HEADER TRANSFERASE 02-FEB-24 8RVR TITLE CRYSTAL STRUCTURE OF TRYPANOSOMA CONGOLENSE PYRUVATE KINASE IN COMPLEX TITLE 2 WITH A SINGLE-DOMAIN ANTIBODY (TCOPYK-SDAB42) IN THE PRESENCE OF TITLE 3 SULFATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PYRUVATE KINASE; COMPND 3 CHAIN: A, B, C, D, E, F; COMPND 4 EC: 2.7.1.40; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CAMELID SINGLE-DOMAIN ANTIBODY 42 (SDAB42); COMPND 8 CHAIN: G, H, I, J, K, L; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CONGOLENSE; SOURCE 3 ORGANISM_TAXID: 5692; SOURCE 4 GENE: TCIL3000_10_12020; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 9 ORGANISM_TAXID: 30538; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS PYRUVATE KINASE, CAMELID SINGLE-DOMAIN ANTIBODY, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR Y.G.-J.STERCKX REVDAT 1 16-APR-25 8RVR 0 JRNL AUTH J.E.PINTO TORRES,M.CLAES,R.HENDRICKX,M.YUAN,N.SMIEJKOWSKA, JRNL AUTH 2 P.VAN WIELENDAELE,A.HACISULEYMAN,H.DE WINTER,S.MUYLDERMANS, JRNL AUTH 3 P.A.M.MICHELS,M.D.WALKINSHAW,W.VERSEES,G.CALJON,S.MAGEZ, JRNL AUTH 4 Y.G.STERCKX JRNL TITL ALLOSTERIC INHIBITION OF TRYPANOSOMATID PYRUVATE KINASES BY JRNL TITL 2 A CAMELID SINGLE-DOMAIN ANTIBODY. JRNL REF ELIFE V. 13 2025 JRNL REFN ESSN 2050-084X JRNL PMID 40163365 JRNL DOI 10.7554/ELIFE.100066 REMARK 2 REMARK 2 RESOLUTION. 3.19 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.19 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.32 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 83419 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.223 REMARK 3 R VALUE (WORKING SET) : 0.221 REMARK 3 FREE R VALUE : 0.275 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4168 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 49.3200 - 9.9000 1.00 2838 150 0.2236 0.2452 REMARK 3 2 9.9000 - 7.8700 1.00 2756 145 0.1544 0.2103 REMARK 3 3 7.8700 - 6.8800 1.00 2704 143 0.1963 0.2487 REMARK 3 4 6.8700 - 6.2500 1.00 2677 141 0.2151 0.2582 REMARK 3 5 6.2500 - 5.8000 1.00 2671 140 0.2165 0.2994 REMARK 3 6 5.8000 - 5.4600 1.00 2689 142 0.2136 0.2909 REMARK 3 7 5.4600 - 5.1900 1.00 2654 140 0.2088 0.2259 REMARK 3 8 5.1900 - 4.9600 1.00 2643 139 0.1923 0.2574 REMARK 3 9 4.9600 - 4.7700 1.00 2651 138 0.1842 0.2316 REMARK 3 10 4.7700 - 4.6100 1.00 2662 141 0.1784 0.2130 REMARK 3 11 4.6100 - 4.4600 1.00 2630 137 0.1790 0.2511 REMARK 3 12 4.4600 - 4.3300 1.00 2633 139 0.1888 0.2702 REMARK 3 13 4.3300 - 4.2200 1.00 2610 137 0.1990 0.2616 REMARK 3 14 4.2200 - 4.1200 1.00 2659 140 0.1987 0.2759 REMARK 3 15 4.1200 - 4.0200 1.00 2622 138 0.2283 0.2903 REMARK 3 16 4.0200 - 3.9400 1.00 2634 139 0.2307 0.3249 REMARK 3 17 3.9400 - 3.8600 1.00 2661 140 0.2361 0.3072 REMARK 3 18 3.8600 - 3.7900 1.00 2608 138 0.2308 0.3051 REMARK 3 19 3.7900 - 3.7200 1.00 2618 137 0.2283 0.2980 REMARK 3 20 3.7200 - 3.6600 1.00 2618 138 0.2441 0.2897 REMARK 3 21 3.6600 - 3.6000 1.00 2622 138 0.2436 0.2543 REMARK 3 22 3.6000 - 3.5400 1.00 2625 137 0.2615 0.3266 REMARK 3 23 3.5400 - 3.4900 1.00 2600 136 0.2727 0.3116 REMARK 3 24 3.4900 - 3.4400 1.00 2611 138 0.3013 0.3456 REMARK 3 25 3.4400 - 3.3900 1.00 2647 138 0.3215 0.3973 REMARK 3 26 3.3900 - 3.3500 1.00 2597 137 0.3429 0.4148 REMARK 3 27 3.3500 - 3.3100 1.00 2635 139 0.3315 0.4036 REMARK 3 28 3.3100 - 3.2700 1.00 2612 138 0.3501 0.3807 REMARK 3 29 3.2700 - 3.2300 1.00 2614 137 0.3540 0.3763 REMARK 3 30 3.2300 - 3.1900 0.94 2450 128 0.3845 0.3973 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) : 0.510 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.910 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 : 0.011 26284 REMARK 3 ANGLE : 1.361 35710 REMARK 3 CHIRALITY : 0.073 4147 REMARK 3 PLANARITY : 0.012 4675 REMARK 3 DIHEDRAL : 6.815 3768 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 66 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -53.9150 32.2256 -51.4025 REMARK 3 T TENSOR REMARK 3 T11: 0.6851 T22: 0.7280 REMARK 3 T33: 0.6393 T12: -0.1235 REMARK 3 T13: -0.0159 T23: 0.0370 REMARK 3 L TENSOR REMARK 3 L11: 1.3982 L22: 4.1345 REMARK 3 L33: 0.7005 L12: 0.3400 REMARK 3 L13: -0.4943 L23: -0.7590 REMARK 3 S TENSOR REMARK 3 S11: -0.1286 S12: -0.4147 S13: -0.0717 REMARK 3 S21: 0.4962 S22: 0.0324 S23: 0.1782 REMARK 3 S31: -0.0233 S32: -0.2571 S33: 0.1089 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 99 THROUGH 183 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.9170 26.9105 -32.6087 REMARK 3 T TENSOR REMARK 3 T11: 1.8783 T22: 2.1121 REMARK 3 T33: 1.2268 T12: -0.5306 REMARK 3 T13: -0.3512 T23: 0.1131 REMARK 3 L TENSOR REMARK 3 L11: 5.1573 L22: 2.9411 REMARK 3 L33: 5.2568 L12: 0.9509 REMARK 3 L13: -0.4802 L23: -0.5422 REMARK 3 S TENSOR REMARK 3 S11: 0.5222 S12: -2.0892 S13: -0.1398 REMARK 3 S21: 1.9653 S22: -0.5858 S23: -1.1795 REMARK 3 S31: -1.0127 S32: 1.6107 S33: 0.0125 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 404 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.4870 32.3844 -60.9766 REMARK 3 T TENSOR REMARK 3 T11: 0.6477 T22: 0.5876 REMARK 3 T33: 0.7579 T12: -0.0512 REMARK 3 T13: 0.0158 T23: 0.0596 REMARK 3 L TENSOR REMARK 3 L11: 0.5755 L22: 0.2614 REMARK 3 L33: 2.1671 L12: 0.1728 REMARK 3 L13: 0.3417 L23: 0.3059 REMARK 3 S TENSOR REMARK 3 S11: 0.0051 S12: -0.1188 S13: -0.1853 REMARK 3 S21: 0.1308 S22: -0.1029 S23: -0.1421 REMARK 3 S31: 0.1694 S32: 0.1229 S33: 0.0792 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 405 THROUGH 500 ) REMARK 3 ORIGIN FOR THE GROUP (A): -62.2184 28.0379 -74.6020 REMARK 3 T TENSOR REMARK 3 T11: 0.7131 T22: 0.7282 REMARK 3 T33: 0.6801 T12: -0.2236 REMARK 3 T13: -0.0058 T23: -0.0276 REMARK 3 L TENSOR REMARK 3 L11: 4.8064 L22: 3.9733 REMARK 3 L33: 7.9714 L12: -0.5515 REMARK 3 L13: -1.1656 L23: -4.6177 REMARK 3 S TENSOR REMARK 3 S11: 0.0408 S12: 0.5138 S13: -0.5363 REMARK 3 S21: -0.4095 S22: 0.2447 S23: 0.4748 REMARK 3 S31: 1.2271 S32: -0.6077 S33: -0.2164 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.4008 54.4548 -58.1179 REMARK 3 T TENSOR REMARK 3 T11: 0.6847 T22: 0.7830 REMARK 3 T33: 0.8769 T12: -0.1433 REMARK 3 T13: 0.0017 T23: -0.0625 REMARK 3 L TENSOR REMARK 3 L11: 1.8397 L22: 1.5665 REMARK 3 L33: 1.3596 L12: 1.3765 REMARK 3 L13: 1.6788 L23: 0.5723 REMARK 3 S TENSOR REMARK 3 S11: -0.0588 S12: 0.2089 S13: -0.0585 REMARK 3 S21: 0.0614 S22: 0.2626 S23: -0.3998 REMARK 3 S31: -0.2444 S32: 0.3419 S33: -0.1690 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.5444 73.9881 -47.4884 REMARK 3 T TENSOR REMARK 3 T11: 0.9527 T22: 0.8482 REMARK 3 T33: 0.9392 T12: -0.1001 REMARK 3 T13: -0.2023 T23: -0.0424 REMARK 3 L TENSOR REMARK 3 L11: 1.8050 L22: 5.0256 REMARK 3 L33: 3.3735 L12: -0.4320 REMARK 3 L13: 1.3078 L23: 1.9046 REMARK 3 S TENSOR REMARK 3 S11: -0.8294 S12: -0.2079 S13: 0.6163 REMARK 3 S21: 0.9335 S22: 0.5082 S23: 0.0791 REMARK 3 S31: -0.5569 S32: 0.7541 S33: 0.3829 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 204 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.0440 79.3632 -50.7438 REMARK 3 T TENSOR REMARK 3 T11: 1.0516 T22: 0.7066 REMARK 3 T33: 0.8708 T12: -0.1823 REMARK 3 T13: -0.0661 T23: -0.2090 REMARK 3 L TENSOR REMARK 3 L11: 2.0460 L22: 3.0026 REMARK 3 L33: 2.9929 L12: -2.3450 REMARK 3 L13: 0.3498 L23: -0.1139 REMARK 3 S TENSOR REMARK 3 S11: -0.1059 S12: 0.3166 S13: 1.0326 REMARK 3 S21: 1.0128 S22: 0.1779 S23: -0.6210 REMARK 3 S31: -0.6200 S32: -0.2009 S33: 0.0312 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 205 THROUGH 392 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.4259 62.7743 -61.4030 REMARK 3 T TENSOR REMARK 3 T11: 0.6902 T22: 0.4550 REMARK 3 T33: 0.8255 T12: -0.1374 REMARK 3 T13: -0.0694 T23: 0.0031 REMARK 3 L TENSOR REMARK 3 L11: 0.7522 L22: 1.2224 REMARK 3 L33: 2.0722 L12: -0.0164 REMARK 3 L13: -0.7558 L23: -0.1348 REMARK 3 S TENSOR REMARK 3 S11: 0.0372 S12: -0.1097 S13: 0.2312 REMARK 3 S21: 0.0170 S22: -0.0914 S23: -0.1365 REMARK 3 S31: -0.4965 S32: 0.2331 S33: 0.0612 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 393 THROUGH 442 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.9782 67.6175 -70.6214 REMARK 3 T TENSOR REMARK 3 T11: 0.8077 T22: 0.7518 REMARK 3 T33: 0.9108 T12: -0.2627 REMARK 3 T13: -0.0541 T23: 0.0186 REMARK 3 L TENSOR REMARK 3 L11: 1.2501 L22: 0.7606 REMARK 3 L33: 2.5288 L12: 0.3721 REMARK 3 L13: -1.0305 L23: 0.7359 REMARK 3 S TENSOR REMARK 3 S11: -0.0894 S12: 0.3067 S13: 0.1544 REMARK 3 S21: -0.0370 S22: 0.1355 S23: -0.1457 REMARK 3 S31: -0.1723 S32: -0.0197 S33: -0.0527 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 443 THROUGH 467 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.9785 73.7364 -73.4427 REMARK 3 T TENSOR REMARK 3 T11: 1.1798 T22: 1.2049 REMARK 3 T33: 1.0575 T12: -0.4448 REMARK 3 T13: -0.0722 T23: 0.0659 REMARK 3 L TENSOR REMARK 3 L11: 2.0248 L22: 0.3878 REMARK 3 L33: 2.9139 L12: -0.6608 REMARK 3 L13: 1.3801 L23: -0.0383 REMARK 3 S TENSOR REMARK 3 S11: -0.3215 S12: 0.2761 S13: -0.1070 REMARK 3 S21: -0.1678 S22: 0.3758 S23: -0.6555 REMARK 3 S31: -1.0994 S32: 0.7665 S33: 0.1253 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 468 THROUGH 501 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.1336 65.8114 -80.8514 REMARK 3 T TENSOR REMARK 3 T11: 1.0697 T22: 0.8685 REMARK 3 T33: 0.8414 T12: -0.3839 REMARK 3 T13: 0.0797 T23: -0.2372 REMARK 3 L TENSOR REMARK 3 L11: 9.9462 L22: 5.5533 REMARK 3 L33: 6.1808 L12: -2.1637 REMARK 3 L13: 0.0889 L23: 2.5007 REMARK 3 S TENSOR REMARK 3 S11: 0.8390 S12: -0.2513 S13: 0.5811 REMARK 3 S21: -1.0331 S22: 0.0339 S23: -0.8127 REMARK 3 S31: -0.6746 S32: 0.5426 S33: -0.7050 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.1748 30.9740-122.1488 REMARK 3 T TENSOR REMARK 3 T11: 0.7461 T22: 0.7513 REMARK 3 T33: 0.5987 T12: -0.1819 REMARK 3 T13: 0.0629 T23: -0.0515 REMARK 3 L TENSOR REMARK 3 L11: 3.2332 L22: 2.3127 REMARK 3 L33: 1.4638 L12: 0.6946 REMARK 3 L13: 0.4738 L23: 0.6849 REMARK 3 S TENSOR REMARK 3 S11: 0.0393 S12: 0.7780 S13: -0.1922 REMARK 3 S21: -0.1460 S22: -0.1334 S23: 0.1749 REMARK 3 S31: 0.3336 S32: -0.0204 S33: 0.0221 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 76 THROUGH 166 ) REMARK 3 ORIGIN FOR THE GROUP (A): -60.7692 55.6905-142.2886 REMARK 3 T TENSOR REMARK 3 T11: 1.5705 T22: 1.2122 REMARK 3 T33: 1.0087 T12: -0.3991 REMARK 3 T13: 0.0693 T23: 0.0229 REMARK 3 L TENSOR REMARK 3 L11: 1.0991 L22: 4.4767 REMARK 3 L33: 4.8881 L12: 0.4844 REMARK 3 L13: -0.5776 L23: -0.9302 REMARK 3 S TENSOR REMARK 3 S11: -0.4174 S12: 0.6021 S13: 0.4276 REMARK 3 S21: -0.8330 S22: 0.1748 S23: -0.8638 REMARK 3 S31: -1.7167 S32: 0.1114 S33: 0.2727 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 167 THROUGH 204 ) REMARK 3 ORIGIN FOR THE GROUP (A): -64.3135 50.3390-133.3663 REMARK 3 T TENSOR REMARK 3 T11: 0.7998 T22: 0.9848 REMARK 3 T33: 1.1825 T12: -0.0022 REMARK 3 T13: -0.0326 T23: 0.2050 REMARK 3 L TENSOR REMARK 3 L11: 4.8747 L22: 7.1397 REMARK 3 L33: 4.0488 L12: 3.1853 REMARK 3 L13: -1.8108 L23: -3.4282 REMARK 3 S TENSOR REMARK 3 S11: -0.3107 S12: -0.3664 S13: -0.2188 REMARK 3 S21: -0.2255 S22: -0.4255 S23: -1.5049 REMARK 3 S31: -0.3458 S32: 0.4668 S33: 0.4438 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 205 THROUGH 404 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.9088 42.7596-114.0061 REMARK 3 T TENSOR REMARK 3 T11: 0.5586 T22: 0.6263 REMARK 3 T33: 0.7161 T12: -0.0958 REMARK 3 T13: -0.0398 T23: -0.0329 REMARK 3 L TENSOR REMARK 3 L11: 1.6486 L22: 0.8670 REMARK 3 L33: 1.7029 L12: 0.1037 REMARK 3 L13: -0.2230 L23: -0.1215 REMARK 3 S TENSOR REMARK 3 S11: 0.0018 S12: 0.2887 S13: 0.1944 REMARK 3 S21: -0.0729 S22: 0.0733 S23: 0.0610 REMARK 3 S31: 0.0291 S32: -0.2454 S33: -0.0631 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 405 THROUGH 499 ) REMARK 3 ORIGIN FOR THE GROUP (A): -59.4731 25.7690-101.5483 REMARK 3 T TENSOR REMARK 3 T11: 0.6102 T22: 0.7137 REMARK 3 T33: 0.6203 T12: -0.2162 REMARK 3 T13: 0.0767 T23: -0.0839 REMARK 3 L TENSOR REMARK 3 L11: 3.7971 L22: 5.1442 REMARK 3 L33: 6.8663 L12: 0.3705 REMARK 3 L13: 3.5533 L23: -0.8479 REMARK 3 S TENSOR REMARK 3 S11: 0.1022 S12: -0.2668 S13: -0.4147 REMARK 3 S21: 0.1292 S22: -0.0980 S23: 0.3658 REMARK 3 S31: 0.9513 S32: -1.2520 S33: -0.0008 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: NULL REMARK 3 ORIGIN FOR THE GROUP (A): -48.2899 9.5088 -96.6841 REMARK 3 T TENSOR REMARK 3 T11: 1.5808 T22: 0.4415 REMARK 3 T33: 0.9331 T12: -0.1511 REMARK 3 T13: -0.3189 T23: 0.2342 REMARK 3 L TENSOR REMARK 3 L11: 1.9998 L22: 2.0002 REMARK 3 L33: 1.9999 L12: 2.0002 REMARK 3 L13: 2.0001 L23: 4.0084 REMARK 3 S TENSOR REMARK 3 S11: -3.9994 S12: -3.5675 S13: -8.7014 REMARK 3 S21: 6.7907 S22: -3.6738 S23: 1.3673 REMARK 3 S31: 10.9734 S32: 0.8473 S33: 7.6805 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.1054 59.7813-124.0746 REMARK 3 T TENSOR REMARK 3 T11: 0.8463 T22: 1.1331 REMARK 3 T33: 0.7631 T12: -0.3391 REMARK 3 T13: 0.0244 T23: 0.1181 REMARK 3 L TENSOR REMARK 3 L11: 1.8673 L22: 