HEADER TRANSCRIPTION 30-SEP-11 4A3J
TITLE RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A 2NT
TITLE 2 DNA-RNA HYBRID AND SOAKED WITH GMPCPP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-1732;
COMPND 5 SYNONYM: RPB1, RNA POLYMERASE II SUBUNIT 1, RNA POLYMERASE II
COMPND 6 SUBUNIT B1, DNA-DIRECTED RNA POLYMERASE III LARGEST SUBUNIT, RNA
COMPND 7 POLYMERASE II SUBUNIT B220;
COMPND 8 EC: 2.7.7.6;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: RPB2, RNA POLYMERASE II SUBUNIT 2, B150, DNA-DIRECTED RNA
COMPND 13 POLYMERASE II 140 KDA POLYPEPTIDE;
COMPND 14 EC: 2.7.7.6;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3;
COMPND 17 CHAIN: C;
COMPND 18 SYNONYM: RPB3, RNA POLYMERASE II SUBUNIT 3, RNA POLYMERASE II
COMPND 19 SUBUNIT B3, B44.5, DNA-DIRECTED RNA POLYMERASE II 45 KDA
COMPND 20 POLYPEPTIDE;
COMPND 21 MOL_ID: 4;
COMPND 22 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4;
COMPND 23 CHAIN: D;
COMPND 24 SYNONYM: RPB4, RNA POLYMERASE II SUBUNIT B4, B32, DNA-DIRECTED RNA
COMPND 25 POLYMERASE II 32 KDA POLYPEPTIDE;
COMPND 26 MOL_ID: 5;
COMPND 27 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC
COMPND 28 1;
COMPND 29 CHAIN: E;
COMPND 30 SYNONYM: RPB5, RNA POLYMERASES I\,II\,AND III SUBUNIT ABC1, ABC27,
COMPND 31 DNA-DIRECTED RNA POLYMERASES I\,II\,AND III 27 KDA POLYPEPTIDE;
COMPND 32 MOL_ID: 6;
COMPND 33 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC
COMPND 34 2;
COMPND 35 CHAIN: F;
COMPND 36 SYNONYM: RPB6, RNA POLYMERASES I\,II\,AND III SUBUNIT ABC2, ABC23,
COMPND 37 DNA-DIRECTED RNA POLYMERASES I\,II\,AND III 23 KDA POLYPEPTIDE;
COMPND 38 MOL_ID: 7;
COMPND 39 MOLECULE: RPB7, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7;
COMPND 40 CHAIN: G;
COMPND 41 SYNONYM: RNA POLYMERASE II SUBUNIT B7, B16;
COMPND 42 MOL_ID: 8;
COMPND 43 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC
COMPND 44 3;
COMPND 45 CHAIN: H;
COMPND 46 SYNONYM: RPB8, RNA POLYMERASES I\,II\,AND III SUBUNIT ABC3,
COMPND 47 ABC14.4, ABC14.5, DNA-DIRECTED RNA POLYMERASES I\,II\,AND III 14.5
COMPND 48 KDA POLYPEPTIDE;
COMPND 49 MOL_ID: 9;
COMPND 50 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9;
COMPND 51 CHAIN: I;
COMPND 52 SYNONYM: RBP9, RNA POLYMERASE II SUBUNIT B9, B12.6, DNA-DIRECTED
COMPND 53 RNA POLYMERASE II 14.2 KDA POLYPEPTIDE, DNA-DIRECTED RNA
COMPND 54 POLYMERASE II SUBUNIT 9;
COMPND 55 MOL_ID: 10;
COMPND 56 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC
COMPND 57 5;
COMPND 58 CHAIN: J;
COMPND 59 SYNONYM: RPB10, RNA POLYMERASES I\,II\,AND III SUBUNIT ABC5,
COMPND 60 ABC10-BETA, ABC8, DNA-DIRECTED RNA POLYMERASES I\,II\,AND III 8.3
COMPND 61 KDA POLYPEPTIDE;
COMPND 62 MOL_ID: 11;
COMPND 63 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11;
COMPND 64 CHAIN: K;
COMPND 65 SYNONYM: RPB11, RNA POLYMERASE II SUBUNIT B11, B13.6, DNA-DIRECTED
COMPND 66 RNA POLYMERASE II 13.6 KDA POLYPEPTIDE;
COMPND 67 MOL_ID: 12;
COMPND 68 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC
COMPND 69 4;
COMPND 70 CHAIN: L;
COMPND 71 SYNONYM: RPB12, RNA POLYMERASES I\,II\,AND III SUBUNIT ABC4,
COMPND 72 ABC10-ALPHA;
COMPND 73 MOL_ID: 13;
COMPND 74 MOLECULE: 5'-D(*GP*TP*AP*GP*AP*AP*AP*GP*CP*TP*AP*GP*CP*TP)-3';
COMPND 75 CHAIN: N;
COMPND 76 SYNONYM: NON TEMPLATE DNA;
COMPND 77 MOL_ID: 14;
COMPND 78 MOLECULE: 5'-R(*CP*AP)-3';
COMPND 79 CHAIN: P;
COMPND 80 SYNONYM: TRANSCRIPT RNA;
COMPND 81 MOL_ID: 15;
COMPND 82 MOLECULE: 5'-D(*AP*GP*CP*TP*AP*GP*CP*TP*TP*TP*CP*BRUP*AP*CP*CP
COMPND 83 *TP*GP*AP*AP*CP*AP*AP*CP*TP*AP*AP*CP)-3';
COMPND 84 CHAIN: T;
COMPND 85 SYNONYM: TEMPLATE DNA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 8 ORGANISM_TAXID: 4932;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 4932;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 15 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 16 ORGANISM_TAXID: 4932;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 4932;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 27 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 28 ORGANISM_TAXID: 4932;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 31 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 32 ORGANISM_TAXID: 4932;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 35 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 36 ORGANISM_TAXID: 4932;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 39 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 40 ORGANISM_TAXID: 4932;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 4932;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 47 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 48 ORGANISM_TAXID: 4932;
SOURCE 49 MOL_ID: 13;
SOURCE 50 SYNTHETIC: YES;
SOURCE 51 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 52 ORGANISM_TAXID: 32630;
SOURCE 53 MOL_ID: 14;
SOURCE 54 SYNTHETIC: YES;
SOURCE 55 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 56 ORGANISM_TAXID: 32630;
SOURCE 57 MOL_ID: 15;
SOURCE 58 SYNTHETIC: YES;
SOURCE 59 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 60 ORGANISM_TAXID: 32630
KEYWDS TRANSCRIPTION, TRANSCRIPTION INITIATION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.M.CHEUNG,S.SAINSBURY,P.CRAMER
REVDAT 2 14-DEC-11 4A3J 1 JRNL
REVDAT 1 07-DEC-11 4A3J 0
JRNL AUTH A.C.M.CHEUNG,S.SAINSBURY,P.CRAMER
JRNL TITL STRUCTURAL BASIS OF INITIAL RNA POLYMERASE II TRANSCRIPTION.
JRNL REF EMBO J. V. 30 4755 2011
JRNL REFN ISSN 0261-4189
JRNL PMID 22056778
JRNL DOI 10.1038/EMBOJ.2011.396
REMARK 2
REMARK 2 RESOLUTION. 3.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.35
REMARK 3 NUMBER OF REFLECTIONS : 128317
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1575
REMARK 3 R VALUE (WORKING SET) : 0.1567
REMARK 3 FREE R VALUE : 0.1939
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.97
REMARK 3 FREE R VALUE TEST SET COUNT : 2526
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.80
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.35
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 9493
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2305
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9323
REMARK 3 BIN R VALUE (WORKING SET) : 0.2302
REMARK 3 BIN FREE R VALUE : 0.2475
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.79
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 170
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 31210
REMARK 3 NUCLEIC ACID ATOMS : 551
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 87.38
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 136.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.3662
REMARK 3 B22 (A**2) : 18.9004
REMARK 3 B33 (A**2) : -19.2666
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.831
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.310
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.346
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 3.122
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.359
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9476
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9275
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 32419 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 43883 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 11624 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 858 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 4575 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 32419 ; 20.00 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.00 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 4274 ; 5.00 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : 64 ; 1.00 ; HARMONIC
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 37907 ; 4.00 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.35
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.82
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 24.46
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN N
REMARK 3 ORIGIN FOR THE GROUP (A): 94.4321 71.8391 -19.6822
REMARK 3 T TENSOR
REMARK 3 T11: 0.0640 T22: -0.0146
REMARK 3 T33: 0.0503 T12: 0.0428
REMARK 3 T13: -0.0490 T23: -0.0530
REMARK 3 L TENSOR
REMARK 3 L11: 0.8547 L22: 1.3527
REMARK 3 L33: 0.0000 L12: 0.0750
REMARK 3 L13: -2.7735 L23: 1.3068
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: 0.0165 S13: 0.0301
REMARK 3 S21: -0.0009 S22: -0.0258 S23: 0.0548
REMARK 3 S31: -0.0387 S32: -0.0535 S33: 0.0182
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 115.3190 61.2420 -6.8670
REMARK 3 T TENSOR
REMARK 3 T11: -0.1365 T22: -0.1732
REMARK 3 T33: -0.0123 T12: -0.0060
REMARK 3 T13: 0.0538 T23: 0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 0.5464 L22: 0.5657
REMARK 3 L33: 0.3551 L12: -0.0071
REMARK 3 L13: 0.0109 L23: -0.0352
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: 0.0128 S13: 0.3813
REMARK 3 S21: 0.1146 S22: -0.0720 S23: -0.0587
REMARK 3 S31: -0.0532 S32: 0.0025 S33: 0.0375
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 81.9822 50.1708 7.6759
REMARK 3 T TENSOR
REMARK 3 T11: -0.1329 T22: -0.1569
REMARK 3 T33: 0.0042 T12: 0.0041
REMARK 3 T13: 0.1520 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.5567 L22: 0.8015
REMARK 3 L33: 0.4852 L12: -0.1333
REMARK 3 L13: 0.1699 L23: -0.2362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0514 S12: -0.1329 S13: 0.1722
REMARK 3 S21: 0.2437 S22: 0.1046 S23: 0.4086
REMARK 3 S31: -0.0659 S32: -0.2148 S33: -0.0533
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 110.6350 16.3183 36.4169
REMARK 3 T TENSOR
REMARK 3 T11: 0.3040 T22: 0.0330
REMARK 3 T33: -0.3040 T12: -0.0056
REMARK 3 T13: 0.0886 T23: 0.0659
REMARK 3 L TENSOR
REMARK 3 L11: 0.3752 L22: 0.7965
REMARK 3 L33: 0.3773 L12: 0.0284
REMARK 3 L13: -0.0149 L23: 0.0528
REMARK 3 S TENSOR
REMARK 3 S11: -0.0275 S12: -0.2886 S13: -0.1131
REMARK 3 S21: 0.4832 S22: 0.0069 S23: 0.0965
REMARK 3 S31: 0.1224 S32: 0.0156 S33: 0.0206
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 136.6690 29.8429 -65.1683
REMARK 3 T TENSOR
REMARK 3 T11: -0.1341 T22: 0.1278
REMARK 3 T33: -0.2591 T12: 0.1228
REMARK 3 T13: 0.0403 T23: -0.0783
REMARK 3 L TENSOR
REMARK 3 L11: 1.2805 L22: 1.7116
REMARK 3 L33: 3.3123 L12: 0.3634
REMARK 3 L13: 0.4897 L23: -0.6031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0446 S12: 0.0276 S13: -0.1465
REMARK 3 S21: 0.1359 S22: 0.0624 S23: -0.0267
REMARK 3 S31: 0.1204 S32: 0.4599 S33: -0.0178
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN E
REMARK 3 ORIGIN FOR THE GROUP (A): 127.0960 92.8455 -25.4396
REMARK 3 T TENSOR
REMARK 3 T11: -0.1625 T22: -0.3040
REMARK 3 T33: 0.2784 T12: -0.0399
REMARK 3 T13: -0.0389 T23: 0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 0.9995 L22: 5.2745
REMARK 3 L33: 0.7262 L12: -0.5059
REMARK 3 L13: -0.1273 L23: -1.1320
REMARK 3 S TENSOR
REMARK 3 S11: -0.0514 S12: 0.1485 S13: 0.5216
REMARK 3 S21: -0.4065 S22: -0.0114 S23: 0.0229
REMARK 3 S31: -0.3304 S32: 0.0573 S33: 0.0629
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN F
REMARK 3 ORIGIN FOR THE GROUP (A): 140.2330 38.8051 -19.5436
REMARK 3 T TENSOR
REMARK 3 T11: -0.1323 T22: 0.0953
REMARK 3 T33: -0.1372 T12: 0.0179
REMARK 3 T13: 0.0104 T23: 0.0813
REMARK 3 L TENSOR
REMARK 3 L11: 1.1744 L22: 7.3681
REMARK 3 L33: 2.9431 L12: -0.3231
REMARK 3 L13: 0.2245 L23: -0.9637
REMARK 3 S TENSOR
REMARK 3 S11: 0.0350 S12: -0.0829 S13: 0.1926
REMARK 3 S21: 0.0856 S22: -0.0203 S23: -0.0458
REMARK 3 S31: 0.2224 S32: 0.2140 S33: -0.0147
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN T
REMARK 3 ORIGIN FOR THE GROUP (A): 96.3665 60.7449 -13.4929
REMARK 3 T TENSOR
REMARK 3 T11: -0.0467 T22: -0.1091
REMARK 3 T33: 0.1222 T12: -0.0573
REMARK 3 T13: 0.0228 T23: -0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 1.5301 L22: 1.1522
REMARK 3 L33: 0.0000 L12: -2.0458
REMARK 3 L13: 1.5302 L23: 1.4343
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: -0.0892 S13: 0.1401
REMARK 3 S21: -0.0226 S22: -0.0870 S23: 0.1952
REMARK 3 S31: -0.1114 S32: -0.1908 S33: 0.0922
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN G
REMARK 3 ORIGIN FOR THE GROUP (A): 127.2590 23.2723 -59.5979
REMARK 3 T TENSOR
REMARK 3 T11: 0.0045 T22: 0.0959
REMARK 3 T33: -0.1236 T12: 0.1367
REMARK 3 T13: 0.0723 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.2952 L22: 0.5499
REMARK 3 L33: 3.8798 L12: 0.0864
REMARK 3 L13: 0.9408 L23: 1.4069
REMARK 3 S TENSOR
REMARK 3 S11: -0.0582 S12: 0.0443 S13: -0.2305
REMARK 3 S21: 0.0387 S22: 0.0864 S23: 0.0872
REMARK 3 S31: 0.3479 S32: 0.2706 S33: -0.0282
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN H
REMARK 3 ORIGIN FOR THE GROUP (A): 152.5130 52.3321 36.8011
REMARK 3 T TENSOR
REMARK 3 T11: 0.0550 T22: -0.0501
REMARK 3 T33: -0.2123 T12: -0.1520
REMARK 3 T13: -0.1520 T23: -0.0580
REMARK 3 L TENSOR
REMARK 3 L11: 6.0553 L22: 2.0359
REMARK 3 L33: 0.5523 L12: 1.4114
REMARK 3 L13: 2.5412 L23: 0.1788
REMARK 3 S TENSOR
REMARK 3 S11: -0.0482 S12: -0.3861 S13: 0.1796
REMARK 3 S21: 0.2395 S22: 0.0787 S23: -0.3383
REMARK 3 S31: -0.1983 S32: 0.4138 S33: -0.0305
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN I
REMARK 3 ORIGIN FOR THE GROUP (A): 76.3623 99.1953 13.7002
REMARK 3 T TENSOR
REMARK 3 T11: 0.0125 T22: -0.2981
REMARK 3 T33: 0.2884 T12: 0.1520
REMARK 3 T13: 0.1520 T23: -0.1450
REMARK 3 L TENSOR
REMARK 3 L11: 0.8725 L22: 1.7641
REMARK 3 L33: 1.0327 L12: -1.0093
REMARK 3 L13: 0.5178 L23: -0.4277
REMARK 3 S TENSOR
REMARK 3 S11: -0.0613 S12: 0.1442 S13: 0.5002
REMARK 3 S21: 0.5207 S22: -0.0606 S23: 0.2693
REMARK 3 S31: 0.1839 S32: 0.0387 S33: 0.1219
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN J
REMARK 3 ORIGIN FOR THE GROUP (A): 91.2071 25.7492 37.4636
REMARK 3 T TENSOR
REMARK 3 T11: 0.3034 T22: -0.1004
REMARK 3 T33: -0.2551 T12: 0.0040
REMARK 3 T13: 0.1520 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 1.3863 L22: 0.0000
REMARK 3 L33: 3.6181 L12: -0.9971
REMARK 3 L13: -1.5579 L23: -1.1008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: -0.1520 S13: 0.0474
REMARK 3 S21: 0.1964 S22: 0.0121 S23: 0.1239
REMARK 3 S31: 0.0592 S32: 0.0041 S33: -0.0276
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN K
REMARK 3 ORIGIN FOR THE GROUP (A): 132.0120 17.3456 28.2830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1483 T22: 0.0227
REMARK 3 T33: -0.2692 T12: 0.1087
REMARK 3 T13: -0.0876 T23: 0.0712
REMARK 3 L TENSOR
REMARK 3 L11: 1.3663 L22: 2.1640
REMARK 3 L33: 0.4582 L12: -0.2436
REMARK 3 L13: 0.6153 L23: -0.6895
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: -0.0760 S13: -0.2079
REMARK 3 S21: 0.5097 S22: -0.1287 S23: -0.3457
REMARK 3 S31: 0.3850 S32: 0.2311 S33: 0.1223
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN L
REMARK 3 ORIGIN FOR THE GROUP (A): 76.5708 9.4737 9.1495
REMARK 3 T TENSOR
REMARK 3 T11: 0.1254 T22: -0.1772
REMARK 3 T33: 0.1365 T12: -0.1520
REMARK 3 T13: 0.0870 T23: 0.1518
REMARK 3 L TENSOR
REMARK 3 L11: 0.8310 L22: 0.0000
REMARK 3 L33: 1.1918 L12: 2.9104
REMARK 3 L13: 0.8030 L23: 0.8729
REMARK 3 S TENSOR
REMARK 3 S11: 0.0129 S12: -0.0595 S13: -0.0498
REMARK 3 S21: 0.1047 S22: 0.0017 S23: 0.3324
REMARK 3 S31: 0.1359 S32: -0.1484 S33: -0.0145
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=ZN MG BRU.
