 S33: -0.1006 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 52 THROUGH 93 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.5748 -5.3178 -36.4190 REMARK 3 T TENSOR REMARK 3 T11: 0.5731 T22: 0.5855 REMARK 3 T33: 0.2780 T12: -0.1739 REMARK 3 T13: -0.0379 T23: -0.0230 REMARK 3 L TENSOR REMARK 3 L11: 1.4681 L22: 1.1110 REMARK 3 L33: 0.1769 L12: 0.6866 REMARK 3 L13: 0.3180 L23: 0.3592 REMARK 3 S TENSOR REMARK 3 S11: 0.2462 S12: -0.5930 S13: -0.0234 REMARK 3 S21: 0.6253 S22: -0.1790 S23: -0.1152 REMARK 3 S31: -0.3569 S32: 0.5161 S33: -0.0361 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 94 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.2322 -13.8541 -38.3188 REMARK 3 T TENSOR REMARK 3 T11: 0.4048 T22: 0.5315 REMARK 3 T33: 0.2166 T12: -0.0632 REMARK 3 T13: -0.0815 T23: 0.0498 REMARK 3 L TENSOR REMARK 3 L11: 1.9026 L22: 0.8869 REMARK 3 L33: 1.9551 L12: 0.0382 REMARK 3 L13: 0.3284 L23: 0.8183 REMARK 3 S TENSOR REMARK 3 S11: 0.3844 S12: -0.9802 S13: -0.0137 REMARK 3 S21: 0.5474 S22: -0.4063 S23: -0.0047 REMARK 3 S31: -0.1672 S32: 0.4051 S33: 0.0340 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 117 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.2184 -45.1204 -57.8034 REMARK 3 T TENSOR REMARK 3 T11: 0.5796 T22: 0.2798 REMARK 3 T33: 1.0299 T12: -0.0429 REMARK 3 T13: 0.1229 T23: 0.0744 REMARK 3 L TENSOR REMARK 3 L11: 4.5088 L22: 1.5050 REMARK 3 L33: 3.9491 L12: -0.5696 REMARK 3 L13: -2.1560 L23: -0.0017 REMARK 3 S TENSOR REMARK 3 S11: 0.0814 S12: 0.4167 S13: -1.0802 REMARK 3 S21: -0.0424 S22: -0.1898 S23: -0.3457 REMARK 3 S31: 0.7281 S32: -0.0216 S33: 0.2048 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 132 THROUGH 153 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.7396 -39.1991 -43.8085 REMARK 3 T TENSOR REMARK 3 T11: 0.5043 T22: 0.4658 REMARK 3 T33: 0.7691 T12: 0.0368 REMARK 3 T13: 0.0470 T23: 0.2916 REMARK 3 L TENSOR REMARK 3 L11: 1.8350 L22: 2.4145 REMARK 3 L33: 3.0014 L12: -0.8520 REMARK 3 L13: 0.2659 L23: 2.0167 REMARK 3 S TENSOR REMARK 3 S11: 0.0389 S12: -0.8034 S13: -1.1686 REMARK 3 S21: 0.0314 S22: -0.0733 S23: -0.7043 REMARK 3 S31: 0.3776 S32: 0.4762 S33: 0.0085 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 154 THROUGH 166 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.2336 -45.5445 -45.9123 REMARK 3 T TENSOR REMARK 3 T11: 0.6585 T22: 0.6647 REMARK 3 T33: 1.1648 T12: 0.1184 REMARK 3 T13: -0.1195 T23: 0.3999 REMARK 3 L TENSOR REMARK 3 L11: 0.0010 L22: 3.0699 REMARK 3 L33: 0.2579 L12: 0.1345 REMARK 3 L13: 0.0247 L23: -0.1277 REMARK 3 S TENSOR REMARK 3 S11: 0.2210 S12: -0.4091 S13: -1.5881 REMARK 3 S21: 0.4878 S22: 0.0280 S23: -0.8002 REMARK 3 S31: 0.7461 S32: 0.1567 S33: 0.0550 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 167 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.9212 -41.1019 -47.7255 REMARK 3 T TENSOR REMARK 3 T11: 0.4821 T22: 0.3956 REMARK 3 T33: 0.7313 T12: 0.0277 REMARK 3 T13: 0.0392 T23: 0.1936 REMARK 3 L TENSOR REMARK 3 L11: 1.6016 L22: 3.8682 REMARK 3 L33: 3.8157 L12: -0.5658 REMARK 3 L13: -0.0271 L23: 1.7661 REMARK 3 S TENSOR REMARK 3 S11: -0.0419 S12: -0.2644 S13: -0.7662 REMARK 3 S21: 0.5388 S22: 0.0818 S23: -0.4279 REMARK 3 S31: 0.9852 S32: 0.1701 S33: -0.0249 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 