HEADER VIRAL PROTEIN 12-DEC-24 9HPA TITLE STRUCTURE OF A16/G9 (VACCINIA VIRUS) IN COMPLEX WITH VHH D07 AND VHH TITLE 2 E12 COMPND MOL_ID: 1; COMPND 2 MOLECULE: VIRION MEMBRANE PROTEIN OPG143; COMPND 3 CHAIN: A, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ENTRY-FUSION COMPLEX PROTEIN OPG094; COMPND 7 CHAIN: B, F; COMPND 8 SYNONYM: EFC PROTEIN OPG094,MYRISTOYLATED PROTEIN G9,PROTEIN F1; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: VHH E12; COMPND 12 CHAIN: D, H; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: VHH D07; COMPND 16 CHAIN: C, G; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VACCINIA VIRUS WESTERN RESERVE; SOURCE 3 ORGANISM_TAXID: 696871; SOURCE 4 GENE: OPG143, VACWR136, A16L; SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VACCINIA VIRUS WESTERN RESERVE; SOURCE 9 ORGANISM_TAXID: 696871; SOURCE 10 GENE: OPG094, VACWR087, G9R; SOURCE 11 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 15 ORGANISM_TAXID: 30538; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 20 ORGANISM_TAXID: 30538; SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 22 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS POXVIRUS, VIRAL FUSION, VACCINIA VIRUS, MPOX VIRUS, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR R.VERNUCCIO,A.MEOLA,P.GUARDADO-CALVO REVDAT 2 10-SEP-25 9HPA 1 JRNL REVDAT 1 03-SEP-25 9HPA 0 JRNL AUTH A.MEOLA,R.VERNUCCIO,L.BATTINI,G.ALBERICIO,P.DELGADO, JRNL AUTH 2 R.BAMFORD,L.POKORNY,M.BROUTIN,A.MARTINEZ LEON,S.GALLIEN, JRNL AUTH 3 M.GIL,M.A.NORIEGA,F.GUIVEL-BENHASSINE,F.PORROT,J.POSTAL, JRNL AUTH 4 J.BUCHRIESER,M.HUBERT,A.HAOUZ,P.LAFAYE,M.ESTEBAN,J.S.HUB, JRNL AUTH 5 M.MAHEVAS,P.CHAPPERT,J.MERCER,J.GARCIA-ARRIAZA,O.SCHWARTZ, JRNL AUTH 6 P.GUARDADO-CALVO JRNL TITL STRUCTURAL BASIS OF POXVIRUS FUSION REGULATION AND JRNL TITL 2 ANTI-A16/G9 ANTIBODY-MEDIATED NEUTRALIZATION AND PROTECTION. JRNL REF CELL 2025 JRNL REFN ISSN 1097-4172 JRNL PMID 40865523 JRNL DOI 10.1016/J.CELL.2025.07.040 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.33 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 3 NUMBER OF REFLECTIONS : 38638 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.225 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.265 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130 REMARK 3 FREE R VALUE TEST SET COUNT : 1982 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 39.3300 - 7.4600 0.93 2695 145 0.1821 0.2062 REMARK 3 2 7.4500 - 5.9200 0.96 2640 146 0.2061 0.2212 REMARK 3 3 5.9200 - 5.1800 0.96 2606 143 0.1929 0.2465 REMARK 3 4 5.1800 - 4.7100 0.96 2620 149 0.1781 0.2386 REMARK 3 5 4.7000 - 4.3700 0.97 2592 148 0.1746 0.2386 REMARK 3 6 4.3700 - 4.1100 0.97 2601 146 0.1980 0.2673 REMARK 3 7 4.1100 - 3.9100 0.98 2618 146 0.2297 0.2534 REMARK 3 8 3.9100 - 3.7400 0.98 2625 134 0.2322 0.2998 REMARK 3 9 3.7400 - 3.5900 0.97 2613 141 0.2506 0.2947 REMARK 3 10 3.5900 - 3.4700 0.97 2582 150 0.2701 0.3391 REMARK 3 11 3.4700 - 3.3600 0.98 2615 126 0.2959 0.3016 REMARK 3 12 3.3600 - 3.2600 0.98 2605 127 0.3150 0.3825 REMARK 3 13 3.2600 - 3.1800 0.98 2650 147 0.3296 0.3528 REMARK 3 14 3.1800 - 3.1000 0.98 2594 134 0.3395 0.3815 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) : 0.477 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.873 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 70.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.56 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 12976 REMARK 3 ANGLE : 0.469 17535 REMARK 3 CHIRALITY : 0.041 1824 REMARK 3 PLANARITY : 0.004 2288 REMARK 3 DIHEDRAL : 10.649 4824 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 24 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESID 5:94) REMARK 3 ORIGIN FOR THE GROUP (A): -10.1902 -15.7488 60.4271 REMARK 3 T TENSOR REMARK 3 T11: 0.8522 T22: 0.8097 REMARK 3 T33: 0.6921 T12: 0.0116 REMARK 3 T13: -0.0679 T23: 0.0430 REMARK 3 L TENSOR REMARK 3 L11: 2.0901 L22: 1.6835 REMARK 3 L33: 1.6563 L12: -0.6029 REMARK 3 L13: 2.3610 L23: -0.7815 REMARK 3 S TENSOR REMARK 3 S11: 0.1437 S12: -0.1384 S13: -0.0295 REMARK 3 S21: 0.2328 S22: 0.1146 S23: -0.1699 REMARK 3 S31: 0.0185 S32: 0.0051 S33: -0.0001 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 95:241) REMARK 3 ORIGIN FOR THE GROUP (A): -26.2361 -18.8304 26.9062 REMARK 3 T TENSOR REMARK 3 T11: 0.7704 T22: 0.7134 REMARK 3 T33: 0.7335 T12: -0.0098 REMARK 3 T13: -0.0188 T23: -0.0023 REMARK 3 L TENSOR REMARK 3 L11: 1.4406 L22: 0.2553 REMARK 3 L33: 5.5621 L12: -0.1601 REMARK 3 L13: 2.7716 L23: -0.4567 REMARK 3 S TENSOR REMARK 3 S11: -0.1261 S12: -0.1341 S13: -0.0813 REMARK 3 S21: 0.1192 S22: 0.0219 S23: -0.0217 REMARK 3 S31: -0.1505 S32: -0.2310 S33: 0.0001 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN A AND RESID 242:294) REMARK 3 ORIGIN FOR THE GROUP (A): -41.4387 -14.7101 -12.3742 REMARK 3 T TENSOR REMARK 3 T11: 0.7108 T22: 0.8203 REMARK 3 T33: 0.7344 T12: -0.1459 REMARK 3 T13: -0.0468 T23: 0.0004 REMARK 3 L TENSOR REMARK 3 L11: 2.1625 L22: 0.9887 REMARK 3 L33: 2.4362 L12: -0.6633 REMARK 3 L13: -0.4933 L23: -0.3329 REMARK 3 S TENSOR REMARK 3 S11: -0.1300 S12: -0.4478 S13: 0.3036 REMARK 3 S21: -0.0428 S22: -0.3341 S23: 0.0959 REMARK 3 S31: -0.0372 S32: -0.2448 S33: 0.0002 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN B AND RESID 7:107) REMARK 3 ORIGIN FOR THE GROUP (A): -19.5523 -30.6772 33.2418 REMARK 3 T TENSOR REMARK 3 T11: 0.8675 T22: 0.6381 REMARK 3 T33: 0.7799 T12: 0.0287 REMARK 3 T13: -0.0992 T23: 0.0165 REMARK 3 L TENSOR REMARK 3 L11: 0.8717 L22: 0.4796 REMARK 3 L33: 3.0441 L12: 0.2499 REMARK 3 L13: -0.4735 L23: 1.2110 REMARK 3 S TENSOR REMARK 3 S11: 0.2061 S12: 0.1502 S13: -0.0123 REMARK 3 S21: 0.0116 S22: -0.0179 S23: -0.0924 REMARK 3 S31: 0.2576 S32: 0.1958 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN B AND RESID 108:158) REMARK 3 ORIGIN FOR THE GROUP (A): -22.1466 -30.3633 5.8797 REMARK 3 T TENSOR REMARK 3 T11: 0.9184 T22: 0.6983 REMARK 3 T33: 0.9318 T12: -0.0390 REMARK 3 T13: -0.0755 T23: 0.0953 REMARK 3 L TENSOR REMARK 3 L11: 2.3367 L22: 1.7727 REMARK 3 L33: 3.0335 L12: -1.1245 REMARK 3 L13: -0.0342 L23: 0.8378 REMARK 3 S TENSOR REMARK 3 S11: -0.0139 S12: 0.0486 S13: -0.2656 REMARK 3 S21: -0.0790 S22: -0.0117 S23: 0.2550 REMARK 3 S31: 0.2649 S32: 0.3506 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN B AND RESID 159:271) REMARK 3 ORIGIN FOR THE GROUP (A): -25.6655 -22.8692 -20.0880 REMARK 3 T TENSOR REMARK 3 T11: 0.6816 T22: 0.7905 REMARK 3 T33: 0.7027 T12: -0.0269 REMARK 3 T13: 0.0682 T23: 0.0281 REMARK 3 L TENSOR REMARK 3 L11: 2.6927 L22: 2.5682 REMARK 3 L33: 4.0467 L12: -1.2752 REMARK 3 L13: 1.1917 L23: -1.1113 REMARK 3 S TENSOR REMARK 3 S11: 0.1350 S12: 0.3195 S13: 0.1157 REMARK 3 S21: -0.0118 S22: -0.2460 S23: -0.1642 REMARK 3 S31: 0.5829 S32: 0.4817 S33: 0.0000 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN C AND RESID 3:47) REMARK 3 ORIGIN FOR THE GROUP (A): -18.2717 -11.4906 -43.8418 REMARK 3 T TENSOR REMARK 3 T11: 0.5441 T22: 0.6103 REMARK 3 T33: 0.6791 T12: 0.0274 REMARK 3 T13: -0.0195 T23: -0.1156 REMARK 3 L TENSOR REMARK 3 L11: 1.2024 L22: 2.0899 REMARK 3 L33: 3.2222 L12: -0.3889 REMARK 3 L13: -0.9524 L23: -0.7560 REMARK 3 S TENSOR REMARK 3 S11: 0.3347 S12: -0.0992 S13: 0.0082 REMARK 3 S21: -0.1963 S22: -0.3650 S23: -0.0652 REMARK 3 S31: 0.0893 S32: 0.0606 S33: 0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN C AND RESID 48:100) REMARK 3 ORIGIN FOR THE GROUP (A): -19.0283 -14.6021 -37.4472 REMARK 3 T TENSOR REMARK 3 T11: 0.5868 T22: 0.8076 REMARK 3 T33: 0.6195 T12: 0.0985 REMARK 3 T13: -0.0291 T23: 0.0602 REMARK 3 L TENSOR REMARK 3 L11: 1.3772 L22: 0.1628 REMARK 3 L33: 1.8302 L12: -0.0662 REMARK 3 L13: -1.4298 L23: -0.1295 REMARK 3 S TENSOR REMARK 3 S11: 0.0264 S12: -0.3029 S13: -0.2913 REMARK 3 S21: 0.4322 S22: 0.0055 S23: 0.0565 REMARK 3 S31: 0.0784 S32: -0.4143 S33: 0.0001 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN C AND RESID 101:120) REMARK 3 ORIGIN