REMARK 3 NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=31773. NUMBER WITH
REMARK 3 APPROX DEFAULT CCP4 ATOM TYPE=20. NUMBER TREATED BY BAD NON-
REMARK 3 BONDED CONTACTS=9.
REMARK 4
REMARK 4 4A3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-NOV-11.
REMARK 100 THE PDBE ID CODE IS EBI-49863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9188
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PSI PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128404
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.70
REMARK 200 RESOLUTION RANGE LOW (A) : 80.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.8
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.2
REMARK 200 R MERGE (I) : 0.65
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 82.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 141.33000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 141.33000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 111.64500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 196.39500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 111.64500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 196.39500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 141.33000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 111.64500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 196.39500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 141.33000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 111.64500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 196.39500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: PENTADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 88070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 189240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -392.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, N, P, 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 VAL A 2
REMARK 465 PHE A 1084
REMARK 465 HIS A 1085
REMARK 465 PHE A 1086
REMARK 465 ALA A 1087
REMARK 465 GLY A 1088
REMARK 465 VAL A 1089
REMARK 465 ALA A 1090
REMARK 465 SER A 1091
REMARK 465 LEU A 1177
REMARK 465 ASP A 1178
REMARK 465 GLU A 1179
REMARK 465 GLU A 1180
REMARK 465 ALA A 1181
REMARK 465 GLU A 1182
REMARK 465 GLN A 1183
REMARK 465 SER A 1184
REMARK 465 PHE A 1185
REMARK 465 ASP A 1186
REMARK 465 ARG A 1244
REMARK 465 PRO A 1245
REMARK 465 LYS A 1246
REMARK 465 SER A 1247
REMARK 465 LEU A 1248
REMARK 465 ASP A 1249
REMARK 465 ALA A 1250
REMARK 465 GLU A 1251
REMARK 465 THR A 1252
REMARK 465 GLU A 1253
REMARK 465 GLU A 1456
REMARK 465 GLN A 1457
REMARK 465 LYS A 1458
REMARK 465 ILE A 1459
REMARK 465 THR A 1460
REMARK 465 GLU A 1461
REMARK 465 ILE A 1462
REMARK 465 GLU A 1463
REMARK 465 ASP A 1464
REMARK 465 GLY A 1465
REMARK 465 GLN A 1466
REMARK 465 ASP A 1467
REMARK 465 GLY A 1468
REMARK 465 GLY A 1469
REMARK 465 VAL A 1470
REMARK 465 THR A 1471
REMARK 465 PRO A 1472
REMARK 465 TYR A 1473
REMARK 465 SER A 1474
REMARK 465 ASN A 1475
REMARK 465 GLU A 1476
REMARK 465 SER A 1477
REMARK 465 GLY A 1478
REMARK 465 LEU A 1479
REMARK 465 VAL A 1480
REMARK 465 ASN A 1481
REMARK 465 ALA A 1482
REMARK 465 ASP A 1483
REMARK 465 LEU A 1484
REMARK 465 ASP A 1485
REMARK 465 VAL A 1486
REMARK 465 LYS A 1487
REMARK 465 ASP A 1488
REMARK 465 GLU A 1489
REMARK 465 LEU A 1490
REMARK 465 MET A 1491
REMARK 465 PHE A 1492
REMARK 465 SER A 1493
REMARK 465 PRO A 1494
REMARK 465 LEU A 1495
REMARK 465 VAL A 1496
REMARK 465 ASP A 1497
REMARK 465 SER A 1498
REMARK 465 GLY A 1499
REMARK 465 SER A 1500
REMARK 465 ASN A 1501
REMARK 465 ASP A 1502
REMARK 465 ALA A 1503
REMARK 465 MET A 1504
REMARK 465 ALA A 1505
REMARK 465 GLY A 1506
REMARK 465 GLY A 1507
REMARK 465 PHE A 1508
REMARK 465 THR A 1509
REMARK 465 ALA A 1510
REMARK 465 TYR A 1511
REMARK 465 GLY A 1512
REMARK 465 GLY A 1513
REMARK 465 ALA A 1514
REMARK 465 ASP A 1515
REMARK 465 TYR A 1516
REMARK 465 GLY A 1517
REMARK 465 GLU A 1518
REMARK 465 ALA A 1519
REMARK 465 THR A 1520
REMARK 465 SER A 1521
REMARK 465 PRO A 1522
REMARK 465 PHE A 1523
REMARK 465 GLY A 1524
REMARK 465 ALA A 1525
REMARK 465 TYR A 1526
REMARK 465 GLY A 1527
REMARK 465 GLU A 1528
REMARK 465 ALA A 1529
REMARK 465 PRO A 1530
REMARK 465 THR A 1531
REMARK 465 SER A 1532
REMARK 465 PRO A 1533
REMARK 465 GLY A 1534
REMARK 465 PHE A 1535
REMARK 465 GLY A 1536
REMARK 465 VAL A 1537
REMARK 465 SER A 1538
REMARK 465 SER A 1539
REMARK 465 PRO A 1540
REMARK 465 GLY A 1541
REMARK 465 PHE A 1542
REMARK 465 SER A 1543
REMARK 465 PRO A 1544
REMARK 465 THR A 1545
REMARK 465 SER A 1546
REMARK 465 PRO A 1547
REMARK 465 THR A 1548
REMARK 465 TYR A 1549
REMARK 465 SER A 1550
REMARK 465 PRO A 1551
REMARK 465 THR A 1552
REMARK 465 SER A 1553
REMARK 465 PRO A 1554
REMARK 465 ALA A 1555
REMARK 465 TYR A 1556
REMARK 465 SER A 1557
REMARK 465 PRO A 1558
REMARK 465 THR A 1559
REMARK 465 SER A 1560
REMARK 465 PRO A 1561
REMARK 465 SER A 1562
REMARK 465 TYR A 1563
REMARK 465 SER A 1564
REMARK 465 PRO A 1565
REMARK 465 THR A 1566
REMARK 465 SER A 1567
REMARK 465 PRO A 1568
REMARK 465 SER A 1569
REMARK 465 TYR A 1570
REMARK 465 SER A 1571
REMARK 465 PRO A 1572
REMARK 465 THR A 1573
REMARK 465 SER A 1574
REMARK 465 PRO A 1575
REMARK 465 SER A 1576
REMARK 465 TYR A 1577
REMARK 465 SER A 1578
REMARK 465 PRO A 1579
REMARK 465 THR A 1580
REMARK 465 SER A 1581
REMARK 465 PRO A 1582
REMARK 465 SER A 1583
REMARK 465 TYR A 1584
REMARK 465 SER A 1585
REMARK 465 PRO A 1586
REMARK 465 THR A 1587
REMARK 465 SER A 1588
REMARK 465 PRO A 1589
REMARK 465 SER A 1590
REMARK 465 TYR A 1591
REMARK 465 SER A 1592
REMARK 465 PRO A 1593
REMARK 465 THR A 1594
REMARK 465 SER A 1595
REMARK 465 PRO A 1596
REMARK 465 SER A 1597
REMARK 465 TYR A 1598
REMARK 465 SER A 1599
REMARK 465 PRO A 1600
REMARK 465 THR A 1601
REMARK 465 SER A 1602
REMARK 465 PRO A 1603
REMARK 465 SER A 1604
REMARK 465 TYR A 1605
REMARK 465 SER A 1606
REMARK 465 PRO A 1607
REMARK 465 THR A 1608
REMARK 465 SER A 1609
REMARK 465 PRO A 1610
REMARK 465 SER A 1611
REMARK 465 TYR A 1612
REMARK 465 SER A 1613
REMARK 465 PRO A 1614
REMARK 465 THR A 1615
REMARK 465 SER A 1616
REMARK 465 PRO A 1617
REMARK 465 SER A 1618
REMARK 465 TYR A 1619
REMARK 465 SER A 1620
REMARK 465 PRO A 1621
REMARK 465 THR A 1622
REMARK 465 SER A 1623
REMARK 465 PRO A 1624
REMARK 465 SER A 1625
REMARK 465 TYR A 1626
REMARK 465 SER A 1627
REMARK 465 PRO A 1628
REMARK 465 THR A 1629
REMARK 465 SER A 1630
REMARK 465 PRO A 1631
REMARK 465 SER A 1632
REMARK 465 TYR A 1633
REMARK 465 SER A 1634
REMARK 465 PRO A 1635
REMARK 465 THR A 1636
REMARK 465 SER A 1637
REMARK 465 PRO A 1638
REMARK 465 SER A 1639
REMARK 465 TYR A 1640
REMARK 465 SER A 1641
REMARK 465 PRO A 1642
REMARK 465 THR A 1643
REMARK 465 SER A 1644
REMARK 465 PRO A 1645
REMARK 465 SER A 1646
REMARK 465 TYR A 1647
REMARK 465 SER A 1648
REMARK 465 PRO A 1649
REMARK 465 THR A 1650
REMARK 465 SER A 1651
REMARK 465 PRO A 1652
REMARK 465 SER A 1653
REMARK 465 TYR A 1654
REMARK 465 SER A 1655
REMARK 465 PRO A 1656
REMARK 465 THR A 1657
REMARK 465 SER A 1658
REMARK 465 PRO A 1659
REMARK 465 ALA A 1660
REMARK 465 TYR A 1661
REMARK 465 SER A 1662
REMARK 465 PRO A 1663
REMARK 465 THR A 1664
REMARK 465 SER A 1665
REMARK 465 PRO A 1666
REMARK 465 SER A 1667
REMARK 465 TYR A 1668
REMARK 465 SER A 1669
REMARK 465 PRO A 1670
REMARK 465 THR A 1671
REMARK 465 SER A 1672
REMARK 465 PRO A 1673
REMARK 465 SER A 1674
REMARK 465 TYR A 1675
REMARK 465 SER A 1676
REMARK 465 PRO A 1677
REMARK 465 THR A 1678
REMARK 465 SER A 1679
REMARK 465 PRO A 1680
REMARK 465 SER A 1681
REMARK 465 TYR A 1682
REMARK 465 SER A 1683
REMARK 465 PRO A 1684
REMARK 465 THR A 1685
REMARK 465 SER A 1686
REMARK 465 PRO A 1687
REMARK 465 SER A 1688
REMARK 465 TYR A 1689
REMARK 465 SER A 1690
REMARK 465 PRO A 1691
REMARK 465 THR A 1692
REMARK 465 SER A 1693
REMARK 465 PRO A 1694
REMARK 465 ASN A 1695
REMARK 465 TYR A 1696
REMARK 465 SER A 1697
REMARK 465 PRO A 1698
REMARK 465 THR A 1699
REMARK 465 SER A 1700
REMARK 465 PRO A 1701
REMARK 465 SER A 1702
REMARK 465 TYR A 1703
REMARK 465 SER A 1704
REMARK 465 PRO A 1705
REMARK 465 THR A 1706
REMARK 465 SER A 1707
REMARK 465 PRO A 1708
REMARK 465 GLY A 1709
REMARK 465 TYR A 1710
REMARK 465 SER A 1711
REMARK 465 PRO A 1712
REMARK 465 GLY A 1713
REMARK 465 SER A 1714
REMARK 465 PRO A 1715
REMARK 465 ALA A 1716
REMARK 465 TYR A 1717
REMARK 465 SER A 1718
REMARK 465 PRO A 1719
REMARK 465 LYS A 1720
REMARK 465 GLN A 1721
REMARK 465 ASP A 1722
REMARK 465 GLU A 1723
REMARK 465 GLN A 1724
REMARK 465 LYS A 1725
REMARK 465 HIS A 1726
REMARK 465 ASN A 1727
REMARK 465 GLU A 1728
REMARK 465 ASN A 1729
REMARK 465 GLU A 1730
REMARK 465 ASN A 1731
REMARK 465 SER A 1732
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
REMARK 465 ASN B 6
REMARK 465 SER B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 9
REMARK 465 TYR B 10
REMARK 465 TYR B 11
REMARK 465 ASP B 12
REMARK 465 GLU B 13
REMARK 465 ASP B 14
REMARK 465 PRO B 15
REMARK 465 TYR B 16
REMARK 465 GLY B 17
REMARK 465 PHE B 18
REMARK 465 GLU B 19
REMARK 465 LEU B 71
REMARK 465 GLU B 72
REMARK 465 GLN B 73
REMARK 465 LEU B 74
REMARK 465 ALA B 75
REMARK 465 GLN B 76
REMARK 465 HIS B 77
REMARK 465 THR B 78
REMARK 465 THR B 79
REMARK 465 GLU B 80
REMARK 465 SER B 81
REMARK 465 ASP B 82
REMARK 465 ASN B 83
REMARK 465 ILE B 84
REMARK 465 SER B 85
REMARK 465 ARG B 86
REMARK 465 LYS B 87
REMARK 465 TYR B 88
REMARK 465 GLU B 89
REMARK 465 ARG B 135
REMARK 465 THR B 136
REMARK 465 TYR B 137
REMARK 465 GLU B 138
REMARK 465 ALA B 139
REMARK 465 ILE B 140
REMARK 465 ASP B 141
REMARK 465 VAL B 142
REMARK 465 PRO B 143
REMARK 465 GLY B 144
REMARK 465 ARG B 145
REMARK 465 GLU B 146
REMARK 465 LEU B 147
REMARK 465 LYS B 148
REMARK 465 TYR B 149
REMARK 465 GLU B 150
REMARK 465 LEU B 151
REMARK 465 ILE B 152
REMARK 465 ALA B 153
REMARK 465 GLU B 154
REMARK 465 GLU B 155
REMARK 465 SER B 156
REMARK 465 GLU B 157
REMARK 465 ASP B 158
REMARK 465 ASP B 159
REMARK 465 SER B 160
REMARK 465 GLU B 161
REMARK 465 SER B 162
REMARK 465 GLY B 163
REMARK 465 GLU B 438
REMARK 465 ALA B 439
REMARK 465 HIS B 440
REMARK 465 ASP B 441
REMARK 465 PHE B 442
REMARK 465 ASN B 443
REMARK 465 MET B 444
REMARK 465 LYS B 445
REMARK 465 GLY B 503
REMARK 465 ARG B 504
REMARK 465 ASP B 505
REMARK 465 GLY B 506
REMARK 465 LYS B 507
REMARK 465 LEU B 508
REMARK 465 ILE B 669
REMARK 465 GLU B 670
REMARK 465 GLY B 671
