HEADER APOPTOSIS 25-FEB-15 5AJK
TITLE CRYSTAL STRUCTURE OF VARIOLA VIRUS VIRULENCE FACTOR F1L IN COMPLEX
TITLE 2 WITH HUMAN BAK BH3 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOLOG OF VACCINIA VIRUS CDS F1L;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 FRAGMENT: RESIDUES 39-201;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BCL-2 HOMOLOGOUS ANTAGONIST/KILLER;
COMPND 8 CHAIN: B, D, F, H, J, L;
COMPND 9 FRAGMENT: RESIDUES 67-92;
COMPND 10 SYNONYM: APOPTOSIS REGULATOR BAK, BCL-2-LIKE PROTEIN 7, BCL2-L-7;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VARIOLA VIRUS;
SOURCE 3 ORGANISM_COMMON: SMALLPOX;
SOURCE 4 ORGANISM_TAXID: 10255;
SOURCE 5 STRAIN: BANGLADESH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P3;
SOURCE 11 OTHER_DETAILS: SYNTHETIC CDNA;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS BCL-2, APOPTOSIS, POXVIRUS, BID
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KVANSAKUL,P.M.COLMAN
REVDAT 3 10-JAN-24 5AJK 1 REMARK
REVDAT 2 08-APR-15 5AJK 1 ATOM MASTER
REVDAT 1 25-MAR-15 5AJK 0
JRNL AUTH B.MARSHALL,H.PUTHALAKATH,S.CARIA,S.CHUGH,M.DOERFLINGER,
JRNL AUTH 2 P.M.COLMAN,M.KVANSAKUL
JRNL TITL VARIOLA VIRUS F1L IS A BCL-2-LIKE PROTEIN THAT UNLIKE ITS
JRNL TITL 2 VACCINIA VIRUS COUNTERPART INHIBITS APOPTOSIS INDEPENDENT OF
JRNL TITL 3 BIM.
JRNL REF CELL DEATH DIS. V. 6 E1680 2015
JRNL REFN ISSN 2041-4889
JRNL PMID 25766319
JRNL DOI 10.1038/CDDIS.2015.52
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 44915
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2293
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 39.7067 - 6.4171 0.98 2734 148 0.1700 0.2009
REMARK 3 2 6.4171 - 5.0969 1.00 2715 152 0.2090 0.2544
REMARK 3 3 5.0969 - 4.4536 1.00 2689 138 0.1575 0.2128
REMARK 3 4 4.4536 - 4.0468 1.00 2692 127 0.1548 0.2090
REMARK 3 5 4.0468 - 3.7570 1.00 2668 148 0.1694 0.2081
REMARK 3 6 3.7570 - 3.5356 0.98 2629 155 0.2042 0.2202
REMARK 3 7 3.5356 - 3.3587 1.00 2639 161 0.2125 0.2358
REMARK 3 8 3.3587 - 3.2125 1.00 2672 139 0.2190 0.2769
REMARK 3 9 3.2125 - 3.0889 1.00 2641 144 0.2318 0.2783
REMARK 3 10 3.0889 - 2.9823 1.00 2680 122 0.2361 0.3292
REMARK 3 11 2.9823 - 2.8891 1.00 2670 127 0.2449 0.3052
REMARK 3 12 2.8891 - 2.8066 1.00 2637 158 0.2441 0.2869
REMARK 3 13 2.8066 - 2.7327 1.00 2654 142 0.2478 0.3118
REMARK 3 14 2.7327 - 2.6660 1.00 2637 153 0.2615 0.3243
REMARK 3 15 2.6660 - 2.6054 1.00 2635 118 0.2720 0.3012
REMARK 3 16 2.6054 - 2.5500 1.00 2630 161 0.2789 0.3151
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.860
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 8060
REMARK 3 ANGLE : 0.570 10875
REMARK 3 CHIRALITY : 0.027 1250
REMARK 3 PLANARITY : 0.002 1391
REMARK 3 DIHEDRAL : 12.488 3048
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 31
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9542 28.4318 68.4568
REMARK 3 T TENSOR
REMARK 3 T11: 0.5630 T22: 0.8099
REMARK 3 T33: 0.5424 T12: 0.0596
REMARK 3 T13: 0.1554 T23: -0.1652
REMARK 3 L TENSOR
REMARK 3 L11: 3.6785 L22: 3.8963
REMARK 3 L33: 3.6329 L12: 0.9560
REMARK 3 L13: 1.0077 L23: 0.8764
REMARK 3 S TENSOR
REMARK 3 S11: 0.2486 S12: 0.1481 S13: 0.2319
REMARK 3 S21: 0.2464 S22: -0.6935 S23: 0.6298
REMARK 3 S31: -0.4349 S32: -0.6000 S33: 0.3043
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 66 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9993 30.8404 51.8023
REMARK 3 T TENSOR
REMARK 3 T11: 0.3886 T22: 0.4131
REMARK 3 T33: 0.4404 T12: -0.0356
REMARK 3 T13: 0.0155 T23: -0.0634
REMARK 3 L TENSOR
REMARK 3 L11: 3.8480 L22: 5.6051
REMARK 3 L33: 2.6820 L12: -0.7541
REMARK 3 L13: -0.0046 L23: 1.7055
REMARK 3 S TENSOR
REMARK 3 S11: -0.1068 S12: 0.2315 S13: -0.3111
REMARK 3 S21: 0.0202 S22: -0.1557 S23: 0.7095
REMARK 3 S31: 0.1809 S32: -0.3937 S33: 0.2207
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6742 11.8191 38.3010
REMARK 3 T TENSOR
REMARK 3 T11: 0.4762 T22: 0.4604
REMARK 3 T33: 0.5501 T12: 0.0420
REMARK 3 T13: 0.0379 T23: -0.1298
REMARK 3 L TENSOR
REMARK 3 L11: 6.5793 L22: 1.4221
REMARK 3 L33: 1.0136 L12: 1.5956
REMARK 3 L13: 0.3565 L23: -0.5517
REMARK 3 S TENSOR
REMARK 3 S11: 0.4816 S12: 1.0812 S13: -0.1457
REMARK 3 S21: -0.0627 S22: -0.0436 S23: 0.1324
REMARK 3 S31: 0.0951 S32: 0.2991 S33: -0.2171
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6607 9.8906 47.3791
REMARK 3 T TENSOR
REMARK 3 T11: 0.4903 T22: 0.6730
REMARK 3 T33: 0.7113 T12: 0.0068
REMARK 3 T13: -0.0034 T23: -0.1527
REMARK 3 L TENSOR
REMARK 3 L11: 4.0712 L22: 4.3795