FOR THE GROUP (A): -23.4353 -11.2296 -46.4247 REMARK 3 T TENSOR REMARK 3 T11: 0.7764 T22: 1.0923 REMARK 3 T33: 0.9779 T12: 0.0956 REMARK 3 T13: -0.1028 T23: 0.0953 REMARK 3 L TENSOR REMARK 3 L11: 0.7774 L22: 0.5450 REMARK 3 L33: 1.6571 L12: 0.4569 REMARK 3 L13: -0.3225 L23: -0.4163 REMARK 3 S TENSOR REMARK 3 S11: -0.1403 S12: -1.1466 S13: 0.2531 REMARK 3 S21: -0.3127 S22: 0.4322 S23: 0.3786 REMARK 3 S31: -0.2393 S32: -0.2573 S33: 0.0004 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN D AND RESID 3:62) REMARK 3 ORIGIN FOR THE GROUP (A): -59.9484 -10.8450 -19.2067 REMARK 3 T TENSOR REMARK 3 T11: 0.6756 T22: 1.4552 REMARK 3 T33: 0.9436 T12: 0.0917 REMARK 3 T13: 0.0438 T23: 0.0834 REMARK 3 L TENSOR REMARK 3 L11: 2.9699 L22: 0.5761 REMARK 3 L33: 2.4845 L12: 0.7913 REMARK 3 L13: 0.7942 L23: -0.5074 REMARK 3 S TENSOR REMARK 3 S11: 0.2893 S12: -0.5018 S13: 0.2282 REMARK 3 S21: 0.2231 S22: 0.3618 S23: 0.0056 REMARK 3 S31: -0.1407 S32: -1.2714 S33: 0.0108 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN D AND RESID 63:96) REMARK 3 ORIGIN FOR THE GROUP (A): -65.6480 -13.5521 -16.2479 REMARK 3 T TENSOR REMARK 3 T11: 0.7560 T22: 1.8650 REMARK 3 T33: 0.9497 T12: 0.0019 REMARK 3 T13: 0.0324 T23: 0.0593 REMARK 3 L TENSOR REMARK 3 L11: 0.6148 L22: 1.2741 REMARK 3 L33: 0.0323 L12: 0.3276 REMARK 3 L13: 0.1254 L23: 0.2624 REMARK 3 S TENSOR REMARK 3 S11: -0.1825 S12: -0.5097 S13: -0.2888 REMARK 3 S21: 0.2551 S22: -0.0224 S23: 0.5391 REMARK 3 S31: -0.6930 S32: -0.3529 S33: 0.0001 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN D AND RESID 97:119) REMARK 3 ORIGIN FOR THE GROUP (A): -52.3261 -8.2944 -24.2550 REMARK 3 T TENSOR REMARK 3 T11: 0.6184 T22: 1.5071 REMARK 3 T33: 0.7363 T12: 0.0911 REMARK 3 T13: -0.0560 T23: -0.0135 REMARK 3 L TENSOR REMARK 3 L11: 1.0701 L22: 1.8056 REMARK 3 L33: 0.8293 L12: 0.9663 REMARK 3 L13: -0.4716 L23: -1.0685 REMARK 3 S TENSOR REMARK 3 S11: -0.0196 S12: 0.4816 S13: 0.7181 REMARK 3 S21: 0.1351 S22: -0.3478 S23: 0.1089 REMARK 3 S31: -1.1831 S32: -0.7866 S33: 0.0194 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: (CHAIN E AND RESID 5:81) REMARK 3 ORIGIN FOR THE GROUP (A): 13.1095 -15.7346 33.1912 REMARK 3 T TENSOR REMARK 3 T11: 1.8284 T22: 0.7803 REMARK 3 T33: 1.0727 T12: -0.1315 REMARK 3 T13: -0.3564 T23: 0.2337 REMARK 3 L TENSOR REMARK 3 L11: 0.7471 L22: 1.9378 REMARK 3 L33: 2.7942 L12: 0.2426 REMARK 3 L13: 0.1324 L23: 2.5129 REMARK 3 S TENSOR REMARK 3 S11: 0.1952 S12: 0.2435 S13: 0.0719 REMARK 3 S21: -0.8257 S22: 0.3266 S23: 0.7915 REMARK 3 S31: 1.0287 S32: -0.3593 S33: 0.0137 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: (CHAIN E AND RESID 82:133) REMARK 3 ORIGIN FOR THE GROUP (A): 7.1614 -20.5221 36.3380 REMARK 3 T TENSOR REMARK 3 T11: 2.2755 T22: 1.2221 REMARK 3 T33: 1.0312 T12: -0.4700 REMARK 3 T13: -0.5982 T23: 0.2146 REMARK 3 L TENSOR REMARK 3 L11: 2.2078 L22: 0.3966 REMARK 3 L33: 0.3572 L12: 0.9702 REMARK 3 L13: 0.9015 L23: 0.3949 REMARK 3 S TENSOR REMARK 3 S11: -0.2449 S12: 0.0392 S13: 0.7103 REMARK 3 S21: -1.6380 S22: 0.2389 S23: 0.9766 REMARK 3 S31: 0.4958 S32: -1.6484 S33: 0.0046 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: (CHAIN E AND RESID 134:294) REMARK 3 ORIGIN FOR THE GROUP (A): 37.8657 -16.9381 90.3941 REMARK 3 T TENSOR REMARK 3 T11: 0.7645 T22: 0.7876 REMARK 3 T33: 0.9886 T12: -0.0225 REMARK 3 T13: -0.0953 T23: -0.0529 REMARK 3 L TENSOR REMARK 3 L11: 0.7461 L22: -0.0983 REMARK 3 L33: 4.7998 L12: -0.3013 REMARK 3 L13: 2.0361 L23: 0.6241 REMARK 3 S TENSOR REMARK 3 S11: -0.1371 S12: 0.2478 S13: 0.2168 REMARK 3 S21: -0.1655 S22: 0.1052 S23: -0.1055 REMARK 3 S31: -0.1642 S32: 0.7455 S33: 0.0001 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: (CHAIN F AND RESID 7:83) REMARK 3 ORIGIN FOR THE GROUP (A): 20.0544 -29.2492 56.0593 REMARK 3 T TENSOR REMARK 3 T11: 1.3084 T22: 0.6419 REMARK 3 T33: 0.8348 T12: 0.0272 REMARK 3 T13: -0.1317 T23: 0.0190 REMARK 3 L TENSOR REMARK 3 L11: 0.6317 L22: 1.9147 REMARK 3 L33: 2.1307 L12: 0.8891 REMARK 3 L13: -0.8854 L23: -0.2588 REMARK 3 S TENSOR REMARK 3 S11: 0.1220 S12: 0.1015 S13: 0.0954 REMARK 3 S21: -0.9549 S22: 0.0502 S23: -0.1125 REMARK 3 S31: -0.0016 S32: -0.1519 S33: 0.0169 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: (CHAIN F AND RESID 84:174) REMARK 3 ORIGIN FOR THE GROUP (A): 22.3426 -31.1349 88.3182 REMARK 3 T TENSOR REMARK 3 T11: 0.9135 T22: 0.6570 REMARK 3 T33: 0.9276 T12: 0.0724 REMARK 3 T13: -0.2422 T23: -0.0764 REMARK 3 L TENSOR REMARK 3 L11: 0.9368 L22: 1.7734 REMARK 3 L33: 4.3058 L12: 1.2672 REMARK 3 L13: 0.2471 L23: -0.4280 REMARK 3 S TENSOR REMARK 3 S11: 0.0278 S12: 0.0765 S13: -0.1393 REMARK 3 S21: -0.0159 S22: 0.0850 S23: -0.0529 REMARK 3 S31: 0.7697 S32: 0.1404 S33: 0.0000 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: (CHAIN F AND RESID 175:271) REMARK 3 ORIGIN FOR THE GROUP (A): 27.4144 -21.8080 118.3117 REMARK 3 T TENSOR REMARK 3 T11: 0.6953 T22: 0.7241 REMARK 3 T33: 0.8138 T12: 0.1068 REMARK 3 T13: -0.1323 T23: -0.0811 REMARK 3 L TENSOR REMARK 3 L11: 1.2733 L22: 1.7311 REMARK 3 L33: 3.3981 L12: 0.1552 REMARK 3 L13: -0.3859 L23: -0.3955 REMARK 3 S TENSOR REMARK 3 S11: 0.0330 S12: -0.3801 S13: 0.0754 REMARK 3 S21: 0.2822 S22: 0.0582 S23: -0.0030 REMARK 3 S31: 0.4701 S32: 0.0397 S33: 0.0000 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: (CHAIN G AND RESID 3:13) REMARK 3 ORIGIN FOR THE GROUP (A): 13.3650 -6.0796 143.0753 REMARK 3 T TENSOR REMARK 3 T11: 0.8564 T22: 0.6164 REMARK 3 T33: 0.7791 T12: 0.0537 REMARK 3 T13: 0.1291 T23: 0.0105 REMARK 3 L TENSOR REMARK 3 L11: 5.1355 L22: 6.4914 REMARK 3 L33: 1.2708 L12: 4.7373 REMARK 3 L13: 2.3413 L23: 1.6111 REMARK 3 S TENSOR REMARK 3 S11: 0.9114 S12: -0.8162 S13: 1.8680 REMARK 3 S21: 0.3505 S22: -1.4522 S23: 2.4466 REMARK 3 S31: -0.4561 S32: -0.8445 S33: -0.1174 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: (CHAIN G AND RESID 14:89) REMARK 3 ORIGIN FOR THE GROUP (A): 17.5151 -12.9250 133.6374 REMARK 3 T TENSOR REMARK 3 T11: 0.5997 T22: 0.8256 REMARK 3 T33: 0.7323 T12: -0.0169 REMARK 3 T13: -0.1097 T23: -0.0915 REMARK 3 L TENSOR REMARK 3 L11: 4.2385 L22: 2.4379 REMARK 3 L33: 2.9566 L12: 0.9343 REMARK 3 L13: -1.7578 L23: 1.0824 REMARK 3 S TENSOR REMARK 3 S11: 0.1575 S12: -0.1075 S13: -0.3923 REMARK 3 S21: -0.1564 S22: -0.2605 S23: -0.1130 REMARK 3 S31: 0.1269 S32: -0.0956 S33: 0.0000 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: (CHAIN G AND RESID 90:120) REMARK 3 ORIGIN FOR THE GROUP (A): 20.2456 -12.3920 140.9008 REMARK 3 T TENSOR REMARK 3 T11: 0.6726 T22: 0.8012 REMARK 3 T33: 0.7984 T12: -0.0140 REMARK 3 T13: -0.1606 T23: -0.0389 REMARK 3 L TENSOR REMARK 3 L11: 2.6699 L22: 2.5466 REMARK 3 L33: 3.0677 L12: -2.4029 REMARK 3 L13: -1.6986 L23: 0.9992 REMARK 3 S TENSOR REMARK 3 S11: 0.1673 S12: -0.7621 S13: 0.8046 REMARK 3 S21: -0.2256 S22: 0.0571 S23: 0.6216 REMARK 3 S31: 0.0743 S32: 0.3715 S33: 0.0001 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: (CHAIN H AND RESID 3:16) REMARK 3 ORIGIN FOR THE GROUP (A): 64.6138 -4.4850 119.5971 REMARK 3 T TENSOR REMARK 3 T11: 0.9724 T22: 1.5667 REMARK 3 T33: 1.3196 T12: -0.1775 REMARK 3 T13: 0.0881 T23: -0.4131 REMARK 3 L TENSOR REMARK 3 L11: 0.3941 L22: 0.2193 REMARK 3 L33: 0.7213 L12: 0.2821 REMARK 3 L13: 0.5324 L23: 0.3819 REMARK 3 S TENSOR REMARK 3 S11: 0.9994 S12: 1.8378 S13: -0.1349 REMARK 3 S21: -0.1559 S22: -0.0308 S23: -1.1336 REMARK 3 S31: -1.5932 S32: 0.3338 S33: 0.0050 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: (CHAIN H AND RESID 17:91) REMARK 3 ORIGIN FOR THE GROUP (A): 61.1808 -13.1573 114.9080 REMARK 3 T TENSOR REMARK 3 T11: 0.6876 T22: 1.2476 REMARK 3 T33: 0.9749 T12: -0.0460 REMARK 3 T13: -0.0207 T23: -0.0861 REMARK 3 L TENSOR REMARK 3 L11: 1.6188 L22: 2.7937 REMARK 3 L33: 1.4225 L12: -0.6090 REMARK 3 L13: 0.1599 L23: 0.5227 REMARK 3 S TENSOR REMARK 3 S11: 0.0228 S12: 0.3198 S13: 0.2429 REMARK 3 S21: -0.2904 S22: 0.3255 S23: 0.0859 REMARK 3 S31: 0.1937 S32: 1.7366 S33: -0.0001 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: (CHAIN H AND RESID 92:119) REMARK 3 ORIGIN FOR THE GROUP (A): 53.9934 -6.7271 118.9079 REMARK 3 T TENSOR REMARK 3 T11: 0.7076 T22: 1.1273 REMARK 3 T33: 1.1547 T12: -0.0780 REMARK 3 T13: -0.0149 T23: 0.0308 REMARK 3 L TENSOR REMARK 3 L11: 0.7002 L22: 1.1112 REMARK 3 L33: 0.0255 L12: -0.6201 REMARK 3 L13: -0.0669 L23: 0.1871 REMARK 3 S TENSOR REMARK 3 S11: 0.0280 S12: 0.2734 S13: 1.2365 REMARK 3 S21: -0.5752 S22: 0.0071 S23: -0.4117 REMARK 3 S31: -0.2454 S32: 0.7916 S33: 0.0003 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 9HPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292143891. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-SEP-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.978565 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38737 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 39.330 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 7.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.24 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 (%): 48.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % W/V PEG 1K, 0.1 M NA PHOS CIT PH REMARK 280 4.2, 0.2 M LISO4 (CRYOPROTECTED WITH 33% ETHYLENE GLYCOL), VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 39.10200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 92.85400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.02050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 92.85400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.10200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.02050 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 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, H, 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 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 -18 REMARK 465 LYS A -17 REMARK 465 LEU A -16 REMARK 465 CYS A -15 REMARK 465 ILE A -14 REMARK 465 LEU A -13 REMARK 465 LEU A -12 REMARK 465 ALA A -11 REMARK 465 VAL A -10 REMARK 465 VAL A -9 REMARK 465 ALA A -8 REMARK 465 PHE A -7 REMARK 465 VAL A -6 REMARK 465 GLY A -5 REMARK 465 LEU A -4 REMARK 465 SER A -3 REMARK 465 LEU A -2 REMARK 465 GLY A -1 REMARK 465 ARG A 0 REMARK 465 SER A 1 REMARK 465 ALA A 2 REMARK 465 ALA A 3 REMARK 465 ALA A 4 REMARK 465 GLY A 295 REMARK 465 GLY A 296 REMARK 465 SER A 297 REMARK 465 GLY A 298 REMARK 465 LEU A 299 REMARK 465 VAL A 300 REMARK 465 PRO A 301 REMARK 465 ARG A 302 REMARK 465 GLY A 303 REMARK 465 SER A 304 REMARK 465 GLY A 305 REMARK 465 GLY A 306 REMARK 465 SER A 307 REMARK 465 GLY A 308 REMARK 465 GLY A 309 REMARK 465 SER A 310 REMARK 465 HIS A 311 REMARK 465 HIS A 312 REMARK 465 HIS A 313 REMARK 465 HIS A 314 REMARK 465 HIS A 315 REMARK 465 HIS A 316 REMARK 465 HIS A 317 REMARK 465 HIS A 318 REMARK 465 GLY A 319 REMARK 465 GLY A 320 REMARK 465 SER A 321 REMARK 465 GLY A 322 REMARK 465 THR A 323 REMARK 465 GLY A 324 REMARK 465 GLY A 325 REMARK 465 LEU A 326 REMARK 465 ASN A 327 REMARK 465 ASP A 328 REMARK 465 ILE A 329 REMARK 465 PHE A 330 REMARK 465 GLU A 331 REMARK 465 ALA A 332 REMARK 465 GLN A 333 REMARK 465 LYS A 334 REMARK 465 ILE A 335 REMARK 465 GLU A 336 REMARK 465 TRP A 337 REMARK 465 HIS A 338 REMARK 465 GLU A 339 REMARK 465 MET B -16 REMARK 465 LYS B -15 REMARK 465 LEU B -14 REMARK 465 CYS B -13 REMARK 465 ILE B -12 REMARK 465 LEU B -11 REMARK 465 LEU B -10 REMARK 465 ALA B -9 REMARK 465 VAL B -8 REMARK 465 VAL B -7 REMARK 465 ALA B -6 REMARK 465 PHE B -5 REMARK 465 VAL B -4 REMARK 465 GLY B -3 REMARK 465 LEU B -2 REMARK 465 SER B -1 REMARK 465 LEU B 0 REMARK 465 GLY B 1 REMARK 465 ALA B 2 REMARK 465 GLY B 3 REMARK 465 GLY B 4 REMARK 465 VAL B 5 REMARK 465 SER B 6 REMARK 465 GLY B 272 REMARK 465 SER B 273 REMARK 465 GLY B 274 REMARK 465 LEU B 275 REMARK 465 VAL B 276 REMARK 465 PRO B 277 REMARK 465 ARG B 278 REMARK 465 GLY B 279 REMARK 465 SER B 280 REMARK 465 LEU B 281 REMARK 465 GLU B 282 REMARK 465 ASP B 283 REMARK 465 ASP B 284 REMARK 465 ASP B 285 REMARK 465 ASP B 286 REMARK 465 LYS B 287 REMARK 465 ALA B 288 REMARK 465 GLY B 289 REMARK 465 TRP B 290 REMARK 465 SER B 291 REMARK 465 HIS B 292 REMARK 465 PRO B 293 REMARK 465 GLN B 294 REMARK 465 PHE B 295 REMARK 465 GLU B 296 REMARK 465 LYS B 297 REMARK 465 GLY B 298 REMARK 465 GLY B 299 REMARK 465 GLY B 300 REMARK 465 SER B 301 REMARK 465 GLY B 302 REMARK 465 GLY B 303 REMARK 465 GLY B 304 REMARK 465 SER B 305 REMARK 465 GLY B 306 REMARK 465 GLY B 307 REMARK 465 GLY B 308 REMARK 465 SER B 309 REMARK 465 TRP B 310 REMARK 465 SER B 311 REMARK 465 HIS B 312 REMARK 465 PRO B 313 REMARK 465 GLN B 314 REMARK 465 PHE B 315 REMARK 465 GLU B 316 REMARK 465 LYS B 317 REMARK 465 MET D 1 REMARK 465 GLY D 2 REMARK 465 VAL D 120 REMARK 465 SER D 121 REMARK 465 SER D 122 REMARK 465 LEU D 123 REMARK 465 GLU D 124 REMARK 465 HIS D 125 REMARK 465 HIS D 126 REMARK 465 HIS D 127 REMARK 465 HIS D 128 REMARK 465 HIS D 129 REMARK 465 HIS D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 465 GLY D 133 REMARK 465 SER D 134 REMARK 465 GLY D 135 REMARK 465 LEU D 136 REMARK 465 VAL D 137 REMARK 465 PRO D 138 REMARK 465 ARG D 139 REMARK 465 GLY D 140 REMARK 465 SER D 141 REMARK 465 GLY D 142 REMARK 465 LEU D 143 REMARK 465 ASN D 144 REMARK 465 ASP D 145 REMARK 465 ILE D 146 REMARK 465 PHE D 147 REMARK 465 GLU D 148 REMARK 465 ALA D 149 REMARK 465 GLN D 150 REMARK 465 LYS D 151 REMARK 465 ILE D 152 REMARK 465 GLU D 153 REMARK 465 TRP D 154 REMARK 465 HIS D 155 REMARK 465 GLU D 156 REMARK 465 MET C 1 REMARK 465 GLY C 2 REMARK 465 LEU C 121 REMARK 465 GLU C 122 REMARK 465 HIS C 123 REMARK 465 HIS C 124 REMARK 465 HIS C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 465 GLY C 131 REMARK 465 SER C 132 REMARK 465 GLY C 133 REMARK 465 LEU C 134 REMARK 465 VAL C 135 REMARK 465 PRO C 136 REMARK 465 ARG C 137 REMARK 465 GLY C 138 REMARK 465 SER C 139 REMARK 465 GLY C 140 REMARK 465 LEU C 141 REMARK 465 ASN C 142 REMARK 465 ASP C 143 REMARK 465 ILE C 144 REMARK 465 PHE C 145 REMARK 465 GLU C 146 REMARK 465 ALA C 147 REMARK 465 GLN C 148 REMARK 465 LYS C 149 REMARK 465 ILE C 150 REMARK 465 GLU C 151 REMARK 465 TRP C 152 REMARK 465 HIS C 153 REMARK 465 GLU C 154 REMARK 465 MET E -18 REMARK 465 LYS E -17 REMARK 465 LEU E -16 REMARK 465 CYS E -15 REMARK 465 ILE E -14 REMARK 465 LEU E -13 REMARK 465 LEU E -12 REMARK 465 ALA E -11 REMARK 465 VAL E -10 REMARK 465 VAL E -9 REMARK 465 ALA E -8 REMARK 465 PHE E -7 REMARK 465 VAL E -6 REMARK 465 GLY E -5 REMARK 465 LEU E -4 REMARK 465 SER E -3 REMARK 465 LEU E -2 REMARK 465 GLY E -1 REMARK 465 ARG E 0 REMARK 465 SER E 1 REMARK 465 ALA E 2 REMARK 465 ALA E 3 REMARK 465 ALA E 4 REMARK 465 GLY E 295 REMARK 465 GLY E 296 REMARK 465 SER E 297 REMARK 465 GLY E 298 REMARK 465 LEU E 299 REMARK 465 VAL E 300 REMARK 465 PRO E 301 REMARK 465 ARG E 302 REMARK 465 GLY E 303 REMARK 465 SER E 304 REMARK 465 GLY E 305 REMARK 465 GLY E 306 REMARK 465 SER E 307 REMARK 465 GLY E 308 REMARK 465 GLY E 309 REMARK 465 SER E 310 REMARK 465 HIS E 311 REMARK 465 HIS E 312 REMARK 465 HIS E 313 REMARK 465 HIS E 314 REMARK 465 HIS E 315 REMARK 465 HIS E 316 REMARK 465 HIS E 317 REMARK 465 HIS E 318 REMARK 465 GLY E 319 REMARK 465 GLY E 320 REMARK 465 SER E 321 REMARK 465 GLY E 322 REMARK 465 THR E 323 REMARK 465 GLY E 324 REMARK 465 GLY E 325 REMARK 465 LEU E 326 REMARK 465 ASN E 327 REMARK 465 ASP E 328 REMARK 465 ILE E 329 REMARK 465 PHE E 330 REMARK 465 GLU E 331 REMARK 465 ALA E 332 REMARK 465 GLN E 333 REMARK 465 LYS E 334 REMARK 465 ILE E 335 REMARK 465 GLU E 336 REMARK 465 TRP E 337 REMARK 465 HIS E 338 REMARK 465 GLU E 339 REMARK 465 MET F -16 REMARK 465 LYS F -15 REMARK 465 LEU F -14 REMARK 465 CYS F -13 REMARK 465 ILE F -12 REMARK 465 LEU F -11 REMARK 465 LEU F -10 REMARK 465 ALA F -9 REMARK 465 VAL F -8 REMARK 465 VAL F -7 REMARK 465 ALA F -6 REMARK 465 PHE F -5 REMARK 465 VAL F -4 REMARK 465 GLY F -3 REMARK 465 LEU F -2 REMARK 465 SER F -1 REMARK 465 LEU F 0 REMARK 465 GLY