REMARK 465 GLY B 672
REMARK 465 PHE B 673
REMARK 465 GLU B 674
REMARK 465 ASP B 675
REMARK 465 VAL B 676
REMARK 465 GLU B 677
REMARK 465 ASN B 716
REMARK 465 GLU B 717
REMARK 465 GLU B 718
REMARK 465 ASN B 719
REMARK 465 ASP B 720
REMARK 465 LEU B 721
REMARK 465 PRO B 920
REMARK 465 ASP B 921
REMARK 465 GLU B 922
REMARK 465 GLU B 923
REMARK 465 GLU B 924
REMARK 465 LEU B 925
REMARK 465 GLY B 926
REMARK 465 GLN B 927
REMARK 465 ARG B 928
REMARK 465 THR B 929
REMARK 465 ALA B 930
REMARK 465 TYR B 931
REMARK 465 HIS B 932
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 269
REMARK 465 VAL C 270
REMARK 465 ASN C 271
REMARK 465 PHE C 272
REMARK 465 ALA C 273
REMARK 465 SER C 274
REMARK 465 GLY C 275
REMARK 465 ASP C 276
REMARK 465 ASN C 277
REMARK 465 ASN C 278
REMARK 465 THR C 279
REMARK 465 ALA C 280
REMARK 465 SER C 281
REMARK 465 ASN C 282
REMARK 465 MET C 283
REMARK 465 LEU C 284
REMARK 465 GLY C 285
REMARK 465 SER C 286
REMARK 465 ASN C 287
REMARK 465 GLU C 288
REMARK 465 ASP C 289
REMARK 465 VAL C 290
REMARK 465 MET C 291
REMARK 465 MET C 292
REMARK 465 THR C 293
REMARK 465 GLY C 294
REMARK 465 ALA C 295
REMARK 465 GLU C 296
REMARK 465 GLN C 297
REMARK 465 ASP C 298
REMARK 465 PRO C 299
REMARK 465 TYR C 300
REMARK 465 SER C 301
REMARK 465 ASN C 302
REMARK 465 ALA C 303
REMARK 465 SER C 304
REMARK 465 GLN C 305
REMARK 465 MET C 306
REMARK 465 GLY C 307
REMARK 465 ASN C 308
REMARK 465 THR C 309
REMARK 465 GLY C 310
REMARK 465 SER C 311
REMARK 465 GLY C 312
REMARK 465 GLY C 313
REMARK 465 TYR C 314
REMARK 465 ASP C 315
REMARK 465 ASN C 316
REMARK 465 ALA C 317
REMARK 465 TRP C 318
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 HIS D 77
REMARK 465 LYS D 78
REMARK 465 LYS D 79
REMARK 465 LYS D 80
REMARK 465 HIS D 81
REMARK 465 LEU D 82
REMARK 465 LYS D 83
REMARK 465 HIS D 84
REMARK 465 GLU D 85
REMARK 465 ASN D 86
REMARK 465 ALA D 87
REMARK 465 ASN D 88
REMARK 465 ASP D 89
REMARK 465 GLU D 90
REMARK 465 THR D 91
REMARK 465 THR D 92
REMARK 465 ALA D 93
REMARK 465 VAL D 94
REMARK 465 GLU D 95
REMARK 465 ASP D 96
REMARK 465 GLU D 97
REMARK 465 ASP D 98
REMARK 465 ASP D 99
REMARK 465 ASP D 100
REMARK 465 LEU D 101
REMARK 465 ASP D 102
REMARK 465 GLU D 103
REMARK 465 ASP D 104
REMARK 465 ASP D 105
REMARK 465 VAL D 106
REMARK 465 ASN D 107
REMARK 465 ALA D 108
REMARK 465 ASP D 109
REMARK 465 ASP D 110
REMARK 465 ASP D 111
REMARK 465 ASP D 112
REMARK 465 PHE D 113
REMARK 465 MET D 114
REMARK 465 HIS D 115
REMARK 465 SER D 116
REMARK 465 GLU D 117
REMARK 465 MET E 1
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 ASP F 3
REMARK 465 TYR F 4
REMARK 465 GLU F 5
REMARK 465 GLU F 6
REMARK 465 ALA F 7
REMARK 465 PHE F 8
REMARK 465 ASN F 9
REMARK 465 ASP F 10
REMARK 465 GLY F 11
REMARK 465 ASN F 12
REMARK 465 GLU F 13
REMARK 465 ASN F 14
REMARK 465 PHE F 15
REMARK 465 GLU F 16
REMARK 465 ASP F 17
REMARK 465 PHE F 18
REMARK 465 ASP F 19
REMARK 465 VAL F 20
REMARK 465 GLU F 21
REMARK 465 HIS F 22
REMARK 465 PHE F 23
REMARK 465 SER F 24
REMARK 465 ASP F 25
REMARK 465 GLU F 26
REMARK 465 GLU F 27
REMARK 465 THR F 28
REMARK 465 TYR F 29
REMARK 465 GLU F 30
REMARK 465 GLU F 31
REMARK 465 LYS F 32
REMARK 465 PRO F 33
REMARK 465 GLN F 34
REMARK 465 PHE F 35
REMARK 465 LYS F 36
REMARK 465 ASP F 37
REMARK 465 GLY F 38
REMARK 465 GLU F 39
REMARK 465 THR F 40
REMARK 465 THR F 41
REMARK 465 ASP F 42
REMARK 465 ALA F 43
REMARK 465 ASN F 44
REMARK 465 GLY F 45
REMARK 465 LYS F 46
REMARK 465 THR F 47
REMARK 465 ILE F 48
REMARK 465 VAL F 49
REMARK 465 THR F 50
REMARK 465 GLY F 51
REMARK 465 GLY F 52
REMARK 465 ASN F 53
REMARK 465 GLY F 54
REMARK 465 PRO F 55
REMARK 465 GLU F 56
REMARK 465 ASP F 57
REMARK 465 PHE F 58
REMARK 465 GLN F 59
REMARK 465 GLN F 60
REMARK 465 HIS F 61
REMARK 465 GLU F 62
REMARK 465 GLN F 63
REMARK 465 ILE F 64
REMARK 465 ARG F 65
REMARK 465 ARG F 66
REMARK 465 LYS F 67
REMARK 465 THR F 68
REMARK 465 LEU F 69
REMARK 465 LYS F 70
REMARK 465 GLU F 71
REMARK 465 MET H 1
REMARK 465 ASN H 64
REMARK 465 LEU H 65
REMARK 465 GLU H 66
REMARK 465 ASP H 67
REMARK 465 THR H 68
REMARK 465 PRO H 69
REMARK 465 ALA H 70
REMARK 465 ASN H 71
REMARK 465 ASP H 72
REMARK 465 SER H 73
REMARK 465 SER H 74
REMARK 465 ALA H 75
REMARK 465 MET I 1
REMARK 465 PHE I 121
REMARK 465 SER I 122
REMARK 465 LEU J 66
REMARK 465 GLU J 67
REMARK 465 LYS J 68
REMARK 465 ARG J 69
REMARK 465 ASP J 70
REMARK 465 ALA K 116
REMARK 465 ASP K 117
REMARK 465 ASP K 118
REMARK 465 ALA K 119
REMARK 465 PHE K 120
REMARK 465 MET L 1
REMARK 465 SER L 2
REMARK 465 ARG L 3
REMARK 465 GLU L 4
REMARK 465 GLY L 5
REMARK 465 PHE L 6
REMARK 465 GLN L 7
REMARK 465 ILE L 8
REMARK 465 PRO L 9
REMARK 465 THR L 10
REMARK 465 ASN L 11
REMARK 465 LEU L 12
REMARK 465 ASP L 13
REMARK 465 ALA L 14
REMARK 465 ALA L 15
REMARK 465 ALA L 16
REMARK 465 ALA L 17
REMARK 465 GLY L 18
REMARK 465 THR L 19
REMARK 465 SER L 20
REMARK 465 GLN L 21
REMARK 465 ALA L 22
REMARK 465 ARG L 23
REMARK 465 THR L 24
REMARK 465 DG N 0
REMARK 465 DA N 10
REMARK 465 DG N 11
REMARK 465 DC N 12
REMARK 465 DT N 13
REMARK 465 DA T 4
REMARK 465 DG T 5
REMARK 465 DC T 6
REMARK 465 DT T 7
REMARK 465 DA T 24
REMARK 465 DA T 25
REMARK 465 DC T 26
REMARK 465 DT T 27
REMARK 465 DA T 28
REMARK 465 DA T 29
REMARK 465 DC T 30
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 A 68 CG CD OE1 NE2
REMARK 470 LYS A 186 CG CD CE NZ
REMARK 470 ALA K 115 CA C O CB
REMARK 470 DT N 1 P OP1 OP2
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 NH2 ARG C 66 O VAL J 3 2.15
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 ILE A 35 C - N - CA ANGL. DEV. = 15.9 DEGREES
REMARK 500 ASP A 55 C - N - CA ANGL. DEV. = 15.7 DEGREES
REMARK 500 ARG A 57 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 HIS A 399 N - CA - CB ANGL. DEV. = 11.6 DEGREES
REMARK 500 LEU B 341 C - N - CA ANGL. DEV. = 16.1 DEGREES
REMARK 500 THR B 882 C - N - CA ANGL. DEV. = 16.0 DEGREES
REMARK 500 DT N 1 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG N 3 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DC T 14 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG T 20 O4' - C1' - N9 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 ALA A 9 126.55 -29.48
REMARK 500 ILE A 35 67.11 71.53
REMARK 500 THR A 40 -74.97 -57.60
REMARK 500 MET A 41 -142.31 -151.17
REMARK 500 ASP A 42 86.69 57.12
REMARK 500 GLU A 43 70.30 -57.72
REMARK 500 THR A 44 63.39 65.45
REMARK 500 GLN A 45 -10.60 72.18
REMARK 500 ARG A 47 106.78 -46.79
REMARK 500 ALA A 48 138.72 159.34
REMARK 500 ASN A 54 78.38 7.34
REMARK 500 ASP A 55 63.50 96.76
REMARK 500 ARG A 57 -24.55 141.90
REMARK 500 LEU A 58 -128.81 -19.78
REMARK 500 ILE A 61 -137.33 -85.22
REMARK 500 ASP A 62 -33.85 54.87
REMARK 500 ARG A 63 -49.75 68.97
REMARK 500 ASN A 64 44.29 -89.88
REMARK 500 THR A 69 -73.06 -92.91
REMARK 500 MET A 74 -105.99 61.48
REMARK 500 GLU A 76 -31.75 101.24
REMARK 500 MET A 108 13.58 -67.80
REMARK 500 HIS A 109 -44.98 -135.03
REMARK 500 ILE A 128 120.56 -36.25
REMARK 500 SER A 154 158.04 -49.17
REMARK 500 GLU A 155 41.71 -79.20
REMARK 500 ASP A 156 -52.43 -161.20
REMARK 500 ARG A 164 -135.83 -80.83
REMARK 500 CYS A 167 119.81 57.36
REMARK 500 ASN A 169 136.41 -26.70
REMARK 500 LEU A 179 -11.75 77.07
REMARK 500 LYS A 186 -39.96 -36.13
REMARK 500 LYS A 187 175.76 70.58
REMARK 500 ASP A 188 -58.49 -129.36
REMARK 500 ARG A 189 95.22 15.22
REMARK 500 THR A 191 -31.94 77.72
REMARK 500 ASP A 193 120.05 1.74
REMARK 500 ASP A 195 95.04 11.20
REMARK 500 GLU A 196 101.36 54.28
REMARK 500 LEU A 199 64.48 -110.10
REMARK 500 PHE A 224 171.55 -51.65
REMARK 500 PRO A 245 -34.17 -37.37
REMARK 500 ARG A 247 67.03 -119.50
REMARK 500 SER A 251 85.26 -60.26
REMARK 500 ASN A 253 -91.86 55.09
REMARK 500 GLU A 254 -87.78 -156.32
REMARK 500 ARG A 257 -132.20 -76.82
REMARK 500 ASN A 282 -161.82 -72.84
REMARK 500 ALA A 284 100.20 -54.68
REMARK 500 PRO A 285 39.58 -88.14
REMARK 500
REMARK 500 THIS ENTRY HAS 330 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 34 ILE A 35 32.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LYS A 34 10.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLN A 5 23.6 L L OUTSIDE RANGE
REMARK 500 ILE A 35 23.1 L L OUTSIDE RANGE
REMARK 500 ASN A 54 20.7 L L OUTSIDE RANGE
REMARK 500 ASP A 55 17.3 L L OUTSIDE RANGE
REMARK 500 ASP A 62 24.3 L L OUTSIDE RANGE
REMARK 500 GLU A 72 23.7 L L OUTSIDE RANGE
REMARK 500 VAL A 93 23.0 L L OUTSIDE RANGE
REMARK 500 THR A 191 23.0 L L OUTSIDE RANGE
REMARK 500 GLU A 196 22.5 L L OUTSIDE RANGE
REMARK 500 PHE A 219 23.8 L L OUTSIDE RANGE
REMARK 500 PHE A 224 23.6 L L OUTSIDE RANGE
REMARK 500 SER A 251 24.1 L L OUTSIDE RANGE
REMARK 500 HIS A 286 23.1 L L OUTSIDE RANGE
REMARK 500 GLN A 311 21.2 L L OUTSIDE RANGE
REMARK 500 ARG A 335 23.8 L L OUTSIDE RANGE
REMARK 500 GLN A 363 24.0 L L OUTSIDE RANGE
REMARK 500 HIS A 399 14.7 L L OUTSIDE RANGE
REMARK 500 ASN A 439 24.1 L L OUTSIDE RANGE
REMARK 500 SER A 466 24.9 L L OUTSIDE RANGE
REMARK 500 LEU A 472 24.7 L L OUTSIDE RANGE
REMARK 500 ASP A 483 24.9 L L OUTSIDE RANGE
REMARK 500 ILE A 511 24.5 L L OUTSIDE RANGE
REMARK 500 LYS A 567 24.1 L L OUTSIDE RANGE
REMARK 500 ILE A 577 22.6 L L OUTSIDE RANGE
REMARK 500 ASN A 626 24.5 L L OUTSIDE RANGE
REMARK 500 GLN A 650 23.8 L L OUTSIDE RANGE
REMARK 500 LYS A 797 24.4 L L OUTSIDE RANGE
REMARK 500 GLU A 846 24.1 L L OUTSIDE RANGE
REMARK 500 ASP A 847 24.7 L L OUTSIDE RANGE
REMARK 500 TYR A 852 24.4 L L OUTSIDE RANGE
REMARK 500 TYR A 868 24.1 L L OUTSIDE RANGE
REMARK 500 ILE A 886 24.3 L L OUTSIDE RANGE
REMARK 500 LEU A 998 24.3 L L OUTSIDE RANGE
REMARK 500 ARG A1001 24.4 L L OUTSIDE RANGE
REMARK 500 VAL A1064 20.9 L L OUTSIDE RANGE
REMARK 500 GLU A1168 24.5 L L OUTSIDE RANGE
REMARK 500 GLN A1211 24.8 L L OUTSIDE RANGE
REMARK 500 GLU A1234 24.2 L L OUTSIDE RANGE
REMARK 500 VAL A1242 22.3 L L OUTSIDE RANGE
REMARK 500 ILE A1341 23.8 L L OUTSIDE RANGE
REMARK 500 THR A1377 23.3 L L OUTSIDE RANGE
REMARK 500 GLU A1403 21.5 L L OUTSIDE RANGE
REMARK 500 MET A1454 24.5 L L OUTSIDE RANGE
REMARK 500 ILE B 292 24.6 L L OUTSIDE RANGE
REMARK 500 ILE B 343 23.5 L L OUTSIDE RANGE
REMARK 500 ILE B 502 24.5 L L OUTSIDE RANGE
REMARK 500 ARG B 579 24.7 L L OUTSIDE RANGE
REMARK 500 GLU B 711 24.3 L L OUTSIDE RANGE
REMARK 500 VAL B 751 24.8 L L OUTSIDE RANGE
REMARK 500 ASP B 837 24.4 L L OUTSIDE RANGE
REMARK 500
REMARK 500 THIS ENTRY HAS 82 CHIRALITY DEVIATIONS.