REMARK 3 L33: 6.3417 L12: -0.1468
REMARK 3 L13: -1.1719 L23: 3.1297
REMARK 3 S TENSOR
REMARK 3 S11: -0.1162 S12: -0.3788 S13: 0.9741
REMARK 3 S21: -0.1187 S22: -0.4035 S23: 0.8594
REMARK 3 S31: -1.0113 S32: -0.6147 S33: 0.2488
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 133 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9830 3.9732 58.2420
REMARK 3 T TENSOR
REMARK 3 T11: 0.9101 T22: 0.8185
REMARK 3 T33: 0.5233 T12: -0.1036
REMARK 3 T13: -0.0164 T23: 0.0549
REMARK 3 L TENSOR
REMARK 3 L11: 0.3215 L22: 1.2699
REMARK 3 L33: 1.3930 L12: 0.1378
REMARK 3 L13: 0.0028 L23: 0.8575
REMARK 3 S TENSOR
REMARK 3 S11: 0.1510 S12: -1.1485 S13: -0.1480
REMARK 3 S21: 1.3295 S22: 0.0406 S23: -0.0640
REMARK 3 S31: -0.2145 S32: -0.6382 S33: 0.2615
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 201 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9255 7.8989 49.2044
REMARK 3 T TENSOR
REMARK 3 T11: 0.3403 T22: 0.3408
REMARK 3 T33: 0.4372 T12: -0.0128
REMARK 3 T13: -0.0691 T23: -0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 2.7002 L22: 4.4484
REMARK 3 L33: 3.6249 L12: 0.7495
REMARK 3 L13: -0.0628 L23: 1.3899
REMARK 3 S TENSOR
REMARK 3 S11: 0.2361 S12: -0.0082 S13: -0.4064
REMARK 3 S21: 0.0478 S22: -0.0255 S23: -0.2089
REMARK 3 S31: 0.3687 S32: 0.0462 S33: -0.2703
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 68 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3372 0.0050 44.1776
REMARK 3 T TENSOR
REMARK 3 T11: 0.5717 T22: 0.3755
REMARK 3 T33: 0.5690 T12: -0.0355
REMARK 3 T13: -0.0404 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 8.0065 L22: 5.7113
REMARK 3 L33: 3.1594 L12: -1.0772
REMARK 3 L13: -2.1702 L23: 1.2590
REMARK 3 S TENSOR
REMARK 3 S11: 0.1881 S12: -0.3582 S13: -1.2615
REMARK 3 S21: 0.0649 S22: -0.7207 S23: 0.2017
REMARK 3 S31: 0.3057 S32: -0.5779 S33: 0.3299
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 63 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2632 16.7081 47.8329
REMARK 3 T TENSOR
REMARK 3 T11: 0.4005 T22: 0.5004
REMARK 3 T33: 0.5486 T12: -0.0340
REMARK 3 T13: 0.0408 T23: -0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 2.6134 L22: 4.4918
REMARK 3 L33: 2.1200 L12: -0.5775
REMARK 3 L13: 0.4813 L23: 1.0506
REMARK 3 S TENSOR
REMARK 3 S11: 0.2395 S12: -0.2781 S13: 0.0351
REMARK 3 S21: -0.2129 S22: 0.0536 S23: -0.4256
REMARK 3 S31: 0.0555 S32: 0.3504 S33: -0.1831
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 97 THROUGH 201 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7533 36.5394 58.5890
REMARK 3 T TENSOR
REMARK 3 T11: 0.3840 T22: 0.4195
REMARK 3 T33: 0.4722 T12: -0.0421
REMARK 3 T13: 0.0418 T23: -0.0827
REMARK 3 L TENSOR
REMARK 3 L11: 2.4874 L22: 1.9178
REMARK 3 L33: 2.3966 L12: 0.6905
REMARK 3 L13: 0.2386 L23: 0.4007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: -0.2362 S13: 0.0502
REMARK 3 S21: 0.0058 S22: -0.0728 S23: 0.0269
REMARK 3 S31: -0.1185 S32: 0.2500 S33: 0.0024
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 68 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4826 44.8674 63.1522
REMARK 3 T TENSOR
REMARK 3 T11: 0.4855 T22: 0.5952
REMARK 3 T33: 0.6106 T12: -0.1346
REMARK 3 T13: 0.0576 T23: -0.1358
REMARK 3 L TENSOR
REMARK 3 L11: 7.9157 L22: 9.2310
REMARK 3 L33: 8.5341 L12: -3.9731
REMARK 3 L13: 3.8751 L23: -6.1324
REMARK 3 S TENSOR
REMARK 3 S11: -0.1966 S12: -0.3914 S13: 0.8424
REMARK 3 S21: 0.4633 S22: -0.2770 S23: -1.1400
REMARK 3 S31: -0.3697 S32: -0.0366 S33: 0.4031
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 47 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6308 25.5838 45.3083
REMARK 3 T TENSOR
REMARK 3 T11: 0.5992 T22: 1.5769
REMARK 3 T33: 0.9687 T12: 0.0701
REMARK 3 T13: 0.0360 T23: 0.1186
REMARK 3 L TENSOR
REMARK 3 L11: 3.9195 L22: 3.6601
REMARK 3 L33: 2.5956 L12: 0.2206
REMARK 3 L13: 0.9189 L23: 0.3621
REMARK 3 S TENSOR
REMARK 3 S11: 0.2268 S12: 2.0185 S13: 0.2183
REMARK 3 S21: -0.6280 S22: -0.5272 S23: -0.2302
REMARK 3 S31: -0.0896 S32: 0.9301 S33: 0.4681
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 73 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.4897 33.5025 64.3664
REMARK 3 T TENSOR
REMARK 3 T11: 0.4485 T22: 0.6662
REMARK 3 T33: 0.5868 T12: 0.0180
REMARK 3 T13: -0.0084 T23: 0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 2.9080 L22: 1.1875
REMARK 3 L33: 2.8309 L12: -0.8494
REMARK 3 L13: 2.1556 L23: -0.8953
REMARK 3 S TENSOR
REMARK 3 S11: -0.3065 S12: 0.2755 S13: 0.3517
REMARK 3 S21: 0.0706 S22: -0.0928 S23: -0.0172