F 1 REMARK 465 ALA F 2 REMARK 465 GLY F 3 REMARK 465 GLY F 4 REMARK 465 VAL F 5 REMARK 465 SER F 6 REMARK 465 GLY F 272 REMARK 465 SER F 273 REMARK 465 GLY F 274 REMARK 465 LEU F 275 REMARK 465 VAL F 276 REMARK 465 PRO F 277 REMARK 465 ARG F 278 REMARK 465 GLY F 279 REMARK 465 SER F 280 REMARK 465 LEU F 281 REMARK 465 GLU F 282 REMARK 465 ASP F 283 REMARK 465 ASP F 284 REMARK 465 ASP F 285 REMARK 465 ASP F 286 REMARK 465 LYS F 287 REMARK 465 ALA F 288 REMARK 465 GLY F 289 REMARK 465 TRP F 290 REMARK 465 SER F 291 REMARK 465 HIS F 292 REMARK 465 PRO F 293 REMARK 465 GLN F 294 REMARK 465 PHE F 295 REMARK 465 GLU F 296 REMARK 465 LYS F 297 REMARK 465 GLY F 298 REMARK 465 GLY F 299 REMARK 465 GLY F 300 REMARK 465 SER F 301 REMARK 465 GLY F 302 REMARK 465 GLY F 303 REMARK 465 GLY F 304 REMARK 465 SER F 305 REMARK 465 GLY F 306 REMARK 465 GLY F 307 REMARK 465 GLY F 308 REMARK 465 SER F 309 REMARK 465 TRP F 310 REMARK 465 SER F 311 REMARK 465 HIS F 312 REMARK 465 PRO F 313 REMARK 465 GLN F 314 REMARK 465 PHE F 315 REMARK 465 GLU F 316 REMARK 465 LYS F 317 REMARK 465 MET H 1 REMARK 465 GLY H 2 REMARK 465 VAL H 120 REMARK 465 SER H 121 REMARK 465 SER H 122 REMARK 465 LEU H 123 REMARK 465 GLU H 124 REMARK 465 HIS H 125 REMARK 465 HIS H 126 REMARK 465 HIS H 127 REMARK 465 HIS H 128 REMARK 465 HIS H 129 REMARK 465 HIS H 130 REMARK 465 HIS H 131 REMARK 465 HIS H 132 REMARK 465 GLY H 133 REMARK 465 SER H 134 REMARK 465 GLY H 135 REMARK 465 LEU H 136 REMARK 465 VAL H 137 REMARK 465 PRO H 138 REMARK 465 ARG H 139 REMARK 465 GLY H 140 REMARK 465 SER H 141 REMARK 465 GLY H 142 REMARK 465 LEU H 143 REMARK 465 ASN H 144 REMARK 465 ASP H 145 REMARK 465 ILE H 146 REMARK 465 PHE H 147 REMARK 465 GLU H 148 REMARK 465 ALA H 149 REMARK 465 GLN H 150 REMARK 465 LYS H 151 REMARK 465 ILE H 152 REMARK 465 GLU H 153 REMARK 465 TRP H 154 REMARK 465 HIS H 155 REMARK 465 GLU H 156 REMARK 465 MET G 1 REMARK 465 GLY G 2 REMARK 465 LEU G 121 REMARK 465 GLU G 122 REMARK 465 HIS G 123 REMARK 465 HIS G 124 REMARK 465 HIS G 125 REMARK 465 HIS G 126 REMARK 465 HIS G 127 REMARK 465 HIS G 128 REMARK 465 HIS G 129 REMARK 465 HIS G 130 REMARK 465 GLY G 131 REMARK 465 SER G 132 REMARK 465 GLY G 133 REMARK 465 LEU G 134 REMARK 465 VAL G 135 REMARK 465 PRO G 136 REMARK 465 ARG G 137 REMARK 465 GLY G 138 REMARK 465 SER G 139 REMARK 465 GLY G 140 REMARK 465 LEU G 141 REMARK 465 ASN G 142 REMARK 465 ASP G 143 REMARK 465 ILE G 144 REMARK 465 PHE G 145 REMARK 465 GLU G 146 REMARK 465 ALA G 147 REMARK 465 GLN G 148 REMARK 465 LYS G 149 REMARK 465 ILE G 150 REMARK 465 GLU G 151 REMARK 465 TRP G 152 REMARK 465 HIS G 153 REMARK 465 GLU G 154 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OH TYR A 224 OD2 ASP B 157 2.04 REMARK 500 OH TYR E 250 OD2 ASP H 35 2.07 REMARK 500 NH2 ARG B 194 O LEU B 256 2.07 REMARK 500 OE2 GLU A 54 NE2 HIS A 129 2.09 REMARK 500 OD2 ASP A 120 O HOH A 501 2.09 REMARK 500 NZ LYS E 252 O HOH E 501 2.16 REMARK 500 NH2 ARG F 259 OE2 GLU G 66 2.18 REMARK 500 OH TYR A 250 OD2 ASP D 35 2.18 REMARK 500 OE2 GLU E 54 NE2 HIS E 129 2.19 REMARK 500 O LEU A 115 OG1 THR A 119 2.19 REMARK 500 O TYR A 259 NE2 GLN A 284 2.19 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 ALA A 17 -85.93 -113.91 REMARK 500 TYR A 30 103.07 62.74 REMARK 500 ALA A 36 78.51 -105.25 REMARK 500 ASN A 105 -114.45 37.55 REMARK 500 LYS A 133 -153.61 -123.53 REMARK 500 THR A 152 31.14 -99.22 REMARK 500 HIS A 154 76.05 -119.38 REMARK 500 ASN A 160 71.49 -158.07 REMARK 500 ASN A 161 29.86 -142.94 REMARK 500 GLU A 166 40.92 -86.74 REMARK 500 TYR A 224 78.81 -109.93 REMARK 500 CYS A 245 45.25 -79.79 REMARK 500 LYS A 252 65.70 -157.12 REMARK 500 SER A 253 -116.02 52.84 REMARK 500 ASN A 254 44.24 -92.72 REMARK 500 SER A 255 32.02 -145.64 REMARK 500 ASP A 257 45.03 -80.35 REMARK 500 TYR A 259 70.58 -117.30 REMARK 500 ARG A 290 73.79 -119.71 REMARK 500 TYR B 60 79.49 -118.35 REMARK 500 MET B 221 41.57 -107.43 REMARK 500 ASP D 34 -72.79 -79.22 REMARK 500 ALA C 105 -59.87 59.35 REMARK 500 ASN E 8 -68.17 -137.18 REMARK 500 ALA E 17 -79.72 -104.49 REMARK 500 ASN E 29 -106.53 44.51 REMARK 500 ASN E 105 -118.34 37.20 REMARK 500 LYS E 133 -145.03 -118.47 REMARK 500 HIS E 154 74.68 -118.25 REMARK 500 ASN E 160 66.64 -152.90 REMARK 500 LYS E 252 55.08 -153.32 REMARK 500 SER E 253 -94.19 53.16 REMARK 500 ASP E 257 33.16 -84.84 REMARK 500 TRP E 279 35.91 -90.49 REMARK 500 ARG E 290 72.97 -119.08 REMARK 500 ALA F 82 74.54 -102.02 REMARK 500 ALA G 105 -64.53 64.61 REMARK 500 REMARK 500 REMARK: NULL DBREF 9HPA A 3 295 UNP P16710 PG143_VACCW 3 295 DBREF 9HPA B 3 271 UNP P07611 PG094_VACCW 3 271 DBREF 9HPA D 1 156 PDB 9HPA 9HPA 1 156 DBREF 9HPA C 1 154 PDB 9HPA 9HPA 1 154 DBREF 9HPA E 3 295 UNP P16710 PG143_VACCW 3 295 DBREF 9HPA F 3 271 UNP P07611 PG094_VACCW 3 271 DBREF 9HPA H 1 156 PDB 9HPA 9HPA 1 156 DBREF 9HPA G 1 154 PDB 9HPA 9HPA 1 154 SEQADV 9HPA MET A -18 UNP P16710 INITIATING METHIONINE SEQADV 9HPA LYS A -17 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU A -16 UNP P16710 EXPRESSION TAG SEQADV 9HPA CYS A -15 UNP P16710 EXPRESSION TAG SEQADV 9HPA ILE A -14 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU A -13 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU A -12 UNP P16710 EXPRESSION TAG SEQADV 9HPA ALA A -11 UNP P16710 EXPRESSION TAG SEQADV 9HPA VAL A -10 UNP P16710 EXPRESSION TAG SEQADV 9HPA VAL A -9 UNP P16710 EXPRESSION TAG SEQADV 9HPA ALA A -8 UNP P16710 EXPRESSION TAG SEQADV 9HPA PHE A -7 UNP P16710 EXPRESSION TAG SEQADV 9HPA VAL A -6 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A -5 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU A -4 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER A -3 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU A -2 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A -1 UNP P16710 EXPRESSION TAG SEQADV 9HPA ARG A 0 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER A 1 UNP P16710 EXPRESSION TAG SEQADV 9HPA ALA A 2 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 296 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER A 297 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 298 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU A 299 UNP P16710 EXPRESSION TAG SEQADV 9HPA VAL A 300 UNP P16710 EXPRESSION TAG SEQADV 9HPA PRO A 301 UNP P16710 EXPRESSION TAG SEQADV 9HPA ARG A 302 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 303 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER A 304 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 305 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 306 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER A 307 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 308 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 309 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER A 310 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS A 311 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS A 312 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS A 313 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS A 314 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS A 315 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS A 316 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS A 317 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS A 318 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 319 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 320 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER A 321 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 322 UNP P16710 EXPRESSION TAG SEQADV 9HPA THR A 323 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 324 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY A 325 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU A 326 UNP P16710 EXPRESSION TAG SEQADV 9HPA ASN A 327 UNP P16710 EXPRESSION TAG SEQADV 9HPA ASP A 328 UNP P16710 EXPRESSION TAG SEQADV 9HPA ILE A 329 UNP P16710 EXPRESSION