202 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.1595 -48.2019 -44.0016 REMARK 3 T TENSOR REMARK 3 T11: 0.8673 T22: 0.4134 REMARK 3 T33: 1.1352 T12: -0.1254 REMARK 3 T13: 0.1031 T23: 0.3886 REMARK 3 L TENSOR REMARK 3 L11: 2.7462 L22: 3.9329 REMARK 3 L33: 2.8863 L12: 0.3464 REMARK 3 L13: -0.6812 L23: 1.7791 REMARK 3 S TENSOR REMARK 3 S11: -0.1611 S12: 0.0633 S13: -1.3964 REMARK 3 S21: 0.1782 S22: 0.0610 S23: -0.2977 REMARK 3 S31: 1.1072 S32: -0.2012 S33: 0.2383 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 12 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.4219 28.0570 -54.5824 REMARK 3 T TENSOR REMARK 3 T11: 1.3066 T22: 0.7529 REMARK 3 T33: 0.7891 T12: -0.2490 REMARK 3 T13: 0.0862 T23: -0.1645 REMARK 3 L TENSOR REMARK 3 L11: 0.4007 L22: 0.2263 REMARK 3 L33: 0.4507 L12: 0.2461 REMARK 3 L13: 0.4018 L23: 0.3042 REMARK 3 S TENSOR REMARK 3 S11: -0.5330 S12: 0.0233 S13: 0.2285 REMARK 3 S21: -0.0074 S22: -0.2189 S23: 0.2553 REMARK 3 S31: -1.1393 S32: -0.9867 S33: 0.5482 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 19 THROUGH 23 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.7721 21.1601 -53.2673 REMARK 3 T TENSOR REMARK 3 T11: 1.2066 T22: 0.3098 REMARK 3 T33: 0.9843 T12: -0.3727 REMARK 3 T13: 0.2167 T23: -0.1962 REMARK 3 L TENSOR REMARK 3 L11: 0.3745 L22: 1.2886 REMARK 3 L33: 1.4056 L12: -0.6957 REMARK 3 L13: 0.4637 L23: -0.9574 REMARK 3 S TENSOR REMARK 3 S11: -0.3157 S12: 0.2137 S13: 0.1922 REMARK 3 S21: -1.0131 S22: -0.2268 S23: -0.6443 REMARK 3 S31: -0.6155 S32: 0.2150 S33: 0.3419 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 24 THROUGH 28 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.3847 14.6706 -50.6411 REMARK 3 T TENSOR REMARK 3 T11: 0.5099 T22: 0.7443 REMARK 3 T33: 0.8471 T12: -0.5846 REMARK 3 T13: 0.1718 T23: -0.3599 REMARK 3 L TENSOR REMARK 3 L11: 1.3630 L22: 4.9585 REMARK 3 L33: 3.0710 L12: 1.1502 REMARK 3 L13: -0.6233 L23: -3.8599 REMARK 3 S TENSOR REMARK 3 S11: -0.2134 S12: -0.3379 S13: 0.3272 REMARK 3 S21: -0.1539 S22: -0.2213 S23: -0.9861 REMARK 3 S31: 0.3543 S32: -0.1653 S33: 0.2049 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 29 THROUGH 43 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.7986 12.0155 -43.4163 REMARK 3 T TENSOR REMARK 3 T11: 0.8697 T22: 0.6751 REMARK 3 T33: 0.6763 T12: -0.5565 REMARK 3 T13: 0.0248 T23: -0.3396 REMARK 3 L TENSOR REMARK 3 L11: 0.5096 L22: 4.3512 REMARK 3 L33: 2.1272 L12: 0.6368 REMARK 3 L13: 1.0377 L23: 0.9497 REMARK 3 S TENSOR REMARK 3 S11: -0.0091 S12: -0.4374 S13: 0.2590 REMARK 3 S21: 0.6965 S22: -0.3205 S23: -0.7223 REMARK 3 S31: -0.4729 S32: 0.4521 S33: -0.4727 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 44 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.8546 23.5716 -46.0798 REMARK 3 T TENSOR REMARK 3 T11: 0.8487 T22: 0.3929 REMARK 3 T33: 1.2720 T12: -0.3288 REMARK 3 T13: 0.2254 T23: -0.4295 REMARK 3 L TENSOR REMARK 3 L11: 3.2219 L22: 9.2978 REMARK 3 L33: 1.6179 L12: -0.0985 REMARK 3 L13: -1.3416 L23: -1.9718 REMARK 3 S TENSOR REMARK 3 S11: -0.3490 S12: -0.0525 S13: 1.2861 REMARK 3 S21: 0.4281 S22: 0.1668 S23: 1.5394 REMARK 3 S31: -0.9193 S32: -0.1033 S33: 0.3675 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.3081 -4.8861 -58.4603 REMARK 3 T