REMARK 3 S31: -0.2119 S32: 0.1695 S33: 0.3689
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 119 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.3069 20.5837 70.7574
REMARK 3 T TENSOR
REMARK 3 T11: 0.4817 T22: 0.8848
REMARK 3 T33: 0.5027 T12: -0.0325
REMARK 3 T13: 0.0508 T23: -0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 4.7988 L22: 0.7876
REMARK 3 L33: 5.5773 L12: 0.1685
REMARK 3 L13: 1.4581 L23: -1.0905
REMARK 3 S TENSOR
REMARK 3 S11: -0.3866 S12: 0.4870 S13: 0.0017
REMARK 3 S21: -0.2548 S22: 0.2629 S23: -0.0067
REMARK 3 S31: -0.4478 S32: 1.3411 S33: 0.0056
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 137 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.9419 11.3316 70.8868
REMARK 3 T TENSOR
REMARK 3 T11: 0.6244 T22: 0.7917
REMARK 3 T33: 0.6648 T12: 0.0558
REMARK 3 T13: -0.0289 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 1.3510 L22: 2.0698
REMARK 3 L33: 6.1057 L12: -0.9888
REMARK 3 L13: 0.6929 L23: 1.9809
REMARK 3 S TENSOR
REMARK 3 S11: -0.0645 S12: 0.1008 S13: -1.1584
REMARK 3 S21: 0.1788 S22: 0.0826 S23: -0.1349
REMARK 3 S31: 0.8923 S32: 0.8885 S33: -0.1460
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 149 THROUGH 201 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.5366 20.8217 72.6427
REMARK 3 T TENSOR
REMARK 3 T11: 0.3334 T22: 0.5845
REMARK 3 T33: 0.3406 T12: 0.0037
REMARK 3 T13: -0.0216 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 3.9178 L22: 3.3421
REMARK 3 L33: 5.0789 L12: -0.9444
REMARK 3 L13: 1.1628 L23: -1.0546
REMARK 3 S TENSOR
REMARK 3 S11: 0.0312 S12: -0.2346 S13: -0.3414
REMARK 3 S21: 0.0829 S22: -0.1190 S23: 0.1054
REMARK 3 S31: 0.1606 S32: 0.2025 S33: -0.0025
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 68 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5685 18.9520 81.6742
REMARK 3 T TENSOR
REMARK 3 T11: 0.4254 T22: 0.7781
REMARK 3 T33: 0.4676 T12: 0.0671
REMARK 3 T13: -0.0496 T23: 0.1302
REMARK 3 L TENSOR
REMARK 3 L11: 6.2737 L22: 5.4721
REMARK 3 L33: 7.7143 L12: -2.6142
REMARK 3 L13: -3.4909 L23: 3.6408
REMARK 3 S TENSOR
REMARK 3 S11: -0.4043 S12: -1.0286 S13: -0.6488
REMARK 3 S21: 0.1296 S22: 0.4055 S23: 0.4276
REMARK 3 S31: 0.4004 S32: 1.4608 S33: -0.1045
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 64 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0837 37.8484 30.1540
REMARK 3 T TENSOR
REMARK 3 T11: 0.5221 T22: 0.5042
REMARK 3 T33: 0.5852 T12: 0.0885
REMARK 3 T13: 0.1060 T23: 0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 4.3042 L22: 4.8398
REMARK 3 L33: 2.6894 L12: -0.1258
REMARK 3 L13: -0.2879 L23: 0.3392
REMARK 3 S TENSOR
REMARK 3 S11: 0.2782 S12: 0.5475 S13: 0.5676
REMARK 3 S21: -0.1028 S22: -0.0218 S23: -0.5409
REMARK 3 S31: -0.1946 S32: 0.5570 S33: -0.1983
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 97 THROUGH 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8880 16.0471 25.8516
REMARK 3 T TENSOR
REMARK 3 T11: 0.5089 T22: 0.4849
REMARK 3 T33: 0.4684 T12: 0.0802
REMARK 3 T13: 0.0364 T23: -0.1079
REMARK 3 L TENSOR
REMARK 3 L11: 4.8603 L22: 2.8912
REMARK 3 L33: 2.4212 L12: -1.5397
REMARK 3 L13: -0.4528 L23: -0.9185
REMARK 3 S TENSOR
REMARK 3 S11: -0.0393 S12: -0.6949 S13: -0.3461
REMARK 3 S21: -0.0367 S22: -0.1894 S23: -0.1366
REMARK 3 S31: 0.0093 S32: 0.2133 S33: 0.1724
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 133 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6233 21.0363 8.6410
REMARK 3 T TENSOR
REMARK 3 T11: 0.9290 T22: 0.9635
REMARK 3 T33: 0.6044 T12: 0.2899
REMARK 3 T13: 0.0839 T23: 0.1205
REMARK 3 L TENSOR
REMARK 3 L11: 1.5304 L22: 0.8671
REMARK 3 L33: 1.5303 L12: 0.8577
REMARK 3 L13: 0.7120 L23: 0.5323
REMARK 3 S TENSOR
REMARK 3 S11: -0.0470 S12: 1.7805 S13: 0.1368
REMARK 3 S21: -0.8369 S22: 0.4791 S23: -0.1826
REMARK 3 S31: 0.1064 S32: 0.7880 S33: -0.0245
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 150 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6442 18.4921 17.9101
REMARK 3 T TENSOR
REMARK 3 T11: 0.5805 T22: 0.4295
REMARK 3 T33: 0.5105 T12: 0.1832
REMARK 3 T13: 0.0330 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 3.1802 L22: 5.7833
REMARK 3 L33: 3.5348 L12: -0.4928
REMARK 3 L13: -1.0784 L23: -0.3995
REMARK 3 S TENSOR
REMARK 3 S11: 0.1223 S12: 0.5690 S13: -0.0335
REMARK 3 S21: -0.7065 S22: -0.0516 S23: 0.1134
REMARK 3 S31: -0.0379 S32: -0.1711 S33: 0.0534
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 68 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5629 9.0325 16.7235
REMARK 3 T TENSOR