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 ZN A2456 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 167 SG
REMARK 620 2 CYS A 110 SG 122.0
REMARK 620 3 CYS A 107 SG 101.6 106.2
REMARK 620 4 CYS A 148 SG 119.8 104.1 100.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2457 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 67 SG
REMARK 620 2 CYS A 70 SG 110.6
REMARK 620 3 CYS A 77 SG 107.2 92.9
REMARK 620 4 HIS A 80 NE2 124.7 101.8 114.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2225 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1182 SG
REMARK 620 2 CYS B1166 SG 125.7
REMARK 620 3 CYS B1185 SG 105.6 90.0
REMARK 620 4 CYS B1163 SG 106.4 120.5 102.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1269 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 88 SG
REMARK 620 2 CYS C 92 SG 108.4
REMARK 620 3 CYS C 95 SG 115.3 111.3
REMARK 620 4 CYS C 86 SG 98.0 107.7 115.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I1121 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 10 SG
REMARK 620 2 CYS I 32 SG 96.9
REMARK 620 3 CYS I 29 SG 107.8 111.8
REMARK 620 4 CYS I 7 SG 120.8 101.8 115.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I1122 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 106 SG
REMARK 620 2 CYS I 103 SG 109.4
REMARK 620 3 CYS I 75 SG 103.3 117.1
REMARK 620 4 CYS I 78 SG 108.6 100.0 118.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J1066 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 7 SG
REMARK 620 2 CYS J 46 SG 132.5
REMARK 620 3 CYS J 45 SG 99.5 93.7
REMARK 620 4 CYS J 10 SG 128.9 92.2 100.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L1071 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 31 SG
REMARK 620 2 CYS L 48 SG 99.4
REMARK 620 3 CYS L 51 SG 107.9 110.6
REMARK 620 4 CYS L 34 SG 86.7 105.6 137.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A2458 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 481 OD1
REMARK 620 2 ASP A 481 OD2 59.9
REMARK 620 3 ASP A 483 OD1 69.3 88.2
REMARK 620 4 ASP A 485 OD1 79.8 107.1 132.3
REMARK 620 5 A P 10 O3' 147.8 133.9 81.2 113.2
REMARK 620 6 A P 10 O2' 136.2 104.7 154.4 65.5 73.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A2456
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A2457
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A2458
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B2225
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C1269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I1121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I1122
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J1066
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L1071
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G2P T1024
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TWC RELATED DB: PDB
REMARK 900 RNA POLYMERASE II COMPLEXED WITH GTP
REMARK 900 RELATED ID: 4A93 RELATED DB: PDB
REMARK 900 RNA POLYMERASE II ELONGATION COMPLEX CONTAINING A CPD
REMARK 900 LESION
REMARK 900 RELATED ID: 4A3K RELATED DB: PDB
REMARK 900 RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A
REMARK 900 7NT DNA-RNA HYBRID
REMARK 900 RELATED ID: 1Y77 RELATED DB: PDB
REMARK 900 COMPLETE RNA POLYMERASE II ELONGATION COMPLEX
REMARK 900 WITHSUBSTRATE ANALOGUE GMPCPP
REMARK 900 RELATED ID: 1R9S RELATED DB: PDB
REMARK 900 RNA POLYMERASE II STRAND SEPARATED ELONGATION COMPLEX,
REMARK 900 MATCHED NUCLEOTIDE
REMARK 900 RELATED ID: 1TWG RELATED DB: PDB
REMARK 900 RNA POLYMERASE II COMPLEXED WITH CTP
REMARK 900 RELATED ID: 1SFO RELATED DB: PDB
REMARK 900 RNA POLYMERASE II STRAND SEPARATED ELONGATION COMPLEX
REMARK 900 RELATED ID: 1I50 RELATED DB: PDB
REMARK 900 RNA POLYMERASE II CRYSTAL FORM II AT 2.8 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 4A3F RELATED DB: PDB
REMARK 900 RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A
REMARK 900 6NT DNA-RNA HYBRID AND SOAKED WITH AMPCPP
REMARK 900 RELATED ID: 4A3D RELATED DB: PDB
REMARK 900 RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A
REMARK 900 6NT DNA-RNA HYBRID
REMARK 900 RELATED ID: 1R5U RELATED DB: PDB
REMARK 900 RNA POLYMERASE II TFIIB COMPLEX
REMARK 900 RELATED ID: 1DZF RELATED DB: PDB
REMARK 900 RPB5 FROM S.CEREVISIAE
REMARK 900 RELATED ID: 4A3E RELATED DB: PDB
REMARK 900 RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A
REMARK 900 5NT DNA-RNA HYBRID AND SOAKED WITH AMPCPP
REMARK 900 RELATED ID: 1Y14 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST SUBCOMPLEX OF RPB4 AND RPB7
REMARK 900 RELATED ID: 1Y1W RELATED DB: PDB
REMARK 900 COMPLETE RNA POLYMERASE II ELONGATION COMPLEX
REMARK 900 RELATED ID: 1NT9 RELATED DB: PDB
REMARK 900 COMPLETE 12-SUBUNIT RNA POLYMERASE II
REMARK 900 RELATED ID: 1PQV RELATED DB: PDB
REMARK 900 RNA POLYMERASE II-TFIIS COMPLEX
REMARK 900 RELATED ID: 1TWF RELATED DB: PDB
REMARK 900 RNA POLYMERASE II COMPLEXED WITH UTP AT 2.3 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1I3Q RELATED DB: PDB
REMARK 900 RNA POLYMERASE II CRYSTAL FORM I AT 3.1 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 4A3G RELATED DB: PDB
REMARK 900 RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A
REMARK 900 2NT DNA-RNA HYBRID
REMARK 900 RELATED ID: 4A3C RELATED DB: PDB
REMARK 900 RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A
REMARK 900 5NT DNA-RNA HYBRID
REMARK 900 RELATED ID: 4A3I RELATED DB: PDB
REMARK 900 RNA POLYMERASE II BINARY COMPLEX WITH DNA
REMARK 900 RELATED ID: 4A3B RELATED DB: PDB
REMARK 900 RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A
REMARK 900 4NT DNA-RNA HYBRID
REMARK 900 RELATED ID: 1I6H RELATED DB: PDB
REMARK 900 RNA POLYMERASE II ELONGATION COMPLEX
REMARK 900 RELATED ID: 1Y1V RELATED DB: PDB
REMARK 900 REFINED RNA POLYMERASE II-TFIIS COMPLEX
REMARK 900 RELATED ID: 1Y1Y RELATED DB: PDB
REMARK 900 RNA POLYMERASE II-TFIIS-DNA/RNA COMPLEX
REMARK 900 RELATED ID: 1WCM RELATED DB: PDB
REMARK 900 COMPLETE 12-SUBUNIT RNA POLYMERASE II AT 3.8 A
REMARK 900 RELATED ID: 4A3M RELATED DB: PDB
REMARK 900 RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A
REMARK 900 4NT DNA-RNA HYBRID AND SOAKED WITH AMPCPP
REMARK 900 RELATED ID: 1TWA RELATED DB: PDB
REMARK 900 RNA POLYMERASE II COMPLEXED WITH ATP
REMARK 900 RELATED ID: 1NIK RELATED DB: PDB
REMARK 900 WILD TYPE RNA POLYMERASE II
REMARK 900 RELATED ID: 1TWH RELATED DB: PDB
REMARK 900 RNA POLYMERASE II COMPLEXED WITH 2'DATP
REMARK 900 RELATED ID: 2VUM RELATED DB: PDB
REMARK 900 ALPHA-AMANITIN INHIBITED COMPLETE RNA POLYMERASE II
REMARK 900 ELONGATION COMPLEX
REMARK 900 RELATED ID: 1R9T RELATED DB: PDB
REMARK 900 RNA POLYMERASE II STRAND SEPARATED ELONGATION COMPLEX,
REMARK 900 MISMATCHED NUCLEOTIDE
REMARK 900 RELATED ID: 2JA7 RELATED DB: PDB
REMARK 900 CPD LESION CONTAINING RNA POLYMERASE II ELONGATION
REMARK 900 COMPLEX C
REMARK 900 RELATED ID: 2JA6 RELATED DB: PDB
REMARK 900 CPD LESION CONTAINING RNA POLYMERASE II ELONGATION
REMARK 900 COMPLEX B
REMARK 900 RELATED ID: 4A3L RELATED DB: PDB
REMARK 900 RNA POLYMERASE II INITIAL TRANSCRIBING COMPLEX WITH A
REMARK 900 7NT DNA-RNA HYBRID AND SOAKED WITH AMPCPP
REMARK 900 RELATED ID: 1A1D RELATED DB: PDB
REMARK 900 YEAST RIBONUCLEIC ACID POLYMERASE SUBUNIT RPB8, NMR,
REMARK 900 MINIMIZED AVERAGE STRUCTURE, ALPHA CARBONS ONLY
REMARK 900 RELATED ID: 1K83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST RNA POLYMERASE II COMPLEXED
REMARK 900 WITHTHE INHIBITOR ALPHA AMANITIN
REMARK 900 RELATED ID: 2B63 RELATED DB: PDB
REMARK 900 COMPLETE RNA POLYMERASE II-RNA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 2B8K RELATED DB: PDB
REMARK 900 12-SUBUNIT RNA POLYMERASE II
REMARK 900 RELATED ID: 2JA5 RELATED DB: PDB
REMARK 900 CPD LESION CONTAINING RNA POLYMERASE II ELONGATION
REMARK 900 COMPLEX A
REMARK 900 RELATED ID: 2JA8 RELATED DB: PDB
REMARK 900 CPD LESION CONTAINING RNA POLYMERASE II ELONGATION
REMARK 900 COMPLEX D
DBREF 4A3J A 1 1732 UNP P04050 RPB1_YEAST 1 1732
DBREF 4A3J B 1 1224 UNP P08518 RPB2_YEAST 1 1224
DBREF 4A3J C 1 318 UNP P16370 RPB3_YEAST 1 318
DBREF 4A3J D 1 221 UNP P20433 RPB4_YEAST 1 221
DBREF 4A3J E 1 215 UNP P20434 RPAB1_YEAST 1 215
DBREF 4A3J F 1 155 UNP P20435 RPAB2_YEAST 1 155
DBREF 4A3J G 1 171 UNP P34087 RPB7_YEAST 1 171
DBREF 4A3J H 1 146 UNP P20436 RPAB3_YEAST 1 146
DBREF 4A3J I 1 122 UNP P27999 RPB9_YEAST 1 122
DBREF 4A3J J 1 70 UNP P22139 RPAB5_YEAST 1 70
DBREF 4A3J K 1 120 UNP P38902 RPB11_YEAST 1 120
DBREF 4A3J L 1 70 UNP P40422 RPAB4_YEAST 1 70
DBREF 4A3J N 0 13 PDB 4A3J 4A3J 0 13
DBREF 4A3J P 9 10 PDB 4A3J 4A3J 9 10
DBREF 4A3J T 4 30 PDB 4A3J 4A3J 4 30
SEQRES 1 A 1732 MET VAL GLY GLN GLN TYR SER SER ALA PRO LEU ARG THR
SEQRES 2 A 1732 VAL LYS GLU VAL GLN PHE GLY LEU PHE SER PRO GLU GLU
SEQRES 3 A 1732 VAL ARG ALA ILE SER VAL ALA LYS ILE ARG PHE PRO GLU
SEQRES 4 A 1732 THR MET ASP GLU THR GLN THR ARG ALA LYS ILE GLY GLY
SEQRES 5 A 1732 LEU ASN ASP PRO ARG LEU GLY SER ILE ASP ARG ASN LEU
SEQRES 6 A 1732 LYS CYS GLN THR CYS GLN GLU GLY MET ASN GLU CYS PRO
SEQRES 7 A 1732 GLY HIS PHE GLY HIS ILE ASP LEU ALA LYS PRO VAL PHE
SEQRES 8 A 1732 HIS VAL GLY PHE ILE ALA LYS ILE LYS LYS VAL CYS GLU
SEQRES 9 A 1732 CYS VAL CYS MET HIS CYS GLY LYS LEU LEU LEU ASP GLU
SEQRES 10 A 1732 HIS ASN GLU LEU MET ARG GLN ALA LEU ALA ILE LYS ASP
SEQRES 11 A 1732 SER LYS LYS ARG PHE ALA ALA ILE TRP THR LEU CYS LYS
SEQRES 12 A 1732 THR LYS MET VAL CYS GLU THR ASP VAL PRO SER GLU ASP
SEQRES 13 A 1732 ASP PRO THR GLN LEU VAL SER ARG GLY GLY CYS GLY ASN
SEQRES 14 A 1732 THR GLN PRO THR ILE ARG LYS ASP GLY LEU LYS LEU VAL
SEQRES 15 A 1732 GLY SER TRP LYS LYS ASP ARG ALA THR GLY ASP ALA ASP
SEQRES 16 A 1732 GLU PRO GLU LEU ARG VAL LEU SER THR GLU GLU ILE LEU
SEQRES 17 A 1732 ASN ILE PHE LYS HIS ILE SER VAL LYS ASP PHE THR SER
SEQRES 18 A 1732 LEU GLY PHE ASN GLU VAL PHE SER ARG PRO GLU TRP MET
SEQRES 19 A 1732 ILE LEU THR CYS LEU PRO VAL PRO PRO PRO PRO VAL ARG
SEQRES 20 A 1732 PRO SER ILE SER PHE ASN GLU SER GLN ARG GLY GLU ASP
SEQRES 21 A 1732 ASP LEU THR PHE LYS LEU ALA ASP ILE LEU LYS ALA ASN
SEQRES 22 A 1732 ILE SER LEU GLU THR LEU GLU HIS ASN GLY ALA PRO HIS
SEQRES 23 A 1732 HIS ALA ILE GLU GLU ALA GLU SER LEU LEU GLN PHE HIS
SEQRES 24 A 1732 VAL ALA THR TYR MET ASP ASN ASP ILE ALA GLY GLN PRO