TENSOR REMARK 3 T11: 0.1928 T22: 0.3351 REMARK 3 T33: 0.3160 T12: -0.0556 REMARK 3 T13: 0.0332 T23: -0.0229 REMARK 3 L TENSOR REMARK 3 L11: 1.2660 L22: 3.4819 REMARK 3 L33: 2.0677 L12: 0.0840 REMARK 3 L13: -0.8093 L23: -0.0544 REMARK 3 S TENSOR REMARK 3 S11: -0.0270 S12: -0.0060 S13: -0.0680 REMARK 3 S21: 0.1010 S22: -0.1721 S23: -0.4352 REMARK 3 S31: -0.0678 S32: 0.2458 S33: 0.1871 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 84 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.8483 -13.2181 -56.4112 REMARK 3 T TENSOR REMARK 3 T11: 0.2438 T22: 0.3191 REMARK 3 T33: 0.2871 T12: -0.0270 REMARK 3 T13: 0.0128 T23: 0.0076 REMARK 3 L TENSOR REMARK 3 L11: 1.6411 L22: 2.9490 REMARK 3 L33: 0.9232 L12: 0.4591 REMARK 3 L13: 0.2153 L23: 0.1798 REMARK 3 S TENSOR REMARK 3 S11: -0.0291 S12: -0.1242 S13: -0.1738 REMARK 3 S21: 0.1812 S22: -0.0611 S23: -0.3643 REMARK 3 S31: -0.0439 S32: 0.1831 S33: 0.0716 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 134 THROUGH 154 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.3718 -39.4928 -54.9712 REMARK 3 T TENSOR REMARK 3 T11: 0.3757 T22: 0.2902 REMARK 3 T33: 0.6044 T12: 0.0351 REMARK 3 T13: 0.0448 T23: 0.1228 REMARK 3 L TENSOR REMARK 3 L11: 0.5935 L22: 3.4870 REMARK 3 L33: 2.8322 L12: -0.8708 REMARK 3 L13: 0.7834 L23: 0.8366 REMARK 3 S TENSOR REMARK 3 S11: -0.3952 S12: -0.2974 S13: -1.5147 REMARK 3 S21: 0.2530 S22: 0.0689 S23: -0.1445 REMARK 3 S31: 0.7914 S32: -0.0865 S33: 0.3498 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 155 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.3709 -30.7951 -58.8084 REMARK 3 T TENSOR REMARK 3 T11: 0.3243 T22: 0.3029 REMARK 3 T33: 0.4229 T12: -0.0125 REMARK 3 T13: 0.0852 T23: 0.0545 REMARK 3 L TENSOR REMARK 3 L11: 2.9198 L22: 0.8825 REMARK 3 L33: 1.6867 L12: -0.5317 REMARK 3 L13: -0.4587 L23: 0.0156 REMARK 3 S TENSOR REMARK 3 S11: -0.0318 S12: -0.1728 S13: -0.1008 REMARK 3 S21: -0.0964 S22: 0.0750 S23: -0.1121 REMARK 3 S31: 0.0975 S32: 0.0060 S33: -0.0502 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 213 THROUGH 225 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.1764 -37.7179 -65.9601 REMARK 3 T TENSOR REMARK 3 T11: 0.3956 T22: 0.3694 REMARK 3 T33: 0.5331 T12: -0.0342 REMARK 3 T13: 0.1227 T23: -0.0722 REMARK 3 L TENSOR REMARK 3 L11: 6.0946 L22: 1.2141 REMARK 3 L33: 3.6959 L12: 0.9520 REMARK 3 L13: -0.3651 L23: 0.8306 REMARK 3 S TENSOR REMARK 3 S11: -0.3162 S12: 0.8769 S13: -0.5672 REMARK 3 S21: -0.4783 S22: 0.2433 S23: 0.2724 REMARK 3 S31: 1.0299 S32: -0.2159 S33: 0.0370 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 8YOR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1300046052. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-SEP-18 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 : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97891 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59732 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 88.995 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 200 DATA REDUNDANCY : 1.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.6400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: 5TL5,4CMH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.65 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG 3350, 0.2 M POTASSIUM REMARK 280 SODIUM TARTRATE TETRAHYDRATE PH7.4, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 289.