3.0644 REMARK 3 L33: 1.2589 L12: 0.4296 REMARK 3 L13: -0.2853 L23: -0.0095 REMARK 3 S TENSOR REMARK 3 S11: 0.2117 S12: 0.1709 S13: 0.4459 REMARK 3 S21: -0.3940 S22: 0.0014 S23: -0.6562 REMARK 3 S31: -0.7257 S32: 0.9865 S33: -0.1669 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 100 THROUGH 204 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.2299 34.4904-136.7869 REMARK 3 T TENSOR REMARK 3 T11: 0.9177 T22: 1.4463 REMARK 3 T33: 1.0153 T12: 0.0163 REMARK 3 T13: 0.2642 T23: 0.0755 REMARK 3 L TENSOR REMARK 3 L11: 3.0015 L22: 4.5994 REMARK 3 L33: 0.9391 L12: 0.7324 REMARK 3 L13: 0.1196 L23: 1.9849 REMARK 3 S TENSOR REMARK 3 S11: 0.3204 S12: 0.3003 S13: -0.2562 REMARK 3 S21: -0.9247 S22: -0.2435 S23: -0.4673 REMARK 3 S31: -0.3962 S32: 0.6732 S33: -0.0107 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 205 THROUGH 442 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.5545 53.6987-111.6432 REMARK 3 T TENSOR REMARK 3 T11: 0.5981 T22: 0.7699 REMARK 3 T33: 0.7143 T12: -0.2383 REMARK 3 T13: 0.0410 T23: 0.0386 REMARK 3 L TENSOR REMARK 3 L11: 1.3664 L22: 1.5300 REMARK 3 L33: 2.1332 L12: 0.4995 REMARK 3 L13: 0.5885 L23: 0.5323 REMARK 3 S TENSOR REMARK 3 S11: -0.0279 S12: 0.2304 S13: 0.1109 REMARK 3 S21: 0.0348 S22: -0.0237 S23: -0.2523 REMARK 3 S31: -0.4024 S32: 0.8510 S33: 0.0490 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 443 THROUGH 468 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.3518 77.9038-101.8153 REMARK 3 T TENSOR REMARK 3 T11: 1.4100 T22: 1.8470 REMARK 3 T33: 1.2599 T12: -0.8913 REMARK 3 T13: 0.0066 T23: 0.3004 REMARK 3 L TENSOR REMARK 3 L11: 5.3204 L22: 3.8498 REMARK 3 L33: 2.6664 L12: -0.7070 REMARK 3 L13: 0.2285 L23: 2.0826 REMARK 3 S TENSOR REMARK 3 S11: 1.2620 S12: 0.2663 S13: 1.9241 REMARK 3 S21: 0.3351 S22: 0.1645 S23: -0.4958 REMARK 3 S31: -1.2299 S32: 1.5257 S33: -1.4579 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 469 THROUGH 499 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.2447 71.4903 -94.0016 REMARK 3 T TENSOR REMARK 3 T11: 0.8160 T22: 0.7481 REMARK 3 T33: 0.9841 T12: -0.3340 REMARK 3 T13: -0.0146 T23: 0.0335 REMARK 3 L TENSOR REMARK 3 L11: 6.1555 L22: 2.3362 REMARK 3 L33: 9.0284 L12: -1.5959 REMARK 3 L13: -1.6523 L23: 0.4511 REMARK 3 S TENSOR REMARK 3 S11: -0.0520 S12: -1.2310 S13: 0.6392 REMARK 3 S21: 0.0920 S22: 0.5109 S23: -0.8601 REMARK 3 S31: -1.0176 S32: 0.5719 S33: -0.2082 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: NULL REMARK 3 ORIGIN FOR THE GROUP (A): -30.5537 86.3988 -98.3427 REMARK 3 T TENSOR REMARK 3 T11: 1.1254 T22: 0.2252 REMARK 3 T33: 1.3617 T12: -0.2000 REMARK 3 T13: -0.0609 T23: -0.2837 REMARK 3 L TENSOR REMARK 3 L11: 1.9999 L22: 2.0000 REMARK 3 L33: 2.0000 L12: 2.0000 REMARK 3 L13: 2.0001 L23: 2.0000 REMARK 3 S TENSOR REMARK 3 S11: -1.8209 S12: 1.7429 S13: -3.7393 REMARK 3 S21: -9.5539 S22: 2.4878 S23: -8.0699 REMARK 3 S31: 6.1574 S32: 0.6388 S33: -0.6798 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -58.0161 17.2058 -14.9424 REMARK 3 T TENSOR REMARK 3 T11: 1.4685 T22: 1.4346 REMARK 3 T33: 0.7766 T12: -0.7487 REMARK 3 T13: -0.2755 T23: 0.1279 REMARK 3 L TENSOR REMARK 3 L11: 1.0517 L22: 0.8696 REMARK 3 L33: 2.9779 L12: 0.6013 REMARK 3 L13: -1.2163 L23: -1.5693 REMARK 3 S TENSOR REMARK 3 S11: 0.7208 S12: -0.5678 S13: -0.0897 REMARK 3 S21: 0.7411 S22: -0.8247 S23: -0.1502 REMARK 3 S31: -0.1469 S32: 0.8975 S33: 0.1100 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 45 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -60.4415 33.4361 -28.4366 REMARK 3 T TENSOR REMARK 3 T11: 1.2380 T22: 1.0891 REMARK 3 T33: 0.7511 T12: -0.4019 REMARK 3 T13: 0.0693 T23: 0.1459 REMARK 3 L TENSOR REMARK 3 L11: 2.8678 L22: 2.6910 REMARK 3 L33: 2.8580 L12: -0.2731 REMARK 3 L13: -1.5352 L23: -1.8916 REMARK 3 S TENSOR REMARK 3 S11: 0.2495 S12: 0.9020 S13: 0.4192 REMARK 3 S21: 1.4457 S22: -0.7474 S23: -0.2110 REMARK 3 S31: 0.3723 S32: -1.0682 S33: 0.4410 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 76 THROUGH 274 ) REMARK 3 ORIGIN FOR THE GROUP (A): -75.5009 35.1084 -18.3824 REMARK 3 T TENSOR REMARK 3 T11: 1.3063 T22: 1.2761 REMARK 3 T33: 0.9898 T12: -0.4993 REMARK 3 T13: 0.2066 T23: 0.0213 REMARK 3 L TENSOR REMARK 3 L11: 1.8471 L22: 2.0865 REMARK 3 L33: 3.0782 L12: -0.3073 REMARK 3 L13: -0.9529 L23: -0.3053 REMARK 3 S TENSOR REMARK 3 S11: 0.1943 S12: 0.1825 S13: 0.4711 REMARK 3 S21: 0.1961 S22: 0.0400 S23: 0.1900 REMARK 3 S31: -0.2256 S32: -0.4931 S33: -0.0394 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 275 THROUGH 425 ) REMARK 3 ORIGIN FOR THE GROUP (A): -69.2964 16.9958 -13.3123 REMARK 3 T TENSOR REMARK 3 T11: 1.5130 T22: 1.4905 REMARK 3 T33: 0.7507 T12: -0.7424 REMARK 3 T13: 0.0176 T23: 0.0650 REMARK 3 L TENSOR REMARK 3 L11: 0.2507 L22: 0.9473 REMARK 3 L33: 2.1334 L12: 0.1667 REMARK 3 L13: 0.7703 L23: 1.5852 REMARK 3 S TENSOR REMARK 3 S11: 0.5726 S12: -0.1783 S13: 0.1968 REMARK 3 S21: 0.8108 S22: -0.4715 S23: -0.0001 REMARK 3 S31: 0.1723 S32: -0.1628 S33: -0.0757 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 426 THROUGH 480 ) REMARK 3 ORIGIN FOR THE GROUP (A): -70.0485 9.2332 -31.4992 REMARK 3 T TENSOR REMARK 3 T11: 1.0820 T22: 1.3653 REMARK 3 T33: 0.8672 T12: -0.5696 REMARK 3 T13: 0.1476 T23: 0.0566 REMARK 3 L TENSOR REMARK 3 L11: 2.5295 L22: 4.8502 REMARK 3 L33: 2.0713 L12: 0.7088 REMARK 3 L13: -0.9096 L23: 0.3628 REMARK 3 S TENSOR REMARK 3 S11: 0.3015 S12: 0.0530 S13: 0.1117 REMARK 3 S21: -0.3532 S22: -0.2004 S23: -0.5883 REMARK 3 S31: -0.3890 S32: -0.1367 S33: -0.0510 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 481 THROUGH 500 ) REMARK 3 ORIGIN FOR THE GROUP (A): -78.8099 1.4186 -29.6174 REMARK 3 T TENSOR REMARK 3 T11: 1.0790 T22: 1.3425 REMARK 3 T33: 0.7897 T12: -0.5965 REMARK 3 T13: 0.0716 T23: 0.2809 REMARK 3 L TENSOR REMARK 3 L11: 5.9883 L22: 4.9584 REMARK 3 L33: 4.7162 L12: -0.3585 REMARK 3 L13: 3.3815 L23: 1.2848 REMARK 3 S TENSOR REMARK 3 S11: -0.6295 S12: 0.4545 S13: 0.8910 REMARK 3 S21: -0.7441 S22: 1.4360 S23: -0.6639 REMARK 3 S31: -0.0881 S32: 0.0881 S33: -0.6025 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 2 THROUGH 22 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.3062 107.7106 -6.1867 REMARK 3 T TENSOR REMARK 3 T11: 1.6137 T22: 2.1429 REMARK 3 T33: 0.9350 T12: 0.9886 REMARK 3 T13: 0.1205 T23: 0.2139 REMARK 3 L TENSOR REMARK 3 L11: 3.7701 L22: 2.0593 REMARK 3 L33: 2.2881 L12: -0.2892 REMARK 3 L13: 2.8696 L23: 0.1051 REMARK 3 S TENSOR REMARK 3 S11: -0.5708 S12: 0.0175 S13: 0.1777 REMARK 3 S21: -0.0373 S22: -0.0819 S23: -0.9713 REMARK 3 S31: 0.3643 S32: 1.4908 S33: 0.7571 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 23 THROUGH 248 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.0962 102.9256 -25.0130 REMARK 3 T TENSOR REMARK 3 T11: 1.2469 T22: 1.7168 REMARK 3 T33: 0.8434 T12: 0.3762 REMARK 3 T13: -0.0849 T23: 0.0998 REMARK 3 L TENSOR REMARK 3 L11: 1.4324 L22: 2.4721 REMARK 3 L33: 3.2735 L12: 0.9149 REMARK 3 L13: -0.1990 L23: -0.9473 REMARK 3 S TENSOR REMARK 3 S11: 0.0640 S12: -0.0518 S13: 0.1779 REMARK 3 S21: -0.2303 S22: 0.0281 S23: 0.0629 REMARK 3 S31: 0.7940 S32: 0.0820 S33: -0.0291 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 249 THROUGH 273 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.9072 95.2720 -9.7083 REMARK 3 T TENSOR REMARK 3 T11: 1.5802 T22: 1.5001 REMARK 3 T33: 1.1032 T12: 0.8460 REMARK 3 T13: -0.2285 T23: 0.1349 REMARK 3 L TENSOR REMARK 3 L11: 1.3686 L22: 0.7810 REMARK 3 L33: 8.4345 L12: 0.9838 REMARK 3 L13: 0.5142 L23: -0.1663 REMARK 3 S TENSOR REMARK 3 S11: 0.3691 S12: -0.0491 S13: 0.2520 REMARK 3 S21: -1.3023 S22: -0.7099 S23: 0.5235 REMARK 3 S31: 1.4842 S32: -0.2962 S33: -0.2098 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 274 THROUGH 425 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.4960 100.4701 -14.2600 REMARK 3 T TENSOR REMARK 3 T11: 1.9409 T22: 2.2378 REMARK 3 T33: 0.6542 T12: 1.1701 REMARK 3 T13: -0.1027 T23: 0.0667 REMARK 3 L TENSOR REMARK 3 L11: 0.1602 L22: -0.1675 REMARK 3 L33: 0.3249 L12: -1.0653 REMARK 3 L13: -0.3391 L23: -0.5636 REMARK 3 S TENSOR REMARK 3 S11: 0.9993 S12: 0.1118 S13: 0.5498 REMARK 3 S21: -0.7022 S22: -0.9857 S23: 0.2929 REMARK 3 S31: 0.7580 S32: 0.8371 S33: -0.0308 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 426 THROUGH 499 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.5369 96.2203 -32.3770 REMARK 3 T TENSOR REMARK 3 T11: 2.5412 T22: 2.5274 REMARK 3 T33: 0.2739 T12: 1.5759 REMARK 3 T13: -0.0469 T23: 0.1472 REMARK 3 L TENSOR REMARK 3 L11: 1.6441 L22: 1.6058 REMARK 3 L33: 0.9550 L12: 1.1461 REMARK 3 L13: -0.9961 L23: -0.6734 REMARK 3 S TENSOR REMARK 3 S11: 1.0328 S12: 1.1669 S13: 0.5389 REMARK 3 S21: -1.0622 S22: -0.9412 S23: 1.0776 REMARK 3 S31: 0.6991 S32: 1.0183 S33: -0.2413 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -80.8553 61.2278 -45.5519 REMARK 3 T TENSOR REMARK 3 T11: 0.6516 T22: 1.2009 REMARK 3 T33: 1.0745 T12: 0.0090 REMARK 3 T13: 0.1009 T23: 0.1179 REMARK 3 L TENSOR REMARK 3 L11: 2.6996 L22: 6.3295 REMARK 3 L33: 2.7561 L12: -1.6649 REMARK 3 L13: 0.0952 L23: 2.0850 REMARK 3 S TENSOR REMARK 3 S11: 0.2729 S12: 0.3428 S13: 0.0614 REMARK 3 S21: 0.4917 S22: -0.8710 S23: 0.5988 REMARK 3 S31: 0.4987 S32: -0.5816 S33: 0.4775 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 18 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -71.0946 61.9869 -52.1135 REMARK 3 T TENSOR REMARK 3 T11: 0.5844 T22: 0.6955 REMARK 3 T33: 0.8218 T12: -0.0799 REMARK 3 T13: -0.0238 T23: 0.0429 REMARK 3 L TENSOR REMARK 3 L11: 3.8194 L22: 4.8766 REMARK 3 L33: 4.3322 L12: -0.2425 REMARK 3 L13: -2.7666 L23: -0.2158 REMARK 3 S TENSOR REMARK 3 S11: -0.1985 S12: 0.6003 S13: 0.2766 REMARK 3 S21: 0.1805 S22: 0.1252 S23: 0.3238 REMARK 3 S31: 0.1281 S32: -0.3429 S33: 0.0539 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 74 THROUGH 89 ) REMARK 3 ORIGIN FOR THE GROUP (A): -70.1901 61.0963 -43.3655 REMARK 3 T TENSOR REMARK 3 T11: 0.8635 T22: 0.8211 REMARK 3 T33: 0.9086 T12: -0.0781 REMARK 3 T13: -0.1210 T23: 0.0999 REMARK 3 L TENSOR REMARK 3 L11: 8.8961 L22: 3.1502 REMARK 3 L33: 5.5857 L12: -3.8670 REMARK 3 L13: -3.0291 L23: 3.8485 REMARK 3 S TENSOR REMARK 3 S11: -0.6626 S12: -0.6545 S13: 0.6569 REMARK 3 S21: 0.7085 S22: 0.9055 S23: 0.5284 REMARK 3 S31: 0.7432 S32: 0.4582 S33: -0.1168 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 90 THROUGH 104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -80.8478 69.3550 -49.0916 REMARK 3 T TENSOR REMARK 3 T11: 0.8386 T22: 0.7740 REMARK 3 T33: 1.1051 T12: -0.1037 REMARK 3 T13: -0.0875 T23: -0.0456 REMARK 3 L TENSOR REMARK 3 L11: 4.1717 L22: 0.4423 REMARK 3 L33: 3.0829 L12: -1.3752 REMARK 3 L13: -0.0545 L23: -0.2326 REMARK 3 S TENSOR REMARK 3 S11: -0.4230 S12: -0.5998 S13: 0.6051 REMARK 3 S21: -0.2853 S22: 0.4209 S23: 0.0055 REMARK 3 S31: 0.1659 S32: -0.4388 S33: -0.1886 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 105 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -64.5303 61.3152 -58.4424 REMARK 3 T TENSOR REMARK 3 T11: 0.7693 T22: 0.9414 REMARK 3 T33: 0.8014 T12: 0.0100 REMARK 3 T13: -0.0527 T23: -0.0727 REMARK 3 L TENSOR REMARK 3 L11: 9.4226 L22: 4.8911 REMARK 3 L33: 4.6251 L12: -4.9858 REMARK 3 L13: 3.4561 L23: -1.9175 REMARK 3 S TENSOR REMARK 3 S11: -0.3864 S12: 1.5213 S13: 0.5687 REMARK 3 S21: -0.8592 S22: 0.4893 S23: -0.6923 REMARK 3 S31: -0.3884 S32: 0.1079 S33: -0.4314 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 114 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -73.8559 57.3931 -58.7913 REMARK 3 T TENSOR REMARK 3 T11: 0.7642 T22: 0.9034 REMARK 3 T33: 0.9988 T12: 0.0177 REMARK 3 T13: 0.0317 T23: -0.1547 REMARK 3 L TENSOR REMARK 3 L11: 5.8036 L22: 7.4196 REMARK 3 L33: 3.6813 L12: 3.3322 REMARK 3 L13: -0.8068 L23: -4.8731 REMARK 3 S TENSOR REMARK 3 S11: -0.1643 S12: -0.2850 S13: 1.0655 REMARK 3 S21: -0.7649 S22: 0.3551 S23: 0.8469 REMARK 3 S31: 0.4198 S32: 0.2902 S33: -0.3193 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 124 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -87.6580 69.4097 -45.9707 REMARK 3 T TENSOR REMARK 3 T11: 0.8091 T22: 0.2068 REMARK 3 T33: 1.3948 T12: 0.6332 REMARK 3 T13: 0.1348 T23: 0.1415 REMARK 3 L TENSOR REMARK 3 L11: 1.1384 L22: 4.6713 REMARK 3 L33: 3.2961 L12: -2.1560 REMARK 3 L13: 0.2828 L23: -1.9388 REMARK 3 S TENSOR REMARK 3 S11: -0.0936 S12: 0.5464 S13: 0.6296 REMARK 3 S21: -0.2127 S22: 0.0194 S23: 0.5179 REMARK 3 S31: -0.1786 S32: -0.3623 S33: -0.2733 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.6890 34.9442 -45.9159 REMARK 3 T TENSOR REMARK 3 T11: 0.8039 T22: 1.6402 REMARK 3 T33: 1.1105 T12: -0.0990 REMARK 3 T13: 0.0288 T23: 0.1775 REMARK 3 L TENSOR REMARK 3 L11: 3.3769 L22: 6.3688 REMARK 3 L33: 2.3432 L12: 1.6618 REMARK 3 L13: -1.1792 L23: -0.0710 REMARK 3 S TENSOR REMARK 3 S11: 0.3378 S12: -0.1177 S13: -0.5029 REMARK 3 S21: -0.1452 S22: -0.9642 S23: -1.9185 REMARK 3 S31: 0.0647 S32: 0.8778 S33: 0.3522 