HEADER PROTEIN BINDING 22-DEC-24 9HUD TITLE ALPHA-1-ANTITRYPSIN IN THE CLEAVED CONFORMATION IN COMPLEX WITH A TITLE 2 CONFORMATIONALLY NONSELECTIVE FAB FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-1-ANTITRYPSIN; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: ALPHA-1 PROTEASE INHIBITOR,ALPHA-1-ANTIPROTEINASE,SERPIN A1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SHORT PEPTIDE FROM AAT; COMPND 8 CHAIN: B, D; COMPND 9 SYNONYM: SPAAT; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: FAB 9C5 HEAVY CHAIN; COMPND 13 CHAIN: H, I; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: FAB 9C5 LIGHT CHAIN; COMPND 16 CHAIN: L, M SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SERPINA1, AAT, PI, PRO0684, PRO2209; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: SERPINA1, AAT, PI, PRO0684, PRO2209; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 17 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PQE30; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 21 ORGANISM_TAXID: 10090; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 24 ORGANISM_TAXID: 10090 KEYWDS COMPLEX, CLEAVED ALPHA-1-ANTITRYPSIN, ALPHA-1-ANTITRYPSIN, KEYWDS 2 ANTITRYPSIN, FAB, FAB FRAGMENT, FRAGMENT ANTIGEN-BINDING REGION, KEYWDS 3 ANTIBODY ANTIGEN COMPLEX, 9C5, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR J.A.IRVING,I.F.ALDOBIYAN REVDAT 1 26-NOV-25 9HUD 0 JRNL AUTH I.ALDOBIYAN,E.L.K.ELLISTON,N.HEYER-CHAUHAN,S.T.AROLD,L.ZHAO, JRNL AUTH 2 B.HUNTINGTON,S.M.LOWEN,E.V.ORLOVA,J.A.IRVING,D.A.LOMAS JRNL TITL THE MECHANISM OF PATHOGENIC ALPHA 1 -ANTITRYPSIN AGGREGATION JRNL TITL 2 IN THE HUMAN LIVER. JRNL REF PROC.NATL.ACAD.SCI.USA V. 122 35122 2025 JRNL REFN ESSN 1091-6490 JRNL PMID 41231946 JRNL DOI 10.1073/PNAS.2507535122 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN, REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY, REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON, REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL, REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS, REMARK 1 AUTH 6 P.D.ADAMS REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS, REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX REMARK 1 REF ACTA CRYSTALLOGR., SECT. D: V. 75 861 2019 REMARK 1 REF 2 BIOL. CRYSTALLOGR. REMARK 1 REFN ISSN 0907-4449 REMARK 1 PMID 31588918 REMARK 1 DOI 10.1107/S2059798319011471 REMARK 2 REMARK 2 RESOLUTION. 2.42 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) : 2.42 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.65 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 74695 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 3827 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 47.6500 - 7.2600 0.98 2797 155 0.1989 0.2167 REMARK 3 2 7.2500 - 5.7600 0.98 2671 148 0.2400 0.2659 REMARK 3 3 5.7600 - 5.0300 0.99 2661 146 0.1933 0.2367 REMARK 3 4 5.0300 - 4.5700 1.00 2688 135 0.1690 0.1880 REMARK 3 5 4.5700 - 4.2400 1.00 2679 123 0.1625 0.1999 REMARK 3 6 4.2400 - 3.9900 1.00 2620 175 0.1811 0.1982 REMARK 3 7 3.9900 - 3.7900 1.00 2653 132 0.1732 0.2110 REMARK 3 8 3.7900 - 3.6300 1.00 2647 127 0.1746 0.2251 REMARK 3 9 3.6300 - 3.4900 1.00 2631 120 0.1748 0.2088 REMARK 3 10 3.4900 - 3.3700 0.99 2594 155 0.1857 0.2104 REMARK 3 11 3.3700 - 3.2600 1.00 2583 161 0.2094 0.2076 REMARK 3 12 3.2600 - 3.1700 0.99 2601 148 0.2066 0.2851 REMARK 3 13 3.1700 - 3.0900 1.00 2609 156 0.2039 0.2476 REMARK 3 14 3.0900 - 3.0100 1.00 2607 131 0.2201 0.2735 REMARK 3 15 3.0100 - 2.9400 1.00 2639 135 0.2211 0.2726 REMARK 3 16 2.9400 - 2.8800 1.00 2597 135 0.2247 0.2684 REMARK 3 17 2.8800 - 2.8200 1.00 2611 161 0.2525 0.3020 REMARK 3 18 2.8200 - 2.7700 1.00 2588 134 0.2600 0.2990 REMARK 3 19 2.7700 - 2.7200 1.00 2575 161 0.2710 0.3258 REMARK 3 20 2.7200 - 2.6700 1.00 2587 143 0.2725 0.3162 REMARK 3 21 2.6700 - 2.6300 1.00 2612 141 0.2774 0.3466 REMARK 3 22 2.6300 - 2.5900 1.00 2607 133 0.2941 0.3331 REMARK 3 23 2.5900 - 2.5500 1.00 2571 129 0.2883 0.3100 REMARK 3 24 2.5500 - 2.5200 1.00 2620 132 0.3112 0.4026 REMARK 3 25 2.5200 - 2.4800 1.00 2608 147 0.3108 0.3375 REMARK 3 26 2.4800 - 2.4500 1.00 2590 133 0.3047 0.3523 REMARK 3 27 2.4500 - 2.4200 1.00 2622 131 0.3258 0.3498 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) : 0.326 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.672 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 35.96 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.41 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 : 0.003 12387 REMARK 3 ANGLE : 0.572 16877 REMARK 3 CHIRALITY : 0.043 1962 REMARK 3 PLANARITY : 0.004 2169 REMARK 3 DIHEDRAL : 13.246 4357 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 37 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 23 THROUGH 43 ) REMARK 3 ORIGIN FOR THE GROUP (A): 144.9566 61.1125 26.0790 REMARK 3 T TENSOR REMARK 3 T11: 0.4622 T22: 0.3091 REMARK 3 T33: 1.0101 T12: 0.0066 REMARK 3 T13: -0.0221 T23: -0.1682 REMARK 3 L TENSOR REMARK 3 L11: 0.1301 L22: 3.3763 REMARK 3 L33: 2.1028 L12: -0.6704 REMARK 3 L13: 0.3639 L23: -1.7304 REMARK 3 S TENSOR REMARK 3 S11: 0.4003 S12: -0.3164 S13: 1.1437 REMARK 3 S21: 0.3468 S22: -0.2152 S23: -0.6192 REMARK 3 S31: -0.2604 S32: 0.2086 S33: -0.1614 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 44 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): 139.7164 63.0546 18.3887 REMARK 3 T TENSOR REMARK 3 T11: 0.4703 T22: -0.5050 REMARK 3 T33: 1.1239 T12: 0.3964 REMARK 3 T13: 0.1495 T23: -0.0652 REMARK 3 L TENSOR REMARK 3 L11: 1.0971 L22: 2.1193 REMARK 3 L33: 0.6828 L12: 0.3388 REMARK 3 L13: 0.3725 L23: -0.9390 REMARK 3 S TENSOR REMARK 3 S11: 0.2773 S12: -0.0614 S13: 0.6847 REMARK 3 S21: 0.2026 S22: -0.1640 S23: 0.3503 REMARK 3 S31: -0.5232 S32: -0.0260 S33: -0.1462 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 146.1878 52.1576 15.7059 REMARK 3 T TENSOR REMARK 3 T11: 0.3898 T22: 0.2441 REMARK 3 T33: 0.7038 T12: 0.0900 REMARK 3 T13: 0.0252 T23: -0.0703 REMARK 3 L TENSOR REMARK 3 L11: 3.6044 L22: 3.3552 REMARK 3 L33: 2.4085 L12: -0.5521 REMARK 3 L13: -1.2424 L23: 0.3080 REMARK 3 S TENSOR REMARK 3 S11: 0.3684 S12: -0.2908 S13: 0.8426 REMARK 3 S21: -0.0068 S22: -0.2665 S23: -0.1546 REMARK 3 S31: -0.2228 S32: -0.0014 S33: -0.0834 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 121 THROUGH 181 ) REMARK 3 ORIGIN FOR THE GROUP (A): 135.8165 57.2375 2.1942 REMARK 3 T TENSOR REMARK 3 T11: 0.7192 T22: 0.7869 REMARK 3 T33: 0.9115 T12: 0.4483 REMARK 3 T13: 0.0381 T23: 0.2375 REMARK 3 L