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1 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+1/2,Y+1/2,Z+1/2 REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2 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 22.01994 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.78000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 71.63413 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 22.01994 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 56.78000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 71.63413 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5240 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22300 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 B 302 LIES ON A SPECIAL POSITION. REMARK 375 HOH D 304 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 CYS B 225 REMARK 465 GLY B 226 REMARK 465 GLY B 227 REMARK 465 SER B 228 REMARK 465 HIS B 229 REMARK 465 HIS B 230 REMARK 465 HIS B 231 REMARK 465 HIS B 232 REMARK 465 HIS B 233 REMARK 465 HIS B 234 REMARK 465 MET E 8 REMARK 465 ALA E 9 REMARK 465 GLU E 10 REMARK 465 GLY E 53 REMARK 465 PRO E 54 REMARK 465 ASP E 55 REMARK 465 GLU E 56 REMARK 465 SER E 57 REMARK 465 LYS E 58 REMARK 465 GLN E 59 REMARK 465 LYS E 60 REMARK 465 PHE E 61 REMARK 465 VAL E 62 REMARK 465 LEU E 63 REMARK 465 LYS E 64 REMARK 465 THR E 65 REMARK 465 PRO E 66 REMARK 465 LYS E 67 REMARK 465 HIS E 68 REMARK 465 HIS E 69 REMARK 465 HIS E 70 REMARK 465 HIS E 71 REMARK 465 HIS E 72 REMARK 465 HIS E 73 REMARK 465 MET F 8 REMARK 465 ALA F 9 REMARK 465 GLU F 10 REMARK 465 ARG F 11 REMARK 465 LEU F 52 REMARK 465 GLY F 53 REMARK 465 PRO F 54 REMARK 465 ASP F 55 REMARK 465 GLU F 56 REMARK 465 SER F 57 REMARK 465 LYS F 58 REMARK 465 GLN F 59 REMARK 465 LYS F 60 REMARK 465 PHE F 61 REMARK 465 VAL F 62 REMARK 465 LEU F 63 REMARK 465 LYS F 64 REMARK 465 THR F 65 REMARK 465 PRO F 66 REMARK 465 LYS F 67 REMARK 465 HIS F 68 REMARK 465 HIS F 69 REMARK 465 HIS F 70 REMARK 465 HIS F 71 REMARK 465 HIS F 72 REMARK 465 HIS F 73 REMARK 465 GLY D 226 REMARK 465 GLY D 227 REMARK 465 SER D 228 REMARK 465 HIS D 229 REMARK 465 HIS D 230 REMARK 465 HIS D 231 REMARK 465 HIS D 232 REMARK 465 HIS D 233 REMARK 465 HIS D 234 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 ALA A 54 -41.75 70.42 REMARK 500 ASN A 141 75.32 51.28 REMARK 500 LYS A 193 -63.67 -121.76 REMARK 500 ASP B 153 69.94 60.56 REMARK 500 SER C 25 -164.25 -164.64 REMARK 500 THR C 30 -162.93 -105.08 REMARK 500 LEU C 50 -60.54 -94.26 REMARK 500 ALA C 54 -37.87 68.07 REMARK 500 ALA C 87 -177.58 -172.21 REMARK 500 TRP C 95 -70.65 -80.46 REMARK 500 ASN C 141 80.35 53.54 REMARK 500 ASN C 155 19.27 59.61 REMARK 500 LYS C 193 -66.80 -124.26 REMARK 500 ASP D 153 71.81 60.04 REMARK 500 PRO D 156 -152.32 -91.