REMARK 3 T11: 0.5703 T22: 0.5656
REMARK 3 T33: 0.4515 T12: 0.2039
REMARK 3 T13: 0.0961 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 7.3721 L22: 9.2509
REMARK 3 L33: 7.0434 L12: 2.6811
REMARK 3 L13: -1.3146 L23: -3.6249
REMARK 3 S TENSOR
REMARK 3 S11: 0.0190 S12: -0.0555 S13: -0.5739
REMARK 3 S21: -0.3875 S22: -0.3788 S23: -0.7217
REMARK 3 S31: 0.2465 S32: 0.3552 S33: -0.1524
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 65 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2676 24.1203 24.5754
REMARK 3 T TENSOR
REMARK 3 T11: 0.5538 T22: 0.5657
REMARK 3 T33: 0.6833 T12: 0.1198
REMARK 3 T13: -0.0263 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 2.2779 L22: 4.4012
REMARK 3 L33: 3.5186 L12: 0.1801
REMARK 3 L13: -0.0785 L23: 2.4032
REMARK 3 S TENSOR
REMARK 3 S11: 0.1733 S12: -0.0039 S13: 0.5118
REMARK 3 S21: -0.3919 S22: -0.5998 S23: 0.7605
REMARK 3 S31: -0.1540 S32: -0.6521 S33: 0.3085
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 97 THROUGH 131 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9936 43.8832 34.2228
REMARK 3 T TENSOR
REMARK 3 T11: 0.6418 T22: 0.3023
REMARK 3 T33: 0.7759 T12: 0.0292
REMARK 3 T13: -0.0311 T23: 0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 4.7000 L22: 2.8149
REMARK 3 L33: 3.4565 L12: -0.2610
REMARK 3 L13: -0.4818 L23: 0.4713
REMARK 3 S TENSOR
REMARK 3 S11: 0.1501 S12: -0.6704 S13: 0.1777
REMARK 3 S21: -0.1634 S22: -0.0053 S23: 0.6668
REMARK 3 S31: -0.2931 S32: -0.5570 S33: -0.2019
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 132 THROUGH 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3219 52.3520 19.1551
REMARK 3 T TENSOR
REMARK 3 T11: 1.1374 T22: 0.6197
REMARK 3 T33: 0.6608 T12: 0.2581
REMARK 3 T13: 0.1375 T23: 0.2343
REMARK 3 L TENSOR
REMARK 3 L11: 3.8802 L22: 2.2614
REMARK 3 L33: 3.1350 L12: 1.2549
REMARK 3 L13: 0.4047 L23: 0.9858
REMARK 3 S TENSOR
REMARK 3 S11: 0.5563 S12: 0.8911 S13: 0.8884
REMARK 3 S21: -0.8317 S22: 0.0014 S23: 0.1529
REMARK 3 S31: -0.5385 S32: -0.4786 S33: 0.0552
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 154 THROUGH 201 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0635 45.9224 27.3833
REMARK 3 T TENSOR
REMARK 3 T11: 0.6951 T22: 0.4229
REMARK 3 T33: 0.6166 T12: 0.1384
REMARK 3 T13: 0.0825 T23: 0.1082
REMARK 3 L TENSOR
REMARK 3 L11: 4.2996 L22: 3.8423
REMARK 3 L33: 5.5670 L12: -1.6771
REMARK 3 L13: -0.3515 L23: 1.8271
REMARK 3 S TENSOR
REMARK 3 S11: 0.4099 S12: 0.1894 S13: 0.3664
REMARK 3 S21: -0.8062 S22: -0.3228 S23: -0.0267
REMARK 3 S31: -0.7422 S32: -0.0716 S33: -0.1593
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 68 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8498 55.1779 29.8979
REMARK 3 T TENSOR
REMARK 3 T11: 0.9593 T22: 0.6623
REMARK 3 T33: 1.3232 T12: 0.1902
REMARK 3 T13: 0.0355 T23: -0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 3.1410 L22: 5.2709
REMARK 3 L33: 5.3259 L12: 1.5007
REMARK 3 L13: -1.0161 L23: 0.5508
REMARK 3 S TENSOR
REMARK 3 S11: 0.8402 S12: 0.0097 S13: 0.6876
REMARK 3 S21: 0.0168 S22: -0.4525 S23: 0.6806
REMARK 3 S31: 0.5777 S32: -0.6225 S33: -0.1560
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 64 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.4228 24.5085 65.2951
REMARK 3 T TENSOR
REMARK 3 T11: 0.7312 T22: 1.3161
REMARK 3 T33: 0.9980 T12: 0.0849
REMARK 3 T13: -0.0211 T23: 0.1720
REMARK 3 L TENSOR
REMARK 3 L11: 0.3922 L22: 0.0846
REMARK 3 L33: 8.9458 L12: -0.0829
REMARK 3 L13: 1.5146 L23: -0.7817
REMARK 3 S TENSOR
REMARK 3 S11: -0.0445 S12: 0.1293 S13: 0.0921
REMARK 3 S21: -0.3729 S22: -0.0198 S23: 0.5599
REMARK 3 S31: 1.0174 S32: -0.9452 S33: -0.1973
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 73 THROUGH 131 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.2041 35.3477 55.9687
REMARK 3 T TENSOR
REMARK 3 T11: 0.5242 T22: 0.6416
REMARK 3 T33: 0.5840 T12: -0.0688
REMARK 3 T13: -0.0606 T23: 0.1370
REMARK 3 L TENSOR
REMARK 3 L11: 3.2886 L22: 0.2476
REMARK 3 L33: 3.6552 L12: -0.9179
REMARK 3 L13: 2.9592 L23: -1.1495
REMARK 3 S TENSOR
REMARK 3 S11: -0.2646 S12: 0.4117 S13: 0.7492
REMARK 3 S21: 0.1084 S22: -0.1866 S23: -0.0005
REMARK 3 S31: -0.5515 S32: 0.4405 S33: 0.2227
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 132 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.2260 22.8332 40.2610
REMARK 3 T TENSOR
REMARK 3 T11: 0.7658 T22: 1.1501
REMARK 3 T33: 0.8257 T12: 0.3606
REMARK 3 T13: -0.2026 T23: -0.2227
REMARK 3 L TENSOR
REMARK 3 L11: 2.5276 L22: 3.6552