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 70 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.6322 35.8378 -52.3008 REMARK 3 T TENSOR REMARK 3 T11: 0.6925 T22: 1.0904 REMARK 3 T33: 0.9660 T12: -0.0395 REMARK 3 T13: 0.1056 T23: 0.0634 REMARK 3 L TENSOR REMARK 3 L11: 4.7542 L22: 4.5822 REMARK 3 L33: 3.0697 L12: -1.3009 REMARK 3 L13: 2.5105 L23: -0.1944 REMARK 3 S TENSOR REMARK 3 S11: -0.2640 S12: 0.1533 S13: -0.2677 REMARK 3 S21: -0.5208 S22: 0.1087 S23: -0.2811 REMARK 3 S31: 0.1681 S32: 0.5093 S33: 0.2070 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 71 THROUGH 89 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.0123 33.1146 -43.8639 REMARK 3 T TENSOR REMARK 3 T11: 0.7646 T22: 1.1182 REMARK 3 T33: 0.9477 T12: -0.0533 REMARK 3 T13: -0.0219 T23: 0.0212 REMARK 3 L TENSOR REMARK 3 L11: 5.5463 L22: 8.9476 REMARK 3 L33: 4.6978 L12: -3.5861 REMARK 3 L13: -1.2964 L23: 0.4406 REMARK 3 S TENSOR REMARK 3 S11: 0.2625 S12: -0.7495 S13: 0.2411 REMARK 3 S21: 0.0787 S22: 0.2693 S23: -0.7533 REMARK 3 S31: 0.1419 S32: 0.3733 S33: -0.4430 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 90 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.7830 32.6902 -53.7666 REMARK 3 T TENSOR REMARK 3 T11: 0.7164 T22: 0.9809 REMARK 3 T33: 0.9916 T12: 0.0266 REMARK 3 T13: 0.1061 T23: -0.0972 REMARK 3 L TENSOR REMARK 3 L11: 3.8778 L22: 4.2514 REMARK 3 L33: 5.2642 L12: -0.8748 REMARK 3 L13: 0.9862 L23: -0.8807 REMARK 3 S TENSOR REMARK 3 S11: 0.4004 S12: 0.6507 S13: -0.1453 REMARK 3 S21: -0.7936 S22: -0.3742 S23: -0.4029 REMARK 3 S31: 0.3096 S32: 1.0301 S33: 0.2390 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 1 THROUGH 9 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.6636 82.6991-128.5997 REMARK 3 T TENSOR REMARK 3 T11: 1.7068 T22: 0.5161 REMARK 3 T33: 1.5412 T12: -0.5277 REMARK 3 T13: -0.0480 T23: 0.2389 REMARK 3 L TENSOR REMARK 3 L11: 9.8905 L22: 1.7268 REMARK 3 L33: 2.5298 L12: -3.8079 REMARK 3 L13: -2.9105 L23: 0.4601 REMARK 3 S TENSOR REMARK 3 S11: 0.7879 S12: -0.7211 S13: 2.2137 REMARK 3 S21: -0.8228 S22: -0.6367 S23: 1.5077 REMARK 3 S31: -1.7048 S32: 0.4542 S33: 0.2901 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 10 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -53.2675 77.6555-126.9051 REMARK 3 T TENSOR REMARK 3 T11: 1.0698 T22: 0.8241 REMARK 3 T33: 1.3530 T12: -0.0945 REMARK 3 T13: -0.2304 T23: 0.2711 REMARK 3 L TENSOR REMARK 3 L11: 3.6914 L22: 2.4251 REMARK 3 L33: 2.8070 L12: -0.4130 REMARK 3 L13: 0.3639 L23: -1.1494 REMARK 3 S TENSOR REMARK 3 S11: -0.3693 S12: -0.0891 S13: 0.5205 REMARK 3 S21: -0.1784 S22: 0.0595 S23: 0.8023 REMARK 3 S31: -0.5954 S32: -0.0291 S33: 0.2390 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 74 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.2651 75.5244-134.4614 REMARK 3 T TENSOR REMARK 3 T11: 0.9866 T22: 1.0405 REMARK 3 T33: 1.3486 T12: -0.1398 REMARK 3 T13: -0.2445 T23: 0.3414 REMARK 3 L TENSOR REMARK 3 L11: 5.4855 L22: 7.1194 REMARK 3 L33: 8.7832 L12: 2.0918 REMARK 3 L13: 0.1840 L23: -0.2182 REMARK 3 S TENSOR REMARK 3 S11: -0.3643 S12: 0.7231 S13: 1.2639 REMARK 3 S21: -0.6026 S22: 0.6442 S23: 1.1177 REMARK 3 S31: -1.7759 S32: -0.5829 S33: -0.1206 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 91 THROUGH 105 ) REMARK 3 ORIGIN FOR THE GROUP (A): -58.3613 84.8359-127.3453 REMARK 3 T TENSOR REMARK 3 T11: 1.6093 T22: 0.8537 REMARK 3 T33: 2.1981 T12: 0.0879 REMARK 3 T13: -0.2197 T23: 0.0741 REMARK 3 L TENSOR REMARK 3 L11: 0.1093 L22: 0.0288 REMARK 3 L33: 0.4717 L12: -0.0800 REMARK 3 L13: -0.2317 L23: 0.1166 REMARK 3 S TENSOR REMARK 3 S11: -0.0264 S12: 0.2838 S13: -0.0741 REMARK 3 S21: -0.1065 S22: 0.0939 S23: 1.5719 REMARK 3 S31: -0.8165 S32: 0.1819 S33: -0.1910 REMARK 3 TLS GROUP : 50 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 106 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -49.8327 75.7299-119.0587 REMARK 3 T TENSOR REMARK 3 T11: 1.4526 T22: 0.7376 REMARK 3 T33: 1.1207 T12: -0.0005 REMARK 3 T13: -0.0905 T23: 0.0812 REMARK 3 L TENSOR REMARK 3 L11: 8.9526 L22: 4.2152 REMARK 3 L33: 4.3418 L12: -0.7013 REMARK 3 L13: -0.2855 L23: 4.2147 REMARK 3 S TENSOR REMARK 3 S11: 0.2702 S12: 0.0359 S13: 1.3257 REMARK 3 S21: 0.4650 S22: 0.4127 S23: 0.1733 REMARK 3 S31: 0.3187 S32: -0.0775 S33: -0.7587 REMARK 3 TLS GROUP : 51 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 124 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -60.4670 92.4641-132.3020 REMARK 3 T TENSOR REMARK 3 T11: 1.5168 T22: 0.2100 REMARK 3 T33: 2.8970 T12: 0.2286 REMARK 3 T13: -0.8303 T23: 0.0582 REMARK 3 L TENSOR REMARK 3 L11: 1.4158 L22: 6.0232 REMARK 3 L33: 1.8335 L12: -0.8356 REMARK 3 L13: -0.2788 L23: 0.0070 REMARK 3 S TENSOR REMARK 3 S11: 0.3372 S12: 0.2296 S13: -0.4249 REMARK 3 S21: -0.3410 S22: -0.0868 S23: 0.9540 REMARK 3 S31: -0.2341 S32: -0.3010 S33: 0.0225 REMARK 3 TLS GROUP : 52 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.0199 6.7951-127.0250 REMARK 3 T TENSOR REMARK 3 T11: 1.0218 T22: 0.8989 REMARK 3 T33: 0.9561 T12: 0.0332 REMARK 3 T13: -0.1949 T23: 0.0441 REMARK 3 L TENSOR REMARK 3 L11: 5.3573 L22: 5.0165 REMARK 3 L33: 3.4936 L12: -3.6392 REMARK 3 L13: -0.4880 L23: 2.2646 REMARK 3 S TENSOR REMARK 3 S11: -0.4772 S12: -0.8039 S13: -0.4341 REMARK 3 S21: -0.3478 S22: 0.6928 S23: 0.1551 REMARK 3 S31: 0.2704 S32: 0.1856 S33: -0.3063 REMARK 3 TLS GROUP : 53 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 18 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.8645 18.8653-123.8649 REMARK 3 T TENSOR REMARK 3 T11: 0.6240 T22: 0.6301 REMARK 3 T33: 0.9467 T12: 0.0387 REMARK 3 T13: -0.0067 T23: 0.0083 REMARK 3 L TENSOR REMARK 3 L11: 2.6110 L22: 6.7181 REMARK 3 L33: 2.7415 L12: -0.0332 REMARK 3 L13: 1.3488 L23: 0.0131 REMARK 3 S TENSOR REMARK 3 S11: -0.5655 S12: -0.4988 S13: -0.8147 REMARK 3 S21: -0.2413 S22: 0.0902 S23: 2.0059 REMARK 3 S31: -0.1659 S32: -0.1341 S33: 0.4004 REMARK 3 TLS GROUP : 54 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 40 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.9218 8.3717-115.5791 REMARK 3 T TENSOR REMARK 3 T11: 1.0211 T22: 0.9687 REMARK 3 T33: 0.9118 T12: 0.1726 REMARK 3 T13: -0.2390 T23: -0.0078 REMARK 3 L TENSOR REMARK 3 L11: 7.7993 L22: 2.1745 REMARK 3 L33: 8.3863 L12: 1.8058 REMARK 3 L13: -2.8259 L23: 1.7509 REMARK 3 S TENSOR REMARK 3 S11: 0.3137 S12: -0.3438 S13: -1.0600 REMARK 3 S21: 1.3928 S22: -0.6760 S23: 0.2152 REMARK 3 S31: 1.7145 S32: 1.2008 S33: 0.2011 REMARK 3 TLS GROUP : 55 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 52 THROUGH 104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.2974 15.4914-124.2973 REMARK 3 T TENSOR REMARK 3 T11: 0.5851 T22: 0.7779 REMARK 3 T33: 0.9592 T12: -0.0097 REMARK 3 T13: -0.0214 T23: 0.0156 REMARK 3 L TENSOR REMARK 3 L11: 3.6033 L22: 3.1694 REMARK 3 L33: 1.2317 L12: -0.3934 REMARK 3 L13: -0.9714 L23: 0.9107 REMARK 3 S TENSOR REMARK 3 S11: -0.2379 S12: -0.2932 S13: -0.5091 REMARK 3 S21: 0.0682 S22: 0.2660 S23: 0.0761 REMARK 3 S31: -0.0966 S32: 0.2302 S33: -0.0334 REMARK 3 TLS GROUP : 56 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 105 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.9055 18.5995-114.9805 REMARK 3 T TENSOR REMARK 3 T11: 0.7358 T22: 1.0266 REMARK 3 T33: 0.8059 T12: -0.0192 REMARK 3 T13: 0.0365 T23: 0.0187 REMARK 3 L TENSOR REMARK 3 L11: 8.7889 L22: 2.1099 REMARK 3 L33: 6.0836 L12: 0.9870 REMARK 3 L13: 1.5145 L23: -0.5543 REMARK 3 S TENSOR REMARK 3 S11: 0.1035 S12: -0.7396 S13: -0.5436 REMARK 3 S21: 1.4901 S22: 0.4928 S23: 0.0513 REMARK 3 S31: 0.5632 S32: -0.3677 S33: -0.6263 REMARK 3 TLS GROUP : 57 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 124 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.1929 0.1064-125.5758 REMARK 3 T TENSOR REMARK 3 T11: 0.7815 T22: 0.4146 REMARK 3 T33: 1.3385 T12: 0.0567 REMARK 3 T13: -0.0079 T23: 0.0937 REMARK 3 L TENSOR REMARK 3 L11: 4.8086 L22: 1.7309 REMARK 3 L33: 5.8954 L12: -0.9313 REMARK 3 L13: -2.9581 L23: 1.5843 REMARK 3 S TENSOR REMARK 3 S11: 0.1974 S12: 0.2957 S13: -0.5480 REMARK 3 S21: 0.2685 S22: -0.4265 S23: -1.5865 REMARK 3 S31: 0.1796 S32: 0.1093 S33: 0.2852 REMARK 3 TLS GROUP : 58 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 1 THROUGH 9 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.4025 7.8218 -20.0085 REMARK 3 T TENSOR REMARK 3 T11: 1.8102 T22: 1.6223 REMARK 3 T33: 1.8730 T12: -0.1256 REMARK 3 T13: 0.8063 T23: -0.5092 REMARK 3 L TENSOR REMARK 3 L11: 2.6834 L22: 6.6768 REMARK 3 L33: 6.0329 L12: 1.4032 REMARK 3 L13: -3.6140 L23: 0.7532 REMARK 3 S TENSOR REMARK 3 S11: -1.0648 S12: -0.0316 S13: -1.3881 REMARK 3 S21: -0.3175 S22: -0.1837 S23: 0.0861 REMARK 3 S31: 1.1890 S32: 0.7781 S33: 0.7786 REMARK 3 TLS GROUP : 59 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 10 THROUGH 23 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.0977 4.4637 -12.6647 REMARK 3 T TENSOR REMARK 3 T11: 1.5772 T22: 2.2443 REMARK 3 T33: 1.3951 T12: -0.1847 REMARK 3 T13: -0.3029 T23: -0.0139 REMARK 3 L TENSOR REMARK 3 L11: 1.8069 L22: 7.8616 REMARK 3 L33: 4.8316 L12: 0.1831 REMARK 3 L13: -2.7544 L23: 1.9350 REMARK 3 S TENSOR REMARK 3 S11: -0.1300 S12: 0.2368 S13: -0.0911 REMARK 3 S21: 2.0212 S22: 0.0443 S23: -0.9667 REMARK 3 S31: 1.5046 S32: 0.1471 S33: -0.1096 REMARK 3 TLS GROUP : 60 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 24 THROUGH 34 ) REMARK 3 ORIGIN FOR THE GROUP (A): -48.4079 13.2178 -18.3639 REMARK 3 T TENSOR REMARK 3 T11: 1.8888 T22: 1.5243 REMARK 3 T33: 1.2540 T12: -0.6634 REMARK 3 T13: -0.3799 T23: 0.3188 REMARK 3 L TENSOR REMARK 3 L11: 4.3425 L22: 5.4270 REMARK 3 L33: 4.8294 L12: -1.6195 REMARK 3 L13: 4.2049 L23: 0.3246 REMARK 3 S TENSOR REMARK 3 S11: -0.1223 S12: 0.9262 S13: -0.8574 REMARK 3 S21: -0.0048 S22: -0.6083 S23: 0.7683 REMARK 3 S31: 1.0207 S32: 1.5884 S33: 0.7490 REMARK 3 TLS GROUP : 61 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 35 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.7080 0.5870 -12.6368 REMARK 3 T TENSOR REMARK 3 T11: 2.3234 T22: 1.9703 REMARK 3 T33: 1.1062 T12: 0.5442 REMARK 3 T13: 0.1633 T23: 0.1884 REMARK 3 L TENSOR REMARK 3 L11: 8.4143 L22: 4.1704 REMARK 3 L33: 4.1845 L12: -4.2159 REMARK 3 L13: -2.0827 L23: 2.6752 REMARK 3 S TENSOR REMARK 3 S11: -0.7390 S12: 0.0187 S13: -0.2657 REMARK 3 S21: 0.1877 S22: 0.1635 S23: -0.2634 REMARK 3 S31: 2.9858 S32: 0.7130 S33: 0.5094 REMARK 3 TLS GROUP : 62 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 52 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.8276 3.6646 -8.6745 REMARK 3 T TENSOR REMARK 3 T11: 1.5220 T22: 1.5311 REMARK 3 T33: 1.0886 T12: -0.1508 REMARK 3 T13: -0.2785 T23: 0.0447 REMARK 3 L TENSOR REMARK 3 L11: 2.8605 L22: 1.7575 REMARK 3 L33: 1.6764 L12: -0.6005 REMARK 3 L13: 0.6067 L23: 0.9568 REMARK 3 S TENSOR REMARK 3 S11: 0.0054 S12: -0.7372 S13: 0.3639 REMARK 3 S21: 0.3684 S22: 0.1758 S23: -0.4382 REMARK 3 S31: 0.7529 S32: 0.3702 S33: -0.0984 REMARK 3 TLS GROUP : 63 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.3552 131.5181 -21.4862 REMARK 3 T TENSOR REMARK 3 T11: 1.6489 T22: 1.5366 REMARK 3 T33: 1.6753 T12: 0.0503 REMARK 3 T13: -0.1358 T23: -0.0160 REMARK 3 L TENSOR REMARK 3 L11: 2.8637 L22: 2.3861 REMARK 3 L33: 2.3921 L12: -2.3586 REMARK 3 L13: 0.8820 L23: -1.6988 REMARK 3 S TENSOR REMARK 3 S11: 0.0381 S12: 0.9010 S13: -2.4421 REMARK 3 S21: 0.6293 S22: -0.3325 S23: -0.0061 REMARK 3 S31: -2.3422 S32: 0.5405 S33: 0.2281 REMARK 3 TLS GROUP : 64 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 8 THROUGH 70 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.6871 133.6822 -11.7001 REMARK 3 T TENSOR REMARK 3 T11: 1.5686 T22: 1.7972 REMARK 3 T33: 0.9996 T12: -0.1071 REMARK 3 T13: 0.1658 T23: 0.2019 REMARK 3 L TENSOR REMARK 3 L11: 3.9065 L22: 3.5529 REMARK 3 L33: 2.9969 L12: -0.7300 REMARK 3 L13: 1.0174 L23: 0.6368 REMARK 3 S TENSOR REMARK 3 S11: 0.1564 S12: 0.2876 S13: -0.5182 REMARK 3 S21: -0.8460 S22: -0.1539 S23: -1.0351 REMARK 3 S31: -1.8069 S32: 1.0132 S33: -0.0517 REMARK 3 TLS GROUP : 65 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 71 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.3152 141.2416 -8.8787 REMARK 3 T TENSOR REMARK 3 T11: 1.9843 T22: 1.8844 REMARK 3 T33: 0.9646 T12: 0.2048 REMARK 3 T13: -0.1853 T23: -0.1989 REMARK 3 L TENSOR REMARK 3 L11: 4.1915 L22: 4.6082 REMARK 3 L33: 3.2418 L12: 1.1078 REMARK 3 L13: -2.2678 L23: -0.5985 REMARK 3 S TENSOR REMARK 3 S11: 0.0012 S12: 0.8855 S13: -0.0010 REMARK 3 S21: 0.3517 S22: 1.0284 S23: -0.5262 REMARK 3 S31: -1.6850 S32: -1.3712 S33: -0.7967 REMARK 3 TLS GROUP : 66 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 99 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.8553 131.0861 -13.3620 REMARK 3 T TENSOR REMARK 3 T11: 1.4482 T22: 2.0395 REMARK 3 T33: 1.2793 T12: -0.0077 REMARK 3 T13: 0.0351 T23: 0.2343 REMARK 3 L TENSOR REMARK 3 L11: 2.3728 L22: 5.6908 REMARK 3 L33: 2.0307 L12: 1.9186 REMARK 3 L13: 1.7824 L23: 3.1954 REMARK 3 S TENSOR REMARK 3 S11: -0.3232 S12: -0.3798 S13: -0.3582 REMARK 3 S21: -0.1247 S22: 0.6971 S23: -0.6942 REMARK 3 S31: -0.7179 S32: 1.0605 S33: -0.6657 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 8RVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1292136192. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUN-20 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83505 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.190 REMARK 200 RESOLUTION RANGE LOW (A) : 49.320 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 13.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.3900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.19 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.97 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS PROPANE PH 7.5, 200 MM REMARK 280 SODIUM SULFATE, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 83.76000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.21000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 83.76000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 84.21000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, J 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K 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: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, 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 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 MET A 1 REMARK 465 ASN A 501 REMARK 465 LEU A 502 REMARK 465 TYR A 503 REMARK 465 PHE A 504 REMARK 465 GLN A 505 REMARK 465 SER A 506 REMARK 465 GLY A 507 REMARK 465 GLY A 508 REMARK 465 HIS A 509 REMARK 465 HIS A 510 REMARK 465 HIS A 511 REMARK 465 HIS A 512 REMARK 465 HIS A 513 REMARK 465 HIS A 514 REMARK 465 MET B 1 REMARK 465 ARG B 91 REMARK 465 THR B 92 REMARK 465 GLY B 93 REMARK 465 LEU B 94 REMARK 465 PHE B 95 REMARK 465 LYS B 96 REMARK 465 ASP B 97 REMARK 465 GLY B 98 REMARK 465 GLU B 99 REMARK 465 ALA B 100 REMARK 465 THR B 101 REMARK 465 TYR B 102 REMARK 465 ALA B 103 REMARK 465 PRO B 104 REMARK 465 GLY B 105 REMARK 465 ASP B 106 REMARK 465 THR B 107 REMARK 465 VAL B 108 REMARK 465 LEU B 109 REMARK 465 VAL B 110 REMARK 465 THR B 111 REMARK 465 THR B 112 REMARK 465 ASP B 113 REMARK 465 PRO B 114 REMARK 465 ALA B 115 REMARK 465 PHE B 116 REMARK 465 GLU B 117 REMARK 465 LYS B 118 REMARK 465 ILE B 119 REMARK 465 GLY B 120 REMARK 465 THR B 121 REMARK 465 LYS B 122 REMARK 465 GLU B 123 REMARK 465 LYS B 124 REMARK 465 PHE B 125 REMARK 465 TYR B 126 REMARK 465 VAL B 127 REMARK 465 ASP B 128 REMARK 465 TYR B 129 REMARK 465 PRO B 130 REMARK 465 GLN B 131 REMARK 465 LEU B 132 REMARK 465 PRO B 133 REMARK 465 ASN B 134 REMARK 465 VAL B 135 REMARK 465 VAL B 136 REMARK 465 ARG B 137 REMARK 465 PRO B 138 REMARK 465 GLY B 139 REMARK 465 GLY B 140 REMARK 465 LEU B 141 REMARK 465 ILE B 142 REMARK 465 TYR B 143 REMARK 465 VAL B 144 REMARK 465 ASP B 145 REMARK 465 ASP B 146 REMARK 465 GLY B 147 REMARK 465 VAL B 148 REMARK 465 LEU B 149 REMARK 465 THR B 150 REMARK 465 LEU B 151 REMARK 465 ARG B 152 REMARK 465 VAL B 153 REMARK 465 LEU B 154 REMARK 465 SER B 155 REMARK 465 LYS B 156 REMARK 465 GLU B 157 REMARK 465 ASP B 158 REMARK 465 ASP B 159 REMARK 465 CYS B 160 REMARK 465 THR B 161 REMARK 465 LEU B 162 REMARK 465 LYS B 163 REMARK 465 CYS B 164 REMARK 465 HIS B 165 REMARK 465 VAL B 166 REMARK 465 ASN B 167 REMARK 465 ASN B 168 REMARK 465 HIS B 169 REMARK 465 HIS B 170 REMARK 465 ARG B 171 REMARK 465 LEU B 172 REMARK 465 THR B 173 REMARK 465 ASP B 174 REMARK 465 ARG B 175 REMARK 465 LYS B 176 REMARK 465 GLY B 177 REMARK 465 ILE B 178 REMARK 465 ASN B 179 REMARK 465 LEU B 180 REMARK 465 PRO B 181 REMARK 465 GLY B 182 REMARK 465 CYS B 183 REMARK 465 GLU B 184 REMARK 465 VAL B 185 REMARK 465 ASP B 186 REMARK 465 LEU B 502 REMARK 465 TYR B 503 REMARK 465 PHE B 504 REMARK 465 GLN B 505 REMARK 465 SER B 506 REMARK 465 GLY B 507 REMARK 465 GLY B 508 REMARK 465 HIS B 509 REMARK 465 HIS B 510 REMARK 465 HIS B 511 REMARK 465 HIS B 512 REMARK 465 HIS B 513 REMARK 465 HIS B 514 REMARK 465 MET C 1 REMARK 465 GLU C 500 REMARK 465 ASN C 501 REMARK 465 LEU C 502 REMARK 465 TYR C 503 REMARK 465 PHE C 504 REMARK 465 GLN C 505 REMARK 465 SER C 506 REMARK 465 GLY C 507 REMARK 465 GLY C 508 REMARK 465 HIS C 509 REMARK 465 HIS C 510 REMARK 465 HIS C 511 REMARK 465 HIS C 512 REMARK 465 HIS C 513 REMARK 465 HIS C 514 REMARK 465 MET D 1 REMARK 465 GLU D 500 REMARK 465 ASN D 501 REMARK 465 LEU D 502 REMARK 465 TYR D 503 REMARK 465 PHE D 504 REMARK 465 GLN D 505 REMARK 465 SER D 506 REMARK 465 GLY D 507 REMARK 465 GLY D 508 REMARK 465 HIS D 509 REMARK 465 HIS D 510 REMARK 465 HIS D 511 REMARK 465 HIS D 512 REMARK 465 HIS D 513 REMARK 465 HIS D 514 REMARK 465 MET E 1 REMARK 465 ILE E 90 REMARK 465 ARG E 91 REMARK 465 THR E 92 REMARK 465 GLY E 93 REMARK 465 LEU E 94 REMARK 465 PHE E 95 REMARK 465 LYS E 96 REMARK 465 ASP E 97 REMARK 465 GLY E 98 REMARK 465 GLU E 99 REMARK 465 ALA E 100 REMARK 465 THR E 101 REMARK 465 TYR E 102 REMARK 465 ALA E 103 REMARK 465 PRO E 104 REMARK 465 GLY E 105 REMARK 465 ASP E 106 REMARK 465 THR E 107 REMARK 465 VAL E 108 REMARK 465 LEU E 109 REMARK 465 VAL E 110 REMARK 465 THR E 111 REMARK 465 THR E 112 REMARK 465 ASP E 113 REMARK 465 PRO E 114 REMARK 465 ALA E 115 REMARK 465 PHE E 116 REMARK 465 GLU E 117 REMARK 465 LYS E 118 REMARK 465 ILE E 119 REMARK 465 GLY E 120 REMARK 465 THR E 121 REMARK 465 LYS E 122 REMARK 465 GLU E 123 REMARK 465 LYS E 124 REMARK 465 PHE E 125 REMARK 465 TYR E 126 REMARK 465 VAL E 127 REMARK 465 ASP E 128 REMARK 465 TYR E 129 REMARK 465 PRO E 130 REMARK 465 GLN E 131 REMARK 465 LEU E 132 REMARK 465 PRO E 133 REMARK 465 ASN E 134 REMARK 465 VAL E 135 REMARK 465 VAL E 136 REMARK 465 ARG E 137 REMARK 465 PRO E 138 REMARK 465 GLY E 139 REMARK 465 GLY E 140 REMARK 465 LEU E 141 REMARK 465 ILE E 142 REMARK 465 TYR E 143 REMARK 465 VAL E 144 REMARK 465 ASP E 145 REMARK 465 ASP E 146 REMARK 465 GLY E 147 REMARK 465 VAL E 148 REMARK 465 LEU E 149 REMARK 465 THR E 150 REMARK 465 LEU E 151 REMARK 465 ARG E 152 REMARK 465 VAL E 153 REMARK 465 LEU E 154 REMARK 465 SER E 155 REMARK 465 LYS E 156 REMARK 465 GLU E 157 REMARK 465 ASP E 158 REMARK 465 ASP E 159 REMARK 465 CYS E 160 REMARK 465 THR E 161 REMARK 465 LEU E 162 REMARK 465 LYS E 163 REMARK 465 CYS E 164 REMARK 465 HIS E 165 REMARK 465 VAL E 166 REMARK 465 ASN E 167 REMARK 465 ASN E 168 REMARK 465 HIS E 169 REMARK 465 HIS E 170 REMARK 465 ARG E 171 REMARK 465 LEU E 172 REMARK 465 THR E 173 REMARK 465 ASP E 174 REMARK 465 ARG E 175 REMARK 465 LYS E 176 REMARK 465 GLY E 177 REMARK 465 ILE E 178 REMARK 465 ASN E 179 REMARK 465 LEU E 180 REMARK 465 PRO E 181 REMARK 465 GLY E 182 REMARK 465 CYS E 183 REMARK 465 GLU E 184 REMARK 465 VAL E 185 REMARK 465 ASP E 186 REMARK 465 LEU E 187 REMARK 465 PRO E 188 REMARK 465 SER E 485 REMARK 465 VAL E 486 REMARK 465 LYS E 487 REMARK 465 ASN E 501 REMARK 465 LEU E 502 REMARK 465 TYR E 503 REMARK 465 PHE E 504 REMARK 465 GLN E 505 REMARK 465 SER E 506 REMARK 465 GLY E 507 REMARK 465 GLY E 508 REMARK 465 HIS E 509 REMARK 465 HIS E 510 REMARK 465 HIS E 511 REMARK 465 HIS E 512 REMARK 465 HIS E 513 REMARK 465 HIS E 514 REMARK 465 MET F 1 REMARK 465 ILE F 90 REMARK 465 ARG F 91 REMARK 465 THR F 92 REMARK 465 GLY F 93 REMARK 465 LEU F 94 REMARK 465 PHE F 95 REMARK 465 LYS F 96 REMARK 465 ASP F 97 REMARK 465 GLY F 98 REMARK 465 GLU F 99 REMARK 465 ALA F 100 REMARK 465 THR F 101 REMARK 465 TYR F 102 REMARK 465 ALA F 103 REMARK 465 PRO F 104 REMARK 465 GLY F 105 REMARK 465 ASP F 106 REMARK 465 THR F 107 REMARK 465 VAL F 108 REMARK 465 LEU F 109 REMARK 465 VAL F 110 REMARK 465 THR F 111 REMARK 465 THR F 112 REMARK 465 ASP F 113 REMARK 465 PRO F 114 REMARK 465 ALA F 115 REMARK 465 PHE F 116 REMARK 465 GLU F 117 REMARK 465 LYS F 118 REMARK 465 ILE F 119 REMARK 465 GLY F 120 REMARK 465 THR F 121 REMARK 465 LYS F 122 REMARK 465 GLU F 123 REMARK 465 LYS F 124 REMARK 465 PHE F 125 REMARK 465 TYR F 126 REMARK 465 VAL F 127 REMARK 465 ASP F 128 REMARK 465 TYR F 129 REMARK 465 PRO F 130 REMARK 465 GLN F 131 REMARK 465 LEU F 132 REMARK 465 PRO F 133 REMARK 465 ASN F 134 REMARK 465 VAL F 135 REMARK 465 VAL F 136 REMARK 465 ARG F 137 REMARK 465 PRO F 138 REMARK 465 GLY F 139 REMARK 465 GLY F 140 REMARK 465 LEU F 141 REMARK 465 ILE F 142 REMARK 465 TYR F 143 REMARK 465 VAL F 144 REMARK 465 ASP F 145 REMARK 465 ASP F 146 REMARK 465 GLY F 147 REMARK 465 VAL F 148 REMARK 465 LEU F 149 REMARK 465 THR F 150 REMARK 465 LEU F 151 REMARK 465 ARG F 152 REMARK 465 VAL F 153 REMARK 465 LEU F 154 REMARK 465 SER F 155 REMARK 465 LYS F 156 REMARK 465 GLU F 157 REMARK 465 ASP F 158 REMARK 465 ASP F 159 REMARK 465 CYS F 160 REMARK 465 THR F 161 REMARK 465 LEU F 162 REMARK 465 LYS F 163 REMARK 465 CYS F 164 REMARK 465 HIS F 165 REMARK 465 VAL F 166 REMARK 465 ASN F 167 REMARK 465 ASN F 168 REMARK 465 HIS F 169 REMARK 465 HIS F 170 REMARK 465 ARG F 171 REMARK 465 LEU F 172 REMARK 465 THR F 173 REMARK 465 ASP F 174 REMARK 465 ARG F 175 REMARK 465 LYS F 176 REMARK 465 GLY F 177 REMARK 465 ILE F 178 REMARK 465 ASN F 179 REMARK 465 LEU F 180 REMARK 465 PRO F 181 REMARK 465 GLY F 182 REMARK 465 CYS F 183 REMARK 465 GLU F 184 REMARK 465 VAL F 185 REMARK 465 ASP F 186 REMARK 465 LEU F 187 REMARK 465 PRO F 188 REMARK 465 GLU F 500 REMARK 465 ASN F 501 REMARK 465 LEU F 502 REMARK 465 TYR F 503 REMARK 465 PHE F 504 REMARK 465 GLN F 505 REMARK 465 SER F 506 REMARK 465 GLY F 507 REMARK 465 GLY F 508 REMARK 465 HIS F 509 REMARK 465 HIS F 510 REMARK 465 HIS F 511 REMARK 465 HIS F 512 REMARK 465 HIS F 513 REMARK 465 HIS F 514 REMARK 465 ALA G 131 REMARK 465 ALA G 132 REMARK 465 ALA G 133 REMARK 465 TYR G 134 REMARK 465 PRO G 135 REMARK 465 TYR G 136 REMARK 465 ASP G 137 REMARK 465 VAL G 138 REMARK 465 PRO G 139 REMARK 465 ASP G 140 REMARK 465 TYR G 141 REMARK 465 GLY G 142 REMARK 465 SER G 143 REMARK 465 HIS G 144 REMARK 465 HIS G 145 REMARK 465 HIS G 146 REMARK 465 HIS G 147 REMARK 465 HIS G 148 REMARK 465 HIS G 149 REMARK 465 ALA H 131 REMARK 465 ALA H 132 REMARK 465 ALA H 133 REMARK 465 TYR H 134 REMARK 465 PRO H 135 REMARK 465 TYR H 136 REMARK 465 ASP H 137 REMARK 465 VAL H 138 REMARK 465 PRO H 139 REMARK 465 ASP H 140 REMARK 465 TYR H 141 REMARK 465 GLY H 142 REMARK 465 SER H 143 REMARK 465 HIS H 144 REMARK 465 HIS H 145 REMARK 465 HIS H 146 REMARK 465 HIS H 147 REMARK 465 HIS H 148 REMARK 465 HIS H 149 REMARK 465 ALA I 131 REMARK 465 ALA I 132 REMARK 465 ALA I 133 REMARK 465 TYR I 134 REMARK 465 PRO I 135 REMARK 465 TYR I 136 REMARK 465 ASP I 137 REMARK 465 VAL I 138 REMARK 465 PRO I 139 REMARK 465 ASP I 140 REMARK 465 TYR I 141 REMARK 465 GLY I 142 REMARK 465 SER I 143 REMARK 465 HIS I 144 REMARK 465 HIS I 145 REMARK 465 HIS I 146 REMARK 465 HIS I 147 REMARK 465 HIS I 148 REMARK 465 HIS I 149 REMARK 465 ALA J 132 REMARK 465 ALA J 133 REMARK 465 TYR J 134 REMARK 465 PRO J 135 REMARK 465 TYR J 136 REMARK 465 ASP J 137 REMARK 465 VAL J 138 REMARK 465 PRO J 139 REMARK 465 ASP J 140 REMARK 465 TYR J 141 REMARK 465 GLY J 142 REMARK 465 SER J 143 REMARK 465 HIS J 144 REMARK 465 HIS J 145 REMARK 465 HIS J 146 REMARK 465 HIS J 147 REMARK 465 HIS J 148 REMARK 465 HIS J 149 REMARK 465 ALA K 131 REMARK 465 ALA K 132 REMARK 465 ALA K 133 REMARK 465 TYR K 134 REMARK 465 PRO K 135 REMARK 465 TYR K 136 REMARK 465 ASP K 137 REMARK 465 VAL K 138 REMARK 465 PRO K 139 REMARK 465 ASP K 140 REMARK 465 TYR K 141 REMARK 465 GLY K 142 REMARK 465 SER K 143 REMARK 465 HIS K 144 REMARK 465 HIS K 145 REMARK 465 HIS K 146 REMARK 465 HIS K 147 REMARK 465 HIS K 148 REMARK 465 HIS K 149 REMARK 465 ALA L 131 REMARK 465 ALA L 132 REMARK 465 ALA L 133 REMARK 465 TYR L 134 REMARK 465 PRO L 135 REMARK 465 TYR L 136 REMARK 465 ASP L 137 REMARK 465 VAL L 138 REMARK 465 PRO L 139 REMARK 465 ASP L 140 REMARK 465 TYR L 141 REMARK 465 GLY L 142 REMARK 465 SER L 143 REMARK 465 HIS L 144 REMARK 465 HIS L 145 REMARK 465 HIS L 146 REMARK 465 HIS L 147 REMARK 465 HIS L 148 REMARK 465 HIS L 149 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 14 CG CD OE1 OE2 REMARK 470 LYS A 18 CG CD CE NZ REMARK 470 ARG A 91 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 96 CG CD CE NZ REMARK 470 LYS A 122 CG CD CE NZ REMARK 470 LYS A 124 CG CD CE NZ REMARK 470 ASN A 134 CG OD1 ND2 REMARK 470 ARG A 137 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 157 CG CD OE1 OE2 REMARK 470 LYS A 163 CG CD CE NZ REMARK 470 ASP A 174 CG OD1 OD2 REMARK 470 LYS A 176 CG CD CE NZ REMARK 470 ASN A 179 CG OD1 ND2 REMARK 470 GLU A 184 CG CD OE1 OE2 REMARK 470 ASP A 186 CG OD1 OD2 REMARK 470 GLU A 192 CG CD OE1 OE2 REMARK 470 LYS A 193 CG CD CE NZ REMARK 470 LYS A 196 CG CD CE NZ REMARK 470 LYS A 230 CG CD CE NZ REMARK 470 LYS A 338 CG CD CE NZ REMARK 470 LYS A 372 CG CD CE NZ REMARK 470 ARG A 405 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 454 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 455 CG CD OE1 OE2 REMARK 