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 427 DISTANCE = 5.89 ANGSTROMS REMARK 525 HOH A 428 DISTANCE = 6.06 ANGSTROMS REMARK 525 HOH A 429 DISTANCE = 6.38 ANGSTROMS REMARK 525 HOH B 479 DISTANCE = 6.38 ANGSTROMS REMARK 525 HOH E 119 DISTANCE = 7.37 ANGSTROMS REMARK 525 HOH F 116 DISTANCE = 6.17 ANGSTROMS REMARK 525 HOH F 117 DISTANCE = 6.39 ANGSTROMS REMARK 525 HOH F 118 DISTANCE = 6.78 ANGSTROMS REMARK 525 HOH D 439 DISTANCE = 5.89 ANGSTROMS REMARK 525 HOH D 440 DISTANCE = 6.01 ANGSTROMS REMARK 525 HOH D 441 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH D 442 DISTANCE = 6.61 ANGSTROMS REMARK 525 HOH D 443 DISTANCE = 6.64 ANGSTROMS REMARK 525 HOH D 444 DISTANCE = 6.78 ANGSTROMS REMARK 525 HOH D 445 DISTANCE = 7.26 ANGSTROMS REMARK 525 HOH D 446 DISTANCE = 7.50 ANGSTROMS DBREF 8YOR A 1 217 PDB 8YOR 8YOR 1 217 DBREF 8YOR B 1 234 PDB 8YOR 8YOR 1 234 DBREF 8YOR E 8 67 UNP P12081 HARS1_HUMAN 1 60 DBREF 8YOR C 1 217 PDB 8YOR 8YOR 1 217 DBREF 8YOR F 8 67 UNP P12081 HARS1_HUMAN 1 60 DBREF 8YOR D 1 234 PDB 8YOR 8YOR 1 234 SEQADV 8YOR HIS E 68 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS E 69 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS E 70 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS E 71 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS E 72 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS E 73 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS F 68 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS F 69 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS F 70 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS F 71 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS F 72 UNP P12081 EXPRESSION TAG SEQADV 8YOR HIS F 73 UNP P12081 EXPRESSION TAG SEQRES 1 A 217 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 A 217 SER LEU GLY GLN ARG ALA THR ILE SER CYS GLN SER GLN SEQRES 3 A 217 SER VAL SER THR SER THR TYR ASN TYR MET HIS TRP TYR SEQRES 4 A 217 GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE LYS SEQRES 5 A 217 TYR ALA SER ASN LEU GLU SER GLY VAL PRO ALA ARG PHE SEQRES 6 A 217 SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN ILE SEQRES 7 A 217 HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR CYS SEQRES 8 A 217 GLN HIS SER TRP GLU ILE PRO TRP THR PHE GLY GLY GLY SEQRES 9 A 217 THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 A 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 A 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 A 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 A 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 A 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 A 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 A 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 A 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 234 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 B 234 PRO GLY SER SER VAL ARG MET SER CYS LYS ALA VAL GLY SEQRES 3 B 234 TYR THR PHE THR ASP TYR CYS ILE GLY TRP ILE LYS GLN SEQRES 4 B 234 ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY ASP ILE CYS SEQRES 5 B 234 PRO GLY ASP ALA TYR THR ASN ASP ASN GLU LYS PHE LYS SEQRES 6 B 234 ASP LYS ALA THR LEU THR ALA ASP THR SER SER THR THR SEQRES 7 B 234 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 B 234 ALA ILE TYR TYR CYS ALA ARG GLY GLU GLU GLN VAL GLY SEQRES 9 B 234 LEU ARG ASN ALA MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 B 234 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 B 234 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 B 234 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 B 234 