TAG SEQADV 9HPA PHE A 330 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLU A 331 UNP P16710 EXPRESSION TAG SEQADV 9HPA ALA A 332 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLN A 333 UNP P16710 EXPRESSION TAG SEQADV 9HPA LYS A 334 UNP P16710 EXPRESSION TAG SEQADV 9HPA ILE A 335 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLU A 336 UNP P16710 EXPRESSION TAG SEQADV 9HPA TRP A 337 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS A 338 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLU A 339 UNP P16710 EXPRESSION TAG SEQADV 9HPA MET B -16 UNP P07611 INITIATING METHIONINE SEQADV 9HPA LYS B -15 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU B -14 UNP P07611 EXPRESSION TAG SEQADV 9HPA CYS B -13 UNP P07611 EXPRESSION TAG SEQADV 9HPA ILE B -12 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU B -11 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU B -10 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA B -9 UNP P07611 EXPRESSION TAG SEQADV 9HPA VAL B -8 UNP P07611 EXPRESSION TAG SEQADV 9HPA VAL B -7 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA B -6 UNP P07611 EXPRESSION TAG SEQADV 9HPA PHE B -5 UNP P07611 EXPRESSION TAG SEQADV 9HPA VAL B -4 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B -3 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU B -2 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER B -1 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU B 0 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 1 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA B 2 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA B 82 UNP P07611 ASN 82 CONFLICT SEQADV 9HPA GLN B 93 UNP P07611 ASN 93 CONFLICT SEQADV 9HPA ALA B 156 UNP P07611 SER 156 CONFLICT SEQADV 9HPA ASP B 157 UNP P07611 ASN 157 CONFLICT SEQADV 9HPA GLY B 272 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER B 273 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 274 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU B 275 UNP P07611 EXPRESSION TAG SEQADV 9HPA VAL B 276 UNP P07611 EXPRESSION TAG SEQADV 9HPA PRO B 277 UNP P07611 EXPRESSION TAG SEQADV 9HPA ARG B 278 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 279 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER B 280 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU B 281 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLU B 282 UNP P07611 EXPRESSION TAG SEQADV 9HPA ASP B 283 UNP P07611 EXPRESSION TAG SEQADV 9HPA ASP B 284 UNP P07611 EXPRESSION TAG SEQADV 9HPA ASP B 285 UNP P07611 EXPRESSION TAG SEQADV 9HPA ASP B 286 UNP P07611 EXPRESSION TAG SEQADV 9HPA LYS B 287 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA B 288 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 289 UNP P07611 EXPRESSION TAG SEQADV 9HPA TRP B 290 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER B 291 UNP P07611 EXPRESSION TAG SEQADV 9HPA HIS B 292 UNP P07611 EXPRESSION TAG SEQADV 9HPA PRO B 293 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLN B 294 UNP P07611 EXPRESSION TAG SEQADV 9HPA PHE B 295 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLU B 296 UNP P07611 EXPRESSION TAG SEQADV 9HPA LYS B 297 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 298 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 299 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 300 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER B 301 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 302 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 303 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 304 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER B 305 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 306 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 307 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY B 308 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER B 309 UNP P07611 EXPRESSION TAG SEQADV 9HPA TRP B 310 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER B 311 UNP P07611 EXPRESSION TAG SEQADV 9HPA HIS B 312 UNP P07611 EXPRESSION TAG SEQADV 9HPA PRO B 313 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLN B 314 UNP P07611 EXPRESSION TAG SEQADV 9HPA PHE B 315 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLU B 316 UNP P07611 EXPRESSION TAG SEQADV 9HPA LYS B 317 UNP P07611 EXPRESSION TAG SEQADV 9HPA MET E -18 UNP P16710 INITIATING METHIONINE SEQADV 9HPA LYS E -17 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU E -16 UNP P16710 EXPRESSION TAG SEQADV 9HPA CYS E -15 UNP P16710 EXPRESSION TAG SEQADV 9HPA ILE E -14 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU E -13 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU E -12 UNP P16710 EXPRESSION TAG SEQADV 9HPA ALA E -11 UNP P16710 EXPRESSION TAG SEQADV 9HPA VAL E -10 UNP P16710 EXPRESSION TAG SEQADV 9HPA VAL E -9 UNP P16710 EXPRESSION TAG SEQADV 9HPA ALA E -8 UNP P16710 EXPRESSION TAG SEQADV 9HPA PHE E -7 UNP P16710 EXPRESSION TAG SEQADV 9HPA VAL E -6 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E -5 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU E -4 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER E -3 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU E -2 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E -1 UNP P16710 EXPRESSION TAG SEQADV 9HPA ARG E 0 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER E 1 UNP P16710 EXPRESSION TAG SEQADV 9HPA ALA E 2 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 296 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER E 297 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 298 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU E 299 UNP P16710 EXPRESSION TAG SEQADV 9HPA VAL E 300 UNP P16710 EXPRESSION TAG SEQADV 9HPA PRO E 301 UNP P16710 EXPRESSION TAG SEQADV 9HPA ARG E 302 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 303 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER E 304 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 305 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 306 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER E 307 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 308 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 309 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER E 310 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS E 311 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS E 312 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS E 313 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS E 314 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS E 315 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS E 316 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS E 317 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS E 318 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 319 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 320 UNP P16710 EXPRESSION TAG SEQADV 9HPA SER E 321 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 322 UNP P16710 EXPRESSION TAG SEQADV 9HPA THR E 323 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 324 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLY E 325 UNP P16710 EXPRESSION TAG SEQADV 9HPA LEU E 326 UNP P16710 EXPRESSION TAG SEQADV 9HPA ASN E 327 UNP P16710 EXPRESSION TAG SEQADV 9HPA ASP E 328 UNP P16710 EXPRESSION TAG SEQADV 9HPA ILE E 329 UNP P16710 EXPRESSION TAG SEQADV 9HPA PHE E 330 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLU E 331 UNP P16710 EXPRESSION TAG SEQADV 9HPA ALA E 332 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLN E 333 UNP P16710 EXPRESSION TAG SEQADV 9HPA LYS E 334 UNP P16710 EXPRESSION TAG SEQADV 9HPA ILE E 335 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLU E 336 UNP P16710 EXPRESSION TAG SEQADV 9HPA TRP E 337 UNP P16710 EXPRESSION TAG SEQADV 9HPA HIS E 338 UNP P16710 EXPRESSION TAG SEQADV 9HPA GLU E 339 UNP P16710 EXPRESSION