470 LYS A 456 CG CD CE NZ REMARK 470 LYS A 466 CG CD CE NZ REMARK 470 LYS A 468 CG CD CE NZ REMARK 470 ASP A 483 CG OD1 OD2 REMARK 470 HIS A 484 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 487 CG CD CE NZ REMARK 470 GLU A 500 CG CD OE1 OE2 REMARK 470 GLU B 36 CG CD OE1 OE2 REMARK 470 LYS B 39 CG CD CE NZ REMARK 470 GLU B 59 CG CD OE1 OE2 REMARK 470 LYS B 196 CG CD CE NZ REMARK 470 LYS B 230 CG CD CE NZ REMARK 470 LYS B 232 CG CD CE NZ REMARK 470 GLU B 254 CG CD OE1 OE2 REMARK 470 LYS B 338 CG CD CE NZ REMARK 470 LYS B 372 CG CD CE NZ REMARK 470 ARG B 425 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 450 CG CD OE1 OE2 REMARK 470 GLU B 455 CG CD OE1 OE2 REMARK 470 LYS B 456 CG CD CE NZ REMARK 470 LYS B 466 CG CD CE NZ REMARK 470 LYS B 468 CG CD CE NZ REMARK 470 ASP B 483 CG OD1 OD2 REMARK 470 LYS B 487 CG CD CE NZ REMARK 470 ASN B 501 CG OD1 ND2 REMARK 470 LYS C 86 CG CD CE NZ REMARK 470 GLU C 89 CG CD OE1 OE2 REMARK 470 LYS C 96 CB CG CD CE NZ REMARK 470 ASP C 97 CG OD1 OD2 REMARK 470 GLU C 99 CG CD OE1 OE2 REMARK 470 THR C 107 OG1 CG2 REMARK 470 GLU C 117 CG CD OE1 OE2 REMARK 470 LYS C 118 CG CD CE NZ REMARK 470 ILE C 119 CG1 CG2 CD1 REMARK 470 THR C 121 OG1 CG2 REMARK 470 LYS C 122 CG CD CE NZ REMARK 470 GLU C 123 CG CD OE1 OE2 REMARK 470 LYS C 124 CG CD CE NZ REMARK 470 GLN C 131 CG CD OE1 NE2 REMARK 470 VAL C 153 CG1 CG2 REMARK 470 LYS C 156 CG CD CE NZ REMARK 470 ASP C 158 CG OD1 OD2 REMARK 470 ASP C 159 CG OD1 OD2 REMARK 470 LYS C 163 CG CD CE NZ REMARK 470 ASP C 174 CG OD1 OD2 REMARK 470 ARG C 175 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 176 CE NZ REMARK 470 GLU C 184 CG CD OE1 OE2 REMARK 470 LYS C 196 CG CD CE NZ REMARK 470 GLU C 229 CG CD OE1 OE2 REMARK 470 LYS C 230 CG CD CE NZ REMARK 470 LYS C 232 CG CD CE NZ REMARK 470 LYS C 338 CG CD CE NZ REMARK 470 LYS C 372 CG CD CE NZ REMARK 470 GLU C 450 CG CD OE1 OE2 REMARK 470 ARG C 454 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 455 CG CD OE1 OE2 REMARK 470 LYS C 456 CG CD CE NZ REMARK 470 LYS C 466 CG CD CE NZ REMARK 470 LYS C 468 CG CD CE NZ REMARK 470 LYS C 487 CG CD CE NZ REMARK 470 ARG C 499 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 18 CG CD CE NZ REMARK 470 GLU D 36 CG CD OE1 OE2 REMARK 470 LYS D 39 CG CD CE NZ REMARK 470 GLU D 59 CG CD OE1 OE2 REMARK 470 LYS D 86 CG CD CE NZ REMARK 470 GLU D 89 CG CD OE1 OE2 REMARK 470 ARG D 91 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 122 CG CD CE NZ REMARK 470 GLU D 123 CG CD OE1 OE2 REMARK 470 LYS D 124 CG CD CE NZ REMARK 470 ASN D 134 CG OD1 ND2 REMARK 470 ASP D 159 CG OD1 OD2 REMARK 470 LYS D 163 CG CD CE NZ REMARK 470 ARG D 171 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 176 CG CD CE NZ REMARK 470 GLU D 184 CG CD OE1 OE2 REMARK 470 ASP D 186 CG OD1 OD2 REMARK 470 GLU D 192 CG CD OE1 OE2 REMARK 470 LYS D 193 CG CD CE NZ REMARK 470 LYS D 196 CG CD CE NZ REMARK 470 LYS D 230 CG CD CE NZ REMARK 470 ARG D 308 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 372 CG CD CE NZ REMARK 470 ARG D 405 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 450 CG CD OE1 OE2 REMARK 470 ASP D 453 CG OD1 OD2 REMARK 470 LYS D 456 CG CD CE NZ REMARK 470 LYS D 466 CG CD CE NZ REMARK 470 LYS D 468 CG CD CE NZ REMARK 470 HIS D 484 CG ND1 CD2 CE1 NE2 REMARK 470 LYS D 487 CG CD CE NZ REMARK 470 LEU E 4 CG CD1 CD2 REMARK 470 GLN E 5 CG CD OE1 NE2 REMARK 470 ILE E 8 CG1 CG2 CD1 REMARK 470 LYS E 18 CG CD CE NZ REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 GLU E 192 CG CD OE1 OE2 REMARK 470 LYS E 193 CG CD CE NZ REMARK 470 LYS E 196 CG CD CE NZ REMARK 470 LYS E 230 CG CD CE NZ REMARK 470 GLU E 254 CG CD OE1 OE2 REMARK 470 ARG E 308 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 338 CG CD CE NZ REMARK 470 LYS E 368 CG CD CE NZ REMARK 470 LYS E 372 CG CD CE NZ REMARK 470 GLU E 450 CG CD OE1 OE2 REMARK 470 ASN E 452 CG OD1 ND2 REMARK 470 GLU E 455 CG CD OE1 OE2 REMARK 470 LYS E 456 CG CD CE NZ REMARK 470 LYS E 466 CG CD CE NZ REMARK 470 LYS E 468 CG CD CE NZ REMARK 470 HIS E 484 CG ND1 CD2 CE1 NE2 REMARK 470 ARG E 499 CG CD NE CZ NH1 NH2 REMARK 470 LYS F 18 CG CD CE NZ REMARK 470 GLU F 36 CG CD OE1 OE2 REMARK 470 LYS F 39 CG CD CE NZ REMARK 470 GLU F 59 CG CD OE1 OE2 REMARK 470 GLU F 89 CG CD OE1 OE2 REMARK 470 GLU F 192 CG CD OE1 OE2 REMARK 470 LYS F 193 CG CD CE NZ REMARK 470 LYS F 196 CG CD CE NZ REMARK 470 ARG F 221 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 229 CG CD OE1 OE2 REMARK 470 LYS F 230 CG CD CE NZ REMARK 470 LYS F 232 CG CD CE NZ REMARK 470 GLU F 273 CG CD OE1 OE2 REMARK 470 ARG F 308 CG CD NE CZ NH1 NH2 REMARK 470 LYS F 338 CG CD CE NZ REMARK 470 LYS F 372 CG CD CE NZ REMARK 470 SER F 376 OG REMARK 470 GLU F 378 CG CD OE1 OE2 REMARK 470 GLU F 450 CG CD OE1 OE2 REMARK 470 ARG F 454 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 455 CG CD OE1 OE2 REMARK 470 LYS F 456 CG CD CE NZ REMARK 470 GLN F 459 CG CD OE1 NE2 REMARK 470 LYS F 466 CG CD CE NZ REMARK 470 LYS F 468 CG CD CE NZ REMARK 470 HIS F 481 CG ND1 CD2 CE1 NE2 REMARK 470 LYS F 487 CG CD CE NZ REMARK 470 ARG F 494 CG CD NE CZ NH1 NH2 REMARK 470 ARG F 497 CG CD NE CZ NH1 NH2 REMARK 470 ARG F 499 CG CD NE CZ NH1 NH2 REMARK 470 ASP G 115 CG OD1 OD2 REMARK 470 GLN G 122 CG CD OE1 NE2 REMARK 470 GLN H 122 CG CD OE1 NE2 REMARK 470 GLN I 5 CG CD OE1 NE2 REMARK 470 GLN I 13 CG CD OE1 NE2 REMARK 470 LYS I 49 CG CD CE NZ REMARK 470 ARG I 51 CG CD NE CZ NH1 NH2 REMARK 470 LYS I 71 CG CD CE NZ REMARK 470 GLU I 95 CG CD OE1 OE2 REMARK 470 GLN K 3 CG CD OE1 NE2 REMARK 470 ARG K 44 CG CD NE CZ NH1 NH2 REMARK 470 LYS K 49 CG CD CE NZ REMARK 470 LYS K 82 CG CD CE NZ REMARK 470 GLU K 95 CG CD OE1 OE2 REMARK 470 TYR K 100 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG K 118 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 3 CG CD OE1 NE2 REMARK 470 GLU L 6 CG CD OE1 OE2 REMARK 470 VAL L 12 CG1 CG2 REMARK 470 LEU L 18 CG CD1 CD2 REMARK 470 LYS L 19 CG CD CE NZ REMARK 470 ARG L 44 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 49 CG CD CE NZ REMARK 470 LYS L 71 CG CD CE NZ REMARK 470 LYS L 82 CG CD CE NZ REMARK 470 TYR L 100 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS L 112 CG CD CE NZ REMARK 470 ARG L 118 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 122 CG CD OE1 NE2 REMARK 470 GLN L 125 CG CD OE1 NE2 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 OE1 GLN H 1 ND2 ASN H 28 2.03 REMARK 500 O SER E 256 NZ LYS E 291 2.03 REMARK 500 OH TYR B 443 O GLY B 449 2.03 REMARK 500 OG1 THR A 92 O TYR A 126 2.06 REMARK 500 OE1 GLU B 379 OH TYR B 413 2.09 REMARK 500 NE2 GLN L 88 OD1 ASN L 90 2.10 REMARK 500 NH1 ARG G 33 OD1 ASP G 38 2.11 REMARK 500 O ILE C 253 NZ LYS C 291 2.11 REMARK 500 OD1 ASP A 218 NH1 ARG A 221 2.12 REMARK 500 OG SER A 302 O HOH A 701 2.12 REMARK 500 NH2 ARG I 33 O ASP I 106 2.12 REMARK 500 O SER L 58 NH1 ARG L 78 2.14 REMARK 500 O GLU D 254 O2 GOL D 603 2.15 REMARK 500 O SER A 331 OE1 GLU A 333 2.15 REMARK 500 OD1 ASN J 28 OG SER J 31 2.15 REMARK 500 O ASP D 451 NH2 ARG D 457 2.16 REMARK 500 O ILE D 253 NZ LYS D 291 2.17 REMARK 500 ND2 ASN B 242 OE1 GLN B 244 2.18 REMARK 500 OG SER F 411 O ARG F 436 2.18 REMARK 500 O GLY F 228 N GLY F 231 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 CYS A 351 CB CYS A 351 SG -0.102 REMARK 500 CYS C 281 CB CYS C 281 SG -0.106 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 SER A 44 CB - CA - C ANGL. DEV. = -11.6 DEGREES REMARK 500 MET A 46 CB - CA - C ANGL. DEV. = -12.5 DEGREES REMARK 500 ILE A 90 CB - CA - C ANGL. DEV. = 12.3 DEGREES REMARK 500 ILE A 90 N - CA - C ANGL. DEV. = -21.4 DEGREES REMARK 500 ILE A 270 CG1 - CB - CG2 ANGL. DEV. = -16.0 DEGREES REMARK 500 ALA A 296 CB - CA - C ANGL. DEV. = -12.3 DEGREES REMARK 500 ALA A 296 N - CA - C ANGL. DEV. = 28.6 DEGREES REMARK 500 MET A 299 CB - CA - C ANGL. DEV. = -12.7 DEGREES REMARK 500 SER A 331 CB - CA - C ANGL. DEV. = 17.3 DEGREES REMARK 500 SER A 331 N - CA - C ANGL. DEV. = -19.6 DEGREES REMARK 500 ALA A 447 CB - CA - C ANGL. DEV. = 14.0 DEGREES REMARK 500 GLY C 120 N - CA - C ANGL. DEV. = 33.0 DEGREES REMARK 500 MET C 280 CG - SD - CE ANGL. DEV. = -10.4 DEGREES REMARK 500 PRO C 374 CB - CA - C ANGL. DEV. = 15.5 DEGREES REMARK 500 PRO C 374 N - CA - C ANGL. DEV. = -16.2 DEGREES REMARK 500 LEU D 172 CA - CB - CG ANGL. DEV. = 18.6 DEGREES REMARK 500 ASP D 453 CB - CA - C ANGL. DEV. = 13.8 DEGREES REMARK 500 ASP D 453 N - CA - C ANGL. DEV. = -19.3 DEGREES REMARK 500 PRO E 88 N - CA - C ANGL. DEV. = -16.6 DEGREES REMARK 500 ALA F 17 N - CA - C ANGL. DEV. = 17.3 DEGREES REMARK 500 PRO F 88 N - CA - C ANGL. DEV. = -18.1 DEGREES REMARK 500 ASP F 360 CB - CA - C ANGL. DEV. = -12.2 DEGREES REMARK 500 ASP F 453 N - CA - C ANGL. DEV. = -17.1 DEGREES REMARK 500 LEU F 460 CB - CG - CD2 ANGL. DEV. = -12.9 DEGREES REMARK 500 GLU K 50 CB - CA - C ANGL. DEV. = -18.7 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 A 54 3.47 -69.34 REMARK 500 GLU A 89 106.02 -168.33 REMARK 500 ASP A 145 68.98 61.97 REMARK 500 VAL A 148 -60.54 -101.17 REMARK 500 ARG A 175 30.96 76.39 REMARK 500 SER A 191 170.89 -59.22 REMARK 500 ALA A 296 -74.76 -106.43 REMARK 500 TYR A 339 44.84 -155.01 REMARK 500 ALA A 396 143.43 -172.02 REMARK 500 SER A 437 -17.21 78.49 REMARK 500 HIS A 448 -157.55 -122.63 REMARK 500 ALA A 473 119.75 -37.09 REMARK 500 HIS A 481 -161.37 -126.82 REMARK 500 TYR A 489 159.07 69.16 REMARK 500 THR B 32 12.64 -142.54 REMARK 500 GLU B 241 18.55 -140.93 REMARK 500 ALA B 296 -61.07 -120.32 REMARK 500 MET B 299 -68.83 -93.69 REMARK 500 MET B 303 0.18 -68.67 REMARK 500 SER B 331 -93.53 -122.03 REMARK 500 SER B 437 -7.59 81.96 REMARK 500 ASN B 491 -4.11 -146.32 REMARK 500 THR C 92 32.73 -93.52 REMARK 500 ASP C 97 15.40 52.26 REMARK 500 ASP C 145 -117.38 59.62 REMARK 500 GLU C 157 -124.68 56.66 REMARK 500 ASN C 167 58.88 -109.97 REMARK 500 HIS C 170 141.99 -170.99 REMARK 500 GLU C 241 27.31 -145.53 REMARK 500 ALA C 296 -53.54 -121.57 REMARK 500 SER C 331 -85.41 -114.94 REMARK 500 ILE C 373 77.75 -117.11 REMARK 500 ASN C 433 -19.69 -49.38 REMARK 500 SER C 437 -15.54 77.46 REMARK 500 HIS C 448 -156.94 -117.36 REMARK 500 ASP C 451 50.31 37.11 REMARK 500 ARG C 454 15.94 53.72 REMARK 500 TYR C 489 139.15 -175.80 REMARK 500 PRO D 114 -7.33 -58.74 REMARK 500 ASP D 145 -113.76 55.48 REMARK 500 CYS D 160 38.89 -149.65 REMARK 500 GLU D 241 30.10 -150.26 REMARK 500 SER D 331 -83.88 -111.95 REMARK 500 PRO D 415 -177.09 -62.02 REMARK 500 SER D 437 -14.94 78.64 REMARK 500 HIS D 448 -152.09 -111.65 REMARK 500 ARG D 454 44.91 -86.15 REMARK 500 LYS D 468 2.43 -66.77 REMARK 500 THR E 32 14.69 -140.21 REMARK 500 PHE E 210 79.39 -103.06 REMARK 500 REMARK 500 THIS ENTRY HAS 86 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASN C 168 HIS C 169 139.98 REMARK 500 ILE C 373 PRO C 374 90.13 REMARK 500 ASP F 233 THR F 234 139.46 REMARK 500 ILE F 373 PRO F 374 93.17 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 D 717 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH J 308 DISTANCE = 6.30 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 GLU C 601 REMARK 610 GLU D 601 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8RTF RELATED DB: PDB DBREF 8RVR A 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RVR B 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RVR C 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RVR D 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RVR E 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RVR F 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RVR G 1 149 PDB 8RVR 8RVR 1 149 DBREF 8RVR H 1 149 PDB 8RVR 8RVR 1 149 DBREF 8RVR I 1 149 PDB 8RVR 8RVR 1 149 DBREF 8RVR J 1 149 PDB 8RVR 8RVR 1 149 DBREF 8RVR K 1 149 PDB 8RVR 8RVR 1 149 DBREF 8RVR L 1 149 PDB 8RVR 8RVR 1 149 SEQADV 8RVR GLU A 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR ASN A 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR LEU A 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR TYR A 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR PHE A 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLN A 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR SER A 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY A 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY A 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS A 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS A 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS A 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS A 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS A 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS A 514 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLU B 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR ASN B 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR LEU B 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR TYR B 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR PHE B 