HEADER TRANSCRIPTION/DNA-RNA HYBRID 06-SEP-12 4GZZ
TITLE CRYSTAL STRUCTURES OF BACTERIAL RNA POLYMERASE PAUSED ELONGATION
TITLE 2 COMPLEXES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RNAP SUBUNIT ALPHA, RNA POLYMERASE SUBUNIT ALPHA,
COMPND 5 TRANSCRIPTASE SUBUNIT ALPHA;
COMPND 6 EC: 2.7.7.6;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA;
COMPND 10 CHAIN: C;
COMPND 11 SYNONYM: RNAP SUBUNIT BETA, RNA POLYMERASE SUBUNIT BETA,
COMPND 12 TRANSCRIPTASE SUBUNIT BETA;
COMPND 13 EC: 2.7.7.6;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA';
COMPND 17 CHAIN: D;
COMPND 18 SYNONYM: RNAP SUBUNIT BETA', RNA POLYMERASE SUBUNIT BETA',
COMPND 19 TRANSCRIPTASE SUBUNIT BETA';
COMPND 20 EC: 2.7.7.6;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 4;
COMPND 23 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA;
COMPND 24 CHAIN: E;
COMPND 25 SYNONYM: RNAP OMEGA SUBUNIT, RNA POLYMERASE OMEGA SUBUNIT,
COMPND 26 TRANSCRIPTASE SUBUNIT OMEGA;
COMPND 27 EC: 2.7.7.6;
COMPND 28 ENGINEERED: YES;
COMPND 29 MOL_ID: 5;
COMPND 30 MOLECULE: NON-TEMPLATE DNA;
COMPND 31 CHAIN: N;
COMPND 32 ENGINEERED: YES;
COMPND 33 MOL_ID: 6;
COMPND 34 MOLECULE: RNA TRANSCRIPT;
COMPND 35 CHAIN: R;
COMPND 36 ENGINEERED: YES;
COMPND 37 MOL_ID: 7;
COMPND 38 MOLECULE: TEMPLATE DNA;
COMPND 39 CHAIN: T;
COMPND 40 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: RPOA, TTHA1664;
SOURCE 6 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 274;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 11 ORGANISM_TAXID: 300852;
SOURCE 12 STRAIN: HB8;
SOURCE 13 GENE: RPOB, TTHA1813;
SOURCE 14 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 274;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 19 ORGANISM_TAXID: 300852;
SOURCE 20 STRAIN: HB8;
SOURCE 21 GENE: RPOC, TTHA1812;
SOURCE 22 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 274;
SOURCE 24 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE 25 MOL_ID: 4;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 27 ORGANISM_TAXID: 300852;
SOURCE 28 STRAIN: HB8;
SOURCE 29 GENE: RPOZ, TTHA1561;
SOURCE 30 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE 31 EXPRESSION_SYSTEM_TAXID: 274;
SOURCE 32 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE 33 MOL_ID: 5;
SOURCE 34 SYNTHETIC: YES;
SOURCE 35 ORGANISM_SCIENTIFIC: SYNTHETIC;
SOURCE 36 ORGANISM_TAXID: 32630;
SOURCE 37 MOL_ID: 6;
SOURCE 38 SYNTHETIC: YES;
SOURCE 39 ORGANISM_SCIENTIFIC: SYNTHETIC;
SOURCE 40 ORGANISM_TAXID: 32630;
SOURCE 41 MOL_ID: 7;
SOURCE 42 SYNTHETIC: YES;
SOURCE 43 ORGANISM_SCIENTIFIC: SYNTHETIC;
SOURCE 44 ORGANISM_TAXID: 32630
KEYWDS RNA POLYMERASE, TRANSCRIPTION, PAUSED TRANSCRIPTION ELONGATION
KEYWDS 2 COMPLEX, TRANSCRIPTIONAL PAUSING, DNA DIRECTED RNA TRANSCRIPTION',
KEYWDS 3 TRANSCRIPTION-DNA-RNA HYBRID COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.WEIXLBAUMER,K.LEON,R.LANDICK,S.A.DARST
REVDAT 4 13-SEP-23 4GZZ 1 REMARK SEQADV LINK
REVDAT 3 17-JUL-19 4GZZ 1 REMARK
REVDAT 2 15-NOV-17 4GZZ 1 REMARK
REVDAT 1 13-FEB-13 4GZZ 0
JRNL AUTH A.WEIXLBAUMER,K.LEON,R.LANDICK,S.A.DARST
JRNL TITL STRUCTURAL BASIS OF TRANSCRIPTIONAL PAUSING IN BACTERIA.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 152 431 2013
JRNL REFN ISSN 0092-8674
JRNL PMID 23374340
JRNL DOI 10.1016/J.CELL.2012.12.020
REMARK 2
REMARK 2 RESOLUTION. 4.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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) : 4.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 41266
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2070
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 38.7867 - 10.5207 0.98 2588 123 0.2142 0.2513
REMARK 3 2 10.5207 - 8.3782 0.99 2648 124 0.1802 0.2351
REMARK 3 3 8.3782 - 7.3273 0.99 2598 126 0.1893 0.2551
REMARK 3 4 7.3273 - 6.6610 1.00 2649 143 0.2145 0.2744
REMARK 3 5 6.6610 - 6.1856 1.00 2618 151 0.2418 0.3088
REMARK 3 6 6.1856 - 5.8222 1.00 2624 146 0.2603 0.3049
REMARK 3 7 5.8222 - 5.5315 0.99 2639 133 0.2716 0.3669
REMARK 3 8 5.5315 - 5.2913 1.00 2626 135 0.2746 0.3372
REMARK 3 9 5.2913 - 5.0881 0.99 2622 124 0.2761 0.2888
REMARK 3 10 5.0881 - 4.9129 1.00 2641 135 0.2736 0.2978
REMARK 3 11 4.9129 - 4.7595 0.99 2624 146 0.2845 0.2951
REMARK 3 12 4.7595 - 4.6237 0.99 2585 164 0.2861 0.3725
REMARK 3 13 4.6237 - 4.5022 0.99 2639 117 0.3042 0.3350
REMARK 3 14 4.5022 - 4.3925 0.99 2579 153 0.3317 0.3291
REMARK 3 15 4.3925 - 4.2927 0.95 2516 150 0.3463 0.3640
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) : 0.670
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 125.9
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 : 0.005 24969
REMARK 3 ANGLE : 0.934 33909
REMARK 3 CHIRALITY : 0.061 3835
REMARK 3 PLANARITY : 0.005 4309
REMARK 3 DIHEDRAL : 16.343 9678
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' ) OR (CHAIN 'B' ) OR (CHAIN 'C' AND
REMARK 3 RESSEQ 1:17) OR (CHAIN 'C' AND RESSEQ 394:700) OR
REMARK 3 (CHAIN 'C' AND RESSEQ 833:997) OR (CHAIN 'D' AND
REMARK 3 RESSEQ 783:1069)
REMARK 3 ORIGIN FOR THE GROUP (A):-166.4984 18.0218 68.3318
REMARK 3 T TENSOR
REMARK 3 T11: 0.3774 T22: 0.1051
REMARK 3 T33: 0.4208 T12: -0.1341
REMARK 3 T13: 0.1219 T23: 0.7028
REMARK 3 L TENSOR
REMARK 3 L11: 1.5699 L22: 1.2443
REMARK 3 L33: 1.6987 L12: -0.4481
REMARK 3 L13: 0.2750 L23: -0.5246
REMARK 3 S TENSOR
REMARK 3 S11: -0.7600 S12: 0.5218 S13: -0.8194
REMARK 3 S21: 0.0555 S22: 0.1704 S23: 0.7952
REMARK 3 S31: 0.2705 S32: -0.7280 S33: -1.7498
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'C' AND RESSEQ 1006:1071) OR (CHAIN 'D' AND
REMARK 3 RESSEQ 621:778) OR (CHAIN 'D' AND RESSEQ 1103:1432)
REMARK 3 OR (CHAIN 'D' AND RESSEQ 1473:1499) OR (CHAIN 'E' )
REMARK 3 ORIGIN FOR THE GROUP (A):-131.8191 41.2202 82.4732
REMARK 3 T TENSOR
REMARK 3 T11: 1.1716 T22: 0.4652
REMARK 3 T33: 0.2829 T12: 0.0973
REMARK 3 T13: -0.6149 T23: 0.4043
REMARK 3 L TENSOR
REMARK 3 L11: 1.2254 L22: 1.9527
REMARK 3 L33: 1.3096 L12: -0.1907
REMARK 3 L13: 0.4292 L23: 0.2561
REMARK 3 S TENSOR
REMARK 3 S11: -0.5483 S12: -0.1968 S13: 0.6432
REMARK 3 S21: 0.0893 S22: 0.5629 S23: -0.6373
REMARK 3 S31: -0.5928 S32: 0.4381 S33: 1.6337
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND RESSEQ 1083:1112) OR (CHAIN 'D' AND
REMARK 3 RESSEQ 2:131) OR (CHAIN 'D' AND RESSEQ 455:605) OR
REMARK 3 (CHAIN 'D' AND RESSEQ 1444:1468)
REMARK 3 ORIGIN FOR THE GROUP (A):-107.3933 28.5831 111.8765
REMARK 3 T TENSOR
REMARK 3 T11: 1.3647 T22: 1.0561
REMARK 3 T33: 0.9259 T12: -0.0659
REMARK 3 T13: -0.8655 T23: 0.1699
REMARK 3 L TENSOR
REMARK 3 L11: 0.3512 L22: 0.5329
REMARK 3 L33: 0.1259 L12: 0.1362
REMARK 3 L13: 0.0322 L23: -0.1691
REMARK 3 S TENSOR
REMARK 3 S11: -0.2261 S12: -0.3808 S13: 0.4309
REMARK 3 S21: 0.4547 S22: 0.1179 S23: 0.0790
REMARK 3 S31: -0.5406 S32: -0.0105 S33: -0.0248
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'D' AND RESSEQ 132:454)
REMARK 3 ORIGIN FOR THE GROUP (A): -56.8438 6.1731 116.7528
REMARK 3 T TENSOR
REMARK 3 T11: 1.0678 T22: 1.4049
REMARK 3 T33: 1.6286 T12: -0.3482
REMARK 3 T13: -0.2900 T23: 0.5920
REMARK 3 L TENSOR
REMARK 3 L11: 0.0384 L22: 0.1206
REMARK 3 L33: 0.1118 L12: -0.0512
REMARK 3 L13: -0.0391 L23: 0.0300
REMARK 3 S TENSOR
REMARK 3 S11: -0.4960 S12: -0.0221 S13: 0.3698
REMARK 3 S21: 0.6768 S22: 0.1451 S23: -0.3394
REMARK 3 S31: 0.1816 S32: 0.2937 S33: -0.0019