TAG SEQADV 9HPA MET F -16 UNP P07611 INITIATING METHIONINE SEQADV 9HPA LYS F -15 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU F -14 UNP P07611 EXPRESSION TAG SEQADV 9HPA CYS F -13 UNP P07611 EXPRESSION TAG SEQADV 9HPA ILE F -12 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU F -11 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU F -10 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA F -9 UNP P07611 EXPRESSION TAG SEQADV 9HPA VAL F -8 UNP P07611 EXPRESSION TAG SEQADV 9HPA VAL F -7 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA F -6 UNP P07611 EXPRESSION TAG SEQADV 9HPA PHE F -5 UNP P07611 EXPRESSION TAG SEQADV 9HPA VAL F -4 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F -3 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU F -2 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER F -1 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU F 0 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 1 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA F 2 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA F 82 UNP P07611 ASN 82 CONFLICT SEQADV 9HPA GLN F 93 UNP P07611 ASN 93 CONFLICT SEQADV 9HPA ALA F 156 UNP P07611 SER 156 CONFLICT SEQADV 9HPA ASP F 157 UNP P07611 ASN 157 CONFLICT SEQADV 9HPA GLY F 272 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER F 273 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 274 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU F 275 UNP P07611 EXPRESSION TAG SEQADV 9HPA VAL F 276 UNP P07611 EXPRESSION TAG SEQADV 9HPA PRO F 277 UNP P07611 EXPRESSION TAG SEQADV 9HPA ARG F 278 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 279 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER F 280 UNP P07611 EXPRESSION TAG SEQADV 9HPA LEU F 281 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLU F 282 UNP P07611 EXPRESSION TAG SEQADV 9HPA ASP F 283 UNP P07611 EXPRESSION TAG SEQADV 9HPA ASP F 284 UNP P07611 EXPRESSION TAG SEQADV 9HPA ASP F 285 UNP P07611 EXPRESSION TAG SEQADV 9HPA ASP F 286 UNP P07611 EXPRESSION TAG SEQADV 9HPA LYS F 287 UNP P07611 EXPRESSION TAG SEQADV 9HPA ALA F 288 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 289 UNP P07611 EXPRESSION TAG SEQADV 9HPA TRP F 290 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER F 291 UNP P07611 EXPRESSION TAG SEQADV 9HPA HIS F 292 UNP P07611 EXPRESSION TAG SEQADV 9HPA PRO F 293 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLN F 294 UNP P07611 EXPRESSION TAG SEQADV 9HPA PHE F 295 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLU F 296 UNP P07611 EXPRESSION TAG SEQADV 9HPA LYS F 297 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 298 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 299 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 300 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER F 301 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 302 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 303 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 304 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER F 305 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 306 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 307 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLY F 308 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER F 309 UNP P07611 EXPRESSION TAG SEQADV 9HPA TRP F 310 UNP P07611 EXPRESSION TAG SEQADV 9HPA SER F 311 UNP P07611 EXPRESSION TAG SEQADV 9HPA HIS F 312 UNP P07611 EXPRESSION TAG SEQADV 9HPA PRO F 313 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLN F 314 UNP P07611 EXPRESSION TAG SEQADV 9HPA PHE F 315 UNP P07611 EXPRESSION TAG SEQADV 9HPA GLU F 316 UNP P07611 EXPRESSION TAG SEQADV 9HPA LYS F 317 UNP P07611 EXPRESSION TAG SEQRES 1 A 358 MET LYS LEU CYS ILE LEU LEU ALA VAL VAL ALA PHE VAL SEQRES 2 A 358 GLY LEU SER LEU GLY ARG SER ALA ALA ALA VAL THR LEU SEQRES 3 A 358 ASN ARG ILE LYS ILE ALA PRO GLY ILE ALA ASP ILE ARG SEQRES 4 A 358 ASP LYS TYR MET GLU LEU GLY PHE ASN TYR PRO GLU TYR SEQRES 5 A 358 ASN ARG ALA VAL LYS PHE ALA GLU GLU SER TYR THR TYR SEQRES 6 A 358 TYR TYR GLU THR SER PRO GLY GLU ILE LYS PRO LYS PHE SEQRES 7 A 358 CYS LEU ILE ASP GLY MET SER ILE ASP HIS CYS SER SER SEQRES 8 A 358 PHE ILE VAL PRO GLU PHE ALA LYS GLN TYR VAL LEU ILE SEQRES 9 A 358 HIS GLY GLU PRO CYS SER SER PHE LYS PHE ARG PRO GLY SEQRES 10 A 358 SER LEU ILE TYR TYR GLN ASN GLU VAL THR PRO GLU TYR SEQRES 11 A 358 ILE LYS ASP LEU LYS HIS ALA THR ASP TYR ILE ALA SER SEQRES 12 A 358 GLY GLN ARG CYS HIS PHE ILE LYS LYS ASP TYR LEU LEU SEQRES 13 A 358 GLY ASP SER ASP SER VAL ALA LYS CYS CYS SER LYS THR SEQRES 14 A 358 ASN THR LYS HIS CYS PRO LYS ILE PHE ASN ASN ASN TYR SEQRES 15 A 358 LYS THR GLU HIS CYS ASP ASP PHE MET THR GLY PHE CYS SEQRES 16 A 358 ARG ASN ASP PRO GLY ASN PRO ASN CYS LEU GLU TRP LEU SEQRES 17 A 358 ARG ALA LYS ARG LYS PRO ALA MET SER THR TYR SER ASP SEQRES 18 A 358 ILE CYS SER LYS HIS MET ASP ALA ARG TYR CYS SER GLU SEQRES 19 A 358 PHE ILE ARG ILE ILE ARG PRO ASP TYR PHE THR PHE GLY SEQRES 20 A 358 ASP THR ALA LEU TYR VAL PHE CYS ASN ASP HIS LYS GLY SEQRES 21 A 358 ASN ARG ASN CYS TRP CYS ALA ASN TYR PRO LYS SER ASN SEQRES 22 A 358 SER GLY ASP LYS TYR LEU GLY PRO ARG VAL CYS TRP LEU SEQRES 23 A 358 HIS GLU CYS THR ASP GLU SER ARG ASP ARG LYS TRP LEU SEQRES 24 A 358 TYR TYR ASN GLN ASP VAL GLN ARG THR ARG CYS LYS TYR SEQRES 25 A 358 VAL GLY GLY SER GLY LEU VAL PRO ARG GLY SER GLY GLY SEQRES 26 A 358 SER GLY GLY SER HIS HIS HIS HIS HIS HIS HIS HIS GLY SEQRES 27 A 358 GLY SER GLY THR GLY GLY LEU ASN ASP ILE PHE GLU ALA SEQRES 28 A 358 GLN LYS ILE GLU TRP HIS GLU SEQRES 1 B 334 MET LYS LEU CYS ILE LEU LEU ALA VAL VAL ALA PHE VAL SEQRES 2 B 334 GLY LEU SER LEU GLY ALA GLY GLY VAL SER VAL GLU LEU SEQRES 3 B 334 PRO LYS ARG ASP PRO PRO PRO GLY VAL PRO THR ASP GLU SEQRES 4 B 334 MET LEU LEU ASN VAL ASP LYS MET HIS ASP VAL ILE ALA SEQRES 5 B 334 PRO ALA LYS LEU LEU GLU TYR VAL HIS ILE GLY PRO LEU SEQRES 6 B 334 ALA LYS ASP LYS GLU ASP LYS VAL LYS LYS ARG TYR PRO SEQRES 7 B 334 GLU PHE ARG LEU VAL ASN THR GLY PRO GLY GLY LEU SER SEQRES 8 B 334 ALA LEU LEU ARG GLN SER TYR ALA GLY THR ALA PRO ASN SEQRES 9 B 334 CYS CYS ARG THR PHE GLN ARG THR HIS TYR TRP LYS LYS SEQRES 10 B 334 ASP GLY LYS ILE SER ASP LYS TYR GLU GLU GLY ALA VAL SEQRES 11 B 334 LEU GLU SER CYS TRP PRO ASP VAL HIS ASP THR GLY LYS SEQRES 12 B 334 CYS ASP VAL ASP LEU PHE ASP TRP CYS GLN GLY ASP THR SEQRES 13 B 334 PHE ASP ARG ASN ILE CYS HIS GLN TRP ILE GLY SER ALA SEQRES 14 B 334 PHE ASN ARG ALA ASP ARG THR VAL GLU GLY GLN GLN SER SEQRES 15 B 334 LEU ILE ASN LEU TYR ASN LYS MET GLN THR LEU CYS SER SEQRES 16 B 334 LYS ASP ALA SER VAL PRO ILE CYS GLU SER PHE LEU HIS SEQRES 17 B 334 HIS LEU ARG ALA HIS ASN THR GLU ASP SER LYS GLU MET SEQRES 18 B 334 ILE ASP TYR ILE LEU ARG GLN GLN SER ALA ASP PHE LYS SEQRES 19 B 334 GLN LYS TYR MET ARG CYS SER TYR PRO THR ARG ASP LYS SEQRES 20 B 334 LEU GLU GLU SER LEU LYS TYR ALA GLU PRO ARG GLU CYS SEQRES 21 B 334 TRP ASP PRO GLU CYS SER ASN ALA ASN VAL ASN PHE LEU SEQRES 22 B 334 LEU THR ARG ASN TYR ASN ASN LEU GLY LEU CYS ASN ILE SEQRES 23 B 334 VAL ARG GLY SER GLY LEU VAL PRO ARG GLY SER LEU GLU SEQRES 24 B 334 ASP ASP ASP ASP LYS ALA GLY TRP SER HIS PRO GLN PHE SEQRES 25 B 334 GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY GLY SEQRES 26 B 334 SER TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 D 156 MET GLY GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 D 156 VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS VAL ALA SEQRES 3 D 156 SER GLY SER ILE PHE MET ILE ASP ASP MET GLY TRP TYR SEQRES 4 D 156 ARG ARG ALA PRO GLY ASN GLU ARG GLU TRP VAL ALA THR SEQRES 5 D 156 THR HIS SER GLY GLY SER THR VAL TYR ALA ASP SER VAL SEQRES 6 D 156 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 D 156 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 D 156 THR ALA VAL TYR TYR CYS ASN ALA GLN GLY LEU THR