REMARK 3 L33: 1.4892 L12: -1.5406
REMARK 3 L13: -0.0283 L23: -0.8402
REMARK 3 S TENSOR
REMARK 3 S11: 0.9722 S12: 1.6910 S13: -1.5102
REMARK 3 S21: -0.8676 S22: -0.7642 S23: 0.7546
REMARK 3 S31: 1.3811 S32: 0.8322 S33: -0.3453
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 149 THROUGH 201 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4201 32.6064 44.0864
REMARK 3 T TENSOR
REMARK 3 T11: 0.3794 T22: 1.1383
REMARK 3 T33: 0.5767 T12: 0.0749
REMARK 3 T13: -0.0214 T23: 0.3134
REMARK 3 L TENSOR
REMARK 3 L11: 2.7615 L22: 2.1905
REMARK 3 L33: 3.1175 L12: -0.2853
REMARK 3 L13: 1.5775 L23: -0.4635
REMARK 3 S TENSOR
REMARK 3 S11: 0.0955 S12: 1.8564 S13: 0.6355
REMARK 3 S21: -0.3792 S22: -0.3261 S23: -0.2924
REMARK 3 S31: 0.2085 S32: 0.8953 S33: 0.1160
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 69 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.4470 37.4916 36.0921
REMARK 3 T TENSOR
REMARK 3 T11: 0.4284 T22: 1.4107
REMARK 3 T33: 0.5808 T12: -0.0240
REMARK 3 T13: -0.0545 T23: 0.3657
REMARK 3 L TENSOR
REMARK 3 L11: 3.4615 L22: 3.5752
REMARK 3 L33: 4.4984 L12: -0.3047
REMARK 3 L13: 0.3480 L23: -0.3110
REMARK 3 S TENSOR
REMARK 3 S11: -0.3735 S12: 1.4935 S13: 0.6938
REMARK 3 S21: -0.6407 S22: 0.3314 S23: -0.4982
REMARK 3 S31: -0.1187 S32: 1.5286 S33: 0.0274
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 5AJK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1290063138.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.975
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45043
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.66000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 4D2M
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M MGSO4, 0.1 M NA-ACETATE PH 5.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.84554
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.38100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.91263
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.84554
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.38100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 80.91263
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, K, 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLY A 34
REMARK 465 PRO A 35
REMARK 465 LEU A 36
REMARK 465 GLY A 37
REMARK 465 SER A 38
REMARK 465 LYS A 39
REMARK 465 ALA A 40
REMARK 465 SER A 41
REMARK 465 ASN A 42
REMARK 465 ASN A 43
REMARK 465 ASP A 44
REMARK 465 ASP A 45
REMARK 465 ASN A 55
REMARK 465 MET A 56
REMARK 465 VAL A 57
REMARK 465 TYR A 58
REMARK 465 ARG A 59
REMARK 465 PHE A 60
REMARK 465 ASN A 61
REMARK 465 LYS A 62
REMARK 465 PRO B 67
REMARK 465 SER B 91
REMARK 465 GLU B 92
REMARK 465 GLY C 34
REMARK 465 PRO C 35
REMARK 465 LEU C 36
REMARK 465 GLY C 37
REMARK 465 SER C 38
REMARK 465 LYS C 39
REMARK 465 ALA C 40
REMARK 465 SER C 41
REMARK 465 ASN C 42
REMARK 465 ASN C 43
REMARK 465 ASP C 44
REMARK 465 ASP C 45
REMARK 465 HIS C 46
REMARK 465 ASN C 47
REMARK 465 TYR C 48
REMARK 465 VAL C 49
REMARK 465 TYR C 50
REMARK 465 PRO C 51
REMARK 465 LEU C 52
REMARK 465 PRO C 53
REMARK 465 GLU C 54
REMARK 465 ASN C 55
REMARK 465 MET C 56
REMARK 465 VAL C 57
REMARK 465 TYR C 58
REMARK 465 ARG C 59
REMARK 465 PHE C 60
REMARK 465 ASN C 61
REMARK 465 LYS C 62
REMARK 465 PRO D 67
REMARK 465 SER D 91
REMARK 465 GLU D 92
REMARK 465 GLY E 34
REMARK 465 PRO E 35
REMARK 465 LEU E 36
REMARK 465 GLY E 37
REMARK 465 SER E 38
REMARK 465 LYS E 39
REMARK 465 ALA E 40
REMARK 465 SER E 41
REMARK 465 ASN E 42
REMARK 465 ASN E 43
REMARK 465 ASP E 44
REMARK 465 ASP E 45
REMARK 465 HIS E 46
REMARK 465 LEU E 52
REMARK 465 PRO E 53
REMARK 465 GLU E 54
REMARK 465 ASN E 55
REMARK 465 MET E 56
REMARK 465 VAL E 57
REMARK 465 TYR E 58
REMARK 465 ARG E 59
REMARK 465 PHE E 60
REMARK 465 ASN E 61
REMARK 465 LYS E 62
REMARK 465 SER E 63
REMARK 465 THR E 64
REMARK 465 ASN E 65
REMARK 465 PRO F 67
REMARK 465 SER F 91
REMARK 465 GLU F 92
REMARK 465 GLY G 34
REMARK 465 PRO G 35
REMARK 465 LEU G 36
REMARK 465 GLY G 37
REMARK 465 SER G 38
REMARK 465 LYS G 39
REMARK 465 ALA G 40
REMARK 465 SER G 41
REMARK 465 ASN G 42
REMARK 465 ASN G 43
REMARK 465 ASP G 44
REMARK 465 ASP G 45
REMARK 465 HIS G 46
REMARK 465 ASN G 47
REMARK 465 TYR G 48
REMARK 465 VAL G 49
REMARK 465 TYR G 50
REMARK 465 PRO G 51
REMARK 465 LEU G 52
REMARK 465 PRO G 53
REMARK 465 GLU G 54
REMARK 465 ASN G 55
REMARK 465 MET G 56
REMARK 465 VAL G 57
REMARK 465 TYR G 58
REMARK 465 ARG G 59
REMARK 465 PHE G 60
REMARK 465 ASN G 61
REMARK 465 LYS G 62