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN 'C' AND RESSEQ 18:142) OR (CHAIN 'C' AND
REMARK 3 RESSEQ 332:393)
REMARK 3 ORIGIN FOR THE GROUP (A):-127.1923 -22.0654 93.1461
REMARK 3 T TENSOR
REMARK 3 T11: 1.3395 T22: 0.8027
REMARK 3 T33: 1.2180 T12: 0.3791
REMARK 3 T13: 0.6399 T23: 0.7270
REMARK 3 L TENSOR
REMARK 3 L11: 0.1532 L22: 0.2115
REMARK 3 L33: 0.4770 L12: 0.1539
REMARK 3 L13: -0.0348 L23: 0.0896
REMARK 3 S TENSOR
REMARK 3 S11: 0.1954 S12: -0.4296 S13: -0.4934
REMARK 3 S21: 0.4087 S22: -0.3011 S23: -0.2063
REMARK 3 S31: 0.4349 S32: 0.4285 S33: 0.4264
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN 'C' AND RESSEQ 143:331)
REMARK 3 ORIGIN FOR THE GROUP (A):-106.1131 -17.3584 67.0582
REMARK 3 T TENSOR
REMARK 3 T11: 1.1220 T22: 0.9526
REMARK 3 T33: 1.1638 T12: 0.0470
REMARK 3 T13: 0.7853 T23: 0.6788
REMARK 3 L TENSOR
REMARK 3 L11: 0.1325 L22: 0.1764
REMARK 3 L33: 0.2809 L12: -0.0127
REMARK 3 L13: 0.0208 L23: -0.1163
REMARK 3 S TENSOR
REMARK 3 S11: 0.2923 S12: -0.3412 S13: -0.2228
REMARK 3 S21: 0.1371 S22: -0.0550 S23: 0.2532
REMARK 3 S31: -0.0219 S32: 0.1154 S33: 0.4169
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN 'C' AND RESSEQ 701:832)
REMARK 3 ORIGIN FOR THE GROUP (A):-150.0728 3.6108 113.0662
REMARK 3 T TENSOR
REMARK 3 T11: 1.3227 T22: 1.1835
REMARK 3 T33: 0.9278 T12: 0.0381
REMARK 3 T13: 0.5687 T23: 0.5449
REMARK 3 L TENSOR
REMARK 3 L11: 0.1538 L22: 0.1541
REMARK 3 L33: 0.4308 L12: 0.0830
REMARK 3 L13: -0.2395 L23: -0.0077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0759 S12: -0.4762 S13: -0.1118
REMARK 3 S21: 0.2774 S22: 0.0517 S23: -0.2153
REMARK 3 S31: 0.2817 S32: 0.3487 S33: 0.4515
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN 'D' AND RESSEQ 1070:1102)
REMARK 3 ORIGIN FOR THE GROUP (A):-130.6122 16.9104 71.9573
REMARK 3 T TENSOR
REMARK 3 T11: 0.9517 T22: 0.8326
REMARK 3 T33: 0.4972 T12: 0.1377
REMARK 3 T13: 0.2335 T23: 0.3786
REMARK 3 L TENSOR
REMARK 3 L11: 0.0387 L22: 0.0390
REMARK 3 L33: 0.0391 L12: 0.0274
REMARK 3 L13: 0.0055 L23: 0.0207
REMARK 3 S TENSOR
REMARK 3 S11: -0.0554 S12: 0.0735 S13: -0.1561
REMARK 3 S21: 0.0436 S22: -0.0648 S23: 0.0435
REMARK 3 S31: 0.0076 S32: 0.0201 S33: -0.0176
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN 'D' AND RESSEQ 779:782)
REMARK 3 ORIGIN FOR THE GROUP (A):-149.7666 34.7499 69.9858
REMARK 3 T TENSOR
REMARK 3 T11: 0.5053 T22: 0.3258
REMARK 3 T33: 0.5549 T12: 0.0665
REMARK 3 T13: 0.1317 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.0282 L22: 0.0041
REMARK 3 L33: 0.0019 L12: 0.0097
REMARK 3 L13: 0.0068 L23: 0.0018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: -0.0078 S13: 0.0013
REMARK 3 S21: 0.0024 S22: 0.0106 S23: -0.0043
REMARK 3 S31: -0.0006 S32: -0.0176 S33: 0.0002
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN 'D' AND RESSEQ 1433:1443)
REMARK 3 ORIGIN FOR THE GROUP (A):-113.9513 30.2542 93.4614
REMARK 3 T TENSOR
REMARK 3 T11: 1.0148 T22: 0.8152
REMARK 3 T33: 0.6460 T12: 0.2490
REMARK 3 T13: -0.0252 T23: -0.0629
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0054
REMARK 3 L33: 0.0039 L12: -0.0008
REMARK 3 L13: -0.0010 L23: -0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0327 S12: 0.0659 S13: -0.0132
REMARK 3 S21: -0.0244 S22: -0.0366 S23: -0.0008
REMARK 3 S31: -0.0038 S32: -0.0118 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN 'D' AND RESSEQ 606:620)
REMARK 3 ORIGIN FOR THE GROUP (A):-122.0115 25.6311 98.8068
REMARK 3 T TENSOR
REMARK 3 T11: 1.0383 T22: 0.9217
REMARK 3 T33: 0.8100 T12: 0.1894
REMARK 3 T13: -0.3368 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 0.0014 L22: 0.0011
REMARK 3 L33: 0.0026 L12: -0.0000
REMARK 3 L13: 0.0014 L23: 0.0017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0128 S12: 0.0456 S13: 0.0170
REMARK 3 S21: -0.0634 S22: 0.0028 S23: -0.0180
REMARK 3 S31: 0.0068 S32: -0.0380 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN 'C' AND RESSEQ 998:1005)
REMARK 3 ORIGIN FOR THE GROUP (A):-151.2594 12.8022 90.9153
REMARK 3 T TENSOR
REMARK 3 T11: 0.7792 T22: 1.1019
REMARK 3 T33: 0.8833 T12: 0.3013
REMARK 3 T13: -0.0913 T23: 0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0035
REMARK 3 L33: 0.0015 L12: -0.0019
REMARK 3 L13: -0.0008 L23: 0.0027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: -0.0281 S13: 0.0102
REMARK 3 S21: 0.0344 S22: -0.0286 S23: 0.0019
REMARK 3 S31: -0.0206 S32: -0.0042 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN 'C' AND RESSEQ 1072:1082)
REMARK 3 ORIGIN FOR THE GROUP (A):-138.3243 42.8575 108.1553
REMARK 3 T TENSOR
REMARK 3 T11: 1.1444 T22: 1.1616
REMARK 3 T33: 0.9612 T12: 0.1688
REMARK 3 T13: -0.1624 T23: -0.2243
REMARK 3 L TENSOR
REMARK 3 L11: 0.0062 L22: 0.0003
REMARK 3 L33: 0.0036 L12: -0.0014
REMARK 3 L13: -0.0007 L23: 0.0018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0239 S12: 0.0202 S13: 0.0101
REMARK 3 S21: 0.0259 S22: 0.0467 S23: 0.0087
REMARK 3 S31: -0.0169 S32: 0.0295 S33: 0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN 'D' AND RESSEQ 1469:1472)
REMARK 3 ORIGIN FOR THE GROUP (A):-126.7661 42.2829 98.0821
REMARK 3 T TENSOR
REMARK 3 T11: 0.7876 T22: 0.7049
REMARK 3 T33: 0.6429 T12: 0.0677
REMARK 3 T13: -0.0241 T23: 0.1356
REMARK 3 L TENSOR
REMARK 3 L11: 0.0174 L22: 0.0020
REMARK 3 L33: 0.0196 L12: -0.0058
REMARK 3 L13: 0.0186 L23: -0.0064
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: -0.0073 S13: -0.0102
REMARK 3 S21: -0.0122 S22: 0.0214 S23: 0.0006
REMARK 3 S31: -0.0113 S32: -0.0107 S33: -0.0001
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN 'N' ) OR (CHAIN 'T' AND RESSEQ 1:13)
REMARK 3 ORIGIN FOR THE GROUP (A):-100.0652 13.3274 82.1262
REMARK 3 T TENSOR
REMARK 3 T11: 4.2683 T22: 4.5109
REMARK 3 T33: 4.4632 T12: -0.1104
REMARK 3 T13: 0.2984 T23: 0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 0.0166 L22: 0.0103
REMARK 3 L33: 0.0249 L12: -0.0041
REMARK 3 L13: 0.0097 L23: -0.0076
REMARK 3 S TENSOR
REMARK 3 S11: -0.1645 S12: 0.1217 S13: -0.0011
REMARK 3 S21: -0.0845 S22: -0.1465 S23: -0.3428
REMARK 3 S31: 0.1877 S32: 0.3544 S33: -0.0004
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'R'
REMARK 3 ORIGIN FOR THE GROUP (A):-133.8017 8.0478 89.6300
REMARK 3 T TENSOR
REMARK 3 T11: 2.7974 T22: 2.4001
REMARK 3 T33: 2.3524 T12: -0.2289
REMARK 3 T13: -0.5274 T23: -0.2007
REMARK 3 L TENSOR
REMARK 3 L11: 0.0099 L22: 0.0254
REMARK 3 L33: 0.0147 L12: 0.0172
REMARK 3 L13: -0.0055 L23: -0.0074
REMARK 3 S TENSOR
REMARK 3 S11: 0.0959 S12: 0.0961 S13: -0.0033
REMARK 3 S21: 0.0160 S22: -0.0141 S23: 0.0119
REMARK 3 S31: -0.0727 S32: 0.0156 S33: 0.0002
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'T' AND RESSEQ 14:22
REMARK 3 ORIGIN FOR THE GROUP (A):-135.5359 9.1147 93.4024
REMARK 3 T TENSOR
REMARK 3 T11: 2.9413 T22: 2.6840
REMARK 3 T33: 2.7615 T12: -0.2469
REMARK 3 T13: 0.6132 T23: 0.4161
REMARK 3 L TENSOR
REMARK 3 L11: 0.0348 L22: 0.0176
REMARK 3 L33: 0.0215 L12: 0.0143
REMARK 3 L13: -0.0001 L23: 0.0153
REMARK 3 S TENSOR
REMARK 3 S11: 0.1144 S12: -0.0368 S13: -0.0056
REMARK 3 S21: -0.1077 S22: 0.1108 S23: -0.0212
REMARK 3 S31: -0.2308 S32: 0.0576 S33: 0.0003
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4GZZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074845.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91956
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51877
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.000