GLY SEQRES 9 D 156 SER ARG GLN ARG TYR ASP VAL LEU GLY GLN GLY THR GLN SEQRES 10 D 156 VAL THR VAL SER SER LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 11 D 156 HIS HIS GLY SER GLY LEU VAL PRO ARG GLY SER GLY LEU SEQRES 12 D 156 ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU SEQRES 1 C 154 MET GLY GLU VAL GLN LEU GLN ALA SER GLY GLY GLY LEU SEQRES 2 C 154 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 C 154 SER GLY ILE VAL PHE SER ASN ASN ARG MET SER TRP TYR SEQRES 4 C 154 ARG GLN ALA PRO GLY LYS GLN ARG GLU VAL VAL ALA THR SEQRES 5 C 154 ILE THR SER GLY GLY ALA THR ASP TYR GLN ASP SER VAL SEQRES 6 C 154 GLU GLY ARG PHE THR ILE SER ARG ASP MET ALA LYS ASN SEQRES 7 C 154 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 C 154 THR ALA VAL TYR PHE CYS ASN ALA ARG ARG ASP ASN PHE SEQRES 9 C 154 ALA THR ALA ILE TYR TRP GLY GLN GLY THR GLN VAL THR SEQRES 10 C 154 VAL SER SER LEU GLU HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 11 C 154 GLY SER GLY LEU VAL PRO ARG GLY SER GLY LEU ASN ASP SEQRES 12 C 154 ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU SEQRES 1 E 358 MET LYS LEU CYS ILE LEU LEU ALA VAL VAL ALA PHE VAL SEQRES 2 E 358 GLY LEU SER LEU GLY ARG SER ALA ALA ALA VAL THR LEU SEQRES 3 E 358 ASN ARG ILE LYS ILE ALA PRO GLY ILE ALA ASP ILE ARG SEQRES 4 E 358 ASP LYS TYR MET GLU LEU GLY PHE ASN TYR PRO GLU TYR SEQRES 5 E 358 ASN ARG ALA VAL LYS PHE ALA GLU GLU SER TYR THR TYR SEQRES 6 E 358 TYR TYR GLU THR SER PRO GLY GLU ILE LYS PRO LYS PHE SEQRES 7 E 358 CYS LEU ILE ASP GLY MET SER ILE ASP HIS CYS SER SER SEQRES 8 E 358 PHE ILE VAL PRO GLU PHE ALA LYS GLN TYR VAL LEU ILE SEQRES 9 E 358 HIS GLY GLU PRO CYS SER SER PHE LYS PHE ARG PRO GLY SEQRES 10 E 358 SER LEU ILE TYR TYR GLN ASN GLU VAL THR PRO GLU TYR SEQRES 11 E 358 ILE LYS ASP LEU LYS HIS ALA THR ASP TYR ILE ALA SER SEQRES 12 E 358 GLY GLN ARG CYS HIS PHE ILE LYS LYS ASP TYR LEU LEU SEQRES 13 E 358 GLY ASP SER ASP SER VAL ALA LYS CYS CYS SER LYS THR SEQRES 14 E 358 ASN THR LYS HIS CYS PRO LYS ILE PHE ASN ASN ASN TYR SEQRES 15 E 358 LYS THR GLU HIS CYS ASP ASP PHE MET THR GLY PHE CYS SEQRES 16 E 358 ARG ASN ASP PRO GLY ASN PRO ASN CYS LEU GLU TRP LEU SEQRES 17 E 358 ARG ALA LYS ARG LYS PRO ALA MET SER THR TYR SER ASP SEQRES 18 E 358 ILE CYS SER LYS HIS MET ASP ALA ARG TYR CYS SER GLU SEQRES 19 E 358 PHE ILE ARG ILE ILE ARG PRO ASP TYR PHE THR PHE GLY SEQRES 20 E 358 ASP THR ALA LEU TYR VAL PHE CYS ASN ASP HIS LYS GLY SEQRES 21 E 358 ASN ARG ASN CYS TRP CYS ALA ASN TYR PRO LYS SER ASN SEQRES 22 E 358 SER GLY ASP LYS TYR LEU GLY PRO ARG VAL CYS TRP LEU SEQRES 23 E 358 HIS GLU CYS THR ASP GLU SER ARG ASP ARG LYS TRP LEU SEQRES 24 E 358 TYR TYR ASN GLN ASP VAL GLN ARG THR ARG CYS LYS TYR SEQRES 25 E 358 VAL GLY GLY SER GLY LEU VAL PRO ARG GLY SER GLY GLY SEQRES 26 E 358 SER GLY GLY SER HIS HIS HIS HIS HIS HIS HIS HIS GLY SEQRES 27 E 358 GLY SER GLY THR GLY GLY LEU ASN ASP ILE PHE GLU ALA SEQRES 28 E 358 GLN LYS ILE GLU TRP HIS GLU SEQRES 1 F 334 MET LYS LEU CYS ILE LEU LEU ALA VAL VAL ALA PHE VAL SEQRES 2 F 334 GLY LEU SER LEU GLY ALA GLY GLY VAL SER VAL GLU LEU SEQRES 3 F 334 PRO LYS ARG ASP PRO PRO PRO GLY VAL PRO THR ASP GLU SEQRES 4 F 334 MET LEU LEU ASN VAL ASP LYS MET HIS ASP VAL ILE ALA SEQRES 5 F 334 PRO ALA LYS LEU LEU GLU TYR VAL HIS ILE GLY PRO LEU SEQRES 6 F 334 ALA LYS ASP LYS GLU ASP LYS VAL LYS LYS ARG TYR PRO SEQRES 7 F 334 GLU PHE ARG LEU VAL ASN THR GLY PRO GLY GLY LEU SER SEQRES 8 F 334 ALA LEU LEU ARG GLN SER TYR ALA GLY THR ALA PRO ASN SEQRES 9 F 334 CYS CYS ARG THR PHE GLN ARG THR HIS TYR TRP LYS LYS SEQRES 10 F 334 ASP GLY LYS ILE SER ASP LYS TYR GLU GLU GLY ALA VAL SEQRES 11 F 334 LEU GLU SER CYS TRP PRO ASP VAL HIS ASP THR GLY LYS SEQRES 12 F 334 CYS ASP VAL ASP LEU PHE ASP TRP CYS GLN GLY ASP THR SEQRES 13 F 334 PHE ASP ARG ASN ILE CYS HIS GLN TRP ILE GLY SER ALA SEQRES 14 F 334 PHE ASN ARG ALA ASP ARG THR VAL GLU GLY GLN GLN SER SEQRES 15 F 334 LEU ILE ASN LEU TYR ASN LYS MET GLN THR LEU CYS SER SEQRES 16 F 334 LYS ASP ALA SER VAL PRO ILE CYS GLU SER PHE LEU HIS SEQRES 17 F 334 HIS LEU ARG ALA HIS ASN THR GLU ASP SER LYS GLU MET SEQRES 18 F 334 ILE ASP TYR ILE LEU ARG GLN GLN SER ALA ASP PHE LYS SEQRES 19 F 334 GLN LYS TYR MET ARG CYS SER TYR PRO THR ARG ASP LYS SEQRES 20 F 334 LEU GLU GLU SER LEU LYS TYR ALA GLU PRO ARG GLU CYS SEQRES 21 F 334 TRP ASP PRO GLU CYS SER ASN ALA ASN VAL ASN PHE LEU SEQRES 22 F 334 LEU THR ARG ASN TYR ASN ASN LEU GLY LEU CYS ASN ILE SEQRES 23 F 334 VAL ARG GLY SER GLY LEU VAL PRO ARG GLY SER LEU GLU SEQRES 24 F 334 ASP ASP ASP ASP LYS ALA GLY TRP SER HIS PRO GLN PHE SEQRES 25 F 334 GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY GLY SEQRES 26 F 334 SER TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 H 156 MET GLY GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 H 156 VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS VAL ALA SEQRES 3 H 156 SER GLY SER ILE PHE MET ILE ASP ASP MET GLY TRP TYR SEQRES 4 H 156 ARG ARG ALA PRO GLY ASN GLU ARG GLU TRP VAL ALA THR SEQRES 5 H 156 THR HIS SER GLY GLY SER THR VAL TYR ALA ASP SER VAL SEQRES 6 H 156 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 H 156 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 H 156 THR ALA VAL TYR TYR CYS ASN ALA GLN GLY LEU THR GLY SEQRES 9 H 156 SER ARG GLN ARG TYR ASP VAL LEU GLY GLN GLY THR GLN SEQRES 10 H 156 VAL THR VAL SER SER LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 11 H 156 HIS HIS GLY SER GLY LEU VAL PRO ARG GLY SER GLY LEU SEQRES 12 H 156 ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU SEQRES 1 G 154 MET GLY GLU VAL GLN LEU GLN ALA SER GLY GLY GLY LEU SEQRES 2 G 154 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 G 154 SER GLY ILE VAL PHE SER ASN ASN ARG MET SER TRP TYR SEQRES 4 G 154 ARG GLN ALA PRO GLY LYS GLN ARG GLU VAL VAL ALA THR SEQRES 5 G 154 ILE THR SER GLY GLY ALA THR ASP TYR GLN ASP SER VAL SEQRES 6 G 154 GLU GLY ARG PHE THR ILE SER ARG ASP MET ALA LYS ASN SEQRES 7 G 154 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 G 154 THR ALA VAL TYR PHE CYS ASN ALA ARG ARG ASP ASN PHE SEQRES 9 G 154 ALA THR ALA ILE TYR TRP GLY GLN GLY THR GLN VAL THR SEQRES 10 G 154 VAL SER SER LEU GLU HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 11 G 154 GLY SER GLY LEU VAL PRO ARG GLY SER GLY LEU ASN ASP SEQRES 12 G 154 ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU HET PO4 A 401 5 HET SO4 A 402 5 HET PEG B 401 7 HET SO4 B 402 5 HET SO4 B 403 5 HET PEG C 201 7 HET PEG E 401 7 HET PEG F 401 7 HET PO4 F 402 5 HET SO4 F 403 5 HET PEG G 201 7 HETNAM PO4 PHOSPHATE ION HETNAM SO4 SULFATE ION HETNAM PEG DI(HYDROXYETHYL)ETHER FORMUL 9 PO4 2(O4 P 3-) FORMUL 10 SO4 4(O4 S 2-) FORMUL 11 PEG 5(C4 H10 O3) FORMUL 20 HOH *99(H2 O) HELIX 1 AA1 TYR A 30 ASN A 34 5 5 HELIX 2 AA2 SER A 66 SER A 71 5 6 HELIX 3 AA3 VAL A 75 LYS A 80 1 6 HELIX 4 AA4 THR A 108 ASP A 120 1 13 HELIX 5 AA5 ASP A 139 SER A 148 1 10 HELIX 6 AA6 PRO A 156 ASN A 160 5 5 HELIX 7 AA7 CYS A 168 ASP A 179 1 12 HELIX 8 AA8 ASN A 182 ARG A 190 1 9 HELIX 9 AA9 ARG A 193 SER A 205 1 13 HELIX 10 AB1 ALA A 210 ARG A 221 1 12 HELIX 11 AB2 PHE A 225 HIS A 239 1 15 HELIX 12 AB3 LEU A 260 ASP A 272 5 13 HELIX 13 AB4 ASP A 276 LEU A 280 5 5 HELIX 14 AB5 TYR A 281 VAL A 286 1 6 HELIX 15 AB6 GLN A 287 ARG A 290 5 4 HELIX 16 AB7 ASP B 21 LEU B 25 5 5 HELIX 17 AB8 ASN B 26 MET B 30 5 5 HELIX 18 AB9 LYS B 52 TYR B 60 1 9 HELIX 19 AC1 THR B 84 CYS B 89 1 6 HELIX 20 AC2 ASP B 120 GLY B 125 5 6 HELIX 21 AC3 CYS B 127 GLN B 136 1 10 HELIX 22 AC4 ASP B 141 ASN B 154 1 14 HELIX 23 AC5 THR B 159 SER B 178 1 20 HELIX 24 AC6 VAL B 183 ASN B 197 1 15 HELIX 25 AC7 THR B 198 GLN B 211 1 14 HELIX 26 AC8 SER B 213 MET B 221 1 9 HELIX 27 AC9 THR B 227 LEU B 235 1 9 HELIX 28 AD1 PRO B 240 ASP B 245 1 6 HELIX 29 AD2 ASP B 245 ASN B 250 1 6 HELIX 30 AD3 ASN B 252 LEU B 256 5 5 HELIX 31 AD4 LEU B 257 LEU B 264 1 8 HELIX 32 AD5 LYS D 88 THR D 92 5 5 HELIX 