SEQRES 25 A 1732 GLN ALA LEU GLN LYS SER GLY ARG PRO VAL LYS SER ILE
SEQRES 26 A 1732 ARG ALA ARG LEU LYS GLY LYS GLU GLY ARG ILE ARG GLY
SEQRES 27 A 1732 ASN LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG THR
SEQRES 28 A 1732 VAL ILE SER GLY ASP PRO ASN LEU GLU LEU ASP GLN VAL
SEQRES 29 A 1732 GLY VAL PRO LYS SER ILE ALA LYS THR LEU THR TYR PRO
SEQRES 30 A 1732 GLU VAL VAL THR PRO TYR ASN ILE ASP ARG LEU THR GLN
SEQRES 31 A 1732 LEU VAL ARG ASN GLY PRO ASN GLU HIS PRO GLY ALA LYS
SEQRES 32 A 1732 TYR VAL ILE ARG ASP SER GLY ASP ARG ILE ASP LEU ARG
SEQRES 33 A 1732 TYR SER LYS ARG ALA GLY ASP ILE GLN LEU GLN TYR GLY
SEQRES 34 A 1732 TRP LYS VAL GLU ARG HIS ILE MET ASP ASN ASP PRO VAL
SEQRES 35 A 1732 LEU PHE ASN ARG GLN PRO SER LEU HIS LYS MET SER MET
SEQRES 36 A 1732 MET ALA HIS ARG VAL LYS VAL ILE PRO TYR SER THR PHE
SEQRES 37 A 1732 ARG LEU ASN LEU SER VAL THR SER PRO TYR ASN ALA ASP
SEQRES 38 A 1732 PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN SER
SEQRES 39 A 1732 GLU GLU THR ARG ALA GLU LEU SER GLN LEU CYS ALA VAL
SEQRES 40 A 1732 PRO LEU GLN ILE VAL SER PRO GLN SER ASN LYS PRO CYS
SEQRES 41 A 1732 MET GLY ILE VAL GLN ASP THR LEU CYS GLY ILE ARG LYS
SEQRES 42 A 1732 LEU THR LEU ARG ASP THR PHE ILE GLU LEU ASP GLN VAL
SEQRES 43 A 1732 LEU ASN MET LEU TYR TRP VAL PRO ASP TRP ASP GLY VAL
SEQRES 44 A 1732 ILE PRO THR PRO ALA ILE ILE LYS PRO LYS PRO LEU TRP
SEQRES 45 A 1732 SER GLY LYS GLN ILE LEU SER VAL ALA ILE PRO ASN GLY
SEQRES 46 A 1732 ILE HIS LEU GLN ARG PHE ASP GLU GLY THR THR LEU LEU
SEQRES 47 A 1732 SER PRO LYS ASP ASN GLY MET LEU ILE ILE ASP GLY GLN
SEQRES 48 A 1732 ILE ILE PHE GLY VAL VAL GLU LYS LYS THR VAL GLY SER
SEQRES 49 A 1732 SER ASN GLY GLY LEU ILE HIS VAL VAL THR ARG GLU LYS
SEQRES 50 A 1732 GLY PRO GLN VAL CYS ALA LYS LEU PHE GLY ASN ILE GLN
SEQRES 51 A 1732 LYS VAL VAL ASN PHE TRP LEU LEU HIS ASN GLY PHE SER
SEQRES 52 A 1732 THR GLY ILE GLY ASP THR ILE ALA ASP GLY PRO THR MET
SEQRES 53 A 1732 ARG GLU ILE THR GLU THR ILE ALA GLU ALA LYS LYS LYS
SEQRES 54 A 1732 VAL LEU ASP VAL THR LYS GLU ALA GLN ALA ASN LEU LEU
SEQRES 55 A 1732 THR ALA LYS HIS GLY MET THR LEU ARG GLU SER PHE GLU
SEQRES 56 A 1732 ASP ASN VAL VAL ARG PHE LEU ASN GLU ALA ARG ASP LYS
SEQRES 57 A 1732 ALA GLY ARG LEU ALA GLU VAL ASN LEU LYS ASP LEU ASN
SEQRES 58 A 1732 ASN VAL LYS GLN MET VAL MET ALA GLY SER LYS GLY SER
SEQRES 59 A 1732 PHE ILE ASN ILE ALA GLN MET SER ALA CYS VAL GLY GLN
SEQRES 60 A 1732 GLN SER VAL GLU GLY LYS ARG ILE ALA PHE GLY PHE VAL
SEQRES 61 A 1732 ASP ARG THR LEU PRO HIS PHE SER LYS ASP ASP TYR SER
SEQRES 62 A 1732 PRO GLU SER LYS GLY PHE VAL GLU ASN SER TYR LEU ARG
SEQRES 63 A 1732 GLY LEU THR PRO GLN GLU PHE PHE PHE HIS ALA MET GLY
SEQRES 64 A 1732 GLY ARG GLU GLY LEU ILE ASP THR ALA VAL LYS THR ALA
SEQRES 65 A 1732 GLU THR GLY TYR ILE GLN ARG ARG LEU VAL LYS ALA LEU
SEQRES 66 A 1732 GLU ASP ILE MET VAL HIS TYR ASP ASN THR THR ARG ASN
SEQRES 67 A 1732 SER LEU GLY ASN VAL ILE GLN PHE ILE TYR GLY GLU ASP
SEQRES 68 A 1732 GLY MET ASP ALA ALA HIS ILE GLU LYS GLN SER LEU ASP
SEQRES 69 A 1732 THR ILE GLY GLY SER ASP ALA ALA PHE GLU LYS ARG TYR
SEQRES 70 A 1732 ARG VAL ASP LEU LEU ASN THR ASP HIS THR LEU ASP PRO
SEQRES 71 A 1732 SER LEU LEU GLU SER GLY SER GLU ILE LEU GLY ASP LEU
SEQRES 72 A 1732 LYS LEU GLN VAL LEU LEU ASP GLU GLU TYR LYS GLN LEU
SEQRES 73 A 1732 VAL LYS ASP ARG LYS PHE LEU ARG GLU VAL PHE VAL ASP
SEQRES 74 A 1732 GLY GLU ALA ASN TRP PRO LEU PRO VAL ASN ILE ARG ARG
SEQRES 75 A 1732 ILE ILE GLN ASN ALA GLN GLN THR PHE HIS ILE ASP HIS
SEQRES 76 A 1732 THR LYS PRO SER ASP LEU THR ILE LYS ASP ILE VAL LEU
SEQRES 77 A 1732 GLY VAL LYS ASP LEU GLN GLU ASN LEU LEU VAL LEU ARG
SEQRES 78 A 1732 GLY LYS ASN GLU ILE ILE GLN ASN ALA GLN ARG ASP ALA
SEQRES 79 A 1732 VAL THR LEU PHE CYS CYS LEU LEU ARG SER ARG LEU ALA
SEQRES 80 A 1732 THR ARG ARG VAL LEU GLN GLU TYR ARG LEU THR LYS GLN
SEQRES 81 A 1732 ALA PHE ASP TRP VAL LEU SER ASN ILE GLU ALA GLN PHE
SEQRES 82 A 1732 LEU ARG SER VAL VAL HIS PRO GLY GLU MET VAL GLY VAL
SEQRES 83 A 1732 LEU ALA ALA GLN SER ILE GLY GLU PRO ALA THR GLN MET
SEQRES 84 A 1732 THR LEU ASN THR PHE HIS PHE ALA GLY VAL ALA SER LYS
SEQRES 85 A 1732 LYS VAL THR SER GLY VAL PRO ARG LEU LYS GLU ILE LEU
SEQRES 86 A 1732 ASN VAL ALA LYS ASN MET LYS THR PRO SER LEU THR VAL
SEQRES 87 A 1732 TYR LEU GLU PRO GLY HIS ALA ALA ASP GLN GLU GLN ALA
SEQRES 88 A 1732 LYS LEU ILE ARG SER ALA ILE GLU HIS THR THR LEU LYS
SEQRES 89 A 1732 SER VAL THR ILE ALA SER GLU ILE TYR TYR ASP PRO ASP
SEQRES 90 A 1732 PRO ARG SER THR VAL ILE PRO GLU ASP GLU GLU ILE ILE
SEQRES 91 A 1732 GLN LEU HIS PHE SER LEU LEU ASP GLU GLU ALA GLU GLN
SEQRES 92 A 1732 SER PHE ASP GLN GLN SER PRO TRP LEU LEU ARG LEU GLU
SEQRES 93 A 1732 LEU ASP ARG ALA ALA MET ASN ASP LYS ASP LEU THR MET
SEQRES 94 A 1732 GLY GLN VAL GLY GLU ARG ILE LYS GLN THR PHE LYS ASN
SEQRES 95 A 1732 ASP LEU PHE VAL ILE TRP SER GLU ASP ASN ASP GLU LYS
SEQRES 96 A 1732 LEU ILE ILE ARG CYS ARG VAL VAL ARG PRO LYS SER LEU
SEQRES 97 A 1732 ASP ALA GLU THR GLU ALA GLU GLU ASP HIS MET LEU LYS
SEQRES 98 A 1732 LYS ILE GLU ASN THR MET LEU GLU ASN ILE THR LEU ARG
SEQRES 99 A 1732 GLY VAL GLU ASN ILE GLU ARG VAL VAL MET MET LYS TYR
SEQRES 100 A 1732 ASP ARG LYS VAL PRO SER PRO THR GLY GLU TYR VAL LYS
SEQRES 101 A 1732 GLU PRO GLU TRP VAL LEU GLU THR ASP GLY VAL ASN LEU
SEQRES 102 A 1732 SER GLU VAL MET THR VAL PRO GLY ILE ASP PRO THR ARG
SEQRES 103 A 1732 ILE TYR THR ASN SER PHE ILE ASP ILE MET GLU VAL LEU
SEQRES 104 A 1732 GLY ILE GLU ALA GLY ARG ALA ALA LEU TYR LYS GLU VAL
SEQRES 105 A 1732 TYR ASN VAL ILE ALA SER ASP GLY SER TYR VAL ASN TYR
SEQRES 106 A 1732 ARG HIS MET ALA LEU LEU VAL ASP VAL MET THR THR GLN
SEQRES 107 A 1732 GLY GLY LEU THR SER VAL THR ARG HIS GLY PHE ASN ARG
SEQRES 108 A 1732 SER ASN THR GLY ALA LEU MET ARG CYS SER PHE GLU GLU
SEQRES 109 A 1732 THR VAL GLU ILE LEU PHE GLU ALA GLY ALA SER ALA GLU
SEQRES 110 A 1732 LEU ASP ASP CYS ARG GLY VAL SER GLU ASN VAL ILE LEU
SEQRES 111 A 1732 GLY GLN MET ALA PRO ILE GLY THR GLY ALA PHE ASP VAL
SEQRES 112 A 1732 MET ILE ASP GLU GLU SER LEU VAL LYS TYR MET PRO GLU
SEQRES 113 A 1732 GLN LYS ILE THR GLU ILE GLU ASP GLY GLN ASP GLY GLY
SEQRES 114 A 1732 VAL THR PRO TYR SER ASN GLU SER GLY LEU VAL ASN ALA
SEQRES 115 A 1732 ASP LEU ASP VAL LYS ASP GLU LEU MET PHE SER PRO LEU
SEQRES 116 A 1732 VAL ASP SER GLY SER ASN ASP ALA MET ALA GLY GLY PHE
SEQRES 117 A 1732 THR ALA TYR GLY GLY ALA ASP TYR GLY GLU ALA THR SER
SEQRES 118 A 1732 PRO PHE GLY ALA TYR GLY GLU ALA PRO THR SER PRO GLY
SEQRES 119 A 1732 PHE GLY VAL SER SER PRO GLY PHE SER PRO THR SER PRO
SEQRES 120 A 1732 THR TYR SER PRO THR SER PRO ALA TYR SER PRO THR SER
SEQRES 121 A 1732 PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR
SEQRES 122 A 1732 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 123 A 1732 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 124 A 1732 PRO THR SER PRO SER TYR SER PRO THR SER PRO SER TYR
SEQRES 125 A 1732 SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER
SEQRES 126 A 1732 TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO
SEQRES 127 A 1732 SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER
SEQRES 128 A 1732 PRO SER TYR SER PRO THR SER PRO ALA TYR SER PRO THR
SEQRES 129 A 1732 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 130 A 1732 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 131 A 1732 PRO THR SER PRO ASN TYR SER PRO THR SER PRO SER TYR
SEQRES 132 A 1732 SER PRO THR SER PRO GLY TYR SER PRO GLY SER PRO ALA
SEQRES 133 A 1732 TYR SER PRO LYS GLN ASP GLU GLN LYS HIS ASN GLU ASN
SEQRES 134 A 1732 GLU ASN SER
SEQRES 1 B 1224 MET SER ASP LEU ALA ASN SER GLU LYS TYR TYR ASP GLU
SEQRES 2 B 1224 ASP PRO TYR GLY PHE GLU ASP GLU SER ALA PRO ILE THR
SEQRES 3 B 1224 ALA GLU ASP SER TRP ALA VAL ILE SER ALA PHE PHE ARG
SEQRES 4 B 1224 GLU LYS GLY LEU VAL SER GLN GLN LEU ASP SER PHE ASN
SEQRES 5 B 1224 GLN PHE VAL ASP TYR THR LEU GLN ASP ILE ILE CYS GLU
SEQRES 6 B 1224 ASP SER THR LEU ILE LEU GLU GLN LEU ALA GLN HIS THR
SEQRES 7 B 1224 THR GLU SER ASP ASN ILE SER ARG LYS TYR GLU ILE SER
SEQRES 8 B 1224 PHE GLY LYS ILE TYR VAL THR LYS PRO MET VAL ASN GLU
SEQRES 9 B 1224 SER ASP GLY VAL THR HIS ALA LEU TYR PRO GLN GLU ALA
SEQRES 10 B 1224 ARG LEU ARG ASN LEU THR TYR SER SER GLY LEU PHE VAL
SEQRES 11 B 1224 ASP VAL LYS LYS ARG THR TYR GLU ALA ILE ASP VAL PRO
SEQRES 12 B 1224 GLY ARG GLU LEU LYS TYR GLU LEU ILE ALA GLU GLU SER
SEQRES 13 B 1224 GLU ASP ASP SER GLU SER GLY LYS VAL PHE ILE GLY ARG
SEQRES 14 B 1224 LEU PRO ILE MET LEU ARG SER LYS ASN CYS TYR LEU SER
SEQRES 15 B 1224 GLU ALA THR GLU SER ASP LEU TYR LYS LEU LYS GLU CYS
SEQRES 16 B 1224 PRO PHE ASP MET GLY GLY TYR PHE ILE ILE ASN GLY SER
SEQRES 17 B 1224 GLU LYS VAL LEU ILE ALA GLN GLU ARG SER ALA GLY ASN
SEQRES 18 B 1224 ILE VAL GLN VAL PHE LYS LYS ALA ALA PRO SER PRO ILE
SEQRES 19 B 1224 SER HIS VAL ALA GLU ILE ARG SER ALA LEU GLU LYS GLY
SEQRES 20 B 1224 SER ARG PHE ILE SER THR LEU GLN VAL LYS LEU TYR GLY
SEQRES 21 B 1224 ARG GLU GLY SER SER ALA ARG THR ILE LYS ALA THR LEU
SEQRES 22 B 1224 PRO TYR ILE LYS GLN ASP ILE PRO ILE VAL ILE ILE PHE
SEQRES 23 B 1224 ARG ALA LEU GLY ILE ILE PRO ASP GLY GLU ILE LEU GLU
SEQRES 24 B 1224 HIS ILE CYS TYR ASP VAL ASN ASP TRP GLN MET LEU GLU
SEQRES 25 B 1224 MET LEU LYS PRO CYS VAL GLU ASP GLY PHE VAL ILE GLN
SEQRES 26 B 1224 ASP ARG GLU THR ALA LEU ASP PHE ILE GLY ARG ARG GLY
SEQRES 27 B 1224 THR ALA LEU GLY ILE LYS LYS GLU LYS ARG ILE GLN TYR
SEQRES 28 B 1224 ALA LYS ASP ILE LEU GLN LYS GLU PHE LEU PRO HIS ILE
SEQRES 29 B 1224 THR GLN LEU GLU GLY PHE GLU SER ARG LYS ALA PHE PHE
SEQRES 30 B 1224 LEU GLY TYR MET ILE ASN ARG LEU LEU LEU CYS ALA LEU
SEQRES 31 B 1224 ASP ARG LYS ASP GLN ASP ASP ARG ASP HIS PHE GLY LYS
SEQRES 32 B 1224 LYS ARG LEU ASP LEU ALA GLY PRO LEU LEU ALA GLN LEU
SEQRES 33 B 1224 PHE LYS THR LEU PHE LYS LYS LEU THR LYS ASP ILE PHE
SEQRES 34 B 1224 ARG TYR MET GLN ARG THR VAL GLU GLU ALA HIS ASP PHE
SEQRES 35 B 1224 ASN MET LYS LEU ALA ILE ASN ALA LYS THR ILE THR SER
SEQRES 36 B 1224 GLY LEU LYS TYR ALA LEU ALA THR GLY ASN TRP GLY GLU
SEQRES 37 B 1224 GLN LYS LYS ALA MET SER SER ARG ALA GLY VAL SER GLN