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.44200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.94700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2O5I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-7% PEG 3000, 0.1M MES PH 6.1-6.3,
REMARK 280 0.3M LICL, 10MM MGCL2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K, PH 6.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 143.27450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 82.71957
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.47033
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 143.27450
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 82.71957
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 66.47033
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 143.27450
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 82.71957
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.47033
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 165.43914
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 132.94067
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 165.43914
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 132.94067
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 165.43914
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 132.94067
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 37460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 128850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -196.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, N, R, T
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 ASP A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 LEU A 6
REMARK 465 ALA A 230
REMARK 465 ALA A 231
REMARK 465 ALA A 232
REMARK 465 VAL A 233
REMARK 465 ALA A 234
REMARK 465 ALA A 235
REMARK 465 PRO A 236
REMARK 465 GLU A 237
REMARK 465 GLU A 238
REMARK 465 ALA A 239
REMARK 465 LYS A 240
REMARK 465 GLU A 241
REMARK 465 PRO A 242
REMARK 465 GLU A 243
REMARK 465 ALA A 244
REMARK 465 PRO A 245
REMARK 465 PRO A 246
REMARK 465 GLU A 247
REMARK 465 GLN A 248
REMARK 465 GLU A 249
REMARK 465 GLU A 250
REMARK 465 GLU A 251
REMARK 465 LEU A 252
REMARK 465 ASP A 253
REMARK 465 LEU A 254
REMARK 465 PRO A 255
REMARK 465 LEU A 256
REMARK 465 GLU A 257
REMARK 465 GLU A 258
REMARK 465 LEU A 259
REMARK 465 GLY A 260
REMARK 465 LEU A 261
REMARK 465 SER A 262
REMARK 465 THR A 263
REMARK 465 ARG A 264
REMARK 465 VAL A 265
REMARK 465 LEU A 266
REMARK 465 HIS A 267
REMARK 465 SER A 268
REMARK 465 LEU A 269
REMARK 465 LYS A 270
REMARK 465 GLU A 271
REMARK 465 GLU A 272
REMARK 465 GLY A 273
REMARK 465 ILE A 274
REMARK 465 GLU A 275
REMARK 465 SER A 276
REMARK 465 VAL A 277
REMARK 465 ARG A 278
REMARK 465 ALA A 279
REMARK 465 LEU A 280
REMARK 465 LEU A 281
REMARK 465 ALA A 282
REMARK 465 LEU A 283
REMARK 465 ASN A 284
REMARK 465 LEU A 285
REMARK 465 LYS A 286
REMARK 465 ASP A 287
REMARK 465 LEU A 288
REMARK 465 LYS A 289
REMARK 465 ASN A 290
REMARK 465 ILE A 291
REMARK 465 PRO A 292
REMARK 465 GLY A 293
REMARK 465 ILE A 294
REMARK 465 GLY A 295
REMARK 465 GLU A 296
REMARK 465 ARG A 297
REMARK 465 SER A 298
REMARK 465 LEU A 299
REMARK 465 GLU A 300
REMARK 465 GLU A 301
REMARK 465 ILE A 302
REMARK 465 LYS A 303
REMARK 465 GLU A 304
REMARK 465 ALA A 305
REMARK 465 LEU A 306
REMARK 465 GLU A 307
REMARK 465 LYS A 308
REMARK 465 LYS A 309
REMARK 465 GLY A 310
REMARK 465 PHE A 311
REMARK 465 THR A 312
REMARK 465 LEU A 313
REMARK 465 LYS A 314
REMARK 465 GLU A 315
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 ASP B 3
REMARK 465 SER B 4
REMARK 465 LYS B 5
REMARK 465 LEU B 6
REMARK 465 ALA B 230
REMARK 465 ALA B 231
REMARK 465 ALA B 232
REMARK 465 VAL B 233
REMARK 465 ALA B 234
REMARK 465 ALA B 235
REMARK 465 PRO B 236
REMARK 465 GLU B 237
REMARK 465 GLU B 238
REMARK 465 ALA B 239
REMARK 465 LYS B 240
REMARK 465 GLU B 241
REMARK 465 PRO B 242
REMARK 465 GLU B 243
REMARK 465 ALA B 244
REMARK 465 PRO B 245
REMARK 465 PRO B 246
REMARK 465 GLU B 247
REMARK 465 GLN B 248
REMARK 465 GLU B 249
REMARK 465 GLU B 250
REMARK 465 GLU B 251
REMARK 465 LEU B 252
REMARK 465 ASP B 253
REMARK 465 LEU B 254
REMARK 465 PRO B 255
REMARK 465 LEU B 256
REMARK 465 GLU B 257
REMARK 465 GLU B 258
REMARK 465 LEU B 259
REMARK 465 GLY B 260
REMARK 465 LEU B 261
REMARK 465 SER B 262
REMARK 465 THR B 263
REMARK 465 ARG B 264
REMARK 465 VAL B 265
REMARK 465 LEU B 266
REMARK 465 HIS B 267
REMARK 465 SER B 268
REMARK 465 LEU B 269
REMARK 465 LYS B 270
REMARK 465 GLU B 271
REMARK 465 GLU B 272
REMARK 465 GLY B 273
REMARK 465 ILE B 274
REMARK 465 GLU B 275
REMARK 465 SER B 276
REMARK 465 VAL B 277
REMARK 465 ARG B 278
REMARK 465 ALA B 279
REMARK 465 LEU B 280
REMARK 465 LEU B 281
REMARK 465 ALA B 282
REMARK 465 LEU B 283
REMARK 465 ASN B 284
REMARK 465 LEU B 285
REMARK 465 LYS B 286
REMARK 465 ASP B 287
REMARK 465 LEU B 288
REMARK 465 LYS B 289
REMARK 465 ASN B 290
REMARK 465 ILE B 291
REMARK 465 PRO B 292
REMARK 465 GLY B 293
REMARK 465 ILE B 294
REMARK 465 GLY B 295
REMARK 465 GLU B 296
REMARK 465 ARG B 297
REMARK 465 SER B 298
REMARK 465 LEU B 299
REMARK 465 GLU B 300
REMARK 465 GLU B 301
REMARK 465 ILE B 302
REMARK 465 LYS B 303
REMARK 465 GLU B 304
REMARK 465 ALA B 305
REMARK 465 LEU B 306
REMARK 465 GLU B 307
REMARK 465 LYS B 308
REMARK 465 LYS B 309
REMARK 465 GLY B 310
REMARK 465 PHE B 311
REMARK 465 THR B 312
REMARK 465 LEU B 313
REMARK 465 LYS B 314
REMARK 465 GLU B 315
REMARK 465 GLU C 57
REMARK 465 ASP C 58
REMARK 465 LYS C 59
REMARK 465 GLY C 60
REMARK 465 LYS C 61
REMARK 465 GLY C 62
REMARK 465 LYS C 762
REMARK 465 GLY C 763
REMARK 465 GLU C 764
REMARK 465 SER C 765
REMARK 465 GLU C 766
REMARK 465 PRO C 767
REMARK 465 THR C 768
REMARK 465 PRO C 769
REMARK 465 GLU C 770
REMARK 465 GLU C 771
REMARK 465 ARG C 772
REMARK 465 LEU C 773
REMARK 465 LEU C 774
REMARK 465 ARG C 775
REMARK 465 SER C 776
REMARK 465 ILE C 777
REMARK 465 PHE C 778
REMARK 465 GLY C 779
REMARK 465 GLU C 780
REMARK 465 LYS C 781
REMARK 465 ALA C 782
REMARK 465 ARG C 783
REMARK 465 ASP C 784
REMARK 465 GLU C 1113
REMARK 465 GLY C 1114
REMARK 465 LEU C 1115
REMARK 465 ALA C 1116
REMARK 465 SER C 1117
REMARK 465 LYS C 1118
REMARK 465 ARG C 1119
REMARK 465 MET D 1
REMARK 465 LYS D 217
REMARK 465 LYS D 218
REMARK 465 GLU D 219
REMARK 465 ARG D 220
REMARK 465 ALA D 221
REMARK 465 GLY D 222
REMARK 465 LEU D 223
REMARK 465 ARG D 224
REMARK 465 LEU D 225
REMARK 465 PRO D 226
REMARK 465 LEU D 227
REMARK 465 ALA D 228
REMARK 465 ALA D 229
REMARK 465 TRP D 230
REMARK 465 VAL D 231
REMARK 465 GLU D 232
REMARK 465 LYS D 233
REMARK 465 GLU D 234
REMARK 465 ALA D 235
REMARK 465 TYR D 236
REMARK 465 LYS D 237
REMARK 465 PRO D 238
REMARK 465 GLY D 239
REMARK 465 GLU D 240
REMARK 465 ILE D 241
REMARK 465 LEU D 242
REMARK 465 ALA D 243
REMARK 465 GLU D 244
REMARK 465 LEU D 245
REMARK 465 PRO D 246
REMARK 465 GLU D 247
REMARK 465 PRO D 248
REMARK 465 TYR D 249
REMARK 465 LEU D 250
REMARK 465 PHE D 251
REMARK 465 ARG D 252
REMARK 465 ALA D 253
REMARK 465 GLU D 254
REMARK 465 GLU D 255
REMARK 465 GLU D 256
REMARK 465 GLY D 257
REMARK 465 VAL D 258
REMARK 465 VAL D 259
REMARK 465 GLU D 260
REMARK 465 LEU D 261
REMARK 465 LYS D 262
REMARK 465 GLU D 263
REMARK 465 LEU D 264
REMARK 465 GLU D 265
REMARK 465 GLU D 266
REMARK 465 GLY D 267
REMARK 465 ALA D 268
REMARK 465 PHE D 269
REMARK 465 LEU D 270
REMARK 465 VAL D 271