33 AD6 VAL C 30 SER C 32 5 3 HELIX 34 AD7 LYS C 88 THR C 92 5 5 HELIX 35 AD8 SER E 66 SER E 72 5 7 HELIX 36 AD9 GLU E 77 LYS E 80 5 4 HELIX 37 AE1 THR E 108 THR E 119 1 12 HELIX 38 AE2 ASP E 139 SER E 148 1 10 HELIX 39 AE3 PRO E 156 ASN E 160 5 5 HELIX 40 AE4 CYS E 168 ASP E 179 1 12 HELIX 41 AE5 ASN E 182 ALA E 191 1 10 HELIX 42 AE6 ARG E 193 HIS E 207 1 15 HELIX 43 AE7 ALA E 210 ARG E 221 1 12 HELIX 44 AE8 PHE E 225 HIS E 239 1 15 HELIX 45 AE9 ASN E 242 TRP E 246 5 5 HELIX 46 AF1 SER E 255 ASP E 272 5 18 HELIX 47 AF2 ASP E 276 LEU E 280 5 5 HELIX 48 AF3 TYR E 281 VAL E 286 1 6 HELIX 49 AF4 GLN E 287 ARG E 290 5 4 HELIX 50 AF5 ASP F 21 LEU F 25 5 5 HELIX 51 AF6 ASN F 26 MET F 30 5 5 HELIX 52 AF7 LYS F 52 TYR F 60 1 9 HELIX 53 AF8 THR F 84 CYS F 89 1 6 HELIX 54 AF9 VAL F 121 GLY F 125 5 5 HELIX 55 AG1 CYS F 127 CYS F 135 1 9 HELIX 56 AG2 ASP F 141 ASN F 154 1 14 HELIX 57 AG3 THR F 159 SER F 178 1 20 HELIX 58 AG4 VAL F 183 ASN F 197 1 15 HELIX 59 AG5 THR F 198 GLN F 211 1 14 HELIX 60 AG6 SER F 213 MET F 221 1 9 HELIX 61 AG7 THR F 227 LEU F 235 1 9 HELIX 62 AG8 PRO F 240 ASP F 245 1 6 HELIX 63 AG9 ASP F 245 ASN F 250 1 6 HELIX 64 AH1 ASN F 252 LEU F 256 5 5 HELIX 65 AH2 LEU F 257 LEU F 264 1 8 HELIX 66 AH3 ASP H 63 LYS H 66 5 4 HELIX 67 AH4 LYS H 88 THR H 92 5 5 HELIX 68 AH5 VAL G 30 SER G 32 5 3 HELIX 69 AH6 LYS G 88 THR G 92 5 5 SHEET 1 AA1 4 LEU A 7 PRO A 14 0 SHEET 2 AA1 4 ASP A 21 PHE A 28 -1 O GLY A 27 N ARG A 9 SHEET 3 AA1 4 ARG A 35 ALA A 40 -1 O ARG A 35 N LEU A 26 SHEET 4 AA1 4 LEU A 100 TYR A 102 -1 O TYR A 102 N LYS A 38 SHEET 1 AA2 3 GLU A 54 ILE A 55 0 SHEET 2 AA2 3 HIS A 129 LYS A 132 -1 O PHE A 130 N ILE A 55 SHEET 3 AA2 3 TYR A 82 ILE A 85 -1 N ILE A 85 O HIS A 129 SHEET 1 AA3 3 CYS A 60 ILE A 62 0 SHEET 2 AA3 3 ILE A 122 ARG A 127 -1 O GLN A 126 N LEU A 61 SHEET 3 AA3 3 PRO A 89 PHE A 93 -1 N CYS A 90 O GLY A 125 SHEET 1 AA4 2 LYS A 292 TYR A 293 0 SHEET 2 AA4 2 ASN B 268 ILE B 269 1 O ILE B 269 N LYS A 292 SHEET 1 AA5 3 TYR B 42 PRO B 47 0 SHEET 2 AA5 3 LEU B 73 ARG B 78 -1 O SER B 74 N GLY B 46 SHEET 3 AA5 3 PHE B 63 ASN B 67 -1 N ARG B 64 O LEU B 77 SHEET 1 AA6 3 ILE B 104 SER B 105 0 SHEET 2 AA6 3 HIS B 96 LYS B 99 -1 N TRP B 98 O SER B 105 SHEET 3 AA6 3 VAL B 113 SER B 116 -1 O GLU B 115 N TYR B 97 SHEET 1 AA7 4 VAL D 4 SER D 9 0 SHEET 2 AA7 4 SER D 19 GLY D 28 -1 O SER D 23 N SER D 9 SHEET 3 AA7 4 THR D 79 ASN D 85 -1 O LEU D 82 N LEU D 22 SHEET 4 AA7 4 PHE D 69 ASP D 74 -1 N THR D 70 O GLN D 83 SHEET 1 AA8 5 THR D 59 TYR D 61 0 SHEET 2 AA8 5 ARG D 47 THR D 53 -1 N THR D 52 O VAL D 60 SHEET 3 AA8 5 ILE D 30 ARG D 41 -1 N TRP D 38 O VAL D 50 SHEET 4 AA8 5 ALA D 93 THR D 103 -1 O VAL D 94 N ARG D 41 SHEET 5 AA8 5 ARG D 108 LEU D 112 -1 O TYR D 109 N GLY D 101 SHEET 1 AA9 5 THR D 59 TYR D 61 0 SHEET 2 AA9 5 ARG D 47 THR D 53 -1 N THR D 52 O VAL D 60 SHEET 3 AA9 5 ILE D 30 ARG D 41 -1 N TRP D 38 O VAL D 50 SHEET 4 AA9 5 ALA D 93 THR D 103 -1 O VAL D 94 N ARG D 41 SHEET 5 AA9 5 GLN D 117 VAL D 118 -1 O VAL D 118 N ALA D 93 SHEET 1 AB1 4 GLN C 5 SER C 9 0 SHEET 2 AB1 4 LEU C 20 SER C 27 -1 O SER C 23 N SER C 9 SHEET 3 AB1 4 THR C 79 MET C 84 -1 O MET C 84 N LEU C 20 SHEET 4 AB1 4 PHE C 69 ASP C 74 -1 N THR C 70 O GLN C 83 SHEET 1 AB2 6 LEU C 13 VAL C 14 0 SHEET 2 AB2 6 THR C 114 VAL C 118 1 O THR C 117 N VAL C 14 SHEET 3 AB2 6 ALA C 93 ARG C 101 -1 N TYR C 95 O THR C 114 SHEET 4 AB2 6 ASN C 34 GLN C 41 -1 N GLN C 41 O VAL C 94 SHEET 5 AB2 6 ARG C 47 ILE C 53 -1 O VAL C 50 N TRP C 38 SHEET 6 AB2 6 THR C 59 TYR C 61 -1 O ASP C 60 N THR C 52 SHEET 1 AB3 4 LEU C 13 VAL C 14 0 SHEET 2 AB3 4 THR C 114 VAL C 118 1 O THR C 117 N VAL C 14 SHEET 3 AB3 4 ALA C 93 ARG C 101 -1 N TYR C 95 O THR C 114 SHEET 4 AB3 4 ILE C 108 TRP C 110 -1 O TYR C 109 N ALA C 99 SHEET 1 AB4 4 ARG E 9 PRO E 14 0 SHEET 2 AB4 4 ASP E 21 GLY E 27 -1 O GLY E 27 N ARG E 9 SHEET 3 AB4 4 ARG E 35 ALA E 40 -1 O VAL E 37 N MET E 24 SHEET 4 AB4 4 LEU E 100 ILE E 101 -1 O LEU E 100 N ALA E 40 SHEET 1 AB5 3 GLU E 54 ILE E 55 0 SHEET 2 AB5 3 HIS E 129 LYS E 132 -1 O PHE E 130 N ILE E 55 SHEET 3 AB5 3 TYR E 82 ILE E 85 -1 N ILE E 85 O HIS E 129 SHEET 1 AB6 3 CYS E 60 ILE E 62 0 SHEET 2 AB6 3 ILE E 122 ARG E 127 -1 O GLN E 126 N LEU E 61 SHEET 3 AB6 3 PRO E 89 PHE E 93 -1 N SER E 92 O ALA E 123 SHEET 1 AB7 2 LYS E 292 TYR E 293 0 SHEET 2 AB7 2 ASN F 268 ILE F 269 1 O ILE F 269 N LYS E 292 SHEET 1 AB8 3 TYR F 42 PRO F 47 0 SHEET 2 AB8 3 LEU F 73 ARG F 78 -1 O LEU F 76 N VAL F 43 SHEET 3 AB8 3 PHE F 63 GLY F 69 -1 N VAL F 66 O ALA F 75 SHEET 1 AB9 3 LYS F 103 SER F 105 0 SHEET 2 AB9 3 HIS F 96 LYS F 100 -1 N TRP F 98 O SER F 105 SHEET 3 AB9 3 VAL F 113 SER F 116 -1 O VAL F 113 N LYS F 99 SHEET 1 AC1 4 VAL H 4 SER H 9 0 SHEET 2 AC1 4 LEU H 20 GLY H 28 -1 O SER H 23 N SER H 9 SHEET 3 AC1 4 THR H 79 MET H 84 -1 O LEU H 82 N LEU H 22 SHEET 4 AC1 4 PHE H 69 ASP H 74 -1 N THR H 70 O GLN H 83 SHEET 1 AC2 5 THR H 59 TYR H 61 0 SHEET 2 AC2 5 ARG H 47 HIS H 54 -1 N THR H 52 O VAL H 60 SHEET 3 AC2 5 ILE H 30 ARG H 41 -1 N MET H 36 O THR H 53 SHEET 4 AC2 5 ALA H 93 THR H 103 -1 O LEU H 102 N PHE H 31 SHEET 5 AC2 5 ARG H 108 LEU H 112 -1 O TYR H 109 N GLY H 101 SHEET 1 AC3 5 THR H 59 TYR H 61 0 SHEET 2 AC3 5 ARG H 47 HIS H 54 -1 N THR H 52 O VAL H 60 SHEET 3 AC3 5 ILE H 30 ARG H 41 -1 N MET H 36 O THR H 53 SHEET 4 AC3 5 ALA H 93 THR H 103 -1 O LEU H 102 N PHE H 31 SHEET 5 AC3 5 GLN H 117 VAL H 118 -1 O VAL H 118 N ALA H 93 SHEET 1 AC4 4 GLN G 5 SER G 9 0 SHEET 2 AC4 4 LEU G 20 SER G 27 -1 O SER G 23 N SER G 9 SHEET 3 AC4 4 THR G 79 MET G 84 -1 O LEU G 82 N LEU G 22 SHEET 4 AC4 4 PHE G 69 ASP G 74 -1 N THR G 70 O GLN G 83 SHEET 1 AC5 6 GLY G 12 VAL G 14 0 SHEET 2 AC5 6 THR G 114 VAL G 118 1 O THR G 117 N VAL G 14 SHEET 3 AC5 6 ALA G 93 ARG G 101 -1 N TYR G 95 O THR G 114 SHEET 4 AC5 6 ASN G 34 GLN G 41 -1 N ARG G 35 O ARG G 100 SHEET 5 AC5 6 ARG G 47 ILE G 53 -1 O VAL G 50 N TRP G 38 SHEET 6 AC5 6 THR G 59 TYR G 61 -1 O ASP G 60 N THR G 52 SHEET 1 AC6 4 GLY G 12 VAL G 14 0 SHEET 2 AC6 4 THR G 114 VAL G 118 1 O THR G 117 N VAL G 14 SHEET 3 AC6 4 ALA G 93 ARG G 101 -1 N TYR G 95 O THR G 114 SHEET 4 AC6 4 TYR G 109 TRP G 110 -1 O TYR G 109 N ALA G 99 SSBOND 1 CYS A 60 CYS A 90 1555 1555 2.04 SSBOND 2 CYS A 70 CYS A 128 1555 1555 2.03 SSBOND 3 CYS A 146 CYS A 155 1555 1555 2.03 SSBOND 4 CYS A 147 CYS A 168 1555 1555 2.03 SSBOND 5 CYS A 176 CYS A 185 1555 1555 2.03 SSBOND 6 CYS A 204 CYS A 213 1555 1555 2.03 SSBOND 7 CYS A 236 CYS A 245 1555 1555 2.03 SSBOND 8 CYS A 247 CYS A 270 1555 1555 2.03 SSBOND 9 CYS A 265 CYS A 291 1555 1555 2.03 SSBOND 10 CYS B 88 CYS B 117 1555 1555 2.03 SSBOND 11 CYS B 89 CYS B 127 1555 1555 2.03 SSBOND 12 CYS B 135 CYS B 145 1555 1555 2.03 SSBOND 13 CYS B 177 CYS B 186 1555 1555 2.03 SSBOND 14 CYS B 223 CYS B 248 1555 1555 2.03 SSBOND 15 CYS B 243 CYS B 267 1555 1555 2.03 SSBOND 16 CYS D 24 CYS D 97 1555 1555 2.03 SSBOND 17 CYS C 24 CYS C 97 1555 1555 2.04 SSBOND 18 CYS E 60 CYS E 90 1555 1555 2.03 SSBOND 19 CYS E 70 CYS E 128 1555 1555 2.03 SSBOND 20 CYS E 146 CYS E 155 1555 1555 2.03 SSBOND 21 CYS E 147 CYS E 168 1555 1555 2.03 SSBOND 22 CYS E 176 CYS E 185 1555 1555 2.03 SSBOND 23 CYS E 204 CYS E 213 1555 1555 2.03 SSBOND 24 CYS E 236 CYS E 245 1555 1555 2.03 SSBOND 25 CYS E 247 CYS E 270 1555 1555 2.03 SSBOND 26 CYS E 265 CYS E 291 1555 1555 2.03 SSBOND 27 CYS F 88 CYS F 117 1555 1555 2.03 SSBOND 28 CYS F 89 CYS F 127 1555 1555 2.03 SSBOND 29 CYS F 135 CYS F 145 1555 1555 2.03 SSBOND 30 CYS F 177 CYS F 186 1555 1555 2.03 SSBOND 31 CYS F 223 CYS F 248 1555 1555 2.03 SSBOND 32 CYS F 243 CYS F 267 1555 1555 2.03 SSBOND 33 CYS H 24 CYS H 97 1555 1555 2.03 SSBOND 34 CYS G 24 CYS G 97 1555 1555 2.04 CISPEP 1 ARG A 221 PRO A 222 0 2.23 CISPEP 2 ARG E 221 PRO E 222 0 0.99 CRYST1 78.204 148.041 185.708 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012787 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006755 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005385 0.00000