REMARK 465 SER G 63
REMARK 465 SER G 201
REMARK 465 PRO H 67
REMARK 465 SER H 91
REMARK 465 GLU H 92
REMARK 465 GLY I 34
REMARK 465 PRO I 35
REMARK 465 LEU I 36
REMARK 465 GLY I 37
REMARK 465 SER I 38
REMARK 465 LYS I 39
REMARK 465 ALA I 40
REMARK 465 SER I 41
REMARK 465 ASN I 42
REMARK 465 ASN I 43
REMARK 465 ASP I 44
REMARK 465 ASP I 45
REMARK 465 HIS I 46
REMARK 465 ASN I 47
REMARK 465 TYR I 48
REMARK 465 VAL I 49
REMARK 465 TYR I 50
REMARK 465 PRO I 51
REMARK 465 LEU I 52
REMARK 465 PRO I 53
REMARK 465 GLU I 54
REMARK 465 ASN I 55
REMARK 465 MET I 56
REMARK 465 VAL I 57
REMARK 465 TYR I 58
REMARK 465 ARG I 59
REMARK 465 PHE I 60
REMARK 465 ASN I 61
REMARK 465 LYS I 62
REMARK 465 SER I 63
REMARK 465 THR I 64
REMARK 465 PRO J 67
REMARK 465 GLU J 92
REMARK 465 GLY K 34
REMARK 465 PRO K 35
REMARK 465 LEU K 36
REMARK 465 GLY K 37
REMARK 465 SER K 38
REMARK 465 LYS K 39
REMARK 465 ALA K 40
REMARK 465 SER K 41
REMARK 465 ASN K 42
REMARK 465 ASN K 43
REMARK 465 ASP K 44
REMARK 465 ASP K 45
REMARK 465 HIS K 46
REMARK 465 ASN K 47
REMARK 465 TYR K 48
REMARK 465 VAL K 49
REMARK 465 TYR K 50
REMARK 465 PRO K 51
REMARK 465 LEU K 52
REMARK 465 PRO K 53
REMARK 465 GLU K 54
REMARK 465 ASN K 55
REMARK 465 MET K 56
REMARK 465 VAL K 57
REMARK 465 TYR K 58
REMARK 465 ARG K 59
REMARK 465 PHE K 60
REMARK 465 ASN K 61
REMARK 465 LYS K 62
REMARK 465 SER K 63
REMARK 465 PRO L 67
REMARK 465 SER L 68
REMARK 465 SER L 91
REMARK 465 GLU L 92
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 54 CG CD OE1 OE2
REMARK 470 TYR D 89 CG CD1 CD2 CE1 CE2 CZ OH
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 ASN A 47 -160.74 -76.82
REMARK 500 ASN A 151 104.18 -160.01
REMARK 500 SER C 71 -72.91 -94.63
REMARK 500 LEU I 70 59.53 -111.85
REMARK 500 SER K 71 -70.17 -96.31
REMARK 500 ASP K 150 -56.39 -120.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A3007 DISTANCE = 7.76 ANGSTROMS
REMARK 525 HOH G3003 DISTANCE = 8.78 ANGSTROMS
REMARK 525 HOH G3005 DISTANCE = 9.59 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT G 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AJJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VARIOLA VIRUS VIRULENCE FACTOR F1L IN COMPLEX
REMARK 900 WITH HUMAN BID BH3 DOMAIN
DBREF 5AJK A 39 201 UNP Q85365 Q85365_VARV 39 201
DBREF 5AJK B 67 92 UNP Q16611 BAK_HUMAN 67 92
DBREF 5AJK C 39 201 UNP Q85365 Q85365_VARV 39 201
DBREF 5AJK D 67 92 UNP Q16611 BAK_HUMAN 67 92
DBREF 5AJK E 39 201 UNP Q85365 Q85365_VARV 39 201
DBREF 5AJK F 67 92 UNP Q16611 BAK_HUMAN 67 92
DBREF 5AJK G 39 201 UNP Q85365 Q85365_VARV 39 201
DBREF 5AJK H 67 92 UNP Q16611 BAK_HUMAN 67 92
DBREF 5AJK I 39 201 UNP Q85365 Q85365_VARV 39 201
DBREF 5AJK J 67 92 UNP Q16611 BAK_HUMAN 67 92
DBREF 5AJK K 39 201 UNP Q85365 Q85365_VARV 39 201
DBREF 5AJK L 67 92 UNP Q16611 BAK_HUMAN 67 92
SEQADV 5AJK GLY A 34 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK PRO A 35 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK LEU A 36 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY A 37 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK SER A 38 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY C 34 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK PRO C 35 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK LEU C 36 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY C 37 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK SER C 38 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY E 34 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK PRO E 35 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK LEU E 36 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY E 37 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK SER E 38 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY G 34 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK PRO G 35 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK LEU G 36 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY G 37 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK SER G 38 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY I 34 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK PRO I 35 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK LEU I 36 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY I 37 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK SER I 38 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY K 34 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK PRO K 35 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK LEU K 36 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK GLY K 37 UNP Q85365 EXPRESSION TAG