TENSOR REMARK 3 L11: 0.5550 L22: 1.4415 REMARK 3 L33: 0.2264 L12: -0.6614 REMARK 3 L13: 0.0055 L23: 0.3839 REMARK 3 S TENSOR REMARK 3 S11: 0.7013 S12: 1.1153 S13: 1.1634 REMARK 3 S21: -0.8157 S22: -0.4334 S23: 0.0344 REMARK 3 S31: -0.5686 S32: -0.9275 S33: -0.0402 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 182 THROUGH 232 ) REMARK 3 ORIGIN FOR THE GROUP (A): 124.4066 59.0115 33.4798 REMARK 3 T TENSOR REMARK 3 T11: 0.4582 T22: 0.3725 REMARK 3 T33: 0.8193 T12: -0.0048 REMARK 3 T13: 0.0353 T23: -0.1327 REMARK 3 L TENSOR REMARK 3 L11: 2.5447 L22: 2.5866 REMARK 3 L33: 2.4113 L12: -2.3136 REMARK 3 L13: -1.6884 L23: 1.6327 REMARK 3 S TENSOR REMARK 3 S11: -0.3044 S12: -0.1074 S13: -0.2378 REMARK 3 S21: 0.3484 S22: -0.1190 S23: 0.3074 REMARK 3 S31: 0.2422 S32: -0.2648 S33: 0.2462 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 289 ) REMARK 3 ORIGIN FOR THE GROUP (A): 136.2701 57.8553 38.8186 REMARK 3 T TENSOR REMARK 3 T11: 0.6286 T22: 0.5138 REMARK 3 T33: 0.8174 T12: 0.1129 REMARK 3 T13: -0.0349 T23: -0.2262 REMARK 3 L TENSOR REMARK 3 L11: 3.7174 L22: 3.2568 REMARK 3 L33: 3.2582 L12: -2.7111 REMARK 3 L13: -2.1970 L23: 1.4268 REMARK 3 S TENSOR REMARK 3 S11: -0.3545 S12: -0.9248 S13: 0.3253 REMARK 3 S21: 0.6396 S22: 0.4701 S23: -0.4619 REMARK 3 S31: 0.4431 S32: 0.6734 S33: -0.0772 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 290 THROUGH 330 ) REMARK 3 ORIGIN FOR THE GROUP (A): 144.0165 67.1551 10.3251 REMARK 3 T TENSOR REMARK 3 T11: 0.8213 T22: 0.2008 REMARK 3 T33: 1.4581 T12: 0.2535 REMARK 3 T13: 0.3124 T23: 0.1960 REMARK 3 L TENSOR REMARK 3 L11: 1.5920 L22: 0.8711 REMARK 3 L33: 0.5217 L12: -0.7323 REMARK 3 L13: -0.5104 L23: 0.6601 REMARK 3 S TENSOR REMARK 3 S11: 0.6527 S12: 0.4492 S13: 1.2414 REMARK 3 S21: -0.3491 S22: -0.4218 S23: -0.0550 REMARK 3 S31: -0.4906 S32: -0.1885 S33: -0.3657 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 331 THROUGH 354 ) REMARK 3 ORIGIN FOR THE GROUP (A): 129.5402 59.8795 18.9372 REMARK 3 T TENSOR REMARK 3 T11: 0.4242 T22: 0.3059 REMARK 3 T33: 1.1393 T12: 0.1686 REMARK 3 T13: 0.0679 T23: -0.0849 REMARK 3 L TENSOR REMARK 3 L11: 5.0184 L22: 2.8827 REMARK 3 L33: 4.6008 L12: -0.4363 REMARK 3 L13: -3.3848 L23: 0.3649 REMARK 3 S TENSOR REMARK 3 S11: 0.4096 S12: 0.6503 S13: 0.6793 REMARK 3 S21: -0.2987 S22: -0.1605 S23: 0.3465 REMARK 3 S31: -0.2390 S32: -0.5282 S33: -0.0109 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 362 THROUGH 369 ) REMARK 3 ORIGIN FOR THE GROUP (A): 126.9297 63.6592 42.8825 REMARK 3 T TENSOR REMARK 3 T11: 0.7733 T22: 0.5154 REMARK 3 T33: 0.7154 T12: 0.1720 REMARK 3 T13: -0.0111 T23: -0.2126 REMARK 3 L TENSOR REMARK 3 L11: 1.8253 L22: 1.4082 REMARK 3 L33: 2.8828 L12: -0.9529 REMARK 3 L13: 0.0965 L23: 1.5299 REMARK 3 S TENSOR REMARK 3 S11: 0.0553 S12: -0.3891 S13: 0.3642 REMARK 3 S21: 0.6855 S22: 0.3222 S23: -0.2541 REMARK 3 S31: -0.0836 S32: -0.4244 S33: 0.0507 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 370 THROUGH 375 ) REMARK 3 ORIGIN FOR THE GROUP (A): 133.6686 58.8123 31.1921 REMARK 3 T TENSOR REMARK 3 T11: 0.4471 T22: 0.3505 REMARK 3 T33: 0.8192 T12: 0.0735 REMARK 3 T13: 0.0552 T23: -0.2723 REMARK 3 L TENSOR REMARK 3 L11: 2.4495 L22: 1.5772 REMARK 3 L33: 4.1872 L12: -1.1732 REMARK 3 L13: -2.0382 L23: 2.5696 REMARK 3 S TENSOR REMARK 3 S11: 0.0472 S12: 0.1787 S13: 0.0580 REMARK 3 S21: 0.2488 S22: 0.3213 S23: -0.3942 REMARK 3 S31: -0.1161 S32: -0.1935 S33: -0.0273 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 376 THROUGH 388 ) REMARK 3 ORIGIN FOR THE GROUP (A): 137.2720 54.2608 27.0690 REMARK 3 T TENSOR REMARK 3 T11: 0.4286 T22: 0.3613 REMARK 3 T33: 0.8170 T12: -0.0794 REMARK 3 T13: 0.0919 T23: -0.2043 REMARK 3 L TENSOR REMARK 3 L11: 2.4954 L22: 0.7094 REMARK 3 L33: 3.6866 L12: -0.3318 REMARK 3 L13: -0.9885 L23: 1.5925 REMARK 3 S TENSOR REMARK 3 S11: 0.1930 S12: -0.2471 S13: 0.1247 REMARK 3 S21: 0.5894 S22: -0.0510 S23: -0.5790 REMARK 3 S31: 0.0508 S32: -0.1706 S33: -0.0372 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 389 THROUGH 393 ) REMARK 3 ORIGIN FOR THE GROUP (A): 123.2742 70.0869 29.7891 REMARK 3 T TENSOR REMARK 3 T11: 0.6527 T22: 0.6949 REMARK 3 T33: 0.7230 T12: 0.4597 REMARK 3 T13: 0.0886 T23: -0.2877 REMARK 3 L TENSOR REMARK 3 L11: 2.7026 L22: 0.5749 REMARK 3 L33: 2.9281 L12: -0.5504 REMARK 3 L13: -1.4371 L23: 0.2565 REMARK 3 S TENSOR REMARK 3 S11: 0.2140 S12: 0.4264 S13: 0.3688 REMARK 3 S21: -0.2197 S22: -0.2298 S23: 0.0988 REMARK 3 S31: -0.4563 S32: -0.6908 S33: 0.0694 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 23 THROUGH 88 ) REMARK 3 ORIGIN FOR THE GROUP (A): 120.5904 27.3716 -3.4072 REMARK 3 T TENSOR REMARK 3 T11: 0.3026 T22: 0.5940 REMARK 3 T33: 0.3928 T12: -0.0841 REMARK 3 T13: -0.0111 T23: 0.0704 REMARK 3 L TENSOR REMARK 3 L11: 5.0221 L22: 2.2106 REMARK 3 L33: 3.3218 L12: -0.1450 REMARK 3 L13: -1.6338 L23: 0.8734 REMARK 3 S TENSOR REMARK 3 S11: 0.1785 S12: 1.0462 S13: 0.4612 REMARK 3 S21: -0.3824 S22: 0.0035 S23: 0.0661 REMARK 3 S31: -0.4044 S32: -0.1499 S33: -0.0706 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 89 THROUGH 121 ) REMARK 3 ORIGIN FOR THE GROUP (A): 117.6350 13.2432 2.4276 REMARK 3 T TENSOR REMARK 3 T11: 0.2593 T22: 0.4355 REMARK 3 T33: 0.4265 T12: -0.0501 REMARK 3 T13: -0.0043 T23: -0.0703 REMARK 3 L TENSOR REMARK 3 L11: 4.7695 L22: 2.1497 REMARK 3 L33: 2.7970 L12: -0.1021 REMARK 3 L13: -1.1810 L23: 0.5999 REMARK 3 S TENSOR REMARK 3 S11: -0.0417 S12: 0.4953 S13: -0.7604 REMARK 3 S21: -0.0757 S22: -0.1202 S23: -0.1004 REMARK 3 S31: 0.1571 S32: -0.1585 S33: 0.2408 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 122 THROUGH 181 ) REMARK 3 ORIGIN FOR THE GROUP (A): 128.0098 18.0497 14.5667 REMARK 3 T TENSOR REMARK 3 T11: 0.2925 T22: 0.5357 REMARK 3 T33: 0.4082 T12: -0.0863 REMARK 3 T13: -0.0333 T23: 0.0843 REMARK 3 L TENSOR REMARK 3 L11: 4.7986 L22: 1.9895 REMARK 3 L33: 3.4845 L12: 0.3010 REMARK 3 L13: -1.2662 L23: 1.3774 REMARK 3 S TENSOR REMARK 3 S11: 0.0284 S12: -0.6741 S13: -0.4319 REMARK 3 S21: 0.2447 S22: -0.0188 S23: -0.3103 REMARK 3 S31: 0.0799 S32: 0.5256 S33: -0.0307 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 182 THROUGH 259 ) REMARK 3 ORIGIN FOR THE GROUP (A): 132.1296 12.9439 -18.7203 REMARK 3 T TENSOR REMARK 3 T11: 0.5123 T22: 1.2180 REMARK 3 T33: 0.5357 T12: -0.1199 REMARK 3 T13: 0.0749 T23: -0.2845 REMARK 3 L TENSOR REMARK 3 L11: 2.8810 L22: 1.3563 REMARK 3 L33: 2.4398 L12: 0.4477 REMARK 3 L13: -0.8901 L23: 0.2443 REMARK 3 S TENSOR REMARK 3 S11: -0.2979 S12: 1.4289 S13: -0.5162 REMARK 3 S21: -0.4881 S22: 0.0620 S23: -0.1584 REMARK 3 S31: 0.1236 S32: -0.0821 S33: 0.0853 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 260 THROUGH 298 ) REMARK 3 ORIGIN FOR THE GROUP (A): 126.4202 18.3860 -18.9936 REMARK 3 T TENSOR REMARK 3 T11: 0.5138 T22: 1.2627 REMARK 3 T33: 0.5496 T12: -0.1303 REMARK 3 T13: 0.0327 T23: -0.1056 REMARK 3 L TENSOR REMARK 3 L11: 2.1238 L22: 1.1666 REMARK 3 L33: 2.6547 L12: -0.4137 REMARK 3 L13: 0.4509 L23: 0.4760 REMARK 3 S TENSOR REMARK 3 S11: -0.0592 S12: 1.4656 S13: -0.1690 REMARK 3 S21: -0.4632 S22: -0.0311 S23: 0.2194 REMARK 3 S31: 0.0342 S32: -0.3917 S33: 0.1754 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 299 THROUGH 354 ) REMARK 3 ORIGIN FOR THE GROUP (A): 127.8461 26.2678 4.4461 REMARK 3 T TENSOR REMARK 3 T11: 0.2595 T22: 0.4423 REMARK 3 T33: 0.3807 T12: -0.0666 REMARK 3 T13: -0.0012 T23: -0.0047 REMARK 3 L TENSOR REMARK 3 L11: 4.1844 L22: 2.3467 REMARK 3 L33: 1.7087 L12: 0.3064 REMARK 3 L13: -0.8564 L23: 0.7302 REMARK 3 S TENSOR REMARK 3 S11: 0.0040 S12: 0.1736 S13: 0.4825 REMARK 3 S21: -0.0108 S22: -0.0169 S23: -0.3719 REMARK 3 S31: -0.0489 S32: 0.1131 S33: -0.0341 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 362 THROUGH 369 ) REMARK 3 ORIGIN FOR THE GROUP (A): 136.0228 15.6144 -27.5772 REMARK 3 T TENSOR REMARK 3 T11: 0.5494 T22: 1.6125 REMARK 3 T33: 0.5708 T12: -0.2157 REMARK 3 T13: 0.0496 T23: -0.2090 REMARK 3 L TENSOR REMARK 3 L11: 1.8697 L22: 0.7464 REMARK 3 L33: 3.5870 L12: 0.3837 REMARK 3 L13: 2.5468 L23: 0.2133 REMARK 3 S TENSOR REMARK 3 S11: 0.0421 S12: 1.0992 S13: -0.6891 REMARK 3 S21: -0.3839 S22: 0.3695 S23: 0.0190 REMARK 3 S31: 0.4367 S32: 0.0634 S33: 0.1274 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 370 THROUGH 380 ) REMARK 3 ORIGIN FOR THE GROUP (A): 123.3080 14.3084 -12.8357 REMARK 3 T TENSOR REMARK 3 T11: 0.3676 T22: 1.0128 REMARK 3 T33: 0.5086 T12: -0.1777 REMARK 3 T13: 0.0976 T23: -0.1495 REMARK 3 L TENSOR REMARK 3 L11: 2.4885 L22: 1.2337 REMARK 3 L33: 1.6149 L12: 1.0112 REMARK 3 L13: -1.7895 L23: -1.2509 REMARK 3 S TENSOR REMARK 3 S11: -0.2653 S12: 1.1540 S13: -0.1889 REMARK 3 S21: -0.4325 S22: 0.0761 S23: -0.5005 REMARK 3 S31: -0.1998 S32: 0.2692 S33: 0.0587 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 381 THROUGH 394 ) REMARK 3 ORIGIN FOR THE GROUP (A): 134.6796 19.2451 -12.2050 REMARK 3 T TENSOR REMARK 3 T11: 0.3804 T22: 1.0315 REMARK 3 T33: 0.4100 T12: -0.0992 REMARK 3 T13: 0.0952 T23: -0.0998 REMARK 3 L TENSOR REMARK 3 L11: 2.1778 L22: 0.7846 REMARK 3 L33: 1.6577 L12: 0.1987 REMARK 3 L13: -1.7869 L23: -0.5495 REMARK 3 S TENSOR REMARK 3 S11: -0.2604 S12: 1.1191 S13: -0.2792 REMARK 3 S21: -0.0588 S22: 0.2155 S23: -0.1943 REMARK 3 S31: -0.1582 S32: 0.3998 S33: 0.0780 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 157.0285 22.7768 -2.0241 REMARK 3 T TENSOR REMARK 3 T11: 0.1511 T22: 0.3451 REMARK 3 T33: 0.2071 T12: 0.0285 REMARK 3 T13: 0.0035 T23: 0.0128 REMARK 3 L TENSOR REMARK 3 L11: 2.7277 L22: 6.0604 REMARK 3 L33: 3.0608 L12: -1.0158 REMARK 3 L13: -0.5104 L23: 3.3195 REMARK 3 S TENSOR REMARK 3 S11: 0.0540 S12: 0.4168 S13: 0.2360 REMARK 3 S21: 0.3222 S22: -0.1727 S23: 0.2147 REMARK 3 S31: 0.4973 S32: -0.1328 S33: 0.1444 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): 151.4430 33.0083 -2.5280 REMARK 3 T TENSOR REMARK 3 T11: 0.2589 T22: 0.3810 REMARK 3 T33: 0.3778 T12: 0.1009 REMARK 3 T13: -0.0203 T23: -0.0012 REMARK 3 L TENSOR REMARK 3 L11: 3.0115 L22: 4.7711 REMARK 3 L33: 2.4175 L12: -1.2569 REMARK 3 L13: -0.5718 L23: 2.1209 REMARK 3 S TENSOR REMARK 3 S11: 0.1547 S12: 0.6205 S13: 0.1347 REMARK 3 S21: -0.4046 S22: -0.3840 S23: 0.3596 REMARK 3 S31: -0.3258 S32: -0.5188 S33: 0.1686 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 82A THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): 162.8235 25.0881 -5.1739 REMARK 3 T TENSOR REMARK 3 T11: 0.2704 T22: 0.3056 REMARK 3 T33: 0.1838 T12: 0.0198 REMARK 3 T13: 0.0373 T23: 0.0455 REMARK 3 L TENSOR REMARK 3 L11: 2.5199 L22: 2.4221 REMARK 3 L33: 0.9253 L12: -1.6378 REMARK 3 L13: -0.7346 L23: 0.8452 REMARK 3 S TENSOR REMARK 3 S11: 0.1872 S12: 0.5495 S13: 0.2344 REMARK 3 S21: -0.2652 S22: -0.2695 S23: 0.0193 REMARK 3 S31: -0.1662 S32: -0.2322 S33: 0.0169 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 124 THROUGH 144 ) REMARK 3 ORIGIN FOR THE GROUP (A): 192.3449 9.3621 -4.8112 REMARK 3 T TENSOR REMARK 3 T11: 0.2762 T22: 0.4655 REMARK 3 T33: 0.2184 T12: -0.0369 REMARK 3 T13: 0.0200 T23: -0.0181 REMARK 3 L TENSOR REMARK 3 L11: 4.0877 L22: 5.8296 REMARK 3 L33: 4.9026 L12: 0.1068 REMARK 3 L13: 0.8738 L23: -0.4032 REMARK 3 S TENSOR REMARK 3 S11: 0.0277 S12: 0.1462 S13: -0.3224 REMARK 3 S21: 0.2053 S22: 0.0636 S23: -1.0783 REMARK 3 S31: 0.0074 S32: 0.7599 S33: 0.0130 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 145 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 182.7756 9.3834 -1.8535 REMARK 3 T TENSOR REMARK 3 T11: 0.2689 T22: 0.2646 REMARK 3 T33: 0.1219 T12: -0.0210 REMARK 3 T13: 0.0204 T23: -0.0141 REMARK 3 L TENSOR REMARK 3 L11: 2.6847 L22: 3.9821 REMARK 3 L33: 2.2079 L12: 0.3527 REMARK 3 L13: -0.4596 L23: -0.5158 REMARK 3 S TENSOR REMARK 3 S11: 0.0352 S12: 0.0482 S13: 0.0797 REMARK 3 S21: 0.1620 S22: -0.0095 S23: -0.3198 REMARK 3 S31: -0.0316 S32: 0.0777 S33: -0.0386 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 177.3963 44.6613 -3.2652 REMARK 3 T TENSOR REMARK 3 T11: 0.4594 T22: 0.4682 REMARK 3 T33: 0.6281 T12: -0.0162 REMARK 3 T13: 0.1728 T23: 0.1842 REMARK 3 L TENSOR REMARK 3 L11: 2.8276 L22: 3.6598 REMARK 3 L33: 3.3563 L12: -0.4468 REMARK 3 L13: 0.1262 L23: -0.4040 REMARK 3 S TENSOR REMARK 3 S11: 0.2606 S12: 0.6436 S13: 1.0901 REMARK 3 S21: -0.4216 S22: -0.1561 S23: -0.3606 REMARK 3 S31: -0.1900 S32: 0.0350 S33: -0.4606 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 168.8526 45.0797 2.5981 REMARK 3 T TENSOR REMARK 3 T11: 0.3802 T22: 0.2483 REMARK 3 T33: 0.5634 T12: 0.0138 REMARK 3 T13: 0.0627 T23: 0.1305 REMARK 3 L TENSOR REMARK 3 L11: 2.0551 L22: 2.8894 REMARK 3 L33: 1.0551 L12: -0.7933 REMARK 3 L13: -0.5030 L23: -0.0268 REMARK 3 S TENSOR REMARK 3 S11: 0.2159 S12: 0.3821 S13: 0.6055 REMARK 3 S21: -0.1942 S22: -0.0463 S23: 0.2474 REMARK 3 S31: -0.3602 S32: 0.0189 S33: -0.1518 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 103 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 190.5539 33.6777 -1.2646 REMARK 3 T TENSOR REMARK 3 T11: 0.2658 T22: 0.3510 REMARK 3 T33: 0.5798 T12: -0.0603 REMARK 3 T13: 0.0793 T23: 0.0472 