REMARK 465 LEU D 272
REMARK 465 ARG D 273
REMARK 465 ARG D 274
REMARK 465 GLU D 275
REMARK 465 ASP D 276
REMARK 465 GLU D 277
REMARK 465 PRO D 278
REMARK 465 VAL D 279
REMARK 465 ALA D 280
REMARK 465 THR D 281
REMARK 465 TYR D 282
REMARK 465 PHE D 283
REMARK 465 LEU D 284
REMARK 465 PRO D 285
REMARK 465 VAL D 286
REMARK 465 GLY D 287
REMARK 465 MET D 288
REMARK 465 THR D 289
REMARK 465 PRO D 290
REMARK 465 LEU D 291
REMARK 465 VAL D 292
REMARK 465 VAL D 293
REMARK 465 HIS D 294
REMARK 465 GLY D 295
REMARK 465 GLU D 296
REMARK 465 ILE D 297
REMARK 465 VAL D 298
REMARK 465 GLU D 299
REMARK 465 LYS D 300
REMARK 465 GLY D 301
REMARK 465 GLN D 302
REMARK 465 PRO D 303
REMARK 465 LEU D 304
REMARK 465 ALA D 305
REMARK 465 GLU D 306
REMARK 465 ALA D 307
REMARK 465 LYS D 308
REMARK 465 GLY D 309
REMARK 465 LEU D 310
REMARK 465 LEU D 311
REMARK 465 ARG D 312
REMARK 465 MET D 313
REMARK 465 PRO D 314
REMARK 465 ARG D 315
REMARK 465 GLN D 316
REMARK 465 VAL D 317
REMARK 465 ARG D 318
REMARK 465 ALA D 319
REMARK 465 ALA D 320
REMARK 465 GLN D 321
REMARK 465 VAL D 322
REMARK 465 GLU D 323
REMARK 465 ALA D 324
REMARK 465 GLU D 325
REMARK 465 GLU D 326
REMARK 465 GLU D 327
REMARK 465 GLY D 328
REMARK 465 GLU D 329
REMARK 465 THR D 330
REMARK 465 VAL D 331
REMARK 465 TYR D 332
REMARK 465 LEU D 333
REMARK 465 THR D 334
REMARK 465 LEU D 335
REMARK 465 PHE D 336
REMARK 465 LEU D 337
REMARK 465 GLU D 338
REMARK 465 TRP D 339
REMARK 465 THR D 1237
REMARK 465 MET D 1238
REMARK 465 ARG D 1239
REMARK 465 THR D 1240
REMARK 465 PHE D 1241
REMARK 465 HIS D 1242
REMARK 465 THR D 1243
REMARK 465 GLY D 1244
REMARK 465 GLY D 1245
REMARK 465 VAL D 1246
REMARK 465 ALA D 1247
REMARK 465 GLY D 1248
REMARK 465 ALA D 1249
REMARK 465 ALA D 1250
REMARK 465 ASP D 1251
REMARK 465 ILE D 1252
REMARK 465 THR D 1253
REMARK 465 LYS D 1500
REMARK 465 GLU D 1501
REMARK 465 ALA D 1502
REMARK 465 VAL D 1503
REMARK 465 GLU D 1504
REMARK 465 ALA D 1505
REMARK 465 LYS D 1506
REMARK 465 GLU D 1507
REMARK 465 ARG D 1508
REMARK 465 PRO D 1509
REMARK 465 ALA D 1510
REMARK 465 ALA D 1511
REMARK 465 ARG D 1512
REMARK 465 ARG D 1513
REMARK 465 GLY D 1514
REMARK 465 VAL D 1515
REMARK 465 LYS D 1516
REMARK 465 ARG D 1517
REMARK 465 GLU D 1518
REMARK 465 GLN D 1519
REMARK 465 PRO D 1520
REMARK 465 GLY D 1521
REMARK 465 LYS D 1522
REMARK 465 GLN D 1523
REMARK 465 ALA D 1524
REMARK 465 HIS D 1525
REMARK 465 HIS D 1526
REMARK 465 HIS D 1527
REMARK 465 HIS D 1528
REMARK 465 HIS D 1529
REMARK 465 HIS D 1530
REMARK 465 HIS D 1531
REMARK 465 HIS D 1532
REMARK 465 HIS D 1533
REMARK 465 HIS D 1534
REMARK 465 MET E 1
REMARK 465 VAL E 95
REMARK 465 GLU E 96
REMARK 465 ARG E 97
REMARK 465 GLU E 98
REMARK 465 GLU E 99
REMARK 465 DG N 1
REMARK 465 DG N 2
REMARK 465 U R 14
REMARK 465 C R 15
REMARK 465 A R 16
REMARK 465 G R 17
REMARK 465 G R 18
REMARK 465 C R 19
REMARK 465 G R 20
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 GLN D1254 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS C 846 OP1 U R 29 1.99
REMARK 500 O GLN B 188 NZ LYS D 646 2.00
REMARK 500 OH TYR C 435 OD2 ASP C 533 2.04
REMARK 500 O GLU D 925 NH1 ARG D 929 2.08
REMARK 500 NH1 ARG C 388 OP1 DT T 22 2.09
REMARK 500 O ALA D 501 OG SER D 505 2.15
REMARK 500 O LEU D 161 NZ LYS D 397 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG B 143 OE2 GLU D 1297 3455 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO C 727 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO D 706 C - N - CA ANGL. DEV. = -12.7 DEGREES
REMARK 500 DG N 7 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DT N 10 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC N 11 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC N 12 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DG T 2 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG T 3 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA T 4 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DA T 5 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DT T 6 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC T 7 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT T 8 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT T 10 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DC T 12 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 29 -90.57 -66.88
REMARK 500 SER A 46 -61.71 -92.41
REMARK 500 SER A 47 -141.32 -86.29
REMARK 500 ILE A 48 127.27 63.54
REMARK 500 GLU A 59 -70.63 -42.27
REMARK 500 LEU A 62 -70.44 -94.30
REMARK 500 PHE A 65 61.29 -100.43
REMARK 500 GLU A 84 31.70 -88.15
REMARK 500 LEU A 94 98.14 -63.53
REMARK 500 PRO A 106 96.25 -67.17
REMARK 500 GLU A 108 104.76 -59.79
REMARK 500 VAL A 109 89.53 -65.53
REMARK 500 ALA A 118 -86.68 -30.66
REMARK 500 GLU A 134 96.97 -66.33
REMARK 500 LYS A 155 -67.56 -96.95
REMARK 500 ARG A 161 -123.30 -89.29
REMARK 500 SER A 172 94.89 -172.82
REMARK 500 GLU A 182 -158.14 -106.12
REMARK 500 THR A 184 -168.11 110.82
REMARK 500 ARG A 185 147.59 69.32
REMARK 500 LEU A 186 94.81 59.98
REMARK 500 GLN A 188 -69.80 -105.40
REMARK 500 PHE A 225 31.28 -83.62
REMARK 500 SER B 46 -17.50 -144.69
REMARK 500 PHE B 65 60.45 -101.05
REMARK 500 LEU B 94 92.47 -69.24
REMARK 500 PRO B 106 44.87 -74.50
REMARK 500 ALA B 118 -119.09 55.19
REMARK 500 ASP B 119 44.74 -94.59
REMARK 500 ARG B 146 57.06 -113.35
REMARK 500 GLU B 154 22.42 -78.76
REMARK 500 ILE B 158 94.77 -61.49
REMARK 500 LYS B 159 74.03 -68.25
REMARK 500 ASN B 163 40.56 -107.99
REMARK 500 VAL B 170 68.92 -101.89
REMARK 500 SER B 172 105.48 -41.86
REMARK 500 GLN B 188 -77.69 -64.12
REMARK 500 ASP B 191 39.23 -78.81
REMARK 500 GLU C 2 175.94 45.14
REMARK 500 GLU C 11 99.62 -61.51
REMARK 500 GLN C 31 38.20 -85.58
REMARK 500 ASP C 33 -82.50 -65.26
REMARK 500 PRO C 35 156.07 -48.28
REMARK 500 LYS C 38 -167.41 -67.63
REMARK 500 ARG C 39 -147.77 -78.09
REMARK 500 VAL C 42 -179.48 -63.61
REMARK 500 PHE C 48 -70.53 -56.49
REMARK 500 ARG C 49 0.45 -68.30
REMARK 500 PHE C 52 -63.48 -100.74
REMARK 500 LEU C 69 63.61 -110.36
REMARK 500
REMARK 500 THIS ENTRY HAS 294 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 739 OD1
REMARK 620 2 ASP D 739 OD2 50.9
REMARK 620 3 ASP D 741 OD1 75.3 63.4
REMARK 620 4 ASP D 743 OD1 74.2 105.8 56.9
REMARK 620 5 U R 29 O3' 126.3 170.9 125.5 80.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1112 SG
REMARK 620 2 CYS D1194 SG 123.6
REMARK 620 3 CYS D1201 SG 83.9 122.0
REMARK 620 4 CYS D1204 SG 101.6 123.4 92.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1603
DBREF 4GZZ A 1 315 UNP Q5SHR6 RPOA_THET8 1 315
DBREF 4GZZ B 1 315 UNP Q5SHR6 RPOA_THET8 1 315
DBREF 4GZZ C 1 1119 UNP Q8RQE9 RPOB_THET8 1 1119
DBREF 4GZZ D 1 1524 UNP Q8RQE8 RPOC_THET8 1 1524
DBREF 4GZZ E 1 99 UNP Q8RQE7 RPOZ_THET8 1 99
DBREF 4GZZ N 1 13 PDB 4GZZ 4GZZ 1 13
DBREF 4GZZ R 14 29 PDB 4GZZ 4GZZ 14 29
DBREF 4GZZ T 1 22 PDB 4GZZ 4GZZ 1 22
SEQADV 4GZZ HIS D 1525 UNP Q8RQE8 EXPRESSION TAG
SEQADV 4GZZ HIS D 1526 UNP Q8RQE8 EXPRESSION TAG
SEQADV 4GZZ HIS D 1527 UNP Q8RQE8 EXPRESSION TAG
SEQADV 4GZZ HIS D 1528 UNP Q8RQE8 EXPRESSION TAG
SEQADV 4GZZ HIS D 1529 UNP Q8RQE8 EXPRESSION TAG
SEQADV 4GZZ HIS D 1530 UNP Q8RQE8 EXPRESSION TAG
SEQADV 4GZZ HIS D 1531 UNP Q8RQE8 EXPRESSION TAG
SEQADV 4GZZ HIS D 1532 UNP Q8RQE8 EXPRESSION TAG
SEQADV 4GZZ HIS D 1533 UNP Q8RQE8 EXPRESSION TAG
SEQADV 4GZZ HIS D 1534 UNP Q8RQE8 EXPRESSION TAG