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 B 234 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 B 234 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 B 234 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 B 234 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 B 234 PRO LYS SER CYS GLY GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 E 66 MET ALA GLU ARG ALA ALA LEU GLU GLU LEU VAL LYS LEU SEQRES 2 E 66 GLN GLY GLU ARG VAL ARG GLY LEU LYS GLN GLN LYS ALA SEQRES 3 E 66 SER ALA GLU LEU ILE GLU GLU GLU VAL ALA LYS LEU LEU SEQRES 4 E 66 LYS LEU LYS ALA GLN LEU GLY PRO ASP GLU SER LYS GLN SEQRES 5 E 66 LYS PHE VAL LEU LYS THR PRO LYS HIS HIS HIS HIS HIS SEQRES 6 E 66 HIS SEQRES 1 C 217 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 C 217 SER LEU GLY GLN ARG ALA THR ILE SER CYS GLN SER GLN SEQRES 3 C 217 SER VAL SER THR SER THR TYR ASN TYR MET HIS TRP TYR SEQRES 4 C 217 GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE LYS SEQRES 5 C 217 TYR ALA SER ASN LEU GLU SER GLY VAL PRO ALA ARG PHE SEQRES 6 C 217 SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN ILE SEQRES 7 C 217 HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR CYS SEQRES 8 C 217 GLN HIS SER TRP GLU ILE PRO TRP THR PHE GLY GLY GLY SEQRES 9 C 217 THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 C 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 C 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 C 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 C 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 C 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 C 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 C 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 C 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 F 66 MET ALA GLU ARG ALA ALA LEU GLU GLU LEU VAL LYS LEU SEQRES 2 F 66 GLN GLY GLU ARG VAL ARG GLY LEU LYS GLN GLN LYS ALA SEQRES 3 F 66 SER ALA GLU LEU ILE GLU GLU GLU VAL ALA LYS LEU LEU SEQRES 4 F 66 LYS LEU LYS ALA GLN LEU GLY PRO ASP GLU SER LYS GLN SEQRES 5 F 66 LYS PHE VAL LEU LYS THR PRO LYS HIS HIS HIS HIS HIS SEQRES 6 F 66 HIS SEQRES 1 D 234 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 D 234 PRO GLY SER SER VAL ARG MET SER CYS LYS ALA VAL GLY SEQRES 3 D 234 TYR THR PHE THR ASP TYR CYS ILE GLY TRP ILE LYS GLN SEQRES 4 D 234 ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY ASP ILE CYS SEQRES 5 D 234 PRO GLY ASP ALA TYR THR ASN ASP ASN GLU LYS PHE LYS SEQRES 6 D 234 ASP LYS ALA THR LEU THR ALA ASP THR SER SER THR THR SEQRES 7 D 234 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 D 234 ALA ILE TYR TYR CYS ALA ARG GLY GLU GLU GLN VAL GLY SEQRES 9 D 234 LEU ARG ASN ALA MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 D 234 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 D 234 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 D 234 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 D 234 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 D 234 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 D 234 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 D 234 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 D 234 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 D 234 PRO LYS SER CYS GLY GLY SER