REMARK 3 L TENSOR REMARK 3 L11: 2.3573 L22: 2.5309 REMARK 3 L33: 0.3544 L12: -1.8717 REMARK 3 L13: -0.6794 L23: 0.1110 REMARK 3 S TENSOR REMARK 3 S11: 0.0826 S12: 0.5098 S13: 0.6437 REMARK 3 S21: -0.3389 S22: 0.0255 S23: -0.1195 REMARK 3 S31: -0.1638 S32: 0.0135 S33: -0.1925 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 114 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 192.7011 16.2496 -14.2419 REMARK 3 T TENSOR REMARK 3 T11: 0.4866 T22: 0.4160 REMARK 3 T33: 0.2894 T12: -0.0279 REMARK 3 T13: 0.1636 T23: 0.0131 REMARK 3 L TENSOR REMARK 3 L11: 1.6615 L22: 3.1558 REMARK 3 L33: 2.3169 L12: 0.5159 REMARK 3 L13: 0.2011 L23: 1.0039 REMARK 3 S TENSOR REMARK 3 S11: 0.0309 S12: 0.4517 S13: 0.0065 REMARK 3 S21: -0.9170 S22: 0.0758 S23: -0.5565 REMARK 3 S31: -0.2324 S32: 0.1656 S33: -0.1070 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 1 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): 96.0704 9.8709 20.3946 REMARK 3 T TENSOR REMARK 3 T11: 0.2116 T22: 0.2627 REMARK 3 T33: 0.2377 T12: -0.0006 REMARK 3 T13: -0.0200 T23: -0.0045 REMARK 3 L TENSOR REMARK 3 L11: 6.2530 L22: 2.4586 REMARK 3 L33: 1.4717 L12: 1.3344 REMARK 3 L13: -2.1191 L23: -0.9248 REMARK 3 S TENSOR REMARK 3 S11: -0.0466 S12: -0.4039 S13: -0.2039 REMARK 3 S21: 0.0564 S22: -0.0346 S23: -0.1431 REMARK 3 S31: 0.0431 S32: 0.0246 S33: 0.0574 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 111 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.4484 11.5657 21.5415 REMARK 3 T TENSOR REMARK 3 T11: 0.3014 T22: 0.1745 REMARK 3 T33: 0.1286 T12: 0.0186 REMARK 3 T13: -0.0003 T23: -0.0399 REMARK 3 L TENSOR REMARK 3 L11: 3.9297 L22: 3.2323 REMARK 3 L33: 1.9029 L12: 0.2184 REMARK 3 L13: 0.3914 L23: -0.3303 REMARK 3 S TENSOR REMARK 3 S11: -0.0849 S12: -0.1628 S13: 0.2793 REMARK 3 S21: 0.0538 S22: 0.0312 S23: 0.1858 REMARK 3 S31: -0.1906 S32: -0.1410 S33: 0.0585 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 87.6882 35.2581 20.9962 REMARK 3 T TENSOR REMARK 3 T11: 0.4393 T22: 0.3555 REMARK 3 T33: 0.4947 T12: -0.0805 REMARK 3 T13: 0.0210 T23: -0.1781 REMARK 3 L TENSOR REMARK 3 L11: 5.2154 L22: 2.6602 REMARK 3 L33: 2.7889 L12: 0.5483 REMARK 3 L13: 0.6218 L23: -0.0429 REMARK 3 S TENSOR REMARK 3 S11: 0.1427 S12: -0.5143 S13: 0.8152 REMARK 3 S21: 0.0780 S22: 0.0692 S23: -0.0234 REMARK 3 S31: -0.2565 S32: 0.2266 S33: -0.2443 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 19 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 94.1706 29.9081 14.9503 REMARK 3 T TENSOR REMARK 3 T11: 0.2647 T22: 0.2766 REMARK 3 T33: 0.4005 T12: -0.0632 REMARK 3 T13: -0.0267 T23: -0.0900 REMARK 3 L TENSOR REMARK 3 L11: 3.2757 L22: 1.1293 REMARK 3 L33: 1.2238 L12: -0.2044 REMARK 3 L13: -0.1776 L23: -0.1215 REMARK 3 S TENSOR REMARK 3 S11: 0.0116 S12: -0.2283 S13: 0.3717 REMARK 3 S21: -0.0095 S22: 0.0633 S23: -0.1147 REMARK 3 S31: -0.0845 S32: 0.0642 S33: -0.0777 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 103 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 69.9264 35.2772 18.9804 REMARK 3 T TENSOR REMARK 3 T11: 0.2872 T22: 0.2765 REMARK 3 T33: 0.3796 T12: -0.0458 REMARK 3 T13: 0.0860 T23: -0.0724 REMARK 3 L TENSOR REMARK 3 L11: 5.7806 L22: 0.0192 REMARK 3 L33: 1.1552 L12: 0.0891 REMARK 3 L13: -0.9388 L23: -0.1389 REMARK 3 S TENSOR REMARK 3 S11: -0.1504 S12: -0.1149 S13: 0.4899 REMARK 3 S21: 0.0464 S22: 0.0378 S23: 0.1804 REMARK 3 S31: -0.0391 S32: 0.2861 S33: -0.2190 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 114 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.4326 23.3276 31.9652 REMARK 3 T TENSOR REMARK 3 T11: 0.3980 T22: 0.3164 REMARK 3 T33: 0.2366 T12: -0.0395 REMARK 3 T13: 0.0336 T23: -0.0981 REMARK 3 L TENSOR REMARK 3 L11: 1.8755 L22: 3.5139 REMARK 3 L33: 1.4093 L12: 1.4270 REMARK 3 L13: -0.9564 L23: -0.6466 REMARK 3 S TENSOR REMARK 3 S11: 0.2537 S12: -0.4904 S13: 0.3230 REMARK 3 S21: 0.5594 S22: -0.2750 S23: 0.2567 REMARK 3 S31: -0.1746 S32: 0.0923 S33: -0.0276 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 201 THROUGH 701 ) REMARK 3 ORIGIN FOR THE GROUP (A): 108.6412 18.1062 11.4986 REMARK 3 T TENSOR REMARK 3 T11: 0.6615 T22: 0.7839 REMARK 3 T33: 0.2576 T12: 0.0537 REMARK 3 T13: -0.1290 T23: -0.0851 REMARK 3 L TENSOR REMARK 3 L11: 0.6061 L22: 0.0504 REMARK 3 L33: -0.0919 L12: -0.2539 REMARK 3 L13: -0.1576 L23: -0.0369 REMARK 3 S TENSOR REMARK 3 S11: -0.2049 S12: 0.0323 S13: -0.0662 REMARK 3 S21: -0.0286 S22: 0.1237 S23: 0.0539 REMARK 3 S31: 0.1565 S32: 0.0893 S33: 0.2183 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 9HUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292144251. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-AUG-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID30B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : VERTICAL CRL / HORIZONTAL REMARK 200 ELLIPTICAL MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER R 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JUN 30, 2024 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.13 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74867 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420 REMARK 200 RESOLUTION RANGE LOW (A) : 47.830 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 11.30 REMARK 200 R MERGE (I) : 0.31700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.47 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 11.80 REMARK 200 R MERGE FOR SHELL (I) : 3.24200 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 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM HEPES, MOPS 0.1M DL REMARK 280 -GLUTAMIC ACID MONOHYDRATE; 0.1M DL-ALANINE; 0.1M GLYCINE; 0.1M REMARK 280 DL-LYSINE 40% V/V GLYCEROL; 20% W/V PEG 4000, PH 7.