SEQADV 5AJK SER K 38 UNP Q85365 EXPRESSION TAG
SEQRES 1 A 168 GLY PRO LEU GLY SER LYS ALA SER ASN ASN ASP ASP HIS
SEQRES 2 A 168 ASN TYR VAL TYR PRO LEU PRO GLU ASN MET VAL TYR ARG
SEQRES 3 A 168 PHE ASN LYS SER THR ASN ILE LEU ASP TYR LEU SER THR
SEQRES 4 A 168 GLU ARG ASP HIS VAL MET MET ALA VAL GLN TYR TYR MET
SEQRES 5 A 168 SER LYS GLN ARG LEU ASP ASP LEU TYR ARG GLN LEU PRO
SEQRES 6 A 168 THR LYS THR ARG SER TYR ILE ASP ILE ILE ASN MET TYR
SEQRES 7 A 168 CYS ASP LYS VAL ASN ASN ASP TYR ASN ARG ASP MET ASN
SEQRES 8 A 168 ILE MET TYR ASP MET ALA SER THR GLU SER PHE THR VAL
SEQRES 9 A 168 TYR ASP ILE ASN ASN GLU VAL ASN THR ILE LEU MET ASP
SEQRES 10 A 168 ASN LYS GLY LEU GLY VAL ARG LEU ALA THR ILE SER PHE
SEQRES 11 A 168 ILE THR GLU LEU GLY LYS ARG CYS MET ASN PRO VAL GLU
SEQRES 12 A 168 THR ILE LYS MET PHE THR LEU LEU SER HIS THR ILE CYS
SEQRES 13 A 168 ASP ASP CYS PHE ILE ASP TYR ILE THR ASP ILE SER
SEQRES 1 B 26 PRO SER SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA
SEQRES 2 B 26 ILE ILE GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU
SEQRES 1 C 168 GLY PRO LEU GLY SER LYS ALA SER ASN ASN ASP ASP HIS
SEQRES 2 C 168 ASN TYR VAL TYR PRO LEU PRO GLU ASN MET VAL TYR ARG
SEQRES 3 C 168 PHE ASN LYS SER THR ASN ILE LEU ASP TYR LEU SER THR
SEQRES 4 C 168 GLU ARG ASP HIS VAL MET MET ALA VAL GLN TYR TYR MET
SEQRES 5 C 168 SER LYS GLN ARG LEU ASP ASP LEU TYR ARG GLN LEU PRO
SEQRES 6 C 168 THR LYS THR ARG SER TYR ILE ASP ILE ILE ASN MET TYR
SEQRES 7 C 168 CYS ASP LYS VAL ASN ASN ASP TYR ASN ARG ASP MET ASN
SEQRES 8 C 168 ILE MET TYR ASP MET ALA SER THR GLU SER PHE THR VAL
SEQRES 9 C 168 TYR ASP ILE ASN ASN GLU VAL ASN THR ILE LEU MET ASP
SEQRES 10 C 168 ASN LYS GLY LEU GLY VAL ARG LEU ALA THR ILE SER PHE
SEQRES 11 C 168 ILE THR GLU LEU GLY LYS ARG CYS MET ASN PRO VAL GLU
SEQRES 12 C 168 THR ILE LYS MET PHE THR LEU LEU SER HIS THR ILE CYS
SEQRES 13 C 168 ASP ASP CYS PHE ILE ASP TYR ILE THR ASP ILE SER
SEQRES 1 D 26 PRO SER SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA
SEQRES 2 D 26 ILE ILE GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU
SEQRES 1 E 168 GLY PRO LEU GLY SER LYS ALA SER ASN ASN ASP ASP HIS
SEQRES 2 E 168 ASN TYR VAL TYR PRO LEU PRO GLU ASN MET VAL TYR ARG
SEQRES 3 E 168 PHE ASN LYS SER THR ASN ILE LEU ASP TYR LEU SER THR
SEQRES 4 E 168 GLU ARG ASP HIS VAL MET MET ALA VAL GLN TYR TYR MET
SEQRES 5 E 168 SER LYS GLN ARG LEU ASP ASP LEU TYR ARG GLN LEU PRO
SEQRES 6 E 168 THR LYS THR ARG SER TYR ILE ASP ILE ILE ASN MET TYR
SEQRES 7 E 168 CYS ASP LYS VAL ASN ASN ASP TYR ASN ARG ASP MET ASN
SEQRES 8 E 168 ILE MET TYR ASP MET ALA SER THR GLU SER PHE THR VAL
SEQRES 9 E 168 TYR ASP ILE ASN ASN GLU VAL ASN THR ILE LEU MET ASP
SEQRES 10 E 168 ASN LYS GLY LEU GLY VAL ARG LEU ALA THR ILE SER PHE
SEQRES 11 E 168 ILE THR GLU LEU GLY LYS ARG CYS MET ASN PRO VAL GLU
SEQRES 12 E 168 THR ILE LYS MET PHE THR LEU LEU SER HIS THR ILE CYS
SEQRES 13 E 168 ASP ASP CYS PHE ILE ASP TYR ILE THR ASP ILE SER
SEQRES 1 F 26 PRO SER SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA
SEQRES 2 F 26 ILE ILE GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU
SEQRES 1 G 168 GLY PRO LEU GLY SER LYS ALA SER ASN ASN ASP ASP HIS
SEQRES 2 G 168 ASN TYR VAL TYR PRO LEU PRO GLU ASN MET VAL TYR ARG
SEQRES 3 G 168 PHE ASN LYS SER THR ASN ILE LEU ASP TYR LEU SER THR
SEQRES 4 G 168 GLU ARG ASP HIS VAL MET MET ALA VAL GLN TYR TYR MET
SEQRES 5 G 168 SER LYS GLN ARG LEU ASP ASP LEU TYR ARG GLN LEU PRO
SEQRES 6 G 168 THR LYS THR ARG SER TYR ILE ASP ILE ILE ASN MET TYR
SEQRES 7 G 168 CYS ASP LYS VAL ASN ASN ASP TYR ASN ARG ASP MET ASN
SEQRES 8 G 168 ILE MET TYR ASP MET ALA SER THR GLU SER PHE THR VAL
SEQRES 9 G 168 TYR ASP ILE ASN ASN GLU VAL ASN THR ILE LEU MET ASP
SEQRES 10 G 168 ASN LYS GLY LEU GLY VAL ARG LEU ALA THR ILE SER PHE
SEQRES 11 G 168 ILE THR GLU LEU GLY LYS ARG CYS MET ASN PRO VAL GLU
SEQRES 12 G 168 THR ILE LYS MET PHE THR LEU LEU SER HIS THR ILE CYS
SEQRES 13 G 168 ASP ASP CYS PHE ILE ASP TYR ILE THR ASP ILE SER
SEQRES 1 H 26 PRO SER SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA
SEQRES 2 H 26 ILE ILE GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU
SEQRES 1 I 168 GLY PRO LEU GLY SER LYS ALA SER ASN ASN ASP ASP HIS
SEQRES 2 I 168 ASN TYR VAL TYR PRO LEU PRO GLU ASN MET VAL TYR ARG
SEQRES 3 I 168 PHE ASN LYS SER THR ASN ILE LEU ASP TYR LEU SER THR