SEQRES 1 A 315 MET LEU ASP SER LYS LEU LYS ALA PRO VAL PHE THR VAL
SEQRES 2 A 315 ARG THR GLN GLY ARG GLU TYR GLY GLU PHE VAL LEU GLU
SEQRES 3 A 315 PRO LEU GLU ARG GLY PHE GLY VAL THR LEU GLY ASN PRO
SEQRES 4 A 315 LEU ARG ARG ILE LEU LEU SER SER ILE PRO GLY THR ALA
SEQRES 5 A 315 VAL THR SER VAL TYR ILE GLU ASP VAL LEU HIS GLU PHE
SEQRES 6 A 315 SER THR ILE PRO GLY VAL LYS GLU ASP VAL VAL GLU ILE
SEQRES 7 A 315 ILE LEU ASN LEU LYS GLU LEU VAL VAL ARG PHE LEU ASN
SEQRES 8 A 315 PRO SER LEU GLN THR VAL THR LEU LEU LEU LYS ALA GLU
SEQRES 9 A 315 GLY PRO LYS GLU VAL LYS ALA ARG ASP PHE LEU PRO VAL
SEQRES 10 A 315 ALA ASP VAL GLU ILE MET ASN PRO ASP LEU HIS ILE ALA
SEQRES 11 A 315 THR LEU GLU GLU GLY GLY ARG LEU ASN MET GLU VAL ARG
SEQRES 12 A 315 VAL ASP ARG GLY VAL GLY TYR VAL PRO ALA GLU LYS HIS
SEQRES 13 A 315 GLY ILE LYS ASP ARG ILE ASN ALA ILE PRO VAL ASP ALA
SEQRES 14 A 315 VAL PHE SER PRO VAL ARG ARG VAL ALA PHE GLN VAL GLU
SEQRES 15 A 315 ASP THR ARG LEU GLY GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 16 A 315 THR LEU ARG ILE TRP THR ASP GLY SER VAL THR PRO LEU
SEQRES 17 A 315 GLU ALA LEU ASN GLN ALA VAL GLU ILE LEU ARG GLU HIS
SEQRES 18 A 315 LEU THR TYR PHE SER ASN PRO GLN ALA ALA ALA VAL ALA
SEQRES 19 A 315 ALA PRO GLU GLU ALA LYS GLU PRO GLU ALA PRO PRO GLU
SEQRES 20 A 315 GLN GLU GLU GLU LEU ASP LEU PRO LEU GLU GLU LEU GLY
SEQRES 21 A 315 LEU SER THR ARG VAL LEU HIS SER LEU LYS GLU GLU GLY
SEQRES 22 A 315 ILE GLU SER VAL ARG ALA LEU LEU ALA LEU ASN LEU LYS
SEQRES 23 A 315 ASP LEU LYS ASN ILE PRO GLY ILE GLY GLU ARG SER LEU
SEQRES 24 A 315 GLU GLU ILE LYS GLU ALA LEU GLU LYS LYS GLY PHE THR
SEQRES 25 A 315 LEU LYS GLU
SEQRES 1 B 315 MET LEU ASP SER LYS LEU LYS ALA PRO VAL PHE THR VAL
SEQRES 2 B 315 ARG THR GLN GLY ARG GLU TYR GLY GLU PHE VAL LEU GLU
SEQRES 3 B 315 PRO LEU GLU ARG GLY PHE GLY VAL THR LEU GLY ASN PRO
SEQRES 4 B 315 LEU ARG ARG ILE LEU LEU SER SER ILE PRO GLY THR ALA
SEQRES 5 B 315 VAL THR SER VAL TYR ILE GLU ASP VAL LEU HIS GLU PHE
SEQRES 6 B 315 SER THR ILE PRO GLY VAL LYS GLU ASP VAL VAL GLU ILE
SEQRES 7 B 315 ILE LEU ASN LEU LYS GLU LEU VAL VAL ARG PHE LEU ASN
SEQRES 8 B 315 PRO SER LEU GLN THR VAL THR LEU LEU LEU LYS ALA GLU
SEQRES 9 B 315 GLY PRO LYS GLU VAL LYS ALA ARG ASP PHE LEU PRO VAL
SEQRES 10 B 315 ALA ASP VAL GLU ILE MET ASN PRO ASP LEU HIS ILE ALA
SEQRES 11 B 315 THR LEU GLU GLU GLY GLY ARG LEU ASN MET GLU VAL ARG
SEQRES 12 B 315 VAL ASP ARG GLY VAL GLY TYR VAL PRO ALA GLU LYS HIS
SEQRES 13 B 315 GLY ILE LYS ASP ARG ILE ASN ALA ILE PRO VAL ASP ALA
SEQRES 14 B 315 VAL PHE SER PRO VAL ARG ARG VAL ALA PHE GLN VAL GLU
SEQRES 15 B 315 ASP THR ARG LEU GLY GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 16 B 315 THR LEU ARG ILE TRP THR ASP GLY SER VAL THR PRO LEU
SEQRES 17 B 315 GLU ALA LEU ASN GLN ALA VAL GLU ILE LEU ARG GLU HIS
SEQRES 18 B 315 LEU THR TYR PHE SER ASN PRO GLN ALA ALA ALA VAL ALA
SEQRES 19 B 315 ALA PRO GLU GLU ALA LYS GLU PRO GLU ALA PRO PRO GLU
SEQRES 20 B 315 GLN GLU GLU GLU LEU ASP LEU PRO LEU GLU GLU LEU GLY
SEQRES 21 B 315 LEU SER THR ARG VAL LEU HIS SER LEU LYS GLU GLU GLY
SEQRES 22 B 315 ILE GLU SER VAL ARG ALA LEU LEU ALA LEU ASN LEU LYS
SEQRES 23 B 315 ASP LEU LYS ASN ILE PRO GLY ILE GLY GLU ARG SER LEU
SEQRES 24 B 315 GLU GLU ILE LYS GLU ALA LEU GLU LYS LYS GLY PHE THR
SEQRES 25 B 315 LEU LYS GLU
SEQRES 1 C 1119 MET GLU ILE LYS ARG PHE GLY ARG ILE ARG GLU VAL ILE
SEQRES 2 C 1119 PRO LEU PRO PRO LEU THR GLU ILE GLN VAL GLU SER TYR
SEQRES 3 C 1119 ARG ARG ALA LEU GLN ALA ASP VAL PRO PRO GLU LYS ARG
SEQRES 4 C 1119 GLU ASN VAL GLY ILE GLN ALA ALA PHE ARG GLU THR PHE
SEQRES 5 C 1119 PRO ILE GLU GLU GLU ASP LYS GLY LYS GLY GLY LEU VAL
SEQRES 6 C 1119 LEU ASP PHE LEU GLU TYR ARG LEU GLY GLU PRO PRO PHE
SEQRES 7 C 1119 PRO GLN ASP GLU CYS ARG GLU LYS ASP LEU THR TYR GLN
SEQRES 8 C 1119 ALA PRO LEU TYR ALA ARG LEU GLN LEU ILE HIS LYS ASP
SEQRES 9 C 1119 THR GLY LEU ILE LYS GLU ASP GLU VAL PHE LEU GLY HIS
SEQRES 10 C 1119 ILE PRO LEU MET THR GLU ASP GLY SER PHE ILE ILE ASN
SEQRES 11 C 1119 GLY ALA ASP ARG VAL ILE VAL SER GLN ILE HIS ARG SER
SEQRES 12 C 1119 PRO GLY VAL TYR PHE THR PRO ASP PRO ALA ARG PRO GLY
SEQRES 13 C 1119 ARG TYR ILE ALA SER ILE ILE PRO LEU PRO LYS ARG GLY
SEQRES 14 C 1119 PRO TRP ILE ASP LEU GLU VAL GLU PRO ASN GLY VAL VAL
SEQRES 15 C 1119 SER MET LYS VAL ASN LYS ARG LYS PHE PRO LEU VAL LEU
SEQRES 16 C 1119 LEU LEU ARG VAL LEU GLY TYR ASP GLN GLU THR LEU ALA
SEQRES 17 C 1119 ARG GLU LEU GLY ALA TYR GLY GLU LEU VAL GLN GLY LEU
SEQRES 18 C 1119 MET ASP GLU SER VAL PHE ALA MET ARG PRO GLU GLU ALA
SEQRES 19 C 1119 LEU ILE ARG LEU PHE THR LEU LEU ARG PRO GLY ASP PRO
SEQRES 20 C 1119 PRO LYS ARG ASP LYS ALA VAL ALA TYR VAL TYR GLY LEU
SEQRES 21 C 1119 ILE ALA ASP PRO ARG ARG TYR ASP LEU GLY GLU ALA GLY
SEQRES 22 C 1119 ARG TYR LYS ALA GLU GLU LYS LEU GLY ILE ARG LEU SER
SEQRES 23 C 1119 GLY ARG THR LEU ALA ARG PHE GLU ASP GLY GLU PHE LYS
SEQRES 24 C 1119 ASP GLU VAL PHE LEU PRO THR LEU ARG TYR LEU PHE ALA
SEQRES 25 C 1119 LEU THR ALA GLY VAL PRO GLY HIS GLU VAL ASP ASP ILE
SEQRES 26 C 1119 ASP HIS LEU GLY ASN ARG ARG ILE ARG THR VAL GLY GLU
SEQRES 27 C 1119 LEU MET THR ASP GLN PHE ARG VAL GLY LEU ALA ARG LEU
SEQRES 28 C 1119 ALA ARG GLY VAL ARG GLU ARG MET LEU MET GLY SER GLU
SEQRES 29 C 1119 ASP SER LEU THR PRO ALA LYS LEU VAL ASN SER ARG PRO
SEQRES 30 C 1119 LEU GLU ALA ALA ILE ARG GLU PHE PHE SER ARG SER GLN
SEQRES 31 C 1119 LEU SER GLN PHE LYS ASP GLU THR ASN PRO LEU SER SER
SEQRES 32 C 1119 LEU ARG HIS LYS ARG ARG ILE SER ALA LEU GLY PRO GLY
SEQRES 33 C 1119 GLY LEU THR ARG GLU ARG ALA GLY PHE ASP VAL ARG ASP
SEQRES 34 C 1119 VAL HIS ARG THR HIS TYR GLY ARG ILE CYS PRO VAL GLU
SEQRES 35 C 1119 THR PRO GLU GLY ALA ASN ILE GLY LEU ILE THR SER LEU
SEQRES 36 C 1119 ALA ALA TYR ALA ARG VAL ASP GLU LEU GLY PHE ILE ARG
SEQRES 37 C 1119 THR PRO TYR ARG ARG VAL VAL GLY GLY VAL VAL THR ASP
SEQRES 38 C 1119 GLU VAL VAL TYR MET THR ALA THR GLU GLU ASP ARG TYR
SEQRES 39 C 1119 THR ILE ALA GLN ALA ASN THR PRO LEU GLU GLY ASN ARG
SEQRES 40 C 1119 ILE ALA ALA GLU ARG VAL VAL ALA ARG ARG LYS GLY GLU
SEQRES 41 C 1119 PRO VAL ILE VAL SER PRO GLU GLU VAL GLU PHE MET ASP
SEQRES 42 C 1119 VAL SER PRO LYS GLN VAL PHE SER VAL ASN THR ASN LEU
SEQRES 43 C 1119 ILE PRO PHE LEU GLU HIS ASP ASP ALA ASN ARG ALA LEU
SEQRES 44 C 1119 MET GLY SER ASN MET GLN THR GLN ALA VAL PRO LEU ILE
SEQRES 45 C 1119 ARG ALA GLN ALA PRO VAL VAL MET THR GLY LEU GLU GLU
SEQRES 46 C 1119 ARG VAL VAL ARG ASP SER LEU ALA ALA LEU TYR ALA GLU
SEQRES 47 C 1119 GLU ASP GLY GLU VAL ALA LYS VAL ASP GLY ASN ARG ILE
SEQRES 48 C 1119 VAL VAL ARG TYR GLU ASP GLY ARG LEU VAL GLU TYR PRO
SEQRES 49 C 1119 LEU ARG ARG PHE TYR ARG SER ASN GLN GLY THR ALA LEU
SEQRES 50 C 1119 ASP GLN ARG PRO ARG VAL VAL VAL GLY GLN ARG VAL ARG
SEQRES 51 C 1119 LYS GLY ASP LEU LEU ALA ASP GLY PRO ALA SER GLU ASN
SEQRES 52 C 1119 GLY PHE LEU ALA LEU GLY GLN ASN VAL LEU VAL ALA ILE
SEQRES 53 C 1119 MET PRO PHE ASP GLY TYR ASN PHE GLU ASP ALA ILE VAL
SEQRES 54 C 1119 ILE SER GLU GLU LEU LEU LYS ARG ASP PHE TYR THR SER
SEQRES 55 C 1119 ILE HIS ILE GLU ARG TYR GLU ILE GLU ALA ARG ASP THR
SEQRES 56 C 1119 LYS LEU GLY PRO GLU ARG ILE THR ARG ASP ILE PRO HIS
SEQRES 57 C 1119 LEU SER GLU ALA ALA LEU ARG ASP LEU ASP GLU GLU GLY
SEQRES 58 C 1119 VAL VAL ARG ILE GLY ALA GLU VAL LYS PRO GLY ASP ILE