HIS HIS HIS HIS HIS HIS FORMUL 7 HOH *573(H2 O) HELIX 1 AA1 GLU A 82 THR A 86 5 5 HELIX 2 AA2 SER A 124 LYS A 129 1 6 HELIX 3 AA3 LYS A 186 GLU A 190 1 5 HELIX 4 AA4 THR B 28 THR B 30 5 3 HELIX 5 AA5 GLU B 62 LYS B 65 5 4 HELIX 6 AA6 THR B 87 SER B 91 5 5 HELIX 7 AA7 SER B 196 LEU B 198 5 3 HELIX 8 AA8 LYS B 210 ASN B 213 5 4 HELIX 9 AA9 ALA E 12 GLN E 31 1 20 HELIX 10 AB1 SER E 34 ALA E 50 1 17 HELIX 11 AB2 GLU C 82 THR C 86 5 5 HELIX 12 AB3 SER C 124 LYS C 129 1 6 HELIX 13 AB4 LYS C 186 GLU C 190 1 5 HELIX 14 AB5 ALA F 13 GLN F 31 1 19 HELIX 15 AB6 SER F 34 GLN F 51 1 18 HELIX 16 AB7 THR D 28 THR D 30 5 3 HELIX 17 AB8 GLU D 62 LYS D 65 5 4 HELIX 18 AB9 THR D 87 SER D 91 5 5 HELIX 19 AC1 SER D 196 LEU D 198 5 3 HELIX 20 AC2 LYS D 210 ASN D 213 5 4 SHEET 1 AA1 4 THR A 5 SER A 7 0 SHEET 2 AA1 4 ALA A 19 GLN A 24 -1 O GLN A 24 N THR A 5 SHEET 3 AA1 4 ASP A 73 ILE A 78 -1 O LEU A 76 N ILE A 21 SHEET 4 AA1 4 PHE A 65 SER A 70 -1 N SER A 66 O ASN A 77 SHEET 1 AA2 6 SER A 10 SER A 14 0 SHEET 2 AA2 6 THR A 105 LYS A 110 1 O GLU A 108 N LEU A 11 SHEET 3 AA2 6 ALA A 87 HIS A 93 -1 N ALA A 87 O LEU A 107 SHEET 4 AA2 6 MET A 36 GLN A 41 -1 N TYR A 39 O TYR A 90 SHEET 5 AA2 6 LYS A 48 LYS A 52 -1 O LYS A 48 N GLN A 40 SHEET 6 AA2 6 ASN A 56 LEU A 57 -1 O ASN A 56 N LYS A 52 SHEET 1 AA3 4 SER A 117 PHE A 121 0 SHEET 2 AA3 4 THR A 132 PHE A 142 -1 O LEU A 138 N PHE A 119 SHEET 3 AA3 4 TYR A 176 SER A 185 -1 O LEU A 182 N VAL A 135 SHEET 4 AA3 4 SER A 162 VAL A 166 -1 N SER A 165 O SER A 179 SHEET 1 AA4 4 ALA A 156 LEU A 157 0 SHEET 2 AA4 4 ALA A 147 VAL A 153 -1 N VAL A 153 O ALA A 156 SHEET 3 AA4 4 VAL A 194 HIS A 201 -1 O ALA A 196 N LYS A 152 SHEET 4 AA4 4 VAL A 208 ASN A 213 -1 O LYS A 210 N CYS A 197 SHEET 1 AA5 4 GLN B 3 GLN B 6 0 SHEET 2 AA5 4 VAL B 18 VAL B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 AA5 4 THR B 78 LEU B 83 -1 O LEU B 83 N VAL B 18 SHEET 4 AA5 4 ALA B 68 ASP B 73 -1 N ASP B 73 O THR B 78 SHEET 1 AA6 6 GLU B 10 VAL B 12 0 SHEET 2 AA6 6 THR B 116 VAL B 120 1 O THR B 119 N GLU B 10 SHEET 3 AA6 6 ALA B 92 GLU B 101 -1 N ALA B 92 O VAL B 118 SHEET 4 AA6 6 TYR B 32 GLN B 39 -1 N GLY B 35 O ALA B 97 SHEET 5 AA6 6 LEU B 45 CYS B 52 -1 O GLU B 46 N LYS B 38 SHEET 6 AA6 6 TYR B 57 ASP B 60 -1 O TYR B 57 N CYS B 52 SHEET 1 AA7 4 GLU B 10 VAL B 12 0 SHEET 2 AA7 4 THR B 116 VAL B 120 1 O THR B 119 N GLU B 10 SHEET 3 AA7 4 ALA B 92 GLU B 101 -1 N ALA B 92 O VAL B 118 SHEET 4 AA7 4 TYR B 111 TRP B 112 -1 O TYR B 111 N ARG B 98 SHEET 1 AA8 4 SER B 129 LEU B 133 0 SHEET 2 AA8 4 THR B 144 TYR B 154 -1 O LEU B 150 N PHE B 131 SHEET 3 AA8 4 TYR B 185 PRO B 194 -1 O VAL B 193 N ALA B 145 SHEET 4 AA8 4 VAL B 172 THR B 174 -1 N HIS B 173 O VAL B 190 SHEET 1 AA9 4 SER B 129 LEU B 133 0 SHEET 2 AA9 4 THR B 144 TYR B 154 -1 O LEU B 150 N PHE B 131 SHEET 3 AA9 4 TYR B 185 PRO B 194 -1 O VAL B 193 N ALA B 145 SHEET 4 AA9 4 VAL B 178 LEU B 179 -1 N VAL B 178 O SER B 186 SHEET 1 AB1 3 THR B 160 TRP B 163 0 SHEET 2 AB1 3 ILE B 204 HIS B 209 -1 O ASN B 206 N SER B 162 SHEET 3 AB1 3 THR B 214 LYS B 219 -1 O THR B 214 N HIS B 209 SHEET 1 AB2 4 THR C 5 SER C 7 0 SHEET 2 AB2 4 ALA C 19 GLN C 24 -1 O SER C 22 N SER C 7 SHEET 3 AB2 4 ASP C 73 ILE C 78 -1 O LEU C 76 N ILE C 21 SHEET 4 AB2 4 PHE C 65 SER C 70 -1 N