SEQRES 4 I 168 GLU ARG ASP HIS VAL MET MET ALA VAL GLN TYR TYR MET
SEQRES 5 I 168 SER LYS GLN ARG LEU ASP ASP LEU TYR ARG GLN LEU PRO
SEQRES 6 I 168 THR LYS THR ARG SER TYR ILE ASP ILE ILE ASN MET TYR
SEQRES 7 I 168 CYS ASP LYS VAL ASN ASN ASP TYR ASN ARG ASP MET ASN
SEQRES 8 I 168 ILE MET TYR ASP MET ALA SER THR GLU SER PHE THR VAL
SEQRES 9 I 168 TYR ASP ILE ASN ASN GLU VAL ASN THR ILE LEU MET ASP
SEQRES 10 I 168 ASN LYS GLY LEU GLY VAL ARG LEU ALA THR ILE SER PHE
SEQRES 11 I 168 ILE THR GLU LEU GLY LYS ARG CYS MET ASN PRO VAL GLU
SEQRES 12 I 168 THR ILE LYS MET PHE THR LEU LEU SER HIS THR ILE CYS
SEQRES 13 I 168 ASP ASP CYS PHE ILE ASP TYR ILE THR ASP ILE SER
SEQRES 1 J 26 PRO SER SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA
SEQRES 2 J 26 ILE ILE GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU
SEQRES 1 K 168 GLY PRO LEU GLY SER LYS ALA SER ASN ASN ASP ASP HIS
SEQRES 2 K 168 ASN TYR VAL TYR PRO LEU PRO GLU ASN MET VAL TYR ARG
SEQRES 3 K 168 PHE ASN LYS SER THR ASN ILE LEU ASP TYR LEU SER THR
SEQRES 4 K 168 GLU ARG ASP HIS VAL MET MET ALA VAL GLN TYR TYR MET
SEQRES 5 K 168 SER LYS GLN ARG LEU ASP ASP LEU TYR ARG GLN LEU PRO
SEQRES 6 K 168 THR LYS THR ARG SER TYR ILE ASP ILE ILE ASN MET TYR
SEQRES 7 K 168 CYS ASP LYS VAL ASN ASN ASP TYR ASN ARG ASP MET ASN
SEQRES 8 K 168 ILE MET TYR ASP MET ALA SER THR GLU SER PHE THR VAL
SEQRES 9 K 168 TYR ASP ILE ASN ASN GLU VAL ASN THR ILE LEU MET ASP
SEQRES 10 K 168 ASN LYS GLY LEU GLY VAL ARG LEU ALA THR ILE SER PHE
SEQRES 11 K 168 ILE THR GLU LEU GLY LYS ARG CYS MET ASN PRO VAL GLU
SEQRES 12 K 168 THR ILE LYS MET PHE THR LEU LEU SER HIS THR ILE CYS
SEQRES 13 K 168 ASP ASP CYS PHE ILE ASP TYR ILE THR ASP ILE SER
SEQRES 1 L 26 PRO SER SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA
SEQRES 2 L 26 ILE ILE GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU
HET CL A1202 1
HET CL A1203 1
HET ACT C1202 7
HET ACT E1202 7
HET ACT G1201 7
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
FORMUL 13 CL 2(CL 1-)
FORMUL 15 ACT 3(C2 H3 O2 1-)
FORMUL 18 HOH *98(H2 O)
HELIX 1 1 ASN A 65 LEU A 70 5 6
HELIX 2 2 THR A 72 LEU A 97 1 26
HELIX 3 3 PRO A 98 TYR A 119 1 22
HELIX 4 4 TYR A 119 SER A 131 1 13
HELIX 5 5 THR A 136 ASP A 150 1 15
HELIX 6 6 LEU A 154 CYS A 171 1 18
HELIX 7 7 ASN A 173 CYS A 189 1 17
HELIX 8 8 ASP A 190 SER A 201 1 12
HELIX 9 9 SER B 68 TYR B 89 1 22
HELIX 10 10 ASN C 65 LEU C 70 1 6
HELIX 11 11 THR C 72 LEU C 97 1 26
HELIX 12 12 PRO C 98 TYR C 119 1 22
HELIX 13 13 TYR C 119 SER C 131 1 13
HELIX 14 14 THR C 136 ASN C 151 1 16
HELIX 15 15 GLY C 153 CYS C 171 1 19
HELIX 16 16 ASN C 173 CYS C 189 1 17
HELIX 17 17 ASP C 190 ILE C 200 1 11
HELIX 18 18 SER D 68 TYR D 89 1 22
HELIX 19 19 ILE E 66 LEU E 70 5 5
HELIX 20 20 THR E 72 GLN E 96 1 25
HELIX 21 21 PRO E 98 TYR E 119 1 22
HELIX 22 22 TYR E 119 THR E 132 1 14
HELIX 23 23 THR E 136 ASN E 151 1 16
HELIX 24 24 LEU E 154 CYS E 171 1 18
HELIX 25 25 ASN E 173 CYS E 189 1 17
HELIX 26 26 ASP E 190 SER E 201 1 12
HELIX 27 27 SER F 68 ASP F 90 1 23
HELIX 28 28 ASN G 65 TYR G 69 5 5
HELIX 29 29 THR G 72 LEU G 97 1 26
HELIX 30 30 PRO G 98 TYR G 119 1 22
HELIX 31 31 TYR G 119 SER G 131 1 13
HELIX 32 32 THR G 136 ASP G 150 1 15
HELIX 33 33 GLY G 153 CYS G 171 1 19
HELIX 34 34 ASN G 173 CYS G 189 1 17
HELIX 35 35 ASP G 190 ILE G 200 1 11
HELIX 36 36 SER H 69 ASP H 90 1 22
HELIX 37 37 ASN I 65 LEU I 70 5 6
HELIX 38 38 THR I 72 LEU I 97 1 26
HELIX 39 39 PRO I 98 TYR I 119 1 22
HELIX 40 40 TYR I 119 THR I 132 1 14
HELIX 41 41 THR I 136 ASN I 151 1 16
HELIX 42 42 GLY I 153 CYS I 171 1 19
HELIX 43 43 ASN I 173 CYS I 189 1 17
HELIX 44 44 ASP I 190 ILE I 200 1 11
HELIX 45 45 THR J 70 ASP J 90 1 21
HELIX 46 46 ASN K 65 LEU K 70 5 6
HELIX 47 47 THR K 72 LEU K 97 1 26
HELIX 48 48 PRO K 98 TYR K 119 1 22
HELIX 49 49 TYR K 119 SER K 131 1 13
HELIX 50 50 THR K 136 MET K 149 1 14
HELIX 51 51 GLY K 153 CYS K 171 1 19
HELIX 52 52 ASN K 173 CYS K 189 1 17
HELIX 53 53 ASP K 190 SER K 201 1 12
HELIX 54 54 SER L 69 ASP L 90 1 22
SITE 1 AC1 2 THR C 99 HOH C2007
SITE 1 AC2 3 PHE G 135 THR G 136 HOH G2006
SITE 1 AC3 1 PHE E 135
SITE 1 AC4 2 LYS A 87 CL A1203
SITE 1 AC5 1 CL A1202
CRYST1 124.774 68.762 171.598 90.00 109.43 90.00 I 1 2 1 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008014 0.000000 0.002827 0.00000
SCALE2 0.000000 0.014543 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006180 0.00000
(ATOM LINES ARE NOT SHOWN.)
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