SEQRES 59 C 1119 LEU VAL GLY ARG THR SER PHE LYS GLY GLU SER GLU PRO
SEQRES 60 C 1119 THR PRO GLU GLU ARG LEU LEU ARG SER ILE PHE GLY GLU
SEQRES 61 C 1119 LYS ALA ARG ASP VAL LYS ASP THR SER LEU ARG VAL PRO
SEQRES 62 C 1119 PRO GLY GLU GLY GLY ILE VAL VAL ARG THR VAL ARG LEU
SEQRES 63 C 1119 ARG ARG GLY ASP PRO GLY VAL GLU LEU LYS PRO GLY VAL
SEQRES 64 C 1119 ARG GLU VAL VAL ARG VAL TYR VAL ALA GLN LYS ARG LYS
SEQRES 65 C 1119 LEU GLN VAL GLY ASP LYS LEU ALA ASN ARG HIS GLY ASN
SEQRES 66 C 1119 LYS GLY VAL VAL ALA LYS ILE LEU PRO VAL GLU ASP MET
SEQRES 67 C 1119 PRO HIS LEU PRO ASP GLY THR PRO VAL ASP VAL ILE LEU
SEQRES 68 C 1119 ASN PRO LEU GLY VAL PRO SER ARG MET ASN LEU GLY GLN
SEQRES 69 C 1119 ILE LEU GLU THR HIS LEU GLY LEU ALA GLY TYR PHE LEU
SEQRES 70 C 1119 GLY GLN ARG TYR ILE SER PRO ILE PHE ASP GLY ALA LYS
SEQRES 71 C 1119 GLU PRO GLU ILE LYS GLU LEU LEU ALA GLN ALA PHE GLU
SEQRES 72 C 1119 VAL TYR PHE GLY LYS ARG LYS GLY GLU GLY PHE GLY VAL
SEQRES 73 C 1119 ASP LYS ARG GLU VAL GLU VAL LEU ARG ARG ALA GLU LYS
SEQRES 74 C 1119 LEU GLY LEU VAL THR PRO GLY LYS THR PRO GLU GLU GLN
SEQRES 75 C 1119 LEU LYS GLU LEU PHE LEU GLN GLY LYS VAL VAL LEU TYR
SEQRES 76 C 1119 ASP GLY ARG THR GLY GLU PRO ILE GLU GLY PRO ILE VAL
SEQRES 77 C 1119 VAL GLY GLN MET PHE ILE MET LYS LEU TYR HIS MET VAL
SEQRES 78 C 1119 GLU ASP LYS MET HIS ALA ARG SER THR GLY PRO TYR SER
SEQRES 79 C 1119 LEU ILE THR GLN GLN PRO LEU GLY GLY LYS ALA GLN PHE
SEQRES 80 C 1119 GLY GLY GLN ARG PHE GLY GLU MET GLU VAL TRP ALA LEU
SEQRES 81 C 1119 GLU ALA TYR GLY ALA ALA HIS THR LEU GLN GLU MET LEU
SEQRES 82 C 1119 THR LEU LYS SER ASP ASP ILE GLU GLY ARG ASN ALA ALA
SEQRES 83 C 1119 TYR GLU ALA ILE ILE LYS GLY GLU ASP VAL PRO GLU PRO
SEQRES 84 C 1119 SER VAL PRO GLU SER PHE ARG VAL LEU VAL LYS GLU LEU
SEQRES 85 C 1119 GLN ALA LEU ALA LEU ASP VAL GLN THR LEU ASP GLU LYS
SEQRES 86 C 1119 ASP ASN PRO VAL ASP ILE PHE GLU GLY LEU ALA SER LYS
SEQRES 87 C 1119 ARG
SEQRES 1 D 1534 MET LYS LYS GLU VAL ARG LYS VAL ARG ILE ALA LEU ALA
SEQRES 2 D 1534 SER PRO GLU LYS ILE ARG SER TRP SER TYR GLY GLU VAL
SEQRES 3 D 1534 GLU LYS PRO GLU THR ILE ASN TYR ARG THR LEU LYS PRO
SEQRES 4 D 1534 GLU ARG ASP GLY LEU PHE ASP GLU ARG ILE PHE GLY PRO
SEQRES 5 D 1534 ILE LYS ASP TYR GLU CYS ALA CYS GLY LYS TYR LYS ARG
SEQRES 6 D 1534 GLN ARG PHE GLU GLY LYS VAL CYS GLU ARG CYS GLY VAL
SEQRES 7 D 1534 GLU VAL THR LYS SER ILE VAL ARG ARG TYR ARG MET GLY
SEQRES 8 D 1534 HIS ILE GLU LEU ALA THR PRO ALA ALA HIS ILE TRP PHE
SEQRES 9 D 1534 VAL LYS ASP VAL PRO SER LYS ILE GLY THR LEU LEU ASP
SEQRES 10 D 1534 LEU SER ALA THR GLU LEU GLU GLN VAL LEU TYR PHE SER
SEQRES 11 D 1534 LYS TYR ILE VAL LEU ASP PRO LYS GLY ALA ILE LEU ASN
SEQRES 12 D 1534 GLY VAL PRO VAL GLU LYS ARG GLN LEU LEU THR ASP GLU
SEQRES 13 D 1534 GLU TYR ARG GLU LEU ARG TYR GLY LYS GLN GLU THR TYR
SEQRES 14 D 1534 PRO LEU PRO PRO GLY VAL ASP ALA LEU VAL LYS ASP GLY
SEQRES 15 D 1534 GLU GLU VAL VAL LYS GLY GLN GLU LEU ALA PRO GLY VAL
SEQRES 16 D 1534 VAL SER ARG LEU ASP GLY VAL ALA LEU TYR ARG PHE PRO
SEQRES 17 D 1534 ARG ARG VAL ARG VAL GLU TYR VAL LYS LYS GLU ARG ALA
SEQRES 18 D 1534 GLY LEU ARG LEU PRO LEU ALA ALA TRP VAL GLU LYS GLU
SEQRES 19 D 1534 ALA TYR LYS PRO GLY GLU ILE LEU ALA GLU LEU PRO GLU
SEQRES 20 D 1534 PRO TYR LEU PHE ARG ALA GLU GLU GLU GLY VAL VAL GLU
SEQRES 21 D 1534 LEU LYS GLU LEU GLU GLU GLY ALA PHE LEU VAL LEU ARG
SEQRES 22 D 1534 ARG GLU ASP GLU PRO VAL ALA THR TYR PHE LEU PRO VAL
SEQRES 23 D 1534 GLY MET THR PRO LEU VAL VAL HIS GLY GLU ILE VAL GLU
SEQRES 24 D 1534 LYS GLY GLN PRO LEU ALA GLU ALA LYS GLY LEU LEU ARG
SEQRES 25 D 1534 MET PRO ARG GLN VAL ARG ALA ALA GLN VAL GLU ALA GLU
SEQRES 26 D 1534 GLU GLU GLY GLU THR VAL TYR LEU THR LEU PHE LEU GLU
SEQRES 27 D 1534 TRP THR GLU PRO LYS ASP TYR ARG VAL GLN PRO HIS MET
SEQRES 28 D 1534 ASN VAL VAL VAL PRO GLU GLY ALA ARG VAL GLU ALA GLY
SEQRES 29 D 1534 ASP LYS ILE VAL ALA ALA ILE ASP PRO GLU GLU GLU VAL
SEQRES 30 D 1534 ILE ALA GLU ALA GLU GLY VAL VAL HIS LEU HIS GLU PRO
SEQRES 31 D 1534 ALA SER ILE LEU VAL VAL LYS ALA ARG VAL TYR PRO PHE
SEQRES 32 D 1534 GLU ASP ASP VAL GLU VAL SER THR GLY ASP ARG VAL ALA
SEQRES 33 D 1534 PRO GLY ASP VAL LEU ALA ASP GLY GLY LYS VAL LYS SER
SEQRES 34 D 1534 ASP VAL TYR GLY ARG VAL GLU VAL ASP LEU VAL ARG ASN
SEQRES 35 D 1534 VAL VAL ARG VAL VAL GLU SER TYR ASP ILE ASP ALA ARG
SEQRES 36 D 1534 MET GLY ALA GLU ALA ILE GLN GLN LEU LEU LYS GLU LEU
SEQRES 37 D 1534 ASP LEU GLU ALA LEU GLU LYS GLU LEU LEU GLU GLU MET
SEQRES 38 D 1534 LYS HIS PRO SER ARG ALA ARG ARG ALA LYS ALA ARG LYS
SEQRES 39 D 1534 ARG LEU GLU VAL VAL ARG ALA PHE LEU ASP SER GLY ASN
SEQRES 40 D 1534 ARG PRO GLU TRP MET ILE LEU GLU ALA VAL PRO VAL LEU
SEQRES 41 D 1534 PRO PRO ASP LEU ARG PRO MET VAL GLN VAL ASP GLY GLY
SEQRES 42 D 1534 ARG PHE ALA THR SER ASP LEU ASN ASP LEU TYR ARG ARG
SEQRES 43 D 1534 LEU ILE ASN ARG ASN ASN ARG LEU LYS LYS LEU LEU ALA
SEQRES 44 D 1534 GLN GLY ALA PRO GLU ILE ILE ILE ARG ASN GLU LYS ARG
SEQRES 45 D 1534 MET LEU GLN GLU ALA VAL ASP ALA LEU LEU ASP ASN GLY
SEQRES 46 D 1534 ARG ARG GLY ALA PRO VAL THR ASN PRO GLY SER ASP ARG
SEQRES 47 D 1534 PRO LEU ARG SER LEU THR ASP ILE LEU SER GLY LYS GLN
SEQRES 48 D 1534 GLY ARG PHE ARG GLN ASN LEU LEU GLY LYS ARG VAL ASP
SEQRES 49 D 1534 TYR SER GLY ARG SER VAL ILE VAL VAL GLY PRO GLN LEU
SEQRES 50 D 1534 LYS LEU HIS GLN CYS GLY LEU PRO LYS ARG MET ALA LEU
SEQRES 51 D 1534 GLU LEU PHE LYS PRO PHE LEU LEU LYS LYS MET GLU GLU
SEQRES 52 D 1534 LYS GLY ILE ALA PRO ASN VAL LYS ALA ALA ARG ARG MET
SEQRES 53 D 1534 LEU GLU ARG GLN ARG ASP ILE LYS ASP GLU VAL TRP ASP
SEQRES 54 D 1534 ALA LEU GLU GLU VAL ILE HIS GLY LYS VAL VAL LEU LEU
SEQRES 55 D 1534 ASN ARG ALA PRO THR LEU HIS ARG LEU GLY ILE GLN ALA
SEQRES 56 D 1534 PHE GLN PRO VAL LEU VAL GLU GLY GLN SER ILE GLN LEU
SEQRES 57 D 1534 HIS PRO LEU VAL CYS GLU ALA PHE ASN ALA ASP PHE ASP
SEQRES 58 D 1534 GLY ASP GLN MET ALA VAL HIS VAL PRO LEU SER SER PHE
SEQRES 59 D 1534 ALA GLN ALA GLU ALA ARG ILE GLN MET LEU SER ALA HIS
SEQRES 60 D 1534 ASN LEU LEU SER PRO ALA SER GLY GLU PRO LEU ALA LYS
SEQRES 61 D 1534 PRO SER ARG ASP ILE ILE LEU GLY LEU TYR TYR ILE THR
SEQRES 62 D 1534 GLN VAL ARG LYS GLU LYS LYS GLY ALA GLY LEU GLU PHE
SEQRES 63 D 1534 ALA THR PRO GLU GLU ALA LEU ALA ALA HIS GLU ARG GLY
SEQRES 64 D 1534 GLU VAL ALA LEU ASN ALA PRO ILE LYS VAL ALA GLY ARG
SEQRES 65 D 1534 GLU THR SER VAL GLY ARG LEU LYS TYR VAL PHE ALA ASN
SEQRES 66 D 1534 PRO ASP GLU ALA LEU LEU ALA VAL ALA HIS GLY ILE VAL
SEQRES 67 D 1534 ASP LEU GLN ASP VAL VAL THR VAL ARG TYR MET GLY LYS
SEQRES 68 D 1534 ARG LEU GLU THR SER PRO GLY ARG ILE LEU PHE ALA ARG
SEQRES 69 D 1534 ILE VAL ALA GLU ALA VAL GLU ASP GLU LYS VAL ALA TRP
SEQRES 70 D 1534 GLU LEU ILE GLN LEU ASP VAL PRO GLN GLU LYS ASN SER
SEQRES 71 D 1534 LEU LYS ASP LEU VAL TYR GLN ALA PHE LEU ARG LEU GLY
SEQRES 72 D 1534 MET GLU LYS THR ALA ARG LEU LEU ASP ALA LEU LYS TYR
SEQRES 73 D 1534 TYR GLY PHE THR PHE SER THR THR SER GLY ILE THR ILE
SEQRES 74 D 1534 GLY ILE ASP ASP ALA VAL ILE PRO GLU GLU LYS LYS GLN
SEQRES 75 D 1534 TYR LEU GLU GLU ALA ASP ARG LYS LEU LEU GLN ILE GLU
SEQRES 76 D 1534 GLN ALA TYR GLU MET GLY PHE LEU THR ASP ARG GLU ARG
SEQRES 77 D 1534 TYR ASP GLN ILE LEU GLN LEU TRP THR GLU THR THR GLU
SEQRES 78 D 1534 LYS VAL THR GLN ALA VAL PHE LYS ASN PHE GLU GLU ASN