SEQRES 38 B 1224 VAL LEU ASN ARG TYR THR TYR SER SER THR LEU SER HIS
SEQRES 39 B 1224 LEU ARG ARG THR ASN THR PRO ILE GLY ARG ASP GLY LYS
SEQRES 40 B 1224 LEU ALA LYS PRO ARG GLN LEU HIS ASN THR HIS TRP GLY
SEQRES 41 B 1224 LEU VAL CYS PRO ALA GLU THR PRO GLU GLY GLN ALA CYS
SEQRES 42 B 1224 GLY LEU VAL LYS ASN LEU SER LEU MET SER CYS ILE SER
SEQRES 43 B 1224 VAL GLY THR ASP PRO MET PRO ILE ILE THR PHE LEU SER
SEQRES 44 B 1224 GLU TRP GLY MET GLU PRO LEU GLU ASP TYR VAL PRO HIS
SEQRES 45 B 1224 GLN SER PRO ASP ALA THR ARG VAL PHE VAL ASN GLY VAL
SEQRES 46 B 1224 TRP HIS GLY VAL HIS ARG ASN PRO ALA ARG LEU MET GLU
SEQRES 47 B 1224 THR LEU ARG THR LEU ARG ARG LYS GLY ASP ILE ASN PRO
SEQRES 48 B 1224 GLU VAL SER MET ILE ARG ASP ILE ARG GLU LYS GLU LEU
SEQRES 49 B 1224 LYS ILE PHE THR ASP ALA GLY ARG VAL TYR ARG PRO LEU
SEQRES 50 B 1224 PHE ILE VAL GLU ASP ASP GLU SER LEU GLY HIS LYS GLU
SEQRES 51 B 1224 LEU LYS VAL ARG LYS GLY HIS ILE ALA LYS LEU MET ALA
SEQRES 52 B 1224 THR GLU TYR GLN ASP ILE GLU GLY GLY PHE GLU ASP VAL
SEQRES 53 B 1224 GLU GLU TYR THR TRP SER SER LEU LEU ASN GLU GLY LEU
SEQRES 54 B 1224 VAL GLU TYR ILE ASP ALA GLU GLU GLU GLU SER ILE LEU
SEQRES 55 B 1224 ILE ALA MET GLN PRO GLU ASP LEU GLU PRO ALA GLU ALA
SEQRES 56 B 1224 ASN GLU GLU ASN ASP LEU ASP VAL ASP PRO ALA LYS ARG
SEQRES 57 B 1224 ILE ARG VAL SER HIS HIS ALA THR THR PHE THR HIS CYS
SEQRES 58 B 1224 GLU ILE HIS PRO SER MET ILE LEU GLY VAL ALA ALA SER
SEQRES 59 B 1224 ILE ILE PRO PHE PRO ASP HIS ASN GLN SER PRO ARG ASN
SEQRES 60 B 1224 THR TYR GLN SER ALA MET GLY LYS GLN ALA MET GLY VAL
SEQRES 61 B 1224 PHE LEU THR ASN TYR ASN VAL ARG MET ASP THR MET ALA
SEQRES 62 B 1224 ASN ILE LEU TYR TYR PRO GLN LYS PRO LEU GLY THR THR
SEQRES 63 B 1224 ARG ALA MET GLU TYR LEU LYS PHE ARG GLU LEU PRO ALA
SEQRES 64 B 1224 GLY GLN ASN ALA ILE VAL ALA ILE ALA CYS TYR SER GLY
SEQRES 65 B 1224 TYR ASN GLN GLU ASP SER MET ILE MET ASN GLN SER SER
SEQRES 66 B 1224 ILE ASP ARG GLY LEU PHE ARG SER LEU PHE PHE ARG SER
SEQRES 67 B 1224 TYR MET ASP GLN GLU LYS LYS TYR GLY MET SER ILE THR
SEQRES 68 B 1224 GLU THR PHE GLU LYS PRO GLN ARG THR ASN THR LEU ARG
SEQRES 69 B 1224 MET LYS HIS GLY THR TYR ASP LYS LEU ASP ASP ASP GLY
SEQRES 70 B 1224 LEU ILE ALA PRO GLY VAL ARG VAL SER GLY GLU ASP VAL
SEQRES 71 B 1224 ILE ILE GLY LYS THR THR PRO ILE SER PRO ASP GLU GLU
SEQRES 72 B 1224 GLU LEU GLY GLN ARG THR ALA TYR HIS SER LYS ARG ASP
SEQRES 73 B 1224 ALA SER THR PRO LEU ARG SER THR GLU ASN GLY ILE VAL
SEQRES 74 B 1224 ASP GLN VAL LEU VAL THR THR ASN GLN ASP GLY LEU LYS
SEQRES 75 B 1224 PHE VAL LYS VAL ARG VAL ARG THR THR LYS ILE PRO GLN
SEQRES 76 B 1224 ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN LYS GLY
SEQRES 77 B 1224 THR ILE GLY ILE THR TYR ARG ARG GLU ASP MET PRO PHE
SEQRES 78 B 1224 THR ALA GLU GLY ILE VAL PRO ASP LEU ILE ILE ASN PRO
SEQRES 79 B 1224 HIS ALA ILE PRO SER ARG MET THR VAL ALA HIS LEU ILE
SEQRES 80 B 1224 GLU CYS LEU LEU SER LYS VAL ALA ALA LEU SER GLY ASN
SEQRES 81 B 1224 GLU GLY ASP ALA SER PRO PHE THR ASP ILE THR VAL GLU
SEQRES 82 B 1224 GLY ILE SER LYS LEU LEU ARG GLU HIS GLY TYR GLN SER
SEQRES 83 B 1224 ARG GLY PHE GLU VAL MET TYR ASN GLY HIS THR GLY LYS
SEQRES 84 B 1224 LYS LEU MET ALA GLN ILE PHE PHE GLY PRO THR TYR TYR
SEQRES 85 B 1224 GLN ARG LEU ARG HIS MET VAL ASP ASP LYS ILE HIS ALA
SEQRES 86 B 1224 ARG ALA ARG GLY PRO MET GLN VAL LEU THR ARG GLN PRO
SEQRES 87 B 1224 VAL GLU GLY ARG SER ARG ASP GLY GLY LEU ARG PHE GLY
SEQRES 88 B 1224 GLU MET GLU ARG ASP CYS MET ILE ALA HIS GLY ALA ALA
SEQRES 89 B 1224 SER PHE LEU LYS GLU ARG LEU MET GLU ALA SER ASP ALA
SEQRES 90 B 1224 PHE ARG VAL HIS ILE CYS GLY ILE CYS GLY LEU MET THR
SEQRES 91 B 1224 VAL ILE ALA LYS LEU ASN HIS ASN GLN PHE GLU CYS LYS
SEQRES 92 B 1224 GLY CYS ASP ASN LYS ILE ASP ILE TYR GLN ILE HIS ILE
SEQRES 93 B 1224 PRO TYR ALA ALA LYS LEU LEU PHE GLN GLU LEU MET ALA
SEQRES 94 B 1224 MET ASN ILE THR PRO ARG LEU TYR THR ASP ARG SER ARG
SEQRES 95 B 1224 ASP PHE
SEQRES 1 C 318 MET SER GLU GLU GLY PRO GLN VAL LYS ILE ARG GLU ALA
SEQRES 2 C 318 SER LYS ASP ASN VAL ASP PHE ILE LEU SER ASN VAL ASP
SEQRES 3 C 318 LEU ALA MET ALA ASN SER LEU ARG ARG VAL MET ILE ALA
SEQRES 4 C 318 GLU ILE PRO THR LEU ALA ILE ASP SER VAL GLU VAL GLU
SEQRES 5 C 318 THR ASN THR THR VAL LEU ALA ASP GLU PHE ILE ALA HIS
SEQRES 6 C 318 ARG LEU GLY LEU ILE PRO LEU GLN SER MET ASP ILE GLU
SEQRES 7 C 318 GLN LEU GLU TYR SER ARG ASP CYS PHE CYS GLU ASP HIS
SEQRES 8 C 318 CYS ASP LYS CYS SER VAL VAL LEU THR LEU GLN ALA PHE
SEQRES 9 C 318 GLY GLU SER GLU SER THR THR ASN VAL TYR SER LYS ASP
SEQRES 10 C 318 LEU VAL ILE VAL SER ASN LEU MET GLY ARG ASN ILE GLY
SEQRES 11 C 318 HIS PRO ILE ILE GLN ASP LYS GLU GLY ASN GLY VAL LEU
SEQRES 12 C 318 ILE CYS LYS LEU ARG LYS GLY GLN GLU LEU LYS LEU THR
SEQRES 13 C 318 CYS VAL ALA LYS LYS GLY ILE ALA LYS GLU HIS ALA LYS
SEQRES 14 C 318 TRP GLY PRO ALA ALA ALA ILE GLU PHE GLU TYR ASP PRO
SEQRES 15 C 318 TRP ASN LYS LEU LYS HIS THR ASP TYR TRP TYR GLU GLN
SEQRES 16 C 318 ASP SER ALA LYS GLU TRP PRO GLN SER LYS ASN CYS GLU
SEQRES 17 C 318 TYR GLU ASP PRO PRO ASN GLU GLY ASP PRO PHE ASP TYR
SEQRES 18 C 318 LYS ALA GLN ALA ASP THR PHE TYR MET ASN VAL GLU SER
SEQRES 19 C 318 VAL GLY SER ILE PRO VAL ASP GLN VAL VAL VAL ARG GLY
SEQRES 20 C 318 ILE ASP THR LEU GLN LYS LYS VAL ALA SER ILE LEU LEU
SEQRES 21 C 318 ALA LEU THR GLN MET ASP GLN ASP LYS VAL ASN PHE ALA
SEQRES 22 C 318 SER GLY ASP ASN ASN THR ALA SER ASN MET LEU GLY SER
SEQRES 23 C 318 ASN GLU ASP VAL MET MET THR GLY ALA GLU GLN ASP PRO
SEQRES 24 C 318 TYR SER ASN ALA SER GLN MET GLY ASN THR GLY SER GLY
SEQRES 25 C 318 GLY TYR ASP ASN ALA TRP
SEQRES 1 D 221 MET ASN VAL SER THR SER THR PHE GLN THR ARG ARG ARG
SEQRES 2 D 221 ARG LEU LYS LYS VAL GLU GLU GLU GLU ASN ALA ALA THR
SEQRES 3 D 221 LEU GLN LEU GLY GLN GLU PHE GLN LEU LYS GLN ILE ASN
SEQRES 4 D 221 HIS GLN GLY GLU GLU GLU GLU LEU ILE ALA LEU ASN LEU
SEQRES 5 D 221 SER GLU ALA ARG LEU VAL ILE LYS GLU ALA LEU VAL GLU
SEQRES 6 D 221 ARG ARG ARG ALA PHE LYS ARG SER GLN LYS LYS HIS LYS
SEQRES 7 D 221 LYS LYS HIS LEU LYS HIS GLU ASN ALA ASN ASP GLU THR
SEQRES 8 D 221 THR ALA VAL GLU ASP GLU ASP ASP ASP LEU ASP GLU ASP
SEQRES 9 D 221 ASP VAL ASN ALA ASP ASP ASP ASP PHE MET HIS SER GLU
SEQRES 10 D 221 THR ARG GLU LYS GLU LEU GLU SER ILE ASP VAL LEU LEU
SEQRES 11 D 221 GLU GLN THR THR GLY GLY ASN ASN LYS ASP LEU LYS ASN
SEQRES 12 D 221 THR MET GLN TYR LEU THR ASN PHE SER ARG PHE ARG ASP
SEQRES 13 D 221 GLN GLU THR VAL GLY ALA VAL ILE GLN LEU LEU LYS SER
SEQRES 14 D 221 THR GLY LEU HIS PRO PHE GLU VAL ALA GLN LEU GLY SER
SEQRES 15 D 221 LEU ALA CYS ASP THR ALA ASP GLU ALA LYS THR LEU ILE
SEQRES 16 D 221 PRO SER LEU ASN ASN LYS ILE SER ASP ASP GLU LEU GLU
SEQRES 17 D 221 ARG ILE LEU LYS GLU LEU SER ASN LEU GLU THR LEU TYR
SEQRES 1 E 215 MET ASP GLN GLU ASN GLU ARG ASN ILE SER ARG LEU TRP
SEQRES 2 E 215 ARG ALA PHE ARG THR VAL LYS GLU MET VAL LYS ASP ARG
SEQRES 3 E 215 GLY TYR PHE ILE THR GLN GLU GLU VAL GLU LEU PRO LEU
SEQRES 4 E 215 GLU ASP PHE LYS ALA LYS TYR CYS ASP SER MET GLY ARG
SEQRES 5 E 215 PRO GLN ARG LYS MET MET SER PHE GLN ALA ASN PRO THR
SEQRES 6 E 215 GLU GLU SER ILE SER LYS PHE PRO ASP MET GLY SER LEU
SEQRES 7 E 215 TRP VAL GLU PHE CYS ASP GLU PRO SER VAL GLY VAL LYS
SEQRES 8 E 215 THR MET LYS THR PHE VAL ILE HIS ILE GLN GLU LYS ASN
SEQRES 9 E 215 PHE GLN THR GLY ILE PHE VAL TYR GLN ASN ASN ILE THR
SEQRES 10 E 215 PRO SER ALA MET LYS LEU VAL PRO SER ILE PRO PRO ALA
SEQRES 11 E 215 THR ILE GLU THR PHE ASN GLU ALA ALA LEU VAL VAL ASN
SEQRES 12 E 215 ILE THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU
SEQRES 13 E 215 SER SER ASP GLU LYS ARG GLU LEU LEU LYS ARG TYR ARG
SEQRES 14 E 215 LEU LYS GLU SER GLN LEU PRO ARG ILE GLN ARG ALA ASP
SEQRES 15 E 215 PRO VAL ALA LEU TYR LEU GLY LEU LYS ARG GLY GLU VAL
SEQRES 16 E 215 VAL LYS ILE ILE ARG LYS SER GLU THR SER GLY ARG TYR
SEQRES 17 E 215 ALA SER TYR ARG ILE CYS MET
SEQRES 1 F 155 MET SER ASP TYR GLU GLU ALA PHE ASN ASP GLY ASN GLU
SEQRES 2 F 155 ASN PHE GLU ASP PHE ASP VAL GLU HIS PHE SER ASP GLU
SEQRES 3 F 155 GLU THR TYR GLU GLU LYS PRO GLN PHE LYS ASP GLY GLU
SEQRES 4 F 155 THR THR ASP ALA ASN GLY LYS THR ILE VAL THR GLY GLY
SEQRES 5 F 155 ASN GLY PRO GLU ASP PHE GLN GLN HIS GLU GLN ILE ARG
SEQRES 6 F 155 ARG LYS THR LEU LYS GLU LYS ALA ILE PRO LYS ASP GLN
SEQRES 7 F 155 ARG ALA THR THR PRO TYR MET THR LYS TYR GLU ARG ALA
SEQRES 8 F 155 ARG ILE LEU GLY THR ARG ALA LEU GLN ILE SER MET ASN
SEQRES 9 F 155 ALA PRO VAL PHE VAL ASP LEU GLU GLY GLU THR ASP PRO
SEQRES 10 F 155 LEU ARG ILE ALA MET LYS GLU LEU ALA GLU LYS LYS ILE
SEQRES 11 F 155 PRO LEU VAL ILE ARG ARG TYR LEU PRO ASP GLY SER PHE
SEQRES 12 F 155 GLU ASP TRP SER VAL GLU GLU LEU ILE VAL ASP LEU
SEQRES 1 G 171 MET PHE PHE ILE LYS ASP LEU SER LEU ASN ILE THR LEU
SEQRES 2 G 171 HIS PRO SER PHE PHE GLY PRO ARG MET LYS GLN TYR LEU
SEQRES 3 G 171 LYS THR LYS LEU LEU GLU GLU VAL GLU GLY SER CYS THR
SEQRES 4 G 171 GLY LYS PHE GLY TYR ILE LEU CYS VAL LEU ASP TYR ASP
SEQRES 5 G 171 ASN ILE ASP ILE GLN ARG GLY ARG ILE LEU PRO THR ASP
SEQRES 6 G 171 GLY SER ALA GLU PHE ASN VAL LYS TYR ARG ALA VAL VAL
SEQRES 7 G 171 PHE LYS PRO PHE LYS GLY GLU VAL VAL ASP GLY THR VAL
SEQRES 8 G 171 VAL SER CYS SER GLN HIS GLY PHE GLU VAL GLN VAL GLY
SEQRES 9 G 171 PRO MET LYS VAL PHE VAL THR LYS HIS LEU MET PRO GLN
SEQRES 10 G 171 ASP LEU THR PHE ASN ALA GLY SER ASN PRO PRO SER TYR
SEQRES 11 G 171 GLN SER SER GLU ASP VAL ILE THR ILE LYS SER ARG ILE
SEQRES 12 G 171 ARG VAL LYS ILE GLU GLY CYS ILE SER GLN VAL SER SER
SEQRES 13 G 171 ILE HIS ALA ILE GLY SER ILE LYS GLU ASP TYR LEU GLY
SEQRES 14 G 171 ALA ILE
SEQRES 1 H 146 MET SER ASN THR LEU PHE ASP ASP ILE PHE GLN VAL SER
SEQRES 2 H 146 GLU VAL ASP PRO GLY ARG TYR ASN LYS VAL CYS ARG ILE
SEQRES 3 H 146 GLU ALA ALA SER THR THR GLN ASP GLN CYS LYS LEU THR
SEQRES 4 H 146 LEU ASP ILE ASN VAL GLU LEU PHE PRO VAL ALA ALA GLN
SEQRES 5 H 146 ASP SER LEU THR VAL THR ILE ALA SER SER LEU ASN LEU
SEQRES 6 H 146 GLU ASP THR PRO ALA ASN ASP SER SER ALA THR ARG SER
SEQRES 7 H 146 TRP ARG PRO PRO GLN ALA GLY ASP ARG SER LEU ALA ASP
SEQRES 8 H 146 ASP TYR ASP TYR VAL MET TYR GLY THR ALA TYR LYS PHE