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLN B 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR SER B 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY B 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY B 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS B 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS B 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS B 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS B 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS B 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS B 514 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLU C 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR ASN C 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR LEU C 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR TYR C 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR PHE C 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLN C 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR SER C 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY C 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY C 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS C 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS C 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS C 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS C 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS C 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS C 514 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLU D 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR ASN D 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR LEU D 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR TYR D 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR PHE D 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLN D 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR SER D 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY D 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY D 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS D 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS D 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS D 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS D 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS D 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS D 514 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLU E 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR ASN E 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR LEU E 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR TYR E 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR PHE E 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLN E 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR SER E 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY E 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY E 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS E 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS E 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS E 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS E 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS E 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS E 514 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLU F 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR ASN F 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR LEU F 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR TYR F 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR PHE F 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLN F 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR SER F 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY F 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR GLY F 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS F 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS F 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS F 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS F 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS F 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RVR HIS F 514 UNP G0UYF4 EXPRESSION TAG SEQRES 1 A 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 A 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 A 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 A 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 A 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 A 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 A 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 A 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 A 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 A 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 A 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 A 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 A 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 A 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 A 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 A 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 A 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 A 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 A 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 A 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 A 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 A 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 A 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 A 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 A 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 A 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 A 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 A 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 A 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 A 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 A 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 A 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 A 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 A 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 A 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 A 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 A 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 A 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 A 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 A 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 B 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 B 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 B 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 B 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 B 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 B 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 B 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 B 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 B 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 B 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 B 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 B 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 B 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 B 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 B 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 B 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 B 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 B 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 B 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 B 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 B 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 B 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 B 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 B 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 B 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 B 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 B 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 B 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 B 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 B 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 B 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 B 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 B 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 B 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 B 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 B 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 B 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 B 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 B 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 B 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 C 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 C 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 C 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 C 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 C 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 C 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 C 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 C 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 C 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 C 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 C 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 C 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 C 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 C 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 C 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 C 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 C 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 C 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 C 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 C 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 C 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 C 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 C 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 C 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 C 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 C 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 C 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 C 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 C 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 C 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 C 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 C 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 C 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 C 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 C 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 C 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 C 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 C 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 C 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 C 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 D 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 D 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 D 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 D 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 D 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 D 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 D 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 D 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 D 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 D 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 D 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 D 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 D 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 D 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 D 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 D 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 D 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 D 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 D 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 D 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 D 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 D 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 D 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 D 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 D 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 D 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 D 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 D 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 D 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 D 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 D 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 D 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 D 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 D 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 D 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 D 