SEQRES 79 D 1534 TYR PRO PHE ASN PRO LEU TYR VAL MET ALA GLN SER GLY
SEQRES 80 D 1534 ALA ARG GLY ASN PRO GLN GLN ILE ARG GLN LEU CYS GLY
SEQRES 81 D 1534 LEU ARG GLY LEU MET GLN LYS PRO SER GLY GLU THR PHE
SEQRES 82 D 1534 GLU VAL PRO VAL ARG SER SER PHE ARG GLU GLY LEU THR
SEQRES 83 D 1534 VAL LEU GLU TYR PHE ILE SER SER HIS GLY ALA ARG LYS
SEQRES 84 D 1534 GLY GLY ALA ASP THR ALA LEU ARG THR ALA ASP SER GLY
SEQRES 85 D 1534 TYR LEU THR ARG LYS LEU VAL ASP VAL THR HIS GLU ILE
SEQRES 86 D 1534 VAL VAL ARG GLU ALA ASP CYS GLY THR THR ASN TYR ILE
SEQRES 87 D 1534 SER VAL PRO LEU PHE GLN PRO ASP GLU VAL THR ARG SER
SEQRES 88 D 1534 LEU ARG LEU ARG LYS ARG ALA ASP ILE GLU ALA GLY LEU
SEQRES 89 D 1534 TYR GLY ARG VAL LEU ALA ARG GLU VAL GLU VAL LEU GLY
SEQRES 90 D 1534 VAL ARG LEU GLU GLU GLY ARG TYR LEU SER MET ASP ASP
SEQRES 91 D 1534 VAL HIS LEU LEU ILE LYS ALA ALA GLU ALA GLY GLU ILE
SEQRES 92 D 1534 GLN GLU VAL PRO VAL ARG SER PRO LEU THR CYS GLN THR
SEQRES 93 D 1534 ARG TYR GLY VAL CYS GLN LYS CYS TYR GLY TYR ASP LEU
SEQRES 94 D 1534 SER MET ALA ARG PRO VAL SER ILE GLY GLU ALA VAL GLY
SEQRES 95 D 1534 ILE VAL ALA ALA GLN SER ILE GLY GLU PRO GLY THR GLN
SEQRES 96 D 1534 LEU THR MET ARG THR PHE HIS THR GLY GLY VAL ALA GLY
SEQRES 97 D 1534 ALA ALA ASP ILE THR GLN GLY LEU PRO ARG VAL ILE GLU
SEQRES 98 D 1534 LEU PHE GLU ALA ARG ARG PRO LYS ALA LYS ALA VAL ILE
SEQRES 99 D 1534 SER GLU ILE ASP GLY VAL VAL ARG ILE GLU GLU THR GLU
SEQRES 100 D 1534 GLU LYS LEU SER VAL PHE VAL GLU SER GLU GLY PHE SER
SEQRES 101 D 1534 LYS GLU TYR LYS LEU PRO LYS GLU ALA ARG LEU LEU VAL
SEQRES 102 D 1534 LYS ASP GLY ASP TYR VAL GLU ALA GLY GLN PRO LEU THR
SEQRES 103 D 1534 ARG GLY ALA ILE ASP PRO HIS GLN LEU LEU GLU ALA LYS
SEQRES 104 D 1534 GLY PRO GLU ALA VAL GLU ARG TYR LEU VAL GLU GLU ILE
SEQRES 105 D 1534 GLN LYS VAL TYR ARG ALA GLN GLY VAL LYS LEU HIS ASP
SEQRES 106 D 1534 LYS HIS ILE GLU ILE VAL VAL ARG GLN MET MET LYS TYR
SEQRES 107 D 1534 VAL GLU VAL THR ASP PRO GLY ASP SER ARG LEU LEU GLU
SEQRES 108 D 1534 GLY GLN VAL LEU GLU LYS TRP ASP VAL GLU ALA LEU ASN
SEQRES 109 D 1534 GLU ARG LEU ILE ALA GLU GLY LYS THR PRO VAL ALA TRP
SEQRES 110 D 1534 LYS PRO LEU LEU MET GLY VAL THR LYS SER ALA LEU SER
SEQRES 111 D 1534 THR LYS SER TRP LEU SER ALA ALA SER PHE GLN ASN THR
SEQRES 112 D 1534 THR HIS VAL LEU THR GLU ALA ALA ILE ALA GLY LYS LYS
SEQRES 113 D 1534 ASP GLU LEU ILE GLY LEU LYS GLU ASN VAL ILE LEU GLY
SEQRES 114 D 1534 ARG LEU ILE PRO ALA GLY THR GLY SER ASP PHE VAL ARG
SEQRES 115 D 1534 PHE THR GLN VAL VAL ASP GLN LYS THR LEU LYS ALA ILE
SEQRES 116 D 1534 GLU GLU ALA ARG LYS GLU ALA VAL GLU ALA LYS GLU ARG
SEQRES 117 D 1534 PRO ALA ALA ARG ARG GLY VAL LYS ARG GLU GLN PRO GLY
SEQRES 118 D 1534 LYS GLN ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 E 99 MET ALA GLU PRO GLY ILE ASP LYS LEU PHE GLY MET VAL
SEQRES 2 E 99 ASP SER LYS TYR ARG LEU THR VAL VAL VAL ALA LYS ARG
SEQRES 3 E 99 ALA GLN GLN LEU LEU ARG HIS GLY PHE LYS ASN THR VAL
SEQRES 4 E 99 LEU GLU PRO GLU GLU ARG PRO LYS MET GLN THR LEU GLU
SEQRES 5 E 99 GLY LEU PHE ASP ASP PRO ASN ALA VAL THR TRP ALA MET
SEQRES 6 E 99 LYS GLU LEU LEU THR GLY ARG LEU VAL PHE GLY GLU ASN
SEQRES 7 E 99 LEU VAL PRO GLU ASP ARG LEU GLN LYS GLU MET GLU ARG
SEQRES 8 E 99 LEU TYR PRO VAL GLU ARG GLU GLU
SEQRES 1 N 13 DG DG DA DA DG DA DG DA DT DT DC DC DC
SEQRES 1 R 16 U C A G G C G A U G U G U
SEQRES 2 R 16 G C U
SEQRES 1 T 22 DG DG DG DA DA DT DC DT DC DT DT DC DC
SEQRES 2 T 22 DA DG DC DA DC DA DC DA DT
HET ZN D1601 1
HET ZN D1602 1
HET MG D1603 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 9 ZN 2(ZN 2+)
FORMUL 11 MG MG 2+
HELIX 1 1 GLY A 33 SER A 47 1 15
HELIX 2 2 ASP A 74 GLU A 84 1 11
HELIX 3 3 ARG A 112 PHE A 114 5 3
HELIX 4 4 PRO A 152 GLY A 157 1 6
HELIX 5 5 THR A 206 THR A 223 1 18
HELIX 6 6 TYR A 224 SER A 226 5 3
HELIX 7 7 GLY B 31 LEU B 45 1 15
HELIX 8 8 ASP B 74 LEU B 85 1 12
HELIX 9 9 PRO B 152 HIS B 156 5 5
HELIX 10 10 THR B 206 THR B 223 1 18
HELIX 11 11 GLN C 22 ALA C 29 1 8
HELIX 12 12 GLY C 43 THR C 51 1 9
HELIX 13 13 ASP C 81 LYS C 86 1 6
HELIX 14 14 LEU C 193 LEU C 200 1 8
HELIX 15 15 ASP C 203 ALA C 213 1 11
HELIX 16 16 GLY C 215 LEU C 217 5 3
HELIX 17 17 VAL C 218 ASP C 223 1 6
HELIX 18 18 GLU C 232 ARG C 243 1 12
HELIX 19 19 LYS C 249 TYR C 258 1 10
HELIX 20 20 GLU C 271 LEU C 281 1 11
HELIX 21 21 VAL C 302 THR C 314 1 13
HELIX 22 22 THR C 335 ARG C 358 1 24
HELIX 23 23 MET C 359 GLY C 362 5 4
HELIX 24 24 ARG C 376 SER C 389 1 14
HELIX 25 25 ASN C 399 ARG C 408 1 10
HELIX 26 26 HIS C 431 TYR C 435 5 5
HELIX 27 27 THR C 487 ASP C 492 1 6
HELIX 28 28 SER C 535 VAL C 539 5 5
HELIX 29 29 ASN C 543 ILE C 547 5 5
HELIX 30 30 PHE C 549 ASP C 553 5 5
HELIX 31 31 ASP C 554 GLN C 565 1 12
HELIX 32 32 THR C 566 ALA C 568 5 3
HELIX 33 33 LEU C 583 SER C 591 1 9
HELIX 34 34 GLU C 692 ARG C 697 1 6
HELIX 35 35 GLU C 731 ARG C 735 5 5
HELIX 36 36 ASN C 872 MET C 880 5 9
HELIX 37 37 LEU C 882 GLY C 898 1 17
HELIX 38 38 LYS C 910 GLY C 933 1 24
HELIX 39 39 ASP C 937 GLY C 951 1 15
HELIX 40 40 THR C 958 GLN C 969 1 12
HELIX 41 41 GLY C 1033 GLY C 1044 1 12
HELIX 42 42 ALA C 1045 THR C 1054 1 10
HELIX 43 43 GLY C 1062 GLY C 1073 1 12
HELIX 44 44 PRO C 1082 ALA C 1094 1 13
HELIX 45 45 SER D 14 TRP D 21 1 8
HELIX 46 46 LYS D 82 ARG D 89 1 8
HELIX 47 47 HIS D 101 LYS D 106 1 6
HELIX 48 48 THR D 121 PHE D 129 1 9
HELIX 49 49 THR D 154 TYR D 163 1 10
HELIX 50 50 GLY D 457 GLU D 467 1 11
HELIX 51 51 ASP D 469 MET D 481 1 13
HELIX 52 52 SER D 485 ASP D 504 1 20
HELIX 53 53 ARG D 508 TRP D 511 5 4
HELIX 54 54 ASP D 539 GLN D 560 1 22
HELIX 55 55 PRO D 563 ASP D 583 1 21
HELIX 56 56 ARG D 615 GLY D 620 1 6
HELIX 57 57 LYS D 646 PHE D 653 1 8
HELIX 58 58 PHE D 653 LYS D 664 1 12
HELIX 59 59 ASN D 669 LEU D 677 1 9
HELIX 60 60 LYS D 684 HIS D 696 1 13
HELIX 61 61 HIS D 709 LEU D 711 5 3
HELIX 62 62 PRO D 730 GLU D 734 5 5
HELIX 63 63 SER D 752 MET D 763 1 12
HELIX 64 64 LEU D 764 ASN D 768 5 5
HELIX 65 65 SER D 782 THR D 793 1 12
HELIX 66 66 ALA D 814 LEU D 823 1 10
HELIX 67 67 SER D 835 TYR D 841 1 7
HELIX 68 68 ASN D 845 ALA D 854 1 10
HELIX 69 69 SER D 876 GLU D 891 1 16
HELIX 70 70 ASP D 892 ILE D 900 1 9
HELIX 71 71 GLU D 907 GLY D 923 1 17
HELIX 72 72 GLY D 923 GLY D 946 1 24
HELIX 73 73 GLU D 959 GLY D 981 1 23
HELIX 74 74 THR D 984 TYR D 1015 1 32
HELIX 75 75 ASN D 1018 SER D 1026 1 9
HELIX 76 76 ASN D 1031 CYS D 1039 1 9
HELIX 77 77 THR D 1066 LEU D 1086 1 21
HELIX 78 78 ARG D 1087 ALA D 1089 5 3
HELIX 79 79 ASP D 1090 ASP D 1100 1 11
HELIX 80 80 LYS D 1136 TYR D 1145 1 10
HELIX 81 81 SER D 1167 GLY D 1181 1 15
HELIX 82 82 SER D 1190 CYS D 1194 5 5
HELIX 83 83 CYS D 1201 GLY D 1206 1 6
HELIX 84 84 ALA D 1220 GLU D 1231 1 12
HELIX 85 85 PRO D 1232 THR D 1234 5 3
HELIX 86 86 GLY D 1255 GLU D 1264 1 10
HELIX 87 87 ASP D 1331 LYS D 1339 1 9
HELIX 88 88 GLY D 1340 GLN D 1359 1 20
HELIX 89 89 HIS D 1364 MET D 1375 1 12
HELIX 90 90 LEU D 1395 ILE D 1408 1 14
HELIX 91 91 GLY D 1423 LEU D 1429 1 7
HELIX 92 92 SER D 1433 PHE D 1440 1 8
HELIX 93 93 ASN D 1442 ILE D 1452 1 11
HELIX 94 94 GLY D 1461 GLY D 1469 1 9
HELIX 95 95 ALA D 1474 GLY D 1477 5 4
HELIX 96 96 SER D 1478 PHE D 1483 1 6
HELIX 97 97 GLN D 1489 ARG D 1499 1 11
HELIX 98 98 GLY E 5 VAL E 13 1 9
HELIX 99 99 SER E 15 HIS E 33 1 19
HELIX 100 100 GLU E 52 ASP E 56 5 5