SEQRES 9 H 146 GLU GLU VAL SER LYS ASP LEU ILE ALA VAL TYR TYR SER
SEQRES 10 H 146 PHE GLY GLY LEU LEU MET ARG LEU GLU GLY ASN TYR ARG
SEQRES 11 H 146 ASN LEU ASN ASN LEU LYS GLN GLU ASN ALA TYR LEU LEU
SEQRES 12 H 146 ILE ARG ARG
SEQRES 1 I 122 MET THR THR PHE ARG PHE CYS ARG ASP CYS ASN ASN MET
SEQRES 2 I 122 LEU TYR PRO ARG GLU ASP LYS GLU ASN ASN ARG LEU LEU
SEQRES 3 I 122 PHE GLU CYS ARG THR CYS SER TYR VAL GLU GLU ALA GLY
SEQRES 4 I 122 SER PRO LEU VAL TYR ARG HIS GLU LEU ILE THR ASN ILE
SEQRES 5 I 122 GLY GLU THR ALA GLY VAL VAL GLN ASP ILE GLY SER ASP
SEQRES 6 I 122 PRO THR LEU PRO ARG SER ASP ARG GLU CYS PRO LYS CYS
SEQRES 7 I 122 HIS SER ARG GLU ASN VAL PHE PHE GLN SER GLN GLN ARG
SEQRES 8 I 122 ARG LYS ASP THR SER MET VAL LEU PHE PHE VAL CYS LEU
SEQRES 9 I 122 SER CYS SER HIS ILE PHE THR SER ASP GLN LYS ASN LYS
SEQRES 10 I 122 ARG THR GLN PHE SER
SEQRES 1 J 70 MET ILE VAL PRO VAL ARG CYS PHE SER CYS GLY LYS VAL
SEQRES 2 J 70 VAL GLY ASP LYS TRP GLU SER TYR LEU ASN LEU LEU GLN
SEQRES 3 J 70 GLU ASP GLU LEU ASP GLU GLY THR ALA LEU SER ARG LEU
SEQRES 4 J 70 GLY LEU LYS ARG TYR CYS CYS ARG ARG MET ILE LEU THR
SEQRES 5 J 70 HIS VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO
SEQRES 6 J 70 LEU GLU LYS ARG ASP
SEQRES 1 K 120 MET ASN ALA PRO ASP ARG PHE GLU LEU PHE LEU LEU GLY
SEQRES 2 K 120 GLU GLY GLU SER LYS LEU LYS ILE ASP PRO ASP THR LYS
SEQRES 3 K 120 ALA PRO ASN ALA VAL VAL ILE THR PHE GLU LYS GLU ASP
SEQRES 4 K 120 HIS THR LEU GLY ASN LEU ILE ARG ALA GLU LEU LEU ASN
SEQRES 5 K 120 ASP ARG LYS VAL LEU PHE ALA ALA TYR LYS VAL GLU HIS
SEQRES 6 K 120 PRO PHE PHE ALA ARG PHE LYS LEU ARG ILE GLN THR THR
SEQRES 7 K 120 GLU GLY TYR ASP PRO LYS ASP ALA LEU LYS ASN ALA CYS
SEQRES 8 K 120 ASN SER ILE ILE ASN LYS LEU GLY ALA LEU LYS THR ASN
SEQRES 9 K 120 PHE GLU THR GLU TRP ASN LEU GLN THR LEU ALA ALA ASP
SEQRES 10 K 120 ASP ALA PHE
SEQRES 1 L 70 MET SER ARG GLU GLY PHE GLN ILE PRO THR ASN LEU ASP
SEQRES 2 L 70 ALA ALA ALA ALA GLY THR SER GLN ALA ARG THR ALA THR
SEQRES 3 L 70 LEU LYS TYR ILE CYS ALA GLU CYS SER SER LYS LEU SER
SEQRES 4 L 70 LEU SER ARG THR ASP ALA VAL ARG CYS LYS ASP CYS GLY
SEQRES 5 L 70 HIS ARG ILE LEU LEU LYS ALA ARG THR LYS ARG LEU VAL
SEQRES 6 L 70 GLN PHE GLU ALA ARG
SEQRES 1 N 14 DG DT DA DG DA DA DA DG DC DT DA DG DC
SEQRES 2 N 14 DT
SEQRES 1 P 2 C A
SEQRES 1 T 27 DA DG DC DT DA DG DC DT DT DT DC BRU DA
SEQRES 2 T 27 DC DC DT DG DA DA DA DA DA DC DT DA DA
SEQRES 3 T 27 DC
MODRES 4A3J BRU T 15 DU 5-BROMO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE
HET BRU T 15 20
HET ZN A2456 1
HET ZN A2457 1
HET MG A2458 1
HET ZN B2225 1
HET ZN C1269 1
HET ZN I1121 1
HET ZN I1122 1
HET ZN J1066 1
HET ZN L1071 1
HET G2P T1024 32
HETNAM BRU 5-BROMO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER
FORMUL 17 BRU C9 H12 BR N2 O8 P
FORMUL 18 ZN 8(ZN 2+)
FORMUL 19 MG MG 2+
FORMUL 20 G2P C11 H18 N5 O13 P3
HELIX 1 1 SER A 23 SER A 31 1 9
HELIX 2 2 PHE A 95 GLU A 104 1 10
HELIX 3 3 ASN A 119 ILE A 128 1 10
HELIX 4 4 LYS A 132 LYS A 143 1 12
HELIX 5 5 SER A 203 HIS A 213 1 11
HELIX 6 6 SER A 215 LEU A 222 1 8
HELIX 7 7 ARG A 230 TRP A 233 5 4
HELIX 8 8 ASP A 260 ASN A 282 1 23
HELIX 9 9 HIS A 286 ASP A 305 1 20
HELIX 10 10 SER A 324 LYS A 330 1 7
HELIX 11 11 GLY A 334 LEU A 340 1 7
HELIX 12 12 LYS A 368 LEU A 374 1 7
HELIX 13 13 ASN A 384 GLY A 395 1 12
HELIX 14 14 HIS A 451 MET A 453 5 3
HELIX 15 15 SER A 473 THR A 475 5 3
HELIX 16 16 SER A 494 CYS A 505 1 12
HELIX 17 17 ALA A 506 ILE A 511 1 6
HELIX 18 18 VAL A 524 THR A 535 1 12
HELIX 19 19 LEU A 543 VAL A 553 1 11
HELIX 20 20 GLY A 574 SER A 579 1 6
HELIX 21 21 GLU A 618 GLY A 623 1 6
HELIX 22 22 GLY A 628 GLY A 638 1 11
HELIX 23 23 GLY A 638 GLY A 661 1 24
HELIX 24 24 GLY A 665 THR A 669 5 5
HELIX 25 25 ASP A 672 ALA A 699 1 28
HELIX 26 26 THR A 709 LEU A 737 1 29
HELIX 27 27 ASN A 741 ALA A 749 1 9
HELIX 28 28 SER A 754 ALA A 763 1 10
HELIX 29 29 SER A 793 GLY A 798 1 6
HELIX 30 30 THR A 809 GLU A 846 1 38
HELIX 31 31 ILE A 867 ASP A 871 5 5
HELIX 32 32 ASP A 874 ILE A 878 5 5
HELIX 33 33 SER A 889 ARG A 898 1 10
HELIX 34 34 SER A 915 LEU A 920 1 6
HELIX 35 35 LYS A 924 PHE A 947 1 24
HELIX 36 36 ASN A 959 HIS A 972 1 14
HELIX 37 37 THR A 982 ASN A 996 1 15
HELIX 38 38 ASN A 1004 LEU A 1026 1 23
HELIX 39 39 ALA A 1027 GLU A 1034 1 8
HELIX 40 40 THR A 1038 VAL A 1057 1 20
HELIX 41 41 MET A 1063 MET A 1079 1 17
HELIX 42 42 GLY A 1097 VAL A 1107 1 11
HELIX 43 43 ASP A 1127 GLU A 1139 1 13
HELIX 44 44 LEU A 1143 VAL A 1146 1 4
HELIX 45 45 ASP A 1166 HIS A 1173 1 8
HELIX 46 46 ASP A 1198 LYS A 1205 1 8
HELIX 47 47 THR A 1208 PHE A 1220 1 13
HELIX 48 48 GLU A 1256 ASN A 1270 1 15
HELIX 49 49 ASN A 1312 MET A 1317 1 6
HELIX 50 50 SER A 1331 GLY A 1340 1 10
HELIX 51 51 ILE A 1341 ALA A 1357 1 17
HELIX 52 52 ASN A 1364 GLN A 1378 1 15
HELIX 53 53 GLY A 1395 CYS A 1400 1 6
HELIX 54 54 GLU A 1404 SER A 1415 1 12
HELIX 55 55 GLY A 1423 GLY A 1431 1 9
HELIX 56 56 ILE A 1436 ALA A 1440 5 5
HELIX 57 57 ASP A 1446 TYR A 1453 1 8
HELIX 58 58 THR B 26 GLY B 42 1 17
HELIX 59 59 VAL B 44 TYR B 57 1 14
HELIX 60 60 TYR B 57 CYS B 64 1 8
HELIX 61 61 TYR B 113 ASN B 121 1 9
HELIX 62 62 CYS B 179 GLU B 183 5 5
HELIX 63 63 THR B 185 LEU B 192 1 8
HELIX 64 64 ILE B 282 GLY B 290 1 9
HELIX 65 65 GLY B 295 CYS B 302 1 8
HELIX 66 66 ASP B 307 MET B 313 1 7
HELIX 67 67 LEU B 314 PHE B 322 1 9
HELIX 68 68 ASP B 326 ARG B 337 1 12
HELIX 69 69 LYS B 344 TYR B 351 1 8
HELIX 70 70 ALA B 352 GLU B 359 1 8
HELIX 71 71 PHE B 370 LEU B 390 1 21
HELIX 72 72 HIS B 400 GLY B 402 5 3
HELIX 73 73 LEU B 408 THR B 435 1 28
HELIX 74 74 ALA B 450 GLY B 464 1 15
HELIX 75 75 THR B 487 ARG B 496 1 10
HELIX 76 76 PRO B 551 TRP B 561 1 11
HELIX 77 77 ASN B 592 GLY B 607 1 16
HELIX 78 78 ILE B 619 GLU B 621 5 3
HELIX 79 79 ARG B 654 GLN B 667 1 14
HELIX 80 80 THR B 680 GLU B 687 1 8
HELIX 81 81 ALA B 695 GLU B 699 1 5
HELIX 82 82 HIS B 744 LEU B 749 5 6
HELIX 83 83 ALA B 752 ILE B 756 5 5
HELIX 84 84 PHE B 758 HIS B 761 5 4
HELIX 85 85 GLN B 763 GLY B 774 1 12
HELIX 86 86 ASN B 784 ARG B 788 5 5
HELIX 87 87 ALA B 808 LYS B 813 1 6
HELIX 88 88 GLN B 843 ARG B 848 1 6
HELIX 89 89 THR B 889 LEU B 893 5 5
HELIX 90 90 HIS B 1015 MET B 1021 1 7
HELIX 91 91 VAL B 1023 GLY B 1039 1 17
HELIX 92 92 THR B 1051 GLU B 1061 1 11
HELIX 93 93 MET B 1098 LYS B 1102 5 5
HELIX 94 94 GLY B 1121 ASP B 1125 5 5
HELIX 95 95 GLY B 1131 GLY B 1142 1 12
HELIX 96 96 ALA B 1143 MET B 1152 1 10
HELIX 97 97 PRO B 1197 MET B 1210 1 14
HELIX 98 98 ASP C 26 GLU C 40 1 15
HELIX 99 99 ALA C 59 ILE C 70 1 12
HELIX 100 100 ASP C 76 LEU C 80 5 5
HELIX 101 101 TYR C 82 CYS C 86 5 5
HELIX 102 102 HIS C 167 GLY C 171 5 5
HELIX 103 103 ASP C 196 TRP C 201 1 6
HELIX 104 104 SER C 204 GLU C 208 5 5
HELIX 105 105 PRO C 239 GLN C 267 1 29
HELIX 106 106 SER D 53 SER D 73 1 21
HELIX 107 107 ARG D 119 THR D 134 1 16
HELIX 108 108 ASN D 138 SER D 152 1 15
HELIX 109 109 ASP D 156 LYS D 168 1 13
HELIX 110 110 HIS D 173 LEU D 183 1 11
HELIX 111 111 THR D 187 ILE D 195 1 9
HELIX 112 112 SER D 203 GLU D 218 1 16
HELIX 113 113 GLU E 4 ARG E 26 1 23
HELIX 114 114 THR E 31 GLU E 36 1 6
HELIX 115 115 PRO E 38 CYS E 47 1 10
HELIX 116 116 GLN E 54 SER E 59 1 6
HELIX 117 117 GLU E 67 PHE E 72 1 6
HELIX 118 118 GLY E 89 LYS E 103 1 15
HELIX 119 119 SER E 119 VAL E 124 5 6
HELIX 120 120 GLU E 137 VAL E 141 1 5
HELIX 121 121 SER E 157 TYR E 168 1 12
HELIX 122 122 LYS E 171 LEU E 175 5 5
HELIX 123 123 ASP E 182 LEU E 188 1 7
HELIX 124 124 THR F 86 MET F 103 1 18
HELIX 125 125 ASP F 116 GLU F 127 1 12
HELIX 126 126 GLU F 149 LEU F 151 5 3
HELIX 127 127 HIS G 14 PHE G 18 5 5
HELIX 128 128 ARG G 21 VAL G 34 1 14
HELIX 129 129 ASP G 50 ILE G 54 5 5
HELIX 130 130 LYS J 17 GLU J 27 1 11
HELIX 131 131 ASP J 31 LEU J 39 1 9
HELIX 132 132 ARG J 43 THR J 52 1 10
HELIX 133 133 LEU J 56 ARG J 62 1 7
HELIX 134 134 ASP K 5 PHE K 10 5 6
HELIX 135 135 ASP K 39 ASN K 52 1 14
HELIX 136 136 ASP K 82 GLN K 112 1 31
SHEET 1 AA 3 LEU A1418 ASP A1419 0
SHEET 2 AA 3 GLU A 16 LEU A 21 -1 O VAL A 17 N ASP A1419
SHEET 3 AA 3 ILE B1212 TYR B1217 -1 N THR B1213 O GLY A 20
SHEET 1 AB 2 GLY A 82 PHE A 91 0
SHEET 2 AB 2 ILE A 235 VAL A 241 -1 O LEU A 236 N VAL A 90
SHEET 1 AC 2 VAL A 152 PRO A 153 0
SHEET 2 AC 2 LEU A 161 VAL A 162 -1 O VAL A 162 N VAL A 152
SHEET 1 AD 3 ARG A 175 LYS A 176 0
SHEET 2 AD 3 LEU A 181 VAL A 182 -1 O VAL A 182 N ARG A 175
SHEET 3 AD 3 VAL A 201 LEU A 202 -1 O LEU A 202 N LEU A 181
SHEET 1 AE 2 LYS A 343 VAL A 345 0
SHEET 2 AE 2 LEU B1128 PHE B1130 -1 O LEU B1128 N VAL A 345
SHEET 1 AF14 SER A 348 ASP A 356 0
SHEET 2 AF14 HIS B1104 ARG B1106 -1 O HIS B1104 N ARG A 350
SHEET 3 AF14 GLN A 363 PRO A 367 0
SHEET 4 AF14 MET A 455 ILE A 463 1 O ARG A 459 N VAL A 364
SHEET 5 AF14 PRO A 441 ASN A 445 -1 O VAL A 442 N HIS A 458
SHEET 6 AF14 PHE A 468 ASN A 471 -1 O ARG A 469 N GLY A 365
SHEET 7 AF14 GLU A 486 HIS A 490 -1 O MET A 487 N THR A 351
SHEET 8 AF14 SER A 348 ASP A 356 -1 O SER A 348 N ARG B1106
SHEET 1 AG 4 THR A 375 VAL A 379 0
SHEET 2 AG 4 LYS A 431 HIS A 435 -1 O VAL A 432 N GLU A 378
SHEET 3 AG 4 ALA A 402 ILE A 406 -1 N LYS A 403 O GLU A 433
SHEET 4 AG 4 ARG A 412 ASP A 414 -1 N ILE A 413 O VAL A 405
SHEET 1 AH 3 PHE A 540 GLU A 542 0
SHEET 2 AH 3 PRO A 570 SER A 573 -1 O TRP A 572 N ILE A 541
SHEET 3 AH 3 ILE A 565 ILE A 566 -1 O ILE A 565 N LEU A 571
SHEET 1 AI 3 LEU A 588 ARG A 590 0
SHEET 2 AI 3 MET A 605 ILE A 607 -1 O MET A 605 N ARG A 590
SHEET 3 AI 3 ILE A 612 PHE A 614 -1 N ILE A 613 O LEU A 606
SHEET 1 AJ 2 GLY A 766 GLN A 767 0
SHEET 2 AJ 2 PHE A 799 VAL A 800 -1 O VAL A 800 N GLY A 766
SHEET 1 AK 2 SER A 769 VAL A 770 0
SHEET 2 AK 2 LYS A 773 ARG A 774 -1 O LYS A 773 N VAL A 770
SHEET 1 AL 3 MET A 849 VAL A 850 0
SHEET 2 AL 3 THR A 856 ARG A 857 -1 O ARG A 857 N MET A 849
SHEET 3 AL 3 VAL A 863 GLN A 865 -1 N ILE A 864 O THR A 856
SHEET 1 AM 2 GLU A 879 SER A 882 0
SHEET 2 AM 2 ASN A 953 LEU A 956 -1 O TRP A 954 N GLN A 881
SHEET 1 AN 4 VAL A1283 TYR A1287 0
SHEET 2 AN 4 GLU A1303 GLU A1307 -1 O GLU A1303 N TYR A1287
SHEET 3 AN 4 LEU A1116 TYR A1119 -1 O VAL A1118 N LEU A1306
SHEET 4 AN 4 TYR A1328 THR A1329 -1 O TYR A1328 N THR A1117
SHEET 1 AO 2 THR A1141 THR A1142 0