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 D 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 D 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 D 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 D 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 E 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 E 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 E 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 E 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 E 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 E 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 E 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 E 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 E 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 E 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 E 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 E 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 E 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 E 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 E 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 E 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 E 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 E 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 E 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 E 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 E 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 E 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 E 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 E 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 E 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 E 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 E 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 E 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 E 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 E 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 E 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 E 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 E 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 E 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 E 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 E 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 E 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 E 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 E 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 E 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 F 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 F 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 F 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 F 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 F 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 F 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 F 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 F 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 F 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 F 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 F 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 F 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 F 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 F 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 F 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 F 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 F 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 F 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 F 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 F 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 F 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 F 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 F 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 F 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 F 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 F 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 F 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 F 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 F 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 F 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 F 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 F 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 F 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 F 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 F 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 F 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 F 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 F 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 F 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 F 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 G 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 G 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 G 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 G 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 G 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 G 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 G 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 G 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 G 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 G 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 G 149 HIS HIS HIS HIS HIS HIS SEQRES 1 H 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 H 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 H 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 H 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 H 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 H 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 H 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 H 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 H 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 H 149 HIS HIS HIS HIS HIS HIS SEQRES 1 I 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 I 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 I 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 I 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 I 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 I 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 I 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 I 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 I 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 I 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 I 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 I 149 HIS HIS HIS HIS HIS HIS SEQRES 1 J 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 J 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 J 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 J 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 J 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 J 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 J 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 J 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 J 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 J 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 J 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 J 149 HIS HIS HIS HIS HIS HIS SEQRES 1 K 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 K 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 K 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 K 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 K 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 K 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 K 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 K 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 K 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 K 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 K 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 K 149 HIS HIS HIS HIS HIS HIS SEQRES 1 L 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 L 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 L 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 L 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 L 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 L 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 L 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 L 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 L 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 L 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 L 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 L 149 HIS HIS HIS HIS HIS HIS HET SO4 A 601 5 HET SO4 B 601 5 HET GOL B 602 6 HET GOL B 603 6 HET GOL B 604 6 HET GLU C 601 5 HET GOL C 602 6 HET GOL C 603 6 HET GOL C 604 6 HET SO4 C 605 5 HET GLU D 601 5 HET GOL D 602 6 HET GOL D 603 6 HET SO4 D 604 5 HET GOL E 601 6 HET SO4 E 602 5 HET SO4 F 601 5 HET GOL G 201 6 HET GOL H 201 6 HET GOL I 201 6 HET GOL J 201 6 HETNAM SO4 SULFATE ION HETNAM GOL GLYCEROL HETNAM GLU GLUTAMIC ACID HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 13 SO4 6(O4 S 2-) FORMUL 15 GOL 13(C3 H8 O3) FORMUL 18 GLU 2(C5 H9 N O4) FORMUL 34 HOH *123(H2 O) HELIX 1 AA1 SER A 2 GLY A 9 1 8 HELIX 2 AA2 SER A 34 GLY A 45 1 12 HELIX 3 AA3 SER A 57 GLY A 76 1 20 HELIX 4 AA4 PHE A 95 ASP A 97 5 3 HELIX 5 AA5 ASP A 113 GLU A 117 5 5 HELIX 6 AA6 SER A 191 GLY A 205 1 15 HELIX 7 AA7 THR A 216 GLY A 228 1 13 HELIX 8 AA8 ASN A 242 ASN A 248 1 7 HELIX 9 AA9 ASN A 248 SER A 256 1 9 HELIX 10 AB1 ALA A 262 ILE A 270 1 9 HELIX 11 AB2 PRO A 271 ALA A 289 1 19 HELIX 12 AB3 LEU A 300 THR A 304 5 5 HELIX 13 AB4 THR A 310 ASN A 323 1 14 HELIX 14 AB5 TYR A 339 THR A 358 1 20 HELIX 15 AB6 SER A 361 LEU A 370 1 10 HELIX 16 AB7 SER A 376 VAL A 392 1 17 HELIX 17 AB8 GLY A 404 TYR A 413 1 10 HELIX 18 AB9 ARG A 425 LEU A 432 1 8 HELIX 19 AC1 ASN A 433 THR A 435 5 3 HELIX 20 AC2 ARG A 454 LYS A 468 1 15 HELIX 21 AC3 GLN B 3 GLY B 9 1 7 HELIX 22 AC4 SER B 34 GLY B 45 1 12 HELIX 23 AC5 SER B 57 GLY B 76 1 20 HELIX 24 AC6 SER B 191 GLN B 204 1 14 HELIX 25 AC7 THR B 216 GLY B 228 1 13 HELIX 26 AC8 GLU B 229 LYS B 232 5 4 HELIX 27 AC9 ASN B 242 ASN B 248 1 7 HELIX 28 AD1 ASN B 248 SER B 256 1 9 HELIX 29 AD2 ALA B 262 ILE B 270 1 9 HELIX 30 AD3 PRO B 271 GLY B 290 1 20 HELIX 31 AD4 LEU B 300 THR B 305 5 6 HELIX 32 AD5 THR B 310 GLY B 324 1 15 HELIX 33 AD6 SER B 331 LYS B 336 1 6 HELIX 34 AD7 TYR B 339 THR B 358 1 20 HELIX 35 AD8 SER B 361 ASN B 369 1 9 HELIX 36 AD9 SER B 376 GLN B 393 1 18 HELIX 37 AE1 GLY B 404 TYR B 413 1 10 HELIX 38 AE2 ARG B 425 LEU B 432 1 8 HELIX 39 AE3 ASN B 433 THR B 435 5 3 HELIX 40 AE4 ARG B 454 LYS B 468 1 15 HELIX 41 AE5 GLN C 3 ILE C 8 1 6 HELIX 42 AE6 SER C 34 SER C 44 1 11 HELIX 43 AE7 SER C 57 GLY C 76 1 20 HELIX 44 AE8 GLN C 131 VAL C 136 1 6 HELIX 45 AE9 SER C 191 GLY C 205 1 15 HELIX 46 AF1 THR C 216 LEU C 227 1 12 HELIX 47 AF2 GLY C 228 LYS C 232 5 5 HELIX 48 AF3 ASN C 242 ASN C 248 1 7 HELIX 49 AF4 ASN C 248 SER C 256 1 9 HELIX 50 AF5 ALA C 262 VAL C 268 1 7 HELIX 51 AF6 PRO C 271 ALA C 289 1 19 HELIX 52 AF7 LEU C 300 THR C 305 5 6 HELIX 53 AF8 THR C 310 ASN C 323 1 14 HELIX 54 AF9 SER C 331 LYS C 336 1 6 HELIX 55 AG1 TYR C 339 THR C 358 1 20 HELIX 56 AG2 SER C 361 ASN C 369 1 9 HELIX 57 AG3 SER C 376 VAL C 392 1 17 HELIX 58 AG4 GLY C 404 TYR C 413 1 10 HELIX 59 AG5 ARG C 425 LEU C 432 1 8 HELIX 60 AG6 ASN C 433 THR C 435 5 3 HELIX 61 AG7 ARG C 454 LYS C 468 1 15 HELIX 62 AG8 GLN D 3 GLY D 9 1 7 HELIX 63 AG9 SER D 34 GLY D 45 1 12 HELIX 64 AH1 SER D 57 GLY D 76 1 20 HELIX 65 AH2 PHE D 95 GLU D 99 5 5 HELIX 66 AH3 ASP D 113 LYS D 118 5 6 HELIX 67 AH4 GLN D 131 VAL D 136 1 6 HELIX 68 AH5 SER D 191 GLY D 205 1 15 HELIX 69 AH6 THR D 216 LEU D 227 1 12 HELIX 70 AH7 GLY D 228 LYS D 232 5 5 HELIX 71 AH8 ASN D 242 ASN D 248 1 7 HELIX 72 AH9 ASN D 248 SER D 256 1 9 HELIX 73 AI1 ALA D 262 ILE D 270 1 9 HELIX 74 AI2 PRO D 271 GLY D 290 1 20 HELIX 75 AI3 LEU D 300 THR D 305 5 6 HELIX 76 AI4 THR D 310 ASN D 323 1 14 HELIX 77 AI5 SER D 331 LYS D 336 1 6 HELIX 78 AI6 TYR D 339 THR D 358 1 20 HELIX 79 AI7 SER D 361 ASN D 369 1 9 HELIX 80 AI8 SER D 376 GLN D 393 1 18 HELIX 81 AI9 GLY D 404 TYR D 413 1 10 HELIX 82 AJ1 ARG D 425 LEU D 432 1 8 HELIX 83 AJ2 ASN D 433 THR D 435 5 3 HELIX 84 AJ3 ARG D 454 LYS D 468 1 15 HELIX 85 AJ4 GLN E 3 ILE E 8 1 6 HELIX 86 AJ5 SER E 34 SER E 44 1 11 HELIX 87 AJ6 SER E 57 GLY E 76 1 20 HELIX 88 AJ7 SER E 191 GLY E 205 1 15 HELIX 89 AJ8 THR E 216 LEU E 227 1 12 HELIX 90 AJ9 GLY E 228 LYS E 232 5 5 HELIX 91 AK1 ASN E 242 ASN E 248 1 7 HELIX 92 AK2 ASN E 248 SER E 256 1 9 HELIX 93 AK3 ALA E 262 VAL E 268 1 7 HELIX 94 AK4 PRO E 271 GLY E 290 1 20 HELIX 95 AK5 LEU E 300 THR E 305 5 6 HELIX 96 AK6 THR E 310 ASN E 323 1 14 HELIX 97 AK7 SER E 331 LYS E 336 1 6 HELIX 98 AK8 TYR E 339 THR E 358 1 20 HELIX 99 AK9 SER E 361 LEU E 370 1 10 HELIX 100 AL1 SER E 376 VAL E 392 1 17 HELIX 101 AL2 GLY E 404 TYR E 413 1 10 HELIX 102 AL3 ARG E 425 LEU E 432 1 8 HELIX 103 AL4 ASN E 433 THR