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, 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 58.62700 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 119.62300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.62700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 119.62300 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, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, I, M REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH H 485 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 491 LIES ON A SPECIAL POSITION. REMARK 375 HOH I 480 LIES ON A SPECIAL POSITION. REMARK 375 HOH I 481 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -9 REMARK 465 ARG A -8 REMARK 465 GLY A -7 REMARK 465 SER A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 HIS A -1 REMARK 465 HIS A 0 REMARK 465 THR A 1 REMARK 465 ASP A 2 REMARK 465 PRO A 3 REMARK 465 GLN A 4 REMARK 465 GLY A 5 REMARK 465 ASP A 6 REMARK 465 ALA A 7 REMARK 465 ALA A 8 REMARK 465 GLN A 9 REMARK 465 LYS A 10 REMARK 465 THR A 11 REMARK 465 ASP A 12 REMARK 465 THR A 13 REMARK 465 SER A 14 REMARK 465 HIS A 15 REMARK 465 HIS A 16 REMARK 465 ASP A 17 REMARK 465 GLN A 18 REMARK 465 ASP A 19 REMARK 465 HIS A 20 REMARK 465 PRO A 21 REMARK 465 THR A 22 REMARK 465 ALA B 355 REMARK 465 ILE B 356 REMARK 465 PRO B 357 REMARK 465 MET B 358 REMARK 465 SER B 359 REMARK 465 ILE B 360 REMARK 465 PRO B 361 REMARK 465 LYS B 394 REMARK 465 MET C -9 REMARK 465 ARG C -8 REMARK 465 GLY C -7 REMARK 465 SER C -6 REMARK 465 HIS C -5 REMARK 465 HIS C -4 REMARK 465 HIS C -3 REMARK 465 HIS C -2 REMARK 465 HIS C -1 REMARK 465 HIS C 0 REMARK 465 THR C 1 REMARK 465 ASP C 2 REMARK 465 PRO C 3 REMARK 465 GLN C 4 REMARK 465 GLY C 5 REMARK 465 ASP C 6 REMARK 465 ALA C 7 REMARK 465 ALA C 8 REMARK 465 GLN C 9 REMARK 465 LYS C 10 REMARK 465 THR C 11 REMARK 465 ASP C 12 REMARK 465 THR C 13 REMARK 465 SER C 14 REMARK 465 HIS C 15 REMARK 465 HIS C 16 REMARK 465 ASP C 17 REMARK 465 GLN C 18 REMARK 465 ASP C 19 REMARK 465 HIS C 20 REMARK 465 PRO C 21 REMARK 465 THR C 22 REMARK 465 ALA D 355 REMARK 465 ILE D 356 REMARK 465 PRO D 357 REMARK 465 MET D 358 REMARK 465 SER D 359 REMARK 465 ILE D 360 REMARK 465 PRO D 361 REMARK 465 CYS H 214 REMARK 465 CYS L 214 REMARK 465 ALA I 129 REMARK 465 GLN I 130 REMARK 465 THR I 131 REMARK 465 CYS I 214 REMARK 465 CYS M 214 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 PHE A 23 CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 25 CG CD CE NZ REMARK 470 SER A 45 OG REMARK 470 GLU A 75 CG CD OE1 OE2 REMARK 470 ARG A 101 NE CZ NH1 NH2 REMARK 470 GLU A 122 CG CD OE1 OE2 REMARK 470 LYS A 125 CG CD CE NZ REMARK 470 PHE A 147 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A 149 CG OD1 OD2 REMARK 470 GLU A 152 CG CD OE1 OE2 REMARK 470 LYS A 154 CD CE NZ REMARK 470 LYS A 155 CG CD CE NZ REMARK 470 GLN A 156 OE1 NE2 REMARK 470 VAL A 173 CG1 CG2 REMARK 470 LYS A 174 CG CD CE NZ REMARK 470 GLU A 175 CG CD OE1 OE2 REMARK 470 ASP A 177 CG OD1 OD2 REMARK 470 ARG A 178 NE CZ NH1 NH2 REMARK 470 ARG A 196 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 201 CD CE NZ REMARK 470 LYS A 222 CG CD CE NZ REMARK 470 GLN A 230 CG CD OE1 NE2 REMARK 470 CYS A 232 SG REMARK 470 LYS A 233 CD CE NZ REMARK 470 LYS A 234 CG CD CE NZ REMARK 470 GLU A 257 CG CD OE1 OE2 REMARK 470 ASP A 270 CG OD1 OD2 REMARK 470 LYS A 274 CG CD CE NZ REMARK 470 GLU A 279 CG CD OE1 OE2 REMARK 470 ASP A 280 CG OD1 OD2 REMARK 470 ARG A 281 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 282 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 300 CG CD CE NZ REMARK 470 LYS A 310 CG CD CE NZ REMARK 470 LYS A 328 CG CD CE NZ REMARK 470 LYS A 331 CG CD CE NZ REMARK 470 GLU B 363 CG CD OE1 OE2 REMARK 470 LYS B 365 CG CD CE NZ REMARK 470 GLN B 377 CG CD OE1 NE2 REMARK 470 GLN B 393 CG CD OE1 NE2 REMARK 470 PHE C 23 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS C 25 CG CD CE NZ REMARK 470 HIS C 43 CG ND1 CD2 CE1 NE2 REMARK 470 ASN C 46 CG OD1 ND2 REMARK 470 ARG C 101 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 105 CG CD OE1 NE2 REMARK 470 GLU C 122 CG CD OE1 OE2 REMARK 470 LYS C 155 CE NZ REMARK 470 ARG C 178 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 193 CE NZ REMARK 470 ARG C 196 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 199 CG CD OE1 OE2 REMARK 470 LYS C 201 CD CE NZ REMARK 470 GLU C 204 CG CD OE1 OE2 REMARK 470 GLN C 212 CG CD OE1 NE2 REMARK 470 LYS C 217 CG CD CE NZ REMARK 470 LYS C 222 CG CD CE NZ REMARK 470 ARG C 223 CG CD NE CZ NH1 NH2 REMARK 470 LEU C 224 CG CD1 CD2 REMARK 470 GLN C 230 CG CD OE1 NE2 REMARK 470 LYS C 233 CG CD CE NZ REMARK 470 LYS C 234 CD CE NZ REMARK 470 GLU C 257 CG CD OE1 OE2 REMARK 470 LYS C 259 CG CD CE NZ REMARK 470 LYS C 274 CG CD CE NZ REMARK 470 ASP C 280 CG OD1 OD2 REMARK 470 ARG C 282 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 343 CE NZ REMARK 470 VAL D 364 CG1 CG2 REMARK 470 LYS D 365 CG CD CE NZ REMARK 470 LYS D 380 CG CD CE NZ REMARK 470 LYS D 394 CG CD CE NZ REMARK 470 GLN H 3 CG CD OE1 NE2 REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 GLU H 42 CG CD OE1 OE2 REMARK 470 GLN H 64 CG CD OE1 NE2 REMARK 470 LYS H 114 CG CD CE NZ REMARK 470 GLN H 130 CD OE1 NE2 REMARK 470 THR H 131 OG1 CG2 REMARK 470 GLN H 170 CG CD OE1 NE2 REMARK 470 GLU H 190 CG CD OE1 OE2 REMARK 470 LYS H 204 CG CD CE NZ REMARK 470 ASP H 213 CG OD1 OD2 REMARK 470 LYS L 24 CG CD CE NZ REMARK 470 LYS L 107 CD CE NZ REMARK 470 LYS L 147 CD CE NZ REMARK 470 LEU L 160 CG CD1 CD2 REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 LYS I 13 CD CE NZ REMARK 470 LYS I 30 CD CE NZ REMARK 470 GLU I 42 CG CD OE1 OE2 REMARK 470 GLN I 64 CG CD OE1 NE2 REMARK 470 LYS I 114 CE NZ REMARK 470 SER I 127 OG REMARK 470 LYS I 204 CE NZ REMARK 470 LYS M 24 CD CE NZ REMARK 470 ASN M 56 CG OD1 ND2 REMARK 470 GLU M 105 CG CD OE1 OE2 REMARK 470 LYS M 107 CG CD CE NZ REMARK 470 LYS M 147 CG CD CE NZ REMARK 470 LYS M 169 CE NZ REMARK 470 GLU M 213 CG CD OE1 OE2 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 70 -133.47 58.27 REMARK 500 ASN A 247 57.35 -94.71 REMARK 500 PHE C 51 116.45 -160.20 REMARK 500 ALA C 70 -136.52 58.12 REMARK 500 ARG H 96 -65.26 -104.98 REMARK 500 THR H 131 10.89 58.47 REMARK 500 ASP H 172 17.93 59.29 REMARK 500 SER L 30 -129.79 57.02 REMARK 500 ALA L 51 -12.43 73.11 REMARK 500 SER L 52 -1.64 -144.75 REMARK 500 ALA L 84 -169.54 -166.38 REMARK 500 PRO L 95 99.40 -69.76 REMARK 500 ASN L 138 60.80 61.25 REMARK 500 SER M 30 -130.04 57.93 REMARK 500 ALA M 51 -13.48 73.15 REMARK 500 ALA M 84 -167.58 -164.03 REMARK 500 REMARK 500 REMARK: NULL DBREF 9HUD A 2 354 UNP P01009 A1AT_HUMAN 26 378 DBREF 9HUD B 355 394 UNP P01009 A1AT_HUMAN 379 418 DBREF 9HUD C 2 354 UNP P01009 A1AT_HUMAN 26 378 DBREF 9HUD D 355 394 UNP P01009 A1AT_HUMAN 379 418 DBREF 9HUD H 1 214 PDB 9HUD 9HUD 1 214 DBREF 9HUD L 1 214 PDB 9HUD 9HUD 1 214 DBREF 9HUD I 1 214 PDB 9HUD 9HUD 1 214 DBREF 9HUD M 1 214 PDB 9HUD 9HUD 1 214 SEQADV 9HUD MET A -9 UNP P01009 INITIATING METHIONINE SEQADV 9HUD ARG A -8 UNP P01009 EXPRESSION TAG SEQADV 9HUD GLY A -7 UNP P01009 EXPRESSION TAG SEQADV 9HUD SER A -6 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS A -5 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS A -4 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS A -3 