SER C 66 O ASN C 77 SHEET 1 AB3 6 SER C 10 SER C 14 0 SHEET 2 AB3 6 THR C 105 LYS C 110 1 O LYS C 110 N VAL C 13 SHEET 3 AB3 6 ALA C 87 HIS C 93 -1 N ALA C 87 O LEU C 107 SHEET 4 AB3 6 MET C 36 GLN C 41 -1 N HIS C 37 O GLN C 92 SHEET 5 AB3 6 LYS C 48 LYS C 52 -1 O LYS C 48 N GLN C 40 SHEET 6 AB3 6 ASN C 56 LEU C 57 -1 O ASN C 56 N LYS C 52 SHEET 1 AB4 4 SER C 117 PHE C 121 0 SHEET 2 AB4 4 THR C 132 PHE C 142 -1 O LEU C 138 N PHE C 119 SHEET 3 AB4 4 TYR C 176 SER C 185 -1 O LEU C 182 N VAL C 135 SHEET 4 AB4 4 SER C 162 VAL C 166 -1 N GLN C 163 O THR C 181 SHEET 1 AB5 4 ALA C 156 LEU C 157 0 SHEET 2 AB5 4 LYS C 148 VAL C 153 -1 N VAL C 153 O ALA C 156 SHEET 3 AB5 4 VAL C 194 THR C 200 -1 O GLU C 198 N GLN C 150 SHEET 4 AB5 4 VAL C 208 ASN C 213 -1 O LYS C 210 N CYS C 197 SHEET 1 AB6 4 GLN D 3 GLN D 6 0 SHEET 2 AB6 4 VAL D 18 VAL D 25 -1 O LYS D 23 N GLN D 5 SHEET 3 AB6 4 THR D 78 LEU D 83 -1 O ALA D 79 N CYS D 22 SHEET 4 AB6 4 ALA D 68 ASP D 73 -1 N ASP D 73 O THR D 78 SHEET 1 AB7 6 GLU D 10 VAL D 12 0 SHEET 2 AB7 6 THR D 116 VAL D 120 1 O THR D 119 N GLU D 10 SHEET 3 AB7 6 ALA D 92 GLU D 101 -1 N ALA D 92 O VAL D 118 SHEET 4 AB7 6 TYR D 32 GLN D 39 -1 N CYS D 33 O GLY D 99 SHEET 5 AB7 6 LEU D 45 CYS D 52 -1 O GLU D 46 N LYS D 38 SHEET 6 AB7 6 TYR D 57 ASP D 60 -1 O TYR D 57 N CYS D 52 SHEET 1 AB8 4 GLU D 10 VAL D 12 0 SHEET 2 AB8 4 THR D 116 VAL D 120 1 O THR D 119 N GLU D 10 SHEET 3 AB8 4 ALA D 92 GLU D 101 -1 N ALA D 92 O VAL D 118 SHEET 4 AB8 4 TYR D 111 TRP D 112 -1 O TYR D 111 N ARG D 98 SHEET 1 AB9 4 SER D 129 LEU D 133 0 SHEET 2 AB9 4 THR D 144 TYR D 154 -1 O LEU D 150 N PHE D 131 SHEET 3 AB9 4 TYR D 185 PRO D 194 -1 O VAL D 193 N ALA D 145 SHEET 4 AB9 4 VAL D 172 THR D 174 -1 N HIS D 173 O VAL D 190 SHEET 1 AC1 4 SER D 129 LEU D 133 0 SHEET 2 AC1 4 THR D 144 TYR D 154 -1 O LEU D 150 N PHE D 131 SHEET 3 AC1 4 TYR D 185 PRO D 194 -1 O VAL D 193 N ALA D 145 SHEET 4 AC1 4 VAL D 178 LEU D 179 -1 N VAL D 178 O SER D 186 SHEET 1 AC2 3 THR D 160 TRP D 163 0 SHEET 2 AC2 3 TYR D 203 HIS D 209 -1 O ASN D 206 N SER D 162 SHEET 3 AC2 3 THR D 214 VAL D 220 -1 O THR D 214 N HIS D 209 SSBOND 1 CYS A 23 CYS A 91 1555 1555 2.03 SSBOND 2 CYS A 137 CYS A 197 1555 1555 2.03 SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 4 CYS B 33 CYS B 52 1555 1555 2.03 SSBOND 5 CYS B 149 CYS B 205 1555 1555 2.03 SSBOND 6 CYS C 23 CYS C 91 1555 1555 2.03 SSBOND 7 CYS C 137 CYS C 197 1555 1555 2.03 SSBOND 8 CYS C 217 CYS D 225 1555 1555 2.03 SSBOND 9 CYS D 22 CYS D 96 1555 1555 2.03 SSBOND 10 CYS D 33 CYS D 52 1555 1555 2.03 SSBOND 11 CYS D 149 CYS D 205 1555 1555 2.03 CISPEP 1 SER A 7 PRO A 8 0 -1.99 CISPEP 2 HIS A 79 PRO A 80 0 -2.45 CISPEP 3 ILE A 97 PRO A 98 0 0.80 CISPEP 4 TYR A 143 PRO A 144 0 3.07 CISPEP 5 PHE B 155 PRO B 156 0 -2.79 CISPEP 6 GLU B 157 PRO B 158 0 -3.64 CISPEP 7 SER C 7 PRO C 8 0 -2.21 CISPEP 8 HIS C 79 PRO C 80 0 -2.29 CISPEP 9 ILE C 97 PRO C 98 0 3.10 CISPEP 10 TYR C 143 PRO C 144 0 3.62 CISPEP 11 PHE D 155 PRO D 156 0 -1.83 CISPEP 12 GLU D 157 PRO D 158 0 -3.36 CRYST1 86.750 113.560 149.499 90.00 106.60 90.00 I 1 2 1 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 0.011527 0.000000 0.003436 0.00000 SCALE2 0.000000 0.008806 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006980 0.00000