SHEET 2 AO 2 THR A1272 ARG A1274 -1 N LEU A1273 O THR A1141
SHEET 1 AP 5 VAL A1226 TRP A1228 0
SHEET 2 AP 5 LEU A1236 CYS A1240 -1 O ARG A1239 N ILE A1227
SHEET 3 AP 5 TRP A1191 LEU A1197 -1 O LEU A1193 N CYS A1240
SHEET 4 AP 5 THR A1147 TYR A1154 -1 N ILE A1148 O GLU A1196
SHEET 5 AP 5 LEU I 42 ARG I 45 -1 N VAL I 43 O ILE A1152
SHEET 1 AQ 2 LYS A1290 PRO A1292 0
SHEET 2 AQ 2 TYR A1298 LYS A1300 -1 O VAL A1299 N VAL A1291
SHEET 1 DA 7 SER D 6 THR D 7 0
SHEET 2 DA 7 PHE G 3 LEU G 13 -1 O SER G 8 N SER D 6
SHEET 3 DA 7 ALA G 68 PHE G 79 -1 O ALA G 68 N LEU G 13
SHEET 4 DA 7 GLY G 59 ILE G 61 -1 O ARG G 60 N GLU G 69
SHEET 5 DA 7 ASP A1442 ILE A1445 -1 O VAL A1443 N ILE G 61
SHEET 6 DA 7 LEU F 132 TYR F 137 -1 O VAL F 133 N MET A1444
SHEET 7 DA 7 PHE F 143 SER F 147 -1 O GLU F 144 N ARG F 136
SHEET 1 DB 5 SER D 6 THR D 7 0
SHEET 2 DB 5 PHE G 3 LEU G 13 -1 O SER G 8 N SER D 6
SHEET 3 DB 5 ALA G 68 PHE G 79 -1 O ALA G 68 N LEU G 13
SHEET 4 DB 5 GLY G 43 VAL G 48 1 O TYR G 44 N PHE G 79
SHEET 5 DB 5 CYS G 38 THR G 39 -1 O THR G 39 N GLY G 43
SHEET 1 BA 3 SER B 91 VAL B 97 0
SHEET 2 BA 3 SER B 125 LYS B 133 -1 O PHE B 129 N TYR B 96
SHEET 3 BA 3 VAL B 165 PRO B 171 -1 O VAL B 165 N VAL B 130
SHEET 1 BB 2 VAL B 102 ASN B 103 0
SHEET 2 BB 2 THR B 109 HIS B 110 -1 O HIS B 110 N VAL B 102
SHEET 1 BC 3 PHE B 203 ILE B 205 0
SHEET 2 BC 3 SER B 208 LEU B 212 -1 O SER B 208 N ILE B 205
SHEET 3 BC 3 SER B 480 VAL B 482 -1 O GLN B 481 N VAL B 211
SHEET 1 BD 4 LYS B 404 ASP B 407 0
SHEET 2 BD 4 ALA B 214 SER B 218 -1 O GLN B 215 N ASP B 407
SHEET 3 BD 4 ARG B 497 ASN B 499 1 O ARG B 497 N ALA B 214
SHEET 4 BD 4 VAL B 536 ASN B 538 -1 O LYS B 537 N THR B 498
SHEET 1 BE 5 ILE B 222 LYS B 227 0
SHEET 2 BE 5 ILE B 234 ARG B 241 -1 O VAL B 237 N PHE B 226
SHEET 3 BE 5 THR B 253 TYR B 259 -1 O LEU B 254 N ILE B 240
SHEET 4 BE 5 ILE B 269 THR B 272 -1 O LYS B 270 N LYS B 257
SHEET 5 BE 5 ASP B 279 PRO B 281 -1 O ILE B 280 N ALA B 271
SHEET 1 BF 2 CYS B 544 ILE B 545 0
SHEET 2 BF 2 VAL B 633 GLU B 641 1 O TYR B 634 N CYS B 544
SHEET 1 BG 2 GLU B 650 LEU B 651 0
SHEET 2 BG 2 VAL B 633 GLU B 641 -1 O GLU B 641 N GLU B 650
SHEET 1 BH 2 VAL B 690 ASP B 694 0
SHEET 2 BH 2 VAL B 633 GLU B 641 -1 O ARG B 635 N ILE B 693
SHEET 1 BI 4 ILE B 703 ALA B 704 0
SHEET 2 BI 4 HIS B 740 CYS B 741 1 O HIS B 740 N ALA B 704
SHEET 3 BI 4 VAL B 633 GLU B 641 -1 O PHE B 638 N CYS B 741
SHEET 4 BI 4 GLU B 650 LEU B 651 -1 O GLU B 650 N GLU B 641
SHEET 1 BJ 4 ILE B 703 ALA B 704 0
SHEET 2 BJ 4 HIS B 740 CYS B 741 1 O HIS B 740 N ALA B 704
SHEET 3 BJ 4 VAL B 633 GLU B 641 -1 O PHE B 638 N CYS B 741
SHEET 4 BJ 4 VAL B 690 ASP B 694 -1 O GLU B 691 N LEU B 637
SHEET 1 BK 5 MET B 563 PRO B 565 0
SHEET 2 BK 5 VAL B 585 HIS B 590 -1 O VAL B 589 N GLU B 564
SHEET 3 BK 5 THR B 578 VAL B 582 -1 O THR B 578 N HIS B 590
SHEET 4 BK 5 GLU B 623 PHE B 627 1 O LEU B 624 N PHE B 581
SHEET 5 BK 5 SER B 614 ASP B 618 -1 O SER B 614 N PHE B 627
SHEET 1 BL 2 GLY B 804 THR B 805 0
SHEET 2 BL 2 GLY B1042 ASP B1043 1 O GLY B1042 N THR B 805
SHEET 1 BM16 GLY B 820 ILE B 827 0
SHEET 2 BM16 LYS B1080 ARG B1094 -1 O PHE B1086 N ILE B 827
SHEET 3 BM16 SER B 838 ASN B 842 0
SHEET 4 BM16 LYS B 987 TYR B 994 1 O THR B 989 N MET B 839
SHEET 5 BM16 LYS B 979 ALA B 981 -1 O PHE B 980 N GLY B 988
SHEET 6 BM16 PHE B1001 THR B1002 0
SHEET 7 BM16 GLU B1070 TYR B1073 -1 O TYR B1073 N PHE B1001
SHEET 8 BM16 LEU B1010 ILE B1012 0
SHEET 9 BM16 GLY B 820 ILE B 827 -1 O GLN B 821 N TYR B1092
SHEET 1 BN 2 SER B 853 PHE B 855 0
SHEET 2 BN 2 LYS B 962 LYS B 972 -1 O THR B 970 N PHE B 855
SHEET 1 BO 2 SER B 858 GLN B 862 0
SHEET 2 BO 2 LYS B 962 LYS B 972 -1 O VAL B 964 N ASP B 861
SHEET 1 BP 4 ARG B 904 VAL B 905 0
SHEET 2 BP 4 GLY B 947 THR B 956 -1 O GLY B 947 N VAL B 905
SHEET 3 BP 4 LYS B 962 LYS B 972 -1 O PHE B 963 N THR B 955
SHEET 4 BP 4 SER B 858 GLN B 862 -1 O TYR B 859 N VAL B 966
SHEET 1 BQ 4 ARG B 904 VAL B 905 0
SHEET 2 BQ 4 GLY B 947 THR B 956 -1 O GLY B 947 N VAL B 905
SHEET 3 BQ 4 LYS B 962 LYS B 972 -1 O PHE B 963 N THR B 955
SHEET 4 BQ 4 SER B 853 PHE B 855 -1 O SER B 853 N LYS B 972
SHEET 1 BR 2 THR B 873 PHE B 874 0
SHEET 2 BR 2 LYS B 914 THR B 915 -1 O THR B 915 N THR B 873
SHEET 1 BS 2 VAL B 910 ILE B 912 0
SHEET 2 BS 2 THR B 939 PRO B 940 -1 O THR B 939 N ILE B 911
SHEET 1 BT 2 PHE B1158 CYS B1163 0
SHEET 2 BT 2 ILE B1191 ILE B1196 -1 O TYR B1192 N ILE B1162
SHEET 1 BU 2 ILE B1172 ALA B1173 0
SHEET 2 BU 2 PHE B1180 GLU B1181 -1 O GLU B1181 N ILE B1172
SHEET 1 CA 4 GLN C 7 ALA C 13 0
SHEET 2 CA 4 ASN C 17 SER C 23 -1 O ASP C 19 N ARG C 11
SHEET 3 CA 4 PHE C 228 SER C 234 -1 O PHE C 228 N LEU C 22
SHEET 4 CA 4 ALA C 173 GLU C 179 -1 N ALA C 174 O GLU C 233
SHEET 1 CB 5 LEU C 118 ILE C 120 0
SHEET 2 CB 5 VAL C 97 PHE C 104 -1 O THR C 100 N VAL C 119
SHEET 3 CB 5 GLU C 152 LYS C 160 -1 O LEU C 153 N ALA C 103
SHEET 4 CB 5 ALA C 45 ASN C 54 -1 O ALA C 45 N LYS C 160
SHEET 5 CB 5 VAL L 65 GLU L 68 -1 O VAL L 65 N VAL C 51
SHEET 1 CC 2 THR C 111 TYR C 114 0
SHEET 2 CC 2 LEU C 143 LEU C 147 -1 N ILE C 144 O VAL C 113
SHEET 1 DC 2 LYS D 36 ILE D 38 0
SHEET 2 DC 2 GLU D 44 GLU D 46 -1 O GLU D 45 N GLN D 37
SHEET 1 EA 5 TYR E 28 PHE E 29 0
SHEET 2 EA 5 PHE E 60 PRO E 64 -1 O ASN E 63 N PHE E 29
SHEET 3 EA 5 LEU E 78 PHE E 82 -1 O LEU E 78 N ALA E 62
SHEET 4 EA 5 THR E 107 TYR E 112 1 O THR E 107 N TRP E 79
SHEET 5 EA 5 THR E 131 ASN E 136 1 O THR E 131 N GLY E 108
SHEET 1 EB 2 SER E 87 VAL E 88 0
SHEET 2 EB 2 ASN E 115 ILE E 116 1 O ASN E 115 N VAL E 88
SHEET 1 EC 4 LYS E 152 ARG E 155 0
SHEET 2 EC 4 VAL E 195 ARG E 200 -1 O LYS E 197 N ILE E 154
SHEET 3 EC 4 TYR E 208 CYS E 214 -1 O TYR E 208 N ARG E 200
SHEET 4 EC 4 ARG E 177 ILE E 178 1 N ILE E 178 O ILE E 213
SHEET 1 GA12 VAL G 86 CYS G 94 0
SHEET 2 GA12 ARG G 142 GLN G 153 -1 O ILE G 143 N GLY G 89
SHEET 3 GA12 GLY G 98 VAL G 103 0
SHEET 4 GA12 MET G 106 THR G 111 0
SHEET 5 GA12 SER G 156 SER G 162 0
SHEET 6 GA12 GLY G 169 ALA G 170 0
SHEET 7 GA12 ARG G 142 GLN G 153 -1 O ARG G 144 N GLY G 169
SHEET 1 GB 3 THR G 120 ASN G 122 0
SHEET 2 GB 3 SER G 129 GLN G 131 -1 O SER G 129 N ASN G 122
SHEET 3 GB 3 VAL G 136 THR G 138 -1 O ILE G 137 N TYR G 130
SHEET 1 HA 9 TYR H 95 TYR H 98 0
SHEET 2 HA 9 TYR H 141 ARG H 145 -1 O LEU H 142 N MET H 97
SHEET 3 HA 9 SER H 54 THR H 58 -1 O THR H 56 N ARG H 145
SHEET 4 HA 9 ASP H 7 ASP H 16 -1 O ASP H 8 N VAL H 57
SHEET 5 HA 9 VAL H 23 SER H 30 -1 O ARG H 25 N ASP H 16
SHEET 6 HA 9 LYS H 37 ASN H 43 -1 O LEU H 38 N ALA H 28
SHEET 7 HA 9 LEU H 121 GLU H 126 -1 O LEU H 122 N ASP H 41
SHEET 8 HA 9 ALA H 113 PHE H 118 -1 O VAL H 114 N LEU H 125
SHEET 9 HA 9 THR H 100 LYS H 103 -1 O THR H 100 N SER H 117
SHEET 1 IA 3 LEU I 14 ASP I 19 0
SHEET 2 IA 3 ARG I 24 CYS I 29 -1 O ARG I 24 N ASP I 19
SHEET 3 IA 3 VAL I 35 GLU I 37 -1 O GLU I 36 N PHE I 27
SHEET 1 IB 4 ARG I 70 SER I 71 0
SHEET 2 IB 4 ASN I 83 GLN I 87 -1 O ASN I 83 N SER I 71
SHEET 3 IB 4 LEU I 99 CYS I 103 -1 O PHE I 100 N PHE I 86
SHEET 4 IB 4 ILE I 109 THR I 111 -1 O PHE I 110 N PHE I 101
SHEET 1 KA 4 LEU K 19 PRO K 23 0
SHEET 2 KA 4 ALA K 30 GLU K 36 -1 O VAL K 32 N ASP K 22
SHEET 3 KA 4 ARG K 70 THR K 77 -1 O PHE K 71 N PHE K 35
SHEET 4 KA 4 VAL K 56 LYS K 62 -1 N LEU K 57 O GLN K 76
LINK ZN ZN A2456 SG CYS A 167 1555 1555 2.32
LINK ZN ZN A2456 SG CYS A 110 1555 1555 2.37
LINK ZN ZN A2456 SG CYS A 107 1555 1555 2.34
LINK ZN ZN A2456 SG CYS A 148 1555 1555 2.41
LINK ZN ZN A2457 SG CYS A 67 1555 1555 2.29
LINK ZN ZN A2457 SG CYS A 70 1555 1555 2.47
LINK ZN ZN A2457 SG CYS A 77 1555 1555 2.51
LINK ZN ZN A2457 NE2 HIS A 80 1555 1555 2.17
LINK MG MG A2458 O2' A P 10 1555 1555 2.39
LINK MG MG A2458 O3' A P 10 1555 1555 2.07
LINK MG MG A2458 OD1 ASP A 481 1555 1555 2.04
LINK MG MG A2458 OD1 ASP A 485 1555 1555 2.19
LINK MG MG A2458 OD1 ASP A 483 1555 1555 2.26
LINK MG MG A2458 OD2 ASP A 481 1555 1555 2.34
LINK ZN ZN B2225 SG CYS B1166 1555 1555 2.26
LINK ZN ZN B2225 SG CYS B1182 1555 1555 2.33
LINK ZN ZN B2225 SG CYS B1163 1555 1555 2.39
LINK ZN ZN B2225 SG CYS B1185 1555 1555 2.44
LINK ZN ZN C1269 SG CYS C 92 1555 1555 2.27
LINK ZN ZN C1269 SG CYS C 95 1555 1555 2.33
LINK ZN ZN C1269 SG CYS C 86 1555 1555 2.34
LINK ZN ZN C1269 SG CYS C 88 1555 1555 2.31
LINK ZN ZN I1121 SG CYS I 7 1555 1555 2.33
LINK ZN ZN I1121 SG CYS I 29 1555 1555 2.23
LINK ZN ZN I1121 SG CYS I 32 1555 1555 2.40
LINK ZN ZN I1121 SG CYS I 10 1555 1555 2.36
LINK ZN ZN I1122 SG CYS I 78 1555 1555 2.30
LINK ZN ZN I1122 SG CYS I 75 1555 1555 2.32
LINK ZN ZN I1122 SG CYS I 103 1555 1555 2.47
LINK ZN ZN I1122 SG CYS I 106 1555 1555 2.32
LINK ZN ZN J1066 SG CYS J 10 1555 1555 2.48
LINK ZN ZN J1066 SG CYS J 45 1555 1555 2.37
LINK ZN ZN J1066 SG CYS J 46 1555 1555 2.41
LINK ZN ZN J1066 SG CYS J 7 1555 1555 2.38
LINK ZN ZN L1071 SG CYS L 34 1555 1555 2.35
LINK ZN ZN L1071 SG CYS L 51 1555 1555 2.44
LINK ZN ZN L1071 SG CYS L 48 1555 1555 2.36
LINK ZN ZN L1071 SG CYS L 31 1555 1555 2.52
LINK P BRU T 15 O3' DC T 14 1555 1555 1.60
LINK O3' BRU T 15 P DA T 16 1555 1555 1.59
CISPEP 1 ASP A 193 ALA A 194 0 4.42
CISPEP 2 ALA A 194 ASP A 195 0 -3.43
CISPEP 3 GLN A 447 PRO A 448 0 -15.05
CISPEP 4 LYS A 567 PRO A 568 0 2.83
CISPEP 5 GLY B 338 THR B 339 0 3.56
CISPEP 6 GLU B 468 GLN B 469 0 -7.48
CISPEP 7 MET B 473 SER B 474 0 -1.04
CISPEP 8 VAL D 18 GLU D 19 0 3.62
CISPEP 9 PRO E 128 PRO E 129 0 2.45
CISPEP 10 ASN G 126 PRO G 127 0 1.00
SITE 1 AC1 4 CYS A 107 CYS A 110 CYS A 148 CYS A 167
SITE 1 AC2 4 CYS A 67 CYS A 70 CYS A 77 HIS A 80
SITE 1 AC3 4 ASP A 481 ASP A 483 ASP A 485 A P 10
SITE 1 AC4 4 CYS B1163 CYS B1166 CYS B1182 CYS B1185
SITE 1 AC5 4 CYS C 86 CYS C 88 CYS C 92 CYS C 95
SITE 1 AC6 4 CYS I 7 CYS I 10 CYS I 29 CYS I 32
SITE 1 AC7 4 CYS I 75 CYS I 78 CYS I 103 CYS I 106
SITE 1 AC8 4 CYS J 7 CYS J 10 CYS J 45 CYS J 46
SITE 1 AC9 4 CYS L 31 CYS L 34 CYS L 48 CYS L 51
SITE 1 BC1 9 ARG A 446 PRO A 448 ASN A 479 ARG B 766
SITE 2 BC1 9 LYS B 987 ARG B1020 A P 10 DC T 18
SITE 3 BC1 9 DT T 19
CRYST1 223.290 392.790 282.660 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004478 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002546 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003538 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