HELIX 101 101 ALA E 60 LEU E 69 1 10
HELIX 102 102 PRO E 81 LEU E 92 1 12
SHEET 1 A 4 VAL A 10 VAL A 13 0
SHEET 2 A 4 TYR A 20 LEU A 28 -1 O VAL A 24 N THR A 12
SHEET 3 A 4 ASP A 193 THR A 201 -1 O ASP A 193 N LEU A 28
SHEET 4 A 4 VAL A 174 GLU A 182 -1 N ARG A 175 O TRP A 200
SHEET 1 B 4 THR A 96 GLU A 104 0
SHEET 2 B 4 ARG A 137 ASP A 145 -1 O MET A 140 N LEU A 101
SHEET 3 B 4 ALA A 52 ILE A 58 -1 N TYR A 57 O GLU A 141
SHEET 4 B 4 ILE A 165 PRO A 166 -1 O ILE A 165 N VAL A 56
SHEET 1 C 2 VAL A 87 ARG A 88 0
SHEET 2 C 2 GLU A 121 ILE A 122 -1 O GLU A 121 N ARG A 88
SHEET 1 D 2 GLU A 108 LYS A 110 0
SHEET 2 D 2 HIS A 128 THR A 131 -1 O ALA A 130 N VAL A 109
SHEET 1 E 2 GLY A 149 VAL A 151 0
SHEET 2 E 2 ALA A 169 PHE A 171 -1 O ALA A 169 N VAL A 151
SHEET 1 F 4 VAL B 10 GLN B 16 0
SHEET 2 F 4 TYR B 20 GLU B 26 -1 O GLU B 22 N ARG B 14
SHEET 3 F 4 LEU B 192 THR B 201 -1 O LEU B 197 N PHE B 23
SHEET 4 F 4 VAL B 174 THR B 184 -1 N ARG B 175 O TRP B 200
SHEET 1 G 4 THR B 96 GLU B 104 0
SHEET 2 G 4 ARG B 137 ASP B 145 -1 O VAL B 142 N LEU B 99
SHEET 3 G 4 ALA B 52 ILE B 58 -1 N TYR B 57 O GLU B 141
SHEET 4 G 4 ILE B 165 PRO B 166 -1 O ILE B 165 N VAL B 56
SHEET 1 H 2 VAL B 87 PHE B 89 0
SHEET 2 H 2 VAL B 120 ILE B 122 -1 O GLU B 121 N ARG B 88
SHEET 1 I 2 GLU B 108 LYS B 110 0
SHEET 2 I 2 HIS B 128 THR B 131 -1 O ALA B 130 N VAL B 109
SHEET 1 J 2 TYR B 150 VAL B 151 0
SHEET 2 J 2 ALA B 169 VAL B 170 -1 O ALA B 169 N VAL B 151
SHEET 1 K 3 ILE C 3 ARG C 5 0
SHEET 2 K 3 ARG C 900 ILE C 902 1 O ILE C 902 N LYS C 4
SHEET 3 K 3 VAL C 579 MET C 580 1 N MET C 580 O TYR C 901
SHEET 1 L 3 VAL C 65 PHE C 68 0
SHEET 2 L 3 ARG C 97 ILE C 101 -1 O ILE C 101 N VAL C 65
SHEET 3 L 3 LEU C 107 GLU C 112 -1 O ILE C 108 N LEU C 100
SHEET 1 M 2 GLN C 91 PRO C 93 0
SHEET 2 M 2 HIS C 117 PRO C 119 -1 O ILE C 118 N ALA C 92
SHEET 1 N 3 PHE C 127 ILE C 128 0
SHEET 2 N 3 ASP C 133 ILE C 136 -1 O ARG C 134 N PHE C 127
SHEET 3 N 3 SER C 392 PHE C 394 -1 O GLN C 393 N VAL C 135
SHEET 1 O 4 ARG C 331 ARG C 334 0
SHEET 2 O 4 SER C 138 ARG C 142 -1 N GLN C 139 O ARG C 334
SHEET 3 O 4 ARG C 409 SER C 411 1 O SER C 411 N SER C 138
SHEET 4 O 4 ILE C 452 SER C 454 -1 O THR C 453 N ILE C 410
SHEET 1 P 5 VAL C 146 PRO C 150 0
SHEET 2 P 5 TYR C 158 ILE C 162 -1 O ILE C 159 N THR C 149
SHEET 3 P 5 ILE C 172 VAL C 176 -1 O LEU C 174 N ALA C 160
SHEET 4 P 5 VAL C 182 LYS C 185 -1 O SER C 183 N GLU C 175
SHEET 5 P 5 LYS C 190 PRO C 192 -1 O PHE C 191 N MET C 184
SHEET 1 Q 3 ARG C 460 VAL C 461 0
SHEET 2 Q 3 ILE C 467 VAL C 475 -1 O ARG C 468 N ARG C 460
SHEET 3 Q 3 VAL C 478 MET C 486 -1 O VAL C 478 N VAL C 475
SHEET 1 R 4 PRO C 521 VAL C 524 0
SHEET 2 R 4 VAL C 513 ARG C 516 -1 N VAL C 513 O VAL C 524
SHEET 3 R 4 ILE C 496 ALA C 497 -1 N ILE C 496 O ARG C 516
SHEET 4 R 4 PHE C 531 MET C 532 1 O PHE C 531 N ALA C 497
SHEET 1 S 2 LEU C 503 GLU C 504 0
SHEET 2 S 2 ARG C 507 ILE C 508 -1 O ARG C 507 N GLU C 504
SHEET 1 T 4 GLU C 622 PRO C 624 0
SHEET 2 T 4 ARG C 610 TYR C 615 -1 N ILE C 611 O TYR C 623
SHEET 3 T 4 GLY C 601 VAL C 606 -1 N GLU C 602 O ARG C 614
SHEET 4 T 4 ARG C 648 VAL C 649 -1 O VAL C 649 N GLY C 601
SHEET 1 U 2 TYR C 629 ARG C 630 0
SHEET 2 U 2 ALA C 636 LEU C 637 -1 O LEU C 637 N TYR C 629
SHEET 1 V 2 ARG C 640 PRO C 641 0
SHEET 2 V 2 ALA C 656 ASP C 657 -1 O ASP C 657 N ARG C 640
SHEET 1 W 2 SER C 661 GLU C 662 0
SHEET 2 W 2 PHE C 665 LEU C 666 -1 O PHE C 665 N GLU C 662
SHEET 1 X 8 LYS C 971 VAL C 972 0
SHEET 2 X 8 ILE C 987 LYS C 996 -1 O ILE C 987 N VAL C 972
SHEET 3 X 8 LYS C 838 ALA C 840 -1 N ALA C 840 O MET C 995
SHEET 4 X 8 GLY C 847 LEU C 853 -1 O GLY C 847 N LEU C 839
SHEET 5 X 8 ILE C 688 SER C 691 1 N ILE C 688 O VAL C 848
SHEET 6 X 8 VAL C 869 LEU C 871 -1 O ILE C 870 N VAL C 689
SHEET 7 X 8 GLN C 670 ILE C 676 1 N ALA C 675 O VAL C 869
SHEET 8 X 8 ILE C 987 LYS C 996 -1 O ILE C 994 N GLN C 670
SHEET 1 Y 3 HIS C 704 TYR C 708 0
SHEET 2 Y 3 VAL C 819 GLN C 829 -1 O GLN C 829 N HIS C 704
SHEET 3 Y 3 GLU C 711 ARG C 713 -1 N ALA C 712 O ARG C 820
SHEET 1 Z 4 HIS C 704 TYR C 708 0
SHEET 2 Z 4 VAL C 819 GLN C 829 -1 O GLN C 829 N HIS C 704
SHEET 3 Z 4 GLY C 798 LEU C 806 -1 N ILE C 799 O ALA C 828
SHEET 4 Z 4 GLU C 748 VAL C 749 -1 N VAL C 749 O GLY C 798
SHEET 1 AA 2 ARG C 721 ILE C 722 0
SHEET 2 AA 2 ARG C 758 THR C 759 -1 O THR C 759 N ARG C 721
SHEET 1 AB 2 ILE C 754 VAL C 756 0
SHEET 2 AB 2 LEU C 790 ARG C 791 -1 O LEU C 790 N LEU C 755
SHEET 1 AC 8 HIS C1006 ARG C1008 0
SHEET 2 AC 8 SER D 626 VAL D 633 -1 O SER D 626 N ARG C1008
SHEET 3 AC 8 GLN D 744 HIS D 748 -1 O MET D 745 N SER D 629
SHEET 4 AC 8 VAL D 700 ASN D 703 -1 N LEU D 701 O HIS D 748
SHEET 5 AC 8 ILE D 713 VAL D 721 -1 O PHE D 716 N VAL D 700
SHEET 6 AC 8 GLN D 641 PRO D 645 1 N CYS D 642 O GLN D 717
SHEET 7 AC 8 ILE D 726 LEU D 728 -1 O GLN D 727 N GLY D 643
SHEET 8 AC 8 SER D 626 VAL D 633 1 N VAL D 632 O LEU D 728
SHEET 1 AD 3 LEU C1097 LEU C1102 0
SHEET 2 AD 3 LYS D 7 LEU D 12 -1 O ARG D 9 N GLN C1100
SHEET 3 AD 3 LYS D1455 ASP D1457 -1 O ASP D1457 N VAL D 8
SHEET 1 AE 3 SER D 22 GLU D 25 0
SHEET 2 AE 3 MET D 90 ALA D 100 1 O MET D 90 N TYR D 23
SHEET 3 AE 3 ILE D 513 VAL D 519 -1 O VAL D 519 N GLY D 91
SHEET 1 AF 2 VAL D 202 LEU D 204 0
SHEET 2 AF 2 LEU D 394 VAL D 396 -1 O VAL D 396 N VAL D 202
SHEET 1 AG 2 ALA D 359 VAL D 361 0
SHEET 2 AG 2 GLY D 383 VAL D 385 -1 O GLY D 383 N VAL D 361
SHEET 1 AH 3 ALA D 398 PRO D 402 0
SHEET 2 AH 3 VAL D 443 VAL D 447 -1 O VAL D 444 N TYR D 401
SHEET 3 AH 3 VAL D 435 ASP D 438 -1 N ASP D 438 O VAL D 443
SHEET 1 AI 2 VAL D 420 ALA D 422 0
SHEET 2 AI 2 VAL D 427 LYS D 428 -1 O VAL D 427 N LEU D 421
SHEET 1 AJ 2 VAL D 528 GLN D 529 0
SHEET 2 AJ 2 PHE D 535 ALA D 536 -1 O ALA D 536 N VAL D 528
SHEET 1 AK 2 VAL D 864 TYR D 868 0
SHEET 2 AK 2 LYS D 871 THR D 875 -1 O LEU D 873 N VAL D 866
SHEET 1 AL 2 ILE D1118 PRO D1121 0
SHEET 2 AL 2 GLU D1185 VAL D1188 -1 O VAL D1188 N ILE D1118
SHEET 1 AM 2 PHE D1123 GLN D1124 0
SHEET 2 AM 2 ARG D1133 LEU D1134 -1 O ARG D1133 N GLN D1124
SHEET 1 AN 2 VAL D1153 GLU D1154 0
SHEET 2 AN 2 ARG D1159 LEU D1160 -1 O LEU D1160 N VAL D1153
SHEET 1 AO 3 GLY D1392 VAL D1394 0
SHEET 2 AO 3 TYR D1378 VAL D1381 -1 N VAL D1379 O GLN D1393
SHEET 3 AO 3 TRP D1417 PRO D1419 -1 O LYS D1418 N GLU D1380
SHEET 1 AP 2 VAL D1487 ASP D1488 0
SHEET 2 AP 2 LEU E 73 VAL E 74 -1 O VAL E 74 N VAL D1487
LINK SG CYS D 73 ZN ZN D1601 1555 1555 2.72
LINK OD1 ASP D 739 MG MG D1603 1555 1555 2.33
LINK OD2 ASP D 739 MG MG D1603 1555 1555 2.72
LINK OD1 ASP D 741 MG MG D1603 1555 1555 2.98
LINK OD1 ASP D 743 MG MG D1603 1555 1555 2.95
LINK SG CYS D1112 ZN ZN D1602 1555 1555 2.55
LINK SG CYS D1194 ZN ZN D1602 1555 1555 2.70
LINK SG CYS D1201 ZN ZN D1602 1555 1555 2.65
LINK SG CYS D1204 ZN ZN D1602 1555 1555 2.33
LINK MG MG D1603 O3' U R 29 1555 1555 2.17
CISPEP 1 GLU A 26 PRO A 27 0 3.94
CISPEP 2 GLU B 26 PRO B 27 0 1.90
CISPEP 3 LEU C 165 PRO C 166 0 1.73
SITE 1 AC1 5 CYS D 58 CYS D 60 LYS D 62 CYS D 73
SITE 2 AC1 5 CYS D 76
SITE 1 AC2 4 CYS D1112 CYS D1194 CYS D1201 CYS D1204
SITE 1 AC3 4 ASP D 739 ASP D 741 ASP D 743 U R 29
CRYST1 286.549 286.549 199.411 90.00 90.00 120.00 H 3 18
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 0.003490 0.002015 0.000000 0.00000
SCALE2 0.000000 0.004030 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005015 0.00000
(ATOM LINES ARE NOT SHOWN.)
END