E 435 5 3 HELIX 104 AL5 ARG E 454 LYS E 468 1 15 HELIX 105 AL6 GLN F 3 ILE F 8 1 6 HELIX 106 AL7 GLY F 29 GLN F 33 5 5 HELIX 107 AL8 SER F 34 SER F 44 1 11 HELIX 108 AL9 SER F 57 GLY F 76 1 20 HELIX 109 AM1 SER F 191 GLY F 205 1 15 HELIX 110 AM2 THR F 216 LEU F 227 1 12 HELIX 111 AM3 GLY F 228 LYS F 232 5 5 HELIX 112 AM4 ASN F 242 ASN F 248 1 7 HELIX 113 AM5 ASN F 248 SER F 256 1 9 HELIX 114 AM6 ALA F 262 VAL F 268 1 7 HELIX 115 AM7 PRO F 271 GLY F 290 1 20 HELIX 116 AM8 LEU F 300 THR F 305 5 6 HELIX 117 AM9 THR F 310 ASN F 323 1 14 HELIX 118 AN1 SER F 331 LYS F 336 1 6 HELIX 119 AN2 TYR F 339 THR F 358 1 20 HELIX 120 AN3 SER F 361 LEU F 370 1 10 HELIX 121 AN4 GLU F 378 VAL F 392 1 15 HELIX 122 AN5 GLY F 404 TYR F 413 1 10 HELIX 123 AN6 ARG F 425 LEU F 432 1 8 HELIX 124 AN7 ASN F 433 THR F 435 5 3 HELIX 125 AN8 GLU F 455 LYS F 468 1 14 HELIX 126 AN9 THR G 34 ASP G 38 5 5 HELIX 127 AO1 ASP G 68 LYS G 71 5 4 HELIX 128 AO2 GLN G 93 THR G 97 5 5 HELIX 129 AO3 VAL G 113 TYR G 117 5 5 HELIX 130 AO4 THR H 34 ASP H 38 5 5 HELIX 131 AO5 GLN H 93 THR H 97 5 5 HELIX 132 AO6 VAL H 113 TYR H 117 5 5 HELIX 133 AO7 THR I 34 ASP I 38 5 5 HELIX 134 AO8 GLN I 93 THR I 97 5 5 HELIX 135 AO9 VAL I 113 TYR I 117 5 5 HELIX 136 AP1 SER J 36 ASP J 38 5 3 HELIX 137 AP2 ASP J 68 LYS J 71 5 4 HELIX 138 AP3 GLN J 93 THR J 97 5 5 HELIX 139 AP4 VAL J 113 TYR J 117 5 5 HELIX 140 AP5 ASP K 68 LYS K 71 5 4 HELIX 141 AP6 GLN K 93 THR K 97 5 5 HELIX 142 AP7 VAL K 113 TYR K 117 5 5 HELIX 143 AP8 ASP L 68 LYS L 71 5 4 HELIX 144 AP9 ASN L 80 LYS L 82 5 3 HELIX 145 AQ1 GLN L 93 THR L 97 5 5 HELIX 146 AQ2 VAL L 113 TYR L 117 5 5 SHEET 1 AA1 9 ARG A 23 THR A 27 0 SHEET 2 AA1 9 MET A 46 ASN A 52 1 O ARG A 50 N CYS A 26 SHEET 3 AA1 9 GLY A 80 ASP A 84 1 O ALA A 82 N MET A 51 SHEET 4 AA1 9 MET A 208 ALA A 211 1 O MET A 208 N LEU A 83 SHEET 5 AA1 9 LEU A 235 ILE A 240 1 O ILE A 237 N ILE A 209 SHEET 6 AA1 9 GLY A 258 VAL A 261 1 O MET A 260 N ILE A 240 SHEET 7 AA1 9 VAL A 293 CYS A 295 1 O ILE A 294 N VAL A 261 SHEET 8 AA1 9 CYS A 327 MET A 329 1 O CYS A 327 N CYS A 295 SHEET 9 AA1 9 ARG A 23 THR A 27 1 N ILE A 25 O VAL A 328 SHEET 1 AA2 2 ARG A 91 THR A 92 0 SHEET 2 AA2 2 LYS A 176 GLY A 177 -1 O LYS A 176 N THR A 92 SHEET 1 AA3 2 GLU A 99 TYR A 102 0 SHEET 2 AA3 2 HIS A 170 THR A 173 -1 O LEU A 172 N ALA A 100 SHEET 1 AA4 5 LYS A 124 TYR A 126 0 SHEET 2 AA4 5 THR A 107 THR A 111 1 N THR A 111 O PHE A 125 SHEET 3 AA4 5 THR A 161 VAL A 166 -1 O CYS A 164 N VAL A 108 SHEET 4 AA4 5 LEU A 149 SER A 155 -1 N ARG A 152 O HIS A 165 SHEET 5 AA4 5 LEU A 141 VAL A 144 -1 N VAL A 144 O LEU A 149 SHEET 1 AA510 VAL A 438 TYR A 442 0 SHEET 2 AA510 ILE A 419 THR A 423 1 N CYS A 421 O VAL A 441 SHEET 3 AA510 ILE A 397 VAL A 399 1 N ILE A 397 O ILE A 420 SHEET 4 AA510 VAL A 476 HIS A 481 1 O VAL A 478 N LEU A 398 SHEET 5 AA510 GLN A 492 ARG A 497 -1 O ARG A 494 N ILE A 479 SHEET 6 AA510 GLN C 492 ARG C 497 -1 O THR C 493 N THR A 493 SHEET 7 AA510 VAL C 476 HIS C 481 -1 N MET C 477 O VAL C 496 SHEET 8 AA510 ALA C 396 LEU C 400 1 N LEU C 398 O VAL C 478 SHEET 9 AA510 ILE C 419 THR C 423 1 O ILE C 420 N ILE C 397 SHEET 10 AA510 VAL C 438 TYR C 442 1 O VAL C 441 N THR C 423 SHEET 1 AA6 9 ARG B 23 THR B 27 0 SHEET 2 AA6 9 MET B 46 ASN B 52 1 O ARG B 50 N CYS B 26 SHEET 3 AA6 9 GLY B 80 ASP B 84 1 O ASP B 84 N MET B 51 SHEET 4 AA6 9 MET B 208 ALA B 211 1 O PHE B 210 N LEU B 83 SHEET 5 AA6 9 LEU B 235 ILE B 240 1 O LEU B 235 N ILE B 209 SHEET 6 AA6 9 GLY B 258 VAL B 261 1 O GLY B 258 N SER B 238 SHEET 7 AA6 9 VAL B 293 CYS B 295 1 O ILE B 294 N VAL B 261 SHEET 8 AA6 9 CYS B 327 LEU B 330 1 O CYS B 327 N CYS B 295 SHEET 9 AA6 9 ARG B 23 THR B 27 1 N ILE B 25 O LEU B 330 SHEET 1 AA710 VAL B 438 TYR B 442 0 SHEET 2 AA710 ILE B 419 THR B 423 1 N CYS B 421 O VAL B 441 SHEET 3 AA710 ILE B 397 VAL B 399 1 N VAL B 399 O ALA B 422 SHEET 4 AA710 VAL B 476 HIS B 481 1 O VAL B 478 N LEU B 398 SHEET 5 AA710 GLN B 492 ARG B 497 -1 O ARG B 494 N ILE B 479 SHEET 6 AA710 GLN D 492 ARG D 497 -1 O THR D 493 N THR B 493 SHEET 7 AA710 VAL D 476 HIS D 481 -1 N MET D 477 O VAL D 496 SHEET 8 AA710 ALA D 396 LEU D 400 1 N LEU D 398 O VAL D 478 SHEET 9 AA710 ILE D 419 THR D 423 1 O ILE D 420 N ILE D 397 SHEET 10 AA710 VAL D 438 TYR D 442 1 O VAL D 441 N CYS D 421 SHEET 1 AA8 9 ARG C 23 THR C 27 0 SHEET 2 AA8 9 MET C 46 ASN C 52 1 O ARG C 50 N CYS C 26 SHEET 3 AA8 9 GLY C 80 ASP C 84 1 O ALA C 82 N ALA C 49 SHEET 4 AA8 9 MET C 208 ALA C 211 1 O MET C 208 N LEU C 83 SHEET 5 AA8 9 LEU C 235 ILE C 240 1 O LYS C 239 N ALA C 211 SHEET 6 AA8 9 GLY C 258 VAL C 261 1 O MET C 260 N ILE C 240 SHEET 7 AA8 9 VAL C 293 CYS C 295 1 O ILE C 294 N VAL C 261 SHEET 8 AA8 9 CYS C 327 LEU C 330 1 O MET C 329 N CYS C 295 SHEET 9 AA8 9 ARG C 23 THR C 27 1 N ILE C 25 O LEU C 330 SHEET 1 AA9 2 ILE C 90 ARG C 91 0 SHEET 2 AA9 2 GLY C 177 ILE C 178 -1 O ILE C 178 N ILE C 90 SHEET 1 AB1 2 ALA C 100 TYR C 102 0 SHEET 2 AB1 2 HIS C 170 LEU C 172 -1 O LEU C 172 N ALA C 100 SHEET 1 AB2 5 LYS C 124 TYR C 126 0 SHEET 2 AB2 5 THR C 107 THR C 111 1 N THR C 111 O PHE C 125 SHEET 3 AB2 5 THR C 161 VAL C 166 -1 O LEU C 162 N VAL C 110 SHEET 4 AB2 5 LEU C 149 SER C 155 -1 N SER C 155 O LYS C 163 SHEET 5 AB2 5 LEU C 141 VAL C 144 -1 N VAL C 144 O LEU C 149 SHEET 1 AB3 9 ARG D 23 THR D 27 0 SHEET 2 AB3 9 VAL D 48 ASN D 52 1 O VAL D 48 N CYS D 26 SHEET 3 AB3 9 GLY D 80 ASP D 84 1 O GLY D 80 N ALA D 49 SHEET 4 AB3 9 MET D 208 ALA D 211 1 O MET D 208 N LEU D 83 SHEET 5 AB3 9 LEU D 235 ILE D 240 1 O ILE D 237 N ILE D 209 SHEET 6 AB3 9 GLY D 258 VAL D 261 1 O MET D 260 N ILE D 240 SHEET 7 AB3 9 VAL D 293 CYS D 295 1 O ILE D 294 N VAL D 261 SHEET 8 AB3 9 CYS D 327 LEU D 330 1 O MET D 329 N CYS D 295 SHEET 9 AB3 9 ARG D 23 THR D 27 1 N ILE D 25 O VAL D 328 SHEET 1 AB4 2 ALA D 100 TYR D 102 0 SHEET 2 AB4 2 HIS D 170 LEU D 172 -1 O HIS D 170 N TYR D 102 SHEET 1 AB5 6 LYS D 124 TYR D 126 0 SHEET 2 AB5 6 THR D 107 THR D 111 1 N THR D 111 O PHE D 125 SHEET 3 AB5 6 THR D 161 VAL D 166 -1 O CYS D 164 N VAL D 108 SHEET 4 AB5 6 LEU D 149 SER D 155 -1 N LEU D 154 O LYS D 163 SHEET 5 AB5 6 LEU D 141 VAL D 144 -1 N VAL D 144 O LEU D 149 SHEET 6 AB5 6 ILE D 178 ASN D 179 -1 O ASN D 179 N TYR D 143 SHEET 1 AB6 9 ARG E 23 THR E 27 0 SHEET 2 AB6 9 MET E 46 ASN E 52 1 O VAL E 48 N CYS E 26 SHEET 3 AB6 9 GLY E 80 ASP E 84 1 O ASP E 84 N MET E 51 SHEET 4 AB6 9 MET E 208 ALA E 211 1 O PHE E 210 N LEU E 83 SHEET 5 AB6 9 LEU E 235 ILE E 240 1 O LEU E 235 N ILE E 209 SHEET 6 AB6 9 GLY E 258 VAL E 261 1 O MET E 260 N SER E 238 SHEET 7 AB6 9 VAL E 293 CYS E 295 1 O ILE E 294 N ILE E 259 SHEET 8 AB6 9 CYS E 327 LEU E 330 1 O CYS E 327 N CYS E 295 SHEET 9 AB6 9 ARG E 23 THR E 27 1 N ILE E 25 O LEU E 330 SHEET 1 AB7 5 VAL E 438 TYR E 442 0 SHEET 2 AB7 5 ILE E 419 THR E 423 1 N CYS E 421 O VAL E 441 SHEET 3 AB7 5 ILE E 397 VAL E 399 1 N VAL E 399 O ILE E 420 SHEET 4 AB7 5 VAL E 476 ALA E 482 1 O VAL E 478 N LEU E 398 SHEET 5 AB7 5 PRO E 490 ARG E 497 -1 O ARG E 494 N ILE E 479 SHEET 1 AB8 9 ARG F 23 THR F 27 0 SHEET 2 AB8 9 MET F 46 ASN F 52 1 O SER F 47 N ILE F 24 SHEET 3 AB8 9 GLY F 80 ASP F 84 1 O ALA F 82 N ALA F 49 SHEET 4 AB8 9 MET F 208 ALA F 211 1 O MET F 208 N LEU F 83 SHEET 5 AB8 9 LEU F 235 ILE F 240 1 O LYS F 239 N ALA F 211 SHEET 6 AB8 9 GLY F 258 VAL F 261 1 O MET F 260 N SER F 238 SHEET 7 AB8 9 VAL F 293 CYS F 295 1 O ILE F 294 N VAL F 261 SHEET 8 AB8 9 CYS F 327 MET F 329 1 O CYS F 327 N CYS F 295 SHEET 9 AB8 9 ARG F 23 THR F 27 1 N ILE F 25 O VAL F 328 SHEET 1 AB9 5 VAL F 438 TYR F 442 0 SHEET 2 AB9 5 ILE F 419 THR F 423 1 N THR F 423 O VAL F 441 SHEET 3 AB9 5 ILE F 397 VAL F 399 1 N VAL F 399 O ILE F 420 SHEET 4 AB9 5 VAL F 476 VAL F 480 1 O VAL F 478 N LEU F 398 SHEET 5 AB9 5 ARG F 494 ARG F 497 -1 O ARG F 494 N ILE F 479 SHEET 1 AC1 4 VAL G 2 SER G 7 0 SHEET 2 AC1 4 LEU G 18 GLY G 26 -1 O SER G 25 N GLN G 3 SHEET 3 AC1 4 THR G 84 MET G 89 -1 O LEU G 87 N LEU G 20 SHEET 4 AC1 4 PHE G 74 ASP G 79 -1 N SER G 77 O TYR G 86 SHEET 1 AC2 6 GLY G 10 GLN G 13 0 SHEET 2 AC2 6 THR G 124 SER G 129 1 O THR G 127 N GLY G 10 SHEET 3 AC2 6 ALA G 98 GLY G 104 -1 N TYR G 100 O THR G 124 SHEET 4 AC2 6 ILE G 40 GLN G 45 -1 N PHE G 43 O TYR G 101 SHEET 5 AC2 6 ARG G 51 ILE G 57 -1 O GLY G 55 N TRP G 42 SHEET 6 AC2 6 THR G 64 TYR G 66 -1 O ASP G 65 N GLY G 56 SHEET 1 AC3 4 GLY G 10 GLN G 13 0 SHEET 2 AC3 4 THR G 124 SER G 129 1 O THR G 127 N GLY G 10 SHEET 3 AC3 4 ALA G 98 GLY G 104 -1 N TYR G 100 O THR G 124 SHEET 4 AC3 4 TYR G 119 TRP G 120 -1 O TYR G 119 N GLY G 104 SHEET 1 AC4 4 GLN H 3 SER H 7 0 SHEET 2 AC4 4 SER H 17 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AC4 4 THR H 84 ASN H 90 -1 O MET H 89 N LEU H 18 SHEET 4 AC4 4 PHE H 74 ASP H 79 -1 N SER H 77 O TYR H 86 SHEET 1 AC5 6 GLY H 10 GLN H 13 0 SHEET 2 AC5 6 THR H 124 SER H 129 1 O THR H 127 N GLY H 10 SHEET 3 AC5 6 ALA H 98 GLY H 104 -1 N TYR H 100 O THR H 124 SHEET 4 AC5 6 ILE H 40 GLN H 45 -1 N PHE H 43 O TYR H 101 SHEET 5 AC5 6 ARG H 51 ILE H 57 -1 O GLY H 55 N TRP H 42 SHEET 6 AC5 6 THR H 64 TYR H 66 -1 O ASP H 65 N GLY H 56 SHEET 1 AC6 4 GLY H 10 GLN H 13 0 SHEET 2 AC6 4 THR H 124 SER H 129 1 O THR H 127 N GLY H 10 SHEET 3 AC6 4 ALA H 98 GLY H 104 -1 N TYR H 100 O THR H 124 SHEET 4 AC6 4 TYR H 119 TRP H 120 -1 O TYR H 119 N GLY H 104 SHEET 1 AC7 4 LEU I 4 SER I 7 0 SHEET 2 AC7 4 SER I 17 ALA I 24 -1 O ALA I 23 N GLN I 5 SHEET 3 AC7 4 THR I 84 ASN I 90 -1 O VAL I 85 N CYS I 22 SHEET 4 AC7 4 PHE I 74 ASP I 79 -1 N ASP I 79 O THR I 84 SHEET 1 AC8 6 LEU I 11 GLN I 13 0 SHEET 2 AC8 6 THR I 124 SER I 129 1 O SER I 129 N VAL I 12 SHEET 3 AC8 6 ALA I 98 GLY I 104 -1 N TYR I 100 O THR I 124 SHEET 4 AC8 6 ILE I 40 GLN I 45 -1 N PHE I 43 O TYR I 101 SHEET 5 AC8 6 GLU I 52 ILE I 57 -1 O GLY I 55 N TRP I 42 SHEET 6 AC8 6 THR I 64 TYR I 66 -1 O ASP I 65 N GLY I 56 SHEET 1 AC9 4 LEU I 11 GLN I 13 0 SHEET 2 AC9 4 THR I 124 SER I 129 1 O SER I 129 N VAL I 12 SHEET 3 AC9 4 ALA I 98 GLY I 104 -1 N TYR I 100 O THR I 124 SHEET 4 AC9 4 TYR I 119 TRP I 120 -1 O TYR I 119 N GLY I 104 SHEET 1 AD1 4 GLN J 3 SER J 7 0 SHEET 2 AD1 4 LEU J 18 SER J 25 -1 O SER J 21 N SER J 7 SHEET 3 AD1 4 THR J 84 MET J 89 -1 O MET J 89 N LEU J 18 SHEET 4 AD1 4 PHE J 74 ASP J 79 -1 N THR J 75 O GLN J 88 SHEET 1 AD2 6 LEU J 11 GLN J 13 0 SHEET 2 AD2 6 THR J 124 SER J 129 1 O SER J 129 N VAL J 12 SHEET 3 AD2 6 ALA J 98 ARG J 105 -1 N ALA J 98 O VAL J 126 SHEET 4 AD2 6 ALA J 39 GLN J 45 -1 N PHE J 43 O TYR J 101 SHEET 5 AD2 6 ARG J 51 ILE J 57 -1 O GLY J 55 N TRP J 42 SHEET 6 AD2 6 THR J 64 TYR J 66 -1 O ASP J 65 N GLY J 56 SHEET 1 AD3 4 LEU J 11 GLN J 13 0 SHEET 2 AD3 4 THR J 124 SER J 129 1 O SER J 129 N VAL J 12 SHEET 3 AD3 4 ALA J 98 ARG J 105 -1 N ALA J 98 O VAL J 126 SHEET 4 AD3 4 TYR J 119 TRP J 120 -1 O TYR J 119 N GLY J 104 SHEET 1 AD4 2 SER J 27 ASN J 28 0 SHEET 2 AD4 2 ARG J 33 THR J 34 -1 O ARG J 33 N ASN J 28 SHEET 1 AD5 4 VAL K 2 SER K 7 0 SHEET 2 AD5 4 SER K 17 GLY K 26 -1 O SER K 21 N SER K 7 SHEET 3 AD5 4 THR K 84 ASN K 90 -1 O LEU K 87 N LEU K 20 SHEET 4 AD5 4 PHE K 74 ASP K 79 -1 N THR K 75 O GLN K 88 SHEET 1 AD6 6 LEU K 11 GLN K 13 0 SHEET 2 AD6 6 THR K 124 SER K 129 1 O THR K 127 N VAL K 12 SHEET 3 AD6 6 ALA K 98 GLY K 104 -1 N ALA K 98 O VAL K 126 SHEET 4 AD6 6 ILE K 40 GLN K 45 -1 N PHE K 43 O TYR K 101 SHEET 5 AD6 6 GLU K 52 ILE K 57 -1 O GLY K 55 N TRP K 42 SHEET 6 AD6 6 THR K 64 TYR K 66 -1 O ASP K 65 N GLY K 56 SHEET 1 AD7 4 LEU K 11 GLN K 13 0 SHEET 2 AD7 4 THR K 124 SER K 129 1 O THR K 127 N VAL K 12 SHEET 3 AD7 4 ALA K 98 GLY K 104 -1 N ALA K 98 O VAL K 126 SHEET 4 AD7 4 TYR K 119 TRP K 120 -1 O TYR K 119 N GLY K 104 SHEET 1 AD8 4 GLN L 3 SER L 7 0 SHEET 2 AD8 4 LEU L 18 SER L 25 -1 O SER L 25 N GLN L 3 SHEET 3 AD8 4 THR L 84 MET L 89 -1 O LEU L 87 N LEU L 20 SHEET 4 AD8 4 PHE L 74 ASP L 79 -1 N THR L 75 O GLN L 88 SHEET 1 AD9 6 GLY L 10 GLN L 13 0 SHEET 2 AD9 6 THR L 124 SER L 129 1 O SER L 129 N VAL L 12 SHEET 3 AD9 6 ALA L 98 GLY L 104 -1 N TYR L 100 O THR L 124 SHEET 4 AD9 6 ILE L 40 GLN L 45 -1 N PHE L 43 O TYR L 101 SHEET 5 AD9 6 ARG L 51 ILE L 57 -1 O GLY L 55 N TRP L 42 SHEET 6 AD9 6 THR L 64 TYR L 66 -1 O ASP L 65 N GLY L 56 SHEET 1 AE1 4 GLY L 10 GLN L 13 0 SHEET 2 AE1 4 THR L 124 SER L 129 1 O SER L 129 N VAL L 12 SHEET 3 AE1 4 ALA L 98 GLY L 104 -1 N TYR L 100 O THR L 124 SHEET 4 AE1 4 TYR L 119 TRP L 120 -1 O TYR L 119 N GLY L 104 SSBOND 1 CYS G 22 CYS G 102 1555 1555 2.04 SSBOND 2 CYS H 22 CYS H 102 1555 1555 2.03 SSBOND 3 CYS I 22 CYS I 102 1555 1555 2.04 SSBOND 4 CYS J 22 CYS J 102 1555 1555 2.04 SSBOND 5 CYS K 22 CYS K 102 1555 1555 2.04 SSBOND 6 CYS L 22 CYS L 102 1555 1555 2.04 CISPEP 1 ILE A 373 PRO A 374 0 3.99 CISPEP 2 ILE D 373 PRO D 374 0 12.53 CRYST1 167.520 168.420 177.130 90.00 90.00 90.00 P 21 21 2 24 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 0.005969 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005938 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005646 0.00000