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS A -2 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS A -1 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS A 0 UNP P01009 EXPRESSION TAG SEQADV 9HUD THR A 1 UNP P01009 EXPRESSION TAG SEQADV 9HUD MET C -9 UNP P01009 INITIATING METHIONINE SEQADV 9HUD ARG C -8 UNP P01009 EXPRESSION TAG SEQADV 9HUD GLY C -7 UNP P01009 EXPRESSION TAG SEQADV 9HUD SER C -6 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS C -5 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS C -4 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS C -3 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS C -2 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS C -1 UNP P01009 EXPRESSION TAG SEQADV 9HUD HIS C 0 UNP P01009 EXPRESSION TAG SEQADV 9HUD THR C 1 UNP P01009 EXPRESSION TAG SEQRES 1 A 364 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO SEQRES 2 A 364 GLN GLY ASP ALA ALA GLN LYS THR ASP THR SER HIS HIS SEQRES 3 A 364 ASP GLN ASP HIS PRO THR PHE ASN LYS ILE THR PRO ASN SEQRES 4 A 364 LEU ALA GLU PHE ALA PHE SER LEU TYR ARG GLN LEU ALA SEQRES 5 A 364 HIS GLN SER ASN SER THR ASN ILE PHE PHE SER PRO VAL SEQRES 6 A 364 SER ILE ALA THR ALA PHE ALA MET LEU SER LEU GLY THR SEQRES 7 A 364 LYS ALA ASP THR HIS ASP GLU ILE LEU GLU GLY LEU ASN SEQRES 8 A 364 PHE ASN LEU THR GLU ILE PRO GLU ALA GLN ILE HIS GLU SEQRES 9 A 364 GLY PHE GLN GLU LEU LEU ARG THR LEU ASN GLN PRO ASP SEQRES 10 A 364 SER GLN LEU GLN LEU THR THR GLY ASN GLY LEU PHE LEU SEQRES 11 A 364 SER GLU GLY LEU LYS LEU VAL ASP LYS PHE LEU GLU ASP SEQRES 12 A 364 VAL LYS LYS LEU TYR HIS SER GLU ALA PHE THR VAL ASN SEQRES 13 A 364 PHE GLY ASP THR GLU GLU ALA LYS LYS GLN ILE ASN ASP SEQRES 14 A 364 TYR VAL GLU LYS GLY THR GLN GLY LYS ILE VAL ASP LEU SEQRES 15 A 364 VAL LYS GLU LEU ASP ARG ASP THR VAL PHE ALA LEU VAL SEQRES 16 A 364 ASN TYR ILE PHE PHE LYS GLY LYS TRP GLU ARG PRO PHE SEQRES 17 A 364 GLU VAL LYS ASP THR GLU GLU GLU ASP PHE HIS VAL ASP SEQRES 18 A 364 GLN VAL THR THR VAL LYS VAL PRO MET MET LYS ARG LEU SEQRES 19 A 364 GLY MET PHE ASN ILE GLN HIS CYS LYS LYS LEU SER SER SEQRES 20 A 364 TRP VAL LEU LEU MET LYS TYR LEU GLY ASN ALA THR ALA SEQRES 21 A 364 ILE PHE PHE LEU PRO ASP GLU GLY LYS LEU GLN HIS LEU SEQRES 22 A 364 GLU ASN GLU LEU THR HIS ASP ILE ILE THR LYS PHE LEU SEQRES 23 A 364 GLU ASN GLU ASP ARG ARG SER ALA SER LEU HIS LEU PRO SEQRES 24 A 364 LYS LEU SER ILE THR GLY THR TYR ASP LEU LYS SER VAL SEQRES 25 A 364 LEU GLY GLN LEU GLY ILE THR LYS VAL PHE SER ASN GLY SEQRES 26 A 364 ALA ASP LEU SER GLY VAL THR GLU GLU ALA PRO LEU LYS SEQRES 27 A 364 LEU SER LYS ALA VAL HIS LYS ALA VAL LEU THR ILE ASP SEQRES 28 A 364 GLU LYS GLY THR GLU ALA ALA GLY ALA MET PHE LEU GLU SEQRES 1 B 40 ALA ILE PRO MET SER ILE PRO PRO GLU VAL LYS PHE ASN SEQRES 2 B 40 LYS PRO PHE VAL PHE LEU MET ILE GLU GLN ASN THR LYS SEQRES 3 B 40 SER PRO LEU PHE MET GLY LYS VAL VAL ASN PRO THR GLN SEQRES 4 B 40 LYS SEQRES 1 C 364 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO SEQRES 2 C 364 GLN GLY ASP ALA ALA GLN LYS THR ASP THR SER HIS HIS SEQRES 3 C 364 ASP GLN ASP HIS PRO THR PHE ASN LYS ILE THR PRO ASN SEQRES 4 C 364 LEU ALA GLU PHE ALA PHE SER LEU TYR ARG GLN LEU ALA SEQRES 5 C 364 HIS GLN SER ASN SER THR ASN ILE PHE PHE SER PRO VAL SEQRES 6 C 364 SER ILE ALA THR ALA PHE ALA MET LEU SER LEU GLY THR SEQRES 7 C 364 LYS ALA ASP THR HIS ASP GLU ILE LEU GLU GLY LEU ASN SEQRES 8 C 364 PHE ASN LEU THR GLU ILE PRO GLU ALA GLN ILE HIS GLU SEQRES 9 C 364 GLY PHE GLN GLU LEU LEU ARG THR LEU ASN GLN PRO ASP SEQRES 10 C 364 SER GLN LEU GLN LEU THR THR GLY ASN GLY LEU PHE LEU SEQRES 11 C 364 SER GLU GLY LEU LYS LEU VAL ASP LYS PHE LEU GLU ASP SEQRES 12 C 364 VAL LYS LYS LEU TYR HIS SER GLU ALA PHE THR VAL ASN SEQRES 13 C 364 PHE GLY ASP THR GLU GLU ALA LYS LYS GLN ILE ASN ASP SEQRES 14 C 364 TYR VAL GLU LYS GLY THR GLN GLY LYS ILE VAL ASP LEU SEQRES 15 C 364 VAL LYS GLU LEU ASP ARG ASP THR VAL PHE ALA LEU VAL SEQRES 16 C 364 ASN TYR ILE PHE PHE LYS GLY LYS TRP GLU ARG PRO PHE SEQRES 17 C 364 GLU VAL LYS ASP THR GLU GLU GLU ASP PHE HIS VAL ASP SEQRES 18 C 364 GLN VAL THR THR VAL LYS VAL PRO MET MET LYS ARG LEU SEQRES 19 C 364 GLY MET PHE ASN ILE GLN HIS CYS LYS LYS LEU SER SER SEQRES 20 C 364 TRP VAL LEU LEU MET LYS TYR LEU GLY ASN ALA THR ALA SEQRES 21 C 364 ILE PHE PHE LEU PRO ASP GLU GLY LYS LEU GLN HIS LEU SEQRES 22 C 364 GLU ASN GLU LEU THR HIS ASP ILE ILE THR LYS PHE LEU SEQRES 23 C 364 GLU ASN GLU ASP ARG ARG SER ALA SER LEU HIS LEU PRO SEQRES 24 C 364 LYS LEU SER ILE THR GLY THR TYR ASP LEU LYS SER VAL SEQRES 25 C 364 LEU GLY GLN LEU GLY ILE THR LYS VAL PHE SER ASN GLY SEQRES 26 C 364 ALA ASP LEU SER GLY VAL THR GLU GLU ALA PRO LEU LYS SEQRES 27 C 364 LEU SER LYS ALA VAL HIS LYS ALA VAL LEU THR ILE ASP SEQRES 28 C 364 GLU LYS GLY THR GLU ALA ALA GLY ALA MET PHE LEU GLU SEQRES 1 D 40 ALA ILE PRO MET SER ILE PRO PRO GLU VAL LYS PHE ASN SEQRES 2 D 40 LYS PRO PHE VAL PHE LEU MET ILE GLU GLN ASN THR LYS SEQRES 3 D 40 SER PRO LEU PHE MET GLY LYS VAL VAL ASN PRO THR GLN SEQRES 4 D 40 LYS SEQRES 1 H 218 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 H 218 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA THR GLY SEQRES 3 H 218 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN SEQRES 4 H 218 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 H 218 PRO ALA ASN GLY ASN THR LYS TYR ASP PRO LYS PHE GLN SEQRES 6 H 218 GLY LYS ALA THR LEU THR ALA ASP THR SER SER ASN THR SEQRES 7 H 218 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 H 218 ALA VAL TYR TYR CYS ALA ARG LYS ARG TYR SER MET ASP SEQRES 9 H 218 TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER ALA SEQRES 10 H 218 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SEQRES 11 H 218 SER GLY ALA GLN THR ASN SER MET VAL THR LEU GLY CYS SEQRES 12 H 218 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR SEQRES 13 H 218 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 H 218 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 H 218 SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR SEQRES 16 H 218 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 H 218 VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 1 L 214 SER ILE VAL MET THR GLN THR PRO LYS PHE LEU LEU VAL SEQRES 2 L 214 SER ALA GLY GLU ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 L 214 GLN SER VAL SER ASN ASP VAL GLY TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ASN ALA SER SEQRES 5 L 214 ASN ARG LYS ASN GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 214 GLY TYR GLY THR ASP PHE THR PHE THR ILE SER THR VAL SEQRES 7 L 214 GLN ALA GLU ASP LEU ALA VAL TYR PHE CYS GLN GLN ASP SEQRES 8 L 214 HIS SER PHE PRO LEU LYS PHE GLY ALA GLY THR LYS LEU SEQRES 9 L 214 GLU LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS SEQRES 1 I 218 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 I 218 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA THR GLY SEQRES 3 I 218 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN SEQRES 4 I 218 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 I 218 PRO ALA ASN GLY ASN THR LYS TYR ASP PRO LYS PHE GLN SEQRES 6 I 218 GLY LYS ALA THR LEU THR ALA ASP THR SER SER ASN THR SEQRES 7 I 218 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 I 218 ALA VAL TYR TYR CYS ALA ARG LYS ARG TYR SER MET ASP SEQRES 9 I 218 TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER ALA SEQRES 10 I 218 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SEQRES 11 I 218 SER GLY ALA GLN THR ASN SER MET VAL THR LEU GLY CYS SEQRES 12 I 218 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR SEQRES 13 I 218 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 I 218 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 I 218 SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR SEQRES 16 I 218 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 I 218 VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 1 M 214 SER ILE VAL MET THR GLN THR PRO LYS PHE LEU LEU VAL SEQRES 2 M 214 SER ALA GLY GLU ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 M 214 GLN SER VAL SER ASN ASP VAL GLY TRP TYR GLN GLN LYS SEQRES 4 M 214 PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ASN ALA SER SEQRES 5 M 214 ASN ARG LYS ASN GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 M 214 GLY TYR GLY THR ASP PHE THR PHE THR ILE SER THR VAL SEQRES 7 M 214 GLN ALA GLU ASP LEU ALA VAL TYR PHE CYS GLN GLN ASP SEQRES 8 M 214 HIS SER PHE PRO LEU LYS PHE GLY ALA GLY THR LYS LEU SEQRES 9 M 214 GLU LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 M 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 M 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 M 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 M 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 M 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 M 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 M 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 M 214 PHE ASN ARG ASN GLU CYS HET EDO C 401 4 HET EDO C 402 4 HET GLY H 301 5 HET GLY H 302 5 HET CL H 303 1 HET EDO L 401 4 HET NA L 402 1 HET GLY I 301 5 HET EDO I 302 4 HET GOL I 303 6 HET EDO M 501 4 HET EDO M 502 4 HET LYS M 503 10 HET CL M 504 1 HET NA M 505 1 HETNAM EDO 1,2-ETHANEDIOL HETNAM GLY GLYCINE HETNAM CL CHLORIDE ION HETNAM NA SODIUM ION HETNAM GOL GLYCEROL HETNAM LYS LYSINE HETSYN EDO ETHYLENE GLYCOL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 9 EDO 6(C2 H6 O2) FORMUL 11 GLY 3(C2 H5 N O2) FORMUL 13 CL 2(CL 1-) FORMUL 15 NA 2(NA 1+) FORMUL 18 GOL C3 H8 O3 FORMUL 21 LYS C6 H15 N2 O2 1+ FORMUL 24 HOH *596(H2 O) HELIX 1 AA1 ILE A 26 SER A 45 1 20 HELIX 2 AA2 SER A 53 LEU A 66 1 14 HELIX 3 AA3 LYS A 69 LEU A 80 1 12 HELIX 4 AA4 PRO A 88 ASN A 104 1 17 HELIX 5 AA5 VAL A 127 TYR A 138 1 12 HELIX 6 AA6 ASP A 149 THR A 165 1 17 HELIX 7 AA7 GLU A 199 THR A 203 5 5 HELIX 8 AA8 LYS A 259 GLU A 266 1 8 HELIX 9 AA9 THR A 268 ASN A 278 1 11 HELIX 10 AB1 LEU A 299 LEU A 306 1 8 HELIX 11 AB2 THR A 309 SER A 313 5 5 HELIX 12 AB3 ILE C 26 SER C 45 1 20 HELIX 13 AB4 SER C 53 LEU C 66 1 14 HELIX 14 AB5 LYS C 69 LEU C 80 1 12 HELIX 15 AB6 PRO C 88 ASN C 104 1 17 HELIX 16 AB7 VAL C 127 TYR C 138 1 12 HELIX 17 AB8 ASP C 149 THR C 165 1 17 HELIX 18 AB9 GLU C 199 THR C 203 5 5 HELIX 19 AC1 LYS C 259 LEU C 267 1 9 HELIX 20 AC2 THR C 268 ASN C 278 1 11 HELIX 21 AC3 LEU C 299 LEU C 306 1 8 HELIX 22 AC4 THR C 309 SER C 313 5 5 HELIX 23 AC5 ASN H 28 THR H 32 5 5 HELIX 24 AC6 PRO H 61 GLN H 64 5 4 HELIX 25 AC7 THR H 73 SER H 75 5 3 HELIX 26 AC8 THR H 83 THR H 87 5 5 HELIX 27 AC9 SER H 155 SER H 157 5 3 HELIX 28 AD1 PRO H 199 SER H 202 5 4 HELIX 29 AD2 GLN L 79 LEU L 83 5 5 HELIX 30 AD3 SER L 121 SER L 127 1 7 HELIX 31 AD4 LYS L 183 GLU L 187 1 5 HELIX 32 AD5 ASN I 28 THR I 32 5 5 HELIX 33 AD6 PRO I 61 GLN I 64 5 4 HELIX 34 AD7 THR I 83 THR I 87 5 5 HELIX 35 AD8 SER I 155 SER I 157 5 3 HELIX 36 AD9 PRO I 199 SER I 202 5 4 HELIX 37 AE1 GLN M 79 LEU M 83 5 5 HELIX 38 AE2 SER M 121 THR M 126 1 6 HELIX 39 AE3 LYS M 183 GLU M 187 1 5 SHEET 1 AA1 7 ILE A 50 PHE A 52 0 SHEET 2 AA1 7 PRO B 382 VAL B 388 -1 O MET B 385 N PHE A 52 SHEET 3 AA1 7 PHE B 370 GLU B 376 -1 N PHE B 370 O VAL B 388 SHEET 4 AA1 7 ALA A 248 PRO A 255 -1 N PHE A 253 O VAL B 371 SHEET 5 AA1 7 SER A 237 TYR A 244 -1 N LEU A 240 O PHE A 252 SHEET 6 AA1 7 THR A 215 CYS A 232 -1 N GLN A 230 O VAL A 239 SHEET 7 AA1 7 GLU A 204 HIS A 209 -1 N GLU A 206 O VAL A 218 SHEET 1 AA2 8 ILE A 50 PHE A 52 0 SHEET 2 AA2 8 PRO B 382 VAL B 388 -1 O MET B 385 N PHE A 52 SHEET 3 AA2 8 PHE B 370 GLU B 376 -1 N PHE B 370 O VAL B 388 SHEET 4 AA2 8 ALA A 248 PRO A 255 -1 N PHE A 253 O VAL B 371 SHEET 5 AA2 8 SER A 237 TYR A 244 -1 N LEU A 240 O PHE A 252 SHEET 6 AA2 8 THR A 215 CYS A 232 -1 N GLN A 230 O VAL A 239 SHEET 7 AA2 8 ARG A 282 PRO A 289 -1 O ARG A 282 N PHE A 227 SHEET 8 AA2 8 GLU B 363 LYS B 365 1 O VAL B 364 N HIS A 287 SHEET 1 AA3 6 GLU A 141 THR A 144 0 SHEET 2 AA3 6 GLN A 111 LEU A 120 1 N LEU A 118 O GLU A 141 SHEET 3 AA3 6 PHE A 182 LYS A 193 -1 O VAL A 185 N GLY A 117 SHEET 4 AA3 6 GLY A 344 GLU A 354 -1 O ALA A 347 N PHE A 190 SHEET 5 AA3 6 LYS A 331 ILE A 340 -1 N VAL A 333 O PHE A 352 SHEET 6 AA3 6 THR A 294 ASP A 298 -1 N GLY A 295 O ALA A 336 SHEET 1 AA4 7 ILE C 50 PHE C 52 0 SHEET 2 AA4 7 PRO D 382 VAL D 388 -1 O MET D 385 N PHE C 52 SHEET 3 AA4 7 PHE D 370 GLU D 376 -1 N MET D 374 O PHE D 384 SHEET 4 AA4 7 ALA C 248 PRO C 255 -1 N PHE C 253 O VAL D 371 SHEET 5 AA4 7 SER C 237 LYS C 243 -1 N MET C 242 O ALA C 250 SHEET 6 AA4 7 THR C 215 CYS C 232 -1 N GLN C 230 O VAL C 239 SHEET 7 AA4 7 GLU C 204 HIS C 209 -1 N GLU C 206 O VAL C 218 SHEET 1 AA5 8 ILE C 50 PHE C 52 0 SHEET 2 AA5 8 PRO D 382 VAL D 388 -1 O MET D 385 N PHE C 52 SHEET 3 AA5 8 PHE D 370 GLU D 376 -1 N MET D 374 O PHE D 384 SHEET 4 AA5 8 ALA C 248 PRO C 255 -1 N PHE C 253 O VAL D 371 SHEET 5 AA5 8 SER C 237 LYS C 243 -1 N MET C 242 O ALA C 250 SHEET 6 AA5 8 THR C 215 CYS C 232 -1 N GLN C 230 O VAL C 239 SHEET 7 AA5 8 ARG C 282 PRO C 289 -1 O LEU C 286 N ARG C 223 SHEET 8 AA5 8 GLU D 363 LYS D 365 1 O VAL D 364 N SER C 285 SHEET 1 AA6 6 GLU C 141 VAL C 145 0 SHEET 2 AA6 6 GLN C 111 SER C 121 1 N LEU C 118 O PHE C 143 SHEET 3 AA6 6 PHE C 182 LYS C 193 -1 O VAL C 185 N GLY C 117 SHEET 4 AA6 6 GLY C 344 GLU C 354 -1 O ALA C 347 N PHE C 190 SHEET 5 AA6 6 LYS C 331 ILE C 340 -1 N VAL C 337 O ALA C 348 SHEET 6 AA6 6 LEU C 291 ASP C 298 -1 N GLY C 295 O ALA C 336 SHEET 1 AA7 4 GLN H 3 GLN H 6 0 SHEET 2 AA7 4 VAL H 18 THR H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA7 4 THR H 77 LEU H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA7 4 ALA H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA8 6 GLU H 10 VAL H 12 0 SHEET 2 AA8 6 THR H 106 VAL H 110 1 O SER H 107 N GLU H 10 SHEET 3 AA8 6 ALA H 88 LYS H 95 -1 N ALA H 88 O VAL H 108 SHEET 4 AA8 6 TYR H 33 GLN H 39 -1 N HIS H 35 O ALA H 93 SHEET 5 AA8 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA8 6 THR H 57 TYR H 59 -1 O LYS H 58 N ARG H 50 SHEET 1 AA9 4 GLU H 10 VAL H 12 0 SHEET 2 AA9 4 THR H 106 VAL H 110 1 O SER H 107 N GLU H 10 SHEET 3 AA9 4 ALA H 88 LYS H 95 -1 N ALA H 88 O VAL H 108 SHEET 4 AA9 4 MET H 99 TRP H 102 -1 O TYR H 101 N ARG H 94 SHEET 1 AB1 4 SER H 119 LEU H 123 0 SHEET 2 AB1 4 MET H 134 TYR H 144 -1 O LEU H 140 N TYR H 121 SHEET 3 AB1 4 LEU H 173 PRO H 183 -1 O VAL H 182 N VAL H 135 SHEET 4 AB1 4 VAL H 162 THR H 164 -1 N HIS H 163 O SER H 179 SHEET 1 AB2 4 SER H 119 LEU H 123 0 SHEET 2 AB2 4 MET H 134 TYR H 144 -1 O LEU H 140 N TYR H 121 SHEET 3 AB2 4 LEU H 173 PRO H 183 -1 O VAL H 182 N VAL H 135 SHEET 4 AB2 4 VAL H 168 GLN H 170 -1 N VAL H 168 O THR H 175 SHEET 1 AB3 3 THR H 150 TRP H 153 0 SHEET 2 AB3 3 THR H 193 HIS H 198 -1 O ASN H 195 N THR H 152 SHEET 3 AB3 3 THR H 203 LYS H 208 -1 O VAL H 205 N VAL H 196 SHEET 1 AB4 4 MET L 4 THR L 7 0 SHEET 2 AB4 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AB4 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AB4 4 PHE L 62 TYR L 67 -1 N SER L 65 O THR L 72 SHEET 1 AB5 6 PHE L 10 VAL L 13 0 SHEET 2 AB5 6 THR L 102 LEU L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AB5 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB5 6 VAL L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AB5 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB5 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AB6 4 PHE L 10 VAL L 13 0 SHEET 2 AB6 4 THR L 102 LEU L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AB6 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB6 4 LYS L 97 PHE L 98 -1 O LYS L 97 N GLN L 90 SHEET 1 AB7 4 THR L 114 PHE L 118 0 SHEET 2 AB7 4 GLY L 129 PHE L 139 -1 O PHE L 135 N SER L 116 SHEET 3 AB7 4 TYR L 173 THR L 182 -1 O MET L 175 N LEU L 136 SHEET 4 AB7 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 AB8 4 SER L 153 GLU L 154 0 SHEET 2 AB8 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AB8 4 SER L 191 THR L 197 -1 O GLU L 195 N LYS L 147 SHEET 4 AB8 4 ILE L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SHEET 1 AB9 4 GLN I 3 GLN I 6 0 SHEET 2 AB9 4 VAL I 18 THR I 25 -1 O THR I 23 N GLN I 5 SHEET 3 AB9 4 THR I 77 LEU I 82 -1 O LEU I 80 N LEU I 20 SHEET 4 AB9 4 ALA I 67 ASP I 72 -1 N ASP I 72 O THR I 77 SHEET 1 AC1 6 GLU I 10 VAL I 12 0 SHEET 2 AC1 6 THR I 106 VAL I 110 1 O SER I 107 N GLU I 10 SHEET 3 AC1 6 ALA I 88 LYS I 95 -1 N ALA I 88 O VAL I 108 SHEET 4 AC1 6 TYR I 33 ARG I 40 -1 N VAL I 37 O TYR I 91 SHEET 5 AC1 6 GLY I 44 ILE I 51 -1 O GLU I 46 N LYS I 38 SHEET 6 AC1 6 THR I 57 TYR I 59 -1 O LYS I 58 N ARG I 50 SHEET 1 AC2 4 GLU I 10 VAL I 12 0 SHEET 2 AC2 4 THR I 106 VAL I 110 1 O SER I 107 N GLU I 10 SHEET 3 AC2 4 ALA I 88 LYS I 95 -1 N ALA I 88 O VAL I 108 SHEET 4 AC2 4 MET I 99 TRP I 102 -1 O TYR I 101 N ARG I 94 SHEET 1 AC3 4 SER I 119 LEU I 123 0 SHEET 2 AC3 4 MET I 134 TYR I 144 -1 O LYS I 142 N SER I 119 SHEET 3 AC3 4 LEU I 173 PRO I 183 -1 O TYR I 174 N TYR I 144 SHEET 4 AC3 4 VAL I 162 THR I 164 -1 N HIS I 163 O SER I 179 SHEET 1 AC4 4 SER I 119 LEU I 123 0 SHEET 2 AC4 4 MET I 134 TYR I 144 -1 O LYS I 142 N SER I 119 SHEET 3 AC4 4 LEU I 173 PRO I 183 -1 O TYR I 174 N TYR I 144 SHEET 4 AC4 4 VAL I 168 GLN I 170 -1 N GLN I 170 O LEU I 173 SHEET 1 AC5 3 THR I 150 TRP I 153 0 SHEET 2 AC5 3 THR I 193 HIS I 198 -1 O ASN I 195 N THR I 152 SHEET 3 AC5 3 THR I 203 LYS I 208 -1 O VAL I 205 N VAL I 196 SHEET 1 AC6 4 MET M 4 THR M 7 0 SHEET 2 AC6 4 VAL M 19 ALA M 25 -1 O THR M 22 N THR M 7 SHEET 3 AC6 4 ASP M 70 ILE M 75 -1 O PHE M 73 N ILE M 21 SHEET 4 AC6 4 PHE M 62 TYR M 67 -1 N SER M 65 O THR M 72 SHEET 1 AC7 6 PHE M 10 VAL M 13 0 SHEET 2 AC7 6 THR M 102 LEU M 106 1 O GLU M 105 N VAL M 13 SHEET 3 AC7 6 VAL M 85 GLN M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AC7 6 VAL M 33 GLN M 38 -1 N GLN M 38 O VAL M 85 SHEET 5 AC7 6 LYS M 45 TYR M 49 -1 O LEU M 47 N TRP M 35 SHEET 6 AC7 6 ASN M 53 ARG M 54 -1 O ASN M 53 N TYR M 49 SHEET 1 AC8 4 PHE M 10 VAL M 13 0 SHEET 2 AC8 4 THR M 102 LEU M 106 1 O GLU M 105 N VAL M 13 SHEET 3 AC8 4 VAL M 85 GLN M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AC8 4 LYS M 97 PHE M 98 -1 O LYS M 97 N GLN M 90 SHEET 1 AC9 4 THR M 114 PHE M 118 0 SHEET 2 AC9 4 GLY M 129 PHE M 139 -1 O ASN M 137 N THR M 114 SHEET 3 AC9 4 TYR M 173 THR M 182 -1 O LEU M 181 N ALA M 130 SHEET 4 AC9 4 VAL M 159 TRP M 163 -1 N SER M 162 O SER M 176 SHEET 1 AD1 4 SER M 153 ARG M 155 0 SHEET 2 AD1 4 ASN M 145 ILE M 150 -1 N ILE M 150 O SER M 153 SHEET 3 AD1 4 SER M 191 THR M 197 -1 O GLU M 195 N LYS M 147 SHEET 4 AD1 4 ILE M 205 ASN M 210 -1 O ILE M 205 N ALA M 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 139 CYS H 194 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 5 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 6 CYS I 139 CYS I 194 1555 1555 2.03 SSBOND 7 CYS M 23 CYS M 88 1555 1555 2.04 SSBOND 8 CYS M 134 CYS M 194 1555 1555 2.03 CISPEP 1 PHE H 145 PRO H 146 0 -5.94 CISPEP 2 GLU H 147 PRO H 148 0 3.58 CISPEP 3 TRP H 187 PRO H 188 0 7.38 CISPEP 4 THR L 7 PRO L 8 0 -6.15 CISPEP 5 TYR L 140 PRO L 141 0 2.34 CISPEP 6 PHE I 145 PRO I 146 0 -6.03 CISPEP 7 GLU I 147 PRO I 148 0 1.26 CISPEP 8 TRP I 187 PRO I 188 0 6.67 CISPEP 9 THR M 7 PRO M 8 0 -4.16 CISPEP 10 TYR M 140 PRO M 141 0 2.93 CRYST1 117.254 239.246 68.945 90.00 90.00 90.00 P 21